data_7HCH
# 
_entry.id   7HCH 
# 
_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   7HCH         pdb_00007hch 10.2210/pdb7hch/pdb 
WWPDB D_1001407299 ?            ?                   
# 
_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                        7HCH 
_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 '2-[(5,6-dimethylthieno[2,3-d]pyrimidin-4-yl)sulfanyl]benzoic acid' 316.398   2   ?                      ? ? ? 
3 water       nat water                                                               18.015    413 ?                      ? ? ? 
# 
_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 '2-[(5,6-dimethylthieno[2,3-d]pyrimidin-4-yl)sulfanyl]benzoic acid' A1A5C 
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 
A1A5C non-polymer         . '2-[(5,6-dimethylthieno[2,3-d]pyrimidin-4-yl)sulfanyl]benzoic acid' ? 'C15 H12 N2 O2 S2' 316.398 
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 A1A5C 1   201 201  A1A5C LA1 A . 
D 2 A1A5C 1   202 301  A1A5C LA2 A . 
E 3 HOH   1   301 292  HOH   HOH A . 
E 3 HOH   2   302 196  HOH   HOH A . 
E 3 HOH   3   303 1301 HOH   HOH A . 
E 3 HOH   4   304 493  HOH   HOH A . 
E 3 HOH   5   305 209  HOH   HOH A . 
E 3 HOH   6   306 1290 HOH   HOH A . 
E 3 HOH   7   307 1275 HOH   HOH A . 
E 3 HOH   8   308 625  HOH   HOH A . 
E 3 HOH   9   309 247  HOH   HOH A . 
E 3 HOH   10  310 229  HOH   HOH A . 
E 3 HOH   11  311 109  HOH   HOH A . 
E 3 HOH   12  312 86   HOH   HOH A . 
E 3 HOH   13  313 337  HOH   HOH A . 
E 3 HOH   14  314 21   HOH   HOH A . 
E 3 HOH   15  315 76   HOH   HOH A . 
E 3 HOH   16  316 236  HOH   HOH A . 
E 3 HOH   17  317 964  HOH   HOH A . 
E 3 HOH   18  318 225  HOH   HOH A . 
E 3 HOH   19  319 57   HOH   HOH A . 
E 3 HOH   20  320 105  HOH   HOH A . 
E 3 HOH   21  321 153  HOH   HOH A . 
E 3 HOH   22  322 296  HOH   HOH A . 
E 3 HOH   23  323 630  HOH   HOH A . 
E 3 HOH   24  324 1295 HOH   HOH A . 
E 3 HOH   25  325 70   HOH   HOH A . 
E 3 HOH   26  326 124  HOH   HOH A . 
E 3 HOH   27  327 15   HOH   HOH A . 
E 3 HOH   28  328 164  HOH   HOH A . 
E 3 HOH   29  329 1300 HOH   HOH A . 
E 3 HOH   30  330 192  HOH   HOH A . 
E 3 HOH   31  331 140  HOH   HOH A . 
E 3 HOH   32  332 33   HOH   HOH A . 
E 3 HOH   33  333 36   HOH   HOH A . 
E 3 HOH   34  334 662  HOH   HOH A . 
E 3 HOH   35  335 136  HOH   HOH A . 
E 3 HOH   36  336 39   HOH   HOH A . 
E 3 HOH   37  337 18   HOH   HOH A . 
E 3 HOH   38  338 469  HOH   HOH A . 
E 3 HOH   39  339 151  HOH   HOH A . 
E 3 HOH   40  340 155  HOH   HOH A . 
E 3 HOH   41  341 241  HOH   HOH A . 
E 3 HOH   42  342 148  HOH   HOH A . 
E 3 HOH   43  343 78   HOH   HOH A . 
E 3 HOH   44  344 165  HOH   HOH A . 
E 3 HOH   45  345 1283 HOH   HOH A . 
E 3 HOH   46  346 42   HOH   HOH A . 
E 3 HOH   47  347 139  HOH   HOH A . 
E 3 HOH   48  348 49   HOH   HOH A . 
E 3 HOH   49  349 66   HOH   HOH A . 
E 3 HOH   50  350 93   HOH   HOH A . 
E 3 HOH   51  351 396  HOH   HOH A . 
E 3 HOH   52  352 68   HOH   HOH A . 
E 3 HOH   53  353 354  HOH   HOH A . 
E 3 HOH   54  354 17   HOH   HOH A . 
E 3 HOH   55  355 278  HOH   HOH A . 
E 3 HOH   56  356 92   HOH   HOH A . 
E 3 HOH   57  357 4    HOH   HOH A . 
E 3 HOH   58  358 320  HOH   HOH A . 
E 3 HOH   59  359 2    HOH   HOH A . 
E 3 HOH   60  360 19   HOH   HOH A . 
E 3 HOH   61  361 162  HOH   HOH A . 
E 3 HOH   62  362 5    HOH   HOH A . 
E 3 HOH   63  363 138  HOH   HOH A . 
E 3 HOH   64  364 27   HOH   HOH A . 
E 3 HOH   65  365 45   HOH   HOH A . 
E 3 HOH   66  366 102  HOH   HOH A . 
E 3 HOH   67  367 939  HOH   HOH A . 
E 3 HOH   68  368 169  HOH   HOH A . 
E 3 HOH   69  369 461  HOH   HOH A . 
E 3 HOH   70  370 393  HOH   HOH A . 
E 3 HOH   71  371 34   HOH   HOH A . 
E 3 HOH   72  372 661  HOH   HOH A . 
E 3 HOH   73  373 56   HOH   HOH A . 
E 3 HOH   74  374 154  HOH   HOH A . 
E 3 HOH   75  375 81   HOH   HOH A . 
E 3 HOH   76  376 3    HOH   HOH A . 
E 3 HOH   77  377 186  HOH   HOH A . 
E 3 HOH   78  378 46   HOH   HOH A . 
E 3 HOH   79  379 96   HOH   HOH A . 
E 3 HOH   80  380 1289 HOH   HOH A . 
E 3 HOH   81  381 1308 HOH   HOH A . 
E 3 HOH   82  382 24   HOH   HOH A . 
E 3 HOH   83  383 8    HOH   HOH A . 
E 3 HOH   84  384 62   HOH   HOH A . 
E 3 HOH   85  385 159  HOH   HOH A . 
E 3 HOH   86  386 366  HOH   HOH A . 
E 3 HOH   87  387 1310 HOH   HOH A . 
E 3 HOH   88  388 281  HOH   HOH A . 
E 3 HOH   89  389 12   HOH   HOH A . 
E 3 HOH   90  390 218  HOH   HOH A . 
E 3 HOH   91  391 409  HOH   HOH A . 
E 3 HOH   92  392 74   HOH   HOH A . 
E 3 HOH   93  393 134  HOH   HOH A . 
E 3 HOH   94  394 40   HOH   HOH A . 
E 3 HOH   95  395 6    HOH   HOH A . 
E 3 HOH   96  396 116  HOH   HOH A . 
E 3 HOH   97  397 35   HOH   HOH A . 
E 3 HOH   98  398 199  HOH   HOH A . 
E 3 HOH   99  399 26   HOH   HOH A . 
E 3 HOH   100 400 6    HOH   HOH A . 
E 3 HOH   101 401 67   HOH   HOH A . 
E 3 HOH   102 402 58   HOH   HOH A . 
E 3 HOH   103 403 83   HOH   HOH A . 
E 3 HOH   104 404 405  HOH   HOH A . 
E 3 HOH   105 405 1315 HOH   HOH A . 
E 3 HOH   106 406 1068 HOH   HOH A . 
E 3 HOH   107 407 25   HOH   HOH A . 
E 3 HOH   108 408 212  HOH   HOH A . 
E 3 HOH   109 409 132  HOH   HOH A . 
E 3 HOH   110 410 1189 HOH   HOH A . 
E 3 HOH   111 411 122  HOH   HOH A . 
E 3 HOH   112 412 51   HOH   HOH A . 
E 3 HOH   113 413 582  HOH   HOH A . 
E 3 HOH   114 414 195  HOH   HOH A . 
E 3 HOH   115 415 121  HOH   HOH A . 
E 3 HOH   116 416 351  HOH   HOH A . 
E 3 HOH   117 417 397  HOH   HOH A . 
E 3 HOH   118 418 1286 HOH   HOH A . 
E 3 HOH   119 419 1222 HOH   HOH A . 
E 3 HOH   120 420 53   HOH   HOH A . 
E 3 HOH   121 421 381  HOH   HOH A . 
E 3 HOH   122 422 156  HOH   HOH A . 
E 3 HOH   123 423 1279 HOH   HOH A . 
E 3 HOH   124 424 115  HOH   HOH A . 
E 3 HOH   125 425 95   HOH   HOH A . 
E 3 HOH   126 426 333  HOH   HOH A . 
E 3 HOH   127 427 1309 HOH   HOH A . 
E 3 HOH   128 428 16   HOH   HOH A . 
E 3 HOH   129 429 85   HOH   HOH A . 
E 3 HOH   130 430 123  HOH   HOH A . 
E 3 HOH   131 431 1    HOH   HOH A . 
E 3 HOH   132 432 125  HOH   HOH A . 
E 3 HOH   133 433 303  HOH   HOH A . 
E 3 HOH   134 434 71   HOH   HOH A . 
E 3 HOH   135 435 1238 HOH   HOH A . 
E 3 HOH   136 436 7    HOH   HOH A . 
E 3 HOH   137 437 80   HOH   HOH A . 
E 3 HOH   138 438 952  HOH   HOH A . 
E 3 HOH   139 439 5    HOH   HOH A . 
E 3 HOH   140 440 73   HOH   HOH A . 
E 3 HOH   141 441 944  HOH   HOH A . 
E 3 HOH   142 442 188  HOH   HOH A . 
E 3 HOH   143 443 94   HOH   HOH A . 
E 3 HOH   144 444 576  HOH   HOH A . 
E 3 HOH   145 445 4    HOH   HOH A . 
E 3 HOH   146 446 104  HOH   HOH A . 
E 3 HOH   147 447 1313 HOH   HOH A . 
E 3 HOH   148 448 97   HOH   HOH A . 
E 3 HOH   149 449 330  HOH   HOH A . 
E 3 HOH   150 450 2    HOH   HOH A . 
E 3 HOH   151 451 1296 HOH   HOH A . 
E 3 HOH   152 452 1094 HOH   HOH A . 
E 3 HOH   153 453 1119 HOH   HOH A . 
E 3 HOH   154 454 79   HOH   HOH A . 
E 3 HOH   155 455 107  HOH   HOH A . 
E 3 HOH   156 456 509  HOH   HOH A . 
E 3 HOH   157 457 1134 HOH   HOH A . 
E 3 HOH   158 458 1276 HOH   HOH A . 
E 3 HOH   159 459 361  HOH   HOH A . 
E 3 HOH   160 460 726  HOH   HOH A . 
E 3 HOH   161 461 163  HOH   HOH A . 
E 3 HOH   162 462 408  HOH   HOH A . 
E 3 HOH   163 463 756  HOH   HOH A . 
E 3 HOH   164 464 3    HOH   HOH A . 
E 3 HOH   165 465 280  HOH   HOH A . 
E 3 HOH   166 466 342  HOH   HOH A . 
E 3 HOH   167 467 556  HOH   HOH A . 
E 3 HOH   168 468 63   HOH   HOH A . 
E 3 HOH   169 469 319  HOH   HOH A . 
E 3 HOH   170 470 801  HOH   HOH A . 
E 3 HOH   171 471 126  HOH   HOH A . 
E 3 HOH   172 472 250  HOH   HOH A . 
E 3 HOH   173 473 370  HOH   HOH A . 
E 3 HOH   174 474 1306 HOH   HOH A . 
E 3 HOH   175 475 1307 HOH   HOH A . 
E 3 HOH   176 476 224  HOH   HOH A . 
E 3 HOH   177 477 267  HOH   HOH A . 
E 3 HOH   178 478 695  HOH   HOH A . 
E 3 HOH   179 479 919  HOH   HOH A . 
E 3 HOH   180 480 674  HOH   HOH A . 
E 3 HOH   181 481 1287 HOH   HOH A . 
E 3 HOH   182 482 135  HOH   HOH A . 
E 3 HOH   183 483 202  HOH   HOH A . 
E 3 HOH   184 484 208  HOH   HOH A . 
E 3 HOH   185 485 309  HOH   HOH A . 
E 3 HOH   186 486 318  HOH   HOH A . 
E 3 HOH   187 487 326  HOH   HOH A . 
E 3 HOH   188 488 521  HOH   HOH A . 
E 3 HOH   189 489 315  HOH   HOH A . 
E 3 HOH   190 490 1314 HOH   HOH A . 
E 3 HOH   191 491 1299 HOH   HOH A . 
E 3 HOH   192 492 711  HOH   HOH A . 
E 3 HOH   193 493 805  HOH   HOH A . 
E 3 HOH   194 494 941  HOH   HOH A . 
E 3 HOH   195 495 152  HOH   HOH A . 
E 3 HOH   196 496 263  HOH   HOH A . 
E 3 HOH   197 497 331  HOH   HOH A . 
E 3 HOH   198 498 356  HOH   HOH A . 
E 3 HOH   199 499 1071 HOH   HOH A . 
E 3 HOH   200 500 180  HOH   HOH A . 
E 3 HOH   201 501 350  HOH   HOH A . 
E 3 HOH   202 502 371  HOH   HOH A . 
E 3 HOH   203 503 363  HOH   HOH A . 
E 3 HOH   204 504 1284 HOH   HOH A . 
E 3 HOH   205 505 313  HOH   HOH A . 
E 3 HOH   206 506 185  HOH   HOH A . 
E 3 HOH   207 507 376  HOH   HOH A . 
E 3 HOH   208 508 429  HOH   HOH A . 
E 3 HOH   209 509 772  HOH   HOH A . 
E 3 HOH   210 510 1074 HOH   HOH A . 
E 3 HOH   211 511 346  HOH   HOH A . 
E 3 HOH   212 512 1292 HOH   HOH A . 
E 3 HOH   213 513 1078 HOH   HOH A . 
F 3 HOH   1   201 64   HOH   HOH B . 
F 3 HOH   2   202 358  HOH   HOH B . 
F 3 HOH   3   203 398  HOH   HOH B . 
F 3 HOH   4   204 549  HOH   HOH B . 
F 3 HOH   5   205 900  HOH   HOH B . 
F 3 HOH   6   206 654  HOH   HOH B . 
F 3 HOH   7   207 743  HOH   HOH B . 
F 3 HOH   8   208 232  HOH   HOH B . 
F 3 HOH   9   209 364  HOH   HOH B . 
F 3 HOH   10  210 758  HOH   HOH B . 
F 3 HOH   11  211 1249 HOH   HOH B . 
F 3 HOH   12  212 240  HOH   HOH B . 
F 3 HOH   13  213 723  HOH   HOH B . 
F 3 HOH   14  214 353  HOH   HOH B . 
F 3 HOH   15  215 120  HOH   HOH B . 
F 3 HOH   16  216 264  HOH   HOH B . 
F 3 HOH   17  217 50   HOH   HOH B . 
F 3 HOH   18  218 276  HOH   HOH B . 
F 3 HOH   19  219 332  HOH   HOH B . 
F 3 HOH   20  220 272  HOH   HOH B . 
F 3 HOH   21  221 531  HOH   HOH B . 
F 3 HOH   22  222 1140 HOH   HOH B . 
F 3 HOH   23  223 444  HOH   HOH B . 
F 3 HOH   24  224 1278 HOH   HOH B . 
F 3 HOH   25  225 54   HOH   HOH B . 
F 3 HOH   26  226 131  HOH   HOH B . 
F 3 HOH   27  227 452  HOH   HOH B . 
F 3 HOH   28  228 343  HOH   HOH B . 
F 3 HOH   29  229 128  HOH   HOH B . 
F 3 HOH   30  230 72   HOH   HOH B . 
F 3 HOH   31  231 282  HOH   HOH B . 
F 3 HOH   32  232 75   HOH   HOH B . 
F 3 HOH   33  233 231  HOH   HOH B . 
F 3 HOH   34  234 127  HOH   HOH B . 
F 3 HOH   35  235 166  HOH   HOH B . 
F 3 HOH   36  236 82   HOH   HOH B . 
F 3 HOH   37  237 1    HOH   HOH B . 
F 3 HOH   38  238 110  HOH   HOH B . 
F 3 HOH   39  239 205  HOH   HOH B . 
F 3 HOH   40  240 325  HOH   HOH B . 
F 3 HOH   41  241 181  HOH   HOH B . 
F 3 HOH   42  242 69   HOH   HOH B . 
F 3 HOH   43  243 9    HOH   HOH B . 
F 3 HOH   44  244 14   HOH   HOH B . 
F 3 HOH   45  245 30   HOH   HOH B . 
F 3 HOH   46  246 144  HOH   HOH B . 
F 3 HOH   47  247 129  HOH   HOH B . 
F 3 HOH   48  248 31   HOH   HOH B . 
F 3 HOH   49  249 60   HOH   HOH B . 
F 3 HOH   50  250 300  HOH   HOH B . 
F 3 HOH   51  251 252  HOH   HOH B . 
F 3 HOH   52  252 150  HOH   HOH B . 
F 3 HOH   53  253 52   HOH   HOH B . 
F 3 HOH   54  254 47   HOH   HOH B . 
F 3 HOH   55  255 59   HOH   HOH B . 
F 3 HOH   56  256 103  HOH   HOH B . 
F 3 HOH   57  257 172  HOH   HOH B . 
F 3 HOH   58  258 133  HOH   HOH B . 
F 3 HOH   59  259 41   HOH   HOH B . 
F 3 HOH   60  260 10   HOH   HOH B . 
F 3 HOH   61  261 143  HOH   HOH B . 
F 3 HOH   62  262 20   HOH   HOH B . 
F 3 HOH   63  263 61   HOH   HOH B . 
F 3 HOH   64  264 271  HOH   HOH B . 
F 3 HOH   65  265 242  HOH   HOH B . 
F 3 HOH   66  266 391  HOH   HOH B . 
F 3 HOH   67  267 114  HOH   HOH B . 
F 3 HOH   68  268 84   HOH   HOH B . 
F 3 HOH   69  269 1106 HOH   HOH B . 
F 3 HOH   70  270 175  HOH   HOH B . 
F 3 HOH   71  271 347  HOH   HOH B . 
F 3 HOH   72  272 287  HOH   HOH B . 
F 3 HOH   73  273 11   HOH   HOH B . 
F 3 HOH   74  274 1312 HOH   HOH B . 
F 3 HOH   75  275 1277 HOH   HOH B . 
F 3 HOH   76  276 77   HOH   HOH B . 
F 3 HOH   77  277 117  HOH   HOH B . 
F 3 HOH   78  278 387  HOH   HOH B . 
F 3 HOH   79  279 1305 HOH   HOH B . 
F 3 HOH   80  280 302  HOH   HOH B . 
F 3 HOH   81  281 299  HOH   HOH B . 
F 3 HOH   82  282 22   HOH   HOH B . 
F 3 HOH   83  283 43   HOH   HOH B . 
F 3 HOH   84  284 235  HOH   HOH B . 
F 3 HOH   85  285 635  HOH   HOH B . 
F 3 HOH   86  286 32   HOH   HOH B . 
F 3 HOH   87  287 1066 HOH   HOH B . 
F 3 HOH   88  288 100  HOH   HOH B . 
F 3 HOH   89  289 221  HOH   HOH B . 
F 3 HOH   90  290 243  HOH   HOH B . 
F 3 HOH   91  291 704  HOH   HOH B . 
F 3 HOH   92  292 147  HOH   HOH B . 
F 3 HOH   93  293 89   HOH   HOH B . 
F 3 HOH   94  294 13   HOH   HOH B . 
F 3 HOH   95  295 1126 HOH   HOH B . 
F 3 HOH   96  296 106  HOH   HOH B . 
F 3 HOH   97  297 88   HOH   HOH B . 
F 3 HOH   98  298 99   HOH   HOH B . 
F 3 HOH   99  299 137  HOH   HOH B . 
F 3 HOH   100 300 216  HOH   HOH B . 
F 3 HOH   101 301 112  HOH   HOH B . 
F 3 HOH   102 302 311  HOH   HOH B . 
F 3 HOH   103 303 316  HOH   HOH B . 
F 3 HOH   104 304 297  HOH   HOH B . 
F 3 HOH   105 305 341  HOH   HOH B . 
F 3 HOH   106 306 38   HOH   HOH B . 
F 3 HOH   107 307 220  HOH   HOH B . 
F 3 HOH   108 308 48   HOH   HOH B . 
F 3 HOH   109 309 215  HOH   HOH B . 
F 3 HOH   110 310 142  HOH   HOH B . 
F 3 HOH   111 311 101  HOH   HOH B . 
F 3 HOH   112 312 160  HOH   HOH B . 
F 3 HOH   113 313 37   HOH   HOH B . 
F 3 HOH   114 314 118  HOH   HOH B . 
F 3 HOH   115 315 91   HOH   HOH B . 
F 3 HOH   116 316 23   HOH   HOH B . 
F 3 HOH   117 317 170  HOH   HOH B . 
F 3 HOH   118 318 416  HOH   HOH B . 
F 3 HOH   119 319 44   HOH   HOH B . 
F 3 HOH   120 320 717  HOH   HOH B . 
F 3 HOH   121 321 28   HOH   HOH B . 
F 3 HOH   122 322 1291 HOH   HOH B . 
F 3 HOH   123 323 1294 HOH   HOH B . 
F 3 HOH   124 324 177  HOH   HOH B . 
F 3 HOH   125 325 334  HOH   HOH B . 
F 3 HOH   126 326 141  HOH   HOH B . 
F 3 HOH   127 327 29   HOH   HOH B . 
F 3 HOH   128 328 182  HOH   HOH B . 
F 3 HOH   129 329 197  HOH   HOH B . 
F 3 HOH   130 330 339  HOH   HOH B . 
F 3 HOH   131 331 161  HOH   HOH B . 
F 3 HOH   132 332 55   HOH   HOH B . 
F 3 HOH   133 333 98   HOH   HOH B . 
F 3 HOH   134 334 1285 HOH   HOH B . 
F 3 HOH   135 335 445  HOH   HOH B . 
F 3 HOH   136 336 65   HOH   HOH B . 
F 3 HOH   137 337 207  HOH   HOH B . 
F 3 HOH   138 338 234  HOH   HOH B . 
F 3 HOH   139 339 1274 HOH   HOH B . 
F 3 HOH   140 340 1293 HOH   HOH B . 
F 3 HOH   141 341 362  HOH   HOH B . 
F 3 HOH   142 342 619  HOH   HOH B . 
F 3 HOH   143 343 203  HOH   HOH B . 
F 3 HOH   144 344 178  HOH   HOH B . 
F 3 HOH   145 345 463  HOH   HOH B . 
F 3 HOH   146 346 90   HOH   HOH B . 
F 3 HOH   147 347 1304 HOH   HOH B . 
F 3 HOH   148 348 960  HOH   HOH B . 
F 3 HOH   149 349 191  HOH   HOH B . 
F 3 HOH   150 350 1046 HOH   HOH B . 
F 3 HOH   151 351 623  HOH   HOH B . 
F 3 HOH   152 352 1280 HOH   HOH B . 
F 3 HOH   153 353 335  HOH   HOH B . 
F 3 HOH   154 354 304  HOH   HOH B . 
F 3 HOH   155 355 541  HOH   HOH B . 
F 3 HOH   156 356 87   HOH   HOH B . 
F 3 HOH   157 357 1077 HOH   HOH B . 
F 3 HOH   158 358 290  HOH   HOH B . 
F 3 HOH   159 359 389  HOH   HOH B . 
F 3 HOH   160 360 1072 HOH   HOH B . 
F 3 HOH   161 361 718  HOH   HOH B . 
F 3 HOH   162 362 283  HOH   HOH B . 
F 3 HOH   163 363 479  HOH   HOH B . 
F 3 HOH   164 364 898  HOH   HOH B . 
F 3 HOH   165 365 667  HOH   HOH B . 
F 3 HOH   166 366 615  HOH   HOH B . 
F 3 HOH   167 367 340  HOH   HOH B . 
F 3 HOH   168 368 373  HOH   HOH B . 
F 3 HOH   169 369 1316 HOH   HOH B . 
F 3 HOH   170 370 190  HOH   HOH B . 
F 3 HOH   171 371 310  HOH   HOH B . 
F 3 HOH   172 372 291  HOH   HOH B . 
F 3 HOH   173 373 1303 HOH   HOH B . 
F 3 HOH   174 374 431  HOH   HOH B . 
F 3 HOH   175 375 149  HOH   HOH B . 
F 3 HOH   176 376 183  HOH   HOH B . 
F 3 HOH   177 377 1173 HOH   HOH B . 
F 3 HOH   178 378 1163 HOH   HOH B . 
F 3 HOH   179 379 418  HOH   HOH B . 
F 3 HOH   180 380 1311 HOH   HOH B . 
F 3 HOH   181 381 1000 HOH   HOH B . 
F 3 HOH   182 382 176  HOH   HOH B . 
F 3 HOH   183 383 424  HOH   HOH B . 
F 3 HOH   184 384 470  HOH   HOH B . 
F 3 HOH   185 385 248  HOH   HOH B . 
F 3 HOH   186 386 1298 HOH   HOH B . 
F 3 HOH   187 387 491  HOH   HOH B . 
F 3 HOH   188 388 265  HOH   HOH B . 
F 3 HOH   189 389 981  HOH   HOH B . 
F 3 HOH   190 390 184  HOH   HOH B . 
F 3 HOH   191 391 360  HOH   HOH B . 
F 3 HOH   192 392 410  HOH   HOH B . 
F 3 HOH   193 393 355  HOH   HOH B . 
F 3 HOH   194 394 792  HOH   HOH B . 
F 3 HOH   195 395 566  HOH   HOH B . 
F 3 HOH   196 396 314  HOH   HOH B . 
F 3 HOH   197 397 274  HOH   HOH B . 
F 3 HOH   198 398 157  HOH   HOH B . 
F 3 HOH   199 399 321  HOH   HOH B . 
F 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           7HCH 
_cell.length_a           88.822 
_cell.length_b           88.822 
_cell.length_c           39.716 
_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                         7HCH 
_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          7HCH 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.16 
_exptl_crystal.density_percent_sol   43.01 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                               1 
_diffrn.crystal_id                       1 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.pdbx_serial_crystal_experiment   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2022-06-29 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HCH 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.410 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   156895 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.700 
_reflns.pdbx_Rmerge_I_obs            0.044 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.600 
_reflns.B_iso_Wilson_estimate        11.470 
_reflns.pdbx_redundancy              6.500 
_reflns.pdbx_Rrim_I_all              0.048 
_reflns.pdbx_Rpim_I_all              0.019 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1016809 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 1.020 1.040  ? 42520 7533 ? 0.791 ? ? ? 5.600 ? 1.600  ? ? ? ? ? ? 97.000 0.873 0.359 0.847 ? 
1 2 5.590 44.410 ? 7137  1041 ? 0.029 ? ? ? 6.900 ? 49.000 ? ? ? ? ? ? 99.900 0.032 0.012 0.998 ? 
# 
_refine.entry_id                                 7HCH 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             44.4100 
_refine.pdbx_ls_sigma_F                          1.360 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.5800 
_refine.ls_number_reflns_obs                     156813 
_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                          0.1434 
_refine.ls_R_factor_R_work                       0.1426 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1590 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7554 
_refine.ls_number_reflns_R_work                  149259 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               17.9710 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1100 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                55.170 
_refine.B_iso_min                                7.790 
_refine.pdbx_overall_phase_error                 16.6900 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0200 
_refine_hist.d_res_low                        44.4100 
_refine_hist.pdbx_number_atoms_ligand         64 
_refine_hist.number_atoms_solvent             413 
_refine_hist.number_atoms_total               3019 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           23.14 
_refine_hist.pdbx_B_iso_mean_solvent          29.19 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.R_factor_obs 
1.0200 1.0300  30 95.0000  4721 . 0.3906 0.4186 . 191 0.0000 4912 . 'X-RAY DIFFRACTION' . 
1.0300 1.0400  30 100.0000 5031 . 0.3074 0.3027 . 280 0.0000 5311 . 'X-RAY DIFFRACTION' . 
1.0400 1.0600  30 100.0000 4857 . 0.2500 0.2546 . 265 0.0000 5122 . 'X-RAY DIFFRACTION' . 
1.0600 1.0700  30 100.0000 4963 . 0.2201 0.2400 . 285 0.0000 5248 . 'X-RAY DIFFRACTION' . 
1.0700 1.0800  30 100.0000 4933 . 0.1876 0.2143 . 259 0.0000 5192 . 'X-RAY DIFFRACTION' . 
1.0800 1.1000  30 100.0000 5004 . 0.1784 0.2089 . 227 0.0000 5231 . 'X-RAY DIFFRACTION' . 
1.1000 1.1100  30 100.0000 4952 . 0.1607 0.1707 . 256 0.0000 5208 . 'X-RAY DIFFRACTION' . 
1.1100 1.1300  30 100.0000 5064 . 0.1489 0.1717 . 237 0.0000 5301 . 'X-RAY DIFFRACTION' . 
1.1300 1.1500  30 100.0000 4856 . 0.1398 0.1484 . 232 0.0000 5088 . 'X-RAY DIFFRACTION' . 
1.1500 1.1700  30 100.0000 5064 . 0.1312 0.1590 . 251 0.0000 5315 . 'X-RAY DIFFRACTION' . 
1.1700 1.1900  30 100.0000 4938 . 0.1290 0.1693 . 252 0.0000 5190 . 'X-RAY DIFFRACTION' . 
1.1900 1.2100  30 100.0000 4909 . 0.1227 0.1647 . 266 0.0000 5175 . 'X-RAY DIFFRACTION' . 
1.2100 1.2300  30 100.0000 5023 . 0.1205 0.1409 . 240 0.0000 5263 . 'X-RAY DIFFRACTION' . 
1.2300 1.2600  30 100.0000 4959 . 0.1256 0.1446 . 249 0.0000 5208 . 'X-RAY DIFFRACTION' . 
1.2600 1.2900  30 100.0000 4942 . 0.1272 0.1456 . 247 0.0000 5189 . 'X-RAY DIFFRACTION' . 
1.2900 1.3200  30 100.0000 5034 . 0.1272 0.1480 . 258 0.0000 5292 . 'X-RAY DIFFRACTION' . 
1.3200 1.3500  30 100.0000 4949 . 0.1322 0.1437 . 264 0.0000 5213 . 'X-RAY DIFFRACTION' . 
1.3500 1.3800  30 100.0000 4935 . 0.1245 0.1495 . 256 0.0000 5191 . 'X-RAY DIFFRACTION' . 
1.3800 1.4300  30 100.0000 5028 . 0.1201 0.1420 . 225 0.0000 5253 . 'X-RAY DIFFRACTION' . 
1.4300 1.4700  30 100.0000 5018 . 0.1198 0.1325 . 270 0.0000 5288 . 'X-RAY DIFFRACTION' . 
1.4700 1.5200  30 100.0000 4960 . 0.1163 0.1389 . 232 0.0000 5192 . 'X-RAY DIFFRACTION' . 
1.5200 1.5800  30 100.0000 5010 . 0.1184 0.1295 . 271 0.0000 5281 . 'X-RAY DIFFRACTION' . 
1.5900 1.6600  30 100.0000 4931 . 0.1198 0.1349 . 259 0.0000 5190 . 'X-RAY DIFFRACTION' . 
1.6600 1.7400  30 100.0000 5056 . 0.1282 0.1473 . 203 0.0000 5259 . 'X-RAY DIFFRACTION' . 
1.7400 1.8500  30 100.0000 4927 . 0.1329 0.1341 . 284 0.0000 5211 . 'X-RAY DIFFRACTION' . 
1.8500 2.0000  30 99.0000  4990 . 0.1356 0.1373 . 259 0.0000 5249 . 'X-RAY DIFFRACTION' . 
2.0000 2.2000  30 99.0000  4974 . 0.1395 0.1478 . 281 0.0000 5255 . 'X-RAY DIFFRACTION' . 
2.2000 2.5200  30 99.0000  5020 . 0.1405 0.1527 . 251 0.0000 5271 . 'X-RAY DIFFRACTION' . 
2.5200 3.1700  30 99.0000  5042 . 0.1523 0.1724 . 250 0.0000 5292 . 'X-RAY DIFFRACTION' . 
3.1700 44.4100 30 99.0000  5169 . 0.1494 0.1746 . 254 0.0000 5423 . 'X-RAY DIFFRACTION' . 
# 
_struct.entry_id                  7HCH 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0000317' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HCH 
_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 2 ? 
E N N 3 ? 
F 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 7HCH A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HCH 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 7HCH SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HCH MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HCH SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HCH MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HCH 
_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  ? ? 55.50 -133.09 
2 1 SER A 128 ? B 68.52 -4.49   
3 1 HIS B 86  ? ? 57.77 -128.26 
# 
_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 511 ? 5.82 . 
2 1 O ? A HOH 512 ? 5.98 . 
3 1 O ? A HOH 513 ? 7.49 . 
4 1 O ? B HOH 400 ? 6.41 . 
# 
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 
A1A5C N2   N Y N 1   
A1A5C C3   C Y N 2   
A1A5C C6   C Y N 3   
A1A5C C9   C Y N 4   
A1A5C C12  C Y N 5   
A1A5C C14  C Y N 6   
A1A5C C1   C N N 7   
A1A5C C10  C Y N 8   
A1A5C C11  C Y N 9   
A1A5C C13  C N N 10  
A1A5C C15  C Y N 11  
A1A5C C2   C Y N 12  
A1A5C C4   C N N 13  
A1A5C C5   C Y N 14  
A1A5C C7   C Y N 15  
A1A5C C8   C Y N 16  
A1A5C N1   N Y N 17  
A1A5C O1   O N N 18  
A1A5C O2   O N N 19  
A1A5C S1   S N N 20  
A1A5C S2   S Y N 21  
A1A5C H8   H N N 22  
A1A5C H11  H N N 23  
A1A5C H2   H N N 24  
A1A5C H3   H N N 25  
A1A5C H1   H N N 26  
A1A5C H9   H N N 27  
A1A5C H10  H N N 28  
A1A5C H5   H N N 29  
A1A5C H6   H N N 30  
A1A5C H4   H N N 31  
A1A5C H7   H N N 32  
A1A5C H12  H N N 33  
ALA   N    N N N 34  
ALA   CA   C N S 35  
ALA   C    C N N 36  
ALA   O    O N N 37  
ALA   CB   C N N 38  
ALA   OXT  O N N 39  
ALA   H    H N N 40  
ALA   H2   H N N 41  
ALA   HA   H N N 42  
ALA   HB1  H N N 43  
ALA   HB2  H N N 44  
ALA   HB3  H N N 45  
ALA   HXT  H N N 46  
ARG   N    N N N 47  
ARG   CA   C N S 48  
ARG   C    C N N 49  
ARG   O    O N N 50  
ARG   CB   C N N 51  
ARG   CG   C N N 52  
ARG   CD   C N N 53  
ARG   NE   N N N 54  
ARG   CZ   C N N 55  
ARG   NH1  N N N 56  
ARG   NH2  N N N 57  
ARG   OXT  O N N 58  
ARG   H    H N N 59  
ARG   H2   H N N 60  
ARG   HA   H N N 61  
ARG   HB2  H N N 62  
ARG   HB3  H N N 63  
ARG   HG2  H N N 64  
ARG   HG3  H N N 65  
ARG   HD2  H N N 66  
ARG   HD3  H N N 67  
ARG   HE   H N N 68  
ARG   HH11 H N N 69  
ARG   HH12 H N N 70  
ARG   HH21 H N N 71  
ARG   HH22 H N N 72  
ARG   HXT  H N N 73  
ASN   N    N N N 74  
ASN   CA   C N S 75  
ASN   C    C N N 76  
ASN   O    O N N 77  
ASN   CB   C N N 78  
ASN   CG   C N N 79  
ASN   OD1  O N N 80  
ASN   ND2  N N N 81  
ASN   OXT  O N N 82  
ASN   H    H N N 83  
ASN   H2   H N N 84  
ASN   HA   H N N 85  
ASN   HB2  H N N 86  
ASN   HB3  H N N 87  
ASN   HD21 H N N 88  
ASN   HD22 H N N 89  
ASN   HXT  H N N 90  
ASP   N    N N N 91  
ASP   CA   C N S 92  
ASP   C    C N N 93  
ASP   O    O N N 94  
ASP   CB   C N N 95  
ASP   CG   C N N 96  
ASP   OD1  O N N 97  
ASP   OD2  O N N 98  
ASP   OXT  O N N 99  
ASP   H    H N N 100 
ASP   H2   H N N 101 
ASP   HA   H N N 102 
ASP   HB2  H N N 103 
ASP   HB3  H N N 104 
ASP   HD2  H N N 105 
ASP   HXT  H N N 106 
CYS   N    N N N 107 
CYS   CA   C N R 108 
CYS   C    C N N 109 
CYS   O    O N N 110 
CYS   CB   C N N 111 
CYS   SG   S N N 112 
CYS   OXT  O N N 113 
CYS   H    H N N 114 
CYS   H2   H N N 115 
CYS   HA   H N N 116 
CYS   HB2  H N N 117 
CYS   HB3  H N N 118 
CYS   HG   H N N 119 
CYS   HXT  H N N 120 
GLN   N    N N N 121 
GLN   CA   C N S 122 
GLN   C    C N N 123 
GLN   O    O N N 124 
GLN   CB   C N N 125 
GLN   CG   C N N 126 
GLN   CD   C N N 127 
GLN   OE1  O N N 128 
GLN   NE2  N N N 129 
GLN   OXT  O N N 130 
GLN   H    H N N 131 
GLN   H2   H N N 132 
GLN   HA   H N N 133 
GLN   HB2  H N N 134 
GLN   HB3  H N N 135 
GLN   HG2  H N N 136 
GLN   HG3  H N N 137 
GLN   HE21 H N N 138 
GLN   HE22 H N N 139 
GLN   HXT  H N N 140 
GLU   N    N N N 141 
GLU   CA   C N S 142 
GLU   C    C N N 143 
GLU   O    O N N 144 
GLU   CB   C N N 145 
GLU   CG   C N N 146 
GLU   CD   C N N 147 
GLU   OE1  O N N 148 
GLU   OE2  O N N 149 
GLU   OXT  O N N 150 
GLU   H    H N N 151 
GLU   H2   H N N 152 
GLU   HA   H N N 153 
GLU   HB2  H N N 154 
GLU   HB3  H N N 155 
GLU   HG2  H N N 156 
GLU   HG3  H N N 157 
GLU   HE2  H N N 158 
GLU   HXT  H N N 159 
GLY   N    N N N 160 
GLY   CA   C N N 161 
GLY   C    C N N 162 
GLY   O    O N N 163 
GLY   OXT  O N N 164 
GLY   H    H N N 165 
GLY   H2   H N N 166 
GLY   HA2  H N N 167 
GLY   HA3  H N N 168 
GLY   HXT  H N N 169 
HIS   N    N N N 170 
HIS   CA   C N S 171 
HIS   C    C N N 172 
HIS   O    O N N 173 
HIS   CB   C N N 174 
HIS   CG   C Y N 175 
HIS   ND1  N Y N 176 
HIS   CD2  C Y N 177 
HIS   CE1  C Y N 178 
HIS   NE2  N Y N 179 
HIS   OXT  O N N 180 
HIS   H    H N N 181 
HIS   H2   H N N 182 
HIS   HA   H N N 183 
HIS   HB2  H N N 184 
HIS   HB3  H N N 185 
HIS   HD1  H N N 186 
HIS   HD2  H N N 187 
HIS   HE1  H N N 188 
HIS   HE2  H N N 189 
HIS   HXT  H N N 190 
HOH   O    O N N 191 
HOH   H1   H N N 192 
HOH   H2   H N N 193 
ILE   N    N N N 194 
ILE   CA   C N S 195 
ILE   C    C N N 196 
ILE   O    O N N 197 
ILE   CB   C N S 198 
ILE   CG1  C N N 199 
ILE   CG2  C N N 200 
ILE   CD1  C N N 201 
ILE   OXT  O N N 202 
ILE   H    H N N 203 
ILE   H2   H N N 204 
ILE   HA   H N N 205 
ILE   HB   H N N 206 
ILE   HG12 H N N 207 
ILE   HG13 H N N 208 
ILE   HG21 H N N 209 
ILE   HG22 H N N 210 
ILE   HG23 H N N 211 
ILE   HD11 H N N 212 
ILE   HD12 H N N 213 
ILE   HD13 H N N 214 
ILE   HXT  H N N 215 
LEU   N    N N N 216 
LEU   CA   C N S 217 
LEU   C    C N N 218 
LEU   O    O N N 219 
LEU   CB   C N N 220 
LEU   CG   C N N 221 
LEU   CD1  C N N 222 
LEU   CD2  C N N 223 
LEU   OXT  O N N 224 
LEU   H    H N N 225 
LEU   H2   H N N 226 
LEU   HA   H N N 227 
LEU   HB2  H N N 228 
LEU   HB3  H N N 229 
LEU   HG   H N N 230 
LEU   HD11 H N N 231 
LEU   HD12 H N N 232 
LEU   HD13 H N N 233 
LEU   HD21 H N N 234 
LEU   HD22 H N N 235 
LEU   HD23 H N N 236 
LEU   HXT  H N N 237 
LYS   N    N N N 238 
LYS   CA   C N S 239 
LYS   C    C N N 240 
LYS   O    O N N 241 
LYS   CB   C N N 242 
LYS   CG   C N N 243 
LYS   CD   C N N 244 
LYS   CE   C N N 245 
LYS   NZ   N N N 246 
LYS   OXT  O N N 247 
LYS   H    H N N 248 
LYS   H2   H N N 249 
LYS   HA   H N N 250 
LYS   HB2  H N N 251 
LYS   HB3  H N N 252 
LYS   HG2  H N N 253 
LYS   HG3  H N N 254 
LYS   HD2  H N N 255 
LYS   HD3  H N N 256 
LYS   HE2  H N N 257 
LYS   HE3  H N N 258 
LYS   HZ1  H N N 259 
LYS   HZ2  H N N 260 
LYS   HZ3  H N N 261 
LYS   HXT  H N N 262 
MET   N    N N N 263 
MET   CA   C N S 264 
MET   C    C N N 265 
MET   O    O N N 266 
MET   CB   C N N 267 
MET   CG   C N N 268 
MET   SD   S N N 269 
MET   CE   C N N 270 
MET   OXT  O N N 271 
MET   H    H N N 272 
MET   H2   H N N 273 
MET   HA   H N N 274 
MET   HB2  H N N 275 
MET   HB3  H N N 276 
MET   HG2  H N N 277 
MET   HG3  H N N 278 
MET   HE1  H N N 279 
MET   HE2  H N N 280 
MET   HE3  H N N 281 
MET   HXT  H N N 282 
PHE   N    N N N 283 
PHE   CA   C N S 284 
PHE   C    C N N 285 
PHE   O    O N N 286 
PHE   CB   C N N 287 
PHE   CG   C Y N 288 
PHE   CD1  C Y N 289 
PHE   CD2  C Y N 290 
PHE   CE1  C Y N 291 
PHE   CE2  C Y N 292 
PHE   CZ   C Y N 293 
PHE   OXT  O N N 294 
PHE   H    H N N 295 
PHE   H2   H N N 296 
PHE   HA   H N N 297 
PHE   HB2  H N N 298 
PHE   HB3  H N N 299 
PHE   HD1  H N N 300 
PHE   HD2  H N N 301 
PHE   HE1  H N N 302 
PHE   HE2  H N N 303 
PHE   HZ   H N N 304 
PHE   HXT  H N N 305 
PRO   N    N N N 306 
PRO   CA   C N S 307 
PRO   C    C N N 308 
PRO   O    O N N 309 
PRO   CB   C N N 310 
PRO   CG   C N N 311 
PRO   CD   C N N 312 
PRO   OXT  O N N 313 
PRO   H    H N N 314 
PRO   HA   H N N 315 
PRO   HB2  H N N 316 
PRO   HB3  H N N 317 
PRO   HG2  H N N 318 
PRO   HG3  H N N 319 
PRO   HD2  H N N 320 
PRO   HD3  H N N 321 
PRO   HXT  H N N 322 
SER   N    N N N 323 
SER   CA   C N S 324 
SER   C    C N N 325 
SER   O    O N N 326 
SER   CB   C N N 327 
SER   OG   O N N 328 
SER   OXT  O N N 329 
SER   H    H N N 330 
SER   H2   H N N 331 
SER   HA   H N N 332 
SER   HB2  H N N 333 
SER   HB3  H N N 334 
SER   HG   H N N 335 
SER   HXT  H N N 336 
THR   N    N N N 337 
THR   CA   C N S 338 
THR   C    C N N 339 
THR   O    O N N 340 
THR   CB   C N R 341 
THR   OG1  O N N 342 
THR   CG2  C N N 343 
THR   OXT  O N N 344 
THR   H    H N N 345 
THR   H2   H N N 346 
THR   HA   H N N 347 
THR   HB   H N N 348 
THR   HG1  H N N 349 
THR   HG21 H N N 350 
THR   HG22 H N N 351 
THR   HG23 H N N 352 
THR   HXT  H N N 353 
TYR   N    N N N 354 
TYR   CA   C N S 355 
TYR   C    C N N 356 
TYR   O    O N N 357 
TYR   CB   C N N 358 
TYR   CG   C Y N 359 
TYR   CD1  C Y N 360 
TYR   CD2  C Y N 361 
TYR   CE1  C Y N 362 
TYR   CE2  C Y N 363 
TYR   CZ   C Y N 364 
TYR   OH   O N N 365 
TYR   OXT  O N N 366 
TYR   H    H N N 367 
TYR   H2   H N N 368 
TYR   HA   H N N 369 
TYR   HB2  H N N 370 
TYR   HB3  H N N 371 
TYR   HD1  H N N 372 
TYR   HD2  H N N 373 
TYR   HE1  H N N 374 
TYR   HE2  H N N 375 
TYR   HH   H N N 376 
TYR   HXT  H N N 377 
VAL   N    N N N 378 
VAL   CA   C N S 379 
VAL   C    C N N 380 
VAL   O    O N N 381 
VAL   CB   C N N 382 
VAL   CG1  C N N 383 
VAL   CG2  C N N 384 
VAL   OXT  O N N 385 
VAL   H    H N N 386 
VAL   H2   H N N 387 
VAL   HA   H N N 388 
VAL   HB   H N N 389 
VAL   HG11 H N N 390 
VAL   HG12 H N N 391 
VAL   HG13 H N N 392 
VAL   HG21 H N N 393 
VAL   HG22 H N N 394 
VAL   HG23 H N N 395 
VAL   HXT  H N N 396 
# 
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 
A1A5C O1  C13  doub N N 1   
A1A5C C13 O2   sing N N 2   
A1A5C C13 C12  sing N N 3   
A1A5C C11 C12  doub Y N 4   
A1A5C C11 C10  sing Y N 5   
A1A5C C12 C7   sing Y N 6   
A1A5C C10 C9   doub Y N 7   
A1A5C C7  S1   sing N N 8   
A1A5C C7  C8   doub Y N 9   
A1A5C N1  C14  doub Y N 10  
A1A5C N1  C6   sing Y N 11  
A1A5C C9  C8   sing Y N 12  
A1A5C C14 N2   sing Y N 13  
A1A5C S1  C6   sing N N 14  
A1A5C C6  C5   doub Y N 15  
A1A5C N2  C15  doub Y N 16  
A1A5C C5  C15  sing Y N 17  
A1A5C C5  C3   sing Y N 18  
A1A5C C15 S2   sing Y N 19  
A1A5C C3  C4   sing N N 20  
A1A5C C3  C2   doub Y N 21  
A1A5C S2  C2   sing Y N 22  
A1A5C C2  C1   sing N N 23  
A1A5C C9  H8   sing N N 24  
A1A5C C14 H11  sing N N 25  
A1A5C C1  H2   sing N N 26  
A1A5C C1  H3   sing N N 27  
A1A5C C1  H1   sing N N 28  
A1A5C C10 H9   sing N N 29  
A1A5C C11 H10  sing N N 30  
A1A5C C4  H5   sing N N 31  
A1A5C C4  H6   sing N N 32  
A1A5C C4  H4   sing N N 33  
A1A5C C8  H7   sing N N 34  
A1A5C O2  H12  sing N N 35  
ALA   N   CA   sing N N 36  
ALA   N   H    sing N N 37  
ALA   N   H2   sing N N 38  
ALA   CA  C    sing N N 39  
ALA   CA  CB   sing N N 40  
ALA   CA  HA   sing N N 41  
ALA   C   O    doub N N 42  
ALA   C   OXT  sing N N 43  
ALA   CB  HB1  sing N N 44  
ALA   CB  HB2  sing N N 45  
ALA   CB  HB3  sing N N 46  
ALA   OXT HXT  sing N N 47  
ARG   N   CA   sing N N 48  
ARG   N   H    sing N N 49  
ARG   N   H2   sing N N 50  
ARG   CA  C    sing N N 51  
ARG   CA  CB   sing N N 52  
ARG   CA  HA   sing N N 53  
ARG   C   O    doub N N 54  
ARG   C   OXT  sing N N 55  
ARG   CB  CG   sing N N 56  
ARG   CB  HB2  sing N N 57  
ARG   CB  HB3  sing N N 58  
ARG   CG  CD   sing N N 59  
ARG   CG  HG2  sing N N 60  
ARG   CG  HG3  sing N N 61  
ARG   CD  NE   sing N N 62  
ARG   CD  HD2  sing N N 63  
ARG   CD  HD3  sing N N 64  
ARG   NE  CZ   sing N N 65  
ARG   NE  HE   sing N N 66  
ARG   CZ  NH1  sing N N 67  
ARG   CZ  NH2  doub N N 68  
ARG   NH1 HH11 sing N N 69  
ARG   NH1 HH12 sing N N 70  
ARG   NH2 HH21 sing N N 71  
ARG   NH2 HH22 sing N N 72  
ARG   OXT HXT  sing N N 73  
ASN   N   CA   sing N N 74  
ASN   N   H    sing N N 75  
ASN   N   H2   sing N N 76  
ASN   CA  C    sing N N 77  
ASN   CA  CB   sing N N 78  
ASN   CA  HA   sing N N 79  
ASN   C   O    doub N N 80  
ASN   C   OXT  sing N N 81  
ASN   CB  CG   sing N N 82  
ASN   CB  HB2  sing N N 83  
ASN   CB  HB3  sing N N 84  
ASN   CG  OD1  doub N N 85  
ASN   CG  ND2  sing N N 86  
ASN   ND2 HD21 sing N N 87  
ASN   ND2 HD22 sing N N 88  
ASN   OXT HXT  sing N N 89  
ASP   N   CA   sing N N 90  
ASP   N   H    sing N N 91  
ASP   N   H2   sing N N 92  
ASP   CA  C    sing N N 93  
ASP   CA  CB   sing N N 94  
ASP   CA  HA   sing N N 95  
ASP   C   O    doub N N 96  
ASP   C   OXT  sing N N 97  
ASP   CB  CG   sing N N 98  
ASP   CB  HB2  sing N N 99  
ASP   CB  HB3  sing N N 100 
ASP   CG  OD1  doub N N 101 
ASP   CG  OD2  sing N N 102 
ASP   OD2 HD2  sing N N 103 
ASP   OXT HXT  sing N N 104 
CYS   N   CA   sing N N 105 
CYS   N   H    sing N N 106 
CYS   N   H2   sing N N 107 
CYS   CA  C    sing N N 108 
CYS   CA  CB   sing N N 109 
CYS   CA  HA   sing N N 110 
CYS   C   O    doub N N 111 
CYS   C   OXT  sing N N 112 
CYS   CB  SG   sing N N 113 
CYS   CB  HB2  sing N N 114 
CYS   CB  HB3  sing N N 115 
CYS   SG  HG   sing N N 116 
CYS   OXT HXT  sing N N 117 
GLN   N   CA   sing N N 118 
GLN   N   H    sing N N 119 
GLN   N   H2   sing N N 120 
GLN   CA  C    sing N N 121 
GLN   CA  CB   sing N N 122 
GLN   CA  HA   sing N N 123 
GLN   C   O    doub N N 124 
GLN   C   OXT  sing N N 125 
GLN   CB  CG   sing N N 126 
GLN   CB  HB2  sing N N 127 
GLN   CB  HB3  sing N N 128 
GLN   CG  CD   sing N N 129 
GLN   CG  HG2  sing N N 130 
GLN   CG  HG3  sing N N 131 
GLN   CD  OE1  doub N N 132 
GLN   CD  NE2  sing N N 133 
GLN   NE2 HE21 sing N N 134 
GLN   NE2 HE22 sing N N 135 
GLN   OXT HXT  sing N N 136 
GLU   N   CA   sing N N 137 
GLU   N   H    sing N N 138 
GLU   N   H2   sing N N 139 
GLU   CA  C    sing N N 140 
GLU   CA  CB   sing N N 141 
GLU   CA  HA   sing N N 142 
GLU   C   O    doub N N 143 
GLU   C   OXT  sing N N 144 
GLU   CB  CG   sing N N 145 
GLU   CB  HB2  sing N N 146 
GLU   CB  HB3  sing N N 147 
GLU   CG  CD   sing N N 148 
GLU   CG  HG2  sing N N 149 
GLU   CG  HG3  sing N N 150 
GLU   CD  OE1  doub N N 151 
GLU   CD  OE2  sing N N 152 
GLU   OE2 HE2  sing N N 153 
GLU   OXT HXT  sing N N 154 
GLY   N   CA   sing N N 155 
GLY   N   H    sing N N 156 
GLY   N   H2   sing N N 157 
GLY   CA  C    sing N N 158 
GLY   CA  HA2  sing N N 159 
GLY   CA  HA3  sing N N 160 
GLY   C   O    doub N N 161 
GLY   C   OXT  sing N N 162 
GLY   OXT HXT  sing N N 163 
HIS   N   CA   sing N N 164 
HIS   N   H    sing N N 165 
HIS   N   H2   sing N N 166 
HIS   CA  C    sing N N 167 
HIS   CA  CB   sing N N 168 
HIS   CA  HA   sing N N 169 
HIS   C   O    doub N N 170 
HIS   C   OXT  sing N N 171 
HIS   CB  CG   sing N N 172 
HIS   CB  HB2  sing N N 173 
HIS   CB  HB3  sing N N 174 
HIS   CG  ND1  sing Y N 175 
HIS   CG  CD2  doub Y N 176 
HIS   ND1 CE1  doub Y N 177 
HIS   ND1 HD1  sing N N 178 
HIS   CD2 NE2  sing Y N 179 
HIS   CD2 HD2  sing N N 180 
HIS   CE1 NE2  sing Y N 181 
HIS   CE1 HE1  sing N N 182 
HIS   NE2 HE2  sing N N 183 
HIS   OXT HXT  sing N N 184 
HOH   O   H1   sing N N 185 
HOH   O   H2   sing N N 186 
ILE   N   CA   sing N N 187 
ILE   N   H    sing N N 188 
ILE   N   H2   sing N N 189 
ILE   CA  C    sing N N 190 
ILE   CA  CB   sing N N 191 
ILE   CA  HA   sing N N 192 
ILE   C   O    doub N N 193 
ILE   C   OXT  sing N N 194 
ILE   CB  CG1  sing N N 195 
ILE   CB  CG2  sing N N 196 
ILE   CB  HB   sing N N 197 
ILE   CG1 CD1  sing N N 198 
ILE   CG1 HG12 sing N N 199 
ILE   CG1 HG13 sing N N 200 
ILE   CG2 HG21 sing N N 201 
ILE   CG2 HG22 sing N N 202 
ILE   CG2 HG23 sing N N 203 
ILE   CD1 HD11 sing N N 204 
ILE   CD1 HD12 sing N N 205 
ILE   CD1 HD13 sing N N 206 
ILE   OXT HXT  sing N N 207 
LEU   N   CA   sing N N 208 
LEU   N   H    sing N N 209 
LEU   N   H2   sing N N 210 
LEU   CA  C    sing N N 211 
LEU   CA  CB   sing N N 212 
LEU   CA  HA   sing N N 213 
LEU   C   O    doub N N 214 
LEU   C   OXT  sing N N 215 
LEU   CB  CG   sing N N 216 
LEU   CB  HB2  sing N N 217 
LEU   CB  HB3  sing N N 218 
LEU   CG  CD1  sing N N 219 
LEU   CG  CD2  sing N N 220 
LEU   CG  HG   sing N N 221 
LEU   CD1 HD11 sing N N 222 
LEU   CD1 HD12 sing N N 223 
LEU   CD1 HD13 sing N N 224 
LEU   CD2 HD21 sing N N 225 
LEU   CD2 HD22 sing N N 226 
LEU   CD2 HD23 sing N N 227 
LEU   OXT HXT  sing N N 228 
LYS   N   CA   sing N N 229 
LYS   N   H    sing N N 230 
LYS   N   H2   sing N N 231 
LYS   CA  C    sing N N 232 
LYS   CA  CB   sing N N 233 
LYS   CA  HA   sing N N 234 
LYS   C   O    doub N N 235 
LYS   C   OXT  sing N N 236 
LYS   CB  CG   sing N N 237 
LYS   CB  HB2  sing N N 238 
LYS   CB  HB3  sing N N 239 
LYS   CG  CD   sing N N 240 
LYS   CG  HG2  sing N N 241 
LYS   CG  HG3  sing N N 242 
LYS   CD  CE   sing N N 243 
LYS   CD  HD2  sing N N 244 
LYS   CD  HD3  sing N N 245 
LYS   CE  NZ   sing N N 246 
LYS   CE  HE2  sing N N 247 
LYS   CE  HE3  sing N N 248 
LYS   NZ  HZ1  sing N N 249 
LYS   NZ  HZ2  sing N N 250 
LYS   NZ  HZ3  sing N N 251 
LYS   OXT HXT  sing N N 252 
MET   N   CA   sing N N 253 
MET   N   H    sing N N 254 
MET   N   H2   sing N N 255 
MET   CA  C    sing N N 256 
MET   CA  CB   sing N N 257 
MET   CA  HA   sing N N 258 
MET   C   O    doub N N 259 
MET   C   OXT  sing N N 260 
MET   CB  CG   sing N N 261 
MET   CB  HB2  sing N N 262 
MET   CB  HB3  sing N N 263 
MET   CG  SD   sing N N 264 
MET   CG  HG2  sing N N 265 
MET   CG  HG3  sing N N 266 
MET   SD  CE   sing N N 267 
MET   CE  HE1  sing N N 268 
MET   CE  HE2  sing N N 269 
MET   CE  HE3  sing N N 270 
MET   OXT HXT  sing N N 271 
PHE   N   CA   sing N N 272 
PHE   N   H    sing N N 273 
PHE   N   H2   sing N N 274 
PHE   CA  C    sing N N 275 
PHE   CA  CB   sing N N 276 
PHE   CA  HA   sing N N 277 
PHE   C   O    doub N N 278 
PHE   C   OXT  sing N N 279 
PHE   CB  CG   sing N N 280 
PHE   CB  HB2  sing N N 281 
PHE   CB  HB3  sing N N 282 
PHE   CG  CD1  doub Y N 283 
PHE   CG  CD2  sing Y N 284 
PHE   CD1 CE1  sing Y N 285 
PHE   CD1 HD1  sing N N 286 
PHE   CD2 CE2  doub Y N 287 
PHE   CD2 HD2  sing N N 288 
PHE   CE1 CZ   doub Y N 289 
PHE   CE1 HE1  sing N N 290 
PHE   CE2 CZ   sing Y N 291 
PHE   CE2 HE2  sing N N 292 
PHE   CZ  HZ   sing N N 293 
PHE   OXT HXT  sing N N 294 
PRO   N   CA   sing N N 295 
PRO   N   CD   sing N N 296 
PRO   N   H    sing N N 297 
PRO   CA  C    sing N N 298 
PRO   CA  CB   sing N N 299 
PRO   CA  HA   sing N N 300 
PRO   C   O    doub N N 301 
PRO   C   OXT  sing N N 302 
PRO   CB  CG   sing N N 303 
PRO   CB  HB2  sing N N 304 
PRO   CB  HB3  sing N N 305 
PRO   CG  CD   sing N N 306 
PRO   CG  HG2  sing N N 307 
PRO   CG  HG3  sing N N 308 
PRO   CD  HD2  sing N N 309 
PRO   CD  HD3  sing N N 310 
PRO   OXT HXT  sing N N 311 
SER   N   CA   sing N N 312 
SER   N   H    sing N N 313 
SER   N   H2   sing N N 314 
SER   CA  C    sing N N 315 
SER   CA  CB   sing N N 316 
SER   CA  HA   sing N N 317 
SER   C   O    doub N N 318 
SER   C   OXT  sing N N 319 
SER   CB  OG   sing N N 320 
SER   CB  HB2  sing N N 321 
SER   CB  HB3  sing N N 322 
SER   OG  HG   sing N N 323 
SER   OXT HXT  sing N N 324 
THR   N   CA   sing N N 325 
THR   N   H    sing N N 326 
THR   N   H2   sing N N 327 
THR   CA  C    sing N N 328 
THR   CA  CB   sing N N 329 
THR   CA  HA   sing N N 330 
THR   C   O    doub N N 331 
THR   C   OXT  sing N N 332 
THR   CB  OG1  sing N N 333 
THR   CB  CG2  sing N N 334 
THR   CB  HB   sing N N 335 
THR   OG1 HG1  sing N N 336 
THR   CG2 HG21 sing N N 337 
THR   CG2 HG22 sing N N 338 
THR   CG2 HG23 sing N N 339 
THR   OXT HXT  sing N N 340 
TYR   N   CA   sing N N 341 
TYR   N   H    sing N N 342 
TYR   N   H2   sing N N 343 
TYR   CA  C    sing N N 344 
TYR   CA  CB   sing N N 345 
TYR   CA  HA   sing N N 346 
TYR   C   O    doub N N 347 
TYR   C   OXT  sing N N 348 
TYR   CB  CG   sing N N 349 
TYR   CB  HB2  sing N N 350 
TYR   CB  HB3  sing N N 351 
TYR   CG  CD1  doub Y N 352 
TYR   CG  CD2  sing Y N 353 
TYR   CD1 CE1  sing Y N 354 
TYR   CD1 HD1  sing N N 355 
TYR   CD2 CE2  doub Y N 356 
TYR   CD2 HD2  sing N N 357 
TYR   CE1 CZ   doub Y N 358 
TYR   CE1 HE1  sing N N 359 
TYR   CE2 CZ   sing Y N 360 
TYR   CE2 HE2  sing N N 361 
TYR   CZ  OH   sing N N 362 
TYR   OH  HH   sing N N 363 
TYR   OXT HXT  sing N N 364 
VAL   N   CA   sing N N 365 
VAL   N   H    sing N N 366 
VAL   N   H2   sing N N 367 
VAL   CA  C    sing N N 368 
VAL   CA  CB   sing N N 369 
VAL   CA  HA   sing N N 370 
VAL   C   O    doub N N 371 
VAL   C   OXT  sing N N 372 
VAL   CB  CG1  sing N N 373 
VAL   CB  CG2  sing N N 374 
VAL   CB  HB   sing N N 375 
VAL   CG1 HG11 sing N N 376 
VAL   CG1 HG12 sing N N 377 
VAL   CG1 HG13 sing N N 378 
VAL   CG2 HG21 sing N N 379 
VAL   CG2 HG22 sing N N 380 
VAL   CG2 HG23 sing N N 381 
VAL   OXT HXT  sing N N 382 
# 
_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                    7HCH 
_atom_sites.fract_transf_matrix[1][1]   0.011258 
_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]   0.011258 
_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]   0.025179 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.795 -16.398 22.290  0.40 39.54 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.791 -16.522 22.440  0.60 40.28 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.823 -15.323 22.453  0.40 39.14 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.877 -15.403 22.634  0.60 39.78 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.474 -13.974 22.167  0.40 37.26 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.559 -14.088 22.273  0.60 37.72 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.589 -13.707 22.614  0.40 37.50 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.691 -13.833 22.686  0.60 38.07 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.186 -15.354 23.858  0.40 40.27 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.323 -15.374 24.075  0.60 40.93 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.158 -14.240 24.004  0.40 40.66 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.372 -14.197 24.261  0.60 41.31 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.546 -16.709 24.123  0.40 40.63 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.622 -16.685 24.399  0.60 41.28 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.112 -15.443 21.809  0.40 46.95 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 18.122 -15.507 22.040  0.60 47.71 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.876 -15.213 24.525  0.40 48.30 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 19.057 -15.265 24.699  0.60 49.09 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.650 -14.385 24.818  0.40 48.77 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.886 -14.313 25.094  0.60 49.54 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.618 -13.387 24.050  0.40 48.77 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.884 -13.374 24.292  0.60 49.54 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.564 -14.257 23.237  0.40 48.77 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.749 -14.174 23.518  0.60 49.54 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 17.092 -16.682 24.980  0.40 48.73 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.237 -16.628 25.287  0.60 49.51 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.909 -16.900 23.417  0.40 48.73 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.923 -16.838 23.744  0.60 49.51 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.238 -17.388 24.137  0.40 48.73 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.270 -17.406 24.364  0.60 49.51 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.773 -13.130 21.412  0.40 34.83 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.870 -13.262 21.489  0.60 34.86 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.216 -11.771 21.126  0.40 32.22 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 19.332 -11.920 21.169  0.60 31.77 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 18.059 -10.809 21.378  0.40 30.19 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 18.195 -10.933 21.394  0.60 29.70 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.954 -11.216 21.753  0.40 30.07 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 17.051 -11.315 21.656  0.60 29.37 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.781 -11.646 19.704  0.40 31.53 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.885 -11.819 19.737  0.60 30.57 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.777 -12.026 18.636  0.40 30.80 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.849 -12.141 18.680  0.60 29.24 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.653 -11.526 18.618  0.40 30.45 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.785 -11.526 18.630  0.60 28.53 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.180 -12.917 17.737  0.40 30.60 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 19.170 -13.092 17.807  0.60 28.89 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 18.018 -13.328 21.048  0.40 41.77 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 18.114 -13.461 21.128  0.60 41.81 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.929 -11.545 21.740  0.40 38.64 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 20.049 -11.685 21.774  0.60 38.10 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 20.049 -10.725 19.551  0.40 37.82 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 20.199 -10.915 19.584  0.60 36.66 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.548 -12.232 19.618  0.40 37.82 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.616 -12.447 19.642  0.60 36.66 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.649 -13.166 17.108  0.40 36.69 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.619 -13.312 17.183  0.60 34.64 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.975 -13.245 17.782  0.40 36.69 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.930 -13.492 17.867  0.60 34.64 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.316 -9.518  21.163  0.40 28.17 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.523 -9.646  21.288  0.60 27.87 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.393 -8.460  21.555  0.40 26.20 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.597 -8.580  21.646  0.60 26.24 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.522 -7.954  20.408  0.40 23.62 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.669 -8.171  20.509  0.60 23.95 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.827 -6.947  20.576  0.40 24.16 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.816 -7.301  20.713  0.60 24.06 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 18.156 -7.295  22.194  0.40 26.74 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 18.366 -7.364  22.177  0.60 26.93 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 19.115 -6.758  21.301  0.40 27.08 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 19.274 -6.887  21.202  0.60 27.31 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 19.030 -9.229  20.780  0.40 33.78 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 19.287 -9.362  21.002  0.60 33.42 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.800 -8.811  22.233  0.40 31.41 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 17.032 -8.886  22.360  0.60 31.46 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.525 -6.597  22.437  0.40 32.07 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.740 -6.653  22.397  0.60 32.29 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.613 -7.613  22.989  0.40 32.07 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.858 -7.621  22.980  0.60 32.29 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.523 -6.117  21.667  0.40 32.46 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.859 -7.467  21.042  0.60 32.75 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.533 -8.618  19.255  0.40 20.37 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.790 -8.778  19.330  0.60 21.61 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.635 -8.227  18.176  0.40 17.57 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.870 -8.462  18.244  0.60 20.23 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 14.201 -8.583  18.550  0.40 16.90 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 14.468 -8.907  18.636  0.60 21.02 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.926 -9.678  19.048  0.40 17.46 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 14.235 -10.090 18.907  0.60 21.78 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 16.025 -8.923  16.872  0.40 16.04 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 16.302 -9.150  16.954  0.60 18.68 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.325 -8.434  16.282  0.40 15.39 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 17.500 -8.520  16.298  0.60 17.83 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.394 -7.210  15.633  0.40 15.30 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.384 -7.328  15.601  0.60 17.86 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.471 -9.206  16.364  0.40 15.60 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.737 -9.132  16.366  0.60 17.76 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.589 -6.765  15.087  0.40 15.26 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.490 -6.757  14.994  0.60 18.04 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.664 -8.768  15.818  0.40 15.60 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.840 -8.569  15.759  0.60 17.90 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.724 -7.546  15.180  0.40 15.38 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.718 -7.381  15.073  0.60 18.04 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 17.037 -9.288  19.078  0.40 24.42 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 17.382 -9.374  19.141  0.60 25.91 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.687 -7.270  18.041  0.40 21.05 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.860 -7.506  18.093  0.60 24.25 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 16.111 -9.876  17.042  0.40 19.22 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 16.523 -10.075 17.149  0.60 22.39 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.320 -8.774  16.218  0.40 19.22 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 15.566 -9.117  16.324  0.60 22.39 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.630 -6.680  15.567  0.40 18.34 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.556 -6.905  15.544  0.60 21.40 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.435 -10.030 16.793  0.40 18.70 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.820 -9.936  16.827  0.60 21.28 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.626 -5.941  14.654  0.40 18.29 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.405 -5.953  14.529  0.60 21.62 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.428 -9.294  15.883  0.40 18.69 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.664 -8.991  15.816  0.60 21.45 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.527 -7.249  14.813  0.40 18.43 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.461 -6.999  14.666  0.60 21.62 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.281 -7.646  18.315  0.40 16.39 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 13.537 -7.961  18.665  0.60 21.51 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.920 -7.754  18.823  0.40 16.89 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 12.192 -8.193  19.167  0.60 22.40 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.915 -7.509  17.707  0.40 15.56 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 11.174 -7.967  18.061  0.60 21.74 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 11.144 -6.675  16.826  0.40 15.43 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 11.293 -7.020  17.276  0.60 21.70 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.696 -6.743  19.963  0.40 18.68 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.886 -7.244  20.331  0.60 24.09 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.363 -6.796  20.440  0.40 20.38 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 10.490 -7.103  20.519  0.60 25.64 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.420 -6.925  17.858  0.40 19.64 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 13.670 -7.158  18.392  0.60 25.79 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.768 -8.639  19.174  0.40 20.24 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 12.115 -9.107  19.484  0.60 26.85 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 12.311 -6.949  20.692  0.40 22.40 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 12.259 -7.610  21.147  0.60 28.88 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.865 -5.847  19.638  0.40 22.40 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 12.288 -6.377  20.146  0.60 28.88 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 10.264 -6.260  21.080  0.40 24.43 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 10.336 -6.550  21.136  0.60 30.74 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.802  -8.243  17.750  0.40 14.46 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 10.176 -8.848  18.005  0.60 21.25 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.706  -7.998  16.836  0.40 13.99 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 9.039  -8.637  17.134  0.60 20.78 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.900  -8.510  15.431  0.40 13.69 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 9.239  -8.988  15.678  0.60 19.32 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 8.149  -8.113  14.533  0.40 14.58 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 8.526  -8.450  14.825  0.60 19.86 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.666  -8.882  18.304  0.40 17.33 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 10.143 -9.575  18.470  0.60 25.48 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.906  -8.420  17.192  0.40 16.76 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 8.298  -9.168  17.465  0.60 24.91 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.540  -7.045  16.787  0.40 16.76 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.785  -7.706  17.181  0.60 24.91 ?  8   GLY   A HA3  1 
ATOM   157  N N    A TYR   A 1 9   ? 9.871  -9.387  15.202  0.40 12.78 ?  9   TYR   A N    1 
ATOM   158  N N    B TYR   A 1 9   ? 10.171 -9.882  15.361  0.60 17.48 ?  9   TYR   A N    1 
ATOM   159  C CA   A TYR   A 1 9   ? 10.105 -9.912  13.867  0.40 12.27 ?  9   TYR   A CA   1 
ATOM   160  C CA   B TYR   A 1 9   ? 10.402 -10.290 13.982  0.60 15.69 ?  9   TYR   A CA   1 
ATOM   161  C C    A TYR   A 1 9   ? 9.208  -11.109 13.591  0.40 11.81 ?  9   TYR   A C    1 
ATOM   162  C C    B TYR   A 1 9   ? 9.588  -11.529 13.633  0.60 15.05 ?  9   TYR   A C    1 
ATOM   163  O O    A TYR   A 1 9   ? 8.903  -11.905 14.489  0.40 11.94 ?  9   TYR   A O    1 
ATOM   164  O O    B TYR   A 1 9   ? 9.440  -12.440 14.451  0.60 16.03 ?  9   TYR   A O    1 
ATOM   165  C CB   A TYR   A 1 9   ? 11.569 -10.317 13.685  0.40 12.90 ?  9   TYR   A CB   1 
ATOM   166  C CB   B TYR   A 1 9   ? 11.882 -10.594 13.760  0.60 14.79 ?  9   TYR   A CB   1 
ATOM   167  C CG   A TYR   A 1 9   ? 12.487 -9.138  13.476  0.40 13.28 ?  9   TYR   A CG   1 
ATOM   168  C CG   B TYR   A 1 9   ? 12.747 -9.364  13.650  0.60 13.72 ?  9   TYR   A CG   1 
ATOM   169  C CD1  A TYR   A 1 9   ? 12.826 -8.307  14.532  0.40 13.61 ?  9   TYR   A CD1  1 
ATOM   170  C CD1  B TYR   A 1 9   ? 13.047 -8.597  14.768  0.60 13.67 ?  9   TYR   A CD1  1 
ATOM   171  C CD2  A TYR   A 1 9   ? 13.001 -8.846  12.220  0.40 13.05 ?  9   TYR   A CD2  1 
ATOM   172  C CD2  B TYR   A 1 9   ? 13.266 -8.967  12.425  0.60 13.41 ?  9   TYR   A CD2  1 
ATOM   173  C CE1  A TYR   A 1 9   ? 13.653 -7.218  14.347  0.40 13.61 ?  9   TYR   A CE1  1 
ATOM   174  C CE1  B TYR   A 1 9   ? 13.837 -7.465  14.669  0.60 14.02 ?  9   TYR   A CE1  1 
ATOM   175  C CE2  A TYR   A 1 9   ? 13.833 -7.761  12.024  0.40 12.99 ?  9   TYR   A CE2  1 
ATOM   176  C CE2  B TYR   A 1 9   ? 14.057 -7.840  12.316  0.60 13.36 ?  9   TYR   A CE2  1 
ATOM   177  C CZ   A TYR   A 1 9   ? 14.155 -6.950  13.090  0.40 13.25 ?  9   TYR   A CZ   1 
ATOM   178  C CZ   B TYR   A 1 9   ? 14.338 -7.095  13.440  0.60 14.07 ?  9   TYR   A CZ   1 
ATOM   179  O OH   A TYR   A 1 9   ? 14.975 -5.868  12.900  0.40 13.29 ?  9   TYR   A OH   1 
ATOM   180  O OH   B TYR   A 1 9   ? 15.121 -5.976  13.327  0.60 15.14 ?  9   TYR   A OH   1 
ATOM   181  H H    A TYR   A 1 9   ? 10.404 -9.699  15.803  0.40 15.31 ?  9   TYR   A H    1 
ATOM   182  H H    B TYR   A 1 9   ? 10.687 -10.271 15.934  0.60 20.95 ?  9   TYR   A H    1 
ATOM   183  H HA   A TYR   A 1 9   ? 9.901  -9.219  13.216  0.40 14.70 ?  9   TYR   A HA   1 
ATOM   184  H HA   B TYR   A 1 9   ? 10.145 -9.574  13.385  0.60 18.80 ?  9   TYR   A HA   1 
ATOM   185  H HB2  A TYR   A 1 9   ? 11.869 -10.802 14.467  0.40 15.45 ?  9   TYR   A HB2  1 
ATOM   186  H HB2  B TYR   A 1 9   ? 12.216 -11.122 14.500  0.60 17.73 ?  9   TYR   A HB2  1 
ATOM   187  H HB3  A TYR   A 1 9   ? 11.625 -10.879 12.897  0.40 15.45 ?  9   TYR   A HB3  1 
ATOM   188  H HB3  B TYR   A 1 9   ? 11.974 -11.088 12.931  0.60 17.73 ?  9   TYR   A HB3  1 
ATOM   189  H HD1  A TYR   A 1 9   ? 12.484 -8.486  15.381  0.40 16.31 ?  9   TYR   A HD1  1 
ATOM   190  H HD1  B TYR   A 1 9   ? 12.703 -8.844  15.597  0.60 16.38 ?  9   TYR   A HD1  1 
ATOM   191  H HD2  A TYR   A 1 9   ? 12.783 -9.389  11.497  0.40 15.63 ?  9   TYR   A HD2  1 
ATOM   192  H HD2  B TYR   A 1 9   ? 13.081 -9.470  11.665  0.60 16.07 ?  9   TYR   A HD2  1 
ATOM   193  H HE1  A TYR   A 1 9   ? 13.870 -6.674  15.069  0.40 16.31 ?  9   TYR   A HE1  1 
ATOM   194  H HE1  B TYR   A 1 9   ? 14.028 -6.956  15.425  0.60 16.80 ?  9   TYR   A HE1  1 
ATOM   195  H HE2  A TYR   A 1 9   ? 14.171 -7.577  11.179  0.40 15.56 ?  9   TYR   A HE2  1 
ATOM   196  H HE2  B TYR   A 1 9   ? 14.404 -7.587  11.489  0.60 16.01 ?  9   TYR   A HE2  1 
ATOM   197  H HH   A TYR   A 1 9   ? 15.084 -5.469  13.632  0.40 15.93 ?  9   TYR   A HH   1 
ATOM   198  H HH   B TYR   A 1 9   ? 15.223 -5.611  14.077  0.60 18.14 ?  9   TYR   A HH   1 
ATOM   199  N N    A LEU   A 1 10  ? 8.763  -11.207 12.344  0.40 12.03 ?  10  LEU   A N    1 
ATOM   200  N N    B LEU   A 1 10  ? 9.072  -11.555 12.402  0.60 13.72 ?  10  LEU   A N    1 
ATOM   201  C CA   A LEU   A 1 10  ? 8.165  -12.433 11.852  0.40 11.76 ?  10  LEU   A CA   1 
ATOM   202  C CA   B LEU   A 1 10  ? 8.496  -12.767 11.830  0.60 13.38 ?  10  LEU   A CA   1 
ATOM   203  C C    A LEU   A 1 10  ? 9.286  -13.369 11.420  0.40 11.12 ?  10  LEU   A C    1 
ATOM   204  C C    B LEU   A 1 10  ? 9.624  -13.685 11.375  0.60 12.56 ?  10  LEU   A C    1 
ATOM   205  O O    A LEU   A 1 10  ? 10.241 -12.956 10.756  0.40 11.45 ?  10  LEU   A O    1 
ATOM   206  O O    B LEU   A 1 10  ? 10.586 -13.234 10.747  0.60 12.87 ?  10  LEU   A O    1 
ATOM   207  C CB   A LEU   A 1 10  ? 7.256  -12.125 10.662  0.40 12.60 ?  10  LEU   A CB   1 
ATOM   208  C CB   B LEU   A 1 10  ? 7.614  -12.405 10.633  0.60 14.89 ?  10  LEU   A CB   1 
ATOM   209  C CG   A LEU   A 1 10  ? 6.629  -13.363 10.013  0.40 13.67 ?  10  LEU   A CG   1 
ATOM   210  C CG   B LEU   A 1 10  ? 7.151  -13.519 9.676   0.60 16.85 ?  10  LEU   A CG   1 
ATOM   211  C CD1  A LEU   A 1 10  ? 5.580  -13.983 10.919  0.40 14.31 ?  10  LEU   A CD1  1 
ATOM   212  C CD1  B LEU   A 1 10  ? 6.119  -14.432 10.319  0.60 17.38 ?  10  LEU   A CD1  1 
ATOM   213  C CD2  A LEU   A 1 10  ? 6.045  -13.034 8.654   0.40 14.50 ?  10  LEU   A CD2  1 
ATOM   214  C CD2  B LEU   A 1 10  ? 6.600  -12.911 8.396   0.60 17.52 ?  10  LEU   A CD2  1 
ATOM   215  H H    A LEU   A 1 10  ? 8.780  -10.557 11.766  0.40 14.41 ?  10  LEU   A H    1 
ATOM   216  H H    B LEU   A 1 10  ? 9.044  -10.872 11.875  0.60 16.44 ?  10  LEU   A H    1 
ATOM   217  H HA   A LEU   A 1 10  ? 7.631  -12.844 12.555  0.40 14.09 ?  10  LEU   A HA   1 
ATOM   218  H HA   B LEU   A 1 10  ? 7.962  -13.228 12.494  0.60 16.03 ?  10  LEU   A HA   1 
ATOM   219  H HB2  A LEU   A 1 10  ? 6.523  -11.549 10.954  0.40 15.10 ?  10  LEU   A HB2  1 
ATOM   220  H HB2  B LEU   A 1 10  ? 6.814  -11.983 10.979  0.60 17.85 ?  10  LEU   A HB2  1 
ATOM   221  H HB3  A LEU   A 1 10  ? 7.772  -11.665 9.982   0.40 15.10 ?  10  LEU   A HB3  1 
ATOM   222  H HB3  B LEU   A 1 10  ? 8.102  -11.761 10.095  0.60 17.85 ?  10  LEU   A HB3  1 
ATOM   223  H HG   A LEU   A 1 10  ? 7.325  -14.023 9.875   0.40 16.37 ?  10  LEU   A HG   1 
ATOM   224  H HG   B LEU   A 1 10  ? 7.914  -14.066 9.429   0.60 20.20 ?  10  LEU   A HG   1 
ATOM   225  H HD11 A LEU   A 1 10  ? 5.249  -14.795 10.504  0.40 17.14 ?  10  LEU   A HD11 1 
ATOM   226  H HD11 B LEU   A 1 10  ? 5.732  -14.997 9.632   0.60 20.83 ?  10  LEU   A HD11 1 
ATOM   227  H HD12 A LEU   A 1 10  ? 5.983  -14.193 11.777  0.40 17.14 ?  10  LEU   A HD12 1 
ATOM   228  H HD12 B LEU   A 1 10  ? 6.555  -14.980 10.992  0.60 20.83 ?  10  LEU   A HD12 1 
ATOM   229  H HD13 A LEU   A 1 10  ? 4.855  -13.353 11.041  0.40 17.14 ?  10  LEU   A HD13 1 
ATOM   230  H HD13 B LEU   A 1 10  ? 5.429  -13.889 10.728  0.60 20.83 ?  10  LEU   A HD13 1 
ATOM   231  H HD21 A LEU   A 1 10  ? 5.658  -13.841 8.283   0.40 17.38 ?  10  LEU   A HD21 1 
ATOM   232  H HD21 B LEU   A 1 10  ? 6.311  -13.625 7.807   0.60 21.00 ?  10  LEU   A HD21 1 
ATOM   233  H HD22 A LEU   A 1 10  ? 5.367  -12.354 8.762   0.40 17.38 ?  10  LEU   A HD22 1 
ATOM   234  H HD22 B LEU   A 1 10  ? 5.845  -12.342 8.620   0.60 21.00 ?  10  LEU   A HD22 1 
ATOM   235  H HD23 A LEU   A 1 10  ? 6.757  -12.711 8.080   0.40 17.38 ?  10  LEU   A HD23 1 
ATOM   236  H HD23 B LEU   A 1 10  ? 7.294  -12.387 7.971   0.60 21.00 ?  10  LEU   A HD23 1 
ATOM   237  N N    A LYS   A 1 11  ? 9.170  -14.631 11.805  0.40 10.83 ?  11  LYS   A N    1 
ATOM   238  N N    B LYS   A 1 11  ? 9.515  -14.967 11.705  0.60 12.07 ?  11  LYS   A N    1 
ATOM   239  C CA   A LYS   A 1 11  ? 10.159 -15.631 11.434  0.40 10.44 ?  11  LYS   A CA   1 
ATOM   240  C CA   B LYS   A 1 11  ? 10.506 -15.964 11.318  0.60 11.97 ?  11  LYS   A CA   1 
ATOM   241  C C    A LYS   A 1 11  ? 9.814  -16.171 10.053  0.40 10.26 ?  11  LYS   A C    1 
ATOM   242  C C    B LYS   A 1 11  ? 10.116 -16.546 9.964   0.60 11.83 ?  11  LYS   A C    1 
ATOM   243  O O    A LYS   A 1 11  ? 8.716  -16.692 9.846   0.40 10.93 ?  11  LYS   A O    1 
ATOM   244  O O    B LYS   A 1 11  ? 9.067  -17.178 9.845   0.60 12.86 ?  11  LYS   A O    1 
ATOM   245  C CB   A LYS   A 1 11  ? 10.152 -16.746 12.475  0.40 10.71 ?  11  LYS   A CB   1 
ATOM   246  C CB   B LYS   A 1 11  ? 10.545 -17.063 12.381  0.60 12.11 ?  11  LYS   A CB   1 
ATOM   247  C CG   A LYS   A 1 11  ? 11.195 -17.826 12.282  0.40 10.91 ?  11  LYS   A CG   1 
ATOM   248  C CG   B LYS   A 1 11  ? 11.592 -18.146 12.176  0.60 12.75 ?  11  LYS   A CG   1 
ATOM   249  C CD   A LYS   A 1 11  ? 11.255 -18.713 13.517  0.40 11.31 ?  11  LYS   A CD   1 
ATOM   250  C CD   B LYS   A 1 11  ? 11.662 -19.047 13.412  0.60 13.25 ?  11  LYS   A CD   1 
ATOM   251  C CE   A LYS   A 1 11  ? 12.237 -19.863 13.354  0.40 11.05 ?  11  LYS   A CE   1 
ATOM   252  C CE   B LYS   A 1 11  ? 12.719 -20.134 13.291  0.60 13.55 ?  11  LYS   A CE   1 
ATOM   253  N NZ   A LYS   A 1 11  ? 13.642 -19.416 13.139  0.40 11.28 ?  11  LYS   A NZ   1 
ATOM   254  N NZ   B LYS   A 1 11  ? 14.069 -19.593 13.003  0.60 13.90 ?  11  LYS   A NZ   1 
ATOM   255  H H    A LYS   A 1 11  ? 8.517  -14.923 12.282  0.40 12.98 ?  11  LYS   A H    1 
ATOM   256  H H    B LYS   A 1 11  ? 8.867  -15.290 12.171  0.60 14.46 ?  11  LYS   A H    1 
ATOM   257  H HA   A LYS   A 1 11  ? 11.033 -15.218 11.402  0.40 12.50 ?  11  LYS   A HA   1 
ATOM   258  H HA   B LYS   A 1 11  ? 11.385 -15.557 11.252  0.60 14.34 ?  11  LYS   A HA   1 
ATOM   259  H HB2  A LYS   A 1 11  ? 10.302 -16.344 13.345  0.40 12.83 ?  11  LYS   A HB2  1 
ATOM   260  H HB2  B LYS   A 1 11  ? 10.723 -16.655 13.243  0.60 14.51 ?  11  LYS   A HB2  1 
ATOM   261  H HB3  A LYS   A 1 11  ? 9.281  -17.169 12.458  0.40 12.83 ?  11  LYS   A HB3  1 
ATOM   262  H HB3  B LYS   A 1 11  ? 9.680  -17.501 12.403  0.60 14.51 ?  11  LYS   A HB3  1 
ATOM   263  H HG2  A LYS   A 1 11  ? 10.956 -18.372 11.516  0.40 13.07 ?  11  LYS   A HG2  1 
ATOM   264  H HG2  B LYS   A 1 11  ? 11.350 -18.695 11.409  0.60 15.28 ?  11  LYS   A HG2  1 
ATOM   265  H HG3  A LYS   A 1 11  ? 12.065 -17.417 12.150  0.40 13.07 ?  11  LYS   A HG3  1 
ATOM   266  H HG3  B LYS   A 1 11  ? 12.462 -17.741 12.040  0.60 15.28 ?  11  LYS   A HG3  1 
ATOM   267  H HD2  A LYS   A 1 11  ? 11.531 -18.176 14.277  0.40 13.55 ?  11  LYS   A HD2  1 
ATOM   268  H HD2  B LYS   A 1 11  ? 11.874 -18.504 14.185  0.60 15.87 ?  11  LYS   A HD2  1 
ATOM   269  H HD3  A LYS   A 1 11  ? 10.371 -19.085 13.678  0.40 13.55 ?  11  LYS   A HD3  1 
ATOM   270  H HD3  B LYS   A 1 11  ? 10.800 -19.479 13.536  0.60 15.87 ?  11  LYS   A HD3  1 
ATOM   271  H HE2  A LYS   A 1 11  ? 12.215 -20.405 14.156  0.40 13.23 ?  11  LYS   A HE2  1 
ATOM   272  H HE2  B LYS   A 1 11  ? 12.765 -20.630 14.127  0.60 16.23 ?  11  LYS   A HE2  1 
ATOM   273  H HE3  A LYS   A 1 11  ? 11.971 -20.392 12.587  0.40 13.23 ?  11  LYS   A HE3  1 
ATOM   274  H HE3  B LYS   A 1 11  ? 12.476 -20.730 12.568  0.60 16.23 ?  11  LYS   A HE3  1 
ATOM   275  H HZ1  A LYS   A 1 11  ? 14.175 -20.123 13.048  0.40 13.51 ?  11  LYS   A HZ1  1 
ATOM   276  H HZ1  B LYS   A 1 11  ? 14.661 -20.256 12.962  0.60 16.66 ?  11  LYS   A HZ1  1 
ATOM   277  H HZ2  A LYS   A 1 11  ? 13.696 -18.918 12.403  0.40 13.51 ?  11  LYS   A HZ2  1 
ATOM   278  H HZ2  B LYS   A 1 11  ? 14.063 -19.162 12.224  0.60 16.66 ?  11  LYS   A HZ2  1 
ATOM   279  H HZ3  A LYS   A 1 11  ? 13.919 -18.933 13.834  0.40 13.51 ?  11  LYS   A HZ3  1 
ATOM   280  H HZ3  B LYS   A 1 11  ? 14.313 -19.027 13.645  0.60 16.66 ?  11  LYS   A HZ3  1 
ATOM   281  N N    A LEU   A 1 12  ? 10.724 -16.016 9.095   0.40 10.46 ?  12  LEU   A N    1 
ATOM   282  N N    B LEU   A 1 12  ? 10.961 -16.358 8.949   0.60 11.29 ?  12  LEU   A N    1 
ATOM   283  C CA   A LEU   A 1 12  ? 10.475 -16.550 7.761   0.40 10.69 ?  12  LEU   A CA   1 
ATOM   284  C CA   B LEU   A 1 12  ? 10.689 -16.933 7.632   0.60 11.67 ?  12  LEU   A CA   1 
ATOM   285  C C    A LEU   A 1 12  ? 11.052 -17.950 7.592   0.40 10.36 ?  12  LEU   A C    1 
ATOM   286  C C    B LEU   A 1 12  ? 11.277 -18.330 7.474   0.60 11.87 ?  12  LEU   A C    1 
ATOM   287  O O    A LEU   A 1 12  ? 10.405 -18.822 7.001   0.40 10.25 ?  12  LEU   A O    1 
ATOM   288  O O    B LEU   A 1 12  ? 10.634 -19.207 6.890   0.60 12.21 ?  12  LEU   A O    1 
ATOM   289  C CB   A LEU   A 1 12  ? 11.060 -15.619 6.698   0.40 11.17 ?  12  LEU   A CB   1 
ATOM   290  C CB   B LEU   A 1 12  ? 11.235 -16.036 6.516   0.60 12.44 ?  12  LEU   A CB   1 
ATOM   291  C CG   A LEU   A 1 12  ? 10.426 -14.234 6.585   0.40 11.73 ?  12  LEU   A CG   1 
ATOM   292  C CG   B LEU   A 1 12  ? 10.565 -14.678 6.309   0.60 13.52 ?  12  LEU   A CG   1 
ATOM   293  C CD1  A LEU   A 1 12  ? 11.170 -13.401 5.556   0.40 12.11 ?  12  LEU   A CD1  1 
ATOM   294  C CD1  B LEU   A 1 12  ? 11.273 -13.928 5.189   0.60 14.21 ?  12  LEU   A CD1  1 
ATOM   295  C CD2  A LEU   A 1 12  ? 8.961  -14.346 6.215   0.40 12.21 ?  12  LEU   A CD2  1 
ATOM   296  C CD2  B LEU   A 1 12  ? 9.079  -14.838 6.000   0.60 14.31 ?  12  LEU   A CD2  1 
ATOM   297  H H    A LEU   A 1 12  ? 11.474 -15.600 9.188   0.40 12.53 ?  12  LEU   A H    1 
ATOM   298  H H    B LEU   A 1 12  ? 11.692 -15.905 8.996   0.60 13.52 ?  12  LEU   A H    1 
ATOM   299  H HA   A LEU   A 1 12  ? 9.511  -16.595 7.619   0.40 12.81 ?  12  LEU   A HA   1 
ATOM   300  H HA   B LEU   A 1 12  ? 9.728  -17.002 7.517   0.60 13.98 ?  12  LEU   A HA   1 
ATOM   301  H HB2  A LEU   A 1 12  ? 11.999 -15.492 6.893   0.40 13.37 ?  12  LEU   A HB2  1 
ATOM   302  H HB2  B LEU   A 1 12  ? 12.169 -15.868 6.695   0.60 14.90 ?  12  LEU   A HB2  1 
ATOM   303  H HB3  A LEU   A 1 12  ? 10.962 -16.051 5.836   0.40 13.37 ?  12  LEU   A HB3  1 
ATOM   304  H HB3  B LEU   A 1 12  ? 11.152 -16.522 5.678   0.60 14.90 ?  12  LEU   A HB3  1 
ATOM   305  H HG   A LEU   A 1 12  ? 10.489 -13.781 7.439   0.40 14.05 ?  12  LEU   A HG   1 
ATOM   306  H HG   B LEU   A 1 12  ? 10.650 -14.156 7.118   0.60 16.20 ?  12  LEU   A HG   1 
ATOM   307  H HD11 A LEU   A 1 12  ? 10.757 -12.525 5.499   0.40 14.51 ?  12  LEU   A HD11 1 
ATOM   308  H HD11 B LEU   A 1 12  ? 10.844 -13.069 5.060   0.60 17.03 ?  12  LEU   A HD11 1 
ATOM   309  H HD12 A LEU   A 1 12  ? 12.096 -13.314 5.828   0.40 14.51 ?  12  LEU   A HD12 1 
ATOM   310  H HD12 B LEU   A 1 12  ? 12.204 -13.801 5.434   0.60 17.03 ?  12  LEU   A HD12 1 
ATOM   311  H HD13 A LEU   A 1 12  ? 11.120 -13.846 4.694   0.40 14.51 ?  12  LEU   A HD13 1 
ATOM   312  H HD13 B LEU   A 1 12  ? 11.218 -14.451 4.372   0.60 17.03 ?  12  LEU   A HD13 1 
ATOM   313  H HD21 A LEU   A 1 12  ? 8.626  -13.466 5.984   0.40 14.63 ?  12  LEU   A HD21 1 
ATOM   314  H HD21 B LEU   A 1 12  ? 8.717  -13.979 5.734   0.60 17.15 ?  12  LEU   A HD21 1 
ATOM   315  H HD22 A LEU   A 1 12  ? 8.874  -14.943 5.454   0.40 14.63 ?  12  LEU   A HD22 1 
ATOM   316  H HD22 B LEU   A 1 12  ? 8.974  -15.478 5.279   0.60 17.15 ?  12  LEU   A HD22 1 
ATOM   317  H HD23 A LEU   A 1 12  ? 8.471  -14.700 6.972   0.40 14.63 ?  12  LEU   A HD23 1 
ATOM   318  H HD23 B LEU   A 1 12  ? 8.625  -15.159 6.794   0.60 17.15 ?  12  LEU   A HD23 1 
ATOM   319  N N    A THR   A 1 13  ? 12.265 -18.173 8.089   0.40 10.29 ?  13  THR   A N    1 
ATOM   320  N N    B THR   A 1 13  ? 12.496 -18.540 7.964   0.60 12.10 ?  13  THR   A N    1 
ATOM   321  C CA   A THR   A 1 13  ? 12.930 -19.466 8.007   0.40 10.55 ?  13  THR   A CA   1 
ATOM   322  C CA   B THR   A 1 13  ? 13.190 -19.818 7.857   0.60 12.25 ?  13  THR   A CA   1 
ATOM   323  C C    A THR   A 1 13  ? 13.697 -19.697 9.306   0.40 10.90 ?  13  THR   A C    1 
ATOM   324  C C    B THR   A 1 13  ? 13.985 -20.038 9.138   0.60 12.11 ?  13  THR   A C    1 
ATOM   325  O O    A THR   A 1 13  ? 13.593 -18.929 10.267  0.40 11.36 ?  13  THR   A O    1 
ATOM   326  O O    B THR   A 1 13  ? 13.897 -19.261 10.095  0.60 11.83 ?  13  THR   A O    1 
ATOM   327  C CB   A THR   A 1 13  ? 13.892 -19.521 6.812   0.40 11.36 ?  13  THR   A CB   1 
ATOM   328  C CB   B THR   A 1 13  ? 14.152 -19.856 6.661   0.60 13.09 ?  13  THR   A CB   1 
ATOM   329  O OG1  A THR   A 1 13  ? 14.959 -18.595 7.030   0.40 11.47 ?  13  THR   A OG1  1 
ATOM   330  O OG1  B THR   A 1 13  ? 15.228 -18.942 6.900   0.60 13.15 ?  13  THR   A OG1  1 
ATOM   331  C CG2  A THR   A 1 13  ? 13.191 -19.182 5.500   0.40 12.41 ?  13  THR   A CG2  1 
ATOM   332  C CG2  B THR   A 1 13  ? 13.461 -19.486 5.365   0.60 14.35 ?  13  THR   A CG2  1 
ATOM   333  H H    A THR   A 1 13  ? 12.732 -17.568 8.475   0.40 12.33 ?  13  THR   A H    1 
ATOM   334  H H    B THR   A 1 13  ? 12.953 -17.943 8.376   0.60 14.49 ?  13  THR   A H    1 
ATOM   335  H HA   A THR   A 1 13  ? 12.261 -20.165 7.903   0.40 12.63 ?  13  THR   A HA   1 
ATOM   336  H HA   B THR   A 1 13  ? 12.544 -20.543 7.759   0.60 14.67 ?  13  THR   A HA   1 
ATOM   337  H HB   A THR   A 1 13  ? 14.259 -20.412 6.742   0.40 13.60 ?  13  THR   A HB   1 
ATOM   338  H HB   B THR   A 1 13  ? 14.508 -20.756 6.565   0.60 15.68 ?  13  THR   A HB   1 
ATOM   339  H HG1  A THR   A 1 13  ? 15.516 -18.914 7.565   0.40 13.74 ?  13  THR   A HG1  1 
ATOM   340  H HG1  B THR   A 1 13  ? 15.771 -18.960 6.258   0.60 15.75 ?  13  THR   A HG1  1 
ATOM   341  H HG21 A THR   A 1 13  ? 13.811 -19.293 4.759   0.40 14.87 ?  13  THR   A HG21 1 
ATOM   342  H HG21 B THR   A 1 13  ? 14.062 -19.633 4.617   0.60 17.19 ?  13  THR   A HG21 1 
ATOM   343  H HG22 A THR   A 1 13  ? 12.437 -19.778 5.365   0.40 14.87 ?  13  THR   A HG22 1 
ATOM   344  H HG22 B THR   A 1 13  ? 12.670 -20.034 5.243   0.60 17.19 ?  13  THR   A HG22 1 
ATOM   345  H HG23 A THR   A 1 13  ? 12.876 -18.268 5.513   0.40 14.87 ?  13  THR   A HG23 1 
ATOM   346  H HG23 B THR   A 1 13  ? 13.200 -18.553 5.382   0.60 17.19 ?  13  THR   A HG23 1 
ATOM   347  N N    A ASP   A 1 14  ? 14.499 -20.759 9.310   0.40 11.25 ?  14  ASP   A N    1 
ATOM   348  N N    B ASP   A 1 14  ? 14.799 -21.098 9.140   0.60 12.68 ?  14  ASP   A N    1 
ATOM   349  C CA   A ASP   A 1 14  ? 15.344 -21.076 10.456  0.40 11.51 ?  14  ASP   A CA   1 
ATOM   350  C CA   B ASP   A 1 14  ? 15.648 -21.371 10.291  0.60 13.65 ?  14  ASP   A CA   1 
ATOM   351  C C    A ASP   A 1 14  ? 16.195 -19.882 10.878  0.40 10.69 ?  14  ASP   A C    1 
ATOM   352  C C    B ASP   A 1 14  ? 16.508 -20.166 10.660  0.60 12.78 ?  14  ASP   A C    1 
ATOM   353  O O    A ASP   A 1 14  ? 16.393 -19.647 12.076  0.40 11.33 ?  14  ASP   A O    1 
ATOM   354  O O    B ASP   A 1 14  ? 16.787 -19.950 11.845  0.60 13.28 ?  14  ASP   A O    1 
ATOM   355  C CB   A ASP   A 1 14  ? 16.240 -22.263 10.101  0.40 13.51 ?  14  ASP   A CB   1 
ATOM   356  C CB   B ASP   A 1 14  ? 16.540 -22.587 10.006  0.60 16.69 ?  14  ASP   A CB   1 
ATOM   357  C CG   A ASP   A 1 14  ? 17.250 -22.581 11.186  0.40 15.74 ?  14  ASP   A CG   1 
ATOM   358  C CG   B ASP   A 1 14  ? 17.235 -23.105 11.251  0.60 20.49 ?  14  ASP   A CG   1 
ATOM   359  O OD1  A ASP   A 1 14  ? 16.834 -23.045 12.268  0.40 16.60 ?  14  ASP   A OD1  1 
ATOM   360  O OD1  B ASP   A 1 14  ? 16.533 -23.543 12.185  0.60 21.93 ?  14  ASP   A OD1  1 
ATOM   361  O OD2  A ASP   A 1 14  ? 18.458 -22.376 10.951  0.40 16.79 -1 14  ASP   A OD2  1 
ATOM   362  O OD2  B ASP   A 1 14  ? 18.483 -23.077 11.290  0.60 22.55 -1 14  ASP   A OD2  1 
ATOM   363  H H    A ASP   A 1 14  ? 14.565 -21.301 8.659   0.40 13.48 ?  14  ASP   A H    1 
ATOM   364  H H    B ASP   A 1 14  ? 14.877 -21.672 8.497   0.60 15.19 ?  14  ASP   A H    1 
ATOM   365  H HA   A ASP   A 1 14  ? 14.777 -21.320 11.206  0.40 13.78 ?  14  ASP   A HA   1 
ATOM   366  H HA   B ASP   A 1 14  ? 15.095 -21.596 11.055  0.60 16.36 ?  14  ASP   A HA   1 
ATOM   367  H HB2  A ASP   A 1 14  ? 15.673 -23.038 9.965   0.40 16.18 ?  14  ASP   A HB2  1 
ATOM   368  H HB2  B ASP   A 1 14  ? 16.003 -23.307 9.615   0.60 20.01 ?  14  ASP   A HB2  1 
ATOM   369  H HB3  A ASP   A 1 14  ? 16.717 -22.051 9.285   0.40 16.18 ?  14  ASP   A HB3  1 
ATOM   370  H HB3  B ASP   A 1 14  ? 17.250 -22.346 9.397   0.60 20.01 ?  14  ASP   A HB3  1 
ATOM   371  N N    A ASN   A 1 15  ? 16.692 -19.101 9.912   0.40 10.44 ?  15  ASN   A N    1 
ATOM   372  N N    B ASN   A 1 15  ? 16.939 -19.369 9.670   0.60 11.52 ?  15  ASN   A N    1 
ATOM   373  C CA   A ASN   A 1 15  ? 17.679 -18.068 10.204  0.40 10.60 ?  15  ASN   A CA   1 
ATOM   374  C CA   B ASN   A 1 15  ? 17.929 -18.323 9.910   0.60 11.49 ?  15  ASN   A CA   1 
ATOM   375  C C    A ASN   A 1 15  ? 17.315 -16.666 9.739   0.40 10.61 ?  15  ASN   A C    1 
ATOM   376  C C    B ASN   A 1 15  ? 17.545 -16.931 9.417   0.60 11.81 ?  15  ASN   A C    1 
ATOM   377  O O    A ASN   A 1 15  ? 18.058 -15.734 10.061  0.40 11.40 ?  15  ASN   A O    1 
ATOM   378  O O    B ASN   A 1 15  ? 18.319 -15.993 9.632   0.60 12.60 ?  15  ASN   A O    1 
ATOM   379  C CB   A ASN   A 1 15  ? 19.055 -18.437 9.622   0.40 10.94 ?  15  ASN   A CB   1 
ATOM   380  C CB   B ASN   A 1 15  ? 19.281 -18.714 9.290   0.60 11.01 ?  15  ASN   A CB   1 
ATOM   381  C CG   A ASN   A 1 15  ? 19.040 -18.598 8.112   0.40 11.18 ?  15  ASN   A CG   1 
ATOM   382  C CG   B ASN   A 1 15  ? 19.237 -18.737 7.776   0.60 11.36 ?  15  ASN   A CG   1 
ATOM   383  O OD1  A ASN   A 1 15  ? 18.233 -19.352 7.567   0.40 11.17 ?  15  ASN   A OD1  1 
ATOM   384  O OD1  B ASN   A 1 15  ? 18.553 -19.570 7.183   0.60 11.71 ?  15  ASN   A OD1  1 
ATOM   385  N ND2  A ASN   A 1 15  ? 19.928 -17.878 7.425   0.40 11.70 ?  15  ASN   A ND2  1 
ATOM   386  N ND2  B ASN   A 1 15  ? 19.954 -17.819 7.141   0.60 12.01 ?  15  ASN   A ND2  1 
ATOM   387  H H    A ASN   A 1 15  ? 16.455 -19.139 9.091   0.40 12.50 ?  15  ASN   A H    1 
ATOM   388  H H    B ASN   A 1 15  ? 16.677 -19.434 8.851   0.60 13.80 ?  15  ASN   A H    1 
ATOM   389  H HA   A ASN   A 1 15  ? 17.784 -18.013 11.165  0.40 12.69 ?  15  ASN   A HA   1 
ATOM   390  H HA   B ASN   A 1 15  ? 18.068 -18.264 10.865  0.60 13.76 ?  15  ASN   A HA   1 
ATOM   391  H HB2  A ASN   A 1 15  ? 19.685 -17.733 9.842   0.40 13.11 ?  15  ASN   A HB2  1 
ATOM   392  H HB2  B ASN   A 1 15  ? 19.954 -18.067 9.563   0.60 13.18 ?  15  ASN   A HB2  1 
ATOM   393  H HB3  A ASN   A 1 15  ? 19.335 -19.274 10.007  0.40 13.11 ?  15  ASN   A HB3  1 
ATOM   394  H HB3  B ASN   A 1 15  ? 19.538 -19.602 9.604   0.60 13.18 ?  15  ASN   A HB3  1 
ATOM   395  H HD21 A ASN   A 1 15  ? 19.961 -17.936 6.565   0.40 14.01 ?  15  ASN   A HD21 1 
ATOM   396  H HD21 B ASN   A 1 15  ? 19.957 -17.806 6.281   0.60 14.38 ?  15  ASN   A HD21 1 
ATOM   397  H HD22 A ASN   A 1 15  ? 20.477 -17.364 7.840   0.40 14.01 ?  15  ASN   A HD22 1 
ATOM   398  H HD22 B ASN   A 1 15  ? 20.417 -17.251 7.584   0.60 14.38 ?  15  ASN   A HD22 1 
ATOM   399  N N    A VAL   A 1 16  ? 16.205 -16.476 9.027   0.40 10.36 ?  16  VAL   A N    1 
ATOM   400  N N    B VAL   A 1 16  ? 16.392 -16.761 8.770   0.60 11.37 ?  16  VAL   A N    1 
ATOM   401  C CA   A VAL   A 1 16  ? 15.834 -15.183 8.461   0.40 10.28 ?  16  VAL   A CA   1 
ATOM   402  C CA   B VAL   A 1 16  ? 15.981 -15.481 8.199   0.60 11.52 ?  16  VAL   A CA   1 
ATOM   403  C C    A VAL   A 1 16  ? 14.551 -14.691 9.122   0.40 10.39 ?  16  VAL   A C    1 
ATOM   404  C C    B VAL   A 1 16  ? 14.730 -14.979 8.919   0.60 11.30 ?  16  VAL   A C    1 
ATOM   405  O O    A VAL   A 1 16  ? 13.545 -15.414 9.175   0.40 10.77 ?  16  VAL   A O    1 
ATOM   406  O O    B VAL   A 1 16  ? 13.728 -15.700 9.024   0.60 11.90 ?  16  VAL   A O    1 
ATOM   407  C CB   A VAL   A 1 16  ? 15.692 -15.244 6.930   0.40 10.12 ?  16  VAL   A CB   1 
ATOM   408  C CB   B VAL   A 1 16  ? 15.729 -15.586 6.683   0.60 12.64 ?  16  VAL   A CB   1 
ATOM   409  C CG1  A VAL   A 1 16  ? 15.315 -13.871 6.368   0.40 10.41 ?  16  VAL   A CG1  1 
ATOM   410  C CG1  B VAL   A 1 16  ? 15.243 -14.255 6.134   0.60 13.31 ?  16  VAL   A CG1  1 
ATOM   411  C CG2  A VAL   A 1 16  ? 16.976 -15.736 6.292   0.40 10.88 ?  16  VAL   A CG2  1 
ATOM   412  C CG2  B VAL   A 1 16  ? 16.984 -16.046 5.946   0.60 13.13 ?  16  VAL   A CG2  1 
ATOM   413  H H    A VAL   A 1 16  ? 15.627 -17.090 8.863   0.40 12.41 ?  16  VAL   A H    1 
ATOM   414  H H    B VAL   A 1 16  ? 15.824 -17.397 8.643   0.60 13.62 ?  16  VAL   A H    1 
ATOM   415  H HA   A VAL   A 1 16  ? 16.521 -14.532 8.661   0.40 12.31 ?  16  VAL   A HA   1 
ATOM   416  H HA   B VAL   A 1 16  ? 16.694 -14.835 8.338   0.60 13.80 ?  16  VAL   A HA   1 
ATOM   417  H HB   A VAL   A 1 16  ? 14.983 -15.866 6.699   0.40 12.12 ?  16  VAL   A HB   1 
ATOM   418  H HB   B VAL   A 1 16  ? 15.035 -16.249 6.531   0.60 15.14 ?  16  VAL   A HB   1 
ATOM   419  H HG11 A VAL   A 1 16  ? 15.390 -13.895 5.399   0.40 12.47 ?  16  VAL   A HG11 1 
ATOM   420  H HG11 B VAL   A 1 16  ? 15.290 -14.283 5.168   0.60 15.95 ?  16  VAL   A HG11 1 
ATOM   421  H HG12 A VAL   A 1 16  ? 14.400 -13.664 6.618   0.40 12.47 ?  16  VAL   A HG12 1 
ATOM   422  H HG12 B VAL   A 1 16  ? 14.326 -14.113 6.418   0.60 15.95 ?  16  VAL   A HG12 1 
ATOM   423  H HG13 A VAL   A 1 16  ? 15.917 -13.206 6.729   0.40 12.47 ?  16  VAL   A HG13 1 
ATOM   424  H HG13 B VAL   A 1 16  ? 15.812 -13.551 6.477   0.60 15.95 ?  16  VAL   A HG13 1 
ATOM   425  H HG21 A VAL   A 1 16  ? 16.973 -15.504 5.350   0.40 13.03 ?  16  VAL   A HG21 1 
ATOM   426  H HG21 B VAL   A 1 16  ? 16.830 -15.969 4.992   0.60 15.73 ?  16  VAL   A HG21 1 
ATOM   427  H HG22 A VAL   A 1 16  ? 17.726 -15.318 6.736   0.40 13.03 ?  16  VAL   A HG22 1 
ATOM   428  H HG22 B VAL   A 1 16  ? 17.727 -15.479 6.206   0.60 15.73 ?  16  VAL   A HG22 1 
ATOM   429  H HG23 A VAL   A 1 16  ? 17.026 -16.699 6.397   0.40 13.03 ?  16  VAL   A HG23 1 
ATOM   430  H HG23 B VAL   A 1 16  ? 17.173 -16.967 6.179   0.60 15.73 ?  16  VAL   A HG23 1 
ATOM   431  N N    A TYR   A 1 17  ? 14.587 -13.443 9.591   0.40 10.31 ?  17  TYR   A N    1 
ATOM   432  N N    B TYR   A 1 17  ? 14.788 -13.718 9.364   0.60 11.16 ?  17  TYR   A N    1 
ATOM   433  C CA   A TYR   A 1 17  ? 13.486 -12.788 10.280  0.40 10.76 ?  17  TYR   A CA   1 
ATOM   434  C CA   B TYR   A 1 17  ? 13.729 -13.039 10.097  0.60 11.12 ?  17  TYR   A CA   1 
ATOM   435  C C    A TYR   A 1 17  ? 13.236 -11.449 9.605   0.40 10.79 ?  17  TYR   A C    1 
ATOM   436  C C    B TYR   A 1 17  ? 13.431 -11.705 9.415   0.60 11.37 ?  17  TYR   A C    1 
ATOM   437  O O    A TYR   A 1 17  ? 14.170 -10.820 9.104   0.40 10.37 ?  17  TYR   A O    1 
ATOM   438  O O    B TYR   A 1 17  ? 14.286 -11.144 8.724   0.60 11.05 ?  17  TYR   A O    1 
ATOM   439  C CB   A TYR   A 1 17  ? 13.848 -12.567 11.755  0.40 11.74 ?  17  TYR   A CB   1 
ATOM   440  C CB   B TYR   A 1 17  ? 14.187 -12.771 11.539  0.60 11.61 ?  17  TYR   A CB   1 
ATOM   441  C CG   A TYR   A 1 17  ? 14.109 -13.861 12.490  0.40 13.06 ?  17  TYR   A CG   1 
ATOM   442  C CG   B TYR   A 1 17  ? 14.332 -14.015 12.396  0.60 12.69 ?  17  TYR   A CG   1 
ATOM   443  C CD1  A TYR   A 1 17  ? 15.307 -14.546 12.333  0.40 13.86 ?  17  TYR   A CD1  1 
ATOM   444  C CD1  B TYR   A 1 17  ? 15.483 -14.799 12.360  0.60 13.54 ?  17  TYR   A CD1  1 
ATOM   445  C CD2  A TYR   A 1 17  ? 13.147 -14.411 13.324  0.40 13.79 ?  17  TYR   A CD2  1 
ATOM   446  C CD2  B TYR   A 1 17  ? 13.307 -14.406 13.247  0.60 13.33 ?  17  TYR   A CD2  1 
ATOM   447  C CE1  A TYR   A 1 17  ? 15.540 -15.742 12.994  0.40 14.37 ?  17  TYR   A CE1  1 
ATOM   448  C CE1  B TYR   A 1 17  ? 15.594 -15.944 13.149  0.60 14.36 ?  17  TYR   A CE1  1 
ATOM   449  C CE2  A TYR   A 1 17  ? 13.372 -15.605 13.991  0.40 14.39 ?  17  TYR   A CE2  1 
ATOM   450  C CE2  B TYR   A 1 17  ? 13.413 -15.539 14.035  0.60 14.28 ?  17  TYR   A CE2  1 
ATOM   451  C CZ   A TYR   A 1 17  ? 14.570 -16.267 13.823  0.40 14.76 ?  17  TYR   A CZ   1 
ATOM   452  C CZ   B TYR   A 1 17  ? 14.552 -16.304 13.984  0.60 14.66 ?  17  TYR   A CZ   1 
ATOM   453  O OH   A TYR   A 1 17  ? 14.802 -17.453 14.483  0.40 15.21 ?  17  TYR   A OH   1 
ATOM   454  O OH   B TYR   A 1 17  ? 14.648 -17.427 14.771  0.60 15.33 ?  17  TYR   A OH   1 
ATOM   455  H H    A TYR   A 1 17  ? 15.268 -12.917 9.502   0.40 12.35 ?  17  TYR   A H    1 
ATOM   456  H H    B TYR   A 1 17  ? 15.476 -13.216 9.232   0.60 13.36 ?  17  TYR   A H    1 
ATOM   457  H HA   A TYR   A 1 17  ? 12.676 -13.313 10.222  0.40 12.88 ?  17  TYR   A HA   1 
ATOM   458  H HA   B TYR   A 1 17  ? 12.930 -13.592 10.103  0.60 13.32 ?  17  TYR   A HA   1 
ATOM   459  H HB2  A TYR   A 1 17  ? 14.648 -12.021 11.805  0.40 14.06 ?  17  TYR   A HB2  1 
ATOM   460  H HB2  B TYR   A 1 17  ? 15.053 -12.333 11.510  0.60 13.91 ?  17  TYR   A HB2  1 
ATOM   461  H HB3  A TYR   A 1 17  ? 13.114 -12.114 12.197  0.40 14.06 ?  17  TYR   A HB3  1 
ATOM   462  H HB3  B TYR   A 1 17  ? 13.541 -12.195 11.963  0.60 13.91 ?  17  TYR   A HB3  1 
ATOM   463  H HD1  A TYR   A 1 17  ? 15.959 -14.195 11.772  0.40 16.60 ?  17  TYR   A HD1  1 
ATOM   464  H HD1  B TYR   A 1 17  ? 16.186 -14.567 11.796  0.60 16.23 ?  17  TYR   A HD1  1 
ATOM   465  H HD2  A TYR   A 1 17  ? 12.334 -13.967 13.438  0.40 16.52 ?  17  TYR   A HD2  1 
ATOM   466  H HD2  B TYR   A 1 17  ? 12.531 -13.900 13.288  0.60 15.98 ?  17  TYR   A HD2  1 
ATOM   467  H HE1  A TYR   A 1 17  ? 16.350 -16.187 12.880  0.40 17.22 ?  17  TYR   A HE1  1 
ATOM   468  H HE1  B TYR   A 1 17  ? 16.369 -16.464 13.119  0.60 17.21 ?  17  TYR   A HE1  1 
ATOM   469  H HE2  A TYR   A 1 17  ? 12.719 -15.958 14.549  0.40 17.24 ?  17  TYR   A HE2  1 
ATOM   470  H HE2  B TYR   A 1 17  ? 12.715 -15.783 14.602  0.60 17.11 ?  17  TYR   A HE2  1 
ATOM   471  H HH   A TYR   A 1 17  ? 15.567 -17.748 14.295  0.40 18.23 ?  17  TYR   A HH   1 
ATOM   472  H HH   B TYR   A 1 17  ? 13.881 -17.680 14.999  0.60 18.37 ?  17  TYR   A HH   1 
ATOM   473  N N    A ILE   A 1 18  ? 11.974 -11.009 9.585   0.40 11.14 ?  18  ILE   A N    1 
ATOM   474  N N    B ILE   A 1 18  ? 12.229 -11.165 9.625   0.60 12.12 ?  18  ILE   A N    1 
ATOM   475  C CA   A ILE   A 1 18  ? 11.592 -9.807  8.849   0.40 11.81 ?  18  ILE   A CA   1 
ATOM   476  C CA   B ILE   A 1 18  ? 11.830 -9.945  8.923   0.60 12.92 ?  18  ILE   A CA   1 
ATOM   477  C C    A ILE   A 1 18  ? 10.668 -8.941  9.691   0.40 12.46 ?  18  ILE   A C    1 
ATOM   478  C C    B ILE   A 1 18  ? 10.849 -9.150  9.781   0.60 13.22 ?  18  ILE   A C    1 
ATOM   479  O O    A ILE   A 1 18  ? 9.873  -9.437  10.498  0.40 12.71 ?  18  ILE   A O    1 
ATOM   480  O O    B ILE   A 1 18  ? 9.988  -9.723  10.458  0.60 13.94 ?  18  ILE   A O    1 
ATOM   481  C CB   A ILE   A 1 18  ? 10.953 -10.144 7.481   0.40 12.21 ?  18  ILE   A CB   1 
ATOM   482  C CB   B ILE   A 1 18  ? 11.286 -10.289 7.516   0.60 13.11 ?  18  ILE   A CB   1 
ATOM   483  C CG1  A ILE   A 1 18  ? 10.905 -8.914  6.569   0.40 13.23 ?  18  ILE   A CG1  1 
ATOM   484  C CG1  B ILE   A 1 18  ? 11.169 -9.037  6.650   0.60 13.96 ?  18  ILE   A CG1  1 
ATOM   485  C CG2  A ILE   A 1 18  ? 9.570  -10.741 7.674   0.40 12.54 ?  18  ILE   A CG2  1 
ATOM   486  C CG2  B ILE   A 1 18  ? 9.952  -11.054 7.607   0.60 12.75 ?  18  ILE   A CG2  1 
ATOM   487  C CD1  A ILE   A 1 18  ? 10.557 -9.250  5.131   0.40 14.84 ?  18  ILE   A CD1  1 
ATOM   488  C CD1  B ILE   A 1 18  ? 10.925 -9.353  5.200   0.60 15.10 ?  18  ILE   A CD1  1 
ATOM   489  H H    A ILE   A 1 18  ? 11.314 -11.390 9.993   0.40 13.34 ?  18  ILE   A H    1 
ATOM   490  H H    B ILE   A 1 18  ? 11.636 -11.483 10.162  0.60 14.52 ?  18  ILE   A H    1 
ATOM   491  H HA   A ILE   A 1 18  ? 12.384 -9.283  8.677   0.40 14.14 ?  18  ILE   A HA   1 
ATOM   492  H HA   B ILE   A 1 18  ? 12.629 -9.397  8.796   0.60 15.48 ?  18  ILE   A HA   1 
ATOM   493  H HB   A ILE   A 1 18  ? 11.507 -10.811 7.055   0.40 14.63 ?  18  ILE   A HB   1 
ATOM   494  H HB   B ILE   A 1 18  ? 11.932 -10.877 7.090   0.60 15.71 ?  18  ILE   A HB   1 
ATOM   495  H HG12 A ILE   A 1 18  ? 10.235 -8.297  6.898   0.40 15.86 ?  18  ILE   A HG12 1 
ATOM   496  H HG12 B ILE   A 1 18  ? 10.431 -8.502  6.972   0.60 16.73 ?  18  ILE   A HG12 1 
ATOM   497  H HG13 A ILE   A 1 18  ? 11.776 -8.487  6.569   0.40 15.86 ?  18  ILE   A HG13 1 
ATOM   498  H HG13 B ILE   A 1 18  ? 11.997 -8.536  6.709   0.60 16.73 ?  18  ILE   A HG13 1 
ATOM   499  H HG21 A ILE   A 1 18  ? 9.180  -10.913 6.804   0.40 15.02 ?  18  ILE   A HG21 1 
ATOM   500  H HG21 B ILE   A 1 18  ? 9.715  -11.380 6.722   0.60 15.28 ?  18  ILE   A HG21 1 
ATOM   501  H HG22 A ILE   A 1 18  ? 9.657  -11.565 8.168   0.40 15.02 ?  18  ILE   A HG22 1 
ATOM   502  H HG22 B ILE   A 1 18  ? 10.059 -11.805 8.213   0.60 15.28 ?  18  ILE   A HG22 1 
ATOM   503  H HG23 A ILE   A 1 18  ? 9.007  -10.124 8.166   0.40 15.02 ?  18  ILE   A HG23 1 
ATOM   504  H HG23 B ILE   A 1 18  ? 9.265  -10.458 7.935   0.60 15.28 ?  18  ILE   A HG23 1 
ATOM   505  H HD11 A ILE   A 1 18  ? 10.711 -8.470  4.576   0.40 17.78 ?  18  ILE   A HD11 1 
ATOM   506  H HD11 B ILE   A 1 18  ? 10.939 -8.527  4.691   0.60 18.09 ?  18  ILE   A HD11 1 
ATOM   507  H HD12 A ILE   A 1 18  ? 11.122 -9.982  4.833   0.40 17.78 ?  18  ILE   A HD12 1 
ATOM   508  H HD12 B ILE   A 1 18  ? 11.615 -9.952  4.882   0.60 18.09 ?  18  ILE   A HD12 1 
ATOM   509  H HD13 A ILE   A 1 18  ? 9.625  -9.513  5.083   0.40 17.78 ?  18  ILE   A HD13 1 
ATOM   510  H HD13 B ILE   A 1 18  ? 10.053 -9.777  5.112   0.60 18.09 ?  18  ILE   A HD13 1 
ATOM   511  N N    A LYS   A 1 19  ? 10.762 -7.631  9.470   0.40 12.67 ?  19  LYS   A N    1 
ATOM   512  N N    B LYS   A 1 19  ? 10.980 -7.818  9.742   0.60 13.63 ?  19  LYS   A N    1 
ATOM   513  C CA   A LYS   A 1 19  ? 9.963  -6.668  10.208  0.40 12.90 ?  19  LYS   A CA   1 
ATOM   514  C CA   B LYS   A 1 19  ? 10.166 -6.919  10.556  0.60 14.99 ?  19  LYS   A CA   1 
ATOM   515  C C    A LYS   A 1 19  ? 9.738  -5.448  9.330   0.40 12.62 ?  19  LYS   A C    1 
ATOM   516  C C    B LYS   A 1 19  ? 9.927  -5.616  9.803   0.60 15.11 ?  19  LYS   A C    1 
ATOM   517  O O    A LYS   A 1 19  ? 10.605 -5.070  8.538   0.40 12.28 ?  19  LYS   A O    1 
ATOM   518  O O    B LYS   A 1 19  ? 10.800 -5.154  9.067   0.60 14.83 ?  19  LYS   A O    1 
ATOM   519  C CB   A LYS   A 1 19  ? 10.705 -6.261  11.485  0.40 13.58 ?  19  LYS   A CB   1 
ATOM   520  C CB   B LYS   A 1 19  ? 10.861 -6.631  11.897  0.60 15.85 ?  19  LYS   A CB   1 
ATOM   521  C CG   A LYS   A 1 19  ? 9.947  -5.391  12.467  0.40 15.05 ?  19  LYS   A CG   1 
ATOM   522  C CG   B LYS   A 1 19  ? 10.147 -5.663  12.839  0.60 17.39 ?  19  LYS   A CG   1 
ATOM   523  C CD   A LYS   A 1 19  ? 10.851 -5.107  13.661  0.40 16.30 ?  19  LYS   A CD   1 
ATOM   524  C CD   B LYS   A 1 19  ? 11.035 -5.367  14.046  0.60 18.74 ?  19  LYS   A CD   1 
ATOM   525  C CE   A LYS   A 1 19  ? 10.199 -4.210  14.696  0.40 17.36 ?  19  LYS   A CE   1 
ATOM   526  C CE   B LYS   A 1 19  ? 10.411 -4.364  15.005  0.60 19.71 ?  19  LYS   A CE   1 
ATOM   527  N NZ   A LYS   A 1 19  ? 11.100 -3.988  15.865  0.40 17.82 ?  19  LYS   A NZ   1 
ATOM   528  N NZ   B LYS   A 1 19  ? 11.325 -4.086  16.151  0.60 20.17 ?  19  LYS   A NZ   1 
ATOM   529  H H    A LYS   A 1 19  ? 11.294 -7.265  8.894   0.40 15.18 ?  19  LYS   A H    1 
ATOM   530  H H    B LYS   A 1 19  ? 11.548 -7.401  9.237   0.60 16.33 ?  19  LYS   A H    1 
ATOM   531  H HA   A LYS   A 1 19  ? 9.106  -7.060  10.446  0.40 15.46 ?  19  LYS   A HA   1 
ATOM   532  H HA   B LYS   A 1 19  ? 9.308  -7.320  10.728  0.60 17.96 ?  19  LYS   A HA   1 
ATOM   533  H HB2  A LYS   A 1 19  ? 10.957 -7.065  11.957  0.40 16.27 ?  19  LYS   A HB2  1 
ATOM   534  H HB2  B LYS   A 1 19  ? 10.949 -7.472  12.371  0.60 19.00 ?  19  LYS   A HB2  1 
ATOM   535  H HB3  A LYS   A 1 19  ? 11.503 -5.772  11.227  0.40 16.27 ?  19  LYS   A HB3  1 
ATOM   536  H HB3  B LYS   A 1 19  ? 11.740 -6.266  11.719  0.60 19.00 ?  19  LYS   A HB3  1 
ATOM   537  H HG2  A LYS   A 1 19  ? 9.709  -4.549  12.048  0.40 18.04 ?  19  LYS   A HG2  1 
ATOM   538  H HG2  B LYS   A 1 19  ? 9.970  -4.826  12.381  0.60 20.84 ?  19  LYS   A HG2  1 
ATOM   539  H HG3  A LYS   A 1 19  ? 9.156  -5.858  12.777  0.40 18.04 ?  19  LYS   A HG3  1 
ATOM   540  H HG3  B LYS   A 1 19  ? 9.321  -6.060  13.154  0.60 20.84 ?  19  LYS   A HG3  1 
ATOM   541  H HD2  A LYS   A 1 19  ? 11.075 -5.949  14.092  0.40 19.53 ?  19  LYS   A HD2  1 
ATOM   542  H HD2  B LYS   A 1 19  ? 11.189 -6.190  14.536  0.60 22.46 ?  19  LYS   A HD2  1 
ATOM   543  H HD3  A LYS   A 1 19  ? 11.658 -4.671  13.349  0.40 19.53 ?  19  LYS   A HD3  1 
ATOM   544  H HD3  B LYS   A 1 19  ? 11.879 -5.001  13.739  0.60 22.46 ?  19  LYS   A HD3  1 
ATOM   545  H HE2  A LYS   A 1 19  ? 10.003 -3.349  14.296  0.40 20.81 ?  19  LYS   A HE2  1 
ATOM   546  H HE2  B LYS   A 1 19  ? 10.244 -3.529  14.537  0.60 23.62 ?  19  LYS   A HE2  1 
ATOM   547  H HE3  A LYS   A 1 19  ? 9.384  -4.627  15.016  0.40 20.81 ?  19  LYS   A HE3  1 
ATOM   548  H HE3  B LYS   A 1 19  ? 9.581  -4.724  15.356  0.60 23.62 ?  19  LYS   A HE3  1 
ATOM   549  H HZ1  A LYS   A 1 19  ? 10.697 -3.474  16.469  0.40 21.36 ?  19  LYS   A HZ1  1 
ATOM   550  H HZ1  B LYS   A 1 19  ? 10.934 -3.529  16.725  0.60 24.18 ?  19  LYS   A HZ1  1 
ATOM   551  H HZ2  A LYS   A 1 19  ? 11.309 -4.767  16.242  0.40 21.36 ?  19  LYS   A HZ2  1 
ATOM   552  H HZ2  B LYS   A 1 19  ? 11.523 -4.844  16.572  0.60 24.18 ?  19  LYS   A HZ2  1 
ATOM   553  H HZ3  A LYS   A 1 19  ? 11.851 -3.587  15.601  0.40 21.36 ?  19  LYS   A HZ3  1 
ATOM   554  H HZ3  B LYS   A 1 19  ? 12.077 -3.714  15.856  0.60 24.18 ?  19  LYS   A HZ3  1 
ATOM   555  N N    A ASN   A 1 20  ? 8.560  -4.840  9.465   0.40 13.06 ?  20  ASN   A N    1 
ATOM   556  N N    B ASN   A 1 20  ? 8.741  -5.035  9.985   0.60 16.10 ?  20  ASN   A N    1 
ATOM   557  C CA   A ASN   A 1 20  ? 8.304  -3.534  8.866   0.40 13.95 ?  20  ASN   A CA   1 
ATOM   558  C CA   B ASN   A 1 20  ? 8.433  -3.703  9.467   0.60 16.91 ?  20  ASN   A CA   1 
ATOM   559  C C    A ASN   A 1 20  ? 8.890  -2.496  9.811   0.40 14.24 ?  20  ASN   A C    1 
ATOM   560  C C    B ASN   A 1 20  ? 9.040  -2.706  10.448  0.60 16.58 ?  20  ASN   A C    1 
ATOM   561  O O    A ASN   A 1 20  ? 8.318  -2.205  10.864  0.40 15.03 ?  20  ASN   A O    1 
ATOM   562  O O    B ASN   A 1 20  ? 8.521  -2.508  11.546  0.60 16.90 ?  20  ASN   A O    1 
ATOM   563  C CB   A ASN   A 1 20  ? 6.809  -3.313  8.664   0.40 14.83 ?  20  ASN   A CB   1 
ATOM   564  C CB   B ASN   A 1 20  ? 6.920  -3.544  9.336   0.60 18.55 ?  20  ASN   A CB   1 
ATOM   565  C CG   A ASN   A 1 20  ? 6.475  -1.874  8.293   0.40 15.93 ?  20  ASN   A CG   1 
ATOM   566  C CG   B ASN   A 1 20  ? 6.493  -2.152  8.914   0.60 20.28 ?  20  ASN   A CG   1 
ATOM   567  O OD1  A ASN   A 1 20  ? 5.570  -1.264  8.864   0.40 17.29 ?  20  ASN   A OD1  1 
ATOM   568  O OD1  B ASN   A 1 20  ? 5.436  -1.673  9.331   0.60 21.86 ?  20  ASN   A OD1  1 
ATOM   569  N ND2  A ASN   A 1 20  ? 7.211  -1.325  7.340   0.40 16.19 ?  20  ASN   A ND2  1 
ATOM   570  N ND2  B ASN   A 1 20  ? 7.298  -1.499  8.079   0.60 20.33 ?  20  ASN   A ND2  1 
ATOM   571  H H    A ASN   A 1 20  ? 7.895  -5.165  9.902   0.40 15.65 ?  20  ASN   A H    1 
ATOM   572  H H    B ASN   A 1 20  ? 8.090  -5.394  10.407  0.60 19.29 ?  20  ASN   A H    1 
ATOM   573  H HA   A ASN   A 1 20  ? 8.753  -3.473  8.009   0.40 16.72 ?  20  ASN   A HA   1 
ATOM   574  H HA   B ASN   A 1 20  ? 8.842  -3.581  8.596   0.60 20.27 ?  20  ASN   A HA   1 
ATOM   575  H HB2  A ASN   A 1 20  ? 6.502  -3.887  7.947   0.40 17.77 ?  20  ASN   A HB2  1 
ATOM   576  H HB2  B ASN   A 1 20  ? 6.596  -4.166  8.670   0.60 22.23 ?  20  ASN   A HB2  1 
ATOM   577  H HB3  A ASN   A 1 20  ? 6.348  -3.533  9.489   0.40 17.77 ?  20  ASN   A HB3  1 
ATOM   578  H HB3  B ASN   A 1 20  ? 6.509  -3.727  10.189  0.60 22.23 ?  20  ASN   A HB3  1 
ATOM   579  H HD21 A ASN   A 1 20  ? 7.061  -0.513  7.105   0.40 19.40 ?  20  ASN   A HD21 1 
ATOM   580  H HD21 B ASN   A 1 20  ? 7.092  -0.709  7.812   0.60 24.37 ?  20  ASN   A HD21 1 
ATOM   581  H HD22 A ASN   A 1 20  ? 7.835  -1.778  6.962   0.40 19.40 ?  20  ASN   A HD22 1 
ATOM   582  H HD22 B ASN   A 1 20  ? 8.029  -1.864  7.804   0.60 24.37 ?  20  ASN   A HD22 1 
ATOM   583  N N    A ALA   A 1 21  ? 10.048 -1.948  9.454   0.40 13.91 ?  21  ALA   A N    1 
ATOM   584  N N    B ALA   A 1 21  ? 10.180 -2.118  10.085  0.60 16.76 ?  21  ALA   A N    1 
ATOM   585  C CA   A ALA   A 1 21  ? 10.728 -1.028  10.352  0.40 13.47 ?  21  ALA   A CA   1 
ATOM   586  C CA   B ALA   A 1 21  ? 10.876 -1.232  11.009  0.60 17.33 ?  21  ALA   A CA   1 
ATOM   587  C C    A ALA   A 1 21  ? 11.706 -0.170  9.569   0.40 12.94 ?  21  ALA   A C    1 
ATOM   588  C C    B ALA   A 1 21  ? 11.848 -0.347  10.248  0.60 17.43 ?  21  ALA   A C    1 
ATOM   589  O O    A ALA   A 1 21  ? 12.156 -0.540  8.480   0.40 13.30 ?  21  ALA   A O    1 
ATOM   590  O O    B ALA   A 1 21  ? 12.291 -0.678  9.145   0.60 17.36 ?  21  ALA   A O    1 
ATOM   591  C CB   A ALA   A 1 21  ? 11.459 -1.779  11.467  0.40 13.93 ?  21  ALA   A CB   1 
ATOM   592  C CB   B ALA   A 1 21  ? 11.612 -2.024  12.097  0.60 18.26 ?  21  ALA   A CB   1 
ATOM   593  H H    A ALA   A 1 21  ? 10.454 -2.096  8.710   0.40 16.66 ?  21  ALA   A H    1 
ATOM   594  H H    B ALA   A 1 21  ? 10.576 -2.219  9.325   0.60 20.09 ?  21  ALA   A H    1 
ATOM   595  H HA   A ALA   A 1 21  ? 10.069 -0.445  10.760  0.40 16.13 ?  21  ALA   A HA   1 
ATOM   596  H HA   B ALA   A 1 21  ? 10.235 -0.653  11.442  0.60 20.77 ?  21  ALA   A HA   1 
ATOM   597  H HB1  A ALA   A 1 21  ? 11.874 -1.135  12.058  0.40 16.69 ?  21  ALA   A HB1  1 
ATOM   598  H HB1  B ALA   A 1 21  ? 12.046 -1.404  12.704  0.60 21.89 ?  21  ALA   A HB1  1 
ATOM   599  H HB2  A ALA   A 1 21  ? 10.813 -2.313  11.960  0.40 16.69 ?  21  ALA   A HB2  1 
ATOM   600  H HB2  B ALA   A 1 21  ? 10.963 -2.560  12.583  0.60 21.89 ?  21  ALA   A HB2  1 
ATOM   601  H HB3  A ALA   A 1 21  ? 12.130 -2.355  11.073  0.40 16.69 ?  21  ALA   A HB3  1 
ATOM   602  H HB3  B ALA   A 1 21  ? 12.271 -2.601  11.683  0.60 21.89 ?  21  ALA   A HB3  1 
ATOM   603  N N    A ASP   A 1 22  ? 12.007 0.993   10.146  0.40 13.31 ?  22  ASP   A N    1 
ATOM   604  N N    B ASP   A 1 22  ? 12.165 0.790   10.869  0.60 17.76 ?  22  ASP   A N    1 
ATOM   605  C CA   A ASP   A 1 22  ? 13.055 1.879   9.660   0.40 13.66 ?  22  ASP   A CA   1 
ATOM   606  C CA   B ASP   A 1 22  ? 13.187 1.706   10.385  0.60 18.31 ?  22  ASP   A CA   1 
ATOM   607  C C    A ASP   A 1 22  ? 14.386 1.390   10.223  0.40 12.92 ?  22  ASP   A C    1 
ATOM   608  C C    B ASP   A 1 22  ? 14.547 1.153   10.791  0.60 17.49 ?  22  ASP   A C    1 
ATOM   609  O O    A ASP   A 1 22  ? 14.575 1.366   11.444  0.40 13.07 ?  22  ASP   A O    1 
ATOM   610  O O    B ASP   A 1 22  ? 14.835 1.028   11.986  0.60 17.75 ?  22  ASP   A O    1 
ATOM   611  C CB   A ASP   A 1 22  ? 12.750 3.298   10.142  0.40 15.37 ?  22  ASP   A CB   1 
ATOM   612  C CB   B ASP   A 1 22  ? 12.944 3.071   11.027  0.60 19.53 ?  22  ASP   A CB   1 
ATOM   613  C CG   A ASP   A 1 22  ? 13.808 4.308   9.718   0.40 17.00 ?  22  ASP   A CG   1 
ATOM   614  C CG   B ASP   A 1 22  ? 13.714 4.188   10.359  0.60 20.71 ?  22  ASP   A CG   1 
ATOM   615  O OD1  A ASP   A 1 22  ? 14.766 3.921   9.019   0.40 17.73 ?  22  ASP   A OD1  1 
ATOM   616  O OD1  B ASP   A 1 22  ? 14.913 4.005   10.077  0.60 20.13 ?  22  ASP   A OD1  1 
ATOM   617  O OD2  A ASP   A 1 22  ? 13.683 5.495   10.095  0.40 18.13 -1 22  ASP   A OD2  1 
ATOM   618  O OD2  B ASP   A 1 22  ? 13.113 5.261   10.128  0.60 22.09 -1 22  ASP   A OD2  1 
ATOM   619  H H    A ASP   A 1 22  ? 11.596 1.297   10.839  0.40 15.94 ?  22  ASP   A H    1 
ATOM   620  H H    B ASP   A 1 22  ? 11.790 1.059   11.595  0.60 21.29 ?  22  ASP   A H    1 
ATOM   621  H HA   A ASP   A 1 22  ? 13.085 1.868   8.689   0.40 16.37 ?  22  ASP   A HA   1 
ATOM   622  H HA   B ASP   A 1 22  ? 13.147 1.791   9.422   0.60 21.94 ?  22  ASP   A HA   1 
ATOM   623  H HB2  A ASP   A 1 22  ? 11.883 3.576   9.789   0.40 18.42 ?  22  ASP   A HB2  1 
ATOM   624  H HB2  B ASP   A 1 22  ? 12.002 3.285   10.967  0.60 23.42 ?  22  ASP   A HB2  1 
ATOM   625  H HB3  A ASP   A 1 22  ? 12.716 3.302   11.113  0.40 18.42 ?  22  ASP   A HB3  1 
ATOM   626  H HB3  B ASP   A 1 22  ? 13.215 3.039   11.957  0.60 23.42 ?  22  ASP   A HB3  1 
ATOM   627  N N    A ILE   A 1 23  ? 15.304 0.989   9.338   0.40 13.19 ?  23  ILE   A N    1 
ATOM   628  N N    B ILE   A 1 23  ? 15.378 0.809   9.802   0.60 17.20 ?  23  ILE   A N    1 
ATOM   629  C CA   A ILE   A 1 23  ? 16.566 0.407   9.791   0.40 13.26 ?  23  ILE   A CA   1 
ATOM   630  C CA   B ILE   A 1 23  ? 16.652 0.157   10.093  0.60 16.60 ?  23  ILE   A CA   1 
ATOM   631  C C    A ILE   A 1 23  ? 17.346 1.380   10.662  0.40 13.53 ?  23  ILE   A C    1 
ATOM   632  C C    B ILE   A 1 23  ? 17.531 1.045   10.958  0.60 16.58 ?  23  ILE   A C    1 
ATOM   633  O O    A ILE   A 1 23  ? 18.086 0.960   11.559  0.40 13.76 ?  23  ILE   A O    1 
ATOM   634  O O    B ILE   A 1 23  ? 18.285 0.553   11.806  0.60 16.38 ?  23  ILE   A O    1 
ATOM   635  C CB   A ILE   A 1 23  ? 17.405 -0.112  8.604   0.40 13.26 ?  23  ILE   A CB   1 
ATOM   636  C CB   B ILE   A 1 23  ? 17.346 -0.291  8.786   0.60 16.37 ?  23  ILE   A CB   1 
ATOM   637  C CG1  A ILE   A 1 23  ? 18.552 -0.989  9.114   0.40 13.39 ?  23  ILE   A CG1  1 
ATOM   638  C CG1  B ILE   A 1 23  ? 18.557 -1.180  9.092   0.60 15.97 ?  23  ILE   A CG1  1 
ATOM   639  C CG2  A ILE   A 1 23  ? 17.941 1.044   7.771   0.40 13.62 ?  23  ILE   A CG2  1 
ATOM   640  C CG2  B ILE   A 1 23  ? 17.726 0.911   7.921   0.60 16.77 ?  23  ILE   A CG2  1 
ATOM   641  C CD1  A ILE   A 1 23  ? 19.401 -1.600  8.014   0.40 13.06 ?  23  ILE   A CD1  1 
ATOM   642  C CD1  B ILE   A 1 23  ? 19.118 -1.887  7.873   0.60 15.48 ?  23  ILE   A CD1  1 
ATOM   643  H H    A ILE   A 1 23  ? 15.207 1.038   8.491   0.40 15.80 ?  23  ILE   A H    1 
ATOM   644  H H    B ILE   A 1 23  ? 15.229 0.947   8.971   0.60 20.61 ?  23  ILE   A H    1 
ATOM   645  H HA   A ILE   A 1 23  ? 16.356 -0.354  10.349  0.40 15.89 ?  23  ILE   A HA   1 
ATOM   646  H HA   B ILE   A 1 23  ? 16.477 -0.639  10.609  0.60 19.90 ?  23  ILE   A HA   1 
ATOM   647  H HB   A ILE   A 1 23  ? 16.828 -0.653  8.045   0.40 15.89 ?  23  ILE   A HB   1 
ATOM   648  H HB   B ILE   A 1 23  ? 16.712 -0.824  8.287   0.60 19.62 ?  23  ILE   A HB   1 
ATOM   649  H HG12 A ILE   A 1 23  ? 19.132 -0.449  9.673   0.40 16.04 ?  23  ILE   A HG12 1 
ATOM   650  H HG12 B ILE   A 1 23  ? 19.265 -0.633  9.466   0.60 19.14 ?  23  ILE   A HG12 1 
ATOM   651  H HG13 A ILE   A 1 23  ? 18.177 -1.715  9.638   0.40 16.04 ?  23  ILE   A HG13 1 
ATOM   652  H HG13 B ILE   A 1 23  ? 18.293 -1.859  9.732   0.60 19.14 ?  23  ILE   A HG13 1 
ATOM   653  H HG21 A ILE   A 1 23  ? 18.281 0.694   6.933   0.40 16.32 ?  23  ILE   A HG21 1 
ATOM   654  H HG21 B ILE   A 1 23  ? 18.052 0.592   7.062   0.60 20.10 ?  23  ILE   A HG21 1 
ATOM   655  H HG22 A ILE   A 1 23  ? 17.218 1.668   7.598   0.40 16.32 ?  23  ILE   A HG22 1 
ATOM   656  H HG22 B ILE   A 1 23  ? 16.939 1.463   7.784   0.60 20.10 ?  23  ILE   A HG22 1 
ATOM   657  H HG23 A ILE   A 1 23  ? 18.650 1.486   8.261   0.40 16.32 ?  23  ILE   A HG23 1 
ATOM   658  H HG23 B ILE   A 1 23  ? 18.416 1.423   8.366   0.60 20.10 ?  23  ILE   A HG23 1 
ATOM   659  H HD11 A ILE   A 1 23  ? 20.026 -2.224  8.412   0.40 15.65 ?  23  ILE   A HD11 1 
ATOM   660  H HD11 B ILE   A 1 23  ? 19.834 -2.477  8.151   0.60 18.54 ?  23  ILE   A HD11 1 
ATOM   661  H HD12 A ILE   A 1 23  ? 18.821 -2.061  7.389   0.40 15.65 ?  23  ILE   A HD12 1 
ATOM   662  H HD12 B ILE   A 1 23  ? 18.408 -2.401  7.454   0.60 18.54 ?  23  ILE   A HD12 1 
ATOM   663  H HD13 A ILE   A 1 23  ? 19.883 -0.891  7.559   0.40 15.65 ?  23  ILE   A HD13 1 
ATOM   664  H HD13 B ILE   A 1 23  ? 19.455 -1.224  7.250   0.60 18.54 ?  23  ILE   A HD13 1 
ATOM   665  N N    A VAL   A 1 24  ? 17.197 2.687   10.426  0.40 13.83 ?  24  VAL   A N    1 
ATOM   666  N N    B VAL   A 1 24  ? 17.430 2.362   10.784  0.60 17.54 ?  24  VAL   A N    1 
ATOM   667  C CA   A VAL   A 1 24  ? 17.879 3.667   11.268  0.40 14.56 ?  24  VAL   A CA   1 
ATOM   668  C CA   B VAL   A 1 24  ? 18.179 3.282   11.631  0.60 18.97 ?  24  VAL   A CA   1 
ATOM   669  C C    A VAL   A 1 24  ? 17.375 3.570   12.699  0.40 14.96 ?  24  VAL   A C    1 
ATOM   670  C C    B VAL   A 1 24  ? 17.680 3.201   13.068  0.60 19.52 ?  24  VAL   A C    1 
ATOM   671  O O    A VAL   A 1 24  ? 18.158 3.462   13.648  0.40 15.06 ?  24  VAL   A O    1 
ATOM   672  O O    B VAL   A 1 24  ? 18.471 3.199   14.019  0.60 19.87 ?  24  VAL   A O    1 
ATOM   673  C CB   A VAL   A 1 24  ? 17.714 5.088   10.700  0.40 15.17 ?  24  VAL   A CB   1 
ATOM   674  C CB   B VAL   A 1 24  ? 18.081 4.703   11.053  0.60 20.11 ?  24  VAL   A CB   1 
ATOM   675  C CG1  A VAL   A 1 24  ? 18.215 6.125   11.705  0.40 15.10 ?  24  VAL   A CG1  1 
ATOM   676  C CG1  B VAL   A 1 24  ? 18.883 5.665   11.892  0.60 20.96 ?  24  VAL   A CG1  1 
ATOM   677  C CG2  A VAL   A 1 24  ? 18.466 5.227   9.385   0.40 15.88 ?  24  VAL   A CG2  1 
ATOM   678  C CG2  B VAL   A 1 24  ? 18.560 4.705   9.602   0.60 20.78 ?  24  VAL   A CG2  1 
ATOM   679  H H    A VAL   A 1 24  ? 16.714 3.033   9.803   0.40 16.57 ?  24  VAL   A H    1 
ATOM   680  H H    B VAL   A 1 24  ? 16.938 2.745   10.196  0.60 21.02 ?  24  VAL   A H    1 
ATOM   681  H HA   A VAL   A 1 24  ? 18.827 3.471   11.280  0.40 17.45 ?  24  VAL   A HA   1 
ATOM   682  H HA   B VAL   A 1 24  ? 19.118 3.032   11.624  0.60 22.74 ?  24  VAL   A HA   1 
ATOM   683  H HB   A VAL   A 1 24  ? 16.775 5.267   10.531  0.40 18.17 ?  24  VAL   A HB   1 
ATOM   684  H HB   B VAL   A 1 24  ? 17.156 4.993   11.061  0.60 24.11 ?  24  VAL   A HB   1 
ATOM   685  H HG11 A VAL   A 1 24  ? 18.379 6.963   11.241  0.40 18.10 ?  24  VAL   A HG11 1 
ATOM   686  H HG11 B VAL   A 1 24  ? 18.905 6.523   11.446  0.60 25.13 ?  24  VAL   A HG11 1 
ATOM   687  H HG12 A VAL   A 1 24  ? 17.541 6.258   12.390  0.40 18.10 ?  24  VAL   A HG12 1 
ATOM   688  H HG12 B VAL   A 1 24  ? 18.460 5.752   12.758  0.60 25.13 ?  24  VAL   A HG12 1 
ATOM   689  H HG13 A VAL   A 1 24  ? 19.038 5.805   12.104  0.40 18.10 ?  24  VAL   A HG13 1 
ATOM   690  H HG13 B VAL   A 1 24  ? 19.783 5.317   11.992  0.60 25.13 ?  24  VAL   A HG13 1 
ATOM   691  H HG21 A VAL   A 1 24  ? 18.200 6.052   8.952   0.40 19.03 ?  24  VAL   A HG21 1 
ATOM   692  H HG21 B VAL   A 1 24  ? 18.677 5.620   9.304   0.60 24.92 ?  24  VAL   A HG21 1 
ATOM   693  H HG22 A VAL   A 1 24  ? 19.420 5.245   9.569   0.40 19.03 ?  24  VAL   A HG22 1 
ATOM   694  H HG22 B VAL   A 1 24  ? 19.405 4.230   9.549   0.60 24.92 ?  24  VAL   A HG22 1 
ATOM   695  H HG23 A VAL   A 1 24  ? 18.251 4.470   8.819   0.40 19.03 ?  24  VAL   A HG23 1 
ATOM   696  H HG23 B VAL   A 1 24  ? 17.899 4.259   9.048   0.60 24.92 ?  24  VAL   A HG23 1 
ATOM   697  N N    A GLU   A 1 25  ? 16.054 3.594   12.875  0.40 15.65 ?  25  GLU   A N    1 
ATOM   698  N N    B GLU   A 1 25  ? 16.361 3.099   13.246  0.60 20.31 ?  25  GLU   A N    1 
ATOM   699  C CA   A GLU   A 1 25  ? 15.497 3.529   14.222  0.40 16.87 ?  25  GLU   A CA   1 
ATOM   700  C CA   B GLU   A 1 25  ? 15.789 2.984   14.584  0.60 21.71 ?  25  GLU   A CA   1 
ATOM   701  C C    A GLU   A 1 25  ? 15.749 2.167   14.855  0.40 16.12 ?  25  GLU   A C    1 
ATOM   702  C C    B GLU   A 1 25  ? 16.072 1.617   15.195  0.60 20.77 ?  25  GLU   A C    1 
ATOM   703  O O    A GLU   A 1 25  ? 16.021 2.078   16.057  0.40 16.17 ?  25  GLU   A O    1 
ATOM   704  O O    B GLU   A 1 25  ? 16.384 1.520   16.388  0.60 21.16 ?  25  GLU   A O    1 
ATOM   705  C CB   A GLU   A 1 25  ? 14.006 3.870   14.196  0.40 18.82 ?  25  GLU   A CB   1 
ATOM   706  C CB   B GLU   A 1 25  ? 14.287 3.255   14.528  0.60 23.89 ?  25  GLU   A CB   1 
ATOM   707  C CG   A GLU   A 1 25  ? 13.731 5.318   13.820  0.40 20.75 ?  25  GLU   A CG   1 
ATOM   708  C CG   B GLU   A 1 25  ? 13.943 4.673   14.103  0.60 25.97 ?  25  GLU   A CG   1 
ATOM   709  C CD   A GLU   A 1 25  ? 14.528 6.306   14.645  0.40 22.47 ?  25  GLU   A CD   1 
ATOM   710  C CD   B GLU   A 1 25  ? 14.332 5.697   15.152  0.60 27.83 ?  25  GLU   A CD   1 
ATOM   711  O OE1  A GLU   A 1 25  ? 14.625 6.115   15.877  0.40 23.01 ?  25  GLU   A OE1  1 
ATOM   712  O OE1  B GLU   A 1 25  ? 13.896 5.560   16.312  0.60 28.41 ?  25  GLU   A OE1  1 
ATOM   713  O OE2  A GLU   A 1 25  ? 15.073 7.264   14.057  0.40 23.31 -1 25  GLU   A OE2  1 
ATOM   714  O OE2  B GLU   A 1 25  ? 15.098 6.628   14.819  0.60 28.51 -1 25  GLU   A OE2  1 
ATOM   715  H H    A GLU   A 1 25  ? 15.470 3.642   12.244  0.40 18.75 ?  25  GLU   A H    1 
ATOM   716  H H    B GLU   A 1 25  ? 15.789 3.089   12.609  0.60 24.34 ?  25  GLU   A H    1 
ATOM   717  H HA   A GLU   A 1 25  ? 15.943 4.184   14.777  0.40 20.21 ?  25  GLU   A HA   1 
ATOM   718  H HA   B GLU   A 1 25  ? 16.190 3.654   15.155  0.60 26.03 ?  25  GLU   A HA   1 
ATOM   719  H HB2  A GLU   A 1 25  ? 13.558 3.308   13.541  0.40 22.55 ?  25  GLU   A HB2  1 
ATOM   720  H HB2  B GLU   A 1 25  ? 13.877 2.640   13.901  0.60 28.64 ?  25  GLU   A HB2  1 
ATOM   721  H HB3  A GLU   A 1 25  ? 13.623 3.715   15.075  0.40 22.55 ?  25  GLU   A HB3  1 
ATOM   722  H HB3  B GLU   A 1 25  ? 13.914 3.116   15.410  0.60 28.64 ?  25  GLU   A HB3  1 
ATOM   723  H HG2  A GLU   A 1 25  ? 13.968 5.451   12.892  0.40 24.88 ?  25  GLU   A HG2  1 
ATOM   724  H HG2  B GLU   A 1 25  ? 14.445 4.903   13.311  0.60 31.14 ?  25  GLU   A HG2  1 
ATOM   725  H HG3  A GLU   A 1 25  ? 12.793 5.510   13.961  0.40 24.88 ?  25  GLU   A HG3  1 
ATOM   726  H HG3  B GLU   A 1 25  ? 12.987 4.723   13.918  0.60 31.14 ?  25  GLU   A HG3  1 
ATOM   727  N N    A GLU   A 1 26  ? 15.684 1.098   14.058  0.40 15.62 ?  26  GLU   A N    1 
ATOM   728  N N    B GLU   A 1 26  ? 15.966 0.548   14.400  0.60 19.73 ?  26  GLU   A N    1 
ATOM   729  C CA   A GLU   A 1 26  ? 15.987 -0.234  14.576  0.40 15.85 ?  26  GLU   A CA   1 
ATOM   730  C CA   B GLU   A 1 26  ? 16.361 -0.770  14.887  0.60 18.89 ?  26  GLU   A CA   1 
ATOM   731  C C    A GLU   A 1 26  ? 17.415 -0.296  15.104  0.40 15.33 ?  26  GLU   A C    1 
ATOM   732  C C    B GLU   A 1 26  ? 17.802 -0.749  15.376  0.60 18.23 ?  26  GLU   A C    1 
ATOM   733  O O    A GLU   A 1 26  ? 17.666 -0.808  16.201  0.40 15.27 ?  26  GLU   A O    1 
ATOM   734  O O    B GLU   A 1 26  ? 18.107 -1.236  16.470  0.60 18.08 ?  26  GLU   A O    1 
ATOM   735  C CB   A GLU   A 1 26  ? 15.807 -1.274  13.470  0.40 16.69 ?  26  GLU   A CB   1 
ATOM   736  C CB   B GLU   A 1 26  ? 16.201 -1.821  13.784  0.60 19.28 ?  26  GLU   A CB   1 
ATOM   737  C CG   A GLU   A 1 26  ? 14.395 -1.757  13.252  0.40 18.01 ?  26  GLU   A CG   1 
ATOM   738  C CG   B GLU   A 1 26  ? 14.834 -2.450  13.690  0.60 19.01 ?  26  GLU   A CG   1 
ATOM   739  C CD   A GLU   A 1 26  ? 13.910 -2.641  14.370  0.40 18.74 ?  26  GLU   A CD   1 
ATOM   740  C CD   B GLU   A 1 26  ? 14.414 -3.113  14.974  0.60 18.12 ?  26  GLU   A CD   1 
ATOM   741  O OE1  A GLU   A 1 26  ? 14.513 -3.712  14.587  0.40 19.73 ?  26  GLU   A OE1  1 
ATOM   742  O OE1  B GLU   A 1 26  ? 14.746 -4.299  15.219  0.60 16.78 ?  26  GLU   A OE1  1 
ATOM   743  O OE2  A GLU   A 1 26  ? 12.936 -2.251  15.038  0.40 18.88 -1 26  GLU   A OE2  1 
ATOM   744  O OE2  B GLU   A 1 26  ? 13.734 -2.428  15.748  0.60 18.73 -1 26  GLU   A OE2  1 
ATOM   745  H H    A GLU   A 1 26  ? 15.465 1.124   13.227  0.40 18.72 ?  26  GLU   A H    1 
ATOM   746  H H    B GLU   A 1 26  ? 15.677 0.559   13.591  0.60 23.65 ?  26  GLU   A H    1 
ATOM   747  H HA   A GLU   A 1 26  ? 15.374 -0.445  15.300  0.40 19.00 ?  26  GLU   A HA   1 
ATOM   748  H HA   B GLU   A 1 26  ? 15.797 -1.018  15.634  0.60 22.64 ?  26  GLU   A HA   1 
ATOM   749  H HB2  A GLU   A 1 26  ? 16.112 -0.888  12.635  0.40 20.00 ?  26  GLU   A HB2  1 
ATOM   750  H HB2  B GLU   A 1 26  ? 16.385 -1.406  12.929  0.60 23.11 ?  26  GLU   A HB2  1 
ATOM   751  H HB3  A GLU   A 1 26  ? 16.352 -2.045  13.689  0.40 20.00 ?  26  GLU   A HB3  1 
ATOM   752  H HB3  B GLU   A 1 26  ? 16.840 -2.537  13.941  0.60 23.11 ?  26  GLU   A HB3  1 
ATOM   753  H HG2  A GLU   A 1 26  ? 13.804 -0.994  13.202  0.40 21.59 ?  26  GLU   A HG2  1 
ATOM   754  H HG2  B GLU   A 1 26  ? 14.179 -1.765  13.492  0.60 22.78 ?  26  GLU   A HG2  1 
ATOM   755  H HG3  A GLU   A 1 26  ? 14.358 -2.265  12.426  0.40 21.59 ?  26  GLU   A HG3  1 
ATOM   756  H HG3  B GLU   A 1 26  ? 14.833 -3.127  13.001  0.60 22.78 ?  26  GLU   A HG3  1 
ATOM   757  N N    A ALA   A 1 27  ? 18.368 0.222   14.327  0.40 14.86 ?  27  ALA   A N    1 
ATOM   758  N N    B ALA   A 1 27  ? 18.704 -0.179  14.575  0.60 18.03 ?  27  ALA   A N    1 
ATOM   759  C CA   A ALA   A 1 27  ? 19.768 0.142   14.724  0.40 15.40 ?  27  ALA   A CA   1 
ATOM   760  C CA   B ALA   A 1 27  ? 20.106 -0.116  14.973  0.60 18.15 ?  27  ALA   A CA   1 
ATOM   761  C C    A ALA   A 1 27  ? 20.020 0.890   16.028  0.40 17.06 ?  27  ALA   A C    1 
ATOM   762  C C    B ALA   A 1 27  ? 20.273 0.741   16.220  0.60 19.60 ?  27  ALA   A C    1 
ATOM   763  O O    A ALA   A 1 27  ? 20.732 0.393   16.907  0.40 16.70 ?  27  ALA   A O    1 
ATOM   764  O O    B ALA   A 1 27  ? 20.944 0.340   17.178  0.60 20.12 ?  27  ALA   A O    1 
ATOM   765  C CB   A ALA   A 1 27  ? 20.660 0.679   13.604  0.40 15.30 ?  27  ALA   A CB   1 
ATOM   766  C CB   B ALA   A 1 27  ? 20.958 0.429   13.825  0.60 18.01 ?  27  ALA   A CB   1 
ATOM   767  H H    A ALA   A 1 27  ? 18.222 0.618   13.578  0.40 17.81 ?  27  ALA   A H    1 
ATOM   768  H H    B ALA   A 1 27  ? 18.534 0.168   13.810  0.60 21.61 ?  27  ALA   A H    1 
ATOM   769  H HA   A ALA   A 1 27  ? 19.995 -0.786  14.867  0.40 18.45 ?  27  ALA   A HA   1 
ATOM   770  H HA   B ALA   A 1 27  ? 20.420 -1.011  15.180  0.60 21.76 ?  27  ALA   A HA   1 
ATOM   771  H HB1  A ALA   A 1 27  ? 21.584 0.619   13.884  0.40 18.33 ?  27  ALA   A HB1  1 
ATOM   772  H HB1  B ALA   A 1 27  ? 21.889 0.450   14.102  0.60 21.59 ?  27  ALA   A HB1  1 
ATOM   773  H HB2  A ALA   A 1 27  ? 20.519 0.144   12.806  0.40 18.33 ?  27  ALA   A HB2  1 
ATOM   774  H HB2  B ALA   A 1 27  ? 20.860 -0.153  13.055  0.60 21.59 ?  27  ALA   A HB2  1 
ATOM   775  H HB3  A ALA   A 1 27  ? 20.424 1.604   13.426  0.40 18.33 ?  27  ALA   A HB3  1 
ATOM   776  H HB3  B ALA   A 1 27  ? 20.660 1.323   13.605  0.60 21.59 ?  27  ALA   A HB3  1 
ATOM   777  N N    A LYS   A 1 28  ? 19.432 2.081   16.181  0.40 19.69 ?  28  LYS   A N    1 
ATOM   778  N N    B LYS   A 1 28  ? 19.658 1.926   16.229  0.60 21.45 ?  28  LYS   A N    1 
ATOM   779  C CA   A LYS   A 1 28  ? 19.666 2.863   17.392  0.40 23.04 ?  28  LYS   A CA   1 
ATOM   780  C CA   B LYS   A 1 28  ? 19.741 2.786   17.405  0.60 24.17 ?  28  LYS   A CA   1 
ATOM   781  C C    A LYS   A 1 28  ? 19.139 2.158   18.637  0.40 24.41 ?  28  LYS   A C    1 
ATOM   782  C C    B LYS   A 1 28  ? 19.201 2.077   18.640  0.60 24.93 ?  28  LYS   A C    1 
ATOM   783  O O    A LYS   A 1 28  ? 19.664 2.366   19.736  0.40 25.41 ?  28  LYS   A O    1 
ATOM   784  O O    B LYS   A 1 28  ? 19.780 2.183   19.728  0.60 26.08 ?  28  LYS   A O    1 
ATOM   785  C CB   A LYS   A 1 28  ? 19.050 4.258   17.252  0.40 24.85 ?  28  LYS   A CB   1 
ATOM   786  C CB   B LYS   A 1 28  ? 19.007 4.108   17.151  0.60 26.05 ?  28  LYS   A CB   1 
ATOM   787  C CG   A LYS   A 1 28  ? 19.818 5.161   16.299  0.40 26.58 ?  28  LYS   A CG   1 
ATOM   788  C CG   B LYS   A 1 28  ? 19.838 5.131   16.382  0.60 27.89 ?  28  LYS   A CG   1 
ATOM   789  C CD   A LYS   A 1 28  ? 19.310 6.593   16.326  0.40 28.26 ?  28  LYS   A CD   1 
ATOM   790  C CD   B LYS   A 1 28  ? 19.301 6.549   16.541  0.60 29.77 ?  28  LYS   A CD   1 
ATOM   791  C CE   A LYS   A 1 28  ? 17.982 6.731   15.604  0.40 29.46 ?  28  LYS   A CE   1 
ATOM   792  C CE   B LYS   A 1 28  ? 18.007 6.756   15.773  0.60 31.08 ?  28  LYS   A CE   1 
ATOM   793  N NZ   A LYS   A 1 28  ? 17.550 8.154   15.522  0.40 30.13 ?  28  LYS   A NZ   1 
ATOM   794  N NZ   B LYS   A 1 28  ? 17.575 8.184   15.797  0.60 31.82 ?  28  LYS   A NZ   1 
ATOM   795  H H    A LYS   A 1 28  ? 18.902 2.449   15.612  0.40 23.60 ?  28  LYS   A H    1 
ATOM   796  H H    B LYS   A 1 28  ? 19.188 2.243   15.586  0.60 25.71 ?  28  LYS   A H    1 
ATOM   797  H HA   A LYS   A 1 28  ? 20.619 2.976   17.508  0.40 27.62 ?  28  LYS   A HA   1 
ATOM   798  H HA   B LYS   A 1 28  ? 20.670 2.996   17.576  0.60 28.98 ?  28  LYS   A HA   1 
ATOM   799  H HB2  A LYS   A 1 28  ? 18.145 4.173   16.915  0.40 29.79 ?  28  LYS   A HB2  1 
ATOM   800  H HB2  B LYS   A 1 28  ? 18.208 3.931   16.630  0.60 31.23 ?  28  LYS   A HB2  1 
ATOM   801  H HB3  A LYS   A 1 28  ? 19.039 4.688   18.123  0.40 29.79 ?  28  LYS   A HB3  1 
ATOM   802  H HB3  B LYS   A 1 28  ? 18.765 4.506   18.000  0.60 31.23 ?  28  LYS   A HB3  1 
ATOM   803  H HG2  A LYS   A 1 28  ? 20.754 5.168   16.553  0.40 31.87 ?  28  LYS   A HG2  1 
ATOM   804  H HG2  B LYS   A 1 28  ? 20.750 5.118   16.714  0.60 33.45 ?  28  LYS   A HG2  1 
ATOM   805  H HG3  A LYS   A 1 28  ? 19.721 4.823   15.395  0.40 31.87 ?  28  LYS   A HG3  1 
ATOM   806  H HG3  B LYS   A 1 28  ? 19.825 4.910   15.437  0.60 33.45 ?  28  LYS   A HG3  1 
ATOM   807  H HD2  A LYS   A 1 28  ? 19.185 6.872   17.247  0.40 33.89 ?  28  LYS   A HD2  1 
ATOM   808  H HD2  B LYS   A 1 28  ? 19.126 6.721   17.480  0.60 35.70 ?  28  LYS   A HD2  1 
ATOM   809  H HD3  A LYS   A 1 28  ? 19.955 7.170   15.887  0.40 33.89 ?  28  LYS   A HD3  1 
ATOM   810  H HD3  B LYS   A 1 28  ? 19.957 7.179   16.203  0.60 35.70 ?  28  LYS   A HD3  1 
ATOM   811  H HE2  A LYS   A 1 28  ? 18.071 6.388   14.701  0.40 35.33 ?  28  LYS   A HE2  1 
ATOM   812  H HE2  B LYS   A 1 28  ? 18.139 6.496   14.848  0.60 37.28 ?  28  LYS   A HE2  1 
ATOM   813  H HE3  A LYS   A 1 28  ? 17.302 6.235   16.086  0.40 35.33 ?  28  LYS   A HE3  1 
ATOM   814  H HE3  B LYS   A 1 28  ? 17.306 6.221   16.175  0.60 37.28 ?  28  LYS   A HE3  1 
ATOM   815  H HZ1  A LYS   A 1 28  ? 16.772 8.213   15.096  0.40 36.13 ?  28  LYS   A HZ1  1 
ATOM   816  H HZ1  B LYS   A 1 28  ? 16.817 8.281   15.341  0.60 38.16 ?  28  LYS   A HZ1  1 
ATOM   817  H HZ2  A LYS   A 1 28  ? 17.459 8.492   16.340  0.40 36.13 ?  28  LYS   A HZ2  1 
ATOM   818  H HZ2  B LYS   A 1 28  ? 17.443 8.448   16.637  0.60 38.16 ?  28  LYS   A HZ2  1 
ATOM   819  H HZ3  A LYS   A 1 28  ? 18.159 8.631   15.080  0.40 36.13 ?  28  LYS   A HZ3  1 
ATOM   820  H HZ3  B LYS   A 1 28  ? 18.201 8.699   15.428  0.60 38.16 ?  28  LYS   A HZ3  1 
ATOM   821  N N    . LYS   A 1 29  ? 18.112 1.321   18.487  1.00 24.99 ?  29  LYS   A N    1 
ATOM   822  C CA   . LYS   A 1 29  ? 17.534 0.614   19.628  1.00 27.16 ?  29  LYS   A CA   1 
ATOM   823  C C    . LYS   A 1 29  ? 18.370 -0.601  20.015  1.00 25.82 ?  29  LYS   A C    1 
ATOM   824  O O    . LYS   A 1 29  ? 18.680 -0.805  21.195  1.00 26.59 ?  29  LYS   A O    1 
ATOM   825  C CB   . LYS   A 1 29  ? 16.108 0.177   19.288  1.00 30.85 ?  29  LYS   A CB   1 
ATOM   826  C CG   . LYS   A 1 29  ? 15.389 -0.551  20.412  1.00 34.57 ?  29  LYS   A CG   1 
ATOM   827  C CD   . LYS   A 1 29  ? 15.005 0.408   21.523  1.00 37.97 ?  29  LYS   A CD   1 
ATOM   828  C CE   . LYS   A 1 29  ? 14.032 -0.231  22.499  1.00 40.58 ?  29  LYS   A CE   1 
ATOM   829  N NZ   . LYS   A 1 29  ? 13.504 0.763   23.473  1.00 42.16 ?  29  LYS   A NZ   1 
ATOM   830  H H    A LYS   A 1 29  ? 17.726 1.151   17.738  0.40 29.96 ?  29  LYS   A H    1 
ATOM   831  H H    B LYS   A 1 29  ? 17.697 1.197   17.744  0.60 29.96 ?  29  LYS   A H    1 
ATOM   832  H HA   . LYS   A 1 29  ? 17.492 1.210   20.390  1.00 32.56 ?  29  LYS   A HA   1 
ATOM   833  H HB2  . LYS   A 1 29  ? 15.584 0.962   19.067  1.00 36.99 ?  29  LYS   A HB2  1 
ATOM   834  H HB3  . LYS   A 1 29  ? 16.138 -0.422  18.525  1.00 36.99 ?  29  LYS   A HB3  1 
ATOM   835  H HG2  . LYS   A 1 29  ? 14.579 -0.954  20.065  1.00 41.46 ?  29  LYS   A HG2  1 
ATOM   836  H HG3  . LYS   A 1 29  ? 15.966 -1.238  20.787  1.00 41.46 ?  29  LYS   A HG3  1 
ATOM   837  H HD2  . LYS   A 1 29  ? 15.801 0.668   22.013  1.00 45.54 ?  29  LYS   A HD2  1 
ATOM   838  H HD3  . LYS   A 1 29  ? 14.579 1.190   21.137  1.00 45.54 ?  29  LYS   A HD3  1 
ATOM   839  H HE2  . LYS   A 1 29  ? 13.283 -0.602  22.006  1.00 48.67 ?  29  LYS   A HE2  1 
ATOM   840  H HE3  . LYS   A 1 29  ? 14.488 -0.930  22.993  1.00 48.67 ?  29  LYS   A HE3  1 
ATOM   841  H HZ1  . LYS   A 1 29  ? 12.937 0.367   24.034  1.00 50.56 ?  29  LYS   A HZ1  1 
ATOM   842  H HZ2  . LYS   A 1 29  ? 14.174 1.116   23.940  1.00 50.56 ?  29  LYS   A HZ2  1 
ATOM   843  H HZ3  . LYS   A 1 29  ? 13.077 1.414   23.042  1.00 50.56 ?  29  LYS   A HZ3  1 
ATOM   844  N N    . VAL   A 1 30  ? 18.715 -1.436  19.037  1.00 24.12 ?  30  VAL   A N    1 
ATOM   845  C CA   . VAL   A 1 30  ? 19.354 -2.713  19.330  1.00 23.22 ?  30  VAL   A CA   1 
ATOM   846  C C    . VAL   A 1 30  ? 20.863 -2.570  19.501  1.00 21.73 ?  30  VAL   A C    1 
ATOM   847  O O    . VAL   A 1 30  ? 21.475 -3.316  20.274  1.00 21.84 ?  30  VAL   A O    1 
ATOM   848  C CB   . VAL   A 1 30  ? 19.012 -3.712  18.211  1.00 24.22 ?  30  VAL   A CB   1 
ATOM   849  C CG1  . VAL   A 1 30  ? 19.773 -5.016  18.391  1.00 24.83 ?  30  VAL   A CG1  1 
ATOM   850  C CG2  . VAL   A 1 30  ? 17.513 -3.970  18.168  1.00 24.69 ?  30  VAL   A CG2  1 
ATOM   851  H H    . VAL   A 1 30  ? 18.583 -1.291  18.199  1.00 28.92 ?  30  VAL   A H    1 
ATOM   852  H HA   . VAL   A 1 30  ? 18.986 -3.062  20.158  1.00 27.84 ?  30  VAL   A HA   1 
ATOM   853  H HB   . VAL   A 1 30  ? 19.270 -3.336  17.358  1.00 29.03 ?  30  VAL   A HB   1 
ATOM   854  H HG11 . VAL   A 1 30  ? 19.367 -5.698  17.829  1.00 29.78 ?  30  VAL   A HG11 1 
ATOM   855  H HG12 . VAL   A 1 30  ? 20.695 -4.884  18.133  1.00 29.78 ?  30  VAL   A HG12 1 
ATOM   856  H HG13 . VAL   A 1 30  ? 19.719 -5.287  19.321  1.00 29.78 ?  30  VAL   A HG13 1 
ATOM   857  H HG21 . VAL   A 1 30  ? 17.323 -4.636  17.486  1.00 29.61 ?  30  VAL   A HG21 1 
ATOM   858  H HG22 . VAL   A 1 30  ? 17.222 -4.297  19.035  1.00 29.61 ?  30  VAL   A HG22 1 
ATOM   859  H HG23 . VAL   A 1 30  ? 17.055 -3.143  17.956  1.00 29.61 ?  30  VAL   A HG23 1 
ATOM   860  N N    A LYS   A 1 31  ? 21.476 -1.618  18.808  0.40 21.25 ?  31  LYS   A N    1 
ATOM   861  N N    B LYS   A 1 31  ? 21.482 -1.618  18.811  0.60 20.45 ?  31  LYS   A N    1 
ATOM   862  C CA   A LYS   A 1 31  ? 22.928 -1.510  18.720  0.40 21.87 ?  31  LYS   A CA   1 
ATOM   863  C CA   B LYS   A 1 31  ? 22.934 -1.515  18.728  0.60 21.08 ?  31  LYS   A CA   1 
ATOM   864  C C    A LYS   A 1 31  ? 23.535 -2.865  18.346  0.40 19.73 ?  31  LYS   A C    1 
ATOM   865  C C    B LYS   A 1 31  ? 23.537 -2.870  18.347  0.60 19.24 ?  31  LYS   A C    1 
ATOM   866  O O    A LYS   A 1 31  ? 24.336 -3.426  19.102  0.40 20.04 ?  31  LYS   A O    1 
ATOM   867  O O    B LYS   A 1 31  ? 24.337 -3.436  19.100  0.60 19.73 ?  31  LYS   A O    1 
ATOM   868  C CB   A LYS   A 1 31  ? 23.534 -0.972  20.009  0.40 25.35 ?  31  LYS   A CB   1 
ATOM   869  C CB   B LYS   A 1 31  ? 23.544 -0.986  20.018  0.60 25.04 ?  31  LYS   A CB   1 
ATOM   870  C CG   A LYS   A 1 31  ? 22.798 0.238   20.577  0.40 28.82 ?  31  LYS   A CG   1 
ATOM   871  C CG   B LYS   A 1 31  ? 22.897 0.293   20.532  0.60 29.24 ?  31  LYS   A CG   1 
ATOM   872  C CD   A LYS   A 1 31  ? 23.749 1.382   20.901  0.40 31.49 ?  31  LYS   A CD   1 
ATOM   873  C CD   B LYS   A 1 31  ? 23.935 1.367   20.829  0.60 32.51 ?  31  LYS   A CD   1 
ATOM   874  C CE   A LYS   A 1 31  ? 23.094 2.418   21.806  0.40 33.24 ?  31  LYS   A CE   1 
ATOM   875  C CE   B LYS   A 1 31  ? 23.369 2.473   21.711  0.60 34.61 ?  31  LYS   A CE   1 
ATOM   876  N NZ   A LYS   A 1 31  ? 21.885 3.043   21.198  0.40 34.15 ?  31  LYS   A NZ   1 
ATOM   877  N NZ   B LYS   A 1 31  ? 22.141 3.103   21.147  0.60 35.67 ?  31  LYS   A NZ   1 
ATOM   878  H H    A LYS   A 1 31  ? 21.059 -1.005  18.373  0.40 25.48 ?  31  LYS   A H    1 
ATOM   879  H H    B LYS   A 1 31  ? 21.070 -1.003  18.374  0.60 24.52 ?  31  LYS   A H    1 
ATOM   880  H HA   A LYS   A 1 31  ? 23.140 -0.885  18.015  0.40 26.21 ?  31  LYS   A HA   1 
ATOM   881  H HA   B LYS   A 1 31  ? 23.151 -0.888  18.026  0.60 25.27 ?  31  LYS   A HA   1 
ATOM   882  H HB2  A LYS   A 1 31  ? 23.521 -1.670  20.679  0.40 30.39 ?  31  LYS   A HB2  1 
ATOM   883  H HB2  B LYS   A 1 31  ? 23.459 -1.660  20.707  0.60 30.03 ?  31  LYS   A HB2  1 
ATOM   884  H HB3  A LYS   A 1 31  ? 24.450 -0.704  19.829  0.40 30.39 ?  31  LYS   A HB3  1 
ATOM   885  H HB3  B LYS   A 1 31  ? 24.484 -0.796  19.857  0.60 30.03 ?  31  LYS   A HB3  1 
ATOM   886  H HG2  A LYS   A 1 31  ? 22.156 0.558   19.925  0.40 34.56 ?  31  LYS   A HG2  1 
ATOM   887  H HG2  B LYS   A 1 31  ? 22.288 0.638   19.860  0.60 35.06 ?  31  LYS   A HG2  1 
ATOM   888  H HG3  A LYS   A 1 31  ? 22.344 -0.021  21.394  0.40 34.56 ?  31  LYS   A HG3  1 
ATOM   889  H HG3  B LYS   A 1 31  ? 22.416 0.100   21.352  0.60 35.06 ?  31  LYS   A HG3  1 
ATOM   890  H HD2  A LYS   A 1 31  ? 24.529 1.031   21.358  0.40 37.76 ?  31  LYS   A HD2  1 
ATOM   891  H HD2  B LYS   A 1 31  ? 24.687 0.965   21.292  0.60 38.99 ?  31  LYS   A HD2  1 
ATOM   892  H HD3  A LYS   A 1 31  ? 24.013 1.822   20.077  0.40 37.76 ?  31  LYS   A HD3  1 
ATOM   893  H HD3  B LYS   A 1 31  ? 24.230 1.764   19.994  0.60 38.99 ?  31  LYS   A HD3  1 
ATOM   894  H HE2  A LYS   A 1 31  ? 22.823 1.988   22.633  0.40 39.86 ?  31  LYS   A HE2  1 
ATOM   895  H HE2  B LYS   A 1 31  ? 23.140 2.101   22.576  0.60 41.51 ?  31  LYS   A HE2  1 
ATOM   896  H HE3  A LYS   A 1 31  ? 23.733 3.123   21.993  0.40 39.86 ?  31  LYS   A HE3  1 
ATOM   897  H HE3  B LYS   A 1 31  ? 24.039 3.166   21.816  0.60 41.51 ?  31  LYS   A HE3  1 
ATOM   898  H HZ1  A LYS   A 1 31  ? 21.538 3.641   21.760  0.40 40.95 ?  31  LYS   A HZ1  1 
ATOM   899  H HZ1  B LYS   A 1 31  ? 21.854 3.748   21.690  0.60 42.78 ?  31  LYS   A HZ1  1 
ATOM   900  H HZ2  A LYS   A 1 31  ? 22.104 3.454   20.440  0.40 40.95 ?  31  LYS   A HZ2  1 
ATOM   901  H HZ2  B LYS   A 1 31  ? 22.318 3.454   20.350  0.60 42.78 ?  31  LYS   A HZ2  1 
ATOM   902  H HZ3  A LYS   A 1 31  ? 21.274 2.420   21.025  0.40 40.95 ?  31  LYS   A HZ3  1 
ATOM   903  H HZ3  B LYS   A 1 31  ? 21.499 2.493   21.059  0.60 42.78 ?  31  LYS   A HZ3  1 
ATOM   904  N N    . PRO   A 1 32  ? 23.171 -3.412  17.190  1.00 17.12 ?  32  PRO   A N    1 
ATOM   905  C CA   . PRO   A 1 32  ? 23.647 -4.742  16.818  1.00 17.10 ?  32  PRO   A CA   1 
ATOM   906  C C    . PRO   A 1 32  ? 25.146 -4.753  16.587  1.00 16.52 ?  32  PRO   A C    1 
ATOM   907  O O    . PRO   A 1 32  ? 25.784 -3.720  16.373  1.00 16.50 ?  32  PRO   A O    1 
ATOM   908  C CB   . PRO   A 1 32  ? 22.896 -5.019  15.511  1.00 17.61 ?  32  PRO   A CB   1 
ATOM   909  C CG   . PRO   A 1 32  ? 22.714 -3.651  14.911  1.00 16.76 ?  32  PRO   A CG   1 
ATOM   910  C CD   . PRO   A 1 32  ? 22.425 -2.768  16.094  1.00 16.75 ?  32  PRO   A CD   1 
ATOM   911  H HA   . PRO   A 1 32  ? 23.409 -5.397  17.484  1.00 20.50 ?  32  PRO   A HA   1 
ATOM   912  H HB2  . PRO   A 1 32  ? 23.426 -5.586  14.929  1.00 21.11 ?  32  PRO   A HB2  1 
ATOM   913  H HB3  . PRO   A 1 32  ? 22.034 -5.428  15.702  1.00 21.11 ?  32  PRO   A HB3  1 
ATOM   914  H HG2  . PRO   A 1 32  ? 23.530 -3.387  14.460  1.00 20.08 ?  32  PRO   A HG2  1 
ATOM   915  H HG3  . PRO   A 1 32  ? 21.966 -3.667  14.290  1.00 20.08 ?  32  PRO   A HG3  1 
ATOM   916  H HD2  . PRO   A 1 32  ? 22.762 -1.873  15.917  1.00 20.08 ?  32  PRO   A HD2  1 
ATOM   917  H HD3  . PRO   A 1 32  ? 21.479 -2.765  16.281  1.00 20.08 ?  32  PRO   A HD3  1 
ATOM   918  N N    . THR   A 1 33  ? 25.708 -5.959  16.606  1.00 16.60 ?  33  THR   A N    1 
ATOM   919  C CA   . THR   A 1 33  ? 27.116 -6.110  16.266  1.00 16.58 ?  33  THR   A CA   1 
ATOM   920  C C    . THR   A 1 33  ? 27.392 -5.635  14.845  1.00 14.70 ?  33  THR   A C    1 
ATOM   921  O O    . THR   A 1 33  ? 28.416 -4.986  14.588  1.00 14.62 ?  33  THR   A O    1 
ATOM   922  C CB   . THR   A 1 33  ? 27.529 -7.569  16.448  1.00 18.14 ?  33  THR   A CB   1 
ATOM   923  O OG1  . THR   A 1 33  ? 27.259 -7.971  17.796  1.00 19.78 ?  33  THR   A OG1  1 
ATOM   924  C CG2  . THR   A 1 33  ? 29.009 -7.757  16.155  1.00 18.93 ?  33  THR   A CG2  1 
ATOM   925  H H    . THR   A 1 33  ? 25.302 -6.691  16.796  1.00 19.89 ?  33  THR   A H    1 
ATOM   926  H HA   . THR   A 1 33  ? 27.649 -5.575  16.871  1.00 19.88 ?  33  THR   A HA   1 
ATOM   927  H HB   . THR   A 1 33  ? 27.023 -8.135  15.839  1.00 21.75 ?  33  THR   A HB   1 
ATOM   928  H HG1  . THR   A 1 33  ? 27.699 -7.495  18.334  1.00 23.71 ?  33  THR   A HG1  1 
ATOM   929  H HG21 . THR   A 1 33  ? 29.295 -8.640  16.438  1.00 22.69 ?  33  THR   A HG21 1 
ATOM   930  H HG22 . THR   A 1 33  ? 29.175 -7.665  15.204  1.00 22.69 ?  33  THR   A HG22 1 
ATOM   931  H HG23 . THR   A 1 33  ? 29.526 -7.092  16.634  1.00 22.69 ?  33  THR   A HG23 1 
ATOM   932  N N    . VAL   A 1 34  ? 26.486 -5.936  13.914  1.00 12.98 ?  34  VAL   A N    1 
ATOM   933  C CA   . VAL   A 1 34  ? 26.651 -5.586  12.508  1.00 11.98 ?  34  VAL   A CA   1 
ATOM   934  C C    . VAL   A 1 34  ? 25.340 -5.024  11.968  1.00 11.46 ?  34  VAL   A C    1 
ATOM   935  O O    . VAL   A 1 34  ? 24.298 -5.690  12.040  1.00 12.10 ?  34  VAL   A O    1 
ATOM   936  C CB   . VAL   A 1 34  ? 27.096 -6.783  11.646  1.00 12.15 ?  34  VAL   A CB   1 
ATOM   937  C CG1  . VAL   A 1 34  ? 27.264 -6.356  10.195  1.00 12.70 ?  34  VAL   A CG1  1 
ATOM   938  C CG2  . VAL   A 1 34  ? 28.392 -7.396  12.181  1.00 13.11 ?  34  VAL   A CG2  1 
ATOM   939  H H    . VAL   A 1 34  ? 25.754 -6.362  14.074  1.00 15.55 ?  34  VAL   A H    1 
ATOM   940  H HA   . VAL   A 1 34  ? 27.328 -4.893  12.429  1.00 14.35 ?  34  VAL   A HA   1 
ATOM   941  H HB   . VAL   A 1 34  ? 26.406 -7.462  11.671  1.00 14.56 ?  34  VAL   A HB   1 
ATOM   942  H HG11 . VAL   A 1 34  ? 27.747 -7.046  9.717   1.00 15.22 ?  34  VAL   A HG11 1 
ATOM   943  H HG12 . VAL   A 1 34  ? 26.392 -6.222  9.795   1.00 15.22 ?  34  VAL   A HG12 1 
ATOM   944  H HG13 . VAL   A 1 34  ? 27.770 -5.524  10.169  1.00 15.22 ?  34  VAL   A HG13 1 
ATOM   945  H HG21 . VAL   A 1 34  ? 28.671 -8.116  11.591  1.00 15.70 ?  34  VAL   A HG21 1 
