data_7HCQ
# 
_entry.id   7HCQ 
# 
_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   7HCQ         pdb_00007hcq 10.2210/pdb7hcq/pdb 
WWPDB D_1001407308 ?            ?                   
# 
_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                        7HCQ 
_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 '7-methyl-N-[6-(methylamino)pyridin-3-yl]-1-benzothiophene-2-sulfonamide' 333.429   1   ?                      ? 
? ?                                                                                    
3 water       nat water                                                                     18.015    428 ?                      ? 
? ?                                                                                    
# 
_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 '7-methyl-N-[6-(methylamino)pyridin-3-yl]-1-benzothiophene-2-sulfonamide' A1A50 
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 
A1A50 non-polymer         . '7-methyl-N-[6-(methylamino)pyridin-3-yl]-1-benzothiophene-2-sulfonamide' ? 'C15 H15 N3 O2 S2' 333.429 
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 A1A50 1   201 201  A1A50 LA1 A . 
D 3 HOH   1   301 1310 HOH   HOH A . 
D 3 HOH   2   302 292  HOH   HOH A . 
D 3 HOH   3   303 625  HOH   HOH A . 
D 3 HOH   4   304 409  HOH   HOH A . 
D 3 HOH   5   305 209  HOH   HOH A . 
D 3 HOH   6   306 21   HOH   HOH A . 
D 3 HOH   7   307 18   HOH   HOH A . 
D 3 HOH   8   308 1301 HOH   HOH A . 
D 3 HOH   9   309 1290 HOH   HOH A . 
D 3 HOH   10  310 337  HOH   HOH A . 
D 3 HOH   11  311 192  HOH   HOH A . 
D 3 HOH   12  312 1295 HOH   HOH A . 
D 3 HOH   13  313 493  HOH   HOH A . 
D 3 HOH   14  314 109  HOH   HOH A . 
D 3 HOH   15  315 124  HOH   HOH A . 
D 3 HOH   16  316 76   HOH   HOH A . 
D 3 HOH   17  317 229  HOH   HOH A . 
D 3 HOH   18  318 136  HOH   HOH A . 
D 3 HOH   19  319 196  HOH   HOH A . 
D 3 HOH   20  320 57   HOH   HOH A . 
D 3 HOH   21  321 49   HOH   HOH A . 
D 3 HOH   22  322 661  HOH   HOH A . 
D 3 HOH   23  323 35   HOH   HOH A . 
D 3 HOH   24  324 469  HOH   HOH A . 
D 3 HOH   25  325 964  HOH   HOH A . 
D 3 HOH   26  326 36   HOH   HOH A . 
D 3 HOH   27  327 153  HOH   HOH A . 
D 3 HOH   28  328 15   HOH   HOH A . 
D 3 HOH   29  329 281  HOH   HOH A . 
D 3 HOH   30  330 247  HOH   HOH A . 
D 3 HOH   31  331 1308 HOH   HOH A . 
D 3 HOH   32  332 393  HOH   HOH A . 
D 3 HOH   33  333 2    HOH   HOH A . 
D 3 HOH   34  334 164  HOH   HOH A . 
D 3 HOH   35  335 225  HOH   HOH A . 
D 3 HOH   36  336 74   HOH   HOH A . 
D 3 HOH   37  337 17   HOH   HOH A . 
D 3 HOH   38  338 140  HOH   HOH A . 
D 3 HOH   39  339 92   HOH   HOH A . 
D 3 HOH   40  340 151  HOH   HOH A . 
D 3 HOH   41  341 105  HOH   HOH A . 
D 3 HOH   42  342 102  HOH   HOH A . 
D 3 HOH   43  343 165  HOH   HOH A . 
D 3 HOH   44  344 236  HOH   HOH A . 
D 3 HOH   45  345 939  HOH   HOH A . 
D 3 HOH   46  346 2    HOH   HOH A . 
D 3 HOH   47  347 1300 HOH   HOH A . 
D 3 HOH   48  348 1296 HOH   HOH A . 
D 3 HOH   49  349 169  HOH   HOH A . 
D 3 HOH   50  350 366  HOH   HOH A . 
D 3 HOH   51  351 93   HOH   HOH A . 
D 3 HOH   52  352 278  HOH   HOH A . 
D 3 HOH   53  353 42   HOH   HOH A . 
D 3 HOH   54  354 20   HOH   HOH A . 
D 3 HOH   55  355 46   HOH   HOH A . 
D 3 HOH   56  356 96   HOH   HOH A . 
D 3 HOH   57  357 662  HOH   HOH A . 
D 3 HOH   58  358 139  HOH   HOH A . 
D 3 HOH   59  359 39   HOH   HOH A . 
D 3 HOH   60  360 320  HOH   HOH A . 
D 3 HOH   61  361 33   HOH   HOH A . 
D 3 HOH   62  362 155  HOH   HOH A . 
D 3 HOH   63  363 56   HOH   HOH A . 
D 3 HOH   64  364 354  HOH   HOH A . 
D 3 HOH   65  365 81   HOH   HOH A . 
D 3 HOH   66  366 1283 HOH   HOH A . 
D 3 HOH   67  367 630  HOH   HOH A . 
D 3 HOH   68  368 186  HOH   HOH A . 
D 3 HOH   69  369 21   HOH   HOH A . 
D 3 HOH   70  370 159  HOH   HOH A . 
D 3 HOH   71  371 162  HOH   HOH A . 
D 3 HOH   72  372 396  HOH   HOH A . 
D 3 HOH   73  373 66   HOH   HOH A . 
D 3 HOH   74  374 26   HOH   HOH A . 
D 3 HOH   75  375 241  HOH   HOH A . 
D 3 HOH   76  376 218  HOH   HOH A . 
D 3 HOH   77  377 86   HOH   HOH A . 
D 3 HOH   78  378 138  HOH   HOH A . 
D 3 HOH   79  379 116  HOH   HOH A . 
D 3 HOH   80  380 19   HOH   HOH A . 
D 3 HOH   81  381 62   HOH   HOH A . 
D 3 HOH   82  382 381  HOH   HOH A . 
D 3 HOH   83  383 3    HOH   HOH A . 
D 3 HOH   84  384 134  HOH   HOH A . 
D 3 HOH   85  385 5    HOH   HOH A . 
D 3 HOH   86  386 78   HOH   HOH A . 
D 3 HOH   87  387 17   HOH   HOH A . 
D 3 HOH   88  388 351  HOH   HOH A . 
D 3 HOH   89  389 27   HOH   HOH A . 
D 3 HOH   90  390 132  HOH   HOH A . 
D 3 HOH   91  391 4    HOH   HOH A . 
D 3 HOH   92  392 58   HOH   HOH A . 
D 3 HOH   93  393 85   HOH   HOH A . 
D 3 HOH   94  394 8    HOH   HOH A . 
D 3 HOH   95  395 1313 HOH   HOH A . 
D 3 HOH   96  396 45   HOH   HOH A . 
D 3 HOH   97  397 148  HOH   HOH A . 
D 3 HOH   98  398 333  HOH   HOH A . 
D 3 HOH   99  399 16   HOH   HOH A . 
D 3 HOH   100 400 296  HOH   HOH A . 
D 3 HOH   101 401 405  HOH   HOH A . 
D 3 HOH   102 402 12   HOH   HOH A . 
D 3 HOH   103 403 154  HOH   HOH A . 
D 3 HOH   104 404 34   HOH   HOH A . 
D 3 HOH   105 405 15   HOH   HOH A . 
D 3 HOH   106 406 1279 HOH   HOH A . 
D 3 HOH   107 407 1309 HOH   HOH A . 
D 3 HOH   108 408 24   HOH   HOH A . 
D 3 HOH   109 409 6    HOH   HOH A . 
D 3 HOH   110 410 1    HOH   HOH A . 
D 3 HOH   111 411 121  HOH   HOH A . 
D 3 HOH   112 412 83   HOH   HOH A . 
D 3 HOH   113 413 1289 HOH   HOH A . 
D 3 HOH   114 414 303  HOH   HOH A . 
D 3 HOH   115 415 123  HOH   HOH A . 
D 3 HOH   116 416 461  HOH   HOH A . 
D 3 HOH   117 417 3    HOH   HOH A . 
D 3 HOH   118 418 67   HOH   HOH A . 
D 3 HOH   119 419 1222 HOH   HOH A . 
D 3 HOH   120 420 122  HOH   HOH A . 
D 3 HOH   121 421 199  HOH   HOH A . 
D 3 HOH   122 422 6    HOH   HOH A . 
D 3 HOH   123 423 68   HOH   HOH A . 
D 3 HOH   124 424 70   HOH   HOH A . 
D 3 HOH   125 425 1315 HOH   HOH A . 
D 3 HOH   126 426 25   HOH   HOH A . 
D 3 HOH   127 427 125  HOH   HOH A . 
D 3 HOH   128 428 1068 HOH   HOH A . 
D 3 HOH   129 429 95   HOH   HOH A . 
D 3 HOH   130 430 53   HOH   HOH A . 
D 3 HOH   131 431 71   HOH   HOH A . 
D 3 HOH   132 432 952  HOH   HOH A . 
D 3 HOH   133 433 397  HOH   HOH A . 
D 3 HOH   134 434 195  HOH   HOH A . 
D 3 HOH   135 435 51   HOH   HOH A . 
D 3 HOH   136 436 7    HOH   HOH A . 
D 3 HOH   137 437 1286 HOH   HOH A . 
D 3 HOH   138 438 1275 HOH   HOH A . 
D 3 HOH   139 439 16   HOH   HOH A . 
D 3 HOH   140 440 1238 HOH   HOH A . 
D 3 HOH   141 441 115  HOH   HOH A . 
D 3 HOH   142 442 80   HOH   HOH A . 
D 3 HOH   143 443 5    HOH   HOH A . 
D 3 HOH   144 444 94   HOH   HOH A . 
D 3 HOH   145 445 188  HOH   HOH A . 
D 3 HOH   146 446 156  HOH   HOH A . 
D 3 HOH   147 447 8    HOH   HOH A . 
D 3 HOH   148 448 104  HOH   HOH A . 
D 3 HOH   149 449 1094 HOH   HOH A . 
D 3 HOH   150 450 40   HOH   HOH A . 
D 3 HOH   151 451 9    HOH   HOH A . 
D 3 HOH   152 452 97   HOH   HOH A . 
D 3 HOH   153 453 212  HOH   HOH A . 
D 3 HOH   154 454 576  HOH   HOH A . 
D 3 HOH   155 455 73   HOH   HOH A . 
D 3 HOH   156 456 582  HOH   HOH A . 
D 3 HOH   157 457 944  HOH   HOH A . 
D 3 HOH   158 458 1189 HOH   HOH A . 
D 3 HOH   159 459 79   HOH   HOH A . 
D 3 HOH   160 460 1134 HOH   HOH A . 
D 3 HOH   161 461 107  HOH   HOH A . 
D 3 HOH   162 462 330  HOH   HOH A . 
D 3 HOH   163 463 509  HOH   HOH A . 
D 3 HOH   164 464 1119 HOH   HOH A . 
D 3 HOH   165 465 726  HOH   HOH A . 
D 3 HOH   166 466 10   HOH   HOH A . 
D 3 HOH   167 467 163  HOH   HOH A . 
D 3 HOH   168 468 408  HOH   HOH A . 
D 3 HOH   169 469 361  HOH   HOH A . 
D 3 HOH   170 470 12   HOH   HOH A . 
D 3 HOH   171 471 126  HOH   HOH A . 
D 3 HOH   172 472 342  HOH   HOH A . 
D 3 HOH   173 473 756  HOH   HOH A . 
D 3 HOH   174 474 319  HOH   HOH A . 
D 3 HOH   175 475 556  HOH   HOH A . 
D 3 HOH   176 476 801  HOH   HOH A . 
D 3 HOH   177 477 4    HOH   HOH A . 
D 3 HOH   178 478 1276 HOH   HOH A . 
D 3 HOH   179 479 250  HOH   HOH A . 
D 3 HOH   180 480 1314 HOH   HOH A . 
D 3 HOH   181 481 63   HOH   HOH A . 
D 3 HOH   182 482 1307 HOH   HOH A . 
D 3 HOH   183 483 280  HOH   HOH A . 
D 3 HOH   184 484 11   HOH   HOH A . 
D 3 HOH   185 485 370  HOH   HOH A . 
D 3 HOH   186 486 13   HOH   HOH A . 
D 3 HOH   187 487 224  HOH   HOH A . 
D 3 HOH   188 488 1287 HOH   HOH A . 
D 3 HOH   189 489 1306 HOH   HOH A . 
D 3 HOH   190 490 135  HOH   HOH A . 
D 3 HOH   191 491 202  HOH   HOH A . 
D 3 HOH   192 492 674  HOH   HOH A . 
D 3 HOH   193 493 7    HOH   HOH A . 
D 3 HOH   194 494 521  HOH   HOH A . 
D 3 HOH   195 495 267  HOH   HOH A . 
D 3 HOH   196 496 919  HOH   HOH A . 
D 3 HOH   197 497 318  HOH   HOH A . 
D 3 HOH   198 498 315  HOH   HOH A . 
D 3 HOH   199 499 1284 HOH   HOH A . 
D 3 HOH   200 500 805  HOH   HOH A . 
D 3 HOH   201 501 711  HOH   HOH A . 
D 3 HOH   202 502 309  HOH   HOH A . 
D 3 HOH   203 503 331  HOH   HOH A . 
D 3 HOH   204 504 695  HOH   HOH A . 
D 3 HOH   205 505 1299 HOH   HOH A . 
D 3 HOH   206 506 18   HOH   HOH A . 
D 3 HOH   207 507 152  HOH   HOH A . 
D 3 HOH   208 508 941  HOH   HOH A . 
D 3 HOH   209 509 208  HOH   HOH A . 
D 3 HOH   210 510 263  HOH   HOH A . 
D 3 HOH   211 511 356  HOH   HOH A . 
D 3 HOH   212 512 180  HOH   HOH A . 
D 3 HOH   213 513 363  HOH   HOH A . 
D 3 HOH   214 514 1071 HOH   HOH A . 
D 3 HOH   215 515 350  HOH   HOH A . 
D 3 HOH   216 516 371  HOH   HOH A . 
D 3 HOH   217 517 313  HOH   HOH A . 
D 3 HOH   218 518 14   HOH   HOH A . 
D 3 HOH   219 519 326  HOH   HOH A . 
D 3 HOH   220 520 19   HOH   HOH A . 
D 3 HOH   221 521 429  HOH   HOH A . 
D 3 HOH   222 522 185  HOH   HOH A . 
D 3 HOH   223 523 772  HOH   HOH A . 
D 3 HOH   224 524 376  HOH   HOH A . 
D 3 HOH   225 525 1074 HOH   HOH A . 
D 3 HOH   226 526 1292 HOH   HOH A . 
D 3 HOH   227 527 346  HOH   HOH A . 
D 3 HOH   228 528 1078 HOH   HOH A . 
E 3 HOH   1   201 64   HOH   HOH B . 
E 3 HOH   2   202 531  HOH   HOH B . 
E 3 HOH   3   203 1249 HOH   HOH B . 
E 3 HOH   4   204 758  HOH   HOH B . 
E 3 HOH   5   205 240  HOH   HOH B . 
E 3 HOH   6   206 549  HOH   HOH B . 
E 3 HOH   7   207 358  HOH   HOH B . 
E 3 HOH   8   208 452  HOH   HOH B . 
E 3 HOH   9   209 364  HOH   HOH B . 
E 3 HOH   10  210 353  HOH   HOH B . 
E 3 HOH   11  211 120  HOH   HOH B . 
E 3 HOH   12  212 232  HOH   HOH B . 
E 3 HOH   13  213 69   HOH   HOH B . 
E 3 HOH   14  214 50   HOH   HOH B . 
E 3 HOH   15  215 398  HOH   HOH B . 
E 3 HOH   16  216 654  HOH   HOH B . 
E 3 HOH   17  217 221  HOH   HOH B . 
E 3 HOH   18  218 743  HOH   HOH B . 
E 3 HOH   19  219 1278 HOH   HOH B . 
E 3 HOH   20  220 264  HOH   HOH B . 
E 3 HOH   21  221 332  HOH   HOH B . 
E 3 HOH   22  222 343  HOH   HOH B . 
E 3 HOH   23  223 75   HOH   HOH B . 
E 3 HOH   24  224 131  HOH   HOH B . 
E 3 HOH   25  225 1    HOH   HOH B . 
E 3 HOH   26  226 82   HOH   HOH B . 
E 3 HOH   27  227 282  HOH   HOH B . 
E 3 HOH   28  228 133  HOH   HOH B . 
E 3 HOH   29  229 900  HOH   HOH B . 
E 3 HOH   30  230 205  HOH   HOH B . 
E 3 HOH   31  231 54   HOH   HOH B . 
E 3 HOH   32  232 110  HOH   HOH B . 
E 3 HOH   33  233 300  HOH   HOH B . 
E 3 HOH   34  234 1140 HOH   HOH B . 
E 3 HOH   35  235 172  HOH   HOH B . 
E 3 HOH   36  236 272  HOH   HOH B . 
E 3 HOH   37  237 723  HOH   HOH B . 
E 3 HOH   38  238 391  HOH   HOH B . 
E 3 HOH   39  239 150  HOH   HOH B . 
E 3 HOH   40  240 444  HOH   HOH B . 
E 3 HOH   41  241 30   HOH   HOH B . 
E 3 HOH   42  242 325  HOH   HOH B . 
E 3 HOH   43  243 128  HOH   HOH B . 
E 3 HOH   44  244 1312 HOH   HOH B . 
E 3 HOH   45  245 144  HOH   HOH B . 
E 3 HOH   46  246 60   HOH   HOH B . 
E 3 HOH   47  247 416  HOH   HOH B . 
E 3 HOH   48  248 41   HOH   HOH B . 
E 3 HOH   49  249 181  HOH   HOH B . 
E 3 HOH   50  250 52   HOH   HOH B . 
E 3 HOH   51  251 14   HOH   HOH B . 
E 3 HOH   52  252 1277 HOH   HOH B . 
E 3 HOH   53  253 166  HOH   HOH B . 
E 3 HOH   54  254 960  HOH   HOH B . 
E 3 HOH   55  255 31   HOH   HOH B . 
E 3 HOH   56  256 9    HOH   HOH B . 
E 3 HOH   57  257 127  HOH   HOH B . 
E 3 HOH   58  258 47   HOH   HOH B . 
E 3 HOH   59  259 231  HOH   HOH B . 
E 3 HOH   60  260 103  HOH   HOH B . 
E 3 HOH   61  261 271  HOH   HOH B . 
E 3 HOH   62  262 129  HOH   HOH B . 
E 3 HOH   63  263 242  HOH   HOH B . 
E 3 HOH   64  264 10   HOH   HOH B . 
E 3 HOH   65  265 59   HOH   HOH B . 
E 3 HOH   66  266 11   HOH   HOH B . 
E 3 HOH   67  267 347  HOH   HOH B . 
E 3 HOH   68  268 143  HOH   HOH B . 
E 3 HOH   69  269 243  HOH   HOH B . 
E 3 HOH   70  270 61   HOH   HOH B . 
E 3 HOH   71  271 89   HOH   HOH B . 
E 3 HOH   72  272 117  HOH   HOH B . 
E 3 HOH   73  273 1305 HOH   HOH B . 
E 3 HOH   74  274 287  HOH   HOH B . 
E 3 HOH   75  275 20   HOH   HOH B . 
E 3 HOH   76  276 252  HOH   HOH B . 
E 3 HOH   77  277 88   HOH   HOH B . 
E 3 HOH   78  278 77   HOH   HOH B . 
E 3 HOH   79  279 43   HOH   HOH B . 
E 3 HOH   80  280 216  HOH   HOH B . 
E 3 HOH   81  281 84   HOH   HOH B . 
E 3 HOH   82  282 106  HOH   HOH B . 
E 3 HOH   83  283 72   HOH   HOH B . 
E 3 HOH   84  284 13   HOH   HOH B . 
E 3 HOH   85  285 99   HOH   HOH B . 
E 3 HOH   86  286 220  HOH   HOH B . 
E 3 HOH   87  287 175  HOH   HOH B . 
E 3 HOH   88  288 235  HOH   HOH B . 
E 3 HOH   89  289 276  HOH   HOH B . 
E 3 HOH   90  290 197  HOH   HOH B . 
E 3 HOH   91  291 22   HOH   HOH B . 
E 3 HOH   92  292 114  HOH   HOH B . 
E 3 HOH   93  293 302  HOH   HOH B . 
E 3 HOH   94  294 147  HOH   HOH B . 
E 3 HOH   95  295 137  HOH   HOH B . 
E 3 HOH   96  296 311  HOH   HOH B . 
E 3 HOH   97  297 1066 HOH   HOH B . 
E 3 HOH   98  298 1106 HOH   HOH B . 
E 3 HOH   99  299 112  HOH   HOH B . 
E 3 HOH   100 300 32   HOH   HOH B . 
E 3 HOH   101 301 170  HOH   HOH B . 
E 3 HOH   102 302 387  HOH   HOH B . 
E 3 HOH   103 303 160  HOH   HOH B . 
E 3 HOH   104 304 142  HOH   HOH B . 
E 3 HOH   105 305 38   HOH   HOH B . 
E 3 HOH   106 306 118  HOH   HOH B . 
E 3 HOH   107 307 55   HOH   HOH B . 
E 3 HOH   108 308 101  HOH   HOH B . 
E 3 HOH   109 309 215  HOH   HOH B . 
E 3 HOH   110 310 23   HOH   HOH B . 
E 3 HOH   111 311 316  HOH   HOH B . 
E 3 HOH   112 312 91   HOH   HOH B . 
E 3 HOH   113 313 37   HOH   HOH B . 
E 3 HOH   114 314 299  HOH   HOH B . 
E 3 HOH   115 315 297  HOH   HOH B . 
E 3 HOH   116 316 1285 HOH   HOH B . 
E 3 HOH   117 317 44   HOH   HOH B . 
E 3 HOH   118 318 28   HOH   HOH B . 
E 3 HOH   119 319 98   HOH   HOH B . 
E 3 HOH   120 320 635  HOH   HOH B . 
E 3 HOH   121 321 1294 HOH   HOH B . 
E 3 HOH   122 322 100  HOH   HOH B . 
E 3 HOH   123 323 1274 HOH   HOH B . 
E 3 HOH   124 324 161  HOH   HOH B . 
E 3 HOH   125 325 48   HOH   HOH B . 
E 3 HOH   126 326 177  HOH   HOH B . 
E 3 HOH   127 327 207  HOH   HOH B . 
E 3 HOH   128 328 29   HOH   HOH B . 
E 3 HOH   129 329 341  HOH   HOH B . 
E 3 HOH   130 330 141  HOH   HOH B . 
E 3 HOH   131 331 717  HOH   HOH B . 
E 3 HOH   132 332 182  HOH   HOH B . 
E 3 HOH   133 333 704  HOH   HOH B . 
E 3 HOH   134 334 65   HOH   HOH B . 
E 3 HOH   135 335 178  HOH   HOH B . 
E 3 HOH   136 336 334  HOH   HOH B . 
E 3 HOH   137 337 1291 HOH   HOH B . 
E 3 HOH   138 338 234  HOH   HOH B . 
E 3 HOH   139 339 1126 HOH   HOH B . 
E 3 HOH   140 340 619  HOH   HOH B . 
E 3 HOH   141 341 1293 HOH   HOH B . 
E 3 HOH   142 342 87   HOH   HOH B . 
E 3 HOH   143 343 463  HOH   HOH B . 
E 3 HOH   144 344 362  HOH   HOH B . 
E 3 HOH   145 345 90   HOH   HOH B . 
E 3 HOH   146 346 445  HOH   HOH B . 
E 3 HOH   147 347 1304 HOH   HOH B . 
E 3 HOH   148 348 1046 HOH   HOH B . 
E 3 HOH   149 349 623  HOH   HOH B . 
E 3 HOH   150 350 191  HOH   HOH B . 
E 3 HOH   151 351 339  HOH   HOH B . 
E 3 HOH   152 352 335  HOH   HOH B . 
E 3 HOH   153 353 1280 HOH   HOH B . 
E 3 HOH   154 354 304  HOH   HOH B . 
E 3 HOH   155 355 1077 HOH   HOH B . 
E 3 HOH   156 356 541  HOH   HOH B . 
E 3 HOH   157 357 290  HOH   HOH B . 
E 3 HOH   158 358 718  HOH   HOH B . 
E 3 HOH   159 359 479  HOH   HOH B . 
E 3 HOH   160 360 203  HOH   HOH B . 
E 3 HOH   161 361 389  HOH   HOH B . 
E 3 HOH   162 362 1072 HOH   HOH B . 
E 3 HOH   163 363 283  HOH   HOH B . 
E 3 HOH   164 364 291  HOH   HOH B . 
E 3 HOH   165 365 615  HOH   HOH B . 
E 3 HOH   166 366 1316 HOH   HOH B . 
E 3 HOH   167 367 431  HOH   HOH B . 
E 3 HOH   168 368 373  HOH   HOH B . 
E 3 HOH   169 369 340  HOH   HOH B . 
E 3 HOH   170 370 667  HOH   HOH B . 
E 3 HOH   171 371 190  HOH   HOH B . 
E 3 HOH   172 372 310  HOH   HOH B . 
E 3 HOH   173 373 1303 HOH   HOH B . 
E 3 HOH   174 374 898  HOH   HOH B . 
E 3 HOH   175 375 1173 HOH   HOH B . 
E 3 HOH   176 376 149  HOH   HOH B . 
E 3 HOH   177 377 1163 HOH   HOH B . 
E 3 HOH   178 378 1000 HOH   HOH B . 
E 3 HOH   179 379 183  HOH   HOH B . 
E 3 HOH   180 380 176  HOH   HOH B . 
E 3 HOH   181 381 418  HOH   HOH B . 
E 3 HOH   182 382 1311 HOH   HOH B . 
E 3 HOH   183 383 1298 HOH   HOH B . 
E 3 HOH   184 384 491  HOH   HOH B . 
E 3 HOH   185 385 248  HOH   HOH B . 
E 3 HOH   186 386 981  HOH   HOH B . 
E 3 HOH   187 387 424  HOH   HOH B . 
E 3 HOH   188 388 265  HOH   HOH B . 
E 3 HOH   189 389 470  HOH   HOH B . 
E 3 HOH   190 390 184  HOH   HOH B . 
E 3 HOH   191 391 360  HOH   HOH B . 
E 3 HOH   192 392 355  HOH   HOH B . 
E 3 HOH   193 393 410  HOH   HOH B . 
E 3 HOH   194 394 157  HOH   HOH B . 
E 3 HOH   195 395 314  HOH   HOH B . 
E 3 HOH   196 396 566  HOH   HOH B . 
E 3 HOH   197 397 274  HOH   HOH B . 
E 3 HOH   198 398 321  HOH   HOH B . 
E 3 HOH   199 399 792  HOH   HOH B . 
E 3 HOH   200 400 558  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           7HCQ 
_cell.length_a           88.752 
_cell.length_b           88.752 
_cell.length_c           39.447 
_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                         7HCQ 
_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          7HCQ 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.53 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2022-07-25 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.72929 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.pdbx_wavelength_list        0.72929 
_diffrn_source.pdbx_synchrotron_site       SSRL 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HCQ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.380 
_reflns.d_resolution_high            0.980 
_reflns.number_obs                   175816 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.900 
_reflns.pdbx_Rmerge_I_obs            0.051 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.200 
_reflns.B_iso_Wilson_estimate        13.130 
_reflns.pdbx_redundancy              6.700 
_reflns.pdbx_Rrim_I_all              0.056 
_reflns.pdbx_Rpim_I_all              0.022 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1173440 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 0.980 1.000  ? 57662 8643 ? 3.735 ? ? ? 6.700 ? 0.400  ? ? ? ? ? ? 99.300 4.052 1.556 0.306 ? 
1 2 5.370 44.380 ? 7898  1162 ? 0.031 ? ? ? 6.800 ? 52.600 ? ? ? ? ? ? 99.700 0.034 0.013 0.999 ? 
# 
_refine.entry_id                                 7HCQ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9800 
_refine.ls_d_res_low                             28.0700 
_refine.pdbx_ls_sigma_F                          1.330 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.6400 
_refine.ls_number_reflns_obs                     175411 
_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                          0.1530 
_refine.ls_R_factor_R_work                       0.1522 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1688 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  8451 
_refine.ls_number_reflns_R_work                  166960 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               21.5630 
_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                            0.1400 
_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                                86.070 
_refine.B_iso_min                                10.390 
_refine.pdbx_overall_phase_error                 22.1300 
_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                        28.0700 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.number_atoms_solvent             428 
_refine_hist.number_atoms_total               3006 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           16.56 
_refine_hist.pdbx_B_iso_mean_solvent          34.02 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.R_factor_obs 
0.9800 0.9900  30 95.0000  5263 . 0.4836 0.4735 . 269 0.0000 5532 . 'X-RAY DIFFRACTION' . 
0.9900 1.0000  30 99.0000  5530 . 0.4409 0.4236 . 281 0.0000 5811 . 'X-RAY DIFFRACTION' . 
1.0000 1.0200  30 100.0000 5565 . 0.4100 0.3596 . 275 0.0000 5840 . 'X-RAY DIFFRACTION' . 
1.0200 1.0300  30 100.0000 5554 . 0.3727 0.3801 . 252 0.0000 5806 . 'X-RAY DIFFRACTION' . 
1.0300 1.0400  30 100.0000 5525 . 0.3531 0.3406 . 305 0.0000 5830 . 'X-RAY DIFFRACTION' . 
1.0400 1.0600  30 100.0000 5555 . 0.3171 0.3069 . 301 0.0000 5856 . 'X-RAY DIFFRACTION' . 
1.0600 1.0700  30 100.0000 5511 . 0.2920 0.3209 . 314 0.0000 5825 . 'X-RAY DIFFRACTION' . 
1.0700 1.0900  30 100.0000 5549 . 0.2776 0.3006 . 249 0.0000 5798 . 'X-RAY DIFFRACTION' . 
1.0900 1.1000  30 100.0000 5575 . 0.2466 0.2738 . 282 0.0000 5857 . 'X-RAY DIFFRACTION' . 
1.1000 1.1200  30 100.0000 5532 . 0.2331 0.2362 . 286 0.0000 5818 . 'X-RAY DIFFRACTION' . 
1.1200 1.1400  30 100.0000 5592 . 0.2141 0.2202 . 256 0.0000 5848 . 'X-RAY DIFFRACTION' . 
1.1400 1.1600  30 100.0000 5549 . 0.1910 0.1949 . 266 0.0000 5815 . 'X-RAY DIFFRACTION' . 
1.1600 1.1800  30 100.0000 5611 . 0.1746 0.1912 . 290 0.0000 5901 . 'X-RAY DIFFRACTION' . 
1.1800 1.2100  30 100.0000 5428 . 0.1606 0.2028 . 306 0.0000 5734 . 'X-RAY DIFFRACTION' . 
1.2100 1.2300  30 100.0000 5659 . 0.1547 0.1700 . 237 0.0000 5896 . 'X-RAY DIFFRACTION' . 
1.2300 1.2600  30 100.0000 5562 . 0.1495 0.1631 . 287 0.0000 5849 . 'X-RAY DIFFRACTION' . 
1.2600 1.3000  30 100.0000 5563 . 0.1424 0.1608 . 286 0.0000 5849 . 'X-RAY DIFFRACTION' . 
1.3000 1.3300  30 100.0000 5551 . 0.1373 0.1647 . 302 0.0000 5853 . 'X-RAY DIFFRACTION' . 
1.3300 1.3700  30 100.0000 5568 . 0.1431 0.1655 . 297 0.0000 5865 . 'X-RAY DIFFRACTION' . 
1.3700 1.4100  30 100.0000 5618 . 0.1341 0.1726 . 241 0.0000 5859 . 'X-RAY DIFFRACTION' . 
1.4100 1.4600  30 100.0000 5543 . 0.1301 0.1484 . 304 0.0000 5847 . 'X-RAY DIFFRACTION' . 
1.4600 1.5200  30 100.0000 5600 . 0.1212 0.1292 . 265 0.0000 5865 . 'X-RAY DIFFRACTION' . 
1.5200 1.5900  30 100.0000 5578 . 0.1181 0.1349 . 304 0.0000 5882 . 'X-RAY DIFFRACTION' . 
1.5900 1.6800  30 100.0000 5595 . 0.1186 0.1356 . 277 0.0000 5872 . 'X-RAY DIFFRACTION' . 
1.6800 1.7800  30 100.0000 5618 . 0.1260 0.1446 . 268 0.0000 5886 . 'X-RAY DIFFRACTION' . 
1.7800 1.9200  30 100.0000 5558 . 0.1293 0.1457 . 296 0.0000 5854 . 'X-RAY DIFFRACTION' . 
1.9200 2.1100  30 99.0000  5592 . 0.1303 0.1346 . 285 0.0000 5877 . 'X-RAY DIFFRACTION' . 
2.1100 2.4200  30 100.0000 5593 . 0.1352 0.1415 . 303 0.0000 5896 . 'X-RAY DIFFRACTION' . 
2.4200 3.0400  30 100.0000 5658 . 0.1457 0.1721 . 289 0.0000 5947 . 'X-RAY DIFFRACTION' . 
3.0400 28.0700 30 99.0000  5765 . 0.1486 0.1721 . 278 0.0000 6043 . 'X-RAY DIFFRACTION' . 
# 
_struct.entry_id                  7HCQ 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0000345' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HCQ 
_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 7HCQ A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HCQ 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 7HCQ SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HCQ MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HCQ SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HCQ 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 ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HCQ 
_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 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 56.29 -132.99 
2 1 SER A 128 ? B 71.65 -1.03   
3 1 HIS B 86  ? ? 58.58 -128.10 
# 
_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 526 ? 5.97 . 
2 1 O ? A HOH 527 ? 6.17 . 
3 1 O ? A HOH 528 ? 7.74 . 
4 1 O ? B HOH 400 ? 6.32 . 
# 
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 
A1A50 N2   N Y N 1   
A1A50 C3   C Y N 2   
A1A50 C6   C Y N 3   
A1A50 C9   C Y N 4   
A1A50 C12  C Y N 5   
A1A50 C14  C Y N 6   
A1A50 C1   C N N 7   
A1A50 C10  C Y N 8   
A1A50 C11  C Y N 9   
A1A50 C13  C N N 10  
A1A50 C15  C Y N 11  
A1A50 C2   C Y N 12  
A1A50 C4   C Y N 13  
A1A50 C5   C Y N 14  
A1A50 C7   C Y N 15  
A1A50 C8   C Y N 16  
A1A50 N1   N N N 17  
A1A50 N3   N N N 18  
A1A50 O1   O N N 19  
A1A50 O2   O N N 20  
A1A50 S1   S N N 21  
A1A50 S2   S Y N 22  
A1A50 H5   H N N 23  
A1A50 H8   H N N 24  
A1A50 H1   H N N 25  
A1A50 H2   H N N 26  
A1A50 H3   H N N 27  
A1A50 H9   H N N 28  
A1A50 H10  H N N 29  
A1A50 H12  H N N 30  
A1A50 H11  H N N 31  
A1A50 H13  H N N 32  
A1A50 H14  H N N 33  
A1A50 H6   H N N 34  
A1A50 H7   H N N 35  
A1A50 H4   H N N 36  
A1A50 H15  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 
A1A50 C1  N1   sing N N 1   
A1A50 N1  C2   sing N N 2   
A1A50 C2  N2   doub Y N 3   
A1A50 C2  C3   sing Y N 4   
A1A50 N2  C15  sing Y N 5   
A1A50 C11 C10  doub Y N 6   
A1A50 C11 C12  sing Y N 7   
A1A50 C3  C4   doub Y N 8   
A1A50 C10 C9   sing Y N 9   
A1A50 C13 C12  sing N N 10  
A1A50 C15 C5   doub Y N 11  
A1A50 C12 C14  doub Y N 12  
A1A50 C9  C8   doub Y N 13  
A1A50 C14 C8   sing Y N 14  
A1A50 C14 S2   sing Y N 15  
A1A50 C8  C7   sing Y N 16  
A1A50 C4  C5   sing Y N 17  
A1A50 C5  N3   sing N N 18  
A1A50 S2  C6   sing Y N 19  
A1A50 C7  C6   doub Y N 20  
A1A50 C6  S1   sing N N 21  
A1A50 O2  S1   doub N N 22  
A1A50 N3  S1   sing N N 23  
A1A50 S1  O1   doub N N 24  
A1A50 C3  H5   sing N N 25  
A1A50 C9  H8   sing N N 26  
A1A50 C1  H1   sing N N 27  
A1A50 C1  H2   sing N N 28  
A1A50 C1  H3   sing N N 29  
A1A50 C10 H9   sing N N 30  
A1A50 C11 H10  sing N N 31  
A1A50 C13 H12  sing N N 32  
A1A50 C13 H11  sing N N 33  
A1A50 C13 H13  sing N N 34  
A1A50 C15 H14  sing N N 35  
A1A50 C4  H6   sing N N 36  
A1A50 C7  H7   sing N N 37  
A1A50 N1  H4   sing N N 38  
A1A50 N3  H15  sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
GLN   N   CA   sing N N 122 
GLN   N   H    sing N N 123 
GLN   N   H2   sing N N 124 
GLN   CA  C    sing N N 125 
GLN   CA  CB   sing N N 126 
GLN   CA  HA   sing N N 127 
GLN   C   O    doub N N 128 
GLN   C   OXT  sing N N 129 
GLN   CB  CG   sing N N 130 
GLN   CB  HB2  sing N N 131 
GLN   CB  HB3  sing N N 132 
GLN   CG  CD   sing N N 133 
GLN   CG  HG2  sing N N 134 
GLN   CG  HG3  sing N N 135 
GLN   CD  OE1  doub N N 136 
GLN   CD  NE2  sing N N 137 
GLN   NE2 HE21 sing N N 138 
GLN   NE2 HE22 sing N N 139 
GLN   OXT HXT  sing N N 140 
GLU   N   CA   sing N N 141 
GLU   N   H    sing N N 142 
GLU   N   H2   sing N N 143 
GLU   CA  C    sing N N 144 
GLU   CA  CB   sing N N 145 
GLU   CA  HA   sing N N 146 
GLU   C   O    doub N N 147 
GLU   C   OXT  sing N N 148 
GLU   CB  CG   sing N N 149 
GLU   CB  HB2  sing N N 150 
GLU   CB  HB3  sing N N 151 
GLU   CG  CD   sing N N 152 
GLU   CG  HG2  sing N N 153 
GLU   CG  HG3  sing N N 154 
GLU   CD  OE1  doub N N 155 
GLU   CD  OE2  sing N N 156 
GLU   OE2 HE2  sing N N 157 
GLU   OXT HXT  sing N N 158 
GLY   N   CA   sing N N 159 
GLY   N   H    sing N N 160 
GLY   N   H2   sing N N 161 
GLY   CA  C    sing N N 162 
GLY   CA  HA2  sing N N 163 
GLY   CA  HA3  sing N N 164 
GLY   C   O    doub N N 165 
GLY   C   OXT  sing N N 166 
GLY   OXT HXT  sing N N 167 
HIS   N   CA   sing N N 168 
HIS   N   H    sing N N 169 
HIS   N   H2   sing N N 170 
HIS   CA  C    sing N N 171 
HIS   CA  CB   sing N N 172 
HIS   CA  HA   sing N N 173 
HIS   C   O    doub N N 174 
HIS   C   OXT  sing N N 175 
HIS   CB  CG   sing N N 176 
HIS   CB  HB2  sing N N 177 
HIS   CB  HB3  sing N N 178 
HIS   CG  ND1  sing Y N 179 
HIS   CG  CD2  doub Y N 180 
HIS   ND1 CE1  doub Y N 181 
HIS   ND1 HD1  sing N N 182 
HIS   CD2 NE2  sing Y N 183 
HIS   CD2 HD2  sing N N 184 
HIS   CE1 NE2  sing Y N 185 
HIS   CE1 HE1  sing N N 186 
HIS   NE2 HE2  sing N N 187 
HIS   OXT HXT  sing N N 188 
HOH   O   H1   sing N N 189 
HOH   O   H2   sing N N 190 
ILE   N   CA   sing N N 191 
ILE   N   H    sing N N 192 
ILE   N   H2   sing N N 193 
ILE   CA  C    sing N N 194 
ILE   CA  CB   sing N N 195 
ILE   CA  HA   sing N N 196 
ILE   C   O    doub N N 197 
ILE   C   OXT  sing N N 198 
ILE   CB  CG1  sing N N 199 
ILE   CB  CG2  sing N N 200 
ILE   CB  HB   sing N N 201 
ILE   CG1 CD1  sing N N 202 
ILE   CG1 HG12 sing N N 203 
ILE   CG1 HG13 sing N N 204 
ILE   CG2 HG21 sing N N 205 
ILE   CG2 HG22 sing N N 206 
ILE   CG2 HG23 sing N N 207 
ILE   CD1 HD11 sing N N 208 
ILE   CD1 HD12 sing N N 209 
ILE   CD1 HD13 sing N N 210 
ILE   OXT HXT  sing N N 211 
LEU   N   CA   sing N N 212 
LEU   N   H    sing N N 213 
LEU   N   H2   sing N N 214 
LEU   CA  C    sing N N 215 
LEU   CA  CB   sing N N 216 
LEU   CA  HA   sing N N 217 
LEU   C   O    doub N N 218 
LEU   C   OXT  sing N N 219 
LEU   CB  CG   sing N N 220 
LEU   CB  HB2  sing N N 221 
LEU   CB  HB3  sing N N 222 
LEU   CG  CD1  sing N N 223 
LEU   CG  CD2  sing N N 224 
LEU   CG  HG   sing N N 225 
LEU   CD1 HD11 sing N N 226 
LEU   CD1 HD12 sing N N 227 
LEU   CD1 HD13 sing N N 228 
LEU   CD2 HD21 sing N N 229 
LEU   CD2 HD22 sing N N 230 
LEU   CD2 HD23 sing N N 231 
LEU   OXT HXT  sing N N 232 
LYS   N   CA   sing N N 233 
LYS   N   H    sing N N 234 
LYS   N   H2   sing N N 235 
LYS   CA  C    sing N N 236 
LYS   CA  CB   sing N N 237 
LYS   CA  HA   sing N N 238 
LYS   C   O    doub N N 239 
LYS   C   OXT  sing N N 240 
LYS   CB  CG   sing N N 241 
LYS   CB  HB2  sing N N 242 
LYS   CB  HB3  sing N N 243 
LYS   CG  CD   sing N N 244 
LYS   CG  HG2  sing N N 245 
LYS   CG  HG3  sing N N 246 
LYS   CD  CE   sing N N 247 
LYS   CD  HD2  sing N N 248 
LYS   CD  HD3  sing N N 249 
LYS   CE  NZ   sing N N 250 
LYS   CE  HE2  sing N N 251 
LYS   CE  HE3  sing N N 252 
LYS   NZ  HZ1  sing N N 253 
LYS   NZ  HZ2  sing N N 254 
LYS   NZ  HZ3  sing N N 255 
LYS   OXT HXT  sing N N 256 
MET   N   CA   sing N N 257 
MET   N   H    sing N N 258 
MET   N   H2   sing N N 259 
MET   CA  C    sing N N 260 
MET   CA  CB   sing N N 261 
MET   CA  HA   sing N N 262 
MET   C   O    doub N N 263 
MET   C   OXT  sing N N 264 
MET   CB  CG   sing N N 265 
MET   CB  HB2  sing N N 266 
MET   CB  HB3  sing N N 267 
MET   CG  SD   sing N N 268 
MET   CG  HG2  sing N N 269 
MET   CG  HG3  sing N N 270 
MET   SD  CE   sing N N 271 
MET   CE  HE1  sing N N 272 
MET   CE  HE2  sing N N 273 
MET   CE  HE3  sing N N 274 
MET   OXT HXT  sing N N 275 
PHE   N   CA   sing N N 276 
PHE   N   H    sing N N 277 
PHE   N   H2   sing N N 278 
PHE   CA  C    sing N N 279 
PHE   CA  CB   sing N N 280 
PHE   CA  HA   sing N N 281 
PHE   C   O    doub N N 282 
PHE   C   OXT  sing N N 283 
PHE   CB  CG   sing N N 284 
PHE   CB  HB2  sing N N 285 
PHE   CB  HB3  sing N N 286 
PHE   CG  CD1  doub Y N 287 
PHE   CG  CD2  sing Y N 288 
PHE   CD1 CE1  sing Y N 289 
PHE   CD1 HD1  sing N N 290 
PHE   CD2 CE2  doub Y N 291 
PHE   CD2 HD2  sing N N 292 
PHE   CE1 CZ   doub Y N 293 
PHE   CE1 HE1  sing N N 294 
PHE   CE2 CZ   sing Y N 295 
PHE   CE2 HE2  sing N N 296 
PHE   CZ  HZ   sing N N 297 
PHE   OXT HXT  sing N N 298 
PRO   N   CA   sing N N 299 
PRO   N   CD   sing N N 300 
PRO   N   H    sing N N 301 
PRO   CA  C    sing N N 302 
PRO   CA  CB   sing N N 303 
PRO   CA  HA   sing N N 304 
PRO   C   O    doub N N 305 
PRO   C   OXT  sing N N 306 
PRO   CB  CG   sing N N 307 
PRO   CB  HB2  sing N N 308 
PRO   CB  HB3  sing N N 309 
PRO   CG  CD   sing N N 310 
PRO   CG  HG2  sing N N 311 
PRO   CG  HG3  sing N N 312 
PRO   CD  HD2  sing N N 313 
PRO   CD  HD3  sing N N 314 
PRO   OXT HXT  sing N N 315 
SER   N   CA   sing N N 316 
SER   N   H    sing N N 317 
SER   N   H2   sing N N 318 
SER   CA  C    sing N N 319 
SER   CA  CB   sing N N 320 
SER   CA  HA   sing N N 321 
SER   C   O    doub N N 322 
SER   C   OXT  sing N N 323 
SER   CB  OG   sing N N 324 
SER   CB  HB2  sing N N 325 
SER   CB  HB3  sing N N 326 
SER   OG  HG   sing N N 327 
SER   OXT HXT  sing N N 328 
THR   N   CA   sing N N 329 
THR   N   H    sing N N 330 
THR   N   H2   sing N N 331 
THR   CA  C    sing N N 332 
THR   CA  CB   sing N N 333 
THR   CA  HA   sing N N 334 
THR   C   O    doub N N 335 
THR   C   OXT  sing N N 336 
THR   CB  OG1  sing N N 337 
THR   CB  CG2  sing N N 338 
THR   CB  HB   sing N N 339 
THR   OG1 HG1  sing N N 340 
THR   CG2 HG21 sing N N 341 
THR   CG2 HG22 sing N N 342 
THR   CG2 HG23 sing N N 343 
THR   OXT HXT  sing N N 344 
TYR   N   CA   sing N N 345 
TYR   N   H    sing N N 346 
TYR   N   H2   sing N N 347 
TYR   CA  C    sing N N 348 
TYR   CA  CB   sing N N 349 
TYR   CA  HA   sing N N 350 
TYR   C   O    doub N N 351 
TYR   C   OXT  sing N N 352 
TYR   CB  CG   sing N N 353 
TYR   CB  HB2  sing N N 354 
TYR   CB  HB3  sing N N 355 
TYR   CG  CD1  doub Y N 356 
TYR   CG  CD2  sing Y N 357 
TYR   CD1 CE1  sing Y N 358 
TYR   CD1 HD1  sing N N 359 
TYR   CD2 CE2  doub Y N 360 
TYR   CD2 HD2  sing N N 361 
TYR   CE1 CZ   doub Y N 362 
TYR   CE1 HE1  sing N N 363 
TYR   CE2 CZ   sing Y N 364 
TYR   CE2 HE2  sing N N 365 
TYR   CZ  OH   sing N N 366 
TYR   OH  HH   sing N N 367 
TYR   OXT HXT  sing N N 368 
VAL   N   CA   sing N N 369 
VAL   N   H    sing N N 370 
VAL   N   H2   sing N N 371 
VAL   CA  C    sing N N 372 
VAL   CA  CB   sing N N 373 
VAL   CA  HA   sing N N 374 
VAL   C   O    doub N N 375 
VAL   C   OXT  sing N N 376 
VAL   CB  CG1  sing N N 377 
VAL   CB  CG2  sing N N 378 
VAL   CB  HB   sing N N 379 
VAL   CG1 HG11 sing N N 380 
VAL   CG1 HG12 sing N N 381 
VAL   CG1 HG13 sing N N 382 
VAL   CG2 HG21 sing N N 383 
VAL   CG2 HG22 sing N N 384 
VAL   CG2 HG23 sing N N 385 
VAL   OXT HXT  sing N N 386 
# 
_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                    7HCQ 
_atom_sites.fract_transf_matrix[1][1]   0.011267 
_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]   0.011267 
_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]   0.025350 
_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    . VAL   A 1 3   ? 19.552 -15.934 22.247  1.00 68.34 ?  3   VAL   A N    1 
ATOM   2    C CA   . VAL   A 1 3   ? 18.585 -14.861 22.440  1.00 67.60 ?  3   VAL   A CA   1 
ATOM   3    C C    . VAL   A 1 3   ? 19.241 -13.509 22.183  1.00 62.64 ?  3   VAL   A C    1 
ATOM   4    O O    . VAL   A 1 3   ? 20.309 -13.219 22.724  1.00 63.45 ?  3   VAL   A O    1 
ATOM   5    C CB   . VAL   A 1 3   ? 17.958 -14.917 23.850  1.00 70.74 ?  3   VAL   A CB   1 
ATOM   6    C CG1  . VAL   A 1 3   ? 16.908 -13.826 24.012  1.00 71.72 ?  3   VAL   A CG1  1 
ATOM   7    C CG2  . VAL   A 1 3   ? 17.355 -16.290 24.113  1.00 71.72 ?  3   VAL   A CG2  1 
ATOM   8    H HA   . VAL   A 1 3   ? 17.869 -14.969 21.800  1.00 81.13 ?  3   VAL   A HA   1 
ATOM   9    H HB   . VAL   A 1 3   ? 18.648 -14.764 24.513  1.00 84.90 ?  3   VAL   A HB   1 
ATOM   10   H HG11 . VAL   A 1 3   ? 16.420 -13.977 24.837  1.00 86.07 ?  3   VAL   A HG11 1 
ATOM   11   H HG12 . VAL   A 1 3   ? 17.348 -12.962 24.043  1.00 86.07 ?  3   VAL   A HG12 1 
ATOM   12   H HG13 . VAL   A 1 3   ? 16.299 -13.862 23.258  1.00 86.07 ?  3   VAL   A HG13 1 
ATOM   13   H HG21 . VAL   A 1 3   ? 16.885 -16.272 24.961  1.00 86.07 ?  3   VAL   A HG21 1 
ATOM   14   H HG22 . VAL   A 1 3   ? 16.737 -16.503 23.397  1.00 86.07 ?  3   VAL   A HG22 1 
ATOM   15   H HG23 . VAL   A 1 3   ? 18.067 -16.947 24.143  1.00 86.07 ?  3   VAL   A HG23 1 
ATOM   16   N N    A ASN   A 1 4   ? 18.596 -12.697 21.346  0.48 59.31 ?  4   ASN   A N    1 
ATOM   17   N N    B ASN   A 1 4   ? 18.605 -12.676 21.361  0.52 59.30 ?  4   ASN   A N    1 
ATOM   18   C CA   A ASN   A 1 4   ? 19.042 -11.343 21.047  0.48 55.57 ?  4   ASN   A CA   1 
ATOM   19   C CA   B ASN   A 1 4   ? 19.107 -11.337 21.072  0.52 55.55 ?  4   ASN   A CA   1 
ATOM   20   C C    A ASN   A 1 4   ? 17.888 -10.374 21.288  0.48 52.00 ?  4   ASN   A C    1 
ATOM   21   C C    B ASN   A 1 4   ? 18.002 -10.314 21.318  0.52 52.11 ?  4   ASN   A C    1 
ATOM   22   O O    A ASN   A 1 4   ? 16.775 -10.774 21.646  0.48 52.07 ?  4   ASN   A O    1 
ATOM   23   O O    B ASN   A 1 4   ? 16.877 -10.657 21.696  0.52 52.16 ?  4   ASN   A O    1 
ATOM   24   C CB   A ASN   A 1 4   ? 19.610 -11.234 19.624  0.48 55.08 ?  4   ASN   A CB   1 
ATOM   25   C CB   B ASN   A 1 4   ? 19.689 -11.236 19.655  0.52 54.94 ?  4   ASN   A CB   1 
ATOM   26   C CG   A ASN   A 1 4   ? 18.630 -11.687 18.563  0.48 54.48 ?  4   ASN   A CG   1 
ATOM   27   C CG   B ASN   A 1 4   ? 18.700 -11.632 18.582  0.52 54.24 ?  4   ASN   A CG   1 
ATOM   28   O OD1  A ASN   A 1 4   ? 17.469 -11.276 18.553  0.48 54.34 ?  4   ASN   A OD1  1 
ATOM   29   O OD1  B ASN   A 1 4   ? 17.545 -11.204 18.592  0.52 54.05 ?  4   ASN   A OD1  1 
ATOM   30   N ND2  A ASN   A 1 4   ? 19.094 -12.545 17.660  0.48 54.22 ?  4   ASN   A ND2  1 
ATOM   31   N ND2  B ASN   A 1 4   ? 19.151 -12.457 17.644  0.52 53.95 ?  4   ASN   A ND2  1 
ATOM   32   H H    A ASN   A 1 4   ? 17.876 -12.920 20.932  0.48 71.18 ?  4   ASN   A H    1 
ATOM   33   H H    B ASN   A 1 4   ? 17.868 -12.869 20.960  0.52 71.17 ?  4   ASN   A H    1 
ATOM   34   H HA   A ASN   A 1 4   ? 19.753 -11.112 21.657  0.48 66.69 ?  4   ASN   A HA   1 
ATOM   35   H HA   B ASN   A 1 4   ? 19.828 -11.145 21.684  0.52 66.67 ?  4   ASN   A HA   1 
ATOM   36   H HB2  A ASN   A 1 4   ? 19.840 -10.307 19.446  0.48 66.11 ?  4   ASN   A HB2  1 
ATOM   37   H HB2  B ASN   A 1 4   ? 19.962 -10.318 19.492  0.52 65.94 ?  4   ASN   A HB2  1 
ATOM   38   H HB3  A ASN   A 1 4   ? 20.403 -11.789 19.557  0.48 66.11 ?  4   ASN   A HB3  1 
ATOM   39   H HB3  B ASN   A 1 4   ? 20.456 -11.824 19.588  0.52 65.94 ?  4   ASN   A HB3  1 
ATOM   40   H HD21 A ASN   A 1 4   ? 18.580 -12.833 17.034  0.48 65.07 ?  4   ASN   A HD21 1 
ATOM   41   H HD21 B ASN   A 1 4   ? 18.632 -12.711 17.009  0.52 64.75 ?  4   ASN   A HD21 1 
ATOM   42   H HD22 A ASN   A 1 4   ? 19.911 -12.813 17.701  0.48 65.07 ?  4   ASN   A HD22 1 
ATOM   43   H HD22 B ASN   A 1 4   ? 19.964 -12.737 17.673  0.52 64.75 ?  4   ASN   A HD22 1 
ATOM   44   N N    A SER   A 1 5   ? 18.158 -9.085  21.088  0.48 48.02 ?  5   SER   A N    1 
ATOM   45   N N    B SER   A 1 5   ? 18.333 -9.041  21.100  0.52 48.31 ?  5   SER   A N    1 
ATOM   46   C CA   A SER   A 1 5   ? 17.235 -8.020  21.461  0.48 43.88 ?  5   SER   A CA   1 
ATOM   47   C CA   B SER   A 1 5   ? 17.462 -7.930  21.460  0.52 44.36 ?  5   SER   A CA   1 
ATOM   48   C C    A SER   A 1 5   ? 16.394 -7.512  20.295  0.48 38.83 ?  5   SER   A C    1 
ATOM   49   C C    B SER   A 1 5   ? 16.596 -7.445  20.302  0.52 39.54 ?  5   SER   A C    1 
ATOM   50   O O    A SER   A 1 5   ? 15.770 -6.452  20.416  0.48 38.84 ?  5   SER   A O    1 
ATOM   51   O O    B SER   A 1 5   ? 15.939 -6.406  20.430  0.52 39.46 ?  5   SER   A O    1 
ATOM   52   C CB   A SER   A 1 5   ? 17.999 -6.857  22.096  0.48 44.73 ?  5   SER   A CB   1 
ATOM   53   C CB   B SER   A 1 5   ? 18.282 -6.768  22.027  0.52 45.25 ?  5   SER   A CB   1 
ATOM   54   O OG   A SER   A 1 5   ? 18.983 -6.350  21.211  0.48 45.14 ?  5   SER   A OG   1 
ATOM   55   O OG   B SER   A 1 5   ? 19.110 -6.193  21.032  0.52 45.66 ?  5   SER   A OG   1 
ATOM   56   H H    A SER   A 1 5   ? 18.883 -8.801  20.726  0.48 57.64 ?  5   SER   A H    1 
ATOM   57   H H    B SER   A 1 5   ? 19.070 -8.797  20.732  0.52 57.98 ?  5   SER   A H    1 
ATOM   58   H HA   A SER   A 1 5   ? 16.630 -8.366  22.136  0.48 52.67 ?  5   SER   A HA   1 
ATOM   59   H HA   B SER   A 1 5   ? 16.865 -8.226  22.161  0.52 53.24 ?  5   SER   A HA   1 
ATOM   60   H HB2  A SER   A 1 5   ? 17.371 -6.147  22.309  0.48 53.69 ?  5   SER   A HB2  1 
ATOM   61   H HB2  B SER   A 1 5   ? 17.674 -6.092  22.370  0.52 54.30 ?  5   SER   A HB2  1 
ATOM   62   H HB3  A SER   A 1 5   ? 18.431 -7.168  22.907  0.48 53.69 ?  5   SER   A HB3  1 
ATOM   63   H HB3  B SER   A 1 5   ? 18.843 -7.099  22.746  0.52 54.30 ?  5   SER   A HB3  1 
ATOM   64   H HG   A SER   A 1 5   ? 19.394 -5.713  21.573  0.48 54.18 ?  5   SER   A HG   1 
ATOM   65   H HG   B SER   A 1 5   ? 19.545 -5.552  21.357  0.52 54.80 ?  5   SER   A HG   1 
ATOM   66   N N    A PHE   A 1 6   ? 16.364 -8.227  19.174  0.48 33.50 ?  6   PHE   A N    1 
ATOM   67   N N    B PHE   A 1 6   ? 16.582 -8.159  19.180  0.52 34.58 ?  6   PHE   A N    1 
ATOM   68   C CA   A PHE   A 1 6   ? 15.474 -7.853  18.082  0.48 28.44 ?  6   PHE   A CA   1 
ATOM   69   C CA   B PHE   A 1 6   ? 15.619 -7.861  18.130  0.52 30.09 ?  6   PHE   A CA   1 
ATOM   70   C C    A PHE   A 1 6   ? 14.040 -8.218  18.440  0.48 26.92 ?  6   PHE   A C    1 
ATOM   71   C C    B PHE   A 1 6   ? 14.230 -8.273  18.598  0.52 28.65 ?  6   PHE   A C    1 
ATOM   72   O O    A PHE   A 1 6   ? 13.767 -9.340  18.876  0.48 27.58 ?  6   PHE   A O    1 
ATOM   73   O O    B PHE   A 1 6   ? 14.056 -9.335  19.199  0.52 29.48 ?  6   PHE   A O    1 
ATOM   74   C CB   A PHE   A 1 6   ? 15.887 -8.563  16.796  0.48 25.65 ?  6   PHE   A CB   1 
ATOM   75   C CB   B PHE   A 1 6   ? 15.974 -8.628  16.855  0.52 27.78 ?  6   PHE   A CB   1 
ATOM   76   C CG   A PHE   A 1 6   ? 17.139 -8.011  16.177  0.48 23.43 ?  6   PHE   A CG   1 
ATOM   77   C CG   B PHE   A 1 6   ? 17.266 -8.192  16.214  0.52 25.90 ?  6   PHE   A CG   1 
ATOM   78   C CD1  A PHE   A 1 6   ? 17.110 -6.818  15.475  0.48 22.50 ?  6   PHE   A CD1  1 
ATOM   79   C CD1  B PHE   A 1 6   ? 17.303 -7.084  15.383  0.52 25.04 ?  6   PHE   A CD1  1 
ATOM   80   C CD2  A PHE   A 1 6   ? 18.342 -8.687  16.292  0.48 23.45 ?  6   PHE   A CD2  1 
ATOM   81   C CD2  B PHE   A 1 6   ? 18.437 -8.903  16.425  0.52 25.90 ?  6   PHE   A CD2  1 
ATOM   82   C CE1  A PHE   A 1 6   ? 18.259 -6.306  14.903  0.48 21.93 ?  6   PHE   A CE1  1 
ATOM   83   C CE1  B PHE   A 1 6   ? 18.487 -6.683  14.784  0.52 24.59 ?  6   PHE   A CE1  1 
ATOM   84   C CE2  A PHE   A 1 6   ? 19.492 -8.181  15.722  0.48 23.09 ?  6   PHE   A CE2  1 
ATOM   85   C CE2  B PHE   A 1 6   ? 19.623 -8.508  15.830  0.52 25.60 ?  6   PHE   A CE2  1 
ATOM   86   C CZ   A PHE   A 1 6   ? 19.450 -6.990  15.026  0.48 22.29 ?  6   PHE   A CZ   1 
ATOM   87   C CZ   B PHE   A 1 6   ? 19.648 -7.397  15.007  0.52 24.91 ?  6   PHE   A CZ   1 
ATOM   88   H H    A PHE   A 1 6   ? 16.847 -8.922  19.021  0.48 40.20 ?  6   PHE   A H    1 
ATOM   89   H H    B PHE   A 1 6   ? 17.109 -8.815  19.005  0.52 41.50 ?  6   PHE   A H    1 
ATOM   90   H HA   A PHE   A 1 6   ? 15.517 -6.899  17.941  0.48 34.14 ?  6   PHE   A HA   1 
ATOM   91   H HA   B PHE   A 1 6   ? 15.618 -6.912  17.940  0.52 36.11 ?  6   PHE   A HA   1 
ATOM   92   H HB2  A PHE   A 1 6   ? 16.040 -9.501  16.995  0.48 30.79 ?  6   PHE   A HB2  1 
ATOM   93   H HB2  B PHE   A 1 6   ? 16.054 -9.571  17.071  0.52 33.35 ?  6   PHE   A HB2  1 
ATOM   94   H HB3  A PHE   A 1 6   ? 15.169 -8.479  16.150  0.48 30.79 ?  6   PHE   A HB3  1 
ATOM   95   H HB3  B PHE   A 1 6   ? 15.265 -8.499  16.207  0.52 33.35 ?  6   PHE   A HB3  1 
ATOM   96   H HD1  A PHE   A 1 6   ? 16.305 -6.354  15.392  0.48 27.01 ?  6   PHE   A HD1  1 
ATOM   97   H HD1  B PHE   A 1 6   ? 16.526 -6.600  15.230  0.52 30.05 ?  6   PHE   A HD1  1 
ATOM   98   H HD2  A PHE   A 1 6   ? 18.372 -9.492  16.763  0.48 28.14 ?  6   PHE   A HD2  1 
ATOM   99   H HD2  B PHE   A 1 6   ? 18.428 -9.652  16.977  0.52 31.09 ?  6   PHE   A HD2  1 
ATOM   100  H HE1  A PHE   A 1 6   ? 18.227 -5.502  14.434  0.48 26.32 ?  6   PHE   A HE1  1 
ATOM   101  H HE1  B PHE   A 1 6   ? 18.501 -5.937  14.230  0.52 29.51 ?  6   PHE   A HE1  1 
ATOM   102  H HE2  A PHE   A 1 6   ? 20.294 -8.645  15.807  0.48 27.71 ?  6   PHE   A HE2  1 
ATOM   103  H HE2  B PHE   A 1 6   ? 20.405 -8.992  15.980  0.52 30.73 ?  6   PHE   A HE2  1 
ATOM   104  H HZ   A PHE   A 1 6   ? 20.222 -6.648  14.642  0.48 26.75 ?  6   PHE   A HZ   1 
ATOM   105  H HZ   B PHE   A 1 6   ? 20.445 -7.132  14.605  0.52 29.89 ?  6   PHE   A HZ   1 
ATOM   106  N N    A SER   A 1 7   ? 13.118 -7.274  18.248  0.48 24.88 ?  7   SER   A N    1 
ATOM   107  N N    B SER   A 1 7   ? 13.236 -7.425  18.334  0.52 26.59 ?  7   SER   A N    1 
ATOM   108  C CA   A SER   A 1 7   ? 11.741 -7.424  18.701  0.48 23.92 ?  7   SER   A CA   1 
ATOM   109  C CA   B SER   A 1 7   ? 11.874 -7.702  18.771  0.52 25.51 ?  7   SER   A CA   1 
ATOM   110  C C    A SER   A 1 7   ? 10.762 -7.155  17.565  0.48 21.96 ?  7   SER   A C    1 
ATOM   111  C C    B SER   A 1 7   ? 10.882 -7.278  17.699  0.52 23.59 ?  7   SER   A C    1 
ATOM   112  O O    A SER   A 1 7   ? 10.971 -6.254  16.747  0.48 22.34 ?  7   SER   A O    1 
ATOM   113  O O    B SER   A 1 7   ? 11.158 -6.394  16.883  0.52 23.84 ?  7   SER   A O    1 
ATOM   114  C CB   A SER   A 1 7   ? 11.454 -6.464  19.866  0.48 25.41 ?  7   SER   A CB   1 
ATOM   115  C CB   B SER   A 1 7   ? 11.540 -6.991  20.092  0.52 26.66 ?  7   SER   A CB   1 
ATOM   116  O OG   A SER   A 1 7   ? 10.112 -6.571  20.302  0.48 26.11 ?  7   SER   A OG   1 
ATOM   117  O OG   B SER   A 1 7   ? 11.328 -5.604  19.893  0.52 27.46 ?  7   SER   A OG   1 
ATOM   118  H H    A SER   A 1 7   ? 13.271 -6.529  17.851  0.48 29.87 ?  7   SER   A H    1 
ATOM   119  H H    B SER   A 1 7   ? 13.325 -6.685  17.904  0.52 31.92 ?  7   SER   A H    1 
ATOM   120  H HA   A SER   A 1 7   ? 11.599 -8.331  19.019  0.48 28.72 ?  7   SER   A HA   1 
ATOM   121  H HA   B SER   A 1 7   ? 11.770 -8.656  18.910  0.52 30.62 ?  7   SER   A HA   1 
ATOM   122  H HB2  A SER   A 1 7   ? 12.046 -6.681  20.606  0.48 30.50 ?  7   SER   A HB2  1 
ATOM   123  H HB2  B SER   A 1 7   ? 10.736 -7.382  20.465  0.52 32.00 ?  7   SER   A HB2  1 
ATOM   124  H HB3  A SER   A 1 7   ? 11.615 -5.555  19.572  0.48 30.50 ?  7   SER   A HB3  1 
ATOM   125  H HB3  B SER   A 1 7   ? 12.281 -7.110  20.707  0.52 32.00 ?  7   SER   A HB3  1 
ATOM   126  H HG   A SER   A 1 7   ? 9.974  -6.044  20.943  0.48 31.34 ?  7   SER   A HG   1 
ATOM   127  H HG   B SER   A 1 7   ? 11.148 -5.233  20.625  0.52 32.96 ?  7   SER   A HG   1 
ATOM   128  N N    A GLY   A 1 8   ? 9.688  -7.946  17.523  0.48 20.52 ?  8   GLY   A N    1 
ATOM   129  N N    B GLY   A 1 8   ? 9.718  -7.927  17.709  0.52 22.30 ?  8   GLY   A N    1 
ATOM   130  C CA   A GLY   A 1 8   ? 8.602  -7.708  16.591  0.48 19.87 ?  8   GLY   A CA   1 
ATOM   131  C CA   B GLY   A 1 8   ? 8.655  -7.601  16.786  0.52 21.35 ?  8   GLY   A CA   1 
ATOM   132  C C    A GLY   A 1 8   ? 8.819  -8.212  15.181  0.48 18.75 ?  8   GLY   A C    1 
ATOM   133  C C    B GLY   A 1 8   ? 8.849  -8.110  15.382  0.52 19.72 ?  8   GLY   A C    1 
ATOM   134  O O    A GLY   A 1 8   ? 8.129  -7.755  14.263  0.48 19.18 ?  8   GLY   A O    1 
ATOM   135  O O    B GLY   A 1 8   ? 8.099  -7.706  14.486  0.52 19.70 ?  8   GLY   A O    1 
ATOM   136  H H    A GLY   A 1 8   ? 9.569  -8.625  18.040  0.48 24.63 ?  8   GLY   A H    1 
ATOM   137  H H    B GLY   A 1 8   ? 9.525  -8.572  18.245  0.52 26.76 ?  8   GLY   A H    1 
ATOM   138  H HA2  A GLY   A 1 8   ? 7.798  -8.127  16.946  0.48 23.85 ?  8   GLY   A HA2  1 
ATOM   139  H HA2  B GLY   A 1 8   ? 7.822  -7.971  17.114  0.52 25.63 ?  8   GLY   A HA2  1 
ATOM   140  H HA3  A GLY   A 1 8   ? 8.436  -6.752  16.548  0.48 23.85 ?  8   GLY   A HA3  1 
ATOM   141  H HA3  B GLY   A 1 8   ? 8.562  -6.641  16.733  0.52 25.63 ?  8   GLY   A HA3  1 
ATOM   142  N N    A TYR   A 1 9   ? 9.754  -9.137  14.974  0.48 17.84 ?  9   TYR   A N    1 
ATOM   143  N N    B TYR   A 1 9   ? 9.827  -8.983  15.155  0.52 18.32 ?  9   TYR   A N    1 
ATOM   144  C CA   A TYR   A 1 9   ? 10.017 -9.695  13.655  0.48 16.62 ?  9   TYR   A CA   1 
ATOM   145  C CA   B TYR   A 1 9   ? 10.096 -9.489  13.821  0.52 17.12 ?  9   TYR   A CA   1 
ATOM   146  C C    A TYR   A 1 9   ? 9.145  -10.915 13.389  0.48 15.63 ?  9   TYR   A C    1 
ATOM   147  C C    B TYR   A 1 9   ? 9.287  -10.746 13.536  0.52 15.94 ?  9   TYR   A C    1 
ATOM   148  O O    A TYR   A 1 9   ? 8.784  -11.661 14.303  0.48 16.68 ?  9   TYR   A O    1 
ATOM   149  O O    B TYR   A 1 9   ? 9.164  -11.632 14.387  0.52 17.15 ?  9   TYR   A O    1 
ATOM   150  C CB   A TYR   A 1 9   ? 11.482 -10.125 13.532  0.48 16.95 ?  9   TYR   A CB   1 
ATOM   151  C CB   B TYR   A 1 9   ? 11.586 -9.785  13.647  0.52 17.49 ?  9   TYR   A CB   1 
ATOM   152  C CG   A TYR   A 1 9   ? 12.435 -8.975  13.348  0.48 16.32 ?  9   TYR   A CG   1 
ATOM   153  C CG   B TYR   A 1 9   ? 12.441 -8.546  13.490  0.52 16.97 ?  9   TYR   A CG   1 
ATOM   154  C CD1  A TYR   A 1 9   ? 12.816 -8.199  14.427  0.48 16.12 ?  9   TYR   A CD1  1 
ATOM   155  C CD1  B TYR   A 1 9   ? 12.716 -7.729  14.576  0.52 17.35 ?  9   TYR   A CD1  1 
ATOM   156  C CD2  A TYR   A 1 9   ? 12.942 -8.659  12.095  0.48 16.43 ?  9   TYR   A CD2  1 
ATOM   157  C CD2  B TYR   A 1 9   ? 12.955 -8.186  12.250  0.52 16.53 ?  9   TYR   A CD2  1 
ATOM   158  C CE1  A TYR   A 1 9   ? 13.672 -7.137  14.270  0.48 16.76 ?  9   TYR   A CE1  1 
ATOM   159  C CE1  B TYR   A 1 9   ? 13.481 -6.590  14.436  0.52 17.23 ?  9   TYR   A CE1  1 
ATOM   160  C CE2  A TYR   A 1 9   ? 13.798 -7.597  11.925  0.48 16.23 ?  9   TYR   A CE2  1 
ATOM   161  C CE2  B TYR   A 1 9   ? 13.722 -7.053  12.100  0.52 16.28 ?  9   TYR   A CE2  1 
ATOM   162  C CZ   A TYR   A 1 9   ? 14.161 -6.839  13.016  0.48 16.89 ?  9   TYR   A CZ   1 
ATOM   163  C CZ   B TYR   A 1 9   ? 13.980 -6.263  13.193  0.52 16.99 ?  9   TYR   A CZ   1 
ATOM   164  O OH   A TYR   A 1 9   ? 15.015 -5.776  12.858  0.48 17.79 ?  9   TYR   A OH   1 
ATOM   165  O OH   B TYR   A 1 9   ? 14.739 -5.135  13.027  0.52 17.65 ?  9   TYR   A OH   1 
ATOM   166  H H    A TYR   A 1 9   ? 10.249 -9.459  15.595  0.48 21.42 ?  9   TYR   A H    1 
ATOM   167  H H    B TYR   A 1 9   ? 10.347 -9.307  15.762  0.52 22.00 ?  9   TYR   A H    1 
ATOM   168  H HA   A TYR   A 1 9   ? 9.832  -9.022  12.977  0.48 19.95 ?  9   TYR   A HA   1 
ATOM   169  H HA   B TYR   A 1 9   ? 9.852  -8.818  13.169  0.52 20.55 ?  9   TYR   A HA   1 
ATOM   170  H HB2  A TYR   A 1 9   ? 11.736 -10.599 14.340  0.48 20.35 ?  9   TYR   A HB2  1 
ATOM   171  H HB2  B TYR   A 1 9   ? 11.915 -10.305 14.404  0.52 20.99 ?  9   TYR   A HB2  1 
ATOM   172  H HB3  A TYR   A 1 9   ? 11.566 -10.710 12.765  0.48 20.35 ?  9   TYR   A HB3  1 
ATOM   173  H HB3  B TYR   A 1 9   ? 11.665 -10.295 12.833  0.52 20.99 ?  9   TYR   A HB3  1 
ATOM   174  H HD1  A TYR   A 1 9   ? 12.477 -8.398  15.275  0.48 19.35 ?  9   TYR   A HD1  1 
ATOM   175  H HD1  B TYR   A 1 9   ? 12.378 -7.954  15.414  0.52 20.83 ?  9   TYR   A HD1  1 
ATOM   176  H HD2  A TYR   A 1 9   ? 12.691 -9.175  11.360  0.48 19.72 ?  9   TYR   A HD2  1 
ATOM   177  H HD2  B TYR   A 1 9   ? 12.777 -8.720  11.509  0.52 19.84 ?  9   TYR   A HD2  1 
ATOM   178  H HE1  A TYR   A 1 9   ? 13.919 -6.628  15.006  0.48 20.12 ?  9   TYR   A HE1  1 
ATOM   179  H HE1  B TYR   A 1 9   ? 13.664 -6.048  15.172  0.52 20.69 ?  9   TYR   A HE1  1 
ATOM   180  H HE2  A TYR   A 1 9   ? 14.137 -7.401  11.083  0.48 19.48 ?  9   TYR   A HE2  1 
ATOM   181  H HE2  B TYR   A 1 9   ? 14.061 -6.817  11.264  0.52 19.54 ?  9   TYR   A HE2  1 
ATOM   182  H HH   A TYR   A 1 9   ? 15.158 -5.420  13.604  0.48 21.36 ?  9   TYR   A HH   1 
ATOM   183  H HH   B TYR   A 1 9   ? 14.833 -4.725  13.757  0.52 21.19 ?  9   TYR   A HH   1 
ATOM   184  N N    A LEU   A 1 10  ? 8.825  -11.116 12.114  0.48 15.51 ?  10  LEU   A N    1 
ATOM   185  N N    B LEU   A 1 10  ? 8.745  -10.811 12.324  0.52 15.51 ?  10  LEU   A N    1 
ATOM   186  C CA   A LEU   A 1 10  ? 8.208  -12.346 11.644  0.48 15.14 ?  10  LEU   A CA   1 
ATOM   187  C CA   B LEU   A 1 10  ? 8.049  -11.993 11.845  0.52 15.42 ?  10  LEU   A CA   1 
ATOM   188  C C    A LEU   A 1 10  ? 9.303  -13.295 11.176  0.48 14.69 ?  10  LEU   A C    1 
ATOM   189  C C    B LEU   A 1 10  ? 9.072  -12.991 11.315  0.52 14.59 ?  10  LEU   A C    1 
ATOM   190  O O    A LEU   A 1 10  ? 10.264 -12.877 10.523  0.48 14.60 ?  10  LEU   A O    1 
ATOM   191  O O    B LEU   A 1 10  ? 9.966  -12.633 10.541  0.52 14.33 ?  10  LEU   A O    1 
ATOM   192  C CB   A LEU   A 1 10  ? 7.275  -12.037 10.475  0.48 16.29 ?  10  LEU   A CB   1 
ATOM   193  C CB   B LEU   A 1 10  ? 7.085  -11.585 10.732  0.52 16.32 ?  10  LEU   A CB   1 
ATOM   194  C CG   A LEU   A 1 10  ? 6.582  -13.208 9.781   0.48 18.39 ?  10  LEU   A CG   1 
ATOM   195  C CG   B LEU   A 1 10  ? 6.211  -12.688 10.152  0.52 18.54 ?  10  LEU   A CG   1 
ATOM   196  C CD1  A LEU   A 1 10  ? 5.508  -13.794 10.678  0.48 18.94 ?  10  LEU   A CD1  1 
ATOM   197  C CD1  B LEU   A 1 10  ? 5.290  -13.242 11.225  0.52 19.70 ?  10  LEU   A CD1  1 
ATOM   198  C CD2  A LEU   A 1 10  ? 5.998  -12.772 8.447   0.48 19.93 ?  10  LEU   A CD2  1 
ATOM   199  C CD2  B LEU   A 1 10  ? 5.408  -12.145 8.986   0.52 20.26 ?  10  LEU   A CD2  1 
ATOM   200  H H    A LEU   A 1 10  ? 8.968  -10.540 11.487  0.48 18.62 ?  10  LEU   A H    1 
ATOM   201  H H    B LEU   A 1 10  ? 8.781  -10.175 11.745  0.52 18.62 ?  10  LEU   A H    1 
ATOM   202  H HA   A LEU   A 1 10  ? 7.705  -12.761 12.365  0.48 18.18 ?  10  LEU   A HA   1 
ATOM   203  H HA   B LEU   A 1 10  ? 7.540  -12.399 12.569  0.52 18.52 ?  10  LEU   A HA   1 
ATOM   204  H HB2  A LEU   A 1 10  ? 6.578  -11.450 10.801  0.48 19.55 ?  10  LEU   A HB2  1 
ATOM   205  H HB2  B LEU   A 1 10  ? 6.484  -10.900 11.077  0.52 19.59 ?  10  LEU   A HB2  1 
ATOM   206  H HB3  A LEU   A 1 10  ? 7.793  -11.576 9.800   0.48 19.55 ?  10  LEU   A HB3  1 
ATOM   207  H HB3  B LEU   A 1 10  ? 7.601  -11.213 10.001  0.52 19.59 ?  10  LEU   A HB3  1 
ATOM   208  H HG   A LEU   A 1 10  ? 7.233  -13.907 9.607   0.48 22.08 ?  10  LEU   A HG   1 
ATOM   209  H HG   B LEU   A 1 10  ? 6.775  -13.407 9.826   0.52 22.25 ?  10  LEU   A HG   1 
ATOM   210  H HD11 A LEU   A 1 10  ? 5.149  -14.595 10.265  0.48 22.73 ?  10  LEU   A HD11 1 
ATOM   211  H HD11 B LEU   A 1 10  ? 4.656  -13.850 10.813  0.52 23.65 ?  10  LEU   A HD11 1 
ATOM   212  H HD12 A LEU   A 1 10  ? 5.895  -14.011 11.541  0.48 22.73 ?  10  LEU   A HD12 1 
ATOM   213  H HD12 B LEU   A 1 10  ? 5.821  -13.717 11.885  0.52 23.65 ?  10  LEU   A HD12 1 
ATOM   214  H HD13 A LEU   A 1 10  ? 4.800  -13.138 10.793  0.48 22.73 ?  10  LEU   A HD13 1 
ATOM   215  H HD13 B LEU   A 1 10  ? 4.817  -12.508 11.647  0.52 23.65 ?  10  LEU   A HD13 1 
ATOM   216  H HD21 A LEU   A 1 10  ? 5.561  -13.531 8.033   0.48 23.92 ?  10  LEU   A HD21 1 
ATOM   217  H HD21 B LEU   A 1 10  ? 4.857  -12.854 8.625   0.52 24.32 ?  10  LEU   A HD21 1 
ATOM   218  H HD22 A LEU   A 1 10  ? 5.358  -12.062 8.603   0.48 23.92 ?  10  LEU   A HD22 1 
ATOM   219  H HD22 B LEU   A 1 10  ? 4.847  -11.418 9.303   0.52 24.32 ?  10  LEU   A HD22 1 
ATOM   220  H HD23 A LEU   A 1 10  ? 6.718  -12.454 7.880   0.48 23.92 ?  10  LEU   A HD23 1 
ATOM   221  H HD23 B LEU   A 1 10  ? 6.018  -11.817 8.307   0.52 24.32 ?  10  LEU   A HD23 1 
ATOM   222  N N    A LYS   A 1 11  ? 9.156  -14.573 11.509  0.48 15.04 ?  11  LYS   A N    1 
ATOM   223  N N    B LYS   A 1 11  ? 8.950  -14.242 11.739  0.52 14.93 ?  11  LYS   A N    1 
ATOM   224  C CA   A LYS   A 1 11  ? 10.148 -15.583 11.165  0.48 15.11 ?  11  LYS   A CA   1 
ATOM   225  C CA   B LYS   A 1 11  ? 9.880  -15.280 11.318  0.52 14.57 ?  11  LYS   A CA   1 
ATOM   226  C C    A LYS   A 1 11  ? 9.786  -16.180 9.808   0.48 14.76 ?  11  LYS   A C    1 
ATOM   227  C C    B LYS   A 1 11  ? 9.520  -15.759 9.918   0.52 13.75 ?  11  LYS   A C    1 
ATOM   228  O O    A LYS   A 1 11  ? 8.699  -16.746 9.647   0.48 15.74 ?  11  LYS   A O    1 
ATOM   229  O O    B LYS   A 1 11  ? 8.404  -16.236 9.688   0.52 14.17 ?  11  LYS   A O    1 
ATOM   230  C CB   A LYS   A 1 11  ? 10.199 -16.647 12.264  0.48 14.94 ?  11  LYS   A CB   1 
ATOM   231  C CB   B LYS   A 1 11  ? 9.814  -16.447 12.295  0.52 15.19 ?  11  LYS   A CB   1 
ATOM   232  C CG   A LYS   A 1 11  ? 11.226 -17.754 12.083  0.48 15.08 ?  11  LYS   A CG   1 
ATOM   233  C CG   B LYS   A 1 11  ? 10.782 -17.563 11.988  0.52 15.50 ?  11  LYS   A CG   1 
ATOM   234  C CD   A LYS   A 1 11  ? 11.290 -18.613 13.345  0.48 14.64 ?  11  LYS   A CD   1 
ATOM   235  C CD   B LYS   A 1 11  ? 10.744 -18.613 13.083  0.52 16.33 ?  11  LYS   A CD   1 
ATOM   236  C CE   A LYS   A 1 11  ? 12.269 -19.768 13.214  0.48 14.83 ?  11  LYS   A CE   1 
ATOM   237  C CE   B LYS   A 1 11  ? 11.778 -19.696 12.855  0.52 16.68 ?  11  LYS   A CE   1 
ATOM   238  N NZ   A LYS   A 1 11  ? 13.656 -19.312 12.914  0.48 15.52 ?  11  LYS   A NZ   1 
ATOM   239  N NZ   B LYS   A 1 11  ? 13.164 -19.152 12.911  0.52 17.00 ?  11  LYS   A NZ   1 
ATOM   240  H H    A LYS   A 1 11  ? 8.471  -14.888 11.927  0.48 18.05 ?  11  LYS   A H    1 
ATOM   241  H H    B LYS   A 1 11  ? 8.331  -14.511 12.271  0.52 17.93 ?  11  LYS   A H    1 
ATOM   242  H HA   A LYS   A 1 11  ? 11.023 -15.169 11.096  0.48 18.14 ?  11  LYS   A HA   1 
ATOM   243  H HA   B LYS   A 1 11  ? 10.782 -14.918 11.303  0.52 17.49 ?  11  LYS   A HA   1 
ATOM   244  H HB2  A LYS   A 1 11  ? 10.403 -16.204 13.107  0.48 17.93 ?  11  LYS   A HB2  1 
ATOM   245  H HB2  B LYS   A 1 11  ? 10.007 -16.116 13.184  0.52 18.24 ?  11  LYS   A HB2  1 
ATOM   246  H HB3  A LYS   A 1 11  ? 9.330  -17.067 12.326  0.48 17.93 ?  11  LYS   A HB3  1 
ATOM   247  H HB3  B LYS   A 1 11  ? 8.922  -16.817 12.265  0.52 18.24 ?  11  LYS   A HB3  1 
ATOM   248  H HG2  A LYS   A 1 11  ? 10.968 -18.318 11.337  0.48 18.10 ?  11  LYS   A HG2  1 
ATOM   249  H HG2  B LYS   A 1 11  ? 10.537 -17.984 11.149  0.52 18.61 ?  11  LYS   A HG2  1 
ATOM   250  H HG3  A LYS   A 1 11  ? 12.103 -17.366 11.930  0.48 18.10 ?  11  LYS   A HG3  1 
ATOM   251  H HG3  B LYS   A 1 11  ? 11.683 -17.203 11.935  0.52 18.61 ?  11  LYS   A HG3  1 
ATOM   252  H HD2  A LYS   A 1 11  ? 11.571 -18.061 14.093  0.48 17.57 ?  11  LYS   A HD2  1 
ATOM   253  H HD2  B LYS   A 1 11  ? 10.931 -18.191 13.937  0.52 19.60 ?  11  LYS   A HD2  1 
ATOM   254  H HD3  A LYS   A 1 11  ? 10.407 -18.983 13.523  0.48 17.57 ?  11  LYS   A HD3  1 
ATOM   255  H HD3  B LYS   A 1 11  ? 9.867  -19.026 13.099  0.52 19.60 ?  11  LYS   A HD3  1 
ATOM   256  H HE2  A LYS   A 1 11  ? 12.289 -20.263 14.049  0.48 17.81 ?  11  LYS   A HE2  1 
ATOM   257  H HE2  B LYS   A 1 11  ? 11.688 -20.374 13.543  0.52 20.02 ?  11  LYS   A HE2  1 
ATOM   258  H HE3  A LYS   A 1 11  ? 11.979 -20.348 12.493  0.48 17.81 ?  11  LYS   A HE3  1 
ATOM   259  H HE3  B LYS   A 1 11  ? 11.639 -20.089 11.977  0.52 20.02 ?  11  LYS   A HE3  1 
ATOM   260  H HZ1  A LYS   A 1 11  ? 14.203 -20.013 12.864  0.48 18.63 ?  11  LYS   A HZ1  1 
ATOM   261  H HZ1  B LYS   A 1 11  ? 13.754 -19.812 12.821  0.52 20.41 ?  11  LYS   A HZ1  1 
ATOM   262  H HZ2  A LYS   A 1 11  ? 13.671 -18.878 12.136  0.48 18.63 ?  11  LYS   A HZ2  1 
ATOM   263  H HZ2  B LYS   A 1 11  ? 13.287 -18.563 12.253  0.52 20.41 ?  11  LYS   A HZ2  1 
ATOM   264  H HZ3  A LYS   A 1 11  ? 13.942 -18.766 13.555  0.48 18.63 ?  11  LYS   A HZ3  1 
ATOM   265  H HZ3  B LYS   A 1 11  ? 13.300 -18.746 13.691  0.52 20.41 ?  11  LYS   A HZ3  1 
ATOM   266  N N    A LEU   A 1 12  ? 10.686 -16.045 8.830   0.48 13.93 ?  12  LEU   A N    1 
ATOM   267  N N    B LEU   A 1 12  ? 10.458 -15.640 8.981   0.52 13.99 ?  12  LEU   A N    1 
ATOM   268  C CA   A LEU   A 1 12  ? 10.454 -16.595 7.496   0.48 13.84 ?  12  LEU   A CA   1 
ATOM   269  C CA   B LEU   A 1 12  ? 10.238 -16.168 7.640   0.52 14.01 ?  12  LEU   A CA   1 
ATOM   270  C C    A LEU   A 1 12  ? 11.068 -17.981 7.319   0.48 13.81 ?  12  LEU   A C    1 
ATOM   271  C C    B LEU   A 1 12  ? 10.804 -17.570 7.472   0.52 14.33 ?  12  LEU   A C    1 
ATOM   272  O O    A LEU   A 1 12  ? 10.448 -18.860 6.708   0.48 14.71 ?  12  LEU   A O    1 
ATOM   273  O O    B LEU   A 1 12  ? 10.149 -18.434 6.878   0.52 14.75 ?  12  LEU   A O    1 
ATOM   274  C CB   A LEU   A 1 12  ? 11.000 -15.652 6.418   0.48 13.98 ?  12  LEU   A CB   1 
ATOM   275  C CB   B LEU   A 1 12  ? 10.846 -15.238 6.591   0.52 14.36 ?  12  LEU   A CB   1 
ATOM   276  C CG   A LEU   A 1 12  ? 10.300 -14.303 6.206   0.48 14.58 ?  12  LEU   A CG   1 
ATOM   277  C CG   B LEU   A 1 12  ? 10.233 -13.845 6.547   0.52 15.03 ?  12  LEU   A CG   1 
ATOM   278  C CD1  A LEU   A 1 12  ? 11.026 -13.500 5.137   0.48 14.53 ?  12  LEU   A CD1  1 
ATOM   279  C CD1  B LEU   A 1 12  ? 10.919 -13.030 5.467   0.52 16.03 ?  12  LEU   A CD1  1 
ATOM   280  C CD2  A LEU   A 1 12  ? 8.831  -14.477 5.828   0.48 15.36 ?  12  LEU   A CD2  1 
ATOM   281  C CD2  B LEU   A 1 12  ? 8.727  -13.915 6.309   0.52 15.25 ?  12  LEU   A CD2  1 
ATOM   282  H H    A LEU   A 1 12  ? 11.436 -15.631 8.914   0.48 16.73 ?  12  LEU   A H    1 
ATOM   283  H H    B LEU   A 1 12  ? 11.212 -15.241 9.090   0.52 16.80 ?  12  LEU   A H    1 
ATOM   284  H HA   A LEU   A 1 12  ? 9.501  -16.681 7.359   0.48 16.62 ?  12  LEU   A HA   1 
ATOM   285  H HA   B LEU   A 1 12  ? 9.282  -16.211 7.473   0.52 16.81 ?  12  LEU   A HA   1 
ATOM   286  H HB2  A LEU   A 1 12  ? 11.926 -15.458 6.635   0.48 16.78 ?  12  LEU   A HB2  1 
ATOM   287  H HB2  B LEU   A 1 12  ? 11.794 -15.136 6.774   0.52 17.25 ?  12  LEU   A HB2  1 
ATOM   288  H HB3  A LEU   A 1 12  ? 10.968 -16.123 5.571   0.48 16.78 ?  12  LEU   A HB3  1 
ATOM   289  H HB3  B LEU   A 1 12  ? 10.725 -15.637 5.713   0.52 17.25 ?  12  LEU   A HB3  1 
ATOM   290  H HG   A LEU   A 1 12  ? 10.339 -13.799 7.032   0.48 17.50 ?  12  LEU   A HG   1 
ATOM   291  H HG   B LEU   A 1 12  ? 10.384 -13.406 7.401   0.52 18.04 ?  12  LEU   A HG   1 
ATOM   292  H HD11 A LEU   A 1 12  ? 10.571 -12.652 5.017   0.48 17.44 ?  12  LEU   A HD11 1 
ATOM   293  H HD11 B LEU   A 1 12  ? 10.527 -12.144 5.447   0.52 19.24 ?  12  LEU   A HD11 1 
ATOM   294  H HD12 A LEU   A 1 12  ? 11.941 -13.347 5.423   0.48 17.44 ?  12  LEU   A HD12 1 
ATOM   295  H HD12 B LEU   A 1 12  ? 11.864 -12.973 5.671   0.52 19.24 ?  12  LEU   A HD12 1 
ATOM   296  H HD13 A LEU   A 1 12  ? 11.019 -14.001 4.306   0.48 17.44 ?  12  LEU   A HD13 1 
ATOM   297  H HD13 B LEU   A 1 12  ? 10.788 -13.472 4.614   0.52 19.24 ?  12  LEU   A HD13 1 
ATOM   298  H HD21 A LEU   A 1 12  ? 8.448  -13.607 5.642   0.48 18.44 ?  12  LEU   A HD21 1 
ATOM   299  H HD21 B LEU   A 1 12  ? 8.405  -13.032 6.071   0.52 18.31 ?  12  LEU   A HD21 1 
ATOM   300  H HD22 A LEU   A 1 12  ? 8.773  -15.040 5.040   0.48 18.44 ?  12  LEU   A HD22 1 
ATOM   301  H HD22 B LEU   A 1 12  ? 8.551  -14.539 5.590   0.52 18.31 ?  12  LEU   A HD22 1 
ATOM   302  H HD23 A LEU   A 1 12  ? 8.362  -14.896 6.567   0.48 18.44 ?  12  LEU   A HD23 1 
ATOM   303  H HD23 B LEU   A 1 12  ? 8.291  -14.217 7.123   0.52 18.31 ?  12  LEU   A HD23 1 
ATOM   304  N N    A THR   A 1 13  ? 12.282 -18.185 7.823   0.48 13.70 ?  13  THR   A N    1 
ATOM   305  N N    B THR   A 1 13  ? 12.016 -17.798 7.973   0.52 14.16 ?  13  THR   A N    1 
ATOM   306  C CA   A THR   A 1 13  ? 12.965 -19.473 7.759   0.48 14.50 ?  13  THR   A CA   1 
ATOM   307  C CA   B THR   A 1 13  ? 12.689 -19.083 7.867   0.52 14.54 ?  13  THR   A CA   1 
ATOM   308  C C    A THR   A 1 13  ? 13.699 -19.680 9.075   0.48 14.87 ?  13  THR   A C    1 
ATOM   309  C C    B THR   A 1 13  ? 13.436 -19.344 9.169   0.52 15.03 ?  13  THR   A C    1 
ATOM   310  O O    A THR   A 1 13  ? 13.575 -18.888 10.014  0.48 14.92 ?  13  THR   A O    1 
ATOM   311  O O    B THR   A 1 13  ? 13.311 -18.605 10.151  0.52 15.58 ?  13  THR   A O    1 
ATOM   312  C CB   A THR   A 1 13  ? 13.941 -19.554 6.573   0.48 15.41 ?  13  THR   A CB   1 
ATOM   313  C CB   B THR   A 1 13  ? 13.690 -19.093 6.705   0.52 14.16 ?  13  THR   A CB   1 
ATOM   314  O OG1  A THR   A 1 13  ? 15.022 -18.635 6.769   0.48 15.91 ?  13  THR   A OG1  1 
ATOM   315  O OG1  B THR   A 1 13  ? 14.745 -18.171 6.996   0.52 14.33 ?  13  THR   A OG1  1 
ATOM   316  C CG2  A THR   A 1 13  ? 13.250 -19.227 5.272   0.48 16.48 ?  13  THR   A CG2  1 
ATOM   317  C CG2  B THR   A 1 13  ? 13.033 -18.731 5.377   0.52 14.51 ?  13  THR   A CG2  1 
ATOM   318  H H    A THR   A 1 13  ? 12.744 -17.580 8.219   0.48 16.45 ?  13  THR   A H    1 
ATOM   319  H H    B THR   A 1 13  ? 12.477 -17.196 8.381   0.52 17.00 ?  13  THR   A H    1 
ATOM   320  H HA   A THR   A 1 13  ? 12.315 -20.187 7.667   0.48 17.41 ?  13  THR   A HA   1 
ATOM   321  H HA   B THR   A 1 13  ? 12.031 -19.781 7.722   0.52 17.46 ?  13  THR   A HA   1 
ATOM   322  H HB   A THR   A 1 13  ? 14.297 -20.459 6.510   0.48 18.50 ?  13  THR   A HB   1 
ATOM   323  H HB   B THR   A 1 13  ? 14.069 -19.976 6.620   0.52 17.00 ?  13  THR   A HB   1 
ATOM   324  H HG1  A THR   A 1 13  ? 15.560 -18.681 6.120   0.48 19.10 ?  13  THR   A HG1  1 
ATOM   325  H HG1  B THR   A 1 13  ? 15.301 -18.151 6.366   0.52 17.21 ?  13  THR   A HG1  1 
ATOM   326  H HG21 A THR   A 1 13  ? 13.812 -19.488 4.527   0.48 19.78 ?  13  THR   A HG21 1 
ATOM   327  H HG21 B THR   A 1 13  ? 13.657 -18.888 4.650   0.52 17.42 ?  13  THR   A HG21 1 
ATOM   328  H HG22 A THR   A 1 13  ? 12.411 -19.708 5.217   0.48 19.78 ?  13  THR   A HG22 1 
ATOM   329  H HG22 B THR   A 1 13  ? 12.248 -19.288 5.237   0.52 17.42 ?  13  THR   A HG22 1 
ATOM   330  H HG23 A THR   A 1 13  ? 13.075 -18.277 5.223   0.48 19.78 ?  13  THR   A HG23 1 
ATOM   331  H HG23 B THR   A 1 13  ? 12.766 -17.802 5.373   0.52 17.42 ?  13  THR   A HG23 1 
ATOM   332  N N    A ASP   A 1 14  ? 14.492 -20.751 9.132   0.48 15.56 ?  14  ASP   A N    1 
ATOM   333  N N    B ASP   A 1 14  ? 14.251 -20.399 9.143   0.52 15.84 ?  14  ASP   A N    1 
ATOM   334  C CA   A ASP   A 1 14  ? 15.305 -21.001 10.312  0.48 16.33 ?  14  ASP   A CA   1 
ATOM   335  C CA   B ASP   A 1 14  ? 15.101 -20.747 10.273  0.52 17.23 ?  14  ASP   A CA   1 
ATOM   336  C C    A ASP   A 1 14  ? 16.214 -19.823 10.633  0.48 15.70 ?  14  ASP   A C    1 
ATOM   337  C C    B ASP   A 1 14  ? 15.893 -19.544 10.780  0.52 16.46 ?  14  ASP   A C    1 
ATOM   338  O O    A ASP   A 1 14  ? 16.528 -19.596 11.806  0.48 15.67 ?  14  ASP   A O    1 
ATOM   339  O O    B ASP   A 1 14  ? 16.002 -19.331 11.993  0.52 16.71 ?  14  ASP   A O    1 
ATOM   340  C CB   A ASP   A 1 14  ? 16.152 -22.252 10.107  0.48 18.20 ?  14  ASP   A CB   1 
ATOM   341  C CB   B ASP   A 1 14  ? 16.050 -21.871 9.843   0.52 19.77 ?  14  ASP   A CB   1 
ATOM   342  C CG   A ASP   A 1 14  ? 17.153 -22.454 11.212  0.48 20.80 ?  14  ASP   A CG   1 
ATOM   343  C CG   B ASP   A 1 14  ? 16.924 -22.371 10.987  0.52 23.42 ?  14  ASP   A CG   1 
ATOM   344  O OD1  A ASP   A 1 14  ? 16.734 -22.881 12.306  0.48 21.60 ?  14  ASP   A OD1  1 
ATOM   345  O OD1  B ASP   A 1 14  ? 16.613 -22.069 12.161  0.52 24.85 ?  14  ASP   A OD1  1 
ATOM   346  O OD2  A ASP   A 1 14  ? 18.344 -22.168 10.986  0.48 21.70 -1 14  ASP   A OD2  1 
ATOM   347  O OD2  B ASP   A 1 14  ? 17.925 -23.065 10.715  0.52 24.76 -1 14  ASP   A OD2  1 
ATOM   348  H H    A ASP   A 1 14  ? 14.582 -21.340 8.513   0.48 18.68 ?  14  ASP   A H    1 
ATOM   349  H H    B ASP   A 1 14  ? 14.319 -20.928 8.478   0.52 19.02 ?  14  ASP   A H    1 
ATOM   350  H HA   A ASP   A 1 14  ? 14.735 -21.156 11.080  0.48 19.61 ?  14  ASP   A HA   1 
ATOM   351  H HA   B ASP   A 1 14  ? 14.553 -21.071 11.002  0.52 20.69 ?  14  ASP   A HA   1 
ATOM   352  H HB2  A ASP   A 1 14  ? 15.577 -23.037 10.097  0.48 21.84 ?  14  ASP   A HB2  1 
ATOM   353  H HB2  B ASP   A 1 14  ? 15.514 -22.611 9.499   0.52 23.73 ?  14  ASP   A HB2  1 
ATOM   354  H HB3  A ASP   A 1 14  ? 16.640 -22.188 9.276   0.48 21.84 ?  14  ASP   A HB3  1 
ATOM   355  H HB3  B ASP   A 1 14  ? 16.625 -21.538 9.128   0.52 23.73 ?  14  ASP   A HB3  1 
ATOM   356  N N    A ASN   A 1 15  ? 16.646 -19.061 9.616   0.48 14.71 ?  15  ASN   A N    1 
ATOM   357  N N    B ASN   A 1 15  ? 16.435 -18.729 9.869   0.52 14.87 ?  15  ASN   A N    1 
ATOM   358  C CA   A ASN   A 1 15  ? 17.644 -18.015 9.820   0.48 14.06 ?  15  ASN   A CA   1 
ATOM   359  C CA   B ASN   A 1 15  ? 17.399 -17.704 10.247  0.52 14.12 ?  15  ASN   A CA   1 
ATOM   360  C C    A ASN   A 1 15  ? 17.275 -16.634 9.284   0.48 13.81 ?  15  ASN   A C    1 
ATOM   361  C C    B ASN   A 1 15  ? 17.059 -16.299 9.770   0.52 13.73 ?  15  ASN   A C    1 
ATOM   362  O O    A ASN   A 1 15  ? 18.076 -15.708 9.447   0.48 14.07 ?  15  ASN   A O    1 
ATOM   363  O O    B ASN   A 1 15  ? 17.826 -15.376 10.060  0.52 13.92 ?  15  ASN   A O    1 
ATOM   364  C CB   A ASN   A 1 15  ? 19.001 -18.440 9.228   0.48 13.59 ?  15  ASN   A CB   1 
ATOM   365  C CB   B ASN   A 1 15  ? 18.800 -18.069 9.731   0.52 14.26 ?  15  ASN   A CB   1 
ATOM   366  C CG   A ASN   A 1 15  ? 18.979 -18.514 7.711   0.48 14.12 ?  15  ASN   A CG   1 
ATOM   367  C CG   B ASN   A 1 15  ? 18.833 -18.259 8.231   0.52 14.85 ?  15  ASN   A CG   1 
ATOM   368  O OD1  A ASN   A 1 15  ? 18.296 -19.356 7.126   0.48 14.51 ?  15  ASN   A OD1  1 
ATOM   369  O OD1  B ASN   A 1 15  ? 18.037 -19.015 7.669   0.52 14.87 ?  15  ASN   A OD1  1 
ATOM   370  N ND2  A ASN   A 1 15  ? 19.737 -17.637 7.066   0.48 14.20 ?  15  ASN   A ND2  1 
ATOM   371  N ND2  B ASN   A 1 15  ? 19.736 -17.546 7.568   0.52 15.53 ?  15  ASN   A ND2  1 
ATOM   372  H H    A ASN   A 1 15  ? 16.386 -19.152 8.803   0.48 17.66 ?  15  ASN   A H    1 
ATOM   373  H H    B ASN   A 1 15  ? 16.249 -18.742 9.031   0.52 17.85 ?  15  ASN   A H    1 
ATOM   374  H HA   A ASN   A 1 15  ? 17.786 -17.928 10.771  0.48 16.88 ?  15  ASN   A HA   1 
ATOM   375  H HA   B ASN   A 1 15  ? 17.449 -17.663 11.215  0.52 16.95 ?  15  ASN   A HA   1 
ATOM   376  H HB2  A ASN   A 1 15  ? 19.680 -17.790 9.490   0.48 16.32 ?  15  ASN   A HB2  1 
ATOM   377  H HB2  B ASN   A 1 15  ? 19.416 -17.351 9.961   0.52 17.12 ?  15  ASN   A HB2  1 
ATOM   378  H HB3  A ASN   A 1 15  ? 19.251 -19.318 9.576   0.48 16.32 ?  15  ASN   A HB3  1 
ATOM   379  H HB3  B ASN   A 1 15  ? 19.078 -18.893 10.147  0.52 17.12 ?  15  ASN   A HB3  1 
ATOM   380  H HD21 A ASN   A 1 15  ? 19.769 -17.648 6.207   0.48 17.05 ?  15  ASN   A HD21 1 
ATOM   381  H HD21 B ASN   A 1 15  ? 19.800 -17.616 6.713   0.52 18.64 ?  15  ASN   A HD21 1 
ATOM   382  H HD22 A ASN   A 1 15  ? 20.209 -17.063 7.505   0.48 17.05 ?  15  ASN   A HD22 1 
ATOM   383  H HD22 B ASN   A 1 15  ? 20.279 -17.028 7.995   0.52 18.64 ?  15  ASN   A HD22 1 
ATOM   384  N N    A VAL   A 1 16  ? 16.107 -16.456 8.666   0.48 13.47 ?  16  VAL   A N    1 
ATOM   385  N N    B VAL   A 1 16  ? 15.945 -16.099 9.070   0.52 13.10 ?  16  VAL   A N    1 
ATOM   386  C CA   A VAL   A 1 16  ? 15.721 -15.181 8.068   0.48 13.39 ?  16  VAL   A CA   1 
ATOM   387  C CA   B VAL   A 1 16  ? 15.594 -14.800 8.508   0.52 13.16 ?  16  VAL   A CA   1 
ATOM   388  C C    A VAL   A 1 16  ? 14.447 -14.661 8.729   0.48 12.48 ?  16  VAL   A C    1 
ATOM   389  C C    B VAL   A 1 16  ? 14.294 -14.317 9.138   0.52 13.53 ?  16  VAL   A C    1 
ATOM   390  O O    A VAL   A 1 16  ? 13.433 -15.371 8.795   0.48 12.05 ?  16  VAL   A O    1 
ATOM   391  O O    B VAL   A 1 16  ? 13.301 -15.057 9.183   0.52 13.28 ?  16  VAL   A O    1 
ATOM   392  C CB   A VAL   A 1 16  ? 15.551 -15.289 6.542   0.48 14.29 ?  16  VAL   A CB   1 
ATOM   393  C CB   B VAL   A 1 16  ? 15.502 -14.844 6.971   0.52 13.34 ?  16  VAL   A CB   1 
ATOM   394  C CG1  A VAL   A 1 16  ? 15.100 -13.951 5.974   0.48 15.00 ?  16  VAL   A CG1  1 
ATOM   395  C CG1  B VAL   A 1 16  ? 15.161 -13.457 6.413   0.52 13.49 ?  16  VAL   A CG1  1 
ATOM   396  C CG2  A VAL   A 1 16  ? 16.848 -15.755 5.879   0.48 15.27 ?  16  VAL   A CG2  1 
ATOM   397  C CG2  B VAL   A 1 16  ? 16.794 -15.381 6.362   0.52 14.24 ?  16  VAL   A CG2  1 
ATOM   398  H H    A VAL   A 1 16  ? 15.523 -17.085 8.574   0.48 16.18 ?  16  VAL   A H    1 
ATOM   399  H H    B VAL   A 1 16  ? 15.357 -16.705 8.918   0.52 15.72 ?  16  VAL   A H    1 
ATOM   400  H HA   A VAL   A 1 16  ? 16.427 -14.544 8.243   0.48 16.07 ?  16  VAL   A HA   1 
ATOM   401  H HA   B VAL   A 1 16  ? 16.276 -14.154 8.737   0.52 15.80 ?  16  VAL   A HA   1 
ATOM   402  H HB   A VAL   A 1 16  ? 14.864 -15.948 6.352   0.48 17.16 ?  16  VAL   A HB   1 
ATOM   403  H HB   B VAL   A 1 16  ? 14.788 -15.446 6.718   0.52 16.02 ?  16  VAL   A HB   1 
ATOM   404  H HG11 A VAL   A 1 16  ? 15.183 -13.979 5.011   0.48 18.01 ?  16  VAL   A HG11 1 
ATOM   405  H HG11 B VAL   A 1 16  ? 15.263 -13.468 5.447   0.52 16.19 ?  16  VAL   A HG11 1 
ATOM   406  H HG12 A VAL   A 1 16  ? 14.176 -13.797 6.224   0.48 18.01 ?  16  VAL   A HG12 1 
ATOM   407  H HG12 B VAL   A 1 16  ? 14.244 -13.239 6.640   0.52 16.19 ?  16  VAL   A HG12 1 
ATOM   408  H HG13 A VAL   A 1 16  ? 15.665 -13.252 6.337   0.48 18.01 ?  16  VAL   A HG13 1 
ATOM   409  H HG13 B VAL   A 1 16  ? 15.763 -12.801 6.798   0.52 16.19 ?  16  VAL   A HG13 1 
ATOM   410  H HG21 A VAL   A 1 16  ? 16.798 -15.562 4.931   0.48 18.33 ?  16  VAL   A HG21 1 
ATOM   411  H HG21 B VAL   A 1 16  ? 16.965 -14.930 5.523   0.52 17.09 ?  16  VAL   A HG21 1 
ATOM   412  H HG22 A VAL   A 1 16  ? 17.593 -15.277 6.275   0.48 18.33 ?  16  VAL   A HG22 1 
ATOM   413  H HG22 B VAL   A 1 16  ? 17.518 -15.235 6.981   0.52 17.09 ?  16  VAL   A HG22 1 
ATOM   414  H HG23 A VAL   A 1 16  ? 16.953 -16.709 6.021   0.48 18.33 ?  16  VAL   A HG23 1 
ATOM   415  H HG23 B VAL   A 1 16  ? 16.685 -16.338 6.206   0.52 17.09 ?  16  VAL   A HG23 1 
ATOM   416  N N    A TYR   A 1 17  ? 14.500 -13.403 9.179   0.48 12.16 ?  17  TYR   A N    1 
ATOM   417  N N    B TYR   A 1 17  ? 14.317 -13.074 9.625   0.52 13.61 ?  17  TYR   A N    1 
ATOM   418  C CA   A TYR   A 1 17  ? 13.422 -12.714 9.877   0.48 12.14 ?  17  TYR   A CA   1 
ATOM   419  C CA   B TYR   A 1 17  ? 13.201 -12.404 10.275  0.52 13.92 ?  17  TYR   A CA   1 
ATOM   420  C C    A TYR   A 1 17  ? 13.151 -11.398 9.160   0.48 12.58 ?  17  TYR   A C    1 
ATOM   421  C C    B TYR   A 1 17  ? 12.984 -11.057 9.604   0.52 12.99 ?  17  TYR   A C    1 
ATOM   422  O O    A TYR   A 1 17  ? 14.043 -10.847 8.508   0.48 12.39 ?  17  TYR   A O    1 
ATOM   423  O O    B TYR   A 1 17  ? 13.930 -10.471 9.073   0.52 13.03 ?  17  TYR   A O    1 
ATOM   424  C CB   A TYR   A 1 17  ? 13.832 -12.421 11.336  0.48 12.84 ?  17  TYR   A CB   1 
ATOM   425  C CB   B TYR   A 1 17  ? 13.520 -12.174 11.750  0.52 15.82 ?  17  TYR   A CB   1 
ATOM   426  C CG   A TYR   A 1 17  ? 14.002 -13.666 12.177  0.48 13.28 ?  17  TYR   A CG   1 
ATOM   427  C CG   B TYR   A 1 17  ? 13.435 -13.442 12.560  0.52 18.19 ?  17  TYR   A CG   1 
ATOM   428  C CD1  A TYR   A 1 17  ? 15.180 -14.404 12.139  0.48 14.56 ?  17  TYR   A CD1  1 
ATOM   429  C CD1  B TYR   A 1 17  ? 14.419 -14.413 12.472  0.52 20.10 ?  17  TYR   A CD1  1 
ATOM   430  C CD2  A TYR   A 1 17  ? 12.970 -14.123 12.995  0.48 13.65 ?  17  TYR   A CD2  1 
ATOM   431  C CD2  B TYR   A 1 17  ? 12.351 -13.678 13.390  0.52 19.03 ?  17  TYR   A CD2  1 
ATOM   432  C CE1  A TYR   A 1 17  ? 15.324 -15.563 12.899  0.48 14.52 ?  17  TYR   A CE1  1 
ATOM   433  C CE1  B TYR   A 1 17  ? 14.331 -15.587 13.201  0.52 21.01 ?  17  TYR   A CE1  1 
ATOM   434  C CE2  A TYR   A 1 17  ? 13.104 -15.277 13.755  0.48 14.60 ?  17  TYR   A CE2  1 
ATOM   435  C CE2  B TYR   A 1 17  ? 12.255 -14.840 14.125  0.52 20.05 ?  17  TYR   A CE2  1 
ATOM   436  C CZ   A TYR   A 1 17  ? 14.280 -15.997 13.708  0.48 14.33 ?  17  TYR   A CZ   1 
ATOM   437  C CZ   B TYR   A 1 17  ? 13.246 -15.795 14.028  0.52 20.51 ?  17  TYR   A CZ   1 
ATOM   438  O OH   A TYR   A 1 17  ? 14.411 -17.145 14.464  0.48 15.29 ?  17  TYR   A OH   1 
ATOM   439  O OH   B TYR   A 1 17  ? 13.151 -16.962 14.758  0.52 21.28 ?  17  TYR   A OH   1 
ATOM   440  H H    A TYR   A 1 17  ? 15.196 -12.909 9.073   0.48 14.60 ?  17  TYR   A H    1 
ATOM   441  H H    B TYR   A 1 17  ? 15.014 -12.571 9.586   0.52 16.34 ?  17  TYR   A H    1 
ATOM   442  H HA   A TYR   A 1 17  ? 12.621 -13.264 9.874   0.48 14.58 ?  17  TYR   A HA   1 
ATOM   443  H HA   B TYR   A 1 17  ? 12.389 -12.919 10.189  0.52 16.71 ?  17  TYR   A HA   1 
ATOM   444  H HB2  A TYR   A 1 17  ? 14.681 -11.950 11.333  0.48 15.42 ?  17  TYR   A HB2  1 
ATOM   445  H HB2  B TYR   A 1 17  ? 14.415 -11.808 11.825  0.52 18.99 ?  17  TYR   A HB2  1 
ATOM   446  H HB3  A TYR   A 1 17  ? 13.150 -11.875 11.746  0.48 15.42 ?  17  TYR   A HB3  1 
ATOM   447  H HB3  B TYR   A 1 17  ? 12.886 -11.538 12.106  0.52 18.99 ?  17  TYR   A HB3  1 
ATOM   448  H HD1  A TYR   A 1 17  ? 15.882 -14.128 11.596  0.48 17.48 ?  17  TYR   A HD1  1 
ATOM   449  H HD1  B TYR   A 1 17  ? 15.151 -14.270 11.908  0.52 24.13 ?  17  TYR   A HD1  1 
ATOM   450  H HD2  A TYR   A 1 17  ? 12.173 -13.640 13.029  0.48 16.39 ?  17  TYR   A HD2  1 
ATOM   451  H HD2  B TYR   A 1 17  ? 11.680 -13.031 13.453  0.52 22.84 ?  17  TYR   A HD2  1 
ATOM   452  H HE1  A TYR   A 1 17  ? 16.116 -16.050 12.870  0.48 17.43 ?  17  TYR   A HE1  1 
ATOM   453  H HE1  B TYR   A 1 17  ? 14.999 -16.227 13.134  0.52 25.22 ?  17  TYR   A HE1  1 
ATOM   454  H HE2  A TYR   A 1 17  ? 12.402 -15.551 14.297  0.48 17.53 ?  17  TYR   A HE2  1 
ATOM   455  H HE2  B TYR   A 1 17  ? 11.524 -14.979 14.677  0.52 24.06 ?  17  TYR   A HE2  1 
ATOM   456  H HH   A TYR   A 1 17  ? 15.182 -17.453 14.365  0.48 18.36 ?  17  TYR   A HH   1 
ATOM   457  H HH   B TYR   A 1 17  ? 12.447 -16.948 15.212  0.52 25.55 ?  17  TYR   A HH   1 
ATOM   458  N N    A ILE   A 1 18  ? 11.926 -10.877 9.283   0.48 13.43 ?  18  ILE   A N    1 
ATOM   459  N N    B ILE   A 1 18  ? 11.749 -10.545 9.643   0.52 12.22 ?  18  ILE   A N    1 
ATOM   460  C CA   A ILE   A 1 18  ? 11.553 -9.658  8.569   0.48 14.21 ?  18  ILE   A CA   1 
ATOM   461  C CA   B ILE   A 1 18  ? 11.390 -9.359  8.868   0.52 12.75 ?  18  ILE   A CA   1 
ATOM   462  C C    A ILE   A 1 18  ? 10.596 -8.818  9.413   0.48 15.18 ?  18  ILE   A C    1 
ATOM   463  C C    B ILE   A 1 18  ? 10.473 -8.452  9.679   0.52 13.01 ?  18  ILE   A C    1 
ATOM   464  O O    A ILE   A 1 18  ? 9.801  -9.347  10.193  0.48 15.47 ?  18  ILE   A O    1 
ATOM   465  O O    B ILE   A 1 18  ? 9.628  -8.922  10.447  0.52 13.49 ?  18  ILE   A O    1 
ATOM   466  C CB   A ILE   A 1 18  ? 10.981 -10.004 7.174   0.48 13.61 ?  18  ILE   A CB   1 
ATOM   467  C CB   B ILE   A 1 18  ? 10.787 -9.734  7.496   0.52 13.01 ?  18  ILE   A CB   1 
ATOM   468  C CG1  A ILE   A 1 18  ? 10.912 -8.755  6.299   0.48 14.06 ?  18  ILE   A CG1  1 
ATOM   469  C CG1  B ILE   A 1 18  ? 10.721 -8.504  6.584   0.52 14.50 ?  18  ILE   A CG1  1 
ATOM   470  C CG2  A ILE   A 1 18  ? 9.633  -10.721 7.302   0.48 13.30 ?  18  ILE   A CG2  1 
ATOM   471  C CG2  B ILE   A 1 18  ? 9.409  -10.363 7.659   0.52 13.84 ?  18  ILE   A CG2  1 
ATOM   472  C CD1  A ILE   A 1 18  ? 10.721 -9.061  4.837   0.48 16.01 ?  18  ILE   A CD1  1 
ATOM   473  C CD1  B ILE   A 1 18  ? 10.508 -8.841  5.122   0.52 16.20 ?  18  ILE   A CD1  1 
ATOM   474  H H    A ILE   A 1 18  ? 11.307 -11.221 9.766   0.48 16.13 ?  18  ILE   A H    1 
ATOM   475  H H    B ILE   A 1 18  ? 11.103 -10.854 10.122  0.52 14.68 ?  18  ILE   A H    1 
ATOM   476  H HA   A ILE   A 1 18  ? 12.360 -9.136  8.431   0.48 17.06 ?  18  ILE   A HA   1 
ATOM   477  H HA   B ILE   A 1 18  ? 12.192 -8.850  8.691   0.52 15.31 ?  18  ILE   A HA   1 
ATOM   478  H HB   A ILE   A 1 18  ? 11.600 -10.624 6.753   0.48 16.34 ?  18  ILE   A HB   1 
ATOM   479  H HB   B ILE   A 1 18  ? 11.370 -10.383 7.082   0.52 15.62 ?  18  ILE   A HB   1 
ATOM   480  H HG12 A ILE   A 1 18  ? 10.171 -8.209  6.592   0.48 16.88 ?  18  ILE   A HG12 1 
ATOM   481  H HG12 B ILE   A 1 18  ? 9.983  -7.939  6.863   0.52 17.40 ?  18  ILE   A HG12 1 
ATOM   482  H HG13 A ILE   A 1 18  ? 11.745 -8.264  6.391   0.48 16.88 ?  18  ILE   A HG13 1 
ATOM   483  H HG13 B ILE   A 1 18  ? 11.554 -8.013  6.653   0.52 17.40 ?  18  ILE   A HG13 1 
ATOM   484  H HG21 A ILE   A 1 18  ? 9.366  -11.042 6.426   0.48 15.97 ?  18  ILE   A HG21 1 
ATOM   485  H HG21 B ILE   A 1 18  ? 9.127  -10.729 6.804   0.52 16.62 ?  18  ILE   A HG21 1 
ATOM   486  H HG22 A ILE   A 1 18  ? 9.729  -11.470 7.912   0.48 15.97 ?  18  ILE   A HG22 1 
ATOM   487  H HG22 B ILE   A 1 18  ? 9.462  -11.070 8.319   0.52 16.62 ?  18  ILE   A HG22 1 
ATOM   488  H HG23 A ILE   A 1 18  ? 8.974  -10.098 7.642   0.48 15.97 ?  18  ILE   A HG23 1 
ATOM   489  H HG23 B ILE   A 1 18  ? 8.778  -9.685  7.949   0.52 16.62 ?  18  ILE   A HG23 1 
ATOM   490  H HD11 A ILE   A 1 18  ? 10.709 -8.225  4.342   0.48 19.22 ?  18  ILE   A HD11 1 
ATOM   491  H HD11 B ILE   A 1 18  ? 10.497 -8.019  4.603   0.52 19.44 ?  18  ILE   A HD11 1 
ATOM   492  H HD12 A ILE   A 1 18  ? 11.452 -9.617  4.529   0.48 19.22 ?  18  ILE   A HD12 1 
ATOM   493  H HD12 B ILE   A 1 18  ? 11.238 -9.408  4.818   0.52 19.44 ?  18  ILE   A HD12 1 
ATOM   494  H HD13 A ILE   A 1 18  ? 9.877  -9.525  4.721   0.48 19.22 ?  18  ILE   A HD13 1 
ATOM   495  H HD13 B ILE   A 1 18  ? 9.665  -9.307  5.020   0.52 19.44 ?  18  ILE   A HD13 1 
ATOM   496  N N    A LYS   A 1 19  ? 10.676 -7.493  9.234   0.48 15.59 ?  19  LYS   A N    1 
ATOM   497  N N    B LYS   A 1 19  ? 10.648 -7.141  9.500   0.52 13.41 ?  19  LYS   A N    1 
ATOM   498  C CA   A LYS   A 1 19  ? 9.890  -6.527  10.000  0.48 16.34 ?  19  LYS   A CA   1 
ATOM   499  C CA   B LYS   A 1 19  ? 9.847  -6.151  10.204  0.52 14.41 ?  19  LYS   A CA   1 
ATOM   500  C C    A LYS   A 1 19  ? 9.683  -5.266  9.169   0.48 16.55 ?  19  LYS   A C    1 
ATOM   501  C C    B LYS   A 1 19  ? 9.644  -4.940  9.307   0.52 14.75 ?  19  LYS   A C    1 
ATOM   502  O O    A LYS   A 1 19  ? 10.528 -4.912  8.343   0.48 15.95 ?  19  LYS   A O    1 
ATOM   503  O O    B LYS   A 1 19  ? 10.558 -4.545  8.580   0.52 14.66 ?  19  LYS   A O    1 
ATOM   504  C CB   A LYS   A 1 19  ? 10.621 -6.177  11.307  0.48 17.12 ?  19  LYS   A CB   1 
ATOM   505  C CB   B LYS   A 1 19  ? 10.551 -5.731  11.498  0.52 15.62 ?  19  LYS   A CB   1 
ATOM   506  C CG   A LYS   A 1 19  ? 9.943  -5.180  12.249  0.48 17.93 ?  19  LYS   A CG   1 
ATOM   507  C CG   B LYS   A 1 19  ? 9.723  -4.877  12.424  0.52 17.53 ?  19  LYS   A CG   1 
ATOM   508  C CD   A LYS   A 1 19  ? 10.845 -4.937  13.469  0.48 18.80 ?  19  LYS   A CD   1 
ATOM   509  C CD   B LYS   A 1 19  ? 10.523 -4.558  13.666  0.52 19.01 ?  19  LYS   A CD   1 
ATOM   510  C CE   A LYS   A 1 19  ? 10.238 -3.987  14.498  0.48 19.51 ?  19  LYS   A CE   1 
ATOM   511  C CE   B LYS   A 1 19  ? 9.773  -3.626  14.589  0.52 19.96 ?  19  LYS   A CE   1 
ATOM   512  N NZ   A LYS   A 1 19  ? 11.138 -3.803  15.682  0.48 19.46 ?  19  LYS   A NZ   1 
ATOM   513  N NZ   B LYS   A 1 19  ? 10.616 -3.249  15.753  0.52 20.59 ?  19  LYS   A NZ   1 
ATOM   514  H H    A LYS   A 1 19  ? 11.198 -7.123  8.656   0.48 18.72 ?  19  LYS   A H    1 
ATOM   515  H H    B LYS   A 1 19  ? 11.239 -6.780  8.971   0.52 16.11 ?  19  LYS   A H    1 
ATOM   516  H HA   A LYS   A 1 19  ? 9.026  -6.904  10.210  0.48 19.62 ?  19  LYS   A HA   1 
ATOM   517  H HA   B LYS   A 1 19  ? 8.980  -6.515  10.429  0.52 17.30 ?  19  LYS   A HA   1 
ATOM   518  H HB2  A LYS   A 1 19  ? 10.739 -6.996  11.808  0.48 20.55 ?  19  LYS   A HB2  1 
ATOM   519  H HB2  B LYS   A 1 19  ? 10.795 -6.532  11.992  0.52 18.76 ?  19  LYS   A HB2  1 
ATOM   520  H HB3  A LYS   A 1 19  ? 11.486 -5.807  11.082  0.48 20.55 ?  19  LYS   A HB3  1 
ATOM   521  H HB3  B LYS   A 1 19  ? 11.351 -5.229  11.277  0.52 18.76 ?  19  LYS   A HB3  1 
ATOM   522  H HG2  A LYS   A 1 19  ? 9.804  -4.333  11.796  0.48 21.52 ?  19  LYS   A HG2  1 
ATOM   523  H HG2  B LYS   A 1 19  ? 9.492  -4.046  11.982  0.52 21.04 ?  19  LYS   A HG2  1 
ATOM   524  H HG3  A LYS   A 1 19  ? 9.096  -5.540  12.562  0.48 21.52 ?  19  LYS   A HG3  1 
ATOM   525  H HG3  B LYS   A 1 19  ? 8.924  -5.361  12.686  0.52 21.04 ?  19  LYS   A HG3  1 
ATOM   526  H HD2  A LYS   A 1 19  ? 11.011 -5.782  13.912  0.48 22.57 ?  19  LYS   A HD2  1 
ATOM   527  H HD2  B LYS   A 1 19  ? 10.709 -5.384  14.143  0.52 22.81 ?  19  LYS   A HD2  1 
ATOM   528  H HD3  A LYS   A 1 19  ? 11.681 -4.549  13.169  0.48 22.57 ?  19  LYS   A HD3  1 
ATOM   529  H HD3  B LYS   A 1 19  ? 11.356 -4.132  13.403  0.52 22.81 ?  19  LYS   A HD3  1 
ATOM   530  H HE2  A LYS   A 1 19  ? 10.097 -3.117  14.092  0.48 23.42 ?  19  LYS   A HE2  1 
ATOM   531  H HE2  B LYS   A 1 19  ? 9.538  -2.820  14.104  0.52 23.96 ?  19  LYS   A HE2  1 
ATOM   532  H HE3  A LYS   A 1 19  ? 9.397  -4.349  14.816  0.48 23.42 ?  19  LYS   A HE3  1 
ATOM   533  H HE3  B LYS   A 1 19  ? 8.977  -4.072  14.913  0.52 23.96 ?  19  LYS   A HE3  1 
ATOM   534  H HZ1  A LYS   A 1 19  ? 10.772 -3.229  16.257  0.48 23.35 ?  19  LYS   A HZ1  1 
ATOM   535  H HZ1  B LYS   A 1 19  ? 10.161 -2.708  16.292  0.52 24.72 ?  19  LYS   A HZ1  1 
ATOM   536  H HZ2  A LYS   A 1 19  ? 11.263 -4.582  16.093  0.48 23.35 ?  19  LYS   A HZ2  1 
ATOM   537  H HZ2  B LYS   A 1 19  ? 10.852 -3.979  16.205  0.52 24.72 ?  19  LYS   A HZ2  1 
ATOM   538  H HZ3  A LYS   A 1 19  ? 11.925 -3.484  15.420  0.48 23.35 ?  19  LYS   A HZ3  1 
ATOM   539  H HZ3  B LYS   A 1 19  ? 11.351 -2.831  15.474  0.52 24.72 ?  19  LYS   A HZ3  1 
ATOM   540  N N    A ASN   A 1 20  ? 8.549  -4.588  9.388   0.48 17.63 ?  20  ASN   A N    1 
ATOM   541  N N    B ASN   A 1 20  ? 8.443  -4.359  9.357   0.52 15.13 ?  20  ASN   A N    1 
ATOM   542  C CA   A ASN   A 1 20  ? 8.313  -3.260  8.821   0.48 17.97 ?  20  ASN   A CA   1 
ATOM   543  C CA   B ASN   A 1 20  ? 8.153  -3.081  8.706   0.52 16.08 ?  20  ASN   A CA   1 
ATOM   544  C C    A ASN   A 1 20  ? 8.935  -2.245  9.772   0.48 17.87 ?  20  ASN   A C    1 
ATOM   545  C C    B ASN   A 1 20  ? 8.695  -1.990  9.616   0.52 16.88 ?  20  ASN   A C    1 
ATOM   546  O O    A ASN   A 1 20  ? 8.434  -2.033  10.882  0.48 18.02 ?  20  ASN   A O    1 
ATOM   547  O O    B ASN   A 1 20  ? 8.032  -1.574  10.569  0.52 17.26 ?  20  ASN   A O    1 
ATOM   548  C CB   A ASN   A 1 20  ? 6.819  -3.001  8.618   0.48 19.04 ?  20  ASN   A CB   1 
ATOM   549  C CB   B ASN   A 1 20  ? 6.648  -2.933  8.492   0.52 17.04 ?  20  ASN   A CB   1 
ATOM   550  C CG   A ASN   A 1 20  ? 6.508  -1.543  8.268   0.48 19.72 ?  20  ASN   A CG   1 
ATOM   551  C CG   B ASN   A 1 20  ? 6.254  -1.603  7.851   0.52 17.19 ?  20  ASN   A CG   1 
ATOM   552  O OD1  A ASN   A 1 20  ? 5.606  -0.936  8.849   0.48 20.19 ?  20  ASN   A OD1  1 
ATOM   553  O OD1  B ASN   A 1 20  ? 5.083  -1.206  7.910   0.52 17.78 ?  20  ASN   A OD1  1 
ATOM   554  N ND2  A ASN   A 1 20  ? 7.248  -0.981  7.316   0.48 20.41 ?  20  ASN   A ND2  1 
ATOM   555  N ND2  B ASN   A 1 20  ? 7.210  -0.919  7.237   0.52 17.58 ?  20  ASN   A ND2  1 
ATOM   556  H H    A ASN   A 1 20  ? 7.895  -4.878  9.868   0.48 21.16 ?  20  ASN   A H    1 
ATOM   557  H H    B ASN   A 1 20  ? 7.768  -4.696  9.761   0.52 18.16 ?  20  ASN   A H    1 
ATOM   558  H HA   A ASN   A 1 20  ? 8.751  -3.189  7.959   0.48 21.58 ?  20  ASN   A HA   1 
ATOM   559  H HA   B ASN   A 1 20  ? 8.602  -3.041  7.849   0.52 19.30 ?  20  ASN   A HA   1 
ATOM   560  H HB2  A ASN   A 1 20  ? 6.493  -3.560  7.890   0.48 22.86 ?  20  ASN   A HB2  1 
ATOM   561  H HB2  B ASN   A 1 20  ? 6.342  -3.646  7.913   0.52 20.46 ?  20  ASN   A HB2  1 
ATOM   562  H HB3  A ASN   A 1 20  ? 6.341  -3.215  9.433   0.48 22.86 ?  20  ASN   A HB3  1 
ATOM   563  H HB3  B ASN   A 1 20  ? 6.197  -2.996  9.344   0.52 20.46 ?  20  ASN   A HB3  1 
ATOM   564  H HD21 A ASN   A 1 20  ? 7.106  -0.164  7.082   0.48 24.50 ?  20  ASN   A HD21 1 
ATOM   565  H HD21 B ASN   A 1 20  ? 7.020  -0.175  6.863   0.52 21.10 ?  20  ASN   A HD21 1 
ATOM   566  H HD22 A ASN   A 1 20  ? 7.875  -1.431  6.936   0.48 24.50 ?  20  ASN   A HD22 1 
ATOM   567  H HD22 B ASN   A 1 20  ? 8.018  -1.216  7.210   0.52 21.10 ?  20  ASN   A HD22 1 
ATOM   568  N N    A ALA   A 1 21  ? 10.043 -1.638  9.352   0.48 17.96 ?  21  ALA   A N    1 
ATOM   569  N N    B ALA   A 1 21  ? 9.916  -1.539  9.335   0.52 17.86 ?  21  ALA   A N    1 
ATOM   570  C CA   A ALA   A 1 21  ? 10.772 -0.756  10.246  0.48 17.55 ?  21  ALA   A CA   1 
ATOM   571  C CA   B ALA   A 1 21  ? 10.576 -0.594  10.220  0.52 18.66 ?  21  ALA   A CA   1 
ATOM   572  C C    A ALA   A 1 21  ? 11.726 0.116   9.447   0.48 16.81 ?  21  ALA   A C    1 
ATOM   573  C C    B ALA   A 1 21  ? 11.611 0.209   9.452   0.52 17.81 ?  21  ALA   A C    1 
ATOM   574  O O    A ALA   A 1 21  ? 12.164 -0.252  8.354   0.48 16.89 ?  21  ALA   A O    1 
ATOM   575  O O    B ALA   A 1 21  ? 12.089 -0.196  8.389   0.52 17.81 ?  21  ALA   A O    1 
ATOM   576  C CB   A ALA   A 1 21  ? 11.549 -1.559  11.293  0.48 18.07 ?  21  ALA   A CB   1 
ATOM   577  C CB   B ALA   A 1 21  ? 11.236 -1.302  11.405  0.52 19.99 ?  21  ALA   A CB   1 
ATOM   578  H H    A ALA   A 1 21  ? 10.388 -1.730  8.570   0.48 21.57 ?  21  ALA   A H    1 
ATOM   579  H H    B ALA   A 1 21  ? 10.374 -1.777  8.649   0.52 21.43 ?  21  ALA   A H    1 
ATOM   580  H HA   A ALA   A 1 21  ? 10.140 -0.180  10.708  0.48 21.07 ?  21  ALA   A HA   1 
ATOM   581  H HA   B ALA   A 1 21  ? 9.914  0.020   10.568  0.52 22.40 ?  21  ALA   A HA   1 
ATOM   582  H HB1  A ALA   A 1 21  ? 11.965 -0.940  11.908  0.48 21.69 ?  21  ALA   A HB1  1 
ATOM   583  H HB1  B ALA   A 1 21  ? 11.662 -0.638  11.968  0.52 24.00 ?  21  ALA   A HB1  1 
ATOM   584  H HB2  A ALA   A 1 21  ? 10.927 -2.134  11.772  0.48 21.69 ?  21  ALA   A HB2  1 
ATOM   585  H HB2  B ALA   A 1 21  ? 10.555 -1.777  11.909  0.52 24.00 ?  21  ALA   A HB2  1 
ATOM   586  H HB3  A ALA   A 1 21  ? 12.217 -2.096  10.846  0.48 21.69 ?  21  ALA   A HB3  1 
ATOM   587  H HB3  B ALA   A 1 21  ? 11.897 -1.929  11.071  0.52 24.00 ?  21  ALA   A HB3  1 
ATOM   588  N N    A ASP   A 1 22  ? 12.018 1.284   10.012  0.48 16.93 ?  22  ASP   A N    1 
ATOM   589  N N    B ASP   A 1 22  ? 11.930 1.368   10.019  0.52 17.71 ?  22  ASP   A N    1 
ATOM   590  C CA   A ASP   A 1 22  ? 13.062 2.170   9.513   0.48 17.05 ?  22  ASP   A CA   1 
ATOM   591  C CA   B ASP   A 1 22  ? 13.015 2.222   9.560   0.52 17.35 ?  22  ASP   A CA   1 
ATOM   592  C C    A ASP   A 1 22  ? 14.398 1.721   10.094  0.48 16.05 ?  22  ASP   A C    1 
ATOM   593  C C    B ASP   A 1 22  ? 14.331 1.635   10.063  0.52 16.29 ?  22  ASP   A C    1 
ATOM   594  O O    A ASP   A 1 22  ? 14.602 1.790   11.310  0.48 16.97 ?  22  ASP   A O    1 
ATOM   595  O O    B ASP   A 1 22  ? 14.534 1.515   11.275  0.52 16.56 ?  22  ASP   A O    1 
ATOM   596  C CB   A ASP   A 1 22  ? 12.742 3.597   9.953   0.48 19.11 ?  22  ASP   A CB   1 
ATOM   597  C CB   B ASP   A 1 22  ? 12.771 3.612   10.150  0.52 19.11 ?  22  ASP   A CB   1 
ATOM   598  C CG   A ASP   A 1 22  ? 13.811 4.597   9.541   0.48 21.50 ?  22  ASP   A CG   1 
ATOM   599  C CG   B ASP   A 1 22  ? 13.717 4.658   9.614   0.52 20.56 ?  22  ASP   A CG   1 
ATOM   600  O OD1  A ASP   A 1 22  ? 14.747 4.207   8.815   0.48 22.06 ?  22  ASP   A OD1  1 
ATOM   601  O OD1  B ASP   A 1 22  ? 14.912 4.348   9.461   0.52 19.60 ?  22  ASP   A OD1  1 
ATOM   602  O OD2  A ASP   A 1 22  ? 13.718 5.776   9.951   0.48 22.59 -1 22  ASP   A OD2  1 
ATOM   603  O OD2  B ASP   A 1 22  ? 13.264 5.799   9.357   0.52 22.22 -1 22  ASP   A OD2  1 
ATOM   604  H H    A ASP   A 1 22  ? 11.597 1.594   10.696  0.48 20.32 ?  22  ASP   A H    1 
ATOM   605  H H    B ASP   A 1 22  ? 11.502 1.690   10.692  0.52 21.26 ?  22  ASP   A H    1 
ATOM   606  H HA   A ASP   A 1 22  ? 13.099 2.126   8.542   0.48 20.47 ?  22  ASP   A HA   1 
ATOM   607  H HA   B ASP   A 1 22  ? 13.021 2.274   8.588   0.52 20.83 ?  22  ASP   A HA   1 
ATOM   608  H HB2  A ASP   A 1 22  ? 11.885 3.858   9.574   0.48 22.94 ?  22  ASP   A HB2  1 
ATOM   609  H HB2  B ASP   A 1 22  ? 11.863 3.888   9.945   0.52 22.93 ?  22  ASP   A HB2  1 
ATOM   610  H HB3  A ASP   A 1 22  ? 12.690 3.617   10.923  0.48 22.94 ?  22  ASP   A HB3  1 
ATOM   611  H HB3  B ASP   A 1 22  ? 12.890 3.565   11.112  0.52 22.93 ?  22  ASP   A HB3  1 
ATOM   612  N N    A ILE   A 1 23  ? 15.305 1.263   9.224   0.48 15.33 ?  23  ILE   A N    1 
ATOM   613  N N    B ILE   A 1 23  ? 15.207 1.232   9.137   0.52 16.01 ?  23  ILE   A N    1 
ATOM   614  C CA   A ILE   A 1 23  ? 16.558 0.662   9.677   0.48 15.01 ?  23  ILE   A CA   1 
ATOM   615  C CA   B ILE   A 1 23  ? 16.448 0.566   9.531   0.52 16.01 ?  23  ILE   A CA   1 
ATOM   616  C C    A ILE   A 1 23  ? 17.346 1.621   10.560  0.48 14.82 ?  23  ILE   A C    1 
ATOM   617  C C    B ILE   A 1 23  ? 17.300 1.467   10.414  0.52 16.34 ?  23  ILE   A C    1 
ATOM   618  O O    A ILE   A 1 23  ? 18.046 1.189   11.485  0.48 14.79 ?  23  ILE   A O    1 
ATOM   619  O O    B ILE   A 1 23  ? 18.034 0.980   11.284  0.52 16.68 ?  23  ILE   A O    1 
ATOM   620  C CB   A ILE   A 1 23  ? 17.372 0.130   8.474   0.48 14.85 ?  23  ILE   A CB   1 
ATOM   621  C CB   B ILE   A 1 23  ? 17.215 0.050   8.293   0.52 15.75 ?  23  ILE   A CB   1 
ATOM   622  C CG1  A ILE   A 1 23  ? 18.509 -0.789  8.946   0.48 15.36 ?  23  ILE   A CG1  1 
ATOM   623  C CG1  B ILE   A 1 23  ? 18.378 -0.856  8.720   0.52 15.92 ?  23  ILE   A CG1  1 
ATOM   624  C CG2  A ILE   A 1 23  ? 17.895 1.281   7.617   0.48 15.35 ?  23  ILE   A CG2  1 
ATOM   625  C CG2  B ILE   A 1 23  ? 17.697 1.212   7.432   0.52 16.19 ?  23  ILE   A CG2  1 
ATOM   626  C CD1  A ILE   A 1 23  ? 19.196 -1.559  7.823   0.48 15.68 ?  23  ILE   A CD1  1 
ATOM   627  C CD1  B ILE   A 1 23  ? 19.137 -1.478  7.559   0.52 16.10 ?  23  ILE   A CD1  1 
ATOM   628  H H    A ILE   A 1 23  ? 15.214 1.297   8.374   0.48 18.40 ?  23  ILE   A H    1 
ATOM   629  H H    B ILE   A 1 23  ? 15.100 1.328   8.292   0.52 19.22 ?  23  ILE   A H    1 
ATOM   630  H HA   A ILE   A 1 23  ? 16.344 -0.102  10.230  0.48 18.03 ?  23  ILE   A HA   1 
ATOM   631  H HA   B ILE   A 1 23  ? 16.213 -0.207  10.066  0.52 19.21 ?  23  ILE   A HA   1 
ATOM   632  H HB   A ILE   A 1 23  ? 16.773 -0.400  7.925   0.48 17.82 ?  23  ILE   A HB   1 
ATOM   633  H HB   B ILE   A 1 23  ? 16.598 -0.480  7.768   0.52 18.91 ?  23  ILE   A HB   1 
ATOM   634  H HG12 A ILE   A 1 23  ? 19.182 -0.253  9.388   0.48 18.44 ?  23  ILE   A HG12 1 
ATOM   635  H HG12 B ILE   A 1 23  ? 19.006 -0.333  9.240   0.52 19.11 ?  23  ILE   A HG12 1 
ATOM   636  H HG13 A ILE   A 1 23  ? 18.146 -1.441  9.567   0.48 18.44 ?  23  ILE   A HG13 1 
ATOM   637  H HG13 B ILE   A 1 23  ? 18.024 -1.579  9.264   0.52 19.11 ?  23  ILE   A HG13 1 
ATOM   638  H HG21 A ILE   A 1 23  ? 18.267 0.917   6.795   0.48 18.42 ?  23  ILE   A HG21 1 
ATOM   639  H HG21 B ILE   A 1 23  ? 18.029 0.861   6.590   0.52 19.44 ?  23  ILE   A HG21 1 
ATOM   640  H HG22 A ILE   A 1 23  ? 17.161 1.877   7.407   0.48 18.42 ?  23  ILE   A HG22 1 
ATOM   641  H HG22 B ILE   A 1 23  ? 16.955 1.813   7.267   0.52 19.44 ?  23  ILE   A HG22 1 
ATOM   642  H HG23 A ILE   A 1 23  ? 18.582 1.756   8.106   0.48 18.42 ?  23  ILE   A HG23 1 
ATOM   643  H HG23 B ILE   A 1 23  ? 18.406 1.680   7.898   0.52 19.44 ?  23  ILE   A HG23 1 
ATOM   644  H HD11 A ILE   A 1 23  ? 19.869 -2.146  8.205   0.48 18.82 ?  23  ILE   A HD11 1 
ATOM   645  H HD11 B ILE   A 1 23  ? 19.781 -2.113  7.909   0.52 19.33 ?  23  ILE   A HD11 1 
ATOM   646  H HD12 A ILE   A 1 23  ? 18.534 -2.085  7.346   0.48 18.82 ?  23  ILE   A HD12 1 
ATOM   647  H HD12 B ILE   A 1 23  ? 18.507 -1.932  6.977   0.52 19.33 ?  23  ILE   A HD12 1 
ATOM   648  H HD13 A ILE   A 1 23  ? 19.615 -0.929  7.216   0.48 18.82 ?  23  ILE   A HD13 1 
ATOM   649  H HD13 B ILE   A 1 23  ? 19.594 -0.777  7.069   0.52 19.33 ?  23  ILE   A HD13 1 
ATOM   650  N N    A VAL   A 1 24  ? 17.235 2.931   10.313  0.48 15.44 ?  24  VAL   A N    1 
ATOM   651  N N    B VAL   A 1 24  ? 17.218 2.785   10.214  0.52 17.18 ?  24  VAL   A N    1 
ATOM   652  C CA   A VAL   A 1 24  ? 17.921 3.907   11.159  0.48 17.11 ?  24  VAL   A CA   1 
ATOM   653  C CA   B VAL   A 1 24  ? 17.944 3.724   11.066  0.52 18.82 ?  24  VAL   A CA   1 
ATOM   654  C C    A VAL   A 1 24  ? 17.393 3.833   12.586  0.48 17.94 ?  24  VAL   A C    1 
ATOM   655  C C    B VAL   A 1 24  ? 17.410 3.671   12.492  0.52 19.64 ?  24  VAL   A C    1 
ATOM   656  O O    A VAL   A 1 24  ? 18.164 3.778   13.554  0.48 18.26 ?  24  VAL   A O    1 
ATOM   657  O O    B VAL   A 1 24  ? 18.176 3.573   13.459  0.52 20.32 ?  24  VAL   A O    1 
ATOM   658  C CB   A VAL   A 1 24  ? 17.781 5.326   10.573  0.48 18.33 ?  24  VAL   A CB   1 
ATOM   659  C CB   B VAL   A 1 24  ? 17.857 5.146   10.483  0.52 20.29 ?  24  VAL   A CB   1 
ATOM   660  C CG1  A VAL   A 1 24  ? 18.241 6.372   11.585  0.48 19.02 ?  24  VAL   A CG1  1 
ATOM   661  C CG1  B VAL   A 1 24  ? 18.514 6.151   11.419  0.52 21.62 ?  24  VAL   A CG1  1 
ATOM   662  C CG2  A VAL   A 1 24  ? 18.573 5.450   9.279   0.48 19.27 ?  24  VAL   A CG2  1 
ATOM   663  C CG2  B VAL   A 1 24  ? 18.488 5.192   9.099   0.52 20.94 ?  24  VAL   A CG2  1 
ATOM   664  H H    A VAL   A 1 24  ? 16.773 3.276   9.673   0.48 18.53 ?  24  VAL   A H    1 
ATOM   665  H H    B VAL   A 1 24  ? 16.754 3.159   9.597   0.52 20.62 ?  24  VAL   A H    1 
ATOM   666  H HA   A VAL   A 1 24  ? 18.867 3.696   11.178  0.48 20.54 ?  24  VAL   A HA   1 
ATOM   667  H HA   B VAL   A 1 24  ? 18.881 3.475   11.088  0.52 22.59 ?  24  VAL   A HA   1 
ATOM   668  H HB   A VAL   A 1 24  ? 16.849 5.498   10.367  0.48 22.01 ?  24  VAL   A HB   1 
ATOM   669  H HB   B VAL   A 1 24  ? 16.924 5.395   10.389  0.52 24.36 ?  24  VAL   A HB   1 
ATOM   670  H HG11 A VAL   A 1 24  ? 18.422 7.201   11.118  0.48 22.83 ?  24  VAL   A HG11 1 
ATOM   671  H HG11 B VAL   A 1 24  ? 18.644 6.983   10.942  0.52 25.95 ?  24  VAL   A HG11 1 
ATOM   672  H HG12 A VAL   A 1 24  ? 17.540 6.505   12.239  0.48 22.83 ?  24  VAL   A HG12 1 
ATOM   673  H HG12 B VAL   A 1 24  ? 17.934 6.294   12.183  0.52 25.95 ?  24  VAL   A HG12 1 
ATOM   674  H HG13 A VAL   A 1 24  ? 19.049 6.053   12.017  0.48 22.83 ?  24  VAL   A HG13 1 
ATOM   675  H HG13 B VAL   A 1 24  ? 19.367 5.795   11.709  0.52 25.95 ?  24  VAL   A HG13 1 
ATOM   676  H HG21 A VAL   A 1 24  ? 18.320 6.273   8.828   0.48 23.14 ?  24  VAL   A HG21 1 
ATOM   677  H HG21 B VAL   A 1 24  ? 18.450 6.102   8.762   0.52 25.14 ?  24  VAL   A HG21 1 
ATOM   678  H HG22 A VAL   A 1 24  ? 19.521 5.470   9.487   0.48 23.14 ?  24  VAL   A HG22 1 
ATOM   679  H HG22 B VAL   A 1 24  ? 19.414 4.906   9.165   0.52 25.14 ?  24  VAL   A HG22 1 
ATOM   680  H HG23 A VAL   A 1 24  ? 18.375 4.690   8.709   0.48 23.14 ?  24  VAL   A HG23 1 
ATOM   681  H HG23 B VAL   A 1 24  ? 18.000 4.600   8.507   0.52 25.14 ?  24  VAL   A HG23 1 
ATOM   682  N N    A GLU   A 1 25  ? 16.067 3.834   12.738  0.48 19.29 ?  25  GLU   A N    1 
ATOM   683  N N    B GLU   A 1 25  ? 16.085 3.737   12.643  0.52 20.37 ?  25  GLU   A N    1 
ATOM   684  C CA   A GLU   A 1 25  ? 15.480 3.760   14.072  0.48 20.93 ?  25  GLU   A CA   1 
ATOM   685  C CA   B GLU   A 1 25  ? 15.495 3.710   13.977  0.52 21.67 ?  25  GLU   A CA   1 
ATOM   686  C C    A GLU   A 1 25  ? 15.704 2.392   14.705  0.48 19.71 ?  25  GLU   A C    1 
ATOM   687  C C    B GLU   A 1 25  ? 15.721 2.366   14.656  0.52 20.14 ?  25  GLU   A C    1 
ATOM   688  O O    A GLU   A 1 25  ? 15.933 2.299   15.918  0.48 20.44 ?  25  GLU   A O    1 
ATOM   689  O O    B GLU   A 1 25  ? 15.935 2.309   15.873  0.52 21.01 ?  25  GLU   A O    1 
ATOM   690  C CB   A GLU   A 1 25  ? 13.994 4.114   14.013  0.48 23.86 ?  25  GLU   A CB   1 
ATOM   691  C CB   B GLU   A 1 25  ? 14.006 4.049   13.900  0.52 24.42 ?  25  GLU   A CB   1 
ATOM   692  C CG   A GLU   A 1 25  ? 13.736 5.556   13.601  0.48 27.37 ?  25  GLU   A CG   1 
ATOM   693  C CG   B GLU   A 1 25  ? 13.742 5.483   13.463  0.52 28.04 ?  25  GLU   A CG   1 
ATOM   694  C CD   A GLU   A 1 25  ? 14.460 6.558   14.481  0.48 30.43 ?  25  GLU   A CD   1 
ATOM   695  C CD   B GLU   A 1 25  ? 14.575 6.503   14.224  0.52 31.19 ?  25  GLU   A CD   1 
ATOM   696  O OE1  A GLU   A 1 25  ? 14.531 6.332   15.709  0.48 31.53 ?  25  GLU   A OE1  1 
ATOM   697  O OE1  B GLU   A 1 25  ? 14.719 6.364   15.457  0.52 32.58 ?  25  GLU   A OE1  1 
ATOM   698  O OE2  A GLU   A 1 25  ? 14.969 7.565   13.945  0.48 31.62 -1 25  GLU   A OE2  1 
ATOM   699  O OE2  B GLU   A 1 25  ? 15.104 7.435   13.581  0.52 32.35 -1 25  GLU   A OE2  1 
ATOM   700  H H    A GLU   A 1 25  ? 15.500 3.887   12.094  0.48 23.15 ?  25  GLU   A H    1 
ATOM   701  H H    B GLU   A 1 25  ? 15.521 3.802   11.997  0.52 24.46 ?  25  GLU   A H    1 
ATOM   702  H HA   A GLU   A 1 25  ? 15.923 4.408   14.637  0.48 25.12 ?  25  GLU   A HA   1 
ATOM   703  H HA   B GLU   A 1 25  ? 15.933 4.375   14.523  0.52 26.01 ?  25  GLU   A HA   1 
ATOM   704  H HB2  A GLU   A 1 25  ? 13.557 3.537   13.366  0.48 28.64 ?  25  GLU   A HB2  1 
ATOM   705  H HB2  B GLU   A 1 25  ? 13.578 3.457   13.255  0.52 29.31 ?  25  GLU   A HB2  1 
ATOM   706  H HB3  A GLU   A 1 25  ? 13.605 3.981   14.891  0.48 28.64 ?  25  GLU   A HB3  1 
ATOM   707  H HB3  B GLU   A 1 25  ? 13.607 3.922   14.774  0.52 29.31 ?  25  GLU   A HB3  1 
ATOM   708  H HG2  A GLU   A 1 25  ? 14.037 5.680   12.687  0.48 32.85 ?  25  GLU   A HG2  1 
ATOM   709  H HG2  B GLU   A 1 25  ? 13.967 5.572   12.527  0.52 33.65 ?  25  GLU   A HG2  1 
ATOM   710  H HG3  A GLU   A 1 25  ? 12.788 5.738   13.670  0.48 32.85 ?  25  GLU   A HG3  1 
ATOM   711  H HG3  B GLU   A 1 25  ? 12.805 5.685   13.607  0.52 33.65 ?  25  GLU   A HG3  1 
ATOM   712  N N    A GLU   A 1 26  ? 15.652 1.322   13.905  0.48 19.38 ?  26  GLU   A N    1 
ATOM   713  N N    B GLU   A 1 26  ? 15.696 1.278   13.883  0.52 19.51 ?  26  GLU   A N    1 
ATOM   714  C CA   A GLU   A 1 26  ? 15.974 -0.002  14.429  0.48 19.56 ?  26  GLU   A CA   1 
ATOM   715  C CA   B GLU   A 1 26  ? 15.978 -0.036  14.450  0.52 19.50 ?  26  GLU   A CA   1 
ATOM   716  C C    A GLU   A 1 26  ? 17.391 -0.028  14.982  0.48 18.85 ?  26  GLU   A C    1 
ATOM   717  C C    B GLU   A 1 26  ? 17.414 -0.124  14.941  0.52 19.03 ?  26  GLU   A C    1 
ATOM   718  O O    A GLU   A 1 26  ? 17.625 -0.482  16.109  0.48 19.17 ?  26  GLU   A O    1 
ATOM   719  O O    B GLU   A 1 26  ? 17.684 -0.727  15.986  0.52 19.63 ?  26  GLU   A O    1 
ATOM   720  C CB   A GLU   A 1 26  ? 15.825 -1.063  13.334  0.48 21.04 ?  26  GLU   A CB   1 
ATOM   721  C CB   B GLU   A 1 26  ? 15.716 -1.120  13.407  0.52 20.53 ?  26  GLU   A CB   1 
ATOM   722  C CG   A GLU   A 1 26  ? 14.441 -1.652  13.180  0.48 23.17 ?  26  GLU   A CG   1 
ATOM   723  C CG   B GLU   A 1 26  ? 14.254 -1.375  13.139  0.52 23.04 ?  26  GLU   A CG   1 
ATOM   724  C CD   A GLU   A 1 26  ? 14.018 -2.450  14.398  0.48 23.75 ?  26  GLU   A CD   1 
ATOM   725  C CD   B GLU   A 1 26  ? 13.533 -1.968  14.327  0.52 23.74 ?  26  GLU   A CD   1 
ATOM   726  O OE1  A GLU   A 1 26  ? 14.462 -3.608  14.575  0.48 23.82 ?  26  GLU   A OE1  1 
ATOM   727  O OE1  B GLU   A 1 26  ? 14.079 -2.891  14.964  0.52 23.58 ?  26  GLU   A OE1  1 
ATOM   728  O OE2  A GLU   A 1 26  ? 13.248 -1.896  15.198  0.48 23.87 -1 26  GLU   A OE2  1 
ATOM   729  O OE2  B GLU   A 1 26  ? 12.421 -1.496  14.624  0.52 24.15 -1 26  GLU   A OE2  1 
ATOM   730  H H    A GLU   A 1 26  ? 15.447 1.338   13.070  0.48 23.26 ?  26  GLU   A H    1 
ATOM   731  H H    B GLU   A 1 26  ? 15.528 1.276   13.040  0.52 23.42 ?  26  GLU   A H    1 
ATOM   732  H HA   A GLU   A 1 26  ? 15.365 -0.216  15.151  0.48 23.48 ?  26  GLU   A HA   1 
ATOM   733  H HA   B GLU   A 1 26  ? 15.394 -0.189  15.205  0.52 23.40 ?  26  GLU   A HA   1 
ATOM   734  H HB2  A GLU   A 1 26  ? 16.067 -0.669  12.486  0.48 25.26 ?  26  GLU   A HB2  1 
ATOM   735  H HB2  B GLU   A 1 26  ? 16.129 -0.850  12.568  0.52 24.64 ?  26  GLU   A HB2  1 
ATOM   736  H HB3  A GLU   A 1 26  ? 16.428 -1.798  13.536  0.48 25.26 ?  26  GLU   A HB3  1 
ATOM   737  H HB3  B GLU   A 1 26  ? 16.119 -1.949  13.712  0.52 24.64 ?  26  GLU   A HB3  1 
ATOM   738  H HG2  A GLU   A 1 26  ? 13.805 -0.929  13.052  0.48 27.82 ?  26  GLU   A HG2  1 
ATOM   739  H HG2  B GLU   A 1 26  ? 13.822 -0.538  12.926  0.52 27.66 ?  26  GLU   A HG2  1 
ATOM   740  H HG3  A GLU   A 1 26  ? 14.424 -2.242  12.408  0.48 27.82 ?  26  GLU   A HG3  1 
ATOM   741  H HG3  B GLU   A 1 26  ? 14.172 -1.999  12.405  0.52 27.66 ?  26  GLU   A HG3  1 
ATOM   742  N N    . ALA   A 1 27  ? 18.352 0.462   14.197  1.00 18.40 ?  27  ALA   A N    1 
ATOM   743  C CA   . ALA   A 1 27  ? 19.746 0.444   14.624  1.00 18.52 ?  27  ALA   A CA   1 
ATOM   744  C C    . ALA   A 1 27  ? 19.929 1.233   15.914  1.00 20.60 ?  27  ALA   A C    1 
ATOM   745  O O    . ALA   A 1 27  ? 20.590 0.769   16.849  1.00 20.27 ?  27  ALA   A O    1 
ATOM   746  C CB   . ALA   A 1 27  ? 20.635 0.993   13.506  1.00 17.99 ?  27  ALA   A CB   1 
ATOM   747  H H    A ALA   A 1 27  ? 18.221 0.822   13.425  0.48 22.08 ?  27  ALA   A H    1 
ATOM   748  H H    B ALA   A 1 27  ? 18.208 0.879   13.456  0.52 22.08 ?  27  ALA   A H    1 
ATOM   749  H HA   . ALA   A 1 27  ? 20.011 -0.472  14.790  1.00 22.24 ?  27  ALA   A HA   1 
ATOM   750  H HB1  . ALA   A 1 27  ? 21.562 0.974   13.798  1.00 21.59 ?  27  ALA   A HB1  1 
ATOM   751  H HB2  . ALA   A 1 27  ? 20.530 0.441   12.714  1.00 21.59 ?  27  ALA   A HB2  1 
ATOM   752  H HB3  . ALA   A 1 27  ? 20.373 1.906   13.307  1.00 21.59 ?  27  ALA   A HB3  1 
ATOM   753  N N    A LYS   A 1 28  ? 19.346 2.432   15.989  0.48 22.73 ?  28  LYS   A N    1 
ATOM   754  N N    B LYS   A 1 28  ? 19.331 2.425   15.990  0.52 22.38 ?  28  LYS   A N    1 
ATOM   755  C CA   A LYS   A 1 28  ? 19.506 3.247   17.190  0.48 25.62 ?  28  LYS   A CA   1 
ATOM   756  C CA   B LYS   A 1 28  ? 19.463 3.239   17.195  0.52 25.03 ?  28  LYS   A CA   1 
ATOM   757  C C    A LYS   A 1 28  ? 18.937 2.555   18.422  0.48 27.01 ?  28  LYS   A C    1 
ATOM   758  C C    B LYS   A 1 28  ? 18.896 2.530   18.419  0.52 26.44 ?  28  LYS   A C    1 
ATOM   759  O O    A LYS   A 1 28  ? 19.467 2.723   19.526  0.48 27.84 ?  28  LYS   A O    1 
ATOM   760  O O    B LYS   A 1 28  ? 19.411 2.706   19.529  0.52 27.42 ?  28  LYS   A O    1 
ATOM   761  C CB   A LYS   A 1 28  ? 18.873 4.627   16.992  0.48 27.64 ?  28  LYS   A CB   1 
ATOM   762  C CB   B LYS   A 1 28  ? 18.792 4.600   16.993  0.52 26.90 ?  28  LYS   A CB   1 
ATOM   763  C CG   A LYS   A 1 28  ? 19.670 5.523   16.059  0.48 29.58 ?  28  LYS   A CG   1 
ATOM   764  C CG   B LYS   A 1 28  ? 19.524 5.500   16.010  0.52 28.81 ?  28  LYS   A CG   1 
ATOM   765  C CD   A LYS   A 1 28  ? 19.196 6.966   16.099  0.48 31.67 ?  28  LYS   A CD   1 
ATOM   766  C CD   B LYS   A 1 28  ? 19.134 6.965   16.163  0.52 31.09 ?  28  LYS   A CD   1 
ATOM   767  C CE   A LYS   A 1 28  ? 17.865 7.137   15.395  0.48 33.16 ?  28  LYS   A CE   1 
ATOM   768  C CE   B LYS   A 1 28  ? 17.908 7.315   15.342  0.52 32.79 ?  28  LYS   A CE   1 
ATOM   769  N NZ   A LYS   A 1 28  ? 17.488 8.575   15.293  0.48 34.13 ?  28  LYS   A NZ   1 
ATOM   770  N NZ   B LYS   A 1 28  ? 17.775 8.791   15.170  0.52 33.88 ?  28  LYS   A NZ   1 
ATOM   771  H H    A LYS   A 1 28  ? 18.867 2.787   15.373  0.48 27.29 ?  28  LYS   A H    1 
ATOM   772  H H    B LYS   A 1 28  ? 18.855 2.776   15.369  0.52 26.87 ?  28  LYS   A H    1 
ATOM   773  H HA   A LYS   A 1 28  ? 20.452 3.384   17.350  0.48 30.75 ?  28  LYS   A HA   1 
ATOM   774  H HA   B LYS   A 1 28  ? 20.403 3.400   17.362  0.52 30.04 ?  28  LYS   A HA   1 
ATOM   775  H HB2  A LYS   A 1 28  ? 17.988 4.518   16.613  0.48 33.18 ?  28  LYS   A HB2  1 
ATOM   776  H HB2  B LYS   A 1 28  ? 17.895 4.464   16.653  0.52 32.29 ?  28  LYS   A HB2  1 
ATOM   777  H HB3  A LYS   A 1 28  ? 18.812 5.075   17.851  0.48 33.18 ?  28  LYS   A HB3  1 
ATOM   778  H HB3  B LYS   A 1 28  ? 18.755 5.062   17.845  0.52 32.29 ?  28  LYS   A HB3  1 
ATOM   779  H HG2  A LYS   A 1 28  ? 20.603 5.507   16.322  0.48 35.51 ?  28  LYS   A HG2  1 
ATOM   780  H HG2  B LYS   A 1 28  ? 20.479 5.429   16.163  0.52 34.58 ?  28  LYS   A HG2  1 
ATOM   781  H HG3  A LYS   A 1 28  ? 19.573 5.201   15.150  0.48 35.51 ?  28  LYS   A HG3  1 
ATOM   782  H HG3  B LYS   A 1 28  ? 19.310 5.225   15.105  0.52 34.58 ?  28  LYS   A HG3  1 
ATOM   783  H HD2  A LYS   A 1 28  ? 19.088 7.243   17.023  0.48 38.02 ?  28  LYS   A HD2  1 
ATOM   784  H HD2  B LYS   A 1 28  ? 18.936 7.149   17.096  0.52 37.31 ?  28  LYS   A HD2  1 
ATOM   785  H HD3  A LYS   A 1 28  ? 19.849 7.530   15.654  0.48 38.02 ?  28  LYS   A HD3  1 
ATOM   786  H HD3  B LYS   A 1 28  ? 19.868 7.523   15.863  0.52 37.31 ?  28  LYS   A HD3  1 
ATOM   787  H HE2  A LYS   A 1 28  ? 17.929 6.774   14.498  0.48 39.80 ?  28  LYS   A HE2  1 
ATOM   788  H HE2  B LYS   A 1 28  ? 17.983 6.913   14.462  0.52 39.35 ?  28  LYS   A HE2  1 
ATOM   789  H HE3  A LYS   A 1 28  ? 17.176 6.676   15.897  0.48 39.80 ?  28  LYS   A HE3  1 
ATOM   790  H HE3  B LYS   A 1 28  ? 17.114 6.989   15.794  0.52 39.35 ?  28  LYS   A HE3  1 
ATOM   791  H HZ1  A LYS   A 1 28  ? 16.706 8.655   14.877  0.48 40.96 ?  28  LYS   A HZ1  1 
ATOM   792  H HZ1  B LYS   A 1 28  ? 17.053 8.978   14.686  0.52 40.67 ?  28  LYS   A HZ1  1 
ATOM   793  H HZ2  A LYS   A 1 28  ? 17.422 8.930   16.106  0.48 40.96 ?  28  LYS   A HZ2  1 
ATOM   794  H HZ2  B LYS   A 1 28  ? 17.701 9.185   15.965  0.52 40.67 ?  28  LYS   A HZ2  1 
ATOM   795  H HZ3  A LYS   A 1 28  ? 18.108 9.020   14.833  0.48 40.96 ?  28  LYS   A HZ3  1 
ATOM   796  H HZ3  B LYS   A 1 28  ? 18.493 9.115   14.754  0.52 40.67 ?  28  LYS   A HZ3  1 
ATOM   797  N N    A LYS   A 1 29  ? 17.872 1.770   18.256  0.48 27.77 ?  29  LYS   A N    1 
ATOM   798  N N    B LYS   A 1 29  ? 17.850 1.723   18.240  0.52 27.13 ?  29  LYS   A N    1 
ATOM   799  C CA   A LYS   A 1 29  ? 17.274 1.066   19.386  0.48 29.41 ?  29  LYS   A CA   1 
ATOM   800  C CA   B LYS   A 1 29  ? 17.220 1.041   19.367  0.52 28.84 ?  29  LYS   A CA   1 
ATOM   801  C C    A LYS   A 1 29  ? 18.086 -0.168  19.765  0.48 28.69 ?  29  LYS   A C    1 
ATOM   802  C C    B LYS   A 1 29  ? 17.993 -0.212  19.766  0.52 28.27 ?  29  LYS   A C    1 
ATOM   803  O O    A LYS   A 1 29  ? 18.438 -0.354  20.935  0.48 29.42 ?  29  LYS   A O    1 
ATOM   804  O O    B LYS   A 1 29  ? 18.214 -0.461  20.957  0.52 28.59 ?  29  LYS   A O    1 
ATOM   805  C CB   A LYS   A 1 29  ? 15.836 0.668   19.043  0.48 32.14 ?  29  LYS   A CB   1 
ATOM   806  C CB   B LYS   A 1 29  ? 15.781 0.670   19.005  0.52 31.63 ?  29  LYS   A CB   1 
ATOM   807  C CG   A LYS   A 1 29  ? 15.096 -0.050  20.164  0.48 34.66 ?  29  LYS   A CG   1 
ATOM   808  C CG   B LYS   A 1 29  ? 14.978 0.054   20.142  0.52 34.21 ?  29  LYS   A CG   1 
ATOM   809  C CD   A LYS   A 1 29  ? 14.751 0.899   21.298  0.48 36.94 ?  29  LYS   A CD   1 
ATOM   810  C CD   B LYS   A 1 29  ? 14.627 1.084   21.203  0.52 36.55 ?  29  LYS   A CD   1 
ATOM   811  C CE   A LYS   A 1 29  ? 13.846 0.229   22.321  0.48 38.40 ?  29  LYS   A CE   1 
ATOM   812  C CE   B LYS   A 1 29  ? 13.699 0.495   22.255  0.52 38.05 ?  29  LYS   A CE   1 
ATOM   813  N NZ   A LYS   A 1 29  ? 13.403 1.178   23.378  0.48 39.25 ?  29  LYS   A NZ   1 
ATOM   814  N NZ   B LYS   A 1 29  ? 13.431 1.455   23.361  0.52 38.94 ?  29  LYS   A NZ   1 
ATOM   815  H H    A LYS   A 1 29  ? 17.478 1.635   17.505  0.48 33.33 ?  29  LYS   A H    1 
ATOM   816  H H    B LYS   A 1 29  ? 17.485 1.563   17.479  0.52 32.57 ?  29  LYS   A H    1 
ATOM   817  H HA   A LYS   A 1 29  ? 17.248 1.656   20.154  0.48 35.30 ?  29  LYS   A HA   1 
ATOM   818  H HA   B LYS   A 1 29  ? 17.198 1.639   20.130  0.52 34.62 ?  29  LYS   A HA   1 
ATOM   819  H HB2  A LYS   A 1 29  ? 15.334 1.470   18.829  0.48 38.58 ?  29  LYS   A HB2  1 
ATOM   820  H HB2  B LYS   A 1 29  ? 15.318 1.471   18.721  0.52 37.97 ?  29  LYS   A HB2  1 
ATOM   821  H HB3  A LYS   A 1 29  ? 15.850 0.077   18.275  0.48 38.58 ?  29  LYS   A HB3  1 
ATOM   822  H HB3  B LYS   A 1 29  ? 15.801 0.027   18.280  0.52 37.97 ?  29  LYS   A HB3  1 
ATOM   823  H HG2  A LYS   A 1 29  ? 14.269 -0.416  19.814  0.48 41.60 ?  29  LYS   A HG2  1 
ATOM   824  H HG2  B LYS   A 1 29  ? 14.151 -0.307  19.786  0.52 41.06 ?  29  LYS   A HG2  1 
ATOM   825  H HG3  A LYS   A 1 29  ? 15.650 -0.763  20.520  0.48 41.60 ?  29  LYS   A HG3  1 
ATOM   826  H HG3  B LYS   A 1 29  ? 15.495 -0.652  20.562  0.52 41.06 ?  29  LYS   A HG3  1 
ATOM   827  H HD2  A LYS   A 1 29  ? 15.566 1.174   21.746  0.48 44.33 ?  29  LYS   A HD2  1 
ATOM   828  H HD2  B LYS   A 1 29  ? 15.438 1.381   21.644  0.52 43.86 ?  29  LYS   A HD2  1 
ATOM   829  H HD3  A LYS   A 1 29  ? 14.286 1.671   20.940  0.48 44.33 ?  29  LYS   A HD3  1 
ATOM   830  H HD3  B LYS   A 1 29  ? 14.177 1.835   20.785  0.52 43.86 ?  29  LYS   A HD3  1 
ATOM   831  H HE2  A LYS   A 1 29  ? 13.057 -0.115  21.873  0.48 46.09 ?  29  LYS   A HE2  1 
ATOM   832  H HE2  B LYS   A 1 29  ? 12.852 0.265   21.841  0.52 45.67 ?  29  LYS   A HE2  1 
ATOM   833  H HE3  A LYS   A 1 29  ? 14.330 -0.496  22.748  0.48 46.09 ?  29  LYS   A HE3  1 
ATOM   834  H HE3  B LYS   A 1 29  ? 14.110 -0.298  22.635  0.52 45.67 ?  29  LYS   A HE3  1 
ATOM   835  H HZ1  A LYS   A 1 29  ? 12.876 0.760   23.961  0.48 47.11 ?  29  LYS   A HZ1  1 
ATOM   836  H HZ1  B LYS   A 1 29  ? 12.887 1.083   23.960  0.52 46.74 ?  29  LYS   A HZ1  1 
ATOM   837  H HZ2  A LYS   A 1 29  ? 14.110 1.505   23.809  0.48 47.11 ?  29  LYS   A HZ2  1 
ATOM   838  H HZ2  B LYS   A 1 29  ? 14.194 1.677   23.762  0.52 46.74 ?  29  LYS   A HZ2  1 
ATOM   839  H HZ3  A LYS   A 1 29  ? 12.951 1.851   23.011  0.48 47.11 ?  29  LYS   A HZ3  1 
ATOM   840  H HZ3  B LYS   A 1 29  ? 13.048 2.190   23.039  0.52 46.74 ?  29  LYS   A HZ3  1 
ATOM   841  N N    . VAL   A 1 30  ? 18.386 -1.023  18.787  1.00 27.42 ?  30  VAL   A N    1 
ATOM   842  C CA   . VAL   A 1 30  ? 19.037 -2.296  19.081  1.00 26.63 ?  30  VAL   A CA   1 
ATOM   843  C C    . VAL   A 1 30  ? 20.541 -2.150  19.286  1.00 24.93 ?  30  VAL   A C    1 
ATOM   844  O O    . VAL   A 1 30  ? 21.132 -2.889  20.079  1.00 25.27 ?  30  VAL   A O    1 
ATOM   845  C CB   . VAL   A 1 30  ? 18.734 -3.293  17.945  1.00 27.27 ?  30  VAL   A CB   1 
ATOM   846  C CG1  . VAL   A 1 30  ? 19.494 -4.603  18.147  1.00 27.98 ?  30  VAL   A CG1  1 
ATOM   847  C CG2  . VAL   A 1 30  ? 17.235 -3.548  17.842  1.00 27.93 ?  30  VAL   A CG2  1 
ATOM   848  H H    A VAL   A 1 30  ? 18.225 -0.892  17.952  0.48 32.91 ?  30  VAL   A H    1 
ATOM   849  H H    B VAL   A 1 30  ? 18.277 -0.867  17.948  0.52 32.91 ?  30  VAL   A H    1 
ATOM   850  H HA   . VAL   A 1 30  ? 18.655 -2.658  19.896  1.00 31.97 ?  30  VAL   A HA   1 
ATOM   851  H HB   . VAL   A 1 30  ? 19.031 -2.910  17.106  1.00 32.73 ?  30  VAL   A HB   1 
ATOM   852  H HG11 . VAL   A 1 30  ? 19.096 -5.288  17.584  1.00 33.59 ?  30  VAL   A HG11 1 
ATOM   853  H HG12 . VAL   A 1 30  ? 20.423 -4.475  17.900  1.00 33.59 ?  30  VAL   A HG12 1 
ATOM   854  H HG13 . VAL   A 1 30  ? 19.430 -4.866  19.077  1.00 33.59 ?  30  VAL   A HG13 1 
ATOM   855  H HG21 . VAL   A 1 30  ? 17.076 -4.213  17.154  1.00 33.52 ?  30  VAL   A HG21 1 
ATOM   856  H HG22 . VAL   A 1 30  ? 16.912 -3.872  18.697  1.00 33.52 ?  30  VAL   A HG22 1 
ATOM   857  H HG23 . VAL   A 1 30  ? 16.791 -2.719  17.611  1.00 33.52 ?  30  VAL   A HG23 1 
ATOM   858  N N    A LYS   A 1 31  ? 21.178 -1.215  18.591  0.48 24.43 ?  31  LYS   A N    1 
ATOM   859  N N    B LYS   A 1 31  ? 21.175 -1.212  18.592  0.52 24.20 ?  31  LYS   A N    1 
ATOM   860  C CA   A LYS   A 1 31  ? 22.632 -1.118  18.544  0.48 25.01 ?  31  LYS   A CA   1 
ATOM   861  C CA   B LYS   A 1 31  ? 22.628 -1.115  18.536  0.52 24.77 ?  31  LYS   A CA   1 
ATOM   862  C C    A LYS   A 1 31  ? 23.235 -2.487  18.218  0.48 22.43 ?  31  LYS   A C    1 
ATOM   863  C C    B LYS   A 1 31  ? 23.231 -2.486  18.218  0.52 22.21 ?  31  LYS   A C    1 
ATOM   864  O O    A LYS   A 1 31  ? 24.000 -3.043  19.014  0.48 23.56 ?  31  LYS   A O    1 
ATOM   865  O O    B LYS   A 1 31  ? 23.989 -3.041  19.020  0.52 23.38 ?  31  LYS   A O    1 
ATOM   866  C CB   A LYS   A 1 31  ? 23.206 -0.561  19.839  0.48 28.80 ?  31  LYS   A CB   1 
ATOM   867  C CB   B LYS   A 1 31  ? 23.210 -0.541  19.821  0.52 28.39 ?  31  LYS   A CB   1 
ATOM   868  C CG   A LYS   A 1 31  ? 22.525 0.707   20.327  0.48 32.74 ?  31  LYS   A CG   1 
ATOM   869  C CG   B LYS   A 1 31  ? 22.469 0.688   20.328  0.52 32.28 ?  31  LYS   A CG   1 
ATOM   870  C CD   A LYS   A 1 31  ? 23.539 1.742   20.787  0.48 35.81 ?  31  LYS   A CD   1 
ATOM   871  C CD   B LYS   A 1 31  ? 23.401 1.656   21.038  0.52 35.21 ?  31  LYS   A CD   1 
ATOM   872  C CE   A LYS   A 1 31  ? 22.899 2.795   21.678  0.48 37.71 ?  31  LYS   A CE   1 
ATOM   873  C CE   B LYS   A 1 31  ? 22.635 2.598   21.957  0.52 37.01 ?  31  LYS   A CE   1 
ATOM   874  N NZ   A LYS   A 1 31  ? 21.735 3.461   21.033  0.48 38.77 ?  31  LYS   A NZ   1 
ATOM   875  N NZ   B LYS   A 1 31  ? 21.516 3.302   21.271  0.52 38.02 ?  31  LYS   A NZ   1 
ATOM   876  H H    A LYS   A 1 31  ? 20.778 -0.612  18.128  0.48 29.32 ?  31  LYS   A H    1 
ATOM   877  H H    B LYS   A 1 31  ? 20.772 -0.606  18.135  0.52 29.05 ?  31  LYS   A H    1 
ATOM   878  H HA   A LYS   A 1 31  ? 22.870 -0.508  17.833  0.48 30.02 ?  31  LYS   A HA   1 
ATOM   879  H HA   B LYS   A 1 31  ? 22.861 -0.511  17.817  0.52 29.73 ?  31  LYS   A HA   1 
ATOM   880  H HB2  A LYS   A 1 31  ? 23.120 -1.231  20.531  0.48 34.57 ?  31  LYS   A HB2  1 
ATOM   881  H HB2  B LYS   A 1 31  ? 23.175 -1.217  20.514  0.52 34.08 ?  31  LYS   A HB2  1 
ATOM   882  H HB3  A LYS   A 1 31  ? 24.144 -0.354  19.697  0.48 34.57 ?  31  LYS   A HB3  1 
ATOM   883  H HB3  B LYS   A 1 31  ? 24.132 -0.284  19.657  0.52 34.08 ?  31  LYS   A HB3  1 
ATOM   884  H HG2  A LYS   A 1 31  ? 22.005 1.091   19.603  0.48 39.29 ?  31  LYS   A HG2  1 
ATOM   885  H HG2  B LYS   A 1 31  ? 22.065 1.151   19.577  0.52 38.75 ?  31  LYS   A HG2  1 
ATOM   886  H HG3  A LYS   A 1 31  ? 21.948 0.492   21.077  0.48 39.29 ?  31  LYS   A HG3  1 
ATOM   887  H HG3  B LYS   A 1 31  ? 21.784 0.410   20.957  0.52 38.75 ?  31  LYS   A HG3  1 
ATOM   888  H HD2  A LYS   A 1 31  ? 24.240 1.301   21.292  0.48 42.98 ?  31  LYS   A HD2  1 
ATOM   889  H HD2  B LYS   A 1 31  ? 24.035 1.155   21.575  0.52 42.26 ?  31  LYS   A HD2  1 
ATOM   890  H HD3  A LYS   A 1 31  ? 23.916 2.188   20.011  0.48 42.98 ?  31  LYS   A HD3  1 
ATOM   891  H HD3  B LYS   A 1 31  ? 23.871 2.190   20.377  0.52 42.26 ?  31  LYS   A HD3  1 
ATOM   892  H HE2  A LYS   A 1 31  ? 22.589 2.372   22.494  0.48 45.26 ?  31  LYS   A HE2  1 
ATOM   893  H HE2  B LYS   A 1 31  ? 22.260 2.086   22.689  0.52 44.42 ?  31  LYS   A HE2  1 
ATOM   894  H HE3  A LYS   A 1 31  ? 23.557 3.476   21.886  0.48 45.26 ?  31  LYS   A HE3  1 
ATOM   895  H HE3  B LYS   A 1 31  ? 23.245 3.270   22.299  0.52 44.42 ?  31  LYS   A HE3  1 
ATOM   896  H HZ1  A LYS   A 1 31  ? 21.401 4.083   21.576  0.48 46.53 ?  31  LYS   A HZ1  1 
ATOM   897  H HZ1  B LYS   A 1 31  ? 21.114 3.858   21.839  0.52 45.63 ?  31  LYS   A HZ1  1 
ATOM   898  H HZ2  A LYS   A 1 31  ? 21.989 3.847   20.272  0.48 46.53 ?  31  LYS   A HZ2  1 
ATOM   899  H HZ2  B LYS   A 1 31  ? 21.826 3.769   20.581  0.52 45.63 ?  31  LYS   A HZ2  1 
ATOM   900  H HZ3  A LYS   A 1 31  ? 21.101 2.862   20.856  0.48 46.53 ?  31  LYS   A HZ3  1 
ATOM   901  H HZ3  B LYS   A 1 31  ? 20.919 2.711   20.977  0.52 45.63 ?  31  LYS   A HZ3  1 
ATOM   902  N N    . PRO   A 1 32  ? 22.913 -3.050  17.058  1.00 20.58 ?  32  PRO   A N    1 
ATOM   903  C CA   . PRO   A 1 32  ? 23.375 -4.397  16.735  1.00 20.83 ?  32  PRO   A CA   1 
ATOM   904  C C    . PRO   A 1 32  ? 24.872 -4.419  16.516  1.00 20.10 ?  32  PRO   A C    1 
ATOM   905  O O    . PRO   A 1 32  ? 25.518 -3.387  16.313  1.00 20.33 ?  32  PRO   A O    1 
ATOM   906  C CB   . PRO   A 1 32  ? 22.646 -4.700  15.424  1.00 20.64 ?  32  PRO   A CB   1 
ATOM   907  C CG   . PRO   A 1 32  ? 22.496 -3.362  14.783  1.00 19.07 ?  32  PRO   A CG   1 
ATOM   908  C CD   . PRO   A 1 32  ? 22.206 -2.432  15.927  1.00 19.37 ?  32  PRO   A CD   1 
ATOM   909  H HA   . PRO   A 1 32  ? 23.122 -5.032  17.423  1.00 25.01 ?  32  PRO   A HA   1 
ATOM   910  H HB2  . PRO   A 1 32  ? 23.183 -5.296  14.876  1.00 24.78 ?  32  PRO   A HB2  1 
ATOM   911  H HB3  . PRO   A 1 32  ? 21.779 -5.098  15.616  1.00 24.78 ?  32  PRO   A HB3  1 
ATOM   912  H HG2  . PRO   A 1 32  ? 23.321 -3.124  14.335  1.00 22.90 ?  32  PRO   A HG2  1 
ATOM   913  H HG3  . PRO   A 1 32  ? 21.755 -3.386  14.155  1.00 22.90 ?  32  PRO   A HG3  1 
ATOM   914  H HD2  . PRO   A 1 32  ? 22.566 -1.554  15.727  1.00 23.26 ?  32  PRO   A HD2  1 
ATOM   915  H HD3  . PRO   A 1 32  ? 21.255 -2.403  16.093  1.00 23.26 ?  32  PRO   A HD3  1 
ATOM   916  N N    . THR   A 1 33  ? 25.419 -5.633  16.536  1.00 20.13 ?  33  THR   A N    1 
ATOM   917  C CA   . THR   A 1 33  ? 26.831 -5.793  16.216  1.00 20.19 ?  33  THR   A CA   1 
ATOM   918  C C    . THR   A 1 33  ? 27.125 -5.335  14.796  1.00 18.41 ?  33  THR   A C    1 
ATOM   919  O O    . THR   A 1 33  ? 28.155 -4.696  14.547  1.00 18.47 ?  33  THR   A O    1 
ATOM   920  C CB   . THR   A 1 33  ? 27.245 -7.251  16.412  1.00 21.74 ?  33  THR   A CB   1 
ATOM   921  O OG1  . THR   A 1 33  ? 26.922 -7.658  17.745  1.00 23.84 ?  33  THR   A OG1  1 
ATOM   922  C CG2  . THR   A 1 33  ? 28.738 -7.422  16.181  1.00 22.21 ?  33  THR   A CG2  1 
ATOM   923  H H    . THR   A 1 33  ? 25.005 -6.363  16.724  1.00 24.16 ?  33  THR   A H    1 
ATOM   924  H HA   . THR   A 1 33  ? 27.358 -5.251  16.823  1.00 24.23 ?  33  THR   A HA   1 
ATOM   925  H HB   . THR   A 1 33  ? 26.774 -7.815  15.776  1.00 26.09 ?  33  THR   A HB   1 
ATOM   926  H HG1  . THR   A 1 33  ? 27.341 -7.186  18.299  1.00 28.62 ?  33  THR   A HG1  1 
ATOM   927  H HG21 . THR   A 1 33  ? 29.020 -8.310  16.452  1.00 26.66 ?  33  THR   A HG21 1 
ATOM   928  H HG22 . THR   A 1 33  ? 28.951 -7.299  15.242  1.00 26.66 ?  33  THR   A HG22 1 
ATOM   929  H HG23 . THR   A 1 33  ? 29.231 -6.766  16.702  1.00 26.66 ?  33  THR   A HG23 1 
ATOM   930  N N    . VAL   A 1 34  ? 26.229 -5.640  13.856  1.00 16.70 ?  34  VAL   A N    1 
ATOM   931  C CA   . VAL   A 1 34  ? 26.422 -5.318  12.446  1.00 15.13 ?  34  VAL   A CA   1 
ATOM   932  C C    . VAL   A 1 34  ? 25.125 -4.750  11.886  1.00 14.28 ?  34  VAL   A C    1 
ATOM   933  O O    . VAL   A 1 34  ? 24.076 -5.404  11.945  1.00 15.60 ?  34  VAL   A O    1 
ATOM   934  C CB   . VAL   A 1 34  ? 26.848 -6.539  11.609  1.00 15.66 ?  34  VAL   A CB   1 
ATOM   935  C CG1  . VAL   A 1 34  ? 26.978 -6.150  10.144  1.00 16.35 ?  34  VAL   A CG1  1 
ATOM   936  C CG2  . VAL   A 1 34  ? 28.135 -7.150  12.138  1.00 16.98 ?  34  VAL   A CG2  1 
ATOM   937  H H    . VAL   A 1 34  ? 25.481 -6.040  14.017  1.00 20.05 ?  34  VAL   A H    1 
ATOM   938  H HA   . VAL   A 1 34  ? 27.106 -4.640  12.355  1.00 18.16 ?  34  VAL   A HA   1 
ATOM   939  H HB   . VAL   A 1 34  ? 26.150 -7.216  11.675  1.00 18.80 ?  34  VAL   A HB   1 
ATOM   940  H HG11 . VAL   A 1 34  ? 27.489 -6.837  9.687   1.00 19.63 ?  34  VAL   A HG11 1 
ATOM   941  H HG12 . VAL   A 1 34  ? 26.087 -6.094  9.753   1.00 19.63 ?  34  VAL   A HG12 1 
ATOM   942  H HG13 . VAL   A 1 34  ? 27.425 -5.301  10.083  1.00 19.63 ?  34  VAL   A HG13 1 
ATOM   943  H HG21 . VAL   A 1 34  ? 28.377 -7.909  11.581  1.00 20.39 ?  34  VAL   A HG21 1 
ATOM   944  H HG22 . VAL   A 1 34  ? 28.835 -6.484  12.113  1.00 20.39 ?  34  VAL   A HG22 1 
ATOM   945  H HG23 . VAL   A 1 34  ? 27.991 -7.449  13.052  1.00 20.39 ?  34  VAL   A HG23 1 
ATOM   946  N N    . VAL   A 1 35  ? 25.197 -3.548  11.319  1.00 13.70 ?  35  VAL   A N    1 
ATOM   947  C CA   . VAL   A 1 35  ? 24.165 -3.031  10.432  1.00 13.10 ?  35  VAL   A CA   1 
ATOM   948  C C    . VAL   A 1 35  ? 24.718 -3.041  9.016   1.00 12.37 ?  35  VAL   A C    1 
ATOM   949  O O    . VAL   A 1 35  ? 25.868 -2.653  8.791   1.00 13.31 ?  35  VAL   A O    1 
ATOM   950  C CB   . VAL   A 1 35  ? 23.650 -1.632  10.842  1.00 14.11 ?  35  VAL   A CB   1 
ATOM   951  C CG1  . VAL   A 1 35  ? 24.725 -0.538  10.709  1.00 14.53 ?  35  VAL   A CG1  1 
ATOM   952  C CG2  . VAL   A 1 35  ? 22.414 -1.279  10.023  1.00 14.62 ?  35  VAL   A CG2  1 
ATOM   953  H H    . VAL   A 1 35  ? 25.845 -2.999  11.438  1.00 16.45 ?  35  VAL   A H    1 
ATOM   954  H HA   . VAL   A 1 35  ? 23.404 -3.639  10.447  1.00 15.73 ?  35  VAL   A HA   1 
ATOM   955  H HB   . VAL   A 1 35  ? 23.372 -1.671  11.770  1.00 16.94 ?  35  VAL   A HB   1 
ATOM   956  H HG11 . VAL   A 1 35  ? 24.372 0.291   11.069  1.00 17.45 ?  35  VAL   A HG11 1 
ATOM   957  H HG12 . VAL   A 1 35  ? 25.508 -0.811  11.202  1.00 17.45 ?  35  VAL   A HG12 1 
ATOM   958  H HG13 . VAL   A 1 35  ? 24.942 -0.423  9.770   1.00 17.45 ?  35  VAL   A HG13 1 
ATOM   959  H HG21 . VAL   A 1 35  ? 22.060 -0.433  10.333  1.00 17.55 ?  35  VAL   A HG21 1 
ATOM   960  H HG22 . VAL   A 1 35  ? 22.662 -1.213  9.087   1.00 17.55 ?  35  VAL   A HG22 1 
ATOM   961  H HG23 . VAL   A 1 35  ? 21.746 -1.978  10.135  1.00 17.55 ?  35  VAL   A HG23 1 
ATOM   962  N N    . VAL   A 1 36  ? 23.907 -3.486  8.064   1.00 11.81 ?  36  VAL   A N    1 
ATOM   963  C CA   . VAL   A 1 36  ? 24.289 -3.519  6.660   1.00 11.82 ?  36  VAL   A CA   1 
ATOM   964  C C    . VAL   A 1 36  ? 23.849 -2.227  5.987   1.00 11.74 ?  36  VAL   A C    1 
ATOM   965  O O    . VAL   A 1 36  ? 22.687 -1.811  6.113   1.00 12.76 ?  36  VAL   A O    1 
ATOM   966  C CB   . VAL   A 1 36  ? 23.667 -4.728  5.949   1.00 11.79 ?  36  VAL   A CB   1 
ATOM   967  C CG1  . VAL   A 1 36  ? 23.937 -4.656  4.457   1.00 12.75 ?  36  VAL   A CG1  1 
ATOM   968  C CG2  . VAL   A 1 36  ? 24.200 -6.021  6.532   1.00 12.90 ?  36  VAL   A CG2  1 
ATOM   969  H H    . VAL   A 1 36  ? 23.106 -3.776  8.202   1.00 14.17 ?  36  VAL   A H    1 
ATOM   970  H HA   . VAL   A 1 36  ? 25.256 -3.592  6.586   1.00 14.19 ?  36  VAL   A HA   1 
ATOM   971  H HB   . VAL   A 1 36  ? 22.706 -4.710  6.074   1.00 14.16 ?  36  VAL   A HB   1 
ATOM   972  H HG11 . VAL   A 1 36  ? 23.801 -5.536  4.068   1.00 15.30 ?  36  VAL   A HG11 1 
ATOM   973  H HG12 . VAL   A 1 36  ? 23.329 -4.021  4.049   1.00 15.30 ?  36  VAL   A HG12 1 
ATOM   974  H HG13 . VAL   A 1 36  ? 24.856 -4.376  4.314   1.00 15.30 ?  36  VAL   A HG13 1 
ATOM   975  H HG21 . VAL   A 1 36  ? 23.799 -6.772  6.059   1.00 15.49 ?  36  VAL   A HG21 1 
ATOM   976  H HG22 . VAL   A 1 36  ? 25.161 -6.045  6.434   1.00 15.49 ?  36  VAL   A HG22 1 
ATOM   977  H HG23 . VAL   A 1 36  ? 23.959 -6.065  7.473   1.00 15.49 ?  36  VAL   A HG23 1 
ATOM   978  N N    . ASN   A 1 37  ? 24.778 -1.598  5.267   1.00 11.14 ?  37  ASN   A N    1 
ATOM   979  C CA   . ASN   A 1 37  ? 24.470 -0.477  4.402   1.00 11.30 ?  37  ASN   A CA   1 
ATOM   980  C C    . ASN   A 1 37  ? 24.349 -0.944  2.964   1.00 11.10 ?  37  ASN   A C    1 
ATOM   981  O O    . ASN   A 1 37  ? 25.145 -1.766  2.496   1.00 11.76 ?  37  ASN   A O    1 
ATOM   982  C CB   . ASN   A 1 37  ? 25.546 0.596   4.501   1.00 11.39 ?  37  ASN   A CB   1 
ATOM   983  C CG   . ASN   A 1 37  ? 25.243 1.785   3.643   1.00 11.75 ?  37  ASN   A CG   1 
ATOM   984  O OD1  . ASN   A 1 37  ? 24.077 2.132   3.438   1.00 12.31 ?  37  ASN   A OD1  1 
ATOM   985  N ND2  . ASN   A 1 37  ? 26.288 2.431   3.141   1.00 12.13 ?  37  ASN   A ND2  1 
ATOM   986  H H    . ASN   A 1 37  ? 25.616 -1.803  5.277   1.00 13.38 ?  37  ASN   A H    1 
ATOM   987  H HA   . ASN   A 1 37  ? 23.629 -0.080  4.668   1.00 13.57 ?  37  ASN   A HA   1 
ATOM   988  H HB2  . ASN   A 1 37  ? 25.616 0.902   5.417   1.00 13.68 ?  37  ASN   A HB2  1 
ATOM   989  H HB3  . ASN   A 1 37  ? 26.398 0.227   4.207   1.00 13.68 ?  37  ASN   A HB3  1 
ATOM   990  H HD21 . ASN   A 1 37  ? 26.166 3.119   2.640   1.00 14.57 ?  37  ASN   A HD21 1 
ATOM   991  H HD22 . ASN   A 1 37  ? 27.079 2.160   3.306   1.00 14.57 ?  37  ASN   A HD22 1 
ATOM   992  N N    A ALA   A 1 38  ? 23.335 -0.409  2.281   0.48 11.20 ?  38  ALA   A N    1 
ATOM   993  N N    B ALA   A 1 38  ? 23.356 -0.409  2.251   0.52 11.43 ?  38  ALA   A N    1 
ATOM   994  C CA   A ALA   A 1 38  ? 23.153 -0.546  0.839   0.48 11.19 ?  38  ALA   A CA   1 
ATOM   995  C CA   B ALA   A 1 38  ? 23.205 -0.653  0.813   0.52 11.63 ?  38  ALA   A CA   1 
ATOM   996  C C    A ALA   A 1 38  ? 24.085 0.458   0.165   0.48 10.87 ?  38  ALA   A C    1 
ATOM   997  C C    B ALA   A 1 38  ? 24.032 0.382   0.044   0.52 11.63 ?  38  ALA   A C    1 
ATOM   998  O O    A ALA   A 1 38  ? 23.693 1.558   -0.232  0.48 10.95 ?  38  ALA   A O    1 
ATOM   999  O O    B ALA   A 1 38  ? 23.541 1.417   -0.417  0.52 11.78 ?  38  ALA   A O    1 
ATOM   1000 C CB   A ALA   A 1 38  ? 21.698 -0.291  0.464   0.48 12.08 ?  38  ALA   A CB   1 
ATOM   1001 C CB   B ALA   A 1 38  ? 21.735 -0.619  0.414   0.52 12.29 ?  38  ALA   A CB   1 
ATOM   1002 H H    A ALA   A 1 38  ? 22.729 0.077   2.645   0.48 13.45 ?  38  ALA   A H    1 
ATOM   1003 H H    B ALA   A 1 38  ? 22.752 0.105   2.585   0.52 13.73 ?  38  ALA   A H    1 
ATOM   1004 H HA   A ALA   A 1 38  ? 23.396 -1.437  0.557   0.48 13.44 ?  38  ALA   A HA   1 
ATOM   1005 H HA   B ALA   A 1 38  ? 23.551 -1.535  0.606   0.52 13.97 ?  38  ALA   A HA   1 
ATOM   1006 H HB1  A ALA   A 1 38  ? 21.591 -0.383  -0.497  0.48 14.50 ?  38  ALA   A HB1  1 
ATOM   1007 H HB1  B ALA   A 1 38  ? 21.666 -0.783  -0.540  0.52 14.75 ?  38  ALA   A HB1  1 
ATOM   1008 H HB2  A ALA   A 1 38  ? 21.138 -0.940  0.920   0.48 14.50 ?  38  ALA   A HB2  1 
ATOM   1009 H HB2  B ALA   A 1 38  ? 21.252 -1.304  0.903   0.52 14.75 ?  38  ALA   A HB2  1 
ATOM   1010 H HB3  A ALA   A 1 38  ? 21.448 0.608   0.737   0.48 14.50 ?  38  ALA   A HB3  1 
ATOM   1011 H HB3  B ALA   A 1 38  ? 21.370 0.256   0.624   0.52 14.75 ?  38  ALA   A HB3  1 
ATOM   1012 N N    A ALA   A 1 39  ? 25.352 0.069   0.057   0.48 10.88 ?  39  ALA   A N    1 
ATOM   1013 N N    B ALA   A 1 39  ? 25.317 0.073   -0.112  0.52 11.33 ?  39  ALA   A N    1 
ATOM   1014 C CA   A ALA   A 1 39  ? 26.406 0.928   -0.457  0.48 10.77 ?  39  ALA   A CA   1 
ATOM   1015 C CA   B ALA   A 1 39  ? 26.304 1.022   -0.600  0.52 11.73 ?  39  ALA   A CA   1 
ATOM   1016 C C    A ALA   A 1 39  ? 26.482 0.869   -1.977  0.48 10.46 ?  39  ALA   A C    1 
ATOM   1017 C C    B ALA   A 1 39  ? 26.489 0.919   -2.111  0.52 12.14 ?  39  ALA   A C    1 
ATOM   1018 O O    A ALA   A 1 39  ? 25.969 -0.053  -2.617  0.48 11.14 ?  39  ALA   A O    1 
ATOM   1019 O O    B ALA   A 1 39  ? 26.038 -0.023  -2.769  0.52 13.08 ?  39  ALA   A O    1 
ATOM   1020 C CB   A ALA   A 1 39  ? 27.752 0.500   0.132   0.48 11.27 ?  39  ALA   A CB   1 
ATOM   1021 C CB   B ALA   A 1 39  ? 27.639 0.772   0.103   0.52 13.15 ?  39  ALA   A CB   1 
ATOM   1022 H H    A ALA   A 1 39  ? 25.631 -0.711  0.282   0.48 13.06 ?  39  ALA   A H    1 
ATOM   1023 H H    B ALA   A 1 39  ? 25.643 -0.701  0.079   0.52 13.61 ?  39  ALA   A H    1 
ATOM   1024 H HA   A ALA   A 1 39  ? 26.232 1.846   -0.198  0.48 12.94 ?  39  ALA   A HA   1 
ATOM   1025 H HA   B ALA   A 1 39  ? 26.008 1.922   -0.375  0.52 14.08 ?  39  ALA   A HA   1 
ATOM   1026 H HB1  A ALA   A 1 39  ? 28.447 1.082   -0.215  0.48 13.54 ?  39  ALA   A HB1  1 
ATOM   1027 H HB1  B ALA   A 1 39  ? 28.288 1.410   -0.230  0.52 15.79 ?  39  ALA   A HB1  1 
ATOM   1028 H HB2  A ALA   A 1 39  ? 27.708 0.578   1.098   0.48 13.54 ?  39  ALA   A HB2  1 
ATOM   1029 H HB2  B ALA   A 1 39  ? 27.525 0.888   1.062   0.52 15.79 ?  39  ALA   A HB2  1 
ATOM   1030 H HB3  A ALA   A 1 39  ? 27.929 -0.417  -0.121  0.48 13.54 ?  39  ALA   A HB3  1 
ATOM   1031 H HB3  B ALA   A 1 39  ? 27.930 -0.132  -0.088  0.52 15.79 ?  39  ALA   A HB3  1 
ATOM   1032 N N    A ASN   A 1 40  ? 27.143 1.879   -2.550  0.48 11.09 ?  40  ASN   A N    1 
