data_7HDK
# 
_entry.id   7HDK 
# 
_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   7HDK         pdb_00007hdk 10.2210/pdb7hdk/pdb 
WWPDB D_1001407338 ?            ?                   
# 
_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                        7HDK 
_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 'trifluoroacetic acid'                                              114.023   1   ?                      ? ? ? 
3 non-polymer syn '(2S,3R)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butane-1,3-diol' 222.244   1   ?                      ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                      35.453    1   ?                      ? ? ? 
5 water       nat water                                                               18.015    424 ?                      ? ? ? 
# 
_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 'trifluoroacetic acid'                                              TFA   
3 '(2S,3R)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butane-1,3-diol' A1A8D 
4 'CHLORIDE ION'                                                      CL    
5 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 
A1A8D non-polymer         . '(2S,3R)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butane-1,3-diol' ? 'C10 H14 N4 O2'  222.244 
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 
CL    non-polymer         . 'CHLORIDE ION'                                                      ? 'Cl -1'          35.453  
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 
TFA   non-polymer         . 'trifluoroacetic acid'                                              ? 'C2 H F3 O2'     114.023 
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 TFA   1   201 201  TFA   TFA A . 
D 3 A1A8D 1   202 201  A1A8D LA1 A . 
E 4 CL    1   203 1    CL    CL  A . 
F 5 HOH   1   301 105  HOH   HOH A . 
F 5 HOH   2   302 292  HOH   HOH A . 
F 5 HOH   3   303 153  HOH   HOH A . 
F 5 HOH   4   304 1289 HOH   HOH A . 
F 5 HOH   5   305 405  HOH   HOH A . 
F 5 HOH   6   306 196  HOH   HOH A . 
F 5 HOH   7   307 625  HOH   HOH A . 
F 5 HOH   8   308 493  HOH   HOH A . 
F 5 HOH   9   309 1301 HOH   HOH A . 
F 5 HOH   10  310 1275 HOH   HOH A . 
F 5 HOH   11  311 109  HOH   HOH A . 
F 5 HOH   12  312 209  HOH   HOH A . 
F 5 HOH   13  313 1    HOH   HOH A . 
F 5 HOH   14  314 247  HOH   HOH A . 
F 5 HOH   15  315 1295 HOH   HOH A . 
F 5 HOH   16  316 9    HOH   HOH A . 
F 5 HOH   17  317 337  HOH   HOH A . 
F 5 HOH   18  318 136  HOH   HOH A . 
F 5 HOH   19  319 76   HOH   HOH A . 
F 5 HOH   20  320 11   HOH   HOH A . 
F 5 HOH   21  321 281  HOH   HOH A . 
F 5 HOH   22  322 124  HOH   HOH A . 
F 5 HOH   23  323 236  HOH   HOH A . 
F 5 HOH   24  324 192  HOH   HOH A . 
F 5 HOH   25  325 8    HOH   HOH A . 
F 5 HOH   26  326 661  HOH   HOH A . 
F 5 HOH   27  327 1283 HOH   HOH A . 
F 5 HOH   28  328 39   HOH   HOH A . 
F 5 HOH   29  329 229  HOH   HOH A . 
F 5 HOH   30  330 151  HOH   HOH A . 
F 5 HOH   31  331 18   HOH   HOH A . 
F 5 HOH   32  332 17   HOH   HOH A . 
F 5 HOH   33  333 49   HOH   HOH A . 
F 5 HOH   34  334 225  HOH   HOH A . 
F 5 HOH   35  335 164  HOH   HOH A . 
F 5 HOH   36  336 86   HOH   HOH A . 
F 5 HOH   37  337 15   HOH   HOH A . 
F 5 HOH   38  338 21   HOH   HOH A . 
F 5 HOH   39  339 409  HOH   HOH A . 
F 5 HOH   40  340 469  HOH   HOH A . 
F 5 HOH   41  341 140  HOH   HOH A . 
F 5 HOH   42  342 33   HOH   HOH A . 
F 5 HOH   43  343 42   HOH   HOH A . 
F 5 HOH   44  344 241  HOH   HOH A . 
F 5 HOH   45  345 630  HOH   HOH A . 
F 5 HOH   46  346 57   HOH   HOH A . 
F 5 HOH   47  347 964  HOH   HOH A . 
F 5 HOH   48  348 320  HOH   HOH A . 
F 5 HOH   49  349 165  HOH   HOH A . 
F 5 HOH   50  350 393  HOH   HOH A . 
F 5 HOH   51  351 155  HOH   HOH A . 
F 5 HOH   52  352 93   HOH   HOH A . 
F 5 HOH   53  353 1300 HOH   HOH A . 
F 5 HOH   54  354 92   HOH   HOH A . 
F 5 HOH   55  355 396  HOH   HOH A . 
F 5 HOH   56  356 1310 HOH   HOH A . 
F 5 HOH   57  357 354  HOH   HOH A . 
F 5 HOH   58  358 102  HOH   HOH A . 
F 5 HOH   59  359 2    HOH   HOH A . 
F 5 HOH   60  360 70   HOH   HOH A . 
F 5 HOH   61  361 139  HOH   HOH A . 
F 5 HOH   62  362 1290 HOH   HOH A . 
F 5 HOH   63  363 66   HOH   HOH A . 
F 5 HOH   64  364 5    HOH   HOH A . 
F 5 HOH   65  365 169  HOH   HOH A . 
F 5 HOH   66  366 662  HOH   HOH A . 
F 5 HOH   67  367 26   HOH   HOH A . 
F 5 HOH   68  368 45   HOH   HOH A . 
F 5 HOH   69  369 8    HOH   HOH A . 
F 5 HOH   70  370 162  HOH   HOH A . 
F 5 HOH   71  371 939  HOH   HOH A . 
F 5 HOH   72  372 296  HOH   HOH A . 
F 5 HOH   73  373 19   HOH   HOH A . 
F 5 HOH   74  374 1308 HOH   HOH A . 
F 5 HOH   75  375 159  HOH   HOH A . 
F 5 HOH   76  376 218  HOH   HOH A . 
F 5 HOH   77  377 115  HOH   HOH A . 
F 5 HOH   78  378 148  HOH   HOH A . 
F 5 HOH   79  379 56   HOH   HOH A . 
F 5 HOH   80  380 138  HOH   HOH A . 
F 5 HOH   81  381 140  HOH   HOH A . 
F 5 HOH   82  382 195  HOH   HOH A . 
F 5 HOH   83  383 81   HOH   HOH A . 
F 5 HOH   84  384 154  HOH   HOH A . 
F 5 HOH   85  385 46   HOH   HOH A . 
F 5 HOH   86  386 36   HOH   HOH A . 
F 5 HOH   87  387 351  HOH   HOH A . 
F 5 HOH   88  388 27   HOH   HOH A . 
F 5 HOH   89  389 461  HOH   HOH A . 
F 5 HOH   90  390 134  HOH   HOH A . 
F 5 HOH   91  391 1313 HOH   HOH A . 
F 5 HOH   92  392 186  HOH   HOH A . 
F 5 HOH   93  393 74   HOH   HOH A . 
F 5 HOH   94  394 15   HOH   HOH A . 
F 5 HOH   95  395 6    HOH   HOH A . 
F 5 HOH   96  396 35   HOH   HOH A . 
F 5 HOH   97  397 58   HOH   HOH A . 
F 5 HOH   98  398 366  HOH   HOH A . 
F 5 HOH   99  399 83   HOH   HOH A . 
F 5 HOH   100 400 116  HOH   HOH A . 
F 5 HOH   101 401 1315 HOH   HOH A . 
F 5 HOH   102 402 4    HOH   HOH A . 
F 5 HOH   103 403 67   HOH   HOH A . 
F 5 HOH   104 404 303  HOH   HOH A . 
F 5 HOH   105 405 85   HOH   HOH A . 
F 5 HOH   106 406 12   HOH   HOH A . 
F 5 HOH   107 407 96   HOH   HOH A . 
F 5 HOH   108 408 121  HOH   HOH A . 
F 5 HOH   109 409 199  HOH   HOH A . 
F 5 HOH   110 410 1296 HOH   HOH A . 
F 5 HOH   111 411 78   HOH   HOH A . 
F 5 HOH   112 412 1068 HOH   HOH A . 
F 5 HOH   113 413 3    HOH   HOH A . 
F 5 HOH   114 414 34   HOH   HOH A . 
F 5 HOH   115 415 68   HOH   HOH A . 
F 5 HOH   116 416 333  HOH   HOH A . 
F 5 HOH   117 417 2    HOH   HOH A . 
F 5 HOH   118 418 25   HOH   HOH A . 
F 5 HOH   119 419 278  HOH   HOH A . 
F 5 HOH   120 420 7    HOH   HOH A . 
F 5 HOH   121 421 123  HOH   HOH A . 
F 5 HOH   122 422 156  HOH   HOH A . 
F 5 HOH   123 423 397  HOH   HOH A . 
F 5 HOH   124 424 53   HOH   HOH A . 
F 5 HOH   125 425 122  HOH   HOH A . 
F 5 HOH   126 426 125  HOH   HOH A . 
F 5 HOH   127 427 95   HOH   HOH A . 
F 5 HOH   128 428 132  HOH   HOH A . 
F 5 HOH   129 429 381  HOH   HOH A . 
F 5 HOH   130 430 51   HOH   HOH A . 
F 5 HOH   131 431 6    HOH   HOH A . 
F 5 HOH   132 432 24   HOH   HOH A . 
F 5 HOH   133 433 1222 HOH   HOH A . 
F 5 HOH   134 434 1279 HOH   HOH A . 
F 5 HOH   135 435 582  HOH   HOH A . 
F 5 HOH   136 436 73   HOH   HOH A . 
F 5 HOH   137 437 212  HOH   HOH A . 
F 5 HOH   138 438 1286 HOH   HOH A . 
F 5 HOH   139 439 1309 HOH   HOH A . 
F 5 HOH   140 440 71   HOH   HOH A . 
F 5 HOH   141 441 40   HOH   HOH A . 
F 5 HOH   142 442 80   HOH   HOH A . 
F 5 HOH   143 443 16   HOH   HOH A . 
F 5 HOH   144 444 944  HOH   HOH A . 
F 5 HOH   145 445 13   HOH   HOH A . 
F 5 HOH   146 446 94   HOH   HOH A . 
F 5 HOH   147 447 1189 HOH   HOH A . 
F 5 HOH   148 448 1238 HOH   HOH A . 
F 5 HOH   149 449 79   HOH   HOH A . 
F 5 HOH   150 450 952  HOH   HOH A . 
F 5 HOH   151 451 16   HOH   HOH A . 
F 5 HOH   152 452 97   HOH   HOH A . 
F 5 HOH   153 453 188  HOH   HOH A . 
F 5 HOH   154 454 104  HOH   HOH A . 
F 5 HOH   155 455 1094 HOH   HOH A . 
F 5 HOH   156 456 576  HOH   HOH A . 
F 5 HOH   157 457 4    HOH   HOH A . 
F 5 HOH   158 458 330  HOH   HOH A . 
F 5 HOH   159 459 1119 HOH   HOH A . 
F 5 HOH   160 460 107  HOH   HOH A . 
F 5 HOH   161 461 509  HOH   HOH A . 
F 5 HOH   162 462 1134 HOH   HOH A . 
F 5 HOH   163 463 163  HOH   HOH A . 
F 5 HOH   164 464 726  HOH   HOH A . 
F 5 HOH   165 465 408  HOH   HOH A . 
F 5 HOH   166 466 756  HOH   HOH A . 
F 5 HOH   167 467 126  HOH   HOH A . 
F 5 HOH   168 468 361  HOH   HOH A . 
F 5 HOH   169 469 14   HOH   HOH A . 
F 5 HOH   170 470 556  HOH   HOH A . 
F 5 HOH   171 471 319  HOH   HOH A . 
F 5 HOH   172 472 801  HOH   HOH A . 
F 5 HOH   173 473 1276 HOH   HOH A . 
F 5 HOH   174 474 280  HOH   HOH A . 
F 5 HOH   175 475 63   HOH   HOH A . 
F 5 HOH   176 476 342  HOH   HOH A . 
F 5 HOH   177 477 1307 HOH   HOH A . 
F 5 HOH   178 478 370  HOH   HOH A . 
F 5 HOH   179 479 250  HOH   HOH A . 
F 5 HOH   180 480 202  HOH   HOH A . 
F 5 HOH   181 481 1287 HOH   HOH A . 
F 5 HOH   182 482 267  HOH   HOH A . 
F 5 HOH   183 483 224  HOH   HOH A . 
F 5 HOH   184 484 1306 HOH   HOH A . 
F 5 HOH   185 485 674  HOH   HOH A . 
F 5 HOH   186 486 695  HOH   HOH A . 
F 5 HOH   187 487 3    HOH   HOH A . 
F 5 HOH   188 488 326  HOH   HOH A . 
F 5 HOH   189 489 135  HOH   HOH A . 
F 5 HOH   190 490 919  HOH   HOH A . 
F 5 HOH   191 491 1299 HOH   HOH A . 
F 5 HOH   192 492 318  HOH   HOH A . 
F 5 HOH   193 493 309  HOH   HOH A . 
F 5 HOH   194 494 521  HOH   HOH A . 
F 5 HOH   195 495 331  HOH   HOH A . 
F 5 HOH   196 496 315  HOH   HOH A . 
F 5 HOH   197 497 1314 HOH   HOH A . 
F 5 HOH   198 498 805  HOH   HOH A . 
F 5 HOH   199 499 711  HOH   HOH A . 
F 5 HOH   200 500 152  HOH   HOH A . 
F 5 HOH   201 501 941  HOH   HOH A . 
F 5 HOH   202 502 263  HOH   HOH A . 
F 5 HOH   203 503 356  HOH   HOH A . 
F 5 HOH   204 504 7    HOH   HOH A . 
F 5 HOH   205 505 208  HOH   HOH A . 
F 5 HOH   206 506 10   HOH   HOH A . 
F 5 HOH   207 507 1071 HOH   HOH A . 
F 5 HOH   208 508 180  HOH   HOH A . 
F 5 HOH   209 509 350  HOH   HOH A . 
F 5 HOH   210 510 363  HOH   HOH A . 
F 5 HOH   211 511 371  HOH   HOH A . 
F 5 HOH   212 512 1284 HOH   HOH A . 
F 5 HOH   213 513 313  HOH   HOH A . 
F 5 HOH   214 514 376  HOH   HOH A . 
F 5 HOH   215 515 185  HOH   HOH A . 
F 5 HOH   216 516 429  HOH   HOH A . 
F 5 HOH   217 517 70   HOH   HOH A . 
F 5 HOH   218 518 772  HOH   HOH A . 
F 5 HOH   219 519 12   HOH   HOH A . 
F 5 HOH   220 520 1074 HOH   HOH A . 
F 5 HOH   221 521 346  HOH   HOH A . 
F 5 HOH   222 522 1292 HOH   HOH A . 
F 5 HOH   223 523 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 549  HOH   HOH B . 
G 5 HOH   3   203 398  HOH   HOH B . 
G 5 HOH   4   204 900  HOH   HOH B . 
G 5 HOH   5   205 240  HOH   HOH B . 
G 5 HOH   6   206 364  HOH   HOH B . 
G 5 HOH   7   207 531  HOH   HOH B . 
G 5 HOH   8   208 358  HOH   HOH B . 
G 5 HOH   9   209 120  HOH   HOH B . 
G 5 HOH   10  210 50   HOH   HOH B . 
G 5 HOH   11  211 232  HOH   HOH B . 
G 5 HOH   12  212 743  HOH   HOH B . 
G 5 HOH   13  213 758  HOH   HOH B . 
G 5 HOH   14  214 444  HOH   HOH B . 
G 5 HOH   15  215 1249 HOH   HOH B . 
G 5 HOH   16  216 205  HOH   HOH B . 
G 5 HOH   17  217 264  HOH   HOH B . 
G 5 HOH   18  218 1140 HOH   HOH B . 
G 5 HOH   19  219 353  HOH   HOH B . 
G 5 HOH   20  220 343  HOH   HOH B . 
G 5 HOH   21  221 452  HOH   HOH B . 
G 5 HOH   22  222 654  HOH   HOH B . 
G 5 HOH   23  223 131  HOH   HOH B . 
G 5 HOH   24  224 1312 HOH   HOH B . 
G 5 HOH   25  225 332  HOH   HOH B . 
G 5 HOH   26  226 75   HOH   HOH B . 
G 5 HOH   27  227 82   HOH   HOH B . 
G 5 HOH   28  228 172  HOH   HOH B . 
G 5 HOH   29  229 276  HOH   HOH B . 
G 5 HOH   30  230 54   HOH   HOH B . 
G 5 HOH   31  231 60   HOH   HOH B . 
G 5 HOH   32  232 300  HOH   HOH B . 
G 5 HOH   33  233 128  HOH   HOH B . 
G 5 HOH   34  234 127  HOH   HOH B . 
G 5 HOH   35  235 69   HOH   HOH B . 
G 5 HOH   36  236 272  HOH   HOH B . 
G 5 HOH   37  237 166  HOH   HOH B . 
G 5 HOH   38  238 110  HOH   HOH B . 
G 5 HOH   39  239 1278 HOH   HOH B . 
G 5 HOH   40  240 1    HOH   HOH B . 
G 5 HOH   41  241 14   HOH   HOH B . 
G 5 HOH   42  242 723  HOH   HOH B . 
G 5 HOH   43  243 41   HOH   HOH B . 
G 5 HOH   44  244 129  HOH   HOH B . 
G 5 HOH   45  245 133  HOH   HOH B . 
G 5 HOH   46  246 143  HOH   HOH B . 
G 5 HOH   47  247 282  HOH   HOH B . 
G 5 HOH   48  248 325  HOH   HOH B . 
G 5 HOH   49  249 9    HOH   HOH B . 
G 5 HOH   50  250 30   HOH   HOH B . 
G 5 HOH   51  251 181  HOH   HOH B . 
G 5 HOH   52  252 52   HOH   HOH B . 
G 5 HOH   53  253 72   HOH   HOH B . 
G 5 HOH   54  254 31   HOH   HOH B . 
G 5 HOH   55  255 144  HOH   HOH B . 
G 5 HOH   56  256 150  HOH   HOH B . 
G 5 HOH   57  257 231  HOH   HOH B . 
G 5 HOH   58  258 47   HOH   HOH B . 
G 5 HOH   59  259 103  HOH   HOH B . 
G 5 HOH   60  260 347  HOH   HOH B . 
G 5 HOH   61  261 62   HOH   HOH B . 
G 5 HOH   62  262 10   HOH   HOH B . 
G 5 HOH   63  263 271  HOH   HOH B . 
G 5 HOH   64  264 252  HOH   HOH B . 
G 5 HOH   65  265 243  HOH   HOH B . 
G 5 HOH   66  266 61   HOH   HOH B . 
G 5 HOH   67  267 117  HOH   HOH B . 
G 5 HOH   68  268 175  HOH   HOH B . 
G 5 HOH   69  269 59   HOH   HOH B . 
G 5 HOH   70  270 302  HOH   HOH B . 
G 5 HOH   71  271 391  HOH   HOH B . 
G 5 HOH   72  272 77   HOH   HOH B . 
G 5 HOH   73  273 11   HOH   HOH B . 
G 5 HOH   74  274 20   HOH   HOH B . 
G 5 HOH   75  275 84   HOH   HOH B . 
G 5 HOH   76  276 147  HOH   HOH B . 
G 5 HOH   77  277 114  HOH   HOH B . 
G 5 HOH   78  278 43   HOH   HOH B . 
G 5 HOH   79  279 242  HOH   HOH B . 
G 5 HOH   80  280 221  HOH   HOH B . 
G 5 HOH   81  281 416  HOH   HOH B . 
G 5 HOH   82  282 216  HOH   HOH B . 
G 5 HOH   83  283 1277 HOH   HOH B . 
G 5 HOH   84  284 1305 HOH   HOH B . 
G 5 HOH   85  285 22   HOH   HOH B . 
G 5 HOH   86  286 99   HOH   HOH B . 
G 5 HOH   87  287 235  HOH   HOH B . 
G 5 HOH   88  288 88   HOH   HOH B . 
G 5 HOH   89  289 1106 HOH   HOH B . 
G 5 HOH   90  290 160  HOH   HOH B . 
G 5 HOH   91  291 13   HOH   HOH B . 
G 5 HOH   92  292 1066 HOH   HOH B . 
G 5 HOH   93  293 137  HOH   HOH B . 
G 5 HOH   94  294 287  HOH   HOH B . 
G 5 HOH   95  295 89   HOH   HOH B . 
G 5 HOH   96  296 220  HOH   HOH B . 
G 5 HOH   97  297 112  HOH   HOH B . 
G 5 HOH   98  298 106  HOH   HOH B . 
G 5 HOH   99  299 316  HOH   HOH B . 
G 5 HOH   100 300 311  HOH   HOH B . 
G 5 HOH   101 301 387  HOH   HOH B . 
G 5 HOH   102 302 299  HOH   HOH B . 
G 5 HOH   103 303 297  HOH   HOH B . 
G 5 HOH   104 304 635  HOH   HOH B . 
G 5 HOH   105 305 101  HOH   HOH B . 
G 5 HOH   106 306 32   HOH   HOH B . 
G 5 HOH   107 307 48   HOH   HOH B . 
G 5 HOH   108 308 142  HOH   HOH B . 
G 5 HOH   109 309 118  HOH   HOH B . 
G 5 HOH   110 310 215  HOH   HOH B . 
G 5 HOH   111 311 38   HOH   HOH B . 
G 5 HOH   112 312 141  HOH   HOH B . 
G 5 HOH   113 313 23   HOH   HOH B . 
G 5 HOH   114 314 37   HOH   HOH B . 
G 5 HOH   115 315 170  HOH   HOH B . 
G 5 HOH   116 316 1274 HOH   HOH B . 
G 5 HOH   117 317 197  HOH   HOH B . 
G 5 HOH   118 318 28   HOH   HOH B . 
G 5 HOH   119 319 1285 HOH   HOH B . 
G 5 HOH   120 320 177  HOH   HOH B . 
G 5 HOH   121 321 91   HOH   HOH B . 
G 5 HOH   122 322 445  HOH   HOH B . 
G 5 HOH   123 323 44   HOH   HOH B . 
G 5 HOH   124 324 704  HOH   HOH B . 
G 5 HOH   125 325 1291 HOH   HOH B . 
G 5 HOH   126 326 182  HOH   HOH B . 
G 5 HOH   127 327 341  HOH   HOH B . 
G 5 HOH   128 328 29   HOH   HOH B . 
G 5 HOH   129 329 100  HOH   HOH B . 
G 5 HOH   130 330 1294 HOH   HOH B . 
G 5 HOH   131 331 55   HOH   HOH B . 
G 5 HOH   132 332 161  HOH   HOH B . 
G 5 HOH   133 333 207  HOH   HOH B . 
G 5 HOH   134 334 717  HOH   HOH B . 
G 5 HOH   135 335 98   HOH   HOH B . 
G 5 HOH   136 336 334  HOH   HOH B . 
G 5 HOH   137 337 234  HOH   HOH B . 
G 5 HOH   138 338 1126 HOH   HOH B . 
G 5 HOH   139 339 65   HOH   HOH B . 
G 5 HOH   140 340 1293 HOH   HOH B . 
G 5 HOH   141 341 619  HOH   HOH B . 
G 5 HOH   142 342 339  HOH   HOH B . 
G 5 HOH   143 343 960  HOH   HOH B . 
G 5 HOH   144 344 178  HOH   HOH B . 
G 5 HOH   145 345 362  HOH   HOH B . 
G 5 HOH   146 346 90   HOH   HOH B . 
G 5 HOH   147 347 463  HOH   HOH B . 
G 5 HOH   148 348 623  HOH   HOH B . 
G 5 HOH   149 349 191  HOH   HOH B . 
G 5 HOH   150 350 335  HOH   HOH B . 
G 5 HOH   151 351 1304 HOH   HOH B . 
G 5 HOH   152 352 1280 HOH   HOH B . 
G 5 HOH   153 353 304  HOH   HOH B . 
G 5 HOH   154 354 87   HOH   HOH B . 
G 5 HOH   155 355 1046 HOH   HOH B . 
G 5 HOH   156 356 290  HOH   HOH B . 
G 5 HOH   157 357 203  HOH   HOH B . 
G 5 HOH   158 358 1077 HOH   HOH B . 
G 5 HOH   159 359 541  HOH   HOH B . 
G 5 HOH   160 360 479  HOH   HOH B . 
G 5 HOH   161 361 389  HOH   HOH B . 
G 5 HOH   162 362 718  HOH   HOH B . 
G 5 HOH   163 363 283  HOH   HOH B . 
G 5 HOH   164 364 1072 HOH   HOH B . 
G 5 HOH   165 365 1316 HOH   HOH B . 
G 5 HOH   166 366 291  HOH   HOH B . 
G 5 HOH   167 367 615  HOH   HOH B . 
G 5 HOH   168 368 898  HOH   HOH B . 
G 5 HOH   169 369 373  HOH   HOH B . 
G 5 HOH   170 370 340  HOH   HOH B . 
G 5 HOH   171 371 667  HOH   HOH B . 
G 5 HOH   172 372 1303 HOH   HOH B . 
G 5 HOH   173 373 190  HOH   HOH B . 
G 5 HOH   174 374 1173 HOH   HOH B . 
G 5 HOH   175 375 310  HOH   HOH B . 
G 5 HOH   176 376 431  HOH   HOH B . 
G 5 HOH   177 377 183  HOH   HOH B . 
G 5 HOH   178 378 149  HOH   HOH B . 
G 5 HOH   179 379 1000 HOH   HOH B . 
G 5 HOH   180 380 1163 HOH   HOH B . 
G 5 HOH   181 381 418  HOH   HOH B . 
G 5 HOH   182 382 1311 HOH   HOH B . 
G 5 HOH   183 383 176  HOH   HOH B . 
G 5 HOH   184 384 424  HOH   HOH B . 
G 5 HOH   185 385 491  HOH   HOH B . 
G 5 HOH   186 386 981  HOH   HOH B . 
G 5 HOH   187 387 248  HOH   HOH B . 
G 5 HOH   188 388 470  HOH   HOH B . 
G 5 HOH   189 389 1298 HOH   HOH B . 
G 5 HOH   190 390 265  HOH   HOH B . 
G 5 HOH   191 391 184  HOH   HOH B . 
G 5 HOH   192 392 360  HOH   HOH B . 
G 5 HOH   193 393 410  HOH   HOH B . 
G 5 HOH   194 394 355  HOH   HOH B . 
G 5 HOH   195 395 274  HOH   HOH B . 
G 5 HOH   196 396 314  HOH   HOH B . 
G 5 HOH   197 397 157  HOH   HOH B . 
G 5 HOH   198 398 566  HOH   HOH B . 
G 5 HOH   199 399 321  HOH   HOH B . 
G 5 HOH   200 400 792  HOH   HOH B . 
G 5 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HDK 
_cell.length_a           88.719 
_cell.length_b           88.719 
_cell.length_c           39.475 
_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                         7HDK 
_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          7HDK 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.52 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HDK 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.360 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   164903 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.500 
_reflns.pdbx_Rmerge_I_obs            0.043 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        15.300 
_reflns.B_iso_Wilson_estimate        12.240 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.047 
_reflns.pdbx_Rpim_I_all              0.018 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1052000 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 33896 7453 ? 1.179 ? ? ? 4.500 ? 0.900  ? ? ? ? ? ? 91.300 1.330 0.599 0.646 
1 2 5.480 44.360 ? 7534  1094 ? 0.027 ? ? ? 6.900 ? 54.200 ? ? ? ? ? ? 99.800 0.029 0.011 0.999 
# 
_refine.entry_id                                 7HDK 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             39.6800 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.4600 
_refine.ls_number_reflns_obs                     164821 
_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                          0.1445 
_refine.ls_R_factor_R_work                       0.1439 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1576 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  7957 
_refine.ls_number_reflns_R_work                  156864 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.3256 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1000 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                70.230 
_refine.B_iso_min                                9.010 
_refine.pdbx_overall_phase_error                 17.7200 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        39.6800 
_refine_hist.pdbx_number_atoms_ligand         38 
_refine_hist.number_atoms_solvent             424 
_refine_hist.number_atoms_total               3004 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           16.91 
_refine_hist.pdbx_B_iso_mean_solvent          30.48 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 89.0000  4699 . 0.3906 0.3534 . 253 0.0000 4952 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 96.0000  5006 . 0.3246 0.3287 . 214 0.0000 5220 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5248 . 0.2832 0.2841 . 272 0.0000 5520 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5172 . 0.2473 0.2605 . 269 0.0000 5441 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5222 . 0.2230 0.2251 . 323 0.0000 5545 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5204 . 0.2097 0.2375 . 248 0.0000 5452 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5234 . 0.1946 0.2112 . 265 0.0000 5499 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5250 . 0.1740 0.1989 . 242 0.0000 5492 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5239 . 0.1669 0.1780 . 286 0.0000 5525 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5234 . 0.1544 0.1636 . 239 0.0000 5473 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5258 . 0.1419 0.1711 . 264 0.0000 5522 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5238 . 0.1346 0.1523 . 261 0.0000 5499 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5149 . 0.1289 0.1572 . 291 0.0000 5440 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5336 . 0.1242 0.1467 . 229 0.0000 5565 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5188 . 0.1227 0.1392 . 258 0.0000 5446 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5261 . 0.1228 0.1463 . 280 0.0000 5541 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5218 . 0.1244 0.1406 . 281 0.0000 5499 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5229 . 0.1281 0.1444 . 280 0.0000 5509 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5274 . 0.1334 0.1657 . 247 0.0000 5521 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5228 . 0.1317 0.1670 . 271 0.0000 5499 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5291 . 0.1244 0.1241 . 245 0.0000 5536 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5227 . 0.1180 0.1299 . 278 0.0000 5505 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5283 . 0.1185 0.1363 . 267 0.0000 5550 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5263 . 0.1239 0.1448 . 260 0.0000 5523 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5286 . 0.1343 0.1366 . 250 0.0000 5536 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5268 . 0.1328 0.1309 . 283 0.0000 5551 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5272 . 0.1374 0.1410 . 289 0.0000 5561 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5294 . 0.1352 0.1447 . 287 0.0000 5581 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5318 . 0.1484 0.1647 . 256 0.0000 5574 . 'X-RAY DIFFRACTION' 
3.1100 39.6800 30 100.0000 5475 . 0.1492 0.1701 . 269 0.0000 5744 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDK 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003730' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDK 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
# 
_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 7HDK A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDK 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 7HDK SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDK MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDK SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDK 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,F 
2 1 B,G       
# 
_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 ? PHE A 168 ? ASP A 157 PHE A 168 1 ? 12 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HDK 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   HD1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HIS 
_pdbx_validate_close_contact.auth_seq_id_1    91 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    307 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.60 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.60 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.96   -133.73 
2 1 SER A 128 ? B 67.25   -1.87   
3 1 PHE A 168 ? B -138.79 -49.55  
4 1 HIS B 86  ? ? 57.64   -128.19 
# 
_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 521 ? 5.83 . 
2 1 O ? A HOH 522 ? 5.92 . 
3 1 O ? A HOH 523 ? 7.53 . 
4 1 O ? B HOH 401 ? 6.32 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER 1 ? A SER 1 
2 1 Y 1 A MET 2 ? A MET 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1A8D N2   N  Y N 1   
A1A8D C3   C  N S 2   
A1A8D C6   C  Y N 3   
A1A8D C9   C  Y N 4   
A1A8D C1   C  N N 5   
A1A8D C10  C  Y N 6   
A1A8D C2   C  N R 7   
A1A8D C4   C  N N 8   
A1A8D C5   C  Y N 9   
A1A8D C7   C  Y N 10  
A1A8D C8   C  Y N 11  
A1A8D N1   N  N N 12  
A1A8D N3   N  Y N 13  
A1A8D N4   N  Y N 14  
A1A8D O1   O  N N 15  
A1A8D O2   O  N N 16  
A1A8D H2   H  N N 17  
A1A8D H11  H  N N 18  
A1A8D H12  H  N N 19  
A1A8D H4   H  N N 20  
A1A8D H3   H  N N 21  
A1A8D H5   H  N N 22  
A1A8D H13  H  N N 23  
A1A8D H1   H  N N 24  
A1A8D H7   H  N N 25  
A1A8D H8   H  N N 26  
A1A8D H10  H  N N 27  
A1A8D H14  H  N N 28  
A1A8D H6   H  N N 29  
A1A8D H9   H  N N 30  
ALA   N    N  N N 31  
ALA   CA   C  N S 32  
ALA   C    C  N N 33  
ALA   O    O  N N 34  
ALA   CB   C  N N 35  
ALA   OXT  O  N N 36  
ALA   H    H  N N 37  
ALA   H2   H  N N 38  
ALA   HA   H  N N 39  
ALA   HB1  H  N N 40  
ALA   HB2  H  N N 41  
ALA   HB3  H  N N 42  
ALA   HXT  H  N N 43  
ARG   N    N  N N 44  
ARG   CA   C  N S 45  
ARG   C    C  N N 46  
ARG   O    O  N N 47  
ARG   CB   C  N N 48  
ARG   CG   C  N N 49  
ARG   CD   C  N N 50  
ARG   NE   N  N N 51  
ARG   CZ   C  N N 52  
ARG   NH1  N  N N 53  
ARG   NH2  N  N N 54  
ARG   OXT  O  N N 55  
ARG   H    H  N N 56  
ARG   H2   H  N N 57  
ARG   HA   H  N N 58  
ARG   HB2  H  N N 59  
ARG   HB3  H  N N 60  
ARG   HG2  H  N N 61  
ARG   HG3  H  N N 62  
ARG   HD2  H  N N 63  
ARG   HD3  H  N N 64  
ARG   HE   H  N N 65  
ARG   HH11 H  N N 66  
ARG   HH12 H  N N 67  
ARG   HH21 H  N N 68  
ARG   HH22 H  N N 69  
ARG   HXT  H  N N 70  
ASN   N    N  N N 71  
ASN   CA   C  N S 72  
ASN   C    C  N N 73  
ASN   O    O  N N 74  
ASN   CB   C  N N 75  
ASN   CG   C  N N 76  
ASN   OD1  O  N N 77  
ASN   ND2  N  N N 78  
ASN   OXT  O  N N 79  
ASN   H    H  N N 80  
ASN   H2   H  N N 81  
ASN   HA   H  N N 82  
ASN   HB2  H  N N 83  
ASN   HB3  H  N N 84  
ASN   HD21 H  N N 85  
ASN   HD22 H  N N 86  
ASN   HXT  H  N N 87  
ASP   N    N  N N 88  
ASP   CA   C  N S 89  
ASP   C    C  N N 90  
ASP   O    O  N N 91  
ASP   CB   C  N N 92  
ASP   CG   C  N N 93  
ASP   OD1  O  N N 94  
ASP   OD2  O  N N 95  
ASP   OXT  O  N N 96  
ASP   H    H  N N 97  
ASP   H2   H  N N 98  
ASP   HA   H  N N 99  
ASP   HB2  H  N N 100 
ASP   HB3  H  N N 101 
ASP   HD2  H  N N 102 
ASP   HXT  H  N N 103 
CL    CL   CL N N 104 
CYS   N    N  N N 105 
CYS   CA   C  N R 106 
CYS   C    C  N N 107 
CYS   O    O  N N 108 
CYS   CB   C  N N 109 
CYS   SG   S  N N 110 
CYS   OXT  O  N N 111 
CYS   H    H  N N 112 
CYS   H2   H  N N 113 
CYS   HA   H  N N 114 
CYS   HB2  H  N N 115 
CYS   HB3  H  N N 116 
CYS   HG   H  N N 117 
CYS   HXT  H  N N 118 
GLN   N    N  N N 119 
GLN   CA   C  N S 120 
GLN   C    C  N N 121 
GLN   O    O  N N 122 
GLN   CB   C  N N 123 
GLN   CG   C  N N 124 
GLN   CD   C  N N 125 
GLN   OE1  O  N N 126 
GLN   NE2  N  N N 127 
GLN   OXT  O  N N 128 
GLN   H    H  N N 129 
GLN   H2   H  N N 130 
GLN   HA   H  N N 131 
GLN   HB2  H  N N 132 
GLN   HB3  H  N N 133 
GLN   HG2  H  N N 134 
GLN   HG3  H  N N 135 
GLN   HE21 H  N N 136 
GLN   HE22 H  N N 137 
GLN   HXT  H  N N 138 
GLU   N    N  N N 139 
GLU   CA   C  N S 140 
GLU   C    C  N N 141 
GLU   O    O  N N 142 
GLU   CB   C  N N 143 
GLU   CG   C  N N 144 
GLU   CD   C  N N 145 
GLU   OE1  O  N N 146 
GLU   OE2  O  N N 147 
GLU   OXT  O  N N 148 
GLU   H    H  N N 149 
GLU   H2   H  N N 150 
GLU   HA   H  N N 151 
GLU   HB2  H  N N 152 
GLU   HB3  H  N N 153 
GLU   HG2  H  N N 154 
GLU   HG3  H  N N 155 
GLU   HE2  H  N N 156 
GLU   HXT  H  N N 157 
GLY   N    N  N N 158 
GLY   CA   C  N N 159 
GLY   C    C  N N 160 
GLY   O    O  N N 161 
GLY   OXT  O  N N 162 
GLY   H    H  N N 163 
GLY   H2   H  N N 164 
GLY   HA2  H  N N 165 
GLY   HA3  H  N N 166 
GLY   HXT  H  N N 167 
HIS   N    N  N N 168 
HIS   CA   C  N S 169 
HIS   C    C  N N 170 
HIS   O    O  N N 171 
HIS   CB   C  N N 172 
HIS   CG   C  Y N 173 
HIS   ND1  N  Y N 174 
HIS   CD2  C  Y N 175 
HIS   CE1  C  Y N 176 
HIS   NE2  N  Y N 177 
HIS   OXT  O  N N 178 
HIS   H    H  N N 179 
HIS   H2   H  N N 180 
HIS   HA   H  N N 181 
HIS   HB2  H  N N 182 
HIS   HB3  H  N N 183 
HIS   HD1  H  N N 184 
HIS   HD2  H  N N 185 
HIS   HE1  H  N N 186 
HIS   HE2  H  N N 187 
HIS   HXT  H  N N 188 
HOH   O    O  N N 189 
HOH   H1   H  N N 190 
HOH   H2   H  N N 191 
ILE   N    N  N N 192 
ILE   CA   C  N S 193 
ILE   C    C  N N 194 
ILE   O    O  N N 195 
ILE   CB   C  N S 196 
ILE   CG1  C  N N 197 
ILE   CG2  C  N N 198 
ILE   CD1  C  N N 199 
ILE   OXT  O  N N 200 
ILE   H    H  N N 201 
ILE   H2   H  N N 202 
ILE   HA   H  N N 203 
ILE   HB   H  N N 204 
ILE   HG12 H  N N 205 
ILE   HG13 H  N N 206 
ILE   HG21 H  N N 207 
ILE   HG22 H  N N 208 
ILE   HG23 H  N N 209 
ILE   HD11 H  N N 210 
ILE   HD12 H  N N 211 
ILE   HD13 H  N N 212 
ILE   HXT  H  N N 213 
LEU   N    N  N N 214 
LEU   CA   C  N S 215 
LEU   C    C  N N 216 
LEU   O    O  N N 217 
LEU   CB   C  N N 218 
LEU   CG   C  N N 219 
LEU   CD1  C  N N 220 
LEU   CD2  C  N N 221 
LEU   OXT  O  N N 222 
LEU   H    H  N N 223 
LEU   H2   H  N N 224 
LEU   HA   H  N N 225 
LEU   HB2  H  N N 226 
LEU   HB3  H  N N 227 
LEU   HG   H  N N 228 
LEU   HD11 H  N N 229 
LEU   HD12 H  N N 230 
LEU   HD13 H  N N 231 
LEU   HD21 H  N N 232 
LEU   HD22 H  N N 233 
LEU   HD23 H  N N 234 
LEU   HXT  H  N N 235 
LYS   N    N  N N 236 
LYS   CA   C  N S 237 
LYS   C    C  N N 238 
LYS   O    O  N N 239 
LYS   CB   C  N N 240 
LYS   CG   C  N N 241 
LYS   CD   C  N N 242 
LYS   CE   C  N N 243 
LYS   NZ   N  N N 244 
LYS   OXT  O  N N 245 
LYS   H    H  N N 246 
LYS   H2   H  N N 247 
LYS   HA   H  N N 248 
LYS   HB2  H  N N 249 
LYS   HB3  H  N N 250 
LYS   HG2  H  N N 251 
LYS   HG3  H  N N 252 
LYS   HD2  H  N N 253 
LYS   HD3  H  N N 254 
LYS   HE2  H  N N 255 
LYS   HE3  H  N N 256 
LYS   HZ1  H  N N 257 
LYS   HZ2  H  N N 258 
LYS   HZ3  H  N N 259 
LYS   HXT  H  N N 260 
MET   N    N  N N 261 
MET   CA   C  N S 262 
MET   C    C  N N 263 
MET   O    O  N N 264 
MET   CB   C  N N 265 
MET   CG   C  N N 266 
MET   SD   S  N N 267 
MET   CE   C  N N 268 
MET   OXT  O  N N 269 
MET   H    H  N N 270 
MET   H2   H  N N 271 
MET   HA   H  N N 272 
MET   HB2  H  N N 273 
MET   HB3  H  N N 274 
MET   HG2  H  N N 275 
MET   HG3  H  N N 276 
MET   HE1  H  N N 277 
MET   HE2  H  N N 278 
MET   HE3  H  N N 279 
MET   HXT  H  N N 280 
PHE   N    N  N N 281 
PHE   CA   C  N S 282 
PHE   C    C  N N 283 
PHE   O    O  N N 284 
PHE   CB   C  N N 285 
PHE   CG   C  Y N 286 
PHE   CD1  C  Y N 287 
PHE   CD2  C  Y N 288 
PHE   CE1  C  Y N 289 
PHE   CE2  C  Y N 290 
PHE   CZ   C  Y N 291 
PHE   OXT  O  N N 292 
PHE   H    H  N N 293 
PHE   H2   H  N N 294 
PHE   HA   H  N N 295 
PHE   HB2  H  N N 296 
PHE   HB3  H  N N 297 
PHE   HD1  H  N N 298 
PHE   HD2  H  N N 299 
PHE   HE1  H  N N 300 
PHE   HE2  H  N N 301 
PHE   HZ   H  N N 302 
PHE   HXT  H  N N 303 
PRO   N    N  N N 304 
PRO   CA   C  N S 305 
PRO   C    C  N N 306 
PRO   O    O  N N 307 
PRO   CB   C  N N 308 
PRO   CG   C  N N 309 
PRO   CD   C  N N 310 
PRO   OXT  O  N N 311 
PRO   H    H  N N 312 
PRO   HA   H  N N 313 
PRO   HB2  H  N N 314 
PRO   HB3  H  N N 315 
PRO   HG2  H  N N 316 
PRO   HG3  H  N N 317 
PRO   HD2  H  N N 318 
PRO   HD3  H  N N 319 
PRO   HXT  H  N N 320 
SER   N    N  N N 321 
SER   CA   C  N S 322 
SER   C    C  N N 323 
SER   O    O  N N 324 
SER   CB   C  N N 325 
SER   OG   O  N N 326 
SER   OXT  O  N N 327 
SER   H    H  N N 328 
SER   H2   H  N N 329 
SER   HA   H  N N 330 
SER   HB2  H  N N 331 
SER   HB3  H  N N 332 
SER   HG   H  N N 333 
SER   HXT  H  N N 334 
TFA   C1   C  N N 335 
TFA   C2   C  N N 336 
TFA   O    O  N N 337 
TFA   F1   F  N N 338 
TFA   F2   F  N N 339 
TFA   F3   F  N N 340 
TFA   OXT  O  N N 341 
TFA   HXT  H  N N 342 
THR   N    N  N N 343 
THR   CA   C  N S 344 
THR   C    C  N N 345 
THR   O    O  N N 346 
THR   CB   C  N R 347 
THR   OG1  O  N N 348 
THR   CG2  C  N N 349 
THR   OXT  O  N N 350 
THR   H    H  N N 351 
THR   H2   H  N N 352 
THR   HA   H  N N 353 
THR   HB   H  N N 354 
THR   HG1  H  N N 355 
THR   HG21 H  N N 356 
THR   HG22 H  N N 357 
THR   HG23 H  N N 358 
THR   HXT  H  N N 359 
TYR   N    N  N N 360 
TYR   CA   C  N S 361 
TYR   C    C  N N 362 
TYR   O    O  N N 363 
TYR   CB   C  N N 364 
TYR   CG   C  Y N 365 
TYR   CD1  C  Y N 366 
TYR   CD2  C  Y N 367 
TYR   CE1  C  Y N 368 
TYR   CE2  C  Y N 369 
TYR   CZ   C  Y N 370 
TYR   OH   O  N N 371 
TYR   OXT  O  N N 372 
TYR   H    H  N N 373 
TYR   H2   H  N N 374 
TYR   HA   H  N N 375 
TYR   HB2  H  N N 376 
TYR   HB3  H  N N 377 
TYR   HD1  H  N N 378 
TYR   HD2  H  N N 379 
TYR   HE1  H  N N 380 
TYR   HE2  H  N N 381 
TYR   HH   H  N N 382 
TYR   HXT  H  N N 383 
VAL   N    N  N N 384 
VAL   CA   C  N S 385 
VAL   C    C  N N 386 
VAL   O    O  N N 387 
VAL   CB   C  N N 388 
VAL   CG1  C  N N 389 
VAL   CG2  C  N N 390 
VAL   OXT  O  N N 391 
VAL   H    H  N N 392 
VAL   H2   H  N N 393 
VAL   HA   H  N N 394 
VAL   HB   H  N N 395 
VAL   HG11 H  N N 396 
VAL   HG12 H  N N 397 
VAL   HG13 H  N N 398 
VAL   HG21 H  N N 399 
VAL   HG22 H  N N 400 
VAL   HG23 H  N N 401 
VAL   HXT  H  N N 402 
# 
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 
A1A8D C1  C2   sing N N 1   
A1A8D C2  O1   sing N N 2   
A1A8D C2  C3   sing N N 3   
A1A8D C4  C3   sing N N 4   
A1A8D C4  O2   sing N N 5   
A1A8D C3  N1   sing N N 6   
A1A8D N1  C5   sing N N 7   
A1A8D C9  C8   sing Y N 8   
A1A8D C9  C10  doub Y N 9   
A1A8D C5  C8   doub Y N 10  
A1A8D C5  N2   sing Y N 11  
A1A8D C8  C7   sing Y N 12  
A1A8D N2  C6   doub Y N 13  
A1A8D C10 N4   sing Y N 14  
A1A8D C7  N4   sing Y N 15  
A1A8D C7  N3   doub Y N 16  
A1A8D C6  N3   sing Y N 17  
A1A8D C3  H2   sing N N 18  
A1A8D C6  H11  sing N N 19  
A1A8D C9  H12  sing N N 20  
A1A8D C1  H4   sing N N 21  
A1A8D C1  H3   sing N N 22  
A1A8D C1  H5   sing N N 23  
A1A8D C10 H13  sing N N 24  
A1A8D C2  H1   sing N N 25  
A1A8D C4  H7   sing N N 26  
A1A8D C4  H8   sing N N 27  
A1A8D N1  H10  sing N N 28  
A1A8D N4  H14  sing N N 29  
A1A8D O1  H6   sing N N 30  
A1A8D O2  H9   sing N N 31  
ALA   N   CA   sing N N 32  
ALA   N   H    sing N N 33  
ALA   N   H2   sing N N 34  
ALA   CA  C    sing N N 35  
ALA   CA  CB   sing N N 36  
ALA   CA  HA   sing N N 37  
ALA   C   O    doub N N 38  
ALA   C   OXT  sing N N 39  
ALA   CB  HB1  sing N N 40  
ALA   CB  HB2  sing N N 41  
ALA   CB  HB3  sing N N 42  
ALA   OXT HXT  sing N N 43  
ARG   N   CA   sing N N 44  
ARG   N   H    sing N N 45  
ARG   N   H2   sing N N 46  
ARG   CA  C    sing N N 47  
ARG   CA  CB   sing N N 48  
ARG   CA  HA   sing N N 49  
ARG   C   O    doub N N 50  
ARG   C   OXT  sing N N 51  
ARG   CB  CG   sing N N 52  
ARG   CB  HB2  sing N N 53  
ARG   CB  HB3  sing N N 54  
ARG   CG  CD   sing N N 55  
ARG   CG  HG2  sing N N 56  
ARG   CG  HG3  sing N N 57  
ARG   CD  NE   sing N N 58  
ARG   CD  HD2  sing N N 59  
ARG   CD  HD3  sing N N 60  
ARG   NE  CZ   sing N N 61  
ARG   NE  HE   sing N N 62  
ARG   CZ  NH1  sing N N 63  
ARG   CZ  NH2  doub N N 64  
ARG   NH1 HH11 sing N N 65  
ARG   NH1 HH12 sing N N 66  
ARG   NH2 HH21 sing N N 67  
ARG   NH2 HH22 sing N N 68  
ARG   OXT HXT  sing N N 69  
ASN   N   CA   sing N N 70  
ASN   N   H    sing N N 71  
ASN   N   H2   sing N N 72  
ASN   CA  C    sing N N 73  
ASN   CA  CB   sing N N 74  
ASN   CA  HA   sing N N 75  
ASN   C   O    doub N N 76  
ASN   C   OXT  sing N N 77  
ASN   CB  CG   sing N N 78  
ASN   CB  HB2  sing N N 79  
ASN   CB  HB3  sing N N 80  
ASN   CG  OD1  doub N N 81  
ASN   CG  ND2  sing N N 82  
ASN   ND2 HD21 sing N N 83  
ASN   ND2 HD22 sing N N 84  
ASN   OXT HXT  sing N N 85  
ASP   N   CA   sing N N 86  
ASP   N   H    sing N N 87  
ASP   N   H2   sing N N 88  
ASP   CA  C    sing N N 89  
ASP   CA  CB   sing N N 90  
ASP   CA  HA   sing N N 91  
ASP   C   O    doub N N 92  
ASP   C   OXT  sing N N 93  
ASP   CB  CG   sing N N 94  
ASP   CB  HB2  sing N N 95  
ASP   CB  HB3  sing N N 96  
ASP   CG  OD1  doub N N 97  
ASP   CG  OD2  sing N N 98  
ASP   OD2 HD2  sing N N 99  
ASP   OXT HXT  sing N N 100 
CYS   N   CA   sing N N 101 
CYS   N   H    sing N N 102 
CYS   N   H2   sing N N 103 
CYS   CA  C    sing N N 104 
CYS   CA  CB   sing N N 105 
CYS   CA  HA   sing N N 106 
CYS   C   O    doub N N 107 
CYS   C   OXT  sing N N 108 
CYS   CB  SG   sing N N 109 
CYS   CB  HB2  sing N N 110 
CYS   CB  HB3  sing N N 111 
CYS   SG  HG   sing N N 112 
CYS   OXT HXT  sing N N 113 
GLN   N   CA   sing N N 114 
GLN   N   H    sing N N 115 
GLN   N   H2   sing N N 116 
GLN   CA  C    sing N N 117 
GLN   CA  CB   sing N N 118 
GLN   CA  HA   sing N N 119 
GLN   C   O    doub N N 120 
GLN   C   OXT  sing N N 121 
GLN   CB  CG   sing N N 122 
GLN   CB  HB2  sing N N 123 
GLN   CB  HB3  sing N N 124 
GLN   CG  CD   sing N N 125 
GLN   CG  HG2  sing N N 126 
GLN   CG  HG3  sing N N 127 
GLN   CD  OE1  doub N N 128 
GLN   CD  NE2  sing N N 129 
GLN   NE2 HE21 sing N N 130 
GLN   NE2 HE22 sing N N 131 
GLN   OXT HXT  sing N N 132 
GLU   N   CA   sing N N 133 
GLU   N   H    sing N N 134 
GLU   N   H2   sing N N 135 
GLU   CA  C    sing N N 136 
GLU   CA  CB   sing N N 137 
GLU   CA  HA   sing N N 138 
GLU   C   O    doub N N 139 
GLU   C   OXT  sing N N 140 
GLU   CB  CG   sing N N 141 
GLU   CB  HB2  sing N N 142 
GLU   CB  HB3  sing N N 143 
GLU   CG  CD   sing N N 144 
GLU   CG  HG2  sing N N 145 
GLU   CG  HG3  sing N N 146 
GLU   CD  OE1  doub N N 147 
GLU   CD  OE2  sing N N 148 
GLU   OE2 HE2  sing N N 149 
GLU   OXT HXT  sing N N 150 
GLY   N   CA   sing N N 151 
GLY   N   H    sing N N 152 
GLY   N   H2   sing N N 153 
GLY   CA  C    sing N N 154 
GLY   CA  HA2  sing N N 155 
GLY   CA  HA3  sing N N 156 
GLY   C   O    doub N N 157 
GLY   C   OXT  sing N N 158 
GLY   OXT HXT  sing N N 159 
HIS   N   CA   sing N N 160 
HIS   N   H    sing N N 161 
HIS   N   H2   sing N N 162 
HIS   CA  C    sing N N 163 
HIS   CA  CB   sing N N 164 
HIS   CA  HA   sing N N 165 
HIS   C   O    doub N N 166 
HIS   C   OXT  sing N N 167 
HIS   CB  CG   sing N N 168 
HIS   CB  HB2  sing N N 169 
HIS   CB  HB3  sing N N 170 
HIS   CG  ND1  sing Y N 171 
HIS   CG  CD2  doub Y N 172 
HIS   ND1 CE1  doub Y N 173 
HIS   ND1 HD1  sing N N 174 
HIS   CD2 NE2  sing Y N 175 
HIS   CD2 HD2  sing N N 176 
HIS   CE1 NE2  sing Y N 177 
HIS   CE1 HE1  sing N N 178 
HIS   NE2 HE2  sing N N 179 
HIS   OXT HXT  sing N N 180 
HOH   O   H1   sing N N 181 
HOH   O   H2   sing N N 182 
ILE   N   CA   sing N N 183 
ILE   N   H    sing N N 184 
ILE   N   H2   sing N N 185 
ILE   CA  C    sing N N 186 
ILE   CA  CB   sing N N 187 
ILE   CA  HA   sing N N 188 
ILE   C   O    doub N N 189 
ILE   C   OXT  sing N N 190 
ILE   CB  CG1  sing N N 191 
ILE   CB  CG2  sing N N 192 
ILE   CB  HB   sing N N 193 
ILE   CG1 CD1  sing N N 194 
ILE   CG1 HG12 sing N N 195 
ILE   CG1 HG13 sing N N 196 
ILE   CG2 HG21 sing N N 197 
ILE   CG2 HG22 sing N N 198 
ILE   CG2 HG23 sing N N 199 
ILE   CD1 HD11 sing N N 200 
ILE   CD1 HD12 sing N N 201 
ILE   CD1 HD13 sing N N 202 
ILE   OXT HXT  sing N N 203 
LEU   N   CA   sing N N 204 
LEU   N   H    sing N N 205 
LEU   N   H2   sing N N 206 
LEU   CA  C    sing N N 207 
LEU   CA  CB   sing N N 208 
LEU   CA  HA   sing N N 209 
LEU   C   O    doub N N 210 
LEU   C   OXT  sing N N 211 
LEU   CB  CG   sing N N 212 
LEU   CB  HB2  sing N N 213 
LEU   CB  HB3  sing N N 214 
LEU   CG  CD1  sing N N 215 
LEU   CG  CD2  sing N N 216 
LEU   CG  HG   sing N N 217 
LEU   CD1 HD11 sing N N 218 
LEU   CD1 HD12 sing N N 219 
LEU   CD1 HD13 sing N N 220 
LEU   CD2 HD21 sing N N 221 
LEU   CD2 HD22 sing N N 222 
LEU   CD2 HD23 sing N N 223 
LEU   OXT HXT  sing N N 224 
LYS   N   CA   sing N N 225 
LYS   N   H    sing N N 226 
LYS   N   H2   sing N N 227 
LYS   CA  C    sing N N 228 
LYS   CA  CB   sing N N 229 
LYS   CA  HA   sing N N 230 
LYS   C   O    doub N N 231 
LYS   C   OXT  sing N N 232 
LYS   CB  CG   sing N N 233 
LYS   CB  HB2  sing N N 234 
LYS   CB  HB3  sing N N 235 
LYS   CG  CD   sing N N 236 
LYS   CG  HG2  sing N N 237 
LYS   CG  HG3  sing N N 238 
LYS   CD  CE   sing N N 239 
LYS   CD  HD2  sing N N 240 
LYS   CD  HD3  sing N N 241 
LYS   CE  NZ   sing N N 242 
LYS   CE  HE2  sing N N 243 
LYS   CE  HE3  sing N N 244 
LYS   NZ  HZ1  sing N N 245 
LYS   NZ  HZ2  sing N N 246 
LYS   NZ  HZ3  sing N N 247 
LYS   OXT HXT  sing N N 248 
MET   N   CA   sing N N 249 
MET   N   H    sing N N 250 
MET   N   H2   sing N N 251 
MET   CA  C    sing N N 252 
MET   CA  CB   sing N N 253 
MET   CA  HA   sing N N 254 
MET   C   O    doub N N 255 
MET   C   OXT  sing N N 256 
MET   CB  CG   sing N N 257 
MET   CB  HB2  sing N N 258 
MET   CB  HB3  sing N N 259 
MET   CG  SD   sing N N 260 
MET   CG  HG2  sing N N 261 
MET   CG  HG3  sing N N 262 
MET   SD  CE   sing N N 263 
MET   CE  HE1  sing N N 264 
MET   CE  HE2  sing N N 265 
MET   CE  HE3  sing N N 266 
MET   OXT HXT  sing N N 267 
PHE   N   CA   sing N N 268 
PHE   N   H    sing N N 269 
PHE   N   H2   sing N N 270 
PHE   CA  C    sing N N 271 
PHE   CA  CB   sing N N 272 
PHE   CA  HA   sing N N 273 
PHE   C   O    doub N N 274 
PHE   C   OXT  sing N N 275 
PHE   CB  CG   sing N N 276 
PHE   CB  HB2  sing N N 277 
PHE   CB  HB3  sing N N 278 
PHE   CG  CD1  doub Y N 279 
PHE   CG  CD2  sing Y N 280 
PHE   CD1 CE1  sing Y N 281 
PHE   CD1 HD1  sing N N 282 
PHE   CD2 CE2  doub Y N 283 
PHE   CD2 HD2  sing N N 284 
PHE   CE1 CZ   doub Y N 285 
PHE   CE1 HE1  sing N N 286 
PHE   CE2 CZ   sing Y N 287 
PHE   CE2 HE2  sing N N 288 
PHE   CZ  HZ   sing N N 289 
PHE   OXT HXT  sing N N 290 
PRO   N   CA   sing N N 291 
PRO   N   CD   sing N N 292 
PRO   N   H    sing N N 293 
PRO   CA  C    sing N N 294 
PRO   CA  CB   sing N N 295 
PRO   CA  HA   sing N N 296 
PRO   C   O    doub N N 297 
PRO   C   OXT  sing N N 298 
PRO   CB  CG   sing N N 299 
PRO   CB  HB2  sing N N 300 
PRO   CB  HB3  sing N N 301 
PRO   CG  CD   sing N N 302 
PRO   CG  HG2  sing N N 303 
PRO   CG  HG3  sing N N 304 
PRO   CD  HD2  sing N N 305 
PRO   CD  HD3  sing N N 306 
PRO   OXT HXT  sing N N 307 
SER   N   CA   sing N N 308 
SER   N   H    sing N N 309 
SER   N   H2   sing N N 310 
SER   CA  C    sing N N 311 
SER   CA  CB   sing N N 312 
SER   CA  HA   sing N N 313 
SER   C   O    doub N N 314 
SER   C   OXT  sing N N 315 
SER   CB  OG   sing N N 316 
SER   CB  HB2  sing N N 317 
SER   CB  HB3  sing N N 318 
SER   OG  HG   sing N N 319 
SER   OXT HXT  sing N N 320 
TFA   C1  C2   sing N N 321 
TFA   C1  O    doub N N 322 
TFA   C1  OXT  sing N N 323 
TFA   C2  F1   sing N N 324 
TFA   C2  F2   sing N N 325 
TFA   C2  F3   sing N N 326 
TFA   OXT HXT  sing N N 327 
THR   N   CA   sing N N 328 
THR   N   H    sing N N 329 
THR   N   H2   sing N N 330 
THR   CA  C    sing N N 331 
THR   CA  CB   sing N N 332 
THR   CA  HA   sing N N 333 
THR   C   O    doub N N 334 
THR   C   OXT  sing N N 335 
THR   CB  OG1  sing N N 336 
THR   CB  CG2  sing N N 337 
THR   CB  HB   sing N N 338 
THR   OG1 HG1  sing N N 339 
THR   CG2 HG21 sing N N 340 
THR   CG2 HG22 sing N N 341 
THR   CG2 HG23 sing N N 342 
THR   OXT HXT  sing N N 343 
TYR   N   CA   sing N N 344 
TYR   N   H    sing N N 345 
TYR   N   H2   sing N N 346 
TYR   CA  C    sing N N 347 
TYR   CA  CB   sing N N 348 
TYR   CA  HA   sing N N 349 
TYR   C   O    doub N N 350 
TYR   C   OXT  sing N N 351 
TYR   CB  CG   sing N N 352 
TYR   CB  HB2  sing N N 353 
TYR   CB  HB3  sing N N 354 
TYR   CG  CD1  doub Y N 355 
TYR   CG  CD2  sing Y N 356 
TYR   CD1 CE1  sing Y N 357 
TYR   CD1 HD1  sing N N 358 
TYR   CD2 CE2  doub Y N 359 
TYR   CD2 HD2  sing N N 360 
TYR   CE1 CZ   doub Y N 361 
TYR   CE1 HE1  sing N N 362 
TYR   CE2 CZ   sing Y N 363 
TYR   CE2 HE2  sing N N 364 
TYR   CZ  OH   sing N N 365 
TYR   OH  HH   sing N N 366 
TYR   OXT HXT  sing N N 367 
VAL   N   CA   sing N N 368 
VAL   N   H    sing N N 369 
VAL   N   H2   sing N N 370 
VAL   CA  C    sing N N 371 
VAL   CA  CB   sing N N 372 
VAL   CA  HA   sing N N 373 
VAL   C   O    doub N N 374 
VAL   C   OXT  sing N N 375 
VAL   CB  CG1  sing N N 376 
VAL   CB  CG2  sing N N 377 
VAL   CB  HB   sing N N 378 
VAL   CG1 HG11 sing N N 379 
VAL   CG1 HG12 sing N N 380 
VAL   CG1 HG13 sing N N 381 
VAL   CG2 HG21 sing N N 382 
VAL   CG2 HG22 sing N N 383 
VAL   CG2 HG23 sing N N 384 
VAL   OXT HXT  sing N N 385 
# 
_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                    7HDK 
_atom_sites.fract_transf_matrix[1][1]   0.011272 
_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]   0.011272 
_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]   0.025332 
_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  
CL 
F  
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    A VAL   A 1 3   ? 19.663 -16.178 22.234  0.72 56.55 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.594 -16.149 22.343  0.28 55.66 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.692 -15.107 22.421  0.72 56.17 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.643 -15.059 22.518  0.28 55.38 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.338 -13.755 22.137  0.72 54.66 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.305 -13.724 22.197  0.28 54.21 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.450 -13.482 22.588  0.72 55.12 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.400 -13.435 22.678  0.28 54.62 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.072 -15.154 23.833  0.72 56.94 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.049 -15.055 23.941  0.28 55.97 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.050 -14.039 24.006  0.72 57.17 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.042 -13.924 24.094  0.28 56.16 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.432 -16.513 24.085  0.72 57.16 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.404 -16.397 24.253  0.28 56.14 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.972 -15.224 21.786  0.72 67.45 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.909 -15.179 21.898  0.28 66.50 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.770 -15.026 24.494  0.72 68.37 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.762 -14.911 24.582  0.28 67.22 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.551 -14.193 24.824  0.72 68.65 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.554 -14.047 24.923  0.28 67.44 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.512 -13.188 24.057  0.72 68.65 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.515 -13.078 24.113  0.28 67.44 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.446 -14.044 23.247  0.72 68.65 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.428 -13.945 23.344  0.28 67.44 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.984 -16.497 24.945  0.72 68.63 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 16.971 -16.345 25.119  0.28 67.42 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.790 -16.694 23.381  0.72 68.63 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.749 -16.599 23.567  0.28 67.42 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.123 -17.193 24.085  0.72 68.63 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.090 -17.082 24.267  0.28 67.42 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.635 -12.915 21.377  1.00 52.32 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.093 -11.570 21.047  1.00 47.74 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 17.970 -10.576 21.332  1.00 43.19 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.858 -10.955 21.715  1.00 43.28 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.624 -11.476 19.609  1.00 47.31 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.600 -11.888 18.575  1.00 46.81 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.470 -11.402 18.573  1.00 46.64 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 18.994 -12.793 17.684  1.00 46.70 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.871 -13.112 21.033  0.72 62.83 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.894 -13.130 20.995  0.28 62.83 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.829 -11.349 21.630  1.00 57.33 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 19.882 -10.556 19.428  1.00 56.82 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.395 -12.057 19.518  1.00 56.82 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.453 -13.061 17.072  1.00 56.08 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.794 -13.112 17.719  1.00 56.08 ?  4   ASN   A HD22 1 
ATOM   46   N  N    A SER   A 1 5   ? 18.252 -9.291  21.119  0.72 40.49 ?  5   SER   A N    1 
ATOM   47   N  N    B SER   A 1 5   ? 18.282 -9.293  21.161  0.28 40.87 ?  5   SER   A N    1 
ATOM   48   C  CA   A SER   A 1 5   ? 17.337 -8.221  21.499  0.72 37.64 ?  5   SER   A CA   1 
ATOM   49   C  CA   B SER   A 1 5   ? 17.379 -8.209  21.527  0.28 38.36 ?  5   SER   A CA   1 
ATOM   50   C  C    A SER   A 1 5   ? 16.461 -7.728  20.348  0.72 33.76 ?  5   SER   A C    1 
ATOM   51   C  C    B SER   A 1 5   ? 16.516 -7.731  20.367  0.28 34.92 ?  5   SER   A C    1 
ATOM   52   O  O    A SER   A 1 5   ? 15.811 -6.687  20.486  0.72 34.01 ?  5   SER   A O    1 
ATOM   53   O  O    B SER   A 1 5   ? 15.762 -6.767  20.534  0.28 35.09 ?  5   SER   A O    1 
ATOM   54   C  CB   A SER   A 1 5   ? 18.111 -7.049  22.108  0.72 38.59 ?  5   SER   A CB   1 
ATOM   55   C  CB   B SER   A 1 5   ? 18.172 -7.033  22.111  0.28 39.13 ?  5   SER   A CB   1 
ATOM   56   O  OG   A SER   A 1 5   ? 19.050 -6.521  21.188  0.72 39.12 ?  5   SER   A OG   1 
ATOM   57   O  OG   B SER   A 1 5   ? 19.070 -6.492  21.157  0.28 39.55 ?  5   SER   A OG   1 
ATOM   58   H  H    A SER   A 1 5   ? 18.976 -9.015  20.747  0.72 48.64 ?  5   SER   A H    1 
ATOM   59   H  H    B SER   A 1 5   ? 19.026 -9.024  20.825  0.28 49.09 ?  5   SER   A H    1 
ATOM   60   H  HA   A SER   A 1 5   ? 16.748 -8.559  22.190  0.72 45.21 ?  5   SER   A HA   1 
ATOM   61   H  HA   B SER   A 1 5   ? 16.783 -8.525  22.219  0.28 46.07 ?  5   SER   A HA   1 
ATOM   62   H  HB2  A SER   A 1 5   ? 17.483 -6.349  22.353  0.72 46.36 ?  5   SER   A HB2  1 
ATOM   63   H  HB2  B SER   A 1 5   ? 17.550 -6.341  22.388  0.28 47.00 ?  5   SER   A HB2  1 
ATOM   64   H  HB3  A SER   A 1 5   ? 18.582 -7.358  22.899  0.72 46.36 ?  5   SER   A HB3  1 
ATOM   65   H  HB3  B SER   A 1 5   ? 18.679 -7.345  22.879  0.28 47.00 ?  5   SER   A HB3  1 
ATOM   66   H  HG   A SER   A 1 5   ? 19.467 -5.881  21.540  0.72 46.99 ?  5   SER   A HG   1 
ATOM   67   H  HG   B SER   A 1 5   ? 19.494 -5.848  21.495  0.28 47.51 ?  5   SER   A HG   1 
ATOM   68   N  N    A PHE   A 1 6   ? 16.423 -8.441  19.224  0.72 29.36 ?  6   PHE   A N    1 
ATOM   69   N  N    B PHE   A 1 6   ? 16.604 -8.371  19.201  0.28 31.17 ?  6   PHE   A N    1 
ATOM   70   C  CA   A PHE   A 1 6   ? 15.520 -8.065  18.143  0.72 25.05 ?  6   PHE   A CA   1 
ATOM   71   C  CA   B PHE   A 1 6   ? 15.712 -8.042  18.096  0.28 27.48 ?  6   PHE   A CA   1 
ATOM   72   C  C    A PHE   A 1 6   ? 14.087 -8.429  18.513  0.72 24.39 ?  6   PHE   A C    1 
ATOM   73   C  C    B PHE   A 1 6   ? 14.273 -8.355  18.489  0.28 26.22 ?  6   PHE   A C    1 
ATOM   74   O  O    A PHE   A 1 6   ? 13.833 -9.489  19.090  0.72 25.26 ?  6   PHE   A O    1 
ATOM   75   O  O    B PHE   A 1 6   ? 13.887 -9.525  18.578  0.28 25.98 ?  6   PHE   A O    1 
ATOM   76   C  CB   A PHE   A 1 6   ? 15.914 -8.773  16.850  0.72 22.45 ?  6   PHE   A CB   1 
ATOM   77   C  CB   B PHE   A 1 6   ? 16.106 -8.811  16.834  0.28 25.35 ?  6   PHE   A CB   1 
ATOM   78   C  CG   A PHE   A 1 6   ? 17.191 -8.257  16.242  0.72 20.55 ?  6   PHE   A CG   1 
ATOM   79   C  CG   B PHE   A 1 6   ? 17.388 -8.334  16.206  0.28 23.56 ?  6   PHE   A CG   1 
ATOM   80   C  CD1  A PHE   A 1 6   ? 17.201 -7.073  15.528  0.72 19.86 ?  6   PHE   A CD1  1 
ATOM   81   C  CD1  B PHE   A 1 6   ? 17.431 -7.132  15.519  0.28 22.76 ?  6   PHE   A CD1  1 
ATOM   82   C  CD2  A PHE   A 1 6   ? 18.374 -8.960  16.385  0.72 20.86 ?  6   PHE   A CD2  1 
ATOM   83   C  CD2  B PHE   A 1 6   ? 18.545 -9.091  16.293  0.28 23.01 ?  6   PHE   A CD2  1 
ATOM   84   C  CE1  A PHE   A 1 6   ? 18.372 -6.594  14.967  0.72 19.68 ?  6   PHE   A CE1  1 
ATOM   85   C  CE1  B PHE   A 1 6   ? 18.605 -6.689  14.937  0.28 22.32 ?  6   PHE   A CE1  1 
ATOM   86   C  CE2  A PHE   A 1 6   ? 19.545 -8.491  15.826  0.72 20.84 ?  6   PHE   A CE2  1 
ATOM   87   C  CE2  B PHE   A 1 6   ? 19.723 -8.654  15.711  0.28 22.59 ?  6   PHE   A CE2  1 
ATOM   88   C  CZ   A PHE   A 1 6   ? 19.545 -7.305  15.116  0.72 20.18 ?  6   PHE   A CZ   1 
ATOM   89   C  CZ   B PHE   A 1 6   ? 19.752 -7.452  15.032  0.28 22.29 ?  6   PHE   A CZ   1 
ATOM   90   H  H    A PHE   A 1 6   ? 16.902 -9.138  19.069  0.72 35.28 ?  6   PHE   A H    1 
ATOM   91   H  H    B PHE   A 1 6   ? 17.172 -8.993  19.027  0.28 37.45 ?  6   PHE   A H    1 
ATOM   92   H  HA   A PHE   A 1 6   ? 15.561 -7.113  18.007  0.72 30.11 ?  6   PHE   A HA   1 
ATOM   93   H  HA   B PHE   A 1 6   ? 15.774 -7.094  17.908  0.28 33.03 ?  6   PHE   A HA   1 
ATOM   94   H  HB2  A PHE   A 1 6   ? 16.026 -9.721  17.038  0.72 26.98 ?  6   PHE   A HB2  1 
ATOM   95   H  HB2  B PHE   A 1 6   ? 16.217 -9.748  17.061  0.28 30.47 ?  6   PHE   A HB2  1 
ATOM   96   H  HB3  A PHE   A 1 6   ? 15.199 -8.654  16.205  0.72 26.98 ?  6   PHE   A HB3  1 
ATOM   97   H  HB3  B PHE   A 1 6   ? 15.400 -8.713  16.177  0.28 30.47 ?  6   PHE   A HB3  1 
ATOM   98   H  HD1  A PHE   A 1 6   ? 16.408 -6.592  15.428  0.72 23.89 ?  6   PHE   A HD1  1 
ATOM   99   H  HD1  B PHE   A 1 6   ? 16.663 -6.615  15.453  0.28 27.36 ?  6   PHE   A HD1  1 
ATOM   100  H  HD2  A PHE   A 1 6   ? 18.377 -9.759  16.867  0.72 25.08 ?  6   PHE   A HD2  1 
ATOM   101  H  HD2  B PHE   A 1 6   ? 18.531 -9.901  16.749  0.28 27.66 ?  6   PHE   A HD2  1 
ATOM   102  H  HE1  A PHE   A 1 6   ? 18.365 -5.796  14.490  0.72 23.66 ?  6   PHE   A HE1  1 
ATOM   103  H  HE1  B PHE   A 1 6   ? 18.623 -5.879  14.480  0.28 26.83 ?  6   PHE   A HE1  1 
ATOM   104  H  HE2  A PHE   A 1 6   ? 20.336 -8.968  15.931  0.72 25.06 ?  6   PHE   A HE2  1 
ATOM   105  H  HE2  B PHE   A 1 6   ? 20.495 -9.170  15.777  0.28 27.15 ?  6   PHE   A HE2  1 
ATOM   106  H  HZ   A PHE   A 1 6   ? 20.330 -6.984  14.741  0.72 24.26 ?  6   PHE   A HZ   1 
ATOM   107  H  HZ   B PHE   A 1 6   ? 20.543 -7.156  14.641  0.28 26.79 ?  6   PHE   A HZ   1 
ATOM   108  N  N    A SER   A 1 7   ? 13.141 -7.550  18.175  0.72 22.71 ?  7   SER   A N    1 
ATOM   109  N  N    B SER   A 1 7   ? 13.475 -7.317  18.720  0.28 25.33 ?  7   SER   A N    1 
ATOM   110  C  CA   A SER   A 1 7   ? 11.767 -7.679  18.652  0.72 22.61 ?  7   SER   A CA   1 
ATOM   111  C  CA   B SER   A 1 7   ? 12.130 -7.454  19.258  0.28 24.77 ?  7   SER   A CA   1 
ATOM   112  C  C    A SER   A 1 7   ? 10.767 -7.407  17.534  0.72 20.06 ?  7   SER   A C    1 
ATOM   113  C  C    B SER   A 1 7   ? 11.096 -7.165  18.178  0.28 23.32 ?  7   SER   A C    1 
ATOM   114  O  O    A SER   A 1 7   ? 10.972 -6.516  16.707  0.72 19.92 ?  7   SER   A O    1 
ATOM   115  O  O    B SER   A 1 7   ? 11.238 -6.212  17.406  0.28 23.51 ?  7   SER   A O    1 
ATOM   116  C  CB   A SER   A 1 7   ? 11.511 -6.710  19.815  0.72 24.78 ?  7   SER   A CB   1 
ATOM   117  C  CB   B SER   A 1 7   ? 11.927 -6.492  20.434  0.28 25.45 ?  7   SER   A CB   1 
ATOM   118  O  OG   A SER   A 1 7   ? 10.181 -6.818  20.286  0.72 26.04 ?  7   SER   A OG   1 
ATOM   119  O  OG   B SER   A 1 7   ? 10.554 -6.342  20.744  0.28 25.95 ?  7   SER   A OG   1 
ATOM   120  H  H    A SER   A 1 7   ? 13.272 -6.876  17.663  0.72 27.31 ?  7   SER   A H    1 
ATOM   121  H  H    B SER   A 1 7   ? 13.698 -6.500  18.564  0.28 30.44 ?  7   SER   A H    1 
ATOM   122  H  HA   A SER   A 1 7   ? 11.619 -8.580  18.975  0.72 27.18 ?  7   SER   A HA   1 
ATOM   123  H  HA   B SER   A 1 7   ? 11.996 -8.359  19.578  0.28 29.77 ?  7   SER   A HA   1 
ATOM   124  H  HB2  A SER   A 1 7   ? 12.122 -6.921  20.541  0.72 29.78 ?  7   SER   A HB2  1 
ATOM   125  H  HB2  B SER   A 1 7   ? 12.383 -6.848  21.215  0.28 30.58 ?  7   SER   A HB2  1 
ATOM   126  H  HB3  A SER   A 1 7   ? 11.666 -5.801  19.510  0.72 29.78 ?  7   SER   A HB3  1 
ATOM   127  H  HB3  B SER   A 1 7   ? 12.297 -5.626  20.203  0.28 30.58 ?  7   SER   A HB3  1 
ATOM   128  H  HG   A SER   A 1 7   ? 10.059 -6.282  20.922  0.72 31.29 ?  7   SER   A HG   1 
ATOM   129  H  HG   B SER   A 1 7   ? 10.460 -5.808  21.386  0.28 31.19 ?  7   SER   A HG   1 
ATOM   130  N  N    A GLY   A 1 8   ? 9.675  -8.176  17.522  0.72 18.21 ?  8   GLY   A N    1 
ATOM   131  N  N    B GLY   A 1 8   ? 10.062 -8.000  18.124  0.28 21.80 ?  8   GLY   A N    1 
ATOM   132  C  CA   A GLY   A 1 8   ? 8.594  -7.940  16.584  0.72 17.14 ?  8   GLY   A CA   1 
ATOM   133  C  CA   B GLY   A 1 8   ? 8.934  -7.765  17.249  0.28 20.15 ?  8   GLY   A CA   1 
ATOM   134  C  C    A GLY   A 1 8   ? 8.816  -8.458  15.182  0.72 15.70 ?  8   GLY   A C    1 
ATOM   135  C  C    B GLY   A 1 8   ? 9.073  -8.280  15.836  0.28 18.62 ?  8   GLY   A C    1 
ATOM   136  O  O    A GLY   A 1 8   ? 8.084  -8.064  14.268  0.72 16.31 ?  8   GLY   A O    1 
ATOM   137  O  O    B GLY   A 1 8   ? 8.257  -7.911  14.983  0.28 18.49 ?  8   GLY   A O    1 
ATOM   138  H  H    A GLY   A 1 8   ? 9.543  -8.837  18.050  0.72 21.90 ?  8   GLY   A H    1 
ATOM   139  H  H    B GLY   A 1 8   ? 9.994  -8.716  18.594  0.28 26.21 ?  8   GLY   A H    1 
ATOM   140  H  HA2  A GLY   A 1 8   ? 7.785  -8.351  16.933  0.72 20.61 ?  8   GLY   A HA2  1 
ATOM   141  H  HA2  B GLY   A 1 8   ? 8.150  -8.186  17.627  0.28 24.23 ?  8   GLY   A HA2  1 
ATOM   142  H  HA3  A GLY   A 1 8   ? 8.436  -6.986  16.519  0.72 20.61 ?  8   GLY   A HA3  1 
ATOM   143  H  HA3  B GLY   A 1 8   ? 8.769  -6.811  17.200  0.28 24.23 ?  8   GLY   A HA3  1 
ATOM   144  N  N    A TYR   A 1 9   ? 9.798  -9.333  14.974  0.72 14.57 ?  9   TYR   A N    1 
ATOM   145  N  N    B TYR   A 1 9   ? 10.066 -9.118  15.554  0.28 17.36 ?  9   TYR   A N    1 
ATOM   146  C  CA   A TYR   A 1 9   ? 10.075 -9.877  13.653  0.72 13.29 ?  9   TYR   A CA   1 
ATOM   147  C  CA   B TYR   A 1 9   ? 10.248 -9.625  14.203  0.28 16.24 ?  9   TYR   A CA   1 
ATOM   148  C  C    A TYR   A 1 9   ? 9.219  -11.104 13.377  0.72 12.92 ?  9   TYR   A C    1 
ATOM   149  C  C    B TYR   A 1 9   ? 9.348  -10.828 13.941  0.28 15.26 ?  9   TYR   A C    1 
ATOM   150  O  O    A TYR   A 1 9   ? 8.961  -11.920 14.266  0.72 14.29 ?  9   TYR   A O    1 
ATOM   151  O  O    B TYR   A 1 9   ? 8.980  -11.573 14.854  0.28 15.87 ?  9   TYR   A O    1 
ATOM   152  C  CB   A TYR   A 1 9   ? 11.554 -10.262 13.512  0.72 13.85 ?  9   TYR   A CB   1 
ATOM   153  C  CB   B TYR   A 1 9   ? 11.710 -10.012 13.962  0.28 16.15 ?  9   TYR   A CB   1 
ATOM   154  C  CG   A TYR   A 1 9   ? 12.465 -9.068  13.349  0.72 14.37 ?  9   TYR   A CG   1 
ATOM   155  C  CG   B TYR   A 1 9   ? 12.624 -8.827  13.729  0.28 15.84 ?  9   TYR   A CG   1 
ATOM   156  C  CD1  A TYR   A 1 9   ? 12.798 -8.283  14.439  0.72 15.28 ?  9   TYR   A CD1  1 
ATOM   157  C  CD1  B TYR   A 1 9   ? 12.951 -7.965  14.765  0.28 16.11 ?  9   TYR   A CD1  1 
ATOM   158  C  CD2  A TYR   A 1 9   ? 12.967 -8.713  12.102  0.72 14.17 ?  9   TYR   A CD2  1 
ATOM   159  C  CD2  B TYR   A 1 9   ? 13.158 -8.572  12.471  0.28 15.59 ?  9   TYR   A CD2  1 
ATOM   160  C  CE1  A TYR   A 1 9   ? 13.605 -7.174  14.300  0.72 16.12 ?  9   TYR   A CE1  1 
ATOM   161  C  CE1  B TYR   A 1 9   ? 13.780 -6.880  14.558  0.28 16.39 ?  9   TYR   A CE1  1 
ATOM   162  C  CE2  A TYR   A 1 9   ? 13.781 -7.609  11.949  0.72 14.81 ?  9   TYR   A CE2  1 
ATOM   163  C  CE2  B TYR   A 1 9   ? 13.987 -7.486  12.253  0.28 15.94 ?  9   TYR   A CE2  1 
ATOM   164  C  CZ   A TYR   A 1 9   ? 14.092 -6.841  13.049  0.72 15.86 ?  9   TYR   A CZ   1 
ATOM   165  C  CZ   B TYR   A 1 9   ? 14.294 -6.645  13.302  0.28 16.53 ?  9   TYR   A CZ   1 
ATOM   166  O  OH   A TYR   A 1 9   ? 14.891 -5.741  12.890  0.72 17.07 ?  9   TYR   A OH   1 
ATOM   167  O  OH   B TYR   A 1 9   ? 15.119 -5.564  13.094  0.28 17.46 ?  9   TYR   A OH   1 
ATOM   168  H  H    A TYR   A 1 9   ? 10.310 -9.638  15.589  0.72 17.54 ?  9   TYR   A H    1 
ATOM   169  H  H    B TYR   A 1 9   ? 10.649 -9.402  16.124  0.28 20.88 ?  9   TYR   A H    1 
ATOM   170  H  HA   A TYR   A 1 9   ? 9.872  -9.210  12.981  0.72 15.99 ?  9   TYR   A HA   1 
ATOM   171  H  HA   B TYR   A 1 9   ? 10.019 -8.926  13.572  0.28 19.54 ?  9   TYR   A HA   1 
ATOM   172  H  HB2  A TYR   A 1 9   ? 11.831 -10.752 14.303  0.72 16.67 ?  9   TYR   A HB2  1 
ATOM   173  H  HB2  B TYR   A 1 9   ? 12.044 -10.500 14.729  0.28 19.43 ?  9   TYR   A HB2  1 
ATOM   174  H  HB3  A TYR   A 1 9   ? 11.649 -10.825 12.727  0.72 16.67 ?  9   TYR   A HB3  1 
ATOM   175  H  HB3  B TYR   A 1 9   ? 11.751 -10.574 13.172  0.28 19.43 ?  9   TYR   A HB3  1 
ATOM   176  H  HD1  A TYR   A 1 9   ? 12.459 -8.505  15.279  0.72 18.39 ?  9   TYR   A HD1  1 
ATOM   177  H  HD1  B TYR   A 1 9   ? 12.604 -8.120  15.613  0.28 19.38 ?  9   TYR   A HD1  1 
ATOM   178  H  HD2  A TYR   A 1 9   ? 12.748 -9.230  11.356  0.72 17.05 ?  9   TYR   A HD2  1 
ATOM   179  H  HD2  B TYR   A 1 9   ? 12.952 -9.138  11.762  0.28 18.75 ?  9   TYR   A HD2  1 
ATOM   180  H  HE1  A TYR   A 1 9   ? 13.820 -6.658  15.042  0.72 19.39 ?  9   TYR   A HE1  1 
ATOM   181  H  HE1  B TYR   A 1 9   ? 13.988 -6.309  15.262  0.28 19.71 ?  9   TYR   A HE1  1 
ATOM   182  H  HE2  A TYR   A 1 9   ? 14.111 -7.383  11.110  0.72 17.82 ?  9   TYR   A HE2  1 
ATOM   183  H  HE2  B TYR   A 1 9   ? 14.340 -7.326  11.406  0.28 19.17 ?  9   TYR   A HE2  1 
ATOM   184  H  HH   A TYR   A 1 9   ? 15.023 -5.373  13.632  0.72 20.54 ?  9   TYR   A HH   1 
ATOM   185  H  HH   B TYR   A 1 9   ? 15.219 -5.138  13.811  0.28 21.00 ?  9   TYR   A HH   1 
ATOM   186  N  N    A LEU   A 1 10  ? 8.800  -11.235 12.126  0.72 12.52 ?  10  LEU   A N    1 
ATOM   187  N  N    B LEU   A 1 10  ? 8.984  -10.996 12.672  0.28 14.30 ?  10  LEU   A N    1 
ATOM   188  C  CA   A LEU   A 1 10  ? 8.197  -12.464 11.630  0.72 12.28 ?  10  LEU   A CA   1 
ATOM   189  C  CA   B LEU   A 1 10  ? 8.285  -12.179 12.194  0.28 14.03 ?  10  LEU   A CA   1 
ATOM   190  C  C    A LEU   A 1 10  ? 9.314  -13.411 11.190  0.72 12.07 ?  10  LEU   A C    1 
ATOM   191  C  C    B LEU   A 1 10  ? 9.323  -13.157 11.658  0.28 13.39 ?  10  LEU   A C    1 
ATOM   192  O  O    A LEU   A 1 10  ? 10.256 -12.997 10.507  0.72 12.57 ?  10  LEU   A O    1 
ATOM   193  O  O    B LEU   A 1 10  ? 10.192 -12.777 10.868  0.28 13.21 ?  10  LEU   A O    1 
ATOM   194  C  CB   A LEU   A 1 10  ? 7.288  -12.135 10.447  0.72 12.94 ?  10  LEU   A CB   1 
ATOM   195  C  CB   B LEU   A 1 10  ? 7.316  -11.790 11.076  0.28 14.46 ?  10  LEU   A CB   1 
ATOM   196  C  CG   A LEU   A 1 10  ? 6.592  -13.316 9.773   0.72 15.27 ?  10  LEU   A CG   1 
ATOM   197  C  CG   B LEU   A 1 10  ? 6.548  -12.908 10.370  0.28 15.19 ?  10  LEU   A CG   1 
ATOM   198  C  CD1  A LEU   A 1 10  ? 5.578  -13.939 10.704  0.72 16.58 ?  10  LEU   A CD1  1 
ATOM   199  C  CD1  B LEU   A 1 10  ? 5.564  -13.564 11.319  0.28 15.75 ?  10  LEU   A CD1  1 
ATOM   200  C  CD2  A LEU   A 1 10  ? 5.943  -12.893 8.462   0.72 16.75 ?  10  LEU   A CD2  1 
ATOM   201  C  CD2  B LEU   A 1 10  ? 5.832  -12.331 9.161   0.28 15.87 ?  10  LEU   A CD2  1 
ATOM   202  H  H    A LEU   A 1 10  ? 8.853  -10.613 11.525  0.72 15.08 ?  10  LEU   A H    1 
ATOM   203  H  H    B LEU   A 1 10  ? 9.141  -10.418 12.057  0.28 17.21 ?  10  LEU   A H    1 
ATOM   204  H  HA   A LEU   A 1 10  ? 7.675  -12.887 12.328  0.72 14.79 ?  10  LEU   A HA   1 
ATOM   205  H  HA   B LEU   A 1 10  ? 7.785  -12.593 12.916  0.28 16.89 ?  10  LEU   A HA   1 
ATOM   206  H  HB2  A LEU   A 1 10  ? 6.590  -11.536 10.753  0.72 15.57 ?  10  LEU   A HB2  1 
ATOM   207  H  HB2  B LEU   A 1 10  ? 6.650  -11.187 11.447  0.28 17.40 ?  10  LEU   A HB2  1 
ATOM   208  H  HB3  A LEU   A 1 10  ? 7.817  -11.694 9.766   0.72 15.57 ?  10  LEU   A HB3  1 
ATOM   209  H  HB3  B LEU   A 1 10  ? 7.819  -11.321 10.393  0.28 17.40 ?  10  LEU   A HB3  1 
ATOM   210  H  HG   A LEU   A 1 10  ? 7.255  -13.994 9.563   0.72 18.37 ?  10  LEU   A HG   1 
ATOM   211  H  HG   B LEU   A 1 10  ? 7.171  -13.584 10.059  0.28 18.28 ?  10  LEU   A HG   1 
ATOM   212  H  HD11 A LEU   A 1 10  ? 5.195  -14.723 10.278  0.72 19.94 ?  10  LEU   A HD11 1 
ATOM   213  H  HD11 B LEU   A 1 10  ? 5.163  -14.329 10.879  0.28 18.95 ?  10  LEU   A HD11 1 
ATOM   214  H  HD12 A LEU   A 1 10  ? 6.018  -14.195 11.529  0.72 19.94 ?  10  LEU   A HD12 1 
ATOM   215  H  HD12 B LEU   A 1 10  ? 6.036  -13.847 12.116  0.28 18.95 ?  10  LEU   A HD12 1 
ATOM   216  H  HD13 A LEU   A 1 10  ? 4.880  -13.291 10.890  0.72 19.94 ?  10  LEU   A HD13 1 
ATOM   217  H  HD13 B LEU   A 1 10  ? 4.878  -12.919 11.553  0.28 18.95 ?  10  LEU   A HD13 1 
ATOM   218  H  HD21 A LEU   A 1 10  ? 5.511  -13.666 8.062   0.72 20.15 ?  10  LEU   A HD21 1 
ATOM   219  H  HD21 B LEU   A 1 10  ? 5.338  -13.037 8.720   0.28 19.10 ?  10  LEU   A HD21 1 
ATOM   220  H  HD22 A LEU   A 1 10  ? 5.286  -12.205 8.645   0.72 20.15 ?  10  LEU   A HD22 1 
ATOM   221  H  HD22 B LEU   A 1 10  ? 5.224  -11.636 9.461   0.28 19.10 ?  10  LEU   A HD22 1 
ATOM   222  H  HD23 A LEU   A 1 10  ? 6.627  -12.552 7.867   0.72 20.15 ?  10  LEU   A HD23 1 
ATOM   223  H  HD23 B LEU   A 1 10  ? 6.491  -11.956 8.556   0.28 19.10 ?  10  LEU   A HD23 1 
ATOM   224  N  N    A LYS   A 1 11  ? 9.213  -14.678 11.582  0.72 12.59 ?  11  LYS   A N    1 
ATOM   225  N  N    B LYS   A 1 11  ? 9.245  -14.407 12.102  0.28 13.30 ?  11  LYS   A N    1 
ATOM   226  C  CA   A LYS   A 1 11  ? 10.212 -15.682 11.240  0.72 12.71 ?  11  LYS   A CA   1 
ATOM   227  C  CA   B LYS   A 1 11  ? 10.184 -15.426 11.650  0.28 13.21 ?  11  LYS   A CA   1 
ATOM   228  C  C    A LYS   A 1 11  ? 9.861  -16.272 9.883   0.72 12.49 ?  11  LYS   A C    1 
ATOM   229  C  C    B LYS   A 1 11  ? 9.760  -15.922 10.274  0.28 12.38 ?  11  LYS   A C    1 
ATOM   230  O  O    A LYS   A 1 11  ? 8.786  -16.852 9.725   0.72 14.18 ?  11  LYS   A O    1 
ATOM   231  O  O    B LYS   A 1 11  ? 8.616  -16.351 10.088  0.28 12.37 ?  11  LYS   A O    1 
ATOM   232  C  CB   A LYS   A 1 11  ? 10.234 -16.763 12.320  0.72 12.92 ?  11  LYS   A CB   1 
ATOM   233  C  CB   B LYS   A 1 11  ? 10.224 -16.579 12.651  0.28 13.41 ?  11  LYS   A CB   1 
ATOM   234  C  CG   A LYS   A 1 11  ? 11.261 -17.865 12.142  0.72 13.17 ?  11  LYS   A CG   1 
ATOM   235  C  CG   B LYS   A 1 11  ? 11.259 -17.658 12.341  0.28 13.57 ?  11  LYS   A CG   1 
ATOM   236  C  CD   A LYS   A 1 11  ? 11.365 -18.681 13.434  0.72 13.85 ?  11  LYS   A CD   1 
ATOM   237  C  CD   B LYS   A 1 11  ? 11.261 -18.746 13.413  0.28 13.99 ?  11  LYS   A CD   1 
ATOM   238  C  CE   A LYS   A 1 11  ? 12.331 -19.854 13.319  0.72 14.15 ?  11  LYS   A CE   1 
ATOM   239  C  CE   B LYS   A 1 11  ? 12.358 -19.784 13.185  0.28 14.07 ?  11  LYS   A CE   1 
ATOM   240  N  NZ   A LYS   A 1 11  ? 13.705 -19.403 12.969  0.72 14.17 ?  11  LYS   A NZ   1 
ATOM   241  N  NZ   B LYS   A 1 11  ? 13.726 -19.195 13.280  0.28 13.77 ?  11  LYS   A NZ   1 
ATOM   242  H  H    A LYS   A 1 11  ? 8.552  -14.989 12.043  0.72 15.16 ?  11  LYS   A H    1 
ATOM   243  H  H    B LYS   A 1 11  ? 8.657  -14.683 12.664  0.28 16.01 ?  11  LYS   A H    1 
ATOM   244  H  HA   A LYS   A 1 11  ? 11.085 -15.271 11.185  0.72 15.30 ?  11  LYS   A HA   1 
ATOM   245  H  HA   B LYS   A 1 11  ? 11.068 -15.035 11.577  0.28 15.90 ?  11  LYS   A HA   1 
ATOM   246  H  HB2  A LYS   A 1 11  ? 10.413 -16.335 13.171  0.72 15.55 ?  11  LYS   A HB2  1 
ATOM   247  H  HB2  B LYS   A 1 11  ? 10.428 -16.213 13.525  0.28 16.14 ?  11  LYS   A HB2  1 
ATOM   248  H  HB3  A LYS   A 1 11  ? 9.360  -17.184 12.349  0.72 15.55 ?  11  LYS   A HB3  1 
ATOM   249  H  HB3  B LYS   A 1 11  ? 9.351  -16.998 12.667  0.28 16.14 ?  11  LYS   A HB3  1 
ATOM   250  H  HG2  A LYS   A 1 11  ? 10.985 -18.458 11.424  0.72 15.85 ?  11  LYS   A HG2  1 
ATOM   251  H  HG2  B LYS   A 1 11  ? 11.048 -18.070 11.488  0.28 16.33 ?  11  LYS   A HG2  1 
ATOM   252  H  HG3  A LYS   A 1 11  ? 12.129 -17.478 11.951  0.72 15.85 ?  11  LYS   A HG3  1 
ATOM   253  H  HG3  B LYS   A 1 11  ? 12.142 -17.257 12.311  0.28 16.33 ?  11  LYS   A HG3  1 
ATOM   254  H  HD2  A LYS   A 1 11  ? 11.674 -18.101 14.147  0.72 16.66 ?  11  LYS   A HD2  1 
ATOM   255  H  HD2  B LYS   A 1 11  ? 11.406 -18.336 14.280  0.28 16.83 ?  11  LYS   A HD2  1 
ATOM   256  H  HD3  A LYS   A 1 11  ? 10.486 -19.034 13.654  0.72 16.66 ?  11  LYS   A HD3  1 
ATOM   257  H  HD3  B LYS   A 1 11  ? 10.404 -19.203 13.401  0.28 16.83 ?  11  LYS   A HD3  1 
ATOM   258  H  HE2  A LYS   A 1 11  ? 12.373 -20.318 14.170  0.72 17.02 ?  11  LYS   A HE2  1 
ATOM   259  H  HE2  B LYS   A 1 11  ? 12.284 -20.480 13.858  0.28 16.93 ?  11  LYS   A HE2  1 
ATOM   260  H  HE3  A LYS   A 1 11  ? 12.024 -20.454 12.623  0.72 17.02 ?  11  LYS   A HE3  1 
ATOM   261  H  HE3  B LYS   A 1 11  ? 12.257 -20.166 12.299  0.28 16.93 ?  11  LYS   A HE3  1 
ATOM   262  H  HZ1  A LYS   A 1 11  ? 14.249 -20.105 12.912  0.72 17.06 ?  11  LYS   A HZ1  1 
ATOM   263  H  HZ1  B LYS   A 1 11  ? 14.340 -19.830 13.159  0.28 16.58 ?  11  LYS   A HZ1  1 
ATOM   264  H  HZ2  A LYS   A 1 11  ? 13.696 -18.979 12.186  0.72 17.06 ?  11  LYS   A HZ2  1 
ATOM   265  H  HZ2  B LYS   A 1 11  ? 13.832 -18.569 12.657  0.28 16.58 ?  11  LYS   A HZ2  1 
ATOM   266  H  HZ3  A LYS   A 1 11  ? 14.012 -18.849 13.594  0.72 17.06 ?  11  LYS   A HZ3  1 
ATOM   267  H  HZ3  B LYS   A 1 11  ? 13.845 -18.829 14.082  0.28 16.58 ?  11  LYS   A HZ3  1 
ATOM   268  N  N    A LEU   A 1 12  ? 10.760 -16.143 8.909   0.72 11.88 ?  12  LEU   A N    1 
ATOM   269  N  N    B LEU   A 1 12  ? 10.672 -15.849 9.305   0.28 12.37 ?  12  LEU   A N    1 
ATOM   270  C  CA   A LEU   A 1 12  ? 10.503 -16.720 7.594   0.72 12.03 ?  12  LEU   A CA   1 
ATOM   271  C  CA   B LEU   A 1 12  ? 10.405 -16.320 7.949   0.28 12.71 ?  12  LEU   A CA   1 
ATOM   272  C  C    A LEU   A 1 12  ? 11.099 -18.114 7.452   0.72 12.08 ?  12  LEU   A C    1 
ATOM   273  C  C    B LEU   A 1 12  ? 10.945 -17.722 7.700   0.28 12.84 ?  12  LEU   A C    1 
ATOM   274  O  O    A LEU   A 1 12  ? 10.479 -18.986 6.835   0.72 12.18 ?  12  LEU   A O    1 
ATOM   275  O  O    B LEU   A 1 12  ? 10.238 -18.575 7.154   0.28 12.75 ?  12  LEU   A O    1 
ATOM   276  C  CB   A LEU   A 1 12  ? 11.047 -15.820 6.480   0.72 12.15 ?  12  LEU   A CB   1 
ATOM   277  C  CB   B LEU   A 1 12  ? 10.988 -15.346 6.916   0.28 13.19 ?  12  LEU   A CB   1 
ATOM   278  C  CG   A LEU   A 1 12  ? 10.393 -14.449 6.304   0.72 13.20 ?  12  LEU   A CG   1 
ATOM   279  C  CG   B LEU   A 1 12  ? 10.305 -13.980 6.831   0.28 13.72 ?  12  LEU   A CG   1 
ATOM   280  C  CD1  A LEU   A 1 12  ? 11.126 -13.675 5.229   0.72 13.32 ?  12  LEU   A CD1  1 
ATOM   281  C  CD1  B LEU   A 1 12  ? 10.893 -13.143 5.703   0.28 14.21 ?  12  LEU   A CD1  1 
ATOM   282  C  CD2  A LEU   A 1 12  ? 8.918  -14.588 5.955   0.72 14.27 ?  12  LEU   A CD2  1 
ATOM   283  C  CD2  B LEU   A 1 12  ? 8.804  -14.142 6.654   0.28 14.04 ?  12  LEU   A CD2  1 
ATOM   284  H  H    A LEU   A 1 12  ? 11.522 -15.739 8.979   0.72 14.31 ?  12  LEU   A H    1 
ATOM   285  H  H    B LEU   A 1 12  ? 11.462 -15.515 9.411   0.28 14.89 ?  12  LEU   A H    1 
ATOM   286  H  HA   A LEU   A 1 12  ? 9.545  -16.805 7.472   0.72 14.48 ?  12  LEU   A HA   1 
ATOM   287  H  HA   B LEU   A 1 12  ? 9.446  -16.351 7.822   0.28 15.30 ?  12  LEU   A HA   1 
ATOM   288  H  HB2  A LEU   A 1 12  ? 11.987 -15.671 6.650   0.72 14.63 ?  12  LEU   A HB2  1 
ATOM   289  H  HB2  B LEU   A 1 12  ? 11.921 -15.189 7.133   0.28 15.87 ?  12  LEU   A HB2  1 
ATOM   290  H  HB3  A LEU   A 1 12  ? 10.946 -16.297 5.638   0.72 14.63 ?  12  LEU   A HB3  1 
ATOM   291  H  HB3  B LEU   A 1 12  ? 10.924 -15.756 6.040   0.28 15.87 ?  12  LEU   A HB3  1 
ATOM   292  H  HG   A LEU   A 1 12  ? 10.462 -13.958 7.134   0.72 15.88 ?  12  LEU   A HG   1 
ATOM   293  H  HG   B LEU   A 1 12  ? 10.455 -13.502 7.662   0.28 16.51 ?  12  LEU   A HG   1 
ATOM   294  H  HD11 A LEU   A 1 12  ? 10.708 -12.810 5.122   0.72 16.03 ?  12  LEU   A HD11 1 
ATOM   295  H  HD11 B LEU   A 1 12  ? 10.443 -12.283 5.680   0.28 17.09 ?  12  LEU   A HD11 1 
ATOM   296  H  HD12 A LEU   A 1 12  ? 12.053 -13.567 5.497   0.72 16.03 ?  12  LEU   A HD12 1 
ATOM   297  H  HD12 B LEU   A 1 12  ? 11.840 -13.016 5.865   0.28 17.09 ?  12  LEU   A HD12 1 
ATOM   298  H  HD13 A LEU   A 1 12  ? 11.082 -14.173 4.395   0.72 16.03 ?  12  LEU   A HD13 1 
ATOM   299  H  HD13 B LEU   A 1 12  ? 10.759 -13.608 4.863   0.28 17.09 ?  12  LEU   A HD13 1 
ATOM   300  H  HD21 A LEU   A 1 12  ? 8.558  -13.713 5.746   0.72 17.17 ?  12  LEU   A HD21 1 
ATOM   301  H  HD21 B LEU   A 1 12  ? 8.431  -13.303 6.345   0.28 16.90 ?  12  LEU   A HD21 1 
ATOM   302  H  HD22 A LEU   A 1 12  ? 8.826  -15.174 5.185   0.72 17.17 ?  12  LEU   A HD22 1 
ATOM   303  H  HD22 B LEU   A 1 12  ? 8.638  -14.841 6.004   0.28 16.90 ?  12  LEU   A HD22 1 
ATOM   304  H  HD23 A LEU   A 1 12  ? 8.444  -14.967 6.713   0.72 17.17 ?  12  LEU   A HD23 1 
ATOM   305  H  HD23 B LEU   A 1 12  ? 8.411  -14.384 7.508   0.28 16.90 ?  12  LEU   A HD23 1 
ATOM   306  N  N    A THR   A 1 13  ? 12.307 -18.317 7.978   0.72 12.33 ?  13  THR   A N    1 
ATOM   307  N  N    B THR   A 1 13  ? 12.197 -17.972 8.070   0.28 13.15 ?  13  THR   A N    1 
ATOM   308  C  CA   A THR   A 1 13  ? 13.014 -19.591 7.911   0.72 12.64 ?  13  THR   A CA   1 
ATOM   309  C  CA   B THR   A 1 13  ? 12.805 -19.285 7.920   0.28 13.23 ?  13  THR   A CA   1 
ATOM   310  C  C    A THR   A 1 13  ? 13.774 -19.790 9.218   0.72 13.05 ?  13  THR   A C    1 
ATOM   311  C  C    B THR   A 1 13  ? 13.599 -19.594 9.183   0.28 13.69 ?  13  THR   A C    1 
ATOM   312  O  O    A THR   A 1 13  ? 13.675 -18.989 10.153  0.72 13.59 ?  13  THR   A O    1 
ATOM   313  O  O    B THR   A 1 13  ? 13.509 -18.890 10.194  0.28 14.13 ?  13  THR   A O    1 
ATOM   314  C  CB   A THR   A 1 13  ? 14.000 -19.634 6.738   0.72 13.37 ?  13  THR   A CB   1 
ATOM   315  C  CB   B THR   A 1 13  ? 13.713 -19.344 6.684   0.28 13.36 ?  13  THR   A CB   1 
ATOM   316  O  OG1  A THR   A 1 13  ? 15.058 -18.710 6.996   0.72 13.58 ?  13  THR   A OG1  1 
ATOM   317  O  OG1  B THR   A 1 13  ? 14.795 -18.422 6.849   0.28 13.53 ?  13  THR   A OG1  1 
ATOM   318  C  CG2  A THR   A 1 13  ? 13.337 -19.292 5.416   0.72 14.47 ?  13  THR   A CG2  1 
ATOM   319  C  CG2  B THR   A 1 13  ? 12.948 -19.007 5.411   0.28 13.70 ?  13  THR   A CG2  1 
ATOM   320  H  H    A THR   A 1 13  ? 12.755 -17.710 8.380   0.72 14.84 ?  13  THR   A H    1 
ATOM   321  H  H    B THR   A 1 13  ? 12.719 -17.378 8.407   0.28 15.82 ?  13  THR   A H    1 
ATOM   322  H  HA   A THR   A 1 13  ? 12.380 -20.319 7.802   0.72 15.22 ?  13  THR   A HA   1 
ATOM   323  H  HA   B THR   A 1 13  ? 12.109 -19.953 7.822   0.28 15.93 ?  13  THR   A HA   1 
ATOM   324  H  HB   A THR   A 1 13  ? 14.374 -20.529 6.660   0.72 16.09 ?  13  THR   A HB   1 
ATOM   325  H  HB   B THR   A 1 13  ? 14.071 -20.240 6.592   0.28 16.08 ?  13  THR   A HB   1 
ATOM   326  H  HG1  A THR   A 1 13  ? 15.657 -19.074 7.456   0.72 16.35 ?  13  THR   A HG1  1 
ATOM   327  H  HG1  B THR   A 1 13  ? 15.300 -18.447 6.179   0.28 16.29 ?  13  THR   A HG1  1 
ATOM   328  H  HG21 A THR   A 1 13  ? 13.954 -19.458 4.683   0.72 17.41 ?  13  THR   A HG21 1 
ATOM   329  H  HG21 B THR   A 1 13  ? 13.529 -19.117 4.640   0.28 16.49 ?  13  THR   A HG21 1 
ATOM   330  H  HG22 A THR   A 1 13  ? 12.550 -19.844 5.292   0.72 17.41 ?  13  THR   A HG22 1 
ATOM   331  H  HG22 B THR   A 1 13  ? 12.187 -19.601 5.317   0.28 16.49 ?  13  THR   A HG22 1 
ATOM   332  H  HG23 A THR   A 1 13  ? 13.078 -18.361 5.406   0.72 17.41 ?  13  THR   A HG23 1 
ATOM   333  H  HG23 B THR   A 1 13  ? 12.636 -18.092 5.442   0.28 16.49 ?  13  THR   A HG23 1 
ATOM   334  N  N    A ASP   A 1 14  ? 14.580 -20.852 9.265   0.72 13.73 ?  14  ASP   A N    1 
ATOM   335  N  N    B ASP   A 1 14  ? 14.400 -20.654 9.106   0.28 13.94 ?  14  ASP   A N    1 
ATOM   336  C  CA   A ASP   A 1 14  ? 15.416 -21.093 10.433  0.72 14.73 ?  14  ASP   A CA   1 
ATOM   337  C  CA   B ASP   A 1 14  ? 15.261 -21.030 10.217  0.28 13.97 ?  14  ASP   A CA   1 
ATOM   338  C  C    A ASP   A 1 14  ? 16.208 -19.849 10.834  0.72 14.29 ?  14  ASP   A C    1 
ATOM   339  C  C    B ASP   A 1 14  ? 16.236 -19.922 10.586  0.28 12.71 ?  14  ASP   A C    1 
ATOM   340  O  O    A ASP   A 1 14  ? 16.350 -19.553 12.026  0.72 14.71 ?  14  ASP   A O    1 
ATOM   341  O  O    B ASP   A 1 14  ? 16.681 -19.862 11.737  0.28 12.74 ?  14  ASP   A O    1 
ATOM   342  C  CB   A ASP   A 1 14  ? 16.377 -22.242 10.150  0.72 17.19 ?  14  ASP   A CB   1 
ATOM   343  C  CB   B ASP   A 1 14  ? 16.050 -22.283 9.840   0.28 15.69 ?  14  ASP   A CB   1 
ATOM   344  C  CG   A ASP   A 1 14  ? 17.293 -22.505 11.312  0.72 21.18 ?  14  ASP   A CG   1 
ATOM   345  C  CG   B ASP   A 1 14  ? 16.972 -22.744 10.943  0.28 17.31 ?  14  ASP   A CG   1 
ATOM   346  O  OD1  A ASP   A 1 14  ? 16.795 -22.921 12.379  0.72 22.78 ?  14  ASP   A OD1  1 
ATOM   347  O  OD1  B ASP   A 1 14  ? 16.458 -23.197 11.989  0.28 17.81 ?  14  ASP   A OD1  1 
ATOM   348  O  OD2  A ASP   A 1 14  ? 18.506 -22.261 11.170  0.72 23.26 -1 14  ASP   A OD2  1 
ATOM   349  O  OD2  B ASP   A 1 14  ? 18.204 -22.665 10.763  0.28 18.26 -1 14  ASP   A OD2  1 
ATOM   350  H  H    A ASP   A 1 14  ? 14.668 -21.438 8.640   0.72 16.53 ?  14  ASP   A H    1 
ATOM   351  H  H    B ASP   A 1 14  ? 14.465 -21.159 8.418   0.28 16.77 ?  14  ASP   A H    1 
ATOM   352  H  HA   A ASP   A 1 14  ? 14.856 -21.352 11.183  0.72 17.72 ?  14  ASP   A HA   1 
ATOM   353  H  HA   B ASP   A 1 14  ? 14.715 -21.233 10.993  0.28 16.82 ?  14  ASP   A HA   1 
ATOM   354  H  HB2  A ASP   A 1 14  ? 15.860 -23.052 9.963   0.72 20.67 ?  14  ASP   A HB2  1 
ATOM   355  H  HB2  B ASP   A 1 14  ? 15.434 -23.008 9.666   0.28 18.88 ?  14  ASP   A HB2  1 
ATOM   356  H  HB3  A ASP   A 1 14  ? 16.924 -22.025 9.380   0.72 20.67 ?  14  ASP   A HB3  1 
ATOM   357  H  HB3  B ASP   A 1 14  ? 16.580 -22.097 9.047   0.28 18.88 ?  14  ASP   A HB3  1 
ATOM   358  N  N    A ASN   A 1 15  ? 16.732 -19.104 9.855   0.72 13.97 ?  15  ASN   A N    1 
ATOM   359  N  N    B ASN   A 1 15  ? 16.569 -19.033 9.639   0.28 11.68 ?  15  ASN   A N    1 
ATOM   360  C  CA   A ASN   A 1 15  ? 17.692 -18.042 10.138  0.72 14.31 ?  15  ASN   A CA   1 
ATOM   361  C  CA   B ASN   A 1 15  ? 17.626 -18.056 9.876   0.28 12.03 ?  15  ASN   A CA   1 
ATOM   362  C  C    A ASN   A 1 15  ? 17.308 -16.660 9.625   0.72 13.66 ?  15  ASN   A C    1 
ATOM   363  C  C    B ASN   A 1 15  ? 17.312 -16.661 9.332   0.28 12.51 ?  15  ASN   A C    1 
ATOM   364  O  O    A ASN   A 1 15  ? 18.034 -15.702 9.926   0.72 13.26 ?  15  ASN   A O    1 
ATOM   365  O  O    B ASN   A 1 15  ? 18.229 -15.838 9.218   0.28 13.07 ?  15  ASN   A O    1 
ATOM   366  C  CB   A ASN   A 1 15  ? 19.074 -18.388 9.553   0.72 14.42 ?  15  ASN   A CB   1 
ATOM   367  C  CB   B ASN   A 1 15  ? 18.969 -18.551 9.311   0.28 11.58 ?  15  ASN   A CB   1 
ATOM   368  C  CG   A ASN   A 1 15  ? 19.044 -18.530 8.048   0.72 14.80 ?  15  ASN   A CG   1 
ATOM   369  C  CG   B ASN   A 1 15  ? 18.996 -18.580 7.794   0.28 12.10 ?  15  ASN   A CG   1 
ATOM   370  O  OD1  A ASN   A 1 15  ? 18.272 -19.323 7.507   0.72 15.04 ?  15  ASN   A OD1  1 
ATOM   371  O  OD1  B ASN   A 1 15  ? 18.385 -19.444 7.166   0.28 12.41 ?  15  ASN   A OD1  1 
ATOM   372  N  ND2  A ASN   A 1 15  ? 19.864 -17.740 7.356   0.72 14.71 ?  15  ASN   A ND2  1 
ATOM   373  N  ND2  B ASN   A 1 15  ? 19.721 -17.640 7.199   0.28 11.90 ?  15  ASN   A ND2  1 
ATOM   374  H  H    A ASN   A 1 15  ? 16.558 -19.205 9.027   0.72 16.81 ?  15  ASN   A H    1 
ATOM   375  H  H    B ASN   A 1 15  ? 16.196 -18.982 8.871   0.28 14.06 ?  15  ASN   A H    1 
ATOM   376  H  HA   A ASN   A 1 15  ? 17.809 -17.978 11.103  0.72 17.22 ?  15  ASN   A HA   1 
ATOM   377  H  HA   B ASN   A 1 15  ? 17.744 -17.969 10.828  0.28 14.49 ?  15  ASN   A HA   1 
ATOM   378  H  HB2  A ASN   A 1 15  ? 19.705 -17.675 9.778   0.72 17.35 ?  15  ASN   A HB2  1 
ATOM   379  H  HB2  B ASN   A 1 15  ? 19.674 -17.957 9.612   0.28 13.94 ?  15  ASN   A HB2  1 
ATOM   380  H  HB3  A ASN   A 1 15  ? 19.387 -19.225 9.932   0.72 17.35 ?  15  ASN   A HB3  1 
ATOM   381  H  HB3  B ASN   A 1 15  ? 19.134 -19.452 9.635   0.28 13.94 ?  15  ASN   A HB3  1 
ATOM   382  H  HD21 A ASN   A 1 15  ? 19.876 -17.781 6.495   0.72 17.71 ?  15  ASN   A HD21 1 
ATOM   383  H  HD21 B ASN   A 1 15  ? 19.774 -17.616 6.341   0.28 14.32 ?  15  ASN   A HD21 1 
ATOM   384  H  HD22 A ASN   A 1 15  ? 20.385 -17.188 7.763   0.72 17.71 ?  15  ASN   A HD22 1 
ATOM   385  H  HD22 B ASN   A 1 15  ? 20.135 -17.054 7.672   0.28 14.32 ?  15  ASN   A HD22 1 
ATOM   386  N  N    A VAL   A 1 16  ? 16.228 -16.522 8.849   0.72 13.69 ?  16  VAL   A N    1 
ATOM   387  N  N    B VAL   A 1 16  ? 16.053 -16.354 9.021   0.28 12.46 ?  16  VAL   A N    1 
ATOM   388  C  CA   A VAL   A 1 16  ? 15.821 -15.243 8.266   0.72 13.55 ?  16  VAL   A CA   1 
ATOM   389  C  CA   B VAL   A 1 16  ? 15.679 -15.064 8.449   0.28 12.31 ?  16  VAL   A CA   1 
ATOM   390  C  C    A VAL   A 1 16  ? 14.530 -14.759 8.920   0.72 12.98 ?  16  VAL   A C    1 
ATOM   391  C  C    B VAL   A 1 16  ? 14.441 -14.541 9.170   0.28 12.25 ?  16  VAL   A C    1 
ATOM   392  O  O    A VAL   A 1 16  ? 13.534 -15.493 8.998   0.72 12.86 ?  16  VAL   A O    1 
ATOM   393  O  O    B VAL   A 1 16  ? 13.434 -15.249 9.285   0.28 12.08 ?  16  VAL   A O    1 
ATOM   394  C  CB   A VAL   A 1 16  ? 15.659 -15.322 6.738   0.72 14.41 ?  16  VAL   A CB   1 
ATOM   395  C  CB   B VAL   A 1 16  ? 15.440 -15.164 6.929   0.28 12.42 ?  16  VAL   A CB   1 
ATOM   396  C  CG1  A VAL   A 1 16  ? 15.230 -13.960 6.174   0.72 15.11 ?  16  VAL   A CG1  1 
ATOM   397  C  CG1  B VAL   A 1 16  ? 15.008 -13.817 6.361   0.28 12.64 ?  16  VAL   A CG1  1 
ATOM   398  C  CG2  A VAL   A 1 16  ? 16.941 -15.793 6.072   0.72 15.15 ?  16  VAL   A CG2  1 
ATOM   399  C  CG2  B VAL   A 1 16  ? 16.690 -15.676 6.215   0.28 12.83 ?  16  VAL   A CG2  1 