ATOM   946  H HG22 . VAL   A 1 34  ? 29.080 -6.711  12.212  1.00 15.70 ?  34  VAL   A HG22 1 
ATOM   947  H HG23 . VAL   A 1 34  ? 28.232 -7.744  13.072  1.00 15.70 ?  34  VAL   A HG23 1 
ATOM   948  N N    . VAL   A 1 35  ? 25.395 -3.810  11.413  1.00 10.67 ?  35  VAL   A N    1 
ATOM   949  C CA   . VAL   A 1 35  ? 24.346 -3.292  10.545  1.00 10.40 ?  35  VAL   A CA   1 
ATOM   950  C C    . VAL   A 1 35  ? 24.884 -3.269  9.123   1.00 9.56  ?  35  VAL   A C    1 
ATOM   951  O O    . VAL   A 1 35  ? 26.022 -2.850  8.885   1.00 10.13 ?  35  VAL   A O    1 
ATOM   952  C CB   . VAL   A 1 35  ? 23.803 -1.911  10.979  1.00 11.30 ?  35  VAL   A CB   1 
ATOM   953  C CG1  . VAL   A 1 35  ? 24.857 -0.805  10.857  1.00 11.98 ?  35  VAL   A CG1  1 
ATOM   954  C CG2  . VAL   A 1 35  ? 22.546 -1.555  10.180  1.00 12.03 ?  35  VAL   A CG2  1 
ATOM   955  H H    . VAL   A 1 35  ? 26.045 -3.254  11.524  1.00 12.78 ?  35  VAL   A H    1 
ATOM   956  H HA   . VAL   A 1 35  ? 23.595 -3.909  10.563  1.00 12.46 ?  35  VAL   A HA   1 
ATOM   957  H HB   . VAL   A 1 35  ? 23.537 -1.959  11.908  1.00 13.54 ?  35  VAL   A HB   1 
ATOM   958  H HG11 . VAL   A 1 35  ? 24.508 0.016   11.243  1.00 14.36 ?  35  VAL   A HG11 1 
ATOM   959  H HG12 . VAL   A 1 35  ? 25.655 -1.079  11.336  1.00 14.36 ?  35  VAL   A HG12 1 
ATOM   960  H HG13 . VAL   A 1 35  ? 25.068 -0.662  9.920   1.00 14.36 ?  35  VAL   A HG13 1 
ATOM   961  H HG21 . VAL   A 1 35  ? 22.189 -0.712  10.502  1.00 14.41 ?  35  VAL   A HG21 1 
ATOM   962  H HG22 . VAL   A 1 35  ? 22.779 -1.473  9.238   1.00 14.41 ?  35  VAL   A HG22 1 
ATOM   963  H HG23 . VAL   A 1 35  ? 21.887 -2.258  10.293  1.00 14.41 ?  35  VAL   A HG23 1 
ATOM   964  N N    . VAL   A 1 36  ? 24.061 -3.717  8.180   1.00 9.20  ?  36  VAL   A N    1 
ATOM   965  C CA   . VAL   A 1 36  ? 24.420 -3.714  6.770   1.00 8.94  ?  36  VAL   A CA   1 
ATOM   966  C C    . VAL   A 1 36  ? 23.951 -2.416  6.129   1.00 9.47  ?  36  VAL   A C    1 
ATOM   967  O O    . VAL   A 1 36  ? 22.792 -2.004  6.292   1.00 10.10 ?  36  VAL   A O    1 
ATOM   968  C CB   . VAL   A 1 36  ? 23.805 -4.923  6.047   1.00 9.00  ?  36  VAL   A CB   1 
ATOM   969  C CG1  . VAL   A 1 36  ? 24.053 -4.840  4.569   1.00 9.56  ?  36  VAL   A CG1  1 
ATOM   970  C CG2  . VAL   A 1 36  ? 24.358 -6.225  6.605   1.00 10.16 ?  36  VAL   A CG2  1 
ATOM   971  H H    . VAL   A 1 36  ? 23.269 -4.036  8.333   1.00 11.02 ?  36  VAL   A H    1 
ATOM   972  H HA   . VAL   A 1 36  ? 25.386 -3.774  6.684   1.00 10.70 ?  36  VAL   A HA   1 
ATOM   973  H HB   . VAL   A 1 36  ? 22.845 -4.920  6.187   1.00 10.78 ?  36  VAL   A HB   1 
ATOM   974  H HG11 . VAL   A 1 36  ? 23.916 -5.715  4.171   1.00 11.44 ?  36  VAL   A HG11 1 
ATOM   975  H HG12 . VAL   A 1 36  ? 23.438 -4.201  4.172   1.00 11.44 ?  36  VAL   A HG12 1 
ATOM   976  H HG13 . VAL   A 1 36  ? 24.970 -4.553  4.415   1.00 11.44 ?  36  VAL   A HG13 1 
ATOM   977  H HG21 . VAL   A 1 36  ? 23.954 -6.976  6.129   1.00 12.16 ?  36  VAL   A HG21 1 
ATOM   978  H HG22 . VAL   A 1 36  ? 25.319 -6.246  6.484   1.00 12.16 ?  36  VAL   A HG22 1 
ATOM   979  H HG23 . VAL   A 1 36  ? 24.141 -6.289  7.549   1.00 12.16 ?  36  VAL   A HG23 1 
ATOM   980  N N    . ASN   A 1 37  ? 24.849 -1.786  5.377   1.00 8.83  ?  37  ASN   A N    1 
ATOM   981  C CA   . ASN   A 1 37  ? 24.508 -0.654  4.531   1.00 8.59  ?  37  ASN   A CA   1 
ATOM   982  C C    . ASN   A 1 37  ? 24.362 -1.095  3.084   1.00 8.75  ?  37  ASN   A C    1 
ATOM   983  O O    . ASN   A 1 37  ? 25.141 -1.921  2.589   1.00 9.23  ?  37  ASN   A O    1 
ATOM   984  C CB   . ASN   A 1 37  ? 25.588 0.422   4.610   1.00 9.08  ?  37  ASN   A CB   1 
ATOM   985  C CG   . ASN   A 1 37  ? 25.254 1.644   3.778   1.00 9.43  ?  37  ASN   A CG   1 
ATOM   986  O OD1  . ASN   A 1 37  ? 24.081 1.989   3.623   1.00 9.83  ?  37  ASN   A OD1  1 
ATOM   987  N ND2  . ASN   A 1 37  ? 26.278 2.305   3.254   1.00 9.55  ?  37  ASN   A ND2  1 
ATOM   988  H H    . ASN   A 1 37  ? 25.686 -1.997  5.345   1.00 10.58 ?  37  ASN   A H    1 
ATOM   989  H HA   . ASN   A 1 37  ? 23.671 -0.266  4.828   1.00 10.29 ?  37  ASN   A HA   1 
ATOM   990  H HB2  . ASN   A 1 37  ? 25.688 0.708   5.533   1.00 10.87 ?  37  ASN   A HB2  1 
ATOM   991  H HB3  . ASN   A 1 37  ? 26.429 0.055   4.286   1.00 10.87 ?  37  ASN   A HB3  1 
ATOM   992  H HD21 . ASN   A 1 37  ? 26.135 3.001   2.767   1.00 11.44 ?  37  ASN   A HD21 1 
ATOM   993  H HD22 . ASN   A 1 37  ? 27.079 2.036   3.382   1.00 11.44 ?  37  ASN   A HD22 1 
ATOM   994  N N    A ALA   A 1 38  ? 23.364 -0.508  2.415   0.40 8.64  ?  38  ALA   A N    1 
ATOM   995  N N    B ALA   A 1 38  ? 23.342 -0.554  2.416   0.60 9.44  ?  38  ALA   A N    1 
ATOM   996  C CA   A ALA   A 1 38  ? 23.146 -0.617  0.972   0.40 8.48  ?  38  ALA   A CA   1 
ATOM   997  C CA   B ALA   A 1 38  ? 23.140 -0.744  0.979   0.60 10.23 ?  38  ALA   A CA   1 
ATOM   998  C C    A ALA   A 1 38  ? 24.094 0.357   0.273   0.40 8.41  ?  38  ALA   A C    1 
ATOM   999  C C    B ALA   A 1 38  ? 23.998 0.280   0.236   0.60 9.63  ?  38  ALA   A C    1 
ATOM   1000 O O    A ALA   A 1 38  ? 23.724 1.467   -0.121  0.40 8.82  ?  38  ALA   A O    1 
ATOM   1001 O O    B ALA   A 1 38  ? 23.536 1.344   -0.189  0.60 10.04 ?  38  ALA   A O    1 
ATOM   1002 C CB   A ALA   A 1 38  ? 21.691 -0.307  0.635   0.40 8.90  ?  38  ALA   A CB   1 
ATOM   1003 C CB   B ALA   A 1 38  ? 21.666 -0.609  0.626   0.60 11.50 ?  38  ALA   A CB   1 
ATOM   1004 H H    A ALA   A 1 38  ? 22.783 -0.002  2.796   0.40 10.35 ?  38  ALA   A H    1 
ATOM   1005 H H    B ALA   A 1 38  ? 22.746 -0.053  2.784   0.60 11.30 ?  38  ALA   A H    1 
ATOM   1006 H HA   A ALA   A 1 38  ? 23.346 -1.518  0.677   0.40 10.15 ?  38  ALA   A HA   1 
ATOM   1007 H HA   B ALA   A 1 38  ? 23.440 -1.634  0.730   0.60 12.25 ?  38  ALA   A HA   1 
ATOM   1008 H HB1  A ALA   A 1 38  ? 21.558 -0.394  -0.323  0.40 10.66 ?  38  ALA   A HB1  1 
ATOM   1009 H HB1  B ALA   A 1 38  ? 21.564 -0.716  -0.332  0.60 13.77 ?  38  ALA   A HB1  1 
ATOM   1010 H HB2  A ALA   A 1 38  ? 21.117 -0.933  1.105   0.40 10.66 ?  38  ALA   A HB2  1 
ATOM   1011 H HB2  B ALA   A 1 38  ? 21.165 -1.296  1.092   0.60 13.77 ?  38  ALA   A HB2  1 
ATOM   1012 H HB3  A ALA   A 1 38  ? 21.486 0.600   0.914   0.40 10.66 ?  38  ALA   A HB3  1 
ATOM   1013 H HB3  B ALA   A 1 38  ? 21.357 0.269   0.896   0.60 13.77 ?  38  ALA   A HB3  1 
ATOM   1014 N N    A ALA   A 1 39  ? 25.345 -0.071  0.121   0.40 8.49  ?  39  ALA   A N    1 
ATOM   1015 N N    B ALA   A 1 39  ? 25.276 -0.056  0.078   0.60 9.68  ?  39  ALA   A N    1 
ATOM   1016 C CA   A ALA   A 1 39  ? 26.428 0.783   -0.340  0.40 8.83  ?  39  ALA   A CA   1 
ATOM   1017 C CA   B ALA   A 1 39  ? 26.285 0.868   -0.413  0.60 9.75  ?  39  ALA   A CA   1 
ATOM   1018 C C    A ALA   A 1 39  ? 26.575 0.741   -1.857  0.40 9.04  ?  39  ALA   A C    1 
ATOM   1019 C C    B ALA   A 1 39  ? 26.414 0.795   -1.930  0.60 9.16  ?  39  ALA   A C    1 
ATOM   1020 O O    A ALA   A 1 39  ? 26.077 -0.162  -2.533  0.40 8.94  ?  39  ALA   A O    1 
ATOM   1021 O O    B ALA   A 1 39  ? 25.938 -0.139  -2.578  0.60 9.83  ?  39  ALA   A O    1 
ATOM   1022 C CB   A ALA   A 1 39  ? 27.738 0.329   0.306   0.40 8.96  ?  39  ALA   A CB   1 
ATOM   1023 C CB   B ALA   A 1 39  ? 27.628 0.533   0.238   0.60 10.60 ?  39  ALA   A CB   1 
ATOM   1024 H H    A ALA   A 1 39  ? 25.594 -0.882  0.287   0.40 10.17 ?  39  ALA   A H    1 
ATOM   1025 H H    B ALA   A 1 39  ? 25.584 -0.846  0.250   0.60 11.59 ?  39  ALA   A H    1 
ATOM   1026 H HA   A ALA   A 1 39  ? 26.251 1.695   -0.080  0.40 10.57 ?  39  ALA   A HA   1 
ATOM   1027 H HA   B ALA   A 1 39  ? 26.035 1.769   -0.167  0.60 11.67 ?  39  ALA   A HA   1 
ATOM   1028 H HB1  A ALA   A 1 39  ? 28.454 0.903   -0.004  0.40 10.73 ?  39  ALA   A HB1  1 
ATOM   1029 H HB1  B ALA   A 1 39  ? 28.296 1.151   -0.088  0.60 12.70 ?  39  ALA   A HB1  1 
ATOM   1030 H HB2  A ALA   A 1 39  ? 27.648 0.400   1.270   0.40 10.73 ?  39  ALA   A HB2  1 
ATOM   1031 H HB2  B ALA   A 1 39  ? 27.538 0.621   1.204   0.60 12.70 ?  39  ALA   A HB2  1 
ATOM   1032 H HB3  A ALA   A 1 39  ? 27.913 -0.590  0.055   0.40 10.73 ?  39  ALA   A HB3  1 
ATOM   1033 H HB3  B ALA   A 1 39  ? 27.872 -0.377  0.014   0.60 12.70 ?  39  ALA   A HB3  1 
ATOM   1034 N N    A ASN   A 1 40  ? 27.287 1.736   -2.386  0.40 9.56  ?  40  ASN   A N    1 
ATOM   1035 N N    B ASN   A 1 40  ? 27.066 1.809   -2.494  0.60 9.03  ?  40  ASN   A N    1 
ATOM   1036 C CA   A ASN   A 1 40  ? 27.834 1.693   -3.736  0.40 9.50  ?  40  ASN   A CA   1 
ATOM   1037 C CA   B ASN   A 1 40  ? 27.565 1.763   -3.861  0.60 9.28  ?  40  ASN   A CA   1 
ATOM   1038 C C    A ASN   A 1 40  ? 29.359 1.614   -3.668  0.40 8.68  ?  40  ASN   A C    1 
ATOM   1039 C C    B ASN   A 1 40  ? 29.088 1.636   -3.845  0.60 8.58  ?  40  ASN   A C    1 
ATOM   1040 O O    A ASN   A 1 40  ? 29.965 1.750   -2.601  0.40 8.94  ?  40  ASN   A O    1 
ATOM   1041 O O    B ASN   A 1 40  ? 29.721 1.692   -2.792  0.60 9.02  ?  40  ASN   A O    1 
ATOM   1042 C CB   A ASN   A 1 40  ? 27.347 2.872   -4.594  0.40 10.36 ?  40  ASN   A CB   1 
ATOM   1043 C CB   B ASN   A 1 40  ? 27.089 2.976   -4.671  0.60 10.14 ?  40  ASN   A CB   1 
ATOM   1044 C CG   A ASN   A 1 40  ? 27.709 4.221   -4.009  0.40 11.63 ?  40  ASN   A CG   1 
ATOM   1045 C CG   B ASN   A 1 40  ? 27.468 4.298   -4.036  0.60 11.39 ?  40  ASN   A CG   1 
ATOM   1046 O OD1  A ASN   A 1 40  ? 28.883 4.560   -3.895  0.40 11.42 ?  40  ASN   A OD1  1 
ATOM   1047 O OD1  B ASN   A 1 40  ? 28.601 4.491   -3.588  0.60 12.94 ?  40  ASN   A OD1  1 
ATOM   1048 N ND2  A ASN   A 1 40  ? 26.700 5.009   -3.660  0.40 11.99 ?  40  ASN   A ND2  1 
ATOM   1049 N ND2  B ASN   A 1 40  ? 26.519 5.224   -4.001  0.60 11.39 ?  40  ASN   A ND2  1 
ATOM   1050 H H    A ASN   A 1 40  ? 27.474 2.462   -1.968  0.40 11.45 ?  40  ASN   A H    1 
ATOM   1051 H H    B ASN   A 1 40  ? 27.230 2.548   -2.094  0.60 10.81 ?  40  ASN   A H    1 
ATOM   1052 H HA   A ASN   A 1 40  ? 27.530 0.884   -4.169  0.40 11.37 ?  40  ASN   A HA   1 
ATOM   1053 H HA   B ASN   A 1 40  ? 27.206 0.968   -4.295  0.60 11.11 ?  40  ASN   A HA   1 
ATOM   1054 H HB2  A ASN   A 1 40  ? 27.747 2.807   -5.481  0.40 12.41 ?  40  ASN   A HB2  1 
ATOM   1055 H HB2  B ASN   A 1 40  ? 27.486 2.937   -5.557  0.60 12.14 ?  40  ASN   A HB2  1 
ATOM   1056 H HB3  A ASN   A 1 40  ? 26.382 2.829   -4.669  0.40 12.41 ?  40  ASN   A HB3  1 
ATOM   1057 H HB3  B ASN   A 1 40  ? 26.122 2.944   -4.747  0.60 12.14 ?  40  ASN   A HB3  1 
ATOM   1058 H HD21 A ASN   A 1 40  ? 26.862 5.791   -3.335  0.40 14.37 ?  40  ASN   A HD21 1 
ATOM   1059 H HD21 B ASN   A 1 40  ? 26.686 6.000   -3.661  0.60 13.64 ?  40  ASN   A HD21 1 
ATOM   1060 H HD22 A ASN   A 1 40  ? 25.893 4.741   -3.757  0.40 14.37 ?  40  ASN   A HD22 1 
ATOM   1061 H HD22 B ASN   A 1 40  ? 25.743 5.056   -4.324  0.60 13.64 ?  40  ASN   A HD22 1 
ATOM   1062 N N    A VAL   A 1 41  ? 29.979 1.357   -4.825  0.40 8.67  ?  41  VAL   A N    1 
ATOM   1063 N N    B VAL   A 1 41  ? 29.675 1.432   -5.028  0.60 9.40  ?  41  VAL   A N    1 
ATOM   1064 C CA   A VAL   A 1 41  ? 31.411 1.056   -4.848  0.40 8.77  ?  41  VAL   A CA   1 
ATOM   1065 C CA   B VAL   A 1 41  ? 31.104 1.124   -5.108  0.60 9.90  ?  41  VAL   A CA   1 
ATOM   1066 C C    A VAL   A 1 41  ? 32.237 2.228   -4.354  0.40 9.22  ?  41  VAL   A C    1 
ATOM   1067 C C    B VAL   A 1 41  ? 31.992 2.261   -4.620  0.60 9.92  ?  41  VAL   A C    1 
ATOM   1068 O O    A VAL   A 1 41  ? 33.338 2.041   -3.820  0.40 9.26  ?  41  VAL   A O    1 
ATOM   1069 O O    B VAL   A 1 41  ? 33.159 2.023   -4.282  0.60 9.57  ?  41  VAL   A O    1 
ATOM   1070 C CB   A VAL   A 1 41  ? 31.882 0.569   -6.239  0.40 8.44  ?  41  VAL   A CB   1 
ATOM   1071 C CB   B VAL   A 1 41  ? 31.528 0.684   -6.528  0.60 11.16 ?  41  VAL   A CB   1 
ATOM   1072 C CG1  A VAL   A 1 41  ? 31.137 -0.694  -6.642  0.40 8.93  ?  41  VAL   A CG1  1 
ATOM   1073 C CG1  B VAL   A 1 41  ? 30.889 -0.649  -6.888  0.60 12.11 ?  41  VAL   A CG1  1 
ATOM   1074 C CG2  A VAL   A 1 41  ? 31.741 1.655   -7.311  0.40 7.79  ?  41  VAL   A CG2  1 
ATOM   1075 C CG2  B VAL   A 1 41  ? 31.199 1.757   -7.571  0.60 12.02 ?  41  VAL   A CG2  1 
ATOM   1076 H H    A VAL   A 1 41  ? 29.607 1.350   -5.597  0.40 10.38 ?  41  VAL   A H    1 
ATOM   1077 H H    B VAL   A 1 41  ? 29.271 1.449   -5.786  0.60 11.25 ?  41  VAL   A H    1 
ATOM   1078 H HA   A VAL   A 1 41  ? 31.581 0.334   -4.233  0.40 10.49 ?  41  VAL   A HA   1 
ATOM   1079 H HA   B VAL   A 1 41  ? 31.276 0.373   -4.523  0.60 11.86 ?  41  VAL   A HA   1 
ATOM   1080 H HB   A VAL   A 1 41  ? 32.826 0.342   -6.189  0.40 10.10 ?  41  VAL   A HB   1 
ATOM   1081 H HB   B VAL   A 1 41  ? 32.491 0.556   -6.534  0.60 13.37 ?  41  VAL   A HB   1 
ATOM   1082 H HG11 A VAL   A 1 41  ? 31.469 -1.006  -7.497  0.40 10.69 ?  41  VAL   A HG11 1 
ATOM   1083 H HG11 B VAL   A 1 41  ? 31.199 -0.922  -7.763  0.60 14.51 ?  41  VAL   A HG11 1 
ATOM   1084 H HG12 A VAL   A 1 41  ? 31.277 -1.373  -5.964  0.40 10.69 ?  41  VAL   A HG12 1 
ATOM   1085 H HG12 B VAL   A 1 41  ? 31.146 -1.311  -6.224  0.60 14.51 ?  41  VAL   A HG12 1 
ATOM   1086 H HG13 A VAL   A 1 41  ? 30.188 -0.491  -6.712  0.40 10.69 ?  41  VAL   A HG13 1 
ATOM   1087 H HG13 B VAL   A 1 41  ? 29.925 -0.546  -6.892  0.60 14.51 ?  41  VAL   A HG13 1 
ATOM   1088 H HG21 A VAL   A 1 41  ? 31.945 1.267   -8.181  0.40 9.33  ?  41  VAL   A HG21 1 
ATOM   1089 H HG21 B VAL   A 1 41  ? 31.510 1.456   -8.441  0.60 14.40 ?  41  VAL   A HG21 1 
ATOM   1090 H HG22 A VAL   A 1 41  ? 30.834 1.987   -7.303  0.40 9.33  ?  41  VAL   A HG22 1 
ATOM   1091 H HG22 B VAL   A 1 41  ? 30.237 1.890   -7.597  0.60 14.40 ?  41  VAL   A HG22 1 
ATOM   1092 H HG23 A VAL   A 1 41  ? 32.364 2.371   -7.118  0.40 9.33  ?  41  VAL   A HG23 1 
ATOM   1093 H HG23 B VAL   A 1 41  ? 31.641 2.583   -7.330  0.60 14.40 ?  41  VAL   A HG23 1 
ATOM   1094 N N    A TYR   A 1 42  ? 31.737 3.448   -4.532  0.40 9.83  ?  42  TYR   A N    1 
ATOM   1095 N N    B TYR   A 1 42  ? 31.486 3.498   -4.600  0.60 10.37 ?  42  TYR   A N    1 
ATOM   1096 C CA   A TYR   A 1 42  ? 32.429 4.651   -4.098  0.40 10.36 ?  42  TYR   A CA   1 
ATOM   1097 C CA   B TYR   A 1 42  ? 32.265 4.658   -4.177  0.60 10.63 ?  42  TYR   A CA   1 
ATOM   1098 C C    A TYR   A 1 42  ? 32.126 4.996   -2.648  0.40 10.16 ?  42  TYR   A C    1 
ATOM   1099 C C    B TYR   A 1 42  ? 32.027 5.036   -2.722  0.60 10.51 ?  42  TYR   A C    1 
ATOM   1100 O O    A TYR   A 1 42  ? 32.713 5.948   -2.115  0.40 10.59 ?  42  TYR   A O    1 
ATOM   1101 O O    B TYR   A 1 42  ? 32.575 6.046   -2.259  0.60 11.18 ?  42  TYR   A O    1 
ATOM   1102 C CB   A TYR   A 1 42  ? 32.040 5.837   -5.004  0.40 11.48 ?  42  TYR   A CB   1 
ATOM   1103 C CB   B TYR   A 1 42  ? 31.979 5.867   -5.090  0.60 11.79 ?  42  TYR   A CB   1 
ATOM   1104 C CG   A TYR   A 1 42  ? 32.142 5.538   -6.492  0.40 12.36 ?  42  TYR   A CG   1 
ATOM   1105 C CG   B TYR   A 1 42  ? 32.211 5.560   -6.552  0.60 12.97 ?  42  TYR   A CG   1 
ATOM   1106 C CD1  A TYR   A 1 42  ? 33.374 5.355   -7.102  0.40 12.56 ?  42  TYR   A CD1  1 
ATOM   1107 C CD1  B TYR   A 1 42  ? 33.488 5.353   -7.044  0.60 13.74 ?  42  TYR   A CD1  1 
ATOM   1108 C CD2  A TYR   A 1 42  ? 31.004 5.431   -7.285  0.40 13.40 ?  42  TYR   A CD2  1 
ATOM   1109 C CD2  B TYR   A 1 42  ? 31.147 5.444   -7.432  0.60 13.80 ?  42  TYR   A CD2  1 
ATOM   1110 C CE1  A TYR   A 1 42  ? 33.474 5.074   -8.455  0.40 13.00 ?  42  TYR   A CE1  1 
ATOM   1111 C CE1  B TYR   A 1 42  ? 33.700 5.050   -8.376  0.60 14.39 ?  42  TYR   A CE1  1 
ATOM   1112 C CE2  A TYR   A 1 42  ? 31.097 5.157   -8.642  0.40 13.89 ?  42  TYR   A CE2  1 
ATOM   1113 C CE2  B TYR   A 1 42  ? 31.349 5.148   -8.765  0.60 14.53 ?  42  TYR   A CE2  1 
ATOM   1114 C CZ   A TYR   A 1 42  ? 32.336 4.979   -9.219  0.40 13.73 ?  42  TYR   A CZ   1 
ATOM   1115 C CZ   B TYR   A 1 42  ? 32.628 4.951   -9.232  0.60 14.85 ?  42  TYR   A CZ   1 
ATOM   1116 O OH   A TYR   A 1 42  ? 32.443 4.703   -10.565 0.40 14.69 ?  42  TYR   A OH   1 
ATOM   1117 O OH   B TYR   A 1 42  ? 32.829 4.651   -10.559 0.60 16.68 ?  42  TYR   A OH   1 
ATOM   1118 H H    A TYR   A 1 42  ? 30.984 3.603   -4.901  0.40 11.77 ?  42  TYR   A H    1 
ATOM   1119 H H    B TYR   A 1 42  ? 30.678 3.693   -4.844  0.60 12.42 ?  42  TYR   A H    1 
ATOM   1120 H HA   A TYR   A 1 42  ? 33.389 4.517   -4.187  0.40 12.40 ?  42  TYR   A HA   1 
ATOM   1121 H HA   B TYR   A 1 42  ? 33.202 4.447   -4.268  0.60 12.73 ?  42  TYR   A HA   1 
ATOM   1122 H HB2  A TYR   A 1 42  ? 31.124 6.088   -4.816  0.40 13.75 ?  42  TYR   A HB2  1 
ATOM   1123 H HB2  B TYR   A 1 42  ? 31.056 6.140   -4.984  0.60 14.12 ?  42  TYR   A HB2  1 
ATOM   1124 H HB3  A TYR   A 1 42  ? 32.632 6.585   -4.815  0.40 13.75 ?  42  TYR   A HB3  1 
ATOM   1125 H HB3  B TYR   A 1 42  ? 32.571 6.599   -4.842  0.60 14.12 ?  42  TYR   A HB3  1 
ATOM   1126 H HD1  A TYR   A 1 42  ? 34.149 5.417   -6.597  0.40 15.05 ?  42  TYR   A HD1  1 
ATOM   1127 H HD1  B TYR   A 1 42  ? 34.219 5.420   -6.471  0.60 16.47 ?  42  TYR   A HD1  1 
ATOM   1128 H HD2  A TYR   A 1 42  ? 30.165 5.551   -6.905  0.40 16.05 ?  42  TYR   A HD2  1 
ATOM   1129 H HD2  B TYR   A 1 42  ? 30.280 5.579   -7.117  0.60 16.53 ?  42  TYR   A HD2  1 
ATOM   1130 H HE1  A TYR   A 1 42  ? 34.310 4.950   -8.849  0.40 15.58 ?  42  TYR   A HE1  1 
ATOM   1131 H HE1  B TYR   A 1 42  ? 34.565 4.922   -8.694  0.60 17.24 ?  42  TYR   A HE1  1 
ATOM   1132 H HE2  A TYR   A 1 42  ? 30.325 5.084   -9.163  0.40 16.64 ?  42  TYR   A HE2  1 
ATOM   1133 H HE2  B TYR   A 1 42  ? 30.621 5.081   -9.341  0.60 17.41 ?  42  TYR   A HE2  1 
ATOM   1134 H HH   A TYR   A 1 42  ? 33.255 4.607   -10.781 0.40 17.61 ?  42  TYR   A HH   1 
ATOM   1135 H HH   B TYR   A 1 42  ? 33.647 4.523   -10.701 0.60 19.99 ?  42  TYR   A HH   1 
ATOM   1136 N N    . LEU   A 1 43  ? 31.218 4.256   -2.005  1.00 10.14 ?  43  LEU   A N    1 
ATOM   1137 C CA   . LEU   A 1 43  ? 30.787 4.575   -0.647  1.00 10.02 ?  43  LEU   A CA   1 
ATOM   1138 C C    . LEU   A 1 43  ? 30.303 6.019   -0.533  1.00 9.96  ?  43  LEU   A C    1 
ATOM   1139 O O    . LEU   A 1 43  ? 30.576 6.709   0.448   1.00 11.19 ?  43  LEU   A O    1 
ATOM   1140 C CB   . LEU   A 1 43  ? 31.852 4.256   0.399   1.00 10.19 ?  43  LEU   A CB   1 
ATOM   1141 C CG   . LEU   A 1 43  ? 32.340 2.802   0.474   1.00 10.39 ?  43  LEU   A CG   1 
ATOM   1142 C CD1  . LEU   A 1 43  ? 33.413 2.672   1.547   1.00 11.38 ?  43  LEU   A CD1  1 
ATOM   1143 C CD2  . LEU   A 1 43  ? 31.198 1.825   0.732   1.00 10.78 ?  43  LEU   A CD2  1 
ATOM   1144 H H    A LEU   A 1 43  ? 30.824 3.565   -2.343  0.40 12.14 ?  43  LEU   A H    1 
ATOM   1145 H H    B LEU   A 1 43  ? 30.895 3.510   -2.296  0.60 12.14 ?  43  LEU   A H    1 
ATOM   1146 H HA   . LEU   A 1 43  ? 30.024 4.010   -0.443  1.00 12.00 ?  43  LEU   A HA   1 
ATOM   1147 H HB2  . LEU   A 1 43  ? 32.627 4.809   0.223   1.00 12.20 ?  43  LEU   A HB2  1 
ATOM   1148 H HB3  . LEU   A 1 43  ? 31.490 4.476   1.272   1.00 12.20 ?  43  LEU   A HB3  1 
ATOM   1149 H HG   . LEU   A 1 43  ? 32.747 2.563   -0.374  1.00 12.44 ?  43  LEU   A HG   1 
ATOM   1150 H HD11 . LEU   A 1 43  ? 33.714 1.748   1.586   1.00 13.63 ?  43  LEU   A HD11 1 
ATOM   1151 H HD12 . LEU   A 1 43  ? 34.157 3.252   1.327   1.00 13.63 ?  43  LEU   A HD12 1 
ATOM   1152 H HD13 . LEU   A 1 43  ? 33.036 2.929   2.405   1.00 13.63 ?  43  LEU   A HD13 1 
ATOM   1153 H HD21 . LEU   A 1 43  ? 31.568 0.938   0.867   1.00 12.91 ?  43  LEU   A HD21 1 
ATOM   1154 H HD22 . LEU   A 1 43  ? 30.718 2.108   1.526   1.00 12.91 ?  43  LEU   A HD22 1 
ATOM   1155 H HD23 . LEU   A 1 43  ? 30.607 1.826   -0.034  1.00 12.91 ?  43  LEU   A HD23 1 
ATOM   1156 N N    A LYS   A 1 44  ? 29.576 6.475   -1.553  0.40 10.57 ?  44  LYS   A N    1 
ATOM   1157 N N    B LYS   A 1 44  ? 29.566 6.470   -1.550  0.60 9.99  ?  44  LYS   A N    1 
ATOM   1158 C CA   A LYS   A 1 44  ? 28.942 7.793   -1.538  0.40 11.60 ?  44  LYS   A CA   1 
ATOM   1159 C CA   B LYS   A 1 44  ? 28.909 7.776   -1.531  0.60 10.59 ?  44  LYS   A CA   1 
ATOM   1160 C C    A LYS   A 1 44  ? 27.520 7.611   -1.027  0.40 10.77 ?  44  LYS   A C    1 
ATOM   1161 C C    B LYS   A 1 44  ? 27.483 7.563   -1.034  0.60 10.11 ?  44  LYS   A C    1 
ATOM   1162 O O    A LYS   A 1 44  ? 26.636 7.145   -1.751  0.40 11.47 ?  44  LYS   A O    1 
ATOM   1163 O O    B LYS   A 1 44  ? 26.632 7.027   -1.754  0.60 11.14 ?  44  LYS   A O    1 
ATOM   1164 C CB   A LYS   A 1 44  ? 28.979 8.427   -2.924  0.40 14.16 ?  44  LYS   A CB   1 
ATOM   1165 C CB   B LYS   A 1 44  ? 28.922 8.415   -2.917  0.60 12.87 ?  44  LYS   A CB   1 
ATOM   1166 C CG   A LYS   A 1 44  ? 30.364 8.882   -3.360  0.40 17.29 ?  44  LYS   A CG   1 
ATOM   1167 C CG   B LYS   A 1 44  ? 30.290 8.879   -3.389  0.60 16.55 ?  44  LYS   A CG   1 
ATOM   1168 C CD   A LYS   A 1 44  ? 31.016 9.796   -2.329  0.40 20.90 ?  44  LYS   A CD   1 
ATOM   1169 C CD   B LYS   A 1 44  ? 31.001 9.762   -2.374  0.60 21.72 ?  44  LYS   A CD   1 
ATOM   1170 C CE   A LYS   A 1 44  ? 32.381 10.265  -2.791  0.40 23.25 ?  44  LYS   A CE   1 
ATOM   1171 C CE   B LYS   A 1 44  ? 32.141 10.523  -3.032  0.60 24.82 ?  44  LYS   A CE   1 
ATOM   1172 N NZ   A LYS   A 1 44  ? 33.110 10.997  -1.723  0.40 24.60 ?  44  LYS   A NZ   1 
ATOM   1173 N NZ   B LYS   A 1 44  ? 33.140 11.009  -2.046  0.60 26.74 ?  44  LYS   A NZ   1 
ATOM   1174 H H    A LYS   A 1 44  ? 29.437 6.033   -2.280  0.40 12.66 ?  44  LYS   A H    1 
ATOM   1175 H H    B LYS   A 1 44  ? 29.427 6.025   -2.274  0.60 11.96 ?  44  LYS   A H    1 
ATOM   1176 H HA   A LYS   A 1 44  ? 29.403 8.366   -0.908  0.40 13.90 ?  44  LYS   A HA   1 
ATOM   1177 H HA   B LYS   A 1 44  ? 29.365 8.359   -0.907  0.60 12.68 ?  44  LYS   A HA   1 
ATOM   1178 H HB2  A LYS   A 1 44  ? 28.661 7.780   -3.575  0.40 16.96 ?  44  LYS   A HB2  1 
ATOM   1179 H HB2  B LYS   A 1 44  ? 28.588 7.773   -3.561  0.60 15.42 ?  44  LYS   A HB2  1 
ATOM   1180 H HB3  A LYS   A 1 44  ? 28.399 9.205   -2.928  0.40 16.96 ?  44  LYS   A HB3  1 
ATOM   1181 H HB3  B LYS   A 1 44  ? 28.340 9.194   -2.903  0.60 15.42 ?  44  LYS   A HB3  1 
ATOM   1182 H HG2  A LYS   A 1 44  ? 30.929 8.103   -3.480  0.40 20.72 ?  44  LYS   A HG2  1 
ATOM   1183 H HG2  B LYS   A 1 44  ? 30.844 8.098   -3.552  0.60 19.83 ?  44  LYS   A HG2  1 
ATOM   1184 H HG3  A LYS   A 1 44  ? 30.289 9.371   -4.196  0.40 20.72 ?  44  LYS   A HG3  1 
ATOM   1185 H HG3  B LYS   A 1 44  ? 30.185 9.386   -4.209  0.60 19.83 ?  44  LYS   A HG3  1 
ATOM   1186 H HD2  A LYS   A 1 44  ? 30.444 10.567  -2.184  0.40 25.05 ?  44  LYS   A HD2  1 
ATOM   1187 H HD2  B LYS   A 1 44  ? 30.370 10.400  -2.007  0.60 26.04 ?  44  LYS   A HD2  1 
ATOM   1188 H HD3  A LYS   A 1 44  ? 31.140 9.308   -1.500  0.40 25.05 ?  44  LYS   A HD3  1 
ATOM   1189 H HD3  B LYS   A 1 44  ? 31.368 9.205   -1.667  0.60 26.04 ?  44  LYS   A HD3  1 
ATOM   1190 H HE2  A LYS   A 1 44  ? 32.909 9.493   -3.045  0.40 27.88 ?  44  LYS   A HE2  1 
ATOM   1191 H HE2  B LYS   A 1 44  ? 32.594 9.934   -3.657  0.60 29.76 ?  44  LYS   A HE2  1 
ATOM   1192 H HE3  A LYS   A 1 44  ? 32.269 10.860  -3.547  0.40 27.88 ?  44  LYS   A HE3  1 
ATOM   1193 H HE3  B LYS   A 1 44  ? 31.778 11.290  -3.501  0.60 29.76 ?  44  LYS   A HE3  1 
ATOM   1194 H HZ1  A LYS   A 1 44  ? 33.905 11.259  -2.025  0.40 29.50 ?  44  LYS   A HZ1  1 
ATOM   1195 H HZ1  B LYS   A 1 44  ? 33.797 11.437  -2.467  0.60 32.07 ?  44  LYS   A HZ1  1 
ATOM   1196 H HZ2  A LYS   A 1 44  ? 32.645 11.715  -1.475  0.40 29.50 ?  44  LYS   A HZ2  1 
ATOM   1197 H HZ2  B LYS   A 1 44  ? 32.752 11.569  -1.472  0.60 32.07 ?  44  LYS   A HZ2  1 
ATOM   1198 H HZ3  A LYS   A 1 44  ? 33.226 10.470  -1.016  0.40 29.50 ?  44  LYS   A HZ3  1 
ATOM   1199 H HZ3  B LYS   A 1 44  ? 33.482 10.324  -1.595  0.60 32.07 ?  44  LYS   A HZ3  1 
ATOM   1200 N N    A HIS   A 1 45  ? 27.302 7.978   0.231   0.40 10.19 ?  45  HIS   A N    1 
ATOM   1201 N N    B HIS   A 1 45  ? 27.232 7.956   0.211   0.60 9.92  ?  45  HIS   A N    1 
ATOM   1202 C CA   A HIS   A 1 45  ? 26.065 7.639   0.930   0.40 10.05 ?  45  HIS   A CA   1 
ATOM   1203 C CA   B HIS   A 1 45  ? 25.990 7.612   0.898   0.60 10.06 ?  45  HIS   A CA   1 
ATOM   1204 C C    A HIS   A 1 45  ? 25.049 8.779   0.833   0.40 10.64 ?  45  HIS   A C    1 
ATOM   1205 C C    B HIS   A 1 45  ? 24.966 8.725   0.689   0.60 10.38 ?  45  HIS   A C    1 
ATOM   1206 O O    A HIS   A 1 45  ? 24.639 9.375   1.825   0.40 11.40 ?  45  HIS   A O    1 
ATOM   1207 O O    B HIS   A 1 45  ? 24.708 9.549   1.566   0.60 12.04 ?  45  HIS   A O    1 
ATOM   1208 C CB   A HIS   A 1 45  ? 26.372 7.282   2.378   0.40 9.76  ?  45  HIS   A CB   1 
ATOM   1209 C CB   B HIS   A 1 45  ? 26.271 7.385   2.373   0.60 9.96  ?  45  HIS   A CB   1 
ATOM   1210 C CG   A HIS   A 1 45  ? 27.494 6.303   2.533   0.40 9.19  ?  45  HIS   A CG   1 
ATOM   1211 C CG   B HIS   A 1 45  ? 27.404 6.444   2.631   0.60 9.13  ?  45  HIS   A CG   1 
ATOM   1212 N ND1  A HIS   A 1 45  ? 27.448 5.021   2.023   0.40 9.30  ?  45  HIS   A ND1  1 
ATOM   1213 N ND1  B HIS   A 1 45  ? 27.427 5.154   2.144   0.60 10.08 ?  45  HIS   A ND1  1 
ATOM   1214 C CD2  A HIS   A 1 45  ? 28.700 6.427   3.139   0.40 9.90  ?  45  HIS   A CD2  1 
ATOM   1215 C CD2  B HIS   A 1 45  ? 28.561 6.615   3.317   0.60 9.01  ?  45  HIS   A CD2  1 
ATOM   1216 C CE1  A HIS   A 1 45  ? 28.577 4.399   2.316   0.40 9.86  ?  45  HIS   A CE1  1 
ATOM   1217 C CE1  B HIS   A 1 45  ? 28.550 4.572   2.527   0.60 9.10  ?  45  HIS   A CE1  1 
ATOM   1218 N NE2  A HIS   A 1 45  ? 29.352 5.229   2.993   0.40 10.19 ?  45  HIS   A NE2  1 
ATOM   1219 N NE2  B HIS   A 1 45  ? 29.253 5.433   3.241   0.60 8.66  ?  45  HIS   A NE2  1 
ATOM   1220 H H    A HIS   A 1 45  ? 27.855 8.440   0.703   0.40 12.20 ?  45  HIS   A H    1 
ATOM   1221 H H    B HIS   A 1 45  ? 27.765 8.429   0.689   0.60 11.87 ?  45  HIS   A H    1 
ATOM   1222 H HA   A HIS   A 1 45  ? 25.668 6.863   0.510   0.40 12.04 ?  45  HIS   A HA   1 
ATOM   1223 H HA   B HIS   A 1 45  ? 25.630 6.785   0.526   0.60 12.05 ?  45  HIS   A HA   1 
ATOM   1224 H HB2  A HIS   A 1 45  ? 26.613 8.089   2.858   0.40 11.68 ?  45  HIS   A HB2  1 
ATOM   1225 H HB2  B HIS   A 1 45  ? 26.490 8.236   2.783   0.60 11.92 ?  45  HIS   A HB2  1 
ATOM   1226 H HB3  A HIS   A 1 45  ? 25.579 6.887   2.777   0.40 11.68 ?  45  HIS   A HB3  1 
ATOM   1227 H HB3  B HIS   A 1 45  ? 25.478 7.012   2.793   0.60 11.92 ?  45  HIS   A HB3  1 
ATOM   1228 H HD2  A HIS   A 1 45  ? 29.026 7.183   3.573   0.40 11.85 ?  45  HIS   A HD2  1 
ATOM   1229 H HD2  B HIS   A 1 45  ? 28.835 7.388   3.756   0.60 10.78 ?  45  HIS   A HD2  1 
ATOM   1230 H HE1  A HIS   A 1 45  ? 28.789 3.519   2.093   0.40 11.81 ?  45  HIS   A HE1  1 
ATOM   1231 H HE1  B HIS   A 1 45  ? 28.795 3.697   2.334   0.60 10.89 ?  45  HIS   A HE1  1 
ATOM   1232 H HE2  A HIS   A 1 45  ? 30.141 5.047   3.292   0.40 12.21 ?  45  HIS   A HE2  1 
ATOM   1233 H HE2  B HIS   A 1 45  ? 30.020 5.279   3.594   0.60 10.37 ?  45  HIS   A HE2  1 
ATOM   1234 N N    A GLY   A 1 46  ? 24.634 9.062   -0.400  0.40 11.16 ?  46  GLY   A N    1 
ATOM   1235 N N    B GLY   A 1 46  ? 24.366 8.741   -0.498  0.60 10.53 ?  46  GLY   A N    1 
ATOM   1236 C CA   A GLY   A 1 46  ? 23.836 10.243  -0.676  0.40 10.91 ?  46  GLY   A CA   1 
ATOM   1237 C CA   B GLY   A 1 46  ? 23.526 9.865   -0.876  0.60 11.35 ?  46  GLY   A CA   1 
ATOM   1238 C C    A GLY   A 1 46  ? 22.337 10.083  -0.526  0.40 10.55 ?  46  GLY   A C    1 
ATOM   1239 C C    B GLY   A 1 46  ? 22.057 9.748   -0.508  0.60 11.64 ?  46  GLY   A C    1 
ATOM   1240 O O    A GLY   A 1 46  ? 21.633 11.068  -0.281  0.40 11.56 ?  46  GLY   A O    1 
ATOM   1241 O O    B GLY   A 1 46  ? 21.424 10.738  -0.122  0.60 13.02 ?  46  GLY   A O    1 
ATOM   1242 H H    A GLY   A 1 46  ? 24.805 8.585   -1.094  0.40 13.36 ?  46  GLY   A H    1 
ATOM   1243 H H    B GLY   A 1 46  ? 24.427 8.125   -1.095  0.60 12.61 ?  46  GLY   A H    1 
ATOM   1244 H HA2  A GLY   A 1 46  ? 24.126 10.960  -0.085  0.40 13.06 ?  46  GLY   A HA2  1 
ATOM   1245 H HA2  B GLY   A 1 46  ? 23.859 10.668  -0.449  0.60 13.59 ?  46  GLY   A HA2  1 
ATOM   1246 H HA3  A GLY   A 1 46  ? 24.005 10.530  -1.588  0.40 13.06 ?  46  GLY   A HA3  1 
ATOM   1247 H HA3  B GLY   A 1 46  ? 23.587 9.994   -1.837  0.60 13.59 ?  46  GLY   A HA3  1 
ATOM   1248 N N    A GLY   A 1 47  ? 21.828 8.866   -0.698  0.40 10.08 ?  47  GLY   A N    1 
ATOM   1249 N N    B GLY   A 1 47  ? 21.491 8.552   -0.629  0.60 11.55 ?  47  GLY   A N    1 
ATOM   1250 C CA   A GLY   A 1 47  ? 20.396 8.641   -0.689  0.40 10.64 ?  47  GLY   A CA   1 
ATOM   1251 C CA   B GLY   A 1 47  ? 20.060 8.380   -0.455  0.60 11.73 ?  47  GLY   A CA   1 
ATOM   1252 C C    A GLY   A 1 47  ? 20.078 7.187   -0.411  0.40 9.97  ?  47  GLY   A C    1 
ATOM   1253 C C    B GLY   A 1 47  ? 19.730 6.961   -0.046  0.60 10.60 ?  47  GLY   A C    1 
ATOM   1254 O O    A GLY   A 1 47  ? 20.965 6.358   -0.197  0.40 10.43 ?  47  GLY   A O    1 
ATOM   1255 O O    B GLY   A 1 47  ? 20.614 6.123   0.148   0.60 10.68 ?  47  GLY   A O    1 
ATOM   1256 H H    A GLY   A 1 47  ? 22.297 8.163   -0.830  0.40 12.07 ?  47  GLY   A H    1 
ATOM   1257 H H    B GLY   A 1 47  ? 21.917 7.817   -0.802  0.60 13.83 ?  47  GLY   A H    1 
ATOM   1258 H HA2  A GLY   A 1 47  ? 19.979 9.193   -0.006  0.40 12.74 ?  47  GLY   A HA2  1 
ATOM   1259 H HA2  B GLY   A 1 47  ? 19.741 8.980   0.234   0.60 14.05 ?  47  GLY   A HA2  1 
ATOM   1260 H HA3  A GLY   A 1 47  ? 20.027 8.885   -1.553  0.40 12.74 ?  47  GLY   A HA3  1 
ATOM   1261 H HA3  B GLY   A 1 47  ? 19.600 8.583   -1.285  0.60 14.05 ?  47  GLY   A HA3  1 
ATOM   1262 N N    A GLY   A 1 48  ? 18.786 6.880   -0.438  0.40 9.37  ?  48  GLY   A N    1 
ATOM   1263 N N    B GLY   A 1 48  ? 18.430 6.694   0.074   0.60 10.72 ?  48  GLY   A N    1 
ATOM   1264 C CA   A GLY   A 1 48  ? 18.324 5.557   -0.089  0.40 9.23  ?  48  GLY   A CA   1 
ATOM   1265 C CA   B GLY   A 1 48  ? 17.995 5.387   0.519   0.60 10.25 ?  48  GLY   A CA   1 
ATOM   1266 C C    A GLY   A 1 48  ? 18.688 5.203   1.339   0.40 9.17  ?  48  GLY   A C    1 
ATOM   1267 C C    B GLY   A 1 48  ? 18.540 5.047   1.896   0.60 9.81  ?  48  GLY   A C    1 
ATOM   1268 O O    A GLY   A 1 48  ? 18.832 6.068   2.211   0.40 9.49  ?  48  GLY   A O    1 
ATOM   1269 O O    B GLY   A 1 48  ? 18.723 5.913   2.762   0.60 10.11 ?  48  GLY   A O    1 
ATOM   1270 H H    A GLY   A 1 48  ? 18.169 7.424   -0.663  0.40 11.21 ?  48  GLY   A H    1 
ATOM   1271 H H    B GLY   A 1 48  ? 17.786 7.248   -0.094  0.60 12.83 ?  48  GLY   A H    1 
ATOM   1272 H HA2  A GLY   A 1 48  ? 17.365 5.519   -0.181  0.40 11.05 ?  48  GLY   A HA2  1 
ATOM   1273 H HA2  B GLY   A 1 48  ? 17.020 5.356   0.547   0.60 12.27 ?  48  GLY   A HA2  1 
ATOM   1274 H HA3  A GLY   A 1 48  ? 18.727 4.904   -0.683  0.40 11.05 ?  48  GLY   A HA3  1 
ATOM   1275 H HA3  B GLY   A 1 48  ? 18.299 4.711   -0.103  0.60 12.27 ?  48  GLY   A HA3  1 
ATOM   1276 N N    A VAL   A 1 49  ? 18.846 3.900   1.583   0.40 9.69  ?  49  VAL   A N    1 
ATOM   1277 N N    B VAL   A 1 49  ? 18.781 3.750   2.106   0.60 9.07  ?  49  VAL   A N    1 
ATOM   1278 C CA   A VAL   A 1 49  ? 19.245 3.434   2.908   0.40 9.77  ?  49  VAL   A CA   1 
ATOM   1279 C CA   B VAL   A 1 49  ? 19.348 3.277   3.367   0.60 9.75  ?  49  VAL   A CA   1 
ATOM   1280 C C    A VAL   A 1 49  ? 20.576 4.054   3.323   0.40 9.57  ?  49  VAL   A C    1 
ATOM   1281 C C    B VAL   A 1 49  ? 20.667 3.985   3.671   0.60 9.41  ?  49  VAL   A C    1 
ATOM   1282 O O    A VAL   A 1 49  ? 20.743 4.475   4.473   0.40 10.02 ?  49  VAL   A O    1 
ATOM   1283 O O    B VAL   A 1 49  ? 20.919 4.402   4.808   0.60 9.45  ?  49  VAL   A O    1 
ATOM   1284 C CB   A VAL   A 1 49  ? 19.289 1.894   2.946   0.40 10.41 ?  49  VAL   A CB   1 
ATOM   1285 C CB   B VAL   A 1 49  ? 19.522 1.748   3.326   0.60 10.94 ?  49  VAL   A CB   1 
ATOM   1286 C CG1  A VAL   A 1 49  ? 19.929 1.410   4.242   0.40 10.85 ?  49  VAL   A CG1  1 
ATOM   1287 C CG1  B VAL   A 1 49  ? 20.410 1.286   4.463   0.60 10.82 ?  49  VAL   A CG1  1 
ATOM   1288 C CG2  A VAL   A 1 49  ? 17.887 1.317   2.786   0.40 10.65 ?  49  VAL   A CG2  1 
ATOM   1289 C CG2  B VAL   A 1 49  ? 18.162 1.054   3.379   0.60 12.39 ?  49  VAL   A CG2  1 
ATOM   1290 H H    A VAL   A 1 49  ? 18.727 3.277   1.006   0.40 11.60 ?  49  VAL   A H    1 
ATOM   1291 H H    B VAL   A 1 49  ? 18.618 3.125   1.538   0.60 10.86 ?  49  VAL   A H    1 
ATOM   1292 H HA   A VAL   A 1 49  ? 18.577 3.721   3.549   0.40 11.70 ?  49  VAL   A HA   1 
ATOM   1293 H HA   B VAL   A 1 49  ? 18.731 3.481   4.089   0.60 11.67 ?  49  VAL   A HA   1 
ATOM   1294 H HB   A VAL   A 1 49  ? 19.832 1.576   2.210   0.40 12.46 ?  49  VAL   A HB   1 
ATOM   1295 H HB   B VAL   A 1 49  ? 19.953 1.503   2.492   0.60 13.10 ?  49  VAL   A HB   1 
ATOM   1296 H HG11 A VAL   A 1 49  ? 19.714 0.472   4.367   0.40 13.00 ?  49  VAL   A HG11 1 
ATOM   1297 H HG11 B VAL   A 1 49  ? 20.276 0.336   4.597   0.60 12.96 ?  49  VAL   A HG11 1 
ATOM   1298 H HG12 A VAL   A 1 49  ? 20.890 1.523   4.188   0.40 13.00 ?  49  VAL   A HG12 1 
ATOM   1299 H HG12 B VAL   A 1 49  ? 21.338 1.458   4.232   0.60 12.96 ?  49  VAL   A HG12 1 
ATOM   1300 H HG13 A VAL   A 1 49  ? 19.574 1.928   4.983   0.40 13.00 ?  49  VAL   A HG13 1 
ATOM   1301 H HG13 B VAL   A 1 49  ? 20.171 1.771   5.267   0.60 12.96 ?  49  VAL   A HG13 1 
ATOM   1302 H HG21 A VAL   A 1 49  ? 17.939 0.349   2.816   0.40 12.75 ?  49  VAL   A HG21 1 
ATOM   1303 H HG21 B VAL   A 1 49  ? 18.296 0.093   3.344   0.60 14.84 ?  49  VAL   A HG21 1 
ATOM   1304 H HG22 A VAL   A 1 49  ? 17.327 1.641   3.509   0.40 12.75 ?  49  VAL   A HG22 1 
ATOM   1305 H HG22 B VAL   A 1 49  ? 17.717 1.294   4.207   0.60 14.84 ?  49  VAL   A HG22 1 
ATOM   1306 H HG23 A VAL   A 1 49  ? 17.525 1.602   1.933   0.40 12.75 ?  49  VAL   A HG23 1 
ATOM   1307 H HG23 B VAL   A 1 49  ? 17.631 1.342   2.622   0.60 14.84 ?  49  VAL   A HG23 1 
ATOM   1308 N N    A ALA   A 1 50  ? 21.545 4.111   2.404   0.40 9.52  ?  50  ALA   A N    1 
ATOM   1309 N N    B ALA   A 1 50  ? 21.543 4.100   2.668   0.60 9.15  ?  50  ALA   A N    1 
ATOM   1310 C CA   A ALA   A 1 50  ? 22.861 4.647   2.747   0.40 9.80  ?  50  ALA   A CA   1 
ATOM   1311 C CA   B ALA   A 1 50  ? 22.864 4.681   2.902   0.60 9.37  ?  50  ALA   A CA   1 
ATOM   1312 C C    A ALA   A 1 50  ? 22.780 6.106   3.179   0.40 9.75  ?  50  ALA   A C    1 
ATOM   1313 C C    B ALA   A 1 50  ? 22.756 6.132   3.350   0.60 9.40  ?  50  ALA   A C    1 
ATOM   1314 O O    A ALA   A 1 50  ? 23.426 6.508   4.154   0.40 10.22 ?  50  ALA   A O    1 
ATOM   1315 O O    B ALA   A 1 50  ? 23.404 6.546   4.320   0.60 9.44  ?  50  ALA   A O    1 
ATOM   1316 C CB   A ALA   A 1 50  ? 23.817 4.501   1.564   0.40 9.84  ?  50  ALA   A CB   1 
ATOM   1317 C CB   B ALA   A 1 50  ? 23.718 4.583   1.638   0.60 9.25  ?  50  ALA   A CB   1 
ATOM   1318 H H    A ALA   A 1 50  ? 21.470 3.844   1.593   0.40 11.40 ?  50  ALA   A H    1 
ATOM   1319 H H    B ALA   A 1 50  ? 21.393 3.864   1.855   0.60 10.96 ?  50  ALA   A H    1 
ATOM   1320 H HA   A ALA   A 1 50  ? 23.224 4.147   3.492   0.40 11.73 ?  50  ALA   A HA   1 
ATOM   1321 H HA   B ALA   A 1 50  ? 23.306 4.191   3.606   0.60 11.22 ?  50  ALA   A HA   1 
ATOM   1322 H HB1  A ALA   A 1 50  ? 24.682 4.865   1.811   0.40 11.78 ?  50  ALA   A HB1  1 
ATOM   1323 H HB1  B ALA   A 1 50  ? 24.588 4.970   1.813   0.60 11.08 ?  50  ALA   A HB1  1 
ATOM   1324 H HB2  A ALA   A 1 50  ? 23.902 3.561   1.345   0.40 11.78 ?  50  ALA   A HB2  1 
ATOM   1325 H HB2  B ALA   A 1 50  ? 23.813 3.647   1.397   0.60 11.08 ?  50  ALA   A HB2  1 
ATOM   1326 H HB3  A ALA   A 1 50  ? 23.457 4.988   0.806   0.40 11.78 ?  50  ALA   A HB3  1 
ATOM   1327 H HB3  B ALA   A 1 50  ? 23.278 5.065   0.919   0.60 11.08 ?  50  ALA   A HB3  1 
ATOM   1328 N N    A GLY   A 1 51  ? 22.003 6.921   2.462   0.40 9.94  ?  51  GLY   A N    1 
ATOM   1329 N N    B GLY   A 1 51  ? 21.948 6.929   2.645   0.60 9.99  ?  51  GLY   A N    1 
ATOM   1330 C CA   A GLY   A 1 51  ? 21.870 8.313   2.853   0.40 10.17 ?  51  GLY   A CA   1 
ATOM   1331 C CA   B GLY   A 1 51  ? 21.772 8.312   3.049   0.60 10.62 ?  51  GLY   A CA   1 
ATOM   1332 C C    A GLY   A 1 51  ? 21.263 8.472   4.230   0.40 9.94  ?  51  GLY   A C    1 
ATOM   1333 C C    B GLY   A 1 51  ? 21.199 8.422   4.445   0.60 11.03 ?  51  GLY   A C    1 
ATOM   1334 O O    A GLY   A 1 51  ? 21.618 9.397   4.966   0.40 10.04 ?  51  GLY   A O    1 
ATOM   1335 O O    B GLY   A 1 51  ? 21.631 9.260   5.242   0.60 11.73 ?  51  GLY   A O    1 
ATOM   1336 H H    A GLY   A 1 51  ? 21.557 6.696   1.763   0.40 11.90 ?  51  GLY   A H    1 
ATOM   1337 H H    B GLY   A 1 51  ? 21.500 6.694   1.947   0.60 11.96 ?  51  GLY   A H    1 
ATOM   1338 H HA2  A GLY   A 1 51  ? 22.741 8.735   2.858   0.40 12.17 ?  51  GLY   A HA2  1 
ATOM   1339 H HA2  B GLY   A 1 51  ? 22.626 8.769   3.029   0.60 12.71 ?  51  GLY   A HA2  1 
ATOM   1340 H HA3  A GLY   A 1 51  ? 21.303 8.780   2.219   0.40 12.17 ?  51  GLY   A HA3  1 
ATOM   1341 H HA3  B GLY   A 1 51  ? 21.169 8.758   2.428   0.60 12.71 ?  51  GLY   A HA3  1 
ATOM   1342 N N    A ALA   A 1 52  ? 20.341 7.578   4.595   0.40 10.29 ?  52  ALA   A N    1 
ATOM   1343 N N    B ALA   A 1 52  ? 20.220 7.570   4.763   0.60 11.11 ?  52  ALA   A N    1 
ATOM   1344 C CA   A ALA   A 1 52  ? 19.693 7.651   5.899   0.40 10.73 ?  52  ALA   A CA   1 
ATOM   1345 C CA   B ALA   A 1 52  ? 19.606 7.605   6.084   0.60 11.79 ?  52  ALA   A CA   1 
ATOM   1346 C C    A ALA   A 1 52  ? 20.641 7.232   7.020   0.40 10.57 ?  52  ALA   A C    1 
ATOM   1347 C C    B ALA   A 1 52  ? 20.586 7.176   7.172   0.60 11.12 ?  52  ALA   A C    1 
ATOM   1348 O O    A ALA   A 1 52  ? 20.742 7.916   8.045   0.40 11.08 ?  52  ALA   A O    1 
ATOM   1349 O O    B ALA   A 1 52  ? 20.657 7.810   8.232   0.60 11.71 ?  52  ALA   A O    1 
ATOM   1350 C CB   A ALA   A 1 52  ? 18.429 6.789   5.895   0.40 11.85 ?  52  ALA   A CB   1 
ATOM   1351 C CB   B ALA   A 1 52  ? 18.349 6.736   6.101   0.60 13.39 ?  52  ALA   A CB   1 
ATOM   1352 H H    A ALA   A 1 52  ? 20.086 6.916   4.111   0.40 12.33 ?  52  ALA   A H    1 
ATOM   1353 H H    B ALA   A 1 52  ? 19.911 6.954   4.237   0.60 13.31 ?  52  ALA   A H    1 
ATOM   1354 H HA   A ALA   A 1 52  ? 19.428 8.564   6.068   0.40 12.85 ?  52  ALA   A HA   1 
ATOM   1355 H HA   B ALA   A 1 52  ? 19.341 8.517   6.267   0.60 14.12 ?  52  ALA   A HA   1 
ATOM   1356 H HB1  A ALA   A 1 52  ? 17.997 6.851   6.763   0.40 14.19 ?  52  ALA   A HB1  1 
ATOM   1357 H HB1  B ALA   A 1 52  ? 17.948 6.786   6.983   0.60 16.05 ?  52  ALA   A HB1  1 
ATOM   1358 H HB2  A ALA   A 1 52  ? 17.826 7.118   5.207   0.40 14.19 ?  52  ALA   A HB2  1 
ATOM   1359 H HB2  B ALA   A 1 52  ? 17.726 7.074   5.437   0.60 16.05 ?  52  ALA   A HB2  1 
ATOM   1360 H HB3  A ALA   A 1 52  ? 18.668 5.868   5.710   0.40 14.19 ?  52  ALA   A HB3  1 
ATOM   1361 H HB3  B ALA   A 1 52  ? 18.591 5.823   5.895   0.60 16.05 ?  52  ALA   A HB3  1 
ATOM   1362 N N    A LEU   A 1 53  ? 21.344 6.107   6.848   0.40 10.49 ?  53  LEU   A N    1 
ATOM   1363 N N    B LEU   A 1 53  ? 21.340 6.097   6.943   0.60 10.54 ?  53  LEU   A N    1 
ATOM   1364 C CA   A LEU   A 1 53  ? 22.273 5.654   7.880   0.40 10.68 ?  53  LEU   A CA   1 
ATOM   1365 C CA   B LEU   A 1 53  ? 22.349 5.698   7.921   0.60 10.42 ?  53  LEU   A CA   1 
ATOM   1366 C C    A LEU   A 1 53  ? 23.376 6.675   8.098   0.40 10.60 ?  53  LEU   A C    1 
ATOM   1367 C C    B LEU   A 1 53  ? 23.377 6.807   8.102   0.60 9.89  ?  53  LEU   A C    1 
ATOM   1368 O O    A LEU   A 1 53  ? 23.776 6.938   9.238   0.40 11.34 ?  53  LEU   A O    1 
ATOM   1369 O O    B LEU   A 1 53  ? 23.687 7.208   9.230   0.60 10.48 ?  53  LEU   A O    1 
ATOM   1370 C CB   A LEU   A 1 53  ? 22.878 4.301   7.496   0.40 10.95 ?  53  LEU   A CB   1 
ATOM   1371 C CB   B LEU   A 1 53  ? 23.035 4.391   7.501   0.60 10.58 ?  53  LEU   A CB   1 
ATOM   1372 C CG   A LEU   A 1 53  ? 21.900 3.124   7.467   0.40 11.04 ?  53  LEU   A CG   1 
ATOM   1373 C CG   B LEU   A 1 53  ? 22.246 3.077   7.609   0.60 10.93 ?  53  LEU   A CG   1 
ATOM   1374 C CD1  A LEU   A 1 53  ? 22.561 1.890   6.868   0.40 10.89 ?  53  LEU   A CD1  1 
ATOM   1375 C CD1  B LEU   A 1 53  ? 23.045 1.936   6.987   0.60 11.02 ?  53  LEU   A CD1  1 
ATOM   1376 C CD2  A LEU   A 1 53  ? 21.382 2.825   8.863   0.40 11.75 ?  53  LEU   A CD2  1 
ATOM   1377 C CD2  B LEU   A 1 53  ? 21.886 2.729   9.044   0.60 11.77 ?  53  LEU   A CD2  1 
ATOM   1378 H H    A LEU   A 1 53  ? 21.307 5.601   6.157   0.40 12.56 ?  53  LEU   A H    1 
ATOM   1379 H H    B LEU   A 1 53  ? 21.279 5.586   6.248   0.60 12.62 ?  53  LEU   A H    1 
ATOM   1380 H HA   A LEU   A 1 53  ? 21.801 5.548   8.721   0.40 12.79 ?  53  LEU   A HA   1 
ATOM   1381 H HA   B LEU   A 1 53  ? 21.912 5.552   8.772   0.60 12.47 ?  53  LEU   A HA   1 
ATOM   1382 H HB2  A LEU   A 1 53  ? 23.266 4.379   6.610   0.40 13.11 ?  53  LEU   A HB2  1 
ATOM   1383 H HB2  B LEU   A 1 53  ? 23.300 4.478   6.573   0.60 12.67 ?  53  LEU   A HB2  1 
ATOM   1384 H HB3  A LEU   A 1 53  ? 23.576 4.081   8.134   0.40 13.11 ?  53  LEU   A HB3  1 
ATOM   1385 H HB3  B LEU   A 1 53  ? 23.825 4.285   8.049   0.60 12.67 ?  53  LEU   A HB3  1 
ATOM   1386 H HG   A LEU   A 1 53  ? 21.143 3.361   6.908   0.40 13.23 ?  53  LEU   A HG   1 
ATOM   1387 H HG   B LEU   A 1 53  ? 21.422 3.160   7.106   0.60 13.09 ?  53  LEU   A HG   1 
ATOM   1388 H HD11 A LEU   A 1 53  ? 21.919 1.164   6.858   0.40 13.04 ?  53  LEU   A HD11 1 
ATOM   1389 H HD11 B LEU   A 1 53  ? 22.537 1.114   7.064   0.60 13.19 ?  53  LEU   A HD11 1 
ATOM   1390 H HD12 A LEU   A 1 53  ? 22.845 2.093   5.962   0.40 13.04 ?  53  LEU   A HD12 1 
ATOM   1391 H HD12 B LEU   A 1 53  ? 23.209 2.138   6.052   0.60 13.19 ?  53  LEU   A HD12 1 
ATOM   1392 H HD13 A LEU   A 1 53  ? 23.328 1.650   7.409   0.40 13.04 ?  53  LEU   A HD13 1 
ATOM   1393 H HD13 B LEU   A 1 53  ? 23.889 1.849   7.459   0.60 13.19 ?  53  LEU   A HD13 1 
ATOM   1394 H HD21 A LEU   A 1 53  ? 20.866 2.006   8.838   0.40 14.08 ?  53  LEU   A HD21 1 
ATOM   1395 H HD21 B LEU   A 1 53  ? 21.256 1.990   9.042   0.60 14.10 ?  53  LEU   A HD21 1 
ATOM   1396 H HD22 A LEU   A 1 53  ? 22.138 2.723   9.463   0.40 14.08 ?  53  LEU   A HD22 1 
ATOM   1397 H HD22 B LEU   A 1 53  ? 22.690 2.478   9.521   0.60 14.10 ?  53  LEU   A HD22 1 
ATOM   1398 H HD23 A LEU   A 1 53  ? 20.824 3.561   9.159   0.40 14.08 ?  53  LEU   A HD23 1 
ATOM   1399 H HD23 B LEU   A 1 53  ? 21.480 3.504   9.464   0.60 14.10 ?  53  LEU   A HD23 1 
ATOM   1400 N N    A ASN   A 1 54  ? 23.878 7.266   7.016   0.40 10.08 ?  54  ASN   A N    1 
ATOM   1401 N N    B ASN   A 1 54  ? 23.903 7.330   6.994   0.60 9.58  ?  54  ASN   A N    1 
ATOM   1402 C CA   A ASN   A 1 54  ? 24.942 8.251   7.163   0.40 9.88  ?  54  ASN   A CA   1 
ATOM   1403 C CA   B ASN   A 1 54  ? 24.945 8.342   7.110   0.60 9.82  ?  54  ASN   A CA   1 
ATOM   1404 C C    A ASN   A 1 54  ? 24.438 9.492   7.895   0.40 10.23 ?  54  ASN   A C    1 
ATOM   1405 C C    B ASN   A 1 54  ? 24.438 9.584   7.837   0.60 10.39 ?  54  ASN   A C    1 
ATOM   1406 O O    A ASN   A 1 54  ? 25.108 10.010  8.798   0.40 10.52 ?  54  ASN   A O    1 
ATOM   1407 O O    B ASN   A 1 54  ? 25.148 10.159  8.674   0.60 10.74 ?  54  ASN   A O    1 
ATOM   1408 C CB   A ASN   A 1 54  ? 25.501 8.621   5.797   0.40 9.73  ?  54  ASN   A CB   1 
ATOM   1409 C CB   B ASN   A 1 54  ? 25.497 8.716   5.742   0.60 10.14 ?  54  ASN   A CB   1 
ATOM   1410 C CG   A ASN   A 1 54  ? 26.565 9.683   5.897   0.40 9.52  ?  54  ASN   A CG   1 
ATOM   1411 C CG   B ASN   A 1 54  ? 26.491 9.846   5.839   0.60 10.25 ?  54  ASN   A CG   1 
ATOM   1412 O OD1  A ASN   A 1 54  ? 27.513 9.552   6.673   0.40 9.15  ?  54  ASN   A OD1  1 
ATOM   1413 O OD1  B ASN   A 1 54  ? 27.539 9.705   6.472   0.60 10.69 ?  54  ASN   A OD1  1 
ATOM   1414 N ND2  A ASN   A 1 54  ? 26.397 10.763  5.150   0.40 10.12 ?  54  ASN   A ND2  1 
ATOM   1415 N ND2  B ASN   A 1 54  ? 26.158 10.988  5.257   0.60 10.16 ?  54  ASN   A ND2  1 
ATOM   1416 H H    A ASN   A 1 54  ? 23.619 7.124   6.207   0.40 12.07 ?  54  ASN   A H    1 
ATOM   1417 H H    B ASN   A 1 54  ? 23.675 7.122   6.190   0.60 11.48 ?  54  ASN   A H    1 
ATOM   1418 H HA   A ASN   A 1 54  ? 25.660 7.862   7.685   0.40 11.83 ?  54  ASN   A HA   1 
ATOM   1419 H HA   B ASN   A 1 54  ? 25.668 7.974   7.634   0.60 11.75 ?  54  ASN   A HA   1 
ATOM   1420 H HB2  A ASN   A 1 54  ? 25.887 7.824   5.385   0.40 11.65 ?  54  ASN   A HB2  1 
ATOM   1421 H HB2  B ASN   A 1 54  ? 25.941 7.940   5.361   0.60 12.14 ?  54  ASN   A HB2  1 
ATOM   1422 H HB3  A ASN   A 1 54  ? 24.783 8.960   5.239   0.40 11.65 ?  54  ASN   A HB3  1 
ATOM   1423 H HB3  B ASN   A 1 54  ? 24.764 8.994   5.169   0.60 12.14 ?  54  ASN   A HB3  1 
ATOM   1424 H HD21 A ASN   A 1 54  ? 26.979 11.393  5.176   0.40 12.11 ?  54  ASN   A HD21 1 
ATOM   1425 H HD21 B ASN   A 1 54  ? 26.697 11.655  5.293   0.60 12.16 ?  54  ASN   A HD21 1 
ATOM   1426 H HD22 A ASN   A 1 54  ? 25.712 10.827  4.636   0.40 12.11 ?  54  ASN   A HD22 1 
ATOM   1427 H HD22 B ASN   A 1 54  ? 25.416 11.052  4.830   0.60 12.16 ?  54  ASN   A HD22 1 
ATOM   1428 N N    A LYS   A 1 55  ? 23.251 9.982   7.515   0.40 10.46 ?  55  LYS   A N    1 
ATOM   1429 N N    B LYS   A 1 55  ? 23.214 10.024  7.522   0.60 10.77 ?  55  LYS   A N    1 
ATOM   1430 C CA   A LYS   A 1 55  ? 22.659 11.135  8.187   0.40 10.81 ?  55  LYS   A CA   1 
ATOM   1431 C CA   B LYS   A 1 55  ? 22.650 11.181  8.209   0.60 11.50 ?  55  LYS   A CA   1 
ATOM   1432 C C    A LYS   A 1 55  ? 22.579 10.902  9.690   0.40 11.18 ?  55  LYS   A C    1 
ATOM   1433 C C    B LYS   A 1 55  ? 22.550 10.920  9.707   0.60 11.52 ?  55  LYS   A C    1 
ATOM   1434 O O    A LYS   A 1 55  ? 22.883 11.797  10.487  0.40 11.73 ?  55  LYS   A O    1 
ATOM   1435 O O    B LYS   A 1 55  ? 22.816 11.813  10.520  0.60 12.17 ?  55  LYS   A O    1 
ATOM   1436 C CB   A LYS   A 1 55  ? 21.272 11.411  7.596   0.40 10.93 ?  55  LYS   A CB   1 
ATOM   1437 C CB   B LYS   A 1 55  ? 21.288 11.531  7.604   0.60 12.47 ?  55  LYS   A CB   1 
ATOM   1438 C CG   A LYS   A 1 55  ? 20.447 12.473  8.323   0.40 10.77 ?  55  LYS   A CG   1 
ATOM   1439 C CG   B LYS   A 1 55  ? 20.686 12.847  8.085   0.60 13.07 ?  55  LYS   A CG   1 
ATOM   1440 C CD   A LYS   A 1 55  ? 19.110 12.710  7.611   0.40 11.01 ?  55  LYS   A CD   1 
ATOM   1441 C CD   B LYS   A 1 55  ? 19.348 13.136  7.399   0.60 13.74 ?  55  LYS   A CD   1 
ATOM   1442 C CE   A LYS   A 1 55  ? 18.306 13.841  8.240   0.40 11.16 ?  55  LYS   A CE   1 
ATOM   1443 C CE   B LYS   A 1 55  ? 18.671 14.377  7.970   0.60 15.09 ?  55  LYS   A CE   1 
ATOM   1444 N NZ   A LYS   A 1 55  ? 17.010 14.068  7.532   0.40 10.99 ?  55  LYS   A NZ   1 
ATOM   1445 N NZ   B LYS   A 1 55  ? 17.377 14.688  7.297   0.60 16.36 ?  55  LYS   A NZ   1 
ATOM   1446 H H    A LYS   A 1 55  ? 22.772 9.660   6.875   0.40 12.53 ?  55  LYS   A H    1 
ATOM   1447 H H    B LYS   A 1 55  ? 22.697 9.677   6.922   0.60 12.90 ?  55  LYS   A H    1 
ATOM   1448 H HA   A LYS   A 1 55  ? 23.214 11.916  8.030   0.40 12.95 ?  55  LYS   A HA   1 
ATOM   1449 H HA   B LYS   A 1 55  ? 23.238 11.941  8.075   0.60 13.78 ?  55  LYS   A HA   1 
ATOM   1450 H HB2  A LYS   A 1 55  ? 21.382 11.709  6.678   0.40 13.09 ?  55  LYS   A HB2  1 
ATOM   1451 H HB2  B LYS   A 1 55  ? 21.381 11.591  6.640   0.60 14.94 ?  55  LYS   A HB2  1 
ATOM   1452 H HB3  A LYS   A 1 55  ? 20.763 10.585  7.607   0.40 13.09 ?  55  LYS   A HB3  1 
ATOM   1453 H HB3  B LYS   A 1 55  ? 20.659 10.829  7.827   0.60 14.94 ?  55  LYS   A HB3  1 
ATOM   1454 H HG2  A LYS   A 1 55  ? 20.260 12.168  9.227   0.40 12.90 ?  55  LYS   A HG2  1 
ATOM   1455 H HG2  B LYS   A 1 55  ? 20.534 12.802  9.042   0.60 15.66 ?  55  LYS   A HG2  1 
ATOM   1456 H HG3  A LYS   A 1 55  ? 20.939 13.304  8.341   0.40 12.90 ?  55  LYS   A HG3  1 
ATOM   1457 H HG3  B LYS   A 1 55  ? 21.298 13.575  7.878   0.60 15.66 ?  55  LYS   A HG3  1 
ATOM   1458 H HD2  A LYS   A 1 55  ? 19.279 12.936  6.685   0.40 13.19 ?  55  LYS   A HD2  1 
ATOM   1459 H HD2  B LYS   A 1 55  ? 19.503 13.285  6.452   0.60 16.46 ?  55  LYS   A HD2  1 
ATOM   1460 H HD3  A LYS   A 1 55  ? 18.576 11.897  7.661   0.40 13.19 ?  55  LYS   A HD3  1 
ATOM   1461 H HD3  B LYS   A 1 55  ? 18.756 12.381  7.527   0.60 16.46 ?  55  LYS   A HD3  1 
ATOM   1462 H HE2  A LYS   A 1 55  ? 18.113 13.617  9.165   0.40 13.36 ?  55  LYS   A HE2  1 
ATOM   1463 H HE2  B LYS   A 1 55  ? 18.493 14.235  8.913   0.60 18.08 ?  55  LYS   A HE2  1 
ATOM   1464 H HE3  A LYS   A 1 55  ? 18.825 14.658  8.196   0.40 13.36 ?  55  LYS   A HE3  1 
ATOM   1465 H HE3  B LYS   A 1 55  ? 19.260 15.142  7.857   0.60 18.08 ?  55  LYS   A HE3  1 
ATOM   1466 H HZ1  A LYS   A 1 55  ? 16.564 14.729  7.922   0.40 13.16 ?  55  LYS   A HZ1  1 
ATOM   1467 H HZ1  B LYS   A 1 55  ? 16.888 15.226  7.811   0.60 19.61 ?  55  LYS   A HZ1  1 
ATOM   1468 H HZ2  A LYS   A 1 55  ? 17.163 14.280  6.682   0.40 13.16 ?  55  LYS   A HZ2  1 
ATOM   1469 H HZ2  B LYS   A 1 55  ? 17.528 15.095  6.519   0.60 19.61 ?  55  LYS   A HZ2  1 
ATOM   1470 H HZ3  A LYS   A 1 55  ? 16.516 13.327  7.561   0.40 13.16 ?  55  LYS   A HZ3  1 
ATOM   1471 H HZ3  B LYS   A 1 55  ? 16.922 13.938  7.150   0.60 19.61 ?  55  LYS   A HZ3  1 
ATOM   1472 N N    . ALA   A 1 56  ? 22.182 9.694   10.092  1.00 11.89 ?  56  ALA   A N    1 
ATOM   1473 C CA   . ALA   A 1 56  ? 22.072 9.359   11.508  1.00 12.85 ?  56  ALA   A CA   1 
ATOM   1474 C C    . ALA   A 1 56  ? 23.419 9.383   12.227  1.00 12.60 ?  56  ALA   A C    1 
ATOM   1475 O O    . ALA   A 1 56  ? 23.445 9.568   13.448  1.00 14.15 ?  56  ALA   A O    1 
ATOM   1476 C CB   . ALA   A 1 56  ? 21.389 7.999   11.678  1.00 13.74 ?  56  ALA   A CB   1 
ATOM   1477 H H    A ALA   A 1 56  ? 21.974 9.052   9.560   0.40 14.24 ?  56  ALA   A H    1 
ATOM   1478 H H    B ALA   A 1 56  ? 21.988 9.052   9.555   0.60 14.24 ?  56  ALA   A H    1 
ATOM   1479 H HA   . ALA   A 1 56  ? 21.508 10.020  11.932  1.00 15.39 ?  56  ALA   A HA   1 
ATOM   1480 H HB1  . ALA   A 1 56  ? 21.313 7.802   12.624  1.00 16.47 ?  56  ALA   A HB1  1 
ATOM   1481 H HB2  . ALA   A 1 56  ? 20.505 8.045   11.277  1.00 16.47 ?  56  ALA   A HB2  1 
ATOM   1482 H HB3  . ALA   A 1 56  ? 21.918 7.320   11.235  1.00 16.47 ?  56  ALA   A HB3  1 
ATOM   1483 N N    . THR   A 1 57  ? 24.532 9.208   11.507  1.00 11.53 ?  57  THR   A N    1 
ATOM   1484 C CA   . THR   A 1 57  ? 25.870 9.336   12.086  1.00 11.51 ?  57  THR   A CA   1 
ATOM   1485 C C    . THR   A 1 57  ? 26.416 10.758  12.015  1.00 12.07 ?  57  THR   A C    1 
ATOM   1486 O O    . THR   A 1 57  ? 27.599 10.972  12.313  1.00 12.61 ?  57  THR   A O    1 
ATOM   1487 C CB   . THR   A 1 57  ? 26.879 8.389   11.410  1.00 11.59 ?  57  THR   A CB   1 
ATOM   1488 O OG1  . THR   A 1 57  ? 27.257 8.894   10.121  1.00 11.04 ?  57  THR   A OG1  1 
ATOM   1489 C CG2  . THR   A 1 57  ? 26.334 6.974   11.286  1.00 11.57 ?  57  THR   A CG2  1 
ATOM   1490 H H    . THR   A 1 57  ? 24.535 8.999   10.667  1.00 13.81 ?  57  THR   A H    1 
ATOM   1491 H HA   . THR   A 1 57  ? 25.817 9.079   13.023  1.00 13.79 ?  57  THR   A HA   1 
ATOM   1492 H HB   . THR   A 1 57  ? 27.671 8.337   11.972  1.00 13.88 ?  57  THR   A HB   1 
ATOM   1493 H HG1  . THR   A 1 57  ? 26.580 8.957   9.633   1.00 13.23 ?  57  THR   A HG1  1 
ATOM   1494 H HG21 . THR   A 1 57  ? 26.989 6.399   10.865  1.00 13.86 ?  57  THR   A HG21 1 
ATOM   1495 H HG22 . THR   A 1 57  ? 26.120 6.619   12.164  1.00 13.86 ?  57  THR   A HG22 1 
ATOM   1496 H HG23 . THR   A 1 57  ? 25.527 6.975   10.748  1.00 13.86 ?  57  THR   A HG23 1 
ATOM   1497 N N    . ASN   A 1 58  ? 25.597 11.730  11.615  1.00 12.40 ?  58  ASN   A N    1 
ATOM   1498 C CA   . ASN   A 1 58  ? 26.054 13.113  11.522  1.00 13.45 ?  58  ASN   A CA   1 
ATOM   1499 C C    . ASN   A 1 58  ? 27.191 13.249  10.505  1.00 12.19 ?  58  ASN   A C    1 
ATOM   1500 O O    . ASN   A 1 58  ? 28.085 14.082  10.662  1.00 12.88 ?  58  ASN   A O    1 
ATOM   1501 C CB   . ASN   A 1 58  ? 26.447 13.648  12.915  1.00 15.81 ?  58  ASN   A CB   1 
ATOM   1502 C CG   . ASN   A 1 58  ? 26.844 15.111  12.912  1.00 18.88 ?  58  ASN   A CG   1 
ATOM   1503 O OD1  . ASN   A 1 58  ? 26.202 15.928  12.265  1.00 20.01 ?  58  ASN   A OD1  1 
ATOM   1504 N ND2  . ASN   A 1 58  ? 27.897 15.452  13.658  1.00 19.79 ?  58  ASN   A ND2  1 
ATOM   1505 H H    . ASN   A 1 58  ? 24.774 11.606  11.386  1.00 14.86 ?  58  ASN   A H    1 
ATOM   1506 H HA   . ASN   A 1 58  ? 25.312 13.648  11.205  1.00 16.12 ?  58  ASN   A HA   1 
ATOM   1507 H HB2  . ASN   A 1 58  ? 25.686 13.541  13.515  1.00 18.94 ?  58  ASN   A HB2  1 
ATOM   1508 H HB3  . ASN   A 1 58  ? 27.198 13.140  13.250  1.00 18.94 ?  58  ASN   A HB3  1 
ATOM   1509 H HD21 . ASN   A 1 58  ? 28.151 16.273  13.691  1.00 23.72 ?  58  ASN   A HD21 1 
ATOM   1510 H HD22 . ASN   A 1 58  ? 28.316 14.851  14.104  1.00 23.72 ?  58  ASN   A HD22 1 
ATOM   1511 N N    . ASN   A 1 59  ? 27.169 12.432  9.449   1.00 11.25 ?  59  ASN   A N    1 
ATOM   1512 C CA   . ASN   A 1 59  ? 28.139 12.423  8.346   1.00 11.02 ?  59  ASN   A CA   1 
ATOM   1513 C C    . ASN   A 1 59  ? 29.459 11.744  8.722   1.00 10.55 ?  59  ASN   A C    1 
ATOM   1514 O O    . ASN   A 1 59  ? 30.376 11.710  7.895   1.00 10.65 ?  59  ASN   A O    1 
ATOM   1515 C CB   . ASN   A 1 59  ? 28.410 13.813  7.746   1.00 11.14 ?  59  ASN   A CB   1 
ATOM   1516 C CG   . ASN   A 1 59  ? 28.768 13.756  6.276   1.00 11.43 ?  59  ASN   A CG   1 
ATOM   1517 O OD1  . ASN   A 1 59  ? 28.059 13.144  5.477   1.00 11.81 ?  59  ASN   A OD1  1 
ATOM   1518 N ND2  . ASN   A 1 59  ? 29.852 14.425  5.902   1.00 12.33 ?  59  ASN   A ND2  1 
ATOM   1519 H H    . ASN   A 1 59  ? 26.555 11.838  9.335   1.00 13.48 ?  59  ASN   A H    1 
ATOM   1520 H HA   . ASN   A 1 59  ? 27.757 11.894  7.632   1.00 13.19 ?  59  ASN   A HA   1 
ATOM   1521 H HB2  . ASN   A 1 59  ? 27.618 14.364  7.835   1.00 13.35 ?  59  ASN   A HB2  1 
ATOM   1522 H HB3  . ASN   A 1 59  ? 29.154 14.226  8.214   1.00 13.35 ?  59  ASN   A HB3  1 
ATOM   1523 H HD21 . ASN   A 1 59  ? 30.103 14.422  5.078   1.00 14.77 ?  59  ASN   A HD21 1 
ATOM   1524 H HD22 . ASN   A 1 59  ? 30.332 14.840  6.489   1.00 14.77 ?  59  ASN   A HD22 1 
ATOM   1525 N N    . ALA   A 1 60  ? 29.594 11.200  9.931   1.00 10.43 ?  60  ALA   A N    1 
ATOM   1526 C CA   . ALA   A 1 60  ? 30.837 10.515  10.276  1.00 10.89 ?  60  ALA   A CA   1 
ATOM   1527 C C    . ALA   A 1 60  ? 31.063 9.280   9.408   1.00 10.88 ?  60  ALA   A C    1 
ATOM   1528 O O    . ALA   A 1 60  ? 32.212 8.963   9.067   1.00 11.23 ?  60  ALA   A O    1 
ATOM   1529 C CB   . ALA   A 1 60  ? 30.847 10.139  11.756  1.00 11.52 ?  60  ALA   A CB   1 
ATOM   1530 H H    . ALA   A 1 60  ? 28.999 11.211  10.552  1.00 12.49 ?  60  ALA   A H    1 
ATOM   1531 H HA   . ALA   A 1 60  ? 31.580 11.126  10.122  1.00 13.04 ?  60  ALA   A HA   1 
ATOM   1532 H HB1  . ALA   A 1 60  ? 31.681 9.690   11.962  1.00 13.79 ?  60  ALA   A HB1  1 
ATOM   1533 H HB2  . ALA   A 1 60  ? 30.767 10.948  12.288  1.00 13.79 ?  60  ALA   A HB2  1 
ATOM   1534 H HB3  . ALA   A 1 60  ? 30.098 9.551   11.935  1.00 13.79 ?  60  ALA   A HB3  1 
ATOM   1535 N N    . MET   A 1 61  ? 29.992 8.578   9.035   1.00 10.18 ?  61  MET   A N    1 
ATOM   1536 C CA   . MET   A 1 61  ? 30.134 7.451   8.121   1.00 10.33 ?  61  MET   A CA   1 
ATOM   1537 C C    . MET   A 1 61  ? 30.757 7.891   6.798   1.00 9.82  ?  61  MET   A C    1 
ATOM   1538 O O    . MET   A 1 61  ? 31.646 7.214   6.269   1.00 10.15 ?  61  MET   A O    1 
ATOM   1539 C CB   . MET   A 1 61  ? 28.773 6.788   7.912   1.00 10.17 ?  61  MET   A CB   1 
ATOM   1540 C CG   . MET   A 1 61  ? 28.777 5.626   6.930   1.00 10.79 ?  61  MET   A CG   1 
ATOM   1541 S SD   . MET   A 1 61  ? 27.149 4.893   6.709   1.00 11.87 ?  61  MET   A SD   1 
ATOM   1542 C CE   . MET   A 1 61  ? 26.975 3.999   8.252   1.00 13.41 ?  61  MET   A CE   1 
ATOM   1543 H H    . MET   A 1 61  ? 29.185 8.741   9.283   1.00 12.19 ?  61  MET   A H    1 
ATOM   1544 H HA   . MET   A 1 61  ? 30.717 6.795   8.532   1.00 12.38 ?  61  MET   A HA   1 
ATOM   1545 H HB2  . MET   A 1 61  ? 28.465 6.446   8.765   1.00 12.18 ?  61  MET   A HB2  1 
ATOM   1546 H HB3  . MET   A 1 61  ? 28.151 7.448   7.580   1.00 12.18 ?  61  MET   A HB3  1 
ATOM   1547 H HG2  . MET   A 1 61  ? 29.076 5.936   6.064   1.00 12.92 ?  61  MET   A HG2  1 
ATOM   1548 H HG3  . MET   A 1 61  ? 29.368 4.931   7.259   1.00 12.92 ?  61  MET   A HG3  1 
ATOM   1549 H HE1  . MET   A 1 61  ? 26.122 3.534   8.253   1.00 16.06 ?  61  MET   A HE1  1 
ATOM   1550 H HE2  . MET   A 1 61  ? 27.700 3.364   8.329   1.00 16.06 ?  61  MET   A HE2  1 
ATOM   1551 H HE3  . MET   A 1 61  ? 27.004 4.632   8.988   1.00 16.06 ?  61  MET   A HE3  1 
ATOM   1552 N N    . GLN   A 1 62  ? 30.310 9.028   6.253   1.00 10.02 ?  62  GLN   A N    1 
ATOM   1553 C CA   . GLN   A 1 62  ? 30.858 9.503   4.988   1.00 10.34 ?  62  GLN   A CA   1 
ATOM   1554 C C    . GLN   A 1 62  ? 32.328 9.882   5.127   1.00 10.32 ?  62  GLN   A C    1 
ATOM   1555 O O    . GLN   A 1 62  ? 33.133 9.585   4.239   1.00 10.78 ?  62  GLN   A O    1 
ATOM   1556 C CB   . GLN   A 1 62  ? 30.048 10.690  4.465   1.00 10.30 ?  62  GLN   A CB   1 
ATOM   1557 C CG   . GLN   A 1 62  ? 30.406 11.067  3.040   1.00 10.30 ?  62  GLN   A CG   1 
ATOM   1558 C CD   . GLN   A 1 62  ? 30.077 9.940   2.087   1.00 10.38 ?  62  GLN   A CD   1 
ATOM   1559 O OE1  . GLN   A 1 62  ? 28.896 9.636   1.877   1.00 11.23 ?  62  GLN   A OE1  1 
ATOM   1560 N NE2  . GLN   A 1 62  ? 31.097 9.271   1.557   1.00 11.25 ?  62  GLN   A NE2  1 
ATOM   1561 H H    . GLN   A 1 62  ? 29.703 9.528   6.594   1.00 11.99 ?  62  GLN   A H    1 
ATOM   1562 H HA   . GLN   A 1 62  ? 30.802 8.788   4.335   1.00 12.38 ?  62  GLN   A HA   1 
ATOM   1563 H HB2  . GLN   A 1 62  ? 29.106 10.468  4.493   1.00 12.33 ?  62  GLN   A HB2  1 
ATOM   1564 H HB3  . GLN   A 1 62  ? 30.223 11.464  5.029   1.00 12.33 ?  62  GLN   A HB3  1 
ATOM   1565 H HG2  . GLN   A 1 62  ? 29.891 11.842  2.773   1.00 12.34 ?  62  GLN   A HG2  1 
ATOM   1566 H HG3  . GLN   A 1 62  ? 31.354 11.249  2.978   1.00 12.34 ?  62  GLN   A HG3  1 
ATOM   1567 H HE21 . GLN   A 1 62  ? 31.907 9.506   1.736   1.00 13.48 ?  62  GLN   A HE21 1 
ATOM   1568 H HE22 . GLN   A 1 62  ? 30.954 8.618   1.013   1.00 13.48 ?  62  GLN   A HE22 1 
ATOM   1569 N N    . VAL   A 1 63  ? 32.697 10.561  6.218   1.00 10.64 ?  63  VAL   A N    1 
ATOM   1570 C CA   . VAL   A 1 63  ? 34.092 10.951  6.426   1.00 11.72 ?  63  VAL   A CA   1 
ATOM   1571 C C    . VAL   A 1 63  ? 34.989 9.715   6.471   1.00 11.07 ?  63  VAL   A C    1 
ATOM   1572 O O    . VAL   A 1 63  ? 36.038 9.655   5.814   1.00 11.59 ?  63  VAL   A O    1 
ATOM   1573 C CB   . VAL   A 1 63  ? 34.211 11.813  7.695   1.00 13.12 ?  63  VAL   A CB   1 
ATOM   1574 C CG1  . VAL   A 1 63  ? 35.663 12.046  8.045   1.00 14.65 ?  63  VAL   A CG1  1 
ATOM   1575 C CG2  . VAL   A 1 63  ? 33.477 13.141  7.501   1.00 13.47 ?  63  VAL   A CG2  1 
ATOM   1576 H H    . VAL   A 1 63  ? 32.155 10.798  6.849   1.00 12.74 ?  63  VAL   A H    1 
ATOM   1577 H HA   . VAL   A 1 63  ? 34.367 11.493  5.675   1.00 14.03 ?  63  VAL   A HA   1 
ATOM   1578 H HB   . VAL   A 1 63  ? 33.794 11.349  8.437   1.00 15.71 ?  63  VAL   A HB   1 
ATOM   1579 H HG11 . VAL   A 1 63  ? 35.723 12.780  8.674   1.00 17.55 ?  63  VAL   A HG11 1 
ATOM   1580 H HG12 . VAL   A 1 63  ? 36.028 11.240  8.441   1.00 17.55 ?  63  VAL   A HG12 1 
ATOM   1581 H HG13 . VAL   A 1 63  ? 36.151 12.268  7.234   1.00 17.55 ?  63  VAL   A HG13 1 
ATOM   1582 H HG21 . VAL   A 1 63  ? 33.576 13.680  8.304   1.00 16.14 ?  63  VAL   A HG21 1 
ATOM   1583 H HG22 . VAL   A 1 63  ? 33.860 13.610  6.743   1.00 16.14 ?  63  VAL   A HG22 1 
ATOM   1584 H HG23 . VAL   A 1 63  ? 32.536 12.967  7.340   1.00 16.14 ?  63  VAL   A HG23 1 
ATOM   1585 N N    . GLU   A 1 64  ? 34.575 8.701   7.234   1.00 11.09 ?  64  GLU   A N    1 
ATOM   1586 C CA   . GLU   A 1 64  ? 35.343 7.464   7.317   1.00 10.96 ?  64  GLU   A CA   1 
ATOM   1587 C C    . GLU   A 1 64  ? 35.424 6.781   5.956   1.00 10.32 ?  64  GLU   A C    1 
ATOM   1588 O O    . GLU   A 1 64  ? 36.471 6.240   5.571   1.00 10.73 ?  64  GLU   A O    1 
ATOM   1589 C CB   . GLU   A 1 64  ? 34.667 6.545   8.334   1.00 11.67 ?  64  GLU   A CB   1 
ATOM   1590 C CG   . GLU   A 1 64  ? 35.330 5.200   8.480   1.00 12.02 ?  64  GLU   A CG   1 
ATOM   1591 C CD   . GLU   A 1 64  ? 34.463 4.203   9.217   1.00 12.79 ?  64  GLU   A CD   1 
ATOM   1592 O OE1  . GLU   A 1 64  ? 33.216 4.297   9.103   1.00 13.73 ?  64  GLU   A OE1  1 
ATOM   1593 O OE2  . GLU   A 1 64  ? 35.028 3.306   9.893   1.00 13.06 -1 64  GLU   A OE2  1 
ATOM   1594 H H    . GLU   A 1 64  ? 33.850 8.704   7.700   1.00 13.28 ?  64  GLU   A H    1 
ATOM   1595 H HA   . GLU   A 1 64  ? 36.240 7.665   7.626   1.00 13.12 ?  64  GLU   A HA   1 
ATOM   1596 H HB2  . GLU   A 1 64  ? 34.686 6.984   9.207   1.00 13.97 ?  64  GLU   A HB2  1 
ATOM   1597 H HB3  . GLU   A 1 64  ? 33.747 6.410   8.064   1.00 13.97 ?  64  GLU   A HB3  1 
ATOM   1598 H HG2  . GLU   A 1 64  ? 35.520 4.832   7.599   1.00 14.39 ?  64  GLU   A HG2  1 
ATOM   1599 H HG3  . GLU   A 1 64  ? 36.155 5.304   8.975   1.00 14.39 ?  64  GLU   A HG3  1 
ATOM   1600 N N    . SER   A 1 65  ? 34.303 6.779   5.229   1.00 10.10 ?  65  SER   A N    1 
ATOM   1601 C CA   . SER   A 1 65  ? 34.244 6.131   3.925   1.00 10.05 ?  65  SER   A CA   1 
ATOM   1602 C C    . SER   A 1 65  ? 35.160 6.806   2.915   1.00 10.36 ?  65  SER   A C    1 
ATOM   1603 O O    . SER   A 1 65  ? 35.800 6.131   2.103   1.00 10.96 ?  65  SER   A O    1 
ATOM   1604 C CB   . SER   A 1 65  ? 32.804 6.145   3.403   1.00 10.23 ?  65  SER   A CB   1 
ATOM   1605 O OG   . SER   A 1 65  ? 31.957 5.319   4.192   1.00 10.63 ?  65  SER   A OG   1 
ATOM   1606 H H    . SER   A 1 65  ? 33.570 7.154   5.469   1.00 12.10 ?  65  SER   A H    1 
ATOM   1607 H HA   . SER   A 1 65  ? 34.527 5.208   4.013   1.00 12.03 ?  65  SER   A HA   1 
ATOM   1608 H HB2  . SER   A 1 65  ? 32.472 7.056   3.429   1.00 12.25 ?  65  SER   A HB2  1 
ATOM   1609 H HB3  . SER   A 1 65  ? 32.802 5.819   2.490   1.00 12.25 ?  65  SER   A HB3  1 
ATOM   1610 H HG   . SER   A 1 65  ? 31.952 5.596   4.988   1.00 12.74 ?  65  SER   A HG   1 
ATOM   1611 N N    . ASP   A 1 66  ? 35.219 8.142   2.932   1.00 10.54 ?  66  ASP   A N    1 
ATOM   1612 C CA   . ASP   A 1 66  ? 36.073 8.853   1.985   1.00 11.60 ?  66  ASP   A CA   1 
ATOM   1613 C C    . ASP   A 1 66  ? 37.540 8.508   2.212   1.00 11.27 ?  66  ASP   A C    1 
ATOM   1614 O O    . ASP   A 1 66  ? 38.306 8.344   1.253   1.00 12.17 ?  66  ASP   A O    1 
ATOM   1615 C CB   . ASP   A 1 66  ? 35.849 10.358  2.106   1.00 12.76 ?  66  ASP   A CB   1 
ATOM   1616 C CG   . ASP   A 1 66  ? 34.506 10.821  1.522   1.00 14.71 ?  66  ASP   A CG   1 
ATOM   1617 O OD1  . ASP   A 1 66  ? 33.798 10.032  0.859   1.00 14.86 ?  66  ASP   A OD1  1 
ATOM   1618 O OD2  . ASP   A 1 66  ? 34.184 12.011  1.714   1.00 17.77 -1 66  ASP   A OD2  1 
ATOM   1619 H H    . ASP   A 1 66  ? 34.769 8.652   3.468   1.00 12.63 ?  66  ASP   A H    1 
ATOM   1620 H HA   . ASP   A 1 66  ? 35.836 8.584   1.084   1.00 13.89 ?  66  ASP   A HA   1 
ATOM   1621 H HB2  . ASP   A 1 66  ? 35.870 10.604  3.044   1.00 15.28 ?  66  ASP   A HB2  1 
ATOM   1622 H HB3  . ASP   A 1 66  ? 36.559 10.817  1.627   1.00 15.28 ?  66  ASP   A HB3  1 
ATOM   1623 N N    . ASP   A 1 67  ? 37.946 8.367   3.476   1.00 11.17 ?  67  ASP   A N    1 
ATOM   1624 C CA   . ASP   A 1 67  ? 39.305 7.925   3.765   1.00 12.00 ?  67  ASP   A CA   1 
ATOM   1625 C C    . ASP   A 1 67  ? 39.534 6.496   3.283   1.00 11.93 ?  67  ASP   A C    1 
ATOM   1626 O O    . ASP   A 1 67  ? 40.597 6.184   2.735   1.00 12.65 ?  67  ASP   A O    1 
ATOM   1627 C CB   . ASP   A 1 67  ? 39.588 8.056   5.259   1.00 13.63 ?  67  ASP   A CB   1 
ATOM   1628 C CG   . ASP   A 1 67  ? 40.896 7.393   5.668   1.00 14.73 ?  67  ASP   A CG   1 
ATOM   1629 O OD1  . ASP   A 1 67  ? 41.970 8.025   5.534   1.00 17.30 ?  67  ASP   A OD1  1 
ATOM   1630 O OD2  . ASP   A 1 67  ? 40.844 6.225   6.116   1.00 14.52 -1 67  ASP   A OD2  1 
ATOM   1631 H H    . ASP   A 1 67  ? 37.458 8.516   4.169   1.00 13.38 ?  67  ASP   A H    1 
ATOM   1632 H HA   . ASP   A 1 67  ? 39.926 8.496   3.290   1.00 14.37 ?  67  ASP   A HA   1 
ATOM   1633 H HB2  . ASP   A 1 67  ? 39.644 8.997   5.482   1.00 16.33 ?  67  ASP   A HB2  1 
ATOM   1634 H HB3  . ASP   A 1 67  ? 38.866 7.638   5.754   1.00 16.33 ?  67  ASP   A HB3  1 
ATOM   1635 N N    A TYR   A 1 68  ? 38.544 5.618   3.462   0.40 11.31 ?  68  TYR   A N    1 
ATOM   1636 N N    B TYR   A 1 68  ? 38.551 5.606   3.486   0.60 11.53 ?  68  TYR   A N    1 
ATOM   1637 C CA   A TYR   A 1 68  ? 38.692 4.239   3.003   0.40 11.38 ?  68  TYR   A CA   1 
ATOM   1638 C CA   B TYR   A 1 68  ? 38.672 4.229   2.998   0.60 12.00 ?  68  TYR   A CA   1 
ATOM   1639 C C    A TYR   A 1 68  ? 38.890 4.177   1.490   0.40 11.12 ?  68  TYR   A C    1 
ATOM   1640 C C    B TYR   A 1 68  ? 38.915 4.204   1.491   0.60 11.50 ?  68  TYR   A C    1 
ATOM   1641 O O    A TYR   A 1 68  ? 39.738 3.420   0.998   0.40 11.34 ?  68  TYR   A O    1 
ATOM   1642 O O    B TYR   A 1 68  ? 39.806 3.497   1.003   0.60 11.95 ?  68  TYR   A O    1 
ATOM   1643 C CB   A TYR   A 1 68  ? 37.479 3.401   3.429   0.40 11.47 ?  68  TYR   A CB   1 
ATOM   1644 C CB   B TYR   A 1 68  ? 37.423 3.394   3.353   0.60 12.59 ?  68  TYR   A CB   1 
ATOM   1645 C CG   A TYR   A 1 68  ? 37.543 1.987   2.897   0.40 12.07 ?  68  TYR   A CG   1 
ATOM   1646 C CG   B TYR   A 1 68  ? 37.437 2.032   2.658   0.60 13.55 ?  68  TYR   A CG   1 
ATOM   1647 C CD1  A TYR   A 1 68  ? 37.060 1.684   1.629   0.40 12.85 ?  68  TYR   A CD1  1 
ATOM   1648 C CD1  B TYR   A 1 68  ? 36.979 1.899   1.347   0.60 13.89 ?  68  TYR   A CD1  1 
ATOM   1649 C CD2  A TYR   A 1 68  ? 38.130 0.968   3.633   0.40 13.31 ?  68  TYR   A CD2  1 
ATOM   1650 C CD2  B TYR   A 1 68  ? 37.959 0.904   3.282   0.60 14.26 ?  68  TYR   A CD2  1 
ATOM   1651 C CE1  A TYR   A 1 68  ? 37.150 0.411   1.113   0.40 14.21 ?  68  TYR   A CE1  1 
ATOM   1652 C CE1  B TYR   A 1 68  ? 37.034 0.697   0.686   0.60 13.82 ?  68  TYR   A CE1  1 
ATOM   1653 C CE2  A TYR   A 1 68  ? 38.215 -0.322  3.126   0.40 14.15 ?  68  TYR   A CE2  1 
ATOM   1654 C CE2  B TYR   A 1 68  ? 38.004 -0.324  2.626   0.60 13.72 ?  68  TYR   A CE2  1 
ATOM   1655 C CZ   A TYR   A 1 68  ? 37.726 -0.587  1.868   0.40 14.91 ?  68  TYR   A CZ   1 
ATOM   1656 C CZ   B TYR   A 1 68  ? 37.546 -0.406  1.333   0.60 13.36 ?  68  TYR   A CZ   1 
ATOM   1657 O OH   A TYR   A 1 68  ? 37.820 -1.853  1.352   0.40 17.05 ?  68  TYR   A OH   1 
ATOM   1658 O OH   B TYR   A 1 68  ? 37.619 -1.609  0.688   0.60 13.59 ?  68  TYR   A OH   1 
ATOM   1659 H H    A TYR   A 1 68  ? 37.787 5.791   3.836   0.40 13.55 ?  68  TYR   A H    1 
ATOM   1660 H H    B TYR   A 1 68  ? 37.810 5.771   3.896   0.60 13.81 ?  68  TYR   A H    1 
ATOM   1661 H HA   A TYR   A 1 68  ? 39.479 3.857   3.419   0.40 13.63 ?  68  TYR   A HA   1 
ATOM   1662 H HA   B TYR   A 1 68  ? 39.434 3.814   3.425   0.60 14.37 ?  68  TYR   A HA   1 
ATOM   1663 H HB2  A TYR   A 1 68  ? 37.454 3.353   4.394   0.40 13.74 ?  68  TYR   A HB2  1 
ATOM   1664 H HB2  B TYR   A 1 68  ? 37.404 3.239   4.311   0.60 15.08 ?  68  TYR   A HB2  1 
ATOM   1665 H HB3  A TYR   A 1 68  ? 36.675 3.813   3.087   0.40 13.74 ?  68  TYR   A HB3  1 
ATOM   1666 H HB3  B TYR   A 1 68  ? 36.627 3.867   3.073   0.60 15.08 ?  68  TYR   A HB3  1 
ATOM   1667 H HD1  A TYR   A 1 68  ? 36.681 2.361   1.112   0.40 15.40 ?  68  TYR   A HD1  1 
ATOM   1668 H HD1  B TYR   A 1 68  ? 36.640 2.642   0.904   0.60 16.64 ?  68  TYR   A HD1  1 
ATOM   1669 H HD2  A TYR   A 1 68  ? 38.475 1.148   4.475   0.40 15.94 ?  68  TYR   A HD2  1 
ATOM   1670 H HD2  B TYR   A 1 68  ? 38.281 0.968   4.149   0.60 17.08 ?  68  TYR   A HD2  1 
ATOM   1671 H HE1  A TYR   A 1 68  ? 36.812 0.230   0.261   0.40 17.02 ?  68  TYR   A HE1  1 
ATOM   1672 H HE1  B TYR   A 1 68  ? 36.715 0.616   -0.188  0.60 16.56 ?  68  TYR   A HE1  1 
ATOM   1673 H HE2  A TYR   A 1 68  ? 38.609 -1.002  3.621   0.40 16.96 ?  68  TYR   A HE2  1 
ATOM   1674 H HE2  B TYR   A 1 68  ? 38.356 -1.078  3.046   0.60 16.44 ?  68  TYR   A HE2  1 
ATOM   1675 H HH   A TYR   A 1 68  ? 38.174 -2.369  1.903   0.40 20.44 ?  68  TYR   A HH   1 
ATOM   1676 H HH   B TYR   A 1 68  ? 37.945 -2.207  1.201   0.60 16.29 ?  68  TYR   A HH   1 
ATOM   1677 N N    . ILE   A 1 69  ? 38.110 4.954   0.734   1.00 10.83 ?  69  ILE   A N    1 
ATOM   1678 C CA   . ILE   A 1 69  ? 38.232 4.938   -0.722  1.00 11.07 ?  69  ILE   A CA   1 
ATOM   1679 C C    . ILE   A 1 69  ? 39.555 5.557   -1.163  1.00 10.77 ?  69  ILE   A C    1 
ATOM   1680 O O    . ILE   A 1 69  ? 40.191 5.088   -2.112  1.00 11.30 ?  69  ILE   A O    1 
ATOM   1681 C CB   . ILE   A 1 69  ? 37.026 5.642   -1.373  1.00 12.13 ?  69  ILE   A CB   1 
ATOM   1682 C CG1  . ILE   A 1 69  ? 35.720 4.891   -1.089  1.00 12.90 ?  69  ILE   A CG1  1 
ATOM   1683 C CG2  . ILE   A 1 69  ? 37.249 5.832   -2.878  1.00 14.06 ?  69  ILE   A CG2  1 
ATOM   1684 C CD1  . ILE   A 1 69  ? 35.548 3.602   -1.874  1.00 13.75 ?  69  ILE   A CD1  1 
ATOM   1685 H H    A ILE   A 1 69  ? 37.513 5.493   1.036   0.40 12.97 ?  69  ILE   A H    1 
ATOM   1686 H H    B ILE   A 1 69  ? 37.501 5.480   1.035   0.60 12.97 ?  69  ILE   A H    1 
ATOM   1687 H HA   . ILE   A 1 69  ? 38.231 4.012   -1.018  1.00 13.25 ?  69  ILE   A HA   1 
ATOM   1688 H HB   . ILE   A 1 69  ? 36.949 6.515   -0.973  1.00 14.53 ?  69  ILE   A HB   1 
ATOM   1689 H HG12 . ILE   A 1 69  ? 35.692 4.662   -0.143  1.00 15.46 ?  69  ILE   A HG12 1 
ATOM   1690 H HG13 . ILE   A 1 69  ? 34.977 5.471   -1.304  1.00 15.46 ?  69  ILE   A HG13 1 
ATOM   1691 H HG21 . ILE   A 1 69  ? 36.397 6.029   -3.299  1.00 16.85 ?  69  ILE   A HG21 1 
ATOM   1692 H HG22 . ILE   A 1 69  ? 37.859 6.577   -3.014  1.00 16.85 ?  69  ILE   A HG22 1 
ATOM   1693 H HG23 . ILE   A 1 69  ? 37.624 5.022   -3.252  1.00 16.85 ?  69  ILE   A HG23 1 
ATOM   1694 H HD11 . ILE   A 1 69  ? 34.757 3.138   -1.549  1.00 16.48 ?  69  ILE   A HD11 1 
ATOM   1695 H HD12 . ILE   A 1 69  ? 35.436 3.815   -2.814  1.00 16.48 ?  69  ILE   A HD12 1 
ATOM   1696 H HD13 . ILE   A 1 69  ? 36.329 3.042   -1.751  1.00 16.48 ?  69  ILE   A HD13 1 
ATOM   1697 N N    . ALA   A 1 70  ? 39.974 6.638   -0.508  1.00 11.35 ?  70  ALA   A N    1 
ATOM   1698 C CA   . ALA   A 1 70  ? 41.243 7.259   -0.872  1.00 12.23 ?  70  ALA   A CA   1 
ATOM   1699 C C    . ALA   A 1 70  ? 42.401 6.279   -0.716  1.00 12.19 ?  70  ALA   A C    1 
ATOM   1700 O O    . ALA   A 1 70  ? 43.350 6.306   -1.503  1.00 14.30 ?  70  ALA   A O    1 
ATOM   1701 C CB   . ALA   A 1 70  ? 41.476 8.509   -0.027  1.00 12.78 ?  70  ALA   A CB   1 
ATOM   1702 H H    . ALA   A 1 70  ? 39.549 7.024   0.130   1.00 13.60 ?  70  ALA   A H    1 
ATOM   1703 H HA   . ALA   A 1 70  ? 41.206 7.533   -1.803  1.00 14.65 ?  70  ALA   A HA   1 
ATOM   1704 H HB1  . ALA   A 1 70  ? 42.328 8.905   -0.280  1.00 15.31 ?  70  ALA   A HB1  1 
ATOM   1705 H HB2  . ALA   A 1 70  ? 40.759 9.138   -0.183  1.00 15.31 ?  70  ALA   A HB2  1 
ATOM   1706 H HB3  . ALA   A 1 70  ? 41.500 8.255   0.910   1.00 15.31 ?  70  ALA   A HB3  1 
ATOM   1707 N N    . THR   A 1 71  ? 42.319 5.377   0.263   1.00 11.85 ?  71  THR   A N    1 
ATOM   1708 C CA   . THR   A 1 71  ? 43.383 4.409   0.503   1.00 13.21 ?  71  THR   A CA   1 
ATOM   1709 C C    . THR   A 1 71  ? 43.267 3.184   -0.395  1.00 13.33 ?  71  THR   A C    1 
ATOM   1710 O O    . THR   A 1 71  ? 44.278 2.686   -0.907  1.00 15.16 ?  71  THR   A O    1 
ATOM   1711 C CB   . THR   A 1 71  ? 43.335 3.965   1.962   1.00 15.05 ?  71  THR   A CB   1 
ATOM   1712 O OG1  . THR   A 1 71  ? 43.594 5.096   2.803   1.00 16.24 ?  71  THR   A OG1  1 
ATOM   1713 C CG2  . THR   A 1 71  ? 44.347 2.843   2.242   1.00 16.32 ?  71  THR   A CG2  1 
ATOM   1714 H H    . THR   A 1 71  ? 41.651 5.301   0.798   1.00 14.19 ?  71  THR   A H    1 
ATOM   1715 H HA   . THR   A 1 71  ? 44.241 4.822   0.330   1.00 15.83 ?  71  THR   A HA   1 
ATOM   1716 H HB   . THR   A 1 71  ? 42.453 3.617   2.157   1.00 18.03 ?  71  THR   A HB   1 
ATOM   1717 H HG1  . THR   A 1 71  ? 43.578 4.853   3.608   1.00 19.46 ?  71  THR   A HG1  1 
ATOM   1718 H HG21 . THR   A 1 71  ? 44.488 2.754   3.200   1.00 19.56 ?  71  THR   A HG21 1 
ATOM   1719 H HG22 . THR   A 1 71  ? 44.025 1.996   1.896   1.00 19.56 ?  71  THR   A HG22 1 
ATOM   1720 H HG23 . THR   A 1 71  ? 45.202 3.048   1.824   1.00 19.56 ?  71  THR   A HG23 1 
ATOM   1721 N N    . ASN   A 1 72  ? 42.045 2.675   -0.581  1.00 12.33 ?  72  ASN   A N    1 
ATOM   1722 C CA   . ASN   A 1 72  ? 41.824 1.348   -1.143  1.00 12.75 ?  72  ASN   A CA   1 
ATOM   1723 C C    . ASN   A 1 72  ? 41.196 1.342   -2.525  1.00 12.75 ?  72  ASN   A C    1 
ATOM   1724 O O    . ASN   A 1 72  ? 41.206 0.291   -3.179  1.00 14.06 ?  72  ASN   A O    1 
ATOM   1725 C CB   . ASN   A 1 72  ? 40.939 0.527   -0.201  1.00 13.44 ?  72  ASN   A CB   1 
ATOM   1726 C CG   . ASN   A 1 72  ? 41.561 0.364   1.158   1.00 14.24 ?  72  ASN   A CG   1 
ATOM   1727 O OD1  . ASN   A 1 72  ? 41.111 0.960   2.134   1.00 15.99 ?  72  ASN   A OD1  1 
ATOM   1728 N ND2  . ASN   A 1 72  ? 42.620 -0.411  1.227   1.00 15.09 ?  72  ASN   A ND2  1 
ATOM   1729 H H    . ASN   A 1 72  ? 41.311 3.091   -0.388  1.00 14.77 ?  72  ASN   A H    1 
ATOM   1730 H HA   . ASN   A 1 72  ? 42.678 0.898   -1.215  1.00 15.28 ?  72  ASN   A HA   1 
ATOM   1731 H HB2  . ASN   A 1 72  ? 40.087 0.974   -0.091  1.00 16.10 ?  72  ASN   A HB2  1 
ATOM   1732 H HB3  . ASN   A 1 72  ? 40.807 -0.358  -0.579  1.00 16.10 ?  72  ASN   A HB3  1 
ATOM   1733 H HD21 . ASN   A 1 72  ? 43.018 -0.533  1.983   1.00 18.09 ?  72  ASN   A HD21 1 
ATOM   1734 H HD22 . ASN   A 1 72  ? 42.916 -0.803  0.522   1.00 18.09 ?  72  ASN   A HD22 1 
ATOM   1735 N N    . GLY   A 1 73  ? 40.640 2.459   -2.978  1.00 12.51 ?  73  GLY   A N    1 
ATOM   1736 C CA   . GLY   A 1 73  ? 39.894 2.487   -4.211  1.00 12.39 ?  73  GLY   A CA   1 
ATOM   1737 C C    . GLY   A 1 73  ? 38.505 1.900   -4.041  1.00 11.72 ?  73  GLY   A C    1 
ATOM   1738 O O    . GLY   A 1 73  ? 38.130 1.432   -2.959  1.00 12.13 ?  73  GLY   A O    1 
ATOM   1739 H H    . GLY   A 1 73  ? 40.684 3.227   -2.581  1.00 14.99 ?  73  GLY   A H    1 
ATOM   1740 H HA2  . GLY   A 1 73  ? 39.811 3.409   -4.518  1.00 14.84 ?  73  GLY   A HA2  1 
ATOM   1741 H HA3  . GLY   A 1 73  ? 40.365 1.981   -4.890  1.00 14.84 ?  73  GLY   A HA3  1 
ATOM   1742 N N    . PRO   A 1 74  ? 37.718 1.921   -5.117  1.00 11.87 ?  74  PRO   A N    1 
ATOM   1743 C CA   . PRO   A 1 74  ? 36.324 1.478   -5.030  1.00 11.95 ?  74  PRO   A CA   1 
ATOM   1744 C C    . PRO   A 1 74  ? 36.184 -0.007  -4.727  1.00 11.24 ?  74  PRO   A C    1 
ATOM   1745 O O    . PRO   A 1 74  ? 37.049 -0.835  -5.031  1.00 12.14 ?  74  PRO   A O    1 
ATOM   1746 C CB   . PRO   A 1 74  ? 35.759 1.803   -6.420  1.00 13.86 ?  74  PRO   A CB   1 
ATOM   1747 C CG   . PRO   A 1 74  ? 36.690 2.823   -7.001  1.00 16.26 ?  74  PRO   A CG   1 
ATOM   1748 C CD   . PRO   A 1 74  ? 38.042 2.474   -6.443  1.00 13.90 ?  74  PRO   A CD   1 
ATOM   1749 H HA   . PRO   A 1 74  ? 35.843 1.996   -4.363  1.00 14.31 ?  74  PRO   A HA   1 
ATOM   1750 H HB2  . PRO   A 1 74  ? 35.746 1.005   -6.966  1.00 16.61 ?  74  PRO   A HB2  1 
ATOM   1751 H HB3  . PRO   A 1 74  ? 34.865 2.176   -6.335  1.00 16.61 ?  74  PRO   A HB3  1 
ATOM   1752 H HG2  . PRO   A 1 74  ? 36.692 2.755   -7.970  1.00 19.49 ?  74  PRO   A HG2  1 
ATOM   1753 H HG3  . PRO   A 1 74  ? 36.422 3.713   -6.723  1.00 19.49 ?  74  PRO   A HG3  1 
ATOM   1754 H HD2  . PRO   A 1 74  ? 38.480 1.810   -6.996  1.00 16.65 ?  74  PRO   A HD2  1 
ATOM   1755 H HD3  . PRO   A 1 74  ? 38.584 3.281   -6.362  1.00 16.65 ?  74  PRO   A HD3  1 
ATOM   1756 N N    . LEU   A 1 75  ? 35.043 -0.335  -4.135  1.00 10.65 ?  75  LEU   A N    1 
ATOM   1757 C CA   . LEU   A 1 75  ? 34.649 -1.723  -3.987  1.00 10.50 ?  75  LEU   A CA   1 
ATOM   1758 C C    . LEU   A 1 75  ? 34.257 -2.301  -5.343  1.00 10.79 ?  75  LEU   A C    1 
ATOM   1759 O O    . LEU   A 1 75  ? 34.127 -1.590  -6.342  1.00 12.29 ?  75  LEU   A O    1 
ATOM   1760 C CB   . LEU   A 1 75  ? 33.465 -1.845  -3.030  1.00 10.50 ?  75  LEU   A CB   1 
ATOM   1761 C CG   . LEU   A 1 75  ? 33.682 -1.461  -1.571  1.00 12.31 ?  75  LEU   A CG   1 
ATOM   1762 C CD1  . LEU   A 1 75  ? 32.411 -1.692  -0.753  1.00 14.30 ?  75  LEU   A CD1  1 
ATOM   1763 C CD2  . LEU   A 1 75  ? 34.854 -2.171  -0.953  1.00 15.92 ?  75  LEU   A CD2  1 
ATOM   1764 H H    . LEU   A 1 75  ? 34.478 0.235   -3.816  1.00 12.76 ?  75  LEU   A H    1 
ATOM   1765 H HA   . LEU   A 1 75  ? 35.396 -2.228  -3.640  1.00 12.57 ?  75  LEU   A HA   1 
ATOM   1766 H HB2  . LEU   A 1 75  ? 32.750 -1.288  -3.369  1.00 12.57 ?  75  LEU   A HB2  1 
ATOM   1767 H HB3  . LEU   A 1 75  ? 33.178 -2.771  -3.041  1.00 12.57 ?  75  LEU   A HB3  1 
ATOM   1768 H HG   . LEU   A 1 75  ? 33.879 -0.511  -1.537  1.00 14.75 ?  75  LEU   A HG   1 
ATOM   1769 H HD11 . LEU   A 1 75  ? 32.580 -1.434  0.168   1.00 17.14 ?  75  LEU   A HD11 1 
ATOM   1770 H HD12 . LEU   A 1 75  ? 31.699 -1.146  -1.122  1.00 17.14 ?  75  LEU   A HD12 1 
ATOM   1771 H HD13 . LEU   A 1 75  ? 32.173 -2.628  -0.798  1.00 17.14 ?  75  LEU   A HD13 1 
ATOM   1772 H HD21 . LEU   A 1 75  ? 34.898 -1.950  -0.010  1.00 19.08 ?  75  LEU   A HD21 1 
ATOM   1773 H HD22 . LEU   A 1 75  ? 34.740 -3.127  -1.064  1.00 19.08 ?  75  LEU   A HD22 1 
ATOM   1774 H HD23 . LEU   A 1 75  ? 35.672 -1.884  -1.395  1.00 19.08 ?  75  LEU   A HD23 1 
ATOM   1775 N N    . LYS   A 1 76  ? 34.084 -3.621  -5.362  1.00 11.44 ?  76  LYS   A N    1 
ATOM   1776 C CA   . LYS   A 1 76  ? 33.475 -4.341  -6.476  1.00 11.91 ?  76  LYS   A CA   1 
ATOM   1777 C C    . LYS   A 1 76  ? 31.964 -4.429  -6.271  1.00 10.41 ?  76  LYS   A C    1 
ATOM   1778 O O    . LYS   A 1 76  ? 31.491 -4.558  -5.145  1.00 10.73 ?  76  LYS   A O    1 
ATOM   1779 C CB   . LYS   A 1 76  ? 34.025 -5.777  -6.541  1.00 13.68 ?  76  LYS   A CB   1 
ATOM   1780 C CG   . LYS   A 1 76  ? 35.533 -5.883  -6.747  1.00 15.34 ?  76  LYS   A CG   1 
ATOM   1781 C CD   . LYS   A 1 76  ? 36.054 -7.297  -6.551  1.00 16.85 ?  76  LYS   A CD   1 
ATOM   1782 C CE   . LYS   A 1 76  ? 37.543 -7.369  -6.808  1.00 19.10 ?  76  LYS   A CE   1 
ATOM   1783 N NZ   . LYS   A 1 76  ? 38.078 -8.727  -6.603  1.00 20.23 ?  76  LYS   A NZ   1 
ATOM   1784 H H    . LYS   A 1 76  ? 34.323 -4.139  -4.716  1.00 13.71 ?  76  LYS   A H    1 
ATOM   1785 H HA   . LYS   A 1 76  ? 33.663 -3.888  -7.314  1.00 14.27 ?  76  LYS   A HA   1 
ATOM   1786 H HB2  . LYS   A 1 76  ? 33.812 -6.226  -5.709  1.00 16.38 ?  76  LYS   A HB2  1 
ATOM   1787 H HB3  . LYS   A 1 76  ? 33.598 -6.236  -7.280  1.00 16.38 ?  76  LYS   A HB3  1 
ATOM   1788 H HG2  . LYS   A 1 76  ? 35.750 -5.602  -7.650  1.00 18.38 ?  76  LYS   A HG2  1 
ATOM   1789 H HG3  . LYS   A 1 76  ? 35.981 -5.304  -6.106  1.00 18.38 ?  76  LYS   A HG3  1 
ATOM   1790 H HD2  . LYS   A 1 76  ? 35.883 -7.576  -5.636  1.00 20.19 ?  76  LYS   A HD2  1 
ATOM   1791 H HD3  . LYS   A 1 76  ? 35.603 -7.891  -7.173  1.00 20.19 ?  76  LYS   A HD3  1 
ATOM   1792 H HE2  . LYS   A 1 76  ? 37.719 -7.107  -7.724  1.00 22.90 ?  76  LYS   A HE2  1 
ATOM   1793 H HE3  . LYS   A 1 76  ? 37.998 -6.770  -6.195  1.00 22.90 ?  76  LYS   A HE3  1 
ATOM   1794 H HZ1  . LYS   A 1 76  ? 38.952 -8.743  -6.762  1.00 24.25 ?  76  LYS   A HZ1  1 
ATOM   1795 H HZ2  . LYS   A 1 76  ? 37.930 -8.995  -5.766  1.00 24.25 ?  76  LYS   A HZ2  1 
ATOM   1796 H HZ3  . LYS   A 1 76  ? 37.675 -9.302  -7.159  1.00 24.25 ?  76  LYS   A HZ3  1 
ATOM   1797 N N    . VAL   A 1 77  ? 31.205 -4.392  -7.372  1.00 10.90 ?  77  VAL   A N    1 
ATOM   1798 C CA   . VAL   A 1 77  ? 29.797 -4.777  -7.282  1.00 11.21 ?  77  VAL   A CA   1 
ATOM   1799 C C    . VAL   A 1 77  ? 29.733 -6.232  -6.843  1.00 10.58 ?  77  VAL   A C    1 
ATOM   1800 O O    . VAL   A 1 77  ? 30.402 -7.100  -7.419  1.00 10.83 ?  77  VAL   A O    1 
ATOM   1801 C CB   . VAL   A 1 77  ? 29.072 -4.556  -8.618  1.00 12.30 ?  77  VAL   A CB   1 
ATOM   1802 C CG1  . VAL   A 1 77  ? 27.615 -4.993  -8.511  1.00 13.13 ?  77  VAL   A CG1  1 
ATOM   1803 C CG2  . VAL   A 1 77  ? 29.155 -3.101  -9.030  1.00 14.04 ?  77  VAL   A CG2  1 
ATOM   1804 H H    . VAL   A 1 77  ? 31.478 -4.144  -8.145  1.00 13.06 ?  77  VAL   A H    1 
ATOM   1805 H HA   . VAL   A 1 77  ? 29.365 -4.232  -6.604  1.00 13.43 ?  77  VAL   A HA   1 
ATOM   1806 H HB   . VAL   A 1 77  ? 29.507 -5.088  -9.302  1.00 14.73 ?  77  VAL   A HB   1 
ATOM   1807 H HG11 . VAL   A 1 77  ? 27.145 -4.697  -9.301  1.00 15.73 ?  77  VAL   A HG11 1 
ATOM   1808 H HG12 . VAL   A 1 77  ? 27.583 -5.960  -8.445  1.00 15.73 ?  77  VAL   A HG12 1 
ATOM   1809 H HG13 . VAL   A 1 77  ? 27.228 -4.591  -7.719  1.00 15.73 ?  77  VAL   A HG13 1 
ATOM   1810 H HG21 . VAL   A 1 77  ? 28.645 -2.978  -9.843  1.00 16.82 ?  77  VAL   A HG21 1 
ATOM   1811 H HG22 . VAL   A 1 77  ? 28.788 -2.553  -8.319  1.00 16.82 ?  77  VAL   A HG22 1 
ATOM   1812 H HG23 . VAL   A 1 77  ? 30.085 -2.866  -9.181  1.00 16.82 ?  77  VAL   A HG23 1 
ATOM   1813 N N    . GLY   A 1 78  ? 28.956 -6.502  -5.790  1.00 10.22 ?  78  GLY   A N    1 
ATOM   1814 C CA   . GLY   A 1 78  ? 28.943 -7.795  -5.140  1.00 10.37 ?  78  GLY   A CA   1 
ATOM   1815 C C    . GLY   A 1 78  ? 29.873 -7.900  -3.954  1.00 10.03 ?  78  GLY   A C    1 
ATOM   1816 O O    . GLY   A 1 78  ? 29.821 -8.909  -3.236  1.00 10.60 ?  78  GLY   A O    1 
ATOM   1817 H H    . GLY   A 1 78  ? 28.404 -5.932  -5.445  1.00 12.23 ?  78  GLY   A H    1 
ATOM   1818 H HA2  . GLY   A 1 78  ? 28.043 -7.983  -4.835  1.00 12.42 ?  78  GLY   A HA2  1 
ATOM   1819 H HA3  . GLY   A 1 78  ? 29.194 -8.472  -5.785  1.00 12.42 ?  78  GLY   A HA3  1 
ATOM   1820 N N    . GLY   A 1 79  ? 30.724 -6.896  -3.731  1.00 10.04 ?  79  GLY   A N    1 
ATOM   1821 C CA   . GLY   A 1 79  ? 31.693 -6.915  -2.663  1.00 10.47 ?  79  GLY   A CA   1 
ATOM   1822 C C    . GLY   A 1 79  ? 31.241 -6.124  -1.447  1.00 9.69  ?  79  GLY   A C    1 
ATOM   1823 O O    . GLY   A 1 79  ? 30.121 -5.615  -1.365  1.00 10.33 ?  79  GLY   A O    1 
ATOM   1824 H H    . GLY   A 1 79  ? 30.767 -6.178  -4.211  1.00 12.03 ?  79  GLY   A H    1 
ATOM   1825 H HA2  . GLY   A 1 79  ? 31.851 -7.840  -2.391  1.00 12.54 ?  79  GLY   A HA2  1 
ATOM   1826 H HA3  . GLY   A 1 79  ? 32.534 -6.549  -2.975  1.00 12.54 ?  79  GLY   A HA3  1 
ATOM   1827 N N    . SER   A 1 80  ? 32.150 -6.036  -0.479  1.00 10.55 ?  80  SER   A N    1 
ATOM   1828 C CA   . SER   A 1 80  ? 31.837 -5.410  0.793   1.00 9.93  ?  80  SER   A CA   1 
ATOM   1829 C C    . SER   A 1 80  ? 33.112 -4.962  1.486   1.00 9.97  ?  80  SER   A C    1 
ATOM   1830 O O    . SER   A 1 80  ? 34.223 -5.384  1.146   1.00 11.47 ?  80  SER   A O    1 
ATOM   1831 C CB   . SER   A 1 80  ? 31.080 -6.375  1.714   1.00 10.92 ?  80  SER   A CB   1 
ATOM   1832 O OG   . SER   A 1 80  ? 31.908 -7.431  2.178   1.00 12.63 ?  80  SER   A OG   1 
ATOM   1833 H H    . SER   A 1 80  ? 32.959 -6.316  -0.539  1.00 12.63 ?  80  SER   A H    1 
ATOM   1834 H HA   . SER   A 1 80  ? 31.281 -4.629  0.630   1.00 11.90 ?  80  SER   A HA   1 
ATOM   1835 H HB2  . SER   A 1 80  ? 30.747 -5.878  2.478   1.00 13.08 ?  80  SER   A HB2  1 
ATOM   1836 H HB3  . SER   A 1 80  ? 30.337 -6.754  1.220   1.00 13.08 ?  80  SER   A HB3  1 
ATOM   1837 H HG   . SER   A 1 80  ? 32.205 -7.862  1.521   1.00 15.13 ?  80  SER   A HG   1 
ATOM   1838 N N    . CYS   A 1 81  ? 32.928 -4.116  2.494   1.00 9.77  ?  81  CYS   A N    1 
ATOM   1839 C CA   . CYS   A 1 81  ? 33.983 -3.832  3.453   1.00 9.90  ?  81  CYS   A CA   1 
ATOM   1840 C C    . CYS   A 1 81  ? 33.342 -3.607  4.815   1.00 9.68  ?  81  CYS   A C    1 
ATOM   1841 O O    . CYS   A 1 81  ? 32.177 -3.209  4.913   1.00 10.77 ?  81  CYS   A O    1 
ATOM   1842 C CB   . CYS   A 1 81  ? 34.851 -2.639  3.032   1.00 10.96 ?  81  CYS   A CB   1 
ATOM   1843 S SG   . CYS   A 1 81  ? 33.952 -1.063  3.065   1.00 11.08 ?  81  CYS   A SG   1 
ATOM   1844 H H    . CYS   A 1 81  ? 32.192 -3.693  2.655   1.00 11.70 ?  81  CYS   A H    1 
ATOM   1845 H HA   . CYS   A 1 81  ? 34.567 -4.605  3.516   1.00 11.85 ?  81  CYS   A HA   1 
ATOM   1846 H HB2  . CYS   A 1 81  ? 35.608 -2.565  3.636   1.00 13.12 ?  81  CYS   A HB2  1 
ATOM   1847 H HB3  . CYS   A 1 81  ? 35.172 -2.784  2.124   1.00 13.12 ?  81  CYS   A HB3  1 
ATOM   1848 H HG   . CYS   A 1 81  ? 34.687 -0.178  2.722   1.00 13.26 ?  81  CYS   A HG   1 
ATOM   1849 N N    . VAL   A 1 82  ? 34.120 -3.875  5.859   1.00 10.32 ?  82  VAL   A N    1 
ATOM   1850 C CA   . VAL   A 1 82  ? 33.714 -3.647  7.238   1.00 10.82 ?  82  VAL   A CA   1 
ATOM   1851 C C    . VAL   A 1 82  ? 34.313 -2.333  7.717   1.00 10.83 ?  82  VAL   A C    1 
ATOM   1852 O O    . VAL   A 1 82  ? 35.536 -2.154  7.698   1.00 11.76 ?  82  VAL   A O    1 
ATOM   1853 C CB   . VAL   A 1 82  ? 34.147 -4.796  8.162   1.00 12.33 ?  82  VAL   A CB   1 
ATOM   1854 C CG1  . VAL   A 1 82  ? 33.701 -4.508  9.587   1.00 13.55 ?  82  VAL   A CG1  1 
ATOM   1855 C CG2  . VAL   A 1 82  ? 33.592 -6.133  7.682   1.00 13.27 ?  82  VAL   A CG2  1 
ATOM   1856 H H    . VAL   A 1 82  ? 34.918 -4.214  5.789   1.00 12.36 ?  82  VAL   A H    1 
ATOM   1857 H HA   . VAL   A 1 82  ? 32.752 -3.572  7.274   1.00 12.96 ?  82  VAL   A HA   1 
ATOM   1858 H HB   . VAL   A 1 82  ? 35.116 -4.854  8.162   1.00 14.77 ?  82  VAL   A HB   1 
ATOM   1859 H HG11 . VAL   A 1 82  ? 33.781 -5.316  10.113  1.00 16.23 ?  82  VAL   A HG11 1 
ATOM   1860 H HG12 . VAL   A 1 82  ? 34.261 -3.810  9.964   1.00 16.23 ?  82  VAL   A HG12 1 
ATOM   1861 H HG13 . VAL   A 1 82  ? 32.774 -4.214  9.573   1.00 16.23 ?  82  VAL   A HG13 1 
ATOM   1862 H HG21 . VAL   A 1 82  ? 33.857 -6.824  8.307   1.00 15.89 ?  82  VAL   A HG21 1 
ATOM   1863 H HG22 . VAL   A 1 82  ? 32.627 -6.074  7.639   1.00 15.89 ?  82  VAL   A HG22 1 
ATOM   1864 H HG23 . VAL   A 1 82  ? 33.954 -6.325  6.802   1.00 15.89 ?  82  VAL   A HG23 1 
ATOM   1865 N N    . LEU   A 1 83  ? 33.455 -1.417  8.151   1.00 10.44 ?  83  LEU   A N    1 
ATOM   1866 C CA   . LEU   A 1 83  ? 33.877 -0.150  8.732   1.00 10.52 ?  83  LEU   A CA   1 
ATOM   1867 C C    . LEU   A 1 83  ? 33.172 0.015   10.074  1.00 10.87 ?  83  LEU   A C    1 
ATOM   1868 O O    . LEU   A 1 83  ? 32.456 -0.878  10.537  1.00 11.28 ?  83  LEU   A O    1 
ATOM   1869 C CB   . LEU   A 1 83  ? 33.617 1.015   7.762   1.00 11.00 ?  83  LEU   A CB   1 
ATOM   1870 C CG   . LEU   A 1 83  ? 34.504 1.018   6.510   1.00 11.79 ?  83  LEU   A CG   1 
ATOM   1871 C CD1  . LEU   A 1 83  ? 34.056 2.065   5.510   1.00 12.32 ?  83  LEU   A CD1  1 
ATOM   1872 C CD2  . LEU   A 1 83  ? 35.973 1.228   6.877   1.00 12.67 ?  83  LEU   A CD2  1 
ATOM   1873 H H    . LEU   A 1 83  ? 32.601 -1.507  8.106   1.00 12.51 ?  83  LEU   A H    1 
ATOM   1874 H HA   . LEU   A 1 83  ? 34.829 -0.180  8.898   1.00 12.60 ?  83  LEU   A HA   1 
ATOM   1875 H HB2  . LEU   A 1 83  ? 32.693 0.976   7.459   1.00 13.17 ?  83  LEU   A HB2  1 
ATOM   1876 H HB3  . LEU   A 1 83  ? 33.767 1.854   8.225   1.00 13.17 ?  83  LEU   A HB3  1 
ATOM   1877 H HG   . LEU   A 1 83  ? 34.436 0.150   6.078   1.00 14.12 ?  83  LEU   A HG   1 
ATOM   1878 H HD11 . LEU   A 1 83  ? 34.638 2.027   4.731   1.00 14.76 ?  83  LEU   A HD11 1 
ATOM   1879 H HD12 . LEU   A 1 83  ? 33.142 1.874   5.245   1.00 14.76 ?  83  LEU   A HD12 1 
ATOM   1880 H HD13 . LEU   A 1 83  ? 34.109 2.938   5.921   1.00 14.76 ?  83  LEU   A HD13 1 
ATOM   1881 H HD21 . LEU   A 1 83  ? 36.484 1.389   6.066   1.00 15.17 ?  83  LEU   A HD21 1 
ATOM   1882 H HD22 . LEU   A 1 83  ? 36.044 1.996   7.466   1.00 15.17 ?  83  LEU   A HD22 1 
ATOM   1883 H HD23 . LEU   A 1 83  ? 36.307 0.436   7.324   1.00 15.17 ?  83  LEU   A HD23 1 
ATOM   1884 N N    . SER   A 1 84  ? 33.388 1.160   10.714  1.00 11.24 ?  84  SER   A N    1 
ATOM   1885 C CA   . SER   A 1 84  ? 32.750 1.403   11.999  1.00 11.58 ?  84  SER   A CA   1 
ATOM   1886 C C    . SER   A 1 84  ? 31.233 1.478   11.859  1.00 11.31 ?  84  SER   A C    1 
ATOM   1887 O O    . SER   A 1 84  ? 30.700 1.944   10.853  1.00 11.79 ?  84  SER   A O    1 
ATOM   1888 C CB   . SER   A 1 84  ? 33.250 2.722   12.579  1.00 12.60 ?  84  SER   A CB   1 
ATOM   1889 O OG   . SER   A 1 84  ? 32.612 2.998   13.812  1.00 13.64 ?  84  SER   A OG   1 
ATOM   1890 H H    . SER   A 1 84  ? 33.886 1.806   10.422  1.00 13.47 ?  84  SER   A H    1 
ATOM   1891 H HA   . SER   A 1 84  ? 32.976 0.687   12.605  1.00 13.87 ?  84  SER   A HA   1 
ATOM   1892 H HB2  . SER   A 1 84  ? 34.208 2.662   12.719  1.00 15.10 ?  84  SER   A HB2  1 
ATOM   1893 H HB3  . SER   A 1 84  ? 33.053 3.439   11.953  1.00 15.10 ?  84  SER   A HB3  1 
ATOM   1894 H HG   . SER   A 1 84  ? 32.897 3.724   14.126  1.00 16.35 ?  84  SER   A HG   1 
ATOM   1895 N N    . GLY   A 1 85  ? 30.535 1.051   12.905  1.00 12.27 ?  85  GLY   A N    1 
ATOM   1896 C CA   . GLY   A 1 85  ? 29.112 1.286   12.998  1.00 12.98 ?  85  GLY   A CA   1 
ATOM   1897 C C    . GLY   A 1 85  ? 28.737 2.587   13.666  1.00 12.65 ?  85  GLY   A C    1 
ATOM   1898 O O    . GLY   A 1 85  ? 27.546 2.888   13.795  1.00 13.41 ?  85  GLY   A O    1 
ATOM   1899 H H    . GLY   A 1 85  ? 30.874 0.617   13.568  1.00 14.70 ?  85  GLY   A H    1 
ATOM   1900 H HA2  . GLY   A 1 85  ? 28.737 1.279   12.101  1.00 15.55 ?  85  GLY   A HA2  1 
ATOM   1901 H HA3  . GLY   A 1 85  ? 28.710 0.567   13.499  1.00 15.55 ?  85  GLY   A HA3  1 
ATOM   1902 N N    . HIS   A 1 86  ? 29.720 3.366   14.109  1.00 12.16 ?  86  HIS   A N    1 
ATOM   1903 C CA   . HIS   A 1 86  ? 29.491 4.696   14.688  1.00 12.85 ?  86  HIS   A CA   1 
ATOM   1904 C C    . HIS   A 1 86  ? 28.510 4.562   15.846  1.00 13.90 ?  86  HIS   A C    1 
ATOM   1905 O O    . HIS   A 1 86  ? 28.694 3.676   16.697  1.00 14.96 ?  86  HIS   A O    1 
ATOM   1906 C CB   . HIS   A 1 86  ? 29.100 5.683   13.596  1.00 13.04 ?  86  HIS   A CB   1 
ATOM   1907 C CG   . HIS   A 1 86  ? 30.141 5.798   12.544  1.00 13.05 ?  86  HIS   A CG   1 
ATOM   1908 N ND1  . HIS   A 1 86  ? 31.223 6.644   12.662  1.00 14.08 ?  86  HIS   A ND1  1 
ATOM   1909 C CD2  . HIS   A 1 86  ? 30.310 5.124   11.385  1.00 13.05 ?  86  HIS   A CD2  1 
ATOM   1910 C CE1  . HIS   A 1 86  ? 32.001 6.501   11.605  1.00 13.94 ?  86  HIS   A CE1  1 
ATOM   1911 N NE2  . HIS   A 1 86  ? 31.476 5.578   10.820  1.00 13.45 ?  86  HIS   A NE2  1 
ATOM   1912 H H    . HIS   A 1 86  ? 30.550 3.143   14.102  1.00 14.57 ?  86  HIS   A H    1 
ATOM   1913 H HA   . HIS   A 1 86  ? 30.331 5.016   15.059  1.00 15.39 ?  86  HIS   A HA   1 
ATOM   1914 H HB2  . HIS   A 1 86  ? 28.276 5.388   13.178  1.00 15.62 ?  86  HIS   A HB2  1 
ATOM   1915 H HB3  . HIS   A 1 86  ? 28.972 6.566   13.988  1.00 15.62 ?  86  HIS   A HB3  1 
ATOM   1916 H HD2  . HIS   A 1 86  ? 29.748 4.464   11.039  1.00 15.63 ?  86  HIS   A HD2  1 
ATOM   1917 H HE1  . HIS   A 1 86  ? 32.786 6.969   11.431  1.00 16.70 ?  86  HIS   A HE1  1 
ATOM   1918 H HE2  . HIS   A 1 86  ? 31.801 5.312   10.063  1.00 16.11 ?  86  HIS   A HE2  1 
ATOM   1919 N N    . ASN   A 1 87  ? 27.492 5.409   15.925  1.00 14.50 ?  87  ASN   A N    1 
ATOM   1920 C CA   . ASN   A 1 87  ? 26.499 5.380   16.986  1.00 15.89 ?  87  ASN   A CA   1 
ATOM   1921 C C    . ASN   A 1 87  ? 25.387 4.372   16.731  1.00 17.20 ?  87  ASN   A C    1 
ATOM   1922 O O    . ASN   A 1 87  ? 24.460 4.291   17.541  1.00 19.25 ?  87  ASN   A O    1 
ATOM   1923 C CB   . ASN   A 1 87  ? 25.890 6.779   17.167  1.00 16.91 ?  87  ASN   A CB   1 
ATOM   1924 C CG   . ASN   A 1 87  ? 25.367 7.373   15.858  1.00 17.59 ?  87  ASN   A CG   1 
ATOM   1925 O OD1  . ASN   A 1 87  ? 26.002 7.266   14.808  1.00 18.39 ?  87  ASN   A OD1  1 
ATOM   1926 N ND2  . ASN   A 1 87  ? 24.211 8.019   15.927  1.00 18.35 ?  87  ASN   A ND2  1 
ATOM   1927 H H    . ASN   A 1 87  ? 27.351 6.030   15.353  1.00 17.37 ?  87  ASN   A H    1 
ATOM   1928 H HA   . ASN   A 1 87  ? 26.928 5.133   17.819  1.00 19.05 ?  87  ASN   A HA   1 
ATOM   1929 H HB2  . ASN   A 1 87  ? 25.146 6.721   17.794  1.00 20.27 ?  87  ASN   A HB2  1 
ATOM   1930 H HB3  . ASN   A 1 87  ? 26.568 7.374   17.518  1.00 20.27 ?  87  ASN   A HB3  1 
ATOM   1931 H HD21 . ASN   A 1 87  ? 23.874 8.374   15.221  1.00 21.99 ?  87  ASN   A HD21 1 
ATOM   1932 H HD22 . ASN   A 1 87  ? 23.794 8.086   16.680  1.00 21.99 ?  87  ASN   A HD22 1 
ATOM   1933 N N    . LEU   A 1 88  ? 25.459 3.597   15.651  1.00 16.52 ?  88  LEU   A N    1 
ATOM   1934 C CA   . LEU   A 1 88  ? 24.356 2.724   15.261  1.00 16.42 ?  88  LEU   A CA   1 
ATOM   1935 C C    . LEU   A 1 88  ? 24.591 1.251   15.562  1.00 16.17 ?  88  LEU   A C    1 
ATOM   1936 O O    . LEU   A 1 88  ? 23.622 0.508   15.751  1.00 17.68 ?  88  LEU   A O    1 
ATOM   1937 C CB   . LEU   A 1 88  ? 24.084 2.874   13.762  1.00 17.45 ?  88  LEU   A CB   1 
ATOM   1938 C CG   . LEU   A 1 88  ? 23.794 4.291   13.270  1.00 19.13 ?  88  LEU   A CG   1 
ATOM   1939 C CD1  . LEU   A 1 88  ? 23.593 4.292   11.765  1.00 19.45 ?  88  LEU   A CD1  1 
ATOM   1940 C CD2  . LEU   A 1 88  ? 22.578 4.870   13.975  1.00 20.79 ?  88  LEU   A CD2  1 
ATOM   1941 H H    . LEU   A 1 88  ? 26.143 3.556   15.129  1.00 19.80 ?  88  LEU   A H    1 
ATOM   1942 H HA   . LEU   A 1 88  ? 23.559 2.998   15.735  1.00 19.68 ?  88  LEU   A HA   1 
ATOM   1943 H HB2  . LEU   A 1 88  ? 24.858 2.555   13.276  1.00 20.92 ?  88  LEU   A HB2  1 
ATOM   1944 H HB3  . LEU   A 1 88  ? 23.313 2.332   13.538  1.00 20.92 ?  88  LEU   A HB3  1 
ATOM   1945 H HG   . LEU   A 1 88  ? 24.557 4.857   13.468  1.00 22.94 ?  88  LEU   A HG   1 
ATOM   1946 H HD11 . LEU   A 1 88  ? 23.417 5.199   11.470  1.00 23.32 ?  88  LEU   A HD11 1 
ATOM   1947 H HD12 . LEU   A 1 88  ? 24.398 3.957   11.338  1.00 23.32 ?  88  LEU   A HD12 1 
ATOM   1948 H HD13 . LEU   A 1 88  ? 22.841 3.721   11.546  1.00 23.32 ?  88  LEU   A HD13 1 
ATOM   1949 H HD21 . LEU   A 1 88  ? 22.350 5.718   13.562  1.00 24.92 ?  88  LEU   A HD21 1 
ATOM   1950 H HD22 . LEU   A 1 88  ? 21.840 4.249   13.888  1.00 24.92 ?  88  LEU   A HD22 1 
ATOM   1951 H HD23 . LEU   A 1 88  ? 22.793 5.004   14.911  1.00 24.92 ?  88  LEU   A HD23 1 
ATOM   1952 N N    . ALA   A 1 89  ? 25.846 0.815   15.595  1.00 14.96 ?  89  ALA   A N    1 
ATOM   1953 C CA   . ALA   A 1 89  ? 26.198 -0.595  15.689  1.00 14.41 ?  89  ALA   A CA   1 
ATOM   1954 C C    . ALA   A 1 89  ? 27.685 -0.650  15.993  1.00 14.87 ?  89  ALA   A C    1 
ATOM   1955 O O    . ALA   A 1 89  ? 28.387 0.355   15.884  1.00 15.51 ?  89  ALA   A O    1 
ATOM   1956 C CB   . ALA   A 1 89  ? 25.911 -1.312  14.370  1.00 13.69 ?  89  ALA   A CB   1 
ATOM   1957 H H    . ALA   A 1 89  ? 26.531 1.335   15.554  1.00 17.93 ?  89  ALA   A H    1 
ATOM   1958 H HA   . ALA   A 1 89  ? 25.700 -1.018  16.406  1.00 17.27 ?  89  ALA   A HA   1 
ATOM   1959 H HB1  . ALA   A 1 89  ? 26.172 -2.245  14.456  1.00 16.40 ?  89  ALA   A HB1  1 
ATOM   1960 H HB2  . ALA   A 1 89  ? 24.959 -1.257  14.179  1.00 16.40 ?  89  ALA   A HB2  1 
ATOM   1961 H HB3  . ALA   A 1 89  ? 26.417 -0.892  13.662  1.00 16.40 ?  89  ALA   A HB3  1 
ATOM   1962 N N    . LYS   A 1 90  ? 28.178 -1.834  16.354  1.00 15.29 ?  90  LYS   A N    1 
ATOM   1963 C CA   . LYS   A 1 90  ? 29.623 -1.976  16.500  1.00 15.95 ?  90  LYS   A CA   1 
ATOM   1964 C C    . LYS   A 1 90  ? 30.316 -1.778  15.155  1.00 14.70 ?  90  LYS   A C    1 
ATOM   1965 O O    . LYS   A 1 90  ? 31.257 -0.978  15.028  1.00 16.13 ?  90  LYS   A O    1 
ATOM   1966 C CB   . LYS   A 1 90  ? 29.965 -3.338  17.108  1.00 19.22 ?  90  LYS   A CB   1 
ATOM   1967 C CG   . LYS   A 1 90  ? 31.442 -3.483  17.444  1.00 23.59 ?  90  LYS   A CG   1 
ATOM   1968 C CD   . LYS   A 1 90  ? 31.709 -4.731  18.270  1.00 27.42 ?  90  LYS   A CD   1 
ATOM   1969 C CE   . LYS   A 1 90  ? 33.113 -4.723  18.859  1.00 30.33 ?  90  LYS   A CE   1 
ATOM   1970 N NZ   . LYS   A 1 90  ? 34.176 -4.883  17.829  1.00 32.42 ?  90  LYS   A NZ   1 
ATOM   1971 H H    . LYS   A 1 90  ? 27.714 -2.540  16.514  1.00 18.32 ?  90  LYS   A H    1 
ATOM   1972 H HA   . LYS   A 1 90  ? 29.943 -1.291  17.108  1.00 19.12 ?  90  LYS   A HA   1 
ATOM   1973 H HB2  . LYS   A 1 90  ? 29.457 -3.454  17.930  1.00 23.03 ?  90  LYS   A HB2  1 
ATOM   1974 H HB3  . LYS   A 1 90  ? 29.729 -4.034  16.476  1.00 23.03 ?  90  LYS   A HB3  1 
ATOM   1975 H HG2  . LYS   A 1 90  ? 31.950 -3.549  16.621  1.00 28.28 ?  90  LYS   A HG2  1 
ATOM   1976 H HG3  . LYS   A 1 90  ? 31.730 -2.712  17.956  1.00 28.28 ?  90  LYS   A HG3  1 
ATOM   1977 H HD2  . LYS   A 1 90  ? 31.073 -4.773  19.002  1.00 32.88 ?  90  LYS   A HD2  1 
ATOM   1978 H HD3  . LYS   A 1 90  ? 31.622 -5.514  17.704  1.00 32.88 ?  90  LYS   A HD3  1 
ATOM   1979 H HE2  . LYS   A 1 90  ? 33.261 -3.876  19.311  1.00 36.37 ?  90  LYS   A HE2  1 
ATOM   1980 H HE3  . LYS   A 1 90  ? 33.196 -5.453  19.491  1.00 36.37 ?  90  LYS   A HE3  1 
ATOM   1981 H HZ1  . LYS   A 1 90  ? 34.978 -4.873  18.216  1.00 38.88 ?  90  LYS   A HZ1  1 
ATOM   1982 H HZ2  . LYS   A 1 90  ? 34.071 -5.658  17.404  1.00 38.88 ?  90  LYS   A HZ2  1 
ATOM   1983 H HZ3  . LYS   A 1 90  ? 34.131 -4.220  17.239  1.00 38.88 ?  90  LYS   A HZ3  1 
ATOM   1984 N N    . HIS   A 1 91  ? 29.833 -2.475  14.130  1.00 12.84 ?  91  HIS   A N    1 
ATOM   1985 C CA   . HIS   A 1 91  ? 30.396 -2.444  12.795  1.00 12.21 ?  91  HIS   A CA   1 
ATOM   1986 C C    . HIS   A 1 91  ? 29.293 -2.169  11.790  1.00 10.85 ?  91  HIS   A C    1 
ATOM   1987 O O    . HIS   A 1 91  ? 28.131 -2.547  11.993  1.00 11.65 ?  91  HIS   A O    1 
ATOM   1988 C CB   . HIS   A 1 91  ? 30.996 -3.806  12.414  1.00 14.48 ?  91  HIS   A CB   1 
ATOM   1989 C CG   . HIS   A 1 91  ? 32.000 -4.327  13.391  1.00 19.13 ?  91  HIS   A CG   1 
ATOM   1990 N ND1  . HIS   A 1 91  ? 33.284 -3.833  13.471  1.00 21.20 ?  91  HIS   A ND1  1 
ATOM   1991 C CD2  . HIS   A 1 91  ? 31.918 -5.310  14.319  1.00 21.04 ?  91  HIS   A CD2  1 
ATOM   1992 C CE1  . HIS   A 1 91  ? 33.948 -4.484  14.410  1.00 22.13 ?  91  HIS   A CE1  1 
ATOM   1993 N NE2  . HIS   A 1 91  ? 33.141 -5.385  14.941  1.00 22.35 ?  91  HIS   A NE2  1 
ATOM   1994 H H    . HIS   A 1 91  ? 29.152 -3.008  14.198  1.00 15.39 ?  91  HIS   A H    1 
ATOM   1995 H HA   . HIS   A 1 91  ? 31.079 -1.766  12.729  1.00 14.63 ?  91  HIS   A HA   1 
ATOM   1996 H HB2  . HIS   A 1 91  ? 30.283 -4.464  12.358  1.00 17.35 ?  91  HIS   A HB2  1 
ATOM   1997 H HB3  . HIS   A 1 91  ? 31.438 -3.728  11.556  1.00 17.35 ?  91  HIS   A HB3  1 
ATOM   1998 H HD1  . HIS   A 1 91  ? 33.606 -3.201  12.984  1.00 25.41 ?  91  HIS   A HD1  1 
ATOM   1999 H HD2  . HIS   A 1 91  ? 31.177 -5.834  14.508  1.00 25.22 ?  91  HIS   A HD2  1 
ATOM   2000 H HE1  . HIS   A 1 91  ? 34.836 -4.330  14.657  1.00 26.53 ?  91  HIS   A HE1  1 
ATOM   2001 N N    . CYS   A 1 92  ? 29.679 -1.554  10.677  1.00 10.59 ?  92  CYS   A N    1 
ATOM   2002 C CA   . CYS   A 1 92  ? 28.830 -1.471  9.499   1.00 10.25 ?  92  CYS   A CA   1 
ATOM   2003 C C    . CYS   A 1 92  ? 29.469 -2.279  8.380   1.00 9.78  ?  92  CYS   A C    1 
ATOM   2004 O O    . CYS   A 1 92  ? 30.625 -2.023  8.007   1.00 10.42 ?  92  CYS   A O    1 
ATOM   2005 C CB   . CYS   A 1 92  ? 28.610 -0.024  9.054   1.00 10.67 ?  92  CYS   A CB   1 
ATOM   2006 S SG   . CYS   A 1 92  ? 27.576 0.094   7.556   1.00 10.49 ?  92  CYS   A SG   1 
ATOM   2007 H H    . CYS   A 1 92  ? 30.442 -1.163  10.586  1.00 12.69 ?  92  CYS   A H    1 
ATOM   2008 H HA   . CYS   A 1 92  ? 27.966 -1.858  9.705   1.00 12.27 ?  92  CYS   A HA   1 
ATOM   2009 H HB2  . CYS   A 1 92  ? 28.160 0.465   9.763   1.00 12.78 ?  92  CYS   A HB2  1 
ATOM   2010 H HB3  . CYS   A 1 92  ? 29.467 0.385   8.861   1.00 12.78 ?  92  CYS   A HB3  1 
ATOM   2011 H HG   . CYS   A 1 92  ? 27.441 1.245   7.273   1.00 12.56 ?  92  CYS   A HG   1 
ATOM   2012 N N    . LEU   A 1 93  ? 28.729 -3.262  7.871   1.00 9.59  ?  93  LEU   A N    1 
ATOM   2013 C CA   . LEU   A 1 93  ? 29.120 -4.014  6.685   1.00 9.38  ?  93  LEU   A CA   1 
ATOM   2014 C C    . LEU   A 1 93  ? 28.517 -3.308  5.477   1.00 9.05  ?  93  LEU   A C    1 
ATOM   2015 O O    . LEU   A 1 93  ? 27.298 -3.366  5.263   1.00 9.06  ?  93  LEU   A O    1 
ATOM   2016 C CB   . LEU   A 1 93  ? 28.632 -5.459  6.785   1.00 9.94  ?  93  LEU   A CB   1 
ATOM   2017 C CG   . LEU   A 1 93  ? 29.026 -6.351  5.608   1.00 9.87  ?  93  LEU   A CG   1 
ATOM   2018 C CD1  . LEU   A 1 93  ? 30.530 -6.593  5.595   1.00 11.16 ?  93  LEU   A CD1  1 
ATOM   2019 C CD2  . LEU   A 1 93  ? 28.264 -7.686  5.618   1.00 10.67 ?  93  LEU   A CD2  1 
ATOM   2020 H H    . LEU   A 1 93  ? 27.975 -3.512  8.213   1.00 11.48 ?  93  LEU   A H    1 
ATOM   2021 H HA   . LEU   A 1 93  ? 30.083 -4.013  6.611   1.00 11.24 ?  93  LEU   A HA   1 
ATOM   2022 H HB2  . LEU   A 1 93  ? 28.998 -5.856  7.592   1.00 11.91 ?  93  LEU   A HB2  1 
ATOM   2023 H HB3  . LEU   A 1 93  ? 27.662 -5.455  6.840   1.00 11.91 ?  93  LEU   A HB3  1 
ATOM   2024 H HG   . LEU   A 1 93  ? 28.798 -5.898  4.786   1.00 11.82 ?  93  LEU   A HG   1 
ATOM   2025 H HD11 . LEU   A 1 93  ? 30.753 -7.218  4.888   1.00 13.37 ?  93  LEU   A HD11 1 
ATOM   2026 H HD12 . LEU   A 1 93  ? 30.992 -5.750  5.445   1.00 13.37 ?  93  LEU   A HD12 1 
ATOM   2027 H HD13 . LEU   A 1 93  ? 30.807 -6.963  6.455   1.00 13.37 ?  93  LEU   A HD13 1 
ATOM   2028 H HD21 . LEU   A 1 93  ? 28.555 -8.218  4.852   1.00 12.78 ?  93  LEU   A HD21 1 
ATOM   2029 H HD22 . LEU   A 1 93  ? 28.465 -8.164  6.438   1.00 12.78 ?  93  LEU   A HD22 1 
ATOM   2030 H HD23 . LEU   A 1 93  ? 27.315 -7.514  5.554   1.00 12.78 ?  93  LEU   A HD23 1 
ATOM   2031 N N    . HIS   A 1 94  ? 29.364 -2.608  4.720   1.00 8.55  ?  94  HIS   A N    1 
ATOM   2032 C CA   . HIS   A 1 94  ? 28.932 -1.928  3.504   1.00 8.77  ?  94  HIS   A CA   1 
ATOM   2033 C C    . HIS   A 1 94  ? 28.935 -2.956  2.388   1.00 8.77  ?  94  HIS   A C    1 
ATOM   2034 O O    . HIS   A 1 94  ? 30.002 -3.461  2.032   1.00 10.08 ?  94  HIS   A O    1 
ATOM   2035 C CB   . HIS   A 1 94  ? 29.876 -0.774  3.175   1.00 8.94  ?  94  HIS   A CB   1 
ATOM   2036 C CG   . HIS   A 1 94  ? 29.869 0.312   4.197   1.00 9.09  ?  94  HIS   A CG   1 
ATOM   2037 N ND1  . HIS   A 1 94  ? 28.989 1.373   4.154   1.00 9.18  ?  94  HIS   A ND1  1 
ATOM   2038 C CD2  . HIS   A 1 94  ? 30.619 0.475   5.310   1.00 9.67  ?  94  HIS   A CD2  1 
ATOM   2039 C CE1  . HIS   A 1 94  ? 29.211 2.147   5.200   1.00 9.41  ?  94  HIS   A CE1  1 
ATOM   2040 N NE2  . HIS   A 1 94  ? 30.193 1.627   5.916   1.00 9.82  ?  94  HIS   A NE2  1 
ATOM   2041 H H    . HIS   A 1 94  ? 30.202 -2.512  4.894   1.00 10.24 ?  94  HIS   A H    1 
ATOM   2042 H HA   . HIS   A 1 94  ? 28.028 -1.592  3.619   1.00 10.50 ?  94  HIS   A HA   1 
ATOM   2043 H HB2  . HIS   A 1 94  ? 30.775 -1.118  3.108   1.00 10.70 ?  94  HIS   A HB2  1 
ATOM   2044 H HB3  . HIS   A 1 94  ? 29.602 -0.385  2.329   1.00 10.70 ?  94  HIS   A HB3  1 
ATOM   2045 H HD2  . HIS   A 1 94  ? 31.303 -0.079  5.606   1.00 11.58 ?  94  HIS   A HD2  1 
ATOM   2046 H HE1  . HIS   A 1 94  ? 28.746 2.929   5.400   1.00 11.27 ?  94  HIS   A HE1  1 
ATOM   2047 H HE2  . HIS   A 1 94  ? 30.518 1.969   6.638   1.00 11.76 ?  94  HIS   A HE2  1 
ATOM   2048 N N    . VAL   A 1 95  ? 27.762 -3.274  1.842   1.00 7.97  ?  95  VAL   A N    1 
ATOM   2049 C CA   . VAL   A 1 95  ? 27.617 -4.303  0.817   1.00 8.59  ?  95  VAL   A CA   1 
ATOM   2050 C C    . VAL   A 1 95  ? 27.063 -3.665  -0.443  1.00 8.22  ?  95  VAL   A C    1 
ATOM   2051 O O    . VAL   A 1 95  ? 26.062 -2.942  -0.384  1.00 8.91  ?  95  VAL   A O    1 
ATOM   2052 C CB   . VAL   A 1 95  ? 26.697 -5.455  1.268   1.00 9.11  ?  95  VAL   A CB   1 
ATOM   2053 C CG1  . VAL   A 1 95  ? 26.594 -6.500  0.168   1.00 10.33 ?  95  VAL   A CG1  1 
ATOM   2054 C CG2  . VAL   A 1 95  ? 27.198 -6.070  2.557   1.00 9.63  ?  95  VAL   A CG2  1 
ATOM   2055 H H    . VAL   A 1 95  ? 27.014 -2.897  2.050   1.00 9.54  ?  95  VAL   A H    1 
ATOM   2056 H HA   . VAL   A 1 95  ? 28.486 -4.676  0.608   1.00 10.28 ?  95  VAL   A HA   1 
ATOM   2057 H HB   . VAL   A 1 95  ? 25.810 -5.107  1.426   1.00 10.91 ?  95  VAL   A HB   1 
ATOM   2058 H HG11 . VAL   A 1 95  ? 26.191 -7.310  0.533   1.00 12.37 ?  95  VAL   A HG11 1 
ATOM   2059 H HG12 . VAL   A 1 95  ? 26.038 -6.163  -0.553  1.00 12.37 ?  95  VAL   A HG12 1 
ATOM   2060 H HG13 . VAL   A 1 95  ? 27.481 -6.707  -0.169  1.00 12.37 ?  95  VAL   A HG13 1 
ATOM   2061 H HG21 . VAL   A 1 95  ? 26.641 -6.832  2.781   1.00 11.53 ?  95  VAL   A HG21 1 
ATOM   2062 H HG22 . VAL   A 1 95  ? 28.116 -6.352  2.440   1.00 11.53 ?  95  VAL   A HG22 1 
ATOM   2063 H HG23 . VAL   A 1 95  ? 27.142 -5.404  3.262   1.00 11.53 ?  95  VAL   A HG23 1 
ATOM   2064 N N    . VAL   A 1 96  ? 27.692 -3.940  -1.578  1.00 8.57  ?  96  VAL   A N    1 
ATOM   2065 C CA   . VAL   A 1 96  ? 27.281 -3.382  -2.856  1.00 9.31  ?  96  VAL   A CA   1 
ATOM   2066 C C    . VAL   A 1 96  ? 26.470 -4.425  -3.618  1.00 9.27  ?  96  VAL   A C    1 
ATOM   2067 O O    . VAL   A 1 96  ? 27.024 -5.360  -4.203  1.00 10.20 ?  96  VAL   A O    1 
ATOM   2068 C CB   . VAL   A 1 96  ? 28.475 -2.899  -3.680  1.00 9.62  ?  96  VAL   A CB   1 
ATOM   2069 C CG1  . VAL   A 1 96  ? 27.968 -2.245  -4.950  1.00 9.90  ?  96  VAL   A CG1  1 
ATOM   2070 C CG2  . VAL   A 1 96  ? 29.342 -1.939  -2.866  1.00 10.43 ?  96  VAL   A CG2  1 
ATOM   2071 H H    . VAL   A 1 96  ? 28.376 -4.458  -1.636  1.00 10.25 ?  96  VAL   A H    1 
ATOM   2072 H HA   . VAL   A 1 96  ? 26.707 -2.612  -2.694  1.00 11.15 ?  96  VAL   A HA   1 
ATOM   2073 H HB   . VAL   A 1 96  ? 29.020 -3.658  -3.927  1.00 11.52 ?  96  VAL   A HB   1 
ATOM   2074 H HG11 . VAL   A 1 96  ? 28.708 -1.772  -5.369  1.00 11.86 ?  96  VAL   A HG11 1 
ATOM   2075 H HG12 . VAL   A 1 96  ? 27.633 -2.926  -5.545  1.00 11.86 ?  96  VAL   A HG12 1 
ATOM   2076 H HG13 . VAL   A 1 96  ? 27.267 -1.616  -4.722  1.00 11.86 ?  96  VAL   A HG13 1 
ATOM   2077 H HG21 . VAL   A 1 96  ? 30.041 -1.581  -3.432  1.00 12.50 ?  96  VAL   A HG21 1 
ATOM   2078 H HG22 . VAL   A 1 96  ? 28.785 -1.215  -2.530  1.00 12.50 ?  96  VAL   A HG22 1 
ATOM   2079 H HG23 . VAL   A 1 96  ? 29.733 -2.421  -2.118  1.00 12.50 ?  96  VAL   A HG23 1 
ATOM   2080 N N    . GLY   A 1 97  ? 25.151 -4.264  -3.638  1.00 9.22  ?  97  GLY   A N    1 
ATOM   2081 C CA   . GLY   A 1 97  ? 24.334 -5.022  -4.548  1.00 9.86  ?  97  GLY   A CA   1 
ATOM   2082 C C    . GLY   A 1 97  ? 24.329 -4.360  -5.913  1.00 9.89  ?  97  GLY   A C    1 
ATOM   2083 O O    . GLY   A 1 97  ? 24.616 -3.165  -6.045  1.00 11.03 ?  97  GLY   A O    1 
ATOM   2084 H H    . GLY   A 1 97  ? 24.704 -3.715  -3.136  1.00 11.04 ?  97  GLY   A H    1 
ATOM   2085 H HA2  . GLY   A 1 97  ? 24.696 -5.922  -4.620  1.00 11.80 ?  97  GLY   A HA2  1 
ATOM   2086 H HA3  . GLY   A 1 97  ? 23.424 -5.079  -4.217  1.00 11.80 ?  97  GLY   A HA3  1 
ATOM   2087 N N    A PRO   A 1 98  ? 23.960 -5.100  -6.955  0.40 9.99  ?  98  PRO   A N    1 
ATOM   2088 N N    B PRO   A 1 98  ? 24.039 -5.135  -6.958  0.60 10.05 ?  98  PRO   A N    1 
ATOM   2089 C CA   A PRO   A 1 98  ? 23.838 -4.475  -8.278  0.40 10.64 ?  98  PRO   A CA   1 
ATOM   2090 C CA   B PRO   A 1 98  ? 23.942 -4.549  -8.298  0.60 11.53 ?  98  PRO   A CA   1 
ATOM   2091 C C    A PRO   A 1 98  ? 22.729 -3.428  -8.308  0.40 10.61 ?  98  PRO   A C    1 
ATOM   2092 C C    B PRO   A 1 98  ? 22.818 -3.529  -8.369  0.60 12.45 ?  98  PRO   A C    1 
ATOM   2093 O O    A PRO   A 1 98  ? 21.636 -3.636  -7.777  0.40 10.68 ?  98  PRO   A O    1 
ATOM   2094 O O    B PRO   A 1 98  ? 21.771 -3.679  -7.735  0.60 12.48 ?  98  PRO   A O    1 
ATOM   2095 C CB   A PRO   A 1 98  ? 23.521 -5.660  -9.199  0.40 11.12 ?  98  PRO   A CB   1 
ATOM   2096 C CB   B PRO   A 1 98  ? 23.654 -5.761  -9.195  0.60 11.79 ?  98  PRO   A CB   1 
ATOM   2097 C CG   A PRO   A 1 98  ? 22.892 -6.682  -8.305  0.40 11.19 ?  98  PRO   A CG   1 
ATOM   2098 C CG   B PRO   A 1 98  ? 23.049 -6.781  -8.279  0.60 12.11 ?  98  PRO   A CG   1 
ATOM   2099 C CD   A PRO   A 1 98  ? 23.586 -6.527  -6.975  0.40 10.36 ?  98  PRO   A CD   1 
ATOM   2100 C CD   B PRO   A 1 98  ? 23.751 -6.582  -6.965  0.60 10.44 ?  98  PRO   A CD   1 
ATOM   2101 H HA   A PRO   A 1 98  ? 24.677 -4.073  -8.541  0.40 12.74 ?  98  PRO   A HA   1 
ATOM   2102 H HA   B PRO   A 1 98  ? 24.781 -4.139  -8.551  0.60 13.82 ?  98  PRO   A HA   1 
ATOM   2103 H HB2  A PRO   A 1 98  ? 22.898 -5.383  -9.890  0.40 13.32 ?  98  PRO   A HB2  1 
ATOM   2104 H HB2  B PRO   A 1 98  ? 23.023 -5.505  -9.892  0.60 14.12 ?  98  PRO   A HB2  1 
ATOM   2105 H HB3  A PRO   A 1 98  ? 24.339 -6.004  -9.589  0.40 13.32 ?  98  PRO   A HB3  1 
ATOM   2106 H HB3  B PRO   A 1 98  ? 24.479 -6.084  -9.582  0.60 14.12 ?  98  PRO   A HB3  1 
ATOM   2107 H HG2  A PRO   A 1 98  ? 21.944 -6.503  -8.223  0.40 13.40 ?  98  PRO   A HG2  1 
ATOM   2108 H HG2  B PRO   A 1 98  ? 22.097 -6.619  -8.192  0.60 14.51 ?  98  PRO   A HG2  1 
ATOM   2109 H HG3  A PRO   A 1 98  ? 23.044 -7.569  -8.670  0.40 13.40 ?  98  PRO   A HG3  1 
ATOM   2110 H HG3  B PRO   A 1 98  ? 23.216 -7.670  -8.630  0.60 14.51 ?  98  PRO   A HG3  1 
ATOM   2111 H HD2  A PRO   A 1 98  ? 22.970 -6.733  -6.250  0.40 12.40 ?  98  PRO   A HD2  1 
ATOM   2112 H HD2  B PRO   A 1 98  ? 23.162 -6.822  -6.229  0.60 12.50 ?  98  PRO   A HD2  1 
ATOM   2113 H HD3  A PRO   A 1 98  ? 24.377 -7.087  -6.936  0.40 12.40 ?  98  PRO   A HD3  1 
ATOM   2114 H HD3  B PRO   A 1 98  ? 24.577 -7.089  -6.939  0.60 12.50 ?  98  PRO   A HD3  1 
ATOM   2115 N N    A ASN   A 1 99  ? 23.027 -2.286  -8.932  0.40 10.64 ?  99  ASN   A N    1 
ATOM   2116 N N    B ASN   A 1 99  ? 23.049 -2.484  -9.154  0.60 14.11 ?  99  ASN   A N    1 
ATOM   2117 C CA   A ASN   A 1 99  ? 22.055 -1.212  -9.154  0.40 10.69 ?  99  ASN   A CA   1 
ATOM   2118 C CA   B ASN   A 1 99  ? 22.078 -1.422  -9.376  0.60 16.38 ?  99  ASN   A CA   1 
ATOM   2119 C C    A ASN   A 1 99  ? 21.530 -1.361  -10.578 0.40 11.76 ?  99  ASN   A C    1 
ATOM   2120 C C    B ASN   A 1 99  ? 21.434 -1.647  -10.738 0.60 17.08 ?  99  ASN   A C    1 
ATOM   2121 O O    A ASN   A 1 99  ? 22.172 -0.924  -11.542 0.40 11.90 ?  99  ASN   A O    1 
ATOM   2122 O O    B ASN   A 1 99  ? 22.122 -1.648  -11.766 0.60 17.58 ?  99  ASN   A O    1 
ATOM   2123 C CB   A ASN   A 1 99  ? 22.693 0.156   -8.930  0.40 10.16 ?  99  ASN   A CB   1 
ATOM   2124 C CB   B ASN   A 1 99  ? 22.765 -0.057  -9.322  0.60 18.97 ?  99  ASN   A CB   1 
ATOM   2125 C CG   A ASN   A 1 99  ? 21.676 1.302   -8.957  0.40 10.16 ?  99  ASN   A CG   1 
ATOM   2126 C CG   B ASN   A 1 99  ? 21.797 1.105   -9.516  0.60 21.61 ?  99  ASN   A CG   1 
ATOM   2127 O OD1  A ASN   A 1 99  ? 20.694 1.279   -9.705  0.40 10.79 ?  99  ASN   A OD1  1 
ATOM   2128 O OD1  B ASN   A 1 99  ? 20.614 0.913   -9.803  0.60 22.48 ?  99  ASN   A OD1  1 
ATOM   2129 N ND2  A ASN   A 1 99  ? 21.922 2.312   -8.140  0.40 10.08 ?  99  ASN   A ND2  1 
ATOM   2130 N ND2  B ASN   A 1 99  ? 22.307 2.323   -9.359  0.60 22.94 ?  99  ASN   A ND2  1 
ATOM   2131 H H    A ASN   A 1 99  ? 23.809 -2.107  -9.234  0.40 12.74 ?  99  ASN   A H    1 
ATOM   2132 H H    B ASN   A 1 99  ? 23.787 -2.356  -9.575  0.60 16.90 ?  99  ASN   A H    1 
ATOM   2133 H HA   A ASN   A 1 99  ? 21.313 -1.314  -8.532  0.40 12.80 ?  99  ASN   A HA   1 
ATOM   2134 H HA   B ASN   A 1 99  ? 21.391 -1.448  -8.687  0.60 19.63 ?  99  ASN   A HA   1 
ATOM   2135 H HB2  A ASN   A 1 99  ? 23.136 0.161   -8.065  0.40 12.17 ?  99  ASN   A HB2  1 
ATOM   2136 H HB2  B ASN   A 1 99  ? 23.185 0.053   -8.451  0.60 22.74 ?  99  ASN   A HB2  1 
ATOM   2137 H HB3  A ASN   A 1 99  ? 23.344 0.314   -9.633  0.40 12.17 ?  99  ASN   A HB3  1 
ATOM   2138 H HB3  B ASN   A 1 99  ? 23.442 -0.012  -10.010 0.60 22.74 ?  99  ASN   A HB3  1 
ATOM   2139 H HD21 A ASN   A 1 99  ? 21.383 2.980   -8.113  0.40 12.07 ?  99  ASN   A HD21 1 
ATOM   2140 H HD21 B ASN   A 1 99  ? 21.814 3.025   -9.452  0.60 27.51 ?  99  ASN   A HD21 1 
ATOM   2141 H HD22 A ASN   A 1 99  ? 22.619 2.301   -7.634  0.40 12.07 ?  99  ASN   A HD22 1 
ATOM   2142 H HD22 B ASN   A 1 99  ? 23.143 2.415   -9.173  0.60 27.51 ?  99  ASN   A HD22 1 
ATOM   2143 N N    A VAL   A 1 100 ? 20.356 -1.990  -10.699 0.40 13.55 ?  100 VAL   A N    1 
ATOM   2144 N N    B VAL   A 1 100 ? 20.116 -1.855  -10.737 0.60 17.73 ?  100 VAL   A N    1 
ATOM   2145 C CA   A VAL   A 1 100 ? 19.753 -2.261  -12.002 0.40 16.57 ?  100 VAL   A CA   1 
ATOM   2146 C CA   B VAL   A 1 100 ? 19.399 -2.019  -11.995 0.60 19.61 ?  100 VAL   A CA   1 
ATOM   2147 C C    A VAL   A 1 100 ? 19.632 -0.990  -12.829 0.40 18.57 ?  100 VAL   A C    1 
ATOM   2148 C C    B VAL   A 1 100 ? 19.324 -0.695  -12.742 0.60 20.08 ?  100 VAL   A C    1 
ATOM   2149 O O    A VAL   A 1 100 ? 19.755 -1.027  -14.060 0.40 19.65 ?  100 VAL   A O    1 
ATOM   2150 O O    B VAL   A 1 100 ? 19.370 -0.663  -13.978 0.60 20.23 ?  100 VAL   A O    1 
ATOM   2151 C CB   A VAL   A 1 100 ? 18.392 -2.967  -11.813 0.40 17.54 ?  100 VAL   A CB   1 
ATOM   2152 C CB   B VAL   A 1 100 ? 18.006 -2.623  -11.740 0.60 20.97 ?  100 VAL   A CB   1 
ATOM   2153 C CG1  A VAL   A 1 100 ? 17.709 -3.204  -13.152 0.40 18.13 ?  100 VAL   A CG1  1 
ATOM   2154 C CG1  B VAL   A 1 100 ? 17.196 -2.648  -13.025 0.60 21.50 ?  100 VAL   A CG1  1 
ATOM   2155 C CG2  A VAL   A 1 100 ? 18.582 -4.283  -11.069 0.40 17.88 ?  100 VAL   A CG2  1 
ATOM   2156 C CG2  B VAL   A 1 100 ? 18.138 -4.018  -11.156 0.60 21.64 ?  100 VAL   A CG2  1 
ATOM   2157 H H    A VAL   A 1 100 ? 19.886 -2.276  -10.033 0.40 16.24 ?  100 VAL   A H    1 
ATOM   2158 H H    B VAL   A 1 100 ? 19.624 -1.903  -10.028 0.60 21.25 ?  100 VAL   A H    1 
ATOM   2159 H HA   A VAL   A 1 100 ? 20.327 -2.873  -12.488 0.40 19.86 ?  100 VAL   A HA   1 
ATOM   2160 H HA   B VAL   A 1 100 ? 19.892 -2.644  -12.543 0.60 23.51 ?  100 VAL   A HA   1 
ATOM   2161 H HB   A VAL   A 1 100 ? 17.813 -2.404  -11.278 0.40 21.02 ?  100 VAL   A HB   1 
ATOM   2162 H HB   B VAL   A 1 100 ? 17.534 -2.076  -11.095 0.60 25.14 ?  100 VAL   A HB   1 
ATOM   2163 H HG11 A VAL   A 1 100 ? 16.960 -3.807  -13.022 0.40 21.73 ?  100 VAL   A HG11 1 
ATOM   2164 H HG11 B VAL   A 1 100 ? 16.431 -3.230  -12.902 0.60 25.78 ?  100 VAL   A HG11 1 
ATOM   2165 H HG12 A VAL   A 1 100 ? 17.391 -2.356  -13.500 0.40 21.73 ?  100 VAL   A HG12 1 
ATOM   2166 H HG12 B VAL   A 1 100 ? 16.898 -1.748  -13.229 0.60 25.78 ?  100 VAL   A HG12 1 
ATOM   2167 H HG13 A VAL   A 1 100 ? 18.346 -3.598  -13.767 0.40 21.73 ?  100 VAL   A HG13 1 
ATOM   2168 H HG13 B VAL   A 1 100 ? 17.756 -2.985  -13.741 0.60 25.78 ?  100 VAL   A HG13 1 
ATOM   2169 H HG21 A VAL   A 1 100 ? 17.738 -4.763  -11.055 0.40 21.43 ?  100 VAL   A HG21 1 
ATOM   2170 H HG21 B VAL   A 1 100 ? 17.252 -4.393  -11.030 0.60 25.94 ?  100 VAL   A HG21 1 
ATOM   2171 H HG22 A VAL   A 1 100 ? 19.254 -4.810  -11.528 0.40 21.43 ?  100 VAL   A HG22 1 
ATOM   2172 H HG22 B VAL   A 1 100 ? 18.646 -4.569  -11.770 0.60 25.94 ?  100 VAL   A HG22 1 
ATOM   2173 H HG23 A VAL   A 1 100 ? 18.869 -4.096  -10.162 0.40 21.43 ?  100 VAL   A HG23 1 
ATOM   2174 H HG23 B VAL   A 1 100 ? 18.598 -3.963  -10.303 0.60 25.94 ?  100 VAL   A HG23 1 
ATOM   2175 N N    A ASN   A 1 101 ? 19.401 0.152   -12.180 0.40 19.76 ?  101 ASN   A N    1 
ATOM   2176 N N    B ASN   A 1 101 ? 19.211 0.414   -12.016 0.60 21.75 ?  101 ASN   A N    1 
ATOM   2177 C CA   A ASN   A 1 101 ? 19.338 1.420   -12.898 0.40 21.41 ?  101 ASN   A CA   1 
ATOM   2178 C CA   B ASN   A 1 101 ? 19.169 1.720   -12.659 0.60 24.15 ?  101 ASN   A CA   1 
ATOM   2179 C C    A ASN   A 1 101 ? 20.685 1.827   -13.488 0.40 22.72 ?  101 ASN   A C    1 
ATOM   2180 C C    B ASN   A 1 101 ? 20.537 2.172   -13.168 0.60 26.83 ?  101 ASN   A C    1 
ATOM   2181 O O    A ASN   A 1 101 ? 20.737 2.783   -14.270 0.40 23.21 ?  101 ASN   A O    1 
ATOM   2182 O O    B ASN   A 1 101 ? 20.621 3.225   -13.814 0.60 27.86 ?  101 ASN   A O    1 
ATOM   2183 C CB   A ASN   A 1 101 ? 18.773 2.504   -11.977 0.40 21.28 ?  101 ASN   A CB   1 
ATOM   2184 C CB   B ASN   A 1 101 ? 18.536 2.733   -11.704 0.60 23.78 ?  101 ASN   A CB   1 
ATOM   2185 C CG   A ASN   A 1 101 ? 17.436 2.106   -11.365 0.40 21.10 ?  101 ASN   A CG   1 
ATOM   2186 C CG   B ASN   A 1 101 ? 17.138 2.318   -11.268 0.60 23.45 ?  101 ASN   A CG   1 
ATOM   2187 O OD1  A ASN   A 1 101 ? 16.568 1.548   -12.040 0.40 21.82 ?  101 ASN   A OD1  1 
ATOM   2188 O OD1  B ASN   A 1 101 ? 16.334 1.860   -12.084 0.60 23.88 ?  101 ASN   A OD1  1 
ATOM   2189 N ND2  A ASN   A 1 101 ? 17.274 2.377   -10.076 0.40 20.53 ?  101 ASN   A ND2  1 
ATOM   2190 N ND2  B ASN   A 1 101 ? 16.847 2.460   -9.978  0.60 22.82 ?  101 ASN   A ND2  1 
ATOM   2191 H H    A ASN   A 1 101 ? 19.279 0.214   -11.330 0.40 23.69 ?  101 ASN   A H    1 
ATOM   2192 H H    B ASN   A 1 101 ? 19.148 0.427   -11.157 0.60 26.08 ?  101 ASN   A H    1 
ATOM   2193 H HA   A ASN   A 1 101 ? 18.725 1.322   -13.637 0.40 25.67 ?  101 ASN   A HA   1 
ATOM   2194 H HA   B ASN   A 1 101 ? 18.586 1.648   -13.426 0.60 28.95 ?  101 ASN   A HA   1 
ATOM   2195 H HB2  A ASN   A 1 101 ? 19.395 2.670   -11.253 0.40 25.51 ?  101 ASN   A HB2  1 
ATOM   2196 H HB2  B ASN   A 1 101 ? 19.087 2.815   -10.912 0.60 28.51 ?  101 ASN   A HB2  1 
ATOM   2197 H HB3  A ASN   A 1 101 ? 18.636 3.316   -12.491 0.40 25.51 ?  101 ASN   A HB3  1 
ATOM   2198 H HB3  B ASN   A 1 101 ? 18.465 3.587   -12.157 0.60 28.51 ?  101 ASN   A HB3  1 
ATOM   2199 H HD21 A ASN   A 1 101 ? 16.536 2.173   -9.686  0.40 24.61 ?  101 ASN   A HD21 1 
ATOM   2200 H HD21 B ASN   A 1 101 ? 16.069 2.236   -9.684  0.60 27.36 ?  101 ASN   A HD21 1 
ATOM   2201 H HD22 A ASN   A 1 101 ? 17.901 2.766   -9.636  0.40 24.61 ?  101 ASN   A HD22 1 
ATOM   2202 H HD22 B ASN   A 1 101 ? 17.431 2.784   -9.439  0.60 27.36 ?  101 ASN   A HD22 1 
ATOM   2203 N N    A LYS   A 1 102 ? 21.761 1.114   -13.151 0.40 24.17 ?  102 LYS   A N    1 
ATOM   2204 N N    B LYS   A 1 102 ? 21.596 1.402   -12.897 0.60 29.02 ?  102 LYS   A N    1 
ATOM   2205 C CA   A LYS   A 1 102 ? 23.057 1.282   -13.792 0.40 25.29 ?  102 LYS   A CA   1 
ATOM   2206 C CA   B LYS   A 1 102 ? 22.892 1.567   -13.545 0.60 30.73 ?  102 LYS   A CA   1 
ATOM   2207 C C    A LYS   A 1 102 ? 23.366 0.148   -14.764 0.40 25.25 ?  102 LYS   A C    1 
ATOM   2208 C C    B LYS   A 1 102 ? 23.136 0.550   -14.650 0.60 30.46 ?  102 LYS   A C    1 
ATOM   2209 O O    A LYS   A 1 102 ? 24.497 0.051   -15.252 0.40 24.81 ?  102 LYS   A O    1 
ATOM   2210 O O    B LYS   A 1 102 ? 24.078 0.726   -15.430 0.60 30.68 ?  102 LYS   A O    1 
ATOM   2211 C CB   A LYS   A 1 102 ? 24.166 1.380   -12.739 0.40 26.14 ?  102 LYS   A CB   1 
ATOM   2212 C CB   B LYS   A 1 102 ? 24.028 1.418   -12.527 0.60 32.28 ?  102 LYS   A CB   1 
ATOM   2213 C CG   A LYS   A 1 102 ? 23.996 2.508   -11.731 0.40 26.74 ?  102 LYS   A CG   1 
ATOM   2214 C CG   B LYS   A 1 102 ? 24.394 2.673   -11.769 0.60 33.40 ?  102 LYS   A CG   1 
ATOM   2215 C CD   A LYS   A 1 102 ? 25.136 2.510   -10.718 0.40 27.32 ?  102 LYS   A CD   1 
ATOM   2216 C CD   B LYS   A 1 102 ? 25.436 2.350   -10.710 0.60 34.19 ?  102 LYS   A CD   1 
ATOM   2217 C CE   A LYS   A 1 102 ? 25.036 3.677   -9.746  0.40 27.74 ?  102 LYS   A CE   1 
ATOM   2218 C CE   B LYS   A 1 102 ? 25.426 3.361   -9.580  0.60 34.75 ?  102 LYS   A CE   1 
ATOM   2219 N NZ   A LYS   A 1 102 ? 26.170 3.689   -8.774  0.40 27.85 ?  102 LYS   A NZ   1 
ATOM   2220 N NZ   B LYS   A 1 102 ? 25.829 2.729   -8.292  0.60 34.98 ?  102 LYS   A NZ   1 
ATOM   2221 H H    A LYS   A 1 102 ? 21.758 0.502   -12.544 0.40 28.98 ?  102 LYS   A H    1 
ATOM   2222 H H    B LYS   A 1 102 ? 21.583 0.761   -12.321 0.60 34.80 ?  102 LYS   A H    1 
ATOM   2223 H HA   A LYS   A 1 102 ? 23.051 2.115   -14.287 0.40 30.32 ?  102 LYS   A HA   1 
ATOM   2224 H HA   B LYS   A 1 102 ? 22.944 2.453   -13.928 0.60 36.85 ?  102 LYS   A HA   1 
ATOM   2225 H HB2  A LYS   A 1 102 ? 24.198 0.548   -12.243 0.40 31.35 ?  102 LYS   A HB2  1 
ATOM   2226 H HB2  B LYS   A 1 102 ? 23.772 0.746   -11.880 0.60 38.71 ?  102 LYS   A HB2  1 
ATOM   2227 H HB3  A LYS   A 1 102 ? 25.012 1.521   -13.194 0.40 31.35 ?  102 LYS   A HB3  1 
ATOM   2228 H HB3  B LYS   A 1 102 ? 24.823 1.124   -12.995 0.60 38.71 ?  102 LYS   A HB3  1 
ATOM   2229 H HG2  A LYS   A 1 102 ? 23.999 3.360   -12.195 0.40 32.06 ?  102 LYS   A HG2  1 
ATOM   2230 H HG2  B LYS   A 1 102 ? 24.776 3.320   -12.383 0.60 40.05 ?  102 LYS   A HG2  1 
ATOM   2231 H HG3  A LYS   A 1 102 ? 23.161 2.389   -11.250 0.40 32.06 ?  102 LYS   A HG3  1 
ATOM   2232 H HG3  B LYS   A 1 102 ? 23.608 3.039   -11.340 0.60 40.05 ?  102 LYS   A HG3  1 
ATOM   2233 H HD2  A LYS   A 1 102 ? 25.109 1.687   -10.204 0.40 32.76 ?  102 LYS   A HD2  1 
ATOM   2234 H HD2  B LYS   A 1 102 ? 25.254 1.473   -10.337 0.60 41.01 ?  102 LYS   A HD2  1 
ATOM   2235 H HD3  A LYS   A 1 102 ? 25.981 2.582   -11.189 0.40 32.76 ?  102 LYS   A HD3  1 
ATOM   2236 H HD3  B LYS   A 1 102 ? 26.319 2.360   -11.118 0.60 41.01 ?  102 LYS   A HD3  1 
ATOM   2237 H HE2  A LYS   A 1 102 ? 25.056 4.510   -10.244 0.40 33.26 ?  102 LYS   A HE2  1 
ATOM   2238 H HE2  B LYS   A 1 102 ? 26.059 4.063   -9.782  0.60 41.68 ?  102 LYS   A HE2  1 
ATOM   2239 H HE3  A LYS   A 1 102 ? 24.208 3.606   -9.245  0.40 33.26 ?  102 LYS   A HE3  1 
ATOM   2240 H HE3  B LYS   A 1 102 ? 24.537 3.736   -9.479  0.60 41.68 ?  102 LYS   A HE3  1 
ATOM   2241 H HZ1  A LYS   A 1 102 ? 26.088 4.380   -8.219  0.40 33.40 ?  102 LYS   A HZ1  1 
ATOM   2242 H HZ1  B LYS   A 1 102 ? 25.815 3.333   -7.640  0.60 41.95 ?  102 LYS   A HZ1  1 
ATOM   2243 H HZ2  A LYS   A 1 102 ? 26.172 2.936   -8.300  0.40 33.40 ?  102 LYS   A HZ2  1 
ATOM   2244 H HZ2  B LYS   A 1 102 ? 25.268 2.068   -8.086  0.60 41.95 ?  102 LYS   A HZ2  1 
ATOM   2245 H HZ3  A LYS   A 1 102 ? 26.943 3.758   -9.210  0.40 33.40 ?  102 LYS   A HZ3  1 
ATOM   2246 H HZ3  B LYS   A 1 102 ? 26.652 2.397   -8.362  0.60 41.95 ?  102 LYS   A HZ3  1 
ATOM   2247 N N    A GLY   A 1 103 ? 22.395 -0.720  -15.043 0.40 25.62 ?  103 GLY   A N    1 
ATOM   2248 N N    B GLY   A 1 103 ? 22.338 -0.512  -14.720 0.60 30.06 ?  103 GLY   A N    1 
ATOM   2249 C CA   A GLY   A 1 103 ? 22.612 -1.818  -15.964 0.40 25.70 ?  103 GLY   A CA   1 
ATOM   2250 C CA   B GLY   A 1 103 ? 22.552 -1.560  -15.698 0.60 29.16 ?  103 GLY   A CA   1 
ATOM   2251 C C    A GLY   A 1 103 ? 23.421 -2.967  -15.407 0.40 25.85 ?  103 GLY   A C    1 
ATOM   2252 C C    B GLY   A 1 103 ? 23.421 -2.708  -15.235 0.60 28.44 ?  103 GLY   A C    1 
ATOM   2253 O O    A GLY   A 1 103 ? 23.916 -3.795  -16.177 0.40 26.56 ?  103 GLY   A O    1 
ATOM   2254 O O    B GLY   A 1 103 ? 24.022 -3.384  -16.077 0.60 29.32 ?  103 GLY   A O    1 
ATOM   2255 H H    A GLY   A 1 103 ? 21.604 -0.693  -14.704 0.40 30.72 ?  103 GLY   A H    1 
ATOM   2256 H H    B GLY   A 1 103 ? 21.661 -0.647  -14.205 0.60 36.05 ?  103 GLY   A H    1 
ATOM   2257 H HA2  A GLY   A 1 103 ? 21.754 -2.170  -16.241 0.40 30.82 ?  103 GLY   A HA2  1 
ATOM   2258 H HA2  B GLY   A 1 103 ? 21.691 -1.921  -15.961 0.60 34.97 ?  103 GLY   A HA2  1 
ATOM   2259 H HA3  A GLY   A 1 103 ? 23.066 -1.477  -16.753 0.40 30.82 ?  103 GLY   A HA3  1 
ATOM   2260 H HA3  B GLY   A 1 103 ? 22.968 -1.175  -16.484 0.60 34.97 ?  103 GLY   A HA3  1 
ATOM   2261 N N    A GLU   A 1 104 ? 23.557 -3.056  -14.088 0.40 24.67 ?  104 GLU   A N    1 
ATOM   2262 N N    B GLU   A 1 104 ? 23.508 -2.955  -13.931 0.60 26.05 ?  104 GLU   A N    1 
ATOM   2263 C CA   A GLU   A 1 104 ? 24.443 -4.039  -13.483 0.40 23.68 ?  104 GLU   A CA   1 
ATOM   2264 C CA   B GLU   A 1 104 ? 24.368 -4.003  -13.400 0.60 23.81 ?  104 GLU   A CA   1 
ATOM   2265 C C    A GLU   A 1 104 ? 23.771 -5.407  -13.380 0.40 23.23 ?  104 GLU   A C    1 
ATOM   2266 C C    B GLU   A 1 104 ? 23.616 -5.326  -13.281 0.60 23.88 ?  104 GLU   A C    1 
ATOM   2267 O O    A GLU   A 1 104 ? 22.547 -5.522  -13.264 0.40 23.04 ?  104 GLU   A O    1 
ATOM   2268 O O    B GLU   A 1 104 ? 22.407 -5.361  -13.039 0.60 24.16 ?  104 GLU   A O    1 
ATOM   2269 C CB   A GLU   A 1 104 ? 24.920 -3.538  -12.118 0.40 23.24 ?  104 GLU   A CB   1 
ATOM   2270 C CB   B GLU   A 1 104 ? 24.961 -3.569  -12.055 0.60 21.66 ?  104 GLU   A CB   1 
ATOM   2271 C CG   A GLU   A 1 104 ? 25.805 -2.296  -12.240 0.40 23.20 ?  104 GLU   A CG   1 
ATOM   2272 C CG   B GLU   A 1 104 ? 26.000 -2.462  -12.230 0.60 20.42 ?  104 GLU   A CG   1 
ATOM   2273 C CD   A GLU   A 1 104 ? 26.052 -1.588  -10.924 0.40 23.15 ?  104 GLU   A CD   1 
ATOM   2274 C CD   B GLU   A 1 104 ? 26.302 -1.667  -10.978 0.60 19.16 ?  104 GLU   A CD   1 
ATOM   2275 O OE1  A GLU   A 1 104 ? 25.529 -2.039  -9.885  0.40 22.77 ?  104 GLU   A OE1  1 
ATOM   2276 O OE1  B GLU   A 1 104 ? 25.663 -1.892  -9.929  0.60 17.72 ?  104 GLU   A OE1  1 
ATOM   2277 O OE2  A GLU   A 1 104 ? 26.768 -0.564  -10.937 0.40 23.54 -1 104 GLU   A OE2  1 
ATOM   2278 O OE2  B GLU   A 1 104 ? 27.190 -0.788  -11.067 0.60 19.61 -1 104 GLU   A OE2  1 
ATOM   2279 H H    A GLU   A 1 104 ? 23.147 -2.551  -13.526 0.40 29.58 ?  104 GLU   A H    1 
ATOM   2280 H H    B GLU   A 1 104 ? 23.077 -2.518  -13.327 0.60 31.23 ?  104 GLU   A H    1 
ATOM   2281 H HA   A GLU   A 1 104 ? 25.226 -4.134  -14.045 0.40 28.39 ?  104 GLU   A HA   1 
ATOM   2282 H HA   B GLU   A 1 104 ? 25.106 -4.140  -14.010 0.60 28.55 ?  104 GLU   A HA   1 
ATOM   2283 H HB2  A GLU   A 1 104 ? 24.152 -3.306  -11.573 0.40 27.86 ?  104 GLU   A HB2  1 
ATOM   2284 H HB2  B GLU   A 1 104 ? 24.255 -3.233  -11.484 0.60 25.96 ?  104 GLU   A HB2  1 
ATOM   2285 H HB3  A GLU   A 1 104 ? 25.439 -4.235  -11.686 0.40 27.86 ?  104 GLU   A HB3  1 
ATOM   2286 H HB3  B GLU   A 1 104 ? 25.399 -4.327  -11.637 0.60 25.96 ?  104 GLU   A HB3  1 
ATOM   2287 H HG2  A GLU   A 1 104 ? 26.664 -2.557  -12.611 0.40 27.81 ?  104 GLU   A HG2  1 
ATOM   2288 H HG2  B GLU   A 1 104 ? 26.831 -2.857  -12.533 0.60 24.48 ?  104 GLU   A HG2  1 
ATOM   2289 H HG3  A GLU   A 1 104 ? 25.375 -1.657  -12.828 0.40 27.81 ?  104 GLU   A HG3  1 
ATOM   2290 H HG3  B GLU   A 1 104 ? 25.676 -1.828  -12.883 0.60 24.48 ?  104 GLU   A HG3  1 
ATOM   2291 N N    A ASP   A 1 105 ? 24.597 -6.449  -13.425 0.40 23.43 ?  105 ASP   A N    1 
ATOM   2292 N N    B ASP   A 1 105 ? 24.354 -6.419  -13.462 0.60 23.49 ?  105 ASP   A N    1 
ATOM   2293 C CA   A ASP   A 1 105 ? 24.117 -7.820  -13.558 0.40 23.97 ?  105 ASP   A CA   1 
ATOM   2294 C CA   B ASP   A 1 105 ? 23.751 -7.742  -13.588 0.60 24.05 ?  105 ASP   A CA   1 
ATOM   2295 C C    A ASP   A 1 105 ? 23.409 -8.265  -12.282 0.40 22.35 ?  105 ASP   A C    1 
ATOM   2296 C C    B ASP   A 1 105 ? 23.204 -8.220  -12.248 0.60 21.93 ?  105 ASP   A C    1 
ATOM   2297 O O    A ASP   A 1 105 ? 24.015 -8.303  -11.207 0.40 21.22 ?  105 ASP   A O    1 
ATOM   2298 O O    B ASP   A 1 105 ? 23.941 -8.315  -11.261 0.60 19.66 ?  105 ASP   A O    1 
ATOM   2299 C CB   A ASP   A 1 105 ? 25.307 -8.731  -13.850 0.40 26.03 ?  105 ASP   A CB   1 
ATOM   2300 C CB   B ASP   A 1 105 ? 24.786 -8.723  -14.132 0.60 27.15 ?  105 ASP   A CB   1 
ATOM   2301 C CG   A ASP   A 1 105 ? 24.892 -10.138 -14.218 0.40 27.78 ?  105 ASP   A CG   1 
ATOM   2302 C CG   B ASP   A 1 105 ? 24.426 -10.167 -13.855 0.60 29.68 ?  105 ASP   A CG   1 
ATOM   2303 O OD1  A ASP   A 1 105 ? 23.678 -10.374 -14.384 0.40 28.34 ?  105 ASP   A OD1  1 
ATOM   2304 O OD1  B ASP   A 1 105 ? 23.257 -10.550 -14.077 0.60 30.23 ?  105 ASP   A OD1  1 
ATOM   2305 O OD2  A ASP   A 1 105 ? 25.783 -11.006 -14.348 0.40 28.49 -1 105 ASP   A OD2  1 
ATOM   2306 O OD2  B ASP   A 1 105 ? 25.322 -10.921 -13.426 0.60 31.14 -1 105 ASP   A OD2  1 
ATOM   2307 H H    A ASP   A 1 105 ? 25.453 -6.380  -13.385 0.40 28.09 ?  105 ASP   A H    1 
ATOM   2308 H H    B ASP   A 1 105 ? 25.212 -6.418  -13.519 0.60 28.16 ?  105 ASP   A H    1 
ATOM   2309 H HA   A ASP   A 1 105 ? 23.491 -7.873  -14.296 0.40 28.74 ?  105 ASP   A HA   1 
ATOM   2310 H HA   B ASP   A 1 105 ? 23.014 -7.697  -14.211 0.60 28.83 ?  105 ASP   A HA   1 
ATOM   2311 H HB2  A ASP   A 1 105 ? 25.804 -8.369  -14.598 0.40 31.21 ?  105 ASP   A HB2  1 
ATOM   2312 H HB2  B ASP   A 1 105 ? 24.844 -8.617  -15.093 0.60 32.55 ?  105 ASP   A HB2  1 
ATOM   2313 H HB3  A ASP   A 1 105 ? 25.870 -8.772  -13.062 0.40 31.21 ?  105 ASP   A HB3  1 
ATOM   2314 H HB3  B ASP   A 1 105 ? 25.648 -8.532  -13.724 0.60 32.55 ?  105 ASP   A HB3  1 
ATOM   2315 N N    A ILE   A 1 106 ? 22.126 -8.618  -12.404 0.40 21.89 ?  106 ILE   A N    1 
ATOM   2316 N N    B ILE   A 1 106 ? 21.909 -8.547  -12.225 0.60 21.80 ?  106 ILE   A N    1 
ATOM   2317 C CA   A ILE   A 1 106 ? 21.353 -9.036  -11.239 0.40 21.12 ?  106 ILE   A CA   1 
ATOM   2318 C CA   B ILE   A 1 106 ? 21.246 -8.933  -10.988 0.60 21.27 ?  106 ILE   A CA   1 
ATOM   2319 C C    A ILE   A 1 106 ? 21.895 -10.325 -10.640 0.40 20.62 ?  106 ILE   A C    1 
ATOM   2320 C C    B ILE   A 1 106 ? 21.793 -10.239 -10.433 0.60 20.09 ?  106 ILE   A C    1 
ATOM   2321 O O    A ILE   A 1 106 ? 21.680 -10.591 -9.454  0.40 19.95 ?  106 ILE   A O    1 
ATOM   2322 O O    B ILE   A 1 106 ? 21.631 -10.511 -9.240  0.60 19.54 ?  106 ILE   A O    1 
ATOM   2323 C CB   A ILE   A 1 106 ? 19.849 -9.146  -11.584 0.40 21.34 ?  106 ILE   A CB   1 
ATOM   2324 C CB   B ILE   A 1 106 ? 19.716 -8.978  -11.192 0.60 22.40 ?  106 ILE   A CB   1 
ATOM   2325 C CG1  A ILE   A 1 106 ? 19.005 -9.238  -10.310 0.40 21.25 ?  106 ILE   A CG1  1 
ATOM   2326 C CG1  B ILE   A 1 106 ? 18.982 -8.982  -9.845  0.60 22.86 ?  106 ILE   A CG1  1 
ATOM   2327 C CG2  A ILE   A 1 106 ? 19.583 -10.355 -12.459 0.40 21.54 ?  106 ILE   A CG2  1 
ATOM   2328 C CG2  B ILE   A 1 106 ? 19.319 -10.190 -12.024 0.60 23.15 ?  106 ILE   A CG2  1 
ATOM   2329 C CD1  A ILE   A 1 106 ? 19.077 -8.005  -9.435  0.40 21.17 ?  106 ILE   A CD1  1 
ATOM   2330 C CD1  B ILE   A 1 106 ? 19.244 -7.755  -8.997  0.60 23.01 ?  106 ILE   A CD1  1 
ATOM   2331 H H    A ILE   A 1 106 ? 21.687 -8.616  -13.141 0.40 26.24 ?  106 ILE   A H    1 
ATOM   2332 H H    B ILE   A 1 106 ? 21.401 -8.555  -12.912 0.60 26.13 ?  106 ILE   A H    1 
ATOM   2333 H HA   A ILE   A 1 106 ? 21.446 -8.353  -10.562 0.40 25.32 ?  106 ILE   A HA   1 
ATOM   2334 H HA   B ILE   A 1 106 ? 21.433 -8.259  -10.324 0.60 25.50 ?  106 ILE   A HA   1 
ATOM   2335 H HB   A ILE   A 1 106 ? 19.586 -8.348  -12.069 0.40 25.58 ?  106 ILE   A HB   1 
ATOM   2336 H HB   B ILE   A 1 106 ? 19.454 -8.182  -11.676 0.60 26.85 ?  106 ILE   A HB   1 
ATOM   2337 H HG12 A ILE   A 1 106 ? 18.077 -9.365  -10.558 0.40 25.48 ?  106 ILE   A HG12 1 
ATOM   2338 H HG12 B ILE   A 1 106 ? 18.027 -9.025  -10.009 0.60 27.40 ?  106 ILE   A HG12 1 
ATOM   2339 H HG13 A ILE   A 1 106 ? 19.310 -9.992  -9.782  0.40 25.48 ?  106 ILE   A HG13 1 
ATOM   2340 H HG13 B ILE   A 1 106 ? 19.262 -9.758  -9.335  0.60 27.40 ?  106 ILE   A HG13 1 