ATOM   1033 N N    B ASN   A 1 40  ? 27.167 1.923   -2.660  0.52 12.21 ?  40  ASN   A N    1 
ATOM   1034 C CA   A ASN   A 1 40  ? 27.654 1.820   -3.914  0.48 11.47 ?  40  ASN   A CA   1 
ATOM   1035 C CA   B ASN   A 1 40  ? 27.773 1.834   -3.980  0.52 12.22 ?  40  ASN   A CA   1 
ATOM   1036 C C    A ASN   A 1 40  ? 29.176 1.688   -3.886  0.48 11.36 ?  40  ASN   A C    1 
ATOM   1037 C C    B ASN   A 1 40  ? 29.286 1.677   -3.837  0.52 11.57 ?  40  ASN   A C    1 
ATOM   1038 O O    A ASN   A 1 40  ? 29.810 1.792   -2.834  0.48 11.74 ?  40  ASN   A O    1 
ATOM   1039 O O    B ASN   A 1 40  ? 29.842 1.772   -2.739  0.52 11.55 ?  40  ASN   A O    1 
ATOM   1040 C CB   A ASN   A 1 40  ? 27.191 3.017   -4.760  0.48 11.81 ?  40  ASN   A CB   1 
ATOM   1041 C CB   B ASN   A 1 40  ? 27.390 3.025   -4.872  0.52 12.61 ?  40  ASN   A CB   1 
ATOM   1042 C CG   A ASN   A 1 40  ? 27.561 4.352   -4.152  0.48 12.98 ?  40  ASN   A CG   1 
ATOM   1043 C CG   B ASN   A 1 40  ? 27.739 4.365   -4.258  0.52 13.14 ?  40  ASN   A CG   1 
ATOM   1044 O OD1  A ASN   A 1 40  ? 28.717 4.593   -3.799  0.48 13.14 ?  40  ASN   A OD1  1 
ATOM   1045 O OD1  B ASN   A 1 40  ? 28.901 4.639   -3.962  0.52 13.45 ?  40  ASN   A OD1  1 
ATOM   1046 N ND2  A ASN   A 1 40  ? 26.568 5.225   -4.014  0.48 13.76 ?  40  ASN   A ND2  1 
ATOM   1047 N ND2  B ASN   A 1 40  ? 26.731 5.215   -4.082  0.52 13.70 ?  40  ASN   A ND2  1 
ATOM   1048 H H    A ASN   A 1 40  ? 27.311 2.628   -2.160  0.48 13.31 ?  40  ASN   A H    1 
ATOM   1049 H H    B ASN   A 1 40  ? 27.284 2.679   -2.273  0.52 14.66 ?  40  ASN   A H    1 
ATOM   1050 H HA   A ASN   A 1 40  ? 27.302 1.020   -4.340  0.48 13.77 ?  40  ASN   A HA   1 
ATOM   1051 H HA   B ASN   A 1 40  ? 27.440 1.026   -4.409  0.52 14.67 ?  40  ASN   A HA   1 
ATOM   1052 H HB2  A ASN   A 1 40  ? 27.605 2.960   -5.642  0.48 14.18 ?  40  ASN   A HB2  1 
ATOM   1053 H HB2  B ASN   A 1 40  ? 27.865 2.945   -5.711  0.52 15.13 ?  40  ASN   A HB2  1 
ATOM   1054 H HB3  A ASN   A 1 40  ? 26.227 2.984   -4.855  0.48 14.18 ?  40  ASN   A HB3  1 
ATOM   1055 H HB3  B ASN   A 1 40  ? 26.433 3.002   -5.026  0.52 15.13 ?  40  ASN   A HB3  1 
ATOM   1056 H HD21 A ASN   A 1 40  ? 26.721 6.001   -3.679  0.48 16.52 ?  40  ASN   A HD21 1 
ATOM   1057 H HD21 B ASN   A 1 40  ? 26.879 5.990   -3.738  0.52 16.45 ?  40  ASN   A HD21 1 
ATOM   1058 H HD22 A ASN   A 1 40  ? 25.772 5.013   -4.265  0.48 16.52 ?  40  ASN   A HD22 1 
ATOM   1059 H HD22 B ASN   A 1 40  ? 25.932 4.991   -4.306  0.52 16.45 ?  40  ASN   A HD22 1 
ATOM   1060 N N    A VAL   A 1 41  ? 29.763 1.432   -5.061  0.48 11.73 ?  41  VAL   A N    1 
ATOM   1061 N N    B VAL   A 1 41  ? 29.949 1.400   -4.965  0.52 11.64 ?  41  VAL   A N    1 
ATOM   1062 C CA   A VAL   A 1 41  ? 31.190 1.103   -5.133  0.48 12.36 ?  41  VAL   A CA   1 
ATOM   1063 C CA   B VAL   A 1 41  ? 31.375 1.066   -4.932  0.52 11.55 ?  41  VAL   A CA   1 
ATOM   1064 C C    A VAL   A 1 41  ? 32.088 2.249   -4.693  0.48 11.55 ?  41  VAL   A C    1 
ATOM   1065 C C    B VAL   A 1 41  ? 32.217 2.216   -4.406  0.52 11.37 ?  41  VAL   A C    1 
ATOM   1066 O O    A VAL   A 1 41  ? 33.275 2.026   -4.420  0.48 10.65 ?  41  VAL   A O    1 
ATOM   1067 O O    B VAL   A 1 41  ? 33.299 1.988   -3.844  0.52 10.86 ?  41  VAL   A O    1 
ATOM   1068 C CB   A VAL   A 1 41  ? 31.619 0.636   -6.541  0.48 13.55 ?  41  VAL   A CB   1 
ATOM   1069 C CB   B VAL   A 1 41  ? 31.899 0.557   -6.296  0.52 11.86 ?  41  VAL   A CB   1 
ATOM   1070 C CG1  A VAL   A 1 41  ? 30.982 -0.700  -6.891  0.48 14.72 ?  41  VAL   A CG1  1 
ATOM   1071 C CG1  B VAL   A 1 41  ? 31.173 -0.711  -6.729  0.52 12.37 ?  41  VAL   A CG1  1 
ATOM   1072 C CG2  A VAL   A 1 41  ? 31.317 1.707   -7.594  0.48 13.91 ?  41  VAL   A CG2  1 
ATOM   1073 C CG2  B VAL   A 1 41  ? 31.819 1.636   -7.378  0.52 11.07 ?  41  VAL   A CG2  1 
ATOM   1074 H H    A VAL   A 1 41  ? 29.359 1.439   -5.821  0.48 14.08 ?  41  VAL   A H    1 
ATOM   1075 H H    B VAL   A 1 41  ? 29.597 1.393   -5.746  0.52 13.98 ?  41  VAL   A H    1 
ATOM   1076 H HA   A VAL   A 1 41  ? 31.346 0.359   -4.531  0.48 14.84 ?  41  VAL   A HA   1 
ATOM   1077 H HA   B VAL   A 1 41  ? 31.502 0.348   -4.306  0.52 13.87 ?  41  VAL   A HA   1 
ATOM   1078 H HB   A VAL   A 1 41  ? 32.582 0.508   -6.531  0.48 16.27 ?  41  VAL   A HB   1 
ATOM   1079 H HB   B VAL   A 1 41  ? 32.841 0.331   -6.194  0.52 14.24 ?  41  VAL   A HB   1 
ATOM   1080 H HG11 A VAL   A 1 41  ? 31.325 -0.995  -7.750  0.48 17.67 ?  41  VAL   A HG11 1 
ATOM   1081 H HG11 B VAL   A 1 41  ? 31.538 -1.015  -7.579  0.52 14.85 ?  41  VAL   A HG11 1 
ATOM   1082 H HG12 A VAL   A 1 41  ? 31.210 -1.347  -6.205  0.48 17.67 ?  41  VAL   A HG12 1 
ATOM   1083 H HG12 B VAL   A 1 41  ? 31.296 -1.395  -6.055  0.52 14.85 ?  41  VAL   A HG12 1 
ATOM   1084 H HG13 A VAL   A 1 41  ? 30.022 -0.589  -6.937  0.48 17.67 ?  41  VAL   A HG13 1 
ATOM   1085 H HG13 B VAL   A 1 41  ? 30.228 -0.512  -6.833  0.52 14.85 ?  41  VAL   A HG13 1 
ATOM   1086 H HG21 A VAL   A 1 41  ? 31.614 1.386   -8.461  0.48 16.70 ?  41  VAL   A HG21 1 
ATOM   1087 H HG21 B VAL   A 1 41  ? 32.036 1.242   -8.242  0.52 13.29 ?  41  VAL   A HG21 1 
ATOM   1088 H HG22 A VAL   A 1 41  ? 30.363 1.874   -7.614  0.48 16.70 ?  41  VAL   A HG22 1 
ATOM   1089 H HG22 B VAL   A 1 41  ? 30.922 1.999   -7.400  0.52 13.29 ?  41  VAL   A HG22 1 
ATOM   1090 H HG23 A VAL   A 1 41  ? 31.791 2.523   -7.367  0.48 16.70 ?  41  VAL   A HG23 1 
ATOM   1091 H HG23 B VAL   A 1 41  ? 32.456 2.344   -7.178  0.52 13.29 ?  41  VAL   A HG23 1 
ATOM   1092 N N    A TYR   A 1 42  ? 31.562 3.479   -4.653  0.48 12.17 ?  42  TYR   A N    1 
ATOM   1093 N N    B TYR   A 1 42  ? 31.755 3.459   -4.581  0.52 12.08 ?  42  TYR   A N    1 
ATOM   1094 C CA   A TYR   A 1 42  ? 32.317 4.662   -4.254  0.48 12.00 ?  42  TYR   A CA   1 
ATOM   1095 C CA   B TYR   A 1 42  ? 32.498 4.638   -4.154  0.52 12.23 ?  42  TYR   A CA   1 
ATOM   1096 C C    A TYR   A 1 42  ? 32.093 5.052   -2.802  0.48 12.01 ?  42  TYR   A C    1 
ATOM   1097 C C    B TYR   A 1 42  ? 32.196 5.010   -2.716  0.52 12.07 ?  42  TYR   A C    1 
ATOM   1098 O O    A TYR   A 1 42  ? 32.634 6.071   -2.357  0.48 12.26 ?  42  TYR   A O    1 
ATOM   1099 O O    B TYR   A 1 42  ? 32.781 5.969   -2.196  0.52 12.61 ?  42  TYR   A O    1 
ATOM   1100 C CB   A TYR   A 1 42  ? 31.950 5.842   -5.158  0.48 12.82 ?  42  TYR   A CB   1 
ATOM   1101 C CB   B TYR   A 1 42  ? 32.209 5.825   -5.088  0.52 12.70 ?  42  TYR   A CB   1 
ATOM   1102 C CG   A TYR   A 1 42  ? 32.103 5.533   -6.628  0.48 13.04 ?  42  TYR   A CG   1 
ATOM   1103 C CG   B TYR   A 1 42  ? 32.421 5.485   -6.547  0.52 13.12 ?  42  TYR   A CG   1 
ATOM   1104 C CD1  A TYR   A 1 42  ? 33.356 5.343   -7.186  0.48 13.41 ?  42  TYR   A CD1  1 
ATOM   1105 C CD1  B TYR   A 1 42  ? 33.698 5.272   -7.049  0.52 14.01 ?  42  TYR   A CD1  1 
ATOM   1106 C CD2  A TYR   A 1 42  ? 30.991 5.420   -7.455  0.48 14.61 ?  42  TYR   A CD2  1 
ATOM   1107 C CD2  B TYR   A 1 42  ? 31.346 5.346   -7.416  0.52 13.70 ?  42  TYR   A CD2  1 
ATOM   1108 C CE1  A TYR   A 1 42  ? 33.505 5.051   -8.529  0.48 13.79 ?  42  TYR   A CE1  1 
ATOM   1109 C CE1  B TYR   A 1 42  ? 33.897 4.942   -8.379  0.52 14.30 ?  42  TYR   A CE1  1 
ATOM   1110 C CE2  A TYR   A 1 42  ? 31.128 5.135   -8.801  0.48 15.41 ?  42  TYR   A CE2  1 
ATOM   1111 C CE2  B TYR   A 1 42  ? 31.537 5.019   -8.745  0.52 14.65 ?  42  TYR   A CE2  1 
ATOM   1112 C CZ   A TYR   A 1 42  ? 32.389 4.946   -9.333  0.48 14.97 ?  42  TYR   A CZ   1 
ATOM   1113 C CZ   B TYR   A 1 42  ? 32.814 4.818   -9.221  0.52 14.59 ?  42  TYR   A CZ   1 
ATOM   1114 O OH   A TYR   A 1 42  ? 32.542 4.662   -10.671 0.48 16.16 ?  42  TYR   A OH   1 
ATOM   1115 O OH   B TYR   A 1 42  ? 33.000 4.488   -10.541 0.52 15.75 ?  42  TYR   A OH   1 
ATOM   1116 H H    A TYR   A 1 42  ? 30.748 3.652   -4.877  0.48 14.61 ?  42  TYR   A H    1 
ATOM   1117 H H    B TYR   A 1 42  ? 30.989 3.643   -4.930  0.52 14.50 ?  42  TYR   A H    1 
ATOM   1118 H HA   A TYR   A 1 42  ? 33.259 4.481   -4.371  0.48 14.40 ?  42  TYR   A HA   1 
ATOM   1119 H HA   B TYR   A 1 42  ? 33.446 4.449   -4.217  0.52 14.69 ?  42  TYR   A HA   1 
ATOM   1120 H HB2  A TYR   A 1 42  ? 31.022 6.086   -4.997  0.48 15.39 ?  42  TYR   A HB2  1 
ATOM   1121 H HB2  B TYR   A 1 42  ? 31.287 6.103   -4.976  0.52 15.24 ?  42  TYR   A HB2  1 
ATOM   1122 H HB3  A TYR   A 1 42  ? 32.527 6.591   -4.947  0.48 15.39 ?  42  TYR   A HB3  1 
ATOM   1123 H HB3  B TYR   A 1 42  ? 32.804 6.560   -4.861  0.52 15.24 ?  42  TYR   A HB3  1 
ATOM   1124 H HD1  A TYR   A 1 42  ? 34.111 5.412   -6.644  0.48 16.10 ?  42  TYR   A HD1  1 
ATOM   1125 H HD1  B TYR   A 1 42  ? 34.434 5.355   -6.484  0.52 16.82 ?  42  TYR   A HD1  1 
ATOM   1126 H HD2  A TYR   A 1 42  ? 30.138 5.546   -7.095  0.48 17.53 ?  42  TYR   A HD2  1 
ATOM   1127 H HD2  B TYR   A 1 42  ? 30.484 5.484   -7.099  0.52 16.45 ?  42  TYR   A HD2  1 
ATOM   1128 H HE1  A TYR   A 1 42  ? 34.354 4.930   -8.884  0.48 16.55 ?  42  TYR   A HE1  1 
ATOM   1129 H HE1  B TYR   A 1 42  ? 34.762 4.808   -8.704  0.52 17.17 ?  42  TYR   A HE1  1 
ATOM   1130 H HE2  A TYR   A 1 42  ? 30.374 5.063   -9.341  0.48 18.50 ?  42  TYR   A HE2  1 
ATOM   1131 H HE2  B TYR   A 1 42  ? 30.808 4.938   -9.318  0.52 17.58 ?  42  TYR   A HE2  1 
ATOM   1132 H HH   A TYR   A 1 42  ? 31.793 4.626   -11.041 0.48 19.40 ?  42  TYR   A HH   1 
ATOM   1133 H HH   B TYR   A 1 42  ? 33.813 4.331   -10.688 0.52 18.90 ?  42  TYR   A HH   1 
ATOM   1134 N N    . LEU   A 1 43  ? 31.284 4.285   -2.072  1.00 11.89 ?  43  LEU   A N    1 
ATOM   1135 C CA   . LEU   A 1 43  ? 30.845 4.627   -0.724  1.00 11.88 ?  43  LEU   A CA   1 
ATOM   1136 C C    . LEU   A 1 43  ? 30.372 6.078   -0.637  1.00 11.96 ?  43  LEU   A C    1 
ATOM   1137 O O    . LEU   A 1 43  ? 30.634 6.783   0.340   1.00 13.20 ?  43  LEU   A O    1 
ATOM   1138 C CB   . LEU   A 1 43  ? 31.889 4.311   0.347   1.00 12.29 ?  43  LEU   A CB   1 
ATOM   1139 C CG   . LEU   A 1 43  ? 32.381 2.858   0.429   1.00 12.73 ?  43  LEU   A CG   1 
ATOM   1140 C CD1  . LEU   A 1 43  ? 33.423 2.735   1.526   1.00 13.99 ?  43  LEU   A CD1  1 
ATOM   1141 C CD2  . LEU   A 1 43  ? 31.246 1.879   0.679   1.00 13.40 ?  43  LEU   A CD2  1 
ATOM   1142 H H    A LEU   A 1 43  ? 30.964 3.534   -2.345  0.48 14.28 ?  43  LEU   A H    1 
ATOM   1143 H H    B LEU   A 1 43  ? 30.901 3.583   -2.391  0.52 14.28 ?  43  LEU   A H    1 
ATOM   1144 H HA   . LEU   A 1 43  ? 30.071 4.075   -0.521  1.00 14.26 ?  43  LEU   A HA   1 
ATOM   1145 H HB2  . LEU   A 1 43  ? 32.662 4.874   0.195   1.00 14.75 ?  43  LEU   A HB2  1 
ATOM   1146 H HB3  . LEU   A 1 43  ? 31.503 4.528   1.215   1.00 14.75 ?  43  LEU   A HB3  1 
ATOM   1147 H HG   . LEU   A 1 43  ? 32.806 2.625   -0.410  1.00 15.28 ?  43  LEU   A HG   1 
ATOM   1148 H HD11 . LEU   A 1 43  ? 33.731 1.815   1.568   1.00 16.80 ?  43  LEU   A HD11 1 
ATOM   1149 H HD12 . LEU   A 1 43  ? 34.168 3.323   1.328   1.00 16.80 ?  43  LEU   A HD12 1 
ATOM   1150 H HD13 . LEU   A 1 43  ? 33.022 2.985   2.375   1.00 16.80 ?  43  LEU   A HD13 1 
ATOM   1151 H HD21 . LEU   A 1 43  ? 31.620 0.993   0.801   1.00 16.08 ?  43  LEU   A HD21 1 
ATOM   1152 H HD22 . LEU   A 1 43  ? 30.767 2.152   1.475   1.00 16.08 ?  43  LEU   A HD22 1 
ATOM   1153 H HD23 . LEU   A 1 43  ? 30.654 1.888   -0.088  1.00 16.08 ?  43  LEU   A HD23 1 
ATOM   1154 N N    A LYS   A 1 44  ? 29.653 6.518   -1.670  0.48 12.14 ?  44  LYS   A N    1 
ATOM   1155 N N    B LYS   A 1 44  ? 29.657 6.526   -1.666  0.52 11.99 ?  44  LYS   A N    1 
ATOM   1156 C CA   A LYS   A 1 44  ? 29.004 7.824   -1.673  0.48 12.75 ?  44  LYS   A CA   1 
ATOM   1157 C CA   B LYS   A 1 44  ? 29.045 7.849   -1.661  0.52 12.51 ?  44  LYS   A CA   1 
ATOM   1158 C C    A LYS   A 1 44  ? 27.574 7.625   -1.191  0.48 12.05 ?  44  LYS   A C    1 
ATOM   1159 C C    B LYS   A 1 44  ? 27.621 7.702   -1.149  0.52 11.57 ?  44  LYS   A C    1 
ATOM   1160 O O    A LYS   A 1 44  ? 26.729 7.092   -1.921  0.48 13.20 ?  44  LYS   A O    1 
ATOM   1161 O O    B LYS   A 1 44  ? 26.743 7.189   -1.854  0.52 12.90 ?  44  LYS   A O    1 
ATOM   1162 C CB   A LYS   A 1 44  ? 29.042 8.442   -3.067  0.48 14.70 ?  44  LYS   A CB   1 
ATOM   1163 C CB   B LYS   A 1 44  ? 29.102 8.480   -3.049  0.52 14.53 ?  44  LYS   A CB   1 
ATOM   1164 C CG   A LYS   A 1 44  ? 30.425 8.902   -3.506  0.48 17.59 ?  44  LYS   A CG   1 
ATOM   1165 C CG   B LYS   A 1 44  ? 30.495 8.958   -3.446  0.52 17.55 ?  44  LYS   A CG   1 
ATOM   1166 C CD   A LYS   A 1 44  ? 31.064 9.864   -2.508  0.48 21.36 ?  44  LYS   A CD   1 
ATOM   1167 C CD   B LYS   A 1 44  ? 31.125 9.856   -2.380  0.52 21.33 ?  44  LYS   A CD   1 
ATOM   1168 C CE   A LYS   A 1 44  ? 32.392 10.389  -3.024  0.48 23.88 ?  44  LYS   A CE   1 
ATOM   1169 C CE   B LYS   A 1 44  ? 32.529 10.271  -2.758  0.52 23.74 ?  44  LYS   A CE   1 
ATOM   1170 N NZ   A LYS   A 1 44  ? 33.181 11.069  -1.960  0.48 25.41 ?  44  LYS   A NZ   1 
ATOM   1171 N NZ   B LYS   A 1 44  ? 33.297 10.744  -1.574  0.52 24.36 ?  44  LYS   A NZ   1 
ATOM   1172 H H    A LYS   A 1 44  ? 29.522 6.061   -2.388  0.48 14.57 ?  44  LYS   A H    1 
ATOM   1173 H H    B LYS   A 1 44  ? 29.511 6.076   -2.384  0.52 14.40 ?  44  LYS   A H    1 
ATOM   1174 H HA   A LYS   A 1 44  ? 29.446 8.413   -1.047  0.48 15.30 ?  44  LYS   A HA   1 
ATOM   1175 H HA   B LYS   A 1 44  ? 29.505 8.413   -1.025  0.52 15.02 ?  44  LYS   A HA   1 
ATOM   1176 H HB2  A LYS   A 1 44  ? 28.731 7.781   -3.706  0.48 17.64 ?  44  LYS   A HB2  1 
ATOM   1177 H HB2  B LYS   A 1 44  ? 28.812 7.823   -3.703  0.52 17.45 ?  44  LYS   A HB2  1 
ATOM   1178 H HB3  A LYS   A 1 44  ? 28.452 9.212   -3.080  0.48 17.64 ?  44  LYS   A HB3  1 
ATOM   1179 H HB3  B LYS   A 1 44  ? 28.506 9.247   -3.069  0.52 17.45 ?  44  LYS   A HB3  1 
ATOM   1180 H HG2  A LYS   A 1 44  ? 31.004 8.131   -3.597  0.48 21.12 ?  44  LYS   A HG2  1 
ATOM   1181 H HG2  B LYS   A 1 44  ? 31.068 8.188   -3.575  0.52 21.07 ?  44  LYS   A HG2  1 
ATOM   1182 H HG3  A LYS   A 1 44  ? 30.348 9.363   -4.359  0.48 21.12 ?  44  LYS   A HG3  1 
ATOM   1183 H HG3  B LYS   A 1 44  ? 30.430 9.468   -4.271  0.52 21.07 ?  44  LYS   A HG3  1 
ATOM   1184 H HD2  A LYS   A 1 44  ? 30.466 10.614  -2.359  0.48 25.65 ?  44  LYS   A HD2  1 
ATOM   1185 H HD2  B LYS   A 1 44  ? 30.572 10.647  -2.268  0.52 25.60 ?  44  LYS   A HD2  1 
ATOM   1186 H HD3  A LYS   A 1 44  ? 31.230 9.396   -1.673  0.48 25.65 ?  44  LYS   A HD3  1 
ATOM   1187 H HD3  B LYS   A 1 44  ? 31.189 9.371   -1.543  0.52 25.60 ?  44  LYS   A HD3  1 
ATOM   1188 H HE2  A LYS   A 1 44  ? 32.916 9.642   -3.358  0.48 28.66 ?  44  LYS   A HE2  1 
ATOM   1189 H HE2  B LYS   A 1 44  ? 32.994 9.509   -3.137  0.52 28.50 ?  44  LYS   A HE2  1 
ATOM   1190 H HE3  A LYS   A 1 44  ? 32.226 11.024  -3.734  0.48 28.66 ?  44  LYS   A HE3  1 
ATOM   1191 H HE3  B LYS   A 1 44  ? 32.483 10.992  -3.402  0.52 28.50 ?  44  LYS   A HE3  1 
ATOM   1192 H HZ1  A LYS   A 1 44  ? 33.951 11.362  -2.295  0.48 30.50 ?  44  LYS   A HZ1  1 
ATOM   1193 H HZ1  B LYS   A 1 44  ? 34.116 10.985  -1.821  0.52 29.24 ?  44  LYS   A HZ1  1 
ATOM   1194 H HZ2  A LYS   A 1 44  ? 32.723 11.760  -1.638  0.48 30.50 ?  44  LYS   A HZ2  1 
ATOM   1195 H HZ2  B LYS   A 1 44  ? 32.887 11.448  -1.209  0.52 29.24 ?  44  LYS   A HZ2  1 
ATOM   1196 H HZ3  A LYS   A 1 44  ? 33.352 10.500  -1.296  0.48 30.50 ?  44  LYS   A HZ3  1 
ATOM   1197 H HZ3  B LYS   A 1 44  ? 33.353 10.097  -0.967  0.52 29.24 ?  44  LYS   A HZ3  1 
ATOM   1198 N N    A HIS   A 1 45  ? 27.311 8.033   0.047   0.48 12.00 ?  45  HIS   A N    1 
ATOM   1199 N N    B HIS   A 1 45  ? 27.401 8.130   0.088   0.52 11.79 ?  45  HIS   A N    1 
ATOM   1200 C CA   A HIS   A 1 45  ? 26.063 7.693   0.732   0.48 12.16 ?  45  HIS   A CA   1 
ATOM   1201 C CA   B HIS   A 1 45  ? 26.158 7.841   0.798   0.52 12.47 ?  45  HIS   A CA   1 
ATOM   1202 C C    A HIS   A 1 45  ? 25.041 8.815   0.545   0.48 12.36 ?  45  HIS   A C    1 
ATOM   1203 C C    B HIS   A 1 45  ? 25.200 9.024   0.678   0.52 13.85 ?  45  HIS   A C    1 
ATOM   1204 O O    A HIS   A 1 45  ? 24.734 9.585   1.454   0.48 14.12 ?  45  HIS   A O    1 
ATOM   1205 O O    B HIS   A 1 45  ? 24.931 9.743   1.640   0.52 15.61 ?  45  HIS   A O    1 
ATOM   1206 C CB   A HIS   A 1 45  ? 26.339 7.431   2.206   0.48 12.28 ?  45  HIS   A CB   1 
ATOM   1207 C CB   B HIS   A 1 45  ? 26.453 7.549   2.261   0.52 11.80 ?  45  HIS   A CB   1 
ATOM   1208 C CG   A HIS   A 1 45  ? 27.461 6.473   2.448   0.48 11.86 ?  45  HIS   A CG   1 
ATOM   1209 C CG   B HIS   A 1 45  ? 27.541 6.550   2.475   0.52 11.89 ?  45  HIS   A CG   1 
ATOM   1210 N ND1  A HIS   A 1 45  ? 27.462 5.183   1.959   0.48 12.41 ?  45  HIS   A ND1  1 
ATOM   1211 N ND1  B HIS   A 1 45  ? 27.504 5.276   1.948   0.52 12.23 ?  45  HIS   A ND1  1 
ATOM   1212 C CD2  A HIS   A 1 45  ? 28.624 6.625   3.125   0.48 12.27 ?  45  HIS   A CD2  1 
ATOM   1213 C CD2  B HIS   A 1 45  ? 28.699 6.643   3.171   0.52 12.19 ?  45  HIS   A CD2  1 
ATOM   1214 C CE1  A HIS   A 1 45  ? 28.579 4.583   2.331   0.48 12.39 ?  45  HIS   A CE1  1 
ATOM   1215 C CE1  B HIS   A 1 45  ? 28.598 4.630   2.313   0.52 11.98 ?  45  HIS   A CE1  1 
ATOM   1216 N NE2  A HIS   A 1 45  ? 29.299 5.433   3.043   0.48 12.65 ?  45  HIS   A NE2  1 
ATOM   1217 N NE2  B HIS   A 1 45  ? 29.335 5.433   3.059   0.52 12.26 ?  45  HIS   A NE2  1 
ATOM   1218 H H    A HIS   A 1 45  ? 27.841 8.515   0.522   0.48 14.41 ?  45  HIS   A H    1 
ATOM   1219 H H    B HIS   A 1 45  ? 27.961 8.600   0.545   0.52 14.15 ?  45  HIS   A H    1 
ATOM   1220 H HA   A HIS   A 1 45  ? 25.696 6.881   0.349   0.48 14.59 ?  45  HIS   A HA   1 
ATOM   1221 H HA   B HIS   A 1 45  ? 25.732 7.067   0.403   0.52 14.98 ?  45  HIS   A HA   1 
ATOM   1222 H HB2  A HIS   A 1 45  ? 26.564 8.270   2.638   0.48 14.75 ?  45  HIS   A HB2  1 
ATOM   1223 H HB2  B HIS   A 1 45  ? 26.712 8.375   2.698   0.52 14.17 ?  45  HIS   A HB2  1 
ATOM   1224 H HB3  A HIS   A 1 45  ? 25.539 7.058   2.615   0.48 14.75 ?  45  HIS   A HB3  1 
ATOM   1225 H HB3  B HIS   A 1 45  ? 25.642 7.203   2.675   0.52 14.17 ?  45  HIS   A HB3  1 
ATOM   1226 H HD2  A HIS   A 1 45  ? 28.916 7.392   3.565   0.48 14.74 ?  45  HIS   A HD2  1 
ATOM   1227 H HD2  B HIS   A 1 45  ? 29.008 7.390   3.637   0.52 14.64 ?  45  HIS   A HD2  1 
ATOM   1228 H HE1  A HIS   A 1 45  ? 28.815 3.702   2.137   0.48 14.88 ?  45  HIS   A HE1  1 
ATOM   1229 H HE1  B HIS   A 1 45  ? 28.806 3.748   2.101   0.52 14.39 ?  45  HIS   A HE1  1 
ATOM   1230 H HE2  A HIS   A 1 45  ? 30.072 5.267   3.390   0.48 15.19 ?  45  HIS   A HE2  1 
ATOM   1231 H HE2  B HIS   A 1 45  ? 30.098 5.234   3.410   0.52 14.72 ?  45  HIS   A HE2  1 
ATOM   1232 N N    A GLY   A 1 46  ? 24.487 8.875   -0.663  0.48 13.14 ?  46  GLY   A N    1 
ATOM   1233 N N    B GLY   A 1 46  ? 24.686 9.220   -0.530  0.52 14.31 ?  46  GLY   A N    1 
ATOM   1234 C CA   A GLY   A 1 46  ? 23.676 10.012  -1.056  0.48 14.07 ?  46  GLY   A CA   1 
ATOM   1235 C CA   B GLY   A 1 46  ? 23.869 10.387  -0.798  0.52 14.37 ?  46  GLY   A CA   1 
ATOM   1236 C C    A GLY   A 1 46  ? 22.183 9.896   -0.824  0.48 14.43 ?  46  GLY   A C    1 
ATOM   1237 C C    B GLY   A 1 46  ? 22.386 10.205  -0.536  0.52 14.10 ?  46  GLY   A C    1 
ATOM   1238 O O    A GLY   A 1 46  ? 21.510 10.908  -0.593  0.48 15.22 ?  46  GLY   A O    1 
ATOM   1239 O O    B GLY   A 1 46  ? 21.714 11.137  -0.077  0.52 14.83 ?  46  GLY   A O    1 
ATOM   1240 H H    A GLY   A 1 46  ? 24.568 8.269   -1.267  0.48 15.77 ?  46  GLY   A H    1 
ATOM   1241 H H    B GLY   A 1 46  ? 24.799 8.699   -1.207  0.52 17.19 ?  46  GLY   A H    1 
ATOM   1242 H HA2  A GLY   A 1 46  ? 23.987 10.793  -0.575  0.48 16.89 ?  46  GLY   A HA2  1 
ATOM   1243 H HA2  B GLY   A 1 46  ? 24.176 11.123  -0.244  0.52 17.25 ?  46  GLY   A HA2  1 
ATOM   1244 H HA3  A GLY   A 1 46  ? 23.803 10.169  -2.000  0.48 16.89 ?  46  GLY   A HA3  1 
ATOM   1245 H HA3  B GLY   A 1 46  ? 23.985 10.648  -1.725  0.52 17.25 ?  46  GLY   A HA3  1 
ATOM   1246 N N    A GLY   A 1 47  ? 21.641 8.685   -0.905  0.48 14.17 ?  47  GLY   A N    1 
ATOM   1247 N N    B GLY   A 1 47  ? 21.856 9.020   -0.839  0.52 13.60 ?  47  GLY   A N    1 
ATOM   1248 C CA   A GLY   A 1 47  ? 20.204 8.521   -0.833  0.48 14.78 ?  47  GLY   A CA   1 
ATOM   1249 C CA   B GLY   A 1 47  ? 20.429 8.785   -0.781  0.52 14.23 ?  47  GLY   A CA   1 
ATOM   1250 C C    A GLY   A 1 47  ? 19.847 7.103   -0.455  0.48 13.98 ?  47  GLY   A C    1 
ATOM   1251 C C    B GLY   A 1 47  ? 20.111 7.375   -0.316  0.52 13.87 ?  47  GLY   A C    1 
ATOM   1252 O O    A GLY   A 1 47  ? 20.716 6.257   -0.226  0.48 13.40 ?  47  GLY   A O    1 
ATOM   1253 O O    B GLY   A 1 47  ? 21.004 6.568   -0.051  0.52 14.17 ?  47  GLY   A O    1 
ATOM   1254 H H    A GLY   A 1 47  ? 22.078 7.947   -1.002  0.48 17.01 ?  47  GLY   A H    1 
ATOM   1255 H H    B GLY   A 1 47  ? 22.313 8.338   -1.088  0.52 16.33 ?  47  GLY   A H    1 
ATOM   1256 H HA2  A GLY   A 1 47  ? 19.831 9.129   -0.175  0.48 17.75 ?  47  GLY   A HA2  1 
ATOM   1257 H HA2  B GLY   A 1 47  ? 20.018 9.415   -0.170  0.52 17.08 ?  47  GLY   A HA2  1 
ATOM   1258 H HA3  A GLY   A 1 47  ? 19.807 8.715   -1.697  0.48 17.75 ?  47  GLY   A HA3  1 
ATOM   1259 H HA3  B GLY   A 1 47  ? 20.041 8.921   -1.667  0.52 17.08 ?  47  GLY   A HA3  1 
ATOM   1260 N N    A GLY   A 1 48  ? 18.546 6.841   -0.401  0.48 14.33 ?  48  GLY   A N    1 
ATOM   1261 N N    B GLY   A 1 48  ? 18.816 7.096   -0.216  0.52 14.38 ?  48  GLY   A N    1 
ATOM   1262 C CA   A GLY   A 1 48  ? 18.140 5.506   -0.028  0.48 14.83 ?  48  GLY   A CA   1 
ATOM   1263 C CA   B GLY   A 1 48  ? 18.366 5.779   0.184   0.52 14.54 ?  48  GLY   A CA   1 
ATOM   1264 C C    A GLY   A 1 48  ? 18.598 5.185   1.380   0.48 14.18 ?  48  GLY   A C    1 
ATOM   1265 C C    B GLY   A 1 48  ? 18.818 5.411   1.587   0.52 13.64 ?  48  GLY   A C    1 
ATOM   1266 O O    A GLY   A 1 48  ? 18.732 6.064   2.241   0.48 14.11 ?  48  GLY   A O    1 
ATOM   1267 O O    B GLY   A 1 48  ? 19.017 6.263   2.464   0.52 13.03 ?  48  GLY   A O    1 
ATOM   1268 H H    A GLY   A 1 48  ? 17.905 7.394   -0.565  0.48 17.20 ?  48  GLY   A H    1 
ATOM   1269 H H    B GLY   A 1 48  ? 18.189 7.652   -0.382  0.52 17.27 ?  48  GLY   A H    1 
ATOM   1270 H HA2  A GLY   A 1 48  ? 17.179 5.423   -0.074  0.48 17.81 ?  48  GLY   A HA2  1 
ATOM   1271 H HA2  B GLY   A 1 48  ? 17.400 5.749   0.150   0.52 17.45 ?  48  GLY   A HA2  1 
ATOM   1272 H HA3  A GLY   A 1 48  ? 18.542 4.862   -0.634  0.48 17.81 ?  48  GLY   A HA3  1 
ATOM   1273 H HA3  B GLY   A 1 48  ? 18.714 5.115   -0.441  0.52 17.45 ?  48  GLY   A HA3  1 
ATOM   1274 N N    A VAL   A 1 49  ? 18.865 3.901   1.616   0.48 13.95 ?  49  VAL   A N    1 
ATOM   1275 N N    B VAL   A 1 49  ? 18.963 4.100   1.799   0.52 12.34 ?  49  VAL   A N    1 
ATOM   1276 C CA   A VAL   A 1 49  ? 19.319 3.483   2.936   0.48 13.76 ?  49  VAL   A CA   1 
ATOM   1277 C CA   B VAL   A 1 49  ? 19.464 3.577   3.069   0.52 12.03 ?  49  VAL   A CA   1 
ATOM   1278 C C    A VAL   A 1 49  ? 20.644 4.148   3.287   0.48 12.33 ?  49  VAL   A C    1 
ATOM   1279 C C    B VAL   A 1 49  ? 20.785 4.239   3.442   0.52 10.68 ?  49  VAL   A C    1 
ATOM   1280 O O    A VAL   A 1 49  ? 20.848 4.586   4.423   0.48 12.44 ?  49  VAL   A O    1 
ATOM   1281 O O    B VAL   A 1 49  ? 20.995 4.638   4.594   0.52 11.56 ?  49  VAL   A O    1 
ATOM   1282 C CB   A VAL   A 1 49  ? 19.416 1.948   3.002   0.48 14.72 ?  49  VAL   A CB   1 
ATOM   1283 C CB   B VAL   A 1 49  ? 19.605 2.045   2.985   0.52 12.63 ?  49  VAL   A CB   1 
ATOM   1284 C CG1  A VAL   A 1 49  ? 20.097 1.522   4.286   0.48 14.96 ?  49  VAL   A CG1  1 
ATOM   1285 C CG1  B VAL   A 1 49  ? 20.442 1.506   4.142   0.52 12.12 ?  49  VAL   A CG1  1 
ATOM   1286 C CG2  A VAL   A 1 49  ? 18.028 1.329   2.894   0.48 16.04 ?  49  VAL   A CG2  1 
ATOM   1287 C CG2  B VAL   A 1 49  ? 18.229 1.375   2.946   0.52 14.53 ?  49  VAL   A CG2  1 
ATOM   1288 H H    A VAL   A 1 49  ? 18.801 3.261   1.038   0.48 16.75 ?  49  VAL   A H    1 
ATOM   1289 H H    B VAL   A 1 49  ? 18.782 3.492   1.221   0.52 14.82 ?  49  VAL   A H    1 
ATOM   1290 H HA   A VAL   A 1 49  ? 18.657 3.758   3.593   0.48 16.52 ?  49  VAL   A HA   1 
ATOM   1291 H HA   B VAL   A 1 49  ? 18.827 3.780   3.770   0.52 14.45 ?  49  VAL   A HA   1 
ATOM   1292 H HB   A VAL   A 1 49  ? 19.951 1.629   2.257   0.48 17.68 ?  49  VAL   A HB   1 
ATOM   1293 H HB   B VAL   A 1 49  ? 20.066 1.818   2.163   0.52 15.17 ?  49  VAL   A HB   1 
ATOM   1294 H HG11 A VAL   A 1 49  ? 19.899 0.589   4.451   0.48 17.96 ?  49  VAL   A HG11 1 
ATOM   1295 H HG11 B VAL   A 1 49  ? 20.277 0.555   4.232   0.52 14.56 ?  49  VAL   A HG11 1 
ATOM   1296 H HG12 A VAL   A 1 49  ? 21.053 1.648   4.197   0.48 17.96 ?  49  VAL   A HG12 1 
ATOM   1297 H HG12 B VAL   A 1 49  ? 21.380 1.662   3.956   0.52 14.56 ?  49  VAL   A HG12 1 
ATOM   1298 H HG13 A VAL   A 1 49  ? 19.755 2.065   5.015   0.48 17.96 ?  49  VAL   A HG13 1 
ATOM   1299 H HG13 B VAL   A 1 49  ? 20.182 1.963   4.958   0.52 14.56 ?  49  VAL   A HG13 1 
ATOM   1300 H HG21 A VAL   A 1 49  ? 18.108 0.364   2.945   0.48 19.25 ?  49  VAL   A HG21 1 
ATOM   1301 H HG21 B VAL   A 1 49  ? 18.343 0.413   2.886   0.52 17.44 ?  49  VAL   A HG21 1 
ATOM   1302 H HG22 A VAL   A 1 49  ? 17.481 1.656   3.625   0.48 19.25 ?  49  VAL   A HG22 1 
ATOM   1303 H HG22 B VAL   A 1 49  ? 17.743 1.599   3.756   0.52 17.44 ?  49  VAL   A HG22 1 
ATOM   1304 H HG23 A VAL   A 1 49  ? 17.635 1.584   2.045   0.48 19.25 ?  49  VAL   A HG23 1 
ATOM   1305 H HG23 B VAL   A 1 49  ? 17.741 1.698   2.171   0.52 17.44 ?  49  VAL   A HG23 1 
ATOM   1306 N N    A ALA   A 1 50  ? 21.571 4.208   2.329   0.48 11.66 ?  50  ALA   A N    1 
ATOM   1307 N N    B ALA   A 1 50  ? 21.706 4.328   2.479   0.52 10.75 ?  50  ALA   A N    1 
ATOM   1308 C CA   A ALA   A 1 50  ? 22.893 4.765   2.601   0.48 11.72 ?  50  ALA   A CA   1 
ATOM   1309 C CA   B ALA   A 1 50  ? 23.030 4.871   2.764   0.52 10.84 ?  50  ALA   A CA   1 
ATOM   1310 C C    A ALA   A 1 50  ? 22.804 6.228   3.004   0.48 11.82 ?  50  ALA   A C    1 
ATOM   1311 C C    B ALA   A 1 50  ? 22.936 6.314   3.236   0.52 10.51 ?  50  ALA   A C    1 
ATOM   1312 O O    A ALA   A 1 50  ? 23.482 6.670   3.937   0.48 12.39 ?  50  ALA   A O    1 
ATOM   1313 O O    B ALA   A 1 50  ? 23.523 6.688   4.260   0.52 10.77 ?  50  ALA   A O    1 
ATOM   1314 C CB   A ALA   A 1 50  ? 23.771 4.626   1.362   0.48 11.61 ?  50  ALA   A CB   1 
ATOM   1315 C CB   B ALA   A 1 50  ? 23.912 4.762   1.518   0.52 10.76 ?  50  ALA   A CB   1 
ATOM   1316 H H    A ALA   A 1 50  ? 21.461 3.919   1.533   0.48 14.00 ?  50  ALA   A H    1 
ATOM   1317 H H    B ALA   A 1 50  ? 21.588 4.083   1.661   0.52 12.90 ?  50  ALA   A H    1 
ATOM   1318 H HA   A ALA   A 1 50  ? 23.302 4.279   3.335   0.48 14.07 ?  50  ALA   A HA   1 
ATOM   1319 H HA   B ALA   A 1 50  ? 23.446 4.359   3.469   0.52 13.02 ?  50  ALA   A HA   1 
ATOM   1320 H HB1  A ALA   A 1 50  ? 24.641 5.006   1.556   0.48 13.94 ?  50  ALA   A HB1  1 
ATOM   1321 H HB1  B ALA   A 1 50  ? 24.791 5.126   1.713   0.52 12.92 ?  50  ALA   A HB1  1 
ATOM   1322 H HB2  A ALA   A 1 50  ? 23.855 3.689   1.142   0.48 13.94 ?  50  ALA   A HB2  1 
ATOM   1323 H HB2  B ALA   A 1 50  ? 23.995 3.826   1.266   0.52 12.92 ?  50  ALA   A HB2  1 
ATOM   1324 H HB3  A ALA   A 1 50  ? 23.353 5.107   0.631   0.48 13.94 ?  50  ALA   A HB3  1 
ATOM   1325 H HB3  B ALA   A 1 50  ? 23.504 5.260   0.790   0.52 12.92 ?  50  ALA   A HB3  1 
ATOM   1326 N N    A GLY   A 1 51  ? 21.999 7.007   2.287   0.48 11.74 ?  51  GLY   A N    1 
ATOM   1327 N N    B GLY   A 1 51  ? 22.198 7.145   2.498   0.52 11.09 ?  51  GLY   A N    1 
ATOM   1328 C CA   A GLY   A 1 51  ? 21.861 8.408   2.636   0.48 12.49 ?  51  GLY   A CA   1 
ATOM   1329 C CA   B GLY   A 1 51  ? 22.037 8.524   2.920   0.52 11.38 ?  51  GLY   A CA   1 
ATOM   1330 C C    A GLY   A 1 51  ? 21.274 8.599   4.019   0.48 12.10 ?  51  GLY   A C    1 
ATOM   1331 C C    B GLY   A 1 51  ? 21.392 8.623   4.288   0.52 11.50 ?  51  GLY   A C    1 
ATOM   1332 O O    A GLY   A 1 51  ? 21.665 9.513   4.748   0.48 11.66 ?  51  GLY   A O    1 
ATOM   1333 O O    B GLY   A 1 51  ? 21.762 9.472   5.104   0.52 12.35 ?  51  GLY   A O    1 
ATOM   1334 H H    A GLY   A 1 51  ? 21.542 6.752   1.610   0.48 14.10 ?  51  GLY   A H    1 
ATOM   1335 H H    B GLY   A 1 51  ? 21.793 6.934   1.762   0.52 13.31 ?  51  GLY   A H    1 
ATOM   1336 H HA2  A GLY   A 1 51  ? 22.729 8.835   2.618   0.48 14.99 ?  51  GLY   A HA2  1 
ATOM   1337 H HA2  B GLY   A 1 51  ? 22.906 8.956   2.947   0.52 13.67 ?  51  GLY   A HA2  1 
ATOM   1338 H HA3  A GLY   A 1 51  ? 21.283 8.847   1.995   0.48 14.99 ?  51  GLY   A HA3  1 
ATOM   1339 H HA3  B GLY   A 1 51  ? 21.486 8.995   2.268   0.52 13.67 ?  51  GLY   A HA3  1 
ATOM   1340 N N    A ALA   A 1 52  ? 20.307 7.753   4.389   0.48 12.88 ?  52  ALA   A N    1 
ATOM   1341 N N    B ALA   A 1 52  ? 20.408 7.761   4.554   0.52 11.52 ?  52  ALA   A N    1 
ATOM   1342 C CA   A ALA   A 1 52  ? 19.674 7.867   5.700   0.48 13.48 ?  52  ALA   A CA   1 
ATOM   1343 C CA   B ALA   A 1 52  ? 19.708 7.785   5.835   0.52 12.18 ?  52  ALA   A CA   1 
ATOM   1344 C C    A ALA   A 1 52  ? 20.615 7.438   6.819   0.48 13.12 ?  52  ALA   A C    1 
ATOM   1345 C C    B ALA   A 1 52  ? 20.625 7.373   6.981   0.52 11.17 ?  52  ALA   A C    1 
ATOM   1346 O O    A ALA   A 1 52  ? 20.693 8.102   7.857   0.48 13.78 ?  52  ALA   A O    1 
ATOM   1347 O O    B ALA   A 1 52  ? 20.664 8.034   8.025   0.52 12.23 ?  52  ALA   A O    1 
ATOM   1348 C CB   A ALA   A 1 52  ? 18.377 7.056   5.732   0.48 13.86 ?  52  ALA   A CB   1 
ATOM   1349 C CB   B ALA   A 1 52  ? 18.473 6.886   5.770   0.52 13.17 ?  52  ALA   A CB   1 
ATOM   1350 H H    A ALA   A 1 52  ? 20.013 7.104   3.911   0.48 15.47 ?  52  ALA   A H    1 
ATOM   1351 H H    B ALA   A 1 52  ? 20.137 7.152   4.006   0.52 13.84 ?  52  ALA   A H    1 
ATOM   1352 H HA   A ALA   A 1 52  ? 19.442 8.791   5.858   0.48 16.19 ?  52  ALA   A HA   1 
ATOM   1353 H HA   B ALA   A 1 52  ? 19.413 8.688   6.003   0.52 14.63 ?  52  ALA   A HA   1 
ATOM   1354 H HB1  A ALA   A 1 52  ? 17.967 7.141   6.609   0.48 16.64 ?  52  ALA   A HB1  1 
ATOM   1355 H HB1  B ALA   A 1 52  ? 18.018 6.919   6.625   0.52 15.81 ?  52  ALA   A HB1  1 
ATOM   1356 H HB2  A ALA   A 1 52  ? 17.773 7.399   5.054   0.48 16.64 ?  52  ALA   A HB2  1 
ATOM   1357 H HB2  B ALA   A 1 52  ? 17.884 7.209   5.069   0.52 15.81 ?  52  ALA   A HB2  1 
ATOM   1358 H HB3  A ALA   A 1 52  ? 18.576 6.123   5.553   0.48 16.64 ?  52  ALA   A HB3  1 
ATOM   1359 H HB3  B ALA   A 1 52  ? 18.750 5.977   5.575   0.52 15.81 ?  52  ALA   A HB3  1 
ATOM   1360 N N    A LEU   A 1 53  ? 21.336 6.329   6.632   0.48 12.67 ?  53  LEU   A N    1 
ATOM   1361 N N    B LEU   A 1 53  ? 21.357 6.268   6.814   0.52 11.43 ?  53  LEU   A N    1 
ATOM   1362 C CA   A LEU   A 1 53  ? 22.279 5.887   7.657   0.48 12.80 ?  53  LEU   A CA   1 
ATOM   1363 C CA   B LEU   A 1 53  ? 22.340 5.886   7.824   0.52 11.38 ?  53  LEU   A CA   1 
ATOM   1364 C C    A LEU   A 1 53  ? 23.368 6.924   7.881   0.48 12.60 ?  53  LEU   A C    1 
ATOM   1365 C C    B LEU   A 1 53  ? 23.365 6.995   8.012   0.52 10.86 ?  53  LEU   A C    1 
ATOM   1366 O O    A LEU   A 1 53  ? 23.757 7.191   9.022   0.48 12.86 ?  53  LEU   A O    1 
ATOM   1367 O O    B LEU   A 1 53  ? 23.637 7.427   9.138   0.52 11.74 ?  53  LEU   A O    1 
ATOM   1368 C CB   A LEU   A 1 53  ? 22.903 4.544   7.270   0.48 13.42 ?  53  LEU   A CB   1 
ATOM   1369 C CB   B LEU   A 1 53  ? 23.031 4.571   7.435   0.52 11.64 ?  53  LEU   A CB   1 
ATOM   1370 C CG   A LEU   A 1 53  ? 21.968 3.335   7.361   0.48 13.66 ?  53  LEU   A CG   1 
ATOM   1371 C CG   B LEU   A 1 53  ? 22.208 3.273   7.464   0.52 12.29 ?  53  LEU   A CG   1 
ATOM   1372 C CD1  A LEU   A 1 53  ? 22.641 2.105   6.789   0.48 13.17 ?  53  LEU   A CD1  1 
ATOM   1373 C CD1  B LEU   A 1 53  ? 22.984 2.125   6.821   0.52 12.66 ?  53  LEU   A CD1  1 
ATOM   1374 C CD2  A LEU   A 1 53  ? 21.531 3.079   8.799   0.48 14.93 ?  53  LEU   A CD2  1 
ATOM   1375 C CD2  B LEU   A 1 53  ? 21.791 2.890   8.879   0.52 13.22 ?  53  LEU   A CD2  1 
ATOM   1376 H H    A LEU   A 1 53  ? 21.300 5.825   5.937   0.48 15.21 ?  53  LEU   A H    1 
ATOM   1377 H H    B LEU   A 1 53  ? 21.310 5.733   6.136   0.52 13.73 ?  53  LEU   A H    1 
ATOM   1378 H HA   A LEU   A 1 53  ? 21.807 5.765   8.495   0.48 15.37 ?  53  LEU   A HA   1 
ATOM   1379 H HA   B LEU   A 1 53  ? 21.890 5.746   8.666   0.52 13.66 ?  53  LEU   A HA   1 
ATOM   1380 H HB2  A LEU   A 1 53  ? 23.216 4.603   6.352   0.48 16.11 ?  53  LEU   A HB2  1 
ATOM   1381 H HB2  B LEU   A 1 53  ? 23.367 4.665   6.528   0.52 13.98 ?  53  LEU   A HB2  1 
ATOM   1382 H HB3  A LEU   A 1 53  ? 23.659 4.372   7.856   0.48 16.11 ?  53  LEU   A HB3  1 
ATOM   1383 H HB3  B LEU   A 1 53  ? 23.781 4.438   8.035   0.52 13.98 ?  53  LEU   A HB3  1 
ATOM   1384 H HG   A LEU   A 1 53  ? 21.174 3.514   6.834   0.48 16.40 ?  53  LEU   A HG   1 
ATOM   1385 H HG   B LEU   A 1 53  ? 21.403 3.402   6.943   0.52 14.76 ?  53  LEU   A HG   1 
ATOM   1386 H HD11 A LEU   A 1 53  ? 22.030 1.353   6.854   0.48 15.82 ?  53  LEU   A HD11 1 
ATOM   1387 H HD11 B LEU   A 1 53  ? 22.442 1.315   6.853   0.52 15.20 ?  53  LEU   A HD11 1 
ATOM   1388 H HD12 A LEU   A 1 53  ? 22.865 2.269   5.860   0.48 15.82 ?  53  LEU   A HD12 1 
ATOM   1389 H HD12 B LEU   A 1 53  ? 23.181 2.346   5.897   0.52 15.20 ?  53  LEU   A HD12 1 
ATOM   1390 H HD13 A LEU   A 1 53  ? 23.447 1.921   7.297   0.48 15.82 ?  53  LEU   A HD13 1 
ATOM   1391 H HD13 B LEU   A 1 53  ? 23.811 1.981   7.309   0.52 15.20 ?  53  LEU   A HD13 1 
ATOM   1392 H HD21 A LEU   A 1 53  ? 21.051 2.238   8.838   0.48 17.92 ?  53  LEU   A HD21 1 
ATOM   1393 H HD21 B LEU   A 1 53  ? 21.242 2.089   8.843   0.52 15.87 ?  53  LEU   A HD21 1 
ATOM   1394 H HD22 A LEU   A 1 53  ? 22.320 3.034   9.365   0.48 17.92 ?  53  LEU   A HD22 1 
ATOM   1395 H HD22 B LEU   A 1 53  ? 22.582 2.725   9.412   0.52 15.87 ?  53  LEU   A HD22 1 
ATOM   1396 H HD23 A LEU   A 1 53  ? 20.956 3.802   9.093   0.48 17.92 ?  53  LEU   A HD23 1 
ATOM   1397 H HD23 B LEU   A 1 53  ? 21.279 3.620   9.264   0.52 15.87 ?  53  LEU   A HD23 1 
ATOM   1398 N N    A ASN   A 1 54  ? 23.891 7.502   6.803   0.48 11.90 ?  54  ASN   A N    1 
ATOM   1399 N N    B ASN   A 1 54  ? 23.936 7.475   6.907   0.52 10.84 ?  54  ASN   A N    1 
ATOM   1400 C CA   A ASN   A 1 54  ? 24.952 8.486   6.961   0.48 12.26 ?  54  ASN   A CA   1 
ATOM   1401 C CA   B ASN   A 1 54  ? 24.974 8.488   7.016   0.52 11.68 ?  54  ASN   A CA   1 
ATOM   1402 C C    A ASN   A 1 54  ? 24.451 9.723   7.704   0.48 12.35 ?  54  ASN   A C    1 
ATOM   1403 C C    B ASN   A 1 54  ? 24.456 9.742   7.719   0.52 11.96 ?  54  ASN   A C    1 
ATOM   1404 O O    A ASN   A 1 54  ? 25.141 10.251  8.587   0.48 13.09 ?  54  ASN   A O    1 
ATOM   1405 O O    B ASN   A 1 54  ? 25.143 10.307  8.581   0.52 12.60 ?  54  ASN   A O    1 
ATOM   1406 C CB   A ASN   A 1 54  ? 25.522 8.858   5.598   0.48 12.27 ?  54  ASN   A CB   1 
ATOM   1407 C CB   B ASN   A 1 54  ? 25.525 8.828   5.638   0.52 11.52 ?  54  ASN   A CB   1 
ATOM   1408 C CG   A ASN   A 1 54  ? 26.549 9.952   5.700   0.48 12.49 ?  54  ASN   A CG   1 
ATOM   1409 C CG   B ASN   A 1 54  ? 26.576 9.900   5.709   0.52 11.51 ?  54  ASN   A CG   1 
ATOM   1410 O OD1  A ASN   A 1 54  ? 27.630 9.748   6.254   0.48 13.55 ?  54  ASN   A OD1  1 
ATOM   1411 O OD1  B ASN   A 1 54  ? 27.495 9.826   6.533   0.52 10.39 ?  54  ASN   A OD1  1 
ATOM   1412 N ND2  A ASN   A 1 54  ? 26.219 11.127  5.188   0.48 12.17 ?  54  ASN   A ND2  1 
ATOM   1413 N ND2  B ASN   A 1 54  ? 26.437 10.923  4.875   0.52 12.61 ?  54  ASN   A ND2  1 
ATOM   1414 H H    A ASN   A 1 54  ? 23.658 7.337   5.994   0.48 14.29 ?  54  ASN   A H    1 
ATOM   1415 H H    B ASN   A 1 54  ? 23.745 7.234   6.101   0.52 13.02 ?  54  ASN   A H    1 
ATOM   1416 H HA   A ASN   A 1 54  ? 25.665 8.092   7.485   0.48 14.72 ?  54  ASN   A HA   1 
ATOM   1417 H HA   B ASN   A 1 54  ? 25.704 8.134   7.544   0.52 14.02 ?  54  ASN   A HA   1 
ATOM   1418 H HB2  A ASN   A 1 54  ? 25.947 8.078   5.209   0.48 14.73 ?  54  ASN   A HB2  1 
ATOM   1419 H HB2  B ASN   A 1 54  ? 25.931 8.033   5.249   0.52 13.84 ?  54  ASN   A HB2  1 
ATOM   1420 H HB3  A ASN   A 1 54  ? 24.802 9.168   5.027   0.48 14.73 ?  54  ASN   A HB3  1 
ATOM   1421 H HB3  B ASN   A 1 54  ? 24.808 9.146   5.070   0.52 13.84 ?  54  ASN   A HB3  1 
ATOM   1422 H HD21 A ASN   A 1 54  ? 26.775 11.780  5.231   0.48 14.62 ?  54  ASN   A HD21 1 
ATOM   1423 H HD21 B ASN   A 1 54  ? 27.012 11.561  4.879   0.52 15.14 ?  54  ASN   A HD21 1 
ATOM   1424 H HD22 A ASN   A 1 54  ? 25.460 11.228  4.802   0.48 14.62 ?  54  ASN   A HD22 1 
ATOM   1425 H HD22 B ASN   A 1 54  ? 25.777 10.940  4.326   0.52 15.14 ?  54  ASN   A HD22 1 
ATOM   1426 N N    . LYS   A 1 55  ? 23.245 10.193  7.369   1.00 12.57 ?  55  LYS   A N    1 
ATOM   1427 C CA   . LYS   A 1 55  ? 22.684 11.365  8.028   1.00 13.54 ?  55  LYS   A CA   1 
ATOM   1428 C C    . LYS   A 1 55  ? 22.582 11.135  9.529   1.00 13.55 ?  55  LYS   A C    1 
ATOM   1429 O O    . LYS   A 1 55  ? 22.875 12.033  10.331  1.00 14.19 ?  55  LYS   A O    1 
ATOM   1430 C CB   . LYS   A 1 55  ? 21.316 11.669  7.412   1.00 14.22 ?  55  LYS   A CB   1 
ATOM   1431 C CG   . LYS   A 1 55  ? 20.583 12.854  8.012   1.00 16.81 ?  55  LYS   A CG   1 
ATOM   1432 C CD   . LYS   A 1 55  ? 19.240 13.043  7.310   1.00 19.58 ?  55  LYS   A CD   1 
ATOM   1433 C CE   . LYS   A 1 55  ? 18.392 14.141  7.937   1.00 22.26 ?  55  LYS   A CE   1 
ATOM   1434 N NZ   . LYS   A 1 55  ? 17.039 14.221  7.307   1.00 23.96 ?  55  LYS   A NZ   1 
ATOM   1435 H H    A LYS   A 1 55  ? 22.734 9.839   6.770   0.48 15.09 ?  55  LYS   A H    1 
ATOM   1436 H H    B LYS   A 1 55  ? 22.737 9.830   6.773   0.52 15.09 ?  55  LYS   A H    1 
ATOM   1437 H HA   . LYS   A 1 55  ? 23.261 12.123  7.875   1.00 16.26 ?  55  LYS   A HA   1 
ATOM   1438 H HB2  . LYS   A 1 55  ? 21.433 11.851  6.468   1.00 17.08 ?  55  LYS   A HB2  1 
ATOM   1439 H HB3  . LYS   A 1 55  ? 20.744 10.892  7.523   1.00 17.08 ?  55  LYS   A HB3  1 
ATOM   1440 H HG2  . LYS   A 1 55  ? 20.413 12.697  8.956   1.00 20.17 ?  55  LYS   A HG2  1 
ATOM   1441 H HG3  . LYS   A 1 55  ? 21.108 13.662  7.892   1.00 20.17 ?  55  LYS   A HG3  1 
ATOM   1442 H HD2  . LYS   A 1 55  ? 19.400 13.278  6.383   1.00 23.51 ?  55  LYS   A HD2  1 
ATOM   1443 H HD3  . LYS   A 1 55  ? 18.739 12.213  7.361   1.00 23.51 ?  55  LYS   A HD3  1 
ATOM   1444 H HE2  . LYS   A 1 55  ? 18.281 13.960  8.884   1.00 26.72 ?  55  LYS   A HE2  1 
ATOM   1445 H HE3  . LYS   A 1 55  ? 18.838 14.998  7.815   1.00 26.72 ?  55  LYS   A HE3  1 
ATOM   1446 H HZ1  . LYS   A 1 55  ? 16.564 14.872  7.691   1.00 28.75 ?  55  LYS   A HZ1  1 
ATOM   1447 H HZ2  . LYS   A 1 55  ? 17.117 14.395  6.439   1.00 28.75 ?  55  LYS   A HZ2  1 
ATOM   1448 H HZ3  . LYS   A 1 55  ? 16.610 13.450  7.413   1.00 28.75 ?  55  LYS   A HZ3  1 
ATOM   1449 N N    . ALA   A 1 56  ? 22.185 9.923   9.927   1.00 13.95 ?  56  ALA   A N    1 
ATOM   1450 C CA   . ALA   A 1 56  ? 22.055 9.606   11.341  1.00 14.89 ?  56  ALA   A CA   1 
ATOM   1451 C C    . ALA   A 1 56  ? 23.390 9.613   12.072  1.00 14.67 ?  56  ALA   A C    1 
ATOM   1452 O O    . ALA   A 1 56  ? 23.400 9.776   13.294  1.00 15.97 ?  56  ALA   A O    1 
ATOM   1453 C CB   . ALA   A 1 56  ? 21.340 8.268   11.531  1.00 15.54 ?  56  ALA   A CB   1 
ATOM   1454 H H    . ALA   A 1 56  ? 21.990 9.272   9.394   1.00 16.75 ?  56  ALA   A H    1 
ATOM   1455 H HA   . ALA   A 1 56  ? 21.506 10.280  11.753  1.00 17.87 ?  56  ALA   A HA   1 
ATOM   1456 H HB1  . ALA   A 1 56  ? 21.266 8.081   12.481  1.00 18.65 ?  56  ALA   A HB1  1 
ATOM   1457 H HB2  . ALA   A 1 56  ? 20.454 8.327   11.138  1.00 18.65 ?  56  ALA   A HB2  1 
ATOM   1458 H HB3  . ALA   A 1 56  ? 21.848 7.566   11.095  1.00 18.65 ?  56  ALA   A HB3  1 
ATOM   1459 N N    . THR   A 1 57  ? 24.506 9.414   11.361  1.00 13.54 ?  57  THR   A N    1 
ATOM   1460 C CA   . THR   A 1 57  ? 25.840 9.527   11.948  1.00 13.56 ?  57  THR   A CA   1 
ATOM   1461 C C    . THR   A 1 57  ? 26.409 10.939  11.872  1.00 14.00 ?  57  THR   A C    1 
ATOM   1462 O O    . THR   A 1 57  ? 27.592 11.132  12.165  1.00 14.54 ?  57  THR   A O    1 
ATOM   1463 C CB   . THR   A 1 57  ? 26.851 8.575   11.283  1.00 13.04 ?  57  THR   A CB   1 
ATOM   1464 O OG1  . THR   A 1 57  ? 27.227 9.065   9.983   1.00 12.77 ?  57  THR   A OG1  1 
ATOM   1465 C CG2  . THR   A 1 57  ? 26.312 7.142   11.204  1.00 13.39 ?  57  THR   A CG2  1 
ATOM   1466 H H    . THR   A 1 57  ? 24.515 9.192   10.527  1.00 16.26 ?  57  THR   A H    1 
ATOM   1467 H HA   . THR   A 1 57  ? 25.779 9.272   12.887  1.00 16.28 ?  57  THR   A HA   1 
ATOM   1468 H HB   . THR   A 1 57  ? 27.645 8.544   11.842  1.00 15.65 ?  57  THR   A HB   1 
ATOM   1469 H HG1  . THR   A 1 57  ? 26.551 9.126   9.495   1.00 15.34 ?  57  THR   A HG1  1 
ATOM   1470 H HG21 . THR   A 1 57  ? 26.985 6.552   10.829  1.00 16.08 ?  57  THR   A HG21 1 
ATOM   1471 H HG22 . THR   A 1 57  ? 26.080 6.821   12.094  1.00 16.08 ?  57  THR   A HG22 1 
ATOM   1472 H HG23 . THR   A 1 57  ? 25.521 7.110   10.648  1.00 16.08 ?  57  THR   A HG23 1 
ATOM   1473 N N    A ASN   A 1 58  ? 25.600 11.921  11.482  0.48 14.72 ?  58  ASN   A N    1 
ATOM   1474 N N    B ASN   A 1 58  ? 25.616 11.934  11.483  0.52 14.13 ?  58  ASN   A N    1 
ATOM   1475 C CA   A ASN   A 1 58  ? 26.064 13.299  11.361  0.48 15.61 ?  58  ASN   A CA   1 
ATOM   1476 C CA   B ASN   A 1 58  ? 26.124 13.301  11.411  0.52 14.47 ?  58  ASN   A CA   1 
ATOM   1477 C C    A ASN   A 1 58  ? 27.225 13.407  10.368  0.48 14.34 ?  58  ASN   A C    1 
ATOM   1478 C C    B ASN   A 1 58  ? 27.232 13.424  10.359  0.52 13.79 ?  58  ASN   A C    1 
ATOM   1479 O O    A ASN   A 1 58  ? 28.144 14.207  10.546  0.48 14.81 ?  58  ASN   A O    1 
ATOM   1480 O O    B ASN   A 1 58  ? 28.121 14.269  10.475  0.52 14.44 ?  58  ASN   A O    1 
ATOM   1481 C CB   A ASN   A 1 58  ? 26.435 13.882  12.731  0.48 18.41 ?  58  ASN   A CB   1 
ATOM   1482 C CB   B ASN   A 1 58  ? 26.588 13.779  12.805  0.52 16.12 ?  58  ASN   A CB   1 
ATOM   1483 C CG   A ASN   A 1 58  ? 26.630 15.383  12.697  0.48 21.28 ?  58  ASN   A CG   1 
ATOM   1484 C CG   B ASN   A 1 58  ? 27.058 15.236  12.834  0.52 16.92 ?  58  ASN   A CG   1 
ATOM   1485 O OD1  A ASN   A 1 58  ? 25.913 16.098  11.992  0.48 22.15 ?  58  ASN   A OD1  1 
ATOM   1486 O OD1  B ASN   A 1 58  ? 26.493 16.098  12.172  0.52 17.99 ?  58  ASN   A OD1  1 
ATOM   1487 N ND2  A ASN   A 1 58  ? 27.609 15.872  13.464  0.48 22.54 ?  58  ASN   A ND2  1 
ATOM   1488 N ND2  B ASN   A 1 58  ? 28.088 15.513  13.631  0.52 16.71 ?  58  ASN   A ND2  1 
ATOM   1489 H H    A ASN   A 1 58  ? 24.769 11.811  11.287  0.48 17.67 ?  58  ASN   A H    1 
ATOM   1490 H H    B ASN   A 1 58  ? 24.791 11.842  11.258  0.52 16.96 ?  58  ASN   A H    1 
ATOM   1491 H HA   A ASN   A 1 58  ? 25.330 13.826  11.022  0.48 18.74 ?  58  ASN   A HA   1 
ATOM   1492 H HA   B ASN   A 1 58  ? 25.398 13.875  11.137  0.52 17.37 ?  58  ASN   A HA   1 
ATOM   1493 H HB2  A ASN   A 1 58  ? 25.727 13.698  13.366  0.48 22.10 ?  58  ASN   A HB2  1 
ATOM   1494 H HB2  B ASN   A 1 58  ? 25.841 13.687  13.434  0.52 19.36 ?  58  ASN   A HB2  1 
ATOM   1495 H HB3  A ASN   A 1 58  ? 27.266 13.479  13.038  0.48 22.10 ?  58  ASN   A HB3  1 
ATOM   1496 H HB3  B ASN   A 1 58  ? 27.328 13.241  13.111  0.52 19.36 ?  58  ASN   A HB3  1 
ATOM   1497 H HD21 A ASN   A 1 58  ? 27.777 16.718  13.476  0.48 27.06 ?  58  ASN   A HD21 1 
ATOM   1498 H HD21 B ASN   A 1 58  ? 28.373 16.326  13.693  0.52 20.06 ?  58  ASN   A HD21 1 
ATOM   1499 H HD22 A ASN   A 1 58  ? 28.089 15.340  13.948  0.48 27.06 ?  58  ASN   A HD22 1 
ATOM   1500 H HD22 B ASN   A 1 58  ? 28.461 14.891  14.080  0.52 20.06 ?  58  ASN   A HD22 1 
ATOM   1501 N N    . ASN   A 1 59  ? 27.184 12.593  9.312   1.00 13.17 ?  59  ASN   A N    1 
ATOM   1502 C CA   . ASN   A 1 59  ? 28.165 12.551  8.208   1.00 13.11 ?  59  ASN   A CA   1 
ATOM   1503 C C    . ASN   A 1 59  ? 29.483 11.873  8.601   1.00 12.67 ?  59  ASN   A C    1 
ATOM   1504 O O    . ASN   A 1 59  ? 30.396 11.813  7.772   1.00 12.85 ?  59  ASN   A O    1 
ATOM   1505 C CB   . ASN   A 1 59  ? 28.441 13.937  7.584   1.00 13.21 ?  59  ASN   A CB   1 
ATOM   1506 C CG   . ASN   A 1 59  ? 28.813 13.861  6.119   1.00 13.77 ?  59  ASN   A CG   1 
ATOM   1507 O OD1  . ASN   A 1 59  ? 28.101 13.247  5.327   1.00 13.89 ?  59  ASN   A OD1  1 
ATOM   1508 N ND2  . ASN   A 1 59  ? 29.925 14.499  5.742   1.00 13.93 ?  59  ASN   A ND2  1 
ATOM   1509 H H    A ASN   A 1 59  ? 26.563 12.008  9.207   0.48 15.81 ?  59  ASN   A H    1 
ATOM   1510 H H    B ASN   A 1 59  ? 26.556 12.014  9.210   0.52 15.81 ?  59  ASN   A H    1 
ATOM   1511 H HA   . ASN   A 1 59  ? 27.775 12.013  7.507   1.00 15.74 ?  59  ASN   A HA   1 
ATOM   1512 H HB2  . ASN   A 1 59  ? 27.638 14.484  7.648   1.00 15.86 ?  59  ASN   A HB2  1 
ATOM   1513 H HB3  . ASN   A 1 59  ? 29.171 14.362  8.046   1.00 15.86 ?  59  ASN   A HB3  1 
ATOM   1514 H HD21 . ASN   A 1 59  ? 30.173 14.487  4.915   1.00 16.73 ?  59  ASN   A HD21 1 
ATOM   1515 H HD22 . ASN   A 1 59  ? 30.395 14.924  6.322   1.00 16.73 ?  59  ASN   A HD22 1 
ATOM   1516 N N    . ALA   A 1 60  ? 29.599 11.329  9.811   1.00 12.90 ?  60  ALA   A N    1 
ATOM   1517 C CA   . ALA   A 1 60  ? 30.827 10.633  10.172  1.00 13.05 ?  60  ALA   A CA   1 
ATOM   1518 C C    . ALA   A 1 60  ? 31.043 9.394   9.310   1.00 12.86 ?  60  ALA   A C    1 
ATOM   1519 O O    . ALA   A 1 60  ? 32.187 9.066   8.979   1.00 13.13 ?  60  ALA   A O    1 
ATOM   1520 C CB   . ALA   A 1 60  ? 30.805 10.285  11.655  1.00 14.04 ?  60  ALA   A CB   1 
ATOM   1521 H H    . ALA   A 1 60  ? 29.001 11.355  10.429  1.00 15.49 ?  60  ALA   A H    1 
ATOM   1522 H HA   . ALA   A 1 60  ? 31.579 11.230  10.020  1.00 15.67 ?  60  ALA   A HA   1 
ATOM   1523 H HB1  . ALA   A 1 60  ? 31.624 9.823   11.882  1.00 16.85 ?  60  ALA   A HB1  1 
ATOM   1524 H HB2  . ALA   A 1 60  ? 30.734 11.108  12.167  1.00 16.85 ?  60  ALA   A HB2  1 
ATOM   1525 H HB3  . ALA   A 1 60  ? 30.039 9.718   11.832  1.00 16.85 ?  60  ALA   A HB3  1 
ATOM   1526 N N    . MET   A 1 61  ? 29.966 8.711   8.917   1.00 12.29 ?  61  MET   A N    1 
ATOM   1527 C CA   . MET   A 1 61  ? 30.100 7.575   8.012   1.00 12.32 ?  61  MET   A CA   1 
ATOM   1528 C C    . MET   A 1 61  ? 30.745 7.993   6.694   1.00 12.09 ?  61  MET   A C    1 
ATOM   1529 O O    . MET   A 1 61  ? 31.638 7.304   6.182   1.00 12.52 ?  61  MET   A O    1 
ATOM   1530 C CB   . MET   A 1 61  ? 28.733 6.920   7.790   1.00 12.46 ?  61  MET   A CB   1 
ATOM   1531 C CG   . MET   A 1 61  ? 28.751 5.756   6.821   1.00 12.93 ?  61  MET   A CG   1 
ATOM   1532 S SD   . MET   A 1 61  ? 27.118 5.039   6.601   1.00 14.73 ?  61  MET   A SD   1 
ATOM   1533 C CE   . MET   A 1 61  ? 26.962 4.130   8.146   1.00 16.24 ?  61  MET   A CE   1 
ATOM   1534 H H    . MET   A 1 61  ? 29.158 8.886   9.149   1.00 14.76 ?  61  MET   A H    1 
ATOM   1535 H HA   . MET   A 1 61  ? 30.668 6.911   8.429   1.00 14.79 ?  61  MET   A HA   1 
ATOM   1536 H HB2  . MET   A 1 61  ? 28.402 6.594   8.638   1.00 14.96 ?  61  MET   A HB2  1 
ATOM   1537 H HB3  . MET   A 1 61  ? 28.121 7.587   7.433   1.00 14.96 ?  61  MET   A HB3  1 
ATOM   1538 H HG2  . MET   A 1 61  ? 29.058 6.055   5.950   1.00 15.52 ?  61  MET   A HG2  1 
ATOM   1539 H HG3  . MET   A 1 61  ? 29.340 5.063   7.161   1.00 15.52 ?  61  MET   A HG3  1 
ATOM   1540 H HE1  . MET   A 1 61  ? 26.113 3.651   8.147   1.00 19.50 ?  61  MET   A HE1  1 
ATOM   1541 H HE2  . MET   A 1 61  ? 27.693 3.498   8.218   1.00 19.50 ?  61  MET   A HE2  1 
ATOM   1542 H HE3  . MET   A 1 61  ? 26.985 4.752   8.889   1.00 19.50 ?  61  MET   A HE3  1 
ATOM   1543 N N    . GLN   A 1 62  ? 30.318 9.125   6.134   1.00 12.12 ?  62  GLN   A N    1 
ATOM   1544 C CA   . GLN   A 1 62  ? 30.893 9.578   4.872   1.00 12.34 ?  62  GLN   A CA   1 
ATOM   1545 C C    . GLN   A 1 62  ? 32.366 9.944   5.024   1.00 12.38 ?  62  GLN   A C    1 
ATOM   1546 O O    . GLN   A 1 62  ? 33.177 9.631   4.147   1.00 12.55 ?  62  GLN   A O    1 
ATOM   1547 C CB   . GLN   A 1 62  ? 30.095 10.764  4.336   1.00 12.43 ?  62  GLN   A CB   1 
ATOM   1548 C CG   . GLN   A 1 62  ? 30.497 11.140  2.923   1.00 12.39 ?  62  GLN   A CG   1 
ATOM   1549 C CD   . GLN   A 1 62  ? 30.177 10.018  1.966   1.00 12.36 ?  62  GLN   A CD   1 
ATOM   1550 O OE1  . GLN   A 1 62  ? 29.004 9.738   1.725   1.00 13.55 ?  62  GLN   A OE1  1 
ATOM   1551 N NE2  . GLN   A 1 62  ? 31.199 9.323   1.469   1.00 12.98 ?  62  GLN   A NE2  1 
ATOM   1552 H H    . GLN   A 1 62  ? 29.704 9.629   6.454   1.00 14.55 ?  62  GLN   A H    1 
ATOM   1553 H HA   . GLN   A 1 62  ? 30.831 8.854   4.225   1.00 14.81 ?  62  GLN   A HA   1 
ATOM   1554 H HB2  . GLN   A 1 62  ? 29.150 10.542  4.340   1.00 14.92 ?  62  GLN   A HB2  1 
ATOM   1555 H HB3  . GLN   A 1 62  ? 30.255 11.535  4.909   1.00 14.92 ?  62  GLN   A HB3  1 
ATOM   1556 H HG2  . GLN   A 1 62  ? 29.990 11.918  2.644   1.00 14.88 ?  62  GLN   A HG2  1 
ATOM   1557 H HG3  . GLN   A 1 62  ? 31.443 11.315  2.887   1.00 14.88 ?  62  GLN   A HG3  1 
ATOM   1558 H HE21 . GLN   A 1 62  ? 32.007 9.543   1.678   1.00 15.58 ?  62  GLN   A HE21 1 
ATOM   1559 H HE22 . GLN   A 1 62  ? 31.058 8.670   0.931   1.00 15.58 ?  62  GLN   A HE22 1 
ATOM   1560 N N    . VAL   A 1 63  ? 32.725 10.615  6.119   1.00 12.87 ?  63  VAL   A N    1 
ATOM   1561 C CA   . VAL   A 1 63  ? 34.117 11.000  6.340   1.00 13.93 ?  63  VAL   A CA   1 
ATOM   1562 C C    . VAL   A 1 63  ? 35.002 9.761   6.409   1.00 13.16 ?  63  VAL   A C    1 
ATOM   1563 O O    . VAL   A 1 63  ? 36.061 9.687   5.769   1.00 13.90 ?  63  VAL   A O    1 
ATOM   1564 C CB   . VAL   A 1 63  ? 34.229 11.871  7.606   1.00 15.70 ?  63  VAL   A CB   1 
ATOM   1565 C CG1  . VAL   A 1 63  ? 35.684 12.105  7.984   1.00 17.79 ?  63  VAL   A CG1  1 
ATOM   1566 C CG2  . VAL   A 1 63  ? 33.508 13.212  7.401   1.00 15.83 ?  63  VAL   A CG2  1 
ATOM   1567 H H    . VAL   A 1 63  ? 32.183 10.861  6.741   1.00 15.45 ?  63  VAL   A H    1 
ATOM   1568 H HA   . VAL   A 1 63  ? 34.415 11.535  5.592   1.00 16.72 ?  63  VAL   A HA   1 
ATOM   1569 H HB   . VAL   A 1 63  ? 33.797 11.415  8.349   1.00 18.85 ?  63  VAL   A HB   1 
ATOM   1570 H HG11 . VAL   A 1 63  ? 35.732 12.837  8.623   1.00 21.35 ?  63  VAL   A HG11 1 
ATOM   1571 H HG12 . VAL   A 1 63  ? 36.045 11.298  8.383   1.00 21.35 ?  63  VAL   A HG12 1 
ATOM   1572 H HG13 . VAL   A 1 63  ? 36.184 12.335  7.186   1.00 21.35 ?  63  VAL   A HG13 1 
ATOM   1573 H HG21 . VAL   A 1 63  ? 33.597 13.749  8.206   1.00 19.00 ?  63  VAL   A HG21 1 
ATOM   1574 H HG22 . VAL   A 1 63  ? 33.908 13.675  6.649   1.00 19.00 ?  63  VAL   A HG22 1 
ATOM   1575 H HG23 . VAL   A 1 63  ? 32.568 13.043  7.223   1.00 19.00 ?  63  VAL   A HG23 1 
ATOM   1576 N N    . GLU   A 1 64  ? 34.578 8.765   7.183   1.00 12.94 ?  64  GLU   A N    1 
ATOM   1577 C CA   . GLU   A 1 64  ? 35.330 7.522   7.277   1.00 13.16 ?  64  GLU   A CA   1 
ATOM   1578 C C    . GLU   A 1 64  ? 35.411 6.831   5.923   1.00 12.86 ?  64  GLU   A C    1 
ATOM   1579 O O    . GLU   A 1 64  ? 36.459 6.280   5.553   1.00 13.52 ?  64  GLU   A O    1 
ATOM   1580 C CB   . GLU   A 1 64  ? 34.641 6.622   8.300   1.00 14.01 ?  64  GLU   A CB   1 
ATOM   1581 C CG   . GLU   A 1 64  ? 35.294 5.278   8.470   1.00 14.96 ?  64  GLU   A CG   1 
ATOM   1582 C CD   . GLU   A 1 64  ? 34.415 4.282   9.203   1.00 16.01 ?  64  GLU   A CD   1 
ATOM   1583 O OE1  . GLU   A 1 64  ? 33.171 4.391   9.094   1.00 17.25 ?  64  GLU   A OE1  1 
ATOM   1584 O OE2  . GLU   A 1 64  ? 34.969 3.372   9.864   1.00 16.71 -1 64  GLU   A OE2  1 
ATOM   1585 H H    . GLU   A 1 64  ? 33.855 8.781   7.654   1.00 15.53 ?  64  GLU   A H    1 
ATOM   1586 H HA   . GLU   A 1 64  ? 36.230 7.714   7.589   1.00 15.80 ?  64  GLU   A HA   1 
ATOM   1587 H HB2  . GLU   A 1 64  ? 34.649 7.069   9.166   1.00 16.82 ?  64  GLU   A HB2  1 
ATOM   1588 H HB3  . GLU   A 1 64  ? 33.722 6.482   8.018   1.00 16.82 ?  64  GLU   A HB3  1 
ATOM   1589 H HG2  . GLU   A 1 64  ? 35.500 4.910   7.594   1.00 17.96 ?  64  GLU   A HG2  1 
ATOM   1590 H HG3  . GLU   A 1 64  ? 36.108 5.394   8.978   1.00 17.96 ?  64  GLU   A HG3  1 
ATOM   1591 N N    . SER   A 1 65  ? 34.300 6.833   5.184   1.00 12.52 ?  65  SER   A N    1 
ATOM   1592 C CA   . SER   A 1 65  ? 34.252 6.171   3.885   1.00 12.61 ?  65  SER   A CA   1 
ATOM   1593 C C    . SER   A 1 65  ? 35.182 6.835   2.878   1.00 12.72 ?  65  SER   A C    1 
ATOM   1594 O O    . SER   A 1 65  ? 35.832 6.153   2.080   1.00 13.58 ?  65  SER   A O    1 
ATOM   1595 C CB   . SER   A 1 65  ? 32.823 6.182   3.347   1.00 12.64 ?  65  SER   A CB   1 
ATOM   1596 O OG   . SER   A 1 65  ? 31.955 5.383   4.144   1.00 13.39 ?  65  SER   A OG   1 
ATOM   1597 H H    . SER   A 1 65  ? 33.561 7.218   5.412   1.00 15.03 ?  65  SER   A H    1 
ATOM   1598 H HA   . SER   A 1 65  ? 34.533 5.250   3.991   1.00 15.14 ?  65  SER   A HA   1 
ATOM   1599 H HB2  . SER   A 1 65  ? 32.491 7.088   3.344   1.00 15.18 ?  65  SER   A HB2  1 
ATOM   1600 H HB3  . SER   A 1 65  ? 32.828 5.824   2.445   1.00 15.18 ?  65  SER   A HB3  1 
ATOM   1601 H HG   . SER   A 1 65  ? 31.947 5.675   4.937   1.00 16.07 ?  65  SER   A HG   1 
ATOM   1602 N N    . ASP   A 1 66  ? 35.252 8.168   2.881   1.00 12.58 ?  66  ASP   A N    1 
ATOM   1603 C CA   . ASP   A 1 66  ? 36.135 8.853   1.941   1.00 13.20 ?  66  ASP   A CA   1 
ATOM   1604 C C    . ASP   A 1 66  ? 37.591 8.493   2.203   1.00 13.56 ?  66  ASP   A C    1 
ATOM   1605 O O    . ASP   A 1 66  ? 38.376 8.324   1.262   1.00 14.14 ?  66  ASP   A O    1 
ATOM   1606 C CB   . ASP   A 1 66  ? 35.928 10.362  2.029   1.00 14.83 ?  66  ASP   A CB   1 
ATOM   1607 C CG   . ASP   A 1 66  ? 34.607 10.828  1.410   1.00 16.97 ?  66  ASP   A CG   1 
ATOM   1608 O OD1  . ASP   A 1 66  ? 33.900 10.038  0.745   1.00 18.10 ?  66  ASP   A OD1  1 
ATOM   1609 O OD2  . ASP   A 1 66  ? 34.308 12.028  1.566   1.00 19.71 -1 66  ASP   A OD2  1 
ATOM   1610 H H    . ASP   A 1 66  ? 34.807 8.685   3.407   1.00 15.10 ?  66  ASP   A H    1 
ATOM   1611 H HA   . ASP   A 1 66  ? 35.912 8.571   1.042   1.00 15.85 ?  66  ASP   A HA   1 
ATOM   1612 H HB2  . ASP   A 1 66  ? 35.926 10.629  2.958   1.00 17.81 ?  66  ASP   A HB2  1 
ATOM   1613 H HB3  . ASP   A 1 66  ? 36.652 10.805  1.556   1.00 17.81 ?  66  ASP   A HB3  1 
ATOM   1614 N N    . ASP   A 1 67  ? 37.975 8.373   3.474   1.00 13.51 ?  67  ASP   A N    1 
ATOM   1615 C CA   . ASP   A 1 67  ? 39.325 7.928   3.787   1.00 14.37 ?  67  ASP   A CA   1 
ATOM   1616 C C    . ASP   A 1 67  ? 39.551 6.496   3.315   1.00 14.38 ?  67  ASP   A C    1 
ATOM   1617 O O    . ASP   A 1 67  ? 40.618 6.176   2.777   1.00 15.33 ?  67  ASP   A O    1 
ATOM   1618 C CB   . ASP   A 1 67  ? 39.581 8.066   5.286   1.00 15.73 ?  67  ASP   A CB   1 
ATOM   1619 C CG   . ASP   A 1 67  ? 40.879 7.411   5.713   1.00 17.83 ?  67  ASP   A CG   1 
ATOM   1620 O OD1  . ASP   A 1 67  ? 41.948 8.051   5.569   1.00 20.80 ?  67  ASP   A OD1  1 
ATOM   1621 O OD2  . ASP   A 1 67  ? 40.835 6.245   6.171   1.00 17.41 -1 67  ASP   A OD2  1 
ATOM   1622 H H    . ASP   A 1 67  ? 37.485 8.551   4.157   1.00 16.22 ?  67  ASP   A H    1 
ATOM   1623 H HA   . ASP   A 1 67  ? 39.963 8.498   3.326   1.00 17.25 ?  67  ASP   A HA   1 
ATOM   1624 H HB2  . ASP   A 1 67  ? 39.627 9.005   5.513   1.00 18.89 ?  67  ASP   A HB2  1 
ATOM   1625 H HB3  . ASP   A 1 67  ? 38.855 7.639   5.771   1.00 18.89 ?  67  ASP   A HB3  1 
ATOM   1626 N N    . TYR   A 1 68  ? 38.551 5.621   3.490   1.00 13.73 ?  68  TYR   A N    1 
ATOM   1627 C CA   . TYR   A 1 68  ? 38.679 4.241   3.024   1.00 13.88 ?  68  TYR   A CA   1 
ATOM   1628 C C    . TYR   A 1 68  ? 38.921 4.186   1.517   1.00 13.90 ?  68  TYR   A C    1 
ATOM   1629 O O    . TYR   A 1 68  ? 39.809 3.461   1.046   1.00 14.50 ?  68  TYR   A O    1 
ATOM   1630 C CB   . TYR   A 1 68  ? 37.428 3.423   3.403   1.00 14.73 ?  68  TYR   A CB   1 
ATOM   1631 C CG   . TYR   A 1 68  ? 37.451 2.030   2.779   1.00 16.33 ?  68  TYR   A CG   1 
ATOM   1632 C CD1  . TYR   A 1 68  ? 37.007 1.832   1.478   1.00 18.18 ?  68  TYR   A CD1  1 
ATOM   1633 C CD2  . TYR   A 1 68  ? 37.976 0.939   3.460   1.00 18.47 ?  68  TYR   A CD2  1 
ATOM   1634 C CE1  . TYR   A 1 68  ? 37.068 0.605   0.869   1.00 19.93 ?  68  TYR   A CE1  1 
ATOM   1635 C CE2  . TYR   A 1 68  ? 38.035 -0.327  2.850   1.00 19.50 ?  68  TYR   A CE2  1 
ATOM   1636 C CZ   . TYR   A 1 68  ? 37.582 -0.468  1.556   1.00 20.48 ?  68  TYR   A CZ   1 
ATOM   1637 O OH   . TYR   A 1 68  ? 37.655 -1.688  0.937   1.00 22.45 ?  68  TYR   A OH   1 
ATOM   1638 H H    . TYR   A 1 68  ? 37.800 5.801   3.869   1.00 16.49 ?  68  TYR   A H    1 
ATOM   1639 H HA   . TYR   A 1 68  ? 39.441 3.831   3.464   1.00 16.66 ?  68  TYR   A HA   1 
ATOM   1640 H HB2  . TYR   A 1 68  ? 37.391 3.324   4.368   1.00 17.68 ?  68  TYR   A HB2  1 
ATOM   1641 H HB3  . TYR   A 1 68  ? 36.636 3.889   3.086   1.00 17.68 ?  68  TYR   A HB3  1 
ATOM   1642 H HD1  . TYR   A 1 68  ? 36.670 2.563   1.002   1.00 21.82 ?  68  TYR   A HD1  1 
ATOM   1643 H HD2  . TYR   A 1 68  ? 38.292 1.044   4.325   1.00 22.17 ?  68  TYR   A HD2  1 
ATOM   1644 H HE1  . TYR   A 1 68  ? 36.758 0.506   -0.002  1.00 23.92 ?  68  TYR   A HE1  1 
ATOM   1645 H HE2  . TYR   A 1 68  ? 38.381 -1.060  3.300   1.00 23.41 ?  68  TYR   A HE2  1 
ATOM   1646 H HH   . TYR   A 1 68  ? 37.972 -2.261  1.461   1.00 26.95 ?  68  TYR   A HH   1 
ATOM   1647 N N    . ILE   A 1 69  ? 38.137 4.940   0.740   1.00 13.49 ?  69  ILE   A N    1 
ATOM   1648 C CA   . ILE   A 1 69  ? 38.287 4.925   -0.713  1.00 13.45 ?  69  ILE   A CA   1 
ATOM   1649 C C    . ILE   A 1 69  ? 39.624 5.540   -1.131  1.00 13.52 ?  69  ILE   A C    1 
ATOM   1650 O O    . ILE   A 1 69  ? 40.275 5.066   -2.069  1.00 13.82 ?  69  ILE   A O    1 
ATOM   1651 C CB   . ILE   A 1 69  ? 37.090 5.630   -1.384  1.00 14.40 ?  69  ILE   A CB   1 
ATOM   1652 C CG1  . ILE   A 1 69  ? 35.779 4.887   -1.108  1.00 15.01 ?  69  ILE   A CG1  1 
ATOM   1653 C CG2  . ILE   A 1 69  ? 37.335 5.797   -2.883  1.00 15.97 ?  69  ILE   A CG2  1 
ATOM   1654 C CD1  . ILE   A 1 69  ? 35.617 3.621   -1.898  1.00 15.80 ?  69  ILE   A CD1  1 
ATOM   1655 H H    . ILE   A 1 69  ? 37.524 5.465   1.030   1.00 16.19 ?  69  ILE   A H    1 
ATOM   1656 H HA   . ILE   A 1 69  ? 38.287 4.004   -1.012  1.00 16.15 ?  69  ILE   A HA   1 
ATOM   1657 H HB   . ILE   A 1 69  ? 37.011 6.514   -0.997  1.00 17.29 ?  69  ILE   A HB   1 
ATOM   1658 H HG12 . ILE   A 1 69  ? 35.747 4.649   -0.165  1.00 18.03 ?  69  ILE   A HG12 1 
ATOM   1659 H HG13 . ILE   A 1 69  ? 35.037 5.470   -1.322  1.00 18.03 ?  69  ILE   A HG13 1 
ATOM   1660 H HG21 . ILE   A 1 69  ? 36.489 5.993   -3.323  1.00 19.17 ?  69  ILE   A HG21 1 
ATOM   1661 H HG22 . ILE   A 1 69  ? 37.951 6.536   -3.026  1.00 19.17 ?  69  ILE   A HG22 1 
ATOM   1662 H HG23 . ILE   A 1 69  ? 37.709 4.980   -3.242  1.00 19.17 ?  69  ILE   A HG23 1 
ATOM   1663 H HD11 . ILE   A 1 69  ? 34.854 3.134   -1.553  1.00 18.96 ?  69  ILE   A HD11 1 
ATOM   1664 H HD12 . ILE   A 1 69  ? 35.466 3.851   -2.830  1.00 18.96 ?  69  ILE   A HD12 1 
ATOM   1665 H HD13 . ILE   A 1 69  ? 36.419 3.087   -1.813  1.00 18.96 ?  69  ILE   A HD13 1 
ATOM   1666 N N    . ALA   A 1 70  ? 40.036 6.623   -0.471  1.00 14.00 ?  70  ALA   A N    1 
ATOM   1667 C CA   . ALA   A 1 70  ? 41.318 7.239   -0.808  1.00 15.14 ?  70  ALA   A CA   1 
ATOM   1668 C C    . ALA   A 1 70  ? 42.472 6.259   -0.633  1.00 15.63 ?  70  ALA   A C    1 
ATOM   1669 O O    . ALA   A 1 70  ? 43.464 6.321   -1.366  1.00 17.58 ?  70  ALA   A O    1 
ATOM   1670 C CB   . ALA   A 1 70  ? 41.543 8.486   0.049   1.00 16.08 ?  70  ALA   A CB   1 
ATOM   1671 H H    . ALA   A 1 70  ? 39.601 7.012   0.158   1.00 16.81 ?  70  ALA   A H    1 
ATOM   1672 H HA   . ALA   A 1 70  ? 41.295 7.521   -1.739  1.00 18.17 ?  70  ALA   A HA   1 
ATOM   1673 H HB1  . ALA   A 1 70  ? 42.402 8.878   -0.191  1.00 19.31 ?  70  ALA   A HB1  1 
ATOM   1674 H HB2  . ALA   A 1 70  ? 40.834 9.120   -0.117  1.00 19.31 ?  70  ALA   A HB2  1 
ATOM   1675 H HB3  . ALA   A 1 70  ? 41.552 8.227   0.983   1.00 19.31 ?  70  ALA   A HB3  1 
ATOM   1676 N N    . THR   A 1 71  ? 42.361 5.346   0.321   1.00 14.88 ?  71  THR   A N    1 
ATOM   1677 C CA   . THR   A 1 71  ? 43.410 4.370   0.576   1.00 16.90 ?  71  THR   A CA   1 
ATOM   1678 C C    . THR   A 1 71  ? 43.290 3.135   -0.302  1.00 17.02 ?  71  THR   A C    1 
ATOM   1679 O O    . THR   A 1 71  ? 44.301 2.618   -0.792  1.00 19.36 ?  71  THR   A O    1 
ATOM   1680 C CB   . THR   A 1 71  ? 43.333 3.935   2.036   1.00 19.30 ?  71  THR   A CB   1 
ATOM   1681 O OG1  . THR   A 1 71  ? 43.545 5.068   2.880   1.00 20.18 ?  71  THR   A OG1  1 
ATOM   1682 C CG2  . THR   A 1 71  ? 44.359 2.847   2.347   1.00 20.89 ?  71  THR   A CG2  1 
ATOM   1683 H H    . THR   A 1 71  ? 41.681 5.265   0.833   1.00 17.87 ?  71  THR   A H    1 
ATOM   1684 H HA   . THR   A 1 71  ? 44.278 4.773   0.412   1.00 20.28 ?  71  THR   A HA   1 
ATOM   1685 H HB   . THR   A 1 71  ? 42.449 3.572   2.206   1.00 23.17 ?  71  THR   A HB   1 
ATOM   1686 H HG1  . THR   A 1 71  ? 42.953 5.648   2.732   1.00 24.23 ?  71  THR   A HG1  1 
ATOM   1687 H HG21 . THR   A 1 71  ? 44.479 2.775   3.307   1.00 25.08 ?  71  THR   A HG21 1 
ATOM   1688 H HG22 . THR   A 1 71  ? 44.061 1.991   2.003   1.00 25.08 ?  71  THR   A HG22 1 
ATOM   1689 H HG23 . THR   A 1 71  ? 45.214 3.070   1.942   1.00 25.08 ?  71  THR   A HG23 1 
ATOM   1690 N N    . ASN   A 1 72  ? 42.070 2.636   -0.501  1.00 15.82 ?  72  ASN   A N    1 
ATOM   1691 C CA   . ASN   A 1 72  ? 41.851 1.313   -1.068  1.00 16.00 ?  72  ASN   A CA   1 
ATOM   1692 C C    . ASN   A 1 72  ? 41.232 1.307   -2.453  1.00 16.03 ?  72  ASN   A C    1 
ATOM   1693 O O    . ASN   A 1 72  ? 41.237 0.251   -3.102  1.00 17.38 ?  72  ASN   A O    1 
ATOM   1694 C CB   . ASN   A 1 72  ? 40.958 0.489   -0.135  1.00 17.11 ?  72  ASN   A CB   1 
ATOM   1695 C CG   . ASN   A 1 72  ? 41.563 0.330   1.228   1.00 18.46 ?  72  ASN   A CG   1 
ATOM   1696 O OD1  . ASN   A 1 72  ? 41.109 0.925   2.206   1.00 19.94 ?  72  ASN   A OD1  1 
ATOM   1697 N ND2  . ASN   A 1 72  ? 42.616 -0.451  1.301   1.00 18.92 ?  72  ASN   A ND2  1 
ATOM   1698 H H    . ASN   A 1 72  ? 41.342 3.052   -0.310  1.00 18.99 ?  72  ASN   A H    1 
ATOM   1699 H HA   . ASN   A 1 72  ? 42.703 0.861   -1.132  1.00 19.21 ?  72  ASN   A HA   1 
ATOM   1700 H HB2  . ASN   A 1 72  ? 40.103 0.933   -0.036  1.00 20.54 ?  72  ASN   A HB2  1 
ATOM   1701 H HB3  . ASN   A 1 72  ? 40.834 -0.395  -0.515  1.00 20.54 ?  72  ASN   A HB3  1 
ATOM   1702 H HD21 . ASN   A 1 72  ? 43.008 -0.578  2.057   1.00 22.71 ?  72  ASN   A HD21 1 
ATOM   1703 H HD22 . ASN   A 1 72  ? 42.911 -0.847  0.595   1.00 22.71 ?  72  ASN   A HD22 1 
ATOM   1704 N N    . GLY   A 1 73  ? 40.691 2.423   -2.919  1.00 15.24 ?  73  GLY   A N    1 
ATOM   1705 C CA   . GLY   A 1 73  ? 39.969 2.423   -4.164  1.00 14.95 ?  73  GLY   A CA   1 
ATOM   1706 C C    . GLY   A 1 73  ? 38.576 1.850   -4.001  1.00 14.43 ?  73  GLY   A C    1 
ATOM   1707 O O    . GLY   A 1 73  ? 38.177 1.413   -2.915  1.00 14.78 ?  73  GLY   A O    1 
ATOM   1708 H H    . GLY   A 1 73  ? 40.726 3.195   -2.530  1.00 18.29 ?  73  GLY   A H    1 
ATOM   1709 H HA2  . GLY   A 1 73  ? 39.904 3.335   -4.497  1.00 17.94 ?  73  GLY   A HA2  1 
ATOM   1710 H HA3  . GLY   A 1 73  ? 40.457 1.894   -4.819  1.00 17.94 ?  73  GLY   A HA3  1 
ATOM   1711 N N    . PRO   A 1 74  ? 37.810 1.860   -5.088  1.00 14.69 ?  74  PRO   A N    1 
ATOM   1712 C CA   . PRO   A 1 74  ? 36.411 1.439   -5.011  1.00 14.95 ?  74  PRO   A CA   1 
ATOM   1713 C C    . PRO   A 1 74  ? 36.246 -0.043  -4.704  1.00 14.18 ?  74  PRO   A C    1 
ATOM   1714 O O    . PRO   A 1 74  ? 37.117 -0.878  -4.967  1.00 14.95 ?  74  PRO   A O    1 
ATOM   1715 C CB   . PRO   A 1 74  ? 35.866 1.763   -6.406  1.00 16.84 ?  74  PRO   A CB   1 
ATOM   1716 C CG   . PRO   A 1 74  ? 36.830 2.717   -7.005  1.00 19.89 ?  74  PRO   A CG   1 
ATOM   1717 C CD   . PRO   A 1 74  ? 38.160 2.358   -6.427  1.00 16.77 ?  74  PRO   A CD   1 
ATOM   1718 H HA   . PRO   A 1 74  ? 35.945 1.960   -4.344  1.00 17.95 ?  74  PRO   A HA   1 
ATOM   1719 H HB2  . PRO   A 1 74  ? 35.816 0.947   -6.929  1.00 20.22 ?  74  PRO   A HB2  1 
ATOM   1720 H HB3  . PRO   A 1 74  ? 34.990 2.168   -6.319  1.00 20.22 ?  74  PRO   A HB3  1 
ATOM   1721 H HG2  . PRO   A 1 74  ? 36.837 2.612   -7.967  1.00 23.87 ?  74  PRO   A HG2  1 
ATOM   1722 H HG3  . PRO   A 1 74  ? 36.589 3.622   -6.758  1.00 23.87 ?  74  PRO   A HG3  1 
ATOM   1723 H HD2  . PRO   A 1 74  ? 38.589 1.660   -6.958  1.00 20.14 ?  74  PRO   A HD2  1 
ATOM   1724 H HD3  . PRO   A 1 74  ? 38.726 3.145   -6.367  1.00 20.14 ?  74  PRO   A HD3  1 
ATOM   1725 N N    . LEU   A 1 75  ? 35.077 -0.361  -4.151  1.00 13.48 ?  75  LEU   A N    1 
ATOM   1726 C CA   . LEU   A 1 75  ? 34.664 -1.748  -3.994  1.00 12.94 ?  75  LEU   A CA   1 
ATOM   1727 C C    . LEU   A 1 75  ? 34.277 -2.316  -5.355  1.00 13.40 ?  75  LEU   A C    1 
ATOM   1728 O O    . LEU   A 1 75  ? 34.168 -1.589  -6.349  1.00 14.74 ?  75  LEU   A O    1 
ATOM   1729 C CB   . LEU   A 1 75  ? 33.473 -1.850  -3.043  1.00 12.93 ?  75  LEU   A CB   1 
ATOM   1730 C CG   . LEU   A 1 75  ? 33.669 -1.451  -1.584  1.00 14.97 ?  75  LEU   A CG   1 
ATOM   1731 C CD1  . LEU   A 1 75  ? 32.410 -1.735  -0.782  1.00 17.15 ?  75  LEU   A CD1  1 
ATOM   1732 C CD2  . LEU   A 1 75  ? 34.845 -2.131  -0.958  1.00 18.49 ?  75  LEU   A CD2  1 
ATOM   1733 H H    . LEU   A 1 75  ? 34.506 0.214   -3.870  1.00 16.18 ?  75  LEU   A H    1 
ATOM   1734 H HA   . LEU   A 1 75  ? 35.404 -2.266  -3.645  1.00 15.53 ?  75  LEU   A HA   1 
ATOM   1735 H HB2  . LEU   A 1 75  ? 32.768 -1.291  -3.396  1.00 15.53 ?  75  LEU   A HB2  1 
ATOM   1736 H HB3  . LEU   A 1 75  ? 33.181 -2.772  -3.043  1.00 15.53 ?  75  LEU   A HB3  1 
ATOM   1737 H HG   . LEU   A 1 75  ? 33.839 -0.490  -1.544  1.00 17.97 ?  75  LEU   A HG   1 
ATOM   1738 H HD11 . LEU   A 1 75  ? 32.552 -1.466  0.139   1.00 20.58 ?  75  LEU   A HD11 1 
ATOM   1739 H HD12 . LEU   A 1 75  ? 31.675 -1.226  -1.164  1.00 20.58 ?  75  LEU   A HD12 1 
ATOM   1740 H HD13 . LEU   A 1 75  ? 32.217 -2.681  -0.828  1.00 20.58 ?  75  LEU   A HD13 1 
ATOM   1741 H HD21 . LEU   A 1 75  ? 34.878 -1.904  -0.016  1.00 22.19 ?  75  LEU   A HD21 1 
ATOM   1742 H HD22 . LEU   A 1 75  ? 34.749 -3.087  -1.068  1.00 22.19 ?  75  LEU   A HD22 1 
ATOM   1743 H HD23 . LEU   A 1 75  ? 35.660 -1.827  -1.396  1.00 22.19 ?  75  LEU   A HD23 1 
ATOM   1744 N N    . LYS   A 1 76  ? 34.063 -3.635  -5.381  1.00 14.25 ?  76  LYS   A N    1 
ATOM   1745 C CA   . LYS   A 1 76  ? 33.455 -4.338  -6.502  1.00 15.31 ?  76  LYS   A CA   1 
ATOM   1746 C C    . LYS   A 1 76  ? 31.947 -4.408  -6.293  1.00 13.44 ?  76  LYS   A C    1 
ATOM   1747 O O    . LYS   A 1 76  ? 31.478 -4.525  -5.162  1.00 13.42 ?  76  LYS   A O    1 
ATOM   1748 C CB   . LYS   A 1 76  ? 33.989 -5.784  -6.574  1.00 16.94 ?  76  LYS   A CB   1 
ATOM   1749 C CG   . LYS   A 1 76  ? 35.504 -5.895  -6.749  1.00 18.74 ?  76  LYS   A CG   1 
ATOM   1750 C CD   . LYS   A 1 76  ? 36.014 -7.311  -6.573  1.00 20.30 ?  76  LYS   A CD   1 
ATOM   1751 C CE   . LYS   A 1 76  ? 37.516 -7.381  -6.732  1.00 22.61 ?  76  LYS   A CE   1 
ATOM   1752 N NZ   . LYS   A 1 76  ? 38.019 -8.749  -6.519  1.00 23.43 ?  76  LYS   A NZ   1 
ATOM   1753 H H    . LYS   A 1 76  ? 34.280 -4.161  -4.730  1.00 17.11 ?  76  LYS   A H    1 
ATOM   1754 H HA   . LYS   A 1 76  ? 33.649 -3.878  -7.334  1.00 18.39 ?  76  LYS   A HA   1 
ATOM   1755 H HB2  . LYS   A 1 76  ? 33.751 -6.238  -5.750  1.00 20.33 ?  76  LYS   A HB2  1 
ATOM   1756 H HB3  . LYS   A 1 76  ? 33.570 -6.226  -7.325  1.00 20.33 ?  76  LYS   A HB3  1 
ATOM   1757 H HG2  . LYS   A 1 76  ? 35.739 -5.595  -7.639  1.00 22.50 ?  76  LYS   A HG2  1 
ATOM   1758 H HG3  . LYS   A 1 76  ? 35.939 -5.335  -6.085  1.00 22.50 ?  76  LYS   A HG3  1 
ATOM   1759 H HD2  . LYS   A 1 76  ? 35.781 -7.626  -5.686  1.00 24.37 ?  76  LYS   A HD2  1 
ATOM   1760 H HD3  . LYS   A 1 76  ? 35.606 -7.879  -7.248  1.00 24.37 ?  76  LYS   A HD3  1 
ATOM   1761 H HE2  . LYS   A 1 76  ? 37.754 -7.102  -7.629  1.00 27.14 ?  76  LYS   A HE2  1 
ATOM   1762 H HE3  . LYS   A 1 76  ? 37.930 -6.798  -6.076  1.00 27.14 ?  76  LYS   A HE3  1 
ATOM   1763 H HZ1  . LYS   A 1 76  ? 38.902 -8.773  -6.616  1.00 28.13 ?  76  LYS   A HZ1  1 
ATOM   1764 H HZ2  . LYS   A 1 76  ? 37.810 -9.031  -5.699  1.00 28.13 ?  76  LYS   A HZ2  1 
ATOM   1765 H HZ3  . LYS   A 1 76  ? 37.650 -9.308  -7.112  1.00 28.13 ?  76  LYS   A HZ3  1 
ATOM   1766 N N    . VAL   A 1 77  ? 31.190 -4.366  -7.394  1.00 13.64 ?  77  VAL   A N    1 
ATOM   1767 C CA   . VAL   A 1 77  ? 29.784 -4.752  -7.302  1.00 13.38 ?  77  VAL   A CA   1 
ATOM   1768 C C    . VAL   A 1 77  ? 29.721 -6.208  -6.868  1.00 13.08 ?  77  VAL   A C    1 
ATOM   1769 O O    . VAL   A 1 77  ? 30.370 -7.075  -7.462  1.00 13.86 ?  77  VAL   A O    1 
ATOM   1770 C CB   . VAL   A 1 77  ? 29.044 -4.525  -8.632  1.00 14.71 ?  77  VAL   A CB   1 
ATOM   1771 C CG1  . VAL   A 1 77  ? 27.576 -4.949  -8.510  1.00 15.21 ?  77  VAL   A CG1  1 
ATOM   1772 C CG2  . VAL   A 1 77  ? 29.146 -3.073  -9.057  1.00 16.50 ?  77  VAL   A CG2  1 
ATOM   1773 H H    . VAL   A 1 77  ? 31.459 -4.121  -8.171  1.00 16.38 ?  77  VAL   A H    1 
ATOM   1774 H HA   . VAL   A 1 77  ? 29.351 -4.216  -6.621  1.00 16.06 ?  77  VAL   A HA   1 
ATOM   1775 H HB   . VAL   A 1 77  ? 29.458 -5.070  -9.321  1.00 17.66 ?  77  VAL   A HB   1 
ATOM   1776 H HG11 . VAL   A 1 77  ? 27.095 -4.652  -9.298  1.00 18.26 ?  77  VAL   A HG11 1 
ATOM   1777 H HG12 . VAL   A 1 77  ? 27.525 -5.914  -8.435  1.00 18.26 ?  77  VAL   A HG12 1 
ATOM   1778 H HG13 . VAL   A 1 77  ? 27.193 -4.535  -7.717  1.00 18.26 ?  77  VAL   A HG13 1 
ATOM   1779 H HG21 . VAL   A 1 77  ? 28.621 -2.944  -9.861  1.00 19.80 ?  77  VAL   A HG21 1 
ATOM   1780 H HG22 . VAL   A 1 77  ? 28.808 -2.513  -8.343  1.00 19.80 ?  77  VAL   A HG22 1 
ATOM   1781 H HG23 . VAL   A 1 77  ? 30.078 -2.861  -9.233  1.00 19.80 ?  77  VAL   A HG23 1 
ATOM   1782 N N    . GLY   A 1 78  ? 28.945 -6.482  -5.822  1.00 12.84 ?  78  GLY   A N    1 
ATOM   1783 C CA   . GLY   A 1 78  ? 28.927 -7.774  -5.169  1.00 13.21 ?  78  GLY   A CA   1 
ATOM   1784 C C    . GLY   A 1 78  ? 29.831 -7.863  -3.960  1.00 12.60 ?  78  GLY   A C    1 
ATOM   1785 O O    . GLY   A 1 78  ? 29.767 -8.862  -3.225  1.00 13.83 ?  78  GLY   A O    1 
ATOM   1786 H H    . GLY   A 1 78  ? 28.396 -5.910  -5.476  1.00 15.41 ?  78  GLY   A H    1 
ATOM   1787 H HA2  . GLY   A 1 78  ? 28.022 -7.972  -4.891  1.00 15.86 ?  78  GLY   A HA2  1 
ATOM   1788 H HA3  . GLY   A 1 78  ? 29.205 -8.449  -5.807  1.00 15.86 ?  78  GLY   A HA3  1 
ATOM   1789 N N    . GLY   A 1 79  ? 30.681 -6.855  -3.738  1.00 12.72 ?  79  GLY   A N    1 
ATOM   1790 C CA   . GLY   A 1 79  ? 31.641 -6.876  -2.660  1.00 12.92 ?  79  GLY   A CA   1 
ATOM   1791 C C    . GLY   A 1 79  ? 31.186 -6.082  -1.445  1.00 12.26 ?  79  GLY   A C    1 
ATOM   1792 O O    . GLY   A 1 79  ? 30.077 -5.549  -1.385  1.00 13.32 ?  79  GLY   A O    1 
ATOM   1793 H H    . GLY   A 1 79  ? 30.717 -6.133  -4.214  1.00 15.27 ?  79  GLY   A H    1 
ATOM   1794 H HA2  . GLY   A 1 79  ? 31.797 -7.798  -2.392  1.00 15.51 ?  79  GLY   A HA2  1 
ATOM   1795 H HA3  . GLY   A 1 79  ? 32.484 -6.508  -2.972  1.00 15.51 ?  79  GLY   A HA3  1 
ATOM   1796 N N    . SER   A 1 80  ? 32.081 -6.007  -0.459  1.00 12.97 ?  80  SER   A N    1 
ATOM   1797 C CA   . SER   A 1 80  ? 31.760 -5.355  0.802   1.00 12.78 ?  80  SER   A CA   1 
ATOM   1798 C C    . SER   A 1 80  ? 33.028 -4.912  1.511   1.00 12.52 ?  80  SER   A C    1 
ATOM   1799 O O    . SER   A 1 80  ? 34.133 -5.356  1.193   1.00 14.57 ?  80  SER   A O    1 
ATOM   1800 C CB   . SER   A 1 80  ? 30.982 -6.297  1.727   1.00 14.06 ?  80  SER   A CB   1 
ATOM   1801 O OG   . SER   A 1 80  ? 31.794 -7.356  2.203   1.00 15.69 ?  80  SER   A OG   1 
ATOM   1802 H H    . SER   A 1 80  ? 32.883 -6.328  -0.495  1.00 15.57 ?  80  SER   A H    1 
ATOM   1803 H HA   . SER   A 1 80  ? 31.216 -4.576  0.615   1.00 15.35 ?  80  SER   A HA   1 
ATOM   1804 H HB2  . SER   A 1 80  ? 30.654 -5.789  2.488   1.00 16.88 ?  80  SER   A HB2  1 
ATOM   1805 H HB3  . SER   A 1 80  ? 30.229 -6.670  1.237   1.00 16.88 ?  80  SER   A HB3  1 
ATOM   1806 H HG   . SER   A 1 80  ? 32.082 -7.807  1.549   1.00 18.83 ?  80  SER   A HG   1 
ATOM   1807 N N    . CYS   A 1 81  ? 32.841 -4.061  2.515   1.00 12.32 ?  81  CYS   A N    1 
ATOM   1808 C CA   . CYS   A 1 81  ? 33.893 -3.774  3.474   1.00 12.89 ?  81  CYS   A CA   1 
ATOM   1809 C C    . CYS   A 1 81  ? 33.244 -3.528  4.829   1.00 12.39 ?  81  CYS   A C    1 
ATOM   1810 O O    . CYS   A 1 81  ? 32.082 -3.109  4.906   1.00 13.76 ?  81  CYS   A O    1 
ATOM   1811 C CB   . CYS   A 1 81  ? 34.773 -2.592  3.046   1.00 14.00 ?  81  CYS   A CB   1 
ATOM   1812 S SG   . CYS   A 1 81  ? 33.895 -1.011  3.039   1.00 14.00 ?  81  CYS   A SG   1 
ATOM   1813 H H    . CYS   A 1 81  ? 32.106 -3.638  2.663   1.00 14.80 ?  81  CYS   A H    1 
ATOM   1814 H HA   . CYS   A 1 81  ? 34.465 -4.554  3.556   1.00 15.47 ?  81  CYS   A HA   1 
ATOM   1815 H HB2  . CYS   A 1 81  ? 35.519 -2.519  3.665   1.00 16.81 ?  81  CYS   A HB2  1 
ATOM   1816 H HB3  . CYS   A 1 81  ? 35.106 -2.760  2.151   1.00 16.81 ?  81  CYS   A HB3  1 
ATOM   1817 H HG   . CYS   A 1 81  ? 34.658 -0.148  2.692   1.00 16.81 ?  81  CYS   A HG   1 
ATOM   1818 N N    . VAL   A 1 82  ? 33.999 -3.796  5.892   1.00 12.95 ?  82  VAL   A N    1 
ATOM   1819 C CA   . VAL   A 1 82  ? 33.570 -3.543  7.260   1.00 13.25 ?  82  VAL   A CA   1 
ATOM   1820 C C    . VAL   A 1 82  ? 34.187 -2.234  7.727   1.00 13.76 ?  82  VAL   A C    1 
ATOM   1821 O O    . VAL   A 1 82  ? 35.414 -2.077  7.719   1.00 14.80 ?  82  VAL   A O    1 
ATOM   1822 C CB   . VAL   A 1 82  ? 33.984 -4.680  8.201   1.00 15.10 ?  82  VAL   A CB   1 
ATOM   1823 C CG1  . VAL   A 1 82  ? 33.529 -4.384  9.621   1.00 16.72 ?  82  VAL   A CG1  1 
ATOM   1824 C CG2  . VAL   A 1 82  ? 33.430 -6.012  7.722   1.00 15.92 ?  82  VAL   A CG2  1 
ATOM   1825 H H    . VAL   A 1 82  ? 34.790 -4.149  5.840   1.00 15.55 ?  82  VAL   A H    1 
ATOM   1826 H HA   . VAL   A 1 82  ? 32.605 -3.457  7.281   1.00 15.91 ?  82  VAL   A HA   1 
ATOM   1827 H HB   . VAL   A 1 82  ? 34.951 -4.743  8.208   1.00 18.13 ?  82  VAL   A HB   1 
ATOM   1828 H HG11 . VAL   A 1 82  ? 33.613 -5.189  10.153  1.00 20.08 ?  82  VAL   A HG11 1 
ATOM   1829 H HG12 . VAL   A 1 82  ? 34.085 -3.682  9.997   1.00 20.08 ?  82  VAL   A HG12 1 
ATOM   1830 H HG13 . VAL   A 1 82  ? 32.601 -4.096  9.603   1.00 20.08 ?  82  VAL   A HG13 1 
ATOM   1831 H HG21 . VAL   A 1 82  ? 33.662 -6.698  8.365   1.00 19.11 ?  82  VAL   A HG21 1 
ATOM   1832 H HG22 . VAL   A 1 82  ? 32.466 -5.941  7.645   1.00 19.11 ?  82  VAL   A HG22 1 
ATOM   1833 H HG23 . VAL   A 1 82  ? 33.817 -6.221  6.858   1.00 19.11 ?  82  VAL   A HG23 1 
ATOM   1834 N N    . LEU   A 1 83  ? 33.340 -1.299  8.141   1.00 13.37 ?  83  LEU   A N    1 
ATOM   1835 C CA   . LEU   A 1 83  ? 33.770 -0.038  8.716   1.00 13.32 ?  83  LEU   A CA   1 
ATOM   1836 C C    . LEU   A 1 83  ? 33.054 0.141   10.052  1.00 13.59 ?  83  LEU   A C    1 
ATOM   1837 O O    . LEU   A 1 83  ? 32.312 -0.739  10.509  1.00 13.98 ?  83  LEU   A O    1 
ATOM   1838 C CB   . LEU   A 1 83  ? 33.528 1.116   7.729   1.00 14.17 ?  83  LEU   A CB   1 
ATOM   1839 C CG   . LEU   A 1 83  ? 34.443 1.115   6.495   1.00 14.79 ?  83  LEU   A CG   1 
ATOM   1840 C CD1  . LEU   A 1 83  ? 34.060 2.215   5.509   1.00 15.96 ?  83  LEU   A CD1  1 
ATOM   1841 C CD2  . LEU   A 1 83  ? 35.915 1.258   6.902   1.00 15.59 ?  83  LEU   A CD2  1 
ATOM   1842 H H    . LEU   A 1 83  ? 32.484 -1.382  8.107   1.00 16.05 ?  83  LEU   A H    1 
ATOM   1843 H HA   . LEU   A 1 83  ? 34.725 -0.078  8.893   1.00 15.99 ?  83  LEU   A HA   1 
ATOM   1844 H HB2  . LEU   A 1 83  ? 32.612 1.063   7.407   1.00 17.02 ?  83  LEU   A HB2  1 
ATOM   1845 H HB3  . LEU   A 1 83  ? 33.659 1.958   8.189   1.00 17.02 ?  83  LEU   A HB3  1 
ATOM   1846 H HG   . LEU   A 1 83  ? 34.348 0.268   6.036   1.00 17.75 ?  83  LEU   A HG   1 
ATOM   1847 H HD11 . LEU   A 1 83  ? 34.662 2.179   4.742   1.00 19.15 ?  83  LEU   A HD11 1 
ATOM   1848 H HD12 . LEU   A 1 83  ? 33.149 2.081   5.218   1.00 19.15 ?  83  LEU   A HD12 1 
ATOM   1849 H HD13 . LEU   A 1 83  ? 34.148 3.079   5.946   1.00 19.15 ?  83  LEU   A HD13 1 
ATOM   1850 H HD21 . LEU   A 1 83  ? 36.444 1.458   6.114   1.00 18.72 ?  83  LEU   A HD21 1 
ATOM   1851 H HD22 . LEU   A 1 83  ? 35.996 1.975   7.548   1.00 18.72 ?  83  LEU   A HD22 1 
ATOM   1852 H HD23 . LEU   A 1 83  ? 36.214 0.422   7.296   1.00 18.72 ?  83  LEU   A HD23 1 
ATOM   1853 N N    . SER   A 1 84  ? 33.291 1.280   10.694  1.00 14.23 ?  84  SER   A N    1 
ATOM   1854 C CA   . SER   A 1 84  ? 32.638 1.550   11.966  1.00 14.28 ?  84  SER   A CA   1 
ATOM   1855 C C    . SER   A 1 84  ? 31.123 1.659   11.805  1.00 14.35 ?  84  SER   A C    1 
ATOM   1856 O O    . SER   A 1 84  ? 30.612 2.134   10.788  1.00 14.42 ?  84  SER   A O    1 
ATOM   1857 C CB   . SER   A 1 84  ? 33.142 2.868   12.536  1.00 15.59 ?  84  SER   A CB   1 
ATOM   1858 O OG   . SER   A 1 84  ? 32.506 3.152   13.766  1.00 16.81 ?  84  SER   A OG   1 
ATOM   1859 H H    . SER   A 1 84  ? 33.823 1.902   10.415  1.00 17.08 ?  84  SER   A H    1 
ATOM   1860 H HA   . SER   A 1 84  ? 32.848 0.837   12.592  1.00 17.14 ?  84  SER   A HA   1 
ATOM   1861 H HB2  . SER   A 1 84  ? 34.100 2.810   12.680  1.00 18.72 ?  84  SER   A HB2  1 
ATOM   1862 H HB3  . SER   A 1 84  ? 32.947 3.579   11.901  1.00 18.72 ?  84  SER   A HB3  1 
ATOM   1863 H HG   . SER   A 1 84  ? 32.785 3.889   14.070  1.00 20.18 ?  84  SER   A HG   1 
ATOM   1864 N N    . GLY   A 1 85  ? 30.402 1.251   12.845  1.00 15.22 ?  85  GLY   A N    1 
ATOM   1865 C CA   . GLY   A 1 85  ? 28.983 1.506   12.918  1.00 15.87 ?  85  GLY   A CA   1 
ATOM   1866 C C    . GLY   A 1 85  ? 28.628 2.822   13.569  1.00 15.14 ?  85  GLY   A C    1 
ATOM   1867 O O    . GLY   A 1 85  ? 27.443 3.150   13.670  1.00 15.95 ?  85  GLY   A O    1 
ATOM   1868 H H    . GLY   A 1 85  ? 30.722 0.817   13.519  1.00 18.27 ?  85  GLY   A H    1 
ATOM   1869 H HA2  . GLY   A 1 85  ? 28.618 1.499   12.018  1.00 19.06 ?  85  GLY   A HA2  1 
ATOM   1870 H HA3  . GLY   A 1 85  ? 28.561 0.791   13.416  1.00 19.06 ?  85  GLY   A HA3  1 
ATOM   1871 N N    . HIS   A 1 86  ? 29.617 3.581   14.029  1.00 14.94 ?  86  HIS   A N    1 
ATOM   1872 C CA   . HIS   A 1 86  ? 29.395 4.917   14.594  1.00 15.87 ?  86  HIS   A CA   1 
ATOM   1873 C C    . HIS   A 1 86  ? 28.399 4.801   15.740  1.00 16.74 ?  86  HIS   A C    1 
ATOM   1874 O O    . HIS   A 1 86  ? 28.565 3.909   16.586  1.00 17.83 ?  86  HIS   A O    1 
ATOM   1875 C CB   . HIS   A 1 86  ? 29.039 5.899   13.488  1.00 16.08 ?  86  HIS   A CB   1 
ATOM   1876 C CG   . HIS   A 1 86  ? 30.096 5.981   12.447  1.00 16.30 ?  86  HIS   A CG   1 
ATOM   1877 N ND1  . HIS   A 1 86  ? 31.188 6.811   12.574  1.00 17.91 ?  86  HIS   A ND1  1 
ATOM   1878 C CD2  . HIS   A 1 86  ? 30.276 5.286   11.302  1.00 16.12 ?  86  HIS   A CD2  1 
ATOM   1879 C CE1  . HIS   A 1 86  ? 31.982 6.644   11.530  1.00 17.77 ?  86  HIS   A CE1  1 
ATOM   1880 N NE2  . HIS   A 1 86  ? 31.457 5.716   10.750  1.00 16.49 ?  86  HIS   A NE2  1 
ATOM   1881 H H    . HIS   A 1 86  ? 30.440 3.342   14.030  1.00 17.93 ?  86  HIS   A H    1 
ATOM   1882 H HA   . HIS   A 1 86  ? 30.230 5.219   14.973  1.00 19.05 ?  86  HIS   A HA   1 
ATOM   1883 H HB2  . HIS   A 1 86  ? 28.215 5.620   13.056  1.00 19.30 ?  86  HIS   A HB2  1 
ATOM   1884 H HB3  . HIS   A 1 86  ? 28.925 6.787   13.868  1.00 19.30 ?  86  HIS   A HB3  1 
ATOM   1885 H HD2  . HIS   A 1 86  ? 29.714 4.631   10.953  1.00 19.35 ?  86  HIS   A HD2  1 
ATOM   1886 H HE1  . HIS   A 1 86  ? 32.778 7.101   11.365  1.00 21.33 ?  86  HIS   A HE1  1 
ATOM   1887 H HE2  . HIS   A 1 86  ? 31.795 5.440   10.001  1.00 19.79 ?  86  HIS   A HE2  1 
ATOM   1888 N N    . ASN   A 1 87  ? 27.385 5.655   15.804  1.00 16.95 ?  87  ASN   A N    1 
ATOM   1889 C CA   . ASN   A 1 87  ? 26.398 5.642   16.870  1.00 18.01 ?  87  ASN   A CA   1 
ATOM   1890 C C    . ASN   A 1 87  ? 25.273 4.646   16.629  1.00 19.15 ?  87  ASN   A C    1 
ATOM   1891 O O    . ASN   A 1 87  ? 24.363 4.556   17.457  1.00 21.93 ?  87  ASN   A O    1 
ATOM   1892 C CB   . ASN   A 1 87  ? 25.804 7.047   17.031  1.00 19.00 ?  87  ASN   A CB   1 
ATOM   1893 C CG   . ASN   A 1 87  ? 25.287 7.618   15.717  1.00 19.70 ?  87  ASN   A CG   1 
ATOM   1894 O OD1  . ASN   A 1 87  ? 25.934 7.504   14.678  1.00 20.28 ?  87  ASN   A OD1  1 
ATOM   1895 N ND2  . ASN   A 1 87  ? 24.116 8.234   15.762  1.00 20.46 ?  87  ASN   A ND2  1 
ATOM   1896 H H    . ASN   A 1 87  ? 27.237 6.264   15.212  1.00 20.35 ?  87  ASN   A H    1 
ATOM   1897 H HA   . ASN   A 1 87  ? 26.834 5.405   17.704  1.00 21.62 ?  87  ASN   A HA   1 
ATOM   1898 H HB2  . ASN   A 1 87  ? 25.061 7.007   17.658  1.00 22.81 ?  87  ASN   A HB2  1 
ATOM   1899 H HB3  . ASN   A 1 87  ? 26.489 7.645   17.373  1.00 22.81 ?  87  ASN   A HB3  1 
ATOM   1900 H HD21 . ASN   A 1 87  ? 23.783 8.570   15.046  1.00 24.56 ?  87  ASN   A HD21 1 
ATOM   1901 H HD22 . ASN   A 1 87  ? 23.689 8.296   16.507  1.00 24.56 ?  87  ASN   A HD22 1 
ATOM   1902 N N    . LEU   A 1 88  ? 25.319 3.891   15.538  1.00 17.32 ?  88  LEU   A N    1 
ATOM   1903 C CA   . LEU   A 1 88  ? 24.211 3.032   15.135  1.00 17.84 ?  88  LEU   A CA   1 
ATOM   1904 C C    . LEU   A 1 88  ? 24.427 1.556   15.435  1.00 17.22 ?  88  LEU   A C    1 
ATOM   1905 O O    . LEU   A 1 88  ? 23.448 0.825   15.610  1.00 18.54 ?  88  LEU   A O    1 
ATOM   1906 C CB   . LEU   A 1 88  ? 23.981 3.176   13.632  1.00 18.34 ?  88  LEU   A CB   1 
ATOM   1907 C CG   . LEU   A 1 88  ? 23.653 4.586   13.143  1.00 20.03 ?  88  LEU   A CG   1 
ATOM   1908 C CD1  . LEU   A 1 88  ? 23.532 4.602   11.628  1.00 20.95 ?  88  LEU   A CD1  1 
ATOM   1909 C CD2  . LEU   A 1 88  ? 22.375 5.100   13.788  1.00 21.68 ?  88  LEU   A CD2  1 
ATOM   1910 H H    . LEU   A 1 88  ? 26.000 3.853   15.016  1.00 20.79 ?  88  LEU   A H    1 
ATOM   1911 H HA   . LEU   A 1 88  ? 23.407 3.317   15.595  1.00 21.42 ?  88  LEU   A HA   1 
ATOM   1912 H HB2  . LEU   A 1 88  ? 24.781 2.893   13.168  1.00 22.01 ?  88  LEU   A HB2  1 
ATOM   1913 H HB3  . LEU   A 1 88  ? 23.238 2.607   13.380  1.00 22.01 ?  88  LEU   A HB3  1 
ATOM   1914 H HG   . LEU   A 1 88  ? 24.374 5.186   13.389  1.00 24.04 ?  88  LEU   A HG   1 
ATOM   1915 H HD11 . LEU   A 1 88  ? 23.360 5.509   11.331  1.00 25.15 ?  88  LEU   A HD11 1 
ATOM   1916 H HD12 . LEU   A 1 88  ? 24.359 4.277   11.240  1.00 25.15 ?  88  LEU   A HD12 1 
ATOM   1917 H HD13 . LEU   A 1 88  ? 22.795 4.025   11.365  1.00 25.15 ?  88  LEU   A HD13 1 
ATOM   1918 H HD21 . LEU   A 1 88  ? 22.123 5.936   13.365  1.00 26.03 ?  88  LEU   A HD21 1 
ATOM   1919 H HD22 . LEU   A 1 88  ? 21.674 4.442   13.664  1.00 26.03 ?  88  LEU   A HD22 1 
ATOM   1920 H HD23 . LEU   A 1 88  ? 22.535 5.241   14.733  1.00 26.03 ?  88  LEU   A HD23 1 
ATOM   1921 N N    . ALA   A 1 89  ? 25.671 1.097   15.468  1.00 16.27 ?  89  ALA   A N    1 
ATOM   1922 C CA   . ALA   A 1 89  ? 26.008 -0.316  15.577  1.00 16.48 ?  89  ALA   A CA   1 
ATOM   1923 C C    . ALA   A 1 89  ? 27.491 -0.393  15.899  1.00 17.19 ?  89  ALA   A C    1 
ATOM   1924 O O    . ALA   A 1 89  ? 28.217 0.594   15.767  1.00 17.63 ?  89  ALA   A O    1 
ATOM   1925 C CB   . ALA   A 1 89  ? 25.732 -1.035  14.257  1.00 16.68 ?  89  ALA   A CB   1 
ATOM   1926 H H    . ALA   A 1 89  ? 26.363 1.605   15.415  1.00 19.54 ?  89  ALA   A H    1 
ATOM   1927 H HA   . ALA   A 1 89  ? 25.494 -0.730  16.291  1.00 19.78 ?  89  ALA   A HA   1 
ATOM   1928 H HB1  . ALA   A 1 89  ? 25.972 -1.972  14.354  1.00 20.02 ?  89  ALA   A HB1  1 
ATOM   1929 H HB2  . ALA   A 1 89  ? 24.787 -0.960  14.043  1.00 20.02 ?  89  ALA   A HB2  1 
ATOM   1930 H HB3  . ALA   A 1 89  ? 26.264 -0.629  13.558  1.00 20.02 ?  89  ALA   A HB3  1 
ATOM   1931 N N    . LYS   A 1 90  ? 27.956 -1.570  16.305  1.00 17.75 ?  90  LYS   A N    1 
ATOM   1932 C CA   . LYS   A 1 90  ? 29.400 -1.736  16.451  1.00 18.48 ?  90  LYS   A CA   1 
ATOM   1933 C C    . LYS   A 1 90  ? 30.100 -1.542  15.109  1.00 17.07 ?  90  LYS   A C    1 
ATOM   1934 O O    . LYS   A 1 90  ? 31.047 -0.746  14.991  1.00 18.01 ?  90  LYS   A O    1 
ATOM   1935 C CB   . LYS   A 1 90  ? 29.727 -3.105  17.051  1.00 21.14 ?  90  LYS   A CB   1 
ATOM   1936 C CG   . LYS   A 1 90  ? 31.208 -3.283  17.365  1.00 26.45 ?  90  LYS   A CG   1 
ATOM   1937 C CD   . LYS   A 1 90  ? 31.447 -4.524  18.210  1.00 32.12 ?  90  LYS   A CD   1 
ATOM   1938 C CE   . LYS   A 1 90  ? 32.835 -4.526  18.836  1.00 36.81 ?  90  LYS   A CE   1 
ATOM   1939 N NZ   . LYS   A 1 90  ? 33.909 -4.828  17.850  1.00 39.88 ?  90  LYS   A NZ   1 
ATOM   1940 H H    . LYS   A 1 90  ? 27.476 -2.252  16.503  1.00 21.31 ?  90  LYS   A H    1 
ATOM   1941 H HA   . LYS   A 1 90  ? 29.733 -1.060  17.060  1.00 22.19 ?  90  LYS   A HA   1 
ATOM   1942 H HB2  . LYS   A 1 90  ? 29.228 -3.214  17.879  1.00 25.37 ?  90  LYS   A HB2  1 
ATOM   1943 H HB3  . LYS   A 1 90  ? 29.467 -3.797  16.421  1.00 25.37 ?  90  LYS   A HB3  1 
ATOM   1944 H HG2  . LYS   A 1 90  ? 31.702 -3.378  16.536  1.00 31.75 ?  90  LYS   A HG2  1 
ATOM   1945 H HG3  . LYS   A 1 90  ? 31.524 -2.511  17.860  1.00 31.75 ?  90  LYS   A HG3  1 
ATOM   1946 H HD2  . LYS   A 1 90  ? 30.791 -4.557  18.924  1.00 38.55 ?  90  LYS   A HD2  1 
ATOM   1947 H HD3  . LYS   A 1 90  ? 31.367 -5.312  17.648  1.00 38.55 ?  90  LYS   A HD3  1 
ATOM   1948 H HE2  . LYS   A 1 90  ? 33.013 -3.651  19.216  1.00 44.18 ?  90  LYS   A HE2  1 
ATOM   1949 H HE3  . LYS   A 1 90  ? 32.867 -5.201  19.532  1.00 44.18 ?  90  LYS   A HE3  1 
ATOM   1950 H HZ1  . LYS   A 1 90  ? 33.775 -5.633  17.492  1.00 47.86 ?  90  LYS   A HZ1  1 
ATOM   1951 H HZ2  . LYS   A 1 90  ? 33.907 -4.219  17.202  1.00 47.86 ?  90  LYS   A HZ2  1 
ATOM   1952 H HZ3  . LYS   A 1 90  ? 34.703 -4.821  18.252  1.00 47.86 ?  90  LYS   A HZ3  1 
ATOM   1953 N N    . HIS   A 1 91  ? 29.624 -2.242  14.082  1.00 15.25 ?  91  HIS   A N    1 
ATOM   1954 C CA   . HIS   A 1 91  ? 30.207 -2.241  12.754  1.00 14.65 ?  91  HIS   A CA   1 
ATOM   1955 C C    . HIS   A 1 91  ? 29.124 -1.958  11.731  1.00 13.03 ?  91  HIS   A C    1 
ATOM   1956 O O    . HIS   A 1 91  ? 27.953 -2.306  11.924  1.00 14.48 ?  91  HIS   A O    1 
ATOM   1957 C CB   . HIS   A 1 91  ? 30.783 -3.614  12.391  1.00 17.37 ?  91  HIS   A CB   1 
ATOM   1958 C CG   . HIS   A 1 91  ? 31.834 -4.097  13.332  1.00 21.67 ?  91  HIS   A CG   1 
ATOM   1959 N ND1  . HIS   A 1 91  ? 33.092 -3.540  13.390  1.00 24.08 ?  91  HIS   A ND1  1 
ATOM   1960 C CD2  . HIS   A 1 91  ? 31.820 -5.094  14.246  1.00 24.00 ?  91  HIS   A CD2  1 
ATOM   1961 C CE1  . HIS   A 1 91  ? 33.809 -4.171  14.303  1.00 25.62 ?  91  HIS   A CE1  1 
ATOM   1962 N NE2  . HIS   A 1 91  ? 33.060 -5.119  14.838  1.00 25.72 ?  91  HIS   A NE2  1 
ATOM   1963 H H    . HIS   A 1 91  ? 28.936 -2.764  14.144  1.00 18.31 ?  91  HIS   A H    1 
ATOM   1964 H HA   . HIS   A 1 91  ? 30.905 -1.574  12.690  1.00 17.58 ?  91  HIS   A HA   1 
ATOM   1965 H HB2  . HIS   A 1 91  ? 30.061 -4.265  12.393  1.00 20.85 ?  91  HIS   A HB2  1 
ATOM   1966 H HB3  . HIS   A 1 91  ? 31.174 -3.563  11.505  1.00 20.85 ?  91  HIS   A HB3  1 
ATOM   1967 H HD1  . HIS   A 1 91  ? 33.369 -2.885  12.903  1.00 28.90 ?  91  HIS   A HD1  1 
ATOM   1968 H HD2  . HIS   A 1 91  ? 31.109 -5.655  14.443  1.00 28.81 ?  91  HIS   A HD2  1 
ATOM   1969 H HE1  . HIS   A 1 91  ? 34.694 -3.977  14.530  1.00 30.76 ?  91  HIS   A HE1  1 
ATOM   1970 N N    . CYS   A 1 92  ? 29.533 -1.371  10.614  1.00 12.99 ?  92  CYS   A N    1 
ATOM   1971 C CA   . CYS   A 1 92  ? 28.694 -1.280  9.432   1.00 13.13 ?  92  CYS   A CA   1 
ATOM   1972 C C    . CYS   A 1 92  ? 29.331 -2.102  8.324   1.00 12.67 ?  92  CYS   A C    1 
ATOM   1973 O O    . CYS   A 1 92  ? 30.494 -1.872  7.963   1.00 13.27 ?  92  CYS   A O    1 
ATOM   1974 C CB   . CYS   A 1 92  ? 28.528 0.164   8.966   1.00 13.63 ?  92  CYS   A CB   1 
ATOM   1975 S SG   . CYS   A 1 92  ? 27.490 0.276   7.462   1.00 13.20 ?  92  CYS   A SG   1 
ATOM   1976 H H    . CYS   A 1 92  ? 30.315 -1.012  10.513  1.00 15.59 ?  92  CYS   A H    1 
ATOM   1977 H HA   . CYS   A 1 92  ? 27.818 -1.642  9.627   1.00 15.76 ?  92  CYS   A HA   1 
ATOM   1978 H HB2  . CYS   A 1 92  ? 28.100 0.685   9.665   1.00 16.37 ?  92  CYS   A HB2  1 
ATOM   1979 H HB3  . CYS   A 1 92  ? 29.399 0.541   8.757   1.00 16.37 ?  92  CYS   A HB3  1 
ATOM   1980 H HG   . CYS   A 1 92  ? 27.378 1.430   7.150   1.00 15.84 ?  92  CYS   A HG   1 
ATOM   1981 N N    . LEU   A 1 93  ? 28.587 -3.078  7.820   1.00 12.26 ?  93  LEU   A N    1 
ATOM   1982 C CA   . LEU   A 1 93  ? 29.000 -3.847  6.656   1.00 12.11 ?  93  LEU   A CA   1 
ATOM   1983 C C    . LEU   A 1 93  ? 28.424 -3.161  5.422   1.00 11.77 ?  93  LEU   A C    1 
ATOM   1984 O O    . LEU   A 1 93  ? 27.215 -3.207  5.184   1.00 11.95 ?  93  LEU   A O    1 
ATOM   1985 C CB   . LEU   A 1 93  ? 28.517 -5.291  6.773   1.00 13.03 ?  93  LEU   A CB   1 
ATOM   1986 C CG   . LEU   A 1 93  ? 28.892 -6.199  5.602   1.00 13.30 ?  93  LEU   A CG   1 
ATOM   1987 C CD1  . LEU   A 1 93  ? 30.403 -6.468  5.562   1.00 14.30 ?  93  LEU   A CD1  1 
ATOM   1988 C CD2  . LEU   A 1 93  ? 28.109 -7.514  5.658   1.00 14.25 ?  93  LEU   A CD2  1 
ATOM   1989 H H    . LEU   A 1 93  ? 27.815 -3.310  8.136   1.00 14.72 ?  93  LEU   A H    1 
ATOM   1990 H HA   . LEU   A 1 93  ? 29.964 -3.844  6.592   1.00 14.54 ?  93  LEU   A HA   1 
ATOM   1991 H HB2  . LEU   A 1 93  ? 28.900 -5.676  7.579   1.00 15.64 ?  93  LEU   A HB2  1 
ATOM   1992 H HB3  . LEU   A 1 93  ? 27.550 -5.288  6.845   1.00 15.64 ?  93  LEU   A HB3  1 
ATOM   1993 H HG   . LEU   A 1 93  ? 28.654 -5.756  4.777   1.00 15.97 ?  93  LEU   A HG   1 
ATOM   1994 H HD11 . LEU   A 1 93  ? 30.601 -7.073  4.827   1.00 17.17 ?  93  LEU   A HD11 1 
ATOM   1995 H HD12 . LEU   A 1 93  ? 30.875 -5.631  5.434   1.00 17.17 ?  93  LEU   A HD12 1 
ATOM   1996 H HD13 . LEU   A 1 93  ? 30.679 -6.876  6.402   1.00 17.17 ?  93  LEU   A HD13 1 
ATOM   1997 H HD21 . LEU   A 1 93  ? 28.369 -8.070  4.903   1.00 17.11 ?  93  LEU   A HD21 1 
ATOM   1998 H HD22 . LEU   A 1 93  ? 28.310 -7.973  6.488   1.00 17.11 ?  93  LEU   A HD22 1 
ATOM   1999 H HD23 . LEU   A 1 93  ? 27.158 -7.321  5.608   1.00 17.11 ?  93  LEU   A HD23 1 
ATOM   2000 N N    . HIS   A 1 94  ? 29.281 -2.479  4.662   1.00 11.42 ?  94  HIS   A N    1 
ATOM   2001 C CA   . HIS   A 1 94  ? 28.870 -1.805  3.432   1.00 11.51 ?  94  HIS   A CA   1 
ATOM   2002 C C    . HIS   A 1 94  ? 28.881 -2.845  2.328   1.00 11.40 ?  94  HIS   A C    1 
ATOM   2003 O O    . HIS   A 1 94  ? 29.947 -3.360  1.987   1.00 13.28 ?  94  HIS   A O    1 
ATOM   2004 C CB   . HIS   A 1 94  ? 29.840 -0.669  3.106   1.00 11.47 ?  94  HIS   A CB   1 
ATOM   2005 C CG   . HIS   A 1 94  ? 29.833 0.419   4.124   1.00 11.57 ?  94  HIS   A CG   1 
ATOM   2006 N ND1  . HIS   A 1 94  ? 28.967 1.492   4.063   1.00 11.87 ?  94  HIS   A ND1  1 
ATOM   2007 C CD2  . HIS   A 1 94  ? 30.565 0.583   5.247   1.00 12.67 ?  94  HIS   A CD2  1 
ATOM   2008 C CE1  . HIS   A 1 94  ? 29.180 2.273   5.106   1.00 12.25 ?  94  HIS   A CE1  1 
ATOM   2009 N NE2  . HIS   A 1 94  ? 30.143 1.743   5.841   1.00 12.52 ?  94  HIS   A NE2  1 
ATOM   2010 H H    . HIS   A 1 94  ? 30.122 -2.393  4.835   1.00 13.71 ?  94  HIS   A H    1 
ATOM   2011 H HA   . HIS   A 1 94  ? 27.971 -1.446  3.527   1.00 13.82 ?  94  HIS   A HA   1 
ATOM   2012 H HB2  . HIS   A 1 94  ? 30.735 -1.023  3.056   1.00 13.78 ?  94  HIS   A HB2  1 
ATOM   2013 H HB3  . HIS   A 1 94  ? 29.588 -0.275  2.252   1.00 13.78 ?  94  HIS   A HB3  1 
ATOM   2014 H HD2  . HIS   A 1 94  ? 31.228 0.015   5.561   1.00 15.21 ?  94  HIS   A HD2  1 
ATOM   2015 H HE1  . HIS   A 1 94  ? 28.726 3.065   5.291   1.00 14.70 ?  94  HIS   A HE1  1 
ATOM   2016 H HE2  . HIS   A 1 94  ? 30.455 2.078   6.571   1.00 15.03 ?  94  HIS   A HE2  1 
ATOM   2017 N N    . VAL   A 1 95  ? 27.714 -3.172  1.784   1.00 10.97 ?  95  VAL   A N    1 
ATOM   2018 C CA   . VAL   A 1 95  ? 27.578 -4.208  0.767   1.00 11.35 ?  95  VAL   A CA   1 
ATOM   2019 C C    . VAL   A 1 95  ? 27.044 -3.570  -0.503  1.00 11.03 ?  95  VAL   A C    1 
ATOM   2020 O O    . VAL   A 1 95  ? 26.056 -2.826  -0.453  1.00 11.52 ?  95  VAL   A O    1 
ATOM   2021 C CB   . VAL   A 1 95  ? 26.624 -5.334  1.215   1.00 12.00 ?  95  VAL   A CB   1 
ATOM   2022 C CG1  . VAL   A 1 95  ? 26.496 -6.372  0.113   1.00 13.26 ?  95  VAL   A CG1  1 
ATOM   2023 C CG2  . VAL   A 1 95  ? 27.102 -5.955  2.512   1.00 12.75 ?  95  VAL   A CG2  1 
ATOM   2024 H H    . VAL   A 1 95  ? 26.961 -2.804  1.989   1.00 13.17 ?  95  VAL   A H    1 
ATOM   2025 H HA   . VAL   A 1 95  ? 28.442 -4.600  0.572   1.00 13.62 ?  95  VAL   A HA   1 
ATOM   2026 H HB   . VAL   A 1 95  ? 25.744 -4.960  1.371   1.00 14.41 ?  95  VAL   A HB   1 
ATOM   2027 H HG11 . VAL   A 1 95  ? 26.108 -7.181  0.485   1.00 15.92 ?  95  VAL   A HG11 1 
ATOM   2028 H HG12 . VAL   A 1 95  ? 25.918 -6.025  -0.587  1.00 15.92 ?  95  VAL   A HG12 1 
ATOM   2029 H HG13 . VAL   A 1 95  ? 27.375 -6.564  -0.246  1.00 15.92 ?  95  VAL   A HG13 1 
ATOM   2030 H HG21 . VAL   A 1 95  ? 26.526 -6.707  2.729   1.00 15.30 ?  95  VAL   A HG21 1 
ATOM   2031 H HG22 . VAL   A 1 95  ? 28.014 -6.259  2.397   1.00 15.30 ?  95  VAL   A HG22 1 
ATOM   2032 H HG23 . VAL   A 1 95  ? 27.055 -5.288  3.211   1.00 15.30 ?  95  VAL   A HG23 1 
ATOM   2033 N N    A VAL   A 1 96  ? 27.670 -3.867  -1.639  0.48 11.08 ?  96  VAL   A N    1 
ATOM   2034 N N    B VAL   A 1 96  ? 27.671 -3.875  -1.636  0.52 11.24 ?  96  VAL   A N    1 
ATOM   2035 C CA   A VAL   A 1 96  ? 27.268 -3.304  -2.923  0.48 11.52 ?  96  VAL   A CA   1 
ATOM   2036 C CA   B VAL   A 1 96  ? 27.281 -3.326  -2.930  0.52 11.68 ?  96  VAL   A CA   1 
ATOM   2037 C C    A VAL   A 1 96  ? 26.464 -4.350  -3.689  0.48 11.72 ?  96  VAL   A C    1 
ATOM   2038 C C    B VAL   A 1 96  ? 26.460 -4.378  -3.666  0.52 11.96 ?  96  VAL   A C    1 
ATOM   2039 O O    A VAL   A 1 96  ? 27.024 -5.282  -4.274  0.48 12.60 ?  96  VAL   A O    1 
ATOM   2040 O O    B VAL   A 1 96  ? 27.003 -5.352  -4.196  0.52 13.01 ?  96  VAL   A O    1 
ATOM   2041 C CB   A VAL   A 1 96  ? 28.464 -2.810  -3.737  0.48 12.10 ?  96  VAL   A CB   1 
ATOM   2042 C CB   B VAL   A 1 96  ? 28.491 -2.890  -3.756  0.52 12.41 ?  96  VAL   A CB   1 
ATOM   2043 C CG1  A VAL   A 1 96  ? 27.964 -2.230  -5.045  0.48 12.28 ?  96  VAL   A CG1  1 
ATOM   2044 C CG1  B VAL   A 1 96  ? 28.011 -2.196  -5.017  0.52 12.67 ?  96  VAL   A CG1  1 
ATOM   2045 C CG2  A VAL   A 1 96  ? 29.258 -1.774  -2.955  0.48 12.40 ?  96  VAL   A CG2  1 
ATOM   2046 C CG2  B VAL   A 1 96  ? 29.407 -1.989  -2.942  0.52 12.60 ?  96  VAL   A CG2  1 
ATOM   2047 H H    A VAL   A 1 96  ? 28.346 -4.402  -1.692  0.48 13.30 ?  96  VAL   A H    1 
ATOM   2048 H H    B VAL   A 1 96  ? 28.341 -4.419  -1.685  0.52 13.50 ?  96  VAL   A H    1 
ATOM   2049 H HA   A VAL   A 1 96  ? 26.691 -2.546  -2.763  0.48 13.83 ?  96  VAL   A HA   1 
ATOM   2050 H HA   B VAL   A 1 96  ? 26.723 -2.550  -2.790  0.52 14.03 ?  96  VAL   A HA   1 
ATOM   2051 H HB   A VAL   A 1 96  ? 29.050 -3.556  -3.939  0.48 14.53 ?  96  VAL   A HB   1 
ATOM   2052 H HB   B VAL   A 1 96  ? 29.001 -3.672  -4.021  0.52 14.90 ?  96  VAL   A HB   1 
ATOM   2053 H HG11 A VAL   A 1 96  ? 28.683 -1.727  -5.458  0.48 14.74 ?  96  VAL   A HG11 1 
ATOM   2054 H HG11 B VAL   A 1 96  ? 28.769 -1.780  -5.456  0.52 15.21 ?  96  VAL   A HG11 1 
ATOM   2055 H HG12 A VAL   A 1 96  ? 27.689 -2.952  -5.629  0.48 14.74 ?  96  VAL   A HG12 1 
ATOM   2056 H HG12 B VAL   A 1 96  ? 27.607 -2.852  -5.606  0.52 15.21 ?  96  VAL   A HG12 1 
ATOM   2057 H HG13 A VAL   A 1 96  ? 27.214 -1.643  -4.863  0.48 14.74 ?  96  VAL   A HG13 1 
ATOM   2058 H HG13 B VAL   A 1 96  ? 27.359 -1.520  -4.774  0.52 15.21 ?  96  VAL   A HG13 1 
ATOM   2059 H HG21 A VAL   A 1 96  ? 29.981 -1.443  -3.510  0.48 14.89 ?  96  VAL   A HG21 1 
ATOM   2060 H HG21 B VAL   A 1 96  ? 30.110 -1.648  -3.517  0.52 15.13 ?  96  VAL   A HG21 1 
ATOM   2061 H HG22 A VAL   A 1 96  ? 28.668 -1.043  -2.710  0.48 14.89 ?  96  VAL   A HG22 1 
ATOM   2062 H HG22 B VAL   A 1 96  ? 28.886 -1.253  -2.584  0.52 15.13 ?  96  VAL   A HG22 1 
ATOM   2063 H HG23 A VAL   A 1 96  ? 29.618 -2.189  -2.155  0.48 14.89 ?  96  VAL   A HG23 1 
ATOM   2064 H HG23 B VAL   A 1 96  ? 29.794 -2.504  -2.217  0.52 15.13 ?  96  VAL   A HG23 1 
ATOM   2065 N N    . GLY   A 1 97  ? 25.145 -4.188  -3.710  1.00 12.00 ?  97  GLY   A N    1 
ATOM   2066 C CA   . GLY   A 1 97  ? 24.315 -4.954  -4.601  1.00 12.38 ?  97  GLY   A CA   1 
ATOM   2067 C C    . GLY   A 1 97  ? 24.311 -4.299  -5.970  1.00 12.52 ?  97  GLY   A C    1 
ATOM   2068 O O    . GLY   A 1 97  ? 24.600 -3.103  -6.102  1.00 13.34 ?  97  GLY   A O    1 
ATOM   2069 H H    A GLY   A 1 97  ? 24.716 -3.627  -3.216  0.48 14.41 ?  97  GLY   A H    1 
ATOM   2070 H H    B GLY   A 1 97  ? 24.720 -3.616  -3.225  0.52 14.41 ?  97  GLY   A H    1 
ATOM   2071 H HA2  . GLY   A 1 97  ? 24.656 -5.857  -4.672  1.00 14.87 ?  97  GLY   A HA2  1 
ATOM   2072 H HA3  . GLY   A 1 97  ? 23.405 -4.989  -4.253  1.00 14.87 ?  97  GLY   A HA3  1 
ATOM   2073 N N    . PRO   A 1 98  ? 23.994 -5.057  -7.015  1.00 12.35 ?  98  PRO   A N    1 
ATOM   2074 C CA   . PRO   A 1 98  ? 23.878 -4.452  -8.347  1.00 13.80 ?  98  PRO   A CA   1 
ATOM   2075 C C    . PRO   A 1 98  ? 22.751 -3.424  -8.406  1.00 14.03 ?  98  PRO   A C    1 
ATOM   2076 O O    . PRO   A 1 98  ? 21.667 -3.619  -7.849  1.00 13.78 ?  98  PRO   A O    1 
ATOM   2077 C CB   . PRO   A 1 98  ? 23.589 -5.656  -9.254  1.00 14.36 ?  98  PRO   A CB   1 
ATOM   2078 C CG   . PRO   A 1 98  ? 22.935 -6.665  -8.338  1.00 14.43 ?  98  PRO   A CG   1 
ATOM   2079 C CD   . PRO   A 1 98  ? 23.688 -6.500  -7.030  1.00 13.14 ?  98  PRO   A CD   1 
ATOM   2080 H HA   . PRO   A 1 98  ? 24.716 -4.046  -8.602  1.00 16.56 ?  98  PRO   A HA   1 
ATOM   2081 H HB2  . PRO   A 1 98  ? 22.983 -5.396  -9.963  1.00 17.24 ?  98  PRO   A HB2  1 
ATOM   2082 H HB3  . PRO   A 1 98  ? 24.415 -6.011  -9.610  1.00 17.24 ?  98  PRO   A HB3  1 
ATOM   2083 H HG2  . PRO   A 1 98  ? 21.990 -6.446  -8.222  1.00 17.33 ?  98  PRO   A HG2  1 
ATOM   2084 H HG3  . PRO   A 1 98  ? 23.037 -7.560  -8.693  1.00 17.33 ?  98  PRO   A HG3  1 
ATOM   2085 H HD2  . PRO   A 1 98  ? 23.121 -6.751  -6.277  1.00 15.77 ?  98  PRO   A HD2  1 
ATOM   2086 H HD3  . PRO   A 1 98  ? 24.505 -7.024  -7.043  1.00 15.77 ?  98  PRO   A HD3  1 
ATOM   2087 N N    A ASN   A 1 99  ? 23.024 -2.320  -9.087  0.48 14.83 ?  99  ASN   A N    1 
ATOM   2088 N N    B ASN   A 1 99  ? 23.022 -2.308  -9.085  0.52 14.18 ?  99  ASN   A N    1 
ATOM   2089 C CA   A ASN   A 1 99  ? 22.038 -1.275  -9.317  0.48 16.13 ?  99  ASN   A CA   1 
ATOM   2090 C CA   B ASN   A 1 99  ? 22.036 -1.246  -9.294  0.52 14.72 ?  99  ASN   A CA   1 
ATOM   2091 C C    A ASN   A 1 99  ? 21.463 -1.492  -10.711 0.48 17.62 ?  99  ASN   A C    1 
ATOM   2092 C C    B ASN   A 1 99  ? 21.505 -1.368  -10.717 0.52 15.48 ?  99  ASN   A C    1 
ATOM   2093 O O    A ASN   A 1 99  ? 22.198 -1.445  -11.705 0.48 18.23 ?  99  ASN   A O    1 
ATOM   2094 O O    B ASN   A 1 99  ? 22.130 -0.898  -11.674 0.52 15.36 ?  99  ASN   A O    1 
ATOM   2095 C CB   A ASN   A 1 99  ? 22.689 0.103   -9.181  0.48 16.57 ?  99  ASN   A CB   1 
ATOM   2096 C CB   B ASN   A 1 99  ? 22.644 0.130   -9.036  0.52 14.90 ?  99  ASN   A CB   1 
ATOM   2097 C CG   A ASN   A 1 99  ? 21.673 1.238   -9.166  0.48 17.17 ?  99  ASN   A CG   1 
ATOM   2098 C CG   B ASN   A 1 99  ? 21.599 1.250   -9.051  0.52 15.29 ?  99  ASN   A CG   1 
ATOM   2099 O OD1  A ASN   A 1 99  ? 20.676 1.203   -9.888  0.48 17.94 ?  99  ASN   A OD1  1 
ATOM   2100 O OD1  B ASN   A 1 99  ? 20.636 1.208   -9.819  0.52 16.55 ?  99  ASN   A OD1  1 
ATOM   2101 N ND2  A ASN   A 1 99  ? 21.931 2.256   -8.345  0.48 17.48 ?  99  ASN   A ND2  1 
ATOM   2102 N ND2  B ASN   A 1 99  ? 21.790 2.251   -8.200  0.52 15.80 ?  99  ASN   A ND2  1 
ATOM   2103 H H    A ASN   A 1 99  ? 23.794 -2.148  -9.428  0.48 17.81 ?  99  ASN   A H    1 
ATOM   2104 H H    B ASN   A 1 99  ? 23.796 -2.134  -9.417  0.52 17.02 ?  99  ASN   A H    1 
ATOM   2105 H HA   A ASN   A 1 99  ? 21.324 -1.345  -8.660  0.48 19.36 ?  99  ASN   A HA   1 
ATOM   2106 H HA   B ASN   A 1 99  ? 21.297 -1.375  -8.670  0.52 17.67 ?  99  ASN   A HA   1 
ATOM   2107 H HB2  A ASN   A 1 99  ? 23.191 0.138   -8.347  0.48 19.89 ?  99  ASN   A HB2  1 
ATOM   2108 H HB2  B ASN   A 1 99  ? 23.079 0.133   -8.170  0.52 17.89 ?  99  ASN   A HB2  1 
ATOM   2109 H HB3  A ASN   A 1 99  ? 23.283 0.249   -9.929  0.48 19.89 ?  99  ASN   A HB3  1 
ATOM   2110 H HB3  B ASN   A 1 99  ? 23.294 0.316   -9.734  0.52 17.89 ?  99  ASN   A HB3  1 
ATOM   2111 H HD21 A ASN   A 1 99  ? 21.389 2.920   -8.293  0.48 20.98 ?  99  ASN   A HD21 1 
ATOM   2112 H HD21 B ASN   A 1 99  ? 21.232 2.902   -8.172  0.52 18.97 ?  99  ASN   A HD21 1 
ATOM   2113 H HD22 A ASN   A 1 99  ? 22.643 2.246   -7.857  0.48 20.98 ?  99  ASN   A HD22 1 
ATOM   2114 H HD22 B ASN   A 1 99  ? 22.475 2.246   -7.680  0.52 18.97 ?  99  ASN   A HD22 1 
ATOM   2115 N N    A VAL   A 1 100 ? 20.161 -1.785  -10.771 0.48 18.11 ?  100 VAL   A N    1 
ATOM   2116 N N    B VAL   A 1 100 ? 20.330 -1.993  -10.839 0.52 16.64 ?  100 VAL   A N    1 
ATOM   2117 C CA   A VAL   A 1 100 ? 19.509 -2.016  -12.058 0.48 19.11 ?  100 VAL   A CA   1 
ATOM   2118 C CA   B VAL   A 1 100 ? 19.722 -2.230  -12.145 0.52 19.37 ?  100 VAL   A CA   1 
ATOM   2119 C C    A VAL   A 1 100 ? 19.379 -0.717  -12.844 0.48 19.80 ?  100 VAL   A C    1 
ATOM   2120 C C    B VAL   A 1 100 ? 19.562 -0.926  -12.916 0.52 20.22 ?  100 VAL   A C    1 
ATOM   2121 O O    A VAL   A 1 100 ? 19.391 -0.727  -14.079 0.48 20.52 ?  100 VAL   A O    1 
ATOM   2122 O O    B VAL   A 1 100 ? 19.676 -0.906  -14.147 0.52 22.18 ?  100 VAL   A O    1 
ATOM   2123 C CB   A VAL   A 1 100 ? 18.154 -2.725  -11.863 0.48 20.00 ?  100 VAL   A CB   1 
ATOM   2124 C CB   B VAL   A 1 100 ? 18.386 -2.987  -11.973 0.52 21.53 ?  100 VAL   A CB   1 
ATOM   2125 C CG1  A VAL   A 1 100 ? 17.402 -2.831  -13.185 0.48 20.45 ?  100 VAL   A CG1  1 
ATOM   2126 C CG1  B VAL   A 1 100 ? 17.803 -3.384  -13.326 0.52 22.68 ?  100 VAL   A CG1  1 
ATOM   2127 C CG2  A VAL   A 1 100 ? 18.368 -4.106  -11.262 0.48 20.34 ?  100 VAL   A CG2  1 
ATOM   2128 C CG2  B VAL   A 1 100 ? 18.585 -4.220  -11.098 0.52 22.26 ?  100 VAL   A CG2  1 
ATOM   2129 H H    A VAL   A 1 100 ? 19.641 -1.859  -10.086 0.48 21.74 ?  100 VAL   A H    1 
ATOM   2130 H H    B VAL   A 1 100 ? 19.857 -2.276  -10.172 0.52 19.98 ?  100 VAL   A H    1 
ATOM   2131 H HA   A VAL   A 1 100 ? 20.071 -2.610  -12.573 0.48 22.94 ?  100 VAL   A HA   1 
ATOM   2132 H HA   B VAL   A 1 100 ? 20.308 -2.801  -12.660 0.52 23.25 ?  100 VAL   A HA   1 
ATOM   2133 H HB   A VAL   A 1 100 ? 17.609 -2.210  -11.249 0.48 24.01 ?  100 VAL   A HB   1 
ATOM   2134 H HB   B VAL   A 1 100 ? 17.744 -2.411  -11.530 0.52 25.84 ?  100 VAL   A HB   1 
ATOM   2135 H HG11 A VAL   A 1 100 ? 16.667 -3.456  -13.079 0.48 24.55 ?  100 VAL   A HG11 1 
ATOM   2136 H HG11 B VAL   A 1 100 ? 17.013 -3.930  -13.184 0.52 27.22 ?  100 VAL   A HG11 1 
ATOM   2137 H HG12 A VAL   A 1 100 ? 17.060 -1.959  -13.430 0.48 24.55 ?  100 VAL   A HG12 1 
ATOM   2138 H HG12 B VAL   A 1 100 ? 17.566 -2.582  -13.815 0.52 27.22 ?  100 VAL   A HG12 1 
ATOM   2139 H HG13 A VAL   A 1 100 ? 18.010 -3.155  -13.869 0.48 24.55 ?  100 VAL   A HG13 1 
ATOM   2140 H HG13 B VAL   A 1 100 ? 18.468 -3.890  -13.819 0.52 27.22 ?  100 VAL   A HG13 1 
ATOM   2141 H HG21 A VAL   A 1 100 ? 17.510 -4.548  -11.169 0.48 24.42 ?  100 VAL   A HG21 1 
ATOM   2142 H HG21 B VAL   A 1 100 ? 17.823 -4.811  -11.203 0.52 26.72 ?  100 VAL   A HG21 1 
ATOM   2143 H HG22 A VAL   A 1 100 ? 18.943 -4.621  -11.851 0.48 24.42 ?  100 VAL   A HG22 1 
ATOM   2144 H HG22 B VAL   A 1 100 ? 19.396 -4.674  -11.374 0.52 26.72 ?  100 VAL   A HG22 1 
ATOM   2145 H HG23 A VAL   A 1 100 ? 18.787 -4.011  -10.392 0.48 24.42 ?  100 VAL   A HG23 1 
ATOM   2146 H HG23 B VAL   A 1 100 ? 18.661 -3.942  -10.171 0.52 26.72 ?  100 VAL   A HG23 1 
ATOM   2147 N N    A ASN   A 1 101 ? 19.245 0.414   -12.158 0.48 21.10 ?  101 ASN   A N    1 
ATOM   2148 N N    B ASN   A 1 101 ? 19.304 0.181   -12.214 0.52 20.32 ?  101 ASN   A N    1 
ATOM   2149 C CA   A ASN   A 1 101 ? 19.222 1.693   -12.854 0.48 22.84 ?  101 ASN   A CA   1 
ATOM   2150 C CA   B ASN   A 1 101 ? 19.140 1.466   -12.885 0.52 20.72 ?  101 ASN   A CA   1 
ATOM   2151 C C    A ASN   A 1 101 ? 20.597 2.098   -13.388 0.48 24.94 ?  101 ASN   A C    1 
ATOM   2152 C C    B ASN   A 1 101 ? 20.447 1.980   -13.474 0.52 21.59 ?  101 ASN   A C    1 
ATOM   2153 O O    A ASN   A 1 101 ? 20.720 3.184   -13.968 0.48 26.23 ?  101 ASN   A O    1 
ATOM   2154 O O    B ASN   A 1 101 ? 20.414 2.819   -14.383 0.52 22.70 ?  101 ASN   A O    1 
ATOM   2155 C CB   A ASN   A 1 101 ? 18.628 2.758   -11.933 0.48 22.94 ?  101 ASN   A CB   1 
ATOM   2156 C CB   B ASN   A 1 101 ? 18.521 2.479   -11.922 0.52 20.12 ?  101 ASN   A CB   1 
ATOM   2157 C CG   A ASN   A 1 101 ? 17.236 2.385   -11.449 0.48 22.83 ?  101 ASN   A CG   1 
ATOM   2158 C CG   B ASN   A 1 101 ? 17.127 2.065   -11.462 0.52 19.22 ?  101 ASN   A CG   1 
ATOM   2159 O OD1  A ASN   A 1 101 ? 16.398 1.931   -12.232 0.48 22.62 ?  101 ASN   A OD1  1 
ATOM   2160 O OD1  B ASN   A 1 101 ? 16.351 1.487   -12.229 0.52 19.49 ?  101 ASN   A OD1  1 
ATOM   2161 N ND2  A ASN   A 1 101 ? 16.987 2.554   -10.154 0.48 23.44 ?  101 ASN   A ND2  1 
ATOM   2162 N ND2  B ASN   A 1 101 ? 16.807 2.350   -10.209 0.52 19.05 ?  101 ASN   A ND2  1 
ATOM   2163 H H    A ASN   A 1 101 ? 19.150 0.464   -11.305 0.48 25.32 ?  101 ASN   A H    1 
ATOM   2164 H H    B ASN   A 1 101 ? 19.216 0.209   -11.360 0.52 24.39 ?  101 ASN   A H    1 
ATOM   2165 H HA   A ASN   A 1 101 ? 18.622 1.605   -13.611 0.48 27.41 ?  101 ASN   A HA   1 
ATOM   2166 H HA   B ASN   A 1 101 ? 18.528 1.351   -13.622 0.52 24.87 ?  101 ASN   A HA   1 
ATOM   2167 H HB2  A ASN   A 1 101 ? 19.202 2.863   -11.160 0.48 27.53 ?  101 ASN   A HB2  1 
ATOM   2168 H HB2  B ASN   A 1 101 ? 19.088 2.562   -11.139 0.52 24.15 ?  101 ASN   A HB2  1 
ATOM   2169 H HB3  A ASN   A 1 101 ? 18.560 3.592   -12.420 0.48 27.53 ?  101 ASN   A HB3  1 
ATOM   2170 H HB3  B ASN   A 1 101 ? 18.452 3.337   -12.372 0.52 24.15 ?  101 ASN   A HB3  1 
ATOM   2171 H HD21 A ASN   A 1 101 ? 16.216 2.349   -9.833  0.48 28.14 ?  101 ASN   A HD21 1 
ATOM   2172 H HD21 B ASN   A 1 101 ? 16.032 2.134   -9.911  0.52 22.87 ?  101 ASN   A HD21 1 
ATOM   2173 H HD22 A ASN   A 1 101 ? 17.596 2.876   -9.639  0.48 28.14 ?  101 ASN   A HD22 1 
ATOM   2174 H HD22 B ASN   A 1 101 ? 17.372 2.751   -9.701  0.52 22.87 ?  101 ASN   A HD22 1 
ATOM   2175 N N    A LYS   A 1 102 ? 21.622 1.259   -13.201 0.48 25.92 ?  102 LYS   A N    1 
ATOM   2176 N N    B LYS   A 1 102 ? 21.589 1.487   -12.987 0.52 22.02 ?  102 LYS   A N    1 
ATOM   2177 C CA   A LYS   A 1 102 ? 22.919 1.403   -13.853 0.48 26.38 ?  102 LYS   A CA   1 
ATOM   2178 C CA   B LYS   A 1 102 ? 22.891 1.773   -13.578 0.52 22.34 ?  102 LYS   A CA   1 
ATOM   2179 C C    A LYS   A 1 102 ? 23.218 0.278   -14.838 0.48 26.18 ?  102 LYS   A C    1 
ATOM   2180 C C    B LYS   A 1 102 ? 23.308 0.741   -14.620 0.52 23.26 ?  102 LYS   A C    1 
ATOM   2181 O O    A LYS   A 1 102 ? 24.334 0.216   -15.358 0.48 26.51 ?  102 LYS   A O    1 
ATOM   2182 O O    B LYS   A 1 102 ? 24.355 0.916   -15.251 0.52 23.93 ?  102 LYS   A O    1 
ATOM   2183 C CB   A LYS   A 1 102 ? 24.048 1.426   -12.812 0.48 27.18 ?  102 LYS   A CB   1 
ATOM   2184 C CB   B LYS   A 1 102 ? 23.968 1.865   -12.487 0.52 22.50 ?  102 LYS   A CB   1 
ATOM   2185 C CG   A LYS   A 1 102 ? 23.992 2.569   -11.823 0.48 27.80 ?  102 LYS   A CG   1 
ATOM   2186 C CG   B LYS   A 1 102 ? 23.804 3.030   -11.521 0.52 23.13 ?  102 LYS   A CG   1 
ATOM   2187 C CD   A LYS   A 1 102 ? 25.177 2.510   -10.867 0.48 28.55 ?  102 LYS   A CD   1 
ATOM   2188 C CD   B LYS   A 1 102 ? 24.890 3.009   -10.451 0.52 23.56 ?  102 LYS   A CD   1 
ATOM   2189 C CE   A LYS   A 1 102 ? 25.134 3.632   -9.843  0.48 29.10 ?  102 LYS   A CE   1 
ATOM   2190 C CE   B LYS   A 1 102 ? 24.713 4.141   -9.447  0.52 24.48 ?  102 LYS   A CE   1 
ATOM   2191 N NZ   A LYS   A 1 102 ? 26.238 3.505   -8.845  0.48 29.13 ?  102 LYS   A NZ   1 
ATOM   2192 N NZ   B LYS   A 1 102 ? 25.688 4.056   -8.319  0.52 24.32 ?  102 LYS   A NZ   1 
ATOM   2193 H H    A LYS   A 1 102 ? 21.591 0.585   -12.673 0.48 31.11 ?  102 LYS   A H    1 
ATOM   2194 H H    B LYS   A 1 102 ? 21.637 0.962   -12.300 0.52 26.43 ?  102 LYS   A H    1 
ATOM   2195 H HA   A LYS   A 1 102 ? 22.943 2.245   -14.334 0.48 31.67 ?  102 LYS   A HA   1 
ATOM   2196 H HA   B LYS   A 1 102 ? 22.850 2.624   -14.023 0.52 26.82 ?  102 LYS   A HA   1 
ATOM   2197 H HB2  A LYS   A 1 102 ? 24.017 0.598   -12.307 0.48 32.63 ?  102 LYS   A HB2  1 
ATOM   2198 H HB2  B LYS   A 1 102 ? 23.956 1.050   -11.962 0.52 27.00 ?  102 LYS   A HB2  1 
ATOM   2199 H HB3  A LYS   A 1 102 ? 24.899 1.485   -13.280 0.48 32.63 ?  102 LYS   A HB3  1 
ATOM   2200 H HB3  B LYS   A 1 102 ? 24.835 1.964   -12.913 0.52 27.00 ?  102 LYS   A HB3  1 
ATOM   2201 H HG2  A LYS   A 1 102 ? 24.025 3.411   -12.302 0.48 33.37 ?  102 LYS   A HG2  1 
ATOM   2202 H HG2  B LYS   A 1 102 ? 23.870 3.865   -12.011 0.52 27.77 ?  102 LYS   A HG2  1 
ATOM   2203 H HG3  A LYS   A 1 102 ? 23.175 2.505   -11.305 0.48 33.37 ?  102 LYS   A HG3  1 
ATOM   2204 H HG3  B LYS   A 1 102 ? 22.941 2.964   -11.083 0.52 27.77 ?  102 LYS   A HG3  1 
ATOM   2205 H HD2  A LYS   A 1 102 ? 25.162 1.664   -10.391 0.48 34.27 ?  102 LYS   A HD2  1 
ATOM   2206 H HD2  B LYS   A 1 102 ? 24.851 2.167   -9.972  0.52 28.28 ?  102 LYS   A HD2  1 
ATOM   2207 H HD3  A LYS   A 1 102 ? 26.001 2.593   -11.373 0.48 34.27 ?  102 LYS   A HD3  1 
ATOM   2208 H HD3  B LYS   A 1 102 ? 25.758 3.113   -10.875 0.52 28.28 ?  102 LYS   A HD3  1 
ATOM   2209 H HE2  A LYS   A 1 102 ? 25.231 4.485   -10.297 0.48 34.92 ?  102 LYS   A HE2  1 
ATOM   2210 H HE2  B LYS   A 1 102 ? 24.846 4.988   -9.899  0.52 29.38 ?  102 LYS   A HE2  1 
ATOM   2211 H HE3  A LYS   A 1 102 ? 24.288 3.600   -9.368  0.48 34.92 ?  102 LYS   A HE3  1 
ATOM   2212 H HE3  B LYS   A 1 102 ? 23.818 4.096   -9.077  0.52 29.38 ?  102 LYS   A HE3  1 
ATOM   2213 H HZ1  A LYS   A 1 102 ? 26.195 4.170   -8.256  0.48 34.96 ?  102 LYS   A HZ1  1 
ATOM   2214 H HZ1  B LYS   A 1 102 ? 25.554 4.730   -7.753  0.52 29.19 ?  102 LYS   A HZ1  1 
ATOM   2215 H HZ2  A LYS   A 1 102 ? 26.168 2.729   -8.412  0.48 34.96 ?  102 LYS   A HZ2  1 
ATOM   2216 H HZ2  B LYS   A 1 102 ? 25.582 3.287   -7.883  0.52 29.19 ?  102 LYS   A HZ2  1 
ATOM   2217 H HZ3  A LYS   A 1 102 ? 27.026 3.534   -9.258  0.48 34.96 ?  102 LYS   A HZ3  1 
ATOM   2218 H HZ3  B LYS   A 1 102 ? 26.519 4.100   -8.632  0.52 29.19 ?  102 LYS   A HZ3  1 
ATOM   2219 N N    A GLY   A 1 103 ? 22.276 -0.631  -15.080 0.48 26.77 ?  103 GLY   A N    1 
ATOM   2220 N N    B GLY   A 1 103 ? 22.526 -0.322  -14.813 0.52 24.50 ?  103 GLY   A N    1 
ATOM   2221 C CA   A GLY   A 1 103 ? 22.514 -1.741  -15.982 0.48 26.59 ?  103 GLY   A CA   1 
ATOM   2222 C CA   B GLY   A 1 103 ? 22.839 -1.331  -15.806 0.52 24.40 ?  103 GLY   A CA   1 
ATOM   2223 C C    A GLY   A 1 103 ? 23.349 -2.869  -15.418 0.48 26.54 ?  103 GLY   A C    1 
ATOM   2224 C C    B GLY   A 1 103 ? 23.742 -2.450  -15.337 0.52 25.63 ?  103 GLY   A C    1 
ATOM   2225 O O    A GLY   A 1 103 ? 23.803 -3.726  -16.184 0.48 26.57 ?  103 GLY   A O    1 
ATOM   2226 O O    B GLY   A 1 103 ? 24.475 -3.017  -16.154 0.52 26.05 ?  103 GLY   A O    1 
ATOM   2227 H H    A GLY   A 1 103 ? 21.498 -0.629  -14.725 0.48 32.13 ?  103 GLY   A H    1 
ATOM   2228 H H    B GLY   A 1 103 ? 21.809 -0.485  -14.375 0.52 29.41 ?  103 GLY   A H    1 
ATOM   2229 H HA2  A GLY   A 1 103 ? 21.664 -2.118  -16.252 0.48 31.92 ?  103 GLY   A HA2  1 
ATOM   2230 H HA2  B GLY   A 1 103 ? 22.008 -1.719  -16.134 0.52 29.29 ?  103 GLY   A HA2  1 
ATOM   2231 H HA3  A GLY   A 1 103 ? 22.959 -1.406  -16.779 0.48 31.92 ?  103 GLY   A HA3  1 
ATOM   2232 H HA3  B GLY   A 1 103 ? 23.284 -0.913  -16.558 0.52 29.29 ?  103 GLY   A HA3  1 
ATOM   2233 N N    A GLU   A 1 104 ? 23.553 -2.910  -14.106 0.48 25.61 ?  104 GLU   A N    1 
ATOM   2234 N N    B GLU   A 1 104 ? 23.709 -2.799  -14.055 0.52 24.95 ?  104 GLU   A N    1 
ATOM   2235 C CA   A GLU   A 1 104 ? 24.441 -3.895  -13.507 0.48 24.69 ?  104 GLU   A CA   1 
ATOM   2236 C CA   B GLU   A 1 104 ? 24.614 -3.783  -13.477 0.52 24.52 ?  104 GLU   A CA   1 
ATOM   2237 C C    A GLU   A 1 104 ? 23.752 -5.252  -13.379 0.48 24.84 ?  104 GLU   A C    1 
ATOM   2238 C C    B GLU   A 1 104 ? 23.966 -5.170  -13.405 0.52 25.08 ?  104 GLU   A C    1 
ATOM   2239 O O    A GLU   A 1 104 ? 22.540 -5.346  -13.157 0.48 25.35 ?  104 GLU   A O    1 
ATOM   2240 O O    B GLU   A 1 104 ? 22.740 -5.313  -13.381 0.52 25.88 ?  104 GLU   A O    1 
ATOM   2241 C CB   A GLU   A 1 104 ? 24.944 -3.388  -12.153 0.48 23.15 ?  104 GLU   A CB   1 
ATOM   2242 C CB   B GLU   A 1 104 ? 25.086 -3.298  -12.099 0.52 22.69 ?  104 GLU   A CB   1 
ATOM   2243 C CG   A GLU   A 1 104 ? 25.911 -2.215  -12.313 0.48 22.72 ?  104 GLU   A CG   1 
ATOM   2244 C CG   B GLU   A 1 104 ? 25.895 -1.989  -12.207 0.52 21.93 ?  104 GLU   A CG   1 
ATOM   2245 C CD   A GLU   A 1 104 ? 26.288 -1.520  -11.019 0.48 21.79 ?  104 GLU   A CD   1 
ATOM   2246 C CD   B GLU   A 1 104 ? 26.086 -1.234  -10.895 0.52 20.95 ?  104 GLU   A CD   1 
ATOM   2247 O OE1  A GLU   A 1 104 ? 25.685 -1.807  -9.965  0.48 20.94 ?  104 GLU   A OE1  1 
ATOM   2248 O OE1  B GLU   A 1 104 ? 25.550 -1.652  -9.848  0.52 19.23 ?  104 GLU   A OE1  1 
ATOM   2249 O OE2  A GLU   A 1 104 ? 27.201 -0.663  -11.070 0.48 22.02 -1 104 GLU   A OE2  1 
ATOM   2250 O OE2  B GLU   A 1 104 ? 26.790 -0.196  -10.927 0.52 21.82 -1 104 GLU   A OE2  1 
ATOM   2251 H H    A GLU   A 1 104 ? 23.180 -2.380  -13.543 0.48 30.74 ?  104 GLU   A H    1 
ATOM   2252 H H    B GLU   A 1 104 ? 23.163 -2.464  -13.482 0.52 29.94 ?  104 GLU   A H    1 
ATOM   2253 H HA   A GLU   A 1 104 ? 25.215 -4.006  -14.084 0.48 29.63 ?  104 GLU   A HA   1 
ATOM   2254 H HA   B GLU   A 1 104 ? 25.396 -3.853  -14.046 0.52 29.43 ?  104 GLU   A HA   1 
ATOM   2255 H HB2  A GLU   A 1 104 ? 24.188 -3.089  -11.626 0.48 27.79 ?  104 GLU   A HB2  1 
ATOM   2256 H HB2  B GLU   A 1 104 ? 24.315 -3.135  -11.537 0.52 27.24 ?  104 GLU   A HB2  1 
ATOM   2257 H HB3  A GLU   A 1 104 ? 25.409 -4.107  -11.699 0.48 27.79 ?  104 GLU   A HB3  1 
ATOM   2258 H HB3  B GLU   A 1 104 ? 25.656 -3.975  -11.701 0.52 27.24 ?  104 GLU   A HB3  1 
ATOM   2259 H HG2  A GLU   A 1 104 ? 26.727 -2.540  -12.723 0.48 27.27 ?  104 GLU   A HG2  1 
ATOM   2260 H HG2  B GLU   A 1 104 ? 26.779 -2.195  -12.553 0.52 26.32 ?  104 GLU   A HG2  1 
ATOM   2261 H HG3  A GLU   A 1 104 ? 25.500 -1.547  -12.878 0.48 27.27 ?  104 GLU   A HG3  1 
ATOM   2262 H HG3  B GLU   A 1 104 ? 25.443 -1.389  -12.822 0.52 26.32 ?  104 GLU   A HG3  1 
ATOM   2263 N N    A ASP   A 1 105 ? 24.549 -6.310  -13.527 0.48 25.15 ?  105 ASP   A N    1 
ATOM   2264 N N    B ASP   A 1 105 ? 24.821 -6.198  -13.373 0.52 25.73 ?  105 ASP   A N    1 
ATOM   2265 C CA   A ASP   A 1 105 ? 24.029 -7.668  -13.638 0.48 25.94 ?  105 ASP   A CA   1 
ATOM   2266 C CA   B ASP   A 1 105 ? 24.391 -7.586  -13.542 0.52 26.70 ?  105 ASP   A CA   1 
ATOM   2267 C C    A ASP   A 1 105 ? 23.352 -8.100  -12.340 0.48 23.74 ?  105 ASP   A C    1 
ATOM   2268 C C    B ASP   A 1 105 ? 23.621 -8.065  -12.314 0.52 25.97 ?  105 ASP   A C    1 
ATOM   2269 O O    A ASP   A 1 105 ? 24.004 -8.208  -11.298 0.48 22.05 ?  105 ASP   A O    1 
ATOM   2270 O O    B ASP   A 1 105 ? 24.181 -8.153  -11.218 0.52 25.05 ?  105 ASP   A O    1 
ATOM   2271 C CB   A ASP   A 1 105 ? 25.180 -8.614  -13.970 0.48 28.53 ?  105 ASP   A CB   1 
ATOM   2272 C CB   B ASP   A 1 105 ? 25.624 -8.461  -13.769 0.52 28.23 ?  105 ASP   A CB   1 
ATOM   2273 C CG   A ASP   A 1 105 ? 24.716 -10.040 -14.189 0.48 30.92 ?  105 ASP   A CG   1 
ATOM   2274 C CG   B ASP   A 1 105 ? 25.282 -9.905  -14.071 0.52 29.55 ?  105 ASP   A CG   1 
ATOM   2275 O OD1  A ASP   A 1 105 ? 23.488 -10.257 -14.274 0.48 31.43 ?  105 ASP   A OD1  1 
ATOM   2276 O OD1  B ASP   A 1 105 ? 24.083 -10.240 -14.179 0.52 29.91 ?  105 ASP   A OD1  1 
ATOM   2277 O OD2  A ASP   A 1 105 ? 25.574 -10.945 -14.274 0.48 32.25 -1 105 ASP   A OD2  1 
ATOM   2278 O OD2  B ASP   A 1 105 ? 26.234 -10.711 -14.200 0.52 30.16 -1 105 ASP   A OD2  1 
ATOM   2279 H H    A ASP   A 1 105 ? 25.410 -6.265  -13.574 0.48 30.19 ?  105 ASP   A H    1 
ATOM   2280 H H    B ASP   A 1 105 ? 25.671 -6.120  -13.252 0.52 30.88 ?  105 ASP   A H    1 
ATOM   2281 H HA   A ASP   A 1 105 ? 23.377 -7.712  -14.354 0.48 31.14 ?  105 ASP   A HA   1 
ATOM   2282 H HA   B ASP   A 1 105 ? 23.814 -7.663  -14.319 0.52 32.05 ?  105 ASP   A HA   1 
ATOM   2283 H HB2  A ASP   A 1 105 ? 25.618 -8.307  -14.783 0.48 34.25 ?  105 ASP   A HB2  1 
ATOM   2284 H HB2  B ASP   A 1 105 ? 26.131 -8.115  -14.520 0.52 33.89 ?  105 ASP   A HB2  1 
ATOM   2285 H HB3  A ASP   A 1 105 ? 25.818 -8.606  -13.235 0.48 34.25 ?  105 ASP   A HB3  1 
ATOM   2286 H HB3  B ASP   A 1 105 ? 26.170 -8.462  -12.970 0.52 33.89 ?  105 ASP   A HB3  1 
ATOM   2287 N N    A ILE   A 1 106 ? 22.050 -8.391  -12.415 0.48 23.32 ?  106 ILE   A N    1 
ATOM   2288 N N    B ILE   A 1 106 ? 22.343 -8.410  -12.505 0.52 26.40 ?  106 ILE   A N    1 
ATOM   2289 C CA   A ILE   A 1 106 ? 21.301 -8.837  -11.244 0.48 22.46 ?  106 ILE   A CA   1 
ATOM   2290 C CA   B ILE   A 1 106 ? 21.511 -8.842  -11.385 0.52 26.54 ?  106 ILE   A CA   1 
ATOM   2291 C C    A ILE   A 1 106 ? 21.858 -10.134 -10.679 0.48 21.75 ?  106 ILE   A C    1 
ATOM   2292 C C    B ILE   A 1 106 ? 21.978 -10.167 -10.801 0.52 26.04 ?  106 ILE   A C    1 
ATOM   2293 O O    A ILE   A 1 106 ? 21.657 -10.424 -9.496  0.48 21.20 ?  106 ILE   A O    1 
ATOM   2294 O O    B ILE   A 1 106 ? 21.702 -10.451 -9.630  0.52 25.33 ?  106 ILE   A O    1 
ATOM   2295 C CB   A ILE   A 1 106 ? 19.794 -8.952  -11.572 0.48 23.34 ?  106 ILE   A CB   1 
ATOM   2296 C CB   B ILE   A 1 106 ? 20.017 -8.892  -11.768 0.52 27.70 ?  106 ILE   A CB   1 
ATOM   2297 C CG1  A ILE   A 1 106 ? 18.962 -9.063  -10.292 0.48 23.48 ?  106 ILE   A CG1  1 
ATOM   2298 C CG1  B ILE   A 1 106 ? 19.132 -8.834  -10.520 0.52 28.33 ?  106 ILE   A CG1  1 
ATOM   2299 C CG2  A ILE   A 1 106 ? 19.527 -10.164 -12.439 0.48 24.40 ?  106 ILE   A CG2  1 
ATOM   2300 C CG2  B ILE   A 1 106 ? 19.701 -10.170 -12.510 0.52 28.26 ?  106 ILE   A CG2  1 
ATOM   2301 C CD1  A ILE   A 1 106 ? 19.070 -7.862  -9.381  0.48 23.78 ?  106 ILE   A CD1  1 
ATOM   2302 C CD1  B ILE   A 1 106 ? 19.372 -7.622  -9.653  0.52 28.91 ?  106 ILE   A CD1  1 
ATOM   2303 H H    A ILE   A 1 106 ? 21.586 -8.336  -13.132 0.48 28.00 ?  106 ILE   A H    1 
ATOM   2304 H H    B ILE   A 1 106 ? 21.941 -8.399  -13.264 0.52 31.69 ?  106 ILE   A H    1 
ATOM   2305 H HA   A ILE   A 1 106 ? 21.405 -8.169  -10.555 0.48 26.96 ?  106 ILE   A HA   1 
ATOM   2306 H HA   B ILE   A 1 106 ? 21.615 -8.188  -10.685 0.52 31.86 ?  106 ILE   A HA   1 
ATOM   2307 H HB   A ILE   A 1 106 ? 19.522 -8.155  -12.054 0.48 28.01 ?  106 ILE   A HB   1 
ATOM   2308 H HB   B ILE   A 1 106 ? 19.810 -8.135  -12.339 0.52 33.25 ?  106 ILE   A HB   1 
ATOM   2309 H HG12 A ILE   A 1 106 ? 18.029 -9.162  -10.537 0.48 28.18 ?  106 ILE   A HG12 1 
ATOM   2310 H HG12 B ILE   A 1 106 ? 18.202 -8.820  -10.796 0.52 34.01 ?  106 ILE   A HG12 1 
ATOM   2311 H HG13 A ILE   A 1 106 ? 19.254 -9.841  -9.793  0.48 28.18 ?  106 ILE   A HG13 1 
ATOM   2312 H HG13 B ILE   A 1 106 ? 19.302 -9.621  -9.980  0.52 34.01 ?  106 ILE   A HG13 1 
ATOM   2313 H HG21 A ILE   A 1 106 ? 18.645 -10.077 -12.830 0.48 29.29 ?  106 ILE   A HG21 1 
ATOM   2314 H HG21 B ILE   A 1 106 ? 18.866 -10.055 -12.987 0.52 33.91 ?  106 ILE   A HG21 1 
ATOM   2315 H HG22 A ILE   A 1 106 ? 20.199 -10.203 -13.134 0.48 29.29 ?  106 ILE   A HG22 1 
ATOM   2316 H HG22 B ILE   A 1 106 ? 20.419 -10.355 -13.130 0.52 33.91 ?  106 ILE   A HG22 1 
ATOM   2317 H HG23 A ILE   A 1 106 ? 19.570 -10.960 -11.887 0.48 29.29 ?  106 ILE   A HG23 1 
ATOM   2318 H HG23 B ILE   A 1 106 ? 19.619 -10.894 -11.868 0.52 33.91 ?  106 ILE   A HG23 1 
ATOM   2319 H HD11 A ILE   A 1 106 ? 18.343 -7.886  -8.741  0.48 28.54 ?  106 ILE   A HD11 1 
ATOM   2320 H HD11 B ILE   A 1 106 ? 18.584 -7.460  -9.116  0.52 34.70 ?  106 ILE   A HD11 1 
ATOM   2321 H HD12 A ILE   A 1 106 ? 19.921 -7.894  -8.914  0.48 28.54 ?  106 ILE   A HD12 1 
ATOM   2322 H HD12 B ILE   A 1 106 ? 20.136 -7.790  -9.079  0.52 34.70 ?  106 ILE   A HD12 1 
ATOM   2323 H HD13 A ILE   A 1 106 ? 19.015 -7.054  -9.915  0.48 28.54 ?  106 ILE   A HD13 1 
ATOM   2324 H HD13 B ILE   A 1 106 ? 19.548 -6.858  -10.225 0.52 34.70 ?  106 ILE   A HD13 1 
ATOM   2325 N N    A GLN   A 1 107 ? 22.574 -10.920 -11.493 0.48 23.00 ?  107 GLN   A N    1 
ATOM   2326 N N    B GLN   A 1 107 ? 22.685 -10.989 -11.583 0.52 26.39 ?  107 GLN   A N    1 
ATOM   2327 C CA   A GLN   A 1 107 ? 23.160 -12.164 -11.002 0.48 25.54 ?  107 GLN   A CA   1 
ATOM   2328 C CA   B GLN   A 1 107 ? 23.249 -12.222 -11.047 0.52 27.87 ?  107 GLN   A CA   1 
ATOM   2329 C C    A GLN   A 1 107 ? 24.134 -11.910 -9.859  0.48 23.61 ?  107 GLN   A C    1 
ATOM   2330 C C    B GLN   A 1 107 ? 24.227 -11.948 -9.916  0.52 24.68 ?  107 GLN   A C    1 
ATOM   2331 O O    A GLN   A 1 107 ? 24.339 -12.787 -9.013  0.48 24.72 ?  107 GLN   A O    1 
ATOM   2332 O O    B GLN   A 1 107 ? 24.521 -12.856 -9.132  0.52 25.90 ?  107 GLN   A O    1 
ATOM   2333 C CB   A GLN   A 1 107 ? 23.859 -12.908 -12.144 0.48 29.95 ?  107 GLN   A CB   1 
ATOM   2334 C CB   B GLN   A 1 107 ? 23.951 -13.013 -12.155 0.52 32.49 ?  107 GLN   A CB   1 
ATOM   2335 C CG   A GLN   A 1 107 ? 22.946 -13.239 -13.318 0.48 34.55 ?  107 GLN   A CG   1 
ATOM   2336 C CG   B GLN   A 1 107 ? 23.082 -13.287 -13.375 0.52 37.32 ?  107 GLN   A CG   1 
ATOM   2337 C CD   A GLN   A 1 107 ? 21.703 -13.998 -12.894 0.48 38.37 ?  107 GLN   A CD   1 
ATOM   2338 C CD   B GLN   A 1 107 ? 21.882 -14.155 -13.057 0.52 41.16 ?  107 GLN   A CD   1 
ATOM   2339 O OE1  A GLN   A 1 107 ? 21.786 -15.030 -12.227 0.48 39.85 ?  107 GLN   A OE1  1 
ATOM   2340 O OE1  B GLN   A 1 107 ? 21.954 -15.052 -12.216 0.52 42.68 ?  107 GLN   A OE1  1 
ATOM   2341 N NE2  A GLN   A 1 107 ? 20.540 -13.484 -13.273 0.48 39.63 ?  107 GLN   A NE2  1 
ATOM   2342 N NE2  B GLN   A 1 107 ? 20.767 -13.891 -13.729 0.52 42.46 ?  107 GLN   A NE2  1 
ATOM   2343 H H    A GLN   A 1 107 ? 22.741 -10.754 -12.318 0.48 27.61 ?  107 GLN   A H    1 
ATOM   2344 H H    B GLN   A 1 107 ? 22.855 -10.855 -12.411 0.52 31.67 ?  107 GLN   A H    1 
ATOM   2345 H HA   A GLN   A 1 107 ? 22.461 -12.736 -10.660 0.48 30.66 ?  107 GLN   A HA   1 
ATOM   2346 H HA   B GLN   A 1 107 ? 22.539 -12.774 -10.691 0.52 33.45 ?  107 GLN   A HA   1 
ATOM   2347 H HB2  A GLN   A 1 107 ? 24.585 -12.361 -12.482 0.48 35.95 ?  107 GLN   A HB2  1 
ATOM   2348 H HB2  B GLN   A 1 107 ? 24.728 -12.516 -12.453 0.52 39.00 ?  107 GLN   A HB2  1 
ATOM   2349 H HB3  A GLN   A 1 107 ? 24.214 -13.747 -11.806 0.48 35.95 ?  107 GLN   A HB3  1 
ATOM   2350 H HB3  B GLN   A 1 107 ? 24.232 -13.873 -11.798 0.52 39.00 ?  107 GLN   A HB3  1 
ATOM   2351 H HG2  A GLN   A 1 107 ? 22.662 -12.414 -13.741 0.48 41.47 ?  107 GLN   A HG2  1 
ATOM   2352 H HG2  B GLN   A 1 107 ? 22.758 -12.445 -13.732 0.52 44.79 ?  107 GLN   A HG2  1 
ATOM   2353 H HG3  A GLN   A 1 107 ? 23.432 -13.788 -13.955 0.48 41.47 ?  107 GLN   A HG3  1 
ATOM   2354 H HG3  B GLN   A 1 107 ? 23.614 -13.746 -14.045 0.52 44.79 ?  107 GLN   A HG3  1 
ATOM   2355 H HE21 A GLN   A 1 107 ? 20.520 -12.760 -13.738 0.48 47.57 ?  107 GLN   A HE21 1 
ATOM   2356 H HE21 B GLN   A 1 107 ? 20.752 -13.255 -14.309 0.52 50.96 ?  107 GLN   A HE21 1 
ATOM   2357 H HE22 A GLN   A 1 107 ? 19.808 -13.876 -13.054 0.48 47.57 ?  107 GLN   A HE22 1 
ATOM   2358 H HE22 B GLN   A 1 107 ? 20.059 -14.356 -13.584 0.52 50.96 ?  107 GLN   A HE22 1 
ATOM   2359 N N    . LEU   A 1 108 ? 24.730 -10.716 -9.807  1.00 20.91 ?  108 LEU   A N    1 
ATOM   2360 C CA   . LEU   A 1 108 ? 25.643 -10.360 -8.731  1.00 17.67 ?  108 LEU   A CA   1 
ATOM   2361 C C    . LEU   A 1 108 ? 24.938 -10.204 -7.394  1.00 15.80 ?  108 LEU   A C    1 
ATOM   2362 O O    . LEU   A 1 108 ? 25.616 -10.047 -6.378  1.00 15.49 ?  108 LEU   A O    1 
ATOM   2363 C CB   . LEU   A 1 108 ? 26.396 -9.070  -9.080  1.00 17.46 ?  108 LEU   A CB   1 
ATOM   2364 C CG   . LEU   A 1 108 ? 27.376 -9.238  -10.242 1.00 19.38 ?  108 LEU   A CG   1 
ATOM   2365 C CD1  . LEU   A 1 108 ? 27.870 -7.883  -10.732 1.00 19.93 ?  108 LEU   A CD1  1 
ATOM   2366 C CD2  . LEU   A 1 108 ? 28.551 -10.126 -9.849  1.00 21.25 ?  108 LEU   A CD2  1 
ATOM   2367 H H    A LEU   A 1 108 ? 24.625 -10.099 -10.388 0.48 25.10 ?  108 LEU   A H    1 
ATOM   2368 H H    B LEU   A 1 108 ? 24.567 -10.077 -10.348 0.52 25.10 ?  108 LEU   A H    1 
ATOM   2369 H HA   . LEU   A 1 108 ? 26.300 -11.065 -8.627  1.00 21.21 ?  108 LEU   A HA   1 
ATOM   2370 H HB2  . LEU   A 1 108 ? 25.751 -8.388  -9.328  1.00 20.96 ?  108 LEU   A HB2  1 
ATOM   2371 H HB3  . LEU   A 1 108 ? 26.899 -8.778  -8.303  1.00 20.96 ?  108 LEU   A HB3  1 
ATOM   2372 H HG   . LEU   A 1 108 ? 26.917 -9.668  -10.979 1.00 23.27 ?  108 LEU   A HG   1 
ATOM   2373 H HD11 . LEU   A 1 108 ? 28.472 -8.020  -11.485 1.00 23.92 ?  108 LEU   A HD11 1 
ATOM   2374 H HD12 . LEU   A 1 108 ? 27.111 -7.351  -11.013 1.00 23.92 ?  108 LEU   A HD12 1 
ATOM   2375 H HD13 . LEU   A 1 108 ? 28.343 -7.437  -10.013 1.00 23.92 ?  108 LEU   A HD13 1 
ATOM   2376 H HD21 . LEU   A 1 108 ? 29.227 -10.079 -10.540 1.00 25.51 ?  108 LEU   A HD21 1 
ATOM   2377 H HD22 . LEU   A 1 108 ? 28.913 -9.813  -9.005  1.00 25.51 ?  108 LEU   A HD22 1 
ATOM   2378 H HD23 . LEU   A 1 108 ? 28.237 -11.040 -9.754  1.00 25.51 ?  108 LEU   A HD23 1 
ATOM   2379 N N    . LEU   A 1 109 ? 23.604 -10.255 -7.362  1.00 15.06 ?  109 LEU   A N    1 
ATOM   2380 C CA   . LEU   A 1 109 ? 22.898 -10.126 -6.092  1.00 14.27 ?  109 LEU   A CA   1 
ATOM   2381 C C    . LEU   A 1 109 ? 23.252 -11.265 -5.138  1.00 13.38 ?  109 LEU   A C    1 
ATOM   2382 O O    . LEU   A 1 109 ? 23.414 -11.048 -3.933  1.00 13.77 ?  109 LEU   A O    1 
ATOM   2383 C CB   . LEU   A 1 109 ? 21.390 -10.052 -6.346  1.00 15.21 ?  109 LEU   A CB   1 
ATOM   2384 C CG   . LEU   A 1 109 ? 20.498 -9.768  -5.135  1.00 14.96 ?  109 LEU   A CG   1 
ATOM   2385 C CD1  . LEU   A 1 109 ? 20.963 -8.515  -4.428  1.00 15.16 ?  109 LEU   A CD1  1 
ATOM   2386 C CD2  . LEU   A 1 109 ? 19.040 -9.646  -5.558  1.00 16.35 ?  109 LEU   A CD2  1 
ATOM   2387 H H    . LEU   A 1 109 ? 23.092 -10.351 -8.048  1.00 18.08 ?  109 LEU   A H    1 
ATOM   2388 H HA   . LEU   A 1 109 ? 23.168 -9.290  -5.676  1.00 17.13 ?  109 LEU   A HA   1 
ATOM   2389 H HB2  . LEU   A 1 109 ? 21.225 -9.343  -6.991  1.00 18.26 ?  109 LEU   A HB2  1 
ATOM   2390 H HB3  . LEU   A 1 109 ? 21.104 -10.896 -6.721  1.00 18.26 ?  109 LEU   A HB3  1 
ATOM   2391 H HG   . LEU   A 1 109 ? 20.566 -10.507 -4.512  1.00 17.96 ?  109 LEU   A HG   1 
ATOM   2392 H HD11 . LEU   A 1 109 ? 20.286 -8.241  -3.796  1.00 18.20 ?  109 LEU   A HD11 1 
ATOM   2393 H HD12 . LEU   A 1 109 ? 21.794 -8.707  -3.967  1.00 18.20 ?  109 LEU   A HD12 1 
ATOM   2394 H HD13 . LEU   A 1 109 ? 21.103 -7.818  -5.090  1.00 18.20 ?  109 LEU   A HD13 1 
ATOM   2395 H HD21 . LEU   A 1 109 ? 18.508 -9.344  -4.800  1.00 19.62 ?  109 LEU   A HD21 1 
ATOM   2396 H HD22 . LEU   A 1 109 ? 18.963 -9.010  -6.285  1.00 19.62 ?  109 LEU   A HD22 1 
ATOM   2397 H HD23 . LEU   A 1 109 ? 18.714 -10.518 -5.851  1.00 19.62 ?  109 LEU   A HD23 1 
ATOM   2398 N N    . LYS   A 1 110 ? 23.371 -12.488 -5.651  1.00 13.75 ?  110 LYS   A N    1 
ATOM   2399 C CA   . LYS   A 1 110 ? 23.743 -13.596 -4.778  1.00 14.03 ?  110 LYS   A CA   1 
ATOM   2400 C C    . LYS   A 1 110 ? 25.121 -13.371 -4.166  1.00 13.53 ?  110 LYS   A C    1 
ATOM   2401 O O    . LYS   A 1 110 ? 25.313 -13.572 -2.964  1.00 13.57 ?  110 LYS   A O    1 
ATOM   2402 C CB   . LYS   A 1 110 ? 23.671 -14.921 -5.538  1.00 15.06 ?  110 LYS   A CB   1 
ATOM   2403 C CG   . LYS   A 1 110 ? 23.860 -16.130 -4.626  1.00 15.36 ?  110 LYS   A CG   1 
ATOM   2404 C CD   . LYS   A 1 110 ? 23.616 -17.462 -5.336  1.00 16.38 ?  110 LYS   A CD   1 
ATOM   2405 C CE   . LYS   A 1 110 ? 23.749 -18.641 -4.385  1.00 17.24 ?  110 LYS   A CE   1 
ATOM   2406 N NZ   . LYS   A 1 110 ? 22.591 -18.756 -3.457  1.00 18.19 ?  110 LYS   A NZ   1 
ATOM   2407 H H    . LYS   A 1 110 ? 23.237 -12.695 -6.471  1.00 16.51 ?  110 LYS   A H    1 
ATOM   2408 H HA   . LYS   A 1 110 ? 23.103 -13.649 -4.051  1.00 16.84 ?  110 LYS   A HA   1 
ATOM   2409 H HB2  . LYS   A 1 110 ? 22.802 -14.998 -5.963  1.00 18.08 ?  110 LYS   A HB2  1 
ATOM   2410 H HB3  . LYS   A 1 110 ? 24.371 -14.940 -6.211  1.00 18.08 ?  110 LYS   A HB3  1 
ATOM   2411 H HG2  . LYS   A 1 110 ? 24.770 -16.130 -4.289  1.00 18.44 ?  110 LYS   A HG2  1 
ATOM   2412 H HG3  . LYS   A 1 110 ? 23.234 -16.066 -3.888  1.00 18.44 ?  110 LYS   A HG3  1 
ATOM   2413 H HD2  . LYS   A 1 110 ? 22.722 -17.472 -5.702  1.00 19.66 ?  110 LYS   A HD2  1 
ATOM   2414 H HD3  . LYS   A 1 110 ? 24.272 -17.568 -6.045  1.00 19.66 ?  110 LYS   A HD3  1 
ATOM   2415 H HE2  . LYS   A 1 110 ? 23.810 -19.465 -4.900  1.00 20.70 ?  110 LYS   A HE2  1 
ATOM   2416 H HE3  . LYS   A 1 110 ? 24.559 -18.535 -3.850  1.00 20.70 ?  110 LYS   A HE3  1 
ATOM   2417 H HZ1  . LYS   A 1 110 ? 22.701 -19.452 -2.916  1.00 21.84 ?  110 LYS   A HZ1  1 
ATOM   2418 H HZ2  . LYS   A 1 110 ? 22.526 -18.014 -2.968  1.00 21.84 ?  110 LYS   A HZ2  1 
ATOM   2419 H HZ3  . LYS   A 1 110 ? 21.843 -18.862 -3.924  1.00 21.84 ?  110 LYS   A HZ3  1 
ATOM   2420 N N    . SER   A 1 111 ? 26.088 -12.942 -4.980  1.00 13.67 ?  111 SER   A N    1 
ATOM   2421 C CA   . SER   A 1 111 ? 27.420 -12.644 -4.465  1.00 13.65 ?  111 SER   A CA   1 
ATOM   2422 C C    . SER   A 1 111 ? 27.359 -11.584 -3.377  1.00 13.22 ?  111 SER   A C    1 
ATOM   2423 O O    . SER   A 1 111 ? 28.053 -11.686 -2.360  1.00 13.74 ?  111 SER   A O    1 
ATOM   2424 C CB   . SER   A 1 111 ? 28.314 -12.170 -5.607  1.00 15.10 ?  111 SER   A CB   1 
ATOM   2425 O OG   . SER   A 1 111 ? 28.412 -13.171 -6.602  1.00 17.01 ?  111 SER   A OG   1 
ATOM   2426 H H    . SER   A 1 111 ? 25.998 -12.817 -5.822  1.00 16.42 ?  111 SER   A H    1 
ATOM   2427 H HA   . SER   A 1 111 ? 27.813 -13.450 -4.085  1.00 16.39 ?  111 SER   A HA   1 
ATOM   2428 H HB2  . SER   A 1 111 ? 27.926 -11.377 -6.007  1.00 18.13 ?  111 SER   A HB2  1 