ATOM   400  H  H    A VAL   A 1 16  ? 15.718 -17.179 8.642   0.72 16.48 ?  16  VAL   A H    1 
ATOM   401  H  H    B VAL   A 1 16  ? 15.385 -16.881 9.142   0.28 15.00 ?  16  VAL   A H    1 
ATOM   402  H  HA   A VAL   A 1 16  ? 16.517 -14.591 8.453   0.72 16.31 ?  16  VAL   A HA   1 
ATOM   403  H  HA   B VAL   A 1 16  ? 16.396 -14.426 8.596   0.28 14.83 ?  16  VAL   A HA   1 
ATOM   404  H  HB   A VAL   A 1 16  ? 14.967 -15.967 6.535   0.72 17.34 ?  16  VAL   A HB   1 
ATOM   405  H  HB   B VAL   A 1 16  ? 14.728 -15.799 6.765   0.28 14.95 ?  16  VAL   A HB   1 
ATOM   406  H  HG11 A VAL   A 1 16  ? 15.319 -13.982 5.209   0.72 18.18 ?  16  VAL   A HG11 1 
ATOM   407  H  HG11 B VAL   A 1 16  ? 15.071 -13.852 5.393   0.28 15.21 ?  16  VAL   A HG11 1 
ATOM   408  H  HG12 A VAL   A 1 16  ? 14.304 -13.797 6.416   0.72 18.18 ?  16  VAL   A HG12 1 
ATOM   409  H  HG12 B VAL   A 1 16  ? 14.092 -13.642 6.625   0.28 15.21 ?  16  VAL   A HG12 1 
ATOM   410  H  HG13 A VAL   A 1 16  ? 15.799 -13.271 6.546   0.72 18.18 ?  16  VAL   A HG13 1 
ATOM   411  H  HG13 B VAL   A 1 16  ? 15.594 -13.127 6.705   0.28 15.21 ?  16  VAL   A HG13 1 
ATOM   412  H  HG21 A VAL   A 1 16  ? 16.821 -15.763 5.110   0.72 18.23 ?  16  VAL   A HG21 1 
ATOM   413  H  HG21 B VAL   A 1 16  ? 16.528 -15.685 5.258   0.28 15.44 ?  16  VAL   A HG21 1 
ATOM   414  H  HG22 A VAL   A 1 16  ? 17.667 -15.208 6.334   0.72 18.23 ?  16  VAL   A HG22 1 
ATOM   415  H  HG22 B VAL   A 1 16  ? 17.435 -15.089 6.417   0.28 15.44 ?  16  VAL   A HG22 1 
ATOM   416  H  HG23 A VAL   A 1 16  ? 17.129 -16.702 6.354   0.72 18.23 ?  16  VAL   A HG23 1 
ATOM   417  H  HG23 B VAL   A 1 16  ? 16.886 -16.575 6.524   0.28 15.44 ?  16  VAL   A HG23 1 
ATOM   418  N  N    A TYR   A 1 17  ? 14.544 -13.490 9.322   0.72 12.51 ?  17  TYR   A N    1 
ATOM   419  N  N    B TYR   A 1 17  ? 14.523 -13.294 9.642   0.28 12.06 ?  17  TYR   A N    1 
ATOM   420  C  CA   A TYR   A 1 17  ? 13.453 -12.807 9.998   0.72 12.26 ?  17  TYR   A CA   1 
ATOM   421  C  CA   B TYR   A 1 17  ? 13.468 -12.628 10.393  0.28 11.49 ?  17  TYR   A CA   1 
ATOM   422  C  C    A TYR   A 1 17  ? 13.182 -11.487 9.286   0.72 11.76 ?  17  TYR   A C    1 
ATOM   423  C  C    B TYR   A 1 17  ? 13.213 -11.268 9.761   0.28 11.58 ?  17  TYR   A C    1 
ATOM   424  O  O    A TYR   A 1 17  ? 14.085 -10.924 8.666   0.72 11.25 ?  17  TYR   A O    1 
ATOM   425  O  O    B TYR   A 1 17  ? 14.132 -10.652 9.221   0.28 11.27 ?  17  TYR   A O    1 
ATOM   426  C  CB   A TYR   A 1 17  ? 13.860 -12.520 11.441  0.72 12.85 ?  17  TYR   A CB   1 
ATOM   427  C  CB   B TYR   A 1 17  ? 13.906 -12.442 11.852  0.28 12.05 ?  17  TYR   A CB   1 
ATOM   428  C  CG   A TYR   A 1 17  ? 14.019 -13.764 12.282  0.72 14.49 ?  17  TYR   A CG   1 
ATOM   429  C  CG   B TYR   A 1 17  ? 14.194 -13.743 12.574  0.28 12.57 ?  17  TYR   A CG   1 
ATOM   430  C  CD1  A TYR   A 1 17  ? 15.179 -14.532 12.232  0.72 15.56 ?  17  TYR   A CD1  1 
ATOM   431  C  CD1  B TYR   A 1 17  ? 15.383 -14.439 12.364  0.28 13.02 ?  17  TYR   A CD1  1 
ATOM   432  C  CD2  A TYR   A 1 17  ? 12.999 -14.182 13.122  0.72 14.53 ?  17  TYR   A CD2  1 
ATOM   433  C  CD2  B TYR   A 1 17  ? 13.277 -14.277 13.467  0.28 12.78 ?  17  TYR   A CD2  1 
ATOM   434  C  CE1  A TYR   A 1 17  ? 15.314 -15.689 13.000  0.72 15.88 ?  17  TYR   A CE1  1 
ATOM   435  C  CE1  B TYR   A 1 17  ? 15.642 -15.634 13.022  0.28 13.49 ?  17  TYR   A CE1  1 
ATOM   436  C  CE2  A TYR   A 1 17  ? 13.120 -15.336 13.890  0.72 15.23 ?  17  TYR   A CE2  1 
ATOM   437  C  CE2  B TYR   A 1 17  ? 13.527 -15.468 14.130  0.28 13.11 ?  17  TYR   A CE2  1 
ATOM   438  C  CZ   A TYR   A 1 17  ? 14.283 -16.083 13.832  0.72 15.70 ?  17  TYR   A CZ   1 
ATOM   439  C  CZ   B TYR   A 1 17  ? 14.708 -16.142 13.905  0.28 13.20 ?  17  TYR   A CZ   1 
ATOM   440  O  OH   A TYR   A 1 17  ? 14.402 -17.224 14.600  0.72 16.30 ?  17  TYR   A OH   1 
ATOM   441  O  OH   B TYR   A 1 17  ? 14.949 -17.323 14.570  0.28 13.26 ?  17  TYR   A OH   1 
ATOM   442  H  H    A TYR   A 1 17  ? 15.229 -12.981 9.197   0.72 15.05 ?  17  TYR   A H    1 
ATOM   443  H  H    B TYR   A 1 17  ? 15.215 -12.789 9.533   0.28 14.52 ?  17  TYR   A H    1 
ATOM   444  H  HA   A TYR   A 1 17  ? 12.658 -13.368 9.982   0.72 14.75 ?  17  TYR   A HA   1 
ATOM   445  H  HA   B TYR   A 1 17  ? 12.651 -13.142 10.365  0.28 13.83 ?  17  TYR   A HA   1 
ATOM   446  H  HB2  A TYR   A 1 17  ? 14.707 -12.057 11.440  0.72 15.47 ?  17  TYR   A HB2  1 
ATOM   447  H  HB2  B TYR   A 1 17  ? 14.716 -11.911 11.864  0.28 14.51 ?  17  TYR   A HB2  1 
ATOM   448  H  HB3  A TYR   A 1 17  ? 13.177 -11.976 11.848  0.72 15.47 ?  17  TYR   A HB3  1 
ATOM   449  H  HB3  B TYR   A 1 17  ? 13.203 -11.981 12.337  0.28 14.51 ?  17  TYR   A HB3  1 
ATOM   450  H  HD1  A TYR   A 1 17  ? 15.878 -14.277 11.671  0.72 18.72 ?  17  TYR   A HD1  1 
ATOM   451  H  HD1  B TYR   A 1 17  ? 16.012 -14.104 11.768  0.28 15.67 ?  17  TYR   A HD1  1 
ATOM   452  H  HD2  A TYR   A 1 17  ? 12.211 -13.691 13.166  0.72 17.48 ?  17  TYR   A HD2  1 
ATOM   453  H  HD2  B TYR   A 1 17  ? 12.478 -13.828 13.622  0.28 15.39 ?  17  TYR   A HD2  1 
ATOM   454  H  HE1  A TYR   A 1 17  ? 16.100 -16.196 12.960  0.72 19.10 ?  17  TYR   A HE1  1 
ATOM   455  H  HE1  B TYR   A 1 17  ? 16.441 -16.092 12.872  0.28 16.23 ?  17  TYR   A HE1  1 
ATOM   456  H  HE2  A TYR   A 1 17  ? 12.424 -15.597 14.449  0.72 18.33 ?  17  TYR   A HE2  1 
ATOM   457  H  HE2  B TYR   A 1 17  ? 12.900 -15.811 14.725  0.28 15.78 ?  17  TYR   A HE2  1 
ATOM   458  H  HH   A TYR   A 1 17  ? 13.649 -17.431 14.915  0.72 19.61 ?  17  TYR   A HH   1 
ATOM   459  H  HH   B TYR   A 1 17  ? 15.662 -17.672 14.296  0.28 15.96 ?  17  TYR   A HH   1 
ATOM   460  N  N    A ILE   A 1 18  ? 11.955 -10.967 9.395   0.72 11.70 ?  18  ILE   A N    1 
ATOM   461  N  N    B ILE   A 1 18  ? 11.969 -10.786 9.825   0.28 11.64 ?  18  ILE   A N    1 
ATOM   462  C  CA   A ILE   A 1 18  ? 11.568 -9.772  8.642   0.72 11.78 ?  18  ILE   A CA   1 
ATOM   463  C  CA   B ILE   A 1 18  ? 11.599 -9.557  9.125   0.28 11.44 ?  18  ILE   A CA   1 
ATOM   464  C  C    A ILE   A 1 18  ? 10.606 -8.905  9.453   0.72 12.29 ?  18  ILE   A C    1 
ATOM   465  C  C    B ILE   A 1 18  ? 10.702 -8.694  10.001  0.28 11.63 ?  18  ILE   A C    1 
ATOM   466  O  O    A ILE   A 1 18  ? 9.777  -9.411  10.211  0.72 12.62 ?  18  ILE   A O    1 
ATOM   467  O  O    B ILE   A 1 18  ? 9.843  -9.203  10.731  0.28 11.91 ?  18  ILE   A O    1 
ATOM   468  C  CB   A ILE   A 1 18  ? 11.003 -10.173 7.259   0.72 11.60 ?  18  ILE   A CB   1 
ATOM   469  C  CB   B ILE   A 1 18  ? 10.952 -9.849  7.755   0.28 11.02 ?  18  ILE   A CB   1 
ATOM   470  C  CG1  A ILE   A 1 18  ? 10.947 -8.974  6.320   0.72 12.24 ?  18  ILE   A CG1  1 
ATOM   471  C  CG1  B ILE   A 1 18  ? 10.903 -8.577  6.905   0.28 11.90 ?  18  ILE   A CG1  1 
ATOM   472  C  CG2  A ILE   A 1 18  ? 9.657  -10.878 7.400   0.72 12.17 ?  18  ILE   A CG2  1 
ATOM   473  C  CG2  B ILE   A 1 18  ? 9.559  -10.444 7.925   0.28 11.16 ?  18  ILE   A CG2  1 
ATOM   474  C  CD1  A ILE   A 1 18  ? 10.723 -9.357  4.885   0.72 14.13 ?  18  ILE   A CD1  1 
ATOM   475  C  CD1  B ILE   A 1 18  ? 10.457 -8.821  5.482   0.28 12.85 ?  18  ILE   A CD1  1 
ATOM   476  H  H    A ILE   A 1 18  ? 11.344 -11.300 9.897   0.72 14.09 ?  18  ILE   A H    1 
ATOM   477  H  H    B ILE   A 1 18  ? 11.326 -11.148 10.268  0.28 14.02 ?  18  ILE   A H    1 
ATOM   478  H  HA   A ILE   A 1 18  ? 12.370 -9.254  8.481   0.72 14.18 ?  18  ILE   A HA   1 
ATOM   479  H  HA   B ILE   A 1 18  ? 12.405 -9.046  8.960   0.28 13.77 ?  18  ILE   A HA   1 
ATOM   480  H  HB   A ILE   A 1 18  ? 11.617 -10.818 6.866   0.72 13.96 ?  18  ILE   A HB   1 
ATOM   481  H  HB   B ILE   A 1 18  ? 11.507 -10.494 7.299   0.28 13.27 ?  18  ILE   A HB   1 
ATOM   482  H  HG12 A ILE   A 1 18  ? 10.222 -8.397  6.591   0.72 14.73 ?  18  ILE   A HG12 1 
ATOM   483  H  HG12 B ILE   A 1 18  ? 10.283 -7.950  7.308   0.28 14.33 ?  18  ILE   A HG12 1 
ATOM   484  H  HG13 A ILE   A 1 18  ? 11.792 -8.500  6.369   0.72 14.73 ?  18  ILE   A HG13 1 
ATOM   485  H  HG13 B ILE   A 1 18  ? 11.792 -8.184  6.874   0.28 14.33 ?  18  ILE   A HG13 1 
ATOM   486  H  HG21 A ILE   A 1 18  ? 9.400  -11.252 6.538   0.72 14.65 ?  18  ILE   A HG21 1 
ATOM   487  H  HG21 B ILE   A 1 18  ? 9.262  -10.796 7.070   0.28 13.45 ?  18  ILE   A HG21 1 
ATOM   488  H  HG22 A ILE   A 1 18  ? 9.737  -11.593 8.052   0.72 14.65 ?  18  ILE   A HG22 1 
ATOM   489  H  HG22 B ILE   A 1 18  ? 9.599  -11.158 8.580   0.28 13.45 ?  18  ILE   A HG22 1 
ATOM   490  H  HG23 A ILE   A 1 18  ? 8.990  -10.239 7.691   0.72 14.65 ?  18  ILE   A HG23 1 
ATOM   491  H  HG23 B ILE   A 1 18  ? 8.949  -9.752  8.226   0.28 13.45 ?  18  ILE   A HG23 1 
ATOM   492  H  HD11 A ILE   A 1 18  ? 10.747 -8.553  4.338   0.72 17.01 ?  18  ILE   A HD11 1 
ATOM   493  H  HD11 B ILE   A 1 18  ? 10.535 -7.995  4.980   0.28 15.47 ?  18  ILE   A HD11 1 
ATOM   494  H  HD12 A ILE   A 1 18  ? 11.421 -9.967  4.604   0.72 17.01 ?  18  ILE   A HD12 1 
ATOM   495  H  HD12 B ILE   A 1 18  ? 11.025 -9.502  5.087   0.28 15.47 ?  18  ILE   A HD12 1 
ATOM   496  H  HD13 A ILE   A 1 18  ? 9.855  -9.783  4.802   0.72 17.01 ?  18  ILE   A HD13 1 
ATOM   497  H  HD13 B ILE   A 1 18  ? 9.535  -9.120  5.487   0.28 15.47 ?  18  ILE   A HD13 1 
ATOM   498  N  N    A LYS   A 1 19  ? 10.708 -7.584  9.264   0.72 11.81 ?  19  LYS   A N    1 
ATOM   499  N  N    B LYS   A 1 19  ? 10.907 -7.376  9.922   0.28 12.27 ?  19  LYS   A N    1 
ATOM   500  C  CA   A LYS   A 1 19  ? 9.892  -6.621  9.996   0.72 13.05 ?  19  LYS   A CA   1 
ATOM   501  C  CA   B LYS   A 1 19  ? 10.147 -6.415  10.707  0.28 13.26 ?  19  LYS   A CA   1 
ATOM   502  C  C    A LYS   A 1 19  ? 9.707  -5.369  9.146   0.72 12.81 ?  19  LYS   A C    1 
ATOM   503  C  C    B LYS   A 1 19  ? 9.871  -5.191  9.852   0.28 13.63 ?  19  LYS   A C    1 
ATOM   504  O  O    A LYS   A 1 19  ? 10.606 -4.983  8.397   0.72 13.09 ?  19  LYS   A O    1 
ATOM   505  O  O    B LYS   A 1 19  ? 10.699 -4.802  9.025   0.28 13.45 ?  19  LYS   A O    1 
ATOM   506  C  CB   A LYS   A 1 19  ? 10.592 -6.247  11.309  0.72 14.53 ?  19  LYS   A CB   1 
ATOM   507  C  CB   B LYS   A 1 19  ? 10.921 -5.995  11.966  0.28 13.63 ?  19  LYS   A CB   1 
ATOM   508  C  CG   A LYS   A 1 19  ? 9.831  -5.310  12.233  0.72 15.87 ?  19  LYS   A CG   1 
ATOM   509  C  CG   B LYS   A 1 19  ? 10.184 -5.076  12.926  0.28 14.36 ?  19  LYS   A CG   1 
ATOM   510  C  CD   A LYS   A 1 19  ? 10.686 -5.008  13.457  0.72 17.39 ?  19  LYS   A CD   1 
ATOM   511  C  CD   B LYS   A 1 19  ? 11.089 -4.740  14.104  0.28 15.05 ?  19  LYS   A CD   1 
ATOM   512  C  CE   A LYS   A 1 19  ? 9.999  -4.071  14.426  0.72 18.35 ?  19  LYS   A CE   1 
ATOM   513  C  CE   B LYS   A 1 19  ? 10.397 -3.890  15.154  0.28 15.54 ?  19  LYS   A CE   1 
ATOM   514  N  NZ   A LYS   A 1 19  ? 10.876 -3.778  15.593  0.72 19.18 ?  19  LYS   A NZ   1 
ATOM   515  N  NZ   B LYS   A 1 19  ? 11.274 -3.720  16.350  0.28 15.69 ?  19  LYS   A NZ   1 
ATOM   516  H  H    A LYS   A 1 19  ? 11.255 -7.228  8.702   0.72 14.22 ?  19  LYS   A H    1 
ATOM   517  H  H    B LYS   A 1 19  ? 11.505 -7.001  9.413   0.28 14.77 ?  19  LYS   A H    1 
ATOM   518  H  HA   A LYS   A 1 19  ? 9.024  -7.016  10.191  0.72 15.71 ?  19  LYS   A HA   1 
ATOM   519  H  HA   B LYS   A 1 19  ? 9.305  -6.799  10.977  0.28 15.96 ?  19  LYS   A HA   1 
ATOM   520  H  HB2  A LYS   A 1 19  ? 10.760 -7.066  11.803  0.72 17.48 ?  19  LYS   A HB2  1 
ATOM   521  H  HB2  B LYS   A 1 19  ? 11.149 -6.791  12.467  0.28 16.40 ?  19  LYS   A HB2  1 
ATOM   522  H  HB3  A LYS   A 1 19  ? 11.432 -5.824  11.089  0.72 17.48 ?  19  LYS   A HB3  1 
ATOM   523  H  HB3  B LYS   A 1 19  ? 11.734 -5.535  11.700  0.28 16.40 ?  19  LYS   A HB3  1 
ATOM   524  H  HG2  A LYS   A 1 19  ? 9.641  -4.479  11.770  0.72 19.10 ?  19  LYS   A HG2  1 
ATOM   525  H  HG2  B LYS   A 1 19  ? 9.946  -4.250  12.478  0.28 17.28 ?  19  LYS   A HG2  1 
ATOM   526  H  HG3  A LYS   A 1 19  ? 9.007  -5.735  12.524  0.72 19.10 ?  19  LYS   A HG3  1 
ATOM   527  H  HG3  B LYS   A 1 19  ? 9.392  -5.522  13.265  0.28 17.28 ?  19  LYS   A HG3  1 
ATOM   528  H  HD2  A LYS   A 1 19  ? 10.877 -5.838  13.924  0.72 20.92 ?  19  LYS   A HD2  1 
ATOM   529  H  HD2  B LYS   A 1 19  ? 11.370 -5.564  14.531  0.28 18.11 ?  19  LYS   A HD2  1 
ATOM   530  H  HD3  A LYS   A 1 19  ? 11.514 -4.592  13.170  0.72 20.92 ?  19  LYS   A HD3  1 
ATOM   531  H  HD3  B LYS   A 1 19  ? 11.861 -4.251  13.781  0.28 18.11 ?  19  LYS   A HD3  1 
ATOM   532  H  HE2  A LYS   A 1 19  ? 9.798  -3.235  13.976  0.72 22.07 ?  19  LYS   A HE2  1 
ATOM   533  H  HE2  B LYS   A 1 19  ? 10.209 -3.011  14.786  0.28 18.70 ?  19  LYS   A HE2  1 
ATOM   534  H  HE3  A LYS   A 1 19  ? 9.184  -4.484  14.750  0.72 22.07 ?  19  LYS   A HE3  1 
ATOM   535  H  HE3  B LYS   A 1 19  ? 9.577  -4.323  15.434  0.28 18.70 ?  19  LYS   A HE3  1 
ATOM   536  H  HZ1  A LYS   A 1 19  ? 10.452 -3.245  16.163  0.72 23.06 ?  19  LYS   A HZ1  1 
ATOM   537  H  HZ1  B LYS   A 1 19  ? 10.861 -3.221  16.962  0.28 18.87 ?  19  LYS   A HZ1  1 
ATOM   538  H  HZ2  A LYS   A 1 19  ? 11.090 -4.536  16.007  0.72 23.06 ?  19  LYS   A HZ2  1 
ATOM   539  H  HZ2  B LYS   A 1 19  ? 11.462 -4.514  16.705  0.28 18.87 ?  19  LYS   A HZ2  1 
ATOM   540  H  HZ3  A LYS   A 1 19  ? 11.620 -3.378  15.318  0.72 23.06 ?  19  LYS   A HZ3  1 
ATOM   541  H  HZ3  B LYS   A 1 19  ? 12.034 -3.319  16.117  0.28 18.87 ?  19  LYS   A HZ3  1 
ATOM   542  N  N    A ASN   A 1 20  ? 8.535  -4.739  9.261   0.72 13.39 ?  20  ASN   A N    1 
ATOM   543  N  N    B ASN   A 1 20  ? 8.702  -4.592  10.053  0.28 14.81 ?  20  ASN   A N    1 
ATOM   544  C  CA   A ASN   A 1 20  ? 8.307  -3.423  8.664   0.72 14.74 ?  20  ASN   A CA   1 
ATOM   545  C  CA   B ASN   A 1 20  ? 8.338  -3.352  9.375   0.28 16.30 ?  20  ASN   A CA   1 
ATOM   546  C  C    A ASN   A 1 20  ? 8.903  -2.393  9.613   0.72 15.97 ?  20  ASN   A C    1 
ATOM   547  C  C    B ASN   A 1 20  ? 8.932  -2.190  10.161  0.28 16.57 ?  20  ASN   A C    1 
ATOM   548  O  O    A ASN   A 1 20  ? 8.355  -2.138  10.689  0.72 17.44 ?  20  ASN   A O    1 
ATOM   549  O  O    B ASN   A 1 20  ? 8.351  -1.728  11.146  0.28 17.11 ?  20  ASN   A O    1 
ATOM   550  C  CB   A ASN   A 1 20  ? 6.812  -3.193  8.437   0.72 15.66 ?  20  ASN   A CB   1 
ATOM   551  C  CB   B ASN   A 1 20  ? 6.822  -3.244  9.274   0.28 17.44 ?  20  ASN   A CB   1 
ATOM   552  C  CG   A ASN   A 1 20  ? 6.476  -1.762  8.000   0.72 17.20 ?  20  ASN   A CG   1 
ATOM   553  C  CG   B ASN   A 1 20  ? 6.365  -1.895  8.762   0.28 18.67 ?  20  ASN   A CG   1 
ATOM   554  O  OD1  A ASN   A 1 20  ? 5.436  -1.223  8.380   0.72 19.36 ?  20  ASN   A OD1  1 
ATOM   555  O  OD1  B ASN   A 1 20  ? 5.671  -1.156  9.461   0.28 19.17 ?  20  ASN   A OD1  1 
ATOM   556  N  ND2  A ASN   A 1 20  ? 7.335  -1.159  7.187   0.72 17.36 ?  20  ASN   A ND2  1 
ATOM   557  N  ND2  B ASN   A 1 20  ? 6.755  -1.564  7.539   0.28 19.10 ?  20  ASN   A ND2  1 
ATOM   558  H  H    A ASN   A 1 20  ? 7.859  -5.060  9.688   0.72 16.12 ?  20  ASN   A H    1 
ATOM   559  H  H    B ASN   A 1 20  ? 8.096  -4.892  10.577  0.28 17.82 ?  20  ASN   A H    1 
ATOM   560  H  HA   A ASN   A 1 20  ? 8.766  -3.373  7.813   0.72 17.74 ?  20  ASN   A HA   1 
ATOM   561  H  HA   B ASN   A 1 20  ? 8.711  -3.354  8.484   0.28 19.61 ?  20  ASN   A HA   1 
ATOM   562  H  HB2  A ASN   A 1 20  ? 6.505  -3.794  7.742   0.72 18.85 ?  20  ASN   A HB2  1 
ATOM   563  H  HB2  B ASN   A 1 20  ? 6.501  -3.926  8.663   0.28 20.98 ?  20  ASN   A HB2  1 
ATOM   564  H  HB3  A ASN   A 1 20  ? 6.340  -3.381  9.265   0.72 18.85 ?  20  ASN   A HB3  1 
ATOM   565  H  HB3  B ASN   A 1 20  ? 6.438  -3.380  10.154  0.28 20.98 ?  20  ASN   A HB3  1 
ATOM   566  H  HD21 A ASN   A 1 20  ? 7.179  -0.355  6.929   0.72 20.88 ?  20  ASN   A HD21 1 
ATOM   567  H  HD21 B ASN   A 1 20  ? 6.517  -0.810  7.204   0.28 22.97 ?  20  ASN   A HD21 1 
ATOM   568  H  HD22 A ASN   A 1 20  ? 8.046  -1.566  6.932   0.72 20.88 ?  20  ASN   A HD22 1 
ATOM   569  H  HD22 B ASN   A 1 20  ? 7.245  -2.104  7.082   0.28 22.97 ?  20  ASN   A HD22 1 
ATOM   570  N  N    A ALA   A 1 21  ? 10.055 -1.836  9.249   0.72 16.15 ?  21  ALA   A N    1 
ATOM   571  N  N    B ALA   A 1 21  ? 10.099 -1.715  9.730   0.28 16.59 ?  21  ALA   A N    1 
ATOM   572  C  CA   A ALA   A 1 21  ? 10.748 -0.949  10.171  0.72 16.32 ?  21  ALA   A CA   1 
ATOM   573  C  CA   B ALA   A 1 21  ? 10.763 -0.615  10.416  0.28 16.33 ?  21  ALA   A CA   1 
ATOM   574  C  C    A ALA   A 1 21  ? 11.710 -0.056  9.412   0.72 16.12 ?  21  ALA   A C    1 
ATOM   575  C  C    B ALA   A 1 21  ? 11.867 -0.057  9.530   0.28 15.62 ?  21  ALA   A C    1 
ATOM   576  O  O    A ALA   A 1 21  ? 12.172 -0.400  8.320   0.72 16.14 ?  21  ALA   A O    1 
ATOM   577  O  O    B ALA   A 1 21  ? 12.415 -0.763  8.679   0.28 15.66 ?  21  ALA   A O    1 
ATOM   578  C  CB   A ALA   A 1 21  ? 11.511 -1.729  11.246  0.72 17.47 ?  21  ALA   A CB   1 
ATOM   579  C  CB   B ALA   A 1 21  ? 11.348 -1.067  11.762  0.28 16.97 ?  21  ALA   A CB   1 
ATOM   580  H  H    A ALA   A 1 21  ? 10.445 -1.962  8.494   0.72 19.43 ?  21  ALA   A H    1 
ATOM   581  H  H    B ALA   A 1 21  ? 10.527 -2.013  9.046   0.28 19.96 ?  21  ALA   A H    1 
ATOM   582  H  HA   A ALA   A 1 21  ? 10.090 -0.387  10.614  0.72 19.63 ?  21  ALA   A HA   1 
ATOM   583  H  HA   B ALA   A 1 21  ? 10.121 0.089   10.587  0.28 19.65 ?  21  ALA   A HA   1 
ATOM   584  H  HB1  A ALA   A 1 21  ? 11.932 -1.099  11.848  0.72 21.01 ?  21  ALA   A HB1  1 
ATOM   585  H  HB1  B ALA   A 1 21  ? 11.786 -0.310  12.186  0.28 20.42 ?  21  ALA   A HB1  1 
ATOM   586  H  HB2  A ALA   A 1 21  ? 10.883 -2.286  11.738  0.72 21.01 ?  21  ALA   A HB2  1 
ATOM   587  H  HB2  B ALA   A 1 21  ? 10.629 -1.389  12.330  0.28 20.42 ?  21  ALA   A HB2  1 
ATOM   588  H  HB3  A ALA   A 1 21  ? 12.179 -2.284  10.819  0.72 21.01 ?  21  ALA   A HB3  1 
ATOM   589  H  HB3  B ALA   A 1 21  ? 11.990 -1.776  11.608  0.28 20.42 ?  21  ALA   A HB3  1 
ATOM   590  N  N    A ASP   A 1 22  ? 11.981 1.103   10.015  0.72 16.73 ?  22  ASP   A N    1 
ATOM   591  N  N    B ASP   A 1 22  ? 12.160 1.227   9.729   0.28 15.18 ?  22  ASP   A N    1 
ATOM   592  C  CA   A ASP   A 1 22  ? 13.021 2.020   9.568   0.72 16.64 ?  22  ASP   A CA   1 
ATOM   593  C  CA   B ASP   A 1 22  ? 13.358 1.837   9.166   0.28 14.76 ?  22  ASP   A CA   1 
ATOM   594  C  C    A ASP   A 1 22  ? 14.349 1.524   10.130  0.72 15.00 ?  22  ASP   A C    1 
ATOM   595  C  C    B ASP   A 1 22  ? 14.583 1.190   9.802   0.28 13.77 ?  22  ASP   A C    1 
ATOM   596  O  O    A ASP   A 1 22  ? 14.543 1.508   11.349  0.72 15.54 ?  22  ASP   A O    1 
ATOM   597  O  O    B ASP   A 1 22  ? 14.677 1.093   11.029  0.28 13.87 ?  22  ASP   A O    1 
ATOM   598  C  CB   A ASP   A 1 22  ? 12.694 3.416   10.090  0.72 18.79 ?  22  ASP   A CB   1 
ATOM   599  C  CB   B ASP   A 1 22  ? 13.330 3.338   9.481   0.28 15.47 ?  22  ASP   A CB   1 
ATOM   600  C  CG   A ASP   A 1 22  ? 13.666 4.471   9.601   0.72 20.87 ?  22  ASP   A CG   1 
ATOM   601  C  CG   B ASP   A 1 22  ? 14.425 4.131   8.778   0.28 15.87 ?  22  ASP   A CG   1 
ATOM   602  O  OD1  A ASP   A 1 22  ? 14.825 4.140   9.292   0.72 21.18 ?  22  ASP   A OD1  1 
ATOM   603  O  OD1  B ASP   A 1 22  ? 15.354 3.528   8.205   0.28 15.66 ?  22  ASP   A OD1  1 
ATOM   604  O  OD2  A ASP   A 1 22  ? 13.271 5.650   9.539   0.72 22.84 -1 22  ASP   A OD2  1 
ATOM   605  O  OD2  B ASP   A 1 22  ? 14.348 5.380   8.808   0.28 16.21 -1 22  ASP   A OD2  1 
ATOM   606  H  H    A ASP   A 1 22  ? 11.540 1.394   10.701  0.72 20.12 ?  22  ASP   A H    1 
ATOM   607  H  H    B ASP   A 1 22  ? 11.667 1.765   10.184  0.28 18.27 ?  22  ASP   A H    1 
ATOM   608  H  HA   A ASP   A 1 22  ? 13.060 2.037   8.599   0.72 20.01 ?  22  ASP   A HA   1 
ATOM   609  H  HA   B ASP   A 1 22  ? 13.376 1.705   8.203   0.28 17.76 ?  22  ASP   A HA   1 
ATOM   610  H  HB2  A ASP   A 1 22  ? 11.800 3.665   9.797   0.72 22.59 ?  22  ASP   A HB2  1 
ATOM   611  H  HB2  B ASP   A 1 22  ? 12.478 3.701   9.204   0.28 18.62 ?  22  ASP   A HB2  1 
ATOM   612  H  HB3  A ASP   A 1 22  ? 12.722 3.402   11.063  0.72 22.59 ?  22  ASP   A HB3  1 
ATOM   613  H  HB3  B ASP   A 1 22  ? 13.449 3.453   10.435  0.28 18.62 ?  22  ASP   A HB3  1 
ATOM   614  N  N    A ILE   A 1 23  ? 15.262 1.114   9.245   0.72 14.17 ?  23  ILE   A N    1 
ATOM   615  N  N    B ILE   A 1 23  ? 15.514 0.721   8.965   0.28 13.34 ?  23  ILE   A N    1 
ATOM   616  C  CA   A ILE   A 1 23  ? 16.518 0.505   9.684   0.72 13.57 ?  23  ILE   A CA   1 
ATOM   617  C  CA   B ILE   A 1 23  ? 16.727 0.087   9.477   0.28 12.95 ?  23  ILE   A CA   1 
ATOM   618  C  C    A ILE   A 1 23  ? 17.318 1.447   10.573  0.72 13.60 ?  23  ILE   A C    1 
ATOM   619  C  C    B ILE   A 1 23  ? 17.483 1.039   10.390  0.28 13.51 ?  23  ILE   A C    1 
ATOM   620  O  O    A ILE   A 1 23  ? 18.041 0.997   11.473  0.72 14.20 ?  23  ILE   A O    1 
ATOM   621  O  O    B ILE   A 1 23  ? 18.142 0.609   11.345  0.28 13.35 ?  23  ILE   A O    1 
ATOM   622  C  CB   A ILE   A 1 23  ? 17.328 0.004   8.470   0.72 13.56 ?  23  ILE   A CB   1 
ATOM   623  C  CB   B ILE   A 1 23  ? 17.612 -0.448  8.326   0.28 12.37 ?  23  ILE   A CB   1 
ATOM   624  C  CG1  A ILE   A 1 23  ? 18.464 -0.911  8.933   0.72 14.09 ?  23  ILE   A CG1  1 
ATOM   625  C  CG1  B ILE   A 1 23  ? 18.697 -1.379  8.882   0.28 12.18 ?  23  ILE   A CG1  1 
ATOM   626  C  CG2  A ILE   A 1 23  ? 17.840 1.175   7.633   0.72 13.37 ?  23  ILE   A CG2  1 
ATOM   627  C  CG2  B ILE   A 1 23  ? 18.235 0.699   7.530   0.28 12.22 ?  23  ILE   A CG2  1 
ATOM   628  C  CD1  A ILE   A 1 23  ? 19.157 -1.640  7.800   0.72 14.72 ?  23  ILE   A CD1  1 
ATOM   629  C  CD1  B ILE   A 1 23  ? 19.575 -2.024  7.822   0.28 11.97 ?  23  ILE   A CD1  1 
ATOM   630  H  H    A ILE   A 1 23  ? 15.169 1.172   8.397   0.72 17.05 ?  23  ILE   A H    1 
ATOM   631  H  H    B ILE   A 1 23  ? 15.470 0.748   8.118   0.28 16.06 ?  23  ILE   A H    1 
ATOM   632  H  HA   A ILE   A 1 23  ? 16.302 -0.271  10.221  0.72 16.33 ?  23  ILE   A HA   1 
ATOM   633  H  HA   B ILE   A 1 23  ? 16.462 -0.678  10.006  0.28 15.59 ?  23  ILE   A HA   1 
ATOM   634  H  HB   A ILE   A 1 23  ? 16.734 -0.521  7.915   0.72 16.32 ?  23  ILE   A HB   1 
ATOM   635  H  HB   B ILE   A 1 23  ? 17.054 -0.964  7.725   0.28 14.89 ?  23  ILE   A HB   1 
ATOM   636  H  HG12 A ILE   A 1 23  ? 19.132 -0.378  9.393   0.72 16.96 ?  23  ILE   A HG12 1 
ATOM   637  H  HG12 B ILE   A 1 23  ? 19.277 -0.870  9.470   0.28 14.67 ?  23  ILE   A HG12 1 
ATOM   638  H  HG13 A ILE   A 1 23  ? 18.104 -1.579  9.539   0.72 16.96 ?  23  ILE   A HG13 1 
ATOM   639  H  HG13 B ILE   A 1 23  ? 18.270 -2.093  9.382   0.28 14.67 ?  23  ILE   A HG13 1 
ATOM   640  H  HG21 A ILE   A 1 23  ? 18.200 0.835   6.800   0.72 16.09 ?  23  ILE   A HG21 1 
ATOM   641  H  HG21 B ILE   A 1 23  ? 18.624 0.341   6.713   0.28 14.72 ?  23  ILE   A HG21 1 
ATOM   642  H  HG22 A ILE   A 1 23  ? 17.097 1.777   7.448   0.72 16.09 ?  23  ILE   A HG22 1 
ATOM   643  H  HG22 B ILE   A 1 23  ? 17.543 1.340   7.311   0.28 14.72 ?  23  ILE   A HG22 1 
ATOM   644  H  HG23 A ILE   A 1 23  ? 18.528 1.646   8.126   0.72 16.09 ?  23  ILE   A HG23 1 
ATOM   645  H  HG23 B ILE   A 1 23  ? 18.924 1.121   8.065   0.28 14.72 ?  23  ILE   A HG23 1 
ATOM   646  H  HD11 A ILE   A 1 23  ? 19.824 -2.237  8.170   0.72 17.71 ?  23  ILE   A HD11 1 
ATOM   647  H  HD11 B ILE   A 1 23  ? 20.157 -2.676  8.248   0.28 14.42 ?  23  ILE   A HD11 1 
ATOM   648  H  HD12 A ILE   A 1 23  ? 18.495 -2.149  7.304   0.72 17.71 ?  23  ILE   A HD12 1 
ATOM   649  H  HD12 B ILE   A 1 23  ? 19.009 -2.465  7.170   0.28 14.42 ?  23  ILE   A HD12 1 
ATOM   650  H  HD13 A ILE   A 1 23  ? 19.577 -0.990  7.217   0.72 17.71 ?  23  ILE   A HD13 1 
ATOM   651  H  HD13 B ILE   A 1 23  ? 20.108 -1.339  7.391   0.28 14.42 ?  23  ILE   A HD13 1 
ATOM   652  N  N    A VAL   A 1 24  ? 17.202 2.758   10.350  0.72 14.51 ?  24  VAL   A N    1 
ATOM   653  N  N    B VAL   A 1 24  ? 17.389 2.342   10.126  0.28 14.47 ?  24  VAL   A N    1 
ATOM   654  C  CA   A VAL   A 1 24  ? 17.893 3.719   11.207  0.72 15.72 ?  24  VAL   A CA   1 
ATOM   655  C  CA   B VAL   A 1 24  ? 18.033 3.328   10.986  0.28 15.23 ?  24  VAL   A CA   1 
ATOM   656  C  C    A VAL   A 1 24  ? 17.361 3.638   12.630  0.72 16.44 ?  24  VAL   A C    1 
ATOM   657  C  C    B VAL   A 1 24  ? 17.412 3.309   12.377  0.28 15.95 ?  24  VAL   A C    1 
ATOM   658  O  O    A VAL   A 1 24  ? 18.125 3.542   13.599  0.72 17.06 ?  24  VAL   A O    1 
ATOM   659  O  O    B VAL   A 1 24  ? 18.119 3.368   13.391  0.28 16.56 ?  24  VAL   A O    1 
ATOM   660  C  CB   A VAL   A 1 24  ? 17.759 5.141   10.635  0.72 16.52 ?  24  VAL   A CB   1 
ATOM   661  C  CB   B VAL   A 1 24  ? 17.957 4.721   10.334  0.28 15.67 ?  24  VAL   A CB   1 
ATOM   662  C  CG1  A VAL   A 1 24  ? 18.223 6.180   11.656  0.72 17.15 ?  24  VAL   A CG1  1 
ATOM   663  C  CG1  B VAL   A 1 24  ? 18.601 5.761   11.229  0.28 16.36 ?  24  VAL   A CG1  1 
ATOM   664  C  CG2  A VAL   A 1 24  ? 18.543 5.264   9.344   0.72 17.42 ?  24  VAL   A CG2  1 
ATOM   665  C  CG2  B VAL   A 1 24  ? 18.620 4.692   8.964   0.28 15.50 ?  24  VAL   A CG2  1 
ATOM   666  H  H    A VAL   A 1 24  ? 16.736 3.110   9.717   0.72 17.45 ?  24  VAL   A H    1 
ATOM   667  H  H    B VAL   A 1 24  ? 16.961 2.675   9.461   0.28 17.41 ?  24  VAL   A H    1 
ATOM   668  H  HA   A VAL   A 1 24  ? 18.836 3.500   11.229  0.72 18.91 ?  24  VAL   A HA   1 
ATOM   669  H  HA   B VAL   A 1 24  ? 18.969 3.097   11.079  0.28 18.32 ?  24  VAL   A HA   1 
ATOM   670  H  HB   A VAL   A 1 24  ? 16.827 5.318   10.430  0.72 19.88 ?  24  VAL   A HB   1 
ATOM   671  H  HB   B VAL   A 1 24  ? 17.026 4.963   10.211  0.28 18.86 ?  24  VAL   A HB   1 
ATOM   672  H  HG11 A VAL   A 1 24  ? 18.408 7.012   11.193  0.72 20.63 ?  24  VAL   A HG11 1 
ATOM   673  H  HG11 B VAL   A 1 24  ? 18.717 6.580   10.724  0.28 19.68 ?  24  VAL   A HG11 1 
ATOM   674  H  HG12 A VAL   A 1 24  ? 17.523 6.313   12.310  0.72 20.63 ?  24  VAL   A HG12 1 
ATOM   675  H  HG12 B VAL   A 1 24  ? 18.024 5.922   11.993  0.28 19.68 ?  24  VAL   A HG12 1 
ATOM   676  H  HG13 A VAL   A 1 24  ? 19.030 5.855   12.086  0.72 20.63 ?  24  VAL   A HG13 1 
ATOM   677  H  HG13 B VAL   A 1 24  ? 19.462 5.430   11.526  0.28 19.68 ?  24  VAL   A HG13 1 
ATOM   678  H  HG21 A VAL   A 1 24  ? 18.321 6.107   8.913   0.72 20.95 ?  24  VAL   A HG21 1 
ATOM   679  H  HG21 B VAL   A 1 24  ? 18.652 5.594   8.609   0.28 18.65 ?  24  VAL   A HG21 1 
ATOM   680  H  HG22 A VAL   A 1 24  ? 19.494 5.245   9.546   0.72 20.95 ?  24  VAL   A HG22 1 
ATOM   681  H  HG22 B VAL   A 1 24  ? 19.522 4.344   9.057   0.28 18.65 ?  24  VAL   A HG22 1 
ATOM   682  H  HG23 A VAL   A 1 24  ? 18.316 4.526   8.756   0.72 20.95 ?  24  VAL   A HG23 1 
ATOM   683  H  HG23 B VAL   A 1 24  ? 18.107 4.121   8.372   0.28 18.65 ?  24  VAL   A HG23 1 
ATOM   684  N  N    A GLU   A 1 25  ? 16.035 3.686   12.775  0.72 17.19 ?  25  GLU   A N    1 
ATOM   685  N  N    B GLU   A 1 25  ? 16.081 3.219   12.449  0.28 16.33 ?  25  GLU   A N    1 
ATOM   686  C  CA   A GLU   A 1 25  ? 15.441 3.624   14.105  0.72 18.44 ?  25  GLU   A CA   1 
ATOM   687  C  CA   B GLU   A 1 25  ? 15.415 3.156   13.747  0.28 17.34 ?  25  GLU   A CA   1 
ATOM   688  C  C    A GLU   A 1 25  ? 15.683 2.266   14.751  0.72 17.33 ?  25  GLU   A C    1 
ATOM   689  C  C    B GLU   A 1 25  ? 15.679 1.824   14.442  0.28 17.24 ?  25  GLU   A C    1 
ATOM   690  O  O    A GLU   A 1 25  ? 15.910 2.180   15.964  0.72 17.97 ?  25  GLU   A O    1 
ATOM   691  O  O    B GLU   A 1 25  ? 15.859 1.783   15.664  0.28 17.41 ?  25  GLU   A O    1 
ATOM   692  C  CB   A GLU   A 1 25  ? 13.949 3.958   14.028  0.72 21.06 ?  25  GLU   A CB   1 
ATOM   693  C  CB   B GLU   A 1 25  ? 13.916 3.421   13.584  0.28 18.49 ?  25  GLU   A CB   1 
ATOM   694  C  CG   A GLU   A 1 25  ? 13.679 5.419   13.682  0.72 24.33 ?  25  GLU   A CG   1 
ATOM   695  C  CG   B GLU   A 1 25  ? 13.599 4.816   13.060  0.28 20.20 ?  25  GLU   A CG   1 
ATOM   696  C  CD   A GLU   A 1 25  ? 14.470 6.390   14.548  0.72 27.14 ?  25  GLU   A CD   1 
ATOM   697  C  CD   B GLU   A 1 25  ? 14.054 5.907   14.005  0.28 21.61 ?  25  GLU   A CD   1 
ATOM   698  O  OE1  A GLU   A 1 25  ? 14.539 6.179   15.778  0.72 28.01 ?  25  GLU   A OE1  1 
ATOM   699  O  OE1  B GLU   A 1 25  ? 13.963 5.700   15.235  0.28 22.36 ?  25  GLU   A OE1  1 
ATOM   700  O  OE2  A GLU   A 1 25  ? 15.043 7.350   13.993  0.72 28.47 -1 25  GLU   A OE2  1 
ATOM   701  O  OE2  B GLU   A 1 25  ? 14.506 6.966   13.521  0.28 22.25 -1 25  GLU   A OE2  1 
ATOM   702  H  H    A GLU   A 1 25  ? 15.469 3.768   12.128  0.72 20.67 ?  25  GLU   A H    1 
ATOM   703  H  H    B GLU   A 1 25  ? 15.552 3.196   11.771  0.28 19.65 ?  25  GLU   A H    1 
ATOM   704  H  HA   A GLU   A 1 25  ? 15.866 4.289   14.667  0.72 22.17 ?  25  GLU   A HA   1 
ATOM   705  H  HA   B GLU   A 1 25  ? 15.776 3.853   14.312  0.28 20.86 ?  25  GLU   A HA   1 
ATOM   706  H  HB2  A GLU   A 1 25  ? 13.532 3.413   13.337  0.72 25.31 ?  25  GLU   A HB2  1 
ATOM   707  H  HB2  B GLU   A 1 25  ? 13.547 2.781   12.957  0.28 22.24 ?  25  GLU   A HB2  1 
ATOM   708  H  HB3  A GLU   A 1 25  ? 13.532 3.777   14.884  0.72 25.31 ?  25  GLU   A HB3  1 
ATOM   709  H  HB3  B GLU   A 1 25  ? 13.484 3.325   14.448  0.28 22.24 ?  25  GLU   A HB3  1 
ATOM   710  H  HG2  A GLU   A 1 25  ? 13.938 5.578   12.763  0.72 29.24 ?  25  GLU   A HG2  1 
ATOM   711  H  HG2  B GLU   A 1 25  ? 14.045 4.947   12.207  0.28 24.29 ?  25  GLU   A HG2  1 
ATOM   712  H  HG3  A GLU   A 1 25  ? 12.732 5.602   13.800  0.72 29.24 ?  25  GLU   A HG3  1 
ATOM   713  H  HG3  B GLU   A 1 25  ? 12.640 4.909   12.950  0.28 24.29 ?  25  GLU   A HG3  1 
ATOM   714  N  N    A GLU   A 1 26  ? 15.656 1.195   13.955  0.72 16.99 ?  26  GLU   A N    1 
ATOM   715  N  N    B GLU   A 1 26  ? 15.712 0.724   13.684  0.28 17.11 ?  26  GLU   A N    1 
ATOM   716  C  CA   A GLU   A 1 26  ? 15.954 -0.133  14.485  0.72 17.16 ?  26  GLU   A CA   1 
ATOM   717  C  CA   B GLU   A 1 26  ? 16.105 -0.553  14.272  0.28 17.55 ?  26  GLU   A CA   1 
ATOM   718  C  C    A GLU   A 1 26  ? 17.380 -0.204  15.020  0.72 16.29 ?  26  GLU   A C    1 
ATOM   719  C  C    B GLU   A 1 26  ? 17.528 -0.502  14.808  0.28 17.62 ?  26  GLU   A C    1 
ATOM   720  O  O    A GLU   A 1 26  ? 17.617 -0.702  16.127  0.72 16.46 ?  26  GLU   A O    1 
ATOM   721  O  O    B GLU   A 1 26  ? 17.837 -1.149  15.815  0.28 17.36 ?  26  GLU   A O    1 
ATOM   722  C  CB   A GLU   A 1 26  ? 15.752 -1.184  13.394  0.72 19.06 ?  26  GLU   A CB   1 
ATOM   723  C  CB   B GLU   A 1 26  ? 15.971 -1.680  13.244  0.28 18.11 ?  26  GLU   A CB   1 
ATOM   724  C  CG   A GLU   A 1 26  ? 14.340 -1.700  13.251  0.72 22.42 ?  26  GLU   A CG   1 
ATOM   725  C  CG   B GLU   A 1 26  ? 14.557 -2.184  13.059  0.28 18.57 ?  26  GLU   A CG   1 
ATOM   726  C  CD   A GLU   A 1 26  ? 13.886 -2.522  14.446  0.72 24.67 ?  26  GLU   A CD   1 
ATOM   727  C  CD   B GLU   A 1 26  ? 13.945 -2.699  14.338  0.28 18.81 ?  26  GLU   A CD   1 
ATOM   728  O  OE1  A GLU   A 1 26  ? 14.339 -3.680  14.612  0.72 25.64 ?  26  GLU   A OE1  1 
ATOM   729  O  OE1  B GLU   A 1 26  ? 14.527 -3.615  14.962  0.28 19.12 ?  26  GLU   A OE1  1 
ATOM   730  O  OE2  A GLU   A 1 26  ? 13.071 -1.996  15.222  0.72 26.05 -1 26  GLU   A OE2  1 
ATOM   731  O  OE2  B GLU   A 1 26  ? 12.878 -2.178  14.714  0.28 18.08 -1 26  GLU   A OE2  1 
ATOM   732  H  H    A GLU   A 1 26  ? 15.465 1.221   13.117  0.72 20.43 ?  26  GLU   A H    1 
ATOM   733  H  H    B GLU   A 1 26  ? 15.512 0.691   12.848  0.28 20.58 ?  26  GLU   A H    1 
ATOM   734  H  HA   A GLU   A 1 26  ? 15.343 -0.321  15.211  0.72 20.64 ?  26  GLU   A HA   1 
ATOM   735  H  HA   B GLU   A 1 26  ? 15.521 -0.749  15.017  0.28 21.11 ?  26  GLU   A HA   1 
ATOM   736  H  HB2  A GLU   A 1 26  ? 16.012 -0.794  12.541  0.72 22.92 ?  26  GLU   A HB2  1 
ATOM   737  H  HB2  B GLU   A 1 26  ? 16.279 -1.359  12.381  0.28 21.79 ?  26  GLU   A HB2  1 
ATOM   738  H  HB3  A GLU   A 1 26  ? 16.326 -1.936  13.594  0.72 22.92 ?  26  GLU   A HB3  1 
ATOM   739  H  HB3  B GLU   A 1 26  ? 16.516 -2.432  13.525  0.28 21.79 ?  26  GLU   A HB3  1 
ATOM   740  H  HG2  A GLU   A 1 26  ? 13.741 -0.941  13.156  0.72 26.95 ?  26  GLU   A HG2  1 
ATOM   741  H  HG2  B GLU   A 1 26  ? 14.004 -1.461  12.728  0.28 22.33 ?  26  GLU   A HG2  1 
ATOM   742  H  HG3  A GLU   A 1 26  ? 14.291 -2.261  12.464  0.72 26.95 ?  26  GLU   A HG3  1 
ATOM   743  H  HG3  B GLU   A 1 26  ? 14.557 -2.922  12.435  0.28 22.33 ?  26  GLU   A HG3  1 
ATOM   744  N  N    A ALA   A 1 27  ? 18.351 0.273   14.237  0.72 15.21 ?  27  ALA   A N    1 
ATOM   745  N  N    B ALA   A 1 27  ? 18.406 0.259   14.155  0.28 17.86 ?  27  ALA   A N    1 
ATOM   746  C  CA   A ALA   A 1 27  ? 19.739 0.218   14.687  0.72 15.65 ?  27  ALA   A CA   1 
ATOM   747  C  CA   B ALA   A 1 27  ? 19.791 0.337   14.606  0.28 18.54 ?  27  ALA   A CA   1 
ATOM   748  C  C    A ALA   A 1 27  ? 19.936 1.039   15.955  0.72 17.12 ?  27  ALA   A C    1 
ATOM   749  C  C    B ALA   A 1 27  ? 19.901 1.116   15.912  0.28 20.14 ?  27  ALA   A C    1 
ATOM   750  O  O    A ALA   A 1 27  ? 20.612 0.598   16.891  0.72 17.23 ?  27  ALA   A O    1 
ATOM   751  O  O    B ALA   A 1 27  ? 20.572 0.678   16.854  0.28 20.01 ?  27  ALA   A O    1 
ATOM   752  C  CB   A ALA   A 1 27  ? 20.687 0.682   13.578  0.72 14.98 ?  27  ALA   A CB   1 
ATOM   753  C  CB   B ALA   A 1 27  ? 20.660 0.968   13.518  0.28 18.11 ?  27  ALA   A CB   1 
ATOM   754  H  H    A ALA   A 1 27  ? 18.234 0.623   13.460  0.72 18.29 ?  27  ALA   A H    1 
ATOM   755  H  H    B ALA   A 1 27  ? 18.224 0.729   13.457  0.28 21.47 ?  27  ALA   A H    1 
ATOM   756  H  HA   A ALA   A 1 27  ? 19.955 -0.702  14.898  0.72 18.83 ?  27  ALA   A HA   1 
ATOM   757  H  HA   B ALA   A 1 27  ? 20.118 -0.562  14.765  0.28 22.29 ?  27  ALA   A HA   1 
ATOM   758  H  HB1  A ALA   A 1 27  ? 21.600 0.629   13.907  0.72 18.02 ?  27  ALA   A HB1  1 
ATOM   759  H  HB1  B ALA   A 1 27  ? 21.579 0.988   13.826  0.28 21.78 ?  27  ALA   A HB1  1 
ATOM   760  H  HB2  A ALA   A 1 27  ? 20.580 0.096   12.812  0.72 18.02 ?  27  ALA   A HB2  1 
ATOM   761  H  HB2  B ALA   A 1 27  ? 20.594 0.433   12.711  0.28 21.78 ?  27  ALA   A HB2  1 
ATOM   762  H  HB3  A ALA   A 1 27  ? 20.472 1.592   13.336  0.72 18.02 ?  27  ALA   A HB3  1 
ATOM   763  H  HB3  B ALA   A 1 27  ? 20.347 1.869   13.345  0.28 21.78 ?  27  ALA   A HB3  1 
ATOM   764  N  N    A LYS   A 1 28  ? 19.333 2.229   16.018  0.72 19.23 ?  28  LYS   A N    1 
ATOM   765  N  N    B LYS   A 1 28  ? 19.240 2.275   15.993  0.28 22.12 ?  28  LYS   A N    1 
ATOM   766  C  CA   A LYS   A 1 28  ? 19.465 3.053   17.215  0.72 22.50 ?  28  LYS   A CA   1 
ATOM   767  C  CA   B LYS   A 1 28  ? 19.357 3.104   17.189  0.28 24.42 ?  28  LYS   A CA   1 
ATOM   768  C  C    A LYS   A 1 28  ? 18.901 2.353   18.444  0.72 23.49 ?  28  LYS   A C    1 
ATOM   769  C  C    B LYS   A 1 28  ? 18.780 2.418   18.420  0.28 25.43 ?  28  LYS   A C    1 
ATOM   770  O  O    A LYS   A 1 28  ? 19.441 2.508   19.545  0.72 24.78 ?  28  LYS   A O    1 
ATOM   771  O  O    B LYS   A 1 28  ? 19.219 2.694   19.542  0.28 25.77 ?  28  LYS   A O    1 
ATOM   772  C  CB   A LYS   A 1 28  ? 18.806 4.418   17.001  0.72 25.24 ?  28  LYS   A CB   1 
ATOM   773  C  CB   B LYS   A 1 28  ? 18.684 4.460   16.968  0.28 25.90 ?  28  LYS   A CB   1 
ATOM   774  C  CG   A LYS   A 1 28  ? 19.654 5.359   16.162  0.72 27.67 ?  28  LYS   A CG   1 
ATOM   775  C  CG   B LYS   A 1 28  ? 19.478 5.387   16.066  0.28 27.34 ?  28  LYS   A CG   1 
ATOM   776  C  CD   A LYS   A 1 28  ? 19.154 6.790   16.218  0.72 30.37 ?  28  LYS   A CD   1 
ATOM   777  C  CD   B LYS   A 1 28  ? 18.972 6.819   16.129  0.28 28.93 ?  28  LYS   A CD   1 
ATOM   778  C  CE   A LYS   A 1 28  ? 17.868 6.953   15.439  0.72 32.26 ?  28  LYS   A CE   1 
ATOM   779  C  CE   B LYS   A 1 28  ? 17.661 6.984   15.385  0.28 30.11 ?  28  LYS   A CE   1 
ATOM   780  N  NZ   A LYS   A 1 28  ? 17.452 8.380   15.370  0.72 33.37 ?  28  LYS   A NZ   1 
ATOM   781  N  NZ   B LYS   A 1 28  ? 17.272 8.418   15.277  0.28 30.78 ?  28  LYS   A NZ   1 
ATOM   782  H  H    A LYS   A 1 28  ? 18.856 2.572   15.395  0.72 23.12 ?  28  LYS   A H    1 
ATOM   783  H  H    B LYS   A 1 28  ? 18.734 2.598   15.379  0.28 26.60 ?  28  LYS   A H    1 
ATOM   784  H  HA   A LYS   A 1 28  ? 20.404 3.210   17.386  0.72 27.05 ?  28  LYS   A HA   1 
ATOM   785  H  HA   B LYS   A 1 28  ? 20.296 3.268   17.358  0.28 29.36 ?  28  LYS   A HA   1 
ATOM   786  H  HB2  A LYS   A 1 28  ? 17.961 4.296   16.543  0.72 30.33 ?  28  LYS   A HB2  1 
ATOM   787  H  HB2  B LYS   A 1 28  ? 17.816 4.318   16.561  0.28 31.13 ?  28  LYS   A HB2  1 
ATOM   788  H  HB3  A LYS   A 1 28  ? 18.660 4.841   17.861  0.72 30.33 ?  28  LYS   A HB3  1 
ATOM   789  H  HB3  B LYS   A 1 28  ? 18.577 4.899   17.827  0.28 31.13 ?  28  LYS   A HB3  1 
ATOM   790  H  HG2  A LYS   A 1 28  ? 20.566 5.348   16.493  0.72 33.25 ?  28  LYS   A HG2  1 
ATOM   791  H  HG2  B LYS   A 1 28  ? 20.407 5.383   16.344  0.28 32.86 ?  28  LYS   A HG2  1 
ATOM   792  H  HG3  A LYS   A 1 28  ? 19.631 5.070   15.237  0.72 33.25 ?  28  LYS   A HG3  1 
ATOM   793  H  HG3  B LYS   A 1 28  ? 19.402 5.080   15.149  0.28 32.86 ?  28  LYS   A HG3  1 
ATOM   794  H  HD2  A LYS   A 1 28  ? 18.984 7.036   17.141  0.72 36.49 ?  28  LYS   A HD2  1 
ATOM   795  H  HD2  B LYS   A 1 28  ? 18.828 7.067   17.057  0.28 34.77 ?  28  LYS   A HD2  1 
ATOM   796  H  HD3  A LYS   A 1 28  ? 19.821 7.379   15.831  0.72 36.49 ?  28  LYS   A HD3  1 
ATOM   797  H  HD3  B LYS   A 1 28  ? 19.627 7.408   15.724  0.28 34.77 ?  28  LYS   A HD3  1 
ATOM   798  H  HE2  A LYS   A 1 28  ? 18.000 6.629   14.534  0.72 38.76 ?  28  LYS   A HE2  1 
ATOM   799  H  HE2  B LYS   A 1 28  ? 17.755 6.626   14.488  0.28 36.18 ?  28  LYS   A HE2  1 
ATOM   800  H  HE3  A LYS   A 1 28  ? 17.164 6.450   15.876  0.72 38.76 ?  28  LYS   A HE3  1 
ATOM   801  H  HE3  B LYS   A 1 28  ? 16.960 6.514   15.863  0.28 36.18 ?  28  LYS   A HE3  1 
ATOM   802  H  HZ1  A LYS   A 1 28  ? 16.696 8.454   14.908  0.72 40.10 ?  28  LYS   A HZ1  1 
ATOM   803  H  HZ1  B LYS   A 1 28  ? 16.503 8.492   14.837  0.28 36.98 ?  28  LYS   A HZ1  1 
ATOM   804  H  HZ2  A LYS   A 1 28  ? 17.324 8.699   16.191  0.72 40.10 ?  28  LYS   A HZ2  1 
ATOM   805  H  HZ2  B LYS   A 1 28  ? 17.178 8.769   16.089  0.28 36.98 ?  28  LYS   A HZ2  1 
ATOM   806  H  HZ3  A LYS   A 1 28  ? 18.085 8.862   14.969  0.72 40.10 ?  28  LYS   A HZ3  1 
ATOM   807  H  HZ3  B LYS   A 1 28  ? 17.901 8.871   14.838  0.28 36.98 ?  28  LYS   A HZ3  1 
ATOM   808  N  N    A LYS   A 1 29  ? 17.836 1.568   18.278  0.72 23.75 ?  29  LYS   A N    1 
ATOM   809  N  N    B LYS   A 1 29  ? 17.802 1.531   18.240  0.28 26.27 ?  29  LYS   A N    1 
ATOM   810  C  CA   A LYS   A 1 29  ? 17.238 0.868   19.411  0.72 25.73 ?  29  LYS   A CA   1 
ATOM   811  C  CA   B LYS   A 1 29  ? 17.189 0.849   19.373  0.28 27.32 ?  29  LYS   A CA   1 
ATOM   812  C  C    A LYS   A 1 29  ? 18.054 -0.360  19.799  0.72 25.39 ?  29  LYS   A C    1 
ATOM   813  C  C    B LYS   A 1 29  ? 17.968 -0.393  19.788  0.28 26.22 ?  29  LYS   A C    1 
ATOM   814  O  O    A LYS   A 1 29  ? 18.365 -0.562  20.979  0.72 26.54 ?  29  LYS   A O    1 
ATOM   815  O  O    B LYS   A 1 29  ? 18.172 -0.627  20.985  0.28 26.59 ?  29  LYS   A O    1 
ATOM   816  C  CB   A LYS   A 1 29  ? 15.802 0.463   19.072  0.72 28.48 ?  29  LYS   A CB   1 
ATOM   817  C  CB   B LYS   A 1 29  ? 15.754 0.450   19.023  0.28 29.32 ?  29  LYS   A CB   1 
ATOM   818  C  CG   A LYS   A 1 29  ? 15.059 -0.226  20.210  0.72 31.40 ?  29  LYS   A CG   1 
ATOM   819  C  CG   B LYS   A 1 29  ? 14.963 -0.143  20.180  0.28 31.22 ?  29  LYS   A CG   1 
ATOM   820  C  CD   A LYS   A 1 29  ? 14.741 0.746   21.334  0.72 34.11 ?  29  LYS   A CD   1 
ATOM   821  C  CD   B LYS   A 1 29  ? 14.651 0.907   21.233  0.28 32.86 ?  29  LYS   A CD   1 
ATOM   822  C  CE   A LYS   A 1 29  ? 13.876 0.096   22.403  0.72 35.97 ?  29  LYS   A CE   1 
ATOM   823  C  CE   B LYS   A 1 29  ? 13.755 0.347   22.325  0.28 34.02 ?  29  LYS   A CE   1 
ATOM   824  N  NZ   A LYS   A 1 29  ? 13.476 1.066   23.459  0.72 37.03 ?  29  LYS   A NZ   1 
ATOM   825  N  NZ   B LYS   A 1 29  ? 13.425 1.372   23.352  0.28 34.70 ?  29  LYS   A NZ   1 
ATOM   826  H  H    A LYS   A 1 29  ? 17.445 1.425   17.525  0.72 28.55 ?  29  LYS   A H    1 
ATOM   827  H  H    B LYS   A 1 29  ? 17.475 1.309   17.474  0.28 31.57 ?  29  LYS   A H    1 
ATOM   828  H  HA   A LYS   A 1 29  ? 17.210 1.466   20.174  0.72 30.93 ?  29  LYS   A HA   1 
ATOM   829  H  HA   B LYS   A 1 29  ? 17.159 1.456   20.129  0.28 32.83 ?  29  LYS   A HA   1 
ATOM   830  H  HB2  A LYS   A 1 29  ? 15.300 1.259   18.837  0.72 34.22 ?  29  LYS   A HB2  1 
ATOM   831  H  HB2  B LYS   A 1 29  ? 15.281 1.238   18.718  0.28 35.23 ?  29  LYS   A HB2  1 
ATOM   832  H  HB3  A LYS   A 1 29  ? 15.818 -0.148  18.321  0.72 34.22 ?  29  LYS   A HB3  1 
ATOM   833  H  HB3  B LYS   A 1 29  ? 15.781 -0.212  18.316  0.28 35.23 ?  29  LYS   A HB3  1 
ATOM   834  H  HG2  A LYS   A 1 29  ? 14.223 -0.584  19.875  0.72 37.73 ?  29  LYS   A HG2  1 
ATOM   835  H  HG2  B LYS   A 1 29  ? 14.123 -0.495  19.844  0.28 37.51 ?  29  LYS   A HG2  1 
ATOM   836  H  HG3  A LYS   A 1 29  ? 15.606 -0.942  20.573  0.72 37.73 ?  29  LYS   A HG3  1 
ATOM   837  H  HG3  B LYS   A 1 29  ? 15.478 -0.852  20.598  0.28 37.51 ?  29  LYS   A HG3  1 
ATOM   838  H  HD2  A LYS   A 1 29  ? 15.567 1.040   21.749  0.72 40.98 ?  29  LYS   A HD2  1 
ATOM   839  H  HD2  B LYS   A 1 29  ? 15.478 1.206   21.642  0.28 39.49 ?  29  LYS   A HD2  1 
ATOM   840  H  HD3  A LYS   A 1 29  ? 14.258 1.506   20.972  0.72 40.98 ?  29  LYS   A HD3  1 
ATOM   841  H  HD3  B LYS   A 1 29  ? 14.194 1.653   20.814  0.28 39.49 ?  29  LYS   A HD3  1 
ATOM   842  H  HE2  A LYS   A 1 29  ? 13.070 -0.255  21.992  0.72 43.21 ?  29  LYS   A HE2  1 
ATOM   843  H  HE2  B LYS   A 1 29  ? 12.925 0.037   21.928  0.28 40.87 ?  29  LYS   A HE2  1 
ATOM   844  H  HE3  A LYS   A 1 29  ? 14.375 -0.622  22.824  0.72 43.21 ?  29  LYS   A HE3  1 
ATOM   845  H  HE3  B LYS   A 1 29  ? 14.210 -0.389  22.765  0.28 40.87 ?  29  LYS   A HE3  1 
ATOM   846  H  HZ1  A LYS   A 1 29  ? 12.972 0.659   24.070  0.72 44.49 ?  29  LYS   A HZ1  1 
ATOM   847  H  HZ1  B LYS   A 1 29  ? 12.900 1.018   23.978  0.28 41.68 ?  29  LYS   A HZ1  1 
ATOM   848  H  HZ2  A LYS   A 1 29  ? 14.200 1.398   23.856  0.72 44.49 ?  29  LYS   A HZ2  1 
ATOM   849  H  HZ2  B LYS   A 1 29  ? 14.171 1.670   23.735  0.28 41.68 ?  29  LYS   A HZ2  1 
ATOM   850  H  HZ3  A LYS   A 1 29  ? 13.011 1.733   23.098  0.72 44.49 ?  29  LYS   A HZ3  1 
ATOM   851  H  HZ3  B LYS   A 1 29  ? 13.001 2.057   22.973  0.28 41.68 ?  29  LYS   A HZ3  1 
ATOM   852  N  N    . VAL   A 1 30  ? 18.398 -1.198  18.820  1.00 24.76 ?  30  VAL   A N    1 
ATOM   853  C  CA   . VAL   A 1 30  ? 19.055 -2.464  19.123  1.00 23.37 ?  30  VAL   A CA   1 
ATOM   854  C  C    . VAL   A 1 30  ? 20.556 -2.304  19.347  1.00 22.13 ?  30  VAL   A C    1 
ATOM   855  O  O    . VAL   A 1 30  ? 21.143 -3.032  20.154  1.00 22.69 ?  30  VAL   A O    1 
ATOM   856  C  CB   . VAL   A 1 30  ? 18.766 -3.460  17.984  1.00 23.92 ?  30  VAL   A CB   1 
ATOM   857  C  CG1  . VAL   A 1 30  ? 19.527 -4.763  18.195  1.00 24.50 ?  30  VAL   A CG1  1 
ATOM   858  C  CG2  . VAL   A 1 30  ? 17.269 -3.725  17.873  1.00 24.40 ?  30  VAL   A CG2  1 
ATOM   859  H  H    A VAL   A 1 30  ? 18.265 -1.057  17.982  0.72 29.76 ?  30  VAL   A H    1 
ATOM   860  H  H    B VAL   A 1 30  ? 18.308 -1.040  17.980  0.28 29.76 ?  30  VAL   A H    1 
ATOM   861  H  HA   . VAL   A 1 30  ? 18.664 -2.830  19.931  1.00 28.10 ?  30  VAL   A HA   1 
ATOM   862  H  HB   . VAL   A 1 30  ? 19.061 -3.079  17.143  1.00 28.75 ?  30  VAL   A HB   1 
ATOM   863  H  HG11 . VAL   A 1 30  ? 19.160 -5.441  17.603  1.00 29.44 ?  30  VAL   A HG11 1 
ATOM   864  H  HG12 . VAL   A 1 30  ? 20.463 -4.619  17.991  1.00 29.44 ?  30  VAL   A HG12 1 
ATOM   865  H  HG13 . VAL   A 1 30  ? 19.423 -5.041  19.118  1.00 29.44 ?  30  VAL   A HG13 1 
ATOM   866  H  HG21 . VAL   A 1 30  ? 17.114 -4.394  17.187  1.00 29.32 ?  30  VAL   A HG21 1 
ATOM   867  H  HG22 . VAL   A 1 30  ? 16.941 -4.047  18.728  1.00 29.32 ?  30  VAL   A HG22 1 
ATOM   868  H  HG23 . VAL   A 1 30  ? 16.819 -2.900  17.636  1.00 29.32 ?  30  VAL   A HG23 1 
ATOM   869  N  N    . LYS   A 1 31  ? 21.192 -1.370  18.649  1.00 21.43 ?  31  LYS   A N    1 
ATOM   870  C  CA   . LYS   A 1 31  ? 22.645 -1.260  18.606  1.00 22.54 ?  31  LYS   A CA   1 
ATOM   871  C  C    . LYS   A 1 31  ? 23.271 -2.621  18.281  1.00 19.92 ?  31  LYS   A C    1 
ATOM   872  O  O    . LYS   A 1 31  ? 24.051 -3.160  19.072  1.00 21.15 ?  31  LYS   A O    1 
ATOM   873  C  CB   . LYS   A 1 31  ? 23.215 -0.686  19.894  1.00 28.15 ?  31  LYS   A CB   1 
ATOM   874  C  CG   . LYS   A 1 31  ? 22.519 0.583   20.359  1.00 34.49 ?  31  LYS   A CG   1 
ATOM   875  C  CD   . LYS   A 1 31  ? 23.520 1.642   20.796  1.00 39.62 ?  31  LYS   A CD   1 
ATOM   876  C  CE   . LYS   A 1 31  ? 22.872 2.677   21.704  1.00 43.10 ?  31  LYS   A CE   1 
ATOM   877  N  NZ   . LYS   A 1 31  ? 21.690 3.335   21.083  1.00 44.74 ?  31  LYS   A NZ   1 
ATOM   878  H  H    . LYS   A 1 31  ? 20.787 -0.777  18.172  1.00 25.76 ?  31  LYS   A H    1 
ATOM   879  H  HA   . LYS   A 1 31  ? 22.876 -0.652  17.892  1.00 27.10 ?  31  LYS   A HA   1 
ATOM   880  H  HB2  . LYS   A 1 31  ? 23.131 -1.348  20.591  1.00 33.83 ?  31  LYS   A HB2  1 
ATOM   881  H  HB3  . LYS   A 1 31  ? 24.151 -0.475  19.749  1.00 33.83 ?  31  LYS   A HB3  1 
ATOM   882  H  HG2  . LYS   A 1 31  ? 21.993 0.946   19.629  1.00 41.43 ?  31  LYS   A HG2  1 
ATOM   883  H  HG3  . LYS   A 1 31  ? 21.947 0.375   21.114  1.00 41.43 ?  31  LYS   A HG3  1 
ATOM   884  H  HD2  . LYS   A 1 31  ? 24.243 1.218   21.284  1.00 47.59 ?  31  LYS   A HD2  1 
ATOM   885  H  HD3  . LYS   A 1 31  ? 23.865 2.099   20.012  1.00 47.59 ?  31  LYS   A HD3  1 
ATOM   886  H  HE2  . LYS   A 1 31  ? 22.574 2.238   22.514  1.00 51.76 ?  31  LYS   A HE2  1 
ATOM   887  H  HE3  . LYS   A 1 31  ? 23.524 3.363   21.919  1.00 51.76 ?  31  LYS   A HE3  1 
ATOM   888  H  HZ1  . LYS   A 1 31  ? 21.352 3.940   21.642  1.00 53.73 ?  31  LYS   A HZ1  1 
ATOM   889  H  HZ2  . LYS   A 1 31  ? 21.929 3.740   20.328  1.00 53.73 ?  31  LYS   A HZ2  1 
ATOM   890  H  HZ3  . LYS   A 1 31  ? 21.065 2.728   20.901  1.00 53.73 ?  31  LYS   A HZ3  1 
ATOM   891  N  N    . PRO   A 1 32  ? 22.955 -3.185  17.120  1.00 17.54 ?  32  PRO   A N    1 
ATOM   892  C  CA   . PRO   A 1 32  ? 23.435 -4.528  16.790  1.00 17.77 ?  32  PRO   A CA   1 
ATOM   893  C  C    . PRO   A 1 32  ? 24.937 -4.541  16.578  1.00 17.70 ?  32  PRO   A C    1 
ATOM   894  O  O    . PRO   A 1 32  ? 25.577 -3.510  16.364  1.00 17.35 ?  32  PRO   A O    1 
ATOM   895  C  CB   . PRO   A 1 32  ? 22.708 -4.840  15.479  1.00 17.68 ?  32  PRO   A CB   1 
ATOM   896  C  CG   . PRO   A 1 32  ? 22.536 -3.490  14.842  1.00 16.18 ?  32  PRO   A CG   1 
ATOM   897  C  CD   . PRO   A 1 32  ? 22.236 -2.570  15.993  1.00 16.47 ?  32  PRO   A CD   1 
ATOM   898  H  HA   . PRO   A 1 32  ? 23.188 -5.169  17.474  1.00 21.37 ?  32  PRO   A HA   1 
ATOM   899  H  HB2  . PRO   A 1 32  ? 23.256 -5.424  14.926  1.00 21.26 ?  32  PRO   A HB2  1 
ATOM   900  H  HB3  . PRO   A 1 32  ? 21.849 -5.254  15.668  1.00 21.26 ?  32  PRO   A HB3  1 
ATOM   901  H  HG2  . PRO   A 1 32  ? 23.354 -3.240  14.391  1.00 19.46 ?  32  PRO   A HG2  1 
ATOM   902  H  HG3  . PRO   A 1 32  ? 21.792 -3.525  14.216  1.00 19.46 ?  32  PRO   A HG3  1 
ATOM   903  H  HD2  . PRO   A 1 32  ? 22.587 -1.687  15.799  1.00 19.82 ?  32  PRO   A HD2  1 
ATOM   904  H  HD3  . PRO   A 1 32  ? 21.284 -2.550  16.160  1.00 19.82 ?  32  PRO   A HD3  1 
ATOM   905  N  N    . THR   A 1 33  ? 25.495 -5.748  16.620  1.00 17.55 ?  33  THR   A N    1 
ATOM   906  C  CA   . THR   A 1 33  ? 26.907 -5.911  16.301  1.00 17.50 ?  33  THR   A CA   1 
ATOM   907  C  C    . THR   A 1 33  ? 27.203 -5.456  14.876  1.00 15.98 ?  33  THR   A C    1 
ATOM   908  O  O    . THR   A 1 33  ? 28.236 -4.817  14.624  1.00 16.26 ?  33  THR   A O    1 
ATOM   909  C  CB   . THR   A 1 33  ? 27.313 -7.369  16.506  1.00 19.34 ?  33  THR   A CB   1 
ATOM   910  O  OG1  . THR   A 1 33  ? 27.009 -7.758  17.848  1.00 20.81 ?  33  THR   A OG1  1 
ATOM   911  C  CG2  . THR   A 1 33  ? 28.801 -7.555  16.252  1.00 20.46 ?  33  THR   A CG2  1 
ATOM   912  H  H    . THR   A 1 33  ? 25.083 -6.475  16.818  1.00 21.10 ?  33  THR   A H    1 
ATOM   913  H  HA   . THR   A 1 33  ? 27.434 -5.368  16.908  1.00 21.05 ?  33  THR   A HA   1 
ATOM   914  H  HB   . THR   A 1 33  ? 26.822 -7.936  15.887  1.00 23.25 ?  33  THR   A HB   1 
ATOM   915  H  HG1  . THR   A 1 33  ? 27.441 -7.281  18.391  1.00 25.02 ?  33  THR   A HG1  1 
ATOM   916  H  HG21 . THR   A 1 33  ? 29.078 -8.440  16.539  1.00 24.60 ?  33  THR   A HG21 1 
ATOM   917  H  HG22 . THR   A 1 33  ? 28.994 -7.459  15.307  1.00 24.60 ?  33  THR   A HG22 1 
ATOM   918  H  HG23 . THR   A 1 33  ? 29.305 -6.892  16.748  1.00 24.60 ?  33  THR   A HG23 1 
ATOM   919  N  N    . VAL   A 1 34  ? 26.307 -5.767  13.937  1.00 14.53 ?  34  VAL   A N    1 
ATOM   920  C  CA   . VAL   A 1 34  ? 26.498 -5.446  12.526  1.00 13.27 ?  34  VAL   A CA   1 
ATOM   921  C  C    . VAL   A 1 34  ? 25.200 -4.892  11.957  1.00 12.53 ?  34  VAL   A C    1 
ATOM   922  O  O    . VAL   A 1 34  ? 24.162 -5.565  11.998  1.00 13.51 ?  34  VAL   A O    1 
ATOM   923  C  CB   . VAL   A 1 34  ? 26.943 -6.663  11.696  1.00 14.02 ?  34  VAL   A CB   1 
ATOM   924  C  CG1  . VAL   A 1 34  ? 27.130 -6.270  10.235  1.00 13.99 ?  34  VAL   A CG1  1 
ATOM   925  C  CG2  . VAL   A 1 34  ? 28.221 -7.275  12.266  1.00 15.23 ?  34  VAL   A CG2  1 
ATOM   926  H  H    . VAL   A 1 34  ? 25.565 -6.175  14.099  1.00 17.49 ?  34  VAL   A H    1 
ATOM   927  H  HA   . VAL   A 1 34  ? 27.180 -4.757  12.445  1.00 15.97 ?  34  VAL   A HA   1 
ATOM   928  H  HB   . VAL   A 1 34  ? 26.248 -7.338  11.740  1.00 16.87 ?  34  VAL   A HB   1 
ATOM   929  H  HG11 . VAL   A 1 34  ? 27.621 -6.974  9.785   1.00 16.83 ?  34  VAL   A HG11 1 
ATOM   930  H  HG12 . VAL   A 1 34  ? 26.261 -6.156  9.824   1.00 16.83 ?  34  VAL   A HG12 1 
ATOM   931  H  HG13 . VAL   A 1 34  ? 27.632 -5.440  10.196  1.00 16.83 ?  34  VAL   A HG13 1 
ATOM   932  H  HG21 . VAL   A 1 34  ? 28.497 -8.012  11.700  1.00 18.32 ?  34  VAL   A HG21 1 
ATOM   933  H  HG22 . VAL   A 1 34  ? 28.915 -6.596  12.286  1.00 18.32 ?  34  VAL   A HG22 1 
ATOM   934  H  HG23 . VAL   A 1 34  ? 28.048 -7.596  13.166  1.00 18.32 ?  34  VAL   A HG23 1 
ATOM   935  N  N    . VAL   A 1 35  ? 25.259 -3.680  11.404  1.00 11.78 ?  35  VAL   A N    1 
ATOM   936  C  CA   . VAL   A 1 35  ? 24.223 -3.173  10.513  1.00 11.39 ?  35  VAL   A CA   1 
ATOM   937  C  C    . VAL   A 1 35  ? 24.777 -3.182  9.095   1.00 10.67 ?  35  VAL   A C    1 
ATOM   938  O  O    . VAL   A 1 35  ? 25.923 -2.774  8.863   1.00 11.55 ?  35  VAL   A O    1 
ATOM   939  C  CB   . VAL   A 1 35  ? 23.694 -1.778  10.918  1.00 11.80 ?  35  VAL   A CB   1 
ATOM   940  C  CG1  . VAL   A 1 35  ? 24.768 -0.692  10.787  1.00 12.97 ?  35  VAL   A CG1  1 
ATOM   941  C  CG2  . VAL   A 1 35  ? 22.465 -1.425  10.084  1.00 12.90 ?  35  VAL   A CG2  1 
ATOM   942  H  H    . VAL   A 1 35  ? 25.901 -3.120  11.528  1.00 14.18 ?  35  VAL   A H    1 
ATOM   943  H  HA   . VAL   A 1 35  ? 23.468 -3.782  10.536  1.00 13.72 ?  35  VAL   A HA   1 
ATOM   944  H  HB   . VAL   A 1 35  ? 23.413 -1.804  11.842  1.00 14.21 ?  35  VAL   A HB   1 
ATOM   945  H  HG11 . VAL   A 1 35  ? 24.426 0.140   11.153  1.00 15.61 ?  35  VAL   A HG11 1 
ATOM   946  H  HG12 . VAL   A 1 35  ? 25.556 -0.970  11.277  1.00 15.61 ?  35  VAL   A HG12 1 
ATOM   947  H  HG13 . VAL   A 1 35  ? 24.988 -0.570  9.848   1.00 15.61 ?  35  VAL   A HG13 1 
ATOM   948  H  HG21 . VAL   A 1 35  ? 22.101 -0.584  10.392  1.00 15.53 ?  35  VAL   A HG21 1 
ATOM   949  H  HG22 . VAL   A 1 35  ? 22.728 -1.347  9.149   1.00 15.53 ?  35  VAL   A HG22 1 
ATOM   950  H  HG23 . VAL   A 1 35  ? 21.806 -2.130  10.179  1.00 15.53 ?  35  VAL   A HG23 1 
ATOM   951  N  N    . VAL   A 1 36  ? 23.963 -3.640  8.145   1.00 10.22 ?  36  VAL   A N    1 
ATOM   952  C  CA   . VAL   A 1 36  ? 24.341 -3.654  6.739   1.00 10.17 ?  36  VAL   A CA   1 
ATOM   953  C  C    . VAL   A 1 36  ? 23.877 -2.366  6.075   1.00 10.27 ?  36  VAL   A C    1 
ATOM   954  O  O    . VAL   A 1 36  ? 22.716 -1.961  6.220   1.00 10.96 ?  36  VAL   A O    1 
ATOM   955  C  CB   . VAL   A 1 36  ? 23.744 -4.872  6.019   1.00 10.32 ?  36  VAL   A CB   1 
ATOM   956  C  CG1  . VAL   A 1 36  ? 24.012 -4.799  4.538   1.00 10.71 ?  36  VAL   A CG1  1 
ATOM   957  C  CG2  . VAL   A 1 36  ? 24.289 -6.158  6.604   1.00 11.23 ?  36  VAL   A CG2  1 
ATOM   958  H  H    . VAL   A 1 36  ? 23.170 -3.962  8.294   1.00 12.32 ?  36  VAL   A H    1 
ATOM   959  H  HA   . VAL   A 1 36  ? 25.310 -3.709  6.672   1.00 12.26 ?  36  VAL   A HA   1 
ATOM   960  H  HB   . VAL   A 1 36  ? 22.784 -4.866  6.144   1.00 12.43 ?  36  VAL   A HB   1 
ATOM   961  H  HG11 . VAL   A 1 36  ? 23.880 -5.676  4.148   1.00 12.90 ?  36  VAL   A HG11 1 
ATOM   962  H  HG12 . VAL   A 1 36  ? 23.402 -4.163  4.130   1.00 12.90 ?  36  VAL   A HG12 1 
ATOM   963  H  HG13 . VAL   A 1 36  ? 24.930 -4.512  4.395   1.00 12.90 ?  36  VAL   A HG13 1 
ATOM   964  H  HG21 . VAL   A 1 36  ? 23.902 -6.913  6.124   1.00 13.52 ?  36  VAL   A HG21 1 
ATOM   965  H  HG22 . VAL   A 1 36  ? 25.252 -6.170  6.513   1.00 13.52 ?  36  VAL   A HG22 1 
ATOM   966  H  HG23 . VAL   A 1 36  ? 24.042 -6.212  7.542   1.00 13.52 ?  36  VAL   A HG23 1 
ATOM   967  N  N    . ASN   A 1 37  ? 24.789 -1.728  5.337   1.00 9.68  ?  37  ASN   A N    1 
ATOM   968  C  CA   . ASN   A 1 37  ? 24.458 -0.607  4.471   1.00 9.59  ?  37  ASN   A CA   1 
ATOM   969  C  C    . ASN   A 1 37  ? 24.323 -1.082  3.036   1.00 9.61  ?  37  ASN   A C    1 
ATOM   970  O  O    . ASN   A 1 37  ? 25.110 -1.913  2.566   1.00 10.05 ?  37  ASN   A O    1 
ATOM   971  C  CB   . ASN   A 1 37  ? 25.542 0.466   4.543   1.00 9.79  ?  37  ASN   A CB   1 
ATOM   972  C  CG   . ASN   A 1 37  ? 25.213 1.665   3.694   1.00 10.02 ?  37  ASN   A CG   1 
ATOM   973  O  OD1  . ASN   A 1 37  ? 24.038 1.991   3.511   1.00 10.65 ?  37  ASN   A OD1  1 
ATOM   974  N  ND2  . ASN   A 1 37  ? 26.240 2.323   3.168   1.00 10.47 ?  37  ASN   A ND2  1 
ATOM   975  H  H    . ASN   A 1 37  ? 25.631 -1.927  5.336   1.00 11.66 ?  37  ASN   A H    1 
ATOM   976  H  HA   . ASN   A 1 37  ? 23.620 -0.216  4.756   1.00 11.56 ?  37  ASN   A HA   1 
ATOM   977  H  HB2  . ASN   A 1 37  ? 25.636 0.764   5.465   1.00 11.80 ?  37  ASN   A HB2  1 
ATOM   978  H  HB3  . ASN   A 1 37  ? 26.385 0.092   4.233   1.00 11.80 ?  37  ASN   A HB3  1 
ATOM   979  H  HD21 . ASN   A 1 37  ? 26.099 3.011   2.671   1.00 12.61 ?  37  ASN   A HD21 1 
ATOM   980  H  HD22 . ASN   A 1 37  ? 27.040 2.066   3.318   1.00 12.61 ?  37  ASN   A HD22 1 
ATOM   981  N  N    A ALA   A 1 38  ? 23.300 -0.552  2.360   0.72 9.86  ?  38  ALA   A N    1 
ATOM   982  N  N    B ALA   A 1 38  ? 23.313 -0.565  2.335   0.28 9.99  ?  38  ALA   A N    1 
ATOM   983  C  CA   A ALA   A 1 38  ? 23.104 -0.686  0.918   0.72 9.86  ?  38  ALA   A CA   1 
ATOM   984  C  CA   B ALA   A 1 38  ? 23.150 -0.840  0.906   0.28 10.55 ?  38  ALA   A CA   1 
ATOM   985  C  C    A ALA   A 1 38  ? 24.016 0.314   0.209   0.72 9.82  ?  38  ALA   A C    1 
ATOM   986  C  C    B ALA   A 1 38  ? 23.973 0.183   0.125   0.28 10.39 ?  38  ALA   A C    1 
ATOM   987  O  O    A ALA   A 1 38  ? 23.610 1.414   -0.176  0.72 9.77  ?  38  ALA   A O    1 
ATOM   988  O  O    B ALA   A 1 38  ? 23.464 1.156   -0.439  0.28 10.14 ?  38  ALA   A O    1 
ATOM   989  C  CB   A ALA   A 1 38  ? 21.640 -0.447  0.566   0.72 11.09 ?  38  ALA   A CB   1 
ATOM   990  C  CB   B ALA   A 1 38  ? 21.678 -0.819  0.518   0.28 11.09 ?  38  ALA   A CB   1 
ATOM   991  H  H    A ALA   A 1 38  ? 22.692 -0.075  2.737   0.72 11.88 ?  38  ALA   A H    1 
ATOM   992  H  H    B ALA   A 1 38  ? 22.707 -0.051  2.668   0.28 12.04 ?  38  ALA   A H    1 
ATOM   993  H  HA   A ALA   A 1 38  ? 23.349 -1.577  0.637   0.72 11.88 ?  38  ALA   A HA   1 
ATOM   994  H  HA   B ALA   A 1 38  ? 23.501 -1.726  0.714   0.28 12.70 ?  38  ALA   A HA   1 
ATOM   995  H  HB1  A ALA   A 1 38  ? 21.522 -0.543  -0.391  0.72 13.35 ?  38  ALA   A HB1  1 
ATOM   996  H  HB1  B ALA   A 1 38  ? 21.608 -0.948  -0.440  0.28 13.36 ?  38  ALA   A HB1  1 
ATOM   997  H  HB2  A ALA   A 1 38  ? 21.093 -1.103  1.033   0.72 13.35 ?  38  ALA   A HB2  1 
ATOM   998  H  HB2  B ALA   A 1 38  ? 21.215 -1.536  0.983   0.28 13.36 ?  38  ALA   A HB2  1 
ATOM   999  H  HB3  A ALA   A 1 38  ? 21.385 0.447   0.845   0.72 13.35 ?  38  ALA   A HB3  1 
ATOM   1000 H  HB3  B ALA   A 1 38  ? 21.299 0.036   0.764   0.28 13.36 ?  38  ALA   A HB3  1 
ATOM   1001 N  N    A ALA   A 1 39  ? 25.273 -0.084  0.038   0.72 10.08 ?  39  ALA   A N    1 
ATOM   1002 N  N    B ALA   A 1 39  ? 25.278 -0.055  0.094   0.28 10.69 ?  39  ALA   A N    1 
ATOM   1003 C  CA   A ALA   A 1 39  ? 26.331 0.794   -0.433  0.72 9.62  ?  39  ALA   A CA   1 
ATOM   1004 C  CA   B ALA   A 1 39  ? 26.227 0.907   -0.439  0.28 10.73 ?  39  ALA   A CA   1 
ATOM   1005 C  C    A ALA   A 1 39  ? 26.451 0.767   -1.954  0.72 9.82  ?  39  ALA   A C    1 
ATOM   1006 C  C    B ALA   A 1 39  ? 26.387 0.745   -1.946  0.28 10.19 ?  39  ALA   A C    1 
ATOM   1007 O  O    A ALA   A 1 39  ? 25.943 -0.129  -2.635  0.72 10.27 ?  39  ALA   A O    1 
ATOM   1008 O  O    B ALA   A 1 39  ? 26.043 -0.285  -2.530  0.28 10.40 ?  39  ALA   A O    1 
ATOM   1009 C  CB   A ALA   A 1 39  ? 27.656 0.375   0.209   0.72 10.31 ?  39  ALA   A CB   1 
ATOM   1010 C  CB   B ALA   A 1 39  ? 27.583 0.720   0.237   0.28 11.40 ?  39  ALA   A CB   1 
ATOM   1011 H  H    A ALA   A 1 39  ? 25.539 -0.888  0.197   0.72 12.14 ?  39  ALA   A H    1 
ATOM   1012 H  H    B ALA   A 1 39  ? 25.641 -0.785  0.376   0.28 12.88 ?  39  ALA   A H    1 
ATOM   1013 H  HA   A ALA   A 1 39  ? 26.131 1.704   -0.161  0.72 11.60 ?  39  ALA   A HA   1 
ATOM   1014 H  HA   B ALA   A 1 39  ? 25.907 1.804   -0.252  0.28 12.93 ?  39  ALA   A HA   1 
ATOM   1015 H  HB1  A ALA   A 1 39  ? 28.355 0.967   -0.105  0.72 12.41 ?  39  ALA   A HB1  1 
ATOM   1016 H  HB1  B ALA   A 1 39  ? 28.201 1.370   -0.125  0.28 13.73 ?  39  ALA   A HB1  1 
ATOM   1017 H  HB2  A ALA   A 1 39  ? 27.572 0.448   1.176   0.72 12.41 ?  39  ALA   A HB2  1 
ATOM   1018 H  HB2  B ALA   A 1 39  ? 27.478 0.855   1.192   0.28 13.73 ?  39  ALA   A HB2  1 
ATOM   1019 H  HB3  A ALA   A 1 39  ? 27.851 -0.538  -0.038  0.72 12.41 ?  39  ALA   A HB3  1 
ATOM   1020 H  HB3  B ALA   A 1 39  ? 27.899 -0.179  0.061   0.28 13.73 ?  39  ALA   A HB3  1 
ATOM   1021 N  N    A ASN   A 1 40  ? 27.165 1.761   -2.483  0.72 10.05 ?  40  ASN   A N    1 
ATOM   1022 N  N    B ASN   A 1 40  ? 26.926 1.787   -2.573  0.28 10.05 ?  40  ASN   A N    1 
ATOM   1023 C  CA   A ASN   A 1 40  ? 27.708 1.713   -3.835  0.72 10.16 ?  40  ASN   A CA   1 
ATOM   1024 C  CA   B ASN   A 1 40  ? 27.400 1.722   -3.947  0.28 10.16 ?  40  ASN   A CA   1 
ATOM   1025 C  C    A ASN   A 1 40  ? 29.232 1.604   -3.768  0.72 9.27  ?  40  ASN   A C    1 
ATOM   1026 C  C    B ASN   A 1 40  ? 28.925 1.611   -3.950  0.28 9.98  ?  40  ASN   A C    1 
ATOM   1027 O  O    A ASN   A 1 40  ? 29.832 1.708   -2.695  0.72 9.77  ?  40  ASN   A O    1 
ATOM   1028 O  O    B ASN   A 1 40  ? 29.579 1.698   -2.910  0.28 10.18 ?  40  ASN   A O    1 
ATOM   1029 C  CB   A ASN   A 1 40  ? 27.228 2.893   -4.700  0.72 11.06 ?  40  ASN   A CB   1 
ATOM   1030 C  CB   B ASN   A 1 40  ? 26.926 2.943   -4.744  0.28 11.03 ?  40  ASN   A CB   1 
ATOM   1031 C  CG   A ASN   A 1 40  ? 27.592 4.250   -4.127  0.72 11.90 ?  40  ASN   A CG   1 
ATOM   1032 C  CG   B ASN   A 1 40  ? 27.347 4.251   -4.112  0.28 11.56 ?  40  ASN   A CG   1 
ATOM   1033 O  OD1  A ASN   A 1 40  ? 28.752 4.503   -3.782  0.72 12.48 ?  40  ASN   A OD1  1 
ATOM   1034 O  OD1  B ASN   A 1 40  ? 28.534 4.583   -4.072  0.28 11.96 ?  40  ASN   A OD1  1 
ATOM   1035 N  ND2  A ASN   A 1 40  ? 26.594 5.137   -4.029  0.72 12.61 ?  40  ASN   A ND2  1 
ATOM   1036 N  ND2  B ASN   A 1 40  ? 26.374 5.005   -3.613  0.28 11.91 ?  40  ASN   A ND2  1 
ATOM   1037 H  H    A ASN   A 1 40  ? 27.357 2.483   -2.067  0.72 12.11 ?  40  ASN   A H    1 
ATOM   1038 H  H    B ASN   A 1 40  ? 27.035 2.559   -2.210  0.28 12.10 ?  40  ASN   A H    1 
ATOM   1039 H  HA   A ASN   A 1 40  ? 27.393 0.899   -4.260  0.72 12.24 ?  40  ASN   A HA   1 
ATOM   1040 H  HA   B ASN   A 1 40  ? 27.034 0.925   -4.371  0.28 12.24 ?  40  ASN   A HA   1 
ATOM   1041 H  HB2  A ASN   A 1 40  ? 27.624 2.814   -5.583  0.72 13.32 ?  40  ASN   A HB2  1 
ATOM   1042 H  HB2  B ASN   A 1 40  ? 27.301 2.903   -5.636  0.28 13.28 ?  40  ASN   A HB2  1 
ATOM   1043 H  HB3  A ASN   A 1 40  ? 26.260 2.844   -4.773  0.72 13.32 ?  40  ASN   A HB3  1 
ATOM   1044 H  HB3  B ASN   A 1 40  ? 25.953 2.929   -4.793  0.28 13.28 ?  40  ASN   A HB3  1 
ATOM   1045 H  HD21 A ASN   A 1 40  ? 26.746 5.924   -3.716  0.72 15.18 ?  40  ASN   A HD21 1 
ATOM   1046 H  HD21 B ASN   A 1 40  ? 26.562 5.755   -3.241  0.28 14.34 ?  40  ASN   A HD21 1 
ATOM   1047 H  HD22 A ASN   A 1 40  ? 25.797 4.919   -4.271  0.72 15.18 ?  40  ASN   A HD22 1 
ATOM   1048 H  HD22 B ASN   A 1 40  ? 25.555 4.743   -3.665  0.28 14.34 ?  40  ASN   A HD22 1 
ATOM   1049 N  N    A VAL   A 1 41  ? 29.854 1.347   -4.923  0.72 9.78  ?  41  VAL   A N    1 
ATOM   1050 N  N    B VAL   A 1 41  ? 29.494 1.410   -5.141  0.28 10.18 ?  41  VAL   A N    1 
ATOM   1051 C  CA   A VAL   A 1 41  ? 31.282 1.037   -4.942  0.72 10.48 ?  41  VAL   A CA   1 
ATOM   1052 C  CA   B VAL   A 1 41  ? 30.919 1.095   -5.229  0.28 10.41 ?  41  VAL   A CA   1 
ATOM   1053 C  C    A VAL   A 1 41  ? 32.135 2.197   -4.466  0.72 10.46 ?  41  VAL   A C    1 
ATOM   1054 C  C    B VAL   A 1 41  ? 31.801 2.228   -4.727  0.28 10.58 ?  41  VAL   A C    1 
ATOM   1055 O  O    A VAL   A 1 41  ? 33.275 1.986   -4.035  0.72 10.89 ?  41  VAL   A O    1 
ATOM   1056 O  O    B VAL   A 1 41  ? 32.955 1.990   -4.356  0.28 10.82 ?  41  VAL   A O    1 
ATOM   1057 C  CB   A VAL   A 1 41  ? 31.773 0.546   -6.325  0.72 10.92 ?  41  VAL   A CB   1 
ATOM   1058 C  CB   B VAL   A 1 41  ? 31.329 0.685   -6.660  0.28 10.86 ?  41  VAL   A CB   1 
ATOM   1059 C  CG1  A VAL   A 1 41  ? 31.091 -0.760  -6.711  0.72 11.47 ?  41  VAL   A CG1  1 
ATOM   1060 C  CG1  B VAL   A 1 41  ? 30.669 -0.626  -7.046  0.28 11.39 ?  41  VAL   A CG1  1 
ATOM   1061 C  CG2  A VAL   A 1 41  ? 31.606 1.612   -7.410  0.72 11.26 ?  41  VAL   A CG2  1 
ATOM   1062 C  CG2  B VAL   A 1 41  ? 30.994 1.789   -7.658  0.28 11.39 ?  41  VAL   A CG2  1 
ATOM   1063 H  H    A VAL   A 1 41  ? 29.482 1.335   -5.695  0.72 11.78 ?  41  VAL   A H    1 
ATOM   1064 H  H    B VAL   A 1 41  ? 29.082 1.454   -5.895  0.28 12.26 ?  41  VAL   A H    1 
ATOM   1065 H  HA   A VAL   A 1 41  ? 31.445 0.312   -4.321  0.72 12.62 ?  41  VAL   A HA   1 
ATOM   1066 H  HA   B VAL   A 1 41  ? 31.083 0.327   -4.658  0.28 12.54 ?  41  VAL   A HA   1 
ATOM   1067 H  HB   A VAL   A 1 41  ? 32.722 0.355   -6.262  0.72 13.15 ?  41  VAL   A HB   1 
ATOM   1068 H  HB   B VAL   A 1 41  ? 32.287 0.546   -6.678  0.28 13.08 ?  41  VAL   A HB   1 
ATOM   1069 H  HG11 A VAL   A 1 41  ? 31.430 -1.059  -7.569  0.72 13.81 ?  41  VAL   A HG11 1 
ATOM   1070 H  HG11 B VAL   A 1 41  ? 30.850 -0.805  -7.980  0.28 13.72 ?  41  VAL   A HG11 1 
ATOM   1071 H  HG12 A VAL   A 1 41  ? 31.277 -1.429  -6.032  0.72 13.81 ?  41  VAL   A HG12 1 
ATOM   1072 H  HG12 B VAL   A 1 41  ? 31.037 -1.338  -6.496  0.28 13.72 ?  41  VAL   A HG12 1 
ATOM   1073 H  HG13 A VAL   A 1 41  ? 30.132 -0.612  -6.769  0.72 13.81 ?  41  VAL   A HG13 1 
ATOM   1074 H  HG13 B VAL   A 1 41  ? 29.715 -0.559  -6.900  0.28 13.72 ?  41  VAL   A HG13 1 
ATOM   1075 H  HG21 A VAL   A 1 41  ? 31.848 1.226   -8.270  0.72 13.56 ?  41  VAL   A HG21 1 
ATOM   1076 H  HG21 B VAL   A 1 41  ? 31.306 1.521   -8.536  0.28 13.71 ?  41  VAL   A HG21 1 
ATOM   1077 H  HG22 A VAL   A 1 41  ? 30.686 1.906   -7.427  0.72 13.56 ?  41  VAL   A HG22 1 
ATOM   1078 H  HG22 B VAL   A 1 41  ? 30.033 1.921   -7.676  0.28 13.71 ?  41  VAL   A HG22 1 
ATOM   1079 H  HG23 A VAL   A 1 41  ? 32.194 2.358   -7.211  0.72 13.56 ?  41  VAL   A HG23 1 
ATOM   1080 H  HG23 B VAL   A 1 41  ? 31.436 2.607   -7.384  0.28 13.71 ?  41  VAL   A HG23 1 
ATOM   1081 N  N    A TYR   A 1 42  ? 31.628 3.427   -4.561  0.72 10.49 ?  42  TYR   A N    1 
ATOM   1082 N  N    B TYR   A 1 42  ? 31.298 3.462   -4.726  0.28 10.89 ?  42  TYR   A N    1 
ATOM   1083 C  CA   A TYR   A 1 42  ? 32.363 4.615   -4.144  0.72 10.75 ?  42  TYR   A CA   1 
ATOM   1084 C  CA   B TYR   A 1 42  ? 32.079 4.619   -4.303  0.28 10.96 ?  42  TYR   A CA   1 
ATOM   1085 C  C    A TYR   A 1 42  ? 32.094 4.992   -2.697  0.72 10.62 ?  42  TYR   A C    1 
ATOM   1086 C  C    B TYR   A 1 42  ? 31.859 4.997   -2.845  0.28 10.92 ?  42  TYR   A C    1 
ATOM   1087 O  O    A TYR   A 1 42  ? 32.656 5.983   -2.209  0.72 11.30 ?  42  TYR   A O    1 
ATOM   1088 O  O    B TYR   A 1 42  ? 32.446 5.981   -2.380  0.28 11.30 ?  42  TYR   A O    1 
ATOM   1089 C  CB   A TYR   A 1 42  ? 32.018 5.802   -5.064  0.72 11.59 ?  42  TYR   A CB   1 
ATOM   1090 C  CB   B TYR   A 1 42  ? 31.762 5.825   -5.192  0.28 11.30 ?  42  TYR   A CB   1 
ATOM   1091 C  CG   A TYR   A 1 42  ? 32.214 5.482   -6.531  0.72 12.02 ?  42  TYR   A CG   1 
ATOM   1092 C  CG   B TYR   A 1 42  ? 31.923 5.539   -6.663  0.28 11.60 ?  42  TYR   A CG   1 
ATOM   1093 C  CD1  A TYR   A 1 42  ? 33.482 5.294   -7.053  0.72 12.98 ?  42  TYR   A CD1  1 
ATOM   1094 C  CD1  B TYR   A 1 42  ? 33.177 5.321   -7.214  0.28 11.59 ?  42  TYR   A CD1  1 
ATOM   1095 C  CD2  A TYR   A 1 42  ? 31.131 5.333   -7.387  0.72 13.46 ?  42  TYR   A CD2  1 
ATOM   1096 C  CD2  B TYR   A 1 42  ? 30.820 5.483   -7.501  0.28 12.55 ?  42  TYR   A CD2  1 
ATOM   1097 C  CE1  A TYR   A 1 42  ? 33.671 4.976   -8.387  0.72 13.42 ?  42  TYR   A CE1  1 
ATOM   1098 C  CE1  B TYR   A 1 42  ? 33.328 5.051   -8.560  0.28 11.98 ?  42  TYR   A CE1  1 
ATOM   1099 C  CE2  A TYR   A 1 42  ? 31.312 5.025   -8.727  0.72 14.41 ?  42  TYR   A CE2  1 
ATOM   1100 C  CE2  B TYR   A 1 42  ? 30.960 5.221   -8.846  0.28 12.90 ?  42  TYR   A CE2  1 
ATOM   1101 C  CZ   A TYR   A 1 42  ? 32.586 4.849   -9.221  0.72 14.21 ?  42  TYR   A CZ   1 
ATOM   1102 C  CZ   B TYR   A 1 42  ? 32.214 5.005   -9.373  0.28 12.41 ?  42  TYR   A CZ   1 
ATOM   1103 O  OH   A TYR   A 1 42  ? 32.776 4.532   -10.546 0.72 15.62 ?  42  TYR   A OH   1 
ATOM   1104 O  OH   B TYR   A 1 42  ? 32.350 4.743   -10.714 0.28 12.80 ?  42  TYR   A OH   1 
ATOM   1105 H  H    A TYR   A 1 42  ? 30.846 3.603   -4.873  0.72 12.64 ?  42  TYR   A H    1 
ATOM   1106 H  H    B TYR   A 1 42  ? 30.496 3.657   -4.986  0.28 13.12 ?  42  TYR   A H    1 
ATOM   1107 H  HA   A TYR   A 1 42  ? 33.313 4.450   -4.236  0.72 12.95 ?  42  TYR   A HA   1 
ATOM   1108 H  HA   B TYR   A 1 42  ? 33.017 4.412   -4.416  0.28 13.20 ?  42  TYR   A HA   1 
ATOM   1109 H  HB2  A TYR   A 1 42  ? 31.089 6.050   -4.933  0.72 13.95 ?  42  TYR   A HB2  1 
ATOM   1110 H  HB2  B TYR   A 1 42  ? 30.843 6.098   -5.040  0.28 13.60 ?  42  TYR   A HB2  1 
ATOM   1111 H  HB3  A TYR   A 1 42  ? 32.593 6.557   -4.843  0.72 13.95 ?  42  TYR   A HB3  1 
ATOM   1112 H  HB3  B TYR   A 1 42  ? 32.363 6.551   -4.961  0.28 13.60 ?  42  TYR   A HB3  1 
ATOM   1113 H  HD1  A TYR   A 1 42  ? 34.225 5.381   -6.498  0.72 15.63 ?  42  TYR   A HD1  1 
ATOM   1114 H  HD1  B TYR   A 1 42  ? 33.929 5.351   -6.665  0.28 13.96 ?  42  TYR   A HD1  1 
ATOM   1115 H  HD2  A TYR   A 1 42  ? 30.269 5.457   -7.058  0.72 16.20 ?  42  TYR   A HD2  1 
ATOM   1116 H  HD2  B TYR   A 1 42  ? 29.971 5.628   -7.148  0.28 15.11 ?  42  TYR   A HD2  1 
ATOM   1117 H  HE1  A TYR   A 1 42  ? 34.531 4.863   -8.725  0.72 16.15 ?  42  TYR   A HE1  1 
ATOM   1118 H  HE1  B TYR   A 1 42  ? 34.177 4.906   -8.913  0.28 14.42 ?  42  TYR   A HE1  1 
ATOM   1119 H  HE2  A TYR   A 1 42  ? 30.572 4.937   -9.289  0.72 17.34 ?  42  TYR   A HE2  1 
ATOM   1120 H  HE2  B TYR   A 1 42  ? 30.212 5.185   -9.394  0.28 15.53 ?  42  TYR   A HE2  1 
ATOM   1121 H  HH   A TYR   A 1 42  ? 33.595 4.436   -10.704 0.72 18.80 ?  42  TYR   A HH   1 
ATOM   1122 H  HH   B TYR   A 1 42  ? 31.600 4.743   -11.083 0.28 15.41 ?  42  TYR   A HH   1 
ATOM   1123 N  N    A LEU   A 1 43  ? 31.237 4.230   -2.014  0.72 10.36 ?  43  LEU   A N    1 
ATOM   1124 N  N    B LEU   A 1 43  ? 31.031 4.246   -2.118  0.28 10.51 ?  43  LEU   A N    1 
ATOM   1125 C  CA   A LEU   A 1 43  ? 30.782 4.565   -0.669  0.72 10.27 ?  43  LEU   A CA   1 
ATOM   1126 C  CA   B LEU   A 1 43  ? 30.632 4.594   -0.752  0.28 10.55 ?  43  LEU   A CA   1 
ATOM   1127 C  C    A LEU   A 1 43  ? 30.311 6.017   -0.582  0.72 10.25 ?  43  LEU   A C    1 
ATOM   1128 C  C    B LEU   A 1 43  ? 30.139 6.037   -0.655  0.28 10.44 ?  43  LEU   A C    1 
ATOM   1129 O  O    A LEU   A 1 43  ? 30.593 6.730   0.385   0.72 11.55 ?  43  LEU   A O    1 
ATOM   1130 O  O    B LEU   A 1 43  ? 30.341 6.722   0.350   0.28 10.17 ?  43  LEU   A O    1 
ATOM   1131 C  CB   A LEU   A 1 43  ? 31.829 4.252   0.398   0.72 10.63 ?  43  LEU   A CB   1 
ATOM   1132 C  CB   B LEU   A 1 43  ? 31.732 4.299   0.270   0.28 10.50 ?  43  LEU   A CB   1 
ATOM   1133 C  CG   A LEU   A 1 43  ? 32.346 2.812   0.480   0.72 10.91 ?  43  LEU   A CG   1 
ATOM   1134 C  CG   B LEU   A 1 43  ? 32.160 2.834   0.393   0.28 10.37 ?  43  LEU   A CG   1 
ATOM   1135 C  CD1  A LEU   A 1 43  ? 33.398 2.718   1.572   0.72 11.91 ?  43  LEU   A CD1  1 
ATOM   1136 C  CD1  B LEU   A 1 43  ? 33.186 2.680   1.502   0.28 10.74 ?  43  LEU   A CD1  1 
ATOM   1137 C  CD2  A LEU   A 1 43  ? 31.223 1.820   0.732   0.72 11.43 ?  43  LEU   A CD2  1 
ATOM   1138 C  CD2  B LEU   A 1 43  ? 30.958 1.925   0.634   0.28 10.30 ?  43  LEU   A CD2  1 
ATOM   1139 H  H    A LEU   A 1 43  ? 30.895 3.495   -2.320  0.72 12.48 ?  43  LEU   A H    1 
ATOM   1140 H  H    B LEU   A 1 43  ? 30.680 3.513   -2.397  0.28 12.66 ?  43  LEU   A H    1 
ATOM   1141 H  HA   A LEU   A 1 43  ? 30.013 4.003   -0.474  0.72 12.37 ?  43  LEU   A HA   1 
ATOM   1142 H  HA   B LEU   A 1 43  ? 29.877 4.036   -0.519  0.28 12.71 ?  43  LEU   A HA   1 
ATOM   1143 H  HB2  A LEU   A 1 43  ? 32.596 4.825   0.240   0.72 12.80 ?  43  LEU   A HB2  1 
ATOM   1144 H  HB2  B LEU   A 1 43  ? 32.518 4.813   0.034   0.28 12.65 ?  43  LEU   A HB2  1 
ATOM   1145 H  HB3  A LEU   A 1 43  ? 31.444 4.463   1.261   0.72 12.80 ?  43  LEU   A HB3  1 
ATOM   1146 H  HB3  B LEU   A 1 43  ? 31.414 4.579   1.145   0.28 12.65 ?  43  LEU   A HB3  1 
ATOM   1147 H  HG   A LEU   A 1 43  ? 32.772 2.579   -0.362  0.72 13.15 ?  43  LEU   A HG   1 
ATOM   1148 H  HG   B LEU   A 1 43  ? 32.579 2.561   -0.437  0.28 12.50 ?  43  LEU   A HG   1 
ATOM   1149 H  HD11 A LEU   A 1 43  ? 33.722 1.805   1.619   0.72 14.34 ?  43  LEU   A HD11 1 
ATOM   1150 H  HD11 B LEU   A 1 43  ? 33.449 1.748   1.562   0.28 12.94 ?  43  LEU   A HD11 1 
ATOM   1151 H  HD12 A LEU   A 1 43  ? 34.127 3.320   1.362   0.72 14.34 ?  43  LEU   A HD12 1 
ATOM   1152 H  HD12 B LEU   A 1 43  ? 33.958 3.230   1.297   0.28 12.94 ?  43  LEU   A HD12 1 
ATOM   1153 H  HD13 A LEU   A 1 43  ? 32.992 2.970   2.417   0.72 14.34 ?  43  LEU   A HD13 1 
ATOM   1154 H  HD13 B LEU   A 1 43  ? 32.790 2.966   2.341   0.28 12.94 ?  43  LEU   A HD13 1 
ATOM   1155 H  HD21 A LEU   A 1 43  ? 31.606 0.938   0.852   0.72 13.76 ?  43  LEU   A HD21 1 
ATOM   1156 H  HD21 B LEU   A 1 43  ? 31.275 1.050   0.902   0.28 12.41 ?  43  LEU   A HD21 1 
ATOM   1157 H  HD22 A LEU   A 1 43  ? 30.746 2.088   1.532   0.72 13.76 ?  43  LEU   A HD22 1 
ATOM   1158 H  HD22 B LEU   A 1 43  ? 30.410 2.310   1.336   0.28 12.41 ?  43  LEU   A HD22 1 
ATOM   1159 H  HD23 A LEU   A 1 43  ? 30.626 1.823   -0.030  0.72 13.76 ?  43  LEU   A HD23 1 
ATOM   1160 H  HD23 B LEU   A 1 43  ? 30.447 1.858   -0.187  0.28 12.41 ?  43  LEU   A HD23 1 
ATOM   1161 N  N    A LYS   A 1 44  ? 29.563 6.452   -1.599  0.72 10.39 ?  44  LYS   A N    1 
ATOM   1162 N  N    B LYS   A 1 44  ? 29.454 6.489   -1.702  0.28 10.93 ?  44  LYS   A N    1 
ATOM   1163 C  CA   A LYS   A 1 44  ? 28.917 7.761   -1.597  0.72 10.65 ?  44  LYS   A CA   1 
ATOM   1164 C  CA   B LYS   A 1 44  ? 28.808 7.799   -1.713  0.28 11.48 ?  44  LYS   A CA   1 
ATOM   1165 C  C    A LYS   A 1 44  ? 27.485 7.565   -1.114  0.72 10.31 ?  44  LYS   A C    1 
ATOM   1166 C  C    B LYS   A 1 44  ? 27.407 7.622   -1.147  0.28 10.55 ?  44  LYS   A C    1 
ATOM   1167 O  O    A LYS   A 1 44  ? 26.641 7.023   -1.836  0.72 11.55 ?  44  LYS   A O    1 
ATOM   1168 O  O    B LYS   A 1 44  ? 26.493 7.177   -1.845  0.28 10.82 ?  44  LYS   A O    1 
ATOM   1169 C  CB   A LYS   A 1 44  ? 28.968 8.410   -2.975  0.72 12.86 ?  44  LYS   A CB   1 
ATOM   1170 C  CB   B LYS   A 1 44  ? 28.768 8.359   -3.130  0.28 13.83 ?  44  LYS   A CB   1 
ATOM   1171 C  CG   A LYS   A 1 44  ? 30.363 8.859   -3.389  0.72 15.78 ?  44  LYS   A CG   1 
ATOM   1172 C  CG   B LYS   A 1 44  ? 30.096 8.911   -3.619  0.28 16.23 ?  44  LYS   A CG   1 
ATOM   1173 C  CD   A LYS   A 1 44  ? 31.005 9.802   -2.371  0.72 21.08 ?  44  LYS   A CD   1 
ATOM   1174 C  CD   B LYS   A 1 44  ? 30.790 9.711   -2.527  0.28 18.94 ?  44  LYS   A CD   1 
ATOM   1175 C  CE   A LYS   A 1 44  ? 32.355 10.304  -2.855  0.72 24.08 ?  44  LYS   A CE   1 
ATOM   1176 C  CE   B LYS   A 1 44  ? 31.889 10.591  -3.080  0.28 20.40 ?  44  LYS   A CE   1 
ATOM   1177 N  NZ   A LYS   A 1 44  ? 33.159 10.894  -1.751  0.72 25.43 ?  44  LYS   A NZ   1 
ATOM   1178 N  NZ   B LYS   A 1 44  ? 32.644 11.269  -1.994  0.28 21.52 ?  44  LYS   A NZ   1 
ATOM   1179 H  H    A LYS   A 1 44  ? 29.415 5.996   -2.319  0.72 12.52 ?  44  LYS   A H    1 
ATOM   1180 H  H    B LYS   A 1 44  ? 29.346 6.046   -2.429  0.28 13.16 ?  44  LYS   A H    1 
ATOM   1181 H  HA   A LYS   A 1 44  ? 29.363 8.335   -0.959  0.72 12.83 ?  44  LYS   A HA   1 
ATOM   1182 H  HA   B LYS   A 1 44  ? 29.279 8.402   -1.119  0.28 13.83 ?  44  LYS   A HA   1 
ATOM   1183 H  HB2  A LYS   A 1 44  ? 28.655 7.776   -3.637  0.72 15.48 ?  44  LYS   A HB2  1 
ATOM   1184 H  HB2  B LYS   A 1 44  ? 28.503 7.647   -3.738  0.28 16.64 ?  44  LYS   A HB2  1 
ATOM   1185 H  HB3  A LYS   A 1 44  ? 28.396 9.195   -2.974  0.72 15.48 ?  44  LYS   A HB3  1 
ATOM   1186 H  HB3  B LYS   A 1 44  ? 28.118 9.076   -3.166  0.28 16.64 ?  44  LYS   A HB3  1 
ATOM   1187 H  HG2  A LYS   A 1 44  ? 30.938 8.083   -3.480  0.72 18.98 ?  44  LYS   A HG2  1 
ATOM   1188 H  HG2  B LYS   A 1 44  ? 30.675 8.176   -3.880  0.28 19.53 ?  44  LYS   A HG2  1 
ATOM   1189 H  HG3  A LYS   A 1 44  ? 30.311 9.333   -4.237  0.72 18.98 ?  44  LYS   A HG3  1 
ATOM   1190 H  HG3  B LYS   A 1 44  ? 29.940 9.501   -4.376  0.28 19.53 ?  44  LYS   A HG3  1 
ATOM   1191 H  HD2  A LYS   A 1 44  ? 30.419 10.562  -2.227  0.72 25.35 ?  44  LYS   A HD2  1 
ATOM   1192 H  HD2  B LYS   A 1 44  ? 30.136 10.271  -2.078  0.28 22.77 ?  44  LYS   A HD2  1 
ATOM   1193 H  HD3  A LYS   A 1 44  ? 31.147 9.324   -1.538  0.72 25.35 ?  44  LYS   A HD3  1 
ATOM   1194 H  HD3  B LYS   A 1 44  ? 31.191 9.092   -1.890  0.28 22.77 ?  44  LYS   A HD3  1 
ATOM   1195 H  HE2  A LYS   A 1 44  ? 32.854 9.563   -3.229  0.72 28.94 ?  44  LYS   A HE2  1 
ATOM   1196 H  HE2  B LYS   A 1 44  ? 32.508 10.043  -3.588  0.28 24.53 ?  44  LYS   A HE2  1 
ATOM   1197 H  HE3  A LYS   A 1 44  ? 32.214 10.988  -3.528  0.72 28.94 ?  44  LYS   A HE3  1 
ATOM   1198 H  HE3  B LYS   A 1 44  ? 31.494 11.269  -3.647  0.28 24.53 ?  44  LYS   A HE3  1 
ATOM   1199 H  HZ1  A LYS   A 1 44  ? 33.939 11.182  -2.065  0.72 30.56 ?  44  LYS   A HZ1  1 
ATOM   1200 H  HZ1  B LYS   A 1 44  ? 33.284 11.778  -2.344  0.28 25.87 ?  44  LYS   A HZ1  1 
ATOM   1201 H  HZ2  A LYS   A 1 44  ? 32.721 11.584  -1.392  0.72 30.56 ?  44  LYS   A HZ2  1 
ATOM   1202 H  HZ2  B LYS   A 1 44  ? 32.097 11.777  -1.514  0.28 25.87 ?  44  LYS   A HZ2  1 
ATOM   1203 H  HZ3  A LYS   A 1 44  ? 33.304 10.286  -1.120  0.72 30.56 ?  44  LYS   A HZ3  1 
ATOM   1204 H  HZ3  B LYS   A 1 44  ? 33.019 10.661  -1.460  0.28 25.87 ?  44  LYS   A HZ3  1 
ATOM   1205 N  N    . HIS   A 1 45  ? 27.234 7.966   0.127   1.00 10.24 ?  45  HIS   A N    1 
ATOM   1206 C  CA   . HIS   A 1 45  ? 25.998 7.630   0.832   1.00 10.44 ?  45  HIS   A CA   1 
ATOM   1207 C  C    . HIS   A 1 45  ? 24.975 8.754   0.670   1.00 10.97 ?  45  HIS   A C    1 
ATOM   1208 O  O    . HIS   A 1 45  ? 24.691 9.519   1.590   1.00 12.98 ?  45  HIS   A O    1 
ATOM   1209 C  CB   . HIS   A 1 45  ? 26.301 7.382   2.296   1.00 10.23 ?  45  HIS   A CB   1 
ATOM   1210 C  CG   . HIS   A 1 45  ? 27.408 6.410   2.525   1.00 9.82  ?  45  HIS   A CG   1 
ATOM   1211 N  ND1  . HIS   A 1 45  ? 27.400 5.125   2.021   1.00 10.46 ?  45  HIS   A ND1  1 
ATOM   1212 C  CD2  . HIS   A 1 45  ? 28.575 6.561   3.196   1.00 10.13 ?  45  HIS   A CD2  1 
ATOM   1213 C  CE1  . HIS   A 1 45  ? 28.520 4.527   2.394   1.00 10.22 ?  45  HIS   A CE1  1 
ATOM   1214 N  NE2  . HIS   A 1 45  ? 29.250 5.373   3.103   1.00 10.46 ?  45  HIS   A NE2  1 
ATOM   1215 H  H    A HIS   A 1 45  ? 27.777 8.442   0.594   0.72 12.33 ?  45  HIS   A H    1 
ATOM   1216 H  H    B HIS   A 1 45  ? 27.812 8.388   0.604   0.28 12.33 ?  45  HIS   A H    1 
ATOM   1217 H  HA   . HIS   A 1 45  ? 25.619 6.819   0.456   1.00 12.58 ?  45  HIS   A HA   1 
ATOM   1218 H  HB2  . HIS   A 1 45  ? 26.545 8.224   2.713   1.00 12.32 ?  45  HIS   A HB2  1 
ATOM   1219 H  HB3  . HIS   A 1 45  ? 25.501 7.029   2.726   1.00 12.32 ?  45  HIS   A HB3  1 
ATOM   1220 H  HD2  . HIS   A 1 45  ? 28.870 7.328   3.639   1.00 12.20 ?  45  HIS   A HD2  1 
ATOM   1221 H  HE1  . HIS   A 1 45  ? 28.749 3.647   2.197   1.00 12.32 ?  45  HIS   A HE1  1 
ATOM   1222 H  HE2  . HIS   A 1 45  ? 30.020 5.201   3.449   1.00 12.60 ?  45  HIS   A HE2  1 
ATOM   1223 N  N    A GLY   A 1 46  ? 24.383 8.815   -0.517  0.72 12.02 ?  46  GLY   A N    1 
ATOM   1224 N  N    B GLY   A 1 46  ? 24.422 8.852   -0.534  0.28 11.39 ?  46  GLY   A N    1 
ATOM   1225 C  CA   A GLY   A 1 46  ? 23.556 9.953   -0.863  0.72 12.95 ?  46  GLY   A CA   1 
ATOM   1226 C  CA   B GLY   A 1 46  ? 23.618 10.011  -0.880  0.28 11.69 ?  46  GLY   A CA   1 
ATOM   1227 C  C    A GLY   A 1 46  ? 22.074 9.798   -0.595  0.72 13.13 ?  46  GLY   A C    1 
ATOM   1228 C  C    B GLY   A 1 46  ? 22.151 9.938   -0.495  0.28 11.61 ?  46  GLY   A C    1 
ATOM   1229 O  O    A GLY   A 1 46  ? 21.405 10.774  -0.236  0.72 14.33 ?  46  GLY   A O    1 
ATOM   1230 O  O    B GLY   A 1 46  ? 21.536 10.964  -0.185  0.28 12.18 ?  46  GLY   A O    1 
ATOM   1231 H  H    A GLY   A 1 46  ? 24.435 8.216   -1.128  0.72 14.47 ?  46  GLY   A H    1 
ATOM   1232 H  H    B GLY   A 1 46  ? 24.494 8.268   -1.159  0.28 13.72 ?  46  GLY   A H    1 
ATOM   1233 H  HA2  A GLY   A 1 46  ? 23.857 10.731  -0.364  0.72 15.59 ?  46  GLY   A HA2  1 
ATOM   1234 H  HA2  B GLY   A 1 46  ? 24.003 10.796  -0.450  0.28 14.08 ?  46  GLY   A HA2  1 
ATOM   1235 H  HA3  A GLY   A 1 46  ? 23.661 10.147  -1.806  0.72 15.59 ?  46  GLY   A HA3  1 
ATOM   1236 H  HA3  B GLY   A 1 46  ? 23.665 10.149  -1.838  0.28 14.08 ?  46  GLY   A HA3  1 
ATOM   1237 N  N    A GLY   A 1 47  ? 21.537 8.597   -0.789  0.72 12.54 ?  47  GLY   A N    1 
ATOM   1238 N  N    B GLY   A 1 47  ? 21.572 8.745   -0.533  0.28 11.37 ?  47  GLY   A N    1 
ATOM   1239 C  CA   A GLY   A 1 47  ? 20.105 8.390   -0.726  0.72 12.31 ?  47  GLY   A CA   1 
ATOM   1240 C  CA   B GLY   A 1 47  ? 20.158 8.576   -0.279  0.28 11.55 ?  47  GLY   A CA   1 
ATOM   1241 C  C    A GLY   A 1 47  ? 19.781 6.962   -0.346  0.72 12.00 ?  47  GLY   A C    1 
ATOM   1242 C  C    B GLY   A 1 47  ? 19.829 7.128   0.018   0.28 11.32 ?  47  GLY   A C    1 
ATOM   1243 O  O    A GLY   A 1 47  ? 20.672 6.133   -0.146  0.72 11.96 ?  47  GLY   A O    1 
ATOM   1244 O  O    B GLY   A 1 47  ? 20.717 6.282   0.151   0.28 11.37 ?  47  GLY   A O    1 
ATOM   1245 H  H    A GLY   A 1 47  ? 21.987 7.879   -0.946  0.72 15.09 ?  47  GLY   A H    1 
ATOM   1246 H  H    B GLY   A 1 47  ? 21.987 8.018   -0.701  0.28 13.69 ?  47  GLY   A H    1 
ATOM   1247 H  HA2  A GLY   A 1 47  ? 19.709 8.990   -0.074  0.72 14.82 ?  47  GLY   A HA2  1 
ATOM   1248 H  HA2  B GLY   A 1 47  ? 19.882 9.118   0.481   0.28 13.91 ?  47  GLY   A HA2  1 
ATOM   1249 H  HA3  A GLY   A 1 47  ? 19.709 8.569   -1.594  0.72 14.82 ?  47  GLY   A HA3  1 
ATOM   1250 H  HA3  B GLY   A 1 47  ? 19.648 8.868   -1.058  0.28 13.91 ?  47  GLY   A HA3  1 
ATOM   1251 N  N    A GLY   A 1 48  ? 18.487 6.666   -0.269  0.72 11.92 ?  48  GLY   A N    1 
ATOM   1252 N  N    B GLY   A 1 48  ? 18.533 6.853   0.129   0.28 11.96 ?  48  GLY   A N    1 
ATOM   1253 C  CA   A GLY   A 1 48  ? 18.085 5.348   0.160   0.72 12.28 ?  48  GLY   A CA   1 
ATOM   1254 C  CA   B GLY   A 1 48  ? 18.077 5.507   0.424   0.28 11.88 ?  48  GLY   A CA   1 
ATOM   1255 C  C    A GLY   A 1 48  ? 18.588 5.060   1.559   0.72 11.34 ?  48  GLY   A C    1 
ATOM   1256 C  C    B GLY   A 1 48  ? 18.576 5.039   1.774   0.28 11.51 ?  48  GLY   A C    1 
ATOM   1257 O  O    A GLY   A 1 48  ? 18.789 5.967   2.378   0.72 11.60 ?  48  GLY   A O    1 
ATOM   1258 O  O    B GLY   A 1 48  ? 18.691 5.816   2.730   0.28 11.78 ?  48  GLY   A O    1 
ATOM   1259 H  H    A GLY   A 1 48  ? 17.834 7.204   -0.446  0.72 14.36 ?  48  GLY   A H    1 
ATOM   1260 H  H    B GLY   A 1 48  ? 17.905 7.427   0.043   0.28 14.40 ?  48  GLY   A H    1 
ATOM   1261 H  HA2  A GLY   A 1 48  ? 17.119 5.272   0.158   0.72 14.79 ?  48  GLY   A HA2  1 
ATOM   1262 H  HA2  B GLY   A 1 48  ? 17.106 5.485   0.420   0.28 14.30 ?  48  GLY   A HA2  1 
ATOM   1263 H  HA3  A GLY   A 1 48  ? 18.455 4.682   -0.437  0.72 14.79 ?  48  GLY   A HA3  1 
ATOM   1264 H  HA3  B GLY   A 1 48  ? 18.403 4.891   -0.250  0.28 14.30 ?  48  GLY   A HA3  1 
ATOM   1265 N  N    A VAL   A 1 49  ? 18.795 3.771   1.839   0.72 11.38 ?  49  VAL   A N    1 
ATOM   1266 N  N    B VAL   A 1 49  ? 18.871 3.741   1.858   0.28 10.97 ?  49  VAL   A N    1 
ATOM   1267 C  CA   A VAL   A 1 49  ? 19.311 3.352   3.139   0.72 11.33 ?  49  VAL   A CA   1 
ATOM   1268 C  CA   B VAL   A 1 49  ? 19.451 3.183   3.075   0.28 10.45 ?  49  VAL   A CA   1 
ATOM   1269 C  C    A VAL   A 1 49  ? 20.620 4.064   3.462   0.72 9.97  ?  49  VAL   A C    1 
ATOM   1270 C  C    B VAL   A 1 49  ? 20.743 3.910   3.425   0.28 9.74  ?  49  VAL   A C    1 
ATOM   1271 O  O    A VAL   A 1 49  ? 20.828 4.511   4.594   0.72 10.52 ?  49  VAL   A O    1 
ATOM   1272 O  O    B VAL   A 1 49  ? 20.976 4.274   4.583   0.28 9.49  ?  49  VAL   A O    1 