ATOM   2341 H HG21 A ILE   A 1 106 ? 18.692 -10.277 -12.835 0.40 25.82 ?  106 ILE   A HG21 1 
ATOM   2342 H HG21 B ILE   A 1 106 ? 18.403 -10.079 -12.322 0.60 27.75 ?  106 ILE   A HG21 1 
ATOM   2343 H HG22 A ILE   A 1 106 ? 20.243 -10.378 -13.166 0.40 25.82 ?  106 ILE   A HG22 1 
ATOM   2344 H HG22 B ILE   A 1 106 ? 19.911 -10.251 -12.790 0.60 27.75 ?  106 ILE   A HG22 1 
ATOM   2345 H HG23 A ILE   A 1 106 ? 19.645 -11.155 -11.916 0.40 25.82 ?  106 ILE   A HG23 1 
ATOM   2346 H HG23 B ILE   A 1 106 ? 19.396 -10.989 -11.481 0.60 27.75 ?  106 ILE   A HG23 1 
ATOM   2347 H HD11 A ILE   A 1 106 ? 18.351 -8.031  -8.794  0.40 25.38 ?  106 ILE   A HD11 1 
ATOM   2348 H HD11 B ILE   A 1 106 ? 18.556 -7.689  -8.319  0.60 27.59 ?  106 ILE   A HD11 1 
ATOM   2349 H HD12 A ILE   A 1 106 ? 19.929 -7.997  -8.968  0.40 25.38 ?  106 ILE   A HD12 1 
ATOM   2350 H HD12 B ILE   A 1 106 ? 20.115 -7.842  -8.577  0.60 27.59 ?  106 ILE   A HD12 1 
ATOM   2351 H HD13 A ILE   A 1 106 ? 18.998 -7.216  -9.994  0.40 25.38 ?  106 ILE   A HD13 1 
ATOM   2352 H HD13 B ILE   A 1 106 ? 19.226 -6.970  -9.566  0.60 27.59 ?  106 ILE   A HD13 1 
ATOM   2353 N N    A GLN   A 1 107 ? 22.601 -11.136 -11.434 0.40 21.11 ?  107 GLN   A N    1 
ATOM   2354 N N    B GLN   A 1 107 ? 22.446 -11.058 -11.265 0.60 21.20 ?  107 GLN   A N    1 
ATOM   2355 C CA   A GLN   A 1 107 ? 23.232 -12.338 -10.904 0.40 22.37 ?  107 GLN   A CA   1 
ATOM   2356 C CA   B GLN   A 1 107 ? 23.064 -12.278 -10.756 0.60 23.01 ?  107 GLN   A CA   1 
ATOM   2357 C C    A GLN   A 1 107 ? 24.207 -12.016 -9.780  0.40 20.33 ?  107 GLN   A C    1 
ATOM   2358 C C    B GLN   A 1 107 ? 24.100 -11.970 -9.680  0.60 20.72 ?  107 GLN   A C    1 
ATOM   2359 O O    A GLN   A 1 107 ? 24.497 -12.887 -8.952  0.40 21.53 ?  107 GLN   A O    1 
ATOM   2360 O O    B GLN   A 1 107 ? 24.328 -12.791 -8.783  0.60 21.53 ?  107 GLN   A O    1 
ATOM   2361 C CB   A GLN   A 1 107 ? 23.956 -13.084 -12.030 0.40 25.47 ?  107 GLN   A CB   1 
ATOM   2362 C CB   B GLN   A 1 107 ? 23.669 -13.086 -11.909 0.60 27.14 ?  107 GLN   A CB   1 
ATOM   2363 C CG   A GLN   A 1 107 ? 23.103 -13.310 -13.276 0.40 28.61 ?  107 GLN   A CG   1 
ATOM   2364 C CG   B GLN   A 1 107 ? 22.647 -13.539 -12.949 0.60 31.28 ?  107 GLN   A CG   1 
ATOM   2365 C CD   A GLN   A 1 107 ? 21.827 -14.074 -12.983 0.40 31.22 ?  107 GLN   A CD   1 
ATOM   2366 C CD   B GLN   A 1 107 ? 21.528 -14.372 -12.347 0.60 34.68 ?  107 GLN   A CD   1 
ATOM   2367 O OE1  A GLN   A 1 107 ? 21.858 -15.158 -12.401 0.40 32.38 ?  107 GLN   A OE1  1 
ATOM   2368 O OE1  B GLN   A 1 107 ? 21.758 -15.194 -11.459 0.60 35.93 ?  107 GLN   A OE1  1 
ATOM   2369 N NE2  A GLN   A 1 107 ? 20.693 -13.507 -13.381 0.40 31.92 ?  107 GLN   A NE2  1 
ATOM   2370 N NE2  B GLN   A 1 107 ? 20.307 -14.154 -12.823 0.60 36.05 ?  107 GLN   A NE2  1 
ATOM   2371 H H    A GLN   A 1 107 ? 22.725 -11.007 -12.273 0.40 25.31 ?  107 GLN   A H    1 
ATOM   2372 H H    B GLN   A 1 107 ? 22.536 -10.933 -12.110 0.60 25.41 ?  107 GLN   A H    1 
ATOM   2373 H HA   A GLN   A 1 107 ? 22.551 -12.928 -10.550 0.40 26.82 ?  107 GLN   A HA   1 
ATOM   2374 H HA   B GLN   A 1 107 ? 22.384 -12.830 -10.345 0.60 27.59 ?  107 GLN   A HA   1 
ATOM   2375 H HB2  A GLN   A 1 107 ? 24.736 -12.573 -12.297 0.40 30.54 ?  107 GLN   A HB2  1 
ATOM   2376 H HB2  B GLN   A 1 107 ? 24.330 -12.546 -12.367 0.60 32.54 ?  107 GLN   A HB2  1 
ATOM   2377 H HB3  A GLN   A 1 107 ? 24.232 -13.956 -11.704 0.40 30.54 ?  107 GLN   A HB3  1 
ATOM   2378 H HB3  B GLN   A 1 107 ? 24.089 -13.882 -11.553 0.60 32.54 ?  107 GLN   A HB3  1 
ATOM   2379 H HG2  A GLN   A 1 107 ? 22.857 -12.454 -13.659 0.40 34.31 ?  107 GLN   A HG2  1 
ATOM   2380 H HG2  B GLN   A 1 107 ? 22.250 -12.757 -13.366 0.60 37.51 ?  107 GLN   A HG2  1 
ATOM   2381 H HG3  A GLN   A 1 107 ? 23.617 -13.821 -13.920 0.40 34.31 ?  107 GLN   A HG3  1 
ATOM   2382 H HG3  B GLN   A 1 107 ? 23.094 -14.080 -13.621 0.60 37.51 ?  107 GLN   A HG3  1 
ATOM   2383 H HE21 A GLN   A 1 107 ? 20.709 -12.749 -13.785 0.40 38.28 ?  107 GLN   A HE21 1 
ATOM   2384 H HE21 B GLN   A 1 107 ? 20.185 -13.570 -13.442 0.60 43.24 ?  107 GLN   A HE21 1 
ATOM   2385 H HE22 A GLN   A 1 107 ? 19.943 -13.903 -13.237 0.40 38.28 ?  107 GLN   A HE22 1 
ATOM   2386 H HE22 B GLN   A 1 107 ? 19.639 -14.598 -12.512 0.60 43.24 ?  107 GLN   A HE22 1 
ATOM   2387 N N    . LEU   A 1 108 ? 24.706 -10.779 -9.723  1.00 17.24 ?  108 LEU   A N    1 
ATOM   2388 C CA   . LEU   A 1 108 ? 25.639 -10.380 -8.680  1.00 13.94 ?  108 LEU   A CA   1 
ATOM   2389 C C    . LEU   A 1 108 ? 24.963 -10.219 -7.328  1.00 12.27 ?  108 LEU   A C    1 
ATOM   2390 O O    . LEU   A 1 108 ? 25.660 -10.079 -6.320  1.00 12.63 ?  108 LEU   A O    1 
ATOM   2391 C CB   . LEU   A 1 108 ? 26.360 -9.088  -9.080  1.00 13.53 ?  108 LEU   A CB   1 
ATOM   2392 C CG   . LEU   A 1 108 ? 27.376 -9.289  -10.207 1.00 15.46 ?  108 LEU   A CG   1 
ATOM   2393 C CD1  . LEU   A 1 108 ? 27.842 -7.959  -10.773 1.00 16.06 ?  108 LEU   A CD1  1 
ATOM   2394 C CD2  . LEU   A 1 108 ? 28.576 -10.098 -9.725  1.00 17.42 ?  108 LEU   A CD2  1 
ATOM   2395 H H    A LEU   A 1 108 ? 24.519 -10.161 -10.284 0.40 20.67 ?  108 LEU   A H    1 
ATOM   2396 H H    B LEU   A 1 108 ? 24.584 -10.193 -10.335 0.60 20.67 ?  108 LEU   A H    1 
ATOM   2397 H HA   . LEU   A 1 108 ? 26.309 -11.073 -8.582  1.00 16.71 ?  108 LEU   A HA   1 
ATOM   2398 H HB2  . LEU   A 1 108 ? 25.703 -8.443  -9.387  1.00 16.21 ?  108 LEU   A HB2  1 
ATOM   2399 H HB3  . LEU   A 1 108 ? 26.833 -8.740  -8.311  1.00 16.21 ?  108 LEU   A HB3  1 
ATOM   2400 H HG   . LEU   A 1 108 ? 26.958 -9.787  -10.927 1.00 18.53 ?  108 LEU   A HG   1 
ATOM   2401 H HD11 . LEU   A 1 108 ? 28.458 -8.124  -11.508 1.00 19.25 ?  108 LEU   A HD11 1 
ATOM   2402 H HD12 . LEU   A 1 108 ? 27.072 -7.465  -11.094 1.00 19.25 ?  108 LEU   A HD12 1 
ATOM   2403 H HD13 . LEU   A 1 108 ? 28.291 -7.456  -10.076 1.00 19.25 ?  108 LEU   A HD13 1 
ATOM   2404 H HD21 . LEU   A 1 108 ? 29.275 -10.057 -10.394 1.00 20.88 ?  108 LEU   A HD21 1 
ATOM   2405 H HD22 . LEU   A 1 108 ? 28.894 -9.720  -8.890  1.00 20.88 ?  108 LEU   A HD22 1 
ATOM   2406 H HD23 . LEU   A 1 108 ? 28.302 -11.018 -9.587  1.00 20.88 ?  108 LEU   A HD23 1 
ATOM   2407 N N    . LEU   A 1 109 ? 23.631 -10.268 -7.274  1.00 12.18 ?  109 LEU   A N    1 
ATOM   2408 C CA   . LEU   A 1 109 ? 22.951 -10.153 -5.991  1.00 11.54 ?  109 LEU   A CA   1 
ATOM   2409 C C    . LEU   A 1 109 ? 23.306 -11.316 -5.069  1.00 10.44 ?  109 LEU   A C    1 
ATOM   2410 O O    . LEU   A 1 109 ? 23.440 -11.134 -3.853  1.00 10.97 ?  109 LEU   A O    1 
ATOM   2411 C CB   . LEU   A 1 109 ? 21.441 -10.058 -6.216  1.00 12.32 ?  109 LEU   A CB   1 
ATOM   2412 C CG   . LEU   A 1 109 ? 20.574 -9.773  -4.994  1.00 12.63 ?  109 LEU   A CG   1 
ATOM   2413 C CD1  . LEU   A 1 109 ? 21.036 -8.514  -4.296  1.00 13.03 ?  109 LEU   A CD1  1 
ATOM   2414 C CD2  . LEU   A 1 109 ? 19.116 -9.644  -5.406  1.00 13.58 ?  109 LEU   A CD2  1 
ATOM   2415 H H    . LEU   A 1 109 ? 23.108 -10.368 -7.952  1.00 14.59 ?  109 LEU   A H    1 
ATOM   2416 H HA   . LEU   A 1 109 ? 23.242 -9.335  -5.562  1.00 13.82 ?  109 LEU   A HA   1 
ATOM   2417 H HB2  . LEU   A 1 109 ? 21.275 -9.341  -6.850  1.00 14.76 ?  109 LEU   A HB2  1 
ATOM   2418 H HB3  . LEU   A 1 109 ? 21.135 -10.894 -6.591  1.00 14.76 ?  109 LEU   A HB3  1 
ATOM   2419 H HG   . LEU   A 1 109 ? 20.645 -10.509 -4.369  1.00 15.13 ?  109 LEU   A HG   1 
ATOM   2420 H HD11 . LEU   A 1 109 ? 20.352 -8.221  -3.680  1.00 15.61 ?  109 LEU   A HD11 1 
ATOM   2421 H HD12 . LEU   A 1 109 ? 21.861 -8.698  -3.823  1.00 15.61 ?  109 LEU   A HD12 1 
ATOM   2422 H HD13 . LEU   A 1 109 ? 21.190 -7.822  -4.967  1.00 15.61 ?  109 LEU   A HD13 1 
ATOM   2423 H HD21 . LEU   A 1 109 ? 18.591 -9.367  -4.635  1.00 16.27 ?  109 LEU   A HD21 1 
ATOM   2424 H HD22 . LEU   A 1 109 ? 19.039 -8.981  -6.109  1.00 16.27 ?  109 LEU   A HD22 1 
ATOM   2425 H HD23 . LEU   A 1 109 ? 18.797 -10.504 -5.727  1.00 16.27 ?  109 LEU   A HD23 1 
ATOM   2426 N N    . LYS   A 1 110 ? 23.454 -12.524 -5.623  1.00 10.37 ?  110 LYS   A N    1 
ATOM   2427 C CA   . LYS   A 1 110 ? 23.840 -13.659 -4.787  1.00 10.16 ?  110 LYS   A CA   1 
ATOM   2428 C C    . LYS   A 1 110 ? 25.223 -13.437 -4.180  1.00 9.58  ?  110 LYS   A C    1 
ATOM   2429 O O    . LYS   A 1 110 ? 25.426 -13.637 -2.980  1.00 10.17 ?  110 LYS   A O    1 
ATOM   2430 C CB   . LYS   A 1 110 ? 23.773 -14.967 -5.578  1.00 10.88 ?  110 LYS   A CB   1 
ATOM   2431 C CG   . LYS   A 1 110 ? 23.975 -16.187 -4.682  1.00 11.30 ?  110 LYS   A CG   1 
ATOM   2432 C CD   . LYS   A 1 110 ? 23.735 -17.504 -5.397  1.00 11.77 ?  110 LYS   A CD   1 
ATOM   2433 C CE   . LYS   A 1 110 ? 23.826 -18.698 -4.450  1.00 12.92 ?  110 LYS   A CE   1 
ATOM   2434 N NZ   . LYS   A 1 110 ? 22.663 -18.823 -3.533  1.00 13.30 ?  110 LYS   A NZ   1 
ATOM   2435 H H    . LYS   A 1 110 ? 23.333 -12.711 -6.453  1.00 12.41 ?  110 LYS   A H    1 
ATOM   2436 H HA   . LYS   A 1 110 ? 23.203 -13.731 -4.054  1.00 12.17 ?  110 LYS   A HA   1 
ATOM   2437 H HB2  . LYS   A 1 110 ? 22.904 -15.040 -5.998  1.00 13.04 ?  110 LYS   A HB2  1 
ATOM   2438 H HB3  . LYS   A 1 110 ? 24.473 -14.962 -6.249  1.00 13.04 ?  110 LYS   A HB3  1 
ATOM   2439 H HG2  . LYS   A 1 110 ? 24.890 -16.188 -4.356  1.00 13.53 ?  110 LYS   A HG2  1 
ATOM   2440 H HG3  . LYS   A 1 110 ? 23.360 -16.133 -3.936  1.00 13.53 ?  110 LYS   A HG3  1 
ATOM   2441 H HD2  . LYS   A 1 110 ? 22.847 -17.495 -5.787  1.00 14.10 ?  110 LYS   A HD2  1 
ATOM   2442 H HD3  . LYS   A 1 110 ? 24.404 -17.617 -6.089  1.00 14.10 ?  110 LYS   A HD3  1 
ATOM   2443 H HE2  . LYS   A 1 110 ? 23.880 -19.511 -4.972  1.00 15.47 ?  110 LYS   A HE2  1 
ATOM   2444 H HE3  . LYS   A 1 110 ? 24.623 -18.603 -3.902  1.00 15.47 ?  110 LYS   A HE3  1 
ATOM   2445 H HZ1  . LYS   A 1 110 ? 22.763 -19.530 -3.003  1.00 15.94 ?  110 LYS   A HZ1  1 
ATOM   2446 H HZ2  . LYS   A 1 110 ? 22.590 -18.092 -3.028  1.00 15.94 ?  110 LYS   A HZ2  1 
ATOM   2447 H HZ3  . LYS   A 1 110 ? 21.912 -18.920 -4.004  1.00 15.94 ?  110 LYS   A HZ3  1 
ATOM   2448 N N    . SER   A 1 111 ? 26.180 -12.990 -4.998  1.00 10.05 ?  111 SER   A N    1 
ATOM   2449 C CA   . SER   A 1 111 ? 27.510 -12.677 -4.482  1.00 10.50 ?  111 SER   A CA   1 
ATOM   2450 C C    . SER   A 1 111 ? 27.441 -11.641 -3.369  1.00 9.98  ?  111 SER   A C    1 
ATOM   2451 O O    . SER   A 1 111 ? 28.144 -11.748 -2.359  1.00 10.59 ?  111 SER   A O    1 
ATOM   2452 C CB   . SER   A 1 111 ? 28.402 -12.178 -5.616  1.00 11.75 ?  111 SER   A CB   1 
ATOM   2453 O OG   . SER   A 1 111 ? 28.505 -13.163 -6.635  1.00 13.97 ?  111 SER   A OG   1 
ATOM   2454 H H    . SER   A 1 111 ? 26.076 -12.855 -5.840  1.00 12.03 ?  111 SER   A H    1 
ATOM   2455 H HA   . SER   A 1 111 ? 27.902 -13.483 -4.119  1.00 12.58 ?  111 SER   A HA   1 
ATOM   2456 H HB2  . SER   A 1 111 ? 28.014 -11.380 -6.002  1.00 14.07 ?  111 SER   A HB2  1 
ATOM   2457 H HB3  . SER   A 1 111 ? 29.284 -11.980 -5.258  1.00 14.07 ?  111 SER   A HB3  1 
ATOM   2458 H HG   . SER   A 1 111 ? 29.025 -12.888 -7.246  1.00 16.73 ?  111 SER   A HG   1 
ATOM   2459 N N    . ALA   A 1 112 ? 26.592 -10.627 -3.537  1.00 9.94  ?  112 ALA   A N    1 
ATOM   2460 C CA   . ALA   A 1 112 ? 26.449 -9.590  -2.515  1.00 9.79  ?  112 ALA   A CA   1 
ATOM   2461 C C    . ALA   A 1 112 ? 25.978 -10.194 -1.195  1.00 9.60  ?  112 ALA   A C    1 
ATOM   2462 O O    . ALA   A 1 112 ? 26.537 -9.913  -0.128  1.00 9.92  ?  112 ALA   A O    1 
ATOM   2463 C CB   . ALA   A 1 112 ? 25.481 -8.503  -2.998  1.00 10.25 ?  112 ALA   A CB   1 
ATOM   2464 H H    . ALA   A 1 112 ? 26.089 -10.508 -4.227  1.00 11.90 ?  112 ALA   A H    1 
ATOM   2465 H HA   . ALA   A 1 112 ? 27.311 -9.169  -2.362  1.00 11.72 ?  112 ALA   A HA   1 
ATOM   2466 H HB1  . ALA   A 1 112 ? 25.419 -7.806  -2.318  1.00 12.27 ?  112 ALA   A HB1  1 
ATOM   2467 H HB2  . ALA   A 1 112 ? 25.815 -8.120  -3.824  1.00 12.27 ?  112 ALA   A HB2  1 
ATOM   2468 H HB3  . ALA   A 1 112 ? 24.607 -8.894  -3.144  1.00 12.27 ?  112 ALA   A HB3  1 
ATOM   2469 N N    . TYR   A 1 113 ? 24.947 -11.044 -1.247  1.00 9.76  ?  113 TYR   A N    1 
ATOM   2470 C CA   . TYR   A 1 113 ? 24.443 -11.654 -0.019  1.00 9.55  ?  113 TYR   A CA   1 
ATOM   2471 C C    . TYR   A 1 113 ? 25.451 -12.614 0.614   1.00 9.17  ?  113 TYR   A C    1 
ATOM   2472 O O    . TYR   A 1 113 ? 25.422 -12.809 1.833   1.00 9.72  ?  113 TYR   A O    1 
ATOM   2473 C CB   . TYR   A 1 113 ? 23.123 -12.379 -0.285  1.00 10.02 ?  113 TYR   A CB   1 
ATOM   2474 C CG   . TYR   A 1 113 ? 21.906 -11.487 -0.185  1.00 10.10 ?  113 TYR   A CG   1 
ATOM   2475 C CD1  . TYR   A 1 113 ? 21.556 -10.895 1.023   1.00 10.09 ?  113 TYR   A CD1  1 
ATOM   2476 C CD2  . TYR   A 1 113 ? 21.092 -11.251 -1.288  1.00 10.57 ?  113 TYR   A CD2  1 
ATOM   2477 C CE1  . TYR   A 1 113 ? 20.432 -10.100 1.133   1.00 10.72 ?  113 TYR   A CE1  1 
ATOM   2478 C CE2  . TYR   A 1 113 ? 19.939 -10.453 -1.185  1.00 10.58 ?  113 TYR   A CE2  1 
ATOM   2479 C CZ   . TYR   A 1 113 ? 19.624 -9.883  0.028   1.00 10.39 ?  113 TYR   A CZ   1 
ATOM   2480 O OH   . TYR   A 1 113 ? 18.504 -9.089  0.166   1.00 11.53 ?  113 TYR   A OH   1 
ATOM   2481 H H    . TYR   A 1 113 ? 24.534 -11.281 -1.965  1.00 11.69 ?  113 TYR   A H    1 
ATOM   2482 H HA   . TYR   A 1 113 ? 24.269 -10.948 0.624   1.00 11.43 ?  113 TYR   A HA   1 
ATOM   2483 H HB2  . TYR   A 1 113 ? 23.148 -12.744 -1.181  1.00 12.00 ?  113 TYR   A HB2  1 
ATOM   2484 H HB3  . TYR   A 1 113 ? 23.029 -13.092 0.363   1.00 12.00 ?  113 TYR   A HB3  1 
ATOM   2485 H HD1  . TYR   A 1 113 ? 22.095 -11.044 1.775   1.00 12.09 ?  113 TYR   A HD1  1 
ATOM   2486 H HD2  . TYR   A 1 113 ? 21.302 -11.652 -2.097  1.00 12.65 ?  113 TYR   A HD2  1 
ATOM   2487 H HE1  . TYR   A 1 113 ? 20.219 -9.714  1.953   1.00 12.84 ?  113 TYR   A HE1  1 
ATOM   2488 H HE2  . TYR   A 1 113 ? 19.399 -10.306 -1.926  1.00 12.67 ?  113 TYR   A HE2  1 
ATOM   2489 H HH   . TYR   A 1 113 ? 18.103 -9.038  -0.578  1.00 13.81 ?  113 TYR   A HH   1 
ATOM   2490 N N    . GLU   A 1 114 ? 26.347 -13.219 -0.179  1.00 9.62  ?  114 GLU   A N    1 
ATOM   2491 C CA   . GLU   A 1 114 ? 27.340 -14.120 0.407   1.00 9.90  ?  114 GLU   A CA   1 
ATOM   2492 C C    . GLU   A 1 114 ? 28.197 -13.416 1.455   1.00 9.76  ?  114 GLU   A C    1 
ATOM   2493 O O    . GLU   A 1 114 ? 28.684 -14.058 2.396   1.00 10.20 ?  114 GLU   A O    1 
ATOM   2494 C CB   . GLU   A 1 114 ? 28.206 -14.747 -0.692  1.00 9.89  ?  114 GLU   A CB   1 
ATOM   2495 C CG   . GLU   A 1 114 ? 27.444 -15.803 -1.468  1.00 10.33 ?  114 GLU   A CG   1 
ATOM   2496 C CD   . GLU   A 1 114 ? 28.143 -16.331 -2.721  1.00 10.88 ?  114 GLU   A CD   1 
ATOM   2497 O OE1  . GLU   A 1 114 ? 29.096 -15.697 -3.222  1.00 11.07 ?  114 GLU   A OE1  1 
ATOM   2498 O OE2  . GLU   A 1 114 ? 27.696 -17.396 -3.217  1.00 11.82 -1 114 GLU   A OE2  1 
ATOM   2499 H H    . GLU   A 1 114 ? 26.393 -13.121 -1.038  1.00 11.52 ?  114 GLU   A H    1 
ATOM   2500 H HA   . GLU   A 1 114 ? 26.867 -14.842 0.844   1.00 11.85 ?  114 GLU   A HA   1 
ATOM   2501 H HB2  . GLU   A 1 114 ? 28.483 -14.060 -1.320  1.00 11.84 ?  114 GLU   A HB2  1 
ATOM   2502 H HB3  . GLU   A 1 114 ? 28.979 -15.168 -0.291  1.00 11.84 ?  114 GLU   A HB3  1 
ATOM   2503 H HG2  . GLU   A 1 114 ? 27.294 -16.567 -0.887  1.00 12.38 ?  114 GLU   A HG2  1 
ATOM   2504 H HG3  . GLU   A 1 114 ? 26.594 -15.436 -1.748  1.00 12.38 ?  114 GLU   A HG3  1 
ATOM   2505 N N    . ASN   A 1 115 ? 28.378 -12.095 1.330   1.00 9.40  ?  115 ASN   A N    1 
ATOM   2506 C CA   . ASN   A 1 115 ? 29.146 -11.369 2.337   1.00 9.85  ?  115 ASN   A CA   1 
ATOM   2507 C C    . ASN   A 1 115 ? 28.538 -11.513 3.729   1.00 9.47  ?  115 ASN   A C    1 
ATOM   2508 O O    . ASN   A 1 115 ? 29.257 -11.450 4.732   1.00 10.17 ?  115 ASN   A O    1 
ATOM   2509 C CB   . ASN   A 1 115 ? 29.243 -9.888  1.964   1.00 10.01 ?  115 ASN   A CB   1 
ATOM   2510 C CG   . ASN   A 1 115 ? 30.041 -9.660  0.704   1.00 11.04 ?  115 ASN   A CG   1 
ATOM   2511 O OD1  . ASN   A 1 115 ? 31.262 -9.752  0.718   1.00 14.36 ?  115 ASN   A OD1  1 
ATOM   2512 N ND2  . ASN   A 1 115 ? 29.363 -9.356  -0.387  1.00 10.69 ?  115 ASN   A ND2  1 
ATOM   2513 H H    . ASN   A 1 115 ? 28.065 -11.609 0.690   1.00 11.26 ?  115 ASN   A H    1 
ATOM   2514 H HA   . ASN   A 1 115 ? 30.040 -11.735 2.368   1.00 11.79 ?  115 ASN   A HA   1 
ATOM   2515 H HB2  . ASN   A 1 115 ? 28.348 -9.538  1.832   1.00 11.98 ?  115 ASN   A HB2  1 
ATOM   2516 H HB3  . ASN   A 1 115 ? 29.679 -9.413  2.692   1.00 11.98 ?  115 ASN   A HB3  1 
ATOM   2517 H HD21 . ASN   A 1 115 ? 29.780 -9.214  -1.123  1.00 12.80 ?  115 ASN   A HD21 1 
ATOM   2518 H HD22 . ASN   A 1 115 ? 28.504 -9.304  -0.360  1.00 12.80 ?  115 ASN   A HD22 1 
ATOM   2519 N N    . PHE   A 1 116 ? 27.214 -11.688 3.814   1.00 9.79  ?  116 PHE   A N    1 
ATOM   2520 C CA   . PHE   A 1 116 ? 26.570 -11.799 5.119   1.00 9.70  ?  116 PHE   A CA   1 
ATOM   2521 C C    . PHE   A 1 116 ? 27.054 -13.036 5.878   1.00 9.71  ?  116 PHE   A C    1 
ATOM   2522 O O    . PHE   A 1 116 ? 26.989 -13.060 7.105   1.00 10.35 ?  116 PHE   A O    1 
ATOM   2523 C CB   . PHE   A 1 116 ? 25.039 -11.927 4.985   1.00 9.87  ?  116 PHE   A CB   1 
ATOM   2524 C CG   . PHE   A 1 116 ? 24.277 -10.677 4.539   1.00 9.57  ?  116 PHE   A CG   1 
ATOM   2525 C CD1  . PHE   A 1 116 ? 24.839 -9.651  3.794   1.00 9.77  ?  116 PHE   A CD1  1 
ATOM   2526 C CD2  . PHE   A 1 116 ? 22.920 -10.577 4.870   1.00 10.45 ?  116 PHE   A CD2  1 
ATOM   2527 C CE1  . PHE   A 1 116 ? 24.070 -8.569  3.394   1.00 10.21 ?  116 PHE   A CE1  1 
ATOM   2528 C CE2  . PHE   A 1 116 ? 22.151 -9.502  4.478   1.00 10.47 ?  116 PHE   A CE2  1 
ATOM   2529 C CZ   . PHE   A 1 116 ? 22.719 -8.494  3.739   1.00 10.09 ?  116 PHE   A CZ   1 
ATOM   2530 H H    . PHE   A 1 116 ? 26.671 -11.744 3.139   1.00 11.73 ?  116 PHE   A H    1 
ATOM   2531 H HA   . PHE   A 1 116 ? 26.762 -11.010 5.643   1.00 11.62 ?  116 PHE   A HA   1 
ATOM   2532 H HB2  . PHE   A 1 116 ? 24.847 -12.631 4.339   1.00 11.82 ?  116 PHE   A HB2  1 
ATOM   2533 H HB3  . PHE   A 1 116 ? 24.681 -12.193 5.849   1.00 11.82 ?  116 PHE   A HB3  1 
ATOM   2534 H HD1  . PHE   A 1 116 ? 25.729 -9.707  3.548   1.00 11.69 ?  116 PHE   A HD1  1 
ATOM   2535 H HD2  . PHE   A 1 116 ? 22.521 -11.269 5.361   1.00 12.51 ?  116 PHE   A HD2  1 
ATOM   2536 H HE1  . PHE   A 1 116 ? 24.456 -7.889  2.896   1.00 12.23 ?  116 PHE   A HE1  1 
ATOM   2537 H HE2  . PHE   A 1 116 ? 21.250 -9.467  4.717   1.00 12.54 ?  116 PHE   A HE2  1 
ATOM   2538 H HZ   . PHE   A 1 116 ? 22.209 -7.761  3.479   1.00 12.08 ?  116 PHE   A HZ   1 
ATOM   2539 N N    . ASN   A 1 117 ? 27.488 -14.083 5.163   1.00 9.87  ?  117 ASN   A N    1 
ATOM   2540 C CA   . ASN   A 1 117 ? 27.869 -15.331 5.816   1.00 10.14 ?  117 ASN   A CA   1 
ATOM   2541 C C    . ASN   A 1 117 ? 29.145 -15.211 6.631   1.00 10.79 ?  117 ASN   A C    1 
ATOM   2542 O O    . ASN   A 1 117 ? 29.454 -16.135 7.392   1.00 11.76 ?  117 ASN   A O    1 
ATOM   2543 C CB   . ASN   A 1 117 ? 27.976 -16.443 4.782   1.00 10.47 ?  117 ASN   A CB   1 
ATOM   2544 C CG   . ASN   A 1 117 ? 26.613 -16.828 4.257   1.00 10.30 ?  117 ASN   A CG   1 
ATOM   2545 O OD1  . ASN   A 1 117 ? 25.644 -16.867 5.022   1.00 11.22 ?  117 ASN   A OD1  1 
ATOM   2546 N ND2  . ASN   A 1 117 ? 26.514 -17.079 2.969   1.00 10.18 ?  117 ASN   A ND2  1 
ATOM   2547 H H    . ASN   A 1 117 ? 27.560 -14.088 4.306   1.00 11.82 ?  117 ASN   A H    1 
ATOM   2548 H HA   . ASN   A 1 117 ? 27.161 -15.570 6.429   1.00 12.14 ?  117 ASN   A HA   1 
ATOM   2549 H HB2  . ASN   A 1 117 ? 28.522 -16.137 4.036   1.00 12.53 ?  117 ASN   A HB2  1 
ATOM   2550 H HB3  . ASN   A 1 117 ? 28.384 -17.221 5.195   1.00 12.53 ?  117 ASN   A HB3  1 
ATOM   2551 H HD21 . ASN   A 1 117 ? 25.754 -17.295 2.633   1.00 12.19 ?  117 ASN   A HD21 1 
ATOM   2552 H HD22 . ASN   A 1 117 ? 27.209 -17.024 2.463   1.00 12.19 ?  117 ASN   A HD22 1 
ATOM   2553 N N    . GLN   A 1 118 ? 29.871 -14.095 6.514   1.00 10.61 ?  118 GLN   A N    1 
ATOM   2554 C CA   . GLN   A 1 118 ? 31.056 -13.859 7.331   1.00 11.25 ?  118 GLN   A CA   1 
ATOM   2555 C C    . GLN   A 1 118 ? 30.721 -13.285 8.702   1.00 11.37 ?  118 GLN   A C    1 
ATOM   2556 O O    . GLN   A 1 118 ? 31.639 -12.990 9.475   1.00 13.21 ?  118 GLN   A O    1 
ATOM   2557 C CB   . GLN   A 1 118 ? 32.037 -12.941 6.591   1.00 11.37 ?  118 GLN   A CB   1 
ATOM   2558 C CG   . GLN   A 1 118 ? 32.501 -13.516 5.264   1.00 11.41 ?  118 GLN   A CG   1 
ATOM   2559 C CD   . GLN   A 1 118 ? 33.326 -14.782 5.434   1.00 11.72 ?  118 GLN   A CD   1 
ATOM   2560 O OE1  . GLN   A 1 118 ? 34.192 -14.859 6.318   1.00 12.51 ?  118 GLN   A OE1  1 
ATOM   2561 N NE2  . GLN   A 1 118 ? 33.076 -15.775 4.585   1.00 11.68 ?  118 GLN   A NE2  1 
ATOM   2562 H H    . GLN   A 1 118 ? 29.685 -13.442 5.975   1.00 12.71 ?  118 GLN   A H    1 
ATOM   2563 H HA   . GLN   A 1 118 ? 31.492 -14.709 7.472   1.00 13.48 ?  118 GLN   A HA   1 
ATOM   2564 H HB2  . GLN   A 1 118 ? 31.607 -12.091 6.421   1.00 13.62 ?  118 GLN   A HB2  1 
ATOM   2565 H HB3  . GLN   A 1 118 ? 32.820 -12.811 7.153   1.00 13.62 ?  118 GLN   A HB3  1 
ATOM   2566 H HG2  . GLN   A 1 118 ? 31.724 -13.731 4.722   1.00 13.67 ?  118 GLN   A HG2  1 
ATOM   2567 H HG3  . GLN   A 1 118 ? 33.051 -12.861 4.811   1.00 13.67 ?  118 GLN   A HG3  1 
ATOM   2568 H HE21 . GLN   A 1 118 ? 32.463 -15.685 3.981   1.00 13.99 ?  118 GLN   A HE21 1 
ATOM   2569 H HE22 . GLN   A 1 118 ? 33.511 -16.515 4.639   1.00 13.99 ?  118 GLN   A HE22 1 
ATOM   2570 N N    . HIS   A 1 119 ? 29.434 -13.146 9.027   1.00 10.95 ?  119 HIS   A N    1 
ATOM   2571 C CA   . HIS   A 1 119 ? 28.979 -12.551 10.279  1.00 11.65 ?  119 HIS   A CA   1 
ATOM   2572 C C    . HIS   A 1 119 ? 27.851 -13.391 10.852  1.00 12.18 ?  119 HIS   A C    1 
ATOM   2573 O O    . HIS   A 1 119 ? 26.899 -13.720 10.140  1.00 12.43 ?  119 HIS   A O    1 
ATOM   2574 C CB   . HIS   A 1 119 ? 28.509 -11.120 10.016  1.00 12.15 ?  119 HIS   A CB   1 
ATOM   2575 C CG   . HIS   A 1 119 ? 29.580 -10.300 9.398   1.00 13.24 ?  119 HIS   A CG   1 
ATOM   2576 N ND1  . HIS   A 1 119 ? 30.567 -9.703  10.145  1.00 15.68 ?  119 HIS   A ND1  1 
ATOM   2577 C CD2  . HIS   A 1 119 ? 29.898 -10.087 8.101   1.00 14.48 ?  119 HIS   A CD2  1 
ATOM   2578 C CE1  . HIS   A 1 119 ? 31.421 -9.108  9.333   1.00 16.17 ?  119 HIS   A CE1  1 
ATOM   2579 N NE2  . HIS   A 1 119 ? 31.043 -9.331  8.088   1.00 16.07 ?  119 HIS   A NE2  1 
ATOM   2580 H H    . HIS   A 1 119 ? 28.782 -13.401 8.523   1.00 13.11 ?  119 HIS   A H    1 
ATOM   2581 H HA   . HIS   A 1 119 ? 29.710 -12.532 10.918  1.00 13.96 ?  119 HIS   A HA   1 
ATOM   2582 H HB2  . HIS   A 1 119 ? 27.747 -11.148 9.412   1.00 14.56 ?  119 HIS   A HB2  1 
ATOM   2583 H HB3  . HIS   A 1 119 ? 28.252 -10.714 10.857  1.00 14.56 ?  119 HIS   A HB3  1 
ATOM   2584 H HD2  . HIS   A 1 119 ? 29.418 -10.385 7.357   1.00 17.35 ?  119 HIS   A HD2  1 
ATOM   2585 H HE1  . HIS   A 1 119 ? 32.158 -8.611  9.594   1.00 19.37 ?  119 HIS   A HE1  1 
ATOM   2586 H HE2  . HIS   A 1 119 ? 31.432 -9.029  7.383   1.00 19.25 ?  119 HIS   A HE2  1 
ATOM   2587 N N    A GLU   A 1 120 ? 27.955 -13.725 12.142  0.40 13.58 ?  120 GLU   A N    1 
ATOM   2588 N N    B GLU   A 1 120 ? 27.946 -13.718 12.143  0.60 12.47 ?  120 GLU   A N    1 
ATOM   2589 C CA   A GLU   A 1 120 ? 27.011 -14.665 12.743  0.40 15.42 ?  120 GLU   A CA   1 
ATOM   2590 C CA   B GLU   A 1 120 ? 27.006 -14.672 12.725  0.60 13.64 ?  120 GLU   A CA   1 
ATOM   2591 C C    A GLU   A 1 120 ? 25.594 -14.099 12.789  0.40 13.60 ?  120 GLU   A C    1 
ATOM   2592 C C    B GLU   A 1 120 ? 25.592 -14.112 12.843  0.60 12.29 ?  120 GLU   A C    1 
ATOM   2593 O O    A GLU   A 1 120 ? 24.619 -14.835 12.582  0.40 13.79 ?  120 GLU   A O    1 
ATOM   2594 O O    B GLU   A 1 120 ? 24.618 -14.879 12.768  0.60 12.25 ?  120 GLU   A O    1 
ATOM   2595 C CB   A GLU   A 1 120 ? 27.484 -15.059 14.144  0.40 19.78 ?  120 GLU   A CB   1 
ATOM   2596 C CB   B GLU   A 1 120 ? 27.499 -15.137 14.097  0.60 17.70 ?  120 GLU   A CB   1 
ATOM   2597 C CG   A GLU   A 1 120 ? 28.657 -16.024 14.160  0.40 24.80 ?  120 GLU   A CG   1 
ATOM   2598 C CG   B GLU   A 1 120 ? 28.737 -16.015 14.052  0.60 23.80 ?  120 GLU   A CG   1 
ATOM   2599 C CD   A GLU   A 1 120 ? 28.811 -16.722 15.497  0.40 28.67 ?  120 GLU   A CD   1 
ATOM   2600 C CD   B GLU   A 1 120 ? 28.965 -16.768 15.349  0.60 28.86 ?  120 GLU   A CD   1 
ATOM   2601 O OE1  A GLU   A 1 120 ? 28.355 -16.162 16.517  0.40 30.50 ?  120 GLU   A OE1  1 
ATOM   2602 O OE1  B GLU   A 1 120 ? 28.485 -16.300 16.404  0.60 31.25 ?  120 GLU   A OE1  1 
ATOM   2603 O OE2  A GLU   A 1 120 ? 29.378 -17.834 15.526  0.40 30.31 -1 120 GLU   A OE2  1 
ATOM   2604 O OE2  B GLU   A 1 120 ? 29.618 -17.832 15.311  0.60 30.93 -1 120 GLU   A OE2  1 
ATOM   2605 H H    A GLU   A 1 120 ? 28.557 -13.425 12.683  0.40 16.27 ?  120 GLU   A H    1 
ATOM   2606 H H    B GLU   A 1 120 ? 28.538 -13.412 12.692  0.60 14.94 ?  120 GLU   A H    1 
ATOM   2607 H HA   A GLU   A 1 120 ? 26.992 -15.473 12.208  0.40 18.48 ?  120 GLU   A HA   1 
ATOM   2608 H HA   B GLU   A 1 120 ? 26.969 -15.454 12.154  0.60 16.35 ?  120 GLU   A HA   1 
ATOM   2609 H HB2  A GLU   A 1 120 ? 27.763 -14.262 14.622  0.40 23.71 ?  120 GLU   A HB2  1 
ATOM   2610 H HB2  B GLU   A 1 120 ? 27.712 -14.361 14.636  0.60 21.22 ?  120 GLU   A HB2  1 
ATOM   2611 H HB3  A GLU   A 1 120 ? 26.754 -15.486 14.617  0.40 23.71 ?  120 GLU   A HB3  1 
ATOM   2612 H HB3  B GLU   A 1 120 ? 26.794 -15.650 14.525  0.60 21.22 ?  120 GLU   A HB3  1 
ATOM   2613 H HG2  A GLU   A 1 120 ? 28.522 -16.701 13.479  0.40 29.74 ?  120 GLU   A HG2  1 
ATOM   2614 H HG2  B GLU   A 1 120 ? 28.643 -16.665 13.339  0.60 28.54 ?  120 GLU   A HG2  1 
ATOM   2615 H HG3  A GLU   A 1 120 ? 29.476 -15.535 13.987  0.40 29.74 ?  120 GLU   A HG3  1 
ATOM   2616 H HG3  B GLU   A 1 120 ? 29.516 -15.461 13.899  0.60 28.54 ?  120 GLU   A HG3  1 
ATOM   2617 N N    . VAL   A 1 121 ? 25.461 -12.802 13.066  1.00 12.47 ?  121 VAL   A N    1 
ATOM   2618 C CA   . VAL   A 1 121 ? 24.168 -12.136 13.213  1.00 12.58 ?  121 VAL   A CA   1 
ATOM   2619 C C    . VAL   A 1 121 ? 24.279 -10.748 12.586  1.00 11.61 ?  121 VAL   A C    1 
ATOM   2620 O O    . VAL   A 1 121 ? 25.255 -10.028 12.828  1.00 12.65 ?  121 VAL   A O    1 
ATOM   2621 C CB   . VAL   A 1 121 ? 23.764 -11.982 14.700  1.00 15.56 ?  121 VAL   A CB   1 
ATOM   2622 C CG1  . VAL   A 1 121 ? 22.379 -11.349 14.823  1.00 16.50 ?  121 VAL   A CG1  1 
ATOM   2623 C CG2  . VAL   A 1 121 ? 23.799 -13.302 15.451  1.00 17.74 ?  121 VAL   A CG2  1 
ATOM   2624 H H    A VAL   A 1 121 ? 26.129 -12.270 13.171  0.40 14.94 ?  121 VAL   A H    1 
ATOM   2625 H H    B VAL   A 1 121 ? 26.129 -12.268 13.152  0.60 14.94 ?  121 VAL   A H    1 
ATOM   2626 H HA   . VAL   A 1 121 ? 23.483 -12.650 12.757  1.00 15.07 ?  121 VAL   A HA   1 
ATOM   2627 H HB   . VAL   A 1 121 ? 24.394 -11.388 15.133  1.00 18.65 ?  121 VAL   A HB   1 
ATOM   2628 H HG11 . VAL   A 1 121 ? 22.089 -11.396 15.749  1.00 19.78 ?  121 VAL   A HG11 1 
ATOM   2629 H HG12 . VAL   A 1 121 ? 22.426 -10.423 14.541  1.00 19.78 ?  121 VAL   A HG12 1 
ATOM   2630 H HG13 . VAL   A 1 121 ? 21.756 -11.836 14.260  1.00 19.78 ?  121 VAL   A HG13 1 
ATOM   2631 H HG21 . VAL   A 1 121 ? 23.486 -13.158 16.366  1.00 21.26 ?  121 VAL   A HG21 1 
ATOM   2632 H HG22 . VAL   A 1 121 ? 23.210 -13.939 15.010  1.00 21.26 ?  121 VAL   A HG22 1 
ATOM   2633 H HG23 . VAL   A 1 121 ? 24.702 -13.643 15.467  1.00 21.26 ?  121 VAL   A HG23 1 
ATOM   2634 N N    . LEU   A 1 122 ? 23.257 -10.349 11.818  1.00 11.31 ?  122 LEU   A N    1 
ATOM   2635 C CA   . LEU   A 1 122 ? 23.249 -9.045  11.159  1.00 11.54 ?  122 LEU   A CA   1 
ATOM   2636 C C    . LEU   A 1 122 ? 21.851 -8.456  11.111  1.00 11.32 ?  122 LEU   A C    1 
ATOM   2637 O O    . LEU   A 1 122 ? 20.866 -9.187  10.982  1.00 12.44 ?  122 LEU   A O    1 
ATOM   2638 C CB   . LEU   A 1 122 ? 23.665 -9.129  9.685   1.00 13.47 ?  122 LEU   A CB   1 
ATOM   2639 C CG   . LEU   A 1 122 ? 24.862 -9.971  9.282   1.00 13.24 ?  122 LEU   A CG   1 
ATOM   2640 C CD1  . LEU   A 1 122 ? 24.457 -11.422 9.065   1.00 14.18 ?  122 LEU   A CD1  1 
ATOM   2641 C CD2  . LEU   A 1 122 ? 25.466 -9.385  8.021   1.00 12.45 ?  122 LEU   A CD2  1 
ATOM   2642 H H    . LEU   A 1 122 ? 22.546 -10.822 11.668  1.00 13.55 ?  122 LEU   A H    1 
ATOM   2643 H HA   . LEU   A 1 122 ? 23.841 -8.435  11.627  1.00 13.82 ?  122 LEU   A HA   1 
ATOM   2644 H HB2  . LEU   A 1 122 ? 22.913 -9.478  9.190   1.00 16.13 ?  122 LEU   A HB2  1 
ATOM   2645 H HB3  . LEU   A 1 122 ? 23.851 -8.228  9.386   1.00 16.13 ?  122 LEU   A HB3  1 
ATOM   2646 H HG   . LEU   A 1 122 ? 25.543 -9.938  9.979   1.00 15.86 ?  122 LEU   A HG   1 
ATOM   2647 H HD11 . LEU   A 1 122 ? 25.229 -11.926 8.760   1.00 16.99 ?  122 LEU   A HD11 1 
ATOM   2648 H HD12 . LEU   A 1 122 ? 24.138 -11.787 9.905   1.00 16.99 ?  122 LEU   A HD12 1 
ATOM   2649 H HD13 . LEU   A 1 122 ? 23.756 -11.456 8.399   1.00 16.99 ?  122 LEU   A HD13 1 
ATOM   2650 H HD21 . LEU   A 1 122 ? 26.196 -9.953  7.719   1.00 14.91 ?  122 LEU   A HD21 1 
ATOM   2651 H HD22 . LEU   A 1 122 ? 24.781 -9.339  7.335   1.00 14.91 ?  122 LEU   A HD22 1 
ATOM   2652 H HD23 . LEU   A 1 122 ? 25.803 -8.494  8.210   1.00 14.91 ?  122 LEU   A HD23 1 
ATOM   2653 N N    A LEU   A 1 123 ? 21.793 -7.124  11.149  0.40 11.06 ?  123 LEU   A N    1 
ATOM   2654 N N    B LEU   A 1 123 ? 21.780 -7.131  11.247  0.60 10.62 ?  123 LEU   A N    1 
ATOM   2655 C CA   A LEU   A 1 123 ? 20.594 -6.337  10.872  0.40 10.92 ?  123 LEU   A CA   1 
ATOM   2656 C CA   B LEU   A 1 123 ? 20.618 -6.338  10.859  0.60 10.48 ?  123 LEU   A CA   1 
ATOM   2657 C C    A LEU   A 1 123 ? 20.784 -5.705  9.499   0.40 10.42 ?  123 LEU   A C    1 
ATOM   2658 C C    B LEU   A 1 123 ? 20.860 -5.831  9.448   0.60 10.05 ?  123 LEU   A C    1 
ATOM   2659 O O    A LEU   A 1 123 ? 21.756 -4.974  9.290   0.40 10.54 ?  123 LEU   A O    1 
ATOM   2660 O O    B LEU   A 1 123 ? 21.938 -5.311  9.157   0.60 9.99  ?  123 LEU   A O    1 
ATOM   2661 C CB   A LEU   A 1 123 ? 20.437 -5.243  11.929  0.40 11.54 ?  123 LEU   A CB   1 
ATOM   2662 C CB   B LEU   A 1 123 ? 20.473 -5.139  11.797  0.60 11.36 ?  123 LEU   A CB   1 
ATOM   2663 C CG   A LEU   A 1 123 ? 19.439 -4.126  11.612  0.40 11.98 ?  123 LEU   A CG   1 
ATOM   2664 C CG   B LEU   A 1 123 ? 19.384 -4.112  11.465  0.60 12.53 ?  123 LEU   A CG   1 
ATOM   2665 C CD1  A LEU   A 1 123 ? 18.016 -4.661  11.615  0.40 12.59 ?  123 LEU   A CD1  1 
ATOM   2666 C CD1  B LEU   A 1 123 ? 18.004 -4.749  11.465  0.60 13.45 ?  123 LEU   A CD1  1 
ATOM   2667 C CD2  A LEU   A 1 123 ? 19.592 -2.978  12.598  0.40 12.54 ?  123 LEU   A CD2  1 
ATOM   2668 C CD2  B LEU   A 1 123 ? 19.430 -2.945  12.446  0.60 13.27 ?  123 LEU   A CD2  1 
ATOM   2669 H H    A LEU   A 1 123 ? 22.477 -6.626  11.326  0.40 13.24 ?  123 LEU   A H    1 
ATOM   2670 H H    B LEU   A 1 123 ? 22.419 -6.650  11.565  0.60 12.71 ?  123 LEU   A H    1 
ATOM   2671 H HA   A LEU   A 1 123 ? 19.806 -6.900  10.864  0.40 13.08 ?  123 LEU   A HA   1 
ATOM   2672 H HA   B LEU   A 1 123 ? 19.813 -6.874  10.877  0.60 12.56 ?  123 LEU   A HA   1 
ATOM   2673 H HB2  A LEU   A 1 123 ? 20.145 -5.660  12.756  0.40 13.82 ?  123 LEU   A HB2  1 
ATOM   2674 H HB2  B LEU   A 1 123 ? 20.281 -5.476  12.681  0.60 13.61 ?  123 LEU   A HB2  1 
ATOM   2675 H HB3  A LEU   A 1 123 ? 21.300 -4.824  12.068  0.40 13.82 ?  123 LEU   A HB3  1 
ATOM   2676 H HB3  B LEU   A 1 123 ? 21.314 -4.662  11.805  0.60 13.61 ?  123 LEU   A HB3  1 
ATOM   2677 H HG   A LEU   A 1 123 ? 19.616 -3.769  10.727  0.40 14.35 ?  123 LEU   A HG   1 
ATOM   2678 H HG   B LEU   A 1 123 ? 19.541 -3.750  10.578  0.60 15.02 ?  123 LEU   A HG   1 
ATOM   2679 H HD11 A LEU   A 1 123 ? 17.403 -3.936  11.418  0.40 15.08 ?  123 LEU   A HD11 1 
ATOM   2680 H HD11 B LEU   A 1 123 ? 17.335 -4.062  11.321  0.60 16.11 ?  123 LEU   A HD11 1 
ATOM   2681 H HD12 A LEU   A 1 123 ? 17.936 -5.354  10.938  0.40 15.08 ?  123 LEU   A HD12 1 
ATOM   2682 H HD12 B LEU   A 1 123 ? 17.961 -5.407  10.753  0.60 16.11 ?  123 LEU   A HD12 1 
ATOM   2683 H HD13 A LEU   A 1 123 ? 17.820 -5.033  12.489  0.40 15.08 ?  123 LEU   A HD13 1 
ATOM   2684 H HD13 B LEU   A 1 123 ? 17.855 -5.180  12.322  0.60 16.11 ?  123 LEU   A HD13 1 
ATOM   2685 H HD21 A LEU   A 1 123 ? 18.949 -2.286  12.378  0.40 15.02 ?  123 LEU   A HD21 1 
ATOM   2686 H HD21 B LEU   A 1 123 ? 18.734 -2.310  12.220  0.60 15.90 ?  123 LEU   A HD21 1 
ATOM   2687 H HD22 A LEU   A 1 123 ? 19.427 -3.311  13.494  0.40 15.02 ?  123 LEU   A HD22 1 
ATOM   2688 H HD22 B LEU   A 1 123 ? 19.287 -3.286  13.345  0.60 15.90 ?  123 LEU   A HD22 1 
ATOM   2689 H HD23 A LEU   A 1 123 ? 20.493 -2.627  12.534  0.40 15.02 ?  123 LEU   A HD23 1 
ATOM   2690 H HD23 B LEU   A 1 123 ? 20.299 -2.520  12.389  0.60 15.90 ?  123 LEU   A HD23 1 
ATOM   2691 N N    . ALA   A 1 124 ? 19.869 -5.968  8.573   1.00 10.02 ?  124 ALA   A N    1 
ATOM   2692 C CA   . ALA   A 1 124 ? 20.105 -5.648  7.176   1.00 10.21 ?  124 ALA   A CA   1 
ATOM   2693 C C    . ALA   A 1 124 ? 18.861 -5.193  6.435   1.00 10.09 ?  124 ALA   A C    1 
ATOM   2694 O O    . ALA   A 1 124 ? 17.734 -5.557  6.806   1.00 10.87 ?  124 ALA   A O    1 
ATOM   2695 C CB   . ALA   A 1 124 ? 20.685 -6.862  6.438   1.00 10.50 ?  124 ALA   A CB   1 
ATOM   2696 H H    A ALA   A 1 124 ? 19.112 -6.349  8.724   0.40 12.00 ?  124 ALA   A H    1 
ATOM   2697 H H    B ALA   A 1 124 ? 19.073 -6.239  8.757   0.60 12.00 ?  124 ALA   A H    1 
ATOM   2698 H HA   . ALA   A 1 124 ? 20.773 -4.948  7.144   1.00 12.23 ?  124 ALA   A HA   1 
ATOM   2699 H HB1  . ALA   A 1 124 ? 20.842 -6.635  5.508   1.00 12.57 ?  124 ALA   A HB1  1 
ATOM   2700 H HB2  . ALA   A 1 124 ? 21.529 -7.120  6.856   1.00 12.57 ?  124 ALA   A HB2  1 
ATOM   2701 H HB3  . ALA   A 1 124 ? 20.059 -7.602  6.495   1.00 12.57 ?  124 ALA   A HB3  1 
ATOM   2702 N N    A PRO   A 1 125 ? 19.037 -4.431  5.360   0.40 9.94  ?  125 PRO   A N    1 
ATOM   2703 N N    B PRO   A 1 125 ? 19.038 -4.415  5.373   0.60 10.25 ?  125 PRO   A N    1 
ATOM   2704 C CA   A PRO   A 1 125 ? 17.972 -4.224  4.380   0.40 10.15 ?  125 PRO   A CA   1 
ATOM   2705 C CA   B PRO   A 1 125 ? 17.949 -4.111  4.448   0.60 10.79 ?  125 PRO   A CA   1 
ATOM   2706 C C    A PRO   A 1 125 ? 18.051 -5.293  3.296   0.40 9.67  ?  125 PRO   A C    1 
ATOM   2707 C C    B PRO   A 1 125 ? 17.980 -5.129  3.314   0.60 10.81 ?  125 PRO   A C    1 
ATOM   2708 O O    A PRO   A 1 125 ? 19.056 -5.989  3.147   0.40 9.86  ?  125 PRO   A O    1 
ATOM   2709 O O    B PRO   A 1 125 ? 18.894 -5.946  3.205   0.60 11.14 ?  125 PRO   A O    1 
ATOM   2710 C CB   A PRO   A 1 125 ? 18.360 -2.869  3.781   0.40 10.40 ?  125 PRO   A CB   1 
ATOM   2711 C CB   B PRO   A 1 125 ? 18.370 -2.736  3.923   0.60 10.91 ?  125 PRO   A CB   1 
ATOM   2712 C CG   A PRO   A 1 125 ? 19.868 -2.940  3.742   0.40 10.56 ?  125 PRO   A CG   1 
ATOM   2713 C CG   B PRO   A 1 125 ? 19.881 -2.886  3.789   0.60 11.14 ?  125 PRO   A CG   1 
ATOM   2714 C CD   A PRO   A 1 125 ? 20.251 -3.662  5.017   0.40 10.10 ?  125 PRO   A CD   1 
ATOM   2715 C CD   B PRO   A 1 125 ? 20.309 -3.815  4.916   0.60 10.50 ?  125 PRO   A CD   1 
ATOM   2716 H HA   A PRO   A 1 125 ? 17.094 -4.198  4.795   0.40 12.16 ?  125 PRO   A HA   1 
ATOM   2717 H HA   B PRO   A 1 125 ? 17.081 -4.086  4.886   0.60 12.92 ?  125 PRO   A HA   1 
ATOM   2718 H HB2  A PRO   A 1 125 ? 17.988 -2.786  2.890   0.40 12.45 ?  125 PRO   A HB2  1 
ATOM   2719 H HB2  B PRO   A 1 125 ? 17.949 -2.566  3.066   0.60 13.06 ?  125 PRO   A HB2  1 
ATOM   2720 H HB3  A PRO   A 1 125 ? 18.056 -2.154  4.359   0.40 12.45 ?  125 PRO   A HB3  1 
ATOM   2721 H HB3  B PRO   A 1 125 ? 18.136 -2.050  4.571   0.60 13.06 ?  125 PRO   A HB3  1 
ATOM   2722 H HG2  A PRO   A 1 125 ? 20.154 -3.445  2.962   0.40 12.65 ?  125 PRO   A HG2  1 
ATOM   2723 H HG2  B PRO   A 1 125 ? 20.091 -3.277  2.926   0.60 13.34 ?  125 PRO   A HG2  1 
ATOM   2724 H HG3  A PRO   A 1 125 ? 20.238 -2.045  3.726   0.40 12.65 ?  125 PRO   A HG3  1 
ATOM   2725 H HG3  B PRO   A 1 125 ? 20.301 -2.018  3.882   0.60 13.34 ?  125 PRO   A HG3  1 
ATOM   2726 H HD2  A PRO   A 1 125 ? 21.004 -4.256  4.856   0.40 12.10 ?  125 PRO   A HD2  1 
ATOM   2727 H HD2  B PRO   A 1 125 ? 20.913 -4.498  4.575   0.60 12.57 ?  125 PRO   A HD2  1 
ATOM   2728 H HD3  A PRO   A 1 125 ? 20.452 -3.021  5.719   0.40 12.10 ?  125 PRO   A HD3  1 
ATOM   2729 H HD3  B PRO   A 1 125 ? 20.725 -3.303  5.629   0.60 12.57 ?  125 PRO   A HD3  1 
ATOM   2730 N N    A LEU   A 1 126 ? 16.979 -5.392  2.514   0.40 9.37  ?  126 LEU   A N    1 
ATOM   2731 N N    B LEU   A 1 126 ? 16.975 -5.049  2.448   0.60 11.16 ?  126 LEU   A N    1 
ATOM   2732 C CA   A LEU   A 1 126 ? 17.033 -6.201  1.304   0.40 9.96  ?  126 LEU   A CA   1 
ATOM   2733 C CA   B LEU   A 1 126 ? 16.939 -5.890  1.256   0.60 11.01 ?  126 LEU   A CA   1 
ATOM   2734 C C    A LEU   A 1 126 ? 17.971 -5.552  0.294   0.40 10.59 ?  126 LEU   A C    1 
ATOM   2735 C C    B LEU   A 1 126 ? 17.862 -5.304  0.191   0.60 10.86 ?  126 LEU   A C    1 
ATOM   2736 O O    A LEU   A 1 126 ? 17.840 -4.364  -0.022  0.40 11.62 ?  126 LEU   A O    1 
ATOM   2737 O O    B LEU   A 1 126 ? 17.574 -4.247  -0.381  0.60 11.45 ?  126 LEU   A O    1 
ATOM   2738 C CB   A LEU   A 1 126 ? 15.638 -6.360  0.701   0.40 10.48 ?  126 LEU   A CB   1 
ATOM   2739 C CB   B LEU   A 1 126 ? 15.514 -5.998  0.730   0.60 12.15 ?  126 LEU   A CB   1 
ATOM   2740 C CG   A LEU   A 1 126 ? 14.723 -7.349  1.427   0.40 11.08 ?  126 LEU   A CG   1 
ATOM   2741 C CG   B LEU   A 1 126 ? 14.594 -6.899  1.543   0.60 12.71 ?  126 LEU   A CG   1 
ATOM   2742 C CD1  A LEU   A 1 126 ? 13.302 -7.252  0.907   0.40 12.14 ?  126 LEU   A CD1  1 
ATOM   2743 C CD1  B LEU   A 1 126 ? 13.181 -6.757  1.018   0.60 13.39 ?  126 LEU   A CD1  1 
ATOM   2744 C CD2  A LEU   A 1 126 ? 15.248 -8.767  1.274   0.40 10.64 ?  126 LEU   A CD2  1 
ATOM   2745 C CD2  B LEU   A 1 126 ? 15.052 -8.353  1.473   0.60 12.84 ?  126 LEU   A CD2  1 
ATOM   2746 H H    A LEU   A 1 126 ? 16.226 -5.004  2.653   0.40 11.21 ?  126 LEU   A H    1 
ATOM   2747 H H    B LEU   A 1 126 ? 16.302 -4.517  2.530   0.60 13.36 ?  126 LEU   A H    1 
ATOM   2748 H HA   A LEU   A 1 126 ? 17.381 -7.082  1.519   0.40 11.93 ?  126 LEU   A HA   1 
ATOM   2749 H HA   B LEU   A 1 126 ? 17.253 -6.779  1.487   0.60 13.19 ?  126 LEU   A HA   1 
ATOM   2750 H HB2  A LEU   A 1 126 ? 15.198 -5.497  0.709   0.40 12.55 ?  126 LEU   A HB2  1 
ATOM   2751 H HB2  B LEU   A 1 126 ? 15.120 -5.110  0.723   0.60 14.55 ?  126 LEU   A HB2  1 
ATOM   2752 H HB3  A LEU   A 1 126 ? 15.731 -6.669  -0.215  0.40 12.55 ?  126 LEU   A HB3  1 
ATOM   2753 H HB3  B LEU   A 1 126 ? 15.544 -6.349  -0.172  0.60 14.55 ?  126 LEU   A HB3  1 
ATOM   2754 H HG   A LEU   A 1 126 ? 14.715 -7.135  2.374   0.40 13.27 ?  126 LEU   A HG   1 
ATOM   2755 H HG   B LEU   A 1 126 ? 14.605 -6.617  2.473   0.60 15.23 ?  126 LEU   A HG   1 
ATOM   2756 H HD11 A LEU   A 1 126 ? 12.748 -7.884  1.388   0.40 14.55 ?  126 LEU   A HD11 1 
ATOM   2757 H HD11 B LEU   A 1 126 ? 12.598 -7.335  1.529   0.60 16.04 ?  126 LEU   A HD11 1 
ATOM   2758 H HD12 A LEU   A 1 126 ? 12.980 -6.349  1.051   0.40 14.55 ?  126 LEU   A HD12 1 
ATOM   2759 H HD12 B LEU   A 1 126 ? 12.904 -5.834  1.109   0.60 16.04 ?  126 LEU   A HD12 1 
ATOM   2760 H HD13 A LEU   A 1 126 ? 13.301 -7.458  -0.040  0.40 14.55 ?  126 LEU   A HD13 1 
ATOM   2761 H HD13 B LEU   A 1 126 ? 13.171 -7.017  0.082   0.60 16.04 ?  126 LEU   A HD13 1 
ATOM   2762 H HD21 A LEU   A 1 126 ? 14.575 -9.386  1.588   0.40 12.74 ?  126 LEU   A HD21 1 
ATOM   2763 H HD21 B LEU   A 1 126 ? 14.356 -8.921  1.831   0.60 15.38 ?  126 LEU   A HD21 1 
ATOM   2764 H HD22 A LEU   A 1 126 ? 15.442 -8.929  0.338   0.40 12.74 ?  126 LEU   A HD22 1 
ATOM   2765 H HD22 B LEU   A 1 126 ? 15.228 -8.582  0.547   0.60 15.38 ?  126 LEU   A HD22 1 
ATOM   2766 H HD23 A LEU   A 1 126 ? 16.059 -8.861  1.800   0.40 12.74 ?  126 LEU   A HD23 1 
ATOM   2767 H HD23 B LEU   A 1 126 ? 15.865 -8.455  1.996   0.60 15.38 ?  126 LEU   A HD23 1 
ATOM   2768 N N    A LEU   A 1 127 ? 18.916 -6.339  -0.214  0.40 10.30 ?  127 LEU   A N    1 
ATOM   2769 N N    B LEU   A 1 127 ? 18.956 -6.000  -0.102  0.60 10.06 ?  127 LEU   A N    1 
ATOM   2770 C CA   A LEU   A 1 127 ? 19.920 -5.808  -1.123  0.40 9.86  ?  127 LEU   A CA   1 
ATOM   2771 C CA   B LEU   A 1 127 ? 19.920 -5.483  -1.059  0.60 9.97  ?  127 LEU   A CA   1 
ATOM   2772 C C    A LEU   A 1 127 ? 19.314 -5.527  -2.488  0.40 9.42  ?  127 LEU   A C    1 
ATOM   2773 C C    B LEU   A 1 127 ? 19.315 -5.399  -2.456  0.60 9.54  ?  127 LEU   A C    1 
ATOM   2774 O O    A LEU   A 1 127 ? 18.511 -6.306  -3.009  0.40 9.56  ?  127 LEU   A O    1 
ATOM   2775 O O    B LEU   A 1 127 ? 18.451 -6.194  -2.839  0.60 10.30 ?  127 LEU   A O    1 
ATOM   2776 C CB   A LEU   A 1 127 ? 21.076 -6.793  -1.266  0.40 9.42  ?  127 LEU   A CB   1 
ATOM   2777 C CB   B LEU   A 1 127 ? 21.157 -6.376  -1.083  0.60 11.21 ?  127 LEU   A CB   1 
ATOM   2778 C CG   A LEU   A 1 127 ? 21.896 -7.018  0.003   0.40 8.55  ?  127 LEU   A CG   1 
ATOM   2779 C CG   B LEU   A 1 127 ? 21.947 -6.426  0.227   0.60 12.59 ?  127 LEU   A CG   1 
ATOM   2780 C CD1  A LEU   A 1 127 ? 23.030 -7.974  -0.290  0.40 8.38  ?  127 LEU   A CD1  1 
ATOM   2781 C CD1  B LEU   A 1 127 ? 23.122 -7.359  0.086   0.60 13.69 ?  127 LEU   A CD1  1 
ATOM   2782 C CD2  A LEU   A 1 127 ? 22.445 -5.707  0.548   0.40 8.81  ?  127 LEU   A CD2  1 
ATOM   2783 C CD2  B LEU   A 1 127 ? 22.422 -5.036  0.627   0.60 13.72 ?  127 LEU   A CD2  1 
ATOM   2784 H H    A LEU   A 1 127 ? 18.996 -7.183  -0.047  0.40 12.33 ?  127 LEU   A H    1 
ATOM   2785 H H    B LEU   A 1 127 ? 19.170 -6.767  0.247   0.60 12.04 ?  127 LEU   A H    1 
ATOM   2786 H HA   A LEU   A 1 127 ? 20.267 -4.981  -0.768  0.40 11.81 ?  127 LEU   A HA   1 
ATOM   2787 H HA   B LEU   A 1 127 ? 20.192 -4.594  -0.789  0.60 11.94 ?  127 LEU   A HA   1 
ATOM   2788 H HB2  A LEU   A 1 127 ? 20.725 -7.656  -1.541  0.40 11.28 ?  127 LEU   A HB2  1 
ATOM   2789 H HB2  B LEU   A 1 127 ? 20.883 -7.284  -1.290  0.60 13.43 ?  127 LEU   A HB2  1 
ATOM   2790 H HB3  A LEU   A 1 127 ? 21.688 -6.463  -1.947  0.40 11.28 ?  127 LEU   A HB3  1 
ATOM   2791 H HB3  B LEU   A 1 127 ? 21.760 -6.054  -1.771  0.60 13.43 ?  127 LEU   A HB3  1 
ATOM   2792 H HG   A LEU   A 1 127 ? 21.327 -7.423  0.683   0.40 10.23 ?  127 LEU   A HG   1 
ATOM   2793 H HG   B LEU   A 1 127 ? 21.374 -6.766  0.935   0.60 15.08 ?  127 LEU   A HG   1 
ATOM   2794 H HD11 A LEU   A 1 127 ? 23.507 -8.165  0.534   0.40 10.03 ?  127 LEU   A HD11 1 
ATOM   2795 H HD11 B LEU   A 1 127 ? 23.644 -7.334  0.904   0.60 16.40 ?  127 LEU   A HD11 1 
ATOM   2796 H HD12 A LEU   A 1 127 ? 22.667 -8.799  -0.657  0.40 10.03 ?  127 LEU   A HD12 1 
ATOM   2797 H HD12 B LEU   A 1 127 ? 22.795 -8.256  -0.072  0.60 16.40 ?  127 LEU   A HD12 1 
ATOM   2798 H HD13 A LEU   A 1 127 ? 23.629 -7.565  -0.932  0.40 10.03 ?  127 LEU   A HD13 1 
ATOM   2799 H HD13 B LEU   A 1 127 ? 23.666 -7.065  -0.661  0.60 16.40 ?  127 LEU   A HD13 1 
ATOM   2800 H HD21 A LEU   A 1 127 ? 23.119 -5.900  1.216   0.40 10.55 ?  127 LEU   A HD21 1 
ATOM   2801 H HD21 B LEU   A 1 127 ? 23.066 -5.117  1.345   0.60 16.43 ?  127 LEU   A HD21 1 
ATOM   2802 H HD22 A LEU   A 1 127 ? 22.837 -5.206  -0.185  0.40 10.55 ?  127 LEU   A HD22 1 
ATOM   2803 H HD22 B LEU   A 1 127 ? 22.832 -4.613  -0.143  0.60 16.43 ?  127 LEU   A HD22 1 
ATOM   2804 H HD23 A LEU   A 1 127 ? 21.719 -5.201  0.943   0.40 10.55 ?  127 LEU   A HD23 1 
ATOM   2805 H HD23 B LEU   A 1 127 ? 21.658 -4.515  0.922   0.60 16.43 ?  127 LEU   A HD23 1 
ATOM   2806 N N    A SER   A 1 128 ? 19.716 -4.404  -3.067  0.40 9.69  ?  128 SER   A N    1 
ATOM   2807 N N    B SER   A 1 128 ? 19.783 -4.410  -3.215  0.60 9.74  ?  128 SER   A N    1 
ATOM   2808 C CA   A SER   A 1 128 ? 19.290 -3.944  -4.380  0.40 9.85  ?  128 SER   A CA   1 
ATOM   2809 C CA   B SER   A 1 128 ? 19.425 -4.115  -4.598  0.60 9.21  ?  128 SER   A CA   1 
ATOM   2810 C C    A SER   A 1 128 ? 17.828 -3.518  -4.411  0.40 10.46 ?  128 SER   A C    1 
ATOM   2811 C C    B SER   A 1 128 ? 17.993 -3.616  -4.779  0.60 9.46  ?  128 SER   A C    1 
ATOM   2812 O O    A SER   A 1 128 ? 17.290 -3.270  -5.493  0.40 11.19 ?  128 SER   A O    1 
ATOM   2813 O O    B SER   A 1 128 ? 17.630 -3.250  -5.898  0.60 10.19 ?  128 SER   A O    1 
ATOM   2814 C CB   A SER   A 1 128 ? 19.617 -4.938  -5.501  0.40 10.04 ?  128 SER   A CB   1 
ATOM   2815 C CB   B SER   A 1 128 ? 19.758 -5.247  -5.584  0.60 9.85  ?  128 SER   A CB   1 
ATOM   2816 O OG   A SER   A 1 128 ? 21.018 -5.169  -5.564  0.40 10.68 ?  128 SER   A OG   1 
ATOM   2817 O OG   B SER   A 1 128 ? 21.167 -5.406  -5.697  0.60 10.37 ?  128 SER   A OG   1 
ATOM   2818 H H    A SER   A 1 128 ? 20.269 -3.862  -2.694  0.40 11.61 ?  128 SER   A H    1 
ATOM   2819 H H    B SER   A 1 128 ? 20.378 -3.856  -2.920  0.60 11.67 ?  128 SER   A H    1 
ATOM   2820 H HA   A SER   A 1 128 ? 19.804 -3.154  -4.571  0.40 11.80 ?  128 SER   A HA   1 
ATOM   2821 H HA   B SER   A 1 128 ? 19.978 -3.375  -4.868  0.60 11.03 ?  128 SER   A HA   1 
ATOM   2822 H HB2  A SER   A 1 128 ? 19.161 -5.777  -5.330  0.40 12.02 ?  128 SER   A HB2  1 
ATOM   2823 H HB2  B SER   A 1 128 ? 19.369 -6.077  -5.268  0.60 11.79 ?  128 SER   A HB2  1 
ATOM   2824 H HB3  A SER   A 1 128 ? 19.322 -4.566  -6.349  0.40 12.02 ?  128 SER   A HB3  1 
ATOM   2825 H HB3  B SER   A 1 128 ? 19.397 -5.023  -6.459  0.60 11.79 ?  128 SER   A HB3  1 
ATOM   2826 H HG   A SER   A 1 128 ? 21.421 -4.443  -5.695  0.40 12.79 ?  128 SER   A HG   1 
ATOM   2827 H HG   B SER   A 1 128 ? 21.513 -4.684  -5.959  0.60 12.42 ?  128 SER   A HG   1 
ATOM   2828 N N    A ALA   A 1 129 ? 17.179 -3.400  -3.253  0.40 10.52 ?  129 ALA   A N    1 
ATOM   2829 N N    B ALA   A 1 129 ? 17.181 -3.577  -3.724  0.60 10.46 ?  129 ALA   A N    1 
ATOM   2830 C CA   A ALA   A 1 129 ? 15.802 -2.933  -3.187  0.40 9.75  ?  129 ALA   A CA   1 
ATOM   2831 C CA   B ALA   A 1 129 ? 15.824 -3.050  -3.808  0.60 11.15 ?  129 ALA   A CA   1 
ATOM   2832 C C    A ALA   A 1 129 ? 15.782 -1.408  -3.208  0.40 9.35  ?  129 ALA   A C    1 
ATOM   2833 C C    B ALA   A 1 129 ? 15.860 -1.523  -3.712  0.60 11.16 ?  129 ALA   A C    1 
ATOM   2834 O O    A ALA   A 1 129 ? 16.813 -0.743  -3.356  0.40 9.27  ?  129 ALA   A O    1 
ATOM   2835 O O    B ALA   A 1 129 ? 16.922 -0.892  -3.744  0.60 11.68 ?  129 ALA   A O    1 
ATOM   2836 C CB   A ALA   A 1 129 ? 15.101 -3.502  -1.956  0.40 9.91  ?  129 ALA   A CB   1 
ATOM   2837 C CB   B ALA   A 1 129 ? 14.933 -3.722  -2.762  0.60 12.62 ?  129 ALA   A CB   1 
ATOM   2838 H H    A ALA   A 1 129 ? 17.521 -3.582  -2.483  0.40 12.60 ?  129 ALA   A H    1 
ATOM   2839 H H    B ALA   A 1 129 ? 17.398 -3.863  -2.936  0.60 12.53 ?  129 ALA   A H    1 
ATOM   2840 H HA   A ALA   A 1 129 ? 15.329 -3.245  -3.966  0.40 11.67 ?  129 ALA   A HA   1 
ATOM   2841 H HA   B ALA   A 1 129 ? 15.468 -3.271  -4.676  0.60 13.35 ?  129 ALA   A HA   1 
ATOM   2842 H HB1  A ALA   A 1 129 ? 14.182 -3.192  -1.941  0.40 11.86 ?  129 ALA   A HB1  1 
ATOM   2843 H HB1  B ALA   A 1 129 ? 14.037 -3.361  -2.837  0.60 15.12 ?  129 ALA   A HB1  1 
ATOM   2844 H HB2  A ALA   A 1 129 ? 15.120 -4.472  -2.006  0.40 11.86 ?  129 ALA   A HB2  1 
ATOM   2845 H HB2  B ALA   A 1 129 ? 14.920 -4.679  -2.925  0.60 15.12 ?  129 ALA   A HB2  1 
ATOM   2846 H HB3  A ALA   A 1 129 ? 15.563 -3.205  -1.157  0.40 11.86 ?  129 ALA   A HB3  1 
ATOM   2847 H HB3  B ALA   A 1 129 ? 15.290 -3.544  -1.877  0.60 15.12 ?  129 ALA   A HB3  1 
ATOM   2848 N N    A GLY   A 1 130 ? 14.593 -0.837  -3.043  0.40 10.31 ?  130 GLY   A N    1 
ATOM   2849 N N    B GLY   A 1 130 ? 14.682 -0.910  -3.625  0.60 11.54 ?  130 GLY   A N    1 
ATOM   2850 C CA   A GLY   A 1 130 ? 14.484 0.611   -3.025  0.40 11.03 ?  130 GLY   A CA   1 
ATOM   2851 C CA   B GLY   A 1 130 ? 14.610 0.540   -3.548  0.60 12.74 ?  130 GLY   A CA   1 
ATOM   2852 C C    A GLY   A 1 130 ? 15.047 1.207   -4.301  0.40 10.31 ?  130 GLY   A C    1 
ATOM   2853 C C    B GLY   A 1 130 ? 15.267 1.191   -4.748  0.60 12.37 ?  130 GLY   A C    1 
ATOM   2854 O O    A GLY   A 1 130 ? 14.771 0.737   -5.410  0.40 9.77  ?  130 GLY   A O    1 
ATOM   2855 O O    B GLY   A 1 130 ? 15.065 0.778   -5.895  0.60 12.62 ?  130 GLY   A O    1 
ATOM   2856 H H    A GLY   A 1 130 ? 13.846 -1.258  -2.933  0.40 12.34 ?  130 GLY   A H    1 
ATOM   2857 H H    B GLY   A 1 130 ? 13.925 -1.311  -3.600  0.60 13.82 ?  130 GLY   A H    1 
ATOM   2858 H HA2  A GLY   A 1 130 ? 13.547 0.868   -2.929  0.40 13.21 ?  130 GLY   A HA2  1 
ATOM   2859 H HA2  B GLY   A 1 130 ? 13.679 0.815   -3.513  0.60 15.26 ?  130 GLY   A HA2  1 
ATOM   2860 H HA3  A GLY   A 1 130 ? 14.976 0.968   -2.271  0.40 13.21 ?  130 GLY   A HA3  1 
ATOM   2861 H HA3  B GLY   A 1 130 ? 15.056 0.854   -2.747  0.60 15.26 ?  130 GLY   A HA3  1 
ATOM   2862 N N    A ILE   A 1 131 ? 15.853 2.256   -4.150  0.40 10.37 ?  131 ILE   A N    1 
ATOM   2863 N N    B ILE   A 1 131 ? 16.075 2.221   -4.485  0.60 12.43 ?  131 ILE   A N    1 
ATOM   2864 C CA   A ILE   A 1 131 ? 16.336 3.021   -5.297  0.40 10.30 ?  131 ILE   A CA   1 
ATOM   2865 C CA   B ILE   A 1 131 ? 16.706 2.989   -5.552  0.60 12.38 ?  131 ILE   A CA   1 
ATOM   2866 C C    A ILE   A 1 131 ? 17.369 2.271   -6.131  0.40 9.82  ?  131 ILE   A C    1 
ATOM   2867 C C    B ILE   A 1 131 ? 17.699 2.177   -6.373  0.60 12.16 ?  131 ILE   A C    1 
ATOM   2868 O O    A ILE   A 1 131 ? 17.788 2.766   -7.182  0.40 10.12 ?  131 ILE   A O    1 
ATOM   2869 O O    B ILE   A 1 131 ? 18.147 2.655   -7.423  0.60 14.03 ?  131 ILE   A O    1 
ATOM   2870 C CB   A ILE   A 1 131 ? 16.854 4.414   -4.889  0.40 10.87 ?  131 ILE   A CB   1 
ATOM   2871 C CB   B ILE   A 1 131 ? 17.344 4.305   -5.040  0.60 13.46 ?  131 ILE   A CB   1 
ATOM   2872 C CG1  A ILE   A 1 131 ? 18.128 4.311   -4.045  0.40 11.74 ?  131 ILE   A CG1  1 
ATOM   2873 C CG1  B ILE   A 1 131 ? 18.553 4.032   -4.131  0.60 14.49 ?  131 ILE   A CG1  1 
ATOM   2874 C CG2  A ILE   A 1 131 ? 15.765 5.183   -4.147  0.40 11.54 ?  131 ILE   A CG2  1 
ATOM   2875 C CG2  B ILE   A 1 131 ? 16.296 5.179   -4.344  0.60 13.96 ?  131 ILE   A CG2  1 
ATOM   2876 C CD1  A ILE   A 1 131 ? 18.789 5.655   -3.768  0.40 12.64 ?  131 ILE   A CD1  1 
ATOM   2877 C CD1  B ILE   A 1 131 ? 19.220 5.297   -3.585  0.60 15.65 ?  131 ILE   A CD1  1 
ATOM   2878 H H    A ILE   A 1 131 ? 16.106 2.561   -3.386  0.40 12.42 ?  131 ILE   A H    1 
ATOM   2879 H H    B ILE   A 1 131 ? 16.258 2.492   -3.693  0.60 14.89 ?  131 ILE   A H    1 
ATOM   2880 H HA   A ILE   A 1 131 ? 15.575 3.165   -5.879  0.40 12.33 ?  131 ILE   A HA   1 
ATOM   2881 H HA   B ILE   A 1 131 ? 16.006 3.254   -6.162  0.60 14.83 ?  131 ILE   A HA   1 
ATOM   2882 H HB   A ILE   A 1 131 ? 17.065 4.900   -5.700  0.40 13.02 ?  131 ILE   A HB   1 
ATOM   2883 H HB   B ILE   A 1 131 ? 17.664 4.793   -5.814  0.60 16.13 ?  131 ILE   A HB   1 
ATOM   2884 H HG12 A ILE   A 1 131 ? 17.905 3.903   -3.193  0.40 14.06 ?  131 ILE   A HG12 1 
ATOM   2885 H HG12 B ILE   A 1 131 ? 18.263 3.501   -3.375  0.60 17.36 ?  131 ILE   A HG12 1 
ATOM   2886 H HG13 A ILE   A 1 131 ? 18.774 3.756   -4.513  0.40 14.06 ?  131 ILE   A HG13 1 
ATOM   2887 H HG13 B ILE   A 1 131 ? 19.224 3.548   -4.638  0.60 17.36 ?  131 ILE   A HG13 1 
ATOM   2888 H HG21 A ILE   A 1 131 ? 16.112 6.045   -3.877  0.40 13.82 ?  131 ILE   A HG21 1 
ATOM   2889 H HG21 B ILE   A 1 131 ? 16.668 6.062   -4.191  0.60 16.72 ?  131 ILE   A HG21 1 
ATOM   2890 H HG22 A ILE   A 1 131 ? 15.009 5.305   -4.741  0.40 13.82 ?  131 ILE   A HG22 1 
ATOM   2891 H HG22 B ILE   A 1 131 ? 15.514 5.247   -4.915  0.60 16.72 ?  131 ILE   A HG22 1 
ATOM   2892 H HG23 A ILE   A 1 131 ? 15.493 4.676   -3.364  0.40 13.82 ?  131 ILE   A HG23 1 
ATOM   2893 H HG23 B ILE   A 1 131 ? 16.052 4.770   -3.499  0.60 16.72 ?  131 ILE   A HG23 1 
ATOM   2894 H HD11 A ILE   A 1 131 ? 19.666 5.498   -3.381  0.40 15.14 ?  131 ILE   A HD11 1 
ATOM   2895 H HD11 B ILE   A 1 131 ? 20.040 5.054   -3.128  0.60 18.75 ?  131 ILE   A HD11 1 
ATOM   2896 H HD12 A ILE   A 1 131 ? 18.878 6.139   -4.603  0.40 15.14 ?  131 ILE   A HD12 1 
ATOM   2897 H HD12 B ILE   A 1 131 ? 19.419 5.898   -4.322  0.60 18.75 ?  131 ILE   A HD12 1 
ATOM   2898 H HD13 A ILE   A 1 131 ? 18.239 6.156   -3.149  0.40 15.14 ?  131 ILE   A HD13 1 
ATOM   2899 H HD13 B ILE   A 1 131 ? 18.614 5.734   -2.962  0.60 18.75 ?  131 ILE   A HD13 1 
ATOM   2900 N N    A PHE   A 1 132 ? 17.788 1.079   -5.687  0.40 9.95  ?  132 PHE   A N    1 
ATOM   2901 N N    B PHE   A 1 132 ? 18.062 0.968   -5.928  0.60 11.02 ?  132 PHE   A N    1 
ATOM   2902 C CA   A PHE   A 1 132 ? 18.647 0.245   -6.519  0.40 10.26 ?  132 PHE   A CA   1 
ATOM   2903 C CA   B PHE   A 1 132 ? 18.920 0.111   -6.739  0.60 11.10 ?  132 PHE   A CA   1 
ATOM   2904 C C    A PHE   A 1 132 ? 17.872 -0.490  -7.612  0.40 10.32 ?  132 PHE   A C    1 
ATOM   2905 C C    B PHE   A 1 132 ? 18.152 -0.658  -7.814  0.60 12.08 ?  132 PHE   A C    1 
ATOM   2906 O O    A PHE   A 1 132 ? 18.494 -1.047  -8.521  0.40 10.65 ?  132 PHE   A O    1 
ATOM   2907 O O    B PHE   A 1 132 ? 18.778 -1.348  -8.628  0.60 13.77 ?  132 PHE   A O    1 
ATOM   2908 C CB   A PHE   A 1 132 ? 19.445 -0.740  -5.654  0.40 10.71 ?  132 PHE   A CB   1 
ATOM   2909 C CB   B PHE   A 1 132 ? 19.713 -0.864  -5.860  0.60 10.33 ?  132 PHE   A CB   1 
ATOM   2910 C CG   A PHE   A 1 132 ? 20.706 -0.157  -5.045  0.40 11.02 ?  132 PHE   A CG   1 
ATOM   2911 C CG   B PHE   A 1 132 ? 20.897 -0.241  -5.146  0.60 10.65 ?  132 PHE   A CG   1 
ATOM   2912 C CD1  A PHE   A 1 132 ? 20.655 0.949   -4.208  0.40 11.81 ?  132 PHE   A CD1  1 
ATOM   2913 C CD1  B PHE   A 1 132 ? 20.711 0.690   -4.135  0.60 12.02 ?  132 PHE   A CD1  1 
ATOM   2914 C CD2  A PHE   A 1 132 ? 21.938 -0.748  -5.282  0.40 11.61 ?  132 PHE   A CD2  1 
ATOM   2915 C CD2  B PHE   A 1 132 ? 22.193 -0.631  -5.455  0.60 11.56 ?  132 PHE   A CD2  1 
ATOM   2916 C CE1  A PHE   A 1 132 ? 21.814 1.468   -3.643  0.40 12.54 ?  132 PHE   A CE1  1 
ATOM   2917 C CE1  B PHE   A 1 132 ? 21.794 1.242   -3.469  0.60 12.54 ?  132 PHE   A CE1  1 
ATOM   2918 C CE2  A PHE   A 1 132 ? 23.097 -0.238  -4.718  0.40 12.23 ?  132 PHE   A CE2  1 
ATOM   2919 C CE2  B PHE   A 1 132 ? 23.280 -0.081  -4.791  0.60 12.36 ?  132 PHE   A CE2  1 
ATOM   2920 C CZ   A PHE   A 1 132 ? 23.033 0.873   -3.896  0.40 12.64 ?  132 PHE   A CZ   1 
ATOM   2921 C CZ   B PHE   A 1 132 ? 23.078 0.857   -3.796  0.60 12.57 ?  132 PHE   A CZ   1 
ATOM   2922 H H    A PHE   A 1 132 ? 17.592 0.736   -4.922  0.40 11.92 ?  132 PHE   A H    1 
ATOM   2923 H H    B PHE   A 1 132 ? 17.833 0.636   -5.163  0.60 13.19 ?  132 PHE   A H    1 
ATOM   2924 H HA   A PHE   A 1 132 ? 19.284 0.816   -6.966  0.40 12.28 ?  132 PHE   A HA   1 
ATOM   2925 H HA   B PHE   A 1 132 ? 19.568 0.678   -7.178  0.60 13.29 ?  132 PHE   A HA   1 
ATOM   2926 H HB2  A PHE   A 1 132 ? 18.880 -1.041  -4.924  0.40 12.83 ?  132 PHE   A HB2  1 
ATOM   2927 H HB2  B PHE   A 1 132 ? 19.122 -1.228  -5.181  0.60 12.37 ?  132 PHE   A HB2  1 
ATOM   2928 H HB3  A PHE   A 1 132 ? 19.704 -1.498  -6.201  0.40 12.83 ?  132 PHE   A HB3  1 
ATOM   2929 H HB3  B PHE   A 1 132 ? 20.049 -1.586  -6.418  0.60 12.37 ?  132 PHE   A HB3  1 
ATOM   2930 H HD1  A PHE   A 1 132 ? 19.838 1.353   -4.032  0.40 14.15 ?  132 PHE   A HD1  1 
ATOM   2931 H HD1  B PHE   A 1 132 ? 19.851 0.951   -3.906  0.60 14.40 ?  132 PHE   A HD1  1 
ATOM   2932 H HD2  A PHE   A 1 132 ? 21.988 -1.496  -5.836  0.40 13.91 ?  132 PHE   A HD2  1 
ATOM   2933 H HD2  B PHE   A 1 132 ? 22.334 -1.267  -6.126  0.60 13.85 ?  132 PHE   A HD2  1 
ATOM   2934 H HE1  A PHE   A 1 132 ? 21.769 2.213   -3.089  0.40 15.02 ?  132 PHE   A HE1  1 
ATOM   2935 H HE1  B PHE   A 1 132 ? 21.657 1.874   -2.802  0.60 15.03 ?  132 PHE   A HE1  1 
ATOM   2936 H HE2  A PHE   A 1 132 ? 23.918 -0.640  -4.896  0.40 14.65 ?  132 PHE   A HE2  1 
ATOM   2937 H HE2  B PHE   A 1 132 ? 24.144 -0.346  -5.021  0.60 14.81 ?  132 PHE   A HE2  1 
ATOM   2938 H HZ   A PHE   A 1 132 ? 23.811 1.219   -3.520  0.40 15.14 ?  132 PHE   A HZ   1 
ATOM   2939 H HZ   B PHE   A 1 132 ? 23.804 1.229   -3.356  0.60 15.06 ?  132 PHE   A HZ   1 
ATOM   2940 N N    A GLY   A 1 133 ? 16.539 -0.510  -7.547  0.40 10.36 ?  133 GLY   A N    1 
ATOM   2941 N N    B GLY   A 1 133 ? 16.821 -0.583  -7.825  0.60 11.93 ?  133 GLY   A N    1 
ATOM   2942 C CA   A GLY   A 1 133 ? 15.718 -0.884  -8.685  0.40 11.26 ?  133 GLY   A CA   1 
ATOM   2943 C CA   B GLY   A 1 133 ? 16.033 -0.945  -8.985  0.60 12.42 ?  133 GLY   A CA   1 
ATOM   2944 C C    A GLY   A 1 133 ? 15.529 -2.363  -8.949  0.40 12.22 ?  133 GLY   A C    1 
ATOM   2945 C C    B GLY   A 1 133 ? 15.471 -2.356  -9.020  0.60 12.51 ?  133 GLY   A C    1 
ATOM   2946 O O    A GLY   A 1 133 ? 15.063 -2.714  -10.040 0.40 13.19 ?  133 GLY   A O    1 
ATOM   2947 O O    B GLY   A 1 133 ? 14.579 -2.616  -9.837  0.60 13.56 ?  133 GLY   A O    1 
ATOM   2948 H H    A GLY   A 1 133 ? 16.082 -0.299  -6.850  0.40 12.41 ?  133 GLY   A H    1 
ATOM   2949 H H    B GLY   A 1 133 ? 16.350 -0.324  -7.155  0.60 14.30 ?  133 GLY   A H    1 
ATOM   2950 H HA2  A GLY   A 1 133 ? 14.841 -0.481  -8.581  0.40 13.48 ?  133 GLY   A HA2  1 
ATOM   2951 H HA2  B GLY   A 1 133 ? 15.274 -0.354  -9.032  0.60 14.88 ?  133 GLY   A HA2  1 
ATOM   2952 H HA3  A GLY   A 1 133 ? 16.116 -0.517  -9.488  0.40 13.48 ?  133 GLY   A HA3  1 
ATOM   2953 H HA3  B GLY   A 1 133 ? 16.567 -0.797  -9.783  0.60 14.88 ?  133 GLY   A HA3  1 
ATOM   2954 N N    A ALA   A 1 134 ? 15.889 -3.244  -8.022  0.40 12.29 ?  134 ALA   A N    1 
ATOM   2955 N N    B ALA   A 1 134 ? 15.955 -3.272  -8.183  0.60 12.00 ?  134 ALA   A N    1 
ATOM   2956 C CA   A ALA   A 1 134 ? 15.621 -4.662  -8.208  0.40 12.76 ?  134 ALA   A CA   1 
ATOM   2957 C CA   B ALA   A 1 134 ? 15.512 -4.654  -8.288  0.60 12.61 ?  134 ALA   A CA   1 
ATOM   2958 C C    A ALA   A 1 134 ? 14.253 -5.024  -7.635  0.40 12.81 ?  134 ALA   A C    1 
ATOM   2959 C C    B ALA   A 1 134 ? 14.194 -4.862  -7.541  0.60 12.76 ?  134 ALA   A C    1 
ATOM   2960 O O    A ALA   A 1 134 ? 13.656 -4.274  -6.858  0.40 13.48 ?  134 ALA   A O    1 
ATOM   2961 O O    B ALA   A 1 134 ? 13.760 -4.033  -6.736  0.60 13.45 ?  134 ALA   A O    1 
ATOM   2962 C CB   A ALA   A 1 134 ? 16.712 -5.519  -7.559  0.40 13.24 ?  134 ALA   A CB   1 
ATOM   2963 C CB   B ALA   A 1 134 ? 16.585 -5.609  -7.769  0.60 13.56 ?  134 ALA   A CB   1 
ATOM   2964 H H    A ALA   A 1 134 ? 16.303 -3.048  -7.290  0.40 14.72 ?  134 ALA   A H    1 
ATOM   2965 H H    B ALA   A 1 134 ? 16.530 -3.116  -7.553  0.60 14.38 ?  134 ALA   A H    1 
ATOM   2966 H HA   A ALA   A 1 134 ? 15.613 -4.861  -9.157  0.40 15.29 ?  134 ALA   A HA   1 
ATOM   2967 H HA   B ALA   A 1 134 ? 15.361 -4.856  -9.223  0.60 15.11 ?  134 ALA   A HA   1 
ATOM   2968 H HB1  A ALA   A 1 134 ? 16.515 -6.456  -7.721  0.40 15.87 ?  134 ALA   A HB1  1 
ATOM   2969 H HB1  B ALA   A 1 134 ? 16.265 -6.519  -7.865  0.60 16.24 ?  134 ALA   A HB1  1 
ATOM   2970 H HB2  A ALA   A 1 134 ? 17.570 -5.291  -7.955  0.40 15.87 ?  134 ALA   A HB2  1 
ATOM   2971 H HB2  B ALA   A 1 134 ? 17.396 -5.487  -8.291  0.60 16.24 ?  134 ALA   A HB2  1 
ATOM   2972 H HB3  A ALA   A 1 134 ? 16.730 -5.343  -6.608  0.40 15.87 ?  134 ALA   A HB3  1 
ATOM   2973 H HB3  B ALA   A 1 134 ? 16.760 -5.413  -6.837  0.60 16.24 ?  134 ALA   A HB3  1 
ATOM   2974 N N    A ASP   A 1 135 ? 13.756 -6.187  -8.041  0.40 12.98 ?  135 ASP   A N    1 
ATOM   2975 N N    B ASP   A 1 135 ? 13.561 -6.000  -7.821  0.60 13.75 ?  135 ASP   A N    1 
ATOM   2976 C CA   A ASP   A 1 135 ? 12.503 -6.709  -7.500  0.40 13.13 ?  135 ASP   A CA   1 
ATOM   2977 C CA   B ASP   A 1 135 ? 12.301 -6.366  -7.182  0.60 14.05 ?  135 ASP   A CA   1 
ATOM   2978 C C    A ASP   A 1 135 ? 12.741 -7.158  -6.064  0.40 12.92 ?  135 ASP   A C    1 
ATOM   2979 C C    B ASP   A 1 135 ? 12.573 -6.855  -5.763  0.60 13.19 ?  135 ASP   A C    1 
ATOM   2980 O O    A ASP   A 1 135 ? 13.555 -8.062  -5.838  0.40 13.04 ?  135 ASP   A O    1 
ATOM   2981 O O    B ASP   A 1 135 ? 13.329 -7.818  -5.586  0.60 13.05 ?  135 ASP   A O    1 
ATOM   2982 C CB   A ASP   A 1 135 ? 12.049 -7.897  -8.345  0.40 13.99 ?  135 ASP   A CB   1 
ATOM   2983 C CB   B ASP   A 1 135 ? 11.639 -7.477  -7.989  0.60 15.58 ?  135 ASP   A CB   1 
ATOM   2984 C CG   A ASP   A 1 135 ? 10.753 -8.536  -7.846  0.40 15.27 ?  135 ASP   A CG   1 
ATOM   2985 C CG   B ASP   A 1 135 ? 10.252 -7.851  -7.476  0.60 17.96 ?  135 ASP   A CG   1 
ATOM   2986 O OD1  A ASP   A 1 135 ? 10.207 -8.117  -6.805  0.40 14.80 ?  135 ASP   A OD1  1 
ATOM   2987 O OD1  B ASP   A 1 135 ? 9.875  -7.428  -6.360  0.60 18.56 ?  135 ASP   A OD1  1 
ATOM   2988 O OD2  A ASP   A 1 135 ? 10.282 -9.480  -8.510  0.40 17.21 -1 135 ASP   A OD2  1 
ATOM   2989 O OD2  B ASP   A 1 135 ? 9.539  -8.584  -8.197  0.60 19.85 -1 135 ASP   A OD2  1 
ATOM   2990 H H    A ASP   A 1 135 ? 14.123 -6.692  -8.632  0.40 15.55 ?  135 ASP   A H    1 
ATOM   2991 H H    B ASP   A 1 135 ? 13.842 -6.579  -8.387  0.60 16.48 ?  135 ASP   A H    1 
ATOM   2992 H HA   A ASP   A 1 135 ? 11.822 -6.020  -7.526  0.40 15.73 ?  135 ASP   A HA   1 
ATOM   2993 H HA   B ASP   A 1 135 ? 11.711 -5.592  -7.170  0.60 16.84 ?  135 ASP   A HA   1 
ATOM   2994 H HB2  A ASP   A 1 135 ? 11.894 -7.597  -9.249  0.40 16.76 ?  135 ASP   A HB2  1 
ATOM   2995 H HB2  B ASP   A 1 135 ? 11.584 -7.193  -8.917  0.60 18.67 ?  135 ASP   A HB2  1 
ATOM   2996 H HB3  A ASP   A 1 135 ? 12.743 -8.575  -8.330  0.40 16.76 ?  135 ASP   A HB3  1 
ATOM   2997 H HB3  B ASP   A 1 135 ? 12.175 -8.274  -7.916  0.60 18.67 ?  135 ASP   A HB3  1 
ATOM   2998 N N    A PRO   A 1 136 ? 12.076 -6.564  -5.071  0.40 13.14 ?  136 PRO   A N    1 
ATOM   2999 N N    B PRO   A 1 136 ? 11.997 -6.226  -4.734  0.60 13.29 ?  136 PRO   A N    1 
ATOM   3000 C CA   A PRO   A 1 136 ? 12.330 -6.978  -3.680  0.40 13.24 ?  136 PRO   A CA   1 
ATOM   3001 C CA   B PRO   A 1 136 ? 12.262 -6.673  -3.354  0.60 13.60 ?  136 PRO   A CA   1 
ATOM   3002 C C    A PRO   A 1 136 ? 11.900 -8.404  -3.378  0.40 12.78 ?  136 PRO   A C    1 
ATOM   3003 C C    B PRO   A 1 136 ? 11.858 -8.118  -3.080  0.60 13.00 ?  136 PRO   A C    1 
ATOM   3004 O O    A PRO   A 1 136 ? 12.526 -9.059  -2.537  0.40 12.80 ?  136 PRO   A O    1 
ATOM   3005 O O    B PRO   A 1 136 ? 12.466 -8.769  -2.220  0.60 12.40 ?  136 PRO   A O    1 
ATOM   3006 C CB   A PRO   A 1 136 ? 11.549 -5.948  -2.852  0.40 14.15 ?  136 PRO   A CB   1 
ATOM   3007 C CB   B PRO   A 1 136 ? 11.460 -5.669  -2.507  0.60 14.76 ?  136 PRO   A CB   1 
ATOM   3008 C CG   A PRO   A 1 136 ? 10.511 -5.415  -3.782  0.40 14.89 ?  136 PRO   A CG   1 
ATOM   3009 C CG   B PRO   A 1 136 ? 10.418 -5.119  -3.446  0.60 15.64 ?  136 PRO   A CG   1 
ATOM   3010 C CD   A PRO   A 1 136 ? 11.094 -5.470  -5.159  0.40 13.90 ?  136 PRO   A CD   1 
ATOM   3011 C CD   B PRO   A 1 136 ? 11.125 -5.039  -4.761  0.60 14.26 ?  136 PRO   A CD   1 
ATOM   3012 H HA   A PRO   A 1 136 ? 13.275 -6.890  -3.473  0.40 15.86 ?  136 PRO   A HA   1 
ATOM   3013 H HA   B PRO   A 1 136 ? 13.206 -6.561  -3.144  0.60 16.30 ?  136 PRO   A HA   1 
ATOM   3014 H HB2  A PRO   A 1 136 ? 11.135 -6.386  -2.090  0.40 16.96 ?  136 PRO   A HB2  1 
ATOM   3015 H HB2  B PRO   A 1 136 ? 11.043 -6.122  -1.761  0.60 17.69 ?  136 PRO   A HB2  1 
ATOM   3016 H HB3  A PRO   A 1 136 ? 12.148 -5.243  -2.558  0.40 16.96 ?  136 PRO   A HB3  1 
ATOM   3017 H HB3  B PRO   A 1 136 ? 12.042 -4.954  -2.194  0.60 17.69 ?  136 PRO   A HB3  1 
ATOM   3018 H HG2  A PRO   A 1 136 ? 9.718  -5.965  -3.729  0.40 17.84 ?  136 PRO   A HG2  1 
ATOM   3019 H HG2  B PRO   A 1 136 ? 9.666  -5.732  -3.499  0.60 18.74 ?  136 PRO   A HG2  1 
ATOM   3020 H HG3  A PRO   A 1 136 ? 10.307 -4.497  -3.541  0.40 17.84 ?  136 PRO   A HG3  1 
ATOM   3021 H HG3  B PRO   A 1 136 ? 10.131 -4.241  -3.154  0.60 18.74 ?  136 PRO   A HG3  1 
ATOM   3022 H HD2  A PRO   A 1 136 ? 10.406 -5.692  -5.808  0.40 16.65 ?  136 PRO   A HD2  1 
ATOM   3023 H HD2  B PRO   A 1 136 ? 10.487 -5.100  -5.491  0.60 17.08 ?  136 PRO   A HD2  1 
ATOM   3024 H HD3  A PRO   A 1 136 ? 11.534 -4.634  -5.380  0.40 16.65 ?  136 PRO   A HD3  1 
ATOM   3025 H HD3  B PRO   A 1 136 ? 11.654 -4.224  -4.820  0.60 17.08 ?  136 PRO   A HD3  1 
ATOM   3026 N N    A ILE   A 1 137 ? 10.845 -8.907  -4.022  0.40 12.90 ?  137 ILE   A N    1 
ATOM   3027 N N    B ILE   A 1 137 ? 10.836 -8.636  -3.766  0.60 13.50 ?  137 ILE   A N    1 
ATOM   3028 C CA   A ILE   A 1 137 ? 10.496 -10.314 -3.858  0.40 13.36 ?  137 ILE   A CA   1 
ATOM   3029 C CA   B ILE   A 1 137 ? 10.458 -10.036 -3.583  0.60 14.00 ?  137 ILE   A CA   1 
ATOM   3030 C C    A ILE   A 1 137 ? 11.664 -11.189 -4.285  0.40 12.93 ?  137 ILE   A C    1 
ATOM   3031 C C    B ILE   A 1 137 ? 11.595 -10.955 -4.024  0.60 13.33 ?  137 ILE   A C    1 
ATOM   3032 O O    A ILE   A 1 137 ? 11.980 -12.196 -3.640  0.40 13.19 ?  137 ILE   A O    1 
ATOM   3033 O O    B ILE   A 1 137 ? 11.920 -11.940 -3.347  0.60 13.15 ?  137 ILE   A O    1 
ATOM   3034 C CB   A ILE   A 1 137 ? 9.204  -10.645 -4.630  0.40 14.44 ?  137 ILE   A CB   1 
ATOM   3035 C CB   B ILE   A 1 137 ? 9.140  -10.336 -4.326  0.60 15.37 ?  137 ILE   A CB   1 
ATOM   3036 C CG1  A ILE   A 1 137 ? 8.070  -9.718  -4.177  0.40 15.74 ?  137 ILE   A CG1  1 
ATOM   3037 C CG1  B ILE   A 1 137 ? 7.954  -9.640  -3.639  0.60 16.72 ?  137 ILE   A CG1  1 
ATOM   3038 C CG2  A ILE   A 1 137 ? 8.821  -12.104 -4.421  0.40 14.87 ?  137 ILE   A CG2  1 
ATOM   3039 C CG2  B ILE   A 1 137 ? 8.905  -11.836 -4.413  0.60 15.94 ?  137 ILE   A CG2  1 
ATOM   3040 C CD1  A ILE   A 1 137 ? 6.779  -9.910  -4.926  0.40 16.91 ?  137 ILE   A CD1  1 
ATOM   3041 C CD1  B ILE   A 1 137 ? 6.651  -9.741  -4.404  0.60 18.02 ?  137 ILE   A CD1  1 
ATOM   3042 H H    A ILE   A 1 137 ? 10.335 -8.467  -4.550  0.40 15.46 ?  137 ILE   A H    1 
ATOM   3043 H H    B ILE   A 1 137 ? 10.356 -8.192  -4.327  0.60 16.18 ?  137 ILE   A H    1 
ATOM   3044 H HA   A ILE   A 1 137 ? 10.333 -10.495 -2.922  0.40 16.01 ?  137 ILE   A HA   1 
ATOM   3045 H HA   B ILE   A 1 137 ? 10.303 -10.183 -2.637  0.60 16.78 ?  137 ILE   A HA   1 
ATOM   3046 H HB   A ILE   A 1 137 ? 9.361  -10.503 -5.575  0.40 17.30 ?  137 ILE   A HB   1 
ATOM   3047 H HB   B ILE   A 1 137 ? 9.213  -9.980  -5.225  0.60 18.42 ?  137 ILE   A HB   1 
ATOM   3048 H HG12 A ILE   A 1 137 ? 7.899  -9.875  -3.235  0.40 18.86 ?  137 ILE   A HG12 1 
ATOM   3049 H HG12 B ILE   A 1 137 ? 7.817  -10.045 -2.769  0.60 20.04 ?  137 ILE   A HG12 1 
ATOM   3050 H HG13 A ILE   A 1 137 ? 8.349  -8.796  -4.307  0.40 18.86 ?  137 ILE   A HG13 1 
ATOM   3051 H HG13 B ILE   A 1 137 ? 8.160  -8.697  -3.532  0.60 20.04 ?  137 ILE   A HG13 1 
ATOM   3052 H HG21 A ILE   A 1 137 ? 7.978  -12.283 -4.867  0.40 17.82 ?  137 ILE   A HG21 1 
ATOM   3053 H HG21 B ILE   A 1 137 ? 7.996  -12.001 -4.706  0.60 19.10 ?  137 ILE   A HG21 1 
ATOM   3054 H HG22 A ILE   A 1 137 ? 9.512  -12.671 -4.794  0.40 17.82 ?  137 ILE   A HG22 1 
ATOM   3055 H HG22 B ILE   A 1 137 ? 9.526  -12.216 -5.052  0.60 19.10 ?  137 ILE   A HG22 1 
ATOM   3056 H HG23 A ILE   A 1 137 ? 8.731  -12.271 -3.470  0.40 17.82 ?  137 ILE   A HG23 1 
ATOM   3057 H HG23 B ILE   A 1 137 ? 9.044  -12.227 -3.537  0.60 19.10 ?  137 ILE   A HG23 1 
ATOM   3058 H HD11 A ILE   A 1 137 ? 6.116  -10.277 -4.321  0.40 20.27 ?  137 ILE   A HD11 1 
ATOM   3059 H HD11 B ILE   A 1 137 ? 6.025  -9.096  -4.045  0.60 21.60 ?  137 ILE   A HD11 1 
ATOM   3060 H HD12 A ILE   A 1 137 ? 6.486  -9.048  -5.258  0.40 20.27 ?  137 ILE   A HD12 1 
ATOM   3061 H HD12 B ILE   A 1 137 ? 6.820  -9.554  -5.341  0.60 21.60 ?  137 ILE   A HD12 1 
ATOM   3062 H HD13 A ILE   A 1 137 ? 6.928  -10.514 -5.667  0.40 20.27 ?  137 ILE   A HD13 1 
ATOM   3063 H HD13 B ILE   A 1 137 ? 6.294  -10.638 -4.307  0.60 21.60 ?  137 ILE   A HD13 1 
ATOM   3064 N N    A HIS   A 1 138 ? 12.331 -10.810 -5.374  0.40 12.82 ?  138 HIS   A N    1 
ATOM   3065 N N    B HIS   A 1 138 ? 12.221 -10.640 -5.162  0.60 13.92 ?  138 HIS   A N    1 
ATOM   3066 C CA   A HIS   A 1 138 ? 13.534 -11.523 -5.780  0.40 12.73 ?  138 HIS   A CA   1 
ATOM   3067 C CA   B HIS   A 1 138 ? 13.350 -11.431 -5.644  0.60 13.85 ?  138 HIS   A CA   1 
ATOM   3068 C C    A HIS   A 1 138 ? 14.660 -11.345 -4.766  0.40 12.31 ?  138 HIS   A C    1 
ATOM   3069 C C    B HIS   A 1 138 ? 14.533 -11.342 -4.690  0.60 12.95 ?  138 HIS   A C    1 
ATOM   3070 O O    A HIS   A 1 138 ? 15.384 -12.302 -4.471  0.40 12.28 ?  138 HIS   A O    1 
ATOM   3071 O O    B HIS   A 1 138 ? 15.172 -12.352 -4.379  0.60 13.27 ?  138 HIS   A O    1 
ATOM   3072 C CB   A HIS   A 1 138 ? 13.971 -11.076 -7.171  0.40 13.50 ?  138 HIS   A CB   1 
ATOM   3073 C CB   B HIS   A 1 138 ? 13.750 -10.958 -7.042  0.60 14.33 ?  138 HIS   A CB   1 
ATOM   3074 C CG   A HIS   A 1 138 ? 15.204 -11.769 -7.654  0.40 14.24 ?  138 HIS   A CG   1 
ATOM   3075 C CG   B HIS   A 1 138 ? 15.031 -11.554 -7.535  0.60 15.01 ?  138 HIS   A CG   1 
ATOM   3076 N ND1  A HIS   A 1 138 ? 15.264 -13.133 -7.850  0.40 15.31 ?  138 HIS   A ND1  1 
ATOM   3077 N ND1  B HIS   A 1 138 ? 15.158 -12.889 -7.854  0.60 16.23 ?  138 HIS   A ND1  1 
ATOM   3078 C CD2  A HIS   A 1 138 ? 16.433 -11.290 -7.956  0.40 14.48 ?  138 HIS   A CD2  1 
ATOM   3079 C CD2  B HIS   A 1 138 ? 16.246 -10.997 -7.755  0.60 15.01 ?  138 HIS   A CD2  1 
ATOM   3080 C CE1  A HIS   A 1 138 ? 16.474 -13.461 -8.264  0.40 15.53 ?  138 HIS   A CE1  1 
ATOM   3081 C CE1  B HIS   A 1 138 ? 16.396 -13.127 -8.252  0.60 16.05 ?  138 HIS   A CE1  1 
ATOM   3082 N NE2  A HIS   A 1 138 ? 17.203 -12.362 -8.336  0.40 14.84 ?  138 HIS   A NE2  1 
ATOM   3083 N NE2  B HIS   A 1 138 ? 17.078 -11.997 -8.200  0.60 15.33 ?  138 HIS   A NE2  1 
ATOM   3084 H H    A HIS   A 1 138 ? 12.106 -10.154 -5.889  0.40 15.36 ?  138 HIS   A H    1 
ATOM   3085 H H    B HIS   A 1 138 ? 12.013 -9.967  -5.662  0.60 16.67 ?  138 HIS   A H    1 
ATOM   3086 H HA   A HIS   A 1 138 ? 13.324 -12.467 -5.832  0.40 15.25 ?  138 HIS   A HA   1 
ATOM   3087 H HA   B HIS   A 1 138 ? 13.077 -12.355 -5.702  0.60 16.59 ?  138 HIS   A HA   1 
ATOM   3088 H HB2  A HIS   A 1 138 ? 13.255 -11.265 -7.802  0.40 16.17 ?  138 HIS   A HB2  1 
ATOM   3089 H HB2  B HIS   A 1 138 ? 13.045 -11.202 -7.666  0.60 17.17 ?  138 HIS   A HB2  1 
ATOM   3090 H HB3  A HIS   A 1 138 ? 14.149 -10.123 -7.155  0.40 16.17 ?  138 HIS   A HB3  1 
ATOM   3091 H HB3  B HIS   A 1 138 ? 13.853 -9.992  -7.030  0.60 17.17 ?  138 HIS   A HB3  1 
ATOM   3092 H HD1  A HIS   A 1 138 ? 14.611 -13.682 -7.727  0.40 18.35 ?  138 HIS   A HD1  1 
ATOM   3093 H HD1  B HIS   A 1 138 ? 14.529 -13.473 -7.801  0.60 19.45 ?  138 HIS   A HD1  1 
ATOM   3094 H HD2  A HIS   A 1 138 ? 16.699 -10.400 -7.916  0.40 17.35 ?  138 HIS   A HD2  1 
ATOM   3095 H HD2  B HIS   A 1 138 ? 16.473 -10.105 -7.628  0.60 17.99 ?  138 HIS   A HD2  1 
ATOM   3096 H HE1  A HIS   A 1 138 ? 16.762 -14.319 -8.468  0.40 18.61 ?  138 HIS   A HE1  1 
ATOM   3097 H HE1  B HIS   A 1 138 ? 16.729 -13.953 -8.522  0.60 19.24 ?  138 HIS   A HE1  1 
ATOM   3098 N N    . SER   A 1 139 ? 14.833 -10.136 -4.218  1.00 12.58 ?  139 SER   A N    1 
ATOM   3099 C CA   . SER   A 1 139 ? 15.914 -9.949  -3.260  1.00 12.27 ?  139 SER   A CA   1 
ATOM   3100 C C    . SER   A 1 139 ? 15.708 -10.810 -2.018  1.00 11.79 ?  139 SER   A C    1 
ATOM   3101 O O    . SER   A 1 139 ? 16.661 -11.407 -1.506  1.00 11.62 ?  139 SER   A O    1 
ATOM   3102 C CB   . SER   A 1 139 ? 16.042 -8.472  -2.893  1.00 12.50 ?  139 SER   A CB   1 
ATOM   3103 O OG   . SER   A 1 139 ? 17.131 -8.311  -2.002  1.00 12.52 ?  139 SER   A OG   1 
ATOM   3104 H H    A SER   A 1 139 ? 14.361 -9.437  -4.380  0.40 15.07 ?  139 SER   A H    1 
ATOM   3105 H H    B SER   A 1 139 ? 14.419 -9.412  -4.427  0.60 15.07 ?  139 SER   A H    1 
ATOM   3106 H HA   . SER   A 1 139 ? 16.750 -10.219 -3.670  1.00 14.69 ?  139 SER   A HA   1 
ATOM   3107 H HB2  . SER   A 1 139 ? 16.201 -7.946  -3.693  1.00 14.97 ?  139 SER   A HB2  1 
ATOM   3108 H HB3  . SER   A 1 139 ? 15.230 -8.172  -2.450  1.00 14.97 ?  139 SER   A HB3  1 
ATOM   3109 H HG   . SER   A 1 139 ? 17.222 -7.498  -1.792  1.00 15.00 ?  139 SER   A HG   1 
ATOM   3110 N N    . LEU   A 1 140 ? 14.475 -10.879 -1.513  1.00 12.17 ?  140 LEU   A N    1 
ATOM   3111 C CA   . LEU   A 1 140 ? 14.210 -11.711 -0.343  1.00 12.18 ?  140 LEU   A CA   1 
ATOM   3112 C C    . LEU   A 1 140 ? 14.473 -13.183 -0.646  1.00 12.38 ?  140 LEU   A C    1 
ATOM   3113 O O    . LEU   A 1 140 ? 15.030 -13.911 0.186   1.00 12.62 ?  140 LEU   A O    1 
ATOM   3114 C CB   . LEU   A 1 140 ? 12.776 -11.485 0.137   1.00 12.71 ?  140 LEU   A CB   1 
ATOM   3115 C CG   . LEU   A 1 140 ? 12.326 -12.371 1.296   1.00 13.36 ?  140 LEU   A CG   1 
ATOM   3116 C CD1  . LEU   A 1 140 ? 13.224 -12.196 2.505   1.00 13.76 ?  140 LEU   A CD1  1 
ATOM   3117 C CD2  . LEU   A 1 140 ? 10.871 -12.076 1.663   1.00 14.17 ?  140 LEU   A CD2  1 
ATOM   3118 H H    . LEU   A 1 140 ? 13.792 -10.460 -1.824  1.00 14.58 ?  140 LEU   A H    1 
ATOM   3119 H HA   . LEU   A 1 140 ? 14.808 -11.447 0.371   1.00 14.59 ?  140 LEU   A HA   1 
ATOM   3120 H HB2  . LEU   A 1 140 ? 12.693 -10.568 0.433   1.00 15.23 ?  140 LEU   A HB2  1 
ATOM   3121 H HB3  . LEU   A 1 140 ? 12.175 -11.648 -0.603  1.00 15.23 ?  140 LEU   A HB3  1 
ATOM   3122 H HG   . LEU   A 1 140 ? 12.368 -13.306 1.023   1.00 16.00 ?  140 LEU   A HG   1 
ATOM   3123 H HD11 . LEU   A 1 140 ? 12.846 -12.690 3.250   1.00 16.49 ?  140 LEU   A HD11 1 
ATOM   3124 H HD12 . LEU   A 1 140 ? 14.103 -12.541 2.291   1.00 16.49 ?  140 LEU   A HD12 1 
ATOM   3125 H HD13 . LEU   A 1 140 ? 13.273 -11.255 2.719   1.00 16.49 ?  140 LEU   A HD13 1 
ATOM   3126 H HD21 . LEU   A 1 140 ? 10.607 -12.660 2.398   1.00 16.98 ?  140 LEU   A HD21 1 
ATOM   3127 H HD22 . LEU   A 1 140 ? 10.796 -11.153 1.933   1.00 16.98 ?  140 LEU   A HD22 1 
ATOM   3128 H HD23 . LEU   A 1 140 ? 10.308 -12.250 0.893   1.00 16.98 ?  140 LEU   A HD23 1 
ATOM   3129 N N    . ARG   A 1 141 ? 14.072 -13.638 -1.836  1.00 12.58 ?  141 ARG   A N    1 
ATOM   3130 C CA   . ARG   A 1 141 ? 14.309 -15.025 -2.225  1.00 13.63 ?  141 ARG   A CA   1 
ATOM   3131 C C    . ARG   A 1 141 ? 15.803 -15.333 -2.251  1.00 12.64 ?  141 ARG   A C    1 
ATOM   3132 O O    . ARG   A 1 141 ? 16.251 -16.357 -1.719  1.00 12.48 ?  141 ARG   A O    1 
ATOM   3133 C CB   . ARG   A 1 141 ? 13.679 -15.254 -3.600  1.00 15.70 ?  141 ARG   A CB   1 
ATOM   3134 C CG   . ARG   A 1 141 ? 13.676 -16.681 -4.089  1.00 18.54 ?  141 ARG   A CG   1 
ATOM   3135 C CD   . ARG   A 1 141 ? 12.657 -17.493 -3.340  1.00 20.59 ?  141 ARG   A CD   1 
ATOM   3136 N NE   . ARG   A 1 141 ? 13.280 -18.284 -2.292  1.00 21.13 ?  141 ARG   A NE   1 
ATOM   3137 C CZ   . ARG   A 1 141 ? 12.603 -18.888 -1.324  1.00 21.91 ?  141 ARG   A CZ   1 
ATOM   3138 N NH1  . ARG   A 1 141 ? 11.305 -18.696 -1.164  1.00 22.33 ?  141 ARG   A NH1  1 
ATOM   3139 N NH2  . ARG   A 1 141 ? 13.248 -19.691 -0.484  1.00 22.42 ?  141 ARG   A NH2  1 
ATOM   3140 H H    . ARG   A 1 141 ? 13.668 -13.166 -2.433  1.00 15.07 ?  141 ARG   A H    1 
ATOM   3141 H HA   . ARG   A 1 141 ? 13.886 -15.619 -1.589  1.00 16.33 ?  141 ARG   A HA   1 
ATOM   3142 H HB2  . ARG   A 1 141 ? 12.758 -14.948 -3.571  1.00 18.81 ?  141 ARG   A HB2  1 
ATOM   3143 H HB3  . ARG   A 1 141 ? 14.169 -14.727 -4.251  1.00 18.81 ?  141 ARG   A HB3  1 
ATOM   3144 H HG2  . ARG   A 1 141 ? 13.446 -16.700 -5.035  1.00 22.22 ?  141 ARG   A HG2  1 
ATOM   3145 H HG3  . ARG   A 1 141 ? 14.549 -17.080 -3.950  1.00 22.22 ?  141 ARG   A HG3  1 
ATOM   3146 H HD2  . ARG   A 1 141 ? 12.015 -16.899 -2.920  1.00 24.68 ?  141 ARG   A HD2  1 
ATOM   3147 H HD3  . ARG   A 1 141 ? 12.201 -18.089 -3.959  1.00 24.68 ?  141 ARG   A HD3  1 
ATOM   3148 H HE   . ARG   A 1 141 ? 14.112 -18.478 -2.378  1.00 25.33 ?  141 ARG   A HE   1 
ATOM   3149 H HH11 . ARG   A 1 141 ? 10.869 -18.194 -1.709  1.00 26.78 ?  141 ARG   A HH11 1 
ATOM   3150 H HH12 . ARG   A 1 141 ? 10.886 -19.097 -0.526  1.00 26.78 ?  141 ARG   A HH12 1 
ATOM   3151 H HH21 . ARG   A 1 141 ? 14.096 -19.818 -0.575  1.00 26.88 ?  141 ARG   A HH21 1 
ATOM   3152 H HH22 . ARG   A 1 141 ? 12.825 -20.075 0.159   1.00 26.88 ?  141 ARG   A HH22 1 
ATOM   3153 N N    . VAL   A 1 142 ? 16.593 -14.454 -2.873  1.00 12.02 ?  142 VAL   A N    1 
ATOM   3154 C CA   . VAL   A 1 142 ? 18.036 -14.672 -2.922  1.00 11.77 ?  142 VAL   A CA   1 
ATOM   3155 C C    . VAL   A 1 142 ? 18.619 -14.671 -1.518  1.00 10.95 ?  142 VAL   A C    1 
ATOM   3156 O O    . VAL   A 1 142 ? 19.482 -15.492 -1.189  1.00 11.50 ?  142 VAL   A O    1 
ATOM   3157 C CB   . VAL   A 1 142 ? 18.726 -13.646 -3.843  1.00 12.28 ?  142 VAL   A CB   1 
ATOM   3158 C CG1  . VAL   A 1 142 ? 20.234 -13.847 -3.805  1.00 12.25 ?  142 VAL   A CG1  1 
ATOM   3159 C CG2  . VAL   A 1 142 ? 18.222 -13.787 -5.268  1.00 13.48 ?  142 VAL   A CG2  1 
ATOM   3160 H H    . VAL   A 1 142 ? 16.326 -13.729 -3.265  1.00 14.40 ?  142 VAL   A H    1 
ATOM   3161 H HA   . VAL   A 1 142 ? 18.198 -15.545 -3.304  1.00 14.09 ?  142 VAL   A HA   1 
ATOM   3162 H HB   . VAL   A 1 142 ? 18.534 -12.744 -3.535  1.00 14.71 ?  142 VAL   A HB   1 
ATOM   3163 H HG11 . VAL   A 1 142 ? 20.639 -13.352 -4.536  1.00 14.67 ?  142 VAL   A HG11 1 
ATOM   3164 H HG12 . VAL   A 1 142 ? 20.582 -13.515 -2.958  1.00 14.67 ?  142 VAL   A HG12 1 
ATOM   3165 H HG13 . VAL   A 1 142 ? 20.431 -14.790 -3.896  1.00 14.67 ?  142 VAL   A HG13 1 
ATOM   3166 H HG21 . VAL   A 1 142 ? 18.678 -13.140 -5.829  1.00 16.15 ?  142 VAL   A HG21 1 
ATOM   3167 H HG22 . VAL   A 1 142 ? 18.419 -14.687 -5.577  1.00 16.15 ?  142 VAL   A HG22 1 
ATOM   3168 H HG23 . VAL   A 1 142 ? 17.270 -13.631 -5.280  1.00 16.15 ?  142 VAL   A HG23 1 
ATOM   3169 N N    . CYS   A 1 143 ? 18.161 -13.756 -0.667  1.00 11.01 ?  143 CYS   A N    1 
ATOM   3170 C CA   . CYS   A 1 143 ? 18.635 -13.724 0.711   1.00 11.12 ?  143 CYS   A CA   1 
ATOM   3171 C C    . CYS   A 1 143 ? 18.410 -15.069 1.389   1.00 11.14 ?  143 CYS   A C    1 
ATOM   3172 O O    . CYS   A 1 143 ? 19.335 -15.661 1.954   1.00 11.27 ?  143 CYS   A O    1 
ATOM   3173 C CB   . CYS   A 1 143 ? 17.906 -12.622 1.470   1.00 11.75 ?  143 CYS   A CB   1 
ATOM   3174 S SG   . CYS   A 1 143 ? 18.411 -12.454 3.184   1.00 12.10 ?  143 CYS   A SG   1 
ATOM   3175 H H    . CYS   A 1 143 ? 17.584 -13.158 -0.864  1.00 13.18 ?  143 CYS   A H    1 
ATOM   3176 H HA   . CYS   A 1 143 ? 19.586 -13.538 0.721   1.00 13.32 ?  143 CYS   A HA   1 
ATOM   3177 H HB2  . CYS   A 1 143 ? 18.070 -11.779 1.021   1.00 14.07 ?  143 CYS   A HB2  1 
ATOM   3178 H HB3  . CYS   A 1 143 ? 16.960 -12.818 1.460   1.00 14.07 ?  143 CYS   A HB3  1 
ATOM   3179 H HG   . CYS   A 1 143 ? 17.872 -11.490 3.650   1.00 14.50 ?  143 CYS   A HG   1 
ATOM   3180 N N    . VAL   A 1 144 ? 17.178 -15.570 1.335   1.00 11.72 ?  144 VAL   A N    1 
ATOM   3181 C CA   . VAL   A 1 144 ? 16.849 -16.813 2.023   1.00 12.91 ?  144 VAL   A CA   1 
ATOM   3182 C C    . VAL   A 1 144 ? 17.664 -17.976 1.477   1.00 12.64 ?  144 VAL   A C    1 
ATOM   3183 O O    . VAL   A 1 144 ? 18.044 -18.887 2.224   1.00 13.36 ?  144 VAL   A O    1 
ATOM   3184 C CB   . VAL   A 1 144 ? 15.332 -17.061 1.920   1.00 15.36 ?  144 VAL   A CB   1 
ATOM   3185 C CG1  . VAL   A 1 144 ? 14.971 -18.499 2.257   1.00 16.80 ?  144 VAL   A CG1  1 
ATOM   3186 C CG2  . VAL   A 1 144 ? 14.589 -16.070 2.817   1.00 15.42 ?  144 VAL   A CG2  1 
ATOM   3187 H H    . VAL   A 1 144 ? 16.516 -15.208 0.910   1.00 14.04 ?  144 VAL   A H    1 
ATOM   3188 H HA   . VAL   A 1 144 ? 17.063 -16.719 2.957   1.00 15.46 ?  144 VAL   A HA   1 
ATOM   3189 H HB   . VAL   A 1 144 ? 15.043 -16.894 1.006   1.00 18.41 ?  144 VAL   A HB   1 
ATOM   3190 H HG11 . VAL   A 1 144 ? 14.019 -18.550 2.455   1.00 20.14 ?  144 VAL   A HG11 1 
ATOM   3191 H HG12 . VAL   A 1 144 ? 15.178 -19.066 1.499   1.00 20.14 ?  144 VAL   A HG12 1 
ATOM   3192 H HG13 . VAL   A 1 144 ? 15.480 -18.776 3.033   1.00 20.14 ?  144 VAL   A HG13 1 
ATOM   3193 H HG21 . VAL   A 1 144 ? 13.632 -16.218 2.739   1.00 18.48 ?  144 VAL   A HG21 1 
ATOM   3194 H HG22 . VAL   A 1 144 ? 14.869 -16.202 3.736   1.00 18.48 ?  144 VAL   A HG22 1 
ATOM   3195 H HG23 . VAL   A 1 144 ? 14.803 -15.164 2.535   1.00 18.48 ?  144 VAL   A HG23 1 
ATOM   3196 N N    . ASP   A 1 145 ? 17.914 -17.988 0.169   1.00 12.74 ?  145 ASP   A N    1 
ATOM   3197 C CA   . ASP   A 1 145 ? 18.626 -19.084 -0.479  1.00 13.76 ?  145 ASP   A CA   1 
ATOM   3198 C C    . ASP   A 1 145 ? 20.147 -18.935 -0.448  1.00 13.26 ?  145 ASP   A C    1 
ATOM   3199 O O    . ASP   A 1 145 ? 20.850 -19.820 -0.953  1.00 15.46 ?  145 ASP   A O    1 
ATOM   3200 C CB   . ASP   A 1 145 ? 18.166 -19.210 -1.932  1.00 15.45 ?  145 ASP   A CB   1 
ATOM   3201 C CG   . ASP   A 1 145 ? 16.712 -19.638 -2.050  1.00 17.38 ?  145 ASP   A CG   1 
ATOM   3202 O OD1  . ASP   A 1 145 ? 16.158 -20.190 -1.075  1.00 17.88 ?  145 ASP   A OD1  1 
ATOM   3203 O OD2  . ASP   A 1 145 ? 16.121 -19.409 -3.123  1.00 18.83 -1 145 ASP   A OD2  1 
ATOM   3204 H H    . ASP   A 1 145 ? 17.664 -17.368 -0.375  1.00 15.26 ?  145 ASP   A H    1 
ATOM   3205 H HA   . ASP   A 1 145 ? 18.399 -19.912 -0.027  1.00 16.49 ?  145 ASP   A HA   1 
ATOM   3206 H HB2  . ASP   A 1 145 ? 18.268 -18.353 -2.375  1.00 18.51 ?  145 ASP   A HB2  1 
ATOM   3207 H HB3  . ASP   A 1 145 ? 18.704 -19.882 -2.379  1.00 18.51 ?  145 ASP   A HB3  1 
ATOM   3208 N N    . THR   A 1 146 ? 20.672 -17.851 0.119   1.00 11.68 ?  146 THR   A N    1 
ATOM   3209 C CA   . THR   A 1 146 ? 22.113 -17.599 0.138   1.00 10.84 ?  146 THR   A CA   1 
ATOM   3210 C C    . THR   A 1 146 ? 22.676 -17.426 1.536   1.00 10.51 ?  146 THR   A C    1 
ATOM   3211 O O    . THR   A 1 146 ? 23.755 -17.953 1.835   1.00 11.57 ?  146 THR   A O    1 
ATOM   3212 C CB   . THR   A 1 146 ? 22.436 -16.338 -0.688  1.00 10.67 ?  146 THR   A CB   1 
ATOM   3213 O OG1  . THR   A 1 146 ? 21.900 -16.478 -2.006  1.00 11.29 ?  146 THR   A OG1  1 
ATOM   3214 C CG2  . THR   A 1 146 ? 23.936 -16.098 -0.767  1.00 11.30 ?  146 THR   A CG2  1 
ATOM   3215 H H    . THR   A 1 146 ? 20.206 -17.230 0.500   1.00 13.99 ?  146 THR   A H    1 
ATOM   3216 H HA   . THR   A 1 146 ? 22.568 -18.343 -0.272  1.00 12.99 ?  146 THR   A HA   1 
ATOM   3217 H HB   . THR   A 1 146 ? 22.035 -15.564 -0.261  1.00 12.78 ?  146 THR   A HB   1 
ATOM   3218 H HG1  . THR   A 1 146 ? 21.064 -16.552 -1.967  1.00 13.52 ?  146 THR   A HG1  1 
ATOM   3219 H HG21 . THR   A 1 146 ? 24.129 -15.429 -1.440  1.00 13.54 ?  146 THR   A HG21 1 
ATOM   3220 H HG22 . THR   A 1 146 ? 24.268 -15.781 0.092   1.00 13.54 ?  146 THR   A HG22 1 
ATOM   3221 H HG23 . THR   A 1 146 ? 24.392 -16.920 -0.996  1.00 13.54 ?  146 THR   A HG23 1 
ATOM   3222 N N    . VAL   A 1 147 ? 21.996 -16.663 2.384   1.00 10.53 ?  147 VAL   A N    1 
ATOM   3223 C CA   . VAL   A 1 147 ? 22.492 -16.376 3.720   1.00 10.53 ?  147 VAL   A CA   1 
ATOM   3224 C C    . VAL   A 1 147 ? 22.175 -17.553 4.628   1.00 10.84 ?  147 VAL   A C    1 
ATOM   3225 O O    . VAL   A 1 147 ? 21.033 -18.027 4.677   1.00 11.68 ?  147 VAL   A O    1 
ATOM   3226 C CB   . VAL   A 1 147 ? 21.878 -15.073 4.251   1.00 10.85 ?  147 VAL   A CB   1 
ATOM   3227 C CG1  . VAL   A 1 147 ? 22.421 -14.769 5.624   1.00 11.69 ?  147 VAL   A CG1  1 
ATOM   3228 C CG2  . VAL   A 1 147 ? 22.132 -13.922 3.285   1.00 11.11 ?  147 VAL   A CG2  1 
ATOM   3229 H H    . VAL   A 1 147 ? 21.228 -16.306 2.213   1.00 12.61 ?  147 VAL   A H    1 
ATOM   3230 H HA   . VAL   A 1 147 ? 23.456 -16.266 3.685   1.00 12.61 ?  147 VAL   A HA   1 
ATOM   3231 H HB   . VAL   A 1 147 ? 20.922 -15.188 4.332   1.00 12.99 ?  147 VAL   A HB   1 
ATOM   3232 H HG11 . VAL   A 1 147 ? 22.177 -13.863 5.867   1.00 14.00 ?  147 VAL   A HG11 1 
ATOM   3233 H HG12 . VAL   A 1 147 ? 22.036 -15.395 6.262   1.00 14.00 ?  147 VAL   A HG12 1 
ATOM   3234 H HG13 . VAL   A 1 147 ? 23.386 -14.861 5.613   1.00 14.00 ?  147 VAL   A HG13 1 
ATOM   3235 H HG21 . VAL   A 1 147 ? 21.807 -13.098 3.685   1.00 13.30 ?  147 VAL   A HG21 1 
ATOM   3236 H HG22 . VAL   A 1 147 ? 23.080 -13.855 3.110   1.00 13.30 ?  147 VAL   A HG22 1 
ATOM   3237 H HG23 . VAL   A 1 147 ? 21.651 -14.095 2.459   1.00 13.30 ?  147 VAL   A HG23 1 
ATOM   3238 N N    . ARG   A 1 148 ? 23.201 -18.029 5.334   1.00 10.98 ?  148 ARG   A N    1 
ATOM   3239 C CA   . ARG   A 1 148 ? 23.075 -19.114 6.291   1.00 11.26 ?  148 ARG   A CA   1 
ATOM   3240 C C    . ARG   A 1 148 ? 23.219 -18.651 7.730   1.00 11.67 ?  148 ARG   A C    1 
ATOM   3241 O O    . ARG   A 1 148 ? 22.817 -19.379 8.645   1.00 13.33 ?  148 ARG   A O    1 
ATOM   3242 C CB   . ARG   A 1 148 ? 24.107 -20.208 5.988   1.00 11.93 ?  148 ARG   A CB   1 
ATOM   3243 C CG   . ARG   A 1 148 ? 23.923 -20.836 4.613   1.00 12.87 ?  148 ARG   A CG   1 
ATOM   3244 C CD   . ARG   A 1 148 ? 24.995 -21.880 4.295   1.00 14.16 ?  148 ARG   A CD   1 
ATOM   3245 N NE   . ARG   A 1 148 ? 26.338 -21.309 4.307   1.00 14.26 ?  148 ARG   A NE   1 
ATOM   3246 C CZ   . ARG   A 1 148 ? 26.831 -20.553 3.336   1.00 13.49 ?  148 ARG   A CZ   1 
ATOM   3247 N NH1  . ARG   A 1 148 ? 26.140 -20.305 2.236   1.00 13.84 ?  148 ARG   A NH1  1 
ATOM   3248 N NH2  . ARG   A 1 148 ? 28.052 -20.030 3.472   1.00 13.87 ?  148 ARG   A NH2  1 
ATOM   3249 H H    . ARG   A 1 148 ? 24.011 -17.727 5.262   1.00 13.15 ?  148 ARG   A H    1 
ATOM   3250 H HA   . ARG   A 1 148 ? 22.196 -19.502 6.196   1.00 13.49 ?  148 ARG   A HA   1 
ATOM   3251 H HB2  . ARG   A 1 148 ? 24.995 -19.830 6.028   1.00 14.30 ?  148 ARG   A HB2  1 
ATOM   3252 H HB3  . ARG   A 1 148 ? 24.014 -20.916 6.648   1.00 14.30 ?  148 ARG   A HB3  1 
ATOM   3253 H HG2  . ARG   A 1 148 ? 23.054 -21.265 4.576   1.00 15.41 ?  148 ARG   A HG2  1 
ATOM   3254 H HG3  . ARG   A 1 148 ? 23.972 -20.133 3.942   1.00 15.41 ?  148 ARG   A HG3  1 
ATOM   3255 H HD2  . ARG   A 1 148 ? 24.959 -22.583 4.960   1.00 16.97 ?  148 ARG   A HD2  1 
ATOM   3256 H HD3  . ARG   A 1 148 ? 24.826 -22.247 3.411   1.00 16.97 ?  148 ARG   A HD3  1 
ATOM   3257 H HE   . ARG   A 1 148 ? 26.818 -21.427 5.007   1.00 17.08 ?  148 ARG   A HE   1 
ATOM   3258 H HH11 . ARG   A 1 148 ? 25.351 -20.628 2.135   1.00 16.58 ?  148 ARG   A HH11 1 
ATOM   3259 H HH12 . ARG   A 1 148 ? 26.477 -19.804 1.619   1.00 16.58 ?  148 ARG   A HH12 1 
ATOM   3260 H HH21 . ARG   A 1 148 ? 28.507 -20.179 4.183   1.00 16.62 ?  148 ARG   A HH21 1 
ATOM   3261 H HH22 . ARG   A 1 148 ? 28.380 -19.530 2.849   1.00 16.62 ?  148 ARG   A HH22 1 
ATOM   3262 N N    . THR   A 1 149 ? 23.787 -17.468 7.945   1.00 11.59 ?  149 THR   A N    1 
ATOM   3263 C CA   . THR   A 1 149 ? 23.877 -16.884 9.267   1.00 11.67 ?  149 THR   A CA   1 
ATOM   3264 C C    . THR   A 1 149 ? 22.552 -16.192 9.594   1.00 11.44 ?  149 THR   A C    1 
ATOM   3265 O O    . THR   A 1 149 ? 21.606 -16.194 8.799   1.00 12.17 ?  149 THR   A O    1 
ATOM   3266 C CB   . THR   A 1 149 ? 25.075 -15.942 9.319   1.00 12.36 ?  149 THR   A CB   1 
ATOM   3267 O OG1  . THR   A 1 149 ? 24.932 -14.995 8.256   1.00 12.35 ?  149 THR   A OG1  1 
ATOM   3268 C CG2  . THR   A 1 149 ? 26.387 -16.734 9.157   1.00 12.95 ?  149 THR   A CG2  1 
ATOM   3269 H H    . THR   A 1 149 ? 24.137 -16.975 7.327   1.00 13.89 ?  149 THR   A H    1 
ATOM   3270 H HA   . THR   A 1 149 ? 24.017 -17.593 9.914   1.00 13.97 ?  149 THR   A HA   1 
ATOM   3271 H HB   . THR   A 1 149 ? 25.090 -15.487 10.175  1.00 14.80 ?  149 THR   A HB   1 
ATOM   3272 H HG1  . THR   A 1 149 ? 25.583 -14.464 8.263   1.00 14.79 ?  149 THR   A HG1  1 
ATOM   3273 H HG21 . THR   A 1 149 ? 27.147 -16.139 9.216   1.00 15.52 ?  149 THR   A HG21 1 
ATOM   3274 H HG22 . THR   A 1 149 ? 26.461 -17.410 9.853   1.00 15.52 ?  149 THR   A HG22 1 
ATOM   3275 H HG23 . THR   A 1 149 ? 26.403 -17.181 8.292   1.00 15.52 ?  149 THR   A HG23 1 
ATOM   3276 N N    . ASN   A 1 150 ? 22.447 -15.648 10.800  1.00 11.87 ?  150 ASN   A N    1 
ATOM   3277 C CA   . ASN   A 1 150 ? 21.169 -15.161 11.316  1.00 12.61 ?  150 ASN   A CA   1 
ATOM   3278 C C    . ASN   A 1 150 ? 20.971 -13.716 10.880  1.00 11.99 ?  150 ASN   A C    1 
ATOM   3279 O O    . ASN   A 1 150 ? 21.691 -12.816 11.330  1.00 13.63 ?  150 ASN   A O    1 
ATOM   3280 C CB   . ASN   A 1 150 ? 21.145 -15.287 12.834  1.00 15.14 ?  150 ASN   A CB   1 
ATOM   3281 C CG   . ASN   A 1 150 ? 21.009 -16.715 13.285  1.00 19.84 ?  150 ASN   A CG   1 
ATOM   3282 O OD1  . ASN   A 1 150 ? 20.349 -17.514 12.627  1.00 21.70 ?  150 ASN   A OD1  1 
ATOM   3283 N ND2  . ASN   A 1 150 ? 21.651 -17.055 14.395  1.00 22.30 ?  150 ASN   A ND2  1 
ATOM   3284 H H    . ASN   A 1 150 ? 23.107 -15.548 11.344  1.00 14.22 ?  150 ASN   A H    1 
ATOM   3285 H HA   . ASN   A 1 150 ? 20.447 -15.699 10.953  1.00 15.11 ?  150 ASN   A HA   1 
ATOM   3286 H HB2  . ASN   A 1 150 ? 21.973 -14.937 13.197  1.00 18.14 ?  150 ASN   A HB2  1 
ATOM   3287 H HB3  . ASN   A 1 150 ? 20.391 -14.785 13.183  1.00 18.14 ?  150 ASN   A HB3  1 
ATOM   3288 H HD21 . ASN   A 1 150 ? 21.600 -17.862 14.695  1.00 26.73 ?  150 ASN   A HD21 1 
ATOM   3289 H HD22 . ASN   A 1 150 ? 22.113 -16.469 14.823  1.00 26.73 ?  150 ASN   A HD22 1 
ATOM   3290 N N    . VAL   A 1 151 ? 19.995 -13.490 10.008  1.00 11.55 ?  151 VAL   A N    1 
ATOM   3291 C CA   . VAL   A 1 151 ? 19.775 -12.175 9.426   1.00 11.82 ?  151 VAL   A CA   1 
ATOM   3292 C C    . VAL   A 1 151 ? 18.387 -11.668 9.797   1.00 11.91 ?  151 VAL   A C    1 
ATOM   3293 O O    . VAL   A 1 151 ? 17.383 -12.384 9.655   1.00 12.78 ?  151 VAL   A O    1 
ATOM   3294 C CB   . VAL   A 1 151 ? 20.052 -12.152 7.909   1.00 12.62 ?  151 VAL   A CB   1 
ATOM   3295 C CG1  . VAL   A 1 151 ? 19.213 -13.163 7.162   1.00 13.78 ?  151 VAL   A CG1  1 
ATOM   3296 C CG2  . VAL   A 1 151 ? 19.869 -10.740 7.351   1.00 13.03 ?  151 VAL   A CG2  1 
ATOM   3297 H H    . VAL   A 1 151 ? 19.441 -14.090 9.736   1.00 13.83 ?  151 VAL   A H    1 
ATOM   3298 H HA   . VAL   A 1 151 ? 20.414 -11.564 9.828   1.00 14.15 ?  151 VAL   A HA   1 
ATOM   3299 H HB   . VAL   A 1 151 ? 20.986 -12.391 7.767   1.00 15.12 ?  151 VAL   A HB   1 
ATOM   3300 H HG11 . VAL   A 1 151 ? 19.390 -13.082 6.211   1.00 16.51 ?  151 VAL   A HG11 1 
ATOM   3301 H HG12 . VAL   A 1 151 ? 19.448 -14.053 7.467   1.00 16.51 ?  151 VAL   A HG12 1 
ATOM   3302 H HG13 . VAL   A 1 151 ? 18.276 -12.987 7.339   1.00 16.51 ?  151 VAL   A HG13 1 
ATOM   3303 H HG21 . VAL   A 1 151 ? 20.186 -10.719 6.431   1.00 15.61 ?  151 VAL   A HG21 1 
ATOM   3304 H HG22 . VAL   A 1 151 ? 18.931 -10.504 7.381   1.00 15.61 ?  151 VAL   A HG22 1 
ATOM   3305 H HG23 . VAL   A 1 151 ? 20.387 -10.115 7.886   1.00 15.61 ?  151 VAL   A HG23 1 
ATOM   3306 N N    . TYR   A 1 152 ? 18.367 -10.429 10.288  1.00 11.59 ?  152 TYR   A N    1 
ATOM   3307 C CA   . TYR   A 1 152 ? 17.178 -9.698  10.695  1.00 11.26 ?  152 TYR   A CA   1 
ATOM   3308 C C    . TYR   A 1 152 ? 16.971 -8.586  9.679   1.00 11.19 ?  152 TYR   A C    1 
ATOM   3309 O O    . TYR   A 1 152 ? 17.738 -7.614  9.644   1.00 11.74 ?  152 TYR   A O    1 
ATOM   3310 C CB   . TYR   A 1 152 ? 17.359 -9.162  12.114  1.00 11.80 ?  152 TYR   A CB   1 
ATOM   3311 C CG   . TYR   A 1 152 ? 17.339 -10.295 13.103  1.00 12.62 ?  152 TYR   A CG   1 
ATOM   3312 C CD1  . TYR   A 1 152 ? 18.475 -11.048 13.360  1.00 14.05 ?  152 TYR   A CD1  1 
ATOM   3313 C CD2  . TYR   A 1 152 ? 16.162 -10.662 13.735  1.00 12.56 ?  152 TYR   A CD2  1 
ATOM   3314 C CE1  . TYR   A 1 152 ? 18.451 -12.119 14.234  1.00 14.82 ?  152 TYR   A CE1  1 
ATOM   3315 C CE2  . TYR   A 1 152 ? 16.119 -11.740 14.610  1.00 13.25 ?  152 TYR   A CE2  1 
ATOM   3316 C CZ   . TYR   A 1 152 ? 17.268 -12.469 14.857  1.00 14.26 ?  152 TYR   A CZ   1 
ATOM   3317 O OH   . TYR   A 1 152 ? 17.233 -13.546 15.726  1.00 16.19 ?  152 TYR   A OH   1 
ATOM   3318 H H    . TYR   A 1 152 ? 19.087 -9.956  10.381  1.00 13.88 ?  152 TYR   A H    1 
ATOM   3319 H HA   . TYR   A 1 152 ? 16.411 -10.291 10.673  1.00 13.48 ?  152 TYR   A HA   1 
ATOM   3320 H HB2  . TYR   A 1 152 ? 18.211 -8.716  12.183  1.00 14.13 ?  152 TYR   A HB2  1 
ATOM   3321 H HB3  . TYR   A 1 152 ? 16.635 -8.555  12.325  1.00 14.13 ?  152 TYR   A HB3  1 
ATOM   3322 H HD1  . TYR   A 1 152 ? 19.269 -10.825 12.934  1.00 16.84 ?  152 TYR   A HD1  1 
ATOM   3323 H HD2  . TYR   A 1 152 ? 15.378 -10.185 13.563  1.00 15.05 ?  152 TYR   A HD2  1 
ATOM   3324 H HE1  . TYR   A 1 152 ? 19.223 -12.605 14.400  1.00 17.76 ?  152 TYR   A HE1  1 
ATOM   3325 H HE2  . TYR   A 1 152 ? 15.317 -11.964 15.032  1.00 15.87 ?  152 TYR   A HE2  1 
ATOM   3326 H HH   . TYR   A 1 152 ? 16.455 -13.628 16.041  1.00 19.40 ?  152 TYR   A HH   1 
ATOM   3327 N N    A LEU   A 1 153 ? 15.933 -8.731  8.860   0.40 11.08 ?  153 LEU   A N    1 
ATOM   3328 N N    B LEU   A 1 153 ? 15.956 -8.741  8.837   0.60 11.62 ?  153 LEU   A N    1 
ATOM   3329 C CA   A LEU   A 1 153 ? 15.657 -7.841  7.741   0.40 11.13 ?  153 LEU   A CA   1 
ATOM   3330 C CA   B LEU   A 1 153 ? 15.675 -7.792  7.768   0.60 12.36 ?  153 LEU   A CA   1 
ATOM   3331 C C    A LEU   A 1 153 ? 14.645 -6.773  8.138   0.40 11.25 ?  153 LEU   A C    1 
ATOM   3332 C C    B LEU   A 1 153 ? 14.680 -6.744  8.249   0.60 13.05 ?  153 LEU   A C    1 
ATOM   3333 O O    A LEU   A 1 153 ? 13.616 -7.072  8.756   0.40 12.36 ?  153 LEU   A O    1 
ATOM   3334 O O    B LEU   A 1 153 ? 13.565 -7.081  8.672   0.60 14.41 ?  153 LEU   A O    1 
ATOM   3335 C CB   A LEU   A 1 153 ? 15.094 -8.636  6.562   0.40 11.18 ?  153 LEU   A CB   1 
ATOM   3336 C CB   B LEU   A 1 153 ? 15.114 -8.522  6.550   0.60 12.51 ?  153 LEU   A CB   1 
ATOM   3337 C CG   A LEU   A 1 153 ? 16.047 -9.577  5.831   0.40 11.25 ?  153 LEU   A CG   1 
ATOM   3338 C CG   B LEU   A 1 153 ? 16.039 -9.572  5.927   0.60 12.42 ?  153 LEU   A CG   1 
ATOM   3339 C CD1  A LEU   A 1 153 ? 15.259 -10.471 4.891   0.40 11.88 ?  153 LEU   A CD1  1 
ATOM   3340 C CD1  B LEU   A 1 153 ? 15.261 -10.440 4.949   0.60 13.09 ?  153 LEU   A CD1  1 
ATOM   3341 C CD2  A LEU   A 1 153 ? 17.074 -8.766  5.065   0.40 11.33 ?  153 LEU   A CD2  1 
ATOM   3342 C CD2  B LEU   A 1 153 ? 17.245 -8.924  5.240   0.60 12.54 ?  153 LEU   A CD2  1 
ATOM   3343 H H    A LEU   A 1 153 ? 15.344 -9.359  8.943   0.40 13.27 ?  153 LEU   A H    1 
ATOM   3344 H H    B LEU   A 1 153 ? 15.398 -9.402  8.868   0.60 13.91 ?  153 LEU   A H    1 
ATOM   3345 H HA   A LEU   A 1 153 ? 16.479 -7.411  7.463   0.40 13.33 ?  153 LEU   A HA   1 
ATOM   3346 H HA   B LEU   A 1 153 ? 16.499 -7.350  7.520   0.60 14.80 ?  153 LEU   A HA   1 
ATOM   3347 H HB2  A LEU   A 1 153 ? 14.360 -9.176  6.885   0.40 13.39 ?  153 LEU   A HB2  1 
ATOM   3348 H HB2  B LEU   A 1 153 ? 14.300 -8.972  6.816   0.60 14.98 ?  153 LEU   A HB2  1 
ATOM   3349 H HB3  A LEU   A 1 153 ? 14.765 -8.005  5.903   0.40 13.39 ?  153 LEU   A HB3  1 
ATOM   3350 H HB3  B LEU   A 1 153 ? 14.916 -7.860  5.870   0.60 14.98 ?  153 LEU   A HB3  1 
ATOM   3351 H HG   A LEU   A 1 153 ? 16.516 -10.136 6.476   0.40 13.48 ?  153 LEU   A HG   1 
ATOM   3352 H HG   B LEU   A 1 153 ? 16.382 -10.141 6.632   0.60 14.88 ?  153 LEU   A HG   1 
ATOM   3353 H HD11 A LEU   A 1 153 ? 15.860 -11.123 4.500   0.40 14.24 ?  153 LEU   A HD11 1 
ATOM   3354 H HD11 B LEU   A 1 153 ? 15.850 -11.133 4.610   0.60 15.68 ?  153 LEU   A HD11 1 
ATOM   3355 H HD12 A LEU   A 1 153 ? 14.565 -10.917 5.394   0.40 14.24 ?  153 LEU   A HD12 1 
ATOM   3356 H HD12 B LEU   A 1 153 ? 14.513 -10.837 5.415   0.60 15.68 ?  153 LEU   A HD12 1 
ATOM   3357 H HD13 A LEU   A 1 153 ? 14.868 -9.920  4.196   0.40 14.24 ?  153 LEU   A HD13 1 
ATOM   3358 H HD13 B LEU   A 1 153 ? 14.947 -9.886  4.219   0.60 15.68 ?  153 LEU   A HD13 1 
ATOM   3359 H HD21 A LEU   A 1 153 ? 17.634 -9.368  4.553   0.40 13.58 ?  153 LEU   A HD21 1 
ATOM   3360 H HD21 B LEU   A 1 153 ? 17.829 -9.621  4.901   0.60 15.03 ?  153 LEU   A HD21 1 
ATOM   3361 H HD22 A LEU   A 1 153 ? 16.610 -8.156  4.470   0.40 13.58 ?  153 LEU   A HD22 1 
ATOM   3362 H HD22 B LEU   A 1 153 ? 16.934 -8.368  4.508   0.60 15.03 ?  153 LEU   A HD22 1 
ATOM   3363 H HD23 A LEU   A 1 153 ? 17.617 -8.264  5.695   0.40 13.58 ?  153 LEU   A HD23 1 
ATOM   3364 H HD23 B LEU   A 1 153 ? 17.728 -8.379  5.885   0.60 15.03 ?  153 LEU   A HD23 1 
ATOM   3365 N N    A ALA   A 1 154 ? 14.940 -5.530  7.755   0.40 10.08 ?  154 ALA   A N    1 
ATOM   3366 N N    B ALA   A 1 154 ? 15.080 -5.475  8.157   0.60 12.40 ?  154 ALA   A N    1 
ATOM   3367 C CA   A ALA   A 1 154 ? 14.060 -4.389  7.973   0.40 10.34 ?  154 ALA   A CA   1 
ATOM   3368 C CA   B ALA   A 1 154 ? 14.228 -4.342  8.491   0.60 13.08 ?  154 ALA   A CA   1 
ATOM   3369 C C    A ALA   A 1 154 ? 13.550 -3.896  6.624   0.40 10.24 ?  154 ALA   A C    1 
ATOM   3370 C C    B ALA   A 1 154 ? 13.701 -3.734  7.196   0.60 13.06 ?  154 ALA   A C    1 
ATOM   3371 O O    A ALA   A 1 154 ? 14.345 -3.558  5.738   0.40 10.85 ?  154 ALA   A O    1 
ATOM   3372 O O    B ALA   A 1 154 ? 14.484 -3.353  6.317   0.60 13.07 ?  154 ALA   A O    1 
ATOM   3373 C CB   A ALA   A 1 154 ? 14.808 -3.261  8.685   0.40 10.75 ?  154 ALA   A CB   1 
ATOM   3374 C CB   B ALA   A 1 154 ? 15.002 -3.296  9.297   0.60 13.64 ?  154 ALA   A CB   1 
ATOM   3375 H H    A ALA   A 1 154 ? 15.676 -5.318  7.361   0.40 12.07 ?  154 ALA   A H    1 
ATOM   3376 H H    B ALA   A 1 154 ? 15.871 -5.239  7.891   0.60 14.85 ?  154 ALA   A H    1 
ATOM   3377 H HA   A ALA   A 1 154 ? 13.305 -4.657  8.522   0.40 12.38 ?  154 ALA   A HA   1 
ATOM   3378 H HA   B ALA   A 1 154 ? 13.479 -4.639  9.022   0.60 15.67 ?  154 ALA   A HA   1 
ATOM   3379 H HB1  A ALA   A 1 154 ? 14.203 -2.516  8.817   0.40 12.88 ?  154 ALA   A HB1  1 
ATOM   3380 H HB1  B ALA   A 1 154 ? 14.415 -2.553  9.505   0.60 16.34 ?  154 ALA   A HB1  1 
ATOM   3381 H HB2  A ALA   A 1 154 ? 15.132 -3.583  9.540   0.40 12.88 ?  154 ALA   A HB2  1 
ATOM   3382 H HB2  B ALA   A 1 154 ? 15.323 -3.702  10.120  0.60 16.34 ?  154 ALA   A HB2  1 
ATOM   3383 H HB3  A ALA   A 1 154 ? 15.558 -2.984  8.132   0.40 12.88 ?  154 ALA   A HB3  1 
ATOM   3384 H HB3  B ALA   A 1 154 ? 15.758 -2.982  8.772   0.60 16.34 ?  154 ALA   A HB3  1 
ATOM   3385 N N    A VAL   A 1 155 ? 12.229 -3.848  6.479   0.40 10.56 ?  155 VAL   A N    1 
ATOM   3386 N N    B VAL   A 1 155 ? 12.379 -3.644  7.084   0.60 13.39 ?  155 VAL   A N    1 
ATOM   3387 C CA   A VAL   A 1 155 ? 11.567 -3.363  5.274   0.40 11.37 ?  155 VAL   A CA   1 
ATOM   3388 C CA   B VAL   A 1 155 ? 11.710 -3.074  5.921   0.60 13.90 ?  155 VAL   A CA   1 
ATOM   3389 C C    A VAL   A 1 155 ? 10.817 -2.092  5.660   0.40 12.76 ?  155 VAL   A C    1 
ATOM   3390 C C    B VAL   A 1 155 ? 10.894 -1.883  6.399   0.60 14.99 ?  155 VAL   A C    1 
ATOM   3391 O O    A VAL   A 1 155 ? 9.867  -2.143  6.449   0.40 13.39 ?  155 VAL   A O    1 
ATOM   3392 O O    B VAL   A 1 155 ? 9.971  -2.044  7.207   0.60 15.19 ?  155 VAL   A O    1 
ATOM   3393 C CB   A VAL   A 1 155 ? 10.624 -4.425  4.685   0.40 11.62 ?  155 VAL   A CB   1 
ATOM   3394 C CB   B VAL   A 1 155 ? 10.820 -4.112  5.221   0.60 14.22 ?  155 VAL   A CB   1 
ATOM   3395 C CG1  A VAL   A 1 155 ? 9.958  -3.913  3.416   0.40 12.01 ?  155 VAL   A CG1  1 
ATOM   3396 C CG1  B VAL   A 1 155 ? 9.997  -3.457  4.129   0.60 14.69 ?  155 VAL   A CG1  1 
ATOM   3397 C CG2  A VAL   A 1 155 ? 11.376 -5.728  4.405   0.40 11.78 ?  155 VAL   A CG2  1 
ATOM   3398 C CG2  B VAL   A 1 155 ? 11.682 -5.230  4.649   0.60 15.04 ?  155 VAL   A CG2  1 
ATOM   3399 H H    A VAL   A 1 155 ? 11.678 -4.110  7.089   0.40 12.65 ?  155 VAL   A H    1 
ATOM   3400 H H    B VAL   A 1 155 ? 11.834 -3.914  7.692   0.60 16.04 ?  155 VAL   A H    1 
ATOM   3401 H HA   A VAL   A 1 155 ? 12.232 -3.146  4.603   0.40 13.61 ?  155 VAL   A HA   1 
ATOM   3402 H HA   B VAL   A 1 155 ? 12.374 -2.759  5.288   0.60 16.66 ?  155 VAL   A HA   1 
ATOM   3403 H HB   A VAL   A 1 155 ? 9.924  -4.623  5.330   0.40 13.92 ?  155 VAL   A HB   1 
ATOM   3404 H HB   B VAL   A 1 155 ? 10.213 -4.498  5.874   0.60 17.04 ?  155 VAL   A HB   1 
ATOM   3405 H HG11 A VAL   A 1 155 ? 9.465  -4.642  3.002   0.40 14.39 ?  155 VAL   A HG11 1 
ATOM   3406 H HG11 B VAL   A 1 155 ? 9.632  -4.149  3.557   0.60 17.61 ?  155 VAL   A HG11 1 
ATOM   3407 H HG12 A VAL   A 1 155 ? 9.350  -3.195  3.645   0.40 14.39 ?  155 VAL   A HG12 1 
ATOM   3408 H HG12 B VAL   A 1 155 ? 9.274  -2.951  4.535   0.60 17.61 ?  155 VAL   A HG12 1 
ATOM   3409 H HG13 A VAL   A 1 155 ? 10.642 -3.593  2.810   0.40 14.39 ?  155 VAL   A HG13 1 
ATOM   3410 H HG13 B VAL   A 1 155 ? 10.567 -2.868  3.614   0.60 17.61 ?  155 VAL   A HG13 1 
ATOM   3411 H HG21 A VAL   A 1 155 ? 10.798 -6.326  3.903   0.40 14.11 ?  155 VAL   A HG21 1 
ATOM   3412 H HG21 B VAL   A 1 155 ? 11.108 -5.870  4.203   0.60 18.02 ?  155 VAL   A HG21 1 
ATOM   3413 H HG22 A VAL   A 1 155 ? 12.171 -5.528  3.889   0.40 14.11 ?  155 VAL   A HG22 1 
ATOM   3414 H HG22 B VAL   A 1 155 ? 12.310 -4.848  4.016   0.60 18.02 ?  155 VAL   A HG22 1 
ATOM   3415 H HG23 A VAL   A 1 155 ? 11.623 -6.139  5.249   0.40 14.11 ?  155 VAL   A HG23 1 
ATOM   3416 H HG23 B VAL   A 1 155 ? 12.162 -5.660  5.373   0.60 18.02 ?  155 VAL   A HG23 1 
ATOM   3417 N N    A PHE   A 1 156 ? 11.246 -0.953  5.106   0.40 14.07 ?  156 PHE   A N    1 
ATOM   3418 N N    B PHE   A 1 156 ? 11.234 -0.690  5.902   0.60 16.04 ?  156 PHE   A N    1 
ATOM   3419 C CA   A PHE   A 1 156 ? 10.723 0.348   5.529   0.40 15.07 ?  156 PHE   A CA   1 
ATOM   3420 C CA   B PHE   A 1 156 ? 10.634 0.530   6.433   0.60 17.84 ?  156 PHE   A CA   1 
ATOM   3421 C C    A PHE   A 1 156 ? 9.265  0.528   5.120   0.40 14.90 ?  156 PHE   A C    1 
ATOM   3422 C C    B PHE   A 1 156 ? 9.151  0.627   6.088   0.60 18.76 ?  156 PHE   A C    1 
ATOM   3423 O O    A PHE   A 1 156 ? 8.461  1.077   5.884   0.40 15.17 ?  156 PHE   A O    1 
ATOM   3424 O O    B PHE   A 1 156 ? 8.326  0.975   6.942   0.60 18.83 ?  156 PHE   A O    1 
ATOM   3425 C CB   A PHE   A 1 156 ? 11.600 1.454   4.926   0.40 16.02 ?  156 PHE   A CB   1 
ATOM   3426 C CB   B PHE   A 1 156 ? 11.387 1.756   5.910   0.60 19.59 ?  156 PHE   A CB   1 
ATOM   3427 C CG   A PHE   A 1 156 ? 11.157 2.859   5.263   0.40 17.13 ?  156 PHE   A CG   1 
ATOM   3428 C CG   B PHE   A 1 156 ? 10.866 3.055   6.455   0.60 21.74 ?  156 PHE   A CG   1 
ATOM   3429 C CD1  A PHE   A 1 156 ? 11.156 3.302   6.574   0.40 17.25 ?  156 PHE   A CD1  1 
ATOM   3430 C CD1  B PHE   A 1 156 ? 9.829  3.722   5.824   0.60 22.94 ?  156 PHE   A CD1  1 
ATOM   3431 C CD2  A PHE   A 1 156 ? 10.788 3.744   4.260   0.40 17.85 ?  156 PHE   A CD2  1 
ATOM   3432 C CD2  B PHE   A 1 156 ? 11.402 3.599   7.609   0.60 22.75 ?  156 PHE   A CD2  1 
ATOM   3433 C CE1  A PHE   A 1 156 ? 10.767 4.595   6.882   0.40 17.83 ?  156 PHE   A CE1  1 
ATOM   3434 C CE1  B PHE   A 1 156 ? 9.345  4.912   6.328   0.60 23.41 ?  156 PHE   A CE1  1 
ATOM   3435 C CE2  A PHE   A 1 156 ? 10.398 5.037   4.563   0.40 18.51 ?  156 PHE   A CE2  1 
ATOM   3436 C CE2  B PHE   A 1 156 ? 10.922 4.790   8.119   0.60 23.28 ?  156 PHE   A CE2  1 
ATOM   3437 C CZ   A PHE   A 1 156 ? 10.394 5.463   5.875   0.40 18.31 ?  156 PHE   A CZ   1 
ATOM   3438 C CZ   B PHE   A 1 156 ? 9.892  5.447   7.478   0.60 23.59 ?  156 PHE   A CZ   1 
ATOM   3439 H H    A PHE   A 1 156 ? 11.843 -0.917  4.491   0.40 16.86 ?  156 PHE   A H    1 
ATOM   3440 H H    B PHE   A 1 156 ? 11.809 -0.561  5.267   0.60 19.23 ?  156 PHE   A H    1 
ATOM   3441 H HA   A PHE   A 1 156 ? 10.782 0.411   6.496   0.40 18.06 ?  156 PHE   A HA   1 
ATOM   3442 H HA   B PHE   A 1 156 ? 10.723 0.527   7.400   0.60 21.38 ?  156 PHE   A HA   1 
ATOM   3443 H HB2  A PHE   A 1 156 ? 12.512 1.341   5.253   0.40 19.20 ?  156 PHE   A HB2  1 
ATOM   3444 H HB2  B PHE   A 1 156 ? 12.324 1.688   6.159   0.60 23.48 ?  156 PHE   A HB2  1 
ATOM   3445 H HB3  A PHE   A 1 156 ? 11.593 1.362   3.960   0.40 19.20 ?  156 PHE   A HB3  1 
ATOM   3446 H HB3  B PHE   A 1 156 ? 11.307 1.789   4.944   0.60 23.48 ?  156 PHE   A HB3  1 
ATOM   3447 H HD1  A PHE   A 1 156 ? 11.414 2.723   7.257   0.40 20.67 ?  156 PHE   A HD1  1 
ATOM   3448 H HD1  B PHE   A 1 156 ? 9.458  3.367   5.048   0.60 27.50 ?  156 PHE   A HD1  1 
ATOM   3449 H HD2  A PHE   A 1 156 ? 10.794 3.458   3.374   0.40 21.40 ?  156 PHE   A HD2  1 
ATOM   3450 H HD2  B PHE   A 1 156 ? 12.097 3.159   8.044   0.60 27.27 ?  156 PHE   A HD2  1 
ATOM   3451 H HE1  A PHE   A 1 156 ? 10.767 4.881   7.767   0.40 21.37 ?  156 PHE   A HE1  1 
ATOM   3452 H HE1  B PHE   A 1 156 ? 8.650  5.353   5.894   0.60 28.06 ?  156 PHE   A HE1  1 
ATOM   3453 H HE2  A PHE   A 1 156 ? 10.146 5.617   3.883   0.40 22.18 ?  156 PHE   A HE2  1 
ATOM   3454 H HE2  B PHE   A 1 156 ? 11.290 5.149   8.893   0.60 27.92 ?  156 PHE   A HE2  1 
ATOM   3455 H HZ   A PHE   A 1 156 ? 10.131 6.330   6.082   0.40 21.94 ?  156 PHE   A HZ   1 
ATOM   3456 H HZ   B PHE   A 1 156 ? 9.565  6.249   7.819   0.60 28.29 ?  156 PHE   A HZ   1 
ATOM   3457 N N    A ASP   A 1 157 ? 8.911  0.070   3.927   0.40 14.87 ?  157 ASP   A N    1 
ATOM   3458 N N    B ASP   A 1 157 ? 8.792  0.348   4.839   0.60 19.97 ?  157 ASP   A N    1 
ATOM   3459 C CA   A ASP   A 1 157 ? 7.598  0.321   3.351   0.40 15.56 ?  157 ASP   A CA   1 
ATOM   3460 C CA   B ASP   A 1 157 ? 7.428  0.591   4.380   0.60 22.21 ?  157 ASP   A CA   1 
ATOM   3461 C C    A ASP   A 1 157 ? 6.615  -0.743  3.836   0.40 15.11 ?  157 ASP   A C    1 
ATOM   3462 C C    B ASP   A 1 157 ? 6.519  -0.560  4.795   0.60 23.01 ?  157 ASP   A C    1 
ATOM   3463 O O    A ASP   A 1 157 ? 6.821  -1.937  3.597   0.40 14.36 ?  157 ASP   A O    1 
ATOM   3464 O O    B ASP   A 1 157 ? 6.786  -1.722  4.468   0.60 22.43 ?  157 ASP   A O    1 
ATOM   3465 C CB   A ASP   A 1 157 ? 7.716  0.293   1.831   0.40 16.86 ?  157 ASP   A CB   1 
ATOM   3466 C CB   B ASP   A 1 157 ? 7.414  0.757   2.865   0.60 23.57 ?  157 ASP   A CB   1 
ATOM   3467 C CG   A ASP   A 1 157 ? 6.498  0.859   1.142   0.40 18.42 ?  157 ASP   A CG   1 
ATOM   3468 C CG   B ASP   A 1 157 ? 6.047  1.119   2.328   0.60 24.63 ?  157 ASP   A CG   1 
ATOM   3469 O OD1  A ASP   A 1 157 ? 6.362  2.100   1.091   0.40 19.54 ?  157 ASP   A OD1  1 
ATOM   3470 O OD1  B ASP   A 1 157 ? 5.591  2.261   2.548   0.60 25.55 ?  157 ASP   A OD1  1 
ATOM   3471 O OD2  A ASP   A 1 157 ? 5.672  0.061   0.651   0.40 18.77 -1 157 ASP   A OD2  1 
ATOM   3472 O OD2  B ASP   A 1 157 ? 5.431  0.254   1.674   0.60 23.99 -1 157 ASP   A OD2  1 
ATOM   3473 H H    A ASP   A 1 157 ? 9.426  -0.409  3.428   0.40 17.82 ?  157 ASP   A H    1 
ATOM   3474 H H    B ASP   A 1 157 ? 9.324  0.029   4.241   0.60 23.94 ?  157 ASP   A H    1 
ATOM   3475 H HA   A ASP   A 1 157 ? 7.280  1.189   3.634   0.40 18.65 ?  157 ASP   A HA   1 
ATOM   3476 H HA   B ASP   A 1 157 ? 7.104  1.406   4.795   0.60 26.63 ?  157 ASP   A HA   1 
ATOM   3477 H HB2  A ASP   A 1 157 ? 8.496  0.812   1.572   0.40 20.21 ?  157 ASP   A HB2  1 
ATOM   3478 H HB2  B ASP   A 1 157 ? 8.043  1.450   2.622   0.60 28.26 ?  157 ASP   A HB2  1 
ATOM   3479 H HB3  A ASP   A 1 157 ? 7.821  -0.626  1.541   0.40 20.21 ?  157 ASP   A HB3  1 
ATOM   3480 H HB3  B ASP   A 1 157 ? 7.653  -0.083  2.459   0.60 28.26 ?  157 ASP   A HB3  1 
ATOM   3481 N N    A LYS   A 1 158 ? 5.543  -0.309  4.509   0.40 15.76 ?  158 LYS   A N    1 
ATOM   3482 N N    B LYS   A 1 158 ? 5.434  -0.230  5.503   0.60 24.65 ?  158 LYS   A N    1 
ATOM   3483 C CA   A LYS   A 1 158 ? 4.602  -1.258  5.104   0.40 16.32 ?  158 LYS   A CA   1 
ATOM   3484 C CA   B LYS   A 1 158 ? 4.502  -1.261  5.951   0.60 26.49 ?  158 LYS   A CA   1 
ATOM   3485 C C    A LYS   A 1 158 ? 3.877  -2.074  4.036   0.40 16.37 ?  158 LYS   A C    1 
ATOM   3486 C C    B LYS   A 1 158 ? 3.862  -1.971  4.767   0.60 26.01 ?  158 LYS   A C    1 
ATOM   3487 O O    A LYS   A 1 158 ? 3.668  -3.281  4.203   0.40 16.61 ?  158 LYS   A O    1 
ATOM   3488 O O    B LYS   A 1 158 ? 3.659  -3.190  4.800   0.60 26.03 ?  158 LYS   A O    1 
ATOM   3489 C CB   A LYS   A 1 158 ? 3.610  -0.513  6.003   0.40 17.47 ?  158 LYS   A CB   1 
ATOM   3490 C CB   B LYS   A 1 158 ? 3.423  -0.641  6.841   0.60 28.87 ?  158 LYS   A CB   1 
ATOM   3491 C CG   A LYS   A 1 158 ? 2.440  -1.352  6.512   0.40 19.26 ?  158 LYS   A CG   1 
ATOM   3492 C CG   B LYS   A 1 158 ? 2.713  -1.637  7.755   0.60 31.07 ?  158 LYS   A CG   1 
ATOM   3493 C CD   A LYS   A 1 158 ? 2.889  -2.552  7.340   0.40 20.80 ?  158 LYS   A CD   1 
ATOM   3494 C CD   B LYS   A 1 158 ? 1.527  -2.326  7.088   0.60 32.79 ?  158 LYS   A CD   1 
ATOM   3495 C CE   A LYS   A 1 158 ? 1.690  -3.271  7.945   0.40 22.09 ?  158 LYS   A CE   1 
ATOM   3496 C CE   B LYS   A 1 158 ? 1.114  -3.563  7.871   0.60 33.89 ?  158 LYS   A CE   1 
ATOM   3497 N NZ   A LYS   A 1 158 ? 2.045  -4.586  8.548   0.40 22.77 ?  158 LYS   A NZ   1 
ATOM   3498 N NZ   B LYS   A 1 158 ? 1.257  -3.365  9.339   0.60 34.52 ?  158 LYS   A NZ   1 
ATOM   3499 H H    A LYS   A 1 158 ? 5.350  0.515   4.638   0.40 18.88 ?  158 LYS   A H    1 
ATOM   3500 H H    B LYS   A 1 158 ? 5.225  0.571   5.734   0.60 29.56 ?  158 LYS   A H    1 
ATOM   3501 H HA   A LYS   A 1 158 ? 5.097  -1.877  5.668   0.40 19.56 ?  158 LYS   A HA   1 
ATOM   3502 H HA   B LYS   A 1 158 ? 4.983  -1.920  6.474   0.60 31.76 ?  158 LYS   A HA   1 
ATOM   3503 H HB2  A LYS   A 1 158 ? 4.088  -0.178  6.781   0.40 20.94 ?  158 LYS   A HB2  1 
ATOM   3504 H HB2  B LYS   A 1 158 ? 3.832  0.033   7.404   0.60 34.62 ?  158 LYS   A HB2  1 
ATOM   3505 H HB3  A LYS   A 1 158 ? 3.242  0.233   5.505   0.40 20.94 ?  158 LYS   A HB3  1 
ATOM   3506 H HB3  B LYS   A 1 158 ? 2.750  -0.229  6.275   0.60 34.62 ?  158 LYS   A HB3  1 
ATOM   3507 H HG2  A LYS   A 1 158 ? 1.880  -0.795  7.075   0.40 23.08 ?  158 LYS   A HG2  1 
ATOM   3508 H HG2  B LYS   A 1 158 ? 3.340  -2.325  8.025   0.60 37.26 ?  158 LYS   A HG2  1 
ATOM   3509 H HG3  A LYS   A 1 158 ? 1.926  -1.679  5.758   0.40 23.08 ?  158 LYS   A HG3  1 
ATOM   3510 H HG3  B LYS   A 1 158 ? 2.379  -1.167  8.536   0.60 37.26 ?  158 LYS   A HG3  1 
ATOM   3511 H HD2  A LYS   A 1 158 ? 3.366  -3.176  6.772   0.40 24.93 ?  158 LYS   A HD2  1 
ATOM   3512 H HD2  B LYS   A 1 158 ? 0.770  -1.718  7.064   0.60 39.32 ?  158 LYS   A HD2  1 
ATOM   3513 H HD3  A LYS   A 1 158 ? 3.462  -2.247  8.062   0.40 24.93 ?  158 LYS   A HD3  1 
ATOM   3514 H HD3  B LYS   A 1 158 ? 1.763  -2.603  6.191   0.60 39.32 ?  158 LYS   A HD3  1 
ATOM   3515 H HE2  A LYS   A 1 158 ? 1.304  -2.713  8.639   0.40 26.48 ?  158 LYS   A HE2  1 
ATOM   3516 H HE2  B LYS   A 1 158 ? 0.185  -3.767  7.680   0.60 40.64 ?  158 LYS   A HE2  1 
ATOM   3517 H HE3  A LYS   A 1 158 ? 1.035  -3.427  7.249   0.40 26.48 ?  158 LYS   A HE3  1 
ATOM   3518 H HE3  B LYS   A 1 158 ? 1.679  -4.308  7.616   0.60 40.64 ?  158 LYS   A HE3  1 
ATOM   3519 H HZ1  A LYS   A 1 158 ? 1.320  -4.971  8.888   0.40 27.30 ?  158 LYS   A HZ1  1 
ATOM   3520 H HZ1  B LYS   A 1 158 ? 0.843  -4.021  9.777   0.60 41.40 ?  158 LYS   A HZ1  1 
ATOM   3521 H HZ2  A LYS   A 1 158 ? 2.391  -5.120  7.924   0.40 27.30 ?  158 LYS   A HZ2  1 
ATOM   3522 H HZ2  B LYS   A 1 158 ? 2.118  -3.367  9.565   0.60 41.40 ?  158 LYS   A HZ2  1 
ATOM   3523 H HZ3  A LYS   A 1 158 ? 2.645  -4.473  9.195   0.40 27.30 ?  158 LYS   A HZ3  1 
ATOM   3524 H HZ3  B LYS   A 1 158 ? 0.897  -2.586  9.576   0.60 41.40 ?  158 LYS   A HZ3  1 
ATOM   3525 N N    A ASN   A 1 159 ? 3.488  -1.438  2.931   0.40 17.06 ?  159 ASN   A N    1 
ATOM   3526 N N    B ASN   A 1 159 ? 3.531  -1.225  3.713   0.60 25.48 ?  159 ASN   A N    1 
ATOM   3527 C CA   A ASN   A 1 159 ? 2.798  -2.167  1.871   0.40 17.40 ?  159 ASN   A CA   1 
ATOM   3528 C CA   B ASN   A 1 159 ? 2.851  -1.830  2.575   0.60 25.00 ?  159 ASN   A CA   1 
ATOM   3529 C C    A ASN   A 1 159 ? 3.690  -3.263  1.287   0.40 16.46 ?  159 ASN   A C    1 
ATOM   3530 C C    B ASN   A 1 159 ? 3.767  -2.793  1.828   0.60 22.28 ?  159 ASN   A C    1 
ATOM   3531 O O    A ASN   A 1 159 ? 3.232  -4.383  1.033   0.40 16.26 ?  159 ASN   A O    1 
ATOM   3532 O O    B ASN   A 1 159 ? 3.342  -3.895  1.459   0.60 21.71 ?  159 ASN   A O    1 
ATOM   3533 C CB   A ASN   A 1 159 ? 2.317  -1.178  0.805   0.40 19.15 ?  159 ASN   A CB   1 
ATOM   3534 C CB   B ASN   A 1 159 ? 2.297  -0.741  1.658   0.60 27.53 ?  159 ASN   A CB   1 
ATOM   3535 C CG   A ASN   A 1 159 ? 1.189  -0.294  1.307   0.40 20.70 ?  159 ASN   A CG   1 
ATOM   3536 C CG   B ASN   A 1 159 ? 1.333  0.184   2.376   0.60 29.97 ?  159 ASN   A CG   1 
ATOM   3537 O OD1  A ASN   A 1 159 ? 0.308  -0.764  2.021   0.40 21.37 ?  159 ASN   A OD1  1 
ATOM   3538 O OD1  B ASN   A 1 159 ? 0.118  0.055   2.239   0.60 31.11 ?  159 ASN   A OD1  1 
ATOM   3539 N ND2  A ASN   A 1 159 ? 1.222  0.988   0.954   0.40 21.66 ?  159 ASN   A ND2  1 
ATOM   3540 N ND2  B ASN   A 1 159 ? 1.873  1.115   3.160   0.60 30.96 ?  159 ASN   A ND2  1 
ATOM   3541 H H    A ASN   A 1 159 ? 3.629  -0.609  2.769   0.40 20.45 ?  159 ASN   A H    1 
ATOM   3542 H H    B ASN   A 1 159 ? 3.689  -0.383  3.635   0.60 30.55 ?  159 ASN   A H    1 
ATOM   3543 H HA   A ASN   A 1 159 ? 2.018  -2.597  2.249   0.40 20.85 ?  159 ASN   A HA   1 
ATOM   3544 H HA   B ASN   A 1 159 ? 2.101  -2.344  2.901   0.60 29.97 ?  159 ASN   A HA   1 
ATOM   3545 H HB2  A ASN   A 1 159 ? 3.054  -0.603  0.547   0.40 22.95 ?  159 ASN   A HB2  1 
ATOM   3546 H HB2  B ASN   A 1 159 ? 3.033  -0.208  1.334   0.60 33.01 ?  159 ASN   A HB2  1 
ATOM   3547 H HB3  A ASN   A 1 159 ? 1.993  -1.671  0.035   0.40 22.95 ?  159 ASN   A HB3  1 
ATOM   3548 H HB3  B ASN   A 1 159 ? 1.823  -1.153  0.915   0.60 33.01 ?  159 ASN   A HB3  1 
ATOM   3549 H HD21 A ASN   A 1 159 ? 0.604  1.526   1.215   0.40 25.97 ?  159 ASN   A HD21 1 
ATOM   3550 H HD21 B ASN   A 1 159 ? 1.368  1.663   3.592   0.60 37.12 ?  159 ASN   A HD21 1 
ATOM   3551 H HD22 A ASN   A 1 159 ? 1.864  1.281   0.464   0.40 25.97 ?  159 ASN   A HD22 1 
ATOM   3552 H HD22 B ASN   A 1 159 ? 2.728  1.173   3.234   0.60 37.12 ?  159 ASN   A HD22 1 
ATOM   3553 N N    A LEU   A 1 160 ? 4.978  -2.975  1.117   0.40 15.60 ?  160 LEU   A N    1 
ATOM   3554 N N    B LEU   A 1 160 ? 5.026  -2.409  1.600   0.60 20.32 ?  160 LEU   A N    1 
ATOM   3555 C CA   A LEU   A 1 160 ? 5.899  -3.965  0.562   0.40 14.86 ?  160 LEU   A CA   1 
ATOM   3556 C CA   B LEU   A 1 160 ? 5.972  -3.356  1.019   0.60 18.61 ?  160 LEU   A CA   1 
ATOM   3557 C C    A LEU   A 1 160 ? 6.117  -5.126  1.523   0.40 14.80 ?  160 LEU   A C    1 
ATOM   3558 C C    B LEU   A 1 160 ? 6.165  -4.556  1.935   0.60 17.82 ?  160 LEU   A C    1 
ATOM   3559 O O    A LEU   A 1 160 ? 6.160  -6.291  1.105   0.40 14.85 ?  160 LEU   A O    1 
ATOM   3560 O O    B LEU   A 1 160 ? 6.208  -5.704  1.476   0.60 18.27 ?  160 LEU   A O    1 
ATOM   3561 C CB   A LEU   A 1 160 ? 7.235  -3.299  0.251   0.40 14.51 ?  160 LEU   A CB   1 
ATOM   3562 C CB   B LEU   A 1 160 ? 7.311  -2.674  0.743   0.60 18.15 ?  160 LEU   A CB   1 
ATOM   3563 C CG   A LEU   A 1 160 ? 8.347  -4.251  -0.181  0.40 14.37 ?  160 LEU   A CG   1 
ATOM   3564 C CG   B LEU   A 1 160 ? 8.417  -3.659  0.353   0.60 17.92 ?  160 LEU   A CG   1 
ATOM   3565 C CD1  A LEU   A 1 160 ? 7.912  -4.983  -1.437  0.40 14.46 ?  160 LEU   A CD1  1 
ATOM   3566 C CD1  B LEU   A 1 160 ? 8.034  -4.429  -0.904  0.60 17.86 ?  160 LEU   A CD1  1 
ATOM   3567 C CD2  A LEU   A 1 160 ? 9.652  -3.502  -0.406  0.40 14.35 ?  160 LEU   A CD2  1 
ATOM   3568 C CD2  B LEU   A 1 160 ? 9.734  -2.936  0.164   0.60 17.87 ?  160 LEU   A CD2  1 
ATOM   3569 H H    A LEU   A 1 160 ? 5.345  -2.238  1.334   0.40 18.69 ?  160 LEU   A H    1 
ATOM   3570 H H    B LEU   A 1 160 ? 5.350  -1.625  1.766   0.60 24.36 ?  160 LEU   A H    1 
ATOM   3571 H HA   A LEU   A 1 160 ? 5.530  -4.323  -0.259  0.40 17.80 ?  160 LEU   A HA   1 
ATOM   3572 H HA   B LEU   A 1 160 ? 5.623  -3.674  0.175   0.60 22.31 ?  160 LEU   A HA   1 
ATOM   3573 H HB2  A LEU   A 1 160 ? 7.098  -2.663  -0.463  0.40 17.38 ?  160 LEU   A HB2  1 
ATOM   3574 H HB2  B LEU   A 1 160 ? 7.203  -2.042  0.010   0.60 21.76 ?  160 LEU   A HB2  1 
ATOM   3575 H HB3  A LEU   A 1 160 ? 7.539  -2.839  1.049   0.40 17.38 ?  160 LEU   A HB3  1 
ATOM   3576 H HB3  B LEU   A 1 160 ? 7.600  -2.201  1.540   0.60 21.76 ?  160 LEU   A HB3  1 
ATOM   3577 H HG   A LEU   A 1 160 ? 8.503  -4.912  0.515   0.40 17.22 ?  160 LEU   A HG   1 
ATOM   3578 H HG   B LEU   A 1 160 ? 8.547  -4.297  1.068   0.60 21.47 ?  160 LEU   A HG   1 
ATOM   3579 H HD11 A LEU   A 1 160 ? 8.657  -5.504  -1.768  0.40 17.32 ?  160 LEU   A HD11 1 
ATOM   3580 H HD11 B LEU   A 1 160 ? 8.798  -4.951  -1.195  0.60 21.41 ?  160 LEU   A HD11 1 
ATOM   3581 H HD12 A LEU   A 1 160 ? 7.169  -5.569  -1.222  0.40 17.32 ?  160 LEU   A HD12 1 
ATOM   3582 H HD12 B LEU   A 1 160 ? 7.291  -5.018  -0.701  0.60 21.41 ?  160 LEU   A HD12 1 
ATOM   3583 H HD13 A LEU   A 1 160 ? 7.639  -4.331  -2.100  0.40 17.32 ?  160 LEU   A HD13 1 
ATOM   3584 H HD13 B LEU   A 1 160 ? 7.780  -3.799  -1.596  0.60 21.41 ?  160 LEU   A HD13 1 
ATOM   3585 H HD21 A LEU   A 1 160 ? 10.337 -4.134  -0.678  0.40 17.20 ?  160 LEU   A HD21 1 
ATOM   3586 H HD21 B LEU   A 1 160 ? 10.415 -3.581  -0.078  0.60 21.42 ?  160 LEU   A HD21 1 
ATOM   3587 H HD22 A LEU   A 1 160 ? 9.519  -2.838  -1.099  0.40 17.20 ?  160 LEU   A HD22 1 
ATOM   3588 H HD22 B LEU   A 1 160 ? 9.636  -2.276  -0.539  0.60 21.42 ?  160 LEU   A HD22 1 
ATOM   3589 H HD23 A LEU   A 1 160 ? 9.914  -3.068  0.422   0.40 17.20 ?  160 LEU   A HD23 1 
ATOM   3590 H HD23 B LEU   A 1 160 ? 9.975  -2.498  0.998   0.60 21.42 ?  160 LEU   A HD23 1 
ATOM   3591 N N    A TYR   A 1 161 ? 6.296  -4.827  2.809   0.40 14.55 ?  161 TYR   A N    1 
ATOM   3592 N N    B TYR   A 1 161 ? 6.288  -4.307  3.237   0.60 17.39 ?  161 TYR   A N    1 
ATOM   3593 C CA   A TYR   A 1 161 ? 6.474  -5.876  3.804   0.40 15.05 ?  161 TYR   A CA   1 
ATOM   3594 C CA   B TYR   A 1 161 ? 6.423  -5.404  4.184   0.60 17.84 ?  161 TYR   A CA   1 
ATOM   3595 C C    A TYR   A 1 161 ? 5.321  -6.867  3.757   0.40 15.51 ?  161 TYR   A C    1 
ATOM   3596 C C    B TYR   A 1 161 ? 5.288  -6.421  4.048   0.60 18.70 ?  161 TYR   A C    1 
ATOM   3597 O O    A TYR   A 1 161 ? 5.534  -8.078  3.626   0.40 15.12 ?  161 TYR   A O    1 
ATOM   3598 O O    B TYR   A 1 161 ? 5.511  -7.623  4.235   0.60 18.34 ?  161 TYR   A O    1 
ATOM   3599 C CB   A TYR   A 1 161 ? 6.590  -5.247  5.194   0.40 15.49 ?  161 TYR   A CB   1 
ATOM   3600 C CB   B TYR   A 1 161 ? 6.518  -4.829  5.598   0.60 18.44 ?  161 TYR   A CB   1 
ATOM   3601 C CG   A TYR   A 1 161 ? 6.524  -6.253  6.315   0.40 15.68 ?  161 TYR   A CG   1 
ATOM   3602 C CG   B TYR   A 1 161 ? 6.406  -5.850  6.694   0.60 19.03 ?  161 TYR   A CG   1 
ATOM   3603 C CD1  A TYR   A 1 161 ? 7.662  -6.919  6.739   0.40 15.60 ?  161 TYR   A CD1  1 
ATOM   3604 C CD1  B TYR   A 1 161 ? 7.517  -6.561  7.135   0.60 19.19 ?  161 TYR   A CD1  1 
ATOM   3605 C CD2  A TYR   A 1 161 ? 5.321  -6.546  6.944   0.40 16.04 ?  161 TYR   A CD2  1 
ATOM   3606 C CD2  B TYR   A 1 161 ? 5.187  -6.090  7.305   0.60 19.71 ?  161 TYR   A CD2  1 
ATOM   3607 C CE1  A TYR   A 1 161 ? 7.608  -7.845  7.757   0.40 15.64 ?  161 TYR   A CE1  1 
ATOM   3608 C CE1  B TYR   A 1 161 ? 7.404  -7.495  8.148   0.60 19.96 ?  161 TYR   A CE1  1 
ATOM   3609 C CE2  A TYR   A 1 161 ? 5.256  -7.470  7.964   0.40 15.95 ?  161 TYR   A CE2  1 
ATOM   3610 C CE2  B TYR   A 1 161 ? 5.064  -7.015  8.312   0.60 20.30 ?  161 TYR   A CE2  1 
ATOM   3611 C CZ   A TYR   A 1 161 ? 6.402  -8.119  8.367   0.40 16.03 ?  161 TYR   A CZ   1 
ATOM   3612 C CZ   B TYR   A 1 161 ? 6.169  -7.716  8.734   0.60 20.86 ?  161 TYR   A CZ   1 
ATOM   3613 O OH   A TYR   A 1 161 ? 6.341  -9.046  9.384   0.40 16.41 ?  161 TYR   A OH   1 
ATOM   3614 O OH   B TYR   A 1 161 ? 6.022  -8.636  9.746   0.60 22.14 ?  161 TYR   A OH   1 
ATOM   3615 H H    A TYR   A 1 161 ? 6.307  -4.043  3.131   0.40 17.43 ?  161 TYR   A H    1 
ATOM   3616 H H    B TYR   A 1 161 ? 6.301  -3.519  3.590   0.60 20.84 ?  161 TYR   A H    1 
ATOM   3617 H HA   A TYR   A 1 161 ? 7.293  -6.370  3.626   0.40 18.03 ?  161 TYR   A HA   1 
ATOM   3618 H HA   B TYR   A 1 161 ? 7.259  -5.862  4.005   0.60 21.38 ?  161 TYR   A HA   1 
ATOM   3619 H HB2  A TYR   A 1 161 ? 7.443  -4.789  5.259   0.40 18.56 ?  161 TYR   A HB2  1 
ATOM   3620 H HB2  B TYR   A 1 161 ? 7.375  -4.383  5.697   0.60 22.11 ?  161 TYR   A HB2  1 
ATOM   3621 H HB3  A TYR   A 1 161 ? 5.865  -4.619  5.317   0.40 18.56 ?  161 TYR   A HB3  1 
ATOM   3622 H HB3  B TYR   A 1 161 ? 5.802  -4.186  5.721   0.60 22.11 ?  161 TYR   A HB3  1 
ATOM   3623 H HD1  A TYR   A 1 161 ? 8.477  -6.743  6.331   0.40 18.69 ?  161 TYR   A HD1  1 
ATOM   3624 H HD1  B TYR   A 1 161 ? 8.347  -6.410  6.739   0.60 23.00 ?  161 TYR   A HD1  1 
ATOM   3625 H HD2  A TYR   A 1 161 ? 4.545  -6.112  6.677   0.40 19.22 ?  161 TYR   A HD2  1 
ATOM   3626 H HD2  B TYR   A 1 161 ? 4.436  -5.618  7.024   0.60 23.63 ?  161 TYR   A HD2  1 
ATOM   3627 H HE1  A TYR   A 1 161 ? 8.380  -8.287  8.032   0.40 18.74 ?  161 TYR   A HE1  1 
ATOM   3628 H HE1  B TYR   A 1 161 ? 8.155  -7.967  8.434   0.60 23.92 ?  161 TYR   A HE1  1 
ATOM   3629 H HE2  A TYR   A 1 161 ? 4.443  -7.658  8.379   0.40 19.11 ?  161 TYR   A HE2  1 
ATOM   3630 H HE2  B TYR   A 1 161 ? 4.236  -7.164  8.709   0.60 24.34 ?  161 TYR   A HE2  1 
ATOM   3631 H HH   A TYR   A 1 161 ? 5.546  -9.117  9.663   0.40 19.67 ?  161 TYR   A HH   1 
ATOM   3632 H HH   B TYR   A 1 161 ? 5.218  -8.656  9.996   0.60 26.54 ?  161 TYR   A HH   1 
ATOM   3633 N N    A ASP   A 1 162 ? 4.089  -6.365  3.862   0.40 16.30 ?  162 ASP   A N    1 
ATOM   3634 N N    B ASP   A 1 162 ? 4.076  -5.969  3.697   0.60 19.89 ?  162 ASP   A N    1 
ATOM   3635 C CA   A ASP   A 1 162 ? 2.920  -7.236  3.791   0.40 17.00 ?  162 ASP   A CA   1 
ATOM   3636 C CA   B ASP   A 1 162 ? 2.940  -6.889  3.587   0.60 21.53 ?  162 ASP   A CA   1 
ATOM   3637 C C    A ASP   A 1 162 ? 2.930  -8.063  2.513   0.40 17.24 ?  162 ASP   A C    1 
ATOM   3638 C C    B ASP   A 1 162 ? 3.038  -7.770  2.348   0.60 21.62 ?  162 ASP   A C    1 
ATOM   3639 O O    A ASP   A 1 162 ? 2.561  -9.243  2.526   0.40 17.47 ?  162 ASP   A O    1 
ATOM   3640 O O    B ASP   A 1 162 ? 2.699  -8.961  2.397   0.60 21.97 ?  162 ASP   A O    1 
ATOM   3641 C CB   A ASP   A 1 162 ? 1.640  -6.399  3.885   0.40 17.96 ?  162 ASP   A CB   1 
ATOM   3642 C CB   B ASP   A 1 162 ? 1.625  -6.113  3.528   0.60 23.45 ?  162 ASP   A CB   1 
ATOM   3643 C CG   A ASP   A 1 162 ? 1.361  -5.904  5.296   0.40 18.98 ?  162 ASP   A CG   1 
ATOM   3644 C CG   B ASP   A 1 162 ? 1.295  -5.415  4.832   0.60 24.93 ?  162 ASP   A CG   1 
ATOM   3645 O OD1  A ASP   A 1 162 ? 2.033  -6.367  6.243   0.40 19.51 ?  162 ASP   A OD1  1 
ATOM   3646 O OD1  B ASP   A 1 162 ? 1.853  -5.809  5.874   0.60 25.47 ?  162 ASP   A OD1  1 
ATOM   3647 O OD2  A ASP   A 1 162 ? 0.442  -5.069  5.460   0.40 19.41 -1 162 ASP   A OD2  1 
ATOM   3648 O OD2  B ASP   A 1 162 ? 0.456  -4.489  4.819   0.60 25.78 -1 162 ASP   A OD2  1 
ATOM   3649 H H    A ASP   A 1 162 ? 3.907  -5.537  3.962   0.40 19.53 ?  162 ASP   A H    1 
ATOM   3650 H H    B ASP   A 1 162 ? 3.890  -5.143  3.523   0.60 23.85 ?  162 ASP   A H    1 
ATOM   3651 H HA   A ASP   A 1 162 ? 2.924  -7.849  4.542   0.40 20.38 ?  162 ASP   A HA   1 
ATOM   3652 H HA   B ASP   A 1 162 ? 2.920  -7.462  4.367   0.60 25.81 ?  162 ASP   A HA   1 
ATOM   3653 H HB2  A ASP   A 1 162 ? 1.713  -5.638  3.280   0.40 21.53 ?  162 ASP   A HB2  1 
ATOM   3654 H HB2  B ASP   A 1 162 ? 1.687  -5.450  2.820   0.60 28.11 ?  162 ASP   A HB2  1 
ATOM   3655 H HB3  A ASP   A 1 162 ? 0.877  -6.941  3.637   0.40 21.53 ?  162 ASP   A HB3  1 
ATOM   3656 H HB3  B ASP   A 1 162 ? 0.908  -6.739  3.325   0.60 28.11 ?  162 ASP   A HB3  1 
ATOM   3657 N N    A LYS   A 1 163 ? 3.368  -7.470  1.401   0.40 17.63 ?  163 LYS   A N    1 
ATOM   3658 N N    B LYS   A 1 163 ? 3.445  -7.188  1.217   0.60 21.87 ?  163 LYS   A N    1 
ATOM   3659 C CA   A LYS   A 1 163 ? 3.451  -8.219  0.151   0.40 18.34 ?  163 LYS   A CA   1 
ATOM   3660 C CA   B LYS   A 1 163 ? 3.567  -7.950  -0.021  0.60 22.29 ?  163 LYS   A CA   1 
ATOM   3661 C C    A LYS   A 1 163 ? 4.556  -9.267  0.213   0.40 17.97 ?  163 LYS   A C    1 
ATOM   3662 C C    B LYS   A 1 163 ? 4.617  -9.043  0.114   0.60 21.11 ?  163 LYS   A C    1 
ATOM   3663 O O    A LYS   A 1 163 ? 4.379  -10.392 -0.270  0.40 18.88 ?  163 LYS   A O    1 
ATOM   3664 O O    B LYS   A 1 163 ? 4.447  -10.148 -0.413  0.60 21.43 ?  163 LYS   A O    1 
ATOM   3665 C CB   A LYS   A 1 163 ? 3.669  -7.257  -1.018  0.40 20.23 ?  163 LYS   A CB   1 
ATOM   3666 C CB   B LYS   A 1 163 ? 3.942  -6.991  -1.153  0.60 24.72 ?  163 LYS   A CB   1 
ATOM   3667 C CG   A LYS   A 1 163 ? 3.691  -7.925  -2.382  0.40 22.80 ?  163 LYS   A CG   1 
ATOM   3668 C CG   B LYS   A 1 163 ? 3.831  -7.535  -2.571  0.60 27.49 ?  163 LYS   A CG   1 
ATOM   3669 C CD   A LYS   A 1 163 ? 4.080  -6.944  -3.476  0.40 25.31 ?  163 LYS   A CD   1 
ATOM   3670 C CD   B LYS   A 1 163 ? 4.116  -6.411  -3.572  0.60 30.20 ?  163 LYS   A CD   1 
ATOM   3671 C CE   A LYS   A 1 163 ? 3.990  -7.589  -4.850  0.40 27.02 ?  163 LYS   A CE   1 
ATOM   3672 C CE   B LYS   A 1 163 ? 3.741  -6.775  -5.005  0.60 32.08 ?  163 LYS   A CE   1 
ATOM   3673 N NZ   A LYS   A 1 163 ? 4.590  -6.734  -5.913  0.40 27.95 ?  163 LYS   A NZ   1 
ATOM   3674 N NZ   B LYS   A 1 163 ? 4.897  -7.284  -5.794  0.60 33.06 ?  163 LYS   A NZ   1 
ATOM   3675 H H    A LYS   A 1 163 ? 3.622  -6.653  1.347   0.40 21.13 ?  163 LYS   A H    1 
ATOM   3676 H H    B LYS   A 1 163 ? 3.654  -6.358  1.141   0.60 26.22 ?  163 LYS   A H    1 
ATOM   3677 H HA   A LYS   A 1 163 ? 2.614  -8.683  0.002   0.40 21.98 ?  163 LYS   A HA   1 
ATOM   3678 H HA   B LYS   A 1 163 ? 2.716  -8.363  -0.235  0.60 26.72 ?  163 LYS   A HA   1 
ATOM   3679 H HB2  A LYS   A 1 163 ? 2.947  -6.606  -1.023  0.40 24.25 ?  163 LYS   A HB2  1 
ATOM   3680 H HB2  B LYS   A 1 163 ? 3.364  -6.216  -1.099  0.60 29.64 ?  163 LYS   A HB2  1 
ATOM   3681 H HB3  A LYS   A 1 163 ? 4.517  -6.804  -0.899  0.40 24.25 ?  163 LYS   A HB3  1 
ATOM   3682 H HB3  B LYS   A 1 163 ? 4.863  -6.715  -1.025  0.60 29.64 ?  163 LYS   A HB3  1 
ATOM   3683 H HG2  A LYS   A 1 163 ? 4.339  -8.645  -2.380  0.40 27.33 ?  163 LYS   A HG2  1 
ATOM   3684 H HG2  B LYS   A 1 163 ? 4.484  -8.241  -2.704  0.60 32.96 ?  163 LYS   A HG2  1 
ATOM   3685 H HG3  A LYS   A 1 163 ? 2.806  -8.270  -2.584  0.40 27.33 ?  163 LYS   A HG3  1 
ATOM   3686 H HG3  B LYS   A 1 163 ? 2.933  -7.868  -2.726  0.60 32.96 ?  163 LYS   A HG3  1 
ATOM   3687 H HD2  A LYS   A 1 163 ? 3.477  -6.184  -3.457  0.40 30.35 ?  163 LYS   A HD2  1 
ATOM   3688 H HD2  B LYS   A 1 163 ? 3.603  -5.627  -3.320  0.60 36.22 ?  163 LYS   A HD2  1 
ATOM   3689 H HD3  A LYS   A 1 163 ? 4.994  -6.651  -3.336  0.40 30.35 ?  163 LYS   A HD3  1 
ATOM   3690 H HD3  B LYS   A 1 163 ? 5.064  -6.205  -3.555  0.60 36.22 ?  163 LYS   A HD3  1 
ATOM   3691 H HE2  A LYS   A 1 163 ? 4.459  -8.437  -4.836  0.40 32.40 ?  163 LYS   A HE2  1 
ATOM   3692 H HE2  B LYS   A 1 163 ? 3.062  -7.466  -4.988  0.60 38.48 ?  163 LYS   A HE2  1 
ATOM   3693 H HE3  A LYS   A 1 163 ? 3.057  -7.730  -5.071  0.40 32.40 ?  163 LYS   A HE3  1 
ATOM   3694 H HE3  B LYS   A 1 163 ? 3.398  -5.984  -5.452  0.60 38.48 ?  163 LYS   A HE3  1 
ATOM   3695 H HZ1  A LYS   A 1 163 ? 4.522  -7.139  -6.703  0.40 33.52 ?  163 LYS   A HZ1  1 
ATOM   3696 H HZ1  B LYS   A 1 163 ? 4.725  -7.213  -6.665  0.60 39.65 ?  163 LYS   A HZ1  1 
ATOM   3697 H HZ2  A LYS   A 1 163 ? 4.164  -5.953  -5.951  0.40 33.52 ?  163 LYS   A HZ2  1 
ATOM   3698 H HZ2  B LYS   A 1 163 ? 5.627  -6.810  -5.605  0.60 39.65 ?  163 LYS   A HZ2  1 
ATOM   3699 H HZ3  A LYS   A 1 163 ? 5.450  -6.587  -5.736  0.40 33.52 ?  163 LYS   A HZ3  1 
ATOM   3700 H HZ3  B LYS   A 1 163 ? 5.047  -8.137  -5.598  0.60 39.65 ?  163 LYS   A HZ3  1 
ATOM   3701 N N    A LEU   A 1 164 ? 5.704  -8.917  0.805   0.40 16.88 ?  164 LEU   A N    1 
ATOM   3702 N N    B LEU   A 1 164 ? 5.718  -8.743  0.812   0.60 19.46 ?  164 LEU   A N    1 
ATOM   3703 C CA   A LEU   A 1 164 ? 6.805  -9.870  0.929   0.40 16.30 ?  164 LEU   A CA   1 
ATOM   3704 C CA   B LEU   A 1 164 ? 6.796  -9.714  0.989   0.60 18.64 ?  164 LEU   A CA   1 
ATOM   3705 C C    A LEU   A 1 164 ? 6.410  -11.054 1.798   0.40 16.61 ?  164 LEU   A C    1 
ATOM   3706 C C    B LEU   A 1 164 ? 6.341  -10.896 1.831   0.60 18.97 ?  164 LEU   A C    1 
ATOM   3707 O O    A LEU   A 1 164 ? 6.720  -12.205 1.471   0.40 17.14 ?  164 LEU   A O    1 
ATOM   3708 O O    B LEU   A 1 164 ? 6.641  -12.049 1.506   0.60 19.40 ?  164 LEU   A O    1 
ATOM   3709 C CB   A LEU   A 1 164 ? 8.024  -9.175  1.532   0.40 15.72 ?  164 LEU   A CB   1 
ATOM   3710 C CB   B LEU   A 1 164 ? 7.985  -9.037  1.664   0.60 17.94 ?  164 LEU   A CB   1 
ATOM   3711 C CG   A LEU   A 1 164 ? 8.778  -8.202  0.628   0.40 15.39 ?  164 LEU   A CG   1 
ATOM   3712 C CG   B LEU   A 1 164 ? 8.709  -7.978  0.838   0.60 17.92 ?  164 LEU   A CG   1 
ATOM   3713 C CD1  A LEU   A 1 164 ? 9.659  -7.289  1.461   0.40 15.11 ?  164 LEU   A CD1  1 
ATOM   3714 C CD1  B LEU   A 1 164 ? 9.654  -7.177  1.716   0.60 17.99 ?  164 LEU   A CD1  1 
ATOM   3715 C CD2  A LEU   A 1 164 ? 9.608  -8.958  -0.398  0.40 15.53 ?  164 LEU   A CD2  1 
ATOM   3716 C CD2  B LEU   A 1 164 ? 9.459  -8.633  -0.309  0.60 18.04 ?  164 LEU   A CD2  1 
ATOM   3717 H H    A LEU   A 1 164 ? 5.867  -8.144  1.144   0.40 20.24 ?  164 LEU   A H    1 
ATOM   3718 H H    B LEU   A 1 164 ? 5.864  -7.986  1.190   0.60 23.33 ?  164 LEU   A H    1 
ATOM   3719 H HA   A LEU   A 1 164 ? 7.043  -10.206 0.053   0.40 19.53 ?  164 LEU   A HA   1 
ATOM   3720 H HA   B LEU   A 1 164 ? 7.078  -10.048 0.123   0.60 22.34 ?  164 LEU   A HA   1 
ATOM   3721 H HB2  A LEU   A 1 164 ? 7.734  -8.678  2.311   0.40 18.84 ?  164 LEU   A HB2  1 
ATOM   3722 H HB2  B LEU   A 1 164 ? 7.672  -8.606  2.473   0.60 21.51 ?  164 LEU   A HB2  1 
ATOM   3723 H HB3  A LEU   A 1 164 ? 8.656  -9.859  1.806   0.40 18.84 ?  164 LEU   A HB3  1 
ATOM   3724 H HB3  B LEU   A 1 164 ? 8.637  -9.718  1.891   0.60 21.51 ?  164 LEU   A HB3  1 
ATOM   3725 H HG   A LEU   A 1 164 ? 8.137  -7.652  0.151   0.40 18.44 ?  164 LEU   A HG   1 
ATOM   3726 H HG   B LEU   A 1 164 ? 8.056  -7.366  0.462   0.60 21.48 ?  164 LEU   A HG   1 
ATOM   3727 H HD11 A LEU   A 1 164 ? 10.135 -6.686  0.871   0.40 18.11 ?  164 LEU   A HD11 1 
ATOM   3728 H HD11 B LEU   A 1 164 ? 10.105 -6.513  1.172   0.60 21.57 ?  164 LEU   A HD11 1 
ATOM   3729 H HD12 A LEU   A 1 164 ? 9.099  -6.784  2.072   0.40 18.11 ?  164 LEU   A HD12 1 
ATOM   3730 H HD12 B LEU   A 1 164 ? 9.140  -6.738  2.414   0.60 21.57 ?  164 LEU   A HD12 1 
ATOM   3731 H HD13 A LEU   A 1 164 ? 10.289 -7.831  1.962   0.40 18.11 ?  164 LEU   A HD13 1 
ATOM   3732 H HD13 B LEU   A 1 164 ? 10.302 -7.778  2.113   0.60 21.57 ?  164 LEU   A HD13 1 
ATOM   3733 H HD21 A LEU   A 1 164 ? 10.087 -8.318  -0.948  0.40 18.61 ?  164 LEU   A HD21 1 
ATOM   3734 H HD21 B LEU   A 1 164 ? 9.981  -7.958  -0.772  0.60 21.62 ?  164 LEU   A HD21 1 
ATOM   3735 H HD22 A LEU   A 1 164 ? 10.237 -9.532  0.066   0.40 18.61 ?  164 LEU   A HD22 1 