ATOM   2429 H HB3  . SER   A 1 111 ? 29.199 -11.972 -5.263  1.00 18.13 ?  111 SER   A HB3  1 
ATOM   2430 H HG   . SER   A 1 111 ? 28.918 -12.907 -7.231  1.00 20.41 ?  111 SER   A HG   1 
ATOM   2431 N N    . ALA   A 1 112 ? 26.528 -10.558 -3.576  1.00 13.14 ?  112 ALA   A N    1 
ATOM   2432 C CA   . ALA   A 1 112 ? 26.379 -9.517  -2.565  1.00 13.40 ?  112 ALA   A CA   1 
ATOM   2433 C C    . ALA   A 1 112 ? 25.884 -10.105 -1.242  1.00 13.01 ?  112 ALA   A C    1 
ATOM   2434 O O    . ALA   A 1 112 ? 26.424 -9.807  -0.171  1.00 13.31 ?  112 ALA   A O    1 
ATOM   2435 C CB   . ALA   A 1 112 ? 25.433 -8.428  -3.079  1.00 13.61 ?  112 ALA   A CB   1 
ATOM   2436 H H    . ALA   A 1 112 ? 26.049 -10.444 -4.283  1.00 15.78 ?  112 ALA   A H    1 
ATOM   2437 H HA   . ALA   A 1 112 ? 27.241 -9.101  -2.410  1.00 16.09 ?  112 ALA   A HA   1 
ATOM   2438 H HB1  . ALA   A 1 112 ? 25.353 -7.729  -2.407  1.00 16.33 ?  112 ALA   A HB1  1 
ATOM   2439 H HB2  . ALA   A 1 112 ? 25.792 -8.048  -3.900  1.00 16.33 ?  112 ALA   A HB2  1 
ATOM   2440 H HB3  . ALA   A 1 112 ? 24.560 -8.816  -3.255  1.00 16.33 ?  112 ALA   A HB3  1 
ATOM   2441 N N    . TYR   A 1 113 ? 24.842 -10.939 -1.290  1.00 12.77 ?  113 TYR   A N    1 
ATOM   2442 C CA   . TYR   A 1 113 ? 24.334 -11.547 -0.058  1.00 12.56 ?  113 TYR   A CA   1 
ATOM   2443 C C    . TYR   A 1 113 ? 25.336 -12.493 0.606   1.00 12.40 ?  113 TYR   A C    1 
ATOM   2444 O O    . TYR   A 1 113 ? 25.293 -12.667 1.827   1.00 13.26 ?  113 TYR   A O    1 
ATOM   2445 C CB   . TYR   A 1 113 ? 23.021 -12.279 -0.319  1.00 13.13 ?  113 TYR   A CB   1 
ATOM   2446 C CG   . TYR   A 1 113 ? 21.797 -11.389 -0.246  1.00 12.70 ?  113 TYR   A CG   1 
ATOM   2447 C CD1  . TYR   A 1 113 ? 21.424 -10.788 0.952   1.00 13.07 ?  113 TYR   A CD1  1 
ATOM   2448 C CD2  . TYR   A 1 113 ? 21.000 -11.171 -1.360  1.00 13.22 ?  113 TYR   A CD2  1 
ATOM   2449 C CE1  . TYR   A 1 113 ? 20.292 -9.995  1.034   1.00 13.21 ?  113 TYR   A CE1  1 
ATOM   2450 C CE2  . TYR   A 1 113 ? 19.845 -10.379 -1.281  1.00 13.25 ?  113 TYR   A CE2  1 
ATOM   2451 C CZ   . TYR   A 1 113 ? 19.510 -9.795  -0.081  1.00 12.97 ?  113 TYR   A CZ   1 
ATOM   2452 O OH   . TYR   A 1 113 ? 18.377 -9.015  0.031   1.00 13.79 ?  113 TYR   A OH   1 
ATOM   2453 H H    . TYR   A 1 113 ? 24.418 -11.157 -2.011  1.00 15.33 ?  113 TYR   A H    1 
ATOM   2454 H HA   . TYR   A 1 113 ? 24.151 -10.838 0.571   1.00 15.08 ?  113 TYR   A HA   1 
ATOM   2455 H HB2  . TYR   A 1 113 ? 23.043 -12.666 -1.207  1.00 15.76 ?  113 TYR   A HB2  1 
ATOM   2456 H HB3  . TYR   A 1 113 ? 22.917 -12.980 0.343   1.00 15.76 ?  113 TYR   A HB3  1 
ATOM   2457 H HD1  . TYR   A 1 113 ? 21.945 -10.930 1.714   1.00 15.70 ?  113 TYR   A HD1  1 
ATOM   2458 H HD2  . TYR   A 1 113 ? 21.218 -11.575 -2.165  1.00 15.87 ?  113 TYR   A HD2  1 
ATOM   2459 H HE1  . TYR   A 1 113 ? 20.055 -9.605  1.845   1.00 15.86 ?  113 TYR   A HE1  1 
ATOM   2460 H HE2  . TYR   A 1 113 ? 19.311 -10.239 -2.031  1.00 15.91 ?  113 TYR   A HE2  1 
ATOM   2461 H HH   . TYR   A 1 113 ? 17.995 -8.979  -0.727  1.00 16.55 ?  113 TYR   A HH   1 
ATOM   2462 N N    . GLU   A 1 114 ? 26.238 -13.114 -0.162  1.00 12.72 ?  114 GLU   A N    1 
ATOM   2463 C CA   . GLU   A 1 114 ? 27.216 -14.017 0.448   1.00 13.30 ?  114 GLU   A CA   1 
ATOM   2464 C C    . GLU   A 1 114 ? 28.067 -13.300 1.493   1.00 13.31 ?  114 GLU   A C    1 
ATOM   2465 O O    . GLU   A 1 114 ? 28.547 -13.925 2.443   1.00 13.68 ?  114 GLU   A O    1 
ATOM   2466 C CB   . GLU   A 1 114 ? 28.089 -14.670 -0.630  1.00 13.88 ?  114 GLU   A CB   1 
ATOM   2467 C CG   . GLU   A 1 114 ? 27.328 -15.728 -1.406  1.00 14.81 ?  114 GLU   A CG   1 
ATOM   2468 C CD   . GLU   A 1 114 ? 28.042 -16.270 -2.629  1.00 14.84 ?  114 GLU   A CD   1 
ATOM   2469 O OE1  . GLU   A 1 114 ? 29.000 -15.646 -3.133  1.00 15.32 ?  114 GLU   A OE1  1 
ATOM   2470 O OE2  . GLU   A 1 114 ? 27.601 -17.332 -3.107  1.00 16.10 -1 114 GLU   A OE2  1 
ATOM   2471 H H    . GLU   A 1 114 ? 26.308 -13.028 -1.019  1.00 15.28 ?  114 GLU   A H    1 
ATOM   2472 H HA   . GLU   A 1 114 ? 26.738 -14.723 0.902   1.00 15.97 ?  114 GLU   A HA   1 
ATOM   2473 H HB2  . GLU   A 1 114 ? 28.388 -13.993 -1.258  1.00 16.66 ?  114 GLU   A HB2  1 
ATOM   2474 H HB3  . GLU   A 1 114 ? 28.853 -15.096 -0.210  1.00 16.66 ?  114 GLU   A HB3  1 
ATOM   2475 H HG2  . GLU   A 1 114 ? 27.157 -16.480 -0.817  1.00 17.78 ?  114 GLU   A HG2  1 
ATOM   2476 H HG3  . GLU   A 1 114 ? 26.484 -15.349 -1.700  1.00 17.78 ?  114 GLU   A HG3  1 
ATOM   2477 N N    . ASN   A 1 115 ? 28.251 -11.987 1.350   1.00 12.88 ?  115 ASN   A N    1 
ATOM   2478 C CA   . ASN   A 1 115 ? 29.008 -11.242 2.351   1.00 13.50 ?  115 ASN   A CA   1 
ATOM   2479 C C    . ASN   A 1 115 ? 28.389 -11.371 3.734   1.00 13.65 ?  115 ASN   A C    1 
ATOM   2480 O O    . ASN   A 1 115 ? 29.096 -11.304 4.747   1.00 13.79 ?  115 ASN   A O    1 
ATOM   2481 C CB   . ASN   A 1 115 ? 29.105 -9.768  1.960   1.00 13.84 ?  115 ASN   A CB   1 
ATOM   2482 C CG   . ASN   A 1 115 ? 29.924 -9.563  0.709   1.00 13.94 ?  115 ASN   A CG   1 
ATOM   2483 O OD1  . ASN   A 1 115 ? 31.146 -9.662  0.746   1.00 17.59 ?  115 ASN   A OD1  1 
ATOM   2484 N ND2  . ASN   A 1 115 ? 29.265 -9.279  -0.400  1.00 13.40 ?  115 ASN   A ND2  1 
ATOM   2485 H H    . ASN   A 1 115 ? 27.950 -11.510 0.700   1.00 15.46 ?  115 ASN   A H    1 
ATOM   2486 H HA   . ASN   A 1 115 ? 29.908 -11.597 2.396   1.00 16.21 ?  115 ASN   A HA   1 
ATOM   2487 H HB2  . ASN   A 1 115 ? 28.203 -9.423  1.809   1.00 16.62 ?  115 ASN   A HB2  1 
ATOM   2488 H HB3  . ASN   A 1 115 ? 29.520 -9.273  2.686   1.00 16.62 ?  115 ASN   A HB3  1 
ATOM   2489 H HD21 . ASN   A 1 115 ? 29.691 -9.155  -1.135  1.00 16.09 ?  115 ASN   A HD21 1 
ATOM   2490 H HD22 . ASN   A 1 115 ? 28.401 -9.239  -0.395  1.00 16.09 ?  115 ASN   A HD22 1 
ATOM   2491 N N    . PHE   A 1 116 ? 27.066 -11.538 3.803   1.00 13.58 ?  116 PHE   A N    1 
ATOM   2492 C CA   . PHE   A 1 116 ? 26.407 -11.635 5.101   1.00 13.11 ?  116 PHE   A CA   1 
ATOM   2493 C C    . PHE   A 1 116 ? 26.884 -12.857 5.880   1.00 13.24 ?  116 PHE   A C    1 
ATOM   2494 O O    . PHE   A 1 116 ? 26.812 -12.871 7.112   1.00 14.13 ?  116 PHE   A O    1 
ATOM   2495 C CB   . PHE   A 1 116 ? 24.882 -11.770 4.945   1.00 13.59 ?  116 PHE   A CB   1 
ATOM   2496 C CG   . PHE   A 1 116 ? 24.135 -10.518 4.496   1.00 12.78 ?  116 PHE   A CG   1 
ATOM   2497 C CD1  . PHE   A 1 116 ? 24.714 -9.490  3.753   1.00 12.67 ?  116 PHE   A CD1  1 
ATOM   2498 C CD2  . PHE   A 1 116 ? 22.786 -10.407 4.820   1.00 13.55 ?  116 PHE   A CD2  1 
ATOM   2499 C CE1  . PHE   A 1 116 ? 23.945 -8.404  3.343   1.00 13.34 ?  116 PHE   A CE1  1 
ATOM   2500 C CE2  . PHE   A 1 116 ? 22.027 -9.328  4.418   1.00 14.06 ?  116 PHE   A CE2  1 
ATOM   2501 C CZ   . PHE   A 1 116 ? 22.604 -8.323  3.682   1.00 13.73 ?  116 PHE   A CZ   1 
ATOM   2502 H H    . PHE   A 1 116 ? 26.535 -11.592 3.124   1.00 16.30 ?  116 PHE   A H    1 
ATOM   2503 H HA   . PHE   A 1 116 ? 26.592 -10.846 5.624   1.00 15.74 ?  116 PHE   A HA   1 
ATOM   2504 H HB2  . PHE   A 1 116 ? 24.699 -12.466 4.290   1.00 16.32 ?  116 PHE   A HB2  1 
ATOM   2505 H HB3  . PHE   A 1 116 ? 24.508 -12.035 5.801   1.00 16.32 ?  116 PHE   A HB3  1 
ATOM   2506 H HD1  . PHE   A 1 116 ? 25.607 -9.552  3.509   1.00 15.22 ?  116 PHE   A HD1  1 
ATOM   2507 H HD2  . PHE   A 1 116 ? 22.380 -11.090 5.307   1.00 16.27 ?  116 PHE   A HD2  1 
ATOM   2508 H HE1  . PHE   A 1 116 ? 24.343 -7.721  2.847   1.00 16.01 ?  116 PHE   A HE1  1 
ATOM   2509 H HE2  . PHE   A 1 116 ? 21.124 -9.277  4.653   1.00 16.89 ?  116 PHE   A HE2  1 
ATOM   2510 H HZ   . PHE   A 1 116 ? 22.099 -7.584  3.420   1.00 16.49 ?  116 PHE   A HZ   1 
ATOM   2511 N N    . ASN   A 1 117 ? 27.336 -13.909 5.185   1.00 13.48 ?  117 ASN   A N    1 
ATOM   2512 C CA   . ASN   A 1 117 ? 27.695 -15.153 5.858   1.00 13.93 ?  117 ASN   A CA   1 
ATOM   2513 C C    . ASN   A 1 117 ? 28.949 -15.037 6.703   1.00 15.01 ?  117 ASN   A C    1 
ATOM   2514 O O    . ASN   A 1 117 ? 29.232 -15.952 7.483   1.00 15.45 ?  117 ASN   A O    1 
ATOM   2515 C CB   . ASN   A 1 117 ? 27.812 -16.282 4.843   1.00 14.22 ?  117 ASN   A CB   1 
ATOM   2516 C CG   . ASN   A 1 117 ? 26.468 -16.681 4.321   1.00 14.19 ?  117 ASN   A CG   1 
ATOM   2517 O OD1  . ASN   A 1 117 ? 25.494 -16.697 5.070   1.00 15.14 ?  117 ASN   A OD1  1 
ATOM   2518 N ND2  . ASN   A 1 117 ? 26.386 -16.957 3.039   1.00 14.24 ?  117 ASN   A ND2  1 
ATOM   2519 H H    . ASN   A 1 117 ? 27.423 -13.928 4.323   1.00 16.18 ?  117 ASN   A H    1 
ATOM   2520 H HA   . ASN   A 1 117 ? 26.968 -15.385 6.454   1.00 16.72 ?  117 ASN   A HA   1 
ATOM   2521 H HB2  . ASN   A 1 117 ? 28.356 -15.989 4.093   1.00 17.07 ?  117 ASN   A HB2  1 
ATOM   2522 H HB3  . ASN   A 1 117 ? 28.209 -17.054 5.268   1.00 17.07 ?  117 ASN   A HB3  1 
ATOM   2523 H HD21 . ASN   A 1 117 ? 25.636 -17.185 2.700   1.00 17.10 ?  117 ASN   A HD21 1 
ATOM   2524 H HD22 . ASN   A 1 117 ? 27.096 -16.933 2.551   1.00 17.10 ?  117 ASN   A HD22 1 
ATOM   2525 N N    . GLN   A 1 118 ? 29.673 -13.924 6.600   1.00 14.55 ?  118 GLN   A N    1 
ATOM   2526 C CA   . GLN   A 1 118 ? 30.842 -13.697 7.431   1.00 15.31 ?  118 GLN   A CA   1 
ATOM   2527 C C    . GLN   A 1 118 ? 30.495 -13.125 8.800   1.00 15.25 ?  118 GLN   A C    1 
ATOM   2528 O O    . GLN   A 1 118 ? 31.408 -12.839 9.583   1.00 16.62 ?  118 GLN   A O    1 
ATOM   2529 C CB   . GLN   A 1 118 ? 31.849 -12.796 6.702   1.00 15.38 ?  118 GLN   A CB   1 
ATOM   2530 C CG   . GLN   A 1 118 ? 32.327 -13.373 5.382   1.00 15.39 ?  118 GLN   A CG   1 
ATOM   2531 C CD   . GLN   A 1 118 ? 33.167 -14.626 5.563   1.00 15.98 ?  118 GLN   A CD   1 
ATOM   2532 O OE1  . GLN   A 1 118 ? 34.028 -14.692 6.450   1.00 16.77 ?  118 GLN   A OE1  1 
ATOM   2533 N NE2  . GLN   A 1 118 ? 32.923 -15.629 4.720   1.00 15.79 ?  118 GLN   A NE2  1 
ATOM   2534 H H    . GLN   A 1 118 ? 29.504 -13.277 6.048   1.00 17.47 ?  118 GLN   A H    1 
ATOM   2535 H HA   . GLN   A 1 118 ? 31.274 -14.552 7.579   1.00 18.38 ?  118 GLN   A HA   1 
ATOM   2536 H HB2  . GLN   A 1 118 ? 31.433 -11.940 6.521   1.00 18.46 ?  118 GLN   A HB2  1 
ATOM   2537 H HB3  . GLN   A 1 118 ? 32.627 -12.673 7.270   1.00 18.46 ?  118 GLN   A HB3  1 
ATOM   2538 H HG2  . GLN   A 1 118 ? 31.557 -13.599 4.832   1.00 18.47 ?  118 GLN   A HG2  1 
ATOM   2539 H HG3  . GLN   A 1 118 ? 32.874 -12.715 4.923   1.00 18.47 ?  118 GLN   A HG3  1 
ATOM   2540 H HE21 . GLN   A 1 118 ? 32.311 -15.546 4.113   1.00 18.96 ?  118 GLN   A HE21 1 
ATOM   2541 H HE22 . GLN   A 1 118 ? 33.364 -16.363 4.778   1.00 18.96 ?  118 GLN   A HE22 1 
ATOM   2542 N N    . HIS   A 1 119 ? 29.207 -12.939 9.103   1.00 14.82 ?  119 HIS   A N    1 
ATOM   2543 C CA   . HIS   A 1 119 ? 28.756 -12.327 10.347  1.00 15.33 ?  119 HIS   A CA   1 
ATOM   2544 C C    . HIS   A 1 119 ? 27.608 -13.137 10.924  1.00 16.13 ?  119 HIS   A C    1 
ATOM   2545 O O    . HIS   A 1 119 ? 26.664 -13.475 10.209  1.00 16.26 ?  119 HIS   A O    1 
ATOM   2546 C CB   . HIS   A 1 119 ? 28.311 -10.900 10.070  1.00 15.97 ?  119 HIS   A CB   1 
ATOM   2547 C CG   . HIS   A 1 119 ? 29.401 -10.098 9.452   1.00 16.78 ?  119 HIS   A CG   1 
ATOM   2548 N ND1  . HIS   A 1 119 ? 30.376 -9.488  10.206  1.00 18.84 ?  119 HIS   A ND1  1 
ATOM   2549 C CD2  . HIS   A 1 119 ? 29.738 -9.900  8.157   1.00 16.94 ?  119 HIS   A CD2  1 
ATOM   2550 C CE1  . HIS   A 1 119 ? 31.245 -8.905  9.399   1.00 18.41 ?  119 HIS   A CE1  1 
ATOM   2551 N NE2  . HIS   A 1 119 ? 30.890 -9.150  8.151   1.00 18.29 ?  119 HIS   A NE2  1 
ATOM   2552 H H    . HIS   A 1 119 ? 28.556 -13.168 8.580   1.00 17.80 ?  119 HIS   A H    1 
ATOM   2553 H HA   . HIS   A 1 119 ? 29.485 -12.316 10.984  1.00 18.41 ?  119 HIS   A HA   1 
ATOM   2554 H HB2  . HIS   A 1 119 ? 27.553 -10.910 9.463   1.00 19.17 ?  119 HIS   A HB2  1 
ATOM   2555 H HB3  . HIS   A 1 119 ? 28.057 -10.479 10.910  1.00 19.17 ?  119 HIS   A HB3  1 
ATOM   2556 H HD2  . HIS   A 1 119 ? 29.274 -10.212 7.411   1.00 20.34 ?  119 HIS   A HD2  1 
ATOM   2557 H HE1  . HIS   A 1 119 ? 31.983 -8.403  9.660   1.00 22.09 ?  119 HIS   A HE1  1 
ATOM   2558 H HE2  . HIS   A 1 119 ? 31.293 -8.863  7.447   1.00 21.95 ?  119 HIS   A HE2  1 
ATOM   2559 N N    A GLU   A 1 120 ? 27.692 -13.458 12.217  0.48 16.99 ?  120 GLU   A N    1 
ATOM   2560 N N    B GLU   A 1 120 ? 27.669 -13.391 12.234  0.52 17.06 ?  120 GLU   A N    1 
ATOM   2561 C CA   A GLU   A 1 120 ? 26.718 -14.376 12.804  0.48 19.55 ?  120 GLU   A CA   1 
ATOM   2562 C CA   B GLU   A 1 120 ? 26.700 -14.283 12.866  0.52 19.41 ?  120 GLU   A CA   1 
ATOM   2563 C C    A GLU   A 1 120 ? 25.308 -13.792 12.850  0.48 17.61 ?  120 GLU   A C    1 
ATOM   2564 C C    B GLU   A 1 120 ? 25.292 -13.692 12.900  0.52 17.86 ?  120 GLU   A C    1 
ATOM   2565 O O    A GLU   A 1 120 ? 24.326 -14.543 12.738  0.48 17.62 ?  120 GLU   A O    1 
ATOM   2566 O O    B GLU   A 1 120 ? 24.304 -14.430 12.765  0.52 18.49 ?  120 GLU   A O    1 
ATOM   2567 C CB   A GLU   A 1 120 ? 27.167 -14.795 14.204  0.48 25.14 ?  120 GLU   A CB   1 
ATOM   2568 C CB   B GLU   A 1 120 ? 27.162 -14.645 14.277  0.52 24.58 ?  120 GLU   A CB   1 
ATOM   2569 C CG   A GLU   A 1 120 ? 28.377 -15.713 14.205  0.48 31.60 ?  120 GLU   A CG   1 
ATOM   2570 C CG   B GLU   A 1 120 ? 28.344 -15.599 14.307  0.52 31.18 ?  120 GLU   A CG   1 
ATOM   2571 C CD   A GLU   A 1 120 ? 28.600 -16.384 15.545  0.48 37.06 ?  120 GLU   A CD   1 
ATOM   2572 C CD   B GLU   A 1 120 ? 28.464 -16.330 15.629  0.52 36.85 ?  120 GLU   A CD   1 
ATOM   2573 O OE1  A GLU   A 1 120 ? 28.144 -15.832 16.569  0.48 38.72 ?  120 GLU   A OE1  1 
ATOM   2574 O OE1  B GLU   A 1 120 ? 27.872 -15.859 16.624  0.52 38.56 ?  120 GLU   A OE1  1 
ATOM   2575 O OE2  A GLU   A 1 120 ? 29.228 -17.464 15.574  0.48 39.14 -1 120 GLU   A OE2  1 
ATOM   2576 O OE2  B GLU   A 1 120 ? 29.145 -17.376 15.672  0.52 39.10 -1 120 GLU   A OE2  1 
ATOM   2577 H H    A GLU   A 1 120 ? 28.295 -13.164 12.761  0.48 20.40 ?  120 GLU   A H    1 
ATOM   2578 H H    B GLU   A 1 120 ? 28.258 -13.060 12.770  0.52 20.48 ?  120 GLU   A H    1 
ATOM   2579 H HA   A GLU   A 1 120 ? 26.690 -15.174 12.260  0.48 23.47 ?  120 GLU   A HA   1 
ATOM   2580 H HA   B GLU   A 1 120 ? 26.660 -15.100 12.354  0.52 23.30 ?  120 GLU   A HA   1 
ATOM   2581 H HB2  A GLU   A 1 120 ? 27.397 -14.004 14.716  0.48 30.17 ?  120 GLU   A HB2  1 
ATOM   2582 H HB2  B GLU   A 1 120 ? 27.425 -13.837 14.745  0.52 29.50 ?  120 GLU   A HB2  1 
ATOM   2583 H HB3  A GLU   A 1 120 ? 26.438 -15.267 14.638  0.48 30.17 ?  120 GLU   A HB3  1 
ATOM   2584 H HB3  B GLU   A 1 120 ? 26.427 -15.072 14.748  0.52 29.50 ?  120 GLU   A HB3  1 
ATOM   2585 H HG2  A GLU   A 1 120 ? 28.255 -16.399 13.528  0.48 37.93 ?  120 GLU   A HG2  1 
ATOM   2586 H HG2  B GLU   A 1 120 ? 28.242 -16.252 13.595  0.52 37.42 ?  120 GLU   A HG2  1 
ATOM   2587 H HG3  A GLU   A 1 120 ? 29.171 -15.193 14.010  0.48 37.93 ?  120 GLU   A HG3  1 
ATOM   2588 H HG3  B GLU   A 1 120 ? 29.162 -15.095 14.180  0.52 37.42 ?  120 GLU   A HG3  1 
ATOM   2589 N N    A VAL   A 1 121 ? 25.188 -12.480 13.047  0.48 16.91 ?  121 VAL   A N    1 
ATOM   2590 N N    B VAL   A 1 121 ? 25.172 -12.383 13.123  0.52 17.19 ?  121 VAL   A N    1 
ATOM   2591 C CA   A VAL   A 1 121 ? 23.904 -11.789 13.134  0.48 16.84 ?  121 VAL   A CA   1 
ATOM   2592 C CA   B VAL   A 1 121 ? 23.871 -11.723 13.230  0.52 17.06 ?  121 VAL   A CA   1 
ATOM   2593 C C    A VAL   A 1 121 ? 24.051 -10.448 12.423  0.48 15.67 ?  121 VAL   A C    1 
ATOM   2594 C C    B VAL   A 1 121 ? 23.969 -10.353 12.581  0.52 15.11 ?  121 VAL   A C    1 
ATOM   2595 O O    A VAL   A 1 121 ? 25.102 -9.805  12.505  0.48 16.48 ?  121 VAL   A O    1 
ATOM   2596 O O    B VAL   A 1 121 ? 24.894 -9.589  12.880  0.52 14.20 ?  121 VAL   A O    1 
ATOM   2597 C CB   A VAL   A 1 121 ? 23.483 -11.571 14.607  0.48 19.60 ?  121 VAL   A CB   1 
ATOM   2598 C CB   B VAL   A 1 121 ? 23.413 -11.562 14.695  0.52 20.10 ?  121 VAL   A CB   1 
ATOM   2599 C CG1  A VAL   A 1 121 ? 22.113 -10.900 14.698  0.48 20.41 ?  121 VAL   A CG1  1 
ATOM   2600 C CG1  B VAL   A 1 121 ? 22.048 -10.884 14.750  0.52 20.78 ?  121 VAL   A CG1  1 
ATOM   2601 C CG2  A VAL   A 1 121 ? 23.478 -12.880 15.388  0.48 21.08 ?  121 VAL   A CG2  1 
ATOM   2602 C CG2  B VAL   A 1 121 ? 23.365 -12.897 15.413  0.52 21.73 ?  121 VAL   A CG2  1 
ATOM   2603 H H    A VAL   A 1 121 ? 25.858 -11.952 13.143  0.48 20.30 ?  121 VAL   A H    1 
ATOM   2604 H H    B VAL   A 1 121 ? 25.840 -11.842 13.217  0.52 20.63 ?  121 VAL   A H    1 
ATOM   2605 H HA   A VAL   A 1 121 ? 23.216 -12.315 12.692  0.48 20.22 ?  121 VAL   A HA   1 
ATOM   2606 H HA   B VAL   A 1 121 ? 23.208 -12.239 12.754  0.52 20.48 ?  121 VAL   A HA   1 
ATOM   2607 H HB   A VAL   A 1 121 ? 24.125 -10.984 15.032  0.48 23.53 ?  121 VAL   A HB   1 
ATOM   2608 H HB   B VAL   A 1 121 ? 24.042 -10.990 15.162  0.52 24.12 ?  121 VAL   A HB   1 
ATOM   2609 H HG11 A VAL   A 1 121 ? 21.822 -10.892 15.626  0.48 24.49 ?  121 VAL   A HG11 1 
ATOM   2610 H HG11 B VAL   A 1 121 ? 21.685 -10.981 15.643  0.52 24.94 ?  121 VAL   A HG11 1 
ATOM   2611 H HG12 A VAL   A 1 121 ? 22.181 -9.991  14.369  0.48 24.49 ?  121 VAL   A HG12 1 
ATOM   2612 H HG12 B VAL   A 1 121 ? 22.147 -9.943  14.535  0.52 24.94 ?  121 VAL   A HG12 1 
ATOM   2613 H HG13 A VAL   A 1 121 ? 21.477 -11.401 14.162  0.48 24.49 ?  121 VAL   A HG13 1 
ATOM   2614 H HG13 B VAL   A 1 121 ? 21.458 -11.311 14.107  0.52 24.94 ?  121 VAL   A HG13 1 
ATOM   2615 H HG21 A VAL   A 1 121 ? 23.143 -12.711 16.288  0.48 25.30 ?  121 VAL   A HG21 1 
ATOM   2616 H HG21 B VAL   A 1 121 ? 23.025 -12.757 16.314  0.52 26.08 ?  121 VAL   A HG21 1 
ATOM   2617 H HG22 A VAL   A 1 121 ? 22.898 -13.515 14.940  0.48 25.30 ?  121 VAL   A HG22 1 
ATOM   2618 H HG22 B VAL   A 1 121 ? 22.774 -13.494 14.930  0.52 26.08 ?  121 VAL   A HG22 1 
ATOM   2619 H HG23 A VAL   A 1 121 ? 24.380 -13.227 15.434  0.48 25.30 ?  121 VAL   A HG23 1 
ATOM   2620 H HG23 B VAL   A 1 121 ? 24.257 -13.267 15.451  0.52 26.08 ?  121 VAL   A HG23 1 
ATOM   2621 N N    . LEU   A 1 122 ? 23.000 -10.023 11.725  1.00 14.66 ?  122 LEU   A N    1 
ATOM   2622 C CA   . LEU   A 1 122 ? 23.005 -8.739  11.033  1.00 14.23 ?  122 LEU   A CA   1 
ATOM   2623 C C    . LEU   A 1 122 ? 21.609 -8.134  10.978  1.00 13.99 ?  122 LEU   A C    1 
ATOM   2624 O O    . LEU   A 1 122 ? 20.613 -8.849  10.841  1.00 15.05 ?  122 LEU   A O    1 
ATOM   2625 C CB   . LEU   A 1 122 ? 23.433 -8.868  9.570   1.00 15.58 ?  122 LEU   A CB   1 
ATOM   2626 C CG   . LEU   A 1 122 ? 24.656 -9.709  9.225   1.00 15.70 ?  122 LEU   A CG   1 
ATOM   2627 C CD1  . LEU   A 1 122 ? 24.255 -11.163 8.993   1.00 16.09 ?  122 LEU   A CD1  1 
ATOM   2628 C CD2  . LEU   A 1 122 ? 25.373 -9.145  8.005   1.00 15.26 ?  122 LEU   A CD2  1 
ATOM   2629 H H    A LEU   A 1 122 ? 22.268 -10.467 11.628  0.48 17.60 ?  122 LEU   A H    1 
ATOM   2630 H H    B LEU   A 1 122 ? 22.331 -10.530 11.528  0.52 17.60 ?  122 LEU   A H    1 
ATOM   2631 H HA   . LEU   A 1 122 ? 23.603 -8.117  11.482  1.00 17.08 ?  122 LEU   A HA   1 
ATOM   2632 H HB2  . LEU   A 1 122 ? 22.699 -9.253  9.079   1.00 18.71 ?  122 LEU   A HB2  1 
ATOM   2633 H HB3  . LEU   A 1 122 ? 23.618 -7.982  9.233   1.00 18.71 ?  122 LEU   A HB3  1 
ATOM   2634 H HG   . LEU   A 1 122 ? 25.289 -9.695  9.963   1.00 18.85 ?  122 LEU   A HG   1 
ATOM   2635 H HD11 . LEU   A 1 122 ? 25.045 -11.682 8.766   1.00 19.31 ?  122 LEU   A HD11 1 
ATOM   2636 H HD12 . LEU   A 1 122 ? 23.853 -11.510 9.800   1.00 19.31 ?  122 LEU   A HD12 1 
ATOM   2637 H HD13 . LEU   A 1 122 ? 23.619 -11.199 8.260   1.00 19.31 ?  122 LEU   A HD13 1 
ATOM   2638 H HD21 . LEU   A 1 122 ? 26.133 -9.712  7.780   1.00 18.32 ?  122 LEU   A HD21 1 
ATOM   2639 H HD22 . LEU   A 1 122 ? 24.757 -9.114  7.257   1.00 18.32 ?  122 LEU   A HD22 1 
ATOM   2640 H HD23 . LEU   A 1 122 ? 25.689 -8.248  8.208   1.00 18.32 ?  122 LEU   A HD23 1 
ATOM   2641 N N    A LEU   A 1 123 ? 21.557 -6.810  11.116  0.48 13.47 ?  123 LEU   A N    1 
ATOM   2642 N N    B LEU   A 1 123 ? 21.555 -6.807  11.043  0.52 13.77 ?  123 LEU   A N    1 
ATOM   2643 C CA   A LEU   A 1 123 ? 20.385 -6.004  10.797  0.48 13.30 ?  123 LEU   A CA   1 
ATOM   2644 C CA   B LEU   A 1 123 ? 20.386 -6.028  10.642  0.52 13.62 ?  123 LEU   A CA   1 
ATOM   2645 C C    A LEU   A 1 123 ? 20.611 -5.444  9.400   0.48 12.39 ?  123 LEU   A C    1 
ATOM   2646 C C    B LEU   A 1 123 ? 20.639 -5.528  9.223   0.52 13.33 ?  123 LEU   A C    1 
ATOM   2647 O O    A LEU   A 1 123 ? 21.622 -4.770  9.166   0.48 12.35 ?  123 LEU   A O    1 
ATOM   2648 O O    B LEU   A 1 123 ? 21.736 -5.033  8.935   0.52 14.21 ?  123 LEU   A O    1 
ATOM   2649 C CB   A LEU   A 1 123 ? 20.246 -4.857  11.800  0.48 14.48 ?  123 LEU   A CB   1 
ATOM   2650 C CB   B LEU   A 1 123 ? 20.227 -4.836  11.588  0.52 13.76 ?  123 LEU   A CB   1 
ATOM   2651 C CG   A LEU   A 1 123 ? 19.227 -3.771  11.433  0.48 15.32 ?  123 LEU   A CG   1 
ATOM   2652 C CG   B LEU   A 1 123 ? 19.191 -3.753  11.275  0.52 15.12 ?  123 LEU   A CG   1 
ATOM   2653 C CD1  A LEU   A 1 123 ? 17.821 -4.353  11.359  0.48 15.69 ?  123 LEU   A CD1  1 
ATOM   2654 C CD1  B LEU   A 1 123 ? 17.780 -4.317  11.275  0.52 15.58 ?  123 LEU   A CD1  1 
ATOM   2655 C CD2  A LEU   A 1 123 ? 19.282 -2.594  12.409  0.48 15.97 ?  123 LEU   A CD2  1 
ATOM   2656 C CD2  B LEU   A 1 123 ? 19.311 -2.591  12.271  0.52 15.52 ?  123 LEU   A CD2  1 
ATOM   2657 H H    A LEU   A 1 123 ? 22.220 -6.337  11.391  0.48 16.17 ?  123 LEU   A H    1 
ATOM   2658 H H    B LEU   A 1 123 ? 22.208 -6.322  11.329  0.52 16.53 ?  123 LEU   A H    1 
ATOM   2659 H HA   A LEU   A 1 123 ? 19.584 -6.544  10.798  0.48 15.97 ?  123 LEU   A HA   1 
ATOM   2660 H HA   B LEU   A 1 123 ? 19.588 -6.586  10.667  0.52 16.36 ?  123 LEU   A HA   1 
ATOM   2661 H HB2  A LEU   A 1 123 ? 19.972 -5.233  12.652  0.48 17.39 ?  123 LEU   A HB2  1 
ATOM   2662 H HB2  B LEU   A 1 123 ? 19.997 -5.189  12.463  0.52 16.52 ?  123 LEU   A HB2  1 
ATOM   2663 H HB3  A LEU   A 1 123 ? 21.107 -4.425  11.898  0.48 17.39 ?  123 LEU   A HB3  1 
ATOM   2664 H HB3  B LEU   A 1 123 ? 21.082 -4.395  11.641  0.52 16.52 ?  123 LEU   A HB3  1 
ATOM   2665 H HG   A LEU   A 1 123 ? 19.440 -3.417  10.556  0.48 18.39 ?  123 LEU   A HG   1 
ATOM   2666 H HG   B LEU   A 1 123 ? 19.365 -3.395  10.391  0.52 18.15 ?  123 LEU   A HG   1 
ATOM   2667 H HD11 A LEU   A 1 123 ? 17.191 -3.639  11.177  0.48 18.84 ?  123 LEU   A HD11 1 
ATOM   2668 H HD11 B LEU   A 1 123 ? 17.150 -3.603  11.085  0.52 18.70 ?  123 LEU   A HD11 1 
ATOM   2669 H HD12 A LEU   A 1 123 ? 17.787 -5.012  10.645  0.48 18.84 ?  123 LEU   A HD12 1 
ATOM   2670 H HD12 B LEU   A 1 123 ? 17.716 -5.004  10.592  0.52 18.70 ?  123 LEU   A HD12 1 
ATOM   2671 H HD13 A LEU   A 1 123 ? 17.608 -4.775  12.206  0.48 18.84 ?  123 LEU   A HD13 1 
ATOM   2672 H HD13 B LEU   A 1 123 ? 17.591 -4.700  12.147  0.52 18.70 ?  123 LEU   A HD13 1 
ATOM   2673 H HD21 A LEU   A 1 123 ? 18.624 -1.931  12.142  0.48 19.17 ?  123 LEU   A HD21 1 
ATOM   2674 H HD21 B LEU   A 1 123 ? 18.646 -1.916  12.056  0.52 18.63 ?  123 LEU   A HD21 1 
ATOM   2675 H HD22 A LEU   A 1 123 ? 19.083 -2.915  13.302  0.48 19.17 ?  123 LEU   A HD22 1 
ATOM   2676 H HD22 B LEU   A 1 123 ? 19.155 -2.928  13.170  0.52 18.63 ?  123 LEU   A HD22 1 
ATOM   2677 H HD23 A LEU   A 1 123 ? 20.170 -2.206  12.386  0.48 19.17 ?  123 LEU   A HD23 1 
ATOM   2678 H HD23 B LEU   A 1 123 ? 20.200 -2.211  12.211  0.52 18.63 ?  123 LEU   A HD23 1 
ATOM   2679 N N    A ALA   A 1 124 ? 19.695 -5.716  8.476   0.48 12.09 ?  124 ALA   A N    1 
ATOM   2680 N N    B ALA   A 1 124 ? 19.646 -5.639  8.334   0.52 12.45 ?  124 ALA   A N    1 
ATOM   2681 C CA   A ALA   A 1 124 ? 19.938 -5.401  7.078   0.48 11.27 ?  124 ALA   A CA   1 
ATOM   2682 C CA   B ALA   A 1 124 ? 19.959 -5.437  6.924   0.52 12.72 ?  124 ALA   A CA   1 
ATOM   2683 C C    A ALA   A 1 124 ? 18.697 -4.870  6.381   0.48 10.93 ?  124 ALA   A C    1 
ATOM   2684 C C    B ALA   A 1 124 ? 18.724 -5.046  6.119   0.52 12.15 ?  124 ALA   A C    1 
ATOM   2685 O O    A ALA   A 1 124 ? 17.566 -5.160  6.790   0.48 11.26 ?  124 ALA   A O    1 
ATOM   2686 O O    B ALA   A 1 124 ? 17.604 -5.451  6.457   0.52 11.99 ?  124 ALA   A O    1 
ATOM   2687 C CB   A ALA   A 1 124 ? 20.426 -6.628  6.297   0.48 11.66 ?  124 ALA   A CB   1 
ATOM   2688 C CB   B ALA   A 1 124 ? 20.595 -6.699  6.326   0.52 13.67 ?  124 ALA   A CB   1 
ATOM   2689 H H    A ALA   A 1 124 ? 18.933 -6.092  8.626   0.48 14.52 ?  124 ALA   A H    1 
ATOM   2690 H H    B ALA   A 1 124 ? 18.824 -5.818  8.522   0.52 14.95 ?  124 ALA   A H    1 
ATOM   2691 H HA   A ALA   A 1 124 ? 20.626 -4.724  7.029   0.48 13.54 ?  124 ALA   A HA   1 
ATOM   2692 H HA   B ALA   A 1 124 ? 20.610 -4.725  6.871   0.52 15.27 ?  124 ALA   A HA   1 
ATOM   2693 H HB1  A ALA   A 1 124 ? 20.576 -6.380  5.368   0.48 14.00 ?  124 ALA   A HB1  1 
ATOM   2694 H HB1  B ALA   A 1 124 ? 20.798 -6.541  5.393   0.52 16.41 ?  124 ALA   A HB1  1 
ATOM   2695 H HB2  A ALA   A 1 124 ? 21.254 -6.942  6.690   0.48 14.00 ?  124 ALA   A HB2  1 
ATOM   2696 H HB2  B ALA   A 1 124 ? 21.415 -6.909  6.810   0.52 16.41 ?  124 ALA   A HB2  1 
ATOM   2697 H HB3  A ALA   A 1 124 ? 19.752 -7.326  6.343   0.48 14.00 ?  124 ALA   A HB3  1 
ATOM   2698 H HB3  B ALA   A 1 124 ? 19.972 -7.442  6.409   0.52 16.41 ?  124 ALA   A HB3  1 
ATOM   2699 N N    A PRO   A 1 125 ? 18.887 -4.100  5.314   0.48 11.07 ?  125 PRO   A N    1 
ATOM   2700 N N    B PRO   A 1 125 ? 18.904 -4.298  5.033   0.52 11.96 ?  125 PRO   A N    1 
ATOM   2701 C CA   A PRO   A 1 125 ? 17.830 -3.866  4.332   0.48 11.89 ?  125 PRO   A CA   1 
ATOM   2702 C CA   B PRO   A 1 125 ? 17.832 -4.084  4.062   0.52 11.85 ?  125 PRO   A CA   1 
ATOM   2703 C C    A PRO   A 1 125 ? 17.870 -4.974  3.286   0.48 12.24 ?  125 PRO   A C    1 
ATOM   2704 C C    B PRO   A 1 125 ? 17.910 -5.143  2.965   0.52 10.70 ?  125 PRO   A C    1 
ATOM   2705 O O    A PRO   A 1 125 ? 18.784 -5.802  3.260   0.48 11.85 ?  125 PRO   A O    1 
ATOM   2706 O O    B PRO   A 1 125 ? 18.910 -5.848  2.817   0.52 11.18 ?  125 PRO   A O    1 
ATOM   2707 C CB   A PRO   A 1 125 ? 18.286 -2.543  3.703   0.48 12.33 ?  125 PRO   A CB   1 
ATOM   2708 C CB   B PRO   A 1 125 ? 18.226 -2.729  3.471   0.52 12.88 ?  125 PRO   A CB   1 
ATOM   2709 C CG   A PRO   A 1 125 ? 19.793 -2.720  3.633   0.48 12.66 ?  125 PRO   A CG   1 
ATOM   2710 C CG   B PRO   A 1 125 ? 19.741 -2.843  3.393   0.52 12.72 ?  125 PRO   A CG   1 
ATOM   2711 C CD   A PRO   A 1 125 ? 20.151 -3.451  4.912   0.48 12.45 ?  125 PRO   A CD   1 
ATOM   2712 C CD   B PRO   A 1 125 ? 20.141 -3.589  4.649   0.52 11.68 ?  125 PRO   A CD   1 
ATOM   2713 H HA   A PRO   A 1 125 ? 16.949 -3.796  4.724   0.48 14.27 ?  125 PRO   A HA   1 
ATOM   2714 H HA   B PRO   A 1 125 ? 16.950 -4.058  4.490   0.52 14.23 ?  125 PRO   A HA   1 
ATOM   2715 H HB2  A PRO   A 1 125 ? 17.900 -2.430  2.819   0.48 14.80 ?  125 PRO   A HB2  1 
ATOM   2716 H HB2  B PRO   A 1 125 ? 17.828 -2.635  2.593   0.52 15.47 ?  125 PRO   A HB2  1 
ATOM   2717 H HB3  A PRO   A 1 125 ? 18.047 -1.802  4.286   0.48 14.80 ?  125 PRO   A HB3  1 
ATOM   2718 H HB3  B PRO   A 1 125 ? 17.951 -2.017  4.066   0.52 15.47 ?  125 PRO   A HB3  1 
ATOM   2719 H HG2  A PRO   A 1 125 ? 20.029 -3.257  2.854   0.48 15.20 ?  125 PRO   A HG2  1 
ATOM   2720 H HG2  B PRO   A 1 125 ? 19.993 -3.352  2.603   0.52 15.27 ?  125 PRO   A HG2  1 
ATOM   2721 H HG3  A PRO   A 1 125 ? 20.232 -1.856  3.595   0.48 15.20 ?  125 PRO   A HG3  1 
ATOM   2722 H HG3  B PRO   A 1 125 ? 20.135 -1.962  3.377   0.52 15.27 ?  125 PRO   A HG3  1 
ATOM   2723 H HD2  A PRO   A 1 125 ? 20.841 -4.109  4.743   0.48 14.95 ?  125 PRO   A HD2  1 
ATOM   2724 H HD2  B PRO   A 1 125 ? 20.848 -4.226  4.472   0.52 14.02 ?  125 PRO   A HD2  1 
ATOM   2725 H HD3  A PRO   A 1 125 ? 20.419 -2.816  5.593   0.48 14.95 ?  125 PRO   A HD3  1 
ATOM   2726 H HD3  B PRO   A 1 125 ? 20.394 -2.966  5.354   0.52 14.02 ?  125 PRO   A HD3  1 
ATOM   2727 N N    A LEU   A 1 126 ? 16.867 -4.960  2.407   0.48 12.72 ?  126 LEU   A N    1 
ATOM   2728 N N    B LEU   A 1 126 ? 16.851 -5.212  2.165   0.52 11.70 ?  126 LEU   A N    1 
ATOM   2729 C CA   A LEU   A 1 126 ? 16.877 -5.832  1.239   0.48 12.47 ?  126 LEU   A CA   1 
ATOM   2730 C CA   B LEU   A 1 126 ? 16.878 -6.042  0.965   0.52 12.26 ?  126 LEU   A CA   1 
ATOM   2731 C C    A LEU   A 1 126 ? 17.847 -5.282  0.200   0.48 12.60 ?  126 LEU   A C    1 
ATOM   2732 C C    B LEU   A 1 126 ? 17.780 -5.398  -0.079  0.52 12.48 ?  126 LEU   A C    1 
ATOM   2733 O O    A LEU   A 1 126 ? 17.727 -4.131  -0.227  0.48 13.60 ?  126 LEU   A O    1 
ATOM   2734 O O    B LEU   A 1 126 ? 17.474 -4.333  -0.623  0.52 12.70 ?  126 LEU   A O    1 
ATOM   2735 C CB   A LEU   A 1 126 ? 15.476 -5.945  0.648   0.48 13.70 ?  126 LEU   A CB   1 
ATOM   2736 C CB   B LEU   A 1 126 ? 15.472 -6.249  0.421   0.52 13.09 ?  126 LEU   A CB   1 
ATOM   2737 C CG   A LEU   A 1 126 ? 14.512 -6.883  1.370   0.48 14.62 ?  126 LEU   A CG   1 
ATOM   2738 C CG   B LEU   A 1 126 ? 14.599 -7.171  1.274   0.52 14.74 ?  126 LEU   A CG   1 
ATOM   2739 C CD1  A LEU   A 1 126 ? 13.123 -6.711  0.791   0.48 15.63 ?  126 LEU   A CD1  1 
ATOM   2740 C CD1  B LEU   A 1 126 ? 13.152 -7.073  0.836   0.52 16.48 ?  126 LEU   A CD1  1 
ATOM   2741 C CD2  A LEU   A 1 126 ? 14.962 -8.335  1.252   0.48 15.27 ?  126 LEU   A CD2  1 
ATOM   2742 C CD2  B LEU   A 1 126 ? 15.084 -8.616  1.207   0.52 14.91 ?  126 LEU   A CD2  1 
ATOM   2743 H H    A LEU   A 1 126 ? 16.165 -4.452  2.459   0.48 15.27 ?  126 LEU   A H    1 
ATOM   2744 H H    B LEU   A 1 126 ? 16.121 -4.778  2.286   0.52 14.05 ?  126 LEU   A H    1 
ATOM   2745 H HA   A LEU   A 1 126 ? 17.174 -6.713  1.498   0.48 14.97 ?  126 LEU   A HA   1 
ATOM   2746 H HA   B LEU   A 1 126 ? 17.250 -6.908  1.187   0.52 14.72 ?  126 LEU   A HA   1 
ATOM   2747 H HB2  A LEU   A 1 126 ? 15.068 -5.066  0.652   0.48 16.45 ?  126 LEU   A HB2  1 
ATOM   2748 H HB2  B LEU   A 1 126 ? 15.024 -5.393  0.369   0.52 15.72 ?  126 LEU   A HB2  1 
ATOM   2749 H HB3  A LEU   A 1 126 ? 15.547 -6.264  -0.263  0.48 16.45 ?  126 LEU   A HB3  1 
ATOM   2750 H HB3  B LEU   A 1 126 ? 15.535 -6.644  -0.464  0.52 15.72 ?  126 LEU   A HB3  1 
ATOM   2751 H HG   A LEU   A 1 126 ? 14.478 -6.652  2.315   0.48 17.56 ?  126 LEU   A HG   1 
ATOM   2752 H HG   B LEU   A 1 126 ? 14.650 -6.888  2.200   0.52 17.70 ?  126 LEU   A HG   1 
ATOM   2753 H HD11 A LEU   A 1 126 ? 12.514 -7.315  1.245   0.48 18.76 ?  126 LEU   A HD11 1 
ATOM   2754 H HD11 B LEU   A 1 126 ? 12.617 -7.666  1.385   0.52 19.79 ?  126 LEU   A HD11 1 
ATOM   2755 H HD12 A LEU   A 1 126 ? 12.840 -5.794  0.919   0.48 18.76 ?  126 LEU   A HD12 1 
ATOM   2756 H HD12 B LEU   A 1 126 ? 12.856 -6.157  0.950   0.52 19.79 ?  126 LEU   A HD12 1 
ATOM   2757 H HD13 A LEU   A 1 126 ? 13.152 -6.922  -0.156  0.48 18.76 ?  126 LEU   A HD13 1 
ATOM   2758 H HD13 B LEU   A 1 126 ? 13.089 -7.332  -0.095  0.52 19.79 ?  126 LEU   A HD13 1 
ATOM   2759 H HD21 A LEU   A 1 126 ? 14.266 -8.912  1.600   0.48 18.33 ?  126 LEU   A HD21 1 
ATOM   2760 H HD21 B LEU   A 1 126 ? 14.438 -9.186  1.653   0.52 17.90 ?  126 LEU   A HD21 1 
ATOM   2761 H HD22 A LEU   A 1 126 ? 15.124 -8.536  0.317   0.48 18.33 ?  126 LEU   A HD22 1 
ATOM   2762 H HD22 B LEU   A 1 126 ? 15.170 -8.875  0.278   0.52 17.90 ?  126 LEU   A HD22 1 
ATOM   2763 H HD23 A LEU   A 1 126 ? 15.779 -8.455  1.762   0.48 18.33 ?  126 LEU   A HD23 1 
ATOM   2764 H HD23 B LEU   A 1 126 ? 15.944 -8.681  1.651   0.52 17.90 ?  126 LEU   A HD23 1 
ATOM   2765 N N    A LEU   A 1 127 ? 18.815 -6.098  -0.210  0.48 12.86 ?  127 LEU   A N    1 
ATOM   2766 N N    B LEU   A 1 127 ? 18.895 -6.055  -0.370  0.52 12.08 ?  127 LEU   A N    1 
ATOM   2767 C CA   A LEU   A 1 127 ? 19.821 -5.639  -1.158  0.48 12.46 ?  127 LEU   A CA   1 
ATOM   2768 C CA   B LEU   A 1 127 ? 19.869 -5.504  -1.298  0.52 11.78 ?  127 LEU   A CA   1 
ATOM   2769 C C    A LEU   A 1 127 ? 19.200 -5.388  -2.523  0.48 11.98 ?  127 LEU   A C    1 
ATOM   2770 C C    B LEU   A 1 127 ? 19.277 -5.405  -2.700  0.52 11.66 ?  127 LEU   A C    1 
ATOM   2771 O O    A LEU   A 1 127 ? 18.322 -6.130  -2.979  0.48 12.52 ?  127 LEU   A O    1 
ATOM   2772 O O    B LEU   A 1 127 ? 18.471 -6.242  -3.128  0.52 11.90 ?  127 LEU   A O    1 
ATOM   2773 C CB   A LEU   A 1 127 ? 20.935 -6.672  -1.304  0.48 12.68 ?  127 LEU   A CB   1 
ATOM   2774 C CB   B LEU   A 1 127 ? 21.132 -6.367  -1.304  0.52 12.37 ?  127 LEU   A CB   1 
ATOM   2775 C CG   A LEU   A 1 127 ? 21.807 -6.926  -0.076  0.48 12.95 ?  127 LEU   A CG   1 
ATOM   2776 C CG   B LEU   A 1 127 ? 21.873 -6.468  0.036   0.52 13.39 ?  127 LEU   A CG   1 
ATOM   2777 C CD1  A LEU   A 1 127 ? 22.892 -7.937  -0.400  0.48 12.60 ?  127 LEU   A CD1  1 
ATOM   2778 C CD1  B LEU   A 1 127 ? 23.022 -7.459  -0.070  0.52 14.08 ?  127 LEU   A CD1  1 
ATOM   2779 C CD2  A LEU   A 1 127 ? 22.426 -5.637  0.422   0.48 13.54 ?  127 LEU   A CD2  1 
ATOM   2780 C CD2  B LEU   A 1 127 ? 22.391 -5.112  0.499   0.52 14.64 ?  127 LEU   A CD2  1 
ATOM   2781 H H    A LEU   A 1 127 ? 18.914 -6.910  0.046   0.48 15.44 ?  127 LEU   A H    1 
ATOM   2782 H H    B LEU   A 1 127 ? 19.111 -6.815  -0.031  0.52 14.50 ?  127 LEU   A H    1 
ATOM   2783 H HA   A LEU   A 1 127 ? 20.211 -4.807  -0.842  0.48 14.96 ?  127 LEU   A HA   1 
ATOM   2784 H HA   B LEU   A 1 127 ? 20.119 -4.614  -1.007  0.52 14.15 ?  127 LEU   A HA   1 
ATOM   2785 H HB2  A LEU   A 1 127 ? 20.529 -7.519  -1.550  0.48 15.23 ?  127 LEU   A HB2  1 
ATOM   2786 H HB2  B LEU   A 1 127 ? 20.891 -7.270  -1.565  0.52 14.85 ?  127 LEU   A HB2  1 
ATOM   2787 H HB3  A LEU   A 1 127 ? 21.525 -6.384  -2.019  0.48 15.23 ?  127 LEU   A HB3  1 
ATOM   2788 H HB3  B LEU   A 1 127 ? 21.756 -5.999  -1.948  0.52 14.85 ?  127 LEU   A HB3  1 
ATOM   2789 H HG   A LEU   A 1 127 ? 21.254 -7.294  0.633   0.48 15.54 ?  127 LEU   A HG   1 
ATOM   2790 H HG   B LEU   A 1 127 ? 21.261 -6.800  0.712   0.52 16.07 ?  127 LEU   A HG   1 
ATOM   2791 H HD11 A LEU   A 1 127 ? 23.365 -8.166  0.418   0.48 15.13 ?  127 LEU   A HD11 1 
ATOM   2792 H HD11 B LEU   A 1 127 ? 23.532 -7.442  0.757   0.52 16.91 ?  127 LEU   A HD11 1 
ATOM   2793 H HD12 A LEU   A 1 127 ? 22.484 -8.733  -0.778  0.48 15.13 ?  127 LEU   A HD12 1 
ATOM   2794 H HD12 B LEU   A 1 127 ? 22.662 -8.348  -0.215  0.52 16.91 ?  127 LEU   A HD12 1 
ATOM   2795 H HD13 A LEU   A 1 127 ? 23.507 -7.546  -1.039  0.48 15.13 ?  127 LEU   A HD13 1 
ATOM   2796 H HD13 B LEU   A 1 127 ? 23.591 -7.205  -0.812  0.52 16.91 ?  127 LEU   A HD13 1 
ATOM   2797 H HD21 A LEU   A 1 127 ? 23.102 -5.848  1.085   0.48 16.25 ?  127 LEU   A HD21 1 
ATOM   2798 H HD21 B LEU   A 1 127 ? 22.930 -5.234  1.298   0.52 17.57 ?  127 LEU   A HD21 1 
ATOM   2799 H HD22 A LEU   A 1 127 ? 22.835 -5.174  -0.329  0.48 16.25 ?  127 LEU   A HD22 1 
ATOM   2800 H HD22 B LEU   A 1 127 ? 22.933 -4.724  -0.206  0.52 17.57 ?  127 LEU   A HD22 1 
ATOM   2801 H HD23 A LEU   A 1 127 ? 21.736 -5.083  0.815   0.48 16.25 ?  127 LEU   A HD23 1 
ATOM   2802 H HD23 B LEU   A 1 127 ? 21.638 -4.535  0.694   0.52 17.57 ?  127 LEU   A HD23 1 
ATOM   2803 N N    A SER   A 1 128 ? 19.671 -4.331  -3.172  0.48 11.83 ?  128 SER   A N    1 
ATOM   2804 N N    B SER   A 1 128 ? 19.677 -4.355  -3.405  0.52 11.74 ?  128 SER   A N    1 
ATOM   2805 C CA   A SER   A 1 128 ? 19.272 -3.924  -4.512  0.48 11.67 ?  128 SER   A CA   1 
ATOM   2806 C CA   B SER   A 1 128 ? 19.300 -4.050  -4.775  0.52 11.97 ?  128 SER   A CA   1 
ATOM   2807 C C    A SER   A 1 128 ? 17.811 -3.500  -4.604  0.48 12.03 ?  128 SER   A C    1 
ATOM   2808 C C    B SER   A 1 128 ? 17.851 -3.592  -4.923  0.52 12.06 ?  128 SER   A C    1 
ATOM   2809 O O    A SER   A 1 128 ? 17.325 -3.238  -5.702  0.48 12.84 ?  128 SER   A O    1 
ATOM   2810 O O    B SER   A 1 128 ? 17.440 -3.281  -6.043  0.52 12.90 ?  128 SER   A O    1 
ATOM   2811 C CB   A SER   A 1 128 ? 19.633 -4.960  -5.587  0.48 11.77 ?  128 SER   A CB   1 
ATOM   2812 C CB   B SER   A 1 128 ? 19.633 -5.178  -5.766  0.52 12.83 ?  128 SER   A CB   1 
ATOM   2813 O OG   A SER   A 1 128 ? 21.041 -5.158  -5.628  0.48 12.06 ?  128 SER   A OG   1 
ATOM   2814 O OG   B SER   A 1 128 ? 21.036 -5.382  -5.850  0.52 13.65 ?  128 SER   A OG   1 
ATOM   2815 H H    A SER   A 1 128 ? 20.256 -3.794  -2.837  0.48 14.21 ?  128 SER   A H    1 
ATOM   2816 H H    B SER   A 1 128 ? 20.217 -3.769  -3.072  0.52 14.09 ?  128 SER   A H    1 
ATOM   2817 H HA   A SER   A 1 128 ? 19.790 -3.140  -4.728  0.48 14.02 ?  128 SER   A HA   1 
ATOM   2818 H HA   B SER   A 1 128 ? 19.840 -3.300  -5.036  0.52 14.37 ?  128 SER   A HA   1 
ATOM   2819 H HB2  A SER   A 1 128 ? 19.200 -5.800  -5.380  0.48 14.13 ?  128 SER   A HB2  1 
ATOM   2820 H HB2  B SER   A 1 128 ? 19.210 -5.998  -5.474  0.52 15.41 ?  128 SER   A HB2  1 
ATOM   2821 H HB3  A SER   A 1 128 ? 19.329 -4.635  -6.454  0.48 14.13 ?  128 SER   A HB3  1 
ATOM   2822 H HB3  B SER   A 1 128 ? 19.310 -4.923  -6.642  0.52 15.41 ?  128 SER   A HB3  1 
ATOM   2823 H HG   A SER   A 1 128 ? 21.427 -4.434  -5.820  0.48 14.48 ?  128 SER   A HG   1 
ATOM   2824 H HG   B SER   A 1 128 ? 21.418 -4.669  -6.077  0.52 16.39 ?  128 SER   A HG   1 
ATOM   2825 N N    A ALA   A 1 129 ? 17.109 -3.404  -3.477  0.48 12.14 ?  129 ALA   A N    1 
ATOM   2826 N N    B ALA   A 1 129 ? 17.074 -3.531  -3.838  0.52 12.27 ?  129 ALA   A N    1 
ATOM   2827 C CA   A ALA   A 1 129 ? 15.744 -2.900  -3.450  0.48 12.75 ?  129 ALA   A CA   1 
ATOM   2828 C CA   B ALA   A 1 129 ? 15.694 -3.055  -3.899  0.52 12.42 ?  129 ALA   A CA   1 
ATOM   2829 C C    A ALA   A 1 129 ? 15.752 -1.371  -3.463  0.48 12.90 ?  129 ALA   A C    1 
ATOM   2830 C C    B ALA   A 1 129 ? 15.668 -1.526  -3.810  0.52 12.73 ?  129 ALA   A C    1 
ATOM   2831 O O    A ALA   A 1 129 ? 16.806 -0.729  -3.473  0.48 12.01 ?  129 ALA   A O    1 
ATOM   2832 O O    B ALA   A 1 129 ? 16.694 -0.852  -3.961  0.52 12.44 ?  129 ALA   A O    1 
ATOM   2833 C CB   A ALA   A 1 129 ? 15.004 -3.429  -2.223  0.48 13.31 ?  129 ALA   A CB   1 
ATOM   2834 C CB   B ALA   A 1 129 ? 14.840 -3.734  -2.824  0.52 12.41 ?  129 ALA   A CB   1 
ATOM   2835 H H    A ALA   A 1 129 ? 17.405 -3.626  -2.708  0.48 14.58 ?  129 ALA   A H    1 
ATOM   2836 H H    B ALA   A 1 129 ? 17.320 -3.770  -3.045  0.52 14.73 ?  129 ALA   A H    1 
ATOM   2837 H HA   A ALA   A 1 129 ? 15.274 -3.209  -4.238  0.48 15.30 ?  129 ALA   A HA   1 
ATOM   2838 H HA   B ALA   A 1 129 ? 15.319 -3.293  -4.755  0.52 14.92 ?  129 ALA   A HA   1 
ATOM   2839 H HB1  A ALA   A 1 129 ? 14.098 -3.083  -2.225  0.48 15.97 ?  129 ALA   A HB1  1 
ATOM   2840 H HB1  B ALA   A 1 129 ? 13.923 -3.426  -2.900  0.52 14.89 ?  129 ALA   A HB1  1 
ATOM   2841 H HB2  A ALA   A 1 129 ? 14.991 -4.397  -2.261  0.48 15.97 ?  129 ALA   A HB2  1 
ATOM   2842 H HB2  B ALA   A 1 129 ? 14.872 -4.698  -2.954  0.52 14.89 ?  129 ALA   A HB2  1 
ATOM   2843 H HB3  A ALA   A 1 129 ? 15.469 -3.135  -1.423  0.48 15.97 ?  129 ALA   A HB3  1 
ATOM   2844 H HB3  B ALA   A 1 129 ? 15.191 -3.513  -1.946  0.52 14.89 ?  129 ALA   A HB3  1 
ATOM   2845 N N    A GLY   A 1 130 ? 14.562 -0.773  -3.455  0.48 14.19 ?  130 GLY   A N    1 
ATOM   2846 N N    B GLY   A 1 130 ? 14.482 -0.958  -3.574  0.52 13.75 ?  130 GLY   A N    1 
ATOM   2847 C CA   A GLY   A 1 130 ? 14.485 0.680   -3.482  0.48 14.72 ?  130 GLY   A CA   1 
ATOM   2848 C CA   B GLY   A 1 130 ? 14.380 0.488   -3.470  0.52 13.76 ?  130 GLY   A CA   1 
ATOM   2849 C C    A GLY   A 1 130 ? 15.133 1.257   -4.725  0.48 14.92 ?  130 GLY   A C    1 
ATOM   2850 C C    B GLY   A 1 130 ? 14.890 1.150   -4.734  0.52 13.12 ?  130 GLY   A C    1 
ATOM   2851 O O    A GLY   A 1 130 ? 14.915 0.786   -5.846  0.48 15.64 ?  130 GLY   A O    1 
ATOM   2852 O O    B GLY   A 1 130 ? 14.582 0.727   -5.853  0.52 13.18 ?  130 GLY   A O    1 
ATOM   2853 H H    A GLY   A 1 130 ? 13.802 -1.177  -3.425  0.48 17.03 ?  130 GLY   A H    1 
ATOM   2854 H H    B GLY   A 1 130 ? 13.735 -1.383  -3.481  0.52 16.51 ?  130 GLY   A H    1 
ATOM   2855 H HA2  A GLY   A 1 130 ? 13.555 0.956   -3.462  0.48 17.67 ?  130 GLY   A HA2  1 
ATOM   2856 H HA2  B GLY   A 1 130 ? 13.451 0.738   -3.321  0.52 16.52 ?  130 GLY   A HA2  1 
ATOM   2857 H HA3  A GLY   A 1 130 ? 14.933 1.041   -2.703  0.48 17.67 ?  130 GLY   A HA3  1 
ATOM   2858 H HA3  B GLY   A 1 130 ? 14.905 0.800   -2.715  0.52 16.52 ?  130 GLY   A HA3  1 
ATOM   2859 N N    A ILE   A 1 131 ? 15.935 2.309   -4.528  0.48 14.66 ?  131 ILE   A N    1 
ATOM   2860 N N    B ILE   A 1 131 ? 15.686 2.210   -4.559  0.52 13.46 ?  131 ILE   A N    1 
ATOM   2861 C CA   A ILE   A 1 131 ? 16.526 3.029   -5.654  0.48 14.54 ?  131 ILE   A CA   1 
ATOM   2862 C CA   B ILE   A 1 131 ? 16.189 2.979   -5.696  0.52 13.24 ?  131 ILE   A CA   1 
ATOM   2863 C C    A ILE   A 1 131 ? 17.511 2.199   -6.463  0.48 14.39 ?  131 ILE   A C    1 
ATOM   2864 C C    B ILE   A 1 131 ? 17.317 2.259   -6.437  0.52 13.80 ?  131 ILE   A C    1 
ATOM   2865 O O    A ILE   A 1 131 ? 17.886 2.621   -7.564  0.48 15.08 ?  131 ILE   A O    1 
ATOM   2866 O O    B ILE   A 1 131 ? 17.865 2.796   -7.409  0.52 14.54 ?  131 ILE   A O    1 
ATOM   2867 C CB   A ILE   A 1 131 ? 17.153 4.377   -5.235  0.48 15.16 ?  131 ILE   A CB   1 
ATOM   2868 C CB   B ILE   A 1 131 ? 16.577 4.425   -5.311  0.52 14.05 ?  131 ILE   A CB   1 
ATOM   2869 C CG1  A ILE   A 1 131 ? 18.445 4.180   -4.436  0.48 17.02 ?  131 ILE   A CG1  1 
ATOM   2870 C CG1  B ILE   A 1 131 ? 17.794 4.477   -4.381  0.52 14.70 ?  131 ILE   A CG1  1 
ATOM   2871 C CG2  A ILE   A 1 131 ? 16.159 5.181   -4.426  0.48 15.32 ?  131 ILE   A CG2  1 
ATOM   2872 C CG2  B ILE   A 1 131 ? 15.388 5.148   -4.687  0.52 13.52 ?  131 ILE   A CG2  1 
ATOM   2873 C CD1  A ILE   A 1 131 ? 19.071 5.494   -3.973  0.48 18.22 ?  131 ILE   A CD1  1 
ATOM   2874 C CD1  B ILE   A 1 131 ? 18.300 5.890   -4.126  0.52 15.39 ?  131 ILE   A CD1  1 
ATOM   2875 H H    A ILE   A 1 131 ? 16.136 2.628   -3.754  0.48 17.60 ?  131 ILE   A H    1 
ATOM   2876 H H    B ILE   A 1 131 ? 15.926 2.508   -3.787  0.52 16.16 ?  131 ILE   A H    1 
ATOM   2877 H HA   A ILE   A 1 131 ? 15.808 3.243   -6.263  0.48 17.46 ?  131 ILE   A HA   1 
ATOM   2878 H HA   B ILE   A 1 131 ? 15.454 3.061   -6.319  0.52 15.90 ?  131 ILE   A HA   1 
ATOM   2879 H HB   A ILE   A 1 131 ? 17.360 4.879   -6.041  0.48 18.20 ?  131 ILE   A HB   1 
ATOM   2880 H HB   B ILE   A 1 131 ? 16.807 4.890   -6.125  0.52 16.87 ?  131 ILE   A HB   1 
ATOM   2881 H HG12 A ILE   A 1 131 ? 18.249 3.647   -3.652  0.48 20.43 ?  131 ILE   A HG12 1 
ATOM   2882 H HG12 B ILE   A 1 131 ? 17.556 4.085   -3.525  0.52 17.65 ?  131 ILE   A HG12 1 
ATOM   2883 H HG13 A ILE   A 1 131 ? 19.096 3.727   -4.993  0.48 20.43 ?  131 ILE   A HG13 1 
ATOM   2884 H HG13 B ILE   A 1 131 ? 18.521 3.969   -4.781  0.52 17.65 ?  131 ILE   A HG13 1 
ATOM   2885 H HG21 A ILE   A 1 131 ? 16.458 6.102   -4.383  0.48 18.40 ?  131 ILE   A HG21 1 
ATOM   2886 H HG21 B ILE   A 1 131 ? 15.615 6.082   -4.553  0.52 16.24 ?  131 ILE   A HG21 1 
ATOM   2887 H HG22 A ILE   A 1 131 ? 15.292 5.133   -4.855  0.48 18.40 ?  131 ILE   A HG22 1 
ATOM   2888 H HG22 B ILE   A 1 131 ? 14.625 5.083   -5.283  0.52 16.24 ?  131 ILE   A HG22 1 
ATOM   2889 H HG23 A ILE   A 1 131 ? 16.108 4.805   -3.533  0.48 18.40 ?  131 ILE   A HG23 1 
ATOM   2890 H HG23 B ILE   A 1 131 ? 15.172 4.736   -3.835  0.52 16.24 ?  131 ILE   A HG23 1 
ATOM   2891 H HD11 A ILE   A 1 131 ? 19.963 5.316   -3.635  0.48 21.87 ?  131 ILE   A HD11 1 
ATOM   2892 H HD11 B ILE   A 1 131 ? 19.152 5.842   -3.672  0.52 18.48 ?  131 ILE   A HD11 1 
ATOM   2893 H HD12 A ILE   A 1 131 ? 19.120 6.106   -4.725  0.48 21.87 ?  131 ILE   A HD12 1 
ATOM   2894 H HD12 B ILE   A 1 131 ? 18.400 6.341   -4.979  0.52 18.48 ?  131 ILE   A HD12 1 
ATOM   2895 H HD13 A ILE   A 1 131 ? 18.524 5.879   -3.270  0.48 21.87 ?  131 ILE   A HD13 1 
ATOM   2896 H HD13 B ILE   A 1 131 ? 17.652 6.358   -3.577  0.52 18.48 ?  131 ILE   A HD13 1 
ATOM   2897 N N    A PHE   A 1 132 ? 17.946 1.038   -5.963  0.48 13.49 ?  132 PHE   A N    1 
ATOM   2898 N N    B PHE   A 1 132 ? 17.676 1.043   -6.000  0.52 13.68 ?  132 PHE   A N    1 
ATOM   2899 C CA   A PHE   A 1 132 ? 18.776 0.162   -6.784  0.48 13.64 ?  132 PHE   A CA   1 
ATOM   2900 C CA   B PHE   A 1 132 ? 18.594 0.217   -6.782  0.52 14.03 ?  132 PHE   A CA   1 
ATOM   2901 C C    A PHE   A 1 132 ? 17.965 -0.603  -7.830  0.48 14.38 ?  132 PHE   A C    1 
ATOM   2902 C C    B PHE   A 1 132 ? 17.901 -0.522  -7.926  0.52 14.87 ?  132 PHE   A C    1 
ATOM   2903 O O    A PHE   A 1 132 ? 18.556 -1.285  -8.675  0.48 14.87 ?  132 PHE   A O    1 
ATOM   2904 O O    B PHE   A 1 132 ? 18.588 -1.055  -8.805  0.52 15.63 ?  132 PHE   A O    1 
ATOM   2905 C CB   A PHE   A 1 132 ? 19.587 -0.813  -5.919  0.48 12.47 ?  132 PHE   A CB   1 
ATOM   2906 C CB   B PHE   A 1 132 ? 19.353 -0.777  -5.890  0.52 13.88 ?  132 PHE   A CB   1 
ATOM   2907 C CG   A PHE   A 1 132 ? 20.795 -0.201  -5.238  0.48 12.03 ?  132 PHE   A CG   1 
ATOM   2908 C CG   B PHE   A 1 132 ? 20.575 -0.208  -5.203  0.52 13.90 ?  132 PHE   A CG   1 
ATOM   2909 C CD1  A PHE   A 1 132 ? 20.660 0.848   -4.343  0.48 13.08 ?  132 PHE   A CD1  1 
ATOM   2910 C CD1  B PHE   A 1 132 ? 20.457 0.789   -4.252  0.52 14.50 ?  132 PHE   A CD1  1 
ATOM   2911 C CD2  A PHE   A 1 132 ? 22.064 -0.721  -5.462  0.48 12.41 ?  132 PHE   A CD2  1 
ATOM   2912 C CD2  B PHE   A 1 132 ? 21.837 -0.720  -5.475  0.52 14.01 ?  132 PHE   A CD2  1 
ATOM   2913 C CE1  A PHE   A 1 132 ? 21.775 1.384   -3.703  0.48 13.53 ?  132 PHE   A CE1  1 
ATOM   2914 C CE1  B PHE   A 1 132 ? 21.577 1.288   -3.604  0.52 14.79 ?  132 PHE   A CE1  1 
ATOM   2915 C CE2  A PHE   A 1 132 ? 23.176 -0.196  -4.825  0.48 12.89 ?  132 PHE   A CE2  1 
ATOM   2916 C CE2  B PHE   A 1 132 ? 22.960 -0.229  -4.830  0.52 14.15 ?  132 PHE   A CE2  1 
ATOM   2917 C CZ   A PHE   A 1 132 ? 23.030 0.862   -3.945  0.48 13.10 ?  132 PHE   A CZ   1 
ATOM   2918 C CZ   B PHE   A 1 132 ? 22.826 0.782   -3.891  0.52 14.10 ?  132 PHE   A CZ   1 
ATOM   2919 H H    A PHE   A 1 132 ? 17.776 0.743   -5.166  0.48 16.19 ?  132 PHE   A H    1 
ATOM   2920 H H    B PHE   A 1 132 ? 17.408 0.686   -5.257  0.52 16.43 ?  132 PHE   A H    1 
ATOM   2921 H HA   A PHE   A 1 132 ? 19.415 0.722   -7.249  0.48 16.38 ?  132 PHE   A HA   1 
ATOM   2922 H HA   B PHE   A 1 132 ? 19.249 0.799   -7.183  0.52 16.85 ?  132 PHE   A HA   1 
ATOM   2923 H HB2  A PHE   A 1 132 ? 19.009 -1.159  -5.225  0.48 14.97 ?  132 PHE   A HB2  1 
ATOM   2924 H HB2  B PHE   A 1 132 ? 18.760 -1.092  -5.193  0.52 16.67 ?  132 PHE   A HB2  1 
ATOM   2925 H HB3  A PHE   A 1 132 ? 19.900 -1.539  -6.483  0.48 14.97 ?  132 PHE   A HB3  1 
ATOM   2926 H HB3  B PHE   A 1 132 ? 19.649 -1.520  -6.434  0.52 16.67 ?  132 PHE   A HB3  1 
ATOM   2927 H HD1  A PHE   A 1 132 ? 19.820 1.202   -4.171  0.48 15.71 ?  132 PHE   A HD1  1 
ATOM   2928 H HD1  B PHE   A 1 132 ? 19.619 1.135   -4.049  0.52 17.40 ?  132 PHE   A HD1  1 
ATOM   2929 H HD2  A PHE   A 1 132 ? 22.171 -1.435  -6.053  0.48 14.90 ?  132 PHE   A HD2  1 
ATOM   2930 H HD2  B PHE   A 1 132 ? 21.933 -1.400  -6.104  0.52 16.83 ?  132 PHE   A HD2  1 
ATOM   2931 H HE1  A PHE   A 1 132 ? 21.674 2.093   -3.109  0.48 16.25 ?  132 PHE   A HE1  1 
ATOM   2932 H HE1  B PHE   A 1 132 ? 21.484 1.964   -2.973  0.52 17.76 ?  132 PHE   A HE1  1 
ATOM   2933 H HE2  A PHE   A 1 132 ? 24.022 -0.550  -4.996  0.48 15.47 ?  132 PHE   A HE2  1 
ATOM   2934 H HE2  B PHE   A 1 132 ? 23.803 -0.575  -5.032  0.52 16.99 ?  132 PHE   A HE2  1 
ATOM   2935 H HZ   A PHE   A 1 132 ? 23.775 1.223   -3.519  0.48 15.73 ?  132 PHE   A HZ   1 
ATOM   2936 H HZ   B PHE   A 1 132 ? 23.576 1.120   -3.457  0.52 16.93 ?  132 PHE   A HZ   1 
ATOM   2937 N N    A GLY   A 1 133 ? 16.634 -0.526  -7.786  0.48 14.15 ?  133 GLY   A N    1 
ATOM   2938 N N    B GLY   A 1 133 ? 16.571 -0.572  -7.947  0.52 14.54 ?  133 GLY   A N    1 
ATOM   2939 C CA   A GLY   A 1 133 ? 15.799 -0.871  -8.923  0.48 14.31 ?  133 GLY   A CA   1 
ATOM   2940 C CA   B GLY   A 1 133 ? 15.852 -0.944  -9.149  0.52 14.24 ?  133 GLY   A CA   1 
ATOM   2941 C C    A GLY   A 1 133 ? 15.406 -2.327  -9.076  0.48 14.26 ?  133 GLY   A C    1 
ATOM   2942 C C    B GLY   A 1 133 ? 15.563 -2.415  -9.374  0.52 14.19 ?  133 GLY   A C    1 
ATOM   2943 O O    A GLY   A 1 133 ? 14.635 -2.637  -9.992  0.48 14.51 ?  133 GLY   A O    1 
ATOM   2944 O O    B GLY   A 1 133 ? 14.992 -2.750  -10.420 0.52 14.55 ?  133 GLY   A O    1 
ATOM   2945 H H    A GLY   A 1 133 ? 16.184 -0.276  -7.093  0.48 16.99 ?  133 GLY   A H    1 
ATOM   2946 H H    B GLY   A 1 133 ? 16.059 -0.373  -7.275  0.52 17.46 ?  133 GLY   A H    1 
ATOM   2947 H HA2  A GLY   A 1 133 ? 14.967 -0.373  -8.861  0.48 17.19 ?  133 GLY   A HA2  1 
ATOM   2948 H HA2  B GLY   A 1 133 ? 15.011 -0.464  -9.158  0.52 17.10 ?  133 GLY   A HA2  1 
ATOM   2949 H HA3  A GLY   A 1 133 ? 16.247 -0.583  -9.738  0.48 17.19 ?  133 GLY   A HA3  1 
ATOM   2950 H HA3  B GLY   A 1 133 ? 16.370 -0.650  -9.912  0.52 17.10 ?  133 GLY   A HA3  1 
ATOM   2951 N N    A ALA   A 1 134 ? 15.887 -3.225  -8.221  0.48 14.14 ?  134 ALA   A N    1 
ATOM   2952 N N    B ALA   A 1 134 ? 15.943 -3.305  -8.458  0.52 13.96 ?  134 ALA   A N    1 
ATOM   2953 C CA   A ALA   A 1 134 ? 15.524 -4.628  -8.358  0.48 14.60 ?  134 ALA   A CA   1 
ATOM   2954 C CA   B ALA   A 1 134 ? 15.607 -4.712  -8.620  0.52 14.43 ?  134 ALA   A CA   1 
ATOM   2955 C C    A ALA   A 1 134 ? 14.184 -4.900  -7.686  0.48 15.05 ?  134 ALA   A C    1 
ATOM   2956 C C    B ALA   A 1 134 ? 14.250 -5.016  -7.989  0.52 14.44 ?  134 ALA   A C    1 
ATOM   2957 O O    A ALA   A 1 134 ? 13.725 -4.148  -6.822  0.48 15.98 ?  134 ALA   A O    1 
ATOM   2958 O O    B ALA   A 1 134 ? 13.678 -4.208  -7.255  0.52 15.10 ?  134 ALA   A O    1 
ATOM   2959 C CB   A ALA   A 1 134 ? 16.579 -5.534  -7.730  0.48 15.35 ?  134 ALA   A CB   1 
ATOM   2960 C CB   B ALA   A 1 134 ? 16.698 -5.606  -8.029  0.52 15.74 ?  134 ALA   A CB   1 
ATOM   2961 H H    A ALA   A 1 134 ? 16.406 -3.044  -7.562  0.48 16.98 ?  134 ALA   A H    1 
ATOM   2962 H H    B ALA   A 1 134 ? 16.403 -3.120  -7.747  0.52 16.76 ?  134 ALA   A H    1 
ATOM   2963 H HA   A ALA   A 1 134 ? 15.454 -4.847  -9.302  0.48 17.53 ?  134 ALA   A HA   1 
ATOM   2964 H HA   B ALA   A 1 134 ? 15.543 -4.911  -9.563  0.52 17.32 ?  134 ALA   A HA   1 
ATOM   2965 H HB1  A ALA   A 1 134 ? 16.313 -6.457  -7.860  0.48 18.43 ?  134 ALA   A HB1  1 
ATOM   2966 H HB1  B ALA   A 1 134 ? 16.458 -6.534  -8.175  0.52 18.89 ?  134 ALA   A HB1  1 
ATOM   2967 H HB2  A ALA   A 1 134 ? 17.430 -5.367  -8.160  0.48 18.43 ?  134 ALA   A HB2  1 
ATOM   2968 H HB2  B ALA   A 1 134 ? 17.541 -5.410  -8.471  0.52 18.89 ?  134 ALA   A HB2  1 
ATOM   2969 H HB3  A ALA   A 1 134 ? 16.638 -5.335  -6.784  0.48 18.43 ?  134 ALA   A HB3  1 
ATOM   2970 H HB3  B ALA   A 1 134 ? 16.776 -5.429  -7.079  0.52 18.89 ?  134 ALA   A HB3  1 
ATOM   2971 N N    A ASP   A 1 135 ? 13.564 -6.004  -8.092  0.48 15.30 ?  135 ASP   A N    1 
ATOM   2972 N N    B ASP   A 1 135 ? 13.730 -6.201  -8.301  0.52 15.16 ?  135 ASP   A N    1 
ATOM   2973 C CA   A ASP   A 1 135 ? 12.305 -6.447  -7.508  0.48 15.72 ?  135 ASP   A CA   1 
ATOM   2974 C CA   B ASP   A 1 135 ? 12.464 -6.657  -7.735  0.52 16.06 ?  135 ASP   A CA   1 
ATOM   2975 C C    A ASP   A 1 135 ? 12.562 -6.885  -6.072  0.48 15.05 ?  135 ASP   A C    1 
ATOM   2976 C C    B ASP   A 1 135 ? 12.686 -7.093  -6.293  0.52 15.07 ?  135 ASP   A C    1 
ATOM   2977 O O    A ASP   A 1 135 ? 13.304 -7.852  -5.856  0.48 15.06 ?  135 ASP   A O    1 
ATOM   2978 O O    B ASP   A 1 135 ? 13.475 -8.014  -6.053  0.52 15.27 ?  135 ASP   A O    1 
ATOM   2979 C CB   A ASP   A 1 135 ? 11.780 -7.621  -8.332  0.48 17.49 ?  135 ASP   A CB   1 
ATOM   2980 C CB   B ASP   A 1 135 ? 11.936 -7.827  -8.558  0.52 18.37 ?  135 ASP   A CB   1 
ATOM   2981 C CG   A ASP   A 1 135 ? 10.424 -8.137  -7.844  0.48 19.94 ?  135 ASP   A CG   1 
ATOM   2982 C CG   B ASP   A 1 135 ? 10.716 -8.503  -7.937  0.52 20.99 ?  135 ASP   A CG   1 
ATOM   2983 O OD1  A ASP   A 1 135 ? 9.966  -7.712  -6.760  0.48 20.50 ?  135 ASP   A OD1  1 
ATOM   2984 O OD1  B ASP   A 1 135 ? 10.038 -7.894  -7.084  0.52 21.78 ?  135 ASP   A OD1  1 
ATOM   2985 O OD2  A ASP   A 1 135 ? 9.803  -8.950  -8.566  0.48 21.64 -1 135 ASP   A OD2  1 
ATOM   2986 O OD2  B ASP   A 1 135 ? 10.441 -9.664  -8.309  0.52 23.28 -1 135 ASP   A OD2  1 
ATOM   2987 H H    A ASP   A 1 135 ? 13.859 -6.528  -8.705  0.48 18.37 ?  135 ASP   A H    1 
ATOM   2988 H H    B ASP   A 1 135 ? 14.093 -6.765  -8.844  0.52 18.20 ?  135 ASP   A H    1 
ATOM   2989 H HA   A ASP   A 1 135 ? 11.651 -5.729  -7.534  0.48 18.88 ?  135 ASP   A HA   1 
ATOM   2990 H HA   B ASP   A 1 135 ? 11.824 -5.937  -7.762  0.52 19.28 ?  135 ASP   A HA   1 
ATOM   2991 H HB2  A ASP   A 1 135 ? 11.653 -7.330  -9.245  0.48 21.00 ?  135 ASP   A HB2  1 
ATOM   2992 H HB2  B ASP   A 1 135 ? 11.704 -7.501  -9.441  0.52 22.06 ?  135 ASP   A HB2  1 
ATOM   2993 H HB3  A ASP   A 1 135 ? 12.444 -8.336  -8.304  0.48 21.00 ?  135 ASP   A HB3  1 
ATOM   2994 H HB3  B ASP   A 1 135 ? 12.618 -8.507  -8.618  0.52 22.06 ?  135 ASP   A HB3  1 
ATOM   2995 N N    A PRO   A 1 136 ? 11.995 -6.212  -5.067  0.48 14.79 ?  136 PRO   A N    1 
ATOM   2996 N N    B PRO   A 1 136 ? 12.029 -6.468  -5.311  0.52 15.03 ?  136 PRO   A N    1 
ATOM   2997 C CA   A PRO   A 1 136 ? 12.255 -6.618  -3.675  0.48 15.07 ?  136 PRO   A CA   1 
ATOM   2998 C CA   B PRO   A 1 136 ? 12.245 -6.878  -3.912  0.52 15.20 ?  136 PRO   A CA   1 
ATOM   2999 C C    A PRO   A 1 136 ? 11.823 -8.039  -3.357  0.48 14.42 ?  136 PRO   A C    1 
ATOM   3000 C C    B PRO   A 1 136 ? 11.819 -8.302  -3.612  0.52 14.57 ?  136 PRO   A C    1 
ATOM   3001 O O    A PRO   A 1 136 ? 12.395 -8.661  -2.454  0.48 12.93 ?  136 PRO   A O    1 
ATOM   3002 O O    B PRO   A 1 136 ? 12.437 -8.944  -2.757  0.52 14.44 ?  136 PRO   A O    1 
ATOM   3003 C CB   A PRO   A 1 136 ? 11.479 -5.578  -2.853  0.48 15.85 ?  136 PRO   A CB   1 
ATOM   3004 C CB   B PRO   A 1 136 ? 11.434 -5.850  -3.109  0.52 15.96 ?  136 PRO   A CB   1 
ATOM   3005 C CG   A PRO   A 1 136 ? 10.451 -5.041  -3.795  0.48 17.10 ?  136 PRO   A CG   1 
ATOM   3006 C CG   B PRO   A 1 136 ? 10.408 -5.343  -4.076  0.52 16.93 ?  136 PRO   A CG   1 
ATOM   3007 C CD   A PRO   A 1 136 ? 11.092 -5.052  -5.141  0.48 15.86 ?  136 PRO   A CD   1 
ATOM   3008 C CD   B PRO   A 1 136 ? 11.070 -5.357  -5.418  0.52 16.28 ?  136 PRO   A CD   1 
ATOM   3009 H HA   A PRO   A 1 136 ? 13.199 -6.527  -3.469  0.48 18.10 ?  136 PRO   A HA   1 
ATOM   3010 H HA   B PRO   A 1 136 ? 13.181 -6.789  -3.672  0.52 18.25 ?  136 PRO   A HA   1 
ATOM   3011 H HB2  A PRO   A 1 136 ? 11.054 -6.002  -2.091  0.48 19.03 ?  136 PRO   A HB2  1 
ATOM   3012 H HB2  B PRO   A 1 136 ? 11.008 -6.282  -2.346  0.52 19.16 ?  136 PRO   A HB2  1 
ATOM   3013 H HB3  A PRO   A 1 136 ? 12.077 -4.869  -2.562  0.48 19.03 ?  136 PRO   A HB3  1 
ATOM   3014 H HB3  B PRO   A 1 136 ? 12.018 -5.134  -2.809  0.52 19.16 ?  136 PRO   A HB3  1 
ATOM   3015 H HG2  A PRO   A 1 136 ? 9.671  -5.618  -3.788  0.48 20.53 ?  136 PRO   A HG2  1 
ATOM   3016 H HG2  B PRO   A 1 136 ? 9.636  -5.927  -4.068  0.52 20.32 ?  136 PRO   A HG2  1 
ATOM   3017 H HG3  A PRO   A 1 136 ? 10.213 -4.137  -3.543  0.48 20.53 ?  136 PRO   A HG3  1 
ATOM   3018 H HG3  B PRO   A 1 136 ? 10.154 -4.437  -3.834  0.52 20.32 ?  136 PRO   A HG3  1 
ATOM   3019 H HD2  A PRO   A 1 136 ? 10.422 -5.194  -5.831  0.48 19.04 ?  136 PRO   A HD2  1 
ATOM   3020 H HD2  B PRO   A 1 136 ? 10.420 -5.544  -6.112  0.52 19.55 ?  136 PRO   A HD2  1 
ATOM   3021 H HD3  A PRO   A 1 136 ? 11.594 -4.237  -5.292  0.48 19.04 ?  136 PRO   A HD3  1 
ATOM   3022 H HD3  B PRO   A 1 136 ? 11.539 -4.524  -5.580  0.52 19.55 ?  136 PRO   A HD3  1 
ATOM   3023 N N    A ILE   A 1 137 ? 10.815 -8.566  -4.052  0.48 14.82 ?  137 ILE   A N    1 
ATOM   3024 N N    B ILE   A 1 137 ? 10.772 -8.815  -4.262  0.52 14.67 ?  137 ILE   A N    1 
ATOM   3025 C CA   A ILE   A 1 137 ? 10.417 -9.957  -3.846  0.48 15.18 ?  137 ILE   A CA   1 
ATOM   3026 C CA   B ILE   A 1 137 ? 10.402 -10.214 -4.066  0.52 15.17 ?  137 ILE   A CA   1 
ATOM   3027 C C    A ILE   A 1 137 ? 11.555 -10.892 -4.238  0.48 14.50 ?  137 ILE   A C    1 
ATOM   3028 C C    B ILE   A 1 137 ? 11.567 -11.111 -4.450  0.52 15.09 ?  137 ILE   A C    1 
ATOM   3029 O O    A ILE   A 1 137 ? 11.864 -11.857 -3.529  0.48 14.32 ?  137 ILE   A O    1 
ATOM   3030 O O    B ILE   A 1 137 ? 11.864 -12.103 -3.774  0.52 15.47 ?  137 ILE   A O    1 
ATOM   3031 C CB   A ILE   A 1 137 ? 9.127  -10.259 -4.629  0.48 16.28 ?  137 ILE   A CB   1 
ATOM   3032 C CB   B ILE   A 1 137 ? 9.124  -10.546 -4.861  0.52 16.54 ?  137 ILE   A CB   1 
ATOM   3033 C CG1  A ILE   A 1 137 ? 7.967  -9.404  -4.102  0.48 17.81 ?  137 ILE   A CG1  1 
ATOM   3034 C CG1  B ILE   A 1 137 ? 7.950  -9.694  -4.366  0.52 18.16 ?  137 ILE   A CG1  1 
ATOM   3035 C CG2  A ILE   A 1 137 ? 8.785  -11.739 -4.548  0.48 16.74 ?  137 ILE   A CG2  1 
ATOM   3036 C CG2  B ILE   A 1 137 ? 8.785  -12.026 -4.738  0.52 17.44 ?  137 ILE   A CG2  1 
ATOM   3037 C CD1  A ILE   A 1 137 ? 6.675  -9.593  -4.861  0.48 18.92 ?  137 ILE   A CD1  1 
ATOM   3038 C CD1  B ILE   A 1 137 ? 6.674  -9.872  -5.170  0.52 19.63 ?  137 ILE   A CD1  1 
ATOM   3039 H H    A ILE   A 1 137 ? 10.347 -8.138  -4.635  0.48 17.80 ?  137 ILE   A H    1 
ATOM   3040 H H    B ILE   A 1 137 ? 10.276 -8.388  -4.816  0.52 17.61 ?  137 ILE   A H    1 
ATOM   3041 H HA   A ILE   A 1 137 ? 10.230 -10.090 -2.904  0.48 18.22 ?  137 ILE   A HA   1 
ATOM   3042 H HA   B ILE   A 1 137 ? 10.213 -10.369 -3.130  0.52 18.21 ?  137 ILE   A HA   1 
ATOM   3043 H HB   A ILE   A 1 137 ? 9.269  -10.026 -5.557  0.48 19.55 ?  137 ILE   A HB   1 
ATOM   3044 H HB   B ILE   A 1 137 ? 9.271  -10.343 -5.795  0.52 19.85 ?  137 ILE   A HB   1 
ATOM   3045 H HG12 A ILE   A 1 137 ? 7.800  -9.631  -3.174  0.48 21.37 ?  137 ILE   A HG12 1 
ATOM   3046 H HG12 B ILE   A 1 137 ? 7.757  -9.927  -3.444  0.52 21.80 ?  137 ILE   A HG12 1 
ATOM   3047 H HG13 A ILE   A 1 137 ? 8.209  -8.464  -4.170  0.48 21.37 ?  137 ILE   A HG13 1 
ATOM   3048 H HG13 B ILE   A 1 137 ? 8.202  -8.755  -4.417  0.52 21.80 ?  137 ILE   A HG13 1 
ATOM   3049 H HG21 A ILE   A 1 137 ? 8.011  -11.920 -5.100  0.48 20.09 ?  137 ILE   A HG21 1 
ATOM   3050 H HG21 B ILE   A 1 137 ? 8.043  -12.238 -5.325  0.52 20.94 ?  137 ILE   A HG21 1 
ATOM   3051 H HG22 A ILE   A 1 137 ? 9.532  -12.260 -4.872  0.48 20.09 ?  137 ILE   A HG22 1 
ATOM   3052 H HG22 B ILE   A 1 137 ? 9.549  -12.557 -4.995  0.52 20.94 ?  137 ILE   A HG22 1 
ATOM   3053 H HG23 A ILE   A 1 137 ? 8.596  -11.966 -3.625  0.48 20.09 ?  137 ILE   A HG23 1 
ATOM   3054 H HG23 B ILE   A 1 137 ? 8.542  -12.216 -3.818  0.52 20.94 ?  137 ILE   A HG23 1 
ATOM   3055 H HD11 A ILE   A 1 137 ? 5.980  -9.144  -4.368  0.48 22.71 ?  137 ILE   A HD11 1 
ATOM   3056 H HD11 B ILE   A 1 137 ? 5.931  -9.571  -4.630  0.52 23.56 ?  137 ILE   A HD11 1 
ATOM   3057 H HD12 A ILE   A 1 137 ? 6.763  -9.210  -5.750  0.48 22.71 ?  137 ILE   A HD12 1 
ATOM   3058 H HD12 B ILE   A 1 137 ? 6.738  -9.341  -5.978  0.52 23.56 ?  137 ILE   A HD12 1 
ATOM   3059 H HD13 A ILE   A 1 137 ? 6.460  -10.538 -4.926  0.48 22.71 ?  137 ILE   A HD13 1 
ATOM   3060 H HD13 B ILE   A 1 137 ? 6.550  -10.804 -5.394  0.52 23.56 ?  137 ILE   A HD13 1 
ATOM   3061 N N    A HIS   A 1 138 ? 12.178 -10.628 -5.390  0.48 14.93 ?  138 HIS   A N    1 
ATOM   3062 N N    B HIS   A 1 138 ? 12.246 -10.768 -5.543  0.52 15.23 ?  138 HIS   A N    1 
ATOM   3063 C CA   A HIS   A 1 138 ? 13.315 -11.430 -5.832  0.48 14.95 ?  138 HIS   A CA   1 
ATOM   3064 C CA   B HIS   A 1 138 ? 13.448 -11.494 -5.928  0.52 15.44 ?  138 HIS   A CA   1 
ATOM   3065 C C    A HIS   A 1 138 ? 14.483 -11.318 -4.860  0.48 14.76 ?  138 HIS   A C    1 
ATOM   3066 C C    B HIS   A 1 138 ? 14.561 -11.326 -4.896  0.52 14.98 ?  138 HIS   A C    1 
ATOM   3067 O O    A HIS   A 1 138 ? 15.126 -12.322 -4.526  0.48 15.14 ?  138 HIS   A O    1 
ATOM   3068 O O    B HIS   A 1 138 ? 15.238 -12.301 -4.545  0.52 15.31 ?  138 HIS   A O    1 
ATOM   3069 C CB   A HIS   A 1 138 ? 13.734 -10.993 -7.236  0.48 15.77 ?  138 HIS   A CB   1 
ATOM   3070 C CB   B HIS   A 1 138 ? 13.908 -11.036 -7.308  0.52 16.74 ?  138 HIS   A CB   1 
ATOM   3071 C CG   A HIS   A 1 138 ? 15.019 -11.602 -7.699  0.48 16.63 ?  138 HIS   A CG   1 
ATOM   3072 C CG   B HIS   A 1 138 ? 15.161 -11.707 -7.766  0.52 17.93 ?  138 HIS   A CG   1 
ATOM   3073 N ND1  A HIS   A 1 138 ? 15.156 -12.949 -7.959  0.48 17.62 ?  138 HIS   A ND1  1 
ATOM   3074 N ND1  B HIS   A 1 138 ? 15.241 -13.067 -7.980  0.52 19.04 ?  138 HIS   A ND1  1 
ATOM   3075 C CD2  A HIS   A 1 138 ? 16.231 -11.048 -7.943  0.48 17.00 ?  138 HIS   A CD2  1 
ATOM   3076 C CD2  B HIS   A 1 138 ? 16.391 -11.211 -8.029  0.52 18.35 ?  138 HIS   A CD2  1 
ATOM   3077 C CE1  A HIS   A 1 138 ? 16.395 -13.197 -8.346  0.48 17.67 ?  138 HIS   A CE1  1 
ATOM   3078 C CE1  B HIS   A 1 138 ? 16.465 -13.376 -8.367  0.52 19.40 ?  138 HIS   A CE1  1 
ATOM   3079 N NE2  A HIS   A 1 138 ? 17.068 -12.061 -8.344  0.48 17.18 ?  138 HIS   A NE2  1 
ATOM   3080 N NE2  B HIS   A 1 138 ? 17.183 -12.269 -8.404  0.52 18.76 ?  138 HIS   A NE2  1 
ATOM   3081 H H    A HIS   A 1 138 ? 11.962 -9.990  -5.929  0.48 17.93 ?  138 HIS   A H    1 
ATOM   3082 H H    B HIS   A 1 138 ? 12.030 -10.126 -6.074  0.52 18.29 ?  138 HIS   A H    1 
ATOM   3083 H HA   A HIS   A 1 138 ? 13.048 -12.357 -5.875  0.48 17.95 ?  138 HIS   A HA   1 
ATOM   3084 H HA   B HIS   A 1 138 ? 13.235 -12.437 -5.988  0.52 18.53 ?  138 HIS   A HA   1 
ATOM   3085 H HB2  A HIS   A 1 138 ? 13.040 -11.252 -7.865  0.48 18.94 ?  138 HIS   A HB2  1 
ATOM   3086 H HB2  B HIS   A 1 138 ? 13.208 -11.232 -7.953  0.52 20.10 ?  138 HIS   A HB2  1 
ATOM   3087 H HB3  A HIS   A 1 138 ? 13.843 -10.029 -7.250  0.48 18.94 ?  138 HIS   A HB3  1 
ATOM   3088 H HB3  B HIS   A 1 138 ? 14.072 -10.080 -7.284  0.52 20.10 ?  138 HIS   A HB3  1 
ATOM   3089 H HD1  A HIS   A 1 138 ? 14.532 -13.537 -7.884  0.48 21.15 ?  138 HIS   A HD1  1 
ATOM   3090 H HD2  A HIS   A 1 138 ? 16.455 -10.150 -7.857  0.48 20.41 ?  138 HIS   A HD2  1 
ATOM   3091 H HD2  B HIS   A 1 138 ? 16.647 -10.320 -7.969  0.52 22.02 ?  138 HIS   A HD2  1 
ATOM   3092 H HE1  A HIS   A 1 138 ? 16.735 -14.033 -8.579  0.48 21.21 ?  138 HIS   A HE1  1 
ATOM   3093 H HE1  B HIS   A 1 138 ? 16.767 -14.229 -8.575  0.52 23.29 ?  138 HIS   A HE1  1 
ATOM   3094 H HE2  B HIS   A 1 138 ? 18.010 -12.217 -8.625  0.52 22.52 ?  138 HIS   A HE2  1 
ATOM   3095 N N    . SER   A 1 139 ? 14.770 -10.106 -4.396  1.00 14.56 ?  139 SER   A N    1 
ATOM   3096 C CA   . SER   A 1 139 ? 15.843 -9.910  -3.428  1.00 14.19 ?  139 SER   A CA   1 
ATOM   3097 C C    . SER   A 1 139 ? 15.613 -10.735 -2.171  1.00 14.00 ?  139 SER   A C    1 
ATOM   3098 O O    . SER   A 1 139 ? 16.552 -11.338 -1.635  1.00 14.40 ?  139 SER   A O    1 
ATOM   3099 C CB   . SER   A 1 139 ? 15.976 -8.431  -3.079  1.00 14.14 ?  139 SER   A CB   1 
ATOM   3100 O OG   . SER   A 1 139 ? 17.047 -8.256  -2.170  1.00 14.84 ?  139 SER   A OG   1 
ATOM   3101 H H    A SER   A 1 139 ? 14.357 -9.387  -4.613  0.48 17.48 ?  139 SER   A H    1 
ATOM   3102 H H    B SER   A 1 139 ? 14.324 -9.400  -4.592  0.52 17.48 ?  139 SER   A H    1 
ATOM   3103 H HA   . SER   A 1 139 ? 16.683 -10.196 -3.818  1.00 17.03 ?  139 SER   A HA   1 
ATOM   3104 H HB2  . SER   A 1 139 ? 16.157 -7.920  -3.881  1.00 16.98 ?  139 SER   A HB2  1 
ATOM   3105 H HB3  . SER   A 1 139 ? 15.154 -8.120  -2.661  1.00 16.98 ?  139 SER   A HB3  1 
ATOM   3106 H HG   . SER   A 1 139 ? 17.130 -7.429  -1.962  1.00 17.81 ?  139 SER   A HG   1 
ATOM   3107 N N    . LEU   A 1 140 ? 14.371 -10.784 -1.688  1.00 13.62 ?  140 LEU   A N    1 
ATOM   3108 C CA   . LEU   A 1 140 ? 14.081 -11.582 -0.499  1.00 14.31 ?  140 LEU   A CA   1 
ATOM   3109 C C    . LEU   A 1 140 ? 14.337 -13.063 -0.761  1.00 14.55 ?  140 LEU   A C    1 
ATOM   3110 O O    . LEU   A 1 140 ? 14.872 -13.774 0.100   1.00 15.40 ?  140 LEU   A O    1 
ATOM   3111 C CB   . LEU   A 1 140 ? 12.645 -11.322 -0.040  1.00 14.78 ?  140 LEU   A CB   1 
ATOM   3112 C CG   . LEU   A 1 140 ? 12.163 -12.144 1.157   1.00 15.61 ?  140 LEU   A CG   1 
ATOM   3113 C CD1  . LEU   A 1 140 ? 13.063 -11.974 2.373   1.00 15.77 ?  140 LEU   A CD1  1 
ATOM   3114 C CD2  . LEU   A 1 140 ? 10.703 -11.791 1.497   1.00 16.17 ?  140 LEU   A CD2  1 
ATOM   3115 H H    . LEU   A 1 140 ? 13.695 -10.373 -2.019  1.00 16.35 ?  140 LEU   A H    1 
ATOM   3116 H HA   . LEU   A 1 140 ? 14.671 -11.304 0.219   1.00 17.18 ?  140 LEU   A HA   1 
ATOM   3117 H HB2  . LEU   A 1 140 ? 12.567 -10.386 0.205   1.00 17.74 ?  140 LEU   A HB2  1 
ATOM   3118 H HB3  . LEU   A 1 140 ? 12.049 -11.512 -0.779  1.00 17.74 ?  140 LEU   A HB3  1 
ATOM   3119 H HG   . LEU   A 1 140 ? 12.171 -13.080 0.914   1.00 18.74 ?  140 LEU   A HG   1 
ATOM   3120 H HD11 . LEU   A 1 140 ? 12.672 -12.447 3.126   1.00 18.93 ?  140 LEU   A HD11 1 
ATOM   3121 H HD12 . LEU   A 1 140 ? 13.935 -12.349 2.168   1.00 18.93 ?  140 LEU   A HD12 1 
ATOM   3122 H HD13 . LEU   A 1 140 ? 13.145 -11.033 2.580   1.00 18.93 ?  140 LEU   A HD13 1 
ATOM   3123 H HD21 . LEU   A 1 140 ? 10.413 -12.323 2.258   1.00 19.41 ?  140 LEU   A HD21 1 
ATOM   3124 H HD22 . LEU   A 1 140 ? 10.642 -10.847 1.716   1.00 19.41 ?  140 LEU   A HD22 1 
ATOM   3125 H HD23 . LEU   A 1 140 ? 10.139 -11.987 0.729   1.00 19.41 ?  140 LEU   A HD23 1 
ATOM   3126 N N    . ARG   A 1 141 ? 13.961 -13.542 -1.947  1.00 15.29 ?  141 ARG   A N    1 
ATOM   3127 C CA   . ARG   A 1 141 ? 14.199 -14.935 -2.299  1.00 16.06 ?  141 ARG   A CA   1 
ATOM   3128 C C    . ARG   A 1 141 ? 15.693 -15.242 -2.313  1.00 15.55 ?  141 ARG   A C    1 
ATOM   3129 O O    . ARG   A 1 141 ? 16.143 -16.249 -1.751  1.00 15.77 ?  141 ARG   A O    1 
ATOM   3130 C CB   . ARG   A 1 141 ? 13.576 -15.200 -3.669  1.00 17.44 ?  141 ARG   A CB   1 
ATOM   3131 C CG   . ARG   A 1 141 ? 13.561 -16.647 -4.101  1.00 19.69 ?  141 ARG   A CG   1 
ATOM   3132 C CD   . ARG   A 1 141 ? 12.510 -17.407 -3.345  1.00 21.96 ?  141 ARG   A CD   1 
ATOM   3133 N NE   . ARG   A 1 141 ? 13.098 -18.188 -2.272  1.00 23.06 ?  141 ARG   A NE   1 
ATOM   3134 C CZ   . ARG   A 1 141 ? 12.401 -18.708 -1.270  1.00 23.42 ?  141 ARG   A CZ   1 
ATOM   3135 N NH1  . ARG   A 1 141 ? 11.122 -18.420 -1.095  1.00 22.73 ?  141 ARG   A NH1  1 
ATOM   3136 N NH2  . ARG   A 1 141 ? 13.006 -19.532 -0.416  1.00 24.37 ?  141 ARG   A NH2  1 
ATOM   3137 H H    . ARG   A 1 141 ? 13.575 -13.074 -2.562  1.00 18.35 ?  141 ARG   A H    1 
ATOM   3138 H HA   . ARG   A 1 141 ? 13.771 -15.507 -1.648  1.00 19.28 ?  141 ARG   A HA   1 
ATOM   3139 H HB2  . ARG   A 1 141 ? 12.656 -14.882 -3.661  1.00 20.93 ?  141 ARG   A HB2  1 
ATOM   3140 H HB3  . ARG   A 1 141 ? 14.076 -14.703 -4.335  1.00 20.93 ?  141 ARG   A HB3  1 
ATOM   3141 H HG2  . ARG   A 1 141 ? 13.361 -16.704 -5.050  1.00 23.64 ?  141 ARG   A HG2  1 
ATOM   3142 H HG3  . ARG   A 1 141 ? 14.427 -17.053 -3.917  1.00 23.64 ?  141 ARG   A HG3  1 
ATOM   3143 H HD2  . ARG   A 1 141 ? 11.884 -16.779 -2.947  1.00 26.36 ?  141 ARG   A HD2  1 
ATOM   3144 H HD3  . ARG   A 1 141 ? 12.043 -18.002 -3.952  1.00 26.36 ?  141 ARG   A HD3  1 
ATOM   3145 H HE   . ARG   A 1 141 ? 13.916 -18.440 -2.359  1.00 27.68 ?  141 ARG   A HE   1 
ATOM   3146 H HH11 . ARG   A 1 141 ? 10.715 -17.896 -1.643  1.00 27.29 ?  141 ARG   A HH11 1 
ATOM   3147 H HH12 . ARG   A 1 141 ? 10.689 -18.760 -0.432  1.00 27.29 ?  141 ARG   A HH12 1 
ATOM   3148 H HH21 . ARG   A 1 141 ? 13.837 -19.727 -0.521  1.00 29.25 ?  141 ARG   A HH21 1 
ATOM   3149 H HH22 . ARG   A 1 141 ? 12.568 -19.865 0.247   1.00 29.25 ?  141 ARG   A HH22 1 
ATOM   3150 N N    . VAL   A 1 142 ? 16.486 -14.378 -2.951  1.00 14.79 ?  142 VAL   A N    1 
ATOM   3151 C CA   . VAL   A 1 142 ? 17.929 -14.597 -2.979  1.00 14.73 ?  142 VAL   A CA   1 
ATOM   3152 C C    . VAL   A 1 142 ? 18.496 -14.575 -1.567  1.00 14.33 ?  142 VAL   A C    1 
ATOM   3153 O O    . VAL   A 1 142 ? 19.349 -15.400 -1.212  1.00 15.08 ?  142 VAL   A O    1 
ATOM   3154 C CB   . VAL   A 1 142 ? 18.634 -13.592 -3.909  1.00 15.17 ?  142 VAL   A CB   1 
ATOM   3155 C CG1  . VAL   A 1 142 ? 20.139 -13.813 -3.854  1.00 15.37 ?  142 VAL   A CG1  1 
ATOM   3156 C CG2  . VAL   A 1 142 ? 18.154 -13.758 -5.340  1.00 16.48 ?  142 VAL   A CG2  1 
ATOM   3157 H H    . VAL   A 1 142 ? 16.220 -13.661 -3.364  1.00 17.75 ?  142 VAL   A H    1 
ATOM   3158 H HA   . VAL   A 1 142 ? 18.092 -15.476 -3.341  1.00 17.69 ?  142 VAL   A HA   1 
ATOM   3159 H HB   . VAL   A 1 142 ? 18.449 -12.681 -3.624  1.00 18.21 ?  142 VAL   A HB   1 
ATOM   3160 H HG11 . VAL   A 1 142 ? 20.556 -13.351 -4.598  1.00 18.45 ?  142 VAL   A HG11 1 
ATOM   3161 H HG12 . VAL   A 1 142 ? 20.484 -13.463 -3.016  1.00 18.45 ?  142 VAL   A HG12 1 
ATOM   3162 H HG13 . VAL   A 1 142 ? 20.320 -14.764 -3.914  1.00 18.45 ?  142 VAL   A HG13 1 
ATOM   3163 H HG21 . VAL   A 1 142 ? 18.626 -13.124 -5.906  1.00 19.79 ?  142 VAL   A HG21 1 
ATOM   3164 H HG22 . VAL   A 1 142 ? 18.353 -14.664 -5.630  1.00 19.79 ?  142 VAL   A HG22 1 
ATOM   3165 H HG23 . VAL   A 1 142 ? 17.206 -13.596 -5.374  1.00 19.79 ?  142 VAL   A HG23 1 
ATOM   3166 N N    . CYS   A 1 143 ? 18.029 -13.644 -0.736  1.00 13.96 ?  143 CYS   A N    1 
ATOM   3167 C CA   . CYS   A 1 143 ? 18.482 -13.585 0.650   1.00 14.10 ?  143 CYS   A CA   1 
ATOM   3168 C C    . CYS   A 1 143 ? 18.264 -14.918 1.356   1.00 15.13 ?  143 CYS   A C    1 
ATOM   3169 O O    . CYS   A 1 143 ? 19.192 -15.489 1.938   1.00 15.01 ?  143 CYS   A O    1 
ATOM   3170 C CB   . CYS   A 1 143 ? 17.738 -12.474 1.381   1.00 14.48 ?  143 CYS   A CB   1 
ATOM   3171 S SG   . CYS   A 1 143 ? 18.219 -12.288 3.104   1.00 15.42 ?  143 CYS   A SG   1 
ATOM   3172 H H    . CYS   A 1 143 ? 17.452 -13.043 -0.947  1.00 16.76 ?  143 CYS   A H    1 
ATOM   3173 H HA   . CYS   A 1 143 ? 19.430 -13.383 0.670   1.00 16.93 ?  143 CYS   A HA   1 
ATOM   3174 H HB2  . CYS   A 1 143 ? 17.909 -11.630 0.931   1.00 17.39 ?  143 CYS   A HB2  1 
ATOM   3175 H HB3  . CYS   A 1 143 ? 16.790 -12.665 1.358   1.00 17.39 ?  143 CYS   A HB3  1 
ATOM   3176 H HG   . CYS   A 1 143 ? 17.615 -11.365 3.571   1.00 18.51 ?  143 CYS   A HG   1 
ATOM   3177 N N    . VAL   A 1 144 ? 17.030 -15.421 1.328   1.00 15.71 ?  144 VAL   A N    1 
ATOM   3178 C CA   . VAL   A 1 144 ? 16.701 -16.644 2.050   1.00 17.14 ?  144 VAL   A CA   1 
ATOM   3179 C C    . VAL   A 1 144 ? 17.482 -17.828 1.511   1.00 17.39 ?  144 VAL   A C    1 
ATOM   3180 O O    . VAL   A 1 144 ? 17.829 -18.750 2.266   1.00 18.04 ?  144 VAL   A O    1 
ATOM   3181 C CB   . VAL   A 1 144 ? 15.174 -16.866 1.974   1.00 20.57 ?  144 VAL   A CB   1 
ATOM   3182 C CG1  . VAL   A 1 144 ? 14.806 -18.307 2.276   1.00 24.09 ?  144 VAL   A CG1  1 
ATOM   3183 C CG2  . VAL   A 1 144 ? 14.468 -15.846 2.883   1.00 19.93 ?  144 VAL   A CG2  1 
ATOM   3184 H H    . VAL   A 1 144 ? 16.370 -15.069 0.898   1.00 18.86 ?  144 VAL   A H    1 
ATOM   3185 H HA   . VAL   A 1 144 ? 16.936 -16.529 2.981   1.00 20.57 ?  144 VAL   A HA   1 
ATOM   3186 H HB   . VAL   A 1 144 ? 14.889 -16.674 1.063   1.00 24.70 ?  144 VAL   A HB   1 
ATOM   3187 H HG11 . VAL   A 1 144 ? 13.854 -18.351 2.459   1.00 28.92 ?  144 VAL   A HG11 1 
ATOM   3188 H HG12 . VAL   A 1 144 ? 15.016 -18.855 1.503   1.00 28.92 ?  144 VAL   A HG12 1 
ATOM   3189 H HG13 . VAL   A 1 144 ? 15.308 -18.604 3.046   1.00 28.92 ?  144 VAL   A HG13 1 
ATOM   3190 H HG21 . VAL   A 1 144 ? 13.509 -15.999 2.841   1.00 23.92 ?  144 VAL   A HG21 1 
ATOM   3191 H HG22 . VAL   A 1 144 ? 14.780 -15.965 3.793   1.00 23.92 ?  144 VAL   A HG22 1 
ATOM   3192 H HG23 . VAL   A 1 144 ? 14.670 -14.947 2.578   1.00 23.92 ?  144 VAL   A HG23 1 
ATOM   3193 N N    . ASP   A 1 145 ? 17.763 -17.836 0.211   1.00 17.53 ?  145 ASP   A N    1 
ATOM   3194 C CA   . ASP   A 1 145 ? 18.454 -18.945 -0.436  1.00 18.31 ?  145 ASP   A CA   1 
ATOM   3195 C C    . ASP   A 1 145 ? 19.976 -18.824 -0.383  1.00 17.86 ?  145 ASP   A C    1 
ATOM   3196 O O    . ASP   A 1 145 ? 20.669 -19.739 -0.842  1.00 19.69 ?  145 ASP   A O    1 
ATOM   3197 C CB   . ASP   A 1 145 ? 18.004 -19.066 -1.896  1.00 20.39 ?  145 ASP   A CB   1 
ATOM   3198 C CG   . ASP   A 1 145 ? 16.549 -19.495 -2.031  1.00 22.89 ?  145 ASP   A CG   1 
ATOM   3199 O OD1  . ASP   A 1 145 ? 15.988 -20.048 -1.062  1.00 23.17 ?  145 ASP   A OD1  1 
ATOM   3200 O OD2  . ASP   A 1 145 ? 15.970 -19.271 -3.110  1.00 24.33 -1 145 ASP   A OD2  1 
ATOM   3201 H H    . ASP   A 1 145 ? 17.543 -17.200 -0.331  1.00 21.04 ?  145 ASP   A H    1 
ATOM   3202 H HA   . ASP   A 1 145 ? 18.206 -19.762 0.017   1.00 21.99 ?  145 ASP   A HA   1 
ATOM   3203 H HB2  . ASP   A 1 145 ? 18.113 -18.202 -2.330  1.00 24.48 ?  145 ASP   A HB2  1 
ATOM   3204 H HB3  . ASP   A 1 145 ? 18.555 -19.729 -2.337  1.00 24.48 ?  145 ASP   A HB3  1 
ATOM   3205 N N    . THR   A 1 146 ? 20.515 -17.734 0.158   1.00 15.84 ?  146 THR   A N    1 
ATOM   3206 C CA   . THR   A 1 146 ? 21.958 -17.506 0.174   1.00 15.49 ?  146 THR   A CA   1 
ATOM   3207 C C    . THR   A 1 146 ? 22.518 -17.322 1.571   1.00 15.19 ?  146 THR   A C    1 
ATOM   3208 O O    . THR   A 1 146 ? 23.597 -17.853 1.878   1.00 16.04 ?  146 THR   A O    1 
ATOM   3209 C CB   . THR   A 1 146 ? 22.288 -16.259 -0.665  1.00 15.72 ?  146 THR   A CB   1 
ATOM   3210 O OG1  . THR   A 1 146 ? 21.771 -16.425 -1.988  1.00 16.35 ?  146 THR   A OG1  1 
ATOM   3211 C CG2  . THR   A 1 146 ? 23.792 -16.027 -0.747  1.00 16.09 ?  146 THR   A CG2  1 
ATOM   3212 H H    . THR   A 1 146 ? 20.062 -17.099 0.527   1.00 19.02 ?  146 THR   A H    1 
ATOM   3213 H HA   . THR   A 1 146 ? 22.406 -18.263 -0.229  1.00 18.60 ?  146 THR   A HA   1 
ATOM   3214 H HB   . THR   A 1 146 ? 21.880 -15.478 -0.255  1.00 18.87 ?  146 THR   A HB   1 
ATOM   3215 H HG1  . THR   A 1 146 ? 20.936 -16.501 -1.962  1.00 19.62 ?  146 THR   A HG1  1 
ATOM   3216 H HG21 . THR   A 1 146 ? 23.984 -15.367 -1.430  1.00 19.32 ?  146 THR   A HG21 1 
ATOM   3217 H HG22 . THR   A 1 146 ? 24.126 -15.708 0.105   1.00 19.32 ?  146 THR   A HG22 1 
ATOM   3218 H HG23 . THR   A 1 146 ? 24.239 -16.857 -0.975  1.00 19.32 ?  146 THR   A HG23 1 
ATOM   3219 N N    . VAL   A 1 147 ? 21.840 -16.556 2.412   1.00 14.86 ?  147 VAL   A N    1 
ATOM   3220 C CA   . VAL   A 1 147 ? 22.352 -16.244 3.737   1.00 15.16 ?  147 VAL   A CA   1 
ATOM   3221 C C    . VAL   A 1 147 ? 22.025 -17.393 4.680   1.00 15.32 ?  147 VAL   A C    1 
ATOM   3222 O O    . VAL   A 1 147 ? 20.877 -17.853 4.751   1.00 16.39 ?  147 VAL   A O    1 
ATOM   3223 C CB   . VAL   A 1 147 ? 21.766 -14.919 4.237   1.00 15.14 ?  147 VAL   A CB   1 
ATOM   3224 C CG1  . VAL   A 1 147 ? 22.326 -14.590 5.605   1.00 16.46 ?  147 VAL   A CG1  1 
ATOM   3225 C CG2  . VAL   A 1 147 ? 22.037 -13.803 3.227   1.00 15.80 ?  147 VAL   A CG2  1 
ATOM   3226 H H    . VAL   A 1 147 ? 21.078 -16.199 2.239   1.00 17.84 ?  147 VAL   A H    1 
ATOM   3227 H HA   . VAL   A 1 147 ? 23.316 -16.154 3.694   1.00 18.20 ?  147 VAL   A HA   1 
ATOM   3228 H HB   . VAL   A 1 147 ? 20.807 -15.014 4.323   1.00 18.18 ?  147 VAL   A HB   1 
ATOM   3229 H HG11 . VAL   A 1 147 ? 22.096 -13.674 5.824   1.00 19.76 ?  147 VAL   A HG11 1 
ATOM   3230 H HG12 . VAL   A 1 147 ? 21.939 -15.193 6.259   1.00 19.76 ?  147 VAL   A HG12 1 
ATOM   3231 H HG13 . VAL   A 1 147 ? 23.289 -14.693 5.585   1.00 19.76 ?  147 VAL   A HG13 1 
ATOM   3232 H HG21 . VAL   A 1 147 ? 21.754 -12.959 3.610   1.00 18.96 ?  147 VAL   A HG21 1 
ATOM   3233 H HG22 . VAL   A 1 147 ? 22.987 -13.779 3.034   1.00 18.96 ?  147 VAL   A HG22 1 
ATOM   3234 H HG23 . VAL   A 1 147 ? 21.538 -13.985 2.416   1.00 18.96 ?  147 VAL   A HG23 1 
ATOM   3235 N N    . ARG   A 1 148 ? 23.044 -17.857 5.406   1.00 15.45 ?  148 ARG   A N    1 
ATOM   3236 C CA   . ARG   A 1 148 ? 22.905 -18.914 6.391   1.00 16.01 ?  148 ARG   A CA   1 
ATOM   3237 C C    . ARG   A 1 148 ? 23.005 -18.412 7.816   1.00 16.47 ?  148 ARG   A C    1 
ATOM   3238 O O    . ARG   A 1 148 ? 22.591 -19.128 8.735   1.00 18.38 ?  148 ARG   A O    1 
ATOM   3239 C CB   . ARG   A 1 148 ? 23.956 -20.005 6.154   1.00 16.90 ?  148 ARG   A CB   1 
ATOM   3240 C CG   . ARG   A 1 148 ? 23.851 -20.636 4.780   1.00 18.10 ?  148 ARG   A CG   1 
ATOM   3241 C CD   . ARG   A 1 148 ? 24.945 -21.669 4.553   1.00 18.85 ?  148 ARG   A CD   1 
ATOM   3242 N NE   . ARG   A 1 148 ? 26.280 -21.078 4.592   1.00 18.85 ?  148 ARG   A NE   1 
ATOM   3243 C CZ   . ARG   A 1 148 ? 26.799 -20.356 3.610   1.00 18.50 ?  148 ARG   A CZ   1 
ATOM   3244 N NH1  . ARG   A 1 148 ? 26.141 -20.158 2.478   1.00 18.68 ?  148 ARG   A NH1  1 
ATOM   3245 N NH2  . ARG   A 1 148 ? 28.007 -19.810 3.768   1.00 18.50 ?  148 ARG   A NH2  1 
ATOM   3246 H H    . ARG   A 1 148 ? 23.849 -17.556 5.342   1.00 18.55 ?  148 ARG   A H    1 
ATOM   3247 H HA   . ARG   A 1 148 ? 22.034 -19.322 6.289   1.00 19.22 ?  148 ARG   A HA   1 
ATOM   3248 H HB2  . ARG   A 1 148 ? 24.840 -19.629 6.242   1.00 20.29 ?  148 ARG   A HB2  1 
ATOM   3249 H HB3  . ARG   A 1 148 ? 23.830 -20.718 6.807   1.00 20.29 ?  148 ARG   A HB3  1 
ATOM   3250 H HG2  . ARG   A 1 148 ? 22.988 -21.067 4.692   1.00 21.73 ?  148 ARG   A HG2  1 
ATOM   3251 H HG3  . ARG   A 1 148 ? 23.941 -19.933 4.110   1.00 21.73 ?  148 ARG   A HG3  1 
ATOM   3252 H HD2  . ARG   A 1 148 ? 24.889 -22.337 5.246   1.00 22.63 ?  148 ARG   A HD2  1 
ATOM   3253 H HD3  . ARG   A 1 148 ? 24.818 -22.070 3.681   1.00 22.63 ?  148 ARG   A HD3  1 
ATOM   3254 H HE   . ARG   A 1 148 ? 26.752 -21.197 5.300   1.00 22.63 ?  148 ARG   A HE   1 
ATOM   3255 H HH11 . ARG   A 1 148 ? 25.361 -20.493 2.369   1.00 22.42 ?  148 ARG   A HH11 1 
ATOM   3256 H HH12 . ARG   A 1 148 ? 26.496 -19.677 1.857   1.00 22.42 ?  148 ARG   A HH12 1 
ATOM   3257 H HH21 . ARG   A 1 148 ? 28.438 -19.921 4.505   1.00 22.21 ?  148 ARG   A HH21 1 
ATOM   3258 H HH22 . ARG   A 1 148 ? 28.352 -19.330 3.140   1.00 22.21 ?  148 ARG   A HH22 1 
ATOM   3259 N N    . THR   A 1 149 ? 23.543 -17.213 8.017   1.00 16.69 ?  149 THR   A N    1 
ATOM   3260 C CA   . THR   A 1 149 ? 23.610 -16.600 9.330   1.00 16.48 ?  149 THR   A CA   1 
ATOM   3261 C C    . THR   A 1 149 ? 22.286 -15.895 9.619   1.00 15.72 ?  149 THR   A C    1 
ATOM   3262 O O    . THR   A 1 149 ? 21.358 -15.898 8.799   1.00 16.53 ?  149 THR   A O    1 
ATOM   3263 C CB   . THR   A 1 149 ? 24.811 -15.665 9.383   1.00 17.12 ?  149 THR   A CB   1 
ATOM   3264 O OG1  . THR   A 1 149 ? 24.697 -14.739 8.297   1.00 16.69 ?  149 THR   A OG1  1 
ATOM   3265 C CG2  . THR   A 1 149 ? 26.118 -16.468 9.268   1.00 16.85 ?  149 THR   A CG2  1 
ATOM   3266 H H    . THR   A 1 149 ? 23.883 -16.728 7.395   1.00 20.04 ?  149 THR   A H    1 
ATOM   3267 H HA   . THR   A 1 149 ? 23.735 -17.299 9.997   1.00 19.79 ?  149 THR   A HA   1 
ATOM   3268 H HB   . THR   A 1 149 ? 24.805 -15.189 10.226  1.00 20.55 ?  149 THR   A HB   1 
ATOM   3269 H HG1  . THR   A 1 149 ? 25.349 -14.211 8.304   1.00 20.03 ?  149 THR   A HG1  1 
ATOM   3270 H HG21 . THR   A 1 149 ? 26.881 -15.866 9.323   1.00 20.23 ?  149 THR   A HG21 1 
ATOM   3271 H HG22 . THR   A 1 149 ? 26.182 -17.117 9.988   1.00 20.23 ?  149 THR   A HG22 1 
ATOM   3272 H HG23 . THR   A 1 149 ? 26.154 -16.938 8.419   1.00 20.23 ?  149 THR   A HG23 1 
ATOM   3273 N N    . ASN   A 1 150 ? 22.165 -15.330 10.816  1.00 15.91 ?  150 ASN   A N    1 
ATOM   3274 C CA   . ASN   A 1 150 ? 20.883 -14.806 11.284  1.00 16.96 ?  150 ASN   A CA   1 
ATOM   3275 C C    . ASN   A 1 150 ? 20.700 -13.374 10.800  1.00 16.18 ?  150 ASN   A C    1 
ATOM   3276 O O    . ASN   A 1 150 ? 21.468 -12.476 11.174  1.00 17.54 ?  150 ASN   A O    1 
ATOM   3277 C CB   . ASN   A 1 150 ? 20.812 -14.897 12.803  1.00 20.14 ?  150 ASN   A CB   1 
ATOM   3278 C CG   . ASN   A 1 150 ? 20.741 -16.327 13.281  1.00 24.34 ?  150 ASN   A CG   1 
ATOM   3279 O OD1  . ASN   A 1 150 ? 20.117 -17.166 12.633  1.00 25.48 ?  150 ASN   A OD1  1 
ATOM   3280 N ND2  . ASN   A 1 150 ? 21.390 -16.622 14.404  1.00 26.77 ?  150 ASN   A ND2  1 
ATOM   3281 H H    . ASN   A 1 150 ? 22.806 -15.246 11.384  1.00 19.10 ?  150 ASN   A H    1 
ATOM   3282 H HA   . ASN   A 1 150 ? 20.163 -15.356 10.921  1.00 20.36 ?  150 ASN   A HA   1 
ATOM   3283 H HB2  . ASN   A 1 150 ? 21.600 -14.496 13.191  1.00 24.18 ?  150 ASN   A HB2  1 
ATOM   3284 H HB3  . ASN   A 1 150 ? 20.012 -14.447 13.120  1.00 24.18 ?  150 ASN   A HB3  1 
ATOM   3285 H HD21 . ASN   A 1 150 ? 21.386 -17.428 14.718  1.00 32.13 ?  150 ASN   A HD21 1 
ATOM   3286 H HD22 . ASN   A 1 150 ? 21.818 -16.007 14.828  1.00 32.13 ?  150 ASN   A HD22 1 
ATOM   3287 N N    . VAL   A 1 151 ? 19.702 -13.164 9.952   1.00 15.65 ?  151 VAL   A N    1 
ATOM   3288 C CA   . VAL   A 1 151 ? 19.482 -11.866 9.338   1.00 15.74 ?  151 VAL   A CA   1 
ATOM   3289 C C    . VAL   A 1 151 ? 18.112 -11.333 9.733   1.00 15.28 ?  151 VAL   A C    1 
ATOM   3290 O O    . VAL   A 1 151 ? 17.095 -12.041 9.639   1.00 17.29 ?  151 VAL   A O    1 
ATOM   3291 C CB   . VAL   A 1 151 ? 19.721 -11.893 7.815   1.00 18.05 ?  151 VAL   A CB   1 
ATOM   3292 C CG1  . VAL   A 1 151 ? 18.907 -12.947 7.140   1.00 20.00 ?  151 VAL   A CG1  1 
ATOM   3293 C CG2  . VAL   A 1 151 ? 19.449 -10.520 7.205   1.00 18.14 ?  151 VAL   A CG2  1 
ATOM   3294 H H    . VAL   A 1 151 ? 19.125 -13.768 9.712   1.00 18.79 ?  151 VAL   A H    1 
ATOM   3295 H HA   . VAL   A 1 151 ? 20.141 -11.254 9.707   1.00 18.90 ?  151 VAL   A HA   1 
ATOM   3296 H HB   . VAL   A 1 151 ? 20.660 -12.097 7.654   1.00 21.67 ?  151 VAL   A HB   1 
ATOM   3297 H HG11 . VAL   A 1 151 ? 19.012 -12.858 6.182   1.00 24.01 ?  151 VAL   A HG11 1 
ATOM   3298 H HG12 . VAL   A 1 151 ? 19.226 -13.817 7.431   1.00 24.01 ?  151 VAL   A HG12 1 
ATOM   3299 H HG13 . VAL   A 1 151 ? 17.980 -12.831 7.389   1.00 24.01 ?  151 VAL   A HG13 1 
ATOM   3300 H HG21 . VAL   A 1 151 ? 19.767 -10.512 6.286   1.00 21.77 ?  151 VAL   A HG21 1 
ATOM   3301 H HG22 . VAL   A 1 151 ? 18.494 -10.347 7.220   1.00 21.77 ?  151 VAL   A HG22 1 
ATOM   3302 H HG23 . VAL   A 1 151 ? 19.917 -9.841  7.717   1.00 21.77 ?  151 VAL   A HG23 1 
ATOM   3303 N N    . TYR   A 1 152 ? 18.113 -10.078 10.187  1.00 15.31 ?  152 TYR   A N    1 
ATOM   3304 C CA   . TYR   A 1 152 ? 16.926 -9.338  10.585  1.00 14.98 ?  152 TYR   A CA   1 
ATOM   3305 C C    . TYR   A 1 152 ? 16.727 -8.245  9.552   1.00 14.09 ?  152 TYR   A C    1 
ATOM   3306 O O    . TYR   A 1 152 ? 17.504 -7.287  9.500   1.00 14.54 ?  152 TYR   A O    1 
ATOM   3307 C CB   . TYR   A 1 152 ? 17.117 -8.784  11.991  1.00 16.36 ?  152 TYR   A CB   1 
ATOM   3308 C CG   . TYR   A 1 152 ? 17.087 -9.897  12.997  1.00 17.22 ?  152 TYR   A CG   1 
ATOM   3309 C CD1  . TYR   A 1 152 ? 18.228 -10.632 13.288  1.00 19.07 ?  152 TYR   A CD1  1 
ATOM   3310 C CD2  . TYR   A 1 152 ? 15.901 -10.256 13.613  1.00 18.08 ?  152 TYR   A CD2  1 
ATOM   3311 C CE1  . TYR   A 1 152 ? 18.194 -11.681 14.186  1.00 20.82 ?  152 TYR   A CE1  1 
ATOM   3312 C CE2  . TYR   A 1 152 ? 15.852 -11.312 14.515  1.00 19.97 ?  152 TYR   A CE2  1 
ATOM   3313 C CZ   . TYR   A 1 152 ? 17.004 -12.020 14.801  1.00 21.18 ?  152 TYR   A CZ   1 
ATOM   3314 O OH   . TYR   A 1 152 ? 16.968 -13.067 15.697  1.00 24.30 ?  152 TYR   A OH   1 
ATOM   3315 H H    . TYR   A 1 152 ? 18.842 -9.609  10.263  1.00 18.38 ?  152 TYR   A H    1 
ATOM   3316 H HA   . TYR   A 1 152 ? 16.162 -9.925  10.571  1.00 17.98 ?  152 TYR   A HA   1 
ATOM   3317 H HB2  . TYR   A 1 152 ? 17.981 -8.343  12.044  1.00 19.64 ?  152 TYR   A HB2  1 
ATOM   3318 H HB3  . TYR   A 1 152 ? 16.408 -8.159  12.187  1.00 19.64 ?  152 TYR   A HB3  1 
ATOM   3319 H HD1  . TYR   A 1 152 ? 19.033 -10.409 12.869  1.00 22.89 ?  152 TYR   A HD1  1 
ATOM   3320 H HD2  . TYR   A 1 152 ? 15.119 -9.779  13.415  1.00 21.71 ?  152 TYR   A HD2  1 
ATOM   3321 H HE1  . TYR   A 1 152 ? 18.968 -12.155 14.378  1.00 24.99 ?  152 TYR   A HE1  1 
ATOM   3322 H HE2  . TYR   A 1 152 ? 15.049 -11.529 14.929  1.00 23.98 ?  152 TYR   A HE2  1 
ATOM   3323 H HH   . TYR   A 1 152 ? 16.190 -13.150 15.998  1.00 29.17 ?  152 TYR   A HH   1 
ATOM   3324 N N    . LEU   A 1 153 ? 15.716 -8.412  8.706   1.00 13.61 ?  153 LEU   A N    1 
ATOM   3325 C CA   . LEU   A 1 153 ? 15.468 -7.515  7.591   1.00 13.75 ?  153 LEU   A CA   1 
ATOM   3326 C C    . LEU   A 1 153 ? 14.486 -6.428  7.996   1.00 14.19 ?  153 LEU   A C    1 
ATOM   3327 O O    . LEU   A 1 153 ? 13.405 -6.718  8.526   1.00 15.44 ?  153 LEU   A O    1 
ATOM   3328 C CB   . LEU   A 1 153 ? 14.886 -8.284  6.404   1.00 14.10 ?  153 LEU   A CB   1 
ATOM   3329 C CG   . LEU   A 1 153 ? 15.810 -9.300  5.738   1.00 14.44 ?  153 LEU   A CG   1 
ATOM   3330 C CD1  . LEU   A 1 153 ? 15.014 -10.168 4.789   1.00 15.00 ?  153 LEU   A CD1  1 
ATOM   3331 C CD2  . LEU   A 1 153 ? 16.926 -8.601  4.987   1.00 15.37 ?  153 LEU   A CD2  1 
ATOM   3332 H H    . LEU   A 1 153 ? 15.139 -9.052  8.767   1.00 16.34 ?  153 LEU   A H    1 
ATOM   3333 H HA   . LEU   A 1 153 ? 16.299 -7.103  7.324   1.00 16.51 ?  153 LEU   A HA   1 
ATOM   3334 H HB2  . LEU   A 1 153 ? 14.105 -8.760  6.709   1.00 16.93 ?  153 LEU   A HB2  1 
ATOM   3335 H HB3  . LEU   A 1 153 ? 14.633 -7.637  5.727   1.00 16.93 ?  153 LEU   A HB3  1 
ATOM   3336 H HG   . LEU   A 1 153 ? 16.214 -9.864  6.420   1.00 17.34 ?  153 LEU   A HG   1 
ATOM   3337 H HD11 . LEU   A 1 153 ? 15.597 -10.834 4.408   1.00 18.00 ?  153 LEU   A HD11 1 
ATOM   3338 H HD12 . LEU   A 1 153 ? 14.294 -10.586 5.281   1.00 18.00 ?  153 LEU   A HD12 1 
ATOM   3339 H HD13 . LEU   A 1 153 ? 14.649 -9.600  4.087   1.00 18.00 ?  153 LEU   A HD13 1 
ATOM   3340 H HD21 . LEU   A 1 153 ? 17.470 -9.265  4.545   1.00 18.46 ?  153 LEU   A HD21 1 
ATOM   3341 H HD22 . LEU   A 1 153 ? 16.530 -8.001  4.333   1.00 18.46 ?  153 LEU   A HD22 1 
ATOM   3342 H HD23 . LEU   A 1 153 ? 17.463 -8.092  5.616   1.00 18.46 ?  153 LEU   A HD23 1 
ATOM   3343 N N    . ALA   A 1 154 ? 14.857 -5.181  7.732   1.00 14.07 ?  154 ALA   A N    1 
ATOM   3344 C CA   . ALA   A 1 154 ? 13.994 -4.034  7.971   1.00 14.50 ?  154 ALA   A CA   1 
ATOM   3345 C C    . ALA   A 1 154 ? 13.500 -3.517  6.626   1.00 14.43 ?  154 ALA   A C    1 
ATOM   3346 O O    . ALA   A 1 154 ? 14.308 -3.194  5.748   1.00 15.34 ?  154 ALA   A O    1 
ATOM   3347 C CB   . ALA   A 1 154 ? 14.762 -2.938  8.705   1.00 15.79 ?  154 ALA   A CB   1 
ATOM   3348 H H    . ALA   A 1 154 ? 15.629 -4.969  7.403   1.00 16.89 ?  154 ALA   A H    1 
ATOM   3349 H HA   . ALA   A 1 154 ? 13.232 -4.304  8.509   1.00 17.40 ?  154 ALA   A HA   1 
ATOM   3350 H HB1  . ALA   A 1 154 ? 14.168 -2.187  8.854   1.00 18.96 ?  154 ALA   A HB1  1 
ATOM   3351 H HB2  . ALA   A 1 154 ? 15.077 -3.286  9.553   1.00 18.96 ?  154 ALA   A HB2  1 
ATOM   3352 H HB3  . ALA   A 1 154 ? 15.515 -2.663  8.159   1.00 18.96 ?  154 ALA   A HB3  1 
ATOM   3353 N N    A VAL   A 1 155 ? 12.180 -3.465  6.459   0.48 14.49 ?  155 VAL   A N    1 
ATOM   3354 N N    B VAL   A 1 155 ? 12.183 -3.437  6.474   0.52 15.05 ?  155 VAL   A N    1 
ATOM   3355 C CA   A VAL   A 1 155 ? 11.538 -2.970  5.244   0.48 14.89 ?  155 VAL   A CA   1 
ATOM   3356 C CA   B VAL   A 1 155 ? 11.548 -2.914  5.271   0.52 15.97 ?  155 VAL   A CA   1 
ATOM   3357 C C    A VAL   A 1 155 ? 10.797 -1.686  5.611   0.48 15.30 ?  155 VAL   A C    1 
ATOM   3358 C C    B VAL   A 1 155 ? 10.814 -1.634  5.658   0.52 16.83 ?  155 VAL   A C    1 
ATOM   3359 O O    A VAL   A 1 155 ? 9.831  -1.716  6.380   0.48 15.94 ?  155 VAL   A O    1 
ATOM   3360 O O    B VAL   A 1 155 ? 9.924  -1.658  6.515   0.52 17.30 ?  155 VAL   A O    1 
ATOM   3361 C CB   A VAL   A 1 155 ? 10.594 -4.021  4.640   0.48 15.23 ?  155 VAL   A CB   1 
ATOM   3362 C CB   B VAL   A 1 155 ? 10.600 -3.948  4.644   0.52 16.32 ?  155 VAL   A CB   1 
ATOM   3363 C CG1  A VAL   A 1 155 ? 9.934  -3.489  3.379   0.48 16.28 ?  155 VAL   A CG1  1 
ATOM   3364 C CG1  B VAL   A 1 155 ? 9.890  -3.345  3.449   0.52 17.21 ?  155 VAL   A CG1  1 
ATOM   3365 C CG2  A VAL   A 1 155 ? 11.355 -5.311  4.343   0.48 16.47 ?  155 VAL   A CG2  1 
ATOM   3366 C CG2  B VAL   A 1 155 ? 11.377 -5.204  4.246   0.52 17.28 ?  155 VAL   A CG2  1 
ATOM   3367 H H    A VAL   A 1 155 ? 11.617 -3.731  7.055   0.48 17.40 ?  155 VAL   A H    1 
ATOM   3368 H H    B VAL   A 1 155 ? 11.619 -3.683  7.077   0.52 18.06 ?  155 VAL   A H    1 
ATOM   3369 H HA   A VAL   A 1 155 ? 12.219 -2.757  4.585   0.48 17.88 ?  155 VAL   A HA   1 
ATOM   3370 H HA   B VAL   A 1 155 ? 12.230 -2.693  4.617   0.52 19.18 ?  155 VAL   A HA   1 
ATOM   3371 H HB   A VAL   A 1 155 ? 9.896  -4.228  5.280   0.48 18.28 ?  155 VAL   A HB   1 
ATOM   3372 H HB   B VAL   A 1 155 ? 9.929  -4.204  5.297   0.52 19.59 ?  155 VAL   A HB   1 
ATOM   3373 H HG11 A VAL   A 1 155 ? 9.461  -4.215  2.940   0.48 19.54 ?  155 VAL   A HG11 1 
ATOM   3374 H HG11 B VAL   A 1 155 ? 9.475  -4.056  2.939   0.52 20.66 ?  155 VAL   A HG11 1 
ATOM   3375 H HG12 A VAL   A 1 155 ? 9.306  -2.790  3.621   0.48 19.54 ?  155 VAL   A HG12 1 
ATOM   3376 H HG12 B VAL   A 1 155 ? 9.214  -2.725  3.763   0.52 20.66 ?  155 VAL   A HG12 1 
ATOM   3377 H HG13 A VAL   A 1 155 ? 10.616 -3.136  2.789   0.48 19.54 ?  155 VAL   A HG13 1 
ATOM   3378 H HG13 B VAL   A 1 155 ? 10.540 -2.880  2.901   0.52 20.66 ?  155 VAL   A HG13 1 
ATOM   3379 H HG21 A VAL   A 1 155 ? 10.761 -5.933  3.893   0.48 19.78 ?  155 VAL   A HG21 1 
ATOM   3380 H HG21 B VAL   A 1 155 ? 10.772 -5.826  3.810   0.52 20.74 ?  155 VAL   A HG21 1 
ATOM   3381 H HG22 A VAL   A 1 155 ? 12.113 -5.107  3.773   0.48 19.78 ?  155 VAL   A HG22 1 
ATOM   3382 H HG22 B VAL   A 1 155 ? 12.090 -4.956  3.637   0.52 20.74 ?  155 VAL   A HG22 1 
ATOM   3383 H HG23 A VAL   A 1 155 ? 11.663 -5.696  5.179   0.48 19.78 ?  155 VAL   A HG23 1 
ATOM   3384 H HG23 B VAL   A 1 155 ? 11.750 -5.613  5.044   0.52 20.74 ?  155 VAL   A HG23 1 
ATOM   3385 N N    A PHE   A 1 156 ? 11.252 -0.554  5.060   0.48 15.58 ?  156 PHE   A N    1 
ATOM   3386 N N    B PHE   A 1 156 ? 11.205 -0.514  5.039   0.52 17.57 ?  156 PHE   A N    1 
ATOM   3387 C CA   A PHE   A 1 156 ? 10.711 0.753   5.440   0.48 16.45 ?  156 PHE   A CA   1 
ATOM   3388 C CA   B PHE   A 1 156 ? 10.640 0.792   5.384   0.52 19.19 ?  156 PHE   A CA   1 
ATOM   3389 C C    A PHE   A 1 156 ? 9.248  0.898   5.041   0.48 16.98 ?  156 PHE   A C    1 
ATOM   3390 C C    B PHE   A 1 156 ? 9.198  0.919   4.900   0.52 20.03 ?  156 PHE   A C    1 
ATOM   3391 O O    A PHE   A 1 156 ? 8.447  1.488   5.778   0.48 17.84 ?  156 PHE   A O    1 
ATOM   3392 O O    B PHE   A 1 156 ? 8.319  1.378   5.641   0.52 20.79 ?  156 PHE   A O    1 
ATOM   3393 C CB   A PHE   A 1 156 ? 11.550 1.851   4.773   0.48 16.91 ?  156 PHE   A CB   1 
ATOM   3394 C CB   B PHE   A 1 156 ? 11.521 1.885   4.764   0.52 20.41 ?  156 PHE   A CB   1 
ATOM   3395 C CG   A PHE   A 1 156 ? 11.117 3.260   5.108   0.48 18.05 ?  156 PHE   A CG   1 
ATOM   3396 C CG   B PHE   A 1 156 ? 11.128 3.300   5.130   0.52 21.78 ?  156 PHE   A CG   1 
ATOM   3397 C CD1  A PHE   A 1 156 ? 11.024 3.671   6.426   0.48 19.22 ?  156 PHE   A CD1  1 
ATOM   3398 C CD1  B PHE   A 1 156 ? 11.580 3.875   6.308   0.52 22.56 ?  156 PHE   A CD1  1 
ATOM   3399 C CD2  A PHE   A 1 156 ? 10.846 4.177   4.102   0.48 18.52 ?  156 PHE   A CD2  1 
ATOM   3400 C CD2  B PHE   A 1 156 ? 10.358 4.067   4.270   0.52 22.56 ?  156 PHE   A CD2  1 
ATOM   3401 C CE1  A PHE   A 1 156 ? 10.642 4.962   6.738   0.48 20.50 ?  156 PHE   A CE1  1 
ATOM   3402 C CE1  B PHE   A 1 156 ? 11.243 5.178   6.638   0.52 23.02 ?  156 PHE   A CE1  1 
ATOM   3403 C CE2  A PHE   A 1 156 ? 10.466 5.475   4.408   0.48 19.43 ?  156 PHE   A CE2  1 
ATOM   3404 C CE2  B PHE   A 1 156 ? 10.014 5.370   4.596   0.52 23.02 ?  156 PHE   A CE2  1 
ATOM   3405 C CZ   A PHE   A 1 156 ? 10.370 5.868   5.729   0.48 20.48 ?  156 PHE   A CZ   1 
ATOM   3406 C CZ   B PHE   A 1 156 ? 10.464 5.926   5.782   0.52 23.27 ?  156 PHE   A CZ   1 
ATOM   3407 H H    A PHE   A 1 156 ? 11.878 -0.525  4.470   0.48 18.71 ?  156 PHE   A H    1 
ATOM   3408 H H    B PHE   A 1 156 ? 11.809 -0.490  4.422   0.52 21.10 ?  156 PHE   A H    1 
ATOM   3409 H HA   A PHE   A 1 156 ? 10.785 0.861   6.399   0.48 19.75 ?  156 PHE   A HA   1 
ATOM   3410 H HA   B PHE   A 1 156 ? 10.657 0.901   6.347   0.52 23.03 ?  156 PHE   A HA   1 
ATOM   3411 H HB2  A PHE   A 1 156 ? 12.479 1.749   5.052   0.48 20.30 ?  156 PHE   A HB2  1 
ATOM   3412 H HB2  B PHE   A 1 156 ? 12.440 1.749   5.058   0.52 24.50 ?  156 PHE   A HB2  1 
ATOM   3413 H HB3  A PHE   A 1 156 ? 11.495 1.743   3.808   0.48 20.30 ?  156 PHE   A HB3  1 
ATOM   3414 H HB3  B PHE   A 1 156 ? 11.479 1.807   3.798   0.52 24.50 ?  156 PHE   A HB3  1 
ATOM   3415 H HD1  A PHE   A 1 156 ? 11.214 3.062   7.107   0.48 23.07 ?  156 PHE   A HD1  1 
ATOM   3416 H HD1  B PHE   A 1 156 ? 12.107 3.373   6.890   0.52 27.08 ?  156 PHE   A HD1  1 
ATOM   3417 H HD2  A PHE   A 1 156 ? 10.914 3.917   3.210   0.48 22.24 ?  156 PHE   A HD2  1 
ATOM   3418 H HD2  B PHE   A 1 156 ? 10.055 3.700   3.471   0.52 27.09 ?  156 PHE   A HD2  1 
ATOM   3419 H HE1  A PHE   A 1 156 ? 10.579 5.219   7.628   0.48 24.61 ?  156 PHE   A HE1  1 
ATOM   3420 H HE1  B PHE   A 1 156 ? 11.543 5.547   7.437   0.52 27.63 ?  156 PHE   A HE1  1 
ATOM   3421 H HE2  A PHE   A 1 156 ? 10.279 6.079   3.726   0.48 23.32 ?  156 PHE   A HE2  1 
ATOM   3422 H HE2  B PHE   A 1 156 ? 9.489  5.874   4.015   0.52 27.63 ?  156 PHE   A HE2  1 
ATOM   3423 H HZ   A PHE   A 1 156 ? 10.109 6.733   5.940   0.48 24.58 ?  156 PHE   A HZ   1 
ATOM   3424 H HZ   B PHE   A 1 156 ? 10.234 6.800   6.004   0.52 27.93 ?  156 PHE   A HZ   1 
ATOM   3425 N N    A ASP   A 1 157 ? 8.887  0.386   3.871   0.48 16.54 ?  157 ASP   A N    1 
ATOM   3426 N N    B ASP   A 1 157 ? 8.943  0.530   3.655   0.52 19.87 ?  157 ASP   A N    1 
ATOM   3427 C CA   A ASP   A 1 157 ? 7.591  0.650   3.264   0.48 17.51 ?  157 ASP   A CA   1 
ATOM   3428 C CA   B ASP   A 1 157 ? 7.637  0.732   3.040   0.52 20.84 ?  157 ASP   A CA   1 
ATOM   3429 C C    A ASP   A 1 157 ? 6.592  -0.411  3.714   0.48 18.04 ?  157 ASP   A C    1 
ATOM   3430 C C    B ASP   A 1 157 ? 6.624  -0.216  3.668   0.52 20.94 ?  157 ASP   A C    1 
ATOM   3431 O O    A ASP   A 1 157 ? 6.753  -1.598  3.400   0.48 17.67 ?  157 ASP   A O    1 
ATOM   3432 O O    B ASP   A 1 157 ? 6.790  -1.440  3.608   0.52 20.84 ?  157 ASP   A O    1 
ATOM   3433 C CB   A ASP   A 1 157 ? 7.752  0.647   1.746   0.48 18.35 ?  157 ASP   A CB   1 
ATOM   3434 C CB   B ASP   A 1 157 ? 7.748  0.462   1.544   0.52 21.72 ?  157 ASP   A CB   1 
ATOM   3435 C CG   A ASP   A 1 157 ? 6.553  1.184   1.031   0.48 19.43 ?  157 ASP   A CG   1 
ATOM   3436 C CG   B ASP   A 1 157 ? 6.545  0.959   0.768   0.52 22.74 ?  157 ASP   A CG   1 
ATOM   3437 O OD1  A ASP   A 1 157 ? 5.553  0.441   0.951   0.48 19.02 ?  157 ASP   A OD1  1 
ATOM   3438 O OD1  B ASP   A 1 157 ? 6.400  2.190   0.610   0.52 24.48 ?  157 ASP   A OD1  1 
ATOM   3439 O OD2  A ASP   A 1 157 ? 6.603  2.340   0.556   0.48 21.16 -1 157 ASP   A OD2  1 
ATOM   3440 O OD2  B ASP   A 1 157 ? 5.736  0.120   0.318   0.52 22.22 -1 157 ASP   A OD2  1 
ATOM   3441 H H    A ASP   A 1 157 ? 9.391  -0.134  3.403   0.48 19.86 ?  157 ASP   A H    1 
ATOM   3442 H H    B ASP   A 1 157 ? 9.513  0.139   3.144   0.52 23.86 ?  157 ASP   A H    1 
ATOM   3443 H HA   A ASP   A 1 157 ? 7.273  1.518   3.550   0.48 21.02 ?  157 ASP   A HA   1 
ATOM   3444 H HA   B ASP   A 1 157 ? 7.345  1.651   3.169   0.52 25.01 ?  157 ASP   A HA   1 
ATOM   3445 H HB2  A ASP   A 1 157 ? 8.509  1.193   1.507   0.48 22.03 ?  157 ASP   A HB2  1 
ATOM   3446 H HB2  B ASP   A 1 157 ? 8.540  0.898   1.211   0.52 26.07 ?  157 ASP   A HB2  1 
ATOM   3447 H HB3  A ASP   A 1 157 ? 7.881  -0.265  1.446   0.48 22.03 ?  157 ASP   A HB3  1 
ATOM   3448 H HB3  B ASP   A 1 157 ? 7.828  -0.490  1.404   0.52 26.07 ?  157 ASP   A HB3  1 
ATOM   3449 N N    A LYS   A 1 158 ? 5.564  0.019   4.453   0.48 19.17 ?  158 LYS   A N    1 
ATOM   3450 N N    B LYS   A 1 158 ? 5.572  0.347   4.264   0.52 21.83 ?  158 LYS   A N    1 
ATOM   3451 C CA   A LYS   A 1 158 ? 4.592  -0.922  5.003   0.48 20.11 ?  158 LYS   A CA   1 
ATOM   3452 C CA   B LYS   A 1 158 ? 4.542  -0.486  4.875   0.52 23.21 ?  158 LYS   A CA   1 
ATOM   3453 C C    A LYS   A 1 158 ? 3.857  -1.663  3.893   0.48 20.04 ?  158 LYS   A C    1 
ATOM   3454 C C    B LYS   A 1 158 ? 3.898  -1.393  3.835   0.52 22.83 ?  158 LYS   A C    1 
ATOM   3455 O O    A LYS   A 1 158 ? 3.645  -2.879  3.978   0.48 20.20 ?  158 LYS   A O    1 
ATOM   3456 O O    B LYS   A 1 158 ? 3.729  -2.598  4.055   0.52 23.19 ?  158 LYS   A O    1 
ATOM   3457 C CB   A LYS   A 1 158 ? 3.616  -0.168  5.909   0.48 21.09 ?  158 LYS   A CB   1 
ATOM   3458 C CB   B LYS   A 1 158 ? 3.500  0.404   5.562   0.52 25.33 ?  158 LYS   A CB   1 
ATOM   3459 C CG   A LYS   A 1 158 ? 2.411  -0.969  6.367   0.48 22.02 ?  158 LYS   A CG   1 
ATOM   3460 C CG   B LYS   A 1 158 ? 2.039  -0.019  5.384   0.52 27.64 ?  158 LYS   A CG   1 
ATOM   3461 C CD   A LYS   A 1 158 ? 2.808  -2.219  7.149   0.48 23.29 ?  158 LYS   A CD   1 
ATOM   3462 C CD   B LYS   A 1 158 ? 1.526  -0.860  6.531   0.52 29.43 ?  158 LYS   A CD   1 
ATOM   3463 C CE   A LYS   A 1 158 ? 1.569  -2.920  7.699   0.48 23.86 ?  158 LYS   A CE   1 
ATOM   3464 C CE   B LYS   A 1 158 ? 0.071  -1.236  6.290   0.52 30.57 ?  158 LYS   A CE   1 
ATOM   3465 N NZ   A LYS   A 1 158 ? 1.868  -4.246  8.313   0.48 24.03 ?  158 LYS   A NZ   1 
ATOM   3466 N NZ   B LYS   A 1 158 ? -0.753 -1.140  7.519   0.52 31.65 ?  158 LYS   A NZ   1 
ATOM   3467 H H    A LYS   A 1 158 ? 5.415  0.838   4.646   0.48 23.01 ?  158 LYS   A H    1 
ATOM   3468 H H    B LYS   A 1 158 ? 5.433  1.194   4.318   0.52 26.21 ?  158 LYS   A H    1 
ATOM   3469 H HA   A LYS   A 1 158 ? 5.058  -1.580  5.547   0.48 24.14 ?  158 LYS   A HA   1 
ATOM   3470 H HA   B LYS   A 1 158 ? 4.946  -1.048  5.550   0.52 27.86 ?  158 LYS   A HA   1 
ATOM   3471 H HB2  A LYS   A 1 158 ? 4.093  0.121   6.704   0.48 25.31 ?  158 LYS   A HB2  1 
ATOM   3472 H HB2  B LYS   A 1 158 ? 3.682  0.417   6.521   0.52 30.40 ?  158 LYS   A HB2  1 
ATOM   3473 H HB3  A LYS   A 1 158 ? 3.287  0.607   5.429   0.48 25.31 ?  158 LYS   A HB3  1 
ATOM   3474 H HB3  B LYS   A 1 158 ? 3.580  1.310   5.216   0.52 30.40 ?  158 LYS   A HB3  1 
ATOM   3475 H HG2  A LYS   A 1 158 ? 1.871  -0.414  6.948   0.48 26.43 ?  158 LYS   A HG2  1 
ATOM   3476 H HG2  B LYS   A 1 158 ? 1.520  0.786   5.378   0.52 33.18 ?  158 LYS   A HG2  1 
ATOM   3477 H HG3  A LYS   A 1 158 ? 1.892  -1.244  5.596   0.48 26.43 ?  158 LYS   A HG3  1 
ATOM   3478 H HG3  B LYS   A 1 158 ? 1.870  -0.491  4.553   0.52 33.18 ?  158 LYS   A HG3  1 
ATOM   3479 H HD2  A LYS   A 1 158 ? 3.273  -2.834  6.560   0.48 27.96 ?  158 LYS   A HD2  1 
ATOM   3480 H HD2  B LYS   A 1 158 ? 2.049  -1.674  6.605   0.52 35.33 ?  158 LYS   A HD2  1 
ATOM   3481 H HD3  A LYS   A 1 158 ? 3.378  -1.966  7.892   0.48 27.96 ?  158 LYS   A HD3  1 
ATOM   3482 H HD3  B LYS   A 1 158 ? 1.582  -0.345  7.352   0.52 35.33 ?  158 LYS   A HD3  1 
ATOM   3483 H HE2  A LYS   A 1 158 ? 1.157  -2.360  8.372   0.48 28.64 ?  158 LYS   A HE2  1 
ATOM   3484 H HE2  B LYS   A 1 158 ? -0.305 -0.636  5.626   0.52 36.69 ?  158 LYS   A HE2  1 
ATOM   3485 H HE3  A LYS   A 1 158 ? 0.951  -3.068  6.973   0.48 28.64 ?  158 LYS   A HE3  1 
ATOM   3486 H HE3  B LYS   A 1 158 ? 0.030  -2.150  5.971   0.52 36.69 ?  158 LYS   A HE3  1 
ATOM   3487 H HZ1  A LYS   A 1 158 ? 1.120  -4.616  8.620   0.48 28.85 ?  158 LYS   A HZ1  1 
ATOM   3488 H HZ1  B LYS   A 1 158 ? -1.243 -1.877  7.618   0.52 37.99 ?  158 LYS   A HZ1  1 
ATOM   3489 H HZ2  A LYS   A 1 158 ? 2.229  -4.789  7.704   0.48 28.85 ?  158 LYS   A HZ2  1 
ATOM   3490 H HZ2  B LYS   A 1 158 ? -0.225 -1.045  8.229   0.52 37.99 ?  158 LYS   A HZ2  1 
ATOM   3491 H HZ3  A LYS   A 1 158 ? 2.442  -4.151  8.988   0.48 28.85 ?  158 LYS   A HZ3  1 
ATOM   3492 H HZ3  B LYS   A 1 158 ? -1.296 -0.436  7.469   0.52 37.99 ?  158 LYS   A HZ3  1 
ATOM   3493 N N    A ASN   A 1 159 ? 3.471  -0.953  2.836   0.48 20.71 ?  159 ASN   A N    1 
ATOM   3494 N N    B ASN   A 1 159 ? 3.512  -0.824  2.695   0.52 22.98 ?  159 ASN   A N    1 
ATOM   3495 C CA   A ASN   A 1 159 ? 2.810  -1.620  1.721   0.48 20.97 ?  159 ASN   A CA   1 
ATOM   3496 C CA   B ASN   A 1 159 ? 2.803  -1.618  1.701   0.52 22.89 ?  159 ASN   A CA   1 
ATOM   3497 C C    A ASN   A 1 159 ? 3.712  -2.687  1.110   0.48 20.58 ?  159 ASN   A C    1 
ATOM   3498 C C    B ASN   A 1 159 ? 3.707  -2.676  1.082   0.52 21.57 ?  159 ASN   A C    1 
ATOM   3499 O O    A ASN   A 1 159 ? 3.267  -3.806  0.830   0.48 19.77 ?  159 ASN   A O    1 
ATOM   3500 O O    B ASN   A 1 159 ? 3.248  -3.779  0.767   0.52 20.82 ?  159 ASN   A O    1 
ATOM   3501 C CB   A ASN   A 1 159 ? 2.366  -0.587  0.684   0.48 22.19 ?  159 ASN   A CB   1 
ATOM   3502 C CB   B ASN   A 1 159 ? 2.194  -0.702  0.642   0.52 24.66 ?  159 ASN   A CB   1 
ATOM   3503 C CG   A ASN   A 1 159 ? 1.134  0.193   1.126   0.48 24.10 ?  159 ASN   A CG   1 
ATOM   3504 C CG   B ASN   A 1 159 ? 0.984  0.063   1.159   0.52 26.77 ?  159 ASN   A CG   1 
ATOM   3505 O OD1  A ASN   A 1 159 ? 0.285  -0.329  1.845   0.48 25.28 ?  159 ASN   A OD1  1 
ATOM   3506 O OD1  B ASN   A 1 159 ? 0.180  -0.473  1.923   0.52 28.00 ?  159 ASN   A OD1  1 
ATOM   3507 N ND2  A ASN   A 1 159 ? 1.032  1.444   0.695   0.48 25.04 ?  159 ASN   A ND2  1 
ATOM   3508 N ND2  B ASN   A 1 159 ? 0.849  1.320   0.745   0.52 27.59 ?  159 ASN   A ND2  1 
ATOM   3509 H H    A ASN   A 1 159 ? 3.577  -0.104  2.748   0.48 24.85 ?  159 ASN   A H    1 
ATOM   3510 H H    B ASN   A 1 159 ? 3.649  -0.001  2.480   0.52 27.58 ?  159 ASN   A H    1 
ATOM   3511 H HA   A ASN   A 1 159 ? 2.015  -2.062  2.053   0.48 25.17 ?  159 ASN   A HA   1 
ATOM   3512 H HA   B ASN   A 1 159 ? 2.072  -2.079  2.138   0.52 27.47 ?  159 ASN   A HA   1 
ATOM   3513 H HB2  A ASN   A 1 159 ? 3.079  0.050   0.539   0.48 26.63 ?  159 ASN   A HB2  1 
ATOM   3514 H HB2  B ASN   A 1 159 ? 2.854  -0.056  0.349   0.52 29.60 ?  159 ASN   A HB2  1 
ATOM   3515 H HB3  A ASN   A 1 159 ? 2.148  -1.042  -0.143  0.48 26.63 ?  159 ASN   A HB3  1 
ATOM   3516 H HB3  B ASN   A 1 159 ? 1.903  -1.250  -0.098  0.52 29.60 ?  159 ASN   A HB3  1 
ATOM   3517 H HD21 A ASN   A 1 159 ? 0.352  1.920   0.919   0.48 30.05 ?  159 ASN   A HD21 1 
ATOM   3518 H HD21 B ASN   A 1 159 ? 0.183  1.794   1.012   0.52 33.11 ?  159 ASN   A HD21 1 
ATOM   3519 H HD22 A ASN   A 1 159 ? 1.643  1.778   0.197   0.48 30.05 ?  159 ASN   A HD22 1 
ATOM   3520 H HD22 B ASN   A 1 159 ? 1.432  1.660   0.212   0.52 33.11 ?  159 ASN   A HD22 1 
ATOM   3521 N N    . LEU   A 1 160 ? 4.994  -2.381  0.930   1.00 20.13 ?  160 LEU   A N    1 
ATOM   3522 C CA   . LEU   A 1 160 ? 5.902  -3.400  0.416   1.00 19.51 ?  160 LEU   A CA   1 
ATOM   3523 C C    . LEU   A 1 160 ? 6.069  -4.544  1.409   1.00 18.55 ?  160 LEU   A C    1 
ATOM   3524 O O    . LEU   A 1 160 ? 6.094  -5.717  1.016   1.00 18.72 ?  160 LEU   A O    1 
ATOM   3525 C CB   . LEU   A 1 160 ? 7.253  -2.789  0.072   1.00 18.88 ?  160 LEU   A CB   1 
ATOM   3526 C CG   . LEU   A 1 160 ? 8.313  -3.809  -0.340  1.00 19.62 ?  160 LEU   A CG   1 
ATOM   3527 C CD1  . LEU   A 1 160 ? 7.855  -4.584  -1.558  1.00 20.39 ?  160 LEU   A CD1  1 
ATOM   3528 C CD2  . LEU   A 1 160 ? 9.623  -3.113  -0.602  1.00 19.90 ?  160 LEU   A CD2  1 
ATOM   3529 H H    A LEU   A 1 160 ? 5.354  -1.611  1.104   0.48 24.17 ?  160 LEU   A H    1 
ATOM   3530 H H    B LEU   A 1 160 ? 5.358  -1.617  1.120   0.52 24.17 ?  160 LEU   A H    1 
ATOM   3531 H HA   . LEU   A 1 160 ? 5.525  -3.752  -0.397  1.00 23.42 ?  160 LEU   A HA   1 
ATOM   3532 H HB2  . LEU   A 1 160 ? 7.150  -2.129  -0.652  1.00 22.66 ?  160 LEU   A HB2  1 
ATOM   3533 H HB3  . LEU   A 1 160 ? 7.593  -2.350  0.862   1.00 22.66 ?  160 LEU   A HB3  1 
ATOM   3534 H HG   . LEU   A 1 160 ? 8.448  -4.429  0.389   1.00 23.56 ?  160 LEU   A HG   1 
ATOM   3535 H HD11 . LEU   A 1 160 ? 8.567  -5.167  -1.839  1.00 24.48 ?  160 LEU   A HD11 1 
ATOM   3536 H HD12 . LEU   A 1 160 ? 7.069  -5.108  -1.322  1.00 24.48 ?  160 LEU   A HD12 1 
ATOM   3537 H HD13 . LEU   A 1 160 ? 7.630  -3.958  -2.265  1.00 24.48 ?  160 LEU   A HD13 1 
ATOM   3538 H HD21 . LEU   A 1 160 ? 10.280 -3.776  -0.856  1.00 23.89 ?  160 LEU   A HD21 1 
ATOM   3539 H HD22 . LEU   A 1 160 ? 9.502  -2.471  -1.319  1.00 23.89 ?  160 LEU   A HD22 1 
ATOM   3540 H HD23 . LEU   A 1 160 ? 9.905  -2.656  0.206   1.00 23.89 ?  160 LEU   A HD23 1 
ATOM   3541 N N    A TYR   A 1 161 ? 6.165  -4.237  2.701   0.48 17.69 ?  161 TYR   A N    1 
ATOM   3542 N N    B TYR   A 1 161 ? 6.223  -4.211  2.694   0.52 17.77 ?  161 TYR   A N    1 
ATOM   3543 C CA   A TYR   A 1 161 ? 6.309  -5.298  3.692   0.48 17.18 ?  161 TYR   A CA   1 
ATOM   3544 C CA   B TYR   A 1 161 ? 6.298  -5.228  3.736   0.52 17.50 ?  161 TYR   A CA   1 
ATOM   3545 C C    A TYR   A 1 161 ? 5.181  -6.319  3.578   0.48 17.65 ?  161 TYR   A C    1 
ATOM   3546 C C    B TYR   A 1 161 ? 5.121  -6.188  3.647   0.52 18.36 ?  161 TYR   A C    1 
ATOM   3547 O O    A TYR   A 1 161 ? 5.421  -7.532  3.552   0.48 17.19 ?  161 TYR   A O    1 
ATOM   3548 O O    B TYR   A 1 161 ? 5.293  -7.413  3.666   0.52 17.57 ?  161 TYR   A O    1 
ATOM   3549 C CB   A TYR   A 1 161 ? 6.350  -4.704  5.095   0.48 17.07 ?  161 TYR   A CB   1 
ATOM   3550 C CB   B TYR   A 1 161 ? 6.320  -4.553  5.105   0.52 17.09 ?  161 TYR   A CB   1 
ATOM   3551 C CG   A TYR   A 1 161 ? 6.270  -5.761  6.161   0.48 16.58 ?  161 TYR   A CG   1 
ATOM   3552 C CG   B TYR   A 1 161 ? 6.273  -5.530  6.256   0.52 16.33 ?  161 TYR   A CG   1 
ATOM   3553 C CD1  A TYR   A 1 161 ? 7.407  -6.446  6.566   0.48 16.39 ?  161 TYR   A CD1  1 
ATOM   3554 C CD1  B TYR   A 1 161 ? 7.404  -6.242  6.636   0.52 16.13 ?  161 TYR   A CD1  1 
ATOM   3555 C CD2  A TYR   A 1 161 ? 5.056  -6.087  6.754   0.48 16.65 ?  161 TYR   A CD2  1 
ATOM   3556 C CD2  B TYR   A 1 161 ? 5.100  -5.723  6.980   0.52 15.95 ?  161 TYR   A CD2  1 
ATOM   3557 C CE1  A TYR   A 1 161 ? 7.340  -7.420  7.528   0.48 16.20 ?  161 TYR   A CE1  1 
ATOM   3558 C CE1  B TYR   A 1 161 ? 7.367  -7.129  7.690   0.52 16.22 ?  161 TYR   A CE1  1 
ATOM   3559 C CE2  A TYR   A 1 161 ? 4.982  -7.058  7.720   0.48 16.21 ?  161 TYR   A CE2  1 
ATOM   3560 C CE2  B TYR   A 1 161 ? 5.056  -6.611  8.037   0.52 15.54 ?  161 TYR   A CE2  1 
ATOM   3561 C CZ   A TYR   A 1 161 ? 6.127  -7.722  8.103   0.48 16.14 ?  161 TYR   A CZ   1 
ATOM   3562 C CZ   B TYR   A 1 161 ? 6.191  -7.309  8.388   0.52 15.98 ?  161 TYR   A CZ   1 
ATOM   3563 O OH   A TYR   A 1 161 ? 6.073  -8.695  9.067   0.48 16.20 ?  161 TYR   A OH   1 
ATOM   3564 O OH   B TYR   A 1 161 ? 6.161  -8.199  9.441   0.52 16.95 ?  161 TYR   A OH   1 
ATOM   3565 H H    A TYR   A 1 161 ? 6.142  -3.438  3.025   0.48 21.24 ?  161 TYR   A H    1 
ATOM   3566 H H    B TYR   A 1 161 ? 6.282  -3.398  2.983   0.52 21.33 ?  161 TYR   A H    1 
ATOM   3567 H HA   A TYR   A 1 161 ? 7.143  -5.760  3.538   0.48 20.63 ?  161 TYR   A HA   1 
ATOM   3568 H HA   B TYR   A 1 161 ? 7.119  -5.727  3.631   0.52 21.01 ?  161 TYR   A HA   1 
ATOM   3569 H HB2  A TYR   A 1 161 ? 7.184  -4.220  5.210   0.48 20.49 ?  161 TYR   A HB2  1 
ATOM   3570 H HB2  B TYR   A 1 161 ? 7.133  -4.029  5.190   0.52 20.52 ?  161 TYR   A HB2  1 
ATOM   3571 H HB3  A TYR   A 1 161 ? 5.598  -4.099  5.209   0.48 20.49 ?  161 TYR   A HB3  1 
ATOM   3572 H HB3  B TYR   A 1 161 ? 5.547  -3.965  5.180   0.52 20.52 ?  161 TYR   A HB3  1 
ATOM   3573 H HD1  A TYR   A 1 161 ? 8.226  -6.241  6.175   0.48 19.68 ?  161 TYR   A HD1  1 
ATOM   3574 H HD1  B TYR   A 1 161 ? 8.197  -6.119  6.167   0.52 19.37 ?  161 TYR   A HD1  1 
ATOM   3575 H HD2  A TYR   A 1 161 ? 4.281  -5.640  6.494   0.48 19.99 ?  161 TYR   A HD2  1 
ATOM   3576 H HD2  B TYR   A 1 161 ? 4.332  -5.249  6.751   0.52 19.14 ?  161 TYR   A HD2  1 
ATOM   3577 H HE1  A TYR   A 1 161 ? 8.110  -7.870  7.791   0.48 19.45 ?  161 TYR   A HE1  1 
ATOM   3578 H HE1  B TYR   A 1 161 ? 8.132  -7.601  7.931   0.52 19.48 ?  161 TYR   A HE1  1 
ATOM   3579 H HE2  A TYR   A 1 161 ? 4.163  -7.271  8.112   0.48 19.46 ?  161 TYR   A HE2  1 
ATOM   3580 H HE2  B TYR   A 1 161 ? 4.267  -6.733  8.517   0.52 18.66 ?  161 TYR   A HE2  1 
ATOM   3581 H HH   A TYR   A 1 161 ? 5.278  -8.787  9.334   0.48 19.45 ?  161 TYR   A HH   1 
ATOM   3582 H HH   B TYR   A 1 161 ? 5.389  -8.213  9.781   0.52 20.35 ?  161 TYR   A HH   1 
ATOM   3583 N N    A ASP   A 1 162 ? 3.935  -5.846  3.531   0.48 18.17 ?  162 ASP   A N    1 
ATOM   3584 N N    B ASP   A 1 162 ? 3.905  -5.644  3.575   0.52 19.41 ?  162 ASP   A N    1 
ATOM   3585 C CA   A ASP   A 1 162 ? 2.803  -6.770  3.501   0.48 18.67 ?  162 ASP   A CA   1 
ATOM   3586 C CA   B ASP   A 1 162 ? 2.730  -6.500  3.446   0.52 20.36 ?  162 ASP   A CA   1 
ATOM   3587 C C    A ASP   A 1 162 ? 2.847  -7.655  2.263   0.48 18.10 ?  162 ASP   A C    1 
ATOM   3588 C C    B ASP   A 1 162 ? 2.791  -7.322  2.168   0.52 19.66 ?  162 ASP   A C    1 
ATOM   3589 O O    A ASP   A 1 162 ? 2.499  -8.842  2.325   0.48 18.51 ?  162 ASP   A O    1 
ATOM   3590 O O    B ASP   A 1 162 ? 2.446  -8.511  2.166   0.52 19.94 ?  162 ASP   A O    1 
ATOM   3591 C CB   A ASP   A 1 162 ? 1.486  -5.994  3.562   0.48 20.18 ?  162 ASP   A CB   1 
ATOM   3592 C CB   B ASP   A 1 162 ? 1.459  -5.655  3.460   0.52 22.21 ?  162 ASP   A CB   1 
ATOM   3593 C CG   A ASP   A 1 162 ? 1.219  -5.399  4.930   0.48 22.16 ?  162 ASP   A CG   1 
ATOM   3594 C CG   B ASP   A 1 162 ? 1.155  -5.070  4.822   0.52 24.07 ?  162 ASP   A CG   1 
ATOM   3595 O OD1  A ASP   A 1 162 ? 1.961  -5.726  5.880   0.48 22.79 ?  162 ASP   A OD1  1 
ATOM   3596 O OD1  B ASP   A 1 162 ? 1.587  -5.656  5.837   0.52 25.09 ?  162 ASP   A OD1  1 
ATOM   3597 O OD2  A ASP   A 1 162 ? 0.248  -4.622  5.059   0.48 23.37 -1 162 ASP   A OD2  1 
ATOM   3598 O OD2  B ASP   A 1 162 ? 0.477  -4.019  4.868   0.52 25.01 -1 162 ASP   A OD2  1 
ATOM   3599 H H    A ASP   A 1 162 ? 3.717  -5.013  3.514   0.48 21.81 ?  162 ASP   A H    1 
ATOM   3600 H H    B ASP   A 1 162 ? 3.737  -4.798  3.609   0.52 23.30 ?  162 ASP   A H    1 
ATOM   3601 H HA   A ASP   A 1 162 ? 2.839  -7.345  4.281   0.48 22.41 ?  162 ASP   A HA   1 
ATOM   3602 H HA   B ASP   A 1 162 ? 2.702  -7.112  4.196   0.52 24.44 ?  162 ASP   A HA   1 
ATOM   3603 H HB2  A ASP   A 1 162 ? 1.499  -5.281  2.905   0.48 24.23 ?  162 ASP   A HB2  1 
ATOM   3604 H HB2  B ASP   A 1 162 ? 1.568  -4.903  2.866   0.52 26.66 ?  162 ASP   A HB2  1 
ATOM   3605 H HB3  A ASP   A 1 162 ? 0.746  -6.595  3.386   0.48 24.23 ?  162 ASP   A HB3  1 
ATOM   3606 H HB3  B ASP   A 1 162 ? 0.714  -6.209  3.170   0.52 26.66 ?  162 ASP   A HB3  1 
ATOM   3607 N N    A LYS   A 1 163 ? 3.269  -7.097  1.128   0.48 18.37 ?  163 LYS   A N    1 
ATOM   3608 N N    B LYS   A 1 163 ? 3.210  -6.702  1.063   0.52 19.69 ?  163 LYS   A N    1 
ATOM   3609 C CA   A LYS   A 1 163 ? 3.372  -7.887  -0.094  0.48 19.09 ?  163 LYS   A CA   1 
ATOM   3610 C CA   B LYS   A 1 163 ? 3.345  -7.449  -0.183  0.52 20.12 ?  163 LYS   A CA   1 
ATOM   3611 C C    A LYS   A 1 163 ? 4.473  -8.941  0.014   0.48 18.83 ?  163 LYS   A C    1 
ATOM   3612 C C    B LYS   A 1 163 ? 4.402  -8.539  -0.059  0.52 18.44 ?  163 LYS   A C    1 
ATOM   3613 O O    A LYS   A 1 163 ? 4.303  -10.079 -0.438  0.48 19.21 ?  163 LYS   A O    1 
ATOM   3614 O O    B LYS   A 1 163 ? 4.236  -9.638  -0.600  0.52 17.66 ?  163 LYS   A O    1 
ATOM   3615 C CB   A LYS   A 1 163 ? 3.613  -6.956  -1.284  0.48 21.33 ?  163 LYS   A CB   1 
ATOM   3616 C CB   B LYS   A 1 163 ? 3.689  -6.503  -1.334  0.52 22.74 ?  163 LYS   A CB   1 
ATOM   3617 C CG   A LYS   A 1 163 ? 3.653  -7.659  -2.628  0.48 24.55 ?  163 LYS   A CG   1 
ATOM   3618 C CG   B LYS   A 1 163 ? 3.870  -7.207  -2.675  0.52 25.92 ?  163 LYS   A CG   1 
ATOM   3619 C CD   A LYS   A 1 163 ? 4.031  -6.700  -3.744  0.48 27.78 ?  163 LYS   A CD   1 
ATOM   3620 C CD   B LYS   A 1 163 ? 4.373  -6.249  -3.743  0.52 29.18 ?  163 LYS   A CD   1 
ATOM   3621 C CE   A LYS   A 1 163 ? 3.931  -7.370  -5.106  0.48 30.09 ?  163 LYS   A CE   1 
ATOM   3622 C CE   B LYS   A 1 163 ? 4.434  -6.913  -5.112  0.52 31.68 ?  163 LYS   A CE   1 
ATOM   3623 N NZ   A LYS   A 1 163 ? 4.617  -6.590  -6.173  0.48 31.37 ?  163 LYS   A NZ   1 
ATOM   3624 N NZ   B LYS   A 1 163 ? 5.054  -6.022  -6.133  0.52 33.20 ?  163 LYS   A NZ   1 
ATOM   3625 H H    A LYS   A 1 163 ? 3.500  -6.268  1.045   0.48 22.05 ?  163 LYS   A H    1 
ATOM   3626 H H    B LYS   A 1 163 ? 3.411  -5.864  1.009   0.52 23.64 ?  163 LYS   A H    1 
ATOM   3627 H HA   A LYS   A 1 163 ? 2.531  -8.343  -0.240  0.48 22.92 ?  163 LYS   A HA   1 
ATOM   3628 H HA   B LYS   A 1 163 ? 2.500  -7.874  -0.383  0.52 24.15 ?  163 LYS   A HA   1 
ATOM   3629 H HB2  A LYS   A 1 163 ? 2.896  -6.298  -1.318  0.48 25.60 ?  163 LYS   A HB2  1 
ATOM   3630 H HB2  B LYS   A 1 163 ? 2.969  -5.858  -1.434  0.52 27.30 ?  163 LYS   A HB2  1 
ATOM   3631 H HB3  A LYS   A 1 163 ? 4.461  -6.503  -1.162  0.48 25.60 ?  163 LYS   A HB3  1 
ATOM   3632 H HB3  B LYS   A 1 163 ? 4.515  -6.041  -1.127  0.52 27.30 ?  163 LYS   A HB3  1 
ATOM   3633 H HG2  A LYS   A 1 163 ? 4.315  -8.366  -2.602  0.48 29.46 ?  163 LYS   A HG2  1 
ATOM   3634 H HG2  B LYS   A 1 163 ? 4.520  -7.921  -2.583  0.52 31.11 ?  163 LYS   A HG2  1 
ATOM   3635 H HG3  A LYS   A 1 163 ? 2.777  -8.024  -2.824  0.48 29.46 ?  163 LYS   A HG3  1 
ATOM   3636 H HG3  B LYS   A 1 163 ? 3.016  -7.567  -2.964  0.52 31.11 ?  163 LYS   A HG3  1 
ATOM   3637 H HD2  A LYS   A 1 163 ? 3.425  -5.941  -3.736  0.48 33.34 ?  163 LYS   A HD2  1 
ATOM   3638 H HD2  B LYS   A 1 163 ? 3.772  -5.492  -3.800  0.52 35.03 ?  163 LYS   A HD2  1 
ATOM   3639 H HD3  A LYS   A 1 163 ? 4.945  -6.399  -3.615  0.48 33.34 ?  163 LYS   A HD3  1 
ATOM   3640 H HD3  B LYS   A 1 163 ? 5.267  -5.954  -3.509  0.52 35.03 ?  163 LYS   A HD3  1 
ATOM   3641 H HE2  A LYS   A 1 163 ? 4.321  -8.256  -5.069  0.48 36.12 ?  163 LYS   A HE2  1 
ATOM   3642 H HE2  B LYS   A 1 163 ? 4.967  -7.720  -5.053  0.52 38.02 ?  163 LYS   A HE2  1 
ATOM   3643 H HE3  A LYS   A 1 163 ? 2.999  -7.439  -5.347  0.48 36.12 ?  163 LYS   A HE3  1 
ATOM   3644 H HE3  B LYS   A 1 163 ? 3.534  -7.130  -5.403  0.52 38.02 ?  163 LYS   A HE3  1 
ATOM   3645 H HZ1  A LYS   A 1 163 ? 4.543  -7.012  -6.953  0.48 37.65 ?  163 LYS   A HZ1  1 
ATOM   3646 H HZ1  B LYS   A 1 163 ? 5.077  -6.433  -6.922  0.52 39.85 ?  163 LYS   A HZ1  1 
ATOM   3647 H HZ2  A LYS   A 1 163 ? 4.247  -5.784  -6.243  0.48 37.65 ?  163 LYS   A HZ2  1 
ATOM   3648 H HZ2  B LYS   A 1 163 ? 4.579  -5.273  -6.211  0.52 39.85 ?  163 LYS   A HZ2  1 
ATOM   3649 H HZ3  A LYS   A 1 163 ? 5.481  -6.495  -5.977  0.48 37.65 ?  163 LYS   A HZ3  1 
ATOM   3650 H HZ3  B LYS   A 1 163 ? 5.885  -5.814  -5.890  0.52 39.85 ?  163 LYS   A HZ3  1 
ATOM   3651 N N    A LEU   A 1 164 ? 5.615  -8.580  0.602   0.48 17.20 ?  164 LEU   A N    1 
ATOM   3652 N N    B LEU   A 1 164 ? 5.500  -8.254  0.645   0.52 17.38 ?  164 LEU   A N    1 
ATOM   3653 C CA   A LEU   A 1 164 ? 6.700  -9.546  0.773   0.48 16.78 ?  164 LEU   A CA   1 
ATOM   3654 C CA   B LEU   A 1 164 ? 6.562  -9.247  0.773   0.52 17.37 ?  164 LEU   A CA   1 
ATOM   3655 C C    A LEU   A 1 164 ? 6.256  -10.720 1.636   0.48 17.31 ?  164 LEU   A C    1 
ATOM   3656 C C    B LEU   A 1 164 ? 6.117  -10.436 1.613   0.52 17.16 ?  164 LEU   A C    1 
ATOM   3657 O O    A LEU   A 1 164 ? 6.552  -11.883 1.331   0.48 17.37 ?  164 LEU   A O    1 
ATOM   3658 O O    B LEU   A 1 164 ? 6.422  -11.587 1.278   0.52 17.56 ?  164 LEU   A O    1 
ATOM   3659 C CB   A LEU   A 1 164 ? 7.901  -8.855  1.413   0.48 16.07 ?  164 LEU   A CB   1 
ATOM   3660 C CB   B LEU   A 1 164 ? 7.803  -8.605  1.380   0.52 17.31 ?  164 LEU   A CB   1 
ATOM   3661 C CG   A LEU   A 1 164 ? 8.667  -7.860  0.546   0.48 16.12 ?  164 LEU   A CG   1 
ATOM   3662 C CG   B LEU   A 1 164 ? 8.589  -7.719  0.420   0.52 17.35 ?  164 LEU   A CG   1 
ATOM   3663 C CD1  A LEU   A 1 164 ? 9.555  -6.983  1.415   0.48 16.23 ?  164 LEU   A CD1  1 
ATOM   3664 C CD1  B LEU   A 1 164 ? 9.607  -6.921  1.200   0.52 17.43 ?  164 LEU   A CD1  1 
ATOM   3665 C CD2  A LEU   A 1 164 ? 9.502  -8.600  -0.487  0.48 16.58 ?  164 LEU   A CD2  1 
ATOM   3666 C CD2  B LEU   A 1 164 ? 9.264  -8.553  -0.665  0.52 17.66 ?  164 LEU   A CD2  1 
ATOM   3667 H H    A LEU   A 1 164 ? 5.788  -7.786  0.901   0.48 20.65 ?  164 LEU   A H    1 
ATOM   3668 H H    B LEU   A 1 164 ? 5.657  -7.500  1.046   0.52 20.86 ?  164 LEU   A H    1 
ATOM   3669 H HA   A LEU   A 1 164 ? 6.971  -9.876  -0.099  0.48 20.14 ?  164 LEU   A HA   1 
ATOM   3670 H HA   B LEU   A 1 164 ? 6.792  -9.570  -0.108  0.52 20.86 ?  164 LEU   A HA   1 
ATOM   3671 H HB2  A LEU   A 1 164 ? 7.598  -8.367  2.193   0.48 19.29 ?  164 LEU   A HB2  1 
ATOM   3672 H HB2  B LEU   A 1 164 ? 7.537  -8.053  2.133   0.52 20.78 ?  164 LEU   A HB2  1 
ATOM   3673 H HB3  A LEU   A 1 164 ? 8.536  -9.534  1.684   0.48 19.29 ?  164 LEU   A HB3  1 
ATOM   3674 H HB3  B LEU   A 1 164 ? 8.400  -9.306  1.684   0.52 20.78 ?  164 LEU   A HB3  1 
ATOM   3675 H HG   A LEU   A 1 164 ? 8.044  -7.282  0.076   0.48 19.35 ?  164 LEU   A HG   1 
ATOM   3676 H HG   B LEU   A 1 164 ? 7.983  -7.096  -0.011  0.52 20.83 ?  164 LEU   A HG   1 
ATOM   3677 H HD11 A LEU   A 1 164 ? 10.048 -6.367  0.851   0.48 19.48 ?  164 LEU   A HD11 1 
ATOM   3678 H HD11 B LEU   A 1 164 ? 10.113 -6.369  0.587   0.52 20.93 ?  164 LEU   A HD11 1 
ATOM   3679 H HD12 A LEU   A 1 164 ? 8.998  -6.489  2.037   0.48 19.48 ?  164 LEU   A HD12 1 
ATOM   3680 H HD12 B LEU   A 1 164 ? 9.141  -6.363  1.844   0.52 20.93 ?  164 LEU   A HD12 1 
ATOM   3681 H HD13 A LEU   A 1 164 ? 10.174 -7.549  1.904   0.48 19.48 ?  164 LEU   A HD13 1 
ATOM   3682 H HD13 B LEU   A 1 164 ? 10.198 -7.535  1.663   0.52 20.93 ?  164 LEU   A HD13 1 
ATOM   3683 H HD21 A LEU   A 1 164 ? 10.006 -7.956  -1.011  0.48 19.90 ?  164 LEU   A HD21 1 
ATOM   3684 H HD21 B LEU   A 1 164 ? 9.881  -7.991  -1.159  0.52 21.19 ?  164 LEU   A HD21 1 
ATOM   3685 H HD22 A LEU   A 1 164 ? 10.111 -9.200  -0.028  0.48 19.90 ?  164 LEU   A HD22 1 
ATOM   3686 H HD22 B LEU   A 1 164 ? 9.748  -9.283  -0.246  0.52 21.19 ?  164 LEU   A HD22 1 
ATOM   3687 H HD23 A LEU   A 1 164 ? 8.910  -9.105  -1.064  0.48 19.90 ?  164 LEU   A HD23 1 
ATOM   3688 H HD23 B LEU   A 1 164 ? 8.587  -8.906  -1.263  0.52 21.19 ?  164 LEU   A HD23 1 
ATOM   3689 N N    A VAL   A 1 165 ? 5.581  -10.426 2.746   0.48 16.67 ?  165 VAL   A N    1 
ATOM   3690 N N    B VAL   A 1 165 ? 5.422  -10.180 2.721   0.52 16.42 ?  165 VAL   A N    1 
ATOM   3691 C CA   A VAL   A 1 165 ? 5.081  -11.486 3.614   0.48 17.33 ?  165 VAL   A CA   1 
ATOM   3692 C CA   B VAL   A 1 165 ? 4.972  -11.273 3.581   0.52 16.71 ?  165 VAL   A CA   1 
ATOM   3693 C C    A VAL   A 1 165 ? 4.004  -12.289 2.900   0.48 17.64 ?  165 VAL   A C    1 
ATOM   3694 C C    B VAL   A 1 165 ? 3.989  -12.166 2.834   0.52 16.50 ?  165 VAL   A C    1 
ATOM   3695 O O    A VAL   A 1 165 ? 4.065  -13.524 2.831   0.48 17.82 ?  165 VAL   A O    1 
ATOM   3696 O O    B VAL   A 1 165 ? 4.129  -13.395 2.811   0.52 16.86 ?  165 VAL   A O    1 
ATOM   3697 C CB   A VAL   A 1 165 ? 4.571  -10.885 4.937   0.48 17.51 ?  165 VAL   A CB   1 
ATOM   3698 C CB   B VAL   A 1 165 ? 4.375  -10.715 4.886   0.52 17.37 ?  165 VAL   A CB   1 
ATOM   3699 C CG1  A VAL   A 1 165 ? 3.776  -11.916 5.727   0.48 18.20 ?  165 VAL   A CG1  1 
ATOM   3700 C CG1  B VAL   A 1 165 ? 3.738  -11.826 5.717   0.52 18.23 ?  165 VAL   A CG1  1 
ATOM   3701 C CG2  A VAL   A 1 165 ? 5.739  -10.343 5.757   0.48 17.70 ?  165 VAL   A CG2  1 
ATOM   3702 C CG2  B VAL   A 1 165 ? 5.448  -9.988  5.687   0.52 17.70 ?  165 VAL   A CG2  1 
ATOM   3703 H H    A VAL   A 1 165 ? 5.408  -9.626  3.013   0.48 20.01 ?  165 VAL   A H    1 
ATOM   3704 H H    B VAL   A 1 165 ? 5.201  -9.394  2.994   0.52 19.71 ?  165 VAL   A H    1 
ATOM   3705 H HA   A VAL   A 1 165 ? 5.815  -12.083 3.827   0.48 20.80 ?  165 VAL   A HA   1 
ATOM   3706 H HA   B VAL   A 1 165 ? 5.739  -11.814 3.823   0.52 20.07 ?  165 VAL   A HA   1 
ATOM   3707 H HB   A VAL   A 1 165 ? 3.985  -10.137 4.741   0.48 21.02 ?  165 VAL   A HB   1 
ATOM   3708 H HB   B VAL   A 1 165 ? 3.686  -10.067 4.672   0.52 20.86 ?  165 VAL   A HB   1 
ATOM   3709 H HG11 A VAL   A 1 165 ? 3.708  -11.625 6.650   0.48 21.85 ?  165 VAL   A HG11 1 
ATOM   3710 H HG11 B VAL   A 1 165 ? 3.600  -11.506 6.624   0.52 21.89 ?  165 VAL   A HG11 1 
ATOM   3711 H HG12 A VAL   A 1 165 ? 2.887  -11.991 5.342   0.48 21.85 ?  165 VAL   A HG12 1 
ATOM   3712 H HG12 B VAL   A 1 165 ? 2.885  -12.067 5.321   0.52 21.89 ?  165 VAL   A HG12 1 
ATOM   3713 H HG13 A VAL   A 1 165 ? 4.232  -12.769 5.683   0.48 21.85 ?  165 VAL   A HG13 1 
ATOM   3714 H HG13 B VAL   A 1 165 ? 4.330  -12.593 5.726   0.52 21.89 ?  165 VAL   A HG13 1 
ATOM   3715 H HG21 A VAL   A 1 165 ? 5.404  -10.003 6.602   0.48 21.25 ?  165 VAL   A HG21 1 
ATOM   3716 H HG21 B VAL   A 1 165 ? 5.054  -9.629  6.497   0.52 21.25 ?  165 VAL   A HG21 1 
ATOM   3717 H HG22 A VAL   A 1 165 ? 6.373  -11.059 5.918   0.48 21.25 ?  165 VAL   A HG22 1 
ATOM   3718 H HG22 B VAL   A 1 165 ? 6.154  -10.614 5.912   0.52 21.25 ?  165 VAL   A HG22 1 
ATOM   3719 H HG23 A VAL   A 1 165 ? 6.170  -9.626  5.262   0.48 21.25 ?  165 VAL   A HG23 1 
ATOM   3720 H HG23 B VAL   A 1 165 ? 5.810  -9.264  5.149   0.52 21.25 ?  165 VAL   A HG23 1 
ATOM   3721 N N    A SER   A 1 166 ? 3.008  -11.598 2.343   0.48 18.03 ?  166 SER   A N    1 
ATOM   3722 N N    B SER   A 1 166 ? 2.993  -11.561 2.191   0.52 16.63 ?  166 SER   A N    1 
ATOM   3723 C CA   A SER   A 1 166 ? 1.888  -12.295 1.722   0.48 18.30 ?  166 SER   A CA   1 
ATOM   3724 C CA   B SER   A 1 166 ? 1.892  -12.345 1.645   0.52 17.31 ?  166 SER   A CA   1 
ATOM   3725 C C    A SER   A 1 166 ? 2.350  -13.188 0.581   0.48 18.74 ?  166 SER   A C    1 
ATOM   3726 C C    B SER   A 1 166 ? 2.289  -13.133 0.407   0.52 17.65 ?  166 SER   A C    1 
ATOM   3727 O O    A SER   A 1 166 ? 1.759  -14.251 0.350   0.48 20.05 ?  166 SER   A O    1 
ATOM   3728 O O    B SER   A 1 166 ? 1.574  -14.072 0.035   0.52 18.87 ?  166 SER   A O    1 
ATOM   3729 C CB   A SER   A 1 166 ? 0.842  -11.291 1.230   0.48 18.97 ?  166 SER   A CB   1 
ATOM   3730 C CB   B SER   A 1 166 ? 0.724  -11.435 1.290   0.52 18.62 ?  166 SER   A CB   1 
ATOM   3731 O OG   A SER   A 1 166 ? 0.137  -10.701 2.311   0.48 19.98 ?  166 SER   A OG   1 
ATOM   3732 O OG   B SER   A 1 166 ? 1.049  -10.641 0.168   0.52 19.99 ?  166 SER   A OG   1 
ATOM   3733 H H    A SER   A 1 166 ? 2.961  -10.738 2.317   0.48 21.64 ?  166 SER   A H    1 
ATOM   3734 H H    B SER   A 1 166 ? 2.931  -10.712 2.065   0.52 19.97 ?  166 SER   A H    1 
ATOM   3735 H HA   A SER   A 1 166 ? 1.465  -12.860 2.385   0.48 21.97 ?  166 SER   A HA   1 
ATOM   3736 H HA   B SER   A 1 166 ? 1.588  -12.975 2.318   0.52 20.78 ?  166 SER   A HA   1 
ATOM   3737 H HB2  A SER   A 1 166 ? 1.282  -10.594 0.720   0.48 22.77 ?  166 SER   A HB2  1 
ATOM   3738 H HB2  B SER   A 1 166 ? -0.052 -11.983 1.081   0.52 22.36 ?  166 SER   A HB2  1 
ATOM   3739 H HB3  A SER   A 1 166 ? 0.197  -11.753 0.674   0.48 22.77 ?  166 SER   A HB3  1 
ATOM   3740 H HB3  B SER   A 1 166 ? 0.527  -10.856 2.043   0.52 22.36 ?  166 SER   A HB3  1 
ATOM   3741 H HG   A SER   A 1 166 ? -0.421 -10.139 2.024   0.48 23.98 ?  166 SER   A HG   1 
ATOM   3742 H HG   B SER   A 1 166 ? 0.399  -10.143 -0.030  0.52 23.99 ?  166 SER   A HG   1 
ATOM   3743 N N    A SER   A 1 167 ? 3.410  -12.795 -0.128  0.48 18.88 ?  167 SER   A N    1 
ATOM   3744 N N    B SER   A 1 167 ? 3.388  -12.769 -0.254  0.52 17.67 ?  167 SER   A N    1 
ATOM   3745 C CA   A SER   A 1 167 ? 3.857  -13.529 -1.304  0.48 19.32 ?  167 SER   A CA   1 
ATOM   3746 C CA   B SER   A 1 167 ? 3.834  -13.488 -1.439  0.52 18.33 ?  167 SER   A CA   1 
ATOM   3747 C C    A SER   A 1 167 ? 5.019  -14.477 -1.026  0.48 19.47 ?  167 SER   A C    1 
ATOM   3748 C C    B SER   A 1 167 ? 4.976  -14.455 -1.152  0.52 18.52 ?  167 SER   A C    1 
ATOM   3749 O O    A SER   A 1 167 ? 5.537  -15.090 -1.966  0.48 20.07 ?  167 SER   A O    1 
ATOM   3750 O O    B SER   A 1 167 ? 5.395  -15.188 -2.054  0.52 19.58 ?  167 SER   A O    1 
ATOM   3751 C CB   A SER   A 1 167 ? 4.249  -12.557 -2.427  0.48 20.22 ?  167 SER   A CB   1 
ATOM   3752 C CB   B SER   A 1 167 ? 4.239  -12.504 -2.546  0.52 18.74 ?  167 SER   A CB   1 
ATOM   3753 O OG   A SER   A 1 167 ? 5.330  -11.726 -2.039  0.48 21.10 ?  167 SER   A OG   1 
ATOM   3754 O OG   B SER   A 1 167 ? 5.354  -11.720 -2.161  0.52 19.30 ?  167 SER   A OG   1 
ATOM   3755 H H    A SER   A 1 167 ? 3.890  -12.097 0.060   0.48 22.67 ?  167 SER   A H    1 
ATOM   3756 H H    B SER   A 1 167 ? 3.891  -12.096 -0.033  0.52 21.21 ?  167 SER   A H    1 
ATOM   3757 H HA   A SER   A 1 167 ? 3.111  -14.049 -1.630  0.48 23.20 ?  167 SER   A HA   1 
ATOM   3758 H HA   B SER   A 1 167 ? 3.090  -14.002 -1.776  0.52 22.00 ?  167 SER   A HA   1 
ATOM   3759 H HB2  A SER   A 1 167 ? 4.517  -13.071 -3.205  0.48 24.27 ?  167 SER   A HB2  1 
ATOM   3760 H HB2  B SER   A 1 167 ? 4.471  -13.006 -3.342  0.52 22.50 ?  167 SER   A HB2  1 
ATOM   3761 H HB3  A SER   A 1 167 ? 3.485  -11.999 -2.650  0.48 24.27 ?  167 SER   A HB3  1 
ATOM   3762 H HB3  B SER   A 1 167 ? 3.490  -11.913 -2.739  0.52 22.50 ?  167 SER   A HB3  1 
ATOM   3763 H HG   A SER   A 1 167 ? 5.118  -11.272 -1.363  0.48 25.33 ?  167 SER   A HG   1 
ATOM   3764 H HG   B SER   A 1 167 ? 5.164  -11.267 -1.476  0.52 23.17 ?  167 SER   A HG   1 
ATOM   3765 N N    A PHE   A 1 168 ? 5.446  -14.618 0.226   0.48 19.17 ?  168 PHE   A N    1 
ATOM   3766 N N    B PHE   A 1 168 ? 5.473  -14.488 0.081   0.52 18.02 ?  168 PHE   A N    1 
ATOM   3767 C CA   A PHE   A 1 168 ? 6.630  -15.421 0.501   0.48 19.72 ?  168 PHE   A CA   1 
ATOM   3768 C CA   B PHE   A 1 168 ? 6.659  -15.275 0.388   0.52 18.80 ?  168 PHE   A CA   1 
ATOM   3769 C C    A PHE   A 1 168 ? 6.315  -16.905 0.382   0.48 21.55 ?  168 PHE   A C    1 
ATOM   3770 C C    B PHE   A 1 168 ? 6.339  -16.763 0.375   0.52 20.12 ?  168 PHE   A C    1 
ATOM   3771 O O    A PHE   A 1 168 ? 5.339  -17.392 0.959   0.48 23.29 ?  168 PHE   A O    1 
ATOM   3772 O O    B PHE   A 1 168 ? 5.399  -17.212 1.036   0.52 21.82 ?  168 PHE   A O    1 
ATOM   3773 C CB   A PHE   A 1 168 ? 7.182  -15.142 1.895   0.48 19.04 ?  168 PHE   A CB   1 
ATOM   3774 C CB   B PHE   A 1 168 ? 7.198  -14.898 1.764   0.52 18.99 ?  168 PHE   A CB   1 
ATOM   3775 C CG   A PHE   A 1 168 ? 8.431  -15.924 2.199   0.48 17.98 ?  168 PHE   A CG   1 
ATOM   3776 C CG   B PHE   A 1 168 ? 8.465  -15.615 2.121   0.52 18.50 ?  168 PHE   A CG   1 
ATOM   3777 C CD1  A PHE   A 1 168 ? 9.611  -15.634 1.535   0.48 17.75 ?  168 PHE   A CD1  1 
ATOM   3778 C CD1  B PHE   A 1 168 ? 9.676  -15.165 1.639   0.52 18.35 ?  168 PHE   A CD1  1 
ATOM   3779 C CD2  A PHE   A 1 168 ? 8.424  -16.961 3.119   0.48 18.20 ?  168 PHE   A CD2  1 
ATOM   3780 C CD2  B PHE   A 1 168 ? 8.446  -16.745 2.918   0.52 18.38 ?  168 PHE   A CD2  1 
ATOM   3781 C CE1  A PHE   A 1 168 ? 10.762 -16.354 1.791   0.48 17.35 ?  168 PHE   A CE1  1 
ATOM   3782 C CE1  B PHE   A 1 168 ? 10.849 -15.825 1.954   0.52 18.47 ?  168 PHE   A CE1  1 
ATOM   3783 C CE2  A PHE   A 1 168 ? 9.577  -17.683 3.382   0.48 18.52 ?  168 PHE   A CE2  1 
ATOM   3784 C CE2  B PHE   A 1 168 ? 9.616  -17.410 3.237   0.52 18.57 ?  168 PHE   A CE2  1 
ATOM   3785 C CZ   A PHE   A 1 168 ? 10.747 -17.377 2.715   0.48 18.02 ?  168 PHE   A CZ   1 
ATOM   3786 C CZ   B PHE   A 1 168 ? 10.819 -16.949 2.753   0.52 18.25 ?  168 PHE   A CZ   1 
ATOM   3787 H H    A PHE   A 1 168 ? 5.081  -14.258 0.918   0.48 23.02 ?  168 PHE   A H    1 
ATOM   3788 H H    B PHE   A 1 168 ? 5.147  -14.057 0.752   0.52 21.63 ?  168 PHE   A H    1 
ATOM   3789 H HA   A PHE   A 1 168 ? 7.318  -15.203 -0.148  0.48 23.68 ?  168 PHE   A HA   1 
ATOM   3790 H HA   B PHE   A 1 168 ? 7.347  -15.093 -0.275  0.52 22.57 ?  168 PHE   A HA   1 
ATOM   3791 H HB2  A PHE   A 1 168 ? 7.396  -14.197 1.965   0.48 22.85 ?  168 PHE   A HB2  1 
ATOM   3792 H HB2  B PHE   A 1 168 ? 7.377  -13.944 1.783   0.52 22.80 ?  168 PHE   A HB2  1 
ATOM   3793 H HB3  A PHE   A 1 168 ? 6.511  -15.378 2.553   0.48 22.85 ?  168 PHE   A HB3  1 
ATOM   3794 H HB3  B PHE   A 1 168 ? 6.531  -15.121 2.432   0.52 22.80 ?  168 PHE   A HB3  1 
ATOM   3795 H HD1  A PHE   A 1 168 ? 9.630  -14.946 0.909   0.48 21.31 ?  168 PHE   A HD1  1 
ATOM   3796 H HD1  B PHE   A 1 168 ? 9.704  -14.406 1.099   0.52 22.03 ?  168 PHE   A HD1  1 
ATOM   3797 H HD2  A PHE   A 1 168 ? 7.635  -17.169 3.569   0.48 21.85 ?  168 PHE   A HD2  1 
ATOM   3798 H HD2  B PHE   A 1 168 ? 7.634  -17.062 3.245   0.52 22.07 ?  168 PHE   A HD2  1 
ATOM   3799 H HE1  A PHE   A 1 168 ? 11.551 -16.148 1.339   0.48 20.83 ?  168 PHE   A HE1  1 
ATOM   3800 H HE1  B PHE   A 1 168 ? 11.661 -15.506 1.625   0.52 22.17 ?  168 PHE   A HE1  1 
ATOM   3801 H HE2  A PHE   A 1 168 ? 9.560  -18.377 4.004   0.48 22.23 ?  168 PHE   A HE2  1 
ATOM   3802 H HE2  B PHE   A 1 168 ? 9.590  -18.168 3.775   0.52 22.29 ?  168 PHE   A HE2  1 
ATOM   3803 H HZ   A PHE   A 1 168 ? 11.525 -17.864 2.886   0.48 21.63 ?  168 PHE   A HZ   1 
ATOM   3804 H HZ   B PHE   A 1 168 ? 11.610 -17.391 2.966   0.52 21.91 ?  168 PHE   A HZ   1 
ATOM   3805 N N    A LEU   A 1 169 ? 7.160  -17.627 -0.346  0.48 23.69 ?  169 LEU   A N    1 
ATOM   3806 N N    B LEU   A 1 169 ? 7.147  -17.533 -0.349  0.52 22.26 ?  169 LEU   A N    1 
ATOM   3807 C CA   A LEU   A 1 169 ? 6.975  -19.063 -0.503  0.48 26.77 ?  169 LEU   A CA   1 
ATOM   3808 C CA   B LEU   A 1 169 ? 6.939  -18.974 -0.432  0.52 25.19 ?  169 LEU   A CA   1 
ATOM   3809 C C    A LEU   A 1 169 ? 7.854  -19.844 0.466   0.48 27.93 ?  169 LEU   A C    1 
ATOM   3810 C C    B LEU   A 1 169 ? 7.740  -19.711 0.639   0.52 25.69 ?  169 LEU   A C    1 
ATOM   3811 O O    A LEU   A 1 169 ? 7.372  -20.324 1.496   0.48 28.56 ?  169 LEU   A O    1 
ATOM   3812 O O    B LEU   A 1 169 ? 7.170  -20.450 1.450   0.52 26.21 ?  169 LEU   A O    1 
ATOM   3813 C CB   A LEU   A 1 169 ? 7.272  -19.483 -1.944  0.48 28.10 ?  169 LEU   A CB   1 
ATOM   3814 C CB   B LEU   A 1 169 ? 7.314  -19.490 -1.825  0.52 27.01 ?  169 LEU   A CB   1 
ATOM   3815 C CG   A LEU   A 1 169 ? 6.957  -20.940 -2.288  0.48 29.49 ?  169 LEU   A CG   1 
ATOM   3816 C CG   B LEU   A 1 169 ? 7.199  -21.001 -2.057  0.52 28.74 ?  169 LEU   A CG   1 
ATOM   3817 C CD1  A LEU   A 1 169 ? 5.535  -21.299 -1.888  0.48 29.92 ?  169 LEU   A CD1  1 
ATOM   3818 C CD1  B LEU   A 1 169 ? 5.858  -21.538 -1.581  0.52 29.36 ?  169 LEU   A CD1  1 
ATOM   3819 C CD2  A LEU   A 1 169 ? 7.170  -21.189 -3.772  0.48 29.99 ?  169 LEU   A CD2  1 
ATOM   3820 C CD2  B LEU   A 1 169 ? 7.406  -21.331 -3.529  0.52 29.30 ?  169 LEU   A CD2  1 
ATOM   3821 O OXT  A LEU   A 1 169 ? 9.055  -20.013 0.246   0.48 28.00 -1 169 LEU   A OXT  1 
ATOM   3822 O OXT  B LEU   A 1 169 ? 8.966  -19.583 0.720   0.52 25.25 -1 169 LEU   A OXT  1 
ATOM   3823 H H    A LEU   A 1 169 ? 7.840  -17.306 -0.762  0.48 28.43 ?  169 LEU   A H    1 