ATOM   1273 C  CB   A VAL   A 1 49  ? 19.466 1.819   3.178   0.72 12.28 ?  49  VAL   A CB   1 
ATOM   1274 C  CB   B VAL   A 1 49  ? 19.677 1.668   2.913   0.28 10.24 ?  49  VAL   A CB   1 
ATOM   1275 C  CG1  A VAL   A 1 49  ? 20.299 1.379   4.380   0.72 11.96 ?  49  VAL   A CG1  1 
ATOM   1276 C  CG1  B VAL   A 1 49  ? 20.556 1.138   4.037   0.28 10.32 ?  49  VAL   A CG1  1 
ATOM   1277 C  CG2  A VAL   A 1 49  ? 18.096 1.151   3.208   0.72 14.29 ?  49  VAL   A CG2  1 
ATOM   1278 C  CG2  B VAL   A 1 49  ? 18.346 0.925   2.875   0.28 10.30 ?  49  VAL   A CG2  1 
ATOM   1279 H  H    A VAL   A 1 49  ? 18.642 3.122   1.300   0.72 13.70 ?  49  VAL   A H    1 
ATOM   1280 H  H    B VAL   A 1 49  ? 18.751 3.172   1.228   0.28 13.22 ?  49  VAL   A H    1 
ATOM   1281 H  HA   A VAL   A 1 49  ? 18.675 3.595   3.827   0.72 13.65 ?  49  VAL   A HA   1 
ATOM   1282 H  HA   B VAL   A 1 49  ? 18.830 3.310   3.811   0.28 12.59 ?  49  VAL   A HA   1 
ATOM   1283 H  HB   A VAL   A 1 49  ? 19.924 1.524   2.374   0.72 14.79 ?  49  VAL   A HB   1 
ATOM   1284 H  HB   B VAL   A 1 49  ? 20.133 1.502   2.073   0.28 12.33 ?  49  VAL   A HB   1 
ATOM   1285 H  HG11 A VAL   A 1 49  ? 20.152 0.434   4.537   0.72 14.40 ?  49  VAL   A HG11 1 
ATOM   1286 H  HG11 B VAL   A 1 49  ? 20.447 0.177   4.097   0.28 12.43 ?  49  VAL   A HG11 1 
ATOM   1287 H  HG12 A VAL   A 1 49  ? 21.238 1.539   4.193   0.72 14.40 ?  49  VAL   A HG12 1 
ATOM   1288 H  HG12 B VAL   A 1 49  ? 21.482 1.353   3.844   0.28 12.43 ?  49  VAL   A HG12 1 
ATOM   1289 H  HG13 A VAL   A 1 49  ? 20.024 1.890   5.157   0.72 14.40 ?  49  VAL   A HG13 1 
ATOM   1290 H  HG13 B VAL   A 1 49  ? 20.284 1.553   4.871   0.28 12.43 ?  49  VAL   A HG13 1 
ATOM   1291 H  HG21 A VAL   A 1 49  ? 18.216 0.189   3.223   0.72 17.20 ?  49  VAL   A HG21 1 
ATOM   1292 H  HG21 B VAL   A 1 49  ? 18.514 -0.024  2.764   0.28 12.41 ?  49  VAL   A HG21 1 
ATOM   1293 H  HG22 A VAL   A 1 49  ? 17.627 1.440   4.006   0.72 17.20 ?  49  VAL   A HG22 1 
ATOM   1294 H  HG22 B VAL   A 1 49  ? 17.874 1.082   3.709   0.28 12.41 ?  49  VAL   A HG22 1 
ATOM   1295 H  HG23 A VAL   A 1 49  ? 17.603 1.414   2.417   0.72 17.20 ?  49  VAL   A HG23 1 
ATOM   1296 H  HG23 B VAL   A 1 49  ? 17.820 1.258   2.131   0.28 12.41 ?  49  VAL   A HG23 1 
ATOM   1297 N  N    A ALA   A 1 50  ? 21.539 4.125   2.492   0.72 9.95  ?  50  ALA   A N    1 
ATOM   1298 N  N    B ALA   A 1 50  ? 21.610 4.111   2.429   0.28 9.57  ?  50  ALA   A N    1 
ATOM   1299 C  CA   A ALA   A 1 50  ? 22.860 4.686   2.767   0.72 9.86  ?  50  ALA   A CA   1 
ATOM   1300 C  CA   B ALA   A 1 50  ? 22.920 4.699   2.691   0.28 9.88  ?  50  ALA   A CA   1 
ATOM   1301 C  C    A ALA   A 1 50  ? 22.764 6.145   3.187   0.72 9.85  ?  50  ALA   A C    1 
ATOM   1302 C  C    B ALA   A 1 50  ? 22.795 6.146   3.152   0.28 10.01 ?  50  ALA   A C    1 
ATOM   1303 O  O    A ALA   A 1 50  ? 23.394 6.567   4.165   0.72 10.43 ?  50  ALA   A O    1 
ATOM   1304 O  O    B ALA   A 1 50  ? 23.429 6.554   4.132   0.28 10.30 ?  50  ALA   A O    1 
ATOM   1305 C  CB   A ALA   A 1 50  ? 23.758 4.543   1.542   0.72 9.60  ?  50  ALA   A CB   1 
ATOM   1306 C  CB   B ALA   A 1 50  ? 23.790 4.602   1.438   0.28 10.10 ?  50  ALA   A CB   1 
ATOM   1307 H  H    A ALA   A 1 50  ? 21.427 3.857   1.681   0.72 11.98 ?  50  ALA   A H    1 
ATOM   1308 H  H    B ALA   A 1 50  ? 21.460 3.918   1.605   0.28 11.53 ?  50  ALA   A H    1 
ATOM   1309 H  HA   A ALA   A 1 50  ? 23.270 4.198   3.495   0.72 11.89 ?  50  ALA   A HA   1 
ATOM   1310 H  HA   B ALA   A 1 50  ? 23.355 4.204   3.397   0.28 11.91 ?  50  ALA   A HA   1 
ATOM   1311 H  HB1  A ALA   A 1 50  ? 24.629 4.924   1.741   0.72 11.57 ?  50  ALA   A HB1  1 
ATOM   1312 H  HB1  B ALA   A 1 50  ? 24.656 4.995   1.624   0.28 12.16 ?  50  ALA   A HB1  1 
ATOM   1313 H  HB2  A ALA   A 1 50  ? 23.849 3.604   1.323   0.72 11.57 ?  50  ALA   A HB2  1 
ATOM   1314 H  HB2  B ALA   A 1 50  ? 23.896 3.667   1.199   0.28 12.16 ?  50  ALA   A HB2  1 
ATOM   1315 H  HB3  A ALA   A 1 50  ? 23.355 5.019   0.797   0.72 11.57 ?  50  ALA   A HB3  1 
ATOM   1316 H  HB3  B ALA   A 1 50  ? 23.357 5.080   0.713   0.28 12.16 ?  50  ALA   A HB3  1 
ATOM   1317 N  N    . GLY   A 1 51  ? 21.982 6.938   2.456   1.00 10.32 ?  51  GLY   A N    1 
ATOM   1318 C  CA   . GLY   A 1 51  ? 21.822 8.327   2.841   1.00 10.46 ?  51  GLY   A CA   1 
ATOM   1319 C  C    . GLY   A 1 51  ? 21.221 8.467   4.224   1.00 10.48 ?  51  GLY   A C    1 
ATOM   1320 O  O    . GLY   A 1 51  ? 21.604 9.356   4.992   1.00 11.25 ?  51  GLY   A O    1 
ATOM   1321 H  H    A GLY   A 1 51  ? 21.546 6.698   1.751   0.72 12.43 ?  51  GLY   A H    1 
ATOM   1322 H  H    B GLY   A 1 51  ? 21.522 6.694   1.770   0.28 12.43 ?  51  GLY   A H    1 
ATOM   1323 H  HA2  . GLY   A 1 51  ? 22.684 8.766   2.835   1.00 12.60 ?  51  GLY   A HA2  1 
ATOM   1324 H  HA3  . GLY   A 1 51  ? 21.241 8.776   2.207   1.00 12.60 ?  51  GLY   A HA3  1 
ATOM   1325 N  N    . ALA   A 1 52  ? 20.254 7.602   4.552   1.00 10.70 ?  52  ALA   A N    1 
ATOM   1326 C  CA   . ALA   A 1 52  ? 19.611 7.653   5.860   1.00 11.47 ?  52  ALA   A CA   1 
ATOM   1327 C  C    . ALA   A 1 52  ? 20.572 7.249   6.978   1.00 10.65 ?  52  ALA   A C    1 
ATOM   1328 O  O    . ALA   A 1 52  ? 20.645 7.914   8.016   1.00 11.47 ?  52  ALA   A O    1 
ATOM   1329 C  CB   . ALA   A 1 52  ? 18.361 6.768   5.858   1.00 12.92 ?  52  ALA   A CB   1 
ATOM   1330 H  H    . ALA   A 1 52  ? 19.968 6.966   4.039   1.00 12.88 ?  52  ALA   A H    1 
ATOM   1331 H  HA   . ALA   A 1 52  ? 19.325 8.558   6.029   1.00 13.82 ?  52  ALA   A HA   1 
ATOM   1332 H  HB1  . ALA   A 1 52  ? 17.933 6.823   6.730   1.00 15.55 ?  52  ALA   A HB1  1 
ATOM   1333 H  HB2  . ALA   A 1 52  ? 17.749 7.086   5.174   1.00 15.55 ?  52  ALA   A HB2  1 
ATOM   1334 H  HB3  . ALA   A 1 52  ? 18.615 5.851   5.674   1.00 15.55 ?  52  ALA   A HB3  1 
ATOM   1335 N  N    A LEU   A 1 53  ? 21.302 6.144   6.804   0.72 10.79 ?  53  LEU   A N    1 
ATOM   1336 N  N    B LEU   A 1 53  ? 21.314 6.152   6.779   0.28 10.56 ?  53  LEU   A N    1 
ATOM   1337 C  CA   A LEU   A 1 53  ? 22.277 5.760   7.822   0.72 10.77 ?  53  LEU   A CA   1 
ATOM   1338 C  CA   B LEU   A 1 53  ? 22.285 5.714   7.779   0.28 10.39 ?  53  LEU   A CA   1 
ATOM   1339 C  C    A LEU   A 1 53  ? 23.310 6.860   8.010   0.72 10.13 ?  53  LEU   A C    1 
ATOM   1340 C  C    B LEU   A 1 53  ? 23.364 6.768   7.993   0.28 10.19 ?  53  LEU   A C    1 
ATOM   1341 O  O    A LEU   A 1 53  ? 23.609 7.263   9.138   0.72 10.92 ?  53  LEU   A O    1 
ATOM   1342 O  O    B LEU   A 1 53  ? 23.763 7.037   9.131   0.28 10.57 ?  53  LEU   A O    1 
ATOM   1343 C  CB   A LEU   A 1 53  ? 22.960 4.437   7.456   0.72 11.23 ?  53  LEU   A CB   1 
ATOM   1344 C  CB   B LEU   A 1 53  ? 22.926 4.387   7.352   0.28 10.30 ?  53  LEU   A CB   1 
ATOM   1345 C  CG   A LEU   A 1 53  ? 22.085 3.175   7.468   0.72 12.35 ?  53  LEU   A CG   1 
ATOM   1346 C  CG   B LEU   A 1 53  ? 22.153 3.073   7.528   0.28 9.93  ?  53  LEU   A CG   1 
ATOM   1347 C  CD1  A LEU   A 1 53  ? 22.876 1.987   6.945   0.72 13.27 ?  53  LEU   A CD1  1 
ATOM   1348 C  CD1  B LEU   A 1 53  ? 22.858 1.955   6.770   0.28 10.60 ?  53  LEU   A CD1  1 
ATOM   1349 C  CD2  A LEU   A 1 53  ? 21.544 2.883   8.858   0.72 13.26 ?  53  LEU   A CD2  1 
ATOM   1350 C  CD2  B LEU   A 1 53  ? 22.019 2.702   8.994   0.28 9.59  ?  53  LEU   A CD2  1 
ATOM   1351 H  H    A LEU   A 1 53  ? 21.249 5.613   6.127   0.72 13.00 ?  53  LEU   A H    1 
ATOM   1352 H  H    B LEU   A 1 53  ? 21.275 5.653   6.077   0.28 12.72 ?  53  LEU   A H    1 
ATOM   1353 H  HA   A LEU   A 1 53  ? 21.818 5.630   8.665   0.72 12.98 ?  53  LEU   A HA   1 
ATOM   1354 H  HA   B LEU   A 1 53  ? 21.831 5.567   8.623   0.28 12.51 ?  53  LEU   A HA   1 
ATOM   1355 H  HB2  A LEU   A 1 53  ? 23.328 4.518   6.560   0.72 13.53 ?  53  LEU   A HB2  1 
ATOM   1356 H  HB2  B LEU   A 1 53  ? 23.136 4.451   6.407   0.28 12.41 ?  53  LEU   A HB2  1 
ATOM   1357 H  HB3  A LEU   A 1 53  ? 23.684 4.281   8.083   0.72 13.53 ?  53  LEU   A HB3  1 
ATOM   1358 H  HB3  B LEU   A 1 53  ? 23.749 4.281   7.849   0.28 12.41 ?  53  LEU   A HB3  1 
ATOM   1359 H  HG   A LEU   A 1 53  ? 21.332 3.310   6.869   0.72 14.86 ?  53  LEU   A HG   1 
ATOM   1360 H  HG   B LEU   A 1 53  ? 21.264 3.167   7.152   0.28 11.96 ?  53  LEU   A HG   1 
ATOM   1361 H  HD11 A LEU   A 1 53  ? 22.306 1.199   6.957   0.72 15.98 ?  53  LEU   A HD11 1 
ATOM   1362 H  HD11 B LEU   A 1 53  ? 22.367 1.127   6.898   0.28 12.76 ?  53  LEU   A HD11 1 
ATOM   1363 H  HD12 A LEU   A 1 53  ? 23.165 2.170   6.038   0.72 15.98 ?  53  LEU   A HD12 1 
ATOM   1364 H  HD12 B LEU   A 1 53  ? 22.890 2.179   5.828   0.28 12.76 ?  53  LEU   A HD12 1 
ATOM   1365 H  HD13 A LEU   A 1 53  ? 23.646 1.845   7.517   0.72 15.98 ?  53  LEU   A HD13 1 
ATOM   1366 H  HD13 B LEU   A 1 53  ? 23.760 1.858   7.118   0.28 12.76 ?  53  LEU   A HD13 1 
ATOM   1367 H  HD21 A LEU   A 1 53  ? 21.073 2.036   8.841   0.72 15.96 ?  53  LEU   A HD21 1 
ATOM   1368 H  HD21 B LEU   A 1 53  ? 21.491 1.891   9.068   0.28 11.55 ?  53  LEU   A HD21 1 
ATOM   1369 H  HD22 A LEU   A 1 53  ? 22.284 2.841   9.480   0.72 15.96 ?  53  LEU   A HD22 1 
ATOM   1370 H  HD22 B LEU   A 1 53  ? 22.903 2.556   9.365   0.28 11.55 ?  53  LEU   A HD22 1 
ATOM   1371 H  HD23 A LEU   A 1 53  ? 20.936 3.594   9.112   0.72 15.96 ?  53  LEU   A HD23 1 
ATOM   1372 H  HD23 B LEU   A 1 53  ? 21.579 3.428   9.461   0.28 11.55 ?  53  LEU   A HD23 1 
ATOM   1373 N  N    . ASN   A 1 54  ? 23.850 7.371   6.909   1.00 10.16 ?  54  ASN   A N    1 
ATOM   1374 C  CA   . ASN   A 1 54  ? 24.897 8.371   7.036   1.00 10.18 ?  54  ASN   A CA   1 
ATOM   1375 C  C    . ASN   A 1 54  ? 24.387 9.622   7.748   1.00 10.46 ?  54  ASN   A C    1 
ATOM   1376 O  O    . ASN   A 1 54  ? 25.075 10.180  8.617   1.00 11.16 ?  54  ASN   A O    1 
ATOM   1377 C  CB   . ASN   A 1 54  ? 25.456 8.725   5.673   1.00 10.23 ?  54  ASN   A CB   1 
ATOM   1378 C  CG   . ASN   A 1 54  ? 26.473 9.831   5.775   1.00 10.40 ?  54  ASN   A CG   1 
ATOM   1379 O  OD1  . ASN   A 1 54  ? 27.488 9.692   6.479   1.00 10.65 ?  54  ASN   A OD1  1 
ATOM   1380 N  ND2  . ASN   A 1 54  ? 26.203 10.952  5.123   1.00 11.26 ?  54  ASN   A ND2  1 
ATOM   1381 H  H    A ASN   A 1 54  ? 23.627 7.162   6.105   0.72 12.24 ?  54  ASN   A H    1 
ATOM   1382 H  H    B ASN   A 1 54  ? 23.576 7.227   6.106   0.28 12.24 ?  54  ASN   A H    1 
ATOM   1383 H  HA   . ASN   A 1 54  ? 25.613 8.002   7.567   1.00 12.26 ?  54  ASN   A HA   1 
ATOM   1384 H  HB2  . ASN   A 1 54  ? 25.892 7.940   5.295   1.00 12.33 ?  54  ASN   A HB2  1 
ATOM   1385 H  HB3  . ASN   A 1 54  ? 24.737 9.017   5.092   1.00 12.33 ?  54  ASN   A HB3  1 
ATOM   1386 H  HD21 . ASN   A 1 54  ? 26.746 11.614  5.165   1.00 13.56 ?  54  ASN   A HD21 1 
ATOM   1387 H  HD22 . ASN   A 1 54  ? 25.477 11.016  4.663   1.00 13.56 ?  54  ASN   A HD22 1 
ATOM   1388 N  N    . LYS   A 1 55  ? 23.173 10.071  7.404   1.00 10.82 ?  55  LYS   A N    1 
ATOM   1389 C  CA   . LYS   A 1 55  ? 22.594 11.225  8.077   1.00 11.54 ?  55  LYS   A CA   1 
ATOM   1390 C  C    . LYS   A 1 55  ? 22.504 10.992  9.578   1.00 11.58 ?  55  LYS   A C    1 
ATOM   1391 O  O    . LYS   A 1 55  ? 22.787 11.895  10.375  1.00 12.49 ?  55  LYS   A O    1 
ATOM   1392 C  CB   . LYS   A 1 55  ? 21.223 11.527  7.471   1.00 12.30 ?  55  LYS   A CB   1 
ATOM   1393 C  CG   . LYS   A 1 55  ? 20.480 12.688  8.113   1.00 13.93 ?  55  LYS   A CG   1 
ATOM   1394 C  CD   . LYS   A 1 55  ? 19.157 12.931  7.394   1.00 15.50 ?  55  LYS   A CD   1 
ATOM   1395 C  CE   . LYS   A 1 55  ? 18.301 13.986  8.085   1.00 17.47 ?  55  LYS   A CE   1 
ATOM   1396 N  NZ   . LYS   A 1 55  ? 16.973 14.144  7.423   1.00 18.34 ?  55  LYS   A NZ   1 
ATOM   1397 H  H    . LYS   A 1 55  ? 22.668 9.722   6.796   1.00 13.03 ?  55  LYS   A H    1 
ATOM   1398 H  HA   . LYS   A 1 55  ? 23.161 11.994  7.931   1.00 13.89 ?  55  LYS   A HA   1 
ATOM   1399 H  HB2  . LYS   A 1 55  ? 21.340 11.744  6.535   1.00 14.80 ?  55  LYS   A HB2  1 
ATOM   1400 H  HB3  . LYS   A 1 55  ? 20.662 10.742  7.560   1.00 14.80 ?  55  LYS   A HB3  1 
ATOM   1401 H  HG2  . LYS   A 1 55  ? 20.284 12.480  9.042   1.00 16.76 ?  55  LYS   A HG2  1 
ATOM   1402 H  HG3  . LYS   A 1 55  ? 21.013 13.494  8.051   1.00 16.76 ?  55  LYS   A HG3  1 
ATOM   1403 H  HD2  . LYS   A 1 55  ? 19.339 13.236  6.491   1.00 18.65 ?  55  LYS   A HD2  1 
ATOM   1404 H  HD3  . LYS   A 1 55  ? 18.652 12.103  7.368   1.00 18.65 ?  55  LYS   A HD3  1 
ATOM   1405 H  HE2  . LYS   A 1 55  ? 18.149 13.720  9.005   1.00 21.01 ?  55  LYS   A HE2  1 
ATOM   1406 H  HE3  . LYS   A 1 55  ? 18.757 14.839  8.052   1.00 21.01 ?  55  LYS   A HE3  1 
ATOM   1407 H  HZ1  . LYS   A 1 55  ? 16.421 14.602  7.953   1.00 22.06 ?  55  LYS   A HZ1  1 
ATOM   1408 H  HZ2  . LYS   A 1 55  ? 17.062 14.584  6.655   1.00 22.06 ?  55  LYS   A HZ2  1 
ATOM   1409 H  HZ3  . LYS   A 1 55  ? 16.614 13.345  7.260   1.00 22.06 ?  55  LYS   A HZ3  1 
ATOM   1410 N  N    . ALA   A 1 56  ? 22.120 9.778   9.987   1.00 12.00 ?  56  ALA   A N    1 
ATOM   1411 C  CA   . ALA   A 1 56  ? 21.998 9.462   11.404  1.00 12.80 ?  56  ALA   A CA   1 
ATOM   1412 C  C    . ALA   A 1 56  ? 23.337 9.486   12.129  1.00 12.26 ?  56  ALA   A C    1 
ATOM   1413 O  O    . ALA   A 1 56  ? 23.359 9.671   13.347  1.00 13.87 ?  56  ALA   A O    1 
ATOM   1414 C  CB   . ALA   A 1 56  ? 21.290 8.116   11.599  1.00 13.29 ?  56  ALA   A CB   1 
ATOM   1415 H  H    . ALA   A 1 56  ? 21.935 9.127   9.461   1.00 14.45 ?  56  ALA   A H    1 
ATOM   1416 H  HA   . ALA   A 1 56  ? 21.448 10.131  11.820  1.00 15.41 ?  56  ALA   A HA   1 
ATOM   1417 H  HB1  . ALA   A 1 56  ? 21.221 7.928   12.552  1.00 16.00 ?  56  ALA   A HB1  1 
ATOM   1418 H  HB2  . ALA   A 1 56  ? 20.402 8.171   11.212  1.00 16.00 ?  56  ALA   A HB2  1 
ATOM   1419 H  HB3  . ALA   A 1 56  ? 21.799 7.416   11.163  1.00 16.00 ?  56  ALA   A HB3  1 
ATOM   1420 N  N    . THR   A 1 57  ? 24.450 9.305   11.411  1.00 11.42 ?  57  THR   A N    1 
ATOM   1421 C  CA   . THR   A 1 57  ? 25.791 9.433   11.987  1.00 11.68 ?  57  THR   A CA   1 
ATOM   1422 C  C    . THR   A 1 57  ? 26.344 10.852  11.900  1.00 12.23 ?  57  THR   A C    1 
ATOM   1423 O  O    . THR   A 1 57  ? 27.532 11.062  12.187  1.00 12.84 ?  57  THR   A O    1 
ATOM   1424 C  CB   . THR   A 1 57  ? 26.802 8.480   11.318  1.00 11.70 ?  57  THR   A CB   1 
ATOM   1425 O  OG1  . THR   A 1 57  ? 27.186 8.980   10.023  1.00 11.44 ?  57  THR   A OG1  1 
ATOM   1426 C  CG2  . THR   A 1 57  ? 26.275 7.061   11.213  1.00 11.64 ?  57  THR   A CG2  1 
ATOM   1427 H  H    . THR   A 1 57  ? 24.457 9.085   10.579  1.00 13.75 ?  57  THR   A H    1 
ATOM   1428 H  HA   . THR   A 1 57  ? 25.746 9.180   12.929  1.00 14.06 ?  57  THR   A HA   1 
ATOM   1429 H  HB   . THR   A 1 57  ? 27.601 8.442   11.876  1.00 14.08 ?  57  THR   A HB   1 
ATOM   1430 H  HG1  . THR   A 1 57  ? 26.503 9.045   9.535   1.00 13.78 ?  57  THR   A HG1  1 
ATOM   1431 H  HG21 . THR   A 1 57  ? 26.884 6.512   10.689  1.00 14.01 ?  57  THR   A HG21 1 
ATOM   1432 H  HG22 . THR   A 1 57  ? 26.186 6.666   12.096  1.00 14.01 ?  57  THR   A HG22 1 
ATOM   1433 H  HG23 . THR   A 1 57  ? 25.407 7.053   10.783  1.00 14.01 ?  57  THR   A HG23 1 
ATOM   1434 N  N    . ASN   A 1 58  ? 25.529 11.825  11.496  1.00 12.71 ?  58  ASN   A N    1 
ATOM   1435 C  CA   . ASN   A 1 58  ? 25.993 13.206  11.400  1.00 13.47 ?  58  ASN   A CA   1 
ATOM   1436 C  C    . ASN   A 1 58  ? 27.141 13.326  10.392  1.00 12.17 ?  58  ASN   A C    1 
ATOM   1437 O  O    . ASN   A 1 58  ? 28.035 14.162  10.543  1.00 13.04 ?  58  ASN   A O    1 
ATOM   1438 C  CB   . ASN   A 1 58  ? 26.375 13.736  12.797  1.00 15.89 ?  58  ASN   A CB   1 
ATOM   1439 C  CG   . ASN   A 1 58  ? 26.809 15.189  12.801  1.00 19.49 ?  58  ASN   A CG   1 
ATOM   1440 O  OD1  . ASN   A 1 58  ? 26.181 16.033  12.171  1.00 21.11 ?  58  ASN   A OD1  1 
ATOM   1441 N  ND2  . ASN   A 1 58  ? 27.881 15.491  13.541  1.00 20.47 ?  58  ASN   A ND2  1 
ATOM   1442 H  H    . ASN   A 1 58  ? 24.706 11.702  11.266  1.00 15.30 ?  58  ASN   A H    1 
ATOM   1443 H  HA   . ASN   A 1 58  ? 25.257 13.743  11.076  1.00 16.22 ?  58  ASN   A HA   1 
ATOM   1444 H  HB2  . ASN   A 1 58  ? 25.600 13.652  13.385  1.00 19.12 ?  58  ASN   A HB2  1 
ATOM   1445 H  HB3  . ASN   A 1 58  ? 27.105 13.210  13.151  1.00 19.12 ?  58  ASN   A HB3  1 
ATOM   1446 H  HD21 . ASN   A 1 58  ? 28.164 16.303  13.580  1.00 24.61 ?  58  ASN   A HD21 1 
ATOM   1447 H  HD22 . ASN   A 1 58  ? 28.289 14.872  13.974  1.00 24.61 ?  58  ASN   A HD22 1 
ATOM   1448 N  N    . ASN   A 1 59  ? 27.118 12.504  9.340   1.00 11.29 ?  59  ASN   A N    1 
ATOM   1449 C  CA   . ASN   A 1 59  ? 28.094 12.481  8.243   1.00 10.90 ?  59  ASN   A CA   1 
ATOM   1450 C  C    . ASN   A 1 59  ? 29.413 11.804  8.633   1.00 10.83 ?  59  ASN   A C    1 
ATOM   1451 O  O    . ASN   A 1 59  ? 30.332 11.763  7.805   1.00 11.14 ?  59  ASN   A O    1 
ATOM   1452 C  CB   . ASN   A 1 59  ? 28.378 13.867  7.635   1.00 11.23 ?  59  ASN   A CB   1 
ATOM   1453 C  CG   . ASN   A 1 59  ? 28.733 13.799  6.163   1.00 11.57 ?  59  ASN   A CG   1 
ATOM   1454 O  OD1  . ASN   A 1 59  ? 28.032 13.171  5.365   1.00 11.78 ?  59  ASN   A OD1  1 
ATOM   1455 N  ND2  . ASN   A 1 59  ? 29.828 14.456  5.789   1.00 12.28 ?  59  ASN   A ND2  1 
ATOM   1456 H  H    . ASN   A 1 59  ? 26.504 11.911  9.230   1.00 13.60 ?  59  ASN   A H    1 
ATOM   1457 H  HA   . ASN   A 1 59  ? 27.714 11.948  7.533   1.00 13.13 ?  59  ASN   A HA   1 
ATOM   1458 H  HB2  . ASN   A 1 59  ? 27.589 14.425  7.719   1.00 13.52 ?  59  ASN   A HB2  1 
ATOM   1459 H  HB3  . ASN   A 1 59  ? 29.125 14.278  8.098   1.00 13.52 ?  59  ASN   A HB3  1 
ATOM   1460 H  HD21 . ASN   A 1 59  ? 30.077 14.450  4.964   1.00 14.79 ?  59  ASN   A HD21 1 
ATOM   1461 H  HD22 . ASN   A 1 59  ? 30.299 14.882  6.372   1.00 14.79 ?  59  ASN   A HD22 1 
ATOM   1462 N  N    . ALA   A 1 60  ? 29.539 11.262  9.845   1.00 10.81 ?  60  ALA   A N    1 
ATOM   1463 C  CA   . ALA   A 1 60  ? 30.778 10.579  10.204  1.00 11.24 ?  60  ALA   A CA   1 
ATOM   1464 C  C    . ALA   A 1 60  ? 31.002 9.342   9.341   1.00 11.12 ?  60  ALA   A C    1 
ATOM   1465 O  O    . ALA   A 1 60  ? 32.147 9.022   9.003   1.00 11.53 ?  60  ALA   A O    1 
ATOM   1466 C  CB   . ALA   A 1 60  ? 30.773 10.221  11.685  1.00 11.98 ?  60  ALA   A CB   1 
ATOM   1467 H  H    . ALA   A 1 60  ? 28.940 11.272  10.459  1.00 13.02 ?  60  ALA   A H    1 
ATOM   1468 H  HA   . ALA   A 1 60  ? 31.523 11.185  10.047  1.00 13.53 ?  60  ALA   A HA   1 
ATOM   1469 H  HB1  . ALA   A 1 60  ? 31.602 9.774   11.905  1.00 14.42 ?  60  ALA   A HB1  1 
ATOM   1470 H  HB2  . ALA   A 1 60  ? 30.690 11.040  12.204  1.00 14.42 ?  60  ALA   A HB2  1 
ATOM   1471 H  HB3  . ALA   A 1 60  ? 30.019 9.640   11.865  1.00 14.42 ?  60  ALA   A HB3  1 
ATOM   1472 N  N    . MET   A 1 61  ? 29.929 8.647   8.961   1.00 10.65 ?  61  MET   A N    1 
ATOM   1473 C  CA   . MET   A 1 61  ? 30.066 7.512   8.054   1.00 10.36 ?  61  MET   A CA   1 
ATOM   1474 C  C    . MET   A 1 61  ? 30.695 7.936   6.728   1.00 10.57 ?  61  MET   A C    1 
ATOM   1475 O  O    . MET   A 1 61  ? 31.585 7.254   6.209   1.00 10.95 ?  61  MET   A O    1 
ATOM   1476 C  CB   . MET   A 1 61  ? 28.705 6.842   7.845   1.00 10.30 ?  61  MET   A CB   1 
ATOM   1477 C  CG   . MET   A 1 61  ? 28.709 5.681   6.861   1.00 11.04 ?  61  MET   A CG   1 
ATOM   1478 S  SD   . MET   A 1 61  ? 27.092 4.934   6.665   1.00 12.07 ?  61  MET   A SD   1 
ATOM   1479 C  CE   . MET   A 1 61  ? 26.973 4.040   8.221   1.00 13.34 ?  61  MET   A CE   1 
ATOM   1480 H  H    . MET   A 1 61  ? 29.123 8.812   9.212   1.00 12.83 ?  61  MET   A H    1 
ATOM   1481 H  HA   . MET   A 1 61  ? 30.645 6.857   8.472   1.00 12.48 ?  61  MET   A HA   1 
ATOM   1482 H  HB2  . MET   A 1 61  ? 28.392 6.502   8.697   1.00 12.41 ?  61  MET   A HB2  1 
ATOM   1483 H  HB3  . MET   A 1 61  ? 28.081 7.506   7.511   1.00 12.41 ?  61  MET   A HB3  1 
ATOM   1484 H  HG2  . MET   A 1 61  ? 28.986 5.997   5.987   1.00 13.29 ?  61  MET   A HG2  1 
ATOM   1485 H  HG3  . MET   A 1 61  ? 29.312 4.994   7.176   1.00 13.29 ?  61  MET   A HG3  1 
ATOM   1486 H  HE1  . MET   A 1 61  ? 26.139 3.545   8.241   1.00 16.05 ?  61  MET   A HE1  1 
ATOM   1487 H  HE2  . MET   A 1 61  ? 27.722 3.425   8.292   1.00 16.05 ?  61  MET   A HE2  1 
ATOM   1488 H  HE3  . MET   A 1 61  ? 26.999 4.673   8.957   1.00 16.05 ?  61  MET   A HE3  1 
ATOM   1489 N  N    . GLN   A 1 62  ? 30.251 9.064   6.169   1.00 10.53 ?  62  GLN   A N    1 
ATOM   1490 C  CA   . GLN   A 1 62  ? 30.811 9.531   4.904   1.00 10.64 ?  62  GLN   A CA   1 
ATOM   1491 C  C    . GLN   A 1 62  ? 32.282 9.907   5.047   1.00 10.51 ?  62  GLN   A C    1 
ATOM   1492 O  O    . GLN   A 1 62  ? 33.089 9.600   4.164   1.00 10.88 ?  62  GLN   A O    1 
ATOM   1493 C  CB   . GLN   A 1 62  ? 30.008 10.716  4.370   1.00 10.55 ?  62  GLN   A CB   1 
ATOM   1494 C  CG   . GLN   A 1 62  ? 30.387 11.076  2.946   1.00 10.58 ?  62  GLN   A CG   1 
ATOM   1495 C  CD   . GLN   A 1 62  ? 30.055 9.948   1.999   1.00 10.92 ?  62  GLN   A CD   1 
ATOM   1496 O  OE1  . GLN   A 1 62  ? 28.875 9.644   1.788   1.00 11.60 ?  62  GLN   A OE1  1 
ATOM   1497 N  NE2  . GLN   A 1 62  ? 31.076 9.276   1.471   1.00 11.58 ?  62  GLN   A NE2  1 
ATOM   1498 H  H    . GLN   A 1 62  ? 29.631 9.559   6.497   1.00 12.69 ?  62  GLN   A H    1 
ATOM   1499 H  HA   . GLN   A 1 62  ? 30.754 8.810   4.260   1.00 12.81 ?  62  GLN   A HA   1 
ATOM   1500 H  HB2  . GLN   A 1 62  ? 29.064 10.493  4.385   1.00 12.70 ?  62  GLN   A HB2  1 
ATOM   1501 H  HB3  . GLN   A 1 62  ? 30.175 11.490  4.932   1.00 12.70 ?  62  GLN   A HB3  1 
ATOM   1502 H  HG2  . GLN   A 1 62  ? 29.887 11.858  2.671   1.00 12.75 ?  62  GLN   A HG2  1 
ATOM   1503 H  HG3  . GLN   A 1 62  ? 31.340 11.249  2.898   1.00 12.75 ?  62  GLN   A HG3  1 
ATOM   1504 H  HE21 . GLN   A 1 62  ? 31.886 9.504   1.660   1.00 13.94 ?  62  GLN   A HE21 1 
ATOM   1505 H  HE22 . GLN   A 1 62  ? 30.930 8.617   0.939   1.00 13.94 ?  62  GLN   A HE22 1 
ATOM   1506 N  N    . VAL   A 1 63  ? 32.643 10.594  6.134   1.00 10.93 ?  63  VAL   A N    1 
ATOM   1507 C  CA   . VAL   A 1 63  ? 34.036 10.990  6.340   1.00 11.77 ?  63  VAL   A CA   1 
ATOM   1508 C  C    . VAL   A 1 63  ? 34.932 9.756   6.409   1.00 11.06 ?  63  VAL   A C    1 
ATOM   1509 O  O    . VAL   A 1 63  ? 35.985 9.686   5.758   1.00 11.61 ?  63  VAL   A O    1 
ATOM   1510 C  CB   . VAL   A 1 63  ? 34.151 11.869  7.597   1.00 13.50 ?  63  VAL   A CB   1 
ATOM   1511 C  CG1  . VAL   A 1 63  ? 35.598 12.113  7.960   1.00 15.46 ?  63  VAL   A CG1  1 
ATOM   1512 C  CG2  . VAL   A 1 63  ? 33.424 13.195  7.373   1.00 13.86 ?  63  VAL   A CG2  1 
ATOM   1513 H  H    . VAL   A 1 63  ? 32.101 10.841  6.761   1.00 13.17 ?  63  VAL   A H    1 
ATOM   1514 H  HA   . VAL   A 1 63  ? 34.319 11.518  5.583   1.00 14.17 ?  63  VAL   A HA   1 
ATOM   1515 H  HB   . VAL   A 1 63  ? 33.729 11.419  8.344   1.00 16.25 ?  63  VAL   A HB   1 
ATOM   1516 H  HG11 . VAL   A 1 63  ? 35.642 12.849  8.588   1.00 18.60 ?  63  VAL   A HG11 1 
ATOM   1517 H  HG12 . VAL   A 1 63  ? 35.962 11.310  8.360   1.00 18.60 ?  63  VAL   A HG12 1 
ATOM   1518 H  HG13 . VAL   A 1 63  ? 36.087 12.337  7.152   1.00 18.60 ?  63  VAL   A HG13 1 
ATOM   1519 H  HG21 . VAL   A 1 63  ? 33.518 13.746  8.167   1.00 16.68 ?  63  VAL   A HG21 1 
ATOM   1520 H  HG22 . VAL   A 1 63  ? 33.818 13.648  6.610   1.00 16.68 ?  63  VAL   A HG22 1 
ATOM   1521 H  HG23 . VAL   A 1 63  ? 32.486 13.018  7.204   1.00 16.68 ?  63  VAL   A HG23 1 
ATOM   1522 N  N    . GLU   A 1 64  ? 34.514 8.752   7.183   1.00 11.22 ?  64  GLU   A N    1 
ATOM   1523 C  CA   . GLU   A 1 64  ? 35.274 7.511   7.284   1.00 11.33 ?  64  GLU   A CA   1 
ATOM   1524 C  C    . GLU   A 1 64  ? 35.364 6.819   5.931   1.00 10.80 ?  64  GLU   A C    1 
ATOM   1525 O  O    . GLU   A 1 64  ? 36.414 6.275   5.556   1.00 11.48 ?  64  GLU   A O    1 
ATOM   1526 C  CB   . GLU   A 1 64  ? 34.585 6.604   8.306   1.00 11.93 ?  64  GLU   A CB   1 
ATOM   1527 C  CG   . GLU   A 1 64  ? 35.246 5.260   8.469   1.00 12.45 ?  64  GLU   A CG   1 
ATOM   1528 C  CD   . GLU   A 1 64  ? 34.370 4.260   9.192   1.00 13.10 ?  64  GLU   A CD   1 
ATOM   1529 O  OE1  . GLU   A 1 64  ? 33.131 4.352   9.056   1.00 14.27 ?  64  GLU   A OE1  1 
ATOM   1530 O  OE2  . GLU   A 1 64  ? 34.920 3.372   9.884   1.00 13.60 -1 64  GLU   A OE2  1 
ATOM   1531 H  H    . GLU   A 1 64  ? 33.790 8.761   7.653   1.00 13.51 ?  64  GLU   A H    1 
ATOM   1532 H  HA   . GLU   A 1 64  ? 36.173 7.711   7.599   1.00 13.65 ?  64  GLU   A HA   1 
ATOM   1533 H  HB2  . GLU   A 1 64  ? 34.599 7.052   9.173   1.00 14.36 ?  64  GLU   A HB2  1 
ATOM   1534 H  HB3  . GLU   A 1 64  ? 33.671 6.467   8.025   1.00 14.36 ?  64  GLU   A HB3  1 
ATOM   1535 H  HG2  . GLU   A 1 64  ? 35.456 4.895   7.595   1.00 14.99 ?  64  GLU   A HG2  1 
ATOM   1536 H  HG3  . GLU   A 1 64  ? 36.059 5.374   8.983   1.00 14.99 ?  64  GLU   A HG3  1 
ATOM   1537 N  N    . SER   A 1 65  ? 34.246 6.807   5.199   1.00 10.55 ?  65  SER   A N    1 
ATOM   1538 C  CA   . SER   A 1 65  ? 34.193 6.148   3.901   1.00 10.51 ?  65  SER   A CA   1 
ATOM   1539 C  C    . SER   A 1 65  ? 35.114 6.818   2.889   1.00 10.84 ?  65  SER   A C    1 
ATOM   1540 O  O    . SER   A 1 65  ? 35.754 6.137   2.078   1.00 11.65 ?  65  SER   A O    1 
ATOM   1541 C  CB   . SER   A 1 65  ? 32.760 6.159   3.369   1.00 10.55 ?  65  SER   A CB   1 
ATOM   1542 O  OG   . SER   A 1 65  ? 31.903 5.344   4.159   1.00 11.06 ?  65  SER   A OG   1 
ATOM   1543 H  H    . SER   A 1 65  ? 33.510 7.179   5.437   1.00 12.70 ?  65  SER   A H    1 
ATOM   1544 H  HA   . SER   A 1 65  ? 34.479 5.229   3.998   1.00 12.65 ?  65  SER   A HA   1 
ATOM   1545 H  HB2  . SER   A 1 65  ? 32.427 7.068   3.383   1.00 12.71 ?  65  SER   A HB2  1 
ATOM   1546 H  HB3  . SER   A 1 65  ? 32.768 5.823   2.459   1.00 12.71 ?  65  SER   A HB3  1 
ATOM   1547 H  HG   . SER   A 1 65  ? 31.898 5.619   4.955   1.00 13.33 ?  65  SER   A HG   1 
ATOM   1548 N  N    . ASP   A 1 66  ? 35.190 8.153   2.907   1.00 10.94 ?  66  ASP   A N    1 
ATOM   1549 C  CA   . ASP   A 1 66  ? 36.052 8.844   1.953   1.00 12.01 ?  66  ASP   A CA   1 
ATOM   1550 C  C    . ASP   A 1 66  ? 37.516 8.491   2.188   1.00 11.95 ?  66  ASP   A C    1 
ATOM   1551 O  O    . ASP   A 1 66  ? 38.286 8.317   1.235   1.00 12.91 ?  66  ASP   A O    1 
ATOM   1552 C  CB   . ASP   A 1 66  ? 35.833 10.350  2.050   1.00 13.13 ?  66  ASP   A CB   1 
ATOM   1553 C  CG   . ASP   A 1 66  ? 34.494 10.807  1.451   1.00 14.82 ?  66  ASP   A CG   1 
ATOM   1554 O  OD1  . ASP   A 1 66  ? 33.780 10.011  0.802   1.00 14.94 ?  66  ASP   A OD1  1 
ATOM   1555 O  OD2  . ASP   A 1 66  ? 34.181 12.004  1.610   1.00 17.83 -1 66  ASP   A OD2  1 
ATOM   1556 H  H    . ASP   A 1 66  ? 34.755 8.671   3.445   1.00 13.17 ?  66  ASP   A H    1 
ATOM   1557 H  HA   . ASP   A 1 66  ? 35.813 8.566   1.055   1.00 14.45 ?  66  ASP   A HA   1 
ATOM   1558 H  HB2  . ASP   A 1 66  ? 35.842 10.613  2.984   1.00 15.81 ?  66  ASP   A HB2  1 
ATOM   1559 H  HB3  . ASP   A 1 66  ? 36.546 10.804  1.573   1.00 15.81 ?  66  ASP   A HB3  1 
ATOM   1560 N  N    . ASP   A 1 67  ? 37.915 8.364   3.452   1.00 12.02 ?  67  ASP   A N    1 
ATOM   1561 C  CA   . ASP   A 1 67  ? 39.269 7.917   3.756   1.00 12.80 ?  67  ASP   A CA   1 
ATOM   1562 C  C    . ASP   A 1 67  ? 39.491 6.481   3.292   1.00 12.69 ?  67  ASP   A C    1 
ATOM   1563 O  O    . ASP   A 1 67  ? 40.552 6.159   2.743   1.00 13.56 ?  67  ASP   A O    1 
ATOM   1564 C  CB   . ASP   A 1 67  ? 39.534 8.050   5.252   1.00 14.16 ?  67  ASP   A CB   1 
ATOM   1565 C  CG   . ASP   A 1 67  ? 40.830 7.395   5.669   1.00 15.41 ?  67  ASP   A CG   1 
ATOM   1566 O  OD1  . ASP   A 1 67  ? 41.903 8.028   5.525   1.00 18.15 ?  67  ASP   A OD1  1 
ATOM   1567 O  OD2  . ASP   A 1 67  ? 40.777 6.234   6.133   1.00 15.31 -1 67  ASP   A OD2  1 
ATOM   1568 H  H    . ASP   A 1 67  ? 37.431 8.531   4.139   1.00 14.47 ?  67  ASP   A H    1 
ATOM   1569 H  HA   . ASP   A 1 67  ? 39.902 8.480   3.284   1.00 15.40 ?  67  ASP   A HA   1 
ATOM   1570 H  HB2  . ASP   A 1 67  ? 39.587 8.988   5.476   1.00 17.04 ?  67  ASP   A HB2  1 
ATOM   1571 H  HB3  . ASP   A 1 67  ? 38.812 7.625   5.739   1.00 17.04 ?  67  ASP   A HB3  1 
ATOM   1572 N  N    . TYR   A 1 68  ? 38.497 5.605   3.488   1.00 12.19 ?  68  TYR   A N    1 
ATOM   1573 C  CA   . TYR   A 1 68  ? 38.613 4.227   3.010   1.00 12.33 ?  68  TYR   A CA   1 
ATOM   1574 C  C    . TYR   A 1 68  ? 38.852 4.180   1.503   1.00 12.30 ?  68  TYR   A C    1 
ATOM   1575 O  O    . TYR   A 1 68  ? 39.726 3.446   1.028   1.00 12.80 ?  68  TYR   A O    1 
ATOM   1576 C  CB   . TYR   A 1 68  ? 37.364 3.406   3.390   1.00 12.81 ?  68  TYR   A CB   1 
ATOM   1577 C  CG   . TYR   A 1 68  ? 37.393 2.018   2.764   1.00 14.14 ?  68  TYR   A CG   1 
ATOM   1578 C  CD1  . TYR   A 1 68  ? 36.938 1.824   1.463   1.00 15.44 ?  68  TYR   A CD1  1 
ATOM   1579 C  CD2  . TYR   A 1 68  ? 37.928 0.931   3.437   1.00 15.86 ?  68  TYR   A CD2  1 
ATOM   1580 C  CE1  . TYR   A 1 68  ? 37.005 0.607   0.850   1.00 16.66 ?  68  TYR   A CE1  1 
ATOM   1581 C  CE2  . TYR   A 1 68  ? 37.992 -0.330  2.822   1.00 16.49 ?  68  TYR   A CE2  1 
ATOM   1582 C  CZ   . TYR   A 1 68  ? 37.538 -0.464  1.527   1.00 17.03 ?  68  TYR   A CZ   1 
ATOM   1583 O  OH   . TYR   A 1 68  ? 37.617 -1.675  0.895   1.00 18.12 ?  68  TYR   A OH   1 
ATOM   1584 H  H    . TYR   A 1 68  ? 37.753 5.782   3.889   1.00 14.68 ?  68  TYR   A H    1 
ATOM   1585 H  HA   . TYR   A 1 68  ? 39.374 3.814   3.442   1.00 14.85 ?  68  TYR   A HA   1 
ATOM   1586 H  HB2  . TYR   A 1 68  ? 37.332 3.302   4.353   1.00 15.42 ?  68  TYR   A HB2  1 
ATOM   1587 H  HB3  . TYR   A 1 68  ? 36.571 3.867   3.074   1.00 15.42 ?  68  TYR   A HB3  1 
ATOM   1588 H  HD1  . TYR   A 1 68  ? 36.594 2.550   0.992   1.00 18.58 ?  68  TYR   A HD1  1 
ATOM   1589 H  HD2  . TYR   A 1 68  ? 38.257 1.042   4.298   1.00 19.08 ?  68  TYR   A HD2  1 
ATOM   1590 H  HE1  . TYR   A 1 68  ? 36.693 0.504   -0.019  1.00 20.04 ?  68  TYR   A HE1  1 
ATOM   1591 H  HE2  . TYR   A 1 68  ? 38.359 -1.058  3.265   1.00 19.84 ?  68  TYR   A HE2  1 
ATOM   1592 H  HH   . TYR   A 1 68  ? 37.948 -2.247  1.417   1.00 21.79 ?  68  TYR   A HH   1 
ATOM   1593 N  N    . ILE   A 1 69  ? 38.063 4.935   0.731   1.00 11.77 ?  69  ILE   A N    1 
ATOM   1594 C  CA   . ILE   A 1 69  ? 38.200 4.924   -0.724  1.00 11.99 ?  69  ILE   A CA   1 
ATOM   1595 C  C    . ILE   A 1 69  ? 39.532 5.531   -1.154  1.00 11.93 ?  69  ILE   A C    1 
ATOM   1596 O  O    . ILE   A 1 69  ? 40.177 5.043   -2.090  1.00 12.20 ?  69  ILE   A O    1 
ATOM   1597 C  CB   . ILE   A 1 69  ? 37.001 5.633   -1.388  1.00 12.55 ?  69  ILE   A CB   1 
ATOM   1598 C  CG1  . ILE   A 1 69  ? 35.687 4.899   -1.114  1.00 13.05 ?  69  ILE   A CG1  1 
ATOM   1599 C  CG2  . ILE   A 1 69  ? 37.245 5.829   -2.890  1.00 13.79 ?  69  ILE   A CG2  1 
ATOM   1600 C  CD1  . ILE   A 1 69  ? 35.537 3.611   -1.881  1.00 13.82 ?  69  ILE   A CD1  1 
ATOM   1601 H  H    . ILE   A 1 69  ? 37.451 5.461   1.026   1.00 14.17 ?  69  ILE   A H    1 
ATOM   1602 H  HA   . ILE   A 1 69  ? 38.197 4.002   -1.022  1.00 14.43 ?  69  ILE   A HA   1 
ATOM   1603 H  HB   . ILE   A 1 69  ? 36.928 6.511   -0.989  1.00 15.11 ?  69  ILE   A HB   1 
ATOM   1604 H  HG12 . ILE   A 1 69  ? 35.643 4.687   -0.167  1.00 15.70 ?  69  ILE   A HG12 1 
ATOM   1605 H  HG13 . ILE   A 1 69  ? 34.952 5.479   -1.355  1.00 15.70 ?  69  ILE   A HG13 1 
ATOM   1606 H  HG21 . ILE   A 1 69  ? 36.399 6.040   -3.321  1.00 16.60 ?  69  ILE   A HG21 1 
ATOM   1607 H  HG22 . ILE   A 1 69  ? 37.864 6.570   -3.017  1.00 16.60 ?  69  ILE   A HG22 1 
ATOM   1608 H  HG23 . ILE   A 1 69  ? 37.614 5.020   -3.265  1.00 16.60 ?  69  ILE   A HG23 1 
ATOM   1609 H  HD11 . ILE   A 1 69  ? 34.738 3.156   -1.574  1.00 16.63 ?  69  ILE   A HD11 1 
ATOM   1610 H  HD12 . ILE   A 1 69  ? 35.457 3.814   -2.827  1.00 16.63 ?  69  ILE   A HD12 1 
ATOM   1611 H  HD13 . ILE   A 1 69  ? 36.314 3.053   -1.727  1.00 16.63 ?  69  ILE   A HD13 1 
ATOM   1612 N  N    . ALA   A 1 70  ? 39.955 6.611   -0.497  1.00 12.21 ?  70  ALA   A N    1 
ATOM   1613 C  CA   . ALA   A 1 70  ? 41.234 7.219   -0.846  1.00 13.16 ?  70  ALA   A CA   1 
ATOM   1614 C  C    . ALA   A 1 70  ? 42.382 6.234   -0.673  1.00 13.13 ?  70  ALA   A C    1 
ATOM   1615 O  O    . ALA   A 1 70  ? 43.353 6.272   -1.433  1.00 15.44 ?  70  ALA   A O    1 
ATOM   1616 C  CB   . ALA   A 1 70  ? 41.466 8.473   0.000   1.00 13.76 ?  70  ALA   A CB   1 
ATOM   1617 H  H    . ALA   A 1 70  ? 39.526 7.007   0.133   1.00 14.70 ?  70  ALA   A H    1 
ATOM   1618 H  HA   . ALA   A 1 70  ? 41.210 7.496   -1.778  1.00 15.84 ?  70  ALA   A HA   1 
ATOM   1619 H  HB1  . ALA   A 1 70  ? 42.324 8.864   -0.244  1.00 16.56 ?  70  ALA   A HB1  1 
ATOM   1620 H  HB2  . ALA   A 1 70  ? 40.756 9.109   -0.167  1.00 16.56 ?  70  ALA   A HB2  1 
ATOM   1621 H  HB3  . ALA   A 1 70  ? 41.477 8.223   0.938   1.00 16.56 ?  70  ALA   A HB3  1 
ATOM   1622 N  N    . THR   A 1 71  ? 42.279 5.336   0.302   1.00 12.95 ?  71  THR   A N    1 
ATOM   1623 C  CA   . THR   A 1 71  ? 43.332 4.357   0.551   1.00 14.43 ?  71  THR   A CA   1 
ATOM   1624 C  C    . THR   A 1 71  ? 43.211 3.132   -0.347  1.00 14.79 ?  71  THR   A C    1 
ATOM   1625 O  O    . THR   A 1 71  ? 44.225 2.625   -0.849  1.00 16.68 ?  71  THR   A O    1 
ATOM   1626 C  CB   . THR   A 1 71  ? 43.263 3.908   2.006   1.00 16.77 ?  71  THR   A CB   1 
ATOM   1627 O  OG1  . THR   A 1 71  ? 43.503 5.034   2.852   1.00 18.27 ?  71  THR   A OG1  1 
ATOM   1628 C  CG2  . THR   A 1 71  ? 44.280 2.810   2.295   1.00 18.20 ?  71  THR   A CG2  1 
ATOM   1629 H  H    . THR   A 1 71  ? 41.604 5.267   0.829   1.00 15.59 ?  71  THR   A H    1 
ATOM   1630 H  HA   . THR   A 1 71  ? 44.196 4.763   0.392   1.00 17.37 ?  71  THR   A HA   1 
ATOM   1631 H  HB   . THR   A 1 71  ? 42.377 3.547   2.187   1.00 20.17 ?  71  THR   A HB   1 
ATOM   1632 H  HG1  . THR   A 1 71  ? 42.915 5.615   2.721   1.00 21.97 ?  71  THR   A HG1  1 
ATOM   1633 H  HG21 . THR   A 1 71  ? 44.415 2.728   3.252   1.00 21.88 ?  71  THR   A HG21 1 
ATOM   1634 H  HG22 . THR   A 1 71  ? 43.971 1.958   1.949   1.00 21.88 ?  71  THR   A HG22 1 
ATOM   1635 H  HG23 . THR   A 1 71  ? 45.131 3.029   1.879   1.00 21.88 ?  71  THR   A HG23 1 
ATOM   1636 N  N    . ASN   A 1 72  ? 41.986 2.624   -0.534  1.00 13.80 ?  72  ASN   A N    1 
ATOM   1637 C  CA   . ASN   A 1 72  ? 41.768 1.301   -1.100  1.00 13.85 ?  72  ASN   A CA   1 
ATOM   1638 C  C    . ASN   A 1 72  ? 41.144 1.292   -2.483  1.00 13.88 ?  72  ASN   A C    1 
ATOM   1639 O  O    . ASN   A 1 72  ? 41.144 0.236   -3.127  1.00 15.14 ?  72  ASN   A O    1 
ATOM   1640 C  CB   . ASN   A 1 72  ? 40.875 0.482   -0.162  1.00 14.81 ?  72  ASN   A CB   1 
ATOM   1641 C  CG   . ASN   A 1 72  ? 41.485 0.326   1.206   1.00 16.10 ?  72  ASN   A CG   1 
ATOM   1642 O  OD1  . ASN   A 1 72  ? 41.035 0.931   2.177   1.00 18.06 ?  72  ASN   A OD1  1 
ATOM   1643 N  ND2  . ASN   A 1 72  ? 42.537 -0.456  1.286   1.00 16.59 ?  72  ASN   A ND2  1 
ATOM   1644 H  H    . ASN   A 1 72  ? 41.253 3.042   -0.340  1.00 16.61 ?  72  ASN   A H    1 
ATOM   1645 H  HA   . ASN   A 1 72  ? 42.620 0.854   -1.167  1.00 16.66 ?  72  ASN   A HA   1 
ATOM   1646 H  HB2  . ASN   A 1 72  ? 40.019 0.926   -0.071  1.00 17.82 ?  72  ASN   A HB2  1 
ATOM   1647 H  HB3  . ASN   A 1 72  ? 40.753 -0.403  -0.542  1.00 17.82 ?  72  ASN   A HB3  1 
ATOM   1648 H  HD21 . ASN   A 1 72  ? 42.925 -0.574  2.045   1.00 19.96 ?  72  ASN   A HD21 1 
ATOM   1649 H  HD22 . ASN   A 1 72  ? 42.834 -0.854  0.585   1.00 19.96 ?  72  ASN   A HD22 1 
ATOM   1650 N  N    . GLY   A 1 73  ? 40.587 2.404   -2.942  1.00 13.56 ?  73  GLY   A N    1 
ATOM   1651 C  CA   . GLY   A 1 73  ? 39.857 2.420   -4.182  1.00 12.99 ?  73  GLY   A CA   1 
ATOM   1652 C  C    . GLY   A 1 73  ? 38.465 1.842   -4.014  1.00 12.42 ?  73  GLY   A C    1 
ATOM   1653 O  O    . GLY   A 1 73  ? 38.076 1.388   -2.931  1.00 13.36 ?  73  GLY   A O    1 
ATOM   1654 H  H    . GLY   A 1 73  ? 40.628 3.175   -2.553  1.00 16.32 ?  73  GLY   A H    1 
ATOM   1655 H  HA2  . GLY   A 1 73  ? 39.784 3.337   -4.503  1.00 15.64 ?  73  GLY   A HA2  1 
ATOM   1656 H  HA3  . GLY   A 1 73  ? 40.335 1.901   -4.850  1.00 15.64 ?  73  GLY   A HA3  1 
ATOM   1657 N  N    . PRO   A 1 74  ? 37.689 1.857   -5.095  1.00 13.28 ?  74  PRO   A N    1 
ATOM   1658 C  CA   . PRO   A 1 74  ? 36.291 1.430   -5.012  1.00 13.42 ?  74  PRO   A CA   1 
ATOM   1659 C  C    . PRO   A 1 74  ? 36.141 -0.052  -4.696  1.00 12.48 ?  74  PRO   A C    1 
ATOM   1660 O  O    . PRO   A 1 74  ? 37.010 -0.881  -4.985  1.00 13.59 ?  74  PRO   A O    1 
ATOM   1661 C  CB   . PRO   A 1 74  ? 35.744 1.734   -6.413  1.00 15.15 ?  74  PRO   A CB   1 
ATOM   1662 C  CG   . PRO   A 1 74  ? 36.692 2.723   -7.009  1.00 17.94 ?  74  PRO   A CG   1 
ATOM   1663 C  CD   . PRO   A 1 74  ? 38.028 2.378   -6.430  1.00 15.47 ?  74  PRO   A CD   1 
ATOM   1664 H  HA   . PRO   A 1 74  ? 35.811 1.957   -4.351  1.00 16.16 ?  74  PRO   A HA   1 
ATOM   1665 H  HB2  . PRO   A 1 74  ? 35.720 0.916   -6.934  1.00 18.23 ?  74  PRO   A HB2  1 
ATOM   1666 H  HB3  . PRO   A 1 74  ? 34.853 2.115   -6.336  1.00 18.23 ?  74  PRO   A HB3  1 
ATOM   1667 H  HG2  . PRO   A 1 74  ? 36.704 2.624   -7.973  1.00 21.57 ?  74  PRO   A HG2  1 
ATOM   1668 H  HG3  . PRO   A 1 74  ? 36.434 3.620   -6.756  1.00 21.57 ?  74  PRO   A HG3  1 
ATOM   1669 H  HD2  . PRO   A 1 74  ? 38.468 1.691   -6.961  1.00 18.62 ?  74  PRO   A HD2  1 
ATOM   1670 H  HD3  . PRO   A 1 74  ? 38.581 3.176   -6.365  1.00 18.62 ?  74  PRO   A HD3  1 
ATOM   1671 N  N    . LEU   A 1 75  ? 34.999 -0.376  -4.101  1.00 11.87 ?  75  LEU   A N    1 
ATOM   1672 C  CA   . LEU   A 1 75  ? 34.600 -1.765  -3.950  1.00 11.50 ?  75  LEU   A CA   1 
ATOM   1673 C  C    . LEU   A 1 75  ? 34.218 -2.340  -5.310  1.00 11.83 ?  75  LEU   A C    1 
ATOM   1674 O  O    . LEU   A 1 75  ? 34.094 -1.624  -6.309  1.00 13.39 ?  75  LEU   A O    1 
ATOM   1675 C  CB   . LEU   A 1 75  ? 33.414 -1.888  -2.994  1.00 11.69 ?  75  LEU   A CB   1 
ATOM   1676 C  CG   . LEU   A 1 75  ? 33.621 -1.475  -1.537  1.00 13.42 ?  75  LEU   A CG   1 
ATOM   1677 C  CD1  . LEU   A 1 75  ? 32.347 -1.712  -0.740  1.00 15.49 ?  75  LEU   A CD1  1 
ATOM   1678 C  CD2  . LEU   A 1 75  ? 34.786 -2.167  -0.889  1.00 16.82 ?  75  LEU   A CD2  1 
ATOM   1679 H  H    . LEU   A 1 75  ? 34.437 0.193   -3.782  1.00 14.29 ?  75  LEU   A H    1 
ATOM   1680 H  HA   . LEU   A 1 75  ? 35.343 -2.275  -3.599  1.00 13.85 ?  75  LEU   A HA   1 
ATOM   1681 H  HB2  . LEU   A 1 75  ? 32.694 -1.345  -3.341  1.00 14.07 ?  75  LEU   A HB2  1 
ATOM   1682 H  HB3  . LEU   A 1 75  ? 33.139 -2.817  -2.986  1.00 14.07 ?  75  LEU   A HB3  1 
ATOM   1683 H  HG   . LEU   A 1 75  ? 33.805 -0.522  -1.515  1.00 16.15 ?  75  LEU   A HG   1 
ATOM   1684 H  HD11 . LEU   A 1 75  ? 32.496 -1.441  0.180   1.00 18.64 ?  75  LEU   A HD11 1 
ATOM   1685 H  HD12 . LEU   A 1 75  ? 31.631 -1.183  -1.128  1.00 18.64 ?  75  LEU   A HD12 1 
ATOM   1686 H  HD13 . LEU   A 1 75  ? 32.121 -2.653  -0.777  1.00 18.64 ?  75  LEU   A HD13 1 
ATOM   1687 H  HD21 . LEU   A 1 75  ? 34.835 -1.905  0.044   1.00 20.23 ?  75  LEU   A HD21 1 
ATOM   1688 H  HD22 . LEU   A 1 75  ? 34.668 -3.126  -0.958  1.00 20.23 ?  75  LEU   A HD22 1 
ATOM   1689 H  HD23 . LEU   A 1 75  ? 35.607 -1.905  -1.344  1.00 20.23 ?  75  LEU   A HD23 1 
ATOM   1690 N  N    . LYS   A 1 76  ? 34.037 -3.660  -5.334  1.00 12.56 ?  76  LYS   A N    1 
ATOM   1691 C  CA   . LYS   A 1 76  ? 33.438 -4.373  -6.456  1.00 13.26 ?  76  LYS   A CA   1 
ATOM   1692 C  C    . LYS   A 1 76  ? 31.928 -4.455  -6.258  1.00 11.62 ?  76  LYS   A C    1 
ATOM   1693 O  O    . LYS   A 1 76  ? 31.450 -4.576  -5.134  1.00 11.83 ?  76  LYS   A O    1 
ATOM   1694 C  CB   . LYS   A 1 76  ? 33.981 -5.813  -6.516  1.00 14.90 ?  76  LYS   A CB   1 
ATOM   1695 C  CG   . LYS   A 1 76  ? 35.495 -5.919  -6.690  1.00 16.31 ?  76  LYS   A CG   1 
ATOM   1696 C  CD   . LYS   A 1 76  ? 36.015 -7.326  -6.471  1.00 17.60 ?  76  LYS   A CD   1 
ATOM   1697 C  CE   . LYS   A 1 76  ? 37.513 -7.389  -6.670  1.00 20.06 ?  76  LYS   A CE   1 
ATOM   1698 N  NZ   . LYS   A 1 76  ? 38.047 -8.745  -6.444  1.00 21.07 ?  76  LYS   A NZ   1 
ATOM   1699 H  H    . LYS   A 1 76  ? 34.260 -4.184  -4.685  1.00 15.11 ?  76  LYS   A H    1 
ATOM   1700 H  HA   . LYS   A 1 76  ? 33.634 -3.918  -7.290  1.00 15.96 ?  76  LYS   A HA   1 
ATOM   1701 H  HB2  . LYS   A 1 76  ? 33.747 -6.265  -5.692  1.00 17.93 ?  76  LYS   A HB2  1 
ATOM   1702 H  HB3  . LYS   A 1 76  ? 33.567 -6.266  -7.267  1.00 17.93 ?  76  LYS   A HB3  1 
ATOM   1703 H  HG2  . LYS   A 1 76  ? 35.729 -5.648  -7.592  1.00 19.62 ?  76  LYS   A HG2  1 
ATOM   1704 H  HG3  . LYS   A 1 76  ? 35.928 -5.335  -6.047  1.00 19.62 ?  76  LYS   A HG3  1 
ATOM   1705 H  HD2  . LYS   A 1 76  ? 35.811 -7.606  -5.564  1.00 21.16 ?  76  LYS   A HD2  1 
ATOM   1706 H  HD3  . LYS   A 1 76  ? 35.594 -7.926  -7.109  1.00 21.16 ?  76  LYS   A HD3  1 
ATOM   1707 H  HE2  . LYS   A 1 76  ? 37.722 -7.129  -7.579  1.00 24.12 ?  76  LYS   A HE2  1 
ATOM   1708 H  HE3  . LYS   A 1 76  ? 37.940 -6.790  -6.040  1.00 24.12 ?  76  LYS   A HE3  1 
ATOM   1709 H  HZ1  . LYS   A 1 76  ? 38.927 -8.757  -6.569  1.00 25.33 ?  76  LYS   A HZ1  1 
ATOM   1710 H  HZ2  . LYS   A 1 76  ? 37.870 -9.016  -5.613  1.00 25.33 ?  76  LYS   A HZ2  1 
ATOM   1711 H  HZ3  . LYS   A 1 76  ? 37.671 -9.325  -7.015  1.00 25.33 ?  76  LYS   A HZ3  1 
ATOM   1712 N  N    . VAL   A 1 77  ? 31.174 -4.421  -7.361  1.00 12.37 ?  77  VAL   A N    1 
ATOM   1713 C  CA   . VAL   A 1 77  ? 29.766 -4.810  -7.274  1.00 12.19 ?  77  VAL   A CA   1 
ATOM   1714 C  C    . VAL   A 1 77  ? 29.705 -6.264  -6.831  1.00 11.74 ?  77  VAL   A C    1 
ATOM   1715 O  O    . VAL   A 1 77  ? 30.361 -7.133  -7.417  1.00 12.32 ?  77  VAL   A O    1 
ATOM   1716 C  CB   . VAL   A 1 77  ? 29.042 -4.604  -8.612  1.00 13.34 ?  77  VAL   A CB   1 
ATOM   1717 C  CG1  . VAL   A 1 77  ? 27.592 -5.042  -8.491  1.00 13.89 ?  77  VAL   A CG1  1 
ATOM   1718 C  CG2  . VAL   A 1 77  ? 29.123 -3.153  -9.049  1.00 14.95 ?  77  VAL   A CG2  1 
ATOM   1719 H  H    . VAL   A 1 77  ? 31.448 -4.178  -8.139  1.00 14.90 ?  77  VAL   A H    1 
ATOM   1720 H  HA   . VAL   A 1 77  ? 29.327 -4.267  -6.603  1.00 14.68 ?  77  VAL   A HA   1 
ATOM   1721 H  HB   . VAL   A 1 77  ? 29.470 -5.147  -9.293  1.00 16.05 ?  77  VAL   A HB   1 
ATOM   1722 H  HG11 . VAL   A 1 77  ? 27.110 -4.737  -9.273  1.00 16.72 ?  77  VAL   A HG11 1 
ATOM   1723 H  HG12 . VAL   A 1 77  ? 27.557 -6.006  -8.432  1.00 16.72 ?  77  VAL   A HG12 1 
ATOM   1724 H  HG13 . VAL   A 1 77  ? 27.214 -4.642  -7.692  1.00 16.72 ?  77  VAL   A HG13 1 
ATOM   1725 H  HG21 . VAL   A 1 77  ? 28.617 -3.043  -9.869  1.00 17.99 ?  77  VAL   A HG21 1 
ATOM   1726 H  HG22 . VAL   A 1 77  ? 28.748 -2.593  -8.351  1.00 17.99 ?  77  VAL   A HG22 1 
ATOM   1727 H  HG23 . VAL   A 1 77  ? 30.052 -2.917  -9.199  1.00 17.99 ?  77  VAL   A HG23 1 
ATOM   1728 N  N    . GLY   A 1 78  ? 28.927 -6.535  -5.782  1.00 11.37 ?  78  GLY   A N    1 
ATOM   1729 C  CA   . GLY   A 1 78  ? 28.910 -7.829  -5.129  1.00 11.81 ?  78  GLY   A CA   1 
ATOM   1730 C  C    . GLY   A 1 78  ? 29.824 -7.921  -3.928  1.00 11.26 ?  78  GLY   A C    1 
ATOM   1731 O  O    . GLY   A 1 78  ? 29.765 -8.921  -3.198  1.00 12.10 ?  78  GLY   A O    1 
ATOM   1732 H  H    . GLY   A 1 78  ? 28.389 -5.961  -5.430  1.00 13.70 ?  78  GLY   A H    1 
ATOM   1733 H  HA2  . GLY   A 1 78  ? 28.006 -8.020  -4.843  1.00 14.21 ?  78  GLY   A HA2  1 
ATOM   1734 H  HA3  . GLY   A 1 78  ? 29.177 -8.506  -5.770  1.00 14.21 ?  78  GLY   A HA3  1 
ATOM   1735 N  N    . GLY   A 1 79  ? 30.676 -6.915  -3.710  1.00 11.14 ?  79  GLY   A N    1 
ATOM   1736 C  CA   . GLY   A 1 79  ? 31.639 -6.923  -2.634  1.00 11.67 ?  79  GLY   A CA   1 
ATOM   1737 C  C    . GLY   A 1 79  ? 31.189 -6.128  -1.418  1.00 11.05 ?  79  GLY   A C    1 
ATOM   1738 O  O    . GLY   A 1 79  ? 30.072 -5.620  -1.340  1.00 11.50 ?  79  GLY   A O    1 
ATOM   1739 H  H    . GLY   A 1 79  ? 30.710 -6.200  -4.189  1.00 13.42 ?  79  GLY   A H    1 
ATOM   1740 H  HA2  . GLY   A 1 79  ? 31.801 -7.846  -2.360  1.00 14.05 ?  79  GLY   A HA2  1 
ATOM   1741 H  HA3  . GLY   A 1 79  ? 32.477 -6.554  -2.948  1.00 14.05 ?  79  GLY   A HA3  1 
ATOM   1742 N  N    . SER   A 1 80  ? 32.094 -6.038  -0.446  1.00 11.57 ?  80  SER   A N    1 
ATOM   1743 C  CA   . SER   A 1 80  ? 31.779 -5.406  0.823   1.00 11.01 ?  80  SER   A CA   1 
ATOM   1744 C  C    . SER   A 1 80  ? 33.052 -4.950  1.519   1.00 10.83 ?  80  SER   A C    1 
ATOM   1745 O  O    . SER   A 1 80  ? 34.165 -5.378  1.190   1.00 12.60 ?  80  SER   A O    1 
ATOM   1746 C  CB   . SER   A 1 80  ? 31.025 -6.368  1.750   1.00 12.35 ?  80  SER   A CB   1 
ATOM   1747 O  OG   . SER   A 1 80  ? 31.865 -7.414  2.215   1.00 13.86 ?  80  SER   A OG   1 
ATOM   1748 H  H    . SER   A 1 80  ? 32.904 -6.321  -0.507  1.00 13.93 ?  80  SER   A H    1 
ATOM   1749 H  HA   . SER   A 1 80  ? 31.223 -4.625  0.648   1.00 13.27 ?  80  SER   A HA   1 
ATOM   1750 H  HB2  . SER   A 1 80  ? 30.693 -5.866  2.509   1.00 14.87 ?  80  SER   A HB2  1 
ATOM   1751 H  HB3  . SER   A 1 80  ? 30.282 -6.750  1.255   1.00 14.87 ?  80  SER   A HB3  1 
ATOM   1752 H  HG   . SER   A 1 80  ? 32.159 -7.848  1.555   1.00 16.69 ?  80  SER   A HG   1 
ATOM   1753 N  N    . CYS   A 1 81  ? 32.862 -4.108  2.531   1.00 10.77 ?  81  CYS   A N    1 
ATOM   1754 C  CA   . CYS   A 1 81  ? 33.916 -3.820  3.491   1.00 10.91 ?  81  CYS   A CA   1 
ATOM   1755 C  C    . CYS   A 1 81  ? 33.273 -3.586  4.852   1.00 10.77 ?  81  CYS   A C    1 
ATOM   1756 O  O    . CYS   A 1 81  ? 32.108 -3.184  4.942   1.00 12.14 ?  81  CYS   A O    1 
ATOM   1757 C  CB   . CYS   A 1 81  ? 34.788 -2.630  3.065   1.00 11.68 ?  81  CYS   A CB   1 
ATOM   1758 S  SG   . CYS   A 1 81  ? 33.889 -1.053  3.088   1.00 11.80 ?  81  CYS   A SG   1 
ATOM   1759 H  H    . CYS   A 1 81  ? 32.122 -3.691  2.688   1.00 12.97 ?  81  CYS   A H    1 
ATOM   1760 H  HA   . CYS   A 1 81  ? 34.491 -4.594  3.564   1.00 13.13 ?  81  CYS   A HA   1 
ATOM   1761 H  HB2  . CYS   A 1 81  ? 35.545 -2.560  3.668   1.00 14.06 ?  81  CYS   A HB2  1 
ATOM   1762 H  HB3  . CYS   A 1 81  ? 35.108 -2.784  2.157   1.00 14.06 ?  81  CYS   A HB3  1 
ATOM   1763 H  HG   . CYS   A 1 81  ? 34.631 -0.174  2.743   1.00 14.21 ?  81  CYS   A HG   1 
ATOM   1764 N  N    . VAL   A 1 82  ? 34.045 -3.845  5.906   1.00 11.26 ?  82  VAL   A N    1 
ATOM   1765 C  CA   . VAL   A 1 82  ? 33.624 -3.602  7.278   1.00 11.85 ?  82  VAL   A CA   1 
ATOM   1766 C  C    . VAL   A 1 82  ? 34.221 -2.286  7.746   1.00 12.12 ?  82  VAL   A C    1 
ATOM   1767 O  O    . VAL   A 1 82  ? 35.446 -2.107  7.733   1.00 12.72 ?  82  VAL   A O    1 
ATOM   1768 C  CB   . VAL   A 1 82  ? 34.050 -4.740  8.217   1.00 13.26 ?  82  VAL   A CB   1 
ATOM   1769 C  CG1  . VAL   A 1 82  ? 33.610 -4.439  9.641   1.00 14.68 ?  82  VAL   A CG1  1 
ATOM   1770 C  CG2  . VAL   A 1 82  ? 33.486 -6.071  7.749   1.00 14.34 ?  82  VAL   A CG2  1 
ATOM   1771 H  H    . VAL   A 1 82  ? 34.841 -4.184  5.844   1.00 13.57 ?  82  VAL   A H    1 
ATOM   1772 H  HA   . VAL   A 1 82  ? 32.657 -3.525  7.304   1.00 14.27 ?  82  VAL   A HA   1 
ATOM   1773 H  HB   . VAL   A 1 82  ? 35.016 -4.803  8.213   1.00 15.96 ?  82  VAL   A HB   1 
ATOM   1774 H  HG11 . VAL   A 1 82  ? 33.695 -5.245  10.174  1.00 17.67 ?  82  VAL   A HG11 1 
ATOM   1775 H  HG12 . VAL   A 1 82  ? 34.172 -3.740  10.011  1.00 17.67 ?  82  VAL   A HG12 1 
ATOM   1776 H  HG13 . VAL   A 1 82  ? 32.682 -4.148  9.633   1.00 17.67 ?  82  VAL   A HG13 1 
ATOM   1777 H  HG21 . VAL   A 1 82  ? 33.736 -6.760  8.384   1.00 17.26 ?  82  VAL   A HG21 1 
ATOM   1778 H  HG22 . VAL   A 1 82  ? 32.518 -6.005  7.699   1.00 17.26 ?  82  VAL   A HG22 1 
ATOM   1779 H  HG23 . VAL   A 1 82  ? 33.848 -6.278  6.874   1.00 17.26 ?  82  VAL   A HG23 1 
ATOM   1780 N  N    . LEU   A 1 83  ? 33.361 -1.364  8.161   1.00 11.61 ?  83  LEU   A N    1 
ATOM   1781 C  CA   . LEU   A 1 83  ? 33.779 -0.098  8.742   1.00 11.26 ?  83  LEU   A CA   1 
ATOM   1782 C  C    . LEU   A 1 83  ? 33.066 0.082   10.078  1.00 11.32 ?  83  LEU   A C    1 
ATOM   1783 O  O    . LEU   A 1 83  ? 32.345 -0.805  10.547  1.00 12.14 ?  83  LEU   A O    1 
ATOM   1784 C  CB   . LEU   A 1 83  ? 33.529 1.062   7.765   1.00 11.65 ?  83  LEU   A CB   1 
ATOM   1785 C  CG   . LEU   A 1 83  ? 34.421 1.064   6.519   1.00 12.48 ?  83  LEU   A CG   1 
ATOM   1786 C  CD1  . LEU   A 1 83  ? 33.985 2.111   5.513   1.00 13.02 ?  83  LEU   A CD1  1 
ATOM   1787 C  CD2  . LEU   A 1 83  ? 35.894 1.275   6.899   1.00 13.31 ?  83  LEU   A CD2  1 
ATOM   1788 H  H    . LEU   A 1 83  ? 32.508 -1.449  8.110   1.00 13.98 ?  83  LEU   A H    1 
ATOM   1789 H  HA   . LEU   A 1 83  ? 34.732 -0.127  8.918   1.00 13.56 ?  83  LEU   A HA   1 
ATOM   1790 H  HB2  . LEU   A 1 83  ? 32.612 1.023   7.454   1.00 14.03 ?  83  LEU   A HB2  1 
ATOM   1791 H  HB3  . LEU   A 1 83  ? 33.679 1.903   8.224   1.00 14.03 ?  83  LEU   A HB3  1 
ATOM   1792 H  HG   . LEU   A 1 83  ? 34.358 0.200   6.089   1.00 15.03 ?  83  LEU   A HG   1 
ATOM   1793 H  HD11 . LEU   A 1 83  ? 34.574 2.074   4.741   1.00 15.68 ?  83  LEU   A HD11 1 
ATOM   1794 H  HD12 . LEU   A 1 83  ? 33.074 1.921   5.241   1.00 15.68 ?  83  LEU   A HD12 1 
ATOM   1795 H  HD13 . LEU   A 1 83  ? 34.034 2.987   5.923   1.00 15.68 ?  83  LEU   A HD13 1 
ATOM   1796 H  HD21 . LEU   A 1 83  ? 36.414 1.430   6.091   1.00 16.02 ?  83  LEU   A HD21 1 
ATOM   1797 H  HD22 . LEU   A 1 83  ? 35.966 2.045   7.485   1.00 16.02 ?  83  LEU   A HD22 1 
ATOM   1798 H  HD23 . LEU   A 1 83  ? 36.225 0.483   7.352   1.00 16.02 ?  83  LEU   A HD23 1 
ATOM   1799 N  N    . SER   A 1 84  ? 33.280 1.234   10.707  1.00 12.17 ?  84  SER   A N    1 
ATOM   1800 C  CA   . SER   A 1 84  ? 32.633 1.495   11.981  1.00 12.07 ?  84  SER   A CA   1 
ATOM   1801 C  C    . SER   A 1 84  ? 31.114 1.581   11.835  1.00 12.12 ?  84  SER   A C    1 
ATOM   1802 O  O    . SER   A 1 84  ? 30.585 2.047   10.825  1.00 12.31 ?  84  SER   A O    1 
ATOM   1803 C  CB   . SER   A 1 84  ? 33.131 2.818   12.555  1.00 13.37 ?  84  SER   A CB   1 
ATOM   1804 O  OG   . SER   A 1 84  ? 32.512 3.087   13.796  1.00 14.22 ?  84  SER   A OG   1 
ATOM   1805 H  H    . SER   A 1 84  ? 33.780 1.877   10.412  1.00 14.65 ?  84  SER   A H    1 
ATOM   1806 H  HA   . SER   A 1 84  ? 32.851 0.786   12.600  1.00 14.54 ?  84  SER   A HA   1 
ATOM   1807 H  HB2  . SER   A 1 84  ? 34.093 2.770   12.681  1.00 16.10 ?  84  SER   A HB2  1 
ATOM   1808 H  HB3  . SER   A 1 84  ? 32.918 3.536   11.934  1.00 16.10 ?  84  SER   A HB3  1 
ATOM   1809 H  HG   . SER   A 1 84  ? 32.794 3.814   14.107  1.00 17.12 ?  84  SER   A HG   1 
ATOM   1810 N  N    . GLY   A 1 85  ? 30.407 1.161   12.882  1.00 13.19 ?  85  GLY   A N    1 
ATOM   1811 C  CA   . GLY   A 1 85  ? 28.982 1.395   12.977  1.00 13.98 ?  85  GLY   A CA   1 
ATOM   1812 C  C    . GLY   A 1 85  ? 28.613 2.713   13.623  1.00 13.28 ?  85  GLY   A C    1 
ATOM   1813 O  O    . GLY   A 1 85  ? 27.421 3.027   13.737  1.00 13.84 ?  85  GLY   A O    1 
ATOM   1814 H  H    . GLY   A 1 85  ? 30.742 0.737   13.554  1.00 15.87 ?  85  GLY   A H    1 
ATOM   1815 H  HA2  . GLY   A 1 85  ? 28.602 1.374   12.085  1.00 16.83 ?  85  GLY   A HA2  1 
ATOM   1816 H  HA3  . GLY   A 1 85  ? 28.580 0.685   13.494  1.00 16.83 ?  85  GLY   A HA3  1 
ATOM   1817 N  N    . HIS   A 1 86  ? 29.600 3.490   14.060  1.00 12.77 ?  86  HIS   A N    1 
ATOM   1818 C  CA   . HIS   A 1 86  ? 29.376 4.827   14.621  1.00 13.43 ?  86  HIS   A CA   1 
ATOM   1819 C  C    . HIS   A 1 86  ? 28.398 4.710   15.783  1.00 14.26 ?  86  HIS   A C    1 
ATOM   1820 O  O    . HIS   A 1 86  ? 28.587 3.838   16.646  1.00 15.59 ?  86  HIS   A O    1 
ATOM   1821 C  CB   . HIS   A 1 86  ? 28.994 5.796   13.509  1.00 13.42 ?  86  HIS   A CB   1 
ATOM   1822 C  CG   . HIS   A 1 86  ? 30.051 5.899   12.467  1.00 13.42 ?  86  HIS   A CG   1 
ATOM   1823 N  ND1  . HIS   A 1 86  ? 31.140 6.735   12.597  1.00 14.47 ?  86  HIS   A ND1  1 
ATOM   1824 C  CD2  . HIS   A 1 86  ? 30.235 5.209   11.318  1.00 13.17 ?  86  HIS   A CD2  1 
ATOM   1825 C  CE1  . HIS   A 1 86  ? 31.932 6.572   11.553  1.00 14.27 ?  86  HIS   A CE1  1 
ATOM   1826 N  NE2  . HIS   A 1 86  ? 31.414 5.645   10.770  1.00 13.65 ?  86  HIS   A NE2  1 
ATOM   1827 H  H    . HIS   A 1 86  ? 30.423 3.264   14.050  1.00 15.37 ?  86  HIS   A H    1 
ATOM   1828 H  HA   . HIS   A 1 86  ? 30.212 5.144   14.987  1.00 16.17 ?  86  HIS   A HA   1 
ATOM   1829 H  HB2  . HIS   A 1 86  ? 28.174 5.498   13.080  1.00 16.15 ?  86  HIS   A HB2  1 
ATOM   1830 H  HB3  . HIS   A 1 86  ? 28.861 6.686   13.882  1.00 16.15 ?  86  HIS   A HB3  1 
ATOM   1831 H  HD2  . HIS   A 1 86  ? 29.671 4.548   10.967  1.00 15.85 ?  86  HIS   A HD2  1 
ATOM   1832 H  HE1  . HIS   A 1 86  ? 32.722 7.033   11.383  1.00 17.18 ?  86  HIS   A HE1  1 
ATOM   1833 H  HE2  . HIS   A 1 86  ? 31.747 5.370   10.015  1.00 16.42 ?  86  HIS   A HE2  1 
ATOM   1834 N  N    . ASN   A 1 87  ? 27.390 5.567   15.861  1.00 15.26 ?  87  ASN   A N    1 
ATOM   1835 C  CA   . ASN   A 1 87  ? 26.410 5.552   16.930  1.00 16.22 ?  87  ASN   A CA   1 
ATOM   1836 C  C    . ASN   A 1 87  ? 25.288 4.554   16.695  1.00 17.37 ?  87  ASN   A C    1 
ATOM   1837 O  O    . ASN   A 1 87  ? 24.374 4.481   17.517  1.00 19.53 ?  87  ASN   A O    1 
ATOM   1838 C  CB   . ASN   A 1 87  ? 25.812 6.958   17.092  1.00 17.14 ?  87  ASN   A CB   1 
ATOM   1839 C  CG   . ASN   A 1 87  ? 25.303 7.536   15.775  1.00 17.69 ?  87  ASN   A CG   1 
ATOM   1840 O  OD1  . ASN   A 1 87  ? 25.944 7.414   14.736  1.00 18.20 ?  87  ASN   A OD1  1 
ATOM   1841 N  ND2  . ASN   A 1 87  ? 24.143 8.166   15.820  1.00 18.97 ?  87  ASN   A ND2  1 
ATOM   1842 H  H    . ASN   A 1 87  ? 27.247 6.188   15.288  1.00 18.36 ?  87  ASN   A H    1 
ATOM   1843 H  HA   . ASN   A 1 87  ? 26.840 5.312   17.768  1.00 19.51 ?  87  ASN   A HA   1 
ATOM   1844 H  HB2  . ASN   A 1 87  ? 25.064 6.918   17.716  1.00 20.62 ?  87  ASN   A HB2  1 
ATOM   1845 H  HB3  . ASN   A 1 87  ? 26.495 7.552   17.439  1.00 20.62 ?  87  ASN   A HB3  1 
ATOM   1846 H  HD21 . ASN   A 1 87  ? 23.818 8.504   15.102  1.00 22.82 ?  87  ASN   A HD21 1 
ATOM   1847 H  HD22 . ASN   A 1 87  ? 23.720 8.242   16.565  1.00 22.82 ?  87  ASN   A HD22 1 
ATOM   1848 N  N    . LEU   A 1 88  ? 25.337 3.781   15.615  1.00 16.08 ?  88  LEU   A N    1 
ATOM   1849 C  CA   . LEU   A 1 88  ? 24.223 2.919   15.228  1.00 15.76 ?  88  LEU   A CA   1 
ATOM   1850 C  C    . LEU   A 1 88  ? 24.440 1.440   15.521  1.00 15.44 ?  88  LEU   A C    1 
ATOM   1851 O  O    . LEU   A 1 88  ? 23.461 0.703   15.682  1.00 16.71 ?  88  LEU   A O    1 
ATOM   1852 C  CB   . LEU   A 1 88  ? 23.952 3.075   13.731  1.00 16.09 ?  88  LEU   A CB   1 
ATOM   1853 C  CG   . LEU   A 1 88  ? 23.658 4.494   13.245  1.00 17.57 ?  88  LEU   A CG   1 
ATOM   1854 C  CD1  . LEU   A 1 88  ? 23.499 4.510   11.735  1.00 18.17 ?  88  LEU   A CD1  1 
ATOM   1855 C  CD2  . LEU   A 1 88  ? 22.416 5.056   13.925  1.00 19.35 ?  88  LEU   A CD2  1 
ATOM   1856 H  H    . LEU   A 1 88  ? 26.013 3.736   15.094  1.00 19.35 ?  88  LEU   A H    1 
ATOM   1857 H  HA   . LEU   A 1 88  ? 23.430 3.202   15.707  1.00 18.96 ?  88  LEU   A HA   1 
ATOM   1858 H  HB2  . LEU   A 1 88  ? 24.724 2.761   13.244  1.00 19.36 ?  88  LEU   A HB2  1 
ATOM   1859 H  HB3  . LEU   A 1 88  ? 23.180 2.532   13.506  1.00 19.36 ?  88  LEU   A HB3  1 
ATOM   1860 H  HG   . LEU   A 1 88  ? 24.405 5.067   13.471  1.00 21.13 ?  88  LEU   A HG   1 
ATOM   1861 H  HD11 . LEU   A 1 88  ? 23.323 5.420   11.446  1.00 21.85 ?  88  LEU   A HD11 1 
ATOM   1862 H  HD12 . LEU   A 1 88  ? 24.317 4.186   11.329  1.00 21.85 ?  88  LEU   A HD12 1 
ATOM   1863 H  HD13 . LEU   A 1 88  ? 22.756 3.937   11.489  1.00 21.85 ?  88  LEU   A HD13 1 
ATOM   1864 H  HD21 . LEU   A 1 88  ? 22.197 5.911   13.522  1.00 23.27 ?  88  LEU   A HD21 1 
ATOM   1865 H  HD22 . LEU   A 1 88  ? 21.683 4.434   13.804  1.00 23.27 ?  88  LEU   A HD22 1 
ATOM   1866 H  HD23 . LEU   A 1 88  ? 22.602 5.173   14.869  1.00 23.27 ?  88  LEU   A HD23 1 
ATOM   1867 N  N    . ALA   A 1 89  ? 25.689 0.994   15.576  1.00 14.99 ?  89  ALA   A N    1 
ATOM   1868 C  CA   . ALA   A 1 89  ? 26.035 -0.417  15.661  1.00 14.82 ?  89  ALA   A CA   1 
ATOM   1869 C  C    . ALA   A 1 89  ? 27.521 -0.485  15.973  1.00 15.18 ?  89  ALA   A C    1 
ATOM   1870 O  O    . ALA   A 1 89  ? 28.238 0.509   15.853  1.00 15.63 ?  89  ALA   A O    1 
ATOM   1871 C  CB   . ALA   A 1 89  ? 25.751 -1.116  14.334  1.00 14.27 ?  89  ALA   A CB   1 
ATOM   1872 H  H    . ALA   A 1 89  ? 26.375 1.511   15.566  1.00 18.04 ?  89  ALA   A H    1 
ATOM   1873 H  HA   . ALA   A 1 89  ? 25.529 -0.846  16.373  1.00 17.83 ?  89  ALA   A HA   1 
ATOM   1874 H  HB1  . ALA   A 1 89  ? 25.998 -2.051  14.411  1.00 17.17 ?  89  ALA   A HB1  1 
ATOM   1875 H  HB2  . ALA   A 1 89  ? 24.804 -1.042  14.129  1.00 17.17 ?  89  ALA   A HB2  1 
ATOM   1876 H  HB3  . ALA   A 1 89  ? 26.273 -0.693  13.636  1.00 17.17 ?  89  ALA   A HB3  1 
ATOM   1877 N  N    . LYS   A 1 90  ? 27.994 -1.662  16.365  1.00 15.74 ?  90  LYS   A N    1 
ATOM   1878 C  CA   . LYS   A 1 90  ? 29.438 -1.813  16.512  1.00 16.61 ?  90  LYS   A CA   1 
ATOM   1879 C  C    . LYS   A 1 90  ? 30.137 -1.629  15.168  1.00 15.37 ?  90  LYS   A C    1 
ATOM   1880 O  O    . LYS   A 1 90  ? 31.075 -0.823  15.040  1.00 16.84 ?  90  LYS   A O    1 
ATOM   1881 C  CB   . LYS   A 1 90  ? 29.776 -3.169  17.132  1.00 19.65 ?  90  LYS   A CB   1 
ATOM   1882 C  CG   . LYS   A 1 90  ? 31.254 -3.318  17.463  1.00 25.07 ?  90  LYS   A CG   1 
ATOM   1883 C  CD   . LYS   A 1 90  ? 31.503 -4.546  18.320  1.00 30.80 ?  90  LYS   A CD   1 
ATOM   1884 C  CE   . LYS   A 1 90  ? 32.920 -4.572  18.871  1.00 35.13 ?  90  LYS   A CE   1 
ATOM   1885 N  NZ   . LYS   A 1 90  ? 33.922 -5.011  17.862  1.00 37.54 ?  90  LYS   A NZ   1 
ATOM   1886 H  H    . LYS   A 1 90  ? 27.522 -2.354  16.551  1.00 18.93 ?  90  LYS   A H    1 
ATOM   1887 H  HA   . LYS   A 1 90  ? 29.765 -1.123  17.107  1.00 19.99 ?  90  LYS   A HA   1 
ATOM   1888 H  HB2  . LYS   A 1 90  ? 29.271 -3.272  17.956  1.00 23.63 ?  90  LYS   A HB2  1 
ATOM   1889 H  HB3  . LYS   A 1 90  ? 29.534 -3.872  16.509  1.00 23.63 ?  90  LYS   A HB3  1 
ATOM   1890 H  HG2  . LYS   A 1 90  ? 31.759 -3.410  16.640  1.00 30.13 ?  90  LYS   A HG2  1 
ATOM   1891 H  HG3  . LYS   A 1 90  ? 31.552 -2.535  17.955  1.00 30.13 ?  90  LYS   A HG3  1 
ATOM   1892 H  HD2  . LYS   A 1 90  ? 30.886 -4.545  19.069  1.00 37.01 ?  90  LYS   A HD2  1 
ATOM   1893 H  HD3  . LYS   A 1 90  ? 31.372 -5.343  17.781  1.00 37.01 ?  90  LYS   A HD3  1 
ATOM   1894 H  HE2  . LYS   A 1 90  ? 33.161 -3.678  19.162  1.00 42.20 ?  90  LYS   A HE2  1 
ATOM   1895 H  HE3  . LYS   A 1 90  ? 32.958 -5.186  19.619  1.00 42.20 ?  90  LYS   A HE3  1 
ATOM   1896 H  HZ1  . LYS   A 1 90  ? 33.714 -5.822  17.559  1.00 45.10 ?  90  LYS   A HZ1  1 
ATOM   1897 H  HZ2  . LYS   A 1 90  ? 33.937 -4.442  17.179  1.00 45.10 ?  90  LYS   A HZ2  1 
ATOM   1898 H  HZ3  . LYS   A 1 90  ? 34.732 -5.041  18.231  1.00 45.10 ?  90  LYS   A HZ3  1 
ATOM   1899 N  N    . HIS   A 1 91  ? 29.670 -2.351  14.149  1.00 13.49 ?  91  HIS   A N    1 
ATOM   1900 C  CA   . HIS   A 1 91  ? 30.244 -2.337  12.817  1.00 13.17 ?  91  HIS   A CA   1 
ATOM   1901 C  C    . HIS   A 1 91  ? 29.159 -2.061  11.794  1.00 11.79 ?  91  HIS   A C    1 
ATOM   1902 O  O    . HIS   A 1 91  ? 27.992 -2.418  11.990  1.00 12.72 ?  91  HIS   A O    1 
ATOM   1903 C  CB   . HIS   A 1 91  ? 30.843 -3.705  12.454  1.00 15.78 ?  91  HIS   A CB   1 
ATOM   1904 C  CG   . HIS   A 1 91  ? 31.833 -4.220  13.447  1.00 19.86 ?  91  HIS   A CG   1 
ATOM   1905 N  ND1  . HIS   A 1 91  ? 33.115 -3.725  13.547  1.00 22.19 ?  91  HIS   A ND1  1 
ATOM   1906 C  CD2  . HIS   A 1 91  ? 31.736 -5.201  14.374  1.00 21.64 ?  91  HIS   A CD2  1 
ATOM   1907 C  CE1  . HIS   A 1 91  ? 33.764 -4.375  14.498  1.00 23.07 ?  91  HIS   A CE1  1 
ATOM   1908 N  NE2  . HIS   A 1 91  ? 32.949 -5.278  15.014  1.00 23.05 ?  91  HIS   A NE2  1 
ATOM   1909 H  H    . HIS   A 1 91  ? 28.992 -2.894  14.218  1.00 16.24 ?  91  HIS   A H    1 
ATOM   1910 H  HA   . HIS   A 1 91  ? 30.931 -1.662  12.754  1.00 15.85 ?  91  HIS   A HA   1 
ATOM   1911 H  HB2  . HIS   A 1 91  ? 30.127 -4.358  12.390  1.00 18.98 ?  91  HIS   A HB2  1 
ATOM   1912 H  HB3  . HIS   A 1 91  ? 31.295 -3.632  11.598  1.00 18.98 ?  91  HIS   A HB3  1 
ATOM   1913 H  HD1  . HIS   A 1 91  ? 33.444 -3.091  13.064  1.00 26.67 ?  91  HIS   A HD1  1 
ATOM   1914 H  HD2  . HIS   A 1 91  ? 30.993 -5.727  14.548  1.00 26.02 ?  91  HIS   A HD2  1 
ATOM   1915 H  HE1  . HIS   A 1 91  ? 34.648 -4.219  14.757  1.00 27.73 ?  91  HIS   A HE1  1 
ATOM   1916 N  N    . CYS   A 1 92  ? 29.564 -1.460  10.679  1.00 11.58 ?  92  CYS   A N    1 
ATOM   1917 C  CA   . CYS   A 1 92  ? 28.733 -1.389  9.485   1.00 11.36 ?  92  CYS   A CA   1 
ATOM   1918 C  C    . CYS   A 1 92  ? 29.380 -2.212  8.381   1.00 11.02 ?  92  CYS   A C    1 
ATOM   1919 O  O    . CYS   A 1 92  ? 30.538 -1.963  8.009   1.00 11.88 ?  92  CYS   A O    1 
ATOM   1920 C  CB   . CYS   A 1 92  ? 28.522 0.050   9.016   1.00 11.74 ?  92  CYS   A CB   1 
ATOM   1921 S  SG   . CYS   A 1 92  ? 27.501 0.157   7.515   1.00 11.19 ?  92  CYS   A SG   1 
ATOM   1922 H  H    . CYS   A 1 92  ? 30.334 -1.074  10.588  1.00 13.95 ?  92  CYS   A H    1 
ATOM   1923 H  HA   . CYS   A 1 92  ? 27.866 -1.769  9.679   1.00 13.68 ?  92  CYS   A HA   1 
ATOM   1924 H  HB2  . CYS   A 1 92  ? 28.076 0.555   9.716   1.00 14.14 ?  92  CYS   A HB2  1 
ATOM   1925 H  HB3  . CYS   A 1 92  ? 29.383 0.454   8.817   1.00 14.14 ?  92  CYS   A HB3  1 
ATOM   1926 H  HG   . CYS   A 1 92  ? 27.360 1.308   7.215   1.00 13.47 ?  92  CYS   A HG   1 
ATOM   1927 N  N    . LEU   A 1 93  ? 28.643 -3.200  7.882   1.00 10.90 ?  93  LEU   A N    1 
ATOM   1928 C  CA   . LEU   A 1 93  ? 29.037 -3.955  6.699   1.00 10.54 ?  93  LEU   A CA   1 
ATOM   1929 C  C    . LEU   A 1 93  ? 28.440 -3.264  5.478   1.00 10.20 ?  93  LEU   A C    1 
ATOM   1930 O  O    . LEU   A 1 93  ? 27.228 -3.329  5.249   1.00 10.34 ?  93  LEU   A O    1 
ATOM   1931 C  CB   . LEU   A 1 93  ? 28.564 -5.403  6.811   1.00 11.12 ?  93  LEU   A CB   1 
ATOM   1932 C  CG   . LEU   A 1 93  ? 28.954 -6.299  5.637   1.00 11.22 ?  93  LEU   A CG   1 
ATOM   1933 C  CD1  . LEU   A 1 93  ? 30.458 -6.563  5.614   1.00 12.33 ?  93  LEU   A CD1  1 
ATOM   1934 C  CD2  . LEU   A 1 93  ? 28.183 -7.622  5.675   1.00 12.03 ?  93  LEU   A CD2  1 
ATOM   1935 H  H    . LEU   A 1 93  ? 27.894 -3.450  8.226   1.00 13.13 ?  93  LEU   A H    1 
ATOM   1936 H  HA   . LEU   A 1 93  ? 29.999 -3.944  6.623   1.00 12.69 ?  93  LEU   A HA   1 
ATOM   1937 H  HB2  . LEU   A 1 93  ? 28.947 -5.788  7.617   1.00 13.40 ?  93  LEU   A HB2  1 
ATOM   1938 H  HB3  . LEU   A 1 93  ? 27.599 -5.410  6.876   1.00 13.40 ?  93  LEU   A HB3  1 
ATOM   1939 H  HG   . LEU   A 1 93  ? 28.730 -5.854  4.813   1.00 13.51 ?  93  LEU   A HG   1 
ATOM   1940 H  HD11 . LEU   A 1 93  ? 30.665 -7.172  4.886   1.00 14.84 ?  93  LEU   A HD11 1 
ATOM   1941 H  HD12 . LEU   A 1 93  ? 30.930 -5.726  5.490   1.00 14.84 ?  93  LEU   A HD12 1 
ATOM   1942 H  HD13 . LEU   A 1 93  ? 30.726 -6.968  6.460   1.00 14.84 ?  93  LEU   A HD13 1 
ATOM   1943 H  HD21 . LEU   A 1 93  ? 28.457 -8.169  4.919   1.00 14.48 ?  93  LEU   A HD21 1 
ATOM   1944 H  HD22 . LEU   A 1 93  ? 28.382 -8.085  6.504   1.00 14.48 ?  93  LEU   A HD22 1 
ATOM   1945 H  HD23 . LEU   A 1 93  ? 27.234 -7.434  5.619   1.00 14.48 ?  93  LEU   A HD23 1 
ATOM   1946 N  N    . HIS   A 1 94  ? 29.290 -2.570  4.719   1.00 9.91  ?  94  HIS   A N    1 
ATOM   1947 C  CA   . HIS   A 1 94  ? 28.870 -1.899  3.492   1.00 9.86  ?  94  HIS   A CA   1 
ATOM   1948 C  C    . HIS   A 1 94  ? 28.878 -2.933  2.381   1.00 9.99  ?  94  HIS   A C    1 
ATOM   1949 O  O    . HIS   A 1 94  ? 29.945 -3.442  2.036   1.00 11.38 ?  94  HIS   A O    1 
ATOM   1950 C  CB   . HIS   A 1 94  ? 29.830 -0.757  3.159   1.00 9.80  ?  94  HIS   A CB   1 
ATOM   1951 C  CG   . HIS   A 1 94  ? 29.819 0.338   4.170   1.00 9.65  ?  94  HIS   A CG   1 
ATOM   1952 N  ND1  . HIS   A 1 94  ? 28.934 1.398   4.114   1.00 10.05 ?  94  HIS   A ND1  1 
ATOM   1953 C  CD2  . HIS   A 1 94  ? 30.554 0.506   5.292   1.00 10.46 ?  94  HIS   A CD2  1 
ATOM   1954 C  CE1  . HIS   A 1 94  ? 29.149 2.181   5.156   1.00 10.44 ?  94  HIS   A CE1  1 
ATOM   1955 N  NE2  . HIS   A 1 94  ? 30.125 1.665   5.885   1.00 10.74 ?  94  HIS   A NE2  1 
ATOM   1956 H  H    . HIS   A 1 94  ? 30.125 -2.474  4.898   1.00 11.95 ?  94  HIS   A H    1 
ATOM   1957 H  HA   . HIS   A 1 94  ? 27.969 -1.546  3.593   1.00 11.88 ?  94  HIS   A HA   1 
ATOM   1958 H  HB2  . HIS   A 1 94  ? 30.727 -1.105  3.108   1.00 11.81 ?  94  HIS   A HB2  1 
ATOM   1959 H  HB3  . HIS   A 1 94  ? 29.570 -0.370  2.306   1.00 11.81 ?  94  HIS   A HB3  1 
ATOM   1960 H  HD2  . HIS   A 1 94  ? 31.230 -0.045  5.602   1.00 12.60 ?  94  HIS   A HD2  1 
ATOM   1961 H  HE1  . HIS   A 1 94  ? 28.676 2.966   5.343   1.00 12.58 ?  94  HIS   A HE1  1 
ATOM   1962 H  HE2  . HIS   A 1 94  ? 30.431 2.011   6.610   1.00 12.94 ?  94  HIS   A HE2  1 
ATOM   1963 N  N    . VAL   A 1 95  ? 27.708 -3.259  1.831   1.00 9.47  ?  95  VAL   A N    1 
ATOM   1964 C  CA   . VAL   A 1 95  ? 27.566 -4.297  0.812   1.00 9.76  ?  95  VAL   A CA   1 
ATOM   1965 C  C    . VAL   A 1 95  ? 27.017 -3.663  -0.452  1.00 9.57  ?  95  VAL   A C    1 
ATOM   1966 O  O    . VAL   A 1 95  ? 26.009 -2.947  -0.396  1.00 10.46 ?  95  VAL   A O    1 
ATOM   1967 C  CB   . VAL   A 1 95  ? 26.639 -5.437  1.271   1.00 10.45 ?  95  VAL   A CB   1 
ATOM   1968 C  CG1  . VAL   A 1 95  ? 26.545 -6.488  0.179   1.00 11.16 ?  95  VAL   A CG1  1 
ATOM   1969 C  CG2  . VAL   A 1 95  ? 27.139 -6.046  2.560   1.00 10.69 ?  95  VAL   A CG2  1 
ATOM   1970 H  H    . VAL   A 1 95  ? 26.961 -2.886  2.045   1.00 11.41 ?  95  VAL   A H    1 
ATOM   1971 H  HA   . VAL   A 1 95  ? 28.434 -4.672  0.612   1.00 11.75 ?  95  VAL   A HA   1 
ATOM   1972 H  HB   . VAL   A 1 95  ? 25.752 -5.087  1.429   1.00 12.59 ?  95  VAL   A HB   1 
ATOM   1973 H  HG11 . VAL   A 1 95  ? 26.150 -7.299  0.547   1.00 13.44 ?  95  VAL   A HG11 1 
ATOM   1974 H  HG12 . VAL   A 1 95  ? 25.986 -6.157  -0.543  1.00 13.44 ?  95  VAL   A HG12 1 
ATOM   1975 H  HG13 . VAL   A 1 95  ? 27.435 -6.688  -0.157  1.00 13.44 ?  95  VAL   A HG13 1 
ATOM   1976 H  HG21 . VAL   A 1 95  ? 26.576 -6.803  2.787   1.00 12.88 ?  95  VAL   A HG21 1 
ATOM   1977 H  HG22 . VAL   A 1 95  ? 28.054 -6.333  2.440   1.00 12.88 ?  95  VAL   A HG22 1 
ATOM   1978 H  HG23 . VAL   A 1 95  ? 27.088 -5.375  3.260   1.00 12.88 ?  95  VAL   A HG23 1 
ATOM   1979 N  N    . VAL   A 1 96  ? 27.648 -3.947  -1.588  1.00 9.48  ?  96  VAL   A N    1 
ATOM   1980 C  CA   . VAL   A 1 96  ? 27.235 -3.397  -2.873  1.00 10.22 ?  96  VAL   A CA   1 
ATOM   1981 C  C    . VAL   A 1 96  ? 26.431 -4.452  -3.626  1.00 10.67 ?  96  VAL   A C    1 
ATOM   1982 O  O    . VAL   A 1 96  ? 26.991 -5.401  -4.186  1.00 11.62 ?  96  VAL   A O    1 
ATOM   1983 C  CB   . VAL   A 1 96  ? 28.426 -2.921  -3.703  1.00 10.62 ?  96  VAL   A CB   1 
ATOM   1984 C  CG1  . VAL   A 1 96  ? 27.916 -2.286  -4.978  1.00 10.96 ?  96  VAL   A CG1  1 
ATOM   1985 C  CG2  . VAL   A 1 96  ? 29.295 -1.951  -2.914  1.00 11.51 ?  96  VAL   A CG2  1 
ATOM   1986 H  H    . VAL   A 1 96  ? 28.342 -4.462  -1.638  1.00 11.42 ?  96  VAL   A H    1 
ATOM   1987 H  HA   . VAL   A 1 96  ? 26.660 -2.635  -2.717  1.00 12.32 ?  96  VAL   A HA   1 
ATOM   1988 H  HB   . VAL   A 1 96  ? 28.972 -3.681  -3.946  1.00 12.79 ?  96  VAL   A HB   1 
ATOM   1989 H  HG11 . VAL   A 1 96  ? 28.650 -1.813  -5.406  1.00 13.20 ?  96  VAL   A HG11 1 
ATOM   1990 H  HG12 . VAL   A 1 96  ? 27.582 -2.976  -5.568  1.00 13.20 ?  96  VAL   A HG12 1 
ATOM   1991 H  HG13 . VAL   A 1 96  ? 27.208 -1.659  -4.759  1.00 13.20 ?  96  VAL   A HG13 1 
ATOM   1992 H  HG21 . VAL   A 1 96  ? 29.998 -1.608  -3.489  1.00 13.86 ?  96  VAL   A HG21 1 
ATOM   1993 H  HG22 . VAL   A 1 96  ? 28.744 -1.213  -2.597  1.00 13.86 ?  96  VAL   A HG22 1 
ATOM   1994 H  HG23 . VAL   A 1 96  ? 29.685 -2.414  -2.156  1.00 13.86 ?  96  VAL   A HG23 1 
ATOM   1995 N  N    . GLY   A 1 97  ? 25.113 -4.293  -3.655  1.00 10.57 ?  97  GLY   A N    1 
ATOM   1996 C  CA   . GLY   A 1 97  ? 24.294 -5.052  -4.563  1.00 11.24 ?  97  GLY   A CA   1 
ATOM   1997 C  C    . GLY   A 1 97  ? 24.306 -4.408  -5.935  1.00 11.32 ?  97  GLY   A C    1 
ATOM   1998 O  O    . GLY   A 1 97  ? 24.587 -3.213  -6.077  1.00 12.17 ?  97  GLY   A O    1 
ATOM   1999 H  H    . GLY   A 1 97  ? 24.674 -3.739  -3.155  1.00 12.73 ?  97  GLY   A H    1 
ATOM   2000 H  HA2  . GLY   A 1 97  ? 24.642 -5.954  -4.616  1.00 13.54 ?  97  GLY   A HA2  1 
ATOM   2001 H  HA3  . GLY   A 1 97  ? 23.381 -5.087  -4.231  1.00 13.54 ?  97  GLY   A HA3  1 
ATOM   2002 N  N    A PRO   A 1 98  ? 23.965 -5.155  -6.981  0.72 11.44 ?  98  PRO   A N    1 
ATOM   2003 N  N    B PRO   A 1 98  ? 24.031 -5.208  -6.965  0.28 11.61 ?  98  PRO   A N    1 
ATOM   2004 C  CA   A PRO   A 1 98  ? 23.839 -4.527  -8.303  0.72 12.40 ?  98  PRO   A CA   1 
ATOM   2005 C  CA   B PRO   A 1 98  ? 24.012 -4.681  -8.330  0.28 12.15 ?  98  PRO   A CA   1 
ATOM   2006 C  C    A PRO   A 1 98  ? 22.723 -3.485  -8.328  0.72 12.30 ?  98  PRO   A C    1 
ATOM   2007 C  C    B PRO   A 1 98  ? 22.889 -3.678  -8.517  0.28 12.22 ?  98  PRO   A C    1 
ATOM   2008 O  O    A PRO   A 1 98  ? 21.648 -3.680  -7.756  0.72 12.65 ?  98  PRO   A O    1 
ATOM   2009 O  O    B PRO   A 1 98  ? 21.803 -3.798  -7.943  0.28 12.62 ?  98  PRO   A O    1 
ATOM   2010 C  CB   A PRO   A 1 98  ? 23.530 -5.710  -9.229  0.72 13.03 ?  98  PRO   A CB   1 
ATOM   2011 C  CB   B PRO   A 1 98  ? 23.776 -5.931  -9.186  0.28 12.36 ?  98  PRO   A CB   1 
ATOM   2012 C  CG   A PRO   A 1 98  ? 22.916 -6.747  -8.328  0.72 13.11 ?  98  PRO   A CG   1 
ATOM   2013 C  CG   B PRO   A 1 98  ? 23.073 -6.883  -8.269  0.28 12.51 ?  98  PRO   A CG   1 
ATOM   2014 C  CD   A PRO   A 1 98  ? 23.657 -6.597  -7.019  0.72 12.06 ?  98  PRO   A CD   1 
ATOM   2015 C  CD   B PRO   A 1 98  ? 23.695 -6.643  -6.923  0.28 11.86 ?  98  PRO   A CD   1 
ATOM   2016 H  HA   A PRO   A 1 98  ? 24.678 -4.120  -8.560  0.72 14.92 ?  98  PRO   A HA   1 
ATOM   2017 H  HA   B PRO   A 1 98  ? 24.867 -4.279  -8.556  0.28 14.63 ?  98  PRO   A HA   1 
ATOM   2018 H  HB2  A PRO   A 1 98  ? 22.903 -5.435  -9.911  0.72 15.69 ?  98  PRO   A HB2  1 
ATOM   2019 H  HB2  B PRO   A 1 98  ? 23.215 -5.705  -9.944  0.28 14.88 ?  98  PRO   A HB2  1 
ATOM   2020 H  HB3  A PRO   A 1 98  ? 24.353 -6.040  -9.623  0.72 15.69 ?  98  PRO   A HB3  1 
ATOM   2021 H  HB3  B PRO   A 1 98  ? 24.624 -6.298  -9.478  0.28 14.88 ?  98  PRO   A HB3  1 
ATOM   2022 H  HG2  A PRO   A 1 98  ? 21.973 -6.566  -8.213  0.72 15.78 ?  98  PRO   A HG2  1 
ATOM   2023 H  HG2  B PRO   A 1 98  ? 22.124 -6.679  -8.250  0.28 15.06 ?  98  PRO   A HG2  1 
ATOM   2024 H  HG3  A PRO   A 1 98  ? 23.058 -7.631  -8.703  0.72 15.78 ?  98  PRO   A HG3  1 
ATOM   2025 H  HG3  B PRO   A 1 98  ? 23.224 -7.794  -8.563  0.28 15.06 ?  98  PRO   A HG3  1 
ATOM   2026 H  HD2  A PRO   A 1 98  ? 23.084 -6.850  -6.274  0.72 14.52 ?  98  PRO   A HD2  1 
ATOM   2027 H  HD2  B PRO   A 1 98  ? 23.054 -6.827  -6.216  0.28 14.28 ?  98  PRO   A HD2  1 
ATOM   2028 H  HD3  A PRO   A 1 98  ? 24.476 -7.119  -7.025  0.72 14.52 ?  98  PRO   A HD3  1 
ATOM   2029 H  HD3  B PRO   A 1 98  ? 24.498 -7.181  -6.820  0.28 14.28 ?  98  PRO   A HD3  1 
ATOM   2030 N  N    A ASN   A 1 99  ? 22.995 -2.360  -8.996  0.72 13.10 ?  99  ASN   A N    1 
ATOM   2031 N  N    B ASN   A 1 99  ? 23.165 -2.678  -9.341  0.28 12.07 ?  99  ASN   A N    1 
ATOM   2032 C  CA   A ASN   A 1 99  ? 22.013 -1.297  -9.210  0.72 14.47 ?  99  ASN   A CA   1 
ATOM   2033 C  CA   B ASN   A 1 99  ? 22.211 -1.623  -9.654  0.28 12.31 ?  99  ASN   A CA   1 
ATOM   2034 C  C    A ASN   A 1 99  ? 21.461 -1.442  -10.625 0.72 15.67 ?  99  ASN   A C    1 
ATOM   2035 C  C    B ASN   A 1 99  ? 21.568 -1.952  -10.995 0.28 13.02 ?  99  ASN   A C    1 
ATOM   2036 O  O    A ASN   A 1 99  ? 22.146 -1.128  -11.606 0.72 16.81 ?  99  ASN   A O    1 
ATOM   2037 O  O    B ASN   A 1 99  ? 22.216 -1.865  -12.043 0.28 12.71 ?  99  ASN   A O    1 
ATOM   2038 C  CB   A ASN   A 1 99  ? 22.645 0.080   -9.013  0.72 14.36 ?  99  ASN   A CB   1 
ATOM   2039 C  CB   B ASN   A 1 99  ? 22.917 -0.273  -9.705  0.28 12.60 ?  99  ASN   A CB   1 
ATOM   2040 C  CG   A ASN   A 1 99  ? 21.617 1.215   -9.018  0.72 14.69 ?  99  ASN   A CG   1 
ATOM   2041 C  CG   B ASN   A 1 99  ? 21.955 0.878   -9.895  0.28 13.24 ?  99  ASN   A CG   1 
ATOM   2042 O  OD1  A ASN   A 1 99  ? 20.622 1.164   -9.740  0.72 15.42 ?  99  ASN   A OD1  1 
ATOM   2043 O  OD1  B ASN   A 1 99  ? 20.947 0.750   -10.587 0.28 13.38 ?  99  ASN   A OD1  1 
ATOM   2044 N  ND2  A ASN   A 1 99  ? 21.864 2.241   -8.212  0.72 15.18 ?  99  ASN   A ND2  1 
ATOM   2045 N  ND2  B ASN   A 1 99  ? 22.261 2.013   -9.275  0.28 14.26 ?  99  ASN   A ND2  1 
ATOM   2046 H  H    A ASN   A 1 99  ? 23.767 -2.187  -9.327  0.72 15.77 ?  99  ASN   A H    1 
ATOM   2047 H  H    B ASN   A 1 99  ? 23.922 -2.585  -9.732  0.28 14.54 ?  99  ASN   A H    1 
ATOM   2048 H  HA   A ASN   A 1 99  ? 21.282 -1.403  -8.573  0.72 17.42 ?  99  ASN   A HA   1 
ATOM   2049 H  HA   B ASN   A 1 99  ? 21.518 -1.596  -8.971  0.28 14.81 ?  99  ASN   A HA   1 
ATOM   2050 H  HB2  A ASN   A 1 99  ? 23.111 0.096   -8.166  0.72 17.28 ?  99  ASN   A HB2  1 
ATOM   2051 H  HB2  B ASN   A 1 99  ? 23.395 -0.136  -8.874  0.28 15.17 ?  99  ASN   A HB2  1 
ATOM   2052 H  HB3  A ASN   A 1 99  ? 23.269 0.238   -9.740  0.72 17.28 ?  99  ASN   A HB3  1 
ATOM   2053 H  HB3  B ASN   A 1 99  ? 23.533 -0.272  -10.451 0.28 15.17 ?  99  ASN   A HB3  1 
ATOM   2054 H  HD21 A ASN   A 1 99  ? 21.317 2.903   -8.176  0.72 18.26 ?  99  ASN   A HD21 1 
ATOM   2055 H  HD21 B ASN   A 1 99  ? 21.744 2.696   -9.345  0.28 17.16 ?  99  ASN   A HD21 1 
ATOM   2056 H  HD22 A ASN   A 1 99  ? 22.571 2.240   -7.722  0.72 18.26 ?  99  ASN   A HD22 1 
ATOM   2057 H  HD22 B ASN   A 1 99  ? 22.977 2.062   -8.799  0.28 17.16 ?  99  ASN   A HD22 1 
ATOM   2058 N  N    A VAL   A 1 100 ? 20.215 -1.919  -10.720 0.72 16.89 ?  100 VAL   A N    1 
ATOM   2059 N  N    B VAL   A 1 100 ? 20.286 -2.321  -10.952 0.28 14.82 ?  100 VAL   A N    1 
ATOM   2060 C  CA   A VAL   A 1 100 ? 19.594 -2.152  -12.021 0.72 19.08 ?  100 VAL   A CA   1 
ATOM   2061 C  CA   B VAL   A 1 100 ? 19.569 -2.715  -12.160 0.28 16.51 ?  100 VAL   A CA   1 
ATOM   2062 C  C    A VAL   A 1 100 ? 19.476 -0.853  -12.803 0.72 19.98 ?  100 VAL   A C    1 
ATOM   2063 C  C    B VAL   A 1 100 ? 19.472 -1.549  -13.132 0.28 16.60 ?  100 VAL   A C    1 
ATOM   2064 O  O    A VAL   A 1 100 ? 19.561 -0.850  -14.036 0.72 20.79 ?  100 VAL   A O    1 
ATOM   2065 O  O    B VAL   A 1 100 ? 19.528 -1.736  -14.354 0.28 16.51 ?  100 VAL   A O    1 
ATOM   2066 C  CB   A VAL   A 1 100 ? 18.238 -2.873  -11.848 0.72 21.14 ?  100 VAL   A CB   1 
ATOM   2067 C  CB   B VAL   A 1 100 ? 18.183 -3.271  -11.788 0.28 18.10 ?  100 VAL   A CB   1 
ATOM   2068 C  CG1  A VAL   A 1 100 ? 17.510 -3.010  -13.182 0.72 21.83 ?  100 VAL   A CG1  1 
ATOM   2069 C  CG1  B VAL   A 1 100 ? 17.385 -3.608  -13.038 0.28 18.53 ?  100 VAL   A CG1  1 
ATOM   2070 C  CG2  A VAL   A 1 100 ? 18.455 -4.242  -11.227 0.72 21.61 ?  100 VAL   A CG2  1 
ATOM   2071 C  CG2  B VAL   A 1 100 ? 18.341 -4.490  -10.899 0.28 18.75 ?  100 VAL   A CG2  1 
ATOM   2072 H  H    A VAL   A 1 100 ? 19.704 -2.117  -10.046 0.72 20.32 ?  100 VAL   A H    1 
ATOM   2073 H  H    B VAL   A 1 100 ? 19.811 -2.347  -10.237 0.28 17.83 ?  100 VAL   A H    1 
ATOM   2074 H  HA   A VAL   A 1 100 ? 20.162 -2.747  -12.530 0.72 22.95 ?  100 VAL   A HA   1 
ATOM   2075 H  HA   B VAL   A 1 100 ? 20.062 -3.417  -12.606 0.28 19.86 ?  100 VAL   A HA   1 
ATOM   2076 H  HB   A VAL   A 1 100 ? 17.672 -2.363  -11.251 0.72 25.41 ?  100 VAL   A HB   1 
ATOM   2077 H  HB   B VAL   A 1 100 ? 17.694 -2.595  -11.290 0.28 21.77 ?  100 VAL   A HB   1 
ATOM   2078 H  HG11 A VAL   A 1 100 ? 16.768 -3.631  -13.077 0.72 26.25 ?  100 VAL   A HG11 1 
ATOM   2079 H  HG11 B VAL   A 1 100 ? 16.614 -4.137  -12.784 0.28 22.28 ?  100 VAL   A HG11 1 
ATOM   2080 H  HG12 A VAL   A 1 100 ? 17.175 -2.143  -13.453 0.72 26.25 ?  100 VAL   A HG12 1 
ATOM   2081 H  HG12 B VAL   A 1 100 ? 17.093 -2.784  -13.462 0.28 22.28 ?  100 VAL   A HG12 1 
ATOM   2082 H  HG13 A VAL   A 1 100 ? 18.128 -3.352  -13.847 0.72 26.25 ?  100 VAL   A HG13 1 
ATOM   2083 H  HG13 B VAL   A 1 100 ? 17.948 -4.111  -13.645 0.28 22.28 ?  100 VAL   A HG13 1 
ATOM   2084 H  HG21 A VAL   A 1 100 ? 17.602 -4.704  -11.164 0.72 25.98 ?  100 VAL   A HG21 1 
ATOM   2085 H  HG21 B VAL   A 1 100 ? 17.469 -4.876  -10.740 0.28 22.55 ?  100 VAL   A HG21 1 
ATOM   2086 H  HG22 A VAL   A 1 100 ? 19.062 -4.753  -11.788 0.72 25.98 ?  100 VAL   A HG22 1 
ATOM   2087 H  HG22 B VAL   A 1 100 ? 18.915 -5.130  -11.348 0.28 22.55 ?  100 VAL   A HG22 1 
ATOM   2088 H  HG23 A VAL   A 1 100 ? 18.836 -4.133  -10.342 0.72 25.98 ?  100 VAL   A HG23 1 
ATOM   2089 H  HG23 B VAL   A 1 100 ? 18.744 -4.217  -10.059 0.28 22.55 ?  100 VAL   A HG23 1 
ATOM   2090 N  N    A ASN   A 1 101 ? 19.288 0.268   -12.112 0.72 21.10 ?  101 ASN   A N    1 
ATOM   2091 N  N    B ASN   A 1 101 ? 19.316 -0.328  -12.608 0.28 16.93 ?  101 ASN   A N    1 
ATOM   2092 C  CA   A ASN   A 1 101 ? 19.225 1.550   -12.801 0.72 22.60 ?  101 ASN   A CA   1 
ATOM   2093 C  CA   B ASN   A 1 101 ? 19.202 0.846   -13.468 0.28 17.45 ?  101 ASN   A CA   1 
ATOM   2094 C  C    A ASN   A 1 101 ? 20.580 1.990   -13.357 0.72 24.75 ?  101 ASN   A C    1 
ATOM   2095 C  C    B ASN   A 1 101 ? 20.487 1.097   -14.244 0.28 18.31 ?  101 ASN   A C    1 
ATOM   2096 O  O    A ASN   A 1 101 ? 20.648 3.044   -14.003 0.72 26.40 ?  101 ASN   A O    1 
ATOM   2097 O  O    B ASN   A 1 101 ? 20.452 1.694   -15.326 0.28 18.17 ?  101 ASN   A O    1 
ATOM   2098 C  CB   A ASN   A 1 101 ? 18.600 2.600   -11.879 0.72 22.18 ?  101 ASN   A CB   1 
ATOM   2099 C  CB   B ASN   A 1 101 ? 18.847 2.073   -12.626 0.28 17.22 ?  101 ASN   A CB   1 
ATOM   2100 C  CG   A ASN   A 1 101 ? 17.219 2.181   -11.377 0.72 21.93 ?  101 ASN   A CG   1 
ATOM   2101 C  CG   B ASN   A 1 101 ? 17.636 1.840   -11.738 0.28 17.55 ?  101 ASN   A CG   1 
ATOM   2102 O  OD1  A ASN   A 1 101 ? 16.385 1.694   -12.147 0.72 22.49 ?  101 ASN   A OD1  1 
ATOM   2103 O  OD1  B ASN   A 1 101 ? 16.635 1.261   -12.166 0.28 17.98 ?  101 ASN   A OD1  1 
ATOM   2104 N  ND2  A ASN   A 1 101 ? 16.979 2.356   -10.081 0.72 21.88 ?  101 ASN   A ND2  1 
ATOM   2105 N  ND2  B ASN   A 1 101 ? 17.727 2.279   -10.489 0.28 17.89 ?  101 ASN   A ND2  1 
ATOM   2106 H  H    A ASN   A 1 101 ? 19.182 0.310   -11.260 0.72 25.36 ?  101 ASN   A H    1 
ATOM   2107 H  H    B ASN   A 1 101 ? 19.271 -0.149  -11.766 0.28 20.36 ?  101 ASN   A H    1 
ATOM   2108 H  HA   A ASN   A 1 101 ? 18.632 1.453   -13.560 0.72 27.17 ?  101 ASN   A HA   1 
ATOM   2109 H  HA   B ASN   A 1 101 ? 18.486 0.713   -14.109 0.28 20.99 ?  101 ASN   A HA   1 
ATOM   2110 H  HB2  A ASN   A 1 101 ? 19.174 2.736   -11.112 0.72 26.66 ?  101 ASN   A HB2  1 
ATOM   2111 H  HB2  B ASN   A 1 101 ? 19.599 2.299   -12.054 0.28 20.71 ?  101 ASN   A HB2  1 
ATOM   2112 H  HB3  A ASN   A 1 101 ? 18.501 3.434   -12.373 0.72 26.66 ?  101 ASN   A HB3  1 
ATOM   2113 H  HB3  B ASN   A 1 101 ? 18.646 2.823   -13.214 0.28 20.71 ?  101 ASN   A HB3  1 
ATOM   2114 H  HD21 A ASN   A 1 101 ? 16.216 2.137   -9.752  0.72 26.30 ?  101 ASN   A HD21 1 
ATOM   2115 H  HD21 B ASN   A 1 101 ? 17.068 2.170   -9.948  0.28 21.52 ?  101 ASN   A HD21 1 
ATOM   2116 H  HD22 A ASN   A 1 101 ? 17.584 2.698   -9.574  0.72 26.30 ?  101 ASN   A HD22 1 
ATOM   2117 H  HD22 B ASN   A 1 101 ? 18.441 2.679   -10.223 0.28 21.52 ?  101 ASN   A HD22 1 
ATOM   2118 N  N    A LYS   A 1 102 ? 21.638 1.197   -13.145 0.72 26.25 ?  102 LYS   A N    1 
ATOM   2119 N  N    B LYS   A 1 102 ? 21.624 0.669   -13.703 0.28 19.90 ?  102 LYS   A N    1 
ATOM   2120 C  CA   A LYS   A 1 102 ? 22.935 1.396   -13.781 0.72 27.52 ?  102 LYS   A CA   1 
ATOM   2121 C  CA   B LYS   A 1 102 ? 22.909 0.763   -14.381 0.28 21.05 ?  102 LYS   A CA   1 
ATOM   2122 C  C    A LYS   A 1 102 ? 23.270 0.309   -14.795 0.72 27.80 ?  102 LYS   A C    1 
ATOM   2123 C  C    B LYS   A 1 102 ? 23.216 -0.478  -15.212 0.28 20.61 ?  102 LYS   A C    1 
ATOM   2124 O  O    A LYS   A 1 102 ? 24.345 0.363   -15.400 0.72 28.44 ?  102 LYS   A O    1 
ATOM   2125 O  O    B LYS   A 1 102 ? 24.339 -0.618  -15.707 0.28 20.17 ?  102 LYS   A O    1 
ATOM   2126 C  CB   A LYS   A 1 102 ? 24.053 1.441   -12.732 0.72 29.04 ?  102 LYS   A CB   1 
ATOM   2127 C  CB   B LYS   A 1 102 ? 24.027 0.997   -13.362 0.28 22.97 ?  102 LYS   A CB   1 
ATOM   2128 C  CG   A LYS   A 1 102 ? 23.950 2.571   -11.730 0.72 30.42 ?  102 LYS   A CG   1 
ATOM   2129 C  CG   B LYS   A 1 102 ? 24.002 2.381   -12.732 0.28 24.75 ?  102 LYS   A CG   1 
ATOM   2130 C  CD   A LYS   A 1 102 ? 25.126 2.529   -10.762 0.72 31.92 ?  102 LYS   A CD   1 
ATOM   2131 C  CD   B LYS   A 1 102 ? 24.812 2.444   -11.446 0.28 26.37 ?  102 LYS   A CD   1 
ATOM   2132 C  CE   A LYS   A 1 102 ? 25.061 3.655   -9.747  0.72 33.20 ?  102 LYS   A CE   1 
ATOM   2133 C  CE   B LYS   A 1 102 ? 24.805 3.854   -10.868 0.28 27.51 ?  102 LYS   A CE   1 
ATOM   2134 N  NZ   A LYS   A 1 102 ? 26.168 3.562   -8.750  0.72 33.77 ?  102 LYS   A NZ   1 
ATOM   2135 N  NZ   B LYS   A 1 102 ? 25.087 3.869   -9.405  0.28 28.10 ?  102 LYS   A NZ   1 
ATOM   2136 H  H    A LYS   A 1 102 ? 21.626 0.507   -12.627 0.72 31.55 ?  102 LYS   A H    1 
ATOM   2137 H  H    B LYS   A 1 102 ? 21.672 0.315   -12.924 0.28 23.93 ?  102 LYS   A H    1 
ATOM   2138 H  HA   A LYS   A 1 102 ? 22.933 2.238   -14.250 0.72 33.07 ?  102 LYS   A HA   1 
ATOM   2139 H  HA   B LYS   A 1 102 ? 22.890 1.537   -14.966 0.28 25.30 ?  102 LYS   A HA   1 
ATOM   2140 H  HB2  A LYS   A 1 102 ? 24.043 0.608   -12.236 0.72 34.90 ?  102 LYS   A HB2  1 
ATOM   2141 H  HB2  B LYS   A 1 102 ? 23.943 0.346   -12.650 0.28 27.61 ?  102 LYS   A HB2  1 
ATOM   2142 H  HB3  A LYS   A 1 102 ? 24.902 1.534   -13.192 0.72 34.90 ?  102 LYS   A HB3  1 
ATOM   2143 H  HB3  B LYS   A 1 102 ? 24.882 0.891   -13.808 0.28 27.61 ?  102 LYS   A HB3  1 
ATOM   2144 H  HG2  A LYS   A 1 102 ? 23.965 3.420   -12.199 0.72 36.55 ?  102 LYS   A HG2  1 
ATOM   2145 H  HG2  B LYS   A 1 102 ? 24.380 3.021   -13.356 0.28 29.75 ?  102 LYS   A HG2  1 