ATOM   3736 H HD22 B LEU   A 1 164 ? 10.048 -9.317  0.048   0.60 21.62 ?  164 LEU   A HD22 1 
ATOM   3737 H HD23 A LEU   A 1 164 ? 9.017  -9.493  -0.950  0.40 18.61 ?  164 LEU   A HD23 1 
ATOM   3738 H HD23 B LEU   A 1 164 ? 8.820  -9.032  -0.920  0.60 21.62 ?  164 LEU   A HD23 1 
ATOM   3739 N N    A VAL   A 1 165 ? 5.743  -10.785 2.919   0.40 16.62 ?  165 VAL   A N    1 
ATOM   3740 N N    B VAL   A 1 165 ? 5.637  -10.623 2.930   0.60 18.98 ?  165 VAL   A N    1 
ATOM   3741 C CA   A VAL   A 1 165 ? 5.288  -11.855 3.797   0.40 16.85 ?  165 VAL   A CA   1 
ATOM   3742 C CA   B VAL   A 1 165 ? 5.132  -11.696 3.781   0.60 19.34 ?  165 VAL   A CA   1 
ATOM   3743 C C    A VAL   A 1 165 ? 4.234  -12.701 3.096   0.40 16.79 ?  165 VAL   A C    1 
ATOM   3744 C C    B VAL   A 1 165 ? 4.106  -12.531 3.025   0.60 19.28 ?  165 VAL   A C    1 
ATOM   3745 O O    A VAL   A 1 165 ? 4.339  -13.931 3.037   0.40 16.63 ?  165 VAL   A O    1 
ATOM   3746 O O    B VAL   A 1 165 ? 4.194  -13.764 2.974   0.60 19.32 ?  165 VAL   A O    1 
ATOM   3747 C CB   A VAL   A 1 165 ? 4.768  -11.263 5.121   0.40 17.29 ?  165 VAL   A CB   1 
ATOM   3748 C CB   B VAL   A 1 165 ? 4.545  -11.111 5.080   0.60 19.98 ?  165 VAL   A CB   1 
ATOM   3749 C CG1  A VAL   A 1 165 ? 3.960  -12.293 5.901   0.40 17.59 ?  165 VAL   A CG1  1 
ATOM   3750 C CG1  B VAL   A 1 165 ? 3.915  -12.210 5.926   0.60 20.53 ?  165 VAL   A CG1  1 
ATOM   3751 C CG2  A VAL   A 1 165 ? 5.929  -10.728 5.954   0.40 17.59 ?  165 VAL   A CG2  1 
ATOM   3752 C CG2  B VAL   A 1 165 ? 5.617  -10.363 5.867   0.60 20.25 ?  165 VAL   A CG2  1 
ATOM   3753 H H    A VAL   A 1 165 ? 5.538  -10.000 3.190   0.40 19.92 ?  165 VAL   A H    1 
ATOM   3754 H H    B VAL   A 1 165 ? 5.447  -9.830  3.204   0.60 22.75 ?  165 VAL   A H    1 
ATOM   3755 H HA   A VAL   A 1 165 ? 6.036  -12.435 4.009   0.40 20.20 ?  165 VAL   A HA   1 
ATOM   3756 H HA   B VAL   A 1 165 ? 5.871  -12.274 4.028   0.60 23.18 ?  165 VAL   A HA   1 
ATOM   3757 H HB   A VAL   A 1 165 ? 4.183  -10.518 4.922   0.40 20.72 ?  165 VAL   A HB   1 
ATOM   3758 H HB   B VAL   A 1 165 ? 3.851  -10.474 4.852   0.60 23.95 ?  165 VAL   A HB   1 
ATOM   3759 H HG11 A VAL   A 1 165 ? 3.859  -11.983 6.813   0.40 21.08 ?  165 VAL   A HG11 1 
ATOM   3760 H HG11 B VAL   A 1 165 ? 3.767  -11.869 6.821   0.60 24.61 ?  165 VAL   A HG11 1 
ATOM   3761 H HG12 A VAL   A 1 165 ? 3.088  -12.390 5.488   0.40 21.08 ?  165 VAL   A HG12 1 
ATOM   3762 H HG12 B VAL   A 1 165 ? 3.072  -12.470 5.527   0.60 24.61 ?  165 VAL   A HG12 1 
ATOM   3763 H HG13 A VAL   A 1 165 ? 4.433  -13.136 5.890   0.40 21.08 ?  165 VAL   A HG13 1 
ATOM   3764 H HG13 B VAL   A 1 165 ? 4.520  -12.967 5.956   0.60 24.61 ?  165 VAL   A HG13 1 
ATOM   3765 H HG21 A VAL   A 1 165 ? 5.586  -10.382 6.793   0.40 21.09 ?  165 VAL   A HG21 1 
ATOM   3766 H HG21 B VAL   A 1 165 ? 5.205  -9.928  6.631   0.60 24.28 ?  165 VAL   A HG21 1 
ATOM   3767 H HG22 A VAL   A 1 165 ? 6.557  -11.447 6.124   0.40 21.09 ?  165 VAL   A HG22 1 
ATOM   3768 H HG22 B VAL   A 1 165 ? 6.288  -10.994 6.168   0.60 24.28 ?  165 VAL   A HG22 1 
ATOM   3769 H HG23 A VAL   A 1 165 ? 6.370  -10.016 5.460   0.40 21.09 ?  165 VAL   A HG23 1 
ATOM   3770 H HG23 B VAL   A 1 165 ? 6.029  -9.695  5.294   0.60 24.28 ?  165 VAL   A HG23 1 
ATOM   3771 N N    A SER   A 1 166 ? 3.209  -12.051 2.539   0.40 17.38 ?  166 SER   A N    1 
ATOM   3772 N N    B SER   A 1 166 ? 3.117  -11.867 2.425   0.60 19.66 ?  166 SER   A N    1 
ATOM   3773 C CA   A SER   A 1 166 ? 2.096  -12.792 1.952   0.40 17.82 ?  166 SER   A CA   1 
ATOM   3774 C CA   B SER   A 1 166 ? 1.987  -12.572 1.824   0.60 20.22 ?  166 SER   A CA   1 
ATOM   3775 C C    A SER   A 1 166 ? 2.536  -13.608 0.749   0.40 18.79 ?  166 SER   A C    1 
ATOM   3776 C C    B SER   A 1 166 ? 2.387  -13.422 0.626   0.60 19.93 ?  166 SER   A C    1 
ATOM   3777 O O    A SER   A 1 166 ? 1.991  -14.694 0.506   0.40 19.50 ?  166 SER   A O    1 
ATOM   3778 O O    B SER   A 1 166 ? 1.655  -14.354 0.273   0.60 20.88 ?  166 SER   A O    1 
ATOM   3779 C CB   A SER   A 1 166 ? 0.965  -11.839 1.554   0.40 18.66 ?  166 SER   A CB   1 
ATOM   3780 C CB   B SER   A 1 166 ? 0.917  -11.572 1.376   0.60 22.21 ?  166 SER   A CB   1 
ATOM   3781 O OG   A SER   A 1 166 ? 0.333  -11.281 2.692   0.40 19.63 ?  166 SER   A OG   1 
ATOM   3782 O OG   B SER   A 1 166 ? 0.509  -10.724 2.435   0.60 24.06 ?  166 SER   A OG   1 
ATOM   3783 H H    A SER   A 1 166 ? 3.131  -11.202 2.494   0.40 20.83 ?  166 SER   A H    1 
ATOM   3784 H H    B SER   A 1 166 ? 3.068  -11.014 2.374   0.60 23.57 ?  166 SER   A H    1 
ATOM   3785 H HA   A SER   A 1 166 ? 1.740  -13.414 2.607   0.40 21.36 ?  166 SER   A HA   1 
ATOM   3786 H HA   B SER   A 1 166 ? 1.585  -13.158 2.485   0.60 24.23 ?  166 SER   A HA   1 
ATOM   3787 H HB2  A SER   A 1 166 ? 1.333  -11.120 1.019   0.40 22.37 ?  166 SER   A HB2  1 
ATOM   3788 H HB2  B SER   A 1 166 ? 1.273  -11.038 0.648   0.60 26.62 ?  166 SER   A HB2  1 
ATOM   3789 H HB3  A SER   A 1 166 ? 0.302  -12.328 1.039   0.40 22.37 ?  166 SER   A HB3  1 
ATOM   3790 H HB3  B SER   A 1 166 ? 0.137  -12.062 1.072   0.60 26.62 ?  166 SER   A HB3  1 
ATOM   3791 H HG   A SER   A 1 166 ? 0.898  -10.858 3.151   0.40 23.53 ?  166 SER   A HG   1 
ATOM   3792 H HG   B SER   A 1 166 ? -0.063 -10.172 2.158   0.60 28.84 ?  166 SER   A HG   1 
ATOM   3793 N N    . SER   A 1 167 ? 3.516  -13.116 -0.010  1.00 19.45 ?  167 SER   A N    1 
ATOM   3794 C CA   . SER   A 1 167 ? 3.978  -13.822 -1.194  1.00 20.49 ?  167 SER   A CA   1 
ATOM   3795 C C    . SER   A 1 167 ? 5.132  -14.767 -0.902  1.00 20.46 ?  167 SER   A C    1 
ATOM   3796 O O    . SER   A 1 167 ? 5.667  -15.373 -1.835  1.00 21.63 ?  167 SER   A O    1 
ATOM   3797 C CB   . SER   A 1 167 ? 4.393  -12.823 -2.284  1.00 21.56 ?  167 SER   A CB   1 
ATOM   3798 O OG   . SER   A 1 167 ? 5.464  -11.998 -1.844  1.00 21.68 ?  167 SER   A OG   1 
ATOM   3799 H H    A SER   A 1 167 ? 3.925  -12.373 0.141   0.40 23.31 ?  167 SER   A H    1 
ATOM   3800 H H    B SER   A 1 167 ? 4.040  -12.476 0.229   0.60 23.31 ?  167 SER   A H    1 
ATOM   3801 H HA   . SER   A 1 167 ? 3.244  -14.345 -1.551  1.00 24.57 ?  167 SER   A HA   1 
ATOM   3802 H HB2  . SER   A 1 167 ? 4.680  -13.316 -3.071  1.00 25.84 ?  167 SER   A HB2  1 
ATOM   3803 H HB3  . SER   A 1 167 ? 3.626  -12.266 -2.514  1.00 25.84 ?  167 SER   A HB3  1 
ATOM   3804 H HG   . SER   A 1 167 ? 5.225  -11.576 -1.154  1.00 25.99 ?  167 SER   A HG   1 
ATOM   3805 N N    . PHE   A 1 168 ? 5.529  -14.912 0.358   1.00 20.08 ?  168 PHE   A N    1 
ATOM   3806 C CA   . PHE   A 1 168 ? 6.713  -15.700 0.670   1.00 21.15 ?  168 PHE   A CA   1 
ATOM   3807 C C    . PHE   A 1 168 ? 6.414  -17.188 0.567   1.00 25.13 ?  168 PHE   A C    1 
ATOM   3808 O O    . PHE   A 1 168 ? 5.456  -17.685 1.171   1.00 24.89 ?  168 PHE   A O    1 
ATOM   3809 C CB   . PHE   A 1 168 ? 7.234  -15.397 2.070   1.00 19.81 ?  168 PHE   A CB   1 
ATOM   3810 C CG   . PHE   A 1 168 ? 8.499  -16.132 2.386   1.00 18.48 ?  168 PHE   A CG   1 
ATOM   3811 C CD1  . PHE   A 1 168 ? 9.681  -15.760 1.781   1.00 18.71 ?  168 PHE   A CD1  1 
ATOM   3812 C CD2  . PHE   A 1 168 ? 8.508  -17.220 3.243   1.00 17.75 ?  168 PHE   A CD2  1 
ATOM   3813 C CE1  . PHE   A 1 168 ? 10.852 -16.436 2.039   1.00 18.30 ?  168 PHE   A CE1  1 
ATOM   3814 C CE2  . PHE   A 1 168 ? 9.686  -17.898 3.508   1.00 17.81 ?  168 PHE   A CE2  1 
ATOM   3815 C CZ   . PHE   A 1 168 ? 10.857 -17.503 2.901   1.00 17.90 ?  168 PHE   A CZ   1 
ATOM   3816 H H    . PHE   A 1 168 ? 5.143  -14.555 1.036   1.00 24.07 ?  168 PHE   A H    1 
ATOM   3817 H HA   . PHE   A 1 168 ? 7.414  -15.486 0.030   1.00 25.36 ?  168 PHE   A HA   1 
ATOM   3818 H HB2  . PHE   A 1 168 ? 7.414  -14.446 2.139   1.00 23.75 ?  168 PHE   A HB2  1 
ATOM   3819 H HB3  . PHE   A 1 168 ? 6.562  -15.657 2.717   1.00 23.75 ?  168 PHE   A HB3  1 
ATOM   3820 H HD1  . PHE   A 1 168 ? 9.692  -15.038 1.197   1.00 22.43 ?  168 PHE   A HD1  1 
ATOM   3821 H HD2  . PHE   A 1 168 ? 7.717  -17.491 3.653   1.00 21.27 ?  168 PHE   A HD2  1 
ATOM   3822 H HE1  . PHE   A 1 168 ? 11.649 -16.170 1.634   1.00 21.94 ?  168 PHE   A HE1  1 
ATOM   3823 H HE2  . PHE   A 1 168 ? 9.686  -18.626 4.091   1.00 21.34 ?  168 PHE   A HE2  1 
ATOM   3824 H HZ   . PHE   A 1 168 ? 11.653 -17.961 3.079   1.00 21.46 ?  168 PHE   A HZ   1 
ATOM   3825 N N    . LEU   A 1 169 ? 7.258  -17.900 -0.175  1.00 30.96 ?  169 LEU   A N    1 
ATOM   3826 C CA   . LEU   A 1 169 ? 7.095  -19.334 -0.346  1.00 37.51 ?  169 LEU   A CA   1 
ATOM   3827 C C    . LEU   A 1 169 ? 8.001  -20.077 0.626   1.00 39.85 ?  169 LEU   A C    1 
ATOM   3828 O O    . LEU   A 1 169 ? 7.555  -20.516 1.687   1.00 40.69 ?  169 LEU   A O    1 
ATOM   3829 C CB   . LEU   A 1 169 ? 7.411  -19.741 -1.788  1.00 40.82 ?  169 LEU   A CB   1 
ATOM   3830 C CG   . LEU   A 1 169 ? 7.084  -21.183 -2.182  1.00 43.40 ?  169 LEU   A CG   1 
ATOM   3831 C CD1  . LEU   A 1 169 ? 5.679  -21.556 -1.738  1.00 44.39 ?  169 LEU   A CD1  1 
ATOM   3832 C CD2  . LEU   A 1 169 ? 7.231  -21.363 -3.686  1.00 44.27 ?  169 LEU   A CD2  1 
ATOM   3833 O OXT  . LEU   A 1 169 ? 9.198  -20.242 0.381   1.00 40.43 -1 169 LEU   A OXT  1 
ATOM   3834 H H    . LEU   A 1 169 ? 7.939  -17.573 -0.592  1.00 37.13 ?  169 LEU   A H    1 
ATOM   3835 H HA   . LEU   A 1 169 ? 6.176  -19.568 -0.153  1.00 44.99 ?  169 LEU   A HA   1 
ATOM   3836 H HB2  . LEU   A 1 169 ? 6.911  -19.163 -2.383  1.00 48.96 ?  169 LEU   A HB2  1 
ATOM   3837 H HB3  . LEU   A 1 169 ? 8.360  -19.613 -1.938  1.00 48.96 ?  169 LEU   A HB3  1 
ATOM   3838 H HG   . LEU   A 1 169 ? 7.709  -21.784 -1.746  1.00 52.05 ?  169 LEU   A HG   1 
ATOM   3839 H HD11 . LEU   A 1 169 ? 5.414  -22.372 -2.186  1.00 53.25 ?  169 LEU   A HD11 1 
ATOM   3840 H HD12 . LEU   A 1 169 ? 5.677  -21.689 -0.777  1.00 53.25 ?  169 LEU   A HD12 1 
ATOM   3841 H HD13 . LEU   A 1 169 ? 5.074  -20.835 -1.976  1.00 53.25 ?  169 LEU   A HD13 1 
ATOM   3842 H HD21 . LEU   A 1 169 ? 7.028  -22.284 -3.915  1.00 53.10 ?  169 LEU   A HD21 1 
ATOM   3843 H HD22 . LEU   A 1 169 ? 6.613  -20.766 -4.136  1.00 53.10 ?  169 LEU   A HD22 1 
ATOM   3844 H HD23 . LEU   A 1 169 ? 8.142  -21.151 -3.942  1.00 53.10 ?  169 LEU   A HD23 1 
ATOM   3845 N N    A SER   B 1 1   ? 50.727 -9.118  -23.727 0.40 29.58 ?  1   SER   B N    1 
ATOM   3846 N N    B SER   B 1 1   ? 50.946 -9.424  -24.022 0.60 26.15 ?  1   SER   B N    1 
ATOM   3847 C CA   A SER   B 1 1   ? 51.269 -10.213 -22.895 0.40 29.20 ?  1   SER   B CA   1 
ATOM   3848 C CA   B SER   B 1 1   ? 51.308 -10.337 -22.915 0.60 26.41 ?  1   SER   B CA   1 
ATOM   3849 C C    A SER   B 1 1   ? 50.218 -11.289 -22.671 0.40 28.33 ?  1   SER   B C    1 
ATOM   3850 C C    B SER   B 1 1   ? 50.208 -11.360 -22.648 0.60 26.61 ?  1   SER   B C    1 
ATOM   3851 O O    A SER   B 1 1   ? 49.036 -11.111 -22.987 0.40 28.08 ?  1   SER   B O    1 
ATOM   3852 O O    B SER   B 1 1   ? 49.031 -11.154 -22.976 0.60 26.25 ?  1   SER   B O    1 
ATOM   3853 C CB   A SER   B 1 1   ? 51.759 -9.673  -21.555 0.40 29.66 ?  1   SER   B CB   1 
ATOM   3854 C CB   B SER   B 1 1   ? 51.629 -9.549  -21.646 0.60 26.51 ?  1   SER   B CB   1 
ATOM   3855 O OG   A SER   B 1 1   ? 50.671 -9.247  -20.756 0.40 30.30 ?  1   SER   B OG   1 
ATOM   3856 O OG   B SER   B 1 1   ? 50.664 -9.791  -20.641 0.60 27.08 ?  1   SER   B OG   1 
ATOM   3857 H H1   A SER   B 1 1   ? 50.399 -9.462  -24.477 0.40 35.47 ?  1   SER   B H1   1 
ATOM   3858 H H1   B SER   B 1 1   ? 51.609 -8.845  -24.145 0.60 31.36 ?  1   SER   B H1   1 
ATOM   3859 H H2   A SER   B 1 1   ? 50.086 -8.703  -23.278 0.40 35.47 ?  1   SER   B H2   1 
ATOM   3860 H H2   B SER   B 1 1   ? 50.823 -9.901  -24.761 0.60 31.36 ?  1   SER   B H2   1 
ATOM   3861 H H3   A SER   B 1 1   ? 51.383 -8.550  -23.916 0.40 35.47 ?  1   SER   B H3   1 
ATOM   3862 H H3   B SER   B 1 1   ? 50.202 -8.992  -23.812 0.60 31.36 ?  1   SER   B H3   1 
ATOM   3863 H HA   A SER   B 1 1   ? 52.016 -10.610 -23.360 0.40 35.01 ?  1   SER   B HA   1 
ATOM   3864 H HA   B SER   B 1 1   ? 52.103 -10.815 -23.178 0.60 31.66 ?  1   SER   B HA   1 
ATOM   3865 H HB2  A SER   B 1 1   ? 52.241 -10.377 -21.095 0.40 35.57 ?  1   SER   B HB2  1 
ATOM   3866 H HB2  B SER   B 1 1   ? 52.496 -9.831  -21.319 0.60 31.79 ?  1   SER   B HB2  1 
ATOM   3867 H HB3  A SER   B 1 1   ? 52.346 -8.916  -21.713 0.40 35.57 ?  1   SER   B HB3  1 
ATOM   3868 H HB3  B SER   B 1 1   ? 51.648 -8.600  -21.858 0.60 31.79 ?  1   SER   B HB3  1 
ATOM   3869 H HG   A SER   B 1 1   ? 50.950 -8.760  -20.133 0.40 36.34 ?  1   SER   B HG   1 
ATOM   3870 H HG   B SER   B 1 1   ? 50.814 -9.295  -19.981 0.60 32.47 ?  1   SER   B HG   1 
ATOM   3871 N N    A MET   B 1 2   ? 50.664 -12.408 -22.115 0.40 27.65 ?  2   MET   B N    1 
ATOM   3872 N N    B MET   B 1 2   ? 50.615 -12.470 -22.044 0.60 26.87 ?  2   MET   B N    1 
ATOM   3873 C CA   A MET   B 1 2   ? 49.841 -13.594 -21.937 0.40 27.10 ?  2   MET   B CA   1 
ATOM   3874 C CA   B MET   B 1 2   ? 49.782 -13.660 -21.897 0.60 27.09 ?  2   MET   B CA   1 
ATOM   3875 C C    A MET   B 1 2   ? 49.604 -13.798 -20.447 0.40 23.82 ?  2   MET   B C    1 
ATOM   3876 C C    B MET   B 1 2   ? 49.525 -13.892 -20.413 0.60 24.15 ?  2   MET   B C    1 
ATOM   3877 O O    A MET   B 1 2   ? 50.553 -14.028 -19.689 0.40 23.36 ?  2   MET   B O    1 
ATOM   3878 O O    B MET   B 1 2   ? 50.416 -14.343 -19.687 0.60 24.36 ?  2   MET   B O    1 
ATOM   3879 C CB   A MET   B 1 2   ? 50.547 -14.801 -22.548 0.40 30.18 ?  2   MET   B CB   1 
ATOM   3880 C CB   B MET   B 1 2   ? 50.506 -14.843 -22.518 0.60 30.71 ?  2   MET   B CB   1 
ATOM   3881 C CG   A MET   B 1 2   ? 49.675 -16.029 -22.730 0.40 32.89 ?  2   MET   B CG   1 
ATOM   3882 C CG   B MET   B 1 2   ? 49.634 -16.043 -22.845 0.60 33.72 ?  2   MET   B CG   1 
ATOM   3883 S SD   A MET   B 1 2   ? 50.512 -17.303 -23.690 0.40 35.30 ?  2   MET   B SD   1 
ATOM   3884 S SD   B MET   B 1 2   ? 50.506 -17.209 -23.904 0.60 36.35 ?  2   MET   B SD   1 
ATOM   3885 C CE   A MET   B 1 2   ? 51.079 -16.327 -25.080 0.40 35.74 ?  2   MET   B CE   1 
ATOM   3886 C CE   B MET   B 1 2   ? 51.292 -16.069 -25.034 0.60 36.91 ?  2   MET   B CE   1 
ATOM   3887 H H    A MET   B 1 2   ? 51.468 -12.507 -21.823 0.40 33.15 ?  2   MET   B H    1 
ATOM   3888 H H    B MET   B 1 2   ? 51.403 -12.567 -21.710 0.60 32.22 ?  2   MET   B H    1 
ATOM   3889 H HA   A MET   B 1 2   ? 48.992 -13.482 -22.388 0.40 32.50 ?  2   MET   B HA   1 
ATOM   3890 H HA   B MET   B 1 2   ? 48.943 -13.536 -22.367 0.60 32.48 ?  2   MET   B HA   1 
ATOM   3891 H HB2  A MET   B 1 2   ? 50.879 -14.525 -23.416 0.40 36.19 ?  2   MET   B HB2  1 
ATOM   3892 H HB2  B MET   B 1 2   ? 50.910 -14.504 -23.325 0.60 36.82 ?  2   MET   B HB2  1 
ATOM   3893 H HB3  A MET   B 1 2   ? 51.289 -15.058 -21.983 0.40 36.19 ?  2   MET   B HB3  1 
ATOM   3894 H HB3  B MET   B 1 2   ? 51.198 -15.158 -21.918 0.60 36.82 ?  2   MET   B HB3  1 
ATOM   3895 H HG2  A MET   B 1 2   ? 49.458 -16.396 -21.858 0.40 39.45 ?  2   MET   B HG2  1 
ATOM   3896 H HG2  B MET   B 1 2   ? 49.393 -16.497 -22.019 0.60 40.43 ?  2   MET   B HG2  1 
ATOM   3897 H HG3  A MET   B 1 2   ? 48.865 -15.786 -23.203 0.40 39.45 ?  2   MET   B HG3  1 
ATOM   3898 H HG3  B MET   B 1 2   ? 48.840 -15.758 -23.316 0.60 40.43 ?  2   MET   B HG3  1 
ATOM   3899 H HE1  A MET   B 1 2   ? 51.241 -16.912 -25.828 0.40 42.87 ?  2   MET   B HE1  1 
ATOM   3900 H HE1  B MET   B 1 2   ? 51.531 -16.547 -25.826 0.60 44.26 ?  2   MET   B HE1  1 
ATOM   3901 H HE2  A MET   B 1 2   ? 50.392 -15.677 -25.305 0.40 42.87 ?  2   MET   B HE2  1 
ATOM   3902 H HE2  B MET   B 1 2   ? 50.660 -15.359 -25.247 0.60 44.26 ?  2   MET   B HE2  1 
ATOM   3903 H HE3  A MET   B 1 2   ? 51.898 -15.862 -24.835 0.40 42.87 ?  2   MET   B HE3  1 
ATOM   3904 H HE3  B MET   B 1 2   ? 52.088 -15.690 -24.616 0.60 44.26 ?  2   MET   B HE3  1 
ATOM   3905 N N    A VAL   B 1 3   ? 48.344 -13.684 -20.032 0.40 21.08 ?  3   VAL   B N    1 
ATOM   3906 N N    B VAL   B 1 3   ? 48.311 -13.582 -19.965 0.60 21.18 ?  3   VAL   B N    1 
ATOM   3907 C CA   A VAL   B 1 3   ? 47.933 -13.921 -18.656 0.40 19.25 ?  3   VAL   B CA   1 
ATOM   3908 C CA   B VAL   B 1 3   ? 47.888 -13.842 -18.595 0.60 19.71 ?  3   VAL   B CA   1 
ATOM   3909 C C    A VAL   B 1 3   ? 46.703 -14.818 -18.675 0.40 17.27 ?  3   VAL   B C    1 
ATOM   3910 C C    B VAL   B 1 3   ? 46.654 -14.730 -18.625 0.60 17.72 ?  3   VAL   B C    1 
ATOM   3911 O O    A VAL   B 1 3   ? 45.990 -14.916 -19.675 0.40 17.22 ?  3   VAL   B O    1 
ATOM   3912 O O    B VAL   B 1 3   ? 45.884 -14.731 -19.590 0.60 18.20 ?  3   VAL   B O    1 
ATOM   3913 C CB   A VAL   B 1 3   ? 47.650 -12.608 -17.886 0.40 20.11 ?  3   VAL   B CB   1 
ATOM   3914 C CB   B VAL   B 1 3   ? 47.617 -12.544 -17.798 0.60 20.95 ?  3   VAL   B CB   1 
ATOM   3915 C CG1  A VAL   B 1 3   ? 48.914 -11.756 -17.793 0.40 20.51 ?  3   VAL   B CG1  1 
ATOM   3916 C CG1  B VAL   B 1 3   ? 48.883 -11.693 -17.709 0.60 21.46 ?  3   VAL   B CG1  1 
ATOM   3917 C CG2  A VAL   B 1 3   ? 46.522 -11.829 -18.548 0.40 20.61 ?  3   VAL   B CG2  1 
ATOM   3918 C CG2  B VAL   B 1 3   ? 46.471 -11.760 -18.420 0.60 21.58 ?  3   VAL   B CG2  1 
ATOM   3919 H H    A VAL   B 1 3   ? 47.695 -13.457 -20.546 0.40 25.28 ?  3   VAL   B H    1 
ATOM   3920 H H    B VAL   B 1 3   ? 47.705 -13.212 -20.451 0.60 25.38 ?  3   VAL   B H    1 
ATOM   3921 H HA   A VAL   B 1 3   ? 48.635 -14.393 -18.187 0.40 23.07 ?  3   VAL   B HA   1 
ATOM   3922 H HA   B VAL   B 1 3   ? 48.587 -14.328 -18.137 0.60 23.62 ?  3   VAL   B HA   1 
ATOM   3923 H HB   A VAL   B 1 3   ? 47.376 -12.822 -16.980 0.40 24.11 ?  3   VAL   B HB   1 
ATOM   3924 H HB   B VAL   B 1 3   ? 47.359 -12.782 -16.894 0.60 25.11 ?  3   VAL   B HB   1 
ATOM   3925 H HG11 A VAL   B 1 3   ? 48.715 -10.947 -17.295 0.40 24.59 ?  3   VAL   B HG11 1 
ATOM   3926 H HG11 B VAL   B 1 3   ? 48.692 -10.896 -17.189 0.60 25.73 ?  3   VAL   B HG11 1 
ATOM   3927 H HG12 A VAL   B 1 3   ? 49.603 -12.264 -17.336 0.40 24.59 ?  3   VAL   B HG12 1 
ATOM   3928 H HG12 B VAL   B 1 3   ? 49.580 -12.210 -17.275 0.60 25.73 ?  3   VAL   B HG12 1 
ATOM   3929 H HG13 A VAL   B 1 3   ? 49.208 -11.530 -18.688 0.40 24.59 ?  3   VAL   B HG13 1 
ATOM   3930 H HG13 B VAL   B 1 3   ? 49.161 -11.446 -18.604 0.60 25.73 ?  3   VAL   B HG13 1 
ATOM   3931 H HG21 A VAL   B 1 3   ? 46.465 -10.949 -18.143 0.40 24.71 ?  3   VAL   B HG21 1 
ATOM   3932 H HG21 B VAL   B 1 3   ? 46.427 -10.884 -18.006 0.60 25.87 ?  3   VAL   B HG21 1 
ATOM   3933 H HG22 A VAL   B 1 3   ? 46.709 -11.746 -19.495 0.40 24.71 ?  3   VAL   B HG22 1 
ATOM   3934 H HG22 B VAL   B 1 3   ? 46.630 -11.669 -19.371 0.60 25.87 ?  3   VAL   B HG22 1 
ATOM   3935 H HG23 A VAL   B 1 3   ? 45.689 -12.307 -18.415 0.40 24.71 ?  3   VAL   B HG23 1 
ATOM   3936 H HG23 B VAL   B 1 3   ? 45.641 -12.239 -18.267 0.60 25.87 ?  3   VAL   B HG23 1 
ATOM   3937 N N    . ASN   B 1 4   ? 46.473 -15.495 -17.554 1.00 15.94 ?  4   ASN   B N    1 
ATOM   3938 C CA   . ASN   B 1 4   ? 45.341 -16.413 -17.432 1.00 14.93 ?  4   ASN   B CA   1 
ATOM   3939 C C    . ASN   B 1 4   ? 45.281 -17.378 -18.615 1.00 15.14 ?  4   ASN   B C    1 
ATOM   3940 O O    . ASN   B 1 4   ? 44.215 -17.641 -19.171 1.00 16.34 ?  4   ASN   B O    1 
ATOM   3941 C CB   . ASN   B 1 4   ? 44.017 -15.659 -17.264 1.00 14.35 ?  4   ASN   B CB   1 
ATOM   3942 C CG   . ASN   B 1 4   ? 43.975 -14.841 -15.991 1.00 13.46 ?  4   ASN   B CG   1 
ATOM   3943 O OD1  . ASN   B 1 4   ? 44.257 -15.350 -14.911 1.00 12.94 ?  4   ASN   B OD1  1 
ATOM   3944 N ND2  . ASN   B 1 4   ? 43.636 -13.560 -16.112 1.00 14.49 ?  4   ASN   B ND2  1 
ATOM   3945 H H    A ASN   B 1 4   ? 46.968 -15.449 -16.856 0.40 19.10 ?  4   ASN   B H    1 
ATOM   3946 H H    B ASN   B 1 4   ? 47.005 -15.505 -16.882 0.60 19.10 ?  4   ASN   B H    1 
ATOM   3947 H HA   . ASN   B 1 4   ? 45.477 -16.945 -16.631 1.00 17.90 ?  4   ASN   B HA   1 
ATOM   3948 H HB2  . ASN   B 1 4   ? 43.899 -15.057 -18.011 1.00 17.19 ?  4   ASN   B HB2  1 
ATOM   3949 H HB3  . ASN   B 1 4   ? 43.293 -16.303 -17.233 1.00 17.19 ?  4   ASN   B HB3  1 
ATOM   3950 H HD21 . ASN   B 1 4   ? 43.604 -13.055 -15.413 1.00 17.36 ?  4   ASN   B HD21 1 
ATOM   3951 H HD22 . ASN   B 1 4   ? 43.452 -13.235 -16.884 1.00 17.36 ?  4   ASN   B HD22 1 
ATOM   3952 N N    . SER   B 1 5   ? 46.439 -17.910 -19.007 1.00 16.15 ?  5   SER   B N    1 
ATOM   3953 C CA   . SER   B 1 5   ? 46.525 -18.835 -20.138 1.00 18.86 ?  5   SER   B CA   1 
ATOM   3954 C C    . SER   B 1 5   ? 46.524 -20.266 -19.608 1.00 19.84 ?  5   SER   B C    1 
ATOM   3955 O O    . SER   B 1 5   ? 47.545 -20.948 -19.560 1.00 21.86 ?  5   SER   B O    1 
ATOM   3956 C CB   . SER   B 1 5   ? 47.770 -18.546 -20.978 1.00 21.07 ?  5   SER   B CB   1 
ATOM   3957 O OG   . SER   B 1 5   ? 48.960 -18.826 -20.257 1.00 24.19 ?  5   SER   B OG   1 
ATOM   3958 H H    . SER   B 1 5   ? 47.200 -17.750 -18.631 1.00 19.35 ?  5   SER   B H    1 
ATOM   3959 H HA   . SER   B 1 5   ? 45.750 -18.721 -20.707 1.00 22.61 ?  5   SER   B HA   1 
ATOM   3960 H HB2  . SER   B 1 5   ? 47.749 -19.097 -21.780 1.00 25.26 ?  5   SER   B HB2  1 
ATOM   3961 H HB3  . SER   B 1 5   ? 47.760 -17.609 -21.228 1.00 25.26 ?  5   SER   B HB3  1 
ATOM   3962 H HG   . SER   B 1 5   ? 49.001 -19.645 -20.080 1.00 29.01 ?  5   SER   B HG   1 
ATOM   3963 N N    . PHE   B 1 6   ? 45.342 -20.697 -19.182 1.00 19.86 ?  6   PHE   B N    1 
ATOM   3964 C CA   . PHE   B 1 6   ? 45.165 -22.041 -18.654 1.00 19.53 ?  6   PHE   B CA   1 
ATOM   3965 C C    . PHE   B 1 6   ? 45.103 -23.027 -19.811 1.00 22.75 ?  6   PHE   B C    1 
ATOM   3966 O O    . PHE   B 1 6   ? 44.421 -22.780 -20.810 1.00 24.53 ?  6   PHE   B O    1 
ATOM   3967 C CB   . PHE   B 1 6   ? 43.879 -22.107 -17.828 1.00 17.89 ?  6   PHE   B CB   1 
ATOM   3968 C CG   . PHE   B 1 6   ? 43.894 -21.226 -16.606 1.00 16.04 ?  6   PHE   B CG   1 
ATOM   3969 C CD1  . PHE   B 1 6   ? 44.395 -21.701 -15.409 1.00 14.77 ?  6   PHE   B CD1  1 
ATOM   3970 C CD2  . PHE   B 1 6   ? 43.407 -19.927 -16.656 1.00 15.52 ?  6   PHE   B CD2  1 
ATOM   3971 C CE1  . PHE   B 1 6   ? 44.412 -20.897 -14.276 1.00 14.33 ?  6   PHE   B CE1  1 
ATOM   3972 C CE2  . PHE   B 1 6   ? 43.425 -19.116 -15.532 1.00 15.44 ?  6   PHE   B CE2  1 
ATOM   3973 C CZ   . PHE   B 1 6   ? 43.930 -19.594 -14.342 1.00 14.26 ?  6   PHE   B CZ   1 
ATOM   3974 H H    . PHE   B 1 6   ? 44.619 -20.226 -19.188 1.00 23.81 ?  6   PHE   B H    1 
ATOM   3975 H HA   . PHE   B 1 6   ? 45.913 -22.274 -18.083 1.00 23.41 ?  6   PHE   B HA   1 
ATOM   3976 H HB2  . PHE   B 1 6   ? 43.133 -21.829 -18.380 1.00 21.44 ?  6   PHE   B HB2  1 
ATOM   3977 H HB3  . PHE   B 1 6   ? 43.744 -23.021 -17.527 1.00 21.44 ?  6   PHE   B HB3  1 
ATOM   3978 H HD1  . PHE   B 1 6   ? 44.729 -22.567 -15.358 1.00 17.70 ?  6   PHE   B HD1  1 
ATOM   3979 H HD2  . PHE   B 1 6   ? 43.067 -19.598 -17.457 1.00 18.60 ?  6   PHE   B HD2  1 
ATOM   3980 H HE1  . PHE   B 1 6   ? 44.761 -21.221 -13.475 1.00 17.17 ?  6   PHE   B HE1  1 
ATOM   3981 H HE2  . PHE   B 1 6   ? 43.094 -18.243 -15.580 1.00 18.50 ?  6   PHE   B HE2  1 
ATOM   3982 H HZ   . PHE   B 1 6   ? 43.940 -19.050 -13.587 1.00 17.09 ?  6   PHE   B HZ   1 
ATOM   3983 N N    A SER   B 1 7   ? 45.815 -24.144 -19.681 0.40 23.06 ?  7   SER   B N    1 
ATOM   3984 N N    B SER   B 1 7   ? 45.829 -24.137 -19.676 0.60 22.86 ?  7   SER   B N    1 
ATOM   3985 C CA   A SER   B 1 7   ? 45.869 -25.140 -20.742 0.40 24.15 ?  7   SER   B CA   1 
ATOM   3986 C CA   B SER   B 1 7   ? 45.955 -25.132 -20.730 0.60 24.28 ?  7   SER   B CA   1 
ATOM   3987 C C    A SER   B 1 7   ? 45.835 -26.543 -20.151 0.40 23.42 ?  7   SER   B C    1 
ATOM   3988 C C    B SER   B 1 7   ? 45.898 -26.529 -20.128 0.60 23.49 ?  7   SER   B C    1 
ATOM   3989 O O    A SER   B 1 7   ? 46.397 -26.794 -19.081 0.40 23.86 ?  7   SER   B O    1 
ATOM   3990 O O    B SER   B 1 7   ? 46.472 -26.783 -19.066 0.60 24.28 ?  7   SER   B O    1 
ATOM   3991 C CB   A SER   B 1 7   ? 47.129 -24.957 -21.604 0.40 25.88 ?  7   SER   B CB   1 
ATOM   3992 C CB   B SER   B 1 7   ? 47.278 -24.947 -21.489 0.60 26.47 ?  7   SER   B CB   1 
ATOM   3993 O OG   A SER   B 1 7   ? 47.081 -25.786 -22.754 0.40 27.23 ?  7   SER   B OG   1 
ATOM   3994 O OG   B SER   B 1 7   ? 47.394 -25.874 -22.554 0.60 28.31 ?  7   SER   B OG   1 
ATOM   3995 H H    A SER   B 1 7   ? 46.280 -24.342 -18.986 0.40 27.65 ?  7   SER   B H    1 
ATOM   3996 H H    B SER   B 1 7   ? 46.268 -24.333 -18.964 0.60 27.41 ?  7   SER   B H    1 
ATOM   3997 H HA   A SER   B 1 7   ? 45.097 -25.036 -21.318 0.40 28.95 ?  7   SER   B HA   1 
ATOM   3998 H HA   B SER   B 1 7   ? 45.224 -25.036 -21.359 0.60 29.11 ?  7   SER   B HA   1 
ATOM   3999 H HB2  A SER   B 1 7   ? 47.189 -24.028 -21.888 0.40 31.03 ?  7   SER   B HB2  1 
ATOM   4000 H HB2  B SER   B 1 7   ? 47.315 -24.042 -21.845 0.60 31.74 ?  7   SER   B HB2  1 
ATOM   4001 H HB3  A SER   B 1 7   ? 47.910 -25.190 -21.079 0.40 31.03 ?  7   SER   B HB3  1 
ATOM   4002 H HB3  B SER   B 1 7   ? 48.016 -25.087 -20.876 0.60 31.74 ?  7   SER   B HB3  1 
ATOM   4003 H HG   A SER   B 1 7   ? 47.775 -25.675 -23.217 0.40 32.65 ?  7   SER   B HG   1 
ATOM   4004 H HG   B SER   B 1 7   ? 48.116 -25.750 -22.966 0.60 33.95 ?  7   SER   B HG   1 
ATOM   4005 N N    A GLY   B 1 8   ? 45.166 -27.451 -20.858 0.40 22.96 ?  8   GLY   B N    1 
ATOM   4006 N N    B GLY   B 1 8   ? 45.200 -27.432 -20.813 0.60 23.13 ?  8   GLY   B N    1 
ATOM   4007 C CA   A GLY   B 1 8   ? 45.123 -28.846 -20.471 0.40 22.28 ?  8   GLY   B CA   1 
ATOM   4008 C CA   B GLY   B 1 8   ? 45.173 -28.821 -20.406 0.60 22.39 ?  8   GLY   B CA   1 
ATOM   4009 C C    A GLY   B 1 8   ? 44.159 -29.187 -19.359 0.40 21.45 ?  8   GLY   B C    1 
ATOM   4010 C C    B GLY   B 1 8   ? 44.224 -29.140 -19.278 0.60 21.47 ?  8   GLY   B C    1 
ATOM   4011 O O    A GLY   B 1 8   ? 44.257 -30.279 -18.787 0.40 22.09 ?  8   GLY   B O    1 
ATOM   4012 O O    B GLY   B 1 8   ? 44.399 -30.168 -18.612 0.60 22.44 ?  8   GLY   B O    1 
ATOM   4013 H H    A GLY   B 1 8   ? 44.739 -27.273 -21.577 0.40 27.53 ?  8   GLY   B H    1 
ATOM   4014 H H    B GLY   B 1 8   ? 44.737 -27.256 -21.513 0.60 27.73 ?  8   GLY   B H    1 
ATOM   4015 H HA2  A GLY   B 1 8   ? 44.876 -29.372 -21.249 0.40 26.71 ?  8   GLY   B HA2  1 
ATOM   4016 H HA2  B GLY   B 1 8   ? 44.926 -29.364 -21.170 0.60 26.85 ?  8   GLY   B HA2  1 
ATOM   4017 H HA3  A GLY   B 1 8   ? 46.006 -29.124 -20.191 0.40 26.71 ?  8   GLY   B HA3  1 
ATOM   4018 H HA3  B GLY   B 1 8   ? 46.062 -29.085 -20.125 0.60 26.85 ?  8   GLY   B HA3  1 
ATOM   4019 N N    . TYR   B 1 9   ? 43.217 -28.303 -19.042 1.00 20.34 ?  9   TYR   B N    1 
ATOM   4020 C CA   . TYR   B 1 9   ? 42.248 -28.569 -17.991 1.00 18.14 ?  9   TYR   B CA   1 
ATOM   4021 C C    . TYR   B 1 9   ? 41.064 -29.355 -18.524 1.00 17.79 ?  9   TYR   B C    1 
ATOM   4022 O O    . TYR   B 1 9   ? 40.662 -29.219 -19.683 1.00 19.82 ?  9   TYR   B O    1 
ATOM   4023 C CB   . TYR   B 1 9   ? 41.745 -27.275 -17.354 1.00 17.66 ?  9   TYR   B CB   1 
ATOM   4024 C CG   . TYR   B 1 9   ? 42.762 -26.650 -16.432 1.00 17.19 ?  9   TYR   B CG   1 
ATOM   4025 C CD1  . TYR   B 1 9   ? 43.873 -25.993 -16.942 1.00 17.85 ?  9   TYR   B CD1  1 
ATOM   4026 C CD2  . TYR   B 1 9   ? 42.624 -26.733 -15.056 1.00 16.53 ?  9   TYR   B CD2  1 
ATOM   4027 C CE1  . TYR   B 1 9   ? 44.820 -25.434 -16.104 1.00 17.98 ?  9   TYR   B CE1  1 
ATOM   4028 C CE2  . TYR   B 1 9   ? 43.563 -26.182 -14.213 1.00 16.81 ?  9   TYR   B CE2  1 
ATOM   4029 C CZ   . TYR   B 1 9   ? 44.661 -25.531 -14.742 1.00 17.95 ?  9   TYR   B CZ   1 
ATOM   4030 O OH   . TYR   B 1 9   ? 45.599 -24.989 -13.903 1.00 18.57 ?  9   TYR   B OH   1 
ATOM   4031 H H    A TYR   B 1 9   ? 43.108 -27.543 -19.432 0.40 24.38 ?  9   TYR   B H    1 
ATOM   4032 H H    B TYR   B 1 9   ? 43.066 -27.579 -19.484 0.60 24.38 ?  9   TYR   B H    1 
ATOM   4033 H HA   . TYR   B 1 9   ? 42.667 -29.096 -17.296 1.00 21.75 ?  9   TYR   B HA   1 
ATOM   4034 H HB2  . TYR   B 1 9   ? 41.530 -26.631 -18.049 1.00 21.16 ?  9   TYR   B HB2  1 
ATOM   4035 H HB3  . TYR   B 1 9   ? 40.956 -27.477 -16.831 1.00 21.16 ?  9   TYR   B HB3  1 
ATOM   4036 H HD1  . TYR   B 1 9   ? 43.984 -25.932 -17.865 1.00 21.39 ?  9   TYR   B HD1  1 
ATOM   4037 H HD2  . TYR   B 1 9   ? 41.886 -27.179 -14.697 1.00 19.81 ?  9   TYR   B HD2  1 
ATOM   4038 H HE1  . TYR   B 1 9   ? 45.556 -25.000 -16.461 1.00 21.55 ?  9   TYR   B HE1  1 
ATOM   4039 H HE2  . TYR   B 1 9   ? 43.449 -26.251 -13.292 1.00 20.15 ?  9   TYR   B HE2  1 
ATOM   4040 H HH   . TYR   B 1 9   ? 46.199 -24.624 -14.355 1.00 22.26 ?  9   TYR   B HH   1 
ATOM   4041 N N    . LEU   B 1 10  ? 40.514 -30.189 -17.655 1.00 15.95 ?  10  LEU   B N    1 
ATOM   4042 C CA   . LEU   B 1 10  ? 39.310 -30.949 -17.933 1.00 15.76 ?  10  LEU   B CA   1 
ATOM   4043 C C    . LEU   B 1 10  ? 38.123 -30.180 -17.369 1.00 15.04 ?  10  LEU   B C    1 
ATOM   4044 O O    . LEU   B 1 10  ? 38.139 -29.764 -16.208 1.00 14.74 ?  10  LEU   B O    1 
ATOM   4045 C CB   . LEU   B 1 10  ? 39.422 -32.327 -17.279 1.00 16.66 ?  10  LEU   B CB   1 
ATOM   4046 C CG   . LEU   B 1 10  ? 38.278 -33.277 -17.609 1.00 18.33 ?  10  LEU   B CG   1 
ATOM   4047 C CD1  . LEU   B 1 10  ? 38.432 -33.817 -19.022 1.00 19.76 ?  10  LEU   B CD1  1 
ATOM   4048 C CD2  . LEU   B 1 10  ? 38.187 -34.402 -16.593 1.00 19.53 ?  10  LEU   B CD2  1 
ATOM   4049 H H    . LEU   B 1 10  ? 40.826 -30.328 -16.861 1.00 19.11 ?  10  LEU   B H    1 
ATOM   4050 H HA   . LEU   B 1 10  ? 39.193 -31.061 -18.886 1.00 18.88 ?  10  LEU   B HA   1 
ATOM   4051 H HB2  . LEU   B 1 10  ? 40.249 -32.746 -17.575 1.00 19.96 ?  10  LEU   B HB2  1 
ATOM   4052 H HB3  . LEU   B 1 10  ? 39.446 -32.217 -16.314 1.00 19.96 ?  10  LEU   B HB3  1 
ATOM   4053 H HG   . LEU   B 1 10  ? 37.446 -32.786 -17.572 1.00 21.97 ?  10  LEU   B HG   1 
ATOM   4054 H HD11 . LEU   B 1 10  ? 37.711 -34.443 -19.199 1.00 23.69 ?  10  LEU   B HD11 1 
ATOM   4055 H HD12 . LEU   B 1 10  ? 38.391 -33.079 -19.647 1.00 23.69 ?  10  LEU   B HD12 1 
ATOM   4056 H HD13 . LEU   B 1 10  ? 39.287 -34.269 -19.096 1.00 23.69 ?  10  LEU   B HD13 1 
ATOM   4057 H HD21 . LEU   B 1 10  ? 37.452 -34.985 -16.838 1.00 23.41 ?  10  LEU   B HD21 1 
ATOM   4058 H HD22 . LEU   B 1 10  ? 39.019 -34.895 -16.592 1.00 23.41 ?  10  LEU   B HD22 1 
ATOM   4059 H HD23 . LEU   B 1 10  ? 38.025 -34.017 -15.716 1.00 23.41 ?  10  LEU   B HD23 1 
ATOM   4060 N N    . LYS   B 1 11  ? 37.094 -30.003 -18.186 1.00 16.21 ?  11  LYS   B N    1 
ATOM   4061 C CA   . LYS   B 1 11  ? 35.906 -29.269 -17.775 1.00 17.70 ?  11  LYS   B CA   1 
ATOM   4062 C C    . LYS   B 1 11  ? 34.989 -30.186 -16.973 1.00 17.08 ?  11  LYS   B C    1 
ATOM   4063 O O    . LYS   B 1 11  ? 34.566 -31.233 -17.471 1.00 19.26 ?  11  LYS   B O    1 
ATOM   4064 C CB   . LYS   B 1 11  ? 35.195 -28.747 -19.022 1.00 21.32 ?  11  LYS   B CB   1 
ATOM   4065 C CG   . LYS   B 1 11  ? 34.006 -27.845 -18.762 1.00 24.67 ?  11  LYS   B CG   1 
ATOM   4066 C CD   . LYS   B 1 11  ? 33.282 -27.525 -20.067 1.00 27.78 ?  11  LYS   B CD   1 
ATOM   4067 C CE   . LYS   B 1 11  ? 32.249 -26.428 -19.883 1.00 29.98 ?  11  LYS   B CE   1 
ATOM   4068 N NZ   . LYS   B 1 11  ? 32.883 -25.121 -19.558 1.00 31.35 ?  11  LYS   B NZ   1 
ATOM   4069 H H    . LYS   B 1 11  ? 37.049 -30.318 -18.984 1.00 19.43 ?  11  LYS   B H    1 
ATOM   4070 H HA   . LYS   B 1 11  ? 36.161 -28.522 -17.217 1.00 21.21 ?  11  LYS   B HA   1 
ATOM   4071 H HB2  . LYS   B 1 11  ? 35.836 -28.241 -19.546 1.00 25.56 ?  11  LYS   B HB2  1 
ATOM   4072 H HB3  . LYS   B 1 11  ? 34.881 -29.505 -19.538 1.00 25.56 ?  11  LYS   B HB3  1 
ATOM   4073 H HG2  . LYS   B 1 11  ? 33.383 -28.293 -18.170 1.00 29.58 ?  11  LYS   B HG2  1 
ATOM   4074 H HG3  . LYS   B 1 11  ? 34.311 -27.014 -18.370 1.00 29.58 ?  11  LYS   B HG3  1 
ATOM   4075 H HD2  . LYS   B 1 11  ? 33.929 -27.228 -20.727 1.00 33.31 ?  11  LYS   B HD2  1 
ATOM   4076 H HD3  . LYS   B 1 11  ? 32.827 -28.323 -20.383 1.00 33.31 ?  11  LYS   B HD3  1 
ATOM   4077 H HE2  . LYS   B 1 11  ? 31.743 -26.324 -20.704 1.00 35.95 ?  11  LYS   B HE2  1 
ATOM   4078 H HE3  . LYS   B 1 11  ? 31.657 -26.668 -19.153 1.00 35.95 ?  11  LYS   B HE3  1 
ATOM   4079 H HZ1  . LYS   B 1 11  ? 32.261 -24.486 -19.508 1.00 37.60 ?  11  LYS   B HZ1  1 
ATOM   4080 H HZ2  . LYS   B 1 11  ? 33.307 -25.173 -18.778 1.00 37.60 ?  11  LYS   B HZ2  1 
ATOM   4081 H HZ3  . LYS   B 1 11  ? 33.468 -24.902 -20.193 1.00 37.60 ?  11  LYS   B HZ3  1 
ATOM   4082 N N    . LEU   B 1 12  ? 34.671 -29.790 -15.740 1.00 15.78 ?  12  LEU   B N    1 
ATOM   4083 C CA   . LEU   B 1 12  ? 33.708 -30.497 -14.903 1.00 15.53 ?  12  LEU   B CA   1 
ATOM   4084 C C    . LEU   B 1 12  ? 32.319 -29.886 -14.989 1.00 15.88 ?  12  LEU   B C    1 
ATOM   4085 O O    . LEU   B 1 12  ? 31.329 -30.600 -15.152 1.00 16.51 ?  12  LEU   B O    1 
ATOM   4086 C CB   . LEU   B 1 12  ? 34.172 -30.507 -13.442 1.00 15.25 ?  12  LEU   B CB   1 
ATOM   4087 C CG   . LEU   B 1 12  ? 35.503 -31.194 -13.161 1.00 15.11 ?  12  LEU   B CG   1 
ATOM   4088 C CD1  . LEU   B 1 12  ? 35.799 -31.156 -11.676 1.00 15.41 ?  12  LEU   B CD1  1 
ATOM   4089 C CD2  . LEU   B 1 12  ? 35.495 -32.621 -13.682 1.00 15.93 ?  12  LEU   B CD2  1 
ATOM   4090 H H    . LEU   B 1 12  ? 35.001 -29.092 -15.360 1.00 18.91 ?  12  LEU   B H    1 
ATOM   4091 H HA   . LEU   B 1 12  ? 33.642 -31.418 -15.207 1.00 18.61 ?  12  LEU   B HA   1 
ATOM   4092 H HB2  . LEU   B 1 12  ? 34.249 -29.590 -13.145 1.00 18.27 ?  12  LEU   B HB2  1 
ATOM   4093 H HB3  . LEU   B 1 12  ? 33.494 -30.961 -12.914 1.00 18.27 ?  12  LEU   B HB3  1 
ATOM   4094 H HG   . LEU   B 1 12  ? 36.208 -30.713 -13.620 1.00 18.10 ?  12  LEU   B HG   1 
ATOM   4095 H HD11 . LEU   B 1 12  ? 36.649 -31.597 -11.512 1.00 18.46 ?  12  LEU   B HD11 1 
ATOM   4096 H HD12 . LEU   B 1 12  ? 35.842 -30.234 -11.385 1.00 18.46 ?  12  LEU   B HD12 1 
ATOM   4097 H HD13 . LEU   B 1 12  ? 35.091 -31.623 -11.200 1.00 18.46 ?  12  LEU   B HD13 1 
ATOM   4098 H HD21 . LEU   B 1 12  ? 36.280 -33.082 -13.350 1.00 19.09 ?  12  LEU   B HD21 1 
ATOM   4099 H HD22 . LEU   B 1 12  ? 34.691 -33.066 -13.373 1.00 19.09 ?  12  LEU   B HD22 1 
ATOM   4100 H HD23 . LEU   B 1 12  ? 35.509 -32.602 -14.654 1.00 19.09 ?  12  LEU   B HD23 1 
ATOM   4101 N N    . THR   B 1 13  ? 32.232 -28.569 -14.870 1.00 15.98 ?  13  THR   B N    1 
ATOM   4102 C CA   . THR   B 1 13  ? 31.004 -27.819 -15.070 1.00 16.05 ?  13  THR   B CA   1 
ATOM   4103 C C    . THR   B 1 13  ? 31.331 -26.614 -15.947 1.00 17.66 ?  13  THR   B C    1 
ATOM   4104 O O    . THR   B 1 13  ? 32.473 -26.414 -16.376 1.00 18.66 ?  13  THR   B O    1 
ATOM   4105 C CB   . THR   B 1 13  ? 30.406 -27.356 -13.737 1.00 16.01 ?  13  THR   B CB   1 
ATOM   4106 O OG1  . THR   B 1 13  ? 31.251 -26.335 -13.186 1.00 15.60 ?  13  THR   B OG1  1 
ATOM   4107 C CG2  . THR   B 1 13  ? 30.290 -28.515 -12.751 1.00 16.70 ?  13  THR   B CG2  1 
ATOM   4108 H H    . THR   B 1 13  ? 32.900 -28.070 -14.655 1.00 19.15 ?  13  THR   B H    1 
ATOM   4109 H HA   . THR   B 1 13  ? 30.352 -28.373 -15.519 1.00 19.23 ?  13  THR   B HA   1 
ATOM   4110 H HB   . THR   B 1 13  ? 29.519 -26.989 -13.887 1.00 19.18 ?  13  THR   B HB   1 
ATOM   4111 H HG1  . THR   B 1 13  ? 30.935 -25.570 -13.357 1.00 18.69 ?  13  THR   B HG1  1 
ATOM   4112 H HG21 . THR   B 1 13  ? 29.760 -28.250 -11.982 1.00 20.01 ?  13  THR   B HG21 1 
ATOM   4113 H HG22 . THR   B 1 13  ? 29.859 -29.272 -13.181 1.00 20.01 ?  13  THR   B HG22 1 
ATOM   4114 H HG23 . THR   B 1 13  ? 31.170 -28.787 -12.447 1.00 20.01 ?  13  THR   B HG23 1 
ATOM   4115 N N    A ASP   B 1 14  ? 30.313 -25.789 -16.197 0.40 18.50 ?  14  ASP   B N    1 
ATOM   4116 N N    B ASP   B 1 14  ? 30.316 -25.789 -16.204 0.60 18.54 ?  14  ASP   B N    1 
ATOM   4117 C CA   A ASP   B 1 14  ? 30.508 -24.616 -17.040 0.40 19.74 ?  14  ASP   B CA   1 
ATOM   4118 C CA   B ASP   B 1 14  ? 30.518 -24.619 -17.051 0.60 20.03 ?  14  ASP   B CA   1 
ATOM   4119 C C    A ASP   B 1 14  ? 31.609 -23.707 -16.507 0.40 18.02 ?  14  ASP   B C    1 
ATOM   4120 C C    B ASP   B 1 14  ? 31.560 -23.658 -16.494 0.60 18.30 ?  14  ASP   B C    1 
ATOM   4121 O O    A ASP   B 1 14  ? 32.257 -23.003 -17.290 0.40 18.88 ?  14  ASP   B O    1 
ATOM   4122 O O    B ASP   B 1 14  ? 32.093 -22.843 -17.254 0.60 19.61 ?  14  ASP   B O    1 
ATOM   4123 C CB   A ASP   B 1 14  ? 29.193 -23.847 -17.177 0.40 22.55 ?  14  ASP   B CB   1 
ATOM   4124 C CB   B ASP   B 1 14  ? 29.201 -23.873 -17.255 0.60 23.18 ?  14  ASP   B CB   1 
ATOM   4125 C CG   A ASP   B 1 14  ? 28.208 -24.526 -18.106 0.40 25.06 ?  14  ASP   B CG   1 
ATOM   4126 C CG   B ASP   B 1 14  ? 28.321 -24.527 -18.299 0.60 26.16 ?  14  ASP   B CG   1 
ATOM   4127 O OD1  A ASP   B 1 14  ? 28.543 -25.587 -18.677 0.40 25.65 ?  14  ASP   B OD1  1 
ATOM   4128 O OD1  B ASP   B 1 14  ? 28.868 -25.199 -19.200 0.60 26.93 ?  14  ASP   B OD1  1 
ATOM   4129 O OD2  A ASP   B 1 14  ? 27.090 -23.991 -18.261 0.40 26.19 -1 14  ASP   B OD2  1 
ATOM   4130 O OD2  B ASP   B 1 14  ? 27.086 -24.370 -18.224 0.60 27.62 -1 14  ASP   B OD2  1 
ATOM   4131 H H    A ASP   B 1 14  ? 29.517 -25.882 -15.889 0.40 22.17 ?  14  ASP   B H    1 
ATOM   4132 H H    B ASP   B 1 14  ? 29.516 -25.883 -15.902 0.60 22.23 ?  14  ASP   B H    1 
ATOM   4133 H HA   A ASP   B 1 14  ? 30.776 -24.904 -17.924 0.40 23.66 ?  14  ASP   B HA   1 
ATOM   4134 H HA   B ASP   B 1 14  ? 30.825 -24.918 -17.920 0.60 24.01 ?  14  ASP   B HA   1 
ATOM   4135 H HB2  A ASP   B 1 14  ? 28.763 -23.787 -16.311 0.40 27.03 ?  14  ASP   B HB2  1 
ATOM   4136 H HB2  B ASP   B 1 14  ? 28.713 -23.853 -16.415 0.60 27.79 ?  14  ASP   B HB2  1 
ATOM   4137 H HB3  A ASP   B 1 14  ? 29.372 -22.961 -17.525 0.40 27.03 ?  14  ASP   B HB3  1 
ATOM   4138 H HB3  B ASP   B 1 14  ? 29.392 -22.966 -17.546 0.60 27.79 ?  14  ASP   B HB3  1 
ATOM   4139 N N    . ASN   B 1 15  ? 31.851 -23.718 -15.193 1.00 15.72 ?  15  ASN   B N    1 
ATOM   4140 C CA   . ASN   B 1 15  ? 32.808 -22.795 -14.591 1.00 13.77 ?  15  ASN   B CA   1 
ATOM   4141 C C    . ASN   B 1 15  ? 33.900 -23.449 -13.754 1.00 12.84 ?  15  ASN   B C    1 
ATOM   4142 O O    . ASN   B 1 15  ? 34.729 -22.718 -13.204 1.00 13.39 ?  15  ASN   B O    1 
ATOM   4143 C CB   . ASN   B 1 15  ? 32.088 -21.737 -13.736 1.00 13.64 ?  15  ASN   B CB   1 
ATOM   4144 C CG   . ASN   B 1 15  ? 31.457 -22.332 -12.496 1.00 13.76 ?  15  ASN   B CG   1 
ATOM   4145 O OD1  . ASN   B 1 15  ? 30.513 -23.125 -12.585 1.00 15.20 ?  15  ASN   B OD1  1 
ATOM   4146 N ND2  . ASN   B 1 15  ? 31.979 -21.985 -11.338 1.00 13.13 ?  15  ASN   B ND2  1 
ATOM   4147 H H    A ASN   B 1 15  ? 31.475 -24.255 -14.633 0.40 18.84 ?  15  ASN   B H    1 
ATOM   4148 H H    B ASN   B 1 15  ? 31.491 -24.270 -14.637 0.60 18.84 ?  15  ASN   B H    1 
ATOM   4149 H HA   . ASN   B 1 15  ? 33.259 -22.320 -15.299 1.00 16.50 ?  15  ASN   B HA   1 
ATOM   4150 H HB2  . ASN   B 1 15  ? 32.736 -21.062 -13.459 1.00 16.34 ?  15  ASN   B HB2  1 
ATOM   4151 H HB3  . ASN   B 1 15  ? 31.389 -21.319 -14.265 1.00 16.34 ?  15  ASN   B HB3  1 
ATOM   4152 H HD21 . ASN   B 1 15  ? 31.652 -22.294 -10.605 1.00 15.73 ?  15  ASN   B HD21 1 
ATOM   4153 H HD22 . ASN   B 1 15  ? 32.643 -21.430 -11.305 1.00 15.73 ?  15  ASN   B HD22 1 
ATOM   4154 N N    . VAL   B 1 16  ? 33.925 -24.775 -13.624 1.00 12.45 ?  16  VAL   B N    1 
ATOM   4155 C CA   . VAL   B 1 16  ? 34.922 -25.465 -12.813 1.00 12.50 ?  16  VAL   B CA   1 
ATOM   4156 C C    . VAL   B 1 16  ? 35.716 -26.403 -13.707 1.00 12.51 ?  16  VAL   B C    1 
ATOM   4157 O O    . VAL   B 1 16  ? 35.139 -27.268 -14.381 1.00 13.86 ?  16  VAL   B O    1 
ATOM   4158 C CB   . VAL   B 1 16  ? 34.291 -26.229 -11.635 1.00 13.01 ?  16  VAL   B CB   1 
ATOM   4159 C CG1  . VAL   B 1 16  ? 35.374 -26.952 -10.824 1.00 13.09 ?  16  VAL   B CG1  1 
ATOM   4160 C CG2  . VAL   B 1 16  ? 33.478 -25.284 -10.758 1.00 13.78 ?  16  VAL   B CG2  1 
ATOM   4161 H H    . VAL   B 1 16  ? 33.358 -25.309 -13.998 1.00 14.92 ?  16  VAL   B H    1 
ATOM   4162 H HA   . VAL   B 1 16  ? 35.536 -24.809 -12.443 1.00 14.98 ?  16  VAL   B HA   1 
ATOM   4163 H HB   . VAL   B 1 16  ? 33.691 -26.904 -11.988 1.00 15.59 ?  16  VAL   B HB   1 
ATOM   4164 H HG11 . VAL   B 1 16  ? 34.983 -27.263 -9.991  1.00 15.68 ?  16  VAL   B HG11 1 
ATOM   4165 H HG12 . VAL   B 1 16  ? 35.710 -27.701 -11.333 1.00 15.68 ?  16  VAL   B HG12 1 
ATOM   4166 H HG13 . VAL   B 1 16  ? 36.092 -26.326 -10.633 1.00 15.68 ?  16  VAL   B HG13 1 
ATOM   4167 H HG21 . VAL   B 1 16  ? 33.140 -25.777 -9.994  1.00 16.51 ?  16  VAL   B HG21 1 
ATOM   4168 H HG22 . VAL   B 1 16  ? 34.047 -24.559 -10.462 1.00 16.51 ?  16  VAL   B HG22 1 
ATOM   4169 H HG23 . VAL   B 1 16  ? 32.737 -24.933 -11.278 1.00 16.51 ?  16  VAL   B HG23 1 
ATOM   4170 N N    . TYR   B 1 17  ? 37.042 -26.244 -13.675 1.00 12.45 ?  17  TYR   B N    1 
ATOM   4171 C CA   . TYR   B 1 17  ? 37.986 -26.996 -14.486 1.00 12.95 ?  17  TYR   B CA   1 
ATOM   4172 C C    . TYR   B 1 17  ? 39.037 -27.609 -13.570 1.00 12.40 ?  17  TYR   B C    1 
ATOM   4173 O O    . TYR   B 1 17  ? 39.312 -27.076 -12.493 1.00 12.80 ?  17  TYR   B O    1 
ATOM   4174 C CB   . TYR   B 1 17  ? 38.691 -26.063 -15.483 1.00 14.93 ?  17  TYR   B CB   1 
ATOM   4175 C CG   . TYR   B 1 17  ? 37.761 -25.288 -16.382 1.00 17.66 ?  17  TYR   B CG   1 
ATOM   4176 C CD1  . TYR   B 1 17  ? 37.155 -24.109 -15.953 1.00 18.54 ?  17  TYR   B CD1  1 
ATOM   4177 C CD2  . TYR   B 1 17  ? 37.488 -25.732 -17.667 1.00 19.44 ?  17  TYR   B CD2  1 
ATOM   4178 C CE1  . TYR   B 1 17  ? 36.300 -23.401 -16.780 1.00 20.08 ?  17  TYR   B CE1  1 
ATOM   4179 C CE2  . TYR   B 1 17  ? 36.640 -25.030 -18.502 1.00 20.88 ?  17  TYR   B CE2  1 
ATOM   4180 C CZ   . TYR   B 1 17  ? 36.049 -23.870 -18.051 1.00 21.26 ?  17  TYR   B CZ   1 
ATOM   4181 O OH   . TYR   B 1 17  ? 35.208 -23.173 -18.881 1.00 23.24 ?  17  TYR   B OH   1 
ATOM   4182 H H    . TYR   B 1 17  ? 37.436 -25.667 -13.162 1.00 14.91 ?  17  TYR   B H    1 
ATOM   4183 H HA   . TYR   B 1 17  ? 37.525 -27.699 -14.970 1.00 15.52 ?  17  TYR   B HA   1 
ATOM   4184 H HB2  . TYR   B 1 17  ? 39.232 -25.427 -14.991 1.00 17.89 ?  17  TYR   B HB2  1 
ATOM   4185 H HB3  . TYR   B 1 17  ? 39.258 -26.602 -16.054 1.00 17.89 ?  17  TYR   B HB3  1 
ATOM   4186 H HD1  . TYR   B 1 17  ? 37.326 -23.793 -15.095 1.00 22.22 ?  17  TYR   B HD1  1 
ATOM   4187 H HD2  . TYR   B 1 17  ? 37.878 -26.516 -17.975 1.00 23.30 ?  17  TYR   B HD2  1 
ATOM   4188 H HE1  . TYR   B 1 17  ? 35.900 -22.612 -16.482 1.00 24.07 ?  17  TYR   B HE1  1 
ATOM   4189 H HE2  . TYR   B 1 17  ? 36.457 -25.343 -19.362 1.00 25.03 ?  17  TYR   B HE2  1 
ATOM   4190 H HH   . TYR   B 1 17  ? 35.130 -23.562 -19.623 1.00 27.86 ?  17  TYR   B HH   1 
ATOM   4191 N N    . ILE   B 1 18  ? 39.656 -28.713 -14.003 1.00 12.26 ?  18  ILE   B N    1 
ATOM   4192 C CA   . ILE   B 1 18  ? 40.592 -29.434 -13.143 1.00 12.09 ?  18  ILE   B CA   1 
ATOM   4193 C C    . ILE   B 1 18  ? 41.756 -29.984 -13.958 1.00 12.52 ?  18  ILE   B C    1 
ATOM   4194 O O    . ILE   B 1 18  ? 41.597 -30.397 -15.111 1.00 13.72 ?  18  ILE   B O    1 
ATOM   4195 C CB   . ILE   B 1 18  ? 39.842 -30.534 -12.346 1.00 12.68 ?  18  ILE   B CB   1 
ATOM   4196 C CG1  . ILE   B 1 18  ? 40.680 -31.076 -11.186 1.00 13.32 ?  18  ILE   B CG1  1 
ATOM   4197 C CG2  . ILE   B 1 18  ? 39.342 -31.654 -13.268 1.00 13.23 ?  18  ILE   B CG2  1 
ATOM   4198 C CD1  . ILE   B 1 18  ? 39.838 -31.834 -10.166 1.00 14.73 ?  18  ILE   B CD1  1 
ATOM   4199 H H    . ILE   B 1 18  ? 39.555 -29.059 -14.784 1.00 14.69 ?  18  ILE   B H    1 
ATOM   4200 H HA   . ILE   B 1 18  ? 40.955 -28.816 -12.493 1.00 14.49 ?  18  ILE   B HA   1 
ATOM   4201 H HB   . ILE   B 1 18  ? 39.053 -30.125 -11.956 1.00 15.19 ?  18  ILE   B HB   1 
ATOM   4202 H HG12 . ILE   B 1 18  ? 41.350 -31.679 -11.530 1.00 15.96 ?  18  ILE   B HG12 1 
ATOM   4203 H HG13 . ILE   B 1 18  ? 41.099 -30.329 -10.728 1.00 15.96 ?  18  ILE   B HG13 1 
ATOM   4204 H HG21 . ILE   B 1 18  ? 38.755 -32.242 -12.762 1.00 15.85 ?  18  ILE   B HG21 1 
ATOM   4205 H HG22 . ILE   B 1 18  ? 38.855 -31.258 -14.005 1.00 15.85 ?  18  ILE   B HG22 1 
ATOM   4206 H HG23 . ILE   B 1 18  ? 40.103 -32.154 -13.599 1.00 15.85 ?  18  ILE   B HG23 1 
ATOM   4207 H HD11 . ILE   B 1 18  ? 40.406 -32.108 -9.430  1.00 17.65 ?  18  ILE   B HD11 1 
ATOM   4208 H HD12 . ILE   B 1 18  ? 39.132 -31.252 -9.841  1.00 17.65 ?  18  ILE   B HD12 1 
ATOM   4209 H HD13 . ILE   B 1 18  ? 39.451 -32.614 -10.594 1.00 17.65 ?  18  ILE   B HD13 1 
ATOM   4210 N N    . LYS   B 1 19  ? 42.936 -30.010 -13.334 1.00 12.77 ?  19  LYS   B N    1 
ATOM   4211 C CA   . LYS   B 1 19  ? 44.147 -30.494 -13.982 1.00 13.49 ?  19  LYS   B CA   1 
ATOM   4212 C C    . LYS   B 1 19  ? 45.039 -31.168 -12.949 1.00 12.88 ?  19  LYS   B C    1 
ATOM   4213 O O    . LYS   B 1 19  ? 45.117 -30.730 -11.800 1.00 12.94 ?  19  LYS   B O    1 
ATOM   4214 C CB   . LYS   B 1 19  ? 44.921 -29.335 -14.628 1.00 14.99 ?  19  LYS   B CB   1 
ATOM   4215 C CG   . LYS   B 1 19  ? 46.145 -29.744 -15.432 1.00 16.41 ?  19  LYS   B CG   1 
ATOM   4216 C CD   . LYS   B 1 19  ? 46.868 -28.513 -15.970 1.00 18.32 ?  19  LYS   B CD   1 
ATOM   4217 C CE   . LYS   B 1 19  ? 48.036 -28.885 -16.866 1.00 20.18 ?  19  LYS   B CE   1 
ATOM   4218 N NZ   . LYS   B 1 19  ? 48.806 -27.689 -17.305 1.00 21.34 ?  19  LYS   B NZ   1 
ATOM   4219 H H    . LYS   B 1 19  ? 43.054 -29.745 -12.521 1.00 15.30 ?  19  LYS   B H    1 
ATOM   4220 H HA   . LYS   B 1 19  ? 43.912 -31.141 -14.668 1.00 16.17 ?  19  LYS   B HA   1 
ATOM   4221 H HB2  . LYS   B 1 19  ? 44.318 -28.866 -15.226 1.00 17.96 ?  19  LYS   B HB2  1 
ATOM   4222 H HB3  . LYS   B 1 19  ? 45.212 -28.735 -13.923 1.00 17.96 ?  19  LYS   B HB3  1 
ATOM   4223 H HG2  . LYS   B 1 19  ? 46.755 -30.237 -14.863 1.00 19.66 ?  19  LYS   B HG2  1 
ATOM   4224 H HG3  . LYS   B 1 19  ? 45.865 -30.292 -16.184 1.00 19.66 ?  19  LYS   B HG3  1 
ATOM   4225 H HD2  . LYS   B 1 19  ? 46.244 -27.978 -16.487 1.00 21.96 ?  19  LYS   B HD2  1 
ATOM   4226 H HD3  . LYS   B 1 19  ? 47.210 -27.995 -15.223 1.00 21.96 ?  19  LYS   B HD3  1 
ATOM   4227 H HE2  . LYS   B 1 19  ? 48.634 -29.474 -16.379 1.00 24.19 ?  19  LYS   B HE2  1 
ATOM   4228 H HE3  . LYS   B 1 19  ? 47.696 -29.338 -17.657 1.00 24.19 ?  19  LYS   B HE3  1 
ATOM   4229 H HZ1  . LYS   B 1 19  ? 49.438 -27.929 -17.883 1.00 25.59 ?  19  LYS   B HZ1  1 
ATOM   4230 H HZ2  . LYS   B 1 19  ? 48.261 -27.105 -17.698 1.00 25.59 ?  19  LYS   B HZ2  1 
ATOM   4231 H HZ3  . LYS   B 1 19  ? 49.188 -27.300 -16.602 1.00 25.59 ?  19  LYS   B HZ3  1 
ATOM   4232 N N    . ASN   B 1 20  ? 45.731 -32.222 -13.376 1.00 13.72 ?  20  ASN   B N    1 
ATOM   4233 C CA   . ASN   B 1 20  ? 46.766 -32.852 -12.558 1.00 14.79 ?  20  ASN   B CA   1 
ATOM   4234 C C    . ASN   B 1 20  ? 48.037 -32.032 -12.745 1.00 15.51 ?  20  ASN   B C    1 
ATOM   4235 O O    . ASN   B 1 20  ? 48.684 -32.106 -13.792 1.00 17.28 ?  20  ASN   B O    1 
ATOM   4236 C CB   . ASN   B 1 20  ? 46.945 -34.302 -12.999 1.00 16.11 ?  20  ASN   B CB   1 
ATOM   4237 C CG   . ASN   B 1 20  ? 48.095 -35.014 -12.304 1.00 17.59 ?  20  ASN   B CG   1 
ATOM   4238 O OD1  . ASN   B 1 20  ? 48.737 -35.888 -12.896 1.00 19.88 ?  20  ASN   B OD1  1 
ATOM   4239 N ND2  . ASN   B 1 20  ? 48.344 -34.674 -11.047 1.00 17.10 ?  20  ASN   B ND2  1 
ATOM   4240 H H    . ASN   B 1 20  ? 45.624 -32.590 -14.145 1.00 16.43 ?  20  ASN   B H    1 
ATOM   4241 H HA   . ASN   B 1 20  ? 46.498 -32.832 -11.626 1.00 17.72 ?  20  ASN   B HA   1 
ATOM   4242 H HB2  . ASN   B 1 20  ? 46.132 -34.791 -12.800 1.00 19.31 ?  20  ASN   B HB2  1 
ATOM   4243 H HB3  . ASN   B 1 20  ? 47.116 -34.317 -13.952 1.00 19.31 ?  20  ASN   B HB3  1 
ATOM   4244 H HD21 . ASN   B 1 20  ? 48.990 -35.044 -10.620 1.00 20.49 ?  20  ASN   B HD21 1 
ATOM   4245 H HD22 . ASN   B 1 20  ? 47.870 -34.065 -10.656 1.00 20.49 ?  20  ASN   B HD22 1 
ATOM   4246 N N    . ALA   B 1 21  ? 48.389 -31.228 -11.739 1.00 15.37 ?  21  ALA   B N    1 
ATOM   4247 C CA   . ALA   B 1 21  ? 49.489 -30.285 -11.887 1.00 16.21 ?  21  ALA   B CA   1 
ATOM   4248 C C    . ALA   B 1 21  ? 49.948 -29.799 -10.521 1.00 15.15 ?  21  ALA   B C    1 
ATOM   4249 O O    . ALA   B 1 21  ? 49.202 -29.831 -9.539  1.00 15.11 ?  21  ALA   B O    1 
ATOM   4250 C CB   . ALA   B 1 21  ? 49.081 -29.094 -12.756 1.00 17.53 ?  21  ALA   B CB   1 
ATOM   4251 H H    . ALA   B 1 21  ? 48.005 -31.215 -10.961 1.00 18.42 ?  21  ALA   B H    1 
ATOM   4252 H HA   . ALA   B 1 21  ? 50.233 -30.738 -12.311 1.00 19.43 ?  21  ALA   B HA   1 
ATOM   4253 H HB1  . ALA   B 1 21  ? 49.861 -28.545 -12.903 1.00 21.01 ?  21  ALA   B HB1  1 
ATOM   4254 H HB2  . ALA   B 1 21  ? 48.742 -29.431 -13.598 1.00 21.01 ?  21  ALA   B HB2  1 
ATOM   4255 H HB3  . ALA   B 1 21  ? 48.391 -28.592 -12.296 1.00 21.01 ?  21  ALA   B HB3  1 
ATOM   4256 N N    . ASP   B 1 22  ? 51.203 -29.345 -10.496 1.00 14.94 ?  22  ASP   B N    1 
ATOM   4257 C CA   . ASP   B 1 22  ? 51.810 -28.654 -9.364  1.00 14.54 ?  22  ASP   B CA   1 
ATOM   4258 C C    . ASP   B 1 22  ? 51.408 -27.185 -9.456  1.00 13.41 ?  22  ASP   B C    1 
ATOM   4259 O O    . ASP   B 1 22  ? 51.731 -26.517 -10.442 1.00 13.65 ?  22  ASP   B O    1 
ATOM   4260 C CB   . ASP   B 1 22  ? 53.325 -28.830 -9.515  1.00 16.01 ?  22  ASP   B CB   1 
ATOM   4261 C CG   . ASP   B 1 22  ? 54.147 -28.079 -8.478  1.00 17.48 ?  22  ASP   B CG   1 
ATOM   4262 O OD1  . ASP   B 1 22  ? 53.779 -26.964 -8.071  1.00 17.81 ?  22  ASP   B OD1  1 
ATOM   4263 O OD2  . ASP   B 1 22  ? 55.220 -28.598 -8.100  1.00 19.86 -1 22  ASP   B OD2  1 
ATOM   4264 H H    . ASP   B 1 22  ? 51.748 -29.432 -11.158 1.00 17.90 ?  22  ASP   B H    1 
ATOM   4265 H HA   . ASP   B 1 22  ? 51.515 -29.032 -8.520  1.00 17.42 ?  22  ASP   B HA   1 
ATOM   4266 H HB2  . ASP   B 1 22  ? 53.548 -29.766 -9.442  1.00 19.18 ?  22  ASP   B HB2  1 
ATOM   4267 H HB3  . ASP   B 1 22  ? 53.596 -28.490 -10.384 1.00 19.18 ?  22  ASP   B HB3  1 
ATOM   4268 N N    . ILE   B 1 23  ? 50.687 -26.688 -8.445  1.00 12.93 ?  23  ILE   B N    1 
ATOM   4269 C CA   . ILE   B 1 23  ? 50.100 -25.349 -8.522  1.00 12.45 ?  23  ILE   B CA   1 
ATOM   4270 C C    . ILE   B 1 23  ? 51.156 -24.260 -8.662  1.00 12.18 ?  23  ILE   B C    1 
ATOM   4271 O O    . ILE   B 1 23  ? 50.885 -23.218 -9.269  1.00 11.77 ?  23  ILE   B O    1 
ATOM   4272 C CB   . ILE   B 1 23  ? 49.153 -25.102 -7.331  1.00 12.52 ?  23  ILE   B CB   1 
ATOM   4273 C CG1  . ILE   B 1 23  ? 48.331 -23.830 -7.541  1.00 13.42 ?  23  ILE   B CG1  1 
ATOM   4274 C CG2  . ILE   B 1 23  ? 49.910 -25.079 -6.020  1.00 13.90 ?  23  ILE   B CG2  1 
ATOM   4275 C CD1  . ILE   B 1 23  ? 47.203 -23.662 -6.539  1.00 14.36 ?  23  ILE   B CD1  1 
ATOM   4276 H H    . ILE   B 1 23  ? 50.529 -27.104 -7.709  1.00 15.49 ?  23  ILE   B H    1 
ATOM   4277 H HA   . ILE   B 1 23  ? 49.557 -25.313 -9.326  1.00 14.92 ?  23  ILE   B HA   1 
ATOM   4278 H HB   . ILE   B 1 23  ? 48.527 -25.845 -7.300  1.00 15.00 ?  23  ILE   B HB   1 
ATOM   4279 H HG12 . ILE   B 1 23  ? 48.921 -23.059 -7.460  1.00 16.07 ?  23  ILE   B HG12 1 
ATOM   4280 H HG13 . ILE   B 1 23  ? 47.942 -23.846 -8.432  1.00 16.07 ?  23  ILE   B HG13 1 
ATOM   4281 H HG21 . ILE   B 1 23  ? 49.272 -25.061 -5.289  1.00 16.65 ?  23  ILE   B HG21 1 
ATOM   4282 H HG22 . ILE   B 1 23  ? 50.456 -25.879 -5.959  1.00 16.65 ?  23  ILE   B HG22 1 
ATOM   4283 H HG23 . ILE   B 1 23  ? 50.471 -24.291 -5.993  1.00 16.65 ?  23  ILE   B HG23 1 
ATOM   4284 H HD11 . ILE   B 1 23  ? 46.680 -22.882 -6.781  1.00 17.21 ?  23  ILE   B HD11 1 
ATOM   4285 H HD12 . ILE   B 1 23  ? 46.646 -24.455 -6.563  1.00 17.21 ?  23  ILE   B HD12 1 
ATOM   4286 H HD13 . ILE   B 1 23  ? 47.582 -23.548 -5.655  1.00 17.21 ?  23  ILE   B HD13 1 
ATOM   4287 N N    . VAL   B 1 24  ? 52.349 -24.457 -8.091  1.00 12.60 ?  24  VAL   B N    1 
ATOM   4288 C CA   . VAL   B 1 24  ? 53.428 -23.481 -8.260  1.00 12.96 ?  24  VAL   B CA   1 
ATOM   4289 C C    . VAL   B 1 24  ? 53.879 -23.433 -9.712  1.00 13.15 ?  24  VAL   B C    1 
ATOM   4290 O O    . VAL   B 1 24  ? 54.017 -22.355 -10.307 1.00 13.78 ?  24  VAL   B O    1 
ATOM   4291 C CB   . VAL   B 1 24  ? 54.605 -23.803 -7.320  1.00 13.92 ?  24  VAL   B CB   1 
ATOM   4292 C CG1  . VAL   B 1 24  ? 55.816 -22.936 -7.662  1.00 14.40 ?  24  VAL   B CG1  1 
ATOM   4293 C CG2  . VAL   B 1 24  ? 54.199 -23.607 -5.882  1.00 15.06 ?  24  VAL   B CG2  1 
ATOM   4294 H H    . VAL   B 1 24  ? 52.553 -25.140 -7.605  1.00 15.09 ?  24  VAL   B H    1 
ATOM   4295 H HA   . VAL   B 1 24  ? 53.092 -22.605 -8.021  1.00 15.53 ?  24  VAL   B HA   1 
ATOM   4296 H HB   . VAL   B 1 24  ? 54.856 -24.734 -7.431  1.00 16.67 ?  24  VAL   B HB   1 
ATOM   4297 H HG11 . VAL   B 1 24  ? 56.409 -22.912 -6.895  1.00 17.26 ?  24  VAL   B HG11 1 
ATOM   4298 H HG12 . VAL   B 1 24  ? 56.275 -23.330 -8.420  1.00 17.26 ?  24  VAL   B HG12 1 
ATOM   4299 H HG13 . VAL   B 1 24  ? 55.513 -22.044 -7.877  1.00 17.26 ?  24  VAL   B HG13 1 
ATOM   4300 H HG21 . VAL   B 1 24  ? 54.924 -23.893 -5.305  1.00 18.04 ?  24  VAL   B HG21 1 
ATOM   4301 H HG22 . VAL   B 1 24  ? 54.012 -22.666 -5.733  1.00 18.04 ?  24  VAL   B HG22 1 
ATOM   4302 H HG23 . VAL   B 1 24  ? 53.405 -24.134 -5.699  1.00 18.04 ?  24  VAL   B HG23 1 
ATOM   4303 N N    . GLU   B 1 25  ? 54.140 -24.605 -10.298 1.00 14.41 ?  25  GLU   B N    1 
ATOM   4304 C CA   . GLU   B 1 25  ? 54.528 -24.649 -11.701 1.00 15.60 ?  25  GLU   B CA   1 
ATOM   4305 C C    . GLU   B 1 25  ? 53.425 -24.097 -12.590 1.00 14.49 ?  25  GLU   B C    1 
ATOM   4306 O O    . GLU   B 1 25  ? 53.696 -23.378 -13.559 1.00 15.34 ?  25  GLU   B O    1 
ATOM   4307 C CB   . GLU   B 1 25  ? 54.898 -26.077 -12.094 1.00 19.53 ?  25  GLU   B CB   1 
ATOM   4308 C CG   . GLU   B 1 25  ? 56.183 -26.551 -11.441 1.00 25.32 ?  25  GLU   B CG   1 
ATOM   4309 C CD   . GLU   B 1 25  ? 57.313 -25.534 -11.538 1.00 30.89 ?  25  GLU   B CD   1 
ATOM   4310 O OE1  . GLU   B 1 25  ? 57.657 -25.123 -12.668 1.00 32.43 ?  25  GLU   B OE1  1 
ATOM   4311 O OE2  . GLU   B 1 25  ? 57.844 -25.128 -10.479 1.00 32.72 -1 25  GLU   B OE2  1 
ATOM   4312 H H    . GLU   B 1 25  ? 54.088 -25.373 -9.912  1.00 17.27 ?  25  GLU   B H    1 
ATOM   4313 H HA   . GLU   B 1 25  ? 55.292 -24.074 -11.828 1.00 18.69 ?  25  GLU   B HA   1 
ATOM   4314 H HB2  . GLU   B 1 25  ? 54.183 -26.678 -11.817 1.00 23.41 ?  25  GLU   B HB2  1 
ATOM   4315 H HB3  . GLU   B 1 25  ? 55.009 -26.122 -13.056 1.00 23.41 ?  25  GLU   B HB3  1 
ATOM   4316 H HG2  . GLU   B 1 25  ? 56.022 -26.711 -10.503 1.00 30.36 ?  25  GLU   B HG2  1 
ATOM   4317 H HG3  . GLU   B 1 25  ? 56.479 -27.361 -11.881 1.00 30.36 ?  25  GLU   B HG3  1 
ATOM   4318 N N    . GLU   B 1 26  ? 52.172 -24.412 -12.262 1.00 13.61 ?  26  GLU   B N    1 
ATOM   4319 C CA   . GLU   B 1 26  ? 51.049 -23.881 -13.025 1.00 14.00 ?  26  GLU   B CA   1 
ATOM   4320 C C    . GLU   B 1 26  ? 50.999 -22.363 -12.942 1.00 13.46 ?  26  GLU   B C    1 
ATOM   4321 O O    . GLU   B 1 26  ? 50.790 -21.686 -13.951 1.00 14.71 ?  26  GLU   B O    1 
ATOM   4322 C CB   . GLU   B 1 26  ? 49.736 -24.470 -12.509 1.00 15.98 ?  26  GLU   B CB   1 
ATOM   4323 C CG   . GLU   B 1 26  ? 49.320 -25.761 -13.170 1.00 18.91 ?  26  GLU   B CG   1 
ATOM   4324 C CD   . GLU   B 1 26  ? 49.074 -25.623 -14.667 1.00 20.56 ?  26  GLU   B CD   1 
ATOM   4325 O OE1  . GLU   B 1 26  ? 48.095 -24.968 -15.084 1.00 20.57 ?  26  GLU   B OE1  1 
ATOM   4326 O OE2  . GLU   B 1 26  ? 49.857 -26.205 -15.429 1.00 22.81 -1 26  GLU   B OE2  1 
ATOM   4327 H H    . GLU   B 1 26  ? 51.944 -24.919 -11.600 1.00 16.31 ?  26  GLU   B H    1 
ATOM   4328 H HA   . GLU   B 1 26  ? 51.149 -24.131 -13.954 1.00 16.77 ?  26  GLU   B HA   1 
ATOM   4329 H HB2  . GLU   B 1 26  ? 49.822 -24.647 -11.557 1.00 19.15 ?  26  GLU   B HB2  1 
ATOM   4330 H HB3  . GLU   B 1 26  ? 49.024 -23.825 -12.653 1.00 19.15 ?  26  GLU   B HB3  1 
ATOM   4331 H HG2  . GLU   B 1 26  ? 50.026 -26.407 -13.051 1.00 22.67 ?  26  GLU   B HG2  1 
ATOM   4332 H HG3  . GLU   B 1 26  ? 48.498 -26.078 -12.761 1.00 22.67 ?  26  GLU   B HG3  1 
ATOM   4333 N N    . ALA   B 1 27  ? 51.149 -21.813 -11.736 1.00 12.67 ?  27  ALA   B N    1 
ATOM   4334 C CA   . ALA   B 1 27  ? 51.114 -20.361 -11.586 1.00 13.06 ?  27  ALA   B CA   1 
ATOM   4335 C C    . ALA   B 1 27  ? 52.182 -19.697 -12.444 1.00 14.27 ?  27  ALA   B C    1 
ATOM   4336 O O    . ALA   B 1 27  ? 51.917 -18.695 -13.122 1.00 15.16 ?  27  ALA   B O    1 
ATOM   4337 C CB   . ALA   B 1 27  ? 51.275 -19.984 -10.115 1.00 13.35 ?  27  ALA   B CB   1 
ATOM   4338 H H    . ALA   B 1 27  ? 51.263 -22.254 -11.000 1.00 15.18 ?  27  ALA   B H    1 
ATOM   4339 H HA   . ALA   B 1 27  ? 50.255 -20.037 -11.876 1.00 15.65 ?  27  ALA   B HA   1 
ATOM   4340 H HB1  . ALA   B 1 27  ? 51.251 -19.021 -10.032 1.00 16.00 ?  27  ALA   B HB1  1 
ATOM   4341 H HB2  . ALA   B 1 27  ? 50.545 -20.379 -9.607  1.00 16.00 ?  27  ALA   B HB2  1 
ATOM   4342 H HB3  . ALA   B 1 27  ? 52.123 -20.326 -9.789  1.00 16.00 ?  27  ALA   B HB3  1 
ATOM   4343 N N    . LYS   B 1 28  ? 53.396 -20.252 -12.443 1.00 15.69 ?  28  LYS   B N    1 
ATOM   4344 C CA   . LYS   B 1 28  ? 54.469 -19.627 -13.205 1.00 17.98 ?  28  LYS   B CA   1 
ATOM   4345 C C    . LYS   B 1 28  ? 54.203 -19.692 -14.701 1.00 19.17 ?  28  LYS   B C    1 
ATOM   4346 O O    . LYS   B 1 28  ? 54.618 -18.791 -15.441 1.00 20.11 ?  28  LYS   B O    1 
ATOM   4347 C CB   . LYS   B 1 28  ? 55.825 -20.232 -12.829 1.00 20.56 ?  28  LYS   B CB   1 
ATOM   4348 C CG   . LYS   B 1 28  ? 56.233 -19.907 -11.392 1.00 23.50 ?  28  LYS   B CG   1 
ATOM   4349 C CD   . LYS   B 1 28  ? 57.661 -20.309 -11.050 1.00 27.28 ?  28  LYS   B CD   1 
ATOM   4350 C CE   . LYS   B 1 28  ? 57.756 -21.761 -10.640 1.00 30.01 ?  28  LYS   B CE   1 
ATOM   4351 N NZ   . LYS   B 1 28  ? 59.092 -22.077 -10.056 1.00 31.53 ?  28  LYS   B NZ   1 
ATOM   4352 H H    . LYS   B 1 28  ? 53.624 -20.967 -12.019 1.00 18.80 ?  28  LYS   B H    1 
ATOM   4353 H HA   . LYS   B 1 28  ? 54.506 -18.689 -12.970 1.00 21.55 ?  28  LYS   B HA   1 
ATOM   4354 H HB2  . LYS   B 1 28  ? 55.782 -21.195 -12.918 1.00 24.65 ?  28  LYS   B HB2  1 
ATOM   4355 H HB3  . LYS   B 1 28  ? 56.509 -19.873 -13.422 1.00 24.65 ?  28  LYS   B HB3  1 
ATOM   4356 H HG2  . LYS   B 1 28  ? 56.151 -18.948 -11.258 1.00 28.18 ?  28  LYS   B HG2  1 
ATOM   4357 H HG3  . LYS   B 1 28  ? 55.636 -20.374 -10.790 1.00 28.18 ?  28  LYS   B HG3  1 
ATOM   4358 H HD2  . LYS   B 1 28  ? 58.224 -20.173 -11.827 1.00 32.71 ?  28  LYS   B HD2  1 
ATOM   4359 H HD3  . LYS   B 1 28  ? 57.973 -19.762 -10.311 1.00 32.71 ?  28  LYS   B HD3  1 
ATOM   4360 H HE2  . LYS   B 1 28  ? 57.079 -21.951 -9.970  1.00 35.99 ?  28  LYS   B HE2  1 
ATOM   4361 H HE3  . LYS   B 1 28  ? 57.623 -22.325 -11.418 1.00 35.99 ?  28  LYS   B HE3  1 
ATOM   4362 H HZ1  . LYS   B 1 28  ? 59.128 -22.935 -9.821  1.00 37.81 ?  28  LYS   B HZ1  1 
ATOM   4363 H HZ2  . LYS   B 1 28  ? 59.731 -21.914 -10.653 1.00 37.81 ?  28  LYS   B HZ2  1 
ATOM   4364 H HZ3  . LYS   B 1 28  ? 59.235 -21.574 -9.334  1.00 37.81 ?  28  LYS   B HZ3  1 
ATOM   4365 N N    A LYS   B 1 29  ? 53.500 -20.728 -15.165 0.40 20.11 ?  29  LYS   B N    1 
ATOM   4366 N N    B LYS   B 1 29  ? 53.486 -20.718 -15.159 0.60 19.96 ?  29  LYS   B N    1 
ATOM   4367 C CA   A LYS   B 1 29  ? 53.212 -20.865 -16.588 0.40 21.79 ?  29  LYS   B CA   1 
ATOM   4368 C CA   B LYS   B 1 29  ? 53.215 -20.865 -16.582 0.60 21.84 ?  29  LYS   B CA   1 
ATOM   4369 C C    A LYS   B 1 29  ? 51.950 -20.122 -17.014 0.40 20.58 ?  29  LYS   B C    1 
ATOM   4370 C C    B LYS   B 1 29  ? 51.950 -20.132 -17.018 0.60 20.65 ?  29  LYS   B C    1 
ATOM   4371 O O    A LYS   B 1 29  ? 51.934 -19.497 -18.080 0.40 21.17 ?  29  LYS   B O    1 
ATOM   4372 O O    B LYS   B 1 29  ? 51.931 -19.529 -18.097 0.60 21.53 ?  29  LYS   B O    1 
ATOM   4373 C CB   A LYS   B 1 29  ? 53.102 -22.344 -16.971 0.40 25.15 ?  29  LYS   B CB   1 
ATOM   4374 C CB   B LYS   B 1 29  ? 53.111 -22.349 -16.943 0.60 25.60 ?  29  LYS   B CB   1 
ATOM   4375 C CG   A LYS   B 1 29  ? 52.834 -22.576 -18.451 0.40 28.20 ?  29  LYS   B CG   1 
ATOM   4376 C CG   B LYS   B 1 29  ? 52.960 -22.617 -18.428 0.60 29.01 ?  29  LYS   B CG   1 
ATOM   4377 C CD   A LYS   B 1 29  ? 53.032 -24.036 -18.832 0.40 30.59 ?  29  LYS   B CD   1 
ATOM   4378 C CD   B LYS   B 1 29  ? 53.228 -24.082 -18.757 0.60 31.65 ?  29  LYS   B CD   1 
ATOM   4379 C CE   A LYS   B 1 29  ? 51.952 -24.928 -18.239 0.40 32.24 ?  29  LYS   B CE   1 
ATOM   4380 C CE   B LYS   B 1 29  ? 52.178 -25.004 -18.154 0.60 33.48 ?  29  LYS   B CE   1 
ATOM   4381 N NZ   A LYS   B 1 29  ? 52.132 -26.350 -18.649 0.40 33.18 ?  29  LYS   B NZ   1 
ATOM   4382 N NZ   B LYS   B 1 29  ? 52.424 -26.431 -18.513 0.60 34.51 ?  29  LYS   B NZ   1 
ATOM   4383 H H    A LYS   B 1 29  ? 53.183 -21.365 -14.673 0.40 24.11 ?  29  LYS   B H    1 
ATOM   4384 H H    B LYS   B 1 29  ? 53.137 -21.335 -14.661 0.60 23.93 ?  29  LYS   B H    1 
ATOM   4385 H HA   A LYS   B 1 29  ? 53.946 -20.490 -17.084 0.40 26.13 ?  29  LYS   B HA   1 
ATOM   4386 H HA   B LYS   B 1 29  ? 53.959 -20.493 -17.074 0.60 26.18 ?  29  LYS   B HA   1 
ATOM   4387 H HB2  A LYS   B 1 29  ? 53.940 -22.784 -16.753 0.40 30.15 ?  29  LYS   B HB2  1 
ATOM   4388 H HB2  B LYS   B 1 29  ? 53.918 -22.798 -16.645 0.60 30.69 ?  29  LYS   B HB2  1 
ATOM   4389 H HB3  A LYS   B 1 29  ? 52.378 -22.749 -16.473 0.40 30.15 ?  29  LYS   B HB3  1 
ATOM   4390 H HB3  B LYS   B 1 29  ? 52.340 -22.727 -16.496 0.60 30.69 ?  29  LYS   B HB3  1 
ATOM   4391 H HG2  A LYS   B 1 29  ? 51.917 -22.332 -18.653 0.40 33.81 ?  29  LYS   B HG2  1 
ATOM   4392 H HG2  B LYS   B 1 29  ? 52.054 -22.402 -18.700 0.60 34.78 ?  29  LYS   B HG2  1 
ATOM   4393 H HG3  A LYS   B 1 29  ? 53.447 -22.039 -18.978 0.40 33.81 ?  29  LYS   B HG3  1 
ATOM   4394 H HG3  B LYS   B 1 29  ? 53.596 -22.072 -18.918 0.60 34.78 ?  29  LYS   B HG3  1 
ATOM   4395 H HD2  A LYS   B 1 29  ? 52.999 -24.122 -19.797 0.40 36.68 ?  29  LYS   B HD2  1 
ATOM   4396 H HD2  B LYS   B 1 29  ? 53.217 -24.200 -19.719 0.60 37.96 ?  29  LYS   B HD2  1 
ATOM   4397 H HD3  A LYS   B 1 29  ? 53.891 -24.339 -18.497 0.40 36.68 ?  29  LYS   B HD3  1 
ATOM   4398 H HD3  B LYS   B 1 29  ? 54.093 -24.337 -18.398 0.60 37.96 ?  29  LYS   B HD3  1 
ATOM   4399 H HE2  A LYS   B 1 29  ? 51.994 -24.884 -17.271 0.40 38.66 ?  29  LYS   B HE2  1 
ATOM   4400 H HE2  B LYS   B 1 29  ? 52.200 -24.929 -17.187 0.60 40.15 ?  29  LYS   B HE2  1 
ATOM   4401 H HE3  A LYS   B 1 29  ? 51.083 -24.630 -18.551 0.40 38.66 ?  29  LYS   B HE3  1 
ATOM   4402 H HE3  B LYS   B 1 29  ? 51.302 -24.753 -18.490 0.60 40.15 ?  29  LYS   B HE3  1 
ATOM   4403 H HZ1  A LYS   B 1 29  ? 51.491 -26.854 -18.292 0.40 39.79 ?  29  LYS   B HZ1  1 
ATOM   4404 H HZ1  B LYS   B 1 29  ? 51.798 -26.950 -18.151 0.60 41.39 ?  29  LYS   B HZ1  1 
ATOM   4405 H HZ2  A LYS   B 1 29  ? 52.094 -26.419 -19.536 0.40 39.79 ?  29  LYS   B HZ2  1 
ATOM   4406 H HZ2  B LYS   B 1 29  ? 52.404 -26.530 -19.398 0.60 41.39 ?  29  LYS   B HZ2  1 
ATOM   4407 H HZ3  A LYS   B 1 29  ? 52.924 -26.649 -18.370 0.40 39.79 ?  29  LYS   B HZ3  1 
ATOM   4408 H HZ3  B LYS   B 1 29  ? 53.221 -26.688 -18.212 0.60 41.39 ?  29  LYS   B HZ3  1 
ATOM   4409 N N    . VAL   B 1 30  ? 50.894 -20.178 -16.201 1.00 19.16 ?  30  VAL   B N    1 
ATOM   4410 C CA   . VAL   B 1 30  ? 49.604 -19.591 -16.580 1.00 18.72 ?  30  VAL   B CA   1 
ATOM   4411 C C    . VAL   B 1 30  ? 49.596 -18.074 -16.448 1.00 17.45 ?  30  VAL   B C    1 
ATOM   4412 O O    . VAL   B 1 30  ? 48.849 -17.383 -17.158 1.00 18.21 ?  30  VAL   B O    1 
ATOM   4413 C CB   . VAL   B 1 30  ? 48.498 -20.207 -15.701 1.00 19.68 ?  30  VAL   B CB   1 
ATOM   4414 C CG1  . VAL   B 1 30  ? 47.208 -19.402 -15.790 1.00 20.11 ?  30  VAL   B CG1  1 
ATOM   4415 C CG2  . VAL   B 1 30  ? 48.261 -21.660 -16.080 1.00 20.32 ?  30  VAL   B CG2  1 
ATOM   4416 H H    A VAL   B 1 30  ? 50.893 -20.554 -15.421 0.40 22.97 ?  30  VAL   B H    1 
ATOM   4417 H H    B VAL   B 1 30  ? 50.890 -20.563 -15.426 0.60 22.97 ?  30  VAL   B H    1 
ATOM   4418 H HA   . VAL   B 1 30  ? 49.415 -19.828 -17.498 1.00 22.44 ?  30  VAL   B HA   1 
ATOM   4419 H HB   . VAL   B 1 30  ? 48.789 -20.195 -14.774 1.00 23.59 ?  30  VAL   B HB   1 
ATOM   4420 H HG11 . VAL   B 1 30  ? 46.469 -19.985 -15.556 1.00 24.11 ?  30  VAL   B HG11 1 
ATOM   4421 H HG12 . VAL   B 1 30  ? 47.251 -18.661 -15.169 1.00 24.11 ?  30  VAL   B HG12 1 
ATOM   4422 H HG13 . VAL   B 1 30  ? 47.094 -19.086 -16.695 1.00 24.11 ?  30  VAL   B HG13 1 
ATOM   4423 H HG21 . VAL   B 1 30  ? 47.571 -22.032 -15.503 1.00 24.35 ?  30  VAL   B HG21 1 
ATOM   4424 H HG22 . VAL   B 1 30  ? 47.970 -21.703 -17.005 1.00 24.35 ?  30  VAL   B HG22 1 
ATOM   4425 H HG23 . VAL   B 1 30  ? 49.085 -22.158 -15.969 1.00 24.35 ?  30  VAL   B HG23 1 
ATOM   4426 N N    . LYS   B 1 31  ? 50.377 -17.550 -15.516 1.00 16.80 ?  31  LYS   B N    1 
ATOM   4427 C CA   . LYS   B 1 31  ? 50.401 -16.142 -15.163 1.00 17.14 ?  31  LYS   B CA   1 
ATOM   4428 C C    . LYS   B 1 31  ? 49.004 -15.672 -14.760 1.00 15.18 ?  31  LYS   B C    1 
ATOM   4429 O O    . LYS   B 1 31  ? 48.443 -14.764 -15.386 1.00 16.16 ?  31  LYS   B O    1 
ATOM   4430 C CB   . LYS   B 1 31  ? 51.016 -15.330 -16.306 1.00 19.97 ?  31  LYS   B CB   1 
ATOM   4431 C CG   . LYS   B 1 31  ? 52.438 -15.776 -16.669 1.00 23.01 ?  31  LYS   B CG   1 
ATOM   4432 C CD   . LYS   B 1 31  ? 53.011 -14.969 -17.822 1.00 26.19 ?  31  LYS   B CD   1 
ATOM   4433 C CE   . LYS   B 1 31  ? 54.498 -15.210 -17.994 1.00 28.78 ?  31  LYS   B CE   1 
ATOM   4434 N NZ   . LYS   B 1 31  ? 55.248 -14.802 -16.775 1.00 30.37 ?  31  LYS   B NZ   1 
ATOM   4435 H H    . LYS   B 1 31  ? 50.914 -18.026 -15.055 1.00 20.13 ?  31  LYS   B H    1 
ATOM   4436 H HA   . LYS   B 1 31  ? 50.971 -16.047 -14.398 1.00 20.55 ?  31  LYS   B HA   1 
ATOM   4437 H HB2  . LYS   B 1 31  ? 50.464 -15.423 -17.096 1.00 23.94 ?  31  LYS   B HB2  1 
ATOM   4438 H HB3  . LYS   B 1 31  ? 51.056 -14.404 -16.032 1.00 23.94 ?  31  LYS   B HB3  1 
ATOM   4439 H HG2  . LYS   B 1 31  ? 53.011 -15.661 -15.896 1.00 27.59 ?  31  LYS   B HG2  1 
ATOM   4440 H HG3  . LYS   B 1 31  ? 52.420 -16.711 -16.934 1.00 27.59 ?  31  LYS   B HG3  1 
ATOM   4441 H HD2  . LYS   B 1 31  ? 52.569 -15.229 -18.643 1.00 31.40 ?  31  LYS   B HD2  1 
ATOM   4442 H HD3  . LYS   B 1 31  ? 52.878 -14.027 -17.648 1.00 31.40 ?  31  LYS   B HD3  1 
ATOM   4443 H HE2  . LYS   B 1 31  ? 54.658 -16.154 -18.149 1.00 34.52 ?  31  LYS   B HE2  1 
ATOM   4444 H HE3  . LYS   B 1 31  ? 54.824 -14.686 -18.744 1.00 34.52 ?  31  LYS   B HE3  1 
ATOM   4445 H HZ1  . LYS   B 1 31  ? 56.123 -14.827 -16.933 1.00 36.42 ?  31  LYS   B HZ1  1 
ATOM   4446 H HZ2  . LYS   B 1 31  ? 55.019 -13.973 -16.543 1.00 36.42 ?  31  LYS   B HZ2  1 
ATOM   4447 H HZ3  . LYS   B 1 31  ? 55.058 -15.352 -16.102 1.00 36.42 ?  31  LYS   B HZ3  1 
ATOM   4448 N N    . PRO   B 1 32  ? 48.407 -16.276 -13.722 1.00 13.41 ?  32  PRO   B N    1 
ATOM   4449 C CA   . PRO   B 1 32  ? 47.028 -15.927 -13.359 1.00 12.53 ?  32  PRO   B CA   1 
ATOM   4450 C C    . PRO   B 1 32  ? 46.944 -14.581 -12.663 1.00 12.56 ?  32  PRO   B C    1 
ATOM   4451 O O    . PRO   B 1 32  ? 47.870 -14.156 -11.963 1.00 13.81 ?  32  PRO   B O    1 
ATOM   4452 C CB   . PRO   B 1 32  ? 46.641 -17.045 -12.383 1.00 12.99 ?  32  PRO   B CB   1 
ATOM   4453 C CG   . PRO   B 1 32  ? 47.941 -17.366 -11.702 1.00 13.33 ?  32  PRO   B CG   1 
ATOM   4454 C CD   . PRO   B 1 32  ? 48.983 -17.259 -12.785 1.00 13.55 ?  32  PRO   B CD   1 
ATOM   4455 H HA   . PRO   B 1 32  ? 46.438 -15.946 -14.135 1.00 15.01 ?  32  PRO   B HA   1 
ATOM   4456 H HB2  . PRO   B 1 32  ? 45.985 -16.726 -11.742 1.00 15.56 ?  32  PRO   B HB2  1 
ATOM   4457 H HB3  . PRO   B 1 32  ? 46.308 -17.819 -12.865 1.00 15.56 ?  32  PRO   B HB3  1 
ATOM   4458 H HG2  . PRO   B 1 32  ? 48.108 -16.717 -10.995 1.00 15.97 ?  32  PRO   B HG2  1 
ATOM   4459 H HG3  . PRO   B 1 32  ? 47.914 -18.265 -11.339 1.00 15.97 ?  32  PRO   B HG3  1 
ATOM   4460 H HD2  . PRO   B 1 32  ? 49.812 -16.921 -12.422 1.00 16.23 ?  32  PRO   B HD2  1 
ATOM   4461 H HD3  . PRO   B 1 32  ? 49.095 -18.108 -13.227 1.00 16.23 ?  32  PRO   B HD3  1 
ATOM   4462 N N    . THR   B 1 33  ? 45.790 -13.930 -12.832 1.00 12.10 ?  33  THR   B N    1 
ATOM   4463 C CA   . THR   B 1 33  ? 45.493 -12.753 -12.027 1.00 12.39 ?  33  THR   B CA   1 
ATOM   4464 C C    . THR   B 1 33  ? 45.444 -13.105 -10.548 1.00 12.26 ?  33  THR   B C    1 
ATOM   4465 O O    . THR   B 1 33  ? 45.915 -12.325 -9.706  1.00 12.93 ?  33  THR   B O    1 
ATOM   4466 C CB   . THR   B 1 33  ? 44.176 -12.115 -12.479 1.00 13.06 ?  33  THR   B CB   1 
ATOM   4467 O OG1  . THR   B 1 33  ? 44.221 -11.866 -13.884 1.00 13.25 ?  33  THR   B OG1  1 
ATOM   4468 C CG2  . THR   B 1 33  ? 43.934 -10.800 -11.745 1.00 14.37 ?  33  THR   B CG2  1 
ATOM   4469 H H    . THR   B 1 33  ? 45.169 -14.155 -13.388 1.00 14.49 ?  33  THR   B H    1 
ATOM   4470 H HA   . THR   B 1 33  ? 46.196 -12.105 -12.153 1.00 14.84 ?  33  THR   B HA   1 
ATOM   4471 H HB   . THR   B 1 33  ? 43.437 -12.712 -12.281 1.00 15.65 ?  33  THR   B HB   1 
ATOM   4472 H HG1  . THR   B 1 33  ? 43.500 -11.499 -14.136 1.00 15.88 ?  33  THR   B HG1  1 
ATOM   4473 H HG21 . THR   B 1 33  ? 43.173 -10.341 -12.126 1.00 17.22 ?  33  THR   B HG21 1 
ATOM   4474 H HG22 . THR   B 1 33  ? 43.764 -10.970 -10.805 1.00 17.22 ?  33  THR   B HG22 1 
ATOM   4475 H HG23 . THR   B 1 33  ? 44.718 -10.230 -11.824 1.00 17.22 ?  33  THR   B HG23 1 
ATOM   4476 N N    . VAL   B 1 34  ? 44.891 -14.275 -10.208 1.00 11.42 ?  34  VAL   B N    1 
ATOM   4477 C CA   . VAL   B 1 34  ? 44.698 -14.673 -8.817  1.00 10.90 ?  34  VAL   B CA   1 
ATOM   4478 C C    . VAL   B 1 34  ? 45.131 -16.119 -8.648  1.00 10.08 ?  34  VAL   B C    1 
ATOM   4479 O O    . VAL   B 1 34  ? 44.615 -17.008 -9.335  1.00 10.81 ?  34  VAL   B O    1 
ATOM   4480 C CB   . VAL   B 1 34  ? 43.230 -14.531 -8.369  1.00 12.02 ?  34  VAL   B CB   1 
ATOM   4481 C CG1  . VAL   B 1 34  ? 43.071 -14.975 -6.921  1.00 12.58 ?  34  VAL   B CG1  1 
ATOM   4482 C CG2  . VAL   B 1 34  ? 42.731 -13.102 -8.563  1.00 12.80 ?  34  VAL   B CG2  1 
ATOM   4483 H H    . VAL   B 1 34  ? 44.627 -14.873 -10.773 1.00 13.68 ?  34  VAL   B H    1 
ATOM   4484 H HA   . VAL   B 1 34  ? 45.247 -14.116 -8.241  1.00 13.05 ?  34  VAL   B HA   1 
ATOM   4485 H HB   . VAL   B 1 34  ? 42.680 -15.108 -8.922  1.00 14.40 ?  34  VAL   B HB   1 
ATOM   4486 H HG11 . VAL   B 1 34  ? 42.219 -14.654 -6.584  1.00 15.07 ?  34  VAL   B HG11 1 
ATOM   4487 H HG12 . VAL   B 1 34  ? 43.098 -15.943 -6.879  1.00 15.07 ?  34  VAL   B HG12 1 
ATOM   4488 H HG13 . VAL   B 1 34  ? 43.794 -14.598 -6.394  1.00 15.07 ?  34  VAL   B HG13 1 
ATOM   4489 H HG21 . VAL   B 1 34  ? 41.815 -13.043 -8.250  1.00 15.34 ?  34  VAL   B HG21 1 
ATOM   4490 H HG22 . VAL   B 1 34  ? 43.296 -12.500 -8.056  1.00 15.34 ?  34  VAL   B HG22 1 
ATOM   4491 H HG23 . VAL   B 1 34  ? 42.772 -12.877 -9.508  1.00 15.34 ?  34  VAL   B HG23 1 
ATOM   4492 N N    . VAL   B 1 35  ? 46.034 -16.364 -7.700  1.00 9.76  ?  35  VAL   B N    1 
ATOM   4493 C CA   . VAL   B 1 35  ? 46.277 -17.707 -7.183  1.00 9.88  ?  35  VAL   B CA   1 
ATOM   4494 C C    . VAL   B 1 35  ? 45.737 -17.768 -5.761  1.00 9.35  ?  35  VAL   B C    1 
ATOM   4495 O O    . VAL   B 1 35  ? 45.951 -16.843 -4.968  1.00 9.59  ?  35  VAL   B O    1 
ATOM   4496 C CB   . VAL   B 1 35  ? 47.762 -18.121 -7.270  1.00 10.55 ?  35  VAL   B CB   1 
ATOM   4497 C CG1  . VAL   B 1 35  ? 48.662 -17.288 -6.348  1.00 11.12 ?  35  VAL   B CG1  1 
ATOM   4498 C CG2  . VAL   B 1 35  ? 47.906 -19.621 -6.964  1.00 11.20 ?  35  VAL   B CG2  1 
ATOM   4499 H H    . VAL   B 1 35  ? 46.528 -15.759 -7.334  1.00 11.68 ?  35  VAL   B H    1 
ATOM   4500 H HA   . VAL   B 1 35  ? 45.764 -18.340 -7.717  1.00 11.83 ?  35  VAL   B HA   1 
ATOM   4501 H HB   . VAL   B 1 35  ? 48.066 -17.990 -8.185  1.00 12.63 ?  35  VAL   B HB   1 
ATOM   4502 H HG11 . VAL   B 1 35  ? 49.584 -17.515 -6.534  1.00 13.32 ?  35  VAL   B HG11 1 
ATOM   4503 H HG12 . VAL   B 1 35  ? 48.498 -16.356 -6.526  1.00 13.32 ?  35  VAL   B HG12 1 
ATOM   4504 H HG13 . VAL   B 1 35  ? 48.441 -17.504 -5.430  1.00 13.32 ?  35  VAL   B HG13 1 
ATOM   4505 H HG21 . VAL   B 1 35  ? 48.830 -19.885 -7.075  1.00 13.41 ?  35  VAL   B HG21 1 
ATOM   4506 H HG22 . VAL   B 1 35  ? 47.622 -19.788 -6.048  1.00 13.41 ?  35  VAL   B HG22 1 
ATOM   4507 H HG23 . VAL   B 1 35  ? 47.343 -20.131 -7.575  1.00 13.41 ?  35  VAL   B HG23 1 
ATOM   4508 N N    . VAL   B 1 36  ? 45.018 -18.847 -5.447  1.00 9.23  ?  36  VAL   B N    1 
ATOM   4509 C CA   . VAL   B 1 36  ? 44.477 -19.062 -4.115  1.00 9.12  ?  36  VAL   B CA   1 
ATOM   4510 C C    . VAL   B 1 36  ? 45.486 -19.821 -3.266  1.00 8.79  ?  36  VAL   B C    1 
ATOM   4511 O O    . VAL   B 1 36  ? 46.025 -20.855 -3.687  1.00 10.03 ?  36  VAL   B O    1 
ATOM   4512 C CB   . VAL   B 1 36  ? 43.142 -19.823 -4.192  1.00 9.35  ?  36  VAL   B CB   1 
ATOM   4513 C CG1  . VAL   B 1 36  ? 42.642 -20.178 -2.796  1.00 10.21 ?  36  VAL   B CG1  1 
ATOM   4514 C CG2  . VAL   B 1 36  ? 42.111 -18.998 -4.951  1.00 10.13 ?  36  VAL   B CG2  1 
ATOM   4515 H H    . VAL   B 1 36  ? 44.841 -19.489 -6.002  1.00 11.05 ?  36  VAL   B H    1 
ATOM   4516 H HA   . VAL   B 1 36  ? 44.311 -18.202 -3.701  1.00 10.92 ?  36  VAL   B HA   1 
ATOM   4517 H HB   . VAL   B 1 36  ? 43.276 -20.650 -4.680  1.00 11.19 ?  36  VAL   B HB   1 
ATOM   4518 H HG11 . VAL   B 1 36  ? 41.701 -20.408 -2.847  1.00 12.23 ?  36  VAL   B HG11 1 
ATOM   4519 H HG12 . VAL   B 1 36  ? 43.150 -20.925 -2.454  1.00 12.23 ?  36  VAL   B HG12 1 
ATOM   4520 H HG13 . VAL   B 1 36  ? 42.756 -19.403 -2.216  1.00 12.23 ?  36  VAL   B HG13 1 
ATOM   4521 H HG21 . VAL   B 1 36  ? 41.268 -19.478 -4.967  1.00 12.13 ?  36  VAL   B HG21 1 
ATOM   4522 H HG22 . VAL   B 1 36  ? 41.999 -18.143 -4.509  1.00 12.13 ?  36  VAL   B HG22 1 
ATOM   4523 H HG23 . VAL   B 1 36  ? 42.425 -18.858 -5.862  1.00 12.13 ?  36  VAL   B HG23 1 
ATOM   4524 N N    . ASN   B 1 37  ? 45.711 -19.327 -2.051  1.00 9.10  ?  37  ASN   B N    1 
ATOM   4525 C CA   . ASN   B 1 37  ? 46.467 -20.050 -1.044  1.00 9.54  ?  37  ASN   B CA   1 
ATOM   4526 C C    . ASN   B 1 37  ? 45.520 -20.720 -0.055  1.00 9.24  ?  37  ASN   B C    1 
ATOM   4527 O O    . ASN   B 1 37  ? 44.513 -20.141 0.361   1.00 9.89  ?  37  ASN   B O    1 
ATOM   4528 C CB   . ASN   B 1 37  ? 47.400 -19.109 -0.287  1.00 9.69  ?  37  ASN   B CB   1 
ATOM   4529 C CG   . ASN   B 1 37  ? 48.244 -19.828 0.731   1.00 9.95  ?  37  ASN   B CG   1 
ATOM   4530 O OD1  . ASN   B 1 37  ? 48.587 -21.002 0.554   1.00 10.68 ?  37  ASN   B OD1  1 
ATOM   4531 N ND2  . ASN   B 1 37  ? 48.589 -19.133 1.807   1.00 10.48 ?  37  ASN   B ND2  1 
ATOM   4532 H H    . ASN   B 1 37  ? 45.426 -18.561 -1.779  1.00 10.90 ?  37  ASN   B H    1 
ATOM   4533 H HA   . ASN   B 1 37  ? 47.000 -20.741 -1.469  1.00 11.42 ?  37  ASN   B HA   1 
ATOM   4534 H HB2  . ASN   B 1 37  ? 47.996 -18.683 -0.924  1.00 11.61 ?  37  ASN   B HB2  1 
ATOM   4535 H HB3  . ASN   B 1 37  ? 46.873 -18.443 0.176   1.00 11.61 ?  37  ASN   B HB3  1 
ATOM   4536 H HD21 . ASN   B 1 37  ? 49.069 -19.505 2.419   1.00 12.55 ?  37  ASN   B HD21 1 
ATOM   4537 H HD22 . ASN   B 1 37  ? 48.328 -18.328 1.901   1.00 12.55 ?  37  ASN   B HD22 1 
ATOM   4538 N N    . ALA   B 1 38  ? 45.869 -21.953 0.321   1.00 9.72  ?  38  ALA   B N    1 
ATOM   4539 C CA   . ALA   B 1 38  ? 45.208 -22.704 1.393   1.00 10.07 ?  38  ALA   B CA   1 
ATOM   4540 C C    . ALA   B 1 38  ? 45.791 -22.228 2.723   1.00 9.82  ?  38  ALA   B C    1 
ATOM   4541 O O    . ALA   B 1 38  ? 46.698 -22.836 3.303   1.00 10.94 ?  38  ALA   B O    1 
ATOM   4542 C CB   . ALA   B 1 38  ? 45.421 -24.201 1.201   1.00 11.23 ?  38  ALA   B CB   1 
ATOM   4543 H H    . ALA   B 1 38  ? 46.523 -22.390 -0.029  1.00 11.63 ?  38  ALA   B H    1 
ATOM   4544 H HA   . ALA   B 1 38  ? 44.255 -22.519 1.385   1.00 12.06 ?  38  ALA   B HA   1 
ATOM   4545 H HB1  . ALA   B 1 38  ? 44.967 -24.679 1.924   1.00 13.45 ?  38  ALA   B HB1  1 
ATOM   4546 H HB2  . ALA   B 1 38  ? 45.039 -24.469 0.351   1.00 13.45 ?  38  ALA   B HB2  1 
ATOM   4547 H HB3  . ALA   B 1 38  ? 46.365 -24.397 1.224   1.00 13.45 ?  38  ALA   B HB3  1 
ATOM   4548 N N    . ALA   B 1 39  ? 45.279 -21.088 3.190   1.00 9.66  ?  39  ALA   B N    1 
ATOM   4549 C CA   . ALA   B 1 39  ? 45.835 -20.367 4.322   1.00 10.23 ?  39  ALA   B CA   1 
ATOM   4550 C C    . ALA   B 1 39  ? 45.218 -20.821 5.643   1.00 10.09 ?  39  ALA   B C    1 
ATOM   4551 O O    . ALA   B 1 39  ? 44.187 -21.493 5.684   1.00 10.96 ?  39  ALA   B O    1 
ATOM   4552 C CB   . ALA   B 1 39  ? 45.595 -18.865 4.138   1.00 10.99 ?  39  ALA   B CB   1 
ATOM   4553 H H    . ALA   B 1 39  ? 44.579 -20.709 2.853   1.00 11.57 ?  39  ALA   B H    1 
ATOM   4554 H HA   . ALA   B 1 39  ? 46.791 -20.521 4.357   1.00 12.25 ?  39  ALA   B HA   1 
ATOM   4555 H HB1  . ALA   B 1 39  ? 45.976 -18.392 4.896   1.00 13.16 ?  39  ALA   B HB1  1 
ATOM   4556 H HB2  . ALA   B 1 39  ? 46.026 -18.573 3.318   1.00 13.16 ?  39  ALA   B HB2  1 
ATOM   4557 H HB3  . ALA   B 1 39  ? 44.642 -18.699 4.088   1.00 13.16 ?  39  ALA   B HB3  1 
ATOM   4558 N N    . ASN   B 1 40  ? 45.861 -20.413 6.736   1.00 11.05 ?  40  ASN   B N    1 
ATOM   4559 C CA   . ASN   B 1 40  ? 45.294 -20.458 8.074   1.00 11.81 ?  40  ASN   B CA   1 
ATOM   4560 C C    . ASN   B 1 40  ? 45.120 -19.032 8.602   1.00 11.43 ?  40  ASN   B C    1 
ATOM   4561 O O    . ASN   B 1 40  ? 45.537 -18.052 7.974   1.00 11.49 ?  40  ASN   B O    1 
ATOM   4562 C CB   . ASN   B 1 40  ? 46.140 -21.334 9.011   1.00 12.73 ?  40  ASN   B CB   1 
ATOM   4563 C CG   . ASN   B 1 40  ? 47.596 -20.922 9.050   1.00 13.57 ?  40  ASN   B CG   1 
ATOM   4564 O OD1  . ASN   B 1 40  ? 47.911 -19.741 9.148   1.00 15.02 ?  40  ASN   B OD1  1 
ATOM   4565 N ND2  . ASN   B 1 40  ? 48.492 -21.898 8.976   1.00 13.74 ?  40  ASN   B ND2  1 
ATOM   4566 H H    . ASN   B 1 40  ? 46.662 -20.089 6.719   1.00 13.23 ?  40  ASN   B H    1 
ATOM   4567 H HA   . ASN   B 1 40  ? 44.413 -20.853 8.023   1.00 14.14 ?  40  ASN   B HA   1 
ATOM   4568 H HB2  . ASN   B 1 40  ? 45.787 -21.270 9.911   1.00 15.25 ?  40  ASN   B HB2  1 
ATOM   4569 H HB3  . ASN   B 1 40  ? 46.097 -22.255 8.703   1.00 15.25 ?  40  ASN   B HB3  1 
ATOM   4570 H HD21 . ASN   B 1 40  ? 49.332 -21.714 8.994   1.00 16.47 ?  40  ASN   B HD21 1 
ATOM   4571 H HD22 . ASN   B 1 40  ? 48.233 -22.716 8.909   1.00 16.47 ?  40  ASN   B HD22 1 
ATOM   4572 N N    . VAL   B 1 41  ? 44.461 -18.906 9.757   1.00 11.82 ?  41  VAL   B N    1 
ATOM   4573 C CA   . VAL   B 1 41  ? 44.008 -17.584 10.209  1.00 12.66 ?  41  VAL   B CA   1 
ATOM   4574 C C    . VAL   B 1 41  ? 45.158 -16.630 10.513  1.00 12.44 ?  41  VAL   B C    1 
ATOM   4575 O O    . VAL   B 1 41  ? 44.976 -15.408 10.448  1.00 12.72 ?  41  VAL   B O    1 
ATOM   4576 C CB   . VAL   B 1 41  ? 43.028 -17.666 11.397  1.00 13.87 ?  41  VAL   B CB   1 
ATOM   4577 C CG1  . VAL   B 1 41  ? 41.726 -18.327 10.971  1.00 13.99 ?  41  VAL   B CG1  1 
ATOM   4578 C CG2  . VAL   B 1 41  ? 43.656 -18.367 12.593  1.00 15.14 ?  41  VAL   B CG2  1 
ATOM   4579 H H    . VAL   B 1 41  ? 44.272 -19.553 10.286  1.00 14.16 ?  41  VAL   B H    1 
ATOM   4580 H HA   . VAL   B 1 41  ? 43.516 -17.186 9.479   1.00 15.17 ?  41  VAL   B HA   1 
ATOM   4581 H HB   . VAL   B 1 41  ? 42.813 -16.764 11.679  1.00 16.61 ?  41  VAL   B HB   1 
ATOM   4582 H HG11 . VAL   B 1 41  ? 41.110 -18.325 11.722  1.00 16.76 ?  41  VAL   B HG11 1 
ATOM   4583 H HG12 . VAL   B 1 41  ? 41.346 -17.825 10.233  1.00 16.76 ?  41  VAL   B HG12 1 
ATOM   4584 H HG13 . VAL   B 1 41  ? 41.909 -19.237 10.695  1.00 16.76 ?  41  VAL   B HG13 1 
ATOM   4585 H HG21 . VAL   B 1 41  ? 43.016 -18.391 13.321  1.00 18.14 ?  41  VAL   B HG21 1 
ATOM   4586 H HG22 . VAL   B 1 41  ? 43.900 -19.273 12.339  1.00 18.14 ?  41  VAL   B HG22 1 
ATOM   4587 H HG23 . VAL   B 1 41  ? 44.449 -17.879 12.867  1.00 18.14 ?  41  VAL   B HG23 1 
ATOM   4588 N N    . TYR   B 1 42  ? 46.330 -17.148 10.884  1.00 12.83 ?  42  TYR   B N    1 
ATOM   4589 C CA   . TYR   B 1 42  ? 47.482 -16.296 11.154  1.00 13.78 ?  42  TYR   B CA   1 
ATOM   4590 C C    . TYR   B 1 42  ? 48.446 -16.216 9.974   1.00 12.32 ?  42  TYR   B C    1 
ATOM   4591 O O    . TYR   B 1 42  ? 49.534 -15.645 10.114  1.00 13.46 ?  42  TYR   B O    1 
ATOM   4592 C CB   . TYR   B 1 42  ? 48.182 -16.694 12.463  1.00 16.08 ?  42  TYR   B CB   1 
ATOM   4593 C CG   . TYR   B 1 42  ? 47.571 -16.023 13.690  1.00 16.85 ?  42  TYR   B CG   1 
ATOM   4594 C CD1  . TYR   B 1 42  ? 47.800 -14.673 13.954  1.00 16.17 ?  42  TYR   B CD1  1 
ATOM   4595 C CD2  . TYR   B 1 42  ? 46.769 -16.730 14.574  1.00 18.92 ?  42  TYR   B CD2  1 
ATOM   4596 C CE1  . TYR   B 1 42  ? 47.248 -14.050 15.062  1.00 17.53 ?  42  TYR   B CE1  1 
ATOM   4597 C CE2  . TYR   B 1 42  ? 46.213 -16.116 15.685  1.00 19.32 ?  42  TYR   B CE2  1 
ATOM   4598 C CZ   . TYR   B 1 42  ? 46.453 -14.775 15.925  1.00 19.34 ?  42  TYR   B CZ   1 
ATOM   4599 O OH   . TYR   B 1 42  ? 45.898 -14.165 17.033  1.00 22.04 ?  42  TYR   B OH   1 
ATOM   4600 H H    . TYR   B 1 42  ? 46.482 -17.992 10.981  1.00 15.38 ?  42  TYR   B H    1 
ATOM   4601 H HA   . TYR   B 1 42  ? 47.152 -15.398 11.290  1.00 16.51 ?  42  TYR   B HA   1 
ATOM   4602 H HB2  . TYR   B 1 42  ? 48.109 -17.652 12.584  1.00 19.27 ?  42  TYR   B HB2  1 
ATOM   4603 H HB3  . TYR   B 1 42  ? 49.115 -16.434 12.415  1.00 19.27 ?  42  TYR   B HB3  1 
ATOM   4604 H HD1  . TYR   B 1 42  ? 48.339 -14.180 13.371  1.00 19.38 ?  42  TYR   B HD1  1 
ATOM   4605 H HD2  . TYR   B 1 42  ? 46.600 -17.630 14.414  1.00 22.68 ?  42  TYR   B HD2  1 
ATOM   4606 H HE1  . TYR   B 1 42  ? 47.418 -13.150 15.221  1.00 21.01 ?  42  TYR   B HE1  1 
ATOM   4607 H HE2  . TYR   B 1 42  ? 45.678 -16.604 16.263  1.00 23.16 ?  42  TYR   B HE2  1 
ATOM   4608 H HH   . TYR   B 1 42  ? 46.131 -13.364 17.054  1.00 26.43 ?  42  TYR   B HH   1 
ATOM   4609 N N    . LEU   B 1 43  ? 48.051 -16.726 8.810   1.00 11.48 ?  43  LEU   B N    1 
ATOM   4610 C CA   . LEU   B 1 43  ? 48.862 -16.651 7.599   1.00 11.63 ?  43  LEU   B CA   1 
ATOM   4611 C C    . LEU   B 1 43  ? 50.278 -17.155 7.854   1.00 11.90 ?  43  LEU   B C    1 
ATOM   4612 O O    . LEU   B 1 43  ? 51.256 -16.557 7.409   1.00 12.60 ?  43  LEU   B O    1 
ATOM   4613 C CB   . LEU   B 1 43  ? 48.873 -15.244 6.996   1.00 11.45 ?  43  LEU   B CB   1 
ATOM   4614 C CG   . LEU   B 1 43  ? 47.510 -14.642 6.631   1.00 11.94 ?  43  LEU   B CG   1 
ATOM   4615 C CD1  . LEU   B 1 43  ? 47.713 -13.243 6.062   1.00 12.94 ?  43  LEU   B CD1  1 
ATOM   4616 C CD2  . LEU   B 1 43  ? 46.748 -15.521 5.655   1.00 11.89 ?  43  LEU   B CD2  1 
ATOM   4617 H H    . LEU   B 1 43  ? 47.310 -17.141 8.698   1.00 13.75 ?  43  LEU   B H    1 
ATOM   4618 H HA   . LEU   B 1 43  ? 48.466 -17.237 6.936   1.00 13.93 ?  43  LEU   B HA   1 
ATOM   4619 H HB2  . LEU   B 1 43  ? 49.291 -14.641 7.631   1.00 13.72 ?  43  LEU   B HB2  1 
ATOM   4620 H HB3  . LEU   B 1 43  ? 49.401 -15.267 6.182   1.00 13.72 ?  43  LEU   B HB3  1 
ATOM   4621 H HG   . LEU   B 1 43  ? 46.979 -14.560 7.434   1.00 14.31 ?  43  LEU   B HG   1 
ATOM   4622 H HD11 . LEU   B 1 43  ? 46.848 -12.864 5.831   1.00 15.50 ?  43  LEU   B HD11 1 
ATOM   4623 H HD12 . LEU   B 1 43  ? 48.144 -12.686 6.732   1.00 15.50 ?  43  LEU   B HD12 1 
ATOM   4624 H HD13 . LEU   B 1 43  ? 48.271 -13.294 5.270   1.00 15.50 ?  43  LEU   B HD13 1 
ATOM   4625 H HD21 . LEU   B 1 43  ? 45.938 -15.059 5.378   1.00 14.25 ?  43  LEU   B HD21 1 
ATOM   4626 H HD22 . LEU   B 1 43  ? 47.304 -15.699 4.881   1.00 14.25 ?  43  LEU   B HD22 1 
ATOM   4627 H HD23 . LEU   B 1 43  ? 46.515 -16.355 6.093   1.00 14.25 ?  43  LEU   B HD23 1 
ATOM   4628 N N    . LYS   B 1 44  ? 50.382 -18.277 8.568   1.00 11.69 ?  44  LYS   B N    1 
ATOM   4629 C CA   . LYS   B 1 44  ? 51.650 -18.960 8.797   1.00 12.41 ?  44  LYS   B CA   1 
ATOM   4630 C C    . LYS   B 1 44  ? 51.762 -20.073 7.761   1.00 11.95 ?  44  LYS   B C    1 
ATOM   4631 O O    . LYS   B 1 44  ? 51.058 -21.086 7.837   1.00 13.05 ?  44  LYS   B O    1 
ATOM   4632 C CB   . LYS   B 1 44  ? 51.714 -19.484 10.230  1.00 14.02 ?  44  LYS   B CB   1 
ATOM   4633 C CG   . LYS   B 1 44  ? 51.890 -18.385 11.265  1.00 17.05 ?  44  LYS   B CG   1 
ATOM   4634 C CD   . LYS   B 1 44  ? 53.098 -17.518 10.910  1.00 20.28 ?  44  LYS   B CD   1 
ATOM   4635 C CE   . LYS   B 1 44  ? 53.476 -16.567 12.017  1.00 23.15 ?  44  LYS   B CE   1 
ATOM   4636 N NZ   . LYS   B 1 44  ? 54.696 -15.788 11.683  1.00 24.43 ?  44  LYS   B NZ   1 
ATOM   4637 H H    . LYS   B 1 44  ? 49.712 -18.668 8.938   1.00 14.00 ?  44  LYS   B H    1 
ATOM   4638 H HA   . LYS   B 1 44  ? 52.382 -18.345 8.641   1.00 14.87 ?  44  LYS   B HA   1 
ATOM   4639 H HB2  . LYS   B 1 44  ? 50.878 -19.948 10.432  1.00 16.80 ?  44  LYS   B HB2  1 
ATOM   4640 H HB3  . LYS   B 1 44  ? 52.455 -20.099 10.312  1.00 16.80 ?  44  LYS   B HB3  1 
ATOM   4641 H HG2  . LYS   B 1 44  ? 51.103 -17.828 11.289  1.00 20.44 ?  44  LYS   B HG2  1 
ATOM   4642 H HG3  . LYS   B 1 44  ? 52.050 -18.789 12.138  1.00 20.44 ?  44  LYS   B HG3  1 
ATOM   4643 H HD2  . LYS   B 1 44  ? 53.859 -18.097 10.717  1.00 24.31 ?  44  LYS   B HD2  1 
ATOM   4644 H HD3  . LYS   B 1 44  ? 52.884 -16.984 10.129  1.00 24.31 ?  44  LYS   B HD3  1 
ATOM   4645 H HE2  . LYS   B 1 44  ? 52.749 -15.943 12.151  1.00 27.75 ?  44  LYS   B HE2  1 
ATOM   4646 H HE3  . LYS   B 1 44  ? 53.648 -17.071 12.824  1.00 27.75 ?  44  LYS   B HE3  1 
ATOM   4647 H HZ1  . LYS   B 1 44  ? 54.891 -15.230 12.349  1.00 29.29 ?  44  LYS   B HZ1  1 
ATOM   4648 H HZ2  . LYS   B 1 44  ? 55.384 -16.334 11.551  1.00 29.29 ?  44  LYS   B HZ2  1 
ATOM   4649 H HZ3  . LYS   B 1 44  ? 54.560 -15.310 10.941  1.00 29.29 ?  44  LYS   B HZ3  1 
ATOM   4650 N N    . HIS   B 1 45  ? 52.622 -19.858 6.768   1.00 11.77 ?  45  HIS   B N    1 
ATOM   4651 C CA   . HIS   B 1 45  ? 52.647 -20.686 5.565   1.00 12.13 ?  45  HIS   B CA   1 
ATOM   4652 C C    . HIS   B 1 45  ? 53.670 -21.806 5.723   1.00 14.16 ?  45  HIS   B C    1 
ATOM   4653 O O    . HIS   B 1 45  ? 54.738 -21.804 5.123   1.00 16.54 ?  45  HIS   B O    1 
ATOM   4654 C CB   . HIS   B 1 45  ? 52.956 -19.827 4.351   1.00 11.77 ?  45  HIS   B CB   1 
ATOM   4655 C CG   . HIS   B 1 45  ? 52.080 -18.624 4.244   1.00 11.44 ?  45  HIS   B CG   1 
ATOM   4656 N ND1  . HIS   B 1 45  ? 50.702 -18.704 4.200   1.00 11.94 ?  45  HIS   B ND1  1 
ATOM   4657 C CD2  . HIS   B 1 45  ? 52.395 -17.309 4.183   1.00 12.54 ?  45  HIS   B CD2  1 
ATOM   4658 C CE1  . HIS   B 1 45  ? 50.214 -17.481 4.103   1.00 11.56 ?  45  HIS   B CE1  1 
ATOM   4659 N NE2  . HIS   B 1 45  ? 51.216 -16.618 4.092   1.00 12.19 ?  45  HIS   B NE2  1 
ATOM   4660 H H    . HIS   B 1 45  ? 53.203 -19.221 6.766   1.00 14.10 ?  45  HIS   B H    1 
ATOM   4661 H HA   . HIS   B 1 45  ? 51.771 -21.085 5.439   1.00 14.53 ?  45  HIS   B HA   1 
ATOM   4662 H HB2  . HIS   B 1 45  ? 53.876 -19.530 4.401   1.00 14.10 ?  45  HIS   B HB2  1 
ATOM   4663 H HB3  . HIS   B 1 45  ? 52.827 -20.366 3.549   1.00 14.10 ?  45  HIS   B HB3  1 
ATOM   4664 H HD2  . HIS   B 1 45  ? 53.251 -16.946 4.196   1.00 15.03 ?  45  HIS   B HD2  1 
ATOM   4665 H HE1  . HIS   B 1 45  ? 49.312 -17.266 4.045   1.00 13.84 ?  45  HIS   B HE1  1 
ATOM   4666 H HE2  . HIS   B 1 45  ? 51.138 -15.764 4.038   1.00 14.61 ?  45  HIS   B HE2  1 
ATOM   4667 N N    A GLY   B 1 46  ? 53.300 -22.791 6.538   0.40 15.02 ?  46  GLY   B N    1 
ATOM   4668 N N    B GLY   B 1 46  ? 53.306 -22.783 6.547   0.60 14.93 ?  46  GLY   B N    1 
ATOM   4669 C CA   A GLY   B 1 46  ? 54.224 -23.849 6.904   0.40 16.45 ?  46  GLY   B CA   1 
ATOM   4670 C CA   B GLY   B 1 46  ? 54.228 -23.849 6.888   0.60 16.51 ?  46  GLY   B CA   1 
ATOM   4671 C C    A GLY   B 1 46  ? 54.263 -25.048 5.976   0.40 18.00 ?  46  GLY   B C    1 
ATOM   4672 C C    B GLY   B 1 46  ? 54.253 -25.016 5.923   0.60 18.29 ?  46  GLY   B C    1 
ATOM   4673 O O    A GLY   B 1 46  ? 55.332 -25.422 5.484   0.40 19.79 ?  46  GLY   B O    1 
ATOM   4674 O O    B GLY   B 1 46  ? 55.300 -25.336 5.349   0.60 20.59 ?  46  GLY   B O    1 
ATOM   4675 H H    A GLY   B 1 46  ? 52.521 -22.860 6.901   0.40 18.00 ?  46  GLY   B H    1 
ATOM   4676 H H    B GLY   B 1 46  ? 52.536 -22.840 6.932   0.60 17.89 ?  46  GLY   B H    1 
ATOM   4677 H HA2  A GLY   B 1 46  ? 55.119 -23.478 6.947   0.40 19.72 ?  46  GLY   B HA2  1 
ATOM   4678 H HA2  B GLY   B 1 46  ? 55.125 -23.485 6.940   0.60 19.78 ?  46  GLY   B HA2  1 
ATOM   4679 H HA3  A GLY   B 1 46  ? 53.994 -24.168 7.792   0.40 19.72 ?  46  GLY   B HA3  1 
ATOM   4680 H HA3  B GLY   B 1 46  ? 53.995 -24.198 7.763   0.60 19.78 ?  46  GLY   B HA3  1 
ATOM   4681 N N    . GLY   B 1 47  ? 53.109 -25.673 5.736   1.00 17.94 ?  47  GLY   B N    1 
ATOM   4682 C CA   . GLY   B 1 47  ? 53.051 -26.936 5.031   1.00 15.61 ?  47  GLY   B CA   1 
ATOM   4683 C C    . GLY   B 1 47  ? 52.135 -26.906 3.824   1.00 13.40 ?  47  GLY   B C    1 
ATOM   4684 O O    . GLY   B 1 47  ? 51.489 -25.899 3.532   1.00 13.23 ?  47  GLY   B O    1 
ATOM   4685 H H    A GLY   B 1 47  ? 52.338 -25.380 5.986   0.40 21.50 ?  47  GLY   B H    1 
ATOM   4686 H H    B GLY   B 1 47  ? 52.344 -25.406 6.029   0.60 21.50 ?  47  GLY   B H    1 
ATOM   4687 H HA2  . GLY   B 1 47  ? 53.939 -27.186 4.729   1.00 18.70 ?  47  GLY   B HA2  1 
ATOM   4688 H HA3  . GLY   B 1 47  ? 52.735 -27.626 5.637   1.00 18.70 ?  47  GLY   B HA3  1 
ATOM   4689 N N    . GLY   B 1 48  ? 52.087 -28.042 3.127   1.00 12.19 ?  48  GLY   B N    1 
ATOM   4690 C CA   . GLY   B 1 48  ? 51.165 -28.182 2.017   1.00 12.26 ?  48  GLY   B CA   1 
ATOM   4691 C C    . GLY   B 1 48  ? 51.296 -27.065 1.005   1.00 11.64 ?  48  GLY   B C    1 
ATOM   4692 O O    . GLY   B 1 48  ? 52.398 -26.596 0.691   1.00 11.99 ?  48  GLY   B O    1 
ATOM   4693 H H    . GLY   B 1 48  ? 52.585 -28.725 3.268   1.00 14.60 ?  48  GLY   B H    1 
ATOM   4694 H HA2  . GLY   B 1 48  ? 51.331 -29.027 1.564   1.00 14.68 ?  48  GLY   B HA2  1 
ATOM   4695 H HA3  . GLY   B 1 48  ? 50.256 -28.186 2.348   1.00 14.68 ?  48  GLY   B HA3  1 
ATOM   4696 N N    . VAL   B 1 49  ? 50.148 -26.633 0.481   1.00 11.49 ?  49  VAL   B N    1 
ATOM   4697 C CA   . VAL   B 1 49  ? 50.131 -25.604 -0.558  1.00 11.45 ?  49  VAL   B CA   1 
ATOM   4698 C C    . VAL   B 1 49  ? 50.792 -24.317 -0.067  1.00 11.04 ?  49  VAL   B C    1 
ATOM   4699 O O    . VAL   B 1 49  ? 51.581 -23.693 -0.789  1.00 11.57 ?  49  VAL   B O    1 
ATOM   4700 C CB   . VAL   B 1 49  ? 48.689 -25.351 -1.036  1.00 12.48 ?  49  VAL   B CB   1 
ATOM   4701 C CG1  . VAL   B 1 49  ? 48.617 -24.087 -1.894  1.00 12.73 ?  49  VAL   B CG1  1 
ATOM   4702 C CG2  . VAL   B 1 49  ? 48.150 -26.559 -1.787  1.00 14.36 ?  49  VAL   B CG2  1 
ATOM   4703 H H    . VAL   B 1 49  ? 49.364 -26.915 0.707   1.00 13.77 ?  49  VAL   B H    1 
ATOM   4704 H HA   . VAL   B 1 49  ? 50.639 -25.922 -1.319  1.00 13.72 ?  49  VAL   B HA   1 
ATOM   4705 H HB   . VAL   B 1 49  ? 48.124 -25.211 -0.262  1.00 14.95 ?  49  VAL   B HB   1 
ATOM   4706 H HG11 . VAL   B 1 49  ? 47.790 -24.094 -2.401  1.00 15.25 ?  49  VAL   B HG11 1 
ATOM   4707 H HG12 . VAL   B 1 49  ? 48.637 -23.305 -1.315  1.00 15.25 ?  49  VAL   B HG12 1 
ATOM   4708 H HG13 . VAL   B 1 49  ? 49.375 -24.068 -2.500  1.00 15.25 ?  49  VAL   B HG13 1 
ATOM   4709 H HG21 . VAL   B 1 49  ? 47.245 -26.370 -2.079  1.00 17.20 ?  49  VAL   B HG21 1 
ATOM   4710 H HG22 . VAL   B 1 49  ? 48.716 -26.728 -2.558  1.00 17.20 ?  49  VAL   B HG22 1 
ATOM   4711 H HG23 . VAL   B 1 49  ? 48.157 -27.325 -1.196  1.00 17.20 ?  49  VAL   B HG23 1 
ATOM   4712 N N    . ALA   B 1 50  ? 50.450 -23.872 1.147   1.00 10.66 ?  50  ALA   B N    1 
ATOM   4713 C CA   . ALA   B 1 50  ? 50.967 -22.592 1.624   1.00 10.49 ?  50  ALA   B CA   1 
ATOM   4714 C C    . ALA   B 1 50  ? 52.485 -22.619 1.726   1.00 10.75 ?  50  ALA   B C    1 
ATOM   4715 O O    . ALA   B 1 50  ? 53.161 -21.647 1.367   1.00 11.05 ?  50  ALA   B O    1 
ATOM   4716 C CB   . ALA   B 1 50  ? 50.347 -22.239 2.975   1.00 11.07 ?  50  ALA   B CB   1 
ATOM   4717 H H    . ALA   B 1 50  ? 49.940 -24.288 1.703   1.00 12.77 ?  50  ALA   B H    1 
ATOM   4718 H HA   . ALA   B 1 50  ? 50.729 -21.901 0.994   1.00 12.57 ?  50  ALA   B HA   1 
ATOM   4719 H HB1  . ALA   B 1 50  ? 50.703 -21.384 3.272   1.00 13.26 ?  50  ALA   B HB1  1 
ATOM   4720 H HB2  . ALA   B 1 50  ? 49.385 -22.178 2.875   1.00 13.26 ?  50  ALA   B HB2  1 
ATOM   4721 H HB3  . ALA   B 1 50  ? 50.571 -22.929 3.619   1.00 13.26 ?  50  ALA   B HB3  1 
ATOM   4722 N N    . GLY   B 1 51  ? 53.041 -23.712 2.235   1.00 11.48 ?  51  GLY   B N    1 
ATOM   4723 C CA   . GLY   B 1 51  ? 54.486 -23.805 2.312   1.00 12.27 ?  51  GLY   B CA   1 
ATOM   4724 C C    . GLY   B 1 51  ? 55.135 -23.761 0.944   1.00 12.14 ?  51  GLY   B C    1 
ATOM   4725 O O    . GLY   B 1 51  ? 56.172 -23.121 0.759   1.00 13.14 ?  51  GLY   B O    1 
ATOM   4726 H H    . GLY   B 1 51  ? 52.617 -24.397 2.537   1.00 13.76 ?  51  GLY   B H    1 
ATOM   4727 H HA2  . GLY   B 1 51  ? 54.833 -23.068 2.845   1.00 14.70 ?  51  GLY   B HA2  1 
ATOM   4728 H HA3  . GLY   B 1 51  ? 54.737 -24.637 2.749   1.00 14.70 ?  51  GLY   B HA3  1 
ATOM   4729 N N    . ALA   B 1 52  ? 54.530 -24.430 -0.036  1.00 11.61 ?  52  ALA   B N    1 
ATOM   4730 C CA   . ALA   B 1 52  ? 55.091 -24.433 -1.382  1.00 11.88 ?  52  ALA   B CA   1 
ATOM   4731 C C    . ALA   B 1 52  ? 55.011 -23.055 -2.029  1.00 11.62 ?  52  ALA   B C    1 
ATOM   4732 O O    . ALA   B 1 52  ? 55.985 -22.597 -2.647  1.00 12.22 ?  52  ALA   B O    1 
ATOM   4733 C CB   . ALA   B 1 52  ? 54.388 -25.475 -2.243  1.00 13.04 ?  52  ALA   B CB   1 
ATOM   4734 H H    . ALA   B 1 52  ? 53.802 -24.884 0.057   1.00 13.91 ?  52  ALA   B H    1 
ATOM   4735 H HA   . ALA   B 1 52  ? 56.027 -24.678 -1.321  1.00 14.23 ?  52  ALA   B HA   1 
ATOM   4736 H HB1  . ALA   B 1 52  ? 54.783 -25.456 -3.131  1.00 15.62 ?  52  ALA   B HB1  1 
ATOM   4737 H HB2  . ALA   B 1 52  ? 54.515 -26.349 -1.844  1.00 15.62 ?  52  ALA   B HB2  1 
ATOM   4738 H HB3  . ALA   B 1 52  ? 53.448 -25.260 -2.292  1.00 15.62 ?  52  ALA   B HB3  1 
ATOM   4739 N N    . LEU   B 1 53  ? 53.860 -22.383 -1.914  1.00 11.08 ?  53  LEU   B N    1 
ATOM   4740 C CA   . LEU   B 1 53  ? 53.746 -21.043 -2.482  1.00 11.31 ?  53  LEU   B CA   1 
ATOM   4741 C C    . LEU   B 1 53  ? 54.752 -20.101 -1.834  1.00 11.04 ?  53  LEU   B C    1 
ATOM   4742 O O    . LEU   B 1 53  ? 55.447 -19.344 -2.519  1.00 11.97 ?  53  LEU   B O    1 
ATOM   4743 C CB   . LEU   B 1 53  ? 52.324 -20.506 -2.306  1.00 11.72 ?  53  LEU   B CB   1 
ATOM   4744 C CG   . LEU   B 1 53  ? 51.192 -21.220 -3.055  1.00 12.19 ?  53  LEU   B CG   1 
ATOM   4745 C CD1  . LEU   B 1 53  ? 49.849 -20.597 -2.717  1.00 13.47 ?  53  LEU   B CD1  1 
ATOM   4746 C CD2  . LEU   B 1 53  ? 51.417 -21.194 -4.554  1.00 13.75 ?  53  LEU   B CD2  1 
ATOM   4747 H H    . LEU   B 1 53  ? 53.150 -22.680 -1.523  1.00 13.27 ?  53  LEU   B H    1 
ATOM   4748 H HA   . LEU   B 1 53  ? 53.938 -21.093 -3.434  1.00 13.55 ?  53  LEU   B HA   1 
ATOM   4749 H HB2  . LEU   B 1 53  ? 52.109 -20.550 -1.362  1.00 14.04 ?  53  LEU   B HB2  1 
ATOM   4750 H HB3  . LEU   B 1 53  ? 52.320 -19.587 -2.596  1.00 14.04 ?  53  LEU   B HB3  1 
ATOM   4751 H HG   . LEU   B 1 53  ? 51.160 -22.149 -2.774  1.00 14.61 ?  53  LEU   B HG   1 
ATOM   4752 H HD11 . LEU   B 1 53  ? 49.149 -21.064 -3.203  1.00 16.14 ?  53  LEU   B HD11 1 
ATOM   4753 H HD12 . LEU   B 1 53  ? 49.693 -20.671 -1.762  1.00 16.14 ?  53  LEU   B HD12 1 
ATOM   4754 H HD13 . LEU   B 1 53  ? 49.860 -19.661 -2.977  1.00 16.14 ?  53  LEU   B HD13 1 
ATOM   4755 H HD21 . LEU   B 1 53  ? 50.663 -21.612 -4.996  1.00 16.47 ?  53  LEU   B HD21 1 
ATOM   4756 H HD22 . LEU   B 1 53  ? 51.499 -20.272 -4.843  1.00 16.47 ?  53  LEU   B HD22 1 
ATOM   4757 H HD23 . LEU   B 1 53  ? 52.231 -21.679 -4.759  1.00 16.47 ?  53  LEU   B HD23 1 
ATOM   4758 N N    . ASN   B 1 54  ? 54.843 -20.132 -0.509  1.00 11.02 ?  54  ASN   B N    1 
ATOM   4759 C CA   . ASN   B 1 54  ? 55.755 -19.217 0.162   1.00 11.88 ?  54  ASN   B CA   1 
ATOM   4760 C C    . ASN   B 1 54  ? 57.199 -19.489 -0.233  1.00 11.98 ?  54  ASN   B C    1 
ATOM   4761 O O    . ASN   B 1 54  ? 57.972 -18.551 -0.466  1.00 12.44 ?  54  ASN   B O    1 
ATOM   4762 C CB   . ASN   B 1 54  ? 55.587 -19.296 1.671   1.00 12.48 ?  54  ASN   B CB   1 
ATOM   4763 C CG   . ASN   B 1 54  ? 56.565 -18.390 2.391   1.00 12.74 ?  54  ASN   B CG   1 
ATOM   4764 O OD1  . ASN   B 1 54  ? 56.588 -17.178 2.156   1.00 12.98 ?  54  ASN   B OD1  1 
ATOM   4765 N ND2  . ASN   B 1 54  ? 57.412 -18.976 3.231   1.00 14.21 ?  54  ASN   B ND2  1 
ATOM   4766 H H    . ASN   B 1 54  ? 54.402 -20.658 0.009   1.00 13.20 ?  54  ASN   B H    1 
ATOM   4767 H HA   . ASN   B 1 54  ? 55.538 -18.311 -0.115  1.00 14.23 ?  54  ASN   B HA   1 
ATOM   4768 H HB2  . ASN   B 1 54  ? 54.682 -19.013 1.904   1.00 14.95 ?  54  ASN   B HB2  1 
ATOM   4769 H HB3  . ASN   B 1 54  ? 55.735 -20.205 1.962   1.00 14.95 ?  54  ASN   B HB3  1 
ATOM   4770 H HD21 . ASN   B 1 54  ? 57.991 -18.508 3.657   1.00 17.03 ?  54  ASN   B HD21 1 
ATOM   4771 H HD22 . ASN   B 1 54  ? 57.373 -19.830 3.356   1.00 17.03 ?  54  ASN   B HD22 1 
ATOM   4772 N N    . LYS   B 1 55  ? 57.588 -20.764 -0.297  1.00 12.65 ?  55  LYS   B N    1 
ATOM   4773 C CA   . LYS   B 1 55  ? 58.945 -21.097 -0.713  1.00 13.91 ?  55  LYS   B CA   1 
ATOM   4774 C C    . LYS   B 1 55  ? 59.240 -20.549 -2.105  1.00 13.34 ?  55  LYS   B C    1 
ATOM   4775 O O    . LYS   B 1 55  ? 60.338 -20.040 -2.359  1.00 13.84 ?  55  LYS   B O    1 
ATOM   4776 C CB   . LYS   B 1 55  ? 59.150 -22.613 -0.661  1.00 14.98 ?  55  LYS   B CB   1 
ATOM   4777 C CG   . LYS   B 1 55  ? 60.543 -23.066 -1.033  1.00 18.93 ?  55  LYS   B CG   1 
ATOM   4778 C CD   . LYS   B 1 55  ? 60.708 -24.570 -0.893  1.00 22.25 ?  55  LYS   B CD   1 
ATOM   4779 C CE   . LYS   B 1 55  ? 60.584 -25.024 0.559   1.00 25.07 ?  55  LYS   B CE   1 
ATOM   4780 N NZ   . LYS   B 1 55  ? 61.053 -26.417 0.752   1.00 26.46 ?  55  LYS   B NZ   1 
ATOM   4781 H H    . LYS   B 1 55  ? 57.088 -21.439 -0.112  1.00 15.15 ?  55  LYS   B H    1 
ATOM   4782 H HA   . LYS   B 1 55  ? 59.571 -20.687 -0.095  1.00 16.67 ?  55  LYS   B HA   1 
ATOM   4783 H HB2  . LYS   B 1 55  ? 58.971 -22.911 0.245   1.00 17.95 ?  55  LYS   B HB2  1 
ATOM   4784 H HB3  . LYS   B 1 55  ? 58.529 -23.032 -1.273  1.00 17.95 ?  55  LYS   B HB3  1 
ATOM   4785 H HG2  . LYS   B 1 55  ? 60.720 -22.827 -1.957  1.00 22.69 ?  55  LYS   B HG2  1 
ATOM   4786 H HG3  . LYS   B 1 55  ? 61.186 -22.634 -0.448  1.00 22.69 ?  55  LYS   B HG3  1 
ATOM   4787 H HD2  . LYS   B 1 55  ? 60.019 -25.019 -1.409  1.00 26.67 ?  55  LYS   B HD2  1 
ATOM   4788 H HD3  . LYS   B 1 55  ? 61.587 -24.829 -1.213  1.00 26.67 ?  55  LYS   B HD3  1 
ATOM   4789 H HE2  . LYS   B 1 55  ? 61.118 -24.434 1.119   1.00 30.05 ?  55  LYS   B HE2  1 
ATOM   4790 H HE3  . LYS   B 1 55  ? 59.649 -24.972 0.826   1.00 30.05 ?  55  LYS   B HE3  1 
ATOM   4791 H HZ1  . LYS   B 1 55  ? 60.946 -26.654 1.602   1.00 31.73 ?  55  LYS   B HZ1  1 
ATOM   4792 H HZ2  . LYS   B 1 55  ? 60.581 -26.965 0.235   1.00 31.73 ?  55  LYS   B HZ2  1 
ATOM   4793 H HZ3  . LYS   B 1 55  ? 61.911 -26.477 0.536   1.00 31.73 ?  55  LYS   B HZ3  1 
ATOM   4794 N N    . ALA   B 1 56  ? 58.268 -20.633 -3.018  1.00 12.93 ?  56  ALA   B N    1 
ATOM   4795 C CA   . ALA   B 1 56  ? 58.488 -20.127 -4.369  1.00 13.82 ?  56  ALA   B CA   1 
ATOM   4796 C C    . ALA   B 1 56  ? 58.760 -18.629 -4.366  1.00 13.46 ?  56  ALA   B C    1 
ATOM   4797 O O    . ALA   B 1 56  ? 59.492 -18.129 -5.232  1.00 14.60 ?  56  ALA   B O    1 
ATOM   4798 C CB   . ALA   B 1 56  ? 57.296 -20.463 -5.263  1.00 14.77 ?  56  ALA   B CB   1 
ATOM   4799 H H    . ALA   B 1 56  ? 57.485 -20.971 -2.881  1.00 15.48 ?  56  ALA   B H    1 
ATOM   4800 H HA   . ALA   B 1 56  ? 59.267 -20.567 -4.738  1.00 16.55 ?  56  ALA   B HA   1 
ATOM   4801 H HB1  . ALA   B 1 56  ? 57.469 -20.124 -6.157  1.00 17.70 ?  56  ALA   B HB1  1 
ATOM   4802 H HB2  . ALA   B 1 56  ? 57.187 -21.428 -5.294  1.00 17.70 ?  56  ALA   B HB2  1 
ATOM   4803 H HB3  . ALA   B 1 56  ? 56.499 -20.052 -4.900  1.00 17.70 ?  56  ALA   B HB3  1 
ATOM   4804 N N    . THR   B 1 57  ? 58.190 -17.899 -3.403  1.00 13.43 ?  57  THR   B N    1 
ATOM   4805 C CA   . THR   B 1 57  ? 58.421 -16.465 -3.273  1.00 13.38 ?  57  THR   B CA   1 
ATOM   4806 C C    . THR   B 1 57  ? 59.672 -16.137 -2.466  1.00 14.37 ?  57  THR   B C    1 
ATOM   4807 O O    . THR   B 1 57  ? 59.901 -14.967 -2.152  1.00 15.07 ?  57  THR   B O    1 
ATOM   4808 C CB   . THR   B 1 57  ? 57.221 -15.750 -2.627  1.00 13.14 ?  57  THR   B CB   1 
ATOM   4809 O OG1  . THR   B 1 57  ? 57.207 -15.974 -1.209  1.00 13.02 ?  57  THR   B OG1  1 
ATOM   4810 C CG2  . THR   B 1 57  ? 55.903 -16.181 -3.252  1.00 12.98 ?  57  THR   B CG2  1 
ATOM   4811 H H    . THR   B 1 57  ? 57.651 -18.217 -2.810  1.00 16.09 ?  57  THR   B H    1 
ATOM   4812 H HA   . THR   B 1 57  ? 58.533 -16.092 -4.162  1.00 16.03 ?  57  THR   B HA   1 
ATOM   4813 H HB   . THR   B 1 57  ? 57.310 -14.799 -2.786  1.00 15.75 ?  57  THR   B HB   1 
ATOM   4814 H HG1  . THR   B 1 57  ? 57.147 -16.796 -1.048  1.00 15.60 ?  57  THR   B HG1  1 
ATOM   4815 H HG21 . THR   B 1 57  ? 55.176 -15.638 -2.911  1.00 15.55 ?  57  THR   B HG21 1 
ATOM   4816 H HG22 . THR   B 1 57  ? 55.942 -16.091 -4.215  1.00 15.55 ?  57  THR   B HG22 1 
ATOM   4817 H HG23 . THR   B 1 57  ? 55.720 -17.113 -3.035  1.00 15.55 ?  57  THR   B HG23 1 
ATOM   4818 N N    . ASN   B 1 58  ? 60.469 -17.137 -2.104  1.00 15.34 ?  58  ASN   B N    1 
ATOM   4819 C CA   . ASN   B 1 58  ? 61.671 -16.913 -1.302  1.00 18.95 ?  58  ASN   B CA   1 
ATOM   4820 C C    . ASN   B 1 58  ? 61.332 -16.213 0.014   1.00 15.89 ?  58  ASN   B C    1 
ATOM   4821 O O    . ASN   B 1 58  ? 62.062 -15.334 0.484   1.00 16.11 ?  58  ASN   B O    1 
ATOM   4822 C CB   . ASN   B 1 58  ? 62.741 -16.146 -2.086  1.00 28.88 ?  58  ASN   B CB   1 
ATOM   4823 C CG   . ASN   B 1 58  ? 64.119 -16.264 -1.463  1.00 38.59 ?  58  ASN   B CG   1 
ATOM   4824 O OD1  . ASN   B 1 58  ? 64.431 -17.254 -0.800  1.00 41.56 ?  58  ASN   B OD1  1 
ATOM   4825 N ND2  . ASN   B 1 58  ? 64.954 -15.251 -1.673  1.00 46.00 ?  58  ASN   B ND2  1 
ATOM   4826 H H    . ASN   B 1 58  ? 60.340 -17.963 -2.311  1.00 18.38 ?  58  ASN   B H    1 
ATOM   4827 H HA   . ASN   B 1 58  ? 62.049 -17.778 -1.082  1.00 22.71 ?  58  ASN   B HA   1 
ATOM   4828 H HB2  . ASN   B 1 58  ? 62.790 -16.499 -2.990  1.00 34.63 ?  58  ASN   B HB2  1 
ATOM   4829 H HB3  . ASN   B 1 58  ? 62.508 -15.206 -2.111  1.00 34.63 ?  58  ASN   B HB3  1 
ATOM   4830 H HD21 . ASN   B 1 58  ? 65.748 -15.272 -1.343  1.00 55.17 ?  58  ASN   B HD21 1 
ATOM   4831 H HD22 . ASN   B 1 58  ? 64.700 -14.575 -2.140  1.00 55.17 ?  58  ASN   B HD22 1 
ATOM   4832 N N    . ASN   B 1 59  ? 60.207 -16.608 0.613   1.00 14.72 ?  59  ASN   B N    1 
ATOM   4833 C CA   . ASN   B 1 59  ? 59.730 -16.152 1.918   1.00 14.69 ?  59  ASN   B CA   1 
ATOM   4834 C C    . ASN   B 1 59  ? 59.134 -14.744 1.873   1.00 13.77 ?  59  ASN   B C    1 
ATOM   4835 O O    . ASN   B 1 59  ? 58.702 -14.241 2.921   1.00 13.87 ?  59  ASN   B O    1 
ATOM   4836 C CB   . ASN   B 1 59  ? 60.804 -16.226 3.020   1.00 15.70 ?  59  ASN   B CB   1 
ATOM   4837 C CG   . ASN   B 1 59  ? 60.217 -16.401 4.400   1.00 16.78 ?  59  ASN   B CG   1 
ATOM   4838 O OD1  . ASN   B 1 59  ? 59.381 -17.275 4.618   1.00 17.07 ?  59  ASN   B OD1  1 
ATOM   4839 N ND2  . ASN   B 1 59  ? 60.645 -15.571 5.341   1.00 17.70 ?  59  ASN   B ND2  1 
ATOM   4840 H H    . ASN   B 1 59  ? 59.674 -17.187 0.260   1.00 17.64 ?  59  ASN   B H    1 
ATOM   4841 H HA   . ASN   B 1 59  ? 59.019 -16.753 2.191   1.00 17.60 ?  59  ASN   B HA   1 
ATOM   4842 H HB2  . ASN   B 1 59  ? 61.383 -16.986 2.855   1.00 18.82 ?  59  ASN   B HB2  1 
ATOM   4843 H HB3  . ASN   B 1 59  ? 61.316 -15.407 3.023   1.00 18.82 ?  59  ASN   B HB3  1 
ATOM   4844 H HD21 . ASN   B 1 59  ? 60.332 -15.629 6.143   1.00 21.22 ?  59  ASN   B HD21 1 
ATOM   4845 H HD22 . ASN   B 1 59  ? 61.231 -14.975 5.151   1.00 21.22 ?  59  ASN   B HD22 1 
ATOM   4846 N N    . ALA   B 1 60  ? 59.075 -14.093 0.708   1.00 13.55 ?  60  ALA   B N    1 
ATOM   4847 C CA   . ALA   B 1 60  ? 58.477 -12.760 0.646   1.00 13.59 ?  60  ALA   B CA   1 
ATOM   4848 C C    . ALA   B 1 60  ? 57.005 -12.786 1.041   1.00 12.52 ?  60  ALA   B C    1 
ATOM   4849 O O    . ALA   B 1 60  ? 56.496 -11.832 1.649   1.00 13.00 ?  60  ALA   B O    1 
ATOM   4850 C CB   . ALA   B 1 60  ? 58.642 -12.165 -0.752  1.00 14.47 ?  60  ALA   B CB   1 
ATOM   4851 H H    . ALA   B 1 60  ? 59.374 -14.395 -0.039  1.00 16.23 ?  60  ALA   B H    1 
ATOM   4852 H HA   . ALA   B 1 60  ? 58.937 -12.185 1.273   1.00 16.28 ?  60  ALA   B HA   1 
ATOM   4853 H HB1  . ALA   B 1 60  ? 58.243 -11.284 -0.767  1.00 17.34 ?  60  ALA   B HB1  1 
ATOM   4854 H HB2  . ALA   B 1 60  ? 59.593 -12.100 -0.953  1.00 17.34 ?  60  ALA   B HB2  1 
ATOM   4855 H HB3  . ALA   B 1 60  ? 58.209 -12.743 -1.396  1.00 17.34 ?  60  ALA   B HB3  1 
ATOM   4856 N N    . MET   B 1 61  ? 56.296 -13.863 0.690   1.00 12.33 ?  61  MET   B N    1 
ATOM   4857 C CA   . MET   B 1 61  ? 54.900 -13.991 1.086   1.00 12.08 ?  61  MET   B CA   1 
ATOM   4858 C C    . MET   B 1 61  ? 54.762 -14.007 2.607   1.00 12.19 ?  61  MET   B C    1 
ATOM   4859 O O    . MET   B 1 61  ? 53.865 -13.359 3.163   1.00 12.25 ?  61  MET   B O    1 
ATOM   4860 C CB   . MET   B 1 61  ? 54.319 -15.256 0.449   1.00 11.84 ?  61  MET   B CB   1 
ATOM   4861 C CG   . MET   B 1 61  ? 52.887 -15.566 0.879   1.00 12.03 ?  61  MET   B CG   1 
ATOM   4862 S SD   . MET   B 1 61  ? 52.241 -17.062 0.108   1.00 12.50 ?  61  MET   B SD   1 
ATOM   4863 C CE   . MET   B 1 61  ? 52.002 -16.489 -1.571  1.00 14.06 ?  61  MET   B CE   1 
ATOM   4864 H H    . MET   B 1 61  ? 56.603 -14.528 0.230   1.00 14.77 ?  61  MET   B H    1 
ATOM   4865 H HA   . MET   B 1 61  ? 54.409 -13.236 0.732   1.00 14.47 ?  61  MET   B HA   1 
ATOM   4866 H HB2  . MET   B 1 61  ? 54.318 -15.148 -0.518  1.00 14.19 ?  61  MET   B HB2  1 
ATOM   4867 H HB3  . MET   B 1 61  ? 54.874 -16.013 0.690   1.00 14.19 ?  61  MET   B HB3  1 
ATOM   4868 H HG2  . MET   B 1 61  ? 52.867 -15.701 1.841   1.00 14.42 ?  61  MET   B HG2  1 
ATOM   4869 H HG3  . MET   B 1 61  ? 52.314 -14.827 0.634   1.00 14.42 ?  61  MET   B HG3  1 
ATOM   4870 H HE1  . MET   B 1 61  ? 51.614 -17.206 -2.096  1.00 16.85 ?  61  MET   B HE1  1 
ATOM   4871 H HE2  . MET   B 1 61  ? 51.413 -15.723 -1.563  1.00 16.85 ?  61  MET   B HE2  1 
ATOM   4872 H HE3  . MET   B 1 61  ? 52.866 -16.240 -1.943  1.00 16.85 ?  61  MET   B HE3  1 
ATOM   4873 N N    . GLN   B 1 62  ? 55.645 -14.727 3.304   1.00 11.94 ?  62  GLN   B N    1 
ATOM   4874 C CA   . GLN   B 1 62  ? 55.544 -14.790 4.758   1.00 12.58 ?  62  GLN   B CA   1 
ATOM   4875 C C    . GLN   B 1 62  ? 55.824 -13.438 5.398   1.00 12.80 ?  62  GLN   B C    1 
ATOM   4876 O O    . GLN   B 1 62  ? 55.146 -13.047 6.354   1.00 12.91 ?  62  GLN   B O    1 
ATOM   4877 C CB   . GLN   B 1 62  ? 56.500 -15.840 5.319   1.00 12.68 ?  62  GLN   B CB   1 
ATOM   4878 C CG   . GLN   B 1 62  ? 56.281 -16.104 6.800   1.00 12.96 ?  62  GLN   B CG   1 
ATOM   4879 C CD   . GLN   B 1 62  ? 54.911 -16.715 7.046   1.00 12.59 ?  62  GLN   B CD   1 
ATOM   4880 O OE1  . GLN   B 1 62  ? 54.674 -17.871 6.705   1.00 12.85 ?  62  GLN   B OE1  1 
ATOM   4881 N NE2  . GLN   B 1 62  ? 53.991 -15.930 7.592   1.00 13.03 ?  62  GLN   B NE2  1 
ATOM   4882 H H    . GLN   B 1 62  ? 56.296 -15.178 2.964   1.00 14.30 ?  62  GLN   B H    1 
ATOM   4883 H HA   . GLN   B 1 62  ? 54.642 -15.048 4.995   1.00 15.06 ?  62  GLN   B HA   1 
ATOM   4884 H HB2  . GLN   B 1 62  ? 56.375 -16.675 4.842   1.00 15.19 ?  62  GLN   B HB2  1 
ATOM   4885 H HB3  . GLN   B 1 62  ? 57.417 -15.529 5.203   1.00 15.19 ?  62  GLN   B HB3  1 
ATOM   4886 H HG2  . GLN   B 1 62  ? 56.954 -16.728 7.115   1.00 15.53 ?  62  GLN   B HG2  1 
ATOM   4887 H HG3  . GLN   B 1 62  ? 56.338 -15.271 7.290   1.00 15.53 ?  62  GLN   B HG3  1 
ATOM   4888 H HE21 . GLN   B 1 62  ? 54.190 -15.122 7.807   1.00 15.61 ?  62  GLN   B HE21 1 
ATOM   4889 H HE22 . GLN   B 1 62  ? 53.203 -16.236 7.737   1.00 15.61 ?  62  GLN   B HE22 1 
ATOM   4890 N N    . VAL   B 1 63  ? 56.835 -12.717 4.906   1.00 13.12 ?  63  VAL   B N    1 
ATOM   4891 C CA   . VAL   B 1 63  ? 57.146 -11.406 5.472   1.00 13.92 ?  63  VAL   B CA   1 
ATOM   4892 C C    . VAL   B 1 63  ? 55.959 -10.467 5.298   1.00 13.46 ?  63  VAL   B C    1 
ATOM   4893 O O    . VAL   B 1 63  ? 55.555 -9.762  6.231   1.00 14.20 ?  63  VAL   B O    1 
ATOM   4894 C CB   . VAL   B 1 63  ? 58.434 -10.843 4.847   1.00 15.70 ?  63  VAL   B CB   1 
ATOM   4895 C CG1  . VAL   B 1 63  ? 58.654 -9.401  5.288   1.00 16.51 ?  63  VAL   B CG1  1 
ATOM   4896 C CG2  . VAL   B 1 63  ? 59.619 -11.715 5.234   1.00 16.42 ?  63  VAL   B CG2  1 
ATOM   4897 H H    . VAL   B 1 63  ? 57.343 -12.955 4.253   1.00 15.72 ?  63  VAL   B H    1 
ATOM   4898 H HA   . VAL   B 1 63  ? 57.301 -11.507 6.422   1.00 16.68 ?  63  VAL   B HA   1 
ATOM   4899 H HB   . VAL   B 1 63  ? 58.354 -10.852 3.882   1.00 18.81 ?  63  VAL   B HB   1 
ATOM   4900 H HG11 . VAL   B 1 63  ? 59.571 -9.149  5.098   1.00 19.79 ?  63  VAL   B HG11 1 
ATOM   4901 H HG12 . VAL   B 1 63  ? 58.046 -8.822  4.803   1.00 19.79 ?  63  VAL   B HG12 1 
ATOM   4902 H HG13 . VAL   B 1 63  ? 58.487 -9.333  6.243   1.00 19.79 ?  63  VAL   B HG13 1 
ATOM   4903 H HG21 . VAL   B 1 63  ? 60.428 -11.335 4.853   1.00 19.68 ?  63  VAL   B HG21 1 
ATOM   4904 H HG22 . VAL   B 1 63  ? 59.693 -11.737 6.203   1.00 19.68 ?  63  VAL   B HG22 1 
ATOM   4905 H HG23 . VAL   B 1 63  ? 59.480 -12.609 4.892   1.00 19.68 ?  63  VAL   B HG23 1 
ATOM   4906 N N    . GLU   B 1 64  ? 55.379 -10.454 4.096   1.00 12.92 ?  64  GLU   B N    1 
ATOM   4907 C CA   . GLU   B 1 64  ? 54.211 -9.616  3.829   1.00 12.50 ?  64  GLU   B CA   1 
ATOM   4908 C C    . GLU   B 1 64  ? 53.031 -10.019 4.706   1.00 12.54 ?  64  GLU   B C    1 
ATOM   4909 O O    . GLU   B 1 64  ? 52.288 -9.157  5.210   1.00 12.98 ?  64  GLU   B O    1 
ATOM   4910 C CB   . GLU   B 1 64  ? 53.846 -9.751  2.351   1.00 12.83 ?  64  GLU   B CB   1 
ATOM   4911 C CG   . GLU   B 1 64  ? 52.585 -9.016  1.926   1.00 13.32 ?  64  GLU   B CG   1 
ATOM   4912 C CD   . GLU   B 1 64  ? 52.039 -9.501  0.586   1.00 14.17 ?  64  GLU   B CD   1 
ATOM   4913 O OE1  . GLU   B 1 64  ? 52.213 -10.701 0.247   1.00 15.35 ?  64  GLU   B OE1  1 
ATOM   4914 O OE2  . GLU   B 1 64  ? 51.404 -8.678  -0.124  1.00 15.00 -1 64  GLU   B OE2  1 
ATOM   4915 H H    . GLU   B 1 64  ? 55.643 -10.919 3.420   1.00 15.48 ?  64  GLU   B H    1 
ATOM   4916 H HA   . GLU   B 1 64  ? 54.428 -8.689  4.014   1.00 14.98 ?  64  GLU   B HA   1 
ATOM   4917 H HB2  . GLU   B 1 64  ? 54.578 -9.391  1.820   1.00 15.37 ?  64  GLU   B HB2  1 
ATOM   4918 H HB3  . GLU   B 1 64  ? 53.726 -10.686 2.147   1.00 15.37 ?  64  GLU   B HB3  1 
ATOM   4919 H HG2  . GLU   B 1 64  ? 51.887 -9.147  2.590   1.00 15.96 ?  64  GLU   B HG2  1 
ATOM   4920 H HG3  . GLU   B 1 64  ? 52.779 -8.069  1.840   1.00 15.96 ?  64  GLU   B HG3  1 
ATOM   4921 N N    . SER   B 1 65  ? 52.844 -11.329 4.887   1.00 12.33 ?  65  SER   B N    1 
ATOM   4922 C CA   . SER   B 1 65  ? 51.740 -11.844 5.688   1.00 12.20 ?  65  SER   B CA   1 
ATOM   4923 C C    . SER   B 1 65  ? 51.882 -11.451 7.153   1.00 12.26 ?  65  SER   B C    1 
ATOM   4924 O O    . SER   B 1 65  ? 50.890 -11.086 7.798   1.00 12.79 ?  65  SER   B O    1 
ATOM   4925 C CB   . SER   B 1 65  ? 51.656 -13.366 5.544   1.00 12.49 ?  65  SER   B CB   1 
ATOM   4926 O OG   . SER   B 1 65  ? 51.315 -13.750 4.218   1.00 12.52 ?  65  SER   B OG   1 
ATOM   4927 H H    . SER   B 1 65  ? 53.356 -11.947 4.561   1.00 14.77 ?  65  SER   B H    1 
ATOM   4928 H HA   . SER   B 1 65  ? 50.911 -11.470 5.356   1.00 14.61 ?  65  SER   B HA   1 
ATOM   4929 H HB2  . SER   B 1 65  ? 52.516 -13.752 5.771   1.00 14.97 ?  65  SER   B HB2  1 
ATOM   4930 H HB3  . SER   B 1 65  ? 50.975 -13.700 6.150   1.00 14.97 ?  65  SER   B HB3  1 
ATOM   4931 H HG   . SER   B 1 65  ? 51.901 -13.459 3.681   1.00 15.00 ?  65  SER   B HG   1 
ATOM   4932 N N    . ASP   B 1 66  ? 53.092 -11.557 7.712   1.00 12.65 ?  66  ASP   B N    1 
ATOM   4933 C CA   . ASP   B 1 66  ? 53.289 -11.177 9.108   1.00 13.28 ?  66  ASP   B CA   1 
ATOM   4934 C C    . ASP   B 1 66  ? 52.976 -9.700  9.323   1.00 13.58 ?  66  ASP   B C    1 
ATOM   4935 O O    . ASP   B 1 66  ? 52.406 -9.316  10.351  1.00 13.76 ?  66  ASP   B O    1 
ATOM   4936 C CB   . ASP   B 1 66  ? 54.722 -11.487 9.542   1.00 14.65 ?  66  ASP   B CB   1 
ATOM   4937 C CG   . ASP   B 1 66  ? 54.982 -12.976 9.703   1.00 16.67 ?  66  ASP   B CG   1 
ATOM   4938 O OD1  . ASP   B 1 66  ? 54.021 -13.779 9.645   1.00 17.26 ?  66  ASP   B OD1  1 
ATOM   4939 O OD2  . ASP   B 1 66  ? 56.160 -13.346 9.895   1.00 19.14 -1 66  ASP   B OD2  1 
ATOM   4940 H H    . ASP   B 1 66  ? 53.793 -11.850 7.312   1.00 15.16 ?  66  ASP   B H    1 
ATOM   4941 H HA   . ASP   B 1 66  ? 52.692 -11.691 9.669   1.00 15.92 ?  66  ASP   B HA   1 
ATOM   4942 H HB2  . ASP   B 1 66  ? 55.341 -11.146 8.873   1.00 17.55 ?  66  ASP   B HB2  1 
ATOM   4943 H HB3  . ASP   B 1 66  ? 54.898 -11.059 10.397  1.00 17.55 ?  66  ASP   B HB3  1 
ATOM   4944 N N    . ASP   B 1 67  ? 53.351 -8.847  8.368   1.00 13.15 ?  67  ASP   B N    1 
ATOM   4945 C CA   . ASP   B 1 67  ? 52.999 -7.436  8.481   1.00 13.84 ?  67  ASP   B CA   1 
ATOM   4946 C C    . ASP   B 1 67  ? 51.486 -7.231  8.391   1.00 13.65 ?  67  ASP   B C    1 
ATOM   4947 O O    . ASP   B 1 67  ? 50.913 -6.425  9.136   1.00 14.34 ?  67  ASP   B O    1 
ATOM   4948 C CB   . ASP   B 1 67  ? 53.722 -6.646  7.402   1.00 15.44 ?  67  ASP   B CB   1 
ATOM   4949 C CG   . ASP   B 1 67  ? 53.311 -5.207  7.390   1.00 17.28 ?  67  ASP   B CG   1 
ATOM   4950 O OD1  . ASP   B 1 67  ? 53.811 -4.433  8.238   1.00 18.13 ?  67  ASP   B OD1  1 
ATOM   4951 O OD2  . ASP   B 1 67  ? 52.463 -4.868  6.546   1.00 18.42 -1 67  ASP   B OD2  1 
ATOM   4952 H H    . ASP   B 1 67  ? 53.807 -9.056  7.667   1.00 15.76 ?  67  ASP   B H    1 
ATOM   4953 H HA   . ASP   B 1 67  ? 53.295 -7.106  9.341   1.00 16.58 ?  67  ASP   B HA   1 
ATOM   4954 H HB2  . ASP   B 1 67  ? 54.681 -6.681  7.563   1.00 18.50 ?  67  ASP   B HB2  1 
ATOM   4955 H HB3  . ASP   B 1 67  ? 53.521 -7.024  6.531   1.00 18.50 ?  67  ASP   B HB3  1 
ATOM   4956 N N    . TYR   B 1 68  ? 50.815 -7.955  7.491   1.00 13.49 ?  68  TYR   B N    1 
ATOM   4957 C CA   . TYR   B 1 68  ? 49.358 -7.873  7.417   1.00 13.94 ?  68  TYR   B CA   1 
ATOM   4958 C C    . TYR   B 1 68  ? 48.722 -8.214  8.762   1.00 13.36 ?  68  TYR   B C    1 
ATOM   4959 O O    . TYR   B 1 68  ? 47.780 -7.546  9.208   1.00 14.06 ?  68  TYR   B O    1 
ATOM   4960 C CB   . TYR   B 1 68  ? 48.823 -8.810  6.326   1.00 14.79 ?  68  TYR   B CB   1 
ATOM   4961 C CG   . TYR   B 1 68  ? 47.310 -8.953  6.382   1.00 15.88 ?  68  TYR   B CG   1 
ATOM   4962 C CD1  . TYR   B 1 68  ? 46.710 -9.899  7.211   1.00 16.86 ?  68  TYR   B CD1  1 
ATOM   4963 C CD2  . TYR   B 1 68  ? 46.487 -8.118  5.649   1.00 17.04 ?  68  TYR   B CD2  1 
ATOM   4964 C CE1  . TYR   B 1 68  ? 45.345 -10.017 7.298   1.00 18.26 ?  68  TYR   B CE1  1 
ATOM   4965 C CE2  . TYR   B 1 68  ? 45.101 -8.241  5.722   1.00 17.59 ?  68  TYR   B CE2  1 
ATOM   4966 C CZ   . TYR   B 1 68  ? 44.549 -9.189  6.554   1.00 18.04 ?  68  TYR   B CZ   1 
ATOM   4967 O OH   . TYR   B 1 68  ? 43.183 -9.316  6.650   1.00 19.08 ?  68  TYR   B OH   1 
ATOM   4968 H H    . TYR   B 1 68  ? 51.174 -8.500  6.922   1.00 16.16 ?  68  TYR   B H    1 
ATOM   4969 H HA   . TYR   B 1 68  ? 49.106 -6.969  7.190   1.00 16.71 ?  68  TYR   B HA   1 
ATOM   4970 H HB2  . TYR   B 1 68  ? 49.054 -8.450  5.458   1.00 17.72 ?  68  TYR   B HB2  1 
ATOM   4971 H HB3  . TYR   B 1 68  ? 49.211 -9.690  6.440   1.00 17.72 ?  68  TYR   B HB3  1 
ATOM   4972 H HD1  . TYR   B 1 68  ? 47.246 -10.466 7.721   1.00 20.21 ?  68  TYR   B HD1  1 
ATOM   4973 H HD2  . TYR   B 1 68  ? 46.864 -7.477  5.096   1.00 20.42 ?  68  TYR   B HD2  1 
ATOM   4974 H HE1  . TYR   B 1 68  ? 44.962 -10.667 7.848   1.00 21.89 ?  68  TYR   B HE1  1 
ATOM   4975 H HE2  . TYR   B 1 68  ? 44.553 -7.680  5.224   1.00 21.08 ?  68  TYR   B HE2  1 
ATOM   4976 H HH   . TYR   B 1 68  ? 42.796 -8.767  6.142   1.00 22.88 ?  68  TYR   B HH   1 
ATOM   4977 N N    . ILE   B 1 69  ? 49.200 -9.286  9.401   1.00 13.40 ?  69  ILE   B N    1 
ATOM   4978 C CA   . ILE   B 1 69  ? 48.641 -9.723  10.677  1.00 14.00 ?  69  ILE   B CA   1 
ATOM   4979 C C    . ILE   B 1 69  ? 48.898 -8.691  11.767  1.00 13.58 ?  69  ILE   B C    1 
ATOM   4980 O O    . ILE   B 1 69  ? 48.029 -8.427  12.604  1.00 14.19 ?  69  ILE   B O    1 
ATOM   4981 C CB   . ILE   B 1 69  ? 49.205 -11.107 11.056  1.00 15.13 ?  69  ILE   B CB   1 
ATOM   4982 C CG1  . ILE   B 1 69  ? 48.678 -12.194 10.113  1.00 15.69 ?  69  ILE   B CG1  1 
ATOM   4983 C CG2  . ILE   B 1 69  ? 48.906 -11.440 12.510  1.00 16.37 ?  69  ILE   B CG2  1 
ATOM   4984 C CD1  . ILE   B 1 69  ? 47.213 -12.524 10.287  1.00 15.85 ?  69  ILE   B CD1  1 
ATOM   4985 H H    . ILE   B 1 69  ? 49.851 -9.774  9.121   1.00 16.06 ?  69  ILE   B H    1 
ATOM   4986 H HA   . ILE   B 1 69  ? 47.680 -9.811  10.578  1.00 16.78 ?  69  ILE   B HA   1 
ATOM   4987 H HB   . ILE   B 1 69  ? 50.168 -11.069 10.954  1.00 18.13 ?  69  ILE   B HB   1 
ATOM   4988 H HG12 . ILE   B 1 69  ? 48.806 -11.897 9.198   1.00 18.81 ?  69  ILE   B HG12 1 
ATOM   4989 H HG13 . ILE   B 1 69  ? 49.186 -13.006 10.266  1.00 18.81 ?  69  ILE   B HG13 1 
ATOM   4990 H HG21 . ILE   B 1 69  ? 49.047 -12.392 12.644  1.00 19.62 ?  69  ILE   B HG21 1 
ATOM   4991 H HG22 . ILE   B 1 69  ? 49.505 -10.937 13.082  1.00 19.62 ?  69  ILE   B HG22 1 
ATOM   4992 H HG23 . ILE   B 1 69  ? 47.985 -11.213 12.704  1.00 19.62 ?  69  ILE   B HG23 1 
ATOM   4993 H HD11 . ILE   B 1 69  ? 46.965 -13.188 9.627   1.00 19.00 ?  69  ILE   B HD11 1 
ATOM   4994 H HD12 . ILE   B 1 69  ? 47.074 -12.880 11.180  1.00 19.00 ?  69  ILE   B HD12 1 
ATOM   4995 H HD13 . ILE   B 1 69  ? 46.688 -11.721 10.164  1.00 19.00 ?  69  ILE   B HD13 1 
ATOM   4996 N N    . ALA   B 1 70  ? 50.098 -8.109  11.795  1.00 13.47 ?  70  ALA   B N    1 
ATOM   4997 C CA   . ALA   B 1 70  ? 50.379 -7.076  12.784  1.00 13.49 ?  70  ALA   B CA   1 
ATOM   4998 C C    . ALA   B 1 70  ? 49.380 -5.930  12.676  1.00 13.55 ?  70  ALA   B C    1 
ATOM   4999 O O    . ALA   B 1 70  ? 48.933 -5.390  13.693  1.00 13.75 ?  70  ALA   B O    1 
ATOM   5000 C CB   . ALA   B 1 70  ? 51.814 -6.574  12.621  1.00 13.92 ?  70  ALA   B CB   1 
ATOM   5001 H H    . ALA   B 1 70  ? 50.744 -8.297  11.268  1.00 16.13 ?  70  ALA   B H    1 
ATOM   5002 H HA   . ALA   B 1 70  ? 50.304 -7.458  13.673  1.00 16.16 ?  70  ALA   B HA   1 
ATOM   5003 H HB1  . ALA   B 1 70  ? 52.003 -5.919  13.310  1.00 16.68 ?  70  ALA   B HB1  1 
ATOM   5004 H HB2  . ALA   B 1 70  ? 52.425 -7.326  12.706  1.00 16.68 ?  70  ALA   B HB2  1 
ATOM   5005 H HB3  . ALA   B 1 70  ? 51.912 -6.172  11.743  1.00 16.68 ?  70  ALA   B HB3  1 
ATOM   5006 N N    . THR   B 1 71  ? 49.007 -5.554  11.452  1.00 13.89 ?  71  THR   B N    1 
ATOM   5007 C CA   . THR   B 1 71  ? 48.118 -4.414  11.252  1.00 14.64 ?  71  THR   B CA   1 
ATOM   5008 C C    . THR   B 1 71  ? 46.650 -4.777  11.454  1.00 15.19 ?  71  THR   B C    1 
ATOM   5009 O O    . THR   B 1 71  ? 45.874 -3.959  11.966  1.00 16.80 ?  71  THR   B O    1 
ATOM   5010 C CB   . THR   B 1 71  ? 48.333 -3.837  9.851   1.00 16.54 ?  71  THR   B CB   1 
ATOM   5011 O OG1  . THR   B 1 71  ? 49.655 -3.296  9.761   1.00 18.62 ?  71  THR   B OG1  1 
ATOM   5012 C CG2  . THR   B 1 71  ? 47.309 -2.752  9.533   1.00 17.47 ?  71  THR   B CG2  1 
ATOM   5013 H H    . THR   B 1 71  ? 49.258 -5.944  10.729  1.00 16.65 ?  71  THR   B H    1 
ATOM   5014 H HA   . THR   B 1 71  ? 48.346 -3.724  11.895  1.00 17.54 ?  71  THR   B HA   1 
ATOM   5015 H HB   . THR   B 1 71  ? 48.242 -4.545  9.195   1.00 19.83 ?  71  THR   B HB   1 
ATOM   5016 H HG1  . THR   B 1 71  ? 49.784 -2.966  8.996   1.00 22.32 ?  71  THR   B HG1  1 
ATOM   5017 H HG21 . THR   B 1 71  ? 47.613 -2.224  8.776   1.00 20.93 ?  71  THR   B HG21 1 
ATOM   5018 H HG22 . THR   B 1 71  ? 46.455 -3.151  9.315   1.00 20.93 ?  71  THR   B HG22 1 
ATOM   5019 H HG23 . THR   B 1 71  ? 47.201 -2.164  10.298  1.00 20.93 ?  71  THR   B HG23 1 
ATOM   5020 N N    . ASN   B 1 72  ? 46.251 -5.990  11.061  1.00 14.80 ?  72  ASN   B N    1 
ATOM   5021 C CA   . ASN   B 1 72  ? 44.848 -6.344  10.930  1.00 15.32 ?  72  ASN   B CA   1 
ATOM   5022 C C    . ASN   B 1 72  ? 44.372 -7.451  11.861  1.00 15.51 ?  72  ASN   B C    1 
ATOM   5023 O O    . ASN   B 1 72  ? 43.155 -7.609  12.026  1.00 16.70 ?  72  ASN   B O    1 
ATOM   5024 C CB   . ASN   B 1 72  ? 44.543 -6.755  9.481   1.00 16.04 ?  72  ASN   B CB   1 
ATOM   5025 C CG   . ASN   B 1 72  ? 44.816 -5.638  8.498   1.00 17.42 ?  72  ASN   B CG   1 
ATOM   5026 O OD1  . ASN   B 1 72  ? 45.822 -5.644  7.785   1.00 18.35 ?  72  ASN   B OD1  1 
ATOM   5027 N ND2  . ASN   B 1 72  ? 43.940 -4.650  8.483   1.00 18.64 ?  72  ASN   B ND2  1 
ATOM   5028 H H    . ASN   B 1 72  ? 46.792 -6.634  10.851  1.00 17.74 ?  72  ASN   B H    1 
ATOM   5029 H HA   . ASN   B 1 72  ? 44.321 -5.556  11.118  1.00 18.36 ?  72  ASN   B HA   1 
ATOM   5030 H HB2  . ASN   B 1 72  ? 45.103 -7.510  9.236   1.00 19.22 ?  72  ASN   B HB2  1 
ATOM   5031 H HB3  . ASN   B 1 72  ? 43.608 -6.996  9.407   1.00 19.22 ?  72  ASN   B HB3  1 
ATOM   5032 H HD21 . ASN   B 1 72  ? 44.039 -3.988  7.941   1.00 22.34 ?  72  ASN   B HD21 1 
ATOM   5033 H HD22 . ASN   B 1 72  ? 43.246 -4.680  8.995   1.00 22.34 ?  72  ASN   B HD22 1 
ATOM   5034 N N    . GLY   B 1 73  ? 45.274 -8.207  12.479  1.00 15.25 ?  73  GLY   B N    1 
ATOM   5035 C CA   . GLY   B 1 73  ? 44.877 -9.347  13.267  1.00 14.62 ?  73  GLY   B CA   1 
ATOM   5036 C C    . GLY   B 1 73  ? 44.515 -10.527 12.393  1.00 13.16 ?  73  GLY   B C    1 
ATOM   5037 O O    . GLY   B 1 73  ? 44.505 -10.438 11.163  1.00 13.38 ?  73  GLY   B O    1 
ATOM   5038 H H    . GLY   B 1 73  ? 46.126 -8.075  12.449  1.00 18.27 ?  73  GLY   B H    1 
ATOM   5039 H HA2  . GLY   B 1 73  ? 45.603 -9.604  13.855  1.00 17.52 ?  73  GLY   B HA2  1 
ATOM   5040 H HA3  . GLY   B 1 73  ? 44.106 -9.115  13.808  1.00 17.52 ?  73  GLY   B HA3  1 
ATOM   5041 N N    . PRO   B 1 74  ? 44.212 -11.659 13.021  1.00 13.60 ?  74  PRO   B N    1 
ATOM   5042 C CA   . PRO   B 1 74  ? 43.967 -12.887 12.263  1.00 13.07 ?  74  PRO   B CA   1 
ATOM   5043 C C    . PRO   B 1 74  ? 42.662 -12.832 11.480  1.00 12.52 ?  74  PRO   B C    1 
ATOM   5044 O O    . PRO   B 1 74  ? 41.720 -12.098 11.803  1.00 13.75 ?  74  PRO   B O    1 
ATOM   5045 C CB   . PRO   B 1 74  ? 43.902 -13.960 13.354  1.00 14.39 ?  74  PRO   B CB   1 
ATOM   5046 C CG   . PRO   B 1 74  ? 43.442 -13.223 14.565  1.00 15.91 ?  74  PRO   B CG   1 
ATOM   5047 C CD   . PRO   B 1 74  ? 44.109 -11.882 14.471  1.00 14.93 ?  74  PRO   B CD   1 
ATOM   5048 H HA   . PRO   B 1 74  ? 44.710 -13.071 11.660  1.00 15.66 ?  74  PRO   B HA   1 
ATOM   5049 H HB2  . PRO   B 1 74  ? 43.266 -14.644 13.099  1.00 17.24 ?  74  PRO   B HB2  1 
ATOM   5050 H HB3  . PRO   B 1 74  ? 44.785 -14.339 13.493  1.00 17.24 ?  74  PRO   B HB3  1 
ATOM   5051 H HG2  . PRO   B 1 74  ? 42.477 -13.130 14.541  1.00 19.07 ?  74  PRO   B HG2  1 
ATOM   5052 H HG3  . PRO   B 1 74  ? 43.725 -13.696 15.360  1.00 19.07 ?  74  PRO   B HG3  1 
ATOM   5053 H HD2  . PRO   B 1 74  ? 43.555 -11.199 14.885  1.00 17.89 ?  74  PRO   B HD2  1 
ATOM   5054 H HD3  . PRO   B 1 74  ? 44.992 -11.913 14.872  1.00 17.89 ?  74  PRO   B HD3  1 
ATOM   5055 N N    . LEU   B 1 75  ? 42.631 -13.641 10.425  1.00 11.96 ?  75  LEU   B N    1 
ATOM   5056 C CA   . LEU   B 1 75  ? 41.416 -13.859 9.662   1.00 12.15 ?  75  LEU   B CA   1 
ATOM   5057 C C    . LEU   B 1 75  ? 40.450 -14.726 10.465  1.00 12.36 ?  75  LEU   B C    1 
ATOM   5058 O O    . LEU   B 1 75  ? 40.799 -15.285 11.508  1.00 13.42 ?  75  LEU   B O    1 
ATOM   5059 C CB   . LEU   B 1 75  ? 41.740 -14.570 8.349   1.00 12.31 ?  75  LEU   B CB   1 
ATOM   5060 C CG   . LEU   B 1 75  ? 42.568 -13.811 7.309   1.00 13.99 ?  75  LEU   B CG   1 
ATOM   5061 C CD1  . LEU   B 1 75  ? 42.726 -14.639 6.034   1.00 15.61 ?  75  LEU   B CD1  1 
ATOM   5062 C CD2  . LEU   B 1 75  ? 41.976 -12.465 6.992   1.00 17.14 ?  75  LEU   B CD2  1 
ATOM   5063 H H    . LEU   B 1 75  ? 43.306 -14.085 10.126  1.00 14.33 ?  75  LEU   B H    1 
ATOM   5064 H HA   . LEU   B 1 75  ? 40.986 -13.014 9.466   1.00 14.55 ?  75  LEU   B HA   1 
ATOM   5065 H HB2  . LEU   B 1 75  ? 42.227 -15.384 8.559   1.00 14.74 ?  75  LEU   B HB2  1 
ATOM   5066 H HB3  . LEU   B 1 75  ? 40.900 -14.813 7.920   1.00 14.74 ?  75  LEU   B HB3  1 
ATOM   5067 H HG   . LEU   B 1 75  ? 43.453 -13.666 7.669   1.00 16.77 ?  75  LEU   B HG   1 
ATOM   5068 H HD11 . LEU   B 1 75  ? 43.259 -14.136 5.394   1.00 18.70 ?  75  LEU   B HD11 1 
ATOM   5069 H HD12 . LEU   B 1 75  ? 43.174 -15.473 6.248   1.00 18.70 ?  75  LEU   B HD12 1 
ATOM   5070 H HD13 . LEU   B 1 75  ? 41.851 -14.822 5.659   1.00 18.70 ?  75  LEU   B HD13 1 
ATOM   5071 H HD21 . LEU   B 1 75  ? 42.459 -12.073 6.250   1.00 20.55 ?  75  LEU   B HD21 1 
ATOM   5072 H HD22 . LEU   B 1 75  ? 41.041 -12.581 6.756   1.00 20.55 ?  75  LEU   B HD22 1 
ATOM   5073 H HD23 . LEU   B 1 75  ? 42.050 -11.898 7.776   1.00 20.55 ?  75  LEU   B HD23 1 
ATOM   5074 N N    . LYS   B 1 76  ? 39.219 -14.833 9.959   1.00 13.57 ?  76  LYS   B N    1 
ATOM   5075 C CA   . LYS   B 1 76  ? 38.233 -15.801 10.425  1.00 14.59 ?  76  LYS   B CA   1 
ATOM   5076 C C    . LYS   B 1 76  ? 38.328 -17.067 9.574   1.00 13.03 ?  76  LYS   B C    1 
ATOM   5077 O O    . LYS   B 1 76  ? 38.588 -16.997 8.375   1.00 12.54 ?  76  LYS   B O    1 
ATOM   5078 C CB   . LYS   B 1 76  ? 36.811 -15.231 10.247  1.00 17.76 ?  76  LYS   B CB   1 
ATOM   5079 C CG   . LYS   B 1 76  ? 36.547 -13.828 10.826  1.00 19.99 ?  76  LYS   B CG   1 
ATOM   5080 C CD   . LYS   B 1 76  ? 35.148 -13.283 10.453  1.00 21.66 ?  76  LYS   B CD   1 
ATOM   5081 C CE   . LYS   B 1 76  ? 34.897 -11.903 11.048  1.00 23.70 ?  76  LYS   B CE   1 
ATOM   5082 N NZ   . LYS   B 1 76  ? 33.606 -11.308 10.593  1.00 24.62 ?  76  LYS   B NZ   1 
ATOM   5083 H H    . LYS   B 1 76  ? 38.923 -14.338 9.325   1.00 16.26 ?  76  LYS   B H    1 
ATOM   5084 H HA   . LYS   B 1 76  ? 38.377 -16.026 11.360  1.00 17.49 ?  76  LYS   B HA   1 
ATOM   5085 H HB2  . LYS   B 1 76  ? 36.620 -15.188 9.297   1.00 21.29 ?  76  LYS   B HB2  1 
ATOM   5086 H HB3  . LYS   B 1 76  ? 36.183 -15.837 10.671  1.00 21.29 ?  76  LYS   B HB3  1 
ATOM   5087 H HG2  . LYS   B 1 76  ? 36.605 -13.868 11.793  1.00 23.96 ?  76  LYS   B HG2  1 
ATOM   5088 H HG3  . LYS   B 1 76  ? 37.211 -13.211 10.479  1.00 23.96 ?  76  LYS   B HG3  1 
ATOM   5089 H HD2  . LYS   B 1 76  ? 35.079 -13.211 9.488   1.00 25.96 ?  76  LYS   B HD2  1 
ATOM   5090 H HD3  . LYS   B 1 76  ? 34.468 -13.885 10.793  1.00 25.96 ?  76  LYS   B HD3  1 
ATOM   5091 H HE2  . LYS   B 1 76  ? 34.870 -11.976 12.015  1.00 28.41 ?  76  LYS   B HE2  1 
ATOM   5092 H HE3  . LYS   B 1 76  ? 35.614 -11.307 10.779  1.00 28.41 ?  76  LYS   B HE3  1 
ATOM   5093 H HZ1  . LYS   B 1 76  ? 33.494 -10.504 10.961  1.00 29.52 ?  76  LYS   B HZ1  1 
ATOM   5094 H HZ2  . LYS   B 1 76  ? 33.605 -11.222 9.707   1.00 29.52 ?  76  LYS   B HZ2  1 
ATOM   5095 H HZ3  . LYS   B 1 76  ? 32.927 -11.831 10.833  1.00 29.52 ?  76  LYS   B HZ3  1 
ATOM   5096 N N    . VAL   B 1 77  ? 38.079 -18.230 10.189  1.00 13.08 ?  77  VAL   B N    1 
ATOM   5097 C CA   . VAL   B 1 77  ? 37.868 -19.435 9.391   1.00 13.02 ?  77  VAL   B CA   1 
ATOM   5098 C C    . VAL   B 1 77  ? 36.670 -19.195 8.482   1.00 12.31 ?  77  VAL   B C    1 
ATOM   5099 O O    . VAL   B 1 77  ? 35.608 -18.740 8.932   1.00 12.61 ?  77  VAL   B O    1 
ATOM   5100 C CB   . VAL   B 1 77  ? 37.673 -20.669 10.285  1.00 14.29 ?  77  VAL   B CB   1 
ATOM   5101 C CG1  . VAL   B 1 77  ? 37.381 -21.899 9.426   1.00 14.98 ?  77  VAL   B CG1  1 
ATOM   5102 C CG2  . VAL   B 1 77  ? 38.908 -20.911 11.145  1.00 16.03 ?  77  VAL   B CG2  1 
ATOM   5103 H H    . VAL   B 1 77  ? 38.036 -18.341 11.036  1.00 15.67 ?  77  VAL   B H    1 
ATOM   5104 H HA   . VAL   B 1 77  ? 38.642 -19.584 8.828   1.00 15.60 ?  77  VAL   B HA   1 
ATOM   5105 H HB   . VAL   B 1 77  ? 36.912 -20.519 10.871  1.00 17.13 ?  77  VAL   B HB   1 
ATOM   5106 H HG11 . VAL   B 1 77  ? 37.434 -22.689 9.986   1.00 17.95 ?  77  VAL   B HG11 1 
ATOM   5107 H HG12 . VAL   B 1 77  ? 36.487 -21.822 9.051   1.00 17.95 ?  77  VAL   B HG12 1 
ATOM   5108 H HG13 . VAL   B 1 77  ? 38.036 -21.950 8.716   1.00 17.95 ?  77  VAL   B HG13 1 
ATOM   5109 H HG21 . VAL   B 1 77  ? 38.766 -21.711 11.672  1.00 19.22 ?  77  VAL   B HG21 1 
ATOM   5110 H HG22 . VAL   B 1 77  ? 39.674 -21.021 10.566  1.00 19.22 ?  77  VAL   B HG22 1 
ATOM   5111 H HG23 . VAL   B 1 77  ? 39.036 -20.147 11.729  1.00 19.22 ?  77  VAL   B HG23 1 
ATOM   5112 N N    . GLY   B 1 78  ? 36.846 -19.468 7.193   1.00 11.89 ?  78  GLY   B N    1 
ATOM   5113 C CA   . GLY   B 1 78  ? 35.872 -19.136 6.180   1.00 11.58 ?  78  GLY   B CA   1 
ATOM   5114 C C    . GLY   B 1 78  ? 36.124 -17.819 5.479   1.00 11.05 ?  78  GLY   B C    1 
ATOM   5115 O O    . GLY   B 1 78  ? 35.448 -17.534 4.485   1.00 11.55 ?  78  GLY   B O    1 
ATOM   5116 H H    . GLY   B 1 78  ? 37.540 -19.865 6.879   1.00 14.24 ?  78  GLY   B H    1 
ATOM   5117 H HA2  . GLY   B 1 78  ? 35.856 -19.832 5.512   1.00 13.87 ?  78  GLY   B HA2  1 
ATOM   5118 H HA3  . GLY   B 1 78  ? 34.992 -19.086 6.590   1.00 13.87 ?  78  GLY   B HA3  1 
ATOM   5119 N N    . GLY   B 1 79  ? 37.074 -17.014 5.968   1.00 11.44 ?  79  GLY   B N    1 
ATOM   5120 C CA   . GLY   B 1 79  ? 37.371 -15.719 5.398   1.00 10.93 ?  79  GLY   B CA   1 
ATOM   5121 C C    . GLY   B 1 79  ? 38.604 -15.733 4.507   1.00 10.83 ?  79  GLY   B C    1 
ATOM   5122 O O    . GLY   B 1 79  ? 39.214 -16.769 4.244   1.00 11.34 ?  79  GLY   B O    1 
ATOM   5123 H H    . GLY   B 1 79  ? 37.578 -17.211 6.634   1.00 13.71 ?  79  GLY   B H    1 
ATOM   5124 H HA2  . GLY   B 1 79  ? 36.616 -15.414 4.866   1.00 13.09 ?  79  GLY   B HA2  1 
ATOM   5125 H HA3  . GLY   B 1 79  ? 37.519 -15.077 6.110   1.00 13.09 ?  79  GLY   B HA3  1 
ATOM   5126 N N    . SER   B 1 80  ? 38.962 -14.534 4.036   1.00 10.83 ?  80  SER   B N    1 
ATOM   5127 C CA   . SER   B 1 80  ? 40.063 -14.389 3.095   1.00 10.88 ?  80  SER   B CA   1 
ATOM   5128 C C    . SER   B 1 80  ? 40.643 -12.982 3.163   1.00 10.93 ?  80  SER   B C    1 
ATOM   5129 O O    . SER   B 1 80  ? 40.026 -12.051 3.688   1.00 12.19 ?  80  SER   B O    1 
ATOM   5130 C CB   . SER   B 1 80  ? 39.611 -14.670 1.660   1.00 11.31 ?  80  SER   B CB   1 