ATOM   3824 H H    B LEU   A 1 169 ? 7.819  -17.240 -0.800  0.52 26.72 ?  169 LEU   A H    1 
ATOM   3825 H HA   A LEU   A 1 169 ? 6.054  -19.280 -0.304  0.48 32.13 ?  169 LEU   A HA   1 
ATOM   3826 H HA   B LEU   A 1 169 ? 6.001  -19.161 -0.284  0.52 30.24 ?  169 LEU   A HA   1 
ATOM   3827 H HB2  A LEU   A 1 169 ? 6.747  -18.926 -2.540  0.48 33.73 ?  169 LEU   A HB2  1 
ATOM   3828 H HB2  B LEU   A 1 169 ? 6.734  -19.059 -2.473  0.52 32.42 ?  169 LEU   A HB2  1 
ATOM   3829 H HB3  A LEU   A 1 169 ? 8.215  -19.343 -2.117  0.48 33.73 ?  169 LEU   A HB3  1 
ATOM   3830 H HB3  B LEU   A 1 169 ? 8.233  -19.244 -2.003  0.52 32.42 ?  169 LEU   A HB3  1 
ATOM   3831 H HG   A LEU   A 1 169 ? 7.562  -21.519 -1.798  0.48 35.39 ?  169 LEU   A HG   1 
ATOM   3832 H HG   B LEU   A 1 169 ? 7.895  -21.452 -1.554  0.52 34.50 ?  169 LEU   A HG   1 
ATOM   3833 H HD11 A LEU   A 1 169 ? 5.293  -22.140 -2.303  0.48 35.91 ?  169 LEU   A HD11 1 
ATOM   3834 H HD11 B LEU   A 1 169 ? 5.774  -22.466 -1.855  0.52 35.24 ?  169 LEU   A HD11 1 
ATOM   3835 H HD12 A LEU   A 1 169 ? 5.490  -21.382 -0.922  0.48 35.91 ?  169 LEU   A HD12 1 
ATOM   3836 H HD12 B LEU   A 1 169 ? 5.818  -21.476 -0.614  0.52 35.24 ?  169 LEU   A HD12 1 
ATOM   3837 H HD13 A LEU   A 1 169 ? 4.936  -20.597 -2.189  0.48 35.91 ?  169 LEU   A HD13 1 
ATOM   3838 H HD13 B LEU   A 1 169 ? 5.148  -21.011 -1.979  0.52 35.24 ?  169 LEU   A HD13 1 
ATOM   3839 H HD21 A LEU   A 1 169 ? 6.973  -22.118 -3.968  0.48 36.00 ?  169 LEU   A HD21 1 
ATOM   3840 H HD21 B LEU   A 1 169 ? 7.332  -22.291 -3.652  0.52 35.16 ?  169 LEU   A HD21 1 
ATOM   3841 H HD22 A LEU   A 1 169 ? 6.577  -20.611 -4.277  0.48 36.00 ?  169 LEU   A HD22 1 
ATOM   3842 H HD22 B LEU   A 1 169 ? 6.725  -20.878 -4.052  0.52 35.16 ?  169 LEU   A HD22 1 
ATOM   3843 H HD23 A LEU   A 1 169 ? 8.093  -20.992 -3.995  0.48 36.00 ?  169 LEU   A HD23 1 
ATOM   3844 H HD23 B LEU   A 1 169 ? 8.286  -21.028 -3.800  0.52 35.16 ?  169 LEU   A HD23 1 
ATOM   3845 N N    A SER   B 1 1   ? 50.796 -9.285  -23.720 0.48 28.62 ?  1   SER   B N    1 
ATOM   3846 N N    B SER   B 1 1   ? 50.590 -9.211  -23.712 0.52 27.27 ?  1   SER   B N    1 
ATOM   3847 C CA   A SER   B 1 1   ? 51.304 -10.344 -22.825 0.48 29.01 ?  1   SER   B CA   1 
ATOM   3848 C CA   B SER   B 1 1   ? 51.085 -10.211 -22.746 0.52 26.99 ?  1   SER   B CA   1 
ATOM   3849 C C    A SER   B 1 1   ? 50.229 -11.390 -22.568 0.48 28.80 ?  1   SER   B C    1 
ATOM   3850 C C    B SER   B 1 1   ? 50.021 -11.265 -22.468 0.52 25.58 ?  1   SER   B C    1 
ATOM   3851 O O    A SER   B 1 1   ? 49.043 -11.173 -22.832 0.48 28.80 ?  1   SER   B O    1 
ATOM   3852 O O    B SER   B 1 1   ? 48.831 -11.092 -22.772 0.52 24.58 ?  1   SER   B O    1 
ATOM   3853 C CB   A SER   B 1 1   ? 51.783 -9.749  -21.503 0.48 29.29 ?  1   SER   B CB   1 
ATOM   3854 C CB   B SER   B 1 1   ? 51.512 -9.542  -21.441 0.52 27.78 ?  1   SER   B CB   1 
ATOM   3855 O OG   A SER   B 1 1   ? 50.695 -9.484  -20.642 0.48 30.82 ?  1   SER   B OG   1 
ATOM   3856 O OG   B SER   B 1 1   ? 50.420 -9.453  -20.545 0.52 29.83 ?  1   SER   B OG   1 
ATOM   3857 H H1   A SER   B 1 1   ? 50.594 -9.643  -24.507 0.48 34.35 ?  1   SER   B H1   1 
ATOM   3858 H H1   B SER   B 1 1   ? 51.258 -8.666  -23.928 0.52 32.74 ?  1   SER   B H1   1 
ATOM   3859 H H2   A SER   B 1 1   ? 50.074 -8.921  -23.358 0.48 34.35 ?  1   SER   B H2   1 
ATOM   3860 H H2   B SER   B 1 1   ? 50.297 -9.631  -24.435 0.52 32.74 ?  1   SER   B H2   1 
ATOM   3861 H H3   A SER   B 1 1   ? 51.428 -8.669  -23.822 0.48 34.35 ?  1   SER   B H3   1 
ATOM   3862 H H3   B SER   B 1 1   ? 49.932 -8.751  -23.338 0.52 32.74 ?  1   SER   B H3   1 
ATOM   3863 H HA   A SER   B 1 1   ? 52.052 -10.774 -23.258 0.48 34.82 ?  1   SER   B HA   1 
ATOM   3864 H HA   B SER   B 1 1   ? 51.859 -10.647 -23.130 0.52 32.40 ?  1   SER   B HA   1 
ATOM   3865 H HB2  A SER   B 1 1   ? 52.376 -10.385 -21.076 0.48 35.16 ?  1   SER   B HB2  1 
ATOM   3866 H HB2  B SER   B 1 1   ? 52.222 -10.068 -21.040 0.52 33.34 ?  1   SER   B HB2  1 
ATOM   3867 H HB3  A SER   B 1 1   ? 52.255 -8.921  -21.682 0.48 35.16 ?  1   SER   B HB3  1 
ATOM   3868 H HB3  B SER   B 1 1   ? 51.832 -8.646  -21.630 0.52 33.34 ?  1   SER   B HB3  1 
ATOM   3869 H HG   A SER   B 1 1   ? 50.967 -9.089  -19.952 0.48 37.00 ?  1   SER   B HG   1 
ATOM   3870 H HG   B SER   B 1 1   ? 50.589 -8.884  -19.951 0.52 35.81 ?  1   SER   B HG   1 
ATOM   3871 N N    A MET   B 1 2   ? 50.665 -12.525 -22.037 0.48 28.59 ?  2   MET   B N    1 
ATOM   3872 N N    B MET   B 1 2   ? 50.472 -12.363 -21.880 0.52 25.40 ?  2   MET   B N    1 
ATOM   3873 C CA   A MET   B 1 2   ? 49.828 -13.703 -21.867 0.48 28.30 ?  2   MET   B CA   1 
ATOM   3874 C CA   B MET   B 1 2   ? 49.665 -13.559 -21.693 0.52 25.48 ?  2   MET   B CA   1 
ATOM   3875 C C    A MET   B 1 2   ? 49.587 -13.916 -20.381 0.48 25.54 ?  2   MET   B C    1 
ATOM   3876 C C    B MET   B 1 2   ? 49.423 -13.739 -20.201 0.52 23.31 ?  2   MET   B C    1 
ATOM   3877 O O    A MET   B 1 2   ? 50.532 -14.163 -19.626 0.48 25.68 ?  2   MET   B O    1 
ATOM   3878 O O    B MET   B 1 2   ? 50.348 -14.068 -19.452 0.52 23.53 ?  2   MET   B O    1 
ATOM   3879 C CB   A MET   B 1 2   ? 50.524 -14.914 -22.478 0.48 31.57 ?  2   MET   B CB   1 
ATOM   3880 C CB   B MET   B 1 2   ? 50.421 -14.746 -22.273 0.52 28.79 ?  2   MET   B CB   1 
ATOM   3881 C CG   A MET   B 1 2   ? 49.675 -16.172 -22.544 0.48 34.56 ?  2   MET   B CG   1 
ATOM   3882 C CG   B MET   B 1 2   ? 49.564 -15.925 -22.713 0.52 31.56 ?  2   MET   B CG   1 
ATOM   3883 S SD   A MET   B 1 2   ? 50.495 -17.473 -23.483 0.48 37.61 ?  2   MET   B SD   1 
ATOM   3884 S SD   B MET   B 1 2   ? 50.505 -17.088 -23.712 0.52 34.42 ?  2   MET   B SD   1 
ATOM   3885 C CE   A MET   B 1 2   ? 51.039 -16.517 -24.898 0.48 37.64 ?  2   MET   B CE   1 
ATOM   3886 C CE   B MET   B 1 2   ? 51.650 -15.985 -24.517 0.52 34.39 ?  2   MET   B CE   1 
ATOM   3887 H H    A MET   B 1 2   ? 51.469 -12.641 -21.754 0.48 34.31 ?  2   MET   B H    1 
ATOM   3888 H H    B MET   B 1 2   ? 51.278 -12.451 -21.581 0.52 30.49 ?  2   MET   B H    1 
ATOM   3889 H HA   A MET   B 1 2   ? 48.982 -13.580 -22.321 0.48 33.97 ?  2   MET   B HA   1 
ATOM   3890 H HA   B MET   B 1 2   ? 48.827 -13.477 -22.173 0.52 30.58 ?  2   MET   B HA   1 
ATOM   3891 H HB2  A MET   B 1 2   ? 50.779 -14.657 -23.375 0.48 37.89 ?  2   MET   B HB2  1 
ATOM   3892 H HB2  B MET   B 1 2   ? 50.877 -14.380 -23.039 0.52 34.56 ?  2   MET   B HB2  1 
ATOM   3893 H HB3  A MET   B 1 2   ? 51.316 -15.127 -21.962 0.48 37.89 ?  2   MET   B HB3  1 
ATOM   3894 H HB3  B MET   B 1 2   ? 51.068 -15.087 -21.637 0.52 34.56 ?  2   MET   B HB3  1 
ATOM   3895 H HG2  A MET   B 1 2   ? 49.515 -16.496 -21.642 0.48 41.48 ?  2   MET   B HG2  1 
ATOM   3896 H HG2  B MET   B 1 2   ? 49.225 -16.393 -21.929 0.52 37.88 ?  2   MET   B HG2  1 
ATOM   3897 H HG3  A MET   B 1 2   ? 48.837 -15.973 -22.986 0.48 41.48 ?  2   MET   B HG3  1 
ATOM   3898 H HG3  B MET   B 1 2   ? 48.832 -15.617 -23.259 0.52 37.88 ?  2   MET   B HG3  1 
ATOM   3899 H HE1  A MET   B 1 2   ? 51.210 -17.117 -25.628 0.48 45.18 ?  2   MET   B HE1  1 
ATOM   3900 H HE1  B MET   B 1 2   ? 52.082 -16.474 -25.206 0.52 41.28 ?  2   MET   B HE1  1 
ATOM   3901 H HE2  A MET   B 1 2   ? 50.333 -15.891 -25.135 0.48 45.18 ?  2   MET   B HE2  1 
ATOM   3902 H HE2  B MET   B 1 2   ? 51.150 -15.242 -24.895 0.52 41.28 ?  2   MET   B HE2  1 
ATOM   3903 H HE3  A MET   B 1 2   ? 51.849 -16.023 -24.673 0.48 45.18 ?  2   MET   B HE3  1 
ATOM   3904 H HE3  B MET   B 1 2   ? 52.311 -15.660 -23.875 0.52 41.28 ?  2   MET   B HE3  1 
ATOM   3905 N N    A VAL   B 1 3   ? 48.327 -13.797 -19.966 0.48 22.98 ?  3   VAL   B N    1 
ATOM   3906 N N    B VAL   B 1 3   ? 48.189 -13.493 -19.772 0.52 21.61 ?  3   VAL   B N    1 
ATOM   3907 C CA   A VAL   B 1 3   ? 47.924 -14.026 -18.587 0.48 21.36 ?  3   VAL   B CA   1 
ATOM   3908 C CA   B VAL   B 1 3   ? 47.765 -13.768 -18.406 0.52 21.07 ?  3   VAL   B CA   1 
ATOM   3909 C C    A VAL   B 1 3   ? 46.682 -14.910 -18.590 0.48 19.27 ?  3   VAL   B C    1 
ATOM   3910 C C    B VAL   B 1 3   ? 46.528 -14.653 -18.446 0.52 19.82 ?  3   VAL   B C    1 
ATOM   3911 O O    A VAL   B 1 3   ? 46.001 -15.068 -19.607 0.48 18.61 ?  3   VAL   B O    1 
ATOM   3912 O O    B VAL   B 1 3   ? 45.717 -14.588 -19.375 0.52 20.19 ?  3   VAL   B O    1 
ATOM   3913 C CB   A VAL   B 1 3   ? 47.666 -12.705 -17.821 0.48 22.35 ?  3   VAL   B CB   1 
ATOM   3914 C CB   B VAL   B 1 3   ? 47.507 -12.482 -17.583 0.52 22.05 ?  3   VAL   B CB   1 
ATOM   3915 C CG1  A VAL   B 1 3   ? 48.944 -11.860 -17.747 0.48 22.97 ?  3   VAL   B CG1  1 
ATOM   3916 C CG1  B VAL   B 1 3   ? 48.789 -11.661 -17.449 0.52 22.63 ?  3   VAL   B CG1  1 
ATOM   3917 C CG2  A VAL   B 1 3   ? 46.541 -11.916 -18.473 0.48 22.79 ?  3   VAL   B CG2  1 
ATOM   3918 C CG2  B VAL   B 1 3   ? 46.396 -11.656 -18.207 0.52 22.43 ?  3   VAL   B CG2  1 
ATOM   3919 H H    A VAL   B 1 3   ? 47.676 -13.575 -20.480 0.48 27.59 ?  3   VAL   B H    1 
ATOM   3920 H H    B VAL   B 1 3   ? 47.573 -13.156 -20.269 0.52 25.95 ?  3   VAL   B H    1 
ATOM   3921 H HA   A VAL   B 1 3   ? 48.633 -14.501 -18.123 0.48 25.63 ?  3   VAL   B HA   1 
ATOM   3922 H HA   B VAL   B 1 3   ? 48.461 -14.263 -17.958 0.52 25.29 ?  3   VAL   B HA   1 
ATOM   3923 H HB   A VAL   B 1 3   ? 47.400 -12.914 -16.912 0.48 26.83 ?  3   VAL   B HB   1 
ATOM   3924 H HB   B VAL   B 1 3   ? 47.228 -12.734 -16.691 0.52 26.47 ?  3   VAL   B HB   1 
ATOM   3925 H HG11 A VAL   B 1 3   ? 48.756 -11.046 -17.251 0.48 27.57 ?  3   VAL   B HG11 1 
ATOM   3926 H HG11 B VAL   B 1 3   ? 48.602 -10.869 -16.921 0.52 27.17 ?  3   VAL   B HG11 1 
ATOM   3927 H HG12 A VAL   B 1 3   ? 49.634 -12.369 -17.293 0.48 27.57 ?  3   VAL   B HG12 1 
ATOM   3928 H HG12 B VAL   B 1 3   ? 49.464 -12.201 -17.009 0.52 27.17 ?  3   VAL   B HG12 1 
ATOM   3929 H HG13 A VAL   B 1 3   ? 49.230 -11.640 -18.646 0.48 27.57 ?  3   VAL   B HG13 1 
ATOM   3930 H HG13 B VAL   B 1 3   ? 49.094 -11.406 -18.334 0.52 27.17 ?  3   VAL   B HG13 1 
ATOM   3931 H HG21 A VAL   B 1 3   ? 46.489 -11.040 -18.059 0.48 27.35 ?  3   VAL   B HG21 1 
ATOM   3932 H HG21 B VAL   B 1 3   ? 46.352 -10.797 -17.760 0.52 26.92 ?  3   VAL   B HG21 1 
ATOM   3933 H HG22 A VAL   B 1 3   ? 46.726 -11.824 -19.420 0.48 27.35 ?  3   VAL   B HG22 1 
ATOM   3934 H HG22 B VAL   B 1 3   ? 46.587 -11.529 -19.149 0.52 26.92 ?  3   VAL   B HG22 1 
ATOM   3935 H HG23 A VAL   B 1 3   ? 45.706 -12.391 -18.343 0.48 27.35 ?  3   VAL   B HG23 1 
ATOM   3936 H HG23 B VAL   B 1 3   ? 45.555 -12.128 -18.100 0.52 26.92 ?  3   VAL   B HG23 1 
ATOM   3937 N N    . ASN   B 1 4   ? 46.399 -15.501 -17.430 1.00 18.68 ?  4   ASN   B N    1 
ATOM   3938 C CA   . ASN   B 1 4   ? 45.261 -16.412 -17.299 1.00 17.91 ?  4   ASN   B CA   1 
ATOM   3939 C C    . ASN   B 1 4   ? 45.199 -17.379 -18.474 1.00 17.84 ?  4   ASN   B C    1 
ATOM   3940 O O    . ASN   B 1 4   ? 44.130 -17.628 -19.030 1.00 18.52 ?  4   ASN   B O    1 
ATOM   3941 C CB   . ASN   B 1 4   ? 43.944 -15.647 -17.142 1.00 17.58 ?  4   ASN   B CB   1 
ATOM   3942 C CG   . ASN   B 1 4   ? 43.896 -14.841 -15.868 1.00 17.33 ?  4   ASN   B CG   1 
ATOM   3943 O OD1  . ASN   B 1 4   ? 44.181 -15.350 -14.794 1.00 16.71 ?  4   ASN   B OD1  1 
ATOM   3944 N ND2  . ASN   B 1 4   ? 43.561 -13.562 -15.986 1.00 18.46 ?  4   ASN   B ND2  1 
ATOM   3945 H H    A ASN   B 1 4   ? 46.851 -15.392 -16.710 0.48 22.42 ?  4   ASN   B H    1 
ATOM   3946 H H    B ASN   B 1 4   ? 46.979 -15.577 -16.803 0.52 22.42 ?  4   ASN   B H    1 
ATOM   3947 H HA   . ASN   B 1 4   ? 45.392 -16.934 -16.494 1.00 21.50 ?  4   ASN   B HA   1 
ATOM   3948 H HB2  . ASN   B 1 4   ? 43.827 -15.043 -17.886 1.00 21.11 ?  4   ASN   B HB2  1 
ATOM   3949 H HB3  . ASN   B 1 4   ? 43.211 -16.289 -17.116 1.00 21.11 ?  4   ASN   B HB3  1 
ATOM   3950 H HD21 . ASN   B 1 4   ? 43.524 -13.059 -15.287 1.00 22.16 ?  4   ASN   B HD21 1 
ATOM   3951 H HD22 . ASN   B 1 4   ? 43.374 -13.234 -16.758 1.00 22.16 ?  4   ASN   B HD22 1 
ATOM   3952 N N    . SER   B 1 5   ? 46.352 -17.911 -18.871 1.00 19.13 ?  5   SER   B N    1 
ATOM   3953 C CA   . SER   B 1 5   ? 46.424 -18.829 -20.004 1.00 21.32 ?  5   SER   B CA   1 
ATOM   3954 C C    . SER   B 1 5   ? 46.399 -20.261 -19.480 1.00 22.82 ?  5   SER   B C    1 
ATOM   3955 O O    . SER   B 1 5   ? 47.407 -20.960 -19.433 1.00 24.95 ?  5   SER   B O    1 
ATOM   3956 C CB   . SER   B 1 5   ? 47.669 -18.546 -20.839 1.00 23.20 ?  5   SER   B CB   1 
ATOM   3957 O OG   . SER   B 1 5   ? 48.840 -18.579 -20.041 1.00 26.29 ?  5   SER   B OG   1 
ATOM   3958 H H    . SER   B 1 5   ? 47.109 -17.757 -18.495 1.00 22.97 ?  5   SER   B H    1 
ATOM   3959 H HA   . SER   B 1 5   ? 45.647 -18.700 -20.569 1.00 25.59 ?  5   SER   B HA   1 
ATOM   3960 H HB2  . SER   B 1 5   ? 47.729 -19.217 -21.540 1.00 27.85 ?  5   SER   B HB2  1 
ATOM   3961 H HB3  . SER   B 1 5   ? 47.571 -17.667 -21.237 1.00 27.85 ?  5   SER   B HB3  1 
ATOM   3962 H HG   . SER   B 1 5   ? 48.932 -19.342 -19.707 1.00 31.56 ?  5   SER   B HG   1 
ATOM   3963 N N    . PHE   B 1 6   ? 45.208 -20.672 -19.055 1.00 23.54 ?  6   PHE   B N    1 
ATOM   3964 C CA   . PHE   B 1 6   ? 44.999 -22.015 -18.540 1.00 23.32 ?  6   PHE   B CA   1 
ATOM   3965 C C    . PHE   B 1 6   ? 44.904 -22.992 -19.701 1.00 26.34 ?  6   PHE   B C    1 
ATOM   3966 O O    . PHE   B 1 6   ? 44.206 -22.729 -20.684 1.00 28.54 ?  6   PHE   B O    1 
ATOM   3967 C CB   . PHE   B 1 6   ? 43.712 -22.068 -17.719 1.00 21.56 ?  6   PHE   B CB   1 
ATOM   3968 C CG   . PHE   B 1 6   ? 43.741 -21.219 -16.488 1.00 19.59 ?  6   PHE   B CG   1 
ATOM   3969 C CD1  . PHE   B 1 6   ? 44.237 -21.718 -15.300 1.00 18.75 ?  6   PHE   B CD1  1 
ATOM   3970 C CD2  . PHE   B 1 6   ? 43.288 -19.908 -16.525 1.00 19.04 ?  6   PHE   B CD2  1 
ATOM   3971 C CE1  . PHE   B 1 6   ? 44.255 -20.933 -14.159 1.00 18.40 ?  6   PHE   B CE1  1 
ATOM   3972 C CE2  . PHE   B 1 6   ? 43.310 -19.118 -15.395 1.00 19.62 ?  6   PHE   B CE2  1 
ATOM   3973 C CZ   . PHE   B 1 6   ? 43.798 -19.622 -14.213 1.00 18.72 ?  6   PHE   B CZ   1 
ATOM   3974 H H    . PHE   B 1 6   ? 44.502 -20.187 -19.060 1.00 28.26 ?  6   PHE   B H    1 
ATOM   3975 H HA   . PHE   B 1 6   ? 45.740 -22.275 -17.979 1.00 27.99 ?  6   PHE   B HA   1 
ATOM   3976 H HB2  . PHE   B 1 6   ? 42.973 -21.764 -18.273 1.00 25.88 ?  6   PHE   B HB2  1 
ATOM   3977 H HB3  . PHE   B 1 6   ? 43.554 -22.985 -17.441 1.00 25.88 ?  6   PHE   B HB3  1 
ATOM   3978 H HD1  . PHE   B 1 6   ? 44.550 -22.592 -15.261 1.00 22.50 ?  6   PHE   B HD1  1 
ATOM   3979 H HD2  . PHE   B 1 6   ? 42.950 -19.565 -17.320 1.00 22.85 ?  6   PHE   B HD2  1 
ATOM   3980 H HE1  . PHE   B 1 6   ? 44.595 -21.270 -13.361 1.00 22.09 ?  6   PHE   B HE1  1 
ATOM   3981 H HE2  . PHE   B 1 6   ? 42.993 -18.242 -15.433 1.00 23.55 ?  6   PHE   B HE2  1 
ATOM   3982 H HZ   . PHE   B 1 6   ? 43.815 -19.092 -13.448 1.00 22.47 ?  6   PHE   B HZ   1 
ATOM   3983 N N    . SER   B 1 7   ? 45.612 -24.115 -19.587 1.00 27.23 ?  7   SER   B N    1 
ATOM   3984 C CA   . SER   B 1 7   ? 45.682 -25.093 -20.659 1.00 29.97 ?  7   SER   B CA   1 
ATOM   3985 C C    . SER   B 1 7   ? 45.637 -26.499 -20.081 1.00 29.34 ?  7   SER   B C    1 
ATOM   3986 O O    . SER   B 1 7   ? 46.256 -26.779 -19.051 1.00 30.06 ?  7   SER   B O    1 
ATOM   3987 C CB   . SER   B 1 7   ? 46.967 -24.909 -21.480 1.00 32.55 ?  7   SER   B CB   1 
ATOM   3988 O OG   . SER   B 1 7   ? 46.924 -25.674 -22.671 1.00 34.93 ?  7   SER   B OG   1 
ATOM   3989 H H    . SER   B 1 7   ? 46.071 -24.327 -18.887 1.00 32.69 ?  7   SER   B H    1 
ATOM   3990 H HA   . SER   B 1 7   ? 44.926 -24.984 -21.248 1.00 35.98 ?  7   SER   B HA   1 
ATOM   3991 H HB2  . SER   B 1 7   ? 47.064 -23.969 -21.710 1.00 39.06 ?  7   SER   B HB2  1 
ATOM   3992 H HB3  . SER   B 1 7   ? 47.730 -25.193 -20.948 1.00 39.06 ?  7   SER   B HB3  1 
ATOM   3993 H HG   . SER   B 1 7   ? 47.634 -25.560 -23.108 1.00 41.92 ?  7   SER   B HG   1 
ATOM   3994 N N    A GLY   B 1 8   ? 44.897 -27.377 -20.751 0.48 29.40 ?  8   GLY   B N    1 
ATOM   3995 N N    B GLY   B 1 8   ? 44.901 -27.379 -20.754 0.52 29.44 ?  8   GLY   B N    1 
ATOM   3996 C CA   A GLY   B 1 8   ? 44.857 -28.770 -20.368 0.48 28.91 ?  8   GLY   B CA   1 
ATOM   3997 C CA   B GLY   B 1 8   ? 44.857 -28.772 -20.368 0.52 28.94 ?  8   GLY   B CA   1 
ATOM   3998 C C    A GLY   B 1 8   ? 43.946 -29.093 -19.212 0.48 27.98 ?  8   GLY   B C    1 
ATOM   3999 C C    B GLY   B 1 8   ? 43.947 -29.093 -19.208 0.52 27.99 ?  8   GLY   B C    1 
ATOM   4000 O O    A GLY   B 1 8   ? 44.157 -30.111 -18.544 0.48 29.06 ?  8   GLY   B O    1 
ATOM   4001 O O    B GLY   B 1 8   ? 44.157 -30.108 -18.534 0.52 29.13 ?  8   GLY   B O    1 
ATOM   4002 H H    A GLY   B 1 8   ? 44.411 -27.181 -21.428 0.48 35.29 ?  8   GLY   B H    1 
ATOM   4003 H H    B GLY   B 1 8   ? 44.427 -27.187 -21.440 0.52 35.34 ?  8   GLY   B H    1 
ATOM   4004 H HA2  A GLY   B 1 8   ? 44.567 -29.296 -21.127 0.48 34.70 ?  8   GLY   B HA2  1 
ATOM   4005 H HA2  B GLY   B 1 8   ? 44.566 -29.298 -21.127 0.52 34.74 ?  8   GLY   B HA2  1 
ATOM   4006 H HA3  A GLY   B 1 8   ? 45.747 -29.059 -20.121 0.48 34.70 ?  8   GLY   B HA3  1 
ATOM   4007 H HA3  B GLY   B 1 8   ? 45.747 -29.063 -20.122 0.52 34.74 ?  8   GLY   B HA3  1 
ATOM   4008 N N    . TYR   B 1 9   ? 42.926 -28.276 -18.961 1.00 26.81 ?  9   TYR   B N    1 
ATOM   4009 C CA   . TYR   B 1 9   ? 41.990 -28.539 -17.881 1.00 23.93 ?  9   TYR   B CA   1 
ATOM   4010 C C    . TYR   B 1 9   ? 40.796 -29.333 -18.379 1.00 23.60 ?  9   TYR   B C    1 
ATOM   4011 O O    . TYR   B 1 9   ? 40.354 -29.185 -19.523 1.00 24.89 ?  9   TYR   B O    1 
ATOM   4012 C CB   . TYR   B 1 9   ? 41.501 -27.246 -17.234 1.00 23.02 ?  9   TYR   B CB   1 
ATOM   4013 C CG   . TYR   B 1 9   ? 42.533 -26.628 -16.318 1.00 21.87 ?  9   TYR   B CG   1 
ATOM   4014 C CD1  . TYR   B 1 9   ? 43.617 -25.940 -16.836 1.00 22.41 ?  9   TYR   B CD1  1 
ATOM   4015 C CD2  . TYR   B 1 9   ? 42.437 -26.760 -14.939 1.00 21.30 ?  9   TYR   B CD2  1 
ATOM   4016 C CE1  . TYR   B 1 9   ? 44.574 -25.383 -16.008 1.00 22.50 ?  9   TYR   B CE1  1 
ATOM   4017 C CE2  . TYR   B 1 9   ? 43.393 -26.207 -14.099 1.00 21.90 ?  9   TYR   B CE2  1 
ATOM   4018 C CZ   . TYR   B 1 9   ? 44.459 -25.517 -14.642 1.00 22.53 ?  9   TYR   B CZ   1 
ATOM   4019 O OH   . TYR   B 1 9   ? 45.418 -24.978 -13.822 1.00 22.88 ?  9   TYR   B OH   1 
ATOM   4020 H H    A TYR   B 1 9   ? 42.740 -27.568 -19.415 0.48 32.18 ?  9   TYR   B H    1 
ATOM   4021 H H    B TYR   B 1 9   ? 42.740 -27.568 -19.415 0.52 32.18 ?  9   TYR   B H    1 
ATOM   4022 H HA   . TYR   B 1 9   ? 42.419 -29.064 -17.196 1.00 28.73 ?  9   TYR   B HA   1 
ATOM   4023 H HB2  . TYR   B 1 9   ? 41.280 -26.595 -17.922 1.00 27.64 ?  9   TYR   B HB2  1 
ATOM   4024 H HB3  . TYR   B 1 9   ? 40.718 -27.445 -16.702 1.00 27.64 ?  9   TYR   B HB3  1 
ATOM   4025 H HD1  . TYR   B 1 9   ? 43.696 -25.845 -17.758 1.00 26.90 ?  9   TYR   B HD1  1 
ATOM   4026 H HD2  . TYR   B 1 9   ? 41.713 -27.228 -14.575 1.00 25.57 ?  9   TYR   B HD2  1 
ATOM   4027 H HE1  . TYR   B 1 9   ? 45.287 -24.923 -16.371 1.00 27.01 ?  9   TYR   B HE1  1 
ATOM   4028 H HE2  . TYR   B 1 9   ? 43.308 -26.304 -13.176 1.00 26.29 ?  9   TYR   B HE2  1 
ATOM   4029 H HH   . TYR   B 1 9   ? 45.996 -24.584 -14.278 1.00 27.46 ?  9   TYR   B HH   1 
ATOM   4030 N N    . LEU   B 1 10  ? 40.295 -30.200 -17.502 1.00 22.16 ?  10  LEU   B N    1 
ATOM   4031 C CA   . LEU   B 1 10  ? 39.083 -30.963 -17.748 1.00 21.91 ?  10  LEU   B CA   1 
ATOM   4032 C C    . LEU   B 1 10  ? 37.900 -30.192 -17.186 1.00 21.45 ?  10  LEU   B C    1 
ATOM   4033 O O    . LEU   B 1 10  ? 37.923 -29.764 -16.030 1.00 20.75 ?  10  LEU   B O    1 
ATOM   4034 C CB   . LEU   B 1 10  ? 39.181 -32.320 -17.054 1.00 23.39 ?  10  LEU   B CB   1 
ATOM   4035 C CG   . LEU   B 1 10  ? 38.022 -33.279 -17.319 1.00 25.05 ?  10  LEU   B CG   1 
ATOM   4036 C CD1  . LEU   B 1 10  ? 38.079 -33.779 -18.754 1.00 26.11 ?  10  LEU   B CD1  1 
ATOM   4037 C CD2  . LEU   B 1 10  ? 38.046 -34.442 -16.342 1.00 26.00 ?  10  LEU   B CD2  1 
ATOM   4038 H H    . LEU   B 1 10  ? 40.644 -30.369 -16.731 1.00 26.61 ?  10  LEU   B H    1 
ATOM   4039 H HA   . LEU   B 1 10  ? 38.952 -31.100 -18.698 1.00 26.30 ?  10  LEU   B HA   1 
ATOM   4040 H HB2  . LEU   B 1 10  ? 39.990 -32.762 -17.350 1.00 28.07 ?  10  LEU   B HB2  1 
ATOM   4041 H HB3  . LEU   B 1 10  ? 39.220 -32.178 -16.094 1.00 28.07 ?  10  LEU   B HB3  1 
ATOM   4042 H HG   . LEU   B 1 10  ? 37.179 -32.810 -17.198 1.00 30.07 ?  10  LEU   B HG   1 
ATOM   4043 H HD11 . LEU   B 1 10  ? 37.383 -34.439 -18.888 1.00 31.33 ?  10  LEU   B HD11 1 
ATOM   4044 H HD12 . LEU   B 1 10  ? 37.944 -33.028 -19.353 1.00 31.33 ?  10  LEU   B HD12 1 
ATOM   4045 H HD13 . LEU   B 1 10  ? 38.950 -34.177 -18.912 1.00 31.33 ?  10  LEU   B HD13 1 
ATOM   4046 H HD21 . LEU   B 1 10  ? 37.301 -35.033 -16.535 1.00 31.21 ?  10  LEU   B HD21 1 
ATOM   4047 H HD22 . LEU   B 1 10  ? 38.883 -34.918 -16.443 1.00 31.21 ?  10  LEU   B HD22 1 
ATOM   4048 H HD23 . LEU   B 1 10  ? 37.967 -34.095 -15.439 1.00 31.21 ?  10  LEU   B HD23 1 
ATOM   4049 N N    A LYS   B 1 11  ? 36.867 -30.023 -18.007 0.48 22.51 ?  11  LYS   B N    1 
ATOM   4050 N N    B LYS   B 1 11  ? 36.874 -30.013 -18.011 0.52 22.44 ?  11  LYS   B N    1 
ATOM   4051 C CA   A LYS   B 1 11  ? 35.670 -29.296 -17.605 0.48 24.47 ?  11  LYS   B CA   1 
ATOM   4052 C CA   B LYS   B 1 11  ? 35.673 -29.301 -17.600 0.52 24.45 ?  11  LYS   B CA   1 
ATOM   4053 C C    A LYS   B 1 11  ? 34.783 -30.204 -16.757 0.48 23.60 ?  11  LYS   B C    1 
ATOM   4054 C C    B LYS   B 1 11  ? 34.814 -30.223 -16.741 0.52 23.49 ?  11  LYS   B C    1 
ATOM   4055 O O    A LYS   B 1 11  ? 34.382 -31.284 -17.207 0.48 24.69 ?  11  LYS   B O    1 
ATOM   4056 O O    B LYS   B 1 11  ? 34.471 -31.334 -17.162 0.52 24.50 ?  11  LYS   B O    1 
ATOM   4057 C CB   A LYS   B 1 11  ? 34.929 -28.843 -18.862 0.48 27.82 ?  11  LYS   B CB   1 
ATOM   4058 C CB   B LYS   B 1 11  ? 34.910 -28.854 -18.847 0.52 28.00 ?  11  LYS   B CB   1 
ATOM   4059 C CG   A LYS   B 1 11  ? 33.858 -27.791 -18.644 0.48 30.56 ?  11  LYS   B CG   1 
ATOM   4060 C CG   B LYS   B 1 11  ? 33.774 -27.884 -18.591 0.52 30.92 ?  11  LYS   B CG   1 
ATOM   4061 C CD   A LYS   B 1 11  ? 33.167 -27.456 -19.961 0.48 32.58 ?  11  LYS   B CD   1 
ATOM   4062 C CD   B LYS   B 1 11  ? 33.022 -27.577 -19.879 0.52 33.08 ?  11  LYS   B CD   1 
ATOM   4063 C CE   A LYS   B 1 11  ? 32.129 -26.360 -19.793 0.48 34.09 ?  11  LYS   B CE   1 
ATOM   4064 C CE   B LYS   B 1 11  ? 32.016 -26.455 -19.686 0.52 34.68 ?  11  LYS   B CE   1 
ATOM   4065 N NZ   A LYS   B 1 11  ? 32.750 -25.045 -19.488 0.48 34.87 ?  11  LYS   B NZ   1 
ATOM   4066 N NZ   B LYS   B 1 11  ? 32.683 -25.150 -19.426 0.52 35.48 ?  11  LYS   B NZ   1 
ATOM   4067 H H    A LYS   B 1 11  ? 36.834 -30.325 -18.814 0.48 27.02 ?  11  LYS   B H    1 
ATOM   4068 H H    B LYS   B 1 11  ? 36.846 -30.301 -18.824 0.52 26.94 ?  11  LYS   B H    1 
ATOM   4069 H HA   A LYS   B 1 11  ? 35.916 -28.515 -17.086 0.48 29.37 ?  11  LYS   B HA   1 
ATOM   4070 H HA   B LYS   B 1 11  ? 35.913 -28.517 -17.083 0.52 29.35 ?  11  LYS   B HA   1 
ATOM   4071 H HB2  A LYS   B 1 11  ? 35.575 -28.472 -19.485 0.48 33.39 ?  11  LYS   B HB2  1 
ATOM   4072 H HB2  B LYS   B 1 11  ? 35.534 -28.417 -19.451 0.52 33.61 ?  11  LYS   B HB2  1 
ATOM   4073 H HB3  A LYS   B 1 11  ? 34.500 -29.614 -19.264 0.48 33.39 ?  11  LYS   B HB3  1 
ATOM   4074 H HB3  B LYS   B 1 11  ? 34.535 -29.635 -19.280 0.52 33.61 ?  11  LYS   B HB3  1 
ATOM   4075 H HG2  A LYS   B 1 11  ? 33.192 -28.130 -18.027 0.48 36.68 ?  11  LYS   B HG2  1 
ATOM   4076 H HG2  B LYS   B 1 11  ? 33.152 -28.277 -17.962 0.52 37.11 ?  11  LYS   B HG2  1 
ATOM   4077 H HG3  A LYS   B 1 11  ? 34.264 -26.982 -18.297 0.48 36.68 ?  11  LYS   B HG3  1 
ATOM   4078 H HG3  B LYS   B 1 11  ? 34.133 -27.054 -18.242 0.52 37.11 ?  11  LYS   B HG3  1 
ATOM   4079 H HD2  A LYS   B 1 11  ? 33.830 -27.149 -20.601 0.48 39.11 ?  11  LYS   B HD2  1 
ATOM   4080 H HD2  B LYS   B 1 11  ? 33.656 -27.303 -20.562 0.52 39.70 ?  11  LYS   B HD2  1 
ATOM   4081 H HD3  A LYS   B 1 11  ? 32.721 -28.250 -20.299 0.48 39.11 ?  11  LYS   B HD3  1 
ATOM   4082 H HD3  B LYS   B 1 11  ? 32.543 -28.370 -20.167 0.52 39.70 ?  11  LYS   B HD3  1 
ATOM   4083 H HE2  A LYS   B 1 11  ? 31.621 -26.274 -20.615 0.48 40.91 ?  11  LYS   B HE2  1 
ATOM   4084 H HE2  B LYS   B 1 11  ? 31.479 -26.366 -20.489 0.52 41.63 ?  11  LYS   B HE2  1 
ATOM   4085 H HE3  A LYS   B 1 11  ? 31.538 -26.596 -19.060 0.48 40.91 ?  11  LYS   B HE3  1 
ATOM   4086 H HE3  B LYS   B 1 11  ? 31.450 -26.666 -18.927 0.52 41.63 ?  11  LYS   B HE3  1 
ATOM   4087 H HZ1  A LYS   B 1 11  ? 32.119 -24.425 -19.399 0.48 41.85 ?  11  LYS   B HZ1  1 
ATOM   4088 H HZ1  B LYS   B 1 11  ? 32.073 -24.505 -19.359 0.52 42.58 ?  11  LYS   B HZ1  1 
ATOM   4089 H HZ2  A LYS   B 1 11  ? 33.214 -25.097 -18.731 0.48 41.85 ?  11  LYS   B HZ2  1 
ATOM   4090 H HZ2  B LYS   B 1 11  ? 33.146 -25.190 -18.667 0.52 42.58 ?  11  LYS   B HZ2  1 
ATOM   4091 H HZ3  A LYS   B 1 11  ? 33.298 -24.809 -20.148 0.48 41.85 ?  11  LYS   B HZ3  1 
ATOM   4092 H HZ3  B LYS   B 1 11  ? 33.238 -24.954 -20.094 0.52 42.58 ?  11  LYS   B HZ3  1 
ATOM   4093 N N    . LEU   B 1 12  ? 34.478 -29.773 -15.532 1.00 21.84 ?  12  LEU   B N    1 
ATOM   4094 C CA   . LEU   B 1 12  ? 33.539 -30.483 -14.665 1.00 20.96 ?  12  LEU   B CA   1 
ATOM   4095 C C    . LEU   B 1 12  ? 32.148 -29.878 -14.729 1.00 21.38 ?  12  LEU   B C    1 
ATOM   4096 O O    . LEU   B 1 12  ? 31.165 -30.601 -14.880 1.00 21.56 ?  12  LEU   B O    1 
ATOM   4097 C CB   . LEU   B 1 12  ? 34.019 -30.506 -13.207 1.00 20.32 ?  12  LEU   B CB   1 
ATOM   4098 C CG   . LEU   B 1 12  ? 35.355 -31.200 -12.948 1.00 19.96 ?  12  LEU   B CG   1 
ATOM   4099 C CD1  . LEU   B 1 12  ? 35.733 -31.151 -11.474 1.00 20.46 ?  12  LEU   B CD1  1 
ATOM   4100 C CD2  . LEU   B 1 12  ? 35.336 -32.639 -13.445 1.00 20.47 ?  12  LEU   B CD2  1 
ATOM   4101 H H    A LEU   B 1 12  ? 34.804 -29.059 -15.177 0.48 26.21 ?  12  LEU   B H    1 
ATOM   4102 H H    B LEU   B 1 12  ? 34.788 -29.048 -15.185 0.52 26.21 ?  12  LEU   B H    1 
ATOM   4103 H HA   . LEU   B 1 12  ? 33.461 -31.395 -14.971 1.00 25.16 ?  12  LEU   B HA   1 
ATOM   4104 H HB2  . LEU   B 1 12  ? 34.095 -29.594 -12.897 1.00 24.40 ?  12  LEU   B HB2  1 
ATOM   4105 H HB3  . LEU   B 1 12  ? 33.344 -30.970 -12.679 1.00 24.40 ?  12  LEU   B HB3  1 
ATOM   4106 H HG   . LEU   B 1 12  ? 36.041 -30.729 -13.441 1.00 23.95 ?  12  LEU   B HG   1 
ATOM   4107 H HD11 . LEU   B 1 12  ? 36.589 -31.595 -11.356 1.00 24.56 ?  12  LEU   B HD11 1 
ATOM   4108 H HD12 . LEU   B 1 12  ? 35.800 -30.225 -11.195 1.00 24.56 ?  12  LEU   B HD12 1 
ATOM   4109 H HD13 . LEU   B 1 12  ? 35.051 -31.606 -10.956 1.00 24.56 ?  12  LEU   B HD13 1 
ATOM   4110 H HD21 . LEU   B 1 12  ? 36.145 -33.084 -13.148 1.00 24.57 ?  12  LEU   B HD21 1 
ATOM   4111 H HD22 . LEU   B 1 12  ? 34.558 -33.089 -13.078 1.00 24.57 ?  12  LEU   B HD22 1 
ATOM   4112 H HD23 . LEU   B 1 12  ? 35.292 -32.639 -14.413 1.00 24.57 ?  12  LEU   B HD23 1 
ATOM   4113 N N    . THR   B 1 13  ? 32.052 -28.561 -14.600 1.00 21.27 ?  13  THR   B N    1 
ATOM   4114 C CA   . THR   B 1 13  ? 30.829 -27.809 -14.816 1.00 21.24 ?  13  THR   B CA   1 
ATOM   4115 C C    . THR   B 1 13  ? 31.170 -26.629 -15.718 1.00 23.45 ?  13  THR   B C    1 
ATOM   4116 O O    . THR   B 1 13  ? 32.321 -26.449 -16.135 1.00 24.29 ?  13  THR   B O    1 
ATOM   4117 C CB   . THR   B 1 13  ? 30.242 -27.318 -13.488 1.00 20.56 ?  13  THR   B CB   1 
ATOM   4118 O OG1  . THR   B 1 13  ? 31.092 -26.297 -12.952 1.00 20.05 ?  13  THR   B OG1  1 
ATOM   4119 C CG2  . THR   B 1 13  ? 30.131 -28.466 -12.485 1.00 20.92 ?  13  THR   B CG2  1 
ATOM   4120 H H    . THR   B 1 13  ? 32.710 -28.057 -14.367 1.00 25.53 ?  13  THR   B H    1 
ATOM   4121 H HA   . THR   B 1 13  ? 30.169 -28.368 -15.255 1.00 25.49 ?  13  THR   B HA   1 
ATOM   4122 H HB   . THR   B 1 13  ? 29.342 -26.960 -13.637 1.00 24.68 ?  13  THR   B HB   1 
ATOM   4123 H HG1  . THR   B 1 13  ? 30.794 -25.535 -13.179 1.00 24.06 ?  13  THR   B HG1  1 
ATOM   4124 H HG21 . THR   B 1 13  ? 29.626 -28.183 -11.704 1.00 25.12 ?  13  THR   B HG21 1 
ATOM   4125 H HG22 . THR   B 1 13  ? 29.678 -29.222 -12.891 1.00 25.12 ?  13  THR   B HG22 1 
ATOM   4126 H HG23 . THR   B 1 13  ? 31.015 -28.744 -12.203 1.00 25.12 ?  13  THR   B HG23 1 
ATOM   4127 N N    A ASP   B 1 14  ? 30.164 -25.803 -16.008 0.48 24.45 ?  14  ASP   B N    1 
ATOM   4128 N N    B ASP   B 1 14  ? 30.165 -25.797 -16.003 0.52 24.39 ?  14  ASP   B N    1 
ATOM   4129 C CA   A ASP   B 1 14  ? 30.397 -24.654 -16.875 0.48 25.71 ?  14  ASP   B CA   1 
ATOM   4130 C CA   B ASP   B 1 14  ? 30.387 -24.651 -16.878 0.52 25.61 ?  14  ASP   B CA   1 
ATOM   4131 C C    A ASP   B 1 14  ? 31.512 -23.761 -16.343 0.48 23.79 ?  14  ASP   B C    1 
ATOM   4132 C C    B ASP   B 1 14  ? 31.427 -23.682 -16.328 0.52 23.73 ?  14  ASP   B C    1 
ATOM   4133 O O    A ASP   B 1 14  ? 32.217 -23.120 -17.131 0.48 24.84 ?  14  ASP   B O    1 
ATOM   4134 O O    B ASP   B 1 14  ? 31.959 -22.872 -17.095 0.52 24.77 ?  14  ASP   B O    1 
ATOM   4135 C CB   A ASP   B 1 14  ? 29.105 -23.856 -17.061 0.48 28.77 ?  14  ASP   B CB   1 
ATOM   4136 C CB   B ASP   B 1 14  ? 29.084 -23.889 -17.116 0.52 28.67 ?  14  ASP   B CB   1 
ATOM   4137 C CG   A ASP   B 1 14  ? 28.130 -24.527 -18.009 0.48 31.43 ?  14  ASP   B CG   1 
ATOM   4138 C CG   B ASP   B 1 14  ? 28.151 -24.610 -18.067 0.52 31.49 ?  14  ASP   B CG   1 
ATOM   4139 O OD1  A ASP   B 1 14  ? 28.470 -25.581 -18.594 0.48 32.01 ?  14  ASP   B OD1  1 
ATOM   4140 O OD1  B ASP   B 1 14  ? 28.645 -25.274 -19.005 0.52 32.34 ?  14  ASP   B OD1  1 
ATOM   4141 O OD2  A ASP   B 1 14  ? 27.011 -23.998 -18.161 0.48 32.47 -1 14  ASP   B OD2  1 
ATOM   4142 O OD2  B ASP   B 1 14  ? 26.922 -24.522 -17.872 0.52 32.45 -1 14  ASP   B OD2  1 
ATOM   4143 H H    A ASP   B 1 14  ? 29.359 -25.872 -15.713 0.48 29.35 ?  14  ASP   B H    1 
ATOM   4144 H H    B ASP   B 1 14  ? 29.361 -25.868 -15.705 0.52 29.28 ?  14  ASP   B H    1 
ATOM   4145 H HA   A ASP   B 1 14  ? 30.679 -24.965 -17.745 0.48 30.86 ?  14  ASP   B HA   1 
ATOM   4146 H HA   B ASP   B 1 14  ? 30.704 -24.970 -17.735 0.52 30.74 ?  14  ASP   B HA   1 
ATOM   4147 H HB2  A ASP   B 1 14  ? 28.654 -23.768 -16.210 0.48 34.53 ?  14  ASP   B HB2  1 
ATOM   4148 H HB2  B ASP   B 1 14  ? 28.622 -23.781 -16.272 0.52 34.41 ?  14  ASP   B HB2  1 
ATOM   4149 H HB3  A ASP   B 1 14  ? 29.314 -22.979 -17.421 0.48 34.53 ?  14  ASP   B HB3  1 
ATOM   4150 H HB3  B ASP   B 1 14  ? 29.297 -23.013 -17.488 0.52 34.41 ?  14  ASP   B HB3  1 
ATOM   4151 N N    . ASN   B 1 15  ? 31.707 -23.718 -15.023 1.00 21.42 ?  15  ASN   B N    1 
ATOM   4152 C CA   . ASN   B 1 15  ? 32.678 -22.801 -14.428 1.00 18.93 ?  15  ASN   B CA   1 
ATOM   4153 C C    . ASN   B 1 15  ? 33.776 -23.455 -13.599 1.00 17.35 ?  15  ASN   B C    1 
ATOM   4154 O O    . ASN   B 1 15  ? 34.638 -22.728 -13.087 1.00 17.24 ?  15  ASN   B O    1 
ATOM   4155 C CB   . ASN   B 1 15  ? 31.976 -21.739 -13.565 1.00 18.53 ?  15  ASN   B CB   1 
ATOM   4156 C CG   . ASN   B 1 15  ? 31.350 -22.331 -12.320 1.00 17.91 ?  15  ASN   B CG   1 
ATOM   4157 O OD1  . ASN   B 1 15  ? 30.403 -23.124 -12.405 1.00 19.80 ?  15  ASN   B OD1  1 
ATOM   4158 N ND2  . ASN   B 1 15  ? 31.876 -21.977 -11.163 1.00 17.08 ?  15  ASN   B ND2  1 
ATOM   4159 H H    A ASN   B 1 15  ? 31.290 -24.211 -14.453 0.48 25.72 ?  15  ASN   B H    1 
ATOM   4160 H H    B ASN   B 1 15  ? 31.321 -24.240 -14.458 0.52 25.72 ?  15  ASN   B H    1 
ATOM   4161 H HA   . ASN   B 1 15  ? 33.124 -22.323 -15.135 1.00 22.73 ?  15  ASN   B HA   1 
ATOM   4162 H HB2  . ASN   B 1 15  ? 32.628 -21.065 -13.291 1.00 22.25 ?  15  ASN   B HB2  1 
ATOM   4163 H HB3  . ASN   B 1 15  ? 31.274 -21.307 -14.087 1.00 22.25 ?  15  ASN   B HB3  1 
ATOM   4164 H HD21 . ASN   B 1 15  ? 31.555 -22.284 -10.427 1.00 20.51 ?  15  ASN   B HD21 1 
ATOM   4165 H HD22 . ASN   B 1 15  ? 32.554 -21.436 -11.135 1.00 20.51 ?  15  ASN   B HD22 1 
ATOM   4166 N N    . VAL   B 1 16  ? 33.779 -24.777 -13.439 1.00 17.05 ?  16  VAL   B N    1 
ATOM   4167 C CA   . VAL   B 1 16  ? 34.772 -25.468 -12.622 1.00 16.75 ?  16  VAL   B CA   1 
ATOM   4168 C C    . VAL   B 1 16  ? 35.562 -26.411 -13.514 1.00 17.26 ?  16  VAL   B C    1 
ATOM   4169 O O    . VAL   B 1 16  ? 34.987 -27.294 -14.169 1.00 17.99 ?  16  VAL   B O    1 
ATOM   4170 C CB   . VAL   B 1 16  ? 34.140 -26.216 -11.439 1.00 16.99 ?  16  VAL   B CB   1 
ATOM   4171 C CG1  . VAL   B 1 16  ? 35.207 -26.987 -10.649 1.00 16.92 ?  16  VAL   B CG1  1 
ATOM   4172 C CG2  . VAL   B 1 16  ? 33.366 -25.240 -10.550 1.00 17.46 ?  16  VAL   B CG2  1 
ATOM   4173 H H    . VAL   B 1 16  ? 33.194 -25.308 -13.800 1.00 20.47 ?  16  VAL   B H    1 
ATOM   4174 H HA   . VAL   B 1 16  ? 35.384 -24.815 -12.261 1.00 20.10 ?  16  VAL   B HA   1 
ATOM   4175 H HB   . VAL   B 1 16  ? 33.501 -26.863 -11.783 1.00 20.39 ?  16  VAL   B HB   1 
ATOM   4176 H HG11 . VAL   B 1 16  ? 34.821 -27.278 -9.805  1.00 20.31 ?  16  VAL   B HG11 1 
ATOM   4177 H HG12 . VAL   B 1 16  ? 35.484 -27.761 -11.165 1.00 20.31 ?  16  VAL   B HG12 1 
ATOM   4178 H HG13 . VAL   B 1 16  ? 35.959 -26.404 -10.485 1.00 20.31 ?  16  VAL   B HG13 1 
ATOM   4179 H HG21 . VAL   B 1 16  ? 33.022 -25.717 -9.778  1.00 20.96 ?  16  VAL   B HG21 1 
ATOM   4180 H HG22 . VAL   B 1 16  ? 33.963 -24.533 -10.262 1.00 20.96 ?  16  VAL   B HG22 1 
ATOM   4181 H HG23 . VAL   B 1 16  ? 32.629 -24.863 -11.058 1.00 20.96 ?  16  VAL   B HG23 1 
ATOM   4182 N N    . TYR   B 1 17  ? 36.882 -26.244 -13.494 1.00 16.81 ?  17  TYR   B N    1 
ATOM   4183 C CA   . TYR   B 1 17  ? 37.824 -26.986 -14.314 1.00 17.87 ?  17  TYR   B CA   1 
ATOM   4184 C C    . TYR   B 1 17  ? 38.881 -27.593 -13.400 1.00 17.11 ?  17  TYR   B C    1 
ATOM   4185 O O    . TYR   B 1 17  ? 39.163 -27.063 -12.324 1.00 16.81 ?  17  TYR   B O    1 
ATOM   4186 C CB   . TYR   B 1 17  ? 38.519 -26.060 -15.321 1.00 21.22 ?  17  TYR   B CB   1 
ATOM   4187 C CG   . TYR   B 1 17  ? 37.588 -25.290 -16.232 1.00 25.76 ?  17  TYR   B CG   1 
ATOM   4188 C CD1  . TYR   B 1 17  ? 37.040 -24.077 -15.838 1.00 27.76 ?  17  TYR   B CD1  1 
ATOM   4189 C CD2  . TYR   B 1 17  ? 37.272 -25.772 -17.496 1.00 28.46 ?  17  TYR   B CD2  1 
ATOM   4190 C CE1  . TYR   B 1 17  ? 36.191 -23.366 -16.675 1.00 29.95 ?  17  TYR   B CE1  1 
ATOM   4191 C CE2  . TYR   B 1 17  ? 36.429 -25.072 -18.339 1.00 30.48 ?  17  TYR   B CE2  1 
ATOM   4192 C CZ   . TYR   B 1 17  ? 35.890 -23.870 -17.923 1.00 31.48 ?  17  TYR   B CZ   1 
ATOM   4193 O OH   . TYR   B 1 17  ? 35.053 -23.173 -18.763 1.00 32.92 ?  17  TYR   B OH   1 
ATOM   4194 H H    . TYR   B 1 17  ? 37.272 -25.664 -12.987 1.00 20.18 ?  17  TYR   B H    1 
ATOM   4195 H HA   . TYR   B 1 17  ? 37.360 -27.694 -14.792 1.00 21.45 ?  17  TYR   B HA   1 
ATOM   4196 H HB2  . TYR   B 1 17  ? 39.059 -25.416 -14.836 1.00 25.47 ?  17  TYR   B HB2  1 
ATOM   4197 H HB3  . TYR   B 1 17  ? 39.083 -26.600 -15.887 1.00 25.47 ?  17  TYR   B HB3  1 
ATOM   4198 H HD1  . TYR   B 1 17  ? 37.242 -23.735 -14.999 1.00 33.32 ?  17  TYR   B HD1  1 
ATOM   4199 H HD2  . TYR   B 1 17  ? 37.630 -26.580 -17.782 1.00 34.16 ?  17  TYR   B HD2  1 
ATOM   4200 H HE1  . TYR   B 1 17  ? 35.829 -22.554 -16.398 1.00 35.95 ?  17  TYR   B HE1  1 
ATOM   4201 H HE2  . TYR   B 1 17  ? 36.222 -25.409 -19.183 1.00 36.59 ?  17  TYR   B HE2  1 
ATOM   4202 H HH   . TYR   B 1 17  ? 34.957 -23.590 -19.486 1.00 39.51 ?  17  TYR   B HH   1 
ATOM   4203 N N    . ILE   B 1 18  ? 39.475 -28.709 -13.822 1.00 16.93 ?  18  ILE   B N    1 
ATOM   4204 C CA   . ILE   B 1 18  ? 40.414 -29.423 -12.966 1.00 16.68 ?  18  ILE   B CA   1 
ATOM   4205 C C    . ILE   B 1 18  ? 41.565 -29.974 -13.796 1.00 17.15 ?  18  ILE   B C    1 
ATOM   4206 O O    . ILE   B 1 18  ? 41.396 -30.350 -14.960 1.00 18.31 ?  18  ILE   B O    1 
ATOM   4207 C CB   . ILE   B 1 18  ? 39.681 -30.526 -12.156 1.00 17.24 ?  18  ILE   B CB   1 
ATOM   4208 C CG1  . ILE   B 1 18  ? 40.566 -31.067 -11.030 1.00 17.66 ?  18  ILE   B CG1  1 
ATOM   4209 C CG2  . ILE   B 1 18  ? 39.181 -31.659 -13.065 1.00 17.61 ?  18  ILE   B CG2  1 
ATOM   4210 C CD1  . ILE   B 1 18  ? 39.811 -31.943 -10.037 1.00 19.22 ?  18  ILE   B CD1  1 
ATOM   4211 H H    . ILE   B 1 18  ? 39.348 -29.067 -14.591 1.00 20.32 ?  18  ILE   B H    1 
ATOM   4212 H HA   . ILE   B 1 18  ? 40.780 -28.801 -12.321 1.00 20.02 ?  18  ILE   B HA   1 
ATOM   4213 H HB   . ILE   B 1 18  ? 38.901 -30.126 -11.740 1.00 20.70 ?  18  ILE   B HB   1 
ATOM   4214 H HG12 . ILE   B 1 18  ? 41.275 -31.600 -11.417 1.00 21.20 ?  18  ILE   B HG12 1 
ATOM   4215 H HG13 . ILE   B 1 18  ? 40.939 -30.319 -10.540 1.00 21.20 ?  18  ILE   B HG13 1 
ATOM   4216 H HG21 . ILE   B 1 18  ? 38.589 -32.240 -12.555 1.00 21.14 ?  18  ILE   B HG21 1 
ATOM   4217 H HG22 . ILE   B 1 18  ? 38.693 -31.271 -13.809 1.00 21.14 ?  18  ILE   B HG22 1 
ATOM   4218 H HG23 . ILE   B 1 18  ? 39.938 -32.165 -13.392 1.00 21.14 ?  18  ILE   B HG23 1 
ATOM   4219 H HD11 . ILE   B 1 18  ? 40.412 -32.194 -9.317  1.00 23.07 ?  18  ILE   B HD11 1 
ATOM   4220 H HD12 . ILE   B 1 18  ? 39.059 -31.445 -9.681  1.00 23.07 ?  18  ILE   B HD12 1 
ATOM   4221 H HD13 . ILE   B 1 18  ? 39.494 -32.740 -10.493 1.00 23.07 ?  18  ILE   B HD13 1 
ATOM   4222 N N    . LYS   B 1 19  ? 42.746 -30.027 -13.180 1.00 17.27 ?  19  LYS   B N    1 
ATOM   4223 C CA   . LYS   B 1 19  ? 43.953 -30.495 -13.842 1.00 18.61 ?  19  LYS   B CA   1 
ATOM   4224 C C    . LYS   B 1 19  ? 44.855 -31.178 -12.825 1.00 18.47 ?  19  LYS   B C    1 
ATOM   4225 O O    . LYS   B 1 19  ? 44.939 -30.762 -11.668 1.00 17.74 ?  19  LYS   B O    1 
ATOM   4226 C CB   . LYS   B 1 19  ? 44.713 -29.327 -14.477 1.00 20.24 ?  19  LYS   B CB   1 
ATOM   4227 C CG   . LYS   B 1 19  ? 45.922 -29.724 -15.301 1.00 22.31 ?  19  LYS   B CG   1 
ATOM   4228 C CD   . LYS   B 1 19  ? 46.626 -28.487 -15.828 1.00 24.46 ?  19  LYS   B CD   1 
ATOM   4229 C CE   . LYS   B 1 19  ? 47.759 -28.838 -16.765 1.00 26.38 ?  19  LYS   B CE   1 
ATOM   4230 N NZ   . LYS   B 1 19  ? 48.406 -27.614 -17.309 1.00 27.23 ?  19  LYS   B NZ   1 
ATOM   4231 H H    . LYS   B 1 19  ? 42.859 -29.788 -12.364 1.00 20.74 ?  19  LYS   B H    1 
ATOM   4232 H HA   . LYS   B 1 19  ? 43.709 -31.131 -14.538 1.00 22.34 ?  19  LYS   B HA   1 
ATOM   4233 H HB2  . LYS   B 1 19  ? 44.105 -28.848 -15.060 1.00 24.30 ?  19  LYS   B HB2  1 
ATOM   4234 H HB3  . LYS   B 1 19  ? 45.014 -28.739 -13.765 1.00 24.30 ?  19  LYS   B HB3  1 
ATOM   4235 H HG2  . LYS   B 1 19  ? 46.538 -30.226 -14.747 1.00 26.78 ?  19  LYS   B HG2  1 
ATOM   4236 H HG3  . LYS   B 1 19  ? 45.628 -30.263 -16.055 1.00 26.78 ?  19  LYS   B HG3  1 
ATOM   4237 H HD2  . LYS   B 1 19  ? 45.987 -27.938 -16.311 1.00 29.36 ?  19  LYS   B HD2  1 
ATOM   4238 H HD3  . LYS   B 1 19  ? 46.992 -27.988 -15.078 1.00 29.36 ?  19  LYS   B HD3  1 
ATOM   4239 H HE2  . LYS   B 1 19  ? 48.427 -29.350 -16.281 1.00 31.67 ?  19  LYS   B HE2  1 
ATOM   4240 H HE3  . LYS   B 1 19  ? 47.411 -29.358 -17.507 1.00 31.67 ?  19  LYS   B HE3  1 
ATOM   4241 H HZ1  . LYS   B 1 19  ? 49.031 -27.837 -17.902 1.00 32.68 ?  19  LYS   B HZ1  1 
ATOM   4242 H HZ2  . LYS   B 1 19  ? 47.798 -27.100 -17.709 1.00 32.68 ?  19  LYS   B HZ2  1 
ATOM   4243 H HZ3  . LYS   B 1 19  ? 48.785 -27.151 -16.650 1.00 32.68 ?  19  LYS   B HZ3  1 
ATOM   4244 N N    . ASN   B 1 20  ? 45.537 -32.224 -13.269 1.00 19.95 ?  20  ASN   B N    1 
ATOM   4245 C CA   . ASN   B 1 20  ? 46.546 -32.880 -12.443 1.00 20.88 ?  20  ASN   B CA   1 
ATOM   4246 C C    . ASN   B 1 20  ? 47.834 -32.079 -12.603 1.00 21.74 ?  20  ASN   B C    1 
ATOM   4247 O O    . ASN   B 1 20  ? 48.516 -32.185 -13.626 1.00 23.86 ?  20  ASN   B O    1 
ATOM   4248 C CB   . ASN   B 1 20  ? 46.705 -34.331 -12.893 1.00 22.43 ?  20  ASN   B CB   1 
ATOM   4249 C CG   . ASN   B 1 20  ? 47.824 -35.066 -12.178 1.00 24.63 ?  20  ASN   B CG   1 
ATOM   4250 O OD1  . ASN   B 1 20  ? 48.428 -35.977 -12.748 1.00 27.37 ?  20  ASN   B OD1  1 
ATOM   4251 N ND2  . ASN   B 1 20  ? 48.089 -34.707 -10.928 1.00 24.49 ?  20  ASN   B ND2  1 
ATOM   4252 H H    . ASN   B 1 20  ? 45.442 -32.571 -14.052 1.00 23.95 ?  20  ASN   B H    1 
ATOM   4253 H HA   . ASN   B 1 20  ? 46.260 -32.867 -11.516 1.00 25.07 ?  20  ASN   B HA   1 
ATOM   4254 H HB2  . ASN   B 1 20  ? 45.876 -34.808 -12.719 1.00 26.93 ?  20  ASN   B HB2  1 
ATOM   4255 H HB3  . ASN   B 1 20  ? 46.897 -34.344 -13.843 1.00 26.93 ?  20  ASN   B HB3  1 
ATOM   4256 H HD21 . ASN   B 1 20  ? 48.719 -35.096 -10.491 1.00 29.40 ?  20  ASN   B HD21 1 
ATOM   4257 H HD22 . ASN   B 1 20  ? 47.648 -34.066 -10.554 1.00 29.40 ?  20  ASN   B HD22 1 
ATOM   4258 N N    . ALA   B 1 21  ? 48.161 -31.246 -11.610 1.00 21.21 ?  21  ALA   B N    1 
ATOM   4259 C CA   . ALA   B 1 21  ? 49.303 -30.359 -11.760 1.00 21.47 ?  21  ALA   B CA   1 
ATOM   4260 C C    . ALA   B 1 21  ? 49.757 -29.833 -10.407 1.00 20.33 ?  21  ALA   B C    1 
ATOM   4261 O O    . ALA   B 1 21  ? 49.016 -29.853 -9.421  1.00 20.48 ?  21  ALA   B O    1 
ATOM   4262 C CB   . ALA   B 1 21  ? 48.965 -29.202 -12.699 1.00 23.30 ?  21  ALA   B CB   1 
ATOM   4263 H H    . ALA   B 1 21  ? 47.734 -31.180 -10.854 1.00 25.46 ?  21  ALA   B H    1 
ATOM   4264 H HA   . ALA   B 1 21  ? 50.030 -30.867 -12.142 1.00 25.78 ?  21  ALA   B HA   1 
ATOM   4265 H HB1  . ALA   B 1 21  ? 49.770 -28.694 -12.848 1.00 27.97 ?  21  ALA   B HB1  1 
ATOM   4266 H HB2  . ALA   B 1 21  ? 48.643 -29.575 -13.536 1.00 27.97 ?  21  ALA   B HB2  1 
ATOM   4267 H HB3  . ALA   B 1 21  ? 48.280 -28.658 -12.291 1.00 27.97 ?  21  ALA   B HB3  1 
ATOM   4268 N N    . ASP   B 1 22  ? 51.014 -29.390 -10.392 1.00 19.66 ?  22  ASP   B N    1 
ATOM   4269 C CA   . ASP   B 1 22  ? 51.633 -28.687 -9.272  1.00 19.33 ?  22  ASP   B CA   1 
ATOM   4270 C C    . ASP   B 1 22  ? 51.225 -27.217 -9.351  1.00 17.40 ?  22  ASP   B C    1 
ATOM   4271 O O    . ASP   B 1 22  ? 51.533 -26.546 -10.339 1.00 17.92 ?  22  ASP   B O    1 
ATOM   4272 C CB   . ASP   B 1 22  ? 53.150 -28.861 -9.433  1.00 20.93 ?  22  ASP   B CB   1 
ATOM   4273 C CG   . ASP   B 1 22  ? 53.975 -28.105 -8.396  1.00 23.09 ?  22  ASP   B CG   1 
ATOM   4274 O OD1  . ASP   B 1 22  ? 53.591 -26.999 -7.981  1.00 22.95 ?  22  ASP   B OD1  1 
ATOM   4275 O OD2  . ASP   B 1 22  ? 55.060 -28.611 -8.025  1.00 25.71 -1 22  ASP   B OD2  1 
ATOM   4276 H H    . ASP   B 1 22  ? 51.553 -29.512 -11.054 1.00 23.60 ?  22  ASP   B H    1 
ATOM   4277 H HA   . ASP   B 1 22  ? 51.346 -29.066 -8.430  1.00 23.21 ?  22  ASP   B HA   1 
ATOM   4278 H HB2  . ASP   B 1 22  ? 53.369 -29.801 -9.365  1.00 25.12 ?  22  ASP   B HB2  1 
ATOM   4279 H HB3  . ASP   B 1 22  ? 53.410 -28.527 -10.310 1.00 25.12 ?  22  ASP   B HB3  1 
ATOM   4280 N N    . ILE   B 1 23  ? 50.512 -26.722 -8.329  1.00 15.97 ?  23  ILE   B N    1 
ATOM   4281 C CA   . ILE   B 1 23  ? 49.935 -25.374 -8.388  1.00 15.07 ?  23  ILE   B CA   1 
ATOM   4282 C C    . ILE   B 1 23  ? 50.999 -24.298 -8.539  1.00 14.71 ?  23  ILE   B C    1 
ATOM   4283 O O    . ILE   B 1 23  ? 50.747 -23.262 -9.163  1.00 14.48 ?  23  ILE   B O    1 
ATOM   4284 C CB   . ILE   B 1 23  ? 49.010 -25.109 -7.182  1.00 15.57 ?  23  ILE   B CB   1 
ATOM   4285 C CG1  . ILE   B 1 23  ? 48.202 -23.829 -7.399  1.00 16.76 ?  23  ILE   B CG1  1 
ATOM   4286 C CG2  . ILE   B 1 23  ? 49.782 -25.061 -5.881  1.00 17.08 ?  23  ILE   B CG2  1 
ATOM   4287 C CD1  . ILE   B 1 23  ? 47.056 -23.643 -6.417  1.00 16.92 ?  23  ILE   B CD1  1 
ATOM   4288 H H    . ILE   B 1 23  ? 50.354 -27.147 -7.603  1.00 19.17 ?  23  ILE   B H    1 
ATOM   4289 H HA   . ILE   B 1 23  ? 49.378 -25.326 -9.179  1.00 18.09 ?  23  ILE   B HA   1 
ATOM   4290 H HB   . ILE   B 1 23  ? 48.380 -25.846 -7.127  1.00 18.70 ?  23  ILE   B HB   1 
ATOM   4291 H HG12 . ILE   B 1 23  ? 48.801 -23.067 -7.304  1.00 20.12 ?  23  ILE   B HG12 1 
ATOM   4292 H HG13 . ILE   B 1 23  ? 47.834 -23.839 -8.296  1.00 20.12 ?  23  ILE   B HG13 1 
ATOM   4293 H HG21 . ILE   B 1 23  ? 49.156 -25.035 -5.142  1.00 20.50 ?  23  ILE   B HG21 1 
ATOM   4294 H HG22 . ILE   B 1 23  ? 50.339 -25.853 -5.815  1.00 20.50 ?  23  ILE   B HG22 1 
ATOM   4295 H HG23 . ILE   B 1 23  ? 50.338 -24.266 -5.872  1.00 20.50 ?  23  ILE   B HG23 1 
ATOM   4296 H HD11 . ILE   B 1 23  ? 46.566 -22.841 -6.655  1.00 20.31 ?  23  ILE   B HD11 1 
ATOM   4297 H HD12 . ILE   B 1 23  ? 46.471 -24.417 -6.474  1.00 20.31 ?  23  ILE   B HD12 1 
ATOM   4298 H HD13 . ILE   B 1 23  ? 47.415 -23.564 -5.523  1.00 20.31 ?  23  ILE   B HD13 1 
ATOM   4299 N N    . VAL   B 1 24  ? 52.188 -24.500 -7.968  1.00 15.21 ?  24  VAL   B N    1 
ATOM   4300 C CA   . VAL   B 1 24  ? 53.268 -23.526 -8.137  1.00 15.96 ?  24  VAL   B CA   1 
ATOM   4301 C C    . VAL   B 1 24  ? 53.718 -23.483 -9.590  1.00 16.49 ?  24  VAL   B C    1 
ATOM   4302 O O    . VAL   B 1 24  ? 53.861 -22.408 -10.184 1.00 16.54 ?  24  VAL   B O    1 
ATOM   4303 C CB   . VAL   B 1 24  ? 54.445 -23.851 -7.197  1.00 16.88 ?  24  VAL   B CB   1 
ATOM   4304 C CG1  . VAL   B 1 24  ? 55.639 -22.963 -7.512  1.00 18.09 ?  24  VAL   B CG1  1 
ATOM   4305 C CG2  . VAL   B 1 24  ? 54.035 -23.679 -5.753  1.00 17.79 ?  24  VAL   B CG2  1 
ATOM   4306 H H    . VAL   B 1 24  ? 52.390 -25.178 -7.481  1.00 18.26 ?  24  VAL   B H    1 
ATOM   4307 H HA   . VAL   B 1 24  ? 52.937 -22.647 -7.899  1.00 19.16 ?  24  VAL   B HA   1 
ATOM   4308 H HB   . VAL   B 1 24  ? 54.712 -24.777 -7.326  1.00 20.26 ?  24  VAL   B HB   1 
ATOM   4309 H HG11 . VAL   B 1 24  ? 56.230 -22.956 -6.746  1.00 21.72 ?  24  VAL   B HG11 1 
ATOM   4310 H HG12 . VAL   B 1 24  ? 56.096 -23.320 -8.285  1.00 21.72 ?  24  VAL   B HG12 1 
ATOM   4311 H HG13 . VAL   B 1 24  ? 55.317 -22.066 -7.693  1.00 21.72 ?  24  VAL   B HG13 1 
ATOM   4312 H HG21 . VAL   B 1 24  ? 54.766 -23.957 -5.180  1.00 21.35 ?  24  VAL   B HG21 1 
ATOM   4313 H HG22 . VAL   B 1 24  ? 53.826 -22.746 -5.595  1.00 21.35 ?  24  VAL   B HG22 1 
ATOM   4314 H HG23 . VAL   B 1 24  ? 53.252 -24.228 -5.577  1.00 21.35 ?  24  VAL   B HG23 1 
ATOM   4315 N N    A GLU   B 1 25  ? 53.976 -24.651 -10.181 0.48 17.84 ?  25  GLU   B N    1 
ATOM   4316 N N    B GLU   B 1 25  ? 53.962 -24.652 -10.184 0.52 17.77 ?  25  GLU   B N    1 
ATOM   4317 C CA   A GLU   B 1 25  ? 54.385 -24.680 -11.580 0.48 19.35 ?  25  GLU   B CA   1 
ATOM   4318 C CA   B GLU   B 1 25  ? 54.353 -24.688 -11.589 0.52 19.21 ?  25  GLU   B CA   1 
ATOM   4319 C C    A GLU   B 1 25  ? 53.273 -24.172 -12.487 0.48 17.74 ?  25  GLU   B C    1 
ATOM   4320 C C    B GLU   B 1 25  ? 53.239 -24.161 -12.482 0.52 17.75 ?  25  GLU   B C    1 
ATOM   4321 O O    A GLU   B 1 25  ? 53.539 -23.480 -13.478 0.48 18.47 ?  25  GLU   B O    1 
ATOM   4322 O O    B GLU   B 1 25  ? 53.502 -23.441 -13.454 0.52 18.50 ?  25  GLU   B O    1 
ATOM   4323 C CB   A GLU   B 1 25  ? 54.825 -26.089 -11.973 0.48 22.97 ?  25  GLU   B CB   1 
ATOM   4324 C CB   B GLU   B 1 25  ? 54.763 -26.105 -11.985 0.52 22.72 ?  25  GLU   B CB   1 
ATOM   4325 C CG   A GLU   B 1 25  ? 56.086 -26.541 -11.246 0.48 26.96 ?  25  GLU   B CG   1 
ATOM   4326 C CG   B GLU   B 1 25  ? 56.050 -26.560 -11.310 0.52 26.85 ?  25  GLU   B CG   1 
ATOM   4327 C CD   A GLU   B 1 25  ? 57.204 -25.507 -11.292 0.48 30.36 ?  25  GLU   B CD   1 
ATOM   4328 C CD   B GLU   B 1 25  ? 57.202 -25.588 -11.517 0.52 30.29 ?  25  GLU   B CD   1 
ATOM   4329 O OE1  A GLU   B 1 25  ? 57.615 -25.110 -12.405 0.48 31.61 ?  25  GLU   B OE1  1 
ATOM   4330 O OE1  B GLU   B 1 25  ? 57.668 -25.460 -12.669 0.52 31.61 ?  25  GLU   B OE1  1 
ATOM   4331 O OE2  A GLU   B 1 25  ? 57.664 -25.073 -10.211 0.48 31.54 -1 25  GLU   B OE2  1 
ATOM   4332 O OE2  B GLU   B 1 25  ? 57.634 -24.941 -10.535 0.52 31.48 -1 25  GLU   B OE2  1 
ATOM   4333 H H    A GLU   B 1 25  ? 53.925 -25.418 -9.801  0.48 21.42 ?  25  GLU   B H    1 
ATOM   4334 H H    B GLU   B 1 25  ? 53.907 -25.420 -9.805  0.52 21.33 ?  25  GLU   B H    1 
ATOM   4335 H HA   A GLU   B 1 25  ? 55.133 -24.078 -11.697 0.48 23.23 ?  25  GLU   B HA   1 
ATOM   4336 H HA   B GLU   B 1 25  ? 55.112 -24.100 -11.714 0.52 23.06 ?  25  GLU   B HA   1 
ATOM   4337 H HB2  A GLU   B 1 25  ? 54.113 -26.713 -11.756 0.48 27.57 ?  25  GLU   B HB2  1 
ATOM   4338 H HB2  B GLU   B 1 25  ? 54.057 -26.720 -11.728 0.52 27.27 ?  25  GLU   B HB2  1 
ATOM   4339 H HB3  A GLU   B 1 25  ? 55.002 -26.110 -12.926 0.48 27.57 ?  25  GLU   B HB3  1 
ATOM   4340 H HB3  B GLU   B 1 25  ? 54.897 -26.138 -12.945 0.52 27.27 ?  25  GLU   B HB3  1 
ATOM   4341 H HG2  A GLU   B 1 25  ? 55.871 -26.697 -10.315 0.48 32.36 ?  25  GLU   B HG2  1 
ATOM   4342 H HG2  B GLU   B 1 25  ? 55.892 -26.650 -10.359 0.52 32.23 ?  25  GLU   B HG2  1 
ATOM   4343 H HG3  A GLU   B 1 25  ? 56.410 -27.355 -11.660 0.48 32.36 ?  25  GLU   B HG3  1 
ATOM   4344 H HG3  B GLU   B 1 25  ? 56.323 -27.406 -11.690 0.52 32.23 ?  25  GLU   B HG3  1 
ATOM   4345 N N    A GLU   B 1 26  ? 52.019 -24.489 -12.154 0.48 16.57 ?  26  GLU   B N    1 
ATOM   4346 N N    B GLU   B 1 26  ? 51.986 -24.490 -12.156 0.52 16.83 ?  26  GLU   B N    1 
ATOM   4347 C CA   A GLU   B 1 26  ? 50.895 -23.955 -12.914 0.48 16.79 ?  26  GLU   B CA   1 
ATOM   4348 C CA   B GLU   B 1 26  ? 50.859 -23.955 -12.913 0.52 17.43 ?  26  GLU   B CA   1 
ATOM   4349 C C    A GLU   B 1 26  ? 50.867 -22.437 -12.849 0.48 16.18 ?  26  GLU   B C    1 
ATOM   4350 C C    B GLU   B 1 26  ? 50.827 -22.437 -12.844 0.52 16.49 ?  26  GLU   B C    1 
ATOM   4351 O O    A GLU   B 1 26  ? 50.701 -21.765 -13.872 0.48 17.11 ?  26  GLU   B O    1 
ATOM   4352 O O    B GLU   B 1 26  ? 50.616 -21.764 -13.858 0.52 17.52 ?  26  GLU   B O    1 
ATOM   4353 C CB   A GLU   B 1 26  ? 49.582 -24.526 -12.381 0.48 17.86 ?  26  GLU   B CB   1 
ATOM   4354 C CB   B GLU   B 1 26  ? 49.544 -24.529 -12.379 0.52 19.18 ?  26  GLU   B CB   1 
ATOM   4355 C CG   A GLU   B 1 26  ? 49.244 -25.896 -12.918 0.48 19.60 ?  26  GLU   B CG   1 
ATOM   4356 C CG   B GLU   B 1 26  ? 49.065 -25.771 -13.095 0.52 21.68 ?  26  GLU   B CG   1 
ATOM   4357 C CD   A GLU   B 1 26  ? 49.107 -25.938 -14.429 0.48 20.29 ?  26  GLU   B CD   1 
ATOM   4358 C CD   B GLU   B 1 26  ? 48.756 -25.493 -14.566 0.52 22.75 ?  26  GLU   B CD   1 
ATOM   4359 O OE1  A GLU   B 1 26  ? 48.311 -25.154 -14.992 0.48 20.26 ?  26  GLU   B OE1  1 
ATOM   4360 O OE1  B GLU   B 1 26  ? 47.737 -24.830 -14.868 0.52 23.62 ?  26  GLU   B OE1  1 
ATOM   4361 O OE2  A GLU   B 1 26  ? 49.803 -26.763 -15.051 0.48 20.92 -1 26  GLU   B OE2  1 
ATOM   4362 O OE2  B GLU   B 1 26  ? 49.544 -25.920 -15.424 0.52 22.73 -1 26  GLU   B OE2  1 
ATOM   4363 H H    A GLU   B 1 26  ? 51.798 -25.006 -11.504 0.48 19.89 ?  26  GLU   B H    1 
ATOM   4364 H H    B GLU   B 1 26  ? 51.766 -25.015 -11.512 0.52 20.21 ?  26  GLU   B H    1 
ATOM   4365 H HA   A GLU   B 1 26  ? 50.985 -24.213 -13.843 0.48 20.15 ?  26  GLU   B HA   1 
ATOM   4366 H HA   B GLU   B 1 26  ? 50.953 -24.211 -13.843 0.52 20.93 ?  26  GLU   B HA   1 
ATOM   4367 H HB2  A GLU   B 1 26  ? 49.642 -24.596 -11.412 0.48 21.44 ?  26  GLU   B HB2  1 
ATOM   4368 H HB2  B GLU   B 1 26  ? 49.655 -24.745 -11.444 0.52 23.03 ?  26  GLU   B HB2  1 
ATOM   4369 H HB3  A GLU   B 1 26  ? 48.858 -23.923 -12.616 0.48 21.44 ?  26  GLU   B HB3  1 
ATOM   4370 H HB3  B GLU   B 1 26  ? 48.851 -23.854 -12.480 0.52 23.03 ?  26  GLU   B HB3  1 
ATOM   4371 H HG2  A GLU   B 1 26  ? 49.962 -26.493 -12.692 0.48 23.53 ?  26  GLU   B HG2  1 
ATOM   4372 H HG2  B GLU   B 1 26  ? 49.749 -26.463 -12.999 0.52 26.02 ?  26  GLU   B HG2  1 
ATOM   4373 H HG3  A GLU   B 1 26  ? 48.412 -26.183 -12.516 0.48 23.53 ?  26  GLU   B HG3  1 
ATOM   4374 H HG3  B GLU   B 1 26  ? 48.240 -26.074 -12.687 0.52 26.02 ?  26  GLU   B HG3  1 
ATOM   4375 N N    . ALA   B 1 27  ? 51.016 -21.879 -11.648 1.00 15.48 ?  27  ALA   B N    1 
ATOM   4376 C CA   . ALA   B 1 27  ? 50.973 -20.430 -11.508 1.00 15.35 ?  27  ALA   B CA   1 
ATOM   4377 C C    . ALA   B 1 27  ? 52.041 -19.776 -12.368 1.00 16.67 ?  27  ALA   B C    1 
ATOM   4378 O O    . ALA   B 1 27  ? 51.784 -18.770 -13.044 1.00 17.25 ?  27  ALA   B O    1 
ATOM   4379 C CB   . ALA   B 1 27  ? 51.136 -20.041 -10.038 1.00 15.21 ?  27  ALA   B CB   1 
ATOM   4380 H H    A ALA   B 1 27  ? 51.144 -22.310 -10.914 0.48 18.58 ?  27  ALA   B H    1 
ATOM   4381 H H    B ALA   B 1 27  ? 51.164 -22.310 -10.918 0.52 18.58 ?  27  ALA   B H    1 
ATOM   4382 H HA   . ALA   B 1 27  ? 50.112 -20.107 -11.807 1.00 18.43 ?  27  ALA   B HA   1 
ATOM   4383 H HB1  . ALA   B 1 27  ? 51.098 -19.074 -9.963  1.00 18.26 ?  27  ALA   B HB1  1 
ATOM   4384 H HB2  . ALA   B 1 27  ? 50.413 -20.439 -9.526  1.00 18.26 ?  27  ALA   B HB2  1 
ATOM   4385 H HB3  . ALA   B 1 27  ? 51.989 -20.366 -9.716  1.00 18.26 ?  27  ALA   B HB3  1 
ATOM   4386 N N    . LYS   B 1 28  ? 53.250 -20.338 -12.364 1.00 18.44 ?  28  LYS   B N    1 
ATOM   4387 C CA   . LYS   B 1 28  ? 54.330 -19.735 -13.135 1.00 20.56 ?  28  LYS   B CA   1 
ATOM   4388 C C    . LYS   B 1 28  ? 54.077 -19.822 -14.635 1.00 21.19 ?  28  LYS   B C    1 
ATOM   4389 O O    . LYS   B 1 28  ? 54.506 -18.936 -15.386 1.00 22.13 ?  28  LYS   B O    1 
ATOM   4390 C CB   . LYS   B 1 28  ? 55.680 -20.346 -12.738 1.00 23.80 ?  28  LYS   B CB   1 
ATOM   4391 C CG   . LYS   B 1 28  ? 56.087 -19.977 -11.310 1.00 27.47 ?  28  LYS   B CG   1 
ATOM   4392 C CD   . LYS   B 1 28  ? 57.513 -20.387 -10.961 1.00 32.21 ?  28  LYS   B CD   1 
ATOM   4393 C CE   . LYS   B 1 28  ? 57.615 -21.858 -10.628 1.00 35.99 ?  28  LYS   B CE   1 
ATOM   4394 N NZ   . LYS   B 1 28  ? 58.981 -22.211 -10.142 1.00 38.07 ?  28  LYS   B NZ   1 
ATOM   4395 H H    . LYS   B 1 28  ? 53.473 -21.047 -11.930 1.00 22.13 ?  28  LYS   B H    1 
ATOM   4396 H HA   . LYS   B 1 28  ? 54.375 -18.793 -12.917 1.00 24.68 ?  28  LYS   B HA   1 
ATOM   4397 H HB2  . LYS   B 1 28  ? 55.621 -21.312 -12.795 1.00 28.57 ?  28  LYS   B HB2  1 
ATOM   4398 H HB3  . LYS   B 1 28  ? 56.368 -20.019 -13.341 1.00 28.57 ?  28  LYS   B HB3  1 
ATOM   4399 H HG2  . LYS   B 1 28  ? 56.017 -19.014 -11.205 1.00 32.98 ?  28  LYS   B HG2  1 
ATOM   4400 H HG3  . LYS   B 1 28  ? 55.488 -20.420 -10.691 1.00 32.98 ?  28  LYS   B HG3  1 
ATOM   4401 H HD2  . LYS   B 1 28  ? 58.090 -20.204 -11.719 1.00 38.66 ?  28  LYS   B HD2  1 
ATOM   4402 H HD3  . LYS   B 1 28  ? 57.807 -19.878 -10.188 1.00 38.66 ?  28  LYS   B HD3  1 
ATOM   4403 H HE2  . LYS   B 1 28  ? 56.979 -22.074 -9.928  1.00 43.20 ?  28  LYS   B HE2  1 
ATOM   4404 H HE3  . LYS   B 1 28  ? 57.430 -22.382 -11.423 1.00 43.20 ?  28  LYS   B HE3  1 
ATOM   4405 H HZ1  . LYS   B 1 28  ? 59.021 -23.079 -9.951  1.00 45.70 ?  28  LYS   B HZ1  1 
ATOM   4406 H HZ2  . LYS   B 1 28  ? 59.584 -22.024 -10.769 1.00 45.70 ?  28  LYS   B HZ2  1 
ATOM   4407 H HZ3  . LYS   B 1 28  ? 59.173 -21.745 -9.409  1.00 45.70 ?  28  LYS   B HZ3  1 
ATOM   4408 N N    . LYS   B 1 29  ? 53.343 -20.843 -15.082 1.00 22.48 ?  29  LYS   B N    1 
ATOM   4409 C CA   . LYS   B 1 29  ? 53.038 -21.014 -16.498 1.00 25.11 ?  29  LYS   B CA   1 
ATOM   4410 C C    . LYS   B 1 29  ? 51.794 -20.241 -16.934 1.00 23.98 ?  29  LYS   B C    1 
ATOM   4411 O O    . LYS   B 1 29  ? 51.795 -19.628 -18.008 1.00 25.87 ?  29  LYS   B O    1 
ATOM   4412 C CB   . LYS   B 1 29  ? 52.862 -22.502 -16.813 1.00 30.55 ?  29  LYS   B CB   1 
ATOM   4413 C CG   . LYS   B 1 29  ? 52.841 -22.829 -18.297 1.00 35.79 ?  29  LYS   B CG   1 
ATOM   4414 C CD   . LYS   B 1 29  ? 53.044 -24.319 -18.537 1.00 39.93 ?  29  LYS   B CD   1 
ATOM   4415 C CE   . LYS   B 1 29  ? 51.858 -25.137 -18.050 1.00 42.85 ?  29  LYS   B CE   1 
ATOM   4416 N NZ   . LYS   B 1 29  ? 52.078 -26.599 -18.244 1.00 44.31 ?  29  LYS   B NZ   1 
ATOM   4417 H H    . LYS   B 1 29  ? 53.004 -21.457 -14.575 1.00 26.99 ?  29  LYS   B H    1 
ATOM   4418 H HA   . LYS   B 1 29  ? 53.783 -20.686 -17.017 1.00 30.14 ?  29  LYS   B HA   1 
ATOM   4419 H HB2  . LYS   B 1 29  ? 53.599 -22.993 -16.416 1.00 36.67 ?  29  LYS   B HB2  1 
ATOM   4420 H HB3  . LYS   B 1 29  ? 52.024 -22.806 -16.434 1.00 36.67 ?  29  LYS   B HB3  1 
ATOM   4421 H HG2  . LYS   B 1 29  ? 51.982 -22.574 -18.669 1.00 42.95 ?  29  LYS   B HG2  1 
ATOM   4422 H HG3  . LYS   B 1 29  ? 53.556 -22.347 -18.742 1.00 42.95 ?  29  LYS   B HG3  1 
ATOM   4423 H HD2  . LYS   B 1 29  ? 53.153 -24.478 -19.487 1.00 47.93 ?  29  LYS   B HD2  1 
ATOM   4424 H HD3  . LYS   B 1 29  ? 53.834 -24.615 -18.056 1.00 47.93 ?  29  LYS   B HD3  1 
ATOM   4425 H HE2  . LYS   B 1 29  ? 51.723 -24.975 -17.103 1.00 51.42 ?  29  LYS   B HE2  1 
ATOM   4426 H HE3  . LYS   B 1 29  ? 51.067 -24.879 -18.550 1.00 51.42 ?  29  LYS   B HE3  1 
ATOM   4427 H HZ1  . LYS   B 1 29  ? 51.371 -27.054 -17.952 1.00 53.18 ?  29  LYS   B HZ1  1 
ATOM   4428 H HZ2  . LYS   B 1 29  ? 52.200 -26.776 -19.108 1.00 53.18 ?  29  LYS   B HZ2  1 
ATOM   4429 H HZ3  . LYS   B 1 29  ? 52.798 -26.861 -17.791 1.00 53.18 ?  29  LYS   B HZ3  1 
ATOM   4430 N N    . VAL   B 1 30  ? 50.735 -20.263 -16.121 1.00 21.69 ?  30  VAL   B N    1 
ATOM   4431 C CA   . VAL   B 1 30  ? 49.454 -19.648 -16.480 1.00 21.42 ?  30  VAL   B CA   1 
ATOM   4432 C C    . VAL   B 1 30  ? 49.485 -18.137 -16.318 1.00 20.27 ?  30  VAL   B C    1 
ATOM   4433 O O    . VAL   B 1 30  ? 48.766 -17.413 -17.021 1.00 21.36 ?  30  VAL   B O    1 
ATOM   4434 C CB   . VAL   B 1 30  ? 48.355 -20.244 -15.581 1.00 22.23 ?  30  VAL   B CB   1 
ATOM   4435 C CG1  . VAL   B 1 30  ? 47.078 -19.417 -15.649 1.00 22.69 ?  30  VAL   B CG1  1 
ATOM   4436 C CG2  . VAL   B 1 30  ? 48.085 -21.691 -15.957 1.00 23.38 ?  30  VAL   B CG2  1 
ATOM   4437 H H    . VAL   B 1 30  ? 50.721 -20.656 -15.349 1.00 26.04 ?  30  VAL   B H    1 
ATOM   4438 H HA   . VAL   B 1 30  ? 49.236 -19.874 -17.401 1.00 25.71 ?  30  VAL   B HA   1 
ATOM   4439 H HB   . VAL   B 1 30  ? 48.658 -20.239 -14.659 1.00 26.69 ?  30  VAL   B HB   1 
ATOM   4440 H HG11 . VAL   B 1 30  ? 46.332 -19.982 -15.393 1.00 27.23 ?  30  VAL   B HG11 1 
ATOM   4441 H HG12 . VAL   B 1 30  ? 47.150 -18.671 -15.038 1.00 27.23 ?  30  VAL   B HG12 1 
ATOM   4442 H HG13 . VAL   B 1 30  ? 46.951 -19.108 -16.556 1.00 27.23 ?  30  VAL   B HG13 1 
ATOM   4443 H HG21 . VAL   B 1 30  ? 47.393 -22.052 -15.374 1.00 28.07 ?  30  VAL   B HG21 1 
ATOM   4444 H HG22 . VAL   B 1 30  ? 47.781 -21.727 -16.880 1.00 28.07 ?  30  VAL   B HG22 1 
ATOM   4445 H HG23 . VAL   B 1 30  ? 48.899 -22.204 -15.857 1.00 28.07 ?  30  VAL   B HG23 1 
ATOM   4446 N N    A LYS   B 1 31  ? 50.297 -17.643 -15.393 0.48 19.92 ?  31  LYS   B N    1 
ATOM   4447 N N    B LYS   B 1 31  ? 50.273 -17.643 -15.373 0.52 19.75 ?  31  LYS   B N    1 
ATOM   4448 C CA   A LYS   B 1 31  ? 50.325 -16.233 -15.026 0.48 20.33 ?  31  LYS   B CA   1 
ATOM   4449 C CA   B LYS   B 1 31  ? 50.322 -16.228 -15.026 0.52 20.13 ?  31  LYS   B CA   1 
ATOM   4450 C C    A LYS   B 1 31  ? 48.932 -15.725 -14.639 0.48 18.48 ?  31  LYS   B C    1 
ATOM   4451 C C    B LYS   B 1 31  ? 48.927 -15.734 -14.649 0.52 18.39 ?  31  LYS   B C    1 
ATOM   4452 O O    A LYS   B 1 31  ? 48.403 -14.800 -15.263 0.48 19.10 ?  31  LYS   B O    1 
ATOM   4453 O O    B LYS   B 1 31  ? 48.385 -14.823 -15.290 0.52 19.08 ?  31  LYS   B O    1 
ATOM   4454 C CB   A LYS   B 1 31  ? 50.943 -15.384 -16.129 0.48 22.97 ?  31  LYS   B CB   1 
ATOM   4455 C CB   B LYS   B 1 31  ? 50.957 -15.427 -16.165 0.52 22.74 ?  31  LYS   B CB   1 
ATOM   4456 C CG   A LYS   B 1 31  ? 52.386 -15.780 -16.428 0.48 26.11 ?  31  LYS   B CG   1 
ATOM   4457 C CG   B LYS   B 1 31  ? 52.367 -15.912 -16.490 0.52 25.93 ?  31  LYS   B CG   1 
ATOM   4458 C CD   A LYS   B 1 31  ? 52.960 -14.993 -17.588 0.48 29.06 ?  31  LYS   B CD   1 
ATOM   4459 C CD   B LYS   B 1 31  ? 52.915 -15.304 -17.761 0.52 28.90 ?  31  LYS   B CD   1 
ATOM   4460 C CE   A LYS   B 1 31  ? 54.429 -15.310 -17.785 0.48 31.15 ?  31  LYS   B CE   1 
ATOM   4461 C CE   B LYS   B 1 31  ? 54.417 -15.495 -17.839 0.52 30.98 ?  31  LYS   B CE   1 
ATOM   4462 N NZ   A LYS   B 1 31  ? 55.232 -14.935 -16.588 0.48 32.10 ?  31  LYS   B NZ   1 
ATOM   4463 N NZ   B LYS   B 1 31  ? 55.111 -14.879 -16.672 0.52 31.83 ?  31  LYS   B NZ   1 
ATOM   4464 H H    A LYS   B 1 31  ? 50.866 -18.124 -14.966 0.48 23.91 ?  31  LYS   B H    1 
ATOM   4465 H H    B LYS   B 1 31  ? 50.816 -18.129 -14.916 0.52 23.71 ?  31  LYS   B H    1 
ATOM   4466 H HA   A LYS   B 1 31  ? 50.885 -16.150 -14.251 0.48 24.40 ?  31  LYS   B HA   1 
ATOM   4467 H HA   B LYS   B 1 31  ? 50.890 -16.136 -14.256 0.52 24.17 ?  31  LYS   B HA   1 
ATOM   4468 H HB2  A LYS   B 1 31  ? 50.428 -15.488 -16.944 0.48 27.57 ?  31  LYS   B HB2  1 
ATOM   4469 H HB2  B LYS   B 1 31  ? 50.417 -15.510 -16.964 0.52 27.30 ?  31  LYS   B HB2  1 
ATOM   4470 H HB3  A LYS   B 1 31  ? 50.939 -14.457 -15.846 0.48 27.57 ?  31  LYS   B HB3  1 
ATOM   4471 H HB3  B LYS   B 1 31  ? 51.015 -14.495 -15.896 0.52 27.30 ?  31  LYS   B HB3  1 
ATOM   4472 H HG2  A LYS   B 1 31  ? 52.928 -15.611 -15.641 0.48 31.35 ?  31  LYS   B HG2  1 
ATOM   4473 H HG2  B LYS   B 1 31  ? 52.954 -15.674 -15.756 0.52 31.13 ?  31  LYS   B HG2  1 
ATOM   4474 H HG3  A LYS   B 1 31  ? 52.416 -16.725 -16.654 0.48 31.35 ?  31  LYS   B HG3  1 
ATOM   4475 H HG3  B LYS   B 1 31  ? 52.355 -16.876 -16.602 0.52 31.13 ?  31  LYS   B HG3  1 
ATOM   4476 H HD2  A LYS   B 1 31  ? 52.482 -15.230 -18.398 0.48 34.89 ?  31  LYS   B HD2  1 
ATOM   4477 H HD2  B LYS   B 1 31  ? 52.508 -15.743 -18.527 0.52 34.68 ?  31  LYS   B HD2  1 
ATOM   4478 H HD3  A LYS   B 1 31  ? 52.870 -14.047 -17.404 0.48 34.89 ?  31  LYS   B HD3  1 
ATOM   4479 H HD3  B LYS   B 1 31  ? 52.721 -14.355 -17.773 0.52 34.68 ?  31  LYS   B HD3  1 
ATOM   4480 H HE2  A LYS   B 1 31  ? 54.535 -16.264 -17.935 0.48 37.39 ?  31  LYS   B HE2  1 
ATOM   4481 H HE2  B LYS   B 1 31  ? 54.619 -16.444 -17.846 0.52 37.18 ?  31  LYS   B HE2  1 
ATOM   4482 H HE3  A LYS   B 1 31  ? 54.764 -14.812 -18.546 0.48 37.39 ?  31  LYS   B HE3  1 
ATOM   4483 H HE3  B LYS   B 1 31  ? 54.750 -15.074 -18.646 0.52 37.18 ?  31  LYS   B HE3  1 
ATOM   4484 H HZ1  A LYS   B 1 31  ? 56.098 -15.042 -16.757 0.48 38.53 ?  31  LYS   B HZ1  1 
ATOM   4485 H HZ1  B LYS   B 1 31  ? 55.983 -14.823 -16.833 0.52 38.20 ?  31  LYS   B HZ1  1 
ATOM   4486 H HZ2  A LYS   B 1 31  ? 55.081 -14.083 -16.378 0.48 38.53 ?  31  LYS   B HZ2  1 
ATOM   4487 H HZ2  B LYS   B 1 31  ? 54.789 -14.063 -16.523 0.52 38.20 ?  31  LYS   B HZ2  1 
ATOM   4488 H HZ3  A LYS   B 1 31  ? 55.006 -15.448 -15.896 0.48 38.53 ?  31  LYS   B HZ3  1 
ATOM   4489 H HZ3  B LYS   B 1 31  ? 54.983 -15.376 -15.943 0.52 38.20 ?  31  LYS   B HZ3  1 
ATOM   4490 N N    . PRO   B 1 32  ? 48.321 -16.305 -13.607 1.00 16.51 ?  32  PRO   B N    1 
ATOM   4491 C CA   . PRO   B 1 32  ? 46.942 -15.949 -13.261 1.00 15.65 ?  32  PRO   B CA   1 
ATOM   4492 C C    . PRO   B 1 32  ? 46.862 -14.603 -12.554 1.00 15.33 ?  32  PRO   B C    1 
ATOM   4493 O O    . PRO   B 1 32  ? 47.787 -14.179 -11.854 1.00 16.46 ?  32  PRO   B O    1 
ATOM   4494 C CB   . PRO   B 1 32  ? 46.540 -17.074 -12.298 1.00 15.52 ?  32  PRO   B CB   1 
ATOM   4495 C CG   . PRO   B 1 32  ? 47.833 -17.415 -11.606 1.00 16.39 ?  32  PRO   B CG   1 
ATOM   4496 C CD   . PRO   B 1 32  ? 48.903 -17.269 -12.648 1.00 16.85 ?  32  PRO   B CD   1 
ATOM   4497 H HA   . PRO   B 1 32  ? 46.373 -15.957 -14.049 1.00 18.78 ?  32  PRO   B HA   1 
ATOM   4498 H HB2  . PRO   B 1 32  ? 45.880 -16.750 -11.666 1.00 18.63 ?  32  PRO   B HB2  1 
ATOM   4499 H HB3  . PRO   B 1 32  ? 46.201 -17.835 -12.798 1.00 18.63 ?  32  PRO   B HB3  1 
ATOM   4500 H HG2  . PRO   B 1 32  ? 47.987 -16.798 -10.872 1.00 19.67 ?  32  PRO   B HG2  1 
ATOM   4501 H HG3  . PRO   B 1 32  ? 47.804 -18.329 -11.279 1.00 19.67 ?  32  PRO   B HG3  1 
ATOM   4502 H HD2  . PRO   B 1 32  ? 49.711 -16.901 -12.251 1.00 20.22 ?  32  PRO   B HD2  1 
ATOM   4503 H HD3  . PRO   B 1 32  ? 49.072 -18.117 -13.078 1.00 20.22 ?  32  PRO   B HD3  1 
ATOM   4504 N N    . THR   B 1 33  ? 45.713 -13.945 -12.721 1.00 15.23 ?  33  THR   B N    1 
ATOM   4505 C CA   . THR   B 1 33  ? 45.428 -12.764 -11.915 1.00 15.07 ?  33  THR   B CA   1 
ATOM   4506 C C    . THR   B 1 33  ? 45.378 -13.112 -10.434 1.00 15.16 ?  33  THR   B C    1 
ATOM   4507 O O    . THR   B 1 33  ? 45.863 -12.338 -9.593  1.00 15.53 ?  33  THR   B O    1 
ATOM   4508 C CB   . THR   B 1 33  ? 44.110 -12.123 -12.357 1.00 16.17 ?  33  THR   B CB   1 
ATOM   4509 O OG1  . THR   B 1 33  ? 44.157 -11.842 -13.758 1.00 16.30 ?  33  THR   B OG1  1 
ATOM   4510 C CG2  . THR   B 1 33  ? 43.866 -10.825 -11.590 1.00 17.43 ?  33  THR   B CG2  1 
ATOM   4511 H H    . THR   B 1 33  ? 45.088 -14.160 -13.281 1.00 18.29 ?  33  THR   B H    1 
ATOM   4512 H HA   . THR   B 1 33  ? 46.134 -12.117 -12.047 1.00 18.09 ?  33  THR   B HA   1 
ATOM   4513 H HB   . THR   B 1 33  ? 43.373 -12.727 -12.173 1.00 19.41 ?  33  THR   B HB   1 
ATOM   4514 H HG1  . THR   B 1 33  ? 43.436 -11.479 -14.005 1.00 19.57 ?  33  THR   B HG1  1 
ATOM   4515 H HG21 . THR   B 1 33  ? 43.129 -10.338 -11.983 1.00 20.92 ?  33  THR   B HG21 1 
ATOM   4516 H HG22 . THR   B 1 33  ? 43.657 -11.020 -10.661 1.00 20.92 ?  33  THR   B HG22 1 
ATOM   4517 H HG23 . THR   B 1 33  ? 44.663 -10.269 -11.620 1.00 20.92 ?  33  THR   B HG23 1 
ATOM   4518 N N    . VAL   B 1 34  ? 44.812 -14.276 -10.094 1.00 14.18 ?  34  VAL   B N    1 
ATOM   4519 C CA   . VAL   B 1 34  ? 44.612 -14.675 -8.704  1.00 14.07 ?  34  VAL   B CA   1 
ATOM   4520 C C    . VAL   B 1 34  ? 45.039 -16.125 -8.534  1.00 12.87 ?  34  VAL   B C    1 
ATOM   4521 O O    . VAL   B 1 34  ? 44.508 -17.014 -9.214  1.00 13.60 ?  34  VAL   B O    1 
ATOM   4522 C CB   . VAL   B 1 34  ? 43.143 -14.527 -8.261  1.00 15.19 ?  34  VAL   B CB   1 
ATOM   4523 C CG1  . VAL   B 1 34  ? 42.982 -14.986 -6.819  1.00 15.32 ?  34  VAL   B CG1  1 
ATOM   4524 C CG2  . VAL   B 1 34  ? 42.649 -13.100 -8.429  1.00 15.71 ?  34  VAL   B CG2  1 
ATOM   4525 H H    . VAL   B 1 34  ? 44.532 -14.864 -10.662 1.00 17.02 ?  34  VAL   B H    1 
ATOM   4526 H HA   . VAL   B 1 34  ? 45.158 -14.120 -8.125  1.00 16.89 ?  34  VAL   B HA   1 
ATOM   4527 H HB   . VAL   B 1 34  ? 42.585 -15.096 -8.814  1.00 18.24 ?  34  VAL   B HB   1 
ATOM   4528 H HG11 . VAL   B 1 34  ? 42.138 -14.652 -6.469  1.00 18.39 ?  34  VAL   B HG11 1 
ATOM   4529 H HG12 . VAL   B 1 34  ? 42.985 -15.956 -6.787  1.00 18.39 ?  34  VAL   B HG12 1 
ATOM   4530 H HG13 . VAL   B 1 34  ? 43.715 -14.633 -6.289  1.00 18.39 ?  34  VAL   B HG13 1 
ATOM   4531 H HG21 . VAL   B 1 34  ? 41.725 -13.045 -8.125  1.00 18.86 ?  34  VAL   B HG21 1 
ATOM   4532 H HG22 . VAL   B 1 34  ? 43.204 -12.508 -7.901  1.00 18.86 ?  34  VAL   B HG22 1 
ATOM   4533 H HG23 . VAL   B 1 34  ? 42.699 -12.856 -9.366  1.00 18.86 ?  34  VAL   B HG23 1 
ATOM   4534 N N    . VAL   B 1 35  ? 45.951 -16.375 -7.601  1.00 12.38 ?  35  VAL   B N    1 
ATOM   4535 C CA   . VAL   B 1 35  ? 46.180 -17.717 -7.081  1.00 12.11 ?  35  VAL   B CA   1 
ATOM   4536 C C    . VAL   B 1 35  ? 45.634 -17.766 -5.664  1.00 11.64 ?  35  VAL   B C    1 
ATOM   4537 O O    . VAL   B 1 35  ? 45.853 -16.849 -4.868  1.00 12.20 ?  35  VAL   B O    1 
ATOM   4538 C CB   . VAL   B 1 35  ? 47.662 -18.150 -7.154  1.00 12.81 ?  35  VAL   B CB   1 
ATOM   4539 C CG1  . VAL   B 1 35  ? 48.561 -17.295 -6.247  1.00 13.60 ?  35  VAL   B CG1  1 
ATOM   4540 C CG2  . VAL   B 1 35  ? 47.804 -19.632 -6.824  1.00 13.41 ?  35  VAL   B CG2  1 
ATOM   4541 H H    . VAL   B 1 35  ? 46.467 -15.774 -7.258  1.00 14.87 ?  35  VAL   B H    1 
ATOM   4542 H HA   . VAL   B 1 35  ? 45.669 -18.345 -7.612  1.00 14.54 ?  35  VAL   B HA   1 
ATOM   4543 H HB   . VAL   B 1 35  ? 47.971 -18.028 -8.065  1.00 15.38 ?  35  VAL   B HB   1 
ATOM   4544 H HG11 . VAL   B 1 35  ? 49.484 -17.533 -6.409  1.00 16.33 ?  35  VAL   B HG11 1 
ATOM   4545 H HG12 . VAL   B 1 35  ? 48.413 -16.361 -6.452  1.00 16.33 ?  35  VAL   B HG12 1 
ATOM   4546 H HG13 . VAL   B 1 35  ? 48.329 -17.473 -5.321  1.00 16.33 ?  35  VAL   B HG13 1 
ATOM   4547 H HG21 . VAL   B 1 35  ? 48.728 -19.898 -6.926  1.00 16.10 ?  35  VAL   B HG21 1 
ATOM   4548 H HG22 . VAL   B 1 35  ? 47.516 -19.784 -5.905  1.00 16.10 ?  35  VAL   B HG22 1 
ATOM   4549 H HG23 . VAL   B 1 35  ? 47.242 -20.149 -7.427  1.00 16.10 ?  35  VAL   B HG23 1 
ATOM   4550 N N    . VAL   B 1 36  ? 44.913 -18.843 -5.351  1.00 11.47 ?  36  VAL   B N    1 
ATOM   4551 C CA   . VAL   B 1 36  ? 44.370 -19.038 -4.017  1.00 11.42 ?  36  VAL   B CA   1 
ATOM   4552 C C    . VAL   B 1 36  ? 45.375 -19.791 -3.157  1.00 11.47 ?  36  VAL   B C    1 
ATOM   4553 O O    . VAL   B 1 36  ? 45.915 -20.825 -3.572  1.00 12.38 ?  36  VAL   B O    1 
ATOM   4554 C CB   . VAL   B 1 36  ? 43.035 -19.794 -4.080  1.00 11.68 ?  36  VAL   B CB   1 
ATOM   4555 C CG1  . VAL   B 1 36  ? 42.545 -20.139 -2.686  1.00 12.79 ?  36  VAL   B CG1  1 
ATOM   4556 C CG2  . VAL   B 1 36  ? 42.007 -18.960 -4.841  1.00 12.61 ?  36  VAL   B CG2  1 
ATOM   4557 H H    . VAL   B 1 36  ? 44.732 -19.488 -5.896  1.00 13.77 ?  36  VAL   B H    1 
ATOM   4558 H HA   . VAL   B 1 36  ? 44.205 -18.174 -3.608  1.00 13.71 ?  36  VAL   B HA   1 
ATOM   4559 H HB   . VAL   B 1 36  ? 43.160 -20.625 -4.563  1.00 14.02 ?  36  VAL   B HB   1 
ATOM   4560 H HG11 . VAL   B 1 36  ? 41.599 -20.356 -2.725  1.00 15.35 ?  36  VAL   B HG11 1 
ATOM   4561 H HG12 . VAL   B 1 36  ? 43.044 -20.895 -2.347  1.00 15.35 ?  36  VAL   B HG12 1 
ATOM   4562 H HG13 . VAL   B 1 36  ? 42.676 -19.366 -2.106  1.00 15.35 ?  36  VAL   B HG13 1 
ATOM   4563 H HG21 . VAL   B 1 36  ? 41.156 -19.433 -4.849  1.00 15.14 ?  36  VAL   B HG21 1 
ATOM   4564 H HG22 . VAL   B 1 36  ? 41.902 -18.104 -4.401  1.00 15.14 ?  36  VAL   B HG22 1 
ATOM   4565 H HG23 . VAL   B 1 36  ? 42.315 -18.830 -5.752  1.00 15.14 ?  36  VAL   B HG23 1 
ATOM   4566 N N    . ASN   B 1 37  ? 45.587 -19.301 -1.942  1.00 11.67 ?  37  ASN   B N    1 
ATOM   4567 C CA   . ASN   B 1 37  ? 46.349 -20.015 -0.935  1.00 12.01 ?  37  ASN   B CA   1 
ATOM   4568 C C    . ASN   B 1 37  ? 45.405 -20.683 0.056   1.00 12.15 ?  37  ASN   B C    1 
ATOM   4569 O O    . ASN   B 1 37  ? 44.400 -20.096 0.469   1.00 12.44 ?  37  ASN   B O    1 
ATOM   4570 C CB   . ASN   B 1 37  ? 47.281 -19.065 -0.182  1.00 11.61 ?  37  ASN   B CB   1 
ATOM   4571 C CG   . ASN   B 1 37  ? 48.126 -19.782 0.840   1.00 12.39 ?  37  ASN   B CG   1 
ATOM   4572 O OD1  . ASN   B 1 37  ? 48.464 -20.957 0.667   1.00 13.25 ?  37  ASN   B OD1  1 
ATOM   4573 N ND2  . ASN   B 1 37  ? 48.467 -19.085 1.917   1.00 12.42 ?  37  ASN   B ND2  1 
ATOM   4574 H H    . ASN   B 1 37  ? 45.287 -18.539 -1.670  1.00 14.01 ?  37  ASN   B H    1 
ATOM   4575 H HA   . ASN   B 1 37  ? 46.887 -20.702 -1.358  1.00 14.42 ?  37  ASN   B HA   1 
ATOM   4576 H HB2  . ASN   B 1 37  ? 47.883 -18.645 -0.814  1.00 13.94 ?  37  ASN   B HB2  1 
ATOM   4577 H HB3  . ASN   B 1 37  ? 46.754 -18.395 0.277   1.00 13.94 ?  37  ASN   B HB3  1 
ATOM   4578 H HD21 . ASN   B 1 37  ? 48.955 -19.447 2.529   1.00 14.92 ?  37  ASN   B HD21 1 
ATOM   4579 H HD22 . ASN   B 1 37  ? 48.220 -18.271 2.002   1.00 14.92 ?  37  ASN   B HD22 1 
ATOM   4580 N N    . ALA   B 1 38  ? 45.745 -21.917 0.430   1.00 12.26 ?  38  ALA   B N    1 
ATOM   4581 C CA   . ALA   B 1 38  ? 45.089 -22.648 1.515   1.00 13.01 ?  38  ALA   B CA   1 
ATOM   4582 C C    . ALA   B 1 38  ? 45.676 -22.159 2.840   1.00 12.59 ?  38  ALA   B C    1 
ATOM   4583 O O    . ALA   B 1 38  ? 46.576 -22.763 3.429   1.00 13.58 ?  38  ALA   B O    1 
ATOM   4584 C CB   . ALA   B 1 38  ? 45.300 -24.146 1.335   1.00 14.44 ?  38  ALA   B CB   1 
ATOM   4585 H H    . ALA   B 1 38  ? 46.394 -22.363 0.071   1.00 14.72 ?  38  ALA   B H    1 
ATOM   4586 H HA   . ALA   B 1 38  ? 44.136 -22.461 1.502   1.00 15.62 ?  38  ALA   B HA   1 
ATOM   4587 H HB1  . ALA   B 1 38  ? 44.853 -24.618 2.060   1.00 17.33 ?  38  ALA   B HB1  1 
ATOM   4588 H HB2  . ALA   B 1 38  ? 44.918 -24.420 0.485   1.00 17.33 ?  38  ALA   B HB2  1 
ATOM   4589 H HB3  . ALA   B 1 38  ? 46.247 -24.339 1.352   1.00 17.33 ?  38  ALA   B HB3  1 
ATOM   4590 N N    . ALA   B 1 39  ? 45.165 -21.019 3.300   1.00 12.37 ?  39  ALA   B N    1 
ATOM   4591 C CA   . ALA   B 1 39  ? 45.721 -20.290 4.428   1.00 12.75 ?  39  ALA   B CA   1 
ATOM   4592 C C    . ALA   B 1 39  ? 45.098 -20.721 5.756   1.00 12.57 ?  39  ALA   B C    1 
ATOM   4593 O O    . ALA   B 1 39  ? 44.060 -21.381 5.805   1.00 13.77 ?  39  ALA   B O    1 
ATOM   4594 C CB   . ALA   B 1 39  ? 45.502 -18.790 4.232   1.00 13.42 ?  39  ALA   B CB   1 
ATOM   4595 H H    . ALA   B 1 39  ? 44.470 -20.641 2.960   1.00 14.85 ?  39  ALA   B H    1 
ATOM   4596 H HA   . ALA   B 1 39  ? 46.669 -20.457 4.476   1.00 15.31 ?  39  ALA   B HA   1 
ATOM   4597 H HB1  . ALA   B 1 39  ? 45.877 -18.316 4.992   1.00 16.11 ?  39  ALA   B HB1  1 
ATOM   4598 H HB2  . ALA   B 1 39  ? 45.950 -18.512 3.417   1.00 16.11 ?  39  ALA   B HB2  1 
ATOM   4599 H HB3  . ALA   B 1 39  ? 44.552 -18.610 4.165   1.00 16.11 ?  39  ALA   B HB3  1 
ATOM   4600 N N    . ASN   B 1 40  ? 45.744 -20.312 6.842   1.00 13.09 ?  40  ASN   B N    1 
ATOM   4601 C CA   . ASN   B 1 40  ? 45.176 -20.356 8.179   1.00 13.83 ?  40  ASN   B CA   1 
ATOM   4602 C C    . ASN   B 1 40  ? 44.993 -18.928 8.696   1.00 13.51 ?  40  ASN   B C    1 
ATOM   4603 O O    . ASN   B 1 40  ? 45.392 -17.954 8.051   1.00 13.42 ?  40  ASN   B O    1 
ATOM   4604 C CB   . ASN   B 1 40  ? 46.026 -21.226 9.119   1.00 14.51 ?  40  ASN   B CB   1 
ATOM   4605 C CG   . ASN   B 1 40  ? 47.476 -20.787 9.180   1.00 15.58 ?  40  ASN   B CG   1 
ATOM   4606 O OD1  . ASN   B 1 40  ? 47.776 -19.607 9.336   1.00 17.52 ?  40  ASN   B OD1  1 
ATOM   4607 N ND2  . ASN   B 1 40  ? 48.385 -21.740 9.064   1.00 15.79 ?  40  ASN   B ND2  1 
ATOM   4608 H H    . ASN   B 1 40  ? 46.540 -19.992 6.823   1.00 15.71 ?  40  ASN   B H    1 
ATOM   4609 H HA   . ASN   B 1 40  ? 44.290 -20.756 8.126   1.00 16.60 ?  40  ASN   B HA   1 
ATOM   4610 H HB2  . ASN   B 1 40  ? 45.653 -21.173 10.012  1.00 17.42 ?  40  ASN   B HB2  1 
ATOM   4611 H HB3  . ASN   B 1 40  ? 45.997 -22.142 8.800   1.00 17.42 ?  40  ASN   B HB3  1 
ATOM   4612 H HD21 . ASN   B 1 40  ? 49.224 -21.545 9.091   1.00 18.95 ?  40  ASN   B HD21 1 
ATOM   4613 H HD22 . ASN   B 1 40  ? 48.141 -22.559 8.955   1.00 18.95 ?  40  ASN   B HD22 1 
ATOM   4614 N N    . VAL   B 1 41  ? 44.341 -18.796 9.854   1.00 14.29 ?  41  VAL   B N    1 
ATOM   4615 C CA   . VAL   B 1 41  ? 43.886 -17.471 10.289  1.00 14.87 ?  41  VAL   B CA   1 
ATOM   4616 C C    . VAL   B 1 41  ? 45.040 -16.521 10.584  1.00 14.85 ?  41  VAL   B C    1 
ATOM   4617 O O    . VAL   B 1 41  ? 44.865 -15.299 10.513  1.00 14.85 ?  41  VAL   B O    1 
ATOM   4618 C CB   . VAL   B 1 41  ? 42.912 -17.533 11.481  1.00 15.82 ?  41  VAL   B CB   1 
ATOM   4619 C CG1  . VAL   B 1 41  ? 41.608 -18.205 11.083  1.00 17.03 ?  41  VAL   B CG1  1 
ATOM   4620 C CG2  . VAL   B 1 41  ? 43.558 -18.213 12.679  1.00 17.32 ?  41  VAL   B CG2  1 
ATOM   4621 H H    . VAL   B 1 41  ? 44.148 -19.436 10.383  1.00 17.15 ?  41  VAL   B H    1 
ATOM   4622 H HA   . VAL   B 1 41  ? 43.396 -17.070 9.559   1.00 17.85 ?  41  VAL   B HA   1 
ATOM   4623 H HB   . VAL   B 1 41  ? 42.696 -16.625 11.751  1.00 18.99 ?  41  VAL   B HB   1 
ATOM   4624 H HG11 . VAL   B 1 41  ? 41.006 -18.205 11.842  1.00 20.45 ?  41  VAL   B HG11 1 
ATOM   4625 H HG12 . VAL   B 1 41  ? 41.212 -17.712 10.346  1.00 20.45 ?  41  VAL   B HG12 1 
ATOM   4626 H HG13 . VAL   B 1 41  ? 41.796 -19.116 10.807  1.00 20.45 ?  41  VAL   B HG13 1 
ATOM   4627 H HG21 . VAL   B 1 41  ? 42.918 -18.243 13.408  1.00 20.79 ?  41  VAL   B HG21 1 
ATOM   4628 H HG22 . VAL   B 1 41  ? 43.816 -19.114 12.431  1.00 20.79 ?  41  VAL   B HG22 1 
ATOM   4629 H HG23 . VAL   B 1 41  ? 44.340 -17.707 12.949  1.00 20.79 ?  41  VAL   B HG23 1 
ATOM   4630 N N    . TYR   B 1 42  ? 46.207 -17.039 10.962  1.00 14.65 ?  42  TYR   B N    1 
ATOM   4631 C CA   . TYR   B 1 42  ? 47.358 -16.185 11.219  1.00 14.80 ?  42  TYR   B CA   1 
ATOM   4632 C C    . TYR   B 1 42  ? 48.314 -16.109 10.032  1.00 14.44 ?  42  TYR   B C    1 
ATOM   4633 O O    . TYR   B 1 42  ? 49.393 -15.517 10.156  1.00 15.64 ?  42  TYR   B O    1 
ATOM   4634 C CB   . TYR   B 1 42  ? 48.065 -16.578 12.524  1.00 17.39 ?  42  TYR   B CB   1 
ATOM   4635 C CG   . TYR   B 1 42  ? 47.460 -15.902 13.753  1.00 18.22 ?  42  TYR   B CG   1 
ATOM   4636 C CD1  . TYR   B 1 42  ? 47.657 -14.541 13.987  1.00 17.93 ?  42  TYR   B CD1  1 
ATOM   4637 C CD2  . TYR   B 1 42  ? 46.699 -16.612 14.670  1.00 20.26 ?  42  TYR   B CD2  1 
ATOM   4638 C CE1  . TYR   B 1 42  ? 47.115 -13.915 15.093  1.00 19.30 ?  42  TYR   B CE1  1 
ATOM   4639 C CE2  . TYR   B 1 42  ? 46.154 -15.993 15.783  1.00 20.29 ?  42  TYR   B CE2  1 
ATOM   4640 C CZ   . TYR   B 1 42  ? 46.362 -14.639 15.986  1.00 21.12 ?  42  TYR   B CZ   1 
ATOM   4641 O OH   . TYR   B 1 42  ? 45.828 -14.005 17.087  1.00 23.98 ?  42  TYR   B OH   1 
ATOM   4642 H H    . TYR   B 1 42  ? 46.360 -17.882 11.068  1.00 17.59 ?  42  TYR   B H    1 
ATOM   4643 H HA   . TYR   B 1 42  ? 47.032 -15.288 11.353  1.00 17.77 ?  42  TYR   B HA   1 
ATOM   4644 H HB2  . TYR   B 1 42  ? 47.998 -17.537 12.648  1.00 20.87 ?  42  TYR   B HB2  1 
ATOM   4645 H HB3  . TYR   B 1 42  ? 49.001 -16.317 12.467  1.00 20.87 ?  42  TYR   B HB3  1 
ATOM   4646 H HD1  . TYR   B 1 42  ? 48.168 -14.044 13.384  1.00 21.52 ?  42  TYR   B HD1  1 
ATOM   4647 H HD2  . TYR   B 1 42  ? 46.555 -17.522 14.533  1.00 24.32 ?  42  TYR   B HD2  1 
ATOM   4648 H HE1  . TYR   B 1 42  ? 47.258 -13.007 15.231  1.00 23.16 ?  42  TYR   B HE1  1 
ATOM   4649 H HE2  . TYR   B 1 42  ? 45.641 -16.484 16.386  1.00 24.36 ?  42  TYR   B HE2  1 
ATOM   4650 H HH   . TYR   B 1 42  ? 46.038 -13.195 17.078  1.00 28.78 ?  42  TYR   B HH   1 
ATOM   4651 N N    . LEU   B 1 43  ? 47.919 -16.634 8.875   1.00 13.14 ?  43  LEU   B N    1 
ATOM   4652 C CA   . LEU   B 1 43  ? 48.731 -16.565 7.662   1.00 13.25 ?  43  LEU   B CA   1 
ATOM   4653 C C    . LEU   B 1 43  ? 50.146 -17.071 7.918   1.00 13.61 ?  43  LEU   B C    1 
ATOM   4654 O O    . LEU   B 1 43  ? 51.129 -16.483 7.457   1.00 14.67 ?  43  LEU   B O    1 
ATOM   4655 C CB   . LEU   B 1 43  ? 48.749 -15.159 7.055   1.00 13.55 ?  43  LEU   B CB   1 
ATOM   4656 C CG   . LEU   B 1 43  ? 47.393 -14.549 6.691   1.00 13.66 ?  43  LEU   B CG   1 
ATOM   4657 C CD1  . LEU   B 1 43  ? 47.602 -13.170 6.070   1.00 14.97 ?  43  LEU   B CD1  1 
ATOM   4658 C CD2  . LEU   B 1 43  ? 46.607 -15.447 5.746   1.00 14.13 ?  43  LEU   B CD2  1 
ATOM   4659 H H    . LEU   B 1 43  ? 47.173 -17.051 8.765   1.00 15.78 ?  43  LEU   B H    1 
ATOM   4660 H HA   . LEU   B 1 43  ? 48.328 -17.154 7.000   1.00 15.91 ?  43  LEU   B HA   1 
ATOM   4661 H HB2  . LEU   B 1 43  ? 49.172 -14.560 7.686   1.00 16.26 ?  43  LEU   B HB2  1 
ATOM   4662 H HB3  . LEU   B 1 43  ? 49.271 -15.190 6.237   1.00 16.26 ?  43  LEU   B HB3  1 
ATOM   4663 H HG   . LEU   B 1 43  ? 46.871 -14.431 7.499   1.00 16.40 ?  43  LEU   B HG   1 
ATOM   4664 H HD11 . LEU   B 1 43  ? 46.738 -12.790 5.846   1.00 17.98 ?  43  LEU   B HD11 1 
ATOM   4665 H HD12 . LEU   B 1 43  ? 48.056 -12.602 6.713   1.00 17.98 ?  43  LEU   B HD12 1 
ATOM   4666 H HD13 . LEU   B 1 43  ? 48.142 -13.263 5.270   1.00 17.98 ?  43  LEU   B HD13 1 
ATOM   4667 H HD21 . LEU   B 1 43  ? 45.804 -14.979 5.456   1.00 16.96 ?  43  LEU   B HD21 1 
ATOM   4668 H HD22 . LEU   B 1 43  ? 47.156 -15.664 4.979   1.00 16.96 ?  43  LEU   B HD22 1 
ATOM   4669 H HD23 . LEU   B 1 43  ? 46.357 -16.260 6.217   1.00 16.96 ?  43  LEU   B HD23 1 
ATOM   4670 N N    . LYS   B 1 44  ? 50.244 -18.185 8.643   1.00 13.70 ?  44  LYS   B N    1 
ATOM   4671 C CA   . LYS   B 1 44  ? 51.513 -18.856 8.890   1.00 14.09 ?  44  LYS   B CA   1 
ATOM   4672 C C    . LYS   B 1 44  ? 51.636 -19.977 7.868   1.00 13.62 ?  44  LYS   B C    1 
ATOM   4673 O O    . LYS   B 1 44  ? 50.943 -20.995 7.958   1.00 15.06 ?  44  LYS   B O    1 
ATOM   4674 C CB   . LYS   B 1 44  ? 51.583 -19.360 10.330  1.00 15.86 ?  44  LYS   B CB   1 
ATOM   4675 C CG   . LYS   B 1 44  ? 51.754 -18.231 11.338  1.00 18.96 ?  44  LYS   B CG   1 
ATOM   4676 C CD   . LYS   B 1 44  ? 52.991 -17.405 10.959  1.00 22.48 ?  44  LYS   B CD   1 
ATOM   4677 C CE   . LYS   B 1 44  ? 53.378 -16.375 11.986  1.00 25.57 ?  44  LYS   B CE   1 
ATOM   4678 N NZ   . LYS   B 1 44  ? 54.668 -15.705 11.664  1.00 26.83 ?  44  LYS   B NZ   1 
ATOM   4679 H H    . LYS   B 1 44  ? 49.567 -18.573 9.010   1.00 16.45 ?  44  LYS   B H    1 
ATOM   4680 H HA   . LYS   B 1 44  ? 52.238 -18.245 8.717   1.00 16.91 ?  44  LYS   B HA   1 
ATOM   4681 H HB2  . LYS   B 1 44  ? 50.754 -19.825 10.543  1.00 19.04 ?  44  LYS   B HB2  1 
ATOM   4682 H HB3  . LYS   B 1 44  ? 52.332 -19.962 10.421  1.00 19.04 ?  44  LYS   B HB3  1 
ATOM   4683 H HG2  . LYS   B 1 44  ? 50.977 -17.654 11.327  1.00 22.76 ?  44  LYS   B HG2  1 
ATOM   4684 H HG3  . LYS   B 1 44  ? 51.892 -18.605 12.226  1.00 22.76 ?  44  LYS   B HG3  1 
ATOM   4685 H HD2  . LYS   B 1 44  ? 53.741 -18.017 10.822  1.00 26.99 ?  44  LYS   B HD2  1 
ATOM   4686 H HD3  . LYS   B 1 44  ? 52.808 -16.928 10.135  1.00 26.99 ?  44  LYS   B HD3  1 
ATOM   4687 H HE2  . LYS   B 1 44  ? 52.680 -15.702 12.040  1.00 30.69 ?  44  LYS   B HE2  1 
ATOM   4688 H HE3  . LYS   B 1 44  ? 53.495 -16.823 12.827  1.00 30.69 ?  44  LYS   B HE3  1 
ATOM   4689 H HZ1  . LYS   B 1 44  ? 54.859 -15.101 12.289  1.00 32.21 ?  44  LYS   B HZ1  1 
ATOM   4690 H HZ2  . LYS   B 1 44  ? 55.324 -16.307 11.633  1.00 32.21 ?  44  LYS   B HZ2  1 
ATOM   4691 H HZ3  . LYS   B 1 44  ? 54.615 -15.296 10.874  1.00 32.21 ?  44  LYS   B HZ3  1 
ATOM   4692 N N    . HIS   B 1 45  ? 52.488 -19.761 6.872   1.00 13.70 ?  45  HIS   B N    1 
ATOM   4693 C CA   . HIS   B 1 45  ? 52.517 -20.599 5.674   1.00 13.65 ?  45  HIS   B CA   1 
ATOM   4694 C C    . HIS   B 1 45  ? 53.538 -21.722 5.835   1.00 16.08 ?  45  HIS   B C    1 
ATOM   4695 O O    . HIS   B 1 45  ? 54.588 -21.750 5.201   1.00 18.77 ?  45  HIS   B O    1 
ATOM   4696 C CB   . HIS   B 1 45  ? 52.827 -19.750 4.454   1.00 13.94 ?  45  HIS   B CB   1 
ATOM   4697 C CG   . HIS   B 1 45  ? 51.951 -18.551 4.338   1.00 14.08 ?  45  HIS   B CG   1 
ATOM   4698 N ND1  . HIS   B 1 45  ? 50.573 -18.633 4.324   1.00 14.19 ?  45  HIS   B ND1  1 
ATOM   4699 C CD2  . HIS   B 1 45  ? 52.265 -17.239 4.246   1.00 14.42 ?  45  HIS   B CD2  1 
ATOM   4700 C CE1  . HIS   B 1 45  ? 50.081 -17.412 4.217   1.00 13.71 ?  45  HIS   B CE1  1 
ATOM   4701 N NE2  . HIS   B 1 45  ? 51.084 -16.550 4.166   1.00 14.25 ?  45  HIS   B NE2  1 
ATOM   4702 H H    . HIS   B 1 45  ? 53.056 -19.114 6.861   1.00 16.44 ?  45  HIS   B H    1 
ATOM   4703 H HA   . HIS   B 1 45  ? 51.642 -20.999 5.546   1.00 16.38 ?  45  HIS   B HA   1 
ATOM   4704 H HB2  . HIS   B 1 45  ? 53.744 -19.443 4.507   1.00 16.73 ?  45  HIS   B HB2  1 
ATOM   4705 H HB3  . HIS   B 1 45  ? 52.700 -20.285 3.656   1.00 16.73 ?  45  HIS   B HB3  1 
ATOM   4706 H HD2  . HIS   B 1 45  ? 53.122 -16.874 4.240   1.00 17.31 ?  45  HIS   B HD2  1 
ATOM   4707 H HE1  . HIS   B 1 45  ? 49.179 -17.192 4.175   1.00 16.46 ?  45  HIS   B HE1  1 
ATOM   4708 H HE2  . HIS   B 1 45  ? 51.008 -15.694 4.102   1.00 17.11 ?  45  HIS   B HE2  1 
ATOM   4709 N N    A GLY   B 1 46  ? 53.180 -22.682 6.683   0.48 17.10 ?  46  GLY   B N    1 
ATOM   4710 N N    B GLY   B 1 46  ? 53.189 -22.672 6.694   0.52 17.05 ?  46  GLY   B N    1 
ATOM   4711 C CA   A GLY   B 1 46  ? 54.105 -23.721 7.088   0.48 18.91 ?  46  GLY   B CA   1 
ATOM   4712 C CA   B GLY   B 1 46  ? 54.115 -23.723 7.060   0.52 18.78 ?  46  GLY   B CA   1 
ATOM   4713 C C    A GLY   B 1 46  ? 54.171 -24.955 6.208   0.48 20.30 ?  46  GLY   B C    1 
ATOM   4714 C C    B GLY   B 1 46  ? 54.167 -24.895 6.100   0.52 20.05 ?  46  GLY   B C    1 
ATOM   4715 O O    A GLY   B 1 46  ? 55.266 -25.417 5.868   0.48 22.74 ?  46  GLY   B O    1 
ATOM   4716 O O    B GLY   B 1 46  ? 55.235 -25.234 5.578   0.52 22.40 ?  46  GLY   B O    1 
ATOM   4717 H H    A GLY   B 1 46  ? 52.401 -22.737 7.047   0.48 20.53 ?  46  GLY   B H    1 
ATOM   4718 H H    B GLY   B 1 46  ? 52.420 -22.718 7.082   0.52 20.47 ?  46  GLY   B H    1 
ATOM   4719 H HA2  A GLY   B 1 46  ? 54.994 -23.338 7.131   0.48 22.70 ?  46  GLY   B HA2  1 
ATOM   4720 H HA2  B GLY   B 1 46  ? 55.004 -23.344 7.121   0.52 22.54 ?  46  GLY   B HA2  1 
ATOM   4721 H HA3  A GLY   B 1 46  ? 53.864 -24.013 7.979   0.48 22.70 ?  46  GLY   B HA3  1 
ATOM   4722 H HA3  B GLY   B 1 46  ? 53.870 -24.056 7.938   0.52 22.54 ?  46  GLY   B HA3  1 
ATOM   4723 N N    . GLY   B 1 47  ? 53.021 -25.524 5.849   1.00 19.75 ?  47  GLY   B N    1 
ATOM   4724 C CA   . GLY   B 1 47  ? 52.982 -26.802 5.165   1.00 17.79 ?  47  GLY   B CA   1 
ATOM   4725 C C    . GLY   B 1 47  ? 52.023 -26.798 3.991   1.00 15.69 ?  47  GLY   B C    1 
ATOM   4726 O O    . GLY   B 1 47  ? 51.347 -25.807 3.721   1.00 15.29 ?  47  GLY   B O    1 
ATOM   4727 H H    A GLY   B 1 47  ? 52.242 -25.189 6.006   0.48 23.70 ?  47  GLY   B H    1 
ATOM   4728 H H    B GLY   B 1 47  ? 52.243 -25.221 6.067   0.52 23.70 ?  47  GLY   B H    1 
ATOM   4729 H HA2  . GLY   B 1 47  ? 53.865 -27.024 4.831   1.00 21.36 ?  47  GLY   B HA2  1 
ATOM   4730 H HA3  . GLY   B 1 47  ? 52.706 -27.490 5.787   1.00 21.36 ?  47  GLY   B HA3  1 
ATOM   4731 N N    . GLY   B 1 48  ? 51.978 -27.939 3.308   1.00 15.11 ?  48  GLY   B N    1 
ATOM   4732 C CA   . GLY   B 1 48  ? 51.038 -28.099 2.214   1.00 14.63 ?  48  GLY   B CA   1 
ATOM   4733 C C    . GLY   B 1 48  ? 51.176 -27.003 1.182   1.00 14.05 ?  48  GLY   B C    1 
ATOM   4734 O O    . GLY   B 1 48  ? 52.275 -26.526 0.880   1.00 14.64 ?  48  GLY   B O    1 
ATOM   4735 H H    . GLY   B 1 48  ? 52.485 -28.614 3.449   1.00 18.14 ?  48  GLY   B H    1 
ATOM   4736 H HA2  . GLY   B 1 48  ? 51.187 -28.961 1.785   1.00 17.57 ?  48  GLY   B HA2  1 
ATOM   4737 H HA3  . GLY   B 1 48  ? 50.132 -28.087 2.561   1.00 17.57 ?  48  GLY   B HA3  1 
ATOM   4738 N N    . VAL   B 1 49  ? 50.030 -26.579 0.647   1.00 13.93 ?  49  VAL   B N    1 
ATOM   4739 C CA   . VAL   B 1 49  ? 50.012 -25.574 -0.408  1.00 13.67 ?  49  VAL   B CA   1 
ATOM   4740 C C    . VAL   B 1 49  ? 50.665 -24.281 0.068   1.00 12.67 ?  49  VAL   B C    1 
ATOM   4741 O O    . VAL   B 1 49  ? 51.450 -23.662 -0.656  1.00 13.53 ?  49  VAL   B O    1 
ATOM   4742 C CB   . VAL   B 1 49  ? 48.565 -25.327 -0.878  1.00 15.22 ?  49  VAL   B CB   1 
ATOM   4743 C CG1  . VAL   B 1 49  ? 48.483 -24.089 -1.761  1.00 15.53 ?  49  VAL   B CG1  1 
ATOM   4744 C CG2  . VAL   B 1 49  ? 48.024 -26.550 -1.611  1.00 17.28 ?  49  VAL   B CG2  1 
ATOM   4745 H H    . VAL   B 1 49  ? 49.248 -26.851 0.884   1.00 16.73 ?  49  VAL   B H    1 
ATOM   4746 H HA   . VAL   B 1 49  ? 50.518 -25.899 -1.167  1.00 16.41 ?  49  VAL   B HA   1 
ATOM   4747 H HB   . VAL   B 1 49  ? 48.004 -25.174 -0.103  1.00 18.27 ?  49  VAL   B HB   1 
ATOM   4748 H HG11 . VAL   B 1 49  ? 47.652 -24.115 -2.261  1.00 18.65 ?  49  VAL   B HG11 1 
ATOM   4749 H HG12 . VAL   B 1 49  ? 48.503 -23.297 -1.200  1.00 18.65 ?  49  VAL   B HG12 1 
ATOM   4750 H HG13 . VAL   B 1 49  ? 49.235 -24.085 -2.371  1.00 18.65 ?  49  VAL   B HG13 1 
ATOM   4751 H HG21 . VAL   B 1 49  ? 47.112 -26.373 -1.892  1.00 20.75 ?  49  VAL   B HG21 1 
ATOM   4752 H HG22 . VAL   B 1 49  ? 48.580 -26.727 -2.385  1.00 20.75 ?  49  VAL   B HG22 1 
ATOM   4753 H HG23 . VAL   B 1 49  ? 48.042 -27.310 -1.009  1.00 20.75 ?  49  VAL   B HG23 1 
ATOM   4754 N N    . ALA   B 1 50  ? 50.323 -23.829 1.273   1.00 12.65 ?  50  ALA   B N    1 
ATOM   4755 C CA   . ALA   B 1 50  ? 50.842 -22.544 1.737   1.00 12.78 ?  50  ALA   B CA   1 
ATOM   4756 C C    . ALA   B 1 50  ? 52.360 -22.570 1.839   1.00 13.15 ?  50  ALA   B C    1 
ATOM   4757 O O    . ALA   B 1 50  ? 53.037 -21.605 1.457   1.00 13.10 ?  50  ALA   B O    1 
ATOM   4758 C CB   . ALA   B 1 50  ? 50.219 -22.191 3.080   1.00 13.31 ?  50  ALA   B CB   1 
ATOM   4759 H H    . ALA   B 1 50  ? 49.797 -24.227 1.823   1.00 15.19 ?  50  ALA   B H    1 
ATOM   4760 H HA   . ALA   B 1 50  ? 50.604 -21.854 1.103   1.00 15.35 ?  50  ALA   B HA   1 
ATOM   4761 H HB1  . ALA   B 1 50  ? 50.577 -21.335 3.378   1.00 15.98 ?  50  ALA   B HB1  1 
ATOM   4762 H HB2  . ALA   B 1 50  ? 49.258 -22.124 2.975   1.00 15.98 ?  50  ALA   B HB2  1 
ATOM   4763 H HB3  . ALA   B 1 50  ? 50.438 -22.880 3.724   1.00 15.98 ?  50  ALA   B HB3  1 
ATOM   4764 N N    . GLY   B 1 51  ? 52.915 -23.661 2.362   1.00 13.19 ?  51  GLY   B N    1 
ATOM   4765 C CA   . GLY   B 1 51  ? 54.359 -23.763 2.435   1.00 14.19 ?  51  GLY   B CA   1 
ATOM   4766 C C    . GLY   B 1 51  ? 55.000 -23.720 1.066   1.00 13.93 ?  51  GLY   B C    1 
ATOM   4767 O O    . GLY   B 1 51  ? 56.050 -23.095 0.879   1.00 14.75 ?  51  GLY   B O    1 
ATOM   4768 H H    . GLY   B 1 51  ? 52.486 -24.338 2.671   1.00 15.84 ?  51  GLY   B H    1 
ATOM   4769 H HA2  . GLY   B 1 51  ? 54.714 -23.035 2.960   1.00 17.04 ?  51  GLY   B HA2  1 
ATOM   4770 H HA3  . GLY   B 1 51  ? 54.603 -24.603 2.866   1.00 17.04 ?  51  GLY   B HA3  1 
ATOM   4771 N N    . ALA   B 1 52  ? 54.396 -24.403 0.093   1.00 13.66 ?  52  ALA   B N    1 
ATOM   4772 C CA   . ALA   B 1 52  ? 54.957 -24.424 -1.251  1.00 13.75 ?  52  ALA   B CA   1 
ATOM   4773 C C    . ALA   B 1 52  ? 54.877 -23.051 -1.908  1.00 13.23 ?  52  ALA   B C    1 
ATOM   4774 O O    . ALA   B 1 52  ? 55.849 -22.601 -2.537  1.00 13.97 ?  52  ALA   B O    1 
ATOM   4775 C CB   . ALA   B 1 52  ? 54.257 -25.474 -2.106  1.00 14.74 ?  52  ALA   B CB   1 
ATOM   4776 H H    . ALA   B 1 52  ? 53.668 -24.857 0.183   1.00 16.40 ?  52  ALA   B H    1 
ATOM   4777 H HA   . ALA   B 1 52  ? 55.890 -24.668 -1.196  1.00 16.51 ?  52  ALA   B HA   1 
ATOM   4778 H HB1  . ALA   B 1 52  ? 54.646 -25.469 -2.998  1.00 17.69 ?  52  ALA   B HB1  1 
ATOM   4779 H HB2  . ALA   B 1 52  ? 54.384 -26.348 -1.701  1.00 17.69 ?  52  ALA   B HB2  1 
ATOM   4780 H HB3  . ALA   B 1 52  ? 53.312 -25.268 -2.159  1.00 17.69 ?  52  ALA   B HB3  1 
ATOM   4781 N N    . LEU   B 1 53  ? 53.733 -22.370 -1.792  1.00 12.81 ?  53  LEU   B N    1 
ATOM   4782 C CA   . LEU   B 1 53  ? 53.627 -21.036 -2.366  1.00 12.91 ?  53  LEU   B CA   1 
ATOM   4783 C C    . LEU   B 1 53  ? 54.639 -20.099 -1.723  1.00 13.03 ?  53  LEU   B C    1 
ATOM   4784 O O    . LEU   B 1 53  ? 55.339 -19.352 -2.416  1.00 13.28 ?  53  LEU   B O    1 
ATOM   4785 C CB   . LEU   B 1 53  ? 52.207 -20.479 -2.204  1.00 13.55 ?  53  LEU   B CB   1 
ATOM   4786 C CG   . LEU   B 1 53  ? 51.070 -21.206 -2.933  1.00 14.19 ?  53  LEU   B CG   1 
ATOM   4787 C CD1  . LEU   B 1 53  ? 49.747 -20.584 -2.592  1.00 15.57 ?  53  LEU   B CD1  1 
ATOM   4788 C CD2  . LEU   B 1 53  ? 51.274 -21.218 -4.436  1.00 16.32 ?  53  LEU   B CD2  1 
ATOM   4789 H H    . LEU   B 1 53  ? 53.027 -22.648 -1.392  1.00 15.38 ?  53  LEU   B H    1 
ATOM   4790 H HA   . LEU   B 1 53  ? 53.830 -21.080 -3.315  1.00 15.50 ?  53  LEU   B HA   1 
ATOM   4791 H HB2  . LEU   B 1 53  ? 51.992 -20.491 -1.259  1.00 16.27 ?  53  LEU   B HB2  1 
ATOM   4792 H HB3  . LEU   B 1 53  ? 52.208 -19.562 -2.518  1.00 16.27 ?  53  LEU   B HB3  1 
ATOM   4793 H HG   . LEU   B 1 53  ? 51.049 -22.124 -2.629  1.00 17.03 ?  53  LEU   B HG   1 
ATOM   4794 H HD11 . LEU   B 1 53  ? 49.043 -21.059 -3.065  1.00 18.69 ?  53  LEU   B HD11 1 
ATOM   4795 H HD12 . LEU   B 1 53  ? 49.600 -20.649 -1.635  1.00 18.69 ?  53  LEU   B HD12 1 
ATOM   4796 H HD13 . LEU   B 1 53  ? 49.751 -19.652 -2.863  1.00 18.69 ?  53  LEU   B HD13 1 
ATOM   4797 H HD21 . LEU   B 1 53  ? 50.608 -21.798 -4.838  1.00 19.59 ?  53  LEU   B HD21 1 
ATOM   4798 H HD22 . LEU   B 1 53  ? 51.174 -20.318 -4.779  1.00 19.59 ?  53  LEU   B HD22 1 
ATOM   4799 H HD23 . LEU   B 1 53  ? 52.162 -21.554 -4.640  1.00 19.59 ?  53  LEU   B HD23 1 
ATOM   4800 N N    . ASN   B 1 54  ? 54.723 -20.109 -0.396  1.00 12.86 ?  54  ASN   B N    1 
ATOM   4801 C CA   . ASN   B 1 54  ? 55.643 -19.193 0.264   1.00 13.37 ?  54  ASN   B CA   1 
ATOM   4802 C C    . ASN   B 1 54  ? 57.086 -19.480 -0.131  1.00 13.95 ?  54  ASN   B C    1 
ATOM   4803 O O    . ASN   B 1 54  ? 57.869 -18.549 -0.366  1.00 14.09 ?  54  ASN   B O    1 
ATOM   4804 C CB   . ASN   B 1 54  ? 55.479 -19.247 1.776   1.00 14.49 ?  54  ASN   B CB   1 
ATOM   4805 C CG   . ASN   B 1 54  ? 56.451 -18.323 2.479   1.00 14.55 ?  54  ASN   B CG   1 
ATOM   4806 O OD1  . ASN   B 1 54  ? 56.478 -17.121 2.215   1.00 14.97 ?  54  ASN   B OD1  1 
ATOM   4807 N ND2  . ASN   B 1 54  ? 57.263 -18.877 3.369   1.00 16.42 ?  54  ASN   B ND2  1 
ATOM   4808 H H    . ASN   B 1 54  ? 54.268 -20.615 0.127   1.00 15.44 ?  54  ASN   B H    1 
ATOM   4809 H HA   . ASN   B 1 54  ? 55.436 -18.286 -0.017  1.00 16.06 ?  54  ASN   B HA   1 
ATOM   4810 H HB2  . ASN   B 1 54  ? 54.577 -18.975 2.016   1.00 17.39 ?  54  ASN   B HB2  1 
ATOM   4811 H HB3  . ASN   B 1 54  ? 55.649 -20.149 2.088   1.00 17.39 ?  54  ASN   B HB3  1 
ATOM   4812 H HD21 . ASN   B 1 54  ? 57.829 -18.389 3.796   1.00 19.72 ?  54  ASN   B HD21 1 
ATOM   4813 H HD22 . ASN   B 1 54  ? 57.214 -19.718 3.528   1.00 19.72 ?  54  ASN   B HD22 1 
ATOM   4814 N N    . LYS   B 1 55  ? 57.465 -20.761 -0.190  1.00 14.80 ?  55  LYS   B N    1 
ATOM   4815 C CA   . LYS   B 1 55  ? 58.819 -21.112 -0.603  1.00 15.77 ?  55  LYS   B CA   1 
ATOM   4816 C C    . LYS   B 1 55  ? 59.118 -20.572 -1.995  1.00 15.42 ?  55  LYS   B C    1 
ATOM   4817 O O    . LYS   B 1 55  ? 60.219 -20.069 -2.251  1.00 15.70 ?  55  LYS   B O    1 
ATOM   4818 C CB   . LYS   B 1 55  ? 59.007 -22.628 -0.555  1.00 18.09 ?  55  LYS   B CB   1 
ATOM   4819 C CG   . LYS   B 1 55  ? 60.376 -23.083 -1.013  1.00 22.56 ?  55  LYS   B CG   1 
ATOM   4820 C CD   . LYS   B 1 55  ? 60.568 -24.573 -0.823  1.00 26.32 ?  55  LYS   B CD   1 
ATOM   4821 C CE   . LYS   B 1 55  ? 60.597 -24.951 0.651   1.00 29.65 ?  55  LYS   B CE   1 
ATOM   4822 N NZ   . LYS   B 1 55  ? 61.081 -26.335 0.856   1.00 31.25 ?  55  LYS   B NZ   1 
ATOM   4823 H H    . LYS   B 1 55  ? 56.953 -21.429 -0.002  1.00 17.76 ?  55  LYS   B H    1 
ATOM   4824 H HA   . LYS   B 1 55  ? 59.444 -20.711 0.018   1.00 18.93 ?  55  LYS   B HA   1 
ATOM   4825 H HB2  . LYS   B 1 55  ? 58.874 -22.926 0.359   1.00 21.71 ?  55  LYS   B HB2  1 
ATOM   4826 H HB3  . LYS   B 1 55  ? 58.344 -23.044 -1.132  1.00 21.71 ?  55  LYS   B HB3  1 
ATOM   4827 H HG2  . LYS   B 1 55  ? 60.480 -22.881 -1.955  1.00 27.09 ?  55  LYS   B HG2  1 
ATOM   4828 H HG3  . LYS   B 1 55  ? 61.052 -22.618 -0.494  1.00 27.09 ?  55  LYS   B HG3  1 
ATOM   4829 H HD2  . LYS   B 1 55  ? 59.834 -25.048 -1.244  1.00 31.60 ?  55  LYS   B HD2  1 
ATOM   4830 H HD3  . LYS   B 1 55  ? 61.412 -24.840 -1.221  1.00 31.60 ?  55  LYS   B HD3  1 
ATOM   4831 H HE2  . LYS   B 1 55  ? 61.190 -24.342 1.122   1.00 35.58 ?  55  LYS   B HE2  1 
ATOM   4832 H HE3  . LYS   B 1 55  ? 59.698 -24.884 1.013   1.00 35.58 ?  55  LYS   B HE3  1 
ATOM   4833 H HZ1  . LYS   B 1 55  ? 61.059 -26.537 1.722   1.00 37.51 ?  55  LYS   B HZ1  1 
ATOM   4834 H HZ2  . LYS   B 1 55  ? 60.563 -26.904 0.411   1.00 37.51 ?  55  LYS   B HZ2  1 
ATOM   4835 H HZ3  . LYS   B 1 55  ? 61.916 -26.410 0.561   1.00 37.51 ?  55  LYS   B HZ3  1 
ATOM   4836 N N    . ALA   B 1 56  ? 58.148 -20.667 -2.909  1.00 15.03 ?  56  ALA   B N    1 
ATOM   4837 C CA   . ALA   B 1 56  ? 58.368 -20.177 -4.265  1.00 15.79 ?  56  ALA   B CA   1 
ATOM   4838 C C    . ALA   B 1 56  ? 58.635 -18.679 -4.282  1.00 15.42 ?  56  ALA   B C    1 
ATOM   4839 O O    . ALA   B 1 56  ? 59.352 -18.189 -5.166  1.00 16.34 ?  56  ALA   B O    1 
ATOM   4840 C CB   . ALA   B 1 56  ? 57.179 -20.530 -5.160  1.00 16.36 ?  56  ALA   B CB   1 
ATOM   4841 H H    . ALA   B 1 56  ? 57.361 -20.995 -2.768  1.00 18.05 ?  56  ALA   B H    1 
ATOM   4842 H HA   . ALA   B 1 56  ? 59.151 -20.615 -4.627  1.00 18.96 ?  56  ALA   B HA   1 
ATOM   4843 H HB1  . ALA   B 1 56  ? 57.354 -20.204 -6.059  1.00 19.64 ?  56  ALA   B HB1  1 
ATOM   4844 H HB2  . ALA   B 1 56  ? 57.073 -21.495 -5.176  1.00 19.64 ?  56  ALA   B HB2  1 
ATOM   4845 H HB3  . ALA   B 1 56  ? 56.379 -20.114 -4.808  1.00 19.64 ?  56  ALA   B HB3  1 
ATOM   4846 N N    . THR   B 1 57  ? 58.073 -17.937 -3.325  1.00 15.04 ?  57  THR   B N    1 
ATOM   4847 C CA   . THR   B 1 57  ? 58.305 -16.501 -3.227  1.00 15.34 ?  57  THR   B CA   1 
ATOM   4848 C C    . THR   B 1 57  ? 59.550 -16.165 -2.420  1.00 16.05 ?  57  THR   B C    1 
ATOM   4849 O O    . THR   B 1 57  ? 59.790 -14.983 -2.140  1.00 16.22 ?  57  THR   B O    1 
ATOM   4850 C CB   . THR   B 1 57  ? 57.099 -15.772 -2.606  1.00 14.87 ?  57  THR   B CB   1 
ATOM   4851 O OG1  . THR   B 1 57  ? 57.069 -15.978 -1.188  1.00 14.88 ?  57  THR   B OG1  1 
ATOM   4852 C CG2  . THR   B 1 57  ? 55.789 -16.204 -3.245  1.00 14.60 ?  57  THR   B CG2  1 
ATOM   4853 H H    . THR   B 1 57  ? 57.543 -18.249 -2.717  1.00 18.06 ?  57  THR   B H    1 
ATOM   4854 H HA   . THR   B 1 57  ? 58.426 -16.154 -4.126  1.00 18.41 ?  57  THR   B HA   1 
ATOM   4855 H HB   . THR   B 1 57  ? 57.198 -14.821 -2.782  1.00 17.86 ?  57  THR   B HB   1 
ATOM   4856 H HG1  . THR   B 1 57  ? 56.991 -16.797 -1.027  1.00 17.86 ?  57  THR   B HG1  1 
ATOM   4857 H HG21 . THR   B 1 57  ? 55.056 -15.669 -2.908  1.00 17.53 ?  57  THR   B HG21 1 
ATOM   4858 H HG22 . THR   B 1 57  ? 55.834 -16.102 -4.212  1.00 17.53 ?  57  THR   B HG22 1 
ATOM   4859 H HG23 . THR   B 1 57  ? 55.611 -17.138 -3.045  1.00 17.53 ?  57  THR   B HG23 1 
ATOM   4860 N N    A ASN   B 1 58  ? 60.346 -17.167 -2.048  0.48 16.56 ?  58  ASN   B N    1 
ATOM   4861 N N    B ASN   B 1 58  ? 60.347 -17.162 -2.041  0.52 16.33 ?  58  ASN   B N    1 
ATOM   4862 C CA   A ASN   B 1 58  ? 61.543 -16.954 -1.237  0.48 18.64 ?  58  ASN   B CA   1 
ATOM   4863 C CA   B ASN   B 1 58  ? 61.545 -16.923 -1.239  0.52 18.35 ?  58  ASN   B CA   1 
ATOM   4864 C C    A ASN   B 1 58  ? 61.207 -16.224 0.063   0.48 17.60 ?  58  ASN   B C    1 
ATOM   4865 C C    B ASN   B 1 58  ? 61.197 -16.198 0.060   0.52 17.45 ?  58  ASN   B C    1 
ATOM   4866 O O    A ASN   B 1 58  ? 61.943 -15.340 0.511   0.48 18.23 ?  58  ASN   B O    1 
ATOM   4867 O O    B ASN   B 1 58  ? 61.912 -15.293 0.502   0.52 18.18 ?  58  ASN   B O    1 
ATOM   4868 C CB   A ASN   B 1 58  ? 62.648 -16.238 -2.020  0.48 23.01 ?  58  ASN   B CB   1 
ATOM   4869 C CB   B ASN   B 1 58  ? 62.619 -16.176 -2.035  0.52 22.74 ?  58  ASN   B CB   1 
ATOM   4870 C CG   A ASN   B 1 58  ? 64.001 -16.350 -1.349  0.48 27.92 ?  58  ASN   B CG   1 
ATOM   4871 C CG   B ASN   B 1 58  ? 63.994 -16.287 -1.409  0.52 27.88 ?  58  ASN   B CG   1 
ATOM   4872 O OD1  A ASN   B 1 58  ? 64.280 -17.326 -0.650  0.48 30.06 ?  58  ASN   B OD1  1 
ATOM   4873 O OD1  B ASN   B 1 58  ? 64.299 -17.262 -0.722  0.52 30.15 ?  58  ASN   B OD1  1 
ATOM   4874 N ND2  A ASN   B 1 58  ? 64.850 -15.351 -1.555  0.48 29.66 ?  58  ASN   B ND2  1 
ATOM   4875 N ND2  B ASN   B 1 58  ? 64.834 -15.289 -1.646  0.52 29.69 ?  58  ASN   B ND2  1 
ATOM   4876 H H    A ASN   B 1 58  ? 60.211 -17.992 -2.254  0.48 19.88 ?  58  ASN   B H    1 
ATOM   4877 H H    B ASN   B 1 58  ? 60.212 -17.990 -2.231  0.52 19.60 ?  58  ASN   B H    1 
ATOM   4878 H HA   A ASN   B 1 58  ? 61.890 -17.825 -0.994  0.48 22.38 ?  58  ASN   B HA   1 
ATOM   4879 H HA   B ASN   B 1 58  ? 61.915 -17.784 -0.994  0.52 22.03 ?  58  ASN   B HA   1 
ATOM   4880 H HB2  A ASN   B 1 58  ? 62.717 -16.635 -2.905  0.48 27.62 ?  58  ASN   B HB2  1 
ATOM   4881 H HB2  B ASN   B 1 58  ? 62.666 -16.551 -2.931  0.52 27.30 ?  58  ASN   B HB2  1 
ATOM   4882 H HB3  A ASN   B 1 58  ? 62.428 -15.298 -2.095  0.48 27.62 ?  58  ASN   B HB3  1 
ATOM   4883 H HB3  B ASN   B 1 58  ? 62.387 -15.237 -2.081  0.52 27.30 ?  58  ASN   B HB3  1 
ATOM   4884 H HD21 A ASN   B 1 58  ? 65.631 -15.369 -1.195  0.48 35.60 ?  58  ASN   B HD21 1 
ATOM   4885 H HD21 B ASN   B 1 58  ? 65.627 -15.307 -1.314  0.52 35.63 ?  58  ASN   B HD21 1 
ATOM   4886 H HD22 A ASN   B 1 58  ? 64.619 -14.685 -2.048  0.48 35.60 ?  58  ASN   B HD22 1 
ATOM   4887 H HD22 B ASN   B 1 58  ? 64.585 -14.624 -2.131  0.52 35.63 ?  58  ASN   B HD22 1 
ATOM   4888 N N    . ASN   B 1 59  ? 60.084 -16.601 0.677   1.00 16.57 ?  59  ASN   B N    1 
ATOM   4889 C CA   . ASN   B 1 59  ? 59.610 -16.109 1.969   1.00 16.32 ?  59  ASN   B CA   1 
ATOM   4890 C C    . ASN   B 1 59  ? 59.011 -14.708 1.903   1.00 15.47 ?  59  ASN   B C    1 
ATOM   4891 O O    . ASN   B 1 59  ? 58.583 -14.187 2.944   1.00 15.67 ?  59  ASN   B O    1 
ATOM   4892 C CB   . ASN   B 1 59  ? 60.679 -16.165 3.074   1.00 17.16 ?  59  ASN   B CB   1 
ATOM   4893 C CG   . ASN   B 1 59  ? 60.083 -16.306 4.459   1.00 18.07 ?  59  ASN   B CG   1 
ATOM   4894 O OD1  . ASN   B 1 59  ? 59.265 -17.195 4.707   1.00 18.65 ?  59  ASN   B OD1  1 
ATOM   4895 N ND2  . ASN   B 1 59  ? 60.502 -15.437 5.379   1.00 18.87 ?  59  ASN   B ND2  1 
ATOM   4896 H H    A ASN   B 1 59  ? 59.546 -17.184 0.341   0.48 19.89 ?  59  ASN   B H    1 
ATOM   4897 H H    B ASN   B 1 59  ? 59.560 -17.201 0.348   0.52 19.89 ?  59  ASN   B H    1 
ATOM   4898 H HA   . ASN   B 1 59  ? 58.898 -16.700 2.257   1.00 19.59 ?  59  ASN   B HA   1 
ATOM   4899 H HB2  . ASN   B 1 59  ? 61.259 -16.931 2.923   1.00 20.60 ?  59  ASN   B HB2  1 
ATOM   4900 H HB3  . ASN   B 1 59  ? 61.199 -15.350 3.063   1.00 20.60 ?  59  ASN   B HB3  1 
ATOM   4901 H HD21 . ASN   B 1 59  ? 60.194 -15.475 6.183   1.00 22.66 ?  59  ASN   B HD21 1 
ATOM   4902 H HD22 . ASN   B 1 59  ? 61.064 -14.824 5.165   1.00 22.66 ?  59  ASN   B HD22 1 
ATOM   4903 N N    . ALA   B 1 60  ? 58.943 -14.084 0.724   1.00 15.37 ?  60  ALA   B N    1 
ATOM   4904 C CA   . ALA   B 1 60  ? 58.345 -12.754 0.637   1.00 15.79 ?  60  ALA   B CA   1 
ATOM   4905 C C    . ALA   B 1 60  ? 56.876 -12.783 1.041   1.00 14.84 ?  60  ALA   B C    1 
ATOM   4906 O O    . ALA   B 1 60  ? 56.369 -11.828 1.645   1.00 15.12 ?  60  ALA   B O    1 
ATOM   4907 C CB   . ALA   B 1 60  ? 58.504 -12.185 -0.773  1.00 16.98 ?  60  ALA   B CB   1 
ATOM   4908 H H    . ALA   B 1 60  ? 59.237 -14.404 -0.020  1.00 18.45 ?  60  ALA   B H    1 
ATOM   4909 H HA   . ALA   B 1 60  ? 58.806 -12.167 1.249   1.00 18.96 ?  60  ALA   B HA   1 
ATOM   4910 H HB1  . ALA   B 1 60  ? 58.099 -11.308 -0.805  1.00 20.38 ?  60  ALA   B HB1  1 
ATOM   4911 H HB2  . ALA   B 1 60  ? 59.451 -12.124 -0.983  1.00 20.38 ?  60  ALA   B HB2  1 
ATOM   4912 H HB3  . ALA   B 1 60  ? 58.067 -12.778 -1.406  1.00 20.38 ?  60  ALA   B HB3  1 
ATOM   4913 N N    . MET   B 1 61  ? 56.169 -13.868 0.712   1.00 14.16 ?  61  MET   B N    1 
ATOM   4914 C CA   . MET   B 1 61  ? 54.773 -13.982 1.106   1.00 13.74 ?  61  MET   B CA   1 
ATOM   4915 C C    . MET   B 1 61  ? 54.633 -13.965 2.623   1.00 14.04 ?  61  MET   B C    1 
ATOM   4916 O O    . MET   B 1 61  ? 53.735 -13.309 3.166   1.00 13.38 ?  61  MET   B O    1 
ATOM   4917 C CB   . MET   B 1 61  ? 54.190 -15.265 0.504   1.00 13.88 ?  61  MET   B CB   1 
ATOM   4918 C CG   . MET   B 1 61  ? 52.758 -15.558 0.929   1.00 13.83 ?  61  MET   B CG   1 
ATOM   4919 S SD   . MET   B 1 61  ? 52.129 -17.056 0.176   1.00 14.61 ?  61  MET   B SD   1 
ATOM   4920 C CE   . MET   B 1 61  ? 51.886 -16.491 -1.510  1.00 15.99 ?  61  MET   B CE   1 
ATOM   4921 H H    . MET   B 1 61  ? 56.471 -14.546 0.263   1.00 17.00 ?  61  MET   B H    1 
ATOM   4922 H HA   . MET   B 1 61  ? 54.276 -13.241 0.735   1.00 16.49 ?  61  MET   B HA   1 
ATOM   4923 H HB2  . MET   B 1 61  ? 54.197 -15.195 -0.463  1.00 16.67 ?  61  MET   B HB2  1 
ATOM   4924 H HB3  . MET   B 1 61  ? 54.736 -16.022 0.779   1.00 16.67 ?  61  MET   B HB3  1 
ATOM   4925 H HG2  . MET   B 1 61  ? 52.724 -15.681 1.895   1.00 16.60 ?  61  MET   B HG2  1 
ATOM   4926 H HG3  . MET   B 1 61  ? 52.187 -14.822 0.669   1.00 16.60 ?  61  MET   B HG3  1 
ATOM   4927 H HE1  . MET   B 1 61  ? 51.482 -17.203 -2.028  1.00 19.20 ?  61  MET   B HE1  1 
ATOM   4928 H HE2  . MET   B 1 61  ? 51.308 -15.712 -1.508  1.00 19.20 ?  61  MET   B HE2  1 
ATOM   4929 H HE3  . MET   B 1 61  ? 52.751 -16.257 -1.888  1.00 19.20 ?  61  MET   B HE3  1 
ATOM   4930 N N    . GLN   B 1 62  ? 55.512 -14.676 3.330   1.00 13.64 ?  62  GLN   B N    1 
ATOM   4931 C CA   . GLN   B 1 62  ? 55.403 -14.728 4.783   1.00 14.45 ?  62  GLN   B CA   1 
ATOM   4932 C C    . GLN   B 1 62  ? 55.689 -13.370 5.409   1.00 14.24 ?  62  GLN   B C    1 
ATOM   4933 O O    . GLN   B 1 62  ? 55.006 -12.963 6.355   1.00 14.67 ?  62  GLN   B O    1 
ATOM   4934 C CB   . GLN   B 1 62  ? 56.357 -15.774 5.355   1.00 14.49 ?  62  GLN   B CB   1 
ATOM   4935 C CG   . GLN   B 1 62  ? 56.137 -16.012 6.841   1.00 14.93 ?  62  GLN   B CG   1 
ATOM   4936 C CD   . GLN   B 1 62  ? 54.767 -16.610 7.106   1.00 14.43 ?  62  GLN   B CD   1 
ATOM   4937 O OE1  . GLN   B 1 62  ? 54.522 -17.772 6.785   1.00 15.23 ?  62  GLN   B OE1  1 
ATOM   4938 N NE2  . GLN   B 1 62  ? 53.857 -15.812 7.659   1.00 14.39 ?  62  GLN   B NE2  1 
ATOM   4939 H H    . GLN   B 1 62  ? 56.166 -15.128 3.002   1.00 16.37 ?  62  GLN   B H    1 
ATOM   4940 H HA   . GLN   B 1 62  ? 54.497 -14.980 5.023   1.00 17.35 ?  62  GLN   B HA   1 
ATOM   4941 H HB2  . GLN   B 1 62  ? 56.219 -16.617 4.896   1.00 17.40 ?  62  GLN   B HB2  1 
ATOM   4942 H HB3  . GLN   B 1 62  ? 57.271 -15.473 5.232   1.00 17.40 ?  62  GLN   B HB3  1 
ATOM   4943 H HG2  . GLN   B 1 62  ? 56.806 -16.629 7.167   1.00 17.93 ?  62  GLN   B HG2  1 
ATOM   4944 H HG3  . GLN   B 1 62  ? 56.199 -15.166 7.316   1.00 17.93 ?  62  GLN   B HG3  1 
ATOM   4945 H HE21 . GLN   B 1 62  ? 54.064 -15.000 7.856   1.00 17.28 ?  62  GLN   B HE21 1 
ATOM   4946 H HE22 . GLN   B 1 62  ? 53.070 -16.109 7.818   1.00 17.28 ?  62  GLN   B HE22 1 
ATOM   4947 N N    . VAL   B 1 63  ? 56.699 -12.659 4.909   1.00 14.48 ?  63  VAL   B N    1 
ATOM   4948 C CA   . VAL   B 1 63  ? 57.002 -11.339 5.458   1.00 15.87 ?  63  VAL   B CA   1 
ATOM   4949 C C    . VAL   B 1 63  ? 55.810 -10.406 5.278   1.00 14.94 ?  63  VAL   B C    1 
ATOM   4950 O O    . VAL   B 1 63  ? 55.403 -9.695  6.207   1.00 15.56 ?  63  VAL   B O    1 
ATOM   4951 C CB   . VAL   B 1 63  ? 58.290 -10.776 4.829   1.00 17.67 ?  63  VAL   B CB   1 
ATOM   4952 C CG1  . VAL   B 1 63  ? 58.503 -9.324  5.247   1.00 17.84 ?  63  VAL   B CG1  1 
ATOM   4953 C CG2  . VAL   B 1 63  ? 59.495 -11.620 5.241   1.00 18.48 ?  63  VAL   B CG2  1 
ATOM   4954 H H    . VAL   B 1 63  ? 57.208 -12.909 4.259   1.00 17.38 ?  63  VAL   B H    1 
ATOM   4955 H HA   . VAL   B 1 63  ? 57.162 -11.431 6.407   1.00 19.05 ?  63  VAL   B HA   1 
ATOM   4956 H HB   . VAL   B 1 63  ? 58.224 -10.806 3.862   1.00 21.22 ?  63  VAL   B HB   1 
ATOM   4957 H HG11 . VAL   B 1 63  ? 59.421 -9.067  5.056   1.00 21.42 ?  63  VAL   B HG11 1 
ATOM   4958 H HG12 . VAL   B 1 63  ? 57.895 -8.755  4.749   1.00 21.42 ?  63  VAL   B HG12 1 
ATOM   4959 H HG13 . VAL   B 1 63  ? 58.333 -9.239  6.199   1.00 21.42 ?  63  VAL   B HG13 1 
ATOM   4960 H HG21 . VAL   B 1 63  ? 60.299 -11.243 4.841   1.00 22.19 ?  63  VAL   B HG21 1 
ATOM   4961 H HG22 . VAL   B 1 63  ? 59.576 -11.602 6.210   1.00 22.19 ?  63  VAL   B HG22 1 
ATOM   4962 H HG23 . VAL   B 1 63  ? 59.368 -12.527 4.935   1.00 22.19 ?  63  VAL   B HG23 1 
ATOM   4963 N N    . GLU   B 1 64  ? 55.231 -10.402 4.077   1.00 14.74 ?  64  GLU   B N    1 
ATOM   4964 C CA   . GLU   B 1 64  ? 54.071 -9.564  3.803   1.00 14.66 ?  64  GLU   B CA   1 
ATOM   4965 C C    . GLU   B 1 64  ? 52.892 -9.961  4.680   1.00 14.00 ?  64  GLU   B C    1 
ATOM   4966 O O    . GLU   B 1 64  ? 52.142 -9.103  5.171   1.00 14.27 ?  64  GLU   B O    1 
ATOM   4967 C CB   . GLU   B 1 64  ? 53.719 -9.716  2.325   1.00 15.06 ?  64  GLU   B CB   1 
ATOM   4968 C CG   . GLU   B 1 64  ? 52.479 -8.961  1.883   1.00 15.70 ?  64  GLU   B CG   1 
ATOM   4969 C CD   . GLU   B 1 64  ? 51.948 -9.449  0.549   1.00 16.94 ?  64  GLU   B CD   1 
ATOM   4970 O OE1  . GLU   B 1 64  ? 52.121 -10.653 0.230   1.00 17.65 ?  64  GLU   B OE1  1 
ATOM   4971 O OE2  . GLU   B 1 64  ? 51.329 -8.628  -0.166  1.00 17.49 -1 64  GLU   B OE2  1 
ATOM   4972 H H    . GLU   B 1 64  ? 55.489 -10.880 3.406   1.00 17.70 ?  64  GLU   B H    1 
ATOM   4973 H HA   . GLU   B 1 64  ? 54.289 -8.634  3.977   1.00 17.60 ?  64  GLU   B HA   1 
ATOM   4974 H HB2  . GLU   B 1 64  ? 54.462 -9.389  1.791   1.00 18.08 ?  64  GLU   B HB2  1 
ATOM   4975 H HB3  . GLU   B 1 64  ? 53.573 -10.655 2.137   1.00 18.08 ?  64  GLU   B HB3  1 
ATOM   4976 H HG2  . GLU   B 1 64  ? 51.774 -9.074  2.539   1.00 18.85 ?  64  GLU   B HG2  1 
ATOM   4977 H HG3  . GLU   B 1 64  ? 52.699 -8.021  1.792   1.00 18.85 ?  64  GLU   B HG3  1 
ATOM   4978 N N    . SER   B 1 65  ? 52.712 -11.267 4.872   1.00 13.27 ?  65  SER   B N    1 
ATOM   4979 C CA   . SER   B 1 65  ? 51.610 -11.778 5.674   1.00 13.83 ?  65  SER   B CA   1 
ATOM   4980 C C    . SER   B 1 65  ? 51.746 -11.376 7.136   1.00 14.29 ?  65  SER   B C    1 
ATOM   4981 O O    . SER   B 1 65  ? 50.752 -10.997 7.774   1.00 14.37 ?  65  SER   B O    1 
ATOM   4982 C CB   . SER   B 1 65  ? 51.543 -13.298 5.537   1.00 13.76 ?  65  SER   B CB   1 
ATOM   4983 O OG   . SER   B 1 65  ? 51.164 -13.697 4.230   1.00 14.03 ?  65  SER   B OG   1 
ATOM   4984 H H    . SER   B 1 65  ? 53.222 -11.884 4.541   1.00 15.93 ?  65  SER   B H    1 
ATOM   4985 H HA   . SER   B 1 65  ? 50.778 -11.412 5.337   1.00 16.60 ?  65  SER   B HA   1 
ATOM   4986 H HB2  . SER   B 1 65  ? 52.416 -13.670 5.734   1.00 16.52 ?  65  SER   B HB2  1 
ATOM   4987 H HB3  . SER   B 1 65  ? 50.891 -13.638 6.171   1.00 16.52 ?  65  SER   B HB3  1 
ATOM   4988 H HG   . SER   B 1 65  ? 51.715 -13.409 3.661   1.00 16.84 ?  65  SER   B HG   1 
ATOM   4989 N N    . ASP   B 1 66  ? 52.959 -11.464 7.693   1.00 14.23 ?  66  ASP   B N    1 
ATOM   4990 C CA   . ASP   B 1 66  ? 53.152 -11.073 9.087   1.00 14.62 ?  66  ASP   B CA   1 
ATOM   4991 C C    . ASP   B 1 66  ? 52.832 -9.597  9.287   1.00 14.57 ?  66  ASP   B C    1 
ATOM   4992 O O    . ASP   B 1 66  ? 52.261 -9.207  10.312  1.00 15.17 ?  66  ASP   B O    1 
ATOM   4993 C CB   . ASP   B 1 66  ? 54.585 -11.371 9.532   1.00 16.46 ?  66  ASP   B CB   1 
ATOM   4994 C CG   . ASP   B 1 66  ? 54.857 -12.857 9.699   1.00 18.85 ?  66  ASP   B CG   1 
ATOM   4995 O OD1  . ASP   B 1 66  ? 53.903 -13.669 9.676   1.00 19.59 ?  66  ASP   B OD1  1 
ATOM   4996 O OD2  . ASP   B 1 66  ? 56.041 -13.218 9.868   1.00 21.85 -1 66  ASP   B OD2  1 
ATOM   4997 H H    . ASP   B 1 66  ? 53.673 -11.744 7.292   1.00 17.09 ?  66  ASP   B H    1 
ATOM   4998 H HA   . ASP   B 1 66  ? 52.556 -11.587 9.649   1.00 17.55 ?  66  ASP   B HA   1 
ATOM   4999 H HB2  . ASP   B 1 66  ? 55.208 -11.032 8.871   1.00 19.76 ?  66  ASP   B HB2  1 
ATOM   5000 H HB3  . ASP   B 1 66  ? 54.752 -10.945 10.391  1.00 19.76 ?  66  ASP   B HB3  1 
ATOM   5001 N N    . ASP   B 1 67  ? 53.206 -8.757  8.320   1.00 14.25 ?  67  ASP   B N    1 
ATOM   5002 C CA   . ASP   B 1 67  ? 52.864 -7.345  8.403   1.00 15.42 ?  67  ASP   B CA   1 
ATOM   5003 C C    . ASP   B 1 67  ? 51.351 -7.138  8.323   1.00 15.74 ?  67  ASP   B C    1 
ATOM   5004 O O    . ASP   B 1 67  ? 50.789 -6.336  9.076   1.00 16.06 ?  67  ASP   B O    1 
ATOM   5005 C CB   . ASP   B 1 67  ? 53.570 -6.579  7.294   1.00 17.06 ?  67  ASP   B CB   1 
ATOM   5006 C CG   . ASP   B 1 67  ? 53.147 -5.137  7.250   1.00 18.55 ?  67  ASP   B CG   1 
ATOM   5007 O OD1  . ASP   B 1 67  ? 53.640 -4.320  8.062   1.00 19.72 ?  67  ASP   B OD1  1 
ATOM   5008 O OD2  . ASP   B 1 67  ? 52.281 -4.835  6.413   1.00 20.11 -1 67  ASP   B OD2  1 
ATOM   5009 H H    . ASP   B 1 67  ? 53.661 -8.977  7.623   1.00 17.10 ?  67  ASP   B H    1 
ATOM   5010 H HA   . ASP   B 1 67  ? 53.175 -6.988  9.253   1.00 18.52 ?  67  ASP   B HA   1 
ATOM   5011 H HB2  . ASP   B 1 67  ? 54.529 -6.609  7.442   1.00 20.48 ?  67  ASP   B HB2  1 
ATOM   5012 H HB3  . ASP   B 1 67  ? 53.358 -6.997  6.438   1.00 20.48 ?  67  ASP   B HB3  1 
ATOM   5013 N N    . TYR   B 1 68  ? 50.672 -7.870  7.431   1.00 15.28 ?  68  TYR   B N    1 
ATOM   5014 C CA   . TYR   B 1 68  ? 49.216 -7.787  7.359   1.00 16.08 ?  68  TYR   B CA   1 
ATOM   5015 C C    . TYR   B 1 68  ? 48.580 -8.134  8.702   1.00 15.36 ?  68  TYR   B C    1 
ATOM   5016 O O    . TYR   B 1 68  ? 47.655 -7.448  9.156   1.00 15.88 ?  68  TYR   B O    1 
ATOM   5017 C CB   . TYR   B 1 68  ? 48.683 -8.693  6.244   1.00 16.89 ?  68  TYR   B CB   1 
ATOM   5018 C CG   . TYR   B 1 68  ? 47.178 -8.838  6.289   1.00 18.05 ?  68  TYR   B CG   1 
ATOM   5019 C CD1  . TYR   B 1 68  ? 46.584 -9.785  7.112   1.00 19.20 ?  68  TYR   B CD1  1 
ATOM   5020 C CD2  . TYR   B 1 68  ? 46.357 -8.005  5.550   1.00 19.27 ?  68  TYR   B CD2  1 
ATOM   5021 C CE1  . TYR   B 1 68  ? 45.224 -9.909  7.191   1.00 20.87 ?  68  TYR   B CE1  1 
ATOM   5022 C CE2  . TYR   B 1 68  ? 44.973 -8.126  5.619   1.00 20.44 ?  68  TYR   B CE2  1 
ATOM   5023 C CZ   . TYR   B 1 68  ? 44.429 -9.077  6.445   1.00 20.96 ?  68  TYR   B CZ   1 
ATOM   5024 O OH   . TYR   B 1 68  ? 43.065 -9.199  6.531   1.00 22.88 ?  68  TYR   B OH   1 
ATOM   5025 H H    . TYR   B 1 68  ? 51.030 -8.426  6.878   1.00 18.35 ?  68  TYR   B H    1 
ATOM   5026 H HA   . TYR   B 1 68  ? 48.975 -6.873  7.150   1.00 19.31 ?  68  TYR   B HA   1 
ATOM   5027 H HB2  . TYR   B 1 68  ? 48.921 -8.303  5.388   1.00 20.28 ?  68  TYR   B HB2  1 
ATOM   5028 H HB3  . TYR   B 1 68  ? 49.075 -9.571  6.335   1.00 20.28 ?  68  TYR   B HB3  1 
ATOM   5029 H HD1  . TYR   B 1 68  ? 47.125 -10.350 7.622   1.00 23.05 ?  68  TYR   B HD1  1 
ATOM   5030 H HD2  . TYR   B 1 68  ? 46.735 -7.355  5.004   1.00 23.13 ?  68  TYR   B HD2  1 
ATOM   5031 H HE1  . TYR   B 1 68  ? 44.843 -10.560 7.740   1.00 25.05 ?  68  TYR   B HE1  1 
ATOM   5032 H HE2  . TYR   B 1 68  ? 44.423 -7.566  5.122   1.00 24.54 ?  68  TYR   B HE2  1 
ATOM   5033 H HH   . TYR   B 1 68  ? 42.683 -8.649  6.017   1.00 27.46 ?  68  TYR   B HH   1 
ATOM   5034 N N    . ILE   B 1 69  ? 49.057 -9.204  9.346   1.00 15.01 ?  69  ILE   B N    1 
ATOM   5035 C CA   . ILE   B 1 69  ? 48.493 -9.628  10.625  1.00 15.61 ?  69  ILE   B CA   1 
ATOM   5036 C C    . ILE   B 1 69  ? 48.751 -8.587  11.707  1.00 15.29 ?  69  ILE   B C    1 
ATOM   5037 O O    . ILE   B 1 69  ? 47.884 -8.315  12.544  1.00 15.46 ?  69  ILE   B O    1 
ATOM   5038 C CB   . ILE   B 1 69  ? 49.064 -11.008 11.013  1.00 16.72 ?  69  ILE   B CB   1 
ATOM   5039 C CG1  . ILE   B 1 69  ? 48.539 -12.113 10.085  1.00 17.19 ?  69  ILE   B CG1  1 
ATOM   5040 C CG2  . ILE   B 1 69  ? 48.774 -11.322 12.476  1.00 17.95 ?  69  ILE   B CG2  1 
ATOM   5041 C CD1  . ILE   B 1 69  ? 47.061 -12.423 10.226  1.00 17.74 ?  69  ILE   B CD1  1 
ATOM   5042 H H    . ILE   B 1 69  ? 49.699 -9.701  9.064   1.00 18.02 ?  69  ILE   B H    1 
ATOM   5043 H HA   . ILE   B 1 69  ? 47.533 -9.720  10.529  1.00 18.73 ?  69  ILE   B HA   1 
ATOM   5044 H HB   . ILE   B 1 69  ? 50.024 -10.971 10.909  1.00 20.07 ?  69  ILE   B HB   1 
ATOM   5045 H HG12 . ILE   B 1 69  ? 48.696 -11.845 9.167   1.00 20.64 ?  69  ILE   B HG12 1 
ATOM   5046 H HG13 . ILE   B 1 69  ? 49.028 -12.932 10.273  1.00 20.64 ?  69  ILE   B HG13 1 
ATOM   5047 H HG21 . ILE   B 1 69  ? 48.901 -12.272 12.623  1.00 21.54 ?  69  ILE   B HG21 1 
ATOM   5048 H HG22 . ILE   B 1 69  ? 49.386 -10.819 13.036  1.00 21.54 ?  69  ILE   B HG22 1 
ATOM   5049 H HG23 . ILE   B 1 69  ? 47.857 -11.077 12.678  1.00 21.54 ?  69  ILE   B HG23 1 
ATOM   5050 H HD11 . ILE   B 1 69  ? 46.834 -13.140 9.613   1.00 21.29 ?  69  ILE   B HD11 1 
ATOM   5051 H HD12 . ILE   B 1 69  ? 46.880 -12.701 11.137  1.00 21.29 ?  69  ILE   B HD12 1 
ATOM   5052 H HD13 . ILE   B 1 69  ? 46.549 -11.630 10.011  1.00 21.29 ?  69  ILE   B HD13 1 
ATOM   5053 N N    . ALA   B 1 70  ? 49.947 -8.004  11.731  1.00 15.73 ?  70  ALA   B N    1 
ATOM   5054 C CA   . ALA   B 1 70  ? 50.228 -6.976  12.728  1.00 15.19 ?  70  ALA   B CA   1 
ATOM   5055 C C    . ALA   B 1 70  ? 49.238 -5.825  12.618  1.00 16.02 ?  70  ALA   B C    1 
ATOM   5056 O O    . ALA   B 1 70  ? 48.795 -5.273  13.631  1.00 16.43 ?  70  ALA   B O    1 
ATOM   5057 C CB   . ALA   B 1 70  ? 51.659 -6.473  12.559  1.00 15.94 ?  70  ALA   B CB   1 
ATOM   5058 H H    . ALA   B 1 70  ? 50.593 -8.186  11.197  1.00 18.89 ?  70  ALA   B H    1 
ATOM   5059 H HA   . ALA   B 1 70  ? 50.154 -7.363  13.616  1.00 18.24 ?  70  ALA   B HA   1 
ATOM   5060 H HB1  . ALA   B 1 70  ? 51.856 -5.826  13.257  1.00 19.14 ?  70  ALA   B HB1  1 
ATOM   5061 H HB2  . ALA   B 1 70  ? 52.275 -7.224  12.632  1.00 19.14 ?  70  ALA   B HB2  1 
ATOM   5062 H HB3  . ALA   B 1 70  ? 51.754 -6.059  11.687  1.00 19.14 ?  70  ALA   B HB3  1 
ATOM   5063 N N    . THR   B 1 71  ? 48.861 -5.465  11.394  1.00 16.16 ?  71  THR   B N    1 
ATOM   5064 C CA   . THR   B 1 71  ? 47.977 -4.325  11.182  1.00 16.92 ?  71  THR   B CA   1 
ATOM   5065 C C    . THR   B 1 71  ? 46.511 -4.686  11.397  1.00 17.39 ?  71  THR   B C    1 
ATOM   5066 O O    . THR   B 1 71  ? 45.741 -3.874  11.927  1.00 18.93 ?  71  THR   B O    1 
ATOM   5067 C CB   . THR   B 1 71  ? 48.193 -3.773  9.771   1.00 18.71 ?  71  THR   B CB   1 
ATOM   5068 O OG1  . THR   B 1 71  ? 49.532 -3.272  9.652   1.00 21.12 ?  71  THR   B OG1  1 
ATOM   5069 C CG2  . THR   B 1 71  ? 47.188 -2.663  9.454   1.00 19.60 ?  71  THR   B CG2  1 
ATOM   5070 H H    . THR   B 1 71  ? 49.102 -5.867  10.677  1.00 19.40 ?  71  THR   B H    1 
ATOM   5071 H HA   . THR   B 1 71  ? 48.205 -3.627  11.815  1.00 20.32 ?  71  THR   B HA   1 
ATOM   5072 H HB   . THR   B 1 71  ? 48.066 -4.487  9.126   1.00 22.46 ?  71  THR   B HB   1 
ATOM   5073 H HG1  . THR   B 1 71  ? 49.651 -2.954  8.880   1.00 25.35 ?  71  THR   B HG1  1 
ATOM   5074 H HG21 . THR   B 1 71  ? 47.480 -2.164  8.675   1.00 23.53 ?  71  THR   B HG21 1 
ATOM   5075 H HG22 . THR   B 1 71  ? 46.313 -3.041  9.274   1.00 23.53 ?  71  THR   B HG22 1 
ATOM   5076 H HG23 . THR   B 1 71  ? 47.119 -2.052  10.207  1.00 23.53 ?  71  THR   B HG23 1 
ATOM   5077 N N    . ASN   B 1 72  ? 46.110 -5.893  11.001  1.00 17.61 ?  72  ASN   B N    1 
ATOM   5078 C CA   . ASN   B 1 72  ? 44.702 -6.241  10.887  1.00 18.18 ?  72  ASN   B CA   1 
ATOM   5079 C C    . ASN   B 1 72  ? 44.240 -7.329  11.843  1.00 18.71 ?  72  ASN   B C    1 
ATOM   5080 O O    . ASN   B 1 72  ? 43.025 -7.500  12.010  1.00 20.14 ?  72  ASN   B O    1 
ATOM   5081 C CB   . ASN   B 1 72  ? 44.382 -6.668  9.448   1.00 18.75 ?  72  ASN   B CB   1 
ATOM   5082 C CG   . ASN   B 1 72  ? 44.667 -5.567  8.446   1.00 19.37 ?  72  ASN   B CG   1 
ATOM   5083 O OD1  . ASN   B 1 72  ? 45.669 -5.594  7.724   1.00 20.69 ?  72  ASN   B OD1  1 
ATOM   5084 N ND2  . ASN   B 1 72  ? 43.803 -4.571  8.421   1.00 20.91 ?  72  ASN   B ND2  1 
ATOM   5085 H H    . ASN   B 1 72  ? 46.647 -6.540  10.787  1.00 21.14 ?  72  ASN   B H    1 
ATOM   5086 H HA   . ASN   B 1 72  ? 44.182 -5.450  11.080  1.00 21.83 ?  72  ASN   B HA   1 
ATOM   5087 H HB2  . ASN   B 1 72  ? 44.925 -7.436  9.215   1.00 22.51 ?  72  ASN   B HB2  1 
ATOM   5088 H HB3  . ASN   B 1 72  ? 43.441 -6.892  9.389   1.00 22.51 ?  72  ASN   B HB3  1 
ATOM   5089 H HD21 . ASN   B 1 72  ? 43.916 -3.918  7.871   1.00 25.09 ?  72  ASN   B HD21 1 
ATOM   5090 H HD22 . ASN   B 1 72  ? 43.116 -4.580  8.938   1.00 25.09 ?  72  ASN   B HD22 1 
ATOM   5091 N N    . GLY   B 1 73  ? 45.149 -8.066  12.470  1.00 18.10 ?  73  GLY   B N    1 
ATOM   5092 C CA   . GLY   B 1 73  ? 44.761 -9.206  13.263  1.00 17.71 ?  73  GLY   B CA   1 
ATOM   5093 C C    . GLY   B 1 73  ? 44.408 -10.401 12.398  1.00 16.71 ?  73  GLY   B C    1 
ATOM   5094 O O    . GLY   B 1 73  ? 44.400 -10.331 11.165  1.00 16.38 ?  73  GLY   B O    1 
ATOM   5095 H H    . GLY   B 1 73  ? 46.002 -7.921  12.456  1.00 21.73 ?  73  GLY   B H    1 
ATOM   5096 H HA2  . GLY   B 1 73  ? 45.486 -9.452  13.860  1.00 21.26 ?  73  GLY   B HA2  1 
ATOM   5097 H HA3  . GLY   B 1 73  ? 43.985 -8.978  13.803  1.00 21.26 ?  73  GLY   B HA3  1 
ATOM   5098 N N    . PRO   B 1 74  ? 44.101 -11.523 13.043  1.00 16.36 ?  74  PRO   B N    1 
ATOM   5099 C CA   . PRO   B 1 74  ? 43.840 -12.757 12.301  1.00 15.48 ?  74  PRO   B CA   1 
ATOM   5100 C C    . PRO   B 1 74  ? 42.548 -12.696 11.502  1.00 15.38 ?  74  PRO   B C    1 
ATOM   5101 O O    . PRO   B 1 74  ? 41.607 -11.958 11.821  1.00 16.63 ?  74  PRO   B O    1 
ATOM   5102 C CB   . PRO   B 1 74  ? 43.756 -13.816 13.407  1.00 17.04 ?  74  PRO   B CB   1 
ATOM   5103 C CG   . PRO   B 1 74  ? 43.349 -13.063 14.622  1.00 19.01 ?  74  PRO   B CG   1 
ATOM   5104 C CD   . PRO   B 1 74  ? 44.007 -11.723 14.498  1.00 18.04 ?  74  PRO   B CD   1 
ATOM   5105 H HA   . PRO   B 1 74  ? 44.585 -12.957 11.708  1.00 18.59 ?  74  PRO   B HA   1 
ATOM   5106 H HB2  . PRO   B 1 74  ? 43.089 -14.481 13.167  1.00 20.46 ?  74  PRO   B HB2  1 
ATOM   5107 H HB3  . PRO   B 1 74  ? 44.625 -14.232 13.528  1.00 20.46 ?  74  PRO   B HB3  1 
ATOM   5108 H HG2  . PRO   B 1 74  ? 42.384 -12.970 14.639  1.00 22.81 ?  74  PRO   B HG2  1 
ATOM   5109 H HG3  . PRO   B 1 74  ? 43.663 -13.528 15.412  1.00 22.81 ?  74  PRO   B HG3  1 
ATOM   5110 H HD2  . PRO   B 1 74  ? 43.452 -11.037 14.907  1.00 21.66 ?  74  PRO   B HD2  1 
ATOM   5111 H HD3  . PRO   B 1 74  ? 44.892 -11.743 14.895  1.00 21.66 ?  74  PRO   B HD3  1 
ATOM   5112 N N    . LEU   B 1 75  ? 42.518 -13.499 10.446  1.00 14.27 ?  75  LEU   B N    1 
ATOM   5113 C CA   . LEU   B 1 75  ? 41.304 -13.709 9.682   1.00 14.39 ?  75  LEU   B CA   1 
ATOM   5114 C C    . LEU   B 1 75  ? 40.322 -14.558 10.484  1.00 14.65 ?  75  LEU   B C    1 
ATOM   5115 O O    . LEU   B 1 75  ? 40.661 -15.144 11.514  1.00 15.92 ?  75  LEU   B O    1 
ATOM   5116 C CB   . LEU   B 1 75  ? 41.621 -14.436 8.375   1.00 14.67 ?  75  LEU   B CB   1 
ATOM   5117 C CG   . LEU   B 1 75  ? 42.463 -13.687 7.337   1.00 16.80 ?  75  LEU   B CG   1 
ATOM   5118 C CD1  . LEU   B 1 75  ? 42.643 -14.514 6.066   1.00 18.33 ?  75  LEU   B CD1  1 
ATOM   5119 C CD2  . LEU   B 1 75  ? 41.870 -12.345 7.010   1.00 20.86 ?  75  LEU   B CD2  1 
ATOM   5120 H H    . LEU   B 1 75  ? 43.195 -13.939 10.149  1.00 17.13 ?  75  LEU   B H    1 
ATOM   5121 H HA   . LEU   B 1 75  ? 40.888 -12.856 9.476   1.00 17.28 ?  75  LEU   B HA   1 
ATOM   5122 H HB2  . LEU   B 1 75  ? 42.096 -15.253 8.591   1.00 17.61 ?  75  LEU   B HB2  1 
ATOM   5123 H HB3  . LEU   B 1 75  ? 40.779 -14.664 7.943   1.00 17.61 ?  75  LEU   B HB3  1 
ATOM   5124 H HG   . LEU   B 1 75  ? 43.344 -13.534 7.712   1.00 20.17 ?  75  LEU   B HG   1 
ATOM   5125 H HD11 . LEU   B 1 75  ? 43.189 -14.011 5.439   1.00 22.01 ?  75  LEU   B HD11 1 
ATOM   5126 H HD12 . LEU   B 1 75  ? 43.085 -15.347 6.292   1.00 22.01 ?  75  LEU   B HD12 1 
ATOM   5127 H HD13 . LEU   B 1 75  ? 41.774 -14.693 5.679   1.00 22.01 ?  75  LEU   B HD13 1 
ATOM   5128 H HD21 . LEU   B 1 75  ? 42.351 -11.961 6.260   1.00 25.04 ?  75  LEU   B HD21 1 
ATOM   5129 H HD22 . LEU   B 1 75  ? 40.937 -12.465 6.782   1.00 25.04 ?  75  LEU   B HD22 1 
ATOM   5130 H HD23 . LEU   B 1 75  ? 41.951 -11.766 7.786   1.00 25.04 ?  75  LEU   B HD23 1 
ATOM   5131 N N    . LYS   B 1 76  ? 39.088 -14.618 9.987   1.00 16.17 ?  76  LYS   B N    1 
ATOM   5132 C CA   . LYS   B 1 76  ? 38.091 -15.568 10.461  1.00 16.96 ?  76  LYS   B CA   1 
ATOM   5133 C C    . LYS   B 1 76  ? 38.202 -16.853 9.646   1.00 15.64 ?  76  LYS   B C    1 
ATOM   5134 O O    . LYS   B 1 76  ? 38.494 -16.820 8.454   1.00 15.49 ?  76  LYS   B O    1 
ATOM   5135 C CB   . LYS   B 1 76  ? 36.675 -15.004 10.253  1.00 18.95 ?  76  LYS   B CB   1 
ATOM   5136 C CG   . LYS   B 1 76  ? 36.386 -13.650 10.916  1.00 20.37 ?  76  LYS   B CG   1 
ATOM   5137 C CD   . LYS   B 1 76  ? 35.003 -13.095 10.528  1.00 21.75 ?  76  LYS   B CD   1 
ATOM   5138 C CE   . LYS   B 1 76  ? 34.744 -11.730 11.146  1.00 24.06 ?  76  LYS   B CE   1 
ATOM   5139 N NZ   . LYS   B 1 76  ? 33.453 -11.145 10.698  1.00 24.94 ?  76  LYS   B NZ   1 
ATOM   5140 H H    . LYS   B 1 76  ? 38.797 -14.111 9.352   1.00 19.41 ?  76  LYS   B H    1 
ATOM   5141 H HA   . LYS   B 1 76  ? 38.228 -15.771 11.398  1.00 20.36 ?  76  LYS   B HA   1 
ATOM   5142 H HB2  . LYS   B 1 76  ? 36.528 -14.901 9.299   1.00 22.75 ?  76  LYS   B HB2  1 
ATOM   5143 H HB3  . LYS   B 1 76  ? 36.038 -15.645 10.608  1.00 22.75 ?  76  LYS   B HB3  1 
ATOM   5144 H HG2  . LYS   B 1 76  ? 36.416 -13.758 11.880  1.00 24.46 ?  76  LYS   B HG2  1 
ATOM   5145 H HG3  . LYS   B 1 76  ? 37.064 -13.010 10.634  1.00 24.46 ?  76  LYS   B HG3  1 
ATOM   5146 H HD2  . LYS   B 1 76  ? 34.957 -13.006 9.562   1.00 26.11 ?  76  LYS   B HD2  1 
ATOM   5147 H HD3  . LYS   B 1 76  ? 34.318 -13.705 10.841  1.00 26.11 ?  76  LYS   B HD3  1 
ATOM   5148 H HE2  . LYS   B 1 76  ? 34.721 -11.818 12.111  1.00 28.88 ?  76  LYS   B HE2  1 
ATOM   5149 H HE3  . LYS   B 1 76  ? 35.459 -11.124 10.885  1.00 28.88 ?  76  LYS   B HE3  1 
ATOM   5150 H HZ1  . LYS   B 1 76  ? 33.332 -10.346 11.077  1.00 29.93 ?  76  LYS   B HZ1  1 
ATOM   5151 H HZ2  . LYS   B 1 76  ? 33.451 -11.044 9.813   1.00 29.93 ?  76  LYS   B HZ2  1 
ATOM   5152 H HZ3  . LYS   B 1 76  ? 32.778 -11.677 10.930  1.00 29.93 ?  76  LYS   B HZ3  1 
ATOM   5153 N N    . VAL   B 1 77  ? 37.940 -17.994 10.289  1.00 16.43 ?  77  VAL   B N    1 
ATOM   5154 C CA   . VAL   B 1 77  ? 37.744 -19.217 9.519   1.00 16.59 ?  77  VAL   B CA   1 
ATOM   5155 C C    . VAL   B 1 77  ? 36.560 -18.997 8.591   1.00 15.48 ?  77  VAL   B C    1 
ATOM   5156 O O    . VAL   B 1 77  ? 35.489 -18.556 9.025   1.00 15.94 ?  77  VAL   B O    1 
ATOM   5157 C CB   . VAL   B 1 77  ? 37.526 -20.428 10.441  1.00 18.65 ?  77  VAL   B CB   1 
ATOM   5158 C CG1  . VAL   B 1 77  ? 37.254 -21.676 9.607   1.00 19.35 ?  77  VAL   B CG1  1 
ATOM   5159 C CG2  . VAL   B 1 77  ? 38.727 -20.640 11.357  1.00 19.86 ?  77  VAL   B CG2  1 
ATOM   5160 H H    . VAL   B 1 77  ? 37.878 -18.087 11.138  1.00 19.72 ?  77  VAL   B H    1 
ATOM   5161 H HA   . VAL   B 1 77  ? 38.527 -19.386 8.972   1.00 19.92 ?  77  VAL   B HA   1 
ATOM   5162 H HB   . VAL   B 1 77  ? 36.745 -20.262 10.993  1.00 22.39 ?  77  VAL   B HB   1 
ATOM   5163 H HG11 . VAL   B 1 77  ? 37.287 -22.451 10.187  1.00 23.23 ?  77  VAL   B HG11 1 
ATOM   5164 H HG12 . VAL   B 1 77  ? 36.369 -21.605 9.206   1.00 23.23 ?  77  VAL   B HG12 1 
ATOM   5165 H HG13 . VAL   B 1 77  ? 37.925 -21.746 8.915   1.00 23.23 ?  77  VAL   B HG13 1 
ATOM   5166 H HG21 . VAL   B 1 77  ? 38.575 -21.432 11.891  1.00 23.85 ?  77  VAL   B HG21 1 
ATOM   5167 H HG22 . VAL   B 1 77  ? 39.519 -20.747 10.812  1.00 23.85 ?  77  VAL   B HG22 1 
ATOM   5168 H HG23 . VAL   B 1 77  ? 38.820 -19.863 11.931  1.00 23.85 ?  77  VAL   B HG23 1 
ATOM   5169 N N    . GLY   B 1 78  ? 36.752 -19.293 7.306   1.00 14.50 ?  78  GLY   B N    1 
ATOM   5170 C CA   . GLY   B 1 78  ? 35.790 -18.980 6.280   1.00 14.60 ?  78  GLY   B CA   1 
ATOM   5171 C C    . GLY   B 1 78  ? 36.024 -17.660 5.584   1.00 14.22 ?  78  GLY   B C    1 
ATOM   5172 O O    . GLY   B 1 78  ? 35.343 -17.382 4.591   1.00 14.95 ?  78  GLY   B O    1 
ATOM   5173 H H    . GLY   B 1 78  ? 37.457 -19.686 7.004   1.00 17.40 ?  78  GLY   B H    1 
ATOM   5174 H HA2  . GLY   B 1 78  ? 35.803 -19.673 5.608   1.00 17.53 ?  78  GLY   B HA2  1 
ATOM   5175 H HA3  . GLY   B 1 78  ? 34.904 -18.953 6.675   1.00 17.53 ?  78  GLY   B HA3  1 
ATOM   5176 N N    . GLY   B 1 79  ? 36.964 -16.845 6.075   1.00 14.24 ?  79  GLY   B N    1 
ATOM   5177 C CA   . GLY   B 1 79  ? 37.267 -15.557 5.490   1.00 14.00 ?  79  GLY   B CA   1 
ATOM   5178 C C    . GLY   B 1 79  ? 38.488 -15.596 4.581   1.00 13.36 ?  79  GLY   B C    1 
ATOM   5179 O O    . GLY   B 1 79  ? 39.092 -16.639 4.342   1.00 13.76 ?  79  GLY   B O    1 
ATOM   5180 H H    . GLY   B 1 79  ? 37.456 -17.027 6.755   1.00 17.09 ?  79  GLY   B H    1 
ATOM   5181 H HA2  . GLY   B 1 79  ? 36.510 -15.247 4.965   1.00 16.80 ?  79  GLY   B HA2  1 
ATOM   5182 H HA3  . GLY   B 1 79  ? 37.437 -14.908 6.191   1.00 16.80 ?  79  GLY   B HA3  1 
ATOM   5183 N N    . SER   B 1 80  ? 38.862 -14.416 4.087   1.00 13.25 ?  80  SER   B N    1 
ATOM   5184 C CA   . SER   B 1 80  ? 39.970 -14.297 3.148   1.00 13.40 ?  80  SER   B CA   1 
ATOM   5185 C C    . SER   B 1 80  ? 40.558 -12.892 3.195   1.00 13.14 ?  80  SER   B C    1 
ATOM   5186 O O    . SER   B 1 80  ? 39.945 -11.951 3.704   1.00 14.25 ?  80  SER   B O    1 
ATOM   5187 C CB   . SER   B 1 80  ? 39.526 -14.595 1.713   1.00 13.54 ?  80  SER   B CB   1 
ATOM   5188 O OG   . SER   B 1 80  ? 38.677 -13.572 1.218   1.00 14.90 ?  80  SER   B OG   1 
ATOM   5189 H H    . SER   B 1 80  ? 38.495 -13.667 4.283   1.00 15.91 ?  80  SER   B H    1 
ATOM   5190 H HA   . SER   B 1 80  ? 40.661 -14.925 3.392   1.00 16.09 ?  80  SER   B HA   1 
ATOM   5191 H HB2  . SER   B 1 80  ? 40.308 -14.647 1.137   1.00 16.25 ?  80  SER   B HB2  1 
ATOM   5192 H HB3  . SER   B 1 80  ? 39.045 -15.434 1.694   1.00 16.25 ?  80  SER   B HB3  1 
ATOM   5193 H HG   . SER   B 1 80  ? 37.986 -13.509 1.697   1.00 17.89 ?  80  SER   B HG   1 
ATOM   5194 N N    . CYS   B 1 81  ? 41.741 -12.757 2.600   1.00 12.70 ?  81  CYS   B N    1 
ATOM   5195 C CA   . CYS   B 1 81  ? 42.293 -11.445 2.292   1.00 12.66 ?  81  CYS   B CA   1 
ATOM   5196 C C    . CYS   B 1 81  ? 43.064 -11.537 0.982   1.00 11.98 ?  81  CYS   B C    1 
ATOM   5197 O O    . CYS   B 1 81  ? 43.558 -12.604 0.601   1.00 13.25 ?  81  CYS   B O    1 
ATOM   5198 C CB   . CYS   B 1 81  ? 43.180 -10.901 3.419   1.00 14.33 ?  81  CYS   B CB   1 
ATOM   5199 S SG   . CYS   B 1 81  ? 44.697 -11.838 3.672   1.00 14.52 ?  81  CYS   B SG   1 
ATOM   5200 H H    . CYS   B 1 81  ? 42.250 -13.412 2.370   1.00 15.25 ?  81  CYS   B H    1 
ATOM   5201 H HA   . CYS   B 1 81  ? 41.560 -10.820 2.164   1.00 15.20 ?  81  CYS   B HA   1 
ATOM   5202 H HB2  . CYS   B 1 81  ? 43.434 -9.987  3.205   1.00 17.21 ?  81  CYS   B HB2  1 
ATOM   5203 H HB3  . CYS   B 1 81  ? 42.675 -10.911 4.248   1.00 17.21 ?  81  CYS   B HB3  1 
ATOM   5204 H HG   . CYS   B 1 81  ? 45.316 -11.342 4.579   1.00 17.44 ?  81  CYS   B HG   1 
ATOM   5205 N N    . VAL   B 1 82  ? 43.168 -10.398 0.303   1.00 12.75 ?  82  VAL   B N    1 
ATOM   5206 C CA   . VAL   B 1 82  ? 43.925 -10.282 -0.942  1.00 12.96 ?  82  VAL   B CA   1 
ATOM   5207 C C    . VAL   B 1 82  ? 45.262 -9.634  -0.630  1.00 13.27 ?  82  VAL   B C    1 
ATOM   5208 O O    . VAL   B 1 82  ? 45.307 -8.512  -0.108  1.00 14.39 ?  82  VAL   B O    1 
ATOM   5209 C CB   . VAL   B 1 82  ? 43.169 -9.448  -1.987  1.00 14.15 ?  82  VAL   B CB   1 
ATOM   5210 C CG1  . VAL   B 1 82  ? 43.987 -9.348  -3.277  1.00 15.90 ?  82  VAL   B CG1  1 
ATOM   5211 C CG2  . VAL   B 1 82  ? 41.790 -10.021 -2.247  1.00 15.57 ?  82  VAL   B CG2  1 
ATOM   5212 H H    . VAL   B 1 82  ? 42.800 -9.652  0.544   1.00 15.30 ?  82  VAL   B H    1 
ATOM   5213 H HA   . VAL   B 1 82  ? 44.081 -11.166 -1.309  1.00 15.55 ?  82  VAL   B HA   1 
ATOM   5214 H HB   . VAL   B 1 82  ? 43.054 -8.550  -1.647  1.00 16.98 ?  82  VAL   B HB   1 
ATOM   5215 H HG11 . VAL   B 1 82  ? 43.423 -8.998  -3.985  1.00 19.08 ?  82  VAL   B HG11 1 
ATOM   5216 H HG12 . VAL   B 1 82  ? 44.740 -8.752  -3.133  1.00 19.08 ?  82  VAL   B HG12 1 
ATOM   5217 H HG13 . VAL   B 1 82  ? 44.307 -10.232 -3.519  1.00 19.08 ?  82  VAL   B HG13 1 
ATOM   5218 H HG21 . VAL   B 1 82  ? 41.362 -9.508  -2.955  1.00 18.69 ?  82  VAL   B HG21 1 
ATOM   5219 H HG22 . VAL   B 1 82  ? 41.875 -10.947 -2.519  1.00 18.69 ?  82  VAL   B HG22 1 