ATOM   2146 H  HG3  A LYS   A 1 102 ? 23.128 2.478   -11.223 0.72 36.55 ?  102 LYS   A HG3  1 
ATOM   2147 H  HG3  B LYS   A 1 102 ? 23.086 2.619   -12.523 0.28 29.75 ?  102 LYS   A HG3  1 
ATOM   2148 H  HD2  A LYS   A 1 102 ? 25.114 1.686   -10.282 0.72 38.36 ?  102 LYS   A HD2  1 
ATOM   2149 H  HD2  B LYS   A 1 102 ? 24.424 1.844   -10.790 0.28 31.69 ?  102 LYS   A HD2  1 
ATOM   2150 H  HD3  A LYS   A 1 102 ? 25.953 2.617   -11.262 0.72 38.36 ?  102 LYS   A HD3  1 
ATOM   2151 H  HD3  B LYS   A 1 102 ? 25.731 2.193   -11.630 0.28 31.69 ?  102 LYS   A HD3  1 
ATOM   2152 H  HE2  A LYS   A 1 102 ? 25.137 4.505   -10.209 0.72 39.89 ?  102 LYS   A HE2  1 
ATOM   2153 H  HE2  B LYS   A 1 102 ? 25.489 4.382   -11.311 0.28 33.05 ?  102 LYS   A HE2  1 
ATOM   2154 H  HE3  A LYS   A 1 102 ? 24.217 3.607   -9.271  0.72 39.89 ?  102 LYS   A HE3  1 
ATOM   2155 H  HE3  B LYS   A 1 102 ? 23.933 4.253   -11.011 0.28 33.05 ?  102 LYS   A HE3  1 
ATOM   2156 H  HZ1  A LYS   A 1 102 ? 26.109 4.230   -8.167  0.72 40.57 ?  102 LYS   A HZ1  1 
ATOM   2157 H  HZ1  B LYS   A 1 102 ? 25.078 4.706   -9.102  0.28 33.77 ?  102 LYS   A HZ1  1 
ATOM   2158 H  HZ2  A LYS   A 1 102 ? 26.117 2.789   -8.312  0.72 40.57 ?  102 LYS   A HZ2  1 
ATOM   2159 H  HZ2  B LYS   A 1 102 ? 24.468 3.398   -8.972  0.28 33.77 ?  102 LYS   A HZ2  1 
ATOM   2160 H  HZ3  A LYS   A 1 102 ? 26.954 3.607   -9.165  0.72 40.57 ?  102 LYS   A HZ3  1 
ATOM   2161 H  HZ3  B LYS   A 1 102 ? 25.886 3.512   -9.246  0.28 33.77 ?  102 LYS   A HZ3  1 
ATOM   2162 N  N    A GLY   A 1 103 ? 22.397 -0.679  -14.982 0.72 28.28 ?  103 GLY   A N    1 
ATOM   2163 N  N    B GLY   A 1 103 ? 22.251 -1.383  -15.360 0.28 20.55 ?  103 GLY   A N    1 
ATOM   2164 C  CA   A GLY   A 1 103 ? 22.661 -1.759  -15.915 0.72 28.36 ?  103 GLY   A CA   1 
ATOM   2165 C  CA   B GLY   A 1 103 ? 22.455 -2.586  -16.142 0.28 20.35 ?  103 GLY   A CA   1 
ATOM   2166 C  C    A GLY   A 1 103 ? 23.508 -2.888  -15.372 0.72 28.31 ?  103 GLY   A C    1 
ATOM   2167 C  C    B GLY   A 1 103 ? 23.364 -3.613  -15.510 0.28 19.77 ?  103 GLY   A C    1 
ATOM   2168 O  O    A GLY   A 1 103 ? 24.120 -3.616  -16.158 0.72 29.18 ?  103 GLY   A O    1 
ATOM   2169 O  O    B GLY   A 1 103 ? 23.775 -4.558  -16.192 0.28 19.57 ?  103 GLY   A O    1 
ATOM   2170 H  H    A GLY   A 1 103 ? 21.642 -0.748  -14.580 0.72 33.98 ?  103 GLY   A H    1 
ATOM   2171 H  H    B GLY   A 1 103 ? 21.466 -1.317  -15.010 0.28 24.71 ?  103 GLY   A H    1 
ATOM   2172 H  HA2  A GLY   A 1 103 ? 21.814 -2.127  -16.225 0.72 34.08 ?  103 GLY   A HA2  1 
ATOM   2173 H  HA2  B GLY   A 1 103 ? 21.595 -3.002  -16.300 0.28 24.47 ?  103 GLY   A HA2  1 
ATOM   2174 H  HA3  A GLY   A 1 103 ? 23.127 -1.404  -16.687 0.72 34.08 ?  103 GLY   A HA3  1 
ATOM   2175 H  HA3  B GLY   A 1 103 ? 22.830 -2.337  -17.002 0.28 24.47 ?  103 GLY   A HA3  1 
ATOM   2176 N  N    A GLU   A 1 104 ? 23.564 -3.062  -14.054 0.72 26.62 ?  104 GLU   A N    1 
ATOM   2177 N  N    B GLU   A 1 104 ? 23.693 -3.465  -14.230 0.28 19.42 ?  104 GLU   A N    1 
ATOM   2178 C  CA   A GLU   A 1 104 ? 24.431 -4.064  -13.449 0.72 24.79 ?  104 GLU   A CA   1 
ATOM   2179 C  CA   B GLU   A 1 104 ? 24.613 -4.390  -13.585 0.28 18.90 ?  104 GLU   A CA   1 
ATOM   2180 C  C    A GLU   A 1 104 ? 23.737 -5.422  -13.346 0.72 24.77 ?  104 GLU   A C    1 
ATOM   2181 C  C    B GLU   A 1 104 ? 23.962 -5.760  -13.400 0.28 18.90 ?  104 GLU   A C    1 
ATOM   2182 O  O    A GLU   A 1 104 ? 22.510 -5.515  -13.245 0.72 25.10 ?  104 GLU   A O    1 
ATOM   2183 O  O    B GLU   A 1 104 ? 22.770 -5.869  -13.096 0.28 18.54 ?  104 GLU   A O    1 
ATOM   2184 C  CB   A GLU   A 1 104 ? 24.929 -3.574  -12.084 0.72 22.92 ?  104 GLU   A CB   1 
ATOM   2185 C  CB   B GLU   A 1 104 ? 25.077 -3.810  -12.248 0.28 18.85 ?  104 GLU   A CB   1 
ATOM   2186 C  CG   A GLU   A 1 104 ? 25.892 -2.391  -12.241 0.72 21.88 ?  104 GLU   A CG   1 
ATOM   2187 C  CG   B GLU   A 1 104 ? 25.774 -2.459  -12.406 0.28 19.49 ?  104 GLU   A CG   1 
ATOM   2188 C  CD   A GLU   A 1 104 ? 26.210 -1.611  -10.972 0.72 20.63 ?  104 GLU   A CD   1 
ATOM   2189 C  CD   B GLU   A 1 104 ? 26.149 -1.808  -11.088 0.28 19.87 ?  104 GLU   A CD   1 
ATOM   2190 O  OE1  A GLU   A 1 104 ? 25.599 -1.857  -9.910  0.72 18.82 ?  104 GLU   A OE1  1 
ATOM   2191 O  OE1  B GLU   A 1 104 ? 25.734 -2.305  -10.021 0.28 20.13 ?  104 GLU   A OE1  1 
ATOM   2192 O  OE2  A GLU   A 1 104 ? 27.086 -0.717  -11.066 0.72 21.68 -1 104 GLU   A OE2  1 
ATOM   2193 O  OE2  B GLU   A 1 104 ? 26.859 -0.782  -11.128 0.28 20.18 -1 104 GLU   A OE2  1 
ATOM   2194 H  H    A GLU   A 1 104 ? 23.113 -2.600  -13.486 0.72 31.99 ?  104 GLU   A H    1 
ATOM   2195 H  H    B GLU   A 1 104 ? 23.401 -2.832  -13.721 0.28 23.35 ?  104 GLU   A H    1 
ATOM   2196 H  HA   A GLU   A 1 104 ? 25.206 -4.176  -14.020 0.72 29.80 ?  104 GLU   A HA   1 
ATOM   2197 H  HA   B GLU   A 1 104 ? 25.396 -4.496  -14.150 0.28 22.73 ?  104 GLU   A HA   1 
ATOM   2198 H  HB2  A GLU   A 1 104 ? 24.169 -3.290  -11.555 0.72 27.55 ?  104 GLU   A HB2  1 
ATOM   2199 H  HB2  B GLU   A 1 104 ? 24.310 -3.683  -11.671 0.28 22.67 ?  104 GLU   A HB2  1 
ATOM   2200 H  HB3  A GLU   A 1 104 ? 25.398 -4.299  -11.643 0.72 27.55 ?  104 GLU   A HB3  1 
ATOM   2201 H  HB3  B GLU   A 1 104 ? 25.708 -4.422  -11.839 0.28 22.67 ?  104 GLU   A HB3  1 
ATOM   2202 H  HG2  A GLU   A 1 104 ? 26.730 -2.726  -12.583 0.72 26.31 ?  104 GLU   A HG2  1 
ATOM   2203 H  HG2  B GLU   A 1 104 ? 26.588 -2.580  -12.921 0.28 23.43 ?  104 GLU   A HG2  1 
ATOM   2204 H  HG3  A GLU   A 1 104 ? 25.503 -1.765  -12.869 0.72 26.31 ?  104 GLU   A HG3  1 
ATOM   2205 H  HG3  B GLU   A 1 104 ? 25.181 -1.847  -12.870 0.28 23.43 ?  104 GLU   A HG3  1 
ATOM   2206 N  N    A ASP   A 1 105 ? 24.551 -6.478  -13.367 0.72 25.20 ?  105 ASP   A N    1 
ATOM   2207 N  N    B ASP   A 1 105 ? 24.766 -6.806  -13.592 0.28 19.97 ?  105 ASP   A N    1 
ATOM   2208 C  CA   A ASP   A 1 105 ? 24.063 -7.845  -13.528 0.72 25.94 ?  105 ASP   A CA   1 
ATOM   2209 C  CA   B ASP   A 1 105 ? 24.282 -8.183  -13.611 0.28 21.31 ?  105 ASP   A CA   1 
ATOM   2210 C  C    A ASP   A 1 105 ? 23.385 -8.329  -12.249 0.72 23.50 ?  105 ASP   A C    1 
ATOM   2211 C  C    B ASP   A 1 105 ? 23.551 -8.525  -12.320 0.28 21.46 ?  105 ASP   A C    1 
ATOM   2212 O  O    A ASP   A 1 105 ? 24.032 -8.463  -11.206 0.72 21.58 ?  105 ASP   A O    1 
ATOM   2213 O  O    B ASP   A 1 105 ? 24.122 -8.444  -11.229 0.28 21.10 ?  105 ASP   A O    1 
ATOM   2214 C  CB   A ASP   A 1 105 ? 25.246 -8.746  -13.879 0.72 29.08 ?  105 ASP   A CB   1 
ATOM   2215 C  CB   B ASP   A 1 105 ? 25.483 -9.111  -13.797 0.28 22.49 ?  105 ASP   A CB   1 
ATOM   2216 C  CG   A ASP   A 1 105 ? 24.838 -10.176 -14.142 0.72 31.74 ?  105 ASP   A CG   1 
ATOM   2217 C  CG   B ASP   A 1 105 ? 25.103 -10.581 -13.832 0.28 23.53 ?  105 ASP   A CG   1 
ATOM   2218 O  OD1  A ASP   A 1 105 ? 23.622 -10.444 -14.208 0.72 32.43 ?  105 ASP   A OD1  1 
ATOM   2219 O  OD1  B ASP   A 1 105 ? 23.897 -10.895 -13.906 0.28 23.53 ?  105 ASP   A OD1  1 
ATOM   2220 O  OD2  A ASP   A 1 105 ? 25.741 -11.031 -14.288 0.72 33.18 -1 105 ASP   A OD2  1 
ATOM   2221 O  OD2  B ASP   A 1 105 ? 26.025 -11.426 -13.778 0.28 24.21 -1 105 ASP   A OD2  1 
ATOM   2222 H  H    A ASP   A 1 105 ? 25.406 -6.427  -13.285 0.72 30.28 ?  105 ASP   A H    1 
ATOM   2223 H  H    B ASP   A 1 105 ? 25.609 -6.733  -13.722 0.28 24.01 ?  105 ASP   A H    1 
ATOM   2224 H  HA   A ASP   A 1 105 ? 23.421 -7.884  -14.254 0.72 31.18 ?  105 ASP   A HA   1 
ATOM   2225 H  HA   B ASP   A 1 105 ? 23.669 -8.300  -14.353 0.28 25.62 ?  105 ASP   A HA   1 
ATOM   2226 H  HB2  A ASP   A 1 105 ? 25.676 -8.408  -14.682 0.72 34.94 ?  105 ASP   A HB2  1 
ATOM   2227 H  HB2  B ASP   A 1 105 ? 25.925 -8.881  -14.630 0.28 27.04 ?  105 ASP   A HB2  1 
ATOM   2228 H  HB3  A ASP   A 1 105 ? 25.877 -8.745  -13.142 0.72 34.94 ?  105 ASP   A HB3  1 
ATOM   2229 H  HB3  B ASP   A 1 105 ? 26.089 -8.989  -13.053 0.28 27.04 ?  105 ASP   A HB3  1 
ATOM   2230 N  N    A ILE   A 1 106 ? 22.083 -8.614  -12.335 0.72 23.17 ?  106 ILE   A N    1 
ATOM   2231 N  N    B ILE   A 1 106 ? 22.284 -8.931  -12.448 0.28 21.86 ?  106 ILE   A N    1 
ATOM   2232 C  CA   A ILE   A 1 106 ? 21.327 -9.053  -11.168 0.72 22.68 ?  106 ILE   A CA   1 
ATOM   2233 C  CA   B ILE   A 1 106 ? 21.489 -9.245  -11.268 0.28 22.39 ?  106 ILE   A CA   1 
ATOM   2234 C  C    A ILE   A 1 106 ? 21.879 -10.344 -10.588 0.72 22.05 ?  106 ILE   A C    1 
ATOM   2235 C  C    B ILE   A 1 106 ? 21.974 -10.514 -10.579 0.28 22.12 ?  106 ILE   A C    1 
ATOM   2236 O  O    A ILE   A 1 106 ? 21.686 -10.613 -9.398  0.72 21.34 ?  106 ILE   A O    1 
ATOM   2237 O  O    B ILE   A 1 106 ? 21.703 -10.707 -9.388  0.28 21.95 ?  106 ILE   A O    1 
ATOM   2238 C  CB   A ILE   A 1 106 ? 19.821 -9.161  -11.505 0.72 24.23 ?  106 ILE   A CB   1 
ATOM   2239 C  CB   B ILE   A 1 106 ? 19.986 -9.301  -11.614 0.28 23.56 ?  106 ILE   A CB   1 
ATOM   2240 C  CG1  A ILE   A 1 106 ? 18.983 -9.308  -10.231 0.72 24.45 ?  106 ILE   A CG1  1 
ATOM   2241 C  CG1  B ILE   A 1 106 ? 19.136 -9.149  -10.349 0.28 24.25 ?  106 ILE   A CG1  1 
ATOM   2242 C  CG2  A ILE   A 1 106 ? 19.558 -10.331 -12.432 0.72 25.00 ?  106 ILE   A CG2  1 
ATOM   2243 C  CG2  B ILE   A 1 106 ? 19.645 -10.606 -12.313 0.28 23.82 ?  106 ILE   A CG2  1 
ATOM   2244 C  CD1  A ILE   A 1 106 ? 19.058 -8.113  -9.307  0.72 24.45 ?  106 ILE   A CD1  1 
ATOM   2245 C  CD1  B ILE   A 1 106 ? 19.435 -7.891  -9.557  0.28 24.63 ?  106 ILE   A CD1  1 
ATOM   2246 H  H    A ILE   A 1 106 ? 21.623 -8.554  -13.053 0.72 27.85 ?  106 ILE   A H    1 
ATOM   2247 H  H    B ILE   A 1 106 ? 21.873 -9.024  -13.196 0.28 26.28 ?  106 ILE   A H    1 
ATOM   2248 H  HA   A ILE   A 1 106 ? 21.426 -8.387  -10.480 0.72 27.26 ?  106 ILE   A HA   1 
ATOM   2249 H  HA   B ILE   A 1 106 ? 21.620 -8.525  -10.641 0.28 26.92 ?  106 ILE   A HA   1 
ATOM   2250 H  HB   A ILE   A 1 106 ? 19.554 -8.346  -11.956 0.72 29.12 ?  106 ILE   A HB   1 
ATOM   2251 H  HB   B ILE   A 1 106 ? 19.776 -8.568  -12.214 0.28 28.32 ?  106 ILE   A HB   1 
ATOM   2252 H  HG12 A ILE   A 1 106 ? 18.054 -9.425  -10.483 0.72 29.39 ?  106 ILE   A HG12 1 
ATOM   2253 H  HG12 B ILE   A 1 106 ? 18.199 -9.120  -10.602 0.28 29.15 ?  106 ILE   A HG12 1 
ATOM   2254 H  HG13 A ILE   A 1 106 ? 19.290 -10.084 -9.738  0.72 29.39 ?  106 ILE   A HG13 1 
ATOM   2255 H  HG13 B ILE   A 1 106 ? 19.297 -9.908  -9.770  0.28 29.15 ?  106 ILE   A HG13 1 
ATOM   2256 H  HG21 A ILE   A 1 106 ? 18.657 -10.255 -12.782 0.72 30.05 ?  106 ILE   A HG21 1 
ATOM   2257 H  HG21 B ILE   A 1 106 ? 18.776 -10.518 -12.736 0.28 28.63 ?  106 ILE   A HG21 1 
ATOM   2258 H  HG22 A ILE   A 1 106 ? 20.200 -10.305 -13.156 0.72 30.05 ?  106 ILE   A HG22 1 
ATOM   2259 H  HG22 B ILE   A 1 106 ? 20.322 -10.788 -12.981 0.28 28.63 ?  106 ILE   A HG22 1 
ATOM   2260 H  HG23 A ILE   A 1 106 ? 19.651 -11.157 -11.933 0.72 30.05 ?  106 ILE   A HG23 1 
ATOM   2261 H  HG23 B ILE   A 1 106 ? 19.623 -11.320 -11.658 0.28 28.63 ?  106 ILE   A HG23 1 
ATOM   2262 H  HD11 A ILE   A 1 106 ? 18.344 -8.174  -8.655  0.72 29.39 ?  106 ILE   A HD11 1 
ATOM   2263 H  HD11 B ILE   A 1 106 ? 18.666 -7.673  -9.012  0.28 29.61 ?  106 ILE   A HD11 1 
ATOM   2264 H  HD12 A ILE   A 1 106 ? 19.918 -8.115  -8.855  0.72 29.39 ?  106 ILE   A HD12 1 
ATOM   2265 H  HD12 B ILE   A 1 106 ? 20.208 -8.051  -8.992  0.28 29.61 ?  106 ILE   A HD12 1 
ATOM   2266 H  HD13 A ILE   A 1 106 ? 18.961 -7.302  -9.830  0.72 29.39 ?  106 ILE   A HD13 1 
ATOM   2267 H  HD13 B ILE   A 1 106 ? 19.620 -7.167  -10.176 0.28 29.61 ?  106 ILE   A HD13 1 
ATOM   2268 N  N    A GLN   A 1 107 ? 22.576 -11.149 -11.400 0.72 22.95 ?  107 GLN   A N    1 
ATOM   2269 N  N    B GLN   A 1 107 ? 22.690 -11.386 -11.295 0.28 22.13 ?  107 GLN   A N    1 
ATOM   2270 C  CA   A GLN   A 1 107 ? 23.217 -12.355 -10.889 0.72 24.95 ?  107 GLN   A CA   1 
ATOM   2271 C  CA   B GLN   A 1 107 ? 23.275 -12.558 -10.652 0.28 22.72 ?  107 GLN   A CA   1 
ATOM   2272 C  C    A GLN   A 1 107 ? 24.193 -12.041 -9.763  0.72 22.09 ?  107 GLN   A C    1 
ATOM   2273 C  C    B GLN   A 1 107 ? 24.247 -12.158 -9.549  0.28 20.28 ?  107 GLN   A C    1 
ATOM   2274 O  O    A GLN   A 1 107 ? 24.448 -12.903 -8.916  0.72 23.77 ?  107 GLN   A O    1 
ATOM   2275 O  O    B GLN   A 1 107 ? 24.457 -12.920 -8.597  0.28 20.14 ?  107 GLN   A O    1 
ATOM   2276 C  CB   A GLN   A 1 107 ? 23.921 -13.096 -12.037 0.72 29.58 ?  107 GLN   A CB   1 
ATOM   2277 C  CB   B GLN   A 1 107 ? 23.959 -13.442 -11.698 0.28 25.76 ?  107 GLN   A CB   1 
ATOM   2278 C  CG   A GLN   A 1 107 ? 23.026 -13.356 -13.249 0.72 34.59 ?  107 GLN   A CG   1 
ATOM   2279 C  CG   B GLN   A 1 107 ? 23.034 -13.881 -12.826 0.28 28.68 ?  107 GLN   A CG   1 
ATOM   2280 C  CD   A GLN   A 1 107 ? 21.769 -14.125 -12.893 0.72 38.52 ?  107 GLN   A CD   1 
ATOM   2281 C  CD   B GLN   A 1 107 ? 21.805 -14.614 -12.323 0.28 31.21 ?  107 GLN   A CD   1 
ATOM   2282 O  OE1  A GLN   A 1 107 ? 21.832 -15.189 -12.275 0.72 40.06 ?  107 GLN   A OE1  1 
ATOM   2283 O  OE1  B GLN   A 1 107 ? 21.860 -15.325 -11.318 0.28 32.07 ?  107 GLN   A OE1  1 
ATOM   2284 N  NE2  A GLN   A 1 107 ? 20.616 -13.587 -13.277 0.72 39.77 ?  107 GLN   A NE2  1 
ATOM   2285 N  NE2  B GLN   A 1 107 ? 20.686 -14.441 -13.018 0.28 32.01 ?  107 GLN   A NE2  1 
ATOM   2286 H  H    A GLN   A 1 107 ? 22.697 -11.018 -12.241 0.72 27.59 ?  107 GLN   A H    1 
ATOM   2287 H  H    B GLN   A 1 107 ? 22.841 -11.323 -12.140 0.28 26.60 ?  107 GLN   A H    1 
ATOM   2288 H  HA   A GLN   A 1 107 ? 22.546 -12.953 -10.533 0.72 29.99 ?  107 GLN   A HA   1 
ATOM   2289 H  HA   B GLN   A 1 107 ? 22.571 -13.074 -10.244 0.28 27.31 ?  107 GLN   A HA   1 
ATOM   2290 H  HB2  A GLN   A 1 107 ? 24.677 -12.571 -12.343 0.72 35.54 ?  107 GLN   A HB2  1 
ATOM   2291 H  HB2  B GLN   A 1 107 ? 24.695 -12.954 -12.097 0.28 30.96 ?  107 GLN   A HB2  1 
ATOM   2292 H  HB3  A GLN   A 1 107 ? 24.231 -13.961 -11.720 0.72 35.54 ?  107 GLN   A HB3  1 
ATOM   2293 H  HB3  B GLN   A 1 107 ? 24.291 -14.243 -11.264 0.28 30.96 ?  107 GLN   A HB3  1 
ATOM   2294 H  HG2  A GLN   A 1 107 ? 22.757 -12.509 -13.638 0.72 41.55 ?  107 GLN   A HG2  1 
ATOM   2295 H  HG2  B GLN   A 1 107 ? 22.737 -13.098 -13.316 0.28 34.46 ?  107 GLN   A HG2  1 
ATOM   2296 H  HG3  A GLN   A 1 107 ? 23.520 -13.875 -13.904 0.72 41.55 ?  107 GLN   A HG3  1 
ATOM   2297 H  HG3  B GLN   A 1 107 ? 23.516 -14.479 -13.418 0.28 34.46 ?  107 GLN   A HG3  1 
ATOM   2298 H  HE21 A GLN   A 1 107 ? 20.609 -12.843 -13.708 0.72 47.77 ?  107 GLN   A HE21 1 
ATOM   2299 H  HE21 B GLN   A 1 107 ? 20.686 -13.934 -13.714 0.28 38.46 ?  107 GLN   A HE21 1 
ATOM   2300 H  HE22 A GLN   A 1 107 ? 19.876 -13.986 -13.097 0.72 47.77 ?  107 GLN   A HE22 1 
ATOM   2301 H  HE22 B GLN   A 1 107 ? 19.961 -14.833 -12.773 0.28 38.46 ?  107 GLN   A HE22 1 
ATOM   2302 N  N    A LEU   A 1 108 ? 24.715 -10.813 -9.710  0.72 17.97 ?  108 LEU   A N    1 
ATOM   2303 N  N    B LEU   A 1 108 ? 24.829 -10.960 -9.644  0.28 18.22 ?  108 LEU   A N    1 
ATOM   2304 C  CA   A LEU   A 1 108 ? 25.647 -10.426 -8.659  0.72 15.58 ?  108 LEU   A CA   1 
ATOM   2305 C  CA   B LEU   A 1 108 ? 25.702 -10.459 -8.592  0.28 16.38 ?  108 LEU   A CA   1 
ATOM   2306 C  C    A LEU   A 1 108 ? 24.964 -10.256 -7.309  0.72 13.89 ?  108 LEU   A C    1 
ATOM   2307 C  C    B LEU   A 1 108 ? 24.967 -10.236 -7.278  0.28 14.71 ?  108 LEU   A C    1 
ATOM   2308 O  O    A LEU   A 1 108 ? 25.659 -10.105 -6.301  0.72 14.08 ?  108 LEU   A O    1 
ATOM   2309 O  O    B LEU   A 1 108 ? 25.626 -10.008 -6.258  0.28 14.83 ?  108 LEU   A O    1 
ATOM   2310 C  CB   A LEU   A 1 108 ? 26.393 -9.145  -9.056  0.72 15.58 ?  108 LEU   A CB   1 
ATOM   2311 C  CB   B LEU   A 1 108 ? 26.390 -9.166  -9.046  0.28 16.51 ?  108 LEU   A CB   1 
ATOM   2312 C  CG   A LEU   A 1 108 ? 27.384 -9.345  -10.206 0.72 17.20 ?  108 LEU   A CG   1 
ATOM   2313 C  CG   B LEU   A 1 108 ? 27.400 -9.332  -10.185 0.28 17.22 ?  108 LEU   A CG   1 
ATOM   2314 C  CD1  A LEU   A 1 108 ? 27.897 -8.017  -10.743 0.72 17.92 ?  108 LEU   A CD1  1 
ATOM   2315 C  CD1  B LEU   A 1 108 ? 27.877 -7.981  -10.700 0.28 17.53 ?  108 LEU   A CD1  1 
ATOM   2316 C  CD2  A LEU   A 1 108 ? 28.553 -10.222 -9.771  0.72 19.01 ?  108 LEU   A CD2  1 
ATOM   2317 C  CD2  B LEU   A 1 108 ? 28.583 -10.176 -9.734  0.28 17.95 ?  108 LEU   A CD2  1 
ATOM   2318 H  H    A LEU   A 1 108 ? 24.535 -10.193 -10.268 0.72 21.61 ?  108 LEU   A H    1 
ATOM   2319 H  H    B LEU   A 1 108 ? 24.737 -10.425 -10.305 0.28 21.91 ?  108 LEU   A H    1 
ATOM   2320 H  HA   A LEU   A 1 108 ? 26.304 -11.129 -8.558  0.72 18.74 ?  108 LEU   A HA   1 
ATOM   2321 H  HA   B LEU   A 1 108 ? 26.394 -11.114 -8.421  0.28 19.70 ?  108 LEU   A HA   1 
ATOM   2322 H  HB2  A LEU   A 1 108 ? 25.746 -8.480  -9.339  0.72 18.75 ?  108 LEU   A HB2  1 
ATOM   2323 H  HB2  B LEU   A 1 108 ? 25.711 -8.544  -9.349  0.28 19.86 ?  108 LEU   A HB2  1 
ATOM   2324 H  HB3  A LEU   A 1 108 ? 26.888 -8.821  -8.291  0.72 18.75 ?  108 LEU   A HB3  1 
ATOM   2325 H  HB3  B LEU   A 1 108 ? 26.865 -8.786  -8.291  0.28 19.86 ?  108 LEU   A HB3  1 
ATOM   2326 H  HG   A LEU   A 1 108 ? 26.933 -9.801  -10.934 0.72 20.69 ?  108 LEU   A HG   1 
ATOM   2327 H  HG   B LEU   A 1 108 ? 26.970 -9.794  -10.922 0.28 20.71 ?  108 LEU   A HG   1 
ATOM   2328 H  HD11 A LEU   A 1 108 ? 28.509 -8.188  -11.480 0.72 21.55 ?  108 LEU   A HD11 1 
ATOM   2329 H  HD11 B LEU   A 1 108 ? 28.474 -8.122  -11.453 0.28 21.09 ?  108 LEU   A HD11 1 
ATOM   2330 H  HD12 A LEU   A 1 108 ? 27.145 -7.491  -11.055 0.72 21.55 ?  108 LEU   A HD12 1 
ATOM   2331 H  HD12 B LEU   A 1 108 ? 27.109 -7.460  -10.981 0.28 21.09 ?  108 LEU   A HD12 1 
ATOM   2332 H  HD13 A LEU   A 1 108 ? 28.361 -7.546  -10.034 0.72 21.55 ?  108 LEU   A HD13 1 
ATOM   2333 H  HD13 B LEU   A 1 108 ? 28.348 -7.519  -9.989  0.28 21.09 ?  108 LEU   A HD13 1 
ATOM   2334 H  HD21 A LEU   A 1 108 ? 29.247 -10.181 -10.446 0.72 22.86 ?  108 LEU   A HD21 1 
ATOM   2335 H  HD21 B LEU   A 1 108 ? 29.279 -10.127 -10.407 0.28 21.59 ?  108 LEU   A HD21 1 
ATOM   2336 H  HD22 A LEU   A 1 108 ? 28.893 -9.893  -8.924  0.72 22.86 ?  108 LEU   A HD22 1 
ATOM   2337 H  HD22 B LEU   A 1 108 ? 28.912 -9.829  -8.890  0.28 21.59 ?  108 LEU   A HD22 1 
ATOM   2338 H  HD23 A LEU   A 1 108 ? 28.242 -11.135 -9.671  0.72 22.86 ?  108 LEU   A HD23 1 
ATOM   2339 H  HD23 B LEU   A 1 108 ? 28.292 -11.094 -9.624  0.28 21.59 ?  108 LEU   A HD23 1 
ATOM   2340 N  N    . LEU   A 1 109 ? 23.632 -10.305 -7.262  1.00 13.63 ?  109 LEU   A N    1 
ATOM   2341 C  CA   . LEU   A 1 109 ? 22.930 -10.177 -5.993  1.00 12.77 ?  109 LEU   A CA   1 
ATOM   2342 C  C    . LEU   A 1 109 ? 23.275 -11.331 -5.059  1.00 11.89 ?  109 LEU   A C    1 
ATOM   2343 O  O    . LEU   A 1 109 ? 23.412 -11.139 -3.845  1.00 12.46 ?  109 LEU   A O    1 
ATOM   2344 C  CB   . LEU   A 1 109 ? 21.427 -10.099 -6.248  1.00 13.52 ?  109 LEU   A CB   1 
ATOM   2345 C  CG   . LEU   A 1 109 ? 20.536 -9.818  -5.041  1.00 13.98 ?  109 LEU   A CG   1 
ATOM   2346 C  CD1  . LEU   A 1 109 ? 20.988 -8.558  -4.319  1.00 14.39 ?  109 LEU   A CD1  1 
ATOM   2347 C  CD2  . LEU   A 1 109 ? 19.083 -9.681  -5.476  1.00 15.16 ?  109 LEU   A CD2  1 
ATOM   2348 H  H    A LEU   A 1 109 ? 23.117 -10.407 -7.943  0.72 16.40 ?  109 LEU   A H    1 
ATOM   2349 H  H    B LEU   A 1 109 ? 23.127 -10.424 -7.948  0.28 16.40 ?  109 LEU   A H    1 
ATOM   2350 H  HA   . LEU   A 1 109 ? 23.212 -9.351  -5.565  1.00 15.37 ?  109 LEU   A HA   1 
ATOM   2351 H  HB2  . LEU   A 1 109 ? 21.269 -9.387  -6.890  1.00 16.27 ?  109 LEU   A HB2  1 
ATOM   2352 H  HB3  . LEU   A 1 109 ? 21.141 -10.941 -6.625  1.00 16.27 ?  109 LEU   A HB3  1 
ATOM   2353 H  HG   . LEU   A 1 109 ? 20.596 -10.558 -4.421  1.00 16.82 ?  109 LEU   A HG   1 
ATOM   2354 H  HD11 . LEU   A 1 109 ? 20.309 -8.292  -3.682  1.00 17.32 ?  109 LEU   A HD11 1 
ATOM   2355 H  HD12 . LEU   A 1 109 ? 21.824 -8.734  -3.860  1.00 17.32 ?  109 LEU   A HD12 1 
ATOM   2356 H  HD13 . LEU   A 1 109 ? 21.118 -7.845  -4.973  1.00 17.32 ?  109 LEU   A HD13 1 
ATOM   2357 H  HD21 . LEU   A 1 109 ? 18.548 -9.402  -4.715  1.00 18.24 ?  109 LEU   A HD21 1 
ATOM   2358 H  HD22 . LEU   A 1 109 ? 19.020 -9.021  -6.183  1.00 18.24 ?  109 LEU   A HD22 1 
ATOM   2359 H  HD23 . LEU   A 1 109 ? 18.766 -10.542 -5.800  1.00 18.24 ?  109 LEU   A HD23 1 
ATOM   2360 N  N    . LYS   A 1 110 ? 23.415 -12.543 -5.598  1.00 12.01 ?  110 LYS   A N    1 
ATOM   2361 C  CA   . LYS   A 1 110 ? 23.789 -13.663 -4.742  1.00 12.05 ?  110 LYS   A CA   1 
ATOM   2362 C  C    . LYS   A 1 110 ? 25.172 -13.443 -4.138  1.00 11.51 ?  110 LYS   A C    1 
ATOM   2363 O  O    . LYS   A 1 110 ? 25.366 -13.641 -2.935  1.00 11.79 ?  110 LYS   A O    1 
ATOM   2364 C  CB   . LYS   A 1 110 ? 23.708 -14.989 -5.504  1.00 12.94 ?  110 LYS   A CB   1 
ATOM   2365 C  CG   . LYS   A 1 110 ? 23.905 -16.198 -4.591  1.00 13.17 ?  110 LYS   A CG   1 
ATOM   2366 C  CD   . LYS   A 1 110 ? 23.690 -17.517 -5.304  1.00 13.96 ?  110 LYS   A CD   1 
ATOM   2367 C  CE   . LYS   A 1 110 ? 23.786 -18.697 -4.353  1.00 14.96 ?  110 LYS   A CE   1 
ATOM   2368 N  NZ   . LYS   A 1 110 ? 22.604 -18.822 -3.461  1.00 15.25 ?  110 LYS   A NZ   1 
ATOM   2369 H  H    . LYS   A 1 110 ? 23.303 -12.737 -6.426  1.00 14.46 ?  110 LYS   A H    1 
ATOM   2370 H  HA   . LYS   A 1 110 ? 23.150 -13.713 -4.008  1.00 14.50 ?  110 LYS   A HA   1 
ATOM   2371 H  HB2  . LYS   A 1 110 ? 22.833 -15.063 -5.918  1.00 15.57 ?  110 LYS   A HB2  1 
ATOM   2372 H  HB3  . LYS   A 1 110 ? 24.401 -15.006 -6.177  1.00 15.57 ?  110 LYS   A HB3  1 
ATOM   2373 H  HG2  . LYS   A 1 110 ? 24.805 -16.186 -4.238  1.00 15.85 ?  110 LYS   A HG2  1 
ATOM   2374 H  HG3  . LYS   A 1 110 ? 23.263 -16.147 -3.860  1.00 15.85 ?  110 LYS   A HG3  1 
ATOM   2375 H  HD2  . LYS   A 1 110 ? 22.813 -17.525 -5.707  1.00 16.80 ?  110 LYS   A HD2  1 
ATOM   2376 H  HD3  . LYS   A 1 110 ? 24.377 -17.622 -5.982  1.00 16.80 ?  110 LYS   A HD3  1 
ATOM   2377 H  HE2  . LYS   A 1 110 ? 23.860 -19.516 -4.866  1.00 17.99 ?  110 LYS   A HE2  1 
ATOM   2378 H  HE3  . LYS   A 1 110 ? 24.572 -18.590 -3.788  1.00 17.99 ?  110 LYS   A HE3  1 
ATOM   2379 H  HZ1  . LYS   A 1 110 ? 22.695 -19.519 -2.922  1.00 18.35 ?  110 LYS   A HZ1  1 
ATOM   2380 H  HZ2  . LYS   A 1 110 ? 22.515 -18.082 -2.969  1.00 18.35 ?  110 LYS   A HZ2  1 
ATOM   2381 H  HZ3  . LYS   A 1 110 ? 21.866 -18.926 -3.951  1.00 18.35 ?  110 LYS   A HZ3  1 
ATOM   2382 N  N    . SER   A 1 111 ? 26.134 -12.999 -4.953  1.00 11.56 ?  111 SER   A N    1 
ATOM   2383 C  CA   . SER   A 1 111 ? 27.466 -12.687 -4.440  1.00 11.80 ?  111 SER   A CA   1 
ATOM   2384 C  C    . SER   A 1 111 ? 27.400 -11.640 -3.333  1.00 11.41 ?  111 SER   A C    1 
ATOM   2385 O  O    . SER   A 1 111 ? 28.095 -11.745 -2.316  1.00 11.98 ?  111 SER   A O    1 
ATOM   2386 C  CB   . SER   A 1 111 ? 28.350 -12.193 -5.585  1.00 13.10 ?  111 SER   A CB   1 
ATOM   2387 O  OG   . SER   A 1 111 ? 28.445 -13.184 -6.599  1.00 15.23 ?  111 SER   A OG   1 
ATOM   2388 H  H    . SER   A 1 111 ? 26.030 -12.875 -5.795  1.00 13.92 ?  111 SER   A H    1 
ATOM   2389 H  HA   . SER   A 1 111 ? 27.861 -13.496 -4.076  1.00 14.21 ?  111 SER   A HA   1 
ATOM   2390 H  HB2  . SER   A 1 111 ? 27.950 -11.395 -5.967  1.00 15.76 ?  111 SER   A HB2  1 
ATOM   2391 H  HB3  . SER   A 1 111 ? 29.229 -11.991 -5.236  1.00 15.76 ?  111 SER   A HB3  1 
ATOM   2392 H  HG   . SER   A 1 111 ? 28.951 -12.901 -7.218  1.00 18.32 ?  111 SER   A HG   1 
ATOM   2393 N  N    . ALA   A 1 112 ? 26.552 -10.625 -3.509  1.00 11.66 ?  112 ALA   A N    1 
ATOM   2394 C  CA   . ALA   A 1 112 ? 26.407 -9.589  -2.491  1.00 11.45 ?  112 ALA   A CA   1 
ATOM   2395 C  C    . ALA   A 1 112 ? 25.933 -10.187 -1.168  1.00 11.42 ?  112 ALA   A C    1 
ATOM   2396 O  O    . ALA   A 1 112 ? 26.484 -9.891  -0.100  1.00 11.90 ?  112 ALA   A O    1 
ATOM   2397 C  CB   . ALA   A 1 112 ? 25.445 -8.505  -2.986  1.00 11.88 ?  112 ALA   A CB   1 
ATOM   2398 H  H    . ALA   A 1 112 ? 26.057 -10.512 -4.202  1.00 14.04 ?  112 ALA   A H    1 
ATOM   2399 H  HA   . ALA   A 1 112 ? 27.267 -9.167  -2.338  1.00 13.78 ?  112 ALA   A HA   1 
ATOM   2400 H  HB1  . ALA   A 1 112 ? 25.375 -7.803  -2.310  1.00 14.30 ?  112 ALA   A HB1  1 
ATOM   2401 H  HB2  . ALA   A 1 112 ? 25.786 -8.122  -3.811  1.00 14.30 ?  112 ALA   A HB2  1 
ATOM   2402 H  HB3  . ALA   A 1 112 ? 24.570 -8.893  -3.140  1.00 14.30 ?  112 ALA   A HB3  1 
ATOM   2403 N  N    . TYR   A 1 113 ? 24.897 -11.029 -1.216  1.00 11.64 ?  113 TYR   A N    1 
ATOM   2404 C  CA   . TYR   A 1 113 ? 24.386 -11.633 0.010   1.00 11.13 ?  113 TYR   A CA   1 
ATOM   2405 C  C    . TYR   A 1 113 ? 25.389 -12.584 0.659   1.00 10.67 ?  113 TYR   A C    1 
ATOM   2406 O  O    . TYR   A 1 113 ? 25.345 -12.769 1.881   1.00 11.44 ?  113 TYR   A O    1 
ATOM   2407 C  CB   . TYR   A 1 113 ? 23.072 -12.363 -0.266  1.00 11.72 ?  113 TYR   A CB   1 
ATOM   2408 C  CG   . TYR   A 1 113 ? 21.855 -11.468 -0.179  1.00 11.46 ?  113 TYR   A CG   1 
ATOM   2409 C  CD1  . TYR   A 1 113 ? 21.495 -10.865 1.023   1.00 11.63 ?  113 TYR   A CD1  1 
ATOM   2410 C  CD2  . TYR   A 1 113 ? 21.048 -11.244 -1.288  1.00 11.57 ?  113 TYR   A CD2  1 
ATOM   2411 C  CE1  . TYR   A 1 113 ? 20.367 -10.070 1.118   1.00 12.06 ?  113 TYR   A CE1  1 
ATOM   2412 C  CE2  . TYR   A 1 113 ? 19.898 -10.443 -1.198  1.00 12.06 ?  113 TYR   A CE2  1 
ATOM   2413 C  CZ   . TYR   A 1 113 ? 19.574 -9.861  0.009   1.00 11.89 ?  113 TYR   A CZ   1 
ATOM   2414 O  OH   . TYR   A 1 113 ? 18.449 -9.069  0.137   1.00 12.31 ?  113 TYR   A OH   1 
ATOM   2415 H  H    . TYR   A 1 113 ? 24.485 -11.253 -1.937  1.00 14.02 ?  113 TYR   A H    1 
ATOM   2416 H  HA   . TYR   A 1 113 ? 24.207 -10.928 0.647   1.00 13.41 ?  113 TYR   A HA   1 
ATOM   2417 H  HB2  . TYR   A 1 113 ? 23.098 -12.732 -1.162  1.00 14.11 ?  113 TYR   A HB2  1 
ATOM   2418 H  HB3  . TYR   A 1 113 ? 22.965 -13.072 0.383   1.00 14.11 ?  113 TYR   A HB3  1 
ATOM   2419 H  HD1  . TYR   A 1 113 ? 22.021 -11.008 1.778   1.00 14.00 ?  113 TYR   A HD1  1 
ATOM   2420 H  HD2  . TYR   A 1 113 ? 21.259 -11.646 -2.096  1.00 13.94 ?  113 TYR   A HD2  1 
ATOM   2421 H  HE1  . TYR   A 1 113 ? 20.146 -9.678  1.931   1.00 14.52 ?  113 TYR   A HE1  1 
ATOM   2422 H  HE2  . TYR   A 1 113 ? 19.356 -10.298 -1.943  1.00 14.52 ?  113 TYR   A HE2  1 
ATOM   2423 H  HH   . TYR   A 1 113 ? 18.053 -9.024  -0.608  1.00 14.81 ?  113 TYR   A HH   1 
ATOM   2424 N  N    . GLU   A 1 114 ? 26.287 -13.200 -0.126  1.00 11.09 ?  114 GLU   A N    1 
ATOM   2425 C  CA   . GLU   A 1 114 ? 27.281 -14.097 0.467   1.00 11.64 ?  114 GLU   A CA   1 
ATOM   2426 C  C    . GLU   A 1 114 ? 28.132 -13.386 1.515   1.00 11.56 ?  114 GLU   A C    1 
ATOM   2427 O  O    . GLU   A 1 114 ? 28.606 -14.021 2.467   1.00 11.79 ?  114 GLU   A O    1 
ATOM   2428 C  CB   . GLU   A 1 114 ? 28.149 -14.734 -0.627  1.00 11.54 ?  114 GLU   A CB   1 
ATOM   2429 C  CG   . GLU   A 1 114 ? 27.389 -15.799 -1.398  1.00 12.06 ?  114 GLU   A CG   1 
ATOM   2430 C  CD   . GLU   A 1 114 ? 28.095 -16.323 -2.642  1.00 12.48 ?  114 GLU   A CD   1 
ATOM   2431 O  OE1  . GLU   A 1 114 ? 29.044 -15.690 -3.140  1.00 12.75 ?  114 GLU   A OE1  1 
ATOM   2432 O  OE2  . GLU   A 1 114 ? 27.656 -17.381 -3.139  1.00 13.69 -1 114 GLU   A OE2  1 
ATOM   2433 H  H    . GLU   A 1 114 ? 26.344 -13.105 -0.989  1.00 13.36 ?  114 GLU   A H    1 
ATOM   2434 H  HA   . GLU   A 1 114 ? 26.809 -14.811 0.908   1.00 14.01 ?  114 GLU   A HA   1 
ATOM   2435 H  HB2  . GLU   A 1 114 ? 28.426 -14.053 -1.262  1.00 13.90 ?  114 GLU   A HB2  1 
ATOM   2436 H  HB3  . GLU   A 1 114 ? 28.919 -15.152 -0.224  1.00 13.90 ?  114 GLU   A HB3  1 
ATOM   2437 H  HG2  . GLU   A 1 114 ? 27.236 -16.559 -0.813  1.00 14.52 ?  114 GLU   A HG2  1 
ATOM   2438 H  HG3  . GLU   A 1 114 ? 26.532 -15.434 -1.680  1.00 14.52 ?  114 GLU   A HG3  1 
ATOM   2439 N  N    . ASN   A 1 115 ? 28.315 -12.067 1.381   1.00 11.25 ?  115 ASN   A N    1 
ATOM   2440 C  CA   . ASN   A 1 115 ? 29.082 -11.341 2.386   1.00 11.51 ?  115 ASN   A CA   1 
ATOM   2441 C  C    . ASN   A 1 115 ? 28.466 -11.475 3.775   1.00 11.40 ?  115 ASN   A C    1 
ATOM   2442 O  O    . ASN   A 1 115 ? 29.182 -11.402 4.781   1.00 11.72 ?  115 ASN   A O    1 
ATOM   2443 C  CB   . ASN   A 1 115 ? 29.189 -9.865  2.007   1.00 12.08 ?  115 ASN   A CB   1 
ATOM   2444 C  CG   . ASN   A 1 115 ? 29.988 -9.649  0.744   1.00 12.61 ?  115 ASN   A CG   1 
ATOM   2445 O  OD1  . ASN   A 1 115 ? 31.206 -9.753  0.756   1.00 16.20 ?  115 ASN   A OD1  1 
ATOM   2446 N  ND2  . ASN   A 1 115 ? 29.312 -9.341  -0.347  1.00 11.95 ?  115 ASN   A ND2  1 
ATOM   2447 H  H    . ASN   A 1 115 ? 28.011 -11.583 0.734   1.00 13.55 ?  115 ASN   A H    1 
ATOM   2448 H  HA   . ASN   A 1 115 ? 29.976 -11.705 2.425   1.00 13.86 ?  115 ASN   A HA   1 
ATOM   2449 H  HB2  . ASN   A 1 115 ? 28.295 -9.507  1.876   1.00 14.54 ?  115 ASN   A HB2  1 
ATOM   2450 H  HB3  . ASN   A 1 115 ? 29.627 -9.387  2.733   1.00 14.54 ?  115 ASN   A HB3  1 
ATOM   2451 H  HD21 . ASN   A 1 115 ? 29.725 -9.209  -1.089  1.00 14.39 ?  115 ASN   A HD21 1 
ATOM   2452 H  HD22 . ASN   A 1 115 ? 28.451 -9.297  -0.322  1.00 14.39 ?  115 ASN   A HD22 1 
ATOM   2453 N  N    . PHE   A 1 116 ? 27.137 -11.637 3.856   1.00 11.46 ?  116 PHE   A N    1 
ATOM   2454 C  CA   . PHE   A 1 116 ? 26.487 -11.736 5.160   1.00 11.26 ?  116 PHE   A CA   1 
ATOM   2455 C  C    . PHE   A 1 116 ? 26.962 -12.967 5.930   1.00 11.60 ?  116 PHE   A C    1 
ATOM   2456 O  O    . PHE   A 1 116 ? 26.894 -12.985 7.161   1.00 12.07 ?  116 PHE   A O    1 
ATOM   2457 C  CB   . PHE   A 1 116 ? 24.961 -11.865 5.021   1.00 11.47 ?  116 PHE   A CB   1 
ATOM   2458 C  CG   . PHE   A 1 116 ? 24.206 -10.619 4.557   1.00 11.55 ?  116 PHE   A CG   1 
ATOM   2459 C  CD1  . PHE   A 1 116 ? 24.779 -9.593  3.816   1.00 11.38 ?  116 PHE   A CD1  1 
ATOM   2460 C  CD2  . PHE   A 1 116 ? 22.857 -10.516 4.873   1.00 11.95 ?  116 PHE   A CD2  1 
ATOM   2461 C  CE1  . PHE   A 1 116 ? 24.013 -8.516  3.396   1.00 11.79 ?  116 PHE   A CE1  1 
ATOM   2462 C  CE2  . PHE   A 1 116 ? 22.093 -9.440  4.463   1.00 12.18 ?  116 PHE   A CE2  1 
ATOM   2463 C  CZ   . PHE   A 1 116 ? 22.664 -8.438  3.726   1.00 11.20 ?  116 PHE   A CZ   1 
ATOM   2464 H  H    . PHE   A 1 116 ? 26.600 -11.683 3.180   1.00 13.81 ?  116 PHE   A H    1 
ATOM   2465 H  HA   . PHE   A 1 116 ? 26.681 -10.945 5.685   1.00 13.56 ?  116 PHE   A HA   1 
ATOM   2466 H  HB2  . PHE   A 1 116 ? 24.778 -12.572 4.376   1.00 13.81 ?  116 PHE   A HB2  1 
ATOM   2467 H  HB3  . PHE   A 1 116 ? 24.601 -12.124 5.883   1.00 13.81 ?  116 PHE   A HB3  1 
ATOM   2468 H  HD1  . PHE   A 1 116 ? 25.671 -9.653  3.582   1.00 13.70 ?  116 PHE   A HD1  1 
ATOM   2469 H  HD2  . PHE   A 1 116 ? 22.447 -11.205 5.366   1.00 14.39 ?  116 PHE   A HD2  1 
ATOM   2470 H  HE1  . PHE   A 1 116 ? 24.406 -7.838  2.905   1.00 14.20 ?  116 PHE   A HE1  1 
ATOM   2471 H  HE2  . PHE   A 1 116 ? 21.187 -9.401  4.695   1.00 14.67 ?  116 PHE   A HE2  1 
ATOM   2472 H  HZ   . PHE   A 1 116 ? 22.155 -7.710  3.464   1.00 13.49 ?  116 PHE   A HZ   1 
ATOM   2473 N  N    . ASN   A 1 117 ? 27.407 -14.015 5.225   1.00 11.93 ?  117 ASN   A N    1 
ATOM   2474 C  CA   . ASN   A 1 117 ? 27.772 -15.258 5.897   1.00 12.13 ?  117 ASN   A CA   1 
ATOM   2475 C  C    . ASN   A 1 117 ? 29.030 -15.140 6.735   1.00 12.54 ?  117 ASN   A C    1 
ATOM   2476 O  O    . ASN   A 1 117 ? 29.328 -16.061 7.505   1.00 13.66 ?  117 ASN   A O    1 
ATOM   2477 C  CB   . ASN   A 1 117 ? 27.891 -16.386 4.879   1.00 12.02 ?  117 ASN   A CB   1 
ATOM   2478 C  CG   . ASN   A 1 117 ? 26.543 -16.770 4.333   1.00 12.16 ?  117 ASN   A CG   1 
ATOM   2479 O  OD1  . ASN   A 1 117 ? 25.566 -16.796 5.077   1.00 13.06 ?  117 ASN   A OD1  1 
ATOM   2480 N  ND2  . ASN   A 1 117 ? 26.461 -17.025 3.042   1.00 12.07 ?  117 ASN   A ND2  1 
ATOM   2481 H  H    . ASN   A 1 117 ? 27.489 -14.029 4.364   1.00 14.36 ?  117 ASN   A H    1 
ATOM   2482 H  HA   . ASN   A 1 117 ? 27.045 -15.488 6.499   1.00 14.61 ?  117 ASN   A HA   1 
ATOM   2483 H  HB2  . ASN   A 1 117 ? 28.448 -16.087 4.141   1.00 14.48 ?  117 ASN   A HB2  1 
ATOM   2484 H  HB3  . ASN   A 1 117 ? 28.279 -17.157 5.308   1.00 14.48 ?  117 ASN   A HB3  1 
ATOM   2485 H  HD21 . ASN   A 1 117 ? 25.708 -17.236 2.698   1.00 14.53 ?  117 ASN   A HD21 1 
ATOM   2486 H  HD22 . ASN   A 1 117 ? 27.167 -16.978 2.553   1.00 14.53 ?  117 ASN   A HD22 1 
ATOM   2487 N  N    . GLN   A 1 118 ? 29.762 -14.033 6.615   1.00 12.58 ?  118 GLN   A N    1 
ATOM   2488 C  CA   . GLN   A 1 118 ? 30.937 -13.794 7.438   1.00 13.23 ?  118 GLN   A CA   1 
ATOM   2489 C  C    . GLN   A 1 118 ? 30.597 -13.222 8.807   1.00 13.05 ?  118 GLN   A C    1 
ATOM   2490 O  O    . GLN   A 1 118 ? 31.512 -12.935 9.586   1.00 14.55 ?  118 GLN   A O    1 
ATOM   2491 C  CB   . GLN   A 1 118 ? 31.933 -12.893 6.706   1.00 13.57 ?  118 GLN   A CB   1 
ATOM   2492 C  CG   . GLN   A 1 118 ? 32.403 -13.470 5.381   1.00 13.23 ?  118 GLN   A CG   1 
ATOM   2493 C  CD   . GLN   A 1 118 ? 33.239 -14.731 5.556   1.00 13.77 ?  118 GLN   A CD   1 
ATOM   2494 O  OE1  . GLN   A 1 118 ? 34.101 -14.799 6.441   1.00 14.56 ?  118 GLN   A OE1  1 
ATOM   2495 N  NE2  . GLN   A 1 118 ? 32.993 -15.733 4.709   1.00 14.06 ?  118 GLN   A NE2  1 
ATOM   2496 H  H    . GLN   A 1 118 ? 29.583 -13.386 6.062   1.00 15.14 ?  118 GLN   A H    1 
ATOM   2497 H  HA   . GLN   A 1 118 ? 31.367 -14.650 7.582   1.00 15.93 ?  118 GLN   A HA   1 
ATOM   2498 H  HB2  . GLN   A 1 118 ? 31.513 -12.039 6.532   1.00 16.33 ?  118 GLN   A HB2  1 
ATOM   2499 H  HB3  . GLN   A 1 118 ? 32.711 -12.772 7.272   1.00 16.33 ?  118 GLN   A HB3  1 
ATOM   2500 H  HG2  . GLN   A 1 118 ? 31.631 -13.690 4.834   1.00 15.92 ?  118 GLN   A HG2  1 
ATOM   2501 H  HG3  . GLN   A 1 118 ? 32.950 -12.808 4.924   1.00 15.92 ?  118 GLN   A HG3  1 
ATOM   2502 H  HE21 . GLN   A 1 118 ? 32.382 -15.646 4.102   1.00 16.92 ?  118 GLN   A HE21 1 
ATOM   2503 H  HE22 . GLN   A 1 118 ? 33.435 -16.466 4.764   1.00 16.92 ?  118 GLN   A HE22 1 
ATOM   2504 N  N    . HIS   A 1 119 ? 29.309 -13.070 9.123   1.00 12.81 ?  119 HIS   A N    1 
ATOM   2505 C  CA   . HIS   A 1 119 ? 28.859 -12.460 10.369  1.00 13.25 ?  119 HIS   A CA   1 
ATOM   2506 C  C    . HIS   A 1 119 ? 27.716 -13.279 10.943  1.00 13.62 ?  119 HIS   A C    1 
ATOM   2507 O  O    . HIS   A 1 119 ? 26.772 -13.618 10.225  1.00 14.26 ?  119 HIS   A O    1 
ATOM   2508 C  CB   . HIS   A 1 119 ? 28.406 -11.029 10.092  1.00 13.91 ?  119 HIS   A CB   1 
ATOM   2509 C  CG   . HIS   A 1 119 ? 29.489 -10.221 9.476   1.00 15.02 ?  119 HIS   A CG   1 
ATOM   2510 N  ND1  . HIS   A 1 119 ? 30.459 -9.600  10.228  1.00 17.46 ?  119 HIS   A ND1  1 
ATOM   2511 C  CD2  . HIS   A 1 119 ? 29.823 -10.025 8.181   1.00 15.96 ?  119 HIS   A CD2  1 
ATOM   2512 C  CE1  . HIS   A 1 119 ? 31.325 -9.018  9.418   1.00 17.45 ?  119 HIS   A CE1  1 
ATOM   2513 N  NE2  . HIS   A 1 119 ? 30.970 -9.270  8.171   1.00 17.38 ?  119 HIS   A NE2  1 
ATOM   2514 H  H    . HIS   A 1 119 ? 28.656 -13.339 8.622   1.00 15.42 ?  119 HIS   A H    1 
ATOM   2515 H  HA   . HIS   A 1 119 ? 29.589 -12.450 11.008  1.00 15.95 ?  119 HIS   A HA   1 
ATOM   2516 H  HB2  . HIS   A 1 119 ? 27.654 -11.053 9.481   1.00 16.74 ?  119 HIS   A HB2  1 
ATOM   2517 H  HB3  . HIS   A 1 119 ? 28.152 -10.616 10.928  1.00 16.74 ?  119 HIS   A HB3  1 
ATOM   2518 H  HD2  . HIS   A 1 119 ? 29.366 -10.345 7.434   1.00 19.20 ?  119 HIS   A HD2  1 
ATOM   2519 H  HE1  . HIS   A 1 119 ? 32.061 -8.514  9.678   1.00 20.98 ?  119 HIS   A HE1  1 
ATOM   2520 H  HE2  . HIS   A 1 119 ? 31.373 -8.979  7.465   1.00 20.90 ?  119 HIS   A HE2  1 
ATOM   2521 N  N    . GLU   A 1 120 ? 27.803 -13.584 12.240  1.00 14.67 ?  120 GLU   A N    1 
ATOM   2522 C  CA   . GLU   A 1 120 ? 26.847 -14.511 12.842  1.00 16.99 ?  120 GLU   A CA   1 
ATOM   2523 C  C    . GLU   A 1 120 ? 25.432 -13.945 12.901  1.00 15.20 ?  120 GLU   A C    1 
ATOM   2524 O  O    . GLU   A 1 120 ? 24.458 -14.709 12.797  1.00 15.14 ?  120 GLU   A O    1 
ATOM   2525 C  CB   . GLU   A 1 120 ? 27.319 -14.909 14.244  1.00 22.75 ?  120 GLU   A CB   1 
ATOM   2526 C  CG   . GLU   A 1 120 ? 28.505 -15.860 14.255  1.00 30.80 ?  120 GLU   A CG   1 
ATOM   2527 C  CD   . GLU   A 1 120 ? 28.652 -16.590 15.574  1.00 37.86 ?  120 GLU   A CD   1 
ATOM   2528 O  OE1  . GLU   A 1 120 ? 28.290 -16.011 16.621  1.00 39.86 ?  120 GLU   A OE1  1 
ATOM   2529 O  OE2  . GLU   A 1 120 ? 29.124 -17.747 15.564  1.00 42.65 -1 120 GLU   A OE2  1 
ATOM   2530 H  H    . GLU   A 1 120 ? 28.401 -13.275 12.783  1.00 17.65 ?  120 GLU   A H    1 
ATOM   2531 H  HA   . GLU   A 1 120 ? 26.823 -15.318 12.312  1.00 20.43 ?  120 GLU   A HA   1 
ATOM   2532 H  HB2  . GLU   A 1 120 ? 27.584 -14.114 14.733  1.00 27.35 ?  120 GLU   A HB2  1 
ATOM   2533 H  HB3  . GLU   A 1 120 ? 26.591 -15.351 14.711  1.00 27.35 ?  120 GLU   A HB3  1 
ATOM   2534 H  HG2  . GLU   A 1 120 ? 28.395 -16.519 13.552  1.00 37.01 ?  120 GLU   A HG2  1 
ATOM   2535 H  HG3  . GLU   A 1 120 ? 29.322 -15.358 14.118  1.00 37.01 ?  120 GLU   A HG3  1 
ATOM   2536 N  N    . VAL   A 1 121 ? 25.300 -12.636 13.112  1.00 14.45 ?  121 VAL   A N    1 
ATOM   2537 C  CA   . VAL   A 1 121 ? 24.005 -11.972 13.231  1.00 14.40 ?  121 VAL   A CA   1 
ATOM   2538 C  C    . VAL   A 1 121 ? 24.117 -10.595 12.588  1.00 13.20 ?  121 VAL   A C    1 
ATOM   2539 O  O    . VAL   A 1 121 ? 25.089 -9.872  12.826  1.00 14.23 ?  121 VAL   A O    1 
ATOM   2540 C  CB   . VAL   A 1 121 ? 23.566 -11.821 14.706  1.00 17.45 ?  121 VAL   A CB   1 
ATOM   2541 C  CG1  . VAL   A 1 121 ? 22.178 -11.189 14.796  1.00 18.15 ?  121 VAL   A CG1  1 
ATOM   2542 C  CG2  . VAL   A 1 121 ? 23.579 -13.150 15.440  1.00 19.61 ?  121 VAL   A CG2  1 
ATOM   2543 H  H    . VAL   A 1 121 ? 25.964 -12.090 13.191  1.00 17.39 ?  121 VAL   A H    1 
ATOM   2544 H  HA   . VAL   A 1 121 ? 23.331 -12.487 12.761  1.00 17.32 ?  121 VAL   A HA   1 
ATOM   2545 H  HB   . VAL   A 1 121 ? 24.184 -11.233 15.160  1.00 20.98 ?  121 VAL   A HB   1 
ATOM   2546 H  HG11 . VAL   A 1 121 ? 21.862 -11.248 15.713  1.00 21.82 ?  121 VAL   A HG11 1 
ATOM   2547 H  HG12 . VAL   A 1 121 ? 22.233 -10.260 14.526  1.00 21.82 ?  121 VAL   A HG12 1 
ATOM   2548 H  HG13 . VAL   A 1 121 ? 21.572 -11.670 14.210  1.00 21.82 ?  121 VAL   A HG13 1 
ATOM   2549 H  HG21 . VAL   A 1 121 ? 23.232 -13.019 16.342  1.00 23.58 ?  121 VAL   A HG21 1 
ATOM   2550 H  HG22 . VAL   A 1 121 ? 23.015 -13.783 14.965  1.00 23.58 ?  121 VAL   A HG22 1 
ATOM   2551 H  HG23 . VAL   A 1 121 ? 24.486 -13.482 15.484  1.00 23.58 ?  121 VAL   A HG23 1 
ATOM   2552 N  N    . LEU   A 1 122 ? 23.103 -10.208 11.805  1.00 12.67 ?  122 LEU   A N    1 
ATOM   2553 C  CA   . LEU   A 1 122 ? 23.103 -8.910  11.136  1.00 12.43 ?  122 LEU   A CA   1 
ATOM   2554 C  C    . LEU   A 1 122 ? 21.706 -8.314  11.098  1.00 12.52 ?  122 LEU   A C    1 
ATOM   2555 O  O    . LEU   A 1 122 ? 20.713 -9.032  10.964  1.00 13.63 ?  122 LEU   A O    1 
ATOM   2556 C  CB   . LEU   A 1 122 ? 23.530 -9.010  9.668   1.00 13.73 ?  122 LEU   A CB   1 
ATOM   2557 C  CG   . LEU   A 1 122 ? 24.742 -9.858  9.312   1.00 14.03 ?  122 LEU   A CG   1 
ATOM   2558 C  CD1  . LEU   A 1 122 ? 24.342 -11.309 9.089   1.00 14.87 ?  122 LEU   A CD1  1 
ATOM   2559 C  CD2  . LEU   A 1 122 ? 25.433 -9.298  8.079   1.00 13.55 ?  122 LEU   A CD2  1 
ATOM   2560 H  H    . LEU   A 1 122 ? 22.394 -10.679 11.649  1.00 15.26 ?  122 LEU   A H    1 
ATOM   2561 H  HA   . LEU   A 1 122 ? 23.699 -8.297  11.599  1.00 14.96 ?  122 LEU   A HA   1 
ATOM   2562 H  HB2  . LEU   A 1 122 ? 22.792 -9.373  9.166   1.00 16.52 ?  122 LEU   A HB2  1 
ATOM   2563 H  HB3  . LEU   A 1 122 ? 23.726 -8.117  9.353   1.00 16.52 ?  122 LEU   A HB3  1 
ATOM   2564 H  HG   . LEU   A 1 122 ? 25.388 -9.837  10.039  1.00 16.88 ?  122 LEU   A HG   1 
ATOM   2565 H  HD11 . LEU   A 1 122 ? 25.118 -11.824 8.818   1.00 17.89 ?  122 LEU   A HD11 1 
ATOM   2566 H  HD12 . LEU   A 1 122 ? 23.983 -11.668 9.917   1.00 17.89 ?  122 LEU   A HD12 1 
ATOM   2567 H  HD13 . LEU   A 1 122 ? 23.664 -11.347 8.394   1.00 17.89 ?  122 LEU   A HD13 1 
ATOM   2568 H  HD21 . LEU   A 1 122 ? 26.186 -9.870  7.838   1.00 16.31 ?  122 LEU   A HD21 1 
ATOM   2569 H  HD22 . LEU   A 1 122 ? 24.802 -9.267  7.344   1.00 16.31 ?  122 LEU   A HD22 1 
ATOM   2570 H  HD23 . LEU   A 1 122 ? 25.759 -8.403  8.273   1.00 16.31 ?  122 LEU   A HD23 1 
ATOM   2571 N  N    A LEU   A 1 123 ? 21.646 -6.988  11.189  0.72 12.00 ?  123 LEU   A N    1 
ATOM   2572 N  N    B LEU   A 1 123 ? 21.652 -6.990  11.233  0.28 12.22 ?  123 LEU   A N    1 
ATOM   2573 C  CA   A LEU   A 1 123 ? 20.479 -6.199  10.810  0.72 11.59 ?  123 LEU   A CA   1 
ATOM   2574 C  CA   B LEU   A 1 123 ? 20.479 -6.185  10.914  0.28 12.09 ?  123 LEU   A CA   1 
ATOM   2575 C  C    A LEU   A 1 123 ? 20.718 -5.683  9.399   0.72 10.88 ?  123 LEU   A C    1 
ATOM   2576 C  C    B LEU   A 1 123 ? 20.722 -5.631  9.517   0.28 11.47 ?  123 LEU   A C    1 
ATOM   2577 O  O    A LEU   A 1 123 ? 21.799 -5.156  9.121   0.72 10.90 ?  123 LEU   A O    1 
ATOM   2578 O  O    B LEU   A 1 123 ? 21.650 -4.841  9.316   0.28 11.17 ?  123 LEU   A O    1 
ATOM   2579 C  CB   A LEU   A 1 123 ? 20.340 -5.006  11.754  0.72 12.12 ?  123 LEU   A CB   1 
ATOM   2580 C  CB   B LEU   A 1 123 ? 20.331 -5.049  11.926  0.28 12.53 ?  123 LEU   A CB   1 
ATOM   2581 C  CG   A LEU   A 1 123 ? 19.268 -3.967  11.420  0.72 13.05 ?  123 LEU   A CG   1 
ATOM   2582 C  CG   B LEU   A 1 123 ? 19.371 -3.922  11.527  0.28 12.43 ?  123 LEU   A CG   1 
ATOM   2583 C  CD1  A LEU   A 1 123 ? 17.886 -4.597  11.449  0.72 13.75 ?  123 LEU   A CD1  1 
ATOM   2584 C  CD1  B LEU   A 1 123 ? 17.937 -4.426  11.471  0.28 12.59 ?  123 LEU   A CD1  1 
ATOM   2585 C  CD2  A LEU   A 1 123 ? 19.353 -2.788  12.387  0.72 13.79 ?  123 LEU   A CD2  1 
ATOM   2586 C  CD2  B LEU   A 1 123 ? 19.496 -2.723  12.459  0.28 12.60 ?  123 LEU   A CD2  1 
ATOM   2587 H  H    A LEU   A 1 123 ? 22.300 -6.504  11.478  0.72 14.45 ?  123 LEU   A H    1 
ATOM   2588 H  H    B LEU   A 1 123 ? 22.312 -6.513  11.507  0.28 14.71 ?  123 LEU   A H    1 
ATOM   2589 H  HA   A LEU   A 1 123 ? 19.676 -6.741  10.834  0.72 13.96 ?  123 LEU   A HA   1 
ATOM   2590 H  HA   B LEU   A 1 123 ? 19.677 -6.723  10.912  0.28 14.56 ?  123 LEU   A HA   1 
ATOM   2591 H  HB2  A LEU   A 1 123 ? 20.133 -5.345  12.640  0.72 14.59 ?  123 LEU   A HB2  1 
ATOM   2592 H  HB2  B LEU   A 1 123 ? 20.005 -5.425  12.760  0.28 15.08 ?  123 LEU   A HB2  1 
ATOM   2593 H  HB3  A LEU   A 1 123 ? 21.186 -4.539  11.781  0.72 14.59 ?  123 LEU   A HB3  1 
ATOM   2594 H  HB3  B LEU   A 1 123 ? 21.202 -4.648  12.072  0.28 15.08 ?  123 LEU   A HB3  1 
ATOM   2595 H  HG   A LEU   A 1 123 ? 19.418 -3.622  10.524  0.72 15.70 ?  123 LEU   A HG   1 
ATOM   2596 H  HG   B LEU   A 1 123 ? 19.601 -3.607  10.643  0.28 14.96 ?  123 LEU   A HG   1 
ATOM   2597 H  HD11 A LEU   A 1 123 ? 17.220 -3.912  11.294  0.72 16.55 ?  123 LEU   A HD11 1 
ATOM   2598 H  HD11 B LEU   A 1 123 ? 17.354 -3.689  11.237  0.28 15.15 ?  123 LEU   A HD11 1 
ATOM   2599 H  HD12 A LEU   A 1 123 ? 17.835 -5.273  10.754  0.72 16.55 ?  123 LEU   A HD12 1 
ATOM   2600 H  HD12 B LEU   A 1 123 ? 17.876 -5.124  10.799  0.28 15.15 ?  123 LEU   A HD12 1 
ATOM   2601 H  HD13 A LEU   A 1 123 ? 17.747 -5.007  12.318  0.72 16.55 ?  123 LEU   A HD13 1 
ATOM   2602 H  HD13 B LEU   A 1 123 ? 17.692 -4.781  12.340  0.28 15.15 ?  123 LEU   A HD13 1 
ATOM   2603 H  HD21 A LEU   A 1 123 ? 18.668 -2.138  12.162  0.72 16.60 ?  123 LEU   A HD21 1 
ATOM   2604 H  HD21 B LEU   A 1 123 ? 18.873 -2.036  12.171  0.28 15.17 ?  123 LEU   A HD21 1 
ATOM   2605 H  HD22 A LEU   A 1 123 ? 19.215 -3.112  13.292  0.72 16.60 ?  123 LEU   A HD22 1 
ATOM   2606 H  HD22 B LEU   A 1 123 ? 19.287 -3.000  13.363  0.28 15.17 ?  123 LEU   A HD22 1 
ATOM   2607 H  HD23 A LEU   A 1 123 ? 20.231 -2.382  12.314  0.72 16.60 ?  123 LEU   A HD23 1 
ATOM   2608 H  HD23 B LEU   A 1 123 ? 20.404 -2.384  12.416  0.28 15.17 ?  123 LEU   A HD23 1 
ATOM   2609 N  N    A ALA   A 1 124 ? 19.725 -5.812  8.514   0.72 10.37 ?  124 ALA   A N    1 
ATOM   2610 N  N    B ALA   A 1 124 ? 19.907 -6.043  8.556   0.28 11.08 ?  124 ALA   A N    1 
ATOM   2611 C  CA   A ALA   A 1 124 ? 20.001 -5.539  7.110   0.72 10.49 ?  124 ALA   A CA   1 
ATOM   2612 C  CA   B ALA   A 1 124 ? 20.171 -5.765  7.154   0.28 10.97 ?  124 ALA   A CA   1 
ATOM   2613 C  C    A ALA   A 1 124 ? 18.764 -5.114  6.328   0.72 10.73 ?  124 ALA   A C    1 
ATOM   2614 C  C    B ALA   A 1 124 ? 18.951 -5.191  6.452   0.28 10.57 ?  124 ALA   A C    1 
ATOM   2615 O  O    A ALA   A 1 124 ? 17.638 -5.495  6.678   0.72 11.60 ?  124 ALA   A O    1 
ATOM   2616 O  O    B ALA   A 1 124 ? 17.813 -5.398  6.887   0.28 10.80 ?  124 ALA   A O    1 
ATOM   2617 C  CB   A ALA   A 1 124 ? 20.617 -6.770  6.433   0.72 11.27 ?  124 ALA   A CB   1 
ATOM   2618 C  CB   B ALA   A 1 124 ? 20.610 -7.046  6.430   0.28 11.58 ?  124 ALA   A CB   1 
ATOM   2619 H  H    A ALA   A 1 124 ? 18.912 -6.035  8.698   0.72 12.50 ?  124 ALA   A H    1 
ATOM   2620 H  H    B ALA   A 1 124 ? 19.190 -6.503  8.690   0.28 13.35 ?  124 ALA   A H    1 
ATOM   2621 H  HA   A ALA   A 1 124 ? 20.653 -4.821  7.067   0.72 12.64 ?  124 ALA   A HA   1 
ATOM   2622 H  HA   B ALA   A 1 124 ? 20.898 -5.127  7.099   0.28 13.21 ?  124 ALA   A HA   1 
ATOM   2623 H  HB1  A ALA   A 1 124 ? 20.800 -6.565  5.503   0.72 13.57 ?  124 ALA   A HB1  1 
ATOM   2624 H  HB1  B ALA   A 1 124 ? 20.788 -6.840  5.499   0.28 13.95 ?  124 ALA   A HB1  1 
ATOM   2625 H  HB2  A ALA   A 1 124 ? 21.449 -6.999  6.887   0.72 13.57 ?  124 ALA   A HB2  1 
ATOM   2626 H  HB2  B ALA   A 1 124 ? 21.418 -7.391  6.850   0.28 13.95 ?  124 ALA   A HB2  1 
ATOM   2627 H  HB3  A ALA   A 1 124 ? 19.997 -7.511  6.496   0.72 13.57 ?  124 ALA   A HB3  1 
ATOM   2628 H  HB3  B ALA   A 1 124 ? 19.901 -7.705  6.494   0.28 13.95 ?  124 ALA   A HB3  1 
ATOM   2629 N  N    A PRO   A 1 125 ? 18.952 -4.371  5.240   0.72 10.64 ?  125 PRO   A N    1 
ATOM   2630 N  N    B PRO   A 1 125 ? 19.163 -4.461  5.345   0.28 9.57  ?  125 PRO   A N    1 
ATOM   2631 C  CA   A PRO   A 1 125 ? 17.897 -4.160  4.250   0.72 11.29 ?  125 PRO   A CA   1 
ATOM   2632 C  CA   B PRO   A 1 125 ? 18.051 -4.051  4.484   0.28 9.94  ?  125 PRO   A CA   1 
ATOM   2633 C  C    A PRO   A 1 125 ? 17.970 -5.233  3.167   0.72 11.01 ?  125 PRO   A C    1 
ATOM   2634 C  C    B PRO   A 1 125 ? 17.919 -5.056  3.351   0.28 10.67 ?  125 PRO   A C    1 
ATOM   2635 O  O    A PRO   A 1 125 ? 18.947 -5.979  3.055   0.72 11.46 ?  125 PRO   A O    1 
ATOM   2636 O  O    B PRO   A 1 125 ? 18.771 -5.944  3.238   0.28 11.07 ?  125 PRO   A O    1 
ATOM   2637 C  CB   A PRO   A 1 125 ? 18.304 -2.808  3.652   0.72 11.32 ?  125 PRO   A CB   1 
ATOM   2638 C  CB   B PRO   A 1 125 ? 18.541 -2.701  3.952   0.28 9.43  ?  125 PRO   A CB   1 
ATOM   2639 C  CG   A PRO   A 1 125 ? 19.812 -2.928  3.586   0.72 11.80 ?  125 PRO   A CG   1 
ATOM   2640 C  CG   B PRO   A 1 125 ? 20.029 -2.952  3.743   0.28 9.23  ?  125 PRO   A CG   1 
ATOM   2641 C  CD   A PRO   A 1 125 ? 20.193 -3.664  4.864   0.72 11.43 ?  125 PRO   A CD   1 
ATOM   2642 C  CD   B PRO   A 1 125 ? 20.447 -3.949  4.830   0.28 9.01  ?  125 PRO   A CD   1 
ATOM   2643 H  HA   A PRO   A 1 125 ? 17.015 -4.126  4.656   0.72 13.59 ?  125 PRO   A HA   1 
ATOM   2644 H  HA   B PRO   A 1 125 ? 17.222 -3.948  4.980   0.28 11.97 ?  125 PRO   A HA   1 
ATOM   2645 H  HB2  A PRO   A 1 125 ? 17.911 -2.707  2.769   0.72 13.63 ?  125 PRO   A HB2  1 
ATOM   2646 H  HB2  B PRO   A 1 125 ? 18.099 -2.485  3.115   0.28 11.36 ?  125 PRO   A HB2  1 
ATOM   2647 H  HB3  A PRO   A 1 125 ? 18.025 -2.089  4.244   0.72 13.63 ?  125 PRO   A HB3  1 
ATOM   2648 H  HB3  B PRO   A 1 125 ? 18.394 -2.003  4.614   0.28 11.36 ?  125 PRO   A HB3  1 
ATOM   2649 H  HG2  A PRO   A 1 125 ? 20.066 -3.444  2.806   0.72 14.21 ?  125 PRO   A HG2  1 
ATOM   2650 H  HG2  B PRO   A 1 125 ? 20.169 -3.327  2.859   0.28 11.12 ?  125 PRO   A HG2  1 
ATOM   2651 H  HG3  A PRO   A 1 125 ? 20.208 -2.045  3.563   0.72 14.21 ?  125 PRO   A HG3  1 
ATOM   2652 H  HG3  B PRO   A 1 125 ? 20.514 -2.117  3.837   0.28 11.12 ?  125 PRO   A HG3  1 
ATOM   2653 H  HD2  A PRO   A 1 125 ? 20.908 -4.291  4.696   0.72 13.77 ?  125 PRO   A HD2  1 
ATOM   2654 H  HD2  B PRO   A 1 125 ? 20.977 -4.665  4.440   0.28 10.86 ?  125 PRO   A HD2  1 
ATOM   2655 H  HD3  A PRO   A 1 125 ? 20.436 -3.024  5.559   0.72 13.77 ?  125 PRO   A HD3  1 
ATOM   2656 H  HD3  B PRO   A 1 125 ? 20.931 -3.492  5.534   0.28 10.86 ?  125 PRO   A HD3  1 
ATOM   2657 N  N    A LEU   A 1 126 ? 16.924 -5.273  2.344   0.72 10.94 ?  126 LEU   A N    1 
ATOM   2658 N  N    B LEU   A 1 126 ? 16.900 -4.945  2.499   0.28 11.07 ?  126 LEU   A N    1 
ATOM   2659 C  CA   A LEU   A 1 126 ? 16.944 -6.092  1.141   0.72 11.45 ?  126 LEU   A CA   1 
ATOM   2660 C  CA   B LEU   A 1 126 ? 16.855 -5.777  1.299   0.28 11.05 ?  126 LEU   A CA   1 
ATOM   2661 C  C    A LEU   A 1 126 ? 17.864 -5.468  0.094   0.72 11.58 ?  126 LEU   A C    1 
ATOM   2662 C  C    B LEU   A 1 126 ? 17.792 -5.185  0.252   0.28 11.02 ?  126 LEU   A C    1 
ATOM   2663 O  O    A LEU   A 1 126 ? 17.618 -4.361  -0.398  0.72 12.28 ?  126 LEU   A O    1 
ATOM   2664 O  O    B LEU   A 1 126 ? 17.556 -4.082  -0.250  0.28 12.10 ?  126 LEU   A O    1 
ATOM   2665 C  CB   A LEU   A 1 126 ? 15.531 -6.256  0.593   0.72 12.27 ?  126 LEU   A CB   1 
ATOM   2666 C  CB   B LEU   A 1 126 ? 15.440 -5.862  0.740   0.28 11.82 ?  126 LEU   A CB   1 
ATOM   2667 C  CG   A LEU   A 1 126 ? 14.647 -7.225  1.381   0.72 13.65 ?  126 LEU   A CG   1 
ATOM   2668 C  CG   B LEU   A 1 126 ? 14.476 -6.809  1.448   0.28 12.03 ?  126 LEU   A CG   1 
ATOM   2669 C  CD1  A LEU   A 1 126 ? 13.210 -7.102  0.925   0.72 15.15 ?  126 LEU   A CD1  1 
ATOM   2670 C  CD1  B LEU   A 1 126 ? 13.100 -6.712  0.816   0.28 12.45 ?  126 LEU   A CD1  1 
ATOM   2671 C  CD2  A LEU   A 1 126 ? 15.132 -8.656  1.214   0.72 13.64 ?  126 LEU   A CD2  1 
ATOM   2672 C  CD2  B LEU   A 1 126 ? 14.978 -8.244  1.407   0.28 12.13 ?  126 LEU   A CD2  1 
ATOM   2673 H  H    A LEU   A 1 126 ? 16.199 -4.826  2.455   0.72 13.18 ?  126 LEU   A H    1 
ATOM   2674 H  H    B LEU   A 1 126 ? 16.221 -4.406  2.595   0.28 13.33 ?  126 LEU   A H    1 
ATOM   2675 H  HA   A LEU   A 1 126 ? 17.288 -6.973  1.357   0.72 13.79 ?  126 LEU   A HA   1 
ATOM   2676 H  HA   B LEU   A 1 126 ? 17.163 -6.668  1.526   0.28 13.31 ?  126 LEU   A HA   1 
ATOM   2677 H  HB2  A LEU   A 1 126 ? 15.089 -5.393  0.604   0.72 14.77 ?  126 LEU   A HB2  1 
ATOM   2678 H  HB2  B LEU   A 1 126 ? 15.048 -4.978  0.769   0.28 14.23 ?  126 LEU   A HB2  1 
ATOM   2679 H  HB3  A LEU   A 1 126 ? 15.581 -6.586  -0.316  0.72 14.77 ?  126 LEU   A HB3  1 
ATOM   2680 H  HB3  B LEU   A 1 126 ? 15.506 -6.156  -0.183  0.28 14.23 ?  126 LEU   A HB3  1 
ATOM   2681 H  HG   A LEU   A 1 126 ? 14.682 -7.004  2.325   0.72 16.42 ?  126 LEU   A HG   1 
ATOM   2682 H  HG   B LEU   A 1 126 ? 14.397 -6.546  2.376   0.28 14.48 ?  126 LEU   A HG   1 
ATOM   2683 H  HD11 A LEU   A 1 126 ? 12.661 -7.725  1.429   0.72 18.22 ?  126 LEU   A HD11 1 
ATOM   2684 H  HD11 B LEU   A 1 126 ? 12.497 -7.316  1.279   0.28 14.99 ?  126 LEU   A HD11 1 
ATOM   2685 H  HD12 A LEU   A 1 126 ? 12.907 -6.195  1.078   0.72 18.22 ?  126 LEU   A HD12 1 
ATOM   2686 H  HD12 B LEU   A 1 126 ? 12.781 -5.801  0.892   0.28 14.99 ?  126 LEU   A HD12 1 
ATOM   2687 H  HD13 A LEU   A 1 126 ? 13.161 -7.313  -0.022  0.72 18.22 ?  126 LEU   A HD13 1 
ATOM   2688 H  HD13 B LEU   A 1 126 ? 13.164 -6.965  -0.120  0.28 14.99 ?  126 LEU   A HD13 1 
ATOM   2689 H  HD21 A LEU   A 1 126 ? 14.475 -9.261  1.587   0.72 16.42 ?  126 LEU   A HD21 1 
ATOM   2690 H  HD21 B LEU   A 1 126 ? 14.266 -8.836  1.687   0.28 14.60 ?  126 LEU   A HD21 1 
ATOM   2691 H  HD22 A LEU   A 1 126 ? 15.254 -8.838  0.269   0.72 16.42 ?  126 LEU   A HD22 1 
ATOM   2692 H  HD22 B LEU   A 1 126 ? 15.250 -8.455  0.499   0.28 14.60 ?  126 LEU   A HD22 1 
ATOM   2693 H  HD23 A LEU   A 1 126 ? 15.978 -8.757  1.680   0.72 16.42 ?  126 LEU   A HD23 1 
ATOM   2694 H  HD23 B LEU   A 1 126 ? 15.737 -8.328  2.006   0.28 14.60 ?  126 LEU   A HD23 1 
ATOM   2695 N  N    A LEU   A 1 127 ? 18.918 -6.193  -0.259  0.72 11.05 ?  127 LEU   A N    1 
ATOM   2696 N  N    B LEU   A 1 127 ? 18.844 -5.916  -0.099  0.28 10.54 ?  127 LEU   A N    1 
ATOM   2697 C  CA   A LEU   A 1 127 ? 19.906 -5.685  -1.194  0.72 10.84 ?  127 LEU   A CA   1 
ATOM   2698 C  CA   B LEU   A 1 127 ? 19.820 -5.383  -1.036  0.28 10.62 ?  127 LEU   A CA   1 
ATOM   2699 C  C    A LEU   A 1 127 ? 19.295 -5.505  -2.572  0.72 10.53 ?  127 LEU   A C    1 
ATOM   2700 C  C    B LEU   A 1 127 ? 19.244 -5.305  -2.444  0.28 10.67 ?  127 LEU   A C    1 
ATOM   2701 O  O    A LEU   A 1 127 ? 18.476 -6.310  -3.026  0.72 10.78 ?  127 LEU   A O    1 
ATOM   2702 O  O    B LEU   A 1 127 ? 18.398 -6.108  -2.846  0.28 11.12 ?  127 LEU   A O    1 
ATOM   2703 C  CB   A LEU   A 1 127 ? 21.083 -6.655  -1.278  0.72 11.55 ?  127 LEU   A CB   1 
ATOM   2704 C  CB   B LEU   A 1 127 ? 21.076 -6.250  -1.064  0.28 10.87 ?  127 LEU   A CB   1 
ATOM   2705 C  CG   A LEU   A 1 127 ? 21.876 -6.893  0.007   0.72 12.13 ?  127 LEU   A CG   1 
ATOM   2706 C  CG   B LEU   A 1 127 ? 21.879 -6.288  0.235   0.28 11.08 ?  127 LEU   A CG   1 
ATOM   2707 C  CD1  A LEU   A 1 127 ? 22.981 -7.895  -0.258  0.72 12.70 ?  127 LEU   A CD1  1 
ATOM   2708 C  CD1  B LEU   A 1 127 ? 23.046 -7.250  0.113   0.28 11.62 ?  127 LEU   A CD1  1 
ATOM   2709 C  CD2  A LEU   A 1 127 ? 22.461 -5.602  0.533   0.72 13.20 ?  127 LEU   A CD2  1 
ATOM   2710 C  CD2  B LEU   A 1 127 ? 22.361 -4.892  0.615   0.28 11.21 ?  127 LEU   A CD2  1 
ATOM   2711 H  H    A LEU   A 1 127 ? 19.082 -6.986  0.034   0.72 13.31 ?  127 LEU   A H    1 
ATOM   2712 H  H    B LEU   A 1 127 ? 19.008 -6.711  0.190   0.28 12.69 ?  127 LEU   A H    1 
ATOM   2713 H  HA   A LEU   A 1 127 ? 20.232 -4.826  -0.883  0.72 13.06 ?  127 LEU   A HA   1 
ATOM   2714 H  HA   B LEU   A 1 127 ? 20.065 -4.488  -0.751  0.28 12.79 ?  127 LEU   A HA   1 
ATOM   2715 H  HB2  A LEU   A 1 127 ? 20.743 -7.517  -1.568  0.72 13.91 ?  127 LEU   A HB2  1 
ATOM   2716 H  HB2  B LEU   A 1 127 ? 20.812 -7.157  -1.280  0.28 13.09 ?  127 LEU   A HB2  1 
ATOM   2717 H  HB3  A LEU   A 1 127 ? 21.705 -6.318  -1.940  0.72 13.91 ?  127 LEU   A HB3  1 
ATOM   2718 H  HB3  B LEU   A 1 127 ? 21.656 -5.907  -1.764  0.28 13.09 ?  127 LEU   A HB3  1 
ATOM   2719 H  HG   A LEU   A 1 127 ? 21.284 -7.261  0.685   0.72 14.60 ?  127 LEU   A HG   1 
ATOM   2720 H  HG   B LEU   A 1 127 ? 21.302 -6.609  0.943   0.28 13.34 ?  127 LEU   A HG   1 
ATOM   2721 H  HD11 A LEU   A 1 127 ? 23.459 -8.066  0.570   0.72 15.28 ?  127 LEU   A HD11 1 
ATOM   2722 H  HD11 B LEU   A 1 127 ? 23.562 -7.218  0.932   0.28 13.99 ?  127 LEU   A HD11 1 
ATOM   2723 H  HD12 A LEU   A 1 127 ? 22.589 -8.722  -0.586  0.72 15.28 ?  127 LEU   A HD12 1 
ATOM   2724 H  HD12 B LEU   A 1 127 ? 22.702 -8.146  -0.028  0.28 13.99 ?  127 LEU   A HD12 1 
ATOM   2725 H  HD13 A LEU   A 1 127 ? 23.586 -7.531  -0.920  0.72 15.28 ?  127 LEU   A HD13 1 
ATOM   2726 H  HD13 B LEU   A 1 127 ? 23.597 -6.984  -0.638  0.28 13.99 ?  127 LEU   A HD13 1 
ATOM   2727 H  HD21 A LEU   A 1 127 ? 23.048 -5.803  1.278   0.72 15.89 ?  127 LEU   A HD21 1 
ATOM   2728 H  HD21 B LEU   A 1 127 ? 23.000 -4.969  1.339   0.28 13.50 ?  127 LEU   A HD21 1 
ATOM   2729 H  HD22 A LEU   A 1 127 ? 22.965 -5.174  -0.178  0.72 15.89 ?  127 LEU   A HD22 1 
ATOM   2730 H  HD22 B LEU   A 1 127 ? 22.781 -4.482  -0.157  0.28 13.50 ?  127 LEU   A HD22 1 
ATOM   2731 H  HD23 A LEU   A 1 127 ? 21.742 -5.022  0.824   0.72 15.89 ?  127 LEU   A HD23 1 
ATOM   2732 H  HD23 B LEU   A 1 127 ? 21.600 -4.362  0.899   0.28 13.50 ?  127 LEU   A HD23 1 
ATOM   2733 N  N    A SER   A 1 128 ? 19.714 -4.441  -3.245  0.72 10.87 ?  128 SER   A N    1 
ATOM   2734 N  N    B SER   A 1 128 ? 19.727 -4.318  -3.196  0.28 10.77 ?  128 SER   A N    1 
ATOM   2735 C  CA   A SER   A 1 128 ? 19.299 -4.067  -4.589  0.72 11.28 ?  128 SER   A CA   1 
ATOM   2736 C  CA   B SER   A 1 128 ? 19.395 -4.040  -4.591  0.28 10.78 ?  128 SER   A CA   1 
ATOM   2737 C  C    A SER   A 1 128 ? 17.840 -3.624  -4.670  0.72 11.60 ?  128 SER   A C    1 
ATOM   2738 C  C    B SER   A 1 128 ? 17.958 -3.582  -4.815  0.28 10.76 ?  128 SER   A C    1 
ATOM   2739 O  O    A SER   A 1 128 ? 17.379 -3.299  -5.765  0.72 13.08 ?  128 SER   A O    1 
ATOM   2740 O  O    B SER   A 1 128 ? 17.604 -3.271  -5.956  0.28 10.98 ?  128 SER   A O    1 
ATOM   2741 C  CB   A SER   A 1 128 ? 19.624 -5.127  -5.651  0.72 11.76 ?  128 SER   A CB   1 
ATOM   2742 C  CB   B SER   A 1 128 ? 19.736 -5.192  -5.547  0.28 10.69 ?  128 SER   A CB   1 
ATOM   2743 O  OG   A SER   A 1 128 ? 21.030 -5.348  -5.719  0.72 12.52 ?  128 SER   A OG   1 
ATOM   2744 O  OG   B SER   A 1 128 ? 21.143 -5.366  -5.639  0.28 10.95 ?  128 SER   A OG   1 
ATOM   2745 H  H    A SER   A 1 128 ? 20.298 -3.893  -2.923  0.72 13.09 ?  128 SER   A H    1 
ATOM   2746 H  H    B SER   A 1 128 ? 20.310 -3.758  -2.892  0.28 12.97 ?  128 SER   A H    1 
ATOM   2747 H  HA   A SER   A 1 128 ? 19.823 -3.290  -4.830  0.72 13.59 ?  128 SER   A HA   1 
ATOM   2748 H  HA   B SER   A 1 128 ? 19.949 -3.295  -4.861  0.28 12.99 ?  128 SER   A HA   1 
ATOM   2749 H  HB2  A SER   A 1 128 ? 19.178 -5.955  -5.423  0.72 14.16 ?  128 SER   A HB2  1 
ATOM   2750 H  HB2  B SER   A 1 128 ? 19.330 -6.006  -5.217  0.28 12.87 ?  128 SER   A HB2  1 
ATOM   2751 H  HB3  A SER   A 1 128 ? 19.311 -4.808  -6.517  0.72 14.16 ?  128 SER   A HB3  1 
ATOM   2752 H  HB3  B SER   A 1 128 ? 19.385 -4.977  -6.429  0.28 12.87 ?  128 SER   A HB3  1 
ATOM   2753 H  HG   A SER   A 1 128 ? 21.420 -4.628  -5.912  0.72 15.08 ?  128 SER   A HG   1 
ATOM   2754 H  HG   B SER   A 1 128 ? 21.495 -4.651  -5.911  0.28 13.19 ?  128 SER   A HG   1 
ATOM   2755 N  N    A ALA   A 1 129 ? 17.119 -3.570  -3.552  0.72 12.43 ?  129 ALA   A N    1 
ATOM   2756 N  N    B ALA   A 1 129 ? 17.131 -3.508  -3.776  0.28 11.34 ?  129 ALA   A N    1 
ATOM   2757 C  CA   A ALA   A 1 129 ? 15.747 -3.082  -3.534  0.72 12.58 ?  129 ALA   A CA   1 
ATOM   2758 C  CA   B ALA   A 1 129 ? 15.775 -3.006  -3.910  0.28 11.91 ?  129 ALA   A CA   1 
ATOM   2759 C  C    A ALA   A 1 129 ? 15.747 -1.554  -3.497  0.72 12.38 ?  129 ALA   A C    1 
ATOM   2760 C  C    B ALA   A 1 129 ? 15.768 -1.485  -3.763  0.28 12.17 ?  129 ALA   A C    1 
ATOM   2761 O  O    A ALA   A 1 129 ? 16.789 -0.897  -3.603  0.72 12.90 ?  129 ALA   A O    1 
ATOM   2762 O  O    B ALA   A 1 129 ? 16.811 -0.837  -3.633  0.28 11.97 ?  129 ALA   A O    1 
ATOM   2763 C  CB   A ALA   A 1 129 ? 14.975 -3.698  -2.368  0.72 13.62 ?  129 ALA   A CB   1 
ATOM   2764 C  CB   B ALA   A 1 129 ? 14.856 -3.681  -2.892  0.28 12.37 ?  129 ALA   A CB   1 
ATOM   2765 H  H    A ALA   A 1 129 ? 17.410 -3.815  -2.777  0.72 14.96 ?  129 ALA   A H    1 
ATOM   2766 H  H    B ALA   A 1 129 ? 17.336 -3.741  -2.972  0.28 13.66 ?  129 ALA   A H    1 
ATOM   2767 H  HA   A ALA   A 1 129 ? 15.317 -3.351  -4.353  0.72 15.14 ?  129 ALA   A HA   1 
ATOM   2768 H  HA   B ALA   A 1 129 ? 15.447 -3.218  -4.794  0.28 14.35 ?  129 ALA   A HA   1 
ATOM   2769 H  HB1  A ALA   A 1 129 ? 14.064 -3.361  -2.386  0.72 16.39 ?  129 ALA   A HB1  1 
ATOM   2770 H  HB1  B ALA   A 1 129 ? 13.955 -3.339  -3.005  0.28 14.89 ?  129 ALA   A HB1  1 
ATOM   2771 H  HB2  A ALA   A 1 129 ? 14.976 -4.659  -2.467  0.72 16.39 ?  129 ALA   A HB2  1 
ATOM   2772 H  HB2  B ALA   A 1 129 ? 14.869 -4.638  -3.045  0.28 14.89 ?  129 ALA   A HB2  1 
ATOM   2773 H  HB3  A ALA   A 1 129 ? 15.404 -3.446  -1.535  0.72 16.39 ?  129 ALA   A HB3  1 
ATOM   2774 H  HB3  B ALA   A 1 129 ? 15.175 -3.484  -1.997  0.28 14.89 ?  129 ALA   A HB3  1 
ATOM   2775 N  N    A GLY   A 1 130 ? 14.560 -0.972  -3.364  0.72 12.48 ?  130 GLY   A N    1 
ATOM   2776 N  N    B GLY   A 1 130 ? 14.574 -0.904  -3.796  0.28 12.60 ?  130 GLY   A N    1 
ATOM   2777 C  CA   A GLY   A 1 130 ? 14.447 0.472   -3.318  0.72 13.38 ?  130 GLY   A CA   1 
ATOM   2778 C  CA   B GLY   A 1 130 ? 14.463 0.540   -3.676  0.28 13.46 ?  130 GLY   A CA   1 
ATOM   2779 C  C    A GLY   A 1 130 ? 15.039 1.105   -4.556  0.72 12.69 ?  130 GLY   A C    1 
ATOM   2780 C  C    B GLY   A 1 130 ? 15.160 1.222   -4.835  0.28 13.47 ?  130 GLY   A C    1 
ATOM   2781 O  O    A GLY   A 1 130 ? 14.805 0.657   -5.684  0.72 12.14 ?  130 GLY   A O    1 
ATOM   2782 O  O    B GLY   A 1 130 ? 14.978 0.857   -6.002  0.28 13.92 ?  130 GLY   A O    1 
ATOM   2783 H  H    A GLY   A 1 130 ? 13.814 -1.392  -3.308  0.72 15.02 ?  130 GLY   A H    1 
ATOM   2784 H  H    B GLY   A 1 130 ? 13.828 -1.317  -3.896  0.28 15.17 ?  130 GLY   A H    1 
ATOM   2785 H  HA2  A GLY   A 1 130 ? 13.506 0.722   -3.263  0.72 16.10 ?  130 GLY   A HA2  1 
ATOM   2786 H  HA2  B GLY   A 1 130 ? 13.521 0.797   -3.653  0.28 16.20 ?  130 GLY   A HA2  1 
ATOM   2787 H  HA3  A GLY   A 1 130 ? 14.907 0.816   -2.548  0.72 16.10 ?  130 GLY   A HA3  1 
ATOM   2788 H  HA3  B GLY   A 1 130 ? 14.883 0.844   -2.858  0.28 16.20 ?  130 GLY   A HA3  1 
ATOM   2789 N  N    A ILE   A 1 131 ? 15.817 2.175   -4.345  0.72 13.21 ?  131 ILE   A N    1 
ATOM   2790 N  N    B ILE   A 1 131 ? 15.997 2.213   -4.511  0.28 13.08 ?  131 ILE   A N    1 
ATOM   2791 C  CA   A ILE   A 1 131 ? 16.371 2.953   -5.451  0.72 13.07 ?  131 ILE   A CA   1 
ATOM   2792 C  CA   B ILE   A 1 131 ? 16.625 3.027   -5.547  0.28 12.79 ?  131 ILE   A CA   1 
ATOM   2793 C  C    A ILE   A 1 131 ? 17.420 2.205   -6.261  0.72 12.58 ?  131 ILE   A C    1 
ATOM   2794 C  C    B ILE   A 1 131 ? 17.573 2.223   -6.426  0.28 12.76 ?  131 ILE   A C    1 
ATOM   2795 O  O    A ILE   A 1 131 ? 17.856 2.726   -7.295  0.72 13.53 ?  131 ILE   A O    1 
ATOM   2796 O  O    B ILE   A 1 131 ? 17.945 2.688   -7.510  0.28 13.35 ?  131 ILE   A O    1 
ATOM   2797 C  CB   A ILE   A 1 131 ? 16.890 4.337   -4.996  0.72 14.09 ?  131 ILE   A CB   1 
ATOM   2798 C  CB   B ILE   A 1 131 ? 17.317 4.280   -4.959  0.28 13.16 ?  131 ILE   A CB   1 
ATOM   2799 C  CG1  A ILE   A 1 131 ? 18.117 4.203   -4.084  0.72 15.19 ?  131 ILE   A CG1  1 
ATOM   2800 C  CG1  B ILE   A 1 131 ? 18.517 3.900   -4.087  0.28 13.75 ?  131 ILE   A CG1  1 
ATOM   2801 C  CG2  A ILE   A 1 131 ? 15.772 5.126   -4.315  0.72 14.60 ?  131 ILE   A CG2  1 
ATOM   2802 C  CG2  B ILE   A 1 131 ? 16.326 5.114   -4.162  0.28 13.15 ?  131 ILE   A CG2  1 
ATOM   2803 C  CD1  A ILE   A 1 131 ? 18.774 5.539   -3.731  0.72 16.15 ?  131 ILE   A CD1  1 
ATOM   2804 C  CD1  B ILE   A 1 131 ? 19.210 5.104   -3.446  0.28 14.18 ?  131 ILE   A CD1  1 
ATOM   2805 H  H    A ILE   A 1 131 ? 16.018 2.478   -3.566  0.72 15.89 ?  131 ILE   A H    1 
ATOM   2806 H  H    B ILE   A 1 131 ? 16.210 2.427   -3.704  0.28 15.74 ?  131 ILE   A H    1 
ATOM   2807 H  HA   A ILE   A 1 131 ? 15.651 3.132   -6.064  0.72 15.73 ?  131 ILE   A HA   1 
ATOM   2808 H  HA   B ILE   A 1 131 ? 15.924 3.351   -6.127  0.28 15.40 ?  131 ILE   A HA   1 
ATOM   2809 H  HB   A ILE   A 1 131 ? 17.161 4.828   -5.784  0.72 16.96 ?  131 ILE   A HB   1 
ATOM   2810 H  HB   B ILE   A 1 131 ? 17.635 4.820   -5.698  0.28 15.84 ?  131 ILE   A HB   1 
ATOM   2811 H  HG12 A ILE   A 1 131 ? 17.851 3.777   -3.255  0.72 18.28 ?  131 ILE   A HG12 1 
ATOM   2812 H  HG12 B ILE   A 1 131 ? 18.217 3.318   -3.374  0.28 16.55 ?  131 ILE   A HG12 1 
ATOM   2813 H  HG13 A ILE   A 1 131 ? 18.788 3.660   -4.531  0.72 18.28 ?  131 ILE   A HG13 1 
ATOM   2814 H  HG13 B ILE   A 1 131 ? 19.174 3.445   -4.635  0.28 16.55 ?  131 ILE   A HG13 1 
ATOM   2815 H  HG21 A ILE   A 1 131 ? 16.082 6.024   -4.130  0.72 17.57 ?  131 ILE   A HG21 1 
ATOM   2816 H  HG21 B ILE   A 1 131 ? 16.708 5.991   -4.000  0.28 15.83 ?  131 ILE   A HG21 1 
ATOM   2817 H  HG22 A ILE   A 1 131 ? 15.006 5.156   -4.910  0.72 17.57 ?  131 ILE   A HG22 1 
ATOM   2818 H  HG22 B ILE   A 1 131 ? 15.507 5.200   -4.672  0.28 15.83 ?  131 ILE   A HG22 1 
ATOM   2819 H  HG23 A ILE   A 1 131 ? 15.528 4.680   -3.487  0.72 17.57 ?  131 ILE   A HG23 1 
ATOM   2820 H  HG23 B ILE   A 1 131 ? 16.146 4.669   -3.320  0.28 15.83 ?  131 ILE   A HG23 1 
ATOM   2821 H  HD11 A ILE   A 1 131 ? 19.596 5.370   -3.241  0.72 19.43 ?  131 ILE   A HD11 1 
ATOM   2822 H  HD11 B ILE   A 1 131 ? 20.050 4.816   -3.054  0.28 17.07 ?  131 ILE   A HD11 1 
ATOM   2823 H  HD12 A ILE   A 1 131 ? 18.973 6.022   -4.549  0.72 19.43 ?  131 ILE   A HD12 1 
ATOM   2824 H  HD12 B ILE   A 1 131 ? 19.379 5.775   -4.128  0.28 17.07 ?  131 ILE   A HD12 1 
ATOM   2825 H  HD13 A ILE   A 1 131 ? 18.165 6.058   -3.182  0.72 19.43 ?  131 ILE   A HD13 1 
ATOM   2826 H  HD13 B ILE   A 1 131 ? 18.635 5.475   -2.757  0.28 17.07 ?  131 ILE   A HD13 1 
ATOM   2827 N  N    A PHE   A 1 132 ? 17.834 1.000   -5.836  0.72 12.47 ?  132 PHE   A N    1 
ATOM   2828 N  N    B PHE   A 1 132 ? 17.973 1.021   -5.996  0.28 12.79 ?  132 PHE   A N    1 
ATOM   2829 C  CA   A PHE   A 1 132 ? 18.698 0.165   -6.668  0.72 12.34 ?  132 PHE   A CA   1 
ATOM   2830 C  CA   B PHE   A 1 132 ? 18.894 0.222   -6.796  0.28 13.12 ?  132 PHE   A CA   1 
ATOM   2831 C  C    A PHE   A 1 132 ? 17.928 -0.597  -7.749  0.72 12.75 ?  132 PHE   A C    1 
ATOM   2832 C  C    B PHE   A 1 132 ? 18.214 -0.495  -7.961  0.28 13.78 ?  132 PHE   A C    1 
ATOM   2833 O  O    A PHE   A 1 132 ? 18.554 -1.242  -8.597  0.72 13.30 ?  132 PHE   A O    1 
ATOM   2834 O  O    B PHE   A 1 132 ? 18.913 -0.977  -8.860  0.28 14.28 ?  132 PHE   A O    1 
ATOM   2835 C  CB   A PHE   A 1 132 ? 19.514 -0.812  -5.812  0.72 11.98 ?  132 PHE   A CB   1 
ATOM   2836 C  CB   B PHE   A 1 132 ? 19.661 -0.768  -5.913  0.28 12.28 ?  132 PHE   A CB   1 
ATOM   2837 C  CG   A PHE   A 1 132 ? 20.747 -0.211  -5.165  0.72 12.29 ?  132 PHE   A CG   1 
ATOM   2838 C  CG   B PHE   A 1 132 ? 20.847 -0.162  -5.201  0.28 12.05 ?  132 PHE   A CG   1 
ATOM   2839 C  CD1  A PHE   A 1 132 ? 20.651 0.846   -4.280  0.72 13.47 ?  132 PHE   A CD1  1 
ATOM   2840 C  CD1  B PHE   A 1 132 ? 20.672 0.777   -4.197  0.28 12.54 ?  132 PHE   A CD1  1 
ATOM   2841 C  CD2  A PHE   A 1 132 ? 22.000 -0.756  -5.409  0.72 12.58 ?  132 PHE   A CD2  1 
ATOM   2842 C  CD2  B PHE   A 1 132 ? 22.136 -0.548  -5.529  0.28 12.03 ?  132 PHE   A CD2  1 
ATOM   2843 C  CE1  A PHE   A 1 132 ? 21.790 1.370   -3.675  0.72 13.81 ?  132 PHE   A CE1  1 
ATOM   2844 C  CE1  B PHE   A 1 132 ? 21.766 1.325   -3.541  0.28 12.60 ?  132 PHE   A CE1  1 
ATOM   2845 C  CE2  A PHE   A 1 132 ? 23.136 -0.243  -4.805  0.72 13.00 ?  132 PHE   A CE2  1 
ATOM   2846 C  CE2  B PHE   A 1 132 ? 23.231 -0.005  -4.878  0.28 12.42 ?  132 PHE   A CE2  1 
ATOM   2847 C  CZ   A PHE   A 1 132 ? 23.029 0.821   -3.936  0.72 13.32 ?  132 PHE   A CZ   1 
ATOM   2848 C  CZ   B PHE   A 1 132 ? 23.044 0.932   -3.882  0.28 12.51 ?  132 PHE   A CZ   1 
ATOM   2849 H  H    A PHE   A 1 132 ? 17.628 0.646   -5.074  0.72 15.01 ?  132 PHE   A H    1 
ATOM   2850 H  H    B PHE   A 1 132 ? 17.727 0.651   -5.252  0.28 15.40 ?  132 PHE   A H    1 
ATOM   2851 H  HA   A PHE   A 1 132 ? 19.332 0.747   -7.112  0.72 14.85 ?  132 PHE   A HA   1 
ATOM   2852 H  HA   B PHE   A 1 132 ? 19.552 0.827   -7.167  0.28 15.80 ?  132 PHE   A HA   1 
ATOM   2853 H  HB2  A PHE   A 1 132 ? 18.950 -1.153  -5.101  0.72 14.43 ?  132 PHE   A HB2  1 
ATOM   2854 H  HB2  B PHE   A 1 132 ? 19.061 -1.117  -5.238  0.28 14.78 ?  132 PHE   A HB2  1 
ATOM   2855 H  HB3  A PHE   A 1 132 ? 19.807 -1.549  -6.376  0.72 14.43 ?  132 PHE   A HB3  1 
ATOM   2856 H  HB3  B PHE   A 1 132 ? 19.989 -1.492  -6.470  0.28 14.78 ?  132 PHE   A HB3  1 
ATOM   2857 H  HD1  A PHE   A 1 132 ? 19.822 1.218   -4.095  0.72 16.22 ?  132 PHE   A HD1  1 
ATOM   2858 H  HD1  B PHE   A 1 132 ? 19.815 1.048   -3.961  0.28 15.09 ?  132 PHE   A HD1  1 
ATOM   2859 H  HD2  A PHE   A 1 132 ? 22.085 -1.477  -5.995  0.72 15.15 ?  132 PHE   A HD2  1 
ATOM   2860 H  HD2  B PHE   A 1 132 ? 22.270 -1.180  -6.199  0.28 14.49 ?  132 PHE   A HD2  1 
ATOM   2861 H  HE1  A PHE   A 1 132 ? 21.716 2.089   -3.087  0.72 16.62 ?  132 PHE   A HE1  1 
ATOM   2862 H  HE1  B PHE   A 1 132 ? 21.640 1.959   -2.871  0.28 15.16 ?  132 PHE   A HE1  1 
ATOM   2863 H  HE2  A PHE   A 1 132 ? 23.972 -0.611  -4.991  0.72 15.65 ?  132 PHE   A HE2  1 
ATOM   2864 H  HE2  B PHE   A 1 132 ? 24.092 -0.272  -5.112  0.28 14.95 ?  132 PHE   A HE2  1 
ATOM   2865 H  HZ   A PHE   A 1 132 ? 23.792 1.177   -3.535  0.72 16.03 ?  132 PHE   A HZ   1 
ATOM   2866 H  HZ   B PHE   A 1 132 ? 23.780 1.301   -3.446  0.28 15.06 ?  132 PHE   A HZ   1 
ATOM   2867 N  N    A GLY   A 1 133 ? 16.596 -0.560  -7.733  0.72 12.88 ?  133 GLY   A N    1 
ATOM   2868 N  N    B GLY   A 1 133 ? 16.884 -0.593  -7.968  0.28 13.70 ?  133 GLY   A N    1 
ATOM   2869 C  CA   A GLY   A 1 133 ? 15.803 -0.924  -8.890  0.72 13.52 ?  133 GLY   A CA   1 
ATOM   2870 C  CA   B GLY   A 1 133 ? 16.131 -0.960  -9.152  0.28 13.82 ?  133 GLY   A CA   1 
ATOM   2871 C  C    A GLY   A 1 133 ? 15.519 -2.398  -9.119  0.72 14.06 ?  133 GLY   A C    1 
ATOM   2872 C  C    B GLY   A 1 133 ? 15.503 -2.340  -9.133  0.28 14.01 ?  133 GLY   A C    1 
ATOM   2873 O  O    A GLY   A 1 133 ? 14.929 -2.727  -10.156 0.72 14.85 ?  133 GLY   A O    1 
ATOM   2874 O  O    B GLY   A 1 133 ? 14.535 -2.568  -9.872  0.28 14.24 ?  133 GLY   A O    1 
ATOM   2875 H  H    A GLY   A 1 133 ? 16.129 -0.325  -7.052  0.72 15.50 ?  133 GLY   A H    1 
ATOM   2876 H  H    B GLY   A 1 133 ? 16.395 -0.456  -7.275  0.28 16.49 ?  133 GLY   A H    1 
ATOM   2877 H  HA2  A GLY   A 1 133 ? 14.946 -0.476  -8.827  0.72 16.27 ?  133 GLY   A HA2  1 
ATOM   2878 H  HA2  B GLY   A 1 133 ? 15.419 -0.317  -9.283  0.28 16.63 ?  133 GLY   A HA2  1 
ATOM   2879 H  HA3  A GLY   A 1 133 ? 16.249 -0.597  -9.686  0.72 16.27 ?  133 GLY   A HA3  1 
ATOM   2880 H  HA3  B GLY   A 1 133 ? 16.716 -0.910  -9.923  0.28 16.63 ?  133 GLY   A HA3  1 
ATOM   2881 N  N    A ALA   A 1 134 ? 15.914 -3.297  -8.219  0.72 13.96 ?  134 ALA   A N    1 
ATOM   2882 N  N    B ALA   A 1 134 ? 16.014 -3.268  -8.327  0.28 14.01 ?  134 ALA   A N    1 
ATOM   2883 C  CA   A ALA   A 1 134 ? 15.600 -4.706  -8.408  0.72 14.79 ?  134 ALA   A CA   1 
ATOM   2884 C  CA   B ALA   A 1 134 ? 15.555 -4.647  -8.408  0.28 14.09 ?  134 ALA   A CA   1 
ATOM   2885 C  C    A ALA   A 1 134 ? 14.247 -5.042  -7.782  0.72 14.86 ?  134 ALA   A C    1 
ATOM   2886 C  C    B ALA   A 1 134 ? 14.237 -4.844  -7.659  0.28 13.90 ?  134 ALA   A C    1 
ATOM   2887 O  O    A ALA   A 1 134 ? 13.678 -4.273  -7.005  0.72 15.78 ?  134 ALA   A O    1 
ATOM   2888 O  O    B ALA   A 1 134 ? 13.833 -4.034  -6.819  0.28 14.28 ?  134 ALA   A O    1 
ATOM   2889 C  CB   A ALA   A 1 134 ? 16.701 -5.595  -7.829  0.72 15.48 ?  134 ALA   A CB   1 
ATOM   2890 C  CB   B ALA   A 1 134 ? 16.611 -5.599  -7.850  0.28 14.32 ?  134 ALA   A CB   1 
ATOM   2891 H  H    A ALA   A 1 134 ? 16.368 -3.116  -7.508  0.72 16.80 ?  134 ALA   A H    1 
ATOM   2892 H  H    B ALA   A 1 134 ? 16.625 -3.121  -7.739  0.28 16.86 ?  134 ALA   A H    1 
ATOM   2893 H  HA   A ALA   A 1 134 ? 15.545 -4.887  -9.360  0.72 17.80 ?  134 ALA   A HA   1 
ATOM   2894 H  HA   B ALA   A 1 134 ? 15.410 -4.871  -9.340  0.28 16.95 ?  134 ALA   A HA   1 
ATOM   2895 H  HB1  A ALA   A 1 134 ? 16.468 -6.523  -7.989  0.72 18.62 ?  134 ALA   A HB1  1 
ATOM   2896 H  HB1  B ALA   A 1 134 ? 16.285 -6.508  -7.933  0.28 17.24 ?  134 ALA   A HB1  1 
ATOM   2897 H  HB2  A ALA   A 1 134 ? 17.540 -5.384  -8.271  0.72 18.62 ?  134 ALA   A HB2  1 
ATOM   2898 H  HB2  B ALA   A 1 134 ? 17.430 -5.492  -8.358  0.28 17.24 ?  134 ALA   A HB2  1 
ATOM   2899 H  HB3  A ALA   A 1 134 ? 16.775 -5.427  -6.879  0.72 18.62 ?  134 ALA   A HB3  1 
ATOM   2900 H  HB3  B ALA   A 1 134 ? 16.768 -5.385  -6.918  0.28 17.24 ?  134 ALA   A HB3  1 
ATOM   2901 N  N    A ASP   A 1 135 ? 13.732 -6.213  -8.143  0.72 15.22 ?  135 ASP   A N    1 
ATOM   2902 N  N    B ASP   A 1 135 ? 13.571 -5.952  -7.979  0.28 14.23 ?  135 ASP   A N    1 
ATOM   2903 C  CA   A ASP   A 1 135 ? 12.472 -6.703  -7.588  0.72 16.24 ?  135 ASP   A CA   1 
ATOM   2904 C  CA   B ASP   A 1 135 ? 12.314 -6.322  -7.338  0.28 14.60 ?  135 ASP   A CA   1 
ATOM   2905 C  C    A ASP   A 1 135 ? 12.698 -7.131  -6.143  0.72 15.63 ?  135 ASP   A C    1 
ATOM   2906 C  C    B ASP   A 1 135 ? 12.600 -6.816  -5.926  0.28 14.23 ?  135 ASP   A C    1 
ATOM   2907 O  O    A ASP   A 1 135 ? 13.502 -8.039  -5.900  0.72 15.69 ?  135 ASP   A O    1 
ATOM   2908 O  O    B ASP   A 1 135 ? 13.304 -7.822  -5.763  0.28 14.14 ?  135 ASP   A O    1 
ATOM   2909 C  CB   A ASP   A 1 135 ? 12.010 -7.895  -8.422  0.72 18.47 ?  135 ASP   A CB   1 
ATOM   2910 C  CB   B ASP   A 1 135 ? 11.651 -7.435  -8.146  0.28 15.33 ?  135 ASP   A CB   1 
ATOM   2911 C  CG   A ASP   A 1 135 ? 10.715 -8.521  -7.915  0.72 20.35 ?  135 ASP   A CG   1 
ATOM   2912 C  CG   B ASP   A 1 135 ? 10.236 -7.751  -7.675  0.28 16.17 ?  135 ASP   A CG   1 
ATOM   2913 O  OD1  A ASP   A 1 135 ? 10.164 -8.075  -6.888  0.72 20.36 ?  135 ASP   A OD1  1 
ATOM   2914 O  OD1  B ASP   A 1 135 ? 9.887  -7.407  -6.524  0.28 16.09 ?  135 ASP   A OD1  1 
ATOM   2915 O  OD2  A ASP   A 1 135 ? 10.240 -9.473  -8.568  0.72 22.84 -1 135 ASP   A OD2  1 
ATOM   2916 O  OD2  B ASP   A 1 135 ? 9.478  -8.362  -8.458  0.28 17.00 -1 135 ASP   A OD2  1 
ATOM   2917 H  H    A ASP   A 1 135 ? 14.092 -6.747  -8.713  0.72 18.31 ?  135 ASP   A H    1 
ATOM   2918 H  H    B ASP   A 1 135 ? 13.830 -6.513  -8.572  0.28 17.12 ?  135 ASP   A H    1 
ATOM   2919 H  HA   A ASP   A 1 135 ? 11.799 -6.006  -7.633  0.72 19.53 ?  135 ASP   A HA   1 
ATOM   2920 H  HA   B ASP   A 1 135 ? 11.715 -5.557  -7.317  0.28 17.56 ?  135 ASP   A HA   1 
ATOM   2921 H  HB2  A ASP   A 1 135 ? 11.844 -7.604  -9.330  0.72 22.21 ?  135 ASP   A HB2  1 
ATOM   2922 H  HB2  B ASP   A 1 135 ? 11.626 -7.169  -9.080  0.28 18.44 ?  135 ASP   A HB2  1 
ATOM   2923 H  HB3  A ASP   A 1 135 ? 12.701 -8.575  -8.412  0.72 22.21 ?  135 ASP   A HB3  1 
ATOM   2924 H  HB3  B ASP   A 1 135 ? 12.171 -8.246  -8.047  0.28 18.44 ?  135 ASP   A HB3  1 
ATOM   2925 N  N    A PRO   A 1 136 ? 12.035 -6.515  -5.161  0.72 15.03 ?  136 PRO   A N    1 
ATOM   2926 N  N    B PRO   A 1 136 ? 12.089 -6.155  -4.886  0.28 14.02 ?  136 PRO   A N    1 
ATOM   2927 C  CA   A PRO   A 1 136 ? 12.276 -6.910  -3.761  0.72 15.03 ?  136 PRO   A CA   1 
ATOM   2928 C  CA   B PRO   A 1 136 ? 12.372 -6.609  -3.514  0.28 14.03 ?  136 PRO   A CA   1 
ATOM   2929 C  C    A PRO   A 1 136 ? 11.862 -8.336  -3.440  0.72 14.03 ?  136 PRO   A C    1 
ATOM   2930 C  C    B PRO   A 1 136 ? 11.883 -8.017  -3.210  0.28 13.33 ?  136 PRO   A C    1 
ATOM   2931 O  O    A PRO   A 1 136 ? 12.469 -8.964  -2.564  0.72 14.01 ?  136 PRO   A O    1 
ATOM   2932 O  O    B PRO   A 1 136 ? 12.433 -8.665  -2.310  0.28 12.63 ?  136 PRO   A O    1 
ATOM   2933 C  CB   A PRO   A 1 136 ? 11.467 -5.881  -2.958  0.72 15.72 ?  136 PRO   A CB   1 
ATOM   2934 C  CB   B PRO   A 1 136 ? 11.688 -5.547  -2.638  0.28 14.70 ?  136 PRO   A CB   1 
ATOM   2935 C  CG   A PRO   A 1 136 ? 10.432 -5.379  -3.911  0.72 16.31 ?  136 PRO   A CG   1 
ATOM   2936 C  CG   B PRO   A 1 136 ? 10.738 -4.847  -3.555  0.28 15.05 ?  136 PRO   A CG   1 
ATOM   2937 C  CD   A PRO   A 1 136 ? 11.058 -5.418  -5.269  0.72 15.86 ?  136 PRO   A CD   1 
ATOM   2938 C  CD   B PRO   A 1 136 ? 11.314 -4.906  -4.911  0.28 14.34 ?  136 PRO   A CD   1 
ATOM   2939 H  HA   A PRO   A 1 136 ? 13.221 -6.805  -3.545  0.72 18.09 ?  136 PRO   A HA   1 
ATOM   2940 H  HA   B PRO   A 1 136 ? 13.323 -6.577  -3.346  0.28 16.88 ?  136 PRO   A HA   1 
ATOM   2941 H  HB2  A PRO   A 1 136 ? 11.055 -6.320  -2.196  0.72 18.91 ?  136 PRO   A HB2  1 
ATOM   2942 H  HB2  B PRO   A 1 136 ? 11.209 -5.970  -1.909  0.28 17.69 ?  136 PRO   A HB2  1 
ATOM   2943 H  HB3  A PRO   A 1 136 ? 12.053 -5.165  -2.667  0.72 18.91 ?  136 PRO   A HB3  1 
ATOM   2944 H  HB3  B PRO   A 1 136 ? 12.352 -4.924  -2.295  0.28 17.69 ?  136 PRO   A HB3  1 
ATOM   2945 H  HG2  A PRO   A 1 136 ? 9.658  -5.958  -3.878  0.72 19.62 ?  136 PRO   A HG2  1 
ATOM   2946 H  HG2  B PRO   A 1 136 ? 9.898  -5.321  -3.562  0.28 18.11 ?  136 PRO   A HG2  1 
ATOM   2947 H  HG3  A PRO   A 1 136 ? 10.196 -4.471  -3.676  0.72 19.62 ?  136 PRO   A HG3  1 
ATOM   2948 H  HG3  B PRO   A 1 136 ? 10.616 -3.926  -3.268  0.28 18.11 ?  136 PRO   A HG3  1 
ATOM   2949 H  HD2  A PRO   A 1 136 ? 10.391 -5.636  -5.942  0.72 19.08 ?  136 PRO   A HD2  1 
ATOM   2950 H  HD2  B PRO   A 1 136 ? 10.601 -4.957  -5.571  0.28 17.26 ?  136 PRO   A HD2  1 
ATOM   2951 H  HD3  A PRO   A 1 136 ? 11.504 -4.582  -5.468  0.72 19.08 ?  136 PRO   A HD3  1 
ATOM   2952 H  HD3  B PRO   A 1 136 ? 11.896 -4.149  -5.073  0.28 17.26 ?  136 PRO   A HD3  1 
ATOM   2953 N  N    A ILE   A 1 137 ? 10.826 -8.859  -4.100  0.72 14.31 ?  137 ILE   A N    1 
ATOM   2954 N  N    B ILE   A 1 137 ? 10.872 -8.514  -3.927  0.28 13.67 ?  137 ILE   A N    1 
ATOM   2955 C  CA   A ILE   A 1 137 ? 10.462 -10.261 -3.905  0.72 14.63 ?  137 ILE   A CA   1 
ATOM   2956 C  CA   B ILE   A 1 137 ? 10.438 -9.897  -3.738  0.28 14.08 ?  137 ILE   A CA   1 
ATOM   2957 C  C    A ILE   A 1 137 ? 11.625 -11.159 -4.295  0.72 14.21 ?  137 ILE   A C    1 
ATOM   2958 C  C    B ILE   A 1 137 ? 11.550 -10.859 -4.139  0.28 13.92 ?  137 ILE   A C    1 
ATOM   2959 O  O    A ILE   A 1 137 ? 11.952 -12.127 -3.596  0.72 14.45 ?  137 ILE   A O    1 
ATOM   2960 O  O    B ILE   A 1 137 ? 11.829 -11.842 -3.441  0.28 13.86 ?  137 ILE   A O    1 
ATOM   2961 C  CB   A ILE   A 1 137 ? 9.181  -10.599 -4.692  0.72 15.89 ?  137 ILE   A CB   1 
ATOM   2962 C  CB   B ILE   A 1 137 ? 9.139  -10.160 -4.523  0.28 14.63 ?  137 ILE   A CB   1 
ATOM   2963 C  CG1  A ILE   A 1 137 ? 7.995  -9.768  -4.187  0.72 17.72 ?  137 ILE   A CG1  1 
ATOM   2964 C  CG1  B ILE   A 1 137 ? 8.042  -9.177  -4.095  0.28 15.36 ?  137 ILE   A CG1  1 
ATOM   2965 C  CG2  A ILE   A 1 137 ? 8.875  -12.093 -4.592  0.72 16.35 ?  137 ILE   A CG2  1 
ATOM   2966 C  CG2  B ILE   A 1 137 ? 8.683  -11.606 -4.339  0.28 14.83 ?  137 ILE   A CG2  1 
ATOM   2967 C  CD1  A ILE   A 1 137 ? 6.721  -9.963  -4.985  0.72 18.98 ?  137 ILE   A CD1  1 
ATOM   2968 C  CD1  B ILE   A 1 137 ? 6.795  -9.246  -4.940  0.28 15.69 ?  137 ILE   A CD1  1 
ATOM   2969 H  H    A ILE   A 1 137 ? 10.331 -8.436  -4.657  0.72 17.22 ?  137 ILE   A H    1 
ATOM   2970 H  H    B ILE   A 1 137 ? 10.424 -8.073  -4.518  0.28 16.45 ?  137 ILE   A H    1 
ATOM   2971 H  HA   A ILE   A 1 137 ? 10.287 -10.415 -2.968  0.72 17.61 ?  137 ILE   A HA   1 
ATOM   2972 H  HA   B ILE   A 1 137 ? 10.243 -10.036 -2.798  0.28 16.94 ?  137 ILE   A HA   1 
ATOM   2973 H  HB   A ILE   A 1 137 ? 9.326  -10.386 -5.624  0.72 19.12 ?  137 ILE   A HB   1 
ATOM   2974 H  HB   B ILE   A 1 137 ? 9.316  -10.016 -5.463  0.28 17.61 ?  137 ILE   A HB   1 
ATOM   2975 H  HG12 A ILE   A 1 137 ? 7.814  -10.011 -3.266  0.72 21.32 ?  137 ILE   A HG12 1 
ATOM   2976 H  HG12 B ILE   A 1 137 ? 7.787  -9.368  -3.180  0.28 18.48 ?  137 ILE   A HG12 1 
ATOM   2977 H  HG13 A ILE   A 1 137 ? 8.236  -8.828  -4.236  0.72 21.32 ?  137 ILE   A HG13 1 
ATOM   2978 H  HG13 B ILE   A 1 137 ? 8.382  -8.271  -4.159  0.28 18.48 ?  137 ILE   A HG13 1 
ATOM   2979 H  HG21 A ILE   A 1 137 ? 7.984  -12.273 -4.936  0.72 19.67 ?  137 ILE   A HG21 1 
ATOM   2980 H  HG21 B ILE   A 1 137 ? 7.818  -11.725 -4.762  0.28 17.84 ?  137 ILE   A HG21 1 
ATOM   2981 H  HG22 A ILE   A 1 137 ? 9.524  -12.587 -5.115  0.72 19.67 ?  137 ILE   A HG22 1 
ATOM   2982 H  HG22 B ILE   A 1 137 ? 9.331  -12.196 -4.751  0.28 17.84 ?  137 ILE   A HG22 1 
ATOM   2983 H  HG23 A ILE   A 1 137 ? 8.923  -12.365 -3.663  0.72 19.67 ?  137 ILE   A HG23 1 
ATOM   2984 H  HG23 B ILE   A 1 137 ? 8.615  -11.797 -3.391  0.28 17.84 ?  137 ILE   A HG23 1 
ATOM   2985 H  HD11 A ILE   A 1 137 ? 6.027  -10.290 -4.393  0.72 22.82 ?  137 ILE   A HD11 1 
ATOM   2986 H  HD11 B ILE   A 1 137 ? 6.264  -8.451  -4.782  0.28 18.88 ?  137 ILE   A HD11 1 
ATOM   2987 H  HD12 A ILE   A 1 137 ? 6.467  -9.111  -5.364  0.72 22.82 ?  137 ILE   A HD12 1 
ATOM   2988 H  HD12 B ILE   A 1 137 ? 7.050  -9.292  -5.875  0.28 18.88 ?  137 ILE   A HD12 1 
ATOM   2989 H  HD13 A ILE   A 1 137 ? 6.882  -10.601 -5.696  0.72 22.82 ?  137 ILE   A HD13 1 
ATOM   2990 H  HD13 B ILE   A 1 137 ? 6.291  -10.037 -4.695  0.28 18.88 ?  137 ILE   A HD13 1 
ATOM   2991 N  N    A HIS   A 1 138 ? 12.275 -10.841 -5.414  0.72 14.43 ?  138 HIS   A N    1 
ATOM   2992 N  N    B HIS   A 1 138 ? 12.205 -10.585 -5.270  0.28 13.88 ?  138 HIS   A N    1 
ATOM   2993 C  CA   A HIS   A 1 138 ? 13.469 -11.574 -5.808  0.72 14.56 ?  138 HIS   A CA   1 
ATOM   2994 C  CA   B HIS   A 1 138 ? 13.300 -11.433 -5.733  0.28 13.73 ?  138 HIS   A CA   1 
ATOM   2995 C  C    A HIS   A 1 138 ? 14.589 -11.399 -4.787  0.72 13.99 ?  138 HIS   A C    1 
ATOM   2996 C  C    B HIS   A 1 138 ? 14.487 -11.372 -4.777  0.28 13.59 ?  138 HIS   A C    1 
ATOM   2997 O  O    A HIS   A 1 138 ? 15.266 -12.373 -4.430  0.72 14.19 ?  138 HIS   A O    1 
ATOM   2998 O  O    B HIS   A 1 138 ? 15.112 -12.396 -4.476  0.28 13.88 ?  138 HIS   A O    1 
ATOM   2999 C  CB   A HIS   A 1 138 ? 13.908 -11.148 -7.208  0.72 15.62 ?  138 HIS   A CB   1 
ATOM   3000 C  CB   B HIS   A 1 138 ? 13.708 -10.998 -7.142  0.28 13.72 ?  138 HIS   A CB   1 
ATOM   3001 C  CG   A HIS   A 1 138 ? 15.160 -11.824 -7.671  0.72 16.75 ?  138 HIS   A CG   1 
ATOM   3002 C  CG   B HIS   A 1 138 ? 15.007 -11.579 -7.606  0.28 14.16 ?  138 HIS   A CG   1 
ATOM   3003 N  ND1  A HIS   A 1 138 ? 15.241 -13.186 -7.872  0.72 17.89 ?  138 HIS   A ND1  1 
ATOM   3004 N  ND1  B HIS   A 1 138 ? 15.150 -12.905 -7.955  0.28 14.80 ?  138 HIS   A ND1  1 
ATOM   3005 C  CD2  A HIS   A 1 138 ? 16.387 -11.327 -7.952  0.72 17.27 ?  138 HIS   A CD2  1 
ATOM   3006 C  CD2  B HIS   A 1 138 ? 16.224 -11.011 -7.781  0.28 14.24 ?  138 HIS   A CD2  1 
ATOM   3007 C  CE1  A HIS   A 1 138 ? 16.462 -13.496 -8.272  0.72 18.38 ?  138 HIS   A CE1  1 
ATOM   3008 C  CE1  B HIS   A 1 138 ? 16.399 -13.128 -8.324  0.28 14.76 ?  138 HIS   A CE1  1 
ATOM   3009 N  NE2  A HIS   A 1 138 ? 17.178 -12.387 -8.325  0.72 17.68 ?  138 HIS   A NE2  1 
ATOM   3010 N  NE2  B HIS   A 1 138 ? 17.072 -11.996 -8.228  0.28 14.47 ?  138 HIS   A NE2  1 
ATOM   3011 H  H    A HIS   A 1 138 ? 12.046 -10.213 -5.961  0.72 17.36 ?  138 HIS   A H    1 
ATOM   3012 H  H    B HIS   A 1 138 ? 12.032 -9.912  -5.780  0.28 16.71 ?  138 HIS   A H    1 
ATOM   3013 H  HA   A HIS   A 1 138 ? 13.255 -12.516 -5.849  0.72 17.52 ?  138 HIS   A HA   1 
ATOM   3014 H  HA   B HIS   A 1 138 ? 12.992 -12.348 -5.777  0.28 16.53 ?  138 HIS   A HA   1 
ATOM   3015 H  HB2  A HIS   A 1 138 ? 13.199 -11.368 -7.839  0.72 18.79 ?  138 HIS   A HB2  1 
ATOM   3016 H  HB2  B HIS   A 1 138 ? 13.017 -11.278 -7.767  0.28 16.51 ?  138 HIS   A HB2  1 
ATOM   3017 H  HB3  A HIS   A 1 138 ? 14.064 -10.192 -7.215  0.72 18.79 ?  138 HIS   A HB3  1 
ATOM   3018 H  HB3  B HIS   A 1 138 ? 13.790 -10.031 -7.163  0.28 16.51 ?  138 HIS   A HB3  1 