ATOM   5131 O OG   . SER   B 1 80  ? 38.773 -13.642 1.169   1.00 12.55 ?  80  SER   B OG   1 
ATOM   5132 H H    . SER   B 1 80  ? 38.583 -13.790 4.248   1.00 12.97 ?  80  SER   B H    1 
ATOM   5133 H HA   . SER   B 1 80  ? 40.756 -15.018 3.332   1.00 13.03 ?  80  SER   B HA   1 
ATOM   5134 H HB2  . SER   B 1 80  ? 40.392 -14.733 1.087   1.00 13.55 ?  80  SER   B HB2  1 
ATOM   5135 H HB3  . SER   B 1 80  ? 39.122 -15.509 1.640   1.00 13.55 ?  80  SER   B HB3  1 
ATOM   5136 H HG   . SER   B 1 80  ? 38.085 -13.579 1.651   1.00 15.03 ?  80  SER   B HG   1 
ATOM   5137 N N    . CYS   B 1 81  ? 41.829 -12.831 2.576   1.00 10.88 ?  81  CYS   B N    1 
ATOM   5138 C CA   . CYS   B 1 81  ? 42.370 -11.516 2.271   1.00 10.87 ?  81  CYS   B CA   1 
ATOM   5139 C C    . CYS   B 1 81  ? 43.141 -11.595 0.965   1.00 10.11 ?  81  CYS   B C    1 
ATOM   5140 O O    . CYS   B 1 81  ? 43.664 -12.652 0.596   1.00 11.22 ?  81  CYS   B O    1 
ATOM   5141 C CB   . CYS   B 1 81  ? 43.263 -10.965 3.393   1.00 11.80 ?  81  CYS   B CB   1 
ATOM   5142 S SG   . CYS   B 1 81  ? 44.783 -11.900 3.649   1.00 11.97 ?  81  CYS   B SG   1 
ATOM   5143 H H    . CYS   B 1 81  ? 42.342 -13.481 2.339   1.00 13.03 ?  81  CYS   B H    1 
ATOM   5144 H HA   . CYS   B 1 81  ? 41.635 -10.892 2.146   1.00 13.02 ?  81  CYS   B HA   1 
ATOM   5145 H HB2  . CYS   B 1 81  ? 43.513 -10.052 3.178   1.00 14.13 ?  81  CYS   B HB2  1 
ATOM   5146 H HB3  . CYS   B 1 81  ? 42.759 -10.975 4.225   1.00 14.13 ?  81  CYS   B HB3  1 
ATOM   5147 H HG   . CYS   B 1 81  ? 45.405 -11.399 4.552   1.00 14.34 ?  81  CYS   B HG   1 
ATOM   5148 N N    . VAL   B 1 82  ? 43.239 -10.451 0.290   1.00 10.67 ?  82  VAL   B N    1 
ATOM   5149 C CA   . VAL   B 1 82  ? 44.005 -10.321 -0.946  1.00 11.09 ?  82  VAL   B CA   1 
ATOM   5150 C C    . VAL   B 1 82  ? 45.343 -9.677  -0.623  1.00 11.30 ?  82  VAL   B C    1 
ATOM   5151 O O    . VAL   B 1 82  ? 45.389 -8.564  -0.082  1.00 12.23 ?  82  VAL   B O    1 
ATOM   5152 C CB   . VAL   B 1 82  ? 43.257 -9.483  -1.993  1.00 12.54 ?  82  VAL   B CB   1 
ATOM   5153 C CG1  . VAL   B 1 82  ? 44.113 -9.325  -3.244  1.00 13.45 ?  82  VAL   B CG1  1 
ATOM   5154 C CG2  . VAL   B 1 82  ? 41.912 -10.098 -2.329  1.00 13.34 ?  82  VAL   B CG2  1 
ATOM   5155 H H    . VAL   B 1 82  ? 42.855 -9.714  0.531   1.00 12.78 ?  82  VAL   B H    1 
ATOM   5156 H HA   . VAL   B 1 82  ? 44.168 -11.198 -1.319  1.00 13.29 ?  82  VAL   B HA   1 
ATOM   5157 H HB   . VAL   B 1 82  ? 43.095 -8.595  -1.634  1.00 15.03 ?  82  VAL   B HB   1 
ATOM   5158 H HG11 . VAL   B 1 82  ? 43.554 -9.022  -3.975  1.00 16.12 ?  82  VAL   B HG11 1 
ATOM   5159 H HG12 . VAL   B 1 82  ? 44.810 -8.669  -3.071  1.00 16.12 ?  82  VAL   B HG12 1 
ATOM   5160 H HG13 . VAL   B 1 82  ? 44.511 -10.181 -3.463  1.00 16.12 ?  82  VAL   B HG13 1 
ATOM   5161 H HG21 . VAL   B 1 82  ? 41.482 -9.564  -3.016  1.00 15.98 ?  82  VAL   B HG21 1 
ATOM   5162 H HG22 . VAL   B 1 82  ? 42.053 -11.002 -2.653  1.00 15.98 ?  82  VAL   B HG22 1 
ATOM   5163 H HG23 . VAL   B 1 82  ? 41.365 -10.114 -1.530  1.00 15.98 ?  82  VAL   B HG23 1 
ATOM   5164 N N    . LEU   B 1 83  ? 46.430 -10.354 -0.991  1.00 11.04 ?  83  LEU   B N    1 
ATOM   5165 C CA   . LEU   B 1 83  ? 47.781 -9.832  -0.863  1.00 10.98 ?  83  LEU   B CA   1 
ATOM   5166 C C    . LEU   B 1 83  ? 48.485 -9.967  -2.211  1.00 10.87 ?  83  LEU   B C    1 
ATOM   5167 O O    . LEU   B 1 83  ? 47.890 -10.394 -3.207  1.00 10.89 ?  83  LEU   B O    1 
ATOM   5168 C CB   . LEU   B 1 83  ? 48.527 -10.511 0.292   1.00 11.60 ?  83  LEU   B CB   1 
ATOM   5169 C CG   . LEU   B 1 83  ? 48.007 -10.159 1.691   1.00 12.95 ?  83  LEU   B CG   1 
ATOM   5170 C CD1  . LEU   B 1 83  ? 48.644 -11.023 2.768   1.00 13.13 ?  83  LEU   B CD1  1 
ATOM   5171 C CD2  . LEU   B 1 83  ? 48.208 -8.672  2.012   1.00 13.96 ?  83  LEU   B CD2  1 
ATOM   5172 H H    . LEU   B 1 83  ? 46.397 -11.146 -1.334  1.00 13.22 ?  83  LEU   B H    1 
ATOM   5173 H HA   . LEU   B 1 83  ? 47.720 -8.889  -0.660  1.00 13.15 ?  83  LEU   B HA   1 
ATOM   5174 H HB2  . LEU   B 1 83  ? 48.458 -11.470 0.188   1.00 13.89 ?  83  LEU   B HB2  1 
ATOM   5175 H HB3  . LEU   B 1 83  ? 49.459 -10.243 0.251   1.00 13.89 ?  83  LEU   B HB3  1 
ATOM   5176 H HG   . LEU   B 1 83  ? 47.057 -10.329 1.712   1.00 15.52 ?  83  LEU   B HG   1 
ATOM   5177 H HD11 . LEU   B 1 83  ? 48.281 -10.770 3.632   1.00 15.72 ?  83  LEU   B HD11 1 
ATOM   5178 H HD12 . LEU   B 1 83  ? 48.440 -11.954 2.585   1.00 15.72 ?  83  LEU   B HD12 1 
ATOM   5179 H HD13 . LEU   B 1 83  ? 49.604 -10.887 2.760   1.00 15.72 ?  83  LEU   B HD13 1 
ATOM   5180 H HD21 . LEU   B 1 83  ? 48.012 -8.521  2.949   1.00 16.73 ?  83  LEU   B HD21 1 
ATOM   5181 H HD22 . LEU   B 1 83  ? 49.128 -8.428  1.822   1.00 16.73 ?  83  LEU   B HD22 1 
ATOM   5182 H HD23 . LEU   B 1 83  ? 47.607 -8.146  1.460   1.00 16.73 ?  83  LEU   B HD23 1 
ATOM   5183 N N    . SER   B 1 84  ? 49.759 -9.586  -2.258  1.00 11.99 ?  84  SER   B N    1 
ATOM   5184 C CA   . SER   B 1 84  ? 50.504 -9.699  -3.503  1.00 12.15 ?  84  SER   B CA   1 
ATOM   5185 C C    . SER   B 1 84  ? 50.653 -11.159 -3.923  1.00 11.66 ?  84  SER   B C    1 
ATOM   5186 O O    . SER   B 1 84  ? 50.767 -12.066 -3.097  1.00 11.35 ?  84  SER   B O    1 
ATOM   5187 C CB   . SER   B 1 84  ? 51.896 -9.093  -3.345  1.00 14.25 ?  84  SER   B CB   1 
ATOM   5188 O OG   . SER   B 1 84  ? 52.646 -9.303  -4.524  1.00 16.21 ?  84  SER   B OG   1 
ATOM   5189 H H    . SER   B 1 84  ? 50.200 -9.260  -1.596  1.00 14.36 ?  84  SER   B H    1 
ATOM   5190 H HA   . SER   B 1 84  ? 50.036 -9.225  -4.207  1.00 14.55 ?  84  SER   B HA   1 
ATOM   5191 H HB2  . SER   B 1 84  ? 51.811 -8.136  -3.183  1.00 17.08 ?  84  SER   B HB2  1 
ATOM   5192 H HB3  . SER   B 1 84  ? 52.351 -9.516  -2.604  1.00 17.08 ?  84  SER   B HB3  1 
ATOM   5193 H HG   . SER   B 1 84  ? 53.409 -8.959  -4.449  1.00 19.42 ?  84  SER   B HG   1 
ATOM   5194 N N    . GLY   B 1 85  ? 50.715 -11.376 -5.229  1.00 12.70 ?  85  GLY   B N    1 
ATOM   5195 C CA   . GLY   B 1 85  ? 51.071 -12.669 -5.763  1.00 13.35 ?  85  GLY   B CA   1 
ATOM   5196 C C    . GLY   B 1 85  ? 52.536 -12.856 -6.075  1.00 12.33 ?  85  GLY   B C    1 
ATOM   5197 O O    . GLY   B 1 85  ? 52.905 -13.932 -6.548  1.00 12.78 ?  85  GLY   B O    1 
ATOM   5198 H H    . GLY   B 1 85  ? 50.559 -10.787 -5.823  1.00 15.22 ?  85  GLY   B H    1 
ATOM   5199 H HA2  . GLY   B 1 85  ? 50.814 -13.359 -5.126  1.00 16.00 ?  85  GLY   B HA2  1 
ATOM   5200 H HA3  . GLY   B 1 85  ? 50.578 -12.820 -6.578  1.00 16.00 ?  85  GLY   B HA3  1 
ATOM   5201 N N    . HIS   B 1 86  ? 53.389 -11.857 -5.850  1.00 12.15 ?  86  HIS   B N    1 
ATOM   5202 C CA   . HIS   B 1 86  ? 54.848 -12.032 -5.931  1.00 12.34 ?  86  HIS   B CA   1 
ATOM   5203 C C    . HIS   B 1 86  ? 55.218 -12.540 -7.323  1.00 12.35 ?  86  HIS   B C    1 
ATOM   5204 O O    . HIS   B 1 86  ? 54.831 -11.918 -8.325  1.00 13.08 ?  86  HIS   B O    1 
ATOM   5205 C CB   . HIS   B 1 86  ? 55.332 -12.883 -4.755  1.00 12.56 ?  86  HIS   B CB   1 
ATOM   5206 C CG   . HIS   B 1 86  ? 55.013 -12.281 -3.426  1.00 13.04 ?  86  HIS   B CG   1 
ATOM   5207 N ND1  . HIS   B 1 86  ? 55.819 -11.339 -2.822  1.00 14.49 ?  86  HIS   B ND1  1 
ATOM   5208 C CD2  . HIS   B 1 86  ? 53.943 -12.446 -2.611  1.00 13.46 ?  86  HIS   B CD2  1 
ATOM   5209 C CE1  . HIS   B 1 86  ? 55.264 -10.964 -1.683  1.00 14.24 ?  86  HIS   B CE1  1 
ATOM   5210 N NE2  . HIS   B 1 86  ? 54.126 -11.618 -1.532  1.00 13.75 ?  86  HIS   B NE2  1 
ATOM   5211 H H    . HIS   B 1 86  ? 53.151 -11.058 -5.655  1.00 14.56 ?  86  HIS   B H    1 
ATOM   5212 H HA   . HIS   B 1 86  ? 55.262 -11.161 -5.828  1.00 14.78 ?  86  HIS   B HA   1 
ATOM   5213 H HB2  . HIS   B 1 86  ? 54.912 -13.758 -4.801  1.00 15.05 ?  86  HIS   B HB2  1 
ATOM   5214 H HB3  . HIS   B 1 86  ? 56.299 -12.983 -4.809  1.00 15.05 ?  86  HIS   B HB3  1 
ATOM   5215 H HD2  . HIS   B 1 86  ? 53.218 -13.020 -2.756  1.00 16.12 ?  86  HIS   B HD2  1 
ATOM   5216 H HE1  . HIS   B 1 86  ? 55.616 -10.353 -1.082  1.00 17.06 ?  86  HIS   B HE1  1 
ATOM   5217 H HE2  . HIS   B 1 86  ? 53.588 -11.552 -0.862  1.00 16.48 ?  86  HIS   B HE2  1 
ATOM   5218 N N    . ASN   B 1 87  ? 55.984 -13.625 -7.437  1.00 12.67 ?  87  ASN   B N    1 
ATOM   5219 C CA   . ASN   B 1 87  ? 56.375 -14.195 -8.718  1.00 13.57 ?  87  ASN   B CA   1 
ATOM   5220 C C    . ASN   B 1 87  ? 55.392 -15.240 -9.221  1.00 13.17 ?  87  ASN   B C    1 
ATOM   5221 O O    . ASN   B 1 87  ? 55.709 -15.953 -10.178 1.00 14.73 ?  87  ASN   B O    1 
ATOM   5222 C CB   . ASN   B 1 87  ? 57.774 -14.818 -8.615  1.00 15.26 ?  87  ASN   B CB   1 
ATOM   5223 C CG   . ASN   B 1 87  ? 57.846 -15.938 -7.579  1.00 15.89 ?  87  ASN   B CG   1 
ATOM   5224 O OD1  . ASN   B 1 87  ? 57.204 -15.873 -6.527  1.00 15.14 ?  87  ASN   B OD1  1 
ATOM   5225 N ND2  . ASN   B 1 87  ? 58.611 -16.986 -7.890  1.00 18.02 ?  87  ASN   B ND2  1 
ATOM   5226 H H    . ASN   B 1 87  ? 56.302 -14.057 -6.763  1.00 15.18 ?  87  ASN   B H    1 
ATOM   5227 H HA   . ASN   B 1 87  ? 56.414 -13.489 -9.377  1.00 16.26 ?  87  ASN   B HA   1 
ATOM   5228 H HB2  . ASN   B 1 87  ? 58.018 -15.190 -9.481  1.00 18.29 ?  87  ASN   B HB2  1 
ATOM   5229 H HB3  . ASN   B 1 87  ? 58.407 -14.131 -8.361  1.00 18.29 ?  87  ASN   B HB3  1 
ATOM   5230 H HD21 . ASN   B 1 87  ? 58.685 -17.639 -7.339  1.00 21.59 ?  87  ASN   B HD21 1 
ATOM   5231 H HD22 . ASN   B 1 87  ? 59.039 -17.000 -8.638  1.00 21.59 ?  87  ASN   B HD22 1 
ATOM   5232 N N    . LEU   B 1 88  ? 54.213 -15.340 -8.605  1.00 12.33 ?  88  LEU   B N    1 
ATOM   5233 C CA   . LEU   B 1 88  ? 53.234 -16.370 -8.934  1.00 12.44 ?  88  LEU   B CA   1 
ATOM   5234 C C    . LEU   B 1 88  ? 51.999 -15.851 -9.649  1.00 12.22 ?  88  LEU   B C    1 
ATOM   5235 O O    . LEU   B 1 88  ? 51.395 -16.595 -10.432 1.00 14.19 ?  88  LEU   B O    1 
ATOM   5236 C CB   . LEU   B 1 88  ? 52.768 -17.069 -7.653  1.00 13.31 ?  88  LEU   B CB   1 
ATOM   5237 C CG   . LEU   B 1 88  ? 53.887 -17.706 -6.840  1.00 15.65 ?  88  LEU   B CG   1 
ATOM   5238 C CD1  . LEU   B 1 88  ? 53.381 -18.043 -5.446  1.00 17.03 ?  88  LEU   B CD1  1 
ATOM   5239 C CD2  . LEU   B 1 88  ? 54.407 -18.940 -7.548  1.00 18.21 ?  88  LEU   B CD2  1 
ATOM   5240 H H    . LEU   B 1 88  ? 53.957 -14.819 -7.964  1.00 14.77 ?  88  LEU   B H    1 
ATOM   5241 H HA   . LEU   B 1 88  ? 53.649 -17.032 -9.498  1.00 14.90 ?  88  LEU   B HA   1 
ATOM   5242 H HB2  . LEU   B 1 88  ? 52.321 -16.425 -7.083  1.00 15.95 ?  88  LEU   B HB2  1 
ATOM   5243 H HB3  . LEU   B 1 88  ? 52.145 -17.777 -7.894  1.00 15.95 ?  88  LEU   B HB3  1 
ATOM   5244 H HG   . LEU   B 1 88  ? 54.618 -17.074 -6.750  1.00 18.76 ?  88  LEU   B HG   1 
ATOM   5245 H HD11 . LEU   B 1 88  ? 53.990 -18.675 -5.033  1.00 20.41 ?  88  LEU   B HD11 1 
ATOM   5246 H HD12 . LEU   B 1 88  ? 53.340 -17.230 -4.919  1.00 20.41 ?  88  LEU   B HD12 1 
ATOM   5247 H HD13 . LEU   B 1 88  ? 52.497 -18.434 -5.521  1.00 20.41 ?  88  LEU   B HD13 1 
ATOM   5248 H HD21 . LEU   B 1 88  ? 55.087 -19.358 -6.993  1.00 21.83 ?  88  LEU   B HD21 1 
ATOM   5249 H HD22 . LEU   B 1 88  ? 53.673 -19.556 -7.690  1.00 21.83 ?  88  LEU   B HD22 1 
ATOM   5250 H HD23 . LEU   B 1 88  ? 54.792 -18.678 -8.399  1.00 21.83 ?  88  LEU   B HD23 1 
ATOM   5251 N N    . ALA   B 1 89  ? 51.591 -14.616 -9.374  1.00 11.49 ?  89  ALA   B N    1 
ATOM   5252 C CA   . ALA   B 1 89  ? 50.302 -14.120 -9.834  1.00 11.03 ?  89  ALA   B CA   1 
ATOM   5253 C C    . ALA   B 1 89  ? 50.268 -12.630 -9.559  1.00 11.21 ?  89  ALA   B C    1 
ATOM   5254 O O    . ALA   B 1 89  ? 51.100 -12.108 -8.817  1.00 12.28 ?  89  ALA   B O    1 
ATOM   5255 C CB   . ALA   B 1 89  ? 49.152 -14.798 -9.087  1.00 11.18 ?  89  ALA   B CB   1 
ATOM   5256 H H    . ALA   B 1 89  ? 52.030 -14.042 -8.899  1.00 13.77 ?  89  ALA   B H    1 
ATOM   5257 H HA   . ALA   B 1 89  ? 50.200 -14.272 -10.785 1.00 13.21 ?  89  ALA   B HA   1 
ATOM   5258 H HB1  . ALA   B 1 89  ? 48.306 -14.464 -9.435  1.00 13.39 ?  89  ALA   B HB1  1 
ATOM   5259 H HB2  . ALA   B 1 89  ? 49.207 -15.756 -9.227  1.00 13.39 ?  89  ALA   B HB2  1 
ATOM   5260 H HB3  . ALA   B 1 89  ? 49.221 -14.595 -8.143  1.00 13.39 ?  89  ALA   B HB3  1 
ATOM   5261 N N    . LYS   B 1 90  ? 49.280 -11.944 -10.130 1.00 12.25 ?  90  LYS   B N    1 
ATOM   5262 C CA   . LYS   B 1 90  ? 49.083 -10.556 -9.733  1.00 12.45 ?  90  LYS   B CA   1 
ATOM   5263 C C    . LYS   B 1 90  ? 48.753 -10.477 -8.247  1.00 12.43 ?  90  LYS   B C    1 
ATOM   5264 O O    . LYS   B 1 90  ? 49.379 -9.715  -7.495  1.00 13.96 ?  90  LYS   B O    1 
ATOM   5265 C CB   . LYS   B 1 90  ? 48.007 -9.902  -10.600 1.00 14.23 ?  90  LYS   B CB   1 
ATOM   5266 C CG   . LYS   B 1 90  ? 47.688 -8.463  -10.225 1.00 15.12 ?  90  LYS   B CG   1 
ATOM   5267 C CD   . LYS   B 1 90  ? 48.874 -7.537  -10.335 1.00 17.65 ?  90  LYS   B CD   1 
ATOM   5268 C CE   . LYS   B 1 90  ? 48.415 -6.115  -10.102 1.00 19.67 ?  90  LYS   B CE   1 
ATOM   5269 N NZ   . LYS   B 1 90  ? 49.557 -5.174  -10.039 1.00 19.95 ?  90  LYS   B NZ   1 
ATOM   5270 H H    . LYS   B 1 90  ? 48.731 -12.247 -10.721 1.00 14.67 ?  90  LYS   B H    1 
ATOM   5271 H HA   . LYS   B 1 90  ? 49.906 -10.074 -9.878  1.00 14.91 ?  90  LYS   B HA   1 
ATOM   5272 H HB2  . LYS   B 1 90  ? 48.310 -9.901  -11.525 1.00 17.05 ?  90  LYS   B HB2  1 
ATOM   5273 H HB3  . LYS   B 1 90  ? 47.187 -10.415 -10.530 1.00 17.05 ?  90  LYS   B HB3  1 
ATOM   5274 H HG2  . LYS   B 1 90  ? 46.994 -8.133  -10.817 1.00 18.12 ?  90  LYS   B HG2  1 
ATOM   5275 H HG3  . LYS   B 1 90  ? 47.369 -8.441  -9.306  1.00 18.12 ?  90  LYS   B HG3  1 
ATOM   5276 H HD2  . LYS   B 1 90  ? 49.530 -7.767  -9.659  1.00 21.16 ?  90  LYS   B HD2  1 
ATOM   5277 H HD3  . LYS   B 1 90  ? 49.255 -7.603  -11.223 1.00 21.16 ?  90  LYS   B HD3  1 
ATOM   5278 H HE2  . LYS   B 1 90  ? 47.838 -5.838  -10.834 1.00 23.57 ?  90  LYS   B HE2  1 
ATOM   5279 H HE3  . LYS   B 1 90  ? 47.936 -6.061  -9.261  1.00 23.57 ?  90  LYS   B HE3  1 
ATOM   5280 H HZ1  . LYS   B 1 90  ? 49.267 -4.342  -9.905  1.00 23.92 ?  90  LYS   B HZ1  1 
ATOM   5281 H HZ2  . LYS   B 1 90  ? 50.105 -5.398  -9.374  1.00 23.92 ?  90  LYS   B HZ2  1 
ATOM   5282 H HZ3  . LYS   B 1 90  ? 50.016 -5.195  -10.806 1.00 23.92 ?  90  LYS   B HZ3  1 
ATOM   5283 N N    . HIS   B 1 91  ? 47.798 -11.301 -7.802  1.00 10.77 ?  91  HIS   B N    1 
ATOM   5284 C CA   . HIS   B 1 91  ? 47.334 -11.326 -6.428  1.00 10.64 ?  91  HIS   B CA   1 
ATOM   5285 C C    . HIS   B 1 91  ? 47.341 -12.754 -5.906  1.00 10.05 ?  91  HIS   B C    1 
ATOM   5286 O O    . HIS   B 1 91  ? 47.110 -13.711 -6.656  1.00 10.66 ?  91  HIS   B O    1 
ATOM   5287 C CB   . HIS   B 1 91  ? 45.876 -10.857 -6.319  1.00 12.27 ?  91  HIS   B CB   1 
ATOM   5288 C CG   . HIS   B 1 91  ? 45.649 -9.461  -6.786  1.00 15.80 ?  91  HIS   B CG   1 
ATOM   5289 N ND1  . HIS   B 1 91  ? 46.217 -8.367  -6.171  1.00 18.43 ?  91  HIS   B ND1  1 
ATOM   5290 C CD2  . HIS   B 1 91  ? 44.885 -8.975  -7.789  1.00 18.26 ?  91  HIS   B CD2  1 
ATOM   5291 C CE1  . HIS   B 1 91  ? 45.829 -7.264  -6.787  1.00 19.32 ?  91  HIS   B CE1  1 
ATOM   5292 N NE2  . HIS   B 1 91  ? 45.015 -7.607  -7.771  1.00 19.53 ?  91  HIS   B NE2  1 
ATOM   5293 H H    . HIS   B 1 91  ? 47.391 -11.870 -8.302  1.00 12.90 ?  91  HIS   B H    1 
ATOM   5294 H HA   . HIS   B 1 91  ? 47.895 -10.761 -5.866  1.00 12.74 ?  91  HIS   B HA   1 
ATOM   5295 H HB2  . HIS   B 1 91  ? 45.316 -11.440 -6.858  1.00 14.69 ?  91  HIS   B HB2  1 
ATOM   5296 H HB3  . HIS   B 1 91  ? 45.595 -10.906 -5.389  1.00 14.69 ?  91  HIS   B HB3  1 
ATOM   5297 H HD1  . HIS   B 1 91  ? 46.743 -8.396  -5.490  1.00 22.09 ?  91  HIS   B HD1  1 
ATOM   5298 H HD2  . HIS   B 1 91  ? 44.374 -9.463  -8.389  1.00 21.89 ?  91  HIS   B HD2  1 
ATOM   5299 H HE1  . HIS   B 1 91  ? 46.082 -6.395  -6.561  1.00 23.16 ?  91  HIS   B HE1  1 
ATOM   5300 N N    . CYS   B 1 92  ? 47.544 -12.887 -4.603  1.00 9.95  ?  92  CYS   B N    1 
ATOM   5301 C CA   . CYS   B 1 92  ? 47.253 -14.126 -3.892  1.00 9.83  ?  92  CYS   B CA   1 
ATOM   5302 C C    . CYS   B 1 92  ? 46.035 -13.898 -3.003  1.00 9.32  ?  92  CYS   B C    1 
ATOM   5303 O O    . CYS   B 1 92  ? 46.029 -12.998 -2.151  1.00 10.35 ?  92  CYS   B O    1 
ATOM   5304 C CB   . CYS   B 1 92  ? 48.438 -14.586 -3.051  1.00 10.35 ?  92  CYS   B CB   1 
ATOM   5305 S SG   . CYS   B 1 92  ? 48.084 -16.121 -2.145  1.00 10.62 ?  92  CYS   B SG   1 
ATOM   5306 H H    . CYS   B 1 92  ? 47.867 -12.264 -4.097  1.00 11.91 ?  92  CYS   B H    1 
ATOM   5307 H HA   . CYS   B 1 92  ? 47.051 -14.820 -4.540  1.00 11.77 ?  92  CYS   B HA   1 
ATOM   5308 H HB2  . CYS   B 1 92  ? 49.198 -14.743 -3.628  1.00 12.39 ?  92  CYS   B HB2  1 
ATOM   5309 H HB3  . CYS   B 1 92  ? 48.646 -13.900 -2.400  1.00 12.39 ?  92  CYS   B HB3  1 
ATOM   5310 H HG   . CYS   B 1 92  ? 49.071 -16.431 -1.531  1.00 12.72 ?  92  CYS   B HG   1 
ATOM   5311 N N    . LEU   B 1 93  ? 45.001 -14.709 -3.220  1.00 9.19  ?  93  LEU   B N    1 
ATOM   5312 C CA   . LEU   B 1 93  ? 43.826 -14.728 -2.360  1.00 9.44  ?  93  LEU   B CA   1 
ATOM   5313 C C    . LEU   B 1 93  ? 44.057 -15.799 -1.301  1.00 8.95  ?  93  LEU   B C    1 
ATOM   5314 O O    . LEU   B 1 93  ? 44.007 -17.001 -1.595  1.00 9.56  ?  93  LEU   B O    1 
ATOM   5315 C CB   . LEU   B 1 93  ? 42.561 -15.017 -3.169  1.00 9.76  ?  93  LEU   B CB   1 
ATOM   5316 C CG   . LEU   B 1 93  ? 41.263 -15.050 -2.366  1.00 10.37 ?  93  LEU   B CG   1 
ATOM   5317 C CD1  . LEU   B 1 93  ? 40.899 -13.666 -1.875  1.00 11.09 ?  93  LEU   B CD1  1 
ATOM   5318 C CD2  . LEU   B 1 93  ? 40.144 -15.630 -3.208  1.00 10.87 ?  93  LEU   B CD2  1 
ATOM   5319 H H    . LEU   B 1 93  ? 44.963 -15.286 -3.872  1.00 11.01 ?  93  LEU   B H    1 
ATOM   5320 H HA   . LEU   B 1 93  ? 43.736 -13.867 -1.928  1.00 11.31 ?  93  LEU   B HA   1 
ATOM   5321 H HB2  . LEU   B 1 93  ? 42.469 -14.318 -3.842  1.00 11.68 ?  93  LEU   B HB2  1 
ATOM   5322 H HB3  . LEU   B 1 93  ? 42.661 -15.871 -3.602  1.00 11.68 ?  93  LEU   B HB3  1 
ATOM   5323 H HG   . LEU   B 1 93  ? 41.379 -15.617 -1.592  1.00 12.42 ?  93  LEU   B HG   1 
ATOM   5324 H HD11 . LEU   B 1 93  ? 40.048 -13.702 -1.416  1.00 13.29 ?  93  LEU   B HD11 1 
ATOM   5325 H HD12 . LEU   B 1 93  ? 41.590 -13.350 -1.271  1.00 13.29 ?  93  LEU   B HD12 1 
ATOM   5326 H HD13 . LEU   B 1 93  ? 40.835 -13.065 -2.640  1.00 13.29 ?  93  LEU   B HD13 1 
ATOM   5327 H HD21 . LEU   B 1 93  ? 39.324 -15.638 -2.687  1.00 13.01 ?  93  LEU   B HD21 1 
ATOM   5328 H HD22 . LEU   B 1 93  ? 40.022 -15.079 -4.000  1.00 13.01 ?  93  LEU   B HD22 1 
ATOM   5329 H HD23 . LEU   B 1 93  ? 40.378 -16.533 -3.469  1.00 13.01 ?  93  LEU   B HD23 1 
ATOM   5330 N N    . HIS   B 1 94  ? 44.341 -15.367 -0.077  1.00 8.91  ?  94  HIS   B N    1 
ATOM   5331 C CA   . HIS   B 1 94  ? 44.551 -16.281 1.040   1.00 9.27  ?  94  HIS   B CA   1 
ATOM   5332 C C    . HIS   B 1 94  ? 43.190 -16.635 1.615   1.00 9.54  ?  94  HIS   B C    1 
ATOM   5333 O O    . HIS   B 1 94  ? 42.515 -15.757 2.157   1.00 11.00 ?  94  HIS   B O    1 
ATOM   5334 C CB   . HIS   B 1 94  ? 45.421 -15.609 2.100   1.00 9.68  ?  94  HIS   B CB   1 
ATOM   5335 C CG   . HIS   B 1 94  ? 46.804 -15.306 1.631   1.00 9.64  ?  94  HIS   B CG   1 
ATOM   5336 N ND1  . HIS   B 1 94  ? 47.838 -16.215 1.712   1.00 9.99  ?  94  HIS   B ND1  1 
ATOM   5337 C CD2  . HIS   B 1 94  ? 47.304 -14.196 1.040   1.00 10.32 ?  94  HIS   B CD2  1 
ATOM   5338 C CE1  . HIS   B 1 94  ? 48.924 -15.655 1.203   1.00 10.24 ?  94  HIS   B CE1  1 
ATOM   5339 N NE2  . HIS   B 1 94  ? 48.629 -14.431 0.793   1.00 10.38 ?  94  HIS   B NE2  1 
ATOM   5340 H H    . HIS   B 1 94  ? 44.415 -14.531 0.136   1.00 10.66 ?  94  HIS   B H    1 
ATOM   5341 H HA   . HIS   B 1 94  ? 44.990 -17.089 0.727   1.00 11.10 ?  94  HIS   B HA   1 
ATOM   5342 H HB2  . HIS   B 1 94  ? 45.007 -14.776 2.362   1.00 11.59 ?  94  HIS   B HB2  1 
ATOM   5343 H HB3  . HIS   B 1 94  ? 45.492 -16.202 2.863   1.00 11.59 ?  94  HIS   B HB3  1 
ATOM   5344 H HD2  . HIS   B 1 94  ? 46.844 -13.412 0.849   1.00 12.36 ?  94  HIS   B HD2  1 
ATOM   5345 H HE1  . HIS   B 1 94  ? 49.764 -16.063 1.142   1.00 12.27 ?  94  HIS   B HE1  1 
ATOM   5346 H HE2  . HIS   B 1 94  ? 49.183 -13.883 0.425   1.00 12.43 ?  94  HIS   B HE2  1 
ATOM   5347 N N    . VAL   B 1 95  ? 42.766 -17.893 1.473   1.00 9.33  ?  95  VAL   B N    1 
ATOM   5348 C CA   . VAL   B 1 95  ? 41.440 -18.338 1.907   1.00 9.57  ?  95  VAL   B CA   1 
ATOM   5349 C C    . VAL   B 1 95  ? 41.607 -19.381 2.998   1.00 9.73  ?  95  VAL   B C    1 
ATOM   5350 O O    . VAL   B 1 95  ? 42.375 -20.335 2.835   1.00 10.16 ?  95  VAL   B O    1 
ATOM   5351 C CB   . VAL   B 1 95  ? 40.619 -18.938 0.748   1.00 9.99  ?  95  VAL   B CB   1 
ATOM   5352 C CG1  . VAL   B 1 95  ? 39.242 -19.392 1.232   1.00 11.15 ?  95  VAL   B CG1  1 
ATOM   5353 C CG2  . VAL   B 1 95  ? 40.504 -17.955 -0.397  1.00 10.14 ?  95  VAL   B CG2  1 
ATOM   5354 H H    . VAL   B 1 95  ? 43.231 -18.518 1.109   1.00 11.17 ?  95  VAL   B H    1 
ATOM   5355 H HA   . VAL   B 1 95  ? 40.946 -17.586 2.273   1.00 11.46 ?  95  VAL   B HA   1 
ATOM   5356 H HB   . VAL   B 1 95  ? 41.079 -19.718 0.415   1.00 11.96 ?  95  VAL   B HB   1 
ATOM   5357 H HG11 . VAL   B 1 95  ? 38.681 -19.586 0.462   1.00 13.35 ?  95  VAL   B HG11 1 
ATOM   5358 H HG12 . VAL   B 1 95  ? 39.343 -20.197 1.770   1.00 13.35 ?  95  VAL   B HG12 1 
ATOM   5359 H HG13 . VAL   B 1 95  ? 38.839 -18.689 1.763   1.00 13.35 ?  95  VAL   B HG13 1 
ATOM   5360 H HG21 . VAL   B 1 95  ? 39.927 -18.335 -1.079  1.00 12.15 ?  95  VAL   B HG21 1 
ATOM   5361 H HG22 . VAL   B 1 95  ? 40.125 -17.128 -0.066  1.00 12.15 ?  95  VAL   B HG22 1 
ATOM   5362 H HG23 . VAL   B 1 95  ? 41.387 -17.798 -0.761  1.00 12.15 ?  95  VAL   B HG23 1 
ATOM   5363 N N    . VAL   B 1 96  ? 40.880 -19.213 4.094   1.00 9.98  ?  96  VAL   B N    1 
ATOM   5364 C CA   . VAL   B 1 96  ? 40.959 -20.129 5.231   1.00 10.27 ?  96  VAL   B CA   1 
ATOM   5365 C C    . VAL   B 1 96  ? 39.770 -21.089 5.179   1.00 10.44 ?  96  VAL   B C    1 
ATOM   5366 O O    . VAL   B 1 96  ? 38.647 -20.738 5.557   1.00 11.17 ?  96  VAL   B O    1 
ATOM   5367 C CB   . VAL   B 1 96  ? 41.011 -19.381 6.566   1.00 11.10 ?  96  VAL   B CB   1 
ATOM   5368 C CG1  . VAL   B 1 96  ? 41.180 -20.358 7.720   1.00 11.67 ?  96  VAL   B CG1  1 
ATOM   5369 C CG2  . VAL   B 1 96  ? 42.131 -18.356 6.566   1.00 12.09 ?  96  VAL   B CG2  1 
ATOM   5370 H H    . VAL   B 1 96  ? 40.318 -18.573 4.210   1.00 11.95 ?  96  VAL   B H    1 
ATOM   5371 H HA   . VAL   B 1 96  ? 41.775 -20.656 5.158   1.00 12.30 ?  96  VAL   B HA   1 
ATOM   5372 H HB   . VAL   B 1 96  ? 40.174 -18.909 6.694   1.00 13.29 ?  96  VAL   B HB   1 
ATOM   5373 H HG11 . VAL   B 1 96  ? 41.349 -19.851 8.535   1.00 13.98 ?  96  VAL   B HG11 1 
ATOM   5374 H HG12 . VAL   B 1 96  ? 40.371 -20.878 7.820   1.00 13.98 ?  96  VAL   B HG12 1 
ATOM   5375 H HG13 . VAL   B 1 96  ? 41.934 -20.937 7.536   1.00 13.98 ?  96  VAL   B HG13 1 
ATOM   5376 H HG21 . VAL   B 1 96  ? 42.192 -17.945 7.446   1.00 14.49 ?  96  VAL   B HG21 1 
ATOM   5377 H HG22 . VAL   B 1 96  ? 42.970 -18.793 6.351   1.00 14.49 ?  96  VAL   B HG22 1 
ATOM   5378 H HG23 . VAL   B 1 96  ? 41.941 -17.670 5.902   1.00 14.49 ?  96  VAL   B HG23 1 
ATOM   5379 N N    . GLY   B 1 97  ? 40.009 -22.324 4.746   1.00 10.78 ?  97  GLY   B N    1 
ATOM   5380 C CA   . GLY   B 1 97  ? 39.034 -23.377 4.910   1.00 10.91 ?  97  GLY   B CA   1 
ATOM   5381 C C    . GLY   B 1 97  ? 39.154 -23.990 6.286   1.00 11.69 ?  97  GLY   B C    1 
ATOM   5382 O O    . GLY   B 1 97  ? 40.195 -23.871 6.946   1.00 12.35 ?  97  GLY   B O    1 
ATOM   5383 H H    . GLY   B 1 97  ? 40.742 -22.569 4.350   1.00 12.91 ?  97  GLY   B H    1 
ATOM   5384 H HA2  . GLY   B 1 97  ? 38.146 -23.005 4.796   1.00 13.07 ?  97  GLY   B HA2  1 
ATOM   5385 H HA3  . GLY   B 1 97  ? 39.178 -24.062 4.240   1.00 13.07 ?  97  GLY   B HA3  1 
ATOM   5386 N N    . PRO   B 1 98  ? 38.102 -24.674 6.744   1.00 12.19 ?  98  PRO   B N    1 
ATOM   5387 C CA   . PRO   B 1 98  ? 38.183 -25.364 8.036   1.00 13.21 ?  98  PRO   B CA   1 
ATOM   5388 C C    . PRO   B 1 98  ? 39.208 -26.482 8.002   1.00 12.93 ?  98  PRO   B C    1 
ATOM   5389 O O    . PRO   B 1 98  ? 39.320 -27.217 7.022   1.00 13.02 ?  98  PRO   B O    1 
ATOM   5390 C CB   . PRO   B 1 98  ? 36.770 -25.921 8.225   1.00 13.32 ?  98  PRO   B CB   1 
ATOM   5391 C CG   . PRO   B 1 98  ? 36.229 -26.057 6.849   1.00 13.01 ?  98  PRO   B CG   1 
ATOM   5392 C CD   . PRO   B 1 98  ? 36.790 -24.877 6.101   1.00 11.97 ?  98  PRO   B CD   1 
ATOM   5393 H HA   . PRO   B 1 98  ? 38.395 -24.747 8.747   1.00 15.83 ?  98  PRO   B HA   1 
ATOM   5394 H HB2  . PRO   B 1 98  ? 36.814 -26.791 8.663   1.00 15.96 ?  98  PRO   B HB2  1 
ATOM   5395 H HB3  . PRO   B 1 98  ? 36.239 -25.303 8.743   1.00 15.96 ?  98  PRO   B HB3  1 
ATOM   5396 H HG2  . PRO   B 1 98  ? 36.536 -26.895 6.462   1.00 15.59 ?  98  PRO   B HG2  1 
ATOM   5397 H HG3  . PRO   B 1 98  ? 35.263 -26.025 6.876   1.00 15.59 ?  98  PRO   B HG3  1 
ATOM   5398 H HD2  . PRO   B 1 98  ? 36.903 -25.096 5.158   1.00 14.33 ?  98  PRO   B HD2  1 
ATOM   5399 H HD3  . PRO   B 1 98  ? 36.232 -24.097 6.221   1.00 14.33 ?  98  PRO   B HD3  1 
ATOM   5400 N N    A ASN   B 1 99  ? 39.973 -26.594 9.085   0.40 13.81 ?  99  ASN   B N    1 
ATOM   5401 N N    B ASN   B 1 99  ? 39.923 -26.631 9.105   0.60 13.64 ?  99  ASN   B N    1 
ATOM   5402 C CA   A ASN   B 1 99  ? 40.976 -27.645 9.243   0.40 14.60 ?  99  ASN   B CA   1 
ATOM   5403 C CA   B ASN   B 1 99  ? 40.882 -27.713 9.280   0.60 14.08 ?  99  ASN   B CA   1 
ATOM   5404 C C    A ASN   B 1 99  ? 40.383 -28.723 10.144  0.40 16.23 ?  99  ASN   B C    1 
ATOM   5405 C C    B ASN   B 1 99  ? 40.205 -28.800 10.115  0.60 15.03 ?  99  ASN   B C    1 
ATOM   5406 O O    A ASN   B 1 99  ? 40.349 -28.576 11.368  0.40 16.87 ?  99  ASN   B O    1 
ATOM   5407 O O    B ASN   B 1 99  ? 40.030 -28.651 11.327  0.60 15.46 ?  99  ASN   B O    1 
ATOM   5408 C CB   A ASN   B 1 99  ? 42.258 -27.071 9.835   0.40 14.87 ?  99  ASN   B CB   1 
ATOM   5409 C CB   B ASN   B 1 99  ? 42.143 -27.183 9.945   0.60 14.79 ?  99  ASN   B CB   1 
ATOM   5410 C CG   A ASN   B 1 99  ? 43.406 -28.064 9.820   0.40 15.88 ?  99  ASN   B CG   1 
ATOM   5411 C CG   B ASN   B 1 99  ? 43.256 -28.201 9.959   0.60 15.72 ?  99  ASN   B CG   1 
ATOM   5412 O OD1  A ASN   B 1 99  ? 43.202 -29.263 9.983   0.40 16.35 ?  99  ASN   B OD1  1 
ATOM   5413 O OD1  B ASN   B 1 99  ? 43.009 -29.395 10.106  0.60 16.43 ?  99  ASN   B OD1  1 
ATOM   5414 N ND2  A ASN   B 1 99  ? 44.621 -27.565 9.621   0.40 16.54 ?  99  ASN   B ND2  1 
ATOM   5415 N ND2  B ASN   B 1 99  ? 44.490 -27.736 9.794   0.60 16.22 ?  99  ASN   B ND2  1 
ATOM   5416 H H    A ASN   B 1 99  ? 39.929 -26.061 9.756   0.40 16.55 ?  99  ASN   B H    1 
ATOM   5417 H H    B ASN   B 1 99  ? 39.868 -26.109 9.784   0.60 16.34 ?  99  ASN   B H    1 
ATOM   5418 H HA   A ASN   B 1 99  ? 41.177 -28.043 8.384   0.40 17.50 ?  99  ASN   B HA   1 
ATOM   5419 H HA   B ASN   B 1 99  ? 41.118 -28.091 8.418   0.60 16.87 ?  99  ASN   B HA   1 
ATOM   5420 H HB2  A ASN   B 1 99  ? 42.525 -26.300 9.321   0.40 17.82 ?  99  ASN   B HB2  1 
ATOM   5421 H HB2  B ASN   B 1 99  ? 42.451 -26.404 9.461   0.60 17.72 ?  99  ASN   B HB2  1 
ATOM   5422 H HB3  A ASN   B 1 99  ? 42.095 -26.821 10.760  0.40 17.82 ?  99  ASN   B HB3  1 
ATOM   5423 H HB3  B ASN   B 1 99  ? 41.942 -26.950 10.865  0.60 17.72 ?  99  ASN   B HB3  1 
ATOM   5424 H HD21 A ASN   B 1 99  ? 45.305 -28.085 9.604   0.40 19.82 ?  99  ASN   B HD21 1 
ATOM   5425 H HD21 B ASN   B 1 99  ? 45.158 -28.274 9.788   0.60 19.43 ?  99  ASN   B HD21 1 
ATOM   5426 H HD22 A ASN   B 1 99  ? 44.720 -26.718 9.512   0.40 19.82 ?  99  ASN   B HD22 1 
ATOM   5427 H HD22 B ASN   B 1 99  ? 44.618 -26.889 9.693   0.60 19.43 ?  99  ASN   B HD22 1 
ATOM   5428 N N    A VAL   B 1 100 ? 39.914 -29.811 9.527   0.40 18.32 ?  100 VAL   B N    1 
ATOM   5429 N N    B VAL   B 1 100 ? 39.793 -29.882 9.449   0.60 16.79 ?  100 VAL   B N    1 
ATOM   5430 C CA   A VAL   B 1 100 ? 39.315 -30.906 10.286  0.40 20.89 ?  100 VAL   B CA   1 
ATOM   5431 C CA   B VAL   B 1 100 ? 39.142 -30.991 10.143  0.60 19.49 ?  100 VAL   B CA   1 
ATOM   5432 C C    A VAL   B 1 100 ? 40.337 -31.542 11.217  0.40 22.03 ?  100 VAL   B C    1 
ATOM   5433 C C    B VAL   B 1 100 ? 40.100 -31.667 11.114  0.60 19.99 ?  100 VAL   B C    1 
ATOM   5434 O O    A VAL   B 1 100 ? 39.992 -31.982 12.321  0.40 22.37 ?  100 VAL   B O    1 
ATOM   5435 O O    B VAL   B 1 100 ? 39.674 -32.209 12.141  0.60 20.03 ?  100 VAL   B O    1 
ATOM   5436 C CB   A VAL   B 1 100 ? 38.678 -31.931 9.327   0.40 22.61 ?  100 VAL   B CB   1 
ATOM   5437 C CB   B VAL   B 1 100 ? 38.557 -31.987 9.122   0.60 22.03 ?  100 VAL   B CB   1 
ATOM   5438 C CG1  A VAL   B 1 100 ? 38.210 -33.165 10.086  0.40 23.24 ?  100 VAL   B CG1  1 
ATOM   5439 C CG1  B VAL   B 1 100 ? 38.047 -33.241 9.822   0.60 23.08 ?  100 VAL   B CG1  1 
ATOM   5440 C CG2  A VAL   B 1 100 ? 37.517 -31.295 8.576   0.40 23.05 ?  100 VAL   B CG2  1 
ATOM   5441 C CG2  B VAL   B 1 100 ? 37.441 -31.328 8.329   0.60 22.58 ?  100 VAL   B CG2  1 
ATOM   5442 H H    A VAL   B 1 100 ? 39.938 -29.943 8.679   0.40 21.96 ?  100 VAL   B H    1 
ATOM   5443 H H    B VAL   B 1 100 ? 39.866 -29.993 8.598   0.60 20.12 ?  100 VAL   B H    1 
ATOM   5444 H HA   A VAL   B 1 100 ? 38.601 -30.548 10.838  0.40 25.04 ?  100 VAL   B HA   1 
ATOM   5445 H HA   B VAL   B 1 100 ? 38.399 -30.641 10.658  0.60 23.36 ?  100 VAL   B HA   1 
ATOM   5446 H HB   A VAL   B 1 100 ? 39.341 -32.214 8.677   0.40 27.10 ?  100 VAL   B HB   1 
ATOM   5447 H HB   B VAL   B 1 100 ? 39.252 -32.256 8.503   0.60 26.41 ?  100 VAL   B HB   1 
ATOM   5448 H HG11 A VAL   B 1 100 ? 37.619 -33.681 9.512   0.40 27.87 ?  100 VAL   B HG11 1 
ATOM   5449 H HG11 B VAL   B 1 100 ? 37.485 -33.740 9.206   0.60 27.67 ?  100 VAL   B HG11 1 
ATOM   5450 H HG12 A VAL   B 1 100 ? 38.979 -33.702 10.331  0.40 27.87 ?  100 VAL   B HG12 1 
ATOM   5451 H HG12 B VAL   B 1 100 ? 38.802 -33.789 10.091  0.60 27.67 ?  100 VAL   B HG12 1 
ATOM   5452 H HG13 A VAL   B 1 100 ? 37.732 -32.884 10.881  0.40 27.87 ?  100 VAL   B HG13 1 
ATOM   5453 H HG13 B VAL   B 1 100 ? 37.530 -32.983 10.601  0.60 27.67 ?  100 VAL   B HG13 1 
ATOM   5454 H HG21 A VAL   B 1 100 ? 37.115 -31.958 7.994   0.40 27.63 ?  100 VAL   B HG21 1 
ATOM   5455 H HG21 B VAL   B 1 100 ? 37.087 -31.967 7.691   0.60 27.06 ?  100 VAL   B HG21 1 
ATOM   5456 H HG22 A VAL   B 1 100 ? 36.861 -30.979 9.219   0.40 27.63 ?  100 VAL   B HG22 1 
ATOM   5457 H HG22 B VAL   B 1 100 ? 36.741 -31.050 8.941   0.60 27.06 ?  100 VAL   B HG22 1 
ATOM   5458 H HG23 A VAL   B 1 100 ? 37.850 -30.551 8.052   0.40 27.63 ?  100 VAL   B HG23 1 
ATOM   5459 H HG23 B VAL   B 1 100 ? 37.800 -30.558 7.864   0.60 27.06 ?  100 VAL   B HG23 1 
ATOM   5460 N N    A ASN   B 1 101 ? 41.606 -31.600 10.802  0.40 22.93 ?  101 ASN   B N    1 
ATOM   5461 N N    B ASN   B 1 101 ? 41.400 -31.674 10.800  0.60 21.03 ?  101 ASN   B N    1 
ATOM   5462 C CA   A ASN   B 1 101 ? 42.648 -32.139 11.671  0.40 24.31 ?  101 ASN   B CA   1 
ATOM   5463 C CA   B ASN   B 1 101 ? 42.395 -32.215 11.723  0.60 22.78 ?  101 ASN   B CA   1 
ATOM   5464 C C    A ASN   B 1 101 ? 42.865 -31.287 12.912  0.40 25.78 ?  101 ASN   B C    1 
ATOM   5465 C C    B ASN   B 1 101 ? 42.520 -31.386 12.996  0.60 24.23 ?  101 ASN   B C    1 
ATOM   5466 O O    A ASN   B 1 101 ? 43.531 -31.743 13.850  0.40 26.19 ?  101 ASN   B O    1 
ATOM   5467 O O    B ASN   B 1 101 ? 43.084 -31.875 13.984  0.60 25.29 ?  101 ASN   B O    1 
ATOM   5468 C CB   A ASN   B 1 101 ? 43.964 -32.296 10.903  0.40 24.20 ?  101 ASN   B CB   1 
ATOM   5469 C CB   B ASN   B 1 101 ? 43.751 -32.346 11.022  0.60 22.87 ?  101 ASN   B CB   1 
ATOM   5470 C CG   A ASN   B 1 101 ? 43.914 -33.422 9.890   0.40 24.10 ?  101 ASN   B CG   1 
ATOM   5471 C CG   B ASN   B 1 101 ? 43.751 -33.425 9.955   0.60 22.82 ?  101 ASN   B CG   1 
ATOM   5472 O OD1  A ASN   B 1 101 ? 43.243 -34.430 10.102  0.40 24.60 ?  101 ASN   B OD1  1 
ATOM   5473 O OD1  B ASN   B 1 101 ? 43.053 -34.429 10.077  0.60 23.93 ?  101 ASN   B OD1  1 
ATOM   5474 N ND2  A ASN   B 1 101 ? 44.625 -33.255 8.783   0.40 23.81 ?  101 ASN   B ND2  1 
ATOM   5475 N ND2  B ASN   B 1 101 ? 44.532 -33.220 8.901   0.60 22.59 ?  101 ASN   B ND2  1 
ATOM   5476 H H    A ASN   B 1 101 ? 41.883 -31.333 10.033  0.40 27.49 ?  101 ASN   B H    1 
ATOM   5477 H H    B ASN   B 1 101 ? 41.719 -31.395 10.052  0.60 25.21 ?  101 ASN   B H    1 
ATOM   5478 H HA   A ASN   B 1 101 ? 42.376 -33.020 11.965  0.40 29.14 ?  101 ASN   B HA   1 
ATOM   5479 H HA   B ASN   B 1 101 ? 42.122 -33.098 11.994  0.60 27.30 ?  101 ASN   B HA   1 
ATOM   5480 H HB2  A ASN   B 1 101 ? 44.157 -31.473 10.428  0.40 29.01 ?  101 ASN   B HB2  1 
ATOM   5481 H HB2  B ASN   B 1 101 ? 43.980 -31.506 10.592  0.60 27.41 ?  101 ASN   B HB2  1 
ATOM   5482 H HB3  A ASN   B 1 101 ? 44.678 -32.490 11.532  0.40 29.01 ?  101 ASN   B HB3  1 
ATOM   5483 H HB3  B ASN   B 1 101 ? 44.428 -32.574 11.677  0.60 27.41 ?  101 ASN   B HB3  1 
ATOM   5484 H HD21 A ASN   B 1 101 ? 44.628 -33.867 8.178   0.40 28.55 ?  101 ASN   B HD21 1 
ATOM   5485 H HD21 B ASN   B 1 101 ? 44.568 -33.806 8.271   0.60 27.08 ?  101 ASN   B HD21 1 
ATOM   5486 H HD22 A ASN   B 1 101 ? 45.084 -32.538 8.671   0.40 28.55 ?  101 ASN   B HD22 1 
ATOM   5487 H HD22 B ASN   B 1 101 ? 45.005 -32.504 8.847   0.60 27.08 ?  101 ASN   B HD22 1 
ATOM   5488 N N    A LYS   B 1 102 ? 42.337 -30.065 12.933  0.40 27.05 ?  102 LYS   B N    1 
ATOM   5489 N N    B LYS   B 1 102 ? 42.000 -30.156 12.998  0.60 25.80 ?  102 LYS   B N    1 
ATOM   5490 C CA   A LYS   B 1 102 ? 42.302 -29.230 14.124  0.40 28.63 ?  102 LYS   B CA   1 
ATOM   5491 C CA   B LYS   B 1 102 ? 41.964 -29.309 14.183  0.60 27.79 ?  102 LYS   B CA   1 
ATOM   5492 C C    A LYS   B 1 102 ? 40.932 -29.228 14.791  0.40 28.24 ?  102 LYS   B C    1 
ATOM   5493 C C    B LYS   B 1 102 ? 40.575 -29.254 14.811  0.60 27.32 ?  102 LYS   B C    1 
ATOM   5494 O O    A LYS   B 1 102 ? 40.723 -28.479 15.750  0.40 28.54 ?  102 LYS   B O    1 
ATOM   5495 O O    B LYS   B 1 102 ? 40.358 -28.478 15.747  0.60 27.80 ?  102 LYS   B O    1 
ATOM   5496 C CB   A LYS   B 1 102 ? 42.700 -27.794 13.776  0.40 30.73 ?  102 LYS   B CB   1 
ATOM   5497 C CB   B LYS   B 1 102 ? 42.424 -27.886 13.848  0.60 30.62 ?  102 LYS   B CB   1 
ATOM   5498 C CG   A LYS   B 1 102 ? 44.157 -27.609 13.384  0.40 32.78 ?  102 LYS   B CG   1 
ATOM   5499 C CG   B LYS   B 1 102 ? 43.892 -27.748 13.465  0.60 33.37 ?  102 LYS   B CG   1 
ATOM   5500 C CD   A LYS   B 1 102 ? 44.424 -26.151 13.041  0.40 34.64 ?  102 LYS   B CD   1 
ATOM   5501 C CD   B LYS   B 1 102 ? 44.201 -26.315 13.048  0.60 35.79 ?  102 LYS   B CD   1 
ATOM   5502 C CE   A LYS   B 1 102 ? 45.882 -25.901 12.702  0.40 36.09 ?  102 LYS   B CE   1 
ATOM   5503 C CE   B LYS   B 1 102 ? 45.676 -26.112 12.733  0.60 37.68 ?  102 LYS   B CE   1 
ATOM   5504 N NZ   A LYS   B 1 102 ? 46.119 -24.473 12.345  0.40 36.93 ?  102 LYS   B NZ   1 
ATOM   5505 N NZ   B LYS   B 1 102 ? 45.946 -24.720 12.267  0.60 38.78 ?  102 LYS   B NZ   1 
ATOM   5506 H H    A LYS   B 1 102 ? 41.989 -29.690 12.244  0.40 32.44 ?  102 LYS   B H    1 
ATOM   5507 H H    B LYS   B 1 102 ? 41.634 -29.784 12.307  0.60 30.93 ?  102 LYS   B H    1 
ATOM   5508 H HA   A LYS   B 1 102 ? 42.944 -29.568 14.765  0.40 34.33 ?  102 LYS   B HA   1 
ATOM   5509 H HA   B LYS   B 1 102 ? 42.584 -29.666 14.837  0.60 33.33 ?  102 LYS   B HA   1 
ATOM   5510 H HB2  A LYS   B 1 102 ? 42.158 -27.495 13.029  0.40 36.85 ?  102 LYS   B HB2  1 
ATOM   5511 H HB2  B LYS   B 1 102 ? 41.898 -27.555 13.104  0.60 36.72 ?  102 LYS   B HB2  1 
ATOM   5512 H HB3  A LYS   B 1 102 ? 42.532 -27.231 14.547  0.40 36.85 ?  102 LYS   B HB3  1 
ATOM   5513 H HB3  B LYS   B 1 102 ? 42.275 -27.322 14.626  0.60 36.72 ?  102 LYS   B HB3  1 
ATOM   5514 H HG2  A LYS   B 1 102 ? 44.728 -27.860 14.127  0.40 39.31 ?  102 LYS   B HG2  1 
ATOM   5515 H HG2  B LYS   B 1 102 ? 44.450 -27.971 14.227  0.60 40.02 ?  102 LYS   B HG2  1 
ATOM   5516 H HG3  A LYS   B 1 102 ? 44.357 -28.151 12.604  0.40 39.31 ?  102 LYS   B HG3  1 
ATOM   5517 H HG3  B LYS   B 1 102 ? 44.089 -28.334 12.718  0.60 40.02 ?  102 LYS   B HG3  1 
ATOM   5518 H HD2  A LYS   B 1 102 ? 43.887 -25.903 12.272  0.40 41.54 ?  102 LYS   B HD2  1 
ATOM   5519 H HD2  B LYS   B 1 102 ? 43.692 -26.098 12.251  0.60 42.92 ?  102 LYS   B HD2  1 
ATOM   5520 H HD3  A LYS   B 1 102 ? 44.191 -25.597 13.803  0.40 41.54 ?  102 LYS   B HD3  1 
ATOM   5521 H HD3  B LYS   B 1 102 ? 43.962 -25.713 13.770  0.60 42.92 ?  102 LYS   B HD3  1 
ATOM   5522 H HE2  A LYS   B 1 102 ? 46.432 -26.118 13.471  0.40 43.28 ?  102 LYS   B HE2  1 
ATOM   5523 H HE2  B LYS   B 1 102 ? 46.200 -26.271 13.534  0.60 45.19 ?  102 LYS   B HE2  1 
ATOM   5524 H HE3  A LYS   B 1 102 ? 46.134 -26.450 11.943  0.40 43.28 ?  102 LYS   B HE3  1 
ATOM   5525 H HE3  B LYS   B 1 102 ? 45.943 -26.724 12.030  0.60 45.19 ?  102 LYS   B HE3  1 
ATOM   5526 H HZ1  A LYS   B 1 102 ? 46.977 -24.346 12.150  0.40 44.29 ?  102 LYS   B HZ1  1 
ATOM   5527 H HZ1  B LYS   B 1 102 ? 46.812 -24.620 12.089  0.60 46.51 ?  102 LYS   B HZ1  1 
ATOM   5528 H HZ2  A LYS   B 1 102 ? 45.625 -24.251 11.638  0.40 44.29 ?  102 LYS   B HZ2  1 
ATOM   5529 H HZ2  B LYS   B 1 102 ? 45.478 -24.550 11.529  0.60 46.51 ?  102 LYS   B HZ2  1 
ATOM   5530 H HZ3  A LYS   B 1 102 ? 45.896 -23.948 13.029  0.40 44.29 ?  102 LYS   B HZ3  1 
ATOM   5531 H HZ3  B LYS   B 1 102 ? 45.712 -24.137 12.898  0.60 46.51 ?  102 LYS   B HZ3  1 
ATOM   5532 N N    A GLY   B 1 103 ? 39.995 -30.039 14.303  0.40 27.85 ?  103 GLY   B N    1 
ATOM   5533 N N    B GLY   B 1 103 ? 39.629 -30.042 14.308  0.60 26.54 ?  103 GLY   B N    1 
ATOM   5534 C CA   A GLY   B 1 103 ? 38.667 -30.100 14.879  0.40 27.68 ?  103 GLY   B CA   1 
ATOM   5535 C CA   B GLY   B 1 103 ? 38.290 -30.071 14.859  0.60 26.10 ?  103 GLY   B CA   1 
ATOM   5536 C C    A GLY   B 1 103 ? 37.712 -29.027 14.410  0.40 27.26 ?  103 GLY   B C    1 
ATOM   5537 C C    B GLY   B 1 103 ? 37.371 -28.969 14.379  0.60 25.21 ?  103 GLY   B C    1 
ATOM   5538 O O    A GLY   B 1 103 ? 36.596 -28.942 14.935  0.40 27.80 ?  103 GLY   B O    1 
ATOM   5539 O O    B GLY   B 1 103 ? 36.286 -28.798 14.947  0.60 25.82 ?  103 GLY   B O    1 
ATOM   5540 H H    A GLY   B 1 103 ? 40.109 -30.569 13.634  0.40 33.40 ?  103 GLY   B H    1 
ATOM   5541 H H    B GLY   B 1 103 ? 39.745 -30.571 13.641  0.60 31.82 ?  103 GLY   B H    1 
ATOM   5542 H HA2  A GLY   B 1 103 ? 38.276 -30.963 14.674  0.40 33.19 ?  103 GLY   B HA2  1 
ATOM   5543 H HA2  B GLY   B 1 103 ? 37.880 -30.918 14.631  0.60 31.29 ?  103 GLY   B HA2  1 
ATOM   5544 H HA3  A GLY   B 1 103 ? 38.741 -30.027 15.843  0.40 33.19 ?  103 GLY   B HA3  1 
ATOM   5545 H HA3  B GLY   B 1 103 ? 38.352 -30.020 15.828  0.60 31.29 ?  103 GLY   B HA3  1 
ATOM   5546 N N    A GLU   B 1 104 ? 38.107 -28.206 13.440  0.40 26.15 ?  104 GLU   B N    1 
ATOM   5547 N N    B GLU   B 1 104 ? 37.761 -28.221 13.352  0.60 23.43 ?  104 GLU   B N    1 
ATOM   5548 C CA   A GLU   B 1 104 ? 37.253 -27.123 12.983  0.40 25.02 ?  104 GLU   B CA   1 
ATOM   5549 C CA   B GLU   B 1 104 ? 36.952 -27.109 12.883  0.60 21.49 ?  104 GLU   B CA   1 
ATOM   5550 C C    A GLU   B 1 104 ? 36.067 -27.668 12.186  0.40 25.37 ?  104 GLU   B C    1 
ATOM   5551 C C    B GLU   B 1 104 ? 35.793 -27.615 12.030  0.60 21.90 ?  104 GLU   B C    1 
ATOM   5552 O O    A GLU   B 1 104 ? 36.108 -28.766 11.623  0.40 25.57 ?  104 GLU   B O    1 
ATOM   5553 O O    B GLU   B 1 104 ? 35.875 -28.666 11.386  0.60 22.68 ?  104 GLU   B O    1 
ATOM   5554 C CB   A GLU   B 1 104 ? 38.071 -26.119 12.168  0.40 23.91 ?  104 GLU   B CB   1 
ATOM   5555 C CB   B GLU   B 1 104 ? 37.824 -26.117 12.113  0.60 20.22 ?  104 GLU   B CB   1 
ATOM   5556 C CG   A GLU   B 1 104 ? 39.185 -25.475 12.986  0.40 23.10 ?  104 GLU   B CG   1 
ATOM   5557 C CG   B GLU   B 1 104 ? 38.958 -25.583 12.979  0.60 19.44 ?  104 GLU   B CG   1 
ATOM   5558 C CD   A GLU   B 1 104 ? 40.085 -24.570 12.168  0.40 22.37 ?  104 GLU   B CD   1 
ATOM   5559 C CD   B GLU   B 1 104 ? 39.924 -24.673 12.254  0.60 18.42 ?  104 GLU   B CD   1 
ATOM   5560 O OE1  A GLU   B 1 104 ? 40.046 -24.643 10.922  0.40 21.29 ?  104 GLU   B OE1  1 
ATOM   5561 O OE1  B GLU   B 1 104 ? 39.945 -24.650 11.005  0.60 16.97 ?  104 GLU   B OE1  1 
ATOM   5562 O OE2  A GLU   B 1 104 ? 40.837 -23.782 12.778  0.40 23.08 -1 104 GLU   B OE2  1 
ATOM   5563 O OE2  B GLU   B 1 104 ? 40.682 -23.981 12.963  0.60 19.07 -1 104 GLU   B OE2  1 
ATOM   5564 H H    A GLU   B 1 104 ? 38.867 -28.254 13.041  0.40 31.36 ?  104 GLU   B H    1 
ATOM   5565 H H    B GLU   B 1 104 ? 38.493 -28.337 12.918  0.60 28.09 ?  104 GLU   B H    1 
ATOM   5566 H HA   A GLU   B 1 104 ? 36.901 -26.655 13.753  0.40 30.00 ?  104 GLU   B HA   1 
ATOM   5567 H HA   B GLU   B 1 104 ? 36.579 -26.647 13.652  0.60 25.76 ?  104 GLU   B HA   1 
ATOM   5568 H HB2  A GLU   B 1 104 ? 38.478 -26.575 11.415  0.40 28.66 ?  104 GLU   B HB2  1 
ATOM   5569 H HB2  B GLU   B 1 104 ? 38.210 -26.561 11.344  0.60 24.24 ?  104 GLU   B HB2  1 
ATOM   5570 H HB3  A GLU   B 1 104 ? 37.486 -25.413 11.853  0.40 28.66 ?  104 GLU   B HB3  1 
ATOM   5571 H HB3  B GLU   B 1 104 ? 37.278 -25.367 11.831  0.60 24.24 ?  104 GLU   B HB3  1 
ATOM   5572 H HG2  A GLU   B 1 104 ? 38.791 -24.940 13.693  0.40 27.70 ?  104 GLU   B HG2  1 
ATOM   5573 H HG2  B GLU   B 1 104 ? 38.580 -25.079 13.716  0.60 23.30 ?  104 GLU   B HG2  1 
ATOM   5574 H HG3  A GLU   B 1 104 ? 39.738 -26.174 13.374  0.40 27.70 ?  104 GLU   B HG3  1 
ATOM   5575 H HG3  B GLU   B 1 104 ? 39.473 -26.329 13.321  0.60 23.30 ?  104 GLU   B HG3  1 
ATOM   5576 N N    A ASP   B 1 105 ? 34.993 -26.880 12.157  0.40 25.74 ?  105 ASP   B N    1 
ATOM   5577 N N    B ASP   B 1 105 ? 34.700 -26.857 12.042  0.60 22.07 ?  105 ASP   B N    1 
ATOM   5578 C CA   A ASP   B 1 105 ? 33.715 -27.327 11.616  0.40 26.38 ?  105 ASP   B CA   1 
ATOM   5579 C CA   B ASP   B 1 105 ? 33.442 -27.330 11.476  0.60 23.10 ?  105 ASP   B CA   1 
ATOM   5580 C C    A ASP   B 1 105 ? 33.766 -27.358 10.092  0.40 25.33 ?  105 ASP   B C    1 
ATOM   5581 C C    B ASP   B 1 105 ? 33.523 -27.358 9.954   0.60 21.24 ?  105 ASP   B C    1 
ATOM   5582 O O    A ASP   B 1 105 ? 33.971 -26.323 9.448   0.40 25.11 ?  105 ASP   B O    1 
ATOM   5583 O O    B ASP   B 1 105 ? 33.694 -26.317 9.310   0.60 20.10 ?  105 ASP   B O    1 
ATOM   5584 C CB   A ASP   B 1 105 ? 32.605 -26.392 12.091  0.40 28.15 ?  105 ASP   B CB   1 
ATOM   5585 C CB   B ASP   B 1 105 ? 32.296 -26.433 11.944  0.60 26.00 ?  105 ASP   B CB   1 
ATOM   5586 C CG   A ASP   B 1 105 ? 31.228 -26.852 11.654  0.40 29.64 ?  105 ASP   B CG   1 
ATOM   5587 C CG   B ASP   B 1 105 ? 30.931 -27.010 11.610  0.60 28.33 ?  105 ASP   B CG   1 
ATOM   5588 O OD1  A ASP   B 1 105 ? 31.113 -27.975 11.119  0.40 29.94 ?  105 ASP   B OD1  1 
ATOM   5589 O OD1  B ASP   B 1 105 ? 30.861 -27.962 10.804  0.60 28.80 ?  105 ASP   B OD1  1 
ATOM   5590 O OD2  A ASP   B 1 105 ? 30.260 -26.083 11.839  0.40 30.51 -1 105 ASP   B OD2  1 
ATOM   5591 O OD2  B ASP   B 1 105 ? 29.925 -26.518 12.166  0.60 29.15 -1 105 ASP   B OD2  1 
ATOM   5592 H H    A ASP   B 1 105 ? 34.982 -26.073 12.455  0.40 30.86 ?  105 ASP   B H    1 
ATOM   5593 H H    B ASP   B 1 105 ? 34.663 -26.063 12.368  0.60 26.46 ?  105 ASP   B H    1 
ATOM   5594 H HA   A ASP   B 1 105 ? 33.523 -28.223 11.938  0.40 31.63 ?  105 ASP   B HA   1 
ATOM   5595 H HA   B ASP   B 1 105 ? 33.266 -28.231 11.790  0.60 27.70 ?  105 ASP   B HA   1 
ATOM   5596 H HB2  A ASP   B 1 105 ? 32.627 -26.343 13.061  0.40 33.75 ?  105 ASP   B HB2  1 
ATOM   5597 H HB2  B ASP   B 1 105 ? 32.355 -26.320 12.909  0.60 31.17 ?  105 ASP   B HB2  1 
ATOM   5598 H HB3  A ASP   B 1 105 ? 32.748 -25.513 11.712  0.40 33.75 ?  105 ASP   B HB3  1 
ATOM   5599 H HB3  B ASP   B 1 105 ? 32.370 -25.569 11.508  0.60 31.17 ?  105 ASP   B HB3  1 
ATOM   5600 N N    A ILE   B 1 106 ? 33.556 -28.546 9.519   0.40 24.78 ?  106 ILE   B N    1 
ATOM   5601 N N    B ILE   B 1 106 ? 33.393 -28.559 9.381   0.60 21.17 ?  106 ILE   B N    1 
ATOM   5602 C CA   A ILE   B 1 106 ? 33.567 -28.717 8.069   0.40 24.18 ?  106 ILE   B CA   1 
ATOM   5603 C CA   B ILE   B 1 106 ? 33.404 -28.722 7.933   0.60 20.86 ?  106 ILE   B CA   1 
ATOM   5604 C C    A ILE   B 1 106 ? 32.476 -27.897 7.388   0.40 23.32 ?  106 ILE   B C    1 
ATOM   5605 C C    B ILE   B 1 106 ? 32.323 -27.882 7.266   0.60 19.93 ?  106 ILE   B C    1 
ATOM   5606 O O    A ILE   B 1 106 ? 32.575 -27.608 6.190   0.40 22.97 ?  106 ILE   B O    1 
ATOM   5607 O O    B ILE   B 1 106 ? 32.438 -27.547 6.082   0.60 18.57 ?  106 ILE   B O    1 
ATOM   5608 C CB   A ILE   B 1 106 ? 33.459 -30.224 7.733   0.40 24.48 ?  106 ILE   B CB   1 
ATOM   5609 C CB   B ILE   B 1 106 ? 33.288 -30.223 7.578   0.60 21.80 ?  106 ILE   B CB   1 
ATOM   5610 C CG1  A ILE   B 1 106 ? 33.678 -30.474 6.239   0.40 24.55 ?  106 ILE   B CG1  1 
ATOM   5611 C CG1  B ILE   B 1 106 ? 33.601 -30.462 6.101   0.60 22.53 ?  106 ILE   B CG1  1 
ATOM   5612 C CG2  A ILE   B 1 106 ? 32.109 -30.780 8.173   0.40 24.92 ?  106 ILE   B CG2  1 
ATOM   5613 C CG2  B ILE   B 1 106 ? 31.899 -30.752 7.916   0.60 22.49 ?  106 ILE   B CG2  1 
ATOM   5614 C CD1  A ILE   B 1 106 ? 35.029 -30.013 5.741   0.40 24.48 ?  106 ILE   B CD1  1 
ATOM   5615 C CD1  B ILE   B 1 106 ? 34.988 -30.021 5.699   0.60 22.74 ?  106 ILE   B CD1  1 
ATOM   5616 H H    A ILE   B 1 106 ? 33.412 -29.272 9.955   0.40 29.71 ?  106 ILE   B H    1 
ATOM   5617 H H    B ILE   B 1 106 ? 33.309 -29.294 9.817   0.60 25.37 ?  106 ILE   B H    1 
ATOM   5618 H HA   A ILE   B 1 106 ? 34.420 -28.403 7.737   0.40 28.99 ?  106 ILE   B HA   1 
ATOM   5619 H HA   B ILE   B 1 106 ? 34.256 -28.405 7.604   0.60 25.01 ?  106 ILE   B HA   1 
ATOM   5620 H HB   A ILE   B 1 106 ? 34.151 -30.696 8.222   0.40 29.35 ?  106 ILE   B HB   1 
ATOM   5621 H HB   B ILE   B 1 106 ? 33.935 -30.716 8.109   0.60 26.13 ?  106 ILE   B HB   1 
ATOM   5622 H HG12 A ILE   B 1 106 ? 33.612 -31.429 6.069   0.40 29.43 ?  106 ILE   B HG12 1 
ATOM   5623 H HG12 B ILE   B 1 106 ? 33.531 -31.413 5.915   0.60 27.01 ?  106 ILE   B HG12 1 
ATOM   5624 H HG13 A ILE   B 1 106 ? 32.998 -30.005 5.735   0.40 29.43 ?  106 ILE   B HG13 1 
ATOM   5625 H HG13 B ILE   B 1 106 ? 32.965 -29.974 5.560   0.60 27.01 ?  106 ILE   B HG13 1 
ATOM   5626 H HG21 A ILE   B 1 106 ? 32.108 -31.742 8.044   0.40 29.88 ?  106 ILE   B HG21 1 
ATOM   5627 H HG21 B ILE   B 1 106 ? 31.907 -31.721 7.857   0.60 26.97 ?  106 ILE   B HG21 1 
ATOM   5628 H HG22 A ILE   B 1 106 ? 31.973 -30.574 9.110   0.40 29.88 ?  106 ILE   B HG22 1 
ATOM   5629 H HG22 B ILE   B 1 106 ? 31.668 -30.478 8.817   0.60 26.97 ?  106 ILE   B HG22 1 
ATOM   5630 H HG23 A ILE   B 1 106 ? 31.409 -30.375 7.639   0.40 29.88 ?  106 ILE   B HG23 1 
ATOM   5631 H HG23 B ILE   B 1 106 ? 31.259 -30.389 7.285   0.60 26.97 ?  106 ILE   B HG23 1 
ATOM   5632 H HD11 A ILE   B 1 106 ? 35.192 -30.403 4.869   0.40 29.35 ?  106 ILE   B HD11 1 
ATOM   5633 H HD11 B ILE   B 1 106 ? 35.222 -30.438 4.856   0.60 27.27 ?  106 ILE   B HD11 1 
ATOM   5634 H HD12 A ILE   B 1 106 ? 35.029 -29.045 5.676   0.40 29.35 ?  106 ILE   B HD12 1 
ATOM   5635 H HD12 B ILE   B 1 106 ? 34.999 -29.054 5.602   0.60 27.27 ?  106 ILE   B HD12 1 
ATOM   5636 H HD13 A ILE   B 1 106 ? 35.712 -30.305 6.366   0.40 29.35 ?  106 ILE   B HD13 1 
ATOM   5637 H HD13 B ILE   B 1 106 ? 35.619 -30.290 6.386   0.60 27.27 ?  106 ILE   B HD13 1 
ATOM   5638 N N    A GLN   B 1 107 ? 31.434 -27.506 8.126   0.40 23.24 ?  107 GLN   B N    1 
ATOM   5639 N N    B GLN   B 1 107 ? 31.280 -27.509 8.009   0.60 20.96 ?  107 GLN   B N    1 
ATOM   5640 C CA   A GLN   B 1 107 ? 30.336 -26.748 7.531   0.40 23.11 ?  107 GLN   B CA   1 
ATOM   5641 C CA   B GLN   B 1 107 ? 30.228 -26.669 7.450   0.60 22.05 ?  107 GLN   B CA   1 
ATOM   5642 C C    A GLN   B 1 107 ? 30.804 -25.410 6.968   0.40 20.73 ?  107 GLN   B C    1 
ATOM   5643 C C    B GLN   B 1 107 ? 30.750 -25.315 6.987   0.60 20.39 ?  107 GLN   B C    1 
ATOM   5644 O O    A GLN   B 1 107 ? 30.182 -24.876 6.043   0.40 20.98 ?  107 GLN   B O    1 
ATOM   5645 O O    B GLN   B 1 107 ? 30.112 -24.680 6.141   0.60 21.28 ?  107 GLN   B O    1 
ATOM   5646 C CB   A GLN   B 1 107 ? 29.236 -26.544 8.576   0.40 25.78 ?  107 GLN   B CB   1 
ATOM   5647 C CB   B GLN   B 1 107 ? 29.111 -26.489 8.482   0.60 25.69 ?  107 GLN   B CB   1 
ATOM   5648 C CG   A GLN   B 1 107 ? 27.914 -26.028 8.025   0.40 28.42 ?  107 GLN   B CG   1 
ATOM   5649 C CG   B GLN   B 1 107 ? 27.755 -26.127 7.891   0.60 29.35 ?  107 GLN   B CG   1 
ATOM   5650 C CD   A GLN   B 1 107 ? 27.864 -24.516 7.929   0.40 30.52 ?  107 GLN   B CD   1 
ATOM   5651 C CD   B GLN   B 1 107 ? 27.558 -24.629 7.735   0.60 32.25 ?  107 GLN   B CD   1 
ATOM   5652 O OE1  A GLN   B 1 107 ? 28.705 -23.815 8.495   0.40 31.29 ?  107 GLN   B OE1  1 
ATOM   5653 O OE1  B GLN   B 1 107 ? 28.348 -23.829 8.240   0.60 33.48 ?  107 GLN   B OE1  1 
ATOM   5654 N NE2  A GLN   B 1 107 ? 26.871 -24.003 7.209   0.40 31.23 ?  107 GLN   B NE2  1 
ATOM   5655 N NE2  B GLN   B 1 107 ? 26.496 -24.243 7.037   0.60 33.16 ?  107 GLN   B NE2  1 
ATOM   5656 H H    A GLN   B 1 107 ? 31.342 -27.671 8.963   0.40 27.87 ?  107 GLN   B H    1 
ATOM   5657 H H    B GLN   B 1 107 ? 31.162 -27.723 8.830   0.60 25.13 ?  107 GLN   B H    1 
ATOM   5658 H HA   A GLN   B 1 107 ? 29.961 -27.263 6.801   0.40 27.71 ?  107 GLN   B HA   1 
ATOM   5659 H HA   B GLN   B 1 107 ? 29.848 -27.118 6.679   0.60 26.43 ?  107 GLN   B HA   1 
ATOM   5660 H HB2  A GLN   B 1 107 ? 29.059 -27.395 9.004   0.40 30.91 ?  107 GLN   B HB2  1 
ATOM   5661 H HB2  B GLN   B 1 107 ? 29.004 -27.321 8.966   0.60 30.80 ?  107 GLN   B HB2  1 
ATOM   5662 H HB3  A GLN   B 1 107 ? 29.550 -25.908 9.237   0.40 30.91 ?  107 GLN   B HB3  1 
ATOM   5663 H HB3  B GLN   B 1 107 ? 29.366 -25.785 9.098   0.60 30.80 ?  107 GLN   B HB3  1 
ATOM   5664 H HG2  A GLN   B 1 107 ? 27.778 -26.387 7.135   0.40 34.08 ?  107 GLN   B HG2  1 
ATOM   5665 H HG2  B GLN   B 1 107 ? 27.672 -26.532 7.014   0.60 35.20 ?  107 GLN   B HG2  1 
ATOM   5666 H HG3  A GLN   B 1 107 ? 27.193 -26.318 8.610   0.40 34.08 ?  107 GLN   B HG3  1 
ATOM   5667 H HG3  B GLN   B 1 107 ? 27.057 -26.464 8.477   0.60 35.20 ?  107 GLN   B HG3  1 
ATOM   5668 H HE21 A GLN   B 1 107 ? 26.303 -24.525 6.826   0.40 37.45 ?  107 GLN   B HE21 1 
ATOM   5669 H HE21 B GLN   B 1 107 ? 25.967 -24.829 6.697   0.60 39.77 ?  107 GLN   B HE21 1 
ATOM   5670 H HE22 A GLN   B 1 107 ? 26.794 -23.151 7.126   0.40 37.45 ?  107 GLN   B HE22 1 
ATOM   5671 H HE22 B GLN   B 1 107 ? 26.340 -23.405 6.924   0.60 39.77 ?  107 GLN   B HE22 1 
ATOM   5672 N N    . LEU   B 1 108 ? 31.899 -24.862 7.500   1.00 18.20 ?  108 LEU   B N    1 
ATOM   5673 C CA   . LEU   B 1 108 ? 32.458 -23.574 7.086   1.00 16.13 ?  108 LEU   B CA   1 
ATOM   5674 C C    . LEU   B 1 108 ? 33.111 -23.611 5.713   1.00 14.24 ?  108 LEU   B C    1 
ATOM   5675 O O    . LEU   B 1 108 ? 33.539 -22.559 5.214   1.00 13.95 ?  108 LEU   B O    1 
ATOM   5676 C CB   . LEU   B 1 108 ? 33.471 -23.095 8.124   1.00 16.75 ?  108 LEU   B CB   1 
ATOM   5677 C CG   . LEU   B 1 108 ? 32.838 -22.648 9.439   1.00 18.00 ?  108 LEU   B CG   1 
ATOM   5678 C CD1  . LEU   B 1 108 ? 33.871 -22.552 10.546  1.00 18.22 ?  108 LEU   B CD1  1 
ATOM   5679 C CD2  . LEU   B 1 108 ? 32.140 -21.308 9.248   1.00 19.37 ?  108 LEU   B CD2  1 
ATOM   5680 H H    A LEU   B 1 108 ? 32.348 -25.234 8.131   0.40 21.81 ?  108 LEU   B H    1 
ATOM   5681 H H    B LEU   B 1 108 ? 32.363 -25.278 8.091   0.60 21.81 ?  108 LEU   B H    1 
ATOM   5682 H HA   . LEU   B 1 108 ? 31.741 -22.925 7.052   1.00 19.33 ?  108 LEU   B HA   1 
ATOM   5683 H HB2  . LEU   B 1 108 ? 34.082 -23.818 8.327   1.00 20.08 ?  108 LEU   B HB2  1 
ATOM   5684 H HB3  . LEU   B 1 108 ? 33.959 -22.340 7.762   1.00 20.08 ?  108 LEU   B HB3  1 
ATOM   5685 H HG   . LEU   B 1 108 ? 32.166 -23.294 9.710   1.00 21.57 ?  108 LEU   B HG   1 
ATOM   5686 H HD11 . LEU   B 1 108 ? 33.430 -22.293 11.373  1.00 21.84 ?  108 LEU   B HD11 1 
ATOM   5687 H HD12 . LEU   B 1 108 ? 34.295 -23.416 10.656  1.00 21.84 ?  108 LEU   B HD12 1 
ATOM   5688 H HD13 . LEU   B 1 108 ? 34.533 -21.885 10.304  1.00 21.84 ?  108 LEU   B HD13 1 
ATOM   5689 H HD21 . LEU   B 1 108 ? 31.851 -20.974 10.112  1.00 23.22 ?  108 LEU   B HD21 1 
ATOM   5690 H HD22 . LEU   B 1 108 ? 32.762 -20.683 8.845   1.00 23.22 ?  108 LEU   B HD22 1 
ATOM   5691 H HD23 . LEU   B 1 108 ? 31.371 -21.429 8.668   1.00 23.22 ?  108 LEU   B HD23 1 
ATOM   5692 N N    . LEU   B 1 109 ? 33.180 -24.786 5.092   1.00 13.23 ?  109 LEU   B N    1 
ATOM   5693 C CA   . LEU   B 1 109 ? 33.808 -24.901 3.785   1.00 12.58 ?  109 LEU   B CA   1 
ATOM   5694 C C    . LEU   B 1 109 ? 33.045 -24.116 2.724   1.00 12.10 ?  109 LEU   B C    1 
ATOM   5695 O O    . LEU   B 1 109 ? 33.657 -23.524 1.831   1.00 11.92 ?  109 LEU   B O    1 
ATOM   5696 C CB   . LEU   B 1 109 ? 33.924 -26.377 3.406   1.00 12.73 ?  109 LEU   B CB   1 
ATOM   5697 C CG   . LEU   B 1 109 ? 34.700 -26.708 2.132   1.00 12.69 ?  109 LEU   B CG   1 
ATOM   5698 C CD1  . LEU   B 1 109 ? 36.084 -26.075 2.140   1.00 13.10 ?  109 LEU   B CD1  1 
ATOM   5699 C CD2  . LEU   B 1 109 ? 34.813 -28.221 1.987   1.00 13.37 ?  109 LEU   B CD2  1 
ATOM   5700 H H    . LEU   B 1 109 ? 32.872 -25.527 5.400   1.00 15.85 ?  109 LEU   B H    1 
ATOM   5701 H HA   . LEU   B 1 109 ? 34.702 -24.535 3.834   1.00 15.07 ?  109 LEU   B HA   1 
ATOM   5702 H HB2  . LEU   B 1 109 ? 34.365 -26.840 4.134   1.00 15.24 ?  109 LEU   B HB2  1 
ATOM   5703 H HB3  . LEU   B 1 109 ? 33.028 -26.733 3.297   1.00 15.24 ?  109 LEU   B HB3  1 
ATOM   5704 H HG   . LEU   B 1 109 ? 34.211 -26.373 1.360   1.00 15.20 ?  109 LEU   B HG   1 
ATOM   5705 H HD11 . LEU   B 1 109 ? 36.599 -26.431 1.400   1.00 15.70 ?  109 LEU   B HD11 1 
ATOM   5706 H HD12 . LEU   B 1 109 ? 35.989 -25.115 2.047   1.00 15.70 ?  109 LEU   B HD12 1 
ATOM   5707 H HD13 . LEU   B 1 109 ? 36.519 -26.288 2.979   1.00 15.70 ?  109 LEU   B HD13 1 
ATOM   5708 H HD21 . LEU   B 1 109 ? 35.379 -28.425 1.225   1.00 16.02 ?  109 LEU   B HD21 1 
ATOM   5709 H HD22 . LEU   B 1 109 ? 35.201 -28.587 2.795   1.00 16.02 ?  109 LEU   B HD22 1 
ATOM   5710 H HD23 . LEU   B 1 109 ? 33.926 -28.596 1.847   1.00 16.02 ?  109 LEU   B HD23 1 
ATOM   5711 N N    . LYS   B 1 110 ? 31.712 -24.093 2.796   1.00 11.81 ?  110 LYS   B N    1 
ATOM   5712 C CA   . LYS   B 1 110 ? 30.956 -23.328 1.808   1.00 11.64 ?  110 LYS   B CA   1 
ATOM   5713 C C    . LYS   B 1 110 ? 31.290 -21.841 1.899   1.00 11.17 ?  110 LYS   B C    1 
ATOM   5714 O O    . LYS   B 1 110 ? 31.530 -21.180 0.883   1.00 11.10 ?  110 LYS   B O    1 
ATOM   5715 C CB   . LYS   B 1 110 ? 29.456 -23.576 1.965   1.00 12.46 ?  110 LYS   B CB   1 
ATOM   5716 C CG   . LYS   B 1 110 ? 28.648 -22.963 0.828   1.00 12.64 ?  110 LYS   B CG   1 
ATOM   5717 C CD   . LYS   B 1 110 ? 27.186 -23.404 0.858   1.00 13.09 ?  110 LYS   B CD   1 
ATOM   5718 C CE   . LYS   B 1 110 ? 26.395 -22.870 -0.339  1.00 13.72 ?  110 LYS   B CE   1 
ATOM   5719 N NZ   . LYS   B 1 110 ? 26.720 -23.545 -1.626  1.00 14.18 ?  110 LYS   B NZ   1 
ATOM   5720 H H    . LYS   B 1 110 ? 31.238 -24.501 3.382   1.00 14.14 ?  110 LYS   B H    1 
ATOM   5721 H HA   . LYS   B 1 110 ? 31.211 -23.630 0.920   1.00 13.94 ?  110 LYS   B HA   1 
ATOM   5722 H HB2  . LYS   B 1 110 ? 29.292 -24.534 1.968   1.00 14.92 ?  110 LYS   B HB2  1 
ATOM   5723 H HB3  . LYS   B 1 110 ? 29.153 -23.184 2.795   1.00 14.92 ?  110 LYS   B HB3  1 
ATOM   5724 H HG2  . LYS   B 1 110 ? 28.663 -21.998 0.902   1.00 15.14 ?  110 LYS   B HG2  1 
ATOM   5725 H HG3  . LYS   B 1 110 ? 29.020 -23.241 -0.023  1.00 15.14 ?  110 LYS   B HG3  1 
ATOM   5726 H HD2  . LYS   B 1 110 ? 27.141 -24.379 0.839   1.00 15.69 ?  110 LYS   B HD2  1 
ATOM   5727 H HD3  . LYS   B 1 110 ? 26.764 -23.076 1.670   1.00 15.69 ?  110 LYS   B HD3  1 
ATOM   5728 H HE2  . LYS   B 1 110 ? 25.447 -22.999 -0.173  1.00 16.44 ?  110 LYS   B HE2  1 
ATOM   5729 H HE3  . LYS   B 1 110 ? 26.587 -21.928 -0.441  1.00 16.44 ?  110 LYS   B HE3  1 
ATOM   5730 H HZ1  . LYS   B 1 110 ? 26.240 -23.195 -2.285  1.00 16.99 ?  110 LYS   B HZ1  1 
ATOM   5731 H HZ2  . LYS   B 1 110 ? 27.588 -23.438 -1.813  1.00 16.99 ?  110 LYS   B HZ2  1 
ATOM   5732 H HZ3  . LYS   B 1 110 ? 26.547 -24.416 -1.568  1.00 16.99 ?  110 LYS   B HZ3  1 
ATOM   5733 N N    . SER   B 1 111 ? 31.315 -21.296 3.118   1.00 11.31 ?  111 SER   B N    1 
ATOM   5734 C CA   . SER   B 1 111 ? 31.691 -19.895 3.296   1.00 11.47 ?  111 SER   B CA   1 
ATOM   5735 C C    . SER   B 1 111 ? 33.074 -19.625 2.716   1.00 10.93 ?  111 SER   B C    1 
ATOM   5736 O O    . SER   B 1 111 ? 33.296 -18.588 2.078   1.00 11.49 ?  111 SER   B O    1 
ATOM   5737 C CB   . SER   B 1 111 ? 31.663 -19.539 4.780   1.00 12.82 ?  111 SER   B CB   1 
ATOM   5738 O OG   . SER   B 1 111 ? 30.348 -19.565 5.292   1.00 15.10 ?  111 SER   B OG   1 
ATOM   5739 H H    . SER   B 1 111 ? 31.122 -21.714 3.845   1.00 13.55 ?  111 SER   B H    1 
ATOM   5740 H HA   . SER   B 1 111 ? 31.049 -19.332 2.837   1.00 13.74 ?  111 SER   B HA   1 
ATOM   5741 H HB2  . SER   B 1 111 ? 32.202 -20.181 5.269   1.00 15.36 ?  111 SER   B HB2  1 
ATOM   5742 H HB3  . SER   B 1 111 ? 32.019 -18.648 4.898   1.00 15.36 ?  111 SER   B HB3  1 
ATOM   5743 H HG   . SER   B 1 111 ? 30.350 -19.374 6.116   1.00 18.10 ?  111 SER   B HG   1 
ATOM   5744 N N    . ALA   B 1 112 ? 34.015 -20.548 2.926   1.00 11.10 ?  112 ALA   B N    1 
ATOM   5745 C CA   . ALA   B 1 112 ? 35.360 -20.371 2.383   1.00 11.00 ?  112 ALA   B CA   1 
ATOM   5746 C C    . ALA   B 1 112 ? 35.327 -20.267 0.861   1.00 10.17 ?  112 ALA   B C    1 
ATOM   5747 O O    . ALA   B 1 112 ? 35.957 -19.379 0.270   1.00 10.47 ?  112 ALA   B O    1 
ATOM   5748 C CB   . ALA   B 1 112 ? 36.270 -21.517 2.845   1.00 11.39 ?  112 ALA   B CB   1 
ATOM   5749 H H    . ALA   B 1 112 ? 33.900 -21.273 3.379   1.00 13.30 ?  112 ALA   B H    1 
ATOM   5750 H HA   . ALA   B 1 112 ? 35.725 -19.543 2.730   1.00 13.18 ?  112 ALA   B HA   1 
ATOM   5751 H HB1  . ALA   B 1 112 ? 37.159 -21.373 2.483   1.00 13.64 ?  112 ALA   B HB1  1 
ATOM   5752 H HB2  . ALA   B 1 112 ? 36.308 -21.515 3.817   1.00 13.64 ?  112 ALA   B HB2  1 
ATOM   5753 H HB3  . ALA   B 1 112 ? 35.910 -22.355 2.529   1.00 13.64 ?  112 ALA   B HB3  1 
ATOM   5754 N N    . TYR   B 1 113 ? 34.598 -21.173 0.202   1.00 10.26 ?  113 TYR   B N    1 
ATOM   5755 C CA   . TYR   B 1 113 ? 34.522 -21.123 -1.251  1.00 9.90  ?  113 TYR   B CA   1 
ATOM   5756 C C    . TYR   B 1 113 ? 33.817 -19.869 -1.762  1.00 9.89  ?  113 TYR   B C    1 
ATOM   5757 O O    . TYR   B 1 113 ? 34.088 -19.441 -2.885  1.00 10.12 ?  113 TYR   B O    1 
ATOM   5758 C CB   . TYR   B 1 113 ? 33.841 -22.383 -1.796  1.00 10.33 ?  113 TYR   B CB   1 
ATOM   5759 C CG   . TYR   B 1 113 ? 34.797 -23.539 -2.056  1.00 10.50 ?  113 TYR   B CG   1 
ATOM   5760 C CD1  . TYR   B 1 113 ? 35.796 -23.440 -3.024  1.00 11.23 ?  113 TYR   B CD1  1 
ATOM   5761 C CD2  . TYR   B 1 113 ? 34.700 -24.730 -1.347  1.00 10.99 ?  113 TYR   B CD2  1 
ATOM   5762 C CE1  . TYR   B 1 113 ? 36.669 -24.484 -3.274  1.00 11.05 ?  113 TYR   B CE1  1 
ATOM   5763 C CE2  . TYR   B 1 113 ? 35.573 -25.785 -1.597  1.00 11.06 ?  113 TYR   B CE2  1 
ATOM   5764 C CZ   . TYR   B 1 113 ? 36.546 -25.657 -2.565  1.00 11.18 ?  113 TYR   B CZ   1 
ATOM   5765 O OH   . TYR   B 1 113 ? 37.422 -26.673 -2.840  1.00 11.86 ?  113 TYR   B OH   1 
ATOM   5766 H H    . TYR   B 1 113 ? 34.138 -21.805 0.573   1.00 12.29 ?  113 TYR   B H    1 
ATOM   5767 H HA   . TYR   B 1 113 ? 35.427 -21.110 -1.590  1.00 11.85 ?  113 TYR   B HA   1 
ATOM   5768 H HB2  . TYR   B 1 113 ? 33.180 -22.690 -1.154  1.00 12.37 ?  113 TYR   B HB2  1 
ATOM   5769 H HB3  . TYR   B 1 113 ? 33.407 -22.164 -2.634  1.00 12.37 ?  113 TYR   B HB3  1 
ATOM   5770 H HD1  . TYR   B 1 113 ? 35.876 -22.650 -3.512  1.00 13.45 ?  113 TYR   B HD1  1 
ATOM   5771 H HD2  . TYR   B 1 113 ? 34.040 -24.821 -0.703  1.00 13.16 ?  113 TYR   B HD2  1 
ATOM   5772 H HE1  . TYR   B 1 113 ? 37.325 -24.397 -3.933  1.00 13.23 ?  113 TYR   B HE1  1 
ATOM   5773 H HE2  . TYR   B 1 113 ? 35.496 -26.578 -1.125  1.00 13.25 ?  113 TYR   B HE2  1 
ATOM   5774 H HH   . TYR   B 1 113 ? 37.247 -27.337 -2.352  1.00 14.20 ?  113 TYR   B HH   1 
ATOM   5775 N N    . GLU   B 1 114 ? 32.884 -19.300 -0.989  1.00 10.00 ?  114 GLU   B N    1 
ATOM   5776 C CA   . GLU   B 1 114 ? 32.196 -18.089 -1.435  1.00 9.90  ?  114 GLU   B CA   1 
ATOM   5777 C C    . GLU   B 1 114 ? 33.175 -16.962 -1.730  1.00 9.76  ?  114 GLU   B C    1 
ATOM   5778 O O    . GLU   B 1 114 ? 32.891 -16.100 -2.565  1.00 10.24 ?  114 GLU   B O    1 
ATOM   5779 C CB   . GLU   B 1 114 ? 31.139 -17.663 -0.414  1.00 10.55 ?  114 GLU   B CB   1 
ATOM   5780 C CG   . GLU   B 1 114 ? 29.925 -18.586 -0.475  1.00 10.74 ?  114 GLU   B CG   1 
ATOM   5781 C CD   . GLU   B 1 114 ? 28.906 -18.396 0.634   1.00 10.75 ?  114 GLU   B CD   1 
ATOM   5782 O OE1  . GLU   B 1 114 ? 29.197 -17.781 1.678   1.00 11.48 ?  114 GLU   B OE1  1 
ATOM   5783 O OE2  . GLU   B 1 114 ? 27.777 -18.927 0.469   1.00 11.85 -1 114 GLU   B OE2  1 
ATOM   5784 H H    . GLU   B 1 114 ? 32.638 -19.600 -0.216  1.00 11.97 ?  114 GLU   B H    1 
ATOM   5785 H HA   . GLU   B 1 114 ? 31.736 -18.293 -2.258  1.00 11.86 ?  114 GLU   B HA   1 
ATOM   5786 H HB2  . GLU   B 1 114 ? 31.515 -17.712 0.483   1.00 12.63 ?  114 GLU   B HB2  1 
ATOM   5787 H HB3  . GLU   B 1 114 ? 30.846 -16.764 -0.608  1.00 12.63 ?  114 GLU   B HB3  1 
ATOM   5788 H HG2  . GLU   B 1 114 ? 29.475 -18.444 -1.316  1.00 12.87 ?  114 GLU   B HG2  1 
ATOM   5789 H HG3  . GLU   B 1 114 ? 30.244 -19.509 -0.431  1.00 12.87 ?  114 GLU   B HG3  1 
ATOM   5790 N N    . ASN   B 1 115 ? 34.346 -16.958 -1.083  1.00 9.87  ?  115 ASN   B N    1 
ATOM   5791 C CA   . ASN   B 1 115 ? 35.334 -15.921 -1.370  1.00 9.86  ?  115 ASN   B CA   1 
ATOM   5792 C C    . ASN   B 1 115 ? 35.748 -15.935 -2.833  1.00 9.54  ?  115 ASN   B C    1 
ATOM   5793 O O    . ASN   B 1 115 ? 36.133 -14.890 -3.376  1.00 10.38 ?  115 ASN   B O    1 
ATOM   5794 C CB   . ASN   B 1 115 ? 36.574 -16.097 -0.487  1.00 10.54 ?  115 ASN   B CB   1 
ATOM   5795 C CG   . ASN   B 1 115 ? 36.304 -15.842 0.973   1.00 10.99 ?  115 ASN   B CG   1 
ATOM   5796 O OD1  . ASN   B 1 115 ? 36.307 -14.698 1.419   1.00 13.10 ?  115 ASN   B OD1  1 
ATOM   5797 N ND2  . ASN   B 1 115 ? 36.145 -16.914 1.748   1.00 10.98 ?  115 ASN   B ND2  1 
ATOM   5798 H H    . ASN   B 1 115 ? 34.584 -17.528 -0.479  1.00 11.82 ?  115 ASN   B H    1 
ATOM   5799 H HA   . ASN   B 1 115 ? 34.951 -15.054 -1.174  1.00 11.80 ?  115 ASN   B HA   1 
ATOM   5800 H HB2  . ASN   B 1 115 ? 36.905 -17.003 -0.576  1.00 12.63 ?  115 ASN   B HB2  1 
ATOM   5801 H HB3  . ASN   B 1 115 ? 37.256 -15.466 -0.769  1.00 12.63 ?  115 ASN   B HB3  1 
ATOM   5802 H HD21 . ASN   B 1 115 ? 35.991 -16.819 2.594   1.00 13.15 ?  115 ASN   B HD21 1 
ATOM   5803 H HD22 . ASN   B 1 115 ? 36.162 -17.702 1.407   1.00 13.15 ?  115 ASN   B HD22 1 
ATOM   5804 N N    . PHE   B 1 116 ? 35.722 -17.111 -3.475  1.00 9.24  ?  116 PHE   B N    1 
ATOM   5805 C CA   . PHE   B 1 116 ? 36.153 -17.200 -4.864  1.00 9.85  ?  116 PHE   B CA   1 
ATOM   5806 C C    . PHE   B 1 116 ? 35.250 -16.373 -5.774  1.00 9.78  ?  116 PHE   B C    1 
ATOM   5807 O O    . PHE   B 1 116 ? 35.685 -15.943 -6.846  1.00 10.05 ?  116 PHE   B O    1 
ATOM   5808 C CB   . PHE   B 1 116 ? 36.129 -18.650 -5.392  1.00 9.76  ?  116 PHE   B CB   1 
ATOM   5809 C CG   . PHE   B 1 116 ? 37.194 -19.603 -4.837  1.00 9.62  ?  116 PHE   B CG   1 
ATOM   5810 C CD1  . PHE   B 1 116 ? 37.844 -19.411 -3.633  1.00 10.31 ?  116 PHE   B CD1  1 
ATOM   5811 C CD2  . PHE   B 1 116 ? 37.490 -20.748 -5.570  1.00 10.08 ?  116 PHE   B CD2  1 
ATOM   5812 C CE1  . PHE   B 1 116 ? 38.778 -20.352 -3.174  1.00 10.46 ?  116 PHE   B CE1  1 
ATOM   5813 C CE2  . PHE   B 1 116 ? 38.419 -21.690 -5.123  1.00 10.25 ?  116 PHE   B CE2  1 
ATOM   5814 C CZ   . PHE   B 1 116 ? 39.060 -21.494 -3.924  1.00 10.13 ?  116 PHE   B CZ   1 
ATOM   5815 H H    . PHE   B 1 116 ? 35.445 -17.860 -3.132  1.00 11.06 ?  116 PHE   B H    1 
ATOM   5816 H HA   . PHE   B 1 116 ? 37.055 -16.865 -4.937  1.00 11.79 ?  116 PHE   B HA   1 
ATOM   5817 H HB2  . PHE   B 1 116 ? 35.258 -19.033 -5.188  1.00 11.68 ?  116 PHE   B HB2  1 
ATOM   5818 H HB3  . PHE   B 1 116 ? 36.241 -18.619 -6.357  1.00 11.68 ?  116 PHE   B HB3  1 
ATOM   5819 H HD1  . PHE   B 1 116 ? 37.653 -18.654 -3.122  1.00 12.35 ?  116 PHE   B HD1  1 
ATOM   5820 H HD2  . PHE   B 1 116 ? 37.045 -20.902 -6.375  1.00 12.07 ?  116 PHE   B HD2  1 
ATOM   5821 H HE1  . PHE   B 1 116 ? 39.218 -20.205 -2.365  1.00 12.53 ?  116 PHE   B HE1  1 
ATOM   5822 H HE2  . PHE   B 1 116 ? 38.600 -22.447 -5.629  1.00 12.27 ?  116 PHE   B HE2  1 
ATOM   5823 H HZ   . PHE   B 1 116 ? 39.692 -22.102 -3.617  1.00 12.13 ?  116 PHE   B HZ   1 
ATOM   5824 N N    . ASN   B 1 117 ? 33.981 -16.173 -5.391  1.00 10.09 ?  117 ASN   B N    1 
ATOM   5825 C CA   . ASN   B 1 117 ? 33.038 -15.470 -6.259  1.00 10.15 ?  117 ASN   B CA   1 
ATOM   5826 C C    . ASN   B 1 117 ? 33.347 -13.989 -6.403  1.00 10.60 ?  117 ASN   B C    1 
ATOM   5827 O O    . ASN   B 1 117 ? 32.752 -13.335 -7.260  1.00 11.71 ?  117 ASN   B O    1 
ATOM   5828 C CB   . ASN   B 1 117 ? 31.610 -15.694 -5.775  1.00 10.30 ?  117 ASN   B CB   1 
ATOM   5829 C CG   . ASN   B 1 117 ? 31.166 -17.102 -6.019  1.00 10.64 ?  117 ASN   B CG   1 
ATOM   5830 O OD1  . ASN   B 1 117 ? 31.514 -17.695 -7.047  1.00 11.46 ?  117 ASN   B OD1  1 
ATOM   5831 N ND2  . ASN   B 1 117 ? 30.432 -17.672 -5.076  1.00 10.54 ?  117 ASN   B ND2  1 
ATOM   5832 H H    . ASN   B 1 117 ? 33.650 -16.428 -4.636  1.00 12.09 ?  117 ASN   B H    1 
ATOM   5833 H HA   . ASN   B 1 117 ? 33.100 -15.863 -7.141  1.00 12.15 ?  117 ASN   B HA   1 
ATOM   5834 H HB2  . ASN   B 1 117 ? 31.560 -15.518 -4.819  1.00 12.34 ?  117 ASN   B HB2  1 
ATOM   5835 H HB3  . ASN   B 1 117 ? 31.011 -15.092 -6.252  1.00 12.34 ?  117 ASN   B HB3  1 
ATOM   5836 H HD21 . ASN   B 1 117 ? 30.160 -18.481 -5.170  1.00 12.63 ?  117 ASN   B HD21 1 
ATOM   5837 H HD22 . ASN   B 1 117 ? 30.220 -17.226 -4.370  1.00 12.63 ?  117 ASN   B HD22 1 
ATOM   5838 N N    . GLN   B 1 118 ? 34.289 -13.465 -5.626  1.00 10.30 ?  118 GLN   B N    1 
ATOM   5839 C CA   . GLN   B 1 118 ? 34.717 -12.078 -5.759  1.00 10.71 ?  118 GLN   B CA   1 
ATOM   5840 C C    . GLN   B 1 118 ? 35.781 -11.887 -6.833  1.00 11.03 ?  118 GLN   B C    1 
ATOM   5841 O O    . GLN   B 1 118 ? 36.247 -10.757 -7.021  1.00 12.51 ?  118 GLN   B O    1 
ATOM   5842 C CB   . GLN   B 1 118 ? 35.190 -11.544 -4.404  1.00 11.20 ?  118 GLN   B CB   1 
ATOM   5843 C CG   . GLN   B 1 118 ? 34.112 -11.588 -3.332  1.00 11.61 ?  118 GLN   B CG   1 
ATOM   5844 C CD   . GLN   B 1 118 ? 32.938 -10.677 -3.651  1.00 11.37 ?  118 GLN   B CD   1 
ATOM   5845 O OE1  . GLN   B 1 118 ? 33.122 -9.535  -4.090  1.00 12.15 ?  118 GLN   B OE1  1 
ATOM   5846 N NE2  . GLN   B 1 118 ? 31.727 -11.168 -3.435  1.00 12.05 ?  118 GLN   B NE2  1 
ATOM   5847 H H    . GLN   B 1 118 ? 34.705 -13.895 -5.009  1.00 12.34 ?  118 GLN   B H    1 
ATOM   5848 H HA   . GLN   B 1 118 ? 33.950 -11.546 -6.026  1.00 12.83 ?  118 GLN   B HA   1 
ATOM   5849 H HB2  . GLN   B 1 118 ? 35.938 -12.073 -4.096  1.00 13.41 ?  118 GLN   B HB2  1 
ATOM   5850 H HB3  . GLN   B 1 118 ? 35.462 -10.614 -4.506  1.00 13.41 ?  118 GLN   B HB3  1 
ATOM   5851 H HG2  . GLN   B 1 118 ? 33.778 -12.496 -3.255  1.00 13.90 ?  118 GLN   B HG2  1 
ATOM   5852 H HG3  . GLN   B 1 118 ? 34.495 -11.305 -2.484  1.00 13.90 ?  118 GLN   B HG3  1 
ATOM   5853 H HE21 . GLN   B 1 118 ? 31.637 -11.964 -3.125  1.00 14.43 ?  118 GLN   B HE21 1 
ATOM   5854 H HE22 . GLN   B 1 118 ? 31.039 -10.685 -3.601  1.00 14.43 ?  118 GLN   B HE22 1 
ATOM   5855 N N    . HIS   B 1 119 ? 36.142 -12.946 -7.560  1.00 10.29 ?  119 HIS   B N    1 
ATOM   5856 C CA   . HIS   B 1 119 ? 37.178 -12.893 -8.583  1.00 10.92 ?  119 HIS   B CA   1 
ATOM   5857 C C    . HIS   B 1 119 ? 36.698 -13.629 -9.818  1.00 10.81 ?  119 HIS   B C    1 
ATOM   5858 O O    . HIS   B 1 119 ? 36.187 -14.745 -9.714  1.00 11.66 ?  119 HIS   B O    1 
ATOM   5859 C CB   . HIS   B 1 119 ? 38.469 -13.515 -8.047  1.00 11.84 ?  119 HIS   B CB   1 
ATOM   5860 C CG   . HIS   B 1 119 ? 38.961 -12.809 -6.832  1.00 13.06 ?  119 HIS   B CG   1 
ATOM   5861 N ND1  . HIS   B 1 119 ? 39.761 -11.689 -6.905  1.00 14.63 ?  119 HIS   B ND1  1 
ATOM   5862 C CD2  . HIS   B 1 119 ? 38.679 -12.990 -5.523  1.00 14.17 ?  119 HIS   B CD2  1 
ATOM   5863 C CE1  . HIS   B 1 119 ? 39.985 -11.236 -5.684  1.00 15.61 ?  119 HIS   B CE1  1 
ATOM   5864 N NE2  . HIS   B 1 119 ? 39.332 -12.001 -4.829  1.00 15.60 ?  119 HIS   B NE2  1 
ATOM   5865 H H    . HIS   B 1 119 ? 35.781 -13.727 -7.480  1.00 12.33 ?  119 HIS   B H    1 
ATOM   5866 H HA   . HIS   B 1 119 ? 37.347 -11.967 -8.822  1.00 13.08 ?  119 HIS   B HA   1 
ATOM   5867 H HB2  . HIS   B 1 119 ? 38.307 -14.439 -7.818  1.00 14.18 ?  119 HIS   B HB2  1 
ATOM   5868 H HB3  . HIS   B 1 119 ? 39.155 -13.453 -8.734  1.00 14.18 ?  119 HIS   B HB3  1 
ATOM   5869 H HD2  . HIS   B 1 119 ? 38.151 -13.662 -5.162  1.00 16.97 ?  119 HIS   B HD2  1 
ATOM   5870 H HE1  . HIS   B 1 119 ? 40.526 -10.509 -5.460  1.00 18.70 ?  119 HIS   B HE1  1 
ATOM   5871 H HE2  . HIS   B 1 119 ? 39.350 -11.919 -3.972  1.00 18.70 ?  119 HIS   B HE2  1 
ATOM   5872 N N    . GLU   B 1 120 ? 36.849 -13.014 -10.990 1.00 11.36 ?  120 GLU   B N    1 
ATOM   5873 C CA   . GLU   B 1 120 ? 36.256 -13.604 -12.185 1.00 12.68 ?  120 GLU   B CA   1 
ATOM   5874 C C    . GLU   B 1 120 ? 36.934 -14.903 -12.602 1.00 11.59 ?  120 GLU   B C    1 
ATOM   5875 O O    . GLU   B 1 120 ? 36.277 -15.774 -13.183 1.00 11.97 ?  120 GLU   B O    1 
ATOM   5876 C CB   . GLU   B 1 120 ? 36.249 -12.598 -13.333 1.00 17.19 ?  120 GLU   B CB   1 
ATOM   5877 C CG   . GLU   B 1 120 ? 35.303 -11.435 -13.087 1.00 23.69 ?  120 GLU   B CG   1 
ATOM   5878 C CD   . GLU   B 1 120 ? 35.080 -10.578 -14.313 1.00 29.83 ?  120 GLU   B CD   1 
ATOM   5879 O OE1  . GLU   B 1 120 ? 36.058 -10.321 -15.046 1.00 32.75 ?  120 GLU   B OE1  1 
ATOM   5880 O OE2  . GLU   B 1 120 ? 33.924 -10.163 -14.540 1.00 33.01 -1 120 GLU   B OE2  1 
ATOM   5881 H H    . GLU   B 1 120 ? 37.273 -12.275 -11.117 1.00 13.60 ?  120 GLU   B H    1 
ATOM   5882 H HA   . GLU   B 1 120 ? 35.333 -13.817 -11.990 1.00 15.20 ?  120 GLU   B HA   1 
ATOM   5883 H HB2  . GLU   B 1 120 ? 37.136 -12.235 -13.452 1.00 20.60 ?  120 GLU   B HB2  1 
ATOM   5884 H HB3  . GLU   B 1 120 ? 35.958 -13.044 -14.147 1.00 20.60 ?  120 GLU   B HB3  1 
ATOM   5885 H HG2  . GLU   B 1 120 ? 34.440 -11.779 -12.804 1.00 28.40 ?  120 GLU   B HG2  1 
ATOM   5886 H HG3  . GLU   B 1 120 ? 35.673 -10.864 -12.399 1.00 28.40 ?  120 GLU   B HG3  1 
ATOM   5887 N N    . VAL   B 1 121 ? 38.233 -15.042 -12.341 1.00 11.23 ?  121 VAL   B N    1 
ATOM   5888 C CA   . VAL   B 1 121 ? 38.981 -16.248 -12.690 1.00 11.00 ?  121 VAL   B CA   1 
ATOM   5889 C C    . VAL   B 1 121 ? 40.097 -16.449 -11.674 1.00 10.69 ?  121 VAL   B C    1 
ATOM   5890 O O    . VAL   B 1 121 ? 40.771 -15.493 -11.280 1.00 11.41 ?  121 VAL   B O    1 
ATOM   5891 C CB   . VAL   B 1 121 ? 39.497 -16.209 -14.146 1.00 12.91 ?  121 VAL   B CB   1 
ATOM   5892 C CG1  . VAL   B 1 121 ? 40.371 -14.991 -14.400 1.00 14.40 ?  121 VAL   B CG1  1 
ATOM   5893 C CG2  . VAL   B 1 121 ? 40.228 -17.497 -14.495 1.00 14.33 ?  121 VAL   B CG2  1 
ATOM   5894 H H    . VAL   B 1 121 ? 38.716 -14.435 -11.962 1.00 13.46 ?  121 VAL   B H    1 
ATOM   5895 H HA   . VAL   B 1 121 ? 38.376 -17.002 -12.616 1.00 13.18 ?  121 VAL   B HA   1 
ATOM   5896 H HB   . VAL   B 1 121 ? 38.731 -16.144 -14.738 1.00 15.47 ?  121 VAL   B HB   1 
ATOM   5897 H HG11 . VAL   B 1 121 ? 40.669 -15.005 -15.321 1.00 17.26 ?  121 VAL   B HG11 1 
ATOM   5898 H HG12 . VAL   B 1 121 ? 39.849 -14.189 -14.233 1.00 17.26 ?  121 VAL   B HG12 1 
ATOM   5899 H HG13 . VAL   B 1 121 ? 41.133 -15.020 -13.802 1.00 17.26 ?  121 VAL   B HG13 1 
ATOM   5900 H HG21 . VAL   B 1 121 ? 40.430 -17.495 -15.445 1.00 17.17 ?  121 VAL   B HG21 1 
ATOM   5901 H HG22 . VAL   B 1 121 ? 41.052 -17.542 -13.984 1.00 17.17 ?  121 VAL   B HG22 1 
ATOM   5902 H HG23 . VAL   B 1 121 ? 39.660 -18.252 -14.280 1.00 17.17 ?  121 VAL   B HG23 1 
ATOM   5903 N N    . LEU   B 1 122 ? 40.280 -17.702 -11.242 1.00 10.24 ?  122 LEU   B N    1 
ATOM   5904 C CA   . LEU   B 1 122 ? 41.260 -18.055 -10.219 1.00 10.22 ?  122 LEU   B CA   1 
ATOM   5905 C C    . LEU   B 1 122 ? 41.920 -19.383 -10.550 1.00 9.71  ?  122 LEU   B C    1 
ATOM   5906 O O    . LEU   B 1 122 ? 41.262 -20.310 -11.040 1.00 11.03 ?  122 LEU   B O    1 
ATOM   5907 C CB   . LEU   B 1 122 ? 40.602 -18.298 -8.847  1.00 11.76 ?  122 LEU   B CB   1 
ATOM   5908 C CG   . LEU   B 1 122 ? 39.580 -17.265 -8.358  1.00 11.61 ?  122 LEU   B CG   1 
ATOM   5909 C CD1  . LEU   B 1 122 ? 38.171 -17.600 -8.827  1.00 12.66 ?  122 LEU   B CD1  1 
ATOM   5910 C CD2  . LEU   B 1 122 ? 39.643 -17.163 -6.851  1.00 11.51 ?  122 LEU   B CD2  1 
ATOM   5911 H H    . LEU   B 1 122 ? 39.837 -18.378 -11.534 1.00 12.26 ?  122 LEU   B H    1 
ATOM   5912 H HA   . LEU   B 1 122 ? 41.934 -17.360 -10.135 1.00 12.24 ?  122 LEU   B HA   1 
ATOM   5913 H HB2  . LEU   B 1 122 ? 40.147 -19.150 -8.881  1.00 14.08 ?  122 LEU   B HB2  1 
ATOM   5914 H HB3  . LEU   B 1 122 ? 41.306 -18.336 -8.181  1.00 14.08 ?  122 LEU   B HB3  1 
ATOM   5915 H HG   . LEU   B 1 122 ? 39.817 -16.397 -8.720  1.00 13.91 ?  122 LEU   B HG   1 
ATOM   5916 H HD11 . LEU   B 1 122 ? 37.558 -16.943 -8.459  1.00 15.17 ?  122 LEU   B HD11 1 
ATOM   5917 H HD12 . LEU   B 1 122 ? 38.147 -17.567 -9.795  1.00 15.17 ?  122 LEU   B HD12 1 
ATOM   5918 H HD13 . LEU   B 1 122 ? 37.938 -18.484 -8.514  1.00 15.17 ?  122 LEU   B HD13 1 
ATOM   5919 H HD21 . LEU   B 1 122 ? 38.968 -16.541 -6.544  1.00 13.78 ?  122 LEU   B HD21 1 
ATOM   5920 H HD22 . LEU   B 1 122 ? 39.486 -18.041 -6.466  1.00 13.78 ?  122 LEU   B HD22 1 
ATOM   5921 H HD23 . LEU   B 1 122 ? 40.527 -16.847 -6.590  1.00 13.78 ?  122 LEU   B HD23 1 
ATOM   5922 N N    . LEU   B 1 123 ? 43.205 -19.490 -10.192 1.00 9.68  ?  123 LEU   B N    1 
ATOM   5923 C CA   . LEU   B 1 123 ? 43.920 -20.760 -10.065 1.00 9.96  ?  123 LEU   B CA   1 
ATOM   5924 C C    . LEU   B 1 123 ? 43.893 -21.157 -8.593  1.00 9.48  ?  123 LEU   B C    1 
ATOM   5925 O O    . LEU   B 1 123 ? 44.246 -20.333 -7.739  1.00 10.37 ?  123 LEU   B O    1 
ATOM   5926 C CB   . LEU   B 1 123 ? 45.372 -20.573 -10.512 1.00 10.50 ?  123 LEU   B CB   1 
ATOM   5927 C CG   . LEU   B 1 123 ? 46.317 -21.758 -10.284 1.00 10.81 ?  123 LEU   B CG   1 
ATOM   5928 C CD1  . LEU   B 1 123 ? 45.884 -22.994 -11.075 1.00 11.27 ?  123 LEU   B CD1  1 
ATOM   5929 C CD2  . LEU   B 1 123 ? 47.742 -21.357 -10.640 1.00 11.71 ?  123 LEU   B CD2  1 
ATOM   5930 H H    . LEU   B 1 123 ? 43.698 -18.811 -9.989  1.00 11.59 ?  123 LEU   B H    1 
ATOM   5931 H HA   . LEU   B 1 123 ? 43.491 -21.449 -10.600 1.00 11.92 ?  123 LEU   B HA   1 
ATOM   5932 H HB2  . LEU   B 1 123 ? 45.369 -20.381 -11.462 1.00 12.57 ?  123 LEU   B HB2  1 
ATOM   5933 H HB3  . LEU   B 1 123 ? 45.738 -19.816 -10.030 1.00 12.57 ?  123 LEU   B HB3  1 
ATOM   5934 H HG   . LEU   B 1 123 ? 46.305 -21.996 -9.345  1.00 12.95 ?  123 LEU   B HG   1 
ATOM   5935 H HD11 . LEU   B 1 123 ? 46.520 -23.705 -10.921 1.00 13.49 ?  123 LEU   B HD11 1 
ATOM   5936 H HD12 . LEU   B 1 123 ? 45.000 -23.266 -10.775 1.00 13.49 ?  123 LEU   B HD12 1 
ATOM   5937 H HD13 . LEU   B 1 123 ? 45.855 -22.769 -12.019 1.00 13.49 ?  123 LEU   B HD13 1 
ATOM   5938 H HD21 . LEU   B 1 123 ? 48.329 -22.113 -10.495 1.00 14.03 ?  123 LEU   B HD21 1 
ATOM   5939 H HD22 . LEU   B 1 123 ? 47.771 -21.087 -11.572 1.00 14.03 ?  123 LEU   B HD22 1 
ATOM   5940 H HD23 . LEU   B 1 123 ? 48.008 -20.615 -10.073 1.00 14.03 ?  123 LEU   B HD23 1 
ATOM   5941 N N    . ALA   B 1 124 ? 43.473 -22.391 -8.283  1.00 9.49  ?  124 ALA   B N    1 
ATOM   5942 C CA   . ALA   B 1 124 ? 43.209 -22.707 -6.888  1.00 9.78  ?  124 ALA   B CA   1 
ATOM   5943 C C    . ALA   B 1 124 ? 43.489 -24.168 -6.569  1.00 9.58  ?  124 ALA   B C    1 
ATOM   5944 O O    . ALA   B 1 124 ? 43.352 -25.048 -7.436  1.00 10.12 ?  124 ALA   B O    1 
ATOM   5945 C CB   . ALA   B 1 124 ? 41.754 -22.402 -6.520  1.00 10.34 ?  124 ALA   B CB   1 
ATOM   5946 H H    . ALA   B 1 124 ? 43.320 -23.030 -8.847  1.00 11.37 ?  124 ALA   B H    1 
ATOM   5947 H HA   . ALA   B 1 124 ? 43.784 -22.163 -6.342  1.00 11.71 ?  124 ALA   B HA   1 
ATOM   5948 H HB1  . ALA   B 1 124 ? 41.603 -22.626 -5.588  1.00 12.38 ?  124 ALA   B HB1  1 
ATOM   5949 H HB2  . ALA   B 1 124 ? 41.585 -21.456 -6.662  1.00 12.38 ?  124 ALA   B HB2  1 
ATOM   5950 H HB3  . ALA   B 1 124 ? 41.160 -22.928 -7.083  1.00 12.38 ?  124 ALA   B HB3  1 
ATOM   5951 N N    . PRO   B 1 125 ? 43.779 -24.467 -5.305  1.00 9.70  ?  125 PRO   B N    1 
ATOM   5952 C CA   . PRO   B 1 125 ? 43.720 -25.836 -4.791  1.00 10.57 ?  125 PRO   B CA   1 
ATOM   5953 C C    . PRO   B 1 125 ? 42.319 -26.119 -4.250  1.00 10.43 ?  125 PRO   B C    1 
ATOM   5954 O O    . PRO   B 1 125 ? 41.519 -25.205 -4.041  1.00 10.99 ?  125 PRO   B O    1 
ATOM   5955 C CB   . PRO   B 1 125 ? 44.709 -25.768 -3.620  1.00 11.70 ?  125 PRO   B CB   1 
ATOM   5956 C CG   . PRO   B 1 125 ? 44.443 -24.374 -3.031  1.00 11.75 ?  125 PRO   B CG   1 
ATOM   5957 C CD   . PRO   B 1 125 ? 44.101 -23.498 -4.236  1.00 10.59 ?  125 PRO   B CD   1 
ATOM   5958 H HA   . PRO   B 1 125 ? 43.996 -26.494 -5.442  1.00 12.66 ?  125 PRO   B HA   1 
ATOM   5959 H HB2  . PRO   B 1 125 ? 44.507 -26.461 -2.967  1.00 14.01 ?  125 PRO   B HB2  1 
ATOM   5960 H HB3  . PRO   B 1 125 ? 45.618 -25.840 -3.938  1.00 14.01 ?  125 PRO   B HB3  1 
ATOM   5961 H HG2  . PRO   B 1 125 ? 43.693 -24.409 -2.409  1.00 14.07 ?  125 PRO   B HG2  1 
ATOM   5962 H HG3  . PRO   B 1 125 ? 45.239 -24.046 -2.576  1.00 14.07 ?  125 PRO   B HG3  1 
ATOM   5963 H HD2  . PRO   B 1 125 ? 43.334 -22.934 -4.044  1.00 12.69 ?  125 PRO   B HD2  1 
ATOM   5964 H HD3  . PRO   B 1 125 ? 44.874 -22.957 -4.487  1.00 12.69 ?  125 PRO   B HD3  1 
ATOM   5965 N N    . LEU   B 1 126 ? 42.050 -27.399 -3.975  1.00 10.94 ?  126 LEU   B N    1 
ATOM   5966 C CA   . LEU   B 1 126 ? 40.823 -27.766 -3.273  1.00 11.39 ?  126 LEU   B CA   1 
ATOM   5967 C C    . LEU   B 1 126 ? 40.930 -27.370 -1.807  1.00 11.45 ?  126 LEU   B C    1 
ATOM   5968 O O    . LEU   B 1 126 ? 41.828 -27.822 -1.092  1.00 13.35 ?  126 LEU   B O    1 
ATOM   5969 C CB   . LEU   B 1 126 ? 40.571 -29.261 -3.392  1.00 12.62 ?  126 LEU   B CB   1 
ATOM   5970 C CG   . LEU   B 1 126 ? 40.041 -29.737 -4.745  1.00 13.90 ?  126 LEU   B CG   1 
ATOM   5971 C CD1  . LEU   B 1 126 ? 40.083 -31.253 -4.837  1.00 15.33 ?  126 LEU   B CD1  1 
ATOM   5972 C CD2  . LEU   B 1 126 ? 38.623 -29.249 -4.983  1.00 14.10 ?  126 LEU   B CD2  1 
ATOM   5973 H H    . LEU   B 1 126 ? 42.571 -28.061 -4.162  1.00 13.10 ?  126 LEU   B H    1 
ATOM   5974 H HA   . LEU   B 1 126 ? 40.080 -27.290 -3.668  1.00 13.64 ?  126 LEU   B HA   1 
ATOM   5975 H HB2  . LEU   B 1 126 ? 41.402 -29.728 -3.225  1.00 15.11 ?  126 LEU   B HB2  1 
ATOM   5976 H HB3  . LEU   B 1 126 ? 39.915 -29.513 -2.725  1.00 15.11 ?  126 LEU   B HB3  1 
ATOM   5977 H HG   . LEU   B 1 126 ? 40.608 -29.383 -5.454  1.00 16.65 ?  126 LEU   B HG   1 
ATOM   5978 H HD11 . LEU   B 1 126 ? 39.745 -31.526 -5.706  1.00 18.37 ?  126 LEU   B HD11 1 
ATOM   5979 H HD12 . LEU   B 1 126 ? 40.995 -31.554 -4.726  1.00 18.37 ?  126 LEU   B HD12 1 
ATOM   5980 H HD13 . LEU   B 1 126 ? 39.522 -31.623 -4.136  1.00 18.37 ?  126 LEU   B HD13 1 
ATOM   5981 H HD21 . LEU   B 1 126 ? 38.280 -29.660 -5.791  1.00 16.90 ?  126 LEU   B HD21 1 
ATOM   5982 H HD22 . LEU   B 1 126 ? 38.078 -29.493 -4.224  1.00 16.90 ?  126 LEU   B HD22 1 
ATOM   5983 H HD23 . LEU   B 1 126 ? 38.639 -28.283 -5.086  1.00 16.90 ?  126 LEU   B HD23 1 
ATOM   5984 N N    . LEU   B 1 127 ? 40.002 -26.538 -1.348  1.00 11.05 ?  127 LEU   B N    1 
ATOM   5985 C CA   . LEU   B 1 127 ? 40.062 -26.051 0.018   1.00 11.35 ?  127 LEU   B CA   1 
ATOM   5986 C C    . LEU   B 1 127 ? 39.794 -27.176 1.012   1.00 11.16 ?  127 LEU   B C    1 
ATOM   5987 O O    . LEU   B 1 127 ? 38.974 -28.070 0.786   1.00 11.74 ?  127 LEU   B O    1 
ATOM   5988 C CB   . LEU   B 1 127 ? 39.045 -24.930 0.233   1.00 11.94 ?  127 LEU   B CB   1 
ATOM   5989 C CG   . LEU   B 1 127 ? 39.222 -23.662 -0.606  1.00 12.61 ?  127 LEU   B CG   1 
ATOM   5990 C CD1  . LEU   B 1 127 ? 38.096 -22.688 -0.276  1.00 12.68 ?  127 LEU   B CD1  1 
ATOM   5991 C CD2  . LEU   B 1 127 ? 40.587 -23.020 -0.387  1.00 13.29 ?  127 LEU   B CD2  1 
ATOM   5992 H H    . LEU   B 1 127 ? 39.337 -26.226 -1.809  1.00 13.24 ?  127 LEU   B H    1 
ATOM   5993 H HA   . LEU   B 1 127 ? 40.946 -25.688 0.194   1.00 13.59 ?  127 LEU   B HA   1 
ATOM   5994 H HB2  . LEU   B 1 127 ? 38.162 -25.280 0.037   1.00 14.30 ?  127 LEU   B HB2  1 
ATOM   5995 H HB3  . LEU   B 1 127 ? 39.079 -24.660 1.165   1.00 14.30 ?  127 LEU   B HB3  1 
ATOM   5996 H HG   . LEU   B 1 127 ? 39.138 -23.890 -1.541  1.00 15.11 ?  127 LEU   B HG   1 
ATOM   5997 H HD11 . LEU   B 1 127 ? 38.207 -21.880 -0.803  1.00 15.19 ?  127 LEU   B HD11 1 
ATOM   5998 H HD12 . LEU   B 1 127 ? 37.241 -23.100 -0.483  1.00 15.19 ?  127 LEU   B HD12 1 
ATOM   5999 H HD13 . LEU   B 1 127 ? 38.131 -22.467 0.671   1.00 15.19 ?  127 LEU   B HD13 1 
ATOM   6000 H HD21 . LEU   B 1 127 ? 40.616 -22.172 -0.858  1.00 15.92 ?  127 LEU   B HD21 1 
ATOM   6001 H HD22 . LEU   B 1 127 ? 40.721 -22.875 0.563   1.00 15.92 ?  127 LEU   B HD22 1 
ATOM   6002 H HD23 . LEU   B 1 127 ? 41.270 -23.614 -0.732  1.00 15.92 ?  127 LEU   B HD23 1 
ATOM   6003 N N    . SER   B 1 128 ? 40.469 -27.087 2.149   1.00 11.11 ?  128 SER   B N    1 
ATOM   6004 C CA   . SER   B 1 128 ? 40.364 -28.006 3.271   1.00 11.89 ?  128 SER   B CA   1 
ATOM   6005 C C    . SER   B 1 128 ? 40.860 -29.410 2.941   1.00 12.63 ?  128 SER   B C    1 
ATOM   6006 O O    . SER   B 1 128 ? 40.771 -30.295 3.791   1.00 14.15 ?  128 SER   B O    1 
ATOM   6007 C CB   . SER   B 1 128 ? 38.966 -28.020 3.905   1.00 12.12 ?  128 SER   B CB   1 
ATOM   6008 O OG   . SER   B 1 128 ? 38.648 -26.745 4.454   1.00 13.10 ?  128 SER   B OG   1 
ATOM   6009 H H    . SER   B 1 128 ? 41.037 -26.454 2.307   1.00 13.30 ?  128 SER   B H    1 
ATOM   6010 H HA   . SER   B 1 128 ? 40.955 -27.672 3.958   1.00 14.25 ?  128 SER   B HA   1 
ATOM   6011 H HB2  . SER   B 1 128 ? 38.306 -28.255 3.233   1.00 14.52 ?  128 SER   B HB2  1 
ATOM   6012 H HB3  . SER   B 1 128 ? 38.949 -28.690 4.621   1.00 14.52 ?  128 SER   B HB3  1 
ATOM   6013 H HG   . SER   B 1 128 ? 39.218 -26.547 5.040   1.00 15.70 ?  128 SER   B HG   1 
ATOM   6014 N N    . ALA   B 1 129 ? 41.434 -29.627 1.756   1.00 13.49 ?  129 ALA   B N    1 
ATOM   6015 C CA   . ALA   B 1 129 ? 41.981 -30.926 1.401   1.00 14.91 ?  129 ALA   B CA   1 
ATOM   6016 C C    . ALA   B 1 129 ? 43.368 -31.105 2.009   1.00 14.10 ?  129 ALA   B C    1 
ATOM   6017 O O    . ALA   B 1 129 ? 43.928 -30.201 2.646   1.00 13.94 ?  129 ALA   B O    1 
ATOM   6018 C CB   . ALA   B 1 129 ? 42.025 -31.092 -0.117  1.00 16.66 ?  129 ALA   B CB   1 
ATOM   6019 H H    . ALA   B 1 129 ? 41.507 -29.036 1.136   1.00 16.17 ?  129 ALA   B H    1 
ATOM   6020 H HA   . ALA   B 1 129 ? 41.407 -31.619 1.760   1.00 17.87 ?  129 ALA   B HA   1 
ATOM   6021 H HB1  . ALA   B 1 129 ? 42.389 -31.967 -0.328  1.00 19.97 ?  129 ALA   B HB1  1 
ATOM   6022 H HB2  . ALA   B 1 129 ? 41.124 -31.016 -0.469  1.00 19.97 ?  129 ALA   B HB2  1 
ATOM   6023 H HB3  . ALA   B 1 129 ? 42.589 -30.400 -0.495  1.00 19.97 ?  129 ALA   B HB3  1 
ATOM   6024 N N    . GLY   B 1 130 ? 43.917 -32.302 1.814   1.00 13.93 ?  130 GLY   B N    1 
ATOM   6025 C CA   . GLY   B 1 130 ? 45.304 -32.539 2.168   1.00 14.69 ?  130 GLY   B CA   1 
ATOM   6026 C C    . GLY   B 1 130 ? 45.516 -32.432 3.662   1.00 14.54 ?  130 GLY   B C    1 
ATOM   6027 O O    . GLY   B 1 130 ? 44.815 -33.071 4.462   1.00 15.26 ?  130 GLY   B O    1 
ATOM   6028 H H    . GLY   B 1 130 ? 43.515 -32.980 1.465   1.00 16.69 ?  130 GLY   B H    1 
ATOM   6029 H HA2  . GLY   B 1 130 ? 45.565 -33.433 1.876   1.00 17.60 ?  130 GLY   B HA2  1 
ATOM   6030 H HA3  . GLY   B 1 130 ? 45.874 -31.896 1.717   1.00 17.60 ?  130 GLY   B HA3  1 
ATOM   6031 N N    . ILE   B 1 131 ? 46.484 -31.595 4.050   1.00 14.68 ?  131 ILE   B N    1 
ATOM   6032 C CA   . ILE   B 1 131 ? 46.834 -31.458 5.456   1.00 15.42 ?  131 ILE   B CA   1 
ATOM   6033 C C    . ILE   B 1 131 ? 45.711 -30.861 6.287   1.00 15.08 ?  131 ILE   B C    1 
ATOM   6034 O O    . ILE   B 1 131 ? 45.780 -30.921 7.518   1.00 16.29 ?  131 ILE   B O    1 
ATOM   6035 C CB   . ILE   B 1 131 ? 48.152 -30.675 5.650   1.00 17.21 ?  131 ILE   B CB   1 
ATOM   6036 C CG1  . ILE   B 1 131 ? 47.984 -29.203 5.249   1.00 18.17 ?  131 ILE   B CG1  1 
ATOM   6037 C CG2  . ILE   B 1 131 ? 49.285 -31.336 4.865   1.00 17.96 ?  131 ILE   B CG2  1 
ATOM   6038 C CD1  . ILE   B 1 131 ? 49.193 -28.341 5.564   1.00 19.48 ?  131 ILE   B CD1  1 
ATOM   6039 H H    . ILE   B 1 131 ? 46.948 -31.102 3.518   1.00 17.59 ?  131 ILE   B H    1 
ATOM   6040 H HA   . ILE   B 1 131 ? 46.984 -32.348 5.805   1.00 18.47 ?  131 ILE   B HA   1 
ATOM   6041 H HB   . ILE   B 1 131 ? 48.379 -30.705 6.593   1.00 20.62 ?  131 ILE   B HB   1 
ATOM   6042 H HG12 . ILE   B 1 131 ? 47.822 -29.158 4.294   1.00 21.78 ?  131 ILE   B HG12 1 
ATOM   6043 H HG13 . ILE   B 1 131 ? 47.225 -28.826 5.726   1.00 21.78 ?  131 ILE   B HG13 1 
ATOM   6044 H HG21 . ILE   B 1 131 ? 50.124 -30.927 5.126   1.00 21.52 ?  131 ILE   B HG21 1 
ATOM   6045 H HG22 . ILE   B 1 131 ? 49.295 -32.281 5.068   1.00 21.52 ?  131 ILE   B HG22 1 
ATOM   6046 H HG23 . ILE   B 1 131 ? 49.128 -31.199 3.918   1.00 21.52 ?  131 ILE   B HG23 1 
ATOM   6047 H HD11 . ILE   B 1 131 ? 48.975 -27.416 5.371   1.00 23.35 ?  131 ILE   B HD11 1 
ATOM   6048 H HD12 . ILE   B 1 131 ? 49.413 -28.442 6.503   1.00 23.35 ?  131 ILE   B HD12 1 
ATOM   6049 H HD13 . ILE   B 1 131 ? 49.935 -28.630 5.014   1.00 23.35 ?  131 ILE   B HD13 1 
ATOM   6050 N N    . PHE   B 1 132 ? 44.684 -30.286 5.651   1.00 13.56 ?  132 PHE   B N    1 
ATOM   6051 C CA   . PHE   B 1 132 ? 43.515 -29.784 6.370   1.00 13.78 ?  132 PHE   B CA   1 
ATOM   6052 C C    . PHE   B 1 132 ? 42.492 -30.877 6.686   1.00 14.83 ?  132 PHE   B C    1 
ATOM   6053 O O    . PHE   B 1 132 ? 41.579 -30.632 7.483   1.00 16.58 ?  132 PHE   B O    1 
ATOM   6054 C CB   . PHE   B 1 132 ? 42.848 -28.652 5.577   1.00 13.02 ?  132 PHE   B CB   1 
ATOM   6055 C CG   . PHE   B 1 132 ? 43.552 -27.311 5.685   1.00 13.01 ?  132 PHE   B CG   1 
ATOM   6056 C CD1  . PHE   B 1 132 ? 44.844 -27.130 5.206   1.00 14.41 ?  132 PHE   B CD1  1 
ATOM   6057 C CD2  . PHE   B 1 132 ? 42.887 -26.212 6.209   1.00 12.84 ?  132 PHE   B CD2  1 
ATOM   6058 C CE1  . PHE   B 1 132 ? 45.465 -25.892 5.295   1.00 15.11 ?  132 PHE   B CE1  1 
ATOM   6059 C CE2  . PHE   B 1 132 ? 43.501 -24.973 6.297   1.00 13.19 ?  132 PHE   B CE2  1 
ATOM   6060 C CZ   . PHE   B 1 132 ? 44.788 -24.815 5.835   1.00 14.54 ?  132 PHE   B CZ   1 
ATOM   6061 H H    . PHE   B 1 132 ? 44.646 -30.165 4.798   1.00 16.25 ?  132 PHE   B H    1 
ATOM   6062 H HA   . PHE   B 1 132 ? 43.814 -29.405 7.209   1.00 16.51 ?  132 PHE   B HA   1 
ATOM   6063 H HB2  . PHE   B 1 132 ? 42.839 -28.899 4.639   1.00 15.60 ?  132 PHE   B HB2  1 
ATOM   6064 H HB3  . PHE   B 1 132 ? 41.942 -28.538 5.898   1.00 15.60 ?  132 PHE   B HB3  1 
ATOM   6065 H HD1  . PHE   B 1 132 ? 45.305 -27.856 4.845   1.00 17.26 ?  132 PHE   B HD1  1 
ATOM   6066 H HD2  . PHE   B 1 132 ? 42.016 -26.317 6.521   1.00 15.38 ?  132 PHE   B HD2  1 
ATOM   6067 H HE1  . PHE   B 1 132 ? 46.337 -25.791 4.985   1.00 18.10 ?  132 PHE   B HE1  1 
ATOM   6068 H HE2  . PHE   B 1 132 ? 43.040 -24.251 6.664   1.00 15.80 ?  132 PHE   B HE2  1 
ATOM   6069 H HZ   . PHE   B 1 132 ? 45.205 -23.983 5.898   1.00 17.42 ?  132 PHE   B HZ   1 
ATOM   6070 N N    . GLY   B 1 133 ? 42.603 -32.066 6.082   1.00 13.98 ?  133 GLY   B N    1 
ATOM   6071 C CA   . GLY   B 1 133 ? 41.894 -33.236 6.570   1.00 14.98 ?  133 GLY   B CA   1 
ATOM   6072 C C    . GLY   B 1 133 ? 40.496 -33.498 6.035   1.00 15.39 ?  133 GLY   B C    1 
ATOM   6073 O O    . GLY   B 1 133 ? 39.906 -34.516 6.408   1.00 17.42 ?  133 GLY   B O    1 
ATOM   6074 H H    . GLY   B 1 133 ? 43.095 -32.213 5.387   1.00 16.75 ?  133 GLY   B H    1 
ATOM   6075 H HA2  . GLY   B 1 133 ? 42.429 -34.017 6.369   1.00 17.95 ?  133 GLY   B HA2  1 
ATOM   6076 H HA3  . GLY   B 1 133 ? 41.832 -33.164 7.536   1.00 17.95 ?  133 GLY   B HA3  1 
ATOM   6077 N N    . ALA   B 1 134 ? 39.934 -32.632 5.200   1.00 14.74 ?  134 ALA   B N    1 
ATOM   6078 C CA   . ALA   B 1 134 ? 38.607 -32.906 4.663   1.00 14.86 ?  134 ALA   B CA   1 
ATOM   6079 C C    . ALA   B 1 134 ? 38.691 -33.902 3.511   1.00 15.09 ?  134 ALA   B C    1 
ATOM   6080 O O    . ALA   B 1 134 ? 39.743 -34.090 2.896   1.00 16.30 ?  134 ALA   B O    1 
ATOM   6081 C CB   . ALA   B 1 134 ? 37.940 -31.615 4.188   1.00 15.40 ?  134 ALA   B CB   1 
ATOM   6082 H H    . ALA   B 1 134 ? 40.291 -31.887 4.942   1.00 17.66 ?  134 ALA   B H    1 
ATOM   6083 H HA   . ALA   B 1 134 ? 38.055 -33.287 5.363   1.00 17.81 ?  134 ALA   B HA   1 
ATOM   6084 H HB1  . ALA   B 1 134 ? 37.057 -31.824 3.848   1.00 18.45 ?  134 ALA   B HB1  1 
ATOM   6085 H HB2  . ALA   B 1 134 ? 37.868 -30.999 4.936   1.00 18.45 ?  134 ALA   B HB2  1 
ATOM   6086 H HB3  . ALA   B 1 134 ? 38.481 -31.218 3.487   1.00 18.45 ?  134 ALA   B HB3  1 
ATOM   6087 N N    . ASP   B 1 135 ? 37.561 -34.536 3.224   1.00 15.05 ?  135 ASP   B N    1 
ATOM   6088 C CA   . ASP   B 1 135 ? 37.461 -35.429 2.077   1.00 15.55 ?  135 ASP   B CA   1 
ATOM   6089 C C    . ASP   B 1 135 ? 37.566 -34.594 0.808   1.00 14.73 ?  135 ASP   B C    1 
ATOM   6090 O O    . ASP   B 1 135 ? 36.716 -33.718 0.587   1.00 14.62 ?  135 ASP   B O    1 
ATOM   6091 C CB   . ASP   B 1 135 ? 36.116 -36.159 2.128   1.00 17.31 ?  135 ASP   B CB   1 
ATOM   6092 C CG   . ASP   B 1 135 ? 35.926 -37.145 0.987   1.00 19.21 ?  135 ASP   B CG   1 
ATOM   6093 O OD1  . ASP   B 1 135 ? 36.795 -37.205 0.091   1.00 19.23 ?  135 ASP   B OD1  1 
ATOM   6094 O OD2  . ASP   B 1 135 ? 34.911 -37.881 1.002   1.00 22.47 -1 135 ASP   B OD2  1 
ATOM   6095 H H    . ASP   B 1 135 ? 36.836 -34.461 3.680   1.00 18.04 ?  135 ASP   B H    1 
ATOM   6096 H HA   . ASP   B 1 135 ? 38.177 -36.080 2.108   1.00 18.63 ?  135 ASP   B HA   1 
ATOM   6097 H HB2  . ASP   B 1 135 ? 36.061 -36.649 2.962   1.00 20.74 ?  135 ASP   B HB2  1 
ATOM   6098 H HB3  . ASP   B 1 135 ? 35.404 -35.504 2.078   1.00 20.74 ?  135 ASP   B HB3  1 
ATOM   6099 N N    . PRO   B 1 136 ? 38.573 -34.811 -0.045  1.00 14.74 ?  136 PRO   B N    1 
ATOM   6100 C CA   . PRO   B 1 136 ? 38.678 -33.985 -1.260  1.00 14.00 ?  136 PRO   B CA   1 
ATOM   6101 C C    . PRO   B 1 136 ? 37.494 -34.135 -2.190  1.00 13.51 ?  136 PRO   B C    1 
ATOM   6102 O O    . PRO   B 1 136 ? 37.171 -33.188 -2.916  1.00 13.23 ?  136 PRO   B O    1 
ATOM   6103 C CB   . PRO   B 1 136 ? 39.986 -34.466 -1.906  1.00 15.37 ?  136 PRO   B CB   1 
ATOM   6104 C CG   . PRO   B 1 136 ? 40.193 -35.849 -1.367  1.00 16.28 ?  136 PRO   B CG   1 
ATOM   6105 C CD   . PRO   B 1 136 ? 39.637 -35.826 0.030   1.00 15.90 ?  136 PRO   B CD   1 
ATOM   6106 H HA   . PRO   B 1 136 ? 38.770 -33.048 -1.024  1.00 16.77 ?  136 PRO   B HA   1 
ATOM   6107 H HB2  . PRO   B 1 136 ? 39.886 -34.486 -2.873  1.00 18.42 ?  136 PRO   B HB2  1 
ATOM   6108 H HB3  . PRO   B 1 136 ? 40.713 -33.880 -1.649  1.00 18.42 ?  136 PRO   B HB3  1 
ATOM   6109 H HG2  . PRO   B 1 136 ? 39.714 -36.489 -1.913  1.00 19.51 ?  136 PRO   B HG2  1 
ATOM   6110 H HG3  . PRO   B 1 136 ? 41.141 -36.052 -1.350  1.00 19.51 ?  136 PRO   B HG3  1 
ATOM   6111 H HD2  . PRO   B 1 136 ? 39.259 -36.689 0.260   1.00 19.06 ?  136 PRO   B HD2  1 
ATOM   6112 H HD3  . PRO   B 1 136 ? 40.316 -35.553 0.668   1.00 19.06 ?  136 PRO   B HD3  1 
ATOM   6113 N N    . ILE   B 1 137 ? 36.840 -35.300 -2.198  1.00 13.85 ?  137 ILE   B N    1 
ATOM   6114 C CA   . ILE   B 1 137 ? 35.624 -35.469 -2.990  1.00 14.55 ?  137 ILE   B CA   1 
ATOM   6115 C C    . ILE   B 1 137 ? 34.545 -34.504 -2.518  1.00 14.20 ?  137 ILE   B C    1 
ATOM   6116 O O    . ILE   B 1 137 ? 33.832 -33.893 -3.326  1.00 13.71 ?  137 ILE   B O    1 
ATOM   6117 C CB   . ILE   B 1 137 ? 35.152 -36.937 -2.931  1.00 16.59 ?  137 ILE   B CB   1 
ATOM   6118 C CG1  . ILE   B 1 137 ? 36.135 -37.835 -3.683  1.00 19.12 ?  137 ILE   B CG1  1 
ATOM   6119 C CG2  . ILE   B 1 137 ? 33.744 -37.070 -3.503  1.00 17.38 ?  137 ILE   B CG2  1 
ATOM   6120 C CD1  . ILE   B 1 137 ? 35.835 -39.314 -3.561  1.00 21.47 ?  137 ILE   B CD1  1 
ATOM   6121 H H    . ILE   B 1 137 ? 37.072 -35.999 -1.757  1.00 16.60 ?  137 ILE   B H    1 
ATOM   6122 H HA   . ILE   B 1 137 ? 35.816 -35.260 -3.917  1.00 17.43 ?  137 ILE   B HA   1 
ATOM   6123 H HB   . ILE   B 1 137 ? 35.124 -37.212 -2.004  1.00 19.88 ?  137 ILE   B HB   1 
ATOM   6124 H HG12 . ILE   B 1 137 ? 36.108 -37.603 -4.625  1.00 22.91 ?  137 ILE   B HG12 1 
ATOM   6125 H HG13 . ILE   B 1 137 ? 37.022 -37.681 -3.330  1.00 22.91 ?  137 ILE   B HG13 1 
ATOM   6126 H HG21 . ILE   B 1 137 ? 33.534 -38.010 -3.622  1.00 20.84 ?  137 ILE   B HG21 1 
ATOM   6127 H HG22 . ILE   B 1 137 ? 33.107 -36.676 -2.887  1.00 20.84 ?  137 ILE   B HG22 1 
ATOM   6128 H HG23 . ILE   B 1 137 ? 33.705 -36.615 -4.358  1.00 20.84 ?  137 ILE   B HG23 1 
ATOM   6129 H HD11 . ILE   B 1 137 ? 36.596 -39.810 -3.891  1.00 25.74 ?  137 ILE   B HD11 1 
ATOM   6130 H HD12 . ILE   B 1 137 ? 35.674 -39.528 -2.629  1.00 25.74 ?  137 ILE   B HD12 1 
ATOM   6131 H HD13 . ILE   B 1 137 ? 35.048 -39.526 -4.089  1.00 25.74 ?  137 ILE   B HD13 1 
ATOM   6132 N N    . HIS   B 1 138 ? 34.408 -34.355 -1.203  1.00 13.84 ?  138 HIS   B N    1 
ATOM   6133 C CA   . HIS   B 1 138 ? 33.463 -33.385 -0.665  1.00 14.19 ?  138 HIS   B CA   1 
ATOM   6134 C C    . HIS   B 1 138 ? 33.882 -31.959 -0.990  1.00 13.53 ?  138 HIS   B C    1 
ATOM   6135 O O    . HIS   B 1 138 ? 33.035 -31.123 -1.326  1.00 13.96 ?  138 HIS   B O    1 
ATOM   6136 C CB   . HIS   B 1 138 ? 33.342 -33.558 0.841   1.00 15.77 ?  138 HIS   B CB   1 
ATOM   6137 C CG   . HIS   B 1 138 ? 32.416 -32.573 1.474   1.00 16.97 ?  138 HIS   B CG   1 
ATOM   6138 N ND1  . HIS   B 1 138 ? 31.075 -32.510 1.161   1.00 18.51 ?  138 HIS   B ND1  1 
ATOM   6139 C CD2  . HIS   B 1 138 ? 32.639 -31.588 2.374   1.00 17.45 ?  138 HIS   B CD2  1 
ATOM   6140 C CE1  . HIS   B 1 138 ? 30.509 -31.538 1.853   1.00 18.56 ?  138 HIS   B CE1  1 
ATOM   6141 N NE2  . HIS   B 1 138 ? 31.437 -30.963 2.598   1.00 18.28 ?  138 HIS   B NE2  1 
ATOM   6142 H H    . HIS   B 1 138 ? 34.846 -34.797 -0.612  1.00 16.58 ?  138 HIS   B H    1 
ATOM   6143 H HA   . HIS   B 1 138 ? 32.589 -33.543 -1.058  1.00 17.00 ?  138 HIS   B HA   1 
ATOM   6144 H HB2  . HIS   B 1 138 ? 32.997 -34.447 1.029   1.00 18.89 ?  138 HIS   B HB2  1 
ATOM   6145 H HB3  . HIS   B 1 138 ? 34.214 -33.449 1.243   1.00 18.89 ?  138 HIS   B HB3  1 
ATOM   6146 H HD1  . HIS   B 1 138 ? 30.669 -33.026 0.604   1.00 22.19 ?  138 HIS   B HD1  1 
ATOM   6147 H HD2  . HIS   B 1 138 ? 33.446 -31.376 2.777   1.00 20.92 ?  138 HIS   B HD2  1 
ATOM   6148 H HE1  . HIS   B 1 138 ? 29.605 -31.303 1.823   1.00 22.24 ?  138 HIS   B HE1  1 
ATOM   6149 N N    . SER   B 1 139 ? 35.175 -31.650 -0.890  1.00 12.93 ?  139 SER   B N    1 
ATOM   6150 C CA   . SER   B 1 139 ? 35.615 -30.299 -1.214  1.00 12.32 ?  139 SER   B CA   1 
ATOM   6151 C C    . SER   B 1 139 ? 35.278 -29.947 -2.656  1.00 11.58 ?  139 SER   B C    1 
ATOM   6152 O O    . SER   B 1 139 ? 34.832 -28.831 -2.936  1.00 11.78 ?  139 SER   B O    1 
ATOM   6153 C CB   . SER   B 1 139 ? 37.110 -30.163 -0.949  1.00 12.80 ?  139 SER   B CB   1 
ATOM   6154 O OG   . SER   B 1 139 ? 37.524 -28.831 -1.215  1.00 13.08 ?  139 SER   B OG   1 
ATOM   6155 H H    . SER   B 1 139 ? 35.794 -32.193 -0.649  1.00 15.49 ?  139 SER   B H    1 
ATOM   6156 H HA   . SER   B 1 139 ? 35.151 -29.674 -0.641  1.00 14.76 ?  139 SER   B HA   1 
ATOM   6157 H HB2  . SER   B 1 139 ? 37.290 -30.381 -0.019  1.00 15.33 ?  139 SER   B HB2  1 
ATOM   6158 H HB3  . SER   B 1 139 ? 37.596 -30.772 -1.531  1.00 15.33 ?  139 SER   B HB3  1 
ATOM   6159 H HG   . SER   B 1 139 ? 38.355 -28.760 -1.060  1.00 15.68 ?  139 SER   B HG   1 
ATOM   6160 N N    . LEU   B 1 140 ? 35.470 -30.887 -3.582  1.00 11.45 ?  140 LEU   B N    1 
ATOM   6161 C CA   . LEU   B 1 140 ? 35.111 -30.638 -4.972  1.00 11.43 ?  140 LEU   B CA   1 
ATOM   6162 C C    . LEU   B 1 140 ? 33.609 -30.405 -5.111  1.00 11.85 ?  140 LEU   B C    1 
ATOM   6163 O O    . LEU   B 1 140 ? 33.177 -29.524 -5.856  1.00 12.04 ?  140 LEU   B O    1 
ATOM   6164 C CB   . LEU   B 1 140 ? 35.581 -31.802 -5.844  1.00 12.03 ?  140 LEU   B CB   1 
ATOM   6165 C CG   . LEU   B 1 140 ? 35.224 -31.688 -7.319  1.00 12.14 ?  140 LEU   B CG   1 
ATOM   6166 C CD1  . LEU   B 1 140 ? 35.795 -30.413 -7.927  1.00 12.68 ?  140 LEU   B CD1  1 
ATOM   6167 C CD2  . LEU   B 1 140 ? 35.707 -32.917 -8.064  1.00 12.93 ?  140 LEU   B CD2  1 
ATOM   6168 H H    . LEU   B 1 140 ? 35.802 -31.666 -3.433  1.00 13.71 ?  140 LEU   B H    1 
ATOM   6169 H HA   . LEU   B 1 140 ? 35.569 -29.837 -5.277  1.00 13.70 ?  140 LEU   B HA   1 
ATOM   6170 H HB2  . LEU   B 1 140 ? 36.550 -31.865 -5.787  1.00 14.41 ?  140 LEU   B HB2  1 
ATOM   6171 H HB3  . LEU   B 1 140 ? 35.184 -32.622 -5.513  1.00 14.41 ?  140 LEU   B HB3  1 
ATOM   6172 H HG   . LEU   B 1 140 ? 34.257 -31.648 -7.408  1.00 14.54 ?  140 LEU   B HG   1 
ATOM   6173 H HD11 . LEU   B 1 140 ? 35.669 -30.436 -8.888  1.00 15.19 ?  140 LEU   B HD11 1 
ATOM   6174 H HD12 . LEU   B 1 140 ? 35.327 -29.645 -7.554  1.00 15.19 ?  140 LEU   B HD12 1 
ATOM   6175 H HD13 . LEU   B 1 140 ? 36.739 -30.357 -7.716  1.00 15.19 ?  140 LEU   B HD13 1 
ATOM   6176 H HD21 . LEU   B 1 140 ? 35.464 -32.829 -9.001  1.00 15.49 ?  140 LEU   B HD21 1 
ATOM   6177 H HD22 . LEU   B 1 140 ? 36.663 -32.986 -7.970  1.00 15.49 ?  140 LEU   B HD22 1 
ATOM   6178 H HD23 . LEU   B 1 140 ? 35.272 -33.699 -7.685  1.00 15.49 ?  140 LEU   B HD23 1 
ATOM   6179 N N    . ARG   B 1 141 ? 32.799 -31.193 -4.400  1.00 11.96 ?  141 ARG   B N    1 
ATOM   6180 C CA   . ARG   B 1 141 ? 31.352 -31.018 -4.408  1.00 12.97 ?  141 ARG   B CA   1 
ATOM   6181 C C    . ARG   B 1 141 ? 30.973 -29.612 -3.961  1.00 12.42 ?  141 ARG   B C    1 
ATOM   6182 O O    . ARG   B 1 141 ? 30.171 -28.928 -4.614  1.00 12.79 ?  141 ARG   B O    1 
ATOM   6183 C CB   . ARG   B 1 141 ? 30.749 -32.071 -3.472  1.00 15.22 ?  141 ARG   B CB   1 
ATOM   6184 C CG   . ARG   B 1 141 ? 29.286 -31.938 -3.123  1.00 18.07 ?  141 ARG   B CG   1 
ATOM   6185 C CD   . ARG   B 1 141 ? 28.421 -32.557 -4.156  1.00 20.56 ?  141 ARG   B CD   1 
ATOM   6186 N NE   . ARG   B 1 141 ? 28.161 -31.666 -5.278  1.00 21.72 ?  141 ARG   B NE   1 
ATOM   6187 C CZ   . ARG   B 1 141 ? 28.266 -32.007 -6.555  1.00 21.80 ?  141 ARG   B CZ   1 
ATOM   6188 N NH1  . ARG   B 1 141 ? 28.738 -33.188 -6.924  1.00 21.77 ?  141 ARG   B NH1  1 
ATOM   6189 N NH2  . ARG   B 1 141 ? 27.864 -31.146 -7.488  1.00 22.82 ?  141 ARG   B NH2  1 
ATOM   6190 H H    . ARG   B 1 141 ? 33.076 -31.839 -3.904  1.00 14.32 ?  141 ARG   B H    1 
ATOM   6191 H HA   . ARG   B 1 141 ? 31.010 -31.166 -5.302  1.00 15.54 ?  141 ARG   B HA   1 
ATOM   6192 H HB2  . ARG   B 1 141 ? 30.872 -32.948 -3.885  1.00 18.24 ?  141 ARG   B HB2  1 
ATOM   6193 H HB3  . ARG   B 1 141 ? 31.247 -32.055 -2.639  1.00 18.24 ?  141 ARG   B HB3  1 
ATOM   6194 H HG2  . ARG   B 1 141 ? 29.125 -32.381 -2.279  1.00 21.65 ?  141 ARG   B HG2  1 
ATOM   6195 H HG3  . ARG   B 1 141 ? 29.051 -30.995 -3.049  1.00 21.65 ?  141 ARG   B HG3  1 
ATOM   6196 H HD2  . ARG   B 1 141 ? 28.855 -33.364 -4.483  1.00 24.65 ?  141 ARG   B HD2  1 
ATOM   6197 H HD3  . ARG   B 1 141 ? 27.577 -32.789 -3.751  1.00 24.65 ?  141 ARG   B HD3  1 
ATOM   6198 H HE   . ARG   B 1 141 ? 27.896 -30.865 -5.095  1.00 26.04 ?  141 ARG   B HE   1 
ATOM   6199 H HH11 . ARG   B 1 141 ? 28.987 -33.760 -6.336  1.00 26.09 ?  141 ARG   B HH11 1 
ATOM   6200 H HH12 . ARG   B 1 141 ? 28.797 -33.377 -7.757  1.00 26.09 ?  141 ARG   B HH12 1 
ATOM   6201 H HH21 . ARG   B 1 141 ? 27.560 -30.371 -7.261  1.00 27.36 ?  141 ARG   B HH21 1 
ATOM   6202 H HH22 . ARG   B 1 141 ? 27.942 -31.346 -8.321  1.00 27.36 ?  141 ARG   B HH22 1 
ATOM   6203 N N    . VAL   B 1 142 ? 31.518 -29.177 -2.826  1.00 12.17 ?  142 VAL   B N    1 
ATOM   6204 C CA   . VAL   B 1 142 ? 31.191 -27.844 -2.336  1.00 12.08 ?  142 VAL   B CA   1 
ATOM   6205 C C    . VAL   B 1 142 ? 31.664 -26.784 -3.325  1.00 11.81 ?  142 VAL   B C    1 
ATOM   6206 O O    . VAL   B 1 142 ? 30.959 -25.800 -3.581  1.00 12.53 ?  142 VAL   B O    1 
ATOM   6207 C CB   . VAL   B 1 142 ? 31.735 -27.622 -0.912  1.00 12.67 ?  142 VAL   B CB   1 
ATOM   6208 C CG1  . VAL   B 1 142 ? 31.416 -26.196 -0.434  1.00 12.71 ?  142 VAL   B CG1  1 
ATOM   6209 C CG2  . VAL   B 1 142 ? 31.150 -28.641 0.048   1.00 13.45 ?  142 VAL   B CG2  1 
ATOM   6210 H H    . VAL   B 1 142 ? 32.070 -29.622 -2.333  1.00 14.57 ?  142 VAL   B H    1 
ATOM   6211 H HA   . VAL   B 1 142 ? 30.229 -27.773 -2.283  1.00 14.47 ?  142 VAL   B HA   1 
ATOM   6212 H HB   . VAL   B 1 142 ? 32.698 -27.727 -0.912  1.00 15.18 ?  142 VAL   B HB   1 
ATOM   6213 H HG11 . VAL   B 1 142 ? 31.597 -26.134 0.516   1.00 15.23 ?  142 VAL   B HG11 1 
ATOM   6214 H HG12 . VAL   B 1 142 ? 31.977 -25.568 -0.917  1.00 15.23 ?  142 VAL   B HG12 1 
ATOM   6215 H HG13 . VAL   B 1 142 ? 30.481 -26.008 -0.607  1.00 15.23 ?  142 VAL   B HG13 1 
ATOM   6216 H HG21 . VAL   B 1 142 ? 31.469 -28.453 0.944   1.00 16.11 ?  142 VAL   B HG21 1 
ATOM   6217 H HG22 . VAL   B 1 142 ? 30.182 -28.580 0.021   1.00 16.11 ?  142 VAL   B HG22 1 
ATOM   6218 H HG23 . VAL   B 1 142 ? 31.433 -29.527 -0.226  1.00 16.11 ?  142 VAL   B HG23 1 
ATOM   6219 N N    . CYS   B 1 143 ? 32.846 -26.979 -3.916  1.00 11.30 ?  143 CYS   B N    1 
ATOM   6220 C CA   . CYS   B 1 143 ? 33.340 -26.038 -4.917  1.00 11.53 ?  143 CYS   B CA   1 
ATOM   6221 C C    . CYS   B 1 143 ? 32.340 -25.886 -6.055  1.00 11.48 ?  143 CYS   B C    1 
ATOM   6222 O O    . CYS   B 1 143 ? 31.935 -24.773 -6.404  1.00 11.63 ?  143 CYS   B O    1 
ATOM   6223 C CB   . CYS   B 1 143 ? 34.691 -26.524 -5.454  1.00 12.04 ?  143 CYS   B CB   1 
ATOM   6224 S SG   . CYS   B 1 143 ? 35.454 -25.408 -6.651  1.00 12.27 ?  143 CYS   B SG   1 
ATOM   6225 H H    . CYS   B 1 143 ? 33.374 -27.640 -3.756  1.00 13.53 ?  143 CYS   B H    1 
ATOM   6226 H HA   . CYS   B 1 143 ? 33.473 -25.169 -4.506  1.00 13.81 ?  143 CYS   B HA   1 
ATOM   6227 H HB2  . CYS   B 1 143 ? 35.310 -26.628 -4.716  1.00 14.42 ?  143 CYS   B HB2  1 
ATOM   6228 H HB3  . CYS   B 1 143 ? 34.562 -27.382 -5.890  1.00 14.42 ?  143 CYS   B HB3  1 
ATOM   6229 H HG   . CYS   B 1 143 ? 36.514 -25.856 -6.994  1.00 14.70 ?  143 CYS   B HG   1 
ATOM   6230 N N    . VAL   B 1 144 ? 31.936 -27.003 -6.657  1.00 11.94 ?  144 VAL   B N    1 
ATOM   6231 C CA   . VAL   B 1 144 ? 31.031 -26.931 -7.801  1.00 13.07 ?  144 VAL   B CA   1 
ATOM   6232 C C    . VAL   B 1 144 ? 29.687 -26.324 -7.425  1.00 13.01 ?  144 VAL   B C    1 
ATOM   6233 O O    . VAL   B 1 144 ? 29.067 -25.619 -8.233  1.00 14.10 ?  144 VAL   B O    1 
ATOM   6234 C CB   . VAL   B 1 144 ? 30.877 -28.333 -8.406  1.00 15.93 ?  144 VAL   B CB   1 
ATOM   6235 C CG1  . VAL   B 1 144 ? 29.606 -28.447 -9.255  1.00 18.59 ?  144 VAL   B CG1  1 
ATOM   6236 C CG2  . VAL   B 1 144 ? 32.131 -28.712 -9.193  1.00 16.01 ?  144 VAL   B CG2  1 
ATOM   6237 H H    . VAL   B 1 144 ? 32.173 -27.798 -6.431  1.00 14.30 ?  144 VAL   B H    1 
ATOM   6238 H HA   . VAL   B 1 144 ? 31.427 -26.367 -8.480  1.00 15.66 ?  144 VAL   B HA   1 
ATOM   6239 H HB   . VAL   B 1 144 ? 30.791 -28.974 -7.682  1.00 19.09 ?  144 VAL   B HB   1 
ATOM   6240 H HG11 . VAL   B 1 144 ? 29.684 -29.224 -9.833  1.00 22.28 ?  144 VAL   B HG11 1 
ATOM   6241 H HG12 . VAL   B 1 144 ? 28.842 -28.552 -8.668  1.00 22.28 ?  144 VAL   B HG12 1 
ATOM   6242 H HG13 . VAL   B 1 144 ? 29.512 -27.647 -9.792  1.00 22.28 ?  144 VAL   B HG13 1 
ATOM   6243 H HG21 . VAL   B 1 144 ? 32.012 -29.603 -9.562  1.00 19.19 ?  144 VAL   B HG21 1 
ATOM   6244 H HG22 . VAL   B 1 144 ? 32.252 -28.071 -9.912  1.00 19.19 ?  144 VAL   B HG22 1 
ATOM   6245 H HG23 . VAL   B 1 144 ? 32.890 -28.695 -8.598  1.00 19.19 ?  144 VAL   B HG23 1 
ATOM   6246 N N    . ASP   B 1 145 ? 29.219 -26.568 -6.204  1.00 12.95 ?  145 ASP   B N    1 
ATOM   6247 C CA   . ASP   B 1 145 ? 27.910 -26.096 -5.775  1.00 13.35 ?  145 ASP   B CA   1 
ATOM   6248 C C    . ASP   B 1 145 ? 27.941 -24.674 -5.217  1.00 12.98 ?  145 ASP   B C    1 
ATOM   6249 O O    . ASP   B 1 145 ? 26.881 -24.127 -4.890  1.00 15.05 ?  145 ASP   B O    1 
ATOM   6250 C CB   . ASP   B 1 145 ? 27.332 -27.024 -4.700  1.00 15.17 ?  145 ASP   B CB   1 
ATOM   6251 C CG   . ASP   B 1 145 ? 26.952 -28.394 -5.227  1.00 17.19 ?  145 ASP   B CG   1 
ATOM   6252 O OD1  . ASP   B 1 145 ? 26.871 -28.580 -6.459  1.00 17.97 ?  145 ASP   B OD1  1 
ATOM   6253 O OD2  . ASP   B 1 145 ? 26.747 -29.288 -4.386  1.00 19.72 -1 145 ASP   B OD2  1 
ATOM   6254 H H    . ASP   B 1 145 ? 29.652 -26.998 -5.601  1.00 15.52 ?  145 ASP   B H    1 
ATOM   6255 H HA   . ASP   B 1 145 ? 27.311 -26.090 -6.537  1.00 16.00 ?  145 ASP   B HA   1 
ATOM   6256 H HB2  . ASP   B 1 145 ? 27.992 -27.148 -4.010  1.00 18.18 ?  145 ASP   B HB2  1 
ATOM   6257 H HB3  . ASP   B 1 145 ? 26.533 -26.612 -4.337  1.00 18.18 ?  145 ASP   B HB3  1 
ATOM   6258 N N    . THR   B 1 146 ? 29.120 -24.060 -5.093  1.00 11.61 ?  146 THR   B N    1 
ATOM   6259 C CA   . THR   B 1 146 ? 29.260 -22.743 -4.479  1.00 11.58 ?  146 THR   B CA   1 
ATOM   6260 C C    . THR   B 1 146 ? 29.891 -21.712 -5.396  1.00 11.12 ?  146 THR   B C    1 
ATOM   6261 O O    . THR   B 1 146 ? 29.438 -20.554 -5.435  1.00 11.71 ?  146 THR   B O    1 
ATOM   6262 C CB   . THR   B 1 146 ? 30.091 -22.853 -3.191  1.00 11.74 ?  146 THR   B CB   1 
ATOM   6263 O OG1  . THR   B 1 146 ? 29.518 -23.850 -2.334  1.00 12.05 ?  146 THR   B OG1  1 
ATOM   6264 C CG2  . THR   B 1 146 ? 30.155 -21.512 -2.463  1.00 11.96 ?  146 THR   B CG2  1 
ATOM   6265 H H    . THR   B 1 146 ? 29.875 -24.398 -5.360  1.00 13.91 ?  146 THR   B H    1 
ATOM   6266 H HA   . THR   B 1 146 ? 28.387 -22.422 -4.235  1.00 13.87 ?  146 THR   B HA   1 
ATOM   6267 H HB   . THR   B 1 146 ? 31.001 -23.109 -3.415  1.00 14.06 ?  146 THR   B HB   1 
ATOM   6268 H HG1  . THR   B 1 146 ? 29.553 -24.607 -2.714  1.00 14.43 ?  146 THR   B HG1  1 
ATOM   6269 H HG21 . THR   B 1 146 ? 30.521 -21.633 -1.573  1.00 14.33 ?  146 THR   B HG21 1 
ATOM   6270 H HG22 . THR   B 1 146 ? 30.727 -20.894 -2.952  1.00 14.33 ?  146 THR   B HG22 1 
ATOM   6271 H HG23 . THR   B 1 146 ? 29.268 -21.130 -2.391  1.00 14.33 ?  146 THR   B HG23 1 
ATOM   6272 N N    . VAL   B 1 147 ? 30.956 -22.082 -6.097  1.00 11.24 ?  147 VAL   B N    1 
ATOM   6273 C CA   . VAL   B 1 147 ? 31.679 -21.139 -6.934  1.00 11.00 ?  147 VAL   B CA   1 
ATOM   6274 C C    . VAL   B 1 147 ? 30.950 -21.004 -8.259  1.00 11.31 ?  147 VAL   B C    1 
ATOM   6275 O O    . VAL   B 1 147 ? 30.591 -22.009 -8.889  1.00 11.80 ?  147 VAL   B O    1 
ATOM   6276 C CB   . VAL   B 1 147 ? 33.130 -21.599 -7.141  1.00 11.33 ?  147 VAL   B CB   1 
ATOM   6277 C CG1  . VAL   B 1 147 ? 33.897 -20.582 -7.971  1.00 11.82 ?  147 VAL   B CG1  1 
ATOM   6278 C CG2  . VAL   B 1 147 ? 33.821 -21.812 -5.799  1.00 11.48 ?  147 VAL   B CG2  1 
ATOM   6279 H H    . VAL   B 1 147 ? 31.285 -22.880 -6.107  1.00 13.46 ?  147 VAL   B H    1 
ATOM   6280 H HA   . VAL   B 1 147 ? 31.697 -20.273 -6.504  1.00 13.18 ?  147 VAL   B HA   1 
ATOM   6281 H HB   . VAL   B 1 147 ? 33.137 -22.446 -7.617  1.00 13.57 ?  147 VAL   B HB   1 
ATOM   6282 H HG11 . VAL   B 1 147 ? 34.840 -20.807 -7.958  1.00 14.16 ?  147 VAL   B HG11 1 
ATOM   6283 H HG12 . VAL   B 1 147 ? 33.567 -20.604 -8.884  1.00 14.16 ?  147 VAL   B HG12 1 
ATOM   6284 H HG13 . VAL   B 1 147 ? 33.763 -19.700 -7.591  1.00 14.16 ?  147 VAL   B HG13 1 
ATOM   6285 H HG21 . VAL   B 1 147 ? 34.759 -22.018 -5.952  1.00 13.75 ?  147 VAL   B HG21 1 
ATOM   6286 H HG22 . VAL   B 1 147 ? 33.747 -20.998 -5.274  1.00 13.75 ?  147 VAL   B HG22 1 
ATOM   6287 H HG23 . VAL   B 1 147 ? 33.395 -22.546 -5.331  1.00 13.75 ?  147 VAL   B HG23 1 
ATOM   6288 N N    . ARG   B 1 148 ? 30.733 -19.754 -8.675  1.00 11.39 ?  148 ARG   B N    1 
ATOM   6289 C CA   . ARG   B 1 148 ? 30.110 -19.429 -9.949  1.00 11.40 ?  148 ARG   B CA   1 
ATOM   6290 C C    . ARG   B 1 148 ? 31.067 -18.757 -10.923 1.00 11.65 ?  148 ARG   B C    1 
ATOM   6291 O O    . ARG   B 1 148 ? 30.786 -18.741 -12.124 1.00 12.94 ?  148 ARG   B O    1 
ATOM   6292 C CB   . ARG   B 1 148 ? 28.879 -18.538 -9.725  1.00 12.33 ?  148 ARG   B CB   1 
ATOM   6293 C CG   . ARG   B 1 148 ? 27.803 -19.233 -8.908  1.00 12.94 ?  148 ARG   B CG   1 
ATOM   6294 C CD   . ARG   B 1 148 ? 26.602 -18.345 -8.602  1.00 13.68 ?  148 ARG   B CD   1 
ATOM   6295 N NE   . ARG   B 1 148 ? 26.984 -17.145 -7.870  1.00 13.33 ?  148 ARG   B NE   1 
ATOM   6296 C CZ   . ARG   B 1 148 ? 27.284 -17.114 -6.577  1.00 12.43 ?  148 ARG   B CZ   1 
ATOM   6297 N NH1  . ARG   B 1 148 ? 27.220 -18.201 -5.822  1.00 12.74 ?  148 ARG   B NH1  1 
ATOM   6298 N NH2  . ARG   B 1 148 ? 27.681 -15.966 -6.032  1.00 12.91 ?  148 ARG   B NH2  1 
ATOM   6299 H H    . ARG   B 1 148 ? 30.951 -19.058 -8.214  1.00 13.64 ?  148 ARG   B H    1 
ATOM   6300 H HA   . ARG   B 1 148 ? 29.806 -20.251 -10.359 1.00 13.66 ?  148 ARG   B HA   1 
ATOM   6301 H HB2  . ARG   B 1 148 ? 29.149 -17.737 -9.250  1.00 14.76 ?  148 ARG   B HB2  1 
ATOM   6302 H HB3  . ARG   B 1 148 ? 28.501 -18.303 -10.587 1.00 14.76 ?  148 ARG   B HB3  1 
ATOM   6303 H HG2  . ARG   B 1 148 ? 27.482 -20.005 -9.404  1.00 15.50 ?  148 ARG   B HG2  1 
ATOM   6304 H HG3  . ARG   B 1 148 ? 28.182 -19.519 -8.064  1.00 15.50 ?  148 ARG   B HG3  1 
ATOM   6305 H HD2  . ARG   B 1 148 ? 26.186 -18.070 -9.435  1.00 16.39 ?  148 ARG   B HD2  1 
ATOM   6306 H HD3  . ARG   B 1 148 ? 25.964 -18.843 -8.063  1.00 16.39 ?  148 ARG   B HD3  1 
ATOM   6307 H HE   . ARG   B 1 148 ? 27.021 -16.408 -8.303  1.00 15.97 ?  148 ARG   B HE   1 
ATOM   6308 H HH11 . ARG   B 1 148 ? 26.964 -18.952 -6.158  1.00 15.27 ?  148 ARG   B HH11 1 
ATOM   6309 H HH12 . ARG   B 1 148 ? 27.415 -18.157 -4.983  1.00 15.27 ?  148 ARG   B HH12 1 
ATOM   6310 H HH21 . ARG   B 1 148 ? 27.729 -15.256 -6.515  1.00 15.46 ?  148 ARG   B HH21 1 
ATOM   6311 H HH22 . ARG   B 1 148 ? 27.877 -15.930 -5.196  1.00 15.46 ?  148 ARG   B HH22 1 
ATOM   6312 N N    . THR   B 1 149 ? 32.176 -18.208 -10.436 1.00 11.44 ?  149 THR   B N    1 
ATOM   6313 C CA   . THR   B 1 149 ? 33.219 -17.649 -11.282 1.00 11.57 ?  149 THR   B CA   1 
ATOM   6314 C C    . THR   B 1 149 ? 34.108 -18.789 -11.788 1.00 11.42 ?  149 THR   B C    1 
ATOM   6315 O O    . THR   B 1 149 ? 33.921 -19.959 -11.441 1.00 11.53 ?  149 THR   B O    1 
ATOM   6316 C CB   . THR   B 1 149 ? 33.985 -16.588 -10.501 1.00 11.85 ?  149 THR   B CB   1 
ATOM   6317 O OG1  . THR   B 1 149 ? 34.444 -17.183 -9.286  1.00 11.78 ?  149 THR   B OG1  1 
ATOM   6318 C CG2  . THR   B 1 149 ? 33.084 -15.380 -10.212 1.00 12.15 ?  149 THR   B CG2  1 
ATOM   6319 H H    . THR   B 1 149 ? 32.339 -18.134 -9.594  1.00 13.71 ?  149 THR   B H    1 
ATOM   6320 H HA   . THR   B 1 149 ? 32.808 -17.219 -12.048 1.00 13.86 ?  149 THR   B HA   1 
ATOM   6321 H HB   . THR   B 1 149 ? 34.745 -16.295 -11.019 1.00 14.20 ?  149 THR   B HB   1 
ATOM   6322 H HG1  . THR   B 1 149 ? 34.856 -16.605 -8.822  1.00 14.11 ?  149 THR   B HG1  1 
ATOM   6323 H HG21 . THR   B 1 149 ? 33.587 -14.704 -9.731  1.00 14.55 ?  149 THR   B HG21 1 
ATOM   6324 H HG22 . THR   B 1 149 ? 32.767 -14.998 -11.047 1.00 14.55 ?  149 THR   B HG22 1 
ATOM   6325 H HG23 . THR   B 1 149 ? 32.323 -15.649 -9.679  1.00 14.55 ?  149 THR   B HG23 1 
ATOM   6326 N N    . ASN   B 1 150 ? 35.067 -18.470 -12.646 1.00 11.51 ?  150 ASN   B N    1 
ATOM   6327 C CA   . ASN   B 1 150 ? 35.834 -19.500 -13.337 1.00 11.92 ?  150 ASN   B CA   1 
ATOM   6328 C C    . ASN   B 1 150 ? 36.999 -19.946 -12.465 1.00 11.55 ?  150 ASN   B C    1 
ATOM   6329 O O    . ASN   B 1 150 ? 37.922 -19.171 -12.202 1.00 12.45 ?  150 ASN   B O    1 
ATOM   6330 C CB   . ASN   B 1 150 ? 36.306 -18.983 -14.688 1.00 13.76 ?  150 ASN   B CB   1 
ATOM   6331 C CG   . ASN   B 1 150 ? 35.158 -18.750 -15.626 1.00 16.25 ?  150 ASN   B CG   1 
ATOM   6332 O OD1  . ASN   B 1 150 ? 34.269 -19.588 -15.730 1.00 17.35 ?  150 ASN   B OD1  1 
ATOM   6333 N ND2  . ASN   B 1 150 ? 35.140 -17.598 -16.280 1.00 17.94 ?  150 ASN   B ND2  1 
ATOM   6334 H H    . ASN   B 1 150 ? 35.303 -17.663 -12.839 1.00 13.78 ?  150 ASN   B H    1 
ATOM   6335 H HA   . ASN   B 1 150 ? 35.258 -20.266 -13.493 1.00 14.28 ?  150 ASN   B HA   1 
ATOM   6336 H HB2  . ASN   B 1 150 ? 36.769 -18.142 -14.565 1.00 16.48 ?  150 ASN   B HB2  1 
ATOM   6337 H HB3  . ASN   B 1 150 ? 36.896 -19.637 -15.091 1.00 16.48 ?  150 ASN   B HB3  1 
ATOM   6338 H HD21 . ASN   B 1 150 ? 34.499 -17.415 -16.830 1.00 21.51 ?  150 ASN   B HD21 1 
ATOM   6339 H HD22 . ASN   B 1 150 ? 35.777 -17.029 -16.170 1.00 21.51 ?  150 ASN   B HD22 1 
ATOM   6340 N N    . VAL   B 1 151 ? 36.962 -21.197 -12.020 1.00 11.15 ?  151 VAL   B N    1 
ATOM   6341 C CA   . VAL   B 1 151 ? 37.983 -21.725 -11.130 1.00 11.29 ?  151 VAL   B CA   1 
ATOM   6342 C C    . VAL   B 1 151 ? 38.691 -22.898 -11.798 1.00 11.06 ?  151 VAL   B C    1 
ATOM   6343 O O    . VAL   B 1 151 ? 38.053 -23.834 -12.299 1.00 12.17 ?  151 VAL   B O    1 
ATOM   6344 C CB   . VAL   B 1 151 ? 37.422 -22.046 -9.731  1.00 12.46 ?  151 VAL   B CB   1 
ATOM   6345 C CG1  . VAL   B 1 151 ? 36.267 -23.045 -9.803  1.00 13.20 ?  151 VAL   B CG1  1 
ATOM   6346 C CG2  . VAL   B 1 151 ? 38.531 -22.521 -8.808  1.00 13.19 ?  151 VAL   B CG2  1 
ATOM   6347 H H    . VAL   B 1 151 ? 36.342 -21.762 -12.222 1.00 13.36 ?  151 VAL   B H    1 
ATOM   6348 H HA   . VAL   B 1 151 ? 38.648 -21.026 -11.005 1.00 13.53 ?  151 VAL   B HA   1 
ATOM   6349 H HB   . VAL   B 1 151 ? 37.068 -21.225 -9.351  1.00 14.93 ?  151 VAL   B HB   1 
ATOM   6350 H HG11 . VAL   B 1 151 ? 35.951 -23.230 -8.904  1.00 15.82 ?  151 VAL   B HG11 1 
ATOM   6351 H HG12 . VAL   B 1 151 ? 35.548 -22.666 -10.333 1.00 15.82 ?  151 VAL   B HG12 1 
ATOM   6352 H HG13 . VAL   B 1 151 ? 36.582 -23.867 -10.215 1.00 15.82 ?  151 VAL   B HG13 1 
ATOM   6353 H HG21 . VAL   B 1 151 ? 38.180 -22.599 -7.906  1.00 15.81 ?  151 VAL   B HG21 1 
ATOM   6354 H HG22 . VAL   B 1 151 ? 38.854 -23.383 -9.112  1.00 15.81 ?  151 VAL   B HG22 1 
ATOM   6355 H HG23 . VAL   B 1 151 ? 39.257 -21.873 -8.821  1.00 15.81 ?  151 VAL   B HG23 1 
ATOM   6356 N N    . TYR   B 1 152 ? 40.020 -22.802 -11.823 1.00 10.63 ?  152 TYR   B N    1 
ATOM   6357 C CA   . TYR   B 1 152 ? 40.929 -23.782 -12.402 1.00 10.88 ?  152 TYR   B CA   1 
ATOM   6358 C C    . TYR   B 1 152 ? 41.649 -24.457 -11.241 1.00 10.46 ?  152 TYR   B C    1 
ATOM   6359 O O    . TYR   B 1 152 ? 42.492 -23.843 -10.582 1.00 10.88 ?  152 TYR   B O    1 
ATOM   6360 C CB   . TYR   B 1 152 ? 41.898 -23.075 -13.352 1.00 11.51 ?  152 TYR   B CB   1 
ATOM   6361 C CG   . TYR   B 1 152 ? 41.214 -22.616 -14.616 1.00 12.38 ?  152 TYR   B CG   1 
ATOM   6362 C CD1  . TYR   B 1 152 ? 40.545 -21.398 -14.675 1.00 12.88 ?  152 TYR   B CD1  1 
ATOM   6363 C CD2  . TYR   B 1 152 ? 41.214 -23.420 -15.745 1.00 13.17 ?  152 TYR   B CD2  1 
ATOM   6364 C CE1  . TYR   B 1 152 ? 39.904 -20.997 -15.829 1.00 13.97 ?  152 TYR   B CE1  1 
ATOM   6365 C CE2  . TYR   B 1 152 ? 40.581 -23.034 -16.898 1.00 14.63 ?  152 TYR   B CE2  1 
ATOM   6366 C CZ   . TYR   B 1 152 ? 39.927 -21.820 -16.941 1.00 14.50 ?  152 TYR   B CZ   1 
ATOM   6367 O OH   . TYR   B 1 152 ? 39.291 -21.440 -18.098 1.00 16.47 ?  152 TYR   B OH   1 
ATOM   6368 H H    . TYR   B 1 152 ? 40.447 -22.127 -11.483 1.00 12.73 ?  152 TYR   B H    1 
ATOM   6369 H HA   . TYR   B 1 152 ? 40.424 -24.448 -12.895 1.00 13.03 ?  152 TYR   B HA   1 
ATOM   6370 H HB2  . TYR   B 1 152 ? 42.269 -22.297 -12.903 1.00 13.78 ?  152 TYR   B HB2  1 
ATOM   6371 H HB3  . TYR   B 1 152 ? 42.612 -23.688 -13.591 1.00 13.78 ?  152 TYR   B HB3  1 
ATOM   6372 H HD1  . TYR   B 1 152 ? 40.529 -20.847 -13.925 1.00 15.43 ?  152 TYR   B HD1  1 
ATOM   6373 H HD2  . TYR   B 1 152 ? 41.654 -24.245 -15.715 1.00 15.78 ?  152 TYR   B HD2  1 
ATOM   6374 H HE1  . TYR   B 1 152 ? 39.462 -20.180 -15.864 1.00 16.74 ?  152 TYR   B HE1  1 
ATOM   6375 H HE2  . TYR   B 1 152 ? 40.596 -23.587 -17.643 1.00 17.53 ?  152 TYR   B HE2  1 
ATOM   6376 H HH   . TYR   B 1 152 ? 38.936 -20.685 -17.988 1.00 19.74 ?  152 TYR   B HH   1 
ATOM   6377 N N    . LEU   B 1 153 ? 41.287 -25.715 -10.976 1.00 10.60 ?  153 LEU   B N    1 
ATOM   6378 C CA   . LEU   B 1 153 ? 41.788 -26.466 -9.831  1.00 10.37 ?  153 LEU   B CA   1 
ATOM   6379 C C    . LEU   B 1 153 ? 43.020 -27.271 -10.219 1.00 10.74 ?  153 LEU   B C    1 
ATOM   6380 O O    . LEU   B 1 153 ? 43.001 -28.009 -11.208 1.00 11.96 ?  153 LEU   B O    1 
ATOM   6381 C CB   . LEU   B 1 153 ? 40.710 -27.420 -9.315  1.00 10.79 ?  153 LEU   B CB   1 
ATOM   6382 C CG   . LEU   B 1 153 ? 39.448 -26.768 -8.755  1.00 11.50 ?  153 LEU   B CG   1 
ATOM   6383 C CD1  . LEU   B 1 153 ? 38.359 -27.820 -8.615  1.00 12.35 ?  153 LEU   B CD1  1 
ATOM   6384 C CD2  . LEU   B 1 153 ? 39.722 -26.102 -7.417  1.00 11.91 ?  153 LEU   B CD2  1 
ATOM   6385 H H    . LEU   B 1 153 ? 40.728 -26.167 -11.458 1.00 12.69 ?  153 LEU   B H    1 
ATOM   6386 H HA   . LEU   B 1 153 ? 42.019 -25.848 -9.121  1.00 12.42 ?  153 LEU   B HA   1 
ATOM   6387 H HB2  . LEU   B 1 153 ? 40.440 -28.001 -10.042 1.00 12.92 ?  153 LEU   B HB2  1 
ATOM   6388 H HB3  . LEU   B 1 153 ? 41.097 -27.959 -8.602  1.00 12.92 ?  153 LEU   B HB3  1 
ATOM   6389 H HG   . LEU   B 1 153 ? 39.137 -26.088 -9.374  1.00 13.78 ?  153 LEU   B HG   1 
ATOM   6390 H HD11 . LEU   B 1 153 ? 37.556 -27.393 -8.283  1.00 14.80 ?  153 LEU   B HD11 1 
ATOM   6391 H HD12 . LEU   B 1 153 ? 38.194 -28.211 -9.485  1.00 14.80 ?  153 LEU   B HD12 1 
ATOM   6392 H HD13 . LEU   B 1 153 ? 38.661 -28.497 -7.994  1.00 14.80 ?  153 LEU   B HD13 1 
ATOM   6393 H HD21 . LEU   B 1 153 ? 38.901 -25.723 -7.074  1.00 14.27 ?  153 LEU   B HD21 1 
ATOM   6394 H HD22 . LEU   B 1 153 ? 40.065 -26.768 -6.798  1.00 14.27 ?  153 LEU   B HD22 1 
ATOM   6395 H HD23 . LEU   B 1 153 ? 40.385 -25.402 -7.543  1.00 14.27 ?  153 LEU   B HD23 1 
ATOM   6396 N N    . ALA   B 1 154 ? 44.073 -27.159 -9.416  1.00 10.64 ?  154 ALA   B N    1 
ATOM   6397 C CA   . ALA   B 1 154 ? 45.300 -27.920 -9.599  1.00 11.56 ?  154 ALA   B CA   1 
ATOM   6398 C C    . ALA   B 1 154 ? 45.369 -28.996 -8.524  1.00 11.94 ?  154 ALA   B C    1 
ATOM   6399 O O    . ALA   B 1 154 ? 45.284 -28.699 -7.327  1.00 13.37 ?  154 ALA   B O    1 
ATOM   6400 C CB   . ALA   B 1 154 ? 46.514 -26.998 -9.537  1.00 12.90 ?  154 ALA   B CB   1 
ATOM   6401 H H    . ALA   B 1 154 ? 44.094 -26.631 -8.732  1.00 12.74 ?  154 ALA   B H    1 
ATOM   6402 H HA   . ALA   B 1 154 ? 45.286 -28.350 -10.464 1.00 13.84 ?  154 ALA   B HA   1 
ATOM   6403 H HB1  . ALA   B 1 154 ? 47.318 -27.525 -9.660  1.00 15.45 ?  154 ALA   B HB1  1 
ATOM   6404 H HB2  . ALA   B 1 154 ? 46.443 -26.332 -10.240 1.00 15.45 ?  154 ALA   B HB2  1 
ATOM   6405 H HB3  . ALA   B 1 154 ? 46.537 -26.558 -8.670  1.00 15.45 ?  154 ALA   B HB3  1 
ATOM   6406 N N    . VAL   B 1 155 ? 45.497 -30.243 -8.957  1.00 11.30 ?  155 VAL   B N    1 
ATOM   6407 C CA   . VAL   B 1 155 ? 45.597 -31.393 -8.068  1.00 11.48 ?  155 VAL   B CA   1 
ATOM   6408 C C    . VAL   B 1 155 ? 46.941 -32.066 -8.334  1.00 11.48 ?  155 VAL   B C    1 
ATOM   6409 O O    . VAL   B 1 155 ? 47.182 -32.563 -9.442  1.00 13.03 ?  155 VAL   B O    1 
ATOM   6410 C CB   . VAL   B 1 155 ? 44.438 -32.385 -8.279  1.00 13.13 ?  155 VAL   B CB   1 
ATOM   6411 C CG1  . VAL   B 1 155 ? 44.616 -33.597 -7.379  1.00 13.01 ?  155 VAL   B CG1  1 
ATOM   6412 C CG2  . VAL   B 1 155 ? 43.094 -31.702 -8.013  1.00 14.07 ?  155 VAL   B CG2  1 
ATOM   6413 H H    . VAL   B 1 155 ? 45.532 -30.455 -9.790  1.00 13.53 ?  155 VAL   B H    1 
ATOM   6414 H HA   . VAL   B 1 155 ? 45.578 -31.101 -7.147  1.00 13.75 ?  155 VAL   B HA   1 
ATOM   6415 H HB   . VAL   B 1 155 ? 44.442 -32.693 -9.201  1.00 15.73 ?  155 VAL   B HB   1 
ATOM   6416 H HG11 . VAL   B 1 155 ? 43.784 -34.097 -7.353  1.00 15.58 ?  155 VAL   B HG11 1 
ATOM   6417 H HG12 . VAL   B 1 155 ? 45.323 -34.160 -7.735  1.00 15.58 ?  155 VAL   B HG12 1 
ATOM   6418 H HG13 . VAL   B 1 155 ? 44.847 -33.298 -6.487  1.00 15.58 ?  155 VAL   B HG13 1 
ATOM   6419 H HG21 . VAL   B 1 155 ? 42.380 -32.350 -8.118  1.00 16.86 ?  155 VAL   B HG21 1 
ATOM   6420 H HG22 . VAL   B 1 155 ? 43.092 -31.353 -7.106  1.00 16.86 ?  155 VAL   B HG22 1 
ATOM   6421 H HG23 . VAL   B 1 155 ? 42.977 -30.976 -8.645  1.00 16.86 ?  155 VAL   B HG23 1 
ATOM   6422 N N    . PHE   B 1 156 ? 47.802 -32.104 -7.311  1.00 11.77 ?  156 PHE   B N    1 
ATOM   6423 C CA   . PHE   B 1 156 ? 49.180 -32.562 -7.500  1.00 13.05 ?  156 PHE   B CA   1 
ATOM   6424 C C    . PHE   B 1 156 ? 49.280 -34.063 -7.788  1.00 13.85 ?  156 PHE   B C    1 
ATOM   6425 O O    . PHE   B 1 156 ? 50.025 -34.488 -8.684  1.00 15.38 ?  156 PHE   B O    1 
ATOM   6426 C CB   . PHE   B 1 156 ? 49.997 -32.203 -6.261  1.00 13.48 ?  156 PHE   B CB   1 
ATOM   6427 C CG   . PHE   B 1 156 ? 51.419 -32.659 -6.317  1.00 13.96 ?  156 PHE   B CG   1 
ATOM   6428 C CD1  . PHE   B 1 156 ? 52.307 -32.104 -7.219  1.00 15.90 ?  156 PHE   B CD1  1 
ATOM   6429 C CD2  . PHE   B 1 156 ? 51.873 -33.634 -5.455  1.00 14.40 ?  156 PHE   B CD2  1 
ATOM   6430 C CE1  . PHE   B 1 156 ? 53.631 -32.514 -7.264  1.00 16.99 ?  156 PHE   B CE1  1 
ATOM   6431 C CE2  . PHE   B 1 156 ? 53.193 -34.053 -5.496  1.00 15.90 ?  156 PHE   B CE2  1 
ATOM   6432 C CZ   . PHE   B 1 156 ? 54.068 -33.492 -6.405  1.00 16.53 ?  156 PHE   B CZ   1 
ATOM   6433 H H    . PHE   B 1 156 ? 47.607 -31.867 -6.504  1.00 14.10 ?  156 PHE   B H    1 
ATOM   6434 H HA   . PHE   B 1 156 ? 49.560 -32.084 -8.251  1.00 15.63 ?  156 PHE   B HA   1 
ATOM   6435 H HB2  . PHE   B 1 156 ? 50.001 -31.237 -6.158  1.00 16.15 ?  156 PHE   B HB2  1 
ATOM   6436 H HB3  . PHE   B 1 156 ? 49.584 -32.611 -5.483  1.00 16.15 ?  156 PHE   B HB3  1 
ATOM   6437 H HD1  . PHE   B 1 156 ? 52.012 -31.439 -7.802  1.00 19.06 ?  156 PHE   B HD1  1 
ATOM   6438 H HD2  . PHE   B 1 156 ? 51.284 -34.018 -4.843  1.00 17.25 ?  156 PHE   B HD2  1 
ATOM   6439 H HE1  . PHE   B 1 156 ? 54.214 -32.131 -7.881  1.00 20.36 ?  156 PHE   B HE1  1 
ATOM   6440 H HE2  . PHE   B 1 156 ? 53.486 -34.717 -4.915  1.00 19.06 ?  156 PHE   B HE2  1 
ATOM   6441 H HZ   . PHE   B 1 156 ? 54.953 -33.774 -6.435  1.00 19.82 ?  156 PHE   B HZ   1 
ATOM   6442 N N    . ASP   B 1 157 ? 48.604 -34.886 -6.999  1.00 13.99 ?  157 ASP   B N    1 
ATOM   6443 C CA   . ASP   B 1 157 ? 48.755 -36.334 -7.098  1.00 15.22 ?  157 ASP   B CA   1 
ATOM   6444 C C    . ASP   B 1 157 ? 47.843 -36.872 -8.193  1.00 15.09 ?  157 ASP   B C    1 
ATOM   6445 O O    . ASP   B 1 157 ? 46.618 -36.756 -8.094  1.00 14.63 ?  157 ASP   B O    1 
ATOM   6446 C CB   . ASP   B 1 157 ? 48.396 -36.947 -5.752  1.00 16.73 ?  157 ASP   B CB   1 
ATOM   6447 C CG   . ASP   B 1 157 ? 48.524 -38.459 -5.732  1.00 18.64 ?  157 ASP   B CG   1 
ATOM   6448 O OD1  . ASP   B 1 157 ? 48.859 -39.069 -6.773  1.00 19.22 ?  157 ASP   B OD1  1 
ATOM   6449 O OD2  . ASP   B 1 157 ? 48.296 -39.041 -4.651  1.00 20.97 -1 157 ASP   B OD2  1 
ATOM   6450 H H    . ASP   B 1 157 ? 48.052 -34.629 -6.394  1.00 16.76 ?  157 ASP   B H    1 
ATOM   6451 H HA   . ASP   B 1 157 ? 49.673 -36.557 -7.317  1.00 18.24 ?  157 ASP   B HA   1 
ATOM   6452 H HB2  . ASP   B 1 157 ? 48.983 -36.582 -5.078  1.00 20.06 ?  157 ASP   B HB2  1 
ATOM   6453 H HB3  . ASP   B 1 157 ? 47.473 -36.725 -5.545  1.00 20.06 ?  157 ASP   B HB3  1 
ATOM   6454 N N    . LYS   B 1 158 ? 48.441 -37.487 -9.221  1.00 16.11 ?  158 LYS   B N    1 
ATOM   6455 C CA   . LYS   B 1 158 ? 47.670 -38.112 -10.300 1.00 17.12 ?  158 LYS   B CA   1 
ATOM   6456 C C    . LYS   B 1 158 ? 46.610 -39.076 -9.769  1.00 16.83 ?  158 LYS   B C    1 
ATOM   6457 O O    . LYS   B 1 158 ? 45.506 -39.164 -10.321 1.00 17.27 ?  158 LYS   B O    1 
ATOM   6458 C CB   . LYS   B 1 158 ? 48.625 -38.836 -11.259 1.00 19.09 ?  158 LYS   B CB   1 
ATOM   6459 C CG   . LYS   B 1 158 ? 47.952 -39.711 -12.312 1.00 21.70 ?  158 LYS   B CG   1 
ATOM   6460 C CD   . LYS   B 1 158 ? 47.102 -38.903 -13.268 1.00 24.26 ?  158 LYS   B CD   1 
ATOM   6461 C CE   . LYS   B 1 158 ? 46.495 -39.793 -14.339 1.00 26.37 ?  158 LYS   B CE   1 
ATOM   6462 N NZ   . LYS   B 1 158 ? 45.450 -39.086 -15.134 1.00 26.61 ?  158 LYS   B NZ   1 
ATOM   6463 H H    . LYS   B 1 158 ? 49.295 -37.557 -9.317  1.00 19.31 ?  158 LYS   B H    1 
ATOM   6464 H HA   . LYS   B 1 158 ? 47.220 -37.420 -10.808 1.00 20.52 ?  158 LYS   B HA   1 
ATOM   6465 H HB2  . LYS   B 1 158 ? 49.154 -38.173 -11.735 1.00 22.88 ?  158 LYS   B HB2  1 
ATOM   6466 H HB3  . LYS   B 1 158 ? 49.215 -39.407 -10.742 1.00 22.88 ?  158 LYS   B HB3  1 
ATOM   6467 H HG2  . LYS   B 1 158 ? 48.640 -40.161 -12.833 1.00 26.02 ?  158 LYS   B HG2  1 
ATOM   6468 H HG3  . LYS   B 1 158 ? 47.389 -40.375 -11.882 1.00 26.02 ?  158 LYS   B HG3  1 
ATOM   6469 H HD2  . LYS   B 1 158 ? 46.381 -38.478 -12.778 1.00 29.08 ?  158 LYS   B HD2  1 
ATOM   6470 H HD3  . LYS   B 1 158 ? 47.654 -38.235 -13.705 1.00 29.08 ?  158 LYS   B HD3  1 
ATOM   6471 H HE2  . LYS   B 1 158 ? 47.191 -40.082 -14.947 1.00 31.62 ?  158 LYS   B HE2  1 
ATOM   6472 H HE3  . LYS   B 1 158 ? 46.081 -40.563 -13.917 1.00 31.62 ?  158 LYS   B HE3  1 
ATOM   6473 H HZ1  . LYS   B 1 158 ? 45.114 -39.632 -15.750 1.00 31.90 ?  158 LYS   B HZ1  1 
ATOM   6474 H HZ2  . LYS   B 1 158 ? 44.793 -38.813 -14.599 1.00 31.90 ?  158 LYS   B HZ2  1 
ATOM   6475 H HZ3  . LYS   B 1 158 ? 45.806 -38.377 -15.539 1.00 31.90 ?  158 LYS   B HZ3  1 
ATOM   6476 N N    . ASN   B 1 159 ? 46.930 -39.833 -8.719  1.00 17.03 ?  159 ASN   B N    1 
ATOM   6477 C CA   . ASN   B 1 159 ? 45.971 -40.814 -8.221  1.00 17.46 ?  159 ASN   B CA   1 
ATOM   6478 C C    . ASN   B 1 159 ? 44.773 -40.145 -7.551  1.00 16.70 ?  159 ASN   B C    1 
ATOM   6479 O O    . ASN   B 1 159 ? 43.642 -40.632 -7.677  1.00 17.00 ?  159 ASN   B O    1 
ATOM   6480 C CB   . ASN   B 1 159 ? 46.666 -41.801 -7.290  1.00 19.21 ?  159 ASN   B CB   1 
ATOM   6481 C CG   . ASN   B 1 159 ? 47.704 -42.635 -8.010  1.00 21.39 ?  159 ASN   B CG   1 
ATOM   6482 O OD1  . ASN   B 1 159 ? 47.457 -43.133 -9.112  1.00 22.41 ?  159 ASN   B OD1  1 
ATOM   6483 N ND2  . ASN   B 1 159 ? 48.871 -42.786 -7.400  1.00 22.24 ?  159 ASN   B ND2  1 
ATOM   6484 H H    . ASN   B 1 159 ? 47.673 -39.793 -8.292  1.00 20.41 ?  159 ASN   B H    1 
ATOM   6485 H HA   . ASN   B 1 159 ? 45.634 -41.316 -8.979  1.00 20.93 ?  159 ASN   B HA   1 
ATOM   6486 H HB2  . ASN   B 1 159 ? 47.111 -41.316 -6.583  1.00 23.03 ?  159 ASN   B HB2  1 
ATOM   6487 H HB3  . ASN   B 1 159 ? 46.003 -42.405 -6.921  1.00 23.03 ?  159 ASN   B HB3  1 
ATOM   6488 H HD21 . ASN   B 1 159 ? 49.495 -43.255 -7.769  1.00 26.66 ?  159 ASN   B HD21 1 
ATOM   6489 H HD22 . ASN   B 1 159 ? 49.004 -42.433 -6.628  1.00 26.66 ?  159 ASN   B HD22 1 
ATOM   6490 N N    . LEU   B 1 160 ? 44.983 -39.010 -6.872  1.00 15.77 ?  160 LEU   B N    1 
ATOM   6491 C CA   . LEU   B 1 160 ? 43.846 -38.275 -6.329  1.00 14.74 ?  160 LEU   B CA   1 
ATOM   6492 C C    . LEU   B 1 160 ? 43.056 -37.606 -7.444  1.00 13.95 ?  160 LEU   B C    1 
ATOM   6493 O O    . LEU   B 1 160 ? 41.817 -37.608 -7.431  1.00 13.76 ?  160 LEU   B O    1 
ATOM   6494 C CB   . LEU   B 1 160 ? 44.306 -37.237 -5.303  1.00 14.32 ?  160 LEU   B CB   1 
ATOM   6495 C CG   . LEU   B 1 160 ? 43.184 -36.343 -4.756  1.00 14.22 ?  160 LEU   B CG   1 
ATOM   6496 C CD1  . LEU   B 1 160 ? 42.059 -37.166 -4.135  1.00 14.94 ?  160 LEU   B CD1  1 
ATOM   6497 C CD2  . LEU   B 1 160 ? 43.730 -35.352 -3.740  1.00 14.71 ?  160 LEU   B CD2  1 
ATOM   6498 H H    . LEU   B 1 160 ? 45.756 -38.655 -6.720  1.00 18.90 ?  160 LEU   B H    1 
ATOM   6499 H HA   . LEU   B 1 160 ? 43.260 -38.897 -5.881  1.00 17.67 ?  160 LEU   B HA   1 
ATOM   6500 H HB2  . LEU   B 1 160 ? 44.709 -37.699 -4.549  1.00 17.16 ?  160 LEU   B HB2  1 
ATOM   6501 H HB3  . LEU   B 1 160 ? 44.970 -36.657 -5.716  1.00 17.16 ?  160 LEU   B HB3  1 
ATOM   6502 H HG   . LEU   B 1 160 ? 42.807 -35.829 -5.486  1.00 17.04 ?  160 LEU   B HG   1 
ATOM   6503 H HD11 . LEU   B 1 160 ? 41.424 -36.569 -3.717  1.00 17.91 ?  160 LEU   B HD11 1 
ATOM   6504 H HD12 . LEU   B 1 160 ? 41.622 -37.682 -4.831  1.00 17.91 ?  160 LEU   B HD12 1 
ATOM   6505 H HD13 . LEU   B 1 160 ? 42.438 -37.766 -3.470  1.00 17.91 ?  160 LEU   B HD13 1 
ATOM   6506 H HD21 . LEU   B 1 160 ? 43.009 -34.778 -3.438  1.00 17.62 ?  160 LEU   B HD21 1 
ATOM   6507 H HD22 . LEU   B 1 160 ? 44.101 -35.841 -2.988  1.00 17.62 ?  160 LEU   B HD22 1 
ATOM   6508 H HD23 . LEU   B 1 160 ? 44.424 -34.817 -4.159  1.00 17.62 ?  160 LEU   B HD23 1 
ATOM   6509 N N    . TYR   B 1 161 ? 43.760 -37.032 -8.421  1.00 14.10 ?  161 TYR   B N    1 
ATOM   6510 C CA   . TYR   B 1 161 ? 43.089 -36.466 -9.583  1.00 14.22 ?  161 TYR   B CA   1 
ATOM   6511 C C    . TYR   B 1 161 ? 42.153 -37.490 -10.214 1.00 14.15 ?  161 TYR   B C    1 
ATOM   6512 O O    . TYR   B 1 161 ? 40.983 -37.194 -10.483 1.00 13.96 ?  161 TYR   B O    1 
ATOM   6513 C CB   . TYR   B 1 161 ? 44.132 -35.974 -10.591 1.00 14.73 ?  161 TYR   B CB   1 
ATOM   6514 C CG   . TYR   B 1 161 ? 43.563 -35.517 -11.908 1.00 15.33 ?  161 TYR   B CG   1 
ATOM   6515 C CD1  . TYR   B 1 161 ? 43.170 -34.201 -12.086 1.00 15.37 ?  161 TYR   B CD1  1 
ATOM   6516 C CD2  . TYR   B 1 161 ? 43.402 -36.399 -12.972 1.00 16.25 ?  161 TYR   B CD2  1 
ATOM   6517 C CE1  . TYR   B 1 161 ? 42.646 -33.771 -13.280 1.00 16.34 ?  161 TYR   B CE1  1 
ATOM   6518 C CE2  . TYR   B 1 161 ? 42.872 -35.976 -14.171 1.00 17.14 ?  161 TYR   B CE2  1 
ATOM   6519 C CZ   . TYR   B 1 161 ? 42.495 -34.657 -14.318 1.00 17.11 ?  161 TYR   B CZ   1 
ATOM   6520 O OH   . TYR   B 1 161 ? 41.966 -34.209 -15.501 1.00 19.16 ?  161 TYR   B OH   1 
ATOM   6521 H H    . TYR   B 1 161 ? 44.616 -36.968 -8.442  1.00 16.90 ?  161 TYR   B H    1 
ATOM   6522 H HA   . TYR   B 1 161 ? 42.555 -35.707 -9.306  1.00 17.04 ?  161 TYR   B HA   1 
ATOM   6523 H HB2  . TYR   B 1 161 ? 44.610 -35.223 -10.201 1.00 17.65 ?  161 TYR   B HB2  1 
ATOM   6524 H HB3  . TYR   B 1 161 ? 44.753 -36.693 -10.777 1.00 17.65 ?  161 TYR   B HB3  1 