ATOM   5220 H HG23 . VAL   B 1 82  ? 41.264 -9.959  -1.435  1.00 18.69 ?  82  VAL   B HG23 1 
ATOM   5221 N N    . LEU   B 1 83  ? 46.346 -10.317 -0.982  1.00 13.11 ?  83  LEU   B N    1 
ATOM   5222 C CA   . LEU   B 1 83  ? 47.700 -9.795  -0.866  1.00 12.89 ?  83  LEU   B CA   1 
ATOM   5223 C C    . LEU   B 1 83  ? 48.402 -9.954  -2.214  1.00 13.09 ?  83  LEU   B C    1 
ATOM   5224 O O    . LEU   B 1 83  ? 47.806 -10.396 -3.198  1.00 12.90 ?  83  LEU   B O    1 
ATOM   5225 C CB   . LEU   B 1 83  ? 48.450 -10.470 0.287   1.00 13.55 ?  83  LEU   B CB   1 
ATOM   5226 C CG   . LEU   B 1 83  ? 47.939 -10.117 1.687   1.00 14.86 ?  83  LEU   B CG   1 
ATOM   5227 C CD1  . LEU   B 1 83  ? 48.585 -10.998 2.736   1.00 15.89 ?  83  LEU   B CD1  1 
ATOM   5228 C CD2  . LEU   B 1 83  ? 48.169 -8.644  2.014   1.00 16.38 ?  83  LEU   B CD2  1 
ATOM   5229 H H    . LEU   B 1 83  ? 46.317 -11.119 -1.304  1.00 15.74 ?  83  LEU   B H    1 
ATOM   5230 H HA   . LEU   B 1 83  ? 47.646 -8.849  -0.674  1.00 15.47 ?  83  LEU   B HA   1 
ATOM   5231 H HB2  . LEU   B 1 83  ? 48.385 -11.427 0.184   1.00 16.26 ?  83  LEU   B HB2  1 
ATOM   5232 H HB3  . LEU   B 1 83  ? 49.380 -10.197 0.245   1.00 16.26 ?  83  LEU   B HB3  1 
ATOM   5233 H HG   . LEU   B 1 83  ? 46.983 -10.282 1.715   1.00 17.84 ?  83  LEU   B HG   1 
ATOM   5234 H HD11 . LEU   B 1 83  ? 48.236 -10.764 3.611   1.00 19.07 ?  83  LEU   B HD11 1 
ATOM   5235 H HD12 . LEU   B 1 83  ? 48.373 -11.932 2.543   1.00 19.07 ?  83  LEU   B HD12 1 
ATOM   5236 H HD13 . LEU   B 1 83  ? 49.545 -10.873 2.716   1.00 19.07 ?  83  LEU   B HD13 1 
ATOM   5237 H HD21 . LEU   B 1 83  ? 47.960 -8.494  2.948   1.00 19.67 ?  83  LEU   B HD21 1 
ATOM   5238 H HD22 . LEU   B 1 83  ? 49.097 -8.426  1.841   1.00 19.67 ?  83  LEU   B HD22 1 
ATOM   5239 H HD23 . LEU   B 1 83  ? 47.591 -8.104  1.453   1.00 19.67 ?  83  LEU   B HD23 1 
ATOM   5240 N N    . SER   B 1 84  ? 49.675 -9.571  -2.275  1.00 13.84 ?  84  SER   B N    1 
ATOM   5241 C CA   . SER   B 1 84  ? 50.407 -9.711  -3.523  1.00 14.18 ?  84  SER   B CA   1 
ATOM   5242 C C    . SER   B 1 84  ? 50.576 -11.177 -3.903  1.00 12.97 ?  84  SER   B C    1 
ATOM   5243 O O    . SER   B 1 84  ? 50.699 -12.057 -3.049  1.00 13.27 ?  84  SER   B O    1 
ATOM   5244 C CB   . SER   B 1 84  ? 51.790 -9.076  -3.396  1.00 15.96 ?  84  SER   B CB   1 
ATOM   5245 O OG   . SER   B 1 84  ? 52.559 -9.330  -4.559  1.00 17.37 ?  84  SER   B OG   1 
ATOM   5246 H H    . SER   B 1 84  ? 50.119 -9.227  -1.624  1.00 16.62 ?  84  SER   B H    1 
ATOM   5247 H HA   . SER   B 1 84  ? 49.927 -9.262  -4.233  1.00 17.02 ?  84  SER   B HA   1 
ATOM   5248 H HB2  . SER   B 1 84  ? 51.686 -8.113  -3.270  1.00 19.16 ?  84  SER   B HB2  1 
ATOM   5249 H HB3  . SER   B 1 84  ? 52.248 -9.455  -2.630  1.00 19.16 ?  84  SER   B HB3  1 
ATOM   5250 H HG   . SER   B 1 84  ? 53.317 -8.952  -4.485  1.00 20.85 ?  84  SER   B HG   1 
ATOM   5251 N N    . GLY   B 1 85  ? 50.657 -11.422 -5.200  1.00 13.70 ?  85  GLY   B N    1 
ATOM   5252 C CA   . GLY   B 1 85  ? 51.005 -12.733 -5.697  1.00 15.09 ?  85  GLY   B CA   1 
ATOM   5253 C C    . GLY   B 1 85  ? 52.470 -12.926 -6.030  1.00 13.98 ?  85  GLY   B C    1 
ATOM   5254 O O    . GLY   B 1 85  ? 52.850 -14.012 -6.477  1.00 14.49 ?  85  GLY   B O    1 
ATOM   5255 H H    . GLY   B 1 85  ? 50.517 -10.841 -5.816  1.00 16.45 ?  85  GLY   B H    1 
ATOM   5256 H HA2  . GLY   B 1 85  ? 50.759 -13.398 -5.027  1.00 18.12 ?  85  GLY   B HA2  1 
ATOM   5257 H HA3  . GLY   B 1 85  ? 50.497 -12.914 -6.495  1.00 18.12 ?  85  GLY   B HA3  1 
ATOM   5258 N N    . HIS   B 1 86  ? 53.312 -11.912 -5.841  1.00 14.08 ?  86  HIS   B N    1 
ATOM   5259 C CA   . HIS   B 1 86  ? 54.771 -12.071 -5.923  1.00 14.39 ?  86  HIS   B CA   1 
ATOM   5260 C C    . HIS   B 1 86  ? 55.135 -12.599 -7.309  1.00 14.49 ?  86  HIS   B C    1 
ATOM   5261 O O    . HIS   B 1 86  ? 54.740 -11.993 -8.317  1.00 15.24 ?  86  HIS   B O    1 
ATOM   5262 C CB   . HIS   B 1 86  ? 55.263 -12.896 -4.734  1.00 15.16 ?  86  HIS   B CB   1 
ATOM   5263 C CG   . HIS   B 1 86  ? 54.943 -12.272 -3.418  1.00 15.57 ?  86  HIS   B CG   1 
ATOM   5264 N ND1  . HIS   B 1 86  ? 55.760 -11.336 -2.819  1.00 17.60 ?  86  HIS   B ND1  1 
ATOM   5265 C CD2  . HIS   B 1 86  ? 53.870 -12.416 -2.604  1.00 15.89 ?  86  HIS   B CD2  1 
ATOM   5266 C CE1  . HIS   B 1 86  ? 55.202 -10.934 -1.691  1.00 17.59 ?  86  HIS   B CE1  1 
ATOM   5267 N NE2  . HIS   B 1 86  ? 54.054 -11.571 -1.539  1.00 16.67 ?  86  HIS   B NE2  1 
ATOM   5268 H H    . HIS   B 1 86  ? 53.065 -11.107 -5.678  1.00 16.91 ?  86  HIS   B H    1 
ATOM   5269 H HA   . HIS   B 1 86  ? 55.175 -11.193 -5.843  1.00 17.28 ?  86  HIS   B HA   1 
ATOM   5270 H HB2  . HIS   B 1 86  ? 54.844 -13.770 -4.760  1.00 18.20 ?  86  HIS   B HB2  1 
ATOM   5271 H HB3  . HIS   B 1 86  ? 56.226 -12.987 -4.787  1.00 18.20 ?  86  HIS   B HB3  1 
ATOM   5272 H HD2  . HIS   B 1 86  ? 53.129 -12.968 -2.746  1.00 19.07 ?  86  HIS   B HD2  1 
ATOM   5273 H HE1  . HIS   B 1 86  ? 55.557 -10.314 -1.096  1.00 21.11 ?  86  HIS   B HE1  1 
ATOM   5274 H HE2  . HIS   B 1 86  ? 53.511 -11.478 -0.870  1.00 20.01 ?  86  HIS   B HE2  1 
ATOM   5275 N N    . ASN   B 1 87  ? 55.907 -13.678 -7.414  1.00 15.02 ?  87  ASN   B N    1 
ATOM   5276 C CA   . ASN   B 1 87  ? 56.285 -14.264 -8.692  1.00 15.79 ?  87  ASN   B CA   1 
ATOM   5277 C C    . ASN   B 1 87  ? 55.291 -15.301 -9.184  1.00 15.67 ?  87  ASN   B C    1 
ATOM   5278 O O    . ASN   B 1 87  ? 55.580 -16.001 -10.162 1.00 17.69 ?  87  ASN   B O    1 
ATOM   5279 C CB   . ASN   B 1 87  ? 57.669 -14.912 -8.587  1.00 17.82 ?  87  ASN   B CB   1 
ATOM   5280 C CG   . ASN   B 1 87  ? 57.717 -16.026 -7.549  1.00 18.28 ?  87  ASN   B CG   1 
ATOM   5281 O OD1  . ASN   B 1 87  ? 57.113 -15.923 -6.477  1.00 17.83 ?  87  ASN   B OD1  1 
ATOM   5282 N ND2  . ASN   B 1 87  ? 58.425 -17.111 -7.875  1.00 20.61 ?  87  ASN   B ND2  1 
ATOM   5283 H H    . ASN   B 1 87  ? 56.233 -14.102 -6.739  1.00 18.03 ?  87  ASN   B H    1 
ATOM   5284 H HA   . ASN   B 1 87  ? 56.333 -13.562 -9.356  1.00 18.95 ?  87  ASN   B HA   1 
ATOM   5285 H HB2  . ASN   B 1 87  ? 57.902 -15.292 -9.452  1.00 21.39 ?  87  ASN   B HB2  1 
ATOM   5286 H HB3  . ASN   B 1 87  ? 58.311 -14.235 -8.338  1.00 21.39 ?  87  ASN   B HB3  1 
ATOM   5287 H HD21 . ASN   B 1 87  ? 58.483 -17.768 -7.325  1.00 24.74 ?  87  ASN   B HD21 1 
ATOM   5288 H HD22 . ASN   B 1 87  ? 58.820 -17.155 -8.640  1.00 24.74 ?  87  ASN   B HD22 1 
ATOM   5289 N N    . LEU   B 1 88  ? 54.129 -15.413 -8.539  1.00 14.35 ?  88  LEU   B N    1 
ATOM   5290 C CA   . LEU   B 1 88  ? 53.143 -16.440 -8.865  1.00 14.51 ?  88  LEU   B CA   1 
ATOM   5291 C C    . LEU   B 1 88  ? 51.908 -15.923 -9.582  1.00 14.52 ?  88  LEU   B C    1 
ATOM   5292 O O    . LEU   B 1 88  ? 51.302 -16.668 -10.351 1.00 16.55 ?  88  LEU   B O    1 
ATOM   5293 C CB   . LEU   B 1 88  ? 52.680 -17.142 -7.585  1.00 15.76 ?  88  LEU   B CB   1 
ATOM   5294 C CG   . LEU   B 1 88  ? 53.819 -17.787 -6.798  1.00 18.89 ?  88  LEU   B CG   1 
ATOM   5295 C CD1  . LEU   B 1 88  ? 53.352 -18.245 -5.420  1.00 20.70 ?  88  LEU   B CD1  1 
ATOM   5296 C CD2  . LEU   B 1 88  ? 54.428 -18.937 -7.587  1.00 21.86 ?  88  LEU   B CD2  1 
ATOM   5297 H H    . LEU   B 1 88  ? 53.889 -14.902 -7.880  1.00 17.22 ?  88  LEU   B H    1 
ATOM   5298 H HA   . LEU   B 1 88  ? 53.560 -17.099 -9.429  1.00 17.42 ?  88  LEU   B HA   1 
ATOM   5299 H HB2  . LEU   B 1 88  ? 52.241 -16.499 -7.003  1.00 18.92 ?  88  LEU   B HB2  1 
ATOM   5300 H HB3  . LEU   B 1 88  ? 52.047 -17.845 -7.824  1.00 18.92 ?  88  LEU   B HB3  1 
ATOM   5301 H HG   . LEU   B 1 88  ? 54.508 -17.125 -6.663  1.00 22.67 ?  88  LEU   B HG   1 
ATOM   5302 H HD11 . LEU   B 1 88  ? 54.095 -18.671 -4.961  1.00 24.84 ?  88  LEU   B HD11 1 
ATOM   5303 H HD12 . LEU   B 1 88  ? 53.049 -17.476 -4.914  1.00 24.84 ?  88  LEU   B HD12 1 
ATOM   5304 H HD13 . LEU   B 1 88  ? 52.626 -18.879 -5.526  1.00 24.84 ?  88  LEU   B HD13 1 
ATOM   5305 H HD21 . LEU   B 1 88  ? 55.047 -19.415 -7.015  1.00 26.23 ?  88  LEU   B HD21 1 
ATOM   5306 H HD22 . LEU   B 1 88  ? 53.719 -19.531 -7.880  1.00 26.23 ?  88  LEU   B HD22 1 
ATOM   5307 H HD23 . LEU   B 1 88  ? 54.897 -18.577 -8.356  1.00 26.23 ?  88  LEU   B HD23 1 
ATOM   5308 N N    . ALA   B 1 89  ? 51.514 -14.679 -9.338  1.00 13.52 ?  89  ALA   B N    1 
ATOM   5309 C CA   . ALA   B 1 89  ? 50.219 -14.177 -9.773  1.00 13.01 ?  89  ALA   B CA   1 
ATOM   5310 C C    . ALA   B 1 89  ? 50.212 -12.689 -9.483  1.00 13.71 ?  89  ALA   B C    1 
ATOM   5311 O O    . ALA   B 1 89  ? 51.039 -12.193 -8.716  1.00 14.50 ?  89  ALA   B O    1 
ATOM   5312 C CB   . ALA   B 1 89  ? 49.084 -14.846 -9.007  1.00 13.29 ?  89  ALA   B CB   1 
ATOM   5313 H H    . ALA   B 1 89  ? 51.987 -14.091 -8.922  1.00 16.23 ?  89  ALA   B H    1 
ATOM   5314 H HA   . ALA   B 1 89  ? 50.096 -14.317 -10.729 1.00 15.63 ?  89  ALA   B HA   1 
ATOM   5315 H HB1  . ALA   B 1 89  ? 48.238 -14.505 -9.337  1.00 15.95 ?  89  ALA   B HB1  1 
ATOM   5316 H HB2  . ALA   B 1 89  ? 49.134 -15.804 -9.155  1.00 15.95 ?  89  ALA   B HB2  1 
ATOM   5317 H HB3  . ALA   B 1 89  ? 49.183 -14.648 -8.067  1.00 15.95 ?  89  ALA   B HB3  1 
ATOM   5318 N N    . LYS   B 1 90  ? 49.244 -11.979 -10.061 1.00 14.53 ?  90  LYS   B N    1 
ATOM   5319 C CA   . LYS   B 1 90  ? 49.064 -10.593 -9.653  1.00 14.47 ?  90  LYS   B CA   1 
ATOM   5320 C C    . LYS   B 1 90  ? 48.743 -10.524 -8.166  1.00 14.13 ?  90  LYS   B C    1 
ATOM   5321 O O    . LYS   B 1 90  ? 49.380 -9.775  -7.410  1.00 15.10 ?  90  LYS   B O    1 
ATOM   5322 C CB   . LYS   B 1 90  ? 47.986 -9.921  -10.503 1.00 16.46 ?  90  LYS   B CB   1 
ATOM   5323 C CG   . LYS   B 1 90  ? 47.688 -8.490  -10.092 1.00 16.88 ?  90  LYS   B CG   1 
ATOM   5324 C CD   . LYS   B 1 90  ? 48.880 -7.585  -10.175 1.00 19.76 ?  90  LYS   B CD   1 
ATOM   5325 C CE   . LYS   B 1 90  ? 48.419 -6.171  -9.920  1.00 21.27 ?  90  LYS   B CE   1 
ATOM   5326 N NZ   . LYS   B 1 90  ? 49.559 -5.236  -9.844  1.00 20.62 ?  90  LYS   B NZ   1 
ATOM   5327 H H    . LYS   B 1 90  ? 48.702 -12.265 -10.671 1.00 17.45 ?  90  LYS   B H    1 
ATOM   5328 H HA   . LYS   B 1 90  ? 49.891 -10.116 -9.799  1.00 17.37 ?  90  LYS   B HA   1 
ATOM   5329 H HB2  . LYS   B 1 90  ? 48.281 -9.904  -11.430 1.00 19.76 ?  90  LYS   B HB2  1 
ATOM   5330 H HB3  . LYS   B 1 90  ? 47.163 -10.432 -10.435 1.00 19.76 ?  90  LYS   B HB3  1 
ATOM   5331 H HG2  . LYS   B 1 90  ? 46.998 -8.135  -10.681 1.00 20.26 ?  90  LYS   B HG2  1 
ATOM   5332 H HG3  . LYS   B 1 90  ? 47.358 -8.484  -9.176  1.00 20.26 ?  90  LYS   B HG3  1 
ATOM   5333 H HD2  . LYS   B 1 90  ? 49.525 -7.829  -9.494  1.00 23.72 ?  90  LYS   B HD2  1 
ATOM   5334 H HD3  . LYS   B 1 90  ? 49.269 -7.634  -11.059 1.00 23.72 ?  90  LYS   B HD3  1 
ATOM   5335 H HE2  . LYS   B 1 90  ? 47.842 -5.877  -10.647 1.00 25.54 ?  90  LYS   B HE2  1 
ATOM   5336 H HE3  . LYS   B 1 90  ? 47.938 -6.125  -9.077  1.00 25.54 ?  90  LYS   B HE3  1 
ATOM   5337 H HZ1  . LYS   B 1 90  ? 49.272 -4.407  -9.695  1.00 24.76 ?  90  LYS   B HZ1  1 
ATOM   5338 H HZ2  . LYS   B 1 90  ? 50.103 -5.475  -9.181  1.00 24.76 ?  90  LYS   B HZ2  1 
ATOM   5339 H HZ3  . LYS   B 1 90  ? 50.015 -5.250  -10.609 1.00 24.76 ?  90  LYS   B HZ3  1 
ATOM   5340 N N    . HIS   B 1 91  ? 47.775 -11.333 -7.728  1.00 13.04 ?  91  HIS   B N    1 
ATOM   5341 C CA   . HIS   B 1 91  ? 47.295 -11.350 -6.357  1.00 12.88 ?  91  HIS   B CA   1 
ATOM   5342 C C    . HIS   B 1 91  ? 47.287 -12.774 -5.829  1.00 12.21 ?  91  HIS   B C    1 
ATOM   5343 O O    . HIS   B 1 91  ? 47.064 -13.730 -6.577  1.00 12.47 ?  91  HIS   B O    1 
ATOM   5344 C CB   . HIS   B 1 91  ? 45.852 -10.853 -6.242  1.00 14.31 ?  91  HIS   B CB   1 
ATOM   5345 C CG   . HIS   B 1 91  ? 45.660 -9.442  -6.675  1.00 17.81 ?  91  HIS   B CG   1 
ATOM   5346 N ND1  . HIS   B 1 91  ? 46.273 -8.374  -6.053  1.00 19.87 ?  91  HIS   B ND1  1 
ATOM   5347 C CD2  . HIS   B 1 91  ? 44.890 -8.915  -7.653  1.00 20.55 ?  91  HIS   B CD2  1 
ATOM   5348 C CE1  . HIS   B 1 91  ? 45.909 -7.251  -6.646  1.00 21.65 ?  91  HIS   B CE1  1 
ATOM   5349 N NE2  . HIS   B 1 91  ? 45.064 -7.552  -7.616  1.00 22.09 ?  91  HIS   B NE2  1 
ATOM   5350 H H    . HIS   B 1 91  ? 47.360 -11.901 -8.228  1.00 15.66 ?  91  HIS   B H    1 
ATOM   5351 H HA   . HIS   B 1 91  ? 47.873 -10.796 -5.793  1.00 15.46 ?  91  HIS   B HA   1 
ATOM   5352 H HB2  . HIS   B 1 91  ? 45.288 -11.413 -6.797  1.00 17.18 ?  91  HIS   B HB2  1 
ATOM   5353 H HB3  . HIS   B 1 91  ? 45.570 -10.920 -5.315  1.00 17.18 ?  91  HIS   B HB3  1 
ATOM   5354 H HD1  . HIS   B 1 91  ? 46.821 -8.435  -5.390  1.00 23.85 ?  91  HIS   B HD1  1 
ATOM   5355 H HD2  . HIS   B 1 91  ? 44.353 -9.376  -8.252  1.00 24.67 ?  91  HIS   B HD2  1 
ATOM   5356 H HE1  . HIS   B 1 91  ? 46.198 -6.395  -6.409  1.00 25.99 ?  91  HIS   B HE1  1 
ATOM   5357 N N    . CYS   B 1 92  ? 47.476 -12.897 -4.525  1.00 12.05 ?  92  CYS   B N    1 
ATOM   5358 C CA   . CYS   B 1 92  ? 47.166 -14.129 -3.816  1.00 11.85 ?  92  CYS   B CA   1 
ATOM   5359 C C    . CYS   B 1 92  ? 45.948 -13.893 -2.936  1.00 11.46 ?  92  CYS   B C    1 
ATOM   5360 O O    . CYS   B 1 92  ? 45.948 -12.981 -2.097  1.00 12.65 ?  92  CYS   B O    1 
ATOM   5361 C CB   . CYS   B 1 92  ? 48.347 -14.582 -2.968  1.00 12.41 ?  92  CYS   B CB   1 
ATOM   5362 S SG   . CYS   B 1 92  ? 47.978 -16.119 -2.058  1.00 13.03 ?  92  CYS   B SG   1 
ATOM   5363 H H    . CYS   B 1 92  ? 47.800 -12.277 -4.022  1.00 14.47 ?  92  CYS   B H    1 
ATOM   5364 H HA   . CYS   B 1 92  ? 46.961 -14.827 -4.462  1.00 14.22 ?  92  CYS   B HA   1 
ATOM   5365 H HB2  . CYS   B 1 92  ? 49.108 -14.753 -3.539  1.00 14.90 ?  92  CYS   B HB2  1 
ATOM   5366 H HB3  . CYS   B 1 92  ? 48.553 -13.898 -2.318  1.00 14.90 ?  92  CYS   B HB3  1 
ATOM   5367 H HG   . CYS   B 1 92  ? 48.943 -16.439 -1.425  1.00 15.64 ?  92  CYS   B HG   1 
ATOM   5368 N N    . LEU   B 1 93  ? 44.911 -14.700 -3.145  1.00 11.53 ?  93  LEU   B N    1 
ATOM   5369 C CA   . LEU   B 1 93  ? 43.735 -14.709 -2.289  1.00 11.29 ?  93  LEU   B CA   1 
ATOM   5370 C C    . LEU   B 1 93  ? 43.959 -15.760 -1.214  1.00 10.65 ?  93  LEU   B C    1 
ATOM   5371 O O    . LEU   B 1 93  ? 43.901 -16.963 -1.492  1.00 11.90 ?  93  LEU   B O    1 
ATOM   5372 C CB   . LEU   B 1 93  ? 42.478 -15.013 -3.097  1.00 11.97 ?  93  LEU   B CB   1 
ATOM   5373 C CG   . LEU   B 1 93  ? 41.183 -15.018 -2.287  1.00 12.69 ?  93  LEU   B CG   1 
ATOM   5374 C CD1  . LEU   B 1 93  ? 40.833 -13.626 -1.800  1.00 13.49 ?  93  LEU   B CD1  1 
ATOM   5375 C CD2  . LEU   B 1 93  ? 40.048 -15.627 -3.108  1.00 13.34 ?  93  LEU   B CD2  1 
ATOM   5376 H H    . LEU   B 1 93  ? 44.864 -15.265 -3.802  1.00 13.85 ?  93  LEU   B H    1 
ATOM   5377 H HA   . LEU   B 1 93  ? 43.635 -13.839 -1.870  1.00 13.56 ?  93  LEU   B HA   1 
ATOM   5378 H HB2  . LEU   B 1 93  ? 42.384 -14.339 -3.794  1.00 14.37 ?  93  LEU   B HB2  1 
ATOM   5379 H HB3  . LEU   B 1 93  ? 42.577 -15.886 -3.507  1.00 14.37 ?  93  LEU   B HB3  1 
ATOM   5380 H HG   . LEU   B 1 93  ? 41.311 -15.581 -1.509  1.00 15.24 ?  93  LEU   B HG   1 
ATOM   5381 H HD11 . LEU   B 1 93  ? 39.975 -13.657 -1.352  1.00 16.20 ?  93  LEU   B HD11 1 
ATOM   5382 H HD12 . LEU   B 1 93  ? 41.519 -13.324 -1.185  1.00 16.20 ?  93  LEU   B HD12 1 
ATOM   5383 H HD13 . LEU   B 1 93  ? 40.786 -13.028 -2.564  1.00 16.20 ?  93  LEU   B HD13 1 
ATOM   5384 H HD21 . LEU   B 1 93  ? 39.235 -15.621 -2.575  1.00 16.01 ?  93  LEU   B HD21 1 
ATOM   5385 H HD22 . LEU   B 1 93  ? 39.918 -15.101 -3.913  1.00 16.01 ?  93  LEU   B HD22 1 
ATOM   5386 H HD23 . LEU   B 1 93  ? 40.277 -16.541 -3.345  1.00 16.01 ?  93  LEU   B HD23 1 
ATOM   5387 N N    . HIS   B 1 94  ? 44.235 -15.317 -0.001  1.00 10.70 ?  94  HIS   B N    1 
ATOM   5388 C CA   . HIS   B 1 94  ? 44.447 -16.223 1.117   1.00 11.01 ?  94  HIS   B CA   1 
ATOM   5389 C C    . HIS   B 1 94  ? 43.084 -16.569 1.696   1.00 11.73 ?  94  HIS   B C    1 
ATOM   5390 O O    . HIS   B 1 94  ? 42.409 -15.686 2.226   1.00 13.39 ?  94  HIS   B O    1 
ATOM   5391 C CB   . HIS   B 1 94  ? 45.317 -15.553 2.179   1.00 11.65 ?  94  HIS   B CB   1 
ATOM   5392 C CG   . HIS   B 1 94  ? 46.698 -15.249 1.716   1.00 11.94 ?  94  HIS   B CG   1 
ATOM   5393 N ND1  . HIS   B 1 94  ? 47.723 -16.167 1.803   1.00 12.34 ?  94  HIS   B ND1  1 
ATOM   5394 C CD2  . HIS   B 1 94  ? 47.211 -14.141 1.131   1.00 12.75 ?  94  HIS   B CD2  1 
ATOM   5395 C CE1  . HIS   B 1 94  ? 48.817 -15.616 1.304   1.00 12.51 ?  94  HIS   B CE1  1 
ATOM   5396 N NE2  . HIS   B 1 94  ? 48.534 -14.393 0.888   1.00 13.24 ?  94  HIS   B NE2  1 
ATOM   5397 H H    . HIS   B 1 94  ? 44.315 -14.477 0.196   1.00 12.85 ?  94  HIS   B H    1 
ATOM   5398 H HA   . HIS   B 1 94  ? 44.882 -17.031 0.807   1.00 13.22 ?  94  HIS   B HA   1 
ATOM   5399 H HB2  . HIS   B 1 94  ? 44.904 -14.720 2.442   1.00 13.99 ?  94  HIS   B HB2  1 
ATOM   5400 H HB3  . HIS   B 1 94  ? 45.385 -16.149 2.939   1.00 13.99 ?  94  HIS   B HB3  1 
ATOM   5401 H HD2  . HIS   B 1 94  ? 46.759 -13.355 0.942   1.00 15.31 ?  94  HIS   B HD2  1 
ATOM   5402 H HE1  . HIS   B 1 94  ? 49.649 -16.034 1.246   1.00 15.02 ?  94  HIS   B HE1  1 
ATOM   5403 H HE2  . HIS   B 1 94  ? 49.097 -13.849 0.533   1.00 15.89 ?  94  HIS   B HE2  1 
ATOM   5404 N N    . VAL   B 1 95  ? 42.655 -17.827 1.567   1.00 11.73 ?  95  VAL   B N    1 
ATOM   5405 C CA   . VAL   B 1 95  ? 41.323 -18.256 1.999   1.00 11.83 ?  95  VAL   B CA   1 
ATOM   5406 C C    . VAL   B 1 95  ? 41.485 -19.280 3.107   1.00 11.87 ?  95  VAL   B C    1 
ATOM   5407 O O    . VAL   B 1 95  ? 42.255 -20.233 2.959   1.00 13.19 ?  95  VAL   B O    1 
ATOM   5408 C CB   . VAL   B 1 95  ? 40.520 -18.872 0.839   1.00 12.12 ?  95  VAL   B CB   1 
ATOM   5409 C CG1  . VAL   B 1 95  ? 39.149 -19.340 1.316   1.00 14.26 ?  95  VAL   B CG1  1 
ATOM   5410 C CG2  . VAL   B 1 95  ? 40.391 -17.890 -0.304  1.00 12.60 ?  95  VAL   B CG2  1 
ATOM   5411 H H    . VAL   B 1 95  ? 43.125 -18.462 1.213   1.00 14.09 ?  95  VAL   B H    1 
ATOM   5412 H HA   . VAL   B 1 95  ? 40.835 -17.497 2.347   1.00 14.20 ?  95  VAL   B HA   1 
ATOM   5413 H HB   . VAL   B 1 95  ? 40.993 -19.645 0.504   1.00 14.55 ?  95  VAL   B HB   1 
ATOM   5414 H HG11 . VAL   B 1 95  ? 38.595 -19.534 0.540   1.00 17.12 ?  95  VAL   B HG11 1 
ATOM   5415 H HG12 . VAL   B 1 95  ? 39.255 -20.142 1.850   1.00 17.12 ?  95  VAL   B HG12 1 
ATOM   5416 H HG13 . VAL   B 1 95  ? 38.738 -18.639 1.843   1.00 17.12 ?  95  VAL   B HG13 1 
ATOM   5417 H HG21 . VAL   B 1 95  ? 39.812 -18.270 -0.984  1.00 15.13 ?  95  VAL   B HG21 1 
ATOM   5418 H HG22 . VAL   B 1 95  ? 40.001 -17.064 0.033   1.00 15.13 ?  95  VAL   B HG22 1 
ATOM   5419 H HG23 . VAL   B 1 95  ? 41.268 -17.715 -0.670  1.00 15.13 ?  95  VAL   B HG23 1 
ATOM   5420 N N    . VAL   B 1 96  ? 40.753 -19.104 4.202   1.00 12.64 ?  96  VAL   B N    1 
ATOM   5421 C CA   . VAL   B 1 96  ? 40.843 -20.005 5.347   1.00 12.95 ?  96  VAL   B CA   1 
ATOM   5422 C C    . VAL   B 1 96  ? 39.662 -20.969 5.302   1.00 13.54 ?  96  VAL   B C    1 
ATOM   5423 O O    . VAL   B 1 96  ? 38.541 -20.620 5.690   1.00 14.73 ?  96  VAL   B O    1 
ATOM   5424 C CB   . VAL   B 1 96  ? 40.877 -19.252 6.677   1.00 13.81 ?  96  VAL   B CB   1 
ATOM   5425 C CG1  . VAL   B 1 96  ? 41.064 -20.252 7.813   1.00 14.08 ?  96  VAL   B CG1  1 
ATOM   5426 C CG2  . VAL   B 1 96  ? 41.986 -18.209 6.693   1.00 14.19 ?  96  VAL   B CG2  1 
ATOM   5427 H H    . VAL   B 1 96  ? 40.197 -18.459 4.307   1.00 15.17 ?  96  VAL   B H    1 
ATOM   5428 H HA   . VAL   B 1 96  ? 41.663 -20.527 5.278   1.00 15.55 ?  96  VAL   B HA   1 
ATOM   5429 H HB   . VAL   B 1 96  ? 40.030 -18.803 6.808   1.00 16.58 ?  96  VAL   B HB   1 
ATOM   5430 H HG11 . VAL   B 1 96  ? 41.259 -19.772 8.632   1.00 16.91 ?  96  VAL   B HG11 1 
ATOM   5431 H HG12 . VAL   B 1 96  ? 40.245 -20.768 7.926   1.00 16.91 ?  96  VAL   B HG12 1 
ATOM   5432 H HG13 . VAL   B 1 96  ? 41.799 -20.850 7.599   1.00 16.91 ?  96  VAL   B HG13 1 
ATOM   5433 H HG21 . VAL   B 1 96  ? 42.012 -17.791 7.573   1.00 17.04 ?  96  VAL   B HG21 1 
ATOM   5434 H HG22 . VAL   B 1 96  ? 42.832 -18.635 6.506   1.00 17.04 ?  96  VAL   B HG22 1 
ATOM   5435 H HG23 . VAL   B 1 96  ? 41.795 -17.534 6.021   1.00 17.04 ?  96  VAL   B HG23 1 
ATOM   5436 N N    . GLY   B 1 97  ? 39.901 -22.198 4.849   1.00 13.43 ?  97  GLY   B N    1 
ATOM   5437 C CA   . GLY   B 1 97  ? 38.937 -23.257 5.014   1.00 14.75 ?  97  GLY   B CA   1 
ATOM   5438 C C    . GLY   B 1 97  ? 39.078 -23.860 6.395   1.00 16.11 ?  97  GLY   B C    1 
ATOM   5439 O O    . GLY   B 1 97  ? 40.120 -23.722 7.046   1.00 16.67 ?  97  GLY   B O    1 
ATOM   5440 H H    . GLY   B 1 97  ? 40.625 -22.430 4.430   1.00 16.13 ?  97  GLY   B H    1 
ATOM   5441 H HA2  . GLY   B 1 97  ? 38.043 -22.897 4.905   1.00 17.71 ?  97  GLY   B HA2  1 
ATOM   5442 H HA3  . GLY   B 1 97  ? 39.083 -23.942 4.340   1.00 17.71 ?  97  GLY   B HA3  1 
ATOM   5443 N N    . PRO   B 1 98  ? 38.037 -24.539 6.873   1.00 16.62 ?  98  PRO   B N    1 
ATOM   5444 C CA   . PRO   B 1 98  ? 38.140 -25.218 8.167   1.00 18.50 ?  98  PRO   B CA   1 
ATOM   5445 C C    . PRO   B 1 98  ? 39.168 -26.343 8.130   1.00 17.68 ?  98  PRO   B C    1 
ATOM   5446 O O    . PRO   B 1 98  ? 39.269 -27.088 7.156   1.00 18.17 ?  98  PRO   B O    1 
ATOM   5447 C CB   . PRO   B 1 98  ? 36.720 -25.752 8.396   1.00 19.30 ?  98  PRO   B CB   1 
ATOM   5448 C CG   . PRO   B 1 98  ? 36.137 -25.890 7.041   1.00 18.82 ?  98  PRO   B CG   1 
ATOM   5449 C CD   . PRO   B 1 98  ? 36.716 -24.742 6.249   1.00 17.51 ?  98  PRO   B CD   1 
ATOM   5450 H HA   . PRO   B 1 98  ? 38.371 -24.587 8.863   1.00 22.21 ?  98  PRO   B HA   1 
ATOM   5451 H HB2  . PRO   B 1 98  ? 36.763 -26.616 8.841   1.00 23.17 ?  98  PRO   B HB2  1 
ATOM   5452 H HB3  . PRO   B 1 98  ? 36.213 -25.119 8.924   1.00 23.17 ?  98  PRO   B HB3  1 
ATOM   5453 H HG2  . PRO   B 1 98  ? 36.401 -26.745 6.658   1.00 22.59 ?  98  PRO   B HG2  1 
ATOM   5454 H HG3  . PRO   B 1 98  ? 35.172 -25.823 7.091   1.00 22.59 ?  98  PRO   B HG3  1 
ATOM   5455 H HD2  . PRO   B 1 98  ? 36.814 -24.992 5.310   1.00 21.01 ?  98  PRO   B HD2  1 
ATOM   5456 H HD3  . PRO   B 1 98  ? 36.175 -23.948 6.348   1.00 21.01 ?  98  PRO   B HD3  1 
ATOM   5457 N N    . ASN   B 1 99  ? 39.938 -26.453 9.210   1.00 19.48 ?  99  ASN   B N    1 
ATOM   5458 C CA   . ASN   B 1 99  ? 40.917 -27.525 9.387   1.00 20.81 ?  99  ASN   B CA   1 
ATOM   5459 C C    . ASN   B 1 99  ? 40.291 -28.583 10.291  1.00 23.72 ?  99  ASN   B C    1 
ATOM   5460 O O    . ASN   B 1 99  ? 40.253 -28.422 11.514  1.00 25.29 ?  99  ASN   B O    1 
ATOM   5461 C CB   . ASN   B 1 99  ? 42.200 -26.962 9.989   1.00 21.44 ?  99  ASN   B CB   1 
ATOM   5462 C CG   . ASN   B 1 99  ? 43.322 -27.977 10.027  1.00 22.26 ?  99  ASN   B CG   1 
ATOM   5463 O OD1  . ASN   B 1 99  ? 43.092 -29.152 10.264  1.00 22.81 ?  99  ASN   B OD1  1 
ATOM   5464 N ND2  . ASN   B 1 99  ? 44.540 -27.525 9.793   1.00 22.49 ?  99  ASN   B ND2  1 
ATOM   5465 H H    . ASN   B 1 99  ? 39.905 -25.902 9.868   1.00 23.38 ?  99  ASN   B H    1 
ATOM   5466 H HA   . ASN   B 1 99  ? 41.114 -27.930 8.529   1.00 24.99 ?  99  ASN   B HA   1 
ATOM   5467 H HB2  . ASN   B 1 99  ? 42.486 -26.208 9.459   1.00 25.74 ?  99  ASN   B HB2  1 
ATOM   5468 H HB3  . ASN   B 1 99  ? 42.015 -26.683 10.901  1.00 25.74 ?  99  ASN   B HB3  1 
ATOM   5469 H HD21 . ASN   B 1 99  ? 45.207 -28.062 9.798   1.00 26.99 ?  99  ASN   B HD21 1 
ATOM   5470 H HD22 . ASN   B 1 99  ? 44.655 -26.688 9.634   1.00 26.99 ?  99  ASN   B HD22 1 
ATOM   5471 N N    . VAL   B 1 100 ? 39.777 -29.655 9.677   1.00 26.29 ?  100 VAL   B N    1 
ATOM   5472 C CA   . VAL   B 1 100 ? 39.151 -30.737 10.436  1.00 29.95 ?  100 VAL   B CA   1 
ATOM   5473 C C    . VAL   B 1 100 ? 40.159 -31.414 11.356  1.00 31.10 ?  100 VAL   B C    1 
ATOM   5474 O O    . VAL   B 1 100 ? 39.796 -31.897 12.433  1.00 32.20 ?  100 VAL   B O    1 
ATOM   5475 C CB   . VAL   B 1 100 ? 38.457 -31.730 9.478   1.00 32.22 ?  100 VAL   B CB   1 
ATOM   5476 C CG1  . VAL   B 1 100 ? 37.979 -32.965 10.227  1.00 33.23 ?  100 VAL   B CG1  1 
ATOM   5477 C CG2  . VAL   B 1 100 ? 37.283 -31.055 8.781   1.00 32.94 ?  100 VAL   B CG2  1 
ATOM   5478 H H    . VAL   B 1 100 ? 39.765 -29.769 8.819   1.00 31.55 ?  100 VAL   B H    1 
ATOM   5479 H HA   . VAL   B 1 100 ? 38.454 -30.359 10.993  1.00 35.95 ?  100 VAL   B HA   1 
ATOM   5480 H HB   . VAL   B 1 100 ? 39.085 -32.018 8.796   1.00 38.67 ?  100 VAL   B HB   1 
ATOM   5481 H HG11 . VAL   B 1 100 ? 37.354 -33.456 9.666   1.00 39.89 ?  100 VAL   B HG11 1 
ATOM   5482 H HG12 . VAL   B 1 100 ? 38.741 -33.527 10.436  1.00 39.89 ?  100 VAL   B HG12 1 
ATOM   5483 H HG13 . VAL   B 1 100 ? 37.535 -32.687 11.044  1.00 39.89 ?  100 VAL   B HG13 1 
ATOM   5484 H HG21 . VAL   B 1 100 ? 36.850 -31.696 8.193   1.00 39.53 ?  100 VAL   B HG21 1 
ATOM   5485 H HG22 . VAL   B 1 100 ? 36.653 -30.747 9.452   1.00 39.53 ?  100 VAL   B HG22 1 
ATOM   5486 H HG23 . VAL   B 1 100 ? 37.611 -30.304 8.266   1.00 39.53 ?  100 VAL   B HG23 1 
ATOM   5487 N N    . ASN   B 1 101 ? 41.434 -31.464 10.956  1.00 31.83 ?  101 ASN   B N    1 
ATOM   5488 C CA   . ASN   B 1 101 ? 42.467 -32.008 11.837  1.00 33.31 ?  101 ASN   B CA   1 
ATOM   5489 C C    . ASN   B 1 101 ? 42.650 -31.167 13.095  1.00 37.03 ?  101 ASN   B C    1 
ATOM   5490 O O    . ASN   B 1 101 ? 43.263 -31.640 14.060  1.00 37.89 ?  101 ASN   B O    1 
ATOM   5491 C CB   . ASN   B 1 101 ? 43.789 -32.170 11.080  1.00 32.45 ?  101 ASN   B CB   1 
ATOM   5492 C CG   . ASN   B 1 101 ? 43.768 -33.347 10.119  1.00 31.40 ?  101 ASN   B CG   1 
ATOM   5493 O OD1  . ASN   B 1 101 ? 43.079 -34.334 10.356  1.00 31.71 ?  101 ASN   B OD1  1 
ATOM   5494 N ND2  . ASN   B 1 101 ? 44.518 -33.245 9.030   1.00 30.95 ?  101 ASN   B ND2  1 
ATOM   5495 H H    . ASN   B 1 101 ? 41.714 -31.207 10.186  1.00 38.20 ?  101 ASN   B H    1 
ATOM   5496 H HA   . ASN   B 1 101 ? 42.188 -32.889 12.120  1.00 39.98 ?  101 ASN   B HA   1 
ATOM   5497 H HB2  . ASN   B 1 101 ? 43.966 -31.370 10.564  1.00 38.94 ?  101 ASN   B HB2  1 
ATOM   5498 H HB3  . ASN   B 1 101 ? 44.502 -32.317 11.721  1.00 38.94 ?  101 ASN   B HB3  1 
ATOM   5499 H HD21 . ASN   B 1 101 ? 44.536 -33.892 8.462   1.00 37.15 ?  101 ASN   B HD21 1 
ATOM   5500 H HD22 . ASN   B 1 101 ? 44.987 -32.541 8.895   1.00 37.15 ?  101 ASN   B HD22 1 
ATOM   5501 N N    A LYS   B 1 102 ? 42.141 -29.933 13.101  0.48 39.16 ?  102 LYS   B N    1 
ATOM   5502 N N    B LYS   B 1 102 ? 42.146 -29.933 13.103  0.52 39.10 ?  102 LYS   B N    1 
ATOM   5503 C CA   A LYS   B 1 102 ? 42.082 -29.100 14.295  0.48 41.10 ?  102 LYS   B CA   1 
ATOM   5504 C CA   B LYS   B 1 102 ? 42.087 -29.113 14.304  0.52 41.00 ?  102 LYS   B CA   1 
ATOM   5505 C C    A LYS   B 1 102 ? 40.694 -29.084 14.924  0.48 40.55 ?  102 LYS   B C    1 
ATOM   5506 C C    B LYS   B 1 102 ? 40.682 -29.054 14.894  0.52 40.39 ?  102 LYS   B C    1 
ATOM   5507 O O    A LYS   B 1 102 ? 40.451 -28.298 15.845  0.48 40.88 ?  102 LYS   B O    1 
ATOM   5508 O O    B LYS   B 1 102 ? 40.417 -28.210 15.755  0.52 40.57 ?  102 LYS   B O    1 
ATOM   5509 C CB   A LYS   B 1 102 ? 42.501 -27.664 13.971  0.48 43.57 ?  102 LYS   B CB   1 
ATOM   5510 C CB   B LYS   B 1 102 ? 42.583 -27.696 14.012  0.52 43.51 ?  102 LYS   B CB   1 
ATOM   5511 C CG   A LYS   B 1 102 ? 43.955 -27.479 13.574  0.48 45.70 ?  102 LYS   B CG   1 
ATOM   5512 C CG   B LYS   B 1 102 ? 44.059 -27.598 13.666  0.52 45.70 ?  102 LYS   B CG   1 
ATOM   5513 C CD   A LYS   B 1 102 ? 44.206 -26.028 13.194  0.48 47.63 ?  102 LYS   B CD   1 
ATOM   5514 C CD   B LYS   B 1 102 ? 44.407 -26.188 13.218  0.52 47.77 ?  102 LYS   B CD   1 
ATOM   5515 C CE   A LYS   B 1 102 ? 45.665 -25.757 12.880  0.48 48.91 ?  102 LYS   B CE   1 
ATOM   5516 C CE   B LYS   B 1 102 ? 45.903 -26.004 13.038  0.52 49.17 ?  102 LYS   B CE   1 
ATOM   5517 N NZ   A LYS   B 1 102 ? 45.873 -24.330 12.497  0.48 49.60 ?  102 LYS   B NZ   1 
ATOM   5518 N NZ   B LYS   B 1 102 ? 46.227 -24.614 12.607  0.52 50.02 ?  102 LYS   B NZ   1 
ATOM   5519 H H    A LYS   B 1 102 ? 41.816 -29.547 12.404  0.48 47.00 ?  102 LYS   B H    1 
ATOM   5520 H H    B LYS   B 1 102 ? 41.826 -29.541 12.406  0.52 46.92 ?  102 LYS   B H    1 
ATOM   5521 H HA   A LYS   B 1 102 ? 42.703 -29.449 14.952  0.48 49.33 ?  102 LYS   B HA   1 
ATOM   5522 H HA   B LYS   B 1 102 ? 42.677 -29.498 14.971  0.52 49.20 ?  102 LYS   B HA   1 
ATOM   5523 H HB2  A LYS   B 1 102 ? 41.957 -27.343 13.237  0.48 52.29 ?  102 LYS   B HB2  1 
ATOM   5524 H HB2  B LYS   B 1 102 ? 42.083 -27.340 13.263  0.52 52.22 ?  102 LYS   B HB2  1 
ATOM   5525 H HB3  A LYS   B 1 102 ? 42.344 -27.114 14.755  0.48 52.29 ?  102 LYS   B HB3  1 
ATOM   5526 H HB3  B LYS   B 1 102 ? 42.432 -27.147 14.798  0.52 52.22 ?  102 LYS   B HB3  1 
ATOM   5527 H HG2  A LYS   B 1 102 ? 44.530 -27.706 14.322  0.48 54.84 ?  102 LYS   B HG2  1 
ATOM   5528 H HG2  B LYS   B 1 102 ? 44.591 -27.811 14.449  0.52 54.84 ?  102 LYS   B HG2  1 
ATOM   5529 H HG3  A LYS   B 1 102 ? 44.157 -28.038 12.808  0.48 54.84 ?  102 LYS   B HG3  1 
ATOM   5530 H HG3  B LYS   B 1 102 ? 44.263 -28.210 12.941  0.52 54.84 ?  102 LYS   B HG3  1 
ATOM   5531 H HD2  A LYS   B 1 102 ? 43.683 -25.810 12.406  0.48 57.16 ?  102 LYS   B HD2  1 
ATOM   5532 H HD2  B LYS   B 1 102 ? 43.976 -26.008 12.367  0.52 57.33 ?  102 LYS   B HD2  1 
ATOM   5533 H HD3  A LYS   B 1 102 ? 43.946 -25.456 13.934  0.48 57.16 ?  102 LYS   B HD3  1 
ATOM   5534 H HD3  B LYS   B 1 102 ? 44.102 -25.555 13.887  0.52 57.33 ?  102 LYS   B HD3  1 
ATOM   5535 H HE2  A LYS   B 1 102 ? 46.204 -25.944 13.665  0.48 58.70 ?  102 LYS   B HE2  1 
ATOM   5536 H HE2  B LYS   B 1 102 ? 46.351 -26.174 13.882  0.52 59.01 ?  102 LYS   B HE2  1 
ATOM   5537 H HE3  A LYS   B 1 102 ? 45.945 -26.316 12.138  0.48 58.70 ?  102 LYS   B HE3  1 
ATOM   5538 H HE3  B LYS   B 1 102 ? 46.223 -26.617 12.357  0.52 59.01 ?  102 LYS   B HE3  1 
ATOM   5539 H HZ1  A LYS   B 1 102 ? 46.731 -24.185 12.316  0.48 59.53 ?  102 LYS   B HZ1  1 
ATOM   5540 H HZ1  B LYS   B 1 102 ? 47.106 -24.524 12.507  0.52 60.03 ?  102 LYS   B HZ1  1 
ATOM   5541 H HZ2  A LYS   B 1 102 ? 45.387 -24.136 11.776  0.48 59.53 ?  102 LYS   B HZ2  1 
ATOM   5542 H HZ2  B LYS   B 1 102 ? 45.827 -24.436 11.832  0.52 60.03 ?  102 LYS   B HZ2  1 
ATOM   5543 H HZ3  A LYS   B 1 102 ? 45.623 -23.797 13.165  0.48 59.53 ?  102 LYS   B HZ3  1 
ATOM   5544 H HZ3  B LYS   B 1 102 ? 45.943 -24.033 13.219  0.52 60.03 ?  102 LYS   B HZ3  1 
ATOM   5545 N N    . GLY   B 1 103 ? 39.775 -29.917 14.440  1.00 40.01 ?  103 GLY   B N    1 
ATOM   5546 C CA   . GLY   B 1 103 ? 38.435 -29.973 14.989  1.00 39.47 ?  103 GLY   B CA   1 
ATOM   5547 C C    . GLY   B 1 103 ? 37.494 -28.884 14.529  1.00 38.76 ?  103 GLY   B C    1 
ATOM   5548 O O    . GLY   B 1 103 ? 36.389 -28.775 15.072  1.00 38.80 ?  103 GLY   B O    1 
ATOM   5549 H H    A GLY   B 1 103 ? 39.909 -30.464 13.791  0.48 48.02 ?  103 GLY   B H    1 
ATOM   5550 H H    B GLY   B 1 103 ? 39.915 -30.481 13.806  0.52 48.02 ?  103 GLY   B H    1 
ATOM   5551 H HA2  . GLY   B 1 103 ? 38.039 -30.828 14.759  1.00 47.37 ?  103 GLY   B HA2  1 
ATOM   5552 H HA3  . GLY   B 1 103 ? 38.491 -29.922 15.956  1.00 47.37 ?  103 GLY   B HA3  1 
ATOM   5553 N N    A GLU   B 1 104 ? 37.887 -28.078 13.546  0.48 38.28 ?  104 GLU   B N    1 
ATOM   5554 N N    B GLU   B 1 104 ? 37.889 -28.075 13.549  0.52 38.19 ?  104 GLU   B N    1 
ATOM   5555 C CA   A GLU   B 1 104 ? 37.040 -26.987 13.090  0.48 37.67 ?  104 GLU   B CA   1 
ATOM   5556 C CA   B GLU   B 1 104 ? 37.045 -26.985 13.085  0.52 37.50 ?  104 GLU   B CA   1 
ATOM   5557 C C    A GLU   B 1 104 ? 35.863 -27.520 12.274  0.48 37.65 ?  104 GLU   B C    1 
ATOM   5558 C C    B GLU   B 1 104 ? 35.866 -27.518 12.271  0.52 37.57 ?  104 GLU   B C    1 
ATOM   5559 O O    A GLU   B 1 104 ? 35.911 -28.608 11.692  0.48 37.88 ?  104 GLU   B O    1 
ATOM   5560 O O    B GLU   B 1 104 ? 35.915 -28.605 11.686  0.52 37.80 ?  104 GLU   B O    1 
ATOM   5561 C CB   A GLU   B 1 104 ? 37.861 -25.982 12.281  0.48 37.21 ?  104 GLU   B CB   1 
ATOM   5562 C CB   B GLU   B 1 104 ? 37.874 -25.991 12.270  0.52 36.90 ?  104 GLU   B CB   1 
ATOM   5563 C CG   A GLU   B 1 104 ? 38.954 -25.320 13.109  0.48 36.65 ?  104 GLU   B CG   1 
ATOM   5564 C CG   B GLU   B 1 104 ? 38.985 -25.351 13.094  0.52 36.18 ?  104 GLU   B CG   1 
ATOM   5565 C CD   A GLU   B 1 104 ? 39.881 -24.439 12.296  0.48 36.03 ?  104 GLU   B CD   1 
ATOM   5566 C CD   B GLU   B 1 104 ? 39.918 -24.476 12.281  0.52 35.40 ?  104 GLU   B CD   1 
ATOM   5567 O OE1  A GLU   B 1 104 ? 39.863 -24.524 11.050  0.48 34.98 ?  104 GLU   B OE1  1 
ATOM   5568 O OE1  B GLU   B 1 104 ? 39.882 -24.539 11.034  0.52 34.18 ?  104 GLU   B OE1  1 
ATOM   5569 O OE2  A GLU   B 1 104 ? 40.637 -23.660 12.912  0.48 35.90 -1 104 GLU   B OE2  1 
ATOM   5570 O OE2  B GLU   B 1 104 ? 40.698 -23.724 12.899  0.52 35.22 -1 104 GLU   B OE2  1 
ATOM   5571 H H    A GLU   B 1 104 ? 38.638 -28.139 13.134  0.48 45.94 ?  104 GLU   B H    1 
ATOM   5572 H H    B GLU   B 1 104 ? 38.646 -28.132 13.146  0.52 45.83 ?  104 GLU   B H    1 
ATOM   5573 H HA   A GLU   B 1 104 ? 36.682 -26.525 13.862  0.48 45.21 ?  104 GLU   B HA   1 
ATOM   5574 H HA   B GLU   B 1 104 ? 36.690 -26.513 13.854  0.52 45.00 ?  104 GLU   B HA   1 
ATOM   5575 H HB2  A GLU   B 1 104 ? 38.281 -26.440 11.537  0.48 44.66 ?  104 GLU   B HB2  1 
ATOM   5576 H HB2  B GLU   B 1 104 ? 38.282 -26.454 11.522  0.52 44.29 ?  104 GLU   B HB2  1 
ATOM   5577 H HB3  A GLU   B 1 104 ? 37.270 -25.285 11.949  0.48 44.66 ?  104 GLU   B HB3  1 
ATOM   5578 H HB3  B GLU   B 1 104 ? 37.294 -25.283 11.945  0.52 44.29 ?  104 GLU   B HB3  1 
ATOM   5579 H HG2  A GLU   B 1 104 ? 38.541 -24.770 13.795  0.48 43.99 ?  104 GLU   B HG2  1 
ATOM   5580 H HG2  B GLU   B 1 104 ? 38.586 -24.802 13.787  0.52 43.42 ?  104 GLU   B HG2  1 
ATOM   5581 H HG3  A GLU   B 1 104 ? 39.497 -26.008 13.522  0.48 43.99 ?  104 GLU   B HG3  1 
ATOM   5582 H HG3  B GLU   B 1 104 ? 39.521 -26.051 13.498  0.52 43.42 ?  104 GLU   B HG3  1 
ATOM   5583 N N    . ASP   B 1 105 ? 34.794 -26.727 12.238  1.00 37.01 ?  105 ASP   B N    1 
ATOM   5584 C CA   . ASP   B 1 105 ? 33.531 -27.172 11.660  1.00 37.61 ?  105 ASP   B CA   1 
ATOM   5585 C C    . ASP   B 1 105 ? 33.616 -27.224 10.140  1.00 34.80 ?  105 ASP   B C    1 
ATOM   5586 O O    . ASP   B 1 105 ? 33.825 -26.198 9.487   1.00 33.67 ?  105 ASP   B O    1 
ATOM   5587 C CB   . ASP   B 1 105 ? 32.411 -26.223 12.086  1.00 40.59 ?  105 ASP   B CB   1 
ATOM   5588 C CG   . ASP   B 1 105 ? 31.046 -26.680 11.611  1.00 43.38 ?  105 ASP   B CG   1 
ATOM   5589 O OD1  . ASP   B 1 105 ? 30.939 -27.812 11.092  1.00 43.40 ?  105 ASP   B OD1  1 
ATOM   5590 O OD2  . ASP   B 1 105 ? 30.077 -25.902 11.749  1.00 45.06 -1 105 ASP   B OD2  1 
ATOM   5591 H H    A ASP   B 1 105 ? 34.775 -25.921 12.538  0.48 44.42 ?  105 ASP   B H    1 
ATOM   5592 H H    B ASP   B 1 105 ? 34.772 -25.923 12.542  0.52 44.42 ?  105 ASP   B H    1 
ATOM   5593 H HA   . ASP   B 1 105 ? 33.317 -28.059 11.984  1.00 45.14 ?  105 ASP   B HA   1 
ATOM   5594 H HB2  . ASP   B 1 105 ? 32.405 -26.155 13.056  1.00 48.72 ?  105 ASP   B HB2  1 
ATOM   5595 H HB3  . ASP   B 1 105 ? 32.565 -25.349 11.695  1.00 48.72 ?  105 ASP   B HB3  1 
ATOM   5596 N N    A ILE   B 1 106 ? 33.440 -28.424 9.579   0.48 34.30 ?  106 ILE   B N    1 
ATOM   5597 N N    B ILE   B 1 106 ? 33.421 -28.420 9.578   0.52 34.25 ?  106 ILE   B N    1 
ATOM   5598 C CA   A ILE   B 1 106 ? 33.421 -28.598 8.131   0.48 33.51 ?  106 ILE   B CA   1 
ATOM   5599 C CA   B ILE   B 1 106 ? 33.424 -28.587 8.131   0.52 33.38 ?  106 ILE   B CA   1 
ATOM   5600 C C    A ILE   B 1 106 ? 32.342 -27.747 7.474   0.48 32.39 ?  106 ILE   B C    1 
ATOM   5601 C C    B ILE   B 1 106 ? 32.339 -27.749 7.472   0.52 32.23 ?  106 ILE   B C    1 
ATOM   5602 O O    A ILE   B 1 106 ? 32.436 -27.442 6.280   0.48 31.67 ?  106 ILE   B O    1 
ATOM   5603 O O    B ILE   B 1 106 ? 32.426 -27.453 6.275   0.52 31.38 ?  106 ILE   B O    1 
ATOM   5604 C CB   A ILE   B 1 106 ? 33.261 -30.099 7.790   0.48 34.08 ?  106 ILE   B CB   1 
ATOM   5605 C CB   B ILE   B 1 106 ? 33.295 -30.087 7.777   0.52 33.98 ?  106 ILE   B CB   1 
ATOM   5606 C CG1  A ILE   B 1 106 ? 33.493 -30.356 6.299   0.48 34.16 ?  106 ILE   B CG1  1 
ATOM   5607 C CG1  B ILE   B 1 106 ? 33.610 -30.332 6.299   0.52 34.13 ?  106 ILE   B CG1  1 
ATOM   5608 C CG2  A ILE   B 1 106 ? 31.885 -30.601 8.208   0.48 34.62 ?  106 ILE   B CG2  1 
ATOM   5609 C CG2  B ILE   B 1 106 ? 31.899 -30.599 8.105   0.52 34.52 ?  106 ILE   B CG2  1 
ATOM   5610 C CD1  A ILE   B 1 106 ? 34.865 -29.953 5.821   0.48 34.15 ?  106 ILE   B CD1  1 
ATOM   5611 C CD1  B ILE   B 1 106 ? 34.990 -29.879 5.889   0.52 34.17 ?  106 ILE   B CD1  1 
ATOM   5612 H H    A ILE   B 1 106 ? 33.338 -29.154 10.018  0.48 41.17 ?  106 ILE   B H    1 
ATOM   5613 H H    B ILE   B 1 106 ? 33.284 -29.146 10.015  0.52 41.11 ?  106 ILE   B H    1 
ATOM   5614 H HA   A ILE   B 1 106 ? 34.271 -28.305 7.777   0.48 40.21 ?  106 ILE   B HA   1 
ATOM   5615 H HA   B ILE   B 1 106 ? 34.271 -28.272 7.794   0.52 40.07 ?  106 ILE   B HA   1 
ATOM   5616 H HB   A ILE   B 1 106 ? 33.926 -30.597 8.288   0.48 40.91 ?  106 ILE   B HB   1 
ATOM   5617 H HB   B ILE   B 1 106 ? 33.933 -30.583 8.312   0.52 40.78 ?  106 ILE   B HB   1 
ATOM   5618 H HG12 A ILE   B 1 106 ? 33.390 -31.307 6.125   0.48 41.00 ?  106 ILE   B HG12 1 
ATOM   5619 H HG12 B ILE   B 1 106 ? 33.547 -31.285 6.120   0.52 40.97 ?  106 ILE   B HG12 1 
ATOM   5620 H HG13 A ILE   B 1 106 ? 32.841 -29.858 5.785   0.48 41.00 ?  106 ILE   B HG13 1 
ATOM   5621 H HG13 B ILE   B 1 106 ? 32.965 -29.855 5.756   0.52 40.97 ?  106 ILE   B HG13 1 
ATOM   5622 H HG21 A ILE   B 1 106 ? 31.866 -31.568 8.134   0.48 41.55 ?  106 ILE   B HG21 1 
ATOM   5623 H HG21 B ILE   B 1 106 ? 31.902 -31.568 8.067   0.52 41.43 ?  106 ILE   B HG21 1 
ATOM   5624 H HG22 A ILE   B 1 106 ? 31.720 -30.337 9.127   0.48 41.55 ?  106 ILE   B HG22 1 
ATOM   5625 H HG22 B ILE   B 1 106 ? 31.657 -30.304 8.997   0.52 41.43 ?  106 ILE   B HG22 1 
ATOM   5626 H HG23 A ILE   B 1 106 ? 31.214 -30.212 7.626   0.48 41.55 ?  106 ILE   B HG23 1 
ATOM   5627 H HG23 B ILE   B 1 106 ? 31.270 -30.245 7.457   0.52 41.43 ?  106 ILE   B HG23 1 
ATOM   5628 H HD11 A ILE   B 1 106 ? 35.030 -30.363 4.958   0.48 40.99 ?  106 ILE   B HD11 1 
ATOM   5629 H HD11 B ILE   B 1 106 ? 35.224 -30.306 5.051   0.52 41.01 ?  106 ILE   B HD11 1 
ATOM   5630 H HD12 A ILE   B 1 106 ? 34.900 -28.987 5.741   0.48 40.99 ?  106 ILE   B HD12 1 
ATOM   5631 H HD12 B ILE   B 1 106 ? 34.986 -28.915 5.780   0.52 41.01 ?  106 ILE   B HD12 1 
ATOM   5632 H HD13 A ILE   B 1 106 ? 35.524 -30.258 6.464   0.48 40.99 ?  106 ILE   B HD13 1 
ATOM   5633 H HD13 B ILE   B 1 106 ? 35.623 -30.134 6.578   0.52 41.01 ?  106 ILE   B HD13 1 
ATOM   5634 N N    . GLN   B 1 107 ? 31.317 -27.343 8.229   1.00 32.53 ?  107 GLN   B N    1 
ATOM   5635 C CA   . GLN   B 1 107 ? 30.238 -26.546 7.658   1.00 32.72 ?  107 GLN   B CA   1 
ATOM   5636 C C    . GLN   B 1 107 ? 30.725 -25.195 7.148   1.00 28.84 ?  107 GLN   B C    1 
ATOM   5637 O O    . GLN   B 1 107 ? 30.091 -24.622 6.258   1.00 29.20 ?  107 GLN   B O    1 
ATOM   5638 C CB   . GLN   B 1 107 ? 29.129 -26.359 8.698   1.00 38.42 ?  107 GLN   B CB   1 
ATOM   5639 C CG   . GLN   B 1 107 ? 27.791 -25.891 8.132   1.00 43.99 ?  107 GLN   B CG   1 
ATOM   5640 C CD   . GLN   B 1 107 ? 27.683 -24.379 8.035   1.00 48.25 ?  107 GLN   B CD   1 
ATOM   5641 O OE1  . GLN   B 1 107 ? 28.515 -23.649 8.575   1.00 49.71 ?  107 GLN   B OE1  1 
ATOM   5642 N NE2  . GLN   B 1 107 ? 26.650 -23.903 7.348   1.00 49.70 ?  107 GLN   B NE2  1 
ATOM   5643 H H    A GLN   B 1 107 ? 31.228 -27.510 9.066   0.48 39.04 ?  107 GLN   B H    1 
ATOM   5644 H H    B GLN   B 1 107 ? 31.229 -27.508 9.066   0.52 39.04 ?  107 GLN   B H    1 
ATOM   5645 H HA   . GLN   B 1 107 ? 29.857 -27.027 6.906   1.00 39.28 ?  107 GLN   B HA   1 
ATOM   5646 H HB2  . GLN   B 1 107 ? 28.976 -27.207 9.138   1.00 46.11 ?  107 GLN   B HB2  1 
ATOM   5647 H HB3  . GLN   B 1 107 ? 29.420 -25.702 9.348   1.00 46.11 ?  107 GLN   B HB3  1 
ATOM   5648 H HG2  . GLN   B 1 107 ? 27.677 -26.255 7.240   1.00 52.80 ?  107 GLN   B HG2  1 
ATOM   5649 H HG3  . GLN   B 1 107 ? 27.076 -26.209 8.710   1.00 52.80 ?  107 GLN   B HG3  1 
ATOM   5650 H HE21 . GLN   B 1 107 ? 26.088 -24.443 6.983   1.00 59.65 ?  107 GLN   B HE21 1 
ATOM   5651 H HE22 . GLN   B 1 107 ? 26.542 -23.053 7.268   1.00 59.65 ?  107 GLN   B HE22 1 
ATOM   5652 N N    . LEU   B 1 108 ? 31.846 -24.683 7.672   1.00 25.55 ?  108 LEU   B N    1 
ATOM   5653 C CA   . LEU   B 1 108 ? 32.388 -23.394 7.245   1.00 21.95 ?  108 LEU   B CA   1 
ATOM   5654 C C    . LEU   B 1 108 ? 33.043 -23.446 5.877   1.00 19.22 ?  108 LEU   B C    1 
ATOM   5655 O O    . LEU   B 1 108 ? 33.486 -22.404 5.375   1.00 17.64 ?  108 LEU   B O    1 
ATOM   5656 C CB   . LEU   B 1 108 ? 33.382 -22.878 8.282   1.00 22.03 ?  108 LEU   B CB   1 
ATOM   5657 C CG   . LEU   B 1 108 ? 32.740 -22.363 9.570   1.00 23.69 ?  108 LEU   B CG   1 
ATOM   5658 C CD1  . LEU   B 1 108 ? 33.742 -22.366 10.706  1.00 24.20 ?  108 LEU   B CD1  1 
ATOM   5659 C CD2  . LEU   B 1 108 ? 32.174 -20.961 9.363   1.00 24.31 ?  108 LEU   B CD2  1 
ATOM   5660 H H    . LEU   B 1 108 ? 32.298 -25.066 8.290   1.00 30.67 ?  108 LEU   B H    1 
ATOM   5661 H HA   . LEU   B 1 108 ? 31.662 -22.756 7.195   1.00 26.35 ?  108 LEU   B HA   1 
ATOM   5662 H HB2  . LEU   B 1 108 ? 33.982 -23.597 8.526   1.00 26.44 ?  108 LEU   B HB2  1 
ATOM   5663 H HB3  . LEU   B 1 108 ? 33.883 -22.145 7.896   1.00 26.44 ?  108 LEU   B HB3  1 
ATOM   5664 H HG   . LEU   B 1 108 ? 32.003 -22.947 9.818   1.00 28.44 ?  108 LEU   B HG   1 
ATOM   5665 H HD11 . LEU   B 1 108 ? 33.304 -22.065 11.518  1.00 29.05 ?  108 LEU   B HD11 1 
ATOM   5666 H HD12 . LEU   B 1 108 ? 34.078 -23.268 10.826  1.00 29.05 ?  108 LEU   B HD12 1 
ATOM   5667 H HD13 . LEU   B 1 108 ? 34.472 -21.767 10.483  1.00 29.05 ?  108 LEU   B HD13 1 
ATOM   5668 H HD21 . LEU   B 1 108 ? 31.787 -20.649 10.196  1.00 29.18 ?  108 LEU   B HD21 1 
ATOM   5669 H HD22 . LEU   B 1 108 ? 32.893 -20.370 9.090   1.00 29.18 ?  108 LEU   B HD22 1 
ATOM   5670 H HD23 . LEU   B 1 108 ? 31.493 -20.994 8.673   1.00 29.18 ?  108 LEU   B HD23 1 
ATOM   5671 N N    . LEU   B 1 109 ? 33.109 -24.625 5.266   1.00 17.94 ?  109 LEU   B N    1 
ATOM   5672 C CA   . LEU   B 1 109 ? 33.736 -24.754 3.959   1.00 17.04 ?  109 LEU   B CA   1 
ATOM   5673 C C    . LEU   B 1 109 ? 32.963 -23.989 2.889   1.00 16.18 ?  109 LEU   B C    1 
ATOM   5674 O O    . LEU   B 1 109 ? 33.572 -23.419 1.974   1.00 15.50 ?  109 LEU   B O    1 
ATOM   5675 C CB   . LEU   B 1 109 ? 33.861 -26.238 3.608   1.00 17.32 ?  109 LEU   B CB   1 
ATOM   5676 C CG   . LEU   B 1 109 ? 34.637 -26.604 2.344   1.00 16.71 ?  109 LEU   B CG   1 
ATOM   5677 C CD1  . LEU   B 1 109 ? 36.014 -25.965 2.346   1.00 16.09 ?  109 LEU   B CD1  1 
ATOM   5678 C CD2  . LEU   B 1 109 ? 34.750 -28.112 2.230   1.00 17.58 ?  109 LEU   B CD2  1 
ATOM   5679 H H    . LEU   B 1 109 ? 32.811 -25.362 5.589   1.00 21.54 ?  109 LEU   B H    1 
ATOM   5680 H HA   . LEU   B 1 109 ? 34.633 -24.381 4.002   1.00 20.45 ?  109 LEU   B HA   1 
ATOM   5681 H HB2  . LEU   B 1 109 ? 34.305 -26.685 4.343   1.00 20.79 ?  109 LEU   B HB2  1 
ATOM   5682 H HB3  . LEU   B 1 109 ? 32.969 -26.597 3.504   1.00 20.79 ?  109 LEU   B HB3  1 
ATOM   5683 H HG   . LEU   B 1 109 ? 34.151 -26.286 1.564   1.00 20.06 ?  109 LEU   B HG   1 
ATOM   5684 H HD11 . LEU   B 1 109 ? 36.537 -26.339 1.618   1.00 19.32 ?  109 LEU   B HD11 1 
ATOM   5685 H HD12 . LEU   B 1 109 ? 35.918 -25.010 2.228   1.00 19.32 ?  109 LEU   B HD12 1 
ATOM   5686 H HD13 . LEU   B 1 109 ? 36.447 -26.157 3.193   1.00 19.32 ?  109 LEU   B HD13 1 
ATOM   5687 H HD21 . LEU   B 1 109 ? 35.303 -28.330 1.463   1.00 21.10 ?  109 LEU   B HD21 1 
ATOM   5688 H HD22 . LEU   B 1 109 ? 35.155 -28.458 3.039   1.00 21.10 ?  109 LEU   B HD22 1 
ATOM   5689 H HD23 . LEU   B 1 109 ? 33.862 -28.489 2.116   1.00 21.10 ?  109 LEU   B HD23 1 
ATOM   5690 N N    . LYS   B 1 110 ? 31.632 -23.953 2.980   1.00 15.51 ?  110 LYS   B N    1 
ATOM   5691 C CA   . LYS   B 1 110 ? 30.870 -23.203 1.990   1.00 15.80 ?  110 LYS   B CA   1 
ATOM   5692 C C    . LYS   B 1 110 ? 31.210 -21.718 2.060   1.00 15.26 ?  110 LYS   B C    1 
ATOM   5693 O O    . LYS   B 1 110 ? 31.461 -21.081 1.033   1.00 15.22 ?  110 LYS   B O    1 
ATOM   5694 C CB   . LYS   B 1 110 ? 29.367 -23.446 2.157   1.00 16.34 ?  110 LYS   B CB   1 
ATOM   5695 C CG   . LYS   B 1 110 ? 28.542 -22.840 1.016   1.00 16.71 ?  110 LYS   B CG   1 
ATOM   5696 C CD   . LYS   B 1 110 ? 27.079 -23.251 1.050   1.00 16.89 ?  110 LYS   B CD   1 
ATOM   5697 C CE   . LYS   B 1 110 ? 26.328 -22.707 -0.164  1.00 18.18 ?  110 LYS   B CE   1 
ATOM   5698 N NZ   . LYS   B 1 110 ? 26.657 -23.434 -1.424  1.00 18.83 ?  110 LYS   B NZ   1 
ATOM   5699 H H    . LYS   B 1 110 ? 31.165 -24.347 3.583   1.00 18.62 ?  110 LYS   B H    1 
ATOM   5700 H HA   . LYS   B 1 110 ? 31.115 -23.514 1.107   1.00 18.97 ?  110 LYS   B HA   1 
ATOM   5701 H HB2  . LYS   B 1 110 ? 29.201 -24.404 2.168   1.00 19.62 ?  110 LYS   B HB2  1 
ATOM   5702 H HB3  . LYS   B 1 110 ? 29.068 -23.049 2.989   1.00 19.62 ?  110 LYS   B HB3  1 
ATOM   5703 H HG2  . LYS   B 1 110 ? 28.576 -21.871 1.082   1.00 20.06 ?  110 LYS   B HG2  1 
ATOM   5704 H HG3  . LYS   B 1 110 ? 28.912 -23.126 0.168   1.00 20.06 ?  110 LYS   B HG3  1 
ATOM   5705 H HD2  . LYS   B 1 110 ? 27.017 -24.224 1.039   1.00 20.27 ?  110 LYS   B HD2  1 
ATOM   5706 H HD3  . LYS   B 1 110 ? 26.660 -22.903 1.854   1.00 20.27 ?  110 LYS   B HD3  1 
ATOM   5707 H HE2  . LYS   B 1 110 ? 25.375 -22.791 -0.012  1.00 21.83 ?  110 LYS   B HE2  1 
ATOM   5708 H HE3  . LYS   B 1 110 ? 26.565 -21.774 -0.285  1.00 21.83 ?  110 LYS   B HE3  1 
ATOM   5709 H HZ1  . LYS   B 1 110 ? 26.205 -23.083 -2.103  1.00 22.60 ?  110 LYS   B HZ1  1 
ATOM   5710 H HZ2  . LYS   B 1 110 ? 27.531 -23.365 -1.591  1.00 22.60 ?  110 LYS   B HZ2  1 
ATOM   5711 H HZ3  . LYS   B 1 110 ? 26.446 -24.292 -1.342  1.00 22.60 ?  110 LYS   B HZ3  1 
ATOM   5712 N N    . SER   B 1 111 ? 31.221 -21.153 3.270   1.00 15.76 ?  111 SER   B N    1 
ATOM   5713 C CA   . SER   B 1 111 ? 31.625 -19.759 3.442   1.00 15.65 ?  111 SER   B CA   1 
ATOM   5714 C C    . SER   B 1 111 ? 32.999 -19.504 2.836   1.00 14.78 ?  111 SER   B C    1 
ATOM   5715 O O    . SER   B 1 111 ? 33.219 -18.479 2.176   1.00 14.87 ?  111 SER   B O    1 
ATOM   5716 C CB   . SER   B 1 111 ? 31.645 -19.402 4.928   1.00 17.10 ?  111 SER   B CB   1 
ATOM   5717 O OG   . SER   B 1 111 ? 30.350 -19.392 5.484   1.00 18.14 ?  111 SER   B OG   1 
ATOM   5718 H H    . SER   B 1 111 ? 31.001 -21.553 3.996   1.00 18.92 ?  111 SER   B H    1 
ATOM   5719 H HA   . SER   B 1 111 ? 30.984 -19.180 2.998   1.00 18.78 ?  111 SER   B HA   1 
ATOM   5720 H HB2  . SER   B 1 111 ? 32.178 -20.063 5.398   1.00 20.53 ?  111 SER   B HB2  1 
ATOM   5721 H HB3  . SER   B 1 111 ? 32.040 -18.525 5.032   1.00 20.53 ?  111 SER   B HB3  1 
ATOM   5722 H HG   . SER   B 1 111 ? 30.390 -19.189 6.302   1.00 21.77 ?  111 SER   B HG   1 
ATOM   5723 N N    . ALA   B 1 112 ? 33.941 -20.422 3.056   1.00 14.37 ?  112 ALA   B N    1 
ATOM   5724 C CA   . ALA   B 1 112 ? 35.280 -20.259 2.504   1.00 14.28 ?  112 ALA   B CA   1 
ATOM   5725 C C    . ALA   B 1 112 ? 35.243 -20.182 0.980   1.00 13.67 ?  112 ALA   B C    1 
ATOM   5726 O O    . ALA   B 1 112 ? 35.860 -19.295 0.375   1.00 13.99 ?  112 ALA   B O    1 
ATOM   5727 C CB   . ALA   B 1 112 ? 36.190 -21.390 2.995   1.00 14.79 ?  112 ALA   B CB   1 
ATOM   5728 H H    . ALA   B 1 112 ? 33.824 -21.145 3.515   1.00 17.25 ?  112 ALA   B H    1 
ATOM   5729 H HA   . ALA   B 1 112 ? 35.642 -19.425 2.830   1.00 17.15 ?  112 ALA   B HA   1 
ATOM   5730 H HB1  . ALA   B 1 112 ? 37.078 -21.257 2.624   1.00 17.75 ?  112 ALA   B HB1  1 
ATOM   5731 H HB2  . ALA   B 1 112 ? 36.234 -21.355 3.967   1.00 17.75 ?  112 ALA   B HB2  1 
ATOM   5732 H HB3  . ALA   B 1 112 ? 35.830 -22.237 2.709   1.00 17.75 ?  112 ALA   B HB3  1 
ATOM   5733 N N    . TYR   B 1 113 ? 34.502 -21.085 0.336   1.00 13.58 ?  113 TYR   B N    1 
ATOM   5734 C CA   . TYR   B 1 113 ? 34.422 -21.052 -1.119  1.00 13.67 ?  113 TYR   B CA   1 
ATOM   5735 C C    . TYR   B 1 113 ? 33.718 -19.803 -1.638  1.00 13.19 ?  113 TYR   B C    1 
ATOM   5736 O O    . TYR   B 1 113 ? 33.986 -19.383 -2.766  1.00 13.10 ?  113 TYR   B O    1 
ATOM   5737 C CB   . TYR   B 1 113 ? 33.748 -22.320 -1.655  1.00 13.51 ?  113 TYR   B CB   1 
ATOM   5738 C CG   . TYR   B 1 113 ? 34.714 -23.468 -1.901  1.00 14.37 ?  113 TYR   B CG   1 
ATOM   5739 C CD1  . TYR   B 1 113 ? 35.724 -23.370 -2.852  1.00 14.78 ?  113 TYR   B CD1  1 
ATOM   5740 C CD2  . TYR   B 1 113 ? 34.611 -24.646 -1.188  1.00 14.46 ?  113 TYR   B CD2  1 
ATOM   5741 C CE1  . TYR   B 1 113 ? 36.602 -24.409 -3.081  1.00 14.87 ?  113 TYR   B CE1  1 
ATOM   5742 C CE2  . TYR   B 1 113 ? 35.487 -25.699 -1.411  1.00 14.89 ?  113 TYR   B CE2  1 
ATOM   5743 C CZ   . TYR   B 1 113 ? 36.478 -25.575 -2.358  1.00 14.53 ?  113 TYR   B CZ   1 
ATOM   5744 O OH   . TYR   B 1 113 ? 37.361 -26.598 -2.611  1.00 15.69 ?  113 TYR   B OH   1 
ATOM   5745 H H    . TYR   B 1 113 ? 34.042 -21.714 0.714   1.00 16.31 ?  113 TYR   B H    1 
ATOM   5746 H HA   . TYR   B 1 113 ? 35.324 -21.039 -1.461  1.00 16.41 ?  113 TYR   B HA   1 
ATOM   5747 H HB2  . TYR   B 1 113 ? 33.088 -22.626 -1.011  1.00 16.22 ?  113 TYR   B HB2  1 
ATOM   5748 H HB3  . TYR   B 1 113 ? 33.312 -22.110 -2.495  1.00 16.22 ?  113 TYR   B HB3  1 
ATOM   5749 H HD1  . TYR   B 1 113 ? 35.813 -22.581 -3.344  1.00 17.75 ?  113 TYR   B HD1  1 
ATOM   5750 H HD2  . TYR   B 1 113 ? 33.939 -24.734 -0.555  1.00 17.36 ?  113 TYR   B HD2  1 
ATOM   5751 H HE1  . TYR   B 1 113 ? 37.269 -24.318 -3.726  1.00 17.85 ?  113 TYR   B HE1  1 
ATOM   5752 H HE2  . TYR   B 1 113 ? 35.396 -26.487 -0.930  1.00 17.87 ?  113 TYR   B HE2  1 
ATOM   5753 H HH   . TYR   B 1 113 ? 37.155 -27.275 -2.151  1.00 18.83 ?  113 TYR   B HH   1 
ATOM   5754 N N    . GLU   B 1 114 ? 32.795 -19.227 -0.861  1.00 13.54 ?  114 GLU   B N    1 
ATOM   5755 C CA   . GLU   B 1 114 ? 32.112 -18.021 -1.323  1.00 13.74 ?  114 GLU   B CA   1 
ATOM   5756 C C    . GLU   B 1 114 ? 33.093 -16.899 -1.635  1.00 13.11 ?  114 GLU   B C    1 
ATOM   5757 O O    . GLU   B 1 114 ? 32.810 -16.042 -2.475  1.00 13.81 ?  114 GLU   B O    1 
ATOM   5758 C CB   . GLU   B 1 114 ? 31.046 -17.574 -0.313  1.00 14.51 ?  114 GLU   B CB   1 
ATOM   5759 C CG   . GLU   B 1 114 ? 29.840 -18.509 -0.358  1.00 14.78 ?  114 GLU   B CG   1 
ATOM   5760 C CD   . GLU   B 1 114 ? 28.812 -18.308 0.746   1.00 15.33 ?  114 GLU   B CD   1 
ATOM   5761 O OE1  . GLU   B 1 114 ? 29.099 -17.684 1.786   1.00 15.09 ?  114 GLU   B OE1  1 
ATOM   5762 O OE2  . GLU   B 1 114 ? 27.695 -18.851 0.589   1.00 16.08 -1 114 GLU   B OE2  1 
ATOM   5763 H H    . GLU   B 1 114 ? 32.554 -19.506 -0.081  1.00 16.26 ?  114 GLU   B H    1 
ATOM   5764 H HA   . GLU   B 1 114 ? 31.657 -18.232 -2.147  1.00 16.50 ?  114 GLU   B HA   1 
ATOM   5765 H HB2  . GLU   B 1 114 ? 31.417 -17.598 0.584   1.00 17.42 ?  114 GLU   B HB2  1 
ATOM   5766 H HB3  . GLU   B 1 114 ? 30.746 -16.681 -0.533  1.00 17.42 ?  114 GLU   B HB3  1 
ATOM   5767 H HG2  . GLU   B 1 114 ? 29.394 -18.383 -1.203  1.00 17.74 ?  114 GLU   B HG2  1 
ATOM   5768 H HG3  . GLU   B 1 114 ? 30.165 -19.420 -0.288  1.00 17.74 ?  114 GLU   B HG3  1 
ATOM   5769 N N    . ASN   B 1 115 ? 34.260 -16.892 -0.992  1.00 13.15 ?  115 ASN   B N    1 
ATOM   5770 C CA   . ASN   B 1 115 ? 35.248 -15.860 -1.294  1.00 13.05 ?  115 ASN   B CA   1 
ATOM   5771 C C    . ASN   B 1 115 ? 35.659 -15.894 -2.756  1.00 12.90 ?  115 ASN   B C    1 
ATOM   5772 O O    . ASN   B 1 115 ? 36.049 -14.858 -3.321  1.00 13.25 ?  115 ASN   B O    1 
ATOM   5773 C CB   . ASN   B 1 115 ? 36.477 -16.030 -0.401  1.00 13.56 ?  115 ASN   B CB   1 
ATOM   5774 C CG   . ASN   B 1 115 ? 36.196 -15.751 1.050   1.00 14.08 ?  115 ASN   B CG   1 
ATOM   5775 O OD1  . ASN   B 1 115 ? 36.177 -14.594 1.481   1.00 16.44 ?  115 ASN   B OD1  1 
ATOM   5776 N ND2  . ASN   B 1 115 ? 36.047 -16.817 1.838   1.00 14.14 ?  115 ASN   B ND2  1 
ATOM   5777 H H    . ASN   B 1 115 ? 34.503 -17.455 -0.382  1.00 15.78 ?  115 ASN   B H    1 
ATOM   5778 H HA   . ASN   B 1 115 ? 34.869 -14.991 -1.109  1.00 15.67 ?  115 ASN   B HA   1 
ATOM   5779 H HB2  . ASN   B 1 115 ? 36.804 -16.942 -0.477  1.00 16.28 ?  115 ASN   B HB2  1 
ATOM   5780 H HB3  . ASN   B 1 115 ? 37.168 -15.411 -0.690  1.00 16.28 ?  115 ASN   B HB3  1 
ATOM   5781 H HD21 . ASN   B 1 115 ? 35.886 -16.721 2.677   1.00 16.98 ?  115 ASN   B HD21 1 
ATOM   5782 H HD22 . ASN   B 1 115 ? 36.083 -17.617 1.504   1.00 16.98 ?  115 ASN   B HD22 1 
ATOM   5783 N N    . PHE   B 1 116 ? 35.624 -17.075 -3.379  1.00 12.77 ?  116 PHE   B N    1 
ATOM   5784 C CA   . PHE   B 1 116 ? 36.062 -17.167 -4.764  1.00 13.06 ?  116 PHE   B CA   1 
ATOM   5785 C C    . PHE   B 1 116 ? 35.164 -16.347 -5.683  1.00 12.70 ?  116 PHE   B C    1 
ATOM   5786 O O    . PHE   B 1 116 ? 35.601 -15.931 -6.761  1.00 13.26 ?  116 PHE   B O    1 
ATOM   5787 C CB   . PHE   B 1 116 ? 36.024 -18.611 -5.276  1.00 12.63 ?  116 PHE   B CB   1 
ATOM   5788 C CG   . PHE   B 1 116 ? 37.094 -19.565 -4.724  1.00 12.55 ?  116 PHE   B CG   1 
ATOM   5789 C CD1  . PHE   B 1 116 ? 37.737 -19.381 -3.512  1.00 13.42 ?  116 PHE   B CD1  1 
ATOM   5790 C CD2  . PHE   B 1 116 ? 37.400 -20.708 -5.454  1.00 13.03 ?  116 PHE   B CD2  1 
ATOM   5791 C CE1  . PHE   B 1 116 ? 38.662 -20.314 -3.059  1.00 13.76 ?  116 PHE   B CE1  1 
ATOM   5792 C CE2  . PHE   B 1 116 ? 38.322 -21.639 -5.002  1.00 12.90 ?  116 PHE   B CE2  1 
ATOM   5793 C CZ   . PHE   B 1 116 ? 38.944 -21.445 -3.813  1.00 13.05 ?  116 PHE   B CZ   1 
ATOM   5794 H H    . PHE   B 1 116 ? 35.364 -17.822 -3.029  1.00 15.33 ?  116 PHE   B H    1 
ATOM   5795 H HA   . PHE   B 1 116 ? 36.971 -16.837 -4.842  1.00 15.68 ?  116 PHE   B HA   1 
ATOM   5796 H HB2  . PHE   B 1 116 ? 35.159 -18.990 -5.054  1.00 15.16 ?  116 PHE   B HB2  1 
ATOM   5797 H HB3  . PHE   B 1 116 ? 36.126 -18.593 -6.241  1.00 15.16 ?  116 PHE   B HB3  1 
ATOM   5798 H HD1  . PHE   B 1 116 ? 37.549 -18.632 -2.992  1.00 16.11 ?  116 PHE   B HD1  1 
ATOM   5799 H HD2  . PHE   B 1 116 ? 36.961 -20.854 -6.263  1.00 15.64 ?  116 PHE   B HD2  1 
ATOM   5800 H HE1  . PHE   B 1 116 ? 39.101 -20.181 -2.246  1.00 16.52 ?  116 PHE   B HE1  1 
ATOM   5801 H HE2  . PHE   B 1 116 ? 38.504 -22.389 -5.517  1.00 15.49 ?  116 PHE   B HE2  1 
ATOM   5802 H HZ   . PHE   B 1 116 ? 39.575 -22.058 -3.514  1.00 15.66 ?  116 PHE   B HZ   1 
ATOM   5803 N N    . ASN   B 1 117 ? 33.897 -16.136 -5.301  1.00 13.29 ?  117 ASN   B N    1 
ATOM   5804 C CA   . ASN   B 1 117 ? 32.946 -15.438 -6.169  1.00 13.47 ?  117 ASN   B CA   1 
ATOM   5805 C C    . ASN   B 1 117 ? 33.266 -13.963 -6.332  1.00 13.89 ?  117 ASN   B C    1 
ATOM   5806 O O    . ASN   B 1 117 ? 32.671 -13.311 -7.190  1.00 15.38 ?  117 ASN   B O    1 
ATOM   5807 C CB   . ASN   B 1 117 ? 31.523 -15.652 -5.665  1.00 13.52 ?  117 ASN   B CB   1 
ATOM   5808 C CG   . ASN   B 1 117 ? 31.061 -17.060 -5.908  1.00 14.15 ?  117 ASN   B CG   1 
ATOM   5809 O OD1  . ASN   B 1 117 ? 31.414 -17.651 -6.933  1.00 15.09 ?  117 ASN   B OD1  1 
ATOM   5810 N ND2  . ASN   B 1 117 ? 30.337 -17.634 -4.950  1.00 14.13 ?  117 ASN   B ND2  1 
ATOM   5811 H H    . ASN   B 1 117 ? 33.571 -16.392 -4.544  1.00 15.96 ?  117 ASN   B H    1 
ATOM   5812 H HA   . ASN   B 1 117 ? 32.998 -15.842 -7.045  1.00 16.18 ?  117 ASN   B HA   1 
ATOM   5813 H HB2  . ASN   B 1 117 ? 31.486 -15.477 -4.706  1.00 16.23 ?  117 ASN   B HB2  1 
ATOM   5814 H HB3  . ASN   B 1 117 ? 30.922 -15.048 -6.132  1.00 16.23 ?  117 ASN   B HB3  1 
ATOM   5815 H HD21 . ASN   B 1 117 ? 30.050 -18.440 -5.049  1.00 16.96 ?  117 ASN   B HD21 1 
ATOM   5816 H HD22 . ASN   B 1 117 ? 30.123 -17.192 -4.240  1.00 16.96 ?  117 ASN   B HD22 1 
ATOM   5817 N N    . GLN   B 1 118 ? 34.210 -13.440 -5.571  1.00 13.44 ?  118 GLN   B N    1 
ATOM   5818 C CA   . GLN   B 1 118 ? 34.626 -12.056 -5.713  1.00 14.44 ?  118 GLN   B CA   1 
ATOM   5819 C C    . GLN   B 1 118 ? 35.692 -11.874 -6.783  1.00 14.45 ?  118 GLN   B C    1 
ATOM   5820 O O    . GLN   B 1 118 ? 36.161 -10.747 -6.978  1.00 15.97 ?  118 GLN   B O    1 
ATOM   5821 C CB   . GLN   B 1 118 ? 35.111 -11.511 -4.361  1.00 15.04 ?  118 GLN   B CB   1 
ATOM   5822 C CG   . GLN   B 1 118 ? 34.026 -11.549 -3.292  1.00 15.25 ?  118 GLN   B CG   1 
ATOM   5823 C CD   . GLN   B 1 118 ? 32.858 -10.634 -3.624  1.00 14.81 ?  118 GLN   B CD   1 
ATOM   5824 O OE1  . GLN   B 1 118 ? 33.053 -9.502  -4.067  1.00 15.79 ?  118 GLN   B OE1  1 
ATOM   5825 N NE2  . GLN   B 1 118 ? 31.641 -11.116 -3.412  1.00 15.29 ?  118 GLN   B NE2  1 
ATOM   5826 H H    . GLN   B 1 118 ? 34.638 -13.867 -4.959  1.00 16.13 ?  118 GLN   B H    1 
ATOM   5827 H HA   . GLN   B 1 118 ? 33.858 -11.529 -5.983  1.00 17.33 ?  118 GLN   B HA   1 
ATOM   5828 H HB2  . GLN   B 1 118 ? 35.857 -12.044 -4.054  1.00 18.06 ?  118 GLN   B HB2  1 
ATOM   5829 H HB3  . GLN   B 1 118 ? 35.384 -10.585 -4.472  1.00 18.06 ?  118 GLN   B HB3  1 
ATOM   5830 H HG2  . GLN   B 1 118 ? 33.689 -12.461 -3.215  1.00 18.31 ?  118 GLN   B HG2  1 
ATOM   5831 H HG3  . GLN   B 1 118 ? 34.402 -11.266 -2.446  1.00 18.31 ?  118 GLN   B HG3  1 
ATOM   5832 H HE21 . GLN   B 1 118 ? 31.542 -11.917 -3.100  1.00 18.35 ?  118 GLN   B HE21 1 
ATOM   5833 H HE22 . GLN   B 1 118 ? 30.954 -10.637 -3.585  1.00 18.35 ?  118 GLN   B HE22 1 
ATOM   5834 N N    . HIS   B 1 119 ? 36.054 -12.938 -7.503  1.00 13.32 ?  119 HIS   B N    1 
ATOM   5835 C CA   . HIS   B 1 119 ? 37.095 -12.896 -8.521  1.00 13.65 ?  119 HIS   B CA   1 
ATOM   5836 C C    . HIS   B 1 119 ? 36.612 -13.629 -9.760  1.00 14.10 ?  119 HIS   B C    1 
ATOM   5837 O O    . HIS   B 1 119 ? 36.101 -14.744 -9.662  1.00 15.08 ?  119 HIS   B O    1 
ATOM   5838 C CB   . HIS   B 1 119 ? 38.373 -13.523 -7.969  1.00 14.33 ?  119 HIS   B CB   1 
ATOM   5839 C CG   . HIS   B 1 119 ? 38.839 -12.834 -6.731  1.00 15.30 ?  119 HIS   B CG   1 
ATOM   5840 N ND1  . HIS   B 1 119 ? 39.637 -11.710 -6.764  1.00 16.90 ?  119 HIS   B ND1  1 
ATOM   5841 C CD2  . HIS   B 1 119 ? 38.535 -13.047 -5.430  1.00 16.21 ?  119 HIS   B CD2  1 
ATOM   5842 C CE1  . HIS   B 1 119 ? 39.836 -11.290 -5.529  1.00 17.63 ?  119 HIS   B CE1  1 
ATOM   5843 N NE2  . HIS   B 1 119 ? 39.166 -12.071 -4.703  1.00 17.81 ?  119 HIS   B NE2  1 
ATOM   5844 H H    . HIS   B 1 119 ? 35.701 -13.724 -7.414  1.00 15.99 ?  119 HIS   B H    1 
ATOM   5845 H HA   . HIS   B 1 119 ? 37.274 -11.968 -8.757  1.00 16.38 ?  119 HIS   B HA   1 
ATOM   5846 H HB2  . HIS   B 1 119 ? 38.208 -14.452 -7.760  1.00 17.20 ?  119 HIS   B HB2  1 
ATOM   5847 H HB3  . HIS   B 1 119 ? 39.075 -13.449 -8.639  1.00 17.20 ?  119 HIS   B HB3  1 
ATOM   5848 H HD2  . HIS   B 1 119 ? 37.989 -13.724 -5.094  1.00 19.47 ?  119 HIS   B HD2  1 
ATOM   5849 H HE1  . HIS   B 1 119 ? 40.371 -10.573 -5.274  1.00 21.17 ?  119 HIS   B HE1  1 
ATOM   5850 H HE2  . HIS   B 1 119 ? 39.161 -12.010 -3.841  1.00 21.38 ?  119 HIS   B HE2  1 
ATOM   5851 N N    A GLU   B 1 120 ? 36.772 -13.008 -10.928 0.48 15.05 ?  120 GLU   B N    1 
ATOM   5852 N N    B GLU   B 1 120 ? 36.773 -13.001 -10.924 0.52 14.72 ?  120 GLU   B N    1 
ATOM   5853 C CA   A GLU   B 1 120 ? 36.185 -13.580 -12.136 0.48 16.81 ?  120 GLU   B CA   1 
ATOM   5854 C CA   B GLU   B 1 120 ? 36.205 -13.563 -12.144 0.52 16.27 ?  120 GLU   B CA   1 
ATOM   5855 C C    A GLU   B 1 120 ? 36.856 -14.886 -12.550 0.48 15.56 ?  120 GLU   B C    1 
ATOM   5856 C C    B GLU   B 1 120 ? 36.851 -14.890 -12.522 0.52 15.28 ?  120 GLU   B C    1 
ATOM   5857 O O    A GLU   B 1 120 ? 36.199 -15.748 -13.144 0.48 15.50 ?  120 GLU   B O    1 
ATOM   5858 O O    B GLU   B 1 120 ? 36.169 -15.772 -13.058 0.52 15.20 ?  120 GLU   B O    1 
ATOM   5859 C CB   A GLU   B 1 120 ? 36.219 -12.561 -13.274 0.48 21.08 ?  120 GLU   B CB   1 
ATOM   5860 C CB   B GLU   B 1 120 ? 36.327 -12.556 -13.286 0.52 20.21 ?  120 GLU   B CB   1 
ATOM   5861 C CG   A GLU   B 1 120 ? 35.216 -11.427 -13.104 0.48 26.22 ?  120 GLU   B CG   1 
ATOM   5862 C CG   B GLU   B 1 120 ? 35.409 -11.350 -13.140 0.52 25.73 ?  120 GLU   B CG   1 
ATOM   5863 C CD   A GLU   B 1 120 ? 35.081 -10.564 -14.343 0.48 30.39 ?  120 GLU   B CD   1 
ATOM   5864 C CD   B GLU   B 1 120 ? 35.354 -10.511 -14.402 0.52 30.47 ?  120 GLU   B CD   1 
ATOM   5865 O OE1  A GLU   B 1 120 ? 36.100 -10.334 -15.030 0.48 32.10 ?  120 GLU   B OE1  1 
ATOM   5866 O OE1  B GLU   B 1 120 ? 36.300 -10.600 -15.216 0.52 32.32 ?  120 GLU   B OE1  1 
ATOM   5867 O OE2  A GLU   B 1 120 ? 33.949 -10.122 -14.635 0.48 32.31 -1 120 GLU   B OE2  1 
ATOM   5868 O OE2  B GLU   B 1 120 ? 34.371 -9.762  -14.582 0.52 32.40 -1 120 GLU   B OE2  1 
ATOM   5869 H H    A GLU   B 1 120 ? 37.199 -12.271 -11.043 0.48 18.07 ?  120 GLU   B H    1 
ATOM   5870 H H    B GLU   B 1 120 ? 37.200 -12.261 -11.030 0.52 17.67 ?  120 GLU   B H    1 
ATOM   5871 H HA   A GLU   B 1 120 ? 35.253 -13.777 -11.957 0.48 20.18 ?  120 GLU   B HA   1 
ATOM   5872 H HA   B GLU   B 1 120 ? 35.260 -13.722 -12.001 0.52 19.54 ?  120 GLU   B HA   1 
ATOM   5873 H HB2  A GLU   B 1 120 ? 37.104 -12.167 -13.319 0.48 25.31 ?  120 GLU   B HB2  1 
ATOM   5874 H HB2  B GLU   B 1 120 ? 37.236 -12.220 -13.323 0.52 24.26 ?  120 GLU   B HB2  1 
ATOM   5875 H HB3  A GLU   B 1 120 ? 36.014 -13.012 -14.107 0.48 25.31 ?  120 GLU   B HB3  1 
ATOM   5876 H HB3  B GLU   B 1 120 ? 36.102 -12.991 -14.123 0.52 24.26 ?  120 GLU   B HB3  1 
ATOM   5877 H HG2  A GLU   B 1 120 ? 34.340 -11.800 -12.923 0.48 31.47 ?  120 GLU   B HG2  1 
ATOM   5878 H HG2  B GLU   B 1 120 ? 34.508 -11.656 -12.930 0.52 30.88 ?  120 GLU   B HG2  1 
ATOM   5879 H HG3  A GLU   B 1 120 ? 35.495 -10.863 -12.365 0.48 31.47 ?  120 GLU   B HG3  1 
ATOM   5880 H HG3  B GLU   B 1 120 ? 35.734 -10.778 -12.427 0.52 30.88 ?  120 GLU   B HG3  1 
ATOM   5881 N N    . VAL   B 1 121 ? 38.147 -15.046 -12.262 1.00 14.76 ?  121 VAL   B N    1 
ATOM   5882 C CA   . VAL   B 1 121 ? 38.888 -16.262 -12.605 1.00 14.64 ?  121 VAL   B CA   1 
ATOM   5883 C C    . VAL   B 1 121 ? 40.008 -16.463 -11.589 1.00 14.32 ?  121 VAL   B C    1 
ATOM   5884 O O    . VAL   B 1 121 ? 40.694 -15.506 -11.204 1.00 14.39 ?  121 VAL   B O    1 
ATOM   5885 C CB   . VAL   B 1 121 ? 39.410 -16.210 -14.061 1.00 16.54 ?  121 VAL   B CB   1 
ATOM   5886 C CG1  . VAL   B 1 121 ? 40.282 -14.978 -14.286 1.00 18.35 ?  121 VAL   B CG1  1 
ATOM   5887 C CG2  . VAL   B 1 121 ? 40.150 -17.497 -14.422 1.00 18.25 ?  121 VAL   B CG2  1 
ATOM   5888 H H    A VAL   B 1 121 ? 38.627 -14.449 -11.871 0.48 17.72 ?  121 VAL   B H    1 
ATOM   5889 H H    B VAL   B 1 121 ? 38.633 -14.445 -11.885 0.52 17.72 ?  121 VAL   B H    1 
ATOM   5890 H HA   . VAL   B 1 121 ? 38.279 -17.015 -12.539 1.00 17.58 ?  121 VAL   B HA   1 
ATOM   5891 H HB   . VAL   B 1 121 ? 38.647 -16.139 -14.659 1.00 19.86 ?  121 VAL   B HB   1 
ATOM   5892 H HG11 . VAL   B 1 121 ? 40.590 -14.974 -15.205 1.00 22.03 ?  121 VAL   B HG11 1 
ATOM   5893 H HG12 . VAL   B 1 121 ? 39.755 -14.181 -14.112 1.00 22.03 ?  121 VAL   B HG12 1 
ATOM   5894 H HG13 . VAL   B 1 121 ? 41.040 -15.011 -13.683 1.00 22.03 ?  121 VAL   B HG13 1 
ATOM   5895 H HG21 . VAL   B 1 121 ? 40.359 -17.484 -15.372 1.00 21.91 ?  121 VAL   B HG21 1 
ATOM   5896 H HG22 . VAL   B 1 121 ? 40.972 -17.546 -13.908 1.00 21.91 ?  121 VAL   B HG22 1 
ATOM   5897 H HG23 . VAL   B 1 121 ? 39.585 -18.257 -14.220 1.00 21.91 ?  121 VAL   B HG23 1 
ATOM   5898 N N    . LEU   B 1 122 ? 40.186 -17.711 -11.145 1.00 13.38 ?  122 LEU   B N    1 
ATOM   5899 C CA   . LEU   B 1 122 ? 41.171 -18.056 -10.124 1.00 13.04 ?  122 LEU   B CA   1 
ATOM   5900 C C    . LEU   B 1 122 ? 41.817 -19.393 -10.444 1.00 12.95 ?  122 LEU   B C    1 
ATOM   5901 O O    . LEU   B 1 122 ? 41.159 -20.312 -10.942 1.00 14.25 ?  122 LEU   B O    1 
ATOM   5902 C CB   . LEU   B 1 122 ? 40.518 -18.272 -8.743  1.00 15.19 ?  122 LEU   B CB   1 
ATOM   5903 C CG   . LEU   B 1 122 ? 39.471 -17.265 -8.257  1.00 15.21 ?  122 LEU   B CG   1 
ATOM   5904 C CD1  . LEU   B 1 122 ? 38.079 -17.653 -8.715  1.00 15.84 ?  122 LEU   B CD1  1 
ATOM   5905 C CD2  . LEU   B 1 122 ? 39.509 -17.146 -6.749  1.00 14.56 ?  122 LEU   B CD2  1 
ATOM   5906 H H    . LEU   B 1 122 ? 39.740 -18.388 -11.427 1.00 16.07 ?  122 LEU   B H    1 
ATOM   5907 H HA   . LEU   B 1 122 ? 41.850 -17.366 -10.051 1.00 15.65 ?  122 LEU   B HA   1 
ATOM   5908 H HB2  . LEU   B 1 122 ? 40.084 -19.136 -8.751  1.00 18.24 ?  122 LEU   B HB2  1 
ATOM   5909 H HB3  . LEU   B 1 122 ? 41.222 -18.276 -8.077  1.00 18.24 ?  122 LEU   B HB3  1 
ATOM   5910 H HG   . LEU   B 1 122 ? 39.671 -16.391 -8.625  1.00 18.27 ?  122 LEU   B HG   1 
ATOM   5911 H HD11 . LEU   B 1 122 ? 37.439 -17.009 -8.372  1.00 19.01 ?  122 LEU   B HD11 1 
ATOM   5912 H HD12 . LEU   B 1 122 ? 38.054 -17.655 -9.685  1.00 19.01 ?  122 LEU   B HD12 1 
ATOM   5913 H HD13 . LEU   B 1 122 ? 37.869 -18.538 -8.378  1.00 19.01 ?  122 LEU   B HD13 1 
ATOM   5914 H HD21 . LEU   B 1 122 ? 38.819 -16.534 -6.456  1.00 17.48 ?  122 LEU   B HD21 1 
ATOM   5915 H HD22 . LEU   B 1 122 ? 39.362 -18.024 -6.358  1.00 17.48 ?  122 LEU   B HD22 1 
ATOM   5916 H HD23 . LEU   B 1 122 ? 40.383 -16.814 -6.481  1.00 17.48 ?  122 LEU   B HD23 1 
ATOM   5917 N N    . LEU   B 1 123 ? 43.099 -19.504 -10.080 1.00 12.42 ?  123 LEU   B N    1 
ATOM   5918 C CA   . LEU   B 1 123 ? 43.803 -20.775 -9.956  1.00 12.31 ?  123 LEU   B CA   1 
ATOM   5919 C C    . LEU   B 1 123 ? 43.776 -21.161 -8.484  1.00 12.39 ?  123 LEU   B C    1 
ATOM   5920 O O    . LEU   B 1 123 ? 44.147 -20.348 -7.633  1.00 12.77 ?  123 LEU   B O    1 
ATOM   5921 C CB   . LEU   B 1 123 ? 45.252 -20.600 -10.412 1.00 12.70 ?  123 LEU   B CB   1 
ATOM   5922 C CG   . LEU   B 1 123 ? 46.184 -21.800 -10.179 1.00 13.30 ?  123 LEU   B CG   1 
ATOM   5923 C CD1  . LEU   B 1 123 ? 45.751 -23.037 -10.965 1.00 14.42 ?  123 LEU   B CD1  1 
ATOM   5924 C CD2  . LEU   B 1 123 ? 47.604 -21.406 -10.548 1.00 14.39 ?  123 LEU   B CD2  1 
ATOM   5925 H H    . LEU   B 1 123 ? 43.591 -18.831 -9.882  1.00 14.92 ?  123 LEU   B H    1 
ATOM   5926 H HA   . LEU   B 1 123 ? 43.365 -21.465 -10.485 1.00 14.79 ?  123 LEU   B HA   1 
ATOM   5927 H HB2  . LEU   B 1 123 ? 45.247 -20.418 -11.366 1.00 15.24 ?  123 LEU   B HB2  1 
ATOM   5928 H HB3  . LEU   B 1 123 ? 45.627 -19.843 -9.940  1.00 15.24 ?  123 LEU   B HB3  1 
ATOM   5929 H HG   . LEU   B 1 123 ? 46.174 -22.026 -9.237  1.00 15.97 ?  123 LEU   B HG   1 
ATOM   5930 H HD11 . LEU   B 1 123 ? 46.380 -23.752 -10.794 1.00 17.31 ?  123 LEU   B HD11 1 
ATOM   5931 H HD12 . LEU   B 1 123 ? 44.862 -23.301 -10.676 1.00 17.31 ?  123 LEU   B HD12 1 
ATOM   5932 H HD13 . LEU   B 1 123 ? 45.740 -22.822 -11.911 1.00 17.31 ?  123 LEU   B HD13 1 
ATOM   5933 H HD21 . LEU   B 1 123 ? 48.185 -22.164 -10.400 1.00 17.27 ?  123 LEU   B HD21 1 
ATOM   5934 H HD22 . LEU   B 1 123 ? 47.623 -21.146 -11.483 1.00 17.27 ?  123 LEU   B HD22 1 
ATOM   5935 H HD23 . LEU   B 1 123 ? 47.876 -20.660 -9.991  1.00 17.27 ?  123 LEU   B HD23 1 
ATOM   5936 N N    . ALA   B 1 124 ? 43.340 -22.384 -8.172  1.00 12.37 ?  124 ALA   B N    1 
ATOM   5937 C CA   . ALA   B 1 124 ? 43.086 -22.691 -6.772  1.00 12.79 ?  124 ALA   B CA   1 
ATOM   5938 C C    . ALA   B 1 124 ? 43.370 -24.149 -6.442  1.00 11.78 ?  124 ALA   B C    1 
ATOM   5939 O O    . ALA   B 1 124 ? 43.231 -25.030 -7.302  1.00 12.56 ?  124 ALA   B O    1 
ATOM   5940 C CB   . ALA   B 1 124 ? 41.632 -22.380 -6.410  1.00 13.43 ?  124 ALA   B CB   1 
ATOM   5941 H H    . ALA   B 1 124 ? 43.168 -23.025 -8.735  1.00 14.86 ?  124 ALA   B H    1 
ATOM   5942 H HA   . ALA   B 1 124 ? 43.662 -22.134 -6.236  1.00 15.35 ?  124 ALA   B HA   1 
ATOM   5943 H HB1  . ALA   B 1 124 ? 41.485 -22.584 -5.479  1.00 16.12 ?  124 ALA   B HB1  1 
ATOM   5944 H HB2  . ALA   B 1 124 ? 41.464 -21.433 -6.574  1.00 16.12 ?  124 ALA   B HB2  1 
ATOM   5945 H HB3  . ALA   B 1 124 ? 41.043 -22.913 -6.969  1.00 16.12 ?  124 ALA   B HB3  1 
ATOM   5946 N N    . PRO   B 1 125 ? 43.669 -24.438 -5.177  1.00 12.15 ?  125 PRO   B N    1 
ATOM   5947 C CA   . PRO   B 1 125 ? 43.610 -25.800 -4.648  1.00 13.03 ?  125 PRO   B CA   1 
ATOM   5948 C C    . PRO   B 1 125 ? 42.210 -26.074 -4.101  1.00 13.41 ?  125 PRO   B C    1 
ATOM   5949 O O    . PRO   B 1 125 ? 41.412 -25.158 -3.895  1.00 14.03 ?  125 PRO   B O    1 
ATOM   5950 C CB   . PRO   B 1 125 ? 44.596 -25.719 -3.478  1.00 14.45 ?  125 PRO   B CB   1 
ATOM   5951 C CG   . PRO   B 1 125 ? 44.325 -24.343 -2.909  1.00 14.46 ?  125 PRO   B CG   1 
ATOM   5952 C CD   . PRO   B 1 125 ? 43.989 -23.462 -4.115  1.00 13.46 ?  125 PRO   B CD   1 
ATOM   5953 H HA   . PRO   B 1 125 ? 43.884 -26.466 -5.295  1.00 15.64 ?  125 PRO   B HA   1 
ATOM   5954 H HB2  . PRO   B 1 125 ? 44.399 -26.407 -2.822  1.00 17.35 ?  125 PRO   B HB2  1 
ATOM   5955 H HB3  . PRO   B 1 125 ? 45.507 -25.785 -3.797  1.00 17.35 ?  125 PRO   B HB3  1 
ATOM   5956 H HG2  . PRO   B 1 125 ? 43.567 -24.378 -2.297  1.00 17.36 ?  125 PRO   B HG2  1 
ATOM   5957 H HG3  . PRO   B 1 125 ? 45.112 -24.008 -2.450  1.00 17.36 ?  125 PRO   B HG3  1 
ATOM   5958 H HD2  . PRO   B 1 125 ? 43.223 -22.894 -3.925  1.00 16.16 ?  125 PRO   B HD2  1 
ATOM   5959 H HD3  . PRO   B 1 125 ? 44.764 -22.927 -4.369  1.00 16.16 ?  125 PRO   B HD3  1 
ATOM   5960 N N    . LEU   B 1 126 ? 41.954 -27.351 -3.795  1.00 13.92 ?  126 LEU   B N    1 
ATOM   5961 C CA   . LEU   B 1 126 ? 40.740 -27.716 -3.072  1.00 14.38 ?  126 LEU   B CA   1 
ATOM   5962 C C    . LEU   B 1 126 ? 40.871 -27.306 -1.612  1.00 14.28 ?  126 LEU   B C    1 
ATOM   5963 O O    . LEU   B 1 126 ? 41.775 -27.765 -0.907  1.00 17.03 ?  126 LEU   B O    1 
ATOM   5964 C CB   . LEU   B 1 126 ? 40.479 -29.216 -3.174  1.00 15.87 ?  126 LEU   B CB   1 
ATOM   5965 C CG   . LEU   B 1 126 ? 39.942 -29.703 -4.520  1.00 17.52 ?  126 LEU   B CG   1 
ATOM   5966 C CD1  . LEU   B 1 126 ? 39.996 -31.211 -4.589  1.00 19.36 ?  126 LEU   B CD1  1 
ATOM   5967 C CD2  . LEU   B 1 126 ? 38.518 -29.219 -4.759  1.00 18.30 ?  126 LEU   B CD2  1 
ATOM   5968 H H    . LEU   B 1 126 ? 42.474 -28.014 -3.973  1.00 16.71 ?  126 LEU   B H    1 
ATOM   5969 H HA   . LEU   B 1 126 ? 39.987 -27.244 -3.452  1.00 17.26 ?  126 LEU   B HA   1 
ATOM   5970 H HB2  . LEU   B 1 126 ? 41.309 -29.683 -3.007  1.00 19.05 ?  126 LEU   B HB2  1 
ATOM   5971 H HB3  . LEU   B 1 126 ? 39.827 -29.459 -2.498  1.00 19.05 ?  126 LEU   B HB3  1 
ATOM   5972 H HG   . LEU   B 1 126 ? 40.500 -29.345 -5.230  1.00 21.03 ?  126 LEU   B HG   1 
ATOM   5973 H HD11 . LEU   B 1 126 ? 39.648 -31.499 -5.449  1.00 23.24 ?  126 LEU   B HD11 1 
ATOM   5974 H HD12 . LEU   B 1 126 ? 40.915 -31.498 -4.490  1.00 23.24 ?  126 LEU   B HD12 1 
ATOM   5975 H HD13 . LEU   B 1 126 ? 39.452 -31.577 -3.874  1.00 23.24 ?  126 LEU   B HD13 1 
ATOM   5976 H HD21 . LEU   B 1 126 ? 38.178 -29.622 -5.573  1.00 21.97 ?  126 LEU   B HD21 1 
ATOM   5977 H HD22 . LEU   B 1 126 ? 37.964 -29.480 -4.005  1.00 21.97 ?  126 LEU   B HD22 1 
ATOM   5978 H HD23 . LEU   B 1 126 ? 38.517 -28.251 -4.847  1.00 21.97 ?  126 LEU   B HD23 1 
ATOM   5979 N N    . LEU   B 1 127 ? 39.938 -26.482 -1.144  1.00 14.29 ?  127 LEU   B N    1 
ATOM   5980 C CA   . LEU   B 1 127 ? 39.996 -25.986 0.219   1.00 14.98 ?  127 LEU   B CA   1 
ATOM   5981 C C    . LEU   B 1 127 ? 39.716 -27.099 1.225   1.00 14.97 ?  127 LEU   B C    1 
ATOM   5982 O O    . LEU   B 1 127 ? 38.889 -27.993 1.006   1.00 15.44 ?  127 LEU   B O    1 
ATOM   5983 C CB   . LEU   B 1 127 ? 38.972 -24.869 0.416   1.00 15.70 ?  127 LEU   B CB   1 
ATOM   5984 C CG   . LEU   B 1 127 ? 39.170 -23.615 -0.432  1.00 16.26 ?  127 LEU   B CG   1 
ATOM   5985 C CD1  . LEU   B 1 127 ? 38.059 -22.620 -0.164  1.00 16.58 ?  127 LEU   B CD1  1 
ATOM   5986 C CD2  . LEU   B 1 127 ? 40.523 -22.980 -0.157  1.00 17.34 ?  127 LEU   B CD2  1 
ATOM   5987 H H    . LEU   B 1 127 ? 39.271 -26.177 -1.602  1.00 17.15 ?  127 LEU   B H    1 
ATOM   5988 H HA   . LEU   B 1 127 ? 40.882 -25.620 0.394   1.00 17.98 ?  127 LEU   B HA   1 
ATOM   5989 H HB2  . LEU   B 1 127 ? 38.093 -25.221 0.205   1.00 18.85 ?  127 LEU   B HB2  1 
ATOM   5990 H HB3  . LEU   B 1 127 ? 38.992 -24.594 1.346   1.00 18.85 ?  127 LEU   B HB3  1 
ATOM   5991 H HG   . LEU   B 1 127 ? 39.129 -23.849 -1.368  1.00 19.52 ?  127 LEU   B HG   1 
ATOM   5992 H HD11 . LEU   B 1 127 ? 38.209 -21.820 -0.705  1.00 19.91 ?  127 LEU   B HD11 1 
ATOM   5993 H HD12 . LEU   B 1 127 ? 37.207 -23.014 -0.400  1.00 19.91 ?  127 LEU   B HD12 1 
ATOM   5994 H HD13 . LEU   B 1 127 ? 38.063 -22.376 0.776   1.00 19.91 ?  127 LEU   B HD13 1 
ATOM   5995 H HD21 . LEU   B 1 127 ? 40.561 -22.113 -0.592  1.00 20.82 ?  127 LEU   B HD21 1 
ATOM   5996 H HD22 . LEU   B 1 127 ? 40.632 -22.871 0.802   1.00 20.82 ?  127 LEU   B HD22 1 
ATOM   5997 H HD23 . LEU   B 1 127 ? 41.215 -23.558 -0.507  1.00 20.82 ?  127 LEU   B HD23 1 
ATOM   5998 N N    . SER   B 1 128 ? 40.397 -27.009 2.359   1.00 14.94 ?  128 SER   B N    1 
ATOM   5999 C CA   . SER   B 1 128 ? 40.266 -27.907 3.494   1.00 15.86 ?  128 SER   B CA   1 
ATOM   6000 C C    . SER   B 1 128 ? 40.752 -29.318 3.197   1.00 17.02 ?  128 SER   B C    1 
ATOM   6001 O O    . SER   B 1 128 ? 40.635 -30.183 4.057   1.00 18.51 ?  128 SER   B O    1 
ATOM   6002 C CB   . SER   B 1 128 ? 38.859 -27.904 4.108   1.00 16.27 ?  128 SER   B CB   1 
ATOM   6003 O OG   . SER   B 1 128 ? 38.556 -26.621 4.645   1.00 16.68 ?  128 SER   B OG   1 
ATOM   6004 H H    . SER   B 1 128 ? 40.967 -26.380 2.503   1.00 17.94 ?  128 SER   B H    1 
ATOM   6005 H HA   . SER   B 1 128 ? 40.851 -27.571 4.177   1.00 19.04 ?  128 SER   B HA   1 
ATOM   6006 H HB2  . SER   B 1 128 ? 38.207 -28.134 3.426   1.00 19.53 ?  128 SER   B HB2  1 
ATOM   6007 H HB3  . SER   B 1 128 ? 38.828 -28.562 4.827   1.00 19.53 ?  128 SER   B HB3  1 
ATOM   6008 H HG   . SER   B 1 128 ? 39.128 -26.414 5.222   1.00 20.02 ?  128 SER   B HG   1 
ATOM   6009 N N    . ALA   B 1 129 ? 41.339 -29.554 2.024   1.00 18.24 ?  129 ALA   B N    1 
ATOM   6010 C CA   . ALA   B 1 129 ? 41.869 -30.860 1.678   1.00 19.29 ?  129 ALA   B CA   1 
ATOM   6011 C C    . ALA   B 1 129 ? 43.270 -31.032 2.254   1.00 18.16 ?  129 ALA   B C    1 
ATOM   6012 O O    . ALA   B 1 129 ? 43.833 -30.130 2.891   1.00 18.01 ?  129 ALA   B O    1 
ATOM   6013 C CB   . ALA   B 1 129 ? 41.902 -31.035 0.163   1.00 21.23 ?  129 ALA   B CB   1 
ATOM   6014 H H    . ALA   B 1 129 ? 41.450 -28.962 1.403   1.00 21.89 ?  129 ALA   B H    1 
ATOM   6015 H HA   . ALA   B 1 129 ? 41.301 -31.547 2.053   1.00 23.15 ?  129 ALA   B HA   1 
ATOM   6016 H HB1  . ALA   B 1 129 ? 42.244 -31.920 -0.048  1.00 25.48 ?  129 ALA   B HB1  1 
ATOM   6017 H HB2  . ALA   B 1 129 ? 41.002 -30.938 -0.184  1.00 25.48 ?  129 ALA   B HB2  1 
ATOM   6018 H HB3  . ALA   B 1 129 ? 42.480 -30.358 -0.223  1.00 25.48 ?  129 ALA   B HB3  1 
ATOM   6019 N N    . GLY   B 1 130 ? 43.845 -32.207 2.006   1.00 18.27 ?  130 GLY   B N    1 
ATOM   6020 C CA   . GLY   B 1 130 ? 45.238 -32.429 2.351   1.00 18.42 ?  130 GLY   B CA   1 
ATOM   6021 C C    . GLY   B 1 130 ? 45.451 -32.331 3.843   1.00 18.40 ?  130 GLY   B C    1 
ATOM   6022 O O    . GLY   B 1 130 ? 44.741 -32.961 4.640   1.00 19.26 ?  130 GLY   B O    1 
ATOM   6023 H H    . GLY   B 1 130 ? 43.456 -32.882 1.635   1.00 21.93 ?  130 GLY   B H    1 
ATOM   6024 H HA2  . GLY   B 1 130 ? 45.515 -33.311 2.051   1.00 22.11 ?  130 GLY   B HA2  1 
ATOM   6025 H HA3  . GLY   B 1 130 ? 45.795 -31.766 1.911   1.00 22.11 ?  130 GLY   B HA3  1 
ATOM   6026 N N    A ILE   B 1 131 ? 46.436 -31.520 4.236   0.48 18.59 ?  131 ILE   B N    1 
ATOM   6027 N N    B ILE   B 1 131 ? 46.433 -31.517 4.240   0.52 18.58 ?  131 ILE   B N    1 
ATOM   6028 C CA   A ILE   B 1 131 ? 46.785 -31.384 5.640   0.48 19.43 ?  131 ILE   B CA   1 
ATOM   6029 C CA   B ILE   B 1 131 ? 46.782 -31.389 5.646   0.52 19.48 ?  131 ILE   B CA   1 
ATOM   6030 C C    A ILE   B 1 131 ? 45.662 -30.785 6.472   0.48 19.11 ?  131 ILE   B C    1 
ATOM   6031 C C    B ILE   B 1 131 ? 45.662 -30.782 6.475   0.52 19.20 ?  131 ILE   B C    1 
ATOM   6032 O O    A ILE   B 1 131 ? 45.721 -30.849 7.703   0.48 20.60 ?  131 ILE   B O    1 
ATOM   6033 O O    B ILE   B 1 131 ? 45.724 -30.835 7.706   0.52 20.81 ?  131 ILE   B O    1 
ATOM   6034 C CB   A ILE   B 1 131 ? 48.105 -30.597 5.826   0.48 20.94 ?  131 ILE   B CB   1 
ATOM   6035 C CB   B ILE   B 1 131 ? 48.111 -30.619 5.842   0.52 20.99 ?  131 ILE   B CB   1 
ATOM   6036 C CG1  A ILE   B 1 131 ? 47.945 -29.133 5.397   0.48 21.70 ?  131 ILE   B CG1  1 
ATOM   6037 C CG1  B ILE   B 1 131 ? 47.952 -29.127 5.516   0.52 21.56 ?  131 ILE   B CG1  1 
ATOM   6038 C CG2  A ILE   B 1 131 ? 49.236 -31.265 5.051   0.48 21.92 ?  131 ILE   B CG2  1 
ATOM   6039 C CG2  B ILE   B 1 131 ? 49.221 -31.249 5.001   0.52 22.15 ?  131 ILE   B CG2  1 
ATOM   6040 C CD1  A ILE   B 1 131 ? 49.192 -28.288 5.613   0.48 22.48 ?  131 ILE   B CD1  1 
ATOM   6041 C CD1  B ILE   B 1 131 ? 49.162 -28.280 5.888   0.52 22.29 ?  131 ILE   B CD1  1 
ATOM   6042 H H    A ILE   B 1 131 ? 46.918 -31.044 3.705   0.48 22.31 ?  131 ILE   B H    1 
ATOM   6043 H H    B ILE   B 1 131 ? 46.910 -31.031 3.715   0.52 22.30 ?  131 ILE   B H    1 
ATOM   6044 H HA   A ILE   B 1 131 ? 46.942 -32.271 5.991   0.48 23.32 ?  131 ILE   B HA   1 
ATOM   6045 H HA   B ILE   B 1 131 ? 46.925 -32.277 5.998   0.52 23.38 ?  131 ILE   B HA   1 
ATOM   6046 H HB   A ILE   B 1 131 ? 48.334 -30.612 6.768   0.48 25.13 ?  131 ILE   B HB   1 
ATOM   6047 H HB   B ILE   B 1 131 ? 48.366 -30.693 6.774   0.52 25.19 ?  131 ILE   B HB   1 
ATOM   6048 H HG12 A ILE   B 1 131 ? 47.728 -29.106 4.453   0.48 26.04 ?  131 ILE   B HG12 1 
ATOM   6049 H HG12 B ILE   B 1 131 ? 47.802 -29.031 4.563   0.52 25.88 ?  131 ILE   B HG12 1 
ATOM   6050 H HG13 A ILE   B 1 131 ? 47.228 -28.729 5.911   0.48 26.04 ?  131 ILE   B HG13 1 
ATOM   6051 H HG13 B ILE   B 1 131 ? 47.192 -28.771 6.004   0.52 25.88 ?  131 ILE   B HG13 1 
ATOM   6052 H HG21 A ILE   B 1 131 ? 50.079 -30.869 5.319   0.48 26.32 ?  131 ILE   B HG21 1 
ATOM   6053 H HG21 B ILE   B 1 131 ? 50.069 -30.851 5.249   0.52 26.58 ?  131 ILE   B HG21 1 
ATOM   6054 H HG22 A ILE   B 1 131 ? 49.235 -32.212 5.251   0.48 26.32 ?  131 ILE   B HG22 1 
ATOM   6055 H HG22 B ILE   B 1 131 ? 49.240 -32.203 5.174   0.52 26.58 ?  131 ILE   B HG22 1 
ATOM   6056 H HG23 A ILE   B 1 131 ? 49.089 -31.126 4.102   0.48 26.32 ?  131 ILE   B HG23 1 
ATOM   6057 H HG23 B ILE   B 1 131 ? 49.038 -31.086 4.063   0.52 26.58 ?  131 ILE   B HG23 1 
ATOM   6058 H HD11 A ILE   B 1 131 ? 48.976 -27.358 5.442   0.48 26.98 ?  131 ILE   B HD11 1 
ATOM   6059 H HD11 B ILE   B 1 131 ? 48.956 -27.346 5.722   0.52 26.76 ?  131 ILE   B HD11 1 
ATOM   6060 H HD12 A ILE   B 1 131 ? 49.491 -28.395 6.530   0.48 26.98 ?  131 ILE   B HD12 1 
ATOM   6061 H HD12 B ILE   B 1 131 ? 49.364 -28.411 6.828   0.52 26.76 ?  131 ILE   B HD12 1 
ATOM   6062 H HD13 A ILE   B 1 131 ? 49.885 -28.584 5.003   0.48 26.98 ?  131 ILE   B HD13 1 
ATOM   6063 H HD13 B ILE   B 1 131 ? 49.918 -28.553 5.346   0.52 26.76 ?  131 ILE   B HD13 1 
ATOM   6064 N N    . PHE   B 1 132 ? 44.638 -30.204 5.836   1.00 17.92 ?  132 PHE   B N    1 
ATOM   6065 C CA   . PHE   B 1 132 ? 43.484 -29.687 6.565   1.00 18.08 ?  132 PHE   B CA   1 
ATOM   6066 C C    . PHE   B 1 132 ? 42.465 -30.770 6.922   1.00 19.66 ?  132 PHE   B C    1 
ATOM   6067 O O    . PHE   B 1 132 ? 41.578 -30.510 7.741   1.00 21.72 ?  132 PHE   B O    1 
ATOM   6068 C CB   . PHE   B 1 132 ? 42.796 -28.570 5.768   1.00 17.40 ?  132 PHE   B CB   1 
ATOM   6069 C CG   . PHE   B 1 132 ? 43.490 -27.226 5.854   1.00 16.78 ?  132 PHE   B CG   1 
ATOM   6070 C CD1  . PHE   B 1 132 ? 44.769 -27.052 5.357   1.00 18.30 ?  132 PHE   B CD1  1 
ATOM   6071 C CD2  . PHE   B 1 132 ? 42.839 -26.127 6.391   1.00 16.35 ?  132 PHE   B CD2  1 
ATOM   6072 C CE1  . PHE   B 1 132 ? 45.398 -25.806 5.425   1.00 19.29 ?  132 PHE   B CE1  1 
ATOM   6073 C CE2  . PHE   B 1 132 ? 43.457 -24.876 6.455   1.00 17.34 ?  132 PHE   B CE2  1 
ATOM   6074 C CZ   . PHE   B 1 132 ? 44.732 -24.725 5.976   1.00 18.43 ?  132 PHE   B CZ   1 
ATOM   6075 H H    A PHE   B 1 132 ? 44.588 -30.100 4.981   0.48 21.51 ?  132 PHE   B H    1 
ATOM   6076 H H    B PHE   B 1 132 ? 44.586 -30.107 4.980   0.52 21.51 ?  132 PHE   B H    1 
ATOM   6077 H HA   . PHE   B 1 132 ? 43.798 -29.297 7.394   1.00 21.70 ?  132 PHE   B HA   1 
ATOM   6078 H HB2  . PHE   B 1 132 ? 42.777 -28.826 4.835   1.00 20.88 ?  132 PHE   B HB2  1 
ATOM   6079 H HB3  . PHE   B 1 132 ? 41.893 -28.457 6.101   1.00 20.88 ?  132 PHE   B HB3  1 
ATOM   6080 H HD1  . PHE   B 1 132 ? 45.227 -27.774 4.987   1.00 21.97 ?  132 PHE   B HD1  1 
ATOM   6081 H HD2  . PHE   B 1 132 ? 41.976 -26.226 6.722   1.00 19.63 ?  132 PHE   B HD2  1 
ATOM   6082 H HE1  . PHE   B 1 132 ? 46.266 -25.702 5.098   1.00 23.16 ?  132 PHE   B HE1  1 
ATOM   6083 H HE2  . PHE   B 1 132 ? 43.007 -24.155 6.835   1.00 20.82 ?  132 PHE   B HE2  1 
ATOM   6084 H HZ   . PHE   B 1 132 ? 45.153 -23.892 6.024   1.00 22.13 ?  132 PHE   B HZ   1 
ATOM   6085 N N    . GLY   B 1 133 ? 42.546 -31.964 6.320   1.00 19.60 ?  133 GLY   B N    1 
ATOM   6086 C CA   . GLY   B 1 133 ? 41.842 -33.127 6.827   1.00 20.32 ?  133 GLY   B CA   1 
ATOM   6087 C C    . GLY   B 1 133 ? 40.457 -33.401 6.271   1.00 21.13 ?  133 GLY   B C    1 
ATOM   6088 O O    . GLY   B 1 133 ? 39.887 -34.441 6.604   1.00 23.02 ?  133 GLY   B O    1 
ATOM   6089 H H    . GLY   B 1 133 ? 43.012 -32.117 5.612   1.00 23.53 ?  133 GLY   B H    1 
ATOM   6090 H HA2  . GLY   B 1 133 ? 42.385 -33.912 6.659   1.00 24.39 ?  133 GLY   B HA2  1 
ATOM   6091 H HA3  . GLY   B 1 133 ? 41.749 -33.035 7.787   1.00 24.39 ?  133 GLY   B HA3  1 
ATOM   6092 N N    . ALA   B 1 134 ? 39.884 -32.521 5.458   1.00 20.30 ?  134 ALA   B N    1 
ATOM   6093 C CA   . ALA   B 1 134 ? 38.563 -32.799 4.913   1.00 20.12 ?  134 ALA   B CA   1 
ATOM   6094 C C    . ALA   B 1 134 ? 38.656 -33.783 3.753   1.00 20.18 ?  134 ALA   B C    1 
ATOM   6095 O O    . ALA   B 1 134 ? 39.712 -33.971 3.140   1.00 21.26 ?  134 ALA   B O    1 
ATOM   6096 C CB   . ALA   B 1 134 ? 37.887 -31.513 4.437   1.00 20.14 ?  134 ALA   B CB   1 
ATOM   6097 H H    . ALA   B 1 134 ? 40.227 -31.768 5.222   1.00 24.36 ?  134 ALA   B H    1 
ATOM   6098 H HA   . ALA   B 1 134 ? 38.008 -33.193 5.605   1.00 24.15 ?  134 ALA   B HA   1 
ATOM   6099 H HB1  . ALA   B 1 134 ? 36.998 -31.725 4.115   1.00 24.18 ?  134 ALA   B HB1  1 
ATOM   6100 H HB2  . ALA   B 1 134 ? 37.833 -30.892 5.180   1.00 24.18 ?  134 ALA   B HB2  1 
ATOM   6101 H HB3  . ALA   B 1 134 ? 38.415 -31.126 3.721   1.00 24.18 ?  134 ALA   B HB3  1 
ATOM   6102 N N    A ASP   B 1 135 ? 37.528 -34.415 3.458   0.48 20.59 ?  135 ASP   B N    1 
ATOM   6103 N N    B ASP   B 1 135 ? 37.529 -34.417 3.459   0.52 20.51 ?  135 ASP   B N    1 
ATOM   6104 C CA   A ASP   B 1 135 ? 37.427 -35.310 2.315   0.48 21.04 ?  135 ASP   B CA   1 
ATOM   6105 C CA   B ASP   B 1 135 ? 37.456 -35.316 2.322   0.52 20.85 ?  135 ASP   B CA   1 
ATOM   6106 C C    A ASP   B 1 135 ? 37.528 -34.486 1.038   0.48 20.11 ?  135 ASP   B C    1 
ATOM   6107 C C    B ASP   B 1 135 ? 37.537 -34.488 1.046   0.52 19.97 ?  135 ASP   B C    1 
ATOM   6108 O O    A ASP   B 1 135 ? 36.670 -33.623 0.803   0.48 19.84 ?  135 ASP   B O    1 
ATOM   6109 O O    B ASP   B 1 135 ? 36.675 -33.627 0.823   0.52 19.69 ?  135 ASP   B O    1 
ATOM   6110 C CB   A ASP   B 1 135 ? 36.074 -36.015 2.377   0.48 22.58 ?  135 ASP   B CB   1 
ATOM   6111 C CB   B ASP   B 1 135 ? 36.146 -36.093 2.364   0.52 22.24 ?  135 ASP   B CB   1 
ATOM   6112 C CG   A ASP   B 1 135 ? 35.839 -36.964 1.213   0.48 23.85 ?  135 ASP   B CG   1 
ATOM   6113 C CG   B ASP   B 1 135 ? 36.069 -37.168 1.292   0.52 23.48 ?  135 ASP   B CG   1 
ATOM   6114 O OD1  A ASP   B 1 135 ? 36.764 -37.166 0.396   0.48 24.30 ?  135 ASP   B OD1  1 
ATOM   6115 O OD1  B ASP   B 1 135 ? 36.862 -37.122 0.325   0.52 23.96 ?  135 ASP   B OD1  1 
ATOM   6116 O OD2  A ASP   B 1 135 ? 34.714 -37.506 1.114   0.48 24.98 -1 135 ASP   B OD2  1 
ATOM   6117 O OD2  B ASP   B 1 135 ? 35.215 -38.070 1.417   0.52 24.15 -1 135 ASP   B OD2  1 
ATOM   6118 H H    A ASP   B 1 135 ? 36.799 -34.340 3.907   0.48 24.71 ?  135 ASP   B H    1 
ATOM   6119 H H    B ASP   B 1 135 ? 36.795 -34.342 3.899   0.52 24.62 ?  135 ASP   B H    1 
ATOM   6120 H HA   A ASP   B 1 135 ? 38.135 -35.972 2.347   0.48 25.26 ?  135 ASP   B HA   1 
ATOM   6121 H HA   B ASP   B 1 135 ? 38.188 -35.947 2.357   0.52 25.03 ?  135 ASP   B HA   1 
ATOM   6122 H HB2  A ASP   B 1 135 ? 36.014 -36.501 3.217   0.48 27.11 ?  135 ASP   B HB2  1 
ATOM   6123 H HB2  B ASP   B 1 135 ? 36.067 -36.530 3.227   0.52 26.69 ?  135 ASP   B HB2  1 
ATOM   6124 H HB3  A ASP   B 1 135 ? 35.371 -35.354 2.326   0.48 27.11 ?  135 ASP   B HB3  1 
ATOM   6125 H HB3  B ASP   B 1 135 ? 35.406 -35.472 2.243   0.52 26.69 ?  135 ASP   B HB3  1 
ATOM   6126 N N    . PRO   B 1 136 ? 38.542 -34.697 0.195   1.00 20.07 ?  136 PRO   B N    1 
ATOM   6127 C CA   . PRO   B 1 136 ? 38.631 -33.888 -1.031  1.00 18.93 ?  136 PRO   B CA   1 
ATOM   6128 C C    . PRO   B 1 136 ? 37.430 -34.040 -1.943  1.00 17.79 ?  136 PRO   B C    1 
ATOM   6129 O O    . PRO   B 1 136 ? 37.106 -33.094 -2.669  1.00 16.69 ?  136 PRO   B O    1 
ATOM   6130 C CB   . PRO   B 1 136 ? 39.933 -34.372 -1.684  1.00 20.53 ?  136 PRO   B CB   1 
ATOM   6131 C CG   . PRO   B 1 136 ? 40.166 -35.740 -1.101  1.00 22.16 ?  136 PRO   B CG   1 
ATOM   6132 C CD   . PRO   B 1 136 ? 39.635 -35.679 0.296   1.00 21.69 ?  136 PRO   B CD   1 
ATOM   6133 H HA   . PRO   B 1 136 ? 38.721 -32.950 -0.812  1.00 22.72 ?  136 PRO   B HA   1 
ATOM   6134 H HB2  . PRO   B 1 136 ? 39.824 -34.426 -2.647  1.00 24.64 ?  136 PRO   B HB2  1 
ATOM   6135 H HB3  . PRO   B 1 136 ? 40.656 -33.771 -1.452  1.00 24.64 ?  136 PRO   B HB3  1 
ATOM   6136 H HG2  . PRO   B 1 136 ? 39.682 -36.408 -1.613  1.00 26.60 ?  136 PRO   B HG2  1 
ATOM   6137 H HG3  . PRO   B 1 136 ? 41.114 -35.940 -1.088  1.00 26.60 ?  136 PRO   B HG3  1 
ATOM   6138 H HD2  . PRO   B 1 136 ? 39.289 -36.544 0.567   1.00 26.03 ?  136 PRO   B HD2  1 
ATOM   6139 H HD3  . PRO   B 1 136 ? 40.312 -35.356 0.913   1.00 26.03 ?  136 PRO   B HD3  1 
ATOM   6140 N N    . ILE   B 1 137 ? 36.765 -35.201 -1.932  1.00 18.34 ?  137 ILE   B N    1 
ATOM   6141 C CA   . ILE   B 1 137 ? 35.542 -35.371 -2.713  1.00 18.66 ?  137 ILE   B CA   1 
ATOM   6142 C C    . ILE   B 1 137 ? 34.469 -34.401 -2.232  1.00 18.22 ?  137 ILE   B C    1 
ATOM   6143 O O    . ILE   B 1 137 ? 33.745 -33.794 -3.034  1.00 17.37 ?  137 ILE   B O    1 
ATOM   6144 C CB   . ILE   B 1 137 ? 35.069 -36.839 -2.646  1.00 20.59 ?  137 ILE   B CB   1 
ATOM   6145 C CG1  . ILE   B 1 137 ? 36.089 -37.756 -3.335  1.00 22.84 ?  137 ILE   B CG1  1 
ATOM   6146 C CG2  . ILE   B 1 137 ? 33.672 -36.982 -3.254  1.00 21.70 ?  137 ILE   B CG2  1 
ATOM   6147 C CD1  . ILE   B 1 137 ? 35.777 -39.229 -3.214  1.00 25.34 ?  137 ILE   B CD1  1 
ATOM   6148 H H    . ILE   B 1 137 ? 37.001 -35.902 -1.492  1.00 22.01 ?  137 ILE   B H    1 
ATOM   6149 H HA   . ILE   B 1 137 ? 35.729 -35.168 -3.646  1.00 22.40 ?  137 ILE   B HA   1 
ATOM   6150 H HB   . ILE   B 1 137 ? 35.014 -37.095 -1.717  1.00 24.71 ?  137 ILE   B HB   1 
ATOM   6151 H HG12 . ILE   B 1 137 ? 36.122 -37.539 -4.280  1.00 27.41 ?  137 ILE   B HG12 1 
ATOM   6152 H HG13 . ILE   B 1 137 ? 36.961 -37.607 -2.935  1.00 27.41 ?  137 ILE   B HG13 1 
ATOM   6153 H HG21 . ILE   B 1 137 ? 33.423 -37.918 -3.287  1.00 26.05 ?  137 ILE   B HG21 1 
ATOM   6154 H HG22 . ILE   B 1 137 ? 33.031 -36.505 -2.702  1.00 26.05 ?  137 ILE   B HG22 1 
ATOM   6155 H HG23 . ILE   B 1 137 ? 33.676 -36.611 -4.150  1.00 26.05 ?  137 ILE   B HG23 1 
ATOM   6156 H HD11 . ILE   B 1 137 ? 36.422 -39.718 -3.742  1.00 30.41 ?  137 ILE   B HD11 1 
ATOM   6157 H HD12 . ILE   B 1 137 ? 35.839 -39.493 -2.282  1.00 30.41 ?  137 ILE   B HD12 1 
ATOM   6158 H HD13 . ILE   B 1 137 ? 34.886 -39.406 -3.551  1.00 30.41 ?  137 ILE   B HD13 1 
ATOM   6159 N N    . HIS   B 1 138 ? 34.347 -34.246 -0.915  1.00 18.63 ?  138 HIS   B N    1 
ATOM   6160 C CA   . HIS   B 1 138 ? 33.400 -33.277 -0.378  1.00 18.98 ?  138 HIS   B CA   1 
ATOM   6161 C C    . HIS   B 1 138 ? 33.818 -31.850 -0.710  1.00 18.21 ?  138 HIS   B C    1 
ATOM   6162 O O    . HIS   B 1 138 ? 32.969 -31.001 -1.003  1.00 18.74 ?  138 HIS   B O    1 
ATOM   6163 C CB   . HIS   B 1 138 ? 33.291 -33.441 1.130   1.00 20.66 ?  138 HIS   B CB   1 
ATOM   6164 C CG   . HIS   B 1 138 ? 32.372 -32.453 1.768   1.00 22.34 ?  138 HIS   B CG   1 
ATOM   6165 N ND1  . HIS   B 1 138 ? 31.029 -32.389 1.466   1.00 24.04 ?  138 HIS   B ND1  1 
ATOM   6166 C CD2  . HIS   B 1 138 ? 32.604 -31.470 2.670   1.00 23.42 ?  138 HIS   B CD2  1 
ATOM   6167 C CE1  . HIS   B 1 138 ? 30.471 -31.415 2.162   1.00 24.32 ?  138 HIS   B CE1  1 
ATOM   6168 N NE2  . HIS   B 1 138 ? 31.403 -30.848 2.908   1.00 23.72 ?  138 HIS   B NE2  1 
ATOM   6169 H H    . HIS   B 1 138 ? 34.801 -34.682 -0.326  1.00 22.37 ?  138 HIS   B H    1 
ATOM   6170 H HA   . HIS   B 1 138 ? 32.528 -33.446 -0.770  1.00 22.78 ?  138 HIS   B HA   1 
ATOM   6171 H HB2  . HIS   B 1 138 ? 32.954 -34.329 1.325   1.00 24.80 ?  138 HIS   B HB2  1 
ATOM   6172 H HB3  . HIS   B 1 138 ? 34.170 -33.327 1.520   1.00 24.80 ?  138 HIS   B HB3  1 
ATOM   6173 H HD2  . HIS   B 1 138 ? 33.416 -31.266 3.067   1.00 28.11 ?  138 HIS   B HD2  1 
ATOM   6174 H HE1  . HIS   B 1 138 ? 29.570 -31.180 2.141   1.00 29.19 ?  138 HIS   B HE1  1 
ATOM   6175 H HE2  . HIS   B 1 138 ? 31.274 -30.193 3.450   1.00 28.47 ?  138 HIS   B HE2  1 
ATOM   6176 N N    . SER   B 1 139 ? 35.112 -31.553 -0.648  1.00 17.53 ?  139 SER   B N    1 
ATOM   6177 C CA   . SER   B 1 139 ? 35.549 -30.207 -0.985  1.00 16.79 ?  139 SER   B CA   1 
ATOM   6178 C C    . SER   B 1 139 ? 35.202 -29.866 -2.426  1.00 16.00 ?  139 SER   B C    1 
ATOM   6179 O O    . SER   B 1 139 ? 34.753 -28.751 -2.711  1.00 16.01 ?  139 SER   B O    1 
ATOM   6180 C CB   . SER   B 1 139 ? 37.041 -30.073 -0.727  1.00 17.07 ?  139 SER   B CB   1 
ATOM   6181 O OG   . SER   B 1 139 ? 37.444 -28.743 -0.991  1.00 17.29 ?  139 SER   B OG   1 
ATOM   6182 H H    . SER   B 1 139 ? 35.736 -32.093 -0.422  1.00 21.04 ?  139 SER   B H    1 
ATOM   6183 H HA   . SER   B 1 139 ? 35.083 -29.574 -0.419  1.00 20.15 ?  139 SER   B HA   1 
ATOM   6184 H HB2  . SER   B 1 139 ? 37.221 -30.279 0.203   1.00 20.49 ?  139 SER   B HB2  1 
ATOM   6185 H HB3  . SER   B 1 139 ? 37.525 -30.672 -1.309  1.00 20.49 ?  139 SER   B HB3  1 
ATOM   6186 H HG   . SER   B 1 139 ? 37.064 -28.210 -0.455  1.00 20.75 ?  139 SER   B HG   1 
ATOM   6187 N N    . LEU   B 1 140 ? 35.375 -30.823 -3.345  1.00 15.53 ?  140 LEU   B N    1 
ATOM   6188 C CA   . LEU   B 1 140 ? 35.017 -30.580 -4.736  1.00 15.71 ?  140 LEU   B CA   1 
ATOM   6189 C C    . LEU   B 1 140 ? 33.517 -30.351 -4.870  1.00 15.56 ?  140 LEU   B C    1 
ATOM   6190 O O    . LEU   B 1 140 ? 33.079 -29.471 -5.615  1.00 15.68 ?  140 LEU   B O    1 
ATOM   6191 C CB   . LEU   B 1 140 ? 35.485 -31.745 -5.611  1.00 15.78 ?  140 LEU   B CB   1 
ATOM   6192 C CG   . LEU   B 1 140 ? 35.138 -31.640 -7.086  1.00 16.37 ?  140 LEU   B CG   1 
ATOM   6193 C CD1  . LEU   B 1 140 ? 35.694 -30.365 -7.701  1.00 17.59 ?  140 LEU   B CD1  1 
ATOM   6194 C CD2  . LEU   B 1 140 ? 35.635 -32.883 -7.818  1.00 17.89 ?  140 LEU   B CD2  1 
ATOM   6195 H H    . LEU   B 1 140 ? 35.684 -31.609 -3.190  1.00 18.65 ?  140 LEU   B H    1 
ATOM   6196 H HA   . LEU   B 1 140 ? 35.476 -29.779 -5.043  1.00 18.86 ?  140 LEU   B HA   1 
ATOM   6197 H HB2  . LEU   B 1 140 ? 36.451 -31.812 -5.547  1.00 18.94 ?  140 LEU   B HB2  1 
ATOM   6198 H HB3  . LEU   B 1 140 ? 35.080 -32.559 -5.280  1.00 18.94 ?  140 LEU   B HB3  1 
ATOM   6199 H HG   . LEU   B 1 140 ? 34.177 -31.612 -7.179  1.00 19.65 ?  140 LEU   B HG   1 
ATOM   6200 H HD11 . LEU   B 1 140 ? 35.563 -30.397 -8.661  1.00 21.11 ?  140 LEU   B HD11 1 
ATOM   6201 H HD12 . LEU   B 1 140 ? 35.221 -29.604 -7.328  1.00 21.11 ?  140 LEU   B HD12 1 
ATOM   6202 H HD13 . LEU   B 1 140 ? 36.639 -30.301 -7.497  1.00 21.11 ?  140 LEU   B HD13 1 
ATOM   6203 H HD21 . LEU   B 1 140 ? 35.408 -32.804 -8.757  1.00 21.48 ?  140 LEU   B HD21 1 
ATOM   6204 H HD22 . LEU   B 1 140 ? 36.595 -32.950 -7.711  1.00 21.48 ?  140 LEU   B HD22 1 
ATOM   6205 H HD23 . LEU   B 1 140 ? 35.201 -33.662 -7.436  1.00 21.48 ?  140 LEU   B HD23 1 
ATOM   6206 N N    . ARG   B 1 141 ? 32.717 -31.136 -4.147  1.00 15.85 ?  141 ARG   B N    1 
ATOM   6207 C CA   . ARG   B 1 141 ? 31.268 -30.959 -4.123  1.00 17.14 ?  141 ARG   B CA   1 
ATOM   6208 C C    . ARG   B 1 141 ? 30.890 -29.547 -3.703  1.00 16.86 ?  141 ARG   B C    1 
ATOM   6209 O O    . ARG   B 1 141 ? 30.076 -28.881 -4.362  1.00 16.88 ?  141 ARG   B O    1 
ATOM   6210 C CB   . ARG   B 1 141 ? 30.686 -31.971 -3.135  1.00 18.49 ?  141 ARG   B CB   1 
ATOM   6211 C CG   . ARG   B 1 141 ? 29.213 -31.868 -2.848  1.00 20.07 ?  141 ARG   B CG   1 
ATOM   6212 C CD   . ARG   B 1 141 ? 28.444 -32.511 -3.929  1.00 21.38 ?  141 ARG   B CD   1 
ATOM   6213 N NE   . ARG   B 1 141 ? 28.177 -31.607 -5.035  1.00 21.40 ?  141 ARG   B NE   1 
ATOM   6214 C CZ   . ARG   B 1 141 ? 28.122 -31.978 -6.305  1.00 20.89 ?  141 ARG   B CZ   1 
ATOM   6215 N NH1  . ARG   B 1 141 ? 28.502 -33.187 -6.689  1.00 20.80 ?  141 ARG   B NH1  1 
ATOM   6216 N NH2  . ARG   B 1 141 ? 27.663 -31.122 -7.211  1.00 21.77 ?  141 ARG   B NH2  1 
ATOM   6217 H H    . ARG   B 1 141 ? 32.998 -31.778 -3.656  1.00 19.02 ?  141 ARG   B H    1 
ATOM   6218 H HA   . ARG   B 1 141 ? 30.901 -31.118 -5.001  1.00 20.58 ?  141 ARG   B HA   1 
ATOM   6219 H HB2  . ARG   B 1 141 ? 30.862 -32.858 -3.481  1.00 22.19 ?  141 ARG   B HB2  1 
ATOM   6220 H HB3  . ARG   B 1 141 ? 31.148 -31.865 -2.290  1.00 22.19 ?  141 ARG   B HB3  1 
ATOM   6221 H HG2  . ARG   B 1 141 ? 29.019 -32.317 -2.012  1.00 24.10 ?  141 ARG   B HG2  1 
ATOM   6222 H HG3  . ARG   B 1 141 ? 28.946 -30.931 -2.790  1.00 24.10 ?  141 ARG   B HG3  1 
ATOM   6223 H HD2  . ARG   B 1 141 ? 28.950 -33.275 -4.260  1.00 25.66 ?  141 ARG   B HD2  1 
ATOM   6224 H HD3  . ARG   B 1 141 ? 27.600 -32.813 -3.573  1.00 25.66 ?  141 ARG   B HD3  1 
ATOM   6225 H HE   . ARG   B 1 141 ? 28.106 -30.768 -4.856  1.00 25.69 ?  141 ARG   B HE   1 
ATOM   6226 H HH11 . ARG   B 1 141 ? 28.783 -33.762 -6.113  1.00 24.97 ?  141 ARG   B HH11 1 
ATOM   6227 H HH12 . ARG   B 1 141 ? 28.456 -33.406 -7.517  1.00 24.97 ?  141 ARG   B HH12 1 
ATOM   6228 H HH21 . ARG   B 1 141 ? 27.428 -30.330 -6.974  1.00 26.14 ?  141 ARG   B HH21 1 
ATOM   6229 H HH22 . ARG   B 1 141 ? 27.642 -31.347 -8.041  1.00 26.14 ?  141 ARG   B HH22 1 
ATOM   6230 N N    . VAL   B 1 142 ? 31.443 -29.090 -2.578  1.00 16.52 ?  142 VAL   B N    1 
ATOM   6231 C CA   . VAL   B 1 142 ? 31.113 -27.753 -2.102  1.00 16.32 ?  142 VAL   B CA   1 
ATOM   6232 C C    . VAL   B 1 142 ? 31.577 -26.706 -3.103  1.00 15.75 ?  142 VAL   B C    1 
ATOM   6233 O O    . VAL   B 1 142 ? 30.873 -25.725 -3.366  1.00 16.28 ?  142 VAL   B O    1 
ATOM   6234 C CB   . VAL   B 1 142 ? 31.666 -27.508 -0.687  1.00 17.47 ?  142 VAL   B CB   1 
ATOM   6235 C CG1  . VAL   B 1 142 ? 31.350 -26.091 -0.233  1.00 17.31 ?  142 VAL   B CG1  1 
ATOM   6236 C CG2  . VAL   B 1 142 ? 31.087 -28.527 0.284   1.00 17.43 ?  142 VAL   B CG2  1 
ATOM   6237 H H    . VAL   B 1 142 ? 32.003 -29.521 -2.081  1.00 19.83 ?  142 VAL   B H    1 
ATOM   6238 H HA   . VAL   B 1 142 ? 30.154 -27.680 -2.040  1.00 19.59 ?  142 VAL   B HA   1 
ATOM   6239 H HB   . VAL   B 1 142 ? 32.636 -27.611 -0.696  1.00 20.97 ?  142 VAL   B HB   1 
ATOM   6240 H HG11 . VAL   B 1 142 ? 31.529 -26.017 0.716   1.00 20.77 ?  142 VAL   B HG11 1 
ATOM   6241 H HG12 . VAL   B 1 142 ? 31.908 -25.466 -0.724  1.00 20.77 ?  142 VAL   B HG12 1 
ATOM   6242 H HG13 . VAL   B 1 142 ? 30.414 -25.909 -0.410  1.00 20.77 ?  142 VAL   B HG13 1 
ATOM   6243 H HG21 . VAL   B 1 142 ? 31.408 -28.330 1.178   1.00 20.92 ?  142 VAL   B HG21 1 
ATOM   6244 H HG22 . VAL   B 1 142 ? 30.121 -28.469 0.257   1.00 20.92 ?  142 VAL   B HG22 1 
ATOM   6245 H HG23 . VAL   B 1 142 ? 31.375 -29.415 0.018   1.00 20.92 ?  142 VAL   B HG23 1 
ATOM   6246 N N    . CYS   B 1 143 ? 32.760 -26.899 -3.686  1.00 15.30 ?  143 CYS   B N    1 
ATOM   6247 C CA   . CYS   B 1 143 ? 33.254 -25.965 -4.692  1.00 15.27 ?  143 CYS   B CA   1 
ATOM   6248 C C    . CYS   B 1 143 ? 32.253 -25.828 -5.832  1.00 15.18 ?  143 CYS   B C    1 
ATOM   6249 O O    . CYS   B 1 143 ? 31.852 -24.718 -6.203  1.00 15.76 ?  143 CYS   B O    1 
ATOM   6250 C CB   . CYS   B 1 143 ? 34.608 -26.456 -5.215  1.00 15.88 ?  143 CYS   B CB   1 
ATOM   6251 S SG   . CYS   B 1 143 ? 35.354 -25.368 -6.454  1.00 16.23 ?  143 CYS   B SG   1 
ATOM   6252 H H    . CYS   B 1 143 ? 33.297 -27.542 -3.510  1.00 18.36 ?  143 CYS   B H    1 
ATOM   6253 H HA   . CYS   B 1 143 ? 33.391 -25.086 -4.293  1.00 18.34 ?  143 CYS   B HA   1 
ATOM   6254 H HB2  . CYS   B 1 143 ? 35.230 -26.534 -4.473  1.00 19.06 ?  143 CYS   B HB2  1 
ATOM   6255 H HB3  . CYS   B 1 143 ? 34.484 -27.328 -5.622  1.00 19.06 ?  143 CYS   B HB3  1 
ATOM   6256 H HG   . CYS   B 1 143 ? 36.426 -25.809 -6.779  1.00 19.49 ?  143 CYS   B HG   1 
ATOM   6257 N N    . VAL   B 1 144 ? 31.844 -26.957 -6.405  1.00 16.15 ?  144 VAL   B N    1 
ATOM   6258 C CA   . VAL   B 1 144 ? 30.941 -26.912 -7.548  1.00 16.99 ?  144 VAL   B CA   1 
ATOM   6259 C C    . VAL   B 1 144 ? 29.603 -26.284 -7.172  1.00 16.98 ?  144 VAL   B C    1 
ATOM   6260 O O    . VAL   B 1 144 ? 28.989 -25.574 -7.979  1.00 18.23 ?  144 VAL   B O    1 
ATOM   6261 C CB   . VAL   B 1 144 ? 30.760 -28.330 -8.102  1.00 19.13 ?  144 VAL   B CB   1 
ATOM   6262 C CG1  . VAL   B 1 144 ? 29.478 -28.446 -8.926  1.00 21.23 ?  144 VAL   B CG1  1 
ATOM   6263 C CG2  . VAL   B 1 144 ? 31.994 -28.753 -8.890  1.00 19.38 ?  144 VAL   B CG2  1 
ATOM   6264 H H    . VAL   B 1 144 ? 32.072 -27.745 -6.156  1.00 19.39 ?  144 VAL   B H    1 
ATOM   6265 H HA   . VAL   B 1 144 ? 31.331 -26.366 -8.245  1.00 20.40 ?  144 VAL   B HA   1 
ATOM   6266 H HB   . VAL   B 1 144 ? 30.672 -28.944 -7.354  1.00 22.96 ?  144 VAL   B HB   1 
ATOM   6267 H HG11 . VAL   B 1 144 ? 29.535 -29.237 -9.483  1.00 25.48 ?  144 VAL   B HG11 1 
ATOM   6268 H HG12 . VAL   B 1 144 ? 28.720 -28.523 -8.324  1.00 25.48 ?  144 VAL   B HG12 1 
ATOM   6269 H HG13 . VAL   B 1 144 ? 29.387 -27.657 -9.481  1.00 25.48 ?  144 VAL   B HG13 1 
ATOM   6270 H HG21 . VAL   B 1 144 ? 31.858 -29.654 -9.230  1.00 23.26 ?  144 VAL   B HG21 1 
ATOM   6271 H HG22 . VAL   B 1 144 ? 32.120 -28.139 -9.631  1.00 23.26 ?  144 VAL   B HG22 1 
ATOM   6272 H HG23 . VAL   B 1 144 ? 32.764 -28.733 -8.305  1.00 23.26 ?  144 VAL   B HG23 1 
ATOM   6273 N N    . ASP   B 1 145 ? 29.127 -26.539 -5.954  1.00 17.21 ?  145 ASP   B N    1 
ATOM   6274 C CA   . ASP   B 1 145 ? 27.821 -26.050 -5.531  1.00 17.98 ?  145 ASP   B CA   1 
ATOM   6275 C C    . ASP   B 1 145 ? 27.859 -24.622 -5.005  1.00 17.71 ?  145 ASP   B C    1 
ATOM   6276 O O    . ASP   B 1 145 ? 26.799 -24.078 -4.672  1.00 19.52 ?  145 ASP   B O    1 
ATOM   6277 C CB   . ASP   B 1 145 ? 27.238 -26.956 -4.440  1.00 20.23 ?  145 ASP   B CB   1 
ATOM   6278 C CG   . ASP   B 1 145 ? 26.889 -28.342 -4.938  1.00 22.34 ?  145 ASP   B CG   1 
ATOM   6279 O OD1  . ASP   B 1 145 ? 26.774 -28.540 -6.166  1.00 22.95 ?  145 ASP   B OD1  1 
ATOM   6280 O OD2  . ASP   B 1 145 ? 26.724 -29.231 -4.080  1.00 24.46 -1 145 ASP   B OD2  1 
ATOM   6281 H H    . ASP   B 1 145 ? 29.548 -26.988 -5.351  1.00 20.66 ?  145 ASP   B H    1 
ATOM   6282 H HA   . ASP   B 1 145 ? 27.221 -26.067 -6.291  1.00 21.58 ?  145 ASP   B HA   1 
ATOM   6283 H HB2  . ASP   B 1 145 ? 27.883 -27.059 -3.732  1.00 24.29 ?  145 ASP   B HB2  1 
ATOM   6284 H HB3  . ASP   B 1 145 ? 26.423 -26.552 -4.099  1.00 24.29 ?  145 ASP   B HB3  1 
ATOM   6285 N N    . THR   B 1 146 ? 29.031 -24.006 -4.920  1.00 15.75 ?  146 THR   B N    1 
ATOM   6286 C CA   . THR   B 1 146 ? 29.164 -22.682 -4.322  1.00 15.68 ?  146 THR   B CA   1 
ATOM   6287 C C    . THR   B 1 146 ? 29.792 -21.659 -5.250  1.00 15.60 ?  146 THR   B C    1 
ATOM   6288 O O    . THR   B 1 146 ? 29.344 -20.500 -5.295  1.00 15.75 ?  146 THR   B O    1 
ATOM   6289 C CB   . THR   B 1 146 ? 30.010 -22.775 -3.045  1.00 15.84 ?  146 THR   B CB   1 
ATOM   6290 O OG1  . THR   B 1 146 ? 29.438 -23.749 -2.166  1.00 15.97 ?  146 THR   B OG1  1 
ATOM   6291 C CG2  . THR   B 1 146 ? 30.096 -21.429 -2.344  1.00 16.12 ?  146 THR   B CG2  1 
ATOM   6292 H H    . THR   B 1 146 ? 29.778 -24.333 -5.204  1.00 18.91 ?  146 THR   B H    1 
ATOM   6293 H HA   . THR   B 1 146 ? 28.292 -22.348 -4.080  1.00 18.83 ?  146 THR   B HA   1 
ATOM   6294 H HB   . THR   B 1 146 ? 30.915 -23.038 -3.277  1.00 19.01 ?  146 THR   B HB   1 
ATOM   6295 H HG1  . THR   B 1 146 ? 29.462 -24.512 -2.531  1.00 19.17 ?  146 THR   B HG1  1 
ATOM   6296 H HG21 . THR   B 1 146 ? 30.442 -21.543 -1.447  1.00 19.35 ?  146 THR   B HG21 1 
ATOM   6297 H HG22 . THR   B 1 146 ? 30.689 -20.833 -2.834  1.00 19.35 ?  146 THR   B HG22 1 
ATOM   6298 H HG23 . THR   B 1 146 ? 29.216 -21.025 -2.295  1.00 19.35 ?  146 THR   B HG23 1 
ATOM   6299 N N    . VAL   B 1 147 ? 30.851 -22.039 -5.961  1.00 15.34 ?  147 VAL   B N    1 
ATOM   6300 C CA   . VAL   B 1 147 ? 31.580 -21.104 -6.804  1.00 15.25 ?  147 VAL   B CA   1 
ATOM   6301 C C    . VAL   B 1 147 ? 30.844 -20.971 -8.125  1.00 14.96 ?  147 VAL   B C    1 
ATOM   6302 O O    . VAL   B 1 147 ? 30.460 -21.974 -8.742  1.00 16.01 ?  147 VAL   B O    1 
ATOM   6303 C CB   . VAL   B 1 147 ? 33.028 -21.573 -7.010  1.00 15.11 ?  147 VAL   B CB   1 
ATOM   6304 C CG1  . VAL   B 1 147 ? 33.792 -20.555 -7.837  1.00 15.11 ?  147 VAL   B CG1  1 
ATOM   6305 C CG2  . VAL   B 1 147 ? 33.709 -21.782 -5.668  1.00 15.00 ?  147 VAL   B CG2  1 
ATOM   6306 H H    . VAL   B 1 147 ? 31.163 -22.839 -5.979  1.00 18.42 ?  147 VAL   B H    1 
ATOM   6307 H HA   . VAL   B 1 147 ? 31.604 -20.232 -6.377  1.00 18.30 ?  147 VAL   B HA   1 
ATOM   6308 H HB   . VAL   B 1 147 ? 33.030 -22.420 -7.489  1.00 18.14 ?  147 VAL   B HB   1 
ATOM   6309 H HG11 . VAL   B 1 147 ? 34.737 -20.781 -7.824  1.00 18.14 ?  147 VAL   B HG11 1 
ATOM   6310 H HG12 . VAL   B 1 147 ? 33.463 -20.567 -8.746  1.00 18.14 ?  147 VAL   B HG12 1 
ATOM   6311 H HG13 . VAL   B 1 147 ? 33.663 -19.674 -7.447  1.00 18.14 ?  147 VAL   B HG13 1 
ATOM   6312 H HG21 . VAL   B 1 147 ? 34.646 -21.987 -5.816  1.00 18.00 ?  147 VAL   B HG21 1 
ATOM   6313 H HG22 . VAL   B 1 147 ? 33.628 -20.969 -5.145  1.00 18.00 ?  147 VAL   B HG22 1 
ATOM   6314 H HG23 . VAL   B 1 147 ? 33.280 -22.518 -5.204  1.00 18.00 ?  147 VAL   B HG23 1 
ATOM   6315 N N    . ARG   B 1 148 ? 30.644 -19.725 -8.552  1.00 15.33 ?  148 ARG   B N    1 
ATOM   6316 C CA   . ARG   B 1 148 ? 30.015 -19.405 -9.823  1.00 15.33 ?  148 ARG   B CA   1 
ATOM   6317 C C    . ARG   B 1 148 ? 30.971 -18.737 -10.798 1.00 14.89 ?  148 ARG   B C    1 
ATOM   6318 O O    . ARG   B 1 148 ? 30.681 -18.701 -11.996 1.00 16.97 ?  148 ARG   B O    1 
ATOM   6319 C CB   . ARG   B 1 148 ? 28.786 -18.510 -9.594  1.00 15.63 ?  148 ARG   B CB   1 
ATOM   6320 C CG   . ARG   B 1 148 ? 27.705 -19.213 -8.767  1.00 16.65 ?  148 ARG   B CG   1 
ATOM   6321 C CD   . ARG   B 1 148 ? 26.502 -18.322 -8.478  1.00 17.52 ?  148 ARG   B CD   1 
ATOM   6322 N NE   . ARG   B 1 148 ? 26.892 -17.126 -7.742  1.00 17.78 ?  148 ARG   B NE   1 
ATOM   6323 C CZ   . ARG   B 1 148 ? 27.197 -17.099 -6.450  1.00 17.09 ?  148 ARG   B CZ   1 
ATOM   6324 N NH1  . ARG   B 1 148 ? 27.129 -18.186 -5.698  1.00 17.00 ?  148 ARG   B NH1  1 
ATOM   6325 N NH2  . ARG   B 1 148 ? 27.600 -15.956 -5.903  1.00 17.26 ?  148 ARG   B NH2  1 
ATOM   6326 H H    . ARG   B 1 148 ? 30.880 -19.021 -8.104  1.00 18.40 ?  148 ARG   B H    1 
ATOM   6327 H HA   . ARG   B 1 148 ? 29.708 -20.227 -10.229 1.00 18.40 ?  148 ARG   B HA   1 
ATOM   6328 H HB2  . ARG   B 1 148 ? 29.052 -17.710 -9.119  1.00 18.76 ?  148 ARG   B HB2  1 
ATOM   6329 H HB3  . ARG   B 1 148 ? 28.396 -18.278 -10.452 1.00 18.76 ?  148 ARG   B HB3  1 
ATOM   6330 H HG2  . ARG   B 1 148 ? 27.394 -19.994 -9.252  1.00 19.99 ?  148 ARG   B HG2  1 
ATOM   6331 H HG3  . ARG   B 1 148 ? 28.089 -19.485 -7.916  1.00 19.99 ?  148 ARG   B HG3  1 
ATOM   6332 H HD2  . ARG   B 1 148 ? 26.103 -18.047 -9.318  1.00 21.03 ?  148 ARG   B HD2  1 
ATOM   6333 H HD3  . ARG   B 1 148 ? 25.860 -18.816 -7.945  1.00 21.03 ?  148 ARG   B HD3  1 
ATOM   6334 H HE   . ARG   B 1 148 ? 26.937 -16.389 -8.175  1.00 21.35 ?  148 ARG   B HE   1 
ATOM   6335 H HH11 . ARG   B 1 148 ? 26.866 -18.937 -6.038  1.00 20.41 ?  148 ARG   B HH11 1 
ATOM   6336 H HH12 . ARG   B 1 148 ? 27.326 -18.151 -4.861  1.00 20.41 ?  148 ARG   B HH12 1 
ATOM   6337 H HH21 . ARG   B 1 148 ? 27.661 -15.250 -6.381  1.00 20.71 ?  148 ARG   B HH21 1 
ATOM   6338 H HH22 . ARG   B 1 148 ? 27.805 -15.930 -5.066  1.00 20.71 ?  148 ARG   B HH22 1 
ATOM   6339 N N    . THR   B 1 149 ? 32.079 -18.186 -10.312 1.00 15.43 ?  149 THR   B N    1 
ATOM   6340 C CA   . THR   B 1 149 ? 33.120 -17.635 -11.165 1.00 15.22 ?  149 THR   B CA   1 
ATOM   6341 C C    . THR   B 1 149 ? 34.000 -18.781 -11.677 1.00 14.90 ?  149 THR   B C    1 
ATOM   6342 O O    . THR   B 1 149 ? 33.808 -19.952 -11.331 1.00 15.13 ?  149 THR   B O    1 
ATOM   6343 C CB   . THR   B 1 149 ? 33.904 -16.586 -10.387 1.00 15.38 ?  149 THR   B CB   1 
ATOM   6344 O OG1  . THR   B 1 149 ? 34.373 -17.195 -9.184  1.00 15.45 ?  149 THR   B OG1  1 
ATOM   6345 C CG2  . THR   B 1 149 ? 33.023 -15.378 -10.058 1.00 16.27 ?  149 THR   B CG2  1 
ATOM   6346 H H    . THR   B 1 149 ? 32.243 -18.112 -9.474  1.00 18.52 ?  149 THR   B H    1 
ATOM   6347 H HA   . THR   B 1 149 ? 32.706 -17.201 -11.931 1.00 18.27 ?  149 THR   B HA   1 
ATOM   6348 H HB   . THR   B 1 149 ? 34.655 -16.291 -10.917 1.00 18.47 ?  149 THR   B HB   1 
ATOM   6349 H HG1  . THR   B 1 149 ? 34.810 -16.636 -8.727  1.00 18.54 ?  149 THR   B HG1  1 
ATOM   6350 H HG21 . THR   B 1 149 ? 33.541 -14.716 -9.572  1.00 19.53 ?  149 THR   B HG21 1 
ATOM   6351 H HG22 . THR   B 1 149 ? 32.688 -14.979 -10.874 1.00 19.53 ?  149 THR   B HG22 1 
ATOM   6352 H HG23 . THR   B 1 149 ? 32.271 -15.652 -9.508  1.00 19.53 ?  149 THR   B HG23 1 
ATOM   6353 N N    . ASN   B 1 150 ? 34.958 -18.466 -12.539 1.00 14.81 ?  150 ASN   B N    1 
ATOM   6354 C CA   . ASN   B 1 150 ? 35.725 -19.500 -13.227 1.00 15.38 ?  150 ASN   B CA   1 
ATOM   6355 C C    . ASN   B 1 150 ? 36.893 -19.939 -12.357 1.00 14.70 ?  150 ASN   B C    1 
ATOM   6356 O O    . ASN   B 1 150 ? 37.828 -19.166 -12.115 1.00 15.20 ?  150 ASN   B O    1 
ATOM   6357 C CB   . ASN   B 1 150 ? 36.198 -19.007 -14.586 1.00 17.28 ?  150 ASN   B CB   1 
ATOM   6358 C CG   . ASN   B 1 150 ? 35.055 -18.770 -15.525 1.00 20.17 ?  150 ASN   B CG   1 
ATOM   6359 O OD1  . ASN   B 1 150 ? 34.121 -19.563 -15.583 1.00 21.34 ?  150 ASN   B OD1  1 
ATOM   6360 N ND2  . ASN   B 1 150 ? 35.091 -17.659 -16.237 1.00 22.24 ?  150 ASN   B ND2  1 
ATOM   6361 H H    . ASN   B 1 150 ? 35.173 -17.662 -12.755 1.00 17.79 ?  150 ASN   B H    1 
ATOM   6362 H HA   . ASN   B 1 150 ? 35.148 -20.271 -13.370 1.00 18.46 ?  150 ASN   B HA   1 
ATOM   6363 H HB2  . ASN   B 1 150 ? 36.673 -18.176 -14.473 1.00 20.75 ?  150 ASN   B HB2  1 
ATOM   6364 H HB3  . ASN   B 1 150 ? 36.776 -19.681 -14.978 1.00 20.75 ?  150 ASN   B HB3  1 
ATOM   6365 H HD21 . ASN   B 1 150 ? 34.458 -17.478 -16.793 1.00 26.70 ?  150 ASN   B HD21 1 
ATOM   6366 H HD22 . ASN   B 1 150 ? 35.760 -17.123 -16.163 1.00 26.70 ?  150 ASN   B HD22 1 
ATOM   6367 N N    . VAL   B 1 151 ? 36.841 -21.179 -11.885 1.00 14.80 ?  151 VAL   B N    1 
ATOM   6368 C CA   . VAL   B 1 151 ? 37.862 -21.705 -10.991 1.00 15.09 ?  151 VAL   B CA   1 
ATOM   6369 C C    . VAL   B 1 151 ? 38.562 -22.882 -11.657 1.00 14.62 ?  151 VAL   B C    1 
ATOM   6370 O O    . VAL   B 1 151 ? 37.916 -23.812 -12.163 1.00 15.67 ?  151 VAL   B O    1 
ATOM   6371 C CB   . VAL   B 1 151 ? 37.305 -22.032 -9.588  1.00 15.69 ?  151 VAL   B CB   1 
ATOM   6372 C CG1  . VAL   B 1 151 ? 36.154 -23.030 -9.652  1.00 17.23 ?  151 VAL   B CG1  1 
ATOM   6373 C CG2  . VAL   B 1 151 ? 38.418 -22.516 -8.667  1.00 16.04 ?  151 VAL   B CG2  1 
ATOM   6374 H H    . VAL   B 1 151 ? 36.210 -21.743 -12.068 1.00 17.77 ?  151 VAL   B H    1 
ATOM   6375 H HA   . VAL   B 1 151 ? 38.527 -21.015 -10.865 1.00 18.12 ?  151 VAL   B HA   1 
ATOM   6376 H HB   . VAL   B 1 151 ? 36.951 -21.213 -9.202  1.00 18.83 ?  151 VAL   B HB   1 
ATOM   6377 H HG11 . VAL   B 1 151 ? 35.840 -23.211 -8.751  1.00 20.68 ?  151 VAL   B HG11 1 
ATOM   6378 H HG12 . VAL   B 1 151 ? 35.435 -22.655 -10.182 1.00 20.68 ?  151 VAL   B HG12 1 
ATOM   6379 H HG13 . VAL   B 1 151 ? 36.471 -23.853 -10.059 1.00 20.68 ?  151 VAL   B HG13 1 
ATOM   6380 H HG21 . VAL   B 1 151 ? 38.066 -22.592 -7.765  1.00 19.26 ?  151 VAL   B HG21 1 
ATOM   6381 H HG22 . VAL   B 1 151 ? 38.730 -23.378 -8.974  1.00 19.26 ?  151 VAL   B HG22 1 
ATOM   6382 H HG23 . VAL   B 1 151 ? 39.142 -21.871 -8.684  1.00 19.26 ?  151 VAL   B HG23 1 
ATOM   6383 N N    . TYR   B 1 152 ? 39.890 -22.802 -11.677 1.00 14.08 ?  152 TYR   B N    1 
ATOM   6384 C CA   . TYR   B 1 152 ? 40.786 -23.794 -12.248 1.00 14.33 ?  152 TYR   B CA   1 
ATOM   6385 C C    . TYR   B 1 152 ? 41.503 -24.465 -11.082 1.00 13.64 ?  152 TYR   B C    1 
ATOM   6386 O O    . TYR   B 1 152 ? 42.351 -23.846 -10.431 1.00 13.71 ?  152 TYR   B O    1 
ATOM   6387 C CB   . TYR   B 1 152 ? 41.759 -23.099 -13.201 1.00 15.37 ?  152 TYR   B CB   1 
ATOM   6388 C CG   . TYR   B 1 152 ? 41.077 -22.627 -14.466 1.00 15.98 ?  152 TYR   B CG   1 
ATOM   6389 C CD1  . TYR   B 1 152 ? 40.440 -21.387 -14.530 1.00 16.40 ?  152 TYR   B CD1  1 
ATOM   6390 C CD2  . TYR   B 1 152 ? 41.043 -23.440 -15.588 1.00 17.35 ?  152 TYR   B CD2  1 
ATOM   6391 C CE1  . TYR   B 1 152 ? 39.799 -20.976 -15.680 1.00 18.05 ?  152 TYR   B CE1  1 
ATOM   6392 C CE2  . TYR   B 1 152 ? 40.406 -23.038 -16.740 1.00 18.62 ?  152 TYR   B CE2  1 
ATOM   6393 C CZ   . TYR   B 1 152 ? 39.789 -21.804 -16.783 1.00 18.26 ?  152 TYR   B CZ   1 
ATOM   6394 O OH   . TYR   B 1 152 ? 39.162 -21.407 -17.937 1.00 20.90 ?  152 TYR   B OH   1 
ATOM   6395 H H    . TYR   B 1 152 ? 40.320 -22.133 -11.339 1.00 16.90 ?  152 TYR   B H    1 
ATOM   6396 H HA   . TYR   B 1 152 ? 40.276 -24.461 -12.732 1.00 17.21 ?  152 TYR   B HA   1 
ATOM   6397 H HB2  . TYR   B 1 152 ? 42.142 -22.329 -12.753 1.00 18.46 ?  152 TYR   B HB2  1 
ATOM   6398 H HB3  . TYR   B 1 152 ? 42.459 -23.723 -13.447 1.00 18.46 ?  152 TYR   B HB3  1 
ATOM   6399 H HD1  . TYR   B 1 152 ? 40.446 -20.832 -13.780 1.00 19.68 ?  152 TYR   B HD1  1 
ATOM   6400 H HD2  . TYR   B 1 152 ? 41.450 -24.276 -15.560 1.00 20.82 ?  152 TYR   B HD2  1 
ATOM   6401 H HE1  . TYR   B 1 152 ? 39.382 -20.143 -15.714 1.00 21.67 ?  152 TYR   B HE1  1 
ATOM   6402 H HE2  . TYR   B 1 152 ? 40.390 -23.591 -17.490 1.00 22.35 ?  152 TYR   B HE2  1 
ATOM   6403 H HH   . TYR   B 1 152 ? 39.230 -22.000 -18.528 1.00 25.09 ?  152 TYR   B HH   1 
ATOM   6404 N N    . LEU   B 1 153 ? 41.137 -25.717 -10.809 1.00 13.29 ?  153 LEU   B N    1 
ATOM   6405 C CA   . LEU   B 1 153 ? 41.655 -26.468 -9.677  1.00 13.52 ?  153 LEU   B CA   1 
ATOM   6406 C C    . LEU   B 1 153 ? 42.884 -27.269 -10.084 1.00 13.75 ?  153 LEU   B C    1 
ATOM   6407 O O    . LEU   B 1 153 ? 42.857 -28.003 -11.076 1.00 14.78 ?  153 LEU   B O    1 
ATOM   6408 C CB   . LEU   B 1 153 ? 40.576 -27.418 -9.158  1.00 14.20 ?  153 LEU   B CB   1 
ATOM   6409 C CG   . LEU   B 1 153 ? 39.320 -26.748 -8.599  1.00 14.62 ?  153 LEU   B CG   1 
ATOM   6410 C CD1  . LEU   B 1 153 ? 38.210 -27.780 -8.438  1.00 15.46 ?  153 LEU   B CD1  1 
ATOM   6411 C CD2  . LEU   B 1 153 ? 39.626 -26.081 -7.263  1.00 15.76 ?  153 LEU   B CD2  1 
ATOM   6412 H H    . LEU   B 1 153 ? 40.557 -26.155 -11.273 1.00 15.96 ?  153 LEU   B H    1 
ATOM   6413 H HA   . LEU   B 1 153 ? 41.888 -25.853 -8.962  1.00 16.23 ?  153 LEU   B HA   1 
ATOM   6414 H HB2  . LEU   B 1 153 ? 40.292 -27.993 -9.884  1.00 17.05 ?  153 LEU   B HB2  1 
ATOM   6415 H HB3  . LEU   B 1 153 ? 40.953 -27.956 -8.444  1.00 17.05 ?  153 LEU   B HB3  1 
ATOM   6416 H HG   . LEU   B 1 153 ? 39.010 -26.062 -9.214  1.00 17.55 ?  153 LEU   B HG   1 
ATOM   6417 H HD11 . LEU   B 1 153 ? 37.406 -27.331 -8.125  1.00 18.56 ?  153 LEU   B HD11 1 
ATOM   6418 H HD12 . LEU   B 1 153 ? 38.045 -28.196 -9.293  1.00 18.56 ?  153 LEU   B HD12 1 
ATOM   6419 H HD13 . LEU   B 1 153 ? 38.492 -28.441 -7.789  1.00 18.56 ?  153 LEU   B HD13 1 
ATOM   6420 H HD21 . LEU   B 1 153 ? 38.813 -25.704 -6.893  1.00 18.93 ?  153 LEU   B HD21 1 
ATOM   6421 H HD22 . LEU   B 1 153 ? 39.992 -26.742 -6.653  1.00 18.93 ?  153 LEU   B HD22 1 
ATOM   6422 H HD23 . LEU   B 1 153 ? 40.280 -25.372 -7.405  1.00 18.93 ?  153 LEU   B HD23 1 
ATOM   6423 N N    . ALA   B 1 154 ? 43.941 -27.152 -9.291  1.00 13.93 ?  154 ALA   B N    1 
ATOM   6424 C CA   . ALA   B 1 154 ? 45.170 -27.910 -9.474  1.00 15.68 ?  154 ALA   B CA   1 
ATOM   6425 C C    . ALA   B 1 154 ? 45.251 -28.976 -8.392  1.00 16.56 ?  154 ALA   B C    1 
ATOM   6426 O O    . ALA   B 1 154 ? 45.223 -28.663 -7.194  1.00 18.22 ?  154 ALA   B O    1 
ATOM   6427 C CB   . ALA   B 1 154 ? 46.392 -26.995 -9.417  1.00 16.43 ?  154 ALA   B CB   1 
ATOM   6428 H H    . ALA   B 1 154 ? 43.967 -26.610 -8.620  1.00 16.72 ?  154 ALA   B H    1 
ATOM   6429 H HA   . ALA   B 1 154 ? 45.153 -28.343 -10.338 1.00 18.82 ?  154 ALA   B HA   1 
ATOM   6430 H HB1  . ALA   B 1 154 ? 47.191 -27.526 -9.539  1.00 19.72 ?  154 ALA   B HB1  1 
ATOM   6431 H HB2  . ALA   B 1 154 ? 46.325 -26.328 -10.122 1.00 19.72 ?  154 ALA   B HB2  1 
ATOM   6432 H HB3  . ALA   B 1 154 ? 46.418 -26.551 -8.552  1.00 19.72 ?  154 ALA   B HB3  1 
ATOM   6433 N N    . VAL   B 1 155 ? 45.343 -30.230 -8.816  1.00 15.29 ?  155 VAL   B N    1 
ATOM   6434 C CA   . VAL   B 1 155 ? 45.447 -31.370 -7.915  1.00 15.85 ?  155 VAL   B CA   1 
ATOM   6435 C C    . VAL   B 1 155 ? 46.774 -32.053 -8.204  1.00 15.74 ?  155 VAL   B C    1 
ATOM   6436 O O    . VAL   B 1 155 ? 46.993 -32.560 -9.312  1.00 17.62 ?  155 VAL   B O    1 
ATOM   6437 C CB   . VAL   B 1 155 ? 44.277 -32.348 -8.093  1.00 17.37 ?  155 VAL   B CB   1 
ATOM   6438 C CG1  . VAL   B 1 155 ? 44.475 -33.569 -7.207  1.00 17.45 ?  155 VAL   B CG1  1 
ATOM   6439 C CG2  . VAL   B 1 155 ? 42.954 -31.645 -7.782  1.00 18.90 ?  155 VAL   B CG2  1 
ATOM   6440 H H    . VAL   B 1 155 ? 45.341 -30.452 -9.647  1.00 18.36 ?  155 VAL   B H    1 
ATOM   6441 H HA   . VAL   B 1 155 ? 45.449 -31.062 -6.997  1.00 19.03 ?  155 VAL   B HA   1 
ATOM   6442 H HB   . VAL   B 1 155 ? 44.246 -32.646 -9.016  1.00 20.85 ?  155 VAL   B HB   1 
ATOM   6443 H HG11 . VAL   B 1 155 ? 43.640 -34.061 -7.147  1.00 20.95 ?  155 VAL   B HG11 1 
ATOM   6444 H HG12 . VAL   B 1 155 ? 45.161 -34.141 -7.596  1.00 20.95 ?  155 VAL   B HG12 1 
ATOM   6445 H HG13 . VAL   B 1 155 ? 44.751 -33.282 -6.322  1.00 20.95 ?  155 VAL   B HG13 1 
ATOM   6446 H HG21 . VAL   B 1 155 ? 42.234 -32.293 -7.846  1.00 22.69 ?  155 VAL   B HG21 1 
ATOM   6447 H HG22 . VAL   B 1 155 ? 42.998 -31.289 -6.880  1.00 22.69 ?  155 VAL   B HG22 1 
ATOM   6448 H HG23 . VAL   B 1 155 ? 42.821 -30.931 -8.418  1.00 22.69 ?  155 VAL   B HG23 1 
ATOM   6449 N N    . PHE   B 1 156 ? 47.649 -32.088 -7.200  1.00 16.31 ?  156 PHE   B N    1 
ATOM   6450 C CA   . PHE   B 1 156 ? 49.018 -32.556 -7.413  1.00 17.44 ?  156 PHE   B CA   1 
ATOM   6451 C C    . PHE   B 1 156 ? 49.094 -34.062 -7.663  1.00 19.21 ?  156 PHE   B C    1 
ATOM   6452 O O    . PHE   B 1 156 ? 49.787 -34.519 -8.583  1.00 21.36 ?  156 PHE   B O    1 
ATOM   6453 C CB   . PHE   B 1 156 ? 49.862 -32.175 -6.203  1.00 17.30 ?  156 PHE   B CB   1 
ATOM   6454 C CG   . PHE   B 1 156 ? 51.282 -32.647 -6.277  1.00 18.19 ?  156 PHE   B CG   1 
ATOM   6455 C CD1  . PHE   B 1 156 ? 52.133 -32.187 -7.271  1.00 20.10 ?  156 PHE   B CD1  1 
ATOM   6456 C CD2  . PHE   B 1 156 ? 51.777 -33.533 -5.338  1.00 19.16 ?  156 PHE   B CD2  1 
ATOM   6457 C CE1  . PHE   B 1 156 ? 53.453 -32.611 -7.334  1.00 21.20 ?  156 PHE   B CE1  1 
ATOM   6458 C CE2  . PHE   B 1 156 ? 53.092 -33.950 -5.393  1.00 20.03 ?  156 PHE   B CE2  1 
ATOM   6459 C CZ   . PHE   B 1 156 ? 53.926 -33.494 -6.398  1.00 20.35 ?  156 PHE   B CZ   1 
ATOM   6460 H H    . PHE   B 1 156 ? 47.475 -31.855 -6.392  1.00 19.58 ?  156 PHE   B H    1 
ATOM   6461 H HA   . PHE   B 1 156 ? 49.383 -32.106 -8.189  1.00 20.94 ?  156 PHE   B HA   1 
ATOM   6462 H HB2  . PHE   B 1 156 ? 49.878 -31.207 -6.131  1.00 20.77 ?  156 PHE   B HB2  1 
ATOM   6463 H HB3  . PHE   B 1 156 ? 49.464 -32.558 -5.408  1.00 20.77 ?  156 PHE   B HB3  1 
ATOM   6464 H HD1  . PHE   B 1 156 ? 51.813 -31.590 -7.909  1.00 24.13 ?  156 PHE   B HD1  1 
ATOM   6465 H HD2  . PHE   B 1 156 ? 51.220 -33.844 -4.661  1.00 23.00 ?  156 PHE   B HD2  1 
ATOM   6466 H HE1  . PHE   B 1 156 ? 54.015 -32.303 -8.009  1.00 25.45 ?  156 PHE   B HE1  1 
ATOM   6467 H HE2  . PHE   B 1 156 ? 53.419 -34.556 -4.761  1.00 24.04 ?  156 PHE   B HE2  1 
ATOM   6468 H HZ   . PHE   B 1 156 ? 54.815 -33.786 -6.436  1.00 24.42 ?  156 PHE   B HZ   1 
ATOM   6469 N N    . ASP   B 1 157 ? 48.440 -34.858 -6.830  1.00 19.38 ?  157 ASP   B N    1 
ATOM   6470 C CA   . ASP   B 1 157 ? 48.578 -36.308 -6.905  1.00 21.14 ?  157 ASP   B CA   1 
ATOM   6471 C C    . ASP   B 1 157 ? 47.670 -36.870 -7.993  1.00 21.30 ?  157 ASP   B C    1 
ATOM   6472 O O    . ASP   B 1 157 ? 46.446 -36.752 -7.895  1.00 20.81 ?  157 ASP   B O    1 
ATOM   6473 C CB   . ASP   B 1 157 ? 48.202 -36.902 -5.555  1.00 22.50 ?  157 ASP   B CB   1 
ATOM   6474 C CG   . ASP   B 1 157 ? 48.371 -38.412 -5.512  1.00 24.91 ?  157 ASP   B CG   1 
ATOM   6475 O OD1  . ASP   B 1 157 ? 48.706 -39.024 -6.555  1.00 25.56 ?  157 ASP   B OD1  1 
ATOM   6476 O OD2  . ASP   B 1 157 ? 48.181 -38.987 -4.423  1.00 27.11 -1 157 ASP   B OD2  1 
ATOM   6477 H H    . ASP   B 1 157 ? 47.912 -34.586 -6.216  1.00 23.27 ?  157 ASP   B H    1 
ATOM   6478 H HA   . ASP   B 1 157 ? 49.494 -36.547 -7.113  1.00 25.37 ?  157 ASP   B HA   1 
ATOM   6479 H HB2  . ASP   B 1 157 ? 48.762 -36.503 -4.877  1.00 27.01 ?  157 ASP   B HB2  1 
ATOM   6480 H HB3  . ASP   B 1 157 ? 47.266 -36.703 -5.373  1.00 27.01 ?  157 ASP   B HB3  1 
ATOM   6481 N N    . LYS   B 1 158 ? 48.266 -37.525 -9.001  1.00 22.92 ?  158 LYS   B N    1 
ATOM   6482 C CA   . LYS   B 1 158 ? 47.497 -38.141 -10.089 1.00 24.19 ?  158 LYS   B CA   1 
ATOM   6483 C C    . LYS   B 1 158 ? 46.425 -39.096 -9.566  1.00 23.46 ?  158 LYS   B C    1 
ATOM   6484 O O    . LYS   B 1 158 ? 45.325 -39.181 -10.126 1.00 23.83 ?  158 LYS   B O    1 
ATOM   6485 C CB   . LYS   B 1 158 ? 48.450 -38.874 -11.044 1.00 26.46 ?  158 LYS   B CB   1 
ATOM   6486 C CG   . LYS   B 1 158 ? 47.778 -39.802 -12.048 1.00 29.09 ?  158 LYS   B CG   1 
ATOM   6487 C CD   . LYS   B 1 158 ? 46.918 -39.046 -13.043 1.00 31.21 ?  158 LYS   B CD   1 
ATOM   6488 C CE   . LYS   B 1 158 ? 46.312 -39.992 -14.071 1.00 33.13 ?  158 LYS   B CE   1 
ATOM   6489 N NZ   . LYS   B 1 158 ? 45.232 -39.348 -14.873 1.00 34.05 ?  158 LYS   B NZ   1 
ATOM   6490 H H    . LYS   B 1 158 ? 49.119 -37.628 -9.080  1.00 27.52 ?  158 LYS   B H    1 
ATOM   6491 H HA   . LYS   B 1 158 ? 47.057 -37.441 -10.603 1.00 29.04 ?  158 LYS   B HA   1 
ATOM   6492 H HB2  . LYS   B 1 158 ? 48.952 -38.212 -11.556 1.00 31.76 ?  158 LYS   B HB2  1 
ATOM   6493 H HB3  . LYS   B 1 158 ? 49.068 -39.406 -10.520 1.00 31.76 ?  158 LYS   B HB3  1 
ATOM   6494 H HG2  . LYS   B 1 158 ? 48.468 -40.269 -12.547 1.00 34.91 ?  158 LYS   B HG2  1 
ATOM   6495 H HG3  . LYS   B 1 158 ? 47.223 -40.449 -11.585 1.00 34.91 ?  158 LYS   B HG3  1 
ATOM   6496 H HD2  . LYS   B 1 158 ? 46.197 -38.601 -12.573 1.00 37.45 ?  158 LYS   B HD2  1 
ATOM   6497 H HD3  . LYS   B 1 158 ? 47.466 -38.397 -13.513 1.00 37.45 ?  158 LYS   B HD3  1 
ATOM   6498 H HE2  . LYS   B 1 158 ? 47.006 -40.284 -14.682 1.00 39.77 ?  158 LYS   B HE2  1 
ATOM   6499 H HE3  . LYS   B 1 158 ? 45.931 -40.758 -13.613 1.00 39.77 ?  158 LYS   B HE3  1 
ATOM   6500 H HZ1  . LYS   B 1 158 ? 44.902 -39.928 -15.462 1.00 40.87 ?  158 LYS   B HZ1  1 
ATOM   6501 H HZ2  . LYS   B 1 158 ? 44.576 -39.074 -14.338 1.00 40.87 ?  158 LYS   B HZ2  1 
ATOM   6502 H HZ3  . LYS   B 1 158 ? 45.558 -38.645 -15.312 1.00 40.87 ?  158 LYS   B HZ3  1 
ATOM   6503 N N    . ASN   B 1 159 ? 46.732 -39.842 -8.505  1.00 23.24 ?  159 ASN   B N    1 
ATOM   6504 C CA   . ASN   B 1 159 ? 45.768 -40.811 -7.992  1.00 24.58 ?  159 ASN   B CA   1 
ATOM   6505 C C    . ASN   B 1 159 ? 44.581 -40.122 -7.319  1.00 22.90 ?  159 ASN   B C    1 
ATOM   6506 O O    . ASN   B 1 159 ? 43.445 -40.606 -7.404  1.00 22.89 ?  159 ASN   B O    1 
ATOM   6507 C CB   . ASN   B 1 159 ? 46.465 -41.770 -7.036  1.00 27.93 ?  159 ASN   B CB   1 
ATOM   6508 C CG   . ASN   B 1 159 ? 47.496 -42.626 -7.733  1.00 31.26 ?  159 ASN   B CG   1 
ATOM   6509 O OD1  . ASN   B 1 159 ? 47.278 -43.076 -8.861  1.00 31.63 ?  159 ASN   B OD1  1 
ATOM   6510 N ND2  . ASN   B 1 159 ? 48.636 -42.846 -7.074  1.00 33.07 ?  159 ASN   B ND2  1 
ATOM   6511 H H    . ASN   B 1 159 ? 47.475 -39.797 -8.084  1.00 27.89 ?  159 ASN   B H    1 
ATOM   6512 H HA   . ASN   B 1 159 ? 45.433 -41.332 -8.743  1.00 29.50 ?  159 ASN   B HA   1 
ATOM   6513 H HB2  . ASN   B 1 159 ? 46.916 -41.262 -6.346  1.00 33.52 ?  159 ASN   B HB2  1 
ATOM   6514 H HB3  . ASN   B 1 159 ? 45.809 -42.362 -6.650  1.00 33.52 ?  159 ASN   B HB3  1 
ATOM   6515 H HD21 . ASN   B 1 159 ? 49.260 -43.325 -7.427  1.00 39.69 ?  159 ASN   B HD21 1 
ATOM   6516 H HD22 . ASN   B 1 159 ? 48.749 -42.515 -6.286  1.00 39.69 ?  159 ASN   B HD22 1 
ATOM   6517 N N    . LEU   B 1 160 ? 44.814 -38.998 -6.639  1.00 22.25 ?  160 LEU   B N    1 
ATOM   6518 C CA   . LEU   B 1 160 ? 43.690 -38.243 -6.100  1.00 20.99 ?  160 LEU   B CA   1 
ATOM   6519 C C    . LEU   B 1 160 ? 42.896 -37.591 -7.220  1.00 20.13 ?  160 LEU   B C    1 
ATOM   6520 O O    . LEU   B 1 160 ? 41.658 -37.595 -7.194  1.00 20.08 ?  160 LEU   B O    1 
ATOM   6521 C CB   . LEU   B 1 160 ? 44.179 -37.195 -5.101  1.00 20.82 ?  160 LEU   B CB   1 
ATOM   6522 C CG   . LEU   B 1 160 ? 43.053 -36.296 -4.565  1.00 20.59 ?  160 LEU   B CG   1 
ATOM   6523 C CD1  . LEU   B 1 160 ? 41.940 -37.120 -3.942  1.00 21.84 ?  160 LEU   B CD1  1 
ATOM   6524 C CD2  . LEU   B 1 160 ? 43.611 -35.302 -3.563  1.00 20.49 ?  160 LEU   B CD2  1 
ATOM   6525 H H    . LEU   B 1 160 ? 45.596 -38.665 -6.489  1.00 26.71 ?  160 LEU   B H    1 
ATOM   6526 H HA   . LEU   B 1 160 ? 43.106 -38.860 -5.641  1.00 25.19 ?  160 LEU   B HA   1 
ATOM   6527 H HB2  . LEU   B 1 160 ? 44.589 -37.652 -4.349  1.00 25.00 ?  160 LEU   B HB2  1 
ATOM   6528 H HB3  . LEU   B 1 160 ? 44.839 -36.630 -5.539  1.00 25.00 ?  160 LEU   B HB3  1 
ATOM   6529 H HG   . LEU   B 1 160 ? 42.680 -35.795 -5.305  1.00 24.72 ?  160 LEU   B HG   1 
ATOM   6530 H HD11 . LEU   B 1 160 ? 41.335 -36.527 -3.482  1.00 26.22 ?  160 LEU   B HD11 1 
ATOM   6531 H HD12 . LEU   B 1 160 ? 41.470 -37.604 -4.641  1.00 26.22 ?  160 LEU   B HD12 1 
ATOM   6532 H HD13 . LEU   B 1 160 ? 42.331 -37.753 -3.313  1.00 26.22 ?  160 LEU   B HD13 1 
ATOM   6533 H HD21 . LEU   B 1 160 ? 42.895 -34.714 -3.284  1.00 24.60 ?  160 LEU   B HD21 1 
ATOM   6534 H HD22 . LEU   B 1 160 ? 43.962 -35.789 -2.802  1.00 24.60 ?  160 LEU   B HD22 1 
ATOM   6535 H HD23 . LEU   B 1 160 ? 44.318 -34.791 -3.987  1.00 24.60 ?  160 LEU   B HD23 1 
ATOM   6536 N N    . TYR   B 1 161 ? 43.593 -37.023 -8.212  1.00 20.44 ?  161 TYR   B N    1 
ATOM   6537 C CA   . TYR   B 1 161 ? 42.917 -36.466 -9.379  1.00 20.29 ?  161 TYR   B CA   1 
ATOM   6538 C C    . TYR   B 1 161 ? 41.975 -37.494 -9.987  1.00 20.00 ?  161 TYR   B C    1 
ATOM   6539 O O    . TYR   B 1 161 ? 40.803 -37.200 -10.243 1.00 19.86 ?  161 TYR   B O    1 
ATOM   6540 C CB   . TYR   B 1 161 ? 43.951 -35.996 -10.412 1.00 20.71 ?  161 TYR   B CB   1 
ATOM   6541 C CG   . TYR   B 1 161 ? 43.368 -35.537 -11.733 1.00 21.40 ?  161 TYR   B CG   1 
ATOM   6542 C CD1  . TYR   B 1 161 ? 42.973 -34.215 -11.917 1.00 21.09 ?  161 TYR   B CD1  1 
ATOM   6543 C CD2  . TYR   B 1 161 ? 43.206 -36.422 -12.797 1.00 21.89 ?  161 TYR   B CD2  1 
ATOM   6544 C CE1  . TYR   B 1 161 ? 42.440 -33.789 -13.114 1.00 22.79 ?  161 TYR   B CE1  1 
ATOM   6545 C CE2  . TYR   B 1 161 ? 42.670 -36.002 -14.001 1.00 23.22 ?  161 TYR   B CE2  1 
ATOM   6546 C CZ   . TYR   B 1 161 ? 42.290 -34.683 -14.151 1.00 23.39 ?  161 TYR   B CZ   1 
ATOM   6547 O OH   . TYR   B 1 161 ? 41.752 -34.245 -15.340 1.00 25.91 ?  161 TYR   B OH   1 
ATOM   6548 H H    . TYR   B 1 161 ? 44.448 -36.963 -8.244  1.00 24.54 ?  161 TYR   B H    1 
ATOM   6549 H HA   . TYR   B 1 161 ? 42.390 -35.700 -9.110  1.00 24.36 ?  161 TYR   B HA   1 
ATOM   6550 H HB2  . TYR   B 1 161 ? 44.442 -35.245 -10.041 1.00 24.86 ?  161 TYR   B HB2  1 
ATOM   6551 H HB3  . TYR   B 1 161 ? 44.559 -36.722 -10.605 1.00 24.86 ?  161 TYR   B HB3  1 
ATOM   6552 H HD1  . TYR   B 1 161 ? 43.070 -33.599 -11.226 1.00 25.31 ?  161 TYR   B HD1  1 
ATOM   6553 H HD2  . TYR   B 1 161 ? 43.458 -37.309 -12.701 1.00 26.27 ?  161 TYR   B HD2  1 
ATOM   6554 H HE1  . TYR   B 1 161 ? 42.180 -32.896 -13.223 1.00 27.36 ?  161 TYR   B HE1  1 
ATOM   6555 H HE2  . TYR   B 1 161 ? 42.564 -36.601 -14.707 1.00 27.87 ?  161 TYR   B HE2  1 
ATOM   6556 H HH   . TYR   B 1 161 ? 41.715 -34.877 -15.894 1.00 31.10 ?  161 TYR   B HH   1 
ATOM   6557 N N    . ASP   B 1 162 ? 42.472 -38.716 -10.202 1.00 20.91 ?  162 ASP   B N    1 
ATOM   6558 C CA   . ASP   B 1 162 ? 41.649 -39.764 -10.797 1.00 21.00 ?  162 ASP   B CA   1 
ATOM   6559 C C    . ASP   B 1 162 ? 40.439 -40.084 -9.927  1.00 20.27 ?  162 ASP   B C    1 
ATOM   6560 O O    . ASP   B 1 162 ? 39.329 -40.280 -10.440 1.00 20.79 ?  162 ASP   B O    1 
ATOM   6561 C CB   . ASP   B 1 162 ? 42.487 -41.025 -11.020 1.00 22.70 ?  162 ASP   B CB   1 
ATOM   6562 C CG   . ASP   B 1 162 ? 43.481 -40.884 -12.151 1.00 24.17 ?  162 ASP   B CG   1 
ATOM   6563 O OD1  . ASP   B 1 162 ? 43.363 -39.953 -12.969 1.00 24.99 ?  162 ASP   B OD1  1 
ATOM   6564 O OD2  . ASP   B 1 162 ? 44.380 -41.744 -12.238 1.00 26.08 -1 162 ASP   B OD2  1 
ATOM   6565 H H    . ASP   B 1 162 ? 43.277 -38.952 -10.022 1.00 25.10 ?  162 ASP   B H    1 
ATOM   6566 H HA   . ASP   B 1 162 ? 41.329 -39.466 -11.661 1.00 25.21 ?  162 ASP   B HA   1 
ATOM   6567 H HB2  . ASP   B 1 162 ? 42.991 -41.223 -10.218 1.00 27.25 ?  162 ASP   B HB2  1 
ATOM   6568 H HB3  . ASP   B 1 162 ? 41.905 -41.762 -11.246 1.00 27.25 ?  162 ASP   B HB3  1 
ATOM   6569 N N    A LYS   B 1 163 ? 40.629 -40.155 -8.608  0.48 19.55 ?  163 LYS   B N    1 
ATOM   6570 N N    B LYS   B 1 163 ? 40.630 -40.147 -8.607  0.52 19.43 ?  163 LYS   B N    1 
ATOM   6571 C CA   A LYS   B 1 163 ? 39.498 -40.414 -7.724  0.48 20.04 ?  163 LYS   B CA   1 
ATOM   6572 C CA   B LYS   B 1 163 ? 39.507 -40.410 -7.712  0.52 19.90 ?  163 LYS   B CA   1 
ATOM   6573 C C    A LYS   B 1 163 ? 38.465 -39.294 -7.808  0.48 18.84 ?  163 LYS   B C    1 
ATOM   6574 C C    B LYS   B 1 163 ? 38.469 -39.294 -7.778  0.52 18.78 ?  163 LYS   B C    1 
ATOM   6575 O O    A LYS   B 1 163 ? 37.253 -39.554 -7.818  0.48 19.09 ?  163 LYS   B O    1 
ATOM   6576 O O    B LYS   B 1 163 ? 37.258 -39.555 -7.739  0.52 19.13 ?  163 LYS   B O    1 
ATOM   6577 C CB   A LYS   B 1 163 ? 39.976 -40.585 -6.283  0.48 22.47 ?  163 LYS   B CB   1 
ATOM   6578 C CB   B LYS   B 1 163 ? 40.007 -40.576 -6.279  0.52 22.35 ?  163 LYS   B CB   1 
ATOM   6579 C CG   A LYS   B 1 163 ? 38.900 -41.147 -5.369  0.48 26.15 ?  163 LYS   B CG   1 
ATOM   6580 C CG   B LYS   B 1 163 ? 38.933 -41.052 -5.321  0.52 26.20 ?  163 LYS   B CG   1 
ATOM   6581 C CD   A LYS   B 1 163 ? 39.312 -41.144 -3.909  0.48 29.32 ?  163 LYS   B CD   1 
ATOM   6582 C CD   B LYS   B 1 163 ? 39.456 -41.224 -3.906  0.52 29.65 ?  163 LYS   B CD   1 
ATOM   6583 C CE   A LYS   B 1 163 ? 38.264 -41.845 -3.057  0.48 31.52 ?  163 LYS   B CE   1 
ATOM   6584 C CE   B LYS   B 1 163 ? 38.401 -41.869 -3.019  0.52 32.07 ?  163 LYS   B CE   1 
ATOM   6585 N NZ   A LYS   B 1 163 ? 38.328 -41.432 -1.629  0.48 32.83 ?  163 LYS   B NZ   1 
ATOM   6586 N NZ   B LYS   B 1 163 ? 38.695 -41.698 -1.570  0.52 33.55 ?  163 LYS   B NZ   1 
ATOM   6587 H H    A LYS   B 1 163 ? 41.391 -40.069 -8.215  0.48 23.46 ?  163 LYS   B H    1 
ATOM   6588 H H    B LYS   B 1 163 ? 41.392 -40.055 -8.218  0.52 23.33 ?  163 LYS   B H    1 
ATOM   6589 H HA   A LYS   B 1 163 ? 39.073 -41.243 -7.998  0.48 24.06 ?  163 LYS   B HA   1 
ATOM   6590 H HA   B LYS   B 1 163 ? 39.081 -41.241 -7.980  0.52 23.89 ?  163 LYS   B HA   1 
ATOM   6591 H HB2  A LYS   B 1 163 ? 40.731 -41.198 -6.269  0.48 26.97 ?  163 LYS   B HB2  1 
ATOM   6592 H HB2  B LYS   B 1 163 ? 40.727 -41.228 -6.269  0.52 26.83 ?  163 LYS   B HB2  1 
ATOM   6593 H HB3  A LYS   B 1 163 ? 40.245 -39.722 -5.936  0.48 26.97 ?  163 LYS   B HB3  1 
ATOM   6594 H HB3  B LYS   B 1 163 ? 40.334 -39.721 -5.961  0.52 26.83 ?  163 LYS   B HB3  1 
ATOM   6595 H HG2  A LYS   B 1 163 ? 38.098 -40.610 -5.455  0.48 31.39 ?  163 LYS   B HG2  1 
ATOM   6596 H HG2  B LYS   B 1 163 ? 38.214 -40.403 -5.297  0.52 31.45 ?  163 LYS   B HG2  1 
ATOM   6597 H HG3  A LYS   B 1 163 ? 38.715 -42.065 -5.625  0.48 31.39 ?  163 LYS   B HG3  1 
ATOM   6598 H HG3  B LYS   B 1 163 ? 38.596 -41.912 -5.622  0.52 31.45 ?  163 LYS   B HG3  1 
ATOM   6599 H HD2  A LYS   B 1 163 ? 40.154 -41.615 -3.808  0.48 35.19 ?  163 LYS   B HD2  1 
ATOM   6600 H HD2  B LYS   B 1 163 ? 40.239 -41.798 -3.918  0.52 35.59 ?  163 LYS   B HD2  1 
ATOM   6601 H HD3  A LYS   B 1 163 ? 39.397 -40.229 -3.598  0.48 35.19 ?  163 LYS   B HD3  1 
ATOM   6602 H HD3  B LYS   B 1 163 ? 39.679 -40.355 -3.537  0.52 35.59 ?  163 LYS   B HD3  1 
ATOM   6603 H HE2  A LYS   B 1 163 ? 37.380 -41.635 -3.397  0.48 37.83 ?  163 LYS   B HE2  1 
ATOM   6604 H HE2  B LYS   B 1 163 ? 37.538 -41.466 -3.204  0.52 38.50 ?  163 LYS   B HE2  1 
ATOM   6605 H HE3  A LYS   B 1 163 ? 38.413 -42.802 -3.099  0.48 37.83 ?  163 LYS   B HE3  1 
ATOM   6606 H HE3  B LYS   B 1 163 ? 38.368 -42.819 -3.210  0.52 38.50 ?  163 LYS   B HE3  1 
ATOM   6607 H HZ1  A LYS   B 1 163 ? 37.702 -41.859 -1.162  0.48 39.41 ?  163 LYS   B HZ1  1 
ATOM   6608 H HZ1  B LYS   B 1 163 ? 38.058 -42.086 -1.084  0.52 40.27 ?  163 LYS   B HZ1  1 
ATOM   6609 H HZ2  A LYS   B 1 163 ? 39.127 -41.629 -1.292  0.48 39.41 ?  163 LYS   B HZ2  1 
ATOM   6610 H HZ2  B LYS   B 1 163 ? 39.477 -42.072 -1.374  0.52 40.27 ?  163 LYS   B HZ2  1 
ATOM   6611 H HZ3  A LYS   B 1 163 ? 38.191 -40.555 -1.561  0.48 39.41 ?  163 LYS   B HZ3  1 
ATOM   6612 H HZ3  B LYS   B 1 163 ? 38.727 -40.832 -1.367  0.52 40.27 ?  163 LYS   B HZ3  1 
ATOM   6613 N N    . LEU   B 1 164 ? 38.927 -38.043 -7.866  1.00 17.84 ?  164 LEU   B N    1 
ATOM   6614 C CA   . LEU   B 1 164 ? 38.017 -36.903 -7.922  1.00 17.61 ?  164 LEU   B CA   1 
ATOM   6615 C C    . LEU   B 1 164 ? 37.232 -36.889 -9.225  1.00 18.41 ?  164 LEU   B C    1 