ATOM   3019 H  HD1  A HIS   A 1 138 ? 14.592 -13.744 -7.765  0.72 21.52 ?  138 HIS   A HD1  1 
ATOM   3020 H  HD1  B HIS   A 1 138 ? 14.522 -13.494 -7.935  0.28 17.80 ?  138 HIS   A HD1  1 
ATOM   3021 H  HD2  A HIS   A 1 138 ? 16.640 -10.435 -7.904  0.72 20.77 ?  138 HIS   A HD2  1 
ATOM   3022 H  HD2  B HIS   A 1 138 ? 16.443 -10.121 -7.628  0.28 17.14 ?  138 HIS   A HD2  1 
ATOM   3023 H  HE1  A HIS   A 1 138 ? 16.763 -14.350 -8.473  0.72 22.10 ?  138 HIS   A HE1  1 
ATOM   3024 H  HE1  B HIS   A 1 138 ? 16.744 -13.946 -8.603  0.28 17.76 ?  138 HIS   A HE1  1 
ATOM   3025 N  N    . SER   A 1 139 ? 14.805 -10.172 -4.298  1.00 13.45 ?  139 SER   A N    1 
ATOM   3026 C  CA   . SER   A 1 139 ? 15.878 -9.985  -3.331  1.00 12.98 ?  139 SER   A CA   1 
ATOM   3027 C  C    . SER   A 1 139 ? 15.659 -10.827 -2.078  1.00 12.66 ?  139 SER   A C    1 
ATOM   3028 O  O    . SER   A 1 139 ? 16.610 -11.409 -1.542  1.00 12.83 ?  139 SER   A O    1 
ATOM   3029 C  CB   . SER   A 1 139 ? 16.009 -8.507  -2.973  1.00 12.90 ?  139 SER   A CB   1 
ATOM   3030 O  OG   . SER   A 1 139 ? 17.094 -8.330  -2.084  1.00 13.37 ?  139 SER   A OG   1 
ATOM   3031 H  H    A SER   A 1 139 ? 14.358 -9.464  -4.497  0.72 16.19 ?  139 SER   A H    1 
ATOM   3032 H  H    B SER   A 1 139 ? 14.400 -9.444  -4.512  0.28 16.19 ?  139 SER   A H    1 
ATOM   3033 H  HA   . SER   A 1 139 ? 16.716 -10.265 -3.733  1.00 15.62 ?  139 SER   A HA   1 
ATOM   3034 H  HB2  . SER   A 1 139 ? 16.171 -7.991  -3.778  1.00 15.53 ?  139 SER   A HB2  1 
ATOM   3035 H  HB3  . SER   A 1 139 ? 15.192 -8.206  -2.541  1.00 15.53 ?  139 SER   A HB3  1 
ATOM   3036 H  HG   . SER   A 1 139 ? 17.177 -7.522  -1.875  1.00 16.09 ?  139 SER   A HG   1 
ATOM   3037 N  N    . LEU   A 1 140 ? 14.420 -10.887 -1.585  1.00 12.76 ?  140 LEU   A N    1 
ATOM   3038 C  CA   . LEU   A 1 140 ? 14.145 -11.701 -0.406  1.00 12.44 ?  140 LEU   A CA   1 
ATOM   3039 C  C    . LEU   A 1 140 ? 14.416 -13.180 -0.683  1.00 12.65 ?  140 LEU   A C    1 
ATOM   3040 O  O    . LEU   A 1 140 ? 14.970 -13.891 0.167   1.00 13.43 ?  140 LEU   A O    1 
ATOM   3041 C  CB   . LEU   A 1 140 ? 12.703 -11.477 0.048   1.00 13.24 ?  140 LEU   A CB   1 
ATOM   3042 C  CG   . LEU   A 1 140 ? 12.246 -12.323 1.236   1.00 13.96 ?  140 LEU   A CG   1 
ATOM   3043 C  CD1  . LEU   A 1 140 ? 13.155 -12.150 2.444   1.00 14.47 ?  140 LEU   A CD1  1 
ATOM   3044 C  CD2  . LEU   A 1 140 ? 10.793 -11.997 1.600   1.00 14.74 ?  140 LEU   A CD2  1 
ATOM   3045 H  H    . LEU   A 1 140 ? 13.741 -10.466 -1.903  1.00 15.35 ?  140 LEU   A H    1 
ATOM   3046 H  HA   . LEU   A 1 140 ? 14.728 -11.423 0.314   1.00 14.98 ?  140 LEU   A HA   1 
ATOM   3047 H  HB2  . LEU   A 1 140 ? 12.599 -10.551 0.300   1.00 15.93 ?  140 LEU   A HB2  1 
ATOM   3048 H  HB3  . LEU   A 1 140 ? 12.113 -11.684 -0.694  1.00 15.93 ?  140 LEU   A HB3  1 
ATOM   3049 H  HG   . LEU   A 1 140 ? 12.269 -13.261 0.981   1.00 16.80 ?  140 LEU   A HG   1 
ATOM   3050 H  HD11 . LEU   A 1 140 ? 12.770 -12.622 3.199   1.00 17.42 ?  140 LEU   A HD11 1 
ATOM   3051 H  HD12 . LEU   A 1 140 ? 14.027 -12.527 2.234   1.00 17.42 ?  140 LEU   A HD12 1 
ATOM   3052 H  HD13 . LEU   A 1 140 ? 13.238 -11.210 2.644   1.00 17.42 ?  140 LEU   A HD13 1 
ATOM   3053 H  HD21 . LEU   A 1 140 ? 10.511 -12.573 2.332   1.00 17.74 ?  140 LEU   A HD21 1 
ATOM   3054 H  HD22 . LEU   A 1 140 ? 10.735 -11.068 1.874   1.00 17.74 ?  140 LEU   A HD22 1 
ATOM   3055 H  HD23 . LEU   A 1 140 ? 10.227 -12.151 0.827   1.00 17.74 ?  140 LEU   A HD23 1 
ATOM   3056 N  N    . ARG   A 1 141 ? 14.033 -13.657 -1.869  1.00 13.26 ?  141 ARG   A N    1 
ATOM   3057 C  CA   . ARG   A 1 141 ? 14.273 -15.048 -2.232  1.00 14.27 ?  141 ARG   A CA   1 
ATOM   3058 C  C    . ARG   A 1 141 ? 15.768 -15.352 -2.246  1.00 13.40 ?  141 ARG   A C    1 
ATOM   3059 O  O    . ARG   A 1 141 ? 16.220 -16.361 -1.691  1.00 14.01 ?  141 ARG   A O    1 
ATOM   3060 C  CB   . ARG   A 1 141 ? 13.646 -15.313 -3.603  1.00 16.13 ?  141 ARG   A CB   1 
ATOM   3061 C  CG   . ARG   A 1 141 ? 13.647 -16.761 -4.045  1.00 19.27 ?  141 ARG   A CG   1 
ATOM   3062 C  CD   . ARG   A 1 141 ? 12.613 -17.532 -3.293  1.00 22.01 ?  141 ARG   A CD   1 
ATOM   3063 N  NE   . ARG   A 1 141 ? 13.221 -18.302 -2.222  1.00 22.81 ?  141 ARG   A NE   1 
ATOM   3064 C  CZ   . ARG   A 1 141 ? 12.534 -18.870 -1.239  1.00 23.59 ?  141 ARG   A CZ   1 
ATOM   3065 N  NH1  . ARG   A 1 141 ? 11.242 -18.633 -1.071  1.00 22.82 ?  141 ARG   A NH1  1 
ATOM   3066 N  NH2  . ARG   A 1 141 ? 13.159 -19.687 -0.397  1.00 24.56 ?  141 ARG   A NH2  1 
ATOM   3067 H  H    . ARG   A 1 141 ? 13.632 -13.194 -2.478  1.00 15.96 ?  141 ARG   A H    1 
ATOM   3068 H  HA   . ARG   A 1 141 ? 13.850 -15.628 -1.584  1.00 17.18 ?  141 ARG   A HA   1 
ATOM   3069 H  HB2  . ARG   A 1 141 ? 12.726 -15.006 -3.589  1.00 19.40 ?  141 ARG   A HB2  1 
ATOM   3070 H  HB3  . ARG   A 1 141 ? 14.141 -14.807 -4.268  1.00 19.40 ?  141 ARG   A HB3  1 
ATOM   3071 H  HG2  . ARG   A 1 141 ? 13.444 -16.812 -4.994  1.00 23.17 ?  141 ARG   A HG2  1 
ATOM   3072 H  HG3  . ARG   A 1 141 ? 14.518 -17.158 -3.869  1.00 23.17 ?  141 ARG   A HG3  1 
ATOM   3073 H  HD2  . ARG   A 1 141 ? 11.975 -16.920 -2.893  1.00 26.46 ?  141 ARG   A HD2  1 
ATOM   3074 H  HD3  . ARG   A 1 141 ? 12.154 -18.137 -3.902  1.00 26.46 ?  141 ARG   A HD3  1 
ATOM   3075 H  HE   . ARG   A 1 141 ? 14.046 -18.518 -2.304  1.00 27.42 ?  141 ARG   A HE   1 
ATOM   3076 H  HH11 . ARG   A 1 141 ? 10.817 -18.122 -1.617  1.00 27.43 ?  141 ARG   A HH11 1 
ATOM   3077 H  HH12 . ARG   A 1 141 ? 10.814 -19.009 -0.423  1.00 27.43 ?  141 ARG   A HH12 1 
ATOM   3078 H  HH21 . ARG   A 1 141 ? 13.997 -19.847 -0.496  1.00 29.51 ?  141 ARG   A HH21 1 
ATOM   3079 H  HH22 . ARG   A 1 141 ? 12.726 -20.049 0.254   1.00 29.51 ?  141 ARG   A HH22 1 
ATOM   3080 N  N    . VAL   A 1 142 ? 16.556 -14.487 -2.888  1.00 12.86 ?  142 VAL   A N    1 
ATOM   3081 C  CA   . VAL   A 1 142 ? 18.003 -14.693 -2.914  1.00 12.91 ?  142 VAL   A CA   1 
ATOM   3082 C  C    . VAL   A 1 142 ? 18.569 -14.670 -1.500  1.00 12.32 ?  142 VAL   A C    1 
ATOM   3083 O  O    . VAL   A 1 142 ? 19.435 -15.479 -1.152  1.00 13.12 ?  142 VAL   A O    1 
ATOM   3084 C  CB   . VAL   A 1 142 ? 18.696 -13.671 -3.833  1.00 13.41 ?  142 VAL   A CB   1 
ATOM   3085 C  CG1  . VAL   A 1 142 ? 20.210 -13.881 -3.797  1.00 13.10 ?  142 VAL   A CG1  1 
ATOM   3086 C  CG2  . VAL   A 1 142 ? 18.192 -13.800 -5.258  1.00 14.43 ?  142 VAL   A CG2  1 
ATOM   3087 H  H    . VAL   A 1 142 ? 16.287 -13.776 -3.307  1.00 15.48 ?  142 VAL   A H    1 
ATOM   3088 H  HA   . VAL   A 1 142 ? 18.179 -15.565 -3.283  1.00 15.54 ?  142 VAL   A HA   1 
ATOM   3089 H  HB   . VAL   A 1 142 ? 18.513 -12.766 -3.523  1.00 16.14 ?  142 VAL   A HB   1 
ATOM   3090 H  HG11 . VAL   A 1 142 ? 20.618 -13.386 -4.527  1.00 15.77 ?  142 VAL   A HG11 1 
ATOM   3091 H  HG12 . VAL   A 1 142 ? 20.559 -13.555 -2.950  1.00 15.77 ?  142 VAL   A HG12 1 
ATOM   3092 H  HG13 . VAL   A 1 142 ? 20.400 -14.825 -3.893  1.00 15.77 ?  142 VAL   A HG13 1 
ATOM   3093 H  HG21 . VAL   A 1 142 ? 18.667 -13.164 -5.818  1.00 17.36 ?  142 VAL   A HG21 1 
ATOM   3094 H  HG22 . VAL   A 1 142 ? 18.366 -14.703 -5.565  1.00 17.36 ?  142 VAL   A HG22 1 
ATOM   3095 H  HG23 . VAL   A 1 142 ? 17.246 -13.615 -5.271  1.00 17.36 ?  142 VAL   A HG23 1 
ATOM   3096 N  N    . CYS   A 1 143 ? 18.101 -13.742 -0.667  1.00 12.08 ?  143 CYS   A N    1 
ATOM   3097 C  CA   . CYS   A 1 143 ? 18.557 -13.693 0.717   1.00 12.42 ?  143 CYS   A CA   1 
ATOM   3098 C  C    . CYS   A 1 143 ? 18.331 -15.032 1.410   1.00 12.86 ?  143 CYS   A C    1 
ATOM   3099 O  O    . CYS   A 1 143 ? 19.251 -15.615 1.989   1.00 12.79 ?  143 CYS   A O    1 
ATOM   3100 C  CB   . CYS   A 1 143 ? 17.830 -12.572 1.457   1.00 12.91 ?  143 CYS   A CB   1 
ATOM   3101 S  SG   . CYS   A 1 143 ? 18.321 -12.396 3.181   1.00 13.44 ?  143 CYS   A SG   1 
ATOM   3102 H  H    . CYS   A 1 143 ? 17.525 -13.144 -0.877  1.00 14.54 ?  143 CYS   A H    1 
ATOM   3103 H  HA   . CYS   A 1 143 ? 19.506 -13.506 0.733   1.00 14.96 ?  143 CYS   A HA   1 
ATOM   3104 H  HB2  . CYS   A 1 143 ? 18.008 -11.734 1.007   1.00 15.55 ?  143 CYS   A HB2  1 
ATOM   3105 H  HB3  . CYS   A 1 143 ? 16.880 -12.756 1.438   1.00 15.55 ?  143 CYS   A HB3  1 
ATOM   3106 H  HG   . CYS   A 1 143 ? 17.747 -11.456 3.644   1.00 16.18 ?  143 CYS   A HG   1 
ATOM   3107 N  N    . VAL   A 1 144 ? 17.102 -15.540 1.349   1.00 13.21 ?  144 VAL   A N    1 
ATOM   3108 C  CA   . VAL   A 1 144 ? 16.768 -16.772 2.051   1.00 14.39 ?  144 VAL   A CA   1 
ATOM   3109 C  C    . VAL   A 1 144 ? 17.584 -17.942 1.520   1.00 14.18 ?  144 VAL   A C    1 
ATOM   3110 O  O    . VAL   A 1 144 ? 17.955 -18.850 2.275   1.00 14.82 ?  144 VAL   A O    1 
ATOM   3111 C  CB   . VAL   A 1 144 ? 15.252 -17.014 1.937   1.00 17.14 ?  144 VAL   A CB   1 
ATOM   3112 C  CG1  . VAL   A 1 144 ? 14.891 -18.441 2.289   1.00 19.24 ?  144 VAL   A CG1  1 
ATOM   3113 C  CG2  . VAL   A 1 144 ? 14.507 -16.003 2.811   1.00 17.11 ?  144 VAL   A CG2  1 
ATOM   3114 H  H    . VAL   A 1 144 ? 16.446 -15.187 0.908   1.00 15.90 ?  144 VAL   A H    1 
ATOM   3115 H  HA   . VAL   A 1 144 ? 16.973 -16.660 2.986   1.00 17.31 ?  144 VAL   A HA   1 
ATOM   3116 H  HB   . VAL   A 1 144 ? 14.974 -16.855 1.015   1.00 20.61 ?  144 VAL   A HB   1 
ATOM   3117 H  HG11 . VAL   A 1 144 ? 13.936 -18.489 2.469   1.00 23.14 ?  144 VAL   A HG11 1 
ATOM   3118 H  HG12 . VAL   A 1 144 ? 15.112 -19.019 1.543   1.00 23.14 ?  144 VAL   A HG12 1 
ATOM   3119 H  HG13 . VAL   A 1 144 ? 15.387 -18.704 3.078   1.00 23.14 ?  144 VAL   A HG13 1 
ATOM   3120 H  HG21 . VAL   A 1 144 ? 13.550 -16.155 2.738   1.00 20.58 ?  144 VAL   A HG21 1 
ATOM   3121 H  HG22 . VAL   A 1 144 ? 14.788 -16.109 3.732   1.00 20.58 ?  144 VAL   A HG22 1 
ATOM   3122 H  HG23 . VAL   A 1 144 ? 14.715 -15.099 2.508   1.00 20.58 ?  144 VAL   A HG23 1 
ATOM   3123 N  N    . ASP   A 1 145 ? 17.851 -17.959 0.217   1.00 14.25 ?  145 ASP   A N    1 
ATOM   3124 C  CA   . ASP   A 1 145 ? 18.561 -19.064 -0.417  1.00 14.85 ?  145 ASP   A CA   1 
ATOM   3125 C  C    . ASP   A 1 145 ? 20.080 -18.918 -0.371  1.00 14.56 ?  145 ASP   A C    1 
ATOM   3126 O  O    . ASP   A 1 145 ? 20.783 -19.818 -0.846  1.00 16.72 ?  145 ASP   A O    1 
ATOM   3127 C  CB   . ASP   A 1 145 ? 18.113 -19.195 -1.875  1.00 16.45 ?  145 ASP   A CB   1 
ATOM   3128 C  CG   . ASP   A 1 145 ? 16.670 -19.651 -2.009  1.00 18.73 ?  145 ASP   A CG   1 
ATOM   3129 O  OD1  . ASP   A 1 145 ? 16.099 -20.191 -1.035  1.00 19.35 ?  145 ASP   A OD1  1 
ATOM   3130 O  OD2  . ASP   A 1 145 ? 16.105 -19.458 -3.100  1.00 20.28 -1 145 ASP   A OD2  1 
ATOM   3131 H  H    . ASP   A 1 145 ? 17.604 -17.344 -0.333  1.00 17.15 ?  145 ASP   A H    1 
ATOM   3132 H  HA   . ASP   A 1 145 ? 18.324 -19.889 0.036   1.00 17.87 ?  145 ASP   A HA   1 
ATOM   3133 H  HB2  . ASP   A 1 145 ? 18.200 -18.332 -2.312  1.00 19.78 ?  145 ASP   A HB2  1 
ATOM   3134 H  HB3  . ASP   A 1 145 ? 18.670 -19.851 -2.320  1.00 19.78 ?  145 ASP   A HB3  1 
ATOM   3135 N  N    . THR   A 1 146 ? 20.603 -17.825 0.186   1.00 12.86 ?  146 THR   A N    1 
ATOM   3136 C  CA   . THR   A 1 146 ? 22.042 -17.570 0.201   1.00 12.45 ?  146 THR   A CA   1 
ATOM   3137 C  C    . THR   A 1 146 ? 22.597 -17.387 1.603   1.00 12.34 ?  146 THR   A C    1 
ATOM   3138 O  O    . THR   A 1 146 ? 23.674 -17.917 1.917   1.00 13.55 ?  146 THR   A O    1 
ATOM   3139 C  CB   . THR   A 1 146 ? 22.363 -16.322 -0.644  1.00 12.59 ?  146 THR   A CB   1 
ATOM   3140 O  OG1  . THR   A 1 146 ? 21.837 -16.492 -1.961  1.00 13.25 ?  146 THR   A OG1  1 
ATOM   3141 C  CG2  . THR   A 1 146 ? 23.860 -16.088 -0.734  1.00 13.26 ?  146 THR   A CG2  1 
ATOM   3142 H  H    . THR   A 1 146 ? 20.136 -17.204 0.559   1.00 15.48 ?  146 THR   A H    1 
ATOM   3143 H  HA   . THR   A 1 146 ? 22.500 -18.319 -0.198  1.00 14.99 ?  146 THR   A HA   1 
ATOM   3144 H  HB   . THR   A 1 146 ? 21.960 -15.539 -0.232  1.00 15.16 ?  146 THR   A HB   1 
ATOM   3145 H  HG1  . THR   A 1 146 ? 21.000 -16.567 -1.926  1.00 15.95 ?  146 THR   A HG1  1 
ATOM   3146 H  HG21 . THR   A 1 146 ? 24.047 -15.419 -1.409  1.00 15.96 ?  146 THR   A HG21 1 
ATOM   3147 H  HG22 . THR   A 1 146 ? 24.200 -15.778 0.120   1.00 15.96 ?  146 THR   A HG22 1 
ATOM   3148 H  HG23 . THR   A 1 146 ? 24.306 -16.913 -0.974  1.00 15.96 ?  146 THR   A HG23 1 
ATOM   3149 N  N    . VAL   A 1 147 ? 21.921 -16.607 2.437   1.00 12.33 ?  147 VAL   A N    1 
ATOM   3150 C  CA   . VAL   A 1 147 ? 22.413 -16.311 3.774   1.00 12.79 ?  147 VAL   A CA   1 
ATOM   3151 C  C    . VAL   A 1 147 ? 22.094 -17.482 4.689   1.00 13.34 ?  147 VAL   A C    1 
ATOM   3152 O  O    . VAL   A 1 147 ? 20.953 -17.961 4.738   1.00 13.68 ?  147 VAL   A O    1 
ATOM   3153 C  CB   . VAL   A 1 147 ? 21.797 -15.005 4.299   1.00 12.96 ?  147 VAL   A CB   1 
ATOM   3154 C  CG1  . VAL   A 1 147 ? 22.326 -14.692 5.679   1.00 14.05 ?  147 VAL   A CG1  1 
ATOM   3155 C  CG2  . VAL   A 1 147 ? 22.056 -13.858 3.333   1.00 12.90 ?  147 VAL   A CG2  1 
ATOM   3156 H  H    . VAL   A 1 147 ? 21.162 -16.235 2.255   1.00 14.84 ?  147 VAL   A H    1 
ATOM   3157 H  HA   . VAL   A 1 147 ? 23.372 -16.201 3.744   1.00 15.39 ?  147 VAL   A HA   1 
ATOM   3158 H  HB   . VAL   A 1 147 ? 20.838 -15.117 4.376   1.00 15.60 ?  147 VAL   A HB   1 
ATOM   3159 H  HG11 . VAL   A 1 147 ? 22.077 -13.789 5.917   1.00 16.91 ?  147 VAL   A HG11 1 
ATOM   3160 H  HG12 . VAL   A 1 147 ? 21.941 -15.320 6.315   1.00 16.91 ?  147 VAL   A HG12 1 
ATOM   3161 H  HG13 . VAL   A 1 147 ? 23.292 -14.782 5.674   1.00 16.91 ?  147 VAL   A HG13 1 
ATOM   3162 H  HG21 . VAL   A 1 147 ? 21.730 -13.034 3.733   1.00 15.53 ?  147 VAL   A HG21 1 
ATOM   3163 H  HG22 . VAL   A 1 147 ? 23.006 -13.795 3.169   1.00 15.53 ?  147 VAL   A HG22 1 
ATOM   3164 H  HG23 . VAL   A 1 147 ? 21.582 -14.034 2.507   1.00 15.53 ?  147 VAL   A HG23 1 
ATOM   3165 N  N    . ARG   A 1 148 ? 23.114 -17.944 5.411   1.00 13.51 ?  148 ARG   A N    1 
ATOM   3166 C  CA   . ARG   A 1 148 ? 22.986 -19.019 6.380   1.00 13.63 ?  148 ARG   A CA   1 
ATOM   3167 C  C    . ARG   A 1 148 ? 23.110 -18.544 7.816   1.00 13.87 ?  148 ARG   A C    1 
ATOM   3168 O  O    . ARG   A 1 148 ? 22.702 -19.271 8.731   1.00 15.78 ?  148 ARG   A O    1 
ATOM   3169 C  CB   . ARG   A 1 148 ? 24.032 -20.110 6.107   1.00 14.49 ?  148 ARG   A CB   1 
ATOM   3170 C  CG   . ARG   A 1 148 ? 23.871 -20.753 4.742   1.00 15.66 ?  148 ARG   A CG   1 
ATOM   3171 C  CD   . ARG   A 1 148 ? 24.954 -21.793 4.455   1.00 16.39 ?  148 ARG   A CD   1 
ATOM   3172 N  NE   . ARG   A 1 148 ? 26.292 -21.211 4.476   1.00 16.29 ?  148 ARG   A NE   1 
ATOM   3173 C  CZ   . ARG   A 1 148 ? 26.801 -20.472 3.498   1.00 15.56 ?  148 ARG   A CZ   1 
ATOM   3174 N  NH1  . ARG   A 1 148 ? 26.127 -20.239 2.384   1.00 15.95 ?  148 ARG   A NH1  1 
ATOM   3175 N  NH2  . ARG   A 1 148 ? 28.019 -19.950 3.642   1.00 15.76 ?  148 ARG   A NH2  1 
ATOM   3176 H  H    . ARG   A 1 148 ? 23.918 -17.637 5.344   1.00 16.25 ?  148 ARG   A H    1 
ATOM   3177 H  HA   . ARG   A 1 148 ? 22.115 -19.422 6.280   1.00 16.41 ?  148 ARG   A HA   1 
ATOM   3178 H  HB2  . ARG   A 1 148 ? 24.919 -19.726 6.151   1.00 17.44 ?  148 ARG   A HB2  1 
ATOM   3179 H  HB3  . ARG   A 1 148 ? 23.939 -20.812 6.772   1.00 17.44 ?  148 ARG   A HB3  1 
ATOM   3180 H  HG2  . ARG   A 1 148 ? 23.005 -21.186 4.701   1.00 18.84 ?  148 ARG   A HG2  1 
ATOM   3181 H  HG3  . ARG   A 1 148 ? 23.927 -20.058 4.065   1.00 18.84 ?  148 ARG   A HG3  1 
ATOM   3182 H  HD2  . ARG   A 1 148 ? 24.914 -22.486 5.132   1.00 19.71 ?  148 ARG   A HD2  1 
ATOM   3183 H  HD3  . ARG   A 1 148 ? 24.797 -22.178 3.577   1.00 19.71 ?  148 ARG   A HD3  1 
ATOM   3184 H  HE   . ARG   A 1 148 ? 26.785 -21.365 5.158   1.00 19.60 ?  148 ARG   A HE   1 
ATOM   3185 H  HH11 . ARG   A 1 148 ? 25.340 -20.564 2.278   1.00 19.18 ?  148 ARG   A HH11 1 
ATOM   3186 H  HH12 . ARG   A 1 148 ? 26.476 -19.751 1.766   1.00 19.18 ?  148 ARG   A HH12 1 
ATOM   3187 H  HH21 . ARG   A 1 148 ? 28.463 -20.091 4.364   1.00 18.96 ?  148 ARG   A HH21 1 
ATOM   3188 H  HH22 . ARG   A 1 148 ? 28.357 -19.463 3.017   1.00 18.96 ?  148 ARG   A HH22 1 
ATOM   3189 N  N    . THR   A 1 149 ? 23.656 -17.350 8.028   1.00 13.94 ?  149 THR   A N    1 
ATOM   3190 C  CA   . THR   A 1 149 ? 23.735 -16.752 9.346   1.00 13.81 ?  149 THR   A CA   1 
ATOM   3191 C  C    . THR   A 1 149 ? 22.410 -16.053 9.652   1.00 13.41 ?  149 THR   A C    1 
ATOM   3192 O  O    . THR   A 1 149 ? 21.475 -16.049 8.841   1.00 14.29 ?  149 THR   A O    1 
ATOM   3193 C  CB   . THR   A 1 149 ? 24.937 -15.816 9.404   1.00 14.17 ?  149 THR   A CB   1 
ATOM   3194 O  OG1  . THR   A 1 149 ? 24.811 -14.888 8.329   1.00 14.29 ?  149 THR   A OG1  1 
ATOM   3195 C  CG2  . THR   A 1 149 ? 26.246 -16.609 9.278   1.00 14.82 ?  149 THR   A CG2  1 
ATOM   3196 H  H    . THR   A 1 149 ? 24.001 -16.857 7.408   1.00 16.78 ?  149 THR   A H    1 
ATOM   3197 H  HA   . THR   A 1 149 ? 23.864 -17.456 10.002  1.00 16.62 ?  149 THR   A HA   1 
ATOM   3198 H  HB   . THR   A 1 149 ? 24.930 -15.342 10.247  1.00 17.05 ?  149 THR   A HB   1 
ATOM   3199 H  HG1  . THR   A 1 149 ? 25.461 -14.356 8.329   1.00 17.20 ?  149 THR   A HG1  1 
ATOM   3200 H  HG21 . THR   A 1 149 ? 27.003 -16.008 9.333   1.00 17.84 ?  149 THR   A HG21 1 
ATOM   3201 H  HG22 . THR   A 1 149 ? 26.310 -17.264 9.993   1.00 17.84 ?  149 THR   A HG22 1 
ATOM   3202 H  HG23 . THR   A 1 149 ? 26.275 -17.075 8.425   1.00 17.84 ?  149 THR   A HG23 1 
ATOM   3203 N  N    . ASN   A 1 150 ? 22.288 -15.513 10.858  1.00 13.58 ?  150 ASN   A N    1 
ATOM   3204 C  CA   . ASN   A 1 150 ? 21.006 -14.998 11.342  1.00 14.28 ?  150 ASN   A CA   1 
ATOM   3205 C  C    . ASN   A 1 150 ? 20.826 -13.560 10.872  1.00 13.45 ?  150 ASN   A C    1 
ATOM   3206 O  O    . ASN   A 1 150 ? 21.580 -12.665 11.276  1.00 14.81 ?  150 ASN   A O    1 
ATOM   3207 C  CB   . ASN   A 1 150 ? 20.942 -15.104 12.860  1.00 16.74 ?  150 ASN   A CB   1 
ATOM   3208 C  CG   . ASN   A 1 150 ? 20.841 -16.535 13.327  1.00 20.86 ?  150 ASN   A CG   1 
ATOM   3209 O  OD1  . ASN   A 1 150 ? 20.252 -17.374 12.645  1.00 22.32 ?  150 ASN   A OD1  1 
ATOM   3210 N  ND2  . ASN   A 1 150 ? 21.426 -16.829 14.483  1.00 23.11 ?  150 ASN   A ND2  1 
ATOM   3211 H  H    . ASN   A 1 150 ? 22.929 -15.446 11.424  1.00 16.34 ?  150 ASN   A H    1 
ATOM   3212 H  HA   . ASN   A 1 150 ? 20.283 -15.537 10.974  1.00 17.19 ?  150 ASN   A HA   1 
ATOM   3213 H  HB2  . ASN   A 1 150 ? 21.745 -14.719 13.241  1.00 20.14 ?  150 ASN   A HB2  1 
ATOM   3214 H  HB3  . ASN   A 1 150 ? 20.158 -14.632 13.182  1.00 20.14 ?  150 ASN   A HB3  1 
ATOM   3215 H  HD21 . ASN   A 1 150 ? 21.402 -17.635 14.791  1.00 27.78 ?  150 ASN   A HD21 1 
ATOM   3216 H  HD22 . ASN   A 1 150 ? 21.831 -16.215 14.933  1.00 27.78 ?  150 ASN   A HD22 1 
ATOM   3217 N  N    . VAL   A 1 151 ? 19.830 -13.333 10.021  1.00 13.14 ?  151 VAL   A N    1 
ATOM   3218 C  CA   . VAL   A 1 151 ? 19.622 -12.027 9.414   1.00 13.05 ?  151 VAL   A CA   1 
ATOM   3219 C  C    . VAL   A 1 151 ? 18.236 -11.510 9.777   1.00 12.99 ?  151 VAL   A C    1 
ATOM   3220 O  O    . VAL   A 1 151 ? 17.227 -12.220 9.635   1.00 14.44 ?  151 VAL   A O    1 
ATOM   3221 C  CB   . VAL   A 1 151 ? 19.907 -12.029 7.897   1.00 14.37 ?  151 VAL   A CB   1 
ATOM   3222 C  CG1  . VAL   A 1 151 ? 19.078 -13.053 7.153   1.00 15.51 ?  151 VAL   A CG1  1 
ATOM   3223 C  CG2  . VAL   A 1 151 ? 19.722 -10.625 7.310   1.00 14.72 ?  151 VAL   A CG2  1 
ATOM   3224 H  H    . VAL   A 1 151 ? 19.258 -13.927 9.776   1.00 15.81 ?  151 VAL   A H    1 
ATOM   3225 H  HA   . VAL   A 1 151 ? 20.265 -11.413 9.805   1.00 15.70 ?  151 VAL   A HA   1 
ATOM   3226 H  HB   . VAL   A 1 151 ? 20.839 -12.269 7.761   1.00 17.29 ?  151 VAL   A HB   1 
ATOM   3227 H  HG11 . VAL   A 1 151 ? 19.280 -13.007 6.204   1.00 18.66 ?  151 VAL   A HG11 1 
ATOM   3228 H  HG12 . VAL   A 1 151 ? 19.293 -13.942 7.488   1.00 18.66 ?  151 VAL   A HG12 1 
ATOM   3229 H  HG13 . VAL   A 1 151 ? 18.136 -12.870 7.298   1.00 18.66 ?  151 VAL   A HG13 1 
ATOM   3230 H  HG21 . VAL   A 1 151 ? 20.034 -10.625 6.388   1.00 17.72 ?  151 VAL   A HG21 1 
ATOM   3231 H  HG22 . VAL   A 1 151 ? 18.782 -10.390 7.338   1.00 17.72 ?  151 VAL   A HG22 1 
ATOM   3232 H  HG23 . VAL   A 1 151 ? 20.241 -9.993  7.831   1.00 17.72 ?  151 VAL   A HG23 1 
ATOM   3233 N  N    . TYR   A 1 152 ? 18.218 -10.267 10.265  1.00 13.01 ?  152 TYR   A N    1 
ATOM   3234 C  CA   . TYR   A 1 152 ? 17.025 -9.535  10.657  1.00 12.53 ?  152 TYR   A CA   1 
ATOM   3235 C  C    . TYR   A 1 152 ? 16.833 -8.431  9.627   1.00 12.20 ?  152 TYR   A C    1 
ATOM   3236 O  O    . TYR   A 1 152 ? 17.610 -7.470  9.582   1.00 12.88 ?  152 TYR   A O    1 
ATOM   3237 C  CB   . TYR   A 1 152 ? 17.207 -8.994  12.072  1.00 13.54 ?  152 TYR   A CB   1 
ATOM   3238 C  CG   . TYR   A 1 152 ? 17.166 -10.117 13.072  1.00 14.47 ?  152 TYR   A CG   1 
ATOM   3239 C  CD1  . TYR   A 1 152 ? 18.293 -10.885 13.340  1.00 15.77 ?  152 TYR   A CD1  1 
ATOM   3240 C  CD2  . TYR   A 1 152 ? 15.984 -10.455 13.709  1.00 14.99 ?  152 TYR   A CD2  1 
ATOM   3241 C  CE1  . TYR   A 1 152 ? 18.250 -11.942 14.230  1.00 17.55 ?  152 TYR   A CE1  1 
ATOM   3242 C  CE2  . TYR   A 1 152 ? 15.929 -11.519 14.603  1.00 16.49 ?  152 TYR   A CE2  1 
ATOM   3243 C  CZ   . TYR   A 1 152 ? 17.068 -12.255 14.860  1.00 17.57 ?  152 TYR   A CZ   1 
ATOM   3244 O  OH   . TYR   A 1 152 ? 17.027 -13.317 15.745  1.00 20.05 ?  152 TYR   A OH   1 
ATOM   3245 H  H    . TYR   A 1 152 ? 18.939 -9.792  10.364  1.00 15.67 ?  152 TYR   A H    1 
ATOM   3246 H  HA   . TYR   A 1 152 ? 16.259 -10.128 10.638  1.00 15.08 ?  152 TYR   A HA   1 
ATOM   3247 H  HB2  . TYR   A 1 152 ? 18.072 -8.561  12.140  1.00 16.29 ?  152 TYR   A HB2  1 
ATOM   3248 H  HB3  . TYR   A 1 152 ? 16.499 -8.372  12.277  1.00 16.29 ?  152 TYR   A HB3  1 
ATOM   3249 H  HD1  . TYR   A 1 152 ? 19.092 -10.680 12.911  1.00 18.97 ?  152 TYR   A HD1  1 
ATOM   3250 H  HD2  . TYR   A 1 152 ? 15.209 -9.963  13.536  1.00 18.04 ?  152 TYR   A HD2  1 
ATOM   3251 H  HE1  . TYR   A 1 152 ? 19.017 -12.436 14.401  1.00 21.11 ?  152 TYR   A HE1  1 
ATOM   3252 H  HE2  . TYR   A 1 152 ? 15.129 -11.725 15.032  1.00 19.84 ?  152 TYR   A HE2  1 
ATOM   3253 H  HH   . TYR   A 1 152 ? 16.253 -13.388 16.064  1.00 24.11 ?  152 TYR   A HH   1 
ATOM   3254 N  N    A LEU   A 1 153 ? 15.834 -8.615  8.764   0.72 12.28 ?  153 LEU   A N    1 
ATOM   3255 N  N    B LEU   A 1 153 ? 15.788 -8.543  8.822   0.28 12.11 ?  153 LEU   A N    1 
ATOM   3256 C  CA   A LEU   A 1 153 ? 15.576 -7.740  7.627   0.72 12.12 ?  153 LEU   A CA   1 
ATOM   3257 C  CA   B LEU   A 1 153 ? 15.529 -7.555  7.787   0.28 11.71 ?  153 LEU   A CA   1 
ATOM   3258 C  C    A LEU   A 1 153 ? 14.565 -6.663  7.993   0.72 12.46 ?  153 LEU   A C    1 
ATOM   3259 C  C    B LEU   A 1 153 ? 14.575 -6.486  8.300   0.28 11.94 ?  153 LEU   A C    1 
ATOM   3260 O  O    A LEU   A 1 153 ? 13.456 -6.967  8.449   0.72 13.46 ?  153 LEU   A O    1 
ATOM   3261 O  O    B LEU   A 1 153 ? 13.507 -6.799  8.837   0.28 12.52 ?  153 LEU   A O    1 
ATOM   3262 C  CB   A LEU   A 1 153 ? 15.019 -8.550  6.453   0.72 12.39 ?  153 LEU   A CB   1 
ATOM   3263 C  CB   B LEU   A 1 153 ? 14.939 -8.230  6.554   0.28 11.67 ?  153 LEU   A CB   1 
ATOM   3264 C  CG   A LEU   A 1 153 ? 15.959 -9.543  5.768   0.72 12.27 ?  153 LEU   A CG   1 
ATOM   3265 C  CG   B LEU   A 1 153 ? 15.846 -9.287  5.924   0.28 11.94 ?  153 LEU   A CG   1 
ATOM   3266 C  CD1  A LEU   A 1 153 ? 15.165 -10.451 4.839   0.72 12.49 ?  153 LEU   A CD1  1 
ATOM   3267 C  CD1  B LEU   A 1 153 ? 15.085 -10.042 4.847   0.28 12.46 ?  153 LEU   A CD1  1 
ATOM   3268 C  CD2  A LEU   A 1 153 ? 17.043 -8.805  4.995   0.72 12.31 ?  153 LEU   A CD2  1 
ATOM   3269 C  CD2  B LEU   A 1 153 ? 17.116 -8.652  5.364   0.28 12.23 ?  153 LEU   A CD2  1 
ATOM   3270 H  H    A LEU   A 1 153 ? 15.265 -9.265  8.827   0.72 14.79 ?  153 LEU   A H    1 
ATOM   3271 H  H    B LEU   A 1 153 ? 15.208 -9.181  8.857   0.28 14.58 ?  153 LEU   A H    1 
ATOM   3272 H  HA   A LEU   A 1 153 ? 16.398 -7.322  7.351   0.72 14.60 ?  153 LEU   A HA   1 
ATOM   3273 H  HA   B LEU   A 1 153 ? 16.362 -7.128  7.543   0.28 14.10 ?  153 LEU   A HA   1 
ATOM   3274 H  HB2  A LEU   A 1 153 ? 14.254 -9.059  6.770   0.72 14.91 ?  153 LEU   A HB2  1 
ATOM   3275 H  HB2  B LEU   A 1 153 ? 14.109 -8.661  6.809   0.28 14.06 ?  153 LEU   A HB2  1 
ATOM   3276 H  HB3  A LEU   A 1 153 ? 14.724 -7.929  5.770   0.72 14.91 ?  153 LEU   A HB3  1 
ATOM   3277 H  HB3  B LEU   A 1 153 ? 14.766 -7.547  5.889   0.28 14.06 ?  153 LEU   A HB3  1 
ATOM   3278 H  HG   A LEU   A 1 153 ? 16.388 -10.100 6.441   0.72 14.78 ?  153 LEU   A HG   1 
ATOM   3279 H  HG   B LEU   A 1 153 ? 16.109 -9.922  6.609   0.28 14.37 ?  153 LEU   A HG   1 
ATOM   3280 H  HD11 A LEU   A 1 153 ? 15.742 -11.163 4.521   0.72 15.04 ?  153 LEU   A HD11 1 
ATOM   3281 H  HD11 B LEU   A 1 153 ? 15.670 -10.710 4.460   0.28 15.00 ?  153 LEU   A HD11 1 
ATOM   3282 H  HD12 A LEU   A 1 153 ? 14.417 -10.825 5.326   0.72 15.04 ?  153 LEU   A HD12 1 
ATOM   3283 H  HD12 B LEU   A 1 153 ? 14.312 -10.469 5.249   0.28 15.00 ?  153 LEU   A HD12 1 
ATOM   3284 H  HD13 A LEU   A 1 153 ? 14.844 -9.925  4.089   0.72 15.04 ?  153 LEU   A HD13 1 
ATOM   3285 H  HD13 B LEU   A 1 153 ? 14.799 -9.414  4.165   0.28 15.00 ?  153 LEU   A HD13 1 
ATOM   3286 H  HD21 A LEU   A 1 153 ? 17.642 -9.455  4.603   0.72 14.83 ?  153 LEU   A HD21 1 
ATOM   3287 H  HD21 B LEU   A 1 153 ? 17.612 -9.325  4.873   0.28 14.73 ?  153 LEU   A HD21 1 
ATOM   3288 H  HD22 A LEU   A 1 153 ? 16.619 -8.278  4.302   0.72 14.83 ?  153 LEU   A HD22 1 
ATOM   3289 H  HD22 B LEU   A 1 153 ? 16.870 -7.924  4.773   0.28 14.73 ?  153 LEU   A HD22 1 
ATOM   3290 H  HD23 A LEU   A 1 153 ? 17.524 -8.233  5.608   0.72 14.83 ?  153 LEU   A HD23 1 
ATOM   3291 H  HD23 B LEU   A 1 153 ? 17.654 -8.315  6.099   0.28 14.73 ?  153 LEU   A HD23 1 
ATOM   3292 N  N    A ALA   A 1 154 ? 14.930 -5.410  7.745   0.72 12.08 ?  154 ALA   A N    1 
ATOM   3293 N  N    B ALA   A 1 154 ? 14.966 -5.226  8.132   0.28 11.69 ?  154 ALA   A N    1 
ATOM   3294 C  CA   A ALA   A 1 154 ? 14.060 -4.260  7.963   0.72 12.15 ?  154 ALA   A CA   1 
ATOM   3295 C  CA   B ALA   A 1 154 ? 14.118 -4.080  8.430   0.28 12.25 ?  154 ALA   A CA   1 
ATOM   3296 C  C    A ALA   A 1 154 ? 13.579 -3.757  6.610   0.72 11.51 ?  154 ALA   A C    1 
ATOM   3297 C  C    B ALA   A 1 154 ? 13.633 -3.505  7.106   0.28 12.29 ?  154 ALA   A C    1 
ATOM   3298 O  O    A ALA   A 1 154 ? 14.392 -3.387  5.757   0.72 12.30 ?  154 ALA   A O    1 
ATOM   3299 O  O    B ALA   A 1 154 ? 14.446 -3.101  6.267   0.28 11.88 ?  154 ALA   A O    1 
ATOM   3300 C  CB   A ALA   A 1 154 ? 14.811 -3.147  8.692   0.72 12.66 ?  154 ALA   A CB   1 
ATOM   3301 C  CB   B ALA   A 1 154 ? 14.888 -3.024  9.225   0.28 12.54 ?  154 ALA   A CB   1 
ATOM   3302 H  H    A ALA   A 1 154 ? 15.699 -5.202  7.430   0.72 14.54 ?  154 ALA   A H    1 
ATOM   3303 H  H    B ALA   A 1 154 ? 15.743 -5.000  7.832   0.28 14.08 ?  154 ALA   A H    1 
ATOM   3304 H  HA   A ALA   A 1 154 ? 13.289 -4.525  8.492   0.72 14.63 ?  154 ALA   A HA   1 
ATOM   3305 H  HA   B ALA   A 1 154 ? 13.350 -4.360  8.951   0.28 14.75 ?  154 ALA   A HA   1 
ATOM   3306 H  HB1  A ALA   A 1 154 ? 14.211 -2.400  8.824   0.72 15.24 ?  154 ALA   A HB1  1 
ATOM   3307 H  HB1  B ALA   A 1 154 ? 14.300 -2.276  9.413   0.28 15.09 ?  154 ALA   A HB1  1 
ATOM   3308 H  HB2  A ALA   A 1 154 ? 15.118 -3.485  9.548   0.72 15.24 ?  154 ALA   A HB2  1 
ATOM   3309 H  HB2  B ALA   A 1 154 ? 15.198 -3.417  10.057  0.28 15.09 ?  154 ALA   A HB2  1 
ATOM   3310 H  HB3  A ALA   A 1 154 ? 15.569 -2.876  8.152   0.72 15.24 ?  154 ALA   A HB3  1 
ATOM   3311 H  HB3  B ALA   A 1 154 ? 15.647 -2.723  8.700   0.28 15.09 ?  154 ALA   A HB3  1 
ATOM   3312 N  N    A VAL   A 1 155 ? 12.262 -3.739  6.424   0.42 9.42  ?  155 VAL   A N    1 
ATOM   3313 N  N    B VAL   A 1 155 ? 12.317 -3.485  6.913   0.28 12.82 ?  155 VAL   A N    1 
ATOM   3314 C  CA   A VAL   A 1 155 ? 11.621 -3.265  5.201   0.42 11.81 ?  155 VAL   A CA   1 
ATOM   3315 C  CA   B VAL   A 1 155 ? 11.690 -2.921  5.721   0.28 14.54 ?  155 VAL   A CA   1 
ATOM   3316 C  CA   T VAL   A 1 155 ? 11.612 -3.301  5.299   0.30 13.75 ?  155 VAL   A CA   1 
ATOM   3317 C  C    A VAL   A 1 155 ? 10.895 -1.969  5.544   0.42 13.16 ?  155 VAL   A C    1 
ATOM   3318 C  C    B VAL   A 1 155 ? 10.687 -1.869  6.176   0.28 16.44 ?  155 VAL   A C    1 
ATOM   3319 C  C    T VAL   A 1 155 ? 10.988 -1.933  5.592   0.30 13.84 ?  155 VAL   A C    1 
ATOM   3320 O  O    A VAL   A 1 155 ? 9.918  -1.985  6.300   0.42 13.89 ?  155 VAL   A O    1 
ATOM   3321 O  O    B VAL   A 1 155 ? 9.734  -2.187  6.897   0.28 16.54 ?  155 VAL   A O    1 
ATOM   3322 O  O    T VAL   A 1 155 ? 10.143 -1.800  6.473   0.30 13.69 ?  155 VAL   A O    1 
ATOM   3323 C  CB   A VAL   A 1 155 ? 10.648 -4.313  4.642   0.42 12.75 ?  155 VAL   A CB   1 
ATOM   3324 C  CB   B VAL   A 1 155 ? 11.001 -4.002  4.874   0.28 14.54 ?  155 VAL   A CB   1 
ATOM   3325 C  CB   T VAL   A 1 155 ? 10.586 -4.325  4.766   0.30 13.85 ?  155 VAL   A CB   1 
ATOM   3326 C  CG1  A VAL   A 1 155 ? 9.960  -3.797  3.388   0.42 13.99 ?  155 VAL   A CG1  1 
ATOM   3327 C  CG1  B VAL   A 1 155 ? 10.378 -3.383  3.631   0.28 14.75 ?  155 VAL   A CG1  1 
ATOM   3328 C  CG1  T VAL   A 1 155 ? 9.875  -3.788  3.535   0.30 14.33 ?  155 VAL   A CG1  1 
ATOM   3329 C  CG2  A VAL   A 1 155 ? 11.384 -5.613  4.353   0.42 13.69 ?  155 VAL   A CG2  1 
ATOM   3330 C  CG2  B VAL   A 1 155 ? 11.993 -5.096  4.496   0.28 14.23 ?  155 VAL   A CG2  1 
ATOM   3331 C  CG2  T VAL   A 1 155 ? 11.276 -5.646  4.444   0.30 14.34 ?  155 VAL   A CG2  1 
ATOM   3332 H  H    A VAL   A 1 155 ? 11.699 -4.031  7.006   0.42 11.35 ?  155 VAL   A H    1 
ATOM   3333 H  H    B VAL   A 1 155 ? 11.751 -3.795  7.480   0.28 15.43 ?  155 VAL   A H    1 
ATOM   3334 H  HA   A VAL   A 1 155 ? 12.295 -3.076  4.530   0.42 14.22 ?  155 VAL   A HA   1 
ATOM   3335 H  HA   B VAL   A 1 155 ? 12.363 -2.484  5.175   0.28 17.50 ?  155 VAL   A HA   1 
ATOM   3336 H  HB   A VAL   A 1 155 ? 9.964  -4.496  5.307   0.42 15.35 ?  155 VAL   A HB   1 
ATOM   3337 H  HB   B VAL   A 1 155 ? 10.293 -4.407  5.398   0.28 17.50 ?  155 VAL   A HB   1 
ATOM   3338 H  HB   T VAL   A 1 155 ? 9.921  -4.493  5.451   0.30 16.66 ?  155 VAL   A HB   1 
ATOM   3339 H  HG11 A VAL   A 1 155 ? 9.477  -4.528  2.972   0.42 16.84 ?  155 VAL   A HG11 1 
ATOM   3340 H  HG11 B VAL   A 1 155 ? 10.111 -4.093  3.028   0.28 17.74 ?  155 VAL   A HG11 1 
ATOM   3341 H  HG11 T VAL   A 1 155 ? 9.361  -4.505  3.130   0.30 17.24 ?  155 VAL   A HG11 1 
ATOM   3342 H  HG12 A VAL   A 1 155 ? 9.342  -3.090  3.632   0.42 16.84 ?  155 VAL   A HG12 1 
ATOM   3343 H  HG12 B VAL   A 1 155 ? 9.602  -2.860  3.891   0.28 17.74 ?  155 VAL   A HG12 1 
ATOM   3344 H  HG12 T VAL   A 1 155 ? 9.285  -3.066  3.798   0.30 17.24 ?  155 VAL   A HG12 1 
ATOM   3345 H  HG13 A VAL   A 1 155 ? 10.632 -3.456  2.779   0.42 16.84 ?  155 VAL   A HG13 1 
ATOM   3346 H  HG13 B VAL   A 1 155 ? 11.033 -2.812  3.200   0.28 17.74 ?  155 VAL   A HG13 1 
ATOM   3347 H  HG13 T VAL   A 1 155 ? 10.539 -3.464  2.905   0.30 17.24 ?  155 VAL   A HG13 1 
ATOM   3348 H  HG21 A VAL   A 1 155 ? 10.770 -6.237  3.934   0.42 16.48 ?  155 VAL   A HG21 1 
ATOM   3349 H  HG21 B VAL   A 1 155 ? 11.551 -5.736  3.918   0.28 17.13 ?  155 VAL   A HG21 1 
ATOM   3350 H  HG21 T VAL   A 1 155 ? 10.616 -6.278  4.117   0.30 17.26 ?  155 VAL   A HG21 1 
ATOM   3351 H  HG22 A VAL   A 1 155 ? 12.126 -5.429  3.757   0.42 16.48 ?  155 VAL   A HG22 1 
ATOM   3352 H  HG22 B VAL   A 1 155 ? 12.745 -4.694  4.033   0.28 17.13 ?  155 VAL   A HG22 1 
ATOM   3353 H  HG22 T VAL   A 1 155 ? 11.950 -5.492  3.761   0.30 17.26 ?  155 VAL   A HG22 1 
ATOM   3354 H  HG23 A VAL   A 1 155 ? 11.713 -5.984  5.187   0.42 16.48 ?  155 VAL   A HG23 1 
ATOM   3355 H  HG23 B VAL   A 1 155 ? 12.301 -5.538  5.304   0.28 17.13 ?  155 VAL   A HG23 1 
ATOM   3356 H  HG23 T VAL   A 1 155 ? 11.694 -5.990  5.248   0.30 17.26 ?  155 VAL   A HG23 1 
ATOM   3357 N  N    A PHE   A 1 156 ? 11.357 -0.843  4.986   0.42 14.36 ?  156 PHE   A N    1 
ATOM   3358 N  N    B PHE   A 1 156 ? 10.899 -0.618  5.758   0.28 17.86 ?  156 PHE   A N    1 
ATOM   3359 N  N    T PHE   A 1 156 ? 11.421 -0.917  4.843   0.30 14.47 ?  156 PHE   A N    1 
ATOM   3360 C  CA   A PHE   A 1 156 ? 10.801 0.461   5.365   0.42 15.76 ?  156 PHE   A CA   1 
ATOM   3361 C  CA   B PHE   A 1 156 ? 10.036 0.470   6.211   0.28 19.36 ?  156 PHE   A CA   1 
ATOM   3362 C  CA   T PHE   A 1 156 ? 10.987 0.454   5.112   0.30 15.01 ?  156 PHE   A CA   1 
ATOM   3363 C  C    A PHE   A 1 156 ? 9.338  0.608   4.951   0.42 15.76 ?  156 PHE   A C    1 
ATOM   3364 C  C    B PHE   A 1 156 ? 8.681  0.448   5.510   0.28 20.12 ?  156 PHE   A C    1 
ATOM   3365 C  C    T PHE   A 1 156 ? 9.524  0.663   4.748   0.30 15.45 ?  156 PHE   A C    1 
ATOM   3366 O  O    A PHE   A 1 156 ? 8.516  1.124   5.722   0.42 16.33 ?  156 PHE   A O    1 
ATOM   3367 O  O    B PHE   A 1 156 ? 7.634  0.553   6.160   0.28 20.60 ?  156 PHE   A O    1 
ATOM   3368 O  O    T PHE   A 1 156 ? 8.776  1.311   5.491   0.30 16.13 ?  156 PHE   A O    1 
ATOM   3369 C  CB   A PHE   A 1 156 ? 11.643 1.588   4.758   0.42 16.93 ?  156 PHE   A CB   1 
ATOM   3370 C  CB   B PHE   A 1 156 ? 10.727 1.814   5.966   0.28 20.17 ?  156 PHE   A CB   1 
ATOM   3371 C  CB   T PHE   A 1 156 ? 11.861 1.420   4.314   0.30 14.55 ?  156 PHE   A CB   1 
ATOM   3372 C  CG   A PHE   A 1 156 ? 11.139 2.973   5.092   0.42 18.07 ?  156 PHE   A CG   1 
ATOM   3373 C  CG   B PHE   A 1 156 ? 10.047 2.992   6.624   0.28 20.87 ?  156 PHE   A CG   1 
ATOM   3374 C  CG   T PHE   A 1 156 ? 11.524 2.875   4.526   0.30 14.41 ?  156 PHE   A CG   1 
ATOM   3375 C  CD1  A PHE   A 1 156 ? 11.076 3.395   6.410   0.42 18.35 ?  156 PHE   A CD1  1 
ATOM   3376 C  CD1  B PHE   A 1 156 ? 9.092  2.815   7.616   0.28 21.16 ?  156 PHE   A CD1  1 
ATOM   3377 C  CD1  T PHE   A 1 156 ? 11.935 3.530   5.678   0.30 15.06 ?  156 PHE   A CD1  1 
ATOM   3378 C  CD2  A PHE   A 1 156 ? 10.745 3.850   4.092   0.42 18.86 ?  156 PHE   A CD2  1 
ATOM   3379 C  CD2  B PHE   A 1 156 ? 10.372 4.284   6.243   0.28 21.02 ?  156 PHE   A CD2  1 
ATOM   3380 C  CD2  T PHE   A 1 156 ? 10.820 3.589   3.568   0.30 14.72 ?  156 PHE   A CD2  1 
ATOM   3381 C  CE1  A PHE   A 1 156 ? 10.622 4.665   6.727   0.42 19.20 ?  156 PHE   A CE1  1 
ATOM   3382 C  CE1  B PHE   A 1 156 ? 8.478  3.906   8.211   0.28 21.22 ?  156 PHE   A CE1  1 
ATOM   3383 C  CE1  T PHE   A 1 156 ? 11.637 4.862   5.880   0.30 15.70 ?  156 PHE   A CE1  1 
ATOM   3384 C  CE2  A PHE   A 1 156 ? 10.286 5.120   4.403   0.42 19.66 ?  156 PHE   A CE2  1 
ATOM   3385 C  CE2  B PHE   A 1 156 ? 9.764  5.374   6.833   0.28 20.96 ?  156 PHE   A CE2  1 
ATOM   3386 C  CE2  T PHE   A 1 156 ? 10.522 4.926   3.763   0.30 15.29 ?  156 PHE   A CE2  1 
ATOM   3387 C  CZ   A PHE   A 1 156 ? 10.229 5.527   5.721   0.42 19.66 ?  156 PHE   A CZ   1 
ATOM   3388 C  CZ   B PHE   A 1 156 ? 8.816  5.187   7.818   0.28 21.07 ?  156 PHE   A CZ   1 
ATOM   3389 C  CZ   T PHE   A 1 156 ? 10.933 5.562   4.923   0.30 15.52 ?  156 PHE   A CZ   1 
ATOM   3390 H  H    A PHE   A 1 156 ? 11.989 -0.812  4.401   0.42 17.27 ?  156 PHE   A H    1 
ATOM   3391 H  H    B PHE   A 1 156 ? 11.535 -0.373  5.230   0.28 21.48 ?  156 PHE   A H    1 
ATOM   3392 H  H    T PHE   A 1 156 ? 11.965 -0.997  4.184   0.30 17.41 ?  156 PHE   A H    1 
ATOM   3393 H  HA   A PHE   A 1 156 ? 10.853 0.551   6.328   0.42 18.96 ?  156 PHE   A HA   1 
ATOM   3394 H  HA   B PHE   A 1 156 ? 9.890  0.361   7.162   0.28 23.28 ?  156 PHE   A HA   1 
ATOM   3395 H  HA   T PHE   A 1 156 ? 11.099 0.641   6.058   0.30 18.06 ?  156 PHE   A HA   1 
ATOM   3396 H  HB2  A PHE   A 1 156 ? 12.558 1.515   5.089   0.42 20.37 ?  156 PHE   A HB2  1 
ATOM   3397 H  HB2  B PHE   A 1 156 ? 11.630 1.765   6.310   0.28 24.25 ?  156 PHE   A HB2  1 
ATOM   3398 H  HB2  T PHE   A 1 156 ? 12.784 1.287   4.574   0.30 17.51 ?  156 PHE   A HB2  1 
ATOM   3399 H  HB3  A PHE   A 1 156 ? 11.643 1.497   3.791   0.42 20.37 ?  156 PHE   A HB3  1 
ATOM   3400 H  HB3  B PHE   A 1 156 ? 10.746 1.983   5.011   0.28 24.25 ?  156 PHE   A HB3  1 
ATOM   3401 H  HB3  T PHE   A 1 156 ? 11.752 1.224   3.371   0.30 17.51 ?  156 PHE   A HB3  1 
ATOM   3402 H  HD1  A PHE   A 1 156 ? 11.347 2.816   7.090   0.42 22.07 ?  156 PHE   A HD1  1 
ATOM   3403 H  HD1  B PHE   A 1 156 ? 8.859  1.956   7.886   0.28 25.44 ?  156 PHE   A HD1  1 
ATOM   3404 H  HD1  T PHE   A 1 156 ? 12.406 3.056   6.331   0.30 18.12 ?  156 PHE   A HD1  1 
ATOM   3405 H  HD2  A PHE   A 1 156 ? 10.788 3.577   3.203   0.42 22.68 ?  156 PHE   A HD2  1 
ATOM   3406 H  HD2  B PHE   A 1 156 ? 11.010 4.418   5.580   0.28 25.27 ?  156 PHE   A HD2  1 
ATOM   3407 H  HD2  T PHE   A 1 156 ? 10.540 3.161   2.793   0.30 17.71 ?  156 PHE   A HD2  1 
ATOM   3408 H  HE1  A PHE   A 1 156 ? 10.585 4.935   7.617   0.42 23.08 ?  156 PHE   A HE1  1 
ATOM   3409 H  HE1  B PHE   A 1 156 ? 7.838  3.778   8.875   0.28 25.51 ?  156 PHE   A HE1  1 
ATOM   3410 H  HE1  T PHE   A 1 156 ? 11.912 5.284   6.662   0.30 18.88 ?  156 PHE   A HE1  1 
ATOM   3411 H  HE2  A PHE   A 1 156 ? 10.026 5.696   3.724   0.42 23.64 ?  156 PHE   A HE2  1 
ATOM   3412 H  HE2  B PHE   A 1 156 ? 9.995  6.234   6.564   0.28 25.20 ?  156 PHE   A HE2  1 
ATOM   3413 H  HE2  T PHE   A 1 156 ? 10.044 5.394   3.122   0.30 18.40 ?  156 PHE   A HE2  1 
ATOM   3414 H  HZ   A PHE   A 1 156 ? 9.923  6.379   5.934   0.42 23.64 ?  156 PHE   A HZ   1 
ATOM   3415 H  HZ   B PHE   A 1 156 ? 8.406  5.922   8.214   0.28 25.33 ?  156 PHE   A HZ   1 
ATOM   3416 H  HZ   T PHE   A 1 156 ? 10.730 6.458   5.061   0.30 18.67 ?  156 PHE   A HZ   1 
ATOM   3417 N  N    A ASP   A 1 157 ? 8.997  0.178   3.740   0.42 16.73 ?  157 ASP   A N    1 
ATOM   3418 N  N    B ASP   A 1 157 ? 8.683  0.332   4.185   0.28 20.25 ?  157 ASP   A N    1 
ATOM   3419 N  N    T ASP   A 1 157 ? 9.108  0.143   3.601   0.30 15.97 ?  157 ASP   A N    1 
ATOM   3420 C  CA   A ASP   A 1 157 ? 7.666  0.418   3.192   0.42 18.54 ?  157 ASP   A CA   1 
ATOM   3421 C  CA   B ASP   A 1 157 ? 7.454  0.471   3.414   0.28 20.80 ?  157 ASP   A CA   1 
ATOM   3422 C  CA   T ASP   A 1 157 ? 7.798  0.431   3.038   0.30 16.89 ?  157 ASP   A CA   1 
ATOM   3423 C  C    A ASP   A 1 157 ? 6.683  -0.620  3.727   0.42 19.00 ?  157 ASP   A C    1 
ATOM   3424 C  C    B ASP   A 1 157 ? 6.471  -0.645  3.756   0.28 20.79 ?  157 ASP   A C    1 
ATOM   3425 C  C    T ASP   A 1 157 ? 6.772  -0.558  3.583   0.30 17.82 ?  157 ASP   A C    1 
ATOM   3426 O  O    A ASP   A 1 157 ? 6.838  -1.818  3.468   0.42 18.57 ?  157 ASP   A O    1 
ATOM   3427 O  O    B ASP   A 1 157 ? 6.804  -1.831  3.684   0.28 20.69 ?  157 ASP   A O    1 
ATOM   3428 O  O    T ASP   A 1 157 ? 6.874  -1.765  3.335   0.30 17.58 ?  157 ASP   A O    1 
ATOM   3429 C  CB   A ASP   A 1 157 ? 7.723  0.358   1.669   0.42 19.79 ?  157 ASP   A CB   1 
ATOM   3430 C  CB   B ASP   A 1 157 ? 7.791  0.457   1.922   0.28 21.37 ?  157 ASP   A CB   1 
ATOM   3431 C  CB   T ASP   A 1 157 ? 7.889  0.332   1.519   0.30 17.01 ?  157 ASP   A CB   1 
ATOM   3432 C  CG   A ASP   A 1 157 ? 6.419  0.788   1.018   0.42 21.17 ?  157 ASP   A CG   1 
ATOM   3433 C  CG   B ASP   A 1 157 ? 6.700  1.062   1.071   0.28 22.03 ?  157 ASP   A CG   1 
ATOM   3434 C  CG   T ASP   A 1 157 ? 6.708  0.934   0.832   0.30 16.75 ?  157 ASP   A CG   1 
ATOM   3435 O  OD1  A ASP   A 1 157 ? 6.070  1.985   1.089   0.42 22.12 ?  157 ASP   A OD1  1 
ATOM   3436 O  OD1  B ASP   A 1 157 ? 6.589  2.306   1.044   0.28 22.52 ?  157 ASP   A OD1  1 
ATOM   3437 O  OD1  T ASP   A 1 157 ? 5.596  0.403   1.026   0.30 16.89 ?  157 ASP   A OD1  1 
ATOM   3438 O  OD2  A ASP   A 1 157 ? 5.730  -0.078  0.439   0.42 21.20 -1 157 ASP   A OD2  1 
ATOM   3439 O  OD2  B ASP   A 1 157 ? 5.955  0.293   0.425   0.28 22.14 -1 157 ASP   A OD2  1 
ATOM   3440 O  OD2  T ASP   A 1 157 ? 6.889  1.939   0.114   0.30 16.04 -1 157 ASP   A OD2  1 
ATOM   3441 H  H    A ASP   A 1 157 ? 9.526  -0.262  3.216   0.42 20.12 ?  157 ASP   A H    1 
ATOM   3442 H  H    B ASP   A 1 157 ? 9.380  0.179   3.709   0.28 24.35 ?  157 ASP   A H    1 
ATOM   3443 H  H    T ASP   A 1 157 ? 9.583  -0.384  3.115   0.30 19.22 ?  157 ASP   A H    1 
ATOM   3444 H  HA   A ASP   A 1 157 ? 7.367  1.300   3.459   0.42 22.29 ?  157 ASP   A HA   1 
ATOM   3445 H  HA   B ASP   A 1 157 ? 7.034  1.317   3.623   0.28 25.01 ?  157 ASP   A HA   1 
ATOM   3446 H  HA   T ASP   A 1 157 ? 7.527  1.330   3.282   0.30 20.32 ?  157 ASP   A HA   1 
ATOM   3447 H  HB2  A ASP   A 1 157 ? 8.466  0.911   1.363   0.42 23.80 ?  157 ASP   A HB2  1 
ATOM   3448 H  HB2  B ASP   A 1 157 ? 8.604  0.968   1.780   0.28 25.69 ?  157 ASP   A HB2  1 
ATOM   3449 H  HB2  T ASP   A 1 157 ? 8.680  0.798   1.219   0.30 20.46 ?  157 ASP   A HB2  1 
ATOM   3450 H  HB3  A ASP   A 1 157 ? 7.872  -0.560  1.397   0.42 23.80 ?  157 ASP   A HB3  1 
ATOM   3451 H  HB3  B ASP   A 1 157 ? 7.915  -0.455  1.630   0.28 25.69 ?  157 ASP   A HB3  1 
ATOM   3452 H  HB3  T ASP   A 1 157 ? 7.935  -0.603  1.267   0.30 20.46 ?  157 ASP   A HB3  1 
ATOM   3453 N  N    A LYS   A 1 158 ? 5.663  -0.160  4.461   0.42 20.08 ?  158 LYS   A N    1 
ATOM   3454 N  N    B LYS   A 1 158 ? 5.249  -0.252  4.124   0.28 20.94 ?  158 LYS   A N    1 
ATOM   3455 N  N    T LYS   A 1 158 ? 5.776  -0.043  4.312   0.30 19.18 ?  158 LYS   A N    1 
ATOM   3456 C  CA   A LYS   A 1 158 ? 4.695  -1.088  5.045   0.42 20.93 ?  158 LYS   A CA   1 
ATOM   3457 C  CA   B LYS   A 1 158 ? 4.253  -1.213  4.589   0.28 21.35 ?  158 LYS   A CA   1 
ATOM   3458 C  CA   T LYS   A 1 158 ? 4.794  -0.919  4.945   0.30 20.76 ?  158 LYS   A CA   1 
ATOM   3459 C  C    A LYS   A 1 158 ? 3.950  -1.859  3.963   0.42 20.38 ?  158 LYS   A C    1 
ATOM   3460 C  C    B LYS   A 1 158 ? 3.718  -2.058  3.437   0.28 20.43 ?  158 LYS   A C    1 
ATOM   3461 C  C    T LYS   A 1 158 ? 4.017  -1.721  3.909   0.30 20.80 ?  158 LYS   A C    1 
ATOM   3462 O  O    A LYS   A 1 158 ? 3.735  -3.070  4.090   0.42 20.53 ?  158 LYS   A O    1 
ATOM   3463 O  O    B LYS   A 1 158 ? 3.708  -3.292  3.511   0.28 19.81 ?  158 LYS   A O    1 
ATOM   3464 O  O    T LYS   A 1 158 ? 3.772  -2.918  4.096   0.30 20.84 ?  158 LYS   A O    1 
ATOM   3465 C  CB   A LYS   A 1 158 ? 3.714  -0.338  5.951   0.42 22.46 ?  158 LYS   A CB   1 
ATOM   3466 C  CB   B LYS   A 1 158 ? 3.113  -0.467  5.287   0.28 22.83 ?  158 LYS   A CB   1 
ATOM   3467 C  CB   T LYS   A 1 158 ? 3.841  -0.106  5.827   0.30 22.53 ?  158 LYS   A CB   1 
ATOM   3468 C  CG   A LYS   A 1 158 ? 2.478  -1.144  6.382   0.42 24.13 ?  158 LYS   A CG   1 
ATOM   3469 C  CG   B LYS   A 1 158 ? 2.001  -1.359  5.821   0.28 24.31 ?  158 LYS   A CG   1 
ATOM   3470 C  CG   T LYS   A 1 158 ? 2.613  -0.879  6.311   0.30 24.22 ?  158 LYS   A CG   1 
ATOM   3471 C  CD   A LYS   A 1 158 ? 2.822  -2.424  7.151   0.42 25.45 ?  158 LYS   A CD   1 
ATOM   3472 C  CD   B LYS   A 1 158 ? 2.481  -2.199  6.992   0.28 25.56 ?  158 LYS   A CD   1 
ATOM   3473 C  CD   T LYS   A 1 158 ? 2.987  -2.096  7.152   0.30 25.74 ?  158 LYS   A CD   1 
ATOM   3474 C  CE   A LYS   A 1 158 ? 1.557  -3.094  7.690   0.42 26.18 ?  158 LYS   A CE   1 
ATOM   3475 C  CE   B LYS   A 1 158 ? 1.356  -3.039  7.571   0.28 26.30 ?  158 LYS   A CE   1 
ATOM   3476 C  CE   T LYS   A 1 158 ? 1.745  -2.883  7.561   0.30 26.80 ?  158 LYS   A CE   1 
ATOM   3477 N  NZ   A LYS   A 1 158 ? 1.806  -4.454  8.257   0.42 26.41 ?  158 LYS   A NZ   1 
ATOM   3478 N  NZ   B LYS   A 1 158 ? 1.788  -3.774  8.792   0.28 26.65 ?  158 LYS   A NZ   1 
ATOM   3479 N  NZ   T LYS   A 1 158 ? 2.076  -4.119  8.327   0.30 27.33 ?  158 LYS   A NZ   1 
ATOM   3480 H  H    A LYS   A 1 158 ? 5.518  0.668   4.633   0.42 24.15 ?  158 LYS   A H    1 
ATOM   3481 H  H    B LYS   A 1 158 ? 4.972  0.560   4.112   0.28 25.17 ?  158 LYS   A H    1 
ATOM   3482 H  H    T LYS   A 1 158 ? 5.650  0.796   4.449   0.30 23.06 ?  158 LYS   A H    1 
ATOM   3483 H  HA   A LYS   A 1 158 ? 5.169  -1.731  5.595   0.42 25.16 ?  158 LYS   A HA   1 
ATOM   3484 H  HA   B LYS   A 1 158 ? 4.661  -1.810  5.235   0.28 25.67 ?  158 LYS   A HA   1 
ATOM   3485 H  HA   T LYS   A 1 158 ? 5.258  -1.546  5.522   0.30 24.97 ?  158 LYS   A HA   1 
ATOM   3486 H  HB2  A LYS   A 1 158 ? 4.180  -0.063  6.757   0.42 27.00 ?  158 LYS   A HB2  1 
ATOM   3487 H  HB2  B LYS   A 1 158 ? 3.480  0.023   6.042   0.28 27.45 ?  158 LYS   A HB2  1 
ATOM   3488 H  HB2  T LYS   A 1 158 ? 4.324  0.196   6.615   0.30 27.08 ?  158 LYS   A HB2  1 
ATOM   3489 H  HB3  A LYS   A 1 158 ? 3.398  0.448   5.479   0.42 27.00 ?  158 LYS   A HB3  1 
ATOM   3490 H  HB3  B LYS   A 1 158 ? 2.715  0.155   4.659   0.28 27.45 ?  158 LYS   A HB3  1 
ATOM   3491 H  HB3  T LYS   A 1 158 ? 3.526  0.661   5.325   0.30 27.08 ?  158 LYS   A HB3  1 
ATOM   3492 H  HG2  A LYS   A 1 158 ? 1.934  -0.590  6.963   0.42 29.01 ?  158 LYS   A HG2  1 
ATOM   3493 H  HG2  B LYS   A 1 158 ? 1.268  -0.803  6.129   0.28 29.22 ?  158 LYS   A HG2  1 
ATOM   3494 H  HG2  T LYS   A 1 158 ? 2.072  -0.294  6.863   0.30 29.11 ?  158 LYS   A HG2  1 
ATOM   3495 H  HG3  A LYS   A 1 158 ? 1.963  -1.392  5.597   0.42 29.01 ?  158 LYS   A HG3  1 
ATOM   3496 H  HG3  B LYS   A 1 158 ? 1.694  -1.956  5.121   0.28 29.22 ?  158 LYS   A HG3  1 
ATOM   3497 H  HG3  T LYS   A 1 158 ? 2.092  -1.182  5.550   0.30 29.11 ?  158 LYS   A HG3  1 
ATOM   3498 H  HD2  A LYS   A 1 158 ? 3.271  -3.047  6.561   0.42 30.59 ?  158 LYS   A HD2  1 
ATOM   3499 H  HD2  B LYS   A 1 158 ? 3.184  -2.796  6.692   0.28 30.72 ?  158 LYS   A HD2  1 
ATOM   3500 H  HD2  T LYS   A 1 158 ? 3.561  -2.683  6.637   0.30 30.94 ?  158 LYS   A HD2  1 
ATOM   3501 H  HD3  A LYS   A 1 158 ? 3.388  -2.203  7.906   0.42 30.59 ?  158 LYS   A HD3  1 
ATOM   3502 H  HD3  B LYS   A 1 158 ? 2.814  -1.613  7.690   0.28 30.72 ?  158 LYS   A HD3  1 
ATOM   3503 H  HD3  T LYS   A 1 158 ? 3.440  -1.802  7.958   0.30 30.94 ?  158 LYS   A HD3  1 
ATOM   3504 H  HE2  A LYS   A 1 158 ? 1.182  -2.542  8.395   0.42 31.47 ?  158 LYS   A HE2  1 
ATOM   3505 H  HE2  B LYS   A 1 158 ? 0.617  -2.459  7.811   0.28 31.61 ?  158 LYS   A HE2  1 
ATOM   3506 H  HE2  T LYS   A 1 158 ? 1.182  -2.324  8.120   0.30 32.21 ?  158 LYS   A HE2  1 
ATOM   3507 H  HE3  A LYS   A 1 158 ? 0.917  -3.185  6.969   0.42 31.47 ?  158 LYS   A HE3  1 
ATOM   3508 H  HE3  B LYS   A 1 158 ? 1.070  -3.689  6.910   0.28 31.61 ?  158 LYS   A HE3  1 
ATOM   3509 H  HE3  T LYS   A 1 158 ? 1.260  -3.146  6.763   0.30 32.21 ?  158 LYS   A HE3  1 
ATOM   3510 H  HZ1  A LYS   A 1 158 ? 1.044  -4.803  8.557   0.42 31.74 ?  158 LYS   A HZ1  1 
ATOM   3511 H  HZ1  B LYS   A 1 158 ? 1.114  -4.259  9.110   0.28 32.03 ?  158 LYS   A HZ1  1 
ATOM   3512 H  HZ1  T LYS   A 1 158 ? 1.329  -4.551  8.547   0.30 32.85 ?  158 LYS   A HZ1  1 
ATOM   3513 H  HZ2  A LYS   A 1 158 ? 2.140  -4.988  7.628   0.42 31.74 ?  158 LYS   A HZ2  1 
ATOM   3514 H  HZ2  B LYS   A 1 158 ? 2.468  -4.314  8.597   0.28 32.03 ?  158 LYS   A HZ2  1 
ATOM   3515 H  HZ2  T LYS   A 1 158 ? 2.584  -4.657  7.831   0.30 32.85 ?  158 LYS   A HZ2  1 
ATOM   3516 H  HZ3  A LYS   A 1 158 ? 2.386  -4.402  8.930   0.42 31.74 ?  158 LYS   A HZ3  1 
ATOM   3517 H  HZ3  B LYS   A 1 158 ? 2.049  -3.196  9.417   0.28 32.03 ?  158 LYS   A HZ3  1 
ATOM   3518 H  HZ3  T LYS   A 1 158 ? 2.518  -3.908  9.070   0.30 32.85 ?  158 LYS   A HZ3  1 
ATOM   3519 N  N    A ASN   A 1 159 ? 3.549  -1.179  2.889   0.42 20.57 ?  159 ASN   A N    1 
ATOM   3520 N  N    B ASN   A 1 159 ? 3.257  -1.407  2.367   0.28 20.61 ?  159 ASN   A N    1 
ATOM   3521 N  N    T ASN   A 1 159 ? 3.611  -1.082  2.818   0.30 21.28 ?  159 ASN   A N    1 
ATOM   3522 C  CA   A ASN   A 1 159 ? 2.850  -1.875  1.815   0.42 20.68 ?  159 ASN   A CA   1 
ATOM   3523 C  CA   B ASN   A 1 159 ? 2.721  -2.146  1.230   0.28 20.97 ?  159 ASN   A CA   1 
ATOM   3524 C  CA   T ASN   A 1 159 ? 2.866  -1.778  1.776   0.30 21.67 ?  159 ASN   A CA   1 
ATOM   3525 C  C    A ASN   A 1 159 ? 3.727  -2.974  1.213   0.42 19.39 ?  159 ASN   A C    1 
ATOM   3526 C  C    B ASN   A 1 159 ? 3.754  -3.119  0.688   0.28 20.15 ?  159 ASN   A C    1 
ATOM   3527 C  C    T ASN   A 1 159 ? 3.692  -2.896  1.142   0.30 21.48 ?  159 ASN   A C    1 
ATOM   3528 O  O    A ASN   A 1 159 ? 3.265  -4.099  0.991   0.42 18.77 ?  159 ASN   A O    1 
ATOM   3529 O  O    B ASN   A 1 159 ? 3.417  -4.237  0.280   0.28 19.87 ?  159 ASN   A O    1 
ATOM   3530 O  O    T ASN   A 1 159 ? 3.156  -3.943  0.790   0.30 21.36 ?  159 ASN   A O    1 
ATOM   3531 C  CB   A ASN   A 1 159 ? 2.366  -0.866  0.768   0.42 22.11 ?  159 ASN   A CB   1 
ATOM   3532 C  CB   B ASN   A 1 159 ? 2.270  -1.171  0.143   0.28 22.33 ?  159 ASN   A CB   1 
ATOM   3533 C  CB   T ASN   A 1 159 ? 2.373  -0.794  0.711   0.30 22.45 ?  159 ASN   A CB   1 
ATOM   3534 C  CG   A ASN   A 1 159 ? 1.148  -0.078  1.237   0.42 23.89 ?  159 ASN   A CG   1 
ATOM   3535 C  CG   B ASN   A 1 159 ? 1.163  -0.253  0.614   0.28 23.65 ?  159 ASN   A CG   1 
ATOM   3536 C  CG   T ASN   A 1 159 ? 1.163  0.003   1.171   0.30 23.42 ?  159 ASN   A CG   1 
ATOM   3537 O  OD1  A ASN   A 1 159 ? 0.293  -0.611  1.940   0.42 24.64 ?  159 ASN   A OD1  1 
ATOM   3538 O  OD1  B ASN   A 1 159 ? 1.393  0.648   1.420   0.28 24.12 ?  159 ASN   A OD1  1 
ATOM   3539 O  OD1  T ASN   A 1 159 ? 0.340  -0.491  1.940   0.30 23.88 ?  159 ASN   A OD1  1 
ATOM   3540 N  ND2  A ASN   A 1 159 ? 1.068  1.193   0.849   0.42 24.45 ?  159 ASN   A ND2  1 
ATOM   3541 N  ND2  B ASN   A 1 159 ? -0.046 -0.476  0.114   0.28 24.16 ?  159 ASN   A ND2  1 
ATOM   3542 N  ND2  T ASN   A 1 159 ? 1.050  1.238   0.702   0.30 23.65 ?  159 ASN   A ND2  1 
ATOM   3543 H  H    A ASN   A 1 159 ? 3.678  -0.339  2.761   0.42 24.73 ?  159 ASN   A H    1 
ATOM   3544 H  H    B ASN   A 1 159 ? 3.259  -0.556  2.272   0.28 24.78 ?  159 ASN   A H    1 
ATOM   3545 H  H    T ASN   A 1 159 ? 3.747  -0.249  2.664   0.30 25.59 ?  159 ASN   A H    1 
ATOM   3546 H  HA   A ASN   A 1 159 ? 2.063  -2.301  2.189   0.42 24.87 ?  159 ASN   A HA   1 
ATOM   3547 H  HA   B ASN   A 1 159 ? 1.951  -2.660  1.511   0.28 25.22 ?  159 ASN   A HA   1 
ATOM   3548 H  HA   T ASN   A 1 159 ? 2.089  -2.193  2.178   0.30 26.06 ?  159 ASN   A HA   1 
ATOM   3549 H  HB2  A ASN   A 1 159 ? 3.071  -0.229  0.583   0.42 26.58 ?  159 ASN   A HB2  1 
ATOM   3550 H  HB2  B ASN   A 1 159 ? 3.022  -0.618  -0.124  0.28 26.85 ?  159 ASN   A HB2  1 
ATOM   3551 H  HB2  T ASN   A 1 159 ? 3.083  -0.169  0.504   0.30 26.98 ?  159 ASN   A HB2  1 
ATOM   3552 H  HB3  A ASN   A 1 159 ? 2.116  -1.337  -0.040  0.42 26.58 ?  159 ASN   A HB3  1 
ATOM   3553 H  HB3  B ASN   A 1 159 ? 1.938  -1.670  -0.620  0.28 26.85 ?  159 ASN   A HB3  1 
ATOM   3554 H  HB3  T ASN   A 1 159 ? 2.123  -1.291  -0.085  0.30 26.98 ?  159 ASN   A HB3  1 
ATOM   3555 H  HD21 A ASN   A 1 159 ? 0.398  1.677   1.092   0.42 29.38 ?  159 ASN   A HD21 1 
ATOM   3556 H  HD21 B ASN   A 1 159 ? -0.710 0.019   0.351   0.28 29.05 ?  159 ASN   A HD21 1 
ATOM   3557 H  HD21 T ASN   A 1 159 ? 0.382  1.724   0.936   0.30 28.43 ?  159 ASN   A HD21 1 
ATOM   3558 H  HD22 A ASN   A 1 159 ? 1.687  1.531   0.361   0.42 29.38 ?  159 ASN   A HD22 1 
ATOM   3559 H  HD22 B ASN   A 1 159 ? -0.168 -1.116  -0.447  0.28 29.05 ?  159 ASN   A HD22 1 
ATOM   3560 H  HD22 T ASN   A 1 159 ? 1.646  1.548   0.169   0.30 28.43 ?  159 ASN   A HD22 1 
ATOM   3561 N  N    A LEU   A 1 160 ? 5.009  -2.688  0.992   0.42 18.57 ?  160 LEU   A N    1 
ATOM   3562 N  N    B LEU   A 1 160 ? 5.022  -2.713  0.689   0.28 19.44 ?  160 LEU   A N    1 
ATOM   3563 N  N    T LEU   A 1 160 ? 4.995  -2.681  1.008   0.30 21.42 ?  160 LEU   A N    1 
ATOM   3564 C  CA   A LEU   A 1 160 ? 5.890  -3.711  0.437   0.42 17.68 ?  160 LEU   A CA   1 
ATOM   3565 C  CA   B LEU   A 1 160 ? 6.081  -3.632  0.302   0.28 18.81 ?  160 LEU   A CA   1 
ATOM   3566 C  CA   T LEU   A 1 160 ? 5.870  -3.711  0.458   0.30 21.18 ?  160 LEU   A CA   1 
ATOM   3567 C  C    A LEU   A 1 160 ? 6.097  -4.854  1.421   0.42 16.74 ?  160 LEU   A C    1 
ATOM   3568 C  C    B LEU   A 1 160 ? 6.216  -4.762  1.315   0.28 17.84 ?  160 LEU   A C    1 
ATOM   3569 O  O    A LEU   A 1 160 ? 6.125  -6.026  1.026   0.42 16.78 ?  160 LEU   A O    1 
ATOM   3570 O  O    B LEU   A 1 160 ? 6.242  -5.942  0.947   0.28 17.91 ?  160 LEU   A O    1 
ATOM   3571 C  CB   A LEU   A 1 160 ? 7.231  -3.097  0.048   0.42 17.70 ?  160 LEU   A CB   1 
ATOM   3572 C  CB   B LEU   A 1 160 ? 7.402  -2.874  0.166   0.28 19.23 ?  160 LEU   A CB   1 
ATOM   3573 C  CB   T LEU   A 1 160 ? 7.241  -3.133  0.116   0.30 20.88 ?  160 LEU   A CB   1 
ATOM   3574 C  CG   A LEU   A 1 160 ? 8.300  -4.116  -0.345  0.42 18.56 ?  160 LEU   A CG   1 
ATOM   3575 C  CG   B LEU   A 1 160 ? 8.524  -3.756  -0.369  0.28 19.94 ?  160 LEU   A CG   1 
ATOM   3576 C  CG   T LEU   A 1 160 ? 8.289  -4.158  -0.320  0.30 20.90 ?  160 LEU   A CG   1 
ATOM   3577 C  CD1  A LEU   A 1 160 ? 7.844  -4.917  -1.550  0.42 19.37 ?  160 LEU   A CD1  1 
ATOM   3578 C  CD1  B LEU   A 1 160 ? 8.023  -4.489  -1.596  0.28 20.15 ?  160 LEU   A CD1  1 
ATOM   3579 C  CD1  T LEU   A 1 160 ? 7.832  -4.899  -1.564  0.30 21.20 ?  160 LEU   A CD1  1 
ATOM   3580 C  CD2  A LEU   A 1 160 ? 9.618  -3.423  -0.618  0.42 18.62 ?  160 LEU   A CD2  1 
ATOM   3581 C  CD2  B LEU   A 1 160 ? 9.765  -2.937  -0.687  0.28 20.15 ?  160 LEU   A CD2  1 
ATOM   3582 C  CD2  T LEU   A 1 160 ? 9.626  -3.480  -0.558  0.30 20.68 ?  160 LEU   A CD2  1 
ATOM   3583 H  H    A LEU   A 1 160 ? 5.384  -1.938  1.174   0.42 22.33 ?  160 LEU   A H    1 
ATOM   3584 H  H    B LEU   A 1 160 ? 5.291  -1.924  0.897   0.28 23.38 ?  160 LEU   A H    1 
ATOM   3585 H  H    T LEU   A 1 160 ? 5.399  -1.954  1.228   0.30 25.75 ?  160 LEU   A H    1 
ATOM   3586 H  HA   A LEU   A 1 160 ? 5.479  -4.073  -0.362  0.42 21.27 ?  160 LEU   A HA   1 
ATOM   3587 H  HA   B LEU   A 1 160 ? 5.833  -4.006  -0.557  0.28 22.62 ?  160 LEU   A HA   1 
ATOM   3588 H  HB2  A LEU   A 1 160 ? 7.093  -2.500  -0.706  0.42 21.29 ?  160 LEU   A HB2  1 
ATOM   3589 H  HB2  B LEU   A 1 160 ? 7.292  -2.125  -0.444  0.28 23.13 ?  160 LEU   A HB2  1 
ATOM   3590 H  HB2  T LEU   A 1 160 ? 7.137  -2.492  -0.606  0.30 25.11 ?  160 LEU   A HB2  1 
ATOM   3591 H  HB3  A LEU   A 1 160 ? 7.569  -2.596  0.805   0.42 21.29 ?  160 LEU   A HB3  1 
ATOM   3592 H  HB3  B LEU   A 1 160 ? 7.675  -2.549  1.041   0.28 23.13 ?  160 LEU   A HB3  1 
ATOM   3593 H  HB3  T LEU   A 1 160 ? 7.589  -2.686  0.902   0.30 25.11 ?  160 LEU   A HB3  1 
ATOM   3594 H  HG   A LEU   A 1 160 ? 8.443  -4.732  0.390   0.42 22.32 ?  160 LEU   A HG   1 
ATOM   3595 H  HG   B LEU   A 1 160 ? 8.764  -4.414  0.303   0.28 23.98 ?  160 LEU   A HG   1 
ATOM   3596 H  HG   T LEU   A 1 160 ? 8.407  -4.808  0.391   0.30 25.12 ?  160 LEU   A HG   1 
ATOM   3597 H  HD11 A LEU   A 1 160 ? 8.572  -5.485  -1.840  0.42 23.30 ?  160 LEU   A HD11 1 
ATOM   3598 H  HD11 B LEU   A 1 160 ? 8.762  -4.945  -1.988  0.28 24.23 ?  160 LEU   A HD11 1 
ATOM   3599 H  HD11 T LEU   A 1 160 ? 8.548  -5.479  -1.864  0.30 25.48 ?  160 LEU   A HD11 1 
ATOM   3600 H  HD12 A LEU   A 1 160 ? 7.079  -5.458  -1.301  0.42 23.30 ?  160 LEU   A HD12 1 
ATOM   3601 H  HD12 B LEU   A 1 160 ? 7.358  -5.148  -1.339  0.28 24.23 ?  160 LEU   A HD12 1 
ATOM   3602 H  HD12 T LEU   A 1 160 ? 7.047  -5.425  -1.347  0.30 25.48 ?  160 LEU   A HD12 1 
ATOM   3603 H  HD13 A LEU   A 1 160 ? 7.598  -4.303  -2.260  0.42 23.30 ?  160 LEU   A HD13 1 
ATOM   3604 H  HD13 B LEU   A 1 160 ? 7.641  -3.849  -2.222  0.28 24.23 ?  160 LEU   A HD13 1 
ATOM   3605 H  HD13 T LEU   A 1 160 ? 7.618  -4.252  -2.254  0.30 25.48 ?  160 LEU   A HD13 1 
ATOM   3606 H  HD21 A LEU   A 1 160 ? 10.279 -4.089  -0.863  0.42 22.39 ?  160 LEU   A HD21 1 
ATOM   3607 H  HD21 B LEU   A 1 160 ? 10.506 -3.539  -0.864  0.28 24.23 ?  160 LEU   A HD21 1 
ATOM   3608 H  HD21 T LEU   A 1 160 ? 10.274 -4.147  -0.831  0.30 24.86 ?  160 LEU   A HD21 1 
ATOM   3609 H  HD22 A LEU   A 1 160 ? 9.500  -2.791  -1.345  0.42 22.39 ?  160 LEU   A HD22 1 
ATOM   3610 H  HD22 B LEU   A 1 160 ? 9.591  -2.388  -1.467  0.28 24.23 ?  160 LEU   A HD22 1 
ATOM   3611 H  HD22 T LEU   A 1 160 ? 9.521  -2.814  -1.256  0.30 24.86 ?  160 LEU   A HD22 1 
ATOM   3612 H  HD23 A LEU   A 1 160 ? 9.903  -2.954  0.183   0.42 22.39 ?  160 LEU   A HD23 1 
ATOM   3613 H  HD23 B LEU   A 1 160 ? 9.973  -2.374  0.075   0.28 24.23 ?  160 LEU   A HD23 1 
ATOM   3614 H  HD23 T LEU   A 1 160 ? 9.915  -3.054  0.264   0.30 24.86 ?  160 LEU   A HD23 1 
ATOM   3615 N  N    A TYR   A 1 161 ? 6.264  -4.532  2.703   0.72 17.29 ?  161 TYR   A N    1 
ATOM   3616 N  N    B TYR   A 1 161 ? 6.310  -4.413  2.600   0.28 17.34 ?  161 TYR   A N    1 
ATOM   3617 C  CA   A TYR   A 1 161 ? 6.390  -5.569  3.719   0.72 17.03 ?  161 TYR   A CA   1 
ATOM   3618 C  CA   B TYR   A 1 161 ? 6.434  -5.424  3.646   0.28 16.92 ?  161 TYR   A CA   1 
ATOM   3619 C  C    A TYR   A 1 161 ? 5.234  -6.557  3.643   0.72 17.44 ?  161 TYR   A C    1 
ATOM   3620 C  C    B TYR   A 1 161 ? 5.275  -6.416  3.620   0.28 17.40 ?  161 TYR   A C    1 
ATOM   3621 O  O    A TYR   A 1 161 ? 5.443  -7.771  3.553   0.72 16.95 ?  161 TYR   A O    1 
ATOM   3622 O  O    B TYR   A 1 161 ? 5.438  -7.569  4.036   0.28 17.10 ?  161 TYR   A O    1 
ATOM   3623 C  CB   A TYR   A 1 161 ? 6.453  -4.935  5.107   0.72 16.64 ?  161 TYR   A CB   1 
ATOM   3624 C  CB   B TYR   A 1 161 ? 6.539  -4.736  5.012   0.28 16.30 ?  161 TYR   A CB   1 
ATOM   3625 C  CG   A TYR   A 1 161 ? 6.366  -5.954  6.206   0.72 16.12 ?  161 TYR   A CG   1 
ATOM   3626 C  CG   B TYR   A 1 161 ? 6.429  -5.661  6.207   0.28 15.65 ?  161 TYR   A CG   1 
ATOM   3627 C  CD1  A TYR   A 1 161 ? 7.484  -6.670  6.597   0.72 16.03 ?  161 TYR   A CD1  1 
ATOM   3628 C  CD1  B TYR   A 1 161 ? 7.553  -6.284  6.740   0.28 15.59 ?  161 TYR   A CD1  1 
ATOM   3629 C  CD2  A TYR   A 1 161 ? 5.158  -6.219  6.843   0.72 15.96 ?  161 TYR   A CD2  1 
ATOM   3630 C  CD2  B TYR   A 1 161 ? 5.202  -5.898  6.813   0.28 15.58 ?  161 TYR   A CD2  1 
ATOM   3631 C  CE1  A TYR   A 1 161 ? 7.411  -7.615  7.587   0.72 15.70 ?  161 TYR   A CE1  1 
ATOM   3632 C  CE1  B TYR   A 1 161 ? 7.453  -7.127  7.835   0.28 15.78 ?  161 TYR   A CE1  1 
ATOM   3633 C  CE2  A TYR   A 1 161 ? 5.076  -7.168  7.839   0.72 15.77 ?  161 TYR   A CE2  1 
ATOM   3634 C  CE2  B TYR   A 1 161 ? 5.092  -6.738  7.905   0.28 15.96 ?  161 TYR   A CE2  1 
ATOM   3635 C  CZ   A TYR   A 1 161 ? 6.209  -7.861  8.205   0.72 15.63 ?  161 TYR   A CZ   1 
ATOM   3636 C  CZ   B TYR   A 1 161 ? 6.219  -7.350  8.413   0.28 16.26 ?  161 TYR   A CZ   1 
ATOM   3637 O  OH   A TYR   A 1 161 ? 6.150  -8.805  9.197   0.72 16.31 ?  161 TYR   A OH   1 
ATOM   3638 O  OH   B TYR   A 1 161 ? 6.108  -8.186  9.502   0.28 17.32 ?  161 TYR   A OH   1 
ATOM   3639 H  H    A TYR   A 1 161 ? 6.298  -3.733  3.008   0.72 20.79 ?  161 TYR   A H    1 
ATOM   3640 H  H    B TYR   A 1 161 ? 6.312  -3.601  2.882   0.28 20.85 ?  161 TYR   A H    1 
ATOM   3641 H  HA   A TYR   A 1 161 ? 7.206  -6.066  3.574   0.72 20.49 ?  161 TYR   A HA   1 
ATOM   3642 H  HA   B TYR   A 1 161 ? 7.253  -5.920  3.501   0.28 20.35 ?  161 TYR   A HA   1 
ATOM   3643 H  HB2  A TYR   A 1 161 ? 7.297  -4.468  5.199   0.72 20.02 ?  161 TYR   A HB2  1 
ATOM   3644 H  HB2  B TYR   A 1 161 ? 7.400  -4.290  5.066   0.28 19.61 ?  161 TYR   A HB2  1 
ATOM   3645 H  HB3  A TYR   A 1 161 ? 5.714  -4.317  5.210   0.72 20.02 ?  161 TYR   A HB3  1 
ATOM   3646 H  HB3  B TYR   A 1 161 ? 5.829  -4.080  5.082   0.28 19.61 ?  161 TYR   A HB3  1 
ATOM   3647 H  HD1  A TYR   A 1 161 ? 8.297  -6.513  6.178   0.72 19.28 ?  161 TYR   A HD1  1 
ATOM   3648 H  HD1  B TYR   A 1 161 ? 8.386  -6.136  6.353   0.28 18.76 ?  161 TYR   A HD1  1 
ATOM   3649 H  HD2  A TYR   A 1 161 ? 4.389  -5.755  6.593   0.72 19.20 ?  161 TYR   A HD2  1 
ATOM   3650 H  HD2  B TYR   A 1 161 ? 4.437  -5.490  6.474   0.28 18.75 ?  161 TYR   A HD2  1 
ATOM   3651 H  HE1  A TYR   A 1 161 ? 8.168  -8.092  7.840   0.72 18.89 ?  161 TYR   A HE1  1 
ATOM   3652 H  HE1  B TYR   A 1 161 ? 8.213  -7.538  8.182   0.28 18.98 ?  161 TYR   A HE1  1 
ATOM   3653 H  HE2  A TYR   A 1 161 ? 4.255  -7.339  8.261   0.72 18.97 ?  161 TYR   A HE2  1 
ATOM   3654 H  HE2  B TYR   A 1 161 ? 4.261  -6.887  8.298   0.28 19.20 ?  161 TYR   A HE2  1 
ATOM   3655 H  HH   A TYR   A 1 161 ? 6.900  -9.155  9.318   0.72 19.62 ?  161 TYR   A HH   1 
ATOM   3656 H  HH   B TYR   A 1 161 ? 6.861  -8.487  9.713   0.28 20.83 ?  161 TYR   A HH   1 
ATOM   3657 N  N    A ASP   A 1 162 ? 3.999  -6.048  3.693   0.72 18.10 ?  162 ASP   A N    1 
ATOM   3658 N  N    B ASP   A 1 162 ? 4.104  -5.998  3.130   0.28 17.93 ?  162 ASP   A N    1 
ATOM   3659 C  CA   A ASP   A 1 162 ? 2.835  -6.925  3.605   0.72 19.17 ?  162 ASP   A CA   1 
ATOM   3660 C  CA   B ASP   A 1 162 ? 2.939  -6.878  3.134   0.28 19.23 ?  162 ASP   A CA   1 
ATOM   3661 C  C    A ASP   A 1 162 ? 2.876  -7.756  2.331   0.72 19.38 ?  162 ASP   A C    1 
ATOM   3662 C  C    B ASP   A 1 162 ? 2.983  -7.900  2.000   0.28 19.19 ?  162 ASP   A C    1 
ATOM   3663 O  O    A ASP   A 1 162 ? 2.502  -8.936  2.337   0.72 20.23 ?  162 ASP   A O    1 
ATOM   3664 O  O    B ASP   A 1 162 ? 2.675  -9.078  2.215   0.28 19.56 ?  162 ASP   A O    1 
ATOM   3665 C  CB   A ASP   A 1 162 ? 1.539  -6.109  3.660   0.72 20.12 ?  162 ASP   A CB   1 
ATOM   3666 C  CB   B ASP   A 1 162 ? 1.652  -6.052  3.087   0.28 20.70 ?  162 ASP   A CB   1 
ATOM   3667 C  CG   A ASP   A 1 162 ? 1.260  -5.527  5.029   0.72 21.47 ?  162 ASP   A CG   1 
ATOM   3668 C  CG   B ASP   A 1 162 ? 1.260  -5.500  4.447   0.28 22.02 ?  162 ASP   A CG   1 
ATOM   3669 O  OD1  A ASP   A 1 162 ? 1.894  -5.955  6.010   0.72 22.09 ?  162 ASP   A OD1  1 
ATOM   3670 O  OD1  B ASP   A 1 162 ? 2.158  -5.091  5.211   0.28 22.83 ?  162 ASP   A OD1  1 
ATOM   3671 O  OD2  A ASP   A 1 162 ? 0.378  -4.646  5.118   0.72 22.77 -1 162 ASP   A OD2  1 
ATOM   3672 O  OD2  B ASP   A 1 162 ? 0.048  -5.459  4.748   0.28 22.22 -1 162 ASP   A OD2  1 
ATOM   3673 H  H    A ASP   A 1 162 ? 3.808  -5.216  3.781   0.72 21.77 ?  162 ASP   A H    1 
ATOM   3674 H  H    B ASP   A 1 162 ? 3.963  -5.215  2.802   0.28 21.57 ?  162 ASP   A H    1 
ATOM   3675 H  HA   A ASP   A 1 162 ? 2.828  -7.539  4.355   0.72 23.06 ?  162 ASP   A HA   1 
ATOM   3676 H  HA   B ASP   A 1 162 ? 2.938  -7.371  3.963   0.28 23.13 ?  162 ASP   A HA   1 
ATOM   3677 H  HB2  A ASP   A 1 162 ? 1.592  -5.372  3.039   0.72 24.20 ?  162 ASP   A HB2  1 
ATOM   3678 H  HB2  B ASP   A 1 162 ? 1.780  -5.301  2.490   0.28 24.89 ?  162 ASP   A HB2  1 
ATOM   3679 H  HB3  A ASP   A 1 162 ? 0.785  -6.681  3.437   0.72 24.20 ?  162 ASP   A HB3  1 
ATOM   3680 H  HB3  B ASP   A 1 162 ? 0.931  -6.616  2.770   0.28 24.89 ?  162 ASP   A HB3  1 
ATOM   3681 N  N    A LYS   A 1 163 ? 3.328  -7.156  1.227   0.72 20.32 ?  163 LYS   A N    1 
ATOM   3682 N  N    B LYS   A 1 163 ? 3.352  -7.474  0.788   0.28 19.18 ?  163 LYS   A N    1 
ATOM   3683 C  CA   A LYS   A 1 163 ? 3.415  -7.904  -0.024  0.72 20.80 ?  163 LYS   A CA   1 
ATOM   3684 C  CA   B LYS   A 1 163 ? 3.526  -8.423  -0.308  0.28 19.17 ?  163 LYS   A CA   1 
ATOM   3685 C  C    A LYS   A 1 163 ? 4.486  -8.988  0.046   0.72 20.07 ?  163 LYS   A C    1 
ATOM   3686 C  C    B LYS   A 1 163 ? 4.677  -9.377  -0.016  0.28 18.40 ?  163 LYS   A C    1 
ATOM   3687 O  O    A LYS   A 1 163 ? 4.312  -10.072 -0.519  0.72 20.17 ?  163 LYS   A O    1 
ATOM   3688 O  O    B LYS   A 1 163 ? 4.590  -10.579 -0.294  0.28 18.65 ?  163 LYS   A O    1 
ATOM   3689 C  CB   A LYS   A 1 163 ? 3.680  -6.957  -1.195  0.72 22.57 ?  163 LYS   A CB   1 
ATOM   3690 C  CB   B LYS   A 1 163 ? 3.771  -7.656  -1.609  0.28 20.42 ?  163 LYS   A CB   1 
ATOM   3691 C  CG   A LYS   A 1 163 ? 3.728  -7.664  -2.541  0.72 25.09 ?  163 LYS   A CG   1 
ATOM   3692 C  CG   B LYS   A 1 163 ? 3.644  -8.480  -2.885  0.28 21.82 ?  163 LYS   A CG   1 
ATOM   3693 C  CD   A LYS   A 1 163 ? 4.187  -6.738  -3.649  0.72 27.58 ?  163 LYS   A CD   1 
ATOM   3694 C  CD   B LYS   A 1 163 ? 3.540  -7.562  -4.102  0.28 23.19 ?  163 LYS   A CD   1 
ATOM   3695 C  CE   A LYS   A 1 163 ? 4.106  -7.424  -5.004  0.72 29.54 ?  163 LYS   A CE   1 
ATOM   3696 C  CE   B LYS   A 1 163 ? 2.861  -8.245  -5.281  0.28 24.27 ?  163 LYS   A CE   1 
ATOM   3697 N  NZ   A LYS   A 1 163 ? 4.754  -6.625  -6.080  0.72 30.66 ?  163 LYS   A NZ   1 
ATOM   3698 N  NZ   B LYS   A 1 163 ? 3.796  -9.044  -6.117  0.28 24.91 ?  163 LYS   A NZ   1 
ATOM   3699 H  H    A LYS   A 1 163 ? 3.581  -6.329  1.179   0.72 24.43 ?  163 LYS   A H    1 
ATOM   3700 H  H    B LYS   A 1 163 ? 3.507  -6.654  0.579   0.28 23.07 ?  163 LYS   A H    1 
ATOM   3701 H  HA   A LYS   A 1 163 ? 2.562  -8.333  -0.184  0.72 25.01 ?  163 LYS   A HA   1 
ATOM   3702 H  HA   B LYS   A 1 163 ? 2.716  -8.945  -0.413  0.28 23.05 ?  163 LYS   A HA   1 
ATOM   3703 H  HB2  A LYS   A 1 163 ? 2.970  -6.293  -1.236  0.72 27.13 ?  163 LYS   A HB2  1 
ATOM   3704 H  HB2  B LYS   A 1 163 ? 3.126  -6.933  -1.665  0.28 24.55 ?  163 LYS   A HB2  1 
ATOM   3705 H  HB3  A LYS   A 1 163 ? 4.532  -6.517  -1.061  0.72 27.13 ?  163 LYS   A HB3  1 
ATOM   3706 H  HB3  B LYS   A 1 163 ? 4.668  -7.289  -1.590  0.28 24.55 ?  163 LYS   A HB3  1 
ATOM   3707 H  HG2  A LYS   A 1 163 ? 4.350  -8.407  -2.497  0.72 30.16 ?  163 LYS   A HG2  1 
ATOM   3708 H  HG2  B LYS   A 1 163 ? 4.430  -9.040  -2.992  0.28 26.24 ?  163 LYS   A HG2  1 
ATOM   3709 H  HG3  A LYS   A 1 163 ? 2.840  -7.988  -2.763  0.72 30.16 ?  163 LYS   A HG3  1 
ATOM   3710 H  HG3  B LYS   A 1 163 ? 2.843  -9.025  -2.842  0.28 26.24 ?  163 LYS   A HG3  1 
ATOM   3711 H  HD2  A LYS   A 1 163 ? 3.616  -5.954  -3.669  0.72 33.14 ?  163 LYS   A HD2  1 
ATOM   3712 H  HD2  B LYS   A 1 163 ? 3.018  -6.779  -3.868  0.28 27.87 ?  163 LYS   A HD2  1 
ATOM   3713 H  HD3  A LYS   A 1 163 ? 5.109  -6.480  -3.490  0.72 33.14 ?  163 LYS   A HD3  1 
ATOM   3714 H  HD3  B LYS   A 1 163 ? 4.432  -7.294  -4.379  0.28 27.87 ?  163 LYS   A HD3  1 
ATOM   3715 H  HE2  A LYS   A 1 163 ? 4.546  -8.286  -4.951  0.72 35.49 ?  163 LYS   A HE2  1 
ATOM   3716 H  HE2  B LYS   A 1 163 ? 2.174  -8.843  -4.946  0.28 29.17 ?  163 LYS   A HE2  1 
ATOM   3717 H  HE3  A LYS   A 1 163 ? 3.174  -7.544  -5.240  0.72 35.49 ?  163 LYS   A HE3  1 
ATOM   3718 H  HE3  B LYS   A 1 163 ? 2.460  -7.567  -5.845  0.28 29.17 ?  163 LYS   A HE3  1 
ATOM   3719 H  HZ1  A LYS   A 1 163 ? 4.690  -7.054  -6.857  0.72 36.84 ?  163 LYS   A HZ1  1 
ATOM   3720 H  HZ1  B LYS   A 1 163 ? 3.351  -9.423  -6.790  0.28 29.94 ?  163 LYS   A HZ1  1 
ATOM   3721 H  HZ2  A LYS   A 1 163 ? 4.354  -5.833  -6.152  0.72 36.84 ?  163 LYS   A HZ2  1 
ATOM   3722 H  HZ2  B LYS   A 1 163 ? 4.431  -8.517  -6.451  0.28 29.94 ?  163 LYS   A HZ2  1 
ATOM   3723 H  HZ3  A LYS   A 1 163 ? 5.614  -6.498  -5.890  0.72 36.84 ?  163 LYS   A HZ3  1 
ATOM   3724 H  HZ3  B LYS   A 1 163 ? 4.175  -9.681  -5.627  0.28 29.94 ?  163 LYS   A HZ3  1 
ATOM   3725 N  N    A LEU   A 1 164 ? 5.610  -8.713  0.713   0.72 18.53 ?  164 LEU   A N    1 
ATOM   3726 N  N    B LEU   A 1 164 ? 5.763  -8.850  0.554   0.28 17.46 ?  164 LEU   A N    1 
ATOM   3727 C  CA   A LEU   A 1 164 ? 6.679  -9.709  0.786   0.72 17.70 ?  164 LEU   A CA   1 
ATOM   3728 C  CA   B LEU   A 1 164 ? 6.888  -9.684  0.967   0.28 16.63 ?  164 LEU   A CA   1 
ATOM   3729 C  C    A LEU   A 1 164 ? 6.256  -10.910 1.621   0.72 17.82 ?  164 LEU   A C    1 
ATOM   3730 C  C    B LEU   A 1 164 ? 6.428  -10.781 1.915   0.28 16.70 ?  164 LEU   A C    1 
ATOM   3731 O  O    A LEU   A 1 164 ? 6.563  -12.057 1.278   0.72 17.90 ?  164 LEU   A O    1 
ATOM   3732 O  O    B LEU   A 1 164 ? 6.739  -11.961 1.717   0.28 16.75 ?  164 LEU   A O    1 
ATOM   3733 C  CB   A LEU   A 1 164 ? 7.937  -9.083  1.380   0.72 17.05 ?  164 LEU   A CB   1 
ATOM   3734 C  CB   B LEU   A 1 164 ? 7.941  -8.812  1.655   0.28 15.94 ?  164 LEU   A CB   1 
ATOM   3735 C  CG   A LEU   A 1 164 ? 8.665  -8.083  0.483   0.72 16.87 ?  164 LEU   A CG   1 
ATOM   3736 C  CG   B LEU   A 1 164 ? 8.810  -7.889  0.797   0.28 15.75 ?  164 LEU   A CG   1 
ATOM   3737 C  CD1  A LEU   A 1 164 ? 9.612  -7.212  1.295   0.72 16.52 ?  164 LEU   A CD1  1 
ATOM   3738 C  CD1  B LEU   A 1 164 ? 9.594  -6.926  1.682   0.28 15.76 ?  164 LEU   A CD1  1 
ATOM   3739 C  CD2  A LEU   A 1 164 ? 9.425  -8.806  -0.612  0.72 16.84 ?  164 LEU   A CD2  1 
ATOM   3740 C  CD2  B LEU   A 1 164 ? 9.755  -8.694  -0.082  0.28 15.37 ?  164 LEU   A CD2  1 
ATOM   3741 H  H    A LEU   A 1 164 ? 5.777  -7.971  1.125   0.72 22.28 ?  164 LEU   A H    1 
ATOM   3742 H  H    B LEU   A 1 164 ? 5.867  -8.019  0.717   0.28 21.00 ?  164 LEU   A H    1 
ATOM   3743 H  HA   A LEU   A 1 164 ? 6.883  -10.018 -0.108  0.72 21.29 ?  164 LEU   A HA   1 
ATOM   3744 H  HA   B LEU   A 1 164 ? 7.291  -10.102 0.190   0.28 20.00 ?  164 LEU   A HA   1 
ATOM   3745 H  HB2  A LEU   A 1 164 ? 7.694  -8.619  2.193   0.72 20.50 ?  164 LEU   A HB2  1 
ATOM   3746 H  HB2  B LEU   A 1 164 ? 7.481  -8.243  2.293   0.28 19.18 ?  164 LEU   A HB2  1 
ATOM   3747 H  HB3  A LEU   A 1 164 ? 8.562  -9.795  1.585   0.72 20.50 ?  164 LEU   A HB3  1 
ATOM   3748 H  HB3  B LEU   A 1 164 ? 8.546  -9.397  2.132   0.28 19.18 ?  164 LEU   A HB3  1 
ATOM   3749 H  HG   A LEU   A 1 164 ? 8.014  -7.501  0.064   0.72 20.29 ?  164 LEU   A HG   1 
ATOM   3750 H  HG   B LEU   A 1 164 ? 8.238  -7.361  0.220   0.28 18.95 ?  164 LEU   A HG   1 
ATOM   3751 H  HD11 A LEU   A 1 164 ? 10.061 -6.593  0.701   0.72 19.88 ?  164 LEU   A HD11 1 
ATOM   3752 H  HD11 B LEU   A 1 164 ? 10.213 -6.422  1.132   0.28 18.96 ?  164 LEU   A HD11 1 
ATOM   3753 H  HD12 A LEU   A 1 164 ? 9.098  -6.721  1.958   0.72 19.88 ?  164 LEU   A HD12 1 
ATOM   3754 H  HD12 B LEU   A 1 164 ? 8.974  -6.320  2.120   0.28 18.96 ?  164 LEU   A HD12 1 
ATOM   3755 H  HD13 A LEU   A 1 164 ? 10.262 -7.780  1.738   0.72 19.88 ?  164 LEU   A HD13 1 
ATOM   3756 H  HD13 B LEU   A 1 164 ? 10.083 -7.435  2.348   0.28 18.96 ?  164 LEU   A HD13 1 
ATOM   3757 H  HD21 A LEU   A 1 164 ? 9.902  -8.151  -1.149  0.72 20.26 ?  164 LEU   A HD21 1 
ATOM   3758 H  HD21 B LEU   A 1 164 ? 10.312 -8.081  -0.589  0.28 18.50 ?  164 LEU   A HD21 1 
ATOM   3759 H  HD22 A LEU   A 1 164 ? 10.053 -9.423  -0.208  0.72 20.26 ?  164 LEU   A HD22 1 
ATOM   3760 H  HD22 B LEU   A 1 164 ? 10.311 -9.255  0.482   0.28 18.50 ?  164 LEU   A HD22 1 
ATOM   3761 H  HD23 A LEU   A 1 164 ? 8.793  -9.289  -1.167  0.72 20.26 ?  164 LEU   A HD23 1 
ATOM   3762 H  HD23 B LEU   A 1 164 ? 9.233  -9.243  -0.686  0.28 18.50 ?  164 LEU   A HD23 1 
ATOM   3763 N  N    A VAL   A 1 165 ? 5.562  -10.658 2.728   0.72 17.24 ?  165 VAL   A N    1 
ATOM   3764 N  N    B VAL   A 1 165 ? 5.693  -10.408 2.963   0.28 16.58 ?  165 VAL   A N    1 
ATOM   3765 C  CA   A VAL   A 1 165 ? 5.099  -11.735 3.594   0.72 16.78 ?  165 VAL   A CA   1 
ATOM   3766 C  CA   B VAL   A 1 165 ? 5.208  -11.409 3.907   0.28 16.88 ?  165 VAL   A CA   1 
ATOM   3767 C  C    A VAL   A 1 165 ? 4.079  -12.600 2.866   0.72 16.93 ?  165 VAL   A C    1 
ATOM   3768 C  C    B VAL   A 1 165 ? 4.092  -12.237 3.282   0.28 16.71 ?  165 VAL   A C    1 
ATOM   3769 O  O    A VAL   A 1 165 ? 4.193  -13.830 2.825   0.72 16.74 ?  165 VAL   A O    1 
ATOM   3770 O  O    B VAL   A 1 165 ? 4.107  -13.472 3.342   0.28 16.61 ?  165 VAL   A O    1 
ATOM   3771 C  CB   A VAL   A 1 165 ? 4.515  -11.134 4.888   0.72 16.91 ?  165 VAL   A CB   1 
ATOM   3772 C  CB   B VAL   A 1 165 ? 4.775  -10.752 5.230   0.28 17.25 ?  165 VAL   A CB   1 
ATOM   3773 C  CG1  A VAL   A 1 165 ? 3.781  -12.191 5.703   0.72 17.20 ?  165 VAL   A CG1  1 
ATOM   3774 C  CG1  B VAL   A 1 165 ? 4.009  -11.751 6.087   0.28 17.57 ?  165 VAL   A CG1  1 
ATOM   3775 C  CG2  A VAL   A 1 165 ? 5.611  -10.461 5.711   0.72 16.99 ?  165 VAL   A CG2  1 
ATOM   3776 C  CG2  B VAL   A 1 165 ? 5.993  -10.236 5.981   0.28 17.49 ?  165 VAL   A CG2  1 
ATOM   3777 H  H    A VAL   A 1 165 ? 5.337  -9.878  2.994   0.72 20.74 ?  165 VAL   A H    1 
ATOM   3778 H  H    B VAL   A 1 165 ? 5.471  -9.593  3.148   0.28 19.94 ?  165 VAL   A H    1 
ATOM   3779 H  HA   A VAL   A 1 165 ? 5.849  -12.300 3.840   0.72 20.19 ?  165 VAL   A HA   1 
ATOM   3780 H  HA   B VAL   A 1 165 ? 5.937  -12.009 4.116   0.28 20.31 ?  165 VAL   A HA   1 
ATOM   3781 H  HB   A VAL   A 1 165 ? 3.869  -10.454 4.649   0.72 20.34 ?  165 VAL   A HB   1 
ATOM   3782 H  HB   B VAL   A 1 165 ? 4.191  -9.998  5.047   0.28 20.75 ?  165 VAL   A HB   1 
ATOM   3783 H  HG11 A VAL   A 1 165 ? 3.657  -11.859 6.608   0.72 20.69 ?  165 VAL   A HG11 1 
ATOM   3784 H  HG11 B VAL   A 1 165 ? 3.991  -11.434 7.004   0.28 21.13 ?  165 VAL   A HG11 1 
ATOM   3785 H  HG12 A VAL   A 1 165 ? 2.915  -12.360 5.297   0.72 20.69 ?  165 VAL   A HG12 1 
ATOM   3786 H  HG12 B VAL   A 1 165 ? 3.102  -11.832 5.751   0.28 21.13 ?  165 VAL   A HG12 1 
ATOM   3787 H  HG13 A VAL   A 1 165 ? 4.308  -13.002 5.719   0.72 20.69 ?  165 VAL   A HG13 1 
ATOM   3788 H  HG13 B VAL   A 1 165 ? 4.457  -12.611 6.046   0.28 21.13 ?  165 VAL   A HG13 1 
ATOM   3789 H  HG21 A VAL   A 1 165 ? 5.223  -10.095 6.522   0.72 20.44 ?  165 VAL   A HG21 1 
ATOM   3790 H  HG21 B VAL   A 1 165 ? 5.704  -9.822  6.809   0.28 21.03 ?  165 VAL   A HG21 1 
ATOM   3791 H  HG22 A VAL   A 1 165 ? 6.291  -11.115 5.935   0.72 20.44 ?  165 VAL   A HG22 1 
ATOM   3792 H  HG22 B VAL   A 1 165 ? 6.583  -10.983 6.172   0.28 21.03 ?  165 VAL   A HG22 1 
ATOM   3793 H  HG23 A VAL   A 1 165 ? 6.005  -9.744  5.183   0.72 20.44 ?  165 VAL   A HG23 1 
ATOM   3794 H  HG23 B VAL   A 1 165 ? 6.451  -9.586  5.427   0.28 21.03 ?  165 VAL   A HG23 1 
ATOM   3795 N  N    A SER   A 1 166 ? 3.063  -11.963 2.281   0.72 17.66 ?  166 SER   A N    1 
ATOM   3796 N  N    B SER   A 1 166 ? 3.109  -11.574 2.664   0.28 16.61 ?  166 SER   A N    1 
ATOM   3797 C  CA   A SER   A 1 166 ? 1.946  -12.696 1.697   0.72 18.81 ?  166 SER   A CA   1 
ATOM   3798 C  CA   B SER   A 1 166 ? 1.941  -12.306 2.185   0.28 16.61 ?  166 SER   A CA   1 
ATOM   3799 C  C    A SER   A 1 166 ? 2.383  -13.520 0.502   0.72 19.52 ?  166 SER   A C    1 
ATOM   3800 C  C    B SER   A 1 166 ? 2.310  -13.346 1.134   0.28 17.27 ?  166 SER   A C    1 
ATOM   3801 O  O    A SER   A 1 166 ? 1.779  -14.564 0.219   0.72 21.13 ?  166 SER   A O    1 
ATOM   3802 O  O    B SER   A 1 166 ? 1.651  -14.388 1.042   0.28 17.72 ?  166 SER   A O    1 
ATOM   3803 C  CB   A SER   A 1 166 ? 0.846  -11.722 1.264   0.72 20.26 ?  166 SER   A CB   1 
ATOM   3804 C  CB   B SER   A 1 166 ? 0.866  -11.349 1.659   0.28 16.32 ?  166 SER   A CB   1 
ATOM   3805 O  OG   A SER   A 1 166 ? 0.276  -11.033 2.369   0.72 21.94 ?  166 SER   A OG   1 
ATOM   3806 O  OG   B SER   A 1 166 ? 1.170  -10.888 0.356   0.28 16.44 ?  166 SER   A OG   1 
ATOM   3807 H  H    A SER   A 1 166 ? 2.993  -11.121 2.218   0.72 21.24 ?  166 SER   A H    1 
ATOM   3808 H  H    B SER   A 1 166 ? 3.090  -10.722 2.524   0.28 19.98 ?  166 SER   A H    1 
ATOM   3809 H  HA   A SER   A 1 166 ? 1.566  -13.308 2.353   0.72 22.62 ?  166 SER   A HA   1 
ATOM   3810 H  HA   B SER   A 1 166 ? 1.552  -12.782 2.932   0.28 19.97 ?  166 SER   A HA   1 
ATOM   3811 H  HB2  A SER   A 1 166 ? 1.229  -11.076 0.652   0.72 24.35 ?  166 SER   A HB2  1 
ATOM   3812 H  HB2  B SER   A 1 166 ? 0.011  -11.818 1.637   0.28 19.63 ?  166 SER   A HB2  1 
ATOM   3813 H  HB3  A SER   A 1 166 ? 0.141  -12.219 0.815   0.72 24.35 ?  166 SER   A HB3  1 
ATOM   3814 H  HB3  B SER   A 1 166 ? 0.798  -10.587 2.258   0.28 19.63 ?  166 SER   A HB3  1 
ATOM   3815 H  HG   A SER   A 1 166 ? 0.880  -10.595 2.766   0.72 26.38 ?  166 SER   A HG   1 
ATOM   3816 H  HG   B SER   A 1 166 ? 0.565  -10.368 0.088   0.28 19.78 ?  166 SER   A HG   1 
ATOM   3817 N  N    A SER   A 1 167 ? 3.413  -13.070 -0.213  0.72 18.55 ?  167 SER   A N    1 
ATOM   3818 N  N    B SER   A 1 167 ? 3.359  -13.106 0.352   0.28 18.42 ?  167 SER   A N    1 
ATOM   3819 C  CA   A SER   A 1 167 ? 3.917  -13.787 -1.370  0.72 19.27 ?  167 SER   A CA   1 
ATOM   3820 C  CA   B SER   A 1 167 ? 3.773  -14.034 -0.699  0.28 19.30 ?  167 SER   A CA   1 
ATOM   3821 C  C    A SER   A 1 167 ? 5.068  -14.714 -1.025  0.72 19.05 ?  167 SER   A C    1 
ATOM   3822 C  C    B SER   A 1 167 ? 5.177  -14.535 -0.367  0.28 19.37 ?  167 SER   A C    1 
ATOM   3823 O  O    A SER   A 1 167 ? 5.560  -15.417 -1.912  0.72 19.62 ?  167 SER   A O    1 
ATOM   3824 O  O    B SER   A 1 167 ? 6.175  -13.949 -0.793  0.28 20.60 ?  167 SER   A O    1 
ATOM   3825 C  CB   A SER   A 1 167 ? 4.356  -12.798 -2.459  0.72 20.05 ?  167 SER   A CB   1 
ATOM   3826 C  CB   B SER   A 1 167 ? 3.708  -13.372 -2.079  0.28 20.37 ?  167 SER   A CB   1 
ATOM   3827 O  OG   A SER   A 1 167 ? 5.413  -11.969 -1.993  0.72 19.89 ?  167 SER   A OG   1 
ATOM   3828 O  OG   B SER   A 1 167 ? 4.613  -12.288 -2.170  0.28 21.12 ?  167 SER   A OG   1 
ATOM   3829 H  H    A SER   A 1 167 ? 3.824  -12.332 -0.050  0.72 22.31 ?  167 SER   A H    1 
ATOM   3830 H  H    B SER   A 1 167 ? 3.858  -12.405 0.415   0.28 22.16 ?  167 SER   A H    1 
ATOM   3831 H  HA   A SER   A 1 167 ? 3.201  -14.324 -1.742  0.72 23.17 ?  167 SER   A HA   1 
ATOM   3832 H  HA   B SER   A 1 167 ? 3.174  -14.794 -0.707  0.28 23.20 ?  167 SER   A HA   1 
ATOM   3833 H  HB2  A SER   A 1 167 ? 4.670  -13.294 -3.233  0.72 24.10 ?  167 SER   A HB2  1 
ATOM   3834 H  HB2  B SER   A 1 167 ? 3.933  -14.032 -2.754  0.28 24.49 ?  167 SER   A HB2  1 
ATOM   3835 H  HB3  A SER   A 1 167 ? 3.595  -12.246 -2.716  0.72 24.10 ?  167 SER   A HB3  1 
ATOM   3836 H  HB3  B SER   A 1 167 ? 2.801  -13.049 -2.228  0.28 24.49 ?  167 SER   A HB3  1 
ATOM   3837 H  HG   A SER   A 1 167 ? 5.137  -11.504 -1.342  0.72 23.91 ?  167 SER   A HG   1 
ATOM   3838 H  HG   B SER   A 1 167 ? 4.403  -11.698 -1.611  0.28 25.39 ?  167 SER   A HG   1 
ATOM   3839 N  N    A PHE   A 1 168 ? 5.514  -14.739 0.229   0.72 18.61 ?  168 PHE   A N    1 
ATOM   3840 N  N    B PHE   A 1 168 ? 5.249  -15.624 0.402   0.28 18.04 ?  168 PHE   A N    1 
ATOM   3841 C  CA   A PHE   A 1 168 ? 6.686  -15.537 0.554   0.72 19.13 ?  168 PHE   A CA   1 
ATOM   3842 C  CA   B PHE   A 1 168 ? 6.537  -16.205 0.766   0.28 17.07 ?  168 PHE   A CA   1 
ATOM   3843 C  C    A PHE   A 1 168 ? 6.368  -17.017 0.442   0.72 20.67 ?  168 PHE   A C    1 
ATOM   3844 C  C    B PHE   A 1 168 ? 6.544  -17.729 0.713   0.28 16.87 ?  168 PHE   A C    1 
ATOM   3845 O  O    A PHE   A 1 168 ? 5.384  -17.500 1.011   0.72 22.26 ?  168 PHE   A O    1 
ATOM   3846 O  O    B PHE   A 1 168 ? 7.456  -18.319 0.125   0.28 16.03 ?  168 PHE   A O    1 
ATOM   3847 C  CB   A PHE   A 1 168 ? 7.211  -15.252 1.957   0.72 18.38 ?  168 PHE   A CB   1 
ATOM   3848 C  CB   B PHE   A 1 168 ? 6.976  -15.731 2.154   0.28 17.02 ?  168 PHE   A CB   1 
ATOM   3849 C  CG   A PHE   A 1 168 ? 8.463  -16.028 2.273   0.72 17.82 ?  168 PHE   A CG   1 
ATOM   3850 C  CG   B PHE   A 1 168 ? 8.333  -16.235 2.564   0.28 17.06 ?  168 PHE   A CG   1 
ATOM   3851 C  CD1  A PHE   A 1 168 ? 9.656  -15.698 1.654   0.72 17.67 ?  168 PHE   A CD1  1 
ATOM   3852 C  CD1  B PHE   A 1 168 ? 9.478  -15.740 1.963   0.28 17.24 ?  168 PHE   A CD1  1 
ATOM   3853 C  CD2  A PHE   A 1 168 ? 8.447  -17.111 3.140   0.72 17.29 ?  168 PHE   A CD2  1 
ATOM   3854 C  CD2  B PHE   A 1 168 ? 8.466  -17.200 3.550   0.28 16.95 ?  168 PHE   A CD2  1 
ATOM   3855 C  CE1  A PHE   A 1 168 ? 10.809 -16.410 1.911   0.72 16.72 ?  168 PHE   A CE1  1 
ATOM   3856 C  CE1  B PHE   A 1 168 ? 10.728 -16.197 2.335   0.28 17.30 ?  168 PHE   A CE1  1 
ATOM   3857 C  CE2  A PHE   A 1 168 ? 9.607  -17.826 3.402   0.72 17.11 ?  168 PHE   A CE2  1 
ATOM   3858 C  CE2  B PHE   A 1 168 ? 9.716  -17.659 3.927   0.28 17.14 ?  168 PHE   A CE2  1 
ATOM   3859 C  CZ   A PHE   A 1 168 ? 10.786 -17.471 2.785   0.72 16.67 ?  168 PHE   A CZ   1 
ATOM   3860 C  CZ   B PHE   A 1 168 ? 10.846 -17.157 3.318   0.28 17.31 ?  168 PHE   A CZ   1 
ATOM   3861 H  H    A PHE   A 1 168 ? 5.169  -14.308 0.888   0.72 22.38 ?  168 PHE   A H    1 
ATOM   3862 H  H    B PHE   A 1 168 ? 4.570  -16.038 0.728   0.28 21.70 ?  168 PHE   A H    1 
ATOM   3863 H  HA   A PHE   A 1 168 ? 7.393  -15.332 -0.080  0.72 23.00 ?  168 PHE   A HA   1 
ATOM   3864 H  HA   B PHE   A 1 168 ? 7.204  -15.902 0.134   0.28 20.53 ?  168 PHE   A HA   1 
ATOM   3865 H  HB2  A PHE   A 1 168 ? 7.413  -14.307 2.033   0.72 22.11 ?  168 PHE   A HB2  1 
ATOM   3866 H  HB2  B PHE   A 1 168 ? 7.009  -14.762 2.155   0.28 20.48 ?  168 PHE   A HB2  1 
ATOM   3867 H  HB3  A PHE   A 1 168 ? 6.530  -15.500 2.603   0.72 22.11 ?  168 PHE   A HB3  1 
ATOM   3868 H  HB3  B PHE   A 1 168 ? 6.335  -16.042 2.810   0.28 20.48 ?  168 PHE   A HB3  1 
ATOM   3869 H  HD1  A PHE   A 1 168 ? 9.682  -14.980 1.064   0.72 21.25 ?  168 PHE   A HD1  1 
ATOM   3870 H  HD1  B PHE   A 1 168 ? 9.407  -15.094 1.299   0.28 20.74 ?  168 PHE   A HD1  1 
ATOM   3871 H  HD2  A PHE   A 1 168 ? 7.652  -17.354 3.558   0.72 20.80 ?  168 PHE   A HD2  1 
ATOM   3872 H  HD2  B PHE   A 1 168 ? 7.707  -17.542 3.964   0.28 20.39 ?  168 PHE   A HD2  1 
ATOM   3873 H  HE1  A PHE   A 1 168 ? 11.609 -16.171 1.497   0.72 20.12 ?  168 PHE   A HE1  1 
ATOM   3874 H  HE1  B PHE   A 1 168 ? 11.492 -15.857 1.925   0.28 20.81 ?  168 PHE   A HE1  1 
ATOM   3875 H  HE2  A PHE   A 1 168 ? 9.587  -18.547 3.991   0.72 20.58 ?  168 PHE   A HE2  1 
ATOM   3876 H  HE2  B PHE   A 1 168 ? 9.792  -18.306 4.591   0.28 20.62 ?  168 PHE   A HE2  1 
ATOM   3877 H  HZ   A PHE   A 1 168 ? 11.565 -17.951 2.959   0.72 20.05 ?  168 PHE   A HZ   1 
ATOM   3878 H  HZ   B PHE   A 1 168 ? 11.686 -17.464 3.571   0.28 20.81 ?  168 PHE   A HZ   1 
ATOM   3879 N  N    A LEU   A 1 169 ? 7.230  -17.744 -0.259  0.72 22.07 ?  169 LEU   A N    1 
ATOM   3880 N  N    B LEU   A 1 169 ? 5.561  -18.380 1.329   0.28 17.57 ?  169 LEU   A N    1 
ATOM   3881 C  CA   A LEU   A 1 169 ? 7.037  -19.172 -0.425  0.72 24.40 ?  169 LEU   A CA   1 
ATOM   3882 C  CA   B LEU   A 1 169 ? 5.571  -19.839 1.420   0.28 18.70 ?  169 LEU   A CA   1 
ATOM   3883 C  C    A LEU   A 1 169 ? 7.857  -19.927 0.609   0.72 24.32 ?  169 LEU   A C    1 
ATOM   3884 C  C    B LEU   A 1 169 ? 4.989  -20.489 0.167   0.28 19.46 ?  169 LEU   A C    1 
ATOM   3885 O  O    A LEU   A 1 169 ? 7.291  -20.412 1.592   0.72 24.72 ?  169 LEU   A O    1 
ATOM   3886 O  O    B LEU   A 1 169 ? 4.061  -19.968 -0.455  0.28 19.55 ?  169 LEU   A O    1 
ATOM   3887 C  CB   A LEU   A 1 169 ? 7.397  -19.606 -1.848  0.72 25.92 ?  169 LEU   A CB   1 
ATOM   3888 C  CB   B LEU   A 1 169 ? 4.800  -20.319 2.652   0.28 18.95 ?  169 LEU   A CB   1 
ATOM   3889 C  CG   A LEU   A 1 169 ? 7.071  -21.059 -2.210  0.72 27.25 ?  169 LEU   A CG   1 
ATOM   3890 C  CG   B LEU   A 1 169 ? 5.038  -21.787 3.018   0.28 19.20 ?  169 LEU   A CG   1 
ATOM   3891 C  CD1  A LEU   A 1 169 ? 5.646  -21.418 -1.814  0.72 27.77 ?  169 LEU   A CD1  1 
ATOM   3892 C  CD1  B LEU   A 1 169 ? 6.489  -21.995 3.430   0.28 19.59 ?  169 LEU   A CD1  1 