ATOM   6525 H HD1  . TYR   B 1 161 ? 43.278 -33.585 -11.391 1.00 18.42 ?  161 TYR   B HD1  1 
ATOM   6526 H HD2  . TYR   B 1 161 ? 43.649 -37.286 -12.872 1.00 19.47 ?  161 TYR   B HD2  1 
ATOM   6527 H HE1  . TYR   B 1 161 ? 42.401 -32.874 -13.384 1.00 19.59 ?  161 TYR   B HE1  1 
ATOM   6528 H HE2  . TYR   B 1 161 ? 42.766 -36.571 -14.877 1.00 20.55 ?  161 TYR   B HE2  1 
ATOM   6529 H HH   . TYR   B 1 161 ? 41.926 -34.846 -16.051 1.00 22.97 ?  161 TYR   B HH   1 
ATOM   6530 N N    . ASP   B 1 162 ? 42.650 -38.711 -10.435 1.00 14.58 ?  162 ASP   B N    1 
ATOM   6531 C CA   . ASP   B 1 162 ? 41.826 -39.750 -11.051 1.00 15.25 ?  162 ASP   B CA   1 
ATOM   6532 C C    . ASP   B 1 162 ? 40.615 -40.084 -10.188 1.00 14.68 ?  162 ASP   B C    1 
ATOM   6533 O O    . ASP   B 1 162 ? 39.511 -40.295 -10.707 1.00 15.24 ?  162 ASP   B O    1 
ATOM   6534 C CB   . ASP   B 1 162 ? 42.657 -41.011 -11.309 1.00 17.02 ?  162 ASP   B CB   1 
ATOM   6535 C CG   . ASP   B 1 162 ? 43.654 -40.844 -12.440 1.00 18.25 ?  162 ASP   B CG   1 
ATOM   6536 O OD1  . ASP   B 1 162 ? 43.522 -39.892 -13.238 1.00 18.37 ?  162 ASP   B OD1  1 
ATOM   6537 O OD2  . ASP   B 1 162 ? 44.565 -41.690 -12.540 1.00 20.33 -1 162 ASP   B OD2  1 
ATOM   6538 H H    . ASP   B 1 162 ? 43.451 -38.960 -10.238 1.00 17.47 ?  162 ASP   B H    1 
ATOM   6539 H HA   . ASP   B 1 162 ? 41.500 -39.426 -11.903 1.00 18.28 ?  162 ASP   B HA   1 
ATOM   6540 H HB2  . ASP   B 1 162 ? 43.152 -41.231 -10.504 1.00 20.40 ?  162 ASP   B HB2  1 
ATOM   6541 H HB3  . ASP   B 1 162 ? 42.062 -41.737 -11.545 1.00 20.40 ?  162 ASP   B HB3  1 
ATOM   6542 N N    . LYS   B 1 163 ? 40.800 -40.159 -8.870  1.00 14.09 ?  163 LYS   B N    1 
ATOM   6543 C CA   . LYS   B 1 163 ? 39.672 -40.430 -7.986  1.00 14.72 ?  163 LYS   B CA   1 
ATOM   6544 C C    . LYS   B 1 163 ? 38.626 -39.324 -8.060  1.00 13.75 ?  163 LYS   B C    1 
ATOM   6545 O O    . LYS   B 1 163 ? 37.417 -39.597 -8.079  1.00 14.92 ?  163 LYS   B O    1 
ATOM   6546 C CB   . LYS   B 1 163 ? 40.152 -40.617 -6.550  1.00 18.18 ?  163 LYS   B CB   1 
ATOM   6547 C CG   . LYS   B 1 163 ? 39.048 -41.077 -5.622  1.00 24.90 ?  163 LYS   B CG   1 
ATOM   6548 C CD   . LYS   B 1 163 ? 39.532 -41.362 -4.215  1.00 31.31 ?  163 LYS   B CD   1 
ATOM   6549 C CE   . LYS   B 1 163 ? 38.420 -42.015 -3.403  1.00 35.77 ?  163 LYS   B CE   1 
ATOM   6550 N NZ   . LYS   B 1 163 ? 38.458 -41.645 -1.961  1.00 40.04 ?  163 LYS   B NZ   1 
ATOM   6551 H H    . LYS   B 1 163 ? 41.555 -40.057 -8.473  1.00 16.88 ?  163 LYS   B H    1 
ATOM   6552 H HA   . LYS   B 1 163 ? 39.246 -41.252 -8.268  1.00 17.64 ?  163 LYS   B HA   1 
ATOM   6553 H HB2  . LYS   B 1 163 ? 40.854 -41.287 -6.541  1.00 21.79 ?  163 LYS   B HB2  1 
ATOM   6554 H HB3  . LYS   B 1 163 ? 40.494 -39.773 -6.219  1.00 21.79 ?  163 LYS   B HB3  1 
ATOM   6555 H HG2  . LYS   B 1 163 ? 38.371 -40.384 -5.568  1.00 29.86 ?  163 LYS   B HG2  1 
ATOM   6556 H HG3  . LYS   B 1 163 ? 38.658 -41.892 -5.976  1.00 29.86 ?  163 LYS   B HG3  1 
ATOM   6557 H HD2  . LYS   B 1 163 ? 40.287 -41.972 -4.249  1.00 37.54 ?  163 LYS   B HD2  1 
ATOM   6558 H HD3  . LYS   B 1 163 ? 39.785 -40.532 -3.783  1.00 37.54 ?  163 LYS   B HD3  1 
ATOM   6559 H HE2  . LYS   B 1 163 ? 37.562 -41.743 -3.765  1.00 42.90 ?  163 LYS   B HE2  1 
ATOM   6560 H HE3  . LYS   B 1 163 ? 38.511 -42.978 -3.467  1.00 42.90 ?  163 LYS   B HE3  1 
ATOM   6561 H HZ1  . LYS   B 1 163 ? 37.791 -42.046 -1.528  1.00 48.03 ?  163 LYS   B HZ1  1 
ATOM   6562 H HZ2  . LYS   B 1 163 ? 39.231 -41.900 -1.603  1.00 48.03 ?  163 LYS   B HZ2  1 
ATOM   6563 H HZ3  . LYS   B 1 163 ? 38.372 -40.764 -1.871  1.00 48.03 ?  163 LYS   B HZ3  1 
ATOM   6564 N N    . LEU   B 1 164 ? 39.077 -38.068 -8.103  1.00 12.65 ?  164 LEU   B N    1 
ATOM   6565 C CA   . LEU   B 1 164 ? 38.163 -36.930 -8.159  1.00 12.46 ?  164 LEU   B CA   1 
ATOM   6566 C C    . LEU   B 1 164 ? 37.381 -36.911 -9.466  1.00 13.09 ?  164 LEU   B C    1 
ATOM   6567 O O    . LEU   B 1 164 ? 36.159 -36.709 -9.469  1.00 13.84 ?  164 LEU   B O    1 
ATOM   6568 C CB   . LEU   B 1 164 ? 38.963 -35.636 -7.998  1.00 12.16 ?  164 LEU   B CB   1 
ATOM   6569 C CG   . LEU   B 1 164 ? 39.489 -35.360 -6.594  1.00 13.06 ?  164 LEU   B CG   1 
ATOM   6570 C CD1  . LEU   B 1 164 ? 40.587 -34.313 -6.636  1.00 13.53 ?  164 LEU   B CD1  1 
ATOM   6571 C CD2  . LEU   B 1 164 ? 38.363 -34.923 -5.682  1.00 14.76 ?  164 LEU   B CD2  1 
ATOM   6572 H H    . LEU   B 1 164 ? 39.915 -37.845 -8.098  1.00 15.15 ?  164 LEU   B H    1 
ATOM   6573 H HA   . LEU   B 1 164 ? 37.537 -36.987 -7.427  1.00 14.93 ?  164 LEU   B HA   1 
ATOM   6574 H HB2  . LEU   B 1 164 ? 39.736 -35.668 -8.591  1.00 14.57 ?  164 LEU   B HB2  1 
ATOM   6575 H HB3  . LEU   B 1 164 ? 38.402 -34.886 -8.248  1.00 14.57 ?  164 LEU   B HB3  1 
ATOM   6576 H HG   . LEU   B 1 164 ? 39.872 -36.171 -6.234  1.00 15.65 ?  164 LEU   B HG   1 
ATOM   6577 H HD11 . LEU   B 1 164 ? 40.903 -34.142 -5.733  1.00 16.21 ?  164 LEU   B HD11 1 
ATOM   6578 H HD12 . LEU   B 1 164 ? 41.324 -34.643 -7.181  1.00 16.21 ?  164 LEU   B HD12 1 
ATOM   6579 H HD13 . LEU   B 1 164 ? 40.238 -33.494 -7.022  1.00 16.21 ?  164 LEU   B HD13 1 
ATOM   6580 H HD21 . LEU   B 1 164 ? 38.726 -34.686 -4.816  1.00 17.69 ?  164 LEU   B HD21 1 
ATOM   6581 H HD22 . LEU   B 1 164 ? 37.914 -34.156 -6.074  1.00 17.69 ?  164 LEU   B HD22 1 
ATOM   6582 H HD23 . LEU   B 1 164 ? 37.734 -35.657 -5.587  1.00 17.69 ?  164 LEU   B HD23 1 
ATOM   6583 N N    . VAL   B 1 165 ? 38.074 -37.080 -10.593 1.00 14.32 ?  165 VAL   B N    1 
ATOM   6584 C CA   . VAL   B 1 165 ? 37.424 -37.016 -11.899 1.00 15.19 ?  165 VAL   B CA   1 
ATOM   6585 C C    . VAL   B 1 165 ? 36.516 -38.223 -12.096 1.00 16.79 ?  165 VAL   B C    1 
ATOM   6586 O O    . VAL   B 1 165 ? 35.361 -38.091 -12.520 1.00 17.69 ?  165 VAL   B O    1 
ATOM   6587 C CB   . VAL   B 1 165 ? 38.478 -36.915 -13.018 1.00 16.06 ?  165 VAL   B CB   1 
ATOM   6588 C CG1  . VAL   B 1 165 ? 37.826 -37.025 -14.374 1.00 17.47 ?  165 VAL   B CG1  1 
ATOM   6589 C CG2  . VAL   B 1 165 ? 39.253 -35.612 -12.903 1.00 15.82 ?  165 VAL   B CG2  1 
ATOM   6590 H H    . VAL   B 1 165 ? 38.922 -37.225 -10.626 1.00 17.16 ?  165 VAL   B H    1 
ATOM   6591 H HA   . VAL   B 1 165 ? 36.875 -36.217 -11.938 1.00 18.20 ?  165 VAL   B HA   1 
ATOM   6592 H HB   . VAL   B 1 165 ? 39.115 -37.639 -12.922 1.00 19.25 ?  165 VAL   B HB   1 
ATOM   6593 H HG11 . VAL   B 1 165 ? 38.444 -36.707 -15.047 1.00 20.94 ?  165 VAL   B HG11 1 
ATOM   6594 H HG12 . VAL   B 1 165 ? 37.610 -37.956 -14.539 1.00 20.94 ?  165 VAL   B HG12 1 
ATOM   6595 H HG13 . VAL   B 1 165 ? 37.020 -36.488 -14.379 1.00 20.94 ?  165 VAL   B HG13 1 
ATOM   6596 H HG21 . VAL   B 1 165 ? 39.895 -35.555 -13.630 1.00 18.96 ?  165 VAL   B HG21 1 
ATOM   6597 H HG22 . VAL   B 1 165 ? 38.632 -34.865 -12.958 1.00 18.96 ?  165 VAL   B HG22 1 
ATOM   6598 H HG23 . VAL   B 1 165 ? 39.719 -35.586 -12.051 1.00 18.96 ?  165 VAL   B HG23 1 
ATOM   6599 N N    . SER   B 1 166 ? 37.028 -39.420 -11.787 1.00 17.39 ?  166 SER   B N    1 
ATOM   6600 C CA   . SER   B 1 166 ? 36.274 -40.633 -12.068 1.00 18.48 ?  166 SER   B CA   1 
ATOM   6601 C C    . SER   B 1 166 ? 35.012 -40.717 -11.225 1.00 18.72 ?  166 SER   B C    1 
ATOM   6602 O O    . SER   B 1 166 ? 34.040 -41.337 -11.653 1.00 19.98 ?  166 SER   B O    1 
ATOM   6603 C CB   . SER   B 1 166 ? 37.133 -41.891 -11.890 1.00 19.23 ?  166 SER   B CB   1 
ATOM   6604 O OG   . SER   B 1 166 ? 37.498 -42.093 -10.536 1.00 19.45 ?  166 SER   B OG   1 
ATOM   6605 H H    . SER   B 1 166 ? 37.803 -39.545 -11.427 1.00 20.84 ?  166 SER   B H    1 
ATOM   6606 H HA   . SER   B 1 166 ? 36.001 -40.607 -12.997 1.00 22.15 ?  166 SER   B HA   1 
ATOM   6607 H HB2  . SER   B 1 166 ? 36.625 -42.658 -12.196 1.00 23.04 ?  166 SER   B HB2  1 
ATOM   6608 H HB3  . SER   B 1 166 ? 37.939 -41.798 -12.425 1.00 23.04 ?  166 SER   B HB3  1 
ATOM   6609 H HG   . SER   B 1 166 ? 37.948 -41.438 -10.263 1.00 23.32 ?  166 SER   B HG   1 
ATOM   6610 N N    . SER   B 1 167 ? 34.991 -40.105 -10.042 1.00 17.42 ?  167 SER   B N    1 
ATOM   6611 C CA   . SER   B 1 167 ? 33.832 -40.168 -9.161  1.00 16.81 ?  167 SER   B CA   1 
ATOM   6612 C C    . SER   B 1 167 ? 32.908 -38.954 -9.271  1.00 16.73 ?  167 SER   B C    1 
ATOM   6613 O O    . SER   B 1 167 ? 31.829 -38.951 -8.665  1.00 16.92 ?  167 SER   B O    1 
ATOM   6614 C CB   . SER   B 1 167 ? 34.271 -40.348 -7.702  1.00 16.47 ?  167 SER   B CB   1 
ATOM   6615 O OG   . SER   B 1 167 ? 34.929 -39.185 -7.224  1.00 16.47 ?  167 SER   B OG   1 
ATOM   6616 H H    . SER   B 1 167 ? 35.644 -39.644 -9.728  1.00 20.88 ?  167 SER   B H    1 
ATOM   6617 H HA   . SER   B 1 167 ? 33.311 -40.950 -9.404  1.00 20.14 ?  167 SER   B HA   1 
ATOM   6618 H HB2  . SER   B 1 167 ? 33.487 -40.518 -7.158  1.00 19.73 ?  167 SER   B HB2  1 
ATOM   6619 H HB3  . SER   B 1 167 ? 34.877 -41.110 -7.650  1.00 19.73 ?  167 SER   B HB3  1 
ATOM   6620 H HG   . SER   B 1 167 ? 35.618 -39.045 -7.685  1.00 19.73 ?  167 SER   B HG   1 
ATOM   6621 N N    . PHE   B 1 168 ? 33.285 -37.930 -10.038 1.00 16.48 ?  168 PHE   B N    1 
ATOM   6622 C CA   . PHE   B 1 168 ? 32.471 -36.716 -10.094 1.00 16.18 ?  168 PHE   B CA   1 
ATOM   6623 C C    . PHE   B 1 168 ? 31.142 -36.958 -10.805 1.00 14.67 ?  168 PHE   B C    1 
ATOM   6624 O O    . PHE   B 1 168 ? 30.118 -36.334 -10.465 1.00 15.47 ?  168 PHE   B O    1 
ATOM   6625 C CB   . PHE   B 1 168 ? 33.233 -35.596 -10.801 1.00 16.57 ?  168 PHE   B CB   1 
ATOM   6626 C CG   . PHE   B 1 168 ? 32.444 -34.334 -10.915 1.00 16.81 ?  168 PHE   B CG   1 
ATOM   6627 C CD1  . PHE   B 1 168 ? 32.150 -33.595 -9.781  1.00 18.18 ?  168 PHE   B CD1  1 
ATOM   6628 C CD2  . PHE   B 1 168 ? 31.962 -33.905 -12.133 1.00 16.21 ?  168 PHE   B CD2  1 
ATOM   6629 C CE1  . PHE   B 1 168 ? 31.401 -32.437 -9.861  1.00 18.97 ?  168 PHE   B CE1  1 
ATOM   6630 C CE2  . PHE   B 1 168 ? 31.218 -32.733 -12.229 1.00 17.41 ?  168 PHE   B CE2  1 
ATOM   6631 C CZ   . PHE   B 1 168 ? 30.933 -32.000 -11.088 1.00 18.03 ?  168 PHE   B CZ   1 
ATOM   6632 H H    . PHE   B 1 168 ? 34.005 -37.905 -10.517 1.00 19.75 ?  168 PHE   B H    1 
ATOM   6633 H HA   . PHE   B 1 168 ? 32.279 -36.425 -9.192  1.00 19.39 ?  168 PHE   B HA   1 
ATOM   6634 H HB2  . PHE   B 1 168 ? 34.039 -35.397 -10.300 1.00 19.85 ?  168 PHE   B HB2  1 
ATOM   6635 H HB3  . PHE   B 1 168 ? 33.462 -35.884 -11.698 1.00 19.85 ?  168 PHE   B HB3  1 
ATOM   6636 H HD1  . PHE   B 1 168 ? 32.459 -33.888 -8.953  1.00 21.79 ?  168 PHE   B HD1  1 
ATOM   6637 H HD2  . PHE   B 1 168 ? 32.149 -34.391 -12.903 1.00 19.42 ?  168 PHE   B HD2  1 
ATOM   6638 H HE1  . PHE   B 1 168 ? 31.212 -31.949 -9.092  1.00 22.73 ?  168 PHE   B HE1  1 
ATOM   6639 H HE2  . PHE   B 1 168 ? 30.899 -32.448 -13.057 1.00 20.86 ?  168 PHE   B HE2  1 
ATOM   6640 H HZ   . PHE   B 1 168 ? 30.427 -31.220 -11.149 1.00 21.61 ?  168 PHE   B HZ   1 
ATOM   6641 N N    . LEU   B 1 169 ? 31.147 -37.851 -11.790 1.00 15.28 ?  169 LEU   B N    1 
ATOM   6642 C CA   . LEU   B 1 169 ? 29.964 -38.145 -12.580 1.00 17.52 ?  169 LEU   B CA   1 
ATOM   6643 C C    . LEU   B 1 169 ? 29.963 -39.578 -13.092 1.00 20.52 ?  169 LEU   B C    1 
ATOM   6644 O O    . LEU   B 1 169 ? 29.054 -39.997 -13.811 1.00 22.95 ?  169 LEU   B O    1 
ATOM   6645 C CB   . LEU   B 1 169 ? 29.877 -37.186 -13.766 1.00 19.32 ?  169 LEU   B CB   1 
ATOM   6646 C CG   . LEU   B 1 169 ? 28.604 -36.345 -13.856 1.00 22.35 ?  169 LEU   B CG   1 
ATOM   6647 C CD1  . LEU   B 1 169 ? 28.552 -35.625 -15.191 1.00 23.54 ?  169 LEU   B CD1  1 
ATOM   6648 C CD2  . LEU   B 1 169 ? 27.359 -37.187 -13.646 1.00 22.82 ?  169 LEU   B CD2  1 
ATOM   6649 O OXT  . LEU   B 1 169 ? 30.885 -40.338 -12.811 1.00 21.83 -1 169 LEU   B OXT  1 
ATOM   6650 H H    . LEU   B 1 169 ? 31.845 -38.301 -12.032 1.00 18.32 ?  169 LEU   B H    1 
ATOM   6651 H HA   . LEU   B 1 169 ? 29.185 -38.021 -12.022 1.00 21.00 ?  169 LEU   B HA   1 
ATOM   6652 H HB2  . LEU   B 1 169 ? 30.626 -36.571 -13.723 1.00 23.16 ?  169 LEU   B HB2  1 
ATOM   6653 H HB3  . LEU   B 1 169 ? 29.934 -37.704 -14.585 1.00 23.16 ?  169 LEU   B HB3  1 
ATOM   6654 H HG   . LEU   B 1 169 ? 28.628 -35.669 -13.159 1.00 26.80 ?  169 LEU   B HG   1 
ATOM   6655 H HD11 . LEU   B 1 169 ? 27.751 -35.078 -15.223 1.00 28.23 ?  169 LEU   B HD11 1 
ATOM   6656 H HD12 . LEU   B 1 169 ? 29.339 -35.065 -15.278 1.00 28.23 ?  169 LEU   B HD12 1 
ATOM   6657 H HD13 . LEU   B 1 169 ? 28.533 -36.284 -15.902 1.00 28.23 ?  169 LEU   B HD13 1 
ATOM   6658 H HD21 . LEU   B 1 169 ? 26.600 -36.741 -14.047 1.00 27.36 ?  169 LEU   B HD21 1 
ATOM   6659 H HD22 . LEU   B 1 169 ? 27.492 -38.056 -14.059 1.00 27.36 ?  169 LEU   B HD22 1 
ATOM   6660 H HD23 . LEU   B 1 169 ? 27.215 -37.295 -12.693 1.00 27.36 ?  169 LEU   B HD23 1 
HETATM 6661 N N2   B A1A5C C 2 .   ? 11.087 4.920   3.042   0.30 22.49 ?  201 A1A5C A N2   1 
HETATM 6662 C C3   B A1A5C C 2 .   ? 14.353 4.332   4.678   0.30 22.26 ?  201 A1A5C A C3   1 
HETATM 6663 C C6   B A1A5C C 2 .   ? 13.181 3.072   2.623   0.30 23.02 ?  201 A1A5C A C6   1 
HETATM 6664 C C9   B A1A5C C 2 .   ? 13.874 -2.083  1.963   0.30 23.42 ?  201 A1A5C A C9   1 
HETATM 6665 C C12  B A1A5C C 2 .   ? 13.170 0.153   0.330   0.30 23.00 ?  201 A1A5C A C12  1 
HETATM 6666 C C14  B A1A5C C 2 .   ? 11.120 3.970   2.108   0.30 22.76 ?  201 A1A5C A C14  1 
HETATM 6667 C C1   B A1A5C C 2 .   ? 14.760 5.961   6.614   0.30 21.99 ?  201 A1A5C A C1   1 
HETATM 6668 C C10  B A1A5C C 2 .   ? 13.172 -2.286  0.767   0.30 23.34 ?  201 A1A5C A C10  1 
HETATM 6669 C C11  B A1A5C C 2 .   ? 12.829 -1.181  -0.034  0.30 23.17 ?  201 A1A5C A C11  1 
HETATM 6670 C C13  B A1A5C C 2 .   ? 12.737 1.254   -0.615  0.30 22.32 ?  201 A1A5C A C13  1 
HETATM 6671 C C15  B A1A5C C 2 .   ? 12.211 4.922   3.810   0.30 22.15 ?  201 A1A5C A C15  1 
HETATM 6672 C C2   B A1A5C C 2 .   ? 13.976 5.382   5.485   0.30 21.94 ?  201 A1A5C A C2   1 
HETATM 6673 C C4   B A1A5C C 2 .   ? 15.670 3.635   4.863   0.30 22.48 ?  201 A1A5C A C4   1 
HETATM 6674 C C5   B A1A5C C 2 .   ? 13.328 4.033   3.678   0.30 22.48 ?  201 A1A5C A C5   1 
HETATM 6675 C C7   B A1A5C C 2 .   ? 13.868 0.348   1.570   0.30 23.36 ?  201 A1A5C A C7   1 
HETATM 6676 C C8   B A1A5C C 2 .   ? 14.219 -0.777  2.346   0.30 23.38 ?  201 A1A5C A C8   1 
HETATM 6677 N N1   B A1A5C C 2 .   ? 12.075 3.073   1.846   0.30 22.94 ?  201 A1A5C A N1   1 
HETATM 6678 O O1   B A1A5C C 2 .   ? 11.804 1.002   -1.414  0.30 22.45 ?  201 A1A5C A O1   1 
HETATM 6679 O O2   B A1A5C C 2 .   ? 13.288 2.377   -0.598  0.30 21.46 ?  201 A1A5C A O2   1 
HETATM 6680 S S1   B A1A5C C 2 .   ? 14.446 1.887   2.258   0.30 23.63 ?  201 A1A5C A S1   1 
HETATM 6681 S S2   B A1A5C C 2 .   ? 12.432 6.076   5.110   0.30 21.69 ?  201 A1A5C A S2   1 
HETATM 6682 H H8   B A1A5C C 2 .   ? 14.146 -2.921  2.589   0.30 28.08 ?  201 A1A5C A H8   1 
HETATM 6683 H H11  B A1A5C C 2 .   ? 10.248 3.932   1.475   0.30 27.28 ?  201 A1A5C A H11  1 
HETATM 6684 H H2   B A1A5C C 2 .   ? 15.083 5.182   7.310   0.30 26.36 ?  201 A1A5C A H2   1 
HETATM 6685 H H3   B A1A5C C 2 .   ? 14.161 6.676   7.176   0.30 26.36 ?  201 A1A5C A H3   1 
HETATM 6686 H H1   B A1A5C C 2 .   ? 15.646 6.468   6.246   0.30 26.36 ?  201 A1A5C A H1   1 
HETATM 6687 H H9   B A1A5C C 2 .   ? 12.902 -3.289  0.461   0.30 27.98 ?  201 A1A5C A H9   1 
HETATM 6688 H H10  B A1A5C C 2 .   ? 12.296 -1.380  -0.953  0.30 27.78 ?  201 A1A5C A H10  1 
HETATM 6689 H H5   B A1A5C C 2 .   ? 16.046 3.231   3.926   0.30 26.96 ?  201 A1A5C A H5   1 
HETATM 6690 H H6   B A1A5C C 2 .   ? 15.611 2.810   5.566   0.30 26.96 ?  201 A1A5C A H6   1 
HETATM 6691 H H4   B A1A5C C 2 .   ? 16.424 4.325   5.243   0.30 26.96 ?  201 A1A5C A H4   1 
HETATM 6692 H H7   B A1A5C C 2 .   ? 14.762 -0.632  3.263   0.30 28.03 ?  201 A1A5C A H7   1 
HETATM 6693 N N2   C A1A5C D 2 .   ? 15.189 0.820   6.419   0.30 19.70 ?  202 A1A5C A N2   1 
HETATM 6694 C C3   C A1A5C D 2 .   ? 14.572 4.066   4.741   0.30 18.78 ?  202 A1A5C A C3   1 
HETATM 6695 C C6   C A1A5C D 2 .   ? 14.698 1.584   3.755   0.30 20.77 ?  202 A1A5C A C6   1 
HETATM 6696 C C9   C A1A5C D 2 .   ? 15.660 -1.577  0.339   0.30 22.86 ?  202 A1A5C A C9   1 
HETATM 6697 C C12  C A1A5C D 2 .   ? 13.191 -0.504  1.278   0.30 22.37 ?  202 A1A5C A C12  1 
HETATM 6698 C C14  C A1A5C D 2 .   ? 15.117 -0.008  5.375   0.30 20.21 ?  202 A1A5C A C14  1 
HETATM 6699 C C1   C A1A5C D 2 .   ? 14.619 6.016   6.416   0.30 18.77 ?  202 A1A5C A C1   1 
HETATM 6700 C C10  C A1A5C D 2 .   ? 14.482 -2.335  0.254   0.30 22.91 ?  202 A1A5C A C10  1 
HETATM 6701 C C11  C A1A5C D 2 .   ? 13.264 -1.802  0.718   0.30 22.76 ?  202 A1A5C A C11  1 
HETATM 6702 C C13  C A1A5C D 2 .   ? 11.854 0.022   1.756   0.30 22.11 ?  202 A1A5C A C13  1 
HETATM 6703 C C15  C A1A5C D 2 .   ? 14.992 2.121   6.061   0.30 19.18 ?  202 A1A5C A C15  1 
HETATM 6704 C C2   C A1A5C D 2 .   ? 14.715 4.586   6.006   0.30 18.60 ?  202 A1A5C A C2   1 
HETATM 6705 C C4   C A1A5C D 2 .   ? 14.307 4.938   3.552   0.30 18.64 ?  202 A1A5C A C4   1 
HETATM 6706 C C5   C A1A5C D 2 .   ? 14.736 2.614   4.743   0.30 19.48 ?  202 A1A5C A C5   1 
HETATM 6707 C C7   C A1A5C D 2 .   ? 14.394 0.258   1.359   0.30 22.60 ?  202 A1A5C A C7   1 
HETATM 6708 C C8   C A1A5C D 2 .   ? 15.615 -0.283  0.891   0.30 22.73 ?  202 A1A5C A C8   1 
HETATM 6709 N N1   C A1A5C D 2 .   ? 14.885 0.288   4.095   0.30 20.50 ?  202 A1A5C A N1   1 
HETATM 6710 O O1   C A1A5C D 2 .   ? 11.454 -0.285  2.901   0.30 21.82 ?  202 A1A5C A O1   1 
HETATM 6711 O O2   C A1A5C D 2 .   ? 11.173 0.766   1.015   0.30 22.29 ?  202 A1A5C A O2   1 
HETATM 6712 S S1   C A1A5C D 2 .   ? 14.393 1.893   2.043   0.30 22.58 ?  202 A1A5C A S1   1 
HETATM 6713 S S2   C A1A5C D 2 .   ? 15.036 3.413   7.238   0.30 18.56 ?  202 A1A5C A S2   1 
HETATM 6714 H H8   C A1A5C D 2 .   ? 16.599 -1.984  -0.018  0.30 27.41 ?  202 A1A5C A H8   1 
HETATM 6715 H H11  C A1A5C D 2 .   ? 15.268 -1.052  5.600   0.30 24.23 ?  202 A1A5C A H11  1 
HETATM 6716 H H2   C A1A5C D 2 .   ? 14.052 6.125   7.341   0.30 22.50 ?  202 A1A5C A H2   1 
HETATM 6717 H H3   C A1A5C D 2 .   ? 14.116 6.606   5.653   0.30 22.50 ?  202 A1A5C A H3   1 
HETATM 6718 H H1   C A1A5C D 2 .   ? 15.609 6.437   6.581   0.30 22.50 ?  202 A1A5C A H1   1 
HETATM 6719 H H9   C A1A5C D 2 .   ? 14.512 -3.329  -0.170  0.30 27.47 ?  202 A1A5C A H9   1 
HETATM 6720 H H10  C A1A5C D 2 .   ? 12.378 -2.411  0.638   0.30 27.28 ?  202 A1A5C A H10  1 
HETATM 6721 H H5   C A1A5C D 2 .   ? 14.761 5.925   3.680   0.30 22.34 ?  202 A1A5C A H5   1 
HETATM 6722 H H6   C A1A5C D 2 .   ? 14.720 4.536   2.632   0.30 22.34 ?  202 A1A5C A H6   1 
HETATM 6723 H H4   C A1A5C D 2 .   ? 13.243 5.083   3.403   0.30 22.34 ?  202 A1A5C A H4   1 
HETATM 6724 H H7   C A1A5C D 2 .   ? 16.531 0.292   0.951   0.30 27.25 ?  202 A1A5C A H7   1 
HETATM 6725 O O    . HOH   E 3 .   ? 14.875 -4.777  20.577  1.00 41.34 ?  301 HOH   A O    1 
HETATM 6726 O O    . HOH   E 3 .   ? 4.837  3.906   0.810   1.00 37.44 ?  302 HOH   A O    1 
HETATM 6727 O O    . HOH   E 3 .   ? 11.506 -10.865 -10.037 1.00 36.72 ?  303 HOH   A O    1 
HETATM 6728 O O    . HOH   E 3 .   ? 7.625  -6.414  -6.489  1.00 38.82 ?  304 HOH   A O    1 
HETATM 6729 O O    . HOH   E 3 .   ? 15.326 -12.353 18.795  1.00 31.86 ?  305 HOH   A O    1 
HETATM 6730 O O    . HOH   E 3 .   ? -0.536 -8.480  2.318   1.00 44.35 ?  306 HOH   A O    1 
HETATM 6731 O O    . HOH   E 3 .   ? 14.415 -24.750 11.644  1.00 32.30 ?  307 HOH   A O    1 
HETATM 6732 O O    . HOH   E 3 .   ? 34.533 -1.873  12.505  1.00 39.12 ?  308 HOH   A O    1 
HETATM 6733 O O    . HOH   E 3 .   ? 0.735  -4.605  0.520   1.00 29.97 ?  309 HOH   A O    1 
HETATM 6734 O O    . HOH   E 3 .   ? 12.259 0.219   15.039  1.00 35.49 ?  310 HOH   A O    1 
HETATM 6735 O O    . HOH   E 3 .   ? 28.926 0.470   -9.662  1.00 19.47 ?  311 HOH   A O    1 
HETATM 6736 O O    . HOH   E 3 .   ? 7.054  -8.322  12.079  1.00 27.87 ?  312 HOH   A O    1 
HETATM 6737 O O    . HOH   E 3 .   ? 19.022 -22.079 6.855   1.00 32.42 ?  313 HOH   A O    1 
HETATM 6738 O O    A HOH   E 3 .   ? 14.677 -3.722  3.185   0.70 17.27 ?  314 HOH   A O    1 
HETATM 6739 O O    . HOH   E 3 .   ? 42.449 10.541  5.195   1.00 18.71 ?  315 HOH   A O    1 
HETATM 6740 O O    . HOH   E 3 .   ? 36.161 -5.046  -0.532  1.00 25.73 ?  316 HOH   A O    1 
HETATM 6741 O O    . HOH   E 3 .   ? 28.344 -0.246  -13.347 1.00 34.60 ?  317 HOH   A O    1 
HETATM 6742 O O    . HOH   E 3 .   ? 34.019 -0.921  -8.868  1.00 26.46 ?  318 HOH   A O    1 
HETATM 6743 O O    . HOH   E 3 .   ? 9.830  -21.438 5.783   1.00 18.22 ?  319 HOH   A O    1 
HETATM 6744 O O    . HOH   E 3 .   ? 8.026  -12.651 -0.761  1.00 21.44 ?  320 HOH   A O    1 
HETATM 6745 O O    . HOH   E 3 .   ? 17.228 -18.197 15.159  1.00 25.74 ?  321 HOH   A O    1 
HETATM 6746 O O    . HOH   E 3 .   ? 15.597 11.910  8.080   1.00 27.28 ?  322 HOH   A O    1 
HETATM 6747 O O    . HOH   E 3 .   ? 18.771 -19.547 13.536  1.00 33.96 ?  323 HOH   A O    1 
HETATM 6748 O O    . HOH   E 3 .   ? 28.354 -6.405  19.616  1.00 41.50 ?  324 HOH   A O    1 
HETATM 6749 O O    . HOH   E 3 .   ? 11.829 -10.937 17.129  1.00 22.84 ?  325 HOH   A O    1 
HETATM 6750 O O    . HOH   E 3 .   ? 30.272 -13.267 -8.603  1.00 19.17 ?  326 HOH   A O    1 
HETATM 6751 O O    . HOH   E 3 .   ? 26.525 -19.353 -1.858  1.00 13.17 ?  327 HOH   A O    1 
HETATM 6752 O O    . HOH   E 3 .   ? 37.604 2.706   10.145  1.00 28.39 ?  328 HOH   A O    1 
HETATM 6753 O O    . HOH   E 3 .   ? 22.574 5.218   19.172  1.00 41.53 ?  329 HOH   A O    1 
HETATM 6754 O O    . HOH   E 3 .   ? 14.209 -4.565  -11.750 1.00 28.17 ?  330 HOH   A O    1 
HETATM 6755 O O    . HOH   E 3 .   ? 31.084 -18.218 7.742   1.00 26.77 ?  331 HOH   A O    1 
HETATM 6756 O O    A HOH   E 3 .   ? 14.323 0.490   6.906   0.70 20.72 ?  332 HOH   A O    1 
HETATM 6757 O O    A HOH   E 3 .   ? 17.528 -1.768  0.529   0.70 20.55 ?  333 HOH   A O    1 
HETATM 6758 O O    . HOH   E 3 .   ? 8.215  -21.554 4.071   1.00 51.86 ?  334 HOH   A O    1 
HETATM 6759 O O    . HOH   E 3 .   ? 14.839 -14.131 16.794  1.00 20.73 ?  335 HOH   A O    1 
HETATM 6760 O O    . HOH   E 3 .   ? 13.307 -1.381  -6.568  1.00 16.90 ?  336 HOH   A O    1 
HETATM 6761 O O    . HOH   E 3 .   ? 22.828 12.511  1.661   1.00 15.47 ?  337 HOH   A O    1 
HETATM 6762 O O    . HOH   E 3 .   ? 38.310 10.122  7.195   1.00 44.35 ?  338 HOH   A O    1 
HETATM 6763 O O    . HOH   E 3 .   ? 19.865 -12.523 -8.891  1.00 26.27 ?  339 HOH   A O    1 
HETATM 6764 O O    . HOH   E 3 .   ? 13.569 -15.193 -7.423  1.00 26.53 ?  340 HOH   A O    1 
HETATM 6765 O O    . HOH   E 3 .   ? 27.321 13.763  2.952   1.00 30.25 ?  341 HOH   A O    1 
HETATM 6766 O O    . HOH   E 3 .   ? 14.082 -5.139  17.701  1.00 22.85 ?  342 HOH   A O    1 
HETATM 6767 O O    . HOH   E 3 .   ? 20.083 4.540   -7.512  1.00 19.13 ?  343 HOH   A O    1 
HETATM 6768 O O    . HOH   E 3 .   ? 44.315 7.102   6.520   1.00 25.70 ?  344 HOH   A O    1 
HETATM 6769 O O    . HOH   E 3 .   ? 15.360 3.838   18.005  1.00 37.64 ?  345 HOH   A O    1 
HETATM 6770 O O    . HOH   E 3 .   ? 38.613 4.947   6.980   1.00 15.18 ?  346 HOH   A O    1 
HETATM 6771 O O    . HOH   E 3 .   ? 17.171 -17.809 -5.054  1.00 25.92 ?  347 HOH   A O    1 
HETATM 6772 O O    . HOH   E 3 .   ? 17.108 -19.397 4.886   1.00 14.03 ?  348 HOH   A O    1 
HETATM 6773 O O    . HOH   E 3 .   ? 35.841 -12.734 6.738   1.00 15.45 ?  349 HOH   A O    1 
HETATM 6774 O O    . HOH   E 3 .   ? 26.825 11.395  1.708   1.00 16.23 ?  350 HOH   A O    1 
HETATM 6775 O O    . HOH   E 3 .   ? 22.413 -19.321 11.337  1.00 32.76 ?  351 HOH   A O    1 
HETATM 6776 O O    . HOH   E 3 .   ? 38.077 -1.301  -1.980  1.00 18.17 ?  352 HOH   A O    1 
HETATM 6777 O O    . HOH   E 3 .   ? 42.579 4.287   5.296   1.00 27.93 ?  353 HOH   A O    1 
HETATM 6778 O O    . HOH   E 3 .   ? 21.271 -2.370  -2.108  1.00 14.08 ?  354 HOH   A O    1 
HETATM 6779 O O    . HOH   E 3 .   ? 16.392 16.777  8.765   1.00 26.55 ?  355 HOH   A O    1 
HETATM 6780 O O    . HOH   E 3 .   ? 39.776 -0.987  -5.208  1.00 19.07 ?  356 HOH   A O    1 
HETATM 6781 O O    . HOH   E 3 .   ? 18.910 -0.687  -1.597  1.00 14.98 ?  357 HOH   A O    1 
HETATM 6782 O O    . HOH   E 3 .   ? 20.655 -19.671 -5.192  1.00 27.12 ?  358 HOH   A O    1 
HETATM 6783 O O    . HOH   E 3 .   ? 24.038 -2.114  -2.037  1.00 9.93  ?  359 HOH   A O    1 
HETATM 6784 O O    . HOH   E 3 .   ? 31.107 -13.956 -2.547  1.00 12.70 ?  360 HOH   A O    1 
HETATM 6785 O O    . HOH   E 3 .   ? 37.394 11.899  5.002   1.00 26.67 ?  361 HOH   A O    1 
HETATM 6786 O O    . HOH   E 3 .   ? 30.869 3.029   8.335   1.00 11.81 ?  362 HOH   A O    1 
HETATM 6787 O O    . HOH   E 3 .   ? 21.909 -21.956 8.331   1.00 29.05 ?  363 HOH   A O    1 
HETATM 6788 O O    . HOH   E 3 .   ? 24.406 3.586   -1.738  1.00 14.77 ?  364 HOH   A O    1 
HETATM 6789 O O    . HOH   E 3 .   ? 33.718 -7.189  4.237   1.00 15.92 ?  365 HOH   A O    1 
HETATM 6790 O O    . HOH   E 3 .   ? 31.741 8.144   14.913  1.00 25.31 ?  366 HOH   A O    1 
HETATM 6791 O O    . HOH   E 3 .   ? 37.228 -3.015  9.694   1.00 37.41 ?  367 HOH   A O    1 
HETATM 6792 O O    . HOH   E 3 .   ? 14.393 -21.180 -4.337  1.00 29.30 ?  368 HOH   A O    1 
HETATM 6793 O O    . HOH   E 3 .   ? 22.688 -12.043 21.963  1.00 33.51 ?  369 HOH   A O    1 
HETATM 6794 O O    A HOH   E 3 .   ? 3.668  -9.571  9.829   0.40 24.21 ?  370 HOH   A O    1 
HETATM 6795 O O    . HOH   E 3 .   ? 14.126 -23.183 7.458   1.00 18.11 ?  371 HOH   A O    1 
HETATM 6796 O O    A HOH   E 3 .   ? 9.347  -10.366 19.459  0.40 24.98 ?  372 HOH   A O    1 
HETATM 6797 O O    . HOH   E 3 .   ? 18.562 9.415   9.052   1.00 21.46 ?  373 HOH   A O    1 
HETATM 6798 O O    . HOH   E 3 .   ? 24.827 -17.635 12.720  1.00 22.73 ?  374 HOH   A O    1 
HETATM 6799 O O    . HOH   E 3 .   ? 31.872 -9.317  -6.660  1.00 20.36 ?  375 HOH   A O    1 
HETATM 6800 O O    . HOH   E 3 .   ? 26.936 4.145   -0.552  1.00 12.31 ?  376 HOH   A O    1 
HETATM 6801 O O    . HOH   E 3 .   ? 16.495 -22.049 0.954   1.00 27.53 ?  377 HOH   A O    1 
HETATM 6802 O O    . HOH   E 3 .   ? 27.642 -10.735 14.050  1.00 16.21 ?  378 HOH   A O    1 
HETATM 6803 O O    . HOH   E 3 .   ? 15.150 -8.046  -9.557  1.00 20.16 ?  379 HOH   A O    1 
HETATM 6804 O O    . HOH   E 3 .   ? 18.807 -2.456  -16.243 1.00 45.35 ?  380 HOH   A O    1 
HETATM 6805 O O    . HOH   E 3 .   ? 27.283 -5.949  -13.953 1.00 36.72 ?  381 HOH   A O    1 
HETATM 6806 O O    . HOH   E 3 .   ? 6.533  -5.856  11.470  1.00 23.38 ?  382 HOH   A O    1 
HETATM 6807 O O    . HOH   E 3 .   ? 27.923 0.856   -7.116  1.00 12.92 ?  383 HOH   A O    1 
HETATM 6808 O O    . HOH   E 3 .   ? 33.603 -17.013 7.987   1.00 18.87 ?  384 HOH   A O    1 
HETATM 6809 O O    . HOH   E 3 .   ? 43.912 8.503   -3.129  1.00 25.61 ?  385 HOH   A O    1 
HETATM 6810 O O    . HOH   E 3 .   ? 21.349 10.236  15.170  1.00 31.76 ?  386 HOH   A O    1 
HETATM 6811 O O    . HOH   E 3 .   ? 28.532 -10.659 -13.987 1.00 41.93 ?  387 HOH   A O    1 
HETATM 6812 O O    . HOH   E 3 .   ? 30.908 6.274   -12.293 1.00 32.94 ?  388 HOH   A O    1 
HETATM 6813 O O    . HOH   E 3 .   ? 23.482 11.335  4.202   1.00 12.60 ?  389 HOH   A O    1 
HETATM 6814 O O    . HOH   E 3 .   ? 43.358 7.882   2.703   1.00 23.94 ?  390 HOH   A O    1 
HETATM 6815 O O    A HOH   E 3 .   ? -0.436 -3.178  3.235   0.40 24.88 ?  391 HOH   A O    1 
HETATM 6816 O O    . HOH   E 3 .   ? 15.321 -21.762 14.263  1.00 17.95 ?  392 HOH   A O    1 
HETATM 6817 O O    . HOH   E 3 .   ? 31.728 -7.285  -9.885  1.00 20.62 ?  393 HOH   A O    1 
HETATM 6818 O O    . HOH   E 3 .   ? 16.204 2.899   -1.438  1.00 16.18 ?  394 HOH   A O    1 
HETATM 6819 O O    . HOH   E 3 .   ? 21.298 3.115   -0.214  1.00 13.23 ?  395 HOH   A O    1 
HETATM 6820 O O    . HOH   E 3 .   ? 37.582 -2.043  5.771   1.00 26.71 ?  396 HOH   A O    1 
HETATM 6821 O O    . HOH   E 3 .   ? 24.409 -7.923  14.493  1.00 16.77 ?  397 HOH   A O    1 
HETATM 6822 O O    . HOH   E 3 .   ? 24.060 -15.659 -9.252  1.00 28.25 ?  398 HOH   A O    1 
HETATM 6823 O O    . HOH   E 3 .   ? 25.701 -0.784  -7.333  1.00 14.69 ?  399 HOH   A O    1 
HETATM 6824 O O    B HOH   E 3 .   ? 12.069 -2.026  -3.599  0.60 22.15 ?  400 HOH   A O    1 
HETATM 6825 O O    . HOH   E 3 .   ? 20.619 -20.061 2.733   1.00 16.49 ?  401 HOH   A O    1 
HETATM 6826 O O    . HOH   E 3 .   ? 32.834 -9.294  5.855   1.00 18.71 ?  402 HOH   A O    1 
HETATM 6827 O O    . HOH   E 3 .   ? 30.801 1.725   16.728  1.00 21.20 ?  403 HOH   A O    1 
HETATM 6828 O O    . HOH   E 3 .   ? 8.882  -12.161 17.351  1.00 45.40 ?  404 HOH   A O    1 
HETATM 6829 O O    . HOH   E 3 .   ? 27.280 2.213   18.738  1.00 29.70 ?  405 HOH   A O    1 
HETATM 6830 O O    . HOH   E 3 .   ? 40.926 -8.270  -6.722  1.00 35.05 ?  406 HOH   A O    1 
HETATM 6831 O O    . HOH   E 3 .   ? 23.967 -20.304 -1.417  1.00 15.00 ?  407 HOH   A O    1 
HETATM 6832 O O    . HOH   E 3 .   ? 27.231 -3.431  19.262  1.00 35.63 ?  408 HOH   A O    1 
HETATM 6833 O O    A HOH   E 3 .   ? 11.100 1.441   12.871  0.40 17.42 ?  409 HOH   A O    1 
HETATM 6834 O O    . HOH   E 3 .   ? 20.667 -17.951 24.815  1.00 45.95 ?  410 HOH   A O    1 
HETATM 6835 O O    . HOH   E 3 .   ? 24.026 3.930   -4.764  1.00 21.59 ?  411 HOH   A O    1 
HETATM 6836 O O    . HOH   E 3 .   ? 10.454 -13.780 -1.632  1.00 16.88 ?  412 HOH   A O    1 
HETATM 6837 O O    . HOH   E 3 .   ? 16.289 -14.341 20.487  1.00 35.93 ?  413 HOH   A O    1 
HETATM 6838 O O    . HOH   E 3 .   ? 14.445 -0.451  -11.995 1.00 29.62 ?  414 HOH   A O    1 
HETATM 6839 O O    . HOH   E 3 .   ? 30.209 -10.225 12.992  1.00 20.03 ?  415 HOH   A O    1 
HETATM 6840 O O    A HOH   E 3 .   ? 6.816  -3.503  13.001  0.40 20.79 ?  416 HOH   A O    1 
HETATM 6841 O O    . HOH   E 3 .   ? 41.665 1.501   4.949   1.00 37.43 ?  417 HOH   A O    1 
HETATM 6842 O O    . HOH   E 3 .   ? 21.430 -9.396  21.430  1.00 40.08 ?  418 HOH   A O    1 
HETATM 6843 O O    . HOH   E 3 .   ? 22.786 7.968   18.477  1.00 42.73 ?  419 HOH   A O    1 
HETATM 6844 O O    . HOH   E 3 .   ? 35.098 -5.211  -3.127  1.00 17.62 ?  420 HOH   A O    1 
HETATM 6845 O O    . HOH   E 3 .   ? 5.147  2.680   5.536   1.00 34.88 ?  421 HOH   A O    1 
HETATM 6846 O O    . HOH   E 3 .   ? 32.642 -10.668 3.137   1.00 27.96 ?  422 HOH   A O    1 
HETATM 6847 O O    . HOH   E 3 .   ? 44.975 -0.562  2.968   1.00 37.94 ?  423 HOH   A O    1 
HETATM 6848 O O    A HOH   E 3 .   ? 11.102 -0.448  2.045   0.70 32.38 ?  424 HOH   A O    1 
HETATM 6849 O O    . HOH   E 3 .   ? 36.781 -5.000  5.325   1.00 23.50 ?  425 HOH   A O    1 
HETATM 6850 O O    . HOH   E 3 .   ? 21.682 -13.902 -8.151  1.00 41.82 ?  426 HOH   A O    1 
HETATM 6851 O O    . HOH   E 3 .   ? 10.532 -22.286 -1.260  1.00 48.24 ?  427 HOH   A O    1 
HETATM 6852 O O    A HOH   E 3 .   ? 18.886 1.986   -0.653  0.40 8.69  ?  428 HOH   A O    1 
HETATM 6853 O O    A HOH   E 3 .   ? 24.587 2.024   -6.906  0.40 10.99 ?  429 HOH   A O    1 
HETATM 6854 O O    . HOH   E 3 .   ? 30.492 -13.019 13.495  1.00 18.76 ?  430 HOH   A O    1 
HETATM 6855 O O    B HOH   E 3 .   ? 16.305 7.562   3.230   0.60 21.87 ?  431 HOH   A O    1 
HETATM 6856 O O    . HOH   E 3 .   ? 32.682 -4.273  -9.940  1.00 24.98 ?  432 HOH   A O    1 
HETATM 6857 O O    A HOH   E 3 .   ? 15.845 -1.020  5.366   0.70 22.70 ?  433 HOH   A O    1 
HETATM 6858 O O    . HOH   E 3 .   ? 23.693 -8.166  17.055  1.00 21.09 ?  434 HOH   A O    1 
HETATM 6859 O O    . HOH   E 3 .   ? 18.464 5.014   -14.958 1.00 49.22 ?  435 HOH   A O    1 
HETATM 6860 O O    A HOH   E 3 .   ? 16.046 6.889   3.116   0.40 11.28 ?  436 HOH   A O    1 
HETATM 6861 O O    . HOH   E 3 .   ? 23.352 -21.017 1.231   1.00 16.12 ?  437 HOH   A O    1 
HETATM 6862 O O    . HOH   E 3 .   ? 9.501  -16.351 -1.967  1.00 40.66 ?  438 HOH   A O    1 
HETATM 6863 O O    B HOH   E 3 .   ? 10.543 3.993   -0.647  0.60 39.99 ?  439 HOH   A O    1 
HETATM 6864 O O    . HOH   E 3 .   ? 37.752 -8.817  -3.554  1.00 24.17 ?  440 HOH   A O    1 
HETATM 6865 O O    . HOH   E 3 .   ? 18.567 -16.212 16.485  1.00 31.11 ?  441 HOH   A O    1 
HETATM 6866 O O    . HOH   E 3 .   ? 23.228 7.575   -3.119  1.00 27.48 ?  442 HOH   A O    1 
HETATM 6867 O O    . HOH   E 3 .   ? 34.461 -8.093  -0.589  1.00 26.28 ?  443 HOH   A O    1 
HETATM 6868 O O    . HOH   E 3 .   ? 21.724 -14.825 18.083  1.00 42.99 ?  444 HOH   A O    1 
HETATM 6869 O O    B HOH   E 3 .   ? 9.480  2.346   -2.994  0.60 30.40 ?  445 HOH   A O    1 
HETATM 6870 O O    . HOH   E 3 .   ? 31.374 -12.799 -0.039  1.00 17.91 ?  446 HOH   A O    1 
HETATM 6871 O O    . HOH   E 3 .   ? 15.988 2.031   24.948  1.00 53.04 ?  447 HOH   A O    1 
HETATM 6872 O O    . HOH   E 3 .   ? 30.585 14.724  2.846   1.00 19.44 ?  448 HOH   A O    1 
HETATM 6873 O O    . HOH   E 3 .   ? 29.845 -16.085 10.534  1.00 36.99 ?  449 HOH   A O    1 
HETATM 6874 O O    B HOH   E 3 .   ? 18.316 1.674   -0.270  0.60 24.73 ?  450 HOH   A O    1 
HETATM 6875 O O    . HOH   E 3 .   ? 19.587 -11.162 24.263  1.00 48.98 ?  451 HOH   A O    1 
HETATM 6876 O O    . HOH   E 3 .   ? -1.700 -5.107  7.873   1.00 48.07 ?  452 HOH   A O    1 
HETATM 6877 O O    . HOH   E 3 .   ? 27.784 7.071   -6.338  1.00 34.64 ?  453 HOH   A O    1 
HETATM 6878 O O    A HOH   E 3 .   ? 14.066 -0.409  3.565   0.40 23.37 ?  454 HOH   A O    1 
HETATM 6879 O O    . HOH   E 3 .   ? 25.487 8.278   -4.729  1.00 26.83 ?  455 HOH   A O    1 
HETATM 6880 O O    . HOH   E 3 .   ? 32.523 -15.914 10.798  1.00 39.15 ?  456 HOH   A O    1 
HETATM 6881 O O    . HOH   E 3 .   ? 29.762 -2.074  -12.811 1.00 43.42 ?  457 HOH   A O    1 
HETATM 6882 O O    . HOH   E 3 .   ? 12.072 -13.527 16.433  1.00 39.23 ?  458 HOH   A O    1 
HETATM 6883 O O    . HOH   E 3 .   ? 26.939 11.562  -1.188  1.00 26.61 ?  459 HOH   A O    1 
HETATM 6884 O O    . HOH   E 3 .   ? 24.967 5.483   20.785  1.00 50.80 ?  460 HOH   A O    1 
HETATM 6885 O O    . HOH   E 3 .   ? 19.914 -17.293 -5.163  1.00 24.91 ?  461 HOH   A O    1 
HETATM 6886 O O    . HOH   E 3 .   ? 23.270 -22.342 -3.334  1.00 32.90 ?  462 HOH   A O    1 
HETATM 6887 O O    . HOH   E 3 .   ? 24.612 14.485  7.929   1.00 31.69 ?  463 HOH   A O    1 
HETATM 6888 O O    B HOH   E 3 .   ? 10.708 1.267   -4.919  0.60 29.60 ?  464 HOH   A O    1 
HETATM 6889 O O    . HOH   E 3 .   ? 21.975 5.258   -5.850  1.00 27.43 ?  465 HOH   A O    1 
HETATM 6890 O O    . HOH   E 3 .   ? 11.040 -14.965 -5.985  1.00 34.22 ?  466 HOH   A O    1 
HETATM 6891 O O    . HOH   E 3 .   ? 39.698 -7.017  -3.654  1.00 39.60 ?  467 HOH   A O    1 
HETATM 6892 O O    . HOH   E 3 .   ? 23.542 13.723  5.554   1.00 20.27 ?  468 HOH   A O    1 
HETATM 6893 O O    . HOH   E 3 .   ? 18.783 10.740  11.459  1.00 34.39 ?  469 HOH   A O    1 
HETATM 6894 O O    . HOH   E 3 .   ? 27.548 -11.557 16.469  1.00 37.28 ?  470 HOH   A O    1 
HETATM 6895 O O    . HOH   E 3 .   ? 15.843 -21.642 3.760   1.00 24.23 ?  471 HOH   A O    1 
HETATM 6896 O O    . HOH   E 3 .   ? 25.884 10.824  -3.630  1.00 25.12 ?  472 HOH   A O    1 
HETATM 6897 O O    . HOH   E 3 .   ? 18.117 -16.183 -8.726  1.00 37.50 ?  473 HOH   A O    1 
HETATM 6898 O O    . HOH   E 3 .   ? 35.117 7.403   12.317  1.00 50.16 ?  474 HOH   A O    1 
HETATM 6899 O O    . HOH   E 3 .   ? 12.329 1.458   17.491  1.00 39.50 ?  475 HOH   A O    1 
HETATM 6900 O O    . HOH   E 3 .   ? 15.768 -17.089 -6.980  1.00 33.67 ?  476 HOH   A O    1 
HETATM 6901 O O    . HOH   E 3 .   ? 14.043 -10.286 -10.853 1.00 29.27 ?  477 HOH   A O    1 
HETATM 6902 O O    . HOH   E 3 .   ? 17.366 -18.739 19.905  1.00 39.91 ?  478 HOH   A O    1 
HETATM 6903 O O    . HOH   E 3 .   ? 30.832 0.665   19.220  1.00 39.36 ?  479 HOH   A O    1 
HETATM 6904 O O    . HOH   E 3 .   ? 40.963 -3.943  -0.373  1.00 38.90 ?  480 HOH   A O    1 
HETATM 6905 O O    . HOH   E 3 .   ? 28.958 8.958   17.521  1.00 37.73 ?  481 HOH   A O    1 
HETATM 6906 O O    . HOH   E 3 .   ? 23.218 11.849  -4.049  1.00 19.03 ?  482 HOH   A O    1 
HETATM 6907 O O    . HOH   E 3 .   ? 16.921 -20.688 16.298  1.00 27.68 ?  483 HOH   A O    1 
HETATM 6908 O O    . HOH   E 3 .   ? 16.207 -23.387 5.824   1.00 28.36 ?  484 HOH   A O    1 
HETATM 6909 O O    . HOH   E 3 .   ? 41.753 9.342   -4.079  1.00 30.59 ?  485 HOH   A O    1 
HETATM 6910 O O    . HOH   E 3 .   ? 44.490 10.451  -1.642  1.00 32.76 ?  486 HOH   A O    1 
HETATM 6911 O O    . HOH   E 3 .   ? 20.539 -16.045 -7.414  1.00 29.28 ?  487 HOH   A O    1 
HETATM 6912 O O    . HOH   E 3 .   ? 28.608 -4.672  -12.284 1.00 32.81 ?  488 HOH   A O    1 
HETATM 6913 O O    . HOH   E 3 .   ? 31.468 -0.554  -10.545 1.00 24.97 ?  489 HOH   A O    1 
HETATM 6914 O O    . HOH   E 3 .   ? 28.625 -7.849  -15.233 1.00 51.44 ?  490 HOH   A O    1 
HETATM 6915 O O    . HOH   E 3 .   ? 23.505 -12.997 19.475  1.00 38.05 ?  491 HOH   A O    1 
HETATM 6916 O O    . HOH   E 3 .   ? 16.033 -6.711  -11.736 1.00 37.95 ?  492 HOH   A O    1 
HETATM 6917 O O    . HOH   E 3 .   ? 18.510 -23.286 1.918   1.00 44.59 ?  493 HOH   A O    1 
HETATM 6918 O O    . HOH   E 3 .   ? 14.116 -25.479 8.980   1.00 30.62 ?  494 HOH   A O    1 
HETATM 6919 O O    . HOH   E 3 .   ? 20.038 -22.406 4.074   1.00 26.68 ?  495 HOH   A O    1 
HETATM 6920 O O    . HOH   E 3 .   ? 40.513 -0.241  -7.821  1.00 33.71 ?  496 HOH   A O    1 
HETATM 6921 O O    . HOH   E 3 .   ? 39.231 2.327   7.595   1.00 29.06 ?  497 HOH   A O    1 
HETATM 6922 O O    . HOH   E 3 .   ? 30.701 5.844   -14.592 1.00 39.39 ?  498 HOH   A O    1 
HETATM 6923 O O    . HOH   E 3 .   ? 30.745 -5.710  -11.812 1.00 46.71 ?  499 HOH   A O    1 
HETATM 6924 O O    . HOH   E 3 .   ? 37.461 -6.668  7.512   1.00 23.55 ?  500 HOH   A O    1 
HETATM 6925 O O    . HOH   E 3 .   ? 23.137 -23.799 1.541   1.00 28.71 ?  501 HOH   A O    1 
HETATM 6926 O O    . HOH   E 3 .   ? 29.000 14.372  1.026   1.00 44.05 ?  502 HOH   A O    1 
HETATM 6927 O O    . HOH   E 3 .   ? 39.621 -0.021  6.591   1.00 30.10 ?  503 HOH   A O    1 
HETATM 6928 O O    . HOH   E 3 .   ? 8.126  -3.043  -5.580  1.00 44.41 ?  504 HOH   A O    1 
HETATM 6929 O O    . HOH   E 3 .   ? 38.081 13.911  6.766   1.00 39.77 ?  505 HOH   A O    1 
HETATM 6930 O O    . HOH   E 3 .   ? 22.077 -24.130 4.421   1.00 25.09 ?  506 HOH   A O    1 
HETATM 6931 O O    . HOH   E 3 .   ? 15.099 8.772   5.024   1.00 35.83 ?  507 HOH   A O    1 
HETATM 6932 O O    . HOH   E 3 .   ? 36.560 -6.576  10.226  1.00 42.17 ?  508 HOH   A O    1 
HETATM 6933 O O    . HOH   E 3 .   ? 17.465 -6.596  -14.090 1.00 34.63 ?  509 HOH   A O    1 
HETATM 6934 O O    . HOH   E 3 .   ? 24.089 8.931   -7.213  1.00 33.37 ?  510 HOH   A O    1 
HETATM 6935 O O    . HOH   E 3 .   ? 16.326 -21.250 18.829  1.00 37.13 ?  511 HOH   A O    1 
HETATM 6936 O O    . HOH   E 3 .   ? 16.033 -12.342 27.555  1.00 42.86 ?  512 HOH   A O    1 
HETATM 6937 O O    . HOH   E 3 .   ? 14.650 -22.793 19.990  1.00 34.62 ?  513 HOH   A O    1 
HETATM 6938 O O    . HOH   F 3 .   ? 29.850 -22.445 5.367   1.00 19.99 ?  201 HOH   B O    1 
HETATM 6939 O O    . HOH   F 3 .   ? 48.224 -6.911  15.558  1.00 30.06 ?  202 HOH   B O    1 
HETATM 6940 O O    . HOH   F 3 .   ? 27.864 -41.731 -15.244 1.00 32.31 ?  203 HOH   B O    1 
HETATM 6941 O O    . HOH   F 3 .   ? 41.898 -35.957 -17.350 1.00 30.49 ?  204 HOH   B O    1 
HETATM 6942 O O    . HOH   F 3 .   ? 49.417 -22.704 -19.844 1.00 47.81 ?  205 HOH   B O    1 
HETATM 6943 O O    . HOH   F 3 .   ? 47.476 -7.498  -4.090  1.00 40.09 ?  206 HOH   B O    1 
HETATM 6944 O O    . HOH   F 3 .   ? 56.397 -19.682 7.371   1.00 33.79 ?  207 HOH   B O    1 
HETATM 6945 O O    . HOH   F 3 .   ? 29.942 -26.343 3.906   1.00 25.91 ?  208 HOH   B O    1 
HETATM 6946 O O    . HOH   F 3 .   ? 59.186 -18.778 6.738   1.00 36.12 ?  209 HOH   B O    1 
HETATM 6947 O O    . HOH   F 3 .   ? 41.408 -7.798  5.465   1.00 38.44 ?  210 HOH   B O    1 
HETATM 6948 O O    . HOH   F 3 .   ? 37.982 -39.510 -0.318  1.00 41.29 ?  211 HOH   B O    1 
HETATM 6949 O O    . HOH   F 3 .   ? 27.741 -29.208 -1.957  1.00 39.57 ?  212 HOH   B O    1 
HETATM 6950 O O    . HOH   F 3 .   ? 45.262 -34.934 6.867   1.00 39.50 ?  213 HOH   B O    1 
HETATM 6951 O O    . HOH   F 3 .   ? 50.360 -3.406  7.164   1.00 34.67 ?  214 HOH   B O    1 
HETATM 6952 O O    . HOH   F 3 .   ? 54.499 -9.340  -8.794  1.00 17.91 ?  215 HOH   B O    1 
HETATM 6953 O O    . HOH   F 3 .   ? 58.299 -12.932 8.375   1.00 33.74 ?  216 HOH   B O    1 
HETATM 6954 O O    . HOH   F 3 .   ? 30.252 -41.054 -8.243  1.00 15.28 ?  217 HOH   B O    1 
HETATM 6955 O O    . HOH   F 3 .   ? 29.849 -34.225 -0.472  1.00 34.19 ?  218 HOH   B O    1 
HETATM 6956 O O    . HOH   F 3 .   ? 56.761 -30.766 -7.859  1.00 35.76 ?  219 HOH   B O    1 
HETATM 6957 O O    . HOH   F 3 .   ? 39.389 -10.953 6.042   1.00 26.52 ?  220 HOH   B O    1 
HETATM 6958 O O    . HOH   F 3 .   ? 53.022 -13.393 -20.519 1.00 39.80 ?  221 HOH   B O    1 
HETATM 6959 O O    . HOH   F 3 .   ? 57.215 -26.850 -7.699  1.00 39.12 ?  222 HOH   B O    1 
HETATM 6960 O O    . HOH   F 3 .   ? 44.474 -7.297  2.108   1.00 32.47 ?  223 HOH   B O    1 
HETATM 6961 O O    . HOH   F 3 .   ? 37.190 -19.761 -18.205 1.00 39.05 ?  224 HOH   B O    1 
HETATM 6962 O O    . HOH   F 3 .   ? 57.418 -16.204 -12.257 1.00 18.41 ?  225 HOH   B O    1 
HETATM 6963 O O    . HOH   F 3 .   ? 50.692 -6.103  0.291   1.00 29.33 ?  226 HOH   B O    1 
HETATM 6964 O O    . HOH   F 3 .   ? 57.810 -24.438 4.895   1.00 34.88 ?  227 HOH   B O    1 
HETATM 6965 O O    . HOH   F 3 .   ? 55.398 -16.416 -14.406 1.00 30.91 ?  228 HOH   B O    1 
HETATM 6966 O O    . HOH   F 3 .   ? 40.605 -16.104 14.086  1.00 24.65 ?  229 HOH   B O    1 
HETATM 6967 O O    . HOH   F 3 .   ? 41.908 -23.560 9.254   1.00 15.63 ?  230 HOH   B O    1 
HETATM 6968 O O    . HOH   F 3 .   ? 35.993 -43.252 -8.583  1.00 28.79 ?  231 HOH   B O    1 
HETATM 6969 O O    . HOH   F 3 .   ? 34.578 -36.375 -7.275  1.00 16.14 ?  232 HOH   B O    1 
HETATM 6970 O O    . HOH   F 3 .   ? 51.588 -13.876 10.870  1.00 29.32 ?  233 HOH   B O    1 
HETATM 6971 O O    . HOH   F 3 .   ? 41.433 -9.695  13.061  1.00 21.70 ?  234 HOH   B O    1 
HETATM 6972 O O    . HOH   F 3 .   ? 45.022 -43.509 -10.559 1.00 27.63 ?  235 HOH   B O    1 
HETATM 6973 O O    . HOH   F 3 .   ? 41.535 -39.168 -14.967 1.00 20.70 ?  236 HOH   B O    1 
HETATM 6974 O O    . HOH   F 3 .   ? 50.798 -12.964 -0.514  1.00 12.17 ?  237 HOH   B O    1 
HETATM 6975 O O    . HOH   F 3 .   ? 35.164 -7.988  -3.128  1.00 17.56 ?  238 HOH   B O    1 
HETATM 6976 O O    . HOH   F 3 .   ? 30.909 -28.764 4.166   1.00 22.54 ?  239 HOH   B O    1 
HETATM 6977 O O    . HOH   F 3 .   ? 46.418 -1.643  13.330  1.00 29.95 ?  240 HOH   B O    1 
HETATM 6978 O O    . HOH   F 3 .   ? 28.424 -19.664 -13.177 1.00 21.91 ?  241 HOH   B O    1 
HETATM 6979 O O    . HOH   F 3 .   ? 32.876 -43.816 -11.435 1.00 18.39 ?  242 HOH   B O    1 
HETATM 6980 O O    . HOH   F 3 .   ? 42.699 -22.897 3.784   1.00 10.86 ?  243 HOH   B O    1 
HETATM 6981 O O    . HOH   F 3 .   ? 42.615 -25.409 2.548   1.00 14.49 ?  244 HOH   B O    1 
HETATM 6982 O O    . HOH   F 3 .   ? 39.548 -11.160 0.259   1.00 16.49 ?  245 HOH   B O    1 
HETATM 6983 O O    . HOH   F 3 .   ? 34.294 -18.584 11.350  1.00 21.51 ?  246 HOH   B O    1 
HETATM 6984 O O    . HOH   F 3 .   ? 43.147 -43.280 -8.292  1.00 27.11 ?  247 HOH   B O    1 
HETATM 6985 O O    . HOH   F 3 .   ? 40.401 -12.776 -11.630 1.00 14.53 ?  248 HOH   B O    1 
HETATM 6986 O O    . HOH   F 3 .   ? 51.715 -6.513  4.452   1.00 20.55 ?  249 HOH   B O    1 
HETATM 6987 O O    . HOH   F 3 .   ? 25.473 -26.014 -1.402  1.00 30.33 ?  250 HOH   B O    1 
HETATM 6988 O O    . HOH   F 3 .   ? 48.140 -24.518 -17.824 1.00 29.16 ?  251 HOH   B O    1 
HETATM 6989 O O    . HOH   F 3 .   ? 58.155 -10.592 -4.126  1.00 21.97 ?  252 HOH   B O    1 
HETATM 6990 O O    . HOH   F 3 .   ? 57.677 -24.400 -3.913  1.00 21.25 ?  253 HOH   B O    1 
HETATM 6991 O O    . HOH   F 3 .   ? 29.770 -25.233 -10.927 1.00 15.38 ?  254 HOH   B O    1 
HETATM 6992 O O    . HOH   F 3 .   ? 48.037 -22.800 5.744   1.00 16.72 ?  255 HOH   B O    1 
HETATM 6993 O O    . HOH   F 3 .   ? 27.164 -31.827 -10.099 1.00 20.57 ?  256 HOH   B O    1 
HETATM 6994 O O    . HOH   F 3 .   ? 34.900 -24.597 13.757  1.00 29.58 ?  257 HOH   B O    1 
HETATM 6995 O O    . HOH   F 3 .   ? 44.608 -27.890 -0.829  1.00 21.60 ?  258 HOH   B O    1 
HETATM 6996 O O    . HOH   F 3 .   ? 38.502 -11.049 -2.335  1.00 18.26 ?  259 HOH   B O    1 
HETATM 6997 O O    . HOH   F 3 .   ? 30.921 -15.774 2.581   1.00 12.63 ?  260 HOH   B O    1 
HETATM 6998 O O    . HOH   F 3 .   ? 43.281 -32.374 -17.152 1.00 20.39 ?  261 HOH   B O    1 
HETATM 6999 O O    . HOH   F 3 .   ? 49.394 -28.720 -6.971  1.00 14.60 ?  262 HOH   B O    1 
HETATM 7000 O O    . HOH   F 3 .   ? 57.546 -9.235  1.423   1.00 19.51 ?  263 HOH   B O    1 
HETATM 7001 O O    . HOH   F 3 .   ? 31.857 -18.019 -14.622 1.00 31.54 ?  264 HOH   B O    1 
HETATM 7002 O O    . HOH   F 3 .   ? 56.209 -23.534 -14.824 1.00 27.00 ?  265 HOH   B O    1 
HETATM 7003 O O    . HOH   F 3 .   ? 51.040 -39.989 -8.308  1.00 27.04 ?  266 HOH   B O    1 
HETATM 7004 O O    . HOH   F 3 .   ? 46.659 -31.305 -4.858  1.00 20.24 ?  267 HOH   B O    1 
HETATM 7005 O O    . HOH   F 3 .   ? 57.032 -8.685  8.387   1.00 20.42 ?  268 HOH   B O    1 
HETATM 7006 O O    . HOH   F 3 .   ? 57.054 -12.186 12.314  1.00 39.97 ?  269 HOH   B O    1 
HETATM 7007 O O    . HOH   F 3 .   ? 34.531 -12.811 2.555   1.00 25.32 ?  270 HOH   B O    1 
HETATM 7008 O O    . HOH   F 3 .   ? 38.951 -12.091 12.392  1.00 31.98 ?  271 HOH   B O    1 
HETATM 7009 O O    . HOH   F 3 .   ? 46.885 -29.609 9.777   1.00 30.81 ?  272 HOH   B O    1 
HETATM 7010 O O    . HOH   F 3 .   ? 43.433 -15.811 -12.236 1.00 13.44 ?  273 HOH   B O    1 
HETATM 7011 O O    . HOH   F 3 .   ? 48.572 -36.522 -15.660 1.00 40.43 ?  274 HOH   B O    1 
HETATM 7012 O O    . HOH   F 3 .   ? 34.953 -33.396 -19.281 1.00 27.11 ?  275 HOH   B O    1 
HETATM 7013 O O    . HOH   F 3 .   ? 28.297 -34.336 -9.568  1.00 20.07 ?  276 HOH   B O    1 
HETATM 7014 O O    . HOH   F 3 .   ? 42.376 -9.906  9.320   1.00 20.38 ?  277 HOH   B O    1 
HETATM 7015 O O    . HOH   F 3 .   ? 42.324 -10.062 -15.032 1.00 32.05 ?  278 HOH   B O    1 
HETATM 7016 O O    . HOH   F 3 .   ? 41.207 -5.566  11.537  1.00 42.52 ?  279 HOH   B O    1 
HETATM 7017 O O    . HOH   F 3 .   ? 49.771 -0.495  10.386  1.00 30.19 ?  280 HOH   B O    1 
HETATM 7018 O O    . HOH   F 3 .   ? 45.981 -40.454 -3.704  1.00 28.42 ?  281 HOH   B O    1 
HETATM 7019 O O    . HOH   F 3 .   ? 48.467 -25.084 3.023   1.00 12.87 ?  282 HOH   B O    1 
HETATM 7020 O O    . HOH   F 3 .   ? 27.993 -22.920 -8.063  1.00 16.16 ?  283 HOH   B O    1 
HETATM 7021 O O    . HOH   F 3 .   ? 27.635 -26.756 -15.791 1.00 31.65 ?  284 HOH   B O    1 
HETATM 7022 O O    . HOH   F 3 .   ? 37.360 -35.686 7.060   1.00 31.64 ?  285 HOH   B O    1 
HETATM 7023 O O    . HOH   F 3 .   ? 40.278 -10.836 -9.604  1.00 15.82 ?  286 HOH   B O    1 
HETATM 7024 O O    . HOH   F 3 .   ? 36.867 -12.790 -1.550  1.00 24.38 ?  287 HOH   B O    1 
HETATM 7025 O O    . HOH   F 3 .   ? 44.632 -24.688 9.541   1.00 19.62 ?  288 HOH   B O    1 
HETATM 7026 O O    . HOH   F 3 .   ? 30.642 -42.274 -10.691 1.00 30.42 ?  289 HOH   B O    1 
HETATM 7027 O O    . HOH   F 3 .   ? 28.485 -30.924 -14.813 1.00 28.51 ?  290 HOH   B O    1 
HETATM 7028 O O    . HOH   F 3 .   ? 62.902 -20.222 -1.052  1.00 39.45 ?  291 HOH   B O    1 
HETATM 7029 O O    . HOH   F 3 .   ? 42.435 -34.699 3.735   1.00 25.64 ?  292 HOH   B O    1 
HETATM 7030 O O    . HOH   F 3 .   ? 47.134 -34.038 -4.663  1.00 15.92 ?  293 HOH   B O    1 
HETATM 7031 O O    . HOH   F 3 .   ? 48.771 -20.073 5.860   1.00 13.46 ?  294 HOH   B O    1 
HETATM 7032 O O    . HOH   F 3 .   ? 41.284 -24.469 15.749  1.00 40.74 ?  295 HOH   B O    1 
HETATM 7033 O O    . HOH   F 3 .   ? 33.547 -15.326 -14.037 1.00 19.78 ?  296 HOH   B O    1 
HETATM 7034 O O    . HOH   F 3 .   ? 52.582 -10.532 12.973  1.00 23.36 ?  297 HOH   B O    1 
HETATM 7035 O O    . HOH   F 3 .   ? 45.454 -33.421 -15.999 1.00 20.45 ?  298 HOH   B O    1 
HETATM 7036 O O    . HOH   F 3 .   ? 51.309 -37.622 -9.612  1.00 23.72 ?  299 HOH   B O    1 
HETATM 7037 O O    . HOH   F 3 .   ? 59.791 -15.518 8.110   1.00 31.62 ?  300 HOH   B O    1 
HETATM 7038 O O    . HOH   F 3 .   ? 44.667 -27.500 1.896   1.00 14.98 ?  301 HOH   B O    1 
HETATM 7039 O O    . HOH   F 3 .   ? 37.606 -18.237 13.053  1.00 28.20 ?  302 HOH   B O    1 
HETATM 7040 O O    . HOH   F 3 .   ? 52.691 -35.639 -8.660  1.00 27.81 ?  303 HOH   B O    1 
HETATM 7041 O O    . HOH   F 3 .   ? 35.083 -33.594 4.433   1.00 26.81 ?  304 HOH   B O    1 
HETATM 7042 O O    . HOH   F 3 .   ? 43.562 -15.408 18.257  1.00 33.86 ?  305 HOH   B O    1 
HETATM 7043 O O    . HOH   F 3 .   ? 25.996 -21.492 -3.578  1.00 15.01 ?  306 HOH   B O    1 
HETATM 7044 O O    . HOH   F 3 .   ? 50.106 -24.661 5.798   1.00 34.14 ?  307 HOH   B O    1 
HETATM 7045 O O    . HOH   F 3 .   ? 32.867 -34.634 -5.992  1.00 15.11 ?  308 HOH   B O    1 
HETATM 7046 O O    . HOH   F 3 .   ? 53.128 -16.043 -12.787 1.00 26.38 ?  309 HOH   B O    1 
HETATM 7047 O O    . HOH   F 3 .   ? 44.108 -29.367 -4.717  1.00 21.63 ?  310 HOH   B O    1 
HETATM 7048 O O    . HOH   F 3 .   ? 53.488 -30.245 4.480   1.00 20.32 ?  311 HOH   B O    1 
HETATM 7049 O O    . HOH   F 3 .   ? 42.717 -12.305 -18.612 1.00 28.04 ?  312 HOH   B O    1 
HETATM 7050 O O    . HOH   F 3 .   ? 37.872 -10.254 -10.830 1.00 16.10 ?  313 HOH   B O    1 
HETATM 7051 O O    . HOH   F 3 .   ? 52.633 -29.245 -13.072 1.00 23.49 ?  314 HOH   B O    1 
HETATM 7052 O O    . HOH   F 3 .   ? 41.772 -8.093  1.297   1.00 24.39 ?  315 HOH   B O    1 
HETATM 7053 O O    . HOH   F 3 .   ? 43.245 -21.479 10.616  1.00 14.94 ?  316 HOH   B O    1 
HETATM 7054 O O    . HOH   F 3 .   ? 62.732 -13.565 4.663   1.00 27.59 ?  317 HOH   B O    1 
HETATM 7055 O O    . HOH   F 3 .   ? 42.811 -20.272 -20.819 1.00 32.96 ?  318 HOH   B O    1 
HETATM 7056 O O    . HOH   F 3 .   ? 38.410 -12.831 7.888   1.00 17.28 ?  319 HOH   B O    1 
HETATM 7057 O O    . HOH   F 3 .   ? 33.777 -31.109 11.052  1.00 35.34 ?  320 HOH   B O    1 
HETATM 7058 O O    . HOH   F 3 .   ? 26.371 -21.042 -6.330  1.00 15.33 ?  321 HOH   B O    1 
HETATM 7059 O O    . HOH   F 3 .   ? 48.243 -32.631 -16.724 1.00 45.33 ?  322 HOH   B O    1 
HETATM 7060 O O    . HOH   F 3 .   ? 44.267 -1.791  7.596   1.00 40.90 ?  323 HOH   B O    1 
HETATM 7061 O O    . HOH   F 3 .   ? 37.240 -30.622 -21.131 1.00 29.10 ?  324 HOH   B O    1 
HETATM 7062 O O    . HOH   F 3 .   ? 28.022 -14.780 -9.426  1.00 31.56 ?  325 HOH   B O    1 
HETATM 7063 O O    . HOH   F 3 .   ? 57.669 -22.072 3.172   1.00 26.50 ?  326 HOH   B O    1 
HETATM 7064 O O    . HOH   F 3 .   ? 36.774 -12.442 4.236   1.00 17.94 ?  327 HOH   B O    1 
HETATM 7065 O O    . HOH   F 3 .   ? 38.396 -9.356  -13.360 1.00 24.75 ?  328 HOH   B O    1 
HETATM 7066 O O    . HOH   F 3 .   ? 53.703 -12.484 -22.406 1.00 32.17 ?  329 HOH   B O    1 
HETATM 7067 O O    . HOH   F 3 .   ? 39.501 -23.475 -20.371 1.00 35.08 ?  330 HOH   B O    1 
HETATM 7068 O O    . HOH   F 3 .   ? 59.985 -17.305 -10.608 1.00 34.54 ?  331 HOH   B O    1 
HETATM 7069 O O    . HOH   F 3 .   ? 43.167 -34.666 0.010   1.00 19.66 ?  332 HOH   B O    1 
HETATM 7070 O O    . HOH   F 3 .   ? 47.219 -24.556 8.079   1.00 26.34 ?  333 HOH   B O    1 
HETATM 7071 O O    . HOH   F 3 .   ? 51.666 -5.901  -7.895  1.00 50.67 ?  334 HOH   B O    1 
HETATM 7072 O O    . HOH   F 3 .   ? 45.849 -36.229 -16.273 1.00 33.28 ?  335 HOH   B O    1 
HETATM 7073 O O    . HOH   F 3 .   ? 47.540 -27.481 1.934   1.00 14.22 ?  336 HOH   B O    1 
HETATM 7074 O O    . HOH   F 3 .   ? 48.615 -11.949 -14.087 1.00 24.73 ?  337 HOH   B O    1 
HETATM 7075 O O    . HOH   F 3 .   ? 42.906 -43.483 -14.466 1.00 43.41 ?  338 HOH   B O    1 
HETATM 7076 O O    . HOH   F 3 .   ? 51.529 -32.936 -10.947 1.00 36.46 ?  339 HOH   B O    1 
HETATM 7077 O O    . HOH   F 3 .   ? 36.999 -15.075 -16.531 1.00 38.17 ?  340 HOH   B O    1 
HETATM 7078 O O    . HOH   F 3 .   ? 28.895 -42.899 -12.491 1.00 37.29 ?  341 HOH   B O    1 
HETATM 7079 O O    . HOH   F 3 .   ? 46.928 -19.957 12.298  1.00 33.59 ?  342 HOH   B O    1 
HETATM 7080 O O    . HOH   F 3 .   ? 23.329 -23.769 6.730   1.00 34.60 ?  343 HOH   B O    1 
HETATM 7081 O O    . HOH   F 3 .   ? 37.189 -45.284 -9.920  1.00 35.09 ?  344 HOH   B O    1 
HETATM 7082 O O    . HOH   F 3 .   ? 39.785 -44.297 -11.353 1.00 35.74 ?  345 HOH   B O    1 
HETATM 7083 O O    . HOH   F 3 .   ? 33.049 -14.714 0.961   1.00 17.83 ?  346 HOH   B O    1 
HETATM 7084 O O    . HOH   F 3 .   ? 38.659 -22.436 15.090  1.00 40.18 ?  347 HOH   B O    1 
HETATM 7085 O O    . HOH   F 3 .   ? 38.504 -12.236 -16.271 1.00 37.06 ?  348 HOH   B O    1 
HETATM 7086 O O    . HOH   F 3 .   ? 40.451 -43.484 -9.305  1.00 25.95 ?  349 HOH   B O    1 
HETATM 7087 O O    . HOH   F 3 .   ? 62.635 -20.129 -4.873  1.00 47.62 ?  350 HOH   B O    1 
HETATM 7088 O O    . HOH   F 3 .   ? 33.763 -9.272  -8.852  1.00 27.64 ?  351 HOH   B O    1 
HETATM 7089 O O    . HOH   F 3 .   ? 44.225 -37.366 -17.858 1.00 33.20 ?  352 HOH   B O    1 
HETATM 7090 O O    . HOH   F 3 .   ? 27.805 -26.712 -0.729  1.00 31.15 ?  353 HOH   B O    1 
HETATM 7091 O O    . HOH   F 3 .   ? 55.681 -8.289  10.879  1.00 26.29 ?  354 HOH   B O    1 
HETATM 7092 O O    . HOH   F 3 .   ? 36.137 -8.569  -9.736  1.00 33.24 ?  355 HOH   B O    1 
HETATM 7093 O O    . HOH   F 3 .   ? 34.731 -10.344 7.405   1.00 22.66 ?  356 HOH   B O    1 
HETATM 7094 O O    . HOH   F 3 .   ? 34.205 -7.923  11.418  1.00 43.06 ?  357 HOH   B O    1 
HETATM 7095 O O    . HOH   F 3 .   ? 56.614 -7.283  3.067   1.00 31.53 ?  358 HOH   B O    1 
HETATM 7096 O O    . HOH   F 3 .   ? 61.535 -19.859 1.603   1.00 33.42 ?  359 HOH   B O    1 
HETATM 7097 O O    . HOH   F 3 .   ? 27.230 -26.041 -11.450 1.00 30.71 ?  360 HOH   B O    1 
HETATM 7098 O O    . HOH   F 3 .   ? 56.968 -21.522 -16.496 1.00 40.74 ?  361 HOH   B O    1 
HETATM 7099 O O    . HOH   F 3 .   ? 40.266 -8.831  9.921   1.00 37.49 ?  362 HOH   B O    1 
HETATM 7100 O O    . HOH   F 3 .   ? 43.179 -12.668 -21.358 1.00 39.88 ?  363 HOH   B O    1 
HETATM 7101 O O    . HOH   F 3 .   ? 32.499 -23.652 14.059  1.00 41.31 ?  364 HOH   B O    1 
HETATM 7102 O O    . HOH   F 3 .   ? 40.029 -7.033  7.750   1.00 41.86 ?  365 HOH   B O    1 
HETATM 7103 O O    . HOH   F 3 .   ? 48.452 -26.551 8.769   1.00 36.44 ?  366 HOH   B O    1 
HETATM 7104 O O    . HOH   F 3 .   ? 36.326 -8.781  8.904   1.00 34.29 ?  367 HOH   B O    1 
HETATM 7105 O O    . HOH   F 3 .   ? 59.049 -10.527 9.091   1.00 38.32 ?  368 HOH   B O    1 
HETATM 7106 O O    . HOH   F 3 .   ? 54.266 -5.763  2.943   1.00 38.38 ?  369 HOH   B O    1 
HETATM 7107 O O    . HOH   F 3 .   ? 56.056 -7.827  -0.593  1.00 37.81 ?  370 HOH   B O    1 
HETATM 7108 O O    . HOH   F 3 .   ? 52.043 -12.985 13.358  1.00 33.04 ?  371 HOH   B O    1 
HETATM 7109 O O    . HOH   F 3 .   ? 40.016 -11.402 -14.051 1.00 32.02 ?  372 HOH   B O    1 
HETATM 7110 O O    . HOH   F 3 .   ? 41.883 -9.933  -17.446 1.00 48.03 ?  373 HOH   B O    1 
HETATM 7111 O O    . HOH   F 3 .   ? 63.019 -12.382 6.834   1.00 36.63 ?  374 HOH   B O    1 
HETATM 7112 O O    . HOH   F 3 .   ? 38.118 -10.631 10.001  1.00 28.85 ?  375 HOH   B O    1 
HETATM 7113 O O    . HOH   F 3 .   ? 36.556 -22.835 13.304  1.00 24.02 ?  376 HOH   B O    1 
HETATM 7114 O O    . HOH   F 3 .   ? 41.902 -6.833  -4.857  1.00 45.54 ?  377 HOH   B O    1 
HETATM 7115 O O    . HOH   F 3 .   ? 44.099 -5.629  -3.484  1.00 44.17 ?  378 HOH   B O    1 
HETATM 7116 O O    . HOH   F 3 .   ? 40.201 -7.678  3.181   1.00 35.05 ?  379 HOH   B O    1 
HETATM 7117 O O    . HOH   F 3 .   ? 39.797 -14.182 15.709  1.00 47.08 ?  380 HOH   B O    1 
HETATM 7118 O O    . HOH   F 3 .   ? 42.686 -17.021 -23.319 1.00 42.08 ?  381 HOH   B O    1 
HETATM 7119 O O    . HOH   F 3 .   ? 52.861 -29.914 7.129   1.00 24.05 ?  382 HOH   B O    1 
HETATM 7120 O O    . HOH   F 3 .   ? 60.533 -22.257 2.721   1.00 43.94 ?  383 HOH   B O    1 
HETATM 7121 O O    . HOH   F 3 .   ? 35.437 -33.738 7.130   1.00 39.21 ?  384 HOH   B O    1 
HETATM 7122 O O    . HOH   F 3 .   ? 23.944 -20.853 -7.745  1.00 26.81 ?  385 HOH   B O    1 
HETATM 7123 O O    . HOH   F 3 .   ? 40.947 -9.893  15.807  1.00 43.54 ?  386 HOH   B O    1 
HETATM 7124 O O    . HOH   F 3 .   ? 46.950 -5.330  2.857   1.00 39.24 ?  387 HOH   B O    1 
HETATM 7125 O O    . HOH   F 3 .   ? 35.356 -20.329 13.327  1.00 28.93 ?  388 HOH   B O    1 
HETATM 7126 O O    . HOH   F 3 .   ? 25.821 -18.835 -12.107 1.00 36.04 ?  389 HOH   B O    1 
HETATM 7127 O O    . HOH   F 3 .   ? 40.703 -6.636  -0.891  1.00 23.38 ?  390 HOH   B O    1 
HETATM 7128 O O    . HOH   F 3 .   ? 44.119 -31.767 -3.885  1.00 28.62 ?  391 HOH   B O    1 
HETATM 7129 O O    . HOH   F 3 .   ? 28.053 -27.141 2.186   1.00 31.99 ?  392 HOH   B O    1 
HETATM 7130 O O    . HOH   F 3 .   ? 26.639 -27.964 -13.499 1.00 31.66 ?  393 HOH   B O    1 
HETATM 7131 O O    . HOH   F 3 .   ? 45.872 -20.355 15.127  1.00 54.37 ?  394 HOH   B O    1 
HETATM 7132 O O    . HOH   F 3 .   ? 34.459 -33.476 9.575   1.00 32.12 ?  395 HOH   B O    1 
HETATM 7133 O O    . HOH   F 3 .   ? 50.652 -30.880 8.699   1.00 28.86 ?  396 HOH   B O    1 
HETATM 7134 O O    . HOH   F 3 .   ? 24.651 -20.765 -10.453 1.00 37.40 ?  397 HOH   B O    1 
HETATM 7135 O O    . HOH   F 3 .   ? 26.880 -30.641 -12.789 1.00 28.41 ?  398 HOH   B O    1 
HETATM 7136 O O    . HOH   F 3 .   ? 57.708 -6.471  -2.424  1.00 35.10 ?  399 HOH   B O    1 
HETATM 7137 O O    . HOH   F 3 .   ? 40.933 -11.862 -22.478 1.00 42.94 ?  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   A VAL   A 3   ? 0.4777 0.4682 0.5565 -0.0100 -0.0132 0.0512  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.4906 0.4687 0.5710 -0.0111 -0.0227 0.0739  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.4742 0.4658 0.5472 -0.0108 -0.0122 0.0503  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.4869 0.4669 0.5578 -0.0129 -0.0211 0.0725  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.4575 0.4535 0.5049 -0.0150 -0.0150 0.0499  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.4686 0.4541 0.5106 -0.0191 -0.0262 0.0704  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.4596 0.4548 0.5104 -0.0129 -0.0164 0.0525  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.4709 0.4550 0.5208 -0.0162 -0.0274 0.0739  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.4846 0.4736 0.5720 -0.0086 -0.0073 0.0496  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.4983 0.4755 0.5814 -0.0097 -0.0139 0.0722  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.4881 0.4763 0.5806 -0.0079 -0.0050 0.0488  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.5021 0.4784 0.5891 -0.0087 -0.0111 0.0706  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.4880 0.4761 0.5798 -0.0077 -0.0050 0.0497  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.5026 0.4784 0.5875 -0.0085 -0.0102 0.0732  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.4360 0.4381 0.4492 -0.0213 -0.0150 0.0459  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.4453 0.4387 0.4405 -0.0288 -0.0281 0.0627  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.4132 0.4209 0.3903 -0.0286 -0.0126 0.0404  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.4210 0.4218 0.3644 -0.0391 -0.0276 0.0528  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.3854 0.4022 0.3596 -0.0379 -0.0013 0.0278  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.3973 0.4086 0.3227 -0.0476 -0.0145 0.0349  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.3869 0.4020 0.3537 -0.0361 -0.0005 0.0313  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.3992 0.4076 0.3090 -0.0457 -0.0123 0.0388  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.4158 0.4212 0.3612 -0.0270 -0.0210 0.0447  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.4184 0.4165 0.3265 -0.0408 -0.0412 0.0565  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.4165 0.4194 0.3343 -0.0263 -0.0276 0.0497  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.4142 0.4092 0.2876 -0.0431 -0.0514 0.0634  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.4173 0.4169 0.3225 -0.0259 -0.0290 0.0514  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.4131 0.4036 0.2673 -0.0454 -0.0526 0.0652  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.4156 0.4199 0.3271 -0.0255 -0.0308 0.0532  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.4112 0.4074 0.2790 -0.0427 -0.0563 0.0685  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.3556 0.3807 0.3340 -0.0492 0.0078  0.0109  5   SER   A N   
60   N N   B SER   A 5   ? 0.3715 0.3928 0.2945 -0.0578 -0.0057 0.0121  5   SER   A N   
61   C CA  A SER   A 5   ? 0.3263 0.3591 0.3100 -0.0568 0.0183  -0.0051 5   SER   A CA  
62   C CA  B SER   A 5   ? 0.3453 0.3782 0.2736 -0.0631 0.0025  -0.0116 5   SER   A CA  
63   C C   A SER   A 5   ? 0.2936 0.3300 0.2738 -0.0582 0.0295  -0.0126 5   SER   A C   
64   C C   B SER   A 5   ? 0.3142 0.3560 0.2397 -0.0607 0.0137  -0.0224 5   SER   A C   
65   O O   A SER   A 5   ? 0.2996 0.3377 0.2807 -0.0486 0.0301  -0.0198 5   SER   A O   
66   O O   B SER   A 5   ? 0.3167 0.3584 0.2392 -0.0562 0.0123  -0.0317 5   SER   A O   
67   C CB  A SER   A 5   ? 0.3305 0.3652 0.3204 -0.0604 0.0191  -0.0091 5   SER   A CB  
68   C CB  B SER   A 5   ? 0.3511 0.3852 0.2870 -0.0672 0.0024  -0.0205 5   SER   A CB  
69   O OG  A SER   A 5   ? 0.3340 0.3688 0.3260 -0.0622 0.0237  -0.0081 5   SER   A OG  
70   O OG  B SER   A 5   ? 0.3552 0.3897 0.2928 -0.0685 0.0052  -0.0233 5   SER   A OG  
81   N N   A PHE   A 6   ? 0.2530 0.2903 0.2307 -0.0699 0.0421  -0.0081 6   PHE   A N   
82   N N   B PHE   A 6   ? 0.2797 0.3296 0.2118 -0.0652 0.0263  -0.0214 6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.2204 0.2534 0.1936 -0.0766 0.0506  0.0046  6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.2549 0.3087 0.2049 -0.0665 0.0404  -0.0087 6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.2091 0.2452 0.1877 -0.0793 0.0643  0.0022  6   PHE   A C   
86   C C   B PHE   A 6   ? 0.2486 0.3130 0.2372 -0.0733 0.0499  -0.0046 6   PHE   A C   
87   O O   A PHE   A 6   ? 0.2095 0.2509 0.2029 -0.0771 0.0673  0.0037  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.2472 0.3165 0.2638 -0.0787 0.0473  0.0025  6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.2037 0.2301 0.1756 -0.0733 0.0444  0.0166  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.2406 0.2851 0.1842 -0.0552 0.0408  -0.0044 6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.1920 0.2171 0.1755 -0.0676 0.0330  0.0234  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.2298 0.2669 0.1807 -0.0447 0.0391  0.0059  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.1886 0.2127 0.1803 -0.0637 0.0256  0.0235  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.2293 0.2607 0.1885 -0.0386 0.0330  0.0092  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.1920 0.2163 0.1846 -0.0589 0.0273  0.0181  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.2290 0.2625 0.1832 -0.0352 0.0421  0.0078  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.1861 0.2097 0.1842 -0.0627 0.0220  0.0259  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.2297 0.2577 0.1980 -0.0353 0.0304  0.0138  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.1903 0.2102 0.1921 -0.0589 0.0256  0.0163  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.2291 0.2587 0.1922 -0.0307 0.0419  0.0104  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.1882 0.2071 0.1891 -0.0631 0.0242  0.0216  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.2309 0.2565 0.1980 -0.0339 0.0337  0.0134  6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.1996 0.2355 0.1877 -0.0762 0.0643  -0.0006 7   SER   A N   
122  N N   B SER   A 7   ? 0.2417 0.3170 0.2587 -0.0709 0.0553  -0.0097 7   SER   A N   
123  C CA  A SER   A 7   ? 0.1996 0.2320 0.2100 -0.0638 0.0608  -0.0074 7   SER   A CA  
124  C CA  B SER   A 7   ? 0.2430 0.3236 0.2845 -0.0611 0.0608  -0.0174 7   SER   A CA  
125  C C   A SER   A 7   ? 0.1858 0.2051 0.2003 -0.0613 0.0616  -0.0008 7   SER   A C   
126  C C   B SER   A 7   ? 0.2337 0.3121 0.2802 -0.0575 0.0626  -0.0172 7   SER   A C   
127  O O   A SER   A 7   ? 0.1905 0.1981 0.1978 -0.0690 0.0641  0.0051  7   SER   A O   
128  O O   B SER   A 7   ? 0.2309 0.3156 0.2780 -0.0548 0.0613  -0.0165 7   SER   A O   
129  C CB  A SER   A 7   ? 0.2158 0.2525 0.2416 -0.0509 0.0588  -0.0139 7   SER   A CB  
130  C CB  B SER   A 7   ? 0.2581 0.3439 0.3132 -0.0524 0.0618  -0.0260 7   SER   A CB  
131  O OG  A SER   A 7   ? 0.2304 0.2701 0.2739 -0.0388 0.0619  -0.0179 7   SER   A OG  
132  O OG  B SER   A 7   ? 0.2714 0.3612 0.3416 -0.0449 0.0636  -0.0265 7   SER   A OG  
143  N N   A GLY   A 8   ? 0.1671 0.1867 0.1957 -0.0556 0.0565  -0.0017 8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2277 0.2959 0.2838 -0.0530 0.0623  -0.0192 8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.1597 0.1730 0.1987 -0.0445 0.0412  -0.0003 8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.2227 0.2808 0.2859 -0.0402 0.0592  -0.0201 8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.1505 0.1694 0.2002 -0.0328 0.0261  0.0116  8   GLY   A C   
148  C C   B GLY   A 8   ? 0.2049 0.2567 0.2724 -0.0351 0.0560  -0.0147 8   GLY   A C   
149  O O   A GLY   A 8   ? 0.1531 0.1811 0.2199 -0.0160 0.0094  0.0002  8   GLY   A O   
150  O O   B GLY   A 8   ? 0.2058 0.2588 0.2900 -0.0286 0.0540  -0.0185 8   GLY   A O   
157  N N   A TYR   A 9   ? 0.1401 0.1547 0.1907 -0.0296 0.0244  0.0192  9   TYR   A N   
158  N N   B TYR   A 9   ? 0.1854 0.2294 0.2492 -0.0335 0.0538  0.0000  9   TYR   A N   
159  C CA  A TYR   A 9   ? 0.1362 0.1496 0.1803 -0.0216 0.0223  0.0227  9   TYR   A CA  
160  C CA  B TYR   A 9   ? 0.1685 0.2033 0.2242 -0.0277 0.0381  0.0103  9   TYR   A CA  
161  C C   A TYR   A 9   ? 0.1336 0.1422 0.1729 -0.0093 0.0245  0.0336  9   TYR   A C   
162  C C   B TYR   A 9   ? 0.1678 0.1827 0.2213 -0.0298 0.0393  0.0244  9   TYR   A C   
163  O O   A TYR   A 9   ? 0.1378 0.1434 0.1724 -0.0016 0.0213  0.0290  9   TYR   A O   
164  O O   B TYR   A 9   ? 0.1902 0.1832 0.2357 -0.0316 0.0246  0.0355  9   TYR   A O   
165  C CB  A TYR   A 9   ? 0.1382 0.1602 0.1915 -0.0169 0.0117  0.0111  9   TYR   A CB  
166  C CB  B TYR   A 9   ? 0.1497 0.1992 0.2132 -0.0168 0.0224  0.0028  9   TYR   A CB  
167  C CG  A TYR   A 9   ? 0.1422 0.1673 0.1950 -0.0132 0.0182  0.0014  9   TYR   A CG  
168  C CG  B TYR   A 9   ? 0.1404 0.1970 0.1838 -0.0102 0.0217  0.0056  9   TYR   A CG  
169  C CD1 A TYR   A 9   ? 0.1453 0.1711 0.2009 -0.0185 0.0201  -0.0025 9   TYR   A CD1 
170  C CD1 B TYR   A 9   ? 0.1433 0.1944 0.1819 -0.0117 0.0225  0.0082  9   TYR   A CD1 
171  C CD2 A TYR   A 9   ? 0.1437 0.1614 0.1906 -0.0136 0.0169  0.0104  9   TYR   A CD2 
172  C CD2 B TYR   A 9   ? 0.1384 0.1966 0.1746 -0.0076 0.0153  0.0142  9   TYR   A CD2 
173  C CE1 A TYR   A 9   ? 0.1466 0.1726 0.1980 -0.0225 0.0251  -0.0017 9   TYR   A CE1 
174  C CE1 B TYR   A 9   ? 0.1486 0.2005 0.1836 -0.0170 0.0214  0.0108  9   TYR   A CE1 
175  C CE2 A TYR   A 9   ? 0.1425 0.1633 0.1877 -0.0161 0.0233  0.0083  9   TYR   A CE2 
176  C CE2 B TYR   A 9   ? 0.1390 0.1987 0.1701 -0.0111 0.0160  0.0118  9   TYR   A CE2 
177  C CZ  A TYR   A 9   ? 0.1416 0.1692 0.1928 -0.0288 0.0278  0.0038  9   TYR   A CZ  
178  C CZ  B TYR   A 9   ? 0.1472 0.2024 0.1851 -0.0254 0.0242  0.0103  9   TYR   A CZ  
179  O OH  A TYR   A 9   ? 0.1401 0.1747 0.1903 -0.0380 0.0304  -0.0014 9   TYR   A OH  
180  O OH  B TYR   A 9   ? 0.1658 0.2111 0.1982 -0.0336 0.0357  0.0035  9   TYR   A OH  
199  N N   A LEU   A 10  ? 0.1279 0.1413 0.1879 -0.0079 0.0199  0.0314  10  LEU   A N   
200  N N   B LEU   A 10  ? 0.1434 0.1617 0.2161 -0.0249 0.0235  0.0335  10  LEU   A N   
201  C CA  A LEU   A 10  ? 0.1205 0.1435 0.1830 -0.0015 0.0134  0.0433  10  LEU   A CA  
202  C CA  B LEU   A 10  ? 0.1341 0.1591 0.2152 -0.0265 0.0240  0.0430  10  LEU   A CA  
203  C C   A LEU   A 10  ? 0.1139 0.1352 0.1735 -0.0002 0.0034  0.0396  10  LEU   A C   
204  C C   B LEU   A 10  ? 0.1222 0.1472 0.2080 -0.0188 0.0190  0.0431  10  LEU   A C   
205  O O   A LEU   A 10  ? 0.1175 0.1314 0.1862 -0.0007 0.0162  0.0413  10  LEU   A O   
206  O O   B LEU   A 10  ? 0.1206 0.1473 0.2211 -0.0213 0.0377  0.0427  10  LEU   A O   
207  C CB  A LEU   A 10  ? 0.1190 0.1521 0.2077 -0.0059 0.0088  0.0622  10  LEU   A CB  
208  C CB  B LEU   A 10  ? 0.1348 0.1875 0.2435 -0.0271 0.0182  0.0372  10  LEU   A CB  
209  C CG  A LEU   A 10  ? 0.1205 0.1661 0.2327 -0.0083 -0.0043 0.0614  10  LEU   A CG  
210  C CG  B LEU   A 10  ? 0.1535 0.2127 0.2740 -0.0205 0.0132  0.0321  10  LEU   A CG  
211  C CD1 A LEU   A 10  ? 0.1302 0.1673 0.2461 -0.0088 -0.0085 0.0639  10  LEU   A CD1 
212  C CD1 B LEU   A 10  ? 0.1573 0.2195 0.2834 -0.0179 0.0223  0.0226  10  LEU   A CD1 
213  C CD2 A LEU   A 10  ? 0.1254 0.1834 0.2422 -0.0106 -0.0027 0.0511  10  LEU   A CD2 
214  C CD2 B LEU   A 10  ? 0.1661 0.2212 0.2783 -0.0223 0.0168  0.0399  10  LEU   A CD2 
237  N N   A LYS   A 11  ? 0.1122 0.1315 0.1679 -0.0006 0.0089  0.0329  11  LYS   A N   
238  N N   B LYS   A 11  ? 0.1207 0.1404 0.1975 -0.0143 0.0251  0.0370  11  LYS   A N   
239  C CA  A LYS   A 11  ? 0.1083 0.1240 0.1642 -0.0064 0.0115  0.0280  11  LYS   A CA  
240  C CA  B LYS   A 11  ? 0.1260 0.1374 0.1914 -0.0166 0.0197  0.0321  11  LYS   A CA  
241  C C   A LYS   A 11  ? 0.1087 0.1188 0.1623 -0.0112 0.0194  0.0252  11  LYS   A C   
242  C C   B LYS   A 11  ? 0.1238 0.1410 0.1848 -0.0130 0.0213  0.0246  11  LYS   A C   
243  O O   A LYS   A 11  ? 0.1077 0.1241 0.1836 -0.0173 0.0215  0.0083  11  LYS   A O   
244  O O   B LYS   A 11  ? 0.1210 0.1481 0.2195 -0.0195 0.0250  0.0197  11  LYS   A O   
245  C CB  A LYS   A 11  ? 0.1138 0.1198 0.1733 -0.0064 0.0119  0.0206  11  LYS   A CB  
246  C CB  B LYS   A 11  ? 0.1269 0.1458 0.1874 -0.0098 0.0120  0.0290  11  LYS   A CB  
247  C CG  A LYS   A 11  ? 0.1219 0.1173 0.1755 -0.0024 0.0188  0.0222  11  LYS   A CG  
248  C CG  B LYS   A 11  ? 0.1374 0.1512 0.1959 -0.0075 0.0107  0.0310  11  LYS   A CG  
249  C CD  A LYS   A 11  ? 0.1289 0.1283 0.1726 0.0050  0.0211  0.0263  11  LYS   A CD  
250  C CD  B LYS   A 11  ? 0.1462 0.1535 0.2036 0.0011  0.0129  0.0399  11  LYS   A CD  
251  C CE  A LYS   A 11  ? 0.1280 0.1283 0.1636 0.0060  0.0221  0.0339  11  LYS   A CE  
252  C CE  B LYS   A 11  ? 0.1535 0.1517 0.2095 -0.0009 0.0062  0.0471  11  LYS   A CE  
253  N NZ  A LYS   A 11  ? 0.1267 0.1336 0.1682 0.0075  0.0195  0.0276  11  LYS   A NZ  
254  N NZ  B LYS   A 11  ? 0.1582 0.1520 0.2181 -0.0027 0.0020  0.0349  11  LYS   A NZ  
281  N N   A LEU   A 12  ? 0.1077 0.1279 0.1619 -0.0092 0.0088  0.0176  12  LEU   A N   
282  N N   B LEU   A 12  ? 0.1274 0.1374 0.1641 -0.0237 0.0220  0.0223  12  LEU   A N   
283  C CA  A LEU   A 12  ? 0.1134 0.1349 0.1581 -0.0090 0.0082  0.0225  12  LEU   A CA  
284  C CA  B LEU   A 12  ? 0.1328 0.1334 0.1772 -0.0219 0.0179  0.0228  12  LEU   A CA  
285  C C   A LEU   A 12  ? 0.1151 0.1333 0.1455 -0.0075 0.0110  0.0240  12  LEU   A C   
286  C C   B LEU   A 12  ? 0.1373 0.1304 0.1835 -0.0231 0.0032  0.0191  12  LEU   A C   
287  O O   A LEU   A 12  ? 0.1259 0.1285 0.1351 -0.0059 0.0055  0.0209  12  LEU   A O   
288  O O   B LEU   A 12  ? 0.1429 0.1303 0.1906 -0.0188 0.0021  0.0153  12  LEU   A O   
289  C CB  A LEU   A 12  ? 0.1195 0.1422 0.1626 -0.0128 0.0071  0.0282  12  LEU   A CB  
290  C CB  B LEU   A 12  ? 0.1440 0.1286 0.2001 -0.0149 0.0168  0.0332  12  LEU   A CB  
291  C CG  A LEU   A 12  ? 0.1271 0.1436 0.1749 -0.0143 0.0135  0.0255  12  LEU   A CG  
292  C CG  B LEU   A 12  ? 0.1554 0.1333 0.2250 -0.0012 0.0166  0.0397  12  LEU   A CG  
293  C CD1 A LEU   A 12  ? 0.1321 0.1460 0.1822 -0.0111 0.0195  0.0213  12  LEU   A CD1 
294  C CD1 B LEU   A 12  ? 0.1670 0.1376 0.2353 0.0051  0.0193  0.0463  12  LEU   A CD1 
295  C CD2 A LEU   A 12  ? 0.1311 0.1464 0.1866 -0.0127 0.0105  0.0213  12  LEU   A CD2 
296  C CD2 B LEU   A 12  ? 0.1557 0.1370 0.2510 0.0123  0.0051  0.0329  12  LEU   A CD2 
319  N N   A THR   A 13  ? 0.1113 0.1294 0.1504 -0.0059 0.0144  0.0214  13  THR   A N   
320  N N   B THR   A 13  ? 0.1357 0.1283 0.1957 -0.0236 0.0011  0.0168  13  THR   A N   
321  C CA  A THR   A 13  ? 0.1179 0.1282 0.1548 -0.0061 0.0179  0.0206  13  THR   A CA  
322  C CA  B THR   A 13  ? 0.1378 0.1322 0.1952 -0.0180 0.0040  0.0135  13  THR   A CA  
323  C C   A THR   A 13  ? 0.1251 0.1294 0.1599 -0.0131 0.0205  0.0167  13  THR   A C   
324  C C   B THR   A 13  ? 0.1333 0.1248 0.2019 -0.0113 -0.0002 0.0176  13  THR   A C   
325  O O   A THR   A 13  ? 0.1325 0.1293 0.1697 -0.0072 0.0195  0.0112  13  THR   A O   
326  O O   B THR   A 13  ? 0.1311 0.1298 0.1886 -0.0032 -0.0041 0.0216  13  THR   A O   
327  C CB  A THR   A 13  ? 0.1240 0.1416 0.1660 0.0006  0.0241  0.0232  13  THR   A CB  
328  C CB  B THR   A 13  ? 0.1433 0.1416 0.2123 -0.0177 0.0068  0.0082  13  THR   A CB  
329  O OG1 A THR   A 13  ? 0.1171 0.1431 0.1757 -0.0038 0.0302  0.0271  13  THR   A OG1 
330  O OG1 B THR   A 13  ? 0.1424 0.1275 0.2296 -0.0202 -0.0037 0.0105  13  THR   A OG1 
331  C CG2 A THR   A 13  ? 0.1351 0.1552 0.1815 0.0029  0.0241  0.0131  13  THR   A CG2 
332  C CG2 B THR   A 13  ? 0.1504 0.1607 0.2340 -0.0171 0.0102  -0.0015 13  THR   A CG2 
347  N N   A ASP   A 14  ? 0.1271 0.1341 0.1662 -0.0174 0.0164  0.0282  14  ASP   A N   
348  N N   B ASP   A 14  ? 0.1453 0.1255 0.2111 -0.0099 0.0022  0.0168  14  ASP   A N   
349  C CA  A ASP   A 14  ? 0.1265 0.1368 0.1740 -0.0169 0.0155  0.0437  14  ASP   A CA  
350  C CA  B ASP   A 14  ? 0.1508 0.1393 0.2286 -0.0072 0.0035  0.0336  14  ASP   A CA  
351  C C   A ASP   A 14  ? 0.1196 0.1355 0.1511 -0.0094 0.0081  0.0450  14  ASP   A C   
352  C C   B ASP   A 14  ? 0.1480 0.1417 0.1959 -0.0169 0.0002  0.0232  14  ASP   A C   
353  O O   A ASP   A 14  ? 0.1194 0.1473 0.1639 -0.0138 -0.0020 0.0496  14  ASP   A O   
354  O O   B ASP   A 14  ? 0.1555 0.1536 0.1956 -0.0169 0.0010  0.0211  14  ASP   A O   
355  C CB  A ASP   A 14  ? 0.1493 0.1434 0.2205 -0.0249 0.0019  0.0515  14  ASP   A CB  
356  C CB  B ASP   A 14  ? 0.1677 0.1721 0.2944 -0.0027 0.0030  0.0567  14  ASP   A CB  
357  C CG  A ASP   A 14  ? 0.1677 0.1638 0.2664 -0.0306 -0.0046 0.0577  14  ASP   A CG  
358  C CG  B ASP   A 14  ? 0.1975 0.2106 0.3703 -0.0090 0.0061  0.0757  14  ASP   A CG  
359  O OD1 A ASP   A 14  ? 0.1752 0.1772 0.2784 -0.0251 -0.0089 0.0548  14  ASP   A OD1 
360  O OD1 B ASP   A 14  ? 0.2106 0.2221 0.4004 -0.0181 0.0141  0.0774  14  ASP   A OD1 
361  O OD2 A ASP   A 14  ? 0.1836 0.1732 0.2811 -0.0304 -0.0079 0.0693  14  ASP   A OD2 
362  O OD2 B ASP   A 14  ? 0.2168 0.2337 0.4064 -0.0067 0.0058  0.0824  14  ASP   A OD2 
371  N N   A ASN   A 15  ? 0.1224 0.1273 0.1469 -0.0088 0.0153  0.0387  15  ASN   A N   
372  N N   B ASN   A 15  ? 0.1372 0.1254 0.1752 -0.0200 0.0020  0.0094  15  ASN   A N   
373  C CA  A ASN   A 15  ? 0.1245 0.1276 0.1506 -0.0031 0.0076  0.0297  15  ASN   A CA  
374  C CA  B ASN   A 15  ? 0.1345 0.1249 0.1771 -0.0183 0.0062  0.0001  15  ASN   A CA  
375  C C   A ASN   A 15  ? 0.1222 0.1218 0.1592 -0.0084 0.0146  0.0242  15  ASN   A C   
376  C C   B ASN   A 15  ? 0.1307 0.1240 0.1942 -0.0151 0.0109  0.0002  15  ASN   A C   
377  O O   A ASN   A 15  ? 0.1223 0.1284 0.1825 -0.0046 0.0117  0.0088  15  ASN   A O   
378  O O   B ASN   A 15  ? 0.1318 0.1247 0.2222 -0.0079 0.0006  -0.0009 15  ASN   A O   
379  C CB  A ASN   A 15  ? 0.1284 0.1340 0.1534 0.0021  0.0084  0.0312  15  ASN   A CB  
380  C CB  B ASN   A 15  ? 0.1321 0.1251 0.1610 -0.0135 0.0132  -0.0033 15  ASN   A CB  
381  C CG  A ASN   A 15  ? 0.1313 0.1435 0.1500 0.0017  0.0204  0.0207  15  ASN   A CG  
382  C CG  B ASN   A 15  ? 0.1305 0.1334 0.1677 -0.0118 0.0141  0.0019  15  ASN   A CG  
383  O OD1 A ASN   A 15  ? 0.1273 0.1347 0.1624 -0.0011 0.0395  0.0170  15  ASN   A OD1 
384  O OD1 B ASN   A 15  ? 0.1298 0.1393 0.1760 -0.0186 0.0081  -0.0073 15  ASN   A OD1 
385  N ND2 A ASN   A 15  ? 0.1385 0.1607 0.1453 -0.0072 0.0161  0.0258  15  ASN   A ND2 
386  N ND2 B ASN   A 15  ? 0.1376 0.1494 0.1692 -0.0226 0.0074  0.0195  15  ASN   A ND2 
399  N N   A VAL   A 16  ? 0.1248 0.1159 0.1530 -0.0112 0.0063  0.0324  16  VAL   A N   
400  N N   B VAL   A 16  ? 0.1304 0.1182 0.1835 -0.0061 0.0137  0.0006  16  VAL   A N   
401  C CA  A VAL   A 16  ? 0.1233 0.1200 0.1471 -0.0112 0.0122  0.0282  16  VAL   A CA  
402  C CA  B VAL   A 16  ? 0.1321 0.1191 0.1867 -0.0117 0.0148  -0.0021 16  VAL   A CA  
403  C C   A VAL   A 16  ? 0.1158 0.1276 0.1515 -0.0066 0.0139  0.0281  16  VAL   A C   
404  C C   B VAL   A 16  ? 0.1277 0.1185 0.1833 -0.0185 0.0108  0.0126  16  VAL   A C   
405  O O   A VAL   A 16  ? 0.1134 0.1319 0.1639 -0.0067 0.0124  0.0291  16  VAL   A O   
406  O O   B VAL   A 16  ? 0.1282 0.1283 0.1957 -0.0211 0.0186  0.0095  16  VAL   A O   
407  C CB  A VAL   A 16  ? 0.1290 0.1191 0.1365 -0.0053 0.0199  0.0357  16  VAL   A CB  
408  C CB  B VAL   A 16  ? 0.1487 0.1360 0.1955 -0.0038 0.0243  -0.0011 16  VAL   A CB  
409  C CG1 A VAL   A 16  ? 0.1330 0.1215 0.1410 -0.0056 0.0128  0.0406  16  VAL   A CG1 
410  C CG1 B VAL   A 16  ? 0.1636 0.1380 0.2042 -0.0056 0.0099  -0.0042 16  VAL   A CG1 
411  C CG2 A VAL   A 16  ? 0.1357 0.1355 0.1423 0.0014  0.0215  0.0321  16  VAL   A CG2 
412  C CG2 B VAL   A 16  ? 0.1533 0.1489 0.1968 -0.0086 0.0287  -0.0107 16  VAL   A CG2 
431  N N   A TYR   A 17  ? 0.1165 0.1276 0.1478 -0.0048 0.0257  0.0200  17  TYR   A N   
432  N N   B TYR   A 17  ? 0.1292 0.1168 0.1778 -0.0191 0.0160  0.0129  17  TYR   A N   
433  C CA  A TYR   A 17  ? 0.1203 0.1346 0.1538 -0.0106 0.0206  0.0266  17  TYR   A CA  
434  C CA  B TYR   A 17  ? 0.1295 0.1257 0.1671 -0.0191 0.0307  0.0223  17  TYR   A CA  
435  C C   A TYR   A 17  ? 0.1136 0.1327 0.1638 -0.0068 0.0184  0.0395  17  TYR   A C   
436  C C   B TYR   A 17  ? 0.1298 0.1245 0.1779 -0.0094 0.0273  0.0177  17  TYR   A C   
437  O O   A TYR   A 17  ? 0.1141 0.1266 0.1532 -0.0097 0.0215  0.0333  17  TYR   A O   
438  O O   B TYR   A 17  ? 0.1292 0.1092 0.1813 -0.0166 0.0343  0.0084  17  TYR   A O   
439  C CB  A TYR   A 17  ? 0.1424 0.1429 0.1607 -0.0248 0.0097  0.0183  17  TYR   A CB  
440  C CB  B TYR   A 17  ? 0.1431 0.1386 0.1594 -0.0246 0.0236  0.0225  17  TYR   A CB  
441  C CG  A TYR   A 17  ? 0.1721 0.1546 0.1696 -0.0312 -0.0016 0.0162  17  TYR   A CG  
442  C CG  B TYR   A 17  ? 0.1641 0.1555 0.1628 -0.0311 0.0078  0.0292  17  TYR   A CG  
443  C CD1 A TYR   A 17  ? 0.1901 0.1586 0.1779 -0.0274 -0.0046 0.0177  17  TYR   A CD1 
444  C CD1 B TYR   A 17  ? 0.1850 0.1643 0.1653 -0.0228 0.0010  0.0322  17  TYR   A CD1 
445  C CD2 A TYR   A 17  ? 0.1852 0.1651 0.1735 -0.0382 -0.0048 0.0162  17  TYR   A CD2 
446  C CD2 B TYR   A 17  ? 0.1777 0.1644 0.1644 -0.0451 0.0104  0.0346  17  TYR   A CD2 
447  C CE1 A TYR   A 17  ? 0.2017 0.1642 0.1802 -0.0310 -0.0124 0.0207  17  TYR   A CE1 
448  C CE1 B TYR   A 17  ? 0.2029 0.1692 0.1736 -0.0332 -0.0091 0.0354  17  TYR   A CE1 
449  C CE2 A TYR   A 17  ? 0.1992 0.1700 0.1775 -0.0392 -0.0100 0.0106  17  TYR   A CE2 
450  C CE2 B TYR   A 17  ? 0.2000 0.1716 0.1708 -0.0456 0.0004  0.0237  17  TYR   A CE2 
451  C CZ  A TYR   A 17  ? 0.2094 0.1705 0.1808 -0.0353 -0.0116 0.0201  17  TYR   A CZ  
452  C CZ  B TYR   A 17  ? 0.2149 0.1696 0.1724 -0.0427 -0.0095 0.0373  17  TYR   A CZ  
453  O OH  A TYR   A 17  ? 0.2200 0.1779 0.1802 -0.0359 -0.0028 0.0244  17  TYR   A OH  
454  O OH  B TYR   A 17  ? 0.2336 0.1752 0.1738 -0.0432 -0.0099 0.0429  17  TYR   A OH  
473  N N   A ILE   A 18  ? 0.1057 0.1390 0.1785 -0.0070 0.0209  0.0518  18  ILE   A N   
474  N N   B ILE   A 18  ? 0.1266 0.1438 0.1902 -0.0107 0.0168  0.0304  18  ILE   A N   
475  C CA  A ILE   A 18  ? 0.1114 0.1436 0.1936 -0.0134 0.0295  0.0533  18  ILE   A CA  
476  C CA  B ILE   A 18  ? 0.1306 0.1594 0.2009 -0.0155 0.0074  0.0350  18  ILE   A CA  
477  C C   A ILE   A 18  ? 0.1178 0.1443 0.2114 -0.0151 0.0370  0.0490  18  ILE   A C   
478  C C   B ILE   A 18  ? 0.1281 0.1669 0.2073 -0.0140 0.0038  0.0394  18  ILE   A C   
479  O O   A ILE   A 18  ? 0.1171 0.1498 0.2159 -0.0139 0.0507  0.0506  18  ILE   A O   
480  O O   B ILE   A 18  ? 0.1340 0.1690 0.2266 -0.0219 0.0149  0.0410  18  ILE   A O   
481  C CB  A ILE   A 18  ? 0.1247 0.1552 0.1840 -0.0083 0.0244  0.0726  18  ILE   A CB  
482  C CB  B ILE   A 18  ? 0.1394 0.1658 0.1931 -0.0136 0.0032  0.0484  18  ILE   A CB  
483  C CG1 A ILE   A 18  ? 0.1415 0.1705 0.1909 -0.0079 0.0128  0.0753  18  ILE   A CG1 
484  C CG1 B ILE   A 18  ? 0.1600 0.1727 0.1977 -0.0092 -0.0057 0.0576  18  ILE   A CG1 
485  C CG2 A ILE   A 18  ? 0.1253 0.1597 0.1915 -0.0085 0.0163  0.0717  18  ILE   A CG2 
486  C CG2 B ILE   A 18  ? 0.1265 0.1582 0.1998 -0.0010 -0.0033 0.0443  18  ILE   A CG2 
487  C CD1 A ILE   A 18  ? 0.1554 0.1892 0.2192 -0.0068 0.0041  0.0682  18  ILE   A CD1 
488  C CD1 B ILE   A 18  ? 0.1775 0.1808 0.2154 -0.0035 -0.0101 0.0647  18  ILE   A CD1 
511  N N   A LYS   A 19  ? 0.1192 0.1381 0.2241 -0.0135 0.0429  0.0448  19  LYS   A N   
512  N N   B LYS   A 19  ? 0.1350 0.1769 0.2060 -0.0094 0.0109  0.0401  19  LYS   A N   
513  C CA  A LYS   A 19  ? 0.1235 0.1409 0.2257 -0.0015 0.0467  0.0491  19  LYS   A CA  
514  C CA  B LYS   A 19  ? 0.1590 0.1979 0.2125 -0.0013 0.0199  0.0409  19  LYS   A CA  
515  C C   A LYS   A 19  ? 0.1129 0.1349 0.2318 0.0012  0.0354  0.0545  19  LYS   A C   
516  C C   B LYS   A 19  ? 0.1538 0.2054 0.2148 0.0068  0.0272  0.0502  19  LYS   A C   
517  O O   A LYS   A 19  ? 0.1053 0.1252 0.2362 0.0032  0.0225  0.0533  19  LYS   A O   
518  O O   B LYS   A 19  ? 0.1481 0.2014 0.2142 -0.0018 0.0279  0.0510  19  LYS   A O   
519  C CB  A LYS   A 19  ? 0.1375 0.1537 0.2248 -0.0008 0.0550  0.0415  19  LYS   A CB  
520  C CB  B LYS   A 19  ? 0.1815 0.2079 0.2130 -0.0097 0.0247  0.0385  19  LYS   A CB  
521  C CG  A LYS   A 19  ? 0.1639 0.1773 0.2309 0.0067  0.0574  0.0256  19  LYS   A CG  
522  C CG  B LYS   A 19  ? 0.2088 0.2223 0.2296 -0.0045 0.0146  0.0309  19  LYS   A CG  
523  C CD  A LYS   A 19  ? 0.1889 0.1947 0.2357 0.0064  0.0620  0.0174  19  LYS   A CD  
524  C CD  B LYS   A 19  ? 0.2343 0.2381 0.2396 0.0002  0.0120  0.0213  19  LYS   A CD  
525  C CE  A LYS   A 19  ? 0.2050 0.2054 0.2494 0.0040  0.0635  0.0068  19  LYS   A CE  
526  C CE  B LYS   A 19  ? 0.2482 0.2478 0.2527 -0.0037 0.0122  0.0109  19  LYS   A CE  
527  N NZ  A LYS   A 19  ? 0.2133 0.2120 0.2519 -0.0022 0.0676  -0.0017 19  LYS   A NZ  
528  N NZ  B LYS   A 19  ? 0.2573 0.2528 0.2563 -0.0130 0.0180  0.0078  19  LYS   A NZ  
555  N N   A ASN   A 20  ? 0.1189 0.1403 0.2371 -0.0014 0.0309  0.0639  20  ASN   A N   
556  N N   B ASN   A 20  ? 0.1657 0.2182 0.2277 0.0213  0.0363  0.0556  20  ASN   A N   
557  C CA  A ASN   A 20  ? 0.1379 0.1559 0.2363 0.0138  0.0302  0.0600  20  ASN   A CA  
558  C CA  B ASN   A 20  ? 0.1769 0.2280 0.2375 0.0401  0.0486  0.0571  20  ASN   A CA  
559  C C   A ASN   A 20  ? 0.1532 0.1612 0.2267 0.0054  0.0309  0.0495  20  ASN   A C   
560  C C   B ASN   A 20  ? 0.1869 0.2205 0.2225 0.0331  0.0470  0.0524  20  ASN   A C   
561  O O   A ASN   A 20  ? 0.1711 0.1728 0.2270 -0.0005 0.0240  0.0535  20  ASN   A O   
562  O O   B ASN   A 20  ? 0.1986 0.2202 0.2233 0.0285  0.0468  0.0441  20  ASN   A O   
563  C CB  A ASN   A 20  ? 0.1475 0.1687 0.2472 0.0242  0.0280  0.0681  20  ASN   A CB  
564  C CB  B ASN   A 20  ? 0.1867 0.2431 0.2749 0.0573  0.0618  0.0650  20  ASN   A CB  
565  C CG  A ASN   A 20  ? 0.1595 0.1770 0.2686 0.0318  0.0275  0.0810  20  ASN   A CG  
566  C CG  B ASN   A 20  ? 0.2027 0.2542 0.3137 0.0686  0.0721  0.0715  20  ASN   A CG  
567  O OD1 A ASN   A 20  ? 0.1818 0.1863 0.2888 0.0318  0.0517  0.0835  20  ASN   A OD1 
568  O OD1 B ASN   A 20  ? 0.2148 0.2655 0.3502 0.0741  0.0845  0.0680  20  ASN   A OD1 
569  N ND2 A ASN   A 20  ? 0.1649 0.1768 0.2734 0.0284  0.0128  0.0789  20  ASN   A ND2 
570  N ND2 B ASN   A 20  ? 0.2117 0.2484 0.3122 0.0670  0.0712  0.0780  20  ASN   A ND2 
583  N N   A ALA   A 21  ? 0.1535 0.1609 0.2140 -0.0037 0.0308  0.0439  21  ALA   A N   
584  N N   B ALA   A 21  ? 0.1927 0.2205 0.2237 0.0300  0.0410  0.0473  21  ALA   A N   
585  C CA  A ALA   A 21  ? 0.1543 0.1593 0.1981 -0.0097 0.0341  0.0423  21  ALA   A CA  
586  C CA  B ALA   A 21  ? 0.2045 0.2210 0.2330 0.0281  0.0269  0.0418  21  ALA   A CA  
587  C C   A ALA   A 21  ? 0.1469 0.1594 0.1855 -0.0095 0.0460  0.0399  21  ALA   A C   
588  C C   B ALA   A 21  ? 0.2081 0.2189 0.2351 0.0183  0.0330  0.0388  21  ALA   A C   
589  O O   A ALA   A 21  ? 0.1494 0.1667 0.1891 -0.0057 0.0386  0.0268  21  ALA   A O   
590  O O   B ALA   A 21  ? 0.2114 0.2185 0.2296 0.0105  0.0374  0.0439  21  ALA   A O   
591  C CB  A ALA   A 21  ? 0.1666 0.1631 0.1995 -0.0206 0.0175  0.0493  21  ALA   A CB  
592  C CB  B ALA   A 21  ? 0.2199 0.2288 0.2451 0.0254  0.0115  0.0434  21  ALA   A CB  
603  N N   A ASP   A 22  ? 0.1491 0.1603 0.1962 -0.0113 0.0446  0.0388  22  ASP   A N   
604  N N   B ASP   A 22  ? 0.2111 0.2179 0.2458 0.0143  0.0335  0.0269  22  ASP   A N   
605  C CA  A ASP   A 22  ? 0.1544 0.1630 0.2017 -0.0097 0.0381  0.0332  22  ASP   A CA  
606  C CA  B ASP   A 22  ? 0.2164 0.2149 0.2642 0.0061  0.0378  0.0161  22  ASP   A CA  
607  C C   A ASP   A 22  ? 0.1458 0.1613 0.1839 -0.0106 0.0482  0.0428  22  ASP   A C   
608  C C   B ASP   A 22  ? 0.2070 0.2131 0.2447 -0.0001 0.0384  0.0180  22  ASP   A C   
609  O O   A ASP   A 22  ? 0.1422 0.1657 0.1886 -0.0111 0.0488  0.0518  22  ASP   A O   
610  O O   B ASP   A 22  ? 0.2072 0.2180 0.2492 0.0090  0.0415  0.0227  22  ASP   A O   
611  C CB  A ASP   A 22  ? 0.1742 0.1736 0.2362 -0.0078 0.0343  0.0150  22  ASP   A CB  
612  C CB  B ASP   A 22  ? 0.2306 0.2134 0.2982 0.0059  0.0349  0.0085  22  ASP   A CB  
613  C CG  A ASP   A 22  ? 0.1910 0.1827 0.2724 -0.0156 0.0250  0.0072  22  ASP   A CG  
614  C CG  B ASP   A 22  ? 0.2389 0.2119 0.3362 -0.0004 0.0378  0.0067  22  ASP   A CG  
615  O OD1 A ASP   A 22  ? 0.1995 0.1921 0.2822 -0.0214 0.0168  0.0109  22  ASP   A OD1 
616  O OD1 B ASP   A 22  ? 0.2370 0.2001 0.3276 -0.0120 0.0392  0.0041  22  ASP   A OD1 
617  O OD2 A ASP   A 22  ? 0.1973 0.1862 0.3054 -0.0181 0.0240  -0.0050 22  ASP   A OD2 
618  O OD2 B ASP   A 22  ? 0.2450 0.2207 0.3735 0.0034  0.0463  0.0048  22  ASP   A OD2 
627  N N   A ILE   A 23  ? 0.1529 0.1630 0.1853 -0.0094 0.0540  0.0334  23  ILE   A N   
628  N N   B ILE   A 23  ? 0.2080 0.2079 0.2375 -0.0064 0.0374  0.0186  23  ILE   A N   
629  C CA  A ILE   A 23  ? 0.1576 0.1596 0.1868 -0.0077 0.0546  0.0301  23  ILE   A CA  
630  C CA  B ILE   A 23  ? 0.2031 0.2069 0.2209 -0.0152 0.0360  0.0098  23  ILE   A CA  
631  C C   A ILE   A 23  ? 0.1600 0.1602 0.1940 -0.0042 0.0657  0.0250  23  ILE   A C   
632  C C   B ILE   A 23  ? 0.1981 0.2089 0.2231 -0.0224 0.0447  -0.0007 23  ILE   A C   
633  O O   A ILE   A 23  ? 0.1677 0.1555 0.1998 0.0011  0.0615  0.0157  23  ILE   A O   
634  O O   B ILE   A 23  ? 0.1951 0.2053 0.2221 -0.0201 0.0464  -0.0091 23  ILE   A O   
635  C CB  A ILE   A 23  ? 0.1650 0.1588 0.1802 -0.0072 0.0488  0.0253  23  ILE   A CB  
636  C CB  B ILE   A 23  ? 0.2142 0.2028 0.2052 -0.0175 0.0286  0.0070  23  ILE   A CB  
637  C CG1 A ILE   A 23  ? 0.1635 0.1653 0.1798 -0.0013 0.0380  0.0088  23  ILE   A CG1 
638  C CG1 B ILE   A 23  ? 0.2109 0.2017 0.1942 -0.0198 0.0250  -0.0028 23  ILE   A CG1 
639  C CG2 A ILE   A 23  ? 0.1724 0.1578 0.1874 -0.0093 0.0533  0.0276  23  ILE   A CG2 
640  C CG2 B ILE   A 23  ? 0.2228 0.2018 0.2126 -0.0169 0.0342  0.0080  23  ILE   A CG2 
641  C CD1 A ILE   A 23  ? 0.1607 0.1639 0.1716 -0.0028 0.0167  0.0024  23  ILE   A CD1 
642  C CD1 B ILE   A 23  ? 0.2105 0.1943 0.1832 -0.0216 0.0201  -0.0085 23  ILE   A CD1 
665  N N   A VAL   A 24  ? 0.1661 0.1615 0.1979 -0.0055 0.0615  0.0249  24  VAL   A N   
666  N N   B VAL   A 24  ? 0.2053 0.2193 0.2419 -0.0333 0.0453  -0.0026 24  VAL   A N   
667  C CA  A VAL   A 24  ? 0.1772 0.1664 0.2096 -0.0069 0.0509  0.0228  24  VAL   A CA  
668  C CA  B VAL   A 24  ? 0.2233 0.2322 0.2653 -0.0349 0.0429  -0.0004 24  VAL   A CA  
669  C C   A VAL   A 24  ? 0.1830 0.1740 0.2113 -0.0123 0.0510  0.0177  24  VAL   A C   
670  C C   B VAL   A 24  ? 0.2284 0.2480 0.2654 -0.0296 0.0564  -0.0191 24  VAL   A C   
671  O O   A VAL   A 24  ? 0.1885 0.1767 0.2072 -0.0086 0.0472  0.0134  24  VAL   A O   
672  O O   B VAL   A 24  ? 0.2322 0.2509 0.2718 -0.0235 0.0605  -0.0337 24  VAL   A O   
673  C CB  A VAL   A 24  ? 0.1796 0.1701 0.2266 -0.0043 0.0512  0.0287  24  VAL   A CB  
674  C CB  B VAL   A 24  ? 0.2334 0.2395 0.2912 -0.0375 0.0358  0.0185  24  VAL   A CB  
675  C CG1 A VAL   A 24  ? 0.1741 0.1714 0.2283 -0.0015 0.0509  0.0243  24  VAL   A CG1 
676  C CG1 B VAL   A 24  ? 0.2387 0.2433 0.3144 -0.0372 0.0197  0.0174  24  VAL   A CG1 
677  C CG2 A VAL   A 24  ? 0.1918 0.1753 0.2363 -0.0041 0.0584  0.0367  24  VAL   A CG2 
678  C CG2 B VAL   A 24  ? 0.2425 0.2462 0.3010 -0.0342 0.0399  0.0261  24  VAL   A CG2 
697  N N   A GLU   A 25  ? 0.1855 0.1881 0.2209 -0.0159 0.0603  0.0160  25  GLU   A N   
698  N N   B GLU   A 25  ? 0.2355 0.2654 0.2707 -0.0239 0.0747  -0.0188 25  GLU   A N   
699  C CA  A GLU   A 25  ? 0.1986 0.2098 0.2324 -0.0173 0.0659  0.0199  25  GLU   A CA  
700  C CA  B GLU   A 25  ? 0.2522 0.2849 0.2879 -0.0223 0.0908  -0.0153 25  GLU   A CA  
701  C C   A GLU   A 25  ? 0.1838 0.2113 0.2173 -0.0247 0.0694  0.0228  25  GLU   A C   
702  C C   B GLU   A 25  ? 0.2468 0.2813 0.2612 -0.0250 0.0961  -0.0169 25  GLU   A C   
703  O O   A GLU   A 25  ? 0.1811 0.2156 0.2177 -0.0202 0.0734  0.0190  25  GLU   A O   
704  O O   B GLU   A 25  ? 0.2505 0.2873 0.2662 -0.0191 0.1038  -0.0227 25  GLU   A O   
705  C CB  A GLU   A 25  ? 0.2224 0.2296 0.2630 -0.0135 0.0701  0.0218  25  GLU   A CB  
706  C CB  B GLU   A 25  ? 0.2741 0.3039 0.3298 -0.0223 0.1031  -0.0061 25  GLU   A CB  
707  C CG  A GLU   A 25  ? 0.2444 0.2465 0.2976 -0.0152 0.0731  0.0233  25  GLU   A CG  
708  C CG  B GLU   A 25  ? 0.2954 0.3213 0.3700 -0.0243 0.1108  -0.0006 25  GLU   A CG  
709  C CD  A GLU   A 25  ? 0.2604 0.2614 0.3318 -0.0213 0.0765  0.0265  25  GLU   A CD  
710  C CD  B GLU   A 25  ? 0.3124 0.3345 0.4106 -0.0284 0.1110  0.0045  25  GLU   A CD  
711  O OE1 A GLU   A 25  ? 0.2645 0.2660 0.3436 -0.0241 0.0732  0.0212  25  GLU   A OE1 
712  O OE1 B GLU   A 25  ? 0.3193 0.3397 0.4206 -0.0254 0.1104  0.0015  25  GLU   A OE1 
713  O OE2 A GLU   A 25  ? 0.2694 0.2663 0.3499 -0.0221 0.0772  0.0280  25  GLU   A OE2 
714  O OE2 B GLU   A 25  ? 0.3203 0.3392 0.4237 -0.0320 0.1111  0.0113  25  GLU   A OE2 
727  N N   A GLU   A 26  ? 0.1762 0.2068 0.2105 -0.0382 0.0715  0.0264  26  GLU   A N   
728  N N   B GLU   A 26  ? 0.2400 0.2667 0.2428 -0.0311 0.0880  -0.0272 26  GLU   A N   
729  C CA  A GLU   A 26  ? 0.1789 0.2086 0.2150 -0.0501 0.0625  0.0325  26  GLU   A CA  
730  C CA  B GLU   A 26  ? 0.2421 0.2499 0.2257 -0.0399 0.0801  -0.0245 26  GLU   A CA  
731  C C   A GLU   A 26  ? 0.1734 0.2047 0.2045 -0.0589 0.0647  0.0226  26  GLU   A C   
732  C C   B GLU   A 26  ? 0.2387 0.2462 0.2078 -0.0439 0.0800  -0.0460 26  GLU   A C   
733  O O   A GLU   A 26  ? 0.1722 0.2053 0.2026 -0.0598 0.0540  0.0207  26  GLU   A O   
734  O O   B GLU   A 26  ? 0.2375 0.2460 0.2035 -0.0426 0.0736  -0.0525 26  GLU   A O   
735  C CB  A GLU   A 26  ? 0.1930 0.2101 0.2309 -0.0532 0.0455  0.0473  26  GLU   A CB  
736  C CB  B GLU   A 26  ? 0.2560 0.2403 0.2363 -0.0414 0.0568  -0.0137 26  GLU   A CB  
737  C CG  A GLU   A 26  ? 0.2116 0.2233 0.2495 -0.0527 0.0320  0.0525  26  GLU   A CG  
738  C CG  B GLU   A 26  ? 0.2624 0.2191 0.2406 -0.0452 0.0549  -0.0051 26  GLU   A CG  
739  C CD  A GLU   A 26  ? 0.2227 0.2297 0.2595 -0.0540 0.0274  0.0564  26  GLU   A CD  
740  C CD  B GLU   A 26  ? 0.2562 0.1982 0.2341 -0.0540 0.0666  0.0031  26  GLU   A CD  
741  O OE1 A GLU   A 26  ? 0.2298 0.2453 0.2746 -0.0404 0.0435  0.0509  26  GLU   A OE1 
742  O OE1 B GLU   A 26  ? 0.2496 0.1770 0.2108 -0.0619 0.0844  0.0025  26  GLU   A OE1 
743  O OE2 A GLU   A 26  ? 0.2286 0.2287 0.2601 -0.0579 0.0169  0.0536  26  GLU   A OE2 
744  O OE2 B GLU   A 26  ? 0.2572 0.2129 0.2417 -0.0341 0.0627  0.0036  26  GLU   A OE2 
757  N N   A ALA   A 27  ? 0.1752 0.1981 0.1914 -0.0650 0.0690  0.0117  27  ALA   A N   
758  N N   B ALA   A 27  ? 0.2390 0.2422 0.2039 -0.0514 0.0811  -0.0576 27  ALA   A N   
759  C CA  A ALA   A 27  ? 0.1969 0.2061 0.1820 -0.0681 0.0714  0.0005  27  ALA   A CA  
760  C CA  B ALA   A 27  ? 0.2476 0.2428 0.1994 -0.0604 0.0912  -0.0568 27  ALA   A CA  
761  C C   A ALA   A 27  ? 0.2296 0.2229 0.1957 -0.0708 0.0740  -0.0255 27  ALA   A C   
762  C C   B ALA   A 27  ? 0.2740 0.2564 0.2142 -0.0649 0.0914  -0.0669 27  ALA   A C   
763  O O   A ALA   A 27  ? 0.2291 0.2156 0.1896 -0.0803 0.0635  -0.0326 27  ALA   A O   
764  O O   B ALA   A 27  ? 0.2815 0.2575 0.2255 -0.0680 0.0821  -0.0570 27  ALA   A O   
765  C CB  A ALA   A 27  ? 0.1954 0.2027 0.1831 -0.0659 0.0627  0.0013  27  ALA   A CB  
766  C CB  B ALA   A 27  ? 0.2389 0.2385 0.2070 -0.0574 0.0911  -0.0498 27  ALA   A CB  
777  N N   A LYS   A 28  ? 0.2685 0.2545 0.2251 -0.0623 0.0746  -0.0443 28  LYS   A N   
778  N N   B LYS   A 28  ? 0.3008 0.2782 0.2358 -0.0624 0.0904  -0.0836 28  LYS   A N   
779  C CA  A LYS   A 28  ? 0.3115 0.2952 0.2686 -0.0509 0.0714  -0.0586 28  LYS   A CA  
780  C CA  B LYS   A 28  ? 0.3345 0.3117 0.2720 -0.0543 0.0839  -0.0850 28  LYS   A CA  
781  C C   A LYS   A 28  ? 0.3355 0.3244 0.2676 -0.0532 0.0842  -0.0603 28  LYS   A C   
782  C C   B LYS   A 28  ? 0.3476 0.3329 0.2667 -0.0549 0.0907  -0.0744 28  LYS   A C   
783  O O   A LYS   A 28  ? 0.3416 0.3320 0.2917 -0.0497 0.0722  -0.0555 28  LYS   A O   
784  O O   B LYS   A 28  ? 0.3552 0.3411 0.2945 -0.0515 0.0751  -0.0680 28  LYS   A O   
785  C CB  A LYS   A 28  ? 0.3269 0.3082 0.3091 -0.0370 0.0616  -0.0653 28  LYS   A CB  
786  C CB  B LYS   A 28  ? 0.3513 0.3270 0.3115 -0.0442 0.0776  -0.0898 28  LYS   A CB  
787  C CG  A LYS   A 28  ? 0.3391 0.3202 0.3507 -0.0268 0.0526  -0.0639 28  LYS   A CG  
788  C CG  B LYS   A 28  ? 0.3652 0.3411 0.3535 -0.0364 0.0724  -0.0873 28  LYS   A CG  
789  C CD  A LYS   A 28  ? 0.3487 0.3324 0.3928 -0.0198 0.0439  -0.0613 28  LYS   A CD  
790  C CD  B LYS   A 28  ? 0.3759 0.3556 0.3999 -0.0314 0.0658  -0.0833 28  LYS   A CD  
791  C CE  A LYS   A 28  ? 0.3545 0.3404 0.4246 -0.0161 0.0370  -0.0593 28  LYS   A CE  
792  C CE  B LYS   A 28  ? 0.3816 0.3642 0.4353 -0.0290 0.0598  -0.0814 28  LYS   A CE  
793  N NZ  A LYS   A 28  ? 0.3577 0.3443 0.4429 -0.0143 0.0334  -0.0574 28  LYS   A NZ  
794  N NZ  B LYS   A 28  ? 0.3847 0.3683 0.4561 -0.0278 0.0571  -0.0787 28  LYS   A NZ  
821  N N   . LYS   A 29  ? 0.3500 0.3448 0.2548 -0.0616 0.1089  -0.0591 29  LYS   A N   
822  C CA  . LYS   A 29  ? 0.3754 0.3784 0.2780 -0.0733 0.1258  -0.0397 29  LYS   A CA  
823  C C   . LYS   A 29  ? 0.3666 0.3697 0.2447 -0.0887 0.1157  -0.0359 29  LYS   A C   
824  O O   . LYS   A 29  ? 0.3729 0.3758 0.2617 -0.0809 0.1085  -0.0399 29  LYS   A O   
825  C CB  . LYS   A 29  ? 0.4042 0.4181 0.3498 -0.0668 0.1445  -0.0291 29  LYS   A CB  
826  C CG  . LYS   A 29  ? 0.4297 0.4488 0.4349 -0.0604 0.1509  -0.0223 29  LYS   A CG  
827  C CD  . LYS   A 29  ? 0.4531 0.4750 0.5146 -0.0542 0.1541  -0.0202 29  LYS   A CD  
828  C CE  . LYS   A 29  ? 0.4712 0.4951 0.5754 -0.0503 0.1554  -0.0169 29  LYS   A CE  
829  N NZ  . LYS   A 29  ? 0.4826 0.5079 0.6113 -0.0492 0.1553  -0.0171 29  LYS   A NZ  
844  N N   . VAL   A 30  ? 0.3514 0.3514 0.2136 -0.1106 0.1076  -0.0284 30  VAL   A N   
845  C CA  . VAL   A 30  ? 0.3452 0.3345 0.2027 -0.1251 0.0887  -0.0141 30  VAL   A CA  
846  C C   . VAL   A 30  ? 0.3481 0.3128 0.1646 -0.1234 0.0712  -0.0084 30  VAL   A C   
847  O O   . VAL   A 30  ? 0.3556 0.3184 0.1559 -0.1230 0.0693  -0.0008 30  VAL   A O   
848  C CB  . VAL   A 30  ? 0.3378 0.3365 0.2457 -0.1380 0.0663  -0.0168 30  VAL   A CB  
849  C CG1 . VAL   A 30  ? 0.3404 0.3397 0.2635 -0.1383 0.0474  -0.0214 30  VAL   A CG1 
850  C CG2 . VAL   A 30  ? 0.3336 0.3364 0.2682 -0.1425 0.0751  -0.0144 30  VAL   A CG2 
860  N N   A LYS   A 31  ? 0.3443 0.3012 0.1621 -0.1191 0.0593  -0.0153 31  LYS   A N   
861  N N   B LYS   A 31  ? 0.3410 0.2954 0.1407 -0.1274 0.0622  -0.0201 31  LYS   A N   
862  C CA  A LYS   A 31  ? 0.3484 0.2980 0.1845 -0.1036 0.0376  -0.0178 31  LYS   A CA  
863  C CA  B LYS   A 31  ? 0.3492 0.2930 0.1586 -0.1122 0.0376  -0.0241 31  LYS   A CA  
864  C C   A LYS   A 31  ? 0.3341 0.2770 0.1385 -0.0999 0.0334  -0.0032 31  LYS   A C   
865  C C   B LYS   A 31  ? 0.3356 0.2740 0.1216 -0.1040 0.0341  -0.0008 31  LYS   A C   
866  O O   A LYS   A 31  ? 0.3351 0.2790 0.1471 -0.0960 0.0301  0.0047  31  LYS   A O   
867  O O   B LYS   A 31  ? 0.3381 0.2759 0.1355 -0.0993 0.0291  0.0129  31  LYS   A O   
868  C CB  A LYS   A 31  ? 0.3697 0.3183 0.2752 -0.0901 0.0203  -0.0257 31  LYS   A CB  
869  C CB  B LYS   A 31  ? 0.3762 0.3141 0.2613 -0.1006 0.0155  -0.0354 31  LYS   A CB  
870  C CG  A LYS   A 31  ? 0.3903 0.3388 0.3660 -0.0738 0.0034  -0.0282 31  LYS   A CG  
871  C CG  B LYS   A 31  ? 0.4038 0.3371 0.3699 -0.0832 -0.0056 -0.0372 31  LYS   A CG  
872  C CD  A LYS   A 31  ? 0.4062 0.3546 0.4357 -0.0613 -0.0107 -0.0299 31  LYS   A CD  
873  C CD  B LYS   A 31  ? 0.4249 0.3549 0.4554 -0.0704 -0.0240 -0.0381 31  LYS   A CD  
874  C CE  A LYS   A 31  ? 0.4172 0.3657 0.4800 -0.0529 -0.0204 -0.0315 31  LYS   A CE  
875  C CE  B LYS   A 31  ? 0.4388 0.3673 0.5090 -0.0624 -0.0388 -0.0411 31  LYS   A CE  
876  N NZ  A LYS   A 31  ? 0.4230 0.3715 0.5028 -0.0492 -0.0245 -0.0317 31  LYS   A NZ  
877  N NZ  B LYS   A 31  ? 0.4451 0.3744 0.5358 -0.0593 -0.0467 -0.0426 31  LYS   A NZ  
904  N N   . PRO   A 32  ? 0.3039 0.2470 0.0997 -0.0916 0.0302  -0.0045 32  PRO   A N   
905  C CA  . PRO   A 32  ? 0.2987 0.2290 0.1220 -0.0841 0.0151  0.0063  32  PRO   A CA  
906  C C   . PRO   A 32  ? 0.2888 0.2131 0.1257 -0.0680 0.0034  0.0193  32  PRO   A C   
907  O O   . PRO   A 32  ? 0.2819 0.2066 0.1384 -0.0698 -0.0120 0.0240  32  PRO   A O   
908  C CB  . PRO   A 32  ? 0.2920 0.2380 0.1393 -0.0799 0.0159  0.0002  32  PRO   A CB  
909  C CG  . PRO   A 32  ? 0.2894 0.2433 0.1041 -0.0787 0.0165  0.0025  32  PRO   A CG  
910  C CD  . PRO   A 32  ? 0.2967 0.2434 0.0965 -0.0868 0.0241  0.0048  32  PRO   A CD  
918  N N   . THR   A 33  ? 0.2864 0.2096 0.1346 -0.0578 -0.0021 0.0289  33  THR   A N   
919  C CA  . THR   A 33  ? 0.2778 0.2115 0.1408 -0.0468 -0.0234 0.0343  33  THR   A CA  
920  C C   . THR   A 33  ? 0.2358 0.1895 0.1331 -0.0441 -0.0282 0.0247  33  THR   A C   
921  O O   . THR   A 33  ? 0.2247 0.1941 0.1369 -0.0340 -0.0410 0.0225  33  THR   A O   
922  C CB  . THR   A 33  ? 0.3038 0.2297 0.1558 -0.0350 -0.0337 0.0490  33  THR   A CB  
923  O OG1 . THR   A 33  ? 0.3260 0.2394 0.1862 -0.0224 -0.0266 0.0647  33  THR   A OG1 
924  C CG2 . THR   A 33  ? 0.3078 0.2362 0.1752 -0.0287 -0.0411 0.0452  33  THR   A CG2 
932  N N   . VAL   A 34  ? 0.2048 0.1767 0.1118 -0.0434 -0.0227 0.0216  34  VAL   A N   
933  C CA  . VAL   A 34  ? 0.1872 0.1633 0.1048 -0.0319 -0.0112 0.0202  34  VAL   A CA  
934  C C   . VAL   A 34  ? 0.1716 0.1575 0.1064 -0.0293 -0.0023 0.0138  34  VAL   A C   
935  O O   . VAL   A 34  ? 0.1751 0.1581 0.1267 -0.0375 0.0018  0.0197  34  VAL   A O   
936  C CB  . VAL   A 34  ? 0.1826 0.1590 0.1202 -0.0277 -0.0076 0.0033  34  VAL   A CB  
937  C CG1 . VAL   A 34  ? 0.1874 0.1709 0.1243 -0.0196 0.0005  -0.0016 34  VAL   A CG1 
938  C CG2 . VAL   A 34  ? 0.1868 0.1701 0.1411 -0.0172 -0.0182 0.0040  34  VAL   A CG2 
948  N N   . VAL   A 35  ? 0.1560 0.1470 0.1024 -0.0302 -0.0051 0.0066  35  VAL   A N   
949  C CA  . VAL   A 35  ? 0.1435 0.1440 0.1077 -0.0266 0.0013  0.0041  35  VAL   A CA  
950  C C   . VAL   A 35  ? 0.1294 0.1335 0.1004 -0.0196 -0.0000 0.0060  35  VAL   A C   
951  O O   . VAL   A 35  ? 0.1262 0.1394 0.1193 -0.0232 0.0083  0.0014  35  VAL   A O   
952  C CB  . VAL   A 35  ? 0.1474 0.1565 0.1255 -0.0180 0.0156  -0.0049 35  VAL   A CB  
953  C CG1 . VAL   A 35  ? 0.1578 0.1611 0.1364 -0.0115 0.0062  -0.0166 35  VAL   A CG1 
954  C CG2 . VAL   A 35  ? 0.1508 0.1568 0.1495 -0.0140 0.0245  -0.0171 35  VAL   A CG2 
964  N N   . VAL   A 36  ? 0.1214 0.1351 0.0931 -0.0229 0.0082  0.0053  36  VAL   A N   
965  C CA  . VAL   A 36  ? 0.1132 0.1201 0.1063 -0.0139 0.0048  0.0034  36  VAL   A CA  
966  C C   . VAL   A 36  ? 0.1125 0.1203 0.1269 -0.0146 0.0118  -0.0002 36  VAL   A C   
967  O O   . VAL   A 36  ? 0.1180 0.1186 0.1472 -0.0060 0.0206  0.0014  36  VAL   A O   
968  C CB  . VAL   A 36  ? 0.1178 0.1094 0.1149 -0.0147 0.0029  0.0086  36  VAL   A CB  
969  C CG1 . VAL   A 36  ? 0.1236 0.1136 0.1259 -0.0198 0.0018  -0.0001 36  VAL   A CG1 
970  C CG2 . VAL   A 36  ? 0.1248 0.1179 0.1432 -0.0111 -0.0011 0.0051  36  VAL   A CG2 
980  N N   . ASN   A 37  ? 0.1085 0.1126 0.1146 -0.0113 0.0071  0.0114  37  ASN   A N   
981  C CA  . ASN   A 37  ? 0.1060 0.1092 0.1112 -0.0030 0.0048  0.0047  37  ASN   A CA  
982  C C   . ASN   A 37  ? 0.1057 0.1058 0.1211 -0.0040 0.0157  0.0148  37  ASN   A C   
983  O O   . ASN   A 37  ? 0.1206 0.1209 0.1092 0.0036  0.0077  0.0096  37  ASN   A O   
984  C CB  . ASN   A 37  ? 0.1103 0.1088 0.1260 -0.0019 -0.0006 -0.0003 37  ASN   A CB  
985  C CG  . ASN   A 37  ? 0.1101 0.1084 0.1398 -0.0013 -0.0011 0.0067  37  ASN   A CG  
986  O OD1 . ASN   A 37  ? 0.1134 0.1101 0.1501 0.0004  -0.0011 0.0054  37  ASN   A OD1 
987  N ND2 . ASN   A 37  ? 0.1111 0.1164 0.1354 -0.0077 -0.0042 0.0159  37  ASN   A ND2 
994  N N   A ALA   A 38  ? 0.1072 0.1084 0.1128 -0.0010 0.0088  -0.0005 38  ALA   A N   
995  N N   B ALA   A 38  ? 0.1073 0.1222 0.1291 -0.0021 0.0119  -0.0011 38  ALA   A N   
996  C CA  A ALA   A 38  ? 0.1127 0.1034 0.1061 -0.0017 0.0007  -0.0044 38  ALA   A CA  
997  C CA  B ALA   A 38  ? 0.1154 0.1332 0.1401 -0.0096 -0.0004 0.0054  38  ALA   A CA  
998  C C   A ALA   A 38  ? 0.1073 0.1082 0.1042 0.0019  -0.0066 -0.0073 38  ALA   A C   
999  C C   B ALA   A 38  ? 0.1095 0.1286 0.1278 -0.0006 -0.0105 0.0030  38  ALA   A C   
1000 O O   A ALA   A 38  ? 0.1091 0.1058 0.1202 0.0015  -0.0119 -0.0077 38  ALA   A O   
1001 O O   B ALA   A 38  ? 0.1115 0.1226 0.1472 -0.0002 -0.0184 0.0037  38  ALA   A O   
1002 C CB  A ALA   A 38  ? 0.1164 0.1095 0.1124 -0.0086 -0.0040 -0.0035 38  ALA   A CB  
1003 C CB  B ALA   A 38  ? 0.1219 0.1524 0.1626 -0.0134 -0.0141 0.0001  38  ALA   A CB  
1014 N N   A ALA   A 39  ? 0.1049 0.1026 0.1153 0.0005  0.0050  -0.0041 39  ALA   A N   
1015 N N   B ALA   A 39  ? 0.1155 0.1223 0.1301 0.0007  -0.0007 0.0083  39  ALA   A N   
1016 C CA  A ALA   A 39  ? 0.1046 0.1023 0.1285 0.0021  0.0090  -0.0013 39  ALA   A CA  
1017 C CA  B ALA   A 39  ? 0.1214 0.1219 0.1270 0.0010  -0.0095 0.0047  39  ALA   A CA  
1018 C C   A ALA   A 39  ? 0.1070 0.1064 0.1301 -0.0003 0.0068  0.0019  39  ALA   A C   
1019 C C   B ALA   A 39  ? 0.1152 0.1093 0.1235 0.0004  -0.0100 0.0028  39  ALA   A C   
1020 O O   A ALA   A 39  ? 0.1097 0.1118 0.1182 -0.0094 0.0120  0.0107  39  ALA   A O   
1021 O O   B ALA   A 39  ? 0.1284 0.1136 0.1316 -0.0027 -0.0014 -0.0069 39  ALA   A O   
1022 C CB  A ALA   A 39  ? 0.0974 0.1043 0.1387 0.0065  0.0026  -0.0000 39  ALA   A CB  
1023 C CB  B ALA   A 39  ? 0.1294 0.1413 0.1321 -0.0006 -0.0202 0.0036  39  ALA   A CB  
1034 N N   A ASN   A 40  ? 0.1106 0.1153 0.1375 -0.0022 0.0088  -0.0002 40  ASN   A N   
1035 N N   B ASN   A 40  ? 0.1179 0.1112 0.1138 -0.0050 0.0074  0.0012  40  ASN   A N   
1036 C CA  A ASN   A 40  ? 0.1123 0.1151 0.1334 0.0054  -0.0002 -0.0019 40  ASN   A CA  
1037 C CA  B ASN   A 40  ? 0.1188 0.1074 0.1263 0.0031  -0.0113 0.0068  40  ASN   A CA  
1038 C C   A ASN   A 40  ? 0.1125 0.1038 0.1134 0.0033  0.0042  0.0048  40  ASN   A C   
1039 C C   B ASN   A 40  ? 0.1164 0.1022 0.1072 -0.0053 0.0095  0.0258  40  ASN   A C   
1040 O O   A ASN   A 40  ? 0.1168 0.1086 0.1141 0.0000  0.0018  -0.0006 40  ASN   A O   
1041 O O   B ASN   A 40  ? 0.1161 0.1039 0.1228 -0.0119 0.0059  0.0198  40  ASN   A O   
1042 C CB  A ASN   A 40  ? 0.1196 0.1276 0.1464 0.0029  0.0072  0.0044  40  ASN   A CB  
1043 C CB  B ASN   A 40  ? 0.1352 0.1093 0.1408 0.0067  -0.0277 0.0098  40  ASN   A CB  
1044 C CG  A ASN   A 40  ? 0.1308 0.1374 0.1736 -0.0037 0.0231  0.0147  40  ASN   A CG  
1045 C CG  B ASN   A 40  ? 0.1524 0.1113 0.1691 0.0117  -0.0336 0.0087  40  ASN   A CG  
1046 O OD1 A ASN   A 40  ? 0.1293 0.1391 0.1653 -0.0100 0.0518  0.0213  40  ASN   A OD1 
1047 O OD1 B ASN   A 40  ? 0.1607 0.1156 0.2152 0.0045  -0.0305 -0.0043 40  ASN   A OD1 
1048 N ND2 A ASN   A 40  ? 0.1349 0.1407 0.1801 -0.0022 0.0191  0.0138  40  ASN   A ND2 
1049 N ND2 B ASN   A 40  ? 0.1569 0.1125 0.1632 0.0136  -0.0363 0.0119  40  ASN   A ND2 
1062 N N   A VAL   A 41  ? 0.1107 0.1040 0.1149 0.0006  0.0062  0.0098  41  VAL   A N   
1063 N N   B VAL   A 41  ? 0.1218 0.1132 0.1221 -0.0006 0.0073  0.0244  41  VAL   A N   
1064 C CA  A VAL   A 41  ? 0.1085 0.1053 0.1193 0.0004  0.0034  0.0095  41  VAL   A CA  
1065 C CA  B VAL   A 41  ? 0.1278 0.1223 0.1261 0.0014  0.0133  0.0206  41  VAL   A CA  
1066 C C   A VAL   A 41  ? 0.1113 0.1051 0.1338 -0.0010 0.0002  0.0078  41  VAL   A C   
1067 C C   B VAL   A 41  ? 0.1284 0.1208 0.1278 -0.0029 0.0172  0.0162  41  VAL   A C   
1068 O O   A VAL   A 41  ? 0.1183 0.1072 0.1265 -0.0039 -0.0064 0.0021  41  VAL   A O   
1069 O O   B VAL   A 41  ? 0.1396 0.1143 0.1099 -0.0024 0.0073  0.0017  41  VAL   A O   
1070 C CB  A VAL   A 41  ? 0.1115 0.1082 0.1009 -0.0006 0.0108  0.0066  41  VAL   A CB  
1071 C CB  B VAL   A 41  ? 0.1475 0.1363 0.1402 -0.0018 0.0148  0.0185  41  VAL   A CB  
1072 C CG1 A VAL   A 41  ? 0.1169 0.1179 0.1044 0.0047  0.0116  -0.0003 41  VAL   A CG1 
1073 C CG1 B VAL   A 41  ? 0.1655 0.1460 0.1487 -0.0039 0.0303  0.0064  41  VAL   A CG1 
1074 C CG2 A VAL   A 41  ? 0.1050 0.1101 0.0811 -0.0018 0.0061  0.0045  41  VAL   A CG2 
1075 C CG2 B VAL   A 41  ? 0.1546 0.1477 0.1544 -0.0043 0.0069  0.0206  41  VAL   A CG2 
1094 N N   A TYR   A 42  ? 0.1092 0.1035 0.1607 -0.0056 0.0002  0.0181  42  TYR   A N   
1095 N N   B TYR   A 42  ? 0.1190 0.1174 0.1575 0.0005  0.0351  0.0213  42  TYR   A N   
1096 C CA  A TYR   A 42  ? 0.1251 0.1048 0.1637 -0.0103 0.0043  0.0185  42  TYR   A CA  
1097 C CA  B TYR   A 42  ? 0.1286 0.1131 0.1623 -0.0043 0.0375  0.0241  42  TYR   A CA  
1098 C C   A TYR   A 42  ? 0.1203 0.1041 0.1616 -0.0067 0.0104  0.0115  42  TYR   A C   
1099 C C   B TYR   A 42  ? 0.1264 0.1094 0.1633 -0.0030 0.0212  0.0181  42  TYR   A C   
1100 O O   A TYR   A 42  ? 0.1189 0.1059 0.1778 -0.0136 0.0151  0.0034  42  TYR   A O   
1101 O O   B TYR   A 42  ? 0.1253 0.1114 0.1880 -0.0114 0.0109  0.0145  42  TYR   A O   
1102 C CB  A TYR   A 42  ? 0.1531 0.1159 0.1671 -0.0106 0.0055  0.0242  42  TYR   A CB  
1103 C CB  B TYR   A 42  ? 0.1573 0.1229 0.1677 -0.0059 0.0394  0.0281  42  TYR   A CB  
1104 C CG  A TYR   A 42  ? 0.1742 0.1289 0.1665 -0.0087 -0.0016 0.0331  42  TYR   A CG  
1105 C CG  B TYR   A 42  ? 0.1806 0.1433 0.1689 -0.0136 0.0395  0.0301  42  TYR   A CG  
1106 C CD1 A TYR   A 42  ? 0.1764 0.1340 0.1668 -0.0118 0.0036  0.0370  42  TYR   A CD1 
1107 C CD1 B TYR   A 42  ? 0.1880 0.1574 0.1768 -0.0187 0.0444  0.0255  42  TYR   A CD1 
1108 C CD2 A TYR   A 42  ? 0.1857 0.1451 0.1783 -0.0074 -0.0029 0.0229  42  TYR   A CD2 
1109 C CD2 B TYR   A 42  ? 0.1855 0.1648 0.1739 -0.0147 0.0433  0.0201  42  TYR   A CD2 
1110 C CE1 A TYR   A 42  ? 0.1792 0.1463 0.1686 -0.0132 0.0064  0.0331  42  TYR   A CE1 
1111 C CE1 B TYR   A 42  ? 0.1911 0.1754 0.1802 -0.0216 0.0517  0.0213  42  TYR   A CE1 
1112 C CE2 A TYR   A 42  ? 0.1900 0.1567 0.1810 -0.0139 0.0006  0.0203  42  TYR   A CE2 
1113 C CE2 B TYR   A 42  ? 0.1893 0.1782 0.1847 -0.0304 0.0424  0.0250  42  TYR   A CE2 
1114 C CZ  A TYR   A 42  ? 0.1875 0.1603 0.1739 -0.0161 0.0116  0.0260  42  TYR   A CZ  
1115 C CZ  B TYR   A 42  ? 0.1966 0.1839 0.1838 -0.0314 0.0527  0.0284  42  TYR   A CZ  
1116 O OH  A TYR   A 42  ? 0.1890 0.1814 0.1879 -0.0206 0.0182  0.0176  42  TYR   A OH  
1117 O OH  B TYR   A 42  ? 0.2093 0.2062 0.2184 -0.0303 0.0509  0.0190  42  TYR   A OH  
1136 N N   . LEU   A 43  ? 0.1248 0.1087 0.1516 -0.0041 0.0123  0.0022  43  LEU   A N   
1137 C CA  . LEU   A 43  ? 0.1156 0.1089 0.1563 -0.0056 0.0118  0.0060  43  LEU   A CA  
1138 C C   . LEU   A 43  ? 0.1130 0.1121 0.1535 -0.0038 0.0061  -0.0013 43  LEU   A C   
1139 O O   . LEU   A 43  ? 0.1330 0.1171 0.1751 0.0018  -0.0099 -0.0028 43  LEU   A O   
1140 C CB  . LEU   A 43  ? 0.1197 0.1105 0.1570 -0.0086 0.0142  -0.0014 43  LEU   A CB  
1141 C CG  . LEU   A 43  ? 0.1241 0.1107 0.1599 -0.0062 0.0057  -0.0028 43  LEU   A CG  
1142 C CD1 . LEU   A 43  ? 0.1343 0.1206 0.1775 -0.0016 -0.0005 0.0072  43  LEU   A CD1 
1143 C CD2 . LEU   A 43  ? 0.1400 0.1185 0.1511 -0.0053 0.0055  0.0083  43  LEU   A CD2 
1156 N N   A LYS   A 44  ? 0.1243 0.1241 0.1533 -0.0019 0.0050  0.0006  44  LYS   A N   
1157 N N   B LYS   A 44  ? 0.1192 0.1098 0.1507 -0.0007 0.0055  0.0068  44  LYS   A N   
1158 C CA  A LYS   A 44  ? 0.1407 0.1338 0.1663 -0.0047 0.0044  0.0033  44  LYS   A CA  
1159 C CA  B LYS   A 44  ? 0.1329 0.1042 0.1653 -0.0060 0.0072  0.0170  44  LYS   A CA  
1160 C C   A LYS   A 44  ? 0.1312 0.1284 0.1497 0.0063  0.0035  -0.0021 44  LYS   A C   
1161 C C   B LYS   A 44  ? 0.1220 0.1010 0.1610 0.0027  -0.0001 0.0048  44  LYS   A C   
1162 O O   A LYS   A 44  ? 0.1387 0.1413 0.1556 0.0062  0.0002  -0.0075 44  LYS   A O   
1163 O O   B LYS   A 44  ? 0.1282 0.1180 0.1772 -0.0034 -0.0009 -0.0106 44  LYS   A O   
1164 C CB  A LYS   A 44  ? 0.1684 0.1549 0.2147 -0.0096 0.0069  0.0072  44  LYS   A CB  
1165 C CB  B LYS   A 44  ? 0.1612 0.1152 0.2127 -0.0015 0.0249  0.0346  44  LYS   A CB  
1166 C CG  A LYS   A 44  ? 0.1975 0.1821 0.2773 -0.0176 0.0132  0.0143  44  LYS   A CG  
1167 C CG  B LYS   A 44  ? 0.1926 0.1469 0.2893 -0.0088 0.0442  0.0533  44  LYS   A CG  
1168 C CD  A LYS   A 44  ? 0.2277 0.2187 0.3476 -0.0217 0.0062  0.0125  44  LYS   A CD  
1169 C CD  B LYS   A 44  ? 0.2301 0.2025 0.3928 -0.0103 0.0259  0.0369  44  LYS   A CD  
1170 C CE  A LYS   A 44  ? 0.2446 0.2425 0.3964 -0.0223 0.0035  0.0143  44  LYS   A CE  
1171 C CE  B LYS   A 44  ? 0.2474 0.2331 0.4626 -0.0105 0.0173  0.0282  44  LYS   A CE  
1172 N NZ  A LYS   A 44  ? 0.2542 0.2596 0.4209 -0.0236 0.0051  0.0151  44  LYS   A NZ  
1173 N NZ  B LYS   A 44  ? 0.2603 0.2554 0.5004 -0.0113 0.0177  0.0207  44  LYS   A NZ  
1200 N N   A HIS   A 45  ? 0.1211 0.1226 0.1435 0.0051  0.0047  0.0021  45  HIS   A N   
1201 N N   B HIS   A 45  ? 0.1202 0.1003 0.1563 -0.0013 -0.0092 0.0119  45  HIS   A N   
1202 C CA  A HIS   A 45  ? 0.1165 0.1190 0.1465 0.0056  0.0062  -0.0015 45  HIS   A CA  
1203 C CA  B HIS   A 45  ? 0.1186 0.1086 0.1552 -0.0008 -0.0111 0.0077  45  HIS   A CA  
1204 C C   A HIS   A 45  ? 0.1214 0.1291 0.1539 0.0084  0.0068  0.0012  45  HIS   A C   
1205 C C   B HIS   A 45  ? 0.1211 0.1165 0.1569 -0.0003 -0.0103 0.0043  45  HIS   A C   
1206 O O   A HIS   A 45  ? 0.1386 0.1307 0.1639 0.0147  0.0118  0.0018  45  HIS   A O   
1207 O O   B HIS   A 45  ? 0.1452 0.1345 0.1779 0.0221  -0.0160 -0.0060 45  HIS   A O   
1208 C CB  A HIS   A 45  ? 0.1180 0.1112 0.1415 0.0062  0.0127  -0.0090 45  HIS   A CB  
1209 C CB  B HIS   A 45  ? 0.1198 0.1086 0.1499 0.0024  -0.0113 -0.0042 45  HIS   A CB  
1210 C CG  A HIS   A 45  ? 0.1172 0.1044 0.1275 0.0009  0.0136  0.0005  45  HIS   A CG  
1211 C CG  B HIS   A 45  ? 0.1069 0.1112 0.1287 -0.0053 0.0041  0.0030  45  HIS   A CG  
1212 N ND1 A HIS   A 45  ? 0.1195 0.1064 0.1276 -0.0053 0.0121  -0.0010 45  HIS   A ND1 
1213 N ND1 B HIS   A 45  ? 0.1063 0.1202 0.1564 -0.0048 -0.0025 0.0122  45  HIS   A ND1 
1214 C CD2 A HIS   A 45  ? 0.1240 0.1088 0.1432 0.0043  0.0085  0.0125  45  HIS   A CD2 
1215 C CD2 B HIS   A 45  ? 0.1064 0.1109 0.1249 -0.0075 0.0004  0.0007  45  HIS   A CD2 
1216 C CE1 A HIS   A 45  ? 0.1261 0.1131 0.1355 -0.0029 0.0120  0.0180  45  HIS   A CE1 
1217 C CE1 B HIS   A 45  ? 0.1069 0.1081 0.1307 -0.0062 -0.0076 0.0019  45  HIS   A CE1 
1218 N NE2 A HIS   A 45  ? 0.1285 0.1105 0.1484 0.0075  0.0113  0.0167  45  HIS   A NE2 
1219 N NE2 B HIS   A 45  ? 0.1038 0.1082 0.1171 -0.0048 -0.0037 -0.0012 45  HIS   A NE2 
1234 N N   A GLY   A 46  ? 0.1203 0.1351 0.1686 0.0087  -0.0127 0.0075  46  GLY   A N   
1235 N N   B GLY   A 46  ? 0.1228 0.1131 0.1643 -0.0028 -0.0253 -0.0003 46  GLY   A N   
1236 C CA  A GLY   A 46  ? 0.1204 0.1252 0.1688 0.0003  -0.0252 0.0169  46  GLY   A CA  
1237 C CA  B GLY   A 46  ? 0.1281 0.1237 0.1793 -0.0008 -0.0243 -0.0006 46  GLY   A CA  
1238 C C   A GLY   A 46  ? 0.1244 0.1131 0.1635 0.0099  -0.0249 0.0210  46  GLY   A C   
1239 C C   B GLY   A 46  ? 0.1324 0.1223 0.1878 0.0098  -0.0185 0.0183  46  GLY   A C   
1240 O O   A GLY   A 46  ? 0.1390 0.1120 0.1882 0.0130  -0.0246 0.0370  46  GLY   A O   
1241 O O   B GLY   A 46  ? 0.1441 0.1343 0.2163 0.0115  -0.0231 0.0045  46  GLY   A O   
1248 N N   A GLY   A 47  ? 0.1171 0.1092 0.1566 0.0024  -0.0192 0.0185  47  GLY   A N   
1249 N N   B GLY   A 47  ? 0.1330 0.1215 0.1842 0.0099  -0.0149 0.0173  47  GLY   A N   
1250 C CA  A GLY   A 47  ? 0.1265 0.1220 0.1557 0.0005  -0.0131 0.0264  47  GLY   A CA  
1251 C CA  B GLY   A 47  ? 0.1309 0.1315 0.1833 0.0074  -0.0242 0.0129  47  GLY   A CA  
1252 C C   A GLY   A 47  ? 0.1228 0.1219 0.1342 0.0044  -0.0122 0.0143  47  GLY   A C   
1253 C C   B GLY   A 47  ? 0.1223 0.1213 0.1591 0.0115  -0.0256 0.0033  47  GLY   A C   
1254 O O   A GLY   A 47  ? 0.1257 0.1210 0.1495 0.0054  -0.0120 0.0169  47  GLY   A O   
1255 O O   B GLY   A 47  ? 0.1177 0.1181 0.1697 0.0164  -0.0175 0.0181  47  GLY   A O   
1262 N N   A GLY   A 48  ? 0.1167 0.1275 0.1117 0.0110  -0.0049 0.0119  48  GLY   A N   
1263 N N   B GLY   A 48  ? 0.1205 0.1263 0.1604 0.0091  -0.0177 0.0027  48  GLY   A N   
1264 C CA  A GLY   A 48  ? 0.1073 0.1292 0.1143 0.0052  0.0051  0.0057  48  GLY   A CA  
1265 C CA  B GLY   A 48  ? 0.1225 0.1223 0.1446 0.0038  -0.0072 -0.0112 48  GLY   A CA  
1266 C C   A GLY   A 48  ? 0.1067 0.1272 0.1144 0.0045  0.0060  0.0041  48  GLY   A C   
1267 C C   B GLY   A 48  ? 0.1176 0.1194 0.1358 0.0002  -0.0066 -0.0031 48  GLY   A C   
1268 O O   A GLY   A 48  ? 0.1187 0.1263 0.1156 0.0086  -0.0056 0.0047  48  GLY   A O   
1269 O O   B GLY   A 48  ? 0.1287 0.1201 0.1354 0.0067  -0.0041 -0.0121 48  GLY   A O   
1276 N N   A VAL   A 49  ? 0.1152 0.1296 0.1232 -0.0016 -0.0010 0.0113  49  VAL   A N   
1277 N N   B VAL   A 49  ? 0.1111 0.1102 0.1234 -0.0030 -0.0063 -0.0056 49  VAL   A N   
1278 C CA  A VAL   A 49  ? 0.1241 0.1215 0.1256 -0.0054 -0.0062 0.0169  49  VAL   A CA  
1279 C CA  B VAL   A 49  ? 0.1212 0.1142 0.1350 -0.0050 0.0017  0.0021  49  VAL   A CA  
1280 C C   A VAL   A 49  ? 0.1170 0.1167 0.1300 -0.0017 -0.0086 0.0216  49  VAL   A C   
1281 C C   B VAL   A 49  ? 0.1149 0.1080 0.1347 0.0015  0.0060  -0.0173 49  VAL   A C   
1282 O O   A VAL   A 49  ? 0.1193 0.1197 0.1417 -0.0135 -0.0168 0.0146  49  VAL   A O   
1283 O O   B VAL   A 49  ? 0.1135 0.1103 0.1355 -0.0017 0.0111  -0.0120 49  VAL   A O   
1284 C CB  A VAL   A 49  ? 0.1373 0.1183 0.1398 -0.0115 -0.0100 0.0189  49  VAL   A CB  
1285 C CB  B VAL   A 49  ? 0.1351 0.1174 0.1631 -0.0073 -0.0218 0.0086  49  VAL   A CB  
1286 C CG1 A VAL   A 49  ? 0.1394 0.1141 0.1589 -0.0114 -0.0131 0.0085  49  VAL   A CG1 
1287 C CG1 B VAL   A 49  ? 0.1224 0.1097 0.1791 0.0062  -0.0184 0.0020  49  VAL   A CG1 
1288 C CG2 A VAL   A 49  ? 0.1419 0.1207 0.1420 -0.0202 -0.0163 0.0211  49  VAL   A CG2 
1289 C CG2 B VAL   A 49  ? 0.1537 0.1279 0.1891 -0.0151 -0.0432 0.0205  49  VAL   A CG2 
1308 N N   A ALA   A 50  ? 0.1092 0.1125 0.1401 0.0025  -0.0075 0.0251  50  ALA   A N   
1309 N N   B ALA   A 50  ? 0.1109 0.1068 0.1300 -0.0015 -0.0074 -0.0195 50  ALA   A N   
1310 C CA  A ALA   A 50  ? 0.1102 0.1149 0.1471 0.0045  -0.0016 0.0269  50  ALA   A CA  
1311 C CA  B ALA   A 50  ? 0.1124 0.1076 0.1360 -0.0060 -0.0026 -0.0206 50  ALA   A CA  
1312 C C   A ALA   A 50  ? 0.1052 0.1140 0.1515 0.0059  -0.0040 0.0180  50  ALA   A C   
1313 C C   B ALA   A 50  ? 0.1062 0.1067 0.1444 -0.0082 -0.0066 -0.0173 50  ALA   A C   
1314 O O   A ALA   A 50  ? 0.1061 0.1156 0.1668 0.0138  -0.0061 0.0164  50  ALA   A O   
1315 O O   B ALA   A 50  ? 0.1090 0.1128 0.1368 -0.0026 -0.0009 -0.0201 50  ALA   A O   
1316 C CB  A ALA   A 50  ? 0.1081 0.1148 0.1508 0.0092  0.0010  0.0324  50  ALA   A CB  
1317 C CB  B ALA   A 50  ? 0.1086 0.1039 0.1392 -0.0012 -0.0009 -0.0325 50  ALA   A CB  
1328 N N   A GLY   A 51  ? 0.1091 0.1130 0.1556 0.0120  -0.0080 0.0113  51  GLY   A N   
1329 N N   B GLY   A 51  ? 0.1140 0.1018 0.1638 0.0006  -0.0168 -0.0149 51  GLY   A N   
1330 C CA  A GLY   A 51  ? 0.1152 0.1133 0.1578 0.0139  -0.0095 0.0064  51  GLY   A CA  
1331 C CA  B GLY   A 51  ? 0.1268 0.1011 0.1755 0.0041  -0.0231 -0.0139 51  GLY   A CA  
1332 C C   A GLY   A 51  ? 0.1087 0.1153 0.1536 0.0063  0.0018  -0.0034 51  GLY   A C   
1333 C C   B GLY   A 51  ? 0.1185 0.1104 0.1902 0.0046  -0.0180 -0.0215 51  GLY   A C   
1334 O O   A GLY   A 51  ? 0.1070 0.1182 0.1562 -0.0004 -0.0066 -0.0008 51  GLY   A O   
1335 O O   B GLY   A 51  ? 0.1257 0.1192 0.2006 0.0046  -0.0214 -0.0273 51  GLY   A O   
1342 N N   A ALA   A 52  ? 0.1097 0.1255 0.1559 0.0054  0.0109  -0.0167 52  ALA   A N   
1343 N N   B ALA   A 52  ? 0.1087 0.1220 0.1916 0.0044  -0.0072 -0.0359 52  ALA   A N   
1344 C CA  A ALA   A 52  ? 0.1139 0.1394 0.1543 0.0040  0.0125  -0.0200 52  ALA   A CA  
1345 C CA  B ALA   A 52  ? 0.1162 0.1447 0.1871 -0.0025 -0.0077 -0.0389 52  ALA   A CA  
1346 C C   A ALA   A 52  ? 0.1127 0.1369 0.1520 -0.0039 0.0168  -0.0132 52  ALA   A C   
1347 C C   B ALA   A 52  ? 0.1154 0.1362 0.1709 -0.0187 0.0049  -0.0365 52  ALA   A C   
1348 O O   A ALA   A 52  ? 0.1174 0.1399 0.1637 -0.0010 0.0085  -0.0167 52  ALA   A O   
1349 O O   B ALA   A 52  ? 0.1270 0.1366 0.1812 -0.0152 0.0189  -0.0393 52  ALA   A O   
1350 C CB  A ALA   A 52  ? 0.1225 0.1605 0.1673 -0.0008 0.0108  -0.0185 52  ALA   A CB  
1351 C CB  B ALA   A 52  ? 0.1268 0.1749 0.2072 -0.0111 -0.0149 -0.0397 52  ALA   A CB  
1362 N N   A LEU   A 53  ? 0.1136 0.1316 0.1533 -0.0038 0.0178  -0.0053 53  LEU   A N   
1363 N N   B LEU   A 53  ? 0.1157 0.1295 0.1553 -0.0117 0.0039  -0.0262 53  LEU   A N   
1364 C CA  A LEU   A 53  ? 0.1256 0.1304 0.1499 -0.0062 0.0168  -0.0021 53  LEU   A CA  
1365 C CA  B LEU   A 53  ? 0.1278 0.1284 0.1395 -0.0084 0.0003  -0.0139 53  LEU   A CA  
1366 C C   A LEU   A 53  ? 0.1242 0.1263 0.1524 -0.0003 0.0150  -0.0155 53  LEU   A C   
1367 C C   B LEU   A 53  ? 0.1251 0.1249 0.1256 0.0009  -0.0003 -0.0088 53  LEU   A C   
1368 O O   A LEU   A 53  ? 0.1312 0.1289 0.1706 -0.0052 0.0164  -0.0123 53  LEU   A O   
1369 O O   B LEU   A 53  ? 0.1403 0.1249 0.1331 -0.0053 0.0037  -0.0072 53  LEU   A O   
1370 C CB  A LEU   A 53  ? 0.1351 0.1311 0.1497 -0.0055 0.0227  0.0077  53  LEU   A CB  
1371 C CB  B LEU   A 53  ? 0.1329 0.1281 0.1408 -0.0107 0.0026  -0.0109 53  LEU   A CB  
1372 C CG  A LEU   A 53  ? 0.1358 0.1311 0.1526 -0.0085 0.0181  0.0135  53  LEU   A CG  
1373 C CG  B LEU   A 53  ? 0.1391 0.1314 0.1447 -0.0129 -0.0024 -0.0121 53  LEU   A CG  
1374 C CD1 A LEU   A 53  ? 0.1356 0.1272 0.1510 -0.0060 0.0052  0.0219  53  LEU   A CD1 
1375 C CD1 B LEU   A 53  ? 0.1396 0.1323 0.1466 -0.0117 -0.0114 -0.0157 53  LEU   A CD1 
1376 C CD2 A LEU   A 53  ? 0.1388 0.1463 0.1615 -0.0122 0.0101  0.0114  53  LEU   A CD2 
1377 C CD2 B LEU   A 53  ? 0.1499 0.1402 0.1572 -0.0231 0.0021  -0.0140 53  LEU   A CD2 
1400 N N   A ASN   A 54  ? 0.1178 0.1166 0.1485 -0.0039 0.0094  -0.0173 54  ASN   A N   
1401 N N   B ASN   A 54  ? 0.1152 0.1236 0.1254 0.0029  -0.0032 0.0017  54  ASN   A N   
1402 C CA  A ASN   A 54  ? 0.1141 0.1097 0.1515 -0.0068 0.0071  -0.0238 54  ASN   A CA  
1403 C CA  B ASN   A 54  ? 0.1096 0.1203 0.1431 0.0014  -0.0053 -0.0050 54  ASN   A CA  
1404 C C   A ASN   A 54  ? 0.1180 0.1197 0.1510 -0.0119 0.0067  -0.0210 54  ASN   A C   
1405 C C   B ASN   A 54  ? 0.1144 0.1281 0.1524 -0.0028 -0.0062 -0.0138 54  ASN   A C   
1406 O O   A ASN   A 54  ? 0.1216 0.1288 0.1491 -0.0114 0.0125  -0.0227 54  ASN   A O   
1407 O O   B ASN   A 54  ? 0.1152 0.1383 0.1547 -0.0028 -0.0100 -0.0161 54  ASN   A O   
1408 C CB  A ASN   A 54  ? 0.1090 0.1035 0.1571 -0.0093 -0.0010 -0.0247 54  ASN   A CB  
1409 C CB  B ASN   A 54  ? 0.1082 0.1209 0.1562 0.0048  -0.0069 -0.0079 54  ASN   A CB  
1410 C CG  A ASN   A 54  ? 0.1056 0.1026 0.1536 -0.0094 -0.0023 -0.0097 54  ASN   A CG  
1411 C CG  B ASN   A 54  ? 0.1096 0.1238 0.1562 0.0094  -0.0025 -0.0066 54  ASN   A CG  
1412 O OD1 A ASN   A 54  ? 0.1062 0.1038 0.1378 -0.0155 -0.0058 -0.0047 54  ASN   A OD1 
1413 O OD1 B ASN   A 54  ? 0.1135 0.1326 0.1599 0.0094  -0.0096 0.0007  54  ASN   A OD1 
1414 N ND2 A ASN   A 54  ? 0.1022 0.1071 0.1750 -0.0072 -0.0143 -0.0000 54  ASN   A ND2 
1415 N ND2 B ASN   A 54  ? 0.1112 0.1219 0.1528 0.0054  -0.0037 -0.0083 54  ASN   A ND2 
1428 N N   A LYS   A 55  ? 0.1169 0.1251 0.1556 -0.0114 0.0038  -0.0252 55  LYS   A N   
1429 N N   B LYS   A 55  ? 0.1161 0.1317 0.1614 0.0017  -0.0010 -0.0212 55  LYS   A N   
1430 C CA  A LYS   A 55  ? 0.1219 0.1303 0.1587 -0.0082 0.0016  -0.0274 55  LYS   A CA  
1431 C CA  B LYS   A 55  ? 0.1270 0.1374 0.1726 0.0090  -0.0015 -0.0254 55  LYS   A CA  
1432 C C   A LYS   A 55  ? 0.1229 0.1407 0.1611 -0.0092 0.0091  -0.0341 55  LYS   A C   
1433 C C   B LYS   A 55  ? 0.1228 0.1440 0.1707 -0.0028 0.0080  -0.0287 55  LYS   A C   
1434 O O   A LYS   A 55  ? 0.1315 0.1431 0.1711 -0.0037 0.0015  -0.0415 55  LYS   A O   
1435 O O   B LYS   A 55  ? 0.1304 0.1480 0.1841 0.0018  0.0040  -0.0315 55  LYS   A O   
1436 C CB  A LYS   A 55  ? 0.1251 0.1308 0.1594 -0.0013 -0.0021 -0.0281 55  LYS   A CB  
1437 C CB  B LYS   A 55  ? 0.1412 0.1465 0.1863 0.0226  -0.0021 -0.0269 55  LYS   A CB  
1438 C CG  A LYS   A 55  ? 0.1214 0.1330 0.1550 -0.0104 -0.0022 -0.0150 55  LYS   A CG  
1439 C CG  B LYS   A 55  ? 0.1521 0.1571 0.1873 0.0204  -0.0010 -0.0182 55  LYS   A CG  
1440 C CD  A LYS   A 55  ? 0.1222 0.1426 0.1536 -0.0020 0.0011  -0.0067 55  LYS   A CD  
1441 C CD  B LYS   A 55  ? 0.1610 0.1710 0.1900 0.0227  0.0100  -0.0091 55  LYS   A CD  
1442 C CE  A LYS   A 55  ? 0.1235 0.1493 0.1510 -0.0004 -0.0071 -0.0045 55  LYS   A CE  
1443 C CE  B LYS   A 55  ? 0.1759 0.1920 0.2053 0.0199  0.0044  -0.0078 55  LYS   A CE  
1444 N NZ  A LYS   A 55  ? 0.1201 0.1499 0.1475 0.0044  -0.0079 0.0021  55  LYS   A NZ  
1445 N NZ  B LYS   A 55  ? 0.1872 0.2077 0.2269 0.0230  0.0044  -0.0102 55  LYS   A NZ  
1472 N N   . ALA   A 56  ? 0.1312 0.1552 0.1653 -0.0066 0.0211  -0.0382 56  ALA   A N   
1473 C CA  . ALA   A 56  ? 0.1491 0.1705 0.1685 -0.0087 0.0181  -0.0356 56  ALA   A CA  
1474 C C   . ALA   A 56  ? 0.1506 0.1809 0.1473 -0.0124 0.0192  -0.0425 56  ALA   A C   
1475 O O   . ALA   A 56  ? 0.1582 0.2160 0.1633 0.0021  0.0224  -0.0266 56  ALA   A O   
1476 C CB  . ALA   A 56  ? 0.1594 0.1829 0.1800 -0.0160 0.0174  -0.0251 56  ALA   A CB  
1483 N N   . THR   A 57  ? 0.1350 0.1560 0.1470 -0.0106 0.0163  -0.0332 57  THR   A N   
1484 C CA  . THR   A 57  ? 0.1331 0.1550 0.1493 -0.0108 0.0056  -0.0241 57  THR   A CA  
1485 C C   . THR   A 57  ? 0.1334 0.1621 0.1630 -0.0060 0.0008  -0.0308 57  THR   A C   
1486 O O   . THR   A 57  ? 0.1316 0.1642 0.1833 -0.0102 -0.0044 -0.0432 57  THR   A O   
1487 C CB  . THR   A 57  ? 0.1366 0.1542 0.1497 -0.0052 0.0083  -0.0197 57  THR   A CB  
1488 O OG1 . THR   A 57  ? 0.1263 0.1428 0.1506 -0.0018 0.0074  -0.0207 57  THR   A OG1 
1489 C CG2 . THR   A 57  ? 0.1406 0.1587 0.1404 -0.0048 0.0086  -0.0134 57  THR   A CG2 
1497 N N   . ASN   A 58  ? 0.1353 0.1590 0.1769 -0.0037 0.0099  -0.0421 58  ASN   A N   
1498 C CA  . ASN   A 58  ? 0.1578 0.1530 0.2002 -0.0061 0.0138  -0.0498 58  ASN   A CA  
1499 C C   . ASN   A 58  ? 0.1367 0.1399 0.1866 0.0013  -0.0008 -0.0393 58  ASN   A C   
1500 O O   . ASN   A 58  ? 0.1407 0.1476 0.2012 -0.0155 -0.0022 -0.0441 58  ASN   A O   
1501 C CB  . ASN   A 58  ? 0.2005 0.1684 0.2317 -0.0159 0.0288  -0.0636 58  ASN   A CB  
1502 C CG  . ASN   A 58  ? 0.2320 0.1889 0.2966 -0.0120 0.0255  -0.0557 58  ASN   A CG  
1503 O OD1 . ASN   A 58  ? 0.2571 0.1847 0.3184 0.0214  0.0520  -0.0532 58  ASN   A OD1 
1504 N ND2 . ASN   A 58  ? 0.2359 0.1953 0.3206 -0.0175 0.0171  -0.0532 58  ASN   A ND2 
1511 N N   . ASN   A 59  ? 0.1177 0.1335 0.1764 -0.0051 -0.0095 -0.0313 59  ASN   A N   
1512 C CA  . ASN   A 59  ? 0.1235 0.1214 0.1736 -0.0053 -0.0061 -0.0214 59  ASN   A CA  
1513 C C   . ASN   A 59  ? 0.1192 0.1203 0.1613 -0.0072 -0.0052 -0.0202 59  ASN   A C   
1514 O O   . ASN   A 59  ? 0.1202 0.1238 0.1605 -0.0082 -0.0013 -0.0099 59  ASN   A O   
1515 C CB  . ASN   A 59  ? 0.1272 0.1173 0.1789 0.0008  -0.0173 -0.0233 59  ASN   A CB  
1516 C CG  . ASN   A 59  ? 0.1355 0.1213 0.1774 0.0005  -0.0252 -0.0081 59  ASN   A CG  
1517 O OD1 . ASN   A 59  ? 0.1462 0.1312 0.1713 -0.0081 -0.0273 -0.0044 59  ASN   A OD1 
1518 N ND2 . ASN   A 59  ? 0.1425 0.1310 0.1951 -0.0104 -0.0183 -0.0001 59  ASN   A ND2 
1525 N N   . ALA   A 60  ? 0.1133 0.1290 0.1538 -0.0033 -0.0016 -0.0192 60  ALA   A N   
1526 C CA  . ALA   A 60  ? 0.1210 0.1304 0.1623 -0.0026 -0.0029 -0.0127 60  ALA   A CA  
1527 C C   . ALA   A 60  ? 0.1224 0.1219 0.1688 -0.0026 -0.0090 -0.0218 60  ALA   A C   
1528 O O   . ALA   A 60  ? 0.1158 0.1290 0.1820 -0.0026 -0.0069 -0.0199 60  ALA   A O   
1529 C CB  . ALA   A 60  ? 0.1363 0.1357 0.1656 -0.0046 -0.0129 -0.0298 60  ALA   A CB  
1535 N N   . MET   A 61  ? 0.1176 0.1154 0.1537 -0.0089 -0.0027 -0.0187 61  MET   A N   
1536 C CA  . MET   A 61  ? 0.1164 0.1158 0.1604 -0.0094 -0.0018 -0.0126 61  MET   A CA  
1537 C C   . MET   A 61  ? 0.1101 0.1075 0.1556 -0.0072 -0.0031 -0.0158 61  MET   A C   
1538 O O   . MET   A 61  ? 0.1166 0.1124 0.1567 -0.0042 0.0043  -0.0043 61  MET   A O   
1539 C CB  . MET   A 61  ? 0.1220 0.1165 0.1478 -0.0074 -0.0009 -0.0125 61  MET   A CB  
1540 C CG  . MET   A 61  ? 0.1216 0.1251 0.1631 -0.0001 0.0005  -0.0135 61  MET   A CG  
1541 S SD  . MET   A 61  ? 0.1245 0.1274 0.1990 -0.0128 0.0028  -0.0274 61  MET   A SD  
1542 C CE  . MET   A 61  ? 0.1495 0.1422 0.2177 -0.0184 0.0182  -0.0200 61  MET   A CE  
1552 N N   . GLN   A 62  ? 0.1122 0.1078 0.1606 -0.0056 -0.0032 -0.0112 62  GLN   A N   
1553 C CA  . GLN   A 62  ? 0.1185 0.1088 0.1656 0.0002  0.0017  -0.0053 62  GLN   A CA  
1554 C C   . GLN   A 62  ? 0.1145 0.1052 0.1724 -0.0025 0.0090  -0.0082 62  GLN   A C   
1555 O O   . GLN   A 62  ? 0.1133 0.1195 0.1766 -0.0075 0.0075  -0.0073 62  GLN   A O   
1556 C CB  . GLN   A 62  ? 0.1148 0.1072 0.1691 0.0003  -0.0016 -0.0054 62  GLN   A CB  
1557 C CG  . GLN   A 62  ? 0.1209 0.1036 0.1669 -0.0049 -0.0052 0.0051  62  GLN   A CG  
1558 C CD  . GLN   A 62  ? 0.1233 0.1049 0.1661 -0.0027 0.0028  0.0078  62  GLN   A CD  
1559 O OE1 . GLN   A 62  ? 0.1324 0.1226 0.1718 -0.0042 -0.0031 -0.0068 62  GLN   A OE1 
1560 N NE2 . GLN   A 62  ? 0.1344 0.1121 0.1810 -0.0005 -0.0068 -0.0139 62  GLN   A NE2 
1569 N N   . VAL   A 63  ? 0.1163 0.1130 0.1748 -0.0084 0.0103  -0.0302 63  VAL   A N   
1570 C CA  . VAL   A 63  ? 0.1196 0.1261 0.1994 -0.0175 -0.0009 -0.0296 63  VAL   A CA  
1571 C C   . VAL   A 63  ? 0.1056 0.1258 0.1893 -0.0151 -0.0112 -0.0288 63  VAL   A C   
1572 O O   . VAL   A 63  ? 0.1054 0.1276 0.2074 -0.0139 -0.0001 -0.0301 63  VAL   A O   
1573 C CB  . VAL   A 63  ? 0.1325 0.1425 0.2233 -0.0147 -0.0056 -0.0479 63  VAL   A CB  
1574 C CG1 . VAL   A 63  ? 0.1452 0.1670 0.2443 -0.0183 -0.0073 -0.0656 63  VAL   A CG1 
1575 C CG2 . VAL   A 63  ? 0.1405 0.1283 0.2431 -0.0134 0.0155  -0.0534 63  VAL   A CG2 
1585 N N   . GLU   A 64  ? 0.1115 0.1317 0.1781 -0.0038 -0.0026 -0.0238 64  GLU   A N   
1586 C CA  . GLU   A 64  ? 0.1097 0.1302 0.1764 -0.0075 -0.0047 -0.0130 64  GLU   A CA  
1587 C C   . GLU   A 64  ? 0.1083 0.1189 0.1651 -0.0106 0.0030  -0.0116 64  GLU   A C   
1588 O O   . GLU   A 64  ? 0.1147 0.1262 0.1667 -0.0018 0.0009  -0.0160 64  GLU   A O   
1589 C CB  . GLU   A 64  ? 0.1207 0.1425 0.1801 -0.0059 0.0041  -0.0133 64  GLU   A CB  
1590 C CG  . GLU   A 64  ? 0.1354 0.1444 0.1767 -0.0130 0.0051  -0.0132 64  GLU   A CG  
1591 C CD  . GLU   A 64  ? 0.1448 0.1540 0.1871 -0.0193 0.0071  -0.0172 64  GLU   A CD  
1592 O OE1 . GLU   A 64  ? 0.1456 0.1652 0.2108 -0.0230 0.0104  -0.0170 64  GLU   A OE1 
1593 O OE2 . GLU   A 64  ? 0.1600 0.1526 0.1837 -0.0261 0.0032  -0.0080 64  GLU   A OE2 
1600 N N   . SER   A 65  ? 0.1033 0.1213 0.1593 -0.0002 0.0031  -0.0122 65  SER   A N   
1601 C CA  . SER   A 65  ? 0.1127 0.1139 0.1551 -0.0023 -0.0025 -0.0130 65  SER   A CA  
1602 C C   . SER   A 65  ? 0.1127 0.1180 0.1630 -0.0038 -0.0058 -0.0070 65  SER   A C   
1603 O O   . SER   A 65  ? 0.1168 0.1235 0.1759 -0.0007 0.0124  -0.0122 65  SER   A O   
1604 C CB  . SER   A 65  ? 0.1147 0.1156 0.1585 -0.0087 -0.0027 -0.0056 65  SER   A CB  
1605 O OG  . SER   A 65  ? 0.1130 0.1228 0.1682 -0.0075 -0.0032 0.0019  65  SER   A OG  
1611 N N   . ASP   A 66  ? 0.1141 0.1155 0.1710 -0.0043 0.0114  -0.0004 66  ASP   A N   
1612 C CA  . ASP   A 66  ? 0.1277 0.1237 0.1893 -0.0003 0.0080  0.0097  66  ASP   A CA  
1613 C C   . ASP   A 66  ? 0.1212 0.1213 0.1857 -0.0055 0.0062  0.0083  66  ASP   A C   
1614 O O   . ASP   A 66  ? 0.1290 0.1333 0.2002 -0.0028 0.0186  0.0124  66  ASP   A O   
1615 C CB  . ASP   A 66  ? 0.1346 0.1336 0.2164 0.0010  0.0022  0.0257  66  ASP   A CB  
1616 C CG  . ASP   A 66  ? 0.1596 0.1541 0.2451 0.0033  -0.0070 0.0372  66  ASP   A CG  
1617 O OD1 . ASP   A 66  ? 0.1562 0.1822 0.2263 -0.0054 -0.0075 0.0410  66  ASP   A OD1 
1618 O OD2 . ASP   A 66  ? 0.1792 0.1714 0.3244 0.0266  -0.0276 0.0107  66  ASP   A OD2 
1623 N N   . ASP   A 67  ? 0.1110 0.1223 0.1913 -0.0033 0.0056  0.0059  67  ASP   A N   
1624 C CA  . ASP   A 67  ? 0.1140 0.1383 0.2036 -0.0033 0.0045  0.0117  67  ASP   A CA  
1625 C C   . ASP   A 67  ? 0.1170 0.1342 0.2020 -0.0047 0.0129  0.0177  67  ASP   A C   
1626 O O   . ASP   A 67  ? 0.1178 0.1506 0.2122 -0.0007 0.0270  0.0196  67  ASP   A O   
1627 C CB  . ASP   A 67  ? 0.1260 0.1542 0.2377 -0.0073 -0.0147 0.0126  67  ASP   A CB  
1628 C CG  . ASP   A 67  ? 0.1286 0.1644 0.2667 -0.0088 -0.0290 0.0199  67  ASP   A CG  
1629 O OD1 . ASP   A 67  ? 0.1338 0.1829 0.3407 -0.0145 -0.0367 0.0312  67  ASP   A OD1 
1630 O OD2 . ASP   A 67  ? 0.1288 0.1635 0.2593 0.0009  -0.0249 0.0129  67  ASP   A OD2 
1635 N N   A TYR   A 68  ? 0.1185 0.1260 0.1852 -0.0033 0.0201  0.0147  68  TYR   A N   
1636 N N   B TYR   A 68  ? 0.1202 0.1288 0.1892 -0.0006 0.0116  0.0205  68  TYR   A N   
1637 C CA  A TYR   A 68  ? 0.1248 0.1238 0.1840 -0.0031 0.0283  0.0145  68  TYR   A CA  
1638 C CA  B TYR   A 68  ? 0.1315 0.1323 0.1921 0.0019  0.0125  0.0279  68  TYR   A CA  
1639 C C   A TYR   A 68  ? 0.1217 0.1217 0.1790 -0.0019 0.0240  0.0133  68  TYR   A C   
1640 C C   B TYR   A 68  ? 0.1218 0.1284 0.1866 0.0022  0.0188  0.0190  68  TYR   A C   
1641 O O   A TYR   A 68  ? 0.1285 0.1195 0.1828 0.0018  0.0288  0.0131  68  TYR   A O   
1642 O O   B TYR   A 68  ? 0.1261 0.1313 0.1968 0.0115  0.0281  0.0164  68  TYR   A O   