ATOM   6616 O O    . LEU   B 1 164 ? 36.010 -36.688 -9.221  1.00 19.83 ?  164 LEU   B O    1 
ATOM   6617 C CB   . LEU   B 1 164 ? 38.818 -35.611 -7.773  1.00 17.01 ?  164 LEU   B CB   1 
ATOM   6618 C CG   . LEU   B 1 164 ? 39.350 -35.317 -6.373  1.00 17.58 ?  164 LEU   B CG   1 
ATOM   6619 C CD1  . LEU   B 1 164 ? 40.414 -34.240 -6.443  1.00 18.22 ?  164 LEU   B CD1  1 
ATOM   6620 C CD2  . LEU   B 1 164 ? 38.228 -34.899 -5.435  1.00 18.94 ?  164 LEU   B CD2  1 
ATOM   6621 H H    A LEU   B 1 164 ? 39.764 -37.833 -7.877  0.48 21.42 ?  164 LEU   B H    1 
ATOM   6622 H H    B LEU   B 1 164 ? 39.764 -37.833 -7.895  0.52 21.42 ?  164 LEU   B H    1 
ATOM   6623 H HA   . LEU   B 1 164 ? 37.386 -36.966 -7.198  1.00 21.14 ?  164 LEU   B HA   1 
ATOM   6624 H HB2  . LEU   B 1 164 ? 39.585 -35.659 -8.370  1.00 20.42 ?  164 LEU   B HB2  1 
ATOM   6625 H HB3  . LEU   B 1 164 ? 38.253 -34.873 -8.033  1.00 20.42 ?  164 LEU   B HB3  1 
ATOM   6626 H HG   . LEU   B 1 164 ? 39.761 -36.119 -6.017  1.00 21.10 ?  164 LEU   B HG   1 
ATOM   6627 H HD11 . LEU   B 1 164 ? 40.732 -34.051 -5.547  1.00 21.87 ?  164 LEU   B HD11 1 
ATOM   6628 H HD12 . LEU   B 1 164 ? 41.147 -34.550 -6.997  1.00 21.87 ?  164 LEU   B HD12 1 
ATOM   6629 H HD13 . LEU   B 1 164 ? 40.026 -33.436 -6.830  1.00 21.87 ?  164 LEU   B HD13 1 
ATOM   6630 H HD21 . LEU   B 1 164 ? 38.608 -34.668 -4.575  1.00 22.74 ?  164 LEU   B HD21 1 
ATOM   6631 H HD22 . LEU   B 1 164 ? 37.768 -34.135 -5.813  1.00 22.74 ?  164 LEU   B HD22 1 
ATOM   6632 H HD23 . LEU   B 1 164 ? 37.609 -35.641 -5.335  1.00 22.74 ?  164 LEU   B HD23 1 
ATOM   6633 N N    . VAL   B 1 165 ? 37.920 -37.094 -10.352 1.00 19.87 ?  165 VAL   B N    1 
ATOM   6634 C CA   . VAL   B 1 165 ? 37.264 -37.041 -11.654 1.00 21.62 ?  165 VAL   B CA   1 
ATOM   6635 C C    . VAL   B 1 165 ? 36.337 -38.236 -11.831 1.00 23.44 ?  165 VAL   B C    1 
ATOM   6636 O O    . VAL   B 1 165 ? 35.175 -38.092 -12.233 1.00 25.01 ?  165 VAL   B O    1 
ATOM   6637 C CB   . VAL   B 1 165 ? 38.311 -36.969 -12.783 1.00 23.14 ?  165 VAL   B CB   1 
ATOM   6638 C CG1  . VAL   B 1 165 ? 37.642 -37.083 -14.135 1.00 24.52 ?  165 VAL   B CG1  1 
ATOM   6639 C CG2  . VAL   B 1 165 ? 39.100 -35.672 -12.693 1.00 22.61 ?  165 VAL   B CG2  1 
ATOM   6640 H H    . VAL   B 1 165 ? 38.766 -37.276 -10.394 1.00 23.85 ?  165 VAL   B H    1 
ATOM   6641 H HA   . VAL   B 1 165 ? 36.730 -36.236 -11.707 1.00 25.95 ?  165 VAL   B HA   1 
ATOM   6642 H HB   . VAL   B 1 165 ? 38.943 -37.701 -12.691 1.00 27.77 ?  165 VAL   B HB   1 
ATOM   6643 H HG11 . VAL   B 1 165 ? 38.250 -36.771 -14.821 1.00 29.43 ?  165 VAL   B HG11 1 
ATOM   6644 H HG12 . VAL   B 1 165 ? 37.421 -38.017 -14.296 1.00 29.43 ?  165 VAL   B HG12 1 
ATOM   6645 H HG13 . VAL   B 1 165 ? 36.836 -36.548 -14.134 1.00 29.43 ?  165 VAL   B HG13 1 
ATOM   6646 H HG21 . VAL   B 1 165 ? 39.735 -35.627 -13.429 1.00 27.14 ?  165 VAL   B HG21 1 
ATOM   6647 H HG22 . VAL   B 1 165 ? 38.485 -34.920 -12.749 1.00 27.14 ?  165 VAL   B HG22 1 
ATOM   6648 H HG23 . VAL   B 1 165 ? 39.577 -35.642 -11.848 1.00 27.14 ?  165 VAL   B HG23 1 
ATOM   6649 N N    A SER   B 1 166 ? 36.834 -39.438 -11.530 0.48 23.75 ?  166 SER   B N    1 
ATOM   6650 N N    B SER   B 1 166 ? 36.837 -39.436 -11.522 0.52 23.79 ?  166 SER   B N    1 
ATOM   6651 C CA   A SER   B 1 166 ? 36.060 -40.640 -11.813 0.48 24.57 ?  166 SER   B CA   1 
ATOM   6652 C CA   B SER   B 1 166 ? 36.069 -40.644 -11.795 0.52 24.73 ?  166 SER   B CA   1 
ATOM   6653 C C    A SER   B 1 166 ? 34.823 -40.752 -10.933 0.48 24.79 ?  166 SER   B C    1 
ATOM   6654 C C    B SER   B 1 166 ? 34.797 -40.694 -10.963 0.52 24.92 ?  166 SER   B C    1 
ATOM   6655 O O    A SER   B 1 166 ? 33.881 -41.451 -11.311 0.48 26.04 ?  166 SER   B O    1 
ATOM   6656 O O    B SER   B 1 166 ? 33.797 -41.259 -11.409 0.52 26.31 ?  166 SER   B O    1 
ATOM   6657 C CB   A SER   B 1 166 ? 36.924 -41.897 -11.673 0.48 24.66 ?  166 SER   B CB   1 
ATOM   6658 C CB   B SER   B 1 166 ? 36.925 -41.896 -11.567 0.52 24.96 ?  166 SER   B CB   1 
ATOM   6659 O OG   A SER   B 1 166 ? 37.345 -42.097 -10.336 0.48 24.36 ?  166 SER   B OG   1 
ATOM   6660 O OG   B SER   B 1 166 ? 37.234 -42.083 -10.197 0.52 24.88 ?  166 SER   B OG   1 
ATOM   6661 H H    A SER   B 1 166 ? 37.599 -39.577 -11.167 0.48 28.51 ?  166 SER   B H    1 
ATOM   6662 H H    B SER   B 1 166 ? 37.599 -39.570 -11.154 0.52 28.56 ?  166 SER   B H    1 
ATOM   6663 H HA   A SER   B 1 166 ? 35.763 -40.601 -12.738 0.48 29.49 ?  166 SER   B HA   1 
ATOM   6664 H HA   B SER   B 1 166 ? 35.801 -40.642 -12.728 0.52 29.69 ?  166 SER   B HA   1 
ATOM   6665 H HB2  A SER   B 1 166 ? 36.403 -42.666 -11.956 0.48 29.60 ?  166 SER   B HB2  1 
ATOM   6666 H HB2  B SER   B 1 166 ? 36.438 -42.673 -11.889 0.52 29.96 ?  166 SER   B HB2  1 
ATOM   6667 H HB3  A SER   B 1 166 ? 37.706 -41.804 -12.238 0.48 29.60 ?  166 SER   B HB3  1 
ATOM   6668 H HB3  B SER   B 1 166 ? 37.755 -41.802 -12.063 0.52 29.96 ?  166 SER   B HB3  1 
ATOM   6669 H HG   A SER   B 1 166 ? 37.794 -41.435 -10.080 0.48 29.24 ?  166 SER   B HG   1 
ATOM   6670 H HG   B SER   B 1 166 ? 37.650 -41.414 -9.905  0.52 29.87 ?  166 SER   B HG   1 
ATOM   6671 N N    . SER   B 1 167 ? 34.803 -40.099 -9.772  1.00 23.48 ?  167 SER   B N    1 
ATOM   6672 C CA   . SER   B 1 167 ? 33.650 -40.142 -8.876  1.00 23.84 ?  167 SER   B CA   1 
ATOM   6673 C C    . SER   B 1 167 ? 32.740 -38.916 -8.970  1.00 23.17 ?  167 SER   B C    1 
ATOM   6674 O O    . SER   B 1 167 ? 31.659 -38.924 -8.369  1.00 23.68 ?  167 SER   B O    1 
ATOM   6675 C CB   . SER   B 1 167 ? 34.109 -40.320 -7.423  1.00 24.19 ?  167 SER   B CB   1 
ATOM   6676 O OG   . SER   B 1 167 ? 34.758 -39.149 -6.952  1.00 24.32 ?  167 SER   B OG   1 
ATOM   6677 H H    A SER   B 1 167 ? 35.462 -39.642 -9.473  0.48 28.19 ?  167 SER   B H    1 
ATOM   6678 H H    B SER   B 1 167 ? 35.467 -39.654 -9.465  0.52 28.19 ?  167 SER   B H    1 
ATOM   6679 H HA   . SER   B 1 167 ? 33.118 -40.923 -9.104  1.00 28.61 ?  167 SER   B HA   1 
ATOM   6680 H HB2  . SER   B 1 167 ? 33.333 -40.507 -6.870  1.00 29.03 ?  167 SER   B HB2  1 
ATOM   6681 H HB3  . SER   B 1 167 ? 34.731 -41.069 -7.376  1.00 29.03 ?  167 SER   B HB3  1 
ATOM   6682 H HG   . SER   B 1 167 ? 35.426 -38.984 -7.427  1.00 29.19 ?  167 SER   B HG   1 
ATOM   6683 N N    . PHE   B 1 168 ? 33.130 -37.870 -9.699  1.00 22.96 ?  168 PHE   B N    1 
ATOM   6684 C CA   . PHE   B 1 168 ? 32.283 -36.682 -9.785  1.00 21.75 ?  168 PHE   B CA   1 
ATOM   6685 C C    . PHE   B 1 168 ? 31.001 -36.960 -10.563 1.00 19.51 ?  168 PHE   B C    1 
ATOM   6686 O O    . PHE   B 1 168 ? 29.938 -36.382 -10.254 1.00 18.83 ?  168 PHE   B O    1 
ATOM   6687 C CB   . PHE   B 1 168 ? 33.051 -35.537 -10.437 1.00 22.37 ?  168 PHE   B CB   1 
ATOM   6688 C CG   . PHE   B 1 168 ? 32.245 -34.292 -10.588 1.00 22.07 ?  168 PHE   B CG   1 
ATOM   6689 C CD1  . PHE   B 1 168 ? 31.894 -33.552 -9.474  1.00 22.98 ?  168 PHE   B CD1  1 
ATOM   6690 C CD2  . PHE   B 1 168 ? 31.820 -33.866 -11.832 1.00 21.81 ?  168 PHE   B CD2  1 
ATOM   6691 C CE1  . PHE   B 1 168 ? 31.133 -32.406 -9.594  1.00 22.73 ?  168 PHE   B CE1  1 
ATOM   6692 C CE2  . PHE   B 1 168 ? 31.066 -32.708 -11.960 1.00 22.26 ?  168 PHE   B CE2  1 
ATOM   6693 C CZ   . PHE   B 1 168 ? 30.724 -31.976 -10.833 1.00 22.32 ?  168 PHE   B CZ   1 
ATOM   6694 H H    . PHE   B 1 168 ? 33.866 -37.826 -10.140 1.00 27.56 ?  168 PHE   B H    1 
ATOM   6695 H HA   . PHE   B 1 168 ? 32.029 -36.413 -8.891  1.00 26.11 ?  168 PHE   B HA   1 
ATOM   6696 H HB2  . PHE   B 1 168 ? 33.821 -35.332 -9.888  1.00 26.85 ?  168 PHE   B HB2  1 
ATOM   6697 H HB3  . PHE   B 1 168 ? 33.336 -35.816 -11.320 1.00 26.85 ?  168 PHE   B HB3  1 
ATOM   6698 H HD1  . PHE   B 1 168 ? 32.163 -33.842 -8.633  1.00 27.59 ?  168 PHE   B HD1  1 
ATOM   6699 H HD2  . PHE   B 1 168 ? 32.050 -34.348 -12.590 1.00 26.18 ?  168 PHE   B HD2  1 
ATOM   6700 H HE1  . PHE   B 1 168 ? 30.905 -31.922 -8.835  1.00 27.28 ?  168 PHE   B HE1  1 
ATOM   6701 H HE2  . PHE   B 1 168 ? 30.786 -32.421 -12.801 1.00 26.72 ?  168 PHE   B HE2  1 
ATOM   6702 H HZ   . PHE   B 1 168 ? 30.213 -31.205 -10.915 1.00 26.80 ?  168 PHE   B HZ   1 
ATOM   6703 N N    A LEU   B 1 169 ? 31.073 -37.823 -11.574 0.48 20.73 ?  169 LEU   B N    1 
ATOM   6704 N N    B LEU   B 1 169 ? 31.081 -37.830 -11.568 0.52 20.78 ?  169 LEU   B N    1 
ATOM   6705 C CA   A LEU   B 1 169 ? 29.905 -38.146 -12.387 0.48 23.18 ?  169 LEU   B CA   1 
ATOM   6706 C CA   B LEU   B 1 169 ? 29.938 -38.168 -12.402 0.52 23.41 ?  169 LEU   B CA   1 
ATOM   6707 C C    A LEU   B 1 169 ? 29.901 -39.597 -12.853 0.48 25.13 ?  169 LEU   B C    1 
ATOM   6708 C C    B LEU   B 1 169 ? 29.974 -39.628 -12.836 0.52 25.88 ?  169 LEU   B C    1 
ATOM   6709 O O    A LEU   B 1 169 ? 28.983 -40.030 -13.552 0.48 26.38 ?  169 LEU   B O    1 
ATOM   6710 O O    B LEU   B 1 169 ? 29.176 -40.059 -13.668 0.52 27.27 ?  169 LEU   B O    1 
ATOM   6711 C CB   A LEU   B 1 169 ? 29.828 -37.227 -13.607 0.48 24.79 ?  169 LEU   B CB   1 
ATOM   6712 C CB   B LEU   B 1 169 ? 29.903 -37.275 -13.642 0.52 24.79 ?  169 LEU   B CB   1 
ATOM   6713 C CG   A LEU   B 1 169 ? 28.578 -36.348 -13.677 0.48 26.52 ?  169 LEU   B CG   1 
ATOM   6714 C CG   B LEU   B 1 169 ? 28.681 -36.368 -13.765 0.52 26.44 ?  169 LEU   B CG   1 
ATOM   6715 C CD1  A LEU   B 1 169 ? 28.531 -35.599 -14.993 0.48 27.33 ?  169 LEU   B CD1  1 
ATOM   6716 C CD1  B LEU   B 1 169 ? 28.657 -35.734 -15.136 0.52 27.17 ?  169 LEU   B CD1  1 
ATOM   6717 C CD2  A LEU   B 1 169 ? 27.322 -37.182 -13.488 0.48 26.51 ?  169 LEU   B CD2  1 
ATOM   6718 C CD2  B LEU   B 1 169 ? 27.398 -37.143 -13.505 0.52 26.44 ?  169 LEU   B CD2  1 
ATOM   6719 O OXT  A LEU   B 1 169 ? 30.811 -40.364 -12.548 0.48 25.78 -1 169 LEU   B OXT  1 
ATOM   6720 O OXT  B LEU   B 1 169 ? 30.801 -40.410 -12.373 0.52 26.88 -1 169 LEU   B OXT  1 
ATOM   6721 H H    A LEU   B 1 169 ? 31.788 -38.237 -11.817 0.48 24.88 ?  169 LEU   B H    1 
ATOM   6722 H H    B LEU   B 1 169 ? 31.801 -38.242 -11.798 0.52 24.94 ?  169 LEU   B H    1 
ATOM   6723 H HA   A LEU   B 1 169 ? 29.115 -38.006 -11.850 0.48 27.83 ?  169 LEU   B HA   1 
ATOM   6724 H HA   B LEU   B 1 169 ? 29.131 -38.031 -11.892 0.52 28.10 ?  169 LEU   B HA   1 
ATOM   6725 H HB2  A LEU   B 1 169 ? 30.597 -36.638 -13.600 0.48 29.76 ?  169 LEU   B HB2  1 
ATOM   6726 H HB2  B LEU   B 1 169 ? 30.687 -36.703 -13.634 0.52 29.76 ?  169 LEU   B HB2  1 
ATOM   6727 H HB3  A LEU   B 1 169 ? 29.843 -37.771 -14.412 0.48 29.76 ?  169 LEU   B HB3  1 
ATOM   6728 H HB3  B LEU   B 1 169 ? 29.923 -37.836 -14.435 0.52 29.76 ?  169 LEU   B HB3  1 
ATOM   6729 H HG   A LEU   B 1 169 ? 28.612 -35.693 -12.962 0.48 31.83 ?  169 LEU   B HG   1 
ATOM   6730 H HG   B LEU   B 1 169 ? 28.743 -35.657 -13.106 0.52 31.74 ?  169 LEU   B HG   1 
ATOM   6731 H HD11 A LEU   B 1 169 ? 27.745 -35.032 -15.005 0.48 32.81 ?  169 LEU   B HD11 1 
ATOM   6732 H HD11 B LEU   B 1 169 ? 27.893 -35.139 -15.193 0.52 32.61 ?  169 LEU   B HD11 1 
ATOM   6733 H HD12 A LEU   B 1 169 ? 29.332 -35.059 -15.075 0.48 32.81 ?  169 LEU   B HD12 1 
ATOM   6734 H HD12 B LEU   B 1 169 ? 29.477 -35.235 -15.264 0.52 32.61 ?  169 LEU   B HD12 1 
ATOM   6735 H HD13 A LEU   B 1 169 ? 28.488 -36.242 -15.718 0.48 32.81 ?  169 LEU   B HD13 1 
ATOM   6736 H HD13 B LEU   B 1 169 ? 28.584 -36.434 -15.802 0.52 32.61 ?  169 LEU   B HD13 1 
ATOM   6737 H HD21 A LEU   B 1 169 ? 26.579 -36.740 -13.921 0.48 31.82 ?  169 LEU   B HD21 1 
ATOM   6738 H HD21 B LEU   B 1 169 ? 26.670 -36.719 -13.979 0.52 31.74 ?  169 LEU   B HD21 1 
ATOM   6739 H HD22 A LEU   B 1 169 ? 27.465 -38.058 -13.883 0.48 31.82 ?  169 LEU   B HD22 1 
ATOM   6740 H HD22 B LEU   B 1 169 ? 27.516 -38.055 -13.821 0.52 31.74 ?  169 LEU   B HD22 1 
ATOM   6741 H HD23 A LEU   B 1 169 ? 27.148 -37.275 -12.539 0.48 31.82 ?  169 LEU   B HD23 1 
ATOM   6742 H HD23 B LEU   B 1 169 ? 27.219 -37.146 -12.551 0.52 31.74 ?  169 LEU   B HD23 1 
HETATM 6743 N N2   B A1A50 C 2 .   ? 10.826 0.054   -2.140  0.52 15.12 ?  201 A1A50 A N2   1 
HETATM 6744 C C3   B A1A50 C 2 .   ? 9.809  2.090   -1.325  0.52 16.16 ?  201 A1A50 A C3   1 
HETATM 6745 C C6   B A1A50 C 2 .   ? 14.369 0.043   0.868   0.52 13.90 ?  201 A1A50 A C6   1 
HETATM 6746 C C9   B A1A50 C 2 .   ? 16.594 2.543   -0.717  0.52 14.33 ?  201 A1A50 A C9   1 
HETATM 6747 C C12  B A1A50 C 2 .   ? 17.875 0.022   -0.840  0.52 14.37 ?  201 A1A50 A C12  1 
HETATM 6748 C C14  B A1A50 C 2 .   ? 16.609 0.173   -0.249  0.52 14.32 ?  201 A1A50 A C14  1 
HETATM 6749 C C1   B A1A50 C 2 .   ? 9.876  0.498   -4.724  0.52 18.57 ?  201 A1A50 A C1   1 
HETATM 6750 C C10  B A1A50 C 2 .   ? 17.857 2.399   -1.313  0.52 14.29 ?  201 A1A50 A C10  1 
HETATM 6751 C C11  B A1A50 C 2 .   ? 18.499 1.152   -1.370  0.52 14.55 ?  201 A1A50 A C11  1 
HETATM 6752 C C13  B A1A50 C 2 .   ? 18.586 -1.316  -0.925  0.52 15.30 ?  201 A1A50 A C13  1 
HETATM 6753 C C15  B A1A50 C 2 .   ? 11.380 -0.137  -0.924  0.52 14.37 ?  201 A1A50 A C15  1 
HETATM 6754 C C2   B A1A50 C 2 .   ? 10.052 1.141   -2.335  0.52 16.25 ?  201 A1A50 A C2   1 
HETATM 6755 C C4   B A1A50 C 2 .   ? 10.399 1.888   -0.071  0.52 15.60 ?  201 A1A50 A C4   1 
HETATM 6756 C C5   B A1A50 C 2 .   ? 11.189 0.745   0.162   0.52 13.75 ?  201 A1A50 A C5   1 
HETATM 6757 C C7   B A1A50 C 2 .   ? 14.636 1.332   0.484   0.52 13.20 ?  201 A1A50 A C7   1 
HETATM 6758 C C8   B A1A50 C 2 .   ? 15.926 1.428   -0.169  0.52 13.84 ?  201 A1A50 A C8   1 
HETATM 6759 N N1   B A1A50 C 2 .   ? 9.483  1.329   -3.597  0.52 17.08 ?  201 A1A50 A N1   1 
HETATM 6760 N N3   B A1A50 C 2 .   ? 11.763 0.527   1.351   0.52 14.94 ?  201 A1A50 A N3   1 
HETATM 6761 O O1   B A1A50 C 2 .   ? 13.305 -0.423  3.123   0.52 16.36 ?  201 A1A50 A O1   1 
HETATM 6762 O O2   B A1A50 C 2 .   ? 12.721 -1.910  1.239   0.52 15.32 ?  201 A1A50 A O2   1 
HETATM 6763 S S1   B A1A50 C 2 .   ? 12.922 -0.530  1.711   0.52 14.30 ?  201 A1A50 A S1   1 
HETATM 6764 S S2   B A1A50 C 2 .   ? 15.620 -1.073  0.469   0.52 14.86 ?  201 A1A50 A S2   1 
HETATM 6765 H H5   B A1A50 C 2 .   ? 9.191  2.960   -1.504  0.52 19.40 ?  201 A1A50 A H5   1 
HETATM 6766 H H8   B A1A50 C 2 .   ? 16.130 3.513   -0.680  0.52 17.20 ?  201 A1A50 A H8   1 
HETATM 6767 H H1   B A1A50 C 2 .   ? 9.352  0.814   -5.625  0.52 22.29 ?  201 A1A50 A H1   1 
HETATM 6768 H H2   B A1A50 C 2 .   ? 9.632  -0.547  -4.532  0.52 22.29 ?  201 A1A50 A H2   1 
HETATM 6769 H H3   B A1A50 C 2 .   ? 10.949 0.579   -4.908  0.52 22.29 ?  201 A1A50 A H3   1 
HETATM 6770 H H9   B A1A50 C 2 .   ? 18.357 3.267   -1.726  0.52 17.15 ?  201 A1A50 A H9   1 
HETATM 6771 H H10  B A1A50 C 2 .   ? 19.472 1.064   -1.835  0.52 17.47 ?  201 A1A50 A H10  1 
HETATM 6772 H H12  B A1A50 C 2 .   ? 19.552 -1.197  -1.418  0.52 18.37 ?  201 A1A50 A H12  1 
HETATM 6773 H H11  B A1A50 C 2 .   ? 18.023 -2.063  -1.488  0.52 18.37 ?  201 A1A50 A H11  1 
HETATM 6774 H H13  B A1A50 C 2 .   ? 18.769 -1.715  0.074   0.52 18.37 ?  201 A1A50 A H13  1 
HETATM 6775 H H14  B A1A50 C 2 .   ? 11.978 -1.028  -0.817  0.52 17.25 ?  201 A1A50 A H14  1 
HETATM 6776 H H6   B A1A50 C 2 .   ? 10.206 2.602   0.718   0.52 18.73 ?  201 A1A50 A H6   1 
HETATM 6777 H H7   B A1A50 C 2 .   ? 13.976 2.173   0.647   0.52 15.85 ?  201 A1A50 A H7   1 
HETATM 6778 H H4   B A1A50 C 2 .   ? 8.792  2.056   -3.741  0.52 20.50 ?  201 A1A50 A H4   1 
HETATM 6779 O O    . HOH   D 3 .   ? 28.530 -10.469 -14.044 1.00 44.41 ?  301 HOH   A O    1 
HETATM 6780 O O    . HOH   D 3 .   ? 14.671 -4.399  20.506  1.00 50.12 ?  302 HOH   A O    1 
HETATM 6781 O O    . HOH   D 3 .   ? 34.488 -1.808  12.469  1.00 43.25 ?  303 HOH   A O    1 
HETATM 6782 O O    . HOH   D 3 .   ? -0.519 -2.971  2.926   1.00 40.76 ?  304 HOH   A O    1 
HETATM 6783 O O    . HOH   D 3 .   ? 15.165 -12.070 18.648  1.00 49.03 ?  305 HOH   A O    1 
HETATM 6784 O O    B HOH   D 3 .   ? 4.332  3.524   0.541   0.52 21.67 ?  306 HOH   A O    1 
HETATM 6785 O O    . HOH   D 3 .   ? 22.739 12.620  1.612   1.00 19.39 ?  307 HOH   A O    1 
HETATM 6786 O O    . HOH   D 3 .   ? 11.725 -10.726 -10.162 1.00 50.33 ?  308 HOH   A O    1 
HETATM 6787 O O    . HOH   D 3 .   ? -0.812 -8.350  2.251   1.00 43.91 ?  309 HOH   A O    1 
HETATM 6788 O O    . HOH   D 3 .   ? 18.909 -21.831 7.016   1.00 42.64 ?  310 HOH   A O    1 
HETATM 6789 O O    . HOH   D 3 .   ? 14.158 -4.633  -11.961 1.00 31.53 ?  311 HOH   A O    1 
HETATM 6790 O O    . HOH   D 3 .   ? 28.054 -6.148  19.494  1.00 43.71 ?  312 HOH   A O    1 
HETATM 6791 O O    . HOH   D 3 .   ? 7.567  -6.117  -6.687  1.00 46.49 ?  313 HOH   A O    1 
HETATM 6792 O O    . HOH   D 3 .   ? 28.965 0.636   -9.705  1.00 24.17 ?  314 HOH   A O    1 
HETATM 6793 O O    . HOH   D 3 .   ? 30.137 -13.312 -8.519  1.00 29.64 ?  315 HOH   A O    1 
HETATM 6794 O O    . HOH   D 3 .   ? 42.416 10.554  5.132   1.00 21.78 ?  316 HOH   A O    1 
HETATM 6795 O O    A HOH   D 3 .   ? 12.261 0.462   14.793  0.48 25.92 ?  317 HOH   A O    1 
HETATM 6796 O O    . HOH   D 3 .   ? 14.660 -13.858 16.578  1.00 36.02 ?  318 HOH   A O    1 
HETATM 6797 O O    A HOH   D 3 .   ? 4.699  4.104   0.515   0.48 25.95 ?  319 HOH   A O    1 
HETATM 6798 O O    A HOH   D 3 .   ? 9.689  -21.155 5.733   0.48 20.77 ?  320 HOH   A O    1 
HETATM 6799 O O    . HOH   D 3 .   ? 16.837 -19.040 4.939   1.00 20.12 ?  321 HOH   A O    1 
HETATM 6800 O O    . HOH   D 3 .   ? 9.097  -10.010 19.159  1.00 44.66 ?  322 HOH   A O    1 
HETATM 6801 O O    . HOH   D 3 .   ? 24.071 -7.584  14.351  1.00 19.66 ?  323 HOH   A O    1 
HETATM 6802 O O    . HOH   D 3 .   ? 38.271 10.164  7.112   1.00 50.31 ?  324 HOH   A O    1 
HETATM 6803 O O    . HOH   D 3 .   ? 28.290 0.012   -13.369 1.00 41.46 ?  325 HOH   A O    1 
HETATM 6804 O O    A HOH   D 3 .   ? 17.480 -1.576  0.383   0.48 23.82 ?  326 HOH   A O    1 
HETATM 6805 O O    . HOH   D 3 .   ? 16.895 -17.951 14.856  1.00 32.17 ?  327 HOH   A O    1 
HETATM 6806 O O    . HOH   D 3 .   ? 26.452 -19.279 -1.737  1.00 17.57 ?  328 HOH   A O    1 
HETATM 6807 O O    . HOH   D 3 .   ? 31.066 6.158   -12.289 1.00 29.27 ?  329 HOH   A O    1 
HETATM 6808 O O    . HOH   D 3 .   ? 0.727  -4.185  0.039   1.00 31.96 ?  330 HOH   A O    1 
HETATM 6809 O O    . HOH   D 3 .   ? 27.343 -5.702  -14.041 1.00 37.72 ?  331 HOH   A O    1 
HETATM 6810 O O    A HOH   D 3 .   ? 3.540  -9.239  9.677   0.48 39.76 ?  332 HOH   A O    1 
HETATM 6811 O O    B HOH   D 3 .   ? 12.880 -1.774  -6.528  0.52 20.82 ?  333 HOH   A O    1 
HETATM 6812 O O    . HOH   D 3 .   ? 37.565 2.832   10.153  1.00 36.52 ?  334 HOH   A O    1 
HETATM 6813 O O    . HOH   D 3 .   ? 34.060 -1.235  -8.994  1.00 30.53 ?  335 HOH   A O    1 
HETATM 6814 O O    . HOH   D 3 .   ? 14.992 -21.306 14.151  1.00 22.40 ?  336 HOH   A O    1 
HETATM 6815 O O    B HOH   D 3 .   ? 15.342 -0.767  4.834   0.52 19.62 ?  337 HOH   A O    1 
HETATM 6816 O O    . HOH   D 3 .   ? 30.953 -17.989 7.801   1.00 21.03 ?  338 HOH   A O    1 
HETATM 6817 O O    . HOH   D 3 .   ? 39.796 -1.004  -5.167  1.00 23.36 ?  339 HOH   A O    1 
HETATM 6818 O O    . HOH   D 3 .   ? 19.826 -12.343 -9.051  1.00 24.50 ?  340 HOH   A O    1 
HETATM 6819 O O    . HOH   D 3 .   ? 7.876  -12.332 -0.974  1.00 20.49 ?  341 HOH   A O    1 
HETATM 6820 O O    . HOH   D 3 .   ? 31.710 8.242   14.799  1.00 33.65 ?  342 HOH   A O    1 
HETATM 6821 O O    . HOH   D 3 .   ? 44.347 7.183   6.460   1.00 27.89 ?  343 HOH   A O    1 
HETATM 6822 O O    . HOH   D 3 .   ? 36.181 -5.048  -0.548  1.00 33.69 ?  344 HOH   A O    1 
HETATM 6823 O O    . HOH   D 3 .   ? 37.124 -2.753  9.705   1.00 47.66 ?  345 HOH   A O    1 
HETATM 6824 O O    . HOH   D 3 .   ? 24.081 -2.008  -2.113  1.00 12.11 ?  346 HOH   A O    1 
HETATM 6825 O O    . HOH   D 3 .   ? 22.273 5.377   18.978  1.00 41.89 ?  347 HOH   A O    1 
HETATM 6826 O O    . HOH   D 3 .   ? 19.406 -11.043 24.075  1.00 81.81 ?  348 HOH   A O    1 
HETATM 6827 O O    . HOH   D 3 .   ? 14.240 -21.073 -4.180  1.00 32.47 ?  349 HOH   A O    1 
HETATM 6828 O O    . HOH   D 3 .   ? 21.316 10.400  14.931  1.00 33.08 ?  350 HOH   A O    1 
HETATM 6829 O O    . HOH   D 3 .   ? 27.012 11.591  1.554   1.00 21.57 ?  351 HOH   A O    1 
HETATM 6830 O O    . HOH   D 3 .   ? 16.169 16.569  8.407   1.00 45.80 ?  352 HOH   A O    1 
HETATM 6831 O O    . HOH   D 3 .   ? 38.564 4.960   6.998   1.00 17.72 ?  353 HOH   A O    1 
HETATM 6832 O O    B HOH   D 3 .   ? 8.307  4.073   1.179   0.52 20.50 ?  354 HOH   A O    1 
HETATM 6833 O O    . HOH   D 3 .   ? 27.341 -10.419 13.960  1.00 19.97 ?  355 HOH   A O    1 
HETATM 6834 O O    . HOH   D 3 .   ? 15.098 -8.071  -9.764  1.00 24.54 ?  356 HOH   A O    1 
HETATM 6835 O O    A HOH   D 3 .   ? 8.093  -21.211 3.989   0.48 45.03 ?  357 HOH   A O    1 
HETATM 6836 O O    . HOH   D 3 .   ? 17.048 -17.700 -5.084  1.00 28.96 ?  358 HOH   A O    1 
HETATM 6837 O O    A HOH   D 3 .   ? 13.305 -1.308  -6.590  0.48 16.11 ?  359 HOH   A O    1 
HETATM 6838 O O    . HOH   D 3 .   ? 20.574 -19.769 -5.018  1.00 29.72 ?  360 HOH   A O    1 
HETATM 6839 O O    . HOH   D 3 .   ? 14.150 0.776   6.643   1.00 18.75 ?  361 HOH   A O    1 
HETATM 6840 O O    . HOH   D 3 .   ? 13.492 -15.150 -7.584  1.00 25.79 ?  362 HOH   A O    1 
HETATM 6841 O O    . HOH   D 3 .   ? 18.614 9.608   8.964   1.00 24.53 ?  363 HOH   A O    1 
HETATM 6842 O O    . HOH   D 3 .   ? 42.650 4.299   5.455   1.00 37.99 ?  364 HOH   A O    1 
HETATM 6843 O O    . HOH   D 3 .   ? 31.738 -9.363  -6.761  1.00 25.53 ?  365 HOH   A O    1 
HETATM 6844 O O    . HOH   D 3 .   ? 15.185 4.350   17.602  1.00 42.54 ?  366 HOH   A O    1 
HETATM 6845 O O    . HOH   D 3 .   ? 18.666 -19.440 13.540  1.00 51.76 ?  367 HOH   A O    1 
HETATM 6846 O O    . HOH   D 3 .   ? 16.408 -21.918 0.923   1.00 34.25 ?  368 HOH   A O    1 
HETATM 6847 O O    . HOH   D 3 .   ? 14.492 -3.629  2.873   1.00 16.82 ?  369 HOH   A O    1 
HETATM 6848 O O    . HOH   D 3 .   ? 44.089 8.470   -2.986  1.00 31.94 ?  370 HOH   A O    1 
HETATM 6849 O O    . HOH   D 3 .   ? 37.334 12.000  4.952   1.00 31.19 ?  371 HOH   A O    1 
HETATM 6850 O O    . HOH   D 3 .   ? 22.049 -19.112 11.446  1.00 39.49 ?  372 HOH   A O    1 
HETATM 6851 O O    . HOH   D 3 .   ? 35.705 -12.542 6.910   1.00 18.32 ?  373 HOH   A O    1 
HETATM 6852 O O    . HOH   D 3 .   ? 25.663 -0.653  -7.271  1.00 16.32 ?  374 HOH   A O    1 
HETATM 6853 O O    . HOH   D 3 .   ? 27.564 13.913  2.696   1.00 31.50 ?  375 HOH   A O    1 
HETATM 6854 O O    . HOH   D 3 .   ? 43.364 7.828   2.810   1.00 38.72 ?  376 HOH   A O    1 
HETATM 6855 O O    A HOH   D 3 .   ? 6.890  -7.942  11.796  0.48 17.28 ?  377 HOH   A O    1 
HETATM 6856 O O    . HOH   D 3 .   ? 21.747 -21.757 8.544   1.00 32.83 ?  378 HOH   A O    1 
HETATM 6857 O O    . HOH   D 3 .   ? 37.556 -2.068  5.956   1.00 33.27 ?  379 HOH   A O    1 
HETATM 6858 O O    . HOH   D 3 .   ? 31.023 -13.877 -2.425  1.00 16.16 ?  380 HOH   A O    1 
HETATM 6859 O O    . HOH   D 3 .   ? 33.474 -16.854 8.108   1.00 21.45 ?  381 HOH   A O    1 
HETATM 6860 O O    . HOH   D 3 .   ? 5.170  3.042   4.817   1.00 38.05 ?  382 HOH   A O    1 
HETATM 6861 O O    B HOH   D 3 .   ? 14.638 -0.741  -12.311 0.52 21.76 ?  383 HOH   A O    1 
HETATM 6862 O O    . HOH   D 3 .   ? 31.734 -7.168  -9.889  1.00 23.97 ?  384 HOH   A O    1 
HETATM 6863 O O    . HOH   D 3 .   ? 30.808 3.170   8.207   1.00 14.40 ?  385 HOH   A O    1 
HETATM 6864 O O    . HOH   D 3 .   ? 20.032 4.545   -7.573  1.00 18.72 ?  386 HOH   A O    1 
HETATM 6865 O O    A HOH   D 3 .   ? 21.232 -2.282  -2.101  0.48 13.24 ?  387 HOH   A O    1 
HETATM 6866 O O    . HOH   D 3 .   ? 6.682  -2.902  12.875  1.00 33.37 ?  388 HOH   A O    1 
HETATM 6867 O O    . HOH   D 3 .   ? 24.366 3.748   -1.831  1.00 16.78 ?  389 HOH   A O    1 
HETATM 6868 O O    . HOH   D 3 .   ? 10.848 1.847   12.553  1.00 27.85 ?  390 HOH   A O    1 
HETATM 6869 O O    A HOH   D 3 .   ? 18.950 -0.544  -1.686  0.48 15.48 ?  391 HOH   A O    1 
HETATM 6870 O O    . HOH   D 3 .   ? 32.743 -9.149  6.055   1.00 21.04 ?  392 HOH   A O    1 
HETATM 6871 O O    A HOH   D 3 .   ? 24.593 2.124   -7.048  0.48 15.03 ?  393 HOH   A O    1 
HETATM 6872 O O    . HOH   D 3 .   ? 27.979 0.861   -7.143  1.00 15.48 ?  394 HOH   A O    1 
HETATM 6873 O O    . HOH   D 3 .   ? 15.766 2.341   24.632  1.00 47.01 ?  395 HOH   A O    1 
HETATM 6874 O O    . HOH   D 3 .   ? 33.615 -7.112  4.320   1.00 18.91 ?  396 HOH   A O    1 
HETATM 6875 O O    . HOH   D 3 .   ? 13.890 -4.715  17.396  1.00 30.17 ?  397 HOH   A O    1 
HETATM 6876 O O    . HOH   D 3 .   ? 21.807 -13.653 -8.153  1.00 36.74 ?  398 HOH   A O    1 
HETATM 6877 O O    B HOH   D 3 .   ? 21.609 -2.430  -2.706  0.52 14.05 ?  399 HOH   A O    1 
HETATM 6878 O O    . HOH   D 3 .   ? 15.589 11.876  7.887   1.00 58.41 ?  400 HOH   A O    1 
HETATM 6879 O O    . HOH   D 3 .   ? 9.003  -11.962 17.182  1.00 44.50 ?  401 HOH   A O    1 
HETATM 6880 O O    . HOH   D 3 .   ? 23.537 11.507  4.047   1.00 15.06 ?  402 HOH   A O    1 
HETATM 6881 O O    . HOH   D 3 .   ? 24.531 -17.360 12.698  1.00 28.98 ?  403 HOH   A O    1 
HETATM 6882 O O    A HOH   D 3 .   ? 13.944 -22.889 7.367   0.48 18.15 ?  404 HOH   A O    1 
HETATM 6883 O O    B HOH   D 3 .   ? 21.168 2.912   -0.012  0.52 12.57 ?  405 HOH   A O    1 
HETATM 6884 O O    . HOH   D 3 .   ? 44.913 -0.645  2.963   1.00 40.25 ?  406 HOH   A O    1 
HETATM 6885 O O    . HOH   D 3 .   ? 10.338 -22.054 -1.272  1.00 48.83 ?  407 HOH   A O    1 
HETATM 6886 O O    A HOH   D 3 .   ? 6.419  -5.386  11.115  0.48 17.79 ?  408 HOH   A O    1 
HETATM 6887 O O    B HOH   D 3 .   ? 24.286 2.005   -6.829  0.52 19.55 ?  409 HOH   A O    1 
HETATM 6888 O O    B HOH   D 3 .   ? 11.794 -2.055  -3.811  0.52 15.74 ?  410 HOH   A O    1 
HETATM 6889 O O    . HOH   D 3 .   ? 29.957 -9.961  12.995  1.00 23.16 ?  411 HOH   A O    1 
HETATM 6890 O O    . HOH   D 3 .   ? 30.644 1.931   16.642  1.00 22.26 ?  412 HOH   A O    1 
HETATM 6891 O O    . HOH   D 3 .   ? 18.669 -2.227  -16.489 1.00 43.71 ?  413 HOH   A O    1 
HETATM 6892 O O    A HOH   D 3 .   ? 15.780 -0.784  5.206   0.48 19.44 ?  414 HOH   A O    1 
HETATM 6893 O O    . HOH   D 3 .   ? 30.165 -12.739 13.509  1.00 24.13 ?  415 HOH   A O    1 
HETATM 6894 O O    . HOH   D 3 .   ? 22.571 -11.744 21.729  1.00 51.76 ?  416 HOH   A O    1 
HETATM 6895 O O    . HOH   D 3 .   ? 26.957 4.292   -0.732  1.00 14.19 ?  417 HOH   A O    1 
HETATM 6896 O O    . HOH   D 3 .   ? 20.469 -19.946 2.816   1.00 24.14 ?  418 HOH   A O    1 
HETATM 6897 O O    . HOH   D 3 .   ? 22.663 8.267   18.249  1.00 45.22 ?  419 HOH   A O    1 
HETATM 6898 O O    A HOH   D 3 .   ? 24.106 4.052   -4.984  0.48 22.92 ?  420 HOH   A O    1 
HETATM 6899 O O    . HOH   D 3 .   ? 23.734 -15.653 -9.258  1.00 39.39 ?  421 HOH   A O    1 
HETATM 6900 O O    A HOH   D 3 .   ? 21.352 3.275   -0.419  0.48 12.79 ?  422 HOH   A O    1 
HETATM 6901 O O    . HOH   D 3 .   ? 38.166 -1.331  -1.905  1.00 22.01 ?  423 HOH   A O    1 
HETATM 6902 O O    . HOH   D 3 .   ? 11.599 -10.472 16.920  1.00 29.82 ?  424 HOH   A O    1 
HETATM 6903 O O    . HOH   D 3 .   ? 27.252 2.344   18.661  1.00 34.00 ?  425 HOH   A O    1 
HETATM 6904 O O    . HOH   D 3 .   ? 23.894 -20.225 -1.304  1.00 21.48 ?  426 HOH   A O    1 
HETATM 6905 O O    . HOH   D 3 .   ? 32.644 -4.114  -9.907  1.00 30.29 ?  427 HOH   A O    1 
HETATM 6906 O O    . HOH   D 3 .   ? 40.879 -8.201  -6.820  1.00 37.69 ?  428 HOH   A O    1 
HETATM 6907 O O    . HOH   D 3 .   ? 36.655 -4.948  5.390   1.00 26.13 ?  429 HOH   A O    1 
HETATM 6908 O O    . HOH   D 3 .   ? 35.050 -5.208  -3.103  1.00 18.30 ?  430 HOH   A O    1 
HETATM 6909 O O    . HOH   D 3 .   ? 23.498 -7.830  17.035  1.00 25.79 ?  431 HOH   A O    1 
HETATM 6910 O O    . HOH   D 3 .   ? 9.447  -16.134 -1.957  1.00 29.21 ?  432 HOH   A O    1 
HETATM 6911 O O    . HOH   D 3 .   ? 41.661 1.564   5.051   1.00 41.14 ?  433 HOH   A O    1 
HETATM 6912 O O    A HOH   D 3 .   ? 14.491 -0.341  -12.107 0.48 21.92 ?  434 HOH   A O    1 
HETATM 6913 O O    . HOH   D 3 .   ? 10.264 -13.597 -1.726  1.00 18.91 ?  435 HOH   A O    1 
HETATM 6914 O O    . HOH   D 3 .   ? 15.923 6.783   2.909   1.00 33.16 ?  436 HOH   A O    1 
HETATM 6915 O O    . HOH   D 3 .   ? 21.303 -8.898  21.269  1.00 61.65 ?  437 HOH   A O    1 
HETATM 6916 O O    . HOH   D 3 .   ? 14.460 -24.643 11.527  1.00 50.26 ?  438 HOH   A O    1 
HETATM 6917 O O    A HOH   D 3 .   ? 18.864 2.161   -0.821  0.48 15.25 ?  439 HOH   A O    1 
HETATM 6918 O O    . HOH   D 3 .   ? 18.416 4.949   -15.125 1.00 51.82 ?  440 HOH   A O    1 
HETATM 6919 O O    A HOH   D 3 .   ? 11.054 -0.213  1.859   0.48 26.31 ?  441 HOH   A O    1 
HETATM 6920 O O    . HOH   D 3 .   ? 23.384 -20.838 1.340   1.00 23.45 ?  442 HOH   A O    1 
HETATM 6921 O O    B HOH   D 3 .   ? 24.031 3.882   -4.639  0.52 14.21 ?  443 HOH   A O    1 
HETATM 6922 O O    . HOH   D 3 .   ? 34.380 -8.045  -0.643  1.00 30.80 ?  444 HOH   A O    1 
HETATM 6923 O O    A HOH   D 3 .   ? 23.226 7.615   -3.319  0.48 31.09 ?  445 HOH   A O    1 
HETATM 6924 O O    . HOH   D 3 .   ? 32.284 -10.577 3.460   1.00 35.74 ?  446 HOH   A O    1 
HETATM 6925 O O    B HOH   D 3 .   ? 20.771 4.517   -2.355  0.52 17.01 ?  447 HOH   A O    1 
HETATM 6926 O O    . HOH   D 3 .   ? 31.292 -12.672 0.034   1.00 27.40 ?  448 HOH   A O    1 
HETATM 6927 O O    . HOH   D 3 .   ? -1.538 -4.632  7.597   1.00 47.15 ?  449 HOH   A O    1 
HETATM 6928 O O    A HOH   D 3 .   ? 16.263 3.083   -1.519  0.48 22.12 ?  450 HOH   A O    1 
HETATM 6929 O O    B HOH   D 3 .   ? 23.500 6.694   -2.125  0.52 17.47 ?  451 HOH   A O    1 
HETATM 6930 O O    . HOH   D 3 .   ? 30.642 14.798  2.661   1.00 22.30 ?  452 HOH   A O    1 
HETATM 6931 O O    . HOH   D 3 .   ? 27.169 -3.121  19.282  1.00 38.08 ?  453 HOH   A O    1 
HETATM 6932 O O    . HOH   D 3 .   ? 21.466 -14.663 17.827  1.00 57.39 ?  454 HOH   A O    1 
HETATM 6933 O O    . HOH   D 3 .   ? 37.679 -8.745  -3.349  1.00 24.63 ?  455 HOH   A O    1 
HETATM 6934 O O    . HOH   D 3 .   ? 16.044 -14.110 20.037  1.00 54.17 ?  456 HOH   A O    1 
HETATM 6935 O O    . HOH   D 3 .   ? 18.331 -15.913 16.222  1.00 49.88 ?  457 HOH   A O    1 
HETATM 6936 O O    . HOH   D 3 .   ? 20.595 -17.560 24.799  1.00 57.31 ?  458 HOH   A O    1 
HETATM 6937 O O    A HOH   D 3 .   ? 14.012 -0.177  3.392   0.48 23.23 ?  459 HOH   A O    1 
HETATM 6938 O O    . HOH   D 3 .   ? 29.788 -1.870  -12.747 1.00 47.32 ?  460 HOH   A O    1 
HETATM 6939 O O    A HOH   D 3 .   ? 25.447 8.292   -4.893  0.48 29.69 ?  461 HOH   A O    1 
HETATM 6940 O O    . HOH   D 3 .   ? 29.726 -16.001 10.834  1.00 37.16 ?  462 HOH   A O    1 
HETATM 6941 O O    . HOH   D 3 .   ? 32.323 -15.863 10.867  1.00 32.93 ?  463 HOH   A O    1 
HETATM 6942 O O    . HOH   D 3 .   ? 27.942 7.091   -6.772  1.00 45.44 ?  464 HOH   A O    1 
HETATM 6943 O O    . HOH   D 3 .   ? 24.869 5.828   20.690  1.00 51.14 ?  465 HOH   A O    1 
HETATM 6944 O O    B HOH   D 3 .   ? 24.140 7.504   -4.877  0.52 28.24 ?  466 HOH   A O    1 
HETATM 6945 O O    . HOH   D 3 .   ? 19.767 -17.315 -5.050  1.00 25.70 ?  467 HOH   A O    1 
HETATM 6946 O O    . HOH   D 3 .   ? 23.011 -22.371 -3.122  1.00 43.53 ?  468 HOH   A O    1 
HETATM 6947 O O    . HOH   D 3 .   ? 26.953 11.906  -1.594  1.00 39.42 ?  469 HOH   A O    1 
HETATM 6948 O O    B HOH   D 3 .   ? 22.515 13.832  -2.490  0.52 25.78 ?  470 HOH   A O    1 
HETATM 6949 O O    . HOH   D 3 .   ? 15.639 -21.411 3.652   1.00 33.01 ?  471 HOH   A O    1 
HETATM 6950 O O    . HOH   D 3 .   ? 10.867 -14.796 -6.165  1.00 37.44 ?  472 HOH   A O    1 
HETATM 6951 O O    . HOH   D 3 .   ? 24.586 14.825  7.778   1.00 45.37 ?  473 HOH   A O    1 
HETATM 6952 O O    . HOH   D 3 .   ? 18.835 11.156  11.090  1.00 36.07 ?  474 HOH   A O    1 
HETATM 6953 O O    . HOH   D 3 .   ? 39.563 -7.015  -3.550  1.00 45.32 ?  475 HOH   A O    1 
HETATM 6954 O O    . HOH   D 3 .   ? 27.423 -11.166 16.451  1.00 39.95 ?  476 HOH   A O    1 
HETATM 6955 O O    B HOH   D 3 .   ? 10.540 -2.133  -6.767  0.52 32.39 ?  477 HOH   A O    1 
HETATM 6956 O O    . HOH   D 3 .   ? 11.948 -12.949 16.616  1.00 60.28 ?  478 HOH   A O    1 
HETATM 6957 O O    . HOH   D 3 .   ? 25.698 10.744  -3.931  1.00 44.24 ?  479 HOH   A O    1 
HETATM 6958 O O    . HOH   D 3 .   ? 28.664 -7.892  -15.311 1.00 50.14 ?  480 HOH   A O    1 
HETATM 6959 O O    . HOH   D 3 .   ? 23.422 13.805  5.504   1.00 22.66 ?  481 HOH   A O    1 
HETATM 6960 O O    . HOH   D 3 .   ? 12.270 1.626   17.215  1.00 45.16 ?  482 HOH   A O    1 
HETATM 6961 O O    A HOH   D 3 .   ? 21.986 5.364   -5.912  0.48 27.32 ?  483 HOH   A O    1 
HETATM 6962 O O    B HOH   D 3 .   ? 22.583 11.500  -3.911  0.52 24.46 ?  484 HOH   A O    1 
HETATM 6963 O O    . HOH   D 3 .   ? 17.957 -16.133 -8.908  1.00 39.88 ?  485 HOH   A O    1 
HETATM 6964 O O    B HOH   D 3 .   ? 20.645 9.862   -4.549  0.52 19.78 ?  486 HOH   A O    1 
HETATM 6965 O O    . HOH   D 3 .   ? 15.675 -16.931 -7.039  1.00 32.80 ?  487 HOH   A O    1 
HETATM 6966 O O    . HOH   D 3 .   ? 28.925 9.018   17.447  1.00 42.17 ?  488 HOH   A O    1 
HETATM 6967 O O    . HOH   D 3 .   ? 35.208 7.571   12.181  1.00 61.01 ?  489 HOH   A O    1 
HETATM 6968 O O    A HOH   D 3 .   ? 23.205 11.920  -4.217  0.48 21.39 ?  490 HOH   A O    1 
HETATM 6969 O O    . HOH   D 3 .   ? 16.787 -20.313 15.955  1.00 35.34 ?  491 HOH   A O    1 
HETATM 6970 O O    . HOH   D 3 .   ? 40.879 -3.970  -0.435  1.00 42.71 ?  492 HOH   A O    1 
HETATM 6971 O O    B HOH   D 3 .   ? 21.456 4.907   -4.975  0.52 16.41 ?  493 HOH   A O    1 
HETATM 6972 O O    . HOH   D 3 .   ? 28.586 -4.574  -12.408 1.00 36.41 ?  494 HOH   A O    1 
HETATM 6973 O O    . HOH   D 3 .   ? 13.875 -10.252 -10.938 1.00 36.42 ?  495 HOH   A O    1 
HETATM 6974 O O    . HOH   D 3 .   ? 30.710 0.758   19.194  1.00 42.43 ?  496 HOH   A O    1 
HETATM 6975 O O    . HOH   D 3 .   ? 44.536 10.449  -1.568  1.00 34.01 ?  497 HOH   A O    1 
HETATM 6976 O O    . HOH   D 3 .   ? 31.457 -0.489  -10.680 1.00 33.68 ?  498 HOH   A O    1 
HETATM 6977 O O    . HOH   D 3 .   ? 8.113  -3.031  -5.813  1.00 51.00 ?  499 HOH   A O    1 
HETATM 6978 O O    . HOH   D 3 .   ? 18.379 -23.000 1.872   1.00 58.87 ?  500 HOH   A O    1 
HETATM 6979 O O    . HOH   D 3 .   ? 15.999 -6.692  -11.949 1.00 40.22 ?  501 HOH   A O    1 
HETATM 6980 O O    . HOH   D 3 .   ? 41.826 9.343   -4.009  1.00 31.06 ?  502 HOH   A O    1 
HETATM 6981 O O    . HOH   D 3 .   ? 39.198 2.385   7.333   1.00 35.44 ?  503 HOH   A O    1 
HETATM 6982 O O    . HOH   D 3 .   ? 17.297 -18.660 19.713  1.00 63.23 ?  504 HOH   A O    1 
HETATM 6983 O O    . HOH   D 3 .   ? 23.200 -12.685 19.310  1.00 59.26 ?  505 HOH   A O    1 
HETATM 6984 O O    B HOH   D 3 .   ? 5.016  6.273   1.417   0.52 20.84 ?  506 HOH   A O    1 
HETATM 6985 O O    . HOH   D 3 .   ? 20.051 -22.169 4.253   1.00 34.32 ?  507 HOH   A O    1 
HETATM 6986 O O    . HOH   D 3 .   ? 13.946 -25.100 8.754   1.00 35.63 ?  508 HOH   A O    1 
HETATM 6987 O O    . HOH   D 3 .   ? 16.074 -23.198 5.793   1.00 40.63 ?  509 HOH   A O    1 
HETATM 6988 O O    . HOH   D 3 .   ? 40.630 -0.275  -7.853  1.00 37.13 ?  510 HOH   A O    1 
HETATM 6989 O O    . HOH   D 3 .   ? 30.939 5.784   -14.795 1.00 36.28 ?  511 HOH   A O    1 
HETATM 6990 O O    . HOH   D 3 .   ? 37.344 -6.545  7.609   1.00 29.75 ?  512 HOH   A O    1 
HETATM 6991 O O    . HOH   D 3 .   ? 39.438 -0.020  6.584   1.00 36.76 ?  513 HOH   A O    1 
HETATM 6992 O O    . HOH   D 3 .   ? 30.703 -5.723  -11.917 1.00 50.88 ?  514 HOH   A O    1 
HETATM 6993 O O    . HOH   D 3 .   ? 22.992 -23.592 1.611   1.00 41.27 ?  515 HOH   A O    1 
HETATM 6994 O O    . HOH   D 3 .   ? 28.999 14.495  0.791   1.00 57.06 ?  516 HOH   A O    1 
HETATM 6995 O O    . HOH   D 3 .   ? 37.984 14.010  6.771   1.00 45.05 ?  517 HOH   A O    1 
HETATM 6996 O O    B HOH   D 3 .   ? 21.417 7.625   -5.623  0.52 32.65 ?  518 HOH   A O    1 
HETATM 6997 O O    . HOH   D 3 .   ? 20.402 -16.160 -7.395  1.00 29.36 ?  519 HOH   A O    1 
HETATM 6998 O O    B HOH   D 3 .   ? 7.638  6.843   2.216   0.52 22.46 ?  520 HOH   A O    1 
HETATM 6999 O O    . HOH   D 3 .   ? 36.428 -6.382  10.330  1.00 55.63 ?  521 HOH   A O    1 
HETATM 7000 O O    . HOH   D 3 .   ? 21.995 -23.926 4.455   1.00 29.92 ?  522 HOH   A O    1 
HETATM 7001 O O    . HOH   D 3 .   ? 17.321 -6.611  -14.200 1.00 41.42 ?  523 HOH   A O    1 
HETATM 7002 O O    . HOH   D 3 .   ? 14.775 8.544   4.950   1.00 47.24 ?  524 HOH   A O    1 
HETATM 7003 O O    . HOH   D 3 .   ? 24.055 9.146   -7.221  1.00 51.14 ?  525 HOH   A O    1 
HETATM 7004 O O    . HOH   D 3 .   ? 15.670 -12.037 27.377  1.00 49.99 ?  526 HOH   A O    1 
HETATM 7005 O O    . HOH   D 3 .   ? 16.312 -21.040 18.850  1.00 43.30 ?  527 HOH   A O    1 
HETATM 7006 O O    . HOH   D 3 .   ? 14.788 -22.805 19.794  1.00 39.52 ?  528 HOH   A O    1 
HETATM 7007 O O    . HOH   E 3 .   ? 29.813 -22.326 5.605   1.00 22.72 ?  201 HOH   B O    1 
HETATM 7008 O O    . HOH   E 3 .   ? 52.814 -13.473 -20.302 1.00 36.88 ?  202 HOH   B O    1 
HETATM 7009 O O    . HOH   E 3 .   ? 37.877 -39.361 -0.093  1.00 45.14 ?  203 HOH   B O    1 
HETATM 7010 O O    . HOH   E 3 .   ? 41.355 -7.726  5.432   1.00 45.22 ?  204 HOH   B O    1 
HETATM 7011 O O    . HOH   E 3 .   ? 27.618 -29.115 -1.724  1.00 37.99 ?  205 HOH   B O    1 
HETATM 7012 O O    . HOH   E 3 .   ? 41.511 -36.189 -17.010 1.00 39.89 ?  206 HOH   B O    1 
HETATM 7013 O O    . HOH   E 3 .   ? 48.041 -6.844  15.534  1.00 28.61 ?  207 HOH   B O    1 
HETATM 7014 O O    . HOH   E 3 .   ? 57.687 -24.510 5.125   1.00 42.62 ?  208 HOH   B O    1 
HETATM 7015 O O    . HOH   E 3 .   ? 59.020 -18.571 6.901   1.00 37.52 ?  209 HOH   B O    1 
HETATM 7016 O O    . HOH   E 3 .   ? 50.134 -3.315  7.120   1.00 41.21 ?  210 HOH   B O    1 
HETATM 7017 O O    . HOH   E 3 .   ? 54.434 -9.438  -8.710  1.00 22.13 ?  211 HOH   B O    1 
HETATM 7018 O O    . HOH   E 3 .   ? 29.884 -26.171 4.171   1.00 30.28 ?  212 HOH   B O    1 
HETATM 7019 O O    . HOH   E 3 .   ? 32.775 -43.815 -11.212 1.00 25.16 ?  213 HOH   B O    1 
HETATM 7020 O O    . HOH   E 3 .   ? 30.161 -41.027 -7.960  1.00 21.02 ?  214 HOH   B O    1 
HETATM 7021 O O    . HOH   E 3 .   ? 27.842 -41.819 -15.082 1.00 38.17 ?  215 HOH   B O    1 
HETATM 7022 O O    . HOH   E 3 .   ? 47.309 -7.363  -3.873  1.00 42.37 ?  216 HOH   B O    1 
HETATM 7023 O O    . HOH   E 3 .   ? 30.467 -42.214 -10.503 1.00 35.15 ?  217 HOH   B O    1 
HETATM 7024 O O    . HOH   E 3 .   ? 56.317 -19.652 7.153   1.00 32.10 ?  218 HOH   B O    1 
HETATM 7025 O O    . HOH   E 3 .   ? 37.043 -19.860 -18.036 1.00 42.89 ?  219 HOH   B O    1 
HETATM 7026 O O    . HOH   E 3 .   ? 58.175 -12.791 8.378   1.00 36.60 ?  220 HOH   B O    1 
HETATM 7027 O O    . HOH   E 3 .   ? 56.565 -30.777 -7.682  1.00 33.24 ?  221 HOH   B O    1 
HETATM 7028 O O    . HOH   E 3 .   ? 55.387 -16.659 -14.308 1.00 33.32 ?  222 HOH   B O    1 
HETATM 7029 O O    . HOH   E 3 .   ? 34.468 -36.351 -7.068  1.00 21.76 ?  223 HOH   B O    1 
HETATM 7030 O O    . HOH   E 3 .   ? 50.593 -6.080  0.228   1.00 32.36 ?  224 HOH   B O    1 
HETATM 7031 O O    . HOH   E 3 .   ? 50.697 -12.955 -0.520  1.00 14.18 ?  225 HOH   B O    1 
HETATM 7032 O O    . HOH   E 3 .   ? 41.486 -39.292 -14.771 1.00 26.14 ?  226 HOH   B O    1 
HETATM 7033 O O    . HOH   E 3 .   ? 35.937 -43.380 -8.232  1.00 42.61 ?  227 HOH   B O    1 
HETATM 7034 O O    . HOH   E 3 .   ? 44.454 -27.793 -0.662  1.00 24.64 ?  228 HOH   B O    1 
HETATM 7035 O O    . HOH   E 3 .   ? 49.384 -22.768 -19.690 1.00 52.70 ?  229 HOH   B O    1 
HETATM 7036 O O    . HOH   E 3 .   ? 30.889 -28.633 4.404   1.00 31.80 ?  230 HOH   B O    1 
HETATM 7037 O O    . HOH   E 3 .   ? 57.351 -16.325 -12.168 1.00 19.23 ?  231 HOH   B O    1 
HETATM 7038 O O    . HOH   E 3 .   ? 35.045 -7.967  -3.071  1.00 20.58 ?  232 HOH   B O    1 
HETATM 7039 O O    . HOH   E 3 .   ? 25.357 -25.801 -1.182  1.00 33.40 ?  233 HOH   B O    1 
HETATM 7040 O O    . HOH   E 3 .   ? 57.070 -26.839 -7.594  1.00 46.48 ?  234 HOH   B O    1 
HETATM 7041 O O    . HOH   E 3 .   ? 34.725 -24.516 13.812  1.00 43.79 ?  235 HOH   B O    1 
HETATM 7042 O O    . HOH   E 3 .   ? 39.323 -10.879 6.121   1.00 26.77 ?  236 HOH   B O    1 
HETATM 7043 O O    . HOH   E 3 .   ? 45.070 -34.901 6.948   1.00 48.78 ?  237 HOH   B O    1 
HETATM 7044 O O    . HOH   E 3 .   ? 50.853 -39.855 -8.015  1.00 42.55 ?  238 HOH   B O    1 
HETATM 7045 O O    . HOH   E 3 .   ? 58.105 -10.692 -4.063  1.00 24.91 ?  239 HOH   B O    1 
HETATM 7046 O O    . HOH   E 3 .   ? 44.365 -7.009  1.970   1.00 37.08 ?  240 HOH   B O    1 
HETATM 7047 O O    . HOH   E 3 .   ? 39.443 -11.092 0.364   1.00 19.49 ?  241 HOH   B O    1 
HETATM 7048 O O    . HOH   E 3 .   ? 46.309 -1.519  13.197  1.00 30.58 ?  242 HOH   B O    1 
HETATM 7049 O O    . HOH   E 3 .   ? 40.514 -16.033 14.098  1.00 27.74 ?  243 HOH   B O    1 
HETATM 7050 O O    . HOH   E 3 .   ? 48.412 -36.528 -15.432 1.00 50.44 ?  244 HOH   B O    1 
HETATM 7051 O O    . HOH   E 3 .   ? 34.266 -18.309 11.467  1.00 28.01 ?  245 HOH   B O    1 
HETATM 7052 O O    . HOH   E 3 .   ? 51.598 -6.461  4.313   1.00 22.67 ?  246 HOH   B O    1 
HETATM 7053 O O    . HOH   E 3 .   ? 42.874 -20.331 -20.660 1.00 36.61 ?  247 HOH   B O    1 
HETATM 7054 O O    . HOH   E 3 .   ? 38.403 -11.058 -2.267  1.00 20.86 ?  248 HOH   B O    1 
HETATM 7055 O O    . HOH   E 3 .   ? 28.355 -19.663 -13.102 1.00 26.75 ?  249 HOH   B O    1 
HETATM 7056 O O    . HOH   E 3 .   ? 57.574 -24.352 -3.771  1.00 22.59 ?  250 HOH   B O    1 
HETATM 7057 O O    . HOH   E 3 .   ? 42.539 -25.330 2.769   1.00 18.19 ?  251 HOH   B O    1 
HETATM 7058 O O    . HOH   E 3 .   ? 34.860 -33.314 -19.039 1.00 40.36 ?  252 HOH   B O    1 
HETATM 7059 O O    . HOH   E 3 .   ? 44.828 -43.642 -10.280 1.00 30.18 ?  253 HOH   B O    1 
HETATM 7060 O O    . HOH   E 3 .   ? 38.347 -12.172 -16.205 1.00 50.14 ?  254 HOH   B O    1 
HETATM 7061 O O    . HOH   E 3 .   ? 40.285 -12.777 -11.490 1.00 17.48 ?  255 HOH   B O    1 
HETATM 7062 O O    . HOH   E 3 .   ? 42.591 -22.830 3.880   1.00 14.02 ?  256 HOH   B O    1 
HETATM 7063 O O    . HOH   E 3 .   ? 41.298 -9.531  13.152  1.00 24.55 ?  257 HOH   B O    1 
HETATM 7064 O O    . HOH   E 3 .   ? 29.675 -25.219 -10.712 1.00 19.67 ?  258 HOH   B O    1 
HETATM 7065 O O    . HOH   E 3 .   ? 51.460 -13.796 11.022  1.00 27.78 ?  259 HOH   B O    1 
HETATM 7066 O O    . HOH   E 3 .   ? 27.110 -31.819 -9.859  1.00 21.69 ?  260 HOH   B O    1 
HETATM 7067 O O    . HOH   E 3 .   ? 31.701 -17.812 -14.440 1.00 32.70 ?  261 HOH   B O    1 
HETATM 7068 O O    . HOH   E 3 .   ? 42.924 -43.281 -8.033  1.00 30.85 ?  262 HOH   B O    1 
HETATM 7069 O O    . HOH   E 3 .   ? 56.062 -23.653 -14.677 1.00 32.47 ?  263 HOH   B O    1 
HETATM 7070 O O    . HOH   E 3 .   ? 30.794 -15.640 2.671   1.00 16.29 ?  264 HOH   B O    1 
HETATM 7071 O O    . HOH   E 3 .   ? 48.001 -22.724 5.842   1.00 21.27 ?  265 HOH   B O    1 
HETATM 7072 O O    . HOH   E 3 .   ? 43.316 -15.808 -12.154 1.00 16.37 ?  266 HOH   B O    1 
HETATM 7073 O O    . HOH   E 3 .   ? 38.851 -11.852 12.351  1.00 43.63 ?  267 HOH   B O    1 
HETATM 7074 O O    . HOH   E 3 .   ? 43.080 -32.422 -17.019 1.00 29.12 ?  268 HOH   B O    1 
HETATM 7075 O O    . HOH   E 3 .   ? 28.403 -30.971 -14.482 1.00 32.02 ?  269 HOH   B O    1 
HETATM 7076 O O    . HOH   E 3 .   ? 57.368 -9.212  1.346   1.00 21.85 ?  270 HOH   B O    1 
HETATM 7077 O O    . HOH   E 3 .   ? 47.031 -33.929 -4.567  1.00 21.45 ?  271 HOH   B O    1 
HETATM 7078 O O    . HOH   E 3 .   ? 42.286 -9.837  9.355   1.00 23.00 ?  272 HOH   B O    1 
HETATM 7079 O O    . HOH   E 3 .   ? 41.149 -5.453  11.481  1.00 51.91 ?  273 HOH   B O    1 
HETATM 7080 O O    . HOH   E 3 .   ? 46.852 -29.467 9.909   1.00 35.75 ?  274 HOH   B O    1 
HETATM 7081 O O    . HOH   E 3 .   ? 49.223 -28.703 -6.768  1.00 18.44 ?  275 HOH   B O    1 
HETATM 7082 O O    . HOH   E 3 .   ? 47.884 -24.444 -17.705 1.00 35.43 ?  276 HOH   B O    1 
HETATM 7083 O O    . HOH   E 3 .   ? 52.573 -10.360 12.886  1.00 24.93 ?  277 HOH   B O    1 
HETATM 7084 O O    . HOH   E 3 .   ? 28.207 -34.358 -9.267  1.00 19.28 ?  278 HOH   B O    1 
HETATM 7085 O O    . HOH   E 3 .   ? 27.897 -22.902 -7.927  1.00 20.10 ?  279 HOH   B O    1 
HETATM 7086 O O    . HOH   E 3 .   ? 59.738 -15.140 8.105   1.00 35.19 ?  280 HOH   B O    1 
HETATM 7087 O O    . HOH   E 3 .   ? 56.844 -8.630  8.419   1.00 20.06 ?  281 HOH   B O    1 
HETATM 7088 O O    . HOH   E 3 .   ? 33.487 -15.323 -13.916 1.00 24.75 ?  282 HOH   B O    1 
HETATM 7089 O O    . HOH   E 3 .   ? 41.849 -23.359 9.339   1.00 23.49 ?  283 HOH   B O    1 
HETATM 7090 O O    . HOH   E 3 .   ? 48.652 -19.960 5.966   1.00 16.06 ?  284 HOH   B O    1 
HETATM 7091 O O    . HOH   E 3 .   ? 45.177 -33.408 -15.842 1.00 26.55 ?  285 HOH   B O    1 
HETATM 7092 O O    . HOH   E 3 .   ? 49.730 -24.795 5.846   1.00 37.47 ?  286 HOH   B O    1 
HETATM 7093 O O    . HOH   E 3 .   ? 34.396 -12.714 2.687   1.00 30.74 ?  287 HOH   B O    1 
HETATM 7094 O O    . HOH   E 3 .   ? 27.491 -26.686 -15.487 1.00 35.75 ?  288 HOH   B O    1 
HETATM 7095 O O    . HOH   E 3 .   ? 29.756 -34.193 -0.363  1.00 40.68 ?  289 HOH   B O    1 
HETATM 7096 O O    . HOH   E 3 .   ? 53.525 -12.667 -22.218 1.00 35.23 ?  290 HOH   B O    1 
HETATM 7097 O O    . HOH   E 3 .   ? 48.348 -25.014 3.189   1.00 15.33 ?  291 HOH   B O    1 
HETATM 7098 O O    . HOH   E 3 .   ? 46.556 -31.199 -4.692  1.00 24.74 ?  292 HOH   B O    1 
HETATM 7099 O O    . HOH   E 3 .   ? 49.647 -0.452  10.223  1.00 33.69 ?  293 HOH   B O    1 
HETATM 7100 O O    . HOH   E 3 .   ? 42.422 -34.644 3.871   1.00 28.58 ?  294 HOH   B O    1 
HETATM 7101 O O    . HOH   E 3 .   ? 51.110 -37.662 -9.498  1.00 30.99 ?  295 HOH   B O    1 
HETATM 7102 O O    . HOH   E 3 .   ? 37.387 -17.842 13.125  1.00 33.94 ?  296 HOH   B O    1 
HETATM 7103 O O    . HOH   E 3 .   ? 36.689 -12.725 -1.449  1.00 31.37 ?  297 HOH   B O    1 
HETATM 7104 O O    . HOH   E 3 .   ? 56.996 -12.073 12.372  1.00 46.19 ?  298 HOH   B O    1 
HETATM 7105 O O    . HOH   E 3 .   ? 44.569 -27.427 2.083   1.00 18.64 ?  299 HOH   B O    1 
HETATM 7106 O O    . HOH   E 3 .   ? 40.191 -10.871 -9.501  1.00 19.75 ?  300 HOH   B O    1 
HETATM 7107 O O    . HOH   E 3 .   ? 62.637 -13.541 4.775   1.00 31.80 ?  301 HOH   B O    1 
HETATM 7108 O O    . HOH   E 3 .   ? 42.344 -9.804  -14.822 1.00 43.58 ?  302 HOH   B O    1 
HETATM 7109 O O    . HOH   E 3 .   ? 42.642 -12.302 -18.465 1.00 32.58 ?  303 HOH   B O    1 
HETATM 7110 O O    . HOH   E 3 .   ? 43.979 -29.321 -4.619  1.00 26.44 ?  304 HOH   B O    1 
HETATM 7111 O O    . HOH   E 3 .   ? 25.896 -21.429 -3.429  1.00 19.24 ?  305 HOH   B O    1 
HETATM 7112 O O    . HOH   E 3 .   ? 52.380 -29.272 -12.991 1.00 27.23 ?  306 HOH   B O    1 
HETATM 7113 O O    . HOH   E 3 .   ? 43.170 -34.435 0.211   1.00 25.96 ?  307 HOH   B O    1 
HETATM 7114 O O    . HOH   E 3 .   ? 53.469 -30.129 4.587   1.00 20.77 ?  308 HOH   B O    1 
HETATM 7115 O O    . HOH   E 3 .   ? 53.079 -16.151 -12.678 1.00 29.37 ?  309 HOH   B O    1 
HETATM 7116 O O    . HOH   E 3 .   ? 43.135 -21.341 10.743  1.00 18.52 ?  310 HOH   B O    1 
HETATM 7117 O O    . HOH   E 3 .   ? 52.480 -35.734 -8.596  1.00 34.39 ?  311 HOH   B O    1 
HETATM 7118 O O    . HOH   E 3 .   ? 41.702 -8.068  1.380   1.00 25.97 ?  312 HOH   B O    1 
HETATM 7119 O O    . HOH   E 3 .   ? 37.823 -10.240 -10.750 1.00 20.67 ?  313 HOH   B O    1 
HETATM 7120 O O    . HOH   E 3 .   ? 45.786 -40.358 -3.347  1.00 33.78 ?  314 HOH   B O    1 
HETATM 7121 O O    . HOH   E 3 .   ? 34.946 -33.608 4.675   1.00 34.65 ?  315 HOH   B O    1 
HETATM 7122 O O    . HOH   E 3 .   ? 51.688 -6.008  -7.926  1.00 52.57 ?  316 HOH   B O    1 
HETATM 7123 O O    . HOH   E 3 .   ? 38.297 -12.628 7.929   1.00 20.09 ?  317 HOH   B O    1 
HETATM 7124 O O    . HOH   E 3 .   ? 26.296 -21.010 -6.164  1.00 18.87 ?  318 HOH   B O    1 
HETATM 7125 O O    . HOH   E 3 .   ? 47.254 -24.377 8.252   1.00 28.15 ?  319 HOH   B O    1 
HETATM 7126 O O    . HOH   E 3 .   ? 37.246 -35.609 7.358   1.00 35.87 ?  320 HOH   B O    1 
HETATM 7127 O O    . HOH   E 3 .   ? 44.170 -1.717  7.624   1.00 50.60 ?  321 HOH   B O    1 
HETATM 7128 O O    . HOH   E 3 .   ? 44.619 -24.542 9.607   1.00 24.19 ?  322 HOH   B O    1 
HETATM 7129 O O    . HOH   E 3 .   ? 51.283 -33.150 -10.781 1.00 46.15 ?  323 HOH   B O    1 
HETATM 7130 O O    . HOH   E 3 .   ? 59.902 -17.231 -10.475 1.00 34.79 ?  324 HOH   B O    1 
HETATM 7131 O O    . HOH   E 3 .   ? 32.752 -34.551 -5.761  1.00 19.24 ?  325 HOH   B O    1 
HETATM 7132 O O    . HOH   E 3 .   ? 37.014 -30.586 -20.958 1.00 34.25 ?  326 HOH   B O    1 
HETATM 7133 O O    . HOH   E 3 .   ? 48.557 -12.030 -14.095 1.00 29.10 ?  327 HOH   B O    1 
HETATM 7134 O O    . HOH   E 3 .   ? 36.693 -12.338 4.325   1.00 19.57 ?  328 HOH   B O    1 
HETATM 7135 O O    . HOH   E 3 .   ? 43.413 -15.461 18.160  1.00 32.75 ?  329 HOH   B O    1 
HETATM 7136 O O    . HOH   E 3 .   ? 57.442 -21.890 3.526   1.00 33.43 ?  330 HOH   B O    1 
HETATM 7137 O O    . HOH   E 3 .   ? 33.618 -31.051 11.094  1.00 40.83 ?  331 HOH   B O    1 
HETATM 7138 O O    . HOH   E 3 .   ? 38.419 -9.392  -13.290 1.00 32.64 ?  332 HOH   B O    1 
HETATM 7139 O O    . HOH   E 3 .   ? 62.898 -20.073 -0.715  1.00 40.44 ?  333 HOH   B O    1 
HETATM 7140 O O    . HOH   E 3 .   ? 47.437 -27.399 2.098   1.00 17.73 ?  334 HOH   B O    1 
HETATM 7141 O O    . HOH   E 3 .   ? 36.986 -45.108 -9.658  1.00 39.77 ?  335 HOH   B O    1 
HETATM 7142 O O    . HOH   E 3 .   ? 27.749 -14.773 -9.548  1.00 41.24 ?  336 HOH   B O    1 
HETATM 7143 O O    . HOH   E 3 .   ? 47.954 -32.704 -16.633 1.00 45.37 ?  337 HOH   B O    1 
HETATM 7144 O O    . HOH   E 3 .   ? 42.873 -43.642 -14.202 1.00 41.59 ?  338 HOH   B O    1 
HETATM 7145 O O    . HOH   E 3 .   ? 41.178 -24.567 15.878  1.00 49.66 ?  339 HOH   B O    1 
HETATM 7146 O O    . HOH   E 3 .   ? 46.788 -19.803 12.430  1.00 35.13 ?  340 HOH   B O    1 
HETATM 7147 O O    . HOH   E 3 .   ? 37.026 -15.142 -16.518 1.00 46.34 ?  341 HOH   B O    1 
HETATM 7148 O O    . HOH   E 3 .   ? 34.439 -10.263 7.797   1.00 25.23 ?  342 HOH   B O    1 
HETATM 7149 O O    . HOH   E 3 .   ? 39.700 -44.172 -11.106 1.00 38.03 ?  343 HOH   B O    1 
HETATM 7150 O O    . HOH   E 3 .   ? 28.838 -42.991 -12.253 1.00 47.79 ?  344 HOH   B O    1 
HETATM 7151 O O    . HOH   E 3 .   ? 32.945 -14.592 1.050   1.00 25.27 ?  345 HOH   B O    1 
HETATM 7152 O O    . HOH   E 3 .   ? 45.584 -36.312 -16.035 1.00 39.17 ?  346 HOH   B O    1 
HETATM 7153 O O    . HOH   E 3 .   ? 38.530 -22.282 15.083  1.00 49.07 ?  347 HOH   B O    1 
HETATM 7154 O O    . HOH   E 3 .   ? 62.436 -20.158 -4.766  1.00 41.42 ?  348 HOH   B O    1 
HETATM 7155 O O    . HOH   E 3 .   ? 33.557 -9.751  -8.897  1.00 35.79 ?  349 HOH   B O    1 
HETATM 7156 O O    . HOH   E 3 .   ? 40.303 -43.510 -8.991  1.00 29.35 ?  350 HOH   B O    1 
HETATM 7157 O O    . HOH   E 3 .   ? 39.609 -23.802 -20.307 1.00 39.65 ?  351 HOH   B O    1 
HETATM 7158 O O    . HOH   E 3 .   ? 27.659 -26.578 -0.447  1.00 33.48 ?  352 HOH   B O    1 
HETATM 7159 O O    . HOH   E 3 .   ? 44.133 -37.480 -17.550 1.00 37.52 ?  353 HOH   B O    1 
HETATM 7160 O O    . HOH   E 3 .   ? 55.625 -8.276  10.876  1.00 25.08 ?  354 HOH   B O    1 
HETATM 7161 O O    . HOH   E 3 .   ? 34.056 -7.731  11.461  1.00 43.21 ?  355 HOH   B O    1 
HETATM 7162 O O    . HOH   E 3 .   ? 36.082 -8.454  -9.705  1.00 42.57 ?  356 HOH   B O    1 
HETATM 7163 O O    . HOH   E 3 .   ? 56.465 -7.243  2.973   1.00 28.61 ?  357 HOH   B O    1 
HETATM 7164 O O    . HOH   E 3 .   ? 56.839 -21.532 -16.314 1.00 41.40 ?  358 HOH   B O    1 
HETATM 7165 O O    . HOH   E 3 .   ? 43.141 -12.684 -21.072 1.00 47.09 ?  359 HOH   B O    1 
HETATM 7166 O O    . HOH   E 3 .   ? 23.060 -23.488 6.804   1.00 42.70 ?  360 HOH   B O    1 
HETATM 7167 O O    . HOH   E 3 .   ? 61.454 -19.853 1.801   1.00 40.37 ?  361 HOH   B O    1 
HETATM 7168 O O    . HOH   E 3 .   ? 27.078 -25.943 -11.152 1.00 37.60 ?  362 HOH   B O    1 
HETATM 7169 O O    . HOH   E 3 .   ? 40.215 -8.748  9.884   1.00 40.67 ?  363 HOH   B O    1 
HETATM 7170 O O    . HOH   E 3 .   ? 40.355 -11.312 -13.878 1.00 32.32 ?  364 HOH   B O    1 
HETATM 7171 O O    . HOH   E 3 .   ? 48.175 -26.366 8.826   1.00 46.85 ?  365 HOH   B O    1 
HETATM 7172 O O    . HOH   E 3 .   ? 54.084 -5.705  2.971   1.00 38.60 ?  366 HOH   B O    1 
HETATM 7173 O O    . HOH   E 3 .   ? 62.836 -12.523 6.885   1.00 43.58 ?  367 HOH   B O    1 
HETATM 7174 O O    . HOH   E 3 .   ? 58.826 -10.377 9.219   1.00 37.19 ?  368 HOH   B O    1 
HETATM 7175 O O    . HOH   E 3 .   ? 36.123 -8.555  9.053   1.00 34.12 ?  369 HOH   B O    1 
HETATM 7176 O O    . HOH   E 3 .   ? 39.817 -7.087  7.857   1.00 44.09 ?  370 HOH   B O    1 
HETATM 7177 O O    . HOH   E 3 .   ? 55.992 -7.834  -0.695  1.00 38.35 ?  371 HOH   B O    1 
HETATM 7178 O O    . HOH   E 3 .   ? 52.024 -12.951 13.280  1.00 35.76 ?  372 HOH   B O    1 
HETATM 7179 O O    . HOH   E 3 .   ? 41.779 -10.106 -17.434 1.00 55.32 ?  373 HOH   B O    1 
HETATM 7180 O O    . HOH   E 3 .   ? 32.550 -23.503 14.102  1.00 46.29 ?  374 HOH   B O    1 
HETATM 7181 O O    . HOH   E 3 .   ? 41.806 -6.755  -4.914  1.00 47.79 ?  375 HOH   B O    1 
HETATM 7182 O O    . HOH   E 3 .   ? 37.961 -10.446 9.968   1.00 30.21 ?  376 HOH   B O    1 
HETATM 7183 O O    . HOH   E 3 .   ? 44.084 -5.641  -3.482  1.00 45.20 ?  377 HOH   B O    1 
HETATM 7184 O O    . HOH   E 3 .   ? 42.630 -17.097 -23.082 1.00 52.41 ?  378 HOH   B O    1 
HETATM 7185 O O    . HOH   E 3 .   ? 36.363 -22.767 13.349  1.00 40.28 ?  379 HOH   B O    1 
HETATM 7186 O O    . HOH   E 3 .   ? 52.825 -29.827 7.183   1.00 24.20 ?  380 HOH   B O    1 
HETATM 7187 O O    . HOH   E 3 .   ? 40.243 -7.600  3.086   1.00 46.70 ?  381 HOH   B O    1 
HETATM 7188 O O    . HOH   E 3 .   ? 39.542 -13.915 15.630  1.00 63.28 ?  382 HOH   B O    1 
HETATM 7189 O O    . HOH   E 3 .   ? 41.008 -9.684  15.747  1.00 54.17 ?  383 HOH   B O    1 
HETATM 7190 O O    . HOH   E 3 .   ? 46.823 -5.349  2.817   1.00 42.53 ?  384 HOH   B O    1 
HETATM 7191 O O    . HOH   E 3 .   ? 23.829 -20.784 -7.567  1.00 34.70 ?  385 HOH   B O    1 
HETATM 7192 O O    . HOH   E 3 .   ? 25.717 -18.772 -11.872 1.00 38.69 ?  386 HOH   B O    1 
HETATM 7193 O O    . HOH   E 3 .   ? 60.436 -22.232 3.018   1.00 57.52 ?  387 HOH   B O    1 
HETATM 7194 O O    . HOH   E 3 .   ? 35.166 -20.357 13.303  1.00 37.86 ?  388 HOH   B O    1 
HETATM 7195 O O    . HOH   E 3 .   ? 35.246 -33.586 7.475   1.00 42.99 ?  389 HOH   B O    1 
HETATM 7196 O O    . HOH   E 3 .   ? 40.724 -6.555  -0.879  1.00 29.93 ?  390 HOH   B O    1 
HETATM 7197 O O    . HOH   E 3 .   ? 44.110 -31.787 -3.703  1.00 43.06 ?  391 HOH   B O    1 
HETATM 7198 O O    . HOH   E 3 .   ? 26.519 -27.923 -13.393 1.00 38.99 ?  392 HOH   B O    1 
HETATM 7199 O O    . HOH   E 3 .   ? 27.873 -27.026 2.372   1.00 31.11 ?  393 HOH   B O    1 
HETATM 7200 O O    . HOH   E 3 .   ? 26.796 -30.643 -12.493 1.00 27.77 ?  394 HOH   B O    1 
HETATM 7201 O O    . HOH   E 3 .   ? 50.583 -30.835 8.796   1.00 34.40 ?  395 HOH   B O    1 
HETATM 7202 O O    . HOH   E 3 .   ? 34.226 -33.349 9.713   1.00 42.69 ?  396 HOH   B O    1 
HETATM 7203 O O    . HOH   E 3 .   ? 24.587 -20.636 -10.502 1.00 38.92 ?  397 HOH   B O    1 
HETATM 7204 O O    . HOH   E 3 .   ? 57.767 -6.697  -2.336  1.00 39.97 ?  398 HOH   B O    1 
HETATM 7205 O O    . HOH   E 3 .   ? 45.593 -20.132 15.364  1.00 51.18 ?  399 HOH   B O    1 
HETATM 7206 O O    . HOH   E 3 .   ? 40.817 -11.849 -22.277 1.00 45.38 ?  400 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   . VAL   A 3   ? 0.8219 0.8218 0.9530 -0.0138 -0.0406 0.0797  3   VAL   A N   
2    C CA  . VAL   A 3   ? 0.8175 0.8184 0.9327 -0.0150 -0.0395 0.0794  3   VAL   A CA  
3    C C   . VAL   A 3   ? 0.7696 0.7750 0.8355 -0.0208 -0.0337 0.0753  3   VAL   A C   
4    O O   . VAL   A 3   ? 0.7735 0.7796 0.8579 -0.0192 -0.0371 0.0774  3   VAL   A O   
5    C CB  . VAL   A 3   ? 0.8515 0.8502 0.9863 -0.0118 -0.0431 0.0815  3   VAL   A CB  
6    C CG1 . VAL   A 3   ? 0.8622 0.8599 1.0028 -0.0103 -0.0446 0.0824  3   VAL   A CG1 
7    C CG2 . VAL   A 3   ? 0.8615 0.8597 1.0038 -0.0110 -0.0441 0.0825  3   VAL   A CG2 
16   N N   A ASN   A 4   ? 0.7385 0.7475 0.7675 -0.0239 -0.0286 0.0711  4   ASN   A N   
17   N N   B ASN   A 4   ? 0.7405 0.7471 0.7655 -0.0255 -0.0288 0.0722  4   ASN   A N   
18   C CA  A ASN   A 4   ? 0.7037 0.7173 0.6903 -0.0283 -0.0234 0.0661  4   ASN   A CA  
19   C CA  B ASN   A 4   ? 0.7077 0.7165 0.6864 -0.0312 -0.0236 0.0681  4   ASN   A CA  
20   C C   A ASN   A 4   ? 0.6516 0.6797 0.6444 -0.0396 -0.0128 0.0512  4   ASN   A C   
21   C C   B ASN   A 4   ? 0.6586 0.6799 0.6414 -0.0420 -0.0129 0.0526  4   ASN   A C   
22   O O   A ASN   A 4   ? 0.6541 0.6814 0.6430 -0.0388 -0.0140 0.0513  4   ASN   A O   
23   O O   B ASN   A 4   ? 0.6608 0.6816 0.6394 -0.0417 -0.0142 0.0532  4   ASN   A O   
24   C CB  A ASN   A 4   ? 0.7172 0.7226 0.6531 -0.0228 -0.0283 0.0764  4   ASN   A CB  
25   C CB  B ASN   A 4   ? 0.7204 0.7206 0.6466 -0.0273 -0.0287 0.0799  4   ASN   A CB  
26   C CG  A ASN   A 4   ? 0.7267 0.7255 0.6177 -0.0187 -0.0334 0.0860  4   ASN   A CG  
27   C CG  B ASN   A 4   ? 0.7295 0.7223 0.6089 -0.0245 -0.0341 0.0906  4   ASN   A CG  
28   O OD1 A ASN   A 4   ? 0.7309 0.7265 0.6073 -0.0174 -0.0372 0.0892  4   ASN   A OD1 
29   O OD1 B ASN   A 4   ? 0.7335 0.7228 0.5975 -0.0239 -0.0385 0.0944  4   ASN   A OD1 
30   N ND2 A ASN   A 4   ? 0.7291 0.7260 0.6050 -0.0170 -0.0336 0.0908  4   ASN   A ND2 
31   N ND2 B ASN   A 4   ? 0.7317 0.7226 0.5957 -0.0231 -0.0342 0.0957  4   ASN   A ND2 
44   N N   A SER   A 5   ? 0.5936 0.6378 0.5933 -0.0537 -0.0007 0.0379  5   SER   A N   
45   N N   B SER   A 5   ? 0.6042 0.6392 0.5923 -0.0545 -0.0005 0.0378  5   SER   A N   
46   C CA  A SER   A 5   ? 0.5330 0.5943 0.5400 -0.0687 0.0135  0.0259  5   SER   A CA  
47   C CA  B SER   A 5   ? 0.5471 0.5970 0.5412 -0.0676 0.0150  0.0244  5   SER   A CA  
48   C C   A SER   A 5   ? 0.4661 0.5430 0.4664 -0.0866 0.0261  0.0278  5   SER   A C   
49   C C   B SER   A 5   ? 0.4849 0.5473 0.4702 -0.0821 0.0295  0.0241  5   SER   A C   
50   O O   A SER   A 5   ? 0.4672 0.5443 0.4643 -0.0842 0.0279  0.0228  5   SER   A O   
51   O O   B SER   A 5   ? 0.4856 0.5471 0.4666 -0.0809 0.0340  0.0199  5   SER   A O   
52   C CB  A SER   A 5   ? 0.5384 0.6007 0.5605 -0.0671 0.0157  0.0157  5   SER   A CB  
53   C CB  B SER   A 5   ? 0.5523 0.6037 0.5632 -0.0663 0.0160  0.0143  5   SER   A CB  
54   O OG  A SER   A 5   ? 0.5407 0.6039 0.5708 -0.0671 0.0173  0.0107  5   SER   A OG  
55   O OG  B SER   A 5   ? 0.5545 0.6073 0.5731 -0.0663 0.0168  0.0087  5   SER   A OG  
66   N N   A PHE   A 6   ? 0.3959 0.4888 0.3880 -0.1078 0.0371  0.0401  6   PHE   A N   
67   N N   B PHE   A 6   ? 0.4206 0.4967 0.3966 -0.0977 0.0381  0.0313  6   PHE   A N   
68   C CA  A PHE   A 6   ? 0.3288 0.4342 0.3176 -0.1246 0.0397  0.0551  6   PHE   A CA  
69   C CA  B PHE   A 6   ? 0.3598 0.4461 0.3373 -0.1103 0.0412  0.0414  6   PHE   A CA  
70   C C   A PHE   A 6   ? 0.3069 0.4151 0.3007 -0.1309 0.0435  0.0499  6   PHE   A C   
71   C C   B PHE   A 6   ? 0.3402 0.4260 0.3223 -0.1081 0.0489  0.0420  6   PHE   A C   
72   O O   A PHE   A 6   ? 0.3099 0.4165 0.3216 -0.1331 0.0394  0.0576  6   PHE   A O   
73   O O   B PHE   A 6   ? 0.3442 0.4290 0.3469 -0.1070 0.0518  0.0544  6   PHE   A O   
74   C CB  A PHE   A 6   ? 0.2958 0.4016 0.2771 -0.1236 0.0339  0.0765  6   PHE   A CB  
75   C CB  B PHE   A 6   ? 0.3290 0.4186 0.3080 -0.1152 0.0288  0.0474  6   PHE   A CB  
76   C CG  A PHE   A 6   ? 0.2688 0.3743 0.2470 -0.1161 0.0234  0.0761  6   PHE   A CG  
77   C CG  B PHE   A 6   ? 0.3028 0.3948 0.2864 -0.1163 0.0165  0.0385  6   PHE   A CG  
78   C CD1 A PHE   A 6   ? 0.2552 0.3629 0.2370 -0.1106 0.0132  0.0764  6   PHE   A CD1 
79   C CD1 B PHE   A 6   ? 0.2901 0.3837 0.2775 -0.1167 0.0079  0.0352  6   PHE   A CD1 
80   C CD2 A PHE   A 6   ? 0.2737 0.3659 0.2512 -0.1015 0.0099  0.0696  6   PHE   A CD2 
81   C CD2 B PHE   A 6   ? 0.3042 0.3879 0.2920 -0.1064 0.0078  0.0294  6   PHE   A CD2 
82   C CE1 A PHE   A 6   ? 0.2513 0.3534 0.2285 -0.1080 0.0031  0.0768  6   PHE   A CE1 
83   C CE1 B PHE   A 6   ? 0.2856 0.3761 0.2725 -0.1173 0.0050  0.0344  6   PHE   A CE1 
84   C CE2 A PHE   A 6   ? 0.2698 0.3593 0.2482 -0.0968 0.0028  0.0693  6   PHE   A CE2 
85   C CE2 B PHE   A 6   ? 0.3005 0.3825 0.2896 -0.1041 0.0030  0.0265  6   PHE   A CE2 
86   C CZ  A PHE   A 6   ? 0.2599 0.3521 0.2347 -0.1020 -0.0055 0.0727  6   PHE   A CZ  
87   C CZ  B PHE   A 6   ? 0.2909 0.3769 0.2785 -0.1116 -0.0030 0.0257  6   PHE   A CZ  
106  N N   A SER   A 7   ? 0.2866 0.3944 0.2645 -0.1272 0.0447  0.0366  7   SER   A N   
107  N N   B SER   A 7   ? 0.3202 0.4034 0.2868 -0.1000 0.0473  0.0276  7   SER   A N   
108  C CA  A SER   A 7   ? 0.2768 0.3782 0.2540 -0.1119 0.0476  0.0263  7   SER   A CA  
109  C CA  B SER   A 7   ? 0.3079 0.3848 0.2766 -0.0851 0.0464  0.0116  7   SER   A CA  
110  C C   A SER   A 7   ? 0.2559 0.3550 0.2234 -0.0949 0.0541  0.0268  7   SER   A C   
111  C C   B SER   A 7   ? 0.2888 0.3568 0.2506 -0.0699 0.0517  0.0153  7   SER   A C   
112  O O   A SER   A 7   ? 0.2656 0.3524 0.2309 -0.0918 0.0448  0.0263  7   SER   A O   
113  O O   B SER   A 7   ? 0.2951 0.3557 0.2550 -0.0678 0.0457  0.0124  7   SER   A O   
114  C CB  A SER   A 7   ? 0.2965 0.3872 0.2818 -0.1022 0.0399  0.0197  7   SER   A CB  
115  C CB  B SER   A 7   ? 0.3186 0.3923 0.3020 -0.0788 0.0410  0.0015  7   SER   A CB  
116  O OG  A SER   A 7   ? 0.3102 0.3979 0.2840 -0.0916 0.0355  0.0125  7   SER   A OG  
117  O OG  B SER   A 7   ? 0.3263 0.3974 0.3195 -0.0731 0.0394  -0.0076 7   SER   A OG  
128  N N   A GLY   A 8   ? 0.2272 0.3344 0.2180 -0.0820 0.0572  0.0210  8   GLY   A N   
129  N N   B GLY   A 8   ? 0.2639 0.3314 0.2518 -0.0582 0.0533  0.0123  8   GLY   A N   
130  C CA  A GLY   A 8   ? 0.2154 0.3147 0.2248 -0.0621 0.0466  0.0269  8   GLY   A CA  
131  C CA  B GLY   A 8   ? 0.2476 0.3068 0.2569 -0.0429 0.0429  0.0132  8   GLY   A CA  
132  C C   A GLY   A 8   ? 0.1916 0.2928 0.2281 -0.0484 0.0390  0.0295  8   GLY   A C   
133  C C   B GLY   A 8   ? 0.2183 0.2804 0.2507 -0.0341 0.0361  0.0113  8   GLY   A C   
134  O O   A GLY   A 8   ? 0.1919 0.2915 0.2455 -0.0369 0.0402  0.0135  8   GLY   A O   
135  O O   B GLY   A 8   ? 0.2204 0.2732 0.2550 -0.0279 0.0335  -0.0005 8   GLY   A O   
142  N N   A TYR   A 9   ? 0.1810 0.2716 0.2254 -0.0404 0.0346  0.0494  9   TYR   A N   
143  N N   B TYR   A 9   ? 0.1949 0.2604 0.2408 -0.0295 0.0369  0.0269  9   TYR   A N   
144  C CA  A TYR   A 9   ? 0.1681 0.2456 0.2179 -0.0387 0.0194  0.0497  9   TYR   A CA  
145  C CA  B TYR   A 9   ? 0.1751 0.2415 0.2338 -0.0278 0.0313  0.0287  9   TYR   A CA  
146  C C   A TYR   A 9   ? 0.1671 0.2251 0.2016 -0.0324 0.0177  0.0670  9   TYR   A C   
147  C C   B TYR   A 9   ? 0.1668 0.2180 0.2210 -0.0173 0.0290  0.0353  9   TYR   A C   
148  O O   A TYR   A 9   ? 0.1757 0.2384 0.2195 -0.0203 0.0137  0.0725  9   TYR   A O   
149  O O   B TYR   A 9   ? 0.1708 0.2280 0.2528 -0.0207 0.0150  0.0411  9   TYR   A O   
150  C CB  A TYR   A 9   ? 0.1675 0.2498 0.2267 -0.0298 0.0156  0.0289  9   TYR   A CB  
151  C CB  B TYR   A 9   ? 0.1694 0.2571 0.2380 -0.0367 0.0196  0.0157  9   TYR   A CB  
152  C CG  A TYR   A 9   ? 0.1648 0.2425 0.2128 -0.0168 0.0271  0.0104  9   TYR   A CG  
153  C CG  B TYR   A 9   ? 0.1660 0.2643 0.2146 -0.0373 0.0217  0.0046  9   TYR   A CG  
154  C CD1 A TYR   A 9   ? 0.1666 0.2379 0.2080 -0.0206 0.0348  -0.0101 9   TYR   A CD1 
155  C CD1 B TYR   A 9   ? 0.1761 0.2734 0.2099 -0.0378 0.0228  0.0026  9   TYR   A CD1 
156  C CD2 A TYR   A 9   ? 0.1688 0.2370 0.2184 -0.0135 0.0170  0.0160  9   TYR   A CD2 
157  C CD2 B TYR   A 9   ? 0.1650 0.2622 0.2008 -0.0336 0.0184  -0.0017 9   TYR   A CD2 
158  C CE1 A TYR   A 9   ? 0.1753 0.2379 0.2236 -0.0197 0.0352  -0.0210 9   TYR   A CE1 
159  C CE1 B TYR   A 9   ? 0.1779 0.2722 0.2047 -0.0344 0.0341  -0.0031 9   TYR   A CE1 
160  C CE2 A TYR   A 9   ? 0.1715 0.2342 0.2109 -0.0109 0.0184  0.0042  9   TYR   A CE2 
161  C CE2 B TYR   A 9   ? 0.1636 0.2652 0.1897 -0.0302 0.0311  0.0041  9   TYR   A CE2 
162  C CZ  A TYR   A 9   ? 0.1775 0.2378 0.2266 -0.0209 0.0381  -0.0096 9   TYR   A CZ  
163  C CZ  B TYR   A 9   ? 0.1684 0.2671 0.2101 -0.0330 0.0449  -0.0019 9   TYR   A CZ  
164  O OH  A TYR   A 9   ? 0.1937 0.2421 0.2403 -0.0239 0.0528  -0.0147 9   TYR   A OH  
165  O OH  B TYR   A 9   ? 0.1659 0.2636 0.2413 -0.0374 0.0539  -0.0101 9   TYR   A OH  
184  N N   A LEU   A 10  ? 0.1685 0.2097 0.2112 -0.0340 0.0098  0.0648  10  LEU   A N   
185  N N   B LEU   A 10  ? 0.1722 0.2021 0.2152 -0.0056 0.0276  0.0248  10  LEU   A N   
186  C CA  A LEU   A 10  ? 0.1572 0.1987 0.2193 -0.0373 0.0132  0.0669  10  LEU   A CA  
187  C CA  B LEU   A 10  ? 0.1771 0.1919 0.2170 -0.0075 0.0200  0.0242  10  LEU   A CA  
188  C C   A LEU   A 10  ? 0.1525 0.1877 0.2179 -0.0350 0.0158  0.0626  10  LEU   A C   
189  C C   B LEU   A 10  ? 0.1708 0.1683 0.2154 -0.0154 0.0190  0.0310  10  LEU   A C   
190  O O   A LEU   A 10  ? 0.1587 0.1717 0.2242 -0.0275 0.0249  0.0649  10  LEU   A O   
191  O O   B LEU   A 10  ? 0.1660 0.1589 0.2194 -0.0115 0.0090  0.0373  10  LEU   A O   
192  C CB  A LEU   A 10  ? 0.1521 0.2076 0.2592 -0.0378 -0.0044 0.0639  10  LEU   A CB  
193  C CB  B LEU   A 10  ? 0.1850 0.2052 0.2300 -0.0062 0.0072  0.0100  10  LEU   A CB  
194  C CG  A LEU   A 10  ? 0.1712 0.2203 0.3073 -0.0257 -0.0238 0.0556  10  LEU   A CG  
195  C CG  B LEU   A 10  ? 0.2021 0.2274 0.2748 -0.0001 -0.0076 0.0161  10  LEU   A CG  
196  C CD1 A LEU   A 10  ? 0.1845 0.2167 0.3183 -0.0340 -0.0193 0.0475  10  LEU   A CD1 
197  C CD1 B LEU   A 10  ? 0.2133 0.2398 0.2954 -0.0080 0.0002  0.0195  10  LEU   A CD1 
198  C CD2 A LEU   A 10  ? 0.1891 0.2350 0.3330 -0.0183 -0.0159 0.0487  10  LEU   A CD2 
199  C CD2 B LEU   A 10  ? 0.2184 0.2433 0.3082 0.0143  -0.0301 0.0170  10  LEU   A CD2 
222  N N   A LYS   A 11  ? 0.1588 0.1934 0.2192 -0.0303 0.0148  0.0574  11  LYS   A N   
223  N N   B LYS   A 11  ? 0.1808 0.1640 0.2227 -0.0149 0.0165  0.0177  11  LYS   A N   
224  C CA  A LYS   A 11  ? 0.1615 0.1892 0.2233 -0.0325 0.0096  0.0481  11  LYS   A CA  
225  C CA  B LYS   A 11  ? 0.1771 0.1575 0.2189 -0.0246 0.0228  0.0267  11  LYS   A CA  
226  C C   A LYS   A 11  ? 0.1518 0.1808 0.2283 -0.0346 0.0047  0.0338  11  LYS   A C   
227  C C   B LYS   A 11  ? 0.1644 0.1516 0.2067 -0.0255 0.0279  0.0344  11  LYS   A C   
228  O O   A LYS   A 11  ? 0.1516 0.1870 0.2596 -0.0454 0.0017  0.0269  11  LYS   A O   
229  O O   B LYS   A 11  ? 0.1650 0.1554 0.2179 -0.0217 0.0260  0.0239  11  LYS   A O   
230  C CB  A LYS   A 11  ? 0.1686 0.1936 0.2053 -0.0300 0.0095  0.0464  11  LYS   A CB  
231  C CB  B LYS   A 11  ? 0.1995 0.1607 0.2170 -0.0279 0.0062  0.0226  11  LYS   A CB  
232  C CG  A LYS   A 11  ? 0.1770 0.1940 0.2018 -0.0302 0.0026  0.0409  11  LYS   A CG  
233  C CG  B LYS   A 11  ? 0.2037 0.1631 0.2222 -0.0367 -0.0045 0.0297  11  LYS   A CG  
234  C CD  A LYS   A 11  ? 0.1767 0.1885 0.1910 -0.0331 -0.0021 0.0436  11  LYS   A CD  
235  C CD  B LYS   A 11  ? 0.2191 0.1699 0.2314 -0.0247 -0.0099 0.0407  11  LYS   A CD  
236  C CE  A LYS   A 11  ? 0.1880 0.1882 0.1875 -0.0196 -0.0086 0.0326  11  LYS   A CE  
237  C CE  B LYS   A 11  ? 0.2229 0.1764 0.2344 -0.0190 -0.0121 0.0409  11  LYS   A CE  
238  N NZ  A LYS   A 11  ? 0.1927 0.1897 0.2073 -0.0126 -0.0160 0.0423  11  LYS   A NZ  
239  N NZ  B LYS   A 11  ? 0.2246 0.1759 0.2456 -0.0168 -0.0175 0.0426  11  LYS   A NZ  
266  N N   A LEU   A 12  ? 0.1444 0.1700 0.2150 -0.0331 0.0008  0.0431  12  LEU   A N   
267  N N   B LEU   A 12  ? 0.1635 0.1580 0.2103 -0.0159 0.0260  0.0313  12  LEU   A N   
268  C CA  A LEU   A 12  ? 0.1559 0.1709 0.1992 -0.0154 0.0006  0.0440  12  LEU   A CA  
269  C CA  B LEU   A 12  ? 0.1606 0.1651 0.2064 -0.0139 0.0275  0.0337  12  LEU   A CA  
270  C C   A LEU   A 12  ? 0.1610 0.1642 0.1995 -0.0262 0.0011  0.0375  12  LEU   A C   
271  C C   B LEU   A 12  ? 0.1574 0.1691 0.2181 -0.0142 0.0226  0.0242  12  LEU   A C   
272  O O   A LEU   A 12  ? 0.1717 0.1727 0.2147 -0.0275 0.0097  0.0322  12  LEU   A O   
273  O O   B LEU   A 12  ? 0.1663 0.1739 0.2201 -0.0079 0.0200  0.0280  12  LEU   A O   
274  C CB  A LEU   A 12  ? 0.1726 0.1674 0.1912 -0.0146 -0.0106 0.0425  12  LEU   A CB  
275  C CB  B LEU   A 12  ? 0.1610 0.1669 0.2179 -0.0117 0.0306  0.0270  12  LEU   A CB  
276  C CG  A LEU   A 12  ? 0.1828 0.1636 0.2074 -0.0123 -0.0032 0.0324  12  LEU   A CG  
277  C CG  B LEU   A 12  ? 0.1612 0.1618 0.2479 -0.0100 0.0318  0.0126  12  LEU   A CG  
278  C CD1 A LEU   A 12  ? 0.1936 0.1582 0.2004 0.0029  0.0174  0.0399  12  LEU   A CD1 
279  C CD1 B LEU   A 12  ? 0.1639 0.1737 0.2713 -0.0035 0.0297  0.0147  12  LEU   A CD1 
280  C CD2 A LEU   A 12  ? 0.1849 0.1650 0.2337 -0.0169 -0.0123 0.0115  12  LEU   A CD2 
281  C CD2 B LEU   A 12  ? 0.1608 0.1625 0.2560 -0.0142 0.0342  0.0115  12  LEU   A CD2 
304  N N   A THR   A 13  ? 0.1569 0.1592 0.2045 -0.0238 0.0069  0.0407  13  THR   A N   
305  N N   B THR   A 13  ? 0.1520 0.1666 0.2194 -0.0066 0.0211  0.0173  13  THR   A N   
306  C CA  A THR   A 13  ? 0.1557 0.1658 0.2294 -0.0257 0.0153  0.0362  13  THR   A CA  
307  C CA  B THR   A 13  ? 0.1579 0.1648 0.2299 -0.0106 0.0151  0.0195  13  THR   A CA  
308  C C   A THR   A 13  ? 0.1541 0.1654 0.2455 -0.0323 -0.0017 0.0632  13  THR   A C   
309  C C   B THR   A 13  ? 0.1662 0.1675 0.2373 -0.0006 0.0196  0.0255  13  THR   A C   
310  O O   A THR   A 13  ? 0.1466 0.1780 0.2424 -0.0290 -0.0094 0.0642  13  THR   A O   
311  O O   B THR   A 13  ? 0.1748 0.1763 0.2407 -0.0105 0.0124  0.0368  13  THR   A O   
312  C CB  A THR   A 13  ? 0.1642 0.1754 0.2460 -0.0182 0.0223  0.0365  13  THR   A CB  
313  C CB  B THR   A 13  ? 0.1555 0.1616 0.2208 -0.0114 0.0164  0.0175  13  THR   A CB  
314  O OG1 A THR   A 13  ? 0.1699 0.1722 0.2624 -0.0137 0.0070  0.0416  13  THR   A OG1 
315  O OG1 B THR   A 13  ? 0.1482 0.1673 0.2291 -0.0151 0.0303  0.0220  13  THR   A OG1 
316  C CG2 A THR   A 13  ? 0.1770 0.1850 0.2642 -0.0035 0.0310  0.0274  13  THR   A CG2 
317  C CG2 B THR   A 13  ? 0.1643 0.1688 0.2181 -0.0076 0.0236  0.0148  13  THR   A CG2 
332  N N   A ASP   A 14  ? 0.1629 0.1680 0.2603 -0.0404 -0.0049 0.0720  14  ASP   A N   
333  N N   B ASP   A 14  ? 0.1779 0.1701 0.2540 -0.0049 0.0094  0.0201  14  ASP   A N   
334  C CA  A ASP   A 14  ? 0.1762 0.1837 0.2606 -0.0333 -0.0140 0.0799  14  ASP   A CA  
335  C CA  B ASP   A 14  ? 0.1964 0.1786 0.2799 -0.0090 -0.0018 0.0574  14  ASP   A CA  
336  C C   A ASP   A 14  ? 0.1674 0.1880 0.2410 -0.0257 -0.0090 0.0627  14  ASP   A C   
337  C C   B ASP   A 14  ? 0.1783 0.1828 0.2644 -0.0171 -0.0023 0.0612  14  ASP   A C   
338  O O   A ASP   A 14  ? 0.1755 0.1980 0.2219 -0.0231 -0.0001 0.0640  14  ASP   A O   
339  O O   B ASP   A 14  ? 0.1676 0.1957 0.2714 -0.0300 -0.0127 0.0752  14  ASP   A O   
340  C CB  A ASP   A 14  ? 0.1991 0.2028 0.2894 -0.0223 -0.0343 0.0896  14  ASP   A CB  
341  C CB  B ASP   A 14  ? 0.2346 0.1990 0.3176 -0.0086 -0.0062 0.0639  14  ASP   A CB  
342  C CG  A ASP   A 14  ? 0.2196 0.2233 0.3474 -0.0153 -0.0344 0.0635  14  ASP   A CG  
343  C CG  B ASP   A 14  ? 0.2709 0.2435 0.3754 0.0001  -0.0084 0.0319  14  ASP   A CG  
344  O OD1 A ASP   A 14  ? 0.2289 0.2221 0.3698 -0.0211 -0.0290 0.0727  14  ASP   A OD1 
345  O OD1 B ASP   A 14  ? 0.2879 0.2605 0.3959 0.0056  -0.0192 0.0314  14  ASP   A OD1 
346  O OD2 A ASP   A 14  ? 0.2302 0.2316 0.3626 -0.0212 -0.0508 0.0466  14  ASP   A OD2 
347  O OD2 B ASP   A 14  ? 0.2856 0.2553 0.3996 -0.0020 -0.0075 0.0210  14  ASP   A OD2 
356  N N   A ASN   A 15  ? 0.1549 0.1692 0.2348 -0.0235 -0.0036 0.0496  15  ASN   A N   
357  N N   B ASN   A 15  ? 0.1675 0.1572 0.2402 -0.0117 0.0128  0.0655  15  ASN   A N   
358  C CA  A ASN   A 15  ? 0.1455 0.1601 0.2287 -0.0187 -0.0001 0.0310  15  ASN   A CA  
359  C CA  B ASN   A 15  ? 0.1576 0.1558 0.2229 -0.0076 0.0217  0.0385  15  ASN   A CA  
360  C C   A ASN   A 15  ? 0.1477 0.1500 0.2269 -0.0214 0.0074  0.0213  15  ASN   A C   
361  C C   B ASN   A 15  ? 0.1485 0.1510 0.2220 -0.0065 0.0216  0.0203  15  ASN   A C   
362  O O   A ASN   A 15  ? 0.1517 0.1478 0.2351 -0.0158 0.0030  0.0171  15  ASN   A O   
363  O O   B ASN   A 15  ? 0.1553 0.1637 0.2097 -0.0087 0.0155  0.0075  15  ASN   A O   
364  C CB  A ASN   A 15  ? 0.1395 0.1655 0.2113 -0.0139 -0.0024 0.0250  15  ASN   A CB  
365  C CB  B ASN   A 15  ? 0.1625 0.1652 0.2142 -0.0020 0.0273  0.0284  15  ASN   A CB  
366  C CG  A ASN   A 15  ? 0.1439 0.1774 0.2151 -0.0141 0.0074  0.0117  15  ASN   A CG  
367  C CG  B ASN   A 15  ? 0.1656 0.1783 0.2205 -0.0011 0.0243  0.0107  15  ASN   A CG  
368  O OD1 A ASN   A 15  ? 0.1575 0.1689 0.2250 -0.0187 0.0232  -0.0060 15  ASN   A OD1 
369  O OD1 B ASN   A 15  ? 0.1676 0.1815 0.2160 -0.0035 0.0355  0.0229  15  ASN   A OD1 
370  N ND2 A ASN   A 15  ? 0.1459 0.1928 0.2008 -0.0220 -0.0046 0.0195  15  ASN   A ND2 
371  N ND2 B ASN   A 15  ? 0.1644 0.1975 0.2282 -0.0099 0.0210  0.0166  15  ASN   A ND2 
384  N N   A VAL   A 16  ? 0.1554 0.1431 0.2134 -0.0248 0.0044  0.0104  16  VAL   A N   
385  N N   B VAL   A 16  ? 0.1397 0.1379 0.2199 -0.0079 0.0271  0.0130  16  VAL   A N   
386  C CA  A VAL   A 16  ? 0.1555 0.1519 0.2012 -0.0228 0.0042  0.0024  16  VAL   A CA  
387  C CA  B VAL   A 16  ? 0.1455 0.1416 0.2128 -0.0086 0.0161  0.0134  16  VAL   A CA  
388  C C   A VAL   A 16  ? 0.1453 0.1516 0.1773 -0.0234 0.0094  0.0144  16  VAL   A C   
389  C C   B VAL   A 16  ? 0.1479 0.1592 0.2069 -0.0106 0.0212  0.0165  16  VAL   A C   
390  O O   A VAL   A 16  ? 0.1394 0.1484 0.1699 -0.0286 0.0180  0.0129  16  VAL   A O   
391  O O   B VAL   A 16  ? 0.1477 0.1663 0.1907 -0.0136 0.0359  0.0043  16  VAL   A O   
392  C CB  A VAL   A 16  ? 0.1697 0.1630 0.2105 -0.0073 0.0177  0.0064  16  VAL   A CB  
393  C CB  B VAL   A 16  ? 0.1563 0.1485 0.2021 -0.0028 0.0186  0.0201  16  VAL   A CB  
394  C CG1 A VAL   A 16  ? 0.1834 0.1686 0.2181 -0.0164 0.0141  0.0004  16  VAL   A CG1 
395  C CG1 B VAL   A 16  ? 0.1652 0.1422 0.2049 0.0009  0.0174  0.0198  16  VAL   A CG1 
396  C CG2 A VAL   A 16  ? 0.1747 0.1793 0.2262 0.0029  0.0394  0.0060  16  VAL   A CG2 
397  C CG2 B VAL   A 16  ? 0.1666 0.1643 0.2100 0.0035  0.0374  0.0085  16  VAL   A CG2 
416  N N   A TYR   A 17  ? 0.1395 0.1455 0.1771 -0.0183 0.0024  0.0261  17  TYR   A N   
417  N N   B TYR   A 17  ? 0.1547 0.1558 0.2067 -0.0052 0.0170  0.0204  17  TYR   A N   
418  C CA  A TYR   A 17  ? 0.1384 0.1489 0.1740 -0.0285 0.0032  0.0281  17  TYR   A CA  
419  C CA  B TYR   A 17  ? 0.1699 0.1587 0.2002 -0.0009 0.0211  0.0255  17  TYR   A CA  
420  C C   A TYR   A 17  ? 0.1370 0.1546 0.1863 -0.0236 0.0052  0.0187  17  TYR   A C   
421  C C   B TYR   A 17  ? 0.1536 0.1523 0.1877 -0.0112 0.0224  0.0296  17  TYR   A C   
422  O O   A TYR   A 17  ? 0.1322 0.1578 0.1807 -0.0240 0.0155  0.0118  17  TYR   A O   
423  O O   B TYR   A 17  ? 0.1447 0.1513 0.1992 -0.0190 0.0193  0.0291  17  TYR   A O   
424  C CB  A TYR   A 17  ? 0.1503 0.1526 0.1850 -0.0280 -0.0067 0.0369  17  TYR   A CB  
425  C CB  B TYR   A 17  ? 0.2102 0.1725 0.2184 0.0021  0.0164  0.0394  17  TYR   A CB  
426  C CG  A TYR   A 17  ? 0.1646 0.1548 0.1854 -0.0310 -0.0258 0.0419  17  TYR   A CG  
427  C CG  B TYR   A 17  ? 0.2543 0.1910 0.2460 0.0057  -0.0006 0.0396  17  TYR   A CG  
428  C CD1 A TYR   A 17  ? 0.1722 0.1709 0.2101 -0.0278 -0.0247 0.0419  17  TYR   A CD1 
429  C CD1 B TYR   A 17  ? 0.2801 0.2107 0.2731 0.0078  -0.0141 0.0342  17  TYR   A CD1 
430  C CD2 A TYR   A 17  ? 0.1763 0.1557 0.1867 -0.0342 -0.0202 0.0413  17  TYR   A CD2 
431  C CD2 B TYR   A 17  ? 0.2743 0.1976 0.2509 -0.0089 -0.0003 0.0463  17  TYR   A CD2 
432  C CE1 A TYR   A 17  ? 0.1800 0.1698 0.2017 -0.0327 -0.0323 0.0446  17  TYR   A CE1 
433  C CE1 B TYR   A 17  ? 0.2984 0.2173 0.2827 -0.0021 -0.0230 0.0262  17  TYR   A CE1 
434  C CE2 A TYR   A 17  ? 0.1909 0.1667 0.1970 -0.0298 -0.0293 0.0357  17  TYR   A CE2 
435  C CE2 B TYR   A 17  ? 0.2909 0.2078 0.2630 -0.0095 -0.0124 0.0381  17  TYR   A CE2 
436  C CZ  A TYR   A 17  ? 0.1959 0.1596 0.1890 -0.0381 -0.0350 0.0502  17  TYR   A CZ  
437  C CZ  B TYR   A 17  ? 0.3048 0.2079 0.2667 -0.0108 -0.0255 0.0330  17  TYR   A CZ  
438  O OH  A TYR   A 17  ? 0.2134 0.1563 0.2113 -0.0318 -0.0388 0.0295  17  TYR   A OH  
439  O OH  B TYR   A 17  ? 0.3197 0.2153 0.2736 -0.0201 -0.0381 0.0336  17  TYR   A OH  
458  N N   A ILE   A 18  ? 0.1445 0.1626 0.2033 -0.0221 0.0114  0.0456  18  ILE   A N   
459  N N   B ILE   A 18  ? 0.1495 0.1481 0.1668 -0.0092 0.0333  0.0259  18  ILE   A N   
460  C CA  A ILE   A 18  ? 0.1491 0.1661 0.2248 -0.0190 0.0103  0.0363  18  ILE   A CA  
461  C CA  B ILE   A 18  ? 0.1504 0.1535 0.1805 -0.0054 0.0279  0.0274  18  ILE   A CA  
462  C C   A ILE   A 18  ? 0.1539 0.1761 0.2469 -0.0276 0.0231  0.0439  18  ILE   A C   
463  C C   B ILE   A 18  ? 0.1551 0.1606 0.1789 -0.0075 0.0343  0.0230  18  ILE   A C   
464  O O   A ILE   A 18  ? 0.1464 0.1868 0.2546 -0.0337 0.0351  0.0464  18  ILE   A O   
465  O O   B ILE   A 18  ? 0.1642 0.1617 0.1868 -0.0055 0.0332  0.0239  18  ILE   A O   
466  C CB  A ILE   A 18  ? 0.1523 0.1647 0.2001 0.0029  0.0104  0.0346  18  ILE   A CB  
467  C CB  B ILE   A 18  ? 0.1555 0.1485 0.1903 -0.0001 0.0316  0.0218  18  ILE   A CB  
468  C CG1 A ILE   A 18  ? 0.1585 0.1752 0.2004 0.0187  0.0021  0.0324  18  ILE   A CG1 
469  C CG1 B ILE   A 18  ? 0.1779 0.1691 0.2038 -0.0156 0.0379  0.0306  18  ILE   A CG1 
470  C CG2 A ILE   A 18  ? 0.1425 0.1651 0.1978 0.0016  0.0045  0.0317  18  ILE   A CG2 
471  C CG2 B ILE   A 18  ? 0.1588 0.1644 0.2027 -0.0129 0.0323  0.0133  18  ILE   A CG2 
472  C CD1 A ILE   A 18  ? 0.1862 0.1919 0.2304 0.0234  -0.0049 0.0305  18  ILE   A CD1 
473  C CD1 B ILE   A 18  ? 0.2051 0.1879 0.2223 -0.0141 0.0382  0.0237  18  ILE   A CD1 
496  N N   A LYS   A 19  ? 0.1686 0.1813 0.2426 -0.0163 0.0341  0.0423  19  LYS   A N   
497  N N   B LYS   A 19  ? 0.1610 0.1613 0.1874 -0.0111 0.0393  0.0217  19  LYS   A N   
498  C CA  A LYS   A 19  ? 0.1819 0.2002 0.2388 -0.0077 0.0455  0.0355  19  LYS   A CA  
499  C CA  B LYS   A 19  ? 0.1689 0.1677 0.2108 -0.0066 0.0510  0.0151  19  LYS   A CA  
500  C C   A LYS   A 19  ? 0.1733 0.2037 0.2517 0.0000  0.0411  0.0365  19  LYS   A C   
501  C C   B LYS   A 19  ? 0.1651 0.1611 0.2343 -0.0100 0.0452  0.0197  19  LYS   A C   
502  O O   A LYS   A 19  ? 0.1598 0.1913 0.2551 0.0070  0.0352  0.0484  19  LYS   A O   
503  O O   B LYS   A 19  ? 0.1561 0.1555 0.2453 -0.0142 0.0458  0.0186  19  LYS   A O   
504  C CB  A LYS   A 19  ? 0.2051 0.2137 0.2316 -0.0052 0.0557  0.0409  19  LYS   A CB  
505  C CB  B LYS   A 19  ? 0.1991 0.1817 0.2128 0.0004  0.0418  0.0081  19  LYS   A CB  
506  C CG  A LYS   A 19  ? 0.2279 0.2239 0.2294 0.0031  0.0562  0.0404  19  LYS   A CG  
507  C CG  B LYS   A 19  ? 0.2260 0.2096 0.2302 0.0084  0.0439  -0.0010 19  LYS   A CG  
508  C CD  A LYS   A 19  ? 0.2476 0.2323 0.2345 0.0114  0.0589  0.0324  19  LYS   A CD  
509  C CD  B LYS   A 19  ? 0.2444 0.2307 0.2471 0.0123  0.0519  -0.0052 19  LYS   A CD  
510  C CE  A LYS   A 19  ? 0.2618 0.2351 0.2444 0.0109  0.0651  0.0306  19  LYS   A CE  
511  C CE  B LYS   A 19  ? 0.2540 0.2451 0.2594 0.0152  0.0580  -0.0013 19  LYS   A CE  
512  N NZ  A LYS   A 19  ? 0.2683 0.2340 0.2370 0.0077  0.0763  0.0187  19  LYS   A NZ  
513  N NZ  B LYS   A 19  ? 0.2588 0.2539 0.2696 0.0174  0.0520  -0.0015 19  LYS   A NZ  
540  N N   A ASN   A 20  ? 0.1818 0.2229 0.2650 0.0029  0.0397  0.0340  20  ASN   A N   
541  N N   B ASN   A 20  ? 0.1651 0.1722 0.2374 -0.0090 0.0507  0.0260  20  ASN   A N   
542  C CA  A ASN   A 20  ? 0.1857 0.2398 0.2574 0.0187  0.0447  0.0247  20  ASN   A CA  
543  C CA  B ASN   A 20  ? 0.1688 0.1918 0.2504 0.0016  0.0549  0.0261  20  ASN   A CA  
544  C C   A ASN   A 20  ? 0.1928 0.2366 0.2494 0.0156  0.0503  0.0309  20  ASN   A C   
545  C C   B ASN   A 20  ? 0.1827 0.2026 0.2561 0.0004  0.0594  0.0229  20  ASN   A C   
546  O O   A ASN   A 20  ? 0.2052 0.2350 0.2446 0.0193  0.0474  0.0277  20  ASN   A O   
547  O O   B ASN   A 20  ? 0.1898 0.2013 0.2646 0.0050  0.0645  0.0223  20  ASN   A O   
548  C CB  A ASN   A 20  ? 0.1994 0.2587 0.2654 0.0206  0.0349  0.0310  20  ASN   A CB  
549  C CB  B ASN   A 20  ? 0.1689 0.2097 0.2688 0.0010  0.0546  0.0394  20  ASN   A CB  
550  C CG  A ASN   A 20  ? 0.2093 0.2679 0.2722 0.0286  0.0344  0.0246  20  ASN   A CG  
551  C CG  B ASN   A 20  ? 0.1587 0.2184 0.2759 0.0228  0.0472  0.0360  20  ASN   A CG  
552  O OD1 A ASN   A 20  ? 0.2184 0.2731 0.2756 0.0283  0.0314  0.0167  20  ASN   A OD1 
553  O OD1 B ASN   A 20  ? 0.1582 0.2282 0.2890 0.0310  0.0314  0.0322  20  ASN   A OD1 
554  N ND2 A ASN   A 20  ? 0.2200 0.2696 0.2859 0.0361  0.0281  0.0283  20  ASN   A ND2 
555  N ND2 B ASN   A 20  ? 0.1669 0.2128 0.2883 0.0385  0.0353  0.0459  20  ASN   A ND2 
568  N N   A ALA   A 21  ? 0.1951 0.2365 0.2510 0.0102  0.0446  0.0256  21  ALA   A N   
569  N N   B ALA   A 21  ? 0.1971 0.2161 0.2652 -0.0029 0.0411  0.0146  21  ALA   A N   
570  C CA  A ALA   A 21  ? 0.1963 0.2321 0.2383 0.0076  0.0410  0.0239  21  ALA   A CA  
571  C CA  B ALA   A 21  ? 0.2097 0.2296 0.2695 -0.0086 0.0265  0.0147  21  ALA   A CA  
572  C C   A ALA   A 21  ? 0.1901 0.2220 0.2265 0.0085  0.0500  0.0192  21  ALA   A C   
573  C C   B ALA   A 21  ? 0.1959 0.2252 0.2555 -0.0098 0.0262  0.0276  21  ALA   A C   
574  O O   A ALA   A 21  ? 0.1795 0.2225 0.2396 0.0122  0.0547  0.0180  21  ALA   A O   
575  O O   B ALA   A 21  ? 0.1886 0.2225 0.2656 -0.0120 0.0281  0.0342  21  ALA   A O   
576  C CB  A ALA   A 21  ? 0.2075 0.2364 0.2428 0.0015  0.0314  0.0217  21  ALA   A CB  
577  C CB  B ALA   A 21  ? 0.2294 0.2387 0.2916 -0.0101 0.0074  -0.0006 21  ALA   A CB  
588  N N   A ASP   A 22  ? 0.1964 0.2148 0.2321 0.0023  0.0544  0.0133  22  ASP   A N   
589  N N   B ASP   A 22  ? 0.1915 0.2255 0.2558 -0.0148 0.0344  0.0252  22  ASP   A N   
590  C CA  A ASP   A 22  ? 0.2138 0.2086 0.2254 -0.0012 0.0415  0.0175  22  ASP   A CA  
591  C CA  B ASP   A 22  ? 0.1938 0.2253 0.2402 -0.0201 0.0265  0.0311  22  ASP   A CA  
592  C C   A ASP   A 22  ? 0.2052 0.2053 0.1994 -0.0006 0.0385  0.0199  22  ASP   A C   
593  C C   B ASP   A 22  ? 0.1763 0.2343 0.2085 -0.0312 0.0355  0.0314  22  ASP   A C   
594  O O   A ASP   A 22  ? 0.2163 0.2117 0.2167 -0.0001 0.0371  0.0215  22  ASP   A O   
595  O O   B ASP   A 22  ? 0.1755 0.2495 0.2043 -0.0404 0.0381  0.0353  22  ASP   A O   
596  C CB  A ASP   A 22  ? 0.2458 0.2168 0.2636 -0.0019 0.0293  0.0112  22  ASP   A CB  
597  C CB  B ASP   A 22  ? 0.2187 0.2280 0.2792 -0.0110 0.0051  0.0263  22  ASP   A CB  
598  C CG  A ASP   A 22  ? 0.2717 0.2352 0.3100 -0.0102 0.0008  0.0113  22  ASP   A CG  
599  C CG  B ASP   A 22  ? 0.2308 0.2373 0.3131 -0.0106 -0.0320 0.0282  22  ASP   A CG  
600  O OD1 A ASP   A 22  ? 0.2759 0.2387 0.3235 -0.0182 -0.0025 0.0263  22  ASP   A OD1 
601  O OD1 B ASP   A 22  ? 0.2254 0.2245 0.2946 -0.0253 -0.0481 0.0289  22  ASP   A OD1 
602  O OD2 A ASP   A 22  ? 0.2856 0.2472 0.3254 -0.0139 -0.0169 -0.0025 22  ASP   A OD2 
603  O OD2 B ASP   A 22  ? 0.2402 0.2571 0.3468 0.0007  -0.0454 0.0309  22  ASP   A OD2 
612  N N   A ILE   A 23  ? 0.1955 0.2059 0.1810 0.0026  0.0288  0.0171  23  ILE   A N   
613  N N   B ILE   A 23  ? 0.1724 0.2365 0.1996 -0.0217 0.0268  0.0275  23  ILE   A N   
614  C CA  A ILE   A 23  ? 0.1939 0.2026 0.1740 -0.0028 0.0249  0.0092  23  ILE   A CA  
615  C CA  B ILE   A 23  ? 0.1766 0.2357 0.1958 -0.0251 0.0217  0.0167  23  ILE   A CA  
616  C C   A ILE   A 23  ? 0.1950 0.2046 0.1635 -0.0095 0.0390  0.0056  23  ILE   A C   
617  C C   B ILE   A 23  ? 0.1811 0.2397 0.2000 -0.0320 0.0303  0.0199  23  ILE   A C   
618  O O   A ILE   A 23  ? 0.1990 0.2130 0.1499 -0.0146 0.0485  -0.0098 23  ILE   A O   
619  O O   B ILE   A 23  ? 0.1850 0.2439 0.2049 -0.0296 0.0305  0.0068  23  ILE   A O   
620  C CB  A ILE   A 23  ? 0.1956 0.1961 0.1724 0.0005  0.0131  0.0057  23  ILE   A CB  
621  C CB  B ILE   A 23  ? 0.1850 0.2303 0.1832 -0.0177 0.0184  0.0111  23  ILE   A CB  
622  C CG1 A ILE   A 23  ? 0.2004 0.1944 0.1887 0.0032  0.0072  -0.0003 23  ILE   A CG1 
623  C CG1 B ILE   A 23  ? 0.1910 0.2263 0.1875 -0.0167 0.0194  0.0011  23  ILE   A CG1 
624  C CG2 A ILE   A 23  ? 0.1991 0.2000 0.1839 0.0003  0.0124  0.0106  23  ILE   A CG2 
625  C CG2 B ILE   A 23  ? 0.1827 0.2351 0.1974 -0.0144 0.0305  0.0160  23  ILE   A CG2 
626  C CD1 A ILE   A 23  ? 0.2045 0.1984 0.1928 0.0031  0.0026  -0.0079 23  ILE   A CD1 
627  C CD1 B ILE   A 23  ? 0.1953 0.2275 0.1889 -0.0155 0.0159  -0.0084 23  ILE   A CD1 
650  N N   A VAL   A 24  ? 0.2010 0.2047 0.1808 -0.0114 0.0394  0.0081  24  VAL   A N   
651  N N   B VAL   A 24  ? 0.1900 0.2467 0.2161 -0.0385 0.0297  0.0278  24  VAL   A N   
652  C CA  A VAL   A 24  ? 0.2155 0.2173 0.2175 -0.0179 0.0357  -0.0040 24  VAL   A CA  
653  C CA  B VAL   A 24  ? 0.2072 0.2654 0.2424 -0.0442 0.0308  0.0248  24  VAL   A CA  
654  C C   A VAL   A 24  ? 0.2199 0.2350 0.2269 -0.0274 0.0305  -0.0145 24  VAL   A C   
655  C C   B VAL   A 24  ? 0.2105 0.2870 0.2487 -0.0430 0.0292  0.0066  24  VAL   A C   
656  O O   A VAL   A 24  ? 0.2326 0.2359 0.2252 -0.0271 0.0378  -0.0205 24  VAL   A O   
657  O O   B VAL   A 24  ? 0.2207 0.2904 0.2609 -0.0347 0.0328  0.0034  24  VAL   A O   
658  C CB  A VAL   A 24  ? 0.2242 0.2214 0.2509 -0.0102 0.0377  -0.0030 24  VAL   A CB  
659  C CB  B VAL   A 24  ? 0.2213 0.2712 0.2787 -0.0451 0.0241  0.0369  24  VAL   A CB  
660  C CG1 A VAL   A 24  ? 0.2298 0.2245 0.2682 -0.0005 0.0351  -0.0104 24  VAL   A CG1 
661  C CG1 B VAL   A 24  ? 0.2366 0.2799 0.3047 -0.0391 0.0084  0.0363  24  VAL   A CG1 
662  C CG2 A VAL   A 24  ? 0.2398 0.2322 0.2603 0.0014  0.0449  0.0027  24  VAL   A CG2 
663  C CG2 B VAL   A 24  ? 0.2327 0.2760 0.2870 -0.0392 0.0319  0.0430  24  VAL   A CG2 
682  N N   A GLU   A 25  ? 0.2251 0.2683 0.2395 -0.0245 0.0320  -0.0127 25  GLU   A N   
683  N N   B GLU   A 25  ? 0.2147 0.3125 0.2469 -0.0369 0.0401  -0.0032 25  GLU   A N   
684  C CA  A GLU   A 25  ? 0.2439 0.3019 0.2493 -0.0222 0.0399  -0.0130 25  GLU   A CA  
685  C CA  B GLU   A 25  ? 0.2348 0.3386 0.2498 -0.0300 0.0517  -0.0077 25  GLU   A CA  
686  C C   A GLU   A 25  ? 0.2324 0.3142 0.2023 -0.0345 0.0499  -0.0098 25  GLU   A C   
687  C C   B GLU   A 25  ? 0.2207 0.3460 0.1985 -0.0408 0.0632  -0.0079 25  GLU   A C   
688  O O   A GLU   A 25  ? 0.2358 0.3228 0.2183 -0.0332 0.0517  -0.0192 25  GLU   A O   
689  O O   B GLU   A 25  ? 0.2237 0.3526 0.2219 -0.0395 0.0632  -0.0174 25  GLU   A O   
690  C CB  A GLU   A 25  ? 0.2739 0.3279 0.3048 -0.0152 0.0458  -0.0119 25  GLU   A CB  
691  C CB  B GLU   A 25  ? 0.2671 0.3610 0.2997 -0.0204 0.0613  -0.0079 25  GLU   A CB  
692  C CG  A GLU   A 25  ? 0.3075 0.3537 0.3787 -0.0132 0.0407  -0.0120 25  GLU   A CG  
693  C CG  B GLU   A 25  ? 0.3031 0.3843 0.3780 -0.0150 0.0540  -0.0072 25  GLU   A CG  
694  C CD  A GLU   A 25  ? 0.3368 0.3759 0.4435 -0.0101 0.0309  -0.0107 25  GLU   A CD  
695  C CD  B GLU   A 25  ? 0.3336 0.4042 0.4472 -0.0097 0.0412  -0.0050 25  GLU   A CD  
696  O OE1 A GLU   A 25  ? 0.3489 0.3860 0.4629 -0.0041 0.0279  -0.0134 25  GLU   A OE1 
697  O OE1 B GLU   A 25  ? 0.3482 0.4145 0.4751 -0.0035 0.0294  -0.0054 25  GLU   A OE1 
698  O OE2 A GLU   A 25  ? 0.3467 0.3829 0.4719 -0.0140 0.0277  -0.0146 25  GLU   A OE2 
699  O OE2 B GLU   A 25  ? 0.3432 0.4101 0.4760 -0.0104 0.0386  -0.0090 25  GLU   A OE2 
712  N N   A GLU   A 26  ? 0.2200 0.3192 0.1971 -0.0488 0.0427  -0.0079 26  GLU   A N   
713  N N   B GLU   A 26  ? 0.2064 0.3484 0.1866 -0.0533 0.0547  -0.0074 26  GLU   A N   
714  C CA  A GLU   A 26  ? 0.2250 0.3233 0.1950 -0.0620 0.0404  0.0002  26  GLU   A CA  
715  C CA  B GLU   A 26  ? 0.2119 0.3507 0.1783 -0.0663 0.0485  0.0057  26  GLU   A CA  
716  C C   A GLU   A 26  ? 0.2227 0.3195 0.1742 -0.0629 0.0355  0.0066  26  GLU   A C   
717  C C   B GLU   A 26  ? 0.2166 0.3360 0.1703 -0.0642 0.0449  0.0079  26  GLU   A C   
718  O O   A GLU   A 26  ? 0.2318 0.3125 0.1839 -0.0710 0.0301  0.0254  26  GLU   A O   
719  O O   B GLU   A 26  ? 0.2255 0.3341 0.1862 -0.0707 0.0456  0.0199  26  GLU   A O   
720  C CB  A GLU   A 26  ? 0.2403 0.3294 0.2298 -0.0640 0.0389  -0.0085 26  GLU   A CB  
721  C CB  B GLU   A 26  ? 0.2234 0.3657 0.1908 -0.0700 0.0371  0.0044  26  GLU   A CB  
722  C CG  A GLU   A 26  ? 0.2573 0.3409 0.2823 -0.0638 0.0559  -0.0168 26  GLU   A CG  
723  C CG  B GLU   A 26  ? 0.2475 0.3835 0.2446 -0.0703 0.0288  0.0070  26  GLU   A CG  
724  C CD  A GLU   A 26  ? 0.2610 0.3453 0.2962 -0.0679 0.0909  -0.0187 26  GLU   A CD  
725  C CD  B GLU   A 26  ? 0.2577 0.3948 0.2494 -0.0756 0.0375  0.0162  26  GLU   A CD  
726  O OE1 A GLU   A 26  ? 0.2526 0.3508 0.3018 -0.0704 0.1114  -0.0445 26  GLU   A OE1 
727  O OE1 B GLU   A 26  ? 0.2679 0.4027 0.2255 -0.0783 0.0586  0.0198  26  GLU   A OE1 
728  O OE2 A GLU   A 26  ? 0.2673 0.3471 0.2926 -0.0672 0.1137  -0.0041 26  GLU   A OE2 
729  O OE2 B GLU   A 26  ? 0.2561 0.3969 0.2645 -0.0770 0.0257  0.0250  26  GLU   A OE2 
742  N N   . ALA   A 27  ? 0.2092 0.3158 0.1740 -0.0611 0.0419  0.0075  27  ALA   A N   
743  C CA  . ALA   A 27  ? 0.2160 0.3207 0.1671 -0.0583 0.0250  0.0043  27  ALA   A CA  
744  C C   . ALA   A 27  ? 0.2512 0.3524 0.1789 -0.0616 0.0364  -0.0161 27  ALA   A C   
745  O O   . ALA   A 27  ? 0.2423 0.3458 0.1820 -0.0634 0.0198  -0.0049 27  ALA   A O   
746  C CB  . ALA   A 27  ? 0.2070 0.3090 0.1673 -0.0556 0.0406  -0.0006 27  ALA   A CB  
753  N N   A LYS   A 28  ? 0.2845 0.3758 0.2033 -0.0539 0.0296  -0.0355 28  LYS   A N   
754  N N   B LYS   A 28  ? 0.2794 0.3739 0.1971 -0.0549 0.0267  -0.0403 28  LYS   A N   
755  C CA  A LYS   A 28  ? 0.3243 0.4030 0.2461 -0.0470 0.0333  -0.0497 28  LYS   A CA  
756  C CA  B LYS   A 28  ? 0.3155 0.3999 0.2355 -0.0487 0.0292  -0.0573 28  LYS   A CA  
757  C C   A LYS   A 28  ? 0.3486 0.4270 0.2506 -0.0502 0.0453  -0.0377 28  LYS   A C   
758  C C   B LYS   A 28  ? 0.3410 0.4245 0.2392 -0.0513 0.0416  -0.0440 28  LYS   A C   
759  O O   A LYS   A 28  ? 0.3559 0.4347 0.2672 -0.0482 0.0321  -0.0388 28  LYS   A O   
760  O O   B LYS   A 28  ? 0.3497 0.4328 0.2592 -0.0484 0.0254  -0.0450 28  LYS   A O   
761  C CB  A LYS   A 28  ? 0.3406 0.4098 0.2999 -0.0362 0.0250  -0.0637 28  LYS   A CB  
762  C CB  B LYS   A 28  ? 0.3289 0.4056 0.2876 -0.0388 0.0193  -0.0724 28  LYS   A CB  
763  C CG  A LYS   A 28  ? 0.3573 0.4145 0.3521 -0.0284 0.0192  -0.0721 28  LYS   A CG  
764  C CG  B LYS   A 28  ? 0.3449 0.4097 0.3399 -0.0313 0.0130  -0.0818 28  LYS   A CG  
765  C CD  A LYS   A 28  ? 0.3716 0.4224 0.4095 -0.0220 0.0119  -0.0739 28  LYS   A CD  
766  C CD  B LYS   A 28  ? 0.3606 0.4185 0.4021 -0.0238 0.0063  -0.0833 28  LYS   A CD  
767  C CE  A LYS   A 28  ? 0.3826 0.4286 0.4488 -0.0188 0.0089  -0.0766 28  LYS   A CE  
768  C CE  B LYS   A 28  ? 0.3740 0.4256 0.4462 -0.0197 0.0033  -0.0868 28  LYS   A CE  
769  N NZ  A LYS   A 28  ? 0.3895 0.4313 0.4760 -0.0163 0.0077  -0.0828 28  LYS   A NZ  
770  N NZ  B LYS   A 28  ? 0.3828 0.4286 0.4759 -0.0161 0.0026  -0.0938 28  LYS   A NZ  
797  N N   A LYS   A 29  ? 0.3627 0.4410 0.2513 -0.0580 0.0687  -0.0182 29  LYS   A N   
798  N N   B LYS   A 29  ? 0.3550 0.4390 0.2368 -0.0593 0.0693  -0.0226 29  LYS   A N   
799  C CA  A LYS   A 29  ? 0.3809 0.4579 0.2786 -0.0621 0.0840  -0.0047 29  LYS   A CA  
800  C CA  B LYS   A 29  ? 0.3737 0.4564 0.2658 -0.0633 0.0870  -0.0084 29  LYS   A CA  
801  C C   A LYS   A 29  ? 0.3811 0.4564 0.2528 -0.0734 0.0803  0.0092  29  LYS   A C   
802  C C   B LYS   A 29  ? 0.3760 0.4552 0.2431 -0.0757 0.0827  0.0079  29  LYS   A C   
803  O O   A LYS   A 29  ? 0.3919 0.4665 0.2595 -0.0662 0.0757  0.0070  29  LYS   A O   
804  O O   B LYS   A 29  ? 0.3833 0.4636 0.2394 -0.0726 0.0845  0.0101  29  LYS   A O   
805  C CB  A LYS   A 29  ? 0.3989 0.4765 0.3459 -0.0504 0.0926  -0.0032 29  LYS   A CB  
806  C CB  B LYS   A 29  ? 0.3911 0.4760 0.3348 -0.0489 0.0953  -0.0098 29  LYS   A CB  
807  C CG  A LYS   A 29  ? 0.4155 0.4927 0.4087 -0.0388 0.0954  -0.0017 29  LYS   A CG  
808  C CG  B LYS   A 29  ? 0.4080 0.4927 0.3991 -0.0343 0.0975  -0.0112 29  LYS   A CG  
809  C CD  A LYS   A 29  ? 0.4307 0.5064 0.4663 -0.0296 0.0926  -0.0014 29  LYS   A CD  
810  C CD  B LYS   A 29  ? 0.4231 0.5068 0.4588 -0.0227 0.0936  -0.0119 29  LYS   A CD  
811  C CE  A LYS   A 29  ? 0.4409 0.5160 0.5022 -0.0225 0.0904  -0.0016 29  LYS   A CE  
812  C CE  B LYS   A 29  ? 0.4322 0.5167 0.4969 -0.0139 0.0904  -0.0146 29  LYS   A CE  
813  N NZ  A LYS   A 29  ? 0.4470 0.5215 0.5229 -0.0179 0.0856  -0.0013 29  LYS   A NZ  
814  N NZ  B LYS   A 29  ? 0.4384 0.5222 0.5190 -0.0094 0.0845  -0.0147 29  LYS   A NZ  
841  N N   . VAL   A 30  ? 0.3684 0.4440 0.2295 -0.0884 0.0813  0.0208  30  VAL   A N   
842  C CA  . VAL   A 30  ? 0.3584 0.4264 0.2271 -0.1072 0.0537  0.0430  30  VAL   A CA  
843  C C   . VAL   A 30  ? 0.3576 0.4084 0.1811 -0.1021 0.0270  0.0521  30  VAL   A C   
844  O O   . VAL   A 30  ? 0.3624 0.4145 0.1834 -0.0981 0.0274  0.0673  30  VAL   A O   
845  C CB  . VAL   A 30  ? 0.3504 0.4202 0.2655 -0.1304 0.0496  0.0539  30  VAL   A CB  
846  C CG1 . VAL   A 30  ? 0.3568 0.4207 0.2857 -0.1360 0.0439  0.0552  30  VAL   A CG1 
847  C CG2 . VAL   A 30  ? 0.3465 0.4188 0.2960 -0.1407 0.0527  0.0631  30  VAL   A CG2 
858  N N   A LYS   A 31  ? 0.3545 0.3967 0.1769 -0.1013 0.0087  0.0503  31  LYS   A N   
859  N N   B LYS   A 31  ? 0.3531 0.3965 0.1701 -0.1007 0.0105  0.0522  31  LYS   A N   
860  C CA  A LYS   A 31  ? 0.3589 0.3916 0.1996 -0.0926 -0.0168 0.0483  31  LYS   A CA  
861  C CA  B LYS   A 31  ? 0.3579 0.3937 0.1895 -0.0922 -0.0143 0.0508  31  LYS   A CA  
862  C C   A LYS   A 31  ? 0.3345 0.3732 0.1446 -0.0926 -0.0187 0.0777  31  LYS   A C   
863  C C   B LYS   A 31  ? 0.3320 0.3710 0.1408 -0.0890 -0.0183 0.0805  31  LYS   A C   
864  O O   A LYS   A 31  ? 0.3424 0.3834 0.1695 -0.0843 -0.0252 0.0816  31  LYS   A O   
865  O O   B LYS   A 31  ? 0.3419 0.3841 0.1624 -0.0817 -0.0275 0.0856  31  LYS   A O   
866  C CB  A LYS   A 31  ? 0.3898 0.4064 0.2981 -0.0803 -0.0338 0.0258  31  LYS   A CB  
867  C CB  B LYS   A 31  ? 0.3875 0.4090 0.2823 -0.0781 -0.0280 0.0293  31  LYS   A CB  
868  C CG  A LYS   A 31  ? 0.4200 0.4207 0.4031 -0.0669 -0.0503 0.0080  31  LYS   A CG  
869  C CG  B LYS   A 31  ? 0.4178 0.4250 0.3839 -0.0640 -0.0426 0.0120  31  LYS   A CG  
870  C CD  A LYS   A 31  ? 0.4429 0.4314 0.4863 -0.0557 -0.0600 -0.0076 31  LYS   A CD  
871  C CD  B LYS   A 31  ? 0.4399 0.4365 0.4614 -0.0522 -0.0508 -0.0036 31  LYS   A CD  
872  C CE  A LYS   A 31  ? 0.4569 0.4385 0.5372 -0.0482 -0.0679 -0.0197 31  LYS   A CE  
873  C CE  B LYS   A 31  ? 0.4533 0.4443 0.5085 -0.0438 -0.0557 -0.0132 31  LYS   A CE  
874  N NZ  A LYS   A 31  ? 0.4637 0.4421 0.5674 -0.0436 -0.0723 -0.0278 31  LYS   A NZ  
875  N NZ  B LYS   A 31  ? 0.4608 0.4479 0.5359 -0.0380 -0.0584 -0.0201 31  LYS   A NZ  
902  N N   . PRO   A 32  ? 0.3034 0.3450 0.1335 -0.1008 -0.0132 0.0667  32  PRO   A N   
903  C CA  . PRO   A 32  ? 0.2874 0.3205 0.1837 -0.0893 -0.0196 0.0853  32  PRO   A CA  
904  C C   . PRO   A 32  ? 0.2724 0.3022 0.1892 -0.0705 -0.0429 0.0934  32  PRO   A C   
905  O O   . PRO   A 32  ? 0.2660 0.2893 0.2173 -0.0652 -0.0496 0.0902  32  PRO   A O   
906  C CB  . PRO   A 32  ? 0.2781 0.3181 0.1880 -0.0939 -0.0196 0.0709  32  PRO   A CB  
907  C CG  . PRO   A 32  ? 0.2744 0.3257 0.1246 -0.0890 -0.0399 0.0497  32  PRO   A CG  
908  C CD  . PRO   A 32  ? 0.2770 0.3306 0.1285 -0.0985 -0.0298 0.0565  32  PRO   A CD  
916  N N   . THR   A 33  ? 0.2793 0.2977 0.1878 -0.0643 -0.0342 0.0919  33  THR   A N   
917  C CA  . THR   A 33  ? 0.2790 0.2912 0.1969 -0.0552 -0.0434 0.0818  33  THR   A CA  
918  C C   . THR   A 33  ? 0.2510 0.2592 0.1892 -0.0561 -0.0403 0.0768  33  THR   A C   
919  O O   . THR   A 33  ? 0.2471 0.2604 0.1941 -0.0560 -0.0451 0.0712  33  THR   A O   
920  C CB  . THR   A 33  ? 0.3066 0.3133 0.2060 -0.0405 -0.0573 0.1017  33  THR   A CB  
921  O OG1 . THR   A 33  ? 0.3302 0.3333 0.2425 -0.0253 -0.0552 0.1043  33  THR   A OG1 
922  C CG2 . THR   A 33  ? 0.3065 0.3175 0.2197 -0.0357 -0.0647 0.1022  33  THR   A CG2 
930  N N   . VAL   A 34  ? 0.2182 0.2399 0.1766 -0.0517 -0.0315 0.0698  34  VAL   A N   
931  C CA  . VAL   A 34  ? 0.1961 0.2261 0.1526 -0.0418 -0.0135 0.0567  34  VAL   A CA  
932  C C   . VAL   A 34  ? 0.1809 0.2135 0.1480 -0.0362 -0.0133 0.0518  34  VAL   A C   
933  O O   . VAL   A 34  ? 0.1839 0.2180 0.1909 -0.0493 -0.0103 0.0533  34  VAL   A O   
934  C CB  . VAL   A 34  ? 0.2011 0.2228 0.1713 -0.0433 -0.0088 0.0453  34  VAL   A CB  
935  C CG1 . VAL   A 34  ? 0.2014 0.2270 0.1928 -0.0329 -0.0028 0.0225  34  VAL   A CG1 
936  C CG2 . VAL   A 34  ? 0.2130 0.2373 0.1949 -0.0367 -0.0146 0.0465  34  VAL   A CG2 
946  N N   . VAL   A 35  ? 0.1729 0.2031 0.1445 -0.0371 -0.0227 0.0417  35  VAL   A N   
947  C CA  . VAL   A 35  ? 0.1641 0.1899 0.1438 -0.0246 -0.0148 0.0221  35  VAL   A CA  
948  C C   . VAL   A 35  ? 0.1530 0.1732 0.1438 -0.0218 -0.0089 0.0234  35  VAL   A C   
949  O O   . VAL   A 35  ? 0.1454 0.1896 0.1709 -0.0242 0.0080  0.0179  35  VAL   A O   
950  C CB  . VAL   A 35  ? 0.1766 0.1975 0.1620 -0.0156 -0.0031 0.0126  35  VAL   A CB  
951  C CG1 . VAL   A 35  ? 0.1800 0.1987 0.1735 -0.0167 -0.0027 0.0197  35  VAL   A CG1 
952  C CG2 . VAL   A 35  ? 0.1744 0.1964 0.1846 -0.0110 0.0100  0.0126  35  VAL   A CG2 
962  N N   . VAL   A 36  ? 0.1442 0.1673 0.1371 -0.0217 -0.0022 0.0270  36  VAL   A N   
963  C CA  . VAL   A 36  ? 0.1363 0.1536 0.1593 -0.0101 -0.0068 0.0191  36  VAL   A CA  
964  C C   . VAL   A 36  ? 0.1330 0.1573 0.1559 -0.0120 0.0026  0.0197  36  VAL   A C   
965  O O   . VAL   A 36  ? 0.1410 0.1574 0.1866 -0.0097 0.0186  0.0128  36  VAL   A O   
966  C CB  . VAL   A 36  ? 0.1345 0.1444 0.1691 -0.0135 -0.0073 0.0157  36  VAL   A CB  
967  C CG1 . VAL   A 36  ? 0.1461 0.1500 0.1882 -0.0098 0.0104  0.0047  36  VAL   A CG1 
968  C CG2 . VAL   A 36  ? 0.1479 0.1563 0.1858 -0.0166 -0.0108 0.0336  36  VAL   A CG2 
978  N N   . ASN   A 37  ? 0.1344 0.1437 0.1453 -0.0080 0.0073  0.0235  37  ASN   A N   
979  C CA  . ASN   A 37  ? 0.1341 0.1412 0.1541 -0.0094 0.0085  0.0196  37  ASN   A CA  
980  C C   . ASN   A 37  ? 0.1374 0.1357 0.1486 -0.0039 0.0096  0.0228  37  ASN   A C   
981  O O   . ASN   A 37  ? 0.1551 0.1460 0.1458 0.0098  0.0077  0.0166  37  ASN   A O   
982  C CB  . ASN   A 37  ? 0.1341 0.1404 0.1584 -0.0040 0.0095  0.0152  37  ASN   A CB  
983  C CG  . ASN   A 37  ? 0.1383 0.1374 0.1708 0.0031  0.0044  0.0150  37  ASN   A CG  
984  O OD1 . ASN   A 37  ? 0.1392 0.1394 0.1890 0.0026  0.0043  0.0171  37  ASN   A OD1 
985  N ND2 . ASN   A 37  ? 0.1383 0.1436 0.1791 0.0003  -0.0035 0.0312  37  ASN   A ND2 
992  N N   A ALA   A 38  ? 0.1347 0.1452 0.1457 -0.0023 0.0117  0.0123  38  ALA   A N   
993  N N   B ALA   A 38  ? 0.1381 0.1441 0.1523 0.0004  0.0089  0.0231  38  ALA   A N   
994  C CA  A ALA   A 38  ? 0.1409 0.1442 0.1402 -0.0039 0.0066  -0.0084 38  ALA   A CA  
995  C CA  B ALA   A 38  ? 0.1461 0.1436 0.1523 -0.0008 0.0047  0.0169  38  ALA   A CA  
996  C C   A ALA   A 38  ? 0.1396 0.1389 0.1346 -0.0070 0.0030  -0.0131 38  ALA   A C   
997  C C   B ALA   A 38  ? 0.1391 0.1429 0.1600 -0.0028 0.0018  0.0211  38  ALA   A C   
998  O O   A ALA   A 38  ? 0.1455 0.1335 0.1372 -0.0062 -0.0045 0.0026  38  ALA   A O   
999  O O   B ALA   A 38  ? 0.1382 0.1325 0.1768 0.0039  -0.0046 0.0181  38  ALA   A O   
1000 C CB  A ALA   A 38  ? 0.1395 0.1612 0.1583 -0.0161 0.0031  0.0020  38  ALA   A CB  
1001 C CB  B ALA   A 38  ? 0.1496 0.1551 0.1622 -0.0114 0.0112  0.0175  38  ALA   A CB  
1012 N N   A ALA   A 39  ? 0.1310 0.1344 0.1480 0.0004  -0.0031 -0.0056 39  ALA   A N   
1013 N N   B ALA   A 39  ? 0.1339 0.1521 0.1445 -0.0007 0.0134  0.0488  39  ALA   A N   
1014 C CA  A ALA   A 39  ? 0.1350 0.1324 0.1420 0.0048  0.0013  -0.0077 39  ALA   A CA  
1015 C CA  B ALA   A 39  ? 0.1398 0.1567 0.1491 0.0018  0.0070  0.0425  39  ALA   A CA  
1016 C C   A ALA   A 39  ? 0.1397 0.1314 0.1265 -0.0042 0.0042  -0.0033 39  ALA   A C   
1017 C C   B ALA   A 39  ? 0.1423 0.1539 0.1650 -0.0033 0.0054  0.0294  39  ALA   A C   
1018 O O   A ALA   A 39  ? 0.1495 0.1394 0.1345 -0.0074 0.0034  -0.0172 39  ALA   A O   
1019 O O   B ALA   A 39  ? 0.1479 0.1630 0.1859 -0.0107 0.0222  0.0318  39  ALA   A O   
1020 C CB  A ALA   A 39  ? 0.1351 0.1412 0.1520 0.0001  -0.0010 -0.0099 39  ALA   A CB  
1021 C CB  B ALA   A 39  ? 0.1521 0.1715 0.1763 -0.0031 -0.0027 0.0265  39  ALA   A CB  
1032 N N   A ASN   A 40  ? 0.1522 0.1358 0.1333 -0.0104 0.0282  -0.0003 40  ASN   A N   
1033 N N   B ASN   A 40  ? 0.1502 0.1490 0.1648 -0.0091 0.0148  0.0202  40  ASN   A N   
1034 C CA  A ASN   A 40  ? 0.1584 0.1372 0.1403 -0.0053 0.0147  0.0159  40  ASN   A CA  
1035 C CA  B ASN   A 40  ? 0.1474 0.1481 0.1687 -0.0102 0.0062  0.0172  40  ASN   A CA  
1036 C C   A ASN   A 40  ? 0.1591 0.1302 0.1423 -0.0077 0.0133  0.0202  40  ASN   A C   
1037 C C   B ASN   A 40  ? 0.1498 0.1396 0.1504 -0.0080 0.0113  0.0128  40  ASN   A C   
1038 O O   A ASN   A 40  ? 0.1555 0.1291 0.1613 -0.0058 0.0134  0.0244  40  ASN   A O   
1039 O O   B ASN   A 40  ? 0.1435 0.1422 0.1533 -0.0023 0.0218  0.0131  40  ASN   A O   
1040 C CB  A ASN   A 40  ? 0.1678 0.1353 0.1457 -0.0010 0.0067  0.0188  40  ASN   A CB  
1041 C CB  B ASN   A 40  ? 0.1494 0.1566 0.1729 0.0026  0.0061  0.0047  40  ASN   A CB  
1042 C CG  A ASN   A 40  ? 0.1696 0.1355 0.1878 0.0065  0.0052  0.0186  40  ASN   A CG  
1043 C CG  B ASN   A 40  ? 0.1525 0.1637 0.1831 0.0021  0.0211  0.0098  40  ASN   A CG  
1044 O OD1 A ASN   A 40  ? 0.1730 0.1296 0.1967 0.0040  0.0018  0.0204  40  ASN   A OD1 
1045 O OD1 B ASN   A 40  ? 0.1566 0.1632 0.1913 -0.0024 0.0252  0.0076  40  ASN   A OD1 
1046 N ND2 A ASN   A 40  ? 0.1738 0.1394 0.2096 0.0080  -0.0029 0.0154  40  ASN   A ND2 
1047 N ND2 B ASN   A 40  ? 0.1600 0.1721 0.1886 0.0088  0.0091  0.0064  40  ASN   A ND2 
1060 N N   A VAL   A 41  ? 0.1613 0.1404 0.1438 -0.0011 0.0218  0.0231  41  VAL   A N   
1061 N N   B VAL   A 41  ? 0.1494 0.1420 0.1509 -0.0042 0.0199  0.0099  41  VAL   A N   
1062 C CA  A VAL   A 41  ? 0.1660 0.1471 0.1564 0.0008  0.0154  0.0281  41  VAL   A CA  
1063 C CA  B VAL   A 41  ? 0.1422 0.1390 0.1576 -0.0050 0.0103  0.0158  41  VAL   A CA  
1064 C C   A VAL   A 41  ? 0.1563 0.1450 0.1377 0.0067  0.0281  0.0232  41  VAL   A C   
1065 C C   B VAL   A 41  ? 0.1375 0.1360 0.1585 -0.0062 0.0173  0.0193  41  VAL   A C   
1066 O O   A VAL   A 41  ? 0.1617 0.1449 0.0979 0.0037  0.0236  0.0197  41  VAL   A O   
1067 O O   B VAL   A 41  ? 0.1500 0.1325 0.1301 -0.0005 0.0171  0.0149  41  VAL   A O   
1068 C CB  A VAL   A 41  ? 0.1760 0.1585 0.1804 -0.0052 0.0172  0.0239  41  VAL   A CB  
1069 C CB  B VAL   A 41  ? 0.1454 0.1495 0.1559 -0.0011 0.0191  0.0092  41  VAL   A CB  
1070 C CG1 A VAL   A 41  ? 0.1930 0.1626 0.2035 -0.0078 0.0260  0.0106  41  VAL   A CG1 
1071 C CG1 B VAL   A 41  ? 0.1505 0.1532 0.1662 -0.0003 0.0173  0.0008  41  VAL   A CG1 
1072 C CG2 A VAL   A 41  ? 0.1845 0.1657 0.1783 -0.0176 0.0065  0.0134  41  VAL   A CG2 
1073 C CG2 B VAL   A 41  ? 0.1334 0.1487 0.1385 -0.0025 0.0254  0.0002  41  VAL   A CG2 
1092 N N   A TYR   A 42  ? 0.1462 0.1389 0.1774 0.0086  0.0365  0.0307  42  TYR   A N   
1093 N N   B TYR   A 42  ? 0.1358 0.1338 0.1894 -0.0098 0.0159  0.0207  42  TYR   A N   
1094 C CA  A TYR   A 42  ? 0.1432 0.1352 0.1773 0.0106  0.0324  0.0345  42  TYR   A CA  
1095 C CA  B TYR   A 42  ? 0.1401 0.1317 0.1929 -0.0067 0.0137  0.0231  42  TYR   A CA  
1096 C C   A TYR   A 42  ? 0.1416 0.1369 0.1778 0.0058  0.0250  0.0317  42  TYR   A C   
1097 C C   B TYR   A 42  ? 0.1334 0.1309 0.1941 0.0011  0.0079  0.0207  42  TYR   A C   
1098 O O   A TYR   A 42  ? 0.1421 0.1381 0.1854 -0.0076 0.0210  0.0288  42  TYR   A O   
1099 O O   B TYR   A 42  ? 0.1385 0.1336 0.2069 -0.0131 0.0008  -0.0000 42  TYR   A O   
1100 C CB  A TYR   A 42  ? 0.1601 0.1425 0.1844 0.0015  0.0246  0.0383  42  TYR   A CB  
1101 C CB  B TYR   A 42  ? 0.1523 0.1421 0.1880 0.0006  0.0163  0.0317  42  TYR   A CB  
1102 C CG  A TYR   A 42  ? 0.1666 0.1496 0.1793 0.0044  0.0172  0.0361  42  TYR   A CG  
1103 C CG  B TYR   A 42  ? 0.1617 0.1542 0.1827 0.0039  0.0126  0.0273  42  TYR   A CG  
1104 C CD1 A TYR   A 42  ? 0.1745 0.1590 0.1760 -0.0044 0.0223  0.0315  42  TYR   A CD1 
1105 C CD1 B TYR   A 42  ? 0.1719 0.1701 0.1902 0.0009  0.0008  0.0187  42  TYR   A CD1 
1106 C CD2 A TYR   A 42  ? 0.1820 0.1699 0.2031 0.0044  0.0136  0.0243  42  TYR   A CD2 
1107 C CD2 B TYR   A 42  ? 0.1642 0.1744 0.1820 0.0031  0.0147  0.0228  42  TYR   A CD2 
1108 C CE1 A TYR   A 42  ? 0.1775 0.1666 0.1797 -0.0052 0.0238  0.0241  42  TYR   A CE1 
1109 C CE1 B TYR   A 42  ? 0.1772 0.1793 0.1868 -0.0013 0.0051  0.0269  42  TYR   A CE1 
1110 C CE2 A TYR   A 42  ? 0.1900 0.1798 0.2159 0.0027  0.0220  0.0204  42  TYR   A CE2 
1111 C CE2 B TYR   A 42  ? 0.1723 0.1893 0.1949 -0.0056 0.0000  0.0262  42  TYR   A CE2 
1112 C CZ  A TYR   A 42  ? 0.1896 0.1801 0.1992 0.0012  0.0259  0.0171  42  TYR   A CZ  
1113 C CZ  B TYR   A 42  ? 0.1839 0.1888 0.1817 -0.0020 0.0076  0.0358  42  TYR   A CZ  
1114 O OH  A TYR   A 42  ? 0.1940 0.1927 0.2274 -0.0039 0.0226  -0.0015 42  TYR   A OH  
1115 O OH  B TYR   A 42  ? 0.1943 0.1987 0.2053 -0.0028 0.0138  0.0290  42  TYR   A OH  
1134 N N   . LEU   A 43  ? 0.1383 0.1323 0.1813 -0.0010 0.0136  0.0104  43  LEU   A N   
1135 C CA  . LEU   A 43  ? 0.1398 0.1347 0.1767 -0.0037 0.0212  0.0107  43  LEU   A CA  
1136 C C   . LEU   A 43  ? 0.1445 0.1368 0.1731 -0.0041 0.0070  0.0139  43  LEU   A C   
1137 O O   . LEU   A 43  ? 0.1702 0.1416 0.1899 0.0039  0.0021  0.0018  43  LEU   A O   
1138 C CB  . LEU   A 43  ? 0.1424 0.1281 0.1964 -0.0062 0.0108  0.0119  43  LEU   A CB  
1139 C CG  . LEU   A 43  ? 0.1494 0.1326 0.2015 -0.0038 0.0023  0.0145  43  LEU   A CG  
1140 C CD1 . LEU   A 43  ? 0.1633 0.1467 0.2218 -0.0071 -0.0111 0.0200  43  LEU   A CD1 
1141 C CD2 . LEU   A 43  ? 0.1663 0.1378 0.2049 -0.0051 0.0113  0.0230  43  LEU   A CD2 
1154 N N   A LYS   A 44  ? 0.1534 0.1363 0.1715 0.0048  0.0087  0.0127  44  LYS   A N   
1155 N N   B LYS   A 44  ? 0.1468 0.1431 0.1657 0.0026  0.0076  0.0109  44  LYS   A N   
1156 C CA  A LYS   A 44  ? 0.1692 0.1362 0.1789 0.0038  0.0145  0.0186  44  LYS   A CA  
1157 C CA  B LYS   A 44  ? 0.1555 0.1509 0.1688 0.0008  0.0124  0.0144  44  LYS   A CA  
1158 C C   A LYS   A 44  ? 0.1608 0.1369 0.1600 0.0058  0.0017  0.0114  44  LYS   A C   
1159 C C   B LYS   A 44  ? 0.1441 0.1492 0.1464 0.0026  0.0052  0.0114  44  LYS   A C   
1160 O O   A LYS   A 44  ? 0.1646 0.1487 0.1880 0.0039  -0.0001 0.0026  44  LYS   A O   
1161 O O   B LYS   A 44  ? 0.1518 0.1655 0.1727 0.0060  0.0020  -0.0098 44  LYS   A O   
1162 C CB  A LYS   A 44  ? 0.1968 0.1465 0.2151 0.0075  0.0247  0.0247  44  LYS   A CB  
1163 C CB  B LYS   A 44  ? 0.1805 0.1685 0.2031 -0.0001 0.0068  0.0116  44  LYS   A CB  
1164 C CG  A LYS   A 44  ? 0.2254 0.1705 0.2725 0.0011  0.0419  0.0343  44  LYS   A CG  
1165 C CG  B LYS   A 44  ? 0.2102 0.1976 0.2590 -0.0079 0.0191  0.0124  44  LYS   A CG  
1166 C CD  A LYS   A 44  ? 0.2556 0.2124 0.3438 -0.0097 0.0354  0.0338  44  LYS   A CD  
1167 C CD  B LYS   A 44  ? 0.2423 0.2401 0.3280 -0.0137 0.0166  0.0139  44  LYS   A CD  
1168 C CE  A LYS   A 44  ? 0.2731 0.2418 0.3924 -0.0180 0.0280  0.0367  44  LYS   A CE  
1169 C CE  B LYS   A 44  ? 0.2601 0.2646 0.3774 -0.0142 0.0105  0.0164  44  LYS   A CE  
1170 N NZ  A LYS   A 44  ? 0.2851 0.2622 0.4181 -0.0222 0.0223  0.0344  44  LYS   A NZ  
1171 N NZ  B LYS   A 44  ? 0.2656 0.2703 0.3898 -0.0087 -0.0018 0.0243  44  LYS   A NZ  
1198 N N   A HIS   A 45  ? 0.1582 0.1330 0.1649 0.0031  -0.0087 0.0123  45  HIS   A N   
1199 N N   B HIS   A 45  ? 0.1325 0.1470 0.1684 0.0017  0.0123  0.0210  45  HIS   A N   
1200 C CA  A HIS   A 45  ? 0.1585 0.1277 0.1757 0.0053  -0.0009 0.0054  45  HIS   A CA  
1201 C CA  B HIS   A 45  ? 0.1413 0.1474 0.1853 0.0014  0.0085  0.0037  45  HIS   A CA  
1202 C C   A HIS   A 45  ? 0.1534 0.1402 0.1761 -0.0031 -0.0039 0.0013  45  HIS   A C   
1203 C C   B HIS   A 45  ? 0.1538 0.1597 0.2126 0.0073  0.0051  -0.0009 45  HIS   A C   
1204 O O   A HIS   A 45  ? 0.1705 0.1540 0.2118 0.0185  -0.0007 -0.0185 45  HIS   A O   
1205 O O   B HIS   A 45  ? 0.1765 0.1658 0.2508 0.0176  -0.0041 -0.0117 45  HIS   A O   
1206 C CB  A HIS   A 45  ? 0.1642 0.1236 0.1790 0.0082  0.0000  -0.0000 45  HIS   A CB  
1207 C CB  B HIS   A 45  ? 0.1327 0.1512 0.1644 -0.0132 0.0177  0.0079  45  HIS   A CB  
1208 C CG  A HIS   A 45  ? 0.1558 0.1172 0.1777 0.0082  -0.0026 0.0062  45  HIS   A CG  
1209 C CG  B HIS   A 45  ? 0.1258 0.1649 0.1611 -0.0114 0.0114  0.0196  45  HIS   A CG  
1210 N ND1 A HIS   A 45  ? 0.1517 0.1245 0.1953 0.0101  -0.0038 0.0087  45  HIS   A ND1 
1211 N ND1 B HIS   A 45  ? 0.1212 0.1748 0.1687 -0.0077 0.0058  0.0330  45  HIS   A ND1 
1212 C CD2 A HIS   A 45  ? 0.1552 0.1280 0.1832 0.0075  -0.0024 0.0165  45  HIS   A CD2 
1213 C CD2 B HIS   A 45  ? 0.1252 0.1717 0.1663 -0.0179 0.0050  0.0317  45  HIS   A CD2 
1214 C CE1 A HIS   A 45  ? 0.1553 0.1371 0.1784 0.0072  -0.0041 0.0082  45  HIS   A CE1 
1215 C CE1 B HIS   A 45  ? 0.1251 0.1781 0.1521 -0.0116 -0.0049 0.0287  45  HIS   A CE1 
1216 N NE2 A HIS   A 45  ? 0.1570 0.1432 0.1805 0.0065  0.0026  0.0170  45  HIS   A NE2 
1217 N NE2 B HIS   A 45  ? 0.1273 0.1821 0.1565 -0.0155 -0.0012 0.0331  45  HIS   A NE2 
1232 N N   A GLY   A 46  ? 0.1630 0.1477 0.1885 -0.0011 -0.0195 0.0169  46  GLY   A N   
1233 N N   B GLY   A 46  ? 0.1589 0.1660 0.2190 0.0149  -0.0097 0.0091  46  GLY   A N   
1234 C CA  A GLY   A 46  ? 0.1769 0.1460 0.2118 0.0082  -0.0277 0.0145  46  GLY   A CA  
1235 C CA  B GLY   A 46  ? 0.1602 0.1697 0.2160 0.0147  -0.0321 0.0295  46  GLY   A CA  
1236 C C   A GLY   A 46  ? 0.1836 0.1546 0.2100 0.0154  -0.0356 0.0091  46  GLY   A C   
1237 C C   B GLY   A 46  ? 0.1620 0.1706 0.2032 0.0244  -0.0370 0.0178  46  GLY   A C   
1238 O O   A GLY   A 46  ? 0.1916 0.1640 0.2226 0.0189  -0.0543 -0.0064 46  GLY   A O   
1239 O O   B GLY   A 46  ? 0.1694 0.1883 0.2057 0.0249  -0.0373 0.0092  46  GLY   A O   
1246 N N   A GLY   A 47  ? 0.1839 0.1600 0.1944 0.0178  -0.0222 0.0170  47  GLY   A N   
1247 N N   B GLY   A 47  ? 0.1537 0.1622 0.2008 0.0251  -0.0219 0.0069  47  GLY   A N   
1248 C CA  A GLY   A 47  ? 0.1819 0.1682 0.2116 0.0168  -0.0323 0.0107  47  GLY   A CA  
1249 C CA  B GLY   A 47  ? 0.1557 0.1682 0.2168 0.0110  -0.0268 0.0053  47  GLY   A CA  
1250 C C   A GLY   A 47  ? 0.1716 0.1559 0.2038 0.0125  -0.0507 0.0068  47  GLY   A C   
1251 C C   B GLY   A 47  ? 0.1548 0.1658 0.2063 0.0063  -0.0394 -0.0065 47  GLY   A C   
1252 O O   A GLY   A 47  ? 0.1621 0.1365 0.2106 0.0129  -0.0576 0.0227  47  GLY   A O   
1253 O O   B GLY   A 47  ? 0.1581 0.1742 0.2062 0.0175  -0.0341 -0.0054 47  GLY   A O   
1260 N N   A GLY   A 48  ? 0.1690 0.1616 0.2138 0.0129  -0.0567 0.0088  48  GLY   A N   
1261 N N   B GLY   A 48  ? 0.1595 0.1641 0.2230 0.0049  -0.0502 -0.0116 48  GLY   A N   
1262 C CA  A GLY   A 48  ? 0.1748 0.1637 0.2251 0.0050  -0.0452 0.0044  48  GLY   A CA  
1263 C CA  B GLY   A 48  ? 0.1585 0.1709 0.2229 0.0026  -0.0489 -0.0171 48  GLY   A CA  
1264 C C   A GLY   A 48  ? 0.1663 0.1550 0.2176 0.0065  -0.0291 -0.0068 48  GLY   A C   
1265 C C   B GLY   A 48  ? 0.1440 0.1716 0.2027 0.0106  -0.0227 -0.0186 48  GLY   A C   
1266 O O   A GLY   A 48  ? 0.1701 0.1486 0.2175 0.0110  -0.0244 -0.0021 48  GLY   A O   
1267 O O   B GLY   A 48  ? 0.1328 0.1629 0.1992 0.0109  -0.0217 -0.0176 48  GLY   A O   
1274 N N   A VAL   A 49  ? 0.1605 0.1490 0.2206 0.0028  -0.0145 0.0053  49  VAL   A N   
1275 N N   B VAL   A 49  ? 0.1372 0.1644 0.1674 0.0029  -0.0102 -0.0223 49  VAL   A N   
1276 C CA  A VAL   A 49  ? 0.1721 0.1545 0.1963 -0.0072 -0.0057 0.0028  49  VAL   A CA  
1277 C CA  B VAL   A 49  ? 0.1391 0.1591 0.1590 0.0015  -0.0029 -0.0075 49  VAL   A CA  
1278 C C   A VAL   A 49  ? 0.1666 0.1424 0.1594 -0.0036 -0.0012 0.0155  49  VAL   A C   
1279 C C   B VAL   A 49  ? 0.1327 0.1466 0.1266 0.0129  0.0016  -0.0058 49  VAL   A C   
1280 O O   A VAL   A 49  ? 0.1784 0.1425 0.1517 -0.0177 0.0092  0.0079  49  VAL   A O   
1281 O O   B VAL   A 49  ? 0.1448 0.1588 0.1357 0.0097  0.0119  -0.0006 49  VAL   A O   
1282 C CB  A VAL   A 49  ? 0.1840 0.1621 0.2134 -0.0176 -0.0099 -0.0099 49  VAL   A CB  
1283 C CB  B VAL   A 49  ? 0.1457 0.1611 0.1731 -0.0034 -0.0001 0.0091  49  VAL   A CB  
1284 C CG1 A VAL   A 49  ? 0.1873 0.1574 0.2238 -0.0272 -0.0006 -0.0122 49  VAL   A CG1 
1285 C CG1 B VAL   A 49  ? 0.1371 0.1449 0.1787 -0.0023 0.0122  0.0278  49  VAL   A CG1 
1286 C CG2 A VAL   A 49  ? 0.1916 0.1727 0.2450 -0.0334 -0.0203 -0.0045 49  VAL   A CG2 
1287 C CG2 B VAL   A 49  ? 0.1661 0.1790 0.2070 -0.0157 -0.0065 0.0093  49  VAL   A CG2 
1306 N N   A ALA   A 50  ? 0.1528 0.1387 0.1516 -0.0099 -0.0199 0.0120  50  ALA   A N   
1307 N N   B ALA   A 50  ? 0.1296 0.1403 0.1384 0.0106  -0.0017 -0.0120 50  ALA   A N   
1308 C CA  A ALA   A 50  ? 0.1461 0.1375 0.1616 -0.0152 -0.0176 0.0207  50  ALA   A CA  
1309 C CA  B ALA   A 50  ? 0.1325 0.1408 0.1388 0.0060  0.0018  -0.0124 50  ALA   A CA  
1310 C C   A ALA   A 50  ? 0.1430 0.1349 0.1713 -0.0114 -0.0169 0.0239  50  ALA   A C   
1311 C C   B ALA   A 50  ? 0.1415 0.1410 0.1168 0.0054  0.0024  -0.0105 50  ALA   A C   
1312 O O   A ALA   A 50  ? 0.1461 0.1418 0.1829 0.0034  -0.0131 0.0225  50  ALA   A O   
1313 O O   B ALA   A 50  ? 0.1445 0.1459 0.1187 0.0062  0.0164  -0.0245 50  ALA   A O   
1314 C CB  A ALA   A 50  ? 0.1455 0.1347 0.1609 -0.0269 -0.0195 0.0184  50  ALA   A CB  
1315 C CB  B ALA   A 50  ? 0.1380 0.1367 0.1340 0.0126  0.0105  -0.0170 50  ALA   A CB  
1326 N N   A GLY   A 51  ? 0.1370 0.1318 0.1774 -0.0000 -0.0144 0.0145  51  GLY   A N   
1327 N N   B GLY   A 51  ? 0.1438 0.1436 0.1338 0.0131  -0.0131 -0.0145 51  GLY   A N   
1328 C CA  A GLY   A 51  ? 0.1415 0.1319 0.2010 -0.0037 -0.0193 0.0162  51  GLY   A CA  
1329 C CA  B GLY   A 51  ? 0.1566 0.1408 0.1350 0.0113  -0.0263 -0.0176 51  GLY   A CA  
1330 C C   A GLY   A 51  ? 0.1362 0.1345 0.1892 0.0038  0.0023  0.0124  51  GLY   A C   
1331 C C   B GLY   A 51  ? 0.1567 0.1461 0.1343 0.0206  -0.0074 -0.0208 51  GLY   A C   
1332 O O   A GLY   A 51  ? 0.1357 0.1390 0.1682 0.0038  -0.0097 0.0041  51  GLY   A O   
1333 O O   B GLY   A 51  ? 0.1661 0.1595 0.1437 0.0195  0.0056  -0.0209 51  GLY   A O   
1340 N N   A ALA   A 52  ? 0.1373 0.1512 0.2010 0.0053  0.0029  0.0167  52  ALA   A N   
1341 N N   B ALA   A 52  ? 0.1612 0.1531 0.1236 0.0101  -0.0052 -0.0370 52  ALA   A N   
1342 C CA  A ALA   A 52  ? 0.1357 0.1643 0.2122 0.0017  0.0087  0.0124  52  ALA   A CA  
1343 C CA  B ALA   A 52  ? 0.1474 0.1662 0.1492 0.0090  0.0015  -0.0219 52  ALA   A CA  
1344 C C   A ALA   A 52  ? 0.1365 0.1686 0.1934 -0.0058 0.0081  0.0152  52  ALA   A C   
1345 C C   B ALA   A 52  ? 0.1420 0.1694 0.1130 -0.0006 0.0131  -0.0151 52  ALA   A C   
1346 O O   A ALA   A 52  ? 0.1416 0.1774 0.2045 -0.0042 0.0002  0.0084  52  ALA   A O   
1347 O O   B ALA   A 52  ? 0.1521 0.1781 0.1344 -0.0013 0.0066  -0.0190 52  ALA   A O   
1348 C CB  A ALA   A 52  ? 0.1356 0.1782 0.2130 -0.0057 -0.0036 0.0072  52  ALA   A CB  
1349 C CB  B ALA   A 52  ? 0.1425 0.1899 0.1680 0.0032  -0.0147 -0.0156 52  ALA   A CB  
1360 N N   A LEU   A 53  ? 0.1377 0.1590 0.1845 -0.0081 0.0065  0.0240  53  LEU   A N   
1361 N N   B LEU   A 53  ? 0.1390 0.1582 0.1371 0.0014  0.0130  -0.0103 53  LEU   A N   
1362 C CA  A LEU   A 53  ? 0.1450 0.1674 0.1740 -0.0096 0.0071  0.0173  53  LEU   A CA  
1363 C CA  B LEU   A 53  ? 0.1407 0.1598 0.1319 0.0063  0.0016  -0.0085 53  LEU   A CA  
1364 C C   A LEU   A 53  ? 0.1495 0.1710 0.1582 -0.0119 0.0077  0.0074  53  LEU   A C   
1365 C C   B LEU   A 53  ? 0.1502 0.1586 0.1038 0.0100  0.0008  -0.0106 53  LEU   A C   
1366 O O   A LEU   A 53  ? 0.1573 0.1751 0.1561 -0.0240 0.0141  -0.0036 53  LEU   A O   
1367 O O   B LEU   A 53  ? 0.1648 0.1623 0.1191 0.0070  0.0009  -0.0016 53  LEU   A O   
1368 C CB  A LEU   A 53  ? 0.1551 0.1703 0.1844 -0.0104 0.0014  0.0115  53  LEU   A CB  
1369 C CB  B LEU   A 53  ? 0.1418 0.1613 0.1392 -0.0052 -0.0072 -0.0108 53  LEU   A CB  
1370 C CG  A LEU   A 53  ? 0.1685 0.1688 0.1817 -0.0105 0.0060  0.0194  53  LEU   A CG  
1371 C CG  B LEU   A 53  ? 0.1556 0.1624 0.1490 -0.0123 -0.0015 0.0040  53  LEU   A CG  
1372 C CD1 A LEU   A 53  ? 0.1684 0.1710 0.1612 0.0008  -0.0008 0.0127  53  LEU   A CD1 
1373 C CD1 B LEU   A 53  ? 0.1600 0.1663 0.1547 -0.0120 -0.0200 -0.0086 53  LEU   A CD1 
1374 C CD2 A LEU   A 53  ? 0.1850 0.1810 0.2013 -0.0151 0.0057  0.0144  53  LEU   A CD2 
1375 C CD2 B LEU   A 53  ? 0.1746 0.1728 0.1547 -0.0138 0.0049  -0.0027 53  LEU   A CD2 
1398 N N   A ASN   A 54  ? 0.1384 0.1635 0.1501 -0.0124 -0.0024 0.0067  54  ASN   A N   
1399 N N   B ASN   A 54  ? 0.1413 0.1519 0.1188 0.0026  -0.0020 -0.0017 54  ASN   A N   
1400 C CA  A ASN   A 54  ? 0.1352 0.1648 0.1658 -0.0092 0.0049  -0.0029 54  ASN   A CA  
1401 C CA  B ASN   A 54  ? 0.1357 0.1544 0.1535 -0.0062 -0.0014 -0.0101 54  ASN   A CA  
1402 C C   A ASN   A 54  ? 0.1420 0.1644 0.1627 -0.0101 0.0101  -0.0032 54  ASN   A C   
1403 C C   B ASN   A 54  ? 0.1419 0.1599 0.1527 -0.0124 0.0027  -0.0084 54  ASN   A C   
1404 O O   A ASN   A 54  ? 0.1514 0.1700 0.1759 -0.0039 0.0064  -0.0073 54  ASN   A O   
1405 O O   B ASN   A 54  ? 0.1513 0.1665 0.1610 -0.0104 -0.0091 -0.0157 54  ASN   A O   
1406 C CB  A ASN   A 54  ? 0.1398 0.1588 0.1676 -0.0027 0.0081  0.0016  54  ASN   A CB  
1407 C CB  B ASN   A 54  ? 0.1400 0.1440 0.1538 -0.0072 -0.0038 -0.0060 54  ASN   A CB  
1408 C CG  A ASN   A 54  ? 0.1369 0.1617 0.1759 0.0059  0.0088  -0.0021 54  ASN   A CG  
1409 C CG  B ASN   A 54  ? 0.1372 0.1449 0.1551 -0.0061 -0.0100 -0.0061 54  ASN   A CG  
1410 O OD1 A ASN   A 54  ? 0.1337 0.1743 0.2069 0.0000  0.0044  0.0056  54  ASN   A OD1 
1411 O OD1 B ASN   A 54  ? 0.1252 0.1446 0.1252 -0.0073 0.0073  -0.0128 54  ASN   A OD1 
1412 N ND2 A ASN   A 54  ? 0.1385 0.1627 0.1613 0.0069  0.0173  -0.0023 54  ASN   A ND2 
1413 N ND2 B ASN   A 54  ? 0.1424 0.1561 0.1807 -0.0181 -0.0257 0.0052  54  ASN   A ND2 
1426 N N   . LYS   A 55  ? 0.1492 0.1601 0.1683 -0.0025 0.0052  -0.0134 55  LYS   A N   
1427 C CA  . LYS   A 55  ? 0.1613 0.1730 0.1803 0.0051  0.0018  -0.0193 55  LYS   A CA  
1428 C C   . LYS   A 55  ? 0.1528 0.1685 0.1936 0.0035  0.0039  -0.0284 55  LYS   A C   
1429 O O   . LYS   A 55  ? 0.1682 0.1775 0.1936 0.0062  0.0074  -0.0313 55  LYS   A O   
1430 C CB  . LYS   A 55  ? 0.1657 0.1805 0.1942 0.0217  0.0034  -0.0112 55  LYS   A CB  
1431 C CG  . LYS   A 55  ? 0.1932 0.2234 0.2219 0.0536  -0.0152 -0.0210 55  LYS   A CG  
1432 C CD  . LYS   A 55  ? 0.2143 0.2726 0.2571 0.0674  -0.0187 -0.0266 55  LYS   A CD  
1433 C CE  . LYS   A 55  ? 0.2431 0.3157 0.2872 0.0777  -0.0304 -0.0263 55  LYS   A CE  
1434 N NZ  . LYS   A 55  ? 0.2521 0.3418 0.3163 0.0861  -0.0334 -0.0250 55  LYS   A NZ  
1449 N N   . ALA   A 56  ? 0.1564 0.1810 0.1928 -0.0057 0.0107  -0.0245 56  ALA   A N   
1450 C CA  . ALA   A 56  ? 0.1691 0.2035 0.1931 -0.0137 0.0143  -0.0168 56  ALA   A CA  
1451 C C   . ALA   A 56  ? 0.1795 0.2085 0.1694 -0.0071 0.0170  -0.0330 56  ALA   A C   
1452 O O   . ALA   A 56  ? 0.1857 0.2409 0.1803 0.0034  0.0280  -0.0284 56  ALA   A O   
1453 C CB  . ALA   A 56  ? 0.1704 0.2235 0.1964 -0.0176 0.0131  -0.0050 56  ALA   A CB  
1459 N N   . THR   A 57  ? 0.1563 0.1937 0.1645 -0.0097 0.0149  -0.0224 57  THR   A N   
1460 C CA  . THR   A 57  ? 0.1607 0.1848 0.1696 -0.0178 0.0066  -0.0151 57  THR   A CA  
1461 C C   . THR   A 57  ? 0.1690 0.1913 0.1718 -0.0062 0.0074  -0.0245 57  THR   A C   
1462 O O   . THR   A 57  ? 0.1627 0.1962 0.1933 -0.0140 -0.0056 -0.0256 57  THR   A O   
1463 C CB  . THR   A 57  ? 0.1566 0.1867 0.1520 -0.0077 0.0084  -0.0168 57  THR   A CB  
1464 O OG1 . THR   A 57  ? 0.1505 0.1871 0.1476 -0.0112 0.0087  -0.0155 57  THR   A OG1 
1465 C CG2 . THR   A 57  ? 0.1652 0.1867 0.1570 -0.0101 0.0023  -0.0051 57  THR   A CG2 
1473 N N   A ASN   A 58  ? 0.1798 0.1888 0.1907 -0.0100 0.0194  -0.0286 58  ASN   A N   
1474 N N   B ASN   A 58  ? 0.1665 0.1848 0.1854 -0.0048 0.0072  -0.0275 58  ASN   A N   
1475 C CA  A ASN   A 58  ? 0.1973 0.1854 0.2103 -0.0184 0.0280  -0.0392 58  ASN   A CA  
1476 C CA  B ASN   A 58  ? 0.1727 0.1777 0.1995 -0.0087 0.0050  -0.0367 58  ASN   A CA  
1477 C C   A ASN   A 58  ? 0.1710 0.1758 0.1981 -0.0063 0.0083  -0.0307 58  ASN   A C   
1478 C C   B ASN   A 58  ? 0.1583 0.1718 0.1938 -0.0003 -0.0071 -0.0313 58  ASN   A C   
1479 O O   A ASN   A 58  ? 0.1752 0.1827 0.2047 -0.0160 0.0077  -0.0380 58  ASN   A O   
1480 O O   B ASN   A 58  ? 0.1637 0.1792 0.2059 -0.0109 -0.0093 -0.0450 58  ASN   A O   
1481 C CB  A ASN   A 58  ? 0.2438 0.2077 0.2482 -0.0207 0.0443  -0.0459 58  ASN   A CB  
1482 C CB  B ASN   A 58  ? 0.1950 0.1944 0.2233 -0.0029 0.0029  -0.0425 58  ASN   A CB  
1483 C CG  A ASN   A 58  ? 0.2750 0.2316 0.3019 -0.0197 0.0515  -0.0353 58  ASN   A CG  
1484 C CG  B ASN   A 58  ? 0.1903 0.2048 0.2476 0.0135  -0.0149 -0.0251 58  ASN   A CG  
1485 O OD1 A ASN   A 58  ? 0.2793 0.2355 0.3268 -0.0119 0.0748  -0.0283 58  ASN   A OD1 
1486 O OD1 B ASN   A 58  ? 0.1929 0.2070 0.2838 0.0346  -0.0258 -0.0064 58  ASN   A OD1 
1487 N ND2 A ASN   A 58  ? 0.2905 0.2428 0.3232 -0.0256 0.0437  -0.0448 58  ASN   A ND2 
1488 N ND2 B ASN   A 58  ? 0.1908 0.1992 0.2451 0.0291  -0.0105 -0.0079 58  ASN   A ND2 
1501 N N   . ASN   A 59  ? 0.1473 0.1616 0.1915 -0.0021 -0.0049 -0.0176 59  ASN   A N   
1502 C CA  . ASN   A 59  ? 0.1552 0.1503 0.1928 0.0040  -0.0060 -0.0083 59  ASN   A CA  
1503 C C   . ASN   A 59  ? 0.1520 0.1502 0.1793 -0.0035 -0.0064 -0.0036 59  ASN   A C   
1504 O O   . ASN   A 59  ? 0.1558 0.1504 0.1821 -0.0032 0.0035  0.0013  59  ASN   A O   
1505 C CB  . ASN   A 59  ? 0.1573 0.1512 0.1933 -0.0011 -0.0155 -0.0066 59  ASN   A CB  
1506 C CG  . ASN   A 59  ? 0.1665 0.1606 0.1961 0.0007  -0.0179 0.0022  59  ASN   A CG  
1507 O OD1 . ASN   A 59  ? 0.1752 0.1610 0.1913 -0.0113 -0.0185 0.0044  59  ASN   A OD1 
1508 N ND2 . ASN   A 59  ? 0.1737 0.1622 0.1936 -0.0095 -0.0042 -0.0054 59  ASN   A ND2 
1516 N N   . ALA   A 60  ? 0.1411 0.1598 0.1892 -0.0049 -0.0008 -0.0013 60  ALA   A N   
1517 C CA  . ALA   A 60  ? 0.1480 0.1668 0.1812 -0.0063 -0.0107 -0.0037 60  ALA   A CA  
1518 C C   . ALA   A 60  ? 0.1479 0.1573 0.1833 -0.0056 -0.0032 -0.0041 60  ALA   A C   
1519 O O   . ALA   A 60  ? 0.1446 0.1565 0.1978 -0.0025 -0.0054 -0.0184 60  ALA   A O   
1520 C CB  . ALA   A 60  ? 0.1636 0.1807 0.1891 -0.0032 -0.0131 -0.0099 60  ALA   A CB  
1526 N N   . MET   A 61  ? 0.1380 0.1526 0.1764 -0.0104 0.0033  -0.0127 61  MET   A N   
1527 C CA  . MET   A 61  ? 0.1473 0.1448 0.1762 -0.0072 0.0011  0.0012  61  MET   A CA  
1528 C C   . MET   A 61  ? 0.1399 0.1424 0.1771 -0.0086 0.0055  -0.0056 61  MET   A C   
1529 O O   . MET   A 61  ? 0.1471 0.1453 0.1834 -0.0021 0.0178  0.0013  61  MET   A O   
1530 C CB  . MET   A 61  ? 0.1478 0.1473 0.1784 -0.0079 0.0065  -0.0120 61  MET   A CB  
1531 C CG  . MET   A 61  ? 0.1520 0.1575 0.1817 -0.0025 -0.0036 0.0036  61  MET   A CG  
1532 S SD  . MET   A 61  ? 0.1610 0.1654 0.2331 -0.0096 -0.0054 -0.0164 61  MET   A SD  
1533 C CE  . MET   A 61  ? 0.1786 0.1692 0.2693 -0.0102 0.0175  -0.0058 61  MET   A CE  
1543 N N   . GLN   A 62  ? 0.1410 0.1330 0.1865 -0.0052 0.0042  -0.0037 62  GLN   A N   
1544 C CA  . GLN   A 62  ? 0.1391 0.1381 0.1914 -0.0032 0.0031  0.0024  62  GLN   A CA  
1545 C C   . GLN   A 62  ? 0.1462 0.1259 0.1983 0.0028  0.0015  0.0003  62  GLN   A C   
1546 O O   . GLN   A 62  ? 0.1507 0.1476 0.1786 0.0011  0.0095  -0.0026 62  GLN   A O   
1547 C CB  . GLN   A 62  ? 0.1464 0.1384 0.1874 0.0002  0.0043  -0.0051 62  GLN   A CB  
1548 C CG  . GLN   A 62  ? 0.1539 0.1353 0.1817 -0.0015 0.0079  0.0125  62  GLN   A CG  
1549 C CD  . GLN   A 62  ? 0.1536 0.1416 0.1745 0.0007  0.0128  0.0063  62  GLN   A CD  
1550 O OE1 . GLN   A 62  ? 0.1589 0.1571 0.1987 0.0037  0.0009  -0.0081 62  GLN   A OE1 
1551 N NE2 . GLN   A 62  ? 0.1588 0.1431 0.1913 -0.0016 0.0069  0.0020  62  GLN   A NE2 
1560 N N   . VAL   A 63  ? 0.1449 0.1375 0.2066 -0.0048 0.0099  -0.0134 63  VAL   A N   
1561 C CA  . VAL   A 63  ? 0.1485 0.1535 0.2271 -0.0108 -0.0000 -0.0138 63  VAL   A CA  
1562 C C   . VAL   A 63  ? 0.1428 0.1583 0.1990 -0.0114 -0.0011 -0.0097 63  VAL   A C   
1563 O O   . VAL   A 63  ? 0.1446 0.1570 0.2265 -0.0123 0.0044  -0.0125 63  VAL   A O   
1564 C CB  . VAL   A 63  ? 0.1602 0.1778 0.2584 -0.0167 -0.0032 -0.0388 63  VAL   A CB  
1565 C CG1 . VAL   A 63  ? 0.1845 0.2033 0.2881 -0.0193 -0.0177 -0.0682 63  VAL   A CG1 
1566 C CG2 . VAL   A 63  ? 0.1772 0.1711 0.2531 -0.0153 0.0132  -0.0286 63  VAL   A CG2 
1576 N N   . GLU   A 64  ? 0.1444 0.1621 0.1851 -0.0003 -0.0036 -0.0046 64  GLU   A N   
1577 C CA  . GLU   A 64  ? 0.1468 0.1578 0.1955 -0.0045 -0.0017 0.0070  64  GLU   A CA  
1578 C C   . GLU   A 64  ? 0.1337 0.1537 0.2011 -0.0039 0.0037  0.0146  64  GLU   A C   
1579 O O   . GLU   A 64  ? 0.1412 0.1569 0.2156 0.0050  0.0116  0.0004  64  GLU   A O   
1580 C CB  . GLU   A 64  ? 0.1603 0.1695 0.2027 -0.0039 0.0057  -0.0092 64  GLU   A CB  
1581 C CG  . GLU   A 64  ? 0.1679 0.1843 0.2164 -0.0115 0.0033  0.0027  64  GLU   A CG  
1582 C CD  . GLU   A 64  ? 0.1779 0.1945 0.2358 -0.0176 0.0011  0.0053  64  GLU   A CD  
1583 O OE1 . GLU   A 64  ? 0.1805 0.2131 0.2618 -0.0283 0.0153  0.0072  64  GLU   A OE1 
1584 O OE2 . GLU   A 64  ? 0.2079 0.1911 0.2357 -0.0242 -0.0140 0.0192  64  GLU   A OE2 
1591 N N   . SER   A 65  ? 0.1339 0.1538 0.1881 0.0010  -0.0005 0.0104  65  SER   A N   
1592 C CA  . SER   A 65  ? 0.1352 0.1458 0.1981 0.0038  -0.0018 -0.0018 65  SER   A CA  
1593 C C   . SER   A 65  ? 0.1462 0.1481 0.1888 -0.0004 -0.0010 0.0029  65  SER   A C   
1594 O O   . SER   A 65  ? 0.1507 0.1597 0.2056 0.0017  0.0171  -0.0070 65  SER   A O   
1595 C CB  . SER   A 65  ? 0.1407 0.1462 0.1935 0.0010  0.0100  0.0067  65  SER   A CB  
1596 O OG  . SER   A 65  ? 0.1367 0.1673 0.2046 -0.0113 0.0035  0.0125  65  SER   A OG  
1602 N N   . ASP   A 66  ? 0.1455 0.1456 0.1867 -0.0047 0.0148  0.0085  66  ASP   A N   
1603 C CA  . ASP   A 66  ? 0.1514 0.1571 0.1931 0.0003  0.0088  0.0184  66  ASP   A CA  
1604 C C   . ASP   A 66  ? 0.1539 0.1510 0.2102 -0.0055 0.0083  0.0196  66  ASP   A C   
1605 O O   . ASP   A 66  ? 0.1579 0.1590 0.2203 -0.0047 0.0402  0.0186  66  ASP   A O   
1606 C CB  . ASP   A 66  ? 0.1624 0.1645 0.2367 0.0049  0.0187  0.0312  66  ASP   A CB  
1607 C CG  . ASP   A 66  ? 0.1912 0.1811 0.2726 -0.0035 0.0147  0.0528  66  ASP   A CG  
1608 O OD1 . ASP   A 66  ? 0.1898 0.2171 0.2808 -0.0030 0.0015  0.0547  66  ASP   A OD1 
1609 O OD2 . ASP   A 66  ? 0.2133 0.1933 0.3425 0.0151  -0.0029 0.0323  66  ASP   A OD2 
1614 N N   . ASP   A 67  ? 0.1407 0.1545 0.2181 -0.0039 0.0023  0.0207  67  ASP   A N   
1615 C CA  . ASP   A 67  ? 0.1471 0.1703 0.2285 -0.0010 -0.0008 0.0208  67  ASP   A CA  
1616 C C   . ASP   A 67  ? 0.1477 0.1766 0.2223 0.0011  0.0161  0.0299  67  ASP   A C   
1617 O O   . ASP   A 67  ? 0.1399 0.1876 0.2548 0.0000  0.0279  0.0339  67  ASP   A O   
1618 C CB  . ASP   A 67  ? 0.1557 0.1755 0.2665 -0.0085 -0.0134 0.0195  67  ASP   A CB  
1619 C CG  . ASP   A 67  ? 0.1561 0.1961 0.3254 -0.0107 -0.0257 0.0267  67  ASP   A CG  
1620 O OD1 . ASP   A 67  ? 0.1621 0.2179 0.4103 -0.0172 -0.0378 0.0403  67  ASP   A OD1 
1621 O OD2 . ASP   A 67  ? 0.1615 0.2059 0.2941 0.0018  -0.0075 0.0270  67  ASP   A OD2 
1626 N N   . TYR   A 68  ? 0.1429 0.1630 0.2160 0.0020  0.0211  0.0268  68  TYR   A N   
1627 C CA  . TYR   A 68  ? 0.1573 0.1546 0.2154 0.0060  0.0214  0.0285  68  TYR   A CA  
1628 C C   . TYR   A 68  ? 0.1533 0.1524 0.2224 0.0007  0.0236  0.0236  68  TYR   A C   
1629 O O   . TYR   A 68  ? 0.1610 0.1623 0.2277 0.0166  0.0323  0.0185  68  TYR   A O   
1630 C CB  . TYR   A 68  ? 0.1646 0.1525 0.2424 0.0062  0.0370  0.0236  68  TYR   A CB  
1631 C CG  . TYR   A 68  ? 0.1685 0.1640 0.2879 0.0040  0.0567  0.0349  68  TYR   A CG  
1632 C CD1 . TYR   A 68  ? 0.1802 0.1773 0.3331 -0.0155 0.0502  -0.0041 68  TYR   A CD1 
1633 C CD2 . TYR   A 68  ? 0.1967 0.1738 0.3310 0.0128  0.0676  0.0371  68  TYR   A CD2 
1634 C CE1 . TYR   A 68  ? 0.1873 0.1948 0.3751 -0.0169 0.0610  -0.0118 68  TYR   A CE1 
1635 C CE2 . TYR   A 68  ? 0.1966 0.1765 0.3678 -0.0026 0.0765  0.0080  68  TYR   A CE2 
1636 C CZ  . TYR   A 68  ? 0.1983 0.1872 0.3926 -0.0165 0.0653  -0.0184 68  TYR   A CZ  
1637 O OH  . TYR   A 68  ? 0.2235 0.1947 0.4350 -0.0115 0.0397  -0.0600 68  TYR   A OH  
1647 N N   . ILE   A 69  ? 0.1432 0.1494 0.2199 0.0001  0.0189  0.0169  69  ILE   A N   
1648 C CA  . ILE   A 69  ? 0.1510 0.1509 0.2093 0.0080  0.0106  0.0091  69  ILE   A CA  
1649 C C   . ILE   A 69  ? 0.1520 0.1553 0.2064 0.0125  0.0183  0.0166  69  ILE   A C   
1650 O O   . ILE   A 69  ? 0.1620 0.1582 0.2050 0.0009  0.0244  0.0181  69  ILE   A O   
1651 C CB  . ILE   A 69  ? 0.1608 0.1734 0.2129 0.0115  0.0134  0.0046  69  ILE   A CB  
1652 C CG1 . ILE   A 69  ? 0.1551 0.1890 0.2264 0.0102  0.0155  -0.0130 69  ILE   A CG1 
1653 C CG2 . ILE   A 69  ? 0.1788 0.1986 0.2294 0.0179  0.0031  -0.0122 69  ILE   A CG2 
1654 C CD1 . ILE   A 69  ? 0.1573 0.1961 0.2468 0.0030  0.0219  -0.0193 69  ILE   A CD1 
1666 N N   . ALA   A 70  ? 0.1502 0.1641 0.2177 -0.0076 0.0179  0.0128  70  ALA   A N   
1667 C CA  . ALA   A 70  ? 0.1645 0.1753 0.2353 -0.0181 0.0302  0.0213  70  ALA   A CA  
1668 C C   . ALA   A 70  ? 0.1551 0.1913 0.2473 -0.0124 0.0245  0.0243  70  ALA   A C   
1669 O O   . ALA   A 70  ? 0.1694 0.2275 0.2709 0.0050  0.0505  0.0514  70  ALA   A O   
1670 C CB  . ALA   A 70  ? 0.1714 0.1761 0.2636 -0.0293 0.0215  0.0160  70  ALA   A CB  
1676 N N   . THR   A 71  ? 0.1493 0.1809 0.2353 -0.0046 0.0140  0.0276  71  THR   A N   
1677 C CA  . THR   A 71  ? 0.1634 0.2007 0.2779 0.0107  0.0080  0.0279  71  THR   A CA  
1678 C C   . THR   A 71  ? 0.1528 0.1970 0.2969 0.0173  0.0247  0.0200  71  THR   A C   
1679 O O   . THR   A 71  ? 0.1596 0.2241 0.3517 0.0112  0.0405  -0.0143 71  THR   A O   
1680 C CB  . THR   A 71  ? 0.2016 0.2280 0.3037 0.0151  -0.0260 0.0349  71  THR   A CB  
1681 O OG1 . THR   A 71  ? 0.2298 0.2378 0.2992 0.0027  -0.0438 0.0272  71  THR   A OG1 
1682 C CG2 . THR   A 71  ? 0.2159 0.2477 0.3302 0.0197  -0.0408 0.0537  71  THR   A CG2 
1690 N N   . ASN   A 72  ? 0.1563 0.1724 0.2723 0.0166  0.0286  0.0280  72  ASN   A N   
1691 C CA  . ASN   A 72  ? 0.1640 0.1718 0.2722 0.0205  0.0421  0.0264  72  ASN   A CA  
1692 C C   . ASN   A 72  ? 0.1744 0.1664 0.2682 0.0103  0.0502  0.0268  72  ASN   A C   
1693 O O   . ASN   A 72  ? 0.1957 0.1719 0.2927 0.0192  0.0495  0.0095  72  ASN   A O   
1694 C CB  . ASN   A 72  ? 0.1910 0.1862 0.2730 0.0174  0.0494  0.0327  72  ASN   A CB  
1695 C CG  . ASN   A 72  ? 0.2141 0.2049 0.2826 0.0277  0.0322  0.0401  72  ASN   A CG  
1696 O OD1 . ASN   A 72  ? 0.2332 0.2345 0.2899 0.0291  0.0369  0.0393  72  ASN   A OD1 
1697 N ND2 . ASN   A 72  ? 0.2384 0.2049 0.2755 0.0570  0.0108  0.0309  72  ASN   A ND2 