ATOM   3893 C  CD2  A LEU   A 1 169 ? 7.284  -21.307 -3.698  0.72 27.59 ?  169 LEU   A CD2  1 
ATOM   3894 C  CD2  B LEU   A 1 169 ? 4.094  -22.248 4.118   0.28 19.36 ?  169 LEU   A CD2  1 
ATOM   3895 O  OXT  A LEU   A 1 169 ? 9.080  -20.055 0.499   0.72 23.78 -1 169 LEU   A OXT  1 
ATOM   3896 O  OXT  B LEU   A 1 169 ? 5.431  -21.564 -0.243  0.28 20.32 -1 169 LEU   A OXT  1 
ATOM   3897 H  H    A LEU   A 1 169 ? 7.940  -17.436 -0.639  0.72 26.54 ?  169 LEU   A H    1 
ATOM   3898 H  H    B LEU   A 1 169 ? 4.883  -18.006 1.699   0.28 21.13 ?  169 LEU   A H    1 
ATOM   3899 H  HA   A LEU   A 1 169 ? 6.111  -19.384 -0.263  0.72 29.32 ?  169 LEU   A HA   1 
ATOM   3900 H  HA   B LEU   A 1 169 ? 6.491  -20.131 1.514   0.28 22.48 ?  169 LEU   A HA   1 
ATOM   3901 H  HB2  A LEU   A 1 169 ? 6.911  -19.040 -2.468  0.72 31.15 ?  169 LEU   A HB2  1 
ATOM   3902 H  HB2  B LEU   A 1 169 ? 5.064  -19.782 3.414   0.28 22.79 ?  169 LEU   A HB2  1 
ATOM   3903 H  HB3  A LEU   A 1 169 ? 8.349  -19.485 -1.978  0.72 31.15 ?  169 LEU   A HB3  1 
ATOM   3904 H  HB3  B LEU   A 1 169 ? 3.851  -20.212 2.488   0.28 22.79 ?  169 LEU   A HB3  1 
ATOM   3905 H  HG   A LEU   A 1 169 ? 7.670  -21.646 -1.725  0.72 32.75 ?  169 LEU   A HG   1 
ATOM   3906 H  HG   B LEU   A 1 169 ? 4.873  -22.337 2.237   0.28 23.09 ?  169 LEU   A HG   1 
ATOM   3907 H  HD11 A LEU   A 1 169 ? 5.400  -22.253 -2.241  0.72 33.37 ?  169 LEU   A HD11 1 
ATOM   3908 H  HD11 B LEU   A 1 169 ? 6.573  -22.855 3.869   0.28 23.55 ?  169 LEU   A HD11 1 
ATOM   3909 H  HD12 A LEU   A 1 169 ? 5.599  -21.514 -0.850  0.72 33.37 ?  169 LEU   A HD12 1 
ATOM   3910 H  HD12 B LEU   A 1 169 ? 7.052  -21.972 2.639   0.28 23.55 ?  169 LEU   A HD12 1 
ATOM   3911 H  HD13 A LEU   A 1 169 ? 5.049  -20.710 -2.106  0.72 33.37 ?  169 LEU   A HD13 1 
ATOM   3912 H  HD13 B LEU   A 1 169 ? 6.750  -21.287 4.041   0.28 23.55 ?  169 LEU   A HD13 1 
ATOM   3913 H  HD21 A LEU   A 1 169 ? 7.079  -22.235 -3.897  0.72 33.15 ?  169 LEU   A HD21 1 
ATOM   3914 H  HD21 B LEU   A 1 169 ? 4.273  -23.181 4.317   0.28 23.28 ?  169 LEU   A HD21 1 
ATOM   3915 H  HD22 A LEU   A 1 169 ? 6.695  -20.724 -4.203  0.72 33.15 ?  169 LEU   A HD22 1 
ATOM   3916 H  HD22 B LEU   A 1 169 ? 4.244  -21.707 4.909   0.28 23.28 ?  169 LEU   A HD22 1 
ATOM   3917 H  HD23 A LEU   A 1 169 ? 8.208  -21.118 -3.921  0.72 33.15 ?  169 LEU   A HD23 1 
ATOM   3918 H  HD23 B LEU   A 1 169 ? 3.181  -22.143 3.812   0.28 23.28 ?  169 LEU   A HD23 1 
ATOM   3919 N  N    A SER   B 1 1   ? 50.799 -9.249  -23.721 0.72 27.41 ?  1   SER   B N    1 
ATOM   3920 N  N    B SER   B 1 1   ? 50.746 -9.245  -23.679 0.28 26.59 ?  1   SER   B N    1 
ATOM   3921 C  CA   A SER   B 1 1   ? 51.282 -10.288 -22.791 0.72 27.42 ?  1   SER   B CA   1 
ATOM   3922 C  CA   B SER   B 1 1   ? 51.244 -10.250 -22.716 0.28 26.50 ?  1   SER   B CA   1 
ATOM   3923 C  C    A SER   B 1 1   ? 50.216 -11.346 -22.555 0.72 26.38 ?  1   SER   B C    1 
ATOM   3924 C  C    B SER   B 1 1   ? 50.194 -11.325 -22.487 0.28 25.97 ?  1   SER   B C    1 
ATOM   3925 O  O    A SER   B 1 1   ? 49.021 -11.146 -22.823 0.72 26.37 ?  1   SER   B O    1 
ATOM   3926 O  O    B SER   B 1 1   ? 49.019 -11.156 -22.826 0.28 25.85 ?  1   SER   B O    1 
ATOM   3927 C  CB   A SER   B 1 1   ? 51.707 -9.672  -21.460 0.72 28.24 ?  1   SER   B CB   1 
ATOM   3928 C  CB   B SER   B 1 1   ? 51.600 -9.591  -21.388 0.28 26.84 ?  1   SER   B CB   1 
ATOM   3929 O  OG   A SER   B 1 1   ? 50.579 -9.338  -20.674 0.72 30.31 ?  1   SER   B OG   1 
ATOM   3930 O  OG   B SER   B 1 1   ? 50.448 -9.440  -20.579 0.28 27.63 ?  1   SER   B OG   1 
ATOM   3931 H  H1   A SER   B 1 1   ? 50.761 -9.590  -24.540 0.72 32.94 ?  1   SER   B H1   1 
ATOM   3932 H  H1   B SER   B 1 1   ? 51.438 -8.805  -24.019 0.28 31.96 ?  1   SER   B H1   1 
ATOM   3933 H  H2   A SER   B 1 1   ? 49.995 -8.983  -23.464 0.72 32.94 ?  1   SER   B H2   1 
ATOM   3934 H  H2   B SER   B 1 1   ? 50.304 -9.660  -24.328 0.28 31.96 ?  1   SER   B H2   1 
ATOM   3935 H  H3   A SER   B 1 1   ? 51.366 -8.565  -23.705 0.72 32.94 ?  1   SER   B H3   1 
ATOM   3936 H  H3   B SER   B 1 1   ? 50.207 -8.683  -23.257 0.28 31.96 ?  1   SER   B H3   1 
ATOM   3937 H  HA   A SER   B 1 1   ? 52.053 -10.714 -23.189 0.72 32.96 ?  1   SER   B HA   1 
ATOM   3938 H  HA   B SER   B 1 1   ? 52.037 -10.660 -23.085 0.28 31.85 ?  1   SER   B HA   1 
ATOM   3939 H  HB2  A SER   B 1 1   ? 52.245 -10.318 -20.979 0.72 33.93 ?  1   SER   B HB2  1 
ATOM   3940 H  HB2  B SER   B 1 1   ? 52.245 -10.150 -20.930 0.28 32.26 ?  1   SER   B HB2  1 
ATOM   3941 H  HB3  A SER   B 1 1   ? 52.224 -8.870  -21.631 0.72 33.93 ?  1   SER   B HB3  1 
ATOM   3942 H  HB3  B SER   B 1 1   ? 51.980 -8.715  -21.559 0.28 32.26 ?  1   SER   B HB3  1 
ATOM   3943 H  HG   A SER   B 1 1   ? 50.819 -8.865  -20.021 0.72 36.42 ?  1   SER   B HG   1 
ATOM   3944 H  HG   B SER   B 1 1   ? 50.582 -8.843  -20.005 0.28 33.20 ?  1   SER   B HG   1 
ATOM   3945 N  N    A MET   B 1 2   ? 50.672 -12.477 -22.038 0.72 25.38 ?  2   MET   B N    1 
ATOM   3946 N  N    B MET   B 1 2   ? 50.631 -12.430 -21.898 0.28 25.47 ?  2   MET   B N    1 
ATOM   3947 C  CA   A MET   B 1 2   ? 49.854 -13.668 -21.867 0.72 25.54 ?  2   MET   B CA   1 
ATOM   3948 C  CA   B MET   B 1 2   ? 49.804 -13.614 -21.709 0.28 25.06 ?  2   MET   B CA   1 
ATOM   3949 C  C    A MET   B 1 2   ? 49.600 -13.858 -20.379 0.72 23.69 ?  2   MET   B C    1 
ATOM   3950 C  C    B MET   B 1 2   ? 49.526 -13.777 -20.222 0.28 23.46 ?  2   MET   B C    1 
ATOM   3951 O  O    A MET   B 1 2   ? 50.533 -14.106 -19.611 0.72 23.92 ?  2   MET   B O    1 
ATOM   3952 O  O    B MET   B 1 2   ? 50.433 -14.096 -19.445 0.28 23.66 ?  2   MET   B O    1 
ATOM   3953 C  CB   A MET   B 1 2   ? 50.587 -14.864 -22.459 0.72 29.16 ?  2   MET   B CB   1 
ATOM   3954 C  CB   B MET   B 1 2   ? 50.543 -14.826 -22.258 0.28 26.61 ?  2   MET   B CB   1 
ATOM   3955 C  CG   A MET   B 1 2   ? 49.741 -16.115 -22.616 0.72 32.61 ?  2   MET   B CG   1 
ATOM   3956 C  CG   B MET   B 1 2   ? 49.649 -15.960 -22.738 0.28 27.87 ?  2   MET   B CG   1 
ATOM   3957 S  SD   A MET   B 1 2   ? 50.562 -17.342 -23.648 0.72 36.03 ?  2   MET   B SD   1 
ATOM   3958 S  SD   B MET   B 1 2   ? 50.536 -17.069 -23.835 0.28 29.06 ?  2   MET   B SD   1 
ATOM   3959 C  CE   A MET   B 1 2   ? 51.100 -16.290 -24.988 0.72 36.12 ?  2   MET   B CE   1 
ATOM   3960 C  CE   B MET   B 1 2   ? 51.519 -15.890 -24.741 0.28 29.25 ?  2   MET   B CE   1 
ATOM   3961 H  H    A MET   B 1 2   ? 51.485 -12.589 -21.772 0.72 30.50 ?  2   MET   B H    1 
ATOM   3962 H  H    B MET   B 1 2   ? 51.433 -12.525 -21.600 0.28 30.62 ?  2   MET   B H    1 
ATOM   3963 H  HA   A MET   B 1 2   ? 49.013 -13.565 -22.335 0.72 30.70 ?  2   MET   B HA   1 
ATOM   3964 H  HA   B MET   B 1 2   ? 48.975 -13.522 -22.205 0.28 30.13 ?  2   MET   B HA   1 
ATOM   3965 H  HB2  A MET   B 1 2   ? 50.910 -14.584 -23.325 0.72 35.05 ?  2   MET   B HB2  1 
ATOM   3966 H  HB2  B MET   B 1 2   ? 51.083 -14.484 -22.981 0.28 31.98 ?  2   MET   B HB2  1 
ATOM   3967 H  HB3  A MET   B 1 2   ? 51.335 -15.099 -21.893 0.72 35.05 ?  2   MET   B HB3  1 
ATOM   3968 H  HB3  B MET   B 1 2   ? 51.118 -15.200 -21.582 0.28 31.98 ?  2   MET   B HB3  1 
ATOM   3969 H  HG2  A MET   B 1 2   ? 49.580 -16.502 -21.737 0.72 39.19 ?  2   MET   B HG2  1 
ATOM   3970 H  HG2  B MET   B 1 2   ? 49.341 -16.472 -21.969 0.28 33.49 ?  2   MET   B HG2  1 
ATOM   3971 H  HG3  A MET   B 1 2   ? 48.901 -15.889 -23.043 0.72 39.19 ?  2   MET   B HG3  1 
ATOM   3972 H  HG3  B MET   B 1 2   ? 48.893 -15.609 -23.227 0.28 33.49 ?  2   MET   B HG3  1 
ATOM   3973 H  HE1  A MET   B 1 2   ? 51.243 -16.837 -25.762 0.72 43.39 ?  2   MET   B HE1  1 
ATOM   3974 H  HE1  B MET   B 1 2   ? 51.788 -16.319 -25.541 0.28 35.15 ?  2   MET   B HE1  1 
ATOM   3975 H  HE2  A MET   B 1 2   ? 50.401 -15.636 -25.160 0.72 43.39 ?  2   MET   B HE2  1 
ATOM   3976 H  HE2  B MET   B 1 2   ? 50.974 -15.108 -24.947 0.28 35.15 ?  2   MET   B HE2  1 
ATOM   3977 H  HE3  A MET   B 1 2   ? 51.925 -15.831 -24.743 0.72 43.39 ?  2   MET   B HE3  1 
ATOM   3978 H  HE3  B MET   B 1 2   ? 52.301 -15.629 -24.216 0.28 35.15 ?  2   MET   B HE3  1 
ATOM   3979 N  N    A VAL   B 1 3   ? 48.343 -13.719 -19.972 0.72 21.42 ?  3   VAL   B N    1 
ATOM   3980 N  N    B VAL   B 1 3   ? 48.279 -13.546 -19.828 0.28 21.65 ?  3   VAL   B N    1 
ATOM   3981 C  CA   A VAL   B 1 3   ? 47.927 -13.950 -18.597 0.72 20.34 ?  3   VAL   B CA   1 
ATOM   3982 C  CA   B VAL   B 1 3   ? 47.832 -13.784 -18.464 0.28 20.13 ?  3   VAL   B CA   1 
ATOM   3983 C  C    A VAL   B 1 3   ? 46.689 -14.836 -18.616 0.72 18.62 ?  3   VAL   B C    1 
ATOM   3984 C  C    B VAL   B 1 3   ? 46.578 -14.643 -18.501 0.28 18.29 ?  3   VAL   B C    1 
ATOM   3985 O  O    A VAL   B 1 3   ? 45.984 -14.943 -19.623 0.72 19.22 ?  3   VAL   B O    1 
ATOM   3986 O  O    B VAL   B 1 3   ? 45.756 -14.543 -19.417 0.28 18.19 ?  3   VAL   B O    1 
ATOM   3987 C  CB   A VAL   B 1 3   ? 47.640 -12.634 -17.839 0.72 21.90 ?  3   VAL   B CB   1 
ATOM   3988 C  CB   B VAL   B 1 3   ? 47.564 -12.477 -17.688 0.28 20.62 ?  3   VAL   B CB   1 
ATOM   3989 C  CG1  A VAL   B 1 3   ? 48.904 -11.780 -17.742 0.72 22.48 ?  3   VAL   B CG1  1 
ATOM   3990 C  CG1  B VAL   B 1 3   ? 48.830 -11.638 -17.592 0.28 20.88 ?  3   VAL   B CG1  1 
ATOM   3991 C  CG2  A VAL   B 1 3   ? 46.515 -11.868 -18.518 0.72 22.69 ?  3   VAL   B CG2  1 
ATOM   3992 C  CG2  B VAL   B 1 3   ? 46.436 -11.696 -18.338 0.28 20.86 ?  3   VAL   B CG2  1 
ATOM   3993 H  H    A VAL   B 1 3   ? 47.698 -13.498 -20.492 0.72 25.76 ?  3   VAL   B H    1 
ATOM   3994 H  H    B VAL   B 1 3   ? 47.670 -13.242 -20.352 0.28 26.03 ?  3   VAL   B H    1 
ATOM   3995 H  HA   A VAL   B 1 3   ? 48.632 -14.425 -18.124 0.72 24.45 ?  3   VAL   B HA   1 
ATOM   3996 H  HA   B VAL   B 1 3   ? 48.523 -14.277 -17.994 0.28 24.21 ?  3   VAL   B HA   1 
ATOM   3997 H  HB   A VAL   B 1 3   ? 47.356 -12.851 -16.937 0.72 26.33 ?  3   VAL   B HB   1 
ATOM   3998 H  HB   B VAL   B 1 3   ? 47.288 -12.706 -16.788 0.28 24.80 ?  3   VAL   B HB   1 
ATOM   3999 H  HG11 A VAL   B 1 3   ? 48.695 -10.968 -17.254 0.72 27.03 ?  3   VAL   B HG11 1 
ATOM   4000 H  HG11 B VAL   B 1 3   ? 48.635 -10.835 -17.084 0.28 25.10 ?  3   VAL   B HG11 1 
ATOM   4001 H  HG12 A VAL   B 1 3   ? 49.589 -12.282 -17.272 0.72 27.03 ?  3   VAL   B HG12 1 
ATOM   4002 H  HG12 B VAL   B 1 3   ? 49.517 -12.155 -17.144 0.28 25.10 ?  3   VAL   B HG12 1 
ATOM   4003 H  HG13 A VAL   B 1 3   ? 49.206 -11.562 -18.636 0.72 27.03 ?  3   VAL   B HG13 1 
ATOM   4004 H  HG13 B VAL   B 1 3   ? 49.121 -11.402 -18.486 0.28 25.10 ?  3   VAL   B HG13 1 
ATOM   4005 H  HG21 A VAL   B 1 3   ? 46.450 -10.989 -18.120 0.72 27.27 ?  3   VAL   B HG21 1 
ATOM   4006 H  HG21 B VAL   B 1 3   ? 46.398 -10.814 -17.942 0.28 25.08 ?  3   VAL   B HG21 1 
ATOM   4007 H  HG22 A VAL   B 1 3   ? 46.709 -11.792 -19.465 0.72 27.27 ?  3   VAL   B HG22 1 
ATOM   4008 H  HG22 B VAL   B 1 3   ? 46.607 -11.627 -19.290 0.28 25.08 ?  3   VAL   B HG22 1 
ATOM   4009 H  HG23 A VAL   B 1 3   ? 45.681 -12.351 -18.391 0.72 27.27 ?  3   VAL   B HG23 1 
ATOM   4010 H  HG23 B VAL   B 1 3   ? 45.599 -12.164 -18.186 0.28 25.08 ?  3   VAL   B HG23 1 
ATOM   4011 N  N    . ASN   B 1 4   ? 46.431 -15.484 -17.480 1.00 16.84 ?  4   ASN   B N    1 
ATOM   4012 C  CA   . ASN   B 1 4   ? 45.292 -16.393 -17.363 1.00 15.87 ?  4   ASN   B CA   1 
ATOM   4013 C  C    . ASN   B 1 4   ? 45.236 -17.359 -18.545 1.00 16.19 ?  4   ASN   B C    1 
ATOM   4014 O  O    . ASN   B 1 4   ? 44.178 -17.610 -19.116 1.00 16.96 ?  4   ASN   B O    1 
ATOM   4015 C  CB   . ASN   B 1 4   ? 43.973 -15.632 -17.203 1.00 15.24 ?  4   ASN   B CB   1 
ATOM   4016 C  CG   . ASN   B 1 4   ? 43.922 -14.820 -15.921 1.00 14.40 ?  4   ASN   B CG   1 
ATOM   4017 O  OD1  . ASN   B 1 4   ? 44.206 -15.331 -14.838 1.00 14.43 ?  4   ASN   B OD1  1 
ATOM   4018 N  ND2  . ASN   B 1 4   ? 43.576 -13.543 -16.041 1.00 15.68 ?  4   ASN   B ND2  1 
ATOM   4019 H  H    A ASN   B 1 4   ? 46.904 -15.417 -16.766 0.72 20.26 ?  4   ASN   B H    1 
ATOM   4020 H  H    B ASN   B 1 4   ? 46.988 -15.544 -16.828 0.28 20.26 ?  4   ASN   B H    1 
ATOM   4021 H  HA   . ASN   B 1 4   ? 45.417 -16.927 -16.561 1.00 19.10 ?  4   ASN   B HA   1 
ATOM   4022 H  HB2  . ASN   B 1 4   ? 43.864 -15.025 -17.950 1.00 18.34 ?  4   ASN   B HB2  1 
ATOM   4023 H  HB3  . ASN   B 1 4   ? 43.242 -16.272 -17.186 1.00 18.34 ?  4   ASN   B HB3  1 
ATOM   4024 H  HD21 . ASN   B 1 4   ? 43.535 -13.039 -15.343 1.00 18.86 ?  4   ASN   B HD21 1 
ATOM   4025 H  HD22 . ASN   B 1 4   ? 43.388 -13.216 -16.815 1.00 18.86 ?  4   ASN   B HD22 1 
ATOM   4026 N  N    . SER   B 1 5   ? 46.396 -17.896 -18.922 1.00 17.51 ?  5   SER   B N    1 
ATOM   4027 C  CA   . SER   B 1 5   ? 46.496 -18.809 -20.060 1.00 19.52 ?  5   SER   B CA   1 
ATOM   4028 C  C    . SER   B 1 5   ? 46.470 -20.243 -19.543 1.00 21.12 ?  5   SER   B C    1 
ATOM   4029 O  O    . SER   B 1 5   ? 47.472 -20.951 -19.521 1.00 23.59 ?  5   SER   B O    1 
ATOM   4030 C  CB   . SER   B 1 5   ? 47.764 -18.524 -20.862 1.00 20.85 ?  5   SER   B CB   1 
ATOM   4031 O  OG   . SER   B 1 5   ? 48.925 -18.725 -20.075 1.00 23.39 ?  5   SER   B OG   1 
ATOM   4032 H  H    . SER   B 1 5   ? 47.148 -17.752 -18.531 1.00 21.06 ?  5   SER   B H    1 
ATOM   4033 H  HA   . SER   B 1 5   ? 45.733 -18.683 -20.644 1.00 23.47 ?  5   SER   B HA   1 
ATOM   4034 H  HB2  . SER   B 1 5   ? 47.793 -19.118 -21.632 1.00 25.07 ?  5   SER   B HB2  1 
ATOM   4035 H  HB3  . SER   B 1 5   ? 47.730 -17.603 -21.161 1.00 25.07 ?  5   SER   B HB3  1 
ATOM   4036 H  HG   . SER   B 1 5   ? 48.969 -19.527 -19.831 1.00 28.11 ?  5   SER   B HG   1 
ATOM   4037 N  N    . PHE   B 1 6   ? 45.287 -20.643 -19.091 1.00 21.65 ?  6   PHE   B N    1 
ATOM   4038 C  CA   . PHE   B 1 6   ? 45.072 -21.990 -18.584 1.00 21.19 ?  6   PHE   B CA   1 
ATOM   4039 C  C    . PHE   B 1 6   ? 44.981 -22.956 -19.757 1.00 24.83 ?  6   PHE   B C    1 
ATOM   4040 O  O    . PHE   B 1 6   ? 44.323 -22.662 -20.759 1.00 26.86 ?  6   PHE   B O    1 
ATOM   4041 C  CB   . PHE   B 1 6   ? 43.780 -22.035 -17.769 1.00 19.15 ?  6   PHE   B CB   1 
ATOM   4042 C  CG   . PHE   B 1 6   ? 43.812 -21.182 -16.531 1.00 17.23 ?  6   PHE   B CG   1 
ATOM   4043 C  CD1  . PHE   B 1 6   ? 44.320 -21.683 -15.346 1.00 15.97 ?  6   PHE   B CD1  1 
ATOM   4044 C  CD2  . PHE   B 1 6   ? 43.332 -19.880 -16.553 1.00 16.42 ?  6   PHE   B CD2  1 
ATOM   4045 C  CE1  . PHE   B 1 6   ? 44.343 -20.903 -14.199 1.00 15.42 ?  6   PHE   B CE1  1 
ATOM   4046 C  CE2  . PHE   B 1 6   ? 43.357 -19.092 -15.415 1.00 16.78 ?  6   PHE   B CE2  1 
ATOM   4047 C  CZ   . PHE   B 1 6   ? 43.869 -19.599 -14.238 1.00 15.90 ?  6   PHE   B CZ   1 
ATOM   4048 H  H    . PHE   B 1 6   ? 44.581 -20.152 -19.072 1.00 26.02 ?  6   PHE   B H    1 
ATOM   4049 H  HA   . PHE   B 1 6   ? 45.810 -22.255 -18.018 1.00 25.47 ?  6   PHE   B HA   1 
ATOM   4050 H  HB2  . PHE   B 1 6   ? 43.048 -21.724 -18.326 1.00 23.03 ?  6   PHE   B HB2  1 
ATOM   4051 H  HB3  . PHE   B 1 6   ? 43.614 -22.951 -17.495 1.00 23.03 ?  6   PHE   B HB3  1 
ATOM   4052 H  HD1  . PHE   B 1 6   ? 44.646 -22.553 -15.317 1.00 19.22 ?  6   PHE   B HD1  1 
ATOM   4053 H  HD2  . PHE   B 1 6   ? 42.985 -19.534 -17.343 1.00 19.76 ?  6   PHE   B HD2  1 
ATOM   4054 H  HE1  . PHE   B 1 6   ? 44.694 -21.247 -13.409 1.00 18.55 ?  6   PHE   B HE1  1 
ATOM   4055 H  HE2  . PHE   B 1 6   ? 43.029 -18.221 -15.443 1.00 20.18 ?  6   PHE   B HE2  1 
ATOM   4056 H  HZ   . PHE   B 1 6   ? 43.885 -19.076 -13.470 1.00 19.12 ?  6   PHE   B HZ   1 
ATOM   4057 N  N    . SER   B 1 7   ? 45.659 -24.098 -19.639 1.00 26.46 ?  7   SER   B N    1 
ATOM   4058 C  CA   . SER   B 1 7   ? 45.730 -25.071 -20.718 1.00 29.96 ?  7   SER   B CA   1 
ATOM   4059 C  C    . SER   B 1 7   ? 45.665 -26.479 -20.149 1.00 28.78 ?  7   SER   B C    1 
ATOM   4060 O  O    . SER   B 1 7   ? 46.272 -26.771 -19.115 1.00 29.62 ?  7   SER   B O    1 
ATOM   4061 C  CB   . SER   B 1 7   ? 47.026 -24.898 -21.524 1.00 33.50 ?  7   SER   B CB   1 
ATOM   4062 O  OG   . SER   B 1 7   ? 47.027 -25.722 -22.677 1.00 35.09 ?  7   SER   B OG   1 
ATOM   4063 H  H    . SER   B 1 7   ? 46.103 -24.328 -18.935 1.00 31.81 ?  7   SER   B H    1 
ATOM   4064 H  HA   . SER   B 1 7   ? 44.980 -24.950 -21.316 1.00 36.00 ?  7   SER   B HA   1 
ATOM   4065 H  HB2  . SER   B 1 7   ? 47.105 -23.970 -21.800 1.00 40.25 ?  7   SER   B HB2  1 
ATOM   4066 H  HB3  . SER   B 1 7   ? 47.783 -25.139 -20.964 1.00 40.25 ?  7   SER   B HB3  1 
ATOM   4067 H  HG   . SER   B 1 7   ? 47.742 -25.615 -23.107 1.00 42.15 ?  7   SER   B HG   1 
ATOM   4068 N  N    . GLY   B 1 8   ? 44.923 -27.349 -20.833 1.00 27.98 ?  8   GLY   B N    1 
ATOM   4069 C  CA   . GLY   B 1 8   ? 44.880 -28.748 -20.468 1.00 26.97 ?  8   GLY   B CA   1 
ATOM   4070 C  C    . GLY   B 1 8   ? 43.957 -29.082 -19.324 1.00 25.22 ?  8   GLY   B C    1 
ATOM   4071 O  O    . GLY   B 1 8   ? 44.094 -30.158 -18.728 1.00 26.82 ?  8   GLY   B O    1 
ATOM   4072 H  H    . GLY   B 1 8   ? 44.440 -27.143 -21.513 1.00 33.62 ?  8   GLY   B H    1 
ATOM   4073 H  HA2  . GLY   B 1 8   ? 44.593 -29.263 -21.236 1.00 32.41 ?  8   GLY   B HA2  1 
ATOM   4074 H  HA3  . GLY   B 1 8   ? 45.772 -29.037 -20.225 1.00 32.41 ?  8   GLY   B HA3  1 
ATOM   4075 N  N    . TYR   B 1 9   ? 42.998 -28.216 -19.011 1.00 23.14 ?  9   TYR   B N    1 
ATOM   4076 C  CA   . TYR   B 1 9   ? 42.058 -28.499 -17.940 1.00 20.84 ?  9   TYR   B CA   1 
ATOM   4077 C  C    . TYR   B 1 9   ? 40.872 -29.293 -18.453 1.00 19.96 ?  9   TYR   B C    1 
ATOM   4078 O  O    . TYR   B 1 9   ? 40.448 -29.153 -19.604 1.00 21.98 ?  9   TYR   B O    1 
ATOM   4079 C  CB   . TYR   B 1 9   ? 41.547 -27.219 -17.284 1.00 20.04 ?  9   TYR   B CB   1 
ATOM   4080 C  CG   . TYR   B 1 9   ? 42.576 -26.592 -16.377 1.00 19.21 ?  9   TYR   B CG   1 
ATOM   4081 C  CD1  . TYR   B 1 9   ? 43.653 -25.901 -16.904 1.00 19.69 ?  9   TYR   B CD1  1 
ATOM   4082 C  CD2  . TYR   B 1 9   ? 42.486 -26.712 -14.998 1.00 18.36 ?  9   TYR   B CD2  1 
ATOM   4083 C  CE1  . TYR   B 1 9   ? 44.610 -25.339 -16.086 1.00 19.78 ?  9   TYR   B CE1  1 
ATOM   4084 C  CE2  . TYR   B 1 9   ? 43.440 -26.151 -14.167 1.00 18.72 ?  9   TYR   B CE2  1 
ATOM   4085 C  CZ   . TYR   B 1 9   ? 44.502 -25.464 -14.719 1.00 19.50 ?  9   TYR   B CZ   1 
ATOM   4086 O  OH   . TYR   B 1 9   ? 45.457 -24.910 -13.904 1.00 20.17 ?  9   TYR   B OH   1 
ATOM   4087 H  H    . TYR   B 1 9   ? 42.854 -27.472 -19.417 1.00 27.82 ?  9   TYR   B H    1 
ATOM   4088 H  HA   . TYR   B 1 9   ? 42.495 -29.029 -17.260 1.00 25.05 ?  9   TYR   B HA   1 
ATOM   4089 H  HB2  . TYR   B 1 9   ? 41.302 -26.574 -17.967 1.00 24.10 ?  9   TYR   B HB2  1 
ATOM   4090 H  HB3  . TYR   B 1 9   ? 40.774 -27.446 -16.747 1.00 24.10 ?  9   TYR   B HB3  1 
ATOM   4091 H  HD1  . TYR   B 1 9   ? 43.726 -25.817 -17.828 1.00 23.68 ?  9   TYR   B HD1  1 
ATOM   4092 H  HD2  . TYR   B 1 9   ? 41.765 -27.184 -14.626 1.00 22.08 ?  9   TYR   B HD2  1 
ATOM   4093 H  HE1  . TYR   B 1 9   ? 45.318 -24.880 -16.458 1.00 23.78 ?  9   TYR   B HE1  1 
ATOM   4094 H  HE2  . TYR   B 1 9   ? 43.356 -26.247 -13.245 1.00 22.51 ?  9   TYR   B HE2  1 
ATOM   4095 H  HH   . TYR   B 1 9   ? 46.030 -24.524 -14.371 1.00 24.25 ?  9   TYR   B HH   1 
ATOM   4096 N  N    . LEU   B 1 10  ? 40.353 -30.143 -17.577 1.00 18.10 ?  10  LEU   B N    1 
ATOM   4097 C  CA   . LEU   B 1 10  ? 39.149 -30.910 -17.836 1.00 18.25 ?  10  LEU   B CA   1 
ATOM   4098 C  C    . LEU   B 1 10  ? 37.963 -30.141 -17.274 1.00 17.84 ?  10  LEU   B C    1 
ATOM   4099 O  O    . LEU   B 1 10  ? 37.980 -29.724 -16.111 1.00 17.17 ?  10  LEU   B O    1 
ATOM   4100 C  CB   . LEU   B 1 10  ? 39.265 -32.271 -17.150 1.00 19.34 ?  10  LEU   B CB   1 
ATOM   4101 C  CG   . LEU   B 1 10  ? 38.137 -33.249 -17.462 1.00 21.16 ?  10  LEU   B CG   1 
ATOM   4102 C  CD1  . LEU   B 1 10  ? 38.257 -33.764 -18.889 1.00 22.26 ?  10  LEU   B CD1  1 
ATOM   4103 C  CD2  . LEU   B 1 10  ? 38.111 -34.396 -16.464 1.00 22.45 ?  10  LEU   B CD2  1 
ATOM   4104 H  H    . LEU   B 1 10  ? 40.684 -30.293 -16.794 1.00 21.77 ?  10  LEU   B H    1 
ATOM   4105 H  HA   . LEU   B 1 10  ? 39.025 -31.043 -18.787 1.00 21.94 ?  10  LEU   B HA   1 
ATOM   4106 H  HB2  . LEU   B 1 10  ? 40.096 -32.690 -17.426 1.00 23.26 ?  10  LEU   B HB2  1 
ATOM   4107 H  HB3  . LEU   B 1 10  ? 39.273 -32.138 -16.188 1.00 23.26 ?  10  LEU   B HB3  1 
ATOM   4108 H  HG   . LEU   B 1 10  ? 37.292 -32.782 -17.390 1.00 25.44 ?  10  LEU   B HG   1 
ATOM   4109 H  HD11 . LEU   B 1 10  ? 37.567 -34.428 -19.042 1.00 26.76 ?  10  LEU   B HD11 1 
ATOM   4110 H  HD12 . LEU   B 1 10  ? 38.141 -33.021 -19.502 1.00 26.76 ?  10  LEU   B HD12 1 
ATOM   4111 H  HD13 . LEU   B 1 10  ? 39.132 -34.161 -19.010 1.00 26.76 ?  10  LEU   B HD13 1 
ATOM   4112 H  HD21 . LEU   B 1 10  ? 37.386 -34.994 -16.696 1.00 26.99 ?  10  LEU   B HD21 1 
ATOM   4113 H  HD22 . LEU   B 1 10  ? 38.957 -34.862 -16.500 1.00 26.99 ?  10  LEU   B HD22 1 
ATOM   4114 H  HD23 . LEU   B 1 10  ? 37.969 -34.029 -15.576 1.00 26.99 ?  10  LEU   B HD23 1 
ATOM   4115 N  N    . LYS   B 1 11  ? 36.941 -29.954 -18.099 1.00 19.08 ?  11  LYS   B N    1 
ATOM   4116 C  CA   . LYS   B 1 11  ? 35.743 -29.241 -17.684 1.00 21.38 ?  11  LYS   B CA   1 
ATOM   4117 C  C    . LYS   B 1 11  ? 34.884 -30.170 -16.834 1.00 20.36 ?  11  LYS   B C    1 
ATOM   4118 O  O    . LYS   B 1 11  ? 34.524 -31.269 -17.274 1.00 22.12 ?  11  LYS   B O    1 
ATOM   4119 C  CB   . LYS   B 1 11  ? 34.984 -28.791 -18.931 1.00 25.32 ?  11  LYS   B CB   1 
ATOM   4120 C  CG   . LYS   B 1 11  ? 33.840 -27.825 -18.681 1.00 28.99 ?  11  LYS   B CG   1 
ATOM   4121 C  CD   . LYS   B 1 11  ? 33.085 -27.551 -19.977 1.00 31.97 ?  11  LYS   B CD   1 
ATOM   4122 C  CE   . LYS   B 1 11  ? 32.077 -26.427 -19.818 1.00 34.06 ?  11  LYS   B CE   1 
ATOM   4123 N  NZ   . LYS   B 1 11  ? 32.743 -25.109 -19.625 1.00 35.19 ?  11  LYS   B NZ   1 
ATOM   4124 H  H    . LYS   B 1 11  ? 36.910 -30.242 -18.910 1.00 22.94 ?  11  LYS   B H    1 
ATOM   4125 H  HA   . LYS   B 1 11  ? 35.984 -28.461 -17.160 1.00 25.70 ?  11  LYS   B HA   1 
ATOM   4126 H  HB2  . LYS   B 1 11  ? 35.609 -28.348 -19.530 1.00 30.44 ?  11  LYS   B HB2  1 
ATOM   4127 H  HB3  . LYS   B 1 11  ? 34.614 -29.572 -19.370 1.00 30.44 ?  11  LYS   B HB3  1 
ATOM   4128 H  HG2  . LYS   B 1 11  ? 33.221 -28.214 -18.043 1.00 34.84 ?  11  LYS   B HG2  1 
ATOM   4129 H  HG3  . LYS   B 1 11  ? 34.190 -26.985 -18.347 1.00 34.84 ?  11  LYS   B HG3  1 
ATOM   4130 H  HD2  . LYS   B 1 11  ? 33.719 -27.296 -20.667 1.00 38.41 ?  11  LYS   B HD2  1 
ATOM   4131 H  HD3  . LYS   B 1 11  ? 32.607 -28.353 -20.244 1.00 38.41 ?  11  LYS   B HD3  1 
ATOM   4132 H  HE2  . LYS   B 1 11  ? 31.528 -26.375 -20.616 1.00 40.92 ?  11  LYS   B HE2  1 
ATOM   4133 H  HE3  . LYS   B 1 11  ? 31.524 -26.607 -19.042 1.00 40.92 ?  11  LYS   B HE3  1 
ATOM   4134 H  HZ1  . LYS   B 1 11  ? 32.131 -24.467 -19.553 1.00 42.28 ?  11  LYS   B HZ1  1 
ATOM   4135 H  HZ2  . LYS   B 1 11  ? 33.238 -25.123 -18.886 1.00 42.28 ?  11  LYS   B HZ2  1 
ATOM   4136 H  HZ3  . LYS   B 1 11  ? 33.268 -24.930 -20.322 1.00 42.28 ?  11  LYS   B HZ3  1 
ATOM   4137 N  N    . LEU   B 1 12  ? 34.561 -29.740 -15.615 1.00 18.61 ?  12  LEU   B N    1 
ATOM   4138 C  CA   . LEU   B 1 12  ? 33.602 -30.446 -14.773 1.00 18.12 ?  12  LEU   B CA   1 
ATOM   4139 C  C    . LEU   B 1 12  ? 32.212 -29.838 -14.861 1.00 18.13 ?  12  LEU   B C    1 
ATOM   4140 O  O    . LEU   B 1 12  ? 31.225 -30.554 -15.036 1.00 18.50 ?  12  LEU   B O    1 
ATOM   4141 C  CB   . LEU   B 1 12  ? 34.066 -30.469 -13.311 1.00 17.71 ?  12  LEU   B CB   1 
ATOM   4142 C  CG   . LEU   B 1 12  ? 35.410 -31.142 -13.037 1.00 17.50 ?  12  LEU   B CG   1 
ATOM   4143 C  CD1  . LEU   B 1 12  ? 35.745 -31.094 -11.557 1.00 17.52 ?  12  LEU   B CD1  1 
ATOM   4144 C  CD2  . LEU   B 1 12  ? 35.416 -32.579 -13.543 1.00 17.98 ?  12  LEU   B CD2  1 
ATOM   4145 H  H    . LEU   B 1 12  ? 34.891 -29.033 -15.249 1.00 22.38 ?  12  LEU   B H    1 
ATOM   4146 H  HA   . LEU   B 1 12  ? 33.533 -31.362 -15.078 1.00 21.79 ?  12  LEU   B HA   1 
ATOM   4147 H  HB2  . LEU   B 1 12  ? 34.129 -29.554 -12.998 1.00 21.30 ?  12  LEU   B HB2  1 
ATOM   4148 H  HB3  . LEU   B 1 12  ? 33.395 -30.941 -12.790 1.00 21.30 ?  12  LEU   B HB3  1 
ATOM   4149 H  HG   . LEU   B 1 12  ? 36.101 -30.657 -13.512 1.00 21.05 ?  12  LEU   B HG   1 
ATOM   4150 H  HD11 . LEU   B 1 12  ? 36.605 -31.525 -11.414 1.00 21.07 ?  12  LEU   B HD11 1 
ATOM   4151 H  HD12 . LEU   B 1 12  ? 35.790 -30.169 -11.270 1.00 21.07 ?  12  LEU   B HD12 1 
ATOM   4152 H  HD13 . LEU   B 1 12  ? 35.057 -31.562 -11.059 1.00 21.07 ?  12  LEU   B HD13 1 
ATOM   4153 H  HD21 . LEU   B 1 12  ? 36.224 -33.016 -13.237 1.00 21.63 ?  12  LEU   B HD21 1 
ATOM   4154 H  HD22 . LEU   B 1 12  ? 34.636 -33.038 -13.196 1.00 21.63 ?  12  LEU   B HD22 1 
ATOM   4155 H  HD23 . LEU   B 1 12  ? 35.390 -32.570 -14.514 1.00 21.63 ?  12  LEU   B HD23 1 
ATOM   4156 N  N    . THR   B 1 13  ? 32.126 -28.519 -14.741 1.00 17.64 ?  13  THR   B N    1 
ATOM   4157 C  CA   . THR   B 1 13  ? 30.902 -27.765 -14.944 1.00 17.59 ?  13  THR   B CA   1 
ATOM   4158 C  C    . THR   B 1 13  ? 31.240 -26.569 -15.828 1.00 19.82 ?  13  THR   B C    1 
ATOM   4159 O  O    . THR   B 1 13  ? 32.388 -26.379 -16.247 1.00 20.66 ?  13  THR   B O    1 
ATOM   4160 C  CB   . THR   B 1 13  ? 30.308 -27.286 -13.615 1.00 17.42 ?  13  THR   B CB   1 
ATOM   4161 O  OG1  . THR   B 1 13  ? 31.155 -26.268 -13.067 1.00 17.27 ?  13  THR   B OG1  1 
ATOM   4162 C  CG2  . THR   B 1 13  ? 30.184 -28.436 -12.622 1.00 17.97 ?  13  THR   B CG2  1 
ATOM   4163 H  H    . THR   B 1 13  ? 32.794 -28.016 -14.529 1.00 21.22 ?  13  THR   B H    1 
ATOM   4164 H  HA   . THR   B 1 13  ? 30.246 -28.321 -15.393 1.00 21.15 ?  13  THR   B HA   1 
ATOM   4165 H  HB   . THR   B 1 13  ? 29.419 -26.917 -13.772 1.00 20.95 ?  13  THR   B HB   1 
ATOM   4166 H  HG1  . THR   B 1 13  ? 30.845 -25.505 -13.256 1.00 20.77 ?  13  THR   B HG1  1 
ATOM   4167 H  HG21 . THR   B 1 13  ? 29.687 -28.150 -11.840 1.00 21.61 ?  13  THR   B HG21 1 
ATOM   4168 H  HG22 . THR   B 1 13  ? 29.719 -29.182 -13.035 1.00 21.61 ?  13  THR   B HG22 1 
ATOM   4169 H  HG23 . THR   B 1 13  ? 31.066 -28.731 -12.346 1.00 21.61 ?  13  THR   B HG23 1 
ATOM   4170 N  N    A ASP   B 1 14  ? 30.229 -25.746 -16.101 0.72 20.78 ?  14  ASP   B N    1 
ATOM   4171 N  N    B ASP   B 1 14  ? 30.232 -25.733 -16.090 0.28 20.63 ?  14  ASP   B N    1 
ATOM   4172 C  CA   A ASP   B 1 14  ? 30.448 -24.588 -16.959 0.72 22.34 ?  14  ASP   B CA   1 
ATOM   4173 C  CA   B ASP   B 1 14  ? 30.436 -24.579 -16.960 0.28 21.52 ?  14  ASP   B CA   1 
ATOM   4174 C  C    A ASP   B 1 14  ? 31.547 -23.681 -16.419 0.72 20.51 ?  14  ASP   B C    1 
ATOM   4175 C  C    B ASP   B 1 14  ? 31.429 -23.577 -16.390 0.28 19.78 ?  14  ASP   B C    1 
ATOM   4176 O  O    A ASP   B 1 14  ? 32.215 -22.993 -17.200 0.72 21.80 ?  14  ASP   B O    1 
ATOM   4177 O  O    B ASP   B 1 14  ? 31.877 -22.689 -17.125 0.28 19.96 ?  14  ASP   B O    1 
ATOM   4178 C  CB   A ASP   B 1 14  ? 29.147 -23.806 -17.136 0.72 25.85 ?  14  ASP   B CB   1 
ATOM   4179 C  CB   B ASP   B 1 14  ? 29.112 -23.864 -17.226 0.28 24.06 ?  14  ASP   B CB   1 
ATOM   4180 C  CG   A ASP   B 1 14  ? 28.175 -24.491 -18.070 0.72 29.30 ?  14  ASP   B CG   1 
ATOM   4181 C  CG   B ASP   B 1 14  ? 28.236 -24.613 -18.213 0.28 26.31 ?  14  ASP   B CG   1 
ATOM   4182 O  OD1  A ASP   B 1 14  ? 28.550 -25.498 -18.712 0.72 30.43 ?  14  ASP   B OD1  1 
ATOM   4183 O  OD1  B ASP   B 1 14  ? 28.792 -25.299 -19.097 0.28 27.04 ?  14  ASP   B OD1  1 
ATOM   4184 O  OD2  A ASP   B 1 14  ? 27.023 -24.019 -18.157 0.72 30.69 -1 14  ASP   B OD2  1 
ATOM   4185 O  OD2  B ASP   B 1 14  ? 26.995 -24.522 -18.105 0.28 27.08 -1 14  ASP   B OD2  1 
ATOM   4186 H  H    A ASP   B 1 14  ? 29.426 -25.825 -15.802 0.72 24.99 ?  14  ASP   B H    1 
ATOM   4187 H  H    B ASP   B 1 14  ? 29.433 -25.808 -15.781 0.28 24.80 ?  14  ASP   B H    1 
ATOM   4188 H  HA   A ASP   B 1 14  ? 30.733 -24.889 -17.830 0.72 26.85 ?  14  ASP   B HA   1 
ATOM   4189 H  HA   B ASP   B 1 14  ? 30.781 -24.889 -17.811 0.28 25.87 ?  14  ASP   B HA   1 
ATOM   4190 H  HB2  A ASP   B 1 14  ? 28.703 -23.720 -16.281 0.72 31.07 ?  14  ASP   B HB2  1 
ATOM   4191 H  HB2  B ASP   B 1 14  ? 28.627 -23.780 -16.390 0.28 28.92 ?  14  ASP   B HB2  1 
ATOM   4192 H  HB3  A ASP   B 1 14  ? 29.345 -22.929 -17.501 0.72 31.07 ?  14  ASP   B HB3  1 
ATOM   4193 H  HB3  B ASP   B 1 14  ? 29.303 -22.977 -17.584 0.28 28.92 ?  14  ASP   B HB3  1 
ATOM   4194 N  N    . ASN   B 1 15  ? 31.759 -23.668 -15.099 1.00 18.08 ?  15  ASN   B N    1 
ATOM   4195 C  CA   . ASN   B 1 15  ? 32.724 -22.755 -14.492 1.00 15.76 ?  15  ASN   B CA   1 
ATOM   4196 C  C    . ASN   B 1 15  ? 33.817 -23.414 -13.659 1.00 14.45 ?  15  ASN   B C    1 
ATOM   4197 O  O    . ASN   B 1 15  ? 34.668 -22.689 -13.130 1.00 14.84 ?  15  ASN   B O    1 
ATOM   4198 C  CB   . ASN   B 1 15  ? 32.013 -21.704 -13.622 1.00 15.97 ?  15  ASN   B CB   1 
ATOM   4199 C  CG   . ASN   B 1 15  ? 31.395 -22.308 -12.383 1.00 15.69 ?  15  ASN   B CG   1 
ATOM   4200 O  OD1  . ASN   B 1 15  ? 30.454 -23.104 -12.474 1.00 17.27 ?  15  ASN   B OD1  1 
ATOM   4201 N  ND2  . ASN   B 1 15  ? 31.918 -21.958 -11.220 1.00 14.60 ?  15  ASN   B ND2  1 
ATOM   4202 H  H    A ASN   B 1 15  ? 31.351 -24.176 -14.536 0.72 21.75 ?  15  ASN   B H    1 
ATOM   4203 H  H    B ASN   B 1 15  ? 31.405 -24.226 -14.547 0.28 21.75 ?  15  ASN   B H    1 
ATOM   4204 H  HA   . ASN   B 1 15  ? 33.169 -22.266 -15.194 1.00 18.96 ?  15  ASN   B HA   1 
ATOM   4205 H  HB2  . ASN   B 1 15  ? 32.660 -21.027 -13.342 1.00 19.21 ?  15  ASN   B HB2  1 
ATOM   4206 H  HB3  . ASN   B 1 15  ? 31.304 -21.278 -14.134 1.00 19.21 ?  15  ASN   B HB3  1 
ATOM   4207 H  HD21 . ASN   B 1 15  ? 31.601 -22.275 -10.484 1.00 17.56 ?  15  ASN   B HD21 1 
ATOM   4208 H  HD22 . ASN   B 1 15  ? 32.584 -21.403 -11.187 1.00 17.56 ?  15  ASN   B HD22 1 
ATOM   4209 N  N    . VAL   B 1 16  ? 33.825 -24.738 -13.510 1.00 14.29 ?  16  VAL   B N    1 
ATOM   4210 C  CA   . VAL   B 1 16  ? 34.826 -25.428 -12.700 1.00 14.09 ?  16  VAL   B CA   1 
ATOM   4211 C  C    . VAL   B 1 16  ? 35.619 -26.362 -13.598 1.00 14.16 ?  16  VAL   B C    1 
ATOM   4212 O  O    . VAL   B 1 16  ? 35.045 -27.249 -14.250 1.00 15.07 ?  16  VAL   B O    1 
ATOM   4213 C  CB   . VAL   B 1 16  ? 34.204 -26.196 -11.525 1.00 14.53 ?  16  VAL   B CB   1 
ATOM   4214 C  CG1  . VAL   B 1 16  ? 35.291 -26.923 -10.736 1.00 14.62 ?  16  VAL   B CG1  1 
ATOM   4215 C  CG2  . VAL   B 1 16  ? 33.409 -25.250 -10.627 1.00 15.37 ?  16  VAL   B CG2  1 
ATOM   4216 H  H    . VAL   B 1 16  ? 33.242 -25.265 -13.869 1.00 17.20 ?  16  VAL   B H    1 
ATOM   4217 H  HA   . VAL   B 1 16  ? 35.434 -24.772 -12.332 1.00 16.95 ?  16  VAL   B HA   1 
ATOM   4218 H  HB   . VAL   B 1 16  ? 33.586 -26.861 -11.872 1.00 17.49 ?  16  VAL   B HB   1 
ATOM   4219 H  HG11 . VAL   B 1 16  ? 34.919 -27.214 -9.888  1.00 17.59 ?  16  VAL   B HG11 1 
ATOM   4220 H  HG12 . VAL   B 1 16  ? 35.593 -27.687 -11.246 1.00 17.59 ?  16  VAL   B HG12 1 
ATOM   4221 H  HG13 . VAL   B 1 16  ? 36.025 -26.309 -10.580 1.00 17.59 ?  16  VAL   B HG13 1 
ATOM   4222 H  HG21 . VAL   B 1 16  ? 33.067 -25.749 -9.867  1.00 18.49 ?  16  VAL   B HG21 1 
ATOM   4223 H  HG22 . VAL   B 1 16  ? 33.989 -24.539 -10.323 1.00 18.49 ?  16  VAL   B HG22 1 
ATOM   4224 H  HG23 . VAL   B 1 16  ? 32.667 -24.879 -11.134 1.00 18.49 ?  16  VAL   B HG23 1 
ATOM   4225 N  N    . TYR   B 1 17  ? 36.940 -26.187 -13.586 1.00 14.75 ?  17  TYR   B N    1 
ATOM   4226 C  CA   . TYR   B 1 17  ? 37.882 -26.942 -14.396 1.00 15.22 ?  17  TYR   B CA   1 
ATOM   4227 C  C    . TYR   B 1 17  ? 38.931 -27.554 -13.480 1.00 13.95 ?  17  TYR   B C    1 
ATOM   4228 O  O    . TYR   B 1 17  ? 39.216 -27.017 -12.406 1.00 14.27 ?  17  TYR   B O    1 
ATOM   4229 C  CB   . TYR   B 1 17  ? 38.591 -26.018 -15.395 1.00 17.88 ?  17  TYR   B CB   1 
ATOM   4230 C  CG   . TYR   B 1 17  ? 37.667 -25.247 -16.303 1.00 20.96 ?  17  TYR   B CG   1 
ATOM   4231 C  CD1  . TYR   B 1 17  ? 37.096 -24.048 -15.896 1.00 22.36 ?  17  TYR   B CD1  1 
ATOM   4232 C  CD2  . TYR   B 1 17  ? 37.366 -25.719 -17.572 1.00 23.07 ?  17  TYR   B CD2  1 
ATOM   4233 C  CE1  . TYR   B 1 17  ? 36.249 -23.339 -16.730 1.00 24.15 ?  17  TYR   B CE1  1 
ATOM   4234 C  CE2  . TYR   B 1 17  ? 36.524 -25.020 -18.413 1.00 24.78 ?  17  TYR   B CE2  1 
ATOM   4235 C  CZ   . TYR   B 1 17  ? 35.966 -23.833 -17.985 1.00 25.32 ?  17  TYR   B CZ   1 
ATOM   4236 O  OH   . TYR   B 1 17  ? 35.128 -23.133 -18.819 1.00 26.54 ?  17  TYR   B OH   1 
ATOM   4237 H  H    . TYR   B 1 17  ? 37.331 -25.599 -13.089 1.00 17.74 ?  17  TYR   B H    1 
ATOM   4238 H  HA   . TYR   B 1 17  ? 37.418 -27.648 -14.878 1.00 18.31 ?  17  TYR   B HA   1 
ATOM   4239 H  HB2  . TYR   B 1 17  ? 39.131 -25.380 -14.906 1.00 21.50 ?  17  TYR   B HB2  1 
ATOM   4240 H  HB3  . TYR   B 1 17  ? 39.153 -26.561 -15.961 1.00 21.50 ?  17  TYR   B HB3  1 
ATOM   4241 H  HD1  . TYR   B 1 17  ? 37.288 -23.715 -15.051 1.00 26.88 ?  17  TYR   B HD1  1 
ATOM   4242 H  HD2  . TYR   B 1 17  ? 37.736 -26.520 -17.864 1.00 27.74 ?  17  TYR   B HD2  1 
ATOM   4243 H  HE1  . TYR   B 1 17  ? 35.872 -22.535 -16.447 1.00 29.02 ?  17  TYR   B HE1  1 
ATOM   4244 H  HE2  . TYR   B 1 17  ? 36.325 -25.349 -19.262 1.00 29.78 ?  17  TYR   B HE2  1 
ATOM   4245 H  HH   . TYR   B 1 17  ? 35.033 -23.536 -19.551 1.00 31.90 ?  17  TYR   B HH   1 
ATOM   4246 N  N    . ILE   B 1 18  ? 39.539 -28.659 -13.910 1.00 14.25 ?  18  ILE   B N    1 
ATOM   4247 C  CA   . ILE   B 1 18  ? 40.470 -29.381 -13.049 1.00 14.19 ?  18  ILE   B CA   1 
ATOM   4248 C  C    . ILE   B 1 18  ? 41.628 -29.933 -13.873 1.00 14.66 ?  18  ILE   B C    1 
ATOM   4249 O  O    . ILE   B 1 18  ? 41.461 -30.327 -15.032 1.00 15.82 ?  18  ILE   B O    1 
ATOM   4250 C  CB   . ILE   B 1 18  ? 39.723 -30.481 -12.243 1.00 14.85 ?  18  ILE   B CB   1 
ATOM   4251 C  CG1  . ILE   B 1 18  ? 40.585 -31.024 -11.096 1.00 15.17 ?  18  ILE   B CG1  1 
ATOM   4252 C  CG2  . ILE   B 1 18  ? 39.213 -31.602 -13.163 1.00 15.36 ?  18  ILE   B CG2  1 
ATOM   4253 C  CD1  . ILE   B 1 18  ? 39.779 -31.843 -10.091 1.00 16.66 ?  18  ILE   B CD1  1 
ATOM   4254 H  H    . ILE   B 1 18  ? 39.428 -29.010 -14.687 1.00 17.14 ?  18  ILE   B H    1 
ATOM   4255 H  HA   . ILE   B 1 18  ? 40.836 -28.762 -12.402 1.00 17.08 ?  18  ILE   B HA   1 
ATOM   4256 H  HB   . ILE   B 1 18  ? 38.944 -30.073 -11.836 1.00 17.87 ?  18  ILE   B HB   1 
ATOM   4257 H  HG12 . ILE   B 1 18  ? 41.277 -31.592 -11.458 1.00 18.25 ?  18  ILE   B HG12 1 
ATOM   4258 H  HG13 . ILE   B 1 18  ? 40.980 -30.276 -10.620 1.00 18.25 ?  18  ILE   B HG13 1 
ATOM   4259 H  HG21 . ILE   B 1 18  ? 38.629 -32.188 -12.655 1.00 18.48 ?  18  ILE   B HG21 1 
ATOM   4260 H  HG22 . ILE   B 1 18  ? 38.719 -31.199 -13.894 1.00 18.48 ?  18  ILE   B HG22 1 
ATOM   4261 H  HG23 . ILE   B 1 18  ? 39.968 -32.100 -13.505 1.00 18.48 ?  18  ILE   B HG23 1 
ATOM   4262 H  HD11 . ILE   B 1 18  ? 40.362 -32.110 -9.361  1.00 20.04 ?  18  ILE   B HD11 1 
ATOM   4263 H  HD12 . ILE   B 1 18  ? 39.051 -31.301 -9.749  1.00 20.04 ?  18  ILE   B HD12 1 
ATOM   4264 H  HD13 . ILE   B 1 18  ? 39.426 -32.630 -10.534 1.00 20.04 ?  18  ILE   B HD13 1 
ATOM   4265 N  N    . LYS   B 1 19  ? 42.807 -29.980 -13.253 1.00 15.14 ?  19  LYS   B N    1 
ATOM   4266 C  CA   . LYS   B 1 19  ? 44.014 -30.450 -13.914 1.00 16.10 ?  19  LYS   B CA   1 
ATOM   4267 C  C    . LYS   B 1 19  ? 44.919 -31.129 -12.898 1.00 15.98 ?  19  LYS   B C    1 
ATOM   4268 O  O    . LYS   B 1 19  ? 45.013 -30.696 -11.746 1.00 15.33 ?  19  LYS   B O    1 
ATOM   4269 C  CB   . LYS   B 1 19  ? 44.774 -29.281 -14.555 1.00 17.75 ?  19  LYS   B CB   1 
ATOM   4270 C  CG   . LYS   B 1 19  ? 45.953 -29.682 -15.421 1.00 19.77 ?  19  LYS   B CG   1 
ATOM   4271 C  CD   . LYS   B 1 19  ? 46.679 -28.448 -15.945 1.00 21.72 ?  19  LYS   B CD   1 
ATOM   4272 C  CE   . LYS   B 1 19  ? 47.846 -28.821 -16.836 1.00 23.74 ?  19  LYS   B CE   1 
ATOM   4273 N  NZ   . LYS   B 1 19  ? 48.600 -27.628 -17.299 1.00 24.79 ?  19  LYS   B NZ   1 
ATOM   4274 H  H    . LYS   B 1 19  ? 42.924 -29.736 -12.432 1.00 18.21 ?  19  LYS   B H    1 
ATOM   4275 H  HA   . LYS   B 1 19  ? 43.773 -31.088 -14.604 1.00 19.36 ?  19  LYS   B HA   1 
ATOM   4276 H  HB2  . LYS   B 1 19  ? 44.155 -28.787 -15.114 1.00 21.34 ?  19  LYS   B HB2  1 
ATOM   4277 H  HB3  . LYS   B 1 19  ? 45.103 -28.705 -13.845 1.00 21.34 ?  19  LYS   B HB3  1 
ATOM   4278 H  HG2  . LYS   B 1 19  ? 46.572 -30.209 -14.895 1.00 23.78 ?  19  LYS   B HG2  1 
ATOM   4279 H  HG3  . LYS   B 1 19  ? 45.628 -30.198 -16.178 1.00 23.78 ?  19  LYS   B HG3  1 
ATOM   4280 H  HD2  . LYS   B 1 19  ? 46.058 -27.909 -16.460 1.00 26.11 ?  19  LYS   B HD2  1 
ATOM   4281 H  HD3  . LYS   B 1 19  ? 47.018 -27.938 -15.192 1.00 26.11 ?  19  LYS   B HD3  1 
ATOM   4282 H  HE2  . LYS   B 1 19  ? 48.452 -29.394 -16.340 1.00 28.53 ?  19  LYS   B HE2  1 
ATOM   4283 H  HE3  . LYS   B 1 19  ? 47.509 -29.292 -17.616 1.00 28.53 ?  19  LYS   B HE3  1 
ATOM   4284 H  HZ1  . LYS   B 1 19  ? 49.221 -27.871 -17.889 1.00 29.79 ?  19  LYS   B HZ1  1 
ATOM   4285 H  HZ2  . LYS   B 1 19  ? 48.046 -27.048 -17.685 1.00 29.79 ?  19  LYS   B HZ2  1 
ATOM   4286 H  HZ3  . LYS   B 1 19  ? 48.997 -27.233 -16.608 1.00 29.79 ?  19  LYS   B HZ3  1 
ATOM   4287 N  N    . ASN   B 1 20  ? 45.602 -32.181 -13.340 1.00 17.10 ?  20  ASN   B N    1 
ATOM   4288 C  CA   . ASN   B 1 20  ? 46.635 -32.811 -12.527 1.00 18.20 ?  20  ASN   B CA   1 
ATOM   4289 C  C    . ASN   B 1 20  ? 47.911 -31.993 -12.706 1.00 18.53 ?  20  ASN   B C    1 
ATOM   4290 O  O    . ASN   B 1 20  ? 48.548 -32.055 -13.764 1.00 20.46 ?  20  ASN   B O    1 
ATOM   4291 C  CB   . ASN   B 1 20  ? 46.806 -34.263 -12.971 1.00 20.03 ?  20  ASN   B CB   1 
ATOM   4292 C  CG   . ASN   B 1 20  ? 47.967 -34.969 -12.290 1.00 21.60 ?  20  ASN   B CG   1 
ATOM   4293 O  OD1  . ASN   B 1 20  ? 48.637 -35.803 -12.906 1.00 23.85 ?  20  ASN   B OD1  1 
ATOM   4294 N  ND2  . ASN   B 1 20  ? 48.204 -34.660 -11.026 1.00 21.16 ?  20  ASN   B ND2  1 
ATOM   4295 H  H    . ASN   B 1 20  ? 45.492 -32.537 -14.113 1.00 20.56 ?  20  ASN   B H    1 
ATOM   4296 H  HA   . ASN   B 1 20  ? 46.365 -32.799 -11.593 1.00 21.89 ?  20  ASN   B HA   1 
ATOM   4297 H  HB2  . ASN   B 1 20  ? 45.993 -34.755 -12.762 1.00 24.09 ?  20  ASN   B HB2  1 
ATOM   4298 H  HB3  . ASN   B 1 20  ? 46.962 -34.280 -13.927 1.00 24.09 ?  20  ASN   B HB3  1 
ATOM   4299 H  HD21 . ASN   B 1 20  ? 48.854 -35.033 -10.607 1.00 25.44 ?  20  ASN   B HD21 1 
ATOM   4300 H  HD22 . ASN   B 1 20  ? 47.716 -34.074 -10.623 1.00 25.44 ?  20  ASN   B HD22 1 
ATOM   4301 N  N    . ALA   B 1 21  ? 48.272 -31.204 -11.693 1.00 18.12 ?  21  ALA   B N    1 
ATOM   4302 C  CA   . ALA   B 1 21  ? 49.391 -30.289 -11.844 1.00 18.79 ?  21  ALA   B CA   1 
ATOM   4303 C  C    . ALA   B 1 21  ? 49.847 -29.780 -10.485 1.00 17.51 ?  21  ALA   B C    1 
ATOM   4304 O  O    . ALA   B 1 21  ? 49.104 -29.798 -9.500  1.00 17.26 ?  21  ALA   B O    1 
ATOM   4305 C  CB   . ALA   B 1 21  ? 49.014 -29.125 -12.757 1.00 20.19 ?  21  ALA   B CB   1 
ATOM   4306 H  H    . ALA   B 1 21  ? 47.885 -31.190 -10.921 1.00 21.79 ?  21  ALA   B H    1 
ATOM   4307 H  HA   . ALA   B 1 21  ? 50.129 -30.771 -12.248 1.00 22.60 ?  21  ALA   B HA   1 
ATOM   4308 H  HB1  . ALA   B 1 21  ? 49.806 -28.601 -12.916 1.00 24.27 ?  21  ALA   B HB1  1 
ATOM   4309 H  HB2  . ALA   B 1 21  ? 48.677 -29.488 -13.591 1.00 24.27 ?  21  ALA   B HB2  1 
ATOM   4310 H  HB3  . ALA   B 1 21  ? 48.330 -28.598 -12.322 1.00 24.27 ?  21  ALA   B HB3  1 
ATOM   4311 N  N    . ASP   B 1 22  ? 51.102 -29.333 -10.464 1.00 16.61 ?  22  ASP   B N    1 
ATOM   4312 C  CA   . ASP   B 1 22  ? 51.717 -28.644 -9.332  1.00 15.78 ?  22  ASP   B CA   1 
ATOM   4313 C  C    . ASP   B 1 22  ? 51.315 -27.172 -9.410  1.00 14.50 ?  22  ASP   B C    1 
ATOM   4314 O  O    . ASP   B 1 22  ? 51.617 -26.502 -10.401 1.00 14.55 ?  22  ASP   B O    1 
ATOM   4315 C  CB   . ASP   B 1 22  ? 53.233 -28.825 -9.488  1.00 17.29 ?  22  ASP   B CB   1 
ATOM   4316 C  CG   . ASP   B 1 22  ? 54.066 -28.060 -8.468  1.00 19.02 ?  22  ASP   B CG   1 
ATOM   4317 O  OD1  . ASP   B 1 22  ? 53.710 -26.938 -8.082  1.00 19.07 ?  22  ASP   B OD1  1 
ATOM   4318 O  OD2  . ASP   B 1 22  ? 55.137 -28.579 -8.084  1.00 21.56 -1 22  ASP   B OD2  1 
ATOM   4319 H  H    . ASP   B 1 22  ? 51.642 -29.426 -11.128 1.00 19.98 ?  22  ASP   B H    1 
ATOM   4320 H  HA   . ASP   B 1 22  ? 51.421 -29.031 -8.491  1.00 18.98 ?  22  ASP   B HA   1 
ATOM   4321 H  HB2  . ASP   B 1 22  ? 53.451 -29.760 -9.401  1.00 20.80 ?  22  ASP   B HB2  1 
ATOM   4322 H  HB3  . ASP   B 1 22  ? 53.496 -28.499 -10.362 1.00 20.80 ?  22  ASP   B HB3  1 
ATOM   4323 N  N    . ILE   B 1 23  ? 50.604 -26.681 -8.386  1.00 13.80 ?  23  ILE   B N    1 
ATOM   4324 C  CA   . ILE   B 1 23  ? 50.015 -25.340 -8.447  1.00 13.08 ?  23  ILE   B CA   1 
ATOM   4325 C  C    . ILE   B 1 23  ? 51.075 -24.252 -8.586  1.00 12.68 ?  23  ILE   B C    1 
ATOM   4326 O  O    . ILE   B 1 23  ? 50.814 -23.212 -9.196  1.00 12.30 ?  23  ILE   B O    1 
ATOM   4327 C  CB   . ILE   B 1 23  ? 49.082 -25.101 -7.246  1.00 13.40 ?  23  ILE   B CB   1 
ATOM   4328 C  CG1  . ILE   B 1 23  ? 48.256 -23.831 -7.448  1.00 14.24 ?  23  ILE   B CG1  1 
ATOM   4329 C  CG2  . ILE   B 1 23  ? 49.857 -25.058 -5.949  1.00 14.57 ?  23  ILE   B CG2  1 
ATOM   4330 C  CD1  . ILE   B 1 23  ? 47.128 -23.669 -6.441  1.00 14.80 ?  23  ILE   B CD1  1 
ATOM   4331 H  H    . ILE   B 1 23  ? 50.447 -27.106 -7.656  1.00 16.61 ?  23  ILE   B H    1 
ATOM   4332 H  HA   . ILE   B 1 23  ? 49.464 -25.297 -9.243  1.00 15.74 ?  23  ILE   B HA   1 
ATOM   4333 H  HB   . ILE   B 1 23  ? 48.462 -25.848 -7.201  1.00 16.13 ?  23  ILE   B HB   1 
ATOM   4334 H  HG12 . ILE   B 1 23  ? 48.844 -23.061 -7.364  1.00 17.14 ?  23  ILE   B HG12 1 
ATOM   4335 H  HG13 . ILE   B 1 23  ? 47.867 -23.845 -8.339  1.00 17.14 ?  23  ILE   B HG13 1 
ATOM   4336 H  HG21 . ILE   B 1 23  ? 49.232 -25.060 -5.211  1.00 17.53 ?  23  ILE   B HG21 1 
ATOM   4337 H  HG22 . ILE   B 1 23  ? 50.430 -25.838 -5.903  1.00 17.53 ?  23  ILE   B HG22 1 
ATOM   4338 H  HG23 . ILE   B 1 23  ? 50.393 -24.251 -5.932  1.00 17.53 ?  23  ILE   B HG23 1 
ATOM   4339 H  HD11 . ILE   B 1 23  ? 46.609 -22.885 -6.674  1.00 17.80 ?  23  ILE   B HD11 1 
ATOM   4340 H  HD12 . ILE   B 1 23  ? 46.565 -24.461 -6.478  1.00 17.80 ?  23  ILE   B HD12 1 
ATOM   4341 H  HD13 . ILE   B 1 23  ? 47.506 -23.572 -5.557  1.00 17.80 ?  23  ILE   B HD13 1 
ATOM   4342 N  N    . VAL   B 1 24  ? 52.269 -24.456 -8.025  1.00 13.06 ?  24  VAL   B N    1 
ATOM   4343 C  CA   . VAL   B 1 24  ? 53.346 -23.478 -8.193  1.00 13.61 ?  24  VAL   B CA   1 
ATOM   4344 C  C    . VAL   B 1 24  ? 53.796 -23.430 -9.646  1.00 13.91 ?  24  VAL   B C    1 
ATOM   4345 O  O    . VAL   B 1 24  ? 53.938 -22.353 -10.240 1.00 14.43 ?  24  VAL   B O    1 
ATOM   4346 C  CB   . VAL   B 1 24  ? 54.523 -23.799 -7.251  1.00 14.64 ?  24  VAL   B CB   1 
ATOM   4347 C  CG1  . VAL   B 1 24  ? 55.730 -22.914 -7.571  1.00 15.58 ?  24  VAL   B CG1  1 
ATOM   4348 C  CG2  . VAL   B 1 24  ? 54.108 -23.631 -5.808  1.00 15.84 ?  24  VAL   B CG2  1 
ATOM   4349 H  H    . VAL   B 1 24  ? 52.478 -25.140 -7.551  1.00 15.72 ?  24  VAL   B H    1 
ATOM   4350 H  HA   . VAL   B 1 24  ? 53.013 -22.601 -7.956  1.00 16.38 ?  24  VAL   B HA   1 
ATOM   4351 H  HB   . VAL   B 1 24  ? 54.789 -24.724 -7.376  1.00 17.62 ?  24  VAL   B HB   1 
ATOM   4352 H  HG11 . VAL   B 1 24  ? 56.325 -22.905 -6.805  1.00 18.74 ?  24  VAL   B HG11 1 
ATOM   4353 H  HG12 . VAL   B 1 24  ? 56.190 -23.277 -8.342  1.00 18.74 ?  24  VAL   B HG12 1 
ATOM   4354 H  HG13 . VAL   B 1 24  ? 55.419 -22.014 -7.757  1.00 18.74 ?  24  VAL   B HG13 1 
ATOM   4355 H  HG21 . VAL   B 1 24  ? 54.831 -23.920 -5.233  1.00 19.06 ?  24  VAL   B HG21 1 
ATOM   4356 H  HG22 . VAL   B 1 24  ? 53.906 -22.697 -5.646  1.00 19.06 ?  24  VAL   B HG22 1 
ATOM   4357 H  HG23 . VAL   B 1 24  ? 53.318 -24.173 -5.642  1.00 19.06 ?  24  VAL   B HG23 1 
ATOM   4358 N  N    . GLU   B 1 25  ? 54.054 -24.600 -10.236 1.00 14.59 ?  25  GLU   B N    1 
ATOM   4359 C  CA   . GLU   B 1 25  ? 54.451 -24.632 -11.638 1.00 16.27 ?  25  GLU   B CA   1 
ATOM   4360 C  C    . GLU   B 1 25  ? 53.343 -24.087 -12.523 1.00 15.16 ?  25  GLU   B C    1 
ATOM   4361 O  O    . GLU   B 1 25  ? 53.606 -23.371 -13.498 1.00 15.97 ?  25  GLU   B O    1 
ATOM   4362 C  CB   . GLU   B 1 25  ? 54.845 -26.052 -12.039 1.00 20.52 ?  25  GLU   B CB   1 
ATOM   4363 C  CG   . GLU   B 1 25  ? 56.134 -26.514 -11.373 1.00 26.37 ?  25  GLU   B CG   1 
ATOM   4364 C  CD   . GLU   B 1 25  ? 57.260 -25.492 -11.473 1.00 31.72 ?  25  GLU   B CD   1 
ATOM   4365 O  OE1  . GLU   B 1 25  ? 57.647 -25.137 -12.606 1.00 33.74 ?  25  GLU   B OE1  1 
ATOM   4366 O  OE2  . GLU   B 1 25  ? 57.746 -25.028 -10.415 1.00 33.52 -1 25  GLU   B OE2  1 
ATOM   4367 H  H    . GLU   B 1 25  ? 54.007 -25.370 -9.851  1.00 17.55 ?  25  GLU   B H    1 
ATOM   4368 H  HA   . GLU   B 1 25  ? 55.211 -24.049 -11.758 1.00 19.58 ?  25  GLU   B HA   1 
ATOM   4369 H  HB2  . GLU   B 1 25  ? 54.139 -26.666 -11.777 1.00 24.67 ?  25  GLU   B HB2  1 
ATOM   4370 H  HB3  . GLU   B 1 25  ? 54.973 -26.086 -13.000 1.00 24.67 ?  25  GLU   B HB3  1 
ATOM   4371 H  HG2  . GLU   B 1 25  ? 55.967 -26.667 -10.435 1.00 31.69 ?  25  GLU   B HG2  1 
ATOM   4372 H  HG3  . GLU   B 1 25  ? 56.436 -27.327 -11.804 1.00 31.69 ?  25  GLU   B HG3  1 
ATOM   4373 N  N    A GLU   B 1 26  ? 52.092 -24.406 -12.191 0.72 14.21 ?  26  GLU   B N    1 
ATOM   4374 N  N    B GLU   B 1 26  ? 52.090 -24.406 -12.193 0.28 14.93 ?  26  GLU   B N    1 
ATOM   4375 C  CA   A GLU   B 1 26  ? 50.965 -23.882 -12.953 0.72 14.70 ?  26  GLU   B CA   1 
ATOM   4376 C  CA   B GLU   B 1 26  ? 50.965 -23.878 -12.958 0.28 15.26 ?  26  GLU   B CA   1 
ATOM   4377 C  C    A GLU   B 1 26  ? 50.915 -22.364 -12.875 0.72 13.50 ?  26  GLU   B C    1 
ATOM   4378 C  C    B GLU   B 1 26  ? 50.917 -22.361 -12.877 0.28 14.02 ?  26  GLU   B C    1 
ATOM   4379 O  O    A GLU   B 1 26  ? 50.724 -21.690 -13.892 0.72 14.92 ?  26  GLU   B O    1 
ATOM   4380 O  O    B GLU   B 1 26  ? 50.743 -21.680 -13.894 0.28 14.66 ?  26  GLU   B O    1 
ATOM   4381 C  CB   A GLU   B 1 26  ? 49.656 -24.472 -12.429 0.72 16.87 ?  26  GLU   B CB   1 
ATOM   4382 C  CB   B GLU   B 1 26  ? 49.654 -24.477 -12.450 0.28 16.93 ?  26  GLU   B CB   1 
ATOM   4383 C  CG   A GLU   B 1 26  ? 49.232 -25.759 -13.104 0.72 20.62 ?  26  GLU   B CG   1 
ATOM   4384 C  CG   B GLU   B 1 26  ? 49.261 -25.771 -13.129 0.28 19.12 ?  26  GLU   B CG   1 
ATOM   4385 C  CD   A GLU   B 1 26  ? 48.956 -25.587 -14.599 0.72 22.59 ?  26  GLU   B CD   1 
ATOM   4386 C  CD   B GLU   B 1 26  ? 49.011 -25.625 -14.620 0.28 20.48 ?  26  GLU   B CD   1 
ATOM   4387 O  OE1  A GLU   B 1 26  ? 47.941 -24.964 -14.985 0.72 22.83 ?  26  GLU   B OE1  1 
ATOM   4388 O  OE1  B GLU   B 1 26  ? 48.124 -24.842 -15.016 0.28 20.50 ?  26  GLU   B OE1  1 
ATOM   4389 O  OE2  A GLU   B 1 26  ? 49.767 -26.086 -15.392 0.72 24.64 -1 26  GLU   B OE2  1 
ATOM   4390 O  OE2  B GLU   B 1 26  ? 49.703 -26.311 -15.397 0.28 21.78 -1 26  GLU   B OE2  1 
ATOM   4391 H  H    A GLU   B 1 26  ? 51.868 -24.925 -11.538 0.72 17.10 ?  26  GLU   B H    1 
ATOM   4392 H  H    B GLU   B 1 26  ? 51.865 -24.922 -11.539 0.28 17.97 ?  26  GLU   B H    1 
ATOM   4393 H  HA   A GLU   B 1 26  ? 51.062 -24.132 -13.882 0.72 17.69 ?  26  GLU   B HA   1 
ATOM   4394 H  HA   B GLU   B 1 26  ? 51.072 -24.124 -13.887 0.28 18.36 ?  26  GLU   B HA   1 
ATOM   4395 H  HB2  A GLU   B 1 26  ? 49.751 -24.653 -11.480 0.72 20.30 ?  26  GLU   B HB2  1 
ATOM   4396 H  HB2  B GLU   B 1 26  ? 49.741 -24.660 -11.498 0.28 20.36 ?  26  GLU   B HB2  1 
ATOM   4397 H  HB3  A GLU   B 1 26  ? 48.944 -23.824 -12.565 0.72 20.30 ?  26  GLU   B HB3  1 
ATOM   4398 H  HB3  B GLU   B 1 26  ? 48.940 -23.837 -12.592 0.28 20.36 ?  26  GLU   B HB3  1 
ATOM   4399 H  HG2  A GLU   B 1 26  ? 49.944 -26.406 -12.993 0.72 24.79 ?  26  GLU   B HG2  1 
ATOM   4400 H  HG2  B GLU   B 1 26  ? 49.979 -26.404 -13.017 0.28 23.00 ?  26  GLU   B HG2  1 
ATOM   4401 H  HG3  A GLU   B 1 26  ? 48.421 -26.078 -12.680 0.72 24.79 ?  26  GLU   B HG3  1 
ATOM   4402 H  HG3  B GLU   B 1 26  ? 48.447 -26.100 -12.723 0.28 23.00 ?  26  GLU   B HG3  1 
ATOM   4403 N  N    . ALA   B 1 27  ? 51.059 -21.812 -11.670 1.00 12.90 ?  27  ALA   B N    1 
ATOM   4404 C  CA   . ALA   B 1 27  ? 51.023 -20.364 -11.519 1.00 13.39 ?  27  ALA   B CA   1 
ATOM   4405 C  C    . ALA   B 1 27  ? 52.097 -19.700 -12.372 1.00 14.56 ?  27  ALA   B C    1 
ATOM   4406 O  O    . ALA   B 1 27  ? 51.840 -18.691 -13.045 1.00 15.38 ?  27  ALA   B O    1 
ATOM   4407 C  CB   . ALA   B 1 27  ? 51.172 -19.990 -10.043 1.00 13.58 ?  27  ALA   B CB   1 
ATOM   4408 H  H    A ALA   B 1 27  ? 51.172 -22.248 -10.936 0.72 15.52 ?  27  ALA   B H    1 
ATOM   4409 H  H    B ALA   B 1 27  ? 51.176 -22.249 -10.937 0.28 15.52 ?  27  ALA   B H    1 
ATOM   4410 H  HA   . ALA   B 1 27  ? 50.164 -20.033 -11.818 1.00 16.11 ?  27  ALA   B HA   1 
ATOM   4411 H  HB1  . ALA   B 1 27  ? 51.139 -19.023 -9.956  1.00 16.35 ?  27  ALA   B HB1  1 
ATOM   4412 H  HB2  . ALA   B 1 27  ? 50.438 -20.387 -9.544  1.00 16.35 ?  27  ALA   B HB2  1 
ATOM   4413 H  HB3  . ALA   B 1 27  ? 52.016 -20.325 -9.713  1.00 16.35 ?  27  ALA   B HB3  1 
ATOM   4414 N  N    . LYS   B 1 28  ? 53.308 -20.255 -12.370 1.00 16.24 ?  28  LYS   B N    1 
ATOM   4415 C  CA   . LYS   B 1 28  ? 54.384 -19.635 -13.134 1.00 18.32 ?  28  LYS   B CA   1 
ATOM   4416 C  C    . LYS   B 1 28  ? 54.128 -19.710 -14.632 1.00 19.27 ?  28  LYS   B C    1 
ATOM   4417 O  O    . LYS   B 1 28  ? 54.531 -18.803 -15.370 1.00 20.29 ?  28  LYS   B O    1 
ATOM   4418 C  CB   . LYS   B 1 28  ? 55.737 -20.240 -12.747 1.00 21.37 ?  28  LYS   B CB   1 
ATOM   4419 C  CG   . LYS   B 1 28  ? 56.145 -19.888 -11.321 1.00 25.05 ?  28  LYS   B CG   1 
ATOM   4420 C  CD   . LYS   B 1 28  ? 57.574 -20.292 -10.989 1.00 29.82 ?  28  LYS   B CD   1 
ATOM   4421 C  CE   . LYS   B 1 28  ? 57.677 -21.758 -10.645 1.00 33.20 ?  28  LYS   B CE   1 
ATOM   4422 N  NZ   . LYS   B 1 28  ? 59.040 -22.103 -10.149 1.00 35.54 ?  28  LYS   B NZ   1 
ATOM   4423 H  H    . LYS   B 1 28  ? 53.524 -20.971 -11.947 1.00 19.53 ?  28  LYS   B H    1 
ATOM   4424 H  HA   . LYS   B 1 28  ? 54.418 -18.696 -12.906 1.00 22.03 ?  28  LYS   B HA   1 
ATOM   4425 H  HB2  . LYS   B 1 28  ? 55.691 -21.205 -12.812 1.00 25.69 ?  28  LYS   B HB2  1 
ATOM   4426 H  HB3  . LYS   B 1 28  ? 56.423 -19.899 -13.344 1.00 25.69 ?  28  LYS   B HB3  1 
ATOM   4427 H  HG2  . LYS   B 1 28  ? 56.068 -18.926 -11.205 1.00 30.11 ?  28  LYS   B HG2  1 
ATOM   4428 H  HG3  . LYS   B 1 28  ? 55.551 -20.343 -10.706 1.00 30.11 ?  28  LYS   B HG3  1 
ATOM   4429 H  HD2  . LYS   B 1 28  ? 58.140 -20.117 -11.757 1.00 35.83 ?  28  LYS   B HD2  1 
ATOM   4430 H  HD3  . LYS   B 1 28  ? 57.878 -19.776 -10.226 1.00 35.83 ?  28  LYS   B HD3  1 
ATOM   4431 H  HE2  . LYS   B 1 28  ? 57.035 -21.969 -9.949  1.00 39.88 ?  28  LYS   B HE2  1 
ATOM   4432 H  HE3  . LYS   B 1 28  ? 57.498 -22.287 -11.438 1.00 39.88 ?  28  LYS   B HE3  1 
ATOM   4433 H  HZ1  . LYS   B 1 28  ? 59.081 -22.970 -9.951  1.00 42.70 ?  28  LYS   B HZ1  1 
ATOM   4434 H  HZ2  . LYS   B 1 28  ? 59.647 -21.919 -10.773 1.00 42.70 ?  28  LYS   B HZ2  1 
ATOM   4435 H  HZ3  . LYS   B 1 28  ? 59.226 -21.631 -9.417  1.00 42.70 ?  28  LYS   B HZ3  1 
ATOM   4436 N  N    . LYS   B 1 29  ? 53.433 -20.749 -15.097 1.00 20.37 ?  29  LYS   B N    1 
ATOM   4437 C  CA   . LYS   B 1 29  ? 53.154 -20.889 -16.523 1.00 23.23 ?  29  LYS   B CA   1 
ATOM   4438 C  C    . LYS   B 1 29  ? 51.900 -20.137 -16.962 1.00 21.92 ?  29  LYS   B C    1 
ATOM   4439 O  O    . LYS   B 1 29  ? 51.896 -19.525 -18.035 1.00 23.21 ?  29  LYS   B O    1 
ATOM   4440 C  CB   . LYS   B 1 29  ? 53.034 -22.370 -16.892 1.00 28.07 ?  29  LYS   B CB   1 
ATOM   4441 C  CG   . LYS   B 1 29  ? 52.903 -22.632 -18.383 1.00 32.50 ?  29  LYS   B CG   1 
ATOM   4442 C  CD   . LYS   B 1 29  ? 53.122 -24.105 -18.708 1.00 36.18 ?  29  LYS   B CD   1 
ATOM   4443 C  CE   . LYS   B 1 29  ? 52.012 -24.984 -18.149 1.00 38.74 ?  29  LYS   B CE   1 
ATOM   4444 N  NZ   . LYS   B 1 29  ? 52.252 -26.429 -18.433 1.00 39.97 ?  29  LYS   B NZ   1 
ATOM   4445 H  H    . LYS   B 1 29  ? 53.111 -21.387 -14.606 1.00 24.49 ?  29  LYS   B H    1 
ATOM   4446 H  HA   . LYS   B 1 29  ? 53.900 -20.525 -17.017 1.00 27.93 ?  29  LYS   B HA   1 
ATOM   4447 H  HB2  . LYS   B 1 29  ? 53.830 -22.833 -16.585 1.00 33.73 ?  29  LYS   B HB2  1 
ATOM   4448 H  HB3  . LYS   B 1 29  ? 52.251 -22.739 -16.461 1.00 33.73 ?  29  LYS   B HB3  1 
ATOM   4449 H  HG2  . LYS   B 1 29  ? 52.012 -22.385 -18.675 1.00 39.05 ?  29  LYS   B HG2  1 
ATOM   4450 H  HG3  . LYS   B 1 29  ? 53.570 -22.113 -18.861 1.00 39.05 ?  29  LYS   B HG3  1 
ATOM   4451 H  HD2  . LYS   B 1 29  ? 53.144 -24.220 -19.670 1.00 43.47 ?  29  LYS   B HD2  1 
ATOM   4452 H  HD3  . LYS   B 1 29  ? 53.962 -24.395 -18.317 1.00 43.47 ?  29  LYS   B HD3  1 
ATOM   4453 H  HE2  . LYS   B 1 29  ? 51.964 -24.871 -17.187 1.00 46.54 ?  29  LYS   B HE2  1 
ATOM   4454 H  HE3  . LYS   B 1 29  ? 51.169 -24.731 -18.558 1.00 46.54 ?  29  LYS   B HE3  1 
ATOM   4455 H  HZ1  . LYS   B 1 29  ? 51.589 -26.920 -18.097 1.00 48.01 ?  29  LYS   B HZ1  1 
ATOM   4456 H  HZ2  . LYS   B 1 29  ? 52.294 -26.564 -19.312 1.00 48.01 ?  29  LYS   B HZ2  1 
ATOM   4457 H  HZ3  . LYS   B 1 29  ? 53.019 -26.689 -18.063 1.00 48.01 ?  29  LYS   B HZ3  1 
ATOM   4458 N  N    . VAL   B 1 30  ? 50.836 -20.181 -16.155 1.00 19.98 ?  30  VAL   B N    1 
ATOM   4459 C  CA   . VAL   B 1 30  ? 49.546 -19.594 -16.529 1.00 20.24 ?  30  VAL   B CA   1 
ATOM   4460 C  C    . VAL   B 1 30  ? 49.544 -18.082 -16.375 1.00 19.41 ?  30  VAL   B C    1 
ATOM   4461 O  O    . VAL   B 1 30  ? 48.803 -17.376 -17.080 1.00 20.31 ?  30  VAL   B O    1 
ATOM   4462 C  CB   . VAL   B 1 30  ? 48.441 -20.222 -15.656 1.00 21.40 ?  30  VAL   B CB   1 
ATOM   4463 C  CG1  . VAL   B 1 30  ? 47.146 -19.417 -15.727 1.00 21.76 ?  30  VAL   B CG1  1 
ATOM   4464 C  CG2  . VAL   B 1 30  ? 48.210 -21.673 -16.049 1.00 22.12 ?  30  VAL   B CG2  1 
ATOM   4465 H  H    . VAL   B 1 30  ? 50.828 -20.571 -15.380 1.00 24.03 ?  30  VAL   B H    1 
ATOM   4466 H  HA   . VAL   B 1 30  ? 49.355 -19.813 -17.452 1.00 24.33 ?  30  VAL   B HA   1 
ATOM   4467 H  HB   . VAL   B 1 30  ? 48.732 -20.224 -14.731 1.00 25.73 ?  30  VAL   B HB   1 
ATOM   4468 H  HG11 . VAL   B 1 30  ? 46.408 -20.001 -15.487 1.00 26.16 ?  30  VAL   B HG11 1 
ATOM   4469 H  HG12 . VAL   B 1 30  ? 47.195 -18.681 -15.101 1.00 26.16 ?  30  VAL   B HG12 1 
ATOM   4470 H  HG13 . VAL   B 1 30  ? 47.020 -19.094 -16.627 1.00 26.16 ?  30  VAL   B HG13 1 
ATOM   4471 H  HG21 . VAL   B 1 30  ? 47.519 -22.052 -15.479 1.00 26.60 ?  30  VAL   B HG21 1 
ATOM   4472 H  HG22 . VAL   B 1 30  ? 47.924 -21.708 -16.976 1.00 26.60 ?  30  VAL   B HG22 1 
ATOM   4473 H  HG23 . VAL   B 1 30  ? 49.035 -22.167 -15.937 1.00 26.60 ?  30  VAL   B HG23 1 
ATOM   4474 N  N    . LYS   B 1 31  ? 50.324 -17.578 -15.433 1.00 19.00 ?  31  LYS   B N    1 
ATOM   4475 C  CA   . LYS   B 1 31  ? 50.353 -16.171 -15.063 1.00 19.28 ?  31  LYS   B CA   1 
ATOM   4476 C  C    . LYS   B 1 31  ? 48.955 -15.692 -14.677 1.00 16.78 ?  31  LYS   B C    1 
ATOM   4477 O  O    . LYS   B 1 31  ? 48.421 -14.769 -15.301 1.00 17.88 ?  31  LYS   B O    1 
ATOM   4478 C  CB   . LYS   B 1 31  ? 50.988 -15.346 -16.191 1.00 22.65 ?  31  LYS   B CB   1 
ATOM   4479 C  CG   . LYS   B 1 31  ? 52.418 -15.786 -16.502 1.00 26.18 ?  31  LYS   B CG   1 
ATOM   4480 C  CD   . LYS   B 1 31  ? 53.006 -15.032 -17.684 1.00 29.59 ?  31  LYS   B CD   1 
ATOM   4481 C  CE   . LYS   B 1 31  ? 54.501 -15.266 -17.808 1.00 31.86 ?  31  LYS   B CE   1 
ATOM   4482 N  NZ   . LYS   B 1 31  ? 55.206 -14.837 -16.569 1.00 33.15 ?  31  LYS   B NZ   1 
ATOM   4483 H  H    . LYS   B 1 31  ? 50.875 -18.066 -14.986 1.00 22.84 ?  31  LYS   B H    1 
ATOM   4484 H  HA   . LYS   B 1 31  ? 50.906 -16.087 -14.282 1.00 23.19 ?  31  LYS   B HA   1 
ATOM   4485 H  HB2  . LYS   B 1 31  ? 50.462 -15.449 -17.001 1.00 27.23 ?  31  LYS   B HB2  1 
ATOM   4486 H  HB3  . LYS   B 1 31  ? 51.011 -14.419 -15.922 1.00 27.23 ?  31  LYS   B HB3  1 
ATOM   4487 H  HG2  . LYS   B 1 31  ? 52.967 -15.622 -15.720 1.00 31.47 ?  31  LYS   B HG2  1 
ATOM   4488 H  HG3  . LYS   B 1 31  ? 52.417 -16.735 -16.714 1.00 31.47 ?  31  LYS   B HG3  1 
ATOM   4489 H  HD2  . LYS   B 1 31  ? 52.579 -15.341 -18.497 1.00 35.55 ?  31  LYS   B HD2  1 
ATOM   4490 H  HD3  . LYS   B 1 31  ? 52.853 -14.085 -17.559 1.00 35.55 ?  31  LYS   B HD3  1 
ATOM   4491 H  HE2  . LYS   B 1 31  ? 54.675 -16.212 -17.947 1.00 38.28 ?  31  LYS   B HE2  1 
ATOM   4492 H  HE3  . LYS   B 1 31  ? 54.849 -14.747 -18.552 1.00 38.28 ?  31  LYS   B HE3  1 
ATOM   4493 H  HZ1  . LYS   B 1 31  ? 56.085 -14.829 -16.705 1.00 39.83 ?  31  LYS   B HZ1  1 
ATOM   4494 H  HZ2  . LYS   B 1 31  ? 54.940 -14.020 -16.338 1.00 39.83 ?  31  LYS   B HZ2  1 
ATOM   4495 H  HZ3  . LYS   B 1 31  ? 55.021 -15.400 -15.904 1.00 39.83 ?  31  LYS   B HZ3  1 
ATOM   4496 N  N    . PRO   B 1 32  ? 48.342 -16.283 -13.647 1.00 14.71 ?  32  PRO   B N    1 
ATOM   4497 C  CA   . PRO   B 1 32  ? 46.963 -15.924 -13.294 1.00 13.62 ?  32  PRO   B CA   1 
ATOM   4498 C  C    . PRO   B 1 32  ? 46.885 -14.582 -12.584 1.00 13.74 ?  32  PRO   B C    1 
ATOM   4499 O  O    . PRO   B 1 32  ? 47.808 -14.167 -11.878 1.00 15.25 ?  32  PRO   B O    1 
ATOM   4500 C  CB   . PRO   B 1 32  ? 46.561 -17.044 -12.327 1.00 13.70 ?  32  PRO   B CB   1 
ATOM   4501 C  CG   . PRO   B 1 32  ? 47.862 -17.379 -11.638 1.00 14.09 ?  32  PRO   B CG   1 
ATOM   4502 C  CD   . PRO   B 1 32  ? 48.916 -17.263 -12.701 1.00 14.44 ?  32  PRO   B CD   1 
ATOM   4503 H  HA   . PRO   B 1 32  ? 46.384 -15.931 -14.076 1.00 16.39 ?  32  PRO   B HA   1 
ATOM   4504 H  HB2  . PRO   B 1 32  ? 45.902 -16.714 -11.695 1.00 16.48 ?  32  PRO   B HB2  1 
ATOM   4505 H  HB3  . PRO   B 1 32  ? 46.221 -17.804 -12.824 1.00 16.48 ?  32  PRO   B HB3  1 
ATOM   4506 H  HG2  . PRO   B 1 32  ? 48.027 -16.741 -10.922 1.00 16.95 ?  32  PRO   B HG2  1 
ATOM   4507 H  HG3  . PRO   B 1 32  ? 47.827 -18.281 -11.291 1.00 16.95 ?  32  PRO   B HG3  1 
ATOM   4508 H  HD2  . PRO   B 1 32  ? 49.739 -16.916 -12.325 1.00 17.38 ?  32  PRO   B HD2  1 
ATOM   4509 H  HD3  . PRO   B 1 32  ? 49.048 -18.112 -13.139 1.00 17.38 ?  32  PRO   B HD3  1 
ATOM   4510 N  N    . THR   B 1 33  ? 45.736 -13.919 -12.751 1.00 13.37 ?  33  THR   B N    1 
ATOM   4511 C  CA   . THR   B 1 33  ? 45.448 -12.742 -11.940 1.00 13.54 ?  33  THR   B CA   1 
ATOM   4512 C  C    . THR   B 1 33  ? 45.403 -13.098 -10.458 1.00 13.14 ?  33  THR   B C    1 
ATOM   4513 O  O    . THR   B 1 33  ? 45.878 -12.324 -9.615  1.00 14.15 ?  33  THR   B O    1 
ATOM   4514 C  CB   . THR   B 1 33  ? 44.128 -12.101 -12.383 1.00 14.41 ?  33  THR   B CB   1 
ATOM   4515 O  OG1  . THR   B 1 33  ? 44.164 -11.850 -13.791 1.00 14.33 ?  33  THR   B OG1  1 
ATOM   4516 C  CG2  . THR   B 1 33  ? 43.885 -10.799 -11.640 1.00 15.70 ?  33  THR   B CG2  1 
ATOM   4517 H  H    . THR   B 1 33  ? 45.115 -14.132 -13.315 1.00 16.09 ?  33  THR   B H    1 
ATOM   4518 H  HA   . THR   B 1 33  ? 46.152 -12.092 -12.072 1.00 16.29 ?  33  THR   B HA   1 
ATOM   4519 H  HB   . THR   B 1 33  ? 43.394 -12.708 -12.184 1.00 17.34 ?  33  THR   B HB   1 
ATOM   4520 H  HG1  . THR   B 1 33  ? 43.443 -11.487 -14.038 1.00 17.24 ?  33  THR   B HG1  1 
ATOM   4521 H  HG21 . THR   B 1 33  ? 43.128 -10.337 -12.021 1.00 18.89 ?  33  THR   B HG21 1 
ATOM   4522 H  HG22 . THR   B 1 33  ? 43.710 -10.979 -10.702 1.00 18.89 ?  33  THR   B HG22 1 
ATOM   4523 H  HG23 . THR   B 1 33  ? 44.671 -10.232 -11.708 1.00 18.89 ?  33  THR   B HG23 1 
ATOM   4524 N  N    . VAL   B 1 34  ? 44.846 -14.267 -10.120 1.00 12.28 ?  34  VAL   B N    1 
ATOM   4525 C  CA   . VAL   B 1 34  ? 44.650 -14.667 -8.728  1.00 11.78 ?  34  VAL   B CA   1 
ATOM   4526 C  C    . VAL   B 1 34  ? 45.074 -16.117 -8.557  1.00 10.86 ?  34  VAL   B C    1 
ATOM   4527 O  O    . VAL   B 1 34  ? 44.553 -17.004 -9.242  1.00 11.65 ?  34  VAL   B O    1 
ATOM   4528 C  CB   . VAL   B 1 34  ? 43.180 -14.521 -8.283  1.00 13.23 ?  34  VAL   B CB   1 
ATOM   4529 C  CG1  . VAL   B 1 34  ? 43.013 -14.971 -6.840  1.00 13.61 ?  34  VAL   B CG1  1 
ATOM   4530 C  CG2  . VAL   B 1 34  ? 42.681 -13.096 -8.473  1.00 14.37 ?  34  VAL   B CG2  1 
ATOM   4531 H  H    . VAL   B 1 34  ? 44.582 -14.859 -10.686 1.00 14.78 ?  34  VAL   B H    1 
ATOM   4532 H  HA   . VAL   B 1 34  ? 45.201 -14.115 -8.147  1.00 14.18 ?  34  VAL   B HA   1 
ATOM   4533 H  HB   . VAL   B 1 34  ? 42.634 -15.100 -8.837  1.00 15.92 ?  34  VAL   B HB   1 
ATOM   4534 H  HG11 . VAL   B 1 34  ? 42.159 -14.653 -6.507  1.00 16.38 ?  34  VAL   B HG11 1 
ATOM   4535 H  HG12 . VAL   B 1 34  ? 43.035 -15.943 -6.804  1.00 16.38 ?  34  VAL   B HG12 1 
ATOM   4536 H  HG13 . VAL   B 1 34  ? 43.733 -14.604 -6.306  1.00 16.38 ?  34  VAL   B HG13 1 
ATOM   4537 H  HG21 . VAL   B 1 34  ? 41.761 -13.039 -8.167  1.00 17.29 ?  34  VAL   B HG21 1 
ATOM   4538 H  HG22 . VAL   B 1 34  ? 43.239 -12.492 -7.963  1.00 17.29 ?  34  VAL   B HG22 1 
ATOM   4539 H  HG23 . VAL   B 1 34  ? 42.725 -12.869 -9.418  1.00 17.29 ?  34  VAL   B HG23 1 
ATOM   4540 N  N    . VAL   B 1 35  ? 45.981 -16.366 -7.616  1.00 10.55 ?  35  VAL   B N    1 
ATOM   4541 C  CA   . VAL   B 1 35  ? 46.215 -17.712 -7.100  1.00 10.24 ?  35  VAL   B CA   1 
ATOM   4542 C  C    . VAL   B 1 35  ? 45.682 -17.768 -5.678  1.00 10.06 ?  35  VAL   B C    1 
ATOM   4543 O  O    . VAL   B 1 35  ? 45.899 -16.841 -4.890  1.00 10.66 ?  35  VAL   B O    1 
ATOM   4544 C  CB   . VAL   B 1 35  ? 47.697 -18.134 -7.189  1.00 11.14 ?  35  VAL   B CB   1 
ATOM   4545 C  CG1  . VAL   B 1 35  ? 48.604 -17.295 -6.270  1.00 11.85 ?  35  VAL   B CG1  1 
ATOM   4546 C  CG2  . VAL   B 1 35  ? 47.848 -19.628 -6.866  1.00 11.84 ?  35  VAL   B CG2  1 
ATOM   4547 H  H    . VAL   B 1 35  ? 46.488 -15.769 -7.257  1.00 12.70 ?  35  VAL   B H    1 
ATOM   4548 H  HA   . VAL   B 1 35  ? 45.698 -18.343 -7.628  1.00 12.34 ?  35  VAL   B HA   1 
ATOM   4549 H  HB   . VAL   B 1 35  ? 47.999 -18.009 -8.103  1.00 13.42 ?  35  VAL   B HB   1 
ATOM   4550 H  HG11 . VAL   B 1 35  ? 49.525 -17.524 -6.452  1.00 14.27 ?  35  VAL   B HG11 1 
ATOM   4551 H  HG12 . VAL   B 1 35  ? 48.442 -16.362 -6.447  1.00 14.27 ?  35  VAL   B HG12 1 
ATOM   4552 H  HG13 . VAL   B 1 35  ? 48.385 -17.506 -5.346  1.00 14.27 ?  35  VAL   B HG13 1 
ATOM   4553 H  HG21 . VAL   B 1 35  ? 48.773 -19.891 -6.977  1.00 14.25 ?  35  VAL   B HG21 1 
ATOM   4554 H  HG22 . VAL   B 1 35  ? 47.568 -19.789 -5.948  1.00 14.25 ?  35  VAL   B HG22 1 
ATOM   4555 H  HG23 . VAL   B 1 35  ? 47.285 -20.149 -7.470  1.00 14.25 ?  35  VAL   B HG23 1 
ATOM   4556 N  N    . VAL   B 1 36  ? 44.954 -18.840 -5.362  1.00 10.03 ?  36  VAL   B N    1 
ATOM   4557 C  CA   . VAL   B 1 36  ? 44.416 -19.045 -4.030  1.00 10.03 ?  36  VAL   B CA   1 
ATOM   4558 C  C    . VAL   B 1 36  ? 45.430 -19.804 -3.182  1.00 9.67  ?  36  VAL   B C    1 
ATOM   4559 O  O    . VAL   B 1 36  ? 45.960 -20.843 -3.602  1.00 10.91 ?  36  VAL   B O    1 
ATOM   4560 C  CB   . VAL   B 1 36  ? 43.080 -19.806 -4.101  1.00 10.49 ?  36  VAL   B CB   1 
ATOM   4561 C  CG1  . VAL   B 1 36  ? 42.585 -20.170 -2.711  1.00 11.21 ?  36  VAL   B CG1  1 
ATOM   4562 C  CG2  . VAL   B 1 36  ? 42.044 -18.972 -4.837  1.00 10.92 ?  36  VAL   B CG2  1 
ATOM   4563 H  H    . VAL   B 1 36  ? 44.761 -19.471 -5.915  1.00 12.09 ?  36  VAL   B H    1 
ATOM   4564 H  HA   . VAL   B 1 36  ? 44.249 -18.185 -3.614  1.00 12.09 ?  36  VAL   B HA   1 
ATOM   4565 H  HB   . VAL   B 1 36  ? 43.209 -20.630 -4.596  1.00 12.64 ?  36  VAL   B HB   1 
ATOM   4566 H  HG11 . VAL   B 1 36  ? 41.647 -20.406 -2.762  1.00 13.50 ?  36  VAL   B HG11 1 
ATOM   4567 H  HG12 . VAL   B 1 36  ? 43.099 -20.917 -2.372  1.00 13.50 ?  36  VAL   B HG12 1 
ATOM   4568 H  HG13 . VAL   B 1 36  ? 42.696 -19.398 -2.127  1.00 13.50 ?  36  VAL   B HG13 1 
ATOM   4569 H  HG21 . VAL   B 1 36  ? 41.203 -19.449 -4.854  1.00 13.15 ?  36  VAL   B HG21 1 
ATOM   4570 H  HG22 . VAL   B 1 36  ? 41.937 -18.123 -4.376  1.00 13.15 ?  36  VAL   B HG22 1 
ATOM   4571 H  HG23 . VAL   B 1 36  ? 42.354 -18.813 -5.745  1.00 13.15 ?  36  VAL   B HG23 1 
ATOM   4572 N  N    . ASN   B 1 37  ? 45.653 -19.311 -1.965  1.00 9.96  ?  37  ASN   B N    1 
ATOM   4573 C  CA   . ASN   B 1 37  ? 46.403 -20.036 -0.953  1.00 10.23 ?  37  ASN   B CA   1 
ATOM   4574 C  C    . ASN   B 1 37  ? 45.454 -20.712 0.029   1.00 10.47 ?  37  ASN   B C    1 
ATOM   4575 O  O    . ASN   B 1 37  ? 44.443 -20.138 0.440   1.00 10.86 ?  37  ASN   B O    1 
ATOM   4576 C  CB   . ASN   B 1 37  ? 47.321 -19.088 -0.189  1.00 10.20 ?  37  ASN   B CB   1 
ATOM   4577 C  CG   . ASN   B 1 37  ? 48.177 -19.806 0.817   1.00 10.74 ?  37  ASN   B CG   1 
ATOM   4578 O  OD1  . ASN   B 1 37  ? 48.517 -20.983 0.637   1.00 11.35 ?  37  ASN   B OD1  1 
ATOM   4579 N  ND2  . ASN   B 1 37  ? 48.527 -19.110 1.892   1.00 10.71 ?  37  ASN   B ND2  1 
ATOM   4580 H  H    . ASN   B 1 37  ? 45.373 -18.540 -1.692  1.00 12.00 ?  37  ASN   B H    1 
ATOM   4581 H  HA   . ASN   B 1 37  ? 46.940 -20.724 -1.368  1.00 12.33 ?  37  ASN   B HA   1 
ATOM   4582 H  HB2  . ASN   B 1 37  ? 47.909 -18.650 -0.821  1.00 12.29 ?  37  ASN   B HB2  1 
ATOM   4583 H  HB3  . ASN   B 1 37  ? 46.787 -18.436 0.285   1.00 12.29 ?  37  ASN   B HB3  1 
ATOM   4584 H  HD21 . ASN   B 1 37  ? 49.021 -19.471 2.499   1.00 12.90 ?  37  ASN   B HD21 1 
ATOM   4585 H  HD22 . ASN   B 1 37  ? 48.270 -18.300 1.984   1.00 12.90 ?  37  ASN   B HD22 1 
ATOM   4586 N  N    . ALA   B 1 38  ? 45.802 -21.944 0.408   1.00 10.64 ?  38  ALA   B N    1 
ATOM   4587 C  CA   . ALA   B 1 38  ? 45.143 -22.688 1.484   1.00 11.21 ?  38  ALA   B CA   1 
ATOM   4588 C  C    . ALA   B 1 38  ? 45.730 -22.203 2.810   1.00 10.91 ?  38  ALA   B C    1 
ATOM   4589 O  O    . ALA   B 1 38  ? 46.638 -22.809 3.393   1.00 11.87 ?  38  ALA   B O    1 
ATOM   4590 C  CB   . ALA   B 1 38  ? 45.369 -24.182 1.296   1.00 12.45 ?  38  ALA   B CB   1 
ATOM   4591 H  H    . ALA   B 1 38  ? 46.453 -22.377 0.059   1.00 12.81 ?  38  ALA   B H    1 
ATOM   4592 H  HA   . ALA   B 1 38  ? 44.189 -22.508 1.480   1.00 13.50 ?  38  ALA   B HA   1 
ATOM   4593 H  HB1  . ALA   B 1 38  ? 44.920 -24.663 2.017   1.00 14.99 ?  38  ALA   B HB1  1 
ATOM   4594 H  HB2  . ALA   B 1 38  ? 44.994 -24.453 0.444   1.00 14.99 ?  38  ALA   B HB2  1 
ATOM   4595 H  HB3  . ALA   B 1 38  ? 46.316 -24.367 1.320   1.00 14.99 ?  38  ALA   B HB3  1 
ATOM   4596 N  N    . ALA   B 1 39  ? 45.217 -21.060 3.270   1.00 10.64 ?  39  ALA   B N    1 
ATOM   4597 C  CA   . ALA   B 1 39  ? 45.768 -20.325 4.398   1.00 11.06 ?  39  ALA   B CA   1 
ATOM   4598 C  C    . ALA   B 1 39  ? 45.154 -20.770 5.723   1.00 11.01 ?  39  ALA   B C    1 
ATOM   4599 O  O    . ALA   B 1 39  ? 44.129 -21.454 5.773   1.00 11.97 ?  39  ALA   B O    1 
ATOM   4600 C  CB   . ALA   B 1 39  ? 45.520 -18.826 4.205   1.00 11.75 ?  39  ALA   B CB   1 
ATOM   4601 H  H    . ALA   B 1 39  ? 44.524 -20.683 2.928   1.00 12.82 ?  39  ALA   B H    1 
ATOM   4602 H  HA   . ALA   B 1 39  ? 46.724 -20.471 4.439   1.00 13.32 ?  39  ALA   B HA   1 
ATOM   4603 H  HB1  . ALA   B 1 39  ? 45.891 -18.344 4.961   1.00 14.15 ?  39  ALA   B HB1  1 
ATOM   4604 H  HB2  . ALA   B 1 39  ? 45.952 -18.536 3.385   1.00 14.15 ?  39  ALA   B HB2  1 
ATOM   4605 H  HB3  . ALA   B 1 39  ? 44.565 -18.666 4.148   1.00 14.15 ?  39  ALA   B HB3  1 
ATOM   4606 N  N    . ASN   B 1 40  ? 45.798 -20.355 6.809   1.00 11.53 ?  40  ASN   B N    1 
ATOM   4607 C  CA   . ASN   B 1 40  ? 45.232 -20.402 8.148   1.00 12.46 ?  40  ASN   B CA   1 
ATOM   4608 C  C    . ASN   B 1 40  ? 45.051 -18.977 8.673   1.00 12.12 ?  40  ASN   B C    1 
ATOM   4609 O  O    . ASN   B 1 40  ? 45.457 -17.994 8.042   1.00 12.15 ?  40  ASN   B O    1 
ATOM   4610 C  CB   . ASN   B 1 40  ? 46.087 -21.271 9.086   1.00 13.43 ?  40  ASN   B CB   1 
ATOM   4611 C  CG   . ASN   B 1 40  ? 47.541 -20.864 9.106   1.00 14.57 ?  40  ASN   B CG   1 
ATOM   4612 O  OD1  . ASN   B 1 40  ? 47.861 -19.682 9.149   1.00 16.63 ?  40  ASN   B OD1  1 
ATOM   4613 N  ND2  . ASN   B 1 40  ? 48.431 -21.839 9.093   1.00 14.42 ?  40  ASN   B ND2  1 
ATOM   4614 H  H    . ASN   B 1 40  ? 46.594 -20.033 6.790   1.00 13.89 ?  40  ASN   B H    1 
ATOM   4615 H  HA   . ASN   B 1 40  ? 44.351 -20.800 8.102   1.00 14.99 ?  40  ASN   B HA   1 
ATOM   4616 H  HB2  . ASN   B 1 40  ? 45.738 -21.198 9.989   1.00 16.16 ?  40  ASN   B HB2  1 
ATOM   4617 H  HB3  . ASN   B 1 40  ? 46.037 -22.194 8.788   1.00 16.16 ?  40  ASN   B HB3  1 
ATOM   4618 H  HD21 . ASN   B 1 40  ? 49.271 -21.656 9.105   1.00 17.35 ?  40  ASN   B HD21 1 
ATOM   4619 H  HD22 . ASN   B 1 40  ? 48.170 -22.658 9.063   1.00 17.35 ?  40  ASN   B HD22 1 
ATOM   4620 N  N    . VAL   B 1 41  ? 44.408 -18.854 9.835   1.00 12.59 ?  41  VAL   B N    1 
ATOM   4621 C  CA   . VAL   B 1 41  ? 43.946 -17.536 10.281  1.00 13.26 ?  41  VAL   B CA   1 
ATOM   4622 C  C    . VAL   B 1 41  ? 45.096 -16.579 10.573  1.00 13.13 ?  41  VAL   B C    1 
ATOM   4623 O  O    . VAL   B 1 41  ? 44.917 -15.359 10.486  1.00 13.44 ?  41  VAL   B O    1 
ATOM   4624 C  CB   . VAL   B 1 41  ? 42.975 -17.615 11.477  1.00 14.83 ?  41  VAL   B CB   1 
ATOM   4625 C  CG1  . VAL   B 1 41  ? 41.671 -18.297 11.079  1.00 15.37 ?  41  VAL   B CG1  1 
ATOM   4626 C  CG2  . VAL   B 1 41  ? 43.628 -18.300 12.665  1.00 16.05 ?  41  VAL   B CG2  1 
ATOM   4627 H  H    . VAL   B 1 41  ? 44.228 -19.499 10.368  1.00 15.15 ?  41  VAL   B H    1 
ATOM   4628 H  HA   . VAL   B 1 41  ? 43.442 -17.142 9.554   1.00 15.96 ?  41  VAL   B HA   1 
ATOM   4629 H  HB   . VAL   B 1 41  ? 42.754 -16.711 11.754  1.00 17.84 ?  41  VAL   B HB   1 
ATOM   4630 H  HG11 . VAL   B 1 41  ? 41.072 -18.305 11.845  1.00 18.49 ?  41  VAL   B HG11 1 
ATOM   4631 H  HG12 . VAL   B 1 41  ? 41.266 -17.804 10.350  1.00 18.49 ?  41  VAL   B HG12 1 
ATOM   4632 H  HG13 . VAL   B 1 41  ? 41.863 -19.206 10.801  1.00 18.49 ?  41  VAL   B HG13 1 
ATOM   4633 H  HG21 . VAL   B 1 41  ? 42.996 -18.331 13.399  1.00 19.31 ?  41  VAL   B HG21 1 
ATOM   4634 H  HG22 . VAL   B 1 41  ? 43.882 -19.202 12.411  1.00 19.31 ?  41  VAL   B HG22 1 
ATOM   4635 H  HG23 . VAL   B 1 41  ? 44.415 -17.798 12.928  1.00 19.31 ?  41  VAL   B HG23 1 
ATOM   4636 N  N    . TYR   B 1 42  ? 46.266 -17.090 10.952  1.00 13.51 ?  42  TYR   B N    1 
ATOM   4637 C  CA   . TYR   B 1 42  ? 47.419 -16.241 11.218  1.00 13.67 ?  42  TYR   B CA   1 
ATOM   4638 C  C    . TYR   B 1 42  ? 48.381 -16.165 10.035  1.00 12.95 ?  42  TYR   B C    1 
ATOM   4639 O  O    . TYR   B 1 42  ? 49.473 -15.601 10.170  1.00 14.21 ?  42  TYR   B O    1 
ATOM   4640 C  CB   . TYR   B 1 42  ? 48.112 -16.654 12.523  1.00 15.40 ?  42  TYR   B CB   1 
ATOM   4641 C  CG   . TYR   B 1 42  ? 47.516 -15.965 13.750  1.00 15.72 ?  42  TYR   B CG   1 
ATOM   4642 C  CD1  . TYR   B 1 42  ? 47.730 -14.608 13.969  1.00 15.10 ?  42  TYR   B CD1  1 
ATOM   4643 C  CD2  . TYR   B 1 42  ? 46.739 -16.657 14.669  1.00 17.51 ?  42  TYR   B CD2  1 
ATOM   4644 C  CE1  . TYR   B 1 42  ? 47.200 -13.960 15.066  1.00 15.94 ?  42  TYR   B CE1  1 
ATOM   4645 C  CE2  . TYR   B 1 42  ? 46.203 -16.013 15.779  1.00 17.77 ?  42  TYR   B CE2  1 
ATOM   4646 C  CZ   . TYR   B 1 42  ? 46.438 -14.659 15.970  1.00 17.76 ?  42  TYR   B CZ   1 
ATOM   4647 O  OH   . TYR   B 1 42  ? 45.924 -13.989 17.064  1.00 20.39 ?  42  TYR   B OH   1 
ATOM   4648 H  H    . TYR   B 1 42  ? 46.417 -17.935 11.049  1.00 16.26 ?  42  TYR   B H    1 
ATOM   4649 H  HA   . TYR   B 1 42  ? 47.091 -15.343 11.355  1.00 16.46 ?  42  TYR   B HA   1 
ATOM   4650 H  HB2  . TYR   B 1 42  ? 48.020 -17.610 12.642  1.00 18.53 ?  42  TYR   B HB2  1 
ATOM   4651 H  HB3  . TYR   B 1 42  ? 49.050 -16.413 12.469  1.00 18.53 ?  42  TYR   B HB3  1 
ATOM   4652 H  HD1  . TYR   B 1 42  ? 48.250 -14.126 13.358  1.00 18.16 ?  42  TYR   B HD1  1 
ATOM   4653 H  HD2  . TYR   B 1 42  ? 46.579 -17.566 14.537  1.00 21.06 ?  42  TYR   B HD2  1 
ATOM   4654 H  HE1  . TYR   B 1 42  ? 47.362 -13.054 15.190  1.00 19.18 ?  42  TYR   B HE1  1 
ATOM   4655 H  HE2  . TYR   B 1 42  ? 45.683 -16.492 16.383  1.00 21.38 ?  42  TYR   B HE2  1 
ATOM   4656 H  HH   . TYR   B 1 42  ? 46.155 -13.185 17.030  1.00 24.51 ?  42  TYR   B HH   1 
ATOM   4657 N  N    . LEU   B 1 43  ? 47.983 -16.679 8.873   1.00 11.87 ?  43  LEU   B N    1 
ATOM   4658 C  CA   . LEU   B 1 43  ? 48.801 -16.612 7.665   1.00 11.84 ?  43  LEU   B CA   1 
ATOM   4659 C  C    . LEU   B 1 43  ? 50.214 -17.120 7.925   1.00 12.24 ?  43  LEU   B C    1 
ATOM   4660 O  O    . LEU   B 1 43  ? 51.196 -16.528 7.475   1.00 13.02 ?  43  LEU   B O    1 
ATOM   4661 C  CB   . LEU   B 1 43  ? 48.824 -15.209 7.057   1.00 12.12 ?  43  LEU   B CB   1 
ATOM   4662 C  CG   . LEU   B 1 43  ? 47.464 -14.599 6.691   1.00 12.53 ?  43  LEU   B CG   1 
ATOM   4663 C  CD1  . LEU   B 1 43  ? 47.668 -13.205 6.107   1.00 13.91 ?  43  LEU   B CD1  1 
ATOM   4664 C  CD2  . LEU   B 1 43  ? 46.692 -15.495 5.725   1.00 12.64 ?  43  LEU   B CD2  1 
ATOM   4665 H  H    . LEU   B 1 43  ? 47.237 -17.087 8.758   1.00 14.29 ?  43  LEU   B H    1 
ATOM   4666 H  HA   . LEU   B 1 43  ? 48.404 -17.205 7.002   1.00 14.25 ?  43  LEU   B HA   1 
ATOM   4667 H  HB2  . LEU   B 1 43  ? 49.249 -14.614 7.691   1.00 14.59 ?  43  LEU   B HB2  1 
ATOM   4668 H  HB3  . LEU   B 1 43  ? 49.351 -15.244 6.243   1.00 14.59 ?  43  LEU   B HB3  1 
ATOM   4669 H  HG   . LEU   B 1 43  ? 46.938 -14.505 7.496   1.00 15.08 ?  43  LEU   B HG   1 
ATOM   4670 H  HD11 . LEU   B 1 43  ? 46.804 -12.826 5.881   1.00 16.74 ?  43  LEU   B HD11 1 
ATOM   4671 H  HD12 . LEU   B 1 43  ? 48.108 -12.645 6.770   1.00 16.74 ?  43  LEU   B HD12 1 
ATOM   4672 H  HD13 . LEU   B 1 43  ? 48.221 -13.267 5.313   1.00 16.74 ?  43  LEU   B HD13 1 
ATOM   4673 H  HD21 . LEU   B 1 43  ? 45.890 -15.029 5.435   1.00 15.22 ?  43  LEU   B HD21 1 
ATOM   4674 H  HD22 . LEU   B 1 43  ? 47.251 -15.697 4.960   1.00 15.22 ?  43  LEU   B HD22 1 
ATOM   4675 H  HD23 . LEU   B 1 43  ? 46.448 -16.315 6.183   1.00 15.22 ?  43  LEU   B HD23 1 
ATOM   4676 N  N    . LYS   B 1 44  ? 50.314 -18.242 8.643   1.00 12.47 ?  44  LYS   B N    1 
ATOM   4677 C  CA   . LYS   B 1 44  ? 51.583 -18.918 8.883   1.00 13.08 ?  44  LYS   B CA   1 
ATOM   4678 C  C    . LYS   B 1 44  ? 51.696 -20.037 7.855   1.00 12.51 ?  44  LYS   B C    1 
ATOM   4679 O  O    . LYS   B 1 44  ? 50.996 -21.050 7.944   1.00 13.69 ?  44  LYS   B O    1 
ATOM   4680 C  CB   . LYS   B 1 44  ? 51.639 -19.436 10.318  1.00 14.82 ?  44  LYS   B CB   1 
ATOM   4681 C  CG   . LYS   B 1 44  ? 51.818 -18.326 11.345  1.00 17.51 ?  44  LYS   B CG   1 
ATOM   4682 C  CD   . LYS   B 1 44  ? 52.994 -17.438 10.934  1.00 21.00 ?  44  LYS   B CD   1 
ATOM   4683 C  CE   . LYS   B 1 44  ? 53.559 -16.621 12.065  1.00 23.88 ?  44  LYS   B CE   1 
ATOM   4684 N  NZ   . LYS   B 1 44  ? 54.717 -15.794 11.645  1.00 25.05 ?  44  LYS   B NZ   1 
ATOM   4685 H  H    . LYS   B 1 44  ? 49.641 -18.632 9.013   1.00 15.01 ?  44  LYS   B H    1 
ATOM   4686 H  HA   . LYS   B 1 44  ? 52.313 -18.302 8.720   1.00 15.74 ?  44  LYS   B HA   1 
ATOM   4687 H  HB2  . LYS   B 1 44  ? 50.803 -19.893 10.521  1.00 17.84 ?  44  LYS   B HB2  1 
ATOM   4688 H  HB3  . LYS   B 1 44  ? 52.380 -20.049 10.407  1.00 17.84 ?  44  LYS   B HB3  1 
ATOM   4689 H  HG2  . LYS   B 1 44  ? 51.015 -17.788 11.388  1.00 21.06 ?  44  LYS   B HG2  1 
ATOM   4690 H  HG3  . LYS   B 1 44  ? 52.015 -18.720 12.213  1.00 21.06 ?  44  LYS   B HG3  1 
ATOM   4691 H  HD2  . LYS   B 1 44  ? 53.699 -18.003 10.572  1.00 25.25 ?  44  LYS   B HD2  1 
ATOM   4692 H  HD3  . LYS   B 1 44  ? 52.686 -16.821 10.249  1.00 25.25 ?  44  LYS   B HD3  1 
ATOM   4693 H  HE2  . LYS   B 1 44  ? 52.879 -16.006 12.348  1.00 28.70 ?  44  LYS   B HE2  1 
ATOM   4694 H  HE3  . LYS   B 1 44  ? 53.830 -17.209 12.792  1.00 28.70 ?  44  LYS   B HE3  1 
ATOM   4695 H  HZ1  . LYS   B 1 44  ? 55.020 -15.325 12.337  1.00 30.10 ?  44  LYS   B HZ1  1 
ATOM   4696 H  HZ2  . LYS   B 1 44  ? 55.369 -16.311 11.335  1.00 30.10 ?  44  LYS   B HZ2  1 
ATOM   4697 H  HZ3  . LYS   B 1 44  ? 54.465 -15.228 11.002  1.00 30.10 ?  44  LYS   B HZ3  1 
ATOM   4698 N  N    . HIS   B 1 45  ? 52.545 -19.822 6.852   1.00 12.41 ?  45  HIS   B N    1 
ATOM   4699 C  CA   . HIS   B 1 45  ? 52.564 -20.657 5.650   1.00 12.21 ?  45  HIS   B CA   1 
ATOM   4700 C  C    . HIS   B 1 45  ? 53.584 -21.778 5.814   1.00 14.51 ?  45  HIS   B C    1 
ATOM   4701 O  O    . HIS   B 1 45  ? 54.648 -21.791 5.205   1.00 17.00 ?  45  HIS   B O    1 
ATOM   4702 C  CB   . HIS   B 1 45  ? 52.875 -19.806 4.430   1.00 12.41 ?  45  HIS   B CB   1 
ATOM   4703 C  CG   . HIS   B 1 45  ? 52.006 -18.602 4.321   1.00 12.44 ?  45  HIS   B CG   1 
ATOM   4704 N  ND1  . HIS   B 1 45  ? 50.628 -18.677 4.297   1.00 12.20 ?  45  HIS   B ND1  1 
ATOM   4705 C  CD2  . HIS   B 1 45  ? 52.324 -17.289 4.252   1.00 12.95 ?  45  HIS   B CD2  1 
ATOM   4706 C  CE1  . HIS   B 1 45  ? 50.142 -17.453 4.199   1.00 11.81 ?  45  HIS   B CE1  1 
ATOM   4707 N  NE2  . HIS   B 1 45  ? 51.147 -16.594 4.165   1.00 12.69 ?  45  HIS   B NE2  1 
ATOM   4708 H  H    . HIS   B 1 45  ? 53.112 -19.177 6.835   1.00 14.94 ?  45  HIS   B H    1 
ATOM   4709 H  HA   . HIS   B 1 45  ? 51.684 -21.053 5.523   1.00 14.70 ?  45  HIS   B HA   1 
ATOM   4710 H  HB2  . HIS   B 1 45  ? 53.795 -19.511 4.477   1.00 14.94 ?  45  HIS   B HB2  1 
ATOM   4711 H  HB3  . HIS   B 1 45  ? 52.743 -20.346 3.629   1.00 14.94 ?  45  HIS   B HB3  1 
ATOM   4712 H  HD2  . HIS   B 1 45  ? 53.179 -16.923 4.250   1.00 15.58 ?  45  HIS   B HD2  1 
ATOM   4713 H  HE1  . HIS   B 1 45  ? 49.238 -17.236 4.151   1.00 14.22 ?  45  HIS   B HE1  1 
ATOM   4714 H  HE2  . HIS   B 1 45  ? 51.067 -15.739 4.112   1.00 15.28 ?  45  HIS   B HE2  1 
ATOM   4715 N  N    A GLY   B 1 46  ? 53.215 -22.750 6.643   0.72 15.39 ?  46  GLY   B N    1 
ATOM   4716 N  N    B GLY   B 1 46  ? 53.225 -22.736 6.660   0.28 15.43 ?  46  GLY   B N    1 
ATOM   4717 C  CA   A GLY   B 1 46  ? 54.138 -23.806 7.017   0.72 17.29 ?  46  GLY   B CA   1 
ATOM   4718 C  CA   B GLY   B 1 46  ? 54.141 -23.804 7.000   0.28 16.64 ?  46  GLY   B CA   1 
ATOM   4719 C  C    A GLY   B 1 46  ? 54.181 -25.024 6.116   0.72 18.76 ?  46  GLY   B C    1 
ATOM   4720 C  C    B GLY   B 1 46  ? 54.163 -24.948 6.007   0.28 17.86 ?  46  GLY   B C    1 
ATOM   4721 O  O    A GLY   B 1 46  ? 55.257 -25.454 5.692   0.72 21.45 ?  46  GLY   B O    1 
ATOM   4722 O  O    B GLY   B 1 46  ? 55.193 -25.224 5.384   0.28 18.58 ?  46  GLY   B O    1 
ATOM   4723 H  H    A GLY   B 1 46  ? 52.437 -22.804 7.017   0.72 18.51 ?  46  GLY   B H    1 
ATOM   4724 H  H    B GLY   B 1 46  ? 52.456 -22.781 7.054   0.28 18.57 ?  46  GLY   B H    1 
ATOM   4725 H  HA2  A GLY   B 1 46  ? 55.030 -23.432 7.056   0.72 20.79 ?  46  GLY   B HA2  1 
ATOM   4726 H  HA2  B GLY   B 1 46  ? 55.036 -23.440 7.059   0.28 20.02 ?  46  GLY   B HA2  1 
ATOM   4727 H  HA3  A GLY   B 1 46  ? 53.905 -24.116 7.906   0.72 20.79 ?  46  GLY   B HA3  1 
ATOM   4728 H  HA3  B GLY   B 1 46  ? 53.901 -24.156 7.872   0.28 20.02 ?  46  GLY   B HA3  1 
ATOM   4729 N  N    . GLY   B 1 47  ? 53.023 -25.616 5.835   1.00 18.60 ?  47  GLY   B N    1 
ATOM   4730 C  CA   . GLY   B 1 47  ? 52.964 -26.881 5.131   1.00 16.43 ?  47  GLY   B CA   1 
ATOM   4731 C  C    . GLY   B 1 47  ? 52.052 -26.851 3.920   1.00 14.24 ?  47  GLY   B C    1 
ATOM   4732 O  O    . GLY   B 1 47  ? 51.404 -25.845 3.628   1.00 14.43 ?  47  GLY   B O    1 
ATOM   4733 H  H    A GLY   B 1 47  ? 52.253 -25.314 6.071   0.72 22.36 ?  47  GLY   B H    1 
ATOM   4734 H  H    B GLY   B 1 47  ? 52.259 -25.349 6.129   0.28 22.36 ?  47  GLY   B H    1 
ATOM   4735 H  HA2  . GLY   B 1 47  ? 53.851 -27.133 4.832   1.00 19.76 ?  47  GLY   B HA2  1 
ATOM   4736 H  HA3  . GLY   B 1 47  ? 52.644 -27.569 5.738   1.00 19.76 ?  47  GLY   B HA3  1 
ATOM   4737 N  N    . GLY   B 1 48  ? 51.999 -27.992 3.233   1.00 13.41 ?  48  GLY   B N    1 
ATOM   4738 C  CA   . GLY   B 1 48  ? 51.077 -28.131 2.125   1.00 12.98 ?  48  GLY   B CA   1 
ATOM   4739 C  C    . GLY   B 1 48  ? 51.222 -27.023 1.110   1.00 12.25 ?  48  GLY   B C    1 
ATOM   4740 O  O    . GLY   B 1 48  ? 52.325 -26.561 0.799   1.00 13.15 ?  48  GLY   B O    1 
ATOM   4741 H  H    . GLY   B 1 48  ? 52.482 -28.680 3.388   1.00 16.14 ?  48  GLY   B H    1 
ATOM   4742 H  HA2  . GLY   B 1 48  ? 51.234 -28.979 1.680   1.00 15.62 ?  48  GLY   B HA2  1 
ATOM   4743 H  HA3  . GLY   B 1 48  ? 50.165 -28.124 2.456   1.00 15.62 ?  48  GLY   B HA3  1 
ATOM   4744 N  N    . VAL   B 1 49  ? 50.078 -26.595 0.575   1.00 12.37 ?  49  VAL   B N    1 
ATOM   4745 C  CA   . VAL   B 1 49  ? 50.063 -25.570 -0.465  1.00 12.30 ?  49  VAL   B CA   1 
ATOM   4746 C  C    . VAL   B 1 49  ? 50.724 -24.284 0.024   1.00 11.52 ?  49  VAL   B C    1 
ATOM   4747 O  O    . VAL   B 1 49  ? 51.510 -23.662 -0.698  1.00 12.24 ?  49  VAL   B O    1 
ATOM   4748 C  CB   . VAL   B 1 49  ? 48.621 -25.316 -0.944  1.00 13.38 ?  49  VAL   B CB   1 
ATOM   4749 C  CG1  . VAL   B 1 49  ? 48.547 -24.070 -1.819  1.00 13.29 ?  49  VAL   B CG1  1 
ATOM   4750 C  CG2  . VAL   B 1 49  ? 48.082 -26.529 -1.693  1.00 15.18 ?  49  VAL   B CG2  1 
ATOM   4751 H  H    . VAL   B 1 49  ? 49.291 -26.881 0.794   1.00 14.89 ?  49  VAL   B H    1 
ATOM   4752 H  HA   . VAL   B 1 49  ? 50.568 -25.891 -1.227  1.00 14.80 ?  49  VAL   B HA   1 
ATOM   4753 H  HB   . VAL   B 1 49  ? 48.053 -25.168 -0.174  1.00 16.10 ?  49  VAL   B HB   1 
ATOM   4754 H  HG11 . VAL   B 1 49  ? 47.715 -24.084 -2.319  1.00 16.00 ?  49  VAL   B HG11 1 
ATOM   4755 H  HG12 . VAL   B 1 49  ? 48.574 -23.281 -1.253  1.00 16.00 ?  49  VAL   B HG12 1 
ATOM   4756 H  HG13 . VAL   B 1 49  ? 49.299 -24.066 -2.431  1.00 16.00 ?  49  VAL   B HG13 1 
ATOM   4757 H  HG21 . VAL   B 1 49  ? 47.174 -26.346 -1.985  1.00 18.26 ?  49  VAL   B HG21 1 
ATOM   4758 H  HG22 . VAL   B 1 49  ? 48.646 -26.700 -2.466  1.00 18.26 ?  49  VAL   B HG22 1 
ATOM   4759 H  HG23 . VAL   B 1 49  ? 48.092 -27.295 -1.101  1.00 18.26 ?  49  VAL   B HG23 1 
ATOM   4760 N  N    . ALA   B 1 50  ? 50.378 -23.838 1.234   1.00 11.40 ?  50  ALA   B N    1 
ATOM   4761 C  CA   . ALA   B 1 50  ? 50.899 -22.561 1.709   1.00 11.24 ?  50  ALA   B CA   1 
ATOM   4762 C  C    . ALA   B 1 50  ? 52.416 -22.596 1.818   1.00 11.47 ?  50  ALA   B C    1 
ATOM   4763 O  O    . ALA   B 1 50  ? 53.097 -21.631 1.453   1.00 11.53 ?  50  ALA   B O    1 
ATOM   4764 C  CB   . ALA   B 1 50  ? 50.270 -22.206 3.054   1.00 11.40 ?  50  ALA   B CB   1 
ATOM   4765 H  H    . ALA   B 1 50  ? 49.854 -24.247 1.781   1.00 13.73 ?  50  ALA   B H    1 