1643 C CB  A TYR   A 68  ? 0.1260 0.1175 0.1922 -0.0023 0.0521  0.0054  68  TYR   A CB  
1644 C CB  B TYR   A 68  ? 0.1412 0.1324 0.2047 0.0055  0.0218  0.0307  68  TYR   A CB  
1645 C CG  A TYR   A 68  ? 0.1245 0.1242 0.2098 -0.0029 0.0720  0.0090  68  TYR   A CG  
1646 C CG  B TYR   A 68  ? 0.1495 0.1500 0.2154 0.0071  0.0176  0.0332  68  TYR   A CG  
1647 C CD1 A TYR   A 68  ? 0.1212 0.1234 0.2438 -0.0288 0.0657  -0.0125 68  TYR   A CD1 
1648 C CD1 B TYR   A 68  ? 0.1564 0.1550 0.2164 -0.0052 0.0076  0.0245  68  TYR   A CD1 
1649 C CD2 A TYR   A 68  ? 0.1426 0.1282 0.2349 0.0045  0.0722  0.0151  68  TYR   A CD2 
1650 C CD2 B TYR   A 68  ? 0.1648 0.1540 0.2229 0.0030  0.0097  0.0407  68  TYR   A CD2 
1651 C CE1 A TYR   A 68  ? 0.1299 0.1367 0.2733 -0.0246 0.0659  -0.0317 68  TYR   A CE1 
1652 C CE1 B TYR   A 68  ? 0.1632 0.1528 0.2091 -0.0080 0.0082  0.0421  68  TYR   A CE1 
1653 C CE2 A TYR   A 68  ? 0.1403 0.1334 0.2639 0.0043  0.0785  0.0016  68  TYR   A CE2 
1654 C CE2 B TYR   A 68  ? 0.1625 0.1536 0.2053 -0.0066 0.0067  0.0342  68  TYR   A CE2 
1655 C CZ  A TYR   A 68  ? 0.1344 0.1372 0.2948 -0.0179 0.0688  -0.0389 68  TYR   A CZ  
1656 C CZ  B TYR   A 68  ? 0.1666 0.1445 0.1967 -0.0065 0.0066  0.0376  68  TYR   A CZ  
1657 O OH  A TYR   A 68  ? 0.1521 0.1532 0.3427 -0.0184 0.0467  -0.0715 68  TYR   A OH  
1658 O OH  B TYR   A 68  ? 0.1876 0.1316 0.1972 -0.0013 -0.0115 0.0217  68  TYR   A OH  
1677 N N   . ILE   A 69  ? 0.1133 0.1209 0.1773 -0.0031 0.0244  0.0136  69  ILE   A N   
1678 C CA  . ILE   A 69  ? 0.1241 0.1253 0.1710 -0.0036 0.0169  0.0023  69  ILE   A CA  
1679 C C   . ILE   A 69  ? 0.1294 0.1245 0.1554 -0.0024 0.0143  0.0127  69  ILE   A C   
1680 O O   . ILE   A 69  ? 0.1415 0.1381 0.1498 -0.0058 0.0156  0.0173  69  ILE   A O   
1681 C CB  . ILE   A 69  ? 0.1336 0.1464 0.1808 0.0034  0.0127  -0.0080 69  ILE   A CB  
1682 C CG1 . ILE   A 69  ? 0.1316 0.1692 0.1895 0.0075  0.0117  -0.0267 69  ILE   A CG1 
1683 C CG2 . ILE   A 69  ? 0.1582 0.1698 0.2063 0.0138  -0.0007 -0.0153 69  ILE   A CG2 
1684 C CD1 . ILE   A 69  ? 0.1374 0.1820 0.2032 -0.0010 0.0027  -0.0363 69  ILE   A CD1 
1697 N N   . ALA   A 70  ? 0.1379 0.1235 0.1700 -0.0072 0.0123  0.0081  70  ALA   A N   
1698 C CA  . ALA   A 70  ? 0.1436 0.1359 0.1852 -0.0178 0.0227  0.0189  70  ALA   A CA  
1699 C C   . ALA   A 70  ? 0.1366 0.1487 0.1781 -0.0185 0.0249  0.0148  70  ALA   A C   
1700 O O   . ALA   A 70  ? 0.1565 0.1849 0.2019 0.0005  0.0423  0.0303  70  ALA   A O   
1701 C CB  . ALA   A 70  ? 0.1441 0.1352 0.2062 -0.0165 0.0167  0.0064  70  ALA   A CB  
1707 N N   . THR   A 71  ? 0.1236 0.1480 0.1785 -0.0094 0.0216  0.0145  71  THR   A N   
1708 C CA  . THR   A 71  ? 0.1355 0.1614 0.2051 -0.0025 0.0278  0.0166  71  THR   A CA  
1709 C C   . THR   A 71  ? 0.1259 0.1609 0.2198 0.0027  0.0349  0.0120  71  THR   A C   
1710 O O   . THR   A 71  ? 0.1324 0.1870 0.2566 0.0057  0.0434  -0.0099 71  THR   A O   
1711 C CB  . THR   A 71  ? 0.1617 0.1863 0.2237 0.0053  -0.0104 0.0187  71  THR   A CB  
1712 O OG1 . THR   A 71  ? 0.1845 0.2045 0.2280 0.0021  -0.0335 0.0068  71  THR   A OG1 
1713 C CG2 . THR   A 71  ? 0.1713 0.2040 0.2450 0.0125  -0.0247 0.0273  71  THR   A CG2 
1721 N N   . ASN   A 72  ? 0.1282 0.1452 0.1951 0.0074  0.0251  0.0146  72  ASN   A N   
1722 C CA  . ASN   A 72  ? 0.1359 0.1419 0.2068 0.0106  0.0327  0.0156  72  ASN   A CA  
1723 C C   . ASN   A 72  ? 0.1405 0.1397 0.2042 0.0067  0.0425  0.0056  72  ASN   A C   
1724 O O   . ASN   A 72  ? 0.1620 0.1450 0.2272 0.0136  0.0423  -0.0063 72  ASN   A O   
1725 C CB  . ASN   A 72  ? 0.1572 0.1503 0.2031 0.0098  0.0324  0.0150  72  ASN   A CB  
1726 C CG  . ASN   A 72  ? 0.1777 0.1601 0.2032 0.0264  0.0309  0.0237  72  ASN   A CG  
1727 O OD1 . ASN   A 72  ? 0.1946 0.1921 0.2207 0.0267  0.0373  0.0214  72  ASN   A OD1 
1728 N ND2 . ASN   A 72  ? 0.1941 0.1685 0.2109 0.0492  0.0091  0.0103  72  ASN   A ND2 
1735 N N   . GLY   A 73  ? 0.1459 0.1413 0.1882 0.0001  0.0399  -0.0040 73  GLY   A N   
1736 C CA  . GLY   A 73  ? 0.1533 0.1381 0.1794 -0.0144 0.0317  -0.0044 73  GLY   A CA  
1737 C C   . GLY   A 73  ? 0.1514 0.1323 0.1617 -0.0015 0.0437  0.0182  73  GLY   A C   
1738 O O   . GLY   A 73  ? 0.1500 0.1379 0.1731 0.0098  0.0370  0.0206  73  GLY   A O   
1742 N N   . PRO   A 74  ? 0.1652 0.1265 0.1594 -0.0094 0.0416  0.0151  74  PRO   A N   
1743 C CA  . PRO   A 74  ? 0.1592 0.1319 0.1629 -0.0031 0.0390  0.0173  74  PRO   A CA  
1744 C C   . PRO   A 74  ? 0.1495 0.1189 0.1588 -0.0032 0.0203  0.0104  74  PRO   A C   
1745 O O   . PRO   A 74  ? 0.1525 0.1236 0.1852 0.0029  0.0305  -0.0067 74  PRO   A O   
1746 C CB  . PRO   A 74  ? 0.1756 0.1601 0.1908 -0.0035 0.0440  0.0260  74  PRO   A CB  
1747 C CG  . PRO   A 74  ? 0.1987 0.1868 0.2324 -0.0165 0.0330  0.0147  74  PRO   A CG  
1748 C CD  . PRO   A 74  ? 0.1848 0.1619 0.1812 -0.0231 0.0315  0.0089  74  PRO   A CD  
1756 N N   . LEU   A 75  ? 0.1366 0.1121 0.1561 -0.0016 0.0241  0.0072  75  LEU   A N   
1757 C CA  . LEU   A 75  ? 0.1394 0.1139 0.1456 -0.0027 0.0107  0.0048  75  LEU   A CA  
1758 C C   . LEU   A 75  ? 0.1465 0.1200 0.1433 0.0027  0.0116  0.0111  75  LEU   A C   
1759 O O   . LEU   A 75  ? 0.1820 0.1420 0.1431 0.0064  0.0060  0.0050  75  LEU   A O   
1760 C CB  . LEU   A 75  ? 0.1454 0.1092 0.1443 -0.0048 0.0001  0.0088  75  LEU   A CB  
1761 C CG  . LEU   A 75  ? 0.1671 0.1458 0.1548 -0.0385 -0.0014 0.0088  75  LEU   A CG  
1762 C CD1 . LEU   A 75  ? 0.1794 0.1967 0.1672 -0.0380 -0.0027 -0.0029 75  LEU   A CD1 
1763 C CD2 . LEU   A 75  ? 0.2033 0.1956 0.2060 -0.0130 0.0049  0.0153  75  LEU   A CD2 
1775 N N   . LYS   A 76  ? 0.1561 0.1226 0.1561 -0.0086 0.0125  -0.0007 76  LYS   A N   
1776 C CA  . LYS   A 76  ? 0.1553 0.1426 0.1547 -0.0120 0.0082  -0.0137 76  LYS   A CA  
1777 C C   . LYS   A 76  ? 0.1539 0.1207 0.1211 -0.0029 0.0093  0.0009  76  LYS   A C   
1778 O O   . LYS   A 76  ? 0.1584 0.1219 0.1273 -0.0019 0.0140  0.0050  76  LYS   A O   
1779 C CB  . LYS   A 76  ? 0.1558 0.1672 0.1966 -0.0003 0.0143  -0.0443 76  LYS   A CB  
1780 C CG  . LYS   A 76  ? 0.1609 0.1672 0.2547 0.0028  0.0172  -0.0385 76  LYS   A CG  
1781 C CD  . LYS   A 76  ? 0.1699 0.1703 0.3000 0.0094  0.0019  -0.0488 76  LYS   A CD  
1782 C CE  . LYS   A 76  ? 0.1821 0.1862 0.3576 0.0074  0.0041  -0.0591 76  LYS   A CE  
1783 N NZ  . LYS   A 76  ? 0.1843 0.1866 0.3978 -0.0022 0.0052  -0.0681 76  LYS   A NZ  
1797 N N   . VAL   A 77  ? 0.1639 0.1254 0.1249 -0.0008 0.0211  0.0064  77  VAL   A N   
1798 C CA  . VAL   A 77  ? 0.1622 0.1295 0.1343 0.0059  0.0192  0.0142  77  VAL   A CA  
1799 C C   . VAL   A 77  ? 0.1533 0.1279 0.1209 0.0051  0.0137  0.0007  77  VAL   A C   
1800 O O   . VAL   A 77  ? 0.1575 0.1309 0.1231 0.0129  0.0229  -0.0028 77  VAL   A O   
1801 C CB  . VAL   A 77  ? 0.1792 0.1480 0.1401 0.0030  0.0112  0.0201  77  VAL   A CB  
1802 C CG1 . VAL   A 77  ? 0.1762 0.1584 0.1644 0.0152  0.0015  0.0052  77  VAL   A CG1 
1803 C CG2 . VAL   A 77  ? 0.2031 0.1646 0.1656 -0.0081 0.0006  0.0278  77  VAL   A CG2 
1813 N N   . GLY   A 78  ? 0.1446 0.1254 0.1181 0.0001  0.0183  0.0054  78  GLY   A N   
1814 C CA  . GLY   A 78  ? 0.1345 0.1235 0.1360 0.0008  0.0180  0.0123  78  GLY   A CA  
1815 C C   . GLY   A 78  ? 0.1292 0.1144 0.1374 0.0069  0.0209  0.0103  78  GLY   A C   
1816 O O   . GLY   A 78  ? 0.1331 0.1226 0.1472 -0.0017 0.0105  0.0239  78  GLY   A O   
1820 N N   . GLY   A 79  ? 0.1306 0.1145 0.1366 -0.0017 0.0125  0.0142  79  GLY   A N   
1821 C CA  . GLY   A 79  ? 0.1273 0.1193 0.1514 0.0000  0.0153  0.0039  79  GLY   A CA  
1822 C C   . GLY   A 79  ? 0.1181 0.1086 0.1414 -0.0032 0.0036  -0.0016 79  GLY   A C   
1823 O O   . GLY   A 79  ? 0.1235 0.1215 0.1475 0.0145  0.0103  0.0049  79  GLY   A O   
1827 N N   . SER   A 80  ? 0.1167 0.1290 0.1550 -0.0007 0.0106  -0.0118 80  SER   A N   
1828 C CA  . SER   A 80  ? 0.1127 0.1230 0.1419 -0.0014 0.0003  -0.0048 80  SER   A CA  
1829 C C   . SER   A 80  ? 0.1137 0.1222 0.1431 -0.0031 0.0024  -0.0011 80  SER   A C   
1830 O O   . SER   A 80  ? 0.1134 0.1436 0.1787 0.0051  0.0138  -0.0096 80  SER   A O   
1831 C CB  . SER   A 80  ? 0.1229 0.1210 0.1710 -0.0074 0.0053  -0.0011 80  SER   A CB  
1832 O OG  . SER   A 80  ? 0.1533 0.1212 0.2053 0.0045  -0.0086 0.0128  80  SER   A OG  
1838 N N   . CYS   A 81  ? 0.1064 0.1179 0.1471 -0.0005 -0.0035 0.0013  81  CYS   A N   
1839 C CA  . CYS   A 81  ? 0.1081 0.1277 0.1402 -0.0037 -0.0115 0.0147  81  CYS   A CA  
1840 C C   . CYS   A 81  ? 0.1071 0.1181 0.1424 -0.0086 -0.0057 0.0172  81  CYS   A C   
1841 O O   . CYS   A 81  ? 0.1095 0.1490 0.1508 -0.0025 -0.0022 0.0280  81  CYS   A O   
1842 C CB  . CYS   A 81  ? 0.1169 0.1365 0.1629 -0.0134 -0.0063 0.0111  81  CYS   A CB  
1843 S SG  . CYS   A 81  ? 0.1360 0.1206 0.1642 -0.0153 -0.0012 0.0055  81  CYS   A SG  
1849 N N   . VAL   A 82  ? 0.1159 0.1314 0.1447 0.0003  -0.0133 0.0114  82  VAL   A N   
1850 C CA  . VAL   A 82  ? 0.1254 0.1378 0.1478 0.0000  -0.0114 0.0184  82  VAL   A CA  
1851 C C   . VAL   A 82  ? 0.1269 0.1393 0.1454 -0.0001 -0.0165 0.0136  82  VAL   A C   
1852 O O   . VAL   A 82  ? 0.1169 0.1514 0.1785 -0.0031 -0.0087 -0.0090 82  VAL   A O   
1853 C CB  . VAL   A 82  ? 0.1564 0.1517 0.1605 -0.0024 -0.0066 0.0168  82  VAL   A CB  
1854 C CG1 . VAL   A 82  ? 0.1788 0.1621 0.1739 0.0078  -0.0004 0.0094  82  VAL   A CG1 
1855 C CG2 . VAL   A 82  ? 0.1659 0.1529 0.1852 -0.0014 -0.0031 0.0258  82  VAL   A CG2 
1865 N N   . LEU   A 83  ? 0.1228 0.1327 0.1413 -0.0081 -0.0148 0.0035  83  LEU   A N   
1866 C CA  . LEU   A 83  ? 0.1201 0.1391 0.1405 -0.0099 -0.0142 0.0010  83  LEU   A CA  
1867 C C   . LEU   A 83  ? 0.1351 0.1416 0.1364 -0.0163 -0.0180 0.0034  83  LEU   A C   
1868 O O   . LEU   A 83  ? 0.1409 0.1421 0.1457 -0.0165 -0.0046 0.0054  83  LEU   A O   
1869 C CB  . LEU   A 83  ? 0.1327 0.1406 0.1445 -0.0120 -0.0118 0.0051  83  LEU   A CB  
1870 C CG  . LEU   A 83  ? 0.1477 0.1517 0.1484 -0.0113 0.0037  -0.0042 83  LEU   A CG  
1871 C CD1 . LEU   A 83  ? 0.1570 0.1507 0.1603 -0.0207 -0.0019 0.0112  83  LEU   A CD1 
1872 C CD2 . LEU   A 83  ? 0.1521 0.1641 0.1652 -0.0101 0.0278  0.0078  83  LEU   A CD2 
1884 N N   . SER   A 84  ? 0.1428 0.1440 0.1405 -0.0163 -0.0109 0.0024  84  SER   A N   
1885 C CA  . SER   A 84  ? 0.1519 0.1532 0.1349 -0.0163 -0.0057 -0.0006 84  SER   A CA  
1886 C C   . SER   A 84  ? 0.1547 0.1454 0.1298 -0.0196 0.0019  -0.0049 84  SER   A C   
1887 O O   . SER   A 84  ? 0.1563 0.1613 0.1304 -0.0185 -0.0078 -0.0042 84  SER   A O   
1888 C CB  . SER   A 84  ? 0.1627 0.1803 0.1359 -0.0181 -0.0028 -0.0069 84  SER   A CB  
1889 O OG  . SER   A 84  ? 0.1706 0.2032 0.1446 -0.0141 -0.0129 -0.0178 84  SER   A OG  
1895 N N   . GLY   A 85  ? 0.1727 0.1634 0.1301 -0.0197 0.0120  -0.0078 85  GLY   A N   
1896 C CA  . GLY   A 85  ? 0.1772 0.1717 0.1442 -0.0267 0.0172  -0.0195 85  GLY   A CA  
1897 C C   . GLY   A 85  ? 0.1724 0.1768 0.1315 -0.0240 0.0063  -0.0152 85  GLY   A C   
1898 O O   . GLY   A 85  ? 0.1677 0.1879 0.1538 -0.0275 0.0210  -0.0237 85  GLY   A O   
1902 N N   . HIS   A 86  ? 0.1768 0.1581 0.1273 -0.0169 0.0056  -0.0095 86  HIS   A N   
1903 C CA  . HIS   A 86  ? 0.1917 0.1690 0.1274 -0.0231 0.0061  -0.0066 86  HIS   A CA  
1904 C C   . HIS   A 86  ? 0.2128 0.1811 0.1343 -0.0236 0.0047  -0.0102 86  HIS   A C   
1905 O O   . HIS   A 86  ? 0.2266 0.2000 0.1416 -0.0086 0.0138  -0.0103 86  HIS   A O   
1906 C CB  . HIS   A 86  ? 0.1871 0.1627 0.1456 -0.0157 0.0132  -0.0100 86  HIS   A CB  
1907 C CG  . HIS   A 86  ? 0.1765 0.1615 0.1576 -0.0123 0.0133  -0.0051 86  HIS   A CG  
1908 N ND1 . HIS   A 86  ? 0.1796 0.1675 0.1877 -0.0209 0.0107  0.0041  86  HIS   A ND1 
1909 C CD2 . HIS   A 86  ? 0.1754 0.1627 0.1576 -0.0053 0.0117  -0.0004 86  HIS   A CD2 
1910 C CE1 . HIS   A 86  ? 0.1769 0.1697 0.1831 -0.0134 0.0208  0.0093  86  HIS   A CE1 
1911 N NE2 . HIS   A 86  ? 0.1795 0.1645 0.1670 -0.0003 0.0133  0.0159  86  HIS   A NE2 
1919 N N   . ASN   A 87  ? 0.2165 0.1934 0.1410 -0.0211 0.0238  -0.0248 87  ASN   A N   
1920 C CA  . ASN   A 87  ? 0.2335 0.2137 0.1567 -0.0126 0.0510  -0.0256 87  ASN   A CA  
1921 C C   . ASN   A 87  ? 0.2319 0.2311 0.1904 -0.0136 0.0615  -0.0128 87  ASN   A C   
1922 O O   . ASN   A 87  ? 0.2500 0.2497 0.2317 -0.0209 0.0866  -0.0095 87  ASN   A O   
1923 C CB  . ASN   A 87  ? 0.2527 0.2241 0.1658 -0.0001 0.0558  -0.0250 87  ASN   A CB  
1924 C CG  . ASN   A 87  ? 0.2647 0.2318 0.1718 0.0090  0.0644  -0.0194 87  ASN   A CG  
1925 O OD1 . ASN   A 87  ? 0.2783 0.2350 0.1855 0.0237  0.0601  -0.0055 87  ASN   A OD1 
1926 N ND2 . ASN   A 87  ? 0.2711 0.2459 0.1801 0.0085  0.0664  -0.0190 87  ASN   A ND2 
1933 N N   . LEU   A 88  ? 0.2140 0.2278 0.1859 -0.0259 0.0445  0.0008  88  LEU   A N   
1934 C CA  . LEU   A 88  ? 0.2026 0.2254 0.1958 -0.0373 0.0373  0.0179  88  LEU   A CA  
1935 C C   . LEU   A 88  ? 0.1999 0.2261 0.1883 -0.0406 0.0333  0.0235  88  LEU   A C   
1936 O O   . LEU   A 88  ? 0.2053 0.2416 0.2247 -0.0416 0.0378  0.0460  88  LEU   A O   
1937 C CB  . LEU   A 88  ? 0.2039 0.2353 0.2239 -0.0453 0.0062  0.0243  88  LEU   A CB  
1938 C CG  . LEU   A 88  ? 0.2192 0.2499 0.2579 -0.0454 -0.0070 0.0213  88  LEU   A CG  
1939 C CD1 . LEU   A 88  ? 0.2281 0.2543 0.2568 -0.0515 -0.0076 0.0100  88  LEU   A CD1 
1940 C CD2 . LEU   A 88  ? 0.2331 0.2657 0.2911 -0.0364 -0.0085 0.0156  88  LEU   A CD2 
1952 N N   . ALA   A 89  ? 0.2059 0.2067 0.1558 -0.0366 0.0272  0.0009  89  ALA   A N   
1953 C CA  . ALA   A 89  ? 0.2136 0.2004 0.1334 -0.0356 0.0167  0.0047  89  ALA   A CA  
1954 C C   . ALA   A 89  ? 0.2222 0.2041 0.1389 -0.0308 -0.0001 -0.0051 89  ALA   A C   
1955 O O   . ALA   A 89  ? 0.2227 0.1974 0.1693 -0.0369 -0.0104 -0.0236 89  ALA   A O   
1956 C CB  . ALA   A 89  ? 0.2038 0.1959 0.1203 -0.0279 0.0144  0.0097  89  ALA   A CB  
1962 N N   . LYS   A 90  ? 0.2373 0.2160 0.1276 -0.0351 -0.0250 0.0060  90  LYS   A N   
1963 C CA  . LYS   A 90  ? 0.2461 0.2264 0.1335 -0.0364 -0.0385 0.0072  90  LYS   A CA  
1964 C C   . LYS   A 90  ? 0.2196 0.2065 0.1325 -0.0314 -0.0319 0.0013  90  LYS   A C   
1965 O O   . LYS   A 90  ? 0.2187 0.2229 0.1714 -0.0372 -0.0392 -0.0088 90  LYS   A O   
1966 C CB  . LYS   A 90  ? 0.2754 0.2615 0.1933 -0.0370 -0.0340 0.0193  90  LYS   A CB  
1967 C CG  . LYS   A 90  ? 0.3038 0.2915 0.3009 -0.0345 -0.0256 0.0259  90  LYS   A CG  
1968 C CD  . LYS   A 90  ? 0.3291 0.3159 0.3967 -0.0346 -0.0170 0.0368  90  LYS   A CD  
1969 C CE  . LYS   A 90  ? 0.3482 0.3357 0.4686 -0.0343 -0.0098 0.0409  90  LYS   A CE  
1970 N NZ  . LYS   A 90  ? 0.3646 0.3536 0.5136 -0.0325 -0.0069 0.0393  90  LYS   A NZ  
1984 N N   . HIS   A 91  ? 0.1995 0.1812 0.1073 -0.0234 -0.0352 0.0028  91  HIS   A N   
1985 C CA  . HIS   A 91  ? 0.1766 0.1647 0.1226 -0.0198 -0.0303 0.0083  91  HIS   A CA  
1986 C C   . HIS   A 91  ? 0.1553 0.1487 0.1081 -0.0219 -0.0148 0.0107  91  HIS   A C   
1987 O O   . HIS   A 91  ? 0.1551 0.1636 0.1240 -0.0240 0.0010  0.0082  91  HIS   A O   
1988 C CB  . HIS   A 91  ? 0.1914 0.1889 0.1699 0.0069  -0.0481 0.0033  91  HIS   A CB  
1989 C CG  . HIS   A 91  ? 0.2373 0.2363 0.2532 0.0144  -0.0756 -0.0033 91  HIS   A CG  
1990 N ND1 . HIS   A 91  ? 0.2482 0.2647 0.2925 0.0198  -0.0851 -0.0224 91  HIS   A ND1 
1991 C CD2 . HIS   A 91  ? 0.2629 0.2580 0.2785 0.0185  -0.0839 0.0081  91  HIS   A CD2 
1992 C CE1 . HIS   A 91  ? 0.2601 0.2729 0.3077 0.0208  -0.0897 -0.0084 91  HIS   A CE1 
1993 N NE2 . HIS   A 91  ? 0.2742 0.2717 0.3032 0.0218  -0.0893 0.0008  91  HIS   A NE2 
2001 N N   . CYS   A 92  ? 0.1411 0.1444 0.1170 -0.0200 -0.0093 0.0018  92  CYS   A N   
2002 C CA  . CYS   A 92  ? 0.1298 0.1371 0.1225 -0.0147 -0.0041 0.0018  92  CYS   A CA  
2003 C C   . CYS   A 92  ? 0.1243 0.1329 0.1145 -0.0129 0.0036  0.0019  92  CYS   A C   
2004 O O   . CYS   A 92  ? 0.1253 0.1398 0.1308 -0.0148 -0.0020 0.0011  92  CYS   A O   
2005 C CB  . CYS   A 92  ? 0.1306 0.1398 0.1349 -0.0061 -0.0088 0.0010  92  CYS   A CB  
2006 S SG  . CYS   A 92  ? 0.1305 0.1262 0.1419 -0.0146 -0.0018 0.0017  92  CYS   A SG  
2012 N N   . LEU   A 93  ? 0.1191 0.1209 0.1245 -0.0096 0.0067  0.0073  93  LEU   A N   
2013 C CA  . LEU   A 93  ? 0.1106 0.1200 0.1259 -0.0093 0.0072  0.0034  93  LEU   A CA  
2014 C C   . LEU   A 93  ? 0.1105 0.1071 0.1262 -0.0043 0.0040  0.0011  93  LEU   A C   
2015 O O   . LEU   A 93  ? 0.1079 0.1167 0.1197 -0.0043 -0.0010 0.0074  93  LEU   A O   
2016 C CB  . LEU   A 93  ? 0.1216 0.1175 0.1388 -0.0099 -0.0032 0.0152  93  LEU   A CB  
2017 C CG  . LEU   A 93  ? 0.1302 0.1176 0.1272 -0.0082 -0.0025 0.0124  93  LEU   A CG  
2018 C CD1 . LEU   A 93  ? 0.1384 0.1177 0.1680 -0.0024 0.0030  0.0062  93  LEU   A CD1 
2019 C CD2 . LEU   A 93  ? 0.1391 0.1177 0.1486 -0.0085 -0.0026 0.0117  93  LEU   A CD2 
2031 N N   . HIS   A 94  ? 0.1035 0.1046 0.1169 -0.0024 0.0038  0.0060  94  HIS   A N   
2032 C CA  . HIS   A 94  ? 0.1048 0.1086 0.1199 -0.0058 -0.0026 0.0087  94  HIS   A CA  
2033 C C   . HIS   A 94  ? 0.1008 0.1041 0.1281 -0.0111 -0.0008 0.0052  94  HIS   A C   
2034 O O   . HIS   A 94  ? 0.1028 0.1251 0.1550 -0.0007 0.0025  -0.0114 94  HIS   A O   
2035 C CB  . HIS   A 94  ? 0.1047 0.1063 0.1288 -0.0047 -0.0050 0.0071  94  HIS   A CB  
2036 C CG  . HIS   A 94  ? 0.1054 0.1110 0.1289 -0.0060 -0.0049 0.0086  94  HIS   A CG  
2037 N ND1 . HIS   A 94  ? 0.1080 0.1071 0.1338 -0.0029 0.0040  0.0089  94  HIS   A ND1 
2038 C CD2 . HIS   A 94  ? 0.1182 0.1196 0.1296 -0.0047 -0.0056 0.0009  94  HIS   A CD2 
2039 C CE1 . HIS   A 94  ? 0.1152 0.1097 0.1326 -0.0112 -0.0136 0.0006  94  HIS   A CE1 
2040 N NE2 . HIS   A 94  ? 0.1213 0.1140 0.1380 -0.0109 -0.0078 -0.0039 94  HIS   A NE2 
2048 N N   . VAL   A 95  ? 0.0996 0.0989 0.1043 -0.0041 0.0076  -0.0021 95  VAL   A N   
2049 C CA  . VAL   A 95  ? 0.1069 0.1049 0.1146 -0.0032 0.0053  0.0064  95  VAL   A CA  
2050 C C   . VAL   A 95  ? 0.1086 0.1020 0.1017 -0.0116 0.0022  0.0019  95  VAL   A C   
2051 O O   . VAL   A 95  ? 0.1126 0.1142 0.1116 0.0067  0.0056  -0.0023 95  VAL   A O   
2052 C CB  . VAL   A 95  ? 0.1091 0.1059 0.1313 -0.0090 0.0061  0.0049  95  VAL   A CB  
2053 C CG1 . VAL   A 95  ? 0.1284 0.1137 0.1504 -0.0183 0.0037  -0.0079 95  VAL   A CG1 
2054 C CG2 . VAL   A 95  ? 0.1172 0.1140 0.1345 -0.0143 0.0049  0.0154  95  VAL   A CG2 
2064 N N   . VAL   A 96  ? 0.1153 0.1069 0.1033 -0.0039 0.0052  0.0063  96  VAL   A N   
2065 C CA  . VAL   A 96  ? 0.1279 0.1090 0.1170 -0.0023 0.0101  0.0108  96  VAL   A CA  
2066 C C   . VAL   A 96  ? 0.1278 0.1136 0.1108 -0.0010 0.0145  0.0120  96  VAL   A C   
2067 O O   . VAL   A 96  ? 0.1314 0.1191 0.1370 -0.0053 0.0154  -0.0093 96  VAL   A O   
2068 C CB  . VAL   A 96  ? 0.1271 0.1117 0.1266 -0.0030 0.0215  0.0089  96  VAL   A CB  
2069 C CG1 . VAL   A 96  ? 0.1381 0.1173 0.1208 0.0002  0.0198  0.0113  96  VAL   A CG1 
2070 C CG2 . VAL   A 96  ? 0.1240 0.1207 0.1518 -0.0141 0.0117  0.0140  96  VAL   A CG2 
2080 N N   . GLY   A 97  ? 0.1234 0.1156 0.1113 -0.0056 0.0072  0.0039  97  GLY   A N   
2081 C CA  . GLY   A 97  ? 0.1297 0.1262 0.1186 -0.0054 -0.0010 0.0076  97  GLY   A CA  
2082 C C   . GLY   A 97  ? 0.1317 0.1429 0.1011 -0.0075 0.0013  0.0026  97  GLY   A C   
2083 O O   . GLY   A 97  ? 0.1492 0.1412 0.1286 -0.0104 -0.0015 0.0118  97  GLY   A O   
2087 N N   A PRO   A 98  ? 0.1362 0.1485 0.0948 0.0005  -0.0065 0.0019  98  PRO   A N   
2088 N N   B PRO   A 98  ? 0.1411 0.1409 0.0998 -0.0014 0.0000  0.0186  98  PRO   A N   
2089 C CA  A PRO   A 98  ? 0.1426 0.1635 0.0981 0.0012  0.0001  -0.0040 98  PRO   A CA  
2090 C CA  B PRO   A 98  ? 0.1577 0.1603 0.1202 -0.0077 -0.0007 0.0150  98  PRO   A CA  
2091 C C   A PRO   A 98  ? 0.1383 0.1725 0.0925 -0.0018 0.0060  0.0095  98  PRO   A C   
2092 C C   B PRO   A 98  ? 0.1786 0.1687 0.1258 -0.0202 -0.0064 0.0370  98  PRO   A C   
2093 O O   A PRO   A 98  ? 0.1351 0.1626 0.1082 0.0021  -0.0042 0.0103  98  PRO   A O   
2094 O O   B PRO   A 98  ? 0.1683 0.1502 0.1557 -0.0211 -0.0092 0.0287  98  PRO   A O   
2095 C CB  A PRO   A 98  ? 0.1517 0.1725 0.0984 0.0059  -0.0073 -0.0154 98  PRO   A CB  
2096 C CB  B PRO   A 98  ? 0.1630 0.1714 0.1136 0.0051  -0.0033 -0.0008 98  PRO   A CB  
2097 C CG  A PRO   A 98  ? 0.1513 0.1629 0.1110 0.0053  -0.0109 -0.0202 98  PRO   A CG  
2098 C CG  B PRO   A 98  ? 0.1684 0.1609 0.1308 0.0045  -0.0024 -0.0032 98  PRO   A CG  
2099 C CD  A PRO   A 98  ? 0.1418 0.1509 0.1007 0.0027  -0.0110 -0.0098 98  PRO   A CD  
2100 C CD  B PRO   A 98  ? 0.1512 0.1394 0.1061 0.0041  -0.0026 0.0087  98  PRO   A CD  
2115 N N   A ASN   A 99  ? 0.1353 0.1871 0.0818 -0.0010 0.0120  0.0201  99  ASN   A N   
2116 N N   B ASN   A 99  ? 0.2118 0.1907 0.1335 -0.0178 -0.0167 0.0586  99  ASN   A N   
2117 C CA  A ASN   A 99  ? 0.1420 0.1862 0.0779 -0.0045 0.0193  0.0333  99  ASN   A CA  
2118 C CA  B ASN   A 99  ? 0.2495 0.2055 0.1674 -0.0163 -0.0291 0.0733  99  ASN   A CA  
2119 C C   A ASN   A 99  ? 0.1630 0.2074 0.0766 -0.0189 0.0206  0.0436  99  ASN   A C   
2120 C C   B ASN   A 99  ? 0.2703 0.2299 0.1486 -0.0190 -0.0336 0.0627  99  ASN   A C   
2121 O O   A ASN   A 99  ? 0.1726 0.2034 0.0760 -0.0167 0.0188  0.0385  99  ASN   A O   
2122 O O   B ASN   A 99  ? 0.2774 0.2266 0.1639 -0.0117 -0.0407 0.0472  99  ASN   A O   
2123 C CB  A ASN   A 99  ? 0.1338 0.1725 0.0797 -0.0004 0.0104  0.0305  99  ASN   A CB  
2124 C CB  B ASN   A 99  ? 0.2648 0.2093 0.2466 -0.0153 -0.0426 0.0731  99  ASN   A CB  
2125 C CG  A ASN   A 99  ? 0.1345 0.1597 0.0921 0.0093  -0.0018 0.0213  99  ASN   A CG  
2126 C CG  B ASN   A 99  ? 0.2798 0.2197 0.3214 -0.0158 -0.0497 0.0688  99  ASN   A CG  
2127 O OD1 A ASN   A 99  ? 0.1484 0.1573 0.1043 0.0084  -0.0009 0.0245  99  ASN   A OD1 
2128 O OD1 B ASN   A 99  ? 0.2903 0.2177 0.3461 -0.0159 -0.0531 0.0696  99  ASN   A OD1 
2129 N ND2 A ASN   A 99  ? 0.1322 0.1439 0.1070 0.0012  -0.0135 0.0308  99  ASN   A ND2 
2130 N ND2 B ASN   A 99  ? 0.2845 0.2290 0.3582 -0.0169 -0.0539 0.0558  99  ASN   A ND2 
2143 N N   A VAL   A 100 ? 0.1831 0.2283 0.1035 -0.0261 -0.0101 0.0569  100 VAL   A N   
2144 N N   B VAL   A 100 ? 0.2825 0.2504 0.1408 -0.0246 -0.0489 0.0501  100 VAL   A N   
2145 C CA  A VAL   A 100 ? 0.2138 0.2558 0.1601 -0.0249 -0.0258 0.0646  100 VAL   A CA  
2146 C CA  B VAL   A 100 ? 0.3012 0.2723 0.1718 -0.0294 -0.0529 0.0456  100 VAL   A CA  
2147 C C   A VAL   A 100 ? 0.2371 0.2772 0.1914 -0.0263 -0.0305 0.0880  100 VAL   A C   
2148 C C   B VAL   A 100 ? 0.3155 0.2877 0.1597 -0.0299 -0.0525 0.0660  100 VAL   A C   
2149 O O   A VAL   A 100 ? 0.2440 0.2888 0.2138 -0.0252 -0.0193 0.0820  100 VAL   A O   
2150 O O   B VAL   A 100 ? 0.3186 0.2873 0.1628 -0.0270 -0.0363 0.0598  100 VAL   A O   
2151 C CB  A VAL   A 100 ? 0.2237 0.2557 0.1871 -0.0238 -0.0383 0.0570  100 VAL   A CB  
2152 C CB  B VAL   A 100 ? 0.3079 0.2728 0.2161 -0.0357 -0.0581 0.0300  100 VAL   A CB  
2153 C CG1 A VAL   A 100 ? 0.2243 0.2589 0.2056 -0.0280 -0.0395 0.0513  100 VAL   A CG1 
2154 C CG1 B VAL   A 100 ? 0.3073 0.2739 0.2357 -0.0357 -0.0579 0.0240  100 VAL   A CG1 
2155 C CG2 A VAL   A 100 ? 0.2297 0.2550 0.1947 -0.0207 -0.0448 0.0513  100 VAL   A CG2 
2156 C CG2 B VAL   A 100 ? 0.3131 0.2753 0.2337 -0.0388 -0.0561 0.0226  100 VAL   A CG2 
2175 N N   A ASN   A 101 ? 0.2547 0.2833 0.2129 -0.0279 -0.0334 0.1178  101 ASN   A N   
2176 N N   B ASN   A 101 ? 0.3294 0.3079 0.1893 -0.0338 -0.0507 0.0907  101 ASN   A N   
2177 C CA  A ASN   A 101 ? 0.2811 0.2887 0.2438 -0.0278 -0.0327 0.1309  101 ASN   A CA  
2178 C CA  B ASN   A 101 ? 0.3518 0.3330 0.2329 -0.0358 -0.0491 0.0970  101 ASN   A CA  
2179 C C   A ASN   A 101 ? 0.3046 0.3037 0.2549 -0.0357 -0.0127 0.1549  101 ASN   A C   
2180 C C   B ASN   A 101 ? 0.3775 0.3666 0.2753 -0.0392 -0.0282 0.1123  101 ASN   A C   
2181 O O   A ASN   A 101 ? 0.3132 0.3051 0.2634 -0.0360 -0.0137 0.1658  101 ASN   A O   
2182 O O   B ASN   A 101 ? 0.3855 0.3673 0.3057 -0.0395 -0.0212 0.1125  101 ASN   A O   
2183 C CB  A ASN   A 101 ? 0.2835 0.2768 0.2483 -0.0187 -0.0542 0.1210  101 ASN   A CB  
2184 C CB  B ASN   A 101 ? 0.3484 0.3269 0.2282 -0.0336 -0.0737 0.0823  101 ASN   A CB  
2185 C CG  A ASN   A 101 ? 0.2856 0.2663 0.2499 -0.0142 -0.0655 0.0959  101 ASN   A CG  
2186 C CG  B ASN   A 101 ? 0.3448 0.3222 0.2241 -0.0346 -0.0902 0.0563  101 ASN   A CG  
2187 O OD1 A ASN   A 101 ? 0.2913 0.2707 0.2672 -0.0096 -0.0588 0.0712  101 ASN   A OD1 
2188 O OD1 B ASN   A 101 ? 0.3439 0.3298 0.2336 -0.0233 -0.0982 0.0296  101 ASN   A OD1 
2189 N ND2 A ASN   A 101 ? 0.2861 0.2553 0.2386 -0.0178 -0.0713 0.0969  101 ASN   A ND2 
2190 N ND2 B ASN   A 101 ? 0.3418 0.3135 0.2117 -0.0438 -0.0919 0.0555  101 ASN   A ND2 
2203 N N   A LYS   A 102 ? 0.3179 0.3217 0.2789 -0.0425 -0.0005 0.1391  102 LYS   A N   
2204 N N   B LYS   A 102 ? 0.3925 0.4046 0.3056 -0.0404 -0.0265 0.1071  102 LYS   A N   
2205 C CA  A LYS   A 102 ? 0.3340 0.3399 0.2870 -0.0438 -0.0006 0.1157  102 LYS   A CA  
2206 C CA  B LYS   A 102 ? 0.4081 0.4391 0.3204 -0.0353 -0.0321 0.0957  102 LYS   A CA  
2207 C C   A LYS   A 102 ? 0.3436 0.3527 0.2632 -0.0355 -0.0060 0.1152  102 LYS   A C   
2208 C C   B LYS   A 102 ? 0.4059 0.4514 0.2999 -0.0318 -0.0261 0.0882  102 LYS   A C   
2209 O O   A LYS   A 102 ? 0.3466 0.3540 0.2421 -0.0297 -0.0091 0.1321  102 LYS   A O   
2210 O O   B LYS   A 102 ? 0.4084 0.4578 0.2997 -0.0287 -0.0223 0.0880  102 LYS   A O   
2211 C CB  A LYS   A 102 ? 0.3402 0.3434 0.3098 -0.0532 0.0018  0.0954  102 LYS   A CB  
2212 C CB  B LYS   A 102 ? 0.4235 0.4571 0.3457 -0.0318 -0.0416 0.0872  102 LYS   A CB  
2213 C CG  A LYS   A 102 ? 0.3462 0.3440 0.3257 -0.0604 0.0010  0.0746  102 LYS   A CG  
2214 C CG  B LYS   A 102 ? 0.4369 0.4710 0.3611 -0.0278 -0.0506 0.0767  102 LYS   A CG  
2215 C CD  A LYS   A 102 ? 0.3533 0.3468 0.3379 -0.0637 -0.0027 0.0543  102 LYS   A CD  
2216 C CD  B LYS   A 102 ? 0.4476 0.4830 0.3686 -0.0245 -0.0618 0.0662  102 LYS   A CD  
2217 C CE  A LYS   A 102 ? 0.3586 0.3482 0.3470 -0.0658 -0.0047 0.0397  102 LYS   A CE  
2218 C CE  B LYS   A 102 ? 0.4565 0.4920 0.3720 -0.0216 -0.0703 0.0581  102 LYS   A CE  
2219 N NZ  A LYS   A 102 ? 0.3609 0.3468 0.3505 -0.0711 -0.0027 0.0315  102 LYS   A NZ  
2220 N NZ  B LYS   A 102 ? 0.4618 0.4969 0.3702 -0.0201 -0.0713 0.0521  102 LYS   A NZ  
2247 N N   A GLY   A 103 ? 0.3472 0.3652 0.2609 -0.0302 -0.0091 0.0896  103 GLY   A N   
2248 N N   B GLY   A 103 ? 0.3976 0.4559 0.2887 -0.0306 -0.0253 0.0699  103 GLY   A N   
2249 C CA  A GLY   A 103 ? 0.3498 0.3730 0.2538 -0.0274 -0.0096 0.0712  103 GLY   A CA  
2250 C CA  B GLY   A 103 ? 0.3870 0.4542 0.2669 -0.0307 -0.0219 0.0573  103 GLY   A CA  
2251 C C   A GLY   A 103 ? 0.3493 0.3806 0.2524 -0.0266 -0.0051 0.0478  103 GLY   A C   
2252 C C   B GLY   A 103 ? 0.3726 0.4509 0.2573 -0.0320 -0.0128 0.0395  103 GLY   A C   
2253 O O   A GLY   A 103 ? 0.3544 0.3850 0.2695 -0.0251 -0.0042 0.0379  103 GLY   A O   
2254 O O   B GLY   A 103 ? 0.3797 0.4579 0.2764 -0.0299 -0.0091 0.0228  103 GLY   A O   
2261 N N   A GLU   A 104 ? 0.3401 0.3794 0.2178 -0.0294 0.0001  0.0382  104 GLU   A N   
2262 N N   B GLU   A 104 ? 0.3466 0.4351 0.2080 -0.0392 -0.0059 0.0389  104 GLU   A N   
2263 C CA  A GLU   A 104 ? 0.3276 0.3758 0.1961 -0.0328 0.0005  0.0255  104 GLU   A CA  
2264 C CA  B GLU   A 104 ? 0.3158 0.4156 0.1732 -0.0496 -0.0022 0.0350  104 GLU   A CA  
2265 C C   A GLU   A 104 ? 0.3174 0.3798 0.1853 -0.0347 0.0058  0.0097  104 GLU   A C   
2266 C C   B GLU   A 104 ? 0.3100 0.4243 0.1730 -0.0468 -0.0014 0.0074  104 GLU   A C   
2267 O O   A GLU   A 104 ? 0.3149 0.3780 0.1825 -0.0373 0.0045  0.0054  104 GLU   A O   
2268 O O   B GLU   A 104 ? 0.3079 0.4257 0.1845 -0.0496 -0.0023 -0.0022 104 GLU   A O   
2269 C CB  A GLU   A 104 ? 0.3241 0.3688 0.1900 -0.0327 -0.0041 0.0325  104 GLU   A CB  
2270 C CB  B GLU   A 104 ? 0.2876 0.3872 0.1481 -0.0632 0.0027  0.0594  104 GLU   A CB  
2271 C CG  A GLU   A 104 ? 0.3228 0.3630 0.1955 -0.0303 -0.0078 0.0400  104 GLU   A CG  
2272 C CG  B GLU   A 104 ? 0.2632 0.3617 0.1511 -0.0705 0.0057  0.0784  104 GLU   A CG  
2273 C CD  A GLU   A 104 ? 0.3201 0.3579 0.2015 -0.0290 -0.0096 0.0442  104 GLU   A CD  
2274 C CD  B GLU   A 104 ? 0.2362 0.3432 0.1486 -0.0803 0.0084  0.0877  104 GLU   A CD  
2275 O OE1 A GLU   A 104 ? 0.3174 0.3547 0.1931 -0.0269 -0.0091 0.0461  104 GLU   A OE1 
2276 O OE1 B GLU   A 104 ? 0.2157 0.3267 0.1309 -0.0700 0.0011  0.0799  104 GLU   A OE1 
2277 O OE2 A GLU   A 104 ? 0.3229 0.3576 0.2138 -0.0270 -0.0093 0.0454  104 GLU   A OE2 
2278 O OE2 B GLU   A 104 ? 0.2355 0.3336 0.1761 -0.0801 0.0152  0.0951  104 GLU   A OE2 
2291 N N   A ASP   A 105 ? 0.3084 0.3856 0.1962 -0.0346 0.0149  -0.0025 105 ASP   A N   
2292 N N   B ASP   A 105 ? 0.2991 0.4277 0.1656 -0.0435 0.0105  -0.0140 105 ASP   A N   
2293 C CA  A ASP   A 105 ? 0.2989 0.3892 0.2227 -0.0325 0.0178  -0.0201 105 ASP   A CA  
2294 C CA  B ASP   A 105 ? 0.2916 0.4265 0.1957 -0.0368 0.0059  -0.0419 105 ASP   A CA  
2295 C C   A ASP   A 105 ? 0.2727 0.3754 0.2012 -0.0386 0.0094  -0.0307 105 ASP   A C   
2296 C C   B ASP   A 105 ? 0.2567 0.4124 0.1641 -0.0462 -0.0033 -0.0581 105 ASP   A C   
2297 O O   A ASP   A 105 ? 0.2621 0.3734 0.1708 -0.0389 0.0099  -0.0389 105 ASP   A O   
2298 O O   B ASP   A 105 ? 0.2315 0.3888 0.1266 -0.0442 -0.0047 -0.0732 105 ASP   A O   
2299 C CB  A ASP   A 105 ? 0.3129 0.4027 0.2734 -0.0268 0.0274  -0.0263 105 ASP   A CB  
2300 C CB  B ASP   A 105 ? 0.3169 0.4464 0.2681 -0.0238 0.0090  -0.0500 105 ASP   A CB  
2301 C CG  A ASP   A 105 ? 0.3249 0.4128 0.3179 -0.0211 0.0353  -0.0325 105 ASP   A CG  
2302 C CG  B ASP   A 105 ? 0.3411 0.4616 0.3250 -0.0131 0.0093  -0.0595 105 ASP   A CG  
2303 O OD1 A ASP   A 105 ? 0.3286 0.4173 0.3309 -0.0214 0.0343  -0.0397 105 ASP   A OD1 
2304 O OD1 B ASP   A 105 ? 0.3495 0.4650 0.3341 -0.0101 0.0085  -0.0686 105 ASP   A OD1 
2305 O OD2 A ASP   A 105 ? 0.3288 0.4161 0.3375 -0.0200 0.0457  -0.0335 105 ASP   A OD2 
2306 O OD2 B ASP   A 105 ? 0.3563 0.4679 0.3589 -0.0088 0.0106  -0.0608 105 ASP   A OD2 
2315 N N   A ILE   A 106 ? 0.2565 0.3614 0.2136 -0.0442 -0.0073 -0.0353 106 ILE   A N   
2316 N N   B ILE   A 106 ? 0.2431 0.3944 0.1907 -0.0509 -0.0200 -0.0585 106 ILE   A N   
2317 C CA  A ILE   A 106 ? 0.2369 0.3441 0.2214 -0.0524 -0.0211 -0.0472 106 ILE   A CA  
2318 C CA  B ILE   A 106 ? 0.2211 0.3789 0.2082 -0.0581 -0.0304 -0.0707 106 ILE   A CA  
2319 C C   A ILE   A 106 ? 0.2267 0.3266 0.2301 -0.0630 -0.0144 -0.0647 106 ILE   A C   
2320 C C   B ILE   A 106 ? 0.2030 0.3463 0.2142 -0.0752 -0.0340 -0.1002 106 ILE   A C   
2321 O O   A ILE   A 106 ? 0.2157 0.3204 0.2219 -0.0665 -0.0101 -0.0740 106 ILE   A O   
2322 O O   B ILE   A 106 ? 0.1881 0.3327 0.2217 -0.0752 -0.0065 -0.1084 106 ILE   A O   
2323 C CB  A ILE   A 106 ? 0.2309 0.3450 0.2350 -0.0459 -0.0399 -0.0351 106 ILE   A CB  
2324 C CB  B ILE   A 106 ? 0.2209 0.3907 0.2394 -0.0425 -0.0313 -0.0525 106 ILE   A CB  
2325 C CG1 A ILE   A 106 ? 0.2206 0.3436 0.2434 -0.0385 -0.0544 -0.0245 106 ILE   A CG1 
2326 C CG1 B ILE   A 106 ? 0.2134 0.3919 0.2631 -0.0279 -0.0277 -0.0367 106 ILE   A CG1 
2327 C CG2 A ILE   A 106 ? 0.2326 0.3463 0.2395 -0.0445 -0.0411 -0.0360 106 ILE   A CG2 
2328 C CG2 B ILE   A 106 ? 0.2259 0.3967 0.2570 -0.0412 -0.0310 -0.0461 106 ILE   A CG2 
2329 C CD1 A ILE   A 106 ? 0.2158 0.3402 0.2483 -0.0323 -0.0592 -0.0198 106 ILE   A CD1 
2330 C CD1 B ILE   A 106 ? 0.2121 0.3902 0.2721 -0.0154 -0.0275 -0.0270 106 ILE   A CD1 
2353 N N   A GLN   A 107 ? 0.2346 0.3140 0.2537 -0.0641 -0.0014 -0.0710 107 GLN   A N   
2354 N N   B GLN   A 107 ? 0.2219 0.3313 0.2522 -0.0771 -0.0331 -0.1001 107 GLN   A N   
2355 C CA  A GLN   A 107 ? 0.2461 0.3006 0.3032 -0.0570 0.0135  -0.0747 107 GLN   A CA  
2356 C CA  B GLN   A 107 ? 0.2461 0.3139 0.3143 -0.0630 -0.0099 -0.0959 107 GLN   A CA  
2357 C C   A GLN   A 107 ? 0.2228 0.2605 0.2890 -0.0497 0.0235  -0.0636 107 GLN   A C   
2358 C C   B GLN   A 107 ? 0.2204 0.2656 0.3013 -0.0518 0.0158  -0.0729 107 GLN   A C   
2359 O O   A GLN   A 107 ? 0.2312 0.2569 0.3300 -0.0439 0.0319  -0.0530 107 GLN   A O   
2360 O O   B GLN   A 107 ? 0.2221 0.2563 0.3397 -0.0400 0.0384  -0.0677 107 GLN   A O   
2361 C CB  A GLN   A 107 ? 0.2755 0.3227 0.3696 -0.0621 0.0134  -0.0793 107 GLN   A CB  
2362 C CB  B GLN   A 107 ? 0.2924 0.3403 0.3984 -0.0669 -0.0218 -0.0922 107 GLN   A CB  
2363 C CG  A GLN   A 107 ? 0.3034 0.3446 0.4392 -0.0632 0.0096  -0.0782 107 GLN   A CG  
2364 C CG  B GLN   A 107 ? 0.3362 0.3669 0.4854 -0.0682 -0.0309 -0.0766 107 GLN   A CG  
2365 C CD  A GLN   A 107 ? 0.3266 0.3614 0.4982 -0.0637 0.0087  -0.0736 107 GLN   A CD  
2366 C CD  B GLN   A 107 ? 0.3681 0.3910 0.5587 -0.0644 -0.0347 -0.0596 107 GLN   A CD  
2367 O OE1 A GLN   A 107 ? 0.3370 0.3698 0.5234 -0.0617 0.0074  -0.0759 107 GLN   A OE1 
2368 O OE1 B GLN   A 107 ? 0.3830 0.3996 0.5828 -0.0634 -0.0323 -0.0522 107 GLN   A OE1 
2369 N NE2 A GLN   A 107 ? 0.3336 0.3643 0.5150 -0.0668 0.0088  -0.0734 107 GLN   A NE2 
2370 N NE2 B GLN   A 107 ? 0.3837 0.4006 0.5856 -0.0640 -0.0372 -0.0563 107 GLN   A NE2 
2387 N N   . LEU   A 108 ? 0.1912 0.2207 0.2432 -0.0476 0.0231  -0.0709 108 LEU   A N   
2388 C CA  . LEU   A 108 ? 0.1677 0.1687 0.1935 -0.0146 0.0187  -0.0171 108 LEU   A CA  
2389 C C   . LEU   A 108 ? 0.1427 0.1337 0.1900 -0.0022 0.0124  0.0114  108 LEU   A C   
2390 O O   . LEU   A 108 ? 0.1393 0.1399 0.2005 -0.0003 0.0208  0.0133  108 LEU   A O   
2391 C CB  . LEU   A 108 ? 0.1702 0.1735 0.1705 -0.0152 0.0245  -0.0138 108 LEU   A CB  
2392 C CG  . LEU   A 108 ? 0.1888 0.2033 0.1954 -0.0159 0.0377  -0.0157 108 LEU   A CG  
2393 C CD1 . LEU   A 108 ? 0.2124 0.2145 0.1834 -0.0250 0.0489  -0.0175 108 LEU   A CD1 
2394 C CD2 . LEU   A 108 ? 0.1903 0.2317 0.2399 -0.0069 0.0371  -0.0016 108 LEU   A CD2 
2407 N N   . LEU   A 109 ? 0.1316 0.1348 0.1963 0.0012  0.0120  0.0296  109 LEU   A N   
2408 C CA  . LEU   A 109 ? 0.1294 0.1321 0.1770 0.0006  0.0040  0.0306  109 LEU   A CA  
2409 C C   . LEU   A 109 ? 0.1168 0.1211 0.1586 -0.0067 -0.0006 0.0114  109 LEU   A C   
2410 O O   . LEU   A 109 ? 0.1316 0.1144 0.1710 -0.0038 -0.0082 0.0075  109 LEU   A O   
2411 C CB  . LEU   A 109 ? 0.1367 0.1423 0.1892 0.0056  -0.0103 0.0447  109 LEU   A CB  
2412 C CG  . LEU   A 109 ? 0.1347 0.1448 0.2004 0.0012  0.0032  0.0444  109 LEU   A CG  
2413 C CD1 . LEU   A 109 ? 0.1425 0.1325 0.2200 -0.0017 0.0125  0.0162  109 LEU   A CD1 
2414 C CD2 . LEU   A 109 ? 0.1339 0.1600 0.2219 0.0073  0.0020  0.0412  109 LEU   A CD2 
2426 N N   . LYS   A 110 ? 0.1237 0.1165 0.1537 -0.0055 -0.0037 0.0083  110 LYS   A N   
2427 C CA  . LYS   A 110 ? 0.1188 0.1140 0.1534 -0.0069 -0.0072 0.0086  110 LYS   A CA  
2428 C C   . LYS   A 110 ? 0.1212 0.1054 0.1374 -0.0028 -0.0050 0.0060  110 LYS   A C   
2429 O O   . LYS   A 110 ? 0.1223 0.1095 0.1545 -0.0070 -0.0005 -0.0017 110 LYS   A O   
2430 C CB  . LYS   A 110 ? 0.1334 0.1181 0.1621 -0.0056 -0.0148 -0.0050 110 LYS   A CB  
2431 C CG  . LYS   A 110 ? 0.1375 0.1137 0.1781 -0.0064 -0.0089 -0.0019 110 LYS   A CG  
2432 C CD  . LYS   A 110 ? 0.1392 0.1211 0.1869 -0.0104 -0.0131 -0.0041 110 LYS   A CD  
2433 C CE  . LYS   A 110 ? 0.1509 0.1270 0.2129 -0.0083 0.0023  -0.0062 110 LYS   A CE  
2434 N NZ  . LYS   A 110 ? 0.1532 0.1331 0.2192 -0.0139 0.0083  0.0036  110 LYS   A NZ  
2448 N N   . SER   A 111 ? 0.1266 0.1167 0.1385 -0.0008 -0.0080 0.0056  111 SER   A N   
2449 C CA  . SER   A 111 ? 0.1262 0.1205 0.1523 -0.0006 0.0005  0.0078  111 SER   A CA  
2450 C C   . SER   A 111 ? 0.1119 0.1118 0.1555 -0.0080 0.0039  0.0124  111 SER   A C   
2451 O O   . SER   A 111 ? 0.1272 0.1040 0.1712 -0.0004 0.0016  0.0091  111 SER   A O   
2452 C CB  . SER   A 111 ? 0.1377 0.1401 0.1686 0.0000  0.0102  -0.0120 111 SER   A CB  
2453 O OG  . SER   A 111 ? 0.1893 0.1604 0.1809 0.0001  0.0124  -0.0143 111 SER   A OG  
2459 N N   . ALA   A 112 ? 0.1148 0.1023 0.1604 -0.0004 0.0062  0.0044  112 ALA   A N   
2460 C CA  . ALA   A 112 ? 0.1218 0.1021 0.1480 -0.0027 0.0101  0.0052  112 ALA   A CA  
2461 C C   . ALA   A 112 ? 0.1140 0.0994 0.1513 -0.0029 -0.0013 0.0014  112 ALA   A C   
2462 O O   . ALA   A 112 ? 0.1194 0.1029 0.1547 -0.0124 0.0053  0.0041  112 ALA   A O   
2463 C CB  . ALA   A 112 ? 0.1330 0.1004 0.1561 -0.0072 0.0036  0.0036  112 ALA   A CB  
2469 N N   . TYR   A 113 ? 0.1073 0.1005 0.1631 -0.0033 -0.0004 0.0096  113 TYR   A N   
2470 C CA  . TYR   A 113 ? 0.1067 0.1021 0.1539 -0.0050 0.0035  0.0119  113 TYR   A CA  
2471 C C   . TYR   A 113 ? 0.1064 0.1030 0.1391 -0.0127 0.0010  0.0052  113 TYR   A C   
2472 O O   . TYR   A 113 ? 0.1112 0.1085 0.1495 -0.0039 0.0088  0.0014  113 TYR   A O   
2473 C CB  . TYR   A 113 ? 0.1082 0.1093 0.1631 -0.0057 -0.0088 0.0167  113 TYR   A CB  
2474 C CG  . TYR   A 113 ? 0.1098 0.1143 0.1594 -0.0109 0.0048  0.0264  113 TYR   A CG  
2475 C CD1 . TYR   A 113 ? 0.1111 0.1244 0.1480 -0.0039 0.0042  0.0255  113 TYR   A CD1 
2476 C CD2 . TYR   A 113 ? 0.1149 0.1259 0.1607 -0.0173 -0.0007 0.0234  113 TYR   A CD2 
2477 C CE1 . TYR   A 113 ? 0.1178 0.1366 0.1531 0.0006  0.0057  0.0332  113 TYR   A CE1 
2478 C CE2 . TYR   A 113 ? 0.1135 0.1345 0.1541 -0.0142 -0.0024 0.0270  113 TYR   A CE2 
2479 C CZ  . TYR   A 113 ? 0.1111 0.1376 0.1460 0.0012  0.0081  0.0372  113 TYR   A CZ  
2480 O OH  . TYR   A 113 ? 0.1127 0.1501 0.1752 0.0128  0.0068  0.0387  113 TYR   A OH  
2490 N N   . GLU   A 114 ? 0.1069 0.1045 0.1540 -0.0044 0.0041  0.0089  114 GLU   A N   
2491 C CA  . GLU   A 114 ? 0.1100 0.0980 0.1682 0.0007  -0.0026 0.0153  114 GLU   A CA  
2492 C C   . GLU   A 114 ? 0.1068 0.1042 0.1600 0.0040  0.0054  0.0025  114 GLU   A C   
2493 O O   . GLU   A 114 ? 0.1226 0.1079 0.1569 0.0023  -0.0058 0.0030  114 GLU   A O   
2494 C CB  . GLU   A 114 ? 0.1078 0.1031 0.1647 -0.0055 -0.0009 0.0082  114 GLU   A CB  
2495 C CG  . GLU   A 114 ? 0.1230 0.1026 0.1671 0.0060  -0.0037 -0.0002 114 GLU   A CG  
2496 C CD  . GLU   A 114 ? 0.1282 0.1048 0.1804 0.0006  -0.0023 0.0001  114 GLU   A CD  
2497 O OE1 . GLU   A 114 ? 0.1296 0.1137 0.1772 -0.0083 0.0091  -0.0094 114 GLU   A OE1 
2498 O OE2 . GLU   A 114 ? 0.1436 0.1127 0.1929 -0.0086 0.0008  -0.0125 114 GLU   A OE2 
2505 N N   . ASN   A 115 ? 0.1126 0.1036 0.1411 -0.0053 0.0014  -0.0006 115 ASN   A N   
2506 C CA  . ASN   A 115 ? 0.1129 0.1127 0.1487 -0.0089 0.0003  0.0032  115 ASN   A CA  
2507 C C   . ASN   A 115 ? 0.1115 0.1029 0.1453 -0.0126 -0.0035 0.0046  115 ASN   A C   
2508 O O   . ASN   A 115 ? 0.1160 0.1222 0.1484 -0.0142 -0.0022 0.0066  115 ASN   A O   
2509 C CB  . ASN   A 115 ? 0.1208 0.1192 0.1402 -0.0159 0.0019  0.0046  115 ASN   A CB  
2510 C CG  . ASN   A 115 ? 0.1145 0.1404 0.1646 -0.0157 0.0074  0.0044  115 ASN   A CG  
2511 O OD1 . ASN   A 115 ? 0.1222 0.2359 0.1877 -0.0172 0.0147  0.0183  115 ASN   A OD1 
2512 N ND2 . ASN   A 115 ? 0.1196 0.1245 0.1619 -0.0166 0.0151  0.0081  115 ASN   A ND2 
2519 N N   . PHE   A 116 ? 0.1101 0.1070 0.1551 -0.0035 0.0033  0.0111  116 PHE   A N   
2520 C CA  . PHE   A 116 ? 0.1135 0.1193 0.1359 -0.0049 0.0052  0.0135  116 PHE   A CA  
2521 C C   . PHE   A 116 ? 0.1127 0.1225 0.1336 -0.0107 0.0008  0.0124  116 PHE   A C   
2522 O O   . PHE   A 116 ? 0.1234 0.1298 0.1398 -0.0034 -0.0015 0.0163  116 PHE   A O   
2523 C CB  . PHE   A 116 ? 0.1099 0.1098 0.1555 -0.0039 0.0080  0.0088  116 PHE   A CB  
2524 C CG  . PHE   A 116 ? 0.1150 0.1062 0.1424 -0.0056 0.0104  0.0036  116 PHE   A CG  
2525 C CD1 . PHE   A 116 ? 0.1156 0.1100 0.1455 -0.0056 0.0087  0.0084  116 PHE   A CD1 
2526 C CD2 . PHE   A 116 ? 0.1204 0.1191 0.1575 -0.0033 0.0098  0.0147  116 PHE   A CD2 
2527 C CE1 . PHE   A 116 ? 0.1202 0.1074 0.1603 -0.0138 0.0094  0.0113  116 PHE   A CE1 
2528 C CE2 . PHE   A 116 ? 0.1157 0.1144 0.1678 -0.0047 0.0105  0.0064  116 PHE   A CE2 
2529 C CZ  . PHE   A 116 ? 0.1196 0.1026 0.1610 -0.0022 0.0089  0.0091  116 PHE   A CZ  
2539 N N   . ASN   A 117 ? 0.1159 0.1148 0.1445 -0.0064 0.0025  0.0130  117 ASN   A N   
2540 C CA  . ASN   A 117 ? 0.1220 0.1147 0.1486 -0.0006 0.0016  0.0183  117 ASN   A CA  
2541 C C   . ASN   A 117 ? 0.1229 0.1244 0.1626 -0.0010 0.0002  0.0147  117 ASN   A C   
2542 O O   . ASN   A 117 ? 0.1304 0.1298 0.1866 -0.0084 -0.0145 0.0308  117 ASN   A O   
2543 C CB  . ASN   A 117 ? 0.1178 0.1207 0.1591 -0.0023 -0.0028 0.0222  117 ASN   A CB  
2544 C CG  . ASN   A 117 ? 0.1143 0.1198 0.1572 -0.0041 0.0020  0.0183  117 ASN   A CG  
2545 O OD1 . ASN   A 117 ? 0.1199 0.1365 0.1700 -0.0156 0.0070  0.0089  117 ASN   A OD1 
2546 N ND2 . ASN   A 117 ? 0.1122 0.1183 0.1563 0.0001  0.0033  0.0195  117 ASN   A ND2 
2553 N N   . GLN   A 118 ? 0.1127 0.1186 0.1719 -0.0033 -0.0116 0.0161  118 GLN   A N   
2554 C CA  . GLN   A 118 ? 0.1247 0.1329 0.1700 -0.0085 -0.0151 0.0133  118 GLN   A CA  
2555 C C   . GLN   A 118 ? 0.1235 0.1430 0.1654 -0.0064 -0.0141 0.0126  118 GLN   A C   
2556 O O   . GLN   A 118 ? 0.1292 0.1761 0.1964 -0.0019 -0.0262 -0.0054 118 GLN   A O   
2557 C CB  . GLN   A 118 ? 0.1201 0.1368 0.1752 -0.0081 -0.0066 0.0154  118 GLN   A CB  
2558 C CG  . GLN   A 118 ? 0.1175 0.1341 0.1820 -0.0044 0.0017  0.0128  118 GLN   A CG  
2559 C CD  . GLN   A 118 ? 0.1152 0.1393 0.1908 0.0005  0.0036  0.0079  118 GLN   A CD  
2560 O OE1 . GLN   A 118 ? 0.1167 0.1500 0.2084 0.0083  -0.0130 0.0032  118 GLN   A OE1 
2561 N NE2 . GLN   A 118 ? 0.1265 0.1297 0.1876 0.0026  -0.0091 0.0126  118 GLN   A NE2 
2570 N N   . HIS   A 119 ? 0.1301 0.1376 0.1483 -0.0067 -0.0103 0.0156  119 HIS   A N   
2571 C CA  . HIS   A 119 ? 0.1390 0.1457 0.1581 -0.0105 -0.0049 0.0236  119 HIS   A CA  
2572 C C   . HIS   A 119 ? 0.1502 0.1550 0.1577 -0.0121 -0.0062 0.0268  119 HIS   A C   
2573 O O   . HIS   A 119 ? 0.1483 0.1622 0.1618 -0.0306 -0.0089 0.0213  119 HIS   A O   
2574 C CB  . HIS   A 119 ? 0.1405 0.1412 0.1801 -0.0070 0.0165  0.0214  119 HIS   A CB  
2575 C CG  . HIS   A 119 ? 0.1442 0.1420 0.2170 -0.0016 0.0161  0.0292  119 HIS   A CG  
2576 N ND1 . HIS   A 119 ? 0.1589 0.1642 0.2727 -0.0169 0.0113  0.0145  119 HIS   A ND1 
2577 C CD2 . HIS   A 119 ? 0.1590 0.1539 0.2372 0.0123  0.0347  0.0521  119 HIS   A CD2 
2578 C CE1 . HIS   A 119 ? 0.1527 0.1695 0.2920 -0.0153 0.0271  0.0432  119 HIS   A CE1 
2579 N NE2 . HIS   A 119 ? 0.1713 0.1617 0.2774 0.0013  0.0485  0.0597  119 HIS   A NE2 
2587 N N   A GLU   A 120 ? 0.1694 0.1785 0.1679 -0.0142 -0.0028 0.0261  120 GLU   A N   
2588 N N   B GLU   A 120 ? 0.1576 0.1653 0.1509 -0.0106 -0.0099 0.0428  120 GLU   A N   
2589 C CA  A GLU   A 120 ? 0.1929 0.2016 0.1916 -0.0100 0.0002  0.0366  120 GLU   A CA  
2590 C CA  B GLU   A 120 ? 0.1768 0.1804 0.1612 0.0019  -0.0139 0.0707  120 GLU   A CA  
2591 C C   A GLU   A 120 ? 0.1756 0.1834 0.1577 -0.0181 -0.0039 0.0347  120 GLU   A C   
2592 C C   B GLU   A 120 ? 0.1628 0.1633 0.1407 -0.0174 -0.0151 0.0570  120 GLU   A C   
2593 O O   A GLU   A 120 ? 0.1774 0.1828 0.1639 -0.0155 -0.0031 0.0278  120 GLU   A O   
2594 O O   B GLU   A 120 ? 0.1622 0.1509 0.1523 -0.0206 -0.0163 0.0600  120 GLU   A O   
2595 C CB  A GLU   A 120 ? 0.2374 0.2490 0.2653 -0.0008 0.0086  0.0522  120 GLU   A CB  
2596 C CB  B GLU   A 120 ? 0.2213 0.2298 0.2216 0.0217  -0.0070 0.1075  120 GLU   A CB  
2597 C CG  A GLU   A 120 ? 0.2898 0.2964 0.3561 0.0069  0.0130  0.0525  120 GLU   A CG  
2598 C CG  B GLU   A 120 ? 0.2832 0.2848 0.3363 0.0336  0.0007  0.1018  120 GLU   A CG  
2599 C CD  A GLU   A 120 ? 0.3236 0.3278 0.4380 0.0137  0.0190  0.0479  120 GLU   A CD  
2600 C CD  B GLU   A 120 ? 0.3295 0.3229 0.4444 0.0427  0.0138  0.0865  120 GLU   A CD  
2601 O OE1 A GLU   A 120 ? 0.3453 0.3479 0.4659 0.0142  0.0207  0.0453  120 GLU   A OE1 
2602 O OE1 B GLU   A 120 ? 0.3541 0.3499 0.4835 0.0422  0.0163  0.0777  120 GLU   A OE1 
2603 O OE2 A GLU   A 120 ? 0.3399 0.3407 0.4709 0.0159  0.0213  0.0479  120 GLU   A OE2 
2604 O OE2 B GLU   A 120 ? 0.3483 0.3407 0.4860 0.0455  0.0197  0.0844  120 GLU   A OE2 
2617 N N   . VAL   A 121 ? 0.1619 0.1741 0.1379 -0.0227 -0.0047 0.0401  121 VAL   A N   
2618 C CA  . VAL   A 121 ? 0.1681 0.1825 0.1273 -0.0197 0.0106  0.0408  121 VAL   A CA  
2619 C C   . VAL   A 121 ? 0.1590 0.1643 0.1177 -0.0259 0.0104  0.0271  121 VAL   A C   
2620 O O   . VAL   A 121 ? 0.1599 0.1757 0.1453 -0.0374 -0.0077 0.0122  121 VAL   A O   
2621 C CB  . VAL   A 121 ? 0.2021 0.2204 0.1687 -0.0093 0.0216  0.0490  121 VAL   A CB  
2622 C CG1 . VAL   A 121 ? 0.2104 0.2396 0.1771 -0.0004 0.0247  0.0477  121 VAL   A CG1 
2623 C CG2 . VAL   A 121 ? 0.2211 0.2383 0.2146 -0.0151 0.0206  0.0320  121 VAL   A CG2 
2634 N N   . LEU   A 122 ? 0.1478 0.1505 0.1316 -0.0225 0.0083  0.0312  122 LEU   A N   
2635 C CA  . LEU   A 122 ? 0.1513 0.1448 0.1424 -0.0269 0.0273  0.0278  122 LEU   A CA  
2636 C C   . LEU   A 122 ? 0.1459 0.1375 0.1466 -0.0286 0.0147  0.0185  122 LEU   A C   
2637 O O   . LEU   A 122 ? 0.1462 0.1492 0.1772 -0.0301 0.0088  0.0257  122 LEU   A O   
2638 C CB  . LEU   A 122 ? 0.1740 0.1522 0.1855 -0.0145 0.0153  0.0348  122 LEU   A CB  
2639 C CG  . LEU   A 122 ? 0.1775 0.1525 0.1728 -0.0162 0.0259  0.0163  122 LEU   A CG  
2640 C CD1 . LEU   A 122 ? 0.1972 0.1548 0.1866 -0.0244 0.0241  0.0213  122 LEU   A CD1 
2641 C CD2 . LEU   A 122 ? 0.1686 0.1400 0.1644 -0.0178 0.0335  0.0109  122 LEU   A CD2 
2653 N N   A LEU   A 123 ? 0.1385 0.1368 0.1448 -0.0253 0.0072  0.0155  123 LEU   A N   
2654 N N   B LEU   A 123 ? 0.1370 0.1348 0.1315 -0.0275 0.0102  0.0201  123 LEU   A N   
2655 C CA  A LEU   A 123 ? 0.1345 0.1396 0.1409 -0.0210 0.0111  0.0148  123 LEU   A CA  
2656 C CA  B LEU   A 123 ? 0.1360 0.1359 0.1265 -0.0249 0.0215  0.0230  123 LEU   A CA  
2657 C C   A LEU   A 123 ? 0.1269 0.1353 0.1339 -0.0156 0.0067  0.0163  123 LEU   A C   
2658 C C   B LEU   A 123 ? 0.1274 0.1270 0.1276 -0.0170 0.0147  0.0209  123 LEU   A C   
2659 O O   A LEU   A 123 ? 0.1199 0.1381 0.1425 -0.0099 -0.0013 0.0127  123 LEU   A O   
2660 O O   B LEU   A 123 ? 0.1219 0.1242 0.1337 -0.0219 0.0161  0.0189  123 LEU   A O   
2661 C CB  A LEU   A 123 ? 0.1403 0.1485 0.1497 -0.0207 0.0197  0.0074  123 LEU   A CB  
2662 C CB  B LEU   A 123 ? 0.1471 0.1479 0.1367 -0.0271 0.0362  0.0204  123 LEU   A CB  
2663 C CG  A LEU   A 123 ? 0.1441 0.1542 0.1568 -0.0207 0.0222  0.0002  123 LEU   A CG  
2664 C CG  B LEU   A 123 ? 0.1580 0.1607 0.1576 -0.0206 0.0398  0.0115  123 LEU   A CG  
2665 C CD1 A LEU   A 123 ? 0.1502 0.1551 0.1731 -0.0141 0.0145  -0.0052 123 LEU   A CD1 
2666 C CD1 B LEU   A 123 ? 0.1672 0.1677 0.1760 -0.0125 0.0323  0.0054  123 LEU   A CD1 
2667 C CD2 A LEU   A 123 ? 0.1518 0.1620 0.1626 -0.0226 0.0189  -0.0122 123 LEU   A CD2 
2668 C CD2 B LEU   A 123 ? 0.1696 0.1699 0.1647 -0.0186 0.0303  0.0040  123 LEU   A CD2 
2691 N N   . ALA   A 124 ? 0.1296 0.1294 0.1218 -0.0190 0.0093  0.0170  124 ALA   A N   
2692 C CA  . ALA   A 124 ? 0.1181 0.1283 0.1418 -0.0164 0.0037  0.0187  124 ALA   A CA  
2693 C C   . ALA   A 124 ? 0.1127 0.1255 0.1453 -0.0154 0.0102  0.0177  124 ALA   A C   
2694 O O   . ALA   A 124 ? 0.1149 0.1356 0.1626 -0.0131 0.0119  0.0294  124 ALA   A O   
2695 C CB  . ALA   A 124 ? 0.1219 0.1286 0.1485 -0.0145 0.0066  0.0196  124 ALA   A CB  
2702 N N   A PRO   A 125 ? 0.1144 0.1200 0.1433 -0.0089 0.0129  0.0278  125 PRO   A N   
2703 N N   B PRO   A 125 ? 0.1180 0.1279 0.1437 -0.0129 0.0081  0.0283  125 PRO   A N   
2704 C CA  A PRO   A 125 ? 0.1169 0.1152 0.1537 -0.0038 0.0151  0.0236  125 PRO   A CA  
2705 C CA  B PRO   A 125 ? 0.1260 0.1333 0.1506 -0.0124 0.0094  0.0220  125 PRO   A CA  
2706 C C   A PRO   A 125 ? 0.1066 0.1078 0.1529 -0.0031 0.0147  0.0217  125 PRO   A C   
2707 C C   B PRO   A 125 ? 0.1225 0.1415 0.1468 -0.0106 0.0045  0.0200  125 PRO   A C   
2708 O O   A PRO   A 125 ? 0.1060 0.1076 0.1611 0.0015  0.0115  0.0231  125 PRO   A O   
2709 O O   B PRO   A 125 ? 0.1236 0.1447 0.1549 -0.0031 -0.0010 0.0191  125 PRO   A O   
2710 C CB  A PRO   A 125 ? 0.1302 0.1144 0.1505 -0.0079 0.0121  0.0204  125 PRO   A CB  
2711 C CB  B PRO   A 125 ? 0.1381 0.1278 0.1485 -0.0147 0.0097  0.0228  125 PRO   A CB  
2712 C CG  A PRO   A 125 ? 0.1297 0.1180 0.1536 -0.0114 0.0157  0.0260  125 PRO   A CG  
2713 C CG  B PRO   A 125 ? 0.1366 0.1289 0.1577 -0.0172 0.0101  0.0247  125 PRO   A CG  
2714 C CD  A PRO   A 125 ? 0.1183 0.1240 0.1415 -0.0104 0.0203  0.0279  125 PRO   A CD  
2715 C CD  B PRO   A 125 ? 0.1226 0.1293 0.1469 -0.0147 0.0145  0.0221  125 PRO   A CD  
2730 N N   A LEU   A 126 ? 0.0999 0.1027 0.1532 0.0026  0.0173  0.0216  126 LEU   A N   
2731 N N   B LEU   A 126 ? 0.1265 0.1457 0.1517 -0.0040 0.0026  0.0193  126 LEU   A N   
2732 C CA  A LEU   A 126 ? 0.1102 0.1086 0.1597 0.0025  0.0143  0.0248  126 LEU   A CA  
2733 C CA  B LEU   A 126 ? 0.1248 0.1380 0.1556 -0.0042 0.0004  0.0305  126 LEU   A CA  
2734 C C   A LEU   A 126 ? 0.1204 0.1187 0.1634 0.0118  0.0032  0.0262  126 LEU   A C   
2735 C C   B LEU   A 126 ? 0.1296 0.1292 0.1540 0.0012  -0.0030 0.0231  126 LEU   A C   
2736 O O   A LEU   A 126 ? 0.1241 0.1316 0.1860 0.0236  0.0085  0.0355  126 LEU   A O   
2737 O O   B LEU   A 126 ? 0.1353 0.1331 0.1669 0.0061  -0.0059 0.0336  126 LEU   A O   
2738 C CB  A LEU   A 126 ? 0.1191 0.1060 0.1730 0.0042  0.0068  0.0178  126 LEU   A CB  
2739 C CB  B LEU   A 126 ? 0.1362 0.1517 0.1737 -0.0078 0.0041  0.0280  126 LEU   A CB  
2740 C CG  A LEU   A 126 ? 0.1169 0.1145 0.1895 0.0083  0.0196  0.0140  126 LEU   A CG  
2741 C CG  B LEU   A 126 ? 0.1298 0.1590 0.1943 -0.0051 0.0096  0.0223  126 LEU   A CG  
2742 C CD1 A LEU   A 126 ? 0.1197 0.1279 0.2138 0.0073  0.0199  0.0194  126 LEU   A CD1 
2743 C CD1 B LEU   A 126 ? 0.1335 0.1569 0.2183 -0.0064 0.0010  0.0000  126 LEU   A CD1 
2744 C CD2 A LEU   A 126 ? 0.1227 0.1075 0.1740 -0.0001 0.0212  0.0102  126 LEU   A CD2 
2745 C CD2 B LEU   A 126 ? 0.1292 0.1654 0.1932 -0.0026 0.0102  0.0250  126 LEU   A CD2 
2768 N N   A LEU   A 127 ? 0.1198 0.1163 0.1552 0.0065  -0.0045 0.0123  127 LEU   A N   
2769 N N   B LEU   A 127 ? 0.1185 0.1254 0.1382 -0.0035 0.0045  0.0260  127 LEU   A N   
2770 C CA  A LEU   A 127 ? 0.1202 0.1122 0.1423 -0.0013 -0.0036 0.0092  127 LEU   A CA  
2771 C CA  B LEU   A 127 ? 0.1155 0.1352 0.1281 -0.0023 -0.0051 0.0271  127 LEU   A CA  
2772 C C   A LEU   A 127 ? 0.1213 0.1105 0.1261 -0.0045 0.0013  0.0067  127 LEU   A C   
2773 C C   B LEU   A 127 ? 0.1132 0.1240 0.1255 0.0024  -0.0050 0.0139  127 LEU   A C   
2774 O O   A LEU   A 127 ? 0.1294 0.1074 0.1263 -0.0099 -0.0005 0.0155  127 LEU   A O   
2775 O O   B LEU   A 127 ? 0.1255 0.1257 0.1400 -0.0027 -0.0022 0.0229  127 LEU   A O   
2776 C CB  A LEU   A 127 ? 0.1172 0.1048 0.1361 0.0013  0.0010  0.0157  127 LEU   A CB  
2777 C CB  B LEU   A 127 ? 0.1272 0.1613 0.1375 -0.0005 -0.0003 0.0227  127 LEU   A CB  
2778 C CG  A LEU   A 127 ? 0.1124 0.0890 0.1234 0.0040  -0.0071 0.0137  127 LEU   A CG  
2779 C CG  B LEU   A 127 ? 0.1357 0.1937 0.1488 0.0012  -0.0093 0.0339  127 LEU   A CG  
2780 C CD1 A LEU   A 127 ? 0.1092 0.0832 0.1259 -0.0033 -0.0136 0.0092  127 LEU   A CD1 
2781 C CD1 B LEU   A 127 ? 0.1376 0.2049 0.1775 0.0082  -0.0036 0.0385  127 LEU   A CD1 
2782 C CD2 A LEU   A 127 ? 0.1270 0.0774 0.1304 0.0102  -0.0138 0.0168  127 LEU   A CD2 
2783 C CD2 B LEU   A 127 ? 0.1528 0.2129 0.1554 -0.0042 -0.0236 0.0178  127 LEU   A CD2 
2806 N N   A SER   A 128 ? 0.1249 0.1172 0.1262 -0.0086 -0.0002 0.0079  128 SER   A N   
2807 N N   B SER   A 128 ? 0.1184 0.1242 0.1276 -0.0051 -0.0150 0.0175  128 SER   A N   
2808 C CA  A SER   A 128 ? 0.1306 0.1196 0.1241 -0.0065 0.0004  0.0033  128 SER   A CA  
2809 C CA  B SER   A 128 ? 0.1183 0.1142 0.1176 -0.0018 -0.0130 0.0127  128 SER   A CA  
2810 C C   A SER   A 128 ? 0.1378 0.1281 0.1317 -0.0062 0.0059  0.0011  128 SER   A C   
2811 C C   B SER   A 128 ? 0.1248 0.1157 0.1189 0.0066  -0.0103 0.0273  128 SER   A C   
2812 O O   A SER   A 128 ? 0.1440 0.1429 0.1382 -0.0099 0.0156  0.0036  128 SER   A O   
2813 O O   B SER   A 128 ? 0.1311 0.1279 0.1281 0.0001  -0.0119 0.0253  128 SER   A O   
2814 C CB  A SER   A 128 ? 0.1262 0.1201 0.1351 -0.0074 0.0084  0.0057  128 SER   A CB  
2815 C CB  B SER   A 128 ? 0.1215 0.1234 0.1292 -0.0026 -0.0093 0.0139  128 SER   A CB  
2816 O OG  A SER   A 128 ? 0.1323 0.1244 0.1492 -0.0044 0.0073  -0.0016 128 SER   A OG  
2817 O OG  B SER   A 128 ? 0.1255 0.1325 0.1361 -0.0012 0.0021  0.0222  128 SER   A OG  
2828 N N   A ALA   A 129 ? 0.1358 0.1361 0.1278 -0.0093 -0.0003 -0.0021 129 ALA   A N   
2829 N N   B ALA   A 129 ? 0.1275 0.1316 0.1383 0.0099  -0.0169 0.0317  129 ALA   A N   
2830 C CA  A ALA   A 129 ? 0.1266 0.1388 0.1051 -0.0077 -0.0064 0.0069  129 ALA   A CA  
2831 C CA  B ALA   A 129 ? 0.1306 0.1422 0.1508 0.0114  -0.0122 0.0312  129 ALA   A CA  
2832 C C   A ALA   A 129 ? 0.1247 0.1402 0.0904 -0.0121 0.0037  0.0026  129 ALA   A C   
2833 C C   B ALA   A 129 ? 0.1385 0.1444 0.1411 0.0170  -0.0114 0.0100  129 ALA   A C   
2834 O O   A ALA   A 129 ? 0.1309 0.1374 0.0839 -0.0204 0.0133  -0.0031 129 ALA   A O   
2835 O O   B ALA   A 129 ? 0.1422 0.1509 0.1507 0.0204  -0.0064 0.0135  129 ALA   A O   
2836 C CB  A ALA   A 129 ? 0.1262 0.1526 0.0975 0.0076  -0.0199 0.0174  129 ALA   A CB  
2837 C CB  B ALA   A 129 ? 0.1360 0.1700 0.1737 0.0111  -0.0083 0.0437  129 ALA   A CB  
2848 N N   A GLY   A 130 ? 0.1234 0.1464 0.1218 -0.0083 0.0291  -0.0119 130 GLY   A N   
2849 N N   B GLY   A 130 ? 0.1415 0.1487 0.1482 0.0214  -0.0072 -0.0110 130 GLY   A N   
2850 C CA  A GLY   A 130 ? 0.1376 0.1443 0.1371 -0.0025 0.0329  -0.0171 130 GLY   A CA  
2851 C CA  B GLY   A 130 ? 0.1600 0.1512 0.1728 0.0218  0.0048  -0.0225 130 GLY   A CA  
2852 C C   A GLY   A 130 ? 0.1342 0.1314 0.1260 0.0044  0.0270  -0.0109 130 GLY   A C   
2853 C C   B GLY   A 130 ? 0.1665 0.1370 0.1663 0.0256  -0.0160 -0.0082 130 GLY   A C   
2854 O O   A GLY   A 130 ? 0.1274 0.1270 0.1167 -0.0029 0.0279  -0.0103 130 GLY   A O   
2855 O O   B GLY   A 130 ? 0.1733 0.1339 0.1722 0.0222  -0.0305 -0.0040 130 GLY   A O   
2862 N N   A ILE   A 131 ? 0.1415 0.1313 0.1213 0.0026  0.0157  -0.0066 131 ILE   A N   
2863 N N   B ILE   A 131 ? 0.1769 0.1344 0.1608 0.0176  -0.0194 0.0047  131 ILE   A N   
2864 C CA  A ILE   A 131 ? 0.1425 0.1294 0.1194 0.0013  0.0051  -0.0052 131 ILE   A CA  
2865 C CA  B ILE   A 131 ? 0.1833 0.1305 0.1565 0.0032  -0.0324 0.0079  131 ILE   A CA  
2866 C C   A ILE   A 131 ? 0.1355 0.1319 0.1058 0.0033  0.0001  0.0006  131 ILE   A C   
2867 C C   B ILE   A 131 ? 0.1778 0.1370 0.1472 -0.0102 -0.0253 0.0218  131 ILE   A C   
2868 O O   A ILE   A 131 ? 0.1364 0.1309 0.1171 0.0153  -0.0008 0.0032  131 ILE   A O   
2869 O O   B ILE   A 131 ? 0.1951 0.1507 0.1873 -0.0067 -0.0156 0.0287  131 ILE   A O   
2870 C CB  A ILE   A 131 ? 0.1441 0.1375 0.1314 0.0024  -0.0031 -0.0104 131 ILE   A CB  
2871 C CB  B ILE   A 131 ? 0.2005 0.1420 0.1689 0.0048  -0.0373 -0.0046 131 ILE   A CB  
2872 C CG1 A ILE   A 131 ? 0.1553 0.1533 0.1374 0.0042  -0.0062 -0.0063 131 ILE   A CG1 
2873 C CG1 B ILE   A 131 ? 0.2110 0.1649 0.1746 0.0079  -0.0481 -0.0022 131 ILE   A CG1 
2874 C CG2 A ILE   A 131 ? 0.1488 0.1369 0.1527 0.0029  -0.0040 -0.0130 131 ILE   A CG2 
2875 C CG2 B ILE   A 131 ? 0.2089 0.1393 0.1821 0.0058  -0.0235 -0.0204 131 ILE   A CG2 
2876 C CD1 A ILE   A 131 ? 0.1602 0.1623 0.1577 0.0019  -0.0212 -0.0070 131 ILE   A CD1 
2877 C CD1 B ILE   A 131 ? 0.2197 0.1781 0.1967 0.0070  -0.0507 -0.0074 131 ILE   A CD1 
2900 N N   A PHE   A 132 ? 0.1378 0.1349 0.1055 0.0072  0.0088  0.0025  132 PHE   A N   
2901 N N   B PHE   A 132 ? 0.1631 0.1297 0.1257 0.0003  -0.0157 0.0141  132 PHE   A N   
2902 C CA  A PHE   A 132 ? 0.1399 0.1438 0.1061 0.0101  0.0140  -0.0026 132 PHE   A CA  
2903 C CA  B PHE   A 132 ? 0.1590 0.1364 0.1262 0.0012  -0.0082 0.0066  132 PHE   A CA  
2904 C C   A PHE   A 132 ? 0.1388 0.1552 0.0982 0.0209  0.0173  -0.0045 132 PHE   A C   
2905 C C   B PHE   A 132 ? 0.1747 0.1463 0.1380 0.0051  -0.0064 0.0100  132 PHE   A C   
2906 O O   A PHE   A 132 ? 0.1368 0.1648 0.1030 0.0262  0.0097  -0.0116 132 PHE   A O   
2907 O O   B PHE   A 132 ? 0.1915 0.1585 0.1730 0.0124  -0.0135 0.0118  132 PHE   A O   
2908 C CB  A PHE   A 132 ? 0.1491 0.1410 0.1169 0.0066  0.0078  -0.0096 132 PHE   A CB  
2909 C CB  B PHE   A 132 ? 0.1441 0.1314 0.1171 0.0042  -0.0127 0.0142  132 PHE   A CB  
2910 C CG  A PHE   A 132 ? 0.1593 0.1376 0.1216 0.0043  0.0052  -0.0033 132 PHE   A CG  
2911 C CG  B PHE   A 132 ? 0.1503 0.1322 0.1223 0.0075  -0.0217 0.0102  132 PHE   A CG  
2912 C CD1 A PHE   A 132 ? 0.1673 0.1417 0.1398 0.0051  -0.0033 -0.0096 132 PHE   A CD1 
2913 C CD1 B PHE   A 132 ? 0.1606 0.1457 0.1504 0.0163  -0.0175 -0.0005 132 PHE   A CD1 
2914 C CD2 A PHE   A 132 ? 0.1611 0.1460 0.1342 0.0016  0.0150  -0.0036 132 PHE   A CD2 
2915 C CD2 B PHE   A 132 ? 0.1509 0.1483 0.1400 0.0028  -0.0188 -0.0024 132 PHE   A CD2 
2916 C CE1 A PHE   A 132 ? 0.1721 0.1497 0.1546 0.0043  -0.0094 -0.0104 132 PHE   A CE1 
2917 C CE1 B PHE   A 132 ? 0.1638 0.1548 0.1579 0.0164  -0.0299 -0.0093 132 PHE   A CE1 
2918 C CE2 A PHE   A 132 ? 0.1644 0.1506 0.1498 0.0029  0.0106  -0.0007 132 PHE   A CE2 
2919 C CE2 B PHE   A 132 ? 0.1511 0.1587 0.1599 0.0053  -0.0190 -0.0045 132 PHE   A CE2 
2920 C CZ  A PHE   A 132 ? 0.1686 0.1517 0.1600 0.0003  0.0005  -0.0022 132 PHE   A CZ  
2921 C CZ  B PHE   A 132 ? 0.1573 0.1573 0.1629 0.0055  -0.0271 -0.0025 132 PHE   A CZ  
2940 N N   A GLY   A 133 ? 0.1428 0.1564 0.0944 0.0240  0.0046  -0.0040 133 GLY   A N   
2941 N N   B GLY   A 133 ? 0.1793 0.1460 0.1281 0.0020  -0.0279 0.0107  133 GLY   A N   
2942 C CA  A GLY   A 133 ? 0.1523 0.1647 0.1108 0.0192  -0.0090 -0.0070 133 GLY   A CA  
2943 C CA  B GLY   A 133 ? 0.1815 0.1560 0.1343 -0.0025 -0.0336 0.0038  133 GLY   A CA  
2944 C C   A GLY   A 133 ? 0.1602 0.1750 0.1290 0.0077  -0.0273 -0.0069 133 GLY   A C   
2945 C C   B GLY   A 133 ? 0.1727 0.1659 0.1369 -0.0055 -0.0480 -0.0064 133 GLY   A C   
2946 O O   A GLY   A 133 ? 0.1687 0.1863 0.1462 0.0048  -0.0337 -0.0182 133 GLY   A O   
2947 O O   B GLY   A 133 ? 0.1671 0.1856 0.1627 0.0000  -0.0436 -0.0190 133 GLY   A O   
2954 N N   A ALA   A 134 ? 0.1581 0.1682 0.1406 0.0044  -0.0197 -0.0015 134 ALA   A N   
2955 N N   B ALA   A 134 ? 0.1709 0.1453 0.1398 -0.0064 -0.0407 -0.0054 134 ALA   A N   
2956 C CA  A ALA   A 134 ? 0.1562 0.1684 0.1603 0.0066  -0.0212 -0.0075 134 ALA   A CA  
2957 C CA  B ALA   A 134 ? 0.1720 0.1374 0.1698 -0.0093 -0.0378 -0.0169 134 ALA   A CA  
2958 C C   A ALA   A 134 ? 0.1546 0.1708 0.1614 0.0043  -0.0176 0.0036  134 ALA   A C   
2959 C C   B ALA   A 134 ? 0.1708 0.1407 0.1733 -0.0043 -0.0304 -0.0063 134 ALA   A C   
2960 O O   A ALA   A 134 ? 0.1619 0.1725 0.1779 0.0035  -0.0003 0.0075  134 ALA   A O   
2961 O O   B ALA   A 134 ? 0.1738 0.1438 0.1936 -0.0058 -0.0019 -0.0028 134 ALA   A O   
2962 C CB  A ALA   A 134 ? 0.1606 0.1674 0.1751 0.0107  -0.0201 -0.0120 134 ALA   A CB  
2963 C CB  B ALA   A 134 ? 0.1798 0.1338 0.2015 -0.0112 -0.0273 -0.0210 134 ALA   A CB  
2974 N N   A ASP   A 135 ? 0.1555 0.1712 0.1663 -0.0002 -0.0209 0.0109  135 ASP   A N   
2975 N N   B ASP   A 135 ? 0.1822 0.1519 0.1884 -0.0104 -0.0380 0.0086  135 ASP   A N   
2976 C CA  A ASP   A 135 ? 0.1519 0.1724 0.1746 -0.0050 -0.0265 0.0189  135 ASP   A CA  
2977 C CA  B ASP   A 135 ? 0.1757 0.1594 0.1988 -0.0134 -0.0429 0.0187  135 ASP   A CA  
2978 C C   A ASP   A 135 ? 0.1467 0.1666 0.1777 -0.0026 -0.0166 0.0348  135 ASP   A C   
2979 C C   B ASP   A 135 ? 0.1592 0.1456 0.1962 -0.0058 -0.0262 0.0246  135 ASP   A C   
2980 O O   A ASP   A 135 ? 0.1443 0.1609 0.1904 0.0017  -0.0189 0.0328  135 ASP   A O   
2981 O O   B ASP   A 135 ? 0.1546 0.1374 0.2039 -0.0011 -0.0242 0.0284  135 ASP   A O   
2982 C CB  A ASP   A 135 ? 0.1554 0.1841 0.1919 -0.0154 -0.0447 0.0086  135 ASP   A CB  
2983 C CB  B ASP   A 135 ? 0.1903 0.1838 0.2179 -0.0175 -0.0615 0.0095  135 ASP   A CB  
2984 C CG  A ASP   A 135 ? 0.1654 0.1952 0.2196 -0.0271 -0.0496 0.0034  135 ASP   A CG  
2985 C CG  B ASP   A 135 ? 0.2096 0.2143 0.2586 -0.0197 -0.0547 -0.0042 135 ASP   A CG  
2986 O OD1 A ASP   A 135 ? 0.1562 0.1905 0.2154 -0.0390 -0.0626 0.0116  135 ASP   A OD1 
2987 O OD1 B ASP   A 135 ? 0.2117 0.2197 0.2736 -0.0154 -0.0488 -0.0011 135 ASP   A OD1 
2988 O OD2 A ASP   A 135 ? 0.1886 0.2090 0.2563 -0.0263 -0.0334 0.0026  135 ASP   A OD2 
2989 O OD2 B ASP   A 135 ? 0.2271 0.2381 0.2890 -0.0177 -0.0492 -0.0114 135 ASP   A OD2 
2998 N N   A PRO   A 136 ? 0.1461 0.1712 0.1821 0.0020  -0.0081 0.0431  136 PRO   A N   
2999 N N   B PRO   A 136 ? 0.1561 0.1489 0.1998 0.0069  -0.0128 0.0284  136 PRO   A N   
3000 C CA  A PRO   A 136 ? 0.1409 0.1723 0.1898 0.0003  0.0024  0.0440  136 PRO   A CA  
3001 C CA  B PRO   A 136 ? 0.1486 0.1591 0.2091 0.0034  -0.0043 0.0257  136 PRO   A CA  
3002 C C   A PRO   A 136 ? 0.1206 0.1660 0.1989 -0.0023 0.0036  0.0394  136 PRO   A C   
3003 C C   B PRO   A 136 ? 0.1261 0.1614 0.2064 0.0003  -0.0115 0.0261  136 PRO   A C   
3004 O O   A PRO   A 136 ? 0.1149 0.1644 0.2069 0.0016  0.0045  0.0385  136 PRO   A O   
3005 O O   B PRO   A 136 ? 0.1203 0.1553 0.1957 -0.0002 -0.0119 0.0194  136 PRO   A O   
3006 C CB  A PRO   A 136 ? 0.1568 0.1785 0.2025 0.0050  0.0064  0.0404  136 PRO   A CB  
3007 C CB  B PRO   A 136 ? 0.1660 0.1639 0.2309 0.0100  0.0021  0.0197  136 PRO   A CB  
3008 C CG  A PRO   A 136 ? 0.1673 0.1841 0.2143 0.0094  0.0018  0.0324  136 PRO   A CG  
3009 C CG  B PRO   A 136 ? 0.1786 0.1688 0.2467 0.0143  0.0027  0.0156  136 PRO   A CG  
3010 C CD  A PRO   A 136 ? 0.1578 0.1761 0.1941 0.0079  -0.0026 0.0444  136 PRO   A CD  
3011 C CD  B PRO   A 136 ? 0.1664 0.1543 0.2210 0.0141  -0.0009 0.0345  136 PRO   A CD  
3026 N N   A ILE   A 137 ? 0.1173 0.1680 0.2049 -0.0053 -0.0074 0.0378  137 ILE   A N   
3027 N N   B ILE   A 137 ? 0.1265 0.1626 0.2240 0.0012  -0.0253 0.0327  137 ILE   A N   
3028 C CA  A ILE   A 137 ? 0.1200 0.1772 0.2105 -0.0139 -0.0168 0.0403  137 ILE   A CA  
3029 C CA  B ILE   A 137 ? 0.1281 0.1751 0.2289 -0.0079 -0.0313 0.0349  137 ILE   A CA  
3030 C C   A ILE   A 137 ? 0.1207 0.1741 0.1965 -0.0138 -0.0262 0.0356  137 ILE   A C   
3031 C C   B ILE   A 137 ? 0.1316 0.1686 0.2061 -0.0181 -0.0332 0.0357  137 ILE   A C   
3032 O O   A ILE   A 137 ? 0.1267 0.1727 0.2018 -0.0152 -0.0208 0.0286  137 ILE   A O   
3033 O O   B ILE   A 137 ? 0.1313 0.1641 0.2044 -0.0169 -0.0240 0.0313  137 ILE   A O   
3034 C CB  A ILE   A 137 ? 0.1262 0.1939 0.2285 -0.0226 -0.0300 0.0380  137 ILE   A CB  
3035 C CB  B ILE   A 137 ? 0.1302 0.1984 0.2554 -0.0135 -0.0398 0.0314  137 ILE   A CB  
3036 C CG1 A ILE   A 137 ? 0.1416 0.2128 0.2434 -0.0114 -0.0326 0.0323  137 ILE   A CG1 
3037 C CG1 B ILE   A 137 ? 0.1437 0.2208 0.2708 -0.0079 -0.0314 0.0349  137 ILE   A CG1 
3038 C CG2 A ILE   A 137 ? 0.1318 0.1940 0.2394 -0.0341 -0.0352 0.0393  137 ILE   A CG2 
3039 C CG2 B ILE   A 137 ? 0.1321 0.1994 0.2740 -0.0176 -0.0509 0.0273  137 ILE   A CG2 
3040 C CD1 A ILE   A 137 ? 0.1540 0.2266 0.2620 -0.0019 -0.0304 0.0270  137 ILE   A CD1 
3041 C CD1 B ILE   A 137 ? 0.1598 0.2389 0.2861 -0.0047 -0.0272 0.0337  137 ILE   A CD1 
3064 N N   A HIS   A 138 ? 0.1164 0.1795 0.1914 -0.0070 -0.0270 0.0345  138 HIS   A N   
3065 N N   B HIS   A 138 ? 0.1346 0.1835 0.2106 -0.0160 -0.0198 0.0340  138 HIS   A N   
3066 C CA  A HIS   A 138 ? 0.1186 0.1827 0.1824 -0.0110 -0.0282 0.0356  138 HIS   A CA  
3067 C CA  B HIS   A 138 ? 0.1391 0.1845 0.2024 -0.0198 -0.0164 0.0362  138 HIS   A CA  
3068 C C   A HIS   A 138 ? 0.1163 0.1747 0.1767 -0.0110 -0.0213 0.0411  138 HIS   A C   
3069 C C   B HIS   A 138 ? 0.1291 0.1744 0.1884 -0.0159 -0.0093 0.0459  138 HIS   A C   
3070 O O   A HIS   A 138 ? 0.1213 0.1748 0.1706 -0.0120 -0.0206 0.0312  138 HIS   A O   
3071 O O   B HIS   A 138 ? 0.1376 0.1740 0.1926 -0.0183 -0.0029 0.0383  138 HIS   A O   
3072 C CB  A HIS   A 138 ? 0.1376 0.1912 0.1840 -0.0141 -0.0324 0.0269  138 HIS   A CB  
3073 C CB  B HIS   A 138 ? 0.1513 0.1893 0.2038 -0.0158 -0.0207 0.0196  138 HIS   A CB  
3074 C CG  A HIS   A 138 ? 0.1571 0.1961 0.1880 -0.0158 -0.0295 0.0236  138 HIS   A CG  
3075 C CG  B HIS   A 138 ? 0.1673 0.1917 0.2112 -0.0132 -0.0281 0.0008  138 HIS   A CG  
3076 N ND1 A HIS   A 138 ? 0.1685 0.2041 0.2091 -0.0212 -0.0266 0.0184  138 HIS   A ND1 
3077 N ND1 B HIS   A 138 ? 0.1798 0.1980 0.2390 -0.0152 -0.0336 -0.0108 138 HIS   A ND1 
3078 C CD2 A HIS   A 138 ? 0.1611 0.2006 0.1886 -0.0110 -0.0239 0.0213  138 HIS   A CD2 
3079 C CD2 B HIS   A 138 ? 0.1665 0.1872 0.2166 -0.0059 -0.0237 -0.0018 138 HIS   A CD2 
3080 C CE1 A HIS   A 138 ? 0.1739 0.2105 0.2058 -0.0143 -0.0251 0.0155  138 HIS   A CE1 
3081 C CE1 B HIS   A 138 ? 0.1804 0.1966 0.2329 -0.0059 -0.0342 -0.0129 138 HIS   A CE1 
3082 N NE2 A HIS   A 138 ? 0.1659 0.2081 0.1899 -0.0085 -0.0201 0.0196  138 HIS   A NE2 
3083 N NE2 B HIS   A 138 ? 0.1715 0.1923 0.2187 -0.0023 -0.0230 -0.0110 138 HIS   A NE2 
3098 N N   . SER   A 139 ? 0.1183 0.1685 0.1910 -0.0118 -0.0174 0.0529  139 SER   A N   
3099 C CA  . SER   A 139 ? 0.1149 0.1624 0.1887 -0.0121 -0.0131 0.0541  139 SER   A CA  
3100 C C   . SER   A 139 ? 0.1114 0.1556 0.1810 -0.0142 -0.0063 0.0408  139 SER   A C   
3101 O O   . SER   A 139 ? 0.1094 0.1470 0.1850 -0.0129 -0.0051 0.0436  139 SER   A O   
3102 C CB  . SER   A 139 ? 0.1162 0.1630 0.1956 -0.0170 -0.0165 0.0588  139 SER   A CB  
3103 O OG  . SER   A 139 ? 0.1254 0.1570 0.1934 -0.0255 -0.0187 0.0552  139 SER   A OG  
3110 N N   . LEU   A 140 ? 0.1080 0.1663 0.1882 -0.0097 -0.0080 0.0527  140 LEU   A N   
3111 C CA  . LEU   A 140 ? 0.1069 0.1627 0.1931 -0.0082 -0.0039 0.0557  140 LEU   A CA  
3112 C C   . LEU   A 140 ? 0.1057 0.1606 0.2042 -0.0172 0.0006  0.0509  140 LEU   A C   
3113 O O   . LEU   A 140 ? 0.1128 0.1572 0.2094 -0.0082 -0.0088 0.0478  140 LEU   A O   
3114 C CB  . LEU   A 140 ? 0.1095 0.1721 0.2013 -0.0057 0.0026  0.0606  140 LEU   A CB  
3115 C CG  . LEU   A 140 ? 0.1145 0.1858 0.2072 -0.0146 0.0054  0.0658  140 LEU   A CG  
3116 C CD1 . LEU   A 140 ? 0.1231 0.1890 0.2108 -0.0090 -0.0008 0.0667  140 LEU   A CD1 
3117 C CD2 . LEU   A 140 ? 0.1198 0.1978 0.2208 -0.0127 0.0163  0.0676  140 LEU   A CD2 
3129 N N   . ARG   A 141 ? 0.1115 0.1605 0.2059 -0.0141 -0.0090 0.0442  141 ARG   A N   
3130 C CA  . ARG   A 141 ? 0.1290 0.1717 0.2173 -0.0267 -0.0244 0.0269  141 ARG   A CA  
3131 C C   . ARG   A 141 ? 0.1297 0.1556 0.1948 -0.0201 -0.0202 0.0282  141 ARG   A C   
3132 O O   . ARG   A 141 ? 0.1314 0.1494 0.1936 -0.0199 -0.0069 0.0177  141 ARG   A O   
3133 C CB  . ARG   A 141 ? 0.1415 0.1995 0.2555 -0.0343 -0.0344 0.0071  141 ARG   A CB  
3134 C CG  . ARG   A 141 ? 0.1783 0.2324 0.2937 -0.0324 -0.0377 0.0023  141 ARG   A CG  
3135 C CD  . ARG   A 141 ? 0.2034 0.2562 0.3227 -0.0433 -0.0360 0.0023  141 ARG   A CD  
3136 N NE  . ARG   A 141 ? 0.1944 0.2770 0.3313 -0.0532 -0.0369 0.0046  141 ARG   A NE  
3137 C CZ  . ARG   A 141 ? 0.1936 0.2967 0.3421 -0.0650 -0.0335 0.0115  141 ARG   A CZ  
3138 N NH1 . ARG   A 141 ? 0.1912 0.3065 0.3508 -0.0697 -0.0242 0.0018  141 ARG   A NH1 
3139 N NH2 . ARG   A 141 ? 0.1940 0.3084 0.3495 -0.0593 -0.0445 0.0168  141 ARG   A NH2 
3153 N N   . VAL   A 142 ? 0.1184 0.1544 0.1838 -0.0163 -0.0160 0.0264  142 VAL   A N   
3154 C CA  . VAL   A 142 ? 0.1234 0.1456 0.1781 -0.0147 -0.0015 0.0208  142 VAL   A CA  
3155 C C   . VAL   A 142 ? 0.1112 0.1394 0.1655 -0.0204 -0.0049 0.0230  142 VAL   A C   
3156 O O   . VAL   A 142 ? 0.1186 0.1439 0.1745 -0.0025 -0.0075 0.0178  142 VAL   A O   
3157 C CB  . VAL   A 142 ? 0.1308 0.1564 0.1794 -0.0126 -0.0001 0.0230  142 VAL   A CB  
3158 C CG1 . VAL   A 142 ? 0.1313 0.1484 0.1856 -0.0159 0.0050  0.0090  142 VAL   A CG1 
3159 C CG2 . VAL   A 142 ? 0.1479 0.1758 0.1886 -0.0029 -0.0041 0.0359  142 VAL   A CG2 
3169 N N   . CYS   A 143 ? 0.1095 0.1419 0.1668 -0.0154 -0.0022 0.0228  143 CYS   A N   
3170 C CA  . CYS   A 143 ? 0.1148 0.1349 0.1729 -0.0123 0.0023  0.0195  143 CYS   A CA  
3171 C C   . CYS   A 143 ? 0.1153 0.1327 0.1752 -0.0131 -0.0020 0.0251  143 CYS   A C   
3172 O O   . CYS   A 143 ? 0.1151 0.1339 0.1792 -0.0095 -0.0029 0.0292  143 CYS   A O   
3173 C CB  . CYS   A 143 ? 0.1259 0.1384 0.1820 -0.0125 0.0154  0.0352  143 CYS   A CB  
3174 S SG  . CYS   A 143 ? 0.1412 0.1496 0.1691 0.0010  0.0106  0.0239  143 CYS   A SG  
3180 N N   . VAL   A 144 ? 0.1202 0.1385 0.1866 -0.0133 0.0005  0.0415  144 VAL   A N   
3181 C CA  . VAL   A 144 ? 0.1204 0.1457 0.2243 -0.0172 0.0085  0.0405  144 VAL   A CA  
3182 C C   . VAL   A 144 ? 0.1286 0.1343 0.2174 -0.0250 -0.0214 0.0331  144 VAL   A C   
3183 O O   . VAL   A 144 ? 0.1458 0.1438 0.2179 -0.0147 -0.0215 0.0375  144 VAL   A O   
3184 C CB  . VAL   A 144 ? 0.1406 0.1708 0.2724 -0.0136 0.0182  0.0476  144 VAL   A CB  
3185 C CG1 . VAL   A 144 ? 0.1518 0.1817 0.3050 -0.0194 0.0024  0.0391  144 VAL   A CG1 
3186 C CG2 . VAL   A 144 ? 0.1298 0.1793 0.2770 -0.0119 0.0260  0.0576  144 VAL   A CG2 
3196 N N   . ASP   A 145 ? 0.1290 0.1313 0.2238 -0.0202 -0.0178 0.0254  145 ASP   A N   
3197 C CA  . ASP   A 145 ? 0.1468 0.1377 0.2385 -0.0209 -0.0283 0.0152  145 ASP   A CA  
3198 C C   . ASP   A 145 ? 0.1446 0.1259 0.2335 -0.0155 -0.0220 0.0050  145 ASP   A C   
3199 O O   . ASP   A 145 ? 0.1610 0.1413 0.2852 -0.0189 -0.0239 -0.0299 145 ASP   A O   
3200 C CB  . ASP   A 145 ? 0.1581 0.1666 0.2623 -0.0273 -0.0408 0.0109  145 ASP   A CB  
3201 C CG  . ASP   A 145 ? 0.1714 0.2008 0.2880 -0.0495 -0.0448 0.0214  145 ASP   A CG  
3202 O OD1 . ASP   A 145 ? 0.1676 0.2118 0.3000 -0.0626 -0.0370 0.0217  145 ASP   A OD1 
3203 O OD2 . ASP   A 145 ? 0.1903 0.2250 0.3002 -0.0577 -0.0569 0.0207  145 ASP   A OD2 
3208 N N   . THR   A 146 ? 0.1306 0.1202 0.1931 -0.0134 -0.0103 0.0141  146 THR   A N   
3209 C CA  . THR   A 146 ? 0.1218 0.1210 0.1693 -0.0084 -0.0074 0.0095  146 THR   A CA  
3210 C C   . THR   A 146 ? 0.1152 0.1162 0.1680 -0.0052 -0.0045 0.0170  146 THR   A C   
3211 O O   . THR   A 146 ? 0.1267 0.1289 0.1841 0.0019  -0.0120 0.0094  146 THR   A O   
3212 C CB  . THR   A 146 ? 0.1197 0.1245 0.1612 -0.0054 -0.0069 0.0127  146 THR   A CB  
3213 O OG1 . THR   A 146 ? 0.1231 0.1381 0.1676 -0.0028 -0.0117 0.0030  146 THR   A OG1 
3214 C CG2 . THR   A 146 ? 0.1227 0.1272 0.1795 -0.0107 -0.0052 0.0105  146 THR   A CG2 
3222 N N   . VAL   A 147 ? 0.1139 0.1211 0.1650 -0.0036 -0.0026 0.0143  147 VAL   A N   
3223 C CA  . VAL   A 147 ? 0.1165 0.1231 0.1604 -0.0078 0.0091  0.0199  147 VAL   A CA  
3224 C C   . VAL   A 147 ? 0.1191 0.1189 0.1739 -0.0111 0.0075  0.0222  147 VAL   A C   
3225 O O   . VAL   A 147 ? 0.1229 0.1264 0.1944 -0.0192 -0.0015 0.0274  147 VAL   A O   
3226 C CB  . VAL   A 147 ? 0.1292 0.1226 0.1603 -0.0124 0.0110  0.0190  147 VAL   A CB  
3227 C CG1 . VAL   A 147 ? 0.1587 0.1311 0.1543 -0.0111 0.0090  0.0232  147 VAL   A CG1 
3228 C CG2 . VAL   A 147 ? 0.1372 0.1207 0.1641 -0.0140 0.0032  0.0221  147 VAL   A CG2 
3238 N N   . ARG   A 148 ? 0.1197 0.1235 0.1738 -0.0113 0.0037  0.0312  148 ARG   A N   
3239 C CA  . ARG   A 148 ? 0.1292 0.1265 0.1722 -0.0110 -0.0011 0.0400  148 ARG   A CA  
3240 C C   . ARG   A 148 ? 0.1419 0.1305 0.1712 -0.0184 0.0004  0.0454  148 ARG   A C   
3241 O O   . ARG   A 148 ? 0.1722 0.1424 0.1918 -0.0239 0.0033  0.0443  148 ARG   A O   
3242 C CB  . ARG   A 148 ? 0.1330 0.1252 0.1952 -0.0106 0.0070  0.0338  148 ARG   A CB  
3243 C CG  . ARG   A 148 ? 0.1433 0.1273 0.2183 -0.0081 0.0179  0.0199  148 ARG   A CG  
3244 C CD  . ARG   A 148 ? 0.1642 0.1314 0.2425 -0.0041 0.0312  0.0411  148 ARG   A CD  
3245 N NE  . ARG   A 148 ? 0.1577 0.1363 0.2475 0.0066  0.0334  0.0475  148 ARG   A NE  
3246 C CZ  . ARG   A 148 ? 0.1564 0.1232 0.2327 0.0032  0.0326  0.0386  148 ARG   A CZ  
3247 N NH1 . ARG   A 148 ? 0.1630 0.1244 0.2383 -0.0053 0.0358  0.0182  148 ARG   A NH1 
3248 N NH2 . ARG   A 148 ? 0.1499 0.1459 0.2313 0.0120  0.0327  0.0438  148 ARG   A NH2 
3262 N N   . THR   A 149 ? 0.1432 0.1364 0.1609 -0.0239 -0.0097 0.0444  149 THR   A N   
3263 C CA  . THR   A 149 ? 0.1471 0.1416 0.1545 -0.0169 -0.0053 0.0386  149 THR   A CA  
3264 C C   . THR   A 149 ? 0.1474 0.1402 0.1470 -0.0266 -0.0016 0.0414  149 THR   A C   
3265 O O   . THR   A 149 ? 0.1481 0.1469 0.1673 -0.0243 -0.0056 0.0327  149 THR   A O   
3266 C CB  . THR   A 149 ? 0.1406 0.1571 0.1717 -0.0214 -0.0002 0.0298  149 THR   A CB  
3267 O OG1 . THR   A 149 ? 0.1452 0.1448 0.1791 -0.0294 -0.0053 0.0244  149 THR   A OG1 
3268 C CG2 . THR   A 149 ? 0.1390 0.1700 0.1833 -0.0169 -0.0024 0.0307  149 THR   A CG2 
3276 N N   . ASN   A 150 ? 0.1489 0.1427 0.1595 -0.0150 -0.0047 0.0359  150 ASN   A N   
3277 C CA  . ASN   A 150 ? 0.1566 0.1561 0.1665 -0.0163 0.0082  0.0362  150 ASN   A CA  
3278 C C   . ASN   A 150 ? 0.1368 0.1442 0.1744 -0.0227 0.0034  0.0334  150 ASN   A C   
3279 O O   . ASN   A 150 ? 0.1477 0.1558 0.2145 -0.0202 -0.0163 0.0257  150 ASN   A O   
3280 C CB  . ASN   A 150 ? 0.1973 0.1857 0.1922 -0.0199 0.0313  0.0565  150 ASN   A CB  
3281 C CG  . ASN   A 150 ? 0.2552 0.2240 0.2747 -0.0184 0.0032  0.0634  150 ASN   A CG  
3282 O OD1 . ASN   A 150 ? 0.2844 0.2383 0.3019 -0.0260 -0.0010 0.0755  150 ASN   A OD1 
3283 N ND2 . ASN   A 150 ? 0.2817 0.2496 0.3158 -0.0093 -0.0087 0.0612  150 ASN   A ND2 
3290 N N   . VAL   A 151 ? 0.1363 0.1366 0.1659 -0.0256 -0.0007 0.0374  151 VAL   A N   
3291 C CA  . VAL   A 151 ? 0.1417 0.1391 0.1682 -0.0272 0.0064  0.0253  151 VAL   A CA  
3292 C C   . VAL   A 151 ? 0.1393 0.1322 0.1809 -0.0294 0.0083  0.0308  151 VAL   A C   
3293 O O   . VAL   A 151 ? 0.1390 0.1420 0.2046 -0.0260 0.0030  0.0274  151 VAL   A O   
3294 C CB  . VAL   A 151 ? 0.1624 0.1530 0.1640 -0.0119 0.0136  0.0280  151 VAL   A CB  
3295 C CG1 . VAL   A 151 ? 0.1513 0.1786 0.1937 -0.0092 0.0073  0.0082  151 VAL   A CG1 
3296 C CG2 . VAL   A 151 ? 0.1745 0.1562 0.1644 -0.0124 0.0285  0.0220  151 VAL   A CG2 
3306 N N   . TYR   A 152 ? 0.1320 0.1349 0.1733 -0.0235 0.0056  0.0306  152 TYR   A N   
3307 C CA  . TYR   A 152 ? 0.1347 0.1372 0.1557 -0.0274 0.0221  0.0200  152 TYR   A CA  
3308 C C   . TYR   A 152 ? 0.1292 0.1374 0.1586 -0.0257 0.0256  0.0282  152 TYR   A C   
3309 O O   . TYR   A 152 ? 0.1378 0.1388 0.1693 -0.0312 0.0200  0.0192  152 TYR   A O   
3310 C CB  . TYR   A 152 ? 0.1513 0.1430 0.1540 -0.0214 0.0264  0.0154  152 TYR   A CB  
3311 C CG  . TYR   A 152 ? 0.1646 0.1578 0.1571 -0.0263 0.0253  0.0253  152 TYR   A CG  
3312 C CD1 . TYR   A 152 ? 0.1746 0.1854 0.1739 -0.0215 0.0247  0.0372  152 TYR   A CD1 
3313 C CD2 . TYR   A 152 ? 0.1645 0.1706 0.1421 -0.0399 0.0184  0.0197  152 TYR   A CD2 
3314 C CE1 . TYR   A 152 ? 0.1931 0.1940 0.1760 -0.0166 0.0058  0.0457  152 TYR   A CE1 
3315 C CE2 . TYR   A 152 ? 0.1799 0.1848 0.1387 -0.0410 0.0230  0.0196  152 TYR   A CE2 
3316 C CZ  . TYR   A 152 ? 0.2026 0.1862 0.1529 -0.0340 0.0125  0.0386  152 TYR   A CZ  
3317 O OH  . TYR   A 152 ? 0.2319 0.2047 0.1784 -0.0169 0.0073  0.0517  152 TYR   A OH  
3327 N N   A LEU   A 153 ? 0.1277 0.1341 0.1593 -0.0253 0.0171  0.0310  153 LEU   A N   
3328 N N   B LEU   A 153 ? 0.1272 0.1466 0.1675 -0.0244 0.0194  0.0356  153 LEU   A N   
3329 C CA  A LEU   A 153 ? 0.1253 0.1275 0.1700 -0.0177 0.0180  0.0308  153 LEU   A CA  
3330 C CA  B LEU   A 153 ? 0.1281 0.1534 0.1879 -0.0147 0.0187  0.0351  153 LEU   A CA  
3331 C C   A LEU   A 153 ? 0.1221 0.1284 0.1770 -0.0175 0.0319  0.0292  153 LEU   A C   
3332 C C   B LEU   A 153 ? 0.1307 0.1654 0.1998 -0.0138 0.0287  0.0342  153 LEU   A C   
3333 O O   A LEU   A 153 ? 0.1315 0.1408 0.1972 -0.0186 0.0355  0.0247  153 LEU   A O   
3334 O O   B LEU   A 153 ? 0.1372 0.1763 0.2340 -0.0165 0.0392  0.0297  153 LEU   A O   
3335 C CB  A LEU   A 153 ? 0.1232 0.1282 0.1734 -0.0201 0.0119  0.0346  153 LEU   A CB  
3336 C CB  B LEU   A 153 ? 0.1219 0.1608 0.1925 -0.0189 0.0201  0.0373  153 LEU   A CB  
3337 C CG  A LEU   A 153 ? 0.1278 0.1279 0.1717 -0.0149 0.0082  0.0299  153 LEU   A CG  
3338 C CG  B LEU   A 153 ? 0.1253 0.1624 0.1844 -0.0180 0.0215  0.0308  153 LEU   A CG  
3339 C CD1 A LEU   A 153 ? 0.1374 0.1340 0.1801 -0.0140 0.0021  0.0347  153 LEU   A CD1 
3340 C CD1 B LEU   A 153 ? 0.1379 0.1691 0.1902 -0.0126 0.0144  0.0327  153 LEU   A CD1 
3341 C CD2 A LEU   A 153 ? 0.1304 0.1301 0.1701 -0.0100 0.0152  0.0179  153 LEU   A CD2 
3342 C CD2 B LEU   A 153 ? 0.1309 0.1650 0.1807 -0.0207 0.0312  0.0233  153 LEU   A CD2 
3365 N N   A ALA   A 154 ? 0.1088 0.1151 0.1590 -0.0155 0.0290  0.0268  154 ALA   A N   
3366 N N   B ALA   A 154 ? 0.1281 0.1661 0.1768 -0.0071 0.0142  0.0304  154 ALA   A N   
3367 C CA  A ALA   A 154 ? 0.1151 0.1204 0.1572 -0.0035 0.0206  0.0202  154 ALA   A CA  
3368 C CA  B ALA   A 154 ? 0.1407 0.1770 0.1791 -0.0009 0.0123  0.0289  154 ALA   A CA  
3369 C C   A ALA   A 154 ? 0.1178 0.1108 0.1603 0.0007  0.0193  0.0214  154 ALA   A C   
3370 C C   B ALA   A 154 ? 0.1434 0.1779 0.1748 -0.0069 0.0033  0.0302  154 ALA   A C   
3371 O O   A ALA   A 154 ? 0.1191 0.1243 0.1687 0.0068  0.0199  0.0127  154 ALA   A O   
3372 O O   B ALA   A 154 ? 0.1516 0.1846 0.1604 -0.0174 -0.0005 0.0378  154 ALA   A O   
3373 C CB  A ALA   A 154 ? 0.1212 0.1337 0.1535 0.0044  0.0127  0.0146  154 ALA   A CB  
3374 C CB  B ALA   A 154 ? 0.1515 0.1829 0.1839 0.0050  0.0028  0.0187  154 ALA   A CB  
3385 N N   A VAL   A 155 ? 0.1252 0.1125 0.1636 0.0033  0.0220  0.0273  155 VAL   A N   
3386 N N   B VAL   A 155 ? 0.1499 0.1782 0.1805 -0.0028 -0.0023 0.0246  155 VAL   A N   
3387 C CA  A VAL   A 155 ? 0.1312 0.1229 0.1777 0.0039  0.0198  0.0326  155 VAL   A CA  
3388 C CA  B VAL   A 155 ? 0.1622 0.1771 0.1889 0.0015  0.0001  0.0281  155 VAL   A CA  
3389 C C   A VAL   A 155 ? 0.1458 0.1358 0.2034 0.0207  0.0189  0.0421  155 VAL   A C   
3390 C C   B VAL   A 155 ? 0.1799 0.1840 0.2056 0.0172  0.0074  0.0249  155 VAL   A C   
3391 O O   A VAL   A 155 ? 0.1461 0.1439 0.2188 0.0293  0.0247  0.0321  155 VAL   A O   
3392 O O   B VAL   A 155 ? 0.1744 0.1900 0.2126 0.0166  -0.0042 0.0214  155 VAL   A O   
3393 C CB  A VAL   A 155 ? 0.1334 0.1269 0.1814 0.0065  0.0075  0.0211  155 VAL   A CB  
3394 C CB  B VAL   A 155 ? 0.1653 0.1771 0.1978 0.0003  -0.0166 0.0261  155 VAL   A CB  
3395 C CG1 A VAL   A 155 ? 0.1462 0.1306 0.1796 0.0168  0.0084  0.0101  155 VAL   A CG1 
3396 C CG1 B VAL   A 155 ? 0.1749 0.1804 0.2029 0.0014  -0.0256 0.0206  155 VAL   A CG1 
3397 C CG2 A VAL   A 155 ? 0.1359 0.1223 0.1894 0.0074  0.0086  0.0199  155 VAL   A CG2 
3398 C CG2 B VAL   A 155 ? 0.1734 0.1801 0.2180 0.0021  -0.0229 0.0271  155 VAL   A CG2 
3417 N N   A PHE   A 156 ? 0.1636 0.1407 0.2303 0.0255  0.0157  0.0561  156 PHE   A N   
3418 N N   B PHE   A 156 ? 0.2032 0.1924 0.2140 0.0350  0.0150  0.0213  156 PHE   A N   
3419 C CA  A PHE   A 156 ? 0.1817 0.1526 0.2382 0.0281  0.0109  0.0542  156 PHE   A CA  
3420 C CA  B PHE   A 156 ? 0.2342 0.2098 0.2339 0.0549  0.0201  0.0224  156 PHE   A CA  
3421 C C   A PHE   A 156 ? 0.1762 0.1622 0.2278 0.0322  0.0166  0.0604  156 PHE   A C   
3422 C C   B PHE   A 156 ? 0.2454 0.2248 0.2428 0.0664  0.0261  0.0238  156 PHE   A C   
3423 O O   A PHE   A 156 ? 0.1810 0.1692 0.2260 0.0260  0.0180  0.0491  156 PHE   A O   
3424 O O   B PHE   A 156 ? 0.2462 0.2237 0.2456 0.0632  0.0412  0.0128  156 PHE   A O   
3425 C CB  A PHE   A 156 ? 0.2039 0.1553 0.2496 0.0270  0.0086  0.0500  156 PHE   A CB  
3426 C CB  B PHE   A 156 ? 0.2626 0.2231 0.2586 0.0555  0.0038  0.0192  156 PHE   A CB  
3427 C CG  A PHE   A 156 ? 0.2240 0.1668 0.2601 0.0286  0.0042  0.0390  156 PHE   A CG  
3428 C CG  B PHE   A 156 ? 0.2927 0.2436 0.2897 0.0557  -0.0129 0.0056  156 PHE   A CG  
3429 C CD1 A PHE   A 156 ? 0.2312 0.1730 0.2511 0.0272  0.0059  0.0375  156 PHE   A CD1 
3430 C CD1 B PHE   A 156 ? 0.3088 0.2550 0.3077 0.0580  -0.0214 -0.0005 156 PHE   A CD1 
3431 C CD2 A PHE   A 156 ? 0.2315 0.1810 0.2659 0.0309  0.0067  0.0359  156 PHE   A CD2 
3432 C CD2 B PHE   A 156 ? 0.3086 0.2522 0.3035 0.0544  -0.0211 -0.0041 156 PHE   A CD2 
3433 C CE1 A PHE   A 156 ? 0.2370 0.1809 0.2596 0.0288  0.0109  0.0277  156 PHE   A CE1 
3434 C CE1 B PHE   A 156 ? 0.3172 0.2583 0.3140 0.0548  -0.0247 -0.0050 156 PHE   A CE1 
3435 C CE2 A PHE   A 156 ? 0.2391 0.1906 0.2734 0.0346  0.0070  0.0268  156 PHE   A CE2 
3436 C CE2 B PHE   A 156 ? 0.3181 0.2575 0.3092 0.0519  -0.0255 -0.0083 156 PHE   A CE2 
3437 C CZ  A PHE   A 156 ? 0.2377 0.1886 0.2692 0.0364  0.0106  0.0183  156 PHE   A CZ  
3438 C CZ  B PHE   A 156 ? 0.3213 0.2615 0.3137 0.0527  -0.0278 -0.0061 156 PHE   A CZ  
3457 N N   A ASP   A 157 ? 0.1763 0.1732 0.2156 0.0352  0.0220  0.0819  157 ASP   A N   
3458 N N   B ASP   A 157 ? 0.2595 0.2389 0.2604 0.0788  0.0103  0.0289  157 ASP   A N   
3459 C CA  A ASP   A 157 ? 0.1837 0.1892 0.2185 0.0349  0.0174  0.0837  157 ASP   A CA  
3460 C CA  B ASP   A 157 ? 0.2832 0.2684 0.2923 0.0727  0.0079  0.0414  157 ASP   A CA  
3461 C C   A ASP   A 157 ? 0.1625 0.1958 0.2160 0.0361  0.0203  0.0913  157 ASP   A C   
3462 C C   B ASP   A 157 ? 0.2833 0.2913 0.2997 0.0731  0.0259  0.0299  157 ASP   A C   
3463 O O   A ASP   A 157 ? 0.1511 0.1817 0.2127 0.0387  0.0262  0.0961  157 ASP   A O   
3464 O O   B ASP   A 157 ? 0.2802 0.2894 0.2825 0.0766  0.0283  0.0313  157 ASP   A O   
3465 C CB  A ASP   A 157 ? 0.2088 0.1970 0.2348 0.0358  0.0204  0.0838  157 ASP   A CB  
3466 C CB  B ASP   A 157 ? 0.3009 0.2713 0.3232 0.0648  -0.0104 0.0621  157 ASP   A CB  
3467 C CG  A ASP   A 157 ? 0.2331 0.2100 0.2569 0.0374  0.0075  0.0828  157 ASP   A CG  
3468 C CG  B ASP   A 157 ? 0.3111 0.2747 0.3500 0.0572  -0.0228 0.0781  157 ASP   A CG  
3469 O OD1 A ASP   A 157 ? 0.2487 0.2146 0.2793 0.0340  -0.0173 0.0835  157 ASP   A OD1 
3470 O OD1 B ASP   A 157 ? 0.3143 0.2830 0.3734 0.0481  -0.0279 0.0802  157 ASP   A OD1 
3471 O OD2 A ASP   A 157 ? 0.2336 0.2131 0.2664 0.0332  0.0188  0.0869  157 ASP   A OD2 
3472 O OD2 B ASP   A 157 ? 0.3122 0.2620 0.3375 0.0579  -0.0272 0.0940  157 ASP   A OD2 
3481 N N   A LYS   A 158 ? 0.1577 0.2150 0.2259 0.0350  0.0177  0.0860  158 LYS   A N   
3482 N N   B LYS   A 158 ? 0.2929 0.3174 0.3264 0.0628  0.0410  0.0249  158 LYS   A N   
3483 C CA  A LYS   A 158 ? 0.1504 0.2355 0.2342 0.0401  0.0227  0.0790  158 LYS   A CA  
3484 C CA  B LYS   A 158 ? 0.3036 0.3452 0.3576 0.0490  0.0517  0.0201  158 LYS   A CA  
3485 C C   A LYS   A 158 ? 0.1345 0.2473 0.2402 0.0418  0.0216  0.0831  158 LYS   A C   
3486 C C   B LYS   A 158 ? 0.2923 0.3482 0.3479 0.0419  0.0461  0.0171  158 LYS   A C   
3487 O O   A LYS   A 158 ? 0.1247 0.2542 0.2523 0.0361  0.0249  0.0928  158 LYS   A O   
3488 O O   B LYS   A 158 ? 0.2910 0.3543 0.3437 0.0393  0.0526  0.0211  158 LYS   A O   
3489 C CB  A LYS   A 158 ? 0.1672 0.2476 0.2490 0.0432  0.0303  0.0738  158 LYS   A CB  
3490 C CB  B LYS   A 158 ? 0.3269 0.3675 0.4027 0.0426  0.0617  0.0217  158 LYS   A CB  
3491 C CG  A LYS   A 158 ? 0.1906 0.2637 0.2774 0.0411  0.0380  0.0613  158 LYS   A CG  
3492 C CG  B LYS   A 158 ? 0.3490 0.3866 0.4448 0.0354  0.0675  0.0251  158 LYS   A CG  
3493 C CD  A LYS   A 158 ? 0.2067 0.2763 0.3073 0.0421  0.0467  0.0550  158 LYS   A CD  
3494 C CD  B LYS   A 158 ? 0.3653 0.4015 0.4791 0.0298  0.0712  0.0272  158 LYS   A CD  
3495 C CE  A LYS   A 158 ? 0.2185 0.2854 0.3354 0.0380  0.0521  0.0535  158 LYS   A CE  
3496 C CE  B LYS   A 158 ? 0.3754 0.4122 0.5000 0.0246  0.0761  0.0280  158 LYS   A CE  
3497 N NZ  A LYS   A 158 ? 0.2266 0.2908 0.3476 0.0328  0.0557  0.0562  158 LYS   A NZ  
3498 N NZ  B LYS   A 158 ? 0.3818 0.4183 0.5116 0.0229  0.0743  0.0284  158 LYS   A NZ  
3525 N N   A ASN   A 159 ? 0.1387 0.2575 0.2520 0.0412  0.0069  0.0773  159 ASN   A N   
3526 N N   B ASN   A 159 ? 0.2813 0.3405 0.3462 0.0359  0.0325  0.0080  159 ASN   A N   
3527 C CA  A ASN   A 159 ? 0.1371 0.2590 0.2649 0.0532  -0.0067 0.0760  159 ASN   A CA  
3528 C CA  B ASN   A 159 ? 0.2698 0.3290 0.3510 0.0314  0.0143  0.0033  159 ASN   A CA  
3529 C C   A ASN   A 159 ? 0.1223 0.2469 0.2562 0.0405  -0.0072 0.0744  159 ASN   A C   
3530 C C   B ASN   A 159 ? 0.2359 0.3002 0.3103 0.0248  0.0068  0.0066  159 ASN   A C   
3531 O O   A ASN   A 159 ? 0.1001 0.2574 0.2601 0.0277  -0.0106 0.0701  159 ASN   A O   
3532 O O   B ASN   A 159 ? 0.2273 0.2958 0.3016 0.0218  -0.0007 -0.0027 159 ASN   A O   
3533 C CB  A ASN   A 159 ? 0.1635 0.2705 0.2934 0.0607  -0.0095 0.0764  159 ASN   A CB  
3534 C CB  B ASN   A 159 ? 0.2949 0.3467 0.4044 0.0292  0.0087  -0.0040 159 ASN   A CB  
3535 C CG  A ASN   A 159 ? 0.1810 0.2800 0.3254 0.0617  -0.0089 0.0714  159 ASN   A CG  
3536 C CG  B ASN   A 159 ? 0.3207 0.3623 0.4559 0.0265  0.0098  -0.0075 159 ASN   A CG  
3537 O OD1 A ASN   A 159 ? 0.1887 0.2822 0.3411 0.0629  0.0000  0.0695  159 ASN   A OD1 
3538 O OD1 B ASN   A 159 ? 0.3325 0.3690 0.4808 0.0256  0.0120  -0.0074 159 ASN   A OD1 
3539 N ND2 A ASN   A 159 ? 0.1910 0.2883 0.3439 0.0546  -0.0046 0.0641  159 ASN   A ND2 
3540 N ND2 B ASN   A 159 ? 0.3312 0.3706 0.4744 0.0235  0.0099  -0.0094 159 ASN   A ND2 
3553 N N   A LEU   A 160 ? 0.1232 0.2223 0.2470 0.0366  -0.0132 0.0723  160 LEU   A N   
3554 N N   B LEU   A 160 ? 0.2112 0.2740 0.2870 0.0247  0.0081  0.0142  160 LEU   A N   
3555 C CA  A LEU   A 160 ? 0.1263 0.2028 0.2353 0.0198  -0.0081 0.0711  160 LEU   A CA  
3556 C CA  B LEU   A 160 ? 0.1968 0.2510 0.2595 0.0134  0.0111  0.0254  160 LEU   A CA  
3557 C C   A LEU   A 160 ? 0.1133 0.2042 0.2450 0.0159  0.0128  0.0621  160 LEU   A C   
3558 C C   B LEU   A 160 ? 0.1738 0.2456 0.2577 0.0063  0.0226  0.0383  160 LEU   A C   
3559 O O   A LEU   A 160 ? 0.1070 0.1941 0.2630 0.0054  0.0155  0.0633  160 LEU   A O   
3560 O O   B LEU   A 160 ? 0.1715 0.2505 0.2721 0.0015  0.0196  0.0269  160 LEU   A O   
3561 C CB  A LEU   A 160 ? 0.1431 0.1916 0.2165 0.0039  -0.0069 0.0626  160 LEU   A CB  
3562 C CB  B LEU   A 160 ? 0.2031 0.2412 0.2454 0.0057  0.0124  0.0238  160 LEU   A CB  
3563 C CG  A LEU   A 160 ? 0.1530 0.1855 0.2076 -0.0135 0.0058  0.0493  160 LEU   A CG  
3564 C CG  B LEU   A 160 ? 0.2101 0.2353 0.2353 -0.0042 0.0146  0.0171  160 LEU   A CG  
3565 C CD1 A LEU   A 160 ? 0.1576 0.1871 0.2047 -0.0181 0.0138  0.0406  160 LEU   A CD1 
3566 C CD1 B LEU   A 160 ? 0.2137 0.2328 0.2321 -0.0087 0.0126  0.0225  160 LEU   A CD1 
3567 C CD2 A LEU   A 160 ? 0.1540 0.1821 0.2091 -0.0206 0.0128  0.0423  160 LEU   A CD2 
3568 C CD2 B LEU   A 160 ? 0.2133 0.2334 0.2324 -0.0092 0.0188  0.0080  160 LEU   A CD2 
3591 N N   A TYR   A 161 ? 0.1053 0.2133 0.2342 0.0178  0.0166  0.0644  161 TYR   A N   
3592 N N   B TYR   A 161 ? 0.1631 0.2411 0.2565 0.0091  0.0239  0.0648  161 TYR   A N   
3593 C CA  A TYR   A 161 ? 0.1121 0.2215 0.2383 0.0165  0.0252  0.0716  161 TYR   A CA  
3594 C CA  B TYR   A 161 ? 0.1610 0.2500 0.2668 0.0117  0.0309  0.0761  161 TYR   A CA  
3595 C C   A TYR   A 161 ? 0.1065 0.2366 0.2460 0.0103  0.0287  0.0798  161 TYR   A C   
3596 C C   B TYR   A 161 ? 0.1566 0.2609 0.2931 0.0029  0.0300  0.0888  161 TYR   A C   
3597 O O   A TYR   A 161 ? 0.1021 0.2372 0.2350 0.0082  0.0340  0.0779  161 TYR   A O   
3598 O O   B TYR   A 161 ? 0.1523 0.2563 0.2882 -0.0079 0.0259  0.0800  161 TYR   A O   
3599 C CB  A TYR   A 161 ? 0.1278 0.2206 0.2402 0.0212  0.0282  0.0601  161 TYR   A CB  
3600 C CB  B TYR   A 161 ? 0.1748 0.2519 0.2741 0.0176  0.0312  0.0684  161 TYR   A CB  
3601 C CG  A TYR   A 161 ? 0.1409 0.2194 0.2356 0.0110  0.0351  0.0464  161 TYR   A CG  
3602 C CG  B TYR   A 161 ? 0.1874 0.2565 0.2791 0.0167  0.0344  0.0628  161 TYR   A CG  
3603 C CD1 A TYR   A 161 ? 0.1457 0.2122 0.2349 0.0047  0.0373  0.0476  161 TYR   A CD1 
3604 C CD1 B TYR   A 161 ? 0.1940 0.2565 0.2784 0.0116  0.0379  0.0686  161 TYR   A CD1 
3605 C CD2 A TYR   A 161 ? 0.1499 0.2222 0.2372 0.0034  0.0341  0.0341  161 TYR   A CD2 
3606 C CD2 B TYR   A 161 ? 0.1962 0.2633 0.2895 0.0184  0.0320  0.0633  161 TYR   A CD2 
3607 C CE1 A TYR   A 161 ? 0.1558 0.2072 0.2313 -0.0059 0.0419  0.0512  161 TYR   A CE1 
3608 C CE1 B TYR   A 161 ? 0.2043 0.2622 0.2919 0.0095  0.0345  0.0756  161 TYR   A CE1 
3609 C CE2 A TYR   A 161 ? 0.1561 0.2155 0.2343 -0.0036 0.0412  0.0366  161 TYR   A CE2 
3610 C CE2 B TYR   A 161 ? 0.2045 0.2662 0.3007 0.0154  0.0345  0.0707  161 TYR   A CE2 
3611 C CZ  A TYR   A 161 ? 0.1663 0.2083 0.2345 -0.0074 0.0380  0.0488  161 TYR   A CZ  
3612 C CZ  B TYR   A 161 ? 0.2139 0.2696 0.3091 0.0122  0.0334  0.0749  161 TYR   A CZ  
3613 O OH  A TYR   A 161 ? 0.1811 0.2047 0.2377 -0.0092 0.0268  0.0541  161 TYR   A OH  
3614 O OH  B TYR   A 161 ? 0.2265 0.2789 0.3356 0.0074  0.0303  0.0734  161 TYR   A OH  
3633 N N   A ASP   A 162 ? 0.1051 0.2496 0.2645 0.0051  0.0347  0.0919  162 ASP   A N   
3634 N N   B ASP   A 162 ? 0.1522 0.2820 0.3218 -0.0019 0.0336  0.1073  162 ASP   A N   
3635 C CA  A ASP   A 162 ? 0.1094 0.2635 0.2733 -0.0049 0.0378  0.1035  162 ASP   A CA  
3636 C CA  B ASP   A 162 ? 0.1554 0.3119 0.3508 -0.0033 0.0296  0.1114  162 ASP   A CA  
3637 C C   A ASP   A 162 ? 0.1137 0.2659 0.2755 -0.0140 0.0320  0.1105  162 ASP   A C   
3638 C C   B ASP   A 162 ? 0.1465 0.3221 0.3528 -0.0026 0.0216  0.1189  162 ASP   A C   
3639 O O   A ASP   A 162 ? 0.1197 0.2640 0.2801 -0.0222 0.0365  0.1047  162 ASP   A O   
3640 O O   B ASP   A 162 ? 0.1429 0.3232 0.3686 -0.0111 0.0238  0.1189  162 ASP   A O   
3641 C CB  A ASP   A 162 ? 0.1155 0.2819 0.2851 0.0040  0.0415  0.1081  162 ASP   A CB  
3642 C CB  B ASP   A 162 ? 0.1730 0.3296 0.3883 0.0018  0.0269  0.1041  162 ASP   A CB  
3643 C CG  A ASP   A 162 ? 0.1293 0.2971 0.2949 0.0125  0.0436  0.1035  162 ASP   A CG  
3644 C CG  B ASP   A 162 ? 0.1883 0.3429 0.4162 0.0074  0.0220  0.0983  162 ASP   A CG  
3645 O OD1 A ASP   A 162 ? 0.1393 0.3027 0.2995 0.0189  0.0524  0.0940  162 ASP   A OD1 
3646 O OD1 B ASP   A 162 ? 0.1898 0.3467 0.4311 0.0058  0.0193  0.0979  162 ASP   A OD1 
3647 O OD2 A ASP   A 162 ? 0.1355 0.3035 0.2984 0.0154  0.0516  0.1064  162 ASP   A OD2 
3648 O OD2 B ASP   A 162 ? 0.2043 0.3484 0.4267 0.0163  0.0218  0.0949  162 ASP   A OD2 
3657 N N   A LYS   A 163 ? 0.1162 0.2751 0.2785 -0.0166 0.0193  0.1278  163 LYS   A N   
3658 N N   B LYS   A 163 ? 0.1521 0.3337 0.3453 -0.0025 0.0114  0.1205  163 LYS   A N   
3659 C CA  A LYS   A 163 ? 0.1341 0.2841 0.2787 -0.0150 0.0099  0.1253  163 LYS   A CA  
3660 C CA  B LYS   A 163 ? 0.1667 0.3439 0.3362 -0.0023 0.0090  0.1138  163 LYS   A CA  
3661 C C   A LYS   A 163 ? 0.1250 0.2798 0.2782 -0.0172 0.0148  0.1147  163 LYS   A C   
3662 C C   B LYS   A 163 ? 0.1500 0.3334 0.3187 -0.0096 0.0150  0.1179  163 LYS   A C   
3663 O O   A LYS   A 163 ? 0.1289 0.2905 0.2978 -0.0186 0.0084  0.1103  163 LYS   A O   
3664 O O   B LYS   A 163 ? 0.1455 0.3386 0.3303 -0.0181 0.0111  0.1185  163 LYS   A O   
3665 C CB  A LYS   A 163 ? 0.1678 0.2984 0.3024 -0.0122 -0.0002 0.1203  163 LYS   A CB  
3666 C CB  B LYS   A 163 ? 0.2099 0.3637 0.3657 0.0082  0.0036  0.0973  163 LYS   A CB  
3667 C CG  A LYS   A 163 ? 0.2075 0.3142 0.3445 -0.0091 0.0013  0.1075  163 LYS   A CG  
3668 C CG  B LYS   A 163 ? 0.2512 0.3816 0.4116 0.0113  0.0106  0.0768  163 LYS   A CG  
3669 C CD  A LYS   A 163 ? 0.2459 0.3285 0.3874 -0.0054 0.0004  0.0918  163 LYS   A CD  
3670 C CD  B LYS   A 163 ? 0.2911 0.3970 0.4595 0.0157  0.0122  0.0611  163 LYS   A CD  
3671 C CE  A LYS   A 163 ? 0.2667 0.3381 0.4218 -0.0035 0.0016  0.0788  163 LYS   A CE  
3672 C CE  B LYS   A 163 ? 0.3133 0.4081 0.4977 0.0197  0.0149  0.0484  163 LYS   A CE  
3673 N NZ  A LYS   A 163 ? 0.2756 0.3445 0.4420 -0.0034 0.0017  0.0719  163 LYS   A NZ  
3674 N NZ  B LYS   A 163 ? 0.3208 0.4141 0.5214 0.0226  0.0146  0.0414  163 LYS   A NZ  
3701 N N   A LEU   A 164 ? 0.1136 0.2621 0.2658 -0.0198 0.0124  0.1076  164 LEU   A N   
3702 N N   B LEU   A 164 ? 0.1325 0.3114 0.2956 -0.0175 0.0162  0.1180  164 LEU   A N   
3703 C CA  A LEU   A 164 ? 0.1208 0.2485 0.2499 -0.0206 0.0171  0.1017  164 LEU   A CA  
3704 C CA  B LEU   A 164 ? 0.1396 0.2936 0.2749 -0.0229 0.0206  0.1125  164 LEU   A CA  
3705 C C   A LEU   A 164 ? 0.1282 0.2517 0.2513 -0.0229 0.0250  0.0995  164 LEU   A C   
3706 C C   B LEU   A 164 ? 0.1471 0.2955 0.2781 -0.0266 0.0219  0.1160  164 LEU   A C   
3707 O O   A LEU   A 164 ? 0.1378 0.2549 0.2586 -0.0228 0.0341  0.0890  164 LEU   A O   
3708 O O   B LEU   A 164 ? 0.1541 0.2978 0.2852 -0.0293 0.0367  0.1067  164 LEU   A O   
3709 C CB  A LEU   A 164 ? 0.1193 0.2359 0.2420 -0.0206 0.0200  0.0975  164 LEU   A CB  
3710 C CB  B LEU   A 164 ? 0.1410 0.2795 0.2613 -0.0227 0.0288  0.0983  164 LEU   A CB  
3711 C CG  A LEU   A 164 ? 0.1188 0.2254 0.2404 -0.0131 0.0150  0.0903  164 LEU   A CG  
3712 C CG  B LEU   A 164 ? 0.1486 0.2696 0.2627 -0.0189 0.0237  0.0817  164 LEU   A CG  
3713 C CD1 A LEU   A 164 ? 0.1148 0.2241 0.2352 -0.0088 0.0113  0.0792  164 LEU   A CD1 
3714 C CD1 B LEU   A 164 ? 0.1447 0.2687 0.2702 -0.0139 0.0156  0.0657  164 LEU   A CD1 
3715 C CD2 A LEU   A 164 ? 0.1291 0.2224 0.2386 -0.0112 0.0172  0.0881  164 LEU   A CD2 
3716 C CD2 B LEU   A 164 ? 0.1626 0.2652 0.2576 -0.0200 0.0272  0.0787  164 LEU   A CD2 
3739 N N   A VAL   A 165 ? 0.1314 0.2536 0.2465 -0.0265 0.0255  0.1005  165 VAL   A N   
3740 N N   B VAL   A 165 ? 0.1511 0.2959 0.2741 -0.0282 0.0157  0.1216  165 VAL   A N   
3741 C CA  A VAL   A 165 ? 0.1324 0.2587 0.2493 -0.0320 0.0335  0.0972  165 VAL   A CA  
3742 C CA  B VAL   A 165 ? 0.1600 0.3005 0.2743 -0.0303 0.0209  0.1206  165 VAL   A CA  
3743 C C   A VAL   A 165 ? 0.1203 0.2645 0.2532 -0.0291 0.0316  0.1028  165 VAL   A C   
3744 C C   B VAL   A 165 ? 0.1508 0.3059 0.2759 -0.0255 0.0239  0.1239  165 VAL   A C   
3745 O O   A VAL   A 165 ? 0.1193 0.2625 0.2498 -0.0253 0.0280  0.1097  165 VAL   A O   
3746 O O   B VAL   A 165 ? 0.1465 0.3048 0.2828 -0.0212 0.0247  0.1212  165 VAL   A O   
3747 C CB  A VAL   A 165 ? 0.1463 0.2575 0.2532 -0.0372 0.0338  0.0829  165 VAL   A CB  
3748 C CB  B VAL   A 165 ? 0.1764 0.3015 0.2814 -0.0363 0.0194  0.1091  165 VAL   A CB  
3749 C CG1 A VAL   A 165 ? 0.1538 0.2567 0.2577 -0.0424 0.0412  0.0781  165 VAL   A CG1 
3750 C CG1 B VAL   A 165 ? 0.1865 0.3047 0.2889 -0.0403 0.0271  0.1022  165 VAL   A CG1 
3751 C CG2 A VAL   A 165 ? 0.1531 0.2573 0.2580 -0.0394 0.0307  0.0836  165 VAL   A CG2 
3752 C CG2 B VAL   A 165 ? 0.1822 0.3022 0.2852 -0.0349 0.0084  0.1078  165 VAL   A CG2 
3771 N N   A SER   A 166 ? 0.1144 0.2745 0.2714 -0.0295 0.0257  0.1009  166 SER   A N   
3772 N N   B SER   A 166 ? 0.1486 0.3130 0.2854 -0.0208 0.0200  0.1200  166 SER   A N   
3773 C CA  A SER   A 166 ? 0.1177 0.2840 0.2755 -0.0365 0.0186  0.1051  166 SER   A CA  
3774 C CA  B SER   A 166 ? 0.1521 0.3240 0.2920 -0.0188 0.0076  0.1070  166 SER   A CA  
3775 C C   A SER   A 166 ? 0.1252 0.3069 0.2820 -0.0307 -0.0046 0.0986  166 SER   A C   
3776 C C   B SER   A 166 ? 0.1383 0.3277 0.2913 -0.0216 -0.0117 0.1004  166 SER   A C   
3777 O O   A SER   A 166 ? 0.1322 0.3111 0.2977 -0.0228 -0.0153 0.0853  166 SER   A O   
3778 O O   B SER   A 166 ? 0.1428 0.3383 0.3122 -0.0212 -0.0144 0.0874  166 SER   A O   
3779 C CB  A SER   A 166 ? 0.1361 0.2775 0.2954 -0.0418 0.0133  0.1056  166 SER   A CB  
3780 C CB  B SER   A 166 ? 0.1833 0.3382 0.3223 -0.0043 -0.0048 0.0850  166 SER   A CB  
3781 O OG  A SER   A 166 ? 0.1578 0.2736 0.3145 -0.0529 0.0156  0.1064  166 SER   A OG  
3782 O OG  B SER   A 166 ? 0.2172 0.3522 0.3446 -0.0067 -0.0046 0.0753  166 SER   A OG  
3793 N N   . SER   A 167 ? 0.1361 0.3264 0.2764 -0.0231 -0.0141 0.1052  167 SER   A N   
3794 C CA  . SER   A 167 ? 0.1621 0.3449 0.2717 -0.0159 -0.0196 0.0918  167 SER   A CA  
3795 C C   . SER   A 167 ? 0.1650 0.3487 0.2636 -0.0137 -0.0162 0.0852  167 SER   A C   
3796 O O   . SER   A 167 ? 0.1798 0.3518 0.2901 -0.0125 -0.0280 0.0780  167 SER   A O   
3797 C CB  . SER   A 167 ? 0.1771 0.3619 0.2801 -0.0118 -0.0095 0.0946  167 SER   A CB  
3798 O OG  . SER   A 167 ? 0.1820 0.3694 0.2724 -0.0162 0.0097  0.1056  167 SER   A OG  
3805 N N   . PHE   A 168 ? 0.1638 0.3507 0.2484 -0.0068 -0.0161 0.0837  168 PHE   A N   
3806 C CA  . PHE   A 168 ? 0.1815 0.3569 0.2653 -0.0125 -0.0140 0.0721  168 PHE   A CA  
3807 C C   . PHE   A 168 ? 0.2309 0.3949 0.3291 -0.0273 -0.0037 0.0509  168 PHE   A C   
3808 O O   . PHE   A 168 ? 0.2175 0.3885 0.3397 -0.0452 0.0280  0.0620  168 PHE   A O   
3809 C CB  . PHE   A 168 ? 0.1753 0.3303 0.2472 -0.0152 -0.0258 0.0695  168 PHE   A CB  
3810 C CG  . PHE   A 168 ? 0.1673 0.3032 0.2317 -0.0226 -0.0327 0.0699  168 PHE   A CG  
3811 C CD1 . PHE   A 168 ? 0.1675 0.3008 0.2427 -0.0256 -0.0318 0.0776  168 PHE   A CD1 
3812 C CD2 . PHE   A 168 ? 0.1675 0.2898 0.2170 -0.0204 -0.0190 0.0649  168 PHE   A CD2 
3813 C CE1 . PHE   A 168 ? 0.1571 0.3008 0.2374 -0.0228 -0.0274 0.0750  168 PHE   A CE1 
3814 C CE2 . PHE   A 168 ? 0.1700 0.2841 0.2225 -0.0238 -0.0131 0.0712  168 PHE   A CE2 
3815 C CZ  . PHE   A 168 ? 0.1620 0.2921 0.2260 -0.0203 -0.0223 0.0728  168 PHE   A CZ  
3825 N N   . LEU   A 169 ? 0.3133 0.4395 0.4235 -0.0282 -0.0391 0.0122  169 LEU   A N   
3826 C CA  . LEU   A 169 ? 0.4067 0.4861 0.5324 -0.0198 -0.0689 -0.0210 169 LEU   A CA  
3827 C C   . LEU   A 169 ? 0.4364 0.4997 0.5781 -0.0165 -0.0830 -0.0265 169 LEU   A C   
3828 O O   . LEU   A 169 ? 0.4492 0.5035 0.5932 -0.0157 -0.0872 -0.0288 169 LEU   A O   
3829 C CB  . LEU   A 169 ? 0.4535 0.5128 0.5846 -0.0158 -0.0785 -0.0415 169 LEU   A CB  
3830 C CG  . LEU   A 169 ? 0.4909 0.5340 0.6240 -0.0128 -0.0827 -0.0585 169 LEU   A CG  
3831 C CD1 . LEU   A 169 ? 0.5051 0.5420 0.6397 -0.0104 -0.0825 -0.0633 169 LEU   A CD1 
3832 C CD2 . LEU   A 169 ? 0.5048 0.5413 0.6360 -0.0129 -0.0833 -0.0649 169 LEU   A CD2 
3833 O OXT . LEU   A 169 ? 0.4429 0.5037 0.5897 -0.0150 -0.0877 -0.0278 169 LEU   A OXT 
3845 N N   A SER   B 1   ? 0.3711 0.3632 0.3895 -0.0990 -0.0638 0.0459  1   SER   B N   
3846 N N   B SER   B 1   ? 0.3676 0.3077 0.3183 -0.1137 -0.0641 0.0219  1   SER   B N   
3847 C CA  A SER   B 1   ? 0.3652 0.3604 0.3838 -0.1011 -0.0639 0.0484  1   SER   B CA  
3848 C CA  B SER   B 1   ? 0.3618 0.3135 0.3280 -0.1166 -0.0723 0.0171  1   SER   B CA  
3849 C C   A SER   B 1   ? 0.3492 0.3552 0.3719 -0.0987 -0.0664 0.0578  1   SER   B C   
3850 C C   B SER   B 1   ? 0.3431 0.3272 0.3408 -0.1124 -0.0797 0.0416  1   SER   B C   
3851 O O   A SER   B 1   ? 0.3528 0.3557 0.3582 -0.0953 -0.0696 0.0558  1   SER   B O   
3852 O O   B SER   B 1   ? 0.3469 0.3269 0.3234 -0.1089 -0.0848 0.0422  1   SER   B O   
3853 C CB  A SER   B 1   ? 0.3722 0.3609 0.3939 -0.1035 -0.0588 0.0409  1   SER   B CB  
3854 C CB  B SER   B 1   ? 0.3721 0.3022 0.3329 -0.1187 -0.0664 -0.0121 1   SER   B CB  
3855 O OG  A SER   B 1   ? 0.3780 0.3640 0.4092 -0.1058 -0.0526 0.0382  1   SER   B OG  
3856 O OG  B SER   B 1   ? 0.3817 0.3004 0.3469 -0.1161 -0.0586 -0.0240 1   SER   B OG  
3871 N N   A MET   B 2   ? 0.3318 0.3475 0.3712 -0.0967 -0.0621 0.0763  2   MET   B N   
3872 N N   B MET   B 2   ? 0.3263 0.3377 0.3569 -0.1044 -0.0764 0.0751  2   MET   B N   
3873 C CA  A MET   B 2   ? 0.3174 0.3390 0.3734 -0.0873 -0.0604 0.0855  2   MET   B CA  
3874 C CA  B MET   B 2   ? 0.3151 0.3449 0.3691 -0.0844 -0.0767 0.0971  2   MET   B CA  
3875 C C   A MET   B 2   ? 0.2800 0.3043 0.3208 -0.0874 -0.0715 0.1038  2   MET   B C   
3876 C C   B MET   B 2   ? 0.2793 0.3176 0.3206 -0.0733 -0.0871 0.1265  2   MET   B C   
3877 O O   A MET   B 2   ? 0.2704 0.3047 0.3123 -0.0878 -0.0809 0.1097  2   MET   B O   
3878 O O   B MET   B 2   ? 0.2740 0.3275 0.3240 -0.0608 -0.1016 0.1298  2   MET   B O   
3879 C CB  A MET   B 2   ? 0.3430 0.3676 0.4362 -0.0711 -0.0478 0.0693  2   MET   B CB  
3880 C CB  B MET   B 2   ? 0.3452 0.3826 0.4389 -0.0656 -0.0667 0.0819  2   MET   B CB  
3881 C CG  A MET   B 2   ? 0.3643 0.3915 0.4940 -0.0572 -0.0351 0.0593  2   MET   B CG  
3882 C CG  B MET   B 2   ? 0.3690 0.4134 0.4986 -0.0500 -0.0568 0.0752  2   MET   B CG  
3883 S SD  A MET   B 2   ? 0.3827 0.4129 0.5455 -0.0459 -0.0253 0.0511  2   MET   B SD  
3884 S SD  B MET   B 2   ? 0.3891 0.4412 0.5507 -0.0377 -0.0506 0.0696  2   MET   B SD  
3885 C CE  A MET   B 2   ? 0.3864 0.4190 0.5527 -0.0430 -0.0197 0.0500  2   MET   B CE  
3886 C CE  B MET   B 2   ? 0.3930 0.4495 0.5599 -0.0349 -0.0439 0.0680  2   MET   B CE  
3905 N N   A VAL   B 3   ? 0.2523 0.2664 0.2824 -0.0932 -0.0696 0.1113  3   VAL   B N   
3906 N N   B VAL   B 3   ? 0.2493 0.2772 0.2781 -0.0826 -0.0771 0.1422  3   VAL   B N   
3907 C CA  A VAL   B 3   ? 0.2344 0.2351 0.2619 -0.0864 -0.0706 0.1000  3   VAL   B CA  
3908 C CA  B VAL   B 3   ? 0.2336 0.2456 0.2695 -0.0774 -0.0723 0.1171  3   VAL   B CA  
3909 C C   A VAL   B 3   ? 0.2095 0.2170 0.2298 -0.0744 -0.0700 0.0962  3   VAL   B C   
3910 C C   B VAL   B 3   ? 0.2086 0.2267 0.2381 -0.0667 -0.0666 0.1006  3   VAL   B C   
3911 O O   A VAL   B 3   ? 0.2056 0.2209 0.2279 -0.0713 -0.0694 0.1117  3   VAL   B O   
3912 O O   B VAL   B 3   ? 0.2055 0.2390 0.2469 -0.0558 -0.0634 0.1071  3   VAL   B O   
3913 C CB  A VAL   B 3   ? 0.2453 0.2324 0.2864 -0.0850 -0.0701 0.0854  3   VAL   B CB  
3914 C CB  B VAL   B 3   ? 0.2487 0.2426 0.3045 -0.0767 -0.0723 0.1000  3   VAL   B CB  
3915 C CG1 A VAL   B 3   ? 0.2498 0.2294 0.3001 -0.0817 -0.0700 0.0803  3   VAL   B CG1 
3916 C CG1 B VAL   B 3   ? 0.2541 0.2383 0.3231 -0.0743 -0.0724 0.0936  3   VAL   B CG1 
3917 C CG2 A VAL   B 3   ? 0.2497 0.2361 0.2973 -0.0833 -0.0631 0.0874  3   VAL   B CG2 
3918 C CG2 B VAL   B 3   ? 0.2553 0.2480 0.3165 -0.0743 -0.0659 0.1031  3   VAL   B CG2 
3937 N N   . ASN   B 4   ? 0.1936 0.1983 0.2138 -0.0604 -0.0661 0.0838  4   ASN   B N   
3938 C CA  . ASN   B 4   ? 0.1914 0.1919 0.1841 -0.0586 -0.0447 0.0403  4   ASN   B CA  
3939 C C   . ASN   B 4   ? 0.2002 0.1972 0.1776 -0.0598 -0.0348 0.0243  4   ASN   B C   
3940 O O   . ASN   B 4   ? 0.2039 0.2078 0.2092 -0.0560 -0.0235 0.0039  4   ASN   B O   
3941 C CB  . ASN   B 4   ? 0.1844 0.1846 0.1761 -0.0467 -0.0515 0.0322  4   ASN   B CB  
3942 C CG  . ASN   B 4   ? 0.1793 0.1650 0.1671 -0.0396 -0.0420 0.0231  4   ASN   B CG  
3943 O OD1 . ASN   B 4   ? 0.1755 0.1561 0.1602 -0.0359 -0.0426 0.0181  4   ASN   B OD1 
3944 N ND2 . ASN   B 4   ? 0.2007 0.1753 0.1745 -0.0199 -0.0224 0.0212  4   ASN   B ND2 
3952 N N   . SER   B 5   ? 0.2192 0.2082 0.1861 -0.0604 -0.0146 0.0261  5   SER   B N   
3953 C CA  . SER   B 5   ? 0.2461 0.2383 0.2322 -0.0500 0.0116  0.0284  5   SER   B CA  
3954 C C   . SER   B 5   ? 0.2572 0.2407 0.2559 -0.0620 0.0392  0.0286  5   SER   B C   
3955 O O   . SER   B 5   ? 0.2695 0.2434 0.3176 -0.0506 0.0535  0.0337  5   SER   B O   
3956 C CB  . SER   B 5   ? 0.2606 0.2650 0.2751 -0.0381 0.0180  0.0397  5   SER   B CB  
3957 O OG  . SER   B 5   ? 0.2865 0.2956 0.3371 -0.0242 0.0207  0.0416  5   SER   B OG  
3963 N N   . PHE   B 6   ? 0.2735 0.2556 0.2255 -0.0649 0.0507  0.0259  6   PHE   B N   
3964 C CA  . PHE   B 6   ? 0.2826 0.2596 0.1998 -0.0798 0.0486  0.0122  6   PHE   B CA  
3965 C C   . PHE   B 6   ? 0.3360 0.2882 0.2401 -0.0771 0.0666  -0.0170 6   PHE   B C   
3966 O O   . PHE   B 6   ? 0.3501 0.3204 0.2615 -0.0653 0.0498  -0.0301 6   PHE   B O   
3967 C CB  . PHE   B 6   ? 0.2465 0.2447 0.1886 -0.0738 0.0191  0.0118  6   PHE   B CB  
3968 C CG  . PHE   B 6   ? 0.2143 0.2185 0.1769 -0.0629 0.0076  0.0139  6   PHE   B CG  
3969 C CD1 . PHE   B 6   ? 0.2081 0.1948 0.1583 -0.0586 -0.0050 0.0121  6   PHE   B CD1 
3970 C CD2 . PHE   B 6   ? 0.1959 0.2147 0.1792 -0.0512 0.0122  0.0308  6   PHE   B CD2 
3971 C CE1 . PHE   B 6   ? 0.1975 0.1799 0.1669 -0.0459 -0.0089 -0.0014 6   PHE   B CE1 
3972 C CE2 . PHE   B 6   ? 0.1916 0.1989 0.1960 -0.0374 0.0128  0.0284  6   PHE   B CE2 
3973 C CZ  . PHE   B 6   ? 0.1873 0.1810 0.1737 -0.0414 0.0070  0.0030  6   PHE   B CZ  
3983 N N   A SER   B 7   ? 0.3511 0.2782 0.2470 -0.0867 0.0816  -0.0282 7   SER   B N   
3984 N N   B SER   B 7   ? 0.3577 0.2739 0.2369 -0.0887 0.0909  -0.0322 7   SER   B N   
3985 C CA  A SER   B 7   ? 0.3664 0.2781 0.2729 -0.0863 0.0930  -0.0317 7   SER   B CA  
3986 C CA  B SER   B 7   ? 0.3801 0.2781 0.2642 -0.0853 0.1089  -0.0349 7   SER   B CA  
3987 C C   A SER   B 7   ? 0.3650 0.2647 0.2600 -0.0872 0.1015  -0.0381 7   SER   B C   
3988 C C   B SER   B 7   ? 0.3784 0.2680 0.2462 -0.0853 0.1193  -0.0424 7   SER   B C   
3989 O O   A SER   B 7   ? 0.3687 0.2660 0.2719 -0.0881 0.1032  -0.0347 7   SER   B O   
3990 O O   B SER   B 7   ? 0.3844 0.2726 0.2657 -0.0853 0.1215  -0.0366 7   SER   B O   
3991 C CB  A SER   B 7   ? 0.3777 0.2892 0.3164 -0.0834 0.0971  -0.0281 7   SER   B CB  
3992 C CB  B SER   B 7   ? 0.3969 0.2913 0.3176 -0.0802 0.1156  -0.0311 7   SER   B CB  
3993 O OG  A SER   B 7   ? 0.3846 0.2994 0.3507 -0.0818 0.0977  -0.0276 7   SER   B OG  
3994 O OG  B SER   B 7   ? 0.4081 0.3058 0.3618 -0.0759 0.1147  -0.0324 7   SER   B OG  
4005 N N   A GLY   B 8   ? 0.3632 0.2534 0.2559 -0.0815 0.1026  -0.0438 8   GLY   B N   
4006 N N   B GLY   B 8   ? 0.3744 0.2589 0.2457 -0.0781 0.1183  -0.0486 8   GLY   B N   
4007 C CA  A GLY   B 8   ? 0.3562 0.2389 0.2514 -0.0784 0.1058  -0.0466 8   GLY   B CA  
4008 C CA  B GLY   B 8   ? 0.3629 0.2443 0.2437 -0.0756 0.1202  -0.0513 8   GLY   B CA  
4009 C C   A GLY   B 8   ? 0.3474 0.2223 0.2452 -0.0778 0.1081  -0.0432 8   GLY   B C   
4010 C C   B GLY   B 8   ? 0.3489 0.2261 0.2409 -0.0773 0.1169  -0.0459 8   GLY   B C   
4011 O O   A GLY   B 8   ? 0.3530 0.2230 0.2635 -0.0760 0.1104  -0.0430 8   GLY   B O   
4012 O O   B GLY   B 8   ? 0.3553 0.2349 0.2626 -0.0696 0.1183  -0.0487 8   GLY   B O   
4019 N N   . TYR   B 9   ? 0.3369 0.2118 0.2240 -0.0710 0.0998  -0.0468 9   TYR   B N   
4020 C CA  . TYR   B 9   ? 0.3137 0.1833 0.1924 -0.0530 0.0675  -0.0344 9   TYR   B CA  
4021 C C   . TYR   B 9   ? 0.3027 0.1890 0.1844 -0.0449 0.0279  -0.0225 9   TYR   B C   
4022 O O   . TYR   B 9   ? 0.3140 0.2180 0.2211 -0.0467 0.0202  -0.0068 9   TYR   B O   
4023 C CB  . TYR   B 9   ? 0.3077 0.1654 0.1977 -0.0419 0.0650  -0.0262 9   TYR   B CB  
4024 C CG  . TYR   B 9   ? 0.3007 0.1479 0.2046 -0.0480 0.0617  -0.0314 9   TYR   B CG  
4025 C CD1 . TYR   B 9   ? 0.3019 0.1483 0.2279 -0.0645 0.0620  -0.0350 9   TYR   B CD1 
4026 C CD2 . TYR   B 9   ? 0.2863 0.1372 0.2044 -0.0455 0.0583  -0.0355 9   TYR   B CD2 
4027 C CE1 . TYR   B 9   ? 0.2906 0.1583 0.2342 -0.0688 0.0720  -0.0426 9   TYR   B CE1 
4028 C CE2 . TYR   B 9   ? 0.2834 0.1409 0.2143 -0.0441 0.0636  -0.0350 9   TYR   B CE2 
4029 C CZ  . TYR   B 9   ? 0.2845 0.1591 0.2385 -0.0594 0.0652  -0.0532 9   TYR   B CZ  
4030 O OH  . TYR   B 9   ? 0.2789 0.1745 0.2521 -0.0742 0.0691  -0.0676 9   TYR   B OH  
4041 N N   . LEU   B 10  ? 0.2781 0.1615 0.1663 -0.0417 0.0020  -0.0256 10  LEU   B N   
4042 C CA  . LEU   B 10  ? 0.2686 0.1587 0.1714 -0.0465 -0.0171 -0.0312 10  LEU   B CA  
4043 C C   . LEU   B 10  ? 0.2476 0.1562 0.1677 -0.0441 -0.0242 -0.0242 10  LEU   B C   
4044 O O   . LEU   B 10  ? 0.2336 0.1588 0.1675 -0.0352 -0.0161 -0.0193 10  LEU   B O   
4045 C CB  . LEU   B 10  ? 0.2825 0.1588 0.1916 -0.0472 -0.0303 -0.0232 10  LEU   B CB  
4046 C CG  . LEU   B 10  ? 0.2963 0.1714 0.2287 -0.0473 -0.0601 -0.0080 10  LEU   B CG  
4047 C CD1 . LEU   B 10  ? 0.3054 0.1909 0.2545 -0.0473 -0.0638 -0.0073 10  LEU   B CD1 
4048 C CD2 . LEU   B 10  ? 0.3067 0.1787 0.2568 -0.0548 -0.0575 0.0096  10  LEU   B CD2 
4060 N N   . LYS   B 11  ? 0.2583 0.1834 0.1744 -0.0358 -0.0272 -0.0261 11  LYS   B N   
4061 C CA  . LYS   B 11  ? 0.2722 0.2139 0.1862 -0.0296 -0.0450 -0.0247 11  LYS   B CA  
4062 C C   . LYS   B 11  ? 0.2551 0.2002 0.1936 -0.0538 -0.0440 -0.0384 11  LYS   B C   
4063 O O   . LYS   B 11  ? 0.2700 0.2224 0.2395 -0.0637 -0.0425 -0.0693 11  LYS   B O   
4064 C CB  . LYS   B 11  ? 0.3057 0.2661 0.2384 -0.0077 -0.0482 -0.0097 11  LYS   B CB  
4065 C CG  . LYS   B 11  ? 0.3375 0.3012 0.2987 0.0042  -0.0400 -0.0054 11  LYS   B CG  
4066 C CD  . LYS   B 11  ? 0.3623 0.3267 0.3663 0.0102  -0.0324 -0.0065 11  LYS   B CD  
4067 C CE  . LYS   B 11  ? 0.3805 0.3422 0.4164 0.0111  -0.0255 -0.0017 11  LYS   B CE  
4068 N NZ  . LYS   B 11  ? 0.3920 0.3517 0.4476 0.0102  -0.0200 0.0030  11  LYS   B NZ  
4082 N N   . LEU   B 12  ? 0.2245 0.1755 0.1996 -0.0542 -0.0293 -0.0436 12  LEU   B N   
4083 C CA  . LEU   B 12  ? 0.2117 0.1600 0.2184 -0.0516 -0.0301 -0.0338 12  LEU   B CA  
4084 C C   . LEU   B 12  ? 0.2078 0.1621 0.2335 -0.0491 -0.0465 -0.0252 12  LEU   B C   
4085 O O   . LEU   B 12  ? 0.2084 0.1659 0.2531 -0.0616 -0.0528 -0.0233 12  LEU   B O   
4086 C CB  . LEU   B 12  ? 0.2120 0.1415 0.2259 -0.0397 -0.0181 -0.0350 12  LEU   B CB  
4087 C CG  . LEU   B 12  ? 0.2099 0.1389 0.2253 -0.0373 -0.0165 -0.0279 12  LEU   B CG  
4088 C CD1 . LEU   B 12  ? 0.2229 0.1408 0.2217 -0.0203 -0.0116 -0.0107 12  LEU   B CD1 
4089 C CD2 . LEU   B 12  ? 0.2160 0.1457 0.2435 -0.0314 -0.0126 -0.0342 12  LEU   B CD2 
4101 N N   . THR   B 13  ? 0.1984 0.1663 0.2426 -0.0482 -0.0508 -0.0334 13  THR   B N   
4102 C CA  . THR   B 13  ? 0.1997 0.1726 0.2373 -0.0522 -0.0561 -0.0211 13  THR   B CA  
4103 C C   . THR   B 13  ? 0.2360 0.1876 0.2473 -0.0564 -0.0685 -0.0170 13  THR   B C   
4104 O O   . THR   B 13  ? 0.2518 0.1837 0.2737 -0.0548 -0.0354 -0.0241 13  THR   B O   
4105 C CB  . THR   B 13  ? 0.1865 0.1777 0.2439 -0.0461 -0.0574 -0.0180 13  THR   B CB  
4106 O OG1 . THR   B 13  ? 0.1774 0.1724 0.2428 -0.0441 -0.0464 -0.0187 13  THR   B OG1 
4107 C CG2 . THR   B 13  ? 0.2016 0.1805 0.2523 -0.0389 -0.0514 -0.0219 13  THR   B CG2 
4115 N N   A ASP   B 14  ? 0.2455 0.1983 0.2590 -0.0611 -0.0838 -0.0089 14  ASP   B N   
4116 N N   B ASP   B 14  ? 0.2475 0.2022 0.2549 -0.0607 -0.0890 -0.0040 14  ASP   B N   
4117 C CA  A ASP   B 14  ? 0.2574 0.2146 0.2780 -0.0615 -0.0870 0.0021  14  ASP   B CA  
4118 C CA  B ASP   B 14  ? 0.2634 0.2241 0.2737 -0.0581 -0.0906 0.0113  14  ASP   B CA  
4119 C C   A ASP   B 14  ? 0.2457 0.1967 0.2422 -0.0614 -0.0786 0.0081  14  ASP   B C   
4120 C C   B ASP   B 14  ? 0.2522 0.2021 0.2412 -0.0607 -0.0783 0.0143  14  ASP   B C   
4121 O O   A ASP   B 14  ? 0.2626 0.2084 0.2462 -0.0636 -0.0774 0.0141  14  ASP   B O   
4122 O O   B ASP   B 14  ? 0.2760 0.2160 0.2531 -0.0627 -0.0744 0.0247  14  ASP   B O   
4123 C CB  A ASP   B 14  ? 0.2763 0.2444 0.3360 -0.0614 -0.0934 0.0019  14  ASP   B CB  
4124 C CB  B ASP   B 14  ? 0.2855 0.2624 0.3329 -0.0520 -0.0957 0.0149  14  ASP   B CB  
4125 C CG  A ASP   B 14  ? 0.2948 0.2673 0.3898 -0.0620 -0.0895 -0.0034 14  ASP   B CG  
4126 C CG  B ASP   B 14  ? 0.3081 0.2944 0.3914 -0.0485 -0.0870 0.0093  14  ASP   B CG  
4127 O OD1 A ASP   B 14  ? 0.3037 0.2721 0.3990 -0.0685 -0.0892 -0.0119 14  ASP   B OD1 
4128 O OD1 B ASP   B 14  ? 0.3167 0.3057 0.4007 -0.0500 -0.0798 0.0032  14  ASP   B OD1 
4129 O OD2 A ASP   B 14  ? 0.2990 0.2781 0.4181 -0.0623 -0.0858 -0.0027 14  ASP   B OD2 
4130 O OD2 B ASP   B 14  ? 0.3156 0.3112 0.4228 -0.0505 -0.0856 0.0082  14  ASP   B OD2 
4139 N N   . ASN   B 15  ? 0.2171 0.1712 0.2090 -0.0489 -0.0816 0.0115  15  ASN   B N   
4140 C CA  . ASN   B 15  ? 0.1763 0.1458 0.2011 -0.0282 -0.0524 0.0022  15  ASN   B CA  
4141 C C   . ASN   B 15  ? 0.1577 0.1331 0.1970 -0.0202 -0.0418 -0.0077 15  ASN   B C   
4142 O O   . ASN   B 15  ? 0.1625 0.1293 0.2167 -0.0208 -0.0545 -0.0155 15  ASN   B O   
4143 C CB  . ASN   B 15  ? 0.1673 0.1429 0.2081 -0.0106 -0.0494 0.0002  15  ASN   B CB  
4144 C CG  . ASN   B 15  ? 0.1548 0.1464 0.2217 -0.0174 -0.0279 0.0017  15  ASN   B CG  
4145 O OD1 . ASN   B 15  ? 0.1561 0.1738 0.2475 -0.0371 -0.0340 0.0094  15  ASN   B OD1 
4146 N ND2 . ASN   B 15  ? 0.1599 0.1271 0.2118 -0.0136 -0.0048 -0.0082 15  ASN   B ND2 
4154 N N   . VAL   B 16  ? 0.1619 0.1260 0.1852 -0.0276 -0.0513 -0.0060 16  VAL   B N   
4155 C CA  . VAL   B 16  ? 0.1598 0.1271 0.1882 -0.0241 -0.0396 -0.0184 16  VAL   B CA  
4156 C C   . VAL   B 16  ? 0.1597 0.1342 0.1815 -0.0308 -0.0417 -0.0161 16  VAL   B C   
4157 O O   . VAL   B 16  ? 0.1693 0.1478 0.2096 -0.0243 -0.0382 -0.0235 16  VAL   B O   
4158 C CB  . VAL   B 16  ? 0.1653 0.1308 0.1984 -0.0111 -0.0218 -0.0199 16  VAL   B CB  
4159 C CG1 . VAL   B 16  ? 0.1746 0.1365 0.1862 0.0047  -0.0197 -0.0055 16  VAL   B CG1 
4160 C CG2 . VAL   B 16  ? 0.1687 0.1392 0.2155 -0.0075 -0.0112 -0.0119 16  VAL   B CG2 
4170 N N   . TYR   B 17  ? 0.1632 0.1397 0.1702 -0.0221 -0.0344 -0.0178 17  TYR   B N   
4171 C CA  . TYR   B 17  ? 0.1732 0.1478 0.1711 -0.0251 -0.0272 -0.0026 17  TYR   B CA  
4172 C C   . TYR   B 17  ? 0.1688 0.1281 0.1744 -0.0291 -0.0197 -0.0093 17  TYR   B C   
4173 O O   . TYR   B 17  ? 0.1696 0.1371 0.1798 -0.0237 -0.0330 -0.0312 17  TYR   B O   
4174 C CB  . TYR   B 17  ? 0.1952 0.1828 0.1891 -0.0168 -0.0273 0.0301  17  TYR   B CB  
4175 C CG  . TYR   B 17  ? 0.2232 0.2231 0.2248 -0.0069 -0.0329 0.0331  17  TYR   B CG  
4176 C CD1 . TYR   B 17  ? 0.2365 0.2341 0.2337 -0.0012 -0.0365 0.0441  17  TYR   B CD1 
4177 C CD2 . TYR   B 17  ? 0.2448 0.2524 0.2414 -0.0008 -0.0397 0.0283  17  TYR   B CD2 
4178 C CE1 . TYR   B 17  ? 0.2566 0.2622 0.2441 0.0060  -0.0451 0.0446  17  TYR   B CE1 
4179 C CE2 . TYR   B 17  ? 0.2598 0.2736 0.2600 0.0121  -0.0500 0.0345  17  TYR   B CE2 
4180 C CZ  . TYR   B 17  ? 0.2691 0.2774 0.2613 0.0155  -0.0577 0.0458  17  TYR   B CZ  
4181 O OH  . TYR   B 17  ? 0.2859 0.3020 0.2951 0.0247  -0.0634 0.0461  17  TYR   B OH  
4191 N N   . ILE   B 18  ? 0.1726 0.1281 0.1653 -0.0250 -0.0119 -0.0161 18  ILE   B N   
4192 C CA  . ILE   B 18  ? 0.1772 0.1256 0.1567 -0.0245 -0.0147 -0.0123 18  ILE   B CA  
4193 C C   . ILE   B 18  ? 0.1896 0.1327 0.1536 -0.0373 -0.0145 -0.0299 18  ILE   B C   
4194 O O   . ILE   B 18  ? 0.2138 0.1495 0.1580 -0.0307 0.0056  -0.0298 18  ILE   B O   
4195 C CB  . ILE   B 18  ? 0.1807 0.1250 0.1760 -0.0307 -0.0173 -0.0086 18  ILE   B CB  
4196 C CG1 . ILE   B 18  ? 0.1844 0.1297 0.1921 -0.0326 -0.0089 0.0058  18  ILE   B CG1 
4197 C CG2 . ILE   B 18  ? 0.1872 0.1336 0.1819 -0.0342 -0.0208 -0.0139 18  ILE   B CG2 
4198 C CD1 . ILE   B 18  ? 0.1884 0.1577 0.2135 -0.0326 -0.0283 0.0223  18  ILE   B CD1 
4210 N N   . LYS   B 19  ? 0.1871 0.1317 0.1664 -0.0194 0.0116  -0.0269 19  LYS   B N   
4211 C CA  . LYS   B 19  ? 0.1968 0.1386 0.1773 -0.0238 0.0125  -0.0256 19  LYS   B CA  
4212 C C   . LYS   B 19  ? 0.1771 0.1362 0.1761 -0.0187 0.0209  -0.0342 19  LYS   B C   
4213 O O   . LYS   B 19  ? 0.1728 0.1459 0.1731 -0.0141 0.0151  -0.0306 19  LYS   B O   
4214 C CB  . LYS   B 19  ? 0.2204 0.1559 0.1931 -0.0244 0.0246  -0.0175 19  LYS   B CB  
4215 C CG  . LYS   B 19  ? 0.2405 0.1774 0.2055 -0.0282 0.0379  -0.0249 19  LYS   B CG  
4216 C CD  . LYS   B 19  ? 0.2665 0.2071 0.2226 -0.0401 0.0405  -0.0110 19  LYS   B CD  
4217 C CE  . LYS   B 19  ? 0.2889 0.2337 0.2443 -0.0425 0.0370  -0.0067 19  LYS   B CE  
4218 N NZ  . LYS   B 19  ? 0.3020 0.2489 0.2601 -0.0489 0.0392  -0.0051 19  LYS   B NZ  
4232 N N   . ASN   B 20  ? 0.1717 0.1494 0.2000 -0.0114 0.0250  -0.0442 20  ASN   B N   
4233 C CA  . ASN   B 20  ? 0.1739 0.1599 0.2281 -0.0096 0.0263  -0.0552 20  ASN   B CA  
4234 C C   . ASN   B 20  ? 0.1719 0.1771 0.2405 -0.0196 0.0373  -0.0612 20  ASN   B C   
4235 O O   . ASN   B 20  ? 0.1910 0.2116 0.2542 -0.0286 0.0371  -0.0588 20  ASN   B O   
4236 C CB  . ASN   B 20  ? 0.1992 0.1581 0.2549 0.0097  0.0181  -0.0516 20  ASN   B CB  
4237 C CG  . ASN   B 20  ? 0.2220 0.1615 0.2849 0.0327  0.0186  -0.0528 20  ASN   B CG  
4238 O OD1 . ASN   B 20  ? 0.2492 0.1896 0.3166 0.0543  0.0128  -0.0586 20  ASN   B OD1 
4239 N ND2 . ASN   B 20  ? 0.2159 0.1606 0.2732 0.0287  0.0110  -0.0515 20  ASN   B ND2 
4246 N N   . ALA   B 21  ? 0.1810 0.1581 0.2450 -0.0212 0.0362  -0.0505 21  ALA   B N   
4247 C CA  . ALA   B 21  ? 0.1890 0.1679 0.2591 -0.0298 0.0218  -0.0385 21  ALA   B CA  
4248 C C   . ALA   B 21  ? 0.1827 0.1480 0.2449 -0.0194 0.0302  -0.0222 21  ALA   B C   
4249 O O   . ALA   B 21  ? 0.1842 0.1393 0.2505 -0.0274 0.0262  -0.0174 21  ALA   B O   
4250 C CB  . ALA   B 21  ? 0.2053 0.1960 0.2648 -0.0415 0.0178  -0.0158 21  ALA   B CB  
4256 N N   . ASP   B 22  ? 0.1725 0.1442 0.2510 -0.0209 0.0210  -0.0201 22  ASP   B N   
4257 C CA  . ASP   B 22  ? 0.1738 0.1375 0.2410 -0.0116 0.0204  -0.0158 22  ASP   B CA  
4258 C C   . ASP   B 22  ? 0.1633 0.1380 0.2083 -0.0144 0.0171  -0.0039 22  ASP   B C   
4259 O O   . ASP   B 22  ? 0.1724 0.1372 0.2091 -0.0069 0.0076  0.0012  22  ASP   B O   
4260 C CB  . ASP   B 22  ? 0.1886 0.1442 0.2754 -0.0037 0.0193  0.0032  22  ASP   B CB  
4261 C CG  . ASP   B 22  ? 0.1929 0.1609 0.3104 0.0005  -0.0116 -0.0005 22  ASP   B CG  
4262 O OD1 . ASP   B 22  ? 0.2061 0.1580 0.3125 0.0011  -0.0339 -0.0039 22  ASP   B OD1 
4263 O OD2 . ASP   B 22  ? 0.2070 0.1963 0.3513 0.0127  -0.0300 -0.0149 22  ASP   B OD2 
4268 N N   . ILE   B 23  ? 0.1637 0.1336 0.1940 -0.0121 0.0047  0.0145  23  ILE   B N   
4269 C CA  . ILE   B 23  ? 0.1591 0.1319 0.1822 -0.0071 -0.0052 0.0075  23  ILE   B CA  
4270 C C   . ILE   B 23  ? 0.1516 0.1289 0.1823 -0.0034 -0.0083 0.0023  23  ILE   B C   
4271 O O   . ILE   B 23  ? 0.1424 0.1272 0.1775 -0.0076 -0.0091 0.0086  23  ILE   B O   
4272 C CB  . ILE   B 23  ? 0.1539 0.1353 0.1866 -0.0204 -0.0041 0.0127  23  ILE   B CB  
4273 C CG1 . ILE   B 23  ? 0.1615 0.1480 0.2003 -0.0115 0.0038  0.0229  23  ILE   B CG1 
4274 C CG2 . ILE   B 23  ? 0.1686 0.1575 0.2019 -0.0174 -0.0022 0.0085  23  ILE   B CG2 
4275 C CD1 . ILE   B 23  ? 0.1669 0.1598 0.2189 -0.0095 0.0059  0.0219  23  ILE   B CD1 
4287 N N   . VAL   B 24  ? 0.1574 0.1325 0.1887 -0.0046 -0.0048 0.0036  24  VAL   B N   
4288 C CA  . VAL   B 24  ? 0.1493 0.1361 0.2072 -0.0041 -0.0119 -0.0032 24  VAL   B CA  
4289 C C   . VAL   B 24  ? 0.1440 0.1382 0.2174 -0.0093 -0.0113 0.0057  24  VAL   B C   
4290 O O   . VAL   B 24  ? 0.1429 0.1490 0.2317 -0.0131 -0.0075 0.0186  24  VAL   B O   
4291 C CB  . VAL   B 24  ? 0.1580 0.1534 0.2174 0.0038  -0.0257 -0.0034 24  VAL   B CB  
4292 C CG1 . VAL   B 24  ? 0.1547 0.1532 0.2393 -0.0032 -0.0143 -0.0024 24  VAL   B CG1 
4293 C CG2 . VAL   B 24  ? 0.1681 0.1821 0.2218 0.0118  -0.0230 -0.0074 24  VAL   B CG2 
4303 N N   . GLU   B 25  ? 0.1652 0.1515 0.2309 -0.0091 -0.0059 0.0062  25  GLU   B N   
4304 C CA  . GLU   B 25  ? 0.1774 0.1736 0.2416 0.0014  0.0097  0.0086  25  GLU   B CA  
4305 C C   . GLU   B 25  ? 0.1749 0.1627 0.2131 -0.0043 0.0183  0.0134  25  GLU   B C   
4306 O O   . GLU   B 25  ? 0.1770 0.1837 0.2220 -0.0069 0.0298  0.0245  25  GLU   B O   
4307 C CB  . GLU   B 25  ? 0.2153 0.2204 0.3063 0.0341  0.0223  0.0041  25  GLU   B CB  
4308 C CG  . GLU   B 25  ? 0.2586 0.2936 0.4100 0.0439  0.0200  -0.0018 25  GLU   B CG  
4309 C CD  . GLU   B 25  ? 0.3146 0.3571 0.5019 0.0396  0.0155  -0.0072 25  GLU   B CD  
4310 O OE1 . GLU   B 25  ? 0.3185 0.3804 0.5331 0.0423  0.0189  -0.0079 25  GLU   B OE1 
4311 O OE2 . GLU   B 25  ? 0.3197 0.3810 0.5425 0.0387  0.0135  -0.0114 25  GLU   B OE2 
4318 N N   . GLU   B 26  ? 0.1741 0.1590 0.1842 -0.0186 0.0114  0.0158  26  GLU   B N   
4319 C CA  . GLU   B 26  ? 0.1713 0.1689 0.1917 -0.0312 -0.0021 0.0138  26  GLU   B CA  
4320 C C   . GLU   B 26  ? 0.1593 0.1632 0.1888 -0.0213 0.0077  0.0217  26  GLU   B C   
4321 O O   . GLU   B 26  ? 0.1789 0.1832 0.1968 -0.0194 0.0052  0.0316  26  GLU   B O   
4322 C CB  . GLU   B 26  ? 0.2032 0.1915 0.2123 -0.0430 -0.0014 0.0129  26  GLU   B CB  
4323 C CG  . GLU   B 26  ? 0.2454 0.2208 0.2523 -0.0510 0.0111  -0.0075 26  GLU   B CG  
4324 C CD  . GLU   B 26  ? 0.2751 0.2419 0.2642 -0.0695 0.0252  -0.0353 26  GLU   B CD  
4325 O OE1 . GLU   B 26  ? 0.2989 0.2236 0.2592 -0.0825 0.0547  -0.0335 26  GLU   B OE1 
4326 O OE2 . GLU   B 26  ? 0.2735 0.2869 0.3062 -0.0590 0.0263  -0.0235 26  GLU   B OE2 
4333 N N   . ALA   B 27  ? 0.1402 0.1445 0.1968 -0.0199 0.0094  0.0189  27  ALA   B N   
4334 C CA  . ALA   B 27  ? 0.1473 0.1418 0.2072 -0.0093 0.0058  0.0304  27  ALA   B CA  
4335 C C   . ALA   B 27  ? 0.1479 0.1536 0.2406 -0.0048 0.0208  0.0447  27  ALA   B C   
4336 O O   . ALA   B 27  ? 0.1608 0.1667 0.2484 0.0028  0.0171  0.0510  27  ALA   B O   
4337 C CB  . ALA   B 27  ? 0.1654 0.1336 0.2082 -0.0155 0.0061  0.0222  27  ALA   B CB  
4343 N N   . LYS   B 28  ? 0.1437 0.1731 0.2793 -0.0136 0.0237  0.0637  28  LYS   B N   
4344 C CA  . LYS   B 28  ? 0.1660 0.2177 0.2994 -0.0035 0.0513  0.0895  28  LYS   B CA  
4345 C C   . LYS   B 28  ? 0.2021 0.2414 0.2847 0.0073  0.0651  0.0847  28  LYS   B C   
4346 O O   . LYS   B 28  ? 0.2213 0.2428 0.3001 -0.0024 0.0639  0.0907  28  LYS   B O   
4347 C CB  . LYS   B 28  ? 0.1885 0.2563 0.3365 0.0084  0.0755  0.1119  28  LYS   B CB  
4348 C CG  . LYS   B 28  ? 0.2168 0.2993 0.3769 0.0203  0.0796  0.1254  28  LYS   B CG  
4349 C CD  . LYS   B 28  ? 0.2586 0.3501 0.4278 0.0306  0.0911  0.1249  28  LYS   B CD  
4350 C CE  . LYS   B 28  ? 0.2890 0.3836 0.4677 0.0416  0.0935  0.1278  28  LYS   B CE  
4351 N NZ  . LYS   B 28  ? 0.3098 0.3967 0.4914 0.0496  0.0887  0.1336  28  LYS   B NZ  
4365 N N   A LYS   B 29  ? 0.2204 0.2597 0.2841 0.0164  0.0593  0.0706  29  LYS   B N   
4366 N N   B LYS   B 29  ? 0.2181 0.2584 0.2819 0.0230  0.0616  0.0705  29  LYS   B N   
4367 C CA  A LYS   B 29  ? 0.2490 0.2807 0.2984 0.0160  0.0505  0.0586  29  LYS   B CA  
4368 C CA  B LYS   B 29  ? 0.2512 0.2804 0.2981 0.0226  0.0548  0.0589  29  LYS   B CA  
4369 C C   A LYS   B 29  ? 0.2456 0.2755 0.2608 0.0139  0.0480  0.0642  29  LYS   B C   
4370 C C   B LYS   B 29  ? 0.2493 0.2769 0.2584 0.0186  0.0510  0.0651  29  LYS   B C   
4371 O O   A LYS   B 29  ? 0.2577 0.2863 0.2605 0.0152  0.0456  0.0642  29  LYS   B O   
4372 O O   B LYS   B 29  ? 0.2658 0.2918 0.2603 0.0204  0.0489  0.0656  29  LYS   B O   
4373 C CB  A LYS   B 29  ? 0.2837 0.3094 0.3624 0.0140  0.0389  0.0410  29  LYS   B CB  
4374 C CB  B LYS   B 29  ? 0.2915 0.3113 0.3698 0.0195  0.0430  0.0416  29  LYS   B CB  
4375 C CG  A LYS   B 29  ? 0.3124 0.3334 0.4257 0.0101  0.0341  0.0293  29  LYS   B CG  
4376 C CG  B LYS   B 29  ? 0.3244 0.3371 0.4406 0.0135  0.0399  0.0316  29  LYS   B CG  
4377 C CD  A LYS   B 29  ? 0.3349 0.3504 0.4768 0.0059  0.0332  0.0200  29  LYS   B CD  
4378 C CD  B LYS   B 29  ? 0.3496 0.3548 0.4982 0.0075  0.0402  0.0236  29  LYS   B CD  
4379 C CE  A LYS   B 29  ? 0.3507 0.3608 0.5134 0.0033  0.0331  0.0137  29  LYS   B CE  
4380 C CE  B LYS   B 29  ? 0.3671 0.3655 0.5394 0.0036  0.0421  0.0186  29  LYS   B CE  
4381 N NZ  A LYS   B 29  ? 0.3595 0.3665 0.5347 0.0025  0.0332  0.0097  29  LYS   B NZ  
4382 N NZ  B LYS   B 29  ? 0.3760 0.3722 0.5631 0.0032  0.0430  0.0150  29  LYS   B NZ  
4409 N N   . VAL   B 30  ? 0.2272 0.2584 0.2424 0.0053  0.0452  0.0669  30  VAL   B N   
4410 C CA  . VAL   B 30  ? 0.2085 0.2406 0.2621 -0.0053 0.0101  0.0699  30  VAL   B CA  
4411 C C   . VAL   B 30  ? 0.1806 0.2293 0.2529 -0.0073 0.0114  0.0796  30  VAL   B C   
4412 O O   . VAL   B 30  ? 0.1903 0.2486 0.2531 0.0013  0.0173  0.0893  30  VAL   B O   
4413 C CB  . VAL   B 30  ? 0.2207 0.2319 0.2952 -0.0191 -0.0214 0.0694  30  VAL   B CB  
4414 C CG1 . VAL   B 30  ? 0.2216 0.2422 0.3003 -0.0231 -0.0194 0.0609  30  VAL   B CG1 
4415 C CG2 . VAL   B 30  ? 0.2309 0.2302 0.3108 -0.0260 -0.0359 0.0583  30  VAL   B CG2 
4426 N N   . LYS   B 31  ? 0.1678 0.1943 0.2761 -0.0243 0.0066  0.0826  31  LYS   B N   
4427 C CA  . LYS   B 31  ? 0.1609 0.1909 0.2996 -0.0367 -0.0072 0.0837  31  LYS   B CA  
4428 C C   . LYS   B 31  ? 0.1509 0.1588 0.2671 -0.0316 -0.0235 0.0680  31  LYS   B C   
4429 O O   . LYS   B 31  ? 0.1586 0.1748 0.2805 -0.0248 -0.0234 0.0830  31  LYS   B O   
4430 C CB  . LYS   B 31  ? 0.1823 0.2375 0.3388 -0.0332 0.0070  0.0969  31  LYS   B CB  
4431 C CG  . LYS   B 31  ? 0.2137 0.2837 0.3770 -0.0416 0.0218  0.0988  31  LYS   B CG  
4432 C CD  . LYS   B 31  ? 0.2506 0.3260 0.4184 -0.0387 0.0166  0.0915  31  LYS   B CD  
4433 C CE  . LYS   B 31  ? 0.2768 0.3569 0.4599 -0.0381 0.0083  0.0820  31  LYS   B CE  
4434 N NZ  . LYS   B 31  ? 0.2931 0.3746 0.4862 -0.0321 -0.0034 0.0689  31  LYS   B NZ  
4448 N N   . PRO   B 32  ? 0.1610 0.1354 0.2133 -0.0279 -0.0389 0.0385  32  PRO   B N   
4449 C CA  . PRO   B 32  ? 0.1613 0.1331 0.1815 -0.0278 -0.0320 0.0266  32  PRO   B CA  
4450 C C   . PRO   B 32  ? 0.1692 0.1254 0.1825 -0.0304 -0.0458 0.0335  32  PRO   B C   
4451 O O   . PRO   B 32  ? 0.1816 0.1262 0.2168 -0.0308 -0.0681 0.0318  32  PRO   B O   
4452 C CB  . PRO   B 32  ? 0.1789 0.1265 0.1880 -0.0297 -0.0221 0.0150  32  PRO   B CB  
4453 C CG  . PRO   B 32  ? 0.1962 0.1233 0.1870 -0.0203 -0.0422 0.0208  32  PRO   B CG  
4454 C CD  . PRO   B 32  ? 0.1847 0.1296 0.2005 -0.0168 -0.0510 0.0215  32  PRO   B CD  
4462 N N   . THR   B 33  ? 0.1749 0.1184 0.1664 -0.0271 -0.0471 0.0220  33  THR   B N   
4463 C CA  . THR   B 33  ? 0.1861 0.1264 0.1581 -0.0327 -0.0453 0.0238  33  THR   B CA  
4464 C C   . THR   B 33  ? 0.1908 0.1179 0.1571 -0.0284 -0.0423 0.0176  33  THR   B C   
4465 O O   . THR   B 33  ? 0.2118 0.1182 0.1613 -0.0392 -0.0513 0.0151  33  THR   B O   
4466 C CB  . THR   B 33  ? 0.1937 0.1362 0.1663 -0.0182 -0.0490 0.0271  33  THR   B CB  
4467 O OG1 . THR   B 33  ? 0.1856 0.1450 0.1729 -0.0154 -0.0454 0.0364  33  THR   B OG1 
4468 C CG2 . THR   B 33  ? 0.2153 0.1447 0.1859 -0.0027 -0.0474 0.0220  33  THR   B CG2 
4476 N N   . VAL   B 34  ? 0.1709 0.1136 0.1495 -0.0269 -0.0338 0.0093  34  VAL   B N   
4477 C CA  . VAL   B 34  ? 0.1608 0.1169 0.1362 -0.0168 -0.0348 0.0114  34  VAL   B CA  
4478 C C   . VAL   B 34  ? 0.1415 0.1106 0.1310 -0.0258 -0.0189 0.0109  34  VAL   B C   
4479 O O   . VAL   B 34  ? 0.1617 0.1101 0.1388 -0.0228 -0.0346 0.0082  34  VAL   B O   
4480 C CB  . VAL   B 34  ? 0.1638 0.1245 0.1685 -0.0060 -0.0316 0.0081  34  VAL   B CB  
4481 C CG1 . VAL   B 34  ? 0.1565 0.1431 0.1785 -0.0076 -0.0152 -0.0058 34  VAL   B CG1 
4482 C CG2 . VAL   B 34  ? 0.1709 0.1338 0.1816 -0.0079 -0.0257 0.0004  34  VAL   B CG2 
4492 N N   . VAL   B 35  ? 0.1368 0.1065 0.1274 -0.0222 -0.0105 0.0074  35  VAL   B N   
4493 C CA  . VAL   B 35  ? 0.1325 0.1053 0.1374 -0.0194 -0.0118 0.0039  35  VAL   B CA  
4494 C C   . VAL   B 35  ? 0.1193 0.1025 0.1333 -0.0142 -0.0146 0.0079  35  VAL   B C   
4495 O O   . VAL   B 35  ? 0.1288 0.1072 0.1282 -0.0217 -0.0054 -0.0038 35  VAL   B O   
4496 C CB  . VAL   B 35  ? 0.1317 0.1236 0.1455 -0.0147 0.0001  0.0072  35  VAL   B CB  
4497 C CG1 . VAL   B 35  ? 0.1230 0.1362 0.1634 -0.0232 -0.0049 0.0035  35  VAL   B CG1 
4498 C CG2 . VAL   B 35  ? 0.1328 0.1271 0.1654 -0.0047 0.0039  0.0019  35  VAL   B CG2 
4508 N N   . VAL   B 36  ? 0.1207 0.1036 0.1263 -0.0169 -0.0206 0.0092  36  VAL   B N   
4509 C CA  . VAL   B 36  ? 0.1182 0.1013 0.1271 -0.0089 -0.0109 0.0044  36  VAL   B CA  
4510 C C   . VAL   B 36  ? 0.1130 0.1041 0.1167 -0.0124 -0.0035 -0.0003 36  VAL   B C   
4511 O O   . VAL   B 36  ? 0.1241 0.1152 0.1416 -0.0107 -0.0050 -0.0061 36  VAL   B O   
4512 C CB  . VAL   B 36  ? 0.1178 0.1040 0.1333 -0.0124 -0.0013 -0.0020 36  VAL   B CB  
4513 C CG1 . VAL   B 36  ? 0.1225 0.1176 0.1478 -0.0194 -0.0070 0.0019  36  VAL   B CG1 
4514 C CG2 . VAL   B 36  ? 0.1242 0.1124 0.1482 -0.0090 -0.0117 0.0111  36  VAL   B CG2 
4524 N N   . ASN   B 37  ? 0.1189 0.1090 0.1179 -0.0009 -0.0085 0.0040  37  ASN   B N   
4525 C CA  . ASN   B 37  ? 0.1191 0.1101 0.1333 -0.0014 -0.0127 0.0079  37  ASN   B CA  
4526 C C   . ASN   B 37  ? 0.1144 0.1107 0.1262 0.0018  -0.0115 0.0002  37  ASN   B C   
4527 O O   . ASN   B 37  ? 0.1256 0.1205 0.1297 0.0039  -0.0007 0.0028  37  ASN   B O   
4528 C CB  . ASN   B 37  ? 0.1187 0.1147 0.1350 -0.0004 -0.0140 0.0040  37  ASN   B CB  
4529 C CG  . ASN   B 37  ? 0.1177 0.1144 0.1461 -0.0023 -0.0210 0.0026  37  ASN   B CG  
4530 O OD1 . ASN   B 37  ? 0.1276 0.1210 0.1574 0.0061  -0.0159 0.0042  37  ASN   B OD1 
4531 N ND2 . ASN   B 37  ? 0.1246 0.1164 0.1573 -0.0006 -0.0238 0.0147  37  ASN   B ND2 
4538 N N   . ALA   B 38  ? 0.1265 0.1096 0.1331 0.0020  -0.0065 0.0026  38  ALA   B N   
4539 C CA  . ALA   B 38  ? 0.1362 0.1122 0.1342 -0.0032 0.0034  0.0105  38  ALA   B CA  
4540 C C   . ALA   B 38  ? 0.1244 0.1130 0.1359 -0.0004 0.0040  0.0072  38  ALA   B C   
4541 O O   . ALA   B 38  ? 0.1376 0.1238 0.1544 0.0066  -0.0018 0.0127  38  ALA   B O   
4542 C CB  . ALA   B 38  ? 0.1590 0.1197 0.1480 -0.0078 0.0084  0.0035  38  ALA   B CB  
4548 N N   . ALA   B 39  ? 0.1292 0.1150 0.1228 0.0085  -0.0045 0.0024  39  ALA   B N   
4549 C CA  . ALA   B 39  ? 0.1390 0.1229 0.1267 0.0040  -0.0076 0.0086  39  ALA   B CA  
4550 C C   . ALA   B 39  ? 0.1397 0.1259 0.1177 0.0015  -0.0091 -0.0003 39  ALA   B C   
4551 O O   . ALA   B 39  ? 0.1406 0.1303 0.1455 -0.0019 -0.0065 0.0092  39  ALA   B O   
4552 C CB  . ALA   B 39  ? 0.1457 0.1225 0.1493 -0.0073 0.0014  -0.0001 39  ALA   B CB  
4558 N N   . ASN   B 40  ? 0.1430 0.1498 0.1270 -0.0124 0.0002  -0.0018 40  ASN   B N   
4559 C CA  . ASN   B 40  ? 0.1484 0.1582 0.1419 -0.0063 -0.0081 -0.0073 40  ASN   B CA  
4560 C C   . ASN   B 40  ? 0.1498 0.1601 0.1244 0.0012  -0.0130 -0.0027 40  ASN   B C   
4561 O O   . ASN   B 40  ? 0.1487 0.1506 0.1371 0.0011  -0.0207 -0.0026 40  ASN   B O   
4562 C CB  . ASN   B 40  ? 0.1627 0.1613 0.1597 0.0062  -0.0159 0.0107  40  ASN   B CB  
4563 C CG  . ASN   B 40  ? 0.1699 0.1600 0.1856 0.0067  -0.0257 0.0118  40  ASN   B CG  
4564 O OD1 . ASN   B 40  ? 0.1668 0.1535 0.2504 0.0034  -0.0363 0.0176  40  ASN   B OD1 
4565 N ND2 . ASN   B 40  ? 0.1716 0.1631 0.1874 0.0081  -0.0177 0.0074  40  ASN   B ND2 
4572 N N   . VAL   B 41  ? 0.1593 0.1647 0.1250 0.0054  -0.0009 0.0013  41  VAL   B N   
4573 C CA  . VAL   B 41  ? 0.1672 0.1767 0.1372 0.0079  -0.0042 -0.0143 41  VAL   B CA  
4574 C C   . VAL   B 41  ? 0.1613 0.1770 0.1346 0.0124  -0.0141 -0.0170 41  VAL   B C   
4575 O O   . VAL   B 41  ? 0.1639 0.1738 0.1455 0.0052  -0.0177 -0.0220 41  VAL   B O   
4576 C CB  . VAL   B 41  ? 0.1792 0.1965 0.1511 -0.0084 0.0137  -0.0317 41  VAL   B CB  
4577 C CG1 . VAL   B 41  ? 0.1750 0.2014 0.1550 -0.0146 0.0253  -0.0442 41  VAL   B CG1 
4578 C CG2 . VAL   B 41  ? 0.1916 0.2179 0.1658 -0.0169 0.0174  -0.0248 41  VAL   B CG2 
4588 N N   . TYR   B 42  ? 0.1642 0.1782 0.1452 0.0187  -0.0296 0.0010  42  TYR   B N   
4589 C CA  . TYR   B 42  ? 0.1740 0.1861 0.1636 0.0137  -0.0355 -0.0191 42  TYR   B CA  
4590 C C   . TYR   B 42  ? 0.1528 0.1554 0.1600 0.0178  -0.0322 -0.0213 42  TYR   B C   
4591 O O   . TYR   B 42  ? 0.1571 0.1649 0.1894 0.0094  -0.0370 -0.0271 42  TYR   B O   
4592 C CB  . TYR   B 42  ? 0.2031 0.2264 0.1815 0.0087  -0.0401 -0.0047 42  TYR   B CB  
4593 C CG  . TYR   B 42  ? 0.2097 0.2517 0.1787 0.0019  -0.0307 0.0114  42  TYR   B CG  
4594 C CD1 . TYR   B 42  ? 0.2059 0.2533 0.1552 -0.0020 -0.0139 0.0037  42  TYR   B CD1 
4595 C CD2 . TYR   B 42  ? 0.2290 0.2714 0.2185 0.0021  -0.0158 0.0195  42  TYR   B CD2 
4596 C CE1 . TYR   B 42  ? 0.2197 0.2731 0.1733 0.0045  -0.0089 0.0151  42  TYR   B CE1 
4597 C CE2 . TYR   B 42  ? 0.2343 0.2818 0.2178 0.0063  0.0037  0.0373  42  TYR   B CE2 
4598 C CZ  . TYR   B 42  ? 0.2404 0.2858 0.2084 0.0194  0.0104  0.0309  42  TYR   B CZ  
4599 O OH  . TYR   B 42  ? 0.2717 0.3102 0.2558 0.0326  0.0212  0.0393  42  TYR   B OH  
4609 N N   . LEU   B 43  ? 0.1444 0.1442 0.1477 0.0087  -0.0208 -0.0161 43  LEU   B N   
4610 C CA  . LEU   B 43  ? 0.1452 0.1424 0.1544 0.0034  -0.0196 -0.0070 43  LEU   B CA  
4611 C C   . LEU   B 43  ? 0.1529 0.1456 0.1536 0.0021  -0.0204 -0.0058 43  LEU   B C   
4612 O O   . LEU   B 43  ? 0.1484 0.1452 0.1851 0.0027  -0.0270 0.0032  43  LEU   B O   
4613 C CB  . LEU   B 43  ? 0.1459 0.1316 0.1577 -0.0012 -0.0281 -0.0095 43  LEU   B CB  
4614 C CG  . LEU   B 43  ? 0.1538 0.1349 0.1651 0.0002  -0.0296 -0.0091 43  LEU   B CG  
4615 C CD1 . LEU   B 43  ? 0.1640 0.1330 0.1946 -0.0015 -0.0425 -0.0059 43  LEU   B CD1 
4616 C CD2 . LEU   B 43  ? 0.1514 0.1354 0.1652 -0.0051 -0.0268 -0.0089 43  LEU   B CD2 
4628 N N   . LYS   B 44  ? 0.1485 0.1447 0.1509 0.0069  -0.0208 -0.0076 44  LYS   B N   