1704 N N   . GLY   A 73  ? 0.1713 0.1649 0.2429 -0.0010 0.0502  0.0161  73  GLY   A N   
1705 C CA  . GLY   A 73  ? 0.1758 0.1617 0.2303 -0.0084 0.0400  0.0076  73  GLY   A CA  
1706 C C   . GLY   A 73  ? 0.1746 0.1542 0.2194 0.0007  0.0396  0.0221  73  GLY   A C   
1707 O O   . GLY   A 73  ? 0.1723 0.1616 0.2275 0.0119  0.0333  0.0319  73  GLY   A O   
1711 N N   . PRO   A 74  ? 0.1815 0.1577 0.2190 -0.0096 0.0549  0.0095  74  PRO   A N   
1712 C CA  . PRO   A 74  ? 0.1796 0.1556 0.2328 0.0049  0.0442  0.0142  74  PRO   A CA  
1713 C C   . PRO   A 74  ? 0.1749 0.1384 0.2253 0.0008  0.0311  0.0086  74  PRO   A C   
1714 O O   . PRO   A 74  ? 0.1774 0.1453 0.2453 0.0071  0.0384  -0.0070 74  PRO   A O   
1715 C CB  . PRO   A 74  ? 0.2001 0.1800 0.2599 0.0090  0.0568  0.0321  74  PRO   A CB  
1716 C CG  . PRO   A 74  ? 0.2325 0.2244 0.2988 -0.0155 0.0413  0.0228  74  PRO   A CG  
1717 C CD  . PRO   A 74  ? 0.2050 0.1972 0.2351 -0.0226 0.0463  0.0106  74  PRO   A CD  
1725 N N   . LEU   A 75  ? 0.1701 0.1321 0.2098 0.0089  0.0293  0.0047  75  LEU   A N   
1726 C CA  . LEU   A 75  ? 0.1715 0.1417 0.1784 0.0010  0.0135  0.0200  75  LEU   A CA  
1727 C C   . LEU   A 75  ? 0.1790 0.1552 0.1751 0.0063  0.0207  0.0175  75  LEU   A C   
1728 O O   . LEU   A 75  ? 0.2123 0.1675 0.1800 0.0186  0.0124  0.0076  75  LEU   A O   
1729 C CB  . LEU   A 75  ? 0.1765 0.1444 0.1706 -0.0071 0.0149  0.0245  75  LEU   A CB  
1730 C CG  . LEU   A 75  ? 0.2058 0.1815 0.1815 -0.0337 0.0104  0.0248  75  LEU   A CG  
1731 C CD1 . LEU   A 75  ? 0.2210 0.2378 0.1926 -0.0458 0.0091  -0.0042 75  LEU   A CD1 
1732 C CD2 . LEU   A 75  ? 0.2380 0.2216 0.2428 -0.0134 0.0115  0.0255  75  LEU   A CD2 
1744 N N   . LYS   A 76  ? 0.1832 0.1536 0.2047 0.0010  0.0104  -0.0039 76  LYS   A N   
1745 C CA  . LYS   A 76  ? 0.1872 0.1809 0.2138 -0.0123 0.0159  -0.0175 76  LYS   A CA  
1746 C C   . LYS   A 76  ? 0.1812 0.1595 0.1699 0.0022  0.0095  -0.0027 76  LYS   A C   
1747 O O   . LYS   A 76  ? 0.1799 0.1475 0.1823 0.0042  0.0103  0.0140  76  LYS   A O   
1748 C CB  . LYS   A 76  ? 0.1826 0.2092 0.2517 0.0008  0.0126  -0.0474 76  LYS   A CB  
1749 C CG  . LYS   A 76  ? 0.1960 0.2033 0.3128 0.0152  0.0053  -0.0342 76  LYS   A CG  
1750 C CD  . LYS   A 76  ? 0.2020 0.1981 0.3712 0.0272  -0.0046 -0.0277 76  LYS   A CD  
1751 C CE  . LYS   A 76  ? 0.2225 0.2164 0.4203 0.0137  0.0019  -0.0270 76  LYS   A CE  
1752 N NZ  . LYS   A 76  ? 0.2294 0.2041 0.4569 -0.0069 -0.0119 -0.0324 76  LYS   A NZ  
1766 N N   . VAL   A 77  ? 0.1850 0.1625 0.1708 0.0027  0.0224  0.0083  77  VAL   A N   
1767 C CA  . VAL   A 77  ? 0.1834 0.1595 0.1655 0.0115  0.0137  0.0038  77  VAL   A CA  
1768 C C   . VAL   A 77  ? 0.1757 0.1496 0.1716 0.0100  0.0088  0.0112  77  VAL   A C   
1769 O O   . VAL   A 77  ? 0.1872 0.1585 0.1809 0.0109  0.0288  -0.0033 77  VAL   A O   
1770 C CB  . VAL   A 77  ? 0.2039 0.1787 0.1762 0.0017  0.0141  0.0130  77  VAL   A CB  
1771 C CG1 . VAL   A 77  ? 0.1886 0.1969 0.1923 0.0090  0.0050  -0.0012 77  VAL   A CG1 
1772 C CG2 . VAL   A 77  ? 0.2318 0.1895 0.2054 -0.0026 0.0087  0.0189  77  VAL   A CG2 
1782 N N   . GLY   A 78  ? 0.1706 0.1464 0.1707 0.0045  0.0234  0.0015  78  GLY   A N   
1783 C CA  . GLY   A 78  ? 0.1679 0.1508 0.1833 0.0035  0.0237  0.0026  78  GLY   A CA  
1784 C C   . GLY   A 78  ? 0.1523 0.1407 0.1857 0.0090  0.0216  0.0070  78  GLY   A C   
1785 O O   . GLY   A 78  ? 0.1594 0.1518 0.2142 0.0058  0.0146  0.0294  78  GLY   A O   
1789 N N   . GLY   A 79  ? 0.1642 0.1438 0.1752 0.0033  0.0140  0.0142  79  GLY   A N   
1790 C CA  . GLY   A 79  ? 0.1621 0.1416 0.1871 0.0040  0.0143  0.0241  79  GLY   A CA  
1791 C C   . GLY   A 79  ? 0.1472 0.1382 0.1805 0.0002  0.0154  0.0136  79  GLY   A C   
1792 O O   . GLY   A 79  ? 0.1568 0.1515 0.1979 0.0198  0.0117  0.0064  79  GLY   A O   
1796 N N   . SER   A 80  ? 0.1437 0.1518 0.1974 0.0036  0.0177  0.0039  80  SER   A N   
1797 C CA  . SER   A 80  ? 0.1401 0.1498 0.1958 0.0055  0.0117  0.0057  80  SER   A CA  
1798 C C   . SER   A 80  ? 0.1349 0.1587 0.1820 0.0050  0.0069  0.0118  80  SER   A C   
1799 O O   . SER   A 80  ? 0.1453 0.1819 0.2262 0.0133  0.0086  -0.0044 80  SER   A O   
1800 C CB  . SER   A 80  ? 0.1611 0.1550 0.2180 -0.0027 0.0110  0.0046  80  SER   A CB  
1801 O OG  . SER   A 80  ? 0.1861 0.1610 0.2490 0.0005  -0.0039 0.0269  80  SER   A OG  
1807 N N   . CYS   A 81  ? 0.1352 0.1550 0.1780 0.0025  -0.0017 0.0127  81  CYS   A N   
1808 C CA  . CYS   A 81  ? 0.1438 0.1630 0.1829 -0.0100 -0.0068 0.0257  81  CYS   A CA  
1809 C C   . CYS   A 81  ? 0.1416 0.1524 0.1767 -0.0092 -0.0065 0.0260  81  CYS   A C   
1810 O O   . CYS   A 81  ? 0.1399 0.1789 0.2038 -0.0033 0.0017  0.0401  81  CYS   A O   
1811 C CB  . CYS   A 81  ? 0.1560 0.1659 0.2102 -0.0230 -0.0034 0.0266  81  CYS   A CB  
1812 S SG  . CYS   A 81  ? 0.1682 0.1561 0.2075 -0.0163 0.0013  0.0168  81  CYS   A SG  
1818 N N   . VAL   A 82  ? 0.1500 0.1612 0.1808 -0.0004 -0.0177 0.0296  82  VAL   A N   
1819 C CA  . VAL   A 82  ? 0.1534 0.1747 0.1753 0.0022  -0.0110 0.0348  82  VAL   A CA  
1820 C C   . VAL   A 82  ? 0.1502 0.1817 0.1907 0.0003  -0.0067 0.0232  82  VAL   A C   
1821 O O   . VAL   A 82  ? 0.1448 0.1885 0.2293 0.0016  -0.0153 0.0086  82  VAL   A O   
1822 C CB  . VAL   A 82  ? 0.1872 0.1895 0.1971 -0.0007 -0.0044 0.0481  82  VAL   A CB  
1823 C CG1 . VAL   A 82  ? 0.2112 0.2031 0.2212 0.0014  -0.0081 0.0446  82  VAL   A CG1 
1824 C CG2 . VAL   A 82  ? 0.1949 0.1792 0.2306 -0.0045 -0.0164 0.0500  82  VAL   A CG2 
1834 N N   . LEU   A 83  ? 0.1497 0.1719 0.1863 -0.0086 -0.0082 0.0085  83  LEU   A N   
1835 C CA  . LEU   A 83  ? 0.1465 0.1740 0.1856 -0.0086 -0.0125 0.0142  83  LEU   A CA  
1836 C C   . LEU   A 83  ? 0.1545 0.1750 0.1867 -0.0106 -0.0134 0.0267  83  LEU   A C   
1837 O O   . LEU   A 83  ? 0.1600 0.1819 0.1893 -0.0211 -0.0152 0.0256  83  LEU   A O   
1838 C CB  . LEU   A 83  ? 0.1588 0.1794 0.2003 -0.0078 -0.0213 0.0207  83  LEU   A CB  
1839 C CG  . LEU   A 83  ? 0.1725 0.1841 0.2053 -0.0033 0.0024  0.0151  83  LEU   A CG  
1840 C CD1 . LEU   A 83  ? 0.1900 0.1962 0.2200 -0.0179 -0.0182 0.0275  83  LEU   A CD1 
1841 C CD2 . LEU   A 83  ? 0.1743 0.1930 0.2252 -0.0084 0.0036  0.0248  83  LEU   A CD2 
1853 N N   . SER   A 84  ? 0.1668 0.1846 0.1891 -0.0216 -0.0155 0.0263  84  SER   A N   
1854 C CA  . SER   A 84  ? 0.1773 0.1884 0.1767 -0.0184 -0.0171 0.0197  84  SER   A CA  
1855 C C   . SER   A 84  ? 0.1836 0.1870 0.1745 -0.0257 -0.0023 0.0207  84  SER   A C   
1856 O O   . SER   A 84  ? 0.1772 0.2026 0.1681 -0.0123 -0.0088 0.0192  84  SER   A O   
1857 C CB  . SER   A 84  ? 0.1805 0.2185 0.1935 -0.0156 -0.0093 0.0097  84  SER   A CB  
1858 O OG  . SER   A 84  ? 0.1926 0.2424 0.2036 -0.0165 -0.0138 -0.0097 84  SER   A OG  
1864 N N   . GLY   A 85  ? 0.2015 0.2019 0.1747 -0.0313 -0.0024 0.0171  85  GLY   A N   
1865 C CA  . GLY   A 85  ? 0.1998 0.2191 0.1842 -0.0302 0.0016  -0.0102 85  GLY   A CA  
1866 C C   . GLY   A 85  ? 0.1826 0.2267 0.1660 -0.0300 0.0016  0.0086  85  GLY   A C   
1867 O O   . GLY   A 85  ? 0.1889 0.2422 0.1749 -0.0318 0.0074  -0.0122 85  GLY   A O   
1871 N N   . HIS   A 86  ? 0.1819 0.2197 0.1661 -0.0246 -0.0113 0.0080  86  HIS   A N   
1872 C CA  . HIS   A 86  ? 0.2135 0.2240 0.1656 -0.0176 -0.0117 0.0057  86  HIS   A CA  
1873 C C   . HIS   A 86  ? 0.2362 0.2350 0.1648 -0.0282 -0.0248 -0.0008 86  HIS   A C   
1874 O O   . HIS   A 86  ? 0.2420 0.2646 0.1708 -0.0193 -0.0185 0.0025  86  HIS   A O   
1875 C CB  . HIS   A 86  ? 0.2110 0.2147 0.1852 -0.0087 -0.0038 0.0138  86  HIS   A CB  
1876 C CG  . HIS   A 86  ? 0.2090 0.2105 0.2000 -0.0034 0.0104  0.0231  86  HIS   A CG  
1877 N ND1 . HIS   A 86  ? 0.2179 0.2132 0.2493 -0.0143 0.0093  0.0292  86  HIS   A ND1 
1878 C CD2 . HIS   A 86  ? 0.2141 0.1993 0.1989 0.0098  0.0210  0.0240  86  HIS   A CD2 
1879 C CE1 . HIS   A 86  ? 0.2109 0.2088 0.2554 -0.0049 0.0285  0.0253  86  HIS   A CE1 
1880 N NE2 . HIS   A 86  ? 0.2098 0.1933 0.2234 0.0173  0.0268  0.0345  86  HIS   A NE2 
1888 N N   . ASN   A 87  ? 0.2500 0.2414 0.1527 -0.0223 0.0010  -0.0165 87  ASN   A N   
1889 C CA  . ASN   A 87  ? 0.2622 0.2532 0.1689 -0.0115 0.0259  -0.0076 87  ASN   A CA  
1890 C C   . ASN   A 87  ? 0.2631 0.2681 0.1964 -0.0195 0.0415  0.0080  87  ASN   A C   
1891 O O   . ASN   A 87  ? 0.2995 0.2921 0.2416 -0.0319 0.0847  -0.0038 87  ASN   A O   
1892 C CB  . ASN   A 87  ? 0.2835 0.2615 0.1768 0.0010  0.0331  -0.0095 87  ASN   A CB  
1893 C CG  . ASN   A 87  ? 0.2989 0.2714 0.1783 0.0004  0.0406  -0.0057 87  ASN   A CG  
1894 O OD1 . ASN   A 87  ? 0.3151 0.2752 0.1803 0.0210  0.0359  -0.0045 87  ASN   A OD1 
1895 N ND2 . ASN   A 87  ? 0.2992 0.2898 0.1883 -0.0093 0.0418  -0.0078 87  ASN   A ND2 
1902 N N   . LEU   A 88  ? 0.2319 0.2512 0.1748 -0.0265 0.0207  0.0140  88  LEU   A N   
1903 C CA  . LEU   A 88  ? 0.2129 0.2525 0.2125 -0.0339 0.0160  0.0202  88  LEU   A CA  
1904 C C   . LEU   A 88  ? 0.2105 0.2526 0.1909 -0.0351 0.0212  0.0227  88  LEU   A C   
1905 O O   . LEU   A 88  ? 0.2103 0.2568 0.2372 -0.0308 0.0274  0.0424  88  LEU   A O   
1906 C CB  . LEU   A 88  ? 0.2136 0.2563 0.2269 -0.0418 -0.0203 0.0282  88  LEU   A CB  
1907 C CG  . LEU   A 88  ? 0.2351 0.2704 0.2554 -0.0414 -0.0250 0.0466  88  LEU   A CG  
1908 C CD1 . LEU   A 88  ? 0.2531 0.2804 0.2626 -0.0434 -0.0328 0.0328  88  LEU   A CD1 
1909 C CD2 . LEU   A 88  ? 0.2484 0.2840 0.2915 -0.0290 -0.0196 0.0424  88  LEU   A CD2 
1921 N N   . ALA   A 89  ? 0.2041 0.2440 0.1703 -0.0349 0.0138  0.0090  89  ALA   A N   
1922 C CA  . ALA   A 89  ? 0.2147 0.2459 0.1656 -0.0370 -0.0099 0.0278  89  ALA   A CA  
1923 C C   . ALA   A 89  ? 0.2256 0.2569 0.1708 -0.0318 -0.0128 0.0305  89  ALA   A C   
1924 O O   . ALA   A 89  ? 0.2189 0.2494 0.2013 -0.0380 -0.0108 0.0015  89  ALA   A O   
1925 C CB  . ALA   A 89  ? 0.2216 0.2403 0.1717 -0.0366 -0.0049 0.0215  89  ALA   A CB  
1931 N N   . LYS   A 90  ? 0.2299 0.2713 0.1733 -0.0402 -0.0242 0.0293  90  LYS   A N   
1932 C CA  . LYS   A 90  ? 0.2412 0.2852 0.1759 -0.0298 -0.0348 0.0336  90  LYS   A CA  
1933 C C   . LYS   A 90  ? 0.2116 0.2627 0.1744 -0.0313 -0.0284 0.0242  90  LYS   A C   
1934 O O   . LYS   A 90  ? 0.2066 0.2715 0.2061 -0.0351 -0.0328 0.0155  90  LYS   A O   
1935 C CB  . LYS   A 90  ? 0.2709 0.3228 0.2095 -0.0312 -0.0459 0.0616  90  LYS   A CB  
1936 C CG  . LYS   A 90  ? 0.3283 0.3709 0.3058 -0.0321 -0.0377 0.0622  90  LYS   A CG  
1937 C CD  . LYS   A 90  ? 0.3871 0.4202 0.4129 -0.0362 -0.0248 0.0599  90  LYS   A CD  
1938 C CE  . LYS   A 90  ? 0.4341 0.4591 0.5053 -0.0386 -0.0099 0.0510  90  LYS   A CE  
1939 N NZ  . LYS   A 90  ? 0.4711 0.4768 0.5674 -0.0421 -0.0031 0.0466  90  LYS   A NZ  
1953 N N   . HIS   A 91  ? 0.1962 0.2317 0.1517 -0.0348 -0.0360 0.0387  91  HIS   A N   
1954 C CA  . HIS   A 91  ? 0.1867 0.2073 0.1625 -0.0249 -0.0312 0.0330  91  HIS   A CA  
1955 C C   . HIS   A 91  ? 0.1674 0.1883 0.1393 -0.0196 -0.0249 0.0247  91  HIS   A C   
1956 O O   . HIS   A 91  ? 0.1648 0.2049 0.1805 -0.0300 -0.0111 0.0320  91  HIS   A O   
1957 C CB  . HIS   A 91  ? 0.2120 0.2373 0.2105 -0.0075 -0.0427 0.0260  91  HIS   A CB  
1958 C CG  . HIS   A 91  ? 0.2605 0.2886 0.2744 0.0067  -0.0775 0.0134  91  HIS   A CG  
1959 N ND1 . HIS   A 91  ? 0.2748 0.3155 0.3245 0.0188  -0.0897 -0.0095 91  HIS   A ND1 
1960 C CD2 . HIS   A 91  ? 0.2902 0.3109 0.3109 0.0175  -0.0890 0.0224  91  HIS   A CD2 
1961 C CE1 . HIS   A 91  ? 0.2925 0.3281 0.3530 0.0260  -0.0921 0.0064  91  HIS   A CE1 
1962 N NE2 . HIS   A 91  ? 0.3039 0.3298 0.3434 0.0281  -0.0997 0.0154  91  HIS   A NE2 
1970 N N   . CYS   A 92  ? 0.1650 0.1843 0.1441 -0.0200 -0.0197 0.0269  92  CYS   A N   
1971 C CA  . CYS   A 92  ? 0.1567 0.1832 0.1589 -0.0186 -0.0085 0.0193  92  CYS   A CA  
1972 C C   . CYS   A 92  ? 0.1506 0.1701 0.1608 -0.0214 -0.0144 0.0216  92  CYS   A C   
1973 O O   . CYS   A 92  ? 0.1501 0.1758 0.1781 -0.0239 -0.0096 0.0135  92  CYS   A O   
1974 C CB  . CYS   A 92  ? 0.1621 0.1823 0.1736 -0.0096 -0.0196 0.0112  92  CYS   A CB  
1975 S SG  . CYS   A 92  ? 0.1617 0.1674 0.1724 -0.0097 -0.0078 0.0159  92  CYS   A SG  
1981 N N   . LEU   A 93  ? 0.1497 0.1561 0.1602 -0.0135 0.0021  0.0126  93  LEU   A N   
1982 C CA  . LEU   A 93  ? 0.1390 0.1531 0.1679 -0.0095 -0.0033 0.0156  93  LEU   A CA  
1983 C C   . LEU   A 93  ? 0.1329 0.1452 0.1690 -0.0021 -0.0021 0.0123  93  LEU   A C   
1984 O O   . LEU   A 93  ? 0.1295 0.1479 0.1766 -0.0016 -0.0003 0.0176  93  LEU   A O   
1985 C CB  . LEU   A 93  ? 0.1484 0.1516 0.1949 -0.0036 -0.0038 0.0383  93  LEU   A CB  
1986 C CG  . LEU   A 93  ? 0.1585 0.1469 0.2000 -0.0010 0.0049  0.0279  93  LEU   A CG  
1987 C CD1 . LEU   A 93  ? 0.1556 0.1597 0.2282 0.0077  0.0174  0.0200  93  LEU   A CD1 
1988 C CD2 . LEU   A 93  ? 0.1720 0.1500 0.2193 -0.0101 -0.0022 0.0090  93  LEU   A CD2 
2000 N N   . HIS   A 94  ? 0.1268 0.1371 0.1698 -0.0043 0.0054  0.0213  94  HIS   A N   
2001 C CA  . HIS   A 94  ? 0.1299 0.1352 0.1722 0.0001  0.0024  0.0266  94  HIS   A CA  
2002 C C   . HIS   A 94  ? 0.1280 0.1357 0.1694 -0.0021 0.0079  0.0082  94  HIS   A C   
2003 O O   . HIS   A 94  ? 0.1373 0.1589 0.2082 -0.0011 0.0074  -0.0084 94  HIS   A O   
2004 C CB  . HIS   A 94  ? 0.1256 0.1324 0.1780 -0.0048 -0.0061 0.0220  94  HIS   A CB  
2005 C CG  . HIS   A 94  ? 0.1442 0.1295 0.1657 -0.0074 -0.0113 0.0179  94  HIS   A CG  
2006 N ND1 . HIS   A 94  ? 0.1378 0.1370 0.1763 -0.0027 -0.0062 0.0248  94  HIS   A ND1 
2007 C CD2 . HIS   A 94  ? 0.1564 0.1466 0.1783 -0.0107 -0.0150 0.0114  94  HIS   A CD2 
2008 C CE1 . HIS   A 94  ? 0.1468 0.1435 0.1750 -0.0084 -0.0243 0.0044  94  HIS   A CE1 
2009 N NE2 . HIS   A 94  ? 0.1551 0.1482 0.1723 -0.0128 -0.0131 -0.0026 94  HIS   A NE2 
2017 N N   . VAL   A 95  ? 0.1281 0.1340 0.1547 0.0014  0.0076  0.0066  95  VAL   A N   
2018 C CA  . VAL   A 95  ? 0.1416 0.1382 0.1513 -0.0032 0.0076  0.0056  95  VAL   A CA  
2019 C C   . VAL   A 95  ? 0.1398 0.1350 0.1442 -0.0065 0.0032  0.0083  95  VAL   A C   
2020 O O   . VAL   A 95  ? 0.1440 0.1474 0.1464 0.0142  0.0061  0.0070  95  VAL   A O   
2021 C CB  . VAL   A 95  ? 0.1430 0.1340 0.1790 -0.0068 0.0040  0.0121  95  VAL   A CB  
2022 C CG1 . VAL   A 95  ? 0.1529 0.1403 0.2107 -0.0140 0.0104  -0.0017 95  VAL   A CG1 
2023 C CG2 . VAL   A 95  ? 0.1422 0.1498 0.1923 -0.0123 0.0096  0.0266  95  VAL   A CG2 
2033 N N   A VAL   A 96  ? 0.1403 0.1385 0.1421 0.0002  0.0027  0.0125  96  VAL   A N   
2034 N N   B VAL   A 96  ? 0.1402 0.1344 0.1525 0.0003  0.0013  0.0110  96  VAL   A N   
2035 C CA  A VAL   A 96  ? 0.1465 0.1431 0.1480 0.0026  0.0097  0.0120  96  VAL   A CA  
2036 C CA  B VAL   A 96  ? 0.1472 0.1349 0.1618 0.0038  0.0072  0.0079  96  VAL   A CA  
2037 C C   A VAL   A 96  ? 0.1489 0.1460 0.1505 -0.0002 0.0089  0.0138  96  VAL   A C   
2038 C C   B VAL   A 96  ? 0.1508 0.1407 0.1627 -0.0031 0.0099  0.0079  96  VAL   A C   
2039 O O   A VAL   A 96  ? 0.1566 0.1515 0.1708 0.0012  0.0145  -0.0029 96  VAL   A O   
2040 O O   B VAL   A 96  ? 0.1613 0.1440 0.1891 -0.0062 0.0237  -0.0164 96  VAL   A O   
2041 C CB  A VAL   A 96  ? 0.1494 0.1472 0.1633 0.0021  0.0211  0.0083  96  VAL   A CB  
2042 C CB  B VAL   A 96  ? 0.1510 0.1372 0.1833 0.0024  0.0103  0.0089  96  VAL   A CB  
2043 C CG1 A VAL   A 96  ? 0.1542 0.1524 0.1599 0.0004  0.0189  0.0091  96  VAL   A CG1 
2044 C CG1 B VAL   A 96  ? 0.1614 0.1442 0.1757 0.0030  0.0032  0.0041  96  VAL   A CG1 
2045 C CG2 A VAL   A 96  ? 0.1500 0.1511 0.1702 -0.0084 0.0304  0.0104  96  VAL   A CG2 
2046 C CG2 B VAL   A 96  ? 0.1472 0.1366 0.1949 -0.0043 0.0206  0.0074  96  VAL   A CG2 
2065 N N   . GLY   A 97  ? 0.1464 0.1515 0.1580 -0.0008 0.0103  0.0128  97  GLY   A N   
2066 C CA  . GLY   A 97  ? 0.1568 0.1603 0.1534 -0.0049 -0.0012 0.0189  97  GLY   A CA  
2067 C C   . GLY   A 97  ? 0.1561 0.1671 0.1525 -0.0103 -0.0001 0.0117  97  GLY   A C   
2068 O O   . GLY   A 97  ? 0.1685 0.1600 0.1785 -0.0120 0.0042  0.0145  97  GLY   A O   
2073 N N   . PRO   A 98  ? 0.1611 0.1676 0.1407 -0.0055 0.0019  0.0125  98  PRO   A N   
2074 C CA  . PRO   A 98  ? 0.1724 0.1877 0.1642 -0.0093 0.0048  0.0060  98  PRO   A CA  
2075 C C   . PRO   A 98  ? 0.1771 0.1954 0.1606 -0.0165 -0.0097 0.0197  98  PRO   A C   
2076 O O   . PRO   A 98  ? 0.1693 0.1787 0.1754 -0.0103 -0.0029 0.0206  98  PRO   A O   
2077 C CB  . PRO   A 98  ? 0.1851 0.1965 0.1640 -0.0013 0.0044  -0.0187 98  PRO   A CB  
2078 C CG  . PRO   A 98  ? 0.1825 0.1920 0.1738 0.0015  0.0073  -0.0237 98  PRO   A CG  
2079 C CD  . PRO   A 98  ? 0.1620 0.1701 0.1670 0.0037  -0.0040 -0.0046 98  PRO   A CD  
2087 N N   A ASN   A 99  ? 0.1931 0.2090 0.1615 -0.0141 -0.0053 0.0337  99  ASN   A N   
2088 N N   B ASN   A 99  ? 0.1787 0.2102 0.1497 -0.0175 0.0048  0.0333  99  ASN   A N   
2089 C CA  A ASN   A 99  ? 0.2228 0.2210 0.1690 -0.0143 -0.0143 0.0499  99  ASN   A CA  
2090 C CA  B ASN   A 99  ? 0.1960 0.2233 0.1398 -0.0224 0.0016  0.0511  99  ASN   A CA  
2091 C C   A ASN   A 99  ? 0.2448 0.2447 0.1802 -0.0165 -0.0087 0.0555  99  ASN   A C   
2092 C C   B ASN   A 99  ? 0.2101 0.2487 0.1294 -0.0414 0.0041  0.0602  99  ASN   A C   
2093 O O   A ASN   A 99  ? 0.2482 0.2498 0.1946 -0.0143 -0.0204 0.0737  99  ASN   A O   
2094 O O   B ASN   A 99  ? 0.2092 0.2462 0.1281 -0.0439 -0.0088 0.0523  99  ASN   A O   
2095 C CB  A ASN   A 99  ? 0.2252 0.2142 0.1903 -0.0192 -0.0346 0.0520  99  ASN   A CB  
2096 C CB  B ASN   A 99  ? 0.1897 0.2144 0.1622 -0.0187 -0.0112 0.0451  99  ASN   A CB  
2097 C CG  A ASN   A 99  ? 0.2306 0.2128 0.2090 -0.0193 -0.0423 0.0496  99  ASN   A CG  
2098 C CG  B ASN   A 99  ? 0.1875 0.2122 0.1812 -0.0118 -0.0148 0.0229  99  ASN   A CG  
2099 O OD1 A ASN   A 99  ? 0.2424 0.2199 0.2192 -0.0167 -0.0503 0.0594  99  ASN   A OD1 
2100 O OD1 B ASN   A 99  ? 0.2031 0.2218 0.2040 -0.0062 -0.0207 0.0278  99  ASN   A OD1 
2101 N ND2 A ASN   A 99  ? 0.2325 0.2087 0.2228 -0.0158 -0.0418 0.0497  99  ASN   A ND2 
2102 N ND2 B ASN   A 99  ? 0.1862 0.2099 0.2042 -0.0081 -0.0159 0.0188  99  ASN   A ND2 
2115 N N   A VAL   A 100 ? 0.2589 0.2533 0.1759 -0.0257 -0.0170 0.0357  100 VAL   A N   
2116 N N   B VAL   A 100 ? 0.2244 0.2672 0.1408 -0.0574 -0.0256 0.0639  100 VAL   A N   
2117 C CA  A VAL   A 100 ? 0.2766 0.2729 0.1768 -0.0282 -0.0205 0.0246  100 VAL   A CA  
2118 C CA  B VAL   A 100 ? 0.2526 0.3033 0.1801 -0.0633 -0.0363 0.0620  100 VAL   A CA  
2119 C C   A VAL   A 100 ? 0.2887 0.2937 0.1701 -0.0367 -0.0218 0.0388  100 VAL   A C   
2120 C C   B VAL   A 100 ? 0.2559 0.3266 0.1859 -0.0666 -0.0404 0.0869  100 VAL   A C   
2121 O O   A VAL   A 100 ? 0.2962 0.3033 0.1803 -0.0348 -0.0075 0.0413  100 VAL   A O   
2122 O O   B VAL   A 100 ? 0.2675 0.3448 0.2306 -0.0628 -0.0275 0.0862  100 VAL   A O   
2123 C CB  A VAL   A 100 ? 0.2868 0.2721 0.2010 -0.0291 -0.0222 0.0071  100 VAL   A CB  
2124 C CB  B VAL   A 100 ? 0.2795 0.3111 0.2274 -0.0628 -0.0434 0.0413  100 VAL   A CB  
2125 C CG1 A VAL   A 100 ? 0.2816 0.2739 0.2214 -0.0272 -0.0084 0.0018  100 VAL   A CG1 
2126 C CG1 B VAL   A 100 ? 0.2853 0.3176 0.2586 -0.0628 -0.0386 0.0378  100 VAL   A CG1 
2127 C CG2 A VAL   A 100 ? 0.2955 0.2740 0.2033 -0.0321 -0.0292 0.0068  100 VAL   A CG2 
2128 C CG2 B VAL   A 100 ? 0.2886 0.3131 0.2439 -0.0610 -0.0439 0.0367  100 VAL   A CG2 
2147 N N   A ASN   A 101 ? 0.2908 0.3080 0.2029 -0.0453 -0.0266 0.0602  101 ASN   A N   
2148 N N   B ASN   A 101 ? 0.2502 0.3262 0.1956 -0.0736 -0.0473 0.1161  101 ASN   A N   
2149 C CA  A ASN   A 101 ? 0.3036 0.3308 0.2334 -0.0503 -0.0310 0.0681  101 ASN   A CA  
2150 C CA  B ASN   A 101 ? 0.2601 0.3305 0.1966 -0.0720 -0.0481 0.1284  101 ASN   A CA  
2151 C C   A ASN   A 101 ? 0.3280 0.3613 0.2581 -0.0539 -0.0180 0.0781  101 ASN   A C   
2152 C C   B ASN   A 101 ? 0.2683 0.3572 0.1949 -0.0753 -0.0263 0.1357  101 ASN   A C   
2153 O O   A ASN   A 101 ? 0.3407 0.3654 0.2905 -0.0580 -0.0211 0.0605  101 ASN   A O   
2154 O O   B ASN   A 101 ? 0.2746 0.3713 0.2167 -0.0789 -0.0370 0.1465  101 ASN   A O   
2155 C CB  A ASN   A 101 ? 0.2942 0.3273 0.2500 -0.0514 -0.0461 0.0585  101 ASN   A CB  
2156 C CB  B ASN   A 101 ? 0.2621 0.3026 0.1997 -0.0655 -0.0620 0.1305  101 ASN   A CB  
2157 C CG  A ASN   A 101 ? 0.2862 0.3233 0.2581 -0.0518 -0.0502 0.0442  101 ASN   A CG  
2158 C CG  B ASN   A 101 ? 0.2616 0.2774 0.1912 -0.0690 -0.0606 0.1057  101 ASN   A CG  
2159 O OD1 A ASN   A 101 ? 0.2744 0.3277 0.2573 -0.0446 -0.0581 0.0285  101 ASN   A OD1 
2160 O OD1 B ASN   A 101 ? 0.2557 0.2782 0.2066 -0.0639 -0.0495 0.0728  101 ASN   A OD1 
2161 N ND2 A ASN   A 101 ? 0.2902 0.3216 0.2788 -0.0522 -0.0426 0.0471  101 ASN   A ND2 
2162 N ND2 B ASN   A 101 ? 0.2580 0.2566 0.2091 -0.0789 -0.0592 0.0838  101 ASN   A ND2 
2175 N N   A LYS   A 102 ? 0.3310 0.3864 0.2674 -0.0563 -0.0131 0.0907  102 LYS   A N   
2176 N N   B LYS   A 102 ? 0.2623 0.3722 0.2021 -0.0924 -0.0057 0.1093  102 LYS   A N   
2177 C CA  A LYS   A 102 ? 0.3353 0.4041 0.2630 -0.0605 -0.0114 0.0964  102 LYS   A CA  
2178 C CA  B LYS   A 102 ? 0.2700 0.3828 0.1961 -0.1010 0.0101  0.0853  102 LYS   A CA  
2179 C C   A LYS   A 102 ? 0.3374 0.4195 0.2378 -0.0605 -0.0130 0.1042  102 LYS   A C   
2180 C C   B LYS   A 102 ? 0.2835 0.3962 0.2039 -0.0989 0.0175  0.0679  102 LYS   A C   
2181 O O   A LYS   A 102 ? 0.3428 0.4265 0.2381 -0.0582 -0.0084 0.1081  102 LYS   A O   
2182 O O   B LYS   A 102 ? 0.2881 0.3980 0.2233 -0.0917 0.0249  0.0563  102 LYS   A O   
2183 C CB  A LYS   A 102 ? 0.3407 0.4053 0.2869 -0.0650 -0.0175 0.0882  102 LYS   A CB  
2184 C CB  B LYS   A 102 ? 0.2738 0.3774 0.2036 -0.1121 0.0053  0.0682  102 LYS   A CB  
2185 C CG  A LYS   A 102 ? 0.3458 0.4050 0.3056 -0.0694 -0.0183 0.0791  102 LYS   A CG  
2186 C CG  B LYS   A 102 ? 0.2832 0.3764 0.2195 -0.1195 0.0070  0.0570  102 LYS   A CG  
2187 C CD  A LYS   A 102 ? 0.3518 0.4061 0.3269 -0.0729 -0.0181 0.0664  102 LYS   A CD  
2188 C CD  B LYS   A 102 ? 0.2940 0.3722 0.2289 -0.1249 0.0124  0.0494  102 LYS   A CD  
2189 C CE  A LYS   A 102 ? 0.3566 0.4066 0.3422 -0.0728 -0.0219 0.0561  102 LYS   A CE  
2190 C CE  B LYS   A 102 ? 0.3041 0.3707 0.2553 -0.1241 0.0177  0.0466  102 LYS   A CE  
2191 N NZ  A LYS   A 102 ? 0.3574 0.4049 0.3445 -0.0762 -0.0214 0.0493  102 LYS   A NZ  
2192 N NZ  B LYS   A 102 ? 0.3095 0.3637 0.2508 -0.1318 0.0261  0.0527  102 LYS   A NZ  
2219 N N   A GLY   A 103 ? 0.3332 0.4311 0.2527 -0.0561 -0.0215 0.0868  103 GLY   A N   
2220 N N   B GLY   A 103 ? 0.2944 0.4104 0.2261 -0.0961 0.0189  0.0464  103 GLY   A N   
2221 C CA  A GLY   A 103 ? 0.3279 0.4366 0.2458 -0.0545 -0.0141 0.0711  103 GLY   A CA  
2222 C CA  B GLY   A 103 ? 0.2977 0.4197 0.2097 -0.0929 0.0276  0.0328  103 GLY   A CA  
2223 C C   A GLY   A 103 ? 0.3207 0.4413 0.2464 -0.0553 -0.0050 0.0547  103 GLY   A C   
2224 C C   B GLY   A 103 ? 0.3027 0.4309 0.2402 -0.0874 0.0345  0.0241  103 GLY   A C   
2225 O O   A GLY   A 103 ? 0.3203 0.4448 0.2444 -0.0572 0.0007  0.0508  103 GLY   A O   
2226 O O   B GLY   A 103 ? 0.3141 0.4363 0.2394 -0.0859 0.0395  0.0172  103 GLY   A O   
2233 N N   A GLU   A 104 ? 0.3090 0.4387 0.2253 -0.0560 -0.0040 0.0435  104 GLU   A N   
2234 N N   B GLU   A 104 ? 0.2958 0.4327 0.2193 -0.0808 0.0378  0.0178  104 GLU   A N   
2235 C CA  A GLU   A 104 ? 0.2934 0.4319 0.2128 -0.0628 -0.0004 0.0309  104 GLU   A CA  
2236 C CA  B GLU   A 104 ? 0.2898 0.4316 0.2101 -0.0771 0.0455  0.0097  104 GLU   A CA  
2237 C C   A GLU   A 104 ? 0.2912 0.4396 0.2130 -0.0718 0.0112  0.0040  104 GLU   A C   
2238 C C   B GLU   A 104 ? 0.3019 0.4422 0.2089 -0.0690 0.0406  -0.0040 104 GLU   A C   
2239 O O   A GLU   A 104 ? 0.2905 0.4451 0.2275 -0.0739 0.0149  0.0019  104 GLU   A O   
2240 O O   B GLU   A 104 ? 0.3080 0.4490 0.2261 -0.0686 0.0259  -0.0078 104 GLU   A O   
2241 C CB  A GLU   A 104 ? 0.2731 0.4143 0.1922 -0.0608 -0.0094 0.0514  104 GLU   A CB  
2242 C CB  B GLU   A 104 ? 0.2667 0.4139 0.1817 -0.0829 0.0650  0.0211  104 GLU   A CB  
2243 C CG  A GLU   A 104 ? 0.2602 0.3980 0.2050 -0.0550 -0.0177 0.0681  104 GLU   A CG  
2244 C CG  B GLU   A 104 ? 0.2523 0.3961 0.1848 -0.0838 0.0589  0.0231  104 GLU   A CG  
2245 C CD  A GLU   A 104 ? 0.2477 0.3815 0.1985 -0.0443 -0.0235 0.0861  104 GLU   A CD  
2246 C CD  B GLU   A 104 ? 0.2393 0.3764 0.1802 -0.0809 0.0414  0.0241  104 GLU   A CD  
2247 O OE1 A GLU   A 104 ? 0.2405 0.3698 0.1852 -0.0368 -0.0277 0.0972  104 GLU   A OE1 
2248 O OE1 B GLU   A 104 ? 0.2233 0.3591 0.1481 -0.0808 0.0400  0.0174  104 GLU   A OE1 
2249 O OE2 A GLU   A 104 ? 0.2467 0.3775 0.2126 -0.0422 -0.0130 0.0931  104 GLU   A OE2 
2250 O OE2 B GLU   A 104 ? 0.2490 0.3758 0.2042 -0.0775 0.0221  0.0342  104 GLU   A OE2 
2263 N N   A ASP   A 105 ? 0.2919 0.4395 0.2241 -0.0754 0.0173  -0.0245 105 ASP   A N   
2264 N N   B ASP   A 105 ? 0.3101 0.4439 0.2236 -0.0577 0.0410  -0.0210 105 ASP   A N   
2265 C CA  A ASP   A 105 ? 0.2927 0.4392 0.2538 -0.0740 0.0305  -0.0495 105 ASP   A CA  
2266 C CA  B ASP   A 105 ? 0.3130 0.4442 0.2571 -0.0466 0.0417  -0.0396 105 ASP   A CA  
2267 C C   A ASP   A 105 ? 0.2664 0.4203 0.2152 -0.0845 0.0303  -0.0734 105 ASP   A C   
2268 C C   B ASP   A 105 ? 0.3104 0.4349 0.2413 -0.0483 0.0360  -0.0515 105 ASP   A C   
2269 O O   A ASP   A 105 ? 0.2512 0.4084 0.1782 -0.0839 0.0354  -0.1073 105 ASP   A O   
2270 O O   B ASP   A 105 ? 0.3058 0.4283 0.2177 -0.0422 0.0431  -0.0673 105 ASP   A O   
2271 C CB  A ASP   A 105 ? 0.3118 0.4542 0.3181 -0.0644 0.0364  -0.0555 105 ASP   A CB  
2272 C CB  B ASP   A 105 ? 0.3168 0.4522 0.3037 -0.0372 0.0461  -0.0548 105 ASP   A CB  
2273 C CG  A ASP   A 105 ? 0.3281 0.4670 0.3795 -0.0581 0.0378  -0.0610 105 ASP   A CG  
2274 C CG  B ASP   A 105 ? 0.3202 0.4591 0.3435 -0.0331 0.0437  -0.0702 105 ASP   A CG  
2275 O OD1 A ASP   A 105 ? 0.3302 0.4718 0.3921 -0.0610 0.0382  -0.0694 105 ASP   A OD1 
2276 O OD1 B ASP   A 105 ? 0.3236 0.4643 0.3485 -0.0339 0.0412  -0.0751 105 ASP   A OD1 
2277 O OD2 A ASP   A 105 ? 0.3406 0.4723 0.4126 -0.0559 0.0371  -0.0581 105 ASP   A OD2 
2278 O OD2 B ASP   A 105 ? 0.3215 0.4619 0.3628 -0.0326 0.0473  -0.0783 105 ASP   A OD2 
2287 N N   A ILE   A 106 ? 0.2541 0.4126 0.2195 -0.0919 0.0114  -0.0694 106 ILE   A N   
2288 N N   B ILE   A 106 ? 0.3116 0.4315 0.2601 -0.0529 0.0141  -0.0513 106 ILE   A N   
2289 C CA  A ILE   A 106 ? 0.2323 0.3944 0.2266 -0.1022 -0.0035 -0.0800 106 ILE   A CA  
2290 C CA  B ILE   A 106 ? 0.3074 0.4214 0.2797 -0.0617 0.0005  -0.0590 106 ILE   A CA  
2291 C C   A ILE   A 106 ? 0.2235 0.3678 0.2350 -0.1125 0.0053  -0.1106 106 ILE   A C   
2292 C C   B ILE   A 106 ? 0.3041 0.4021 0.2832 -0.0692 0.0137  -0.0764 106 ILE   A C   
2293 O O   A ILE   A 106 ? 0.2070 0.3525 0.2459 -0.1158 0.0261  -0.1083 106 ILE   A O   
2294 O O   B ILE   A 106 ? 0.2933 0.3933 0.2760 -0.0696 0.0239  -0.0771 106 ILE   A O   
2295 C CB  A ILE   A 106 ? 0.2329 0.4027 0.2512 -0.0877 -0.0197 -0.0461 106 ILE   A CB  
2296 C CB  B ILE   A 106 ? 0.3129 0.4304 0.3093 -0.0563 -0.0192 -0.0375 106 ILE   A CB  
2297 C CG1 A ILE   A 106 ? 0.2212 0.3985 0.2723 -0.0759 -0.0176 -0.0187 106 ILE   A CG1 
2298 C CG1 B ILE   A 106 ? 0.3103 0.4293 0.3370 -0.0524 -0.0272 -0.0261 106 ILE   A CG1 
2299 C CG2 A ILE   A 106 ? 0.2453 0.4104 0.2715 -0.0806 -0.0268 -0.0345 106 ILE   A CG2 
2300 C CG2 B ILE   A 106 ? 0.3183 0.4356 0.3197 -0.0533 -0.0231 -0.0288 106 ILE   A CG2 
2301 C CD1 A ILE   A 106 ? 0.2261 0.3932 0.2841 -0.0586 -0.0014 -0.0046 106 ILE   A CD1 
2302 C CD1 B ILE   A 106 ? 0.3140 0.4257 0.3588 -0.0458 -0.0207 -0.0207 106 ILE   A CD1 
2325 N N   A GLN   A 107 ? 0.2484 0.3600 0.2656 -0.1037 0.0201  -0.1243 107 GLN   A N   
2326 N N   B GLN   A 107 ? 0.3139 0.3901 0.2986 -0.0705 0.0289  -0.0911 107 GLN   A N   
2327 C CA  A GLN   A 107 ? 0.2814 0.3492 0.3399 -0.0837 0.0375  -0.1109 107 GLN   A CA  
2328 C CA  B GLN   A 107 ? 0.3271 0.3739 0.3579 -0.0671 0.0406  -0.0862 107 GLN   A CA  
2329 C C   A GLN   A 107 ? 0.2633 0.3069 0.3269 -0.0706 0.0595  -0.0865 107 GLN   A C   
2330 C C   B GLN   A 107 ? 0.2884 0.3207 0.3287 -0.0627 0.0620  -0.0778 107 GLN   A C   
2331 O O   A GLN   A 107 ? 0.2679 0.2937 0.3776 -0.0651 0.0733  -0.0858 107 GLN   A O   
2332 O O   B GLN   A 107 ? 0.2966 0.3124 0.3750 -0.0588 0.0732  -0.0779 107 GLN   A O   
2333 C CB  A GLN   A 107 ? 0.3275 0.3787 0.4318 -0.0815 0.0235  -0.1090 107 GLN   A CB  
2334 C CB  B GLN   A 107 ? 0.3748 0.4094 0.4504 -0.0705 0.0249  -0.0820 107 GLN   A CB  
2335 C CG  A GLN   A 107 ? 0.3726 0.4087 0.5314 -0.0776 0.0114  -0.0922 107 GLN   A CG  
2336 C CG  B GLN   A 107 ? 0.4239 0.4462 0.5478 -0.0722 0.0117  -0.0682 107 GLN   A CG  
2337 C CD  A GLN   A 107 ? 0.4101 0.4305 0.6173 -0.0710 0.0049  -0.0734 107 GLN   A CD  
2338 C CD  B GLN   A 107 ? 0.4606 0.4703 0.6328 -0.0707 0.0041  -0.0526 107 GLN   A CD  
2339 O OE1 A GLN   A 107 ? 0.4248 0.4392 0.6503 -0.0688 0.0038  -0.0674 107 GLN   A OE1 
2340 O OE1 B GLN   A 107 ? 0.4752 0.4809 0.6654 -0.0695 0.0022  -0.0479 107 GLN   A OE1 
2341 N NE2 A GLN   A 107 ? 0.4219 0.4392 0.6448 -0.0692 0.0012  -0.0698 107 GLN   A NE2 
2342 N NE2 B GLN   A 107 ? 0.4723 0.4796 0.6614 -0.0713 -0.0002 -0.0495 107 GLN   A NE2 
2359 N N   . LEU   A 108 ? 0.2434 0.2722 0.2790 -0.0602 0.0626  -0.0819 108 LEU   A N   
2360 C CA  . LEU   A 108 ? 0.2085 0.2175 0.2452 -0.0315 0.0506  -0.0326 108 LEU   A CA  
2361 C C   . LEU   A 108 ? 0.1895 0.1690 0.2419 -0.0151 0.0350  -0.0110 108 LEU   A C   
2362 O O   . LEU   A 108 ? 0.1768 0.1717 0.2402 -0.0010 0.0304  -0.0013 108 LEU   A O   
2363 C CB  . LEU   A 108 ? 0.2061 0.2291 0.2283 -0.0297 0.0513  -0.0196 108 LEU   A CB  
2364 C CG  . LEU   A 108 ? 0.2158 0.2581 0.2624 -0.0299 0.0520  -0.0228 108 LEU   A CG  
2365 C CD1 . LEU   A 108 ? 0.2329 0.2605 0.2637 -0.0406 0.0691  -0.0150 108 LEU   A CD1 
2366 C CD2 . LEU   A 108 ? 0.2182 0.2868 0.3024 -0.0136 0.0399  -0.0053 108 LEU   A CD2 
2379 N N   . LEU   A 109 ? 0.1752 0.1629 0.2341 0.0035  0.0316  0.0081  109 LEU   A N   
2380 C CA  . LEU   A 109 ? 0.1644 0.1546 0.2231 0.0041  0.0169  0.0159  109 LEU   A CA  
2381 C C   . LEU   A 109 ? 0.1498 0.1430 0.2155 -0.0033 0.0037  0.0059  109 LEU   A C   
2382 O O   . LEU   A 109 ? 0.1576 0.1390 0.2265 0.0025  -0.0004 0.0027  109 LEU   A O   
2383 C CB  . LEU   A 109 ? 0.1646 0.1664 0.2467 0.0139  0.0011  0.0212  109 LEU   A CB  
2384 C CG  . LEU   A 109 ? 0.1575 0.1681 0.2427 0.0093  0.0080  0.0309  109 LEU   A CG  
2385 C CD1 . LEU   A 109 ? 0.1728 0.1661 0.2371 0.0076  0.0182  0.0187  109 LEU   A CD1 
2386 C CD2 . LEU   A 109 ? 0.1582 0.1964 0.2665 -0.0015 0.0042  0.0319  109 LEU   A CD2 
2398 N N   . LYS   A 110 ? 0.1510 0.1497 0.2218 0.0003  -0.0090 -0.0000 110 LYS   A N   
2399 C CA  . LYS   A 110 ? 0.1520 0.1411 0.2399 -0.0041 -0.0100 0.0073  110 LYS   A CA  
2400 C C   . LYS   A 110 ? 0.1495 0.1386 0.2260 -0.0066 0.0033  0.0010  110 LYS   A C   
2401 O O   . LYS   A 110 ? 0.1516 0.1408 0.2233 -0.0052 0.0049  -0.0102 110 LYS   A O   
2402 C CB  . LYS   A 110 ? 0.1625 0.1501 0.2596 -0.0012 -0.0208 -0.0046 110 LYS   A CB  
2403 C CG  . LYS   A 110 ? 0.1662 0.1458 0.2715 0.0018  -0.0223 -0.0085 110 LYS   A CG  
2404 C CD  . LYS   A 110 ? 0.1789 0.1569 0.2864 -0.0061 -0.0169 -0.0175 110 LYS   A CD  
2405 C CE  . LYS   A 110 ? 0.1849 0.1598 0.3104 -0.0162 0.0019  -0.0057 110 LYS   A CE  
2406 N NZ  . LYS   A 110 ? 0.1925 0.1664 0.3323 -0.0195 0.0076  0.0004  110 LYS   A NZ  
2420 N N   . SER   A 111 ? 0.1529 0.1419 0.2247 -0.0015 0.0036  0.0025  111 SER   A N   
2421 C CA  . SER   A 111 ? 0.1429 0.1487 0.2270 0.0000  0.0138  -0.0057 111 SER   A CA  
2422 C C   . SER   A 111 ? 0.1387 0.1399 0.2238 -0.0008 0.0102  0.0097  111 SER   A C   
2423 O O   . SER   A 111 ? 0.1512 0.1370 0.2338 -0.0031 0.0115  0.0073  111 SER   A O   
2424 C CB  . SER   A 111 ? 0.1650 0.1762 0.2326 0.0015  0.0130  -0.0214 111 SER   A CB  
2425 O OG  . SER   A 111 ? 0.2134 0.1985 0.2342 0.0094  0.0231  -0.0361 111 SER   A OG  
2431 N N   . ALA   A 112 ? 0.1467 0.1318 0.2208 -0.0032 0.0143  0.0090  112 ALA   A N   
2432 C CA  . ALA   A 112 ? 0.1610 0.1291 0.2191 -0.0064 0.0165  0.0114  112 ALA   A CA  
2433 C C   . ALA   A 112 ? 0.1435 0.1257 0.2251 0.0016  0.0093  0.0083  112 ALA   A C   
2434 O O   . ALA   A 112 ? 0.1450 0.1347 0.2260 -0.0081 0.0116  0.0171  112 ALA   A O   
2435 C CB  . ALA   A 112 ? 0.1720 0.1325 0.2125 -0.0035 0.0246  0.0039  112 ALA   A CB  
2441 N N   . TYR   A 113 ? 0.1342 0.1345 0.2166 -0.0021 0.0093  0.0210  113 TYR   A N   
2442 C CA  . TYR   A 113 ? 0.1359 0.1346 0.2068 -0.0002 0.0120  0.0139  113 TYR   A CA  
2443 C C   . TYR   A 113 ? 0.1357 0.1296 0.2060 -0.0079 0.0095  0.0194  113 TYR   A C   
2444 O O   . TYR   A 113 ? 0.1434 0.1393 0.2211 -0.0034 0.0126  0.0148  113 TYR   A O   
2445 C CB  . TYR   A 113 ? 0.1348 0.1427 0.2214 -0.0039 -0.0044 0.0212  113 TYR   A CB  
2446 C CG  . TYR   A 113 ? 0.1360 0.1383 0.2084 -0.0111 0.0035  0.0240  113 TYR   A CG  
2447 C CD1 . TYR   A 113 ? 0.1429 0.1521 0.2017 0.0005  0.0024  0.0236  113 TYR   A CD1 
2448 C CD2 . TYR   A 113 ? 0.1457 0.1463 0.2103 -0.0119 0.0061  0.0166  113 TYR   A CD2 
2449 C CE1 . TYR   A 113 ? 0.1449 0.1545 0.2024 0.0025  0.0095  0.0258  113 TYR   A CE1 
2450 C CE2 . TYR   A 113 ? 0.1438 0.1534 0.2062 -0.0111 -0.0040 0.0325  113 TYR   A CE2 
2451 C CZ  . TYR   A 113 ? 0.1440 0.1556 0.1932 -0.0001 0.0050  0.0259  113 TYR   A CZ  
2452 O OH  . TYR   A 113 ? 0.1361 0.1680 0.2197 0.0096  0.0071  0.0330  113 TYR   A OH  
2462 N N   . GLU   A 114 ? 0.1405 0.1281 0.2149 -0.0041 0.0147  0.0154  114 GLU   A N   
2463 C CA  . GLU   A 114 ? 0.1463 0.1269 0.2322 0.0029  0.0083  0.0177  114 GLU   A CA  
2464 C C   . GLU   A 114 ? 0.1393 0.1347 0.2318 -0.0030 0.0139  0.0112  114 GLU   A C   
2465 O O   . GLU   A 114 ? 0.1461 0.1377 0.2362 0.0027  0.0068  0.0207  114 GLU   A O   
2466 C CB  . GLU   A 114 ? 0.1546 0.1351 0.2377 -0.0014 0.0046  0.0138  114 GLU   A CB  
2467 C CG  . GLU   A 114 ? 0.1560 0.1427 0.2640 0.0033  0.0009  0.0030  114 GLU   A CG  
2468 C CD  . GLU   A 114 ? 0.1631 0.1379 0.2629 -0.0062 -0.0069 0.0129  114 GLU   A CD  
2469 O OE1 . GLU   A 114 ? 0.1672 0.1478 0.2671 -0.0096 0.0002  0.0049  114 GLU   A OE1 
2470 O OE2 . GLU   A 114 ? 0.1817 0.1456 0.2843 -0.0153 0.0007  -0.0056 114 GLU   A OE2 
2477 N N   . ASN   A 115 ? 0.1377 0.1352 0.2164 -0.0054 0.0068  0.0075  115 ASN   A N   
2478 C CA  . ASN   A 115 ? 0.1454 0.1426 0.2250 -0.0092 0.0114  0.0194  115 ASN   A CA  
2479 C C   . ASN   A 115 ? 0.1445 0.1423 0.2318 -0.0082 0.0009  0.0183  115 ASN   A C   
2480 O O   . ASN   A 115 ? 0.1450 0.1536 0.2253 -0.0122 0.0106  0.0311  115 ASN   A O   
2481 C CB  . ASN   A 115 ? 0.1591 0.1503 0.2166 -0.0095 0.0063  0.0112  115 ASN   A CB  
2482 C CG  . ASN   A 115 ? 0.1532 0.1600 0.2164 -0.0134 0.0187  0.0089  115 ASN   A CG  
2483 O OD1 . ASN   A 115 ? 0.1591 0.2560 0.2533 -0.0127 0.0285  0.0185  115 ASN   A OD1 
2484 N ND2 . ASN   A 115 ? 0.1517 0.1470 0.2106 -0.0187 0.0319  0.0088  115 ASN   A ND2 
2491 N N   . PHE   A 116 ? 0.1379 0.1413 0.2367 -0.0021 0.0040  0.0253  116 PHE   A N   
2492 C CA  . PHE   A 116 ? 0.1370 0.1531 0.2081 -0.0034 0.0058  0.0241  116 PHE   A CA  
2493 C C   . PHE   A 116 ? 0.1338 0.1582 0.2110 -0.0098 0.0089  0.0273  116 PHE   A C   
2494 O O   . PHE   A 116 ? 0.1458 0.1650 0.2260 0.0045  0.0050  0.0403  116 PHE   A O   
2495 C CB  . PHE   A 116 ? 0.1420 0.1466 0.2279 -0.0060 0.0102  0.0261  116 PHE   A CB  
2496 C CG  . PHE   A 116 ? 0.1357 0.1444 0.2054 -0.0023 0.0069  0.0215  116 PHE   A CG  
2497 C CD1 . PHE   A 116 ? 0.1452 0.1395 0.1969 -0.0060 -0.0014 0.0105  116 PHE   A CD1 
2498 C CD2 . PHE   A 116 ? 0.1439 0.1554 0.2158 -0.0044 0.0011  0.0210  116 PHE   A CD2 
2499 C CE1 . PHE   A 116 ? 0.1467 0.1386 0.2215 -0.0116 0.0048  0.0187  116 PHE   A CE1 
2500 C CE2 . PHE   A 116 ? 0.1469 0.1519 0.2355 0.0042  0.0057  0.0158  116 PHE   A CE2 
2501 C CZ  . PHE   A 116 ? 0.1522 0.1336 0.2360 -0.0039 0.0014  0.0144  116 PHE   A CZ  
2511 N N   . ASN   A 117 ? 0.1399 0.1435 0.2286 -0.0103 0.0091  0.0304  117 ASN   A N   
2512 C CA  . ASN   A 117 ? 0.1429 0.1420 0.2442 -0.0079 0.0114  0.0352  117 ASN   A CA  
2513 C C   . ASN   A 117 ? 0.1448 0.1571 0.2684 -0.0062 0.0127  0.0339  117 ASN   A C   
2514 O O   . ASN   A 117 ? 0.1515 0.1606 0.2748 -0.0064 -0.0062 0.0455  117 ASN   A O   
2515 C CB  . ASN   A 117 ? 0.1427 0.1496 0.2481 -0.0047 0.0120  0.0388  117 ASN   A CB  
2516 C CG  . ASN   A 117 ? 0.1353 0.1484 0.2554 -0.0026 0.0035  0.0336  117 ASN   A CG  
2517 O OD1 . ASN   A 117 ? 0.1377 0.1753 0.2622 -0.0155 0.0037  0.0304  117 ASN   A OD1 
2518 N ND2 . ASN   A 117 ? 0.1381 0.1415 0.2615 0.0011  -0.0001 0.0387  117 ASN   A ND2 
2525 N N   . GLN   A 118 ? 0.1298 0.1644 0.2588 -0.0115 -0.0008 0.0310  118 GLN   A N   
2526 C CA  . GLN   A 118 ? 0.1443 0.1755 0.2619 -0.0154 -0.0090 0.0314  118 GLN   A CA  
2527 C C   . GLN   A 118 ? 0.1482 0.1803 0.2510 -0.0150 -0.0148 0.0470  118 GLN   A C   
2528 O O   . GLN   A 118 ? 0.1476 0.2159 0.2679 -0.0094 -0.0151 0.0244  118 GLN   A O   
2529 C CB  . GLN   A 118 ? 0.1405 0.1721 0.2716 -0.0106 0.0071  0.0384  118 GLN   A CB  
2530 C CG  . GLN   A 118 ? 0.1462 0.1753 0.2633 -0.0047 0.0124  0.0461  118 GLN   A CG  
2531 C CD  . GLN   A 118 ? 0.1471 0.1753 0.2846 -0.0078 0.0062  0.0339  118 GLN   A CD  
2532 O OE1 . GLN   A 118 ? 0.1494 0.1851 0.3027 0.0065  0.0025  0.0203  118 GLN   A OE1 
2533 N NE2 . GLN   A 118 ? 0.1540 0.1745 0.2716 -0.0013 0.0002  0.0387  118 GLN   A NE2 
2542 N N   . HIS   A 119 ? 0.1487 0.1789 0.2356 -0.0119 -0.0102 0.0482  119 HIS   A N   
2543 C CA  . HIS   A 119 ? 0.1594 0.1937 0.2296 -0.0175 -0.0057 0.0643  119 HIS   A CA  
2544 C C   . HIS   A 119 ? 0.1722 0.2111 0.2295 -0.0198 -0.0014 0.0644  119 HIS   A C   
2545 O O   . HIS   A 119 ? 0.1732 0.2101 0.2343 -0.0335 -0.0098 0.0571  119 HIS   A O   
2546 C CB  . HIS   A 119 ? 0.1705 0.1865 0.2496 -0.0129 0.0125  0.0666  119 HIS   A CB  
2547 C CG  . HIS   A 119 ? 0.1719 0.1908 0.2748 -0.0037 0.0017  0.0629  119 HIS   A CG  
2548 N ND1 . HIS   A 119 ? 0.1916 0.2076 0.3168 -0.0128 0.0036  0.0428  119 HIS   A ND1 
2549 C CD2 . HIS   A 119 ? 0.1744 0.1897 0.2795 0.0083  0.0130  0.0605  119 HIS   A CD2 
2550 C CE1 . HIS   A 119 ? 0.1850 0.1957 0.3187 -0.0233 0.0157  0.0566  119 HIS   A CE1 
2551 N NE2 . HIS   A 119 ? 0.1886 0.1932 0.3130 -0.0050 0.0242  0.0668  119 HIS   A NE2 
2559 N N   A GLU   A 120 ? 0.1794 0.2328 0.2335 -0.0186 -0.0091 0.0826  120 GLU   A N   
2560 N N   B GLU   A 120 ? 0.1758 0.2362 0.2362 -0.0209 -0.0104 0.0885  120 GLU   A N   
2561 C CA  A GLU   A 120 ? 0.2133 0.2654 0.2641 -0.0128 -0.0027 0.1109  120 GLU   A CA  
2562 C CA  B GLU   A 120 ? 0.2092 0.2692 0.2590 -0.0148 -0.0050 0.1250  120 GLU   A CA  
2563 C C   A GLU   A 120 ? 0.1838 0.2505 0.2350 -0.0237 0.0036  0.1093  120 GLU   A C   
2564 C C   B GLU   A 120 ? 0.1827 0.2618 0.2339 -0.0222 -0.0041 0.1152  120 GLU   A C   
2565 O O   A GLU   A 120 ? 0.1812 0.2395 0.2487 -0.0323 -0.0035 0.1158  120 GLU   A O   
2566 O O   B GLU   A 120 ? 0.1848 0.2627 0.2549 -0.0295 -0.0108 0.1090  120 GLU   A O   
2567 C CB  A GLU   A 120 ? 0.2904 0.3271 0.3375 -0.0012 -0.0045 0.1210  120 GLU   A CB  
2568 C CB  B GLU   A 120 ? 0.2841 0.3266 0.3232 -0.0064 -0.0018 0.1444  120 GLU   A CB  
2569 C CG  A GLU   A 120 ? 0.3722 0.3923 0.4361 0.0054  -0.0037 0.1115  120 GLU   A CG  
2570 C CG  B GLU   A 120 ? 0.3667 0.3924 0.4255 0.0003  0.0007  0.1335  120 GLU   A CG  
2571 C CD  A GLU   A 120 ? 0.4396 0.4425 0.5261 0.0105  0.0024  0.0962  120 GLU   A CD  
2572 C CD  B GLU   A 120 ? 0.4368 0.4439 0.5193 0.0061  0.0072  0.1153  120 GLU   A CD  
2573 O OE1 A GLU   A 120 ? 0.4612 0.4593 0.5507 0.0108  0.0039  0.0908  120 GLU   A OE1 
2574 O OE1 B GLU   A 120 ? 0.4606 0.4617 0.5428 0.0071  0.0100  0.1101  120 GLU   A OE1 
2575 O OE2 A GLU   A 120 ? 0.4628 0.4627 0.5616 0.0121  0.0049  0.0871  120 GLU   A OE2 
2576 O OE2 B GLU   A 120 ? 0.4629 0.4647 0.5581 0.0075  0.0093  0.1044  120 GLU   A OE2 
2589 N N   A VAL   A 121 ? 0.1776 0.2536 0.2112 -0.0169 0.0077  0.0923  121 VAL   A N   
2590 N N   B VAL   A 121 ? 0.1785 0.2608 0.2137 -0.0140 -0.0036 0.1005  121 VAL   A N   
2591 C CA  A VAL   A 121 ? 0.1833 0.2585 0.1982 -0.0229 0.0215  0.0812  121 VAL   A CA  
2592 C CA  B VAL   A 121 ? 0.1860 0.2632 0.1990 -0.0194 0.0102  0.0895  121 VAL   A CA  
2593 C C   A VAL   A 121 ? 0.1689 0.2346 0.1918 -0.0282 0.0091  0.0658  121 VAL   A C   
2594 C C   B VAL   A 121 ? 0.1657 0.2357 0.1726 -0.0245 0.0071  0.0745  121 VAL   A C   
2595 O O   A VAL   A 121 ? 0.1714 0.2353 0.2194 -0.0322 0.0046  0.0508  121 VAL   A O   
2596 O O   B VAL   A 121 ? 0.1559 0.2310 0.1528 -0.0274 0.0090  0.0671  121 VAL   A O   
2597 C CB  A VAL   A 121 ? 0.2141 0.2931 0.2377 -0.0153 0.0338  0.0771  121 VAL   A CB  
2598 C CB  B VAL   A 121 ? 0.2242 0.2973 0.2421 -0.0102 0.0188  0.0838  121 VAL   A CB  
2599 C CG1 A VAL   A 121 ? 0.2198 0.3072 0.2484 -0.0109 0.0399  0.0801  121 VAL   A CG1 
2600 C CG1 B VAL   A 121 ? 0.2312 0.3106 0.2478 -0.0058 0.0285  0.0883  121 VAL   A CG1 
2601 C CG2 A VAL   A 121 ? 0.2298 0.3048 0.2664 -0.0222 0.0318  0.0688  121 VAL   A CG2 
2602 C CG2 B VAL   A 121 ? 0.2435 0.3104 0.2717 -0.0150 0.0149  0.0717  121 VAL   A CG2 
2621 N N   . LEU   A 122 ? 0.1582 0.2146 0.1842 -0.0321 -0.0011 0.0586  122 LEU   A N   
2622 C CA  . LEU   A 122 ? 0.1694 0.1927 0.1786 -0.0261 0.0058  0.0499  122 LEU   A CA  
2623 C C   . LEU   A 122 ? 0.1611 0.1911 0.1792 -0.0354 0.0001  0.0360  122 LEU   A C   
2624 O O   . LEU   A 122 ? 0.1663 0.1968 0.2087 -0.0337 -0.0049 0.0415  122 LEU   A O   
2625 C CB  . LEU   A 122 ? 0.1884 0.1870 0.2166 -0.0128 0.0024  0.0624  122 LEU   A CB  
2626 C CG  . LEU   A 122 ? 0.1845 0.1914 0.2208 -0.0130 0.0126  0.0399  122 LEU   A CG  
2627 C CD1 . LEU   A 122 ? 0.2019 0.1895 0.2198 -0.0229 0.0227  0.0442  122 LEU   A CD1 
2628 C CD2 . LEU   A 122 ? 0.1779 0.1865 0.2153 -0.0093 0.0223  0.0371  122 LEU   A CD2 
2641 N N   A LEU   A 123 ? 0.1544 0.1876 0.1698 -0.0341 -0.0065 0.0238  123 LEU   A N   
2642 N N   B LEU   A 123 ? 0.1502 0.1926 0.1804 -0.0371 -0.0026 0.0408  123 LEU   A N   
2643 C CA  A LEU   A 123 ? 0.1604 0.1886 0.1564 -0.0237 -0.0096 0.0129  123 LEU   A CA  
2644 C CA  B LEU   A 123 ? 0.1507 0.1980 0.1690 -0.0312 0.0008  0.0488  123 LEU   A CA  
2645 C C   A LEU   A 123 ? 0.1629 0.1786 0.1294 -0.0182 0.0037  0.0143  123 LEU   A C   
2646 C C   B LEU   A 123 ? 0.1446 0.1894 0.1724 -0.0306 0.0001  0.0528  123 LEU   A C   
2647 O O   A LEU   A 123 ? 0.1615 0.1762 0.1317 -0.0220 0.0065  0.0092  123 LEU   A O   
2648 O O   B LEU   A 123 ? 0.1374 0.1922 0.2103 -0.0361 0.0010  0.0478  123 LEU   A O   
2649 C CB  A LEU   A 123 ? 0.1696 0.2061 0.1746 -0.0238 -0.0119 0.0105  123 LEU   A CB  
2650 C CB  B LEU   A 123 ? 0.1617 0.2127 0.1486 -0.0389 0.0281  0.0569  123 LEU   A CB  
2651 C CG  A LEU   A 123 ? 0.1741 0.2189 0.1890 -0.0164 -0.0088 0.0075  123 LEU   A CG  
2652 C CG  B LEU   A 123 ? 0.1677 0.2250 0.1816 -0.0312 0.0197  0.0312  123 LEU   A CG  
2653 C CD1 A LEU   A 123 ? 0.1778 0.2216 0.1968 -0.0124 -0.0026 -0.0036 123 LEU   A CD1 
2654 C CD1 B LEU   A 123 ? 0.1743 0.2262 0.1914 -0.0248 0.0222  0.0146  123 LEU   A CD1 
2655 C CD2 A LEU   A 123 ? 0.1798 0.2269 0.2000 -0.0150 -0.0153 0.0046  123 LEU   A CD2 
2656 C CD2 B LEU   A 123 ? 0.1730 0.2337 0.1829 -0.0308 0.0160  0.0254  123 LEU   A CD2 
2679 N N   A ALA   A 124 ? 0.1602 0.1676 0.1316 -0.0152 0.0037  0.0145  124 ALA   A N   
2680 N N   B ALA   A 124 ? 0.1407 0.1741 0.1583 -0.0349 0.0001  0.0552  124 ALA   A N   
2681 C CA  A ALA   A 124 ? 0.1516 0.1580 0.1187 -0.0070 0.0082  0.0074  124 ALA   A CA  
2682 C CA  B ALA   A 124 ? 0.1394 0.1652 0.1786 -0.0321 0.0076  0.0394  124 ALA   A CA  
2683 C C   A ALA   A 124 ? 0.1534 0.1536 0.1085 -0.0057 0.0076  0.0110  124 ALA   A C   
2684 C C   B ALA   A 124 ? 0.1349 0.1593 0.1675 -0.0207 0.0054  0.0212  124 ALA   A C   
2685 O O   A ALA   A 124 ? 0.1617 0.1533 0.1127 -0.0068 0.0195  0.0157  124 ALA   A O   
2686 O O   B ALA   A 124 ? 0.1265 0.1476 0.1816 -0.0127 0.0090  0.0043  124 ALA   A O   
2687 C CB  A ALA   A 124 ? 0.1484 0.1514 0.1432 0.0054  0.0090  0.0110  124 ALA   A CB  
2688 C CB  B ALA   A 124 ? 0.1520 0.1621 0.2052 -0.0234 0.0144  0.0371  124 ALA   A CB  
2699 N N   A PRO   A 125 ? 0.1523 0.1490 0.1193 -0.0058 0.0048  0.0212  125 PRO   A N   
2700 N N   B PRO   A 125 ? 0.1352 0.1532 0.1659 -0.0196 -0.0003 0.0116  125 PRO   A N   
2701 C CA  A PRO   A 125 ? 0.1552 0.1526 0.1437 -0.0117 0.0051  0.0087  125 PRO   A CA  
2702 C CA  B PRO   A 125 ? 0.1385 0.1470 0.1646 -0.0076 0.0037  0.0085  125 PRO   A CA  
2703 C C   A PRO   A 125 ? 0.1535 0.1650 0.1466 -0.0086 0.0059  0.0008  125 PRO   A C   
2704 C C   B PRO   A 125 ? 0.1278 0.1444 0.1342 -0.0051 0.0135  0.0130  125 PRO   A C   
2705 O O   A PRO   A 125 ? 0.1568 0.1659 0.1274 -0.0040 0.0093  0.0004  125 PRO   A O   
2706 O O   B PRO   A 125 ? 0.1376 0.1470 0.1403 -0.0026 0.0174  0.0232  125 PRO   A O   
2707 C CB  A PRO   A 125 ? 0.1622 0.1521 0.1540 -0.0176 0.0195  0.0056  125 PRO   A CB  
2708 C CB  B PRO   A 125 ? 0.1629 0.1485 0.1781 -0.0127 0.0130  0.0119  125 PRO   A CB  
2709 C CG  A PRO   A 125 ? 0.1631 0.1554 0.1626 -0.0213 0.0102  0.0178  125 PRO   A CG  
2710 C CG  B PRO   A 125 ? 0.1626 0.1491 0.1715 -0.0167 0.0165  0.0201  125 PRO   A CG  
2711 C CD  A PRO   A 125 ? 0.1596 0.1567 0.1568 -0.0145 0.0107  0.0172  125 PRO   A CD  
2712 C CD  B PRO   A 125 ? 0.1406 0.1475 0.1556 -0.0240 0.0151  0.0147  125 PRO   A CD  
2727 N N   A LEU   A 126 ? 0.1576 0.1731 0.1527 -0.0153 0.0103  -0.0040 126 LEU   A N   
2728 N N   B LEU   A 126 ? 0.1256 0.1480 0.1711 0.0021  0.0030  0.0174  126 LEU   A N   
2729 C CA  A LEU   A 126 ? 0.1543 0.1673 0.1521 -0.0206 0.0137  -0.0000 126 LEU   A CA  
2730 C CA  B LEU   A 126 ? 0.1324 0.1551 0.1783 -0.0022 -0.0015 0.0239  126 LEU   A CA  
2731 C C   A LEU   A 126 ? 0.1597 0.1554 0.1638 -0.0117 0.0149  -0.0021 126 LEU   A C   
2732 C C   B LEU   A 126 ? 0.1360 0.1490 0.1890 -0.0020 -0.0154 0.0211  126 LEU   A C   
2733 O O   A LEU   A 126 ? 0.1724 0.1449 0.1996 -0.0123 0.0193  0.0089  126 LEU   A O   
2734 O O   B LEU   A 126 ? 0.1451 0.1371 0.2005 -0.0035 -0.0014 0.0108  126 LEU   A O   
2735 C CB  A LEU   A 126 ? 0.1511 0.1827 0.1866 -0.0311 0.0081  0.0032  126 LEU   A CB  
2736 C CB  B LEU   A 126 ? 0.1472 0.1653 0.1849 -0.0002 0.0084  0.0229  126 LEU   A CB  
2737 C CG  A LEU   A 126 ? 0.1449 0.1980 0.2127 -0.0309 0.0040  0.0045  126 LEU   A CG  
2738 C CG  B LEU   A 126 ? 0.1605 0.1810 0.2186 -0.0018 0.0116  0.0270  126 LEU   A CG  
2739 C CD1 A LEU   A 126 ? 0.1407 0.2073 0.2457 -0.0271 0.0024  0.0096  126 LEU   A CD1 
2740 C CD1 B LEU   A 126 ? 0.1700 0.1960 0.2602 -0.0046 0.0084  0.0276  126 LEU   A CD1 
2741 C CD2 A LEU   A 126 ? 0.1571 0.2026 0.2203 -0.0368 -0.0015 0.0139  126 LEU   A CD2 
2742 C CD2 B LEU   A 126 ? 0.1727 0.1734 0.2206 -0.0033 0.0113  0.0299  126 LEU   A CD2 
2765 N N   A LEU   A 127 ? 0.1610 0.1643 0.1632 -0.0008 0.0242  0.0047  127 LEU   A N   
2766 N N   B LEU   A 127 ? 0.1308 0.1564 0.1718 0.0028  -0.0021 0.0514  127 LEU   A N   
2767 C CA  A LEU   A 127 ? 0.1632 0.1586 0.1515 -0.0019 0.0122  0.0085  127 LEU   A CA  
2768 C CA  B LEU   A 127 ? 0.1277 0.1527 0.1674 -0.0021 -0.0043 0.0390  127 LEU   A CA  
2769 C C   A LEU   A 127 ? 0.1636 0.1571 0.1347 -0.0015 0.0146  0.0157  127 LEU   A C   
2770 C C   B LEU   A 127 ? 0.1264 0.1354 0.1812 0.0115  -0.0096 0.0180  127 LEU   A C   
2771 O O   A LEU   A 127 ? 0.1706 0.1611 0.1442 -0.0010 0.0182  0.0153  127 LEU   A O   
2772 O O   B LEU   A 127 ? 0.1316 0.1292 0.1915 0.0008  -0.0047 0.0165  127 LEU   A O   
2773 C CB  A LEU   A 127 ? 0.1615 0.1499 0.1705 0.0052  0.0048  0.0122  127 LEU   A CB  
2774 C CB  B LEU   A 127 ? 0.1341 0.1640 0.1720 -0.0037 0.0047  0.0352  127 LEU   A CB  
2775 C CG  A LEU   A 127 ? 0.1614 0.1388 0.1916 0.0095  -0.0099 0.0113  127 LEU   A CG  
2776 C CG  B LEU   A 127 ? 0.1464 0.1879 0.1743 0.0004  -0.0022 0.0323  127 LEU   A CG  
2777 C CD1 A LEU   A 127 ? 0.1536 0.1287 0.1964 0.0021  -0.0120 0.0003  127 LEU   A CD1 
2778 C CD1 B LEU   A 127 ? 0.1484 0.1961 0.1906 0.0099  0.0065  0.0280  127 LEU   A CD1 
2779 C CD2 A LEU   A 127 ? 0.1709 0.1333 0.2101 0.0220  -0.0042 0.0077  127 LEU   A CD2 
2780 C CD2 B LEU   A 127 ? 0.1677 0.2039 0.1846 0.0093  -0.0102 0.0028  127 LEU   A CD2 
2803 N N   A SER   A 128 ? 0.1606 0.1571 0.1318 -0.0127 0.0123  0.0217  128 SER   A N   
2804 N N   B SER   A 128 ? 0.1374 0.1347 0.1739 0.0002  -0.0203 0.0096  128 SER   A N   
2805 C CA  A SER   A 128 ? 0.1601 0.1582 0.1253 -0.0161 0.0014  0.0129  128 SER   A CA  
2806 C CA  B SER   A 128 ? 0.1565 0.1391 0.1592 0.0070  -0.0176 0.0047  128 SER   A CA  
2807 C C   A SER   A 128 ? 0.1683 0.1546 0.1341 -0.0095 0.0029  0.0062  128 SER   A C   
2808 C C   B SER   A 128 ? 0.1693 0.1407 0.1481 0.0143  -0.0203 0.0237  128 SER   A C   
2809 O O   A SER   A 128 ? 0.1795 0.1671 0.1414 -0.0088 -0.0007 -0.0041 128 SER   A O   
2810 O O   B SER   A 128 ? 0.1796 0.1550 0.1557 0.0168  -0.0058 0.0213  128 SER   A O   
2811 C CB  A SER   A 128 ? 0.1534 0.1586 0.1352 -0.0195 0.0098  0.0115  128 SER   A CB  
2812 C CB  B SER   A 128 ? 0.1634 0.1529 0.1712 0.0107  -0.0074 0.0033  128 SER   A CB  
2813 O OG  A SER   A 128 ? 0.1547 0.1551 0.1484 -0.0165 0.0081  0.0018  128 SER   A OG  
2814 O OG  B SER   A 128 ? 0.1686 0.1659 0.1842 0.0070  0.0054  -0.0004 128 SER   A OG  
2825 N N   A ALA   A 129 ? 0.1652 0.1523 0.1439 -0.0067 0.0013  0.0052  129 ALA   A N   
2826 N N   B ALA   A 129 ? 0.1684 0.1452 0.1524 0.0137  -0.0175 0.0227  129 ALA   A N   
2827 C CA  A ALA   A 129 ? 0.1624 0.1541 0.1677 0.0025  -0.0034 0.0053  129 ALA   A CA  
2828 C CA  B ALA   A 129 ? 0.1624 0.1457 0.1639 0.0122  -0.0164 0.0156  129 ALA   A CA  
2829 C C   A ALA   A 129 ? 0.1645 0.1579 0.1679 0.0019  -0.0109 0.0041  129 ALA   A C   
2830 C C   B ALA   A 129 ? 0.1637 0.1507 0.1695 0.0134  -0.0205 0.0013  129 ALA   A C   
2831 O O   A ALA   A 129 ? 0.1655 0.1640 0.1267 -0.0120 -0.0108 0.0242  129 ALA   A O   
2832 O O   B ALA   A 129 ? 0.1662 0.1579 0.1486 0.0150  -0.0248 0.0109  129 ALA   A O   
2833 C CB  A ALA   A 129 ? 0.1647 0.1601 0.1808 -0.0040 -0.0071 -0.0121 129 ALA   A CB  
2834 C CB  B ALA   A 129 ? 0.1588 0.1609 0.1517 0.0011  -0.0160 0.0093  129 ALA   A CB  
2845 N N   A GLY   A 130 ? 0.1779 0.1518 0.2093 0.0070  -0.0154 0.0020  130 GLY   A N   
2846 N N   B GLY   A 130 ? 0.1656 0.1517 0.2052 -0.0006 -0.0165 0.0130  130 GLY   A N   
2847 C CA  A GLY   A 130 ? 0.1871 0.1524 0.2198 0.0117  -0.0247 0.0044  130 GLY   A CA  
2848 C CA  B GLY   A 130 ? 0.1700 0.1543 0.1987 0.0011  -0.0089 0.0096  130 GLY   A CA  
2849 C C   A GLY   A 130 ? 0.1931 0.1545 0.2193 0.0131  -0.0343 -0.0026 130 GLY   A C   
2850 C C   B GLY   A 130 ? 0.1695 0.1478 0.1812 0.0009  -0.0099 0.0045  130 GLY   A C   
2851 O O   A GLY   A 130 ? 0.1888 0.1642 0.2412 0.0219  -0.0445 -0.0058 130 GLY   A O   
2852 O O   B GLY   A 130 ? 0.1633 0.1512 0.1864 -0.0043 -0.0072 0.0120  130 GLY   A O   
2859 N N   A ILE   A 131 ? 0.1975 0.1507 0.2088 -0.0001 -0.0364 0.0129  131 ILE   A N   
2860 N N   B ILE   A 131 ? 0.1729 0.1423 0.1962 0.0013  -0.0115 0.0120  131 ILE   A N   
2861 C CA  A ILE   A 131 ? 0.2047 0.1588 0.1890 -0.0107 -0.0496 0.0187  131 ILE   A CA  
2862 C CA  B ILE   A 131 ? 0.1724 0.1438 0.1870 0.0009  -0.0261 0.0005  131 ILE   A CA  
2863 C C   A ILE   A 131 ? 0.1979 0.1619 0.1872 -0.0115 -0.0398 0.0301  131 ILE   A C   
2864 C C   B ILE   A 131 ? 0.1782 0.1524 0.1937 -0.0036 -0.0208 0.0202  131 ILE   A C   
2865 O O   A ILE   A 131 ? 0.2102 0.1689 0.1937 -0.0084 -0.0334 0.0265  131 ILE   A O   
2866 O O   B ILE   A 131 ? 0.1875 0.1538 0.2113 -0.0080 -0.0138 0.0287  131 ILE   A O   
2867 C CB  A ILE   A 131 ? 0.2163 0.1777 0.1819 -0.0185 -0.0679 0.0179  131 ILE   A CB  
2868 C CB  B ILE   A 131 ? 0.1796 0.1518 0.2025 -0.0021 -0.0379 -0.0077 131 ILE   A CB  
2869 C CG1 A ILE   A 131 ? 0.2255 0.2081 0.2131 -0.0252 -0.0619 0.0152  131 ILE   A CG1 
2870 C CG1 B ILE   A 131 ? 0.1785 0.1684 0.2118 -0.0013 -0.0324 0.0023  131 ILE   A CG1 
2871 C CG2 A ILE   A 131 ? 0.2231 0.1724 0.1868 -0.0182 -0.0619 0.0121  131 ILE   A CG2 
2872 C CG2 B ILE   A 131 ? 0.1815 0.1313 0.2010 0.0047  -0.0439 -0.0165 131 ILE   A CG2 
2873 C CD1 A ILE   A 131 ? 0.2318 0.2203 0.2400 -0.0251 -0.0647 0.0149  131 ILE   A CD1 
2874 C CD1 B ILE   A 131 ? 0.1844 0.1760 0.2244 -0.0047 -0.0307 -0.0055 131 ILE   A CD1 
2897 N N   A PHE   A 132 ? 0.1782 0.1569 0.1774 -0.0040 -0.0286 0.0352  132 PHE   A N   
2898 N N   B PHE   A 132 ? 0.1769 0.1554 0.1876 0.0060  -0.0054 0.0192  132 PHE   A N   
2899 C CA  A PHE   A 132 ? 0.1760 0.1576 0.1847 -0.0198 -0.0157 0.0202  132 PHE   A CA  
2900 C CA  B PHE   A 132 ? 0.1876 0.1688 0.1768 -0.0052 -0.0127 0.0187  132 PHE   A CA  
2901 C C   A PHE   A 132 ? 0.1870 0.1698 0.1894 -0.0167 -0.0116 0.0228  132 PHE   A C   
2902 C C   B PHE   A 132 ? 0.2016 0.1772 0.1861 -0.0041 -0.0158 0.0254  132 PHE   A C   
2903 O O   A PHE   A 132 ? 0.1911 0.1788 0.1953 -0.0151 -0.0054 0.0239  132 PHE   A O   
2904 O O   B PHE   A 132 ? 0.2066 0.1914 0.1958 0.0010  -0.0243 0.0295  132 PHE   A O   
2905 C CB  A PHE   A 132 ? 0.1537 0.1463 0.1736 -0.0269 -0.0108 0.0237  132 PHE   A CB  
2906 C CB  B PHE   A 132 ? 0.1873 0.1715 0.1686 -0.0030 -0.0082 0.0153  132 PHE   A CB  
2907 C CG  A PHE   A 132 ? 0.1512 0.1382 0.1675 -0.0181 -0.0155 0.0175  132 PHE   A CG  
2908 C CG  B PHE   A 132 ? 0.1790 0.1742 0.1750 0.0071  -0.0059 0.0169  132 PHE   A CG  
2909 C CD1 A PHE   A 132 ? 0.1596 0.1503 0.1871 -0.0056 -0.0113 0.0093  132 PHE   A CD1 
2910 C CD1 B PHE   A 132 ? 0.1789 0.1838 0.1882 0.0107  -0.0101 0.0038  132 PHE   A CD1 
2911 C CD2 A PHE   A 132 ? 0.1563 0.1491 0.1662 -0.0043 -0.0204 0.0058  132 PHE   A CD2 
2912 C CD2 B PHE   A 132 ? 0.1768 0.1810 0.1747 0.0053  0.0001  0.0131  132 PHE   A CD2 
2913 C CE1 A PHE   A 132 ? 0.1659 0.1526 0.1957 -0.0034 -0.0133 -0.0019 132 PHE   A CE1 
2914 C CE1 B PHE   A 132 ? 0.1792 0.1858 0.1971 0.0098  0.0061  -0.0046 132 PHE   A CE1 
2915 C CE2 A PHE   A 132 ? 0.1579 0.1544 0.1773 0.0003  -0.0120 0.0033  132 PHE   A CE2 
2916 C CE2 B PHE   A 132 ? 0.1757 0.1800 0.1821 0.0050  0.0203  0.0091  132 PHE   A CE2 
2917 C CZ  A PHE   A 132 ? 0.1624 0.1518 0.1836 -0.0053 -0.0312 0.0033  132 PHE   A CZ  
2918 C CZ  B PHE   A 132 ? 0.1758 0.1814 0.1784 0.0032  0.0097  0.0078  132 PHE   A CZ  
2937 N N   A GLY   A 133 ? 0.1821 0.1759 0.1798 -0.0191 -0.0338 0.0202  133 GLY   A N   
2938 N N   B GLY   A 133 ? 0.1978 0.1726 0.1820 -0.0112 -0.0286 0.0227  133 GLY   A N   
2939 C CA  A GLY   A 133 ? 0.1865 0.1834 0.1740 -0.0126 -0.0264 0.0135  133 GLY   A CA  
2940 C CA  B GLY   A 133 ? 0.1995 0.1703 0.1714 -0.0119 -0.0243 0.0082  133 GLY   A CA  
2941 C C   A GLY   A 133 ? 0.1886 0.1915 0.1617 -0.0122 -0.0215 -0.0008 133 GLY   A C   
2942 C C   B GLY   A 133 ? 0.1972 0.1783 0.1638 -0.0166 -0.0290 0.0012  133 GLY   A C   
2943 O O   A GLY   A 133 ? 0.1963 0.2065 0.1485 -0.0038 -0.0096 -0.0355 133 GLY   A O   
2944 O O   B GLY   A 133 ? 0.2072 0.1993 0.1464 -0.0133 -0.0126 -0.0019 133 GLY   A O   
2951 N N   A ALA   A 134 ? 0.1867 0.1851 0.1655 -0.0147 -0.0127 -0.0010 134 ALA   A N   
2952 N N   B ALA   A 134 ? 0.1927 0.1674 0.1703 -0.0223 -0.0321 -0.0030 134 ALA   A N   
2953 C CA  A ALA   A 134 ? 0.1875 0.1834 0.1840 -0.0100 0.0004  0.0070  134 ALA   A CA  
2954 C CA  B ALA   A 134 ? 0.1924 0.1682 0.1877 -0.0133 -0.0315 -0.0067 134 ALA   A CA  
2955 C C   A ALA   A 134 ? 0.1922 0.1873 0.1924 -0.0101 0.0050  0.0130  134 ALA   A C   
2956 C C   B ALA   A 134 ? 0.1927 0.1769 0.1793 -0.0098 -0.0282 0.0053  134 ALA   A C   
2957 O O   A ALA   A 134 ? 0.2060 0.1937 0.2074 -0.0077 0.0194  0.0103  134 ALA   A O   
2958 O O   B ALA   A 134 ? 0.2110 0.1853 0.1776 -0.0073 -0.0133 0.0170  134 ALA   A O   
2959 C CB  A ALA   A 134 ? 0.1946 0.1813 0.2073 -0.0034 -0.0014 -0.0032 134 ALA   A CB  
2960 C CB  B ALA   A 134 ? 0.2039 0.1660 0.2280 -0.0061 -0.0363 -0.0203 134 ALA   A CB  
2971 N N   A ASP   A 135 ? 0.1971 0.1902 0.1940 -0.0131 -0.0039 0.0154  135 ASP   A N   
2972 N N   B ASP   A 135 ? 0.1948 0.1814 0.2000 -0.0130 -0.0292 0.0041  135 ASP   A N   
2973 C CA  A ASP   A 135 ? 0.1933 0.2054 0.1987 -0.0227 -0.0174 0.0167  135 ASP   A CA  
2974 C CA  B ASP   A 135 ? 0.1939 0.2006 0.2157 -0.0221 -0.0326 0.0184  135 ASP   A CA  
2975 C C   A ASP   A 135 ? 0.1833 0.1968 0.1917 -0.0086 -0.0085 0.0122  135 ASP   A C   
2976 C C   B ASP   A 135 ? 0.1794 0.1904 0.2027 -0.0178 -0.0144 0.0307  135 ASP   A C   
2977 O O   A ASP   A 135 ? 0.1808 0.1977 0.1934 -0.0009 0.0019  0.0166  135 ASP   A O   
2978 O O   B ASP   A 135 ? 0.1761 0.1828 0.2210 -0.0152 -0.0157 0.0473  135 ASP   A O   
2979 C CB  A ASP   A 135 ? 0.2100 0.2347 0.2199 -0.0401 -0.0446 0.0130  135 ASP   A CB  
2980 C CB  B ASP   A 135 ? 0.2159 0.2304 0.2518 -0.0391 -0.0465 0.0135  135 ASP   A CB  
2981 C CG  A ASP   A 135 ? 0.2193 0.2677 0.2707 -0.0482 -0.0548 0.0113  135 ASP   A CG  
2982 C CG  B ASP   A 135 ? 0.2324 0.2559 0.3092 -0.0462 -0.0441 0.0018  135 ASP   A CG  
2983 O OD1 A ASP   A 135 ? 0.2209 0.2842 0.2736 -0.0426 -0.0559 0.0319  135 ASP   A OD1 
2984 O OD1 B ASP   A 135 ? 0.2329 0.2781 0.3167 -0.0514 -0.0352 0.0109  135 ASP   A OD1 
2985 O OD2 A ASP   A 135 ? 0.2243 0.2805 0.3173 -0.0562 -0.0500 0.0127  135 ASP   A OD2 
2986 O OD2 B ASP   A 135 ? 0.2540 0.2711 0.3595 -0.0399 -0.0259 0.0032  135 ASP   A OD2 
2995 N N   A PRO   A 136 ? 0.1772 0.1877 0.1972 0.0026  -0.0004 0.0084  136 PRO   A N   
2996 N N   B PRO   A 136 ? 0.1736 0.1861 0.2114 -0.0068 -0.0072 0.0359  136 PRO   A N   
2997 C CA  A PRO   A 136 ? 0.1752 0.1895 0.2080 -0.0055 0.0084  -0.0046 136 PRO   A CA  
2998 C CA  B PRO   A 136 ? 0.1709 0.1857 0.2210 -0.0141 -0.0003 0.0287  136 PRO   A CA  
2999 C C   A PRO   A 136 ? 0.1601 0.1843 0.2036 -0.0026 0.0095  -0.0012 136 PRO   A C   
3000 C C   B PRO   A 136 ? 0.1523 0.1850 0.2163 -0.0097 -0.0066 0.0222  136 PRO   A C   
3001 O O   A PRO   A 136 ? 0.1537 0.1668 0.1707 0.0098  0.0231  0.0014  136 PRO   A O   
3002 O O   B PRO   A 136 ? 0.1502 0.1881 0.2105 -0.0072 -0.0207 0.0252  136 PRO   A O   
3003 C CB  A PRO   A 136 ? 0.1877 0.1927 0.2220 -0.0006 0.0002  -0.0057 136 PRO   A CB  
3004 C CB  B PRO   A 136 ? 0.1849 0.1822 0.2393 -0.0100 0.0043  0.0341  136 PRO   A CB  
3005 C CG  A PRO   A 136 ? 0.2028 0.2032 0.2438 0.0110  -0.0051 0.0032  136 PRO   A CG  
3006 C CG  B PRO   A 136 ? 0.1988 0.1908 0.2535 0.0008  -0.0051 0.0291  136 PRO   A CG  
3007 C CD  A PRO   A 136 ? 0.1911 0.1945 0.2170 0.0139  -0.0045 0.0135  136 PRO   A CD  
3008 C CD  B PRO   A 136 ? 0.1923 0.1909 0.2354 0.0065  -0.0068 0.0432  136 PRO   A CD  
3023 N N   A ILE   A 137 ? 0.1594 0.1894 0.2145 -0.0076 0.0035  0.0112  137 ILE   A N   
3024 N N   B ILE   A 137 ? 0.1441 0.1862 0.2271 -0.0178 -0.0099 0.0385  137 ILE   A N   
3025 C CA  A ILE   A 137 ? 0.1616 0.2005 0.2147 -0.0009 -0.0006 0.0078  137 ILE   A CA  
3026 C CA  B ILE   A 137 ? 0.1502 0.1942 0.2320 -0.0201 -0.0204 0.0378  137 ILE   A CA  
3027 C C   A ILE   A 137 ? 0.1557 0.1980 0.1971 -0.0043 0.0038  0.0106  137 ILE   A C   
3028 C C   B ILE   A 137 ? 0.1564 0.1913 0.2256 -0.0186 -0.0261 0.0392  137 ILE   A C   
3029 O O   A ILE   A 137 ? 0.1569 0.2005 0.1869 -0.0130 0.0044  0.0157  137 ILE   A O   
3030 O O   B ILE   A 137 ? 0.1681 0.1837 0.2359 -0.0228 -0.0240 0.0327  137 ILE   A O   
3031 C CB  A ILE   A 137 ? 0.1697 0.2105 0.2385 -0.0029 -0.0121 0.0070  137 ILE   A CB  
3032 C CB  B ILE   A 137 ? 0.1574 0.2176 0.2534 -0.0169 -0.0274 0.0246  137 ILE   A CB  
3033 C CG1 A ILE   A 137 ? 0.1798 0.2370 0.2597 0.0011  -0.0289 0.0154  137 ILE   A CG1 
3034 C CG1 B ILE   A 137 ? 0.1699 0.2423 0.2778 -0.0116 -0.0280 0.0226  137 ILE   A CG1 
3035 C CG2 A ILE   A 137 ? 0.1793 0.2030 0.2536 -0.0103 -0.0137 -0.0021 137 ILE   A CG2 
3036 C CG2 B ILE   A 137 ? 0.1670 0.2207 0.2749 -0.0316 -0.0308 0.0103  137 ILE   A CG2 
3037 C CD1 A ILE   A 137 ? 0.1955 0.2539 0.2694 0.0041  -0.0296 0.0227  137 ILE   A CD1 
3038 C CD1 B ILE   A 137 ? 0.1892 0.2589 0.2976 -0.0036 -0.0282 0.0226  137 ILE   A CD1 
3061 N N   A HIS   A 138 ? 0.1576 0.2028 0.2069 -0.0050 0.0189  0.0154  138 HIS   A N   
3062 N N   B HIS   A 138 ? 0.1578 0.1987 0.2224 -0.0188 -0.0143 0.0385  138 HIS   A N   
3063 C CA  A HIS   A 138 ? 0.1611 0.2023 0.2046 -0.0037 0.0199  0.0105  138 HIS   A CA  
3064 C CA  B HIS   A 138 ? 0.1603 0.2066 0.2197 -0.0204 -0.0112 0.0306  138 HIS   A CA  
3065 C C   A HIS   A 138 ? 0.1565 0.1895 0.2147 0.0032  0.0101  0.0199  138 HIS   A C   
3066 C C   B HIS   A 138 ? 0.1506 0.1972 0.2215 -0.0066 -0.0102 0.0286  138 HIS   A C   
3067 O O   A HIS   A 138 ? 0.1697 0.1869 0.2187 -0.0002 0.0161  0.0210  138 HIS   A O   
3068 O O   B HIS   A 138 ? 0.1581 0.2034 0.2200 -0.0112 -0.0054 0.0306  138 HIS   A O   
3069 C CB  A HIS   A 138 ? 0.1673 0.2199 0.2121 -0.0064 0.0191  -0.0038 138 HIS   A CB  
3070 C CB  B HIS   A 138 ? 0.1828 0.2283 0.2250 -0.0259 -0.0275 0.0205  138 HIS   A CB  
3071 C CG  A HIS   A 138 ? 0.1789 0.2316 0.2214 -0.0083 0.0131  -0.0193 138 HIS   A CG  
3072 C CG  B HIS   A 138 ? 0.2008 0.2472 0.2332 -0.0269 -0.0258 0.0129  138 HIS   A CG  
3073 N ND1 A HIS   A 138 ? 0.1886 0.2386 0.2422 -0.0114 0.0099  -0.0278 138 HIS   A ND1 
3074 N ND1 B HIS   A 138 ? 0.2097 0.2593 0.2542 -0.0299 -0.0201 0.0060  138 HIS   A ND1 
3075 C CD2 A HIS   A 138 ? 0.1803 0.2394 0.2262 -0.0023 0.0159  -0.0163 138 HIS   A CD2 
3076 C CD2 B HIS   A 138 ? 0.2053 0.2582 0.2335 -0.0229 -0.0238 0.0140  138 HIS   A CD2 
3077 C CE1 A HIS   A 138 ? 0.1898 0.2403 0.2413 -0.0004 0.0106  -0.0272 138 HIS   A CE1 
3078 C CE1 B HIS   A 138 ? 0.2142 0.2662 0.2569 -0.0225 -0.0195 0.0102  138 HIS   A CE1 
3079 N NE2 A HIS   A 138 ? 0.1860 0.2423 0.2245 0.0022  0.0165  -0.0212 138 HIS   A NE2 
3080 N NE2 B HIS   A 138 ? 0.2096 0.2669 0.2361 -0.0196 -0.0189 0.0140  138 HIS   A NE2 
3095 N N   . SER   A 139 ? 0.1468 0.1846 0.2218 -0.0013 -0.0060 0.0327  139 SER   A N   
3096 C CA  . SER   A 139 ? 0.1406 0.1810 0.2175 -0.0053 0.0017  0.0379  139 SER   A CA  
3097 C C   . SER   A 139 ? 0.1376 0.1771 0.2172 -0.0111 0.0079  0.0327  139 SER   A C   
3098 O O   . SER   A 139 ? 0.1350 0.1732 0.2387 -0.0106 -0.0037 0.0416  139 SER   A O   
3099 C CB  . SER   A 139 ? 0.1406 0.1875 0.2093 -0.0080 -0.0042 0.0387  139 SER   A CB  
3100 O OG  . SER   A 139 ? 0.1552 0.1842 0.2244 -0.0190 -0.0099 0.0501  139 SER   A OG  
3107 N N   . LEU   A 140 ? 0.1356 0.1777 0.2041 -0.0087 0.0041  0.0417  140 LEU   A N   
3108 C CA  . LEU   A 140 ? 0.1425 0.1764 0.2250 -0.0151 0.0012  0.0309  140 LEU   A CA  
3109 C C   . LEU   A 140 ? 0.1379 0.1835 0.2314 -0.0138 -0.0045 0.0419  140 LEU   A C   
3110 O O   . LEU   A 140 ? 0.1449 0.1817 0.2587 -0.0109 -0.0065 0.0473  140 LEU   A O   
3111 C CB  . LEU   A 140 ? 0.1428 0.1876 0.2310 -0.0130 0.0092  0.0356  140 LEU   A CB  
3112 C CG  . LEU   A 140 ? 0.1465 0.2030 0.2439 -0.0253 0.0050  0.0441  140 LEU   A CG  
3113 C CD1 . LEU   A 140 ? 0.1490 0.2065 0.2436 -0.0272 0.0014  0.0516  140 LEU   A CD1 
3114 C CD2 . LEU   A 140 ? 0.1484 0.2268 0.2391 -0.0168 0.0070  0.0564  140 LEU   A CD2 
3126 N N   . ARG   A 141 ? 0.1486 0.1842 0.2481 -0.0157 -0.0144 0.0410  141 ARG   A N   
3127 C CA  . ARG   A 141 ? 0.1591 0.1938 0.2573 -0.0222 -0.0129 0.0311  141 ARG   A CA  
3128 C C   . ARG   A 141 ? 0.1620 0.1789 0.2498 -0.0155 -0.0188 0.0277  141 ARG   A C   
3129 O O   . ARG   A 141 ? 0.1609 0.1718 0.2665 -0.0184 -0.0078 0.0269  141 ARG   A O   
3130 C CB  . ARG   A 141 ? 0.1764 0.2160 0.2701 -0.0301 -0.0176 0.0227  141 ARG   A CB  
3131 C CG  . ARG   A 141 ? 0.2085 0.2426 0.2972 -0.0316 -0.0016 0.0147  141 ARG   A CG  
3132 C CD  . ARG   A 141 ? 0.2432 0.2571 0.3342 -0.0344 -0.0057 0.0051  141 ARG   A CD  
3133 N NE  . ARG   A 141 ? 0.2373 0.2730 0.3660 -0.0316 -0.0169 0.0189  141 ARG   A NE  
3134 C CZ  . ARG   A 141 ? 0.2423 0.2909 0.3567 -0.0480 -0.0148 0.0302  141 ARG   A CZ  
3135 N NH1 . ARG   A 141 ? 0.2340 0.2969 0.3328 -0.0562 0.0094  0.0232  141 ARG   A NH1 
3136 N NH2 . ARG   A 141 ? 0.2516 0.2972 0.3773 -0.0482 -0.0332 0.0397  141 ARG   A NH2 
3150 N N   . VAL   A 142 ? 0.1489 0.1772 0.2357 -0.0173 -0.0079 0.0270  142 VAL   A N   
3151 C CA  . VAL   A 142 ? 0.1513 0.1686 0.2398 -0.0118 0.0083  0.0229  142 VAL   A CA  
3152 C C   . VAL   A 142 ? 0.1381 0.1636 0.2426 -0.0124 0.0066  0.0214  142 VAL   A C   
3153 O O   . VAL   A 142 ? 0.1506 0.1643 0.2582 0.0004  0.0042  0.0232  142 VAL   A O   
3154 C CB  . VAL   A 142 ? 0.1568 0.1837 0.2359 -0.0032 0.0064  0.0335  142 VAL   A CB  
3155 C CG1 . VAL   A 142 ? 0.1610 0.1854 0.2375 -0.0088 0.0083  0.0174  142 VAL   A CG1 
3156 C CG2 . VAL   A 142 ? 0.1718 0.2001 0.2543 0.0062  0.0145  0.0357  142 VAL   A CG2 
3166 N N   . CYS   A 143 ? 0.1399 0.1608 0.2297 -0.0143 0.0005  0.0286  143 CYS   A N   
3167 C CA  . CYS   A 143 ? 0.1424 0.1658 0.2277 -0.0159 0.0014  0.0278  143 CYS   A CA  
3168 C C   . CYS   A 143 ? 0.1438 0.1662 0.2649 -0.0110 0.0011  0.0467  143 CYS   A C   
3169 O O   . CYS   A 143 ? 0.1391 0.1697 0.2617 -0.0089 -0.0010 0.0426  143 CYS   A O   
3170 C CB  . CYS   A 143 ? 0.1613 0.1666 0.2223 -0.0122 0.0101  0.0337  143 CYS   A CB  
3171 S SG  . CYS   A 143 ? 0.1766 0.1824 0.2270 -0.0029 0.0072  0.0324  143 CYS   A SG  
3177 N N   . VAL   A 144 ? 0.1364 0.1773 0.2834 -0.0180 0.0002  0.0595  144 VAL   A N   
3178 C CA  . VAL   A 144 ? 0.1543 0.1810 0.3158 -0.0184 0.0143  0.0700  144 VAL   A CA  
3179 C C   . VAL   A 144 ? 0.1625 0.1739 0.3244 -0.0195 -0.0218 0.0591  144 VAL   A C   
3180 O O   . VAL   A 144 ? 0.1830 0.1780 0.3246 -0.0180 -0.0192 0.0584  144 VAL   A O   
3181 C CB  . VAL   A 144 ? 0.1901 0.2154 0.3762 -0.0025 0.0419  0.0846  144 VAL   A CB  
3182 C CG1 . VAL   A 144 ? 0.2231 0.2508 0.4415 -0.0112 0.0221  0.0735  144 VAL   A CG1 
3183 C CG2 . VAL   A 144 ? 0.1626 0.2274 0.3671 -0.0025 0.0463  0.0809  144 VAL   A CG2 
3193 N N   . ASP   A 145 ? 0.1622 0.1668 0.3369 -0.0249 -0.0316 0.0428  145 ASP   A N   
3194 C CA  . ASP   A 145 ? 0.1786 0.1807 0.3365 -0.0268 -0.0314 0.0388  145 ASP   A CA  
3195 C C   . ASP   A 145 ? 0.1764 0.1673 0.3350 -0.0100 -0.0318 0.0289  145 ASP   A C   
3196 O O   . ASP   A 145 ? 0.1969 0.1790 0.3722 -0.0115 -0.0260 -0.0063 145 ASP   A O   
3197 C CB  . ASP   A 145 ? 0.2070 0.2056 0.3622 -0.0344 -0.0502 0.0384  145 ASP   A CB  
3198 C CG  . ASP   A 145 ? 0.2336 0.2434 0.3927 -0.0529 -0.0666 0.0408  145 ASP   A CG  
3199 O OD1 . ASP   A 145 ? 0.2239 0.2625 0.3941 -0.0663 -0.0576 0.0455  145 ASP   A OD1 
3200 O OD2 . ASP   A 145 ? 0.2535 0.2630 0.4080 -0.0641 -0.0893 0.0274  145 ASP   A OD2 
3205 N N   . THR   A 146 ? 0.1560 0.1547 0.2913 -0.0174 -0.0132 0.0190  146 THR   A N   
3206 C CA  . THR   A 146 ? 0.1547 0.1548 0.2793 -0.0035 -0.0011 0.0252  146 THR   A CA  
3207 C C   . THR   A 146 ? 0.1496 0.1558 0.2717 -0.0012 0.0074  0.0307  146 THR   A C   
3208 O O   . THR   A 146 ? 0.1627 0.1662 0.2807 0.0073  -0.0118 0.0328  146 THR   A O   
3209 C CB  . THR   A 146 ? 0.1520 0.1593 0.2859 -0.0014 0.0003  0.0187  146 THR   A CB  
3210 O OG1 . THR   A 146 ? 0.1589 0.1756 0.2866 -0.0023 0.0027  0.0080  146 THR   A OG1 
3211 C CG2 . THR   A 146 ? 0.1529 0.1612 0.2973 -0.0032 -0.0028 0.0268  146 THR   A CG2 
3219 N N   . VAL   A 147 ? 0.1358 0.1643 0.2646 -0.0051 -0.0004 0.0280  147 VAL   A N   
3220 C CA  . VAL   A 147 ? 0.1411 0.1642 0.2709 -0.0159 0.0203  0.0386  147 VAL   A CA  
3221 C C   . VAL   A 147 ? 0.1424 0.1576 0.2821 -0.0156 0.0096  0.0438  147 VAL   A C   
3222 O O   . VAL   A 147 ? 0.1463 0.1760 0.3004 -0.0205 -0.0026 0.0450  147 VAL   A O   
3223 C CB  . VAL   A 147 ? 0.1573 0.1622 0.2557 -0.0149 0.0204  0.0428  147 VAL   A CB  
3224 C CG1 . VAL   A 147 ? 0.1919 0.1806 0.2528 -0.0079 0.0232  0.0469  147 VAL   A CG1 
3225 C CG2 . VAL   A 147 ? 0.1740 0.1602 0.2661 -0.0193 0.0137  0.0273  147 VAL   A CG2 
3235 N N   . ARG   A 148 ? 0.1450 0.1588 0.2832 -0.0191 0.0109  0.0554  148 ARG   A N   
3236 C CA  . ARG   A 148 ? 0.1527 0.1671 0.2887 -0.0176 0.0069  0.0596  148 ARG   A CA  
3237 C C   . ARG   A 148 ? 0.1637 0.1730 0.2891 -0.0209 0.0047  0.0804  148 ARG   A C   
3238 O O   . ARG   A 148 ? 0.2053 0.1914 0.3015 -0.0252 0.0140  0.0790  148 ARG   A O   
3239 C CB  . ARG   A 148 ? 0.1583 0.1706 0.3131 -0.0134 0.0155  0.0606  148 ARG   A CB  
3240 C CG  . ARG   A 148 ? 0.1713 0.1729 0.3436 -0.0139 0.0268  0.0445  148 ARG   A CG  
3241 C CD  . ARG   A 148 ? 0.1944 0.1680 0.3540 -0.0084 0.0449  0.0599  148 ARG   A CD  
3242 N NE  . ARG   A 148 ? 0.1894 0.1668 0.3600 0.0103  0.0505  0.0628  148 ARG   A NE  
3243 C CZ  . ARG   A 148 ? 0.1923 0.1620 0.3485 0.0033  0.0440  0.0572  148 ARG   A CZ  
3244 N NH1 . ARG   A 148 ? 0.2053 0.1559 0.3486 -0.0149 0.0426  0.0189  148 ARG   A NH1 
3245 N NH2 . ARG   A 148 ? 0.1827 0.1810 0.3393 0.0101  0.0390  0.0667  148 ARG   A NH2 
3259 N N   . THR   A 149 ? 0.1647 0.1802 0.2893 -0.0200 -0.0006 0.0710  149 THR   A N   
3260 C CA  . THR   A 149 ? 0.1659 0.1847 0.2757 -0.0163 -0.0102 0.0708  149 THR   A CA  
3261 C C   . THR   A 149 ? 0.1571 0.1824 0.2579 -0.0194 -0.0037 0.0657  149 THR   A C   
3262 O O   . THR   A 149 ? 0.1580 0.1958 0.2741 -0.0203 -0.0044 0.0641  149 THR   A O   
3263 C CB  . THR   A 149 ? 0.1630 0.1964 0.2910 -0.0220 -0.0092 0.0595  149 THR   A CB  
3264 O OG1 . THR   A 149 ? 0.1652 0.1842 0.2846 -0.0273 -0.0030 0.0630  149 THR   A OG1 
3265 C CG2 . THR   A 149 ? 0.1637 0.2007 0.2758 -0.0134 -0.0164 0.0416  149 THR   A CG2 
3273 N N   . ASN   A 150 ? 0.1572 0.1993 0.2480 -0.0146 -0.0100 0.0767  150 ASN   A N   
3274 C CA  . ASN   A 150 ? 0.1772 0.2064 0.2609 -0.0214 -0.0077 0.0745  150 ASN   A CA  
3275 C C   . ASN   A 150 ? 0.1670 0.1981 0.2497 -0.0253 -0.0027 0.0785  150 ASN   A C   
3276 O O   . ASN   A 150 ? 0.1749 0.2110 0.2805 -0.0255 -0.0184 0.0748  150 ASN   A O   
3277 C CB  . ASN   A 150 ? 0.2286 0.2443 0.2924 -0.0201 0.0077  0.0912  150 ASN   A CB  
3278 C CG  . ASN   A 150 ? 0.2898 0.2790 0.3559 -0.0143 0.0057  0.0885  150 ASN   A CG  
3279 O OD1 . ASN   A 150 ? 0.3153 0.2731 0.3796 -0.0249 0.0246  0.1155  150 ASN   A OD1 
3280 N ND2 . ASN   A 150 ? 0.3235 0.3090 0.3847 -0.0012 -0.0043 0.0755  150 ASN   A ND2 
3287 N N   . VAL   A 151 ? 0.1717 0.1802 0.2427 -0.0238 -0.0128 0.0609  151 VAL   A N   
3288 C CA  . VAL   A 151 ? 0.1880 0.1733 0.2368 -0.0226 -0.0023 0.0620  151 VAL   A CA  
3289 C C   . VAL   A 151 ? 0.1619 0.1745 0.2442 -0.0280 -0.0036 0.0614  151 VAL   A C   
3290 O O   . VAL   A 151 ? 0.1694 0.1910 0.2963 -0.0309 -0.0074 0.0704  151 VAL   A O   
3291 C CB  . VAL   A 151 ? 0.2443 0.2034 0.2381 -0.0145 -0.0037 0.0548  151 VAL   A CB  
3292 C CG1 . VAL   A 151 ? 0.2396 0.2383 0.2820 -0.0179 -0.0045 0.0421  151 VAL   A CG1 
3293 C CG2 . VAL   A 151 ? 0.2685 0.1895 0.2312 -0.0053 0.0039  0.0546  151 VAL   A CG2 
3303 N N   . TYR   A 152 ? 0.1558 0.1851 0.2410 -0.0288 0.0008  0.0560  152 TYR   A N   
3304 C CA  . TYR   A 152 ? 0.1564 0.2003 0.2124 -0.0355 -0.0090 0.0552  152 TYR   A CA  
3305 C C   . TYR   A 152 ? 0.1515 0.1873 0.1967 -0.0285 0.0045  0.0523  152 TYR   A C   
3306 O O   . TYR   A 152 ? 0.1634 0.1784 0.2108 -0.0289 0.0019  0.0424  152 TYR   A O   
3307 C CB  . TYR   A 152 ? 0.1763 0.2272 0.2182 -0.0351 0.0035  0.0749  152 TYR   A CB  
3308 C CG  . TYR   A 152 ? 0.1842 0.2536 0.2166 -0.0384 0.0054  0.0905  152 TYR   A CG  
3309 C CD1 . TYR   A 152 ? 0.2029 0.2760 0.2456 -0.0306 0.0066  0.0934  152 TYR   A CD1 
3310 C CD2 . TYR   A 152 ? 0.1981 0.2703 0.2186 -0.0462 0.0031  0.0846  152 TYR   A CD2 
3311 C CE1 . TYR   A 152 ? 0.2350 0.2955 0.2607 -0.0209 0.0025  0.1043  152 TYR   A CE1 
3312 C CE2 . TYR   A 152 ? 0.2288 0.2878 0.2424 -0.0445 0.0060  0.0951  152 TYR   A CE2 
3313 C CZ  . TYR   A 152 ? 0.2520 0.2970 0.2556 -0.0326 0.0075  0.1235  152 TYR   A CZ  
3314 O OH  . TYR   A 152 ? 0.2912 0.3248 0.3074 -0.0241 0.0128  0.1463  152 TYR   A OH  
3324 N N   . LEU   A 153 ? 0.1445 0.1805 0.1923 -0.0297 0.0007  0.0519  153 LEU   A N   
3325 C CA  . LEU   A 153 ? 0.1413 0.1749 0.2062 -0.0240 0.0084  0.0413  153 LEU   A CA  
3326 C C   . LEU   A 153 ? 0.1386 0.1790 0.2216 -0.0144 0.0130  0.0499  153 LEU   A C   
3327 O O   . LEU   A 153 ? 0.1526 0.1919 0.2423 -0.0154 0.0322  0.0512  153 LEU   A O   
3328 C CB  . LEU   A 153 ? 0.1363 0.1814 0.2180 -0.0157 -0.0007 0.0498  153 LEU   A CB  
3329 C CG  . LEU   A 153 ? 0.1481 0.1839 0.2167 -0.0180 0.0086  0.0412  153 LEU   A CG  
3330 C CD1 . LEU   A 153 ? 0.1677 0.1841 0.2181 -0.0174 -0.0084 0.0485  153 LEU   A CD1 
3331 C CD2 . LEU   A 153 ? 0.1641 0.1815 0.2385 -0.0178 0.0083  0.0256  153 LEU   A CD2 
3343 N N   . ALA   A 154 ? 0.1474 0.1712 0.2160 -0.0086 0.0234  0.0449  154 ALA   A N   
3344 C CA  . ALA   A 154 ? 0.1632 0.1710 0.2165 -0.0029 0.0244  0.0405  154 ALA   A CA  
3345 C C   . ALA   A 154 ? 0.1526 0.1770 0.2187 -0.0023 0.0216  0.0404  154 ALA   A C   
3346 O O   . ALA   A 154 ? 0.1557 0.2021 0.2252 0.0004  0.0221  0.0598  154 ALA   A O   
3347 C CB  . ALA   A 154 ? 0.1840 0.1850 0.2311 -0.0071 0.0174  0.0213  154 ALA   A CB  
3353 N N   A VAL   A 155 ? 0.1514 0.1785 0.2208 -0.0017 0.0264  0.0445  155 VAL   A N   
3354 N N   B VAL   A 155 ? 0.1617 0.1861 0.2239 0.0098  0.0233  0.0415  155 VAL   A N   
3355 C CA  A VAL   A 155 ? 0.1541 0.1801 0.2316 -0.0071 0.0287  0.0456  155 VAL   A CA  
3356 C CA  B VAL   A 155 ? 0.1741 0.1955 0.2373 0.0166  0.0207  0.0393  155 VAL   A CA  
3357 C C   A VAL   A 155 ? 0.1603 0.1838 0.2370 -0.0028 0.0323  0.0465  155 VAL   A C   
3358 C C   B VAL   A 155 ? 0.1833 0.2091 0.2471 0.0341  0.0215  0.0316  155 VAL   A C   
3359 O O   A VAL   A 155 ? 0.1657 0.2007 0.2391 0.0014  0.0401  0.0427  155 VAL   A O   
3360 O O   B VAL   A 155 ? 0.1849 0.2204 0.2522 0.0391  0.0229  0.0267  155 VAL   A O   
3361 C CB  A VAL   A 155 ? 0.1546 0.1871 0.2369 -0.0147 0.0052  0.0430  155 VAL   A CB  
3362 C CB  B VAL   A 155 ? 0.1793 0.2001 0.2405 0.0064  -0.0046 0.0409  155 VAL   A CB  
3363 C CG1 A VAL   A 155 ? 0.1667 0.2039 0.2480 -0.0091 -0.0016 0.0439  155 VAL   A CG1 
3364 C CG1 B VAL   A 155 ? 0.1894 0.2144 0.2500 -0.0000 -0.0101 0.0376  155 VAL   A CG1 
3365 C CG2 A VAL   A 155 ? 0.1736 0.1932 0.2591 -0.0136 -0.0097 0.0374  155 VAL   A CG2 
3366 C CG2 B VAL   A 155 ? 0.1957 0.2019 0.2589 0.0062  -0.0188 0.0389  155 VAL   A CG2 
3385 N N   A PHE   A 156 ? 0.1708 0.1751 0.2461 0.0029  0.0289  0.0552  156 PHE   A N   
3386 N N   B PHE   A 156 ? 0.1967 0.2135 0.2575 0.0491  0.0179  0.0276  156 PHE   A N   
3387 C CA  A PHE   A 156 ? 0.1819 0.1779 0.2653 0.0041  0.0250  0.0688  156 PHE   A CA  
3388 C CA  B PHE   A 156 ? 0.2143 0.2311 0.2836 0.0519  0.0096  0.0307  156 PHE   A CA  
3389 C C   A PHE   A 156 ? 0.1834 0.1905 0.2712 0.0090  0.0358  0.0704  156 PHE   A C   
3390 C C   B PHE   A 156 ? 0.2214 0.2454 0.2941 0.0589  0.0230  0.0433  156 PHE   A C   
3391 O O   A PHE   A 156 ? 0.1929 0.1979 0.2870 0.0035  0.0390  0.0453  156 PHE   A O   
3392 O O   B PHE   A 156 ? 0.2279 0.2545 0.3074 0.0595  0.0285  0.0303  156 PHE   A O   
3393 C CB  A PHE   A 156 ? 0.1944 0.1799 0.2682 -0.0060 0.0176  0.0920  156 PHE   A CB  
3394 C CB  B PHE   A 156 ? 0.2330 0.2440 0.2987 0.0398  -0.0081 0.0295  156 PHE   A CB  
3395 C CG  A PHE   A 156 ? 0.2182 0.1864 0.2811 0.0123  -0.0030 0.0896  156 PHE   A CG  
3396 C CG  B PHE   A 156 ? 0.2569 0.2548 0.3156 0.0401  -0.0314 0.0200  156 PHE   A CG  
3397 C CD1 A PHE   A 156 ? 0.2313 0.1951 0.3039 0.0221  -0.0088 0.0812  156 PHE   A CD1 
3398 C CD1 B PHE   A 156 ? 0.2675 0.2588 0.3308 0.0378  -0.0433 0.0161  156 PHE   A CD1 
3399 C CD2 A PHE   A 156 ? 0.2270 0.1892 0.2875 0.0128  -0.0014 0.0882  156 PHE   A CD2 
3400 C CD2 B PHE   A 156 ? 0.2678 0.2620 0.3276 0.0387  -0.0346 0.0159  156 PHE   A CD2 
3401 C CE1 A PHE   A 156 ? 0.2452 0.2030 0.3307 0.0272  -0.0098 0.0708  156 PHE   A CE1 
3402 C CE1 B PHE   A 156 ? 0.2718 0.2616 0.3412 0.0342  -0.0521 0.0125  156 PHE   A CE1 
3403 C CE2 A PHE   A 156 ? 0.2416 0.1977 0.2989 0.0225  0.0005  0.0893  156 PHE   A CE2 
3404 C CE2 B PHE   A 156 ? 0.2732 0.2637 0.3378 0.0416  -0.0450 0.0141  156 PHE   A CE2 
3405 C CZ  A PHE   A 156 ? 0.2490 0.2022 0.3268 0.0264  -0.0049 0.0729  156 PHE   A CZ  
3406 C CZ  B PHE   A 156 ? 0.2759 0.2626 0.3456 0.0389  -0.0484 0.0113  156 PHE   A CZ  
3425 N N   A ASP   A 157 ? 0.1737 0.1997 0.2552 0.0138  0.0243  0.0791  157 ASP   A N   
3426 N N   B ASP   A 157 ? 0.2217 0.2501 0.2832 0.0601  0.0101  0.0589  157 ASP   A N   
3427 C CA  A ASP   A 157 ? 0.1779 0.2212 0.2663 0.0173  0.0239  0.0867  157 ASP   A CA  
3428 C CA  B ASP   A 157 ? 0.2351 0.2665 0.2902 0.0578  0.0085  0.0691  157 ASP   A CA  
3429 C C   A ASP   A 157 ? 0.1512 0.2452 0.2890 0.0321  0.0314  0.0880  157 ASP   A C   
3430 C C   B ASP   A 157 ? 0.2280 0.2706 0.2971 0.0576  0.0062  0.0695  157 ASP   A C   
3431 O O   A ASP   A 157 ? 0.1369 0.2471 0.2874 0.0279  0.0358  0.0805  157 ASP   A O   
3432 O O   B ASP   A 157 ? 0.2301 0.2623 0.2993 0.0457  0.0046  0.0693  157 ASP   A O   
3433 C CB  A ASP   A 157 ? 0.2015 0.2169 0.2789 0.0139  0.0092  0.0791  157 ASP   A CB  
3434 C CB  B ASP   A 157 ? 0.2498 0.2784 0.2970 0.0614  0.0116  0.0775  157 ASP   A CB  
3435 C CG  A ASP   A 157 ? 0.2276 0.2057 0.3048 0.0112  -0.0079 0.0755  157 ASP   A CG  
3436 C CG  B ASP   A 157 ? 0.2661 0.2840 0.3137 0.0666  0.0114  0.0888  157 ASP   A CG  
3437 O OD1 A ASP   A 157 ? 0.2179 0.1822 0.3225 0.0078  -0.0088 0.0579  157 ASP   A OD1 
3438 O OD1 B ASP   A 157 ? 0.2923 0.2949 0.3429 0.0577  -0.0105 0.0908  157 ASP   A OD1 
3439 O OD2 A ASP   A 157 ? 0.2548 0.2228 0.3263 0.0062  -0.0259 0.0791  157 ASP   A OD2 
3440 O OD2 B ASP   A 157 ? 0.2538 0.2806 0.3098 0.0680  0.0243  0.0965  157 ASP   A OD2 
3449 N N   A LYS   A 158 ? 0.1600 0.2627 0.3058 0.0294  0.0509  0.0903  158 LYS   A N   
3450 N N   B LYS   A 158 ? 0.2353 0.2865 0.3078 0.0534  0.0148  0.0654  158 LYS   A N   
3451 C CA  A LYS   A 158 ? 0.1619 0.2824 0.3200 0.0343  0.0531  0.0851  158 LYS   A CA  
3452 C CA  B LYS   A 158 ? 0.2422 0.3109 0.3289 0.0453  0.0135  0.0591  158 LYS   A CA  
3453 C C   A LYS   A 158 ? 0.1568 0.2898 0.3148 0.0284  0.0416  0.1002  158 LYS   A C   
3454 C C   B LYS   A 158 ? 0.2277 0.3112 0.3285 0.0350  0.0141  0.0641  158 LYS   A C   
3455 O O   A LYS   A 158 ? 0.1512 0.2964 0.3199 0.0125  0.0337  0.0948  158 LYS   A O   
3456 O O   B LYS   A 158 ? 0.2297 0.3126 0.3388 0.0243  0.0206  0.0522  158 LYS   A O   
3457 C CB  A LYS   A 158 ? 0.1746 0.2934 0.3334 0.0388  0.0793  0.0620  158 LYS   A CB  
3458 C CB  B LYS   A 158 ? 0.2715 0.3336 0.3573 0.0388  0.0200  0.0514  158 LYS   A CB  
3459 C CG  A LYS   A 158 ? 0.1872 0.3054 0.3440 0.0450  0.0849  0.0491  158 LYS   A CG  
3460 C CG  B LYS   A 158 ? 0.3002 0.3548 0.3952 0.0307  0.0191  0.0383  158 LYS   A CG  
3461 C CD  A LYS   A 158 ? 0.2134 0.3175 0.3542 0.0458  0.0894  0.0514  158 LYS   A CD  
3462 C CD  B LYS   A 158 ? 0.3192 0.3692 0.4299 0.0307  0.0137  0.0323  158 LYS   A CD  
3463 C CE  A LYS   A 158 ? 0.2329 0.3178 0.3560 0.0462  0.0915  0.0665  158 LYS   A CE  
3464 C CE  B LYS   A 158 ? 0.3308 0.3793 0.4515 0.0327  0.0074  0.0288  158 LYS   A CE  
3465 N NZ  A LYS   A 158 ? 0.2427 0.3139 0.3566 0.0463  0.0925  0.0802  158 LYS   A NZ  
3466 N NZ  B LYS   A 158 ? 0.3397 0.3867 0.4763 0.0313  -0.0013 0.0270  158 LYS   A NZ  
3493 N N   A ASN   A 159 ? 0.1655 0.2925 0.3287 0.0229  0.0337  0.0908  159 ASN   A N   
3494 N N   B ASN   A 159 ? 0.2191 0.3162 0.3379 0.0257  0.0109  0.0707  159 ASN   A N   
3495 C CA  A ASN   A 159 ? 0.1729 0.2918 0.3318 0.0231  0.0116  0.0895  159 ASN   A CA  
3496 C CA  B ASN   A 159 ? 0.2098 0.3188 0.3410 0.0221  0.0006  0.0831  159 ASN   A CA  
3497 C C   A ASN   A 159 ? 0.1694 0.2927 0.3198 0.0113  0.0059  0.0863  159 ASN   A C   
3498 C C   B ASN   A 159 ? 0.1904 0.3074 0.3215 0.0081  0.0013  0.0832  159 ASN   A C   
3499 O O   A ASN   A 159 ? 0.1608 0.2843 0.3062 0.0143  -0.0063 0.0687  159 ASN   A O   
3500 O O   B ASN   A 159 ? 0.1854 0.3027 0.3029 0.0041  -0.0103 0.0635  159 ASN   A O   
3501 C CB  A ASN   A 159 ? 0.1843 0.2902 0.3685 0.0285  -0.0097 0.0872  159 ASN   A CB  
3502 C CB  B ASN   A 159 ? 0.2227 0.3325 0.3819 0.0262  -0.0131 0.0903  159 ASN   A CB  
3503 C CG  A ASN   A 159 ? 0.2047 0.2965 0.4143 0.0327  -0.0139 0.0763  159 ASN   A CG  
3504 C CG  B ASN   A 159 ? 0.2392 0.3477 0.4301 0.0261  -0.0156 0.0825  159 ASN   A CG  
3505 O OD1 A ASN   A 159 ? 0.2090 0.3107 0.4407 0.0339  0.0028  0.0700  159 ASN   A OD1 
3506 O OD1 B ASN   A 159 ? 0.2454 0.3607 0.4577 0.0272  -0.0041 0.0798  159 ASN   A OD1 
3507 N ND2 A ASN   A 159 ? 0.2170 0.2983 0.4360 0.0325  -0.0298 0.0689  159 ASN   A ND2 
3508 N ND2 B ASN   A 159 ? 0.2460 0.3528 0.4495 0.0254  -0.0298 0.0761  159 ASN   A ND2 
3521 N N   . LEU   A 160 ? 0.1700 0.2913 0.3037 0.0055  0.0003  0.0973  160 LEU   A N   
3522 C CA  . LEU   A 160 ? 0.1766 0.2809 0.2837 -0.0055 0.0205  0.0903  160 LEU   A CA  
3523 C C   . LEU   A 160 ? 0.1668 0.2728 0.2652 -0.0129 0.0303  0.0799  160 LEU   A C   
3524 O O   . LEU   A 160 ? 0.1560 0.2803 0.2748 -0.0166 0.0197  0.0868  160 LEU   A O   
3525 C CB  . LEU   A 160 ? 0.1784 0.2737 0.2652 -0.0083 0.0263  0.0955  160 LEU   A CB  
3526 C CG  . LEU   A 160 ? 0.1876 0.2718 0.2862 -0.0223 0.0220  0.0765  160 LEU   A CG  
3527 C CD1 . LEU   A 160 ? 0.2142 0.2707 0.2900 -0.0263 0.0389  0.0601  160 LEU   A CD1 
3528 C CD2 . LEU   A 160 ? 0.1943 0.2673 0.2944 -0.0251 0.0313  0.0830  160 LEU   A CD2 
3541 N N   A TYR   A 161 ? 0.1608 0.2646 0.2468 -0.0140 0.0189  0.0831  161 TYR   A N   
3542 N N   B TYR   A 161 ? 0.1756 0.2536 0.2460 -0.0071 0.0266  0.0811  161 TYR   A N   
3543 C CA  A TYR   A 161 ? 0.1458 0.2615 0.2455 -0.0189 0.0169  0.0732  161 TYR   A CA  
3544 C CA  B TYR   A 161 ? 0.1818 0.2423 0.2407 -0.0106 0.0334  0.0688  161 TYR   A CA  
3545 C C   A TYR   A 161 ? 0.1405 0.2810 0.2491 -0.0182 0.0095  0.0738  161 TYR   A C   
3546 C C   B TYR   A 161 ? 0.1929 0.2569 0.2480 -0.0152 0.0312  0.0671  161 TYR   A C   
3547 O O   A TYR   A 161 ? 0.1354 0.2829 0.2348 -0.0175 0.0169  0.0681  161 TYR   A O   
3548 O O   B TYR   A 161 ? 0.1845 0.2512 0.2319 -0.0165 0.0370  0.0627  161 TYR   A O   
3549 C CB  A TYR   A 161 ? 0.1573 0.2474 0.2439 -0.0146 0.0219  0.0641  161 TYR   A CB  
3550 C CB  B TYR   A 161 ? 0.1945 0.2239 0.2310 0.0008  0.0335  0.0593  161 TYR   A CB  
3551 C CG  A TYR   A 161 ? 0.1487 0.2347 0.2468 -0.0101 0.0160  0.0436  161 TYR   A CG  
3552 C CG  B TYR   A 161 ? 0.1878 0.2003 0.2325 0.0119  0.0286  0.0404  161 TYR   A CG  
3553 C CD1 A TYR   A 161 ? 0.1451 0.2262 0.2515 -0.0024 0.0184  0.0343  161 TYR   A CD1 
3554 C CD1 B TYR   A 161 ? 0.1819 0.1918 0.2394 0.0153  0.0302  0.0281  161 TYR   A CD1 
3555 C CD2 A TYR   A 161 ? 0.1458 0.2319 0.2551 -0.0062 0.0154  0.0365  161 TYR   A CD2 
3556 C CD2 B TYR   A 161 ? 0.1833 0.1852 0.2374 0.0135  0.0272  0.0461  161 TYR   A CD2 
3557 C CE1 A TYR   A 161 ? 0.1434 0.2207 0.2514 -0.0001 0.0032  0.0407  161 TYR   A CE1 
3558 C CE1 B TYR   A 161 ? 0.1784 0.1900 0.2479 0.0203  0.0103  0.0313  161 TYR   A CE1 
3559 C CE2 A TYR   A 161 ? 0.1505 0.2230 0.2424 -0.0031 0.0087  0.0414  161 TYR   A CE2 
3560 C CE2 B TYR   A 161 ? 0.1804 0.1795 0.2306 0.0016  0.0179  0.0511  161 TYR   A CE2 
3561 C CZ  A TYR   A 161 ? 0.1557 0.2153 0.2421 -0.0051 0.0037  0.0385  161 TYR   A CZ  
3562 C CZ  B TYR   A 161 ? 0.1872 0.1840 0.2360 0.0106  0.0050  0.0474  161 TYR   A CZ  
3563 O OH  A TYR   A 161 ? 0.1700 0.2037 0.2417 -0.0061 -0.0017 0.0423  161 TYR   A OH  
3564 O OH  B TYR   A 161 ? 0.1984 0.1849 0.2609 0.0070  -0.0149 0.0587  161 TYR   A OH  
3583 N N   A ASP   A 162 ? 0.1311 0.2949 0.2644 -0.0191 0.0191  0.0815  162 ASP   A N   
3584 N N   B ASP   A 162 ? 0.1995 0.2774 0.2606 -0.0134 0.0422  0.0629  162 ASP   A N   
3585 C CA  A ASP   A 162 ? 0.1267 0.3105 0.2721 -0.0196 0.0318  0.0895  162 ASP   A CA  
3586 C CA  B ASP   A 162 ? 0.2066 0.2973 0.2696 -0.0007 0.0428  0.0640  162 ASP   A CA  
3587 C C   A ASP   A 162 ? 0.1137 0.3118 0.2622 -0.0315 0.0229  0.0988  162 ASP   A C   
3588 C C   B ASP   A 162 ? 0.2117 0.2814 0.2540 -0.0017 0.0336  0.0679  162 ASP   A C   
3589 O O   A ASP   A 162 ? 0.1116 0.3120 0.2796 -0.0387 0.0108  0.0909  162 ASP   A O   
3590 O O   B ASP   A 162 ? 0.2139 0.2786 0.2652 -0.0037 0.0325  0.0664  162 ASP   A O   
3591 C CB  A ASP   A 162 ? 0.1379 0.3282 0.3008 -0.0068 0.0410  0.0720  162 ASP   A CB  
3592 C CB  B ASP   A 162 ? 0.2074 0.3292 0.3073 0.0105  0.0479  0.0560  162 ASP   A CB  
3593 C CG  A ASP   A 162 ? 0.1545 0.3511 0.3363 0.0044  0.0464  0.0537  162 ASP   A CG  
3594 C CG  B ASP   A 162 ? 0.2102 0.3587 0.3458 0.0224  0.0534  0.0480  162 ASP   A CG  
3595 O OD1 A ASP   A 162 ? 0.1569 0.3637 0.3452 0.0069  0.0475  0.0408  162 ASP   A OD1 
3596 O OD1 B ASP   A 162 ? 0.2153 0.3746 0.3635 0.0227  0.0424  0.0418  162 ASP   A OD1 
3597 O OD2 A ASP   A 162 ? 0.1597 0.3557 0.3726 0.0030  0.0543  0.0517  162 ASP   A OD2 
3598 O OD2 B ASP   A 162 ? 0.2085 0.3691 0.3724 0.0234  0.0616  0.0467  162 ASP   A OD2 
3607 N N   A LYS   A 163 ? 0.1241 0.3196 0.2543 -0.0244 -0.0053 0.1037  163 LYS   A N   
3608 N N   B LYS   A 163 ? 0.2263 0.2794 0.2425 0.0104  0.0173  0.0634  163 LYS   A N   
3609 C CA  A LYS   A 163 ? 0.1379 0.3238 0.2638 -0.0262 -0.0118 0.0935  163 LYS   A CA  
3610 C CA  B LYS   A 163 ? 0.2402 0.2779 0.2462 0.0068  0.0209  0.0551  163 LYS   A CA  
3611 C C   A LYS   A 163 ? 0.1344 0.3140 0.2671 -0.0388 -0.0038 0.0787  163 LYS   A C   
3612 C C   B LYS   A 163 ? 0.2296 0.2431 0.2279 0.0001  0.0171  0.0489  163 LYS   A C   
3613 O O   A LYS   A 163 ? 0.1380 0.3156 0.2761 -0.0447 -0.0066 0.0836  163 LYS   A O   
3614 O O   B LYS   A 163 ? 0.2261 0.2270 0.2178 -0.0062 0.0246  0.0167  163 LYS   A O   
3615 C CB  A LYS   A 163 ? 0.1750 0.3405 0.2950 -0.0049 -0.0298 0.0847  163 LYS   A CB  
3616 C CB  B LYS   A 163 ? 0.2734 0.3080 0.2827 0.0108  0.0226  0.0573  163 LYS   A CB  
3617 C CG  A LYS   A 163 ? 0.2239 0.3556 0.3531 0.0043  -0.0307 0.0667  163 LYS   A CG  
3618 C CG  B LYS   A 163 ? 0.3064 0.3367 0.3416 0.0093  0.0277  0.0561  163 LYS   A CG  
3619 C CD  A LYS   A 163 ? 0.2718 0.3700 0.4136 0.0089  -0.0265 0.0501  163 LYS   A CD  
3620 C CD  B LYS   A 163 ? 0.3367 0.3626 0.4094 0.0065  0.0302  0.0505  163 LYS   A CD  
3621 C CE  A LYS   A 163 ? 0.3063 0.3788 0.4582 0.0098  -0.0243 0.0408  163 LYS   A CE  
3622 C CE  B LYS   A 163 ? 0.3605 0.3815 0.4616 0.0005  0.0333  0.0491  163 LYS   A CE  
3623 N NZ  A LYS   A 163 ? 0.3224 0.3858 0.4837 0.0080  -0.0215 0.0404  163 LYS   A NZ  
3624 N NZ  B LYS   A 163 ? 0.3747 0.3907 0.4962 -0.0028 0.0309  0.0451  163 LYS   A NZ  
3651 N N   A LEU   A 164 ? 0.1145 0.2901 0.2488 -0.0391 0.0025  0.0715  164 LEU   A N   
3652 N N   B LEU   A 164 ? 0.2114 0.2265 0.2224 0.0090  0.0008  0.0685  164 LEU   A N   
3653 C CA  A LEU   A 164 ? 0.1252 0.2751 0.2372 -0.0423 0.0215  0.0612  164 LEU   A CA  
3654 C CA  B LEU   A 164 ? 0.2113 0.2294 0.2195 0.0046  0.0032  0.0547  164 LEU   A CA  
3655 C C   A LEU   A 164 ? 0.1407 0.2785 0.2386 -0.0388 0.0272  0.0561  164 LEU   A C   
3656 C C   B LEU   A 164 ? 0.2047 0.2240 0.2233 0.0001  0.0010  0.0537  164 LEU   A C   
3657 O O   A LEU   A 164 ? 0.1435 0.2793 0.2370 -0.0462 0.0304  0.0558  164 LEU   A O   
3658 O O   B LEU   A 164 ? 0.2052 0.2144 0.2478 -0.0108 0.0037  0.0468  164 LEU   A O   
3659 C CB  A LEU   A 164 ? 0.1251 0.2591 0.2263 -0.0404 0.0342  0.0653  164 LEU   A CB  
3660 C CB  B LEU   A 164 ? 0.2067 0.2336 0.2175 0.0080  0.0016  0.0442  164 LEU   A CB  
3661 C CG  A LEU   A 164 ? 0.1290 0.2454 0.2381 -0.0351 0.0298  0.0623  164 LEU   A CG  
3662 C CG  B LEU   A 164 ? 0.2053 0.2346 0.2192 0.0030  0.0066  0.0377  164 LEU   A CG  
3663 C CD1 A LEU   A 164 ? 0.1199 0.2446 0.2520 -0.0274 0.0197  0.0632  164 LEU   A CD1 
3664 C CD1 B LEU   A 164 ? 0.1984 0.2403 0.2238 0.0083  0.0058  0.0382  164 LEU   A CD1 
3665 C CD2 A LEU   A 164 ? 0.1380 0.2461 0.2459 -0.0422 0.0344  0.0580  164 LEU   A CD2 
3666 C CD2 B LEU   A 164 ? 0.2102 0.2376 0.2230 -0.0056 0.0055  0.0391  164 LEU   A CD2 
3689 N N   A VAL   A 165 ? 0.1305 0.2769 0.2258 -0.0396 0.0229  0.0601  165 VAL   A N   
3690 N N   B VAL   A 165 ? 0.1856 0.2307 0.2077 -0.0122 0.0031  0.0603  165 VAL   A N   
3691 C CA  A VAL   A 165 ? 0.1537 0.2786 0.2260 -0.0295 0.0189  0.0637  165 VAL   A CA  
3692 C CA  B VAL   A 165 ? 0.1891 0.2393 0.2067 -0.0141 -0.0004 0.0565  165 VAL   A CA  
3693 C C   A VAL   A 165 ? 0.1556 0.2834 0.2313 -0.0286 0.0261  0.0599  165 VAL   A C   
3694 C C   B VAL   A 165 ? 0.1731 0.2465 0.2073 -0.0216 0.0180  0.0549  165 VAL   A C   
3695 O O   A VAL   A 165 ? 0.1560 0.2807 0.2404 -0.0359 0.0295  0.0570  165 VAL   A O   
3696 O O   B VAL   A 165 ? 0.1723 0.2469 0.2215 -0.0177 0.0227  0.0384  165 VAL   A O   
3697 C CB  A VAL   A 165 ? 0.1666 0.2774 0.2214 -0.0292 0.0235  0.0706  165 VAL   A CB  
3698 C CB  B VAL   A 165 ? 0.2068 0.2439 0.2094 -0.0217 0.0079  0.0560  165 VAL   A CB  
3699 C CG1 A VAL   A 165 ? 0.1788 0.2841 0.2289 -0.0275 0.0287  0.0645  165 VAL   A CG1 
3700 C CG1 B VAL   A 165 ? 0.2190 0.2535 0.2202 -0.0208 0.0157  0.0520  165 VAL   A CG1 
3701 C CG2 A VAL   A 165 ? 0.1725 0.2761 0.2239 -0.0237 0.0069  0.0726  165 VAL   A CG2 
3702 C CG2 B VAL   A 165 ? 0.2163 0.2439 0.2123 -0.0223 -0.0109 0.0493  165 VAL   A CG2 
3721 N N   A SER   A 166 ? 0.1543 0.2897 0.2409 -0.0165 0.0250  0.0507  166 SER   A N   
3722 N N   B SER   A 166 ? 0.1576 0.2586 0.2158 -0.0249 0.0216  0.0506  166 SER   A N   
3723 C CA  A SER   A 166 ? 0.1576 0.2991 0.2385 -0.0108 0.0278  0.0392  166 SER   A CA  
3724 C CA  B SER   A 166 ? 0.1557 0.2709 0.2310 -0.0278 0.0184  0.0463  166 SER   A CA  
3725 C C   A SER   A 166 ? 0.1608 0.3024 0.2488 -0.0034 0.0126  0.0394  166 SER   A C   
3726 C C   B SER   A 166 ? 0.1541 0.2828 0.2337 -0.0189 0.0031  0.0378  166 SER   A C   
3727 O O   A SER   A 166 ? 0.1740 0.3115 0.2762 -0.0019 0.0183  0.0336  166 SER   A O   
3728 O O   B SER   A 166 ? 0.1640 0.2937 0.2592 -0.0198 -0.0045 0.0211  166 SER   A O   
3729 C CB  A SER   A 166 ? 0.1635 0.3093 0.2480 -0.0027 0.0192  0.0179  166 SER   A CB  
3730 C CB  B SER   A 166 ? 0.1642 0.2749 0.2686 -0.0215 0.0020  0.0298  166 SER   A CB  
3731 O OG  A SER   A 166 ? 0.1813 0.3220 0.2560 0.0026  0.0165  0.0086  166 SER   A OG  
3732 O OG  B SER   A 166 ? 0.1806 0.2822 0.2966 -0.0141 -0.0041 0.0262  166 SER   A OG  
3743 N N   A SER   A 167 ? 0.1703 0.3035 0.2437 0.0016  0.0062  0.0463  167 SER   A N   
3744 N N   B SER   A 167 ? 0.1643 0.2896 0.2175 -0.0054 0.0049  0.0448  167 SER   A N   
3745 C CA  A SER   A 167 ? 0.1883 0.3024 0.2435 0.0051  0.0035  0.0431  167 SER   A CA  
3746 C CA  B SER   A 167 ? 0.1854 0.2910 0.2201 0.0095  0.0056  0.0362  167 SER   A CA  
3747 C C   A SER   A 167 ? 0.1953 0.3007 0.2438 0.0094  0.0237  0.0456  167 SER   A C   
3748 C C   B SER   A 167 ? 0.1955 0.2858 0.2224 0.0220  0.0318  0.0367  167 SER   A C   
3749 O O   A SER   A 167 ? 0.2132 0.3000 0.2492 0.0167  0.0056  0.0466  167 SER   A O   
3750 O O   B SER   A 167 ? 0.2178 0.2892 0.2371 0.0248  0.0196  0.0331  167 SER   A O   
3751 C CB  A SER   A 167 ? 0.2033 0.3079 0.2569 0.0097  0.0117  0.0508  167 SER   A CB  
3752 C CB  B SER   A 167 ? 0.1981 0.3006 0.2134 0.0168  0.0155  0.0461  167 SER   A CB  
3753 O OG  A SER   A 167 ? 0.2076 0.3120 0.2821 0.0110  0.0218  0.0567  167 SER   A OG  
3754 O OG  B SER   A 167 ? 0.1974 0.3070 0.2288 0.0193  0.0384  0.0548  167 SER   A OG  
3765 N N   A PHE   A 168 ? 0.1847 0.3020 0.2418 0.0088  0.0320  0.0552  168 PHE   A N   
3766 N N   B PHE   A 168 ? 0.1847 0.2786 0.2214 0.0329  0.0320  0.0524  168 PHE   A N   
3767 C CA  A PHE   A 168 ? 0.1812 0.3101 0.2581 0.0004  0.0379  0.0565  168 PHE   A CA  
3768 C CA  B PHE   A 168 ? 0.1817 0.2818 0.2510 0.0246  0.0375  0.0639  168 PHE   A CA  
3769 C C   A PHE   A 168 ? 0.1993 0.3280 0.2917 -0.0005 0.0613  0.0444  168 PHE   A C   
3770 C C   B PHE   A 168 ? 0.1937 0.2966 0.2741 0.0136  0.0537  0.0549  168 PHE   A C   
3771 O O   A PHE   A 168 ? 0.2089 0.3362 0.3399 -0.0108 0.0753  0.0483  168 PHE   A O   
3772 O O   B PHE   A 168 ? 0.2062 0.2995 0.3232 -0.0033 0.0674  0.0571  168 PHE   A O   
3773 C CB  A PHE   A 168 ? 0.1735 0.3043 0.2455 -0.0066 0.0208  0.0582  168 PHE   A CB  
3774 C CB  B PHE   A 168 ? 0.1797 0.2748 0.2671 0.0283  0.0305  0.0698  168 PHE   A CB  
3775 C CG  A PHE   A 168 ? 0.1625 0.2982 0.2224 -0.0154 0.0001  0.0611  168 PHE   A CG  
3776 C CG  B PHE   A 168 ? 0.1705 0.2655 0.2670 0.0191  0.0272  0.0786  168 PHE   A CG  
3777 C CD1 A PHE   A 168 ? 0.1599 0.2933 0.2214 -0.0244 -0.0055 0.0576  168 PHE   A CD1 
3778 C CD1 B PHE   A 168 ? 0.1706 0.2565 0.2700 0.0147  0.0207  0.0835  168 PHE   A CD1 
3779 C CD2 A PHE   A 168 ? 0.1684 0.3009 0.2222 -0.0173 -0.0003 0.0606  168 PHE   A CD2 
3780 C CD2 B PHE   A 168 ? 0.1677 0.2639 0.2668 0.0028  0.0465  0.0921  168 PHE   A CD2 
3781 C CE1 A PHE   A 168 ? 0.1570 0.2882 0.2141 -0.0257 -0.0089 0.0596  168 PHE   A CE1 
3782 C CE1 B PHE   A 168 ? 0.1734 0.2513 0.2772 0.0088  0.0214  0.0945  168 PHE   A CE1 
3783 C CE2 A PHE   A 168 ? 0.1773 0.2946 0.2317 -0.0182 -0.0029 0.0605  168 PHE   A CE2 
3784 C CE2 B PHE   A 168 ? 0.1773 0.2546 0.2737 0.0017  0.0424  0.1038  168 PHE   A CE2 
3785 C CZ  A PHE   A 168 ? 0.1689 0.2886 0.2272 -0.0206 -0.0072 0.0603  168 PHE   A CZ  
3786 C CZ  B PHE   A 168 ? 0.1726 0.2481 0.2728 0.0024  0.0344  0.1030  168 PHE   A CZ  
3805 N N   A LEU   A 169 ? 0.2380 0.3396 0.3224 -0.0012 0.0655  0.0261  169 LEU   A N   
3806 N N   B LEU   A 169 ? 0.2313 0.3106 0.3038 0.0050  0.0545  0.0423  169 LEU   A N   
3807 C CA  A LEU   A 169 ? 0.2795 0.3573 0.3804 0.0027  0.0446  0.0121  169 LEU   A CA  
3808 C CA  B LEU   A 169 ? 0.2693 0.3313 0.3566 0.0013  0.0342  0.0314  169 LEU   A CA  
3809 C C   A LEU   A 169 ? 0.2869 0.3614 0.4129 0.0017  0.0441  0.0200  169 LEU   A C   
3810 C C   B LEU   A 169 ? 0.2693 0.3270 0.3797 -0.0062 0.0264  0.0533  169 LEU   A C   
3811 O O   A LEU   A 169 ? 0.2923 0.3648 0.4278 0.0092  0.0334  0.0118  169 LEU   A O   
3812 O O   B LEU   A 169 ? 0.2679 0.3297 0.3984 -0.0010 0.0226  0.0543  169 LEU   A O   
3813 C CB  A LEU   A 169 ? 0.3064 0.3703 0.3912 0.0034  0.0287  -0.0089 169 LEU   A CB  
3814 C CB  B LEU   A 169 ? 0.3004 0.3548 0.3710 -0.0015 0.0255  0.0033  169 LEU   A CB  
3815 C CG  A LEU   A 169 ? 0.3281 0.3841 0.4082 -0.0005 0.0117  -0.0299 169 LEU   A CG  
3816 C CG  B LEU   A 169 ? 0.3255 0.3762 0.3904 -0.0082 0.0156  -0.0229 169 LEU   A CG  
3817 C CD1 A LEU   A 169 ? 0.3361 0.3870 0.4136 -0.0049 -0.0001 -0.0352 169 LEU   A CD1 
3818 C CD1 B LEU   A 169 ? 0.3325 0.3806 0.4023 -0.0096 0.0089  -0.0285 169 LEU   A CD1 
3819 C CD2 A LEU   A 169 ? 0.3369 0.3914 0.4111 -0.0016 0.0086  -0.0377 169 LEU   A CD2 
3820 C CD2 B LEU   A 169 ? 0.3359 0.3867 0.3905 -0.0103 0.0158  -0.0317 169 LEU   A CD2 
3821 O OXT A LEU   A 169 ? 0.2843 0.3644 0.4153 -0.0042 0.0555  0.0294  169 LEU   A OXT 
3822 O OXT B LEU   A 169 ? 0.2671 0.3223 0.3702 -0.0134 0.0191  0.0653  169 LEU   A OXT 
3845 N N   A SER   B 1   ? 0.3896 0.3458 0.3520 -0.0658 -0.0965 0.0245  1   SER   B N   
3846 N N   B SER   B 1   ? 0.3539 0.3451 0.3373 -0.0900 -0.0707 0.0295  1   SER   B N   
3847 C CA  A SER   B 1   ? 0.3879 0.3505 0.3640 -0.0725 -0.0955 0.0216  1   SER   B CA  
3848 C CA  B SER   B 1   ? 0.3446 0.3459 0.3352 -0.0971 -0.0711 0.0287  1   SER   B CA  
3849 C C   A SER   B 1   ? 0.3739 0.3549 0.3653 -0.0722 -0.0928 0.0368  1   SER   B C   
3850 C C   B SER   B 1   ? 0.3181 0.3447 0.3092 -0.1006 -0.0804 0.0448  1   SER   B C   
3851 O O   A SER   B 1   ? 0.3830 0.3567 0.3545 -0.0665 -0.0881 0.0381  1   SER   B O   
3852 O O   B SER   B 1   ? 0.3205 0.3443 0.2693 -0.0950 -0.0775 0.0412  1   SER   B O   
3853 C CB  A SER   B 1   ? 0.3960 0.3473 0.3698 -0.0766 -0.0958 0.0034  1   SER   B CB  
3854 C CB  B SER   B 1   ? 0.3571 0.3446 0.3538 -0.0970 -0.0597 0.0071  1   SER   B CB  
3855 O OG  A SER   B 1   ? 0.4088 0.3542 0.4082 -0.0759 -0.0861 -0.0063 1   SER   B OG  
3856 O OG  B SER   B 1   ? 0.3724 0.3566 0.4045 -0.0935 -0.0517 -0.0049 1   SER   B OG  
3871 N N   A MET   B 2   ? 0.3551 0.3554 0.3757 -0.0755 -0.0861 0.0599  2   MET   B N   
3872 N N   B MET   B 2   ? 0.2986 0.3433 0.3232 -0.1039 -0.0767 0.0820  2   MET   B N   
3873 C CA  A MET   B 2   ? 0.3367 0.3562 0.3823 -0.0706 -0.0824 0.0767  2   MET   B CA  
3874 C CA  B MET   B 2   ? 0.2869 0.3482 0.3331 -0.0884 -0.0792 0.1024  2   MET   B CA  
3875 C C   A MET   B 2   ? 0.2965 0.3353 0.3388 -0.0711 -0.0911 0.1014  2   MET   B C   
3876 C C   B MET   B 2   ? 0.2518 0.3338 0.3001 -0.0789 -0.0839 0.1205  2   MET   B C   
3877 O O   A MET   B 2   ? 0.2932 0.3442 0.3385 -0.0656 -0.0975 0.1029  2   MET   B O   
3878 O O   B MET   B 2   ? 0.2454 0.3429 0.3058 -0.0754 -0.0833 0.1171  2   MET   B O   
3879 C CB  A MET   B 2   ? 0.3632 0.3820 0.4543 -0.0548 -0.0624 0.0585  2   MET   B CB  
3880 C CB  B MET   B 2   ? 0.3183 0.3747 0.4011 -0.0654 -0.0709 0.0888  2   MET   B CB  
3881 C CG  A MET   B 2   ? 0.3893 0.4035 0.5204 -0.0387 -0.0413 0.0467  2   MET   B CG  
3882 C CG  B MET   B 2   ? 0.3480 0.3965 0.4547 -0.0422 -0.0574 0.0880  2   MET   B CG  
3883 S SD  A MET   B 2   ? 0.4154 0.4240 0.5895 -0.0244 -0.0249 0.0383  2   MET   B SD  
3884 S SD  B MET   B 2   ? 0.3771 0.4210 0.5098 -0.0200 -0.0501 0.0868  2   MET   B SD  
3885 C CE  A MET   B 2   ? 0.4184 0.4276 0.5844 -0.0241 -0.0233 0.0397  2   MET   B CE  
3886 C CE  B MET   B 2   ? 0.3804 0.4245 0.5019 -0.0192 -0.0512 0.0821  2   MET   B CE  
3905 N N   A VAL   B 3   ? 0.2626 0.3021 0.3085 -0.0815 -0.0882 0.1134  3   VAL   B N   
3906 N N   B VAL   B 3   ? 0.2307 0.3091 0.2814 -0.0798 -0.0781 0.1251  3   VAL   B N   
3907 C CA  A VAL   B 3   ? 0.2441 0.2744 0.2929 -0.0802 -0.0853 0.1031  3   VAL   B CA  
3908 C CA  B VAL   B 3   ? 0.2317 0.2898 0.2789 -0.0662 -0.0673 0.0972  3   VAL   B CA  
3909 C C   A VAL   B 3   ? 0.2194 0.2593 0.2534 -0.0749 -0.0842 0.0985  3   VAL   B C   
3910 C C   B VAL   B 3   ? 0.2220 0.2781 0.2532 -0.0592 -0.0653 0.0926  3   VAL   B C   
3911 O O   A VAL   B 3   ? 0.2062 0.2501 0.2509 -0.0791 -0.0822 0.1130  3   VAL   B O   
3912 O O   B VAL   B 3   ? 0.2231 0.2862 0.2576 -0.0430 -0.0644 0.1020  3   VAL   B O   
3913 C CB  A VAL   B 3   ? 0.2544 0.2649 0.3300 -0.0883 -0.0708 0.0917  3   VAL   B CB  
3914 C CB  B VAL   B 3   ? 0.2473 0.2811 0.3092 -0.0669 -0.0510 0.0808  3   VAL   B CB  
3915 C CG1 A VAL   B 3   ? 0.2612 0.2631 0.3485 -0.0824 -0.0744 0.0875  3   VAL   B CG1 
3916 C CG1 B VAL   B 3   ? 0.2543 0.2778 0.3280 -0.0619 -0.0515 0.0707  3   VAL   B CG1 
3917 C CG2 A VAL   B 3   ? 0.2602 0.2638 0.3417 -0.0888 -0.0518 0.0931  3   VAL   B CG2 
3918 C CG2 B VAL   B 3   ? 0.2548 0.2831 0.3142 -0.0626 -0.0371 0.0847  3   VAL   B CG2 
3937 N N   . ASN   B 4   ? 0.2151 0.2539 0.2407 -0.0688 -0.0679 0.0790  4   ASN   B N   
3938 C CA  . ASN   B 4   ? 0.2143 0.2494 0.2167 -0.0678 -0.0536 0.0449  4   ASN   B CA  
3939 C C   . ASN   B 4   ? 0.2056 0.2602 0.2122 -0.0669 -0.0395 0.0340  4   ASN   B C   
3940 O O   . ASN   B 4   ? 0.2098 0.2667 0.2271 -0.0638 -0.0273 0.0235  4   ASN   B O   
3941 C CB  . ASN   B 4   ? 0.2158 0.2372 0.2151 -0.0591 -0.0630 0.0455  4   ASN   B CB  
3942 C CG  . ASN   B 4   ? 0.2189 0.2221 0.2173 -0.0584 -0.0619 0.0324  4   ASN   B CG  
3943 O OD1 . ASN   B 4   ? 0.2224 0.2046 0.2079 -0.0514 -0.0606 0.0307  4   ASN   B OD1 
3944 N ND2 . ASN   B 4   ? 0.2451 0.2318 0.2244 -0.0425 -0.0449 0.0357  4   ASN   B ND2 
3952 N N   . SER   B 5   ? 0.2200 0.2794 0.2276 -0.0684 -0.0235 0.0328  5   SER   B N   
3953 C CA  . SER   B 5   ? 0.2560 0.3107 0.2434 -0.0564 -0.0022 0.0255  5   SER   B CA  
3954 C C   . SER   B 5   ? 0.2786 0.3152 0.2731 -0.0761 0.0119  0.0235  5   SER   B C   
3955 O O   . SER   B 5   ? 0.2977 0.3050 0.3452 -0.0670 0.0569  0.0274  5   SER   B O   
3956 C CB  . SER   B 5   ? 0.2777 0.3339 0.2699 -0.0373 -0.0036 0.0314  5   SER   B CB  
3957 O OG  . SER   B 5   ? 0.3105 0.3618 0.3266 -0.0235 0.0038  0.0392  5   SER   B OG  
3963 N N   . PHE   B 6   ? 0.3003 0.3381 0.2561 -0.0872 0.0163  0.0308  6   PHE   B N   
3964 C CA  . PHE   B 6   ? 0.3137 0.3458 0.2264 -0.1120 0.0168  0.0076  6   PHE   B CA  
3965 C C   . PHE   B 6   ? 0.3632 0.3815 0.2560 -0.1187 0.0419  -0.0311 6   PHE   B C   
3966 O O   . PHE   B 6   ? 0.3803 0.4196 0.2845 -0.1048 0.0332  -0.0369 6   PHE   B O   
3967 C CB  . PHE   B 6   ? 0.2910 0.3283 0.2000 -0.1058 0.0033  0.0171  6   PHE   B CB  
3968 C CG  . PHE   B 6   ? 0.2610 0.2931 0.1903 -0.1074 -0.0124 0.0133  6   PHE   B CG  
3969 C CD1 . PHE   B 6   ? 0.2640 0.2622 0.1861 -0.1018 -0.0225 0.0150  6   PHE   B CD1 
3970 C CD2 . PHE   B 6   ? 0.2428 0.2939 0.1865 -0.0871 -0.0091 0.0385  6   PHE   B CD2 
3971 C CE1 . PHE   B 6   ? 0.2603 0.2492 0.1896 -0.0887 -0.0306 0.0163  6   PHE   B CE1 
3972 C CE2 . PHE   B 6   ? 0.2439 0.2863 0.2153 -0.0811 -0.0078 0.0332  6   PHE   B CE2 
3973 C CZ  . PHE   B 6   ? 0.2469 0.2587 0.2057 -0.0867 -0.0263 0.0158  6   PHE   B CZ  
3983 N N   . SER   B 7   ? 0.3975 0.3638 0.2734 -0.1452 0.0651  -0.0758 7   SER   B N   
3984 C CA  . SER   B 7   ? 0.4328 0.3802 0.3259 -0.1418 0.0863  -0.0930 7   SER   B CA  
3985 C C   . SER   B 7   ? 0.4314 0.3636 0.3196 -0.1469 0.1099  -0.0944 7   SER   B C   
3986 O O   . SER   B 7   ? 0.4409 0.3642 0.3370 -0.1495 0.1269  -0.0872 7   SER   B O   
3987 C CB  . SER   B 7   ? 0.4566 0.4013 0.3787 -0.1334 0.1000  -0.1029 7   SER   B CB  
3988 O OG  . SER   B 7   ? 0.4739 0.4127 0.4405 -0.1271 0.1039  -0.0946 7   SER   B OG  
3994 N N   A GLY   B 8   ? 0.4302 0.3599 0.3271 -0.1382 0.1135  -0.0915 8   GLY   B N   
3995 N N   B GLY   B 8   ? 0.4305 0.3605 0.3276 -0.1379 0.1143  -0.0921 8   GLY   B N   
3996 C CA  A GLY   B 8   ? 0.4206 0.3510 0.3268 -0.1295 0.1171  -0.0895 8   GLY   B CA  
3997 C CA  B GLY   B 8   ? 0.4208 0.3518 0.3270 -0.1292 0.1188  -0.0902 8   GLY   B CA  
3998 C C   A GLY   B 8   ? 0.4066 0.3358 0.3207 -0.1240 0.1158  -0.0842 8   GLY   B C   
3999 C C   B GLY   B 8   ? 0.4063 0.3364 0.3207 -0.1238 0.1178  -0.0843 8   GLY   B C   
4000 O O   A GLY   B 8   ? 0.4134 0.3465 0.3442 -0.1137 0.1168  -0.0884 8   GLY   B O   
4001 O O   B GLY   B 8   ? 0.4133 0.3478 0.3456 -0.1128 0.1192  -0.0891 8   GLY   B O   
4008 N N   . TYR   B 9   ? 0.3961 0.3152 0.3073 -0.1183 0.0972  -0.0913 9   TYR   B N   
4009 C CA  . TYR   B 9   ? 0.3671 0.2720 0.2702 -0.1090 0.0719  -0.0755 9   TYR   B CA  
4010 C C   . TYR   B 9   ? 0.3570 0.2676 0.2720 -0.1040 0.0497  -0.0647 9   TYR   B C   
4011 O O   . TYR   B 9   ? 0.3616 0.2816 0.3025 -0.0963 0.0659  -0.0531 9   TYR   B O   
4012 C CB  . TYR   B 9   ? 0.3567 0.2399 0.2782 -0.0958 0.0730  -0.0665 9   TYR   B CB  
4013 C CG  . TYR   B 9   ? 0.3473 0.2136 0.2701 -0.0995 0.0683  -0.0670 9   TYR   B CG  
4014 C CD1 . TYR   B 9   ? 0.3519 0.2231 0.2766 -0.1046 0.0665  -0.0586 9   TYR   B CD1 
4015 C CD2 . TYR   B 9   ? 0.3433 0.2018 0.2643 -0.0870 0.0552  -0.0748 9   TYR   B CD2 
4016 C CE1 . TYR   B 9   ? 0.3470 0.2299 0.2781 -0.1067 0.0656  -0.0743 9   TYR   B CE1 
4017 C CE2 . TYR   B 9   ? 0.3410 0.2086 0.2824 -0.0916 0.0592  -0.0540 9   TYR   B CE2 
4018 C CZ  . TYR   B 9   ? 0.3416 0.2322 0.2822 -0.0977 0.0612  -0.0828 9   TYR   B CZ  
4019 O OH  . TYR   B 9   ? 0.3359 0.2440 0.2894 -0.1058 0.0668  -0.0877 9   TYR   B OH  
4030 N N   . LEU   B 10  ? 0.3445 0.2368 0.2609 -0.1119 0.0236  -0.0634 10  LEU   B N   
4031 C CA  . LEU   B 10  ? 0.3466 0.2335 0.2524 -0.1156 -0.0086 -0.0511 10  LEU   B CA  
4032 C C   . LEU   B 10  ? 0.3247 0.2422 0.2480 -0.1084 -0.0178 -0.0378 10  LEU   B C   
4033 O O   . LEU   B 10  ? 0.3021 0.2434 0.2427 -0.0917 -0.0186 -0.0424 10  LEU   B O   
4034 C CB  . LEU   B 10  ? 0.3779 0.2288 0.2818 -0.1121 -0.0311 -0.0305 10  LEU   B CB  
4035 C CG  . LEU   B 10  ? 0.4083 0.2325 0.3111 -0.1079 -0.0600 -0.0223 10  LEU   B CG  
4036 C CD1 . LEU   B 10  ? 0.4260 0.2462 0.3197 -0.0991 -0.0602 -0.0181 10  LEU   B CD1 
4037 C CD2 . LEU   B 10  ? 0.4144 0.2349 0.3386 -0.1097 -0.0522 0.0067  10  LEU   B CD2 
4049 N N   A LYS   B 11  ? 0.3322 0.2639 0.2591 -0.0994 -0.0224 -0.0295 11  LYS   B N   
4050 N N   B LYS   B 11  ? 0.3320 0.2637 0.2569 -0.1003 -0.0238 -0.0300 11  LYS   B N   
4051 C CA  A LYS   B 11  ? 0.3439 0.2886 0.2972 -0.0868 -0.0284 -0.0308 11  LYS   B CA  
4052 C CA  B LYS   B 11  ? 0.3443 0.2889 0.2959 -0.0876 -0.0316 -0.0330 11  LYS   B CA  
4053 C C   A LYS   B 11  ? 0.3268 0.2703 0.2995 -0.1005 -0.0277 -0.0407 11  LYS   B C   
4054 C C   B LYS   B 11  ? 0.3272 0.2681 0.2973 -0.1040 -0.0330 -0.0460 11  LYS   B C   
4055 O O   A LYS   B 11  ? 0.3412 0.2814 0.3154 -0.1078 -0.0273 -0.0482 11  LYS   B O   
4056 O O   B LYS   B 11  ? 0.3425 0.2759 0.3124 -0.1165 -0.0381 -0.0610 11  LYS   B O   
4057 C CB  A LYS   B 11  ? 0.3689 0.3270 0.3612 -0.0638 -0.0310 -0.0258 11  LYS   B CB  
4058 C CB  B LYS   B 11  ? 0.3698 0.3302 0.3640 -0.0620 -0.0335 -0.0267 11  LYS   B CB  
4059 C CG  A LYS   B 11  ? 0.3914 0.3521 0.4176 -0.0485 -0.0338 -0.0239 11  LYS   B CG  
4060 C CG  B LYS   B 11  ? 0.3927 0.3581 0.4241 -0.0442 -0.0360 -0.0235 11  LYS   B CG  
4061 C CD  A LYS   B 11  ? 0.4057 0.3688 0.4636 -0.0401 -0.0351 -0.0224 11  LYS   B CD  
4062 C CD  B LYS   B 11  ? 0.4074 0.3762 0.4733 -0.0357 -0.0378 -0.0233 11  LYS   B CD  
4063 C CE  A LYS   B 11  ? 0.4167 0.3797 0.4987 -0.0360 -0.0357 -0.0233 11  LYS   B CE  
4064 C CE  B LYS   B 11  ? 0.4190 0.3888 0.5101 -0.0302 -0.0389 -0.0232 11  LYS   B CE  
4065 N NZ  A LYS   B 11  ? 0.4225 0.3869 0.5156 -0.0335 -0.0364 -0.0218 11  LYS   B NZ  
4066 N NZ  B LYS   B 11  ? 0.4248 0.3957 0.5276 -0.0280 -0.0404 -0.0214 11  LYS   B NZ  
4093 N N   . LEU   B 12  ? 0.2952 0.2465 0.2879 -0.0995 -0.0359 -0.0508 12  LEU   B N   
4094 C CA  . LEU   B 12  ? 0.2716 0.2241 0.3006 -0.0771 -0.0261 -0.0440 12  LEU   B CA  
4095 C C   . LEU   B 12  ? 0.2647 0.2263 0.3214 -0.0726 -0.0541 -0.0335 12  LEU   B C   
4096 O O   . LEU   B 12  ? 0.2599 0.2234 0.3358 -0.0840 -0.0767 -0.0291 12  LEU   B O   
4097 C CB  . LEU   B 12  ? 0.2623 0.2002 0.3098 -0.0566 -0.0142 -0.0334 12  LEU   B CB  
4098 C CG  . LEU   B 12  ? 0.2553 0.1932 0.3097 -0.0541 -0.0070 -0.0380 12  LEU   B CG  
4099 C CD1 . LEU   B 12  ? 0.2627 0.1960 0.3189 -0.0346 -0.0066 -0.0230 12  LEU   B CD1 
4100 C CD2 . LEU   B 12  ? 0.2626 0.1908 0.3244 -0.0485 -0.0042 -0.0536 12  LEU   B CD2 
4113 N N   . THR   B 13  ? 0.2588 0.2256 0.3239 -0.0752 -0.0662 -0.0447 13  THR   B N   
4114 C CA  . THR   B 13  ? 0.2571 0.2264 0.3233 -0.0798 -0.0785 -0.0158 13  THR   B CA  
4115 C C   . THR   B 13  ? 0.3027 0.2476 0.3405 -0.0988 -0.0947 -0.0092 13  THR   B C   
4116 O O   . THR   B 13  ? 0.3263 0.2536 0.3429 -0.0899 -0.0550 -0.0072 13  THR   B O   
4117 C CB  . THR   B 13  ? 0.2286 0.2250 0.3275 -0.0583 -0.0714 -0.0143 13  THR   B CB  
4118 O OG1 . THR   B 13  ? 0.2122 0.2126 0.3369 -0.0552 -0.0570 -0.0251 13  THR   B OG1 
4119 C CG2 . THR   B 13  ? 0.2287 0.2312 0.3352 -0.0522 -0.0646 -0.0078 13  THR   B CG2 
4127 N N   A ASP   B 14  ? 0.3145 0.2633 0.3513 -0.1035 -0.1158 0.0030  14  ASP   B N   
4128 N N   B ASP   B 14  ? 0.3160 0.2655 0.3452 -0.1007 -0.1172 0.0087  14  ASP   B N   
4129 C CA  A ASP   B 14  ? 0.3289 0.2761 0.3718 -0.1016 -0.1120 0.0132  14  ASP   B CA  
4130 C CA  B ASP   B 14  ? 0.3320 0.2800 0.3610 -0.0960 -0.1124 0.0234  14  ASP   B CA  
4131 C C   A ASP   B 14  ? 0.3180 0.2611 0.3249 -0.1000 -0.1138 0.0103  14  ASP   B C   
4132 C C   B ASP   B 14  ? 0.3198 0.2609 0.3208 -0.0970 -0.1110 0.0178  14  ASP   B C   
4133 O O   A ASP   B 14  ? 0.3407 0.2794 0.3235 -0.0989 -0.1170 0.0078  14  ASP   B O   
4134 O O   B ASP   B 14  ? 0.3435 0.2731 0.3247 -0.0955 -0.1084 0.0223  14  ASP   B O   
4135 C CB  A ASP   B 14  ? 0.3492 0.3063 0.4377 -0.0981 -0.1097 0.0139  14  ASP   B CB  
4136 C CB  B ASP   B 14  ? 0.3551 0.3157 0.4183 -0.0859 -0.1110 0.0297  14  ASP   B CB  
4137 C CG  A ASP   B 14  ? 0.3691 0.3277 0.4975 -0.0949 -0.1056 0.0017  14  ASP   B CG  
4138 C CG  B ASP   B 14  ? 0.3780 0.3454 0.4729 -0.0749 -0.1064 0.0215  14  ASP   B CG  
4139 O OD1 A ASP   B 14  ? 0.3780 0.3284 0.5098 -0.1021 -0.1103 -0.0126 14  ASP   B OD1 
4140 O OD1 B ASP   B 14  ? 0.3892 0.3574 0.4822 -0.0713 -0.1031 0.0110  14  ASP   B OD1 
4141 O OD2 A ASP   B 14  ? 0.3714 0.3386 0.5239 -0.0951 -0.0983 0.0070  14  ASP   B OD2 
4142 O OD2 B ASP   B 14  ? 0.3815 0.3533 0.4980 -0.0771 -0.1052 0.0265  14  ASP   B OD2 
4151 N N   . ASN   B 15  ? 0.2820 0.2347 0.2973 -0.0901 -0.1160 0.0140  15  ASN   B N   
4152 C CA  . ASN   B 15  ? 0.2355 0.2052 0.2786 -0.0587 -0.0940 0.0040  15  ASN   B CA  
4153 C C   . ASN   B 15  ? 0.2136 0.1821 0.2637 -0.0389 -0.0711 0.0033  15  ASN   B C   
4154 O O   . ASN   B 15  ? 0.2078 0.1674 0.2797 -0.0357 -0.0727 -0.0083 15  ASN   B O   
4155 C CB  . ASN   B 15  ? 0.2207 0.1981 0.2853 -0.0399 -0.0919 0.0132  15  ASN   B CB  
4156 C CG  . ASN   B 15  ? 0.1937 0.1884 0.2984 -0.0376 -0.0572 0.0280  15  ASN   B CG  
4157 O OD1 . ASN   B 15  ? 0.2044 0.2150 0.3328 -0.0571 -0.0622 0.0352  15  ASN   B OD1 
4158 N ND2 . ASN   B 15  ? 0.1897 0.1668 0.2925 -0.0250 -0.0191 0.0044  15  ASN   B ND2 
4166 N N   . VAL   B 16  ? 0.2113 0.1719 0.2647 -0.0471 -0.0715 0.0044  16  VAL   B N   
4167 C CA  . VAL   B 16  ? 0.2095 0.1773 0.2495 -0.0389 -0.0580 -0.0182 16  VAL   B CA  
4168 C C   . VAL   B 16  ? 0.2052 0.1943 0.2561 -0.0458 -0.0505 -0.0218 16  VAL   B C   
4169 O O   . VAL   B 16  ? 0.2061 0.2079 0.2694 -0.0507 -0.0500 -0.0392 16  VAL   B O   
4170 C CB  . VAL   B 16  ? 0.2079 0.1680 0.2695 -0.0230 -0.0436 -0.0246 16  VAL   B CB  
4171 C CG1 . VAL   B 16  ? 0.2099 0.1622 0.2707 -0.0110 -0.0347 -0.0112 16  VAL   B CG1 
4172 C CG2 . VAL   B 16  ? 0.2092 0.1655 0.2887 -0.0107 -0.0393 -0.0269 16  VAL   B CG2 
4182 N N   . TYR   B 17  ? 0.2062 0.1880 0.2444 -0.0499 -0.0409 -0.0227 17  TYR   B N   
4183 C CA  . TYR   B 17  ? 0.2184 0.2111 0.2493 -0.0583 -0.0388 -0.0048 17  TYR   B CA  
4184 C C   . TYR   B 17  ? 0.2109 0.1860 0.2533 -0.0552 -0.0325 -0.0203 17  TYR   B C   
4185 O O   . TYR   B 17  ? 0.2061 0.1843 0.2482 -0.0362 -0.0433 -0.0361 17  TYR   B O   
4186 C CB  . TYR   B 17  ? 0.2583 0.2663 0.2816 -0.0509 -0.0483 0.0366  17  TYR   B CB  
4187 C CG  . TYR   B 17  ? 0.3040 0.3304 0.3444 -0.0436 -0.0684 0.0506  17  TYR   B CG  
4188 C CD1 . TYR   B 17  ? 0.3252 0.3554 0.3742 -0.0418 -0.0777 0.0643  17  TYR   B CD1 
4189 C CD2 . TYR   B 17  ? 0.3279 0.3656 0.3880 -0.0380 -0.0851 0.0504  17  TYR   B CD2 
4190 C CE1 . TYR   B 17  ? 0.3458 0.3886 0.4036 -0.0359 -0.0908 0.0588  17  TYR   B CE1 
4191 C CE2 . TYR   B 17  ? 0.3487 0.3934 0.4162 -0.0278 -0.0984 0.0596  17  TYR   B CE2 
4192 C CZ  . TYR   B 17  ? 0.3570 0.4074 0.4318 -0.0277 -0.1034 0.0595  17  TYR   B CZ  
4193 O OH  . TYR   B 17  ? 0.3747 0.4247 0.4514 -0.0192 -0.1098 0.0619  17  TYR   B OH  
4203 N N   . ILE   B 18  ? 0.2214 0.1892 0.2326 -0.0475 -0.0245 -0.0252 18  ILE   B N   
4204 C CA  . ILE   B 18  ? 0.2279 0.1740 0.2317 -0.0530 -0.0035 -0.0377 18  ILE   B CA  
4205 C C   . ILE   B 18  ? 0.2378 0.1771 0.2366 -0.0592 -0.0011 -0.0456 18  ILE   B C   
4206 O O   . ILE   B 18  ? 0.2612 0.1965 0.2380 -0.0511 0.0052  -0.0554 18  ILE   B O   
4207 C CB  . ILE   B 18  ? 0.2361 0.1743 0.2447 -0.0554 -0.0081 -0.0284 18  ILE   B CB  
4208 C CG1 . ILE   B 18  ? 0.2337 0.1869 0.2505 -0.0547 -0.0122 -0.0191 18  ILE   B CG1 
4209 C CG2 . ILE   B 18  ? 0.2432 0.1798 0.2461 -0.0584 -0.0061 -0.0175 18  ILE   B CG2 
4210 C CD1 . ILE   B 18  ? 0.2383 0.2165 0.2756 -0.0485 -0.0176 0.0188  18  ILE   B CD1 
4222 N N   . LYS   B 19  ? 0.2341 0.1754 0.2469 -0.0407 0.0350  -0.0525 19  LYS   B N   
4223 C CA  . LYS   B 19  ? 0.2394 0.1889 0.2787 -0.0469 0.0314  -0.0525 19  LYS   B CA  
4224 C C   . LYS   B 19  ? 0.2217 0.1760 0.3041 -0.0338 0.0362  -0.0737 19  LYS   B C   
4225 O O   . LYS   B 19  ? 0.2074 0.1772 0.2895 -0.0200 0.0227  -0.0648 19  LYS   B O   
4226 C CB  . LYS   B 19  ? 0.2686 0.2135 0.2870 -0.0548 0.0571  -0.0487 19  LYS   B CB  
4227 C CG  . LYS   B 19  ? 0.3035 0.2327 0.3115 -0.0637 0.0648  -0.0572 19  LYS   B CG  
4228 C CD  . LYS   B 19  ? 0.3368 0.2698 0.3228 -0.0743 0.0782  -0.0545 19  LYS   B CD  
4229 C CE  . LYS   B 19  ? 0.3595 0.3019 0.3410 -0.0825 0.0750  -0.0583 19  LYS   B CE  
4230 N NZ  . LYS   B 19  ? 0.3749 0.3186 0.3410 -0.0860 0.0786  -0.0559 19  LYS   B NZ  
4244 N N   . ASN   B 20  ? 0.2256 0.1920 0.3405 -0.0385 0.0532  -0.0799 20  ASN   B N   
4245 C CA  . ASN   B 20  ? 0.2188 0.2056 0.3692 -0.0298 0.0535  -0.1016 20  ASN   B CA  
4246 C C   . ASN   B 20  ? 0.2207 0.2279 0.3772 -0.0300 0.0622  -0.1085 20  ASN   B C   
4247 O O   . ASN   B 20  ? 0.2461 0.2673 0.3934 -0.0445 0.0700  -0.1023 20  ASN   B O   
4248 C CB  . ASN   B 20  ? 0.2444 0.2084 0.3996 -0.0036 0.0409  -0.0996 20  ASN   B CB  
4249 C CG  . ASN   B 20  ? 0.2792 0.2245 0.4322 0.0325  0.0466  -0.1140 20  ASN   B CG  
4250 O OD1 . ASN   B 20  ? 0.3206 0.2549 0.4645 0.0530  0.0505  -0.1102 20  ASN   B OD1 
4251 N ND2 . ASN   B 20  ? 0.2710 0.2244 0.4353 0.0365  0.0401  -0.1151 20  ASN   B ND2 
4258 N N   . ALA   B 21  ? 0.2184 0.2103 0.3772 -0.0362 0.0686  -0.0844 21  ALA   B N   
4259 C CA  . ALA   B 21  ? 0.2320 0.2118 0.3721 -0.0364 0.0576  -0.0715 21  ALA   B CA  
4260 C C   . ALA   B 21  ? 0.2332 0.1865 0.3529 -0.0268 0.0588  -0.0566 21  ALA   B C   
4261 O O   . ALA   B 21  ? 0.2373 0.1847 0.3562 -0.0350 0.0533  -0.0502 21  ALA   B O   
4262 C CB  . ALA   B 21  ? 0.2574 0.2424 0.3856 -0.0519 0.0514  -0.0548 21  ALA   B CB  
4268 N N   . ASP   B 22  ? 0.2235 0.1769 0.3467 -0.0251 0.0374  -0.0505 22  ASP   B N   
4269 C CA  . ASP   B 22  ? 0.2255 0.1722 0.3369 -0.0138 0.0243  -0.0327 22  ASP   B CA  
4270 C C   . ASP   B 22  ? 0.2172 0.1608 0.2832 -0.0177 0.0125  -0.0266 22  ASP   B C   
4271 O O   . ASP   B 22  ? 0.2236 0.1659 0.2913 -0.0135 0.0069  -0.0090 22  ASP   B O   
4272 C CB  . ASP   B 22  ? 0.2360 0.1828 0.3763 -0.0072 0.0258  -0.0078 22  ASP   B CB  
4273 C CG  . ASP   B 22  ? 0.2356 0.2050 0.4366 0.0091  0.0110  -0.0006 22  ASP   B CG  
4274 O OD1 . ASP   B 22  ? 0.2418 0.1936 0.4364 0.0054  -0.0148 0.0119  22  ASP   B OD1 
4275 O OD2 . ASP   B 22  ? 0.2509 0.2309 0.4951 0.0299  -0.0040 -0.0116 22  ASP   B OD2 
4280 N N   . ILE   B 23  ? 0.2048 0.1536 0.2484 -0.0147 0.0024  0.0156  23  ILE   B N   
4281 C CA  . ILE   B 23  ? 0.1925 0.1535 0.2267 -0.0162 -0.0096 0.0121  23  ILE   B CA  
4282 C C   . ILE   B 23  ? 0.1872 0.1612 0.2106 -0.0138 -0.0126 0.0046  23  ILE   B C   
4283 O O   . ILE   B 23  ? 0.1784 0.1612 0.2104 -0.0101 -0.0060 0.0072  23  ILE   B O   
4284 C CB  . ILE   B 23  ? 0.1884 0.1629 0.2404 -0.0229 -0.0092 0.0162  23  ILE   B CB  
4285 C CG1 . ILE   B 23  ? 0.1903 0.1831 0.2635 -0.0173 -0.0014 0.0314  23  ILE   B CG1 
4286 C CG2 . ILE   B 23  ? 0.2004 0.1907 0.2577 -0.0147 0.0021  0.0097  23  ILE   B CG2 
4287 C CD1 . ILE   B 23  ? 0.1896 0.1953 0.2580 -0.0138 0.0006  0.0255  23  ILE   B CD1 
4299 N N   . VAL   B 24  ? 0.1926 0.1559 0.2296 -0.0123 -0.0205 0.0122  24  VAL   B N   
4300 C CA  . VAL   B 24  ? 0.1841 0.1677 0.2547 -0.0063 -0.0213 -0.0058 24  VAL   B CA  
4301 C C   . VAL   B 24  ? 0.1898 0.1755 0.2614 -0.0077 -0.0056 -0.0005 24  VAL   B C   
4302 O O   . VAL   B 24  ? 0.1860 0.1799 0.2625 -0.0179 -0.0029 0.0128  24  VAL   B O   
4303 C CB  . VAL   B 24  ? 0.1943 0.1817 0.2651 0.0024  -0.0342 0.0024  24  VAL   B CB  
4304 C CG1 . VAL   B 24  ? 0.1968 0.1849 0.3056 -0.0087 -0.0453 -0.0055 24  VAL   B CG1 
4305 C CG2 . VAL   B 24  ? 0.2000 0.2126 0.2633 0.0101  -0.0235 -0.0087 24  VAL   B CG2 
4315 N N   A GLU   B 25  ? 0.2078 0.1915 0.2785 -0.0055 0.0037  0.0008  25  GLU   B N   
4316 N N   B GLU   B 25  ? 0.2055 0.1906 0.2791 -0.0062 0.0063  0.0012  25  GLU   B N   
4317 C CA  A GLU   B 25  ? 0.2294 0.2180 0.2879 -0.0015 0.0057  -0.0189 25  GLU   B CA  
4318 C CA  B GLU   B 25  ? 0.2242 0.2170 0.2889 -0.0027 0.0108  -0.0191 25  GLU   B CA  
4319 C C   A GLU   B 25  ? 0.2207 0.2070 0.2463 -0.0111 0.0085  -0.0180 25  GLU   B C   
4320 C C   B GLU   B 25  ? 0.2125 0.2084 0.2535 -0.0107 0.0126  -0.0108 25  GLU   B C   
4321 O O   A GLU   B 25  ? 0.2213 0.2139 0.2666 -0.0103 0.0173  -0.0132 25  GLU   B O   
4322 O O   B GLU   B 25  ? 0.2122 0.2159 0.2750 -0.0094 0.0181  -0.0060 25  GLU   B O   
4323 C CB  A GLU   B 25  ? 0.2639 0.2618 0.3469 0.0104  0.0087  -0.0171 25  GLU   B CB  
4324 C CB  B GLU   B 25  ? 0.2593 0.2604 0.3436 0.0082  0.0174  -0.0221 25  GLU   B CB  
4325 C CG  A GLU   B 25  ? 0.2984 0.3052 0.4209 0.0140  0.0042  -0.0181 25  GLU   B CG  
4326 C CG  B GLU   B 25  ? 0.2958 0.3059 0.4184 0.0102  0.0156  -0.0256 25  GLU   B CG  
4327 C CD  A GLU   B 25  ? 0.3296 0.3423 0.4817 0.0091  -0.0034 -0.0197 25  GLU   B CD  
4328 C CD  B GLU   B 25  ? 0.3287 0.3435 0.4786 0.0026  0.0111  -0.0291 25  GLU   B CD  
4329 O OE1 A GLU   B 25  ? 0.3406 0.3576 0.5027 0.0129  0.0028  -0.0152 25  GLU   B OE1 
4330 O OE1 B GLU   B 25  ? 0.3398 0.3608 0.5003 0.0046  0.0167  -0.0291 25  GLU   B OE1 
4331 O OE2 A GLU   B 25  ? 0.3397 0.3551 0.5034 0.0053  -0.0139 -0.0274 25  GLU   B OE2 
4332 O OE2 B GLU   B 25  ? 0.3412 0.3555 0.4992 -0.0015 0.0022  -0.0350 25  GLU   B OE2 
4345 N N   A GLU   B 26  ? 0.2170 0.1958 0.2168 -0.0281 0.0071  -0.0200 26  GLU   B N   
4346 N N   B GLU   B 26  ? 0.2072 0.2004 0.2321 -0.0272 0.0132  -0.0035 26  GLU   B N   
4347 C CA  A GLU   B 26  ? 0.2213 0.2055 0.2110 -0.0411 -0.0038 -0.0099 26  GLU   B CA  
4348 C CA  B GLU   B 26  ? 0.2111 0.2133 0.2380 -0.0394 0.0031  0.0123  26  GLU   B CA  
4349 C C   A GLU   B 26  ? 0.1998 0.2050 0.2100 -0.0333 -0.0019 0.0074  26  GLU   B C   
4350 C C   B GLU   B 26  ? 0.1929 0.2090 0.2245 -0.0341 0.0012  0.0167  26  GLU   B C   
4351 O O   A GLU   B 26  ? 0.2143 0.2243 0.2114 -0.0291 -0.0062 0.0072  26  GLU   B O   
4352 O O   B GLU   B 26  ? 0.2065 0.2292 0.2300 -0.0328 -0.0061 0.0122  26  GLU   B O   
4353 C CB  A GLU   B 26  ? 0.2525 0.2148 0.2112 -0.0402 0.0026  -0.0102 26  GLU   B CB  
4354 C CB  B GLU   B 26  ? 0.2369 0.2300 0.2621 -0.0364 0.0129  0.0265  26  GLU   B CB  
4355 C CG  A GLU   B 26  ? 0.2849 0.2281 0.2318 -0.0343 0.0046  -0.0279 26  GLU   B CG  
4356 C CG  B GLU   B 26  ? 0.2618 0.2528 0.3090 -0.0259 0.0223  0.0192  26  GLU   B CG  
4357 C CD  A GLU   B 26  ? 0.3066 0.2299 0.2344 -0.0437 0.0130  -0.0488 26  GLU   B CD  
4358 C CD  B GLU   B 26  ? 0.2708 0.2562 0.3373 -0.0282 0.0373  0.0155  26  GLU   B CD  
4359 O OE1 A GLU   B 26  ? 0.3138 0.2182 0.2377 -0.0422 0.0331  -0.0694 26  GLU   B OE1 
4360 O OE1 B GLU   B 26  ? 0.2739 0.2545 0.3690 -0.0380 0.0707  0.0089  26  GLU   B OE1 
4361 O OE2 A GLU   B 26  ? 0.3153 0.2408 0.2389 -0.0504 0.0175  -0.0179 26  GLU   B OE2 
4362 O OE2 B GLU   B 26  ? 0.2667 0.2587 0.3382 -0.0212 0.0385  0.0087  26  GLU   B OE2 
4375 N N   . ALA   B 27  ? 0.1778 0.1917 0.2186 -0.0290 0.0004  0.0180  27  ALA   B N   
4376 C CA  . ALA   B 27  ? 0.1781 0.1846 0.2205 -0.0245 -0.0099 0.0256  27  ALA   B CA  
4377 C C   . ALA   B 27  ? 0.1876 0.1948 0.2509 -0.0225 0.0081  0.0359  27  ALA   B C   
4378 O O   . ALA   B 27  ? 0.1924 0.1989 0.2641 -0.0065 0.0063  0.0387  27  ALA   B O   
4379 C CB  . ALA   B 27  ? 0.1902 0.1687 0.2189 -0.0208 0.0015  0.0174  27  ALA   B CB  
4386 N N   . LYS   B 28  ? 0.1907 0.2155 0.2943 -0.0232 0.0221  0.0572  28  LYS   B N   
4387 C CA  . LYS   B 28  ? 0.2009 0.2551 0.3254 -0.0150 0.0541  0.0734  28  LYS   B CA  
4388 C C   . LYS   B 28  ? 0.2289 0.2675 0.3087 -0.0174 0.0605  0.0601  28  LYS   B C   
4389 O O   . LYS   B 28  ? 0.2538 0.2736 0.3134 -0.0192 0.0597  0.0490  28  LYS   B O   
4390 C CB  . LYS   B 28  ? 0.2268 0.2978 0.3798 -0.0043 0.0900  0.0870  28  LYS   B CB  
4391 C CG  . LYS   B 28  ? 0.2716 0.3534 0.4190 0.0031  0.1011  0.0993  28  LYS   B CG  
4392 C CD  . LYS   B 28  ? 0.3313 0.4171 0.4756 0.0083  0.1133  0.1020  28  LYS   B CD  
4393 C CE  . LYS   B 28  ? 0.3794 0.4643 0.5237 0.0139  0.1152  0.1072  28  LYS   B CE  
4394 N NZ  . LYS   B 28  ? 0.4190 0.4839 0.5437 0.0197  0.1141  0.1113  28  LYS   B NZ  
4408 N N   . LYS   B 29  ? 0.2488 0.2963 0.3092 -0.0028 0.0574  0.0465  29  LYS   B N   
4409 C CA  . LYS   B 29  ? 0.2960 0.3366 0.3216 0.0014  0.0714  0.0510  29  LYS   B CA  
4410 C C   . LYS   B 29  ? 0.2929 0.3356 0.2825 -0.0035 0.0469  0.0634  29  LYS   B C   
4411 O O   . LYS   B 29  ? 0.3141 0.3638 0.3052 -0.0015 0.0560  0.0678  29  LYS   B O   
4412 C CB  . LYS   B 29  ? 0.3586 0.3836 0.4186 0.0091  0.0786  0.0377  29  LYS   B CB  
4413 C CG  . LYS   B 29  ? 0.4127 0.4214 0.5257 0.0135  0.0847  0.0326  29  LYS   B CG  
4414 C CD  . LYS   B 29  ? 0.4592 0.4544 0.6036 0.0126  0.0953  0.0281  29  LYS   B CD  
4415 C CE  . LYS   B 29  ? 0.4921 0.4761 0.6598 0.0113  0.1028  0.0245  29  LYS   B CE  
4416 N NZ  . LYS   B 29  ? 0.5067 0.4846 0.6922 0.0099  0.1072  0.0221  29  LYS   B NZ  
4430 N N   . VAL   B 30  ? 0.2607 0.3131 0.2504 -0.0186 0.0268  0.0512  30  VAL   B N   
4431 C CA  . VAL   B 30  ? 0.2418 0.2991 0.2730 -0.0318 -0.0078 0.0598  30  VAL   B CA  
4432 C C   . VAL   B 30  ? 0.2138 0.2853 0.2709 -0.0288 -0.0139 0.0845  30  VAL   B C   
4433 O O   . VAL   B 30  ? 0.2273 0.2982 0.2861 -0.0198 -0.0077 0.1074  30  VAL   B O   
4434 C CB  . VAL   B 30  ? 0.2415 0.2947 0.3085 -0.0448 -0.0285 0.0596  30  VAL   B CB  
4435 C CG1 . VAL   B 30  ? 0.2445 0.3077 0.3098 -0.0437 -0.0189 0.0448  30  VAL   B CG1 
4436 C CG2 . VAL   B 30  ? 0.2569 0.2926 0.3390 -0.0549 -0.0333 0.0441  30  VAL   B CG2 
4446 N N   A LYS   B 31  ? 0.2035 0.2655 0.2877 -0.0400 -0.0119 0.0894  31  LYS   B N   
4447 N N   B LYS   B 31  ? 0.2000 0.2644 0.2860 -0.0410 -0.0104 0.0866  31  LYS   B N   
4448 C CA  A LYS   B 31  ? 0.1993 0.2609 0.3122 -0.0465 -0.0103 0.0941  31  LYS   B CA  
4449 C CA  B LYS   B 31  ? 0.1951 0.2605 0.3094 -0.0477 -0.0115 0.0870  31  LYS   B CA  
4450 C C   A LYS   B 31  ? 0.1904 0.2265 0.2855 -0.0454 -0.0295 0.0837  31  LYS   B C   
4451 C C   B LYS   B 31  ? 0.1871 0.2263 0.2853 -0.0452 -0.0299 0.0802  31  LYS   B C   
4452 O O   A LYS   B 31  ? 0.1911 0.2319 0.3027 -0.0488 -0.0317 0.0959  31  LYS   B O   
4453 O O   B LYS   B 31  ? 0.1874 0.2328 0.3049 -0.0472 -0.0313 0.0928  31  LYS   B O   
4454 C CB  A LYS   B 31  ? 0.2149 0.2985 0.3592 -0.0418 0.0150  0.1031  31  LYS   B CB  
4455 C CB  B LYS   B 31  ? 0.2115 0.2997 0.3529 -0.0426 0.0101  0.0867  31  LYS   B CB  
4456 C CG  A LYS   B 31  ? 0.2454 0.3347 0.4121 -0.0356 0.0231  0.0948  31  LYS   B CG  
4457 C CG  B LYS   B 31  ? 0.2447 0.3370 0.4036 -0.0352 0.0144  0.0696  31  LYS   B CG  
4458 C CD  A LYS   B 31  ? 0.2776 0.3690 0.4577 -0.0268 0.0188  0.0792  31  LYS   B CD  
4459 C CD  B LYS   B 31  ? 0.2772 0.3722 0.4485 -0.0301 0.0068  0.0496  31  LYS   B CD  
4460 C CE  A LYS   B 31  ? 0.3009 0.3915 0.4912 -0.0208 0.0160  0.0661  31  LYS   B CE  
4461 C CE  B LYS   B 31  ? 0.2992 0.3944 0.4833 -0.0262 0.0033  0.0379  31  LYS   B CE  
4462 N NZ  A LYS   B 31  ? 0.3132 0.4028 0.5037 -0.0138 0.0120  0.0587  31  LYS   B NZ  
4463 N NZ  B LYS   B 31  ? 0.3093 0.4039 0.4961 -0.0192 -0.0033 0.0305  31  LYS   B NZ  
4490 N N   . PRO   B 32  ? 0.1963 0.1904 0.2406 -0.0439 -0.0486 0.0591  32  PRO   B N   
4491 C CA  . PRO   B 32  ? 0.2128 0.1822 0.1995 -0.0377 -0.0458 0.0310  32  PRO   B CA  
4492 C C   . PRO   B 32  ? 0.2223 0.1738 0.1863 -0.0450 -0.0546 0.0340  32  PRO   B C   
4493 O O   . PRO   B 32  ? 0.2252 0.1760 0.2243 -0.0451 -0.0739 0.0322  32  PRO   B O   
4494 C CB  . PRO   B 32  ? 0.2247 0.1717 0.1933 -0.0429 -0.0335 0.0221  32  PRO   B CB  
4495 C CG  . PRO   B 32  ? 0.2407 0.1593 0.2226 -0.0371 -0.0582 0.0233  32  PRO   B CG  
4496 C CD  . PRO   B 32  ? 0.2276 0.1736 0.2389 -0.0357 -0.0691 0.0245  32  PRO   B CD  
4504 N N   . THR   B 33  ? 0.2242 0.1608 0.1939 -0.0415 -0.0525 0.0203  33  THR   B N   
4505 C CA  . THR   B 33  ? 0.2257 0.1604 0.1865 -0.0431 -0.0524 0.0205  33  THR   B CA  
4506 C C   . THR   B 33  ? 0.2259 0.1546 0.1955 -0.0402 -0.0542 0.0184  33  THR   B C   
4507 O O   . THR   B 33  ? 0.2494 0.1537 0.1869 -0.0443 -0.0695 0.0213  33  THR   B O   
4508 C CB  . THR   B 33  ? 0.2448 0.1711 0.1983 -0.0253 -0.0568 0.0308  33  THR   B CB  
4509 O OG1 . THR   B 33  ? 0.2300 0.1793 0.2101 -0.0298 -0.0602 0.0243  33  THR   B OG1 
4510 C CG2 . THR   B 33  ? 0.2639 0.1721 0.2261 -0.0162 -0.0631 0.0297  33  THR   B CG2 
4518 N N   . VAL   B 34  ? 0.2085 0.1487 0.1816 -0.0388 -0.0470 0.0098  34  VAL   B N   
4519 C CA  . VAL   B 34  ? 0.1978 0.1451 0.1918 -0.0312 -0.0433 0.0079  34  VAL   B CA  
4520 C C   . VAL   B 34  ? 0.1781 0.1392 0.1716 -0.0380 -0.0247 0.0116  34  VAL   B C   
4521 O O   . VAL   B 34  ? 0.1949 0.1485 0.1732 -0.0308 -0.0492 0.0107  34  VAL   B O   
4522 C CB  . VAL   B 34  ? 0.2071 0.1551 0.2149 -0.0100 -0.0360 0.0108  34  VAL   B CB  
4523 C CG1 . VAL   B 34  ? 0.2040 0.1665 0.2115 -0.0047 -0.0248 0.0053  34  VAL   B CG1 
4524 C CG2 . VAL   B 34  ? 0.2073 0.1595 0.2301 -0.0091 -0.0318 0.0177  34  VAL   B CG2 
4534 N N   . VAL   B 35  ? 0.1617 0.1373 0.1715 -0.0246 -0.0297 0.0120  35  VAL   B N   
4535 C CA  . VAL   B 35  ? 0.1597 0.1337 0.1666 -0.0219 -0.0162 0.0001  35  VAL   B CA  
4536 C C   . VAL   B 35  ? 0.1482 0.1292 0.1648 -0.0192 -0.0179 0.0031  35  VAL   B C   
4537 O O   . VAL   B 35  ? 0.1529 0.1368 0.1739 -0.0255 -0.0068 -0.0045 35  VAL   B O   
4538 C CB  . VAL   B 35  ? 0.1591 0.1514 0.1764 -0.0181 -0.0073 -0.0036 35  VAL   B CB  
4539 C CG1 . VAL   B 35  ? 0.1433 0.1656 0.2077 -0.0169 -0.0030 -0.0048 35  VAL   B CG1 
4540 C CG2 . VAL   B 35  ? 0.1648 0.1549 0.1898 -0.0111 -0.0057 0.0020  35  VAL   B CG2 
4550 N N   . VAL   B 36  ? 0.1502 0.1327 0.1529 -0.0185 -0.0200 0.0038  36  VAL   B N   
4551 C CA  . VAL   B 36  ? 0.1421 0.1252 0.1667 -0.0148 -0.0149 -0.0019 36  VAL   B CA  
4552 C C   . VAL   B 36  ? 0.1426 0.1262 0.1670 -0.0114 -0.0122 0.0018  36  VAL   B C   
4553 O O   . VAL   B 36  ? 0.1511 0.1414 0.1780 -0.0119 -0.0167 -0.0029 36  VAL   B O   
4554 C CB  . VAL   B 36  ? 0.1450 0.1334 0.1654 -0.0208 -0.0176 0.0018  36  VAL   B CB  
4555 C CG1 . VAL   B 36  ? 0.1500 0.1577 0.1781 -0.0272 -0.0083 0.0010  36  VAL   B CG1 
4556 C CG2 . VAL   B 36  ? 0.1580 0.1401 0.1810 -0.0170 -0.0303 0.0015  36  VAL   B CG2 
4566 N N   . ASN   B 37  ? 0.1403 0.1348 0.1684 -0.0034 -0.0177 0.0054  37  ASN   B N   
4567 C CA  . ASN   B 37  ? 0.1408 0.1394 0.1760 -0.0023 -0.0245 0.0002  37  ASN   B CA  
4568 C C   . ASN   B 37  ? 0.1420 0.1476 0.1721 -0.0024 -0.0128 0.0024  37  ASN   B C   
4569 O O   . ASN   B 37  ? 0.1504 0.1557 0.1668 0.0016  -0.0034 0.0146  37  ASN   B O   
4570 C CB  . ASN   B 37  ? 0.1457 0.1366 0.1589 -0.0025 -0.0144 -0.0013 37  ASN   B CB  
4571 C CG  . ASN   B 37  ? 0.1501 0.1390 0.1816 -0.0043 -0.0154 0.0027  37  ASN   B CG  
4572 O OD1 . ASN   B 37  ? 0.1596 0.1520 0.1916 0.0081  -0.0285 -0.0009 37  ASN   B OD1 
4573 N ND2 . ASN   B 37  ? 0.1574 0.1410 0.1737 -0.0079 -0.0290 0.0117  37  ASN   B ND2 
4580 N N   . ALA   B 38  ? 0.1587 0.1380 0.1690 0.0056  -0.0089 0.0138  38  ALA   B N   
4581 C CA  . ALA   B 38  ? 0.1695 0.1523 0.1726 -0.0092 -0.0076 0.0132  38  ALA   B CA  
4582 C C   . ALA   B 38  ? 0.1627 0.1474 0.1684 0.0011  -0.0059 0.0197  38  ALA   B C   
4583 O O   . ALA   B 38  ? 0.1724 0.1576 0.1859 0.0099  -0.0106 0.0149  38  ALA   B O   
4584 C CB  . ALA   B 38  ? 0.1870 0.1593 0.2022 -0.0104 0.0073  0.0091  38  ALA   B CB  
4590 N N   . ALA   B 39  ? 0.1598 0.1427 0.1675 0.0082  -0.0100 0.0067  39  ALA   B N   
4591 C CA  . ALA   B 39  ? 0.1671 0.1483 0.1689 -0.0021 -0.0120 0.0115  39  ALA   B CA  
4592 C C   . ALA   B 39  ? 0.1673 0.1545 0.1557 0.0039  -0.0145 0.0029  39  ALA   B C   
4593 O O   . ALA   B 39  ? 0.1800 0.1643 0.1788 -0.0085 -0.0134 0.0124  39  ALA   B O   
4594 C CB  . ALA   B 39  ? 0.1656 0.1517 0.1925 -0.0073 -0.0055 -0.0010 39  ALA   B CB  
4600 N N   . ASN   B 40  ? 0.1791 0.1790 0.1393 -0.0052 -0.0149 -0.0017 40  ASN   B N   
4601 C CA  . ASN   B 40  ? 0.1856 0.1794 0.1605 0.0003  -0.0162 -0.0007 40  ASN   B CA  
4602 C C   . ASN   B 40  ? 0.1847 0.1757 0.1529 0.0044  -0.0271 0.0051  40  ASN   B C   
4603 O O   . ASN   B 40  ? 0.1861 0.1666 0.1572 0.0098  -0.0162 0.0069  40  ASN   B O   
4604 C CB  . ASN   B 40  ? 0.1969 0.1800 0.1746 0.0157  -0.0104 0.0160  40  ASN   B CB  
4605 C CG  . ASN   B 40  ? 0.1960 0.1824 0.2134 0.0062  -0.0270 0.0252  40  ASN   B CG  
4606 O OD1 . ASN   B 40  ? 0.1975 0.1806 0.2876 0.0017  -0.0463 0.0208  40  ASN   B OD1 
4607 N ND2 . ASN   B 40  ? 0.1967 0.1800 0.2232 0.0016  -0.0185 0.0129  40  ASN   B ND2 
4614 N N   . VAL   B 41  ? 0.1974 0.1844 0.1610 0.0113  -0.0102 0.0053  41  VAL   B N   
4615 C CA  . VAL   B 41  ? 0.2032 0.1922 0.1695 0.0018  -0.0039 -0.0007 41  VAL   B CA  
4616 C C   . VAL   B 41  ? 0.2037 0.1940 0.1666 0.0037  -0.0095 -0.0091 41  VAL   B C   
4617 O O   . VAL   B 41  ? 0.1948 0.1898 0.1796 -0.0016 -0.0175 -0.0138 41  VAL   B O   
4618 C CB  . VAL   B 41  ? 0.2072 0.2003 0.1936 -0.0084 0.0172  -0.0158 41  VAL   B CB  
4619 C CG1 . VAL   B 41  ? 0.2089 0.2100 0.2282 -0.0122 0.0346  -0.0221 41  VAL   B CG1 
4620 C CG2 . VAL   B 41  ? 0.2308 0.2252 0.2021 -0.0161 0.0084  -0.0103 41  VAL   B CG2 
4630 N N   . TYR   B 42  ? 0.2052 0.1911 0.1604 0.0120  -0.0257 0.0059  42  TYR   B N   
4631 C CA  . TYR   B 42  ? 0.2071 0.2045 0.1507 0.0213  -0.0281 -0.0119 42  TYR   B CA  
4632 C C   . TYR   B 42  ? 0.1918 0.1845 0.1723 0.0170  -0.0250 -0.0112 42  TYR   B C   
4633 O O   . TYR   B 42  ? 0.1915 0.1857 0.2171 0.0074  -0.0287 -0.0097 42  TYR   B O   
4634 C CB  . TYR   B 42  ? 0.2375 0.2445 0.1786 0.0238  -0.0383 0.0003  42  TYR   B CB  
4635 C CG  . TYR   B 42  ? 0.2390 0.2756 0.1776 0.0118  -0.0350 0.0090  42  TYR   B CG  
4636 C CD1 . TYR   B 42  ? 0.2384 0.2786 0.1641 0.0117  -0.0253 0.0041  42  TYR   B CD1 
4637 C CD2 . TYR   B 42  ? 0.2555 0.2981 0.2161 0.0154  -0.0112 0.0216  42  TYR   B CD2 
4638 C CE1 . TYR   B 42  ? 0.2565 0.3034 0.1733 0.0150  -0.0213 0.0104  42  TYR   B CE1 
4639 C CE2 . TYR   B 42  ? 0.2572 0.3123 0.2014 0.0210  0.0170  0.0437  42  TYR   B CE2 
4640 C CZ  . TYR   B 42  ? 0.2718 0.3303 0.2002 0.0278  0.0151  0.0216  42  TYR   B CZ  
4641 O OH  . TYR   B 42  ? 0.3034 0.3592 0.2484 0.0426  0.0278  0.0443  42  TYR   B OH  
4651 N N   . LEU   B 43  ? 0.1793 0.1579 0.1621 0.0093  -0.0188 -0.0121 43  LEU   B N   
4652 C CA  . LEU   B 43  ? 0.1789 0.1630 0.1615 -0.0030 -0.0223 0.0030  43  LEU   B CA  
4653 C C   . LEU   B 43  ? 0.1881 0.1680 0.1611 0.0015  -0.0161 0.0052  43  LEU   B C   
4654 O O   . LEU   B 43  ? 0.1847 0.1723 0.2002 -0.0007 -0.0263 0.0082  43  LEU   B O   
4655 C CB  . LEU   B 43  ? 0.1757 0.1620 0.1770 -0.0015 -0.0325 0.0038  43  LEU   B CB  
4656 C CG  . LEU   B 43  ? 0.1779 0.1598 0.1813 -0.0019 -0.0313 -0.0005 43  LEU   B CG  
4657 C CD1 . LEU   B 43  ? 0.1873 0.1600 0.2216 -0.0024 -0.0355 -0.0036 43  LEU   B CD1 
4658 C CD2 . LEU   B 43  ? 0.1735 0.1648 0.1984 -0.0050 -0.0221 0.0017  43  LEU   B CD2 
4670 N N   . LYS   B 44  ? 0.1863 0.1704 0.1637 0.0091  -0.0167 -0.0003 44  LYS   B N   
4671 C CA  . LYS   B 44  ? 0.1941 0.1744 0.1667 0.0072  -0.0265 0.0009  44  LYS   B CA  
4672 C C   . LYS   B 44  ? 0.1826 0.1684 0.1664 0.0091  -0.0224 0.0060  44  LYS   B C   
4673 O O   . LYS   B 44  ? 0.1985 0.1717 0.2021 0.0009  -0.0113 0.0131  44  LYS   B O   
4674 C CB  . LYS   B 44  ? 0.2272 0.1902 0.1854 0.0153  -0.0296 -0.0038 44  LYS   B CB  
4675 C CG  . LYS   B 44  ? 0.2744 0.2198 0.2263 0.0131  -0.0536 0.0030  44  LYS   B CG  
4676 C CD  . LYS   B 44  ? 0.3185 0.2464 0.2894 -0.0063 -0.0591 -0.0016 44  LYS   B CD  
4677 C CE  . LYS   B 44  ? 0.3550 0.2773 0.3393 -0.0155 -0.0680 0.0084  44  LYS   B CE  