ATOM   4766 H  HA   . ALA   B 1 50  ? 50.666 -21.869 1.077   1.00 13.54 ?  50  ALA   B HA   1 
ATOM   4767 H  HB1  . ALA   B 1 50  ? 50.626 -21.352 3.354   1.00 13.73 ?  50  ALA   B HB1  1 
ATOM   4768 H  HB2  . ALA   B 1 50  ? 49.307 -22.138 2.946   1.00 13.73 ?  50  ALA   B HB2  1 
ATOM   4769 H  HB3  . ALA   B 1 50  ? 50.481 -22.896 3.700   1.00 13.73 ?  50  ALA   B HB3  1 
ATOM   4770 N  N    . GLY   B 1 51  ? 52.966 -23.693 2.329   1.00 12.24 ?  51  GLY   B N    1 
ATOM   4771 C  CA   . GLY   B 1 51  ? 54.410 -23.796 2.403   1.00 12.73 ?  51  GLY   B CA   1 
ATOM   4772 C  C    . GLY   B 1 51  ? 55.056 -23.740 1.034   1.00 12.54 ?  51  GLY   B C    1 
ATOM   4773 O  O    . GLY   B 1 51  ? 56.097 -23.102 0.853   1.00 13.35 ?  51  GLY   B O    1 
ATOM   4774 H  H    . GLY   B 1 51  ? 52.537 -24.379 2.629   1.00 14.74 ?  51  GLY   B H    1 
ATOM   4775 H  HA2  . GLY   B 1 51  ? 54.760 -23.066 2.939   1.00 15.33 ?  51  GLY   B HA2  1 
ATOM   4776 H  HA3  . GLY   B 1 51  ? 54.657 -24.634 2.826   1.00 15.33 ?  51  GLY   B HA3  1 
ATOM   4777 N  N    . ALA   B 1 52  ? 54.451 -24.408 0.052   1.00 12.14 ?  52  ALA   B N    1 
ATOM   4778 C  CA   . ALA   B 1 52  ? 55.007 -24.413 -1.293  1.00 12.54 ?  52  ALA   B CA   1 
ATOM   4779 C  C    . ALA   B 1 52  ? 54.929 -23.034 -1.938  1.00 12.01 ?  52  ALA   B C    1 
ATOM   4780 O  O    . ALA   B 1 52  ? 55.905 -22.581 -2.559  1.00 12.71 ?  52  ALA   B O    1 
ATOM   4781 C  CB   . ALA   B 1 52  ? 54.304 -25.456 -2.153  1.00 13.25 ?  52  ALA   B CB   1 
ATOM   4782 H  H    . ALA   B 1 52  ? 53.715 -24.849 0.138   1.00 14.61 ?  52  ALA   B H    1 
ATOM   4783 H  HA   . ALA   B 1 52  ? 55.942 -24.655 -1.235  1.00 15.09 ?  52  ALA   B HA   1 
ATOM   4784 H  HB1  . ALA   B 1 52  ? 54.696 -25.443 -3.042  1.00 15.94 ?  52  ALA   B HB1  1 
ATOM   4785 H  HB2  . ALA   B 1 52  ? 54.431 -26.330 -1.750  1.00 15.94 ?  52  ALA   B HB2  1 
ATOM   4786 H  HB3  . ALA   B 1 52  ? 53.362 -25.244 -2.202  1.00 15.94 ?  52  ALA   B HB3  1 
ATOM   4787 N  N    . LEU   B 1 53  ? 53.782 -22.355 -1.823  1.00 11.79 ?  53  LEU   B N    1 
ATOM   4788 C  CA   . LEU   B 1 53  ? 53.675 -21.015 -2.393  1.00 11.72 ?  53  LEU   B CA   1 
ATOM   4789 C  C    . LEU   B 1 53  ? 54.685 -20.078 -1.746  1.00 11.62 ?  53  LEU   B C    1 
ATOM   4790 O  O    . LEU   B 1 53  ? 55.386 -19.329 -2.434  1.00 12.51 ?  53  LEU   B O    1 
ATOM   4791 C  CB   . LEU   B 1 53  ? 52.253 -20.474 -2.222  1.00 12.37 ?  53  LEU   B CB   1 
ATOM   4792 C  CG   . LEU   B 1 53  ? 51.117 -21.206 -2.948  1.00 12.66 ?  53  LEU   B CG   1 
ATOM   4793 C  CD1  . LEU   B 1 53  ? 49.778 -20.586 -2.611  1.00 14.27 ?  53  LEU   B CD1  1 
ATOM   4794 C  CD2  . LEU   B 1 53  ? 51.333 -21.222 -4.452  1.00 14.51 ?  53  LEU   B CD2  1 
ATOM   4795 H  H    . LEU   B 1 53  ? 53.075 -22.639 -1.428  1.00 14.19 ?  53  LEU   B H    1 
ATOM   4796 H  HA   . LEU   B 1 53  ? 53.871 -21.062 -3.347  1.00 14.11 ?  53  LEU   B HA   1 
ATOM   4797 H  HB2  . LEU   B 1 53  ? 52.043 -20.491 -1.279  1.00 14.89 ?  53  LEU   B HB2  1 
ATOM   4798 H  HB3  . LEU   B 1 53  ? 52.245 -19.560 -2.539  1.00 14.89 ?  53  LEU   B HB3  1 
ATOM   4799 H  HG   . LEU   B 1 53  ? 51.096 -22.126 -2.642  1.00 15.25 ?  53  LEU   B HG   1 
ATOM   4800 H  HD11 . LEU   B 1 53  ? 49.077 -21.071 -3.078  1.00 17.18 ?  53  LEU   B HD11 1 
ATOM   4801 H  HD12 . LEU   B 1 53  ? 49.633 -20.649 -1.650  1.00 17.18 ?  53  LEU   B HD12 1 
ATOM   4802 H  HD13 . LEU   B 1 53  ? 49.778 -19.658 -2.884  1.00 17.18 ?  53  LEU   B HD13 1 
ATOM   4803 H  HD21 . LEU   B 1 53  ? 50.591 -21.685 -4.874  1.00 17.46 ?  53  LEU   B HD21 1 
ATOM   4804 H  HD22 . LEU   B 1 53  ? 51.381 -20.311 -4.777  1.00 17.46 ?  53  LEU   B HD22 1 
ATOM   4805 H  HD23 . LEU   B 1 53  ? 52.162 -21.689 -4.649  1.00 17.46 ?  53  LEU   B HD23 1 
ATOM   4806 N  N    . ASN   B 1 54  ? 54.775 -20.106 -0.419  1.00 11.37 ?  54  ASN   B N    1 
ATOM   4807 C  CA   . ASN   B 1 54  ? 55.691 -19.193 0.248   1.00 12.02 ?  54  ASN   B CA   1 
ATOM   4808 C  C    . ASN   B 1 54  ? 57.133 -19.473 -0.154  1.00 12.58 ?  54  ASN   B C    1 
ATOM   4809 O  O    . ASN   B 1 54  ? 57.910 -18.537 -0.386  1.00 13.07 ?  54  ASN   B O    1 
ATOM   4810 C  CB   . ASN   B 1 54  ? 55.532 -19.270 1.756   1.00 12.69 ?  54  ASN   B CB   1 
ATOM   4811 C  CG   . ASN   B 1 54  ? 56.508 -18.360 2.466   1.00 12.87 ?  54  ASN   B CG   1 
ATOM   4812 O  OD1  . ASN   B 1 54  ? 56.526 -17.150 2.227   1.00 13.17 ?  54  ASN   B OD1  1 
ATOM   4813 N  ND2  . ASN   B 1 54  ? 57.350 -18.936 3.317   1.00 14.61 ?  54  ASN   B ND2  1 
ATOM   4814 H  H    . ASN   B 1 54  ? 54.337 -20.633 0.097   1.00 13.69 ?  54  ASN   B H    1 
ATOM   4815 H  HA   . ASN   B 1 54  ? 55.477 -18.288 -0.027  1.00 14.47 ?  54  ASN   B HA   1 
ATOM   4816 H  HB2  . ASN   B 1 54  ? 54.631 -18.993 1.997   1.00 15.28 ?  54  ASN   B HB2  1 
ATOM   4817 H  HB3  . ASN   B 1 54  ? 55.693 -20.176 2.052   1.00 15.28 ?  54  ASN   B HB3  1 
ATOM   4818 H  HD21 . ASN   B 1 54  ? 57.929 -18.457 3.739   1.00 17.58 ?  54  ASN   B HD21 1 
ATOM   4819 H  HD22 . ASN   B 1 54  ? 57.318 -19.784 3.448   1.00 17.58 ?  54  ASN   B HD22 1 
ATOM   4820 N  N    . LYS   B 1 55  ? 57.519 -20.751 -0.218  1.00 13.10 ?  55  LYS   B N    1 
ATOM   4821 C  CA   . LYS   B 1 55  ? 58.875 -21.093 -0.636  1.00 13.89 ?  55  LYS   B CA   1 
ATOM   4822 C  C    . LYS   B 1 55  ? 59.172 -20.554 -2.029  1.00 13.74 ?  55  LYS   B C    1 
ATOM   4823 O  O    . LYS   B 1 55  ? 60.273 -20.052 -2.283  1.00 14.61 ?  55  LYS   B O    1 
ATOM   4824 C  CB   . LYS   B 1 55  ? 59.067 -22.608 -0.586  1.00 15.52 ?  55  LYS   B CB   1 
ATOM   4825 C  CG   . LYS   B 1 55  ? 60.449 -23.069 -1.005  1.00 19.54 ?  55  LYS   B CG   1 
ATOM   4826 C  CD   . LYS   B 1 55  ? 60.608 -24.571 -0.846  1.00 22.99 ?  55  LYS   B CD   1 
ATOM   4827 C  CE   . LYS   B 1 55  ? 60.597 -24.993 0.622   1.00 25.80 ?  55  LYS   B CE   1 
ATOM   4828 N  NZ   . LYS   B 1 55  ? 61.012 -26.405 0.801   1.00 27.10 ?  55  LYS   B NZ   1 
ATOM   4829 H  H    . LYS   B 1 55  ? 57.019 -21.421 -0.026  1.00 15.77 ?  55  LYS   B H    1 
ATOM   4830 H  HA   . LYS   B 1 55  ? 59.506 -20.691 -0.021  1.00 16.71 ?  55  LYS   B HA   1 
ATOM   4831 H  HB2  . LYS   B 1 55  ? 58.916 -22.905 0.325   1.00 18.67 ?  55  LYS   B HB2  1 
ATOM   4832 H  HB3  . LYS   B 1 55  ? 58.424 -23.025 -1.178  1.00 18.67 ?  55  LYS   B HB3  1 
ATOM   4833 H  HG2  . LYS   B 1 55  ? 60.593 -22.847 -1.938  1.00 23.49 ?  55  LYS   B HG2  1 
ATOM   4834 H  HG3  . LYS   B 1 55  ? 61.114 -22.632 -0.450  1.00 23.49 ?  55  LYS   B HG3  1 
ATOM   4835 H  HD2  . LYS   B 1 55  ? 59.874 -25.023 -1.294  1.00 27.63 ?  55  LYS   B HD2  1 
ATOM   4836 H  HD3  . LYS   B 1 55  ? 61.455 -24.850 -1.231  1.00 27.63 ?  55  LYS   B HD3  1 
ATOM   4837 H  HE2  . LYS   B 1 55  ? 61.211 -24.423 1.116   1.00 31.01 ?  55  LYS   B HE2  1 
ATOM   4838 H  HE3  . LYS   B 1 55  ? 59.696 -24.890 0.973   1.00 31.01 ?  55  LYS   B HE3  1 
ATOM   4839 H  HZ1  . LYS   B 1 55  ? 60.971 -26.624 1.663   1.00 32.57 ?  55  LYS   B HZ1  1 
ATOM   4840 H  HZ2  . LYS   B 1 55  ? 60.471 -26.939 0.340   1.00 32.57 ?  55  LYS   B HZ2  1 
ATOM   4841 H  HZ3  . LYS   B 1 55  ? 61.845 -26.514 0.513   1.00 32.57 ?  55  LYS   B HZ3  1 
ATOM   4842 N  N    . ALA   B 1 56  ? 58.199 -20.635 -2.942  1.00 13.38 ?  56  ALA   B N    1 
ATOM   4843 C  CA   . ALA   B 1 56  ? 58.415 -20.135 -4.293  1.00 14.10 ?  56  ALA   B CA   1 
ATOM   4844 C  C    . ALA   B 1 56  ? 58.694 -18.640 -4.294  1.00 13.87 ?  56  ALA   B C    1 
ATOM   4845 O  O    . ALA   B 1 56  ? 59.424 -18.147 -5.164  1.00 15.17 ?  56  ALA   B O    1 
ATOM   4846 C  CB   . ALA   B 1 56  ? 57.216 -20.465 -5.182  1.00 15.10 ?  56  ALA   B CB   1 
ATOM   4847 H  H    . ALA   B 1 56  ? 57.412 -20.954 -2.800  1.00 16.10 ?  56  ALA   B H    1 
ATOM   4848 H  HA   . ALA   B 1 56  ? 59.192 -20.572 -4.667  1.00 16.97 ?  56  ALA   B HA   1 
ATOM   4849 H  HB1  . ALA   B 1 56  ? 57.386 -20.132 -6.079  1.00 18.17 ?  56  ALA   B HB1  1 
ATOM   4850 H  HB2  . ALA   B 1 56  ? 57.101 -21.429 -5.206  1.00 18.17 ?  56  ALA   B HB2  1 
ATOM   4851 H  HB3  . ALA   B 1 56  ? 56.423 -20.045 -4.818  1.00 18.17 ?  56  ALA   B HB3  1 
ATOM   4852 N  N    . THR   B 1 57  ? 58.128 -17.904 -3.334  1.00 13.77 ?  57  THR   B N    1 
ATOM   4853 C  CA   . THR   B 1 57  ? 58.364 -16.469 -3.207  1.00 13.90 ?  57  THR   B CA   1 
ATOM   4854 C  C    . THR   B 1 57  ? 59.614 -16.144 -2.395  1.00 14.51 ?  57  THR   B C    1 
ATOM   4855 O  O    . THR   B 1 57  ? 59.845 -14.967 -2.083  1.00 14.81 ?  57  THR   B O    1 
ATOM   4856 C  CB   . THR   B 1 57  ? 57.163 -15.741 -2.571  1.00 12.99 ?  57  THR   B CB   1 
ATOM   4857 O  OG1  . THR   B 1 57  ? 57.142 -15.956 -1.151  1.00 13.50 ?  57  THR   B OG1  1 
ATOM   4858 C  CG2  . THR   B 1 57  ? 55.843 -16.155 -3.209  1.00 12.92 ?  57  THR   B CG2  1 
ATOM   4859 H  H    . THR   B 1 57  ? 57.582 -18.215 -2.743  1.00 16.57 ?  57  THR   B H    1 
ATOM   4860 H  HA   . THR   B 1 57  ? 58.485 -16.101 -4.097  1.00 16.73 ?  57  THR   B HA   1 
ATOM   4861 H  HB   . THR   B 1 57  ? 57.270 -14.789 -2.735  1.00 15.63 ?  57  THR   B HB   1 
ATOM   4862 H  HG1  . THR   B 1 57  ? 57.072 -16.774 -0.988  1.00 16.25 ?  57  THR   B HG1  1 
ATOM   4863 H  HG21 . THR   B 1 57  ? 55.120 -15.621 -2.851  1.00 15.55 ?  57  THR   B HG21 1 
ATOM   4864 H  HG22 . THR   B 1 57  ? 55.885 -16.026 -4.171  1.00 15.55 ?  57  THR   B HG22 1 
ATOM   4865 H  HG23 . THR   B 1 57  ? 55.666 -17.090 -3.028  1.00 15.55 ?  57  THR   B HG23 1 
ATOM   4866 N  N    . ASN   B 1 58  ? 60.413 -17.146 -2.036  1.00 15.31 ?  58  ASN   B N    1 
ATOM   4867 C  CA   . ASN   B 1 58  ? 61.611 -16.928 -1.232  1.00 18.45 ?  58  ASN   B CA   1 
ATOM   4868 C  C    . ASN   B 1 58  ? 61.277 -16.221 0.082   1.00 15.83 ?  58  ASN   B C    1 
ATOM   4869 O  O    . ASN   B 1 58  ? 62.011 -15.346 0.547   1.00 16.54 ?  58  ASN   B O    1 
ATOM   4870 C  CB   . ASN   B 1 58  ? 62.692 -16.174 -2.014  1.00 26.82 ?  58  ASN   B CB   1 
ATOM   4871 C  CG   . ASN   B 1 58  ? 64.067 -16.314 -1.386  1.00 36.15 ?  58  ASN   B CG   1 
ATOM   4872 O  OD1  . ASN   B 1 58  ? 64.362 -17.309 -0.725  1.00 38.94 ?  58  ASN   B OD1  1 
ATOM   4873 N  ND2  . ASN   B 1 58  ? 64.915 -15.312 -1.588  1.00 43.07 ?  58  ASN   B ND2  1 
ATOM   4874 H  H    . ASN   B 1 58  ? 60.279 -17.973 -2.249  1.00 18.42 ?  58  ASN   B H    1 
ATOM   4875 H  HA   . ASN   B 1 58  ? 61.980 -17.797 -1.011  1.00 22.19 ?  58  ASN   B HA   1 
ATOM   4876 H  HB2  . ASN   B 1 58  ? 62.737 -16.527 -2.920  1.00 32.23 ?  58  ASN   B HB2  1 
ATOM   4877 H  HB3  . ASN   B 1 58  ? 62.470 -15.231 -2.038  1.00 32.23 ?  58  ASN   B HB3  1 
ATOM   4878 H  HD21 . ASN   B 1 58  ? 65.707 -15.346 -1.253  1.00 51.74 ?  58  ASN   B HD21 1 
ATOM   4879 H  HD22 . ASN   B 1 58  ? 64.674 -14.631 -2.053  1.00 51.74 ?  58  ASN   B HD22 1 
ATOM   4880 N  N    . ASN   B 1 59  ? 60.153 -16.607 0.688   1.00 14.77 ?  59  ASN   B N    1 
ATOM   4881 C  CA   . ASN   B 1 59  ? 59.676 -16.131 1.989   1.00 14.67 ?  59  ASN   B CA   1 
ATOM   4882 C  C    . ASN   B 1 59  ? 59.077 -14.728 1.930   1.00 14.31 ?  59  ASN   B C    1 
ATOM   4883 O  O    . ASN   B 1 59  ? 58.648 -14.218 2.974   1.00 14.27 ?  59  ASN   B O    1 
ATOM   4884 C  CB   . ASN   B 1 59  ? 60.748 -16.178 3.094   1.00 16.19 ?  59  ASN   B CB   1 
ATOM   4885 C  CG   . ASN   B 1 59  ? 60.160 -16.368 4.477   1.00 17.25 ?  59  ASN   B CG   1 
ATOM   4886 O  OD1  . ASN   B 1 59  ? 59.336 -17.258 4.699   1.00 17.25 ?  59  ASN   B OD1  1 
ATOM   4887 N  ND2  . ASN   B 1 59  ? 60.581 -15.534 5.420   1.00 18.01 ?  59  ASN   B ND2  1 
ATOM   4888 H  H    . ASN   B 1 59  ? 59.619 -17.193 0.346   1.00 17.77 ?  59  ASN   B H    1 
ATOM   4889 H  HA   . ASN   B 1 59  ? 58.970 -16.728 2.274   1.00 17.65 ?  59  ASN   B HA   1 
ATOM   4890 H  HB2  . ASN   B 1 59  ? 61.350 -16.920 2.930   1.00 19.47 ?  59  ASN   B HB2  1 
ATOM   4891 H  HB3  . ASN   B 1 59  ? 61.240 -15.344 3.099   1.00 19.47 ?  59  ASN   B HB3  1 
ATOM   4892 H  HD21 . ASN   B 1 59  ? 60.272 -15.599 6.221   1.00 21.66 ?  59  ASN   B HD21 1 
ATOM   4893 H  HD22 . ASN   B 1 59  ? 61.155 -14.925 5.229   1.00 21.66 ?  59  ASN   B HD22 1 
ATOM   4894 N  N    . ALA   B 1 60  ? 59.011 -14.090 0.758   1.00 13.89 ?  60  ALA   B N    1 
ATOM   4895 C  CA   . ALA   B 1 60  ? 58.418 -12.756 0.685   1.00 13.87 ?  60  ALA   B CA   1 
ATOM   4896 C  C    . ALA   B 1 60  ? 56.948 -12.778 1.087   1.00 13.25 ?  60  ALA   B C    1 
ATOM   4897 O  O    . ALA   B 1 60  ? 56.444 -11.822 1.693   1.00 13.71 ?  60  ALA   B O    1 
ATOM   4898 C  CB   . ALA   B 1 60  ? 58.582 -12.179 -0.720  1.00 15.13 ?  60  ALA   B CB   1 
ATOM   4899 H  H    . ALA   B 1 60  ? 59.298 -14.405 0.012   1.00 16.71 ?  60  ALA   B H    1 
ATOM   4900 H  HA   . ALA   B 1 60  ? 58.884 -12.176 1.306   1.00 16.69 ?  60  ALA   B HA   1 
ATOM   4901 H  HB1  . ALA   B 1 60  ? 58.187 -11.296 -0.745  1.00 18.21 ?  60  ALA   B HB1  1 
ATOM   4902 H  HB2  . ALA   B 1 60  ? 59.532 -12.123 -0.928  1.00 18.21 ?  60  ALA   B HB2  1 
ATOM   4903 H  HB3  . ALA   B 1 60  ? 58.141 -12.762 -1.356  1.00 18.21 ?  60  ALA   B HB3  1 
ATOM   4904 N  N    . MET   B 1 61  ? 56.241 -13.855 0.745   1.00 12.58 ?  61  MET   B N    1 
ATOM   4905 C  CA   . MET   B 1 61  ? 54.845 -13.976 1.141   1.00 12.21 ?  61  MET   B CA   1 
ATOM   4906 C  C    . MET   B 1 61  ? 54.712 -13.985 2.663   1.00 12.18 ?  61  MET   B C    1 
ATOM   4907 O  O    . MET   B 1 61  ? 53.810 -13.341 3.216   1.00 12.00 ?  61  MET   B O    1 
ATOM   4908 C  CB   . MET   B 1 61  ? 54.263 -15.243 0.511   1.00 12.05 ?  61  MET   B CB   1 
ATOM   4909 C  CG   . MET   B 1 61  ? 52.823 -15.539 0.926   1.00 11.96 ?  61  MET   B CG   1 
ATOM   4910 S  SD   . MET   B 1 61  ? 52.182 -17.043 0.163   1.00 12.63 ?  61  MET   B SD   1 
ATOM   4911 C  CE   . MET   B 1 61  ? 51.919 -16.457 -1.511  1.00 13.90 ?  61  MET   B CE   1 
ATOM   4912 H  H    . MET   B 1 61  ? 56.543 -14.528 0.288   1.00 15.14 ?  61  MET   B H    1 
ATOM   4913 H  HA   . MET   B 1 61  ? 54.352 -13.220 0.782   1.00 14.70 ?  61  MET   B HA   1 
ATOM   4914 H  HB2  . MET   B 1 61  ? 54.275 -15.150 -0.456  1.00 14.51 ?  61  MET   B HB2  1 
ATOM   4915 H  HB3  . MET   B 1 61  ? 54.807 -16.001 0.772   1.00 14.51 ?  61  MET   B HB3  1 
ATOM   4916 H  HG2  . MET   B 1 61  ? 52.783 -15.655 1.889   1.00 14.41 ?  61  MET   B HG2  1 
ATOM   4917 H  HG3  . MET   B 1 61  ? 52.254 -14.801 0.656   1.00 14.41 ?  61  MET   B HG3  1 
ATOM   4918 H  HE1  . MET   B 1 61  ? 51.538 -17.173 -2.041  1.00 16.73 ?  61  MET   B HE1  1 
ATOM   4919 H  HE2  . MET   B 1 61  ? 51.307 -15.701 -1.490  1.00 16.73 ?  61  MET   B HE2  1 
ATOM   4920 H  HE3  . MET   B 1 61  ? 52.768 -16.179 -1.889  1.00 16.73 ?  61  MET   B HE3  1 
ATOM   4921 N  N    . GLN   B 1 62  ? 55.596 -14.704 3.361   1.00 12.20 ?  62  GLN   B N    1 
ATOM   4922 C  CA   . GLN   B 1 62  ? 55.490 -14.761 4.816   1.00 12.62 ?  62  GLN   B CA   1 
ATOM   4923 C  C    . GLN   B 1 62  ? 55.772 -13.407 5.450   1.00 12.90 ?  62  GLN   B C    1 
ATOM   4924 O  O    . GLN   B 1 62  ? 55.088 -13.006 6.400   1.00 13.57 ?  62  GLN   B O    1 
ATOM   4925 C  CB   . GLN   B 1 62  ? 56.443 -15.810 5.383   1.00 12.80 ?  62  GLN   B CB   1 
ATOM   4926 C  CG   . GLN   B 1 62  ? 56.224 -16.076 6.863   1.00 13.14 ?  62  GLN   B CG   1 
ATOM   4927 C  CD   . GLN   B 1 62  ? 54.849 -16.670 7.110   1.00 12.80 ?  62  GLN   B CD   1 
ATOM   4928 O  OE1  . GLN   B 1 62  ? 54.594 -17.823 6.758   1.00 13.22 ?  62  GLN   B OE1  1 
ATOM   4929 N  NE2  . GLN   B 1 62  ? 53.936 -15.877 7.667   1.00 13.30 ?  62  GLN   B NE2  1 
ATOM   4930 H  H    . GLN   B 1 62  ? 56.246 -15.158 3.020   1.00 14.68 ?  62  GLN   B H    1 
ATOM   4931 H  HA   . GLN   B 1 62  ? 54.585 -15.019 5.046   1.00 15.19 ?  62  GLN   B HA   1 
ATOM   4932 H  HB2  . GLN   B 1 62  ? 56.315 -16.646 4.906   1.00 15.41 ?  62  GLN   B HB2  1 
ATOM   4933 H  HB3  . GLN   B 1 62  ? 57.356 -15.502 5.266   1.00 15.41 ?  62  GLN   B HB3  1 
ATOM   4934 H  HG2  . GLN   B 1 62  ? 56.890 -16.711 7.173   1.00 15.81 ?  62  GLN   B HG2  1 
ATOM   4935 H  HG3  . GLN   B 1 62  ? 56.295 -15.246 7.355   1.00 15.81 ?  62  GLN   B HG3  1 
ATOM   4936 H  HE21 . GLN   B 1 62  ? 54.142 -15.072 7.886   1.00 16.00 ?  62  GLN   B HE21 1 
ATOM   4937 H  HE22 . GLN   B 1 62  ? 53.142 -16.174 7.816   1.00 16.00 ?  62  GLN   B HE22 1 
ATOM   4938 N  N    . VAL   B 1 63  ? 56.789 -12.695 4.960   1.00 13.40 ?  63  VAL   B N    1 
ATOM   4939 C  CA   . VAL   B 1 63  ? 57.095 -11.376 5.510   1.00 14.35 ?  63  VAL   B CA   1 
ATOM   4940 C  C    . VAL   B 1 63  ? 55.903 -10.443 5.333   1.00 13.55 ?  63  VAL   B C    1 
ATOM   4941 O  O    . VAL   B 1 63  ? 55.493 -9.737  6.267   1.00 14.14 ?  63  VAL   B O    1 
ATOM   4942 C  CB   . VAL   B 1 63  ? 58.380 -10.815 4.877   1.00 15.69 ?  63  VAL   B CB   1 
ATOM   4943 C  CG1  . VAL   B 1 63  ? 58.609 -9.374  5.318   1.00 16.31 ?  63  VAL   B CG1  1 
ATOM   4944 C  CG2  . VAL   B 1 63  ? 59.570 -11.686 5.267   1.00 16.39 ?  63  VAL   B CG2  1 
ATOM   4945 H  H    . VAL   B 1 63  ? 57.303 -12.948 4.315   1.00 16.13 ?  63  VAL   B H    1 
ATOM   4946 H  HA   . VAL   B 1 63  ? 57.258 -11.471 6.458   1.00 17.26 ?  63  VAL   B HA   1 
ATOM   4947 H  HB   . VAL   B 1 63  ? 58.305 -10.834 3.911   1.00 18.88 ?  63  VAL   B HB   1 
ATOM   4948 H  HG11 . VAL   B 1 63  ? 59.526 -9.131  5.128   1.00 19.62 ?  63  VAL   B HG11 1 
ATOM   4949 H  HG12 . VAL   B 1 63  ? 58.002 -8.800  4.832   1.00 19.62 ?  63  VAL   B HG12 1 
ATOM   4950 H  HG13 . VAL   B 1 63  ? 58.440 -9.313  6.272   1.00 19.62 ?  63  VAL   B HG13 1 
ATOM   4951 H  HG21 . VAL   B 1 63  ? 60.380 -11.314 4.882   1.00 19.71 ?  63  VAL   B HG21 1 
ATOM   4952 H  HG22 . VAL   B 1 63  ? 59.648 -11.702 6.237   1.00 19.71 ?  63  VAL   B HG22 1 
ATOM   4953 H  HG23 . VAL   B 1 63  ? 59.432 -12.587 4.936   1.00 19.71 ?  63  VAL   B HG23 1 
ATOM   4954 N  N    . GLU   B 1 64  ? 55.330 -10.428 4.128   1.00 13.14 ?  64  GLU   B N    1 
ATOM   4955 C  CA   . GLU   B 1 64  ? 54.164 -9.591  3.857   1.00 12.75 ?  64  GLU   B CA   1 
ATOM   4956 C  C    . GLU   B 1 64  ? 52.982 -9.992  4.734   1.00 12.24 ?  64  GLU   B C    1 
ATOM   4957 O  O    . GLU   B 1 64  ? 52.235 -9.132  5.229   1.00 12.99 ?  64  GLU   B O    1 
ATOM   4958 C  CB   . GLU   B 1 64  ? 53.802 -9.735  2.377   1.00 12.88 ?  64  GLU   B CB   1 
ATOM   4959 C  CG   . GLU   B 1 64  ? 52.534 -9.012  1.943   1.00 13.11 ?  64  GLU   B CG   1 
ATOM   4960 C  CD   . GLU   B 1 64  ? 52.006 -9.512  0.604   1.00 13.94 ?  64  GLU   B CD   1 
ATOM   4961 O  OE1  . GLU   B 1 64  ? 52.188 -10.722 0.283   1.00 14.63 ?  64  GLU   B OE1  1 
ATOM   4962 O  OE2  . GLU   B 1 64  ? 51.383 -8.691  -0.114  1.00 14.68 -1 64  GLU   B OE2  1 
ATOM   4963 H  H    . GLU   B 1 64  ? 55.603 -10.889 3.449   1.00 15.82 ?  64  GLU   B H    1 
ATOM   4964 H  HA   . GLU   B 1 64  ? 54.379 -8.665  4.034   1.00 15.35 ?  64  GLU   B HA   1 
ATOM   4965 H  HB2  . GLU   B 1 64  ? 54.529 -9.371  1.842   1.00 15.51 ?  64  GLU   B HB2  1 
ATOM   4966 H  HB3  . GLU   B 1 64  ? 53.686 -10.671 2.173   1.00 15.51 ?  64  GLU   B HB3  1 
ATOM   4967 H  HG2  . GLU   B 1 64  ? 51.831 -9.150  2.603   1.00 15.78 ?  64  GLU   B HG2  1 
ATOM   4968 H  HG3  . GLU   B 1 64  ? 52.717 -8.062  1.859   1.00 15.78 ?  64  GLU   B HG3  1 
ATOM   4969 N  N    . SER   B 1 65  ? 52.802 -11.300 4.929   1.00 12.15 ?  65  SER   B N    1 
ATOM   4970 C  CA   . SER   B 1 65  ? 51.692 -11.808 5.727   1.00 12.14 ?  65  SER   B CA   1 
ATOM   4971 C  C    . SER   B 1 65  ? 51.821 -11.410 7.190   1.00 12.21 ?  65  SER   B C    1 
ATOM   4972 O  O    . SER   B 1 65  ? 50.822 -11.039 7.824   1.00 12.81 ?  65  SER   B O    1 
ATOM   4973 C  CB   . SER   B 1 65  ? 51.617 -13.329 5.594   1.00 12.47 ?  65  SER   B CB   1 
ATOM   4974 O  OG   . SER   B 1 65  ? 51.260 -13.727 4.278   1.00 12.60 ?  65  SER   B OG   1 
ATOM   4975 H  H    . SER   B 1 65  ? 53.313 -11.922 4.611   1.00 14.63 ?  65  SER   B H    1 
ATOM   4976 H  HA   . SER   B 1 65  ? 50.861 -11.438 5.385   1.00 14.62 ?  65  SER   B HA   1 
ATOM   4977 H  HB2  . SER   B 1 65  ? 52.478 -13.709 5.810   1.00 15.01 ?  65  SER   B HB2  1 
ATOM   4978 H  HB3  . SER   B 1 65  ? 50.943 -13.663 6.212   1.00 15.01 ?  65  SER   B HB3  1 
ATOM   4979 H  HG   . SER   B 1 65  ? 51.827 -13.437 3.726   1.00 15.16 ?  65  SER   B HG   1 
ATOM   4980 N  N    . ASP   B 1 66  ? 53.030 -11.504 7.756   1.00 12.95 ?  66  ASP   B N    1 
ATOM   4981 C  CA   . ASP   B 1 66  ? 53.214 -11.114 9.152   1.00 12.88 ?  66  ASP   B CA   1 
ATOM   4982 C  C    . ASP   B 1 66  ? 52.905 -9.634  9.352   1.00 13.05 ?  66  ASP   B C    1 
ATOM   4983 O  O    . ASP   B 1 66  ? 52.325 -9.243  10.373  1.00 13.71 ?  66  ASP   B O    1 
ATOM   4984 C  CB   . ASP   B 1 66  ? 54.641 -11.419 9.609   1.00 14.35 ?  66  ASP   B CB   1 
ATOM   4985 C  CG   . ASP   B 1 66  ? 54.914 -12.914 9.761   1.00 16.34 ?  66  ASP   B CG   1 
ATOM   4986 O  OD1  . ASP   B 1 66  ? 53.969 -13.732 9.673   1.00 16.83 ?  66  ASP   B OD1  1 
ATOM   4987 O  OD2  . ASP   B 1 66  ? 56.093 -13.278 9.979   1.00 19.12 -1 66  ASP   B OD2  1 
ATOM   4988 H  H    . ASP   B 1 66  ? 53.734 -11.798 7.367   1.00 15.59 ?  66  ASP   B H    1 
ATOM   4989 H  HA   . ASP   B 1 66  ? 52.605 -11.619 9.712   1.00 15.50 ?  66  ASP   B HA   1 
ATOM   4990 H  HB2  . ASP   B 1 66  ? 55.263 -11.071 8.954   1.00 17.26 ?  66  ASP   B HB2  1 
ATOM   4991 H  HB3  . ASP   B 1 66  ? 54.793 -10.989 10.470  1.00 17.26 ?  66  ASP   B HB3  1 
ATOM   4992 N  N    . ASP   B 1 67  ? 53.279 -8.793  8.384   1.00 12.95 ?  67  ASP   B N    1 
ATOM   4993 C  CA   . ASP   B 1 67  ? 52.932 -7.381  8.463   1.00 13.41 ?  67  ASP   B CA   1 
ATOM   4994 C  C    . ASP   B 1 67  ? 51.421 -7.177  8.380   1.00 13.56 ?  67  ASP   B C    1 
ATOM   4995 O  O    . ASP   B 1 67  ? 50.857 -6.373  9.131   1.00 14.13 ?  67  ASP   B O    1 
ATOM   4996 C  CB   . ASP   B 1 67  ? 53.647 -6.619  7.356   1.00 14.84 ?  67  ASP   B CB   1 
ATOM   4997 C  CG   . ASP   B 1 67  ? 53.221 -5.177  7.305   1.00 16.09 ?  67  ASP   B CG   1 
ATOM   4998 O  OD1  . ASP   B 1 67  ? 53.714 -4.363  8.123   1.00 17.38 ?  67  ASP   B OD1  1 
ATOM   4999 O  OD2  . ASP   B 1 67  ? 52.353 -4.877  6.473   1.00 17.05 -1 67  ASP   B OD2  1 
ATOM   5000 H  H    . ASP   B 1 67  ? 53.737 -9.015  7.689   1.00 15.58 ?  67  ASP   B H    1 
ATOM   5001 H  HA   . ASP   B 1 67  ? 53.236 -7.028  9.311   1.00 16.14 ?  67  ASP   B HA   1 
ATOM   5002 H  HB2  . ASP   B 1 67  ? 54.607 -6.649  7.514   1.00 17.86 ?  67  ASP   B HB2  1 
ATOM   5003 H  HB3  . ASP   B 1 67  ? 53.446 -7.036  6.498   1.00 17.86 ?  67  ASP   B HB3  1 
ATOM   5004 N  N    . TYR   B 1 68  ? 50.746 -7.910  7.485   1.00 13.34 ?  68  TYR   B N    1 
ATOM   5005 C  CA   . TYR   B 1 68  ? 49.288 -7.838  7.414   1.00 13.97 ?  68  TYR   B CA   1 
ATOM   5006 C  C    . TYR   B 1 68  ? 48.655 -8.177  8.760   1.00 13.54 ?  68  TYR   B C    1 
ATOM   5007 O  O    . TYR   B 1 68  ? 47.717 -7.502  9.203   1.00 14.52 ?  68  TYR   B O    1 
ATOM   5008 C  CB   . TYR   B 1 68  ? 48.753 -8.776  6.326   1.00 14.87 ?  68  TYR   B CB   1 
ATOM   5009 C  CG   . TYR   B 1 68  ? 47.248 -8.925  6.388   1.00 15.95 ?  68  TYR   B CG   1 
ATOM   5010 C  CD1  . TYR   B 1 68  ? 46.660 -9.883  7.210   1.00 16.88 ?  68  TYR   B CD1  1 
ATOM   5011 C  CD2  . TYR   B 1 68  ? 46.419 -8.092  5.658   1.00 16.87 ?  68  TYR   B CD2  1 
ATOM   5012 C  CE1  . TYR   B 1 68  ? 45.294 -10.003 7.301   1.00 17.69 ?  68  TYR   B CE1  1 
ATOM   5013 C  CE2  . TYR   B 1 68  ? 45.038 -8.217  5.736   1.00 17.10 ?  68  TYR   B CE2  1 
ATOM   5014 C  CZ   . TYR   B 1 68  ? 44.495 -9.171  6.560   1.00 17.53 ?  68  TYR   B CZ   1 
ATOM   5015 O  OH   . TYR   B 1 68  ? 43.127 -9.287  6.652   1.00 18.44 ?  68  TYR   B OH   1 
ATOM   5016 H  H    . TYR   B 1 68  ? 51.108 -8.456  6.917   1.00 16.05 ?  68  TYR   B H    1 
ATOM   5017 H  HA   . TYR   B 1 68  ? 49.034 -6.935  7.184   1.00 16.82 ?  68  TYR   B HA   1 
ATOM   5018 H  HB2  . TYR   B 1 68  ? 48.981 -8.417  5.457   1.00 17.90 ?  68  TYR   B HB2  1 
ATOM   5019 H  HB3  . TYR   B 1 68  ? 49.148 -9.655  6.440   1.00 17.90 ?  68  TYR   B HB3  1 
ATOM   5020 H  HD1  . TYR   B 1 68  ? 47.200 -10.452 7.715   1.00 20.31 ?  68  TYR   B HD1  1 
ATOM   5021 H  HD2  . TYR   B 1 68  ? 46.794 -7.442  5.115   1.00 20.29 ?  68  TYR   B HD2  1 
ATOM   5022 H  HE1  . TYR   B 1 68  ? 44.912 -10.659 7.846   1.00 21.27 ?  68  TYR   B HE1  1 
ATOM   5023 H  HE2  . TYR   B 1 68  ? 44.486 -7.652  5.246   1.00 20.57 ?  68  TYR   B HE2  1 
ATOM   5024 H  HH   . TYR   B 1 68  ? 42.742 -8.730  6.143   1.00 22.17 ?  68  TYR   B HH   1 
ATOM   5025 N  N    . ILE   B 1 69  ? 49.142 -9.236  9.412   1.00 13.38 ?  69  ILE   B N    1 
ATOM   5026 C  CA   . ILE   B 1 69  ? 48.584 -9.662  10.693  1.00 13.78 ?  69  ILE   B CA   1 
ATOM   5027 C  C    . ILE   B 1 69  ? 48.836 -8.615  11.771  1.00 13.33 ?  69  ILE   B C    1 
ATOM   5028 O  O    . ILE   B 1 69  ? 47.968 -8.341  12.607  1.00 13.76 ?  69  ILE   B O    1 
ATOM   5029 C  CB   . ILE   B 1 69  ? 49.161 -11.038 11.085  1.00 14.64 ?  69  ILE   B CB   1 
ATOM   5030 C  CG1  . ILE   B 1 69  ? 48.628 -12.145 10.163  1.00 15.18 ?  69  ILE   B CG1  1 
ATOM   5031 C  CG2  . ILE   B 1 69  ? 48.883 -11.348 12.552  1.00 15.31 ?  69  ILE   B CG2  1 
ATOM   5032 C  CD1  . ILE   B 1 69  ? 47.149 -12.455 10.332  1.00 15.33 ?  69  ILE   B CD1  1 
ATOM   5033 H  H    . ILE   B 1 69  ? 49.797 -9.723  9.136   1.00 16.10 ?  69  ILE   B H    1 
ATOM   5034 H  HA   . ILE   B 1 69  ? 47.627 -9.759  10.598  1.00 16.59 ?  69  ILE   B HA   1 
ATOM   5035 H  HB   . ILE   B 1 69  ? 50.125 -11.000 10.972  1.00 17.62 ?  69  ILE   B HB   1 
ATOM   5036 H  HG12 . ILE   B 1 69  ? 48.770 -11.869 9.243   1.00 18.27 ?  69  ILE   B HG12 1 
ATOM   5037 H  HG13 . ILE   B 1 69  ? 49.125 -12.958 10.339  1.00 18.27 ?  69  ILE   B HG13 1 
ATOM   5038 H  HG21 . ILE   B 1 69  ? 49.017 -12.299 12.701  1.00 18.41 ?  69  ILE   B HG21 1 
ATOM   5039 H  HG22 . ILE   B 1 69  ? 49.495 -10.842 13.108  1.00 18.41 ?  69  ILE   B HG22 1 
ATOM   5040 H  HG23 . ILE   B 1 69  ? 47.967 -11.110 12.757  1.00 18.41 ?  69  ILE   B HG23 1 
ATOM   5041 H  HD11 . ILE   B 1 69  ? 46.910 -13.169 9.723   1.00 18.45 ?  69  ILE   B HD11 1 
ATOM   5042 H  HD12 . ILE   B 1 69  ? 46.987 -12.733 11.247  1.00 18.45 ?  69  ILE   B HD12 1 
ATOM   5043 H  HD13 . ILE   B 1 69  ? 46.632 -11.661 10.130  1.00 18.45 ?  69  ILE   B HD13 1 
ATOM   5044 N  N    . ALA   B 1 70  ? 50.031 -8.028  11.790  1.00 13.36 ?  70  ALA   B N    1 
ATOM   5045 C  CA   . ALA   B 1 70  ? 50.309 -6.991  12.777  1.00 13.41 ?  70  ALA   B CA   1 
ATOM   5046 C  C    . ALA   B 1 70  ? 49.308 -5.852  12.664  1.00 13.93 ?  70  ALA   B C    1 
ATOM   5047 O  O    . ALA   B 1 70  ? 48.871 -5.301  13.679  1.00 14.32 ?  70  ALA   B O    1 
ATOM   5048 C  CB   . ALA   B 1 70  ? 51.735 -6.471  12.606  1.00 14.18 ?  70  ALA   B CB   1 
ATOM   5049 H  H    . ALA   B 1 70  ? 50.677 -8.210  11.261  1.00 16.08 ?  70  ALA   B H    1 
ATOM   5050 H  HA   . ALA   B 1 70  ? 50.234 -7.368  13.668  1.00 16.14 ?  70  ALA   B HA   1 
ATOM   5051 H  HB1  . ALA   B 1 70  ? 51.919 -5.814  13.297  1.00 17.06 ?  70  ALA   B HB1  1 
ATOM   5052 H  HB2  . ALA   B 1 70  ? 52.356 -7.214  12.686  1.00 17.06 ?  70  ALA   B HB2  1 
ATOM   5053 H  HB3  . ALA   B 1 70  ? 51.823 -6.063  11.729  1.00 17.06 ?  70  ALA   B HB3  1 
ATOM   5054 N  N    . THR   B 1 71  ? 48.931 -5.491  11.438  1.00 14.45 ?  71  THR   B N    1 
ATOM   5055 C  CA   . THR   B 1 71  ? 48.039 -4.356  11.228  1.00 15.56 ?  71  THR   B CA   1 
ATOM   5056 C  C    . THR   B 1 71  ? 46.573 -4.725  11.435  1.00 16.28 ?  71  THR   B C    1 
ATOM   5057 O  O    . THR   B 1 71  ? 45.792 -3.908  11.943  1.00 17.66 ?  71  THR   B O    1 
ATOM   5058 C  CB   . THR   B 1 71  ? 48.254 -3.786  9.824   1.00 17.36 ?  71  THR   B CB   1 
ATOM   5059 O  OG1  . THR   B 1 71  ? 49.573 -3.235  9.731   1.00 19.47 ?  71  THR   B OG1  1 
ATOM   5060 C  CG2  . THR   B 1 71  ? 47.226 -2.708  9.499   1.00 18.25 ?  71  THR   B CG2  1 
ATOM   5061 H  H    . THR   B 1 71  ? 49.183 -5.887  10.715  1.00 17.39 ?  71  THR   B H    1 
ATOM   5062 H  HA   . THR   B 1 71  ? 48.264 -3.662  11.862  1.00 18.72 ?  71  THR   B HA   1 
ATOM   5063 H  HB   . THR   B 1 71  ? 48.170 -4.495  9.167   1.00 20.87 ?  71  THR   B HB   1 
ATOM   5064 H  HG1  . THR   B 1 71  ? 49.703 -2.906  8.962   1.00 23.41 ?  71  THR   B HG1  1 
ATOM   5065 H  HG21 . THR   B 1 71  ? 47.529 -2.176  8.745   1.00 21.94 ?  71  THR   B HG21 1 
ATOM   5066 H  HG22 . THR   B 1 71  ? 46.377 -3.115  9.273   1.00 21.94 ?  71  THR   B HG22 1 
ATOM   5067 H  HG23 . THR   B 1 71  ? 47.106 -2.124  10.264  1.00 21.94 ?  71  THR   B HG23 1 
ATOM   5068 N  N    . ASN   B 1 72  ? 46.182 -5.944  11.047  1.00 15.67 ?  72  ASN   B N    1 
ATOM   5069 C  CA   . ASN   B 1 72  ? 44.777 -6.304  10.922  1.00 16.01 ?  72  ASN   B CA   1 
ATOM   5070 C  C    . ASN   B 1 72  ? 44.308 -7.403  11.865  1.00 16.36 ?  72  ASN   B C    1 
ATOM   5071 O  O    . ASN   B 1 72  ? 43.092 -7.566  12.030  1.00 17.74 ?  72  ASN   B O    1 
ATOM   5072 C  CB   . ASN   B 1 72  ? 44.469 -6.734  9.479   1.00 16.97 ?  72  ASN   B CB   1 
ATOM   5073 C  CG   . ASN   B 1 72  ? 44.745 -5.637  8.483   1.00 17.93 ?  72  ASN   B CG   1 
ATOM   5074 O  OD1  . ASN   B 1 72  ? 45.759 -5.650  7.782   1.00 19.26 ?  72  ASN   B OD1  1 
ATOM   5075 N  ND2  . ASN   B 1 72  ? 43.865 -4.657  8.440   1.00 19.62 ?  72  ASN   B ND2  1 
ATOM   5076 H  H    . ASN   B 1 72  ? 46.725 -6.585  10.841  1.00 18.85 ?  72  ASN   B H    1 
ATOM   5077 H  HA   . ASN   B 1 72  ? 44.247 -5.516  11.105  1.00 19.26 ?  72  ASN   B HA   1 
ATOM   5078 H  HB2  . ASN   B 1 72  ? 45.026 -7.495  9.246   1.00 20.41 ?  72  ASN   B HB2  1 
ATOM   5079 H  HB3  . ASN   B 1 72  ? 43.533 -6.971  9.412   1.00 20.41 ?  72  ASN   B HB3  1 
ATOM   5080 H  HD21 . ASN   B 1 72  ? 43.969 -4.005  7.888   1.00 23.59 ?  72  ASN   B HD21 1 
ATOM   5081 H  HD22 . ASN   B 1 72  ? 43.166 -4.681  8.945   1.00 23.59 ?  72  ASN   B HD22 1 
ATOM   5082 N  N    . GLY   B 1 73  ? 45.212 -8.152  12.485  1.00 15.98 ?  73  GLY   B N    1 
ATOM   5083 C  CA   . GLY   B 1 73  ? 44.813 -9.291  13.275  1.00 15.55 ?  73  GLY   B CA   1 
ATOM   5084 C  C    . GLY   B 1 73  ? 44.452 -10.477 12.405  1.00 13.89 ?  73  GLY   B C    1 
ATOM   5085 O  O    . GLY   B 1 73  ? 44.440 -10.395 11.174  1.00 13.86 ?  73  GLY   B O    1 
ATOM   5086 H  H    . GLY   B 1 73  ? 46.063 -8.014  12.463  1.00 19.22 ?  73  GLY   B H    1 
ATOM   5087 H  HA2  . GLY   B 1 73  ? 45.540 -9.545  13.865  1.00 18.71 ?  73  GLY   B HA2  1 
ATOM   5088 H  HA3  . GLY   B 1 73  ? 44.043 -9.056  13.817  1.00 18.71 ?  73  GLY   B HA3  1 
ATOM   5089 N  N    . PRO   B 1 74  ? 44.145 -11.604 13.045  1.00 14.26 ?  74  PRO   B N    1 
ATOM   5090 C  CA   . PRO   B 1 74  ? 43.896 -12.836 12.299  1.00 13.84 ?  74  PRO   B CA   1 
ATOM   5091 C  C    . PRO   B 1 74  ? 42.598 -12.782 11.508  1.00 13.39 ?  74  PRO   B C    1 
ATOM   5092 O  O    . PRO   B 1 74  ? 41.657 -12.048 11.834  1.00 14.48 ?  74  PRO   B O    1 
ATOM   5093 C  CB   . PRO   B 1 74  ? 43.818 -13.900 13.401  1.00 14.90 ?  74  PRO   B CB   1 
ATOM   5094 C  CG   . PRO   B 1 74  ? 43.368 -13.150 14.609  1.00 16.52 ?  74  PRO   B CG   1 
ATOM   5095 C  CD   . PRO   B 1 74  ? 44.033 -11.806 14.498  1.00 15.99 ?  74  PRO   B CD   1 
ATOM   5096 H  HA   . PRO   B 1 74  ? 44.640 -13.027 11.701  1.00 16.66 ?  74  PRO   B HA   1 
ATOM   5097 H  HB2  . PRO   B 1 74  ? 43.172 -14.577 13.149  1.00 17.93 ?  74  PRO   B HB2  1 
ATOM   5098 H  HB3  . PRO   B 1 74  ? 44.695 -14.288 13.538  1.00 17.93 ?  74  PRO   B HB3  1 
ATOM   5099 H  HG2  . PRO   B 1 74  ? 42.402 -13.056 14.594  1.00 19.87 ?  74  PRO   B HG2  1 
ATOM   5100 H  HG3  . PRO   B 1 74  ? 43.660 -13.613 15.406  1.00 19.87 ?  74  PRO   B HG3  1 
ATOM   5101 H  HD2  . PRO   B 1 74  ? 43.476 -11.116 14.900  1.00 19.23 ?  74  PRO   B HD2  1 
ATOM   5102 H  HD3  . PRO   B 1 74  ? 44.915 -11.825 14.901  1.00 19.23 ?  74  PRO   B HD3  1 
ATOM   5103 N  N    . LEU   B 1 75  ? 42.568 -13.584 10.450  1.00 12.79 ?  75  LEU   B N    1 
ATOM   5104 C  CA   . LEU   B 1 75  ? 41.355 -13.808 9.687   1.00 12.99 ?  75  LEU   B CA   1 
ATOM   5105 C  C    . LEU   B 1 75  ? 40.384 -14.669 10.491  1.00 13.62 ?  75  LEU   B C    1 
ATOM   5106 O  O    . LEU   B 1 75  ? 40.729 -15.236 11.530  1.00 14.51 ?  75  LEU   B O    1 
ATOM   5107 C  CB   . LEU   B 1 75  ? 41.683 -14.526 8.377   1.00 12.84 ?  75  LEU   B CB   1 
ATOM   5108 C  CG   . LEU   B 1 75  ? 42.529 -13.770 7.345   1.00 14.84 ?  75  LEU   B CG   1 
ATOM   5109 C  CD1  . LEU   B 1 75  ? 42.743 -14.607 6.082   1.00 16.76 ?  75  LEU   B CD1  1 
ATOM   5110 C  CD2  . LEU   B 1 75  ? 41.927 -12.436 6.996   1.00 18.21 ?  75  LEU   B CD2  1 
ATOM   5111 H  H    . LEU   B 1 75  ? 43.247 -14.018 10.150  1.00 15.40 ?  75  LEU   B H    1 
ATOM   5112 H  HA   . LEU   B 1 75  ? 40.925 -12.964 9.481   1.00 15.64 ?  75  LEU   B HA   1 
ATOM   5113 H  HB2  . LEU   B 1 75  ? 42.161 -15.343 8.587   1.00 15.45 ?  75  LEU   B HB2  1 
ATOM   5114 H  HB3  . LEU   B 1 75  ? 40.847 -14.755 7.935   1.00 15.45 ?  75  LEU   B HB3  1 
ATOM   5115 H  HG   . LEU   B 1 75  ? 43.403 -13.605 7.731   1.00 17.85 ?  75  LEU   B HG   1 
ATOM   5116 H  HD11 . LEU   B 1 75  ? 43.290 -14.098 5.456   1.00 20.16 ?  75  LEU   B HD11 1 
ATOM   5117 H  HD12 . LEU   B 1 75  ? 43.200 -15.430 6.318   1.00 20.16 ?  75  LEU   B HD12 1 
ATOM   5118 H  HD13 . LEU   B 1 75  ? 41.885 -14.806 5.681   1.00 20.16 ?  75  LEU   B HD13 1 
ATOM   5119 H  HD21 . LEU   B 1 75  ? 42.437 -12.040 6.273   1.00 21.90 ?  75  LEU   B HD21 1 
ATOM   5120 H  HD22 . LEU   B 1 75  ? 41.007 -12.569 6.722   1.00 21.90 ?  75  LEU   B HD22 1 
ATOM   5121 H  HD23 . LEU   B 1 75  ? 41.961 -11.863 7.778   1.00 21.90 ?  75  LEU   B HD23 1 
ATOM   5122 N  N    . LYS   B 1 76  ? 39.151 -14.753 9.994   1.00 14.66 ?  76  LYS   B N    1 
ATOM   5123 C  CA   . LYS   B 1 76  ? 38.168 -15.715 10.472  1.00 16.06 ?  76  LYS   B CA   1 
ATOM   5124 C  C    . LYS   B 1 76  ? 38.263 -16.988 9.636   1.00 14.57 ?  76  LYS   B C    1 
ATOM   5125 O  O    . LYS   B 1 76  ? 38.535 -16.935 8.438   1.00 14.38 ?  76  LYS   B O    1 
ATOM   5126 C  CB   . LYS   B 1 76  ? 36.750 -15.148 10.297  1.00 18.34 ?  76  LYS   B CB   1 
ATOM   5127 C  CG   . LYS   B 1 76  ? 36.473 -13.765 10.916  1.00 20.50 ?  76  LYS   B CG   1 
ATOM   5128 C  CD   . LYS   B 1 76  ? 35.062 -13.245 10.574  1.00 21.84 ?  76  LYS   B CD   1 
ATOM   5129 C  CE   . LYS   B 1 76  ? 34.799 -11.874 11.180  1.00 23.71 ?  76  LYS   B CE   1 
ATOM   5130 N  NZ   . LYS   B 1 76  ? 33.500 -11.284 10.746  1.00 24.37 ?  76  LYS   B NZ   1 
ATOM   5131 H  H    . LYS   B 1 76  ? 38.854 -14.252 9.360   1.00 17.64 ?  76  LYS   B H    1 
ATOM   5132 H  HA   . LYS   B 1 76  ? 38.319 -15.928 11.408  1.00 19.32 ?  76  LYS   B HA   1 
ATOM   5133 H  HB2  . LYS   B 1 76  ? 36.567 -15.077 9.347   1.00 22.05 ?  76  LYS   B HB2  1 
ATOM   5134 H  HB3  . LYS   B 1 76  ? 36.121 -15.769 10.697  1.00 22.05 ?  76  LYS   B HB3  1 
ATOM   5135 H  HG2  . LYS   B 1 76  ? 36.548 -13.826 11.881  1.00 24.64 ?  76  LYS   B HG2  1 
ATOM   5136 H  HG3  . LYS   B 1 76  ? 37.122 -13.127 10.572  1.00 24.64 ?  76  LYS   B HG3  1 
ATOM   5137 H  HD2  . LYS   B 1 76  ? 34.974 -13.172 9.610   1.00 26.25 ?  76  LYS   B HD2  1 
ATOM   5138 H  HD3  . LYS   B 1 76  ? 34.402 -13.863 10.924  1.00 26.25 ?  76  LYS   B HD3  1 
ATOM   5139 H  HE2  . LYS   B 1 76  ? 34.785 -11.956 12.146  1.00 28.50 ?  76  LYS   B HE2  1 
ATOM   5140 H  HE3  . LYS   B 1 76  ? 35.508 -11.270 10.908  1.00 28.50 ?  76  LYS   B HE3  1 
ATOM   5141 H  HZ1  . LYS   B 1 76  ? 33.388 -10.485 11.123  1.00 29.29 ?  76  LYS   B HZ1  1 
ATOM   5142 H  HZ2  . LYS   B 1 76  ? 33.487 -11.189 9.861   1.00 29.29 ?  76  LYS   B HZ2  1 
ATOM   5143 H  HZ3  . LYS   B 1 76  ? 32.827 -11.814 10.989  1.00 29.29 ?  76  LYS   B HZ3  1 
ATOM   5144 N  N    . VAL   B 1 77  ? 38.017 -18.142 10.268  1.00 15.16 ?  77  VAL   B N    1 
ATOM   5145 C  CA   . VAL   B 1 77  ? 37.812 -19.354 9.484   1.00 15.35 ?  77  VAL   B CA   1 
ATOM   5146 C  C    . VAL   B 1 77  ? 36.620 -19.122 8.568   1.00 14.16 ?  77  VAL   B C    1 
ATOM   5147 O  O    . VAL   B 1 77  ? 35.556 -18.675 9.013   1.00 14.29 ?  77  VAL   B O    1 
ATOM   5148 C  CB   . VAL   B 1 77  ? 37.613 -20.573 10.398  1.00 16.90 ?  77  VAL   B CB   1 
ATOM   5149 C  CG1  . VAL   B 1 77  ? 37.325 -21.808 9.557   1.00 17.47 ?  77  VAL   B CG1  1 
ATOM   5150 C  CG2  . VAL   B 1 77  ? 38.843 -20.795 11.281  1.00 18.41 ?  77  VAL   B CG2  1 
ATOM   5151 H  H    . VAL   B 1 77  ? 37.970 -18.243 11.116  1.00 18.24 ?  77  VAL   B H    1 
ATOM   5152 H  HA   . VAL   B 1 77  ? 38.586 -19.514 8.927   1.00 18.47 ?  77  VAL   B HA   1 
ATOM   5153 H  HB   . VAL   B 1 77  ? 36.847 -20.415 10.974  1.00 20.32 ?  77  VAL   B HB   1 
ATOM   5154 H  HG11 . VAL   B 1 77  ? 37.381 -22.592 10.125  1.00 21.01 ?  77  VAL   B HG11 1 
ATOM   5155 H  HG12 . VAL   B 1 77  ? 36.430 -21.739 9.183   1.00 21.01 ?  77  VAL   B HG12 1 
ATOM   5156 H  HG13 . VAL   B 1 77  ? 37.978 -21.866 8.846   1.00 21.01 ?  77  VAL   B HG13 1 
ATOM   5157 H  HG21 . VAL   B 1 77  ? 38.703 -21.591 11.814  1.00 22.14 ?  77  VAL   B HG21 1 
ATOM   5158 H  HG22 . VAL   B 1 77  ? 39.619 -20.903 10.712  1.00 22.14 ?  77  VAL   B HG22 1 
ATOM   5159 H  HG23 . VAL   B 1 77  ? 38.956 -20.023 11.857  1.00 22.14 ?  77  VAL   B HG23 1 
ATOM   5160 N  N    . GLY   B 1 78  ? 36.800 -19.395 7.280   1.00 13.47 ?  78  GLY   B N    1 
ATOM   5161 C  CA   . GLY   B 1 78  ? 35.823 -19.077 6.266   1.00 13.27 ?  78  GLY   B CA   1 
ATOM   5162 C  C    . GLY   B 1 78  ? 36.061 -17.760 5.562   1.00 12.55 ?  78  GLY   B C    1 
ATOM   5163 O  O    . GLY   B 1 78  ? 35.374 -17.476 4.574   1.00 13.10 ?  78  GLY   B O    1 
ATOM   5164 H  H    . GLY   B 1 78  ? 37.504 -19.778 6.962   1.00 16.21 ?  78  GLY   B H    1 
ATOM   5165 H  HA2  . GLY   B 1 78  ? 35.819 -19.771 5.594   1.00 15.97 ?  78  GLY   B HA2  1 
ATOM   5166 H  HA3  . GLY   B 1 78  ? 34.943 -19.040 6.672   1.00 15.97 ?  78  GLY   B HA3  1 
ATOM   5167 N  N    . GLY   B 1 79  ? 37.010 -16.951 6.043   1.00 12.69 ?  79  GLY   B N    1 
ATOM   5168 C  CA   . GLY   B 1 79  ? 37.302 -15.655 5.466   1.00 12.27 ?  79  GLY   B CA   1 
ATOM   5169 C  C    . GLY   B 1 79  ? 38.539 -15.672 4.577   1.00 11.93 ?  79  GLY   B C    1 
ATOM   5170 O  O    . GLY   B 1 79  ? 39.158 -16.705 4.330   1.00 12.46 ?  79  GLY   B O    1 
ATOM   5171 H  H    . GLY   B 1 79  ? 37.515 -17.144 6.708   1.00 15.28 ?  79  GLY   B H    1 
ATOM   5172 H  HA2  . GLY   B 1 79  ? 36.547 -15.356 4.931   1.00 14.77 ?  79  GLY   B HA2  1 
ATOM   5173 H  HA3  . GLY   B 1 79  ? 37.445 -15.008 6.175   1.00 14.77 ?  79  GLY   B HA3  1 
ATOM   5174 N  N    . SER   B 1 80  ? 38.901 -14.478 4.101   1.00 11.86 ?  80  SER   B N    1 
ATOM   5175 C  CA   . SER   B 1 80  ? 40.012 -14.350 3.168   1.00 11.45 ?  80  SER   B CA   1 
ATOM   5176 C  C    . SER   B 1 80  ? 40.594 -12.943 3.227   1.00 11.43 ?  80  SER   B C    1 
ATOM   5177 O  O    . SER   B 1 80  ? 39.974 -12.008 3.739   1.00 12.94 ?  80  SER   B O    1 
ATOM   5178 C  CB   . SER   B 1 80  ? 39.575 -14.643 1.730   1.00 11.98 ?  80  SER   B CB   1 
ATOM   5179 O  OG   . SER   B 1 80  ? 38.734 -13.624 1.223   1.00 13.07 ?  80  SER   B OG   1 
ATOM   5180 H  H    . SER   B 1 80  ? 38.529 -13.731 4.308   1.00 14.27 ?  80  SER   B H    1 
ATOM   5181 H  HA   . SER   B 1 80  ? 40.705 -14.980 3.418   1.00 13.78 ?  80  SER   B HA   1 
ATOM   5182 H  HB2  . SER   B 1 80  ? 40.359 -14.704 1.166   1.00 14.43 ?  80  SER   B HB2  1 
ATOM   5183 H  HB3  . SER   B 1 80  ? 39.088 -15.482 1.714   1.00 14.43 ?  80  SER   B HB3  1 
ATOM   5184 H  HG   . SER   B 1 80  ? 38.043 -13.555 1.703   1.00 15.74 ?  80  SER   B HG   1 
ATOM   5185 N  N    . CYS   B 1 81  ? 41.785 -12.802 2.648   1.00 11.51 ?  81  CYS   B N    1 
ATOM   5186 C  CA   . CYS   B 1 81  ? 42.330 -11.490 2.331   1.00 11.47 ?  81  CYS   B CA   1 
ATOM   5187 C  C    . CYS   B 1 81  ? 43.097 -11.575 1.022   1.00 10.68 ?  81  CYS   B C    1 
ATOM   5188 O  O    . CYS   B 1 81  ? 43.600 -12.638 0.644   1.00 11.91 ?  81  CYS   B O    1 
ATOM   5189 C  CB   . CYS   B 1 81  ? 43.223 -10.933 3.449   1.00 12.19 ?  81  CYS   B CB   1 
ATOM   5190 S  SG   . CYS   B 1 81  ? 44.743 -11.870 3.694   1.00 12.71 ?  81  CYS   B SG   1 
ATOM   5191 H  H    . CYS   B 1 81  ? 42.299 -13.457 2.419   1.00 13.86 ?  81  CYS   B H    1 
ATOM   5192 H  HA   . CYS   B 1 81  ? 41.596 -10.868 2.205   1.00 13.81 ?  81  CYS   B HA   1 
ATOM   5193 H  HB2  . CYS   B 1 81  ? 43.470 -10.020 3.232   1.00 14.67 ?  81  CYS   B HB2  1 
ATOM   5194 H  HB3  . CYS   B 1 81  ? 42.724 -10.944 4.285   1.00 14.67 ?  81  CYS   B HB3  1 
ATOM   5195 H  HG   . CYS   B 1 81  ? 45.373 -11.372 4.588   1.00 15.29 ?  81  CYS   B HG   1 
ATOM   5196 N  N    . VAL   B 1 82  ? 43.199 -10.431 0.348   1.00 11.23 ?  82  VAL   B N    1 
ATOM   5197 C  CA   . VAL   B 1 82  ? 43.965 -10.298 -0.889  1.00 11.41 ?  82  VAL   B CA   1 
ATOM   5198 C  C    . VAL   B 1 82  ? 45.305 -9.657  -0.571  1.00 11.72 ?  82  VAL   B C    1 
ATOM   5199 O  O    . VAL   B 1 82  ? 45.358 -8.543  -0.035  1.00 12.78 ?  82  VAL   B O    1 
ATOM   5200 C  CB   . VAL   B 1 82  ? 43.215 -9.457  -1.935  1.00 12.71 ?  82  VAL   B CB   1 
ATOM   5201 C  CG1  . VAL   B 1 82  ? 44.063 -9.307  -3.193  1.00 13.87 ?  82  VAL   B CG1  1 
ATOM   5202 C  CG2  . VAL   B 1 82  ? 41.861 -10.060 -2.254  1.00 13.33 ?  82  VAL   B CG2  1 
ATOM   5203 H  H    . VAL   B 1 82  ? 42.815 -9.694  0.589   1.00 13.53 ?  82  VAL   B H    1 
ATOM   5204 H  HA   . VAL   B 1 82  ? 44.125 -11.175 -1.263  1.00 13.74 ?  82  VAL   B HA   1 
ATOM   5205 H  HB   . VAL   B 1 82  ? 43.064 -8.570  -1.578  1.00 15.30 ?  82  VAL   B HB   1 
ATOM   5206 H  HG11 . VAL   B 1 82  ? 43.502 -8.991  -3.921  1.00 16.69 ?  82  VAL   B HG11 1 
ATOM   5207 H  HG12 . VAL   B 1 82  ? 44.772 -8.661  -3.027  1.00 16.69 ?  82  VAL   B HG12 1 
ATOM   5208 H  HG13 . VAL   B 1 82  ? 44.448 -10.166 -3.424  1.00 16.69 ?  82  VAL   B HG13 1 
ATOM   5209 H  HG21 . VAL   B 1 82  ? 41.428 -9.530  -2.945  1.00 16.04 ?  82  VAL   B HG21 1 
ATOM   5210 H  HG22 . VAL   B 1 82  ? 41.982 -10.971 -2.569  1.00 16.04 ?  82  VAL   B HG22 1 
ATOM   5211 H  HG23 . VAL   B 1 82  ? 41.315 -10.059 -1.452  1.00 16.04 ?  82  VAL   B HG23 1 
ATOM   5212 N  N    . LEU   B 1 83  ? 46.383 -10.342 -0.940  1.00 11.22 ?  83  LEU   B N    1 
ATOM   5213 C  CA   . LEU   B 1 83  ? 47.741 -9.829  -0.824  1.00 11.21 ?  83  LEU   B CA   1 
ATOM   5214 C  C    . LEU   B 1 83  ? 48.437 -9.979  -2.176  1.00 11.08 ?  83  LEU   B C    1 
ATOM   5215 O  O    . LEU   B 1 83  ? 47.833 -10.394 -3.169  1.00 11.26 ?  83  LEU   B O    1 
ATOM   5216 C  CB   . LEU   B 1 83  ? 48.495 -10.508 0.328   1.00 12.00 ?  83  LEU   B CB   1 
ATOM   5217 C  CG   . LEU   B 1 83  ? 47.991 -10.152 1.732   1.00 13.12 ?  83  LEU   B CG   1 
ATOM   5218 C  CD1  . LEU   B 1 83  ? 48.615 -11.015 2.809   1.00 13.89 ?  83  LEU   B CD1  1 
ATOM   5219 C  CD2  . LEU   B 1 83  ? 48.200 -8.662  2.047   1.00 13.99 ?  83  LEU   B CD2  1 
ATOM   5220 H  H    . LEU   B 1 83  ? 46.345 -11.138 -1.275  1.00 13.51 ?  83  LEU   B H    1 
ATOM   5221 H  HA   . LEU   B 1 83  ? 47.689 -8.883  -0.629  1.00 13.50 ?  83  LEU   B HA   1 
ATOM   5222 H  HB2  . LEU   B 1 83  ? 48.421 -11.468 0.222   1.00 14.45 ?  83  LEU   B HB2  1 
ATOM   5223 H  HB3  . LEU   B 1 83  ? 49.428 -10.246 0.274   1.00 14.45 ?  83  LEU   B HB3  1 
ATOM   5224 H  HG   . LEU   B 1 83  ? 47.038 -10.314 1.752   1.00 15.79 ?  83  LEU   B HG   1 
ATOM   5225 H  HD11 . LEU   B 1 83  ? 48.252 -10.753 3.671   1.00 16.72 ?  83  LEU   B HD11 1 
ATOM   5226 H  HD12 . LEU   B 1 83  ? 48.398 -11.946 2.632   1.00 16.72 ?  83  LEU   B HD12 1 
ATOM   5227 H  HD13 . LEU   B 1 83  ? 49.575 -10.893 2.801   1.00 16.72 ?  83  LEU   B HD13 1 
ATOM   5228 H  HD21 . LEU   B 1 83  ? 48.002 -8.510  2.984   1.00 16.84 ?  83  LEU   B HD21 1 
ATOM   5229 H  HD22 . LEU   B 1 83  ? 49.119 -8.423  1.857   1.00 16.84 ?  83  LEU   B HD22 1 
ATOM   5230 H  HD23 . LEU   B 1 83  ? 47.600 -8.135  1.493   1.00 16.84 ?  83  LEU   B HD23 1 
ATOM   5231 N  N    . SER   B 1 84  ? 49.714 -9.605  -2.229  1.00 12.21 ?  84  SER   B N    1 
ATOM   5232 C  CA   . SER   B 1 84  ? 50.451 -9.723  -3.478  1.00 12.36 ?  84  SER   B CA   1 
ATOM   5233 C  C    . SER   B 1 84  ? 50.611 -11.184 -3.886  1.00 11.57 ?  84  SER   B C    1 
ATOM   5234 O  O    . SER   B 1 84  ? 50.719 -12.077 -3.049  1.00 11.50 ?  84  SER   B O    1 
ATOM   5235 C  CB   . SER   B 1 84  ? 51.842 -9.113  -3.332  1.00 14.27 ?  84  SER   B CB   1 
ATOM   5236 O  OG   . SER   B 1 84  ? 52.582 -9.326  -4.518  1.00 15.92 ?  84  SER   B OG   1 
ATOM   5237 H  H    . SER   B 1 84  ? 50.157 -9.276  -1.569  1.00 14.70 ?  84  SER   B H    1 
ATOM   5238 H  HA   . SER   B 1 84  ? 49.977 -9.257  -4.181  1.00 14.88 ?  84  SER   B HA   1 
ATOM   5239 H  HB2  . SER   B 1 84  ? 51.752 -8.154  -3.171  1.00 17.17 ?  84  SER   B HB2  1 
ATOM   5240 H  HB3  . SER   B 1 84  ? 52.301 -9.529  -2.587  1.00 17.17 ?  84  SER   B HB3  1 
ATOM   5241 H  HG   . SER   B 1 84  ? 53.348 -8.978  -4.442  1.00 19.15 ?  84  SER   B HG   1 
ATOM   5242 N  N    . GLY   B 1 85  ? 50.668 -11.413 -5.191  1.00 12.74 ?  85  GLY   B N    1 
ATOM   5243 C  CA   . GLY   B 1 85  ? 51.014 -12.703 -5.731  1.00 13.53 ?  85  GLY   B CA   1 
ATOM   5244 C  C    . GLY   B 1 85  ? 52.485 -12.890 -6.040  1.00 12.59 ?  85  GLY   B C    1 
ATOM   5245 O  O    . GLY   B 1 85  ? 52.863 -13.969 -6.497  1.00 13.08 ?  85  GLY   B O    1 
ATOM   5246 H  H    . GLY   B 1 85  ? 50.516 -10.821 -5.787  1.00 15.34 ?  85  GLY   B H    1 
ATOM   5247 H  HA2  . GLY   B 1 85  ? 50.754 -13.394 -5.098  1.00 16.29 ?  85  GLY   B HA2  1 
ATOM   5248 H  HA3  . GLY   B 1 85  ? 50.521 -12.847 -6.549  1.00 16.29 ?  85  GLY   B HA3  1 
ATOM   5249 N  N    . HIS   B 1 86  ? 53.337 -11.889 -5.821  1.00 12.75 ?  86  HIS   B N    1 
ATOM   5250 C  CA   . HIS   B 1 86  ? 54.801 -12.058 -5.904  1.00 12.69 ?  86  HIS   B CA   1 
ATOM   5251 C  C    . HIS   B 1 86  ? 55.171 -12.573 -7.294  1.00 12.55 ?  86  HIS   B C    1 
ATOM   5252 O  O    . HIS   B 1 86  ? 54.782 -11.960 -8.301  1.00 13.67 ?  86  HIS   B O    1 
ATOM   5253 C  CB   . HIS   B 1 86  ? 55.292 -12.899 -4.727  1.00 12.99 ?  86  HIS   B CB   1 
ATOM   5254 C  CG   . HIS   B 1 86  ? 54.981 -12.293 -3.401  1.00 13.29 ?  86  HIS   B CG   1 
ATOM   5255 N  ND1  . HIS   B 1 86  ? 55.809 -11.381 -2.784  1.00 14.70 ?  86  HIS   B ND1  1 
ATOM   5256 C  CD2  . HIS   B 1 86  ? 53.905 -12.437 -2.591  1.00 13.47 ?  86  HIS   B CD2  1 
ATOM   5257 C  CE1  . HIS   B 1 86  ? 55.255 -10.991 -1.650  1.00 14.57 ?  86  HIS   B CE1  1 
ATOM   5258 N  NE2  . HIS   B 1 86  ? 54.096 -11.610 -1.513  1.00 13.85 ?  86  HIS   B NE2  1 
ATOM   5259 H  H    . HIS   B 1 86  ? 53.094 -11.090 -5.615  1.00 15.35 ?  86  HIS   B H    1 
ATOM   5260 H  HA   . HIS   B 1 86  ? 55.207 -11.187 -5.812  1.00 15.27 ?  86  HIS   B HA   1 
ATOM   5261 H  HB2  . HIS   B 1 86  ? 54.877 -13.773 -4.763  1.00 15.64 ?  86  HIS   B HB2  1 
ATOM   5262 H  HB3  . HIS   B 1 86  ? 56.259 -12.991 -4.789  1.00 15.64 ?  86  HIS   B HB3  1 
ATOM   5263 H  HD2  . HIS   B 1 86  ? 53.162 -12.979 -2.748  1.00 16.21 ?  86  HIS   B HD2  1 
ATOM   5264 H  HE1  . HIS   B 1 86  ? 55.624 -10.392 -1.044  1.00 17.54 ?  86  HIS   B HE1  1 
ATOM   5265 H  HE2  . HIS   B 1 86  ? 53.559 -11.531 -0.844  1.00 16.67 ?  86  HIS   B HE2  1 
ATOM   5266 N  N    . ASN   B 1 87  ? 55.941 -13.656 -7.403  1.00 12.99 ?  87  ASN   B N    1 
ATOM   5267 C  CA   . ASN   B 1 87  ? 56.336 -14.234 -8.678  1.00 14.02 ?  87  ASN   B CA   1 
ATOM   5268 C  C    . ASN   B 1 87  ? 55.347 -15.274 -9.179  1.00 13.67 ?  87  ASN   B C    1 
ATOM   5269 O  O    . ASN   B 1 87  ? 55.654 -15.983 -10.144 1.00 15.45 ?  87  ASN   B O    1 
ATOM   5270 C  CB   . ASN   B 1 87  ? 57.726 -14.872 -8.564  1.00 15.99 ?  87  ASN   B CB   1 
ATOM   5271 C  CG   . ASN   B 1 87  ? 57.778 -15.987 -7.525  1.00 16.70 ?  87  ASN   B CG   1 
ATOM   5272 O  OD1  . ASN   B 1 87  ? 57.139 -15.904 -6.472  1.00 15.89 ?  87  ASN   B OD1  1 
ATOM   5273 N  ND2  . ASN   B 1 87  ? 58.516 -17.057 -7.837  1.00 18.97 ?  87  ASN   B ND2  1 
ATOM   5274 H  H    . ASN   B 1 87  ? 56.243 -14.093 -6.727  1.00 15.64 ?  87  ASN   B H    1 
ATOM   5275 H  HA   . ASN   B 1 87  ? 56.380 -13.530 -9.337  1.00 16.87 ?  87  ASN   B HA   1 
ATOM   5276 H  HB2  . ASN   B 1 87  ? 57.970 -15.248 -9.425  1.00 19.24 ?  87  ASN   B HB2  1 
ATOM   5277 H  HB3  . ASN   B 1 87  ? 58.361 -14.190 -8.305  1.00 19.24 ?  87  ASN   B HB3  1 
ATOM   5278 H  HD21 . ASN   B 1 87  ? 58.580 -17.710 -7.285  1.00 22.82 ?  87  ASN   B HD21 1 
ATOM   5279 H  HD22 . ASN   B 1 87  ? 58.942 -17.082 -8.586  1.00 22.82 ?  87  ASN   B HD22 1 
ATOM   5280 N  N    . LEU   B 1 88  ? 54.170 -15.373 -8.555  1.00 12.52 ?  88  LEU   B N    1 
ATOM   5281 C  CA   . LEU   B 1 88  ? 53.186 -16.400 -8.879  1.00 12.79 ?  88  LEU   B CA   1 
ATOM   5282 C  C    . LEU   B 1 88  ? 51.956 -15.880 -9.603  1.00 12.80 ?  88  LEU   B C    1 
ATOM   5283 O  O    . LEU   B 1 88  ? 51.353 -16.629 -10.384 1.00 14.56 ?  88  LEU   B O    1 
ATOM   5284 C  CB   . LEU   B 1 88  ? 52.713 -17.082 -7.594  1.00 13.66 ?  88  LEU   B CB   1 
ATOM   5285 C  CG   . LEU   B 1 88  ? 53.829 -17.752 -6.810  1.00 15.97 ?  88  LEU   B CG   1 
ATOM   5286 C  CD1  . LEU   B 1 88  ? 53.337 -18.105 -5.420  1.00 17.60 ?  88  LEU   B CD1  1 
ATOM   5287 C  CD2  . LEU   B 1 88  ? 54.294 -18.986 -7.553  1.00 19.05 ?  88  LEU   B CD2  1 
ATOM   5288 H  H    . LEU   B 1 88  ? 53.910 -14.843 -7.920  1.00 15.08 ?  88  LEU   B H    1 
ATOM   5289 H  HA   . LEU   B 1 88  ? 53.595 -17.064 -9.442  1.00 15.39 ?  88  LEU   B HA   1 
ATOM   5290 H  HB2  . LEU   B 1 88  ? 52.300 -16.422 -7.016  1.00 16.43 ?  88  LEU   B HB2  1 
ATOM   5291 H  HB3  . LEU   B 1 88  ? 52.063 -17.766 -7.825  1.00 16.43 ?  88  LEU   B HB3  1 
ATOM   5292 H  HG   . LEU   B 1 88  ? 54.577 -17.141 -6.725  1.00 19.21 ?  88  LEU   B HG   1 
ATOM   5293 H  HD11 . LEU   B 1 88  ? 53.974 -18.704 -5.002  1.00 21.16 ?  88  LEU   B HD11 1 
ATOM   5294 H  HD12 . LEU   B 1 88  ? 53.253 -17.292 -4.898  1.00 21.16 ?  88  LEU   B HD12 1 
ATOM   5295 H  HD13 . LEU   B 1 88  ? 52.473 -18.540 -5.495  1.00 21.16 ?  88  LEU   B HD13 1 
ATOM   5296 H  HD21 . LEU   B 1 88  ? 54.936 -19.460 -7.004  1.00 22.91 ?  88  LEU   B HD21 1 
ATOM   5297 H  HD22 . LEU   B 1 88  ? 53.529 -19.552 -7.734  1.00 22.91 ?  88  LEU   B HD22 1 
ATOM   5298 H  HD23 . LEU   B 1 88  ? 54.709 -18.714 -8.388  1.00 22.91 ?  88  LEU   B HD23 1 
ATOM   5299 N  N    . ALA   B 1 89  ? 51.554 -14.642 -9.340  1.00 12.03 ?  89  ALA   B N    1 
ATOM   5300 C  CA   . ALA   B 1 89  ? 50.260 -14.145 -9.783  1.00 11.48 ?  89  ALA   B CA   1 
ATOM   5301 C  C    . ALA   B 1 89  ? 50.234 -12.653 -9.501  1.00 11.97 ?  89  ALA   B C    1 
ATOM   5302 O  O    . ALA   B 1 89  ? 51.069 -12.138 -8.755  1.00 12.94 ?  89  ALA   B O    1 
ATOM   5303 C  CB   . ALA   B 1 89  ? 49.124 -14.823 -9.022  1.00 11.61 ?  89  ALA   B CB   1 
ATOM   5304 H  H    . ALA   B 1 89  ? 52.006 -14.059 -8.891  1.00 14.48 ?  89  ALA   B H    1 
ATOM   5305 H  HA   . ALA   B 1 89  ? 50.144 -14.291 -10.738 1.00 13.83 ?  89  ALA   B HA   1 
ATOM   5306 H  HB1  . ALA   B 1 89  ? 48.273 -14.487 -9.356  1.00 13.98 ?  89  ALA   B HB1  1 
ATOM   5307 H  HB2  . ALA   B 1 89  ? 49.176 -15.781 -9.172  1.00 13.98 ?  89  ALA   B HB2  1 
ATOM   5308 H  HB3  . ALA   B 1 89  ? 49.212 -14.627 -8.082  1.00 13.98 ?  89  ALA   B HB3  1 
ATOM   5309 N  N    . LYS   B 1 90  ? 49.245 -11.960 -10.065 1.00 12.92 ?  90  LYS   B N    1 
ATOM   5310 C  CA   . LYS   B 1 90  ? 49.053 -10.574 -9.657  1.00 13.00 ?  90  LYS   B CA   1 
ATOM   5311 C  C    . LYS   B 1 90  ? 48.741 -10.504 -8.168  1.00 12.53 ?  90  LYS   B C    1 
ATOM   5312 O  O    . LYS   B 1 90  ? 49.384 -9.755  -7.417  1.00 13.76 ?  90  LYS   B O    1 
ATOM   5313 C  CB   . LYS   B 1 90  ? 47.967 -9.910  -10.505 1.00 14.63 ?  90  LYS   B CB   1 
ATOM   5314 C  CG   . LYS   B 1 90  ? 47.676 -8.465  -10.115 1.00 15.16 ?  90  LYS   B CG   1 
ATOM   5315 C  CD   . LYS   B 1 90  ? 48.886 -7.577  -10.192 1.00 17.91 ?  90  LYS   B CD   1 
ATOM   5316 C  CE   . LYS   B 1 90  ? 48.447 -6.159  -9.931  1.00 19.69 ?  90  LYS   B CE   1 
ATOM   5317 N  NZ   . LYS   B 1 90  ? 49.590 -5.223  -9.842  1.00 19.27 ?  90  LYS   B NZ   1 
ATOM   5318 H  H    . LYS   B 1 90  ? 48.693 -12.258 -10.657 1.00 15.55 ?  90  LYS   B H    1 
ATOM   5319 H  HA   . LYS   B 1 90  ? 49.877 -10.095 -9.809  1.00 15.65 ?  90  LYS   B HA   1 
ATOM   5320 H  HB2  . LYS   B 1 90  ? 48.252 -9.913  -11.435 1.00 17.61 ?  90  LYS   B HB2  1 
ATOM   5321 H  HB3  . LYS   B 1 90  ? 47.143 -10.416 -10.418 1.00 17.61 ?  90  LYS   B HB3  1 
ATOM   5322 H  HG2  . LYS   B 1 90  ? 47.002 -8.109  -10.715 1.00 18.23 ?  90  LYS   B HG2  1 
ATOM   5323 H  HG3  . LYS   B 1 90  ? 47.341 -8.446  -9.202  1.00 18.23 ?  90  LYS   B HG3  1 
ATOM   5324 H  HD2  . LYS   B 1 90  ? 49.529 -7.835  -9.512  1.00 21.54 ?  90  LYS   B HD2  1 
ATOM   5325 H  HD3  . LYS   B 1 90  ? 49.278 -7.630  -11.077 1.00 21.54 ?  90  LYS   B HD3  1 
ATOM   5326 H  HE2  . LYS   B 1 90  ? 47.876 -5.860  -10.658 1.00 23.68 ?  90  LYS   B HE2  1 
ATOM   5327 H  HE3  . LYS   B 1 90  ? 47.965 -6.117  -9.092  1.00 23.68 ?  90  LYS   B HE3  1 
ATOM   5328 H  HZ1  . LYS   B 1 90  ? 49.301 -4.392  -9.692  1.00 23.17 ?  90  LYS   B HZ1  1 
ATOM   5329 H  HZ2  . LYS   B 1 90  ? 50.134 -5.462  -9.179  1.00 23.17 ?  90  LYS   B HZ2  1 
ATOM   5330 H  HZ3  . LYS   B 1 90  ? 50.052 -5.228  -10.607 1.00 23.17 ?  90  LYS   B HZ3  1 
ATOM   5331 N  N    . HIS   B 1 91  ? 47.782 -11.319 -7.721  1.00 11.16 ?  91  HIS   B N    1 
ATOM   5332 C  CA   . HIS   B 1 91  ? 47.319 -11.341 -6.347  1.00 11.36 ?  91  HIS   B CA   1 
ATOM   5333 C  C    . HIS   B 1 91  ? 47.318 -12.767 -5.829  1.00 10.62 ?  91  HIS   B C    1 
ATOM   5334 O  O    . HIS   B 1 91  ? 47.091 -13.720 -6.584  1.00 11.14 ?  91  HIS   B O    1 
ATOM   5335 C  CB   . HIS   B 1 91  ? 45.867 -10.857 -6.230  1.00 12.93 ?  91  HIS   B CB   1 
ATOM   5336 C  CG   . HIS   B 1 91  ? 45.662 -9.444  -6.648  1.00 16.20 ?  91  HIS   B CG   1 
ATOM   5337 N  ND1  . HIS   B 1 91  ? 46.290 -8.383  -6.031  1.00 18.73 ?  91  HIS   B ND1  1 
ATOM   5338 C  CD2  . HIS   B 1 91  ? 44.865 -8.910  -7.598  1.00 18.68 ?  91  HIS   B CD2  1 
ATOM   5339 C  CE1  . HIS   B 1 91  ? 45.908 -7.254  -6.602  1.00 19.72 ?  91  HIS   B CE1  1 
ATOM   5340 N  NE2  . HIS   B 1 91  ? 45.036 -7.546  -7.552  1.00 19.94 ?  91  HIS   B NE2  1 
ATOM   5341 H  H    . HIS   B 1 91  ? 47.367 -11.881 -8.220  1.00 13.44 ?  91  HIS   B H    1 
ATOM   5342 H  HA   . HIS   B 1 91  ? 47.890 -10.787 -5.785  1.00 13.68 ?  91  HIS   B HA   1 
ATOM   5343 H  HB2  . HIS   B 1 91  ? 45.305 -11.412 -6.791  1.00 15.57 ?  91  HIS   B HB2  1 
ATOM   5344 H  HB3  . HIS   B 1 91  ? 45.582 -10.933 -5.304  1.00 15.57 ?  91  HIS   B HB3  1 
ATOM   5345 H  HD1  . HIS   B 1 91  ? 46.852 -8.446  -5.383  1.00 22.52 ?  91  HIS   B HD1  1 
ATOM   5346 H  HD2  . HIS   B 1 91  ? 44.310 -9.364  -8.183  1.00 22.46 ?  91  HIS   B HD2  1 
ATOM   5347 H  HE1  . HIS   B 1 91  ? 46.199 -6.398  -6.364  1.00 23.71 ?  91  HIS   B HE1  1 
ATOM   5348 N  N    . CYS   B 1 92  ? 47.514 -12.901 -4.524  1.00 10.59 ?  92  CYS   B N    1 
ATOM   5349 C  CA   . CYS   B 1 92  ? 47.209 -14.137 -3.816  1.00 10.53 ?  92  CYS   B CA   1 
ATOM   5350 C  C    . CYS   B 1 92  ? 45.988 -13.905 -2.934  1.00 10.09 ?  92  CYS   B C    1 
ATOM   5351 O  O    . CYS   B 1 92  ? 45.988 -13.004 -2.083  1.00 11.04 ?  92  CYS   B O    1 
ATOM   5352 C  CB   . CYS   B 1 92  ? 48.387 -14.597 -2.961  1.00 10.99 ?  92  CYS   B CB   1 
ATOM   5353 S  SG   . CYS   B 1 92  ? 48.027 -16.131 -2.067  1.00 11.03 ?  92  CYS   B SG   1 
ATOM   5354 H  H    . CYS   B 1 92  ? 47.846 -12.282 -4.016  1.00 12.76 ?  92  CYS   B H    1 
ATOM   5355 H  HA   . CYS   B 1 92  ? 47.011 -14.833 -4.460  1.00 12.68 ?  92  CYS   B HA   1 
ATOM   5356 H  HB2  . CYS   B 1 92  ? 49.154 -14.744 -3.528  1.00 13.23 ?  92  CYS   B HB2  1 
ATOM   5357 H  HB3  . CYS   B 1 92  ? 48.583 -13.906 -2.304  1.00 13.23 ?  92  CYS   B HB3  1 
ATOM   5358 H  HG   . CYS   B 1 92  ? 49.002 -16.442 -1.437  1.00 13.28 ?  92  CYS   B HG   1 
ATOM   5359 N  N    . LEU   B 1 93  ? 44.952 -14.713 -3.147  1.00 10.20 ?  93  LEU   B N    1 
ATOM   5360 C  CA   . LEU   B 1 93  ? 43.776 -14.723 -2.286  1.00 10.35 ?  93  LEU   B CA   1 
ATOM   5361 C  C    . LEU   B 1 93  ? 44.002 -15.787 -1.218  1.00 9.79  ?  93  LEU   B C    1 
ATOM   5362 O  O    . LEU   B 1 93  ? 43.955 -16.988 -1.507  1.00 10.47 ?  93  LEU   B O    1 
ATOM   5363 C  CB   . LEU   B 1 93  ? 42.513 -15.009 -3.094  1.00 10.84 ?  93  LEU   B CB   1 
ATOM   5364 C  CG   . LEU   B 1 93  ? 41.216 -15.024 -2.281  1.00 11.47 ?  93  LEU   B CG   1 
ATOM   5365 C  CD1  . LEU   B 1 93  ? 40.863 -13.644 -1.783  1.00 11.89 ?  93  LEU   B CD1  1 
ATOM   5366 C  CD2  . LEU   B 1 93  ? 40.082 -15.619 -3.105  1.00 11.86 ?  93  LEU   B CD2  1 
ATOM   5367 H  H    . LEU   B 1 93  ? 44.912 -15.288 -3.799  1.00 12.29 ?  93  LEU   B H    1 
ATOM   5368 H  HA   . LEU   B 1 93  ? 43.685 -13.862 -1.860  1.00 12.46 ?  93  LEU   B HA   1 
ATOM   5369 H  HB2  . LEU   B 1 93  ? 42.421 -14.320 -3.774  1.00 13.05 ?  93  LEU   B HB2  1 
ATOM   5370 H  HB3  . LEU   B 1 93  ? 42.603 -15.873 -3.520  1.00 13.05 ?  93  LEU   B HB3  1 
ATOM   5371 H  HG   . LEU   B 1 93  ? 41.340 -15.592 -1.507  1.00 13.82 ?  93  LEU   B HG   1 
ATOM   5372 H  HD11 . LEU   B 1 93  ? 40.011 -13.681 -1.325  1.00 14.32 ?  93  LEU   B HD11 1 
ATOM   5373 H  HD12 . LEU   B 1 93  ? 41.555 -13.341 -1.175  1.00 14.32 ?  93  LEU   B HD12 1 
ATOM   5374 H  HD13 . LEU   B 1 93  ? 40.804 -13.041 -2.543  1.00 14.32 ?  93  LEU   B HD13 1 
ATOM   5375 H  HD21 . LEU   B 1 93  ? 39.269 -15.613 -2.573  1.00 14.28 ?  93  LEU   B HD21 1 
ATOM   5376 H  HD22 . LEU   B 1 93  ? 39.956 -15.084 -3.904  1.00 14.28 ?  93  LEU   B HD22 1 
ATOM   5377 H  HD23 . LEU   B 1 93  ? 40.310 -16.529 -3.348  1.00 14.28 ?  93  LEU   B HD23 1 
ATOM   5378 N  N    . HIS   B 1 94  ? 44.277 -15.349 0.007   1.00 9.85  ?  94  HIS   B N    1 
ATOM   5379 C  CA   . HIS   B 1 94  ? 44.495 -16.257 1.127   1.00 10.01 ?  94  HIS   B CA   1 
ATOM   5380 C  C    . HIS   B 1 94  ? 43.138 -16.610 1.709   1.00 10.58 ?  94  HIS   B C    1 
ATOM   5381 O  O    . HIS   B 1 94  ? 42.473 -15.735 2.263   1.00 11.87 ?  94  HIS   B O    1 
ATOM   5382 C  CB   . HIS   B 1 94  ? 45.366 -15.579 2.182   1.00 10.52 ?  94  HIS   B CB   1 
ATOM   5383 C  CG   . HIS   B 1 94  ? 46.748 -15.277 1.709   1.00 10.59 ?  94  HIS   B CG   1 
ATOM   5384 N  ND1  . HIS   B 1 94  ? 47.777 -16.191 1.795   1.00 10.89 ?  94  HIS   B ND1  1 
ATOM   5385 C  CD2  . HIS   B 1 94  ? 47.256 -14.169 1.116   1.00 10.72 ?  94  HIS   B CD2  1 
ATOM   5386 C  CE1  . HIS   B 1 94  ? 48.865 -15.639 1.287   1.00 11.06 ?  94  HIS   B CE1  1 
ATOM   5387 N  NE2  . HIS   B 1 94  ? 48.578 -14.417 0.867   1.00 11.06 ?  94  HIS   B NE2  1 
ATOM   5388 H  H    . HIS   B 1 94  ? 44.348 -14.514 0.214   1.00 11.86 ?  94  HIS   B H    1 
ATOM   5389 H  HA   . HIS   B 1 94  ? 44.933 -17.065 0.817   1.00 12.06 ?  94  HIS   B HA   1 
ATOM   5390 H  HB2  . HIS   B 1 94  ? 44.949 -14.743 2.437   1.00 12.67 ?  94  HIS   B HB2  1 
ATOM   5391 H  HB3  . HIS   B 1 94  ? 45.436 -16.165 2.947   1.00 12.67 ?  94  HIS   B HB3  1 
ATOM   5392 H  HD2  . HIS   B 1 94  ? 46.798 -13.386 0.918   1.00 12.91 ?  94  HIS   B HD2  1 
ATOM   5393 H  HE1  . HIS   B 1 94  ? 49.697 -16.054 1.232   1.00 13.32 ?  94  HIS   B HE1  1 
ATOM   5394 H  HE2  . HIS   B 1 94  ? 49.135 -13.875 0.501   1.00 13.31 ?  94  HIS   B HE2  1 
ATOM   5395 N  N    . VAL   B 1 95  ? 42.709 -17.865 1.561   1.00 10.53 ?  95  VAL   B N    1 
ATOM   5396 C  CA   . VAL   B 1 95  ? 41.382 -18.305 1.990   1.00 10.47 ?  95  VAL   B CA   1 
ATOM   5397 C  C    . VAL   B 1 95  ? 41.548 -19.343 3.083   1.00 10.77 ?  95  VAL   B C    1 
ATOM   5398 O  O    . VAL   B 1 95  ? 42.320 -20.293 2.922   1.00 11.43 ?  95  VAL   B O    1 
ATOM   5399 C  CB   . VAL   B 1 95  ? 40.564 -18.907 0.830   1.00 10.82 ?  95  VAL   B CB   1 
ATOM   5400 C  CG1  . VAL   B 1 95  ? 39.185 -19.350 1.313   1.00 12.03 ?  95  VAL   B CG1  1 
ATOM   5401 C  CG2  . VAL   B 1 95  ? 40.448 -17.923 -0.311  1.00 10.94 ?  95  VAL   B CG2  1 
ATOM   5402 H  H    . VAL   B 1 95  ? 43.176 -18.492 1.200   1.00 12.68 ?  95  VAL   B H    1 
ATOM   5403 H  HA   . VAL   B 1 95  ? 40.889 -17.553 2.353   1.00 12.61 ?  95  VAL   B HA   1 
ATOM   5404 H  HB   . VAL   B 1 95  ? 41.023 -19.690 0.496   1.00 13.03 ?  95  VAL   B HB   1 
ATOM   5405 H  HG11 . VAL   B 1 95  ? 38.623 -19.543 0.541   1.00 14.48 ?  95  VAL   B HG11 1 
ATOM   5406 H  HG12 . VAL   B 1 95  ? 39.274 -20.150 1.856   1.00 14.48 ?  95  VAL   B HG12 1 
ATOM   5407 H  HG13 . VAL   B 1 95  ? 38.782 -18.639 1.837   1.00 14.48 ?  95  VAL   B HG13 1 
ATOM   5408 H  HG21 . VAL   B 1 95  ? 39.872 -18.302 -0.992  1.00 13.18 ?  95  VAL   B HG21 1 
ATOM   5409 H  HG22 . VAL   B 1 95  ? 40.064 -17.098 0.027   1.00 13.18 ?  95  VAL   B HG22 1 
ATOM   5410 H  HG23 . VAL   B 1 95  ? 41.330 -17.759 -0.670  1.00 13.18 ?  95  VAL   B HG23 1 
ATOM   5411 N  N    . VAL   B 1 96  ? 40.823 -19.171 4.181   1.00 11.23 ?  96  VAL   B N    1 
ATOM   5412 C  CA   . VAL   B 1 96  ? 40.905 -20.085 5.321   1.00 11.50 ?  96  VAL   B CA   1 
ATOM   5413 C  C    . VAL   B 1 96  ? 39.716 -21.044 5.271   1.00 12.23 ?  96  VAL   B C    1 
ATOM   5414 O  O    . VAL   B 1 96  ? 38.596 -20.687 5.651   1.00 12.79 ?  96  VAL   B O    1 
ATOM   5415 C  CB   . VAL   B 1 96  ? 40.948 -19.335 6.656   1.00 12.37 ?  96  VAL   B CB   1 
ATOM   5416 C  CG1  . VAL   B 1 96  ? 41.124 -20.325 7.803   1.00 13.35 ?  96  VAL   B CG1  1 
ATOM   5417 C  CG2  . VAL   B 1 96  ? 42.061 -18.296 6.670   1.00 13.24 ?  96  VAL   B CG2  1 
ATOM   5418 H  H    . VAL   B 1 96  ? 40.263 -18.529 4.299   1.00 13.53 ?  96  VAL   B H    1 
ATOM   5419 H  HA   . VAL   B 1 96  ? 41.718 -20.612 5.253   1.00 13.85 ?  96  VAL   B HA   1 
ATOM   5420 H  HB   . VAL   B 1 96  ? 40.104 -18.875 6.791   1.00 14.89 ?  96  VAL   B HB   1 
ATOM   5421 H  HG11 . VAL   B 1 96  ? 41.306 -19.832 8.623   1.00 16.06 ?  96  VAL   B HG11 1 
ATOM   5422 H  HG12 . VAL   B 1 96  ? 40.313 -20.844 7.910   1.00 16.06 ?  96  VAL   B HG12 1 
ATOM   5423 H  HG13 . VAL   B 1 96  ? 41.872 -20.911 7.606   1.00 16.06 ?  96  VAL   B HG13 1 
ATOM   5424 H  HG21 . VAL   B 1 96  ? 42.103 -17.882 7.549   1.00 15.93 ?  96  VAL   B HG21 1 
ATOM   5425 H  HG22 . VAL   B 1 96  ? 42.903 -18.727 6.467   1.00 15.93 ?  96  VAL   B HG22 1 
ATOM   5426 H  HG23 . VAL   B 1 96  ? 41.868 -17.617 6.000   1.00 15.93 ?  96  VAL   B HG23 1 
ATOM   5427 N  N    . GLY   B 1 97  ? 39.949 -22.275 4.822   1.00 12.01 ?  97  GLY   B N    1 
ATOM   5428 C  CA   . GLY   B 1 97  ? 38.978 -23.335 4.984   1.00 12.72 ?  97  GLY   B CA   1 
ATOM   5429 C  C    . GLY   B 1 97  ? 39.106 -23.944 6.363   1.00 13.83 ?  97  GLY   B C    1 
ATOM   5430 O  O    . GLY   B 1 97  ? 40.146 -23.816 7.021   1.00 14.39 ?  97  GLY   B O    1 
ATOM   5431 H  H    . GLY   B 1 97  ? 40.671 -22.517 4.417   1.00 14.46 ?  97  GLY   B H    1 
ATOM   5432 H  HA2  . GLY   B 1 97  ? 38.083 -22.970 4.869   1.00 15.31 ?  97  GLY   B HA2  1 
ATOM   5433 H  HA3  . GLY   B 1 97  ? 39.122 -24.020 4.312   1.00 15.31 ?  97  GLY   B HA3  1 
ATOM   5434 N  N    . PRO   B 1 98  ? 38.059 -24.626 6.829   1.00 14.75 ?  98  PRO   B N    1 
ATOM   5435 C  CA   . PRO   B 1 98  ? 38.153 -25.322 8.117   1.00 15.75 ?  98  PRO   B CA   1 
ATOM   5436 C  C    . PRO   B 1 98  ? 39.178 -26.444 8.071   1.00 15.38 ?  98  PRO   B C    1 
ATOM   5437 O  O    . PRO   B 1 98  ? 39.284 -27.176 7.088   1.00 15.66 ?  98  PRO   B O    1 
ATOM   5438 C  CB   . PRO   B 1 98  ? 36.733 -25.863 8.327   1.00 16.27 ?  98  PRO   B CB   1 
ATOM   5439 C  CG   . PRO   B 1 98  ? 36.160 -25.985 6.958   1.00 16.02 ?  98  PRO   B CG   1 
ATOM   5440 C  CD   . PRO   B 1 98  ? 36.741 -24.820 6.195   1.00 15.09 ?  98  PRO   B CD   1 
ATOM   5441 H  HA   . PRO   B 1 98  ? 38.378 -24.699 8.821   1.00 18.95 ?  98  PRO   B HA   1 
ATOM   5442 H  HB2  . PRO   B 1 98  ? 36.776 -26.731 8.757   1.00 19.57 ?  98  PRO   B HB2  1 
ATOM   5443 H  HB3  . PRO   B 1 98  ? 36.221 -25.237 8.857   1.00 19.57 ?  98  PRO   B HB3  1 
ATOM   5444 H  HG2  . PRO   B 1 98  ? 36.433 -26.828 6.561   1.00 19.27 ?  98  PRO   B HG2  1 
ATOM   5445 H  HG3  . PRO   B 1 98  ? 35.193 -25.922 7.000   1.00 19.27 ?  98  PRO   B HG3  1 
ATOM   5446 H  HD2  . PRO   B 1 98  ? 36.838 -25.048 5.252   1.00 18.16 ?  98  PRO   B HD2  1 
ATOM   5447 H  HD3  . PRO   B 1 98  ? 36.192 -24.029 6.310   1.00 18.16 ?  98  PRO   B HD3  1 
ATOM   5448 N  N    . ASN   B 1 99  ? 39.930 -26.575 9.157   1.00 16.63 ?  99  ASN   B N    1 
ATOM   5449 C  CA   . ASN   B 1 99  ? 40.913 -27.644 9.316   1.00 17.79 ?  99  ASN   B CA   1 
ATOM   5450 C  C    . ASN   B 1 99  ? 40.293 -28.727 10.196  1.00 20.45 ?  99  ASN   B C    1 
ATOM   5451 O  O    . ASN   B 1 99  ? 40.224 -28.583 11.419  1.00 21.17 ?  99  ASN   B O    1 
ATOM   5452 C  CB   . ASN   B 1 99  ? 42.187 -27.084 9.935   1.00 18.15 ?  99  ASN   B CB   1 
ATOM   5453 C  CG   . ASN   B 1 99  ? 43.324 -28.082 9.934   1.00 19.01 ?  99  ASN   B CG   1 
ATOM   5454 O  OD1  . ASN   B 1 99  ? 43.107 -29.275 10.087  1.00 19.70 ?  99  ASN   B OD1  1 
ATOM   5455 N  ND2  . ASN   B 1 99  ? 44.539 -27.598 9.758   1.00 18.92 ?  99  ASN   B ND2  1 
ATOM   5456 H  H    . ASN   B 1 99  ? 39.884 -26.045 9.830   1.00 20.00 ?  99  ASN   B H    1 
ATOM   5457 H  HA   . ASN   B 1 99  ? 41.121 -28.032 8.452   1.00 21.40 ?  99  ASN   B HA   1 
ATOM   5458 H  HB2  . ASN   B 1 99  ? 42.461 -26.308 9.432   1.00 21.83 ?  99  ASN   B HB2  1 
ATOM   5459 H  HB3  . ASN   B 1 99  ? 42.000 -26.840 10.857  1.00 21.83 ?  99  ASN   B HB3  1 
ATOM   5460 H  HD21 . ASN   B 1 99  ? 45.213 -28.125 9.745   1.00 22.76 ?  99  ASN   B HD21 1 
ATOM   5461 H  HD22 . ASN   B 1 99  ? 44.646 -26.751 9.655   1.00 22.76 ?  99  ASN   B HD22 1 
ATOM   5462 N  N    A VAL   B 1 100 ? 39.830 -29.811 9.568   0.72 22.44 ?  100 VAL   B N    1 
ATOM   5463 N  N    B VAL   B 1 100 ? 39.838 -29.812 9.563   0.28 22.64 ?  100 VAL   B N    1 
ATOM   5464 C  CA   A VAL   B 1 100 ? 39.218 -30.902 10.325  0.72 25.06 ?  100 VAL   B CA   1 
ATOM   5465 C  CA   B VAL   B 1 100 ? 39.226 -30.914 10.301  0.28 24.90 ?  100 VAL   B CA   1 
ATOM   5466 C  C    A VAL   B 1 100 ? 40.233 -31.569 11.245  0.72 25.57 ?  100 VAL   B C    1 
ATOM   5467 C  C    B VAL   B 1 100 ? 40.232 -31.569 11.236  0.28 25.64 ?  100 VAL   B C    1 
ATOM   5468 O  O    A VAL   B 1 100 ? 39.871 -32.085 12.309  0.72 26.37 ?  100 VAL   B O    1 
ATOM   5469 O  O    B VAL   B 1 100 ? 39.864 -32.064 12.308  0.28 26.05 ?  100 VAL   B O    1 
ATOM   5470 C  CB   A VAL   B 1 100 ? 38.547 -31.913 9.373   0.72 27.36 ?  100 VAL   B CB   1 
ATOM   5471 C  CB   B VAL   B 1 100 ? 38.597 -31.926 9.320   0.28 26.39 ?  100 VAL   B CB   1 
ATOM   5472 C  CG1  A VAL   B 1 100 ? 38.055 -33.130 10.143  0.72 28.25 ?  100 VAL   B CG1  1 
ATOM   5473 C  CG1  B VAL   B 1 100 ? 38.096 -33.158 10.061  0.28 26.92 ?  100 VAL   B CG1  1 
ATOM   5474 C  CG2  A VAL   B 1 100 ? 37.393 -31.257 8.632   0.72 27.79 ?  100 VAL   B CG2  1 
ATOM   5475 C  CG2  B VAL   B 1 100 ? 37.462 -31.272 8.548   0.28 26.82 ?  100 VAL   B CG2  1 
ATOM   5476 H  H    A VAL   B 1 100 ? 39.845 -29.932 8.716   0.72 26.98 ?  100 VAL   B H    1 
ATOM   5477 H  H    B VAL   B 1 100 ? 39.869 -29.930 8.712   0.28 27.22 ?  100 VAL   B H    1 
ATOM   5478 H  HA   A VAL   B 1 100 ? 38.517 -30.532 10.882  0.72 30.12 ?  100 VAL   B HA   1 
ATOM   5479 H  HA   B VAL   B 1 100 ? 38.508 -30.559 10.846  0.28 29.93 ?  100 VAL   B HA   1 
ATOM   5480 H  HB   A VAL   B 1 100 ? 39.196 -32.216 8.723   0.72 32.88 ?  100 VAL   B HB   1 
ATOM   5481 H  HB   B VAL   B 1 100 ? 39.269 -32.213 8.683   0.28 31.71 ?  100 VAL   B HB   1 
ATOM   5482 H  HG11 A VAL   B 1 100 ? 37.457 -33.641 9.574   0.72 33.95 ?  100 VAL   B HG11 1 
ATOM   5483 H  HG11 B VAL   B 1 100 ? 37.520 -33.669 9.469   0.28 32.35 ?  100 VAL   B HG11 1 
ATOM   5484 H  HG12 A VAL   B 1 100 ? 38.814 -33.679 10.397  0.72 33.95 ?  100 VAL   B HG12 1 
ATOM   5485 H  HG12 B VAL   B 1 100 ? 38.854 -33.700 10.329  0.28 32.35 ?  100 VAL   B HG12 1 
ATOM   5486 H  HG13 A VAL   B 1 100 ? 37.579 -32.835 10.936  0.72 33.95 ?  100 VAL   B HG13 1 
ATOM   5487 H  HG13 B VAL   B 1 100 ? 37.595 -32.876 10.842  0.28 32.35 ?  100 VAL   B HG13 1 
ATOM   5488 H  HG21 A VAL   B 1 100 ? 36.981 -31.914 8.048   0.72 33.40 ?  100 VAL   B HG21 1 
ATOM   5489 H  HG21 B VAL   B 1 100 ? 37.064 -31.928 7.955   0.28 32.24 ?  100 VAL   B HG21 1 
ATOM   5490 H  HG22 A VAL   B 1 100 ? 36.743 -30.938 9.278   0.72 33.40 ?  100 VAL   B HG22 1 
ATOM   5491 H  HG22 B VAL   B 1 100 ? 36.798 -30.949 9.178   0.28 32.24 ?  100 VAL   B HG22 1 
ATOM   5492 H  HG23 A VAL   B 1 100 ? 37.734 -30.517 8.110   0.72 33.40 ?  100 VAL   B HG23 1 
ATOM   5493 H  HG23 B VAL   B 1 100 ? 37.817 -30.531 8.033   0.28 32.24 ?  100 VAL   B HG23 1 
ATOM   5494 N  N    . ASN   B 1 101 ? 41.510 -31.594 10.851  1.00 26.14 ?  101 ASN   B N    1 
ATOM   5495 C  CA   . ASN   B 1 101 ? 42.553 -32.124 11.727  1.00 28.05 ?  101 ASN   B CA   1 
ATOM   5496 C  C    . ASN   B 1 101 ? 42.749 -31.286 12.984  1.00 30.42 ?  101 ASN   B C    1 
ATOM   5497 O  O    . ASN   B 1 101 ? 43.388 -31.761 13.932  1.00 31.37 ?  101 ASN   B O    1 
ATOM   5498 C  CB   . ASN   B 1 101 ? 43.876 -32.255 10.967  1.00 27.77 ?  101 ASN   B CB   1 
ATOM   5499 C  CG   . ASN   B 1 101 ? 43.867 -33.408 9.980   1.00 27.08 ?  101 ASN   B CG   1 
ATOM   5500 O  OD1  . ASN   B 1 101 ? 43.215 -34.422 10.206  1.00 27.84 ?  101 ASN   B OD1  1 
ATOM   5501 N  ND2  . ASN   B 1 101 ? 44.586 -33.254 8.878   1.00 26.83 ?  101 ASN   B ND2  1 
ATOM   5502 H  H    A ASN   B 1 101 ? 41.787 -31.333 10.080  0.72 31.41 ?  101 ASN   B H    1 
ATOM   5503 H  H    B ASN   B 1 101 ? 41.792 -31.321 10.086  0.28 31.41 ?  101 ASN   B H    1 
ATOM   5504 H  HA   . ASN   B 1 101 ? 42.292 -33.008 12.013  1.00 33.70 ?  101 ASN   B HA   1 
ATOM   5505 H  HB2  . ASN   B 1 101 ? 44.047 -31.440 10.472  1.00 33.38 ?  101 ASN   B HB2  1 
ATOM   5506 H  HB3  . ASN   B 1 101 ? 44.592 -32.409 11.606  1.00 33.38 ?  101 ASN   B HB3  1 
ATOM   5507 H  HD21 . ASN   B 1 101 ? 44.610 -33.883 8.293   1.00 32.24 ?  101 ASN   B HD21 1 
ATOM   5508 H  HD22 . ASN   B 1 101 ? 45.025 -32.528 8.750   1.00 32.24 ?  101 ASN   B HD22 1 
ATOM   5509 N  N    . LYS   B 1 102 ? 42.226 -30.059 13.009  1.00 33.33 ?  102 LYS   B N    1 
ATOM   5510 C  CA   . LYS   B 1 102 ? 42.191 -29.225 14.202  1.00 36.60 ?  102 LYS   B CA   1 
ATOM   5511 C  C    . LYS   B 1 102 ? 40.807 -29.181 14.836  1.00 35.89 ?  102 LYS   B C    1 
ATOM   5512 O  O    . LYS   B 1 102 ? 40.576 -28.374 15.742  1.00 36.36 ?  102 LYS   B O    1 
ATOM   5513 C  CB   . LYS   B 1 102 ? 42.637 -27.799 13.871  1.00 40.56 ?  102 LYS   B CB   1 
ATOM   5514 C  CG   . LYS   B 1 102 ? 44.103 -27.650 13.507  1.00 44.36 ?  102 LYS   B CG   1 
ATOM   5515 C  CD   . LYS   B 1 102 ? 44.386 -26.231 13.038  1.00 47.74 ?  102 LYS   B CD   1 
ATOM   5516 C  CE   . LYS   B 1 102 ? 45.870 -25.978 12.844  1.00 50.22 ?  102 LYS   B CE   1 
ATOM   5517 N  NZ   . LYS   B 1 102 ? 46.125 -24.584 12.375  1.00 51.70 ?  102 LYS   B NZ   1 
ATOM   5518 H  H    . LYS   B 1 102 ? 41.870 -29.678 12.324  1.00 40.05 ?  102 LYS   B H    1 
ATOM   5519 H  HA   . LYS   B 1 102 ? 42.811 -29.583 14.855  1.00 43.96 ?  102 LYS   B HA   1 
ATOM   5520 H  HB2  . LYS   B 1 102 ? 42.115 -27.479 13.119  1.00 48.72 ?  102 LYS   B HB2  1 
ATOM   5521 H  HB3  . LYS   B 1 102 ? 42.471 -27.235 14.644  1.00 48.72 ?  102 LYS   B HB3  1 
ATOM   5522 H  HG2  . LYS   B 1 102 ? 44.652 -27.832 14.286  1.00 53.27 ?  102 LYS   B HG2  1 
ATOM   5523 H  HG3  . LYS   B 1 102 ? 44.323 -28.262 12.787  1.00 53.27 ?  102 LYS   B HG3  1 
ATOM   5524 H  HD2  . LYS   B 1 102 ? 43.940 -26.082 12.189  1.00 57.34 ?  102 LYS   B HD2  1 
ATOM   5525 H  HD3  . LYS   B 1 102 ? 44.056 -25.605 13.702  1.00 57.34 ?  102 LYS   B HD3  1 
ATOM   5526 H  HE2  . LYS   B 1 102 ? 46.330 -26.104 13.689  1.00 60.31 ?  102 LYS   B HE2  1 
ATOM   5527 H  HE3  . LYS   B 1 102 ? 46.216 -26.592 12.177  1.00 60.31 ?  102 LYS   B HE3  1 
ATOM   5528 H  HZ1  . LYS   B 1 102 ? 46.998 -24.454 12.267  1.00 62.09 ?  102 LYS   B HZ1  1 
ATOM   5529 H  HZ2  . LYS   B 1 102 ? 45.713 -24.445 11.598  1.00 62.09 ?  102 LYS   B HZ2  1 
ATOM   5530 H  HZ3  . LYS   B 1 102 ? 45.817 -24.001 12.973  1.00 62.09 ?  102 LYS   B HZ3  1 
ATOM   5531 N  N    . GLY   B 1 103 ? 39.877 -30.011 14.369  1.00 35.00 ?  103 GLY   B N    1 
ATOM   5532 C  CA   . GLY   B 1 103 ? 38.548 -30.074 14.942  1.00 34.35 ?  103 GLY   B CA   1 
ATOM   5533 C  C    . GLY   B 1 103 ? 37.596 -28.990 14.495  1.00 33.06 ?  103 GLY   B C    1 
ATOM   5534 O  O    . GLY   B 1 103 ? 36.509 -28.868 15.071  1.00 33.63 ?  103 GLY   B O    1 
ATOM   5535 H  H    . GLY   B 1 103 ? 39.997 -30.550 13.712  1.00 42.05 ?  103 GLY   B H    1 
ATOM   5536 H  HA2  . GLY   B 1 103 ? 38.152 -30.929 14.716  1.00 41.26 ?  103 GLY   B HA2  1 
ATOM   5537 H  HA3  . GLY   B 1 103 ? 38.621 -30.024 15.908  1.00 41.26 ?  103 GLY   B HA3  1 
ATOM   5538 N  N    A GLU   B 1 104 ? 37.968 -28.194 13.495  0.72 31.63 ?  104 GLU   B N    1 
ATOM   5539 N  N    B GLU   B 1 104 ? 37.954 -28.208 13.482  0.28 32.33 ?  104 GLU   B N    1 
ATOM   5540 C  CA   A GLU   B 1 104 ? 37.127 -27.094 13.053  0.72 30.12 ?  104 GLU   B CA   1 
ATOM   5541 C  CA   B GLU   B 1 104 ? 37.093 -27.130 13.023  0.28 31.43 ?  104 GLU   B CA   1 
ATOM   5542 C  C    A GLU   B 1 104 ? 35.940 -27.615 12.243  0.72 30.54 ?  104 GLU   B C    1 
ATOM   5543 C  C    B GLU   B 1 104 ? 35.935 -27.677 12.193  0.28 31.56 ?  104 GLU   B C    1 
ATOM   5544 O  O    A GLU   B 1 104 ? 35.974 -28.705 11.662  0.72 31.13 ?  104 GLU   B O    1 
ATOM   5545 O  O    B GLU   B 1 104 ? 36.021 -28.752 11.592  0.28 31.74 ?  104 GLU   B O    1 
ATOM   5546 C  CB   A GLU   B 1 104 ? 37.954 -26.092 12.246  0.72 28.73 ?  104 GLU   B CB   1 
ATOM   5547 C  CB   B GLU   B 1 104 ? 37.906 -26.109 12.226  0.28 30.45 ?  104 GLU   B CB   1 
ATOM   5548 C  CG   A GLU   B 1 104 ? 39.067 -25.462 13.074  0.72 27.41 ?  104 GLU   B CG   1 
ATOM   5549 C  CG   B GLU   B 1 104 ? 39.008 -25.466 13.059  0.28 29.59 ?  104 GLU   B CG   1 
ATOM   5550 C  CD   A GLU   B 1 104 ? 39.992 -24.565 12.279  0.72 25.84 ?  104 GLU   B CD   1 
ATOM   5551 C  CD   B GLU   B 1 104 ? 39.940 -24.594 12.243  0.28 28.80 ?  104 GLU   B CD   1 
ATOM   5552 O  OE1  A GLU   B 1 104 ? 39.987 -24.620 11.031  0.72 23.86 ?  104 GLU   B OE1  1 
ATOM   5553 O  OE1  B GLU   B 1 104 ? 39.852 -24.617 10.997  0.28 28.26 ?  104 GLU   B OE1  1 
ATOM   5554 O  OE2  A GLU   B 1 104 ? 40.734 -23.793 12.920  0.72 26.06 -1 104 GLU   B OE2  1 
ATOM   5555 O  OE2  B GLU   B 1 104 ? 40.766 -23.884 12.853  0.28 28.68 -1 104 GLU   B OE2  1 
ATOM   5556 H  H    A GLU   B 1 104 ? 38.707 -28.269 13.063  0.72 38.01 ?  104 GLU   B H    1 
ATOM   5557 H  H    B GLU   B 1 104 ? 38.694 -28.278 13.050  0.28 38.85 ?  104 GLU   B H    1 
ATOM   5558 H  HA   A GLU   B 1 104 ? 36.781 -26.631 13.832  0.72 36.20 ?  104 GLU   B HA   1 
ATOM   5559 H  HA   B GLU   B 1 104 ? 36.720 -26.675 13.792  0.28 37.76 ?  104 GLU   B HA   1 
ATOM   5560 H  HB2  A GLU   B 1 104 ? 38.360 -26.547 11.492  0.72 34.52 ?  104 GLU   B HB2  1 
ATOM   5561 H  HB2  B GLU   B 1 104 ? 38.320 -26.552 11.470  0.28 36.59 ?  104 GLU   B HB2  1 
ATOM   5562 H  HB3  A GLU   B 1 104 ? 37.374 -25.379 11.932  0.72 34.52 ?  104 GLU   B HB3  1 
ATOM   5563 H  HB3  B GLU   B 1 104 ? 37.315 -25.404 11.916  0.28 36.59 ?  104 GLU   B HB3  1 
ATOM   5564 H  HG2  A GLU   B 1 104 ? 38.672 -24.919 13.774  0.72 32.94 ?  104 GLU   B HG2  1 
ATOM   5565 H  HG2  B GLU   B 1 104 ? 38.602 -24.910 13.743  0.28 35.55 ?  104 GLU   B HG2  1 
ATOM   5566 H  HG3  A GLU   B 1 104 ? 39.605 -26.166 13.469  0.72 32.94 ?  104 GLU   B HG3  1 
ATOM   5567 H  HG3  B GLU   B 1 104 ? 39.538 -26.165 13.476  0.28 35.55 ?  104 GLU   B HG3  1 
ATOM   5568 N  N    A ASP   B 1 105 ? 34.876 -26.815 12.217  0.72 30.29 ?  105 ASP   B N    1 
ATOM   5569 N  N    B ASP   B 1 105 ? 34.841 -26.917 12.170  0.28 31.42 ?  105 ASP   B N    1 
ATOM   5570 C  CA   A ASP   B 1 105 ? 33.600 -27.264 11.672  0.72 30.89 ?  105 ASP   B CA   1 
ATOM   5571 C  CA   B ASP   B 1 105 ? 33.586 -27.392 11.600  0.28 31.45 ?  105 ASP   B CA   1 
ATOM   5572 C  C    A ASP   B 1 105 ? 33.660 -27.319 10.150  0.72 28.84 ?  105 ASP   B C    1 
ATOM   5573 C  C    B ASP   B 1 105 ? 33.667 -27.405 10.078  0.28 30.39 ?  105 ASP   B C    1 
ATOM   5574 O  O    A ASP   B 1 105 ? 33.831 -26.291 9.488   0.72 28.06 ?  105 ASP   B O    1 
ATOM   5575 O  O    B ASP   B 1 105 ? 33.897 -26.367 9.449   0.28 30.15 ?  105 ASP   B O    1 
ATOM   5576 C  CB   A ASP   B 1 105 ? 32.489 -26.319 12.125  0.72 33.84 ?  105 ASP   B CB   1 
ATOM   5577 C  CB   B ASP   B 1 105 ? 32.438 -26.499 12.067  0.28 32.46 ?  105 ASP   B CB   1 
ATOM   5578 C  CG   A ASP   B 1 105 ? 31.112 -26.795 11.705  0.72 36.23 ?  105 ASP   B CG   1 
ATOM   5579 C  CG   B ASP   B 1 105 ? 31.075 -27.071 11.719  0.28 33.31 ?  105 ASP   B CG   1 
ATOM   5580 O  OD1  A ASP   B 1 105 ? 31.007 -27.911 11.153  0.72 36.39 ?  105 ASP   B OD1  1 
ATOM   5581 O  OD1  B ASP   B 1 105 ? 31.024 -28.110 11.027  0.28 33.48 ?  105 ASP   B OD1  1 
ATOM   5582 O  OD2  A ASP   B 1 105 ? 30.132 -26.051 11.926  0.72 37.63 -1 105 ASP   B OD2  1 
ATOM   5583 O  OD2  B ASP   B 1 105 ? 30.055 -26.489 12.145  0.28 33.63 -1 105 ASP   B OD2  1 
ATOM   5584 H  H    A ASP   B 1 105 ? 34.867 -26.005 12.511  0.72 36.40 ?  105 ASP   B H    1 
ATOM   5585 H  H    B ASP   B 1 105 ? 34.804 -26.119 12.476  0.28 37.75 ?  105 ASP   B H    1 
ATOM   5586 H  HA   A ASP   B 1 105 ? 33.401 -28.153 12.008  0.72 37.11 ?  105 ASP   B HA   1 
ATOM   5587 H  HA   B ASP   B 1 105 ? 33.406 -28.295 11.905  0.28 37.78 ?  105 ASP   B HA   1 
ATOM   5588 H  HB2  A ASP   B 1 105 ? 32.511 -26.246 13.094  0.72 40.65 ?  105 ASP   B HB2  1 
ATOM   5589 H  HB2  B ASP   B 1 105 ? 32.481 -26.402 13.033  0.28 39.00 ?  105 ASP   B HB2  1 
ATOM   5590 H  HB3  A ASP   B 1 105 ? 32.633 -25.448 11.725  0.72 40.65 ?  105 ASP   B HB3  1 
ATOM   5591 H  HB3  B ASP   B 1 105 ? 32.521 -25.626 11.647  0.28 39.00 ?  105 ASP   B HB3  1 
ATOM   5592 N  N    A ILE   B 1 106 ? 33.484 -28.523 9.597   0.72 28.10 ?  106 ILE   B N    1 
ATOM   5593 N  N    B ILE   B 1 106 ? 33.468 -28.587 9.488   0.28 29.55 ?  106 ILE   B N    1 
ATOM   5594 C  CA   A ILE   B 1 106 ? 33.488 -28.710 8.151   0.72 27.05 ?  106 ILE   B CA   1 
ATOM   5595 C  CA   B ILE   B 1 106 ? 33.481 -28.730 8.037   0.28 28.80 ?  106 ILE   B CA   1 
ATOM   5596 C  C    A ILE   B 1 106 ? 32.395 -27.891 7.472   0.72 25.68 ?  106 ILE   B C    1 
ATOM   5597 C  C    B ILE   B 1 106 ? 32.381 -27.909 7.377   0.28 28.06 ?  106 ILE   B C    1 
ATOM   5598 O  O    A ILE   B 1 106 ? 32.509 -27.574 6.283   0.72 24.96 ?  106 ILE   B O    1 
ATOM   5599 O  O    B ILE   B 1 106 ? 32.460 -27.619 6.178   0.28 27.86 ?  106 ILE   B O    1 
ATOM   5600 C  CB   A ILE   B 1 106 ? 33.386 -30.219 7.826   0.72 27.61 ?  106 ILE   B CB   1 
ATOM   5601 C  CB   B ILE   B 1 106 ? 33.388 -30.228 7.664   0.28 28.89 ?  106 ILE   B CB   1 
ATOM   5602 C  CG1  A ILE   B 1 106 ? 33.649 -30.483 6.343   0.72 27.93 ?  106 ILE   B CG1  1 
ATOM   5603 C  CG1  B ILE   B 1 106 ? 33.677 -30.444 6.176   0.28 28.88 ?  106 ILE   B CG1  1 
ATOM   5604 C  CG2  A ILE   B 1 106 ? 32.021 -30.767 8.231   0.72 28.39 ?  106 ILE   B CG2  1 
ATOM   5605 C  CG2  B ILE   B 1 106 ? 32.019 -30.789 8.026   0.28 29.14 ?  106 ILE   B CG2  1 
ATOM   5606 C  CD1  A ILE   B 1 106 ? 35.007 -30.016 5.881   0.72 27.80 ?  106 ILE   B CD1  1 
ATOM   5607 C  CD1  B ILE   B 1 106 ? 35.036 -29.944 5.743   0.28 28.85 ?  106 ILE   B CD1  1 
ATOM   5608 H  H    A ILE   B 1 106 ? 33.359 -29.244 10.046  0.72 33.77 ?  106 ILE   B H    1 
ATOM   5609 H  H    B ILE   B 1 106 ? 33.334 -29.321 9.911   0.28 35.51 ?  106 ILE   B H    1 
ATOM   5610 H  HA   A ILE   B 1 106 ? 34.335 -28.394 7.815   0.72 32.50 ?  106 ILE   B HA   1 
ATOM   5611 H  HA   B ILE   B 1 106 ? 34.326 -28.394 7.711   0.28 34.61 ?  106 ILE   B HA   1 
ATOM   5612 H  HB   A ILE   B 1 106 ? 34.060 -30.689 8.342   0.72 33.18 ?  106 ILE   B HB   1 
ATOM   5613 H  HB   B ILE   B 1 106 ? 34.056 -30.710 8.174   0.28 34.72 ?  106 ILE   B HB   1 
ATOM   5614 H  HG12 A ILE   B 1 106 ? 33.596 -31.440 6.181   0.72 33.57 ?  106 ILE   B HG12 1 
ATOM   5615 H  HG12 B ILE   B 1 106 ? 33.640 -31.396 5.986   0.28 34.71 ?  106 ILE   B HG12 1 
ATOM   5616 H  HG13 A ILE   B 1 106 ? 32.980 -30.023 5.817   0.72 33.57 ?  106 ILE   B HG13 1 
ATOM   5617 H  HG13 B ILE   B 1 106 ? 33.008 -29.979 5.653   0.28 34.71 ?  106 ILE   B HG13 1 
ATOM   5618 H  HG21 A ILE   B 1 106 ? 32.029 -31.734 8.150   0.72 34.11 ?  106 ILE   B HG21 1 
ATOM   5619 H  HG21 B ILE   B 1 106 ? 32.039 -31.754 7.934   0.28 35.01 ?  106 ILE   B HG21 1 
ATOM   5620 H  HG22 A ILE   B 1 106 ? 31.839 -30.517 9.152   0.72 34.11 ?  106 ILE   B HG22 1 
ATOM   5621 H  HG22 B ILE   B 1 106 ? 31.814 -30.550 8.944   0.28 35.01 ?  106 ILE   B HG22 1 
ATOM   5622 H  HG23 A ILE   B 1 106 ? 31.341 -30.394 7.649   0.72 34.11 ?  106 ILE   B HG23 1 
ATOM   5623 H  HG23 B ILE   B 1 106 ? 31.353 -30.414 7.430   0.28 35.01 ?  106 ILE   B HG23 1 
ATOM   5624 H  HD11 A ILE   B 1 106 ? 35.211 -30.433 5.031   0.72 33.41 ?  106 ILE   B HD11 1 
ATOM   5625 H  HD11 B ILE   B 1 106 ? 35.259 -30.341 4.888   0.28 34.66 ?  106 ILE   B HD11 1 
ATOM   5626 H  HD12 A ILE   B 1 106 ? 34.993 -29.051 5.781   0.72 33.41 ?  106 ILE   B HD12 1 
ATOM   5627 H  HD12 B ILE   B 1 106 ? 35.005 -28.978 5.663   0.28 34.66 ?  106 ILE   B HD12 1 
ATOM   5628 H  HD13 A ILE   B 1 106 ? 35.672 -30.271 6.541   0.72 33.41 ?  106 ILE   B HD13 1 
ATOM   5629 H  HD13 B ILE   B 1 106 ? 35.693 -30.202 6.409   0.28 34.66 ?  106 ILE   B HD13 1 
ATOM   5630 N  N    A GLN   B 1 107 ? 31.341 -27.522 8.203   0.72 25.90 ?  107 GLN   B N    1 
ATOM   5631 N  N    B GLN   B 1 107 ? 31.349 -27.522 8.132   0.28 27.78 ?  107 GLN   B N    1 
ATOM   5632 C  CA   A GLN   B 1 107 ? 30.266 -26.725 7.620   0.72 26.16 ?  107 GLN   B CA   1 
ATOM   5633 C  CA   B GLN   B 1 107 ? 30.267 -26.720 7.572   0.28 27.43 ?  107 GLN   B CA   1 
ATOM   5634 C  C    A GLN   B 1 107 ? 30.749 -25.373 7.109   0.72 23.88 ?  107 GLN   B C    1 
ATOM   5635 C  C    B GLN   B 1 107 ? 30.746 -25.352 7.101   0.28 24.79 ?  107 GLN   B C    1 
ATOM   5636 O  O    A GLN   B 1 107 ? 30.098 -24.792 6.237   0.72 24.32 ?  107 GLN   B O    1 
ATOM   5637 O  O    B GLN   B 1 107 ? 30.087 -24.737 6.256   0.28 24.99 ?  107 GLN   B O    1 
ATOM   5638 C  CB   A GLN   B 1 107 ? 29.150 -26.522 8.650   0.72 29.78 ?  107 GLN   B CB   1 