4629 C CA  . LYS   B 44  ? 0.1607 0.1528 0.1580 0.0095  -0.0219 -0.0003 44  LYS   B CA  
4630 C C   . LYS   B 44  ? 0.1489 0.1481 0.1569 0.0111  -0.0188 -0.0024 44  LYS   B C   
4631 O O   . LYS   B 44  ? 0.1656 0.1422 0.1881 0.0033  -0.0125 -0.0011 44  LYS   B O   
4632 C CB  . LYS   B 44  ? 0.1884 0.1731 0.1714 0.0171  -0.0340 -0.0016 44  LYS   B CB  
4633 C CG  . LYS   B 44  ? 0.2298 0.2032 0.2149 0.0171  -0.0490 -0.0004 44  LYS   B CG  
4634 C CD  . LYS   B 44  ? 0.2683 0.2234 0.2789 0.0017  -0.0521 0.0009  44  LYS   B CD  
4635 C CE  . LYS   B 44  ? 0.2971 0.2437 0.3386 -0.0056 -0.0561 0.0086  44  LYS   B CE  
4636 N NZ  . LYS   B 44  ? 0.3069 0.2498 0.3715 -0.0036 -0.0615 0.0182  44  LYS   B NZ  
4650 N N   . HIS   B 45  ? 0.1471 0.1516 0.1484 0.0048  -0.0197 0.0021  45  HIS   B N   
4651 C CA  . HIS   B 45  ? 0.1561 0.1475 0.1574 0.0098  -0.0132 -0.0007 45  HIS   B CA  
4652 C C   . HIS   B 45  ? 0.1850 0.1658 0.1872 0.0145  -0.0318 -0.0092 45  HIS   B C   
4653 O O   . HIS   B 45  ? 0.1979 0.1947 0.2357 0.0480  0.0044  -0.0040 45  HIS   B O   
4654 C CB  . HIS   B 45  ? 0.1415 0.1541 0.1518 0.0008  -0.0108 0.0008  45  HIS   B CB  
4655 C CG  . HIS   B 45  ? 0.1422 0.1437 0.1489 -0.0039 -0.0109 0.0014  45  HIS   B CG  
4656 N ND1 . HIS   B 45  ? 0.1490 0.1415 0.1631 0.0023  -0.0236 -0.0070 45  HIS   B ND1 
4657 C CD2 . HIS   B 45  ? 0.1576 0.1430 0.1760 -0.0075 -0.0215 -0.0015 45  HIS   B CD2 
4658 C CE1 . HIS   B 45  ? 0.1577 0.1307 0.1508 -0.0038 -0.0282 -0.0123 45  HIS   B CE1 
4659 N NE2 . HIS   B 45  ? 0.1625 0.1385 0.1623 -0.0022 -0.0279 -0.0044 45  HIS   B NE2 
4667 N N   A GLY   B 46  ? 0.1948 0.1694 0.2064 0.0180  -0.0437 -0.0016 46  GLY   B N   
4668 N N   B GLY   B 46  ? 0.1961 0.1659 0.2051 0.0200  -0.0493 0.0042  46  GLY   B N   
4669 C CA  A GLY   B 46  ? 0.2063 0.1816 0.2372 0.0167  -0.0437 -0.0005 46  GLY   B CA  
4670 C CA  B GLY   B 46  ? 0.2103 0.1801 0.2368 0.0185  -0.0492 0.0070  46  GLY   B CA  
4671 C C   A GLY   B 46  ? 0.2117 0.1962 0.2758 0.0202  -0.0409 -0.0029 46  GLY   B C   
4672 C C   B GLY   B 46  ? 0.2161 0.1988 0.2800 0.0234  -0.0459 0.0060  46  GLY   B C   
4673 O O   A GLY   B 46  ? 0.2217 0.2088 0.3214 0.0221  -0.0306 -0.0137 46  GLY   B O   
4674 O O   B GLY   B 46  ? 0.2313 0.2197 0.3313 0.0225  -0.0347 0.0001  46  GLY   B O   
4681 N N   . GLY   B 47  ? 0.2106 0.2026 0.2684 0.0088  -0.0342 -0.0038 47  GLY   B N   
4682 C CA  . GLY   B 47  ? 0.1928 0.1725 0.2277 0.0028  -0.0231 0.0021  47  GLY   B CA  
4683 C C   . GLY   B 47  ? 0.1702 0.1456 0.1931 0.0052  -0.0081 0.0076  47  GLY   B C   
4684 O O   . GLY   B 47  ? 0.1802 0.1368 0.1858 0.0065  -0.0128 0.0092  47  GLY   B O   
4689 N N   . GLY   B 48  ? 0.1463 0.1352 0.1817 0.0051  -0.0168 0.0172  48  GLY   B N   
4690 C CA  . GLY   B 48  ? 0.1479 0.1320 0.1858 -0.0002 -0.0032 0.0124  48  GLY   B CA  
4691 C C   . GLY   B 48  ? 0.1413 0.1257 0.1754 0.0019  0.0042  0.0019  48  GLY   B C   
4692 O O   . GLY   B 48  ? 0.1425 0.1302 0.1827 0.0089  -0.0088 0.0020  48  GLY   B O   
4696 N N   . VAL   B 49  ? 0.1405 0.1307 0.1654 0.0099  -0.0005 0.0069  49  VAL   B N   
4697 C CA  . VAL   B 49  ? 0.1427 0.1364 0.1559 0.0102  -0.0170 -0.0002 49  VAL   B CA  
4698 C C   . VAL   B 49  ? 0.1352 0.1336 0.1505 0.0151  -0.0093 0.0075  49  VAL   B C   
4699 O O   . VAL   B 49  ? 0.1445 0.1404 0.1546 0.0088  -0.0100 0.0083  49  VAL   B O   
4700 C CB  . VAL   B 49  ? 0.1457 0.1566 0.1719 0.0035  -0.0231 0.0009  49  VAL   B CB  
4701 C CG1 . VAL   B 49  ? 0.1442 0.1696 0.1696 0.0070  -0.0238 0.0071  49  VAL   B CG1 
4702 C CG2 . VAL   B 49  ? 0.1657 0.1757 0.2041 -0.0041 -0.0387 0.0075  49  VAL   B CG2 
4712 N N   . ALA   B 50  ? 0.1314 0.1247 0.1490 0.0047  -0.0053 0.0081  50  ALA   B N   
4713 C CA  . ALA   B 50  ? 0.1299 0.1174 0.1515 0.0076  -0.0074 0.0084  50  ALA   B CA  
4714 C C   . ALA   B 50  ? 0.1392 0.1223 0.1470 0.0111  -0.0091 0.0043  50  ALA   B C   
4715 O O   . ALA   B 50  ? 0.1332 0.1271 0.1594 0.0066  -0.0051 0.0027  50  ALA   B O   
4716 C CB  . ALA   B 50  ? 0.1326 0.1256 0.1625 -0.0001 -0.0020 0.0120  50  ALA   B CB  
4722 N N   . GLY   B 51  ? 0.1355 0.1383 0.1626 0.0161  -0.0160 0.0069  51  GLY   B N   
4723 C CA  . GLY   B 51  ? 0.1382 0.1428 0.1852 0.0185  -0.0168 0.0106  51  GLY   B CA  
4724 C C   . GLY   B 51  ? 0.1364 0.1394 0.1856 0.0213  -0.0124 0.0071  51  GLY   B C   
4725 O O   . GLY   B 51  ? 0.1401 0.1532 0.2058 0.0117  -0.0109 0.0001  51  GLY   B O   
4729 N N   . ALA   B 52  ? 0.1365 0.1314 0.1733 0.0193  -0.0073 0.0146  52  ALA   B N   
4730 C CA  . ALA   B 52  ? 0.1383 0.1381 0.1751 0.0211  -0.0033 0.0043  52  ALA   B CA  
4731 C C   . ALA   B 52  ? 0.1304 0.1403 0.1707 0.0139  -0.0042 0.0062  52  ALA   B C   
4732 O O   . ALA   B 52  ? 0.1345 0.1424 0.1874 0.0117  0.0038  0.0084  52  ALA   B O   
4733 C CB  . ALA   B 52  ? 0.1608 0.1452 0.1895 0.0037  0.0026  0.0020  52  ALA   B CB  
4739 N N   . LEU   B 53  ? 0.1251 0.1366 0.1592 0.0131  0.0003  0.0038  53  LEU   B N   
4740 C CA  . LEU   B 53  ? 0.1277 0.1411 0.1611 0.0135  -0.0045 0.0104  53  LEU   B CA  
4741 C C   . LEU   B 53  ? 0.1326 0.1347 0.1524 0.0131  0.0058  0.0145  53  LEU   B C   
4742 O O   . LEU   B 53  ? 0.1401 0.1476 0.1672 0.0029  0.0050  0.0158  53  LEU   B O   
4743 C CB  . LEU   B 53  ? 0.1295 0.1449 0.1709 0.0136  -0.0003 0.0175  53  LEU   B CB  
4744 C CG  . LEU   B 53  ? 0.1257 0.1642 0.1733 0.0028  -0.0034 0.0243  53  LEU   B CG  
4745 C CD1 . LEU   B 53  ? 0.1292 0.1894 0.1932 0.0114  -0.0008 0.0107  53  LEU   B CD1 
4746 C CD2 . LEU   B 53  ? 0.1365 0.1893 0.1965 -0.0095 -0.0090 -0.0052 53  LEU   B CD2 
4758 N N   . ASN   B 54  ? 0.1302 0.1297 0.1588 0.0028  -0.0027 0.0167  54  ASN   B N   
4759 C CA  . ASN   B 54  ? 0.1367 0.1430 0.1716 0.0001  -0.0010 0.0056  54  ASN   B CA  
4760 C C   . ASN   B 54  ? 0.1303 0.1417 0.1834 0.0026  -0.0027 0.0139  54  ASN   B C   
4761 O O   . ASN   B 54  ? 0.1300 0.1516 0.1911 -0.0019 0.0022  0.0027  54  ASN   B O   
4762 C CB  . ASN   B 54  ? 0.1421 0.1517 0.1804 -0.0000 0.0057  -0.0001 54  ASN   B CB  
4763 C CG  . ASN   B 54  ? 0.1376 0.1606 0.1859 0.0007  -0.0066 0.0009  54  ASN   B CG  
4764 O OD1 . ASN   B 54  ? 0.1325 0.1632 0.1976 -0.0058 -0.0066 -0.0063 54  ASN   B OD1 
4765 N ND2 . ASN   B 54  ? 0.1483 0.1837 0.2080 0.0023  -0.0313 0.0162  54  ASN   B ND2 
4772 N N   . LYS   B 55  ? 0.1300 0.1498 0.2008 0.0138  -0.0012 0.0114  55  LYS   B N   
4773 C CA  . LYS   B 55  ? 0.1398 0.1709 0.2179 0.0197  -0.0018 0.0103  55  LYS   B CA  
4774 C C   . LYS   B 55  ? 0.1306 0.1640 0.2125 0.0146  0.0005  0.0099  55  LYS   B C   
4775 O O   . LYS   B 55  ? 0.1287 0.1766 0.2207 0.0107  0.0045  -0.0005 55  LYS   B O   
4776 C CB  . LYS   B 55  ? 0.1545 0.1785 0.2362 0.0300  0.0096  0.0248  55  LYS   B CB  
4777 C CG  . LYS   B 55  ? 0.1970 0.2073 0.3149 0.0350  0.0278  0.0381  55  LYS   B CG  
4778 C CD  . LYS   B 55  ? 0.2336 0.2292 0.3826 0.0445  0.0402  0.0474  55  LYS   B CD  
4779 C CE  . LYS   B 55  ? 0.2612 0.2533 0.4379 0.0470  0.0490  0.0485  55  LYS   B CE  
4780 N NZ  . LYS   B 55  ? 0.2693 0.2683 0.4678 0.0452  0.0394  0.0546  55  LYS   B NZ  
4794 N N   . ALA   B 56  ? 0.1279 0.1656 0.1976 0.0092  -0.0027 0.0037  56  ALA   B N   
4795 C CA  . ALA   B 56  ? 0.1429 0.1799 0.2022 0.0053  -0.0007 0.0046  56  ALA   B CA  
4796 C C   . ALA   B 56  ? 0.1441 0.1765 0.1909 0.0059  0.0170  0.0134  56  ALA   B C   
4797 O O   . ALA   B 56  ? 0.1615 0.1856 0.2078 0.0083  0.0327  0.0139  56  ALA   B O   
4798 C CB  . ALA   B 56  ? 0.1572 0.2036 0.2003 -0.0048 -0.0049 -0.0036 56  ALA   B CB  
4804 N N   . THR   B 57  ? 0.1411 0.1681 0.2009 0.0080  0.0138  0.0186  57  THR   B N   
4805 C CA  . THR   B 57  ? 0.1410 0.1720 0.1954 0.0062  0.0199  0.0226  57  THR   B CA  
4806 C C   . THR   B 57  ? 0.1418 0.1846 0.2196 0.0003  0.0202  0.0211  57  THR   B C   
4807 O O   . THR   B 57  ? 0.1534 0.1767 0.2425 -0.0165 0.0145  0.0183  57  THR   B O   
4808 C CB  . THR   B 57  ? 0.1486 0.1583 0.1925 0.0029  0.0144  0.0199  57  THR   B CB  
4809 O OG1 . THR   B 57  ? 0.1481 0.1481 0.1984 0.0042  0.0113  0.0101  57  THR   B OG1 
4810 C CG2 . THR   B 57  ? 0.1455 0.1595 0.1883 -0.0017 0.0187  0.0177  57  THR   B CG2 
4818 N N   . ASN   B 58  ? 0.1242 0.2100 0.2485 -0.0123 0.0069  0.0015  58  ASN   B N   
4819 C CA  . ASN   B 58  ? 0.1617 0.2626 0.2956 -0.0238 0.0269  0.0078  58  ASN   B CA  
4820 C C   . ASN   B 58  ? 0.1299 0.2249 0.2490 -0.0135 -0.0004 0.0063  58  ASN   B C   
4821 O O   . ASN   B 58  ? 0.1382 0.2237 0.2503 -0.0138 0.0042  -0.0010 58  ASN   B O   
4822 C CB  . ASN   B 58  ? 0.2885 0.3624 0.4463 -0.0301 0.0549  0.0164  58  ASN   B CB  
4823 C CG  . ASN   B 58  ? 0.4142 0.4505 0.6017 -0.0256 0.0645  0.0293  58  ASN   B CG  
4824 O OD1 . ASN   B 58  ? 0.4447 0.4778 0.6564 -0.0234 0.0666  0.0347  58  ASN   B OD1 
4825 N ND2 . ASN   B 58  ? 0.5454 0.5454 0.6569 -0.0250 0.0679  0.0334  58  ASN   B ND2 
4832 N N   . ASN   B 59  ? 0.1257 0.2022 0.2316 -0.0094 -0.0031 0.0172  59  ASN   B N   
4833 C CA  . ASN   B 59  ? 0.1333 0.1980 0.2267 -0.0062 -0.0101 0.0197  59  ASN   B CA  
4834 C C   . ASN   B 59  ? 0.1279 0.1846 0.2108 -0.0090 -0.0148 0.0033  59  ASN   B C   
4835 O O   . ASN   B 59  ? 0.1294 0.1850 0.2125 -0.0108 -0.0142 -0.0037 59  ASN   B O   
4836 C CB  . ASN   B 59  ? 0.1417 0.2150 0.2399 -0.0015 -0.0248 0.0180  59  ASN   B CB  
4837 C CG  . ASN   B 59  ? 0.1534 0.2312 0.2529 0.0018  -0.0354 0.0208  59  ASN   B CG  
4838 O OD1 . ASN   B 59  ? 0.1576 0.2380 0.2530 0.0042  -0.0244 0.0318  59  ASN   B OD1 
4839 N ND2 . ASN   B 59  ? 0.1662 0.2446 0.2618 -0.0078 -0.0414 0.0147  59  ASN   B ND2 
4846 N N   . ALA   B 60  ? 0.1365 0.1690 0.2093 -0.0072 -0.0030 0.0085  60  ALA   B N   
4847 C CA  . ALA   B 60  ? 0.1430 0.1623 0.2111 -0.0177 -0.0009 0.0102  60  ALA   B CA  
4848 C C   . ALA   B 60  ? 0.1384 0.1465 0.1907 -0.0108 -0.0046 0.0160  60  ALA   B C   
4849 O O   . ALA   B 60  ? 0.1448 0.1562 0.1929 -0.0159 -0.0010 0.0015  60  ALA   B O   
4850 C CB  . ALA   B 60  ? 0.1542 0.1643 0.2313 -0.0177 0.0057  0.0180  60  ALA   B CB  
4856 N N   . MET   B 61  ? 0.1312 0.1456 0.1918 -0.0080 -0.0062 0.0118  61  MET   B N   
4857 C CA  . MET   B 61  ? 0.1280 0.1398 0.1912 -0.0098 -0.0130 0.0090  61  MET   B CA  
4858 C C   . MET   B 61  ? 0.1340 0.1348 0.1942 -0.0114 -0.0117 0.0063  61  MET   B C   
4859 O O   . MET   B 61  ? 0.1382 0.1391 0.1880 -0.0053 -0.0076 -0.0122 61  MET   B O   
4860 C CB  . MET   B 61  ? 0.1277 0.1455 0.1769 -0.0016 -0.0089 0.0013  61  MET   B CB  
4861 C CG  . MET   B 61  ? 0.1299 0.1497 0.1777 -0.0002 -0.0134 0.0068  61  MET   B CG  
4862 S SD  . MET   B 61  ? 0.1330 0.1448 0.1970 -0.0038 -0.0070 -0.0070 61  MET   B SD  
4863 C CE  . MET   B 61  ? 0.1362 0.1683 0.2300 0.0003  -0.0018 -0.0170 61  MET   B CE  
4873 N N   . GLN   B 62  ? 0.1323 0.1422 0.1792 -0.0075 -0.0129 0.0083  62  GLN   B N   
4874 C CA  . GLN   B 62  ? 0.1356 0.1502 0.1920 -0.0034 -0.0186 -0.0028 62  GLN   B CA  
4875 C C   . GLN   B 62  ? 0.1415 0.1572 0.1877 -0.0064 -0.0268 -0.0106 62  GLN   B C   
4876 O O   . GLN   B 62  ? 0.1492 0.1534 0.1881 -0.0081 -0.0301 -0.0193 62  GLN   B O   
4877 C CB  . GLN   B 62  ? 0.1342 0.1544 0.1933 -0.0063 -0.0221 0.0045  62  GLN   B CB  
4878 C CG  . GLN   B 62  ? 0.1397 0.1622 0.1905 0.0003  -0.0316 -0.0020 62  GLN   B CG  
4879 C CD  . GLN   B 62  ? 0.1418 0.1564 0.1802 0.0022  -0.0333 0.0036  62  GLN   B CD  
4880 O OE1 . GLN   B 62  ? 0.1450 0.1532 0.1902 0.0009  -0.0341 -0.0055 62  GLN   B OE1 
4881 N NE2 . GLN   B 62  ? 0.1412 0.1535 0.2004 -0.0051 -0.0327 -0.0067 62  GLN   B NE2 
4890 N N   . VAL   B 63  ? 0.1423 0.1544 0.2019 -0.0147 -0.0230 -0.0134 63  VAL   B N   
4891 C CA  . VAL   B 63  ? 0.1524 0.1599 0.2166 -0.0187 -0.0269 -0.0108 63  VAL   B CA  
4892 C C   . VAL   B 63  ? 0.1542 0.1495 0.2076 -0.0226 -0.0291 -0.0118 63  VAL   B C   
4893 O O   . VAL   B 63  ? 0.1622 0.1526 0.2248 -0.0146 -0.0386 -0.0147 63  VAL   B O   
4894 C CB  . VAL   B 63  ? 0.1558 0.1774 0.2632 -0.0234 -0.0227 -0.0116 63  VAL   B CB  
4895 C CG1 . VAL   B 63  ? 0.1672 0.1851 0.2750 -0.0350 -0.0188 -0.0102 63  VAL   B CG1 
4896 C CG2 . VAL   B 63  ? 0.1523 0.1941 0.2777 -0.0126 -0.0239 -0.0145 63  VAL   B CG2 
4906 N N   . GLU   B 64  ? 0.1527 0.1388 0.1996 -0.0138 -0.0258 -0.0087 64  GLU   B N   
4907 C CA  . GLU   B 64  ? 0.1494 0.1354 0.1903 -0.0140 -0.0312 -0.0090 64  GLU   B CA  
4908 C C   . GLU   B 64  ? 0.1465 0.1386 0.1915 -0.0093 -0.0253 -0.0153 64  GLU   B C   
4909 O O   . GLU   B 64  ? 0.1617 0.1484 0.1831 -0.0157 -0.0275 -0.0153 64  GLU   B O   
4910 C CB  . GLU   B 64  ? 0.1480 0.1463 0.1933 -0.0178 -0.0265 -0.0000 64  GLU   B CB  
4911 C CG  . GLU   B 64  ? 0.1582 0.1523 0.1958 -0.0309 -0.0184 -0.0141 64  GLU   B CG  
4912 C CD  . GLU   B 64  ? 0.1580 0.1640 0.2165 -0.0388 -0.0245 -0.0189 64  GLU   B CD  
4913 O OE1 . GLU   B 64  ? 0.1654 0.1839 0.2340 -0.0372 -0.0262 -0.0330 64  GLU   B OE1 
4914 O OE2 . GLU   B 64  ? 0.1758 0.1759 0.2181 -0.0337 -0.0458 -0.0164 64  GLU   B OE2 
4921 N N   . SER   B 65  ? 0.1463 0.1311 0.1910 -0.0138 -0.0140 -0.0155 65  SER   B N   
4922 C CA  . SER   B 65  ? 0.1430 0.1309 0.1895 -0.0055 -0.0172 -0.0198 65  SER   B CA  
4923 C C   . SER   B 65  ? 0.1446 0.1354 0.1860 -0.0071 -0.0274 -0.0176 65  SER   B C   
4924 O O   . SER   B 65  ? 0.1516 0.1472 0.1870 -0.0089 -0.0216 -0.0319 65  SER   B O   
4925 C CB  . SER   B 65  ? 0.1435 0.1423 0.1890 -0.0132 -0.0224 -0.0118 65  SER   B CB  
4926 O OG  . SER   B 65  ? 0.1504 0.1402 0.1851 -0.0084 -0.0205 -0.0261 65  SER   B OG  
4932 N N   . ASP   B 66  ? 0.1505 0.1437 0.1866 -0.0071 -0.0299 -0.0178 66  ASP   B N   
4933 C CA  . ASP   B 66  ? 0.1585 0.1520 0.1942 -0.0036 -0.0319 -0.0160 66  ASP   B CA  
4934 C C   . ASP   B 66  ? 0.1590 0.1573 0.1994 -0.0094 -0.0293 -0.0229 66  ASP   B C   
4935 O O   . ASP   B 66  ? 0.1644 0.1610 0.1975 0.0017  -0.0294 -0.0237 66  ASP   B O   
4936 C CB  . ASP   B 66  ? 0.1792 0.1646 0.2128 0.0076  -0.0463 -0.0140 66  ASP   B CB  
4937 C CG  . ASP   B 66  ? 0.2113 0.1814 0.2407 0.0189  -0.0560 -0.0065 66  ASP   B CG  
4938 O OD1 . ASP   B 66  ? 0.2334 0.1769 0.2457 0.0088  -0.0564 -0.0059 66  ASP   B OD1 
4939 O OD2 . ASP   B 66  ? 0.2264 0.2049 0.2958 0.0359  -0.0551 -0.0111 66  ASP   B OD2 
4944 N N   . ASP   B 67  ? 0.1569 0.1521 0.1909 -0.0187 -0.0220 -0.0218 67  ASP   B N   
4945 C CA  . ASP   B 67  ? 0.1734 0.1471 0.2053 -0.0199 -0.0262 -0.0115 67  ASP   B CA  
4946 C C   . ASP   B 67  ? 0.1716 0.1435 0.2036 -0.0054 -0.0237 -0.0243 67  ASP   B C   
4947 O O   . ASP   B 67  ? 0.1768 0.1487 0.2192 -0.0065 -0.0196 -0.0270 67  ASP   B O   
4948 C CB  . ASP   B 67  ? 0.1990 0.1547 0.2328 -0.0195 -0.0472 -0.0072 67  ASP   B CB  
4949 C CG  . ASP   B 67  ? 0.2358 0.1655 0.2555 -0.0114 -0.0686 -0.0109 67  ASP   B CG  
4950 O OD1 . ASP   B 67  ? 0.2573 0.1688 0.2628 -0.0153 -0.0761 -0.0064 67  ASP   B OD1 
4951 O OD2 . ASP   B 67  ? 0.2517 0.1758 0.2723 0.0007  -0.0800 -0.0026 67  ASP   B OD2 
4956 N N   . TYR   B 68  ? 0.1650 0.1528 0.1947 -0.0033 -0.0343 -0.0276 68  TYR   B N   
4957 C CA  . TYR   B 68  ? 0.1636 0.1629 0.2033 0.0054  -0.0395 -0.0354 68  TYR   B CA  
4958 C C   . TYR   B 68  ? 0.1515 0.1601 0.1959 -0.0002 -0.0329 -0.0401 68  TYR   B C   
4959 O O   . TYR   B 68  ? 0.1604 0.1710 0.2028 -0.0002 -0.0323 -0.0559 68  TYR   B O   
4960 C CB  . TYR   B 68  ? 0.1687 0.1843 0.2090 0.0099  -0.0396 -0.0487 68  TYR   B CB  
4961 C CG  . TYR   B 68  ? 0.1798 0.2011 0.2224 0.0158  -0.0377 -0.0707 68  TYR   B CG  
4962 C CD1 . TYR   B 68  ? 0.1835 0.2088 0.2484 -0.0022 -0.0406 -0.0856 68  TYR   B CD1 
4963 C CD2 . TYR   B 68  ? 0.1871 0.2190 0.2414 0.0228  -0.0480 -0.0649 68  TYR   B CD2 
4964 C CE1 . TYR   B 68  ? 0.1929 0.2262 0.2748 -0.0014 -0.0395 -0.0859 68  TYR   B CE1 
4965 C CE2 . TYR   B 68  ? 0.1900 0.2275 0.2507 0.0188  -0.0418 -0.0836 68  TYR   B CE2 
4966 C CZ  . TYR   B 68  ? 0.1838 0.2327 0.2688 0.0029  -0.0435 -0.0861 68  TYR   B CZ  
4967 O OH  . TYR   B 68  ? 0.1797 0.2499 0.2956 -0.0006 -0.0377 -0.0636 68  TYR   B OH  
4977 N N   . ILE   B 69  ? 0.1537 0.1514 0.2040 0.0008  -0.0294 -0.0439 69  ILE   B N   
4978 C CA  . ILE   B 69  ? 0.1624 0.1574 0.2121 -0.0075 -0.0208 -0.0429 69  ILE   B CA  
4979 C C   . ILE   B 69  ? 0.1658 0.1515 0.1986 0.0040  -0.0350 -0.0279 69  ILE   B C   
4980 O O   . ILE   B 69  ? 0.1743 0.1572 0.2077 0.0011  -0.0254 -0.0249 69  ILE   B O   
4981 C CB  . ILE   B 69  ? 0.1711 0.1625 0.2413 -0.0113 0.0094  -0.0331 69  ILE   B CB  
4982 C CG1 . ILE   B 69  ? 0.1735 0.1682 0.2546 -0.0095 0.0130  -0.0404 69  ILE   B CG1 
4983 C CG2 . ILE   B 69  ? 0.1914 0.1718 0.2589 -0.0077 -0.0028 -0.0279 69  ILE   B CG2 
4984 C CD1 . ILE   B 69  ? 0.1706 0.1723 0.2593 -0.0186 0.0104  -0.0420 69  ILE   B CD1 
4996 N N   . ALA   B 70  ? 0.1651 0.1530 0.1936 0.0025  -0.0431 -0.0219 70  ALA   B N   
4997 C CA  . ALA   B 70  ? 0.1668 0.1618 0.1839 0.0007  -0.0430 -0.0229 70  ALA   B CA  
4998 C C   . ALA   B 70  ? 0.1724 0.1590 0.1836 -0.0040 -0.0528 -0.0254 70  ALA   B C   
4999 O O   . ALA   B 70  ? 0.1827 0.1604 0.1792 0.0005  -0.0417 -0.0316 70  ALA   B O   
5000 C CB  . ALA   B 70  ? 0.1625 0.1758 0.1908 -0.0040 -0.0364 -0.0205 70  ALA   B CB  
5006 N N   . THR   B 71  ? 0.1829 0.1561 0.1889 0.0015  -0.0583 -0.0323 71  THR   B N   
5007 C CA  . THR   B 71  ? 0.1943 0.1621 0.1998 0.0046  -0.0702 -0.0299 71  THR   B CA  
5008 C C   . THR   B 71  ? 0.1863 0.1640 0.2268 0.0202  -0.0689 -0.0478 71  THR   B C   
5009 O O   . THR   B 71  ? 0.1978 0.1759 0.2647 0.0226  -0.0586 -0.0694 71  THR   B O   
5010 C CB  . THR   B 71  ? 0.2177 0.1885 0.2224 -0.0030 -0.0842 -0.0085 71  THR   B CB  
5011 O OG1 . THR   B 71  ? 0.2333 0.2152 0.2591 -0.0170 -0.0734 0.0092  71  THR   B OG1 
5012 C CG2 . THR   B 71  ? 0.2334 0.1855 0.2447 0.0033  -0.0765 0.0046  71  THR   B CG2 
5020 N N   . ASN   B 72  ? 0.1706 0.1641 0.2276 0.0096  -0.0624 -0.0695 72  ASN   B N   
5021 C CA  . ASN   B 72  ? 0.1764 0.1820 0.2237 0.0168  -0.0480 -0.0732 72  ASN   B CA  
5022 C C   . ASN   B 72  ? 0.1713 0.1957 0.2221 0.0008  -0.0292 -0.0716 72  ASN   B C   
5023 O O   . ASN   B 72  ? 0.1704 0.2129 0.2510 0.0071  -0.0152 -0.0683 72  ASN   B O   
5024 C CB  . ASN   B 72  ? 0.1847 0.1937 0.2310 0.0191  -0.0591 -0.0716 72  ASN   B CB  
5025 C CG  . ASN   B 72  ? 0.2008 0.2145 0.2466 0.0308  -0.0590 -0.0417 72  ASN   B CG  
5026 O OD1 . ASN   B 72  ? 0.2230 0.2280 0.2462 0.0188  -0.0431 -0.0433 72  ASN   B OD1 
5027 N ND2 . ASN   B 72  ? 0.2095 0.2233 0.2754 0.0443  -0.0440 -0.0101 72  ASN   B ND2 
5034 N N   . GLY   B 73  ? 0.1749 0.1985 0.2059 -0.0044 -0.0336 -0.0691 73  GLY   B N   
5035 C CA  . GLY   B 73  ? 0.1747 0.2022 0.1787 -0.0080 -0.0255 -0.0498 73  GLY   B CA  
5036 C C   . GLY   B 73  ? 0.1668 0.1941 0.1390 -0.0003 -0.0308 -0.0443 73  GLY   B C   
5037 O O   . GLY   B 73  ? 0.1682 0.1830 0.1573 0.0051  -0.0269 -0.0319 73  GLY   B O   
5041 N N   . PRO   B 74  ? 0.1693 0.2068 0.1407 0.0016  -0.0309 -0.0389 74  PRO   B N   
5042 C CA  . PRO   B 74  ? 0.1633 0.2050 0.1284 0.0061  -0.0273 -0.0287 74  PRO   B CA  
5043 C C   . PRO   B 74  ? 0.1516 0.1925 0.1316 0.0018  -0.0258 -0.0287 74  PRO   B C   
5044 O O   . PRO   B 74  ? 0.1509 0.1950 0.1768 0.0050  -0.0183 -0.0414 74  PRO   B O   
5045 C CB  . PRO   B 74  ? 0.1789 0.2213 0.1464 0.0044  -0.0239 -0.0248 74  PRO   B CB  
5046 C CG  . PRO   B 74  ? 0.1951 0.2325 0.1770 0.0028  -0.0109 -0.0257 74  PRO   B CG  
5047 C CD  . PRO   B 74  ? 0.1862 0.2247 0.1563 0.0017  -0.0132 -0.0407 74  PRO   B CD  
5055 N N   . LEU   B 75  ? 0.1452 0.1849 0.1244 0.0042  -0.0259 -0.0311 75  LEU   B N   
5056 C CA  . LEU   B 75  ? 0.1443 0.1778 0.1394 0.0028  -0.0211 -0.0144 75  LEU   B CA  
5057 C C   . LEU   B 75  ? 0.1510 0.1871 0.1315 0.0051  -0.0161 -0.0066 75  LEU   B C   
5058 O O   . LEU   B 75  ? 0.1690 0.2017 0.1390 0.0001  -0.0154 -0.0041 75  LEU   B O   
5059 C CB  . LEU   B 75  ? 0.1533 0.1777 0.1365 -0.0088 -0.0239 -0.0032 75  LEU   B CB  
5060 C CG  . LEU   B 75  ? 0.1853 0.1881 0.1582 -0.0335 -0.0176 -0.0115 75  LEU   B CG  
5061 C CD1 . LEU   B 75  ? 0.2180 0.2122 0.1628 -0.0451 0.0073  -0.0108 75  LEU   B CD1 
5062 C CD2 . LEU   B 75  ? 0.2254 0.2065 0.2196 -0.0217 -0.0083 -0.0027 75  LEU   B CD2 
5074 N N   . LYS   B 76  ? 0.1521 0.2040 0.1595 0.0017  -0.0078 -0.0034 76  LYS   B N   
5075 C CA  . LYS   B 76  ? 0.1642 0.2100 0.1803 -0.0028 0.0196  -0.0106 76  LYS   B CA  
5076 C C   . LYS   B 76  ? 0.1514 0.1927 0.1509 0.0065  0.0038  0.0090  76  LYS   B C   
5077 O O   . LYS   B 76  ? 0.1489 0.1786 0.1489 0.0002  -0.0062 0.0122  76  LYS   B O   
5078 C CB  . LYS   B 76  ? 0.1847 0.2218 0.2683 -0.0039 0.0334  -0.0448 76  LYS   B CB  
5079 C CG  . LYS   B 76  ? 0.1931 0.2383 0.3280 0.0036  0.0199  -0.0570 76  LYS   B CG  
5080 C CD  . LYS   B 76  ? 0.1881 0.2473 0.3875 0.0105  0.0038  -0.0697 76  LYS   B CD  
5081 C CE  . LYS   B 76  ? 0.1950 0.2653 0.4401 0.0121  -0.0124 -0.0800 76  LYS   B CE  
5082 N NZ  . LYS   B 76  ? 0.1927 0.2738 0.4690 0.0116  -0.0319 -0.0907 76  LYS   B NZ  
5096 N N   . VAL   B 77  ? 0.1604 0.2009 0.1355 0.0191  0.0075  0.0108  77  VAL   B N   
5097 C CA  . VAL   B 77  ? 0.1586 0.1895 0.1467 0.0223  0.0102  0.0328  77  VAL   B CA  
5098 C C   . VAL   B 77  ? 0.1468 0.1692 0.1517 0.0201  0.0086  0.0235  77  VAL   B C   
5099 O O   . VAL   B 77  ? 0.1534 0.1702 0.1556 0.0275  0.0161  0.0185  77  VAL   B O   
5100 C CB  . VAL   B 77  ? 0.1668 0.1985 0.1778 0.0217  0.0202  0.0443  77  VAL   B CB  
5101 C CG1 . VAL   B 77  ? 0.1724 0.1892 0.2077 0.0100  0.0222  0.0547  77  VAL   B CG1 
5102 C CG2 . VAL   B 77  ? 0.1793 0.2202 0.2097 0.0221  0.0058  0.0495  77  VAL   B CG2 
5112 N N   . GLY   B 78  ? 0.1432 0.1604 0.1483 0.0144  0.0010  0.0164  78  GLY   B N   
5113 C CA  . GLY   B 78  ? 0.1383 0.1540 0.1477 0.0113  0.0093  0.0021  78  GLY   B CA  
5114 C C   . GLY   B 78  ? 0.1360 0.1472 0.1367 0.0080  0.0066  0.0133  78  GLY   B C   
5115 O O   . GLY   B 78  ? 0.1459 0.1429 0.1501 0.0130  0.0026  0.0133  78  GLY   B O   
5119 N N   . GLY   B 79  ? 0.1311 0.1557 0.1480 0.0078  0.0068  0.0043  79  GLY   B N   
5120 C CA  . GLY   B 79  ? 0.1350 0.1431 0.1373 0.0050  0.0021  -0.0002 79  GLY   B CA  
5121 C C   . GLY   B 79  ? 0.1259 0.1374 0.1482 0.0105  -0.0000 0.0020  79  GLY   B C   
5122 O O   . GLY   B 79  ? 0.1343 0.1354 0.1611 0.0117  0.0076  0.0122  79  GLY   B O   
5126 N N   . SER   B 80  ? 0.1312 0.1282 0.1522 0.0041  0.0109  -0.0017 80  SER   B N   
5127 C CA  . SER   B 80  ? 0.1273 0.1241 0.1619 -0.0008 0.0006  0.0011  80  SER   B CA  
5128 C C   . SER   B 80  ? 0.1300 0.1252 0.1600 0.0078  -0.0086 -0.0080 80  SER   B C   
5129 O O   . SER   B 80  ? 0.1431 0.1289 0.1911 0.0077  0.0020  -0.0191 80  SER   B O   
5130 C CB  . SER   B 80  ? 0.1308 0.1301 0.1688 -0.0045 -0.0073 -0.0000 80  SER   B CB  
5131 O OG  . SER   B 80  ? 0.1387 0.1465 0.1914 -0.0007 -0.0197 0.0121  80  SER   B OG  
5137 N N   . CYS   B 81  ? 0.1315 0.1109 0.1709 0.0009  -0.0089 -0.0102 81  CYS   B N   
5138 C CA  . CYS   B 81  ? 0.1349 0.1074 0.1710 0.0056  -0.0173 -0.0086 81  CYS   B CA  
5139 C C   . CYS   B 81  ? 0.1280 0.1041 0.1518 -0.0002 -0.0250 -0.0072 81  CYS   B C   
5140 O O   . CYS   B 81  ? 0.1550 0.1115 0.1596 0.0042  -0.0094 -0.0096 81  CYS   B O   
5141 C CB  . CYS   B 81  ? 0.1490 0.1219 0.1774 -0.0082 -0.0208 -0.0088 81  CYS   B CB  
5142 S SG  . CYS   B 81  ? 0.1465 0.1454 0.1627 -0.0076 -0.0287 -0.0115 81  CYS   B SG  
5148 N N   . VAL   B 82  ? 0.1355 0.1060 0.1640 -0.0008 -0.0161 -0.0086 82  VAL   B N   
5149 C CA  . VAL   B 82  ? 0.1359 0.1132 0.1724 -0.0068 -0.0136 -0.0037 82  VAL   B CA  
5150 C C   . VAL   B 82  ? 0.1433 0.1078 0.1783 -0.0055 -0.0108 -0.0081 82  VAL   B C   
5151 O O   . VAL   B 82  ? 0.1544 0.1107 0.1997 -0.0028 -0.0129 -0.0214 82  VAL   B O   
5152 C CB  . VAL   B 82  ? 0.1488 0.1366 0.1913 -0.0021 -0.0186 0.0022  82  VAL   B CB  
5153 C CG1 . VAL   B 82  ? 0.1665 0.1597 0.1849 0.0045  -0.0135 0.0107  82  VAL   B CG1 
5154 C CG2 . VAL   B 82  ? 0.1579 0.1524 0.1965 -0.0026 -0.0355 0.0094  82  VAL   B CG2 
5164 N N   . LEU   B 83  ? 0.1331 0.1089 0.1775 -0.0149 -0.0213 -0.0083 83  LEU   B N   
5165 C CA  . LEU   B 83  ? 0.1385 0.1156 0.1632 -0.0129 -0.0196 -0.0079 83  LEU   B CA  
5166 C C   . LEU   B 83  ? 0.1367 0.1133 0.1628 -0.0187 -0.0169 -0.0014 83  LEU   B C   
5167 O O   . LEU   B 83  ? 0.1374 0.1244 0.1520 -0.0220 -0.0102 0.0058  83  LEU   B O   
5168 C CB  . LEU   B 83  ? 0.1430 0.1281 0.1694 -0.0160 -0.0309 -0.0127 83  LEU   B CB  
5169 C CG  . LEU   B 83  ? 0.1656 0.1504 0.1762 -0.0146 -0.0210 -0.0121 83  LEU   B CG  
5170 C CD1 . LEU   B 83  ? 0.1760 0.1562 0.1665 -0.0106 -0.0329 -0.0028 83  LEU   B CD1 
5171 C CD2 . LEU   B 83  ? 0.1779 0.1561 0.1965 -0.0078 -0.0134 -0.0318 83  LEU   B CD2 
5183 N N   . SER   B 84  ? 0.1414 0.1235 0.1906 -0.0226 -0.0156 0.0007  84  SER   B N   
5184 C CA  . SER   B 84  ? 0.1420 0.1430 0.1766 -0.0242 -0.0157 0.0148  84  SER   B CA  
5185 C C   . SER   B 84  ? 0.1338 0.1621 0.1471 -0.0230 -0.0210 0.0209  84  SER   B C   
5186 O O   . SER   B 84  ? 0.1483 0.1410 0.1419 -0.0189 -0.0135 -0.0005 84  SER   B O   
5187 C CB  . SER   B 84  ? 0.1618 0.1449 0.2349 -0.0286 0.0091  0.0193  84  SER   B CB  
5188 O OG  . SER   B 84  ? 0.1669 0.1601 0.2889 -0.0315 0.0194  0.0318  84  SER   B OG  
5194 N N   . GLY   B 85  ? 0.1384 0.1899 0.1545 -0.0237 -0.0167 0.0259  85  GLY   B N   
5195 C CA  . GLY   B 85  ? 0.1416 0.1964 0.1693 -0.0365 -0.0032 -0.0021 85  GLY   B CA  
5196 C C   . GLY   B 85  ? 0.1356 0.1706 0.1624 -0.0444 -0.0030 0.0070  85  GLY   B C   
5197 O O   . GLY   B 85  ? 0.1526 0.1745 0.1584 -0.0568 0.0157  -0.0044 85  GLY   B O   
5201 N N   . HIS   B 86  ? 0.1366 0.1516 0.1737 -0.0256 -0.0240 0.0146  86  HIS   B N   
5202 C CA  . HIS   B 86  ? 0.1387 0.1521 0.1779 -0.0272 -0.0211 0.0188  86  HIS   B CA  
5203 C C   . HIS   B 86  ? 0.1459 0.1621 0.1612 -0.0380 -0.0096 0.0389  86  HIS   B C   
5204 O O   . HIS   B 86  ? 0.1607 0.1713 0.1648 -0.0284 0.0040  0.0375  86  HIS   B O   
5205 C CB  . HIS   B 86  ? 0.1490 0.1488 0.1795 -0.0113 -0.0329 0.0087  86  HIS   B CB  
5206 C CG  . HIS   B 86  ? 0.1544 0.1581 0.1831 -0.0087 -0.0249 0.0125  86  HIS   B CG  
5207 N ND1 . HIS   B 86  ? 0.1693 0.1807 0.2004 -0.0206 -0.0291 0.0024  86  HIS   B ND1 
5208 C CD2 . HIS   B 86  ? 0.1561 0.1593 0.1959 -0.0101 -0.0248 0.0099  86  HIS   B CD2 
5209 C CE1 . HIS   B 86  ? 0.1686 0.1811 0.1912 -0.0138 -0.0115 -0.0154 86  HIS   B CE1 
5210 N NE2 . HIS   B 86  ? 0.1632 0.1729 0.1864 -0.0046 -0.0175 0.0005  86  HIS   B NE2 
5218 N N   . ASN   B 87  ? 0.1467 0.1655 0.1694 -0.0341 -0.0027 0.0366  87  ASN   B N   
5219 C CA  . ASN   B 87  ? 0.1507 0.1819 0.1829 -0.0285 0.0215  0.0228  87  ASN   B CA  
5220 C C   . ASN   B 87  ? 0.1599 0.1679 0.1728 -0.0245 0.0272  0.0132  87  ASN   B C   
5221 O O   . ASN   B 87  ? 0.1883 0.1729 0.1986 -0.0210 0.0441  0.0143  87  ASN   B O   
5222 C CB  . ASN   B 87  ? 0.1520 0.2171 0.2108 -0.0228 0.0236  0.0184  87  ASN   B CB  
5223 C CG  . ASN   B 87  ? 0.1553 0.2359 0.2125 0.0063  0.0337  0.0385  87  ASN   B CG  
5224 O OD1 . ASN   B 87  ? 0.1543 0.2264 0.1946 0.0129  0.0395  0.0578  87  ASN   B OD1 
5225 N ND2 . ASN   B 87  ? 0.1941 0.2442 0.2463 0.0053  0.0382  0.0241  87  ASN   B ND2 
5232 N N   . LEU   B 88  ? 0.1514 0.1616 0.1556 -0.0327 0.0135  0.0145  88  LEU   B N   
5233 C CA  . LEU   B 88  ? 0.1604 0.1544 0.1577 -0.0317 -0.0015 0.0054  88  LEU   B CA  
5234 C C   . LEU   B 88  ? 0.1613 0.1429 0.1601 -0.0388 -0.0029 0.0110  88  LEU   B C   
5235 O O   . LEU   B 88  ? 0.1873 0.1540 0.1979 -0.0204 -0.0252 -0.0090 88  LEU   B O   
5236 C CB  . LEU   B 88  ? 0.1719 0.1579 0.1761 -0.0395 -0.0037 0.0219  88  LEU   B CB  
5237 C CG  . LEU   B 88  ? 0.2085 0.1885 0.1978 -0.0366 -0.0206 0.0419  88  LEU   B CG  
5238 C CD1 . LEU   B 88  ? 0.2215 0.2158 0.2097 -0.0469 -0.0135 0.0504  88  LEU   B CD1 
5239 C CD2 . LEU   B 88  ? 0.2371 0.2162 0.2387 0.0044  -0.0474 0.0206  88  LEU   B CD2 
5251 N N   . ALA   B 89  ? 0.1538 0.1376 0.1453 -0.0340 0.0148  0.0101  89  ALA   B N   
5252 C CA  . ALA   B 89  ? 0.1501 0.1356 0.1335 -0.0340 0.0030  0.0133  89  ALA   B CA  
5253 C C   . ALA   B 89  ? 0.1562 0.1338 0.1358 -0.0390 0.0109  0.0071  89  ALA   B C   
5254 O O   . ALA   B 89  ? 0.1428 0.1495 0.1743 -0.0390 0.0073  -0.0210 89  ALA   B O   
5255 C CB  . ALA   B 89  ? 0.1419 0.1356 0.1473 -0.0368 -0.0033 0.0202  89  ALA   B CB  
5261 N N   . LYS   B 90  ? 0.1930 0.1308 0.1416 -0.0430 -0.0060 0.0087  90  LYS   B N   
5262 C CA  . LYS   B 90  ? 0.2091 0.1242 0.1397 -0.0430 -0.0069 0.0037  90  LYS   B CA  
5263 C C   . LYS   B 90  ? 0.2004 0.1140 0.1578 -0.0427 -0.0054 -0.0046 90  LYS   B C   
5264 O O   . LYS   B 90  ? 0.2152 0.1361 0.1793 -0.0594 0.0065  -0.0034 90  LYS   B O   
5265 C CB  . LYS   B 90  ? 0.2340 0.1321 0.1746 -0.0297 0.0070  0.0206  90  LYS   B CB  
5266 C CG  . LYS   B 90  ? 0.2408 0.1436 0.1901 -0.0199 0.0336  0.0256  90  LYS   B CG  
5267 C CD  . LYS   B 90  ? 0.2638 0.1718 0.2352 -0.0172 0.0501  0.0056  90  LYS   B CD  
5268 C CE  . LYS   B 90  ? 0.2785 0.1932 0.2756 -0.0234 0.0541  -0.0076 90  LYS   B CE  
5269 N NZ  . LYS   B 90  ? 0.2824 0.1904 0.2852 -0.0305 0.0665  -0.0037 90  LYS   B NZ  
5283 N N   . HIS   B 91  ? 0.1722 0.1069 0.1302 -0.0313 -0.0162 0.0015  91  HIS   B N   
5284 C CA  . HIS   B 91  ? 0.1513 0.1116 0.1413 -0.0217 -0.0130 -0.0009 91  HIS   B CA  
5285 C C   . HIS   B 91  ? 0.1403 0.1175 0.1239 -0.0260 -0.0136 0.0015  91  HIS   B C   
5286 O O   . HIS   B 91  ? 0.1560 0.1196 0.1296 -0.0219 -0.0190 -0.0003 91  HIS   B O   
5287 C CB  . HIS   B 91  ? 0.1706 0.1115 0.1839 -0.0075 -0.0014 0.0136  91  HIS   B CB  
5288 C CG  . HIS   B 91  ? 0.2195 0.1320 0.2490 0.0047  0.0277  0.0258  91  HIS   B CG  
5289 N ND1 . HIS   B 91  ? 0.2540 0.1416 0.3047 0.0018  0.0374  0.0074  91  HIS   B ND1 
5290 C CD2 . HIS   B 91  ? 0.2362 0.1671 0.2906 0.0190  0.0159  0.0561  91  HIS   B CD2 
5291 C CE1 . HIS   B 91  ? 0.2578 0.1558 0.3206 0.0214  0.0370  0.0180  91  HIS   B CE1 
5292 N NE2 . HIS   B 91  ? 0.2493 0.1747 0.3179 0.0287  0.0289  0.0634  91  HIS   B NE2 
5300 N N   . CYS   B 92  ? 0.1318 0.1156 0.1307 -0.0258 -0.0147 -0.0027 92  CYS   B N   
5301 C CA  . CYS   B 92  ? 0.1315 0.1143 0.1277 -0.0222 -0.0123 0.0012  92  CYS   B CA  
5302 C C   . CYS   B 92  ? 0.1264 0.1030 0.1248 -0.0111 -0.0098 0.0002  92  CYS   B C   
5303 O O   . CYS   B 92  ? 0.1320 0.1140 0.1474 -0.0164 -0.0097 -0.0010 92  CYS   B O   
5304 C CB  . CYS   B 92  ? 0.1343 0.1257 0.1332 -0.0136 -0.0136 0.0018  92  CYS   B CB  
5305 S SG  . CYS   B 92  ? 0.1310 0.1251 0.1475 -0.0111 -0.0129 0.0070  92  CYS   B SG  
5311 N N   . LEU   B 93  ? 0.1200 0.1073 0.1220 -0.0133 -0.0088 -0.0017 93  LEU   B N   
5312 C CA  . LEU   B 93  ? 0.1243 0.1069 0.1277 -0.0032 -0.0107 0.0046  93  LEU   B CA  
5313 C C   . LEU   B 93  ? 0.1160 0.1040 0.1202 -0.0012 -0.0109 -0.0002 93  LEU   B C   
5314 O O   . LEU   B 93  ? 0.1199 0.1075 0.1361 -0.0057 -0.0066 -0.0019 93  LEU   B O   
5315 C CB  . LEU   B 93  ? 0.1199 0.1088 0.1420 0.0004  -0.0115 0.0014  93  LEU   B CB  
5316 C CG  . LEU   B 93  ? 0.1180 0.1225 0.1533 -0.0025 -0.0085 0.0106  93  LEU   B CG  
5317 C CD1 . LEU   B 93  ? 0.1229 0.1342 0.1644 0.0044  -0.0054 -0.0061 93  LEU   B CD1 
5318 C CD2 . LEU   B 93  ? 0.1173 0.1299 0.1657 0.0017  -0.0150 0.0022  93  LEU   B CD2 
5330 N N   . HIS   B 94  ? 0.1163 0.1059 0.1162 -0.0074 -0.0129 0.0033  94  HIS   B N   
5331 C CA  . HIS   B 94  ? 0.1252 0.1060 0.1210 -0.0038 -0.0117 0.0033  94  HIS   B CA  
5332 C C   . HIS   B 94  ? 0.1168 0.1065 0.1393 -0.0021 -0.0035 0.0005  94  HIS   B C   
5333 O O   . HIS   B 94  ? 0.1254 0.1197 0.1730 -0.0035 0.0048  -0.0126 94  HIS   B O   
5334 C CB  . HIS   B 94  ? 0.1226 0.1125 0.1327 -0.0067 -0.0133 0.0053  94  HIS   B CB  
5335 C CG  . HIS   B 94  ? 0.1256 0.1107 0.1298 -0.0096 -0.0290 0.0038  94  HIS   B CG  
5336 N ND1 . HIS   B 94  ? 0.1263 0.1179 0.1353 -0.0074 -0.0227 -0.0011 94  HIS   B ND1 
5337 C CD2 . HIS   B 94  ? 0.1276 0.1186 0.1461 -0.0026 -0.0185 0.0096  94  HIS   B CD2 
5338 C CE1 . HIS   B 94  ? 0.1288 0.1195 0.1408 -0.0131 -0.0256 0.0055  94  HIS   B CE1 
5339 N NE2 . HIS   B 94  ? 0.1244 0.1254 0.1448 -0.0128 -0.0157 0.0036  94  HIS   B NE2 
5347 N N   . VAL   B 95  ? 0.1129 0.1027 0.1390 -0.0011 -0.0053 0.0003  95  VAL   B N   
5348 C CA  . VAL   B 95  ? 0.1131 0.1135 0.1370 -0.0008 -0.0025 0.0097  95  VAL   B CA  
5349 C C   . VAL   B 95  ? 0.1147 0.1154 0.1397 -0.0038 0.0039  0.0012  95  VAL   B C   
5350 O O   . VAL   B 95  ? 0.1212 0.1145 0.1501 0.0035  0.0019  0.0091  95  VAL   B O   
5351 C CB  . VAL   B 95  ? 0.1251 0.1123 0.1422 -0.0044 -0.0141 0.0026  95  VAL   B CB  
5352 C CG1 . VAL   B 95  ? 0.1277 0.1319 0.1639 -0.0143 -0.0091 0.0089  95  VAL   B CG1 
5353 C CG2 . VAL   B 95  ? 0.1320 0.1124 0.1411 0.0021  -0.0162 -0.0012 95  VAL   B CG2 
5363 N N   . VAL   B 96  ? 0.1237 0.1214 0.1342 0.0051  0.0003  0.0094  96  VAL   B N   
5364 C CA  . VAL   B 96  ? 0.1336 0.1317 0.1249 0.0065  -0.0011 0.0105  96  VAL   B CA  
5365 C C   . VAL   B 96  ? 0.1327 0.1323 0.1317 0.0093  0.0020  0.0151  96  VAL   B C   
5366 O O   . VAL   B 96  ? 0.1352 0.1415 0.1477 0.0058  0.0051  0.0005  96  VAL   B O   
5367 C CB  . VAL   B 96  ? 0.1394 0.1521 0.1302 0.0073  -0.0001 0.0015  96  VAL   B CB  
5368 C CG1 . VAL   B 96  ? 0.1456 0.1662 0.1315 0.0133  0.0040  -0.0002 96  VAL   B CG1 
5369 C CG2 . VAL   B 96  ? 0.1460 0.1626 0.1508 0.0045  0.0022  -0.0098 96  VAL   B CG2 
5379 N N   . GLY   B 97  ? 0.1392 0.1306 0.1399 0.0062  -0.0016 0.0169  97  GLY   B N   
5380 C CA  . GLY   B 97  ? 0.1511 0.1350 0.1286 0.0048  0.0041  0.0147  97  GLY   B CA  
5381 C C   . GLY   B 97  ? 0.1642 0.1474 0.1326 0.0125  0.0010  0.0124  97  GLY   B C   
5382 O O   . GLY   B 97  ? 0.1710 0.1569 0.1414 0.0071  -0.0041 0.0138  97  GLY   B O   
5386 N N   . PRO   B 98  ? 0.1695 0.1470 0.1467 0.0083  0.0159  0.0241  98  PRO   B N   
5387 C CA  . PRO   B 98  ? 0.1791 0.1645 0.1583 0.0135  0.0276  0.0208  98  PRO   B CA  
5388 C C   . PRO   B 98  ? 0.1903 0.1678 0.1334 0.0260  0.0189  0.0342  98  PRO   B C   
5389 O O   . PRO   B 98  ? 0.1875 0.1637 0.1435 0.0239  0.0206  0.0274  98  PRO   B O   
5390 C CB  . PRO   B 98  ? 0.1666 0.1653 0.1744 0.0063  0.0398  0.0173  98  PRO   B CB  
5391 C CG  . PRO   B 98  ? 0.1676 0.1585 0.1682 0.0058  0.0228  0.0227  98  PRO   B CG  
5392 C CD  . PRO   B 98  ? 0.1508 0.1492 0.1546 0.0114  0.0164  0.0245  98  PRO   B CD  
5400 N N   A ASN   B 99  ? 0.2025 0.1788 0.1434 0.0444  0.0238  0.0281  99  ASN   B N   
5401 N N   B ASN   B 99  ? 0.1995 0.1764 0.1424 0.0277  0.0122  0.0182  99  ASN   B N   
5402 C CA  A ASN   B 99  ? 0.2169 0.1876 0.1504 0.0590  0.0239  0.0413  99  ASN   B CA  
5403 C CA  B ASN   B 99  ? 0.2121 0.1776 0.1452 0.0254  -0.0009 0.0307  99  ASN   B CA  
5404 C C   A ASN   B 99  ? 0.2353 0.2126 0.1690 0.0610  0.0300  0.0451  99  ASN   B C   
5405 C C   B ASN   B 99  ? 0.2280 0.1967 0.1464 0.0141  0.0108  0.0406  99  ASN   B C   
5406 O O   A ASN   B 99  ? 0.2443 0.2174 0.1794 0.0648  0.0243  0.0463  99  ASN   B O   
5407 O O   B ASN   B 99  ? 0.2324 0.1989 0.1563 0.0041  0.0071  0.0359  99  ASN   B O   
5408 C CB  A ASN   B 99  ? 0.2212 0.1848 0.1590 0.0609  0.0243  0.0399  99  ASN   B CB  
5409 C CB  B ASN   B 99  ? 0.2179 0.1712 0.1726 0.0241  -0.0155 0.0268  99  ASN   B CB  
5410 C CG  A ASN   B 99  ? 0.2247 0.1928 0.1858 0.0598  0.0182  0.0336  99  ASN   B CG  
5411 C CG  B ASN   B 99  ? 0.2235 0.1759 0.1979 0.0202  -0.0336 0.0311  99  ASN   B CG  
5412 O OD1 A ASN   B 99  ? 0.2257 0.1933 0.2021 0.0692  0.0239  0.0311  99  ASN   B OD1 
5413 O OD1 B ASN   B 99  ? 0.2294 0.1817 0.2131 0.0223  -0.0422 0.0254  99  ASN   B OD1 
5414 N ND2 A ASN   B 99  ? 0.2276 0.1992 0.2015 0.0558  0.0057  0.0273  99  ASN   B ND2 
5415 N ND2 B ASN   B 99  ? 0.2224 0.1758 0.2179 0.0204  -0.0464 0.0333  99  ASN   B ND2 
5428 N N   A VAL   B 100 ? 0.2558 0.2337 0.2068 0.0442  0.0315  0.0496  100 VAL   B N   
5429 N N   B VAL   B 100 ? 0.2498 0.2119 0.1763 0.0035  0.0166  0.0651  100 VAL   B N   
5430 C CA  A VAL   B 100 ? 0.2832 0.2559 0.2545 0.0293  0.0296  0.0496  100 VAL   B CA  
5431 C CA  B VAL   B 100 ? 0.2830 0.2293 0.2283 -0.0003 0.0203  0.0802  100 VAL   B CA  
5432 C C   A VAL   B 100 ? 0.3065 0.2685 0.2620 0.0311  0.0277  0.0561  100 VAL   B C   
5433 C C   B VAL   B 100 ? 0.3079 0.2299 0.2215 0.0142  0.0160  0.0998  100 VAL   B C   
5434 O O   A VAL   B 100 ? 0.3083 0.2746 0.2671 0.0291  0.0399  0.0539  100 VAL   B O   
5435 O O   B VAL   B 100 ? 0.3122 0.2343 0.2145 0.0081  0.0262  0.0880  100 VAL   B O   
5436 C CB  A VAL   B 100 ? 0.2891 0.2675 0.3023 0.0095  0.0260  0.0481  100 VAL   B CB  
5437 C CB  B VAL   B 100 ? 0.2938 0.2509 0.2925 -0.0208 0.0218  0.0824  100 VAL   B CB  
5438 C CG1 A VAL   B 100 ? 0.2911 0.2720 0.3200 0.0055  0.0266  0.0482  100 VAL   B CG1 
5439 C CG1 B VAL   B 100 ? 0.2977 0.2593 0.3199 -0.0254 0.0238  0.0815  100 VAL   B CG1 
5440 C CG2 A VAL   B 100 ? 0.2913 0.2693 0.3152 0.0031  0.0261  0.0510  100 VAL   B CG2 
5441 C CG2 B VAL   B 100 ? 0.2984 0.2552 0.3041 -0.0256 0.0264  0.0937  100 VAL   B CG2 
5460 N N   A ASN   B 101 ? 0.3263 0.2788 0.2660 0.0346  0.0145  0.0598  101 ASN   B N   
5461 N N   B ASN   B 101 ? 0.3304 0.2379 0.2307 0.0306  0.0012  0.1160  101 ASN   B N   
5462 C CA  A ASN   B 101 ? 0.3487 0.2921 0.2828 0.0340  0.0035  0.0602  101 ASN   B CA  
5463 C CA  B ASN   B 101 ? 0.3595 0.2528 0.2530 0.0419  -0.0108 0.1286  101 ASN   B CA  
5464 C C   A ASN   B 101 ? 0.3720 0.3153 0.2923 0.0327  -0.0014 0.0618  101 ASN   B C   
5465 C C   B ASN   B 101 ? 0.3859 0.2842 0.2506 0.0425  -0.0236 0.1387  101 ASN   B C   
5466 O O   A ASN   B 101 ? 0.3732 0.3190 0.3029 0.0337  0.0003  0.0571  101 ASN   B O   
5467 O O   B ASN   B 101 ? 0.3917 0.2981 0.2710 0.0448  -0.0277 0.1196  101 ASN   B O   
5468 C CB  A ASN   B 101 ? 0.3482 0.2841 0.2871 0.0311  0.0026  0.0554  101 ASN   B CB  
5469 C CB  B ASN   B 101 ? 0.3619 0.2430 0.2639 0.0431  -0.0021 0.1205  101 ASN   B CB  
5470 C CG  A ASN   B 101 ? 0.3481 0.2773 0.2903 0.0271  0.0018  0.0551  101 ASN   B CG  
5471 C CG  B ASN   B 101 ? 0.3622 0.2331 0.2719 0.0438  0.0054  0.1213  101 ASN   B CG  
5472 O OD1 A ASN   B 101 ? 0.3512 0.2789 0.3046 0.0223  0.0099  0.0514  101 ASN   B OD1 
5473 O OD1 B ASN   B 101 ? 0.3690 0.2378 0.3024 0.0346  0.0219  0.1093  101 ASN   B OD1 
5474 N ND2 A ASN   B 101 ? 0.3461 0.2740 0.2848 0.0258  -0.0033 0.0522  101 ASN   B ND2 
5475 N ND2 B ASN   B 101 ? 0.3576 0.2320 0.2685 0.0472  0.0025  0.1082  101 ASN   B ND2 
5488 N N   A LYS   B 102 ? 0.3922 0.3361 0.2997 0.0289  -0.0029 0.0582  102 LYS   B N   
5489 N N   B LYS   B 102 ? 0.4048 0.3109 0.2645 0.0345  -0.0171 0.1315  102 LYS   B N   
5490 C CA  A LYS   B 102 ? 0.4118 0.3593 0.3165 0.0228  0.0002  0.0520  102 LYS   B CA  
5491 C CA  B LYS   B 102 ? 0.4241 0.3471 0.2848 0.0240  -0.0034 0.1097  102 LYS   B CA  
5492 C C   A LYS   B 102 ? 0.4130 0.3615 0.2986 0.0265  0.0057  0.0593  102 LYS   B C   
5493 C C   B LYS   B 102 ? 0.4224 0.3516 0.2641 0.0282  0.0054  0.1144  102 LYS   B C   
5494 O O   A LYS   B 102 ? 0.4191 0.3641 0.3013 0.0270  0.0007  0.0571  102 LYS   B O   
5495 O O   B LYS   B 102 ? 0.4291 0.3575 0.2696 0.0304  0.0000  0.1057  102 LYS   B O   
5496 C CB  A LYS   B 102 ? 0.4285 0.3781 0.3609 0.0145  0.0041  0.0336  102 LYS   B CB  
5497 C CB  B LYS   B 102 ? 0.4440 0.3762 0.3433 0.0124  0.0084  0.0710  102 LYS   B CB  
5498 C CG  A LYS   B 102 ? 0.4426 0.3937 0.4093 0.0082  0.0092  0.0152  102 LYS   B CG  
5499 C CG  B LYS   B 102 ? 0.4611 0.4012 0.4056 0.0044  0.0196  0.0343  102 LYS   B CG  
5500 C CD  A LYS   B 102 ? 0.4538 0.4065 0.4557 0.0030  0.0145  0.0005  102 LYS   B CD  
5501 C CD  B LYS   B 102 ? 0.4747 0.4208 0.4643 -0.0028 0.0284  0.0065  102 LYS   B CD  
5502 C CE  A LYS   B 102 ? 0.4614 0.4161 0.4936 -0.0013 0.0195  -0.0098 102 LYS   B CE  
5503 C CE  B LYS   B 102 ? 0.4837 0.4353 0.5125 -0.0088 0.0358  -0.0128 102 LYS   B CE  
5504 N NZ  A LYS   B 102 ? 0.4653 0.4223 0.5154 -0.0036 0.0217  -0.0157 102 LYS   B NZ  
5505 N NZ  B LYS   B 102 ? 0.4884 0.4439 0.5410 -0.0121 0.0398  -0.0229 102 LYS   B NZ  
5532 N N   A GLY   B 103 ? 0.4062 0.3598 0.2923 0.0290  0.0184  0.0637  103 GLY   B N   
5533 N N   B GLY   B 103 ? 0.4098 0.3476 0.2510 0.0278  0.0249  0.1231  103 GLY   B N   
5534 C CA  A GLY   B 103 ? 0.3987 0.3574 0.2957 0.0315  0.0321  0.0610  103 GLY   B CA  
5535 C CA  B GLY   B 103 ? 0.3966 0.3433 0.2518 0.0279  0.0401  0.1144  103 GLY   B CA  
5536 C C   A GLY   B 103 ? 0.3881 0.3521 0.2954 0.0323  0.0427  0.0522  103 GLY   B C   
5537 C C   B GLY   B 103 ? 0.3798 0.3344 0.2437 0.0243  0.0541  0.0960  103 GLY   B C   
5538 O O   A GLY   B 103 ? 0.3918 0.3575 0.3069 0.0310  0.0418  0.0556  103 GLY   B O   
5539 O O   B GLY   B 103 ? 0.3849 0.3411 0.2550 0.0284  0.0550  0.0942  103 GLY   B O   
5546 N N   A GLU   B 104 ? 0.3720 0.3392 0.2825 0.0347  0.0506  0.0354  104 GLU   B N   
5547 N N   B GLU   B 104 ? 0.3560 0.3145 0.2198 0.0166  0.0594  0.0719  104 GLU   B N   
5548 C CA  A GLU   B 104 ? 0.3555 0.3272 0.2680 0.0371  0.0539  0.0190  104 GLU   B CA  
5549 C CA  B GLU   B 104 ? 0.3336 0.2971 0.1859 0.0083  0.0589  0.0500  104 GLU   B CA  
5550 C C   A GLU   B 104 ? 0.3586 0.3277 0.2775 0.0233  0.0682  0.0142  104 GLU   B C   
5551 C C   B GLU   B 104 ? 0.3356 0.2996 0.1971 -0.0046 0.0769  0.0347  104 GLU   B C   
5552 O O   A GLU   B 104 ? 0.3592 0.3268 0.2856 0.0225  0.0667  0.0089  104 GLU   B O   
5553 O O   B GLU   B 104 ? 0.3392 0.3034 0.2189 -0.0052 0.0702  0.0254  104 GLU   B O   
5554 C CB  A GLU   B 104 ? 0.3383 0.3139 0.2562 0.0541  0.0374  0.0013  104 GLU   B CB  
5555 C CB  B GLU   B 104 ? 0.3155 0.2772 0.1755 0.0122  0.0290  0.0274  104 GLU   B CB  
5556 C CG  A GLU   B 104 ? 0.3236 0.3041 0.2500 0.0677  0.0159  -0.0192 104 GLU   B CG  
5557 C CG  B GLU   B 104 ? 0.3026 0.2619 0.1741 0.0158  -0.0066 -0.0015 104 GLU   B CG  
5558 C CD  A GLU   B 104 ? 0.3099 0.2958 0.2443 0.0792  -0.0017 -0.0293 104 GLU   B CD  
5559 C CD  B GLU   B 104 ? 0.2915 0.2458 0.1626 0.0112  -0.0279 -0.0056 104 GLU   B CD  
5560 O OE1 A GLU   B 104 ? 0.2970 0.2869 0.2251 0.0875  0.0026  -0.0296 104 GLU   B OE1 
5561 O OE1 B GLU   B 104 ? 0.2734 0.2272 0.1444 0.0039  -0.0246 0.0011  104 GLU   B OE1 
5562 O OE2 A GLU   B 104 ? 0.3120 0.3022 0.2628 0.0781  -0.0158 -0.0339 104 GLU   B OE2 
5563 O OE2 B GLU   B 104 ? 0.2982 0.2550 0.1714 0.0053  -0.0437 -0.0082 104 GLU   B OE2 
5576 N N   A ASP   B 105 ? 0.3599 0.3312 0.2869 0.0096  0.0819  0.0149  105 ASP   B N   
5577 N N   B ASP   B 105 ? 0.3322 0.3012 0.2052 -0.0189 0.1013  0.0273  105 ASP   B N   
5578 C CA  A ASP   B 105 ? 0.3623 0.3338 0.3063 -0.0009 0.0918  0.0105  105 ASP   B CA  
5579 C CA  B ASP   B 105 ? 0.3331 0.3036 0.2411 -0.0322 0.1158  0.0111  105 ASP   B CA  
5580 C C   A ASP   B 105 ? 0.3532 0.3175 0.2917 -0.0072 0.0943  0.0098  105 ASP   B C   
5581 C C   B ASP   B 105 ? 0.3153 0.2723 0.2193 -0.0449 0.1193  0.0052  105 ASP   B C   
5582 O O   A ASP   B 105 ? 0.3507 0.3156 0.2878 -0.0071 0.0997  0.0109  105 ASP   B O   
5583 O O   B ASP   B 105 ? 0.2950 0.2608 0.2081 -0.0511 0.1248  -0.0042 105 ASP   B O   
5584 C CB  A ASP   B 105 ? 0.3714 0.3490 0.3490 -0.0010 0.0942  0.0052  105 ASP   B CB  
5585 C CB  B ASP   B 105 ? 0.3484 0.3301 0.3092 -0.0276 0.1175  -0.0037 105 ASP   B CB  
5586 C CG  A ASP   B 105 ? 0.3765 0.3588 0.3909 -0.0026 0.0989  0.0012  105 ASP   B CG  
5587 C CG  B ASP   B 105 ? 0.3577 0.3461 0.3725 -0.0280 0.1231  -0.0118 105 ASP   B CG  
5588 O OD1 A ASP   B 105 ? 0.3760 0.3628 0.3989 -0.0047 0.1043  0.0042  105 ASP   B OD1 
5589 O OD1 B ASP   B 105 ? 0.3577 0.3520 0.3846 -0.0325 0.1304  -0.0083 105 ASP   B OD1 
5590 O OD2 A ASP   B 105 ? 0.3799 0.3627 0.4167 -0.0024 0.0943  -0.0038 105 ASP   B OD2 
5591 O OD2 B ASP   B 105 ? 0.3598 0.3527 0.3950 -0.0303 0.1289  -0.0152 105 ASP   B OD2 
5600 N N   A ILE   B 106 ? 0.3458 0.3021 0.2935 -0.0097 0.0852  0.0102  106 ILE   B N   
5601 N N   B ILE   B 106 ? 0.3161 0.2519 0.2362 -0.0487 0.1064  0.0102  106 ILE   B N   
5602 C CA  A ILE   B 106 ? 0.3350 0.2872 0.2965 -0.0121 0.0849  0.0096  106 ILE   B CA  
5603 C CA  B ILE   B 106 ? 0.3080 0.2308 0.2537 -0.0577 0.1118  0.0125  106 ILE   B CA  
5604 C C   A ILE   B 106 ? 0.3157 0.2822 0.2883 -0.0080 0.0857  -0.0042 106 ILE   B C   
5605 C C   B ILE   B 106 ? 0.2810 0.2318 0.2445 -0.0539 0.1126  -0.0182 106 ILE   B C   
5606 O O   A ILE   B 106 ? 0.3131 0.2726 0.2870 -0.0062 0.0818  -0.0071 106 ILE   B O   
5607 O O   B ILE   B 106 ? 0.2685 0.2071 0.2299 -0.0594 0.1032  -0.0330 106 ILE   B O   
5608 C CB  A ILE   B 106 ? 0.3432 0.2798 0.3072 -0.0169 0.0799  0.0200  106 ILE   B CB  
5609 C CB  B ILE   B 106 ? 0.3271 0.2188 0.2824 -0.0619 0.1072  0.0354  106 ILE   B CB  
5610 C CG1 A ILE   B 106 ? 0.3473 0.2755 0.3099 -0.0133 0.0727  0.0212  106 ILE   B CG1 
5611 C CG1 B ILE   B 106 ? 0.3379 0.2171 0.3012 -0.0452 0.0942  0.0331  106 ILE   B CG1 
5612 C CG2 A ILE   B 106 ? 0.3466 0.2807 0.3197 -0.0206 0.0796  0.0242  106 ILE   B CG2 
5613 C CG2 B ILE   B 106 ? 0.3335 0.2186 0.3026 -0.0716 0.1095  0.0437  106 ILE   B CG2 
5614 C CD1 A ILE   B 106 ? 0.3488 0.2737 0.3075 -0.0097 0.0713  0.0240  106 ILE   B CD1 
5615 C CD1 B ILE   B 106 ? 0.3425 0.2178 0.3039 -0.0322 0.0921  0.0392  106 ILE   B CD1 
5638 N N   A GLN   B 107 ? 0.3007 0.2879 0.2946 -0.0103 0.0811  -0.0096 107 GLN   B N   
5639 N N   B GLN   B 107 ? 0.2721 0.2594 0.2649 -0.0505 0.1072  -0.0234 107 GLN   B N   
5640 C CA  A GLN   B 107 ? 0.2850 0.2904 0.3029 -0.0127 0.0728  -0.0098 107 GLN   B CA  
5641 C CA  B GLN   B 107 ? 0.2658 0.2824 0.2897 -0.0421 0.0988  -0.0191 107 GLN   B CA  
5642 C C   A GLN   B 107 ? 0.2513 0.2653 0.2708 -0.0081 0.0618  -0.0178 107 GLN   B C   
5643 C C   B GLN   B 107 ? 0.2401 0.2652 0.2694 -0.0257 0.0736  -0.0233 107 GLN   B C   
5644 O O   A GLN   B 107 ? 0.2485 0.2635 0.2851 -0.0044 0.0481  -0.0271 107 GLN   B O   
5645 O O   B GLN   B 107 ? 0.2366 0.2723 0.2997 -0.0236 0.0515  -0.0375 107 GLN   B O   
5646 C CB  A GLN   B 107 ? 0.3069 0.3177 0.3549 -0.0151 0.0654  -0.0045 107 GLN   B CB  
5647 C CB  B GLN   B 107 ? 0.2980 0.3227 0.3554 -0.0395 0.0864  -0.0150 107 GLN   B CB  
5648 C CG  A GLN   B 107 ? 0.3282 0.3416 0.4102 -0.0137 0.0492  0.0005  107 GLN   B CG  
5649 C CG  B GLN   B 107 ? 0.3325 0.3577 0.4250 -0.0322 0.0587  -0.0115 107 GLN   B CG  
5650 C CD  A GLN   B 107 ? 0.3443 0.3591 0.4563 -0.0129 0.0378  0.0053  107 GLN   B CD  
5651 C CD  B GLN   B 107 ? 0.3596 0.3839 0.4818 -0.0264 0.0385  -0.0082 107 GLN   B CD  
5652 O OE1 A GLN   B 107 ? 0.3493 0.3663 0.4734 -0.0102 0.0374  0.0048  107 GLN   B OE1 
5653 O OE1 B GLN   B 107 ? 0.3700 0.3959 0.5060 -0.0233 0.0351  -0.0088 107 GLN   B OE1 
5654 N NE2 A GLN   B 107 ? 0.3504 0.3643 0.4719 -0.0122 0.0325  0.0090  107 GLN   B NE2 
5655 N NE2 B GLN   B 107 ? 0.3705 0.3919 0.4977 -0.0234 0.0305  -0.0052 107 GLN   B NE2 
5672 N N   . LEU   B 108 ? 0.2175 0.2406 0.2333 -0.0039 0.0652  -0.0186 108 LEU   B N   
5673 C CA  . LEU   B 108 ? 0.1995 0.2072 0.2063 0.0228  0.0399  -0.0021 108 LEU   B CA  
5674 C C   . LEU   B 108 ? 0.1756 0.1659 0.1996 0.0188  0.0159  0.0191  108 LEU   B C   
5675 O O   . LEU   B 108 ? 0.1771 0.1517 0.2013 0.0180  0.0131  0.0051  108 LEU   B O   
5676 C CB  . LEU   B 108 ? 0.2169 0.2275 0.1921 0.0275  0.0317  -0.0028 108 LEU   B CB  
5677 C CG  . LEU   B 108 ? 0.2306 0.2572 0.1960 0.0279  0.0264  -0.0194 108 LEU   B CG  
5678 C CD1 . LEU   B 108 ? 0.2385 0.2735 0.1802 0.0135  0.0273  -0.0181 108 LEU   B CD1 
5679 C CD2 . LEU   B 108 ? 0.2455 0.2679 0.2226 0.0329  0.0191  -0.0252 108 LEU   B CD2 
5692 N N   . LEU   B 109 ? 0.1615 0.1464 0.1946 0.0145  0.0222  0.0247  109 LEU   B N   
5693 C CA  . LEU   B 109 ? 0.1475 0.1274 0.2029 0.0125  0.0191  0.0249  109 LEU   B CA  
5694 C C   . LEU   B 109 ? 0.1357 0.1178 0.2061 0.0070  0.0188  0.0133  109 LEU   B C   
5695 O O   . LEU   B 109 ? 0.1327 0.1188 0.2012 0.0072  0.0188  0.0240  109 LEU   B O   
5696 C CB  . LEU   B 109 ? 0.1564 0.1218 0.2053 0.0120  0.0151  0.0324  109 LEU   B CB  
5697 C CG  . LEU   B 109 ? 0.1555 0.1291 0.1974 0.0056  0.0050  0.0198  109 LEU   B CG  
5698 C CD1 . LEU   B 109 ? 0.1512 0.1403 0.2063 0.0096  0.0108  0.0147  109 LEU   B CD1 
5699 C CD2 . LEU   B 109 ? 0.1685 0.1347 0.2047 0.0062  0.0024  0.0145  109 LEU   B CD2 
5711 N N   . LYS   B 110 ? 0.1351 0.1210 0.1926 0.0026  0.0190  0.0221  110 LYS   B N   
5712 C CA  . LYS   B 110 ? 0.1310 0.1136 0.1977 0.0020  0.0107  0.0129  110 LYS   B CA  
5713 C C   . LYS   B 110 ? 0.1246 0.1161 0.1836 0.0008  0.0124  0.0100  110 LYS   B C   
5714 O O   . LYS   B 110 ? 0.1212 0.1198 0.1807 -0.0053 0.0056  0.0043  110 LYS   B O   
5715 C CB  . LYS   B 110 ? 0.1332 0.1173 0.2229 -0.0085 0.0122  0.0073  110 LYS   B CB  
5716 C CG  . LYS   B 110 ? 0.1346 0.1218 0.2237 -0.0065 0.0036  0.0144  110 LYS   B CG  
5717 C CD  . LYS   B 110 ? 0.1344 0.1259 0.2372 -0.0103 0.0002  0.0060  110 LYS   B CD  
5718 C CE  . LYS   B 110 ? 0.1336 0.1383 0.2495 -0.0052 -0.0016 -0.0014 110 LYS   B CE  
5719 N NZ  . LYS   B 110 ? 0.1380 0.1575 0.2433 0.0037  -0.0042 -0.0032 110 LYS   B NZ  
5733 N N   . SER   B 111 ? 0.1321 0.1201 0.1776 -0.0061 0.0153  0.0090  111 SER   B N   
5734 C CA  . SER   B 111 ? 0.1391 0.1208 0.1759 0.0011  0.0090  0.0103  111 SER   B CA  
5735 C C   . SER   B 111 ? 0.1281 0.1175 0.1696 -0.0025 0.0066  0.0032  111 SER   B C   
5736 O O   . SER   B 111 ? 0.1291 0.1215 0.1861 -0.0007 -0.0022 0.0081  111 SER   B O   
5737 C CB  . SER   B 111 ? 0.1551 0.1429 0.1891 0.0014  0.0234  0.0193  111 SER   B CB  
5738 O OG  . SER   B 111 ? 0.1740 0.1886 0.2111 0.0043  0.0376  0.0150  111 SER   B OG  
5744 N N   . ALA   B 112 ? 0.1205 0.1232 0.1782 0.0080  0.0118  0.0142  112 ALA   B N   
5745 C CA  . ALA   B 112 ? 0.1203 0.1270 0.1706 0.0027  0.0017  0.0008  112 ALA   B CA  
5746 C C   . ALA   B 112 ? 0.1170 0.1145 0.1548 0.0052  -0.0020 -0.0011 112 ALA   B C   
5747 O O   . ALA   B 112 ? 0.1179 0.1166 0.1633 -0.0043 -0.0006 0.0007  112 ALA   B O   
5748 C CB  . ALA   B 112 ? 0.1307 0.1322 0.1698 0.0070  -0.0066 0.0108  112 ALA   B CB  
5754 N N   . TYR   B 113 ? 0.1121 0.1072 0.1707 0.0013  -0.0032 0.0007  113 TYR   B N   
5755 C CA  . TYR   B 113 ? 0.1110 0.1047 0.1603 -0.0037 0.0022  -0.0053 113 TYR   B CA  
5756 C C   . TYR   B 113 ? 0.1107 0.1008 0.1642 -0.0069 -0.0006 -0.0057 113 TYR   B C   
5757 O O   . TYR   B 113 ? 0.1153 0.1069 0.1623 -0.0024 -0.0033 -0.0059 113 TYR   B O   
5758 C CB  . TYR   B 113 ? 0.1165 0.1025 0.1736 -0.0008 0.0040  0.0067  113 TYR   B CB  
5759 C CG  . TYR   B 113 ? 0.1190 0.1037 0.1763 -0.0024 -0.0043 0.0067  113 TYR   B CG  
5760 C CD1 . TYR   B 113 ? 0.1361 0.1023 0.1883 -0.0032 0.0036  0.0113  113 TYR   B CD1 
5761 C CD2 . TYR   B 113 ? 0.1246 0.1020 0.1908 -0.0054 -0.0043 0.0010  113 TYR   B CD2 
5762 C CE1 . TYR   B 113 ? 0.1286 0.1095 0.1815 0.0018  0.0080  0.0044  113 TYR   B CE1 
5763 C CE2 . TYR   B 113 ? 0.1295 0.1018 0.1889 0.0006  0.0001  0.0077  113 TYR   B CE2 
5764 C CZ  . TYR   B 113 ? 0.1234 0.1083 0.1931 0.0076  -0.0091 0.0019  113 TYR   B CZ  
5765 O OH  . TYR   B 113 ? 0.1331 0.1076 0.2097 0.0117  0.0006  0.0022  113 TYR   B OH  
5775 N N   . GLU   B 114 ? 0.1139 0.1010 0.1650 -0.0020 -0.0021 -0.0015 114 GLU   B N   
5776 C CA  . GLU   B 114 ? 0.1123 0.0990 0.1650 -0.0030 -0.0075 -0.0039 114 GLU   B CA  
5777 C C   . GLU   B 114 ? 0.1085 0.1019 0.1603 0.0054  -0.0005 -0.0024 114 GLU   B C   
5778 O O   . GLU   B 114 ? 0.1095 0.1056 0.1740 0.0044  -0.0064 0.0032  114 GLU   B O   
5779 C CB  . GLU   B 114 ? 0.1167 0.1049 0.1791 -0.0012 0.0004  0.0026  114 GLU   B CB  
5780 C CG  . GLU   B 114 ? 0.1167 0.1090 0.1825 -0.0016 0.0037  0.0053  114 GLU   B CG  
5781 C CD  . GLU   B 114 ? 0.1166 0.1098 0.1821 -0.0062 -0.0050 0.0050  114 GLU   B CD  
5782 O OE1 . GLU   B 114 ? 0.1155 0.1326 0.1883 -0.0080 0.0086  0.0015  114 GLU   B OE1 
5783 O OE2 . GLU   B 114 ? 0.1194 0.1308 0.2003 -0.0154 0.0027  0.0085  114 GLU   B OE2 
5790 N N   . ASN   B 115 ? 0.1141 0.0954 0.1656 -0.0007 -0.0058 0.0030  115 ASN   B N   
5791 C CA  . ASN   B 115 ? 0.1156 0.1036 0.1554 -0.0066 -0.0008 0.0016  115 ASN   B CA  
5792 C C   . ASN   B 115 ? 0.1082 0.1018 0.1523 -0.0094 -0.0069 0.0016  115 ASN   B C   
5793 O O   . ASN   B 115 ? 0.1215 0.1099 0.1630 -0.0120 -0.0034 0.0003  115 ASN   B O   
5794 C CB  . ASN   B 115 ? 0.1269 0.1147 0.1590 -0.0042 -0.0014 -0.0036 115 ASN   B CB  
5795 C CG  . ASN   B 115 ? 0.1350 0.1237 0.1588 0.0039  -0.0099 -0.0048 115 ASN   B CG  
5796 O OD1 . ASN   B 115 ? 0.1844 0.1364 0.1768 0.0009  0.0034  -0.0113 115 ASN   B OD1 
5797 N ND2 . ASN   B 115 ? 0.1285 0.1311 0.1577 -0.0069 -0.0046 0.0028  115 ASN   B ND2 
5804 N N   . PHE   B 116 ? 0.1123 0.1010 0.1377 -0.0006 -0.0046 0.0025  116 PHE   B N   
5805 C CA  . PHE   B 116 ? 0.1203 0.1043 0.1495 -0.0076 -0.0069 0.0043  116 PHE   B CA  
5806 C C   . PHE   B 116 ? 0.1239 0.0955 0.1522 -0.0081 -0.0088 0.0085  116 PHE   B C   
5807 O O   . PHE   B 116 ? 0.1208 0.1066 0.1545 -0.0005 -0.0064 0.0044  116 PHE   B O   
5808 C CB  . PHE   B 116 ? 0.1168 0.0985 0.1553 -0.0046 -0.0145 0.0017  116 PHE   B CB  
5809 C CG  . PHE   B 116 ? 0.1072 0.1071 0.1510 -0.0028 -0.0072 -0.0012 116 PHE   B CG  
5810 C CD1 . PHE   B 116 ? 0.1159 0.1073 0.1685 -0.0017 -0.0057 0.0035  116 PHE   B CD1 
5811 C CD2 . PHE   B 116 ? 0.1148 0.1131 0.1551 -0.0014 -0.0034 -0.0066 116 PHE   B CD2 
5812 C CE1 . PHE   B 116 ? 0.1214 0.1139 0.1620 -0.0025 -0.0177 -0.0005 116 PHE   B CE1 
5813 C CE2 . PHE   B 116 ? 0.1145 0.1155 0.1595 0.0049  -0.0007 -0.0005 116 PHE   B CE2 
5814 C CZ  . PHE   B 116 ? 0.1062 0.1154 0.1633 -0.0012 -0.0163 0.0045  116 PHE   B CZ  
5824 N N   . ASN   B 117 ? 0.1195 0.1010 0.1629 -0.0002 -0.0100 -0.0025 117 ASN   B N   
5825 C CA  . ASN   B 117 ? 0.1228 0.1029 0.1599 0.0057  -0.0076 -0.0018 117 ASN   B CA  
5826 C C   . ASN   B 117 ? 0.1230 0.1031 0.1767 0.0080  -0.0034 -0.0021 117 ASN   B C   
5827 O O   . ASN   B 117 ? 0.1364 0.1101 0.1985 0.0000  -0.0305 0.0025  117 ASN   B O   
5828 C CB  . ASN   B 117 ? 0.1242 0.1097 0.1575 0.0003  -0.0063 -0.0052 117 ASN   B CB  
5829 C CG  . ASN   B 117 ? 0.1228 0.1145 0.1671 0.0016  -0.0046 -0.0061 117 ASN   B CG  
5830 O OD1 . ASN   B 117 ? 0.1412 0.1119 0.1824 -0.0101 -0.0004 -0.0094 117 ASN   B OD1 
5831 N ND2 . ASN   B 117 ? 0.1243 0.1115 0.1648 -0.0013 0.0008  -0.0047 117 ASN   B ND2 
5838 N N   . GLN   B 118 ? 0.1230 0.0996 0.1687 -0.0041 -0.0210 -0.0062 118 GLN   B N   
5839 C CA  . GLN   B 118 ? 0.1258 0.1050 0.1762 0.0031  -0.0111 -0.0012 118 GLN   B CA  
5840 C C   . GLN   B 118 ? 0.1322 0.1046 0.1822 -0.0022 -0.0054 -0.0041 118 GLN   B C   
5841 O O   . GLN   B 118 ? 0.1545 0.1058 0.2149 -0.0056 -0.0015 -0.0012 118 GLN   B O   
5842 C CB  . GLN   B 118 ? 0.1342 0.1131 0.1783 -0.0014 -0.0196 -0.0055 118 GLN   B CB  
5843 C CG  . GLN   B 118 ? 0.1439 0.1158 0.1812 0.0027  -0.0088 -0.0147 118 GLN   B CG  
5844 C CD  . GLN   B 118 ? 0.1452 0.1082 0.1788 0.0027  -0.0076 -0.0165 118 GLN   B CD  
5845 O OE1 . GLN   B 118 ? 0.1549 0.1092 0.1977 0.0044  0.0035  0.0017  118 GLN   B OE1 
5846 N NE2 . GLN   B 118 ? 0.1517 0.1128 0.1933 0.0029  -0.0148 -0.0030 118 GLN   B NE2 
5855 N N   . HIS   B 119 ? 0.1321 0.1017 0.1573 -0.0069 -0.0090 0.0056  119 HIS   B N   
5856 C CA  . HIS   B 119 ? 0.1426 0.1146 0.1578 -0.0040 -0.0170 0.0044  119 HIS   B CA  
5857 C C   . HIS   B 119 ? 0.1442 0.1142 0.1523 -0.0002 -0.0266 0.0064  119 HIS   B C   
5858 O O   . HIS   B 119 ? 0.1570 0.1145 0.1714 -0.0213 -0.0163 0.0050  119 HIS   B O   
5859 C CB  . HIS   B 119 ? 0.1455 0.1324 0.1720 0.0015  -0.0231 -0.0062 119 HIS   B CB  
5860 C CG  . HIS   B 119 ? 0.1484 0.1563 0.1914 0.0119  -0.0337 -0.0225 119 HIS   B CG  
5861 N ND1 . HIS   B 119 ? 0.1668 0.1746 0.2146 0.0018  -0.0461 -0.0432 119 HIS   B ND1 
5862 C CD2 . HIS   B 119 ? 0.1641 0.1777 0.1964 0.0343  -0.0413 -0.0258 119 HIS   B CD2 
5863 C CE1 . HIS   B 119 ? 0.1838 0.1857 0.2234 0.0157  -0.0524 -0.0523 119 HIS   B CE1 
5864 N NE2 . HIS   B 119 ? 0.1833 0.2014 0.2081 0.0273  -0.0489 -0.0422 119 HIS   B NE2 
5872 N N   . GLU   B 120 ? 0.1597 0.1149 0.1569 -0.0060 -0.0311 0.0146  120 GLU   B N   
5873 C CA  . GLU   B 120 ? 0.1830 0.1312 0.1678 0.0011  -0.0443 0.0211  120 GLU   B CA  
5874 C C   . GLU   B 120 ? 0.1690 0.1193 0.1522 -0.0118 -0.0241 0.0238  120 GLU   B C   
5875 O O   . GLU   B 120 ? 0.1679 0.1304 0.1566 -0.0103 -0.0258 0.0057  120 GLU   B O   
5876 C CB  . GLU   B 120 ? 0.2492 0.1705 0.2335 0.0248  -0.0641 0.0536  120 GLU   B CB  
5877 C CG  . GLU   B 120 ? 0.3125 0.2492 0.3385 0.0415  -0.0853 0.0860  120 GLU   B CG  
5878 C CD  . GLU   B 120 ? 0.3603 0.3229 0.4500 0.0429  -0.0874 0.1057  120 GLU   B CD  
5879 O OE1 . GLU   B 120 ? 0.3777 0.3777 0.4888 0.0414  -0.0812 0.1224  120 GLU   B OE1 
5880 O OE2 . GLU   B 120 ? 0.3876 0.3573 0.5093 0.0394  -0.0851 0.0963  120 GLU   B OE2 
5887 N N   . VAL   B 121 ? 0.1578 0.1146 0.1544 -0.0140 -0.0145 0.0181  121 VAL   B N   
5888 C CA  . VAL   B 121 ? 0.1523 0.1276 0.1381 -0.0103 -0.0183 0.0135  121 VAL   B CA  
5889 C C   . VAL   B 121 ? 0.1438 0.1246 0.1380 -0.0208 -0.0176 0.0126  121 VAL   B C   
5890 O O   . VAL   B 121 ? 0.1512 0.1182 0.1641 -0.0268 -0.0219 0.0096  121 VAL   B O   
5891 C CB  . VAL   B 121 ? 0.1787 0.1650 0.1469 -0.0036 -0.0303 0.0139  121 VAL   B CB  
5892 C CG1 . VAL   B 121 ? 0.1882 0.1725 0.1866 -0.0101 -0.0109 0.0064  121 VAL   B CG1 
5893 C CG2 . VAL   B 121 ? 0.1985 0.1865 0.1593 0.0105  -0.0202 0.0085  121 VAL   B CG2 
5903 N N   . LEU   B 122 ? 0.1388 0.1191 0.1310 -0.0175 -0.0220 0.0110  122 LEU   B N   
5904 C CA  . LEU   B 122 ? 0.1294 0.1270 0.1318 -0.0193 -0.0177 0.0070  122 LEU   B CA  
5905 C C   . LEU   B 122 ? 0.1254 0.1099 0.1335 -0.0242 -0.0163 0.0112  122 LEU   B C   
5906 O O   . LEU   B 122 ? 0.1450 0.1149 0.1592 -0.0279 -0.0294 0.0029  122 LEU   B O   
5907 C CB  . LEU   B 122 ? 0.1453 0.1375 0.1639 -0.0016 -0.0213 0.0102  122 LEU   B CB  
5908 C CG  . LEU   B 122 ? 0.1387 0.1445 0.1580 -0.0111 -0.0068 0.0083  122 LEU   B CG  
5909 C CD1 . LEU   B 122 ? 0.1460 0.1693 0.1657 -0.0160 -0.0087 0.0080  122 LEU   B CD1 
5910 C CD2 . LEU   B 122 ? 0.1416 0.1480 0.1475 -0.0081 -0.0011 0.0003  122 LEU   B CD2 
5922 N N   . LEU   B 123 ? 0.1334 0.1005 0.1340 -0.0208 -0.0073 0.0052  123 LEU   B N   
5923 C CA  . LEU   B 123 ? 0.1308 0.1056 0.1418 -0.0200 -0.0151 0.0038  123 LEU   B CA  
5924 C C   . LEU   B 123 ? 0.1281 0.1011 0.1310 -0.0185 -0.0135 -0.0004 123 LEU   B C   
5925 O O   . LEU   B 123 ? 0.1419 0.1098 0.1425 -0.0291 -0.0164 0.0004  123 LEU   B O   
5926 C CB  . LEU   B 123 ? 0.1414 0.1103 0.1472 -0.0177 -0.0093 0.0023  123 LEU   B CB  
5927 C CG  . LEU   B 123 ? 0.1368 0.1173 0.1567 -0.0116 -0.0015 0.0119  123 LEU   B CG  
5928 C CD1 . LEU   B 123 ? 0.1406 0.1234 0.1641 -0.0116 0.0035  -0.0057 123 LEU   B CD1 
5929 C CD2 . LEU   B 123 ? 0.1462 0.1180 0.1808 -0.0087 0.0026  0.0166  123 LEU   B CD2 
5941 N N   . ALA   B 124 ? 0.1300 0.1012 0.1295 -0.0179 -0.0082 -0.0031 124 ALA   B N   
5942 C CA  . ALA   B 124 ? 0.1252 0.1048 0.1415 -0.0113 -0.0110 -0.0073 124 ALA   B CA  
5943 C C   . ALA   B 124 ? 0.1179 0.1023 0.1437 -0.0125 -0.0128 -0.0033 124 ALA   B C   
5944 O O   . ALA   B 124 ? 0.1305 0.1091 0.1448 -0.0120 -0.0123 -0.0030 124 ALA   B O   
5945 C CB  . ALA   B 124 ? 0.1269 0.1135 0.1524 -0.0051 0.0025  0.0025  124 ALA   B CB  
5951 N N   . PRO   B 125 ? 0.1305 0.1108 0.1274 -0.0120 -0.0173 0.0056  125 PRO   B N   
5952 C CA  . PRO   B 125 ? 0.1379 0.1123 0.1515 -0.0103 -0.0167 0.0195  125 PRO   B CA  
5953 C C   . PRO   B 125 ? 0.1275 0.1057 0.1632 -0.0112 -0.0123 0.0055  125 PRO   B C   
5954 O O   . PRO   B 125 ? 0.1314 0.1057 0.1807 -0.0104 -0.0049 0.0144  125 PRO   B O   
5955 C CB  . PRO   B 125 ? 0.1420 0.1376 0.1649 -0.0173 -0.0256 0.0264  125 PRO   B CB  
5956 C CG  . PRO   B 125 ? 0.1496 0.1441 0.1526 -0.0266 -0.0272 0.0139  125 PRO   B CG  
5957 C CD  . PRO   B 125 ? 0.1409 0.1227 0.1389 -0.0261 -0.0183 0.0040  125 PRO   B CD  
5965 N N   . LEU   B 126 ? 0.1369 0.1014 0.1773 -0.0125 0.0041  0.0107  126 LEU   B N   
5966 C CA  . LEU   B 126 ? 0.1445 0.1100 0.1782 -0.0126 0.0080  0.0134  126 LEU   B CA  
5967 C C   . LEU   B 126 ? 0.1390 0.1214 0.1746 0.0003  0.0065  0.0156  126 LEU   B C   
5968 O O   . LEU   B 126 ? 0.1600 0.1510 0.1964 0.0178  -0.0103 -0.0060 126 LEU   B O   
5969 C CB  . LEU   B 126 ? 0.1575 0.1153 0.2066 -0.0163 0.0199  0.0067  126 LEU   B CB  
5970 C CG  . LEU   B 126 ? 0.1770 0.1308 0.2203 -0.0275 0.0179  -0.0100 126 LEU   B CG  
5971 C CD1 . LEU   B 126 ? 0.1887 0.1322 0.2617 -0.0266 0.0129  -0.0153 126 LEU   B CD1 
5972 C CD2 . LEU   B 126 ? 0.1808 0.1382 0.2169 -0.0329 0.0062  -0.0052 126 LEU   B CD2 
5984 N N   . LEU   B 127 ? 0.1316 0.1110 0.1775 0.0029  0.0090  0.0093  127 LEU   B N   
5985 C CA  . LEU   B 127 ? 0.1249 0.1219 0.1843 -0.0081 0.0141  0.0137  127 LEU   B CA  
5986 C C   . LEU   B 127 ? 0.1282 0.1163 0.1797 -0.0022 0.0073  0.0114  127 LEU   B C   
5987 O O   . LEU   B 127 ? 0.1367 0.1237 0.1856 -0.0161 -0.0022 0.0143  127 LEU   B O   
5988 C CB  . LEU   B 127 ? 0.1410 0.1205 0.1921 -0.0049 0.0091  0.0176  127 LEU   B CB  
5989 C CG  . LEU   B 127 ? 0.1541 0.1233 0.2018 -0.0026 0.0081  0.0147  127 LEU   B CG  
5990 C CD1 . LEU   B 127 ? 0.1539 0.1285 0.1993 0.0010  -0.0025 0.0074  127 LEU   B CD1 
5991 C CD2 . LEU   B 127 ? 0.1594 0.1339 0.2117 -0.0113 0.0117  0.0279  127 LEU   B CD2 
6003 N N   . SER   B 128 ? 0.1336 0.1146 0.1737 0.0008  -0.0088 0.0127  128 SER   B N   
6004 C CA  . SER   B 128 ? 0.1457 0.1250 0.1812 0.0094  -0.0168 0.0120  128 SER   B CA  
6005 C C   . SER   B 128 ? 0.1549 0.1266 0.1983 0.0080  -0.0301 0.0127  128 SER   B C   
6006 O O   . SER   B 128 ? 0.1760 0.1291 0.2326 0.0086  -0.0291 0.0256  128 SER   B O   
6007 C CB  . SER   B 128 ? 0.1567 0.1267 0.1772 0.0113  -0.0069 0.0198  128 SER   B CB  
6008 O OG  . SER   B 128 ? 0.1673 0.1380 0.1926 0.0103  0.0025  0.0243  128 SER   B OG  
6014 N N   . ALA   B 129 ? 0.1699 0.1296 0.2133 0.0231  -0.0158 0.0001  129 ALA   B N   
6015 C CA  . ALA   B 129 ? 0.1880 0.1430 0.2356 0.0283  -0.0145 -0.0113 129 ALA   B CA  
6016 C C   . ALA   B 129 ? 0.1758 0.1337 0.2263 0.0237  0.0041  -0.0006 129 ALA   B C   
6017 O O   . ALA   B 129 ? 0.1626 0.1381 0.2289 0.0193  -0.0064 0.0133  129 ALA   B O   
6018 C CB  . ALA   B 129 ? 0.2069 0.1633 0.2630 0.0311  -0.0099 -0.0182 129 ALA   B CB  
6024 N N   . GLY   B 130 ? 0.1715 0.1295 0.2283 0.0267  0.0122  -0.0050 130 GLY   B N   
6025 C CA  . GLY   B 130 ? 0.1768 0.1436 0.2377 0.0199  0.0328  -0.0020 130 GLY   B CA  
6026 C C   . GLY   B 130 ? 0.1767 0.1426 0.2333 0.0145  0.0149  0.0060  130 GLY   B C   
6027 O O   . GLY   B 130 ? 0.1934 0.1524 0.2340 0.0178  0.0076  0.0122  130 GLY   B O   
6031 N N   . ILE   B 131 ? 0.1641 0.1603 0.2335 0.0291  0.0101  0.0014  131 ILE   B N   
6032 C CA  . ILE   B 131 ? 0.1769 0.1786 0.2302 0.0262  -0.0038 0.0165  131 ILE   B CA  
6033 C C   . ILE   B 131 ? 0.1924 0.1734 0.2073 0.0212  -0.0103 0.0208  131 ILE   B C   
6034 O O   . ILE   B 131 ? 0.2246 0.1835 0.2109 0.0271  -0.0252 0.0205  131 ILE   B O   
6035 C CB  . ILE   B 131 ? 0.1758 0.2179 0.2601 0.0261  -0.0136 0.0224  131 ILE   B CB  
6036 C CG1 . ILE   B 131 ? 0.1861 0.2355 0.2687 0.0051  -0.0071 0.0260  131 ILE   B CG1 
6037 C CG2 . ILE   B 131 ? 0.1709 0.2351 0.2763 0.0331  -0.0097 0.0129  131 ILE   B CG2 
6038 C CD1 . ILE   B 131 ? 0.2038 0.2527 0.2836 -0.0100 -0.0145 0.0265  131 ILE   B CD1 
6050 N N   . PHE   B 132 ? 0.1724 0.1479 0.1949 0.0176  0.0016  0.0207  132 PHE   B N   
6051 C CA  . PHE   B 132 ? 0.1833 0.1517 0.1885 0.0065  0.0133  0.0142  132 PHE   B CA  
6052 C C   . PHE   B 132 ? 0.2004 0.1641 0.1989 0.0105  0.0156  0.0145  132 PHE   B C   
6053 O O   . PHE   B 132 ? 0.2229 0.1821 0.2250 0.0102  0.0274  0.0193  132 PHE   B O   
6054 C CB  . PHE   B 132 ? 0.1682 0.1472 0.1792 0.0089  0.0140  0.0209  132 PHE   B CB  
6055 C CG  . PHE   B 132 ? 0.1660 0.1479 0.1805 0.0183  0.0165  0.0155  132 PHE   B CG  
6056 C CD1 . PHE   B 132 ? 0.1736 0.1531 0.2207 0.0141  0.0242  0.0174  132 PHE   B CD1 
6057 C CD2 . PHE   B 132 ? 0.1711 0.1493 0.1673 0.0268  0.0128  0.0258  132 PHE   B CD2 
6058 C CE1 . PHE   B 132 ? 0.1785 0.1615 0.2339 0.0114  0.0192  0.0220  132 PHE   B CE1 
6059 C CE2 . PHE   B 132 ? 0.1775 0.1588 0.1647 0.0211  0.0112  0.0181  132 PHE   B CE2 
6060 C CZ  . PHE   B 132 ? 0.1812 0.1588 0.2123 0.0096  0.0010  0.0276  132 PHE   B CZ  
6070 N N   . GLY   B 133 ? 0.1954 0.1487 0.1871 0.0116  0.0092  0.0283  133 GLY   B N   
6071 C CA  . GLY   B 133 ? 0.2107 0.1596 0.1989 -0.0095 0.0051  0.0343  133 GLY   B CA  
6072 C C   . GLY   B 133 ? 0.2155 0.1659 0.2033 -0.0218 0.0150  0.0315  133 GLY   B C   
6073 O O   . GLY   B 133 ? 0.2326 0.1789 0.2506 -0.0350 0.0204  0.0479  133 GLY   B O   
6077 N N   . ALA   B 134 ? 0.2006 0.1663 0.1931 -0.0270 0.0125  0.0131  134 ALA   B N   
6078 C CA  . ALA   B 134 ? 0.1935 0.1608 0.2104 -0.0200 0.0265  0.0017  134 ALA   B CA  
6079 C C   . ALA   B 134 ? 0.2030 0.1574 0.2129 -0.0116 0.0248  0.0066  134 ALA   B C   
6080 O O   . ALA   B 134 ? 0.2078 0.1788 0.2325 -0.0016 0.0197  -0.0012 134 ALA   B O   
6081 C CB  . ALA   B 134 ? 0.1875 0.1581 0.2394 -0.0136 0.0146  -0.0091 134 ALA   B CB  
6087 N N   . ASP   B 135 ? 0.2145 0.1460 0.2114 -0.0124 0.0097  0.0150  135 ASP   B N   
6088 C CA  . ASP   B 135 ? 0.2289 0.1411 0.2207 -0.0115 -0.0081 0.0222  135 ASP   B CA  
6089 C C   . ASP   B 135 ? 0.2121 0.1337 0.2138 -0.0041 -0.0021 0.0176  135 ASP   B C   
6090 O O   . ASP   B 135 ? 0.2007 0.1277 0.2270 -0.0056 -0.0002 0.0282  135 ASP   B O   
6091 C CB  . ASP   B 135 ? 0.2570 0.1545 0.2461 -0.0323 -0.0033 0.0263  135 ASP   B CB  
6092 C CG  . ASP   B 135 ? 0.2859 0.1568 0.2872 -0.0459 -0.0032 0.0201  135 ASP   B CG  
6093 O OD1 . ASP   B 135 ? 0.2959 0.1447 0.2901 -0.0345 -0.0079 0.0213  135 ASP   B OD1 
6094 O OD2 . ASP   B 135 ? 0.3115 0.1921 0.3500 -0.0550 -0.0050 -0.0061 135 ASP   B OD2 
6099 N N   . PRO   B 136 ? 0.2058 0.1343 0.2199 0.0177  -0.0125 0.0165  136 PRO   B N   
6100 C CA  . PRO   B 136 ? 0.1842 0.1281 0.2195 0.0173  -0.0165 0.0017  136 PRO   B CA  
6101 C C   . PRO   B 136 ? 0.1713 0.1143 0.2278 0.0156  -0.0083 0.0018  136 PRO   B C   
6102 O O   . PRO   B 136 ? 0.1544 0.1122 0.2359 0.0097  -0.0108 0.0058  136 PRO   B O   
6103 C CB  . PRO   B 136 ? 0.1910 0.1591 0.2338 0.0264  -0.0262 -0.0067 136 PRO   B CB  
6104 C CG  . PRO   B 136 ? 0.2109 0.1626 0.2452 0.0337  -0.0178 -0.0037 136 PRO   B CG  
6105 C CD  . PRO   B 136 ? 0.2129 0.1543 0.2371 0.0395  -0.0121 0.0070  136 PRO   B CD  
6113 N N   . ILE   B 137 ? 0.1812 0.1118 0.2334 0.0163  -0.0151 0.0050  137 ILE   B N   
6114 C CA  . ILE   B 137 ? 0.1881 0.1161 0.2485 -0.0027 -0.0122 -0.0016 137 ILE   B CA  
6115 C C   . ILE   B 137 ? 0.1778 0.1189 0.2429 -0.0101 -0.0065 0.0091  137 ILE   B C   
6116 O O   . ILE   B 137 ? 0.1657 0.1164 0.2388 -0.0102 -0.0080 0.0027  137 ILE   B O   
6117 C CB  . ILE   B 137 ? 0.2137 0.1196 0.2969 0.0014  -0.0193 0.0010  137 ILE   B CB  
6118 C CG1 . ILE   B 137 ? 0.2399 0.1404 0.3461 0.0077  -0.0120 -0.0157 137 ILE   B CG1 
6119 C CG2 . ILE   B 137 ? 0.2209 0.1251 0.3146 -0.0217 -0.0227 0.0043  137 ILE   B CG2 
6120 C CD1 . ILE   B 137 ? 0.2663 0.1636 0.3858 0.0235  -0.0154 -0.0024 137 ILE   B CD1 
6132 N N   . HIS   B 138 ? 0.1837 0.1111 0.2311 -0.0062 -0.0004 0.0121  138 HIS   B N   
6133 C CA  . HIS   B 138 ? 0.1856 0.1234 0.2302 -0.0026 0.0188  0.0069  138 HIS   B CA  
6134 C C   . HIS   B 138 ? 0.1672 0.1230 0.2240 -0.0044 0.0141  0.0128  138 HIS   B C   
6135 O O   . HIS   B 138 ? 0.1555 0.1282 0.2466 0.0004  0.0150  0.0293  138 HIS   B O   
6136 C CB  . HIS   B 138 ? 0.2114 0.1384 0.2493 -0.0047 0.0448  0.0029  138 HIS   B CB  
6137 C CG  . HIS   B 138 ? 0.2314 0.1542 0.2593 -0.0023 0.0603  0.0218  138 HIS   B CG  
6138 N ND1 . HIS   B 138 ? 0.2438 0.1748 0.2847 0.0051  0.0643  0.0233  138 HIS   B ND1 
6139 C CD2 . HIS   B 138 ? 0.2460 0.1619 0.2553 -0.0048 0.0695  0.0099  138 HIS   B CD2 
6140 C CE1 . HIS   B 138 ? 0.2487 0.1720 0.2844 0.0087  0.0661  0.0283  138 HIS   B CE1 
6141 N NE2 . HIS   B 138 ? 0.2578 0.1617 0.2751 0.0099  0.0667  0.0132  138 HIS   B NE2 
6149 N N   . SER   B 139 ? 0.1663 0.1102 0.2146 0.0026  0.0108  0.0037  139 SER   B N   
6150 C CA  . SER   B 139 ? 0.1614 0.1054 0.2014 0.0006  0.0055  -0.0022 139 SER   B CA  
6151 C C   . SER   B 139 ? 0.1399 0.1020 0.1980 -0.0013 -0.0021 -0.0051 139 SER   B C   
6152 O O   . SER   B 139 ? 0.1398 0.1038 0.2040 -0.0007 -0.0105 0.0022  139 SER   B O   
6153 C CB  . SER   B 139 ? 0.1708 0.1072 0.2081 0.0004  -0.0046 0.0008  139 SER   B CB  
6154 O OG  . SER   B 139 ? 0.1706 0.1128 0.2138 -0.0041 -0.0205 0.0056  139 SER   B OG  
6160 N N   . LEU   B 140 ? 0.1385 0.1028 0.1936 -0.0028 -0.0011 -0.0065 140 LEU   B N   
6161 C CA  . LEU   B 140 ? 0.1347 0.1011 0.1986 -0.0007 0.0058  -0.0021 140 LEU   B CA  
6162 C C   . LEU   B 140 ? 0.1353 0.1031 0.2117 -0.0044 -0.0063 -0.0023 140 LEU   B C   
6163 O O   . LEU   B 140 ? 0.1352 0.1052 0.2172 -0.0022 -0.0108 -0.0034 140 LEU   B O   
6164 C CB  . LEU   B 140 ? 0.1357 0.1039 0.2175 -0.0060 0.0114  -0.0101 140 LEU   B CB  
6165 C CG  . LEU   B 140 ? 0.1463 0.1088 0.2062 -0.0116 0.0007  -0.0007 140 LEU   B CG  
6166 C CD1 . LEU   B 140 ? 0.1604 0.1113 0.2101 -0.0130 0.0088  -0.0047 140 LEU   B CD1 
6167 C CD2 . LEU   B 140 ? 0.1619 0.1175 0.2117 -0.0088 -0.0053 -0.0110 140 LEU   B CD2 
6179 N N   . ARG   B 141 ? 0.1291 0.1069 0.2183 -0.0075 0.0021  -0.0025 141 ARG   B N   
6180 C CA  . ARG   B 141 ? 0.1288 0.1059 0.2582 -0.0092 0.0173  -0.0024 141 ARG   B CA  
6181 C C   . ARG   B 141 ? 0.1259 0.1094 0.2367 -0.0150 0.0030  -0.0061 141 ARG   B C   
6182 O O   . ARG   B 141 ? 0.1354 0.1148 0.2358 -0.0077 -0.0096 -0.0139 141 ARG   B O   
6183 C CB  . ARG   B 141 ? 0.1553 0.1204 0.3025 -0.0168 0.0255  -0.0086 141 ARG   B CB  
6184 C CG  . ARG   B 141 ? 0.1973 0.1514 0.3377 -0.0195 0.0419  0.0043  141 ARG   B CG  
6185 C CD  . ARG   B 141 ? 0.2548 0.1711 0.3553 -0.0085 0.0299  -0.0068 141 ARG   B CD  
6186 N NE  . ARG   B 141 ? 0.2883 0.1736 0.3634 -0.0271 0.0292  -0.0076 141 ARG   B NE  
6187 C CZ  . ARG   B 141 ? 0.3028 0.1620 0.3634 -0.0255 0.0395  -0.0218 141 ARG   B CZ  
6188 N NH1 . ARG   B 141 ? 0.3077 0.1558 0.3634 -0.0293 0.0431  -0.0283 141 ARG   B NH1 
6189 N NH2 . ARG   B 141 ? 0.3219 0.1748 0.3703 -0.0085 0.0272  -0.0180 141 ARG   B NH2 
6203 N N   . VAL   B 142 ? 0.1319 0.1047 0.2256 -0.0038 0.0042  -0.0107 142 VAL   B N   
6204 C CA  . VAL   B 142 ? 0.1283 0.1089 0.2218 -0.0031 0.0046  -0.0110 142 VAL   B CA  
6205 C C   . VAL   B 142 ? 0.1276 0.1058 0.2154 0.0033  0.0003  -0.0112 142 VAL   B C   
6206 O O   . VAL   B 142 ? 0.1324 0.1078 0.2358 0.0023  -0.0039 -0.0080 142 VAL   B O   
6207 C CB  . VAL   B 142 ? 0.1417 0.1182 0.2216 0.0018  0.0051  0.0003  142 VAL   B CB  
6208 C CG1 . VAL   B 142 ? 0.1397 0.1119 0.2314 0.0097  0.0109  -0.0042 142 VAL   B CG1 
6209 C CG2 . VAL   B 142 ? 0.1687 0.1181 0.2240 0.0020  0.0043  0.0023  142 VAL   B CG2 
6219 N N   . CYS   B 143 ? 0.1261 0.1008 0.2023 0.0004  -0.0055 0.0001  143 CYS   B N   
6220 C CA  . CYS   B 143 ? 0.1258 0.1034 0.2088 -0.0013 -0.0109 -0.0008 143 CYS   B CA  
6221 C C   . CYS   B 143 ? 0.1201 0.1081 0.2079 -0.0019 -0.0060 -0.0047 143 CYS   B C   
6222 O O   . CYS   B 143 ? 0.1253 0.1102 0.2065 -0.0012 -0.0102 -0.0063 143 CYS   B O   
6223 C CB  . CYS   B 143 ? 0.1317 0.1152 0.2105 -0.0042 -0.0113 -0.0083 143 CYS   B CB  
6224 S SG  . CYS   B 143 ? 0.1338 0.1336 0.1990 -0.0013 -0.0025 -0.0000 143 CYS   B SG  
6230 N N   . VAL   B 144 ? 0.1251 0.1110 0.2176 -0.0041 -0.0119 -0.0196 144 VAL   B N   
6231 C CA  . VAL   B 144 ? 0.1326 0.1206 0.2435 -0.0167 -0.0171 -0.0264 144 VAL   B CA  
6232 C C   . VAL   B 144 ? 0.1327 0.1207 0.2408 -0.0101 -0.0215 -0.0066 144 VAL   B C   
6233 O O   . VAL   B 144 ? 0.1405 0.1396 0.2556 0.0018  -0.0166 0.0113  144 VAL   B O   
6234 C CB  . VAL   B 144 ? 0.1629 0.1377 0.3045 -0.0092 -0.0241 -0.0342 144 VAL   B CB  
6235 C CG1 . VAL   B 144 ? 0.1859 0.1773 0.3431 -0.0040 -0.0347 -0.0320 144 VAL   B CG1 
6236 C CG2 . VAL   B 144 ? 0.1791 0.1358 0.2935 -0.0006 -0.0349 -0.0418 144 VAL   B CG2 
6246 N N   . ASP   B 145 ? 0.1323 0.1143 0.2455 -0.0069 -0.0185 -0.0145 145 ASP   B N   
6247 C CA  . ASP   B 145 ? 0.1250 0.1183 0.2640 -0.0057 -0.0101 -0.0114 145 ASP   B CA  
6248 C C   . ASP   B 145 ? 0.1215 0.1237 0.2481 -0.0056 -0.0032 -0.0082 145 ASP   B C   
6249 O O   . ASP   B 145 ? 0.1265 0.1367 0.3085 -0.0097 0.0005  -0.0247 145 ASP   B O   
6250 C CB  . ASP   B 145 ? 0.1441 0.1257 0.3065 -0.0102 0.0065  -0.0024 145 ASP   B CB  
6251 C CG  . ASP   B 145 ? 0.1652 0.1356 0.3525 -0.0248 0.0176  -0.0019 145 ASP   B CG  
6252 O OD1 . ASP   B 145 ? 0.1727 0.1416 0.3686 -0.0273 -0.0103 -0.0210 145 ASP   B OD1 
6253 O OD2 . ASP   B 145 ? 0.1981 0.1505 0.4006 -0.0292 0.0407  0.0087  145 ASP   B OD2 
6258 N N   . THR   B 146 ? 0.1182 0.1162 0.2069 -0.0061 -0.0017 -0.0008 146 THR   B N   
6259 C CA  . THR   B 146 ? 0.1263 0.1076 0.2060 -0.0099 -0.0001 -0.0105 146 THR   B CA  
6260 C C   . THR   B 146 ? 0.1204 0.1025 0.1994 -0.0055 -0.0117 -0.0056 146 THR   B C   
6261 O O   . THR   B 146 ? 0.1309 0.1100 0.2039 -0.0036 -0.0097 -0.0039 146 THR   B O   
6262 C CB  . THR   B 146 ? 0.1296 0.1054 0.2110 -0.0045 0.0048  -0.0034 146 THR   B CB  
6263 O OG1 . THR   B 146 ? 0.1353 0.1070 0.2155 -0.0012 0.0028  0.0062  146 THR   B OG1 
6264 C CG2 . THR   B 146 ? 0.1445 0.1147 0.1953 -0.0036 0.0024  0.0004  146 THR   B CG2 
6272 N N   . VAL   B 147 ? 0.1269 0.1109 0.1892 -0.0034 0.0023  -0.0018 147 VAL   B N   
6273 C CA  . VAL   B 147 ? 0.1278 0.1089 0.1814 -0.0089 -0.0054 -0.0024 147 VAL   B CA  
6274 C C   . VAL   B 147 ? 0.1243 0.1070 0.1986 -0.0140 -0.0131 -0.0019 147 VAL   B C   
6275 O O   . VAL   B 147 ? 0.1377 0.1176 0.1931 -0.0172 -0.0303 -0.0108 147 VAL   B O   
6276 C CB  . VAL   B 147 ? 0.1312 0.1201 0.1791 -0.0035 -0.0145 -0.0008 147 VAL   B CB  
6277 C CG1 . VAL   B 147 ? 0.1331 0.1367 0.1793 -0.0058 -0.0163 0.0031  147 VAL   B CG1 
6278 C CG2 . VAL   B 147 ? 0.1352 0.1168 0.1842 -0.0100 -0.0119 -0.0017 147 VAL   B CG2 
6288 N N   . ARG   B 148 ? 0.1300 0.1067 0.1961 -0.0076 -0.0230 -0.0081 148 ARG   B N   
6289 C CA  . ARG   B 148 ? 0.1297 0.1158 0.1877 -0.0055 -0.0286 -0.0102 148 ARG   B CA  
6290 C C   . ARG   B 148 ? 0.1394 0.1293 0.1741 -0.0064 -0.0308 -0.0052 148 ARG   B C   
6291 O O   . ARG   B 148 ? 0.1566 0.1551 0.1801 -0.0183 -0.0379 0.0033  148 ARG   B O   
6292 C CB  . ARG   B 148 ? 0.1402 0.1287 0.1994 -0.0008 -0.0377 -0.0226 148 ARG   B CB  
6293 C CG  . ARG   B 148 ? 0.1391 0.1429 0.2095 -0.0074 -0.0246 -0.0313 148 ARG   B CG  
6294 C CD  . ARG   B 148 ? 0.1478 0.1628 0.2091 0.0058  -0.0300 -0.0356 148 ARG   B CD  
6295 N NE  . ARG   B 148 ? 0.1489 0.1577 0.2001 0.0255  -0.0317 -0.0315 148 ARG   B NE  
6296 C CZ  . ARG   B 148 ? 0.1415 0.1498 0.1811 0.0182  -0.0300 -0.0226 148 ARG   B CZ  
6297 N NH1 . ARG   B 148 ? 0.1342 0.1556 0.1944 0.0012  -0.0142 -0.0149 148 ARG   B NH1 
6298 N NH2 . ARG   B 148 ? 0.1631 0.1405 0.1868 0.0182  -0.0211 -0.0184 148 ARG   B NH2 
6312 N N   . THR   B 149 ? 0.1393 0.1228 0.1726 -0.0089 -0.0292 -0.0017 149 THR   B N   
6313 C CA  . THR   B 149 ? 0.1439 0.1263 0.1693 -0.0114 -0.0286 0.0031  149 THR   B CA  
6314 C C   . THR   B 149 ? 0.1427 0.1217 0.1695 -0.0109 -0.0292 0.0019  149 THR   B C   
6315 O O   . THR   B 149 ? 0.1499 0.1190 0.1692 -0.0163 -0.0190 -0.0010 149 THR   B O   
6316 C CB  . THR   B 149 ? 0.1479 0.1259 0.1766 -0.0164 -0.0304 -0.0001 149 THR   B CB  
6317 O OG1 . THR   B 149 ? 0.1523 0.1284 0.1669 -0.0212 -0.0306 -0.0007 149 THR   B OG1 
6318 C CG2 . THR   B 149 ? 0.1538 0.1255 0.1823 -0.0027 -0.0178 -0.0018 149 THR   B CG2 
6326 N N   . ASN   B 150 ? 0.1517 0.1200 0.1655 -0.0095 -0.0299 -0.0006 150 ASN   B N   
6327 C CA  . ASN   B 150 ? 0.1574 0.1326 0.1630 -0.0142 -0.0298 -0.0046 150 ASN   B CA  
6328 C C   . ASN   B 150 ? 0.1447 0.1243 0.1700 -0.0107 -0.0239 -0.0005 150 ASN   B C   
6329 O O   . ASN   B 150 ? 0.1559 0.1276 0.1897 -0.0194 -0.0491 -0.0024 150 ASN   B O   
6330 C CB  . ASN   B 150 ? 0.1825 0.1648 0.1754 -0.0168 -0.0349 0.0034  150 ASN   B CB  
6331 C CG  . ASN   B 150 ? 0.2076 0.2101 0.1996 -0.0159 -0.0372 0.0174  150 ASN   B CG  
6332 O OD1 . ASN   B 150 ? 0.2156 0.2306 0.2129 -0.0273 -0.0583 0.0107  150 ASN   B OD1 
6333 N ND2 . ASN   B 150 ? 0.2169 0.2314 0.2335 -0.0081 -0.0379 0.0458  150 ASN   B ND2 
6340 N N   . VAL   B 151 ? 0.1359 0.1196 0.1683 -0.0158 -0.0257 0.0008  151 VAL   B N   
6341 C CA  . VAL   B 151 ? 0.1350 0.1270 0.1671 -0.0181 -0.0224 -0.0009 151 VAL   B CA  
6342 C C   . VAL   B 151 ? 0.1407 0.1167 0.1628 -0.0222 -0.0279 -0.0063 151 VAL   B C   
6343 O O   . VAL   B 151 ? 0.1503 0.1301 0.1820 -0.0226 -0.0202 -0.0111 151 VAL   B O   
6344 C CB  . VAL   B 151 ? 0.1569 0.1407 0.1760 -0.0049 -0.0178 -0.0086 151 VAL   B CB  
6345 C CG1 . VAL   B 151 ? 0.1692 0.1387 0.1937 -0.0072 0.0038  -0.0199 151 VAL   B CG1 
6346 C CG2 . VAL   B 151 ? 0.1703 0.1531 0.1779 0.0081  -0.0244 0.0062  151 VAL   B CG2 
6356 N N   . TYR   B 152 ? 0.1398 0.1056 0.1586 -0.0154 -0.0242 -0.0046 152 TYR   B N   
6357 C CA  . TYR   B 152 ? 0.1422 0.1157 0.1555 -0.0209 -0.0140 -0.0045 152 TYR   B CA  
6358 C C   . TYR   B 152 ? 0.1383 0.1093 0.1496 -0.0206 -0.0146 -0.0064 152 TYR   B C   
6359 O O   . TYR   B 152 ? 0.1477 0.1133 0.1523 -0.0259 -0.0149 0.0008  152 TYR   B O   
6360 C CB  . TYR   B 152 ? 0.1501 0.1282 0.1590 -0.0169 -0.0091 0.0064  152 TYR   B CB  
6361 C CG  . TYR   B 152 ? 0.1722 0.1383 0.1599 -0.0336 -0.0175 0.0055  152 TYR   B CG  
6362 C CD1 . TYR   B 152 ? 0.1796 0.1533 0.1563 -0.0201 -0.0285 0.0146  152 TYR   B CD1 
6363 C CD2 . TYR   B 152 ? 0.1939 0.1490 0.1578 -0.0286 -0.0189 -0.0034 152 TYR   B CD2 
6364 C CE1 . TYR   B 152 ? 0.1977 0.1680 0.1653 -0.0183 -0.0336 0.0247  152 TYR   B CE1 
6365 C CE2 . TYR   B 152 ? 0.2090 0.1749 0.1720 -0.0285 -0.0266 0.0022  152 TYR   B CE2 
6366 C CZ  . TYR   B 152 ? 0.2077 0.1846 0.1586 -0.0239 -0.0472 0.0174  152 TYR   B CZ  
6367 O OH  . TYR   B 152 ? 0.2260 0.2155 0.1843 -0.0118 -0.0442 0.0195  152 TYR   B OH  
6377 N N   . LEU   B 153 ? 0.1417 0.1112 0.1498 -0.0211 -0.0151 -0.0058 153 LEU   B N   
6378 C CA  . LEU   B 153 ? 0.1418 0.1094 0.1429 -0.0149 -0.0086 -0.0060 153 LEU   B CA  
6379 C C   . LEU   B 153 ? 0.1373 0.1083 0.1624 -0.0209 -0.0119 -0.0121 153 LEU   B C   
6380 O O   . LEU   B 153 ? 0.1476 0.1291 0.1777 -0.0135 -0.0188 -0.0281 153 LEU   B O   
6381 C CB  . LEU   B 153 ? 0.1394 0.1075 0.1629 -0.0213 -0.0070 -0.0047 153 LEU   B CB  
6382 C CG  . LEU   B 153 ? 0.1369 0.1161 0.1840 -0.0195 -0.0057 -0.0081 153 LEU   B CG  
6383 C CD1 . LEU   B 153 ? 0.1463 0.1320 0.1911 -0.0261 0.0029  0.0015  153 LEU   B CD1 
6384 C CD2 . LEU   B 153 ? 0.1382 0.1262 0.1882 -0.0190 0.0015  -0.0024 153 LEU   B CD2 
6396 N N   . ALA   B 154 ? 0.1386 0.1071 0.1586 -0.0080 -0.0168 -0.0063 154 ALA   B N   
6397 C CA  . ALA   B 154 ? 0.1445 0.1182 0.1765 -0.0014 -0.0178 -0.0191 154 ALA   B CA  
6398 C C   . ALA   B 154 ? 0.1581 0.1191 0.1763 0.0013  -0.0269 -0.0268 154 ALA   B C   
6399 O O   . ALA   B 154 ? 0.1879 0.1258 0.1943 0.0061  -0.0191 -0.0120 154 ALA   B O   
6400 C CB  . ALA   B 154 ? 0.1458 0.1395 0.2047 -0.0037 -0.0156 -0.0216 154 ALA   B CB  
6406 N N   . VAL   B 155 ? 0.1331 0.1124 0.1839 -0.0029 -0.0098 -0.0141 155 VAL   B N   
6407 C CA  . VAL   B 155 ? 0.1294 0.1091 0.1977 -0.0029 -0.0129 -0.0061 155 VAL   B CA  
6408 C C   . VAL   B 155 ? 0.1309 0.1121 0.1931 0.0028  -0.0160 -0.0098 155 VAL   B C   
6409 O O   . VAL   B 155 ? 0.1470 0.1320 0.2160 0.0067  -0.0141 -0.0254 155 VAL   B O   
6410 C CB  . VAL   B 155 ? 0.1373 0.1308 0.2308 -0.0046 -0.0167 0.0100  155 VAL   B CB  
6411 C CG1 . VAL   B 155 ? 0.1346 0.1295 0.2301 -0.0102 -0.0165 0.0011  155 VAL   B CG1 
6412 C CG2 . VAL   B 155 ? 0.1281 0.1436 0.2630 -0.0040 -0.0160 0.0350  155 VAL   B CG2 
6422 N N   . PHE   B 156 ? 0.1174 0.1255 0.2046 0.0069  -0.0055 -0.0100 156 PHE   B N   
6423 C CA  . PHE   B 156 ? 0.1251 0.1350 0.2357 0.0055  -0.0061 -0.0126 156 PHE   B CA  
6424 C C   . PHE   B 156 ? 0.1273 0.1381 0.2607 0.0124  -0.0143 -0.0264 156 PHE   B C   
6425 O O   . PHE   B 156 ? 0.1509 0.1568 0.2766 0.0262  -0.0053 -0.0328 156 PHE   B O   
6426 C CB  . PHE   B 156 ? 0.1344 0.1331 0.2447 0.0020  -0.0213 -0.0077 156 PHE   B CB  
6427 C CG  . PHE   B 156 ? 0.1308 0.1377 0.2618 -0.0050 -0.0225 0.0094  156 PHE   B CG  
6428 C CD1 . PHE   B 156 ? 0.1398 0.1652 0.2993 -0.0001 -0.0123 0.0454  156 PHE   B CD1 
6429 C CD2 . PHE   B 156 ? 0.1401 0.1485 0.2584 0.0093  -0.0345 0.0134  156 PHE   B CD2 
6430 C CE1 . PHE   B 156 ? 0.1456 0.1856 0.3142 0.0034  -0.0080 0.0466  156 PHE   B CE1 
6431 C CE2 . PHE   B 156 ? 0.1474 0.1742 0.2826 0.0132  -0.0264 0.0208  156 PHE   B CE2 
6432 C CZ  . PHE   B 156 ? 0.1393 0.1840 0.3050 0.0156  -0.0207 0.0357  156 PHE   B CZ  
6442 N N   . ASP   B 157 ? 0.1280 0.1262 0.2772 0.0111  -0.0260 -0.0124 157 ASP   B N   
6443 C CA  . ASP   B 157 ? 0.1405 0.1320 0.3058 0.0084  -0.0312 -0.0224 157 ASP   B CA  
6444 C C   . ASP   B 157 ? 0.1401 0.1263 0.3070 0.0130  -0.0285 -0.0376 157 ASP   B C   
6445 O O   . ASP   B 157 ? 0.1299 0.1328 0.2934 0.0050  -0.0260 -0.0254 157 ASP   B O   
6446 C CB  . ASP   B 157 ? 0.1622 0.1498 0.3239 0.0078  -0.0490 -0.0045 157 ASP   B CB  
6447 C CG  . ASP   B 157 ? 0.1950 0.1648 0.3486 0.0037  -0.0332 0.0011  157 ASP   B CG  
6448 O OD1 . ASP   B 157 ? 0.2048 0.1639 0.3615 0.0100  -0.0336 0.0064  157 ASP   B OD1 
6449 O OD2 . ASP   B 157 ? 0.2312 0.1858 0.3797 0.0024  -0.0085 -0.0063 157 ASP   B OD2 
6454 N N   . LYS   B 158 ? 0.1407 0.1512 0.3202 0.0052  -0.0097 -0.0556 158 LYS   B N   
6455 C CA  . LYS   B 158 ? 0.1552 0.1679 0.3275 0.0044  -0.0049 -0.0658 158 LYS   B CA  
6456 C C   . LYS   B 158 ? 0.1564 0.1582 0.3248 0.0089  -0.0097 -0.0631 158 LYS   B C   
6457 O O   . LYS   B 158 ? 0.1630 0.1569 0.3362 -0.0022 -0.0172 -0.0699 158 LYS   B O   
6458 C CB  . LYS   B 158 ? 0.1803 0.2085 0.3364 0.0004  0.0052  -0.0864 158 LYS   B CB  
6459 C CG  . LYS   B 158 ? 0.2199 0.2544 0.3503 0.0102  0.0153  -0.1036 158 LYS   B CG  
6460 C CD  . LYS   B 158 ? 0.2467 0.2990 0.3759 0.0121  0.0179  -0.1003 158 LYS   B CD  
6461 C CE  . LYS   B 158 ? 0.2686 0.3314 0.4020 0.0170  0.0160  -0.0925 158 LYS   B CE  
6462 N NZ  . LYS   B 158 ? 0.2642 0.3397 0.4071 0.0209  0.0207  -0.0925 158 LYS   B NZ  
6476 N N   . ASN   B 159 ? 0.1545 0.1518 0.3408 0.0034  -0.0107 -0.0435 159 ASN   B N   
6477 C CA  . ASN   B 159 ? 0.1667 0.1444 0.3525 0.0137  -0.0314 -0.0343 159 ASN   B CA  
6478 C C   . ASN   B 159 ? 0.1540 0.1350 0.3456 0.0105  -0.0340 -0.0321 159 ASN   B C   
6479 O O   . ASN   B 159 ? 0.1622 0.1272 0.3567 -0.0041 -0.0318 -0.0278 159 ASN   B O   
6480 C CB  . ASN   B 159 ? 0.1883 0.1573 0.3844 0.0237  -0.0406 -0.0229 159 ASN   B CB  
6481 C CG  . ASN   B 159 ? 0.2157 0.1779 0.4191 0.0253  -0.0466 -0.0477 159 ASN   B CG  
6482 O OD1 . ASN   B 159 ? 0.2330 0.1923 0.4260 0.0372  -0.0444 -0.0655 159 ASN   B OD1 
6483 N ND2 . ASN   B 159 ? 0.2191 0.1864 0.4395 0.0322  -0.0520 -0.0441 159 ASN   B ND2 
6490 N N   . LEU   B 160 ? 0.1425 0.1330 0.3238 0.0053  -0.0410 -0.0271 160 LEU   B N   
6491 C CA  . LEU   B 160 ? 0.1371 0.1364 0.2867 0.0072  -0.0320 -0.0137 160 LEU   B CA  
6492 C C   . LEU   B 160 ? 0.1318 0.1222 0.2760 0.0025  -0.0251 -0.0264 160 LEU   B C   
6493 O O   . LEU   B 160 ? 0.1277 0.1316 0.2635 -0.0042 -0.0284 -0.0193 160 LEU   B O   
6494 C CB  . LEU   B 160 ? 0.1349 0.1409 0.2685 0.0069  -0.0309 -0.0060 160 LEU   B CB  
6495 C CG  . LEU   B 160 ? 0.1373 0.1574 0.2458 0.0090  -0.0330 -0.0051 160 LEU   B CG  
6496 C CD1 . LEU   B 160 ? 0.1508 0.1729 0.2440 -0.0020 -0.0328 -0.0099 160 LEU   B CD1 
6497 C CD2 . LEU   B 160 ? 0.1434 0.1619 0.2534 0.0200  -0.0311 -0.0239 160 LEU   B CD2 
6509 N N   . TYR   B 161 ? 0.1309 0.1325 0.2723 -0.0042 -0.0086 -0.0343 161 TYR   B N   
6510 C CA  . TYR   B 161 ? 0.1414 0.1327 0.2664 -0.0081 0.0038  -0.0366 161 TYR   B CA  
6511 C C   . TYR   B 161 ? 0.1480 0.1304 0.2594 -0.0081 0.0078  -0.0306 161 TYR   B C   
6512 O O   . TYR   B 161 ? 0.1531 0.1277 0.2496 -0.0118 -0.0021 -0.0293 161 TYR   B O   
6513 C CB  . TYR   B 161 ? 0.1545 0.1387 0.2664 -0.0163 0.0149  -0.0329 161 TYR   B CB  
6514 C CG  . TYR   B 161 ? 0.1764 0.1370 0.2691 -0.0189 0.0283  -0.0405 161 TYR   B CG  
6515 C CD1 . TYR   B 161 ? 0.1864 0.1351 0.2625 -0.0324 0.0246  -0.0387 161 TYR   B CD1 
6516 C CD2 . TYR   B 161 ? 0.1998 0.1506 0.2669 -0.0133 0.0282  -0.0389 161 TYR   B CD2 
6517 C CE1 . TYR   B 161 ? 0.1999 0.1520 0.2692 -0.0341 0.0211  -0.0375 161 TYR   B CE1 
6518 C CE2 . TYR   B 161 ? 0.2122 0.1650 0.2742 -0.0236 0.0267  -0.0271 161 TYR   B CE2 
6519 C CZ  . TYR   B 161 ? 0.2105 0.1669 0.2728 -0.0390 0.0247  -0.0179 161 TYR   B CZ  
6520 O OH  . TYR   B 161 ? 0.2369 0.1924 0.2988 -0.0414 0.0226  -0.0152 161 TYR   B OH  
6530 N N   . ASP   B 162 ? 0.1488 0.1296 0.2756 -0.0058 -0.0039 -0.0450 162 ASP   B N   
6531 C CA  . ASP   B 162 ? 0.1635 0.1377 0.2783 -0.0068 -0.0064 -0.0465 162 ASP   B CA  
6532 C C   . ASP   B 162 ? 0.1581 0.1292 0.2703 -0.0099 -0.0127 -0.0418 162 ASP   B C   
6533 O O   . ASP   B 162 ? 0.1673 0.1388 0.2730 -0.0176 -0.0258 -0.0358 162 ASP   B O   
6534 C CB  . ASP   B 162 ? 0.1844 0.1541 0.3083 0.0020  -0.0089 -0.0633 162 ASP   B CB  
6535 C CG  . ASP   B 162 ? 0.1914 0.1778 0.3243 0.0085  -0.0066 -0.0804 162 ASP   B CG  
6536 O OD1 . ASP   B 162 ? 0.1910 0.1965 0.3106 0.0042  -0.0001 -0.0738 162 ASP   B OD1 
6537 O OD2 . ASP   B 162 ? 0.2082 0.2012 0.3630 0.0221  0.0063  -0.0763 162 ASP   B OD2 
6542 N N   . LYS   B 163 ? 0.1508 0.1170 0.2675 -0.0111 -0.0215 -0.0259 163 LYS   B N   
6543 C CA  . LYS   B 163 ? 0.1615 0.1292 0.2686 -0.0207 -0.0234 -0.0096 163 LYS   B CA  
6544 C C   . LYS   B 163 ? 0.1377 0.1257 0.2590 -0.0207 -0.0218 -0.0057 163 LYS   B C   
6545 O O   . LYS   B 163 ? 0.1417 0.1384 0.2868 -0.0241 -0.0219 -0.0061 163 LYS   B O   
6546 C CB  . LYS   B 163 ? 0.2075 0.1643 0.3190 -0.0118 -0.0349 0.0135  163 LYS   B CB  
6547 C CG  . LYS   B 163 ? 0.2908 0.2557 0.3996 -0.0223 -0.0328 0.0111  163 LYS   B CG  
6548 C CD  . LYS   B 163 ? 0.3672 0.3415 0.4808 -0.0347 -0.0407 0.0029  163 LYS   B CD  
6549 C CE  . LYS   B 163 ? 0.4184 0.4018 0.5390 -0.0447 -0.0460 0.0014  163 LYS   B CE  
6550 N NZ  . LYS   B 163 ? 0.4732 0.4732 0.5750 -0.0494 -0.0464 -0.0004 163 LYS   B NZ  
6564 N N   . LEU   B 164 ? 0.1258 0.1176 0.2373 -0.0138 -0.0192 0.0000  164 LEU   B N   
6565 C CA  . LEU   B 164 ? 0.1311 0.1172 0.2251 -0.0113 -0.0253 -0.0023 164 LEU   B CA  
6566 C C   . LEU   B 164 ? 0.1383 0.1229 0.2362 -0.0115 -0.0334 -0.0016 164 LEU   B C   
6567 O O   . LEU   B 164 ? 0.1399 0.1428 0.2433 -0.0099 -0.0363 -0.0027 164 LEU   B O   
6568 C CB  . LEU   B 164 ? 0.1269 0.1148 0.2205 -0.0054 -0.0219 -0.0034 164 LEU   B CB  
6569 C CG  . LEU   B 164 ? 0.1360 0.1302 0.2302 -0.0124 -0.0153 0.0001  164 LEU   B CG  
6570 C CD1 . LEU   B 164 ? 0.1480 0.1316 0.2344 -0.0172 -0.0267 -0.0024 164 LEU   B CD1 
6571 C CD2 . LEU   B 164 ? 0.1471 0.1732 0.2405 -0.0045 0.0004  -0.0195 164 LEU   B CD2 
6583 N N   . VAL   B 165 ? 0.1604 0.1307 0.2531 -0.0190 -0.0331 -0.0169 165 VAL   B N   
6584 C CA  . VAL   B 165 ? 0.1971 0.1382 0.2417 -0.0272 -0.0513 -0.0079 165 VAL   B CA  
6585 C C   . VAL   B 165 ? 0.2277 0.1521 0.2582 -0.0391 -0.0736 -0.0022 165 VAL   B C   
6586 O O   . VAL   B 165 ? 0.2440 0.1661 0.2619 -0.0448 -0.0754 0.0082  165 VAL   B O   
6587 C CB  . VAL   B 165 ? 0.2197 0.1557 0.2351 -0.0077 -0.0217 -0.0146 165 VAL   B CB  
6588 C CG1 . VAL   B 165 ? 0.2367 0.1605 0.2666 -0.0126 -0.0147 -0.0210 165 VAL   B CG1 
6589 C CG2 . VAL   B 165 ? 0.2081 0.1620 0.2311 -0.0060 -0.0157 -0.0080 165 VAL   B CG2 
6599 N N   . SER   B 166 ? 0.2363 0.1406 0.2839 -0.0391 -0.0756 -0.0220 166 SER   B N   
6600 C CA  . SER   B 166 ? 0.2264 0.1438 0.3320 -0.0391 -0.0701 -0.0254 166 SER   B CA  
6601 C C   . SER   B 166 ? 0.2121 0.1517 0.3474 -0.0416 -0.0708 -0.0079 166 SER   B C   
6602 O O   . SER   B 166 ? 0.2146 0.1715 0.3731 -0.0519 -0.0907 -0.0257 166 SER   B O   
6603 C CB  . SER   B 166 ? 0.2258 0.1475 0.3572 -0.0330 -0.0620 -0.0351 166 SER   B CB  
6604 O OG  . SER   B 166 ? 0.2185 0.1454 0.3751 -0.0235 -0.0617 -0.0199 166 SER   B OG  
6610 N N   . SER   B 167 ? 0.1960 0.1442 0.3218 -0.0328 -0.0628 0.0157  167 SER   B N   
6611 C CA  . SER   B 167 ? 0.1847 0.1494 0.3045 -0.0306 -0.0445 0.0165  167 SER   B CA  
6612 C C   . SER   B 167 ? 0.1745 0.1637 0.2976 -0.0456 -0.0421 0.0330  167 SER   B C   
6613 O O   . SER   B 167 ? 0.1801 0.1722 0.2905 -0.0485 -0.0361 0.0301  167 SER   B O   
6614 C CB  . SER   B 167 ? 0.1750 0.1551 0.2956 -0.0309 -0.0181 0.0306  167 SER   B CB  
6615 O OG  . SER   B 167 ? 0.1742 0.1680 0.2834 -0.0227 -0.0078 0.0288  167 SER   B OG  
6621 N N   . PHE   B 168 ? 0.1739 0.1594 0.2929 -0.0406 -0.0262 0.0385  168 PHE   B N   
6622 C CA  . PHE   B 168 ? 0.1820 0.1570 0.2758 -0.0431 -0.0247 0.0272  168 PHE   B CA  
6623 C C   . PHE   B 168 ? 0.1613 0.1503 0.2460 -0.0237 -0.0093 0.0110  168 PHE   B C   
6624 O O   . PHE   B 168 ? 0.1926 0.1403 0.2548 -0.0048 -0.0064 0.0004  168 PHE   B O   
6625 C CB  . PHE   B 168 ? 0.1994 0.1605 0.2695 -0.0517 -0.0452 0.0465  168 PHE   B CB  
6626 C CG  . PHE   B 168 ? 0.2283 0.1466 0.2639 -0.0537 -0.0534 0.0231  168 PHE   B CG  
6627 C CD1 . PHE   B 168 ? 0.2616 0.1507 0.2783 -0.0460 -0.0624 0.0238  168 PHE   B CD1 
6628 C CD2 . PHE   B 168 ? 0.2170 0.1376 0.2611 -0.0426 -0.0506 0.0280  168 PHE   B CD2 
6629 C CE1 . PHE   B 168 ? 0.2724 0.1649 0.2833 -0.0263 -0.0547 0.0225  168 PHE   B CE1 
6630 C CE2 . PHE   B 168 ? 0.2385 0.1501 0.2728 -0.0258 -0.0560 0.0155  168 PHE   B CE2 
6631 C CZ  . PHE   B 168 ? 0.2567 0.1466 0.2819 -0.0136 -0.0582 0.0260  168 PHE   B CZ  
6641 N N   . LEU   B 169 ? 0.1623 0.1672 0.2511 -0.0019 -0.0071 -0.0038 169 LEU   B N   
6642 C CA  . LEU   B 169 ? 0.1806 0.1919 0.2932 -0.0068 -0.0098 -0.0290 169 LEU   B CA  
6643 C C   . LEU   B 169 ? 0.2016 0.2122 0.3661 0.0031  -0.0073 -0.0682 169 LEU   B C   
6644 O O   . LEU   B 169 ? 0.2231 0.2281 0.4209 -0.0006 -0.0125 -0.0897 169 LEU   B O   
6645 C CB  . LEU   B 169 ? 0.2008 0.2318 0.3015 -0.0172 -0.0236 -0.0006 169 LEU   B CB  
6646 C CG  . LEU   B 169 ? 0.2409 0.2711 0.3373 -0.0054 -0.0196 0.0128  169 LEU   B CG  
6647 C CD1 . LEU   B 169 ? 0.2536 0.2944 0.3465 -0.0059 -0.0219 0.0284  169 LEU   B CD1 
6648 C CD2 . LEU   B 169 ? 0.2407 0.2787 0.3477 0.0113  -0.0052 0.0061  169 LEU   B CD2 
6649 O OXT . LEU   B 169 ? 0.2270 0.2281 0.3743 0.0270  0.0038  -0.0742 169 LEU   B OXT 
6661 N N2  B A1A5C C .   ? 0.3222 0.2737 0.2586 -0.0352 0.0108  0.0267  201 A1A5C A N2  
6662 C C3  B A1A5C C .   ? 0.3119 0.2687 0.2652 -0.0337 0.0088  0.0269  201 A1A5C A C3  
6663 C C6  B A1A5C C .   ? 0.3287 0.2759 0.2702 -0.0369 0.0156  0.0333  201 A1A5C A C6  
6664 C C9  B A1A5C C .   ? 0.3242 0.2773 0.2884 -0.0062 -0.0167 0.0295  201 A1A5C A C9  
6665 C C12 B A1A5C C .   ? 0.3202 0.2779 0.2758 -0.0027 -0.0088 0.0306  201 A1A5C A C12 
6666 C C14 B A1A5C C .   ? 0.3264 0.2752 0.2631 -0.0375 0.0130  0.0307  201 A1A5C A C14 
6667 C C1  B A1A5C C .   ? 0.3120 0.2634 0.2600 -0.0316 0.0059  0.0276  201 A1A5C A C1  
6668 C C10 B A1A5C C .   ? 0.3236 0.2763 0.2867 -0.0056 -0.0188 0.0290  201 A1A5C A C10 
6669 C C11 B A1A5C C .   ? 0.3222 0.2767 0.2815 -0.0043 -0.0146 0.0301  201 A1A5C A C11 
6670 C C13 B A1A5C C .   ? 0.3119 0.2762 0.2598 0.0082  -0.0075 0.0345  201 A1A5C A C13 
6671 C C15 B A1A5C C .   ? 0.3155 0.2709 0.2551 -0.0362 0.0071  0.0230  201 A1A5C A C15 
6672 C C2  B A1A5C C .   ? 0.3101 0.2670 0.2566 -0.0328 0.0058  0.0255  201 A1A5C A C2  
6673 C C4  B A1A5C C .   ? 0.3124 0.2706 0.2714 -0.0308 0.0093  0.0280  201 A1A5C A C4  
6674 C C5  B A1A5C C .   ? 0.3193 0.2721 0.2627 -0.0347 0.0116  0.0268  201 A1A5C A C5  
6675 C C7  B A1A5C C .   ? 0.3275 0.2788 0.2814 -0.0138 -0.0010 0.0332  201 A1A5C A C7  
6676 C C8  B A1A5C C .   ? 0.3255 0.2779 0.2848 -0.0105 -0.0086 0.0323  201 A1A5C A C8  
6677 N N1  B A1A5C C .   ? 0.3289 0.2762 0.2667 -0.0380 0.0148  0.0330  201 A1A5C A N1  
6678 O O1  B A1A5C C .   ? 0.3124 0.2801 0.2604 0.0126  -0.0059 0.0403  201 A1A5C A O1  
6679 O O2  B A1A5C C .   ? 0.3042 0.2678 0.2435 0.0190  -0.0109 0.0355  201 A1A5C A O2  
6680 S S1  B A1A5C C .   ? 0.3369 0.2802 0.2808 -0.0315 0.0170  0.0383  201 A1A5C A S1  
6681 S S2  B A1A5C C .   ? 0.3072 0.2670 0.2497 -0.0355 -0.0012 0.0193  201 A1A5C A S2  
6693 N N2  C A1A5C D .   ? 0.2505 0.2427 0.2554 -0.0070 0.0036  0.0074  202 A1A5C A N2  
6694 C C3  C A1A5C D .   ? 0.2434 0.2310 0.2394 -0.0106 0.0013  0.0146  202 A1A5C A C3  
6695 C C6  C A1A5C D .   ? 0.2616 0.2557 0.2719 -0.0109 -0.0071 -0.0008 202 A1A5C A C6  
6696 C C9  C A1A5C D .   ? 0.2801 0.2929 0.2956 -0.0112 0.0022  -0.0152 202 A1A5C A C9  
6697 C C12 C A1A5C D .   ? 0.2734 0.2914 0.2851 -0.0148 0.0068  -0.0091 202 A1A5C A C12 
6698 C C14 C A1A5C D .   ? 0.2545 0.2494 0.2642 -0.0061 -0.0012 0.0012  202 A1A5C A C14 
6699 C C1  C A1A5C D .   ? 0.2460 0.2187 0.2485 0.0000  0.0033  0.0141  202 A1A5C A C1  
6700 C C10 C A1A5C D .   ? 0.2803 0.2946 0.2957 -0.0097 0.0020  -0.0141 202 A1A5C A C10 
6701 C C11 C A1A5C D .   ? 0.2784 0.2948 0.2915 -0.0113 0.0022  -0.0133 202 A1A5C A C11 
6702 C C13 C A1A5C D .   ? 0.2693 0.2945 0.2763 -0.0139 0.0133  -0.0063 202 A1A5C A C13 
6703 C C15 C A1A5C D .   ? 0.2463 0.2349 0.2474 -0.0071 0.0029  0.0093  202 A1A5C A C15 
6704 C C2  C A1A5C D .   ? 0.2444 0.2223 0.2400 -0.0044 0.0087  0.0165  202 A1A5C A C2  
6705 C C4  C A1A5C D .   ? 0.2439 0.2350 0.2294 -0.0133 0.0022  0.0139  202 A1A5C A C4  
6706 C C5  C A1A5C D .   ? 0.2501 0.2408 0.2493 -0.0092 -0.0030 0.0070  202 A1A5C A C5  
6707 C C7  C A1A5C D .   ? 0.2776 0.2872 0.2939 -0.0151 0.0016  -0.0102 202 A1A5C A C7  
6708 C C8  C A1A5C D .   ? 0.2786 0.2897 0.2952 -0.0110 -0.0005 -0.0150 202 A1A5C A C8  
6709 N N1  C A1A5C D .   ? 0.2587 0.2525 0.2676 -0.0065 -0.0044 -0.0015 202 A1A5C A N1  
6710 O O1  C A1A5C D .   ? 0.2647 0.2962 0.2682 -0.0125 0.0167  -0.0024 202 A1A5C A O1  
6711 O O2  C A1A5C D .   ? 0.2697 0.2971 0.2803 -0.0134 0.0160  -0.0085 202 A1A5C A O2  
6712 S S1  C A1A5C D .   ? 0.2814 0.2766 0.2998 -0.0183 -0.0010 -0.0091 202 A1A5C A S1  
6713 S S2  C A1A5C D .   ? 0.2422 0.2225 0.2406 -0.0062 0.0113  0.0166  202 A1A5C A S2  
6725 O O   . HOH   E .   ? 0.4786 0.6478 0.4445 -0.1392 0.1281  -0.0418 301 HOH   A O   
6726 O O   . HOH   E .   ? 0.7536 0.2214 0.4476 0.0103  -0.0613 0.0832  302 HOH   A O   
6727 O O   . HOH   E .   ? 0.4429 0.5661 0.3862 -0.1314 -0.1118 -0.0525 303 HOH   A O   
6728 O O   . HOH   E .   ? 0.2794 0.6672 0.5285 0.0269  -0.0649 0.1520  304 HOH   A O   
6729 O O   . HOH   E .   ? 0.4407 0.3031 0.4668 -0.0526 0.1359  0.0787  305 HOH   A O   
6730 O O   . HOH   E .   ? 0.6042 0.4692 0.6117 -0.0163 -0.0937 0.0798  306 HOH   A O   
6731 O O   . HOH   E .   ? 0.4400 0.3690 0.4182 0.0192  0.0428  -0.1062 307 HOH   A O   
6732 O O   . HOH   E .   ? 0.6220 0.5008 0.3634 0.2096  -0.0955 0.0708  308 HOH   A O   
6733 O O   . HOH   E .   ? 0.2504 0.4926 0.3957 -0.0105 -0.0477 0.0819  309 HOH   A O   
6734 O O   . HOH   E .   ? 0.4575 0.3523 0.5387 -0.0552 0.2011  -0.1373 310 HOH   A O   
6735 O O   . HOH   E .   ? 0.2913 0.2686 0.1800 -0.0199 0.0574  0.0400  311 HOH   A O   
6736 O O   . HOH   E .   ? 0.2984 0.3781 0.3825 -0.1228 0.1034  -0.0419 312 HOH   A O   
6737 O O   . HOH   E .   ? 0.5416 0.1922 0.4980 0.0685  0.0014  0.0198  313 HOH   A O   
6738 O O   A HOH   E .   ? 0.1402 0.2827 0.2334 0.0812  0.0491  0.0984  314 HOH   A O   
6739 O O   . HOH   E .   ? 0.2074 0.1653 0.3382 -0.0386 0.0028  -0.0223 315 HOH   A O   
6740 O O   . HOH   E .   ? 0.3554 0.3060 0.3161 -0.0328 0.1356  0.0174  316 HOH   A O   
6741 O O   . HOH   E .   ? 0.4750 0.5201 0.3198 -0.1011 0.1667  0.0848  317 HOH   A O   
6742 O O   . HOH   E .   ? 0.3346 0.4437 0.2271 -0.0153 0.0539  0.0442  318 HOH   A O   
6743 O O   . HOH   E .   ? 0.2533 0.1906 0.2484 -0.0369 0.0017  -0.0126 319 HOH   A O   
6744 O O   . HOH   E .   ? 0.1335 0.3848 0.2962 -0.0205 0.0077  0.1144  320 HOH   A O   
6745 O O   . HOH   E .   ? 0.2802 0.2304 0.4673 -0.0275 -0.1184 0.1035  321 HOH   A O   
6746 O O   . HOH   E .   ? 0.3159 0.3758 0.3447 0.1409  0.0019  -0.0187 322 HOH   A O   
6747 O O   . HOH   E .   ? 0.4866 0.4227 0.3809 -0.2056 -0.0833 0.1810  323 HOH   A O   
6748 O O   . HOH   E .   ? 0.7281 0.5035 0.3451 0.0512  -0.0841 0.0848  324 HOH   A O   
6749 O O   . HOH   E .   ? 0.3382 0.2421 0.2876 -0.0228 -0.0224 0.0223  325 HOH   A O   
6750 O O   . HOH   E .   ? 0.1787 0.2480 0.3017 0.0216  -0.0322 -0.0262 326 HOH   A O   
6751 O O   . HOH   E .   ? 0.1509 0.1399 0.2095 -0.0221 -0.0034 0.0050  327 HOH   A O   
6752 O O   . HOH   E .   ? 0.2156 0.3985 0.4647 -0.0105 -0.0597 0.1833  328 HOH   A O   
6753 O O   . HOH   E .   ? 0.5957 0.4548 0.5273 0.0621  0.2749  -0.0957 329 HOH   A O   
6754 O O   . HOH   E .   ? 0.3519 0.3657 0.3527 -0.0332 -0.0491 -0.0710 330 HOH   A O   
6755 O O   . HOH   E .   ? 0.5183 0.2493 0.2497 0.1570  -0.0054 0.0345  331 HOH   A O   
6756 O O   A HOH   E .   ? 0.2789 0.2274 0.2809 0.0398  0.0125  0.0213  332 HOH   A O   
6757 O O   A HOH   E .   ? 0.4570 0.1408 0.1828 0.0140  0.0161  0.0197  333 HOH   A O   
6758 O O   . HOH   E .   ? 0.8606 0.4917 0.6181 -0.0949 -0.1346 0.0723  334 HOH   A O   
6759 O O   . HOH   E .   ? 0.3063 0.2488 0.2327 -0.0919 0.0376  0.0326  335 HOH   A O   
6760 O O   . HOH   E .   ? 0.2035 0.1655 0.2733 0.0026  -0.0577 -0.0188 336 HOH   A O   
6761 O O   . HOH   E .   ? 0.1821 0.1720 0.2338 0.0051  -0.0234 0.0189  337 HOH   A O   
6762 O O   . HOH   E .   ? 0.5751 0.5688 0.5412 -0.0937 -0.1158 -0.1439 338 HOH   A O   
6763 O O   . HOH   E .   ? 0.1687 0.3226 0.5069 -0.0305 0.0280  -0.1295 339 HOH   A O   
6764 O O   . HOH   E .   ? 0.3465 0.2967 0.3647 -0.1315 -0.0425 -0.0010 340 HOH   A O   
6765 O O   . HOH   E .   ? 0.4509 0.2818 0.4169 0.0624  -0.1080 0.1285  341 HOH   A O   
6766 O O   . HOH   E .   ? 0.2437 0.2507 0.3738 -0.0518 0.0956  0.0005  342 HOH   A O   
6767 O O   . HOH   E .   ? 0.2321 0.2143 0.2804 0.0231  -0.0017 0.0695  343 HOH   A O   
6768 O O   . HOH   E .   ? 0.2254 0.3694 0.3817 0.0807  -0.0727 -0.0544 344 HOH   A O   
6769 O O   . HOH   E .   ? 0.4760 0.4827 0.4714 0.1390  0.1467  -0.0752 345 HOH   A O   
6770 O O   . HOH   E .   ? 0.1396 0.2036 0.2337 0.0050  -0.0074 0.0442  346 HOH   A O   
6771 O O   . HOH   E .   ? 0.2708 0.4148 0.2993 -0.0441 0.0281  0.0090  347 HOH   A O   
6772 O O   . HOH   E .   ? 0.1698 0.1584 0.2051 -0.0243 -0.0050 0.0321  348 HOH   A O   
6773 O O   . HOH   E .   ? 0.1362 0.1808 0.2699 0.0121  -0.0249 0.0011  349 HOH   A O   
6774 O O   . HOH   E .   ? 0.2091 0.1634 0.2440 0.0244  -0.0341 0.0006  350 HOH   A O   
6775 O O   . HOH   E .   ? 0.5981 0.3752 0.2716 -0.0492 -0.0123 0.0952  351 HOH   A O   
6776 O O   . HOH   E .   ? 0.2526 0.1985 0.2394 -0.0614 0.0091  0.0386  352 HOH   A O   
6777 O O   . HOH   E .   ? 0.3520 0.3692 0.3398 0.1722  0.0544  0.0460  353 HOH   A O   
6778 O O   . HOH   E .   ? 0.1353 0.1625 0.2371 0.0064  -0.0288 -0.0489 354 HOH   A O   
6779 O O   . HOH   E .   ? 0.3138 0.3563 0.3387 0.1243  -0.0785 -0.1185 355 HOH   A O   
6780 O O   . HOH   E .   ? 0.1746 0.1928 0.3573 0.0096  0.0711  -0.0163 356 HOH   A O   
6781 O O   . HOH   E .   ? 0.1683 0.1651 0.2356 0.0018  -0.0448 -0.0026 357 HOH   A O   
6782 O O   . HOH   E .   ? 0.3069 0.3472 0.3763 -0.1057 -0.1032 -0.0413 358 HOH   A O   
6783 O O   . HOH   E .   ? 0.1211 0.1184 0.1378 -0.0080 0.0095  0.0003  359 HOH   A O   
6784 O O   . HOH   E .   ? 0.1422 0.1217 0.2185 -0.0060 0.0103  -0.0087 360 HOH   A O   
6785 O O   . HOH   E .   ? 0.4591 0.2329 0.3212 -0.1387 0.1286  -0.0528 361 HOH   A O   
6786 O O   . HOH   E .   ? 0.1398 0.1420 0.1670 -0.0042 -0.0172 -0.0203 362 HOH   A O   
6787 O O   . HOH   E .   ? 0.3959 0.2159 0.4920 -0.1194 0.0925  0.0313  363 HOH   A O   
6788 O O   . HOH   E .   ? 0.1938 0.1838 0.1836 -0.0000 0.0028  0.0068  364 HOH   A O   
6789 O O   . HOH   E .   ? 0.1883 0.1815 0.2352 -0.0353 0.0173  0.0259  365 HOH   A O   
6790 O O   . HOH   E .   ? 0.3285 0.3898 0.2434 -0.1137 -0.0227 -0.0777 366 HOH   A O   
6791 O O   . HOH   E .   ? 0.3585 0.5687 0.4943 -0.0284 -0.1575 0.0439  367 HOH   A O   
6792 O O   . HOH   E .   ? 0.2770 0.3006 0.5355 -0.0527 -0.1293 -0.0531 368 HOH   A O   
6793 O O   . HOH   E .   ? 0.4283 0.3798 0.4650 -0.0874 -0.0342 0.0238  369 HOH   A O   
6794 O O   A HOH   E .   ? 0.2775 0.2902 0.3523 -0.0814 0.0812  0.0743  370 HOH   A O   
6795 O O   . HOH   E .   ? 0.2540 0.1815 0.2527 -0.0198 0.0009  0.0154  371 HOH   A O   
6796 O O   A HOH   E .   ? 0.4012 0.2599 0.2881 -0.0845 0.1087  0.0243  372 HOH   A O   
6797 O O   . HOH   E .   ? 0.1818 0.2211 0.4127 0.0229  0.0851  -0.0555 373 HOH   A O   
6798 O O   . HOH   E .   ? 0.2977 0.2428 0.3233 -0.0157 -0.0492 0.0797  374 HOH   A O   
6799 O O   . HOH   E .   ? 0.3638 0.1931 0.2167 0.1184  0.0346  0.0168  375 HOH   A O   
6800 O O   . HOH   E .   ? 0.1715 0.1247 0.1715 -0.0232 0.0091  -0.0059 376 HOH   A O   
6801 O O   . HOH   E .   ? 0.3266 0.2248 0.4948 -0.0787 -0.1052 0.0492  377 HOH   A O   
6802 O O   . HOH   E .   ? 0.1938 0.2169 0.2053 -0.0332 -0.0405 0.0252  378 HOH   A O   
6803 O O   . HOH   E .   ? 0.2596 0.2257 0.2808 -0.0015 -0.0291 -0.0511 379 HOH   A O   
6804 O O   . HOH   E .   ? 0.6998 0.5516 0.4717 -0.1219 0.0253  0.2031  380 HOH   A O   
6805 O O   . HOH   E .   ? 0.3539 0.6232 0.4180 -0.0613 -0.0136 0.1524  381 HOH   A O   
6806 O O   . HOH   E .   ? 0.1601 0.3663 0.3619 -0.0364 0.0697  0.0395  382 HOH   A O   
6807 O O   . HOH   E .   ? 0.1923 0.1519 0.1466 -0.0067 0.0149  0.0111  383 HOH   A O   
6808 O O   . HOH   E .   ? 0.1738 0.2649 0.2783 0.0430  0.0361  0.1107  384 HOH   A O   
6809 O O   . HOH   E .   ? 0.2865 0.4041 0.2826 0.0024  0.0770  0.1521  385 HOH   A O   
6810 O O   . HOH   E .   ? 0.3396 0.5040 0.3630 0.0642  0.1143  -0.0854 386 HOH   A O   
6811 O O   . HOH   E .   ? 0.5909 0.6247 0.3774 0.1803  -0.0688 -0.0534 387 HOH   A O   
6812 O O   . HOH   E .   ? 0.5483 0.3069 0.3962 -0.1283 0.1438  0.0567  388 HOH   A O   
6813 O O   . HOH   E .   ? 0.1386 0.1379 0.2023 0.0052  -0.0148 -0.0021 389 HOH   A O   
6814 O O   . HOH   E .   ? 0.2148 0.3502 0.3447 -0.0281 -0.0199 0.0176  390 HOH   A O   
6815 O O   A HOH   E .   ? 0.2050 0.3864 0.3541 0.0411  -0.0071 -0.0092 391 HOH   A O   
6816 O O   . HOH   E .   ? 0.2088 0.2231 0.2502 -0.0246 -0.0144 0.0699  392 HOH   A O   
6817 O O   . HOH   E .   ? 0.2945 0.2881 0.2007 0.0319  0.0727  -0.0019 393 HOH   A O   
6818 O O   . HOH   E .   ? 0.2071 0.1607 0.2469 0.0042  -0.0487 -0.0151 394 HOH   A O   
6819 O O   . HOH   E .   ? 0.1424 0.1714 0.1887 0.0152  -0.0279 -0.0338 395 HOH   A O   
6820 O O   . HOH   E .   ? 0.2483 0.4406 0.3259 -0.0464 0.0790  -0.1149 396 HOH   A O   
6821 O O   . HOH   E .   ? 0.2711 0.1892 0.1771 -0.0641 0.0242  0.0155  397 HOH   A O   
6822 O O   . HOH   E .   ? 0.4907 0.2423 0.3403 0.0341  -0.0773 -0.0288 398 HOH   A O   
6823 O O   . HOH   E .   ? 0.1746 0.1956 0.1879 -0.0080 0.0168  0.0562  399 HOH   A O   
6824 O O   B HOH   E .   ? 0.1459 0.2128 0.4828 -0.0143 -0.0428 0.0786  400 HOH   A O   
6825 O O   . HOH   E .   ? 0.2075 0.1499 0.2690 -0.0066 -0.0461 0.0154  401 HOH   A O   
6826 O O   . HOH   E .   ? 0.1744 0.1705 0.3659 0.0283  0.0923  0.0813  402 HOH   A O   
6827 O O   . HOH   E .   ? 0.2981 0.2684 0.2388 -0.0729 -0.0883 0.0275  403 HOH   A O   
6828 O O   . HOH   E .   ? 0.6272 0.4299 0.6679 -0.1318 0.0687  0.0317  404 HOH   A O   
6829 O O   . HOH   E .   ? 0.5067 0.4327 0.1891 0.0239  0.0690  0.0278  405 HOH   A O   
6830 O O   . HOH   E .   ? 0.2854 0.3761 0.6702 -0.0307 0.1254  -0.0178 406 HOH   A O   
6831 O O   . HOH   E .   ? 0.1478 0.1566 0.2655 -0.0030 -0.0146 0.0122  407 HOH   A O   
6832 O O   . HOH   E .   ? 0.5565 0.4874 0.3100 0.0035  -0.1135 0.0199  408 HOH   A O   
6833 O O   A HOH   E .   ? 0.1875 0.2286 0.2460 0.0002  0.0660  -0.0472 409 HOH   A O   
6834 O O   . HOH   E .   ? 0.5714 0.6722 0.5022 0.0338  -0.1126 0.0466  410 HOH   A O   
6835 O O   . HOH   E .   ? 0.2051 0.2299 0.3855 0.0221  -0.0637 -0.0469 411 HOH   A O   
6836 O O   . HOH   E .   ? 0.1493 0.2142 0.2778 -0.0287 -0.0088 0.0684  412 HOH   A O   
6837 O O   . HOH   E .   ? 0.4689 0.4003 0.4960 -0.1529 -0.0356 -0.0722 413 HOH   A O   
6838 O O   . HOH   E .   ? 0.4394 0.4219 0.2640 -0.0341 -0.1418 -0.0092 414 HOH   A O   
6839 O O   . HOH   E .   ? 0.1983 0.2501 0.3128 -0.0287 -0.0319 -0.0044 415 HOH   A O   
6840 O O   A HOH   E .   ? 0.2445 0.2845 0.2610 -0.0100 0.0712  0.0043  416 HOH   A O   
6841 O O   . HOH   E .   ? 0.4600 0.6317 0.3303 -0.0487 -0.0037 0.1493  417 HOH   A O   
6842 O O   . HOH   E .   ? 0.5021 0.4634 0.5574 -0.1613 0.1031  -0.0214 418 HOH   A O   
6843 O O   . HOH   E .   ? 0.5618 0.6654 0.3962 0.0939  0.2380  -0.1058 419 HOH   A O   
6844 O O   . HOH   E .   ? 0.3280 0.1221 0.2193 -0.0076 -0.0721 0.0007  420 HOH   A O   
6845 O O   . HOH   E .   ? 0.4236 0.3325 0.5691 0.0889  0.1223  0.0346  421 HOH   A O   
6846 O O   . HOH   E .   ? 0.4025 0.2178 0.4421 -0.0756 -0.1998 0.0897  422 HOH   A O   
6847 O O   . HOH   E .   ? 0.6461 0.3351 0.4603 0.1220  -0.0742 0.0775  423 HOH   A O   
6848 O O   A HOH   E .   ? 0.5534 0.2387 0.4382 0.0404  0.1362  0.1343  424 HOH   A O   
6849 O O   . HOH   E .   ? 0.2329 0.4202 0.2399 0.1665  -0.0234 -0.0031 425 HOH   A O   
6850 O O   . HOH   E .   ? 0.3959 0.6848 0.5084 0.0141  0.0122  0.1014  426 HOH   A O   
6851 O O   . HOH   E .   ? 0.6350 0.6019 0.5959 -0.0778 -0.0275 0.0856  427 HOH   A O   
6852 O O   A HOH   E .   ? 0.1244 0.0745 0.1313 -0.0005 -0.0361 -0.0066 428 HOH   A O   
6853 O O   A HOH   E .   ? 0.1319 0.1239 0.1616 -0.0085 -0.0324 0.0278  429 HOH   A O   
6854 O O   . HOH   E .   ? 0.2102 0.2610 0.2414 -0.0017 -0.0592 0.0182  430 HOH   A O   
6855 O O   B HOH   E .   ? 0.2584 0.2708 0.3016 0.1026  0.0590  0.1102  431 HOH   A O   
6856 O O   . HOH   E .   ? 0.2837 0.4959 0.1695 -0.0805 0.0663  -0.0254 432 HOH   A O   
6857 O O   A HOH   E .   ? 0.3335 0.1749 0.3541 0.0133  0.1056  0.0064  433 HOH   A O   
6858 O O   . HOH   E .   ? 0.3870 0.2447 0.1696 -0.1041 0.0598  0.0203  434 HOH   A O   
6859 O O   . HOH   E .   ? 0.7182 0.7354 0.4166 0.2414  -0.1427 0.1049  435 HOH   A O   
6860 O O   A HOH   E .   ? 0.1157 0.1230 0.1900 0.0148  -0.0278 0.0369  436 HOH   A O   
6861 O O   . HOH   E .   ? 0.2222 0.1432 0.2470 0.0069  0.0059  0.0130  437 HOH   A O   
6862 O O   . HOH   E .   ? 0.4777 0.3978 0.6692 0.0636  -0.0471 -0.1118 438 HOH   A O   
6863 O O   B HOH   E .   ? 0.3771 0.6607 0.4814 0.2729  0.0381  0.0600  439 HOH   A O   
6864 O O   . HOH   E .   ? 0.1706 0.1941 0.5537 -0.0206 -0.0740 0.0472  440 HOH   A O   
6865 O O   . HOH   E .   ? 0.3928 0.3260 0.4633 -0.0448 -0.1167 -0.1080 441 HOH   A O   
6866 O O   . HOH   E .   ? 0.2995 0.2767 0.4678 0.0204  0.1007  -0.0855 442 HOH   A O   
6867 O O   . HOH   E .   ? 0.3363 0.3215 0.3409 0.1798  -0.0493 -0.0563 443 HOH   A O   
6868 O O   . HOH   E .   ? 0.4967 0.4584 0.6782 0.0687  -0.1329 0.1402  444 HOH   A O   
6869 O O   B HOH   E .   ? 0.3389 0.4348 0.3813 0.0156  -0.0433 0.0454  445 HOH   A O   
6870 O O   . HOH   E .   ? 0.2094 0.2410 0.2299 0.0070  -0.0239 -0.0517 446 HOH   A O   
6871 O O   . HOH   E .   ? 0.5923 0.7597 0.6633 0.1247  0.0271  -0.0144 447 HOH   A O   
6872 O O   . HOH   E .   ? 0.2368 0.1919 0.3099 0.0151  0.0364  0.0107  448 HOH   A O   
6873 O O   . HOH   E .   ? 0.6308 0.2894 0.4851 0.0536  -0.0044 0.1565  449 HOH   A O   
6874 O O   B HOH   E .   ? 0.2552 0.3612 0.3233 0.0048  -0.0601 -0.1352 450 HOH   A O   
6875 O O   . HOH   E .   ? 0.6849 0.6690 0.5072 -0.0706 0.0060  -0.1117 451 HOH   A O   
6876 O O   . HOH   E .   ? 0.6796 0.6190 0.5277 -0.0298 0.0951  0.2428  452 HOH   A O   
6877 O O   . HOH   E .   ? 0.3996 0.4862 0.4304 -0.0127 -0.0280 0.1221  453 HOH   A O   
6878 O O   A HOH   E .   ? 0.3738 0.1997 0.3142 -0.0524 0.0347  0.1296  454 HOH   A O   
6879 O O   . HOH   E .   ? 0.2443 0.3682 0.4070 0.0767  -0.0163 0.1268  455 HOH   A O   
6880 O O   . HOH   E .   ? 0.5493 0.4126 0.5254 -0.0057 -0.0359 0.1268  456 HOH   A O   
6881 O O   . HOH   E .   ? 0.6801 0.5332 0.4366 -0.1054 0.1165  0.0101  457 HOH   A O   
6882 O O   . HOH   E .   ? 0.5381 0.4798 0.4728 0.1514  0.2535  0.2031  458 HOH   A O   
6883 O O   . HOH   E .   ? 0.2631 0.3873 0.3605 0.0144  -0.0473 0.0010  459 HOH   A O   
6884 O O   . HOH   E .   ? 0.6506 0.8033 0.4763 0.1231  -0.0573 0.0267  460 HOH   A O   
6885 O O   . HOH   E .   ? 0.3013 0.2972 0.3480 -0.0930 0.0018  -0.0685 461 HOH   A O   
6886 O O   . HOH   E .   ? 0.2607 0.4878 0.5016 -0.1131 0.0433  -0.1820 462 HOH   A O   
6887 O O   . HOH   E .   ? 0.3252 0.4578 0.4210 0.0931  -0.0546 0.0965  463 HOH   A O   
6888 O O   B HOH   E .   ? 0.5456 0.2392 0.3399 0.0529  -0.0801 0.0228  464 HOH   A O   
6889 O O   . HOH   E .   ? 0.3118 0.2784 0.4520 0.0979  -0.0963 -0.0441 465 HOH   A O   
6890 O O   . HOH   E .   ? 0.3823 0.5760 0.3420 0.0412  -0.0998 -0.0499 466 HOH   A O   
6891 O O   . HOH   E .   ? 0.5233 0.2918 0.6895 0.0360  0.0979  0.1899  467 HOH   A O   
6892 O O   . HOH   E .   ? 0.3046 0.1791 0.2864 0.0476  -0.0910 -0.0332 468 HOH   A O   
6893 O O   . HOH   E .   ? 0.2881 0.3914 0.6273 0.0878  0.0474  -0.1616 469 HOH   A O   
6894 O O   . HOH   E .   ? 0.3795 0.6901 0.3468 -0.0710 -0.0479 0.2304  470 HOH   A O   
6895 O O   . HOH   E .   ? 0.2796 0.3028 0.3383 -0.1223 0.0783  -0.0745 471 HOH   A O   
6896 O O   . HOH   E .   ? 0.2491 0.2985 0.4070 0.0262  0.0085  -0.0504 472 HOH   A O   
6897 O O   . HOH   E .   ? 0.4359 0.4999 0.4890 0.0607  -0.0461 -0.0366 473 HOH   A O   
6898 O O   . HOH   E .   ? 0.4760 0.7188 0.7111 -0.1386 -0.1142 -0.0093 474 HOH   A O   
6899 O O   . HOH   E .   ? 0.5407 0.5273 0.4331 0.0352  0.1414  0.0475  475 HOH   A O   
6900 O O   . HOH   E .   ? 0.4996 0.4968 0.2830 -0.0594 -0.0708 0.0655  476 HOH   A O   
6901 O O   . HOH   E .   ? 0.4319 0.3606 0.3197 -0.0236 -0.0572 -0.0358 477 HOH   A O   
6902 O O   . HOH   E .   ? 0.5075 0.3703 0.6386 -0.0032 0.0219  0.0094  478 HOH   A O   
6903 O O   . HOH   E .   ? 0.7863 0.3876 0.3217 -0.0706 -0.0635 -0.0249 479 HOH   A O   
6904 O O   . HOH   E .   ? 0.5683 0.5258 0.3839 -0.0395 0.0020  -0.1212 480 HOH   A O   
6905 O O   . HOH   E .   ? 0.5302 0.4108 0.4925 -0.2054 0.0092  0.0234  481 HOH   A O   
6906 O O   . HOH   E .   ? 0.2341 0.2308 0.2584 0.0223  -0.0028 -0.0201 482 HOH   A O   
6907 O O   . HOH   E .   ? 0.4632 0.2814 0.3073 -0.0266 -0.0683 0.0443  483 HOH   A O   
6908 O O   . HOH   E .   ? 0.2547 0.3691 0.4537 -0.0113 0.0782  -0.0876 484 HOH   A O   
6909 O O   . HOH   E .   ? 0.2684 0.5239 0.3699 0.1054  0.1082  0.2312  485 HOH   A O   
6910 O O   . HOH   E .   ? 0.3643 0.4370 0.4436 -0.0352 0.1128  0.1152  486 HOH   A O   
6911 O O   . HOH   E .   ? 0.3106 0.4616 0.3405 -0.0453 -0.0300 -0.0572 487 HOH   A O   
6912 O O   . HOH   E .   ? 0.4974 0.4334 0.3160 -0.0737 0.1054  -0.0319 488 HOH   A O   
6913 O O   . HOH   E .   ? 0.3655 0.3271 0.2563 -0.0454 0.0954  -0.0119 489 HOH   A O   
6914 O O   . HOH   E .   ? 0.6350 0.6607 0.6587 0.0563  0.0807  -0.1334 490 HOH   A O   
6915 O O   . HOH   E .   ? 0.5099 0.5876 0.3481 0.0455  0.0639  0.1257  491 HOH   A O   
6916 O O   . HOH   E .   ? 0.5218 0.5650 0.3553 -0.0969 -0.0716 -0.0496 492 HOH   A O   
6917 O O   . HOH   E .   ? 0.5657 0.5676 0.5610 -0.0766 -0.1266 0.0216  493 HOH   A O   
6918 O O   . HOH   E .   ? 0.4710 0.3043 0.3882 -0.1316 0.0832  0.0483  494 HOH   A O   
6919 O O   . HOH   E .   ? 0.3048 0.1877 0.5214 0.0009  0.0299  0.0685  495 HOH   A O   
6920 O O   . HOH   E .   ? 0.4811 0.3206 0.4791 -0.0531 0.1673  0.0561  496 HOH   A O   
6921 O O   . HOH   E .   ? 0.2583 0.2481 0.5977 -0.0149 -0.1190 0.0242  497 HOH   A O   
6922 O O   . HOH   E .   ? 0.7574 0.2779 0.4614 0.0097  0.0764  0.0924  498 HOH   A O   
6923 O O   . HOH   E .   ? 0.4115 0.8665 0.4967 -0.1090 -0.0714 0.2169  499 HOH   A O   
6924 O O   . HOH   E .   ? 0.2205 0.3324 0.3420 0.0571  -0.0468 0.0568  500 HOH   A O   
6925 O O   . HOH   E .   ? 0.4217 0.2330 0.4363 -0.1169 -0.0188 0.0610  501 HOH   A O   
6926 O O   . HOH   E .   ? 0.5121 0.6652 0.4965 0.0570  -0.0938 0.0829  502 HOH   A O   
6927 O O   . HOH   E .   ? 0.2765 0.4520 0.4151 0.0911  0.0216  0.0313  503 HOH   A O   
6928 O O   . HOH   E .   ? 0.6598 0.4893 0.5384 0.0514  -0.1467 -0.0333 504 HOH   A O   
6929 O O   . HOH   E .   ? 0.5969 0.3803 0.5338 -0.0226 -0.0015 0.0383  505 HOH   A O   
6930 O O   . HOH   E .   ? 0.3280 0.2143 0.4112 0.0073  0.0344  0.0463  506 HOH   A O   
6931 O O   . HOH   E .   ? 0.3725 0.6610 0.3278 0.0699  0.1272  -0.0531 507 HOH   A O   
6932 O O   . HOH   E .   ? 0.4132 0.6457 0.5434 0.2577  -0.0404 0.0626  508 HOH   A O   
6933 O O   . HOH   E .   ? 0.3455 0.5290 0.4414 0.0170  -0.0374 -0.1564 509 HOH   A O   
6934 O O   . HOH   E .   ? 0.2764 0.6509 0.3407 0.0788  0.0380  -0.0013 510 HOH   A O   
6935 O O   . HOH   E .   ? 0.4667 0.4767 0.4673 0.0970  0.0041  0.0873  511 HOH   A O   
6936 O O   . HOH   E .   ? 0.4403 0.6218 0.5664 -0.0690 -0.1072 -0.0108 512 HOH   A O   
6937 O O   . HOH   E .   ? 0.4268 0.3526 0.5362 -0.0834 -0.1051 0.2192  513 HOH   A O   
6938 O O   . HOH   F .   ? 0.2323 0.2325 0.2948 0.0265  0.0539  0.0295  201 HOH   B O   
6939 O O   . HOH   F .   ? 0.4901 0.4352 0.2170 0.0402  -0.0457 -0.1135 202 HOH   B O   
6940 O O   . HOH   F .   ? 0.2382 0.5318 0.4576 -0.0141 0.0987  -0.2133 203 HOH   B O   
6941 O O   . HOH   F .   ? 0.5265 0.3072 0.3250 0.0119  -0.0325 -0.1148 204 HOH   B O   
6942 O O   . HOH   F .   ? 0.6136 0.6561 0.5470 0.2640  -0.0134 0.0830  205 HOH   B O   
6943 O O   . HOH   F .   ? 0.5025 0.3761 0.6448 0.0569  -0.1000 0.2412  206 HOH   B O   
6944 O O   . HOH   F .   ? 0.2937 0.3007 0.6895 0.0700  -0.1187 0.0521  207 HOH   B O   
6945 O O   . HOH   F .   ? 0.3028 0.1982 0.4836 0.0098  0.1652  0.0803  208 HOH   B O   
6946 O O   . HOH   F .   ? 0.3536 0.6778 0.3411 0.0925  -0.0032 0.2063  209 HOH   B O   
6947 O O   . HOH   F .   ? 0.4656 0.5516 0.4433 0.2635  -0.1066 0.0368  210 HOH   B O   
6948 O O   . HOH   F .   ? 0.6635 0.3230 0.5824 0.1214  0.1707  0.0255  211 HOH   B O   
6949 O O   . HOH   F .   ? 0.3850 0.5310 0.5874 -0.0509 0.0981  -0.1259 212 HOH   B O   
6950 O O   . HOH   F .   ? 0.5563 0.6502 0.2943 0.1053  -0.0667 -0.0189 213 HOH   B O   
6951 O O   . HOH   F .   ? 0.3874 0.5381 0.3918 0.2227  -0.0340 0.0505  214 HOH   B O   
6952 O O   . HOH   F .   ? 0.1940 0.2078 0.2787 -0.0008 0.0153  -0.0143 215 HOH   B O   
6953 O O   . HOH   F .   ? 0.4222 0.4882 0.3715 -0.0432 -0.1059 0.1286  216 HOH   B O   
6954 O O   . HOH   F .   ? 0.1511 0.1768 0.2527 -0.0197 -0.0007 -0.0019 217 HOH   B O   
6955 O O   . HOH   F .   ? 0.3365 0.4868 0.4759 -0.1762 -0.0328 0.1025  218 HOH   B O   
6956 O O   . HOH   F .   ? 0.3147 0.4485 0.5955 0.0005  -0.0460 -0.0094 219 HOH   B O   
6957 O O   . HOH   F .   ? 0.2550 0.3223 0.4303 -0.0742 0.0453  -0.0632 220 HOH   B O   
6958 O O   . HOH   F .   ? 0.4743 0.4735 0.5643 -0.1348 -0.0460 -0.1299 221 HOH   B O   
6959 O O   . HOH   F .   ? 0.4180 0.4623 0.6062 -0.0437 -0.1588 -0.0766 222 HOH   B O   
6960 O O   . HOH   F .   ? 0.4380 0.4348 0.3609 0.0317  0.0715  -0.1269 223 HOH   B O   
6961 O O   . HOH   F .   ? 0.3878 0.6903 0.4057 0.2479  -0.0273 -0.0520 224 HOH   B O   
6962 O O   . HOH   F .   ? 0.2506 0.1758 0.2729 -0.0281 0.0899  0.0205  225 HOH   B O   
6963 O O   . HOH   F .   ? 0.4955 0.1825 0.4362 -0.0165 -0.1080 0.0143  226 HOH   B O   
6964 O O   . HOH   F .   ? 0.3521 0.5857 0.3873 0.2458  0.0314  -0.0230 227 HOH   B O   
6965 O O   . HOH   F .   ? 0.4673 0.3092 0.3981 -0.1603 0.0491  0.0149  228 HOH   B O   
6966 O O   . HOH   F .   ? 0.3650 0.3388 0.2327 0.0389  0.0497  0.0474  229 HOH   B O   
6967 O O   . HOH   F .   ? 0.2160 0.2065 0.1715 0.0163  -0.0132 -0.0048 230 HOH   B O   
6968 O O   . HOH   F .   ? 0.3177 0.2378 0.5382 -0.0067 0.0551  -0.0247 231 HOH   B O   
6969 O O   . HOH   F .   ? 0.1587 0.1919 0.2625 -0.0133 -0.0041 -0.0045 232 HOH   B O   
6970 O O   . HOH   F .   ? 0.2574 0.4781 0.3786 -0.1052 -0.0279 -0.0767 233 HOH   B O   
6971 O O   . HOH   F .   ? 0.2750 0.2598 0.2895 0.0366  0.0073  -0.0912 234 HOH   B O   
6972 O O   . HOH   F .   ? 0.4214 0.2387 0.3898 0.1042  -0.0727 -0.0825 235 HOH   B O   
6973 O O   . HOH   F .   ? 0.2092 0.2179 0.3592 -0.0300 -0.0265 -0.0664 236 HOH   B O   
6974 O O   . HOH   F .   ? 0.1407 0.1385 0.1832 -0.0152 -0.0062 0.0037  237 HOH   B O   
6975 O O   . HOH   F .   ? 0.1993 0.1181 0.3496 0.0151  -0.0658 -0.0384 238 HOH   B O   
6976 O O   . HOH   F .   ? 0.2981 0.2104 0.3481 0.0026  0.1100  -0.0150 239 HOH   B O   
6977 O O   . HOH   F .   ? 0.3267 0.4147 0.3967 0.0737  -0.1018 -0.1575 240 HOH   B O   
6978 O O   . HOH   F .   ? 0.2310 0.3314 0.2701 -0.0407 -0.0528 -0.0262 241 HOH   B O   
6979 O O   . HOH   F .   ? 0.1961 0.2291 0.2736 -0.0508 0.0137  -0.0411 242 HOH   B O   
6980 O O   . HOH   F .   ? 0.1343 0.1215 0.1567 -0.0030 -0.0087 0.0044  243 HOH   B O   
6981 O O   . HOH   F .   ? 0.1519 0.1434 0.2553 -0.0157 0.0063  -0.0254 244 HOH   B O   
6982 O O   . HOH   F .   ? 0.2122 0.1982 0.2160 -0.0312 -0.0483 -0.0007 245 HOH   B O   
6983 O O   . HOH   F .   ? 0.3008 0.3134 0.2032 0.0424  0.0521  0.0090  246 HOH   B O   
6984 O O   . HOH   F .   ? 0.3029 0.1643 0.5629 -0.0108 -0.1391 -0.0306 247 HOH   B O   
6985 O O   . HOH   F .   ? 0.2116 0.1316 0.2090 -0.0238 -0.0410 0.0216  248 HOH   B O   
6986 O O   . HOH   F .   ? 0.3697 0.1695 0.2415 0.0155  -0.0732 -0.0005 249 HOH   B O   
6987 O O   . HOH   F .   ? 0.4230 0.3020 0.4272 -0.2076 0.0148  -0.0071 250 HOH   B O   
6988 O O   . HOH   F .   ? 0.4233 0.3063 0.3784 -0.0572 0.0793  -0.0286 251 HOH   B O   
6989 O O   . HOH   F .   ? 0.2385 0.3536 0.2427 -0.0792 0.0170  0.0600  252 HOH   B O   
6990 O O   . HOH   F .   ? 0.2749 0.2379 0.2948 0.1017  0.0762  0.0175  253 HOH   B O   
6991 O O   . HOH   F .   ? 0.1557 0.1564 0.2724 -0.0163 -0.0280 0.0066  254 HOH   B O   
6992 O O   . HOH   F .   ? 0.2239 0.2173 0.1942 0.0224  -0.0069 0.0030  255 HOH   B O   
6993 O O   . HOH   F .   ? 0.2213 0.1957 0.3647 0.0013  -0.0512 -0.0557 256 HOH   B O   
6994 O O   . HOH   F .   ? 0.5400 0.3385 0.2453 0.1094  0.0895  -0.0090 257 HOH   B O   
6995 O O   . HOH   F .   ? 0.1885 0.3978 0.2343 -0.0203 -0.0297 0.0667  258 HOH   B O   
6996 O O   . HOH   F .   ? 0.2235 0.2123 0.2578 0.0846  -0.0844 -0.0790 259 HOH   B O   
6997 O O   . HOH   F .   ? 0.1281 0.1479 0.2036 -0.0100 -0.0059 0.0061  260 HOH   B O   
6998 O O   . HOH   F .   ? 0.2820 0.2137 0.2792 -0.0233 0.0125  -0.0451 261 HOH   B O   
6999 O O   . HOH   F .   ? 0.2031 0.1369 0.2148 -0.0310 -0.0137 0.0100  262 HOH   B O   
7000 O O   . HOH   F .   ? 0.2331 0.1997 0.3086 -0.0690 0.0222  -0.0012 263 HOH   B O   
7001 O O   . HOH   F .   ? 0.2957 0.4735 0.4291 -0.0453 -0.1240 0.1663  264 HOH   B O   
7002 O O   . HOH   F .   ? 0.2610 0.3647 0.4000 0.0301  0.1197  0.0353  265 HOH   B O   
7003 O O   . HOH   F .   ? 0.2248 0.2928 0.5099 0.0744  -0.0722 -0.0819 266 HOH   B O   
7004 O O   . HOH   F .   ? 0.2389 0.3375 0.1928 0.1182  -0.0091 0.0112  267 HOH   B O   
7005 O O   . HOH   F .   ? 0.2321 0.2675 0.2764 -0.0462 -0.0743 -0.0305 268 HOH   B O   
7006 O O   . HOH   F .   ? 0.4137 0.5308 0.5742 -0.0489 -0.1399 0.0063  269 HOH   B O   
7007 O O   . HOH   F .   ? 0.2897 0.3440 0.3285 -0.0980 0.0830  -0.1392 270 HOH   B O   
7008 O O   . HOH   F .   ? 0.2712 0.4153 0.5285 0.0069  0.0737  -0.1158 271 HOH   B O   
7009 O O   . HOH   F .   ? 0.3838 0.3746 0.4123 0.1512  -0.1136 -0.1192 272 HOH   B O   
7010 O O   . HOH   F .   ? 0.1782 0.1686 0.1638 -0.0381 -0.0402 0.0125  273 HOH   B O   
7011 O O   . HOH   F .   ? 0.6169 0.3840 0.5353 0.1724  0.0064  -0.1259 274 HOH   B O   
7012 O O   . HOH   F .   ? 0.2423 0.2763 0.5114 -0.0143 -0.0144 -0.1467 275 HOH   B O   
7013 O O   . HOH   F .   ? 0.1710 0.1418 0.4497 -0.0126 -0.0222 -0.0105 276 HOH   B O   
7014 O O   . HOH   F .   ? 0.2602 0.2676 0.2467 -0.0483 -0.0962 -0.0050 277 HOH   B O   
7015 O O   . HOH   F .   ? 0.2909 0.6724 0.2545 0.1827  -0.0343 0.0012  278 HOH   B O   
7016 O O   . HOH   F .   ? 0.2793 0.6495 0.6870 0.1694  -0.0283 -0.1238 279 HOH   B O   
7017 O O   . HOH   F .   ? 0.3850 0.3431 0.4188 -0.0673 -0.0942 -0.0220 280 HOH   B O   
7018 O O   . HOH   F .   ? 0.2743 0.2708 0.5347 -0.0320 -0.0738 0.1419  281 HOH   B O   
7019 O O   . HOH   F .   ? 0.1515 0.1457 0.1917 -0.0060 0.0107  -0.0058 282 HOH   B O   
7020 O O   . HOH   F .   ? 0.1468 0.1521 0.3149 -0.0116 0.0098  -0.0097 283 HOH   B O   
7021 O O   . HOH   F .   ? 0.2585 0.4455 0.4985 -0.0859 -0.1159 0.1008  284 HOH   B O   
7022 O O   . HOH   F .   ? 0.3999 0.3030 0.4994 -0.0486 -0.0002 0.0579  285 HOH   B O   
7023 O O   . HOH   F .   ? 0.2083 0.1397 0.2532 -0.0212 -0.0240 0.0003  286 HOH   B O   
7024 O O   . HOH   F .   ? 0.3459 0.2050 0.3756 -0.0787 -0.1917 0.0506  287 HOH   B O   
7025 O O   . HOH   F .   ? 0.2853 0.2014 0.2588 0.0113  -0.0531 0.0267  288 HOH   B O   
7026 O O   . HOH   F .   ? 0.4351 0.4685 0.2522 0.0046  0.0145  -0.1541 289 HOH   B O   
7027 O O   . HOH   F .   ? 0.2075 0.4503 0.4254 -0.0384 -0.0352 -0.1396 290 HOH   B O   
7028 O O   . HOH   F .   ? 0.4580 0.3931 0.6479 0.0887  0.0045  0.1042  291 HOH   B O   
7029 O O   . HOH   F .   ? 0.2513 0.2166 0.5062 0.0080  0.0541  0.0106  292 HOH   B O   
7030 O O   . HOH   F .   ? 0.1589 0.1751 0.2710 0.0125  -0.0170 -0.0101 293 HOH   B O   
7031 O O   . HOH   F .   ? 0.1487 0.1949 0.1679 -0.0153 -0.0230 -0.0004 294 HOH   B O   
7032 O O   . HOH   F .   ? 0.5720 0.5192 0.4565 -0.0984 -0.0288 0.1077  295 HOH   B O   
7033 O O   . HOH   F .   ? 0.2349 0.2424 0.2743 0.0223  -0.0700 0.0300  296 HOH   B O   
7034 O O   . HOH   F .   ? 0.3654 0.2930 0.2292 0.0753  -0.0988 -0.0417 297 HOH   B O   
7035 O O   . HOH   F .   ? 0.2958 0.2544 0.2268 -0.0111 0.0185  -0.0817 298 HOH   B O   
7036 O O   . HOH   F .   ? 0.1593 0.2871 0.4550 0.0154  -0.0165 -0.1047 299 HOH   B O   
7037 O O   . HOH   F .   ? 0.2356 0.6836 0.2824 0.0740  -0.0352 -0.0743 300 HOH   B O   
7038 O O   . HOH   F .   ? 0.1727 0.1482 0.2481 0.0078  -0.0008 0.0138  301 HOH   B O   
7039 O O   . HOH   F .   ? 0.4090 0.4756 0.1870 -0.0273 0.0504  0.0425  302 HOH   B O   
7040 O O   . HOH   F .   ? 0.1878 0.2451 0.6237 0.0320  -0.0438 -0.0826 303 HOH   B O   
7041 O O   . HOH   F .   ? 0.3012 0.3103 0.4072 -0.1281 0.1223  -0.0753 304 HOH   B O   
7042 O O   . HOH   F .   ? 0.5560 0.4445 0.2859 0.1395  -0.0533 -0.0460 305 HOH   B O   
7043 O O   . HOH   F .   ? 0.1522 0.1437 0.2743 0.0061  -0.0082 -0.0110 306 HOH   B O   
7044 O O   . HOH   F .   ? 0.5758 0.3559 0.3653 0.2442  0.1281  0.0729  307 HOH   B O   
7045 O O   . HOH   F .   ? 0.1525 0.1727 0.2490 -0.0204 -0.0075 0.0053  308 HOH   B O   
7046 O O   . HOH   F .   ? 0.4552 0.2888 0.2582 -0.1798 0.0588  -0.0061 309 HOH   B O   
7047 O O   . HOH   F .   ? 0.3329 0.1672 0.3219 0.0724  0.1120  0.0417  310 HOH   B O   
7048 O O   . HOH   F .   ? 0.2305 0.1489 0.3926 0.0399  -0.1424 -0.0179 311 HOH   B O   
7049 O O   . HOH   F .   ? 0.4530 0.3757 0.2367 0.1442  -0.0932 0.0499  312 HOH   B O   
7050 O O   . HOH   F .   ? 0.2227 0.1318 0.2572 -0.0124 -0.0166 0.0262  313 HOH   B O   
7051 O O   . HOH   F .   ? 0.2615 0.2885 0.3423 -0.0408 0.0845  -0.0724 314 HOH   B O   
7052 O O   . HOH   F .   ? 0.3916 0.2254 0.3098 0.1465  0.1100  0.0315  315 HOH   B O   
7053 O O   . HOH   F .   ? 0.2011 0.1907 0.1758 -0.0110 0.0114  0.0191  316 HOH   B O   
7054 O O   . HOH   F .   ? 0.2198 0.3549 0.4736 -0.0242 -0.0538 -0.0435 317 HOH   B O   
7055 O O   . HOH   F .   ? 0.4594 0.5227 0.2703 0.0687  -0.0410 0.0687  318 HOH   B O   
7056 O O   . HOH   F .   ? 0.1570 0.2619 0.2376 -0.0078 -0.0374 0.0534  319 HOH   B O   
7057 O O   . HOH   F .   ? 0.6882 0.3409 0.3138 -0.0632 0.0799  0.0889  320 HOH   B O   
7058 O O   . HOH   F .   ? 0.1546 0.1442 0.2836 -0.0070 -0.0214 -0.0112 321 HOH   B O   
7059 O O   . HOH   F .   ? 0.7758 0.4515 0.4952 0.2270  0.1142  0.0415  322 HOH   B O   
7060 O O   . HOH   F .   ? 0.4774 0.5188 0.5580 0.0545  -0.1269 0.2287  323 HOH   B O   
7061 O O   . HOH   F .   ? 0.4304 0.4251 0.2502 0.0857  -0.0237 -0.0435 324 HOH   B O   
7062 O O   . HOH   F .   ? 0.7356 0.1930 0.2705 -0.0231 -0.0678 0.0206  325 HOH   B O   
7063 O O   . HOH   F .   ? 0.2469 0.2942 0.4657 -0.0326 -0.1413 0.1065  326 HOH   B O   
7064 O O   . HOH   F .   ? 0.1894 0.1858 0.3063 0.0404  0.0325  0.0153  327 HOH   B O   
7065 O O   . HOH   F .   ? 0.4131 0.2357 0.2915 0.0362  0.0164  0.0841  328 HOH   B O   
7066 O O   . HOH   F .   ? 0.2292 0.4858 0.5072 0.0063  -0.0178 -0.0244 329 HOH   B O   
7067 O O   . HOH   F .   ? 0.5011 0.5112 0.3206 0.0057  -0.0772 0.0499  330 HOH   B O   
7068 O O   . HOH   F .   ? 0.4218 0.3360 0.5545 0.1484  0.2144  0.2021  331 HOH   B O   
7069 O O   . HOH   F .   ? 0.1775 0.2851 0.2843 0.0344  -0.0209 -0.0503 332 HOH   B O   
7070 O O   . HOH   F .   ? 0.2578 0.1916 0.5513 0.0055  -0.0290 0.0121  333 HOH   B O   
7071 O O   . HOH   F .   ? 0.7124 0.5839 0.6290 0.3318  0.0224  0.0038  334 HOH   B O   
7072 O O   . HOH   F .   ? 0.5336 0.3092 0.4216 0.0630  0.0403  -0.1551 335 HOH   B O   
7073 O O   . HOH   F .   ? 0.1658 0.1420 0.2326 0.0058  -0.0287 0.0057  336 HOH   B O   
7074 O O   . HOH   F .   ? 0.2240 0.2027 0.5127 -0.0405 0.0097  0.1220  337 HOH   B O   
7075 O O   . HOH   F .   ? 0.5343 0.5125 0.6025 -0.0543 -0.0986 -0.1123 338 HOH   B O   
7076 O O   . HOH   F .   ? 0.2873 0.3598 0.7381 -0.0354 -0.0694 0.2273  339 HOH   B O   
7077 O O   . HOH   F .   ? 0.4174 0.7401 0.2928 -0.0516 -0.0008 0.1005  340 HOH   B O   
7078 O O   . HOH   F .   ? 0.2132 0.5554 0.6484 0.0374  -0.0497 0.0459  341 HOH   B O   
7079 O O   . HOH   F .   ? 0.5452 0.3982 0.3330 0.0606  -0.1183 -0.0383 342 HOH   B O   
7080 O O   . HOH   F .   ? 0.4775 0.2761 0.5611 -0.0818 0.1877  0.0331  343 HOH   B O   
7081 O O   . HOH   F .   ? 0.3983 0.5455 0.3894 -0.1235 -0.0966 -0.0612 344 HOH   B O   
7082 O O   . HOH   F .   ? 0.4193 0.5088 0.4300 0.0005  -0.0837 0.0502  345 HOH   B O   
7083 O O   . HOH   F .   ? 0.2142 0.1754 0.2878 -0.0111 0.0527  -0.0123 346 HOH   B O   
7084 O O   . HOH   F .   ? 0.4784 0.6354 0.4127 -0.1366 0.0027  0.0673  347 HOH   B O   
7085 O O   . HOH   F .   ? 0.5892 0.5251 0.2937 -0.0081 -0.0745 0.1116  348 HOH   B O   
7086 O O   . HOH   F .   ? 0.2683 0.2199 0.4978 -0.0420 -0.0891 -0.0445 349 HOH   B O   
7087 O O   . HOH   F .   ? 0.4923 0.6576 0.6597 0.1351  0.0560  0.0083  350 HOH   B O   
7088 O O   . HOH   F .   ? 0.2213 0.5071 0.3217 0.1343  -0.0386 -0.0980 351 HOH   B O   
7089 O O   . HOH   F .   ? 0.3443 0.4216 0.4957 -0.1450 -0.0163 0.0644  352 HOH   B O   
7090 O O   . HOH   F .   ? 0.2247 0.3799 0.5791 0.0570  0.0061  0.0024  353 HOH   B O   
7091 O O   . HOH   F .   ? 0.3716 0.2375 0.3900 -0.0972 0.0339  -0.1013 354 HOH   B O   
7092 O O   . HOH   F .   ? 0.5091 0.3679 0.3861 0.1072  0.1230  -0.0184 355 HOH   B O   
7093 O O   . HOH   F .   ? 0.3151 0.1905 0.3553 0.0585  -0.1181 -0.0553 356 HOH   B O   
7094 O O   . HOH   F .   ? 0.4436 0.6444 0.5482 0.1725  -0.1250 0.1671  357 HOH   B O   
7095 O O   . HOH   F .   ? 0.3973 0.3071 0.4936 -0.1219 -0.0379 -0.0742 358 HOH   B O   
7096 O O   . HOH   F .   ? 0.4017 0.4063 0.4618 0.0458  -0.1734 -0.0616 359 HOH   B O   
7097 O O   . HOH   F .   ? 0.2298 0.3371 0.5998 -0.0675 -0.0547 -0.0894 360 HOH   B O   
7098 O O   . HOH   F .   ? 0.5442 0.3905 0.6132 -0.0193 0.1542  0.0283  361 HOH   B O   
7099 O O   . HOH   F .   ? 0.4806 0.6362 0.3077 0.1752  -0.0644 0.0554  362 HOH   B O   
7100 O O   . HOH   F .   ? 0.4586 0.5793 0.4773 -0.0922 -0.0390 0.0216  363 HOH   B O   
7101 O O   . HOH   F .   ? 0.6477 0.4795 0.4425 0.1484  0.1753  0.0877  364 HOH   B O   
7102 O O   . HOH   F .   ? 0.4652 0.5094 0.6157 0.2323  0.0921  0.1130  365 HOH   B O   
7103 O O   . HOH   F .   ? 0.4281 0.5043 0.4521 0.0007  -0.0978 -0.1158 366 HOH   B O   
7104 O O   . HOH   F .   ? 0.5525 0.3363 0.4142 0.0783  -0.1611 -0.0302 367 HOH   B O   
7105 O O   . HOH   F .   ? 0.5862 0.5163 0.3535 0.1624  -0.1207 0.0565  368 HOH   B O   
7106 O O   . HOH   F .   ? 0.5698 0.2943 0.5942 -0.1573 -0.0436 0.0002  369 HOH   B O   
7107 O O   . HOH   F .   ? 0.6861 0.4301 0.3205 -0.1373 -0.1149 -0.0691 370 HOH   B O   
7108 O O   . HOH   F .   ? 0.4404 0.3420 0.4730 0.0345  -0.1538 0.0276  371 HOH   B O   
7109 O O   . HOH   F .   ? 0.6267 0.1922 0.3976 0.0110  0.0570  0.0474  372 HOH   B O   
7110 O O   . HOH   F .   ? 0.6660 0.6564 0.5025 0.1991  -0.1407 0.0629  373 HOH   B O   
7111 O O   . HOH   F .   ? 0.4610 0.4381 0.4926 -0.1140 -0.1063 0.0679  374 HOH   B O   
7112 O O   . HOH   F .   ? 0.2371 0.4215 0.4375 0.0494  -0.0931 -0.0583 375 HOH   B O   
7113 O O   . HOH   F .   ? 0.3077 0.3954 0.2096 0.0645  0.0154  0.0261  376 HOH   B O   
7114 O O   . HOH   F .   ? 0.4731 0.6761 0.5812 0.1662  0.0409  0.2477  377 HOH   B O   
7115 O O   . HOH   F .   ? 0.7176 0.3564 0.6043 -0.0547 -0.0385 -0.0570 378 HOH   B O   
7116 O O   . HOH   F .   ? 0.3152 0.5387 0.4777 0.0553  -0.0349 0.0782  379 HOH   B O   
7117 O O   . HOH   F .   ? 0.5395 0.6641 0.5851 0.0224  0.2041  0.1342  380 HOH   B O   
7118 O O   . HOH   F .   ? 0.5054 0.7079 0.3855 -0.1313 0.0571  -0.1471 381 HOH   B O   
7119 O O   . HOH   F .   ? 0.2912 0.2578 0.3648 0.0011  0.0171  0.0424  382 HOH   B O   
7120 O O   . HOH   F .   ? 0.3715 0.7440 0.5540 0.1438  0.1718  0.1891  383 HOH   B O   
7121 O O   . HOH   F .   ? 0.5135 0.4594 0.5170 -0.0593 -0.0173 0.0118  384 HOH   B O   
7122 O O   . HOH   F .   ? 0.2520 0.4155 0.3513 -0.0945 -0.1065 -0.0051 385 HOH   B O   
7123 O O   . HOH   F .   ? 0.6643 0.5762 0.4137 0.1791  -0.0335 0.1202  386 HOH   B O   
7124 O O   . HOH   F .   ? 0.7046 0.3500 0.4362 0.0494  0.0300  -0.0983 387 HOH   B O   
7125 O O   . HOH   F .   ? 0.4518 0.4101 0.2372 0.0379  0.0158  0.0045  388 HOH   B O   
7126 O O   . HOH   F .   ? 0.4514 0.5077 0.4103 -0.0390 -0.0665 -0.0787 389 HOH   B O   
7127 O O   . HOH   F .   ? 0.3923 0.2055 0.2905 0.0810  -0.0283 0.0015  390 HOH   B O   
7128 O O   . HOH   F .   ? 0.3947 0.3541 0.3385 -0.0323 -0.0386 0.0241  391 HOH   B O   
7129 O O   . HOH   F .   ? 0.5417 0.2289 0.4448 -0.0683 0.0939  0.0482  392 HOH   B O   
7130 O O   . HOH   F .   ? 0.2379 0.3906 0.5745 -0.1236 -0.0391 -0.0157 393 HOH   B O   
7131 O O   . HOH   F .   ? 0.6311 0.7296 0.7051 0.2264  -0.0608 0.2656  394 HOH   B O   
7132 O O   . HOH   F .   ? 0.4035 0.4302 0.3866 -0.0214 0.0728  0.0511  395 HOH   B O   
7133 O O   . HOH   F .   ? 0.3405 0.4224 0.3337 0.0395  0.0102  -0.0825 396 HOH   B O   
7134 O O   . HOH   F .   ? 0.5063 0.5502 0.3646 0.1588  0.0455  -0.0421 397 HOH   B O   
7135 O O   . HOH   F .   ? 0.2185 0.2883 0.5727 -0.0710 -0.0882 0.0326  398 HOH   B O   
7136 O O   . HOH   F .   ? 0.6298 0.3951 0.3087 -0.1953 0.0342  0.1059  399 HOH   B O   
7137 O O   . HOH   F .   ? 0.5812 0.6494 0.4010 0.2190  -0.0060 0.0536  400 HOH   B O   
# 