4678 N NZ  . LYS   B 44  ? 0.3698 0.2879 0.3618 -0.0160 -0.0834 0.0149  44  LYS   B NZ  
4692 N N   . HIS   B 45  ? 0.1772 0.1741 0.1691 -0.0020 -0.0068 0.0083  45  HIS   B N   
4693 C CA  . HIS   B 45  ? 0.1710 0.1686 0.1790 -0.0018 -0.0070 0.0029  45  HIS   B CA  
4694 C C   . HIS   B 45  ? 0.1957 0.1909 0.2242 0.0068  -0.0238 0.0020  45  HIS   B C   
4695 O O   . HIS   B 45  ? 0.2111 0.2230 0.2789 0.0385  -0.0028 0.0062  45  HIS   B O   
4696 C CB  . HIS   B 45  ? 0.1662 0.1779 0.1855 -0.0011 -0.0131 -0.0054 45  HIS   B CB  
4697 C CG  . HIS   B 45  ? 0.1709 0.1686 0.1955 -0.0108 -0.0175 0.0079  45  HIS   B CG  
4698 N ND1 . HIS   B 45  ? 0.1770 0.1556 0.2067 -0.0032 -0.0149 0.0014  45  HIS   B ND1 
4699 C CD2 . HIS   B 45  ? 0.1843 0.1740 0.1895 -0.0160 -0.0177 -0.0039 45  HIS   B CD2 
4700 C CE1 . HIS   B 45  ? 0.1889 0.1510 0.1812 -0.0012 -0.0228 -0.0083 45  HIS   B CE1 
4701 N NE2 . HIS   B 45  ? 0.1921 0.1675 0.1818 -0.0052 -0.0203 -0.0088 45  HIS   B NE2 
4709 N N   A GLY   B 46  ? 0.2110 0.1862 0.2525 0.0135  -0.0353 0.0080  46  GLY   B N   
4710 N N   B GLY   B 46  ? 0.2125 0.1875 0.2477 0.0155  -0.0361 0.0145  46  GLY   B N   
4711 C CA  A GLY   B 46  ? 0.2283 0.1990 0.2912 0.0149  -0.0457 0.0081  46  GLY   B CA  
4712 C CA  B GLY   B 46  ? 0.2314 0.2023 0.2798 0.0179  -0.0482 0.0206  46  GLY   B CA  
4713 C C   A GLY   B 46  ? 0.2316 0.2158 0.3238 0.0232  -0.0337 0.0092  46  GLY   B C   
4714 C C   B GLY   B 46  ? 0.2357 0.2213 0.3049 0.0270  -0.0351 0.0279  46  GLY   B C   
4715 O O   A GLY   B 46  ? 0.2411 0.2306 0.3924 0.0220  -0.0183 -0.0174 46  GLY   B O   
4716 O O   B GLY   B 46  ? 0.2510 0.2441 0.3561 0.0246  -0.0140 0.0202  46  GLY   B O   
4723 N N   . GLY   B 47  ? 0.2285 0.2258 0.2960 0.0179  -0.0286 0.0172  47  GLY   B N   
4724 C CA  . GLY   B 47  ? 0.2083 0.2043 0.2634 0.0146  -0.0213 0.0205  47  GLY   B CA  
4725 C C   . GLY   B 47  ? 0.1805 0.1785 0.2370 0.0062  -0.0094 0.0209  47  GLY   B C   
4726 O O   . GLY   B 47  ? 0.1921 0.1584 0.2306 0.0058  -0.0091 0.0223  47  GLY   B O   
4731 N N   . GLY   B 48  ? 0.1673 0.1636 0.2430 0.0068  -0.0251 0.0368  48  GLY   B N   
4732 C CA  . GLY   B 48  ? 0.1711 0.1569 0.2280 -0.0044 -0.0101 0.0175  48  GLY   B CA  
4733 C C   . GLY   B 48  ? 0.1627 0.1523 0.2186 -0.0025 -0.0026 0.0073  48  GLY   B C   
4734 O O   . GLY   B 48  ? 0.1520 0.1528 0.2516 -0.0004 -0.0091 0.0098  48  GLY   B O   
4738 N N   . VAL   B 49  ? 0.1613 0.1594 0.2086 0.0078  -0.0144 0.0066  49  VAL   B N   
4739 C CA  . VAL   B 49  ? 0.1576 0.1645 0.1974 0.0116  -0.0167 -0.0019 49  VAL   B CA  
4740 C C   . VAL   B 49  ? 0.1467 0.1571 0.1776 0.0098  -0.0131 0.0031  49  VAL   B C   
4741 O O   . VAL   B 49  ? 0.1562 0.1640 0.1938 0.0013  -0.0090 0.0052  49  VAL   B O   
4742 C CB  . VAL   B 49  ? 0.1668 0.1837 0.2276 -0.0044 -0.0239 0.0026  49  VAL   B CB  
4743 C CG1 . VAL   B 49  ? 0.1711 0.1965 0.2226 -0.0011 -0.0374 0.0074  49  VAL   B CG1 
4744 C CG2 . VAL   B 49  ? 0.1883 0.1996 0.2688 -0.0210 -0.0471 -0.0049 49  VAL   B CG2 
4754 N N   . ALA   B 50  ? 0.1486 0.1527 0.1793 0.0011  -0.0145 0.0132  50  ALA   B N   
4755 C CA  . ALA   B 50  ? 0.1538 0.1471 0.1849 0.0082  -0.0147 0.0072  50  ALA   B CA  
4756 C C   . ALA   B 50  ? 0.1610 0.1528 0.1858 -0.0012 -0.0101 0.0031  50  ALA   B C   
4757 O O   . ALA   B 50  ? 0.1619 0.1501 0.1859 0.0009  -0.0100 0.0034  50  ALA   B O   
4758 C CB  . ALA   B 50  ? 0.1590 0.1505 0.1963 -0.0024 -0.0142 0.0085  50  ALA   B CB  
4764 N N   . GLY   B 51  ? 0.1546 0.1609 0.1857 -0.0032 -0.0220 0.0163  51  GLY   B N   
4765 C CA  . GLY   B 51  ? 0.1595 0.1625 0.2173 0.0130  -0.0294 0.0040  51  GLY   B CA  
4766 C C   . GLY   B 51  ? 0.1572 0.1626 0.2096 0.0123  -0.0127 0.0176  51  GLY   B C   
4767 O O   . GLY   B 51  ? 0.1584 0.1762 0.2260 -0.0017 -0.0164 0.0084  51  GLY   B O   
4771 N N   . ALA   B 52  ? 0.1595 0.1564 0.2030 0.0104  -0.0110 0.0117  52  ALA   B N   
4772 C CA  . ALA   B 52  ? 0.1624 0.1583 0.2016 0.0072  -0.0097 0.0024  52  ALA   B CA  
4773 C C   . ALA   B 52  ? 0.1556 0.1615 0.1856 0.0024  -0.0114 0.0039  52  ALA   B C   
4774 O O   . ALA   B 52  ? 0.1548 0.1595 0.2167 0.0058  0.0051  -0.0008 52  ALA   B O   
4775 C CB  . ALA   B 52  ? 0.1913 0.1613 0.2073 0.0054  0.0106  -0.0013 52  ALA   B CB  
4781 N N   . LEU   B 53  ? 0.1485 0.1524 0.1857 0.0115  -0.0112 0.0104  53  LEU   B N   
4782 C CA  . LEU   B 53  ? 0.1499 0.1624 0.1784 0.0050  -0.0079 0.0094  53  LEU   B CA  
4783 C C   . LEU   B 53  ? 0.1526 0.1619 0.1808 0.0002  -0.0010 0.0125  53  LEU   B C   
4784 O O   . LEU   B 53  ? 0.1611 0.1698 0.1735 -0.0074 -0.0030 0.0198  53  LEU   B O   
4785 C CB  . LEU   B 53  ? 0.1494 0.1658 0.1998 0.0088  -0.0060 0.0050  53  LEU   B CB  
4786 C CG  . LEU   B 53  ? 0.1514 0.1912 0.1963 0.0032  -0.0055 0.0143  53  LEU   B CG  
4787 C CD1 . LEU   B 53  ? 0.1549 0.2170 0.2197 0.0113  -0.0032 -0.0035 53  LEU   B CD1 
4788 C CD2 . LEU   B 53  ? 0.1781 0.2238 0.2181 -0.0081 -0.0150 -0.0042 53  LEU   B CD2 
4800 N N   . ASN   B 54  ? 0.1524 0.1500 0.1861 0.0003  -0.0063 0.0112  54  ASN   B N   
4801 C CA  . ASN   B 54  ? 0.1566 0.1637 0.1878 -0.0022 -0.0025 0.0008  54  ASN   B CA  
4802 C C   . ASN   B 54  ? 0.1519 0.1647 0.2135 -0.0015 -0.0073 -0.0006 54  ASN   B C   
4803 O O   . ASN   B 54  ? 0.1529 0.1727 0.2099 -0.0084 0.0007  0.0024  54  ASN   B O   
4804 C CB  . ASN   B 54  ? 0.1665 0.1775 0.2064 0.0057  -0.0027 -0.0022 54  ASN   B CB  
4805 C CG  . ASN   B 54  ? 0.1637 0.1833 0.2059 0.0043  -0.0171 -0.0013 54  ASN   B CG  
4806 O OD1 . ASN   B 54  ? 0.1639 0.1782 0.2266 0.0035  -0.0231 -0.0110 54  ASN   B OD1 
4807 N ND2 . ASN   B 54  ? 0.1888 0.2043 0.2310 -0.0085 -0.0352 0.0121  54  ASN   B ND2 
4814 N N   . LYS   B 55  ? 0.1531 0.1640 0.2451 0.0032  0.0004  0.0008  55  LYS   B N   
4815 C CA  . LYS   B 55  ? 0.1565 0.1811 0.2615 0.0091  -0.0068 0.0001  55  LYS   B CA  
4816 C C   . LYS   B 55  ? 0.1516 0.1764 0.2577 0.0060  0.0041  -0.0047 55  LYS   B C   
4817 O O   . LYS   B 55  ? 0.1470 0.1922 0.2575 0.0091  0.0020  -0.0098 55  LYS   B O   
4818 C CB  . LYS   B 55  ? 0.1787 0.1960 0.3126 0.0287  0.0010  0.0057  55  LYS   B CB  
4819 C CG  . LYS   B 55  ? 0.2327 0.2394 0.3853 0.0312  0.0188  0.0204  55  LYS   B CG  
4820 C CD  . LYS   B 55  ? 0.2784 0.2788 0.4430 0.0394  0.0397  0.0414  55  LYS   B CD  
4821 C CE  . LYS   B 55  ? 0.3111 0.3113 0.5040 0.0399  0.0525  0.0507  55  LYS   B CE  
4822 N NZ  . LYS   B 55  ? 0.3205 0.3311 0.5358 0.0358  0.0387  0.0643  55  LYS   B NZ  
4836 N N   . ALA   B 56  ? 0.1536 0.1709 0.2467 -0.0037 -0.0008 0.0003  56  ALA   B N   
4837 C CA  . ALA   B 56  ? 0.1715 0.1903 0.2383 -0.0074 0.0067  0.0005  56  ALA   B CA  
4838 C C   . ALA   B 56  ? 0.1711 0.1890 0.2259 -0.0050 0.0111  0.0039  56  ALA   B C   
4839 O O   . ALA   B 56  ? 0.1884 0.1996 0.2329 0.0036  0.0303  0.0102  56  ALA   B O   
4840 C CB  . ALA   B 56  ? 0.1794 0.2130 0.2292 -0.0069 0.0090  0.0039  56  ALA   B CB  
4846 N N   . THR   B 57  ? 0.1656 0.1749 0.2310 -0.0026 0.0219  0.0005  57  THR   B N   
4847 C CA  . THR   B 57  ? 0.1726 0.1780 0.2322 -0.0036 0.0164  0.0087  57  THR   B CA  
4848 C C   . THR   B 57  ? 0.1659 0.1940 0.2499 -0.0048 0.0269  0.0074  57  THR   B C   
4849 O O   . THR   B 57  ? 0.1767 0.1903 0.2495 -0.0257 0.0140  0.0066  57  THR   B O   
4850 C CB  . THR   B 57  ? 0.1815 0.1681 0.2156 -0.0006 0.0052  0.0098  57  THR   B CB  
4851 O OG1 . THR   B 57  ? 0.1797 0.1617 0.2239 -0.0025 0.0035  -0.0010 57  THR   B OG1 
4852 C CG2 . THR   B 57  ? 0.1755 0.1608 0.2185 -0.0062 0.0054  -0.0057 57  THR   B CG2 
4860 N N   A ASN   B 58  ? 0.1578 0.2094 0.2621 -0.0153 0.0202  -0.0059 58  ASN   B N   
4861 N N   B ASN   B 58  ? 0.1534 0.2073 0.2598 -0.0145 0.0214  -0.0056 58  ASN   B N   
4862 C CA  A ASN   B 58  ? 0.1789 0.2357 0.2939 -0.0231 0.0144  -0.0042 58  ASN   B CA  
4863 C CA  B ASN   B 58  ? 0.1737 0.2327 0.2907 -0.0208 0.0181  -0.0021 58  ASN   B CA  
4864 C C   A ASN   B 58  ? 0.1627 0.2293 0.2765 -0.0202 -0.0091 -0.0080 58  ASN   B C   
4865 C C   B ASN   B 58  ? 0.1595 0.2268 0.2770 -0.0180 -0.0092 -0.0062 58  ASN   B C   
4866 O O   A ASN   B 58  ? 0.1670 0.2402 0.2855 -0.0241 -0.0004 -0.0166 58  ASN   B O   
4867 O O   B ASN   B 58  ? 0.1642 0.2364 0.2902 -0.0196 -0.0020 -0.0131 58  ASN   B O   
4868 C CB  A ASN   B 58  ? 0.2365 0.2751 0.3627 -0.0313 0.0227  0.0045  58  ASN   B CB  
4869 C CB  B ASN   B 58  ? 0.2329 0.2728 0.3585 -0.0274 0.0303  0.0072  58  ASN   B CB  
4870 C CG  A ASN   B 58  ? 0.2968 0.3111 0.4529 -0.0282 0.0246  0.0178  58  ASN   B CG  
4871 C CG  B ASN   B 58  ? 0.2966 0.3098 0.4531 -0.0244 0.0310  0.0232  58  ASN   B CG  
4872 O OD1 A ASN   B 58  ? 0.3217 0.3283 0.4922 -0.0252 0.0219  0.0204  58  ASN   B OD1 
4873 O OD1 B ASN   B 58  ? 0.3234 0.3283 0.4938 -0.0203 0.0268  0.0263  58  ASN   B OD1 
4874 N ND2 A ASN   B 58  ? 0.3134 0.3290 0.4847 -0.0298 0.0291  0.0187  58  ASN   B ND2 
4875 N ND2 B ASN   B 58  ? 0.3138 0.3280 0.4863 -0.0253 0.0350  0.0258  58  ASN   B ND2 
4888 N N   . ASN   B 59  ? 0.1522 0.2162 0.2610 -0.0138 -0.0162 0.0058  59  ASN   B N   
4889 C CA  . ASN   B 59  ? 0.1555 0.2176 0.2468 -0.0185 -0.0216 0.0102  59  ASN   B CA  
4890 C C   . ASN   B 59  ? 0.1503 0.2067 0.2308 -0.0198 -0.0136 -0.0056 59  ASN   B C   
4891 O O   . ASN   B 59  ? 0.1625 0.2145 0.2184 -0.0113 -0.0123 -0.0036 59  ASN   B O   
4892 C CB  . ASN   B 59  ? 0.1681 0.2371 0.2468 -0.0149 -0.0352 0.0065  59  ASN   B CB  
4893 C CG  . ASN   B 59  ? 0.1826 0.2492 0.2549 -0.0087 -0.0472 -0.0031 59  ASN   B CG  
4894 O OD1 . ASN   B 59  ? 0.1884 0.2608 0.2592 -0.0137 -0.0377 0.0158  59  ASN   B OD1 
4895 N ND2 . ASN   B 59  ? 0.1930 0.2562 0.2679 -0.0116 -0.0466 -0.0102 59  ASN   B ND2 
4903 N N   . ALA   B 60  ? 0.1593 0.1991 0.2256 -0.0179 0.0022  0.0011  60  ALA   B N   
4904 C CA  . ALA   B 60  ? 0.1734 0.1924 0.2342 -0.0279 -0.0023 0.0055  60  ALA   B CA  
4905 C C   . ALA   B 60  ? 0.1779 0.1749 0.2112 -0.0256 -0.0100 -0.0087 60  ALA   B C   
4906 O O   . ALA   B 60  ? 0.1785 0.1740 0.2221 -0.0284 0.0048  -0.0134 60  ALA   B O   
4907 C CB  . ALA   B 60  ? 0.1878 0.1957 0.2616 -0.0311 0.0089  0.0110  60  ALA   B CB  
4913 N N   . MET   B 61  ? 0.1624 0.1624 0.2133 -0.0201 -0.0132 -0.0017 61  MET   B N   
4914 C CA  . MET   B 61  ? 0.1546 0.1601 0.2072 -0.0123 -0.0181 -0.0046 61  MET   B CA  
4915 C C   . MET   B 61  ? 0.1644 0.1625 0.2066 -0.0102 -0.0145 0.0059  61  MET   B C   
4916 O O   . MET   B 61  ? 0.1667 0.1613 0.1804 -0.0087 -0.0167 -0.0098 61  MET   B O   
4917 C CB  . MET   B 61  ? 0.1563 0.1605 0.2107 -0.0057 -0.0180 0.0026  61  MET   B CB  
4918 C CG  . MET   B 61  ? 0.1576 0.1669 0.2009 -0.0041 -0.0155 0.0011  61  MET   B CG  
4919 S SD  . MET   B 61  ? 0.1653 0.1718 0.2180 -0.0119 -0.0086 -0.0112 61  MET   B SD  
4920 C CE  . MET   B 61  ? 0.1806 0.1940 0.2330 -0.0003 -0.0155 -0.0221 61  MET   B CE  
4930 N N   . GLN   B 62  ? 0.1600 0.1644 0.1937 -0.0060 -0.0223 0.0018  62  GLN   B N   
4931 C CA  . GLN   B 62  ? 0.1636 0.1720 0.2134 -0.0064 -0.0325 0.0028  62  GLN   B CA  
4932 C C   . GLN   B 62  ? 0.1612 0.1725 0.2072 -0.0060 -0.0315 0.0029  62  GLN   B C   
4933 O O   . GLN   B 62  ? 0.1736 0.1777 0.2061 -0.0064 -0.0299 -0.0112 62  GLN   B O   
4934 C CB  . GLN   B 62  ? 0.1704 0.1770 0.2033 0.0003  -0.0307 0.0109  62  GLN   B CB  
4935 C CG  . GLN   B 62  ? 0.1815 0.1788 0.2072 -0.0054 -0.0359 0.0013  62  GLN   B CG  
4936 C CD  . GLN   B 62  ? 0.1832 0.1759 0.1892 0.0003  -0.0312 0.0126  62  GLN   B CD  
4937 O OE1 . GLN   B 62  ? 0.1799 0.1773 0.2216 -0.0041 -0.0206 -0.0050 62  GLN   B OE1 
4938 N NE2 . GLN   B 62  ? 0.1809 0.1762 0.1898 -0.0008 -0.0227 -0.0090 62  GLN   B NE2 
4947 N N   . VAL   B 63  ? 0.1659 0.1730 0.2113 -0.0146 -0.0248 -0.0047 63  VAL   B N   
4948 C CA  . VAL   B 63  ? 0.1860 0.1794 0.2375 -0.0164 -0.0264 -0.0089 63  VAL   B CA  
4949 C C   . VAL   B 63  ? 0.1885 0.1659 0.2132 -0.0279 -0.0287 -0.0175 63  VAL   B C   
4950 O O   . VAL   B 63  ? 0.2037 0.1685 0.2192 -0.0210 -0.0419 -0.0152 63  VAL   B O   
4951 C CB  . VAL   B 63  ? 0.1852 0.2029 0.2834 -0.0266 -0.0280 -0.0132 63  VAL   B CB  
4952 C CG1 . VAL   B 63  ? 0.1929 0.2022 0.2829 -0.0364 -0.0124 -0.0179 63  VAL   B CG1 
4953 C CG2 . VAL   B 63  ? 0.1790 0.2230 0.3003 -0.0214 -0.0311 -0.0154 63  VAL   B CG2 
4963 N N   . GLU   B 64  ? 0.1828 0.1649 0.2125 -0.0210 -0.0240 -0.0147 64  GLU   B N   
4964 C CA  . GLU   B 64  ? 0.1836 0.1547 0.2188 -0.0168 -0.0247 -0.0152 64  GLU   B CA  
4965 C C   . GLU   B 64  ? 0.1782 0.1545 0.1991 -0.0083 -0.0338 -0.0171 64  GLU   B C   
4966 O O   . GLU   B 64  ? 0.1895 0.1626 0.1899 -0.0124 -0.0252 -0.0209 64  GLU   B O   
4967 C CB  . GLU   B 64  ? 0.1841 0.1670 0.2212 -0.0229 -0.0221 -0.0184 64  GLU   B CB  
4968 C CG  . GLU   B 64  ? 0.1971 0.1768 0.2226 -0.0266 -0.0277 -0.0283 64  GLU   B CG  
4969 C CD  . GLU   B 64  ? 0.1968 0.1950 0.2517 -0.0341 -0.0318 -0.0192 64  GLU   B CD  
4970 O OE1 . GLU   B 64  ? 0.2013 0.2074 0.2620 -0.0294 -0.0247 -0.0196 64  GLU   B OE1 
4971 O OE2 . GLU   B 64  ? 0.2120 0.2053 0.2472 -0.0332 -0.0414 -0.0085 64  GLU   B OE2 
4978 N N   . SER   B 65  ? 0.1765 0.1515 0.1761 -0.0102 -0.0198 -0.0157 65  SER   B N   
4979 C CA  . SER   B 65  ? 0.1825 0.1534 0.1896 -0.0008 -0.0224 -0.0226 65  SER   B CA  
4980 C C   . SER   B 65  ? 0.1818 0.1668 0.1944 -0.0067 -0.0229 -0.0201 65  SER   B C   
4981 O O   . SER   B 65  ? 0.1834 0.1728 0.1899 -0.0063 -0.0133 -0.0275 65  SER   B O   
4982 C CB  . SER   B 65  ? 0.1788 0.1581 0.1858 -0.0153 -0.0226 -0.0087 65  SER   B CB  
4983 O OG  . SER   B 65  ? 0.1853 0.1551 0.1925 -0.0103 -0.0173 -0.0213 65  SER   B OG  
4989 N N   . ASP   B 66  ? 0.1882 0.1676 0.1849 -0.0059 -0.0336 -0.0197 66  ASP   B N   
4990 C CA  . ASP   B 66  ? 0.1979 0.1713 0.1861 -0.0016 -0.0352 -0.0124 66  ASP   B CA  
4991 C C   . ASP   B 66  ? 0.2003 0.1731 0.1803 -0.0056 -0.0260 -0.0180 66  ASP   B C   
4992 O O   . ASP   B 66  ? 0.2077 0.1792 0.1895 0.0050  -0.0283 -0.0228 66  ASP   B O   
4993 C CB  . ASP   B 66  ? 0.2178 0.1890 0.2188 0.0134  -0.0564 -0.0204 66  ASP   B CB  
4994 C CG  . ASP   B 66  ? 0.2550 0.2128 0.2483 0.0206  -0.0679 -0.0020 66  ASP   B CG  
4995 O OD1 . ASP   B 66  ? 0.2787 0.2102 0.2554 0.0099  -0.0625 0.0070  66  ASP   B OD1 
4996 O OD2 . ASP   B 66  ? 0.2770 0.2410 0.3123 0.0398  -0.0654 0.0046  66  ASP   B OD2 
5001 N N   . ASP   B 67  ? 0.1962 0.1627 0.1824 -0.0075 -0.0350 -0.0166 67  ASP   B N   
5002 C CA  . ASP   B 67  ? 0.2143 0.1601 0.2115 -0.0104 -0.0350 -0.0104 67  ASP   B CA  
5003 C C   . ASP   B 67  ? 0.2106 0.1632 0.2242 -0.0045 -0.0383 -0.0236 67  ASP   B C   
5004 O O   . ASP   B 67  ? 0.2136 0.1715 0.2250 -0.0056 -0.0328 -0.0325 67  ASP   B O   
5005 C CB  . ASP   B 67  ? 0.2355 0.1675 0.2452 -0.0144 -0.0415 -0.0067 67  ASP   B CB  
5006 C CG  . ASP   B 67  ? 0.2755 0.1797 0.2496 -0.0177 -0.0637 -0.0088 67  ASP   B CG  
5007 O OD1 . ASP   B 67  ? 0.2974 0.1817 0.2702 -0.0104 -0.0761 -0.0108 67  ASP   B OD1 
5008 O OD2 . ASP   B 67  ? 0.2894 0.2012 0.2736 -0.0024 -0.0753 0.0012  67  ASP   B OD2 
5013 N N   . TYR   B 68  ? 0.2036 0.1624 0.2145 0.0024  -0.0446 -0.0303 68  TYR   B N   
5014 C CA  . TYR   B 68  ? 0.1989 0.1853 0.2270 0.0058  -0.0465 -0.0272 68  TYR   B CA  
5015 C C   . TYR   B 68  ? 0.1951 0.1753 0.2131 -0.0007 -0.0342 -0.0376 68  TYR   B C   
5016 O O   . TYR   B 68  ? 0.2009 0.1847 0.2178 0.0081  -0.0340 -0.0485 68  TYR   B O   
5017 C CB  . TYR   B 68  ? 0.2033 0.2146 0.2239 0.0109  -0.0543 -0.0471 68  TYR   B CB  
5018 C CG  . TYR   B 68  ? 0.2112 0.2438 0.2308 0.0138  -0.0460 -0.0720 68  TYR   B CG  
5019 C CD1 . TYR   B 68  ? 0.2178 0.2530 0.2587 -0.0090 -0.0401 -0.0881 68  TYR   B CD1 
5020 C CD2 . TYR   B 68  ? 0.2151 0.2648 0.2522 0.0207  -0.0692 -0.0719 68  TYR   B CD2 
5021 C CE1 . TYR   B 68  ? 0.2214 0.2765 0.2952 -0.0050 -0.0263 -0.0892 68  TYR   B CE1 
5022 C CE2 . TYR   B 68  ? 0.2159 0.2788 0.2819 0.0187  -0.0515 -0.0852 68  TYR   B CE2 
5023 C CZ  . TYR   B 68  ? 0.2104 0.2849 0.3012 -0.0006 -0.0398 -0.0942 68  TYR   B CZ  
5024 O OH  . TYR   B 68  ? 0.2097 0.3095 0.3500 -0.0081 -0.0255 -0.0768 68  TYR   B OH  
5034 N N   . ILE   B 69  ? 0.1885 0.1710 0.2109 -0.0020 -0.0419 -0.0359 69  ILE   B N   
5035 C CA  . ILE   B 69  ? 0.1960 0.1718 0.2252 -0.0073 -0.0221 -0.0439 69  ILE   B CA  
5036 C C   . ILE   B 69  ? 0.1913 0.1734 0.2161 0.0042  -0.0285 -0.0328 69  ILE   B C   
5037 O O   . ILE   B 69  ? 0.2002 0.1901 0.1973 0.0026  -0.0218 -0.0339 69  ILE   B O   
5038 C CB  . ILE   B 69  ? 0.2135 0.1781 0.2438 -0.0055 0.0089  -0.0387 69  ILE   B CB  
5039 C CG1 . ILE   B 69  ? 0.2078 0.1822 0.2633 -0.0046 0.0148  -0.0440 69  ILE   B CG1 
5040 C CG2 . ILE   B 69  ? 0.2349 0.1934 0.2535 -0.0079 -0.0003 -0.0259 69  ILE   B CG2 
5041 C CD1 . ILE   B 69  ? 0.2109 0.1901 0.2729 -0.0110 0.0265  -0.0477 69  ILE   B CD1 
5053 N N   . ALA   B 70  ? 0.1944 0.1782 0.2253 0.0001  -0.0362 -0.0346 70  ALA   B N   
5054 C CA  . ALA   B 70  ? 0.1961 0.1759 0.2052 0.0045  -0.0347 -0.0305 70  ALA   B CA  
5055 C C   . ALA   B 70  ? 0.2060 0.1760 0.2269 0.0033  -0.0403 -0.0392 70  ALA   B C   
5056 O O   . ALA   B 70  ? 0.2186 0.1755 0.2302 0.0074  -0.0349 -0.0371 70  ALA   B O   
5057 C CB  . ALA   B 70  ? 0.2022 0.1945 0.2091 0.0074  -0.0417 -0.0296 70  ALA   B CB  
5063 N N   . THR   B 71  ? 0.2107 0.1776 0.2257 0.0051  -0.0560 -0.0352 71  THR   B N   
5064 C CA  . THR   B 71  ? 0.2180 0.1817 0.2433 0.0070  -0.0660 -0.0337 71  THR   B CA  
5065 C C   . THR   B 71  ? 0.2114 0.1855 0.2640 0.0262  -0.0634 -0.0595 71  THR   B C   
5066 O O   . THR   B 71  ? 0.2201 0.1977 0.3013 0.0311  -0.0528 -0.0653 71  THR   B O   
5067 C CB  . THR   B 71  ? 0.2410 0.2023 0.2675 -0.0039 -0.0693 -0.0064 71  THR   B CB  
5068 O OG1 . THR   B 71  ? 0.2621 0.2336 0.3066 -0.0233 -0.0784 0.0178  71  THR   B OG1 
5069 C CG2 . THR   B 71  ? 0.2595 0.2001 0.2852 0.0029  -0.0512 -0.0013 71  THR   B CG2 
5077 N N   . ASN   B 72  ? 0.2069 0.1883 0.2737 0.0149  -0.0679 -0.0698 72  ASN   B N   
5078 C CA  . ASN   B 72  ? 0.2054 0.2064 0.2791 0.0101  -0.0528 -0.0752 72  ASN   B CA  
5079 C C   . ASN   B 72  ? 0.2058 0.2186 0.2864 -0.0050 -0.0330 -0.0719 72  ASN   B C   
5080 O O   . ASN   B 72  ? 0.2044 0.2418 0.3189 -0.0006 -0.0090 -0.0788 72  ASN   B O   
5081 C CB  . ASN   B 72  ? 0.2100 0.2225 0.2800 0.0105  -0.0586 -0.0599 72  ASN   B CB  
5082 C CG  . ASN   B 72  ? 0.2292 0.2390 0.2678 0.0252  -0.0554 -0.0411 72  ASN   B CG  
5083 O OD1 . ASN   B 72  ? 0.2564 0.2622 0.2677 0.0203  -0.0480 -0.0431 72  ASN   B OD1 
5084 N ND2 . ASN   B 72  ? 0.2337 0.2483 0.3123 0.0444  -0.0600 -0.0076 72  ASN   B ND2 
5091 N N   . GLY   B 73  ? 0.2135 0.2154 0.2590 -0.0060 -0.0398 -0.0708 73  GLY   B N   
5092 C CA  . GLY   B 73  ? 0.2104 0.2227 0.2398 -0.0029 -0.0295 -0.0512 73  GLY   B CA  
5093 C C   . GLY   B 73  ? 0.2026 0.2206 0.2117 0.0004  -0.0243 -0.0384 73  GLY   B C   
5094 O O   . GLY   B 73  ? 0.1954 0.2060 0.2210 -0.0015 -0.0135 -0.0329 73  GLY   B O   
5098 N N   . PRO   B 74  ? 0.2014 0.2302 0.1899 -0.0060 -0.0241 -0.0336 74  PRO   B N   
5099 C CA  . PRO   B 74  ? 0.1936 0.2272 0.1675 -0.0009 -0.0282 -0.0169 74  PRO   B CA  
5100 C C   . PRO   B 74  ? 0.1829 0.2111 0.1905 -0.0003 -0.0177 -0.0121 74  PRO   B C   
5101 O O   . PRO   B 74  ? 0.1845 0.2177 0.2296 -0.0056 -0.0122 -0.0271 74  PRO   B O   
5102 C CB  . PRO   B 74  ? 0.2159 0.2523 0.1793 -0.0065 -0.0250 -0.0197 74  PRO   B CB  
5103 C CG  . PRO   B 74  ? 0.2373 0.2679 0.2169 -0.0062 -0.0181 -0.0149 74  PRO   B CG  
5104 C CD  . PRO   B 74  ? 0.2337 0.2550 0.1968 -0.0033 -0.0184 -0.0239 74  PRO   B CD  
5112 N N   . LEU   B 75  ? 0.1755 0.1930 0.1735 -0.0002 -0.0211 -0.0157 75  LEU   B N   
5113 C CA  . LEU   B 75  ? 0.1832 0.1980 0.1658 -0.0034 -0.0216 -0.0037 75  LEU   B CA  
5114 C C   . LEU   B 75  ? 0.1888 0.2037 0.1643 0.0033  -0.0080 -0.0013 75  LEU   B C   
5115 O O   . LEU   B 75  ? 0.2027 0.2183 0.1838 -0.0024 -0.0083 -0.0043 75  LEU   B O   
5116 C CB  . LEU   B 75  ? 0.1931 0.2039 0.1604 -0.0131 -0.0243 0.0212  75  LEU   B CB  
5117 C CG  . LEU   B 75  ? 0.2249 0.2153 0.1982 -0.0345 -0.0212 0.0143  75  LEU   B CG  
5118 C CD1 . LEU   B 75  ? 0.2542 0.2347 0.2076 -0.0469 0.0044  0.0037  75  LEU   B CD1 
5119 C CD2 . LEU   B 75  ? 0.2692 0.2440 0.2795 -0.0196 -0.0040 0.0252  75  LEU   B CD2 
5131 N N   . LYS   B 76  ? 0.1847 0.2285 0.2013 -0.0066 -0.0055 0.0165  76  LYS   B N   
5132 C CA  . LYS   B 76  ? 0.1981 0.2273 0.2191 -0.0143 0.0102  0.0133  76  LYS   B CA  
5133 C C   . LYS   B 76  ? 0.1906 0.2095 0.1940 0.0002  0.0050  0.0348  76  LYS   B C   
5134 O O   . LYS   B 76  ? 0.1949 0.1920 0.2015 -0.0020 0.0043  0.0293  76  LYS   B O   
5135 C CB  . LYS   B 76  ? 0.2093 0.2342 0.2766 -0.0198 0.0292  -0.0159 76  LYS   B CB  
5136 C CG  . LYS   B 76  ? 0.2153 0.2530 0.3058 -0.0092 0.0175  -0.0225 76  LYS   B CG  
5137 C CD  . LYS   B 76  ? 0.2139 0.2624 0.3501 -0.0059 0.0106  -0.0319 76  LYS   B CD  
5138 C CE  . LYS   B 76  ? 0.2270 0.2845 0.4026 -0.0001 -0.0007 -0.0406 76  LYS   B CE  
5139 N NZ  . LYS   B 76  ? 0.2336 0.2936 0.4202 0.0002  -0.0248 -0.0601 76  LYS   B NZ  
5153 N N   . VAL   B 77  ? 0.1966 0.2220 0.2054 0.0033  0.0126  0.0362  77  VAL   B N   
5154 C CA  . VAL   B 77  ? 0.1974 0.2120 0.2212 0.0001  0.0090  0.0643  77  VAL   B CA  
5155 C C   . VAL   B 77  ? 0.1811 0.1955 0.2117 0.0030  0.0265  0.0538  77  VAL   B C   
5156 O O   . VAL   B 77  ? 0.1810 0.2009 0.2236 0.0132  0.0342  0.0387  77  VAL   B O   
5157 C CB  . VAL   B 77  ? 0.2095 0.2235 0.2756 0.0042  0.0163  0.0680  77  VAL   B CB  
5158 C CG1 . VAL   B 77  ? 0.2163 0.2187 0.3002 0.0028  0.0239  0.0763  77  VAL   B CG1 
5159 C CG2 . VAL   B 77  ? 0.2222 0.2433 0.2893 -0.0067 -0.0071 0.0709  77  VAL   B CG2 
5169 N N   . GLY   B 78  ? 0.1773 0.1815 0.1920 0.0013  0.0167  0.0399  78  GLY   B N   
5170 C CA  . GLY   B 78  ? 0.1792 0.1825 0.1930 0.0073  0.0288  0.0289  78  GLY   B CA  
5171 C C   . GLY   B 78  ? 0.1757 0.1748 0.1897 0.0174  0.0161  0.0304  78  GLY   B C   
5172 O O   . GLY   B 78  ? 0.1737 0.1759 0.2183 0.0179  0.0062  0.0284  78  GLY   B O   
5176 N N   . GLY   B 79  ? 0.1628 0.1765 0.2018 0.0050  0.0192  0.0251  79  GLY   B N   
5177 C CA  . GLY   B 79  ? 0.1637 0.1693 0.1988 0.0082  0.0009  0.0245  79  GLY   B CA  
5178 C C   . GLY   B 79  ? 0.1570 0.1609 0.1897 0.0116  0.0031  0.0162  79  GLY   B C   
5179 O O   . GLY   B 79  ? 0.1709 0.1591 0.1926 0.0111  0.0158  0.0290  79  GLY   B O   
5183 N N   . SER   B 80  ? 0.1579 0.1528 0.1927 0.0119  0.0227  0.0149  80  SER   B N   
5184 C CA  . SER   B 80  ? 0.1493 0.1511 0.2088 0.0039  0.0008  0.0109  80  SER   B CA  
5185 C C   . SER   B 80  ? 0.1556 0.1469 0.1969 0.0045  0.0031  0.0073  80  SER   B C   
5186 O O   . SER   B 80  ? 0.1746 0.1545 0.2123 0.0092  0.0044  0.0036  80  SER   B O   
5187 C CB  . SER   B 80  ? 0.1524 0.1567 0.2053 0.0006  -0.0032 0.0073  80  SER   B CB  
5188 O OG  . SER   B 80  ? 0.1660 0.1728 0.2274 -0.0035 -0.0072 0.0070  80  SER   B OG  
5194 N N   . CYS   B 81  ? 0.1530 0.1380 0.1917 0.0021  -0.0042 0.0093  81  CYS   B N   
5195 C CA  . CYS   B 81  ? 0.1595 0.1317 0.1898 0.0019  -0.0088 -0.0000 81  CYS   B CA  
5196 C C   . CYS   B 81  ? 0.1560 0.1327 0.1666 0.0014  -0.0088 0.0003  81  CYS   B C   
5197 O O   . CYS   B 81  ? 0.1826 0.1345 0.1862 0.0055  0.0003  0.0025  81  CYS   B O   
5198 C CB  . CYS   B 81  ? 0.1778 0.1582 0.2087 -0.0043 -0.0161 -0.0103 81  CYS   B CB  
5199 S SG  . CYS   B 81  ? 0.1794 0.1772 0.1952 -0.0062 -0.0273 -0.0088 81  CYS   B SG  
5205 N N   . VAL   B 82  ? 0.1604 0.1322 0.1917 -0.0002 -0.0090 -0.0072 82  VAL   B N   
5206 C CA  . VAL   B 82  ? 0.1676 0.1351 0.1896 -0.0086 -0.0115 0.0047  82  VAL   B CA  
5207 C C   . VAL   B 82  ? 0.1782 0.1362 0.1899 -0.0040 -0.0035 0.0001  82  VAL   B C   
5208 O O   . VAL   B 82  ? 0.1863 0.1353 0.2252 -0.0031 -0.0041 -0.0171 82  VAL   B O   
5209 C CB  . VAL   B 82  ? 0.1673 0.1661 0.2041 -0.0026 -0.0127 0.0068  82  VAL   B CB  
5210 C CG1 . VAL   B 82  ? 0.1896 0.2041 0.2103 0.0090  -0.0066 0.0236  82  VAL   B CG1 
5211 C CG2 . VAL   B 82  ? 0.1840 0.1821 0.2254 -0.0089 -0.0237 0.0167  82  VAL   B CG2 
5221 N N   . LEU   B 83  ? 0.1670 0.1326 0.1984 -0.0153 -0.0276 -0.0111 83  LEU   B N   
5222 C CA  . LEU   B 83  ? 0.1662 0.1401 0.1835 -0.0133 -0.0162 -0.0040 83  LEU   B CA  
5223 C C   . LEU   B 83  ? 0.1655 0.1455 0.1863 -0.0253 -0.0161 0.0018  83  LEU   B C   
5224 O O   . LEU   B 83  ? 0.1714 0.1497 0.1690 -0.0244 -0.0193 0.0029  83  LEU   B O   
5225 C CB  . LEU   B 83  ? 0.1757 0.1474 0.1917 -0.0125 -0.0200 -0.0007 83  LEU   B CB  
5226 C CG  . LEU   B 83  ? 0.1972 0.1743 0.1931 -0.0202 -0.0115 -0.0030 83  LEU   B CG  
5227 C CD1 . LEU   B 83  ? 0.2191 0.1771 0.2075 -0.0126 -0.0205 0.0025  83  LEU   B CD1 
5228 C CD2 . LEU   B 83  ? 0.2247 0.1847 0.2130 -0.0176 -0.0269 -0.0149 83  LEU   B CD2 
5240 N N   . SER   B 84  ? 0.1734 0.1488 0.2038 -0.0282 -0.0247 0.0039  84  SER   B N   
5241 C CA  . SER   B 84  ? 0.1731 0.1724 0.1932 -0.0289 -0.0064 0.0211  84  SER   B CA  
5242 C C   . SER   B 84  ? 0.1617 0.1914 0.1398 -0.0242 -0.0124 0.0173  84  SER   B C   
5243 O O   . SER   B 84  ? 0.1746 0.1827 0.1471 -0.0195 -0.0069 0.0036  84  SER   B O   
5244 C CB  . SER   B 84  ? 0.1918 0.1815 0.2331 -0.0323 0.0118  0.0063  84  SER   B CB  
5245 O OG  . SER   B 84  ? 0.1873 0.1961 0.2765 -0.0413 0.0098  0.0185  84  SER   B OG  
5251 N N   . GLY   B 85  ? 0.1678 0.2062 0.1464 -0.0259 -0.0204 0.0307  85  GLY   B N   
5252 C CA  . GLY   B 85  ? 0.1672 0.2106 0.1956 -0.0307 0.0045  -0.0054 85  GLY   B CA  
5253 C C   . GLY   B 85  ? 0.1611 0.1937 0.1765 -0.0395 0.0009  0.0092  85  GLY   B C   
5254 O O   . GLY   B 85  ? 0.1694 0.1952 0.1858 -0.0489 0.0122  -0.0048 85  GLY   B O   
5258 N N   . HIS   B 86  ? 0.1687 0.1798 0.1865 -0.0394 -0.0173 0.0178  86  HIS   B N   
5259 C CA  . HIS   B 86  ? 0.1680 0.1818 0.1971 -0.0325 -0.0197 0.0124  86  HIS   B CA  
5260 C C   . HIS   B 86  ? 0.1708 0.1935 0.1861 -0.0388 -0.0128 0.0290  86  HIS   B C   
5261 O O   . HIS   B 86  ? 0.1799 0.2106 0.1887 -0.0291 0.0056  0.0320  86  HIS   B O   
5262 C CB  . HIS   B 86  ? 0.1795 0.1995 0.1969 -0.0196 -0.0320 0.0036  86  HIS   B CB  
5263 C CG  . HIS   B 86  ? 0.1849 0.2132 0.1933 -0.0097 -0.0351 0.0013  86  HIS   B CG  
5264 N ND1 . HIS   B 86  ? 0.2005 0.2392 0.2291 -0.0215 -0.0294 -0.0264 86  HIS   B ND1 
5265 C CD2 . HIS   B 86  ? 0.1858 0.2092 0.2087 0.0023  -0.0287 -0.0012 86  HIS   B CD2 
5266 C CE1 . HIS   B 86  ? 0.2123 0.2335 0.2224 -0.0115 -0.0160 -0.0452 86  HIS   B CE1 
5267 N NE2 . HIS   B 86  ? 0.2013 0.2232 0.2090 0.0053  -0.0208 -0.0140 86  HIS   B NE2 
5275 N N   . ASN   B 87  ? 0.1722 0.1946 0.2039 -0.0280 -0.0008 0.0209  87  ASN   B N   
5276 C CA  . ASN   B 87  ? 0.1831 0.2132 0.2035 -0.0279 0.0211  0.0220  87  ASN   B CA  
5277 C C   . ASN   B 87  ? 0.1979 0.1953 0.2021 -0.0222 0.0206  0.0153  87  ASN   B C   
5278 O O   . ASN   B 87  ? 0.2271 0.2139 0.2310 -0.0146 0.0444  0.0119  87  ASN   B O   
5279 C CB  . ASN   B 87  ? 0.1905 0.2516 0.2349 -0.0217 0.0192  0.0118  87  ASN   B CB  
5280 C CG  . ASN   B 87  ? 0.1980 0.2738 0.2225 0.0164  0.0183  0.0300  87  ASN   B CG  
5281 O OD1 . ASN   B 87  ? 0.1968 0.2617 0.2191 0.0175  0.0421  0.0432  87  ASN   B OD1 
5282 N ND2 . ASN   B 87  ? 0.2279 0.2859 0.2693 0.0190  0.0221  0.0239  87  ASN   B ND2 
5289 N N   . LEU   B 88  ? 0.1832 0.1842 0.1777 -0.0281 0.0145  0.0061  88  LEU   B N   
5290 C CA  . LEU   B 88  ? 0.1953 0.1805 0.1754 -0.0318 0.0096  -0.0078 88  LEU   B CA  
5291 C C   . LEU   B 88  ? 0.1939 0.1715 0.1864 -0.0389 -0.0095 0.0044  88  LEU   B C   
5292 O O   . LEU   B 88  ? 0.2227 0.1808 0.2252 -0.0175 -0.0410 -0.0081 88  LEU   B O   
5293 C CB  . LEU   B 88  ? 0.2188 0.1890 0.1910 -0.0433 -0.0026 0.0073  88  LEU   B CB  
5294 C CG  . LEU   B 88  ? 0.2664 0.2238 0.2273 -0.0388 -0.0196 0.0177  88  LEU   B CG  
5295 C CD1 . LEU   B 88  ? 0.2751 0.2571 0.2541 -0.0527 -0.0194 0.0335  88  LEU   B CD1 
5296 C CD2 . LEU   B 88  ? 0.3058 0.2529 0.2716 -0.0018 -0.0486 0.0026  88  LEU   B CD2 
5308 N N   . ALA   B 89  ? 0.1819 0.1672 0.1646 -0.0390 0.0162  0.0034  89  ALA   B N   
5309 C CA  . ALA   B 89  ? 0.1781 0.1644 0.1519 -0.0305 0.0041  0.0128  89  ALA   B CA  
5310 C C   . ALA   B 89  ? 0.1882 0.1676 0.1652 -0.0351 0.0081  0.0033  89  ALA   B C   
5311 O O   . ALA   B 89  ? 0.1676 0.1795 0.2038 -0.0398 0.0152  -0.0218 89  ALA   B O   
5312 C CB  . ALA   B 89  ? 0.1661 0.1651 0.1735 -0.0334 0.0093  0.0205  89  ALA   B CB  
5318 N N   . LYS   B 90  ? 0.2220 0.1524 0.1777 -0.0395 -0.0165 0.0195  90  LYS   B N   
5319 C CA  . LYS   B 90  ? 0.2353 0.1519 0.1625 -0.0420 -0.0175 0.0163  90  LYS   B CA  
5320 C C   . LYS   B 90  ? 0.2137 0.1419 0.1813 -0.0401 -0.0183 0.0077  90  LYS   B C   
5321 O O   . LYS   B 90  ? 0.2209 0.1616 0.1913 -0.0511 -0.0103 0.0058  90  LYS   B O   
5322 C CB  . LYS   B 90  ? 0.2640 0.1581 0.2032 -0.0357 -0.0151 0.0256  90  LYS   B CB  
5323 C CG  . LYS   B 90  ? 0.2659 0.1687 0.2066 -0.0258 0.0089  0.0167  90  LYS   B CG  
5324 C CD  . LYS   B 90  ? 0.2975 0.2003 0.2528 -0.0130 0.0381  -0.0007 90  LYS   B CD  
5325 C CE  . LYS   B 90  ? 0.3087 0.2135 0.2861 -0.0193 0.0541  -0.0126 90  LYS   B CE  
5326 N NZ  . LYS   B 90  ? 0.3093 0.2006 0.2737 -0.0266 0.0782  -0.0180 90  LYS   B NZ  
5340 N N   . HIS   B 91  ? 0.1874 0.1384 0.1698 -0.0329 -0.0228 0.0061  91  HIS   B N   
5341 C CA  . HIS   B 91  ? 0.1748 0.1447 0.1697 -0.0283 -0.0271 -0.0079 91  HIS   B CA  
5342 C C   . HIS   B 91  ? 0.1653 0.1413 0.1575 -0.0307 -0.0148 -0.0069 91  HIS   B C   
5343 O O   . HIS   B 91  ? 0.1814 0.1436 0.1490 -0.0260 -0.0250 0.0004  91  HIS   B O   
5344 C CB  . HIS   B 91  ? 0.1954 0.1539 0.1943 -0.0119 -0.0250 0.0155  91  HIS   B CB  
5345 C CG  . HIS   B 91  ? 0.2466 0.1690 0.2612 -0.0028 0.0024  0.0343  91  HIS   B CG  
5346 N ND1 . HIS   B 91  ? 0.2740 0.1663 0.3147 0.0014  0.0070  0.0240  91  HIS   B ND1 
5347 C CD2 . HIS   B 91  ? 0.2604 0.2027 0.3177 0.0161  -0.0134 0.0537  91  HIS   B CD2 
5348 C CE1 . HIS   B 91  ? 0.2879 0.1889 0.3460 0.0092  0.0067  0.0225  91  HIS   B CE1 
5349 N NE2 . HIS   B 91  ? 0.2795 0.2060 0.3539 0.0254  0.0043  0.0596  91  HIS   B NE2 
5357 N N   . CYS   B 92  ? 0.1617 0.1359 0.1602 -0.0253 -0.0175 -0.0085 92  CYS   B N   
5358 C CA  . CYS   B 92  ? 0.1553 0.1330 0.1618 -0.0220 -0.0106 -0.0045 92  CYS   B CA  
5359 C C   . CYS   B 92  ? 0.1515 0.1275 0.1566 -0.0167 -0.0101 0.0107  92  CYS   B C   
5360 O O   . CYS   B 92  ? 0.1635 0.1390 0.1782 -0.0214 -0.0022 0.0015  92  CYS   B O   
5361 C CB  . CYS   B 92  ? 0.1537 0.1410 0.1769 -0.0153 -0.0058 0.0025  92  CYS   B CB  
5362 S SG  . CYS   B 92  ? 0.1612 0.1507 0.1832 -0.0119 -0.0151 0.0107  92  CYS   B SG  
5368 N N   . LEU   B 93  ? 0.1470 0.1353 0.1559 -0.0134 -0.0123 0.0074  93  LEU   B N   
5369 C CA  . LEU   B 93  ? 0.1435 0.1370 0.1485 -0.0050 -0.0209 0.0086  93  LEU   B CA  
5370 C C   . LEU   B 93  ? 0.1320 0.1337 0.1389 -0.0038 -0.0167 0.0114  93  LEU   B C   
5371 O O   . LEU   B 93  ? 0.1517 0.1286 0.1717 -0.0076 -0.0147 -0.0006 93  LEU   B O   
5372 C CB  . LEU   B 93  ? 0.1507 0.1398 0.1643 -0.0025 -0.0163 0.0118  93  LEU   B CB  
5373 C CG  . LEU   B 93  ? 0.1454 0.1556 0.1813 -0.0057 -0.0117 0.0166  93  LEU   B CG  
5374 C CD1 . LEU   B 93  ? 0.1528 0.1639 0.1960 -0.0016 -0.0085 -0.0016 93  LEU   B CD1 
5375 C CD2 . LEU   B 93  ? 0.1493 0.1578 0.1997 -0.0009 -0.0189 0.0114  93  LEU   B CD2 
5387 N N   . HIS   B 94  ? 0.1433 0.1345 0.1288 -0.0092 -0.0191 0.0062  94  HIS   B N   
5388 C CA  . HIS   B 94  ? 0.1436 0.1314 0.1434 -0.0030 -0.0144 0.0022  94  HIS   B CA  
5389 C C   . HIS   B 94  ? 0.1431 0.1321 0.1704 -0.0008 -0.0145 0.0138  94  HIS   B C   
5390 O O   . HIS   B 94  ? 0.1489 0.1438 0.2162 -0.0059 0.0152  -0.0021 94  HIS   B O   
5391 C CB  . HIS   B 94  ? 0.1438 0.1376 0.1613 -0.0061 -0.0094 0.0065  94  HIS   B CB  
5392 C CG  . HIS   B 94  ? 0.1492 0.1328 0.1716 -0.0085 -0.0280 0.0049  94  HIS   B CG  
5393 N ND1 . HIS   B 94  ? 0.1520 0.1402 0.1767 -0.0039 -0.0350 0.0027  94  HIS   B ND1 
5394 C CD2 . HIS   B 94  ? 0.1527 0.1416 0.1903 -0.0057 -0.0307 0.0071  94  HIS   B CD2 
5395 C CE1 . HIS   B 94  ? 0.1532 0.1361 0.1861 -0.0144 -0.0251 0.0057  94  HIS   B CE1 
5396 N NE2 . HIS   B 94  ? 0.1531 0.1518 0.1981 -0.0207 -0.0213 0.0089  94  HIS   B NE2 
5404 N N   . VAL   B 95  ? 0.1382 0.1289 0.1787 -0.0005 -0.0082 0.0150  95  VAL   B N   
5405 C CA  . VAL   B 95  ? 0.1405 0.1419 0.1670 -0.0011 0.0027  0.0182  95  VAL   B CA  
5406 C C   . VAL   B 95  ? 0.1468 0.1381 0.1662 -0.0018 0.0075  0.0186  95  VAL   B C   
5407 O O   . VAL   B 95  ? 0.1582 0.1395 0.2033 0.0065  0.0041  0.0262  95  VAL   B O   
5408 C CB  . VAL   B 95  ? 0.1421 0.1424 0.1760 -0.0019 -0.0173 0.0085  95  VAL   B CB  
5409 C CG1 . VAL   B 95  ? 0.1562 0.1662 0.2193 -0.0160 -0.0092 0.0140  95  VAL   B CG1 
5410 C CG2 . VAL   B 95  ? 0.1554 0.1469 0.1766 0.0026  -0.0200 0.0101  95  VAL   B CG2 
5420 N N   . VAL   B 96  ? 0.1574 0.1524 0.1704 0.0106  0.0065  0.0280  96  VAL   B N   
5421 C CA  . VAL   B 96  ? 0.1611 0.1609 0.1699 0.0083  -0.0015 0.0282  96  VAL   B CA  
5422 C C   . VAL   B 96  ? 0.1692 0.1655 0.1799 0.0043  0.0055  0.0217  96  VAL   B C   
5423 O O   . VAL   B 96  ? 0.1777 0.1726 0.2096 -0.0063 0.0224  0.0114  96  VAL   B O   
5424 C CB  . VAL   B 96  ? 0.1697 0.1805 0.1747 0.0036  -0.0030 0.0231  96  VAL   B CB  
5425 C CG1 . VAL   B 96  ? 0.1742 0.1906 0.1703 0.0170  0.0090  0.0082  96  VAL   B CG1 
5426 C CG2 . VAL   B 96  ? 0.1751 0.1841 0.1802 0.0044  0.0104  0.0230  96  VAL   B CG2 
5436 N N   . GLY   B 97  ? 0.1791 0.1609 0.1704 -0.0017 -0.0058 0.0258  97  GLY   B N   
5437 C CA  . GLY   B 97  ? 0.2040 0.1683 0.1881 -0.0014 0.0009  0.0269  97  GLY   B CA  
5438 C C   . GLY   B 97  ? 0.2333 0.1751 0.2038 0.0020  0.0136  0.0216  97  GLY   B C   
5439 O O   . GLY   B 97  ? 0.2548 0.1824 0.1960 0.0028  -0.0005 0.0173  97  GLY   B O   
5443 N N   . PRO   B 98  ? 0.2419 0.1799 0.2096 0.0126  0.0380  0.0395  98  PRO   B N   
5444 C CA  . PRO   B 98  ? 0.2713 0.2065 0.2251 0.0285  0.0497  0.0411  98  PRO   B CA  
5445 C C   . PRO   B 98  ? 0.2828 0.2024 0.1865 0.0473  0.0611  0.0619  98  PRO   B C   
5446 O O   . PRO   B 98  ? 0.2660 0.1943 0.2300 0.0403  0.0493  0.0564  98  PRO   B O   
5447 C CB  . PRO   B 98  ? 0.2625 0.2161 0.2547 0.0248  0.0689  0.0513  98  PRO   B CB  
5448 C CG  . PRO   B 98  ? 0.2497 0.2023 0.2629 0.0112  0.0640  0.0683  98  PRO   B CG  
5449 C CD  . PRO   B 98  ? 0.2299 0.1853 0.2500 0.0100  0.0596  0.0584  98  PRO   B CD  
5457 N N   . ASN   B 99  ? 0.3066 0.2297 0.2037 0.0700  0.0602  0.0456  99  ASN   B N   
5458 C CA  . ASN   B 99  ? 0.3368 0.2489 0.2051 0.0906  0.0618  0.0685  99  ASN   B CA  
5459 C C   . ASN   B 99  ? 0.3627 0.2913 0.2474 0.0992  0.0828  0.1043  99  ASN   B C   
5460 O O   . ASN   B 99  ? 0.3815 0.3081 0.2714 0.1023  0.0827  0.1054  99  ASN   B O   
5461 C CB  . ASN   B 99  ? 0.3479 0.2440 0.2227 0.0910  0.0437  0.0562  99  ASN   B CB  
5462 C CG  . ASN   B 99  ? 0.3559 0.2497 0.2403 0.0810  0.0423  0.0532  99  ASN   B CG  
5463 O OD1 . ASN   B 99  ? 0.3589 0.2409 0.2669 0.0858  0.0414  0.0617  99  ASN   B OD1 
5464 N ND2 . ASN   B 99  ? 0.3546 0.2543 0.2454 0.0807  0.0197  0.0394  99  ASN   B ND2 
5471 N N   . VAL   B 100 ? 0.3799 0.3081 0.3109 0.0879  0.0965  0.1328  100 VAL   B N   
5472 C CA  . VAL   B 100 ? 0.4164 0.3415 0.3802 0.0654  0.0890  0.1548  100 VAL   B CA  
5473 C C   . VAL   B 100 ? 0.4470 0.3578 0.3768 0.0693  0.0772  0.1880  100 VAL   B C   
5474 O O   . VAL   B 100 ? 0.4563 0.3722 0.3950 0.0660  0.0851  0.1844  100 VAL   B O   
5475 C CB  . VAL   B 100 ? 0.4227 0.3540 0.4475 0.0324  0.0901  0.1578  100 VAL   B CB  
5476 C CG1 . VAL   B 100 ? 0.4278 0.3577 0.4771 0.0258  0.0865  0.1519  100 VAL   B CG1 
5477 C CG2 . VAL   B 100 ? 0.4232 0.3608 0.4674 0.0198  0.0894  0.1603  100 VAL   B CG2 
5487 N N   . ASN   B 101 ? 0.4695 0.3661 0.3738 0.0765  0.0529  0.2035  101 ASN   B N   
5488 C CA  . ASN   B 101 ? 0.5011 0.3915 0.3728 0.0686  0.0351  0.1920  101 ASN   B CA  
5489 C C   . ASN   B 101 ? 0.5507 0.4528 0.4037 0.0504  0.0207  0.1682  101 ASN   B C   
5490 O O   . ASN   B 101 ? 0.5534 0.4608 0.4255 0.0539  0.0250  0.1481  101 ASN   B O   
5491 C CB  . ASN   B 101 ? 0.4873 0.3694 0.3762 0.0670  0.0383  0.1712  101 ASN   B CB  
5492 C CG  . ASN   B 101 ? 0.4738 0.3504 0.3688 0.0666  0.0439  0.1621  101 ASN   B CG  
5493 O OD1 . ASN   B 101 ? 0.4702 0.3446 0.3900 0.0582  0.0693  0.1527  101 ASN   B OD1 
5494 N ND2 . ASN   B 101 ? 0.4651 0.3420 0.3690 0.0695  0.0388  0.1468  101 ASN   B ND2 
5501 N N   A LYS   B 102 ? 0.5721 0.4814 0.4343 0.0374  0.0195  0.1478  102 LYS   B N   
5502 N N   B LYS   B 102 ? 0.5731 0.4818 0.4306 0.0390  0.0177  0.1481  102 LYS   B N   
5503 C CA  A LYS   B 102 ? 0.5905 0.5085 0.4628 0.0225  0.0209  0.1219  102 LYS   B CA  
5504 C CA  B LYS   B 102 ? 0.5923 0.5095 0.4558 0.0254  0.0173  0.1219  102 LYS   B CA  
5505 C C   A LYS   B 102 ? 0.5915 0.5113 0.4379 0.0217  0.0220  0.1281  102 LYS   B C   
5506 C C   B LYS   B 102 ? 0.5924 0.5119 0.4301 0.0233  0.0197  0.1293  102 LYS   B C   
5507 O O   A LYS   B 102 ? 0.5961 0.5147 0.4423 0.0212  0.0155  0.1268  102 LYS   B O   
5508 O O   B LYS   B 102 ? 0.5971 0.5161 0.4282 0.0229  0.0118  0.1293  102 LYS   B O   
5509 C CB  A LYS   B 102 ? 0.6051 0.5305 0.5199 0.0096  0.0255  0.0842  102 LYS   B CB  
5510 C CB  B LYS   B 102 ? 0.6085 0.5323 0.5123 0.0149  0.0197  0.0820  102 LYS   B CB  
5511 C CG  A LYS   B 102 ? 0.6180 0.5490 0.5693 -0.0004 0.0307  0.0493  102 LYS   B CG  
5512 C CG  B LYS   B 102 ? 0.6226 0.5515 0.5622 0.0074  0.0223  0.0463  102 LYS   B CG  
5513 C CD  A LYS   B 102 ? 0.6290 0.5634 0.6173 -0.0078 0.0347  0.0219  102 LYS   B CD  
5514 C CD  B LYS   B 102 ? 0.6348 0.5668 0.6134 0.0019  0.0249  0.0182  102 LYS   B CD  
5515 C CE  A LYS   B 102 ? 0.6368 0.5726 0.6492 -0.0129 0.0381  0.0016  102 LYS   B CE  
5516 C CE  B LYS   B 102 ? 0.6436 0.5770 0.6477 -0.0017 0.0264  -0.0019 102 LYS   B CE  
5517 N NZ  A LYS   B 102 ? 0.6412 0.5772 0.6662 -0.0150 0.0388  -0.0105 102 LYS   B NZ  
5518 N NZ  B LYS   B 102 ? 0.6488 0.5825 0.6691 -0.0034 0.0259  -0.0139 102 LYS   B NZ  
5545 N N   . GLY   B 103 ? 0.5858 0.5089 0.4255 0.0218  0.0303  0.1271  103 GLY   B N   
5546 C CA  . GLY   B 103 ? 0.5720 0.5013 0.4265 0.0201  0.0521  0.1145  103 GLY   B CA  
5547 C C   . GLY   B 103 ? 0.5544 0.4897 0.4286 0.0191  0.0714  0.0981  103 GLY   B C   
5548 O O   . GLY   B 103 ? 0.5574 0.4941 0.4226 0.0154  0.0804  0.0991  103 GLY   B O   
5553 N N   A GLU   B 104 ? 0.5428 0.4808 0.4307 0.0187  0.0769  0.0875  104 GLU   B N   
5554 N N   B GLU   B 104 ? 0.5418 0.4793 0.4300 0.0202  0.0779  0.0870  104 GLU   B N   
5555 C CA  A GLU   B 104 ? 0.5284 0.4711 0.4316 0.0218  0.0792  0.0736  104 GLU   B CA  
5556 C CA  B GLU   B 104 ? 0.5262 0.4680 0.4304 0.0254  0.0807  0.0723  104 GLU   B CA  
5557 C C   A GLU   B 104 ? 0.5217 0.4688 0.4400 0.0131  0.1168  0.0760  104 GLU   B C   
5558 C C   B GLU   B 104 ? 0.5205 0.4673 0.4397 0.0146  0.1180  0.0755  104 GLU   B C   
5559 O O   A GLU   B 104 ? 0.5209 0.4706 0.4477 0.0120  0.1218  0.0771  104 GLU   B O   
5560 O O   B GLU   B 104 ? 0.5195 0.4690 0.4477 0.0133  0.1237  0.0768  104 GLU   B O   
5561 C CB  A GLU   B 104 ? 0.5235 0.4622 0.4282 0.0329  0.0431  0.0542  104 GLU   B CB  
5562 C CB  B GLU   B 104 ? 0.5194 0.4559 0.4266 0.0404  0.0451  0.0513  104 GLU   B CB  
5563 C CG  A GLU   B 104 ? 0.5188 0.4539 0.4197 0.0436  0.0062  0.0350  104 GLU   B CG  
5564 C CG  B GLU   B 104 ? 0.5128 0.4445 0.4171 0.0551  0.0083  0.0306  104 GLU   B CG  
5565 C CD  A GLU   B 104 ? 0.5153 0.4459 0.4076 0.0529  -0.0244 0.0225  104 GLU   B CD  
5566 C CD  B GLU   B 104 ? 0.5074 0.4336 0.4040 0.0684  -0.0228 0.0176  104 GLU   B CD  
5567 O OE1 A GLU   B 104 ? 0.5111 0.4380 0.3798 0.0580  -0.0288 0.0205  104 GLU   B OE1 
5568 O OE1 B GLU   B 104 ? 0.5018 0.4241 0.3727 0.0758  -0.0264 0.0160  104 GLU   B OE1 
5569 O OE2 A GLU   B 104 ? 0.5153 0.4470 0.4019 0.0554  -0.0450 0.0135  104 GLU   B OE2 
5570 O OE2 B GLU   B 104 ? 0.5071 0.4336 0.3974 0.0718  -0.0440 0.0078  104 GLU   B OE2 
5583 N N   . ASP   B 105 ? 0.5111 0.4627 0.4324 0.0081  0.1461  0.0743  105 ASP   B N   
5584 C CA  . ASP   B 105 ? 0.5030 0.4581 0.4678 -0.0062 0.1814  0.0528  105 ASP   B CA  
5585 C C   . ASP   B 105 ? 0.4766 0.4286 0.4169 -0.0273 0.1991  0.0401  105 ASP   B C   
5586 O O   . ASP   B 105 ? 0.4612 0.4184 0.3996 -0.0197 0.2249  0.0548  105 ASP   B O   
5587 C CB  . ASP   B 105 ? 0.5129 0.4776 0.5519 0.0002  0.2004  0.0412  105 ASP   B CB  
5588 C CG  . ASP   B 105 ? 0.5225 0.4957 0.6301 0.0021  0.2184  0.0335  105 ASP   B CG  
5589 O OD1 . ASP   B 105 ? 0.5178 0.4971 0.6340 -0.0052 0.2451  0.0441  105 ASP   B OD1 
5590 O OD2 . ASP   B 105 ? 0.5291 0.5066 0.6766 0.0086  0.2088  0.0186  105 ASP   B OD2 
5596 N N   A ILE   B 106 ? 0.4734 0.4189 0.4111 -0.0391 0.1839  0.0328  106 ILE   B N   
5597 N N   B ILE   B 106 ? 0.4734 0.4182 0.4097 -0.0383 0.1853  0.0322  106 ILE   B N   
5598 C CA  A ILE   B 106 ? 0.4643 0.4062 0.4026 -0.0567 0.1769  0.0273  106 ILE   B CA  
5599 C CA  B ILE   B 106 ? 0.4638 0.4048 0.3997 -0.0555 0.1804  0.0263  106 ILE   B CA  
5600 C C   A ILE   B 106 ? 0.4456 0.3977 0.3875 -0.0620 0.1803  0.0199  106 ILE   B C   
5601 C C   B ILE   B 106 ? 0.4446 0.3960 0.3840 -0.0618 0.1834  0.0196  106 ILE   B C   
5602 O O   A ILE   B 106 ? 0.4393 0.3861 0.3779 -0.0710 0.1855  0.0221  106 ILE   B O   
5603 O O   B ILE   B 106 ? 0.4370 0.3829 0.3724 -0.0718 0.1904  0.0227  106 ILE   B O   
5604 C CB  A ILE   B 106 ? 0.4745 0.4027 0.4177 -0.0643 0.1604  0.0248  106 ILE   B CB  
5605 C CB  B ILE   B 106 ? 0.4745 0.4013 0.4151 -0.0613 0.1645  0.0216  106 ILE   B CB  
5606 C CG1 A ILE   B 106 ? 0.4764 0.4005 0.4210 -0.0633 0.1505  0.0177  106 ILE   B CG1 
5607 C CG1 B ILE   B 106 ? 0.4775 0.3997 0.4198 -0.0574 0.1528  0.0115  106 ILE   B CG1 
5608 C CG2 A ILE   B 106 ? 0.4785 0.4051 0.4318 -0.0676 0.1572  0.0271  106 ILE   B CG2 
5609 C CG2 B ILE   B 106 ? 0.4781 0.4039 0.4294 -0.0648 0.1624  0.0230  106 ILE   B CG2 
5610 C CD1 A ILE   B 106 ? 0.4772 0.4006 0.4200 -0.0617 0.1463  0.0151  106 ILE   B CD1 
5611 C CD1 B ILE   B 106 ? 0.4792 0.4002 0.4189 -0.0544 0.1475  0.0073  106 ILE   B CD1 
5634 N N   . GLN   B 107 ? 0.4329 0.4006 0.4023 -0.0618 0.1742  0.0187  107 GLN   B N   
5635 C CA  . GLN   B 107 ? 0.4091 0.4079 0.4264 -0.0541 0.1531  0.0174  107 GLN   B CA  
5636 C C   . GLN   B 107 ? 0.3474 0.3595 0.3890 -0.0360 0.1263  0.0167  107 GLN   B C   
5637 O O   . GLN   B 107 ? 0.3294 0.3626 0.4174 -0.0261 0.0960  -0.0056 107 GLN   B O   
5638 C CB  . GLN   B 107 ? 0.4670 0.4751 0.5176 -0.0519 0.1314  0.0102  107 GLN   B CB  
5639 C CG  . GLN   B 107 ? 0.5265 0.5402 0.6048 -0.0471 0.1014  0.0027  107 GLN   B CG  
5640 C CD  . GLN   B 107 ? 0.5691 0.5892 0.6748 -0.0458 0.0798  -0.0030 107 GLN   B CD  
5641 O OE1 . GLN   B 107 ? 0.5831 0.6055 0.7001 -0.0453 0.0774  -0.0058 107 GLN   B OE1 
5642 N NE2 . GLN   B 107 ? 0.5834 0.6047 0.7003 -0.0434 0.0695  -0.0019 107 GLN   B NE2 
5652 N N   . LEU   B 108 ? 0.3034 0.3167 0.3507 -0.0060 0.1107  0.0220  108 LEU   B N   
5653 C CA  . LEU   B 108 ? 0.2671 0.2774 0.2896 0.0085  0.0846  0.0387  108 LEU   B CA  
5654 C C   . LEU   B 108 ? 0.2111 0.2264 0.2930 0.0066  0.0445  0.0403  108 LEU   B C   
5655 O O   . LEU   B 108 ? 0.1989 0.1991 0.2722 0.0207  0.0374  0.0255  108 LEU   B O   
5656 C CB  . LEU   B 108 ? 0.2807 0.2941 0.2622 0.0110  0.0882  0.0515  108 LEU   B CB  
5657 C CG  . LEU   B 108 ? 0.2981 0.3267 0.2756 0.0183  0.0805  0.0267  108 LEU   B CG  
5658 C CD1 . LEU   B 108 ? 0.3083 0.3428 0.2684 0.0116  0.0828  0.0256  108 LEU   B CD1 
5659 C CD2 . LEU   B 108 ? 0.3130 0.3368 0.2740 0.0287  0.0513  0.0025  108 LEU   B CD2 
5671 N N   . LEU   B 109 ? 0.1838 0.2017 0.2963 0.0080  0.0374  0.0355  109 LEU   B N   
5672 C CA  . LEU   B 109 ? 0.1753 0.1647 0.3074 0.0085  0.0272  0.0412  109 LEU   B CA  
5673 C C   . LEU   B 109 ? 0.1643 0.1492 0.3014 0.0025  0.0286  0.0286  109 LEU   B C   
5674 O O   . LEU   B 109 ? 0.1632 0.1476 0.2780 0.0076  0.0256  0.0341  109 LEU   B O   
5675 C CB  . LEU   B 109 ? 0.1779 0.1612 0.3189 0.0093  0.0146  0.0544  109 LEU   B CB  
5676 C CG  . LEU   B 109 ? 0.1708 0.1566 0.3074 0.0022  0.0182  0.0333  109 LEU   B CG  
5677 C CD1 . LEU   B 109 ? 0.1640 0.1679 0.2795 0.0120  0.0168  0.0332  109 LEU   B CD1 
5678 C CD2 . LEU   B 109 ? 0.1886 0.1622 0.3171 0.0076  0.0008  0.0342  109 LEU   B CD2 
5690 N N   . LYS   B 110 ? 0.1562 0.1483 0.2849 -0.0048 0.0212  0.0266  110 LYS   B N   
5691 C CA  . LYS   B 110 ? 0.1535 0.1495 0.2975 -0.0011 0.0205  0.0253  110 LYS   B CA  
5692 C C   . LYS   B 110 ? 0.1474 0.1559 0.2764 -0.0056 0.0203  0.0206  110 LYS   B C   
5693 O O   . LYS   B 110 ? 0.1557 0.1505 0.2723 -0.0117 0.0184  0.0140  110 LYS   B O   
5694 C CB  . LYS   B 110 ? 0.1588 0.1437 0.3185 -0.0062 0.0210  0.0173  110 LYS   B CB  
5695 C CG  . LYS   B 110 ? 0.1570 0.1448 0.3331 -0.0016 -0.0022 0.0259  110 LYS   B CG  
5696 C CD  . LYS   B 110 ? 0.1611 0.1535 0.3271 -0.0028 0.0088  0.0237  110 LYS   B CD  
5697 C CE  . LYS   B 110 ? 0.1617 0.1707 0.3584 0.0058  0.0095  0.0021  110 LYS   B CE  
5698 N NZ  . LYS   B 110 ? 0.1671 0.1846 0.3637 0.0059  -0.0001 0.0075  110 LYS   B NZ  
5712 N N   . SER   B 111 ? 0.1519 0.1540 0.2928 -0.0066 0.0301  0.0178  111 SER   B N   
5713 C CA  . SER   B 111 ? 0.1661 0.1581 0.2703 0.0013  0.0180  0.0206  111 SER   B CA  
5714 C C   . SER   B 111 ? 0.1622 0.1449 0.2543 0.0006  0.0042  0.0119  111 SER   B C   
5715 O O   . SER   B 111 ? 0.1571 0.1452 0.2627 0.0027  0.0040  0.0095  111 SER   B O   
5716 C CB  . SER   B 111 ? 0.1757 0.1894 0.2847 0.0060  0.0342  0.0228  111 SER   B CB  
5717 O OG  . SER   B 111 ? 0.1871 0.2129 0.2891 0.0060  0.0359  0.0306  111 SER   B OG  
5723 N N   . ALA   B 112 ? 0.1476 0.1491 0.2493 0.0027  0.0071  0.0144  112 ALA   B N   
5724 C CA  . ALA   B 112 ? 0.1486 0.1610 0.2331 0.0037  -0.0020 -0.0045 112 ALA   B CA  
5725 C C   . ALA   B 112 ? 0.1410 0.1474 0.2310 0.0024  -0.0056 -0.0001 112 ALA   B C   
5726 O O   . ALA   B 112 ? 0.1413 0.1459 0.2446 -0.0047 0.0004  0.0030  112 ALA   B O   
5727 C CB  . ALA   B 112 ? 0.1531 0.1714 0.2374 0.0044  -0.0027 0.0049  112 ALA   B CB  
5733 N N   . TYR   B 113 ? 0.1434 0.1346 0.2380 -0.0029 -0.0023 0.0042  113 TYR   B N   
5734 C CA  . TYR   B 113 ? 0.1410 0.1342 0.2443 -0.0027 0.0066  -0.0024 113 TYR   B CA  
5735 C C   . TYR   B 113 ? 0.1376 0.1300 0.2336 -0.0121 0.0049  0.0063  113 TYR   B C   
5736 O O   . TYR   B 113 ? 0.1374 0.1343 0.2260 -0.0046 -0.0009 -0.0027 113 TYR   B O   
5737 C CB  . TYR   B 113 ? 0.1412 0.1269 0.2454 -0.0009 0.0027  0.0012  113 TYR   B CB  
5738 C CG  . TYR   B 113 ? 0.1430 0.1380 0.2648 -0.0068 -0.0009 0.0146  113 TYR   B CG  
5739 C CD1 . TYR   B 113 ? 0.1487 0.1426 0.2704 -0.0051 0.0065  0.0154  113 TYR   B CD1 
5740 C CD2 . TYR   B 113 ? 0.1482 0.1448 0.2563 -0.0059 0.0034  0.0222  113 TYR   B CD2 
5741 C CE1 . TYR   B 113 ? 0.1560 0.1415 0.2674 -0.0047 0.0165  0.0093  113 TYR   B CE1 
5742 C CE2 . TYR   B 113 ? 0.1546 0.1413 0.2699 0.0004  -0.0029 0.0252  113 TYR   B CE2 
5743 C CZ  . TYR   B 113 ? 0.1453 0.1386 0.2681 0.0042  -0.0005 0.0171  113 TYR   B CZ  
5744 O OH  . TYR   B 113 ? 0.1518 0.1358 0.3083 0.0094  0.0083  0.0150  113 TYR   B OH  
5754 N N   . GLU   B 114 ? 0.1363 0.1253 0.2529 -0.0041 0.0008  0.0105  114 GLU   B N   
5755 C CA  . GLU   B 114 ? 0.1401 0.1253 0.2567 0.0011  -0.0055 0.0121  114 GLU   B CA  
5756 C C   . GLU   B 114 ? 0.1355 0.1234 0.2392 -0.0035 0.0024  0.0053  114 GLU   B C   
5757 O O   . GLU   B 114 ? 0.1388 0.1306 0.2554 0.0032  -0.0091 0.0079  114 GLU   B O   
5758 C CB  . GLU   B 114 ? 0.1388 0.1430 0.2696 -0.0050 0.0073  -0.0005 114 GLU   B CB  
5759 C CG  . GLU   B 114 ? 0.1417 0.1406 0.2792 -0.0008 0.0052  0.0104  114 GLU   B CG  
5760 C CD  . GLU   B 114 ? 0.1449 0.1454 0.2920 -0.0122 0.0090  0.0128  114 GLU   B CD  
5761 O OE1 . GLU   B 114 ? 0.1410 0.1551 0.2771 -0.0117 0.0069  0.0110  114 GLU   B OE1 
5762 O OE2 . GLU   B 114 ? 0.1479 0.1667 0.2963 -0.0196 0.0185  0.0089  114 GLU   B OE2 
5769 N N   . ASN   B 115 ? 0.1422 0.1221 0.2352 -0.0036 -0.0086 0.0009  115 ASN   B N   
5770 C CA  . ASN   B 115 ? 0.1435 0.1352 0.2171 -0.0050 -0.0162 0.0090  115 ASN   B CA  
5771 C C   . ASN   B 115 ? 0.1419 0.1321 0.2163 -0.0104 -0.0187 -0.0015 115 ASN   B C   
5772 O O   . ASN   B 115 ? 0.1570 0.1352 0.2112 -0.0146 -0.0082 0.0009  115 ASN   B O   
5773 C CB  . ASN   B 115 ? 0.1518 0.1450 0.2182 -0.0135 -0.0033 0.0027  115 ASN   B CB  
5774 C CG  . ASN   B 115 ? 0.1612 0.1490 0.2247 -0.0047 -0.0083 0.0011  115 ASN   B CG  
5775 O OD1 . ASN   B 115 ? 0.2041 0.1757 0.2447 -0.0062 0.0138  -0.0096 115 ASN   B OD1 
5776 N ND2 . ASN   B 115 ? 0.1606 0.1619 0.2147 -0.0096 -0.0096 0.0063  115 ASN   B ND2 
5783 N N   . PHE   B 116 ? 0.1325 0.1348 0.2179 -0.0091 -0.0072 0.0010  116 PHE   B N   
5784 C CA  . PHE   B 116 ? 0.1431 0.1341 0.2189 -0.0063 -0.0054 0.0040  116 PHE   B CA  
5785 C C   . PHE   B 116 ? 0.1440 0.1247 0.2139 -0.0075 -0.0151 0.0011  116 PHE   B C   
5786 O O   . PHE   B 116 ? 0.1532 0.1359 0.2148 -0.0034 -0.0118 0.0069  116 PHE   B O   
5787 C CB  . PHE   B 116 ? 0.1383 0.1321 0.2094 -0.0037 -0.0161 0.0078  116 PHE   B CB  
5788 C CG  . PHE   B 116 ? 0.1384 0.1279 0.2107 -0.0101 -0.0053 0.0058  116 PHE   B CG  
5789 C CD1 . PHE   B 116 ? 0.1498 0.1350 0.2250 -0.0023 -0.0130 0.0023  116 PHE   B CD1 
5790 C CD2 . PHE   B 116 ? 0.1387 0.1406 0.2157 -0.0123 -0.0027 0.0002  116 PHE   B CD2 
5791 C CE1 . PHE   B 116 ? 0.1505 0.1442 0.2283 -0.0094 -0.0091 0.0000  116 PHE   B CE1 
5792 C CE2 . PHE   B 116 ? 0.1409 0.1370 0.2123 -0.0045 -0.0114 0.0015  116 PHE   B CE2 
5793 C CZ  . PHE   B 116 ? 0.1329 0.1497 0.2131 -0.0068 -0.0175 0.0054  116 PHE   B CZ  
5803 N N   . ASN   B 117 ? 0.1469 0.1313 0.2269 -0.0042 -0.0144 0.0060  117 ASN   B N   
5804 C CA  . ASN   B 117 ? 0.1511 0.1318 0.2291 -0.0004 -0.0136 -0.0004 117 ASN   B CA  
5805 C C   . ASN   B 117 ? 0.1572 0.1372 0.2335 0.0053  -0.0263 -0.0026 117 ASN   B C   
5806 O O   . ASN   B 117 ? 0.1583 0.1508 0.2751 -0.0021 -0.0443 0.0178  117 ASN   B O   
5807 C CB  . ASN   B 117 ? 0.1504 0.1342 0.2290 -0.0006 -0.0222 -0.0111 117 ASN   B CB  
5808 C CG  . ASN   B 117 ? 0.1538 0.1304 0.2534 0.0069  -0.0185 -0.0072 117 ASN   B CG  
5809 O OD1 . ASN   B 117 ? 0.1748 0.1349 0.2638 -0.0089 -0.0120 -0.0003 117 ASN   B OD1 
5810 N ND2 . ASN   B 117 ? 0.1525 0.1398 0.2444 -0.0032 -0.0123 -0.0049 117 ASN   B ND2 
5817 N N   . GLN   B 118 ? 0.1546 0.1288 0.2272 -0.0020 -0.0248 -0.0037 118 GLN   B N   
5818 C CA  . GLN   B 118 ? 0.1653 0.1336 0.2497 0.0007  -0.0163 0.0017  118 GLN   B CA  
5819 C C   . GLN   B 118 ? 0.1685 0.1265 0.2539 0.0054  -0.0217 0.0074  118 GLN   B C   
5820 O O   . GLN   B 118 ? 0.1916 0.1282 0.2870 -0.0070 -0.0096 0.0108  118 GLN   B O   
5821 C CB  . GLN   B 118 ? 0.1682 0.1401 0.2633 -0.0008 -0.0196 0.0002  118 GLN   B CB  
5822 C CG  . GLN   B 118 ? 0.1727 0.1443 0.2624 0.0071  -0.0201 -0.0146 118 GLN   B CG  
5823 C CD  . GLN   B 118 ? 0.1720 0.1298 0.2610 0.0068  -0.0220 -0.0203 118 GLN   B CD  
5824 O OE1 . GLN   B 118 ? 0.1836 0.1347 0.2818 0.0107  -0.0045 -0.0061 118 GLN   B OE1 
5825 N NE2 . GLN   B 118 ? 0.1778 0.1416 0.2615 0.0091  -0.0215 0.0008  118 GLN   B NE2 
5834 N N   . HIS   B 119 ? 0.1708 0.1347 0.2005 -0.0008 -0.0252 0.0095  119 HIS   B N   
5835 C CA  . HIS   B 119 ? 0.1845 0.1452 0.1888 0.0002  -0.0337 0.0110  119 HIS   B CA  
5836 C C   . HIS   B 119 ? 0.1955 0.1538 0.1863 -0.0027 -0.0513 0.0078  119 HIS   B C   
5837 O O   . HIS   B 119 ? 0.1944 0.1467 0.2321 -0.0297 -0.0326 0.0107  119 HIS   B O   
5838 C CB  . HIS   B 119 ? 0.1861 0.1517 0.2067 -0.0095 -0.0332 0.0106  119 HIS   B CB  
5839 C CG  . HIS   B 119 ? 0.1931 0.1715 0.2167 0.0021  -0.0419 -0.0016 119 HIS   B CG  
5840 N ND1 . HIS   B 119 ? 0.1989 0.1911 0.2522 -0.0063 -0.0530 -0.0189 119 HIS   B ND1 
5841 C CD2 . HIS   B 119 ? 0.2024 0.1925 0.2212 0.0340  -0.0536 -0.0017 119 HIS   B CD2 
5842 C CE1 . HIS   B 119 ? 0.2155 0.2001 0.2543 0.0087  -0.0578 -0.0415 119 HIS   B CE1 
5843 N NE2 . HIS   B 119 ? 0.2173 0.2146 0.2449 0.0271  -0.0508 -0.0206 119 HIS   B NE2 
5851 N N   A GLU   B 120 ? 0.2134 0.1629 0.1957 -0.0076 -0.0535 0.0121  120 GLU   B N   
5852 N N   B GLU   B 120 ? 0.2128 0.1587 0.1876 -0.0004 -0.0552 0.0208  120 GLU   B N   
5853 C CA  A GLU   B 120 ? 0.2325 0.1816 0.2248 -0.0115 -0.0573 0.0303  120 GLU   B CA  
5854 C CA  B GLU   B 120 ? 0.2320 0.1752 0.2111 0.0009  -0.0601 0.0469  120 GLU   B CA  
5855 C C   A GLU   B 120 ? 0.2135 0.1648 0.2129 -0.0202 -0.0508 0.0325  120 GLU   B C   
5856 C C   B GLU   B 120 ? 0.2104 0.1613 0.2089 -0.0134 -0.0504 0.0381  120 GLU   B C   
5857 O O   A GLU   B 120 ? 0.2071 0.1698 0.2121 -0.0234 -0.0460 0.0281  120 GLU   B O   
5858 O O   B GLU   B 120 ? 0.1991 0.1681 0.2104 -0.0158 -0.0402 0.0284  120 GLU   B O   
5859 C CB  A GLU   B 120 ? 0.2829 0.2181 0.3001 0.0016  -0.0724 0.0477  120 GLU   B CB  
5860 C CB  B GLU   B 120 ? 0.2864 0.2066 0.2747 0.0246  -0.0810 0.0812  120 GLU   B CB  
5861 C CG  A GLU   B 120 ? 0.3306 0.2750 0.3907 0.0067  -0.0749 0.0565  120 GLU   B CG  
5862 C CG  B GLU   B 120 ? 0.3384 0.2729 0.3662 0.0322  -0.0836 0.0883  120 GLU   B CG  
5863 C CD  A GLU   B 120 ? 0.3624 0.3202 0.4719 0.0086  -0.0775 0.0662  120 GLU   B CD  
5864 C CD  B GLU   B 120 ? 0.3770 0.3290 0.4517 0.0356  -0.0791 0.0913  120 GLU   B CD  
5865 O OE1 A GLU   B 120 ? 0.3791 0.3377 0.5029 0.0046  -0.0748 0.0734  120 GLU   B OE1 
5866 O OE1 B GLU   B 120 ? 0.3936 0.3504 0.4839 0.0330  -0.0725 0.0938  120 GLU   B OE1 
5867 O OE2 A GLU   B 120 ? 0.3788 0.3403 0.5086 0.0072  -0.0756 0.0621  120 GLU   B OE2 
5868 O OE2 B GLU   B 120 ? 0.3959 0.3479 0.4871 0.0360  -0.0766 0.0909  120 GLU   B OE2 
5881 N N   . VAL   B 121 ? 0.2048 0.1516 0.2045 -0.0210 -0.0419 0.0265  121 VAL   B N   
5882 C CA  . VAL   B 121 ? 0.1996 0.1655 0.1914 -0.0197 -0.0382 0.0249  121 VAL   B CA  
5883 C C   . VAL   B 121 ? 0.1854 0.1587 0.2001 -0.0271 -0.0321 0.0154  121 VAL   B C   
5884 O O   . VAL   B 121 ? 0.1881 0.1519 0.2068 -0.0333 -0.0376 0.0139  121 VAL   B O   
5885 C CB  . VAL   B 121 ? 0.2196 0.2059 0.2029 -0.0112 -0.0254 0.0201  121 VAL   B CB  
5886 C CG1 . VAL   B 121 ? 0.2241 0.2315 0.2416 -0.0160 -0.0204 0.0050  121 VAL   B CG1 
5887 C CG2 . VAL   B 121 ? 0.2498 0.2340 0.2097 -0.0044 -0.0150 0.0122  121 VAL   B CG2 
5898 N N   . LEU   B 122 ? 0.1742 0.1518 0.1825 -0.0240 -0.0336 0.0167  122 LEU   B N   
5899 C CA  . LEU   B 122 ? 0.1631 0.1617 0.1706 -0.0228 -0.0326 0.0140  122 LEU   B CA  
5900 C C   . LEU   B 122 ? 0.1663 0.1516 0.1742 -0.0324 -0.0323 0.0122  122 LEU   B C   
5901 O O   . LEU   B 122 ? 0.1790 0.1533 0.2090 -0.0408 -0.0428 0.0013  122 LEU   B O   
5902 C CB  . LEU   B 122 ? 0.1903 0.1767 0.2103 -0.0085 -0.0418 0.0185  122 LEU   B CB  
5903 C CG  . LEU   B 122 ? 0.1766 0.1837 0.2178 -0.0164 -0.0341 0.0102  122 LEU   B CG  
5904 C CD1 . LEU   B 122 ? 0.1792 0.2060 0.2165 -0.0209 -0.0337 0.0024  122 LEU   B CD1 
5905 C CD2 . LEU   B 122 ? 0.1736 0.1854 0.1944 -0.0066 -0.0179 0.0034  122 LEU   B CD2 
5917 N N   . LEU   B 123 ? 0.1648 0.1413 0.1660 -0.0335 -0.0263 0.0061  123 LEU   B N   
5918 C CA  . LEU   B 123 ? 0.1664 0.1385 0.1629 -0.0266 -0.0339 -0.0053 123 LEU   B CA  
5919 C C   . LEU   B 123 ? 0.1670 0.1334 0.1703 -0.0238 -0.0248 -0.0063 123 LEU   B C   
5920 O O   . LEU   B 123 ? 0.1790 0.1420 0.1640 -0.0284 -0.0266 -0.0005 123 LEU   B O   
5921 C CB  . LEU   B 123 ? 0.1715 0.1443 0.1665 -0.0235 -0.0240 -0.0053 123 LEU   B CB  
5922 C CG  . LEU   B 123 ? 0.1701 0.1492 0.1861 -0.0179 -0.0172 0.0027  123 LEU   B CG  
5923 C CD1 . LEU   B 123 ? 0.1800 0.1434 0.2245 -0.0136 -0.0119 -0.0103 123 LEU   B CD1 
5924 C CD2 . LEU   B 123 ? 0.1790 0.1676 0.2001 -0.0156 -0.0177 0.0164  123 LEU   B CD2 
5936 N N   . ALA   B 124 ? 0.1609 0.1375 0.1718 -0.0206 -0.0153 -0.0026 124 ALA   B N   
5937 C CA  . ALA   B 124 ? 0.1516 0.1406 0.1937 -0.0193 -0.0221 -0.0067 124 ALA   B CA  
5938 C C   . ALA   B 124 ? 0.1415 0.1353 0.1709 -0.0248 -0.0171 0.0006  124 ALA   B C   
5939 O O   . ALA   B 124 ? 0.1593 0.1376 0.1803 -0.0187 -0.0172 -0.0006 124 ALA   B O   
5940 C CB  . ALA   B 124 ? 0.1587 0.1381 0.2134 -0.0128 -0.0125 -0.0012 124 ALA   B CB  
5946 N N   . PRO   B 125 ? 0.1521 0.1353 0.1743 -0.0210 -0.0198 0.0107  125 PRO   B N   
5947 C CA  . PRO   B 125 ? 0.1580 0.1420 0.1950 -0.0197 -0.0203 0.0212  125 PRO   B CA  
5948 C C   . PRO   B 125 ? 0.1536 0.1381 0.2177 -0.0169 -0.0193 0.0233  125 PRO   B C   
5949 O O   . PRO   B 125 ? 0.1598 0.1386 0.2345 -0.0115 -0.0086 0.0195  125 PRO   B O   
5950 C CB  . PRO   B 125 ? 0.1669 0.1658 0.2164 -0.0226 -0.0303 0.0267  125 PRO   B CB  
5951 C CG  . PRO   B 125 ? 0.1756 0.1690 0.2050 -0.0316 -0.0315 0.0175  125 PRO   B CG  
5952 C CD  . PRO   B 125 ? 0.1696 0.1549 0.1869 -0.0303 -0.0202 0.0111  125 PRO   B CD  
5960 N N   . LEU   B 126 ? 0.1522 0.1373 0.2392 -0.0204 0.0027  0.0204  126 LEU   B N   
5961 C CA  . LEU   B 126 ? 0.1593 0.1478 0.2392 -0.0137 -0.0042 0.0239  126 LEU   B CA  
5962 C C   . LEU   B 126 ? 0.1564 0.1570 0.2293 -0.0091 0.0055  0.0269  126 LEU   B C   
5963 O O   . LEU   B 126 ? 0.1866 0.1996 0.2610 0.0204  -0.0235 0.0049  126 LEU   B O   
5964 C CB  . LEU   B 126 ? 0.1869 0.1471 0.2690 -0.0228 0.0090  0.0098  126 LEU   B CB  
5965 C CG  . LEU   B 126 ? 0.2105 0.1616 0.2935 -0.0306 0.0059  -0.0140 126 LEU   B CG  
5966 C CD1 . LEU   B 126 ? 0.2307 0.1650 0.3399 -0.0242 0.0020  -0.0377 126 LEU   B CD1 
5967 C CD2 . LEU   B 126 ? 0.2101 0.1859 0.2993 -0.0376 0.0008  -0.0215 126 LEU   B CD2 
5979 N N   . LEU   B 127 ? 0.1570 0.1408 0.2449 -0.0021 0.0160  0.0146  127 LEU   B N   
5980 C CA  . LEU   B 127 ? 0.1603 0.1498 0.2591 -0.0131 0.0253  0.0323  127 LEU   B CA  
5981 C C   . LEU   B 127 ? 0.1577 0.1458 0.2654 -0.0066 0.0127  0.0280  127 LEU   B C   
5982 O O   . LEU   B 127 ? 0.1640 0.1545 0.2682 -0.0132 0.0069  0.0178  127 LEU   B O   
5983 C CB  . LEU   B 127 ? 0.1740 0.1490 0.2737 -0.0090 0.0279  0.0263  127 LEU   B CB  
5984 C CG  . LEU   B 127 ? 0.1882 0.1518 0.2779 0.0034  0.0242  0.0245  127 LEU   B CG  
5985 C CD1 . LEU   B 127 ? 0.1966 0.1573 0.2762 0.0104  0.0148  0.0114  127 LEU   B CD1 
5986 C CD2 . LEU   B 127 ? 0.1956 0.1627 0.3006 -0.0084 0.0158  0.0390  127 LEU   B CD2 
5998 N N   . SER   B 128 ? 0.1541 0.1473 0.2663 -0.0007 -0.0041 0.0321  128 SER   B N   
5999 C CA  . SER   B 128 ? 0.1829 0.1520 0.2676 0.0029  -0.0161 0.0292  128 SER   B CA  
6000 C C   . SER   B 128 ? 0.1909 0.1603 0.2954 -0.0016 -0.0363 0.0227  128 SER   B C   
6001 O O   . SER   B 128 ? 0.2079 0.1633 0.3320 -0.0038 -0.0347 0.0394  128 SER   B O   
6002 C CB  . SER   B 128 ? 0.1993 0.1615 0.2574 0.0024  -0.0002 0.0400  128 SER   B CB  
6003 O OG  . SER   B 128 ? 0.1983 0.1739 0.2616 0.0056  0.0111  0.0397  128 SER   B OG  
6009 N N   . ALA   B 129 ? 0.2028 0.1657 0.3244 0.0221  -0.0233 0.0018  129 ALA   B N   
6010 C CA  . ALA   B 129 ? 0.2213 0.1756 0.3360 0.0334  -0.0192 -0.0015 129 ALA   B CA  
6011 C C   . ALA   B 129 ? 0.2034 0.1641 0.3226 0.0198  0.0036  0.0054  129 ALA   B C   
6012 O O   . ALA   B 129 ? 0.1973 0.1707 0.3164 0.0134  -0.0061 0.0063  129 ALA   B O   
6013 C CB  . ALA   B 129 ? 0.2484 0.2003 0.3579 0.0328  -0.0081 0.0103  129 ALA   B CB  
6019 N N   . GLY   B 130 ? 0.1994 0.1704 0.3244 0.0277  0.0106  0.0030  130 GLY   B N   
6020 C CA  . GLY   B 130 ? 0.2004 0.1768 0.3227 0.0193  0.0289  0.0088  130 GLY   B CA  
6021 C C   . GLY   B 130 ? 0.2001 0.1882 0.3106 0.0122  0.0203  0.0216  130 GLY   B C   
6022 O O   . GLY   B 130 ? 0.2069 0.1950 0.3300 0.0112  0.0121  0.0246  130 GLY   B O   
6026 N N   A ILE   B 131 ? 0.2009 0.1937 0.3116 0.0244  0.0168  0.0224  131 ILE   B N   
6027 N N   B ILE   B 131 ? 0.1993 0.1945 0.3122 0.0248  0.0153  0.0190  131 ILE   B N   
6028 C CA  A ILE   B 131 ? 0.2215 0.2090 0.3077 0.0153  0.0059  0.0338  131 ILE   B CA  
6029 C CA  B ILE   B 131 ? 0.2202 0.2114 0.3085 0.0141  0.0018  0.0280  131 ILE   B CA  
6030 C C   A ILE   B 131 ? 0.2346 0.2044 0.2872 0.0101  0.0051  0.0340  131 ILE   B C   
6031 C C   B ILE   B 131 ? 0.2350 0.2065 0.2879 0.0093  0.0029  0.0313  131 ILE   B C   
6032 O O   A ILE   B 131 ? 0.2586 0.2220 0.3022 0.0084  -0.0133 0.0412  131 ILE   B O   
6033 O O   B ILE   B 131 ? 0.2605 0.2259 0.3045 0.0070  -0.0161 0.0394  131 ILE   B O   
6034 C CB  A ILE   B 131 ? 0.2255 0.2347 0.3354 0.0104  -0.0073 0.0412  131 ILE   B CB  
6035 C CB  B ILE   B 131 ? 0.2223 0.2388 0.3363 0.0075  -0.0169 0.0305  131 ILE   B CB  
6036 C CG1 A ILE   B 131 ? 0.2323 0.2502 0.3419 -0.0127 -0.0015 0.0386  131 ILE   B CG1 
6037 C CG1 B ILE   B 131 ? 0.2259 0.2547 0.3385 -0.0185 -0.0213 0.0231  131 ILE   B CG1 
6038 C CG2 A ILE   B 131 ? 0.2272 0.2473 0.3585 0.0201  -0.0087 0.0404  131 ILE   B CG2 
6039 C CG2 B ILE   B 131 ? 0.2256 0.2531 0.3627 0.0171  -0.0152 0.0299  131 ILE   B CG2 
6040 C CD1 A ILE   B 131 ? 0.2377 0.2631 0.3532 -0.0221 -0.0022 0.0386  131 ILE   B CD1 
6041 C CD1 B ILE   B 131 ? 0.2294 0.2691 0.3486 -0.0283 -0.0277 0.0206  131 ILE   B CD1 
6064 N N   . PHE   B 132 ? 0.2190 0.1868 0.2750 0.0039  0.0179  0.0292  132 PHE   B N   
6065 C CA  . PHE   B 132 ? 0.2296 0.1846 0.2727 0.0032  0.0320  0.0210  132 PHE   B CA  
6066 C C   . PHE   B 132 ? 0.2455 0.2037 0.2978 0.0100  0.0484  0.0172  132 PHE   B C   
6067 O O   . PHE   B 132 ? 0.2651 0.2308 0.3294 0.0055  0.0632  0.0252  132 PHE   B O   
6068 C CB  . PHE   B 132 ? 0.2144 0.1801 0.2665 0.0045  0.0309  0.0191  132 PHE   B CB  
6069 C CG  . PHE   B 132 ? 0.2087 0.1833 0.2454 0.0089  0.0241  0.0278  132 PHE   B CG  
6070 C CD1 . PHE   B 132 ? 0.2141 0.1906 0.2906 0.0043  0.0317  0.0357  132 PHE   B CD1 
6071 C CD2 . PHE   B 132 ? 0.2104 0.1861 0.2247 0.0090  0.0127  0.0293  132 PHE   B CD2 
6072 C CE1 . PHE   B 132 ? 0.2230 0.1961 0.3138 -0.0024 0.0218  0.0405  132 PHE   B CE1 
6073 C CE2 . PHE   B 132 ? 0.2230 0.1873 0.2487 0.0171  0.0009  0.0277  132 PHE   B CE2 
6074 C CZ  . PHE   B 132 ? 0.2254 0.1868 0.2882 0.0011  0.0016  0.0421  132 PHE   B CZ  
6085 N N   . GLY   B 133 ? 0.2503 0.1947 0.2997 -0.0014 0.0313  0.0509  133 GLY   B N   
6086 C CA  . GLY   B 133 ? 0.2532 0.1982 0.3205 -0.0123 0.0401  0.0523  133 GLY   B CA  
6087 C C   . GLY   B 133 ? 0.2630 0.2065 0.3332 -0.0272 0.0481  0.0596  133 GLY   B C   
6088 O O   . GLY   B 133 ? 0.2866 0.2149 0.3731 -0.0381 0.0448  0.0739  133 GLY   B O   
6092 N N   . ALA   B 134 ? 0.2401 0.2109 0.3202 -0.0324 0.0481  0.0452  134 ALA   B N   
6093 C CA  . ALA   B 134 ? 0.2340 0.2084 0.3220 -0.0221 0.0454  0.0320  134 ALA   B CA  
6094 C C   . ALA   B 134 ? 0.2427 0.1915 0.3326 -0.0163 0.0260  0.0428  134 ALA   B C   
6095 O O   . ALA   B 134 ? 0.2542 0.2124 0.3414 -0.0044 0.0120  0.0282  134 ALA   B O   
6096 C CB  . ALA   B 134 ? 0.2325 0.2096 0.3231 -0.0121 0.0369  0.0092  134 ALA   B CB  
6102 N N   A ASP   B 135 ? 0.2544 0.1906 0.3372 -0.0145 0.0158  0.0448  135 ASP   B N   
6103 N N   B ASP   B 135 ? 0.2556 0.1858 0.3380 -0.0192 0.0166  0.0513  135 ASP   B N   
6104 C CA  A ASP   B 135 ? 0.2643 0.1873 0.3478 -0.0078 -0.0028 0.0379  135 ASP   B CA  
6105 C CA  B ASP   B 135 ? 0.2671 0.1773 0.3478 -0.0165 -0.0019 0.0495  135 ASP   B CA  
6106 C C   A ASP   B 135 ? 0.2475 0.1743 0.3423 -0.0001 -0.0163 0.0394  135 ASP   B C   
6107 C C   B ASP   B 135 ? 0.2479 0.1678 0.3432 -0.0050 -0.0157 0.0457  135 ASP   B C   
6108 O O   A ASP   B 135 ? 0.2370 0.1673 0.3495 -0.0028 -0.0099 0.0396  135 ASP   B O   
6109 O O   B ASP   B 135 ? 0.2359 0.1589 0.3534 -0.0088 -0.0082 0.0454  135 ASP   B O   
6110 C CB  A ASP   B 135 ? 0.2891 0.1994 0.3696 -0.0135 -0.0055 0.0317  135 ASP   B CB  
6111 C CB  B ASP   B 135 ? 0.2962 0.1808 0.3680 -0.0305 -0.0040 0.0527  135 ASP   B CB  
6112 C CG  A ASP   B 135 ? 0.3060 0.2007 0.3997 -0.0165 -0.0082 0.0281  135 ASP   B CG  
6113 C CG  B ASP   B 135 ? 0.3190 0.1742 0.3988 -0.0463 -0.0053 0.0578  135 ASP   B CG  
6114 O OD1 A ASP   B 135 ? 0.3167 0.1974 0.4093 -0.0138 -0.0112 0.0215  135 ASP   B OD1 
6115 O OD1 B ASP   B 135 ? 0.3304 0.1735 0.4063 -0.0358 -0.0102 0.0540  135 ASP   B OD1 
6116 O OD2 A ASP   B 135 ? 0.3157 0.2112 0.4223 -0.0094 -0.0116 0.0291  135 ASP   B OD2 
6117 O OD2 B ASP   B 135 ? 0.3322 0.1650 0.4204 -0.0555 -0.0100 0.0693  135 ASP   B OD2 
6126 N N   . PRO   B 136 ? 0.2414 0.1728 0.3482 0.0140  -0.0308 0.0333  136 PRO   B N   
6127 C CA  . PRO   B 136 ? 0.2162 0.1659 0.3370 0.0157  -0.0323 0.0091  136 PRO   B CA  
6128 C C   . PRO   B 136 ? 0.1923 0.1456 0.3381 0.0108  -0.0233 0.0089  136 PRO   B C   
6129 O O   . PRO   B 136 ? 0.1754 0.1437 0.3152 0.0079  -0.0111 0.0089  136 PRO   B O   
6130 C CB  . PRO   B 136 ? 0.2274 0.1935 0.3590 0.0307  -0.0400 0.0039  136 PRO   B CB  
6131 C CG  . PRO   B 136 ? 0.2482 0.2039 0.3900 0.0377  -0.0315 0.0142  136 PRO   B CG  
6132 C CD  . PRO   B 136 ? 0.2495 0.1969 0.3777 0.0433  -0.0193 0.0288  136 PRO   B CD  
6140 N N   . ILE   B 137 ? 0.1993 0.1478 0.3495 0.0095  -0.0279 0.0084  137 ILE   B N   
6141 C CA  . ILE   B 137 ? 0.2099 0.1383 0.3610 0.0007  -0.0199 0.0116  137 ILE   B CA  
6142 C C   . ILE   B 137 ? 0.1985 0.1438 0.3500 -0.0086 -0.0009 0.0169  137 ILE   B C   
6143 O O   . ILE   B 137 ? 0.1812 0.1481 0.3305 -0.0108 0.0077  0.0070  137 ILE   B O   
6144 C CB  . ILE   B 137 ? 0.2395 0.1408 0.4019 -0.0033 -0.0243 0.0042  137 ILE   B CB  
6145 C CG1 . ILE   B 137 ? 0.2630 0.1594 0.4452 0.0042  -0.0150 -0.0071 137 ILE   B CG1 
6146 C CG2 . ILE   B 137 ? 0.2504 0.1556 0.4185 -0.0269 -0.0259 0.0044  137 ILE   B CG2 
6147 C CD1 . ILE   B 137 ? 0.2882 0.1887 0.4859 0.0138  -0.0095 -0.0012 137 ILE   B CD1 
6159 N N   . HIS   B 138 ? 0.2026 0.1515 0.3539 -0.0062 0.0111  0.0171  138 HIS   B N   
6160 C CA  . HIS   B 138 ? 0.2149 0.1520 0.3543 -0.0062 0.0238  0.0149  138 HIS   B CA  
6161 C C   . HIS   B 138 ? 0.1998 0.1481 0.3441 -0.0058 0.0059  0.0241  138 HIS   B C   
6162 O O   . HIS   B 138 ? 0.1900 0.1538 0.3683 -0.0021 0.0165  0.0321  138 HIS   B O   
6163 C CB  . HIS   B 138 ? 0.2471 0.1640 0.3739 -0.0158 0.0553  0.0295  138 HIS   B CB  
6164 C CG  . HIS   B 138 ? 0.2754 0.1937 0.3798 -0.0131 0.0815  0.0474  138 HIS   B CG  
6165 N ND1 . HIS   B 138 ? 0.2918 0.2183 0.4031 -0.0016 0.0928  0.0479  138 HIS   B ND1 
6166 C CD2 . HIS   B 138 ? 0.2985 0.2114 0.3799 -0.0147 0.0878  0.0416  138 HIS   B CD2 
6167 C CE1 . HIS   B 138 ? 0.3008 0.2244 0.3988 -0.0063 0.1028  0.0448  138 HIS   B CE1 
6168 N NE2 . HIS   B 138 ? 0.3090 0.2187 0.3736 -0.0073 0.1050  0.0422  138 HIS   B NE2 
6176 N N   . SER   B 139 ? 0.1956 0.1354 0.3350 0.0019  0.0053  0.0199  139 SER   B N   
6177 C CA  . SER   B 139 ? 0.1925 0.1368 0.3085 -0.0022 0.0088  0.0039  139 SER   B CA  
6178 C C   . SER   B 139 ? 0.1660 0.1337 0.3084 -0.0011 -0.0013 -0.0015 139 SER   B C   
6179 O O   . SER   B 139 ? 0.1648 0.1329 0.3107 0.0037  -0.0130 0.0096  139 SER   B O   
6180 C CB  . SER   B 139 ? 0.1998 0.1370 0.3117 0.0034  -0.0060 -0.0010 139 SER   B CB  
6181 O OG  . SER   B 139 ? 0.2013 0.1347 0.3208 0.0029  -0.0200 0.0194  139 SER   B OG  
6187 N N   . LEU   B 140 ? 0.1659 0.1270 0.2973 -0.0086 0.0075  0.0058  140 LEU   B N   
6188 C CA  . LEU   B 140 ? 0.1580 0.1346 0.3044 -0.0051 0.0012  -0.0012 140 LEU   B CA  
6189 C C   . LEU   B 140 ? 0.1577 0.1337 0.2997 -0.0043 -0.0205 -0.0010 140 LEU   B C   
6190 O O   . LEU   B 140 ? 0.1533 0.1423 0.3002 -0.0014 -0.0119 0.0098  140 LEU   B O   
6191 C CB  . LEU   B 140 ? 0.1532 0.1355 0.3108 -0.0149 0.0124  -0.0131 140 LEU   B CB  
6192 C CG  . LEU   B 140 ? 0.1713 0.1366 0.3140 -0.0181 0.0100  -0.0006 140 LEU   B CG  
6193 C CD1 . LEU   B 140 ? 0.1882 0.1464 0.3337 -0.0210 0.0204  0.0016  140 LEU   B CD1 
6194 C CD2 . LEU   B 140 ? 0.2043 0.1453 0.3303 -0.0178 -0.0124 -0.0051 140 LEU   B CD2 
6206 N N   . ARG   B 141 ? 0.1473 0.1309 0.3239 -0.0089 -0.0116 0.0016  141 ARG   B N   
6207 C CA  . ARG   B 141 ? 0.1556 0.1346 0.3611 -0.0187 0.0060  0.0059  141 ARG   B CA  
6208 C C   . ARG   B 141 ? 0.1470 0.1371 0.3566 -0.0151 -0.0077 0.0044  141 ARG   B C   
6209 O O   . ARG   B 141 ? 0.1510 0.1411 0.3491 -0.0148 -0.0160 -0.0096 141 ARG   B O   
6210 C CB  . ARG   B 141 ? 0.1725 0.1441 0.3858 -0.0256 0.0179  0.0036  141 ARG   B CB  
6211 C CG  . ARG   B 141 ? 0.2016 0.1746 0.3864 -0.0228 0.0152  0.0014  141 ARG   B CG  
6212 C CD  . ARG   B 141 ? 0.2365 0.1939 0.3818 -0.0205 0.0038  -0.0102 141 ARG   B CD  
6213 N NE  . ARG   B 141 ? 0.2499 0.1967 0.3665 -0.0280 0.0125  -0.0172 141 ARG   B NE  
6214 C CZ  . ARG   B 141 ? 0.2672 0.1826 0.3441 -0.0294 0.0117  -0.0199 141 ARG   B CZ  
6215 N NH1 . ARG   B 141 ? 0.2836 0.1669 0.3398 -0.0375 0.0131  -0.0105 141 ARG   B NH1 
6216 N NH2 . ARG   B 141 ? 0.2769 0.1965 0.3539 -0.0162 0.0004  -0.0222 141 ARG   B NH2 
6230 N N   . VAL   B 142 ? 0.1610 0.1299 0.3366 -0.0079 0.0094  0.0034  142 VAL   B N   
6231 C CA  . VAL   B 142 ? 0.1510 0.1369 0.3323 -0.0067 0.0135  -0.0035 142 VAL   B CA  
6232 C C   . VAL   B 142 ? 0.1523 0.1312 0.3150 -0.0069 -0.0005 -0.0062 142 VAL   B C   
6233 O O   . VAL   B 142 ? 0.1615 0.1341 0.3229 0.0060  -0.0151 -0.0016 142 VAL   B O   
6234 C CB  . VAL   B 142 ? 0.1716 0.1522 0.3400 0.0009  0.0128  0.0068  142 VAL   B CB  
6235 C CG1 . VAL   B 142 ? 0.1669 0.1526 0.3381 0.0064  0.0232  -0.0047 142 VAL   B CG1 
6236 C CG2 . VAL   B 142 ? 0.1827 0.1534 0.3262 0.0032  0.0036  0.0080  142 VAL   B CG2 
6246 N N   . CYS   B 143 ? 0.1477 0.1343 0.2992 -0.0016 0.0062  0.0054  143 CYS   B N   
6247 C CA  . CYS   B 143 ? 0.1429 0.1342 0.3033 -0.0111 -0.0054 0.0043  143 CYS   B CA  
6248 C C   . CYS   B 143 ? 0.1394 0.1288 0.3087 -0.0077 -0.0111 -0.0017 143 CYS   B C   
6249 O O   . CYS   B 143 ? 0.1485 0.1407 0.3095 -0.0039 -0.0214 -0.0101 143 CYS   B O   
6250 C CB  . CYS   B 143 ? 0.1518 0.1459 0.3055 -0.0047 -0.0120 0.0099  143 CYS   B CB  
6251 S SG  . CYS   B 143 ? 0.1578 0.1639 0.2950 -0.0050 -0.0074 0.0050  143 CYS   B SG  
6257 N N   . VAL   B 144 ? 0.1486 0.1333 0.3317 -0.0126 -0.0179 -0.0120 144 VAL   B N   
6258 C CA  . VAL   B 144 ? 0.1553 0.1455 0.3448 -0.0131 -0.0261 -0.0138 144 VAL   B CA  
6259 C C   . VAL   B 144 ? 0.1482 0.1514 0.3458 -0.0116 -0.0285 0.0000  144 VAL   B C   
6260 O O   . VAL   B 144 ? 0.1644 0.1720 0.3563 0.0018  -0.0313 0.0255  144 VAL   B O   
6261 C CB  . VAL   B 144 ? 0.1790 0.1593 0.3885 -0.0131 -0.0240 -0.0364 144 VAL   B CB  
6262 C CG1 . VAL   B 144 ? 0.2024 0.2004 0.4038 -0.0081 -0.0230 -0.0332 144 VAL   B CG1 
6263 C CG2 . VAL   B 144 ? 0.1911 0.1553 0.3899 -0.0107 -0.0359 -0.0437 144 VAL   B CG2 
6273 N N   . ASP   B 145 ? 0.1511 0.1408 0.3620 -0.0114 -0.0204 -0.0201 145 ASP   B N   
6274 C CA  . ASP   B 145 ? 0.1517 0.1469 0.3845 -0.0086 -0.0129 -0.0131 145 ASP   B CA  
6275 C C   . ASP   B 145 ? 0.1536 0.1507 0.3688 -0.0074 -0.0148 -0.0050 145 ASP   B C   
6276 O O   . ASP   B 145 ? 0.1540 0.1647 0.4232 -0.0053 -0.0074 -0.0268 145 ASP   B O   
6277 C CB  . ASP   B 145 ? 0.1607 0.1632 0.4450 -0.0128 0.0181  0.0023  145 ASP   B CB  
6278 C CG  . ASP   B 145 ? 0.1743 0.1629 0.5114 -0.0238 0.0302  0.0007  145 ASP   B CG  
6279 O OD1 . ASP   B 145 ? 0.1805 0.1658 0.5255 -0.0268 -0.0114 -0.0101 145 ASP   B OD1 
6280 O OD2 . ASP   B 145 ? 0.2050 0.1695 0.5548 -0.0317 0.0577  0.0039  145 ASP   B OD2 
6285 N N   . THR   B 146 ? 0.1493 0.1381 0.3109 -0.0158 -0.0160 0.0025  146 THR   B N   
6286 C CA  . THR   B 146 ? 0.1594 0.1360 0.3004 -0.0128 -0.0115 0.0041  146 THR   B CA  
6287 C C   . THR   B 146 ? 0.1558 0.1348 0.3020 -0.0082 -0.0138 0.0136  146 THR   B C   
6288 O O   . THR   B 146 ? 0.1598 0.1320 0.3069 -0.0052 -0.0156 0.0108  146 THR   B O   
6289 C CB  . THR   B 146 ? 0.1615 0.1390 0.3013 -0.0065 0.0029  0.0074  146 THR   B CB  
6290 O OG1 . THR   B 146 ? 0.1614 0.1369 0.3083 -0.0058 0.0089  0.0136  146 THR   B OG1 
6291 C CG2 . THR   B 146 ? 0.1667 0.1472 0.2984 -0.0082 0.0055  -0.0069 146 THR   B CG2 
6299 N N   . VAL   B 147 ? 0.1544 0.1337 0.2947 -0.0040 -0.0058 0.0065  147 VAL   B N   
6300 C CA  . VAL   B 147 ? 0.1587 0.1360 0.2845 -0.0122 -0.0224 0.0062  147 VAL   B CA  
6301 C C   . VAL   B 147 ? 0.1535 0.1355 0.2795 -0.0135 -0.0252 -0.0055 147 VAL   B C   
6302 O O   . VAL   B 147 ? 0.1691 0.1509 0.2882 -0.0225 -0.0406 -0.0116 147 VAL   B O   
6303 C CB  . VAL   B 147 ? 0.1613 0.1449 0.2679 -0.0104 -0.0249 0.0034  147 VAL   B CB  
6304 C CG1 . VAL   B 147 ? 0.1624 0.1650 0.2468 -0.0145 -0.0234 0.0065  147 VAL   B CG1 
6305 C CG2 . VAL   B 147 ? 0.1544 0.1465 0.2689 -0.0129 -0.0022 0.0152  147 VAL   B CG2 
6315 N N   . ARG   B 148 ? 0.1581 0.1390 0.2852 -0.0116 -0.0387 -0.0135 148 ARG   B N   
6316 C CA  . ARG   B 148 ? 0.1557 0.1559 0.2707 -0.0115 -0.0432 -0.0075 148 ARG   B CA  
6317 C C   . ARG   B 148 ? 0.1607 0.1639 0.2411 -0.0115 -0.0514 0.0049  148 ARG   B C   
6318 O O   . ARG   B 148 ? 0.1770 0.2032 0.2644 -0.0262 -0.0566 0.0052  148 ARG   B O   
6319 C CB  . ARG   B 148 ? 0.1672 0.1611 0.2655 -0.0000 -0.0471 -0.0084 148 ARG   B CB  
6320 C CG  . ARG   B 148 ? 0.1695 0.1764 0.2868 -0.0038 -0.0489 -0.0298 148 ARG   B CG  
6321 C CD  . ARG   B 148 ? 0.1753 0.1916 0.2987 0.0112  -0.0492 -0.0262 148 ARG   B CD  
6322 N NE  . ARG   B 148 ? 0.1867 0.1924 0.2966 0.0187  -0.0479 -0.0230 148 ARG   B NE  
6323 C CZ  . ARG   B 148 ? 0.1762 0.1847 0.2884 0.0204  -0.0325 -0.0325 148 ARG   B CZ  
6324 N NH1 . ARG   B 148 ? 0.1628 0.1820 0.3012 0.0002  -0.0089 -0.0325 148 ARG   B NH1 
6325 N NH2 . ARG   B 148 ? 0.2045 0.1633 0.2878 0.0254  -0.0299 -0.0293 148 ARG   B NH2 
6339 N N   . THR   B 149 ? 0.1698 0.1511 0.2652 -0.0179 -0.0529 0.0046  149 THR   B N   
6340 C CA  . THR   B 149 ? 0.1724 0.1578 0.2482 -0.0197 -0.0487 0.0081  149 THR   B CA  
6341 C C   . THR   B 149 ? 0.1731 0.1559 0.2372 -0.0181 -0.0476 0.0011  149 THR   B C   
6342 O O   . THR   B 149 ? 0.1800 0.1476 0.2474 -0.0261 -0.0322 0.0074  149 THR   B O   
6343 C CB  . THR   B 149 ? 0.1807 0.1562 0.2476 -0.0218 -0.0489 0.0117  149 THR   B CB  
6344 O OG1 . THR   B 149 ? 0.1853 0.1612 0.2404 -0.0267 -0.0535 0.0098  149 THR   B OG1 
6345 C CG2 . THR   B 149 ? 0.2008 0.1672 0.2500 -0.0114 -0.0415 0.0122  149 THR   B CG2 
6353 N N   . ASN   B 150 ? 0.1791 0.1601 0.2237 -0.0194 -0.0479 -0.0058 150 ASN   B N   
6354 C CA  . ASN   B 150 ? 0.1917 0.1730 0.2196 -0.0294 -0.0461 -0.0007 150 ASN   B CA  
6355 C C   . ASN   B 150 ? 0.1817 0.1638 0.2128 -0.0248 -0.0377 -0.0097 150 ASN   B C   
6356 O O   . ASN   B 150 ? 0.1932 0.1632 0.2210 -0.0321 -0.0485 -0.0029 150 ASN   B O   
6357 C CB  . ASN   B 150 ? 0.2201 0.2055 0.2311 -0.0344 -0.0690 0.0204  150 ASN   B CB  
6358 C CG  . ASN   B 150 ? 0.2479 0.2486 0.2701 -0.0249 -0.0733 0.0331  150 ASN   B CG  
6359 O OD1 . ASN   B 150 ? 0.2579 0.2698 0.2829 -0.0290 -0.0857 0.0148  150 ASN   B OD1 
6360 N ND2 . ASN   B 150 ? 0.2644 0.2713 0.3094 -0.0160 -0.0652 0.0770  150 ASN   B ND2 
6367 N N   . VAL   B 151 ? 0.1748 0.1645 0.2230 -0.0231 -0.0433 0.0012  151 VAL   B N   
6368 C CA  . VAL   B 151 ? 0.1847 0.1670 0.2218 -0.0301 -0.0371 0.0012  151 VAL   B CA  
6369 C C   . VAL   B 151 ? 0.1765 0.1587 0.2202 -0.0336 -0.0489 -0.0012 151 VAL   B C   
6370 O O   . VAL   B 151 ? 0.1911 0.1678 0.2365 -0.0324 -0.0356 -0.0112 151 VAL   B O   
6371 C CB  . VAL   B 151 ? 0.2039 0.1737 0.2184 -0.0167 -0.0341 0.0071  151 VAL   B CB  
6372 C CG1 . VAL   B 151 ? 0.2111 0.1814 0.2620 -0.0161 -0.0273 -0.0014 151 VAL   B CG1 
6373 C CG2 . VAL   B 151 ? 0.2151 0.1912 0.2033 -0.0005 -0.0325 0.0064  151 VAL   B CG2 
6383 N N   . TYR   B 152 ? 0.1750 0.1457 0.2143 -0.0261 -0.0383 -0.0011 152 TYR   B N   
6384 C CA  . TYR   B 152 ? 0.1867 0.1654 0.1925 -0.0314 -0.0226 -0.0099 152 TYR   B CA  
6385 C C   . TYR   B 152 ? 0.1837 0.1477 0.1871 -0.0289 -0.0190 -0.0107 152 TYR   B C   
6386 O O   . TYR   B 152 ? 0.1845 0.1494 0.1872 -0.0339 -0.0202 -0.0038 152 TYR   B O   
6387 C CB  . TYR   B 152 ? 0.2049 0.1831 0.1961 -0.0326 -0.0180 0.0011  152 TYR   B CB  
6388 C CG  . TYR   B 152 ? 0.2215 0.1965 0.1893 -0.0515 -0.0286 -0.0024 152 TYR   B CG  
6389 C CD1 . TYR   B 152 ? 0.2349 0.2154 0.1727 -0.0465 -0.0342 0.0007  152 TYR   B CD1 
6390 C CD2 . TYR   B 152 ? 0.2463 0.2175 0.1953 -0.0519 -0.0174 -0.0067 152 TYR   B CD2 
6391 C CE1 . TYR   B 152 ? 0.2548 0.2432 0.1878 -0.0408 -0.0396 0.0151  152 TYR   B CE1 
6392 C CE2 . TYR   B 152 ? 0.2575 0.2495 0.2003 -0.0547 -0.0319 -0.0142 152 TYR   B CE2 
6393 C CZ  . TYR   B 152 ? 0.2615 0.2614 0.1709 -0.0487 -0.0584 0.0142  152 TYR   B CZ  
6394 O OH  . TYR   B 152 ? 0.2824 0.2989 0.2128 -0.0410 -0.0591 0.0212  152 TYR   B OH  
6404 N N   . LEU   B 153 ? 0.1726 0.1393 0.1931 -0.0285 -0.0197 -0.0096 153 LEU   B N   
6405 C CA  . LEU   B 153 ? 0.1744 0.1379 0.2012 -0.0221 -0.0203 -0.0168 153 LEU   B CA  
6406 C C   . LEU   B 153 ? 0.1751 0.1426 0.2047 -0.0238 -0.0096 -0.0167 153 LEU   B C   
6407 O O   . LEU   B 153 ? 0.1845 0.1656 0.2113 -0.0204 -0.0067 -0.0327 153 LEU   B O   
6408 C CB  . LEU   B 153 ? 0.1805 0.1406 0.2186 -0.0325 -0.0098 -0.0056 153 LEU   B CB  
6409 C CG  . LEU   B 153 ? 0.1695 0.1512 0.2347 -0.0267 -0.0103 0.0009  153 LEU   B CG  
6410 C CD1 . LEU   B 153 ? 0.1828 0.1637 0.2408 -0.0243 -0.0170 0.0053  153 LEU   B CD1 
6411 C CD2 . LEU   B 153 ? 0.1679 0.1738 0.2574 -0.0280 0.0052  0.0100  153 LEU   B CD2 
6423 N N   . ALA   B 154 ? 0.1688 0.1372 0.2233 -0.0037 -0.0204 -0.0229 154 ALA   B N   
6424 C CA  . ALA   B 154 ? 0.1863 0.1562 0.2533 -0.0084 -0.0179 -0.0207 154 ALA   B CA  
6425 C C   . ALA   B 154 ? 0.2047 0.1558 0.2687 0.0032  -0.0320 -0.0348 154 ALA   B C   
6426 O O   . ALA   B 154 ? 0.2543 0.1541 0.2840 0.0080  -0.0290 -0.0163 154 ALA   B O   
6427 C CB  . ALA   B 154 ? 0.1810 0.1741 0.2691 -0.0110 -0.0202 -0.0269 154 ALA   B CB  
6433 N N   . VAL   B 155 ? 0.1625 0.1458 0.2728 -0.0014 -0.0055 -0.0218 155 VAL   B N   
6434 C CA  . VAL   B 155 ? 0.1548 0.1519 0.2957 -0.0042 -0.0114 -0.0198 155 VAL   B CA  
6435 C C   . VAL   B 155 ? 0.1525 0.1514 0.2944 -0.0010 -0.0072 -0.0245 155 VAL   B C   
6436 O O   . VAL   B 155 ? 0.1740 0.1698 0.3258 0.0046  -0.0071 -0.0469 155 VAL   B O   
6437 C CB  . VAL   B 155 ? 0.1619 0.1692 0.3289 -0.0098 -0.0319 0.0006  155 VAL   B CB  
6438 C CG1 . VAL   B 155 ? 0.1761 0.1659 0.3210 -0.0133 -0.0301 0.0023  155 VAL   B CG1 
6439 C CG2 . VAL   B 155 ? 0.1543 0.1859 0.3779 -0.0093 -0.0289 0.0241  155 VAL   B CG2 
6449 N N   . PHE   B 156 ? 0.1436 0.1583 0.3177 0.0025  -0.0077 -0.0226 156 PHE   B N   
6450 C CA  . PHE   B 156 ? 0.1437 0.1645 0.3546 0.0040  -0.0083 -0.0249 156 PHE   B CA  
6451 C C   . PHE   B 156 ? 0.1475 0.1850 0.3974 0.0044  -0.0113 -0.0509 156 PHE   B C   
6452 O O   . PHE   B 156 ? 0.1722 0.2052 0.4341 0.0243  -0.0059 -0.0622 156 PHE   B O   
6453 C CB  . PHE   B 156 ? 0.1528 0.1590 0.3456 -0.0010 -0.0208 -0.0087 156 PHE   B CB  
6454 C CG  . PHE   B 156 ? 0.1499 0.1801 0.3609 -0.0007 -0.0100 0.0106  156 PHE   B CG  
6455 C CD1 . PHE   B 156 ? 0.1578 0.2124 0.3935 0.0049  -0.0066 0.0394  156 PHE   B CD1 
6456 C CD2 . PHE   B 156 ? 0.1658 0.1979 0.3643 0.0056  -0.0081 0.0172  156 PHE   B CD2 
6457 C CE1 . PHE   B 156 ? 0.1699 0.2292 0.4065 0.0102  -0.0063 0.0497  156 PHE   B CE1 
6458 C CE2 . PHE   B 156 ? 0.1749 0.2084 0.3776 0.0095  -0.0084 0.0116  156 PHE   B CE2 
6459 C CZ  . PHE   B 156 ? 0.1619 0.2140 0.3971 0.0160  -0.0142 0.0330  156 PHE   B CZ  
6469 N N   . ASP   B 157 ? 0.1428 0.1723 0.4214 0.0147  -0.0315 -0.0222 157 ASP   B N   
6470 C CA  . ASP   B 157 ? 0.1634 0.1802 0.4595 0.0112  -0.0312 -0.0287 157 ASP   B CA  
6471 C C   . ASP   B 157 ? 0.1630 0.1756 0.4709 0.0037  -0.0265 -0.0590 157 ASP   B C   
6472 O O   . ASP   B 157 ? 0.1546 0.1663 0.4699 -0.0044 -0.0269 -0.0429 157 ASP   B O   
6473 C CB  . ASP   B 157 ? 0.1985 0.2049 0.4514 0.0056  -0.0524 -0.0065 157 ASP   B CB  
6474 C CG  . ASP   B 157 ? 0.2581 0.2273 0.4611 -0.0104 -0.0432 -0.0099 157 ASP   B CG  
6475 O OD1 . ASP   B 157 ? 0.2750 0.2225 0.4737 -0.0039 -0.0353 -0.0015 157 ASP   B OD1 
6476 O OD2 . ASP   B 157 ? 0.2939 0.2540 0.4821 -0.0074 -0.0305 -0.0097 157 ASP   B OD2 
6481 N N   . LYS   B 158 ? 0.1794 0.2085 0.4832 0.0001  -0.0107 -0.0970 158 LYS   B N   
6482 C CA  . LYS   B 158 ? 0.2020 0.2328 0.4846 -0.0006 0.0108  -0.1122 158 LYS   B CA  
6483 C C   . LYS   B 158 ? 0.1965 0.2096 0.4853 0.0002  -0.0023 -0.1028 158 LYS   B C   
6484 O O   . LYS   B 158 ? 0.1959 0.2090 0.5006 -0.0099 0.0016  -0.1028 158 LYS   B O   
6485 C CB  . LYS   B 158 ? 0.2371 0.2893 0.4789 -0.0050 0.0183  -0.1273 158 LYS   B CB  
6486 C CG  . LYS   B 158 ? 0.2820 0.3417 0.4815 -0.0061 0.0181  -0.1336 158 LYS   B CG  
6487 C CD  . LYS   B 158 ? 0.3112 0.3856 0.4889 -0.0086 0.0155  -0.1374 158 LYS   B CD  
6488 C CE  . LYS   B 158 ? 0.3336 0.4201 0.5052 -0.0068 0.0102  -0.1338 158 LYS   B CE  
6489 N NZ  . LYS   B 158 ? 0.3401 0.4411 0.5127 -0.0094 0.0136  -0.1310 158 LYS   B NZ  
6503 N N   . ASN   B 159 ? 0.1896 0.1914 0.5019 0.0012  -0.0188 -0.0801 159 ASN   B N   
6504 C CA  . ASN   B 159 ? 0.2212 0.1920 0.5208 0.0275  -0.0394 -0.0595 159 ASN   B CA  
6505 C C   . ASN   B 159 ? 0.1894 0.1662 0.5146 0.0186  -0.0566 -0.0441 159 ASN   B C   
6506 O O   . ASN   B 159 ? 0.1896 0.1635 0.5166 -0.0058 -0.0652 -0.0325 159 ASN   B O   
6507 C CB  . ASN   B 159 ? 0.2829 0.2346 0.5436 0.0532  -0.0563 -0.0358 159 ASN   B CB  
6508 C CG  . ASN   B 159 ? 0.3292 0.2916 0.5667 0.0727  -0.0784 -0.0203 159 ASN   B CG  
6509 O OD1 . ASN   B 159 ? 0.3377 0.2944 0.5698 0.0871  -0.0782 -0.0230 159 ASN   B OD1 
6510 N ND2 . ASN   B 159 ? 0.3645 0.3135 0.5783 0.0807  -0.0922 -0.0166 159 ASN   B ND2 
6517 N N   . LEU   B 160 ? 0.1766 0.1702 0.4985 0.0114  -0.0601 -0.0400 160 LEU   B N   
6518 C CA  . LEU   B 160 ? 0.1763 0.1634 0.4577 0.0077  -0.0560 -0.0250 160 LEU   B CA  
6519 C C   . LEU   B 160 ? 0.1708 0.1545 0.4396 -0.0018 -0.0366 -0.0281 160 LEU   B C   
6520 O O   . LEU   B 160 ? 0.1558 0.1700 0.4373 -0.0070 -0.0410 -0.0232 160 LEU   B O   
6521 C CB  . LEU   B 160 ? 0.1746 0.1875 0.4291 0.0061  -0.0562 -0.0216 160 LEU   B CB  
6522 C CG  . LEU   B 160 ? 0.1736 0.2030 0.4057 0.0090  -0.0485 -0.0032 160 LEU   B CG  
6523 C CD1 . LEU   B 160 ? 0.1959 0.2229 0.4111 -0.0009 -0.0367 0.0044  160 LEU   B CD1 
6524 C CD2 . LEU   B 160 ? 0.1778 0.2086 0.3921 0.0147  -0.0341 -0.0074 160 LEU   B CD2 
6536 N N   . TYR   B 161 ? 0.1652 0.1681 0.4434 -0.0136 -0.0025 -0.0564 161 TYR   B N   
6537 C CA  . TYR   B 161 ? 0.1818 0.1678 0.4214 -0.0202 0.0216  -0.0633 161 TYR   B CA  
6538 C C   . TYR   B 161 ? 0.1844 0.1584 0.4169 -0.0203 0.0220  -0.0530 161 TYR   B C   
6539 O O   . TYR   B 161 ? 0.1889 0.1620 0.4037 -0.0240 0.0112  -0.0412 161 TYR   B O   
6540 C CB  . TYR   B 161 ? 0.2013 0.1792 0.4064 -0.0286 0.0389  -0.0684 161 TYR   B CB  
6541 C CG  . TYR   B 161 ? 0.2363 0.1889 0.3879 -0.0385 0.0400  -0.0739 161 TYR   B CG  
6542 C CD1 . TYR   B 161 ? 0.2395 0.1870 0.3748 -0.0479 0.0534  -0.0689 161 TYR   B CD1 
6543 C CD2 . TYR   B 161 ? 0.2608 0.1953 0.3756 -0.0377 0.0295  -0.0726 161 TYR   B CD2 
6544 C CE1 . TYR   B 161 ? 0.2722 0.2189 0.3750 -0.0487 0.0514  -0.0720 161 TYR   B CE1 
6545 C CE2 . TYR   B 161 ? 0.2877 0.2240 0.3707 -0.0408 0.0356  -0.0795 161 TYR   B CE2 
6546 C CZ  . TYR   B 161 ? 0.2892 0.2308 0.3685 -0.0619 0.0363  -0.0714 161 TYR   B CZ  
6547 O OH  . TYR   B 161 ? 0.3233 0.2593 0.4018 -0.0609 0.0395  -0.0657 161 TYR   B OH  
6557 N N   . ASP   B 162 ? 0.1925 0.1624 0.4395 -0.0160 0.0031  -0.0714 162 ASP   B N   
6558 C CA  . ASP   B 162 ? 0.1925 0.1680 0.4373 -0.0089 -0.0086 -0.0689 162 ASP   B CA  
6559 C C   . ASP   B 162 ? 0.1883 0.1608 0.4209 -0.0056 -0.0264 -0.0381 162 ASP   B C   
6560 O O   . ASP   B 162 ? 0.1915 0.1628 0.4357 -0.0250 -0.0402 -0.0326 162 ASP   B O   
6561 C CB  . ASP   B 162 ? 0.2126 0.1883 0.4616 0.0012  -0.0107 -0.0895 162 ASP   B CB  
6562 C CG  . ASP   B 162 ? 0.2211 0.2146 0.4825 0.0090  -0.0078 -0.1017 162 ASP   B CG  
6563 O OD1 . ASP   B 162 ? 0.2353 0.2386 0.4755 0.0020  0.0157  -0.1048 162 ASP   B OD1 
6564 O OD2 . ASP   B 162 ? 0.2416 0.2368 0.5124 0.0304  -0.0102 -0.0988 162 ASP   B OD2 
6569 N N   A LYS   B 163 ? 0.1886 0.1525 0.4015 -0.0047 -0.0391 -0.0263 163 LYS   B N   
6570 N N   B LYS   B 163 ? 0.1876 0.1499 0.4009 -0.0049 -0.0412 -0.0244 163 LYS   B N   
6571 C CA  A LYS   B 163 ? 0.1993 0.1616 0.4005 -0.0144 -0.0297 -0.0125 163 LYS   B CA  
6572 C CA  B LYS   B 163 ? 0.1985 0.1576 0.4001 -0.0164 -0.0320 -0.0084 163 LYS   B CA  
6573 C C   A LYS   B 163 ? 0.1729 0.1549 0.3882 -0.0184 -0.0286 -0.0013 163 LYS   B C   
6574 C C   B LYS   B 163 ? 0.1722 0.1528 0.3887 -0.0192 -0.0315 0.0041  163 LYS   B C   
6575 O O   A LYS   B 163 ? 0.1663 0.1642 0.3949 -0.0259 -0.0348 0.0005  163 LYS   B O   
6576 O O   B LYS   B 163 ? 0.1653 0.1634 0.3981 -0.0258 -0.0404 0.0115  163 LYS   B O   
6577 C CB  A LYS   B 163 ? 0.2379 0.1975 0.4183 -0.0142 -0.0337 -0.0077 163 LYS   B CB  
6578 C CB  B LYS   B 163 ? 0.2376 0.1936 0.4180 -0.0170 -0.0356 -0.0012 163 LYS   B CB  
6579 C CG  A LYS   B 163 ? 0.2924 0.2567 0.4446 -0.0147 -0.0301 -0.0061 163 LYS   B CG  
6580 C CG  B LYS   B 163 ? 0.2953 0.2553 0.4448 -0.0188 -0.0317 0.0013  163 LYS   B CG  
6581 C CD  A LYS   B 163 ? 0.3385 0.3023 0.4730 -0.0189 -0.0266 -0.0078 163 LYS   B CD  
6582 C CD  B LYS   B 163 ? 0.3444 0.3058 0.4764 -0.0246 -0.0278 0.0016  163 LYS   B CD  
6583 C CE  A LYS   B 163 ? 0.3703 0.3347 0.4927 -0.0207 -0.0198 -0.0070 163 LYS   B CE  
6584 C CE  B LYS   B 163 ? 0.3784 0.3418 0.4984 -0.0282 -0.0201 0.0037  163 LYS   B CE  
6585 N NZ  A LYS   B 163 ? 0.3887 0.3505 0.5083 -0.0217 -0.0179 -0.0082 163 LYS   B NZ  
6586 N NZ  B LYS   B 163 ? 0.3982 0.3607 0.5160 -0.0302 -0.0177 0.0051  163 LYS   B NZ  
6613 N N   . LEU   B 164 ? 0.1587 0.1428 0.3764 -0.0184 -0.0309 -0.0020 164 LEU   B N   
6614 C CA  . LEU   B 164 ? 0.1582 0.1518 0.3590 -0.0177 -0.0363 -0.0063 164 LEU   B CA  
6615 C C   . LEU   B 164 ? 0.1767 0.1576 0.3653 -0.0234 -0.0509 -0.0035 164 LEU   B C   
6616 O O   . LEU   B 164 ? 0.1680 0.1796 0.4058 -0.0241 -0.0484 0.0031  164 LEU   B O   
6617 C CB  . LEU   B 164 ? 0.1530 0.1507 0.3427 -0.0081 -0.0224 0.0006  164 LEU   B CB  
6618 C CG  . LEU   B 164 ? 0.1595 0.1651 0.3432 -0.0071 -0.0165 0.0014  164 LEU   B CG  
6619 C CD1 . LEU   B 164 ? 0.1708 0.1704 0.3510 -0.0165 -0.0202 -0.0135 164 LEU   B CD1 
6620 C CD2 . LEU   B 164 ? 0.1791 0.1952 0.3454 0.0006  0.0044  -0.0065 164 LEU   B CD2 
6633 N N   . VAL   B 165 ? 0.2235 0.1589 0.3726 -0.0301 -0.0543 -0.0103 165 VAL   B N   
6634 C CA  . VAL   B 165 ? 0.2641 0.1775 0.3798 -0.0383 -0.0779 -0.0154 165 VAL   B CA  
6635 C C   . VAL   B 165 ? 0.2830 0.1885 0.4192 -0.0429 -0.1082 -0.0088 165 VAL   B C   
6636 O O   . VAL   B 165 ? 0.3058 0.2064 0.4382 -0.0531 -0.1172 0.0026  165 VAL   B O   
6637 C CB  . VAL   B 165 ? 0.2964 0.1938 0.3888 -0.0272 -0.0519 -0.0247 165 VAL   B CB  
6638 C CG1 . VAL   B 165 ? 0.3205 0.2080 0.4032 -0.0298 -0.0373 -0.0148 165 VAL   B CG1 
6639 C CG2 . VAL   B 165 ? 0.2935 0.1851 0.3804 -0.0242 -0.0481 -0.0311 165 VAL   B CG2 
6649 N N   A SER   B 166 ? 0.2838 0.1827 0.4358 -0.0377 -0.1114 -0.0217 166 SER   B N   
6650 N N   B SER   B 166 ? 0.2870 0.1798 0.4372 -0.0426 -0.1131 -0.0223 166 SER   B N   
6651 C CA  A SER   B 166 ? 0.2773 0.1890 0.4673 -0.0354 -0.0983 -0.0203 166 SER   B CA  
6652 C CA  B SER   B 166 ? 0.2834 0.1851 0.4712 -0.0452 -0.0985 -0.0189 166 SER   B CA  
6653 C C   A SER   B 166 ? 0.2582 0.1957 0.4878 -0.0439 -0.0938 0.0021  166 SER   B C   
6654 C C   B SER   B 166 ? 0.2622 0.1925 0.4922 -0.0547 -0.0884 0.0069  166 SER   B C   
6655 O O   A SER   B 166 ? 0.2602 0.2137 0.5154 -0.0535 -0.0987 -0.0129 166 SER   B O   
6656 O O   B SER   B 166 ? 0.2663 0.2090 0.5243 -0.0755 -0.0845 -0.0017 166 SER   B O   
6657 C CB  A SER   B 166 ? 0.2791 0.1853 0.4724 -0.0279 -0.0873 -0.0286 166 SER   B CB  
6658 C CB  B SER   B 166 ? 0.2893 0.1804 0.4785 -0.0425 -0.0899 -0.0271 166 SER   B CB  
6659 O OG  A SER   B 166 ? 0.2688 0.1792 0.4776 -0.0246 -0.0844 -0.0169 166 SER   B OG  
6660 O OG  B SER   B 166 ? 0.2824 0.1735 0.4896 -0.0440 -0.0872 -0.0131 166 SER   B OG  
6671 N N   . SER   B 167 ? 0.2338 0.1829 0.4756 -0.0502 -0.0991 0.0376  167 SER   B N   
6672 C CA  . SER   B 167 ? 0.2292 0.1993 0.4772 -0.0381 -0.0705 0.0561  167 SER   B CA  
6673 C C   . SER   B 167 ? 0.2168 0.2036 0.4599 -0.0488 -0.0728 0.0768  167 SER   B C   
6674 O O   . SER   B 167 ? 0.2153 0.2198 0.4647 -0.0578 -0.0660 0.0771  167 SER   B O   
6675 C CB  . SER   B 167 ? 0.2151 0.2098 0.4941 -0.0365 -0.0503 0.0445  167 SER   B CB  
6676 O OG  . SER   B 167 ? 0.2062 0.2169 0.5008 -0.0241 -0.0277 0.0353  167 SER   B OG  
6683 N N   . PHE   B 168 ? 0.2167 0.1999 0.4557 -0.0455 -0.0676 0.0777  168 PHE   B N   
6684 C CA  . PHE   B 168 ? 0.2169 0.1970 0.4125 -0.0521 -0.0498 0.0499  168 PHE   B CA  
6685 C C   . PHE   B 168 ? 0.1926 0.1982 0.3507 -0.0321 -0.0226 0.0200  168 PHE   B C   
6686 O O   . PHE   B 168 ? 0.2075 0.1778 0.3301 -0.0142 -0.0174 0.0075  168 PHE   B O   
6687 C CB  . PHE   B 168 ? 0.2360 0.1964 0.4173 -0.0597 -0.0589 0.0638  168 PHE   B CB  
6688 C CG  . PHE   B 168 ? 0.2608 0.1842 0.3935 -0.0572 -0.0618 0.0414  168 PHE   B CG  
6689 C CD1 . PHE   B 168 ? 0.2854 0.1884 0.3995 -0.0572 -0.0592 0.0381  168 PHE   B CD1 
6690 C CD2 . PHE   B 168 ? 0.2565 0.1806 0.3916 -0.0561 -0.0586 0.0339  168 PHE   B CD2 
6691 C CE1 . PHE   B 168 ? 0.2905 0.1922 0.3807 -0.0560 -0.0480 0.0353  168 PHE   B CE1 
6692 C CE2 . PHE   B 168 ? 0.2768 0.1782 0.3908 -0.0491 -0.0608 0.0169  168 PHE   B CE2 
6693 C CZ  . PHE   B 168 ? 0.2820 0.1822 0.3840 -0.0409 -0.0576 0.0286  168 PHE   B CZ  
6703 N N   A LEU   B 169 ? 0.2203 0.2137 0.3537 -0.0108 -0.0137 0.0069  169 LEU   B N   
6704 N N   B LEU   B 169 ? 0.2213 0.2117 0.3565 -0.0086 -0.0128 0.0074  169 LEU   B N   
6705 C CA  A LEU   B 169 ? 0.2634 0.2436 0.3739 -0.0009 -0.0135 -0.0175 169 LEU   B CA  
6706 C CA  B LEU   B 169 ? 0.2672 0.2414 0.3808 0.0020  -0.0112 -0.0175 169 LEU   B CA  
6707 C C   A LEU   B 169 ? 0.2907 0.2598 0.4042 0.0112  -0.0111 -0.0317 169 LEU   B C   
6708 C C   B LEU   B 169 ? 0.3015 0.2619 0.4201 0.0107  -0.0076 -0.0307 169 LEU   B C   
6709 O O   A LEU   B 169 ? 0.3060 0.2692 0.4269 0.0122  -0.0084 -0.0456 169 LEU   B O   
6710 O O   B LEU   B 169 ? 0.3207 0.2747 0.4407 0.0103  -0.0043 -0.0427 169 LEU   B O   
6711 C CB  A LEU   B 169 ? 0.2898 0.2728 0.3794 -0.0045 -0.0137 -0.0083 169 LEU   B CB  
6712 C CB  B LEU   B 169 ? 0.2908 0.2681 0.3832 0.0028  -0.0121 -0.0081 169 LEU   B CB  
6713 C CG  A LEU   B 169 ? 0.3164 0.2979 0.3934 -0.0049 -0.0161 -0.0071 169 LEU   B CG  
6714 C CG  B LEU   B 169 ? 0.3165 0.2924 0.3957 0.0044  -0.0126 -0.0060 169 LEU   B CG  
6715 C CD1 A LEU   B 169 ? 0.3284 0.3121 0.3982 -0.0059 -0.0220 0.0026  169 LEU   B CD1 
6716 C CD1 B LEU   B 169 ? 0.3284 0.3068 0.3970 0.0028  -0.0162 0.0021  169 LEU   B CD1 
6717 C CD2 A LEU   B 169 ? 0.3156 0.3031 0.3886 -0.0008 -0.0086 -0.0169 169 LEU   B CD2 
6718 C CD2 B LEU   B 169 ? 0.3152 0.2974 0.3921 0.0078  -0.0062 -0.0145 169 LEU   B CD2 
6719 O OXT A LEU   B 169 ? 0.3024 0.2658 0.4114 0.0288  -0.0075 -0.0323 169 LEU   B OXT 
6720 O OXT B LEU   B 169 ? 0.3150 0.2681 0.4381 0.0254  -0.0045 -0.0318 169 LEU   B OXT 
6743 N N2  B A1A50 C .   ? 0.2045 0.1947 0.1754 -0.0243 0.0222  0.0250  201 A1A50 A N2  
6744 C C3  B A1A50 C .   ? 0.2103 0.2035 0.2002 -0.0183 0.0146  0.0086  201 A1A50 A C3  
6745 C C6  B A1A50 C .   ? 0.1664 0.1798 0.1819 -0.0001 0.0006  0.0147  201 A1A50 A C6  
6746 C C9  B A1A50 C .   ? 0.1715 0.1597 0.2133 -0.0082 -0.0048 0.0231  201 A1A50 A C9  
6747 C C12 B A1A50 C .   ? 0.1632 0.1744 0.2084 -0.0012 0.0067  0.0084  201 A1A50 A C12 
6748 C C14 B A1A50 C .   ? 0.1645 0.1742 0.2052 -0.0092 0.0014  0.0068  201 A1A50 A C14 
6749 C C1  B A1A50 C .   ? 0.2383 0.2164 0.2509 0.0004  -0.0241 0.0201  201 A1A50 A C1  
6750 C C10 B A1A50 C .   ? 0.1617 0.1688 0.2123 -0.0154 -0.0089 0.0241  201 A1A50 A C10 
6751 C C11 B A1A50 C .   ? 0.1673 0.1765 0.2091 -0.0158 0.0090  0.0199  201 A1A50 A C11 
6752 C C13 B A1A50 C .   ? 0.1666 0.1797 0.2352 0.0131  -0.0070 -0.0045 201 A1A50 A C13 
6753 C C15 B A1A50 C .   ? 0.1855 0.1880 0.1724 -0.0287 0.0269  0.0198  201 A1A50 A C15 
6754 C C2  B A1A50 C .   ? 0.2156 0.1961 0.2059 -0.0167 0.0140  0.0066  201 A1A50 A C2  
6755 C C4  B A1A50 C .   ? 0.2024 0.2018 0.1886 -0.0234 0.0201  0.0195  201 A1A50 A C4  
6756 C C5  B A1A50 C .   ? 0.1837 0.1864 0.1523 -0.0274 0.0254  0.0076  201 A1A50 A C5  
6757 C C7  B A1A50 C .   ? 0.1637 0.1672 0.1707 -0.0112 0.0085  -0.0072 201 A1A50 A C7  
6758 C C8  B A1A50 C .   ? 0.1666 0.1666 0.1928 -0.0120 0.0035  0.0110  201 A1A50 A C8  
6759 N N1  B A1A50 C .   ? 0.2239 0.2014 0.2235 -0.0026 -0.0195 0.0194  201 A1A50 A N1  
6760 N N3  B A1A50 C .   ? 0.1804 0.1979 0.1894 -0.0006 0.0204  0.0139  201 A1A50 A N3  
6761 O O1  B A1A50 C .   ? 0.1840 0.2013 0.2365 0.0113  0.0214  0.0166  201 A1A50 A O1  
6762 O O2  B A1A50 C .   ? 0.1617 0.2009 0.2193 0.0073  0.0227  0.0438  201 A1A50 A O2  
6763 S S1  B A1A50 C .   ? 0.1685 0.1896 0.1850 0.0189  0.0187  0.0319  201 A1A50 A S1  
6764 S S2  B A1A50 C .   ? 0.1659 0.1731 0.2255 -0.0074 0.0114  0.0153  201 A1A50 A S2  
6779 O O   . HOH   D .   ? 0.5210 0.7158 0.4505 0.2782  -0.0163 -0.0836 301 HOH   A O   
6780 O O   . HOH   D .   ? 0.4598 0.8926 0.5520 -0.1378 0.0500  0.0355  302 HOH   A O   
6781 O O   . HOH   D .   ? 0.7200 0.5269 0.3966 0.2019  -0.1319 0.0788  303 HOH   A O   
6782 O O   . HOH   D .   ? 0.3245 0.5347 0.6894 0.0932  0.1052  0.1576  304 HOH   A O   
6783 O O   . HOH   D .   ? 0.7362 0.5708 0.5559 -0.1290 0.2213  0.1767  305 HOH   A O   
6784 O O   B HOH   D .   ? 0.2849 0.1752 0.3631 -0.0617 -0.0900 0.0440  306 HOH   A O   
6785 O O   . HOH   D .   ? 0.2393 0.2050 0.2923 0.0288  -0.0178 0.0353  307 HOH   A O   
6786 O O   . HOH   D .   ? 0.6947 0.6624 0.5551 -0.1298 -0.1172 -0.0382 308 HOH   A O   
6787 O O   . HOH   D .   ? 0.6241 0.4886 0.5558 -0.1351 0.0945  -0.0152 309 HOH   A O   
6788 O O   . HOH   D .   ? 0.6224 0.2827 0.7152 0.0739  0.0265  -0.0333 310 HOH   A O   
6789 O O   . HOH   D .   ? 0.5001 0.3930 0.3047 -0.0796 -0.1137 -0.0034 311 HOH   A O   
6790 O O   . HOH   D .   ? 0.6539 0.5995 0.4075 -0.0349 -0.0232 0.1156  312 HOH   A O   
6791 O O   . HOH   D .   ? 0.3421 0.8338 0.5906 -0.0665 -0.1020 0.2259  313 HOH   A O   
6792 O O   . HOH   D .   ? 0.3031 0.4294 0.1857 -0.0909 0.0173  0.0527  314 HOH   A O   
6793 O O   . HOH   D .   ? 0.2173 0.5099 0.3990 0.1132  0.0149  0.0746  315 HOH   A O   
6794 O O   . HOH   D .   ? 0.2293 0.2172 0.3813 -0.0481 0.0074  -0.0332 316 HOH   A O   
6795 O O   A HOH   D .   ? 0.3574 0.3540 0.2736 0.0210  0.0731  0.0044  317 HOH   A O   
6796 O O   . HOH   D .   ? 0.5145 0.3519 0.5020 -0.1247 0.0392  0.1074  318 HOH   A O   
6797 O O   A HOH   D .   ? 0.4292 0.1601 0.3969 0.0319  -0.0386 0.0295  319 HOH   A O   
6798 O O   A HOH   D .   ? 0.3373 0.2340 0.2180 -0.0305 0.0015  0.0213  320 HOH   A O   
6799 O O   . HOH   D .   ? 0.2019 0.2206 0.3418 -0.0370 -0.0063 0.0764  321 HOH   A O   
6800 O O   . HOH   D .   ? 0.6665 0.5040 0.5264 -0.0685 0.1642  0.2141  322 HOH   A O   
6801 O O   . HOH   D .   ? 0.2656 0.2563 0.2253 -0.0712 -0.0041 0.0506  323 HOH   A O   
6802 O O   . HOH   D .   ? 0.6514 0.7295 0.5308 -0.0483 0.1061  0.0039  324 HOH   A O   
6803 O O   . HOH   D .   ? 0.6136 0.5951 0.3666 -0.1399 0.1632  0.1028  325 HOH   A O   
6804 O O   A HOH   D .   ? 0.4616 0.1884 0.2549 0.0497  0.0703  0.0244  326 HOH   A O   
6805 O O   . HOH   D .   ? 0.4466 0.3262 0.4495 -0.0319 -0.1655 0.1208  327 HOH   A O   
6806 O O   . HOH   D .   ? 0.1861 0.1856 0.2957 -0.0292 -0.0043 -0.0012 328 HOH   A O   
6807 O O   . HOH   D .   ? 0.4864 0.2677 0.3580 -0.1194 0.0926  0.0074  329 HOH   A O   
6808 O O   . HOH   D .   ? 0.2716 0.5196 0.4233 0.0264  -0.0749 0.0093  330 HOH   A O   
6809 O O   . HOH   D .   ? 0.3791 0.5669 0.4874 -0.0969 0.0429  0.1017  331 HOH   A O   
6810 O O   A HOH   D .   ? 0.4370 0.5828 0.4911 -0.1325 0.1495  0.0795  332 HOH   A O   
6811 O O   B HOH   D .   ? 0.2572 0.1580 0.3757 -0.0800 -0.0700 -0.0230 333 HOH   A O   
6812 O O   . HOH   D .   ? 0.3410 0.5079 0.5386 0.1121  -0.0659 0.1434  334 HOH   A O   
6813 O O   . HOH   D .   ? 0.4009 0.4615 0.2977 -0.0360 0.0874  0.0024  335 HOH   A O   
6814 O O   . HOH   D .   ? 0.3035 0.2559 0.2919 -0.0397 -0.0420 0.0683  336 HOH   A O   
6815 O O   B HOH   D .   ? 0.1845 0.2359 0.3251 -0.0218 -0.0038 0.0360  337 HOH   A O   
6816 O O   . HOH   D .   ? 0.2527 0.2413 0.3052 0.0244  0.0126  0.0366  338 HOH   A O   
6817 O O   . HOH   D .   ? 0.2072 0.2222 0.4581 0.0281  0.1046  0.0101  339 HOH   A O   
6818 O O   . HOH   D .   ? 0.2194 0.3099 0.4018 -0.0308 0.0478  -0.0481 340 HOH   A O   
6819 O O   . HOH   D .   ? 0.1671 0.3262 0.2852 0.0080  0.0357  0.0590  341 HOH   A O   
6820 O O   . HOH   D .   ? 0.4180 0.5650 0.2956 -0.2207 -0.0556 -0.0380 342 HOH   A O   
6821 O O   . HOH   D .   ? 0.2707 0.4022 0.3869 0.0899  -0.0594 -0.0297 343 HOH   A O   
6822 O O   . HOH   D .   ? 0.4402 0.3320 0.5077 -0.0425 0.2237  0.0305  344 HOH   A O   
6823 O O   . HOH   D .   ? 0.4377 0.7872 0.5858 -0.0702 -0.1747 0.0944  345 HOH   A O   
6824 O O   . HOH   D .   ? 0.1505 0.1381 0.1715 -0.0025 0.0083  0.0130  346 HOH   A O   
6825 O O   . HOH   D .   ? 0.4200 0.6761 0.4956 0.0116  0.1806  -0.1027 347 HOH   A O   
6826 O O   . HOH   D .   ? 1.1302 1.0435 0.9348 0.0903  -0.0264 -0.0173 348 HOH   A O   
6827 O O   . HOH   D .   ? 0.3068 0.3768 0.5500 -0.0514 -0.1142 -0.0891 349 HOH   A O   
6828 O O   . HOH   D .   ? 0.3333 0.6460 0.2777 0.0944  0.0202  -0.1000 350 HOH   A O   
6829 O O   . HOH   D .   ? 0.2840 0.2021 0.3333 0.0504  -0.0698 -0.0177 351 HOH   A O   
6830 O O   . HOH   D .   ? 0.6747 0.5850 0.4806 0.1655  -0.1203 -0.1341 352 HOH   A O   
6831 O O   . HOH   D .   ? 0.1730 0.2373 0.2630 0.0150  -0.0109 0.0425  353 HOH   A O   
6832 O O   B HOH   D .   ? 0.3441 0.2090 0.2256 0.1055  -0.1051 0.0074  354 HOH   A O   
6833 O O   . HOH   D .   ? 0.2188 0.2708 0.2691 -0.0353 -0.0432 0.0587  355 HOH   A O   
6834 O O   . HOH   D .   ? 0.2718 0.2969 0.3637 -0.0229 -0.0305 -0.0909 356 HOH   A O   
6835 O O   A HOH   D .   ? 0.6389 0.4906 0.5815 -0.0250 -0.1016 -0.0074 357 HOH   A O   
6836 O O   . HOH   D .   ? 0.2558 0.4372 0.4074 -0.0453 0.0422  -0.0004 358 HOH   A O   
6837 O O   A HOH   D .   ? 0.1825 0.1128 0.3168 -0.0387 -0.0665 0.0061  359 HOH   A O   
6838 O O   . HOH   D .   ? 0.3004 0.3348 0.4940 -0.0328 -0.0937 -0.0818 360 HOH   A O   
6839 O O   . HOH   D .   ? 0.1967 0.2863 0.2295 0.0222  0.0096  0.0235  361 HOH   A O   
6840 O O   . HOH   D .   ? 0.2842 0.3090 0.3867 -0.0638 0.0282  -0.0388 362 HOH   A O   
6841 O O   . HOH   D .   ? 0.2154 0.3256 0.3909 0.0209  0.0732  -0.0764 363 HOH   A O   
6842 O O   . HOH   D .   ? 0.4386 0.5127 0.4924 0.2392  0.0357  -0.0080 364 HOH   A O   
6843 O O   . HOH   D .   ? 0.4102 0.2362 0.3236 0.0979  0.0322  0.0452  365 HOH   A O   
6844 O O   . HOH   D .   ? 0.4611 0.5714 0.5837 0.0892  0.0582  -0.1502 366 HOH   A O   
6845 O O   . HOH   D .   ? 0.7926 0.6017 0.5723 -0.1679 -0.1041 0.3069  367 HOH   A O   
6846 O O   . HOH   D .   ? 0.5096 0.3479 0.4439 -0.0953 0.0412  0.0587  368 HOH   A O   
6847 O O   . HOH   D .   ? 0.1815 0.2107 0.2468 0.0324  0.0351  0.0471  369 HOH   A O   
6848 O O   . HOH   D .   ? 0.2791 0.5403 0.3941 0.0069  0.0633  0.2503  370 HOH   A O   
6849 O O   . HOH   D .   ? 0.4432 0.2979 0.4439 -0.1633 0.1634  -0.0732 371 HOH   A O   
6850 O O   . HOH   D .   ? 0.6448 0.4548 0.4009 -0.0247 -0.0169 0.1717  372 HOH   A O   
6851 O O   . HOH   D .   ? 0.1630 0.2054 0.3276 0.0026  -0.0061 0.0244  373 HOH   A O   
6852 O O   . HOH   D .   ? 0.1871 0.2163 0.2167 -0.0196 -0.0030 0.0525  374 HOH   A O   
6853 O O   . HOH   D .   ? 0.5056 0.2598 0.4314 0.0717  -0.0435 0.0387  375 HOH   A O   
6854 O O   . HOH   D .   ? 0.5067 0.5428 0.4217 0.0414  -0.0631 0.1076  376 HOH   A O   
6855 O O   A HOH   D .   ? 0.1652 0.2239 0.2673 0.0099  0.0320  0.0804  377 HOH   A O   
6856 O O   . HOH   D .   ? 0.4650 0.2742 0.5082 -0.1284 0.0743  0.0456  378 HOH   A O   
6857 O O   . HOH   D .   ? 0.2863 0.5246 0.4531 -0.0179 0.0997  -0.1553 379 HOH   A O   
6858 O O   . HOH   D .   ? 0.1811 0.1572 0.2758 -0.0093 0.0100  0.0004  380 HOH   A O   
6859 O O   . HOH   D .   ? 0.1985 0.2935 0.3231 0.0361  0.0332  0.0728  381 HOH   A O   
6860 O O   . HOH   D .   ? 0.3735 0.6304 0.4417 0.2600  0.0361  -0.0392 382 HOH   A O   
6861 O O   B HOH   D .   ? 0.3350 0.2599 0.2319 -0.0828 -0.0761 -0.0029 383 HOH   A O   
6862 O O   . HOH   D .   ? 0.3133 0.3584 0.2389 0.0305  0.0651  0.0076  384 HOH   A O   
6863 O O   . HOH   D .   ? 0.1674 0.1748 0.2048 -0.0033 -0.0116 0.0001  385 HOH   A O   
6864 O O   . HOH   D .   ? 0.2292 0.2092 0.2731 0.0074  -0.0122 0.0349  386 HOH   A O   
6865 O O   A HOH   D .   ? 0.1173 0.1800 0.2059 0.0381  -0.0088 -0.0753 387 HOH   A O   
6866 O O   . HOH   D .   ? 0.3737 0.4726 0.4216 -0.1101 0.1607  -0.0533 388 HOH   A O   
6867 O O   . HOH   D .   ? 0.2153 0.2027 0.2196 0.0009  0.0287  0.0079  389 HOH   A O   
6868 O O   . HOH   D .   ? 0.3161 0.4347 0.3073 -0.0421 0.0981  -0.0411 390 HOH   A O   
6869 O O   A HOH   D .   ? 0.1862 0.1657 0.2365 0.0132  -0.0129 -0.0056 391 HOH   A O   
6870 O O   . HOH   D .   ? 0.1942 0.2245 0.3809 0.0344  0.0776  0.0880  392 HOH   A O   
6871 O O   A HOH   D .   ? 0.1479 0.1615 0.2617 -0.0035 -0.0203 0.0213  393 HOH   A O   
6872 O O   . HOH   D .   ? 0.2075 0.1866 0.1943 -0.0045 0.0244  0.0198  394 HOH   A O   
6873 O O   . HOH   D .   ? 0.5675 0.7766 0.4419 -0.0364 0.1397  0.0918  395 HOH   A O   
6874 O O   . HOH   D .   ? 0.2130 0.2245 0.2809 -0.0301 0.0045  0.0506  396 HOH   A O   
6875 O O   . HOH   D .   ? 0.3175 0.4294 0.3996 -0.1466 0.0991  -0.0244 397 HOH   A O   
6876 O O   . HOH   D .   ? 0.3373 0.5568 0.5019 0.1041  0.0734  -0.1206 398 HOH   A O   
6877 O O   B HOH   D .   ? 0.1767 0.1657 0.1914 0.0076  0.0592  -0.0167 399 HOH   A O   
6878 O O   . HOH   D .   ? 0.6929 0.8159 0.7103 0.0321  -0.1239 0.3246  400 HOH   A O   
6879 O O   . HOH   D .   ? 0.5431 0.6166 0.5310 -0.1227 -0.0920 0.2133  401 HOH   A O   
6880 O O   . HOH   D .   ? 0.1649 0.1708 0.2365 -0.0022 -0.0132 0.0089  402 HOH   A O   
6881 O O   . HOH   D .   ? 0.4108 0.3416 0.3486 -0.0149 -0.0314 0.1188  403 HOH   A O   
6882 O O   A HOH   D .   ? 0.2401 0.1963 0.2533 0.0204  0.0029  -0.0126 404 HOH   A O   
6883 O O   B HOH   D .   ? 0.1544 0.1440 0.1791 -0.0064 -0.0023 -0.0004 405 HOH   A O   
6884 O O   . HOH   D .   ? 0.5641 0.4673 0.4980 0.1027  -0.1493 0.1367  406 HOH   A O   
6885 O O   . HOH   D .   ? 0.4419 0.7686 0.6449 -0.0051 0.0292  0.0597  407 HOH   A O   
6886 O O   A HOH   D .   ? 0.1418 0.2713 0.2628 -0.0341 0.0629  0.0302  408 HOH   A O   
6887 O O   B HOH   D .   ? 0.2295 0.2696 0.2436 -0.0506 0.0172  0.0700  409 HOH   A O   
6888 O O   B HOH   D .   ? 0.1667 0.1634 0.2678 -0.0114 0.0079  0.0337  410 HOH   A O   
6889 O O   . HOH   D .   ? 0.2222 0.3009 0.3569 -0.0321 -0.0330 0.0436  411 HOH   A O   
6890 O O   . HOH   D .   ? 0.2865 0.2781 0.2814 -0.0705 -0.0629 0.0402  412 HOH   A O   
6891 O O   . HOH   D .   ? 0.7252 0.5522 0.3833 -0.2146 -0.0614 0.1582  413 HOH   A O   
6892 O O   A HOH   D .   ? 0.2159 0.1839 0.3389 -0.0236 0.0938  -0.0190 414 HOH   A O   
6893 O O   . HOH   D .   ? 0.2109 0.3642 0.3418 -0.0383 -0.0642 0.1097  415 HOH   A O   
6894 O O   . HOH   D .   ? 0.6287 0.6233 0.7148 -0.0941 -0.1229 0.2130  416 HOH   A O   
6895 O O   . HOH   D .   ? 0.1936 0.1521 0.1933 -0.0170 0.0134  0.0057  417 HOH   A O   
6896 O O   . HOH   D .   ? 0.3211 0.2198 0.3765 -0.0006 -0.0773 0.0406  418 HOH   A O   
6897 O O   . HOH   D .   ? 0.6004 0.7148 0.4029 0.0134  0.2636  -0.0713 419 HOH   A O   
6898 O O   A HOH   D .   ? 0.2785 0.2764 0.3158 -0.0412 -0.0521 -0.0202 420 HOH   A O   
6899 O O   . HOH   D .   ? 0.5929 0.3674 0.5364 0.0347  0.0456  0.0527  421 HOH   A O   
6900 O O   A HOH   D .   ? 0.1555 0.1537 0.1769 -0.0178 -0.0080 0.0127  422 HOH   A O   
6901 O O   . HOH   D .   ? 0.2639 0.2458 0.3266 -0.0555 -0.0012 0.0621  423 HOH   A O   
6902 O O   . HOH   D .   ? 0.4203 0.4472 0.2654 -0.0783 -0.0567 0.0614  424 HOH   A O   
6903 O O   . HOH   D .   ? 0.5712 0.4806 0.2400 -0.0358 0.0581  0.0513  425 HOH   A O   
6904 O O   . HOH   D .   ? 0.1817 0.2063 0.4283 0.0136  -0.0053 0.0449  426 HOH   A O   
6905 O O   . HOH   D .   ? 0.3136 0.6223 0.2148 -0.0226 0.0660  0.0420  427 HOH   A O   
6906 O O   . HOH   D .   ? 0.3547 0.3737 0.7035 0.0008  0.0832  -0.0633 428 HOH   A O   
6907 O O   . HOH   D .   ? 0.2624 0.4393 0.2910 0.1572  0.0069  0.0604  429 HOH   A O   
6908 O O   . HOH   D .   ? 0.3116 0.1480 0.2358 0.0138  -0.0454 0.0087  430 HOH   A O   
6909 O O   . HOH   D .   ? 0.3772 0.3517 0.2508 -0.1103 0.0029  0.1065  431 HOH   A O   
6910 O O   . HOH   D .   ? 0.3012 0.2666 0.5422 -0.0304 0.1426  0.0043  432 HOH   A O   
6911 O O   . HOH   D .   ? 0.5217 0.7063 0.3350 -0.1115 -0.0651 0.1669  433 HOH   A O   
6912 O O   A HOH   D .   ? 0.3381 0.2967 0.1983 0.1032  -0.0444 -0.0133 434 HOH   A O   
6913 O O   . HOH   D .   ? 0.1771 0.2203 0.3211 -0.0079 0.0102  0.0440  435 HOH   A O   
6914 O O   . HOH   D .   ? 0.3444 0.3860 0.5293 0.0271  -0.1550 0.1188  436 HOH   A O   
6915 O O   . HOH   D .   ? 0.7488 0.7809 0.8127 -0.1296 0.0122  -0.1309 437 HOH   A O   
6916 O O   . HOH   D .   ? 0.6515 0.5255 0.7326 0.1482  0.1378  -0.0904 438 HOH   A O   
6917 O O   A HOH   D .   ? 0.2074 0.1681 0.2038 0.0013  0.0104  -0.0128 439 HOH   A O   
6918 O O   . HOH   D .   ? 0.6259 0.8251 0.5180 0.2350  -0.1103 0.2391  440 HOH   A O   
6919 O O   A HOH   D .   ? 0.4313 0.2152 0.3531 0.0704  0.1522  0.0499  441 HOH   A O   
6920 O O   . HOH   D .   ? 0.3120 0.2022 0.3769 0.0143  -0.0352 0.0150  442 HOH   A O   
6921 O O   B HOH   D .   ? 0.1537 0.1572 0.2293 -0.0029 0.0202  0.0114  443 HOH   A O   
6922 O O   . HOH   D .   ? 0.4488 0.3739 0.3476 0.2273  -0.0653 -0.0571 444 HOH   A O   
6923 O O   A HOH   D .   ? 0.3915 0.3374 0.4523 0.0135  0.1659  -0.0542 445 HOH   A O   
6924 O O   . HOH   D .   ? 0.4274 0.2958 0.6347 -0.1216 -0.2415 0.1723  446 HOH   A O   
6925 O O   B HOH   D .   ? 0.2588 0.1544 0.2332 0.0100  0.0026  0.0086  447 HOH   A O   
6926 O O   . HOH   D .   ? 0.3593 0.3858 0.2961 -0.0749 0.0042  -0.0732 448 HOH   A O   
6927 O O   . HOH   D .   ? 0.8245 0.5269 0.4403 -0.1453 0.0733  0.1526  449 HOH   A O   
6928 O O   A HOH   D .   ? 0.3031 0.2187 0.3187 -0.0444 -0.1087 0.0774  450 HOH   A O   
6929 O O   B HOH   D .   ? 0.2330 0.2104 0.2202 0.0617  0.0024  -0.0045 451 HOH   A O   
6930 O O   . HOH   D .   ? 0.2874 0.2125 0.3473 0.0184  0.0268  0.0287  452 HOH   A O   
6931 O O   . HOH   D .   ? 0.5308 0.4963 0.4197 -0.0188 -0.1358 0.0101  453 HOH   A O   
6932 O O   . HOH   D .   ? 0.8109 0.6354 0.7345 0.0467  -0.0221 0.1531  454 HOH   A O   
6933 O O   . HOH   D .   ? 0.2051 0.2430 0.4877 0.0042  -0.0563 0.0886  455 HOH   A O   
6934 O O   . HOH   D .   ? 0.6682 0.6315 0.7586 -0.1402 -0.1159 -0.0495 456 HOH   A O   
6935 O O   . HOH   D .   ? 0.6702 0.5981 0.6270 -0.1514 -0.0922 -0.1345 457 HOH   A O   
6936 O O   . HOH   D .   ? 0.8098 0.6665 0.7012 0.0665  -0.1185 -0.0749 458 HOH   A O   
6937 O O   A HOH   D .   ? 0.2330 0.2473 0.4025 -0.0083 0.0717  0.0838  459 HOH   A O   
6938 O O   . HOH   D .   ? 0.6398 0.6830 0.4752 -0.1017 0.1109  0.0126  460 HOH   A O   
6939 O O   A HOH   D .   ? 0.3809 0.3606 0.3866 0.0965  -0.0830 0.1213  461 HOH   A O   
6940 O O   . HOH   D .   ? 0.5985 0.3753 0.4380 0.0387  0.1241  0.0272  462 HOH   A O   
6941 O O   . HOH   D .   ? 0.4765 0.3448 0.4300 0.0242  0.0039  0.0530  463 HOH   A O   
6942 O O   . HOH   D .   ? 0.4450 0.7908 0.4906 0.1021  -0.0026 0.0679  464 HOH   A O   
6943 O O   . HOH   D .   ? 0.7216 0.7348 0.4866 0.1830  -0.0247 -0.1385 465 HOH   A O   
6944 O O   B HOH   D .   ? 0.4093 0.3188 0.3447 -0.0242 -0.0449 -0.0488 466 HOH   A O   
6945 O O   . HOH   D .   ? 0.2835 0.2598 0.4332 -0.0359 0.0210  -0.0359 467 HOH   A O   
6946 O O   . HOH   D .   ? 0.4966 0.5767 0.5807 -0.1009 0.0683  -0.1744 468 HOH   A O   
6947 O O   . HOH   D .   ? 0.3797 0.4274 0.6907 -0.0829 0.1342  -0.0208 469 HOH   A O   
6948 O O   B HOH   D .   ? 0.2717 0.3394 0.3686 0.0548  -0.0510 0.0257  470 HOH   A O   
6949 O O   . HOH   D .   ? 0.3723 0.3885 0.4933 -0.1611 0.0716  -0.0960 471 HOH   A O   
6950 O O   . HOH   D .   ? 0.4499 0.5421 0.4307 0.0242  -0.0082 -0.0617 472 HOH   A O   
6951 O O   . HOH   D .   ? 0.4914 0.5190 0.7134 -0.0136 0.0017  0.1781  473 HOH   A O   
6952 O O   . HOH   D .   ? 0.3341 0.4767 0.5598 0.0652  -0.0018 -0.1786 474 HOH   A O   
6953 O O   . HOH   D .   ? 0.5768 0.3856 0.7596 0.0037  -0.1079 0.2158  475 HOH   A O   
6954 O O   . HOH   D .   ? 0.3955 0.7265 0.3958 -0.1217 -0.1064 0.2303  476 HOH   A O   
6955 O O   B HOH   D .   ? 0.3533 0.3234 0.5538 0.1061  0.0523  0.2060  477 HOH   A O   
6956 O O   . HOH   D .   ? 0.7902 0.8826 0.6177 0.0989  0.1138  0.1586  478 HOH   A O   
6957 O O   . HOH   D .   ? 0.6500 0.5645 0.4665 0.1249  0.1897  0.0747  479 HOH   A O   
6958 O O   . HOH   D .   ? 0.5946 0.6797 0.6308 0.0997  0.1685  -0.0668 480 HOH   A O   
6959 O O   . HOH   D .   ? 0.3019 0.1897 0.3693 0.0170  -0.1098 -0.0321 481 HOH   A O   
6960 O O   . HOH   D .   ? 0.5644 0.6154 0.5361 -0.0031 0.1353  0.0741  482 HOH   A O   
6961 O O   A HOH   D .   ? 0.2861 0.2834 0.4685 0.0388  -0.0924 -0.0252 483 HOH   A O   
6962 O O   B HOH   D .   ? 0.3139 0.3292 0.2862 0.0841  0.0512  0.0423  484 HOH   A O   
6963 O O   . HOH   D .   ? 0.5083 0.4710 0.5359 0.0550  -0.0036 -0.0457 485 HOH   A O   
6964 O O   B HOH   D .   ? 0.2845 0.2345 0.2326 -0.0393 -0.0323 0.0236  486 HOH   A O   
6965 O O   . HOH   D .   ? 0.4468 0.4998 0.2995 0.0542  0.0215  -0.0106 487 HOH   A O   
6966 O O   . HOH   D .   ? 0.5352 0.5086 0.5585 -0.2313 -0.0806 -0.0755 488 HOH   A O   
6967 O O   . HOH   D .   ? 0.7791 0.7281 0.8109 -0.1650 -0.1369 0.0949  489 HOH   A O   
6968 O O   A HOH   D .   ? 0.2757 0.3413 0.1956 0.0391  -0.0160 -0.0231 490 HOH   A O   
6969 O O   . HOH   D .   ? 0.5703 0.3717 0.4006 -0.0954 -0.0919 -0.0154 491 HOH   A O   
6970 O O   . HOH   D .   ? 0.5785 0.5248 0.5195 -0.0050 -0.0348 -0.0989 492 HOH   A O   
6971 O O   B HOH   D .   ? 0.1713 0.1904 0.2618 -0.0088 0.0140  0.0228  493 HOH   A O   
6972 O O   . HOH   D .   ? 0.5947 0.4263 0.3626 -0.0593 0.1254  -0.0054 494 HOH   A O   
6973 O O   . HOH   D .   ? 0.4354 0.5719 0.3767 -0.0645 -0.0207 -0.0472 495 HOH   A O   
6974 O O   . HOH   D .   ? 0.8060 0.4413 0.3650 0.0507  -0.1296 0.0365  496 HOH   A O   
6975 O O   . HOH   D .   ? 0.3717 0.4579 0.4627 -0.0477 0.1548  0.0439  497 HOH   A O   
6976 O O   . HOH   D .   ? 0.5233 0.4251 0.3313 -0.1247 0.1859  -0.0655 498 HOH   A O   
6977 O O   . HOH   D .   ? 0.7403 0.7155 0.4821 -0.0066 -0.1366 0.0770  499 HOH   A O   
6978 O O   . HOH   D .   ? 0.7118 0.7196 0.8055 0.1225  -0.1105 0.1407  500 HOH   A O   
6979 O O   . HOH   D .   ? 0.6134 0.4458 0.4688 -0.0916 -0.0343 -0.0259 501 HOH   A O   
6980 O O   . HOH   D .   ? 0.2930 0.4975 0.3898 0.0822  0.1060  0.2321  502 HOH   A O   
6981 O O   . HOH   D .   ? 0.2934 0.2998 0.7533 -0.0243 -0.1478 0.0262  503 HOH   A O   
6982 O O   . HOH   D .   ? 0.8328 0.7582 0.8115 0.0579  0.1323  -0.0858 504 HOH   A O   
6983 O O   . HOH   D .   ? 0.7330 0.8796 0.6389 -0.0891 0.1079  0.1915  505 HOH   A O   
6984 O O   B HOH   D .   ? 0.1827 0.3003 0.3089 -0.0179 -0.0700 0.0579  506 HOH   A O   
6985 O O   . HOH   D .   ? 0.3716 0.3293 0.6033 -0.0020 0.0146  0.0617  507 HOH   A O   
6986 O O   . HOH   D .   ? 0.4303 0.3045 0.6189 -0.0629 0.0251  0.0825  508 HOH   A O   
6987 O O   . HOH   D .   ? 0.4302 0.5301 0.5833 -0.1150 0.0855  -0.0338 509 HOH   A O   
6988 O O   . HOH   D .   ? 0.5565 0.3668 0.4876 -0.0306 0.1804  0.0067  510 HOH   A O   
6989 O O   . HOH   D .   ? 0.7499 0.2693 0.3593 -0.0510 0.0612  0.0167  511 HOH   A O   
6990 O O   . HOH   D .   ? 0.2893 0.4836 0.3573 0.0886  -0.0329 0.0695  512 HOH   A O   
6991 O O   . HOH   D .   ? 0.3191 0.4801 0.5974 0.0890  0.0094  0.0048  513 HOH   A O   
6992 O O   . HOH   D .   ? 0.5598 0.7889 0.5844 -0.0771 -0.0707 0.2477  514 HOH   A O   
6993 O O   . HOH   D .   ? 0.5326 0.4772 0.5581 -0.2095 -0.0542 0.0990  515 HOH   A O   
6994 O O   . HOH   D .   ? 0.6227 0.8994 0.6459 0.1044  -0.0381 0.1622  516 HOH   A O   
6995 O O   . HOH   D .   ? 0.6798 0.4529 0.5789 0.1274  -0.0351 0.0531  517 HOH   A O   
6996 O O   B HOH   D .   ? 0.2842 0.4358 0.5204 0.0554  0.0184  -0.0389 518 HOH   A O   
6997 O O   . HOH   D .   ? 0.3749 0.3823 0.3583 -0.0181 -0.0678 -0.0789 519 HOH   A O   
6998 O O   B HOH   D .   ? 0.3097 0.2608 0.2830 0.0106  0.0567  0.0429  520 HOH   A O   
6999 O O   . HOH   D .   ? 0.6185 0.7971 0.6981 0.3536  -0.0279 0.1904  521 HOH   A O   
7000 O O   . HOH   D .   ? 0.3467 0.2877 0.5023 0.0396  0.0546  0.0615  522 HOH   A O   
7001 O O   . HOH   D .   ? 0.5800 0.6262 0.3677 -0.0803 -0.0843 -0.1095 523 HOH   A O   
7002 O O   . HOH   D .   ? 0.4648 0.8430 0.4869 0.1062  0.0773  0.2547  524 HOH   A O   
7003 O O   . HOH   D .   ? 0.5354 0.7787 0.6289 0.0549  0.1901  -0.1004 525 HOH   A O   
7004 O O   . HOH   D .   ? 0.4782 0.7740 0.6469 -0.0597 -0.1061 0.0875  526 HOH   A O   
7005 O O   . HOH   D .   ? 0.4924 0.6388 0.5139 0.0974  -0.0557 0.1719  527 HOH   A O   
7006 O O   . HOH   D .   ? 0.2807 0.5628 0.6581 0.0370  -0.0649 0.2883  528 HOH   A O   
7007 O O   . HOH   E .   ? 0.2743 0.2472 0.3418 0.0103  0.0685  0.0355  201 HOH   B O   
7008 O O   . HOH   E .   ? 0.4224 0.4593 0.5197 -0.0831 0.0205  -0.1532 202 HOH   B O   
7009 O O   . HOH   E .   ? 0.8376 0.3631 0.5145 0.1032  0.0636  -0.0397 203 HOH   B O   
7010 O O   . HOH   E .   ? 0.4796 0.7307 0.5079 0.3168  -0.1045 -0.0084 204 HOH   B O   
7011 O O   . HOH   E .   ? 0.3384 0.4061 0.6989 -0.0514 -0.0276 -0.0728 205 HOH   B O   
7012 O O   . HOH   E .   ? 0.5683 0.4323 0.5151 -0.0061 -0.0031 -0.1974 206 HOH   B O   
7013 O O   . HOH   E .   ? 0.3803 0.4543 0.2526 -0.0276 -0.0125 -0.0687 207 HOH   B O   
7014 O O   . HOH   E .   ? 0.4611 0.5516 0.6065 0.2673  0.0929  -0.0612 208 HOH   B O   
7015 O O   . HOH   E .   ? 0.2868 0.7415 0.3973 0.1004  0.0238  0.2553  209 HOH   B O   
7016 O O   . HOH   E .   ? 0.5506 0.5571 0.4581 0.3038  -0.0015 0.0392  210 HOH   B O   
7017 O O   . HOH   E .   ? 0.2294 0.2786 0.3328 0.0010  0.0245  -0.0274 211 HOH   B O   
7018 O O   . HOH   E .   ? 0.2920 0.2170 0.6414 0.0086  0.1773  0.0674  212 HOH   B O   
7019 O O   . HOH   E .   ? 0.2745 0.2849 0.3968 -0.0637 0.0623  -0.0334 213 HOH   B O   
7020 O O   . HOH   E .   ? 0.1726 0.2129 0.4132 -0.0129 -0.0128 0.0359  214 HOH   B O   
7021 O O   . HOH   E .   ? 0.3498 0.5566 0.5438 -0.0287 0.1734  -0.1652 215 HOH   B O   
7022 O O   . HOH   E .   ? 0.5036 0.4167 0.6895 -0.0010 -0.1197 0.2834  216 HOH   B O   
7023 O O   . HOH   E .   ? 0.4620 0.5038 0.3698 0.0230  -0.0492 -0.0426 217 HOH   B O   
7024 O O   . HOH   E .   ? 0.2861 0.3185 0.6149 0.0551  -0.0572 0.0766  218 HOH   B O   
7025 O O   . HOH   E .   ? 0.4613 0.7184 0.4500 0.1704  0.0357  0.0483  219 HOH   B O   
7026 O O   . HOH   E .   ? 0.5233 0.5035 0.3640 -0.0219 -0.1259 0.0568  220 HOH   B O   
7027 O O   . HOH   E .   ? 0.4102 0.4169 0.4358 0.0252  -0.1226 0.0371  221 HOH   B O   
7028 O O   . HOH   E .   ? 0.6043 0.3216 0.3402 -0.1673 0.0137  -0.0006 222 HOH   B O   
7029 O O   . HOH   E .   ? 0.1939 0.2245 0.4083 -0.0200 0.0022  -0.0041 223 HOH   B O   
7030 O O   . HOH   E .   ? 0.5722 0.2384 0.4189 0.0001  -0.0390 0.0208  224 HOH   B O   
7031 O O   . HOH   E .   ? 0.1677 0.1695 0.2016 -0.0164 -0.0091 0.0009  225 HOH   B O   
7032 O O   . HOH   E .   ? 0.2657 0.2429 0.4845 -0.0283 -0.0024 -0.0563 226 HOH   B O   
7033 O O   . HOH   E .   ? 0.3316 0.5355 0.7517 0.0005  0.1347  0.0214  227 HOH   B O   
7034 O O   . HOH   E .   ? 0.2077 0.4043 0.3243 -0.0125 -0.0263 0.0420  228 HOH   B O   
7035 O O   . HOH   E .   ? 0.6926 0.6574 0.6523 0.0888  -0.0231 0.0563  229 HOH   B O   
7036 O O   . HOH   E .   ? 0.3550 0.2327 0.6206 -0.0166 0.2073  0.0200  230 HOH   B O   
7037 O O   . HOH   E .   ? 0.2553 0.2043 0.2710 -0.0226 0.0713  -0.0234 231 HOH   B O   
7038 O O   . HOH   E .   ? 0.2279 0.1527 0.4014 0.0125  -0.0681 -0.0160 232 HOH   B O   
7039 O O   . HOH   E .   ? 0.5721 0.2795 0.4175 -0.2060 -0.0004 0.0242  233 HOH   B O   
7040 O O   . HOH   E .   ? 0.5389 0.5345 0.6926 0.0288  -0.1608 -0.1159 234 HOH   B O   
7041 O O   . HOH   E .   ? 0.7643 0.5080 0.3915 -0.0918 -0.0647 0.0520  235 HOH   B O   
7042 O O   . HOH   E .   ? 0.3236 0.3452 0.3483 -0.1060 0.0182  -0.0466 236 HOH   B O   
7043 O O   . HOH   E .   ? 0.8037 0.6066 0.4430 -0.0570 0.0620  0.0490  237 HOH   B O   
7044 O O   . HOH   E .   ? 0.2891 0.7179 0.6098 0.2030  -0.0132 -0.0083 238 HOH   B O   
7045 O O   . HOH   E .   ? 0.2654 0.4212 0.2597 -0.0797 0.0010  0.0487  239 HOH   B O   
7046 O O   . HOH   E .   ? 0.5367 0.4645 0.4076 0.0285  0.1064  -0.1565 240 HOH   B O   
7047 O O   . HOH   E .   ? 0.2547 0.2185 0.2673 -0.0334 -0.0529 0.0280  241 HOH   B O   
7048 O O   . HOH   E .   ? 0.4320 0.2649 0.4648 0.0276  -0.1074 -0.1264 242 HOH   B O   
7049 O O   . HOH   E .   ? 0.4531 0.3359 0.2652 0.0668  0.0814  0.0535  243 HOH   B O   
7050 O O   . HOH   E .   ? 0.8074 0.5922 0.5170 0.2574  -0.0075 -0.1412 244 HOH   B O   
7051 O O   . HOH   E .   ? 0.3659 0.4348 0.2636 0.0039  0.0789  0.0428  245 HOH   B O   
7052 O O   . HOH   E .   ? 0.4192 0.2010 0.2411 0.0213  -0.0803 -0.0054 246 HOH   B O   
7053 O O   . HOH   E .   ? 0.5034 0.5601 0.3274 -0.0944 -0.0813 0.0127  247 HOH   B O   
7054 O O   . HOH   E .   ? 0.2541 0.2225 0.3159 0.0631  -0.0715 -0.0435 248 HOH   B O   
7055 O O   . HOH   E .   ? 0.2613 0.3974 0.3577 -0.0607 -0.0670 -0.0626 249 HOH   B O   
7056 O O   . HOH   E .   ? 0.2974 0.2294 0.3317 0.0778  0.0646  0.0102  250 HOH   B O   
7057 O O   . HOH   E .   ? 0.1848 0.1643 0.3421 -0.0093 -0.0035 -0.0078 251 HOH   B O   
7058 O O   . HOH   E .   ? 0.5709 0.4405 0.5223 -0.0708 0.0105  -0.1285 252 HOH   B O   
7059 O O   . HOH   E .   ? 0.3997 0.2717 0.4755 0.0656  -0.0636 -0.0691 253 HOH   B O   
7060 O O   . HOH   E .   ? 0.8357 0.7037 0.3656 0.0466  -0.0160 0.0582  254 HOH   B O   
7061 O O   . HOH   E .   ? 0.2256 0.1792 0.2593 -0.0283 -0.0537 0.0300  255 HOH   B O   
7062 O O   . HOH   E .   ? 0.1657 0.1453 0.2218 0.0017  -0.0236 0.0096  256 HOH   B O   
7063 O O   . HOH   E .   ? 0.2914 0.2774 0.3640 0.0306  0.0185  -0.0858 257 HOH   B O   
7064 O O   . HOH   E .   ? 0.1832 0.2037 0.3606 -0.0336 -0.0300 0.0052  258 HOH   B O   
7065 O O   . HOH   E .   ? 0.2953 0.4186 0.3414 -0.1042 -0.0554 -0.0016 259 HOH   B O   
7066 O O   . HOH   E .   ? 0.2411 0.2039 0.3791 -0.0010 -0.0658 -0.0148 260 HOH   B O   
7067 O O   . HOH   E .   ? 0.3974 0.4864 0.3587 -0.0228 -0.1182 0.0816  261 HOH   B O   
7068 O O   . HOH   E .   ? 0.3468 0.2001 0.6252 -0.0453 -0.1448 -0.0063 262 HOH   B O   
7069 O O   . HOH   E .   ? 0.3353 0.5054 0.3931 0.0285  0.1072  0.0003  263 HOH   B O   
7070 O O   . HOH   E .   ? 0.1521 0.1956 0.2713 -0.0071 0.0004  0.0136  264 HOH   B O   
7071 O O   . HOH   E .   ? 0.2646 0.2835 0.2601 -0.0011 -0.0219 0.0054  265 HOH   B O   
7072 O O   . HOH   E .   ? 0.2161 0.2015 0.2045 -0.0523 -0.0528 0.0103  266 HOH   B O   
7073 O O   . HOH   E .   ? 0.3260 0.6269 0.7048 -0.0044 0.0744  -0.1460 267 HOH   B O   
7074 O O   . HOH   E .   ? 0.4158 0.3056 0.3852 -0.0620 0.0138  -0.0682 268 HOH   B O   
7075 O O   . HOH   E .   ? 0.2290 0.5069 0.4809 -0.0572 -0.0196 -0.1511 269 HOH   B O   
7076 O O   . HOH   E .   ? 0.2782 0.2172 0.3350 -0.0674 0.0125  -0.0084 270 HOH   B O   
7077 O O   . HOH   E .   ? 0.1905 0.2540 0.3704 0.0185  -0.0008 0.0402  271 HOH   B O   
7078 O O   . HOH   E .   ? 0.2733 0.3081 0.2924 -0.0498 -0.0767 0.0135  272 HOH   B O   
7079 O O   . HOH   E .   ? 0.3432 0.7935 0.8356 0.2184  -0.0713 -0.1404 273 HOH   B O   
7080 O O   . HOH   E .   ? 0.4457 0.4630 0.4495 0.1711  -0.0343 -0.1489 274 HOH   B O   
7081 O O   . HOH   E .   ? 0.2421 0.1645 0.2941 -0.0253 -0.0116 0.0220  275 HOH   B O   
7082 O O   . HOH   E .   ? 0.4679 0.3998 0.4784 -0.1735 0.0957  -0.1363 276 HOH   B O   
7083 O O   . HOH   E .   ? 0.4111 0.2921 0.2438 0.0344  -0.0725 -0.0304 277 HOH   B O   
7084 O O   . HOH   E .   ? 0.2020 0.1564 0.3743 -0.0201 -0.0322 -0.0096 278 HOH   B O   
7085 O O   . HOH   E .   ? 0.1895 0.1757 0.3986 -0.0158 -0.0219 -0.0031 279 HOH   B O   
7086 O O   . HOH   E .   ? 0.2911 0.7877 0.2583 0.0498  -0.0532 -0.0965 280 HOH   B O   
7087 O O   . HOH   E .   ? 0.2273 0.2607 0.2742 -0.0414 -0.0460 -0.0364 281 HOH   B O   
7088 O O   . HOH   E .   ? 0.2939 0.3040 0.3424 0.0102  -0.1011 0.0226  282 HOH   B O   
7089 O O   . HOH   E .   ? 0.4075 0.2398 0.2454 0.0116  -0.0763 -0.0072 283 HOH   B O   
7090 O O   . HOH   E .   ? 0.1771 0.2272 0.2060 -0.0159 -0.0310 0.0022  284 HOH   B O   
7091 O O   . HOH   E .   ? 0.3150 0.3322 0.3616 -0.0338 0.0469  -0.1436 285 HOH   B O   
7092 O O   . HOH   E .   ? 0.6327 0.4159 0.3751 0.2905  0.0578  0.0616  286 HOH   B O   
7093 O O   . HOH   E .   ? 0.2903 0.4761 0.4017 -0.1028 0.0773  -0.1819 287 HOH   B O   
7094 O O   . HOH   E .   ? 0.3639 0.5194 0.4750 -0.0901 -0.1291 0.0767  288 HOH   B O   
7095 O O   . HOH   E .   ? 0.3658 0.5142 0.6657 -0.1389 -0.0639 0.1921  289 HOH   B O   
7096 O O   . HOH   E .   ? 0.2526 0.4729 0.6130 -0.0596 -0.0412 0.0687  290 HOH   B O   
7097 O O   . HOH   E .   ? 0.1842 0.1718 0.2263 -0.0070 -0.0039 -0.0059 291 HOH   B O   
7098 O O   . HOH   E .   ? 0.2591 0.3808 0.2999 0.0929  -0.0142 -0.0605 292 HOH   B O   
7099 O O   . HOH   E .   ? 0.4424 0.3623 0.4753 -0.0354 -0.0910 -0.0168 293 HOH   B O   
7100 O O   . HOH   E .   ? 0.3300 0.2437 0.5123 0.0010  0.0432  0.0733  294 HOH   B O   
7101 O O   . HOH   E .   ? 0.1875 0.4161 0.5736 0.0482  -0.0115 -0.1334 295 HOH   B O   
7102 O O   . HOH   E .   ? 0.5025 0.5005 0.2865 0.0162  0.1120  0.1025  296 HOH   B O   
7103 O O   . HOH   E .   ? 0.4093 0.2658 0.5168 -0.1209 -0.2424 0.1469  297 HOH   B O   
7104 O O   . HOH   E .   ? 0.5079 0.7107 0.5365 0.0413  -0.1877 -0.0542 298 HOH   B O   
7105 O O   . HOH   E .   ? 0.2560 0.1800 0.2721 0.0101  -0.0070 0.0179  299 HOH   B O   
7106 O O   . HOH   E .   ? 0.2483 0.1882 0.3139 -0.0250 -0.0446 0.0021  300 HOH   B O   
7107 O O   . HOH   E .   ? 0.2663 0.3592 0.5827 -0.0714 -0.0389 0.0281  301 HOH   B O   
7108 O O   . HOH   E .   ? 0.4401 0.6909 0.5249 0.1062  -0.0904 0.1927  302 HOH   B O   
7109 O O   . HOH   E .   ? 0.5416 0.4058 0.2904 0.1192  -0.1057 0.0433  303 HOH   B O   
7110 O O   . HOH   E .   ? 0.3977 0.1950 0.4118 0.0798  0.1082  0.0207  304 HOH   B O   
7111 O O   . HOH   E .   ? 0.1847 0.1730 0.3732 0.0158  -0.0199 0.0073  305 HOH   B O   
7112 O O   . HOH   E .   ? 0.2819 0.3529 0.3999 -0.0358 0.0833  -0.1056 306 HOH   B O   
7113 O O   . HOH   E .   ? 0.2529 0.3128 0.4207 0.0302  -0.0379 -0.0883 307 HOH   B O   
7114 O O   . HOH   E .   ? 0.2166 0.1825 0.3903 0.0248  -0.0650 0.0235  308 HOH   B O   
7115 O O   . HOH   E .   ? 0.5143 0.3233 0.2783 -0.1789 0.0631  -0.0292 309 HOH   B O   
7116 O O   . HOH   E .   ? 0.2492 0.2046 0.2498 -0.0101 0.0187  0.0201  310 HOH   B O   
7117 O O   . HOH   E .   ? 0.2524 0.3614 0.6928 0.0909  0.0141  -0.0309 311 HOH   B O   
7118 O O   . HOH   E .   ? 0.4134 0.2531 0.3202 0.1409  0.0941  0.0460  312 HOH   B O   
7119 O O   . HOH   E .   ? 0.3123 0.1608 0.3121 -0.0244 -0.0267 0.0365  313 HOH   B O   
7120 O O   . HOH   E .   ? 0.4041 0.3563 0.5231 -0.0683 -0.1009 0.1109  314 HOH   B O   
7121 O O   . HOH   E .   ? 0.4570 0.4122 0.4473 -0.2008 0.1150  -0.0392 315 HOH   B O   
7122 O O   . HOH   E .   ? 0.6814 0.6931 0.6228 0.2996  -0.0624 0.0359  316 HOH   B O   
7123 O O   . HOH   E .   ? 0.1885 0.2883 0.2866 -0.0201 -0.0240 0.0862  317 HOH   B O   
7124 O O   . HOH   E .   ? 0.1921 0.1855 0.3394 -0.0083 -0.0283 -0.0132 318 HOH   B O   
7125 O O   . HOH   E .   ? 0.3041 0.2209 0.5447 -0.0068 -0.0488 0.0611  319 HOH   B O   
7126 O O   . HOH   E .   ? 0.5242 0.3890 0.4497 -0.1092 -0.0073 0.0955  320 HOH   B O   
7127 O O   . HOH   E .   ? 0.6407 0.5076 0.7741 0.1381  -0.1391 0.2428  321 HOH   B O   
7128 O O   . HOH   E .   ? 0.3726 0.2695 0.2772 0.0388  -0.0246 0.0181  322 HOH   B O   
7129 O O   . HOH   E .   ? 0.3579 0.5524 0.8430 -0.0267 -0.0786 0.2561  323 HOH   B O   
7130 O O   . HOH   E .   ? 0.4555 0.3540 0.5124 0.0903  0.2126  0.1626  324 HOH   B O   
7131 O O   . HOH   E .   ? 0.1693 0.2124 0.3492 -0.0266 -0.0260 0.0004  325 HOH   B O   
7132 O O   . HOH   E .   ? 0.5644 0.4661 0.2706 -0.0396 -0.0603 -0.0599 326 HOH   B O   
7133 O O   . HOH   E .   ? 0.2684 0.2481 0.5892 -0.0764 -0.0205 0.1332  327 HOH   B O   
7134 O O   . HOH   E .   ? 0.2178 0.2008 0.3249 0.0283  0.0445  0.0294  328 HOH   B O   
7135 O O   . HOH   E .   ? 0.5248 0.4595 0.2602 0.0622  -0.0168 -0.0032 329 HOH   B O   
7136 O O   . HOH   E .   ? 0.3212 0.3660 0.5832 -0.0821 -0.1820 0.1890  330 HOH   B O   
7137 O O   . HOH   E .   ? 0.6236 0.4291 0.4986 0.1057  0.1520  0.2434  331 HOH   B O   
7138 O O   . HOH   E .   ? 0.5790 0.3238 0.3375 0.0401  0.0012  0.1045  332 HOH   B O   
7139 O O   . HOH   E .   ? 0.4489 0.4775 0.6103 0.0773  -0.0355 0.0986  333 HOH   B O   
7140 O O   . HOH   E .   ? 0.1942 0.1624 0.3171 0.0032  -0.0275 0.0215  334 HOH   B O   
7141 O O   . HOH   E .   ? 0.4029 0.6891 0.4192 -0.0814 -0.1036 -0.0755 335 HOH   B O   
7142 O O   . HOH   E .   ? 0.8761 0.2411 0.4496 0.0783  -0.1205 0.0040  336 HOH   B O   
7143 O O   . HOH   E .   ? 0.6133 0.5127 0.5978 0.0304  0.1306  -0.1110 337 HOH   B O   
7144 O O   . HOH   E .   ? 0.6886 0.4252 0.4666 -0.0647 -0.1033 -0.1376 338 HOH   B O   
7145 O O   . HOH   E .   ? 0.6688 0.6021 0.6162 -0.0664 -0.1127 0.2096  339 HOH   B O   
7146 O O   . HOH   E .   ? 0.5503 0.4193 0.3652 -0.0333 -0.1086 -0.0255 340 HOH   B O   
7147 O O   . HOH   E .   ? 0.5013 0.7900 0.4693 -0.0719 -0.0898 0.2286  341 HOH   B O   
7148 O O   . HOH   E .   ? 0.2958 0.2354 0.4275 0.0352  -0.1071 -0.0489 342 HOH   B O   
7149 O O   . HOH   E .   ? 0.3539 0.5297 0.5613 0.0294  -0.1106 -0.0072 343 HOH   B O   
7150 O O   . HOH   E .   ? 0.4747 0.5473 0.7939 -0.0608 -0.1149 -0.0318 344 HOH   B O   
7151 O O   . HOH   E .   ? 0.2448 0.2631 0.4522 -0.0105 0.0862  -0.0151 345 HOH   B O   
7152 O O   . HOH   E .   ? 0.6135 0.4142 0.4605 -0.0293 0.0621  -0.1877 346 HOH   B O   
7153 O O   . HOH   E .   ? 0.5089 0.7443 0.6114 -0.1327 -0.0075 0.1602  347 HOH   B O   
7154 O O   . HOH   E .   ? 0.4417 0.5224 0.6097 -0.0316 -0.0378 -0.1109 348 HOH   B O   
7155 O O   . HOH   E .   ? 0.2567 0.7126 0.3906 0.1506  -0.0697 -0.1741 349 HOH   B O   
7156 O O   . HOH   E .   ? 0.3581 0.2502 0.5070 -0.0661 -0.0732 -0.0359 350 HOH   B O   
7157 O O   . HOH   E .   ? 0.5608 0.5600 0.3857 -0.0707 -0.1116 0.0094  351 HOH   B O   
7158 O O   . HOH   E .   ? 0.2474 0.3726 0.6522 -0.0059 0.0339  0.0380  352 HOH   B O   
7159 O O   . HOH   E .   ? 0.4252 0.4805 0.5198 -0.1376 -0.0180 0.0012  353 HOH   B O   
7160 O O   . HOH   E .   ? 0.4065 0.2382 0.3083 -0.0655 0.0150  -0.0803 354 HOH   B O   
7161 O O   . HOH   E .   ? 0.5378 0.6111 0.4930 0.1992  -0.1297 0.1038  355 HOH   B O   
7162 O O   . HOH   E .   ? 0.6589 0.3862 0.5724 0.1016  0.2463  -0.0608 356 HOH   B O   
7163 O O   . HOH   E .   ? 0.3907 0.2801 0.4161 -0.0930 0.0063  -0.0527 357 HOH   B O   
7164 O O   . HOH   E .   ? 0.4487 0.5186 0.6057 -0.0362 0.0689  0.0902  358 HOH   B O   
7165 O O   . HOH   E .   ? 0.6759 0.6084 0.5048 -0.0642 0.0078  0.0811  359 HOH   B O   
7166 O O   . HOH   E .   ? 0.4962 0.4564 0.6700 -0.1122 0.1305  0.0303  360 HOH   B O   
7167 O O   . HOH   E .   ? 0.6385 0.3825 0.5129 0.0074  -0.1589 -0.0409 361 HOH   B O   
7168 O O   . HOH   E .   ? 0.2389 0.4629 0.7269 -0.0666 -0.1141 -0.0655 362 HOH   B O   
7169 O O   . HOH   E .   ? 0.5062 0.6721 0.3669 0.1603  -0.0165 0.0495  363 HOH   B O   
7170 O O   . HOH   E .   ? 0.6676 0.2395 0.3211 -0.0392 -0.0293 0.0213  364 HOH   B O   
7171 O O   . HOH   E .   ? 0.5750 0.6096 0.5955 -0.1227 -0.0530 -0.1050 365 HOH   B O   
7172 O O   . HOH   E .   ? 0.6288 0.3163 0.5216 -0.1996 0.0136  -0.0225 366 HOH   B O   
7173 O O   . HOH   E .   ? 0.5343 0.6161 0.5053 -0.0520 -0.0767 -0.0202 367 HOH   B O   
7174 O O   . HOH   E .   ? 0.5603 0.4761 0.3766 0.1361  -0.1603 0.0157  368 HOH   B O   
7175 O O   . HOH   E .   ? 0.4766 0.3224 0.4973 0.0635  -0.1062 -0.0102 369 HOH   B O   
7176 O O   . HOH   E .   ? 0.4832 0.5887 0.6032 0.2522  0.1233  0.1928  370 HOH   B O   
7177 O O   . HOH   E .   ? 0.6857 0.4213 0.3500 -0.0862 -0.1196 -0.0965 371 HOH   B O   
7178 O O   . HOH   E .   ? 0.4567 0.4093 0.4929 0.0584  -0.1390 -0.0500 372 HOH   B O   
7179 O O   . HOH   E .   ? 0.8458 0.7196 0.5363 0.2103  -0.0604 0.0629  373 HOH   B O   
7180 O O   . HOH   E .   ? 0.7130 0.5506 0.4952 0.1522  0.0220  0.0729  374 HOH   B O   
7181 O O   . HOH   E .   ? 0.4801 0.6679 0.6677 0.0459  0.0281  0.2902  375 HOH   B O   
7182 O O   . HOH   E .   ? 0.2398 0.4087 0.4995 0.0150  -0.0483 -0.0380 376 HOH   B O   
7183 O O   . HOH   E .   ? 0.7012 0.4834 0.5330 -0.0701 -0.0754 -0.0166 377 HOH   B O   
7184 O O   . HOH   E .   ? 0.6864 0.7994 0.5054 -0.1390 0.0242  -0.1370 378 HOH   B O   
7185 O O   . HOH   E .   ? 0.5157 0.7206 0.2942 -0.1090 0.0825  0.0483  379 HOH   B O   
7186 O O   . HOH   E .   ? 0.3330 0.2776 0.3090 -0.0020 0.0529  0.0098  380 HOH   B O   
7187 O O   . HOH   E .   ? 0.5267 0.6145 0.6332 0.1992  0.0595  0.1167  381 HOH   B O   
7188 O O   . HOH   E .   ? 0.7652 0.8097 0.8297 -0.1054 0.2465  0.1431  382 HOH   B O   
7189 O O   . HOH   E .   ? 0.7925 0.7091 0.5566 0.2839  0.1158  -0.0719 383 HOH   B O   
7190 O O   . HOH   E .   ? 0.6870 0.4436 0.4853 0.0353  0.0586  -0.1186 384 HOH   B O   
7191 O O   . HOH   E .   ? 0.2824 0.5808 0.4553 -0.0592 -0.1089 -0.0144 385 HOH   B O   
7192 O O   . HOH   E .   ? 0.4780 0.5509 0.4412 0.0397  -0.0994 -0.0760 386 HOH   B O   
7193 O O   . HOH   E .   ? 0.6067 0.9421 0.6368 0.0741  0.1324  -0.0190 387 HOH   B O   
7194 O O   . HOH   E .   ? 0.4949 0.4652 0.4785 0.0047  0.0441  -0.0307 388 HOH   B O   
7195 O O   . HOH   E .   ? 0.6807 0.4366 0.5161 -0.0649 0.0499  -0.0165 389 HOH   B O   
7196 O O   . HOH   E .   ? 0.4266 0.3010 0.4095 0.0953  -0.0871 -0.0174 390 HOH   B O   
7197 O O   . HOH   E .   ? 0.6401 0.3705 0.6253 0.0242  -0.0207 -0.0275 391 HOH   B O   
7198 O O   . HOH   E .   ? 0.2884 0.4287 0.7645 -0.1350 -0.0421 -0.0616 392 HOH   B O   
7199 O O   . HOH   E .   ? 0.3941 0.2568 0.5310 0.0152  0.0303  0.0684  393 HOH   B O   
7200 O O   . HOH   E .   ? 0.2180 0.2982 0.5391 -0.0476 -0.0767 -0.0129 394 HOH   B O   
7201 O O   . HOH   E .   ? 0.3602 0.4719 0.4752 0.0407  0.0307  -0.0792 395 HOH   B O   
7202 O O   . HOH   E .   ? 0.4896 0.5306 0.6018 -0.0840 0.0939  0.1445  396 HOH   B O   
7203 O O   . HOH   E .   ? 0.4714 0.6039 0.4034 0.1125  -0.0838 -0.1121 397 HOH   B O   
7204 O O   . HOH   E .   ? 0.6314 0.4707 0.4167 -0.2531 -0.0707 0.1772  398 HOH   B O   
7205 O O   . HOH   E .   ? 0.5434 0.7191 0.6821 -0.0164 -0.1523 0.2497  399 HOH   B O   
7206 O O   . HOH   E .   ? 0.6598 0.6363 0.4283 0.1473  0.0144  -0.0321 400 HOH   B O   
# 