ATOM   5639 C  CB   B GLN   B 1 107 ? 29.150 -26.562 8.608   0.28 29.92 ?  107 GLN   B CB   1 
ATOM   5640 C  CG   A GLN   B 1 107 ? 27.825 -26.024 8.070   0.72 33.32 ?  107 GLN   B CG   1 
ATOM   5641 C  CG   B GLN   B 1 107 ? 27.817 -26.082 8.044   0.28 32.20 ?  107 GLN   B CG   1 
ATOM   5642 C  CD   A GLN   B 1 107 ? 27.749 -24.509 7.966   0.72 35.95 ?  107 GLN   B CD   1 
ATOM   5643 C  CD   B GLN   B 1 107 ? 27.700 -24.569 8.006   0.28 34.00 ?  107 GLN   B CD   1 
ATOM   5644 O  OE1  A GLN   B 1 107 ? 28.584 -23.792 8.521   0.72 36.91 ?  107 GLN   B OE1  1 
ATOM   5645 O  OE1  B GLN   B 1 107 ? 28.513 -23.855 8.594   0.28 34.64 ?  107 GLN   B OE1  1 
ATOM   5646 N  NE2  A GLN   B 1 107 ? 26.738 -24.014 7.253   0.72 36.85 ?  107 GLN   B NE2  1 
ATOM   5647 N  NE2  B GLN   B 1 107 ? 26.680 -24.072 7.313   0.28 34.63 ?  107 GLN   B NE2  1 
ATOM   5648 H  H    A GLN   B 1 107 ? 31.225 -27.719 9.028   0.72 31.12 ?  107 GLN   B H    1 
ATOM   5649 H  H    B GLN   B 1 107 ? 31.252 -27.713 8.963   0.28 33.38 ?  107 GLN   B H    1 
ATOM   5650 H  HA   A GLN   B 1 107 ? 29.890 -27.210 6.867   0.72 31.44 ?  107 GLN   B HA   1 
ATOM   5651 H  HA   B GLN   B 1 107 ? 29.895 -27.186 6.808   0.28 32.97 ?  107 GLN   B HA   1 
ATOM   5652 H  HB2  A GLN   B 1 107 ? 28.977 -27.368 9.085   0.72 35.78 ?  107 GLN   B HB2  1 
ATOM   5653 H  HB2  B GLN   B 1 107 ? 28.996 -27.422 9.023   0.28 35.95 ?  107 GLN   B HB2  1 
ATOM   5654 H  HB3  A GLN   B 1 107 ? 29.448 -25.872 9.305   0.72 35.78 ?  107 GLN   B HB3  1 
ATOM   5655 H  HB3  B GLN   B 1 107 ? 29.436 -25.923 9.278   0.28 35.95 ?  107 GLN   B HB3  1 
ATOM   5656 H  HG2  A GLN   B 1 107 ? 27.711 -26.387 7.179   0.72 40.03 ?  107 GLN   B HG2  1 
ATOM   5657 H  HG2  B GLN   B 1 107 ? 27.717 -26.411 7.138   0.28 38.69 ?  107 GLN   B HG2  1 
ATOM   5658 H  HG3  A GLN   B 1 107 ? 27.099 -26.323 8.643   0.72 40.03 ?  107 GLN   B HG3  1 
ATOM   5659 H  HG3  B GLN   B 1 107 ? 27.097 -26.426 8.601   0.28 38.69 ?  107 GLN   B HG3  1 
ATOM   5660 H  HE21 A GLN   B 1 107 ? 26.173 -24.545 6.878   0.72 44.27 ?  107 GLN   B HE21 1 
ATOM   5661 H  HE21 B GLN   B 1 107 ? 26.131 -24.601 6.914   0.28 41.60 ?  107 GLN   B HE21 1 
ATOM   5662 H  HE22 A GLN   B 1 107 ? 26.646 -23.162 7.167   0.72 44.27 ?  107 GLN   B HE22 1 
ATOM   5663 H  HE22 B GLN   B 1 107 ? 26.569 -23.221 7.264   0.28 41.60 ?  107 GLN   B HE22 1 
ATOM   5664 N  N    . LEU   B 1 108 ? 31.876 -24.864 7.619   1.00 22.13 ?  108 LEU   B N    1 
ATOM   5665 C  CA   . LEU   B 1 108 ? 32.414 -23.565 7.206   1.00 19.49 ?  108 LEU   B CA   1 
ATOM   5666 C  C    . LEU   B 1 108 ? 33.061 -23.589 5.830   1.00 16.64 ?  108 LEU   B C    1 
ATOM   5667 O  O    . LEU   B 1 108 ? 33.493 -22.532 5.341   1.00 16.11 ?  108 LEU   B O    1 
ATOM   5668 C  CB   . LEU   B 1 108 ? 33.418 -23.068 8.244   1.00 20.20 ?  108 LEU   B CB   1 
ATOM   5669 C  CG   . LEU   B 1 108 ? 32.789 -22.589 9.553   1.00 21.42 ?  108 LEU   B CG   1 
ATOM   5670 C  CD1  . LEU   B 1 108 ? 33.815 -22.543 10.673  1.00 21.91 ?  108 LEU   B CD1  1 
ATOM   5671 C  CD2  . LEU   B 1 108 ? 32.168 -21.220 9.351   1.00 22.42 ?  108 LEU   B CD2  1 
ATOM   5672 H  H    A LEU   B 1 108 ? 32.341 -25.256 8.224   0.72 26.61 ?  108 LEU   B H    1 
ATOM   5673 H  H    B LEU   B 1 108 ? 32.340 -25.264 8.219   0.28 26.61 ?  108 LEU   B H    1 
ATOM   5674 H  HA   . LEU   B 1 108 ? 31.685 -22.930 7.175   1.00 23.44 ?  108 LEU   B HA   1 
ATOM   5675 H  HB2  . LEU   B 1 108 ? 34.024 -23.792 8.459   1.00 24.29 ?  108 LEU   B HB2  1 
ATOM   5676 H  HB3  . LEU   B 1 108 ? 33.909 -22.326 7.866   1.00 24.29 ?  108 LEU   B HB3  1 
ATOM   5677 H  HG   . LEU   B 1 108 ? 32.083 -23.204 9.815   1.00 25.75 ?  108 LEU   B HG   1 
ATOM   5678 H  HD11 . LEU   B 1 108 ? 33.374 -22.272 11.495  1.00 26.34 ?  108 LEU   B HD11 1 
ATOM   5679 H  HD12 . LEU   B 1 108 ? 34.202 -23.425 10.782  1.00 26.34 ?  108 LEU   B HD12 1 
ATOM   5680 H  HD13 . LEU   B 1 108 ? 34.505 -21.903 10.442  1.00 26.34 ?  108 LEU   B HD13 1 
ATOM   5681 H  HD21 . LEU   B 1 108 ? 31.824 -20.900 10.200  1.00 26.96 ?  108 LEU   B HD21 1 
ATOM   5682 H  HD22 . LEU   B 1 108 ? 32.848 -20.613 9.020   1.00 26.96 ?  108 LEU   B HD22 1 
ATOM   5683 H  HD23 . LEU   B 1 108 ? 31.446 -21.291 8.708   1.00 26.96 ?  108 LEU   B HD23 1 
ATOM   5684 N  N    . LEU   B 1 109 ? 33.125 -24.757 5.196   1.00 15.66 ?  109 LEU   B N    1 
ATOM   5685 C  CA   . LEU   B 1 109 ? 33.753 -24.863 3.888   1.00 14.80 ?  109 LEU   B CA   1 
ATOM   5686 C  C    . LEU   B 1 109 ? 32.986 -24.079 2.828   1.00 14.08 ?  109 LEU   B C    1 
ATOM   5687 O  O    . LEU   B 1 109 ? 33.601 -23.488 1.932   1.00 13.79 ?  109 LEU   B O    1 
ATOM   5688 C  CB   . LEU   B 1 109 ? 33.879 -26.337 3.509   1.00 14.89 ?  109 LEU   B CB   1 
ATOM   5689 C  CG   . LEU   B 1 109 ? 34.659 -26.681 2.244   1.00 14.69 ?  109 LEU   B CG   1 
ATOM   5690 C  CD1  . LEU   B 1 109 ? 36.035 -26.028 2.252   1.00 14.31 ?  109 LEU   B CD1  1 
ATOM   5691 C  CD2  . LEU   B 1 109 ? 34.783 -28.191 2.102   1.00 15.48 ?  109 LEU   B CD2  1 
ATOM   5692 H  H    . LEU   B 1 109 ? 32.823 -25.502 5.498   1.00 18.84 ?  109 LEU   B H    1 
ATOM   5693 H  HA   . LEU   B 1 109 ? 34.646 -24.494 3.934   1.00 17.81 ?  109 LEU   B HA   1 
ATOM   5694 H  HB2  . LEU   B 1 109 ? 34.321 -26.801 4.238   1.00 17.92 ?  109 LEU   B HB2  1 
ATOM   5695 H  HB3  . LEU   B 1 109 ? 32.989 -26.702 3.394   1.00 17.92 ?  109 LEU   B HB3  1 
ATOM   5696 H  HG   . LEU   B 1 109 ? 34.173 -26.358 1.467   1.00 17.67 ?  109 LEU   B HG   1 
ATOM   5697 H  HD11 . LEU   B 1 109 ? 36.564 -26.391 1.523   1.00 17.22 ?  109 LEU   B HD11 1 
ATOM   5698 H  HD12 . LEU   B 1 109 ? 35.928 -25.073 2.140   1.00 17.22 ?  109 LEU   B HD12 1 
ATOM   5699 H  HD13 . LEU   B 1 109 ? 36.468 -26.221 3.099   1.00 17.22 ?  109 LEU   B HD13 1 
ATOM   5700 H  HD21 . LEU   B 1 109 ? 35.353 -28.397 1.343   1.00 18.62 ?  109 LEU   B HD21 1 
ATOM   5701 H  HD22 . LEU   B 1 109 ? 35.170 -28.556 2.912   1.00 18.62 ?  109 LEU   B HD22 1 
ATOM   5702 H  HD23 . LEU   B 1 109 ? 33.899 -28.573 1.960   1.00 18.62 ?  109 LEU   B HD23 1 
ATOM   5703 N  N    . LYS   B 1 110 ? 31.652 -24.043 2.912   1.00 14.05 ?  110 LYS   B N    1 
ATOM   5704 C  CA   . LYS   B 1 110 ? 30.895 -23.285 1.919   1.00 13.72 ?  110 LYS   B CA   1 
ATOM   5705 C  C    . LYS   B 1 110 ? 31.231 -21.797 2.006   1.00 13.29 ?  110 LYS   B C    1 
ATOM   5706 O  O    . LYS   B 1 110 ? 31.489 -21.147 0.986   1.00 13.23 ?  110 LYS   B O    1 
ATOM   5707 C  CB   . LYS   B 1 110 ? 29.390 -23.534 2.063   1.00 14.29 ?  110 LYS   B CB   1 
ATOM   5708 C  CG   . LYS   B 1 110 ? 28.587 -22.914 0.925   1.00 14.52 ?  110 LYS   B CG   1 
ATOM   5709 C  CD   . LYS   B 1 110 ? 27.117 -23.333 0.957   1.00 14.68 ?  110 LYS   B CD   1 
ATOM   5710 C  CE   . LYS   B 1 110 ? 26.356 -22.806 -0.258  1.00 15.71 ?  110 LYS   B CE   1 
ATOM   5711 N  NZ   . LYS   B 1 110 ? 26.679 -23.538 -1.510  1.00 16.12 ?  110 LYS   B NZ   1 
ATOM   5712 H  H    . LYS   B 1 110 ? 31.182 -24.437 3.511   1.00 16.91 ?  110 LYS   B H    1 
ATOM   5713 H  HA   . LYS   B 1 110 ? 31.156 -23.590 1.035   1.00 16.51 ?  110 LYS   B HA   1 
ATOM   5714 H  HB2  . LYS   B 1 110 ? 29.228 -24.496 2.058   1.00 17.20 ?  110 LYS   B HB2  1 
ATOM   5715 H  HB3  . LYS   B 1 110 ? 29.082 -23.154 2.898   1.00 17.20 ?  110 LYS   B HB3  1 
ATOM   5716 H  HG2  . LYS   B 1 110 ? 28.622 -21.950 1.002   1.00 17.47 ?  110 LYS   B HG2  1 
ATOM   5717 H  HG3  . LYS   B 1 110 ? 28.959 -23.200 0.078   1.00 17.47 ?  110 LYS   B HG3  1 
ATOM   5718 H  HD2  . LYS   B 1 110 ? 27.057 -24.305 0.955   1.00 17.67 ?  110 LYS   B HD2  1 
ATOM   5719 H  HD3  . LYS   B 1 110 ? 26.696 -22.979 1.760   1.00 17.67 ?  110 LYS   B HD3  1 
ATOM   5720 H  HE2  . LYS   B 1 110 ? 25.404 -22.887 -0.099  1.00 18.90 ?  110 LYS   B HE2  1 
ATOM   5721 H  HE3  . LYS   B 1 110 ? 26.590 -21.871 -0.391  1.00 18.90 ?  110 LYS   B HE3  1 
ATOM   5722 H  HZ1  . LYS   B 1 110 ? 26.220 -23.198 -2.189  1.00 19.40 ?  110 LYS   B HZ1  1 
ATOM   5723 H  HZ2  . LYS   B 1 110 ? 27.550 -23.472 -1.684  1.00 19.40 ?  110 LYS   B HZ2  1 
ATOM   5724 H  HZ3  . LYS   B 1 110 ? 26.468 -24.399 -1.418  1.00 19.40 ?  110 LYS   B HZ3  1 
ATOM   5725 N  N    . SER   B 1 111 ? 31.251 -21.245 3.226   1.00 13.97 ?  111 SER   B N    1 
ATOM   5726 C  CA   . SER   B 1 111 ? 31.645 -19.849 3.403   1.00 13.79 ?  111 SER   B CA   1 
ATOM   5727 C  C    . SER   B 1 111 ? 33.021 -19.590 2.807   1.00 12.95 ?  111 SER   B C    1 
ATOM   5728 O  O    . SER   B 1 111 ? 33.247 -18.558 2.158   1.00 13.37 ?  111 SER   B O    1 
ATOM   5729 C  CB   . SER   B 1 111 ? 31.650 -19.493 4.889   1.00 14.90 ?  111 SER   B CB   1 
ATOM   5730 O  OG   . SER   B 1 111 ? 30.347 -19.486 5.427   1.00 16.31 ?  111 SER   B OG   1 
ATOM   5731 H  H    . SER   B 1 111 ? 31.058 -21.664 3.954   1.00 16.82 ?  111 SER   B H    1 
ATOM   5732 H  HA   . SER   B 1 111 ? 31.009 -19.280 2.954   1.00 16.60 ?  111 SER   B HA   1 
ATOM   5733 H  HB2  . SER   B 1 111 ? 32.177 -20.150 5.372   1.00 17.93 ?  111 SER   B HB2  1 
ATOM   5734 H  HB3  . SER   B 1 111 ? 32.036 -18.613 5.002   1.00 17.93 ?  111 SER   B HB3  1 
ATOM   5735 H  HG   . SER   B 1 111 ? 30.369 -19.286 6.251   1.00 19.62 ?  111 SER   B HG   1 
ATOM   5736 N  N    . ALA   B 1 112 ? 33.959 -20.510 3.030   1.00 13.08 ?  112 ALA   B N    1 
ATOM   5737 C  CA   . ALA   B 1 112 ? 35.304 -20.338 2.492   1.00 12.81 ?  112 ALA   B CA   1 
ATOM   5738 C  C    . ALA   B 1 112 ? 35.274 -20.243 0.970   1.00 12.17 ?  112 ALA   B C    1 
ATOM   5739 O  O    . ALA   B 1 112 ? 35.901 -19.355 0.378   1.00 12.48 ?  112 ALA   B O    1 
ATOM   5740 C  CB   . ALA   B 1 112 ? 36.200 -21.488 2.957   1.00 13.00 ?  112 ALA   B CB   1 
ATOM   5741 H  H    . ALA   B 1 112 ? 33.845 -21.235 3.491   1.00 15.75 ?  112 ALA   B H    1 
ATOM   5742 H  HA   . ALA   B 1 112 ? 35.675 -19.516 2.838   1.00 15.42 ?  112 ALA   B HA   1 
ATOM   5743 H  HB1  . ALA   B 1 112 ? 37.092 -21.357 2.597   1.00 15.65 ?  112 ALA   B HB1  1 
ATOM   5744 H  HB2  . ALA   B 1 112 ? 36.237 -21.489 3.929   1.00 15.65 ?  112 ALA   B HB2  1 
ATOM   5745 H  HB3  . ALA   B 1 112 ? 35.834 -22.327 2.641   1.00 15.65 ?  112 ALA   B HB3  1 
ATOM   5746 N  N    . TYR   B 1 113 ? 34.537 -21.145 0.315   1.00 12.14 ?  113 TYR   B N    1 
ATOM   5747 C  CA   . TYR   B 1 113 ? 34.464 -21.097 -1.139  1.00 11.77 ?  113 TYR   B CA   1 
ATOM   5748 C  C    . TYR   B 1 113 ? 33.758 -19.845 -1.653  1.00 11.39 ?  113 TYR   B C    1 
ATOM   5749 O  O    . TYR   B 1 113 ? 34.028 -19.414 -2.778  1.00 11.51 ?  113 TYR   B O    1 
ATOM   5750 C  CB   . TYR   B 1 113 ? 33.801 -22.354 -1.699  1.00 12.15 ?  113 TYR   B CB   1 
ATOM   5751 C  CG   . TYR   B 1 113 ? 34.760 -23.504 -1.957  1.00 12.66 ?  113 TYR   B CG   1 
ATOM   5752 C  CD1  . TYR   B 1 113 ? 35.761 -23.403 -2.919  1.00 12.98 ?  113 TYR   B CD1  1 
ATOM   5753 C  CD2  . TYR   B 1 113 ? 34.659 -24.693 -1.253  1.00 12.74 ?  113 TYR   B CD2  1 
ATOM   5754 C  CE1  . TYR   B 1 113 ? 36.635 -24.433 -3.161  1.00 12.96 ?  113 TYR   B CE1  1 
ATOM   5755 C  CE2  . TYR   B 1 113 ? 35.532 -25.746 -1.495  1.00 12.93 ?  113 TYR   B CE2  1 
ATOM   5756 C  CZ   . TYR   B 1 113 ? 36.510 -25.611 -2.455  1.00 13.01 ?  113 TYR   B CZ   1 
ATOM   5757 O  OH   . TYR   B 1 113 ? 37.395 -26.625 -2.726  1.00 13.63 ?  113 TYR   B OH   1 
ATOM   5758 H  H    . TYR   B 1 113 ? 34.074 -21.776 0.687   1.00 14.61 ?  113 TYR   B H    1 
ATOM   5759 H  HA   . TYR   B 1 113 ? 35.366 -21.077 -1.475  1.00 14.17 ?  113 TYR   B HA   1 
ATOM   5760 H  HB2  . TYR   B 1 113 ? 33.132 -22.670 -1.066  1.00 14.63 ?  113 TYR   B HB2  1 
ATOM   5761 H  HB3  . TYR   B 1 113 ? 33.370 -22.133 -2.540  1.00 14.63 ?  113 TYR   B HB3  1 
ATOM   5762 H  HD1  . TYR   B 1 113 ? 35.849 -22.609 -3.403  1.00 15.63 ?  113 TYR   B HD1  1 
ATOM   5763 H  HD2  . TYR   B 1 113 ? 33.987 -24.786 -0.618  1.00 15.34 ?  113 TYR   B HD2  1 
ATOM   5764 H  HE1  . TYR   B 1 113 ? 37.301 -24.345 -3.814  1.00 15.60 ?  113 TYR   B HE1  1 
ATOM   5765 H  HE2  . TYR   B 1 113 ? 35.442 -26.542 -1.023  1.00 15.57 ?  113 TYR   B HE2  1 
ATOM   5766 H  HH   . TYR   B 1 113 ? 37.222 -27.298 -2.252  1.00 16.40 ?  113 TYR   B HH   1 
ATOM   5767 N  N    . GLU   B 1 114 ? 32.834 -19.271 -0.874  1.00 11.77 ?  114 GLU   B N    1 
ATOM   5768 C  CA   . GLU   B 1 114 ? 32.149 -18.063 -1.329  1.00 11.90 ?  114 GLU   B CA   1 
ATOM   5769 C  C    . GLU   B 1 114 ? 33.132 -16.940 -1.629  1.00 11.74 ?  114 GLU   B C    1 
ATOM   5770 O  O    . GLU   B 1 114 ? 32.859 -16.087 -2.475  1.00 11.81 ?  114 GLU   B O    1 
ATOM   5771 C  CB   . GLU   B 1 114 ? 31.095 -17.638 -0.305  1.00 12.40 ?  114 GLU   B CB   1 
ATOM   5772 C  CG   . GLU   B 1 114 ? 29.876 -18.555 -0.379  1.00 12.32 ?  114 GLU   B CG   1 
ATOM   5773 C  CD   . GLU   B 1 114 ? 28.851 -18.373 0.732   1.00 12.98 ?  114 GLU   B CD   1 
ATOM   5774 O  OE1  . GLU   B 1 114 ? 29.148 -17.751 1.772   1.00 13.07 ?  114 GLU   B OE1  1 
ATOM   5775 O  OE2  . GLU   B 1 114 ? 27.730 -18.917 0.570   1.00 13.56 -1 114 GLU   B OE2  1 
ATOM   5776 H  H    . GLU   B 1 114 ? 32.584 -19.562 -0.100  1.00 14.18 ?  114 GLU   B H    1 
ATOM   5777 H  HA   . GLU   B 1 114 ? 31.686 -18.266 -2.151  1.00 14.33 ?  114 GLU   B HA   1 
ATOM   5778 H  HB2  . GLU   B 1 114 ? 31.469 -17.700 0.591   1.00 14.93 ?  114 GLU   B HB2  1 
ATOM   5779 H  HB3  . GLU   B 1 114 ? 30.810 -16.734 -0.490  1.00 14.93 ?  114 GLU   B HB3  1 
ATOM   5780 H  HG2  . GLU   B 1 114 ? 29.430 -18.395 -1.220  1.00 14.83 ?  114 GLU   B HG2  1 
ATOM   5781 H  HG3  . GLU   B 1 114 ? 30.187 -19.474 -0.342  1.00 14.83 ?  114 GLU   B HG3  1 
ATOM   5782 N  N    . ASN   B 1 115 ? 34.297 -16.935 -0.979  1.00 11.49 ?  115 ASN   B N    1 
ATOM   5783 C  CA   . ASN   B 1 115 ? 35.287 -15.899 -1.279  1.00 11.24 ?  115 ASN   B CA   1 
ATOM   5784 C  C    . ASN   B 1 115 ? 35.699 -15.920 -2.745  1.00 11.15 ?  115 ASN   B C    1 
ATOM   5785 O  O    . ASN   B 1 115 ? 36.088 -14.883 -3.301  1.00 11.71 ?  115 ASN   B O    1 
ATOM   5786 C  CB   . ASN   B 1 115 ? 36.527 -16.071 -0.396  1.00 11.90 ?  115 ASN   B CB   1 
ATOM   5787 C  CG   . ASN   B 1 115 ? 36.260 -15.810 1.067   1.00 12.36 ?  115 ASN   B CG   1 
ATOM   5788 O  OD1  . ASN   B 1 115 ? 36.260 -14.663 1.509   1.00 14.26 ?  115 ASN   B OD1  1 
ATOM   5789 N  ND2  . ASN   B 1 115 ? 36.092 -16.875 1.844   1.00 12.56 ?  115 ASN   B ND2  1 
ATOM   5790 H  H    . ASN   B 1 115 ? 34.536 -17.498 -0.368  1.00 13.84 ?  115 ASN   B H    1 
ATOM   5791 H  HA   . ASN   B 1 115 ? 34.907 -15.029 -1.087  1.00 13.54 ?  115 ASN   B HA   1 
ATOM   5792 H  HB2  . ASN   B 1 115 ? 36.856 -16.980 -0.486  1.00 14.33 ?  115 ASN   B HB2  1 
ATOM   5793 H  HB3  . ASN   B 1 115 ? 37.211 -15.445 -0.687  1.00 14.33 ?  115 ASN   B HB3  1 
ATOM   5794 H  HD21 . ASN   B 1 115 ? 35.949 -16.773 2.687   1.00 15.12 ?  115 ASN   B HD21 1 
ATOM   5795 H  HD22 . ASN   B 1 115 ? 36.113 -17.664 1.505   1.00 15.12 ?  115 ASN   B HD22 1 
ATOM   5796 N  N    . PHE   B 1 116 ? 35.670 -17.097 -3.381  1.00 10.87 ?  116 PHE   B N    1 
ATOM   5797 C  CA   . PHE   B 1 116 ? 36.103 -17.190 -4.770  1.00 11.42 ?  116 PHE   B CA   1 
ATOM   5798 C  C    . PHE   B 1 116 ? 35.198 -16.369 -5.683  1.00 11.06 ?  116 PHE   B C    1 
ATOM   5799 O  O    . PHE   B 1 116 ? 35.628 -15.944 -6.760  1.00 11.67 ?  116 PHE   B O    1 
ATOM   5800 C  CB   . PHE   B 1 116 ? 36.065 -18.638 -5.289  1.00 10.90 ?  116 PHE   B CB   1 
ATOM   5801 C  CG   . PHE   B 1 116 ? 37.136 -19.592 -4.742  1.00 10.80 ?  116 PHE   B CG   1 
ATOM   5802 C  CD1  . PHE   B 1 116 ? 37.791 -19.408 -3.536  1.00 11.69 ?  116 PHE   B CD1  1 
ATOM   5803 C  CD2  . PHE   B 1 116 ? 37.439 -20.726 -5.478  1.00 11.29 ?  116 PHE   B CD2  1 
ATOM   5804 C  CE1  . PHE   B 1 116 ? 38.725 -20.348 -3.086  1.00 11.68 ?  116 PHE   B CE1  1 
ATOM   5805 C  CE2  . PHE   B 1 116 ? 38.366 -21.663 -5.032  1.00 11.51 ?  116 PHE   B CE2  1 
ATOM   5806 C  CZ   . PHE   B 1 116 ? 39.007 -21.473 -3.842  1.00 11.40 ?  116 PHE   B CZ   1 
ATOM   5807 H  H    . PHE   B 1 116 ? 35.406 -17.844 -3.034  1.00 13.09 ?  116 PHE   B H    1 
ATOM   5808 H  HA   . PHE   B 1 116 ? 37.010 -16.861 -4.850  1.00 13.75 ?  116 PHE   B HA   1 
ATOM   5809 H  HB2  . PHE   B 1 116 ? 35.194 -19.015 -5.063  1.00 13.13 ?  116 PHE   B HB2  1 
ATOM   5810 H  HB3  . PHE   B 1 116 ? 36.157 -18.616 -6.253  1.00 13.13 ?  116 PHE   B HB3  1 
ATOM   5811 H  HD1  . PHE   B 1 116 ? 37.591 -18.660 -3.018  1.00 14.07 ?  116 PHE   B HD1  1 
ATOM   5812 H  HD2  . PHE   B 1 116 ? 36.996 -20.877 -6.284  1.00 13.59 ?  116 PHE   B HD2  1 
ATOM   5813 H  HE1  . PHE   B 1 116 ? 39.161 -20.208 -2.277  1.00 14.06 ?  116 PHE   B HE1  1 
ATOM   5814 H  HE2  . PHE   B 1 116 ? 38.554 -22.412 -5.546  1.00 13.86 ?  116 PHE   B HE2  1 
ATOM   5815 H  HZ   . PHE   B 1 116 ? 39.639 -22.085 -3.546  1.00 13.73 ?  116 PHE   B HZ   1 
ATOM   5816 N  N    . ASN   B 1 117 ? 33.932 -16.166 -5.292  1.00 11.42 ?  117 ASN   B N    1 
ATOM   5817 C  CA   . ASN   B 1 117 ? 32.984 -15.461 -6.155  1.00 11.85 ?  117 ASN   B CA   1 
ATOM   5818 C  C    . ASN   B 1 117 ? 33.296 -13.981 -6.307  1.00 12.18 ?  117 ASN   B C    1 
ATOM   5819 O  O    . ASN   B 1 117 ? 32.698 -13.326 -7.166  1.00 13.35 ?  117 ASN   B O    1 
ATOM   5820 C  CB   . ASN   B 1 117 ? 31.558 -15.685 -5.663  1.00 11.91 ?  117 ASN   B CB   1 
ATOM   5821 C  CG   . ASN   B 1 117 ? 31.111 -17.095 -5.921  1.00 12.13 ?  117 ASN   B CG   1 
ATOM   5822 O  OD1  . ASN   B 1 117 ? 31.470 -17.681 -6.943  1.00 13.04 ?  117 ASN   B OD1  1 
ATOM   5823 N  ND2  . ASN   B 1 117 ? 30.372 -17.673 -4.988  1.00 12.29 ?  117 ASN   B ND2  1 
ATOM   5824 H  H    . ASN   B 1 117 ? 33.610 -16.422 -4.530  1.00 13.75 ?  117 ASN   B H    1 
ATOM   5825 H  HA   . ASN   B 1 117 ? 33.046 -15.857 -7.031  1.00 14.27 ?  117 ASN   B HA   1 
ATOM   5826 H  HB2  . ASN   B 1 117 ? 31.517 -15.524 -4.703  1.00 14.34 ?  117 ASN   B HB2  1 
ATOM   5827 H  HB3  . ASN   B 1 117 ? 30.964 -15.074 -6.126  1.00 14.34 ?  117 ASN   B HB3  1 
ATOM   5828 H  HD21 . ASN   B 1 117 ? 30.093 -18.479 -5.097  1.00 14.79 ?  117 ASN   B HD21 1 
ATOM   5829 H  HD22 . ASN   B 1 117 ? 30.149 -17.234 -4.281  1.00 14.79 ?  117 ASN   B HD22 1 
ATOM   5830 N  N    . GLN   B 1 118 ? 34.232 -13.455 -5.526  1.00 11.78 ?  118 GLN   B N    1 
ATOM   5831 C  CA   . GLN   B 1 118 ? 34.668 -12.070 -5.662  1.00 12.38 ?  118 GLN   B CA   1 
ATOM   5832 C  C    . GLN   B 1 118 ? 35.735 -11.881 -6.735  1.00 12.40 ?  118 GLN   B C    1 
ATOM   5833 O  O    . GLN   B 1 118 ? 36.199 -10.753 -6.923  1.00 13.92 ?  118 GLN   B O    1 
ATOM   5834 C  CB   . GLN   B 1 118 ? 35.145 -11.538 -4.307  1.00 13.02 ?  118 GLN   B CB   1 
ATOM   5835 C  CG   . GLN   B 1 118 ? 34.057 -11.577 -3.239  1.00 13.13 ?  118 GLN   B CG   1 
ATOM   5836 C  CD   . GLN   B 1 118 ? 32.885 -10.675 -3.576  1.00 13.16 ?  118 GLN   B CD   1 
ATOM   5837 O  OE1  . GLN   B 1 118 ? 33.069 -9.536  -4.020  1.00 13.88 ?  118 GLN   B OE1  1 
ATOM   5838 N  NE2  . GLN   B 1 118 ? 31.673 -11.175 -3.378  1.00 13.49 ?  118 GLN   B NE2  1 
ATOM   5839 H  H    . GLN   B 1 118 ? 34.646 -13.884 -4.902  1.00 14.19 ?  118 GLN   B H    1 
ATOM   5840 H  HA   . GLN   B 1 118 ? 33.905 -11.540 -5.933  1.00 14.90 ?  118 GLN   B HA   1 
ATOM   5841 H  HB2  . GLN   B 1 118 ? 35.888 -12.070 -3.997  1.00 15.67 ?  118 GLN   B HB2  1 
ATOM   5842 H  HB3  . GLN   B 1 118 ? 35.420 -10.610 -4.412  1.00 15.67 ?  118 GLN   B HB3  1 
ATOM   5843 H  HG2  . GLN   B 1 118 ? 33.726 -12.485 -3.157  1.00 15.81 ?  118 GLN   B HG2  1 
ATOM   5844 H  HG3  . GLN   B 1 118 ? 34.433 -11.282 -2.393  1.00 15.81 ?  118 GLN   B HG3  1 
ATOM   5845 H  HE21 . GLN   B 1 118 ? 31.585 -11.973 -3.065  1.00 16.23 ?  118 GLN   B HE21 1 
ATOM   5846 H  HE22 . GLN   B 1 118 ? 30.982 -10.702 -3.555  1.00 16.23 ?  118 GLN   B HE22 1 
ATOM   5847 N  N    . HIS   B 1 119 ? 36.083 -12.936 -7.473  1.00 11.77 ?  119 HIS   B N    1 
ATOM   5848 C  CA   . HIS   B 1 119 ? 37.122 -12.885 -8.492  1.00 12.17 ?  119 HIS   B CA   1 
ATOM   5849 C  C    . HIS   B 1 119 ? 36.646 -13.617 -9.731  1.00 12.02 ?  119 HIS   B C    1 
ATOM   5850 O  O    . HIS   B 1 119 ? 36.142 -14.734 -9.632  1.00 12.93 ?  119 HIS   B O    1 
ATOM   5851 C  CB   . HIS   B 1 119 ? 38.405 -13.512 -7.944  1.00 12.82 ?  119 HIS   B CB   1 
ATOM   5852 C  CG   . HIS   B 1 119 ? 38.879 -12.822 -6.710  1.00 13.90 ?  119 HIS   B CG   1 
ATOM   5853 N  ND1  . HIS   B 1 119 ? 39.678 -11.699 -6.752  1.00 15.46 ?  119 HIS   B ND1  1 
ATOM   5854 C  CD2  . HIS   B 1 119 ? 38.580 -13.027 -5.407  1.00 15.15 ?  119 HIS   B CD2  1 
ATOM   5855 C  CE1  . HIS   B 1 119 ? 39.881 -11.269 -5.520  1.00 16.56 ?  119 HIS   B CE1  1 
ATOM   5856 N  NE2  . HIS   B 1 119 ? 39.217 -12.049 -4.686  1.00 16.51 ?  119 HIS   B NE2  1 
ATOM   5857 H  H    . HIS   B 1 119 ? 35.710 -13.714 -7.408  1.00 14.17 ?  119 HIS   B H    1 
ATOM   5858 H  HA   . HIS   B 1 119 ? 37.300 -11.960 -8.727  1.00 14.65 ?  119 HIS   B HA   1 
ATOM   5859 H  HB2  . HIS   B 1 119 ? 38.241 -14.440 -7.733  1.00 15.44 ?  119 HIS   B HB2  1 
ATOM   5860 H  HB3  . HIS   B 1 119 ? 39.103 -13.438 -8.618  1.00 15.44 ?  119 HIS   B HB3  1 
ATOM   5861 H  HD2  . HIS   B 1 119 ? 38.045 -13.710 -5.065  1.00 18.23 ?  119 HIS   B HD2  1 
ATOM   5862 H  HE1  . HIS   B 1 119 ? 40.407 -10.542 -5.274  1.00 19.92 ?  119 HIS   B HE1  1 
ATOM   5863 H  HE2  . HIS   B 1 119 ? 39.216 -11.982 -3.826  1.00 19.86 ?  119 HIS   B HE2  1 
ATOM   5864 N  N    . GLU   B 1 120 ? 36.797 -12.997 -10.900 1.00 12.61 ?  120 GLU   B N    1 
ATOM   5865 C  CA   . GLU   B 1 120 ? 36.208 -13.580 -12.101 1.00 14.22 ?  120 GLU   B CA   1 
ATOM   5866 C  C    . GLU   B 1 120 ? 36.886 -14.878 -12.519 1.00 13.04 ?  120 GLU   B C    1 
ATOM   5867 O  O    . GLU   B 1 120 ? 36.226 -15.752 -13.093 1.00 13.40 ?  120 GLU   B O    1 
ATOM   5868 C  CB   . GLU   B 1 120 ? 36.219 -12.571 -13.246 1.00 19.58 ?  120 GLU   B CB   1 
ATOM   5869 C  CG   . GLU   B 1 120 ? 35.249 -11.422 -13.036 1.00 25.83 ?  120 GLU   B CG   1 
ATOM   5870 C  CD   . GLU   B 1 120 ? 35.127 -10.523 -14.250 1.00 32.10 ?  120 GLU   B CD   1 
ATOM   5871 O  OE1  . GLU   B 1 120 ? 36.126 -10.373 -14.986 1.00 34.49 ?  120 GLU   B OE1  1 
ATOM   5872 O  OE2  . GLU   B 1 120 ? 34.028 -9.970  -14.468 1.00 35.16 -1 120 GLU   B OE2  1 
ATOM   5873 H  H    . GLU   B 1 120 ? 37.215 -12.250 -11.023 1.00 15.18 ?  120 GLU   B H    1 
ATOM   5874 H  HA   . GLU   B 1 120 ? 35.285 -13.789 -11.915 1.00 17.12 ?  120 GLU   B HA   1 
ATOM   5875 H  HB2  . GLU   B 1 120 ? 37.105 -12.191 -13.336 1.00 23.55 ?  120 GLU   B HB2  1 
ATOM   5876 H  HB3  . GLU   B 1 120 ? 35.965 -13.018 -14.070 1.00 23.55 ?  120 GLU   B HB3  1 
ATOM   5877 H  HG2  . GLU   B 1 120 ? 34.366 -11.778 -12.846 1.00 31.04 ?  120 GLU   B HG2  1 
ATOM   5878 H  HG3  . GLU   B 1 120 ? 35.553 -10.877 -12.295 1.00 31.04 ?  120 GLU   B HG3  1 
ATOM   5879 N  N    . VAL   B 1 121 ? 38.185 -15.017 -12.259 1.00 12.62 ?  121 VAL   B N    1 
ATOM   5880 C  CA   . VAL   B 1 121 ? 38.930 -16.225 -12.607 1.00 12.24 ?  121 VAL   B CA   1 
ATOM   5881 C  C    . VAL   B 1 121 ? 40.044 -16.430 -11.589 1.00 11.89 ?  121 VAL   B C    1 
ATOM   5882 O  O    . VAL   B 1 121 ? 40.719 -15.474 -11.195 1.00 12.69 ?  121 VAL   B O    1 
ATOM   5883 C  CB   . VAL   B 1 121 ? 39.440 -16.174 -14.066 1.00 14.45 ?  121 VAL   B CB   1 
ATOM   5884 C  CG1  . VAL   B 1 121 ? 40.314 -14.947 -14.313 1.00 15.64 ?  121 VAL   B CG1  1 
ATOM   5885 C  CG2  . VAL   B 1 121 ? 40.168 -17.460 -14.426 1.00 15.96 ?  121 VAL   B CG2  1 
ATOM   5886 H  H    . VAL   B 1 121 ? 38.671 -14.413 -11.879 1.00 15.19 ?  121 VAL   B H    1 
ATOM   5887 H  HA   . VAL   B 1 121 ? 38.323 -16.978 -12.541 1.00 14.74 ?  121 VAL   B HA   1 
ATOM   5888 H  HB   . VAL   B 1 121 ? 38.670 -16.106 -14.658 1.00 17.38 ?  121 VAL   B HB   1 
ATOM   5889 H  HG11 . VAL   B 1 121 ? 40.618 -14.956 -15.234 1.00 18.82 ?  121 VAL   B HG11 1 
ATOM   5890 H  HG12 . VAL   B 1 121 ? 39.790 -14.148 -14.146 1.00 18.82 ?  121 VAL   B HG12 1 
ATOM   5891 H  HG13 . VAL   B 1 121 ? 41.074 -14.976 -13.713 1.00 18.82 ?  121 VAL   B HG13 1 
ATOM   5892 H  HG21 . VAL   B 1 121 ? 40.370 -17.454 -15.377 1.00 19.20 ?  121 VAL   B HG21 1 
ATOM   5893 H  HG22 . VAL   B 1 121 ? 40.992 -17.512 -13.917 1.00 19.20 ?  121 VAL   B HG22 1 
ATOM   5894 H  HG23 . VAL   B 1 121 ? 39.600 -18.217 -14.217 1.00 19.20 ?  121 VAL   B HG23 1 
ATOM   5895 N  N    . LEU   B 1 122 ? 40.225 -17.684 -11.155 1.00 11.50 ?  122 LEU   B N    1 
ATOM   5896 C  CA   . LEU   B 1 122 ? 41.206 -18.040 -10.133 1.00 11.01 ?  122 LEU   B CA   1 
ATOM   5897 C  C    . LEU   B 1 122 ? 41.859 -19.372 -10.462 1.00 11.05 ?  122 LEU   B C    1 
ATOM   5898 O  O    . LEU   B 1 122 ? 41.200 -20.294 -10.961 1.00 12.45 ?  122 LEU   B O    1 
ATOM   5899 C  CB   . LEU   B 1 122 ? 40.558 -18.266 -8.756  1.00 12.96 ?  122 LEU   B CB   1 
ATOM   5900 C  CG   . LEU   B 1 122 ? 39.526 -17.248 -8.268  1.00 13.04 ?  122 LEU   B CG   1 
ATOM   5901 C  CD1  . LEU   B 1 122 ? 38.127 -17.595 -8.746  1.00 14.09 ?  122 LEU   B CD1  1 
ATOM   5902 C  CD2  . LEU   B 1 122 ? 39.573 -17.139 -6.757  1.00 12.69 ?  122 LEU   B CD2  1 
ATOM   5903 H  H    . LEU   B 1 122 ? 39.780 -18.363 -11.451 1.00 13.85 ?  122 LEU   B H    1 
ATOM   5904 H  HA   . LEU   B 1 122 ? 41.884 -17.349 -10.063 1.00 13.26 ?  122 LEU   B HA   1 
ATOM   5905 H  HB2  . LEU   B 1 122 ? 40.114 -19.125 -8.772  1.00 15.60 ?  122 LEU   B HB2  1 
ATOM   5906 H  HB3  . LEU   B 1 122 ? 41.265 -18.284 -8.094  1.00 15.60 ?  122 LEU   B HB3  1 
ATOM   5907 H  HG   . LEU   B 1 122 ? 39.752 -16.376 -8.628  1.00 15.69 ?  122 LEU   B HG   1 
ATOM   5908 H  HD11 . LEU   B 1 122 ? 37.500 -16.953 -8.374  1.00 16.96 ?  122 LEU   B HD11 1 
ATOM   5909 H  HD12 . LEU   B 1 122 ? 38.105 -17.551 -9.715  1.00 16.96 ?  122 LEU   B HD12 1 
ATOM   5910 H  HD13 . LEU   B 1 122 ? 37.903 -18.487 -8.447  1.00 16.96 ?  122 LEU   B HD13 1 
ATOM   5911 H  HD21 . LEU   B 1 122 ? 38.891 -16.517 -6.460  1.00 15.28 ?  122 LEU   B HD21 1 
ATOM   5912 H  HD22 . LEU   B 1 122 ? 39.413 -18.015 -6.371  1.00 15.28 ?  122 LEU   B HD22 1 
ATOM   5913 H  HD23 . LEU   B 1 122 ? 40.451 -16.818 -6.490  1.00 15.28 ?  122 LEU   B HD23 1 
ATOM   5914 N  N    . LEU   B 1 123 ? 43.144 -19.482 -10.103 1.00 10.69 ?  123 LEU   B N    1 
ATOM   5915 C  CA   . LEU   B 1 123 ? 43.859 -20.749 -9.987  1.00 10.93 ?  123 LEU   B CA   1 
ATOM   5916 C  C    . LEU   B 1 123 ? 43.829 -21.142 -8.516  1.00 10.75 ?  123 LEU   B C    1 
ATOM   5917 O  O    . LEU   B 1 123 ? 44.180 -20.320 -7.661  1.00 11.09 ?  123 LEU   B O    1 
ATOM   5918 C  CB   . LEU   B 1 123 ? 45.307 -20.569 -10.453 1.00 11.37 ?  123 LEU   B CB   1 
ATOM   5919 C  CG   . LEU   B 1 123 ? 46.249 -21.750 -10.202 1.00 11.89 ?  123 LEU   B CG   1 
ATOM   5920 C  CD1  . LEU   B 1 123 ? 45.835 -23.001 -10.972 1.00 12.40 ?  123 LEU   B CD1  1 
ATOM   5921 C  CD2  . LEU   B 1 123 ? 47.664 -21.352 -10.572 1.00 12.71 ?  123 LEU   B CD2  1 
ATOM   5922 H  H    . LEU   B 1 123 ? 43.640 -18.802 -9.903  1.00 12.87 ?  123 LEU   B H    1 
ATOM   5923 H  HA   . LEU   B 1 123 ? 43.418 -21.436 -10.515 1.00 13.16 ?  123 LEU   B HA   1 
ATOM   5924 H  HB2  . LEU   B 1 123 ? 45.292 -20.410 -11.409 1.00 13.69 ?  123 LEU   B HB2  1 
ATOM   5925 H  HB3  . LEU   B 1 123 ? 45.675 -19.801 -9.999  1.00 13.69 ?  123 LEU   B HB3  1 
ATOM   5926 H  HG   . LEU   B 1 123 ? 46.242 -21.967 -9.257  1.00 14.31 ?  123 LEU   B HG   1 
ATOM   5927 H  HD11 . LEU   B 1 123 ? 46.473 -23.707 -10.785 1.00 14.92 ?  123 LEU   B HD11 1 
ATOM   5928 H  HD12 . LEU   B 1 123 ? 44.950 -23.269 -10.683 1.00 14.92 ?  123 LEU   B HD12 1 
ATOM   5929 H  HD13 . LEU   B 1 123 ? 45.830 -22.798 -11.919 1.00 14.92 ?  123 LEU   B HD13 1 
ATOM   5930 H  HD21 . LEU   B 1 123 ? 48.256 -22.103 -10.412 1.00 15.30 ?  123 LEU   B HD21 1 
ATOM   5931 H  HD22 . LEU   B 1 123 ? 47.687 -21.106 -11.511 1.00 15.30 ?  123 LEU   B HD22 1 
ATOM   5932 H  HD23 . LEU   B 1 123 ? 47.932 -20.596 -10.027 1.00 15.30 ?  123 LEU   B HD23 1 
ATOM   5933 N  N    . ALA   B 1 124 ? 43.389 -22.369 -8.209  1.00 10.74 ?  124 ALA   B N    1 
ATOM   5934 C  CA   . ALA   B 1 124 ? 43.144 -22.694 -6.811  1.00 10.91 ?  124 ALA   B CA   1 
ATOM   5935 C  C    . ALA   B 1 124 ? 43.414 -24.157 -6.480  1.00 10.36 ?  124 ALA   B C    1 
ATOM   5936 O  O    . ALA   B 1 124 ? 43.278 -25.032 -7.346  1.00 11.22 ?  124 ALA   B O    1 
ATOM   5937 C  CB   . ALA   B 1 124 ? 41.690 -22.375 -6.432  1.00 11.57 ?  124 ALA   B CB   1 
ATOM   5938 H  H    . ALA   B 1 124 ? 43.219 -23.005 -8.769  1.00 12.93 ?  124 ALA   B H    1 
ATOM   5939 H  HA   . ALA   B 1 124 ? 43.720 -22.145 -6.266  1.00 13.14 ?  124 ALA   B HA   1 
ATOM   5940 H  HB1  . ALA   B 1 124 ? 41.542 -22.593 -5.499  1.00 13.93 ?  124 ALA   B HB1  1 
ATOM   5941 H  HB2  . ALA   B 1 124 ? 41.529 -21.422 -6.573  1.00 13.93 ?  124 ALA   B HB2  1 
ATOM   5942 H  HB3  . ALA   B 1 124 ? 41.089 -22.890 -6.992  1.00 13.93 ?  124 ALA   B HB3  1 
ATOM   5943 N  N    . PRO   B 1 125 ? 43.722 -24.449 -5.218  1.00 10.69 ?  125 PRO   B N    1 
ATOM   5944 C  CA   . PRO   B 1 125 ? 43.656 -25.814 -4.694  1.00 11.43 ?  125 PRO   B CA   1 
ATOM   5945 C  C    . PRO   B 1 125 ? 42.254 -26.086 -4.150  1.00 11.51 ?  125 PRO   B C    1 
ATOM   5946 O  O    . PRO   B 1 125 ? 41.457 -25.168 -3.946  1.00 12.18 ?  125 PRO   B O    1 
ATOM   5947 C  CB   . PRO   B 1 125 ? 44.636 -25.740 -3.520  1.00 12.58 ?  125 PRO   B CB   1 
ATOM   5948 C  CG   . PRO   B 1 125 ? 44.401 -24.349 -2.958  1.00 12.61 ?  125 PRO   B CG   1 
ATOM   5949 C  CD   . PRO   B 1 125 ? 44.051 -23.480 -4.158  1.00 11.44 ?  125 PRO   B CD   1 
ATOM   5950 H  HA   . PRO   B 1 125 ? 43.929 -26.484 -5.339  1.00 13.77 ?  125 PRO   B HA   1 
ATOM   5951 H  HB2  . PRO   B 1 125 ? 44.420 -26.418 -2.857  1.00 15.15 ?  125 PRO   B HB2  1 
ATOM   5952 H  HB3  . PRO   B 1 125 ? 45.546 -25.839 -3.834  1.00 15.15 ?  125 PRO   B HB3  1 
ATOM   5953 H  HG2  . PRO   B 1 125 ? 43.666 -24.362 -2.326  1.00 15.18 ?  125 PRO   B HG2  1 
ATOM   5954 H  HG3  . PRO   B 1 125 ? 45.212 -24.023 -2.527  1.00 15.18 ?  125 PRO   B HG3  1 
ATOM   5955 H  HD2  . PRO   B 1 125 ? 43.288 -22.918 -3.965  1.00 13.77 ?  125 PRO   B HD2  1 
ATOM   5956 H  HD3  . PRO   B 1 125 ? 44.824 -22.944 -4.423  1.00 13.77 ?  125 PRO   B HD3  1 
ATOM   5957 N  N    . LEU   B 1 126 ? 41.985 -27.365 -3.868  1.00 12.25 ?  126 LEU   B N    1 
ATOM   5958 C  CA   . LEU   B 1 126 ? 40.766 -27.732 -3.152  1.00 12.76 ?  126 LEU   B CA   1 
ATOM   5959 C  C    . LEU   B 1 126 ? 40.881 -27.330 -1.689  1.00 13.03 ?  126 LEU   B C    1 
ATOM   5960 O  O    . LEU   B 1 126 ? 41.772 -27.790 -0.970  1.00 14.82 ?  126 LEU   B O    1 
ATOM   5961 C  CB   . LEU   B 1 126 ? 40.518 -29.230 -3.266  1.00 13.99 ?  126 LEU   B CB   1 
ATOM   5962 C  CG   . LEU   B 1 126 ? 39.990 -29.713 -4.616  1.00 15.02 ?  126 LEU   B CG   1 
ATOM   5963 C  CD1  . LEU   B 1 126 ? 40.022 -31.220 -4.691  1.00 17.00 ?  126 LEU   B CD1  1 
ATOM   5964 C  CD2  . LEU   B 1 126 ? 38.576 -29.208 -4.861  1.00 15.40 ?  126 LEU   B CD2  1 
ATOM   5965 H  H    . LEU   B 1 126 ? 42.492 -28.029 -4.070  1.00 14.75 ?  126 LEU   B H    1 
ATOM   5966 H  HA   . LEU   B 1 126 ? 40.014 -27.260 -3.541  1.00 15.37 ?  126 LEU   B HA   1 
ATOM   5967 H  HB2  . LEU   B 1 126 ? 41.354 -29.689 -3.099  1.00 16.83 ?  126 LEU   B HB2  1 
ATOM   5968 H  HB3  . LEU   B 1 126 ? 39.868 -29.480 -2.594  1.00 16.83 ?  126 LEU   B HB3  1 
ATOM   5969 H  HG   . LEU   B 1 126 ? 40.560 -29.364 -5.322  1.00 18.07 ?  126 LEU   B HG   1 
ATOM   5970 H  HD11 . LEU   B 1 126 ? 39.683 -31.501 -5.556  1.00 20.45 ?  126 LEU   B HD11 1 
ATOM   5971 H  HD12 . LEU   B 1 126 ? 40.933 -31.525 -4.575  1.00 20.45 ?  126 LEU   B HD12 1 
ATOM   5972 H  HD13 . LEU   B 1 126 ? 39.459 -31.581 -3.985  1.00 20.45 ?  126 LEU   B HD13 1 
ATOM   5973 H  HD21 . LEU   B 1 126 ? 38.222 -29.633 -5.657  1.00 18.52 ?  126 LEU   B HD21 1 
ATOM   5974 H  HD22 . LEU   B 1 126 ? 38.026 -29.428 -4.094  1.00 18.52 ?  126 LEU   B HD22 1 
ATOM   5975 H  HD23 . LEU   B 1 126 ? 38.599 -28.244 -4.985  1.00 18.52 ?  126 LEU   B HD23 1 
ATOM   5976 N  N    . LEU   B 1 127 ? 39.956 -26.493 -1.234  1.00 13.01 ?  127 LEU   B N    1 
ATOM   5977 C  CA   . LEU   B 1 127 ? 40.011 -26.006 0.132   1.00 13.29 ?  127 LEU   B CA   1 
ATOM   5978 C  C    . LEU   B 1 127 ? 39.738 -27.127 1.126   1.00 13.04 ?  127 LEU   B C    1 
ATOM   5979 O  O    . LEU   B 1 127 ? 38.916 -28.021 0.900   1.00 13.74 ?  127 LEU   B O    1 
ATOM   5980 C  CB   . LEU   B 1 127 ? 38.996 -24.883 0.348   1.00 14.00 ?  127 LEU   B CB   1 
ATOM   5981 C  CG   . LEU   B 1 127 ? 39.175 -23.622 -0.496  1.00 14.56 ?  127 LEU   B CG   1 
ATOM   5982 C  CD1  . LEU   B 1 127 ? 38.055 -22.651 -0.172  1.00 14.58 ?  127 LEU   B CD1  1 
ATOM   5983 C  CD2  . LEU   B 1 127 ? 40.535 -22.974 -0.264  1.00 15.25 ?  127 LEU   B CD2  1 
ATOM   5984 H  H    . LEU   B 1 127 ? 39.293 -26.185 -1.695  1.00 15.66 ?  127 LEU   B H    1 
ATOM   5985 H  HA   . LEU   B 1 127 ? 40.898 -25.648 0.308   1.00 15.99 ?  127 LEU   B HA   1 
ATOM   5986 H  HB2  . LEU   B 1 127 ? 38.112 -25.231 0.157   1.00 16.85 ?  127 LEU   B HB2  1 
ATOM   5987 H  HB3  . LEU   B 1 127 ? 39.037 -24.609 1.279   1.00 16.85 ?  127 LEU   B HB3  1 
ATOM   5988 H  HG   . LEU   B 1 127 ? 39.098 -23.846 -1.433  1.00 17.51 ?  127 LEU   B HG   1 
ATOM   5989 H  HD11 . LEU   B 1 127 ? 38.169 -21.842 -0.701  1.00 17.54 ?  127 LEU   B HD11 1 
ATOM   5990 H  HD12 . LEU   B 1 127 ? 37.202 -23.061 -0.380  1.00 17.54 ?  127 LEU   B HD12 1 
ATOM   5991 H  HD13 . LEU   B 1 127 ? 38.091 -22.426 0.774   1.00 17.54 ?  127 LEU   B HD13 1 
ATOM   5992 H  HD21 . LEU   B 1 127 ? 40.570 -22.126 -0.734  1.00 18.34 ?  127 LEU   B HD21 1 
ATOM   5993 H  HD22 . LEU   B 1 127 ? 40.659 -22.829 0.688   1.00 18.34 ?  127 LEU   B HD22 1 
ATOM   5994 H  HD23 . LEU   B 1 127 ? 41.223 -23.568 -0.600  1.00 18.34 ?  127 LEU   B HD23 1 
ATOM   5995 N  N    . SER   B 1 128 ? 40.420 -27.040 2.258   1.00 13.03 ?  128 SER   B N    1 
ATOM   5996 C  CA   . SER   B 1 128 ? 40.309 -27.957 3.381   1.00 13.71 ?  128 SER   B CA   1 
ATOM   5997 C  C    . SER   B 1 128 ? 40.802 -29.366 3.061   1.00 14.86 ?  128 SER   B C    1 
ATOM   5998 O  O    . SER   B 1 128 ? 40.709 -30.248 3.916   1.00 16.16 ?  128 SER   B O    1 
ATOM   5999 C  CB   . SER   B 1 128 ? 38.908 -27.962 4.013   1.00 14.01 ?  128 SER   B CB   1 
ATOM   6000 O  OG   . SER   B 1 128 ? 38.602 -26.682 4.557   1.00 14.66 ?  128 SER   B OG   1 
ATOM   6001 H  H    . SER   B 1 128 ? 40.988 -26.409 2.405   1.00 15.68 ?  128 SER   B H    1 
ATOM   6002 H  HA   . SER   B 1 128 ? 40.900 -27.622 4.065   1.00 16.50 ?  128 SER   B HA   1 
ATOM   6003 H  HB2  . SER   B 1 128 ? 38.249 -28.199 3.340   1.00 16.86 ?  128 SER   B HB2  1 
ATOM   6004 H  HB3  . SER   B 1 128 ? 38.890 -28.629 4.731   1.00 16.86 ?  128 SER   B HB3  1 
ATOM   6005 H  HG   . SER   B 1 128 ? 39.173 -26.480 5.137   1.00 17.64 ?  128 SER   B HG   1 
ATOM   6006 N  N    . ALA   B 1 129 ? 41.369 -29.593 1.874   1.00 15.87 ?  129 ALA   B N    1 
ATOM   6007 C  CA   . ALA   B 1 129 ? 41.915 -30.893 1.519   1.00 16.73 ?  129 ALA   B CA   1 
ATOM   6008 C  C    . ALA   B 1 129 ? 43.309 -31.066 2.113   1.00 16.19 ?  129 ALA   B C    1 
ATOM   6009 O  O    . ALA   B 1 129 ? 43.864 -30.167 2.762   1.00 15.59 ?  129 ALA   B O    1 
ATOM   6010 C  CB   . ALA   B 1 129 ? 41.962 -31.054 0.002   1.00 18.89 ?  129 ALA   B CB   1 
ATOM   6011 H  H    . ALA   B 1 129 ? 41.448 -29.003 1.248   1.00 19.09 ?  129 ALA   B H    1 
ATOM   6012 H  HA   . ALA   B 1 129 ? 41.345 -31.586 1.877   1.00 20.12 ?  129 ALA   B HA   1 
ATOM   6013 H  HB1  . ALA   B 1 129 ? 42.317 -31.932 -0.212  1.00 22.71 ?  129 ALA   B HB1  1 
ATOM   6014 H  HB2  . ALA   B 1 129 ? 41.064 -30.967 -0.350  1.00 22.71 ?  129 ALA   B HB2  1 
ATOM   6015 H  HB3  . ALA   B 1 129 ? 42.534 -30.366 -0.373  1.00 22.71 ?  129 ALA   B HB3  1 
ATOM   6016 N  N    . GLY   B 1 130 ? 43.881 -32.244 1.868   1.00 15.90 ?  130 GLY   B N    1 
ATOM   6017 C  CA   . GLY   B 1 130 ? 45.268 -32.478 2.218   1.00 16.54 ?  130 GLY   B CA   1 
ATOM   6018 C  C    . GLY   B 1 130 ? 45.485 -32.389 3.710   1.00 16.53 ?  130 GLY   B C    1 
ATOM   6019 O  O    . GLY   B 1 130 ? 44.791 -33.033 4.509   1.00 17.44 ?  130 GLY   B O    1 
ATOM   6020 H  H    . GLY   B 1 130 ? 43.492 -32.915 1.491   1.00 19.12 ?  130 GLY   B H    1 
ATOM   6021 H  HA2  . GLY   B 1 130 ? 45.539 -33.362 1.917   1.00 19.90 ?  130 GLY   B HA2  1 
ATOM   6022 H  HA3  . GLY   B 1 130 ? 45.833 -31.820 1.780   1.00 19.90 ?  130 GLY   B HA3  1 
ATOM   6023 N  N    . ILE   B 1 131 ? 46.463 -31.563 4.095   1.00 16.92 ?  131 ILE   B N    1 
ATOM   6024 C  CA   . ILE   B 1 131 ? 46.829 -31.433 5.498   1.00 17.56 ?  131 ILE   B CA   1 
ATOM   6025 C  C    . ILE   B 1 131 ? 45.714 -30.836 6.337   1.00 16.57 ?  131 ILE   B C    1 
ATOM   6026 O  O    . ILE   B 1 131 ? 45.786 -30.907 7.567   1.00 17.88 ?  131 ILE   B O    1 
ATOM   6027 C  CB   . ILE   B 1 131 ? 48.151 -30.656 5.695   1.00 19.51 ?  131 ILE   B CB   1 
ATOM   6028 C  CG1  . ILE   B 1 131 ? 47.977 -29.168 5.356   1.00 20.50 ?  131 ILE   B CG1  1 
ATOM   6029 C  CG2  . ILE   B 1 131 ? 49.267 -31.273 4.852   1.00 20.64 ?  131 ILE   B CG2  1 
ATOM   6030 C  CD1  . ILE   B 1 131 ? 49.185 -28.304 5.700   1.00 21.47 ?  131 ILE   B CD1  1 
ATOM   6031 H  H    . ILE   B 1 131 ? 46.924 -31.067 3.564   1.00 20.35 ?  131 ILE   B H    1 
ATOM   6032 H  HA   . ILE   B 1 131 ? 46.977 -32.324 5.843   1.00 21.12 ?  131 ILE   B HA   1 
ATOM   6033 H  HB   . ILE   B 1 131 ? 48.401 -30.725 6.630   1.00 23.46 ?  131 ILE   B HB   1 
ATOM   6034 H  HG12 . ILE   B 1 131 ? 47.810 -29.085 4.404   1.00 24.64 ?  131 ILE   B HG12 1 
ATOM   6035 H  HG13 . ILE   B 1 131 ? 47.218 -28.813 5.850   1.00 24.64 ?  131 ILE   B HG13 1 
ATOM   6036 H  HG21 . ILE   B 1 131 ? 50.108 -30.863 5.101   1.00 24.81 ?  131 ILE   B HG21 1 
ATOM   6037 H  HG22 . ILE   B 1 131 ? 49.294 -32.225 5.020   1.00 24.81 ?  131 ILE   B HG22 1 
ATOM   6038 H  HG23 . ILE   B 1 131 ? 49.078 -31.105 3.915   1.00 24.81 ?  131 ILE   B HG23 1 
ATOM   6039 H  HD11 . ILE   B 1 131 ? 48.962 -27.374 5.538   1.00 25.81 ?  131 ILE   B HD11 1 
ATOM   6040 H  HD12 . ILE   B 1 131 ? 49.406 -28.432 6.636   1.00 25.81 ?  131 ILE   B HD12 1 
ATOM   6041 H  HD13 . ILE   B 1 131 ? 49.931 -28.569 5.143   1.00 25.81 ?  131 ILE   B HD13 1 
ATOM   6042 N  N    . PHE   B 1 132 ? 44.684 -30.254 5.709   1.00 15.73 ?  132 PHE   B N    1 
ATOM   6043 C  CA   . PHE   B 1 132 ? 43.529 -29.752 6.445   1.00 16.09 ?  132 PHE   B CA   1 
ATOM   6044 C  C    . PHE   B 1 132 ? 42.504 -30.840 6.776   1.00 17.63 ?  132 PHE   B C    1 
ATOM   6045 O  O    . PHE   B 1 132 ? 41.604 -30.585 7.580   1.00 19.20 ?  132 PHE   B O    1 
ATOM   6046 C  CB   . PHE   B 1 132 ? 42.844 -28.619 5.668   1.00 15.29 ?  132 PHE   B CB   1 
ATOM   6047 C  CG   . PHE   B 1 132 ? 43.538 -27.276 5.775   1.00 15.10 ?  132 PHE   B CG   1 
ATOM   6048 C  CD1  . PHE   B 1 132 ? 44.826 -27.090 5.297   1.00 16.12 ?  132 PHE   B CD1  1 
ATOM   6049 C  CD2  . PHE   B 1 132 ? 42.864 -26.182 6.303   1.00 14.86 ?  132 PHE   B CD2  1 
ATOM   6050 C  CE1  . PHE   B 1 132 ? 45.442 -25.847 5.382   1.00 16.57 ?  132 PHE   B CE1  1 
ATOM   6051 C  CE2  . PHE   B 1 132 ? 43.467 -24.935 6.384   1.00 15.45 ?  132 PHE   B CE2  1 
ATOM   6052 C  CZ   . PHE   B 1 132 ? 44.755 -24.770 5.925   1.00 16.04 ?  132 PHE   B CZ   1 
ATOM   6053 H  H    . PHE   B 1 132 ? 44.629 -30.150 4.857   1.00 18.92 ?  132 PHE   B H    1 
ATOM   6054 H  HA   . PHE   B 1 132 ? 43.840 -29.382 7.284   1.00 19.36 ?  132 PHE   B HA   1 
ATOM   6055 H  HB2  . PHE   B 1 132 ? 42.825 -28.861 4.730   1.00 18.40 ?  132 PHE   B HB2  1 
ATOM   6056 H  HB3  . PHE   B 1 132 ? 41.941 -28.515 6.001   1.00 18.40 ?  132 PHE   B HB3  1 
ATOM   6057 H  HD1  . PHE   B 1 132 ? 45.292 -27.812 4.936   1.00 19.40 ?  132 PHE   B HD1  1 
ATOM   6058 H  HD2  . PHE   B 1 132 ? 41.994 -26.288 6.617   1.00 17.88 ?  132 PHE   B HD2  1 
ATOM   6059 H  HE1  . PHE   B 1 132 ? 46.311 -25.735 5.071   1.00 19.93 ?  132 PHE   B HE1  1 
ATOM   6060 H  HE2  . PHE   B 1 132 ? 43.006 -24.213 6.754   1.00 18.59 ?  132 PHE   B HE2  1 
ATOM   6061 H  HZ   . PHE   B 1 132 ? 45.165 -23.934 5.984   1.00 19.30 ?  132 PHE   B HZ   1 
ATOM   6062 N  N    . GLY   B 1 133 ? 42.596 -32.031 6.171   1.00 17.26 ?  133 GLY   B N    1 
ATOM   6063 C  CA   . GLY   B 1 133 ? 41.886 -33.199 6.665   1.00 18.20 ?  133 GLY   B CA   1 
ATOM   6064 C  C    . GLY   B 1 133 ? 40.486 -33.459 6.139   1.00 18.60 ?  133 GLY   B C    1 
ATOM   6065 O  O    . GLY   B 1 133 ? 39.896 -34.474 6.518   1.00 20.69 ?  133 GLY   B O    1 
ATOM   6066 H  H    . GLY   B 1 133 ? 43.071 -32.177 5.470   1.00 20.75 ?  133 GLY   B H    1 
ATOM   6067 H  HA2  . GLY   B 1 133 ? 42.418 -33.980 6.463   1.00 21.89 ?  133 GLY   B HA2  1 
ATOM   6068 H  HA3  . GLY   B 1 133 ? 41.821 -33.125 7.628   1.00 21.89 ?  133 GLY   B HA3  1 
ATOM   6069 N  N    . ALA   B 1 134 ? 39.922 -32.595 5.303   1.00 17.63 ?  134 ALA   B N    1 
ATOM   6070 C  CA   . ALA   B 1 134 ? 38.597 -32.880 4.772   1.00 17.65 ?  134 ALA   B CA   1 
ATOM   6071 C  C    . ALA   B 1 134 ? 38.686 -33.870 3.617   1.00 17.72 ?  134 ALA   B C    1 
ATOM   6072 O  O    . ALA   B 1 134 ? 39.741 -34.060 3.004   1.00 18.73 ?  134 ALA   B O    1 
ATOM   6073 C  CB   . ALA   B 1 134 ? 37.914 -31.597 4.300   1.00 18.40 ?  134 ALA   B CB   1 
ATOM   6074 H  H    . ALA   B 1 134 ? 40.270 -31.847 5.040   1.00 21.20 ?  134 ALA   B H    1 
ATOM   6075 H  HA   . ALA   B 1 134 ? 38.050 -33.270 5.473   1.00 21.23 ?  134 ALA   B HA   1 
ATOM   6076 H  HB1  . ALA   B 1 134 ? 37.027 -31.815 3.969   1.00 22.13 ?  134 ALA   B HB1  1 
ATOM   6077 H  HB2  . ALA   B 1 134 ? 37.843 -30.981 5.047   1.00 22.13 ?  134 ALA   B HB2  1 
ATOM   6078 H  HB3  . ALA   B 1 134 ? 38.442 -31.199 3.591   1.00 22.13 ?  134 ALA   B HB3  1 
ATOM   6079 N  N    . ASP   B 1 135 ? 37.554 -34.496 3.323   1.00 18.23 ?  135 ASP   B N    1 
ATOM   6080 C  CA   . ASP   B 1 135 ? 37.459 -35.385 2.176   1.00 18.96 ?  135 ASP   B CA   1 
ATOM   6081 C  C    . ASP   B 1 135 ? 37.556 -34.545 0.909   1.00 17.70 ?  135 ASP   B C    1 
ATOM   6082 O  O    . ASP   B 1 135 ? 36.701 -33.677 0.688   1.00 17.68 ?  135 ASP   B O    1 
ATOM   6083 C  CB   . ASP   B 1 135 ? 36.118 -36.114 2.230   1.00 20.68 ?  135 ASP   B CB   1 
ATOM   6084 C  CG   . ASP   B 1 135 ? 35.938 -37.111 1.101   1.00 22.30 ?  135 ASP   B CG   1 
ATOM   6085 O  OD1  . ASP   B 1 135 ? 36.796 -37.160 0.194   1.00 22.09 ?  135 ASP   B OD1  1 
ATOM   6086 O  OD2  . ASP   B 1 135 ? 34.942 -37.870 1.136   1.00 25.11 -1 135 ASP   B OD2  1 
ATOM   6087 H  H    . ASP   B 1 135 ? 36.825 -34.421 3.773   1.00 21.92 ?  135 ASP   B H    1 
ATOM   6088 H  HA   . ASP   B 1 135 ? 38.176 -36.040 2.205   1.00 22.80 ?  135 ASP   B HA   1 
ATOM   6089 H  HB2  . ASP   B 1 135 ? 36.059 -36.602 3.065   1.00 24.86 ?  135 ASP   B HB2  1 
ATOM   6090 H  HB3  . ASP   B 1 135 ? 35.405 -35.462 2.172   1.00 24.86 ?  135 ASP   B HB3  1 
ATOM   6091 N  N    . PRO   B 1 136 ? 38.566 -34.747 0.062   1.00 17.84 ?  136 PRO   B N    1 
ATOM   6092 C  CA   . PRO   B 1 136 ? 38.659 -33.927 -1.155  1.00 17.00 ?  136 PRO   B CA   1 
ATOM   6093 C  C    . PRO   B 1 136 ? 37.467 -34.084 -2.080  1.00 16.37 ?  136 PRO   B C    1 
ATOM   6094 O  O    . PRO   B 1 136 ? 37.142 -33.140 -2.807  1.00 15.56 ?  136 PRO   B O    1 
ATOM   6095 C  CB   . PRO   B 1 136 ? 39.972 -34.394 -1.800  1.00 18.14 ?  136 PRO   B CB   1 
ATOM   6096 C  CG   . PRO   B 1 136 ? 40.179 -35.783 -1.268  1.00 19.12 ?  136 PRO   B CG   1 
ATOM   6097 C  CD   . PRO   B 1 136 ? 39.635 -35.757 0.132   1.00 18.85 ?  136 PRO   B CD   1 
ATOM   6098 H  HA   . PRO   B 1 136 ? 38.741 -32.991 -0.917  1.00 20.45 ?  136 PRO   B HA   1 
ATOM   6099 H  HB2  . PRO   B 1 136 ? 39.879 -34.405 -2.768  1.00 21.82 ?  136 PRO   B HB2  1 
ATOM   6100 H  HB3  . PRO   B 1 136 ? 40.695 -33.807 -1.532  1.00 21.82 ?  136 PRO   B HB3  1 
ATOM   6101 H  HG2  . PRO   B 1 136 ? 39.690 -36.421 -1.810  1.00 23.00 ?  136 PRO   B HG2  1 
ATOM   6102 H  HG3  . PRO   B 1 136 ? 41.126 -35.995 -1.261  1.00 23.00 ?  136 PRO   B HG3  1 
ATOM   6103 H  HD2  . PRO   B 1 136 ? 39.271 -36.623 0.371   1.00 22.66 ?  136 PRO   B HD2  1 
ATOM   6104 H  HD3  . PRO   B 1 136 ? 40.320 -35.472 0.760   1.00 22.66 ?  136 PRO   B HD3  1 
ATOM   6105 N  N    . ILE   B 1 137 ? 36.809 -35.249 -2.079  1.00 16.73 ?  137 ILE   B N    1 
ATOM   6106 C  CA   . ILE   B 1 137 ? 35.589 -35.419 -2.863  1.00 17.01 ?  137 ILE   B CA   1 
ATOM   6107 C  C    . ILE   B 1 137 ? 34.519 -34.447 -2.383  1.00 16.58 ?  137 ILE   B C    1 
ATOM   6108 O  O    . ILE   B 1 137 ? 33.803 -33.831 -3.185  1.00 16.30 ?  137 ILE   B O    1 
ATOM   6109 C  CB   . ILE   B 1 137 ? 35.116 -36.887 -2.796  1.00 19.06 ?  137 ILE   B CB   1 
ATOM   6110 C  CG1  . ILE   B 1 137 ? 36.104 -37.799 -3.529  1.00 21.36 ?  137 ILE   B CG1  1 
ATOM   6111 C  CG2  . ILE   B 1 137 ? 33.708 -37.031 -3.378  1.00 19.33 ?  137 ILE   B CG2  1 
ATOM   6112 C  CD1  . ILE   B 1 137 ? 35.784 -39.283 -3.414  1.00 23.40 ?  137 ILE   B CD1  1 
ATOM   6113 H  H    . ILE   B 1 137 ? 37.047 -35.950 -1.639  1.00 20.12 ?  137 ILE   B H    1 
ATOM   6114 H  HA   . ILE   B 1 137 ? 35.779 -35.219 -3.793  1.00 20.45 ?  137 ILE   B HA   1 
ATOM   6115 H  HB   . ILE   B 1 137 ? 35.085 -37.160 -1.869  1.00 22.92 ?  137 ILE   B HB   1 
ATOM   6116 H  HG12 . ILE   B 1 137 ? 36.103 -37.576 -4.472  1.00 25.68 ?  137 ILE   B HG12 1 
ATOM   6117 H  HG13 . ILE   B 1 137 ? 36.988 -37.665 -3.158  1.00 25.68 ?  137 ILE   B HG13 1 
ATOM   6118 H  HG21 . ILE   B 1 137 ? 33.460 -37.970 -3.408  1.00 23.24 ?  137 ILE   B HG21 1 
ATOM   6119 H  HG22 . ILE   B 1 137 ? 33.079 -36.557 -2.816  1.00 23.24 ?  137 ILE   B HG22 1 
ATOM   6120 H  HG23 . ILE   B 1 137 ? 33.698 -36.663 -4.275  1.00 23.24 ?  137 ILE   B HG23 1 
ATOM   6121 H  HD11 . ILE   B 1 137 ? 36.447 -39.777 -3.918  1.00 28.13 ?  137 ILE   B HD11 1 
ATOM   6122 H  HD12 . ILE   B 1 137 ? 35.813 -39.546 -2.479  1.00 28.13 ?  137 ILE   B HD12 1 
ATOM   6123 H  HD13 . ILE   B 1 137 ? 34.904 -39.461 -3.781  1.00 28.13 ?  137 ILE   B HD13 1 
ATOM   6124 N  N    . HIS   B 1 138 ? 34.392 -34.297 -1.068  1.00 16.68 ?  138 HIS   B N    1 
ATOM   6125 C  CA   . HIS   B 1 138 ? 33.443 -33.334 -0.531  1.00 17.21 ?  138 HIS   B CA   1 
ATOM   6126 C  C    . HIS   B 1 138 ? 33.855 -31.907 -0.864  1.00 16.22 ?  138 HIS   B C    1 
ATOM   6127 O  O    . HIS   B 1 138 ? 33.007 -31.070 -1.190  1.00 16.51 ?  138 HIS   B O    1 
ATOM   6128 C  CB   . HIS   B 1 138 ? 33.329 -33.505 0.976   1.00 18.36 ?  138 HIS   B CB   1 
ATOM   6129 C  CG   . HIS   B 1 138 ? 32.386 -32.533 1.606   1.00 19.67 ?  138 HIS   B CG   1 
ATOM   6130 N  ND1  . HIS   B 1 138 ? 31.049 -32.479 1.277   1.00 21.13 ?  138 HIS   B ND1  1 
ATOM   6131 C  CD2  . HIS   B 1 138 ? 32.590 -31.551 2.515   1.00 20.07 ?  138 HIS   B CD2  1 
ATOM   6132 C  CE1  . HIS   B 1 138 ? 30.465 -31.519 1.971   1.00 20.90 ?  138 HIS   B CE1  1 
ATOM   6133 N  NE2  . HIS   B 1 138 ? 31.378 -30.942 2.732   1.00 20.21 ?  138 HIS   B NE2  1 
ATOM   6134 H  H    . HIS   B 1 138 ? 34.843 -34.733 -0.480  1.00 20.06 ?  138 HIS   B H    1 
ATOM   6135 H  HA   . HIS   B 1 138 ? 32.570 -33.502 -0.923  1.00 20.70 ?  138 HIS   B HA   1 
ATOM   6136 H  HB2  . HIS   B 1 138 ? 33.003 -34.400 1.168   1.00 22.08 ?  138 HIS   B HB2  1 
ATOM   6137 H  HB3  . HIS   B 1 138 ? 34.200 -33.377 1.375   1.00 22.08 ?  138 HIS   B HB3  1 
ATOM   6138 H  HD1  . HIS   B 1 138 ? 30.653 -32.999 0.713   1.00 25.41 ?  138 HIS   B HD1  1 
ATOM   6139 H  HD2  . HIS   B 1 138 ? 33.389 -31.336 2.929   1.00 24.13 ?  138 HIS   B HD2  1 
ATOM   6140 H  HE1  . HIS   B 1 138 ? 29.558 -31.296 1.932   1.00 25.13 ?  138 HIS   B HE1  1 
ATOM   6141 N  N    . SER   B 1 139 ? 35.149 -31.605 -0.787  1.00 15.75 ?  139 SER   B N    1 
ATOM   6142 C  CA   . SER   B 1 139 ? 35.585 -30.254 -1.105  1.00 15.10 ?  139 SER   B CA   1 
ATOM   6143 C  C    . SER   B 1 139 ? 35.249 -29.904 -2.546  1.00 14.29 ?  139 SER   B C    1 
ATOM   6144 O  O    . SER   B 1 139 ? 34.805 -28.787 -2.829  1.00 14.49 ?  139 SER   B O    1 
ATOM   6145 C  CB   . SER   B 1 139 ? 37.079 -30.112 -0.836  1.00 15.67 ?  139 SER   B CB   1 
ATOM   6146 O  OG   . SER   B 1 139 ? 37.493 -28.785 -1.114  1.00 15.41 ?  139 SER   B OG   1 
ATOM   6147 H  H    . SER   B 1 139 ? 35.770 -32.148 -0.566  1.00 18.95 ?  139 SER   B H    1 
ATOM   6148 H  HA   . SER   B 1 139 ? 35.111 -29.630 -0.536  1.00 18.17 ?  139 SER   B HA   1 
ATOM   6149 H  HB2  . SER   B 1 139 ? 37.251 -30.317 0.097   1.00 18.86 ?  139 SER   B HB2  1 
ATOM   6150 H  HB3  . SER   B 1 139 ? 37.566 -30.722 -1.409  1.00 18.86 ?  139 SER   B HB3  1 
ATOM   6151 H  HG   . SER   B 1 139 ? 38.317 -28.704 -0.954  1.00 18.54 ?  139 SER   B HG   1 
ATOM   6152 N  N    . LEU   B 1 140 ? 35.437 -30.849 -3.469  1.00 13.98 ?  140 LEU   B N    1 
ATOM   6153 C  CA   . LEU   B 1 140 ? 35.071 -30.599 -4.856  1.00 14.01 ?  140 LEU   B CA   1 
ATOM   6154 C  C    . LEU   B 1 140 ? 33.570 -30.375 -4.985  1.00 14.32 ?  140 LEU   B C    1 
ATOM   6155 O  O    . LEU   B 1 140 ? 33.131 -29.487 -5.723  1.00 14.38 ?  140 LEU   B O    1 
ATOM   6156 C  CB   . LEU   B 1 140 ? 35.536 -31.763 -5.733  1.00 13.90 ?  140 LEU   B CB   1 
ATOM   6157 C  CG   . LEU   B 1 140 ? 35.169 -31.655 -7.206  1.00 14.51 ?  140 LEU   B CG   1 
ATOM   6158 C  CD1  . LEU   B 1 140 ? 35.735 -30.376 -7.803  1.00 15.09 ?  140 LEU   B CD1  1 
ATOM   6159 C  CD2  . LEU   B 1 140 ? 35.644 -32.881 -7.958  1.00 15.73 ?  140 LEU   B CD2  1 
ATOM   6160 H  H    . LEU   B 1 140 ? 35.766 -31.627 -3.323  1.00 16.83 ?  140 LEU   B H    1 
ATOM   6161 H  HA   . LEU   B 1 140 ? 35.524 -29.797 -5.164  1.00 16.86 ?  140 LEU   B HA   1 
ATOM   6162 H  HB2  . LEU   B 1 140 ? 36.503 -31.827 -5.681  1.00 16.72 ?  140 LEU   B HB2  1 
ATOM   6163 H  HB3  . LEU   B 1 140 ? 35.138 -32.583 -5.400  1.00 16.72 ?  140 LEU   B HB3  1 
ATOM   6164 H  HG   . LEU   B 1 140 ? 34.204 -31.608 -7.287  1.00 17.46 ?  140 LEU   B HG   1 
ATOM   6165 H  HD11 . LEU   B 1 140 ? 35.623 -30.402 -8.764  1.00 18.15 ?  140 LEU   B HD11 1 
ATOM   6166 H  HD12 . LEU   B 1 140 ? 35.253 -29.614 -7.437  1.00 18.15 ?  140 LEU   B HD12 1 
ATOM   6167 H  HD13 . LEU   B 1 140 ? 36.675 -30.311 -7.578  1.00 18.15 ?  140 LEU   B HD13 1 
ATOM   6168 H  HD21 . LEU   B 1 140 ? 35.396 -32.785 -8.892  1.00 18.93 ?  140 LEU   B HD21 1 
ATOM   6169 H  HD22 . LEU   B 1 140 ? 36.602 -32.949 -7.871  1.00 18.93 ?  140 LEU   B HD22 1 
ATOM   6170 H  HD23 . LEU   B 1 140 ? 35.211 -33.659 -7.578  1.00 18.93 ?  140 LEU   B HD23 1 
ATOM   6171 N  N    . ARG   B 1 141 ? 32.769 -31.169 -4.269  1.00 14.49 ?  141 ARG   B N    1 
ATOM   6172 C  CA   . ARG   B 1 141 ? 31.320 -30.991 -4.247  1.00 15.69 ?  141 ARG   B CA   1 
ATOM   6173 C  C    . ARG   B 1 141 ? 30.945 -29.580 -3.820  1.00 15.27 ?  141 ARG   B C    1 
ATOM   6174 O  O    . ARG   B 1 141 ? 30.139 -28.904 -4.478  1.00 15.14 ?  141 ARG   B O    1 
ATOM   6175 C  CB   . ARG   B 1 141 ? 30.733 -32.023 -3.275  1.00 16.86 ?  141 ARG   B CB   1 
ATOM   6176 C  CG   . ARG   B 1 141 ? 29.271 -31.897 -2.945  1.00 18.64 ?  141 ARG   B CG   1 
ATOM   6177 C  CD   . ARG   B 1 141 ? 28.467 -32.531 -4.010  1.00 20.55 ?  141 ARG   B CD   1 
ATOM   6178 N  NE   . ARG   B 1 141 ? 28.209 -31.624 -5.115  1.00 20.73 ?  141 ARG   B NE   1 
ATOM   6179 C  CZ   . ARG   B 1 141 ? 28.204 -31.973 -6.394  1.00 20.19 ?  141 ARG   B CZ   1 
ATOM   6180 N  NH1  . ARG   B 1 141 ? 28.648 -33.156 -6.793  1.00 20.19 ?  141 ARG   B NH1  1 
ATOM   6181 N  NH2  . ARG   B 1 141 ? 27.741 -31.112 -7.296  1.00 20.95 ?  141 ARG   B NH2  1 
ATOM   6182 H  H    . ARG   B 1 141 ? 33.050 -31.823 -3.787  1.00 17.44 ?  141 ARG   B H    1 
ATOM   6183 H  HA   . ARG   B 1 141 ? 30.958 -31.153 -5.128  1.00 18.87 ?  141 ARG   B HA   1 
ATOM   6184 H  HB2  . ARG   B 1 141 ? 30.880 -32.908 -3.652  1.00 20.28 ?  141 ARG   B HB2  1 
ATOM   6185 H  HB3  . ARG   B 1 141 ? 31.220 -31.960 -2.439  1.00 20.28 ?  141 ARG   B HB3  1 
ATOM   6186 H  HG2  . ARG   B 1 141 ? 29.097 -32.348 -2.107  1.00 22.41 ?  141 ARG   B HG2  1 
ATOM   6187 H  HG3  . ARG   B 1 141 ? 29.023 -30.959 -2.880  1.00 22.41 ?  141 ARG   B HG3  1 
ATOM   6188 H  HD2  . ARG   B 1 141 ? 28.941 -33.312 -4.346  1.00 24.71 ?  141 ARG   B HD2  1 
ATOM   6189 H  HD3  . ARG   B 1 141 ? 27.621 -32.806 -3.636  1.00 24.71 ?  141 ARG   B HD3  1 
ATOM   6190 H  HE   . ARG   B 1 141 ? 28.023 -30.807 -4.923  1.00 24.93 ?  141 ARG   B HE   1 
ATOM   6191 H  HH11 . ARG   B 1 141 ? 28.941 -33.727 -6.223  1.00 24.28 ?  141 ARG   B HH11 1 
ATOM   6192 H  HH12 . ARG   B 1 141 ? 28.643 -33.352 -7.629  1.00 24.28 ?  141 ARG   B HH12 1 
ATOM   6193 H  HH21 . ARG   B 1 141 ? 27.454 -30.340 -7.048  1.00 25.18 ?  141 ARG   B HH21 1 
ATOM   6194 H  HH22 . ARG   B 1 141 ? 27.749 -31.318 -8.132  1.00 25.18 ?  141 ARG   B HH22 1 
ATOM   6195 N  N    . VAL   B 1 142 ? 31.493 -29.132 -2.693  1.00 14.93 ?  142 VAL   B N    1 
ATOM   6196 C  CA   . VAL   B 1 142 ? 31.158 -27.798 -2.209  1.00 14.58 ?  142 VAL   B CA   1 
ATOM   6197 C  C    . VAL   B 1 142 ? 31.625 -26.741 -3.201  1.00 14.25 ?  142 VAL   B C    1 
ATOM   6198 O  O    . VAL   B 1 142 ? 30.924 -25.754 -3.458  1.00 14.82 ?  142 VAL   B O    1 
ATOM   6199 C  CB   . VAL   B 1 142 ? 31.705 -27.571 -0.787  1.00 15.12 ?  142 VAL   B CB   1 
ATOM   6200 C  CG1  . VAL   B 1 142 ? 31.395 -26.152 -0.316  1.00 14.98 ?  142 VAL   B CG1  1 
ATOM   6201 C  CG2  . VAL   B 1 142 ? 31.115 -28.593 0.174   1.00 15.74 ?  142 VAL   B CG2  1 
ATOM   6202 H  H    . VAL   B 1 142 ? 32.049 -29.569 -2.201  1.00 17.96 ?  142 VAL   B H    1 
ATOM   6203 H  HA   . VAL   B 1 142 ? 30.198 -27.729 -2.151  1.00 17.54 ?  142 VAL   B HA   1 
ATOM   6204 H  HB   . VAL   B 1 142 ? 32.670 -27.685 -0.788  1.00 18.20 ?  142 VAL   B HB   1 
ATOM   6205 H  HG11 . VAL   B 1 142 ? 31.578 -26.087 0.633   1.00 18.02 ?  142 VAL   B HG11 1 
ATOM   6206 H  HG12 . VAL   B 1 142 ? 31.958 -25.528 -0.804  1.00 18.02 ?  142 VAL   B HG12 1 
ATOM   6207 H  HG13 . VAL   B 1 142 ? 30.461 -25.961 -0.489  1.00 18.02 ?  142 VAL   B HG13 1 
ATOM   6208 H  HG21 . VAL   B 1 142 ? 31.429 -28.406 1.071   1.00 18.94 ?  142 VAL   B HG21 1 
ATOM   6209 H  HG22 . VAL   B 1 142 ? 30.147 -28.530 0.142   1.00 18.94 ?  142 VAL   B HG22 1 
ATOM   6210 H  HG23 . VAL   B 1 142 ? 31.396 -29.482 -0.097  1.00 18.94 ?  142 VAL   B HG23 1 
ATOM   6211 N  N    . CYS   B 1 143 ? 32.807 -26.937 -3.789  1.00 13.66 ?  143 CYS   B N    1 
ATOM   6212 C  CA   . CYS   B 1 143 ? 33.298 -25.996 -4.790  1.00 13.74 ?  143 CYS   B CA   1 
ATOM   6213 C  C    . CYS   B 1 143 ? 32.298 -25.852 -5.931  1.00 13.54 ?  143 CYS   B C    1 
ATOM   6214 O  O    . CYS   B 1 143 ? 31.894 -24.741 -6.292  1.00 13.70 ?  143 CYS   B O    1 
ATOM   6215 C  CB   . CYS   B 1 143 ? 34.656 -26.478 -5.315  1.00 13.92 ?  143 CYS   B CB   1 
ATOM   6216 S  SG   . CYS   B 1 143 ? 35.403 -25.384 -6.552  1.00 13.87 ?  143 CYS   B SG   1 
ATOM   6217 H  H    . CYS   B 1 143 ? 33.338 -27.595 -3.625  1.00 16.43 ?  143 CYS   B H    1 
ATOM   6218 H  HA   . CYS   B 1 143 ? 33.427 -25.127 -4.383  1.00 16.53 ?  143 CYS   B HA   1 
ATOM   6219 H  HB2  . CYS   B 1 143 ? 35.280 -26.548 -4.571  1.00 16.75 ?  143 CYS   B HB2  1 
ATOM   6220 H  HB3  . CYS   B 1 143 ? 34.546 -27.348 -5.721  1.00 16.75 ?  143 CYS   B HB3  1 
ATOM   6221 H  HG   . CYS   B 1 143 ? 36.484 -25.812 -6.864  1.00 16.70 ?  143 CYS   B HG   1 
ATOM   6222 N  N    . VAL   B 1 144 ? 31.903 -26.973 -6.528  1.00 13.99 ?  144 VAL   B N    1 
ATOM   6223 C  CA   . VAL   B 1 144 ? 30.988 -26.915 -7.662  1.00 14.96 ?  144 VAL   B CA   1 
ATOM   6224 C  C    . VAL   B 1 144 ? 29.646 -26.307 -7.281  1.00 15.10 ?  144 VAL   B C    1 
ATOM   6225 O  O    . VAL   B 1 144 ? 29.027 -25.602 -8.089  1.00 16.21 ?  144 VAL   B O    1 
ATOM   6226 C  CB   . VAL   B 1 144 ? 30.827 -28.325 -8.239  1.00 17.58 ?  144 VAL   B CB   1 
ATOM   6227 C  CG1  . VAL   B 1 144 ? 29.552 -28.454 -9.069  1.00 20.24 ?  144 VAL   B CG1  1 
ATOM   6228 C  CG2  . VAL   B 1 144 ? 32.068 -28.715 -9.034  1.00 17.82 ?  144 VAL   B CG2  1 
ATOM   6229 H  H    . VAL   B 1 144 ? 32.148 -27.768 -6.304  1.00 16.84 ?  144 VAL   B H    1 
ATOM   6230 H  HA   . VAL   B 1 144 ? 31.374 -26.361 -8.352  1.00 17.99 ?  144 VAL   B HA   1 
ATOM   6231 H  HB   . VAL   B 1 144 ? 30.755 -28.956 -7.503  1.00 21.14 ?  144 VAL   B HB   1 
ATOM   6232 H  HG11 . VAL   B 1 144 ? 29.628 -29.242 -9.637  1.00 24.34 ?  144 VAL   B HG11 1 
ATOM   6233 H  HG12 . VAL   B 1 144 ? 28.796 -28.557 -8.472  1.00 24.34 ?  144 VAL   B HG12 1 
ATOM   6234 H  HG13 . VAL   B 1 144 ? 29.449 -27.665 -9.617  1.00 24.34 ?  144 VAL   B HG13 1 
ATOM   6235 H  HG21 . VAL   B 1 144 ? 31.953 -29.613 -9.385  1.00 21.43 ?  144 VAL   B HG21 1 
ATOM   6236 H  HG22 . VAL   B 1 144 ? 32.181 -28.087 -9.767  1.00 21.43 ?  144 VAL   B HG22 1 
ATOM   6237 H  HG23 . VAL   B 1 144 ? 32.840 -28.684 -8.450  1.00 21.43 ?  144 VAL   B HG23 1 
ATOM   6238 N  N    . ASP   B 1 145 ? 29.181 -26.551 -6.062  1.00 15.43 ?  145 ASP   B N    1 
ATOM   6239 C  CA   . ASP   B 1 145 ? 27.874 -26.082 -5.623  1.00 16.07 ?  145 ASP   B CA   1 
ATOM   6240 C  C    . ASP   B 1 145 ? 27.906 -24.660 -5.079  1.00 15.43 ?  145 ASP   B C    1 
ATOM   6241 O  O    . ASP   B 1 145 ? 26.849 -24.119 -4.737  1.00 17.26 ?  145 ASP   B O    1 
ATOM   6242 C  CB   . ASP   B 1 145 ? 27.292 -27.004 -4.543  1.00 17.74 ?  145 ASP   B CB   1 
ATOM   6243 C  CG   . ASP   B 1 145 ? 26.921 -28.375 -5.059  1.00 19.32 ?  145 ASP   B CG   1 
ATOM   6244 O  OD1  . ASP   B 1 145 ? 26.819 -28.566 -6.288  1.00 19.85 ?  145 ASP   B OD1  1 
ATOM   6245 O  OD2  . ASP   B 1 145 ? 26.723 -29.259 -4.208  1.00 21.42 -1 145 ASP   B OD2  1 
ATOM   6246 H  H    . ASP   B 1 145 ? 29.617 -26.978 -5.460  1.00 18.56 ?  145 ASP   B H    1 
ATOM   6247 H  HA   . ASP   B 1 145 ? 27.275 -26.075 -6.380  1.00 19.33 ?  145 ASP   B HA   1 
ATOM   6248 H  HB2  . ASP   B 1 145 ? 27.945 -27.122 -3.845  1.00 21.34 ?  145 ASP   B HB2  1 
ATOM   6249 H  HB3  . ASP   B 1 145 ? 26.486 -26.595 -4.188  1.00 21.34 ?  145 ASP   B HB3  1 
ATOM   6250 N  N    . THR   B 1 146 ? 29.082 -24.043 -4.984  1.00 13.79 ?  146 THR   B N    1 
ATOM   6251 C  CA   . THR   B 1 146 ? 29.215 -22.721 -4.378  1.00 13.51 ?  146 THR   B CA   1 
ATOM   6252 C  C    . THR   B 1 146 ? 29.846 -21.694 -5.298  1.00 13.31 ?  146 THR   B C    1 
ATOM   6253 O  O    . THR   B 1 146 ? 29.392 -20.535 -5.344  1.00 13.68 ?  146 THR   B O    1 
ATOM   6254 C  CB   . THR   B 1 146 ? 30.043 -22.822 -3.091  1.00 13.88 ?  146 THR   B CB   1 
ATOM   6255 O  OG1  . THR   B 1 146 ? 29.469 -23.815 -2.233  1.00 14.16 ?  146 THR   B OG1  1 
ATOM   6256 C  CG2  . THR   B 1 146 ? 30.117 -21.483 -2.367  1.00 14.37 ?  146 THR   B CG2  1 
ATOM   6257 H  H    . THR   B 1 146 ? 29.830 -24.368 -5.268  1.00 16.60 ?  146 THR   B H    1 
ATOM   6258 H  HA   . THR   B 1 146 ? 28.342 -22.393 -4.139  1.00 16.26 ?  146 THR   B HA   1 
ATOM   6259 H  HB   . THR   B 1 146 ? 30.953 -23.081 -3.314  1.00 16.71 ?  146 THR   B HB   1 
ATOM   6260 H  HG1  . THR   B 1 146 ? 29.510 -24.575 -2.609  1.00 17.04 ?  146 THR   B HG1  1 
ATOM   6261 H  HG21 . THR   B 1 146 ? 30.470 -21.610 -1.475  1.00 17.30 ?  146 THR   B HG21 1 
ATOM   6262 H  HG22 . THR   B 1 146 ? 30.698 -20.876 -2.853  1.00 17.30 ?  146 THR   B HG22 1 
ATOM   6263 H  HG23 . THR   B 1 146 ? 29.232 -21.095 -2.307  1.00 17.30 ?  146 THR   B HG23 1 
ATOM   6264 N  N    . VAL   B 1 147 ? 30.908 -22.065 -6.001  1.00 13.04 ?  147 VAL   B N    1 
ATOM   6265 C  CA   . VAL   B 1 147 ? 31.629 -21.119 -6.837  1.00 12.90 ?  147 VAL   B CA   1 
ATOM   6266 C  C    . VAL   B 1 147 ? 30.894 -20.986 -8.157  1.00 13.15 ?  147 VAL   B C    1 
ATOM   6267 O  O    . VAL   B 1 147 ? 30.524 -21.988 -8.785  1.00 14.01 ?  147 VAL   B O    1 
ATOM   6268 C  CB   . VAL   B 1 147 ? 33.082 -21.574 -7.044  1.00 12.75 ?  147 VAL   B CB   1 
ATOM   6269 C  CG1  . VAL   B 1 147 ? 33.842 -20.541 -7.855  1.00 13.15 ?  147 VAL   B CG1  1 
ATOM   6270 C  CG2  . VAL   B 1 147 ? 33.761 -21.797 -5.706  1.00 13.25 ?  147 VAL   B CG2  1 
ATOM   6271 H  H    . VAL   B 1 147 ? 31.229 -22.868 -6.024  1.00 15.70 ?  147 VAL   B H    1 
ATOM   6272 H  HA   . VAL   B 1 147 ? 31.644 -20.253 -6.402  1.00 15.52 ?  147 VAL   B HA   1 
ATOM   6273 H  HB   . VAL   B 1 147 ? 33.092 -22.412 -7.536  1.00 15.34 ?  147 VAL   B HB   1 
ATOM   6274 H  HG11 . VAL   B 1 147 ? 34.786 -20.764 -7.849  1.00 15.83 ?  147 VAL   B HG11 1 
ATOM   6275 H  HG12 . VAL   B 1 147 ? 33.509 -20.537 -8.765  1.00 15.83 ?  147 VAL   B HG12 1 
ATOM   6276 H  HG13 . VAL   B 1 147 ? 33.711 -19.666 -7.451  1.00 15.83 ?  147 VAL   B HG13 1 
ATOM   6277 H  HG21 . VAL   B 1 147 ? 34.702 -21.986 -5.856  1.00 15.94 ?  147 VAL   B HG21 1 
ATOM   6278 H  HG22 . VAL   B 1 147 ? 33.669 -20.995 -5.168  1.00 15.94 ?  147 VAL   B HG22 1 
ATOM   6279 H  HG23 . VAL   B 1 147 ? 33.342 -22.547 -5.258  1.00 15.94 ?  147 VAL   B HG23 1 
ATOM   6280 N  N    . ARG   B 1 148 ? 30.681 -19.736 -8.573  1.00 13.07 ?  148 ARG   B N    1 
ATOM   6281 C  CA   . ARG   B 1 148 ? 30.061 -19.417 -9.849  1.00 13.09 ?  148 ARG   B CA   1 
ATOM   6282 C  C    . ARG   B 1 148 ? 31.015 -18.738 -10.820 1.00 13.28 ?  148 ARG   B C    1 
ATOM   6283 O  O    . ARG   B 1 148 ? 30.730 -18.716 -12.021 1.00 14.56 ?  148 ARG   B O    1 
ATOM   6284 C  CB   . ARG   B 1 148 ? 28.820 -18.536 -9.634  1.00 13.56 ?  148 ARG   B CB   1 
ATOM   6285 C  CG   . ARG   B 1 148 ? 27.747 -19.245 -8.822  1.00 14.24 ?  148 ARG   B CG   1 
ATOM   6286 C  CD   . ARG   B 1 148 ? 26.539 -18.359 -8.511  1.00 15.17 ?  148 ARG   B CD   1 
ATOM   6287 N  NE   . ARG   B 1 148 ? 26.920 -17.161 -7.773  1.00 15.23 ?  148 ARG   B NE   1 
ATOM   6288 C  CZ   . ARG   B 1 148 ? 27.222 -17.133 -6.480  1.00 14.16 ?  148 ARG   B CZ   1 
ATOM   6289 N  NH1  . ARG   B 1 148 ? 27.169 -18.226 -5.730  1.00 14.22 ?  148 ARG   B NH1  1 
ATOM   6290 N  NH2  . ARG   B 1 148 ? 27.609 -15.983 -5.930  1.00 14.13 ?  148 ARG   B NH2  1 
ATOM   6291 H  H    . ARG   B 1 148 ? 30.895 -19.032 -8.111  1.00 15.73 ?  148 ARG   B H    1 
ATOM   6292 H  HA   . ARG   B 1 148 ? 29.764 -20.243 -10.256 1.00 15.75 ?  148 ARG   B HA   1 
ATOM   6293 H  HB2  . ARG   B 1 148 ? 29.075 -17.732 -9.155  1.00 16.32 ?  148 ARG   B HB2  1 
ATOM   6294 H  HB3  . ARG   B 1 148 ? 28.441 -18.305 -10.496 1.00 16.32 ?  148 ARG   B HB3  1 
ATOM   6295 H  HG2  . ARG   B 1 148 ? 27.426 -20.013 -9.323  1.00 17.14 ?  148 ARG   B HG2  1 
ATOM   6296 H  HG3  . ARG   B 1 148 ? 28.125 -19.536 -7.979  1.00 17.14 ?  148 ARG   B HG3  1 
ATOM   6297 H  HD2  . ARG   B 1 148 ? 26.126 -18.080 -9.343  1.00 18.25 ?  148 ARG   B HD2  1 
ATOM   6298 H  HD3  . ARG   B 1 148 ? 25.906 -18.858 -7.972  1.00 18.25 ?  148 ARG   B HD3  1 
ATOM   6299 H  HE   . ARG   B 1 148 ? 26.966 -16.421 -8.205  1.00 18.33 ?  148 ARG   B HE   1 
ATOM   6300 H  HH11 . ARG   B 1 148 ? 26.920 -18.978 -6.071  1.00 17.12 ?  148 ARG   B HH11 1 
ATOM   6301 H  HH12 . ARG   B 1 148 ? 27.363 -18.186 -4.892  1.00 17.12 ?  148 ARG   B HH12 1 
ATOM   6302 H  HH21 . ARG   B 1 148 ? 27.654 -15.274 -6.409  1.00 17.00 ?  148 ARG   B HH21 1 
ATOM   6303 H  HH22 . ARG   B 1 148 ? 27.806 -15.953 -5.094  1.00 17.00 ?  148 ARG   B HH22 1 
ATOM   6304 N  N    . THR   B 1 149 ? 32.121 -18.179 -10.332 1.00 13.06 ?  149 THR   B N    1 
ATOM   6305 C  CA   . THR   B 1 149 ? 33.164 -17.620 -11.179 1.00 13.14 ?  149 THR   B CA   1 
ATOM   6306 C  C    . THR   B 1 149 ? 34.046 -18.759 -11.694 1.00 12.77 ?  149 THR   B C    1 
ATOM   6307 O  O    . THR   B 1 149 ? 33.852 -19.930 -11.357 1.00 13.42 ?  149 THR   B O    1 
ATOM   6308 C  CB   . THR   B 1 149 ? 33.937 -16.569 -10.396 1.00 13.29 ?  149 THR   B CB   1 
ATOM   6309 O  OG1  . THR   B 1 149 ? 34.394 -17.174 -9.186  1.00 13.16 ?  149 THR   B OG1  1 
ATOM   6310 C  CG2  . THR   B 1 149 ? 33.038 -15.366 -10.093 1.00 13.96 ?  149 THR   B CG2  1 
ATOM   6311 H  H    . THR   B 1 149 ? 32.283 -18.105 -9.491  1.00 15.72 ?  149 THR   B H    1 
ATOM   6312 H  HA   . THR   B 1 149 ? 32.753 -17.186 -11.943 1.00 15.82 ?  149 THR   B HA   1 
ATOM   6313 H  HB   . THR   B 1 149 ? 34.697 -16.273 -10.913 1.00 15.99 ?  149 THR   B HB   1 
ATOM   6314 H  HG1  . THR   B 1 149 ? 34.809 -16.601 -8.722  1.00 15.83 ?  149 THR   B HG1  1 
ATOM   6315 H  HG21 . THR   B 1 149 ? 33.542 -14.690 -9.610  1.00 16.80 ?  149 THR   B HG21 1 
ATOM   6316 H  HG22 . THR   B 1 149 ? 32.711 -14.978 -10.921 1.00 16.80 ?  149 THR   B HG22 1 
ATOM   6317 H  HG23 . THR   B 1 149 ? 32.281 -15.638 -9.552  1.00 16.80 ?  149 THR   B HG23 1 
ATOM   6318 N  N    . ASN   B 1 150 ? 35.010 -18.433 -12.543 1.00 13.01 ?  150 ASN   B N    1 
ATOM   6319 C  CA   . ASN   B 1 150 ? 35.773 -19.458 -13.249 1.00 13.34 ?  150 ASN   B CA   1 
ATOM   6320 C  C    . ASN   B 1 150 ? 36.941 -19.912 -12.382 1.00 12.77 ?  150 ASN   B C    1 
ATOM   6321 O  O    . ASN   B 1 150 ? 37.874 -19.144 -12.132 1.00 13.50 ?  150 ASN   B O    1 
ATOM   6322 C  CB   . ASN   B 1 150 ? 36.239 -18.922 -14.595 1.00 15.23 ?  150 ASN   B CB   1 
ATOM   6323 C  CG   . ASN   B 1 150 ? 35.093 -18.702 -15.539 1.00 17.83 ?  150 ASN   B CG   1 
ATOM   6324 O  OD1  . ASN   B 1 150 ? 34.194 -19.529 -15.626 1.00 18.76 ?  150 ASN   B OD1  1 
ATOM   6325 N  ND2  . ASN   B 1 150 ? 35.098 -17.576 -16.232 1.00 19.78 ?  150 ASN   B ND2  1 
ATOM   6326 H  H    . ASN   B 1 150 ? 35.253 -17.623 -12.718 1.00 15.65 ?  150 ASN   B H    1 
ATOM   6327 H  HA   . ASN   B 1 150 ? 35.191 -20.220 -13.413 1.00 16.05 ?  150 ASN   B HA   1 
ATOM   6328 H  HB2  . ASN   B 1 150 ? 36.686 -18.070 -14.459 1.00 18.32 ?  150 ASN   B HB2  1 
ATOM   6329 H  HB3  . ASN   B 1 150 ? 36.843 -19.558 -14.999 1.00 18.32 ?  150 ASN   B HB3  1 
ATOM   6330 H  HD21 . ASN   B 1 150 ? 34.461 -17.404 -16.787 1.00 23.78 ?  150 ASN   B HD21 1 
ATOM   6331 H  HD22 . ASN   B 1 150 ? 35.745 -17.014 -16.139 1.00 23.78 ?  150 ASN   B HD22 1 
ATOM   6332 N  N    . VAL   B 1 151 ? 36.898 -21.158 -11.925 1.00 12.54 ?  151 VAL   B N    1 
ATOM   6333 C  CA   . VAL   B 1 151 ? 37.916 -21.687 -11.032 1.00 12.83 ?  151 VAL   B CA   1 
ATOM   6334 C  C    . VAL   B 1 151 ? 38.621 -22.857 -11.707 1.00 12.47 ?  151 VAL   B C    1 
ATOM   6335 O  O    . VAL   B 1 151 ? 37.978 -23.788 -12.215 1.00 13.45 ?  151 VAL   B O    1 
ATOM   6336 C  CB   . VAL   B 1 151 ? 37.356 -22.031 -9.635  1.00 13.82 ?  151 VAL   B CB   1 
ATOM   6337 C  CG1  . VAL   B 1 151 ? 36.180 -23.013 -9.714  1.00 14.85 ?  151 VAL   B CG1  1 
ATOM   6338 C  CG2  . VAL   B 1 151 ? 38.469 -22.541 -8.729  1.00 14.10 ?  151 VAL   B CG2  1 
ATOM   6339 H  H    . VAL   B 1 151 ? 36.275 -21.724 -12.128 1.00 15.10 ?  151 VAL   B H    1 
ATOM   6340 H  HA   . VAL   B 1 151 ? 38.580 -20.992 -10.902 1.00 15.44 ?  151 VAL   B HA   1 
ATOM   6341 H  HB   . VAL   B 1 151 ? 37.017 -21.211 -9.239  1.00 16.63 ?  151 VAL   B HB   1 
ATOM   6342 H  HG11 . VAL   B 1 151 ? 35.869 -23.207 -8.816  1.00 17.86 ?  151 VAL   B HG11 1 
ATOM   6343 H  HG12 . VAL   B 1 151 ? 35.462 -22.612 -10.231 1.00 17.86 ?  151 VAL   B HG12 1 
ATOM   6344 H  HG13 . VAL   B 1 151 ? 36.478 -23.831 -10.144 1.00 17.86 ?  151 VAL   B HG13 1 
ATOM   6345 H  HG21 . VAL   B 1 151 ? 38.126 -22.612 -7.823  1.00 16.97 ?  151 VAL   B HG21 1 
ATOM   6346 H  HG22 . VAL   B 1 151 ? 38.756 -23.414 -9.040  1.00 16.97 ?  151 VAL   B HG22 1 
ATOM   6347 H  HG23 . VAL   B 1 151 ? 39.210 -21.918 -8.753  1.00 16.97 ?  151 VAL   B HG23 1 
ATOM   6348 N  N    . TYR   B 1 152 ? 39.949 -22.772 -11.726 1.00 12.02 ?  152 TYR   B N    1 
ATOM   6349 C  CA   . TYR   B 1 152 ? 40.847 -23.751 -12.314 1.00 12.19 ?  152 TYR   B CA   1 
ATOM   6350 C  C    . TYR   B 1 152 ? 41.566 -24.429 -11.152 1.00 11.50 ?  152 TYR   B C    1 
ATOM   6351 O  O    . TYR   B 1 152 ? 42.416 -23.814 -10.499 1.00 12.02 ?  152 TYR   B O    1 
ATOM   6352 C  CB   . TYR   B 1 152 ? 41.817 -23.038 -13.258 1.00 13.15 ?  152 TYR   B CB   1 
ATOM   6353 C  CG   . TYR   B 1 152 ? 41.133 -22.576 -14.523 1.00 13.54 ?  152 TYR   B CG   1 
ATOM   6354 C  CD1  . TYR   B 1 152 ? 40.474 -21.350 -14.586 1.00 14.01 ?  152 TYR   B CD1  1 
ATOM   6355 C  CD2  . TYR   B 1 152 ? 41.124 -23.383 -15.649 1.00 14.83 ?  152 TYR   B CD2  1 
ATOM   6356 C  CE1  . TYR   B 1 152 ? 39.830 -20.944 -15.743 1.00 15.79 ?  152 TYR   B CE1  1 
ATOM   6357 C  CE2  . TYR   B 1 152 ? 40.486 -22.989 -16.805 1.00 15.70 ?  152 TYR   B CE2  1 
ATOM   6358 C  CZ   . TYR   B 1 152 ? 39.842 -21.768 -16.852 1.00 16.13 ?  152 TYR   B CZ   1 
ATOM   6359 O  OH   . TYR   B 1 152 ? 39.211 -21.389 -18.014 1.00 18.56 ?  152 TYR   B OH   1 
ATOM   6360 H  H    . TYR   B 1 152 ? 40.383 -22.107 -11.374 1.00 14.47 ?  152 TYR   B H    1 
ATOM   6361 H  HA   . TYR   B 1 152 ? 40.339 -24.413 -12.812 1.00 14.68 ?  152 TYR   B HA   1 
ATOM   6362 H  HB2  . TYR   B 1 152 ? 42.182 -22.261 -12.805 1.00 15.83 ?  152 TYR   B HB2  1 
ATOM   6363 H  HB3  . TYR   B 1 152 ? 42.530 -23.647 -13.502 1.00 15.83 ?  152 TYR   B HB3  1 
ATOM   6364 H  HD1  . TYR   B 1 152 ? 40.463 -20.796 -13.836 1.00 16.87 ?  152 TYR   B HD1  1 
ATOM   6365 H  HD2  . TYR   B 1 152 ? 41.553 -24.208 -15.620 1.00 17.85 ?  152 TYR   B HD2  1 
ATOM   6366 H  HE1  . TYR   B 1 152 ? 39.396 -20.124 -15.775 1.00 18.99 ?  152 TYR   B HE1  1 
ATOM   6367 H  HE2  . TYR   B 1 152 ? 40.496 -23.545 -17.549 1.00 18.89 ?  152 TYR   B HE2  1 
ATOM   6368 H  HH   . TYR   B 1 152 ? 39.306 -21.990 -18.594 1.00 22.32 ?  152 TYR   B HH   1 
ATOM   6369 N  N    . LEU   B 1 153 ? 41.197 -25.684 -10.880 1.00 12.04 ?  153 LEU   B N    1 
ATOM   6370 C  CA   . LEU   B 1 153 ? 41.708 -26.435 -9.742  1.00 11.57 ?  153 LEU   B CA   1 
ATOM   6371 C  C    . LEU   B 1 153 ? 42.940 -27.233 -10.140 1.00 12.01 ?  153 LEU   B C    1 
ATOM   6372 O  O    . LEU   B 1 153 ? 42.924 -27.959 -11.136 1.00 13.21 ?  153 LEU   B O    1 
ATOM   6373 C  CB   . LEU   B 1 153 ? 40.634 -27.395 -9.227  1.00 12.24 ?  153 LEU   B CB   1 
ATOM   6374 C  CG   . LEU   B 1 153 ? 39.377 -26.742 -8.655  1.00 13.13 ?  153 LEU   B CG   1 
ATOM   6375 C  CD1  . LEU   B 1 153 ? 38.275 -27.776 -8.508  1.00 13.79 ?  153 LEU   B CD1  1 
ATOM   6376 C  CD2  . LEU   B 1 153 ? 39.675 -26.092 -7.313  1.00 13.73 ?  153 LEU   B CD2  1 
ATOM   6377 H  H    . LEU   B 1 153 ? 40.619 -26.129 -11.354 1.00 14.50 ?  153 LEU   B H    1 
ATOM   6378 H  HA   . LEU   B 1 153 ? 41.937 -25.818 -9.036  1.00 13.93 ?  153 LEU   B HA   1 
ATOM   6379 H  HB2  . LEU   B 1 153 ? 40.354 -27.967 -9.957  1.00 14.73 ?  153 LEU   B HB2  1 
ATOM   6380 H  HB3  . LEU   B 1 153 ? 41.023 -27.935 -8.521  1.00 14.73 ?  153 LEU   B HB3  1 
ATOM   6381 H  HG   . LEU   B 1 153 ? 39.067 -26.046 -9.262  1.00 15.80 ?  153 LEU   B HG   1 
ATOM   6382 H  HD11 . LEU   B 1 153 ? 37.472 -27.330 -8.191  1.00 16.60 ?  153 LEU   B HD11 1 
ATOM   6383 H  HD12 . LEU   B 1 153 ? 38.113 -28.178 -9.371  1.00 16.60 ?  153 LEU   B HD12 1 
ATOM   6384 H  HD13 . LEU   B 1 153 ? 38.560 -28.442 -7.869  1.00 16.60 ?  153 LEU   B HD13 1 
ATOM   6385 H  HD21 . LEU   B 1 153 ? 38.861 -25.715 -6.949  1.00 16.52 ?  153 LEU   B HD21 1 
ATOM   6386 H  HD22 . LEU   B 1 153 ? 40.029 -26.765 -6.708  1.00 16.52 ?  153 LEU   B HD22 1 
ATOM   6387 H  HD23 . LEU   B 1 153 ? 40.336 -25.388 -7.440  1.00 16.52 ?  153 LEU   B HD23 1 
ATOM   6388 N  N    . ALA   B 1 154 ? 43.991 -27.130 -9.336  1.00 12.16 ?  154 ALA   B N    1 
ATOM   6389 C  CA   . ALA   B 1 154 ? 45.219 -27.887 -9.531  1.00 13.37 ?  154 ALA   B CA   1 
ATOM   6390 C  C    . ALA   B 1 154 ? 45.291 -28.966 -8.459  1.00 14.07 ?  154 ALA   B C    1 
ATOM   6391 O  O    . ALA   B 1 154 ? 45.227 -28.666 -7.259  1.00 15.34 ?  154 ALA   B O    1 
ATOM   6392 C  CB   . ALA   B 1 154 ? 46.440 -26.971 -9.472  1.00 13.97 ?  154 ALA   B CB   1 
ATOM   6393 H  H    . ALA   B 1 154 ? 44.010 -26.606 -8.649  1.00 14.64 ?  154 ALA   B H    1 
ATOM   6394 H  HA   . ALA   B 1 154 ? 45.201 -28.314 -10.397 1.00 16.09 ?  154 ALA   B HA   1 
ATOM   6395 H  HB1  . ALA   B 1 154 ? 47.242 -27.497 -9.603  1.00 16.82 ?  154 ALA   B HB1  1 
ATOM   6396 H  HB2  . ALA   B 1 154 ? 46.369 -26.299 -10.173 1.00 16.82 ?  154 ALA   B HB2  1 
ATOM   6397 H  HB3  . ALA   B 1 154 ? 46.471 -26.531 -8.605  1.00 16.82 ?  154 ALA   B HB3  1 
ATOM   6398 N  N    . VAL   B 1 155 ? 45.407 -30.214 -8.893  1.00 13.30 ?  155 VAL   B N    1 
ATOM   6399 C  CA   . VAL   B 1 155 ? 45.514 -31.363 -8.001  1.00 13.28 ?  155 VAL   B CA   1 
ATOM   6400 C  C    . VAL   B 1 155 ? 46.853 -32.035 -8.281  1.00 13.24 ?  155 VAL   B C    1 
ATOM   6401 O  O    . VAL   B 1 155 ? 47.086 -32.528 -9.393  1.00 15.34 ?  155 VAL   B O    1 
ATOM   6402 C  CB   . VAL   B 1 155 ? 44.355 -32.354 -8.196  1.00 14.74 ?  155 VAL   B CB   1 
ATOM   6403 C  CG1  . VAL   B 1 155 ? 44.542 -33.561 -7.292  1.00 14.80 ?  155 VAL   B CG1  1 
ATOM   6404 C  CG2  . VAL   B 1 155 ? 43.019 -31.667 -7.917  1.00 15.61 ?  155 VAL   B CG2  1 
ATOM   6405 H  H    . VAL   B 1 155 ? 45.441 -30.430 -9.726  1.00 16.01 ?  155 VAL   B H    1 
ATOM   6406 H  HA   . VAL   B 1 155 ? 45.506 -31.064 -7.078  1.00 15.99 ?  155 VAL   B HA   1 
ATOM   6407 H  HB   . VAL   B 1 155 ? 44.347 -32.659 -9.117  1.00 17.73 ?  155 VAL   B HB   1 
ATOM   6408 H  HG11 . VAL   B 1 155 ? 43.711 -34.063 -7.252  1.00 17.81 ?  155 VAL   B HG11 1 
ATOM   6409 H  HG12 . VAL   B 1 155 ? 45.245 -34.128 -7.654  1.00 17.81 ?  155 VAL   B HG12 1 
ATOM   6410 H  HG13 . VAL   B 1 155 ? 44.786 -33.261 -6.403  1.00 17.81 ?  155 VAL   B HG13 1 
ATOM   6411 H  HG21 . VAL   B 1 155 ? 42.302 -32.316 -8.013  1.00 18.78 ?  155 VAL   B HG21 1 
ATOM   6412 H  HG22 . VAL   B 1 155 ? 43.025 -31.318 -7.011  1.00 18.78 ?  155 VAL   B HG22 1 
ATOM   6413 H  HG23 . VAL   B 1 155 ? 42.893 -30.942 -8.549  1.00 18.78 ?  155 VAL   B HG23 1 
ATOM   6414 N  N    . PHE   B 1 156 ? 47.721 -32.073 -7.268  1.00 13.88 ?  156 PHE   B N    1 
ATOM   6415 C  CA   . PHE   B 1 156 ? 49.098 -32.530 -7.471  1.00 15.01 ?  156 PHE   B CA   1 
ATOM   6416 C  C    . PHE   B 1 156 ? 49.191 -34.027 -7.761  1.00 16.36 ?  156 PHE   B C    1 
ATOM   6417 O  O    . PHE   B 1 156 ? 49.911 -34.451 -8.676  1.00 18.27 ?  156 PHE   B O    1 
ATOM   6418 C  CB   . PHE   B 1 156 ? 49.932 -32.167 -6.244  1.00 14.87 ?  156 PHE   B CB   1 
ATOM   6419 C  CG   . PHE   B 1 156 ? 51.352 -32.629 -6.308  1.00 15.61 ?  156 PHE   B CG   1 
ATOM   6420 C  CD1  . PHE   B 1 156 ? 52.230 -32.094 -7.232  1.00 17.42 ?  156 PHE   B CD1  1 
ATOM   6421 C  CD2  . PHE   B 1 156 ? 51.814 -33.577 -5.419  1.00 16.07 ?  156 PHE   B CD2  1 
ATOM   6422 C  CE1  . PHE   B 1 156 ? 53.549 -32.506 -7.278  1.00 18.12 ?  156 PHE   B CE1  1 
ATOM   6423 C  CE2  . PHE   B 1 156 ? 53.128 -33.994 -5.459  1.00 17.75 ?  156 PHE   B CE2  1 
ATOM   6424 C  CZ   . PHE   B 1 156 ? 53.989 -33.462 -6.394  1.00 18.11 ?  156 PHE   B CZ   1 
ATOM   6425 H  H    . PHE   B 1 156 ? 47.535 -31.851 -6.457  1.00 16.71 ?  156 PHE   B H    1 
ATOM   6426 H  HA   . PHE   B 1 156 ? 49.467 -32.060 -8.228  1.00 18.06 ?  156 PHE   B HA   1 
ATOM   6427 H  HB2  . PHE   B 1 156 ? 49.941 -31.201 -6.154  1.00 17.89 ?  156 PHE   B HB2  1 
ATOM   6428 H  HB3  . PHE   B 1 156 ? 49.528 -32.565 -5.458  1.00 17.89 ?  156 PHE   B HB3  1 
ATOM   6429 H  HD1  . PHE   B 1 156 ? 51.932 -31.445 -7.832  1.00 20.95 ?  156 PHE   B HD1  1 
ATOM   6430 H  HD2  . PHE   B 1 156 ? 51.227 -33.941 -4.791  1.00 19.33 ?  156 PHE   B HD2  1 
ATOM   6431 H  HE1  . PHE   B 1 156 ? 54.133 -32.144 -7.907  1.00 21.79 ?  156 PHE   B HE1  1 
ATOM   6432 H  HE2  . PHE   B 1 156 ? 53.426 -34.644 -4.862  1.00 21.35 ?  156 PHE   B HE2  1 
ATOM   6433 H  HZ   . PHE   B 1 156 ? 54.876 -33.746 -6.420  1.00 21.77 ?  156 PHE   B HZ   1 
ATOM   6434 N  N    . ASP   B 1 157 ? 48.534 -34.848 -6.956  1.00 16.65 ?  157 ASP   B N    1 
ATOM   6435 C  CA   . ASP   B 1 157 ? 48.673 -36.295 -7.061  1.00 17.94 ?  157 ASP   B CA   1 
ATOM   6436 C  C    . ASP   B 1 157 ? 47.755 -36.836 -8.156  1.00 17.88 ?  157 ASP   B C    1 
ATOM   6437 O  O    . ASP   B 1 157 ? 46.527 -36.711 -8.062  1.00 17.39 ?  157 ASP   B O    1 
ATOM   6438 C  CB   . ASP   B 1 157 ? 48.310 -36.908 -5.716  1.00 19.66 ?  157 ASP   B CB   1 
ATOM   6439 C  CG   . ASP   B 1 157 ? 48.442 -38.415 -5.703  1.00 21.45 ?  157 ASP   B CG   1 
ATOM   6440 O  OD1  . ASP   B 1 157 ? 48.768 -39.019 -6.752  1.00 21.64 ?  157 ASP   B OD1  1 
ATOM   6441 O  OD2  . ASP   B 1 157 ? 48.225 -38.996 -4.623  1.00 23.37 -1 157 ASP   B OD2  1 
ATOM   6442 H  H    . ASP   B 1 157 ? 48.002 -34.596 -6.334  1.00 20.03 ?  157 ASP   B H    1 
ATOM   6443 H  HA   . ASP   B 1 157 ? 49.591 -36.532 -7.277  1.00 21.57 ?  157 ASP   B HA   1 
ATOM   6444 H  HB2  . ASP   B 1 157 ? 48.886 -36.531 -5.034  1.00 23.64 ?  157 ASP   B HB2  1 
ATOM   6445 H  HB3  . ASP   B 1 157 ? 47.384 -36.693 -5.516  1.00 23.64 ?  157 ASP   B HB3  1 
ATOM   6446 N  N    A LYS   B 1 158 ? 48.350 -37.467 -9.174  0.72 18.79 ?  158 LYS   B N    1 
ATOM   6447 N  N    B LYS   B 1 158 ? 48.354 -37.441 -9.187  0.28 18.46 ?  158 LYS   B N    1 
ATOM   6448 C  CA   A LYS   B 1 158 ? 47.575 -38.086 -10.250 0.72 19.80 ?  158 LYS   B CA   1 
ATOM   6449 C  CA   B LYS   B 1 158 ? 47.583 -38.015 -10.289 0.28 19.24 ?  158 LYS   B CA   1 
ATOM   6450 C  C    A LYS   B 1 158 ? 46.517 -39.045 -9.710  0.72 19.77 ?  158 LYS   B C    1 
ATOM   6451 C  C    B LYS   B 1 158 ? 46.525 -38.992 -9.786  0.28 18.84 ?  158 LYS   B C    1 
ATOM   6452 O  O    A LYS   B 1 158 ? 45.406 -39.124 -10.249 0.72 19.80 ?  158 LYS   B O    1 
ATOM   6453 O  O    B LYS   B 1 158 ? 45.432 -39.086 -10.359 0.28 18.65 ?  158 LYS   B O    1 
ATOM   6454 C  CB   A LYS   B 1 158 ? 48.522 -38.818 -11.208 0.72 21.48 ?  158 LYS   B CB   1 
ATOM   6455 C  CB   B LYS   B 1 158 ? 48.536 -38.704 -11.274 0.28 20.68 ?  158 LYS   B CB   1 
ATOM   6456 C  CG   A LYS   B 1 158 ? 47.842 -39.727 -12.225 0.72 23.66 ?  158 LYS   B CG   1 
ATOM   6457 C  CG   B LYS   B 1 158 ? 47.868 -39.613 -12.302 0.28 22.20 ?  158 LYS   B CG   1 
ATOM   6458 C  CD   A LYS   B 1 158 ? 46.983 -38.951 -13.204 0.72 25.37 ?  158 LYS   B CD   1 
ATOM   6459 C  CD   B LYS   B 1 158 ? 46.968 -38.840 -13.249 0.28 23.58 ?  158 LYS   B CD   1 
ATOM   6460 C  CE   A LYS   B 1 158 ? 46.387 -39.876 -14.253 0.72 26.95 ?  158 LYS   B CE   1 
ATOM   6461 C  CE   B LYS   B 1 158 ? 46.382 -39.756 -14.312 0.28 24.73 ?  158 LYS   B CE   1 
ATOM   6462 N  NZ   A LYS   B 1 158 ? 45.320 -39.210 -15.051 0.72 27.45 ?  158 LYS   B NZ   1 
ATOM   6463 N  NZ   B LYS   B 1 158 ? 45.356 -39.065 -15.143 0.28 25.22 ?  158 LYS   B NZ   1 
ATOM   6464 H  H    A LYS   B 1 158 ? 49.203 -37.560 -9.260  0.72 22.60 ?  158 LYS   B H    1 
ATOM   6465 H  H    B LYS   B 1 158 ? 49.205 -37.532 -9.273  0.28 22.20 ?  158 LYS   B H    1 
ATOM   6466 H  HA   A LYS   B 1 158 ? 47.125 -37.391 -10.756 0.72 23.81 ?  158 LYS   B HA   1 
ATOM   6467 H  HA   B LYS   B 1 158 ? 47.130 -37.303 -10.766 0.28 23.13 ?  158 LYS   B HA   1 
ATOM   6468 H  HB2  A LYS   B 1 158 ? 49.031 -38.159 -11.710 0.72 25.83 ?  158 LYS   B HB2  1 
ATOM   6469 H  HB2  B LYS   B 1 158 ? 49.022 -38.021 -11.768 0.28 24.86 ?  158 LYS   B HB2  1 
ATOM   6470 H  HB3  A LYS   B 1 158 ? 49.130 -39.367 -10.689 0.72 25.83 ?  158 LYS   B HB3  1 
ATOM   6471 H  HB3  B LYS   B 1 158 ? 49.165 -39.247 -10.773 0.28 24.86 ?  158 LYS   B HB3  1 
ATOM   6472 H  HG2  A LYS   B 1 158 ? 48.525 -40.191 -12.735 0.72 28.43 ?  158 LYS   B HG2  1 
ATOM   6473 H  HG2  B LYS   B 1 158 ? 48.557 -40.042 -12.833 0.28 26.68 ?  158 LYS   B HG2  1 
ATOM   6474 H  HG3  A LYS   B 1 158 ? 47.282 -40.377 -11.771 0.72 28.43 ?  158 LYS   B HG3  1 
ATOM   6475 H  HG3  B LYS   B 1 158 ? 47.336 -40.289 -11.853 0.28 26.68 ?  158 LYS   B HG3  1 
ATOM   6476 H  HD2  A LYS   B 1 158 ? 46.257 -38.520 -12.727 0.72 30.49 ?  158 LYS   B HD2  1 
ATOM   6477 H  HD2  B LYS   B 1 158 ? 46.238 -38.445 -12.749 0.28 28.34 ?  158 LYS   B HD2  1 
ATOM   6478 H  HD3  A LYS   B 1 158 ? 47.529 -38.288 -13.657 0.72 30.49 ?  158 LYS   B HD3  1 
ATOM   6479 H  HD3  B LYS   B 1 158 ? 47.487 -38.150 -13.692 0.28 28.34 ?  158 LYS   B HD3  1 
ATOM   6480 H  HE2  A LYS   B 1 158 ? 47.086 -40.157 -14.863 0.72 32.39 ?  158 LYS   B HE2  1 
ATOM   6481 H  HE2  B LYS   B 1 158 ? 47.093 -40.059 -14.899 0.28 29.72 ?  158 LYS   B HE2  1 
ATOM   6482 H  HE3  A LYS   B 1 158 ? 45.999 -40.648 -13.813 0.72 32.39 ?  158 LYS   B HE3  1 
ATOM   6483 H  HE3  B LYS   B 1 158 ? 45.960 -40.516 -13.881 0.28 29.72 ?  158 LYS   B HE3  1 
ATOM   6484 H  HZ1  A LYS   B 1 158 ? 44.991 -39.776 -15.654 0.72 32.99 ?  158 LYS   B HZ1  1 
ATOM   6485 H  HZ1  B LYS   B 1 158 ? 45.032 -39.625 -15.754 0.28 30.31 ?  158 LYS   B HZ1  1 
ATOM   6486 H  HZ2  A LYS   B 1 158 ? 44.660 -38.943 -14.515 0.72 32.99 ?  158 LYS   B HZ2  1 
ATOM   6487 H  HZ2  B LYS   B 1 158 ? 44.688 -38.781 -14.627 0.28 30.31 ?  158 LYS   B HZ2  1 
ATOM   6488 H  HZ3  A LYS   B 1 158 ? 45.653 -38.500 -15.472 0.72 32.99 ?  158 LYS   B HZ3  1 
ATOM   6489 H  HZ3  B LYS   B 1 158 ? 45.720 -38.366 -15.556 0.28 30.31 ?  158 LYS   B HZ3  1 
ATOM   6490 N  N    A ASN   B 1 159 ? 46.846 -39.805 -8.663  0.72 19.86 ?  159 ASN   B N    1 
ATOM   6491 N  N    B ASN   B 1 159 ? 46.832 -39.739 -8.724  0.28 18.89 ?  159 ASN   B N    1 
ATOM   6492 C  CA   A ASN   B 1 159 ? 45.892 -40.785 -8.148  0.72 20.44 ?  159 ASN   B CA   1 
ATOM   6493 C  CA   B ASN   B 1 159 ? 45.885 -40.732 -8.224  0.28 19.14 ?  159 ASN   B CA   1 
ATOM   6494 C  C    A ASN   B 1 159 ? 44.697 -40.110 -7.474  0.72 19.45 ?  159 ASN   B C    1 
ATOM   6495 C  C    B ASN   B 1 159 ? 44.689 -40.072 -7.540  0.28 18.75 ?  159 ASN   B C    1 
ATOM   6496 O  O    A ASN   B 1 159 ? 43.569 -40.612 -7.559  0.72 19.89 ?  159 ASN   B O    1 
ATOM   6497 O  O    B ASN   B 1 159 ? 43.555 -40.552 -7.666  0.28 18.73 ?  159 ASN   B O    1 
ATOM   6498 C  CB   A ASN   B 1 159 ? 46.601 -41.758 -7.206  0.72 21.88 ?  159 ASN   B CB   1 
ATOM   6499 C  CB   B ASN   B 1 159 ? 46.599 -41.716 -7.296  0.28 19.72 ?  159 ASN   B CB   1 
ATOM   6500 C  CG   A ASN   B 1 159 ? 47.623 -42.615 -7.922  0.72 23.81 ?  159 ASN   B CG   1 
ATOM   6501 C  CG   B ASN   B 1 159 ? 47.629 -42.561 -8.028  0.28 20.64 ?  159 ASN   B CG   1 
ATOM   6502 O  OD1  A ASN   B 1 159 ? 47.370 -43.115 -9.025  0.72 24.58 ?  159 ASN   B OD1  1 
ATOM   6503 O  OD1  B ASN   B 1 159 ? 47.402 -42.995 -9.159  0.28 21.00 ?  159 ASN   B OD1  1 
ATOM   6504 N  ND2  A ASN   B 1 159 ? 48.786 -42.794 -7.302  0.72 24.63 ?  159 ASN   B ND2  1 
ATOM   6505 N  ND2  B ASN   B 1 159 ? 48.769 -42.797 -7.386  0.28 21.12 ?  159 ASN   B ND2  1 
ATOM   6506 H  H    A ASN   B 1 159 ? 47.594 -39.761 -8.243  0.72 23.88 ?  159 ASN   B H    1 
ATOM   6507 H  H    B ASN   B 1 159 ? 47.571 -39.694 -8.289  0.28 22.71 ?  159 ASN   B H    1 
ATOM   6508 H  HA   A ASN   B 1 159 ? 45.557 -41.300 -8.899  0.72 24.57 ?  159 ASN   B HA   1 
ATOM   6509 H  HA   B ASN   B 1 159 ? 45.549 -41.242 -8.979  0.28 23.01 ?  159 ASN   B HA   1 
ATOM   6510 H  HB2  A ASN   B 1 159 ? 47.064 -41.257 -6.517  0.72 26.30 ?  159 ASN   B HB2  1 
ATOM   6511 H  HB2  B ASN   B 1 159 ? 47.060 -41.225 -6.600  0.28 23.71 ?  159 ASN   B HB2  1 
ATOM   6512 H  HB3  A ASN   B 1 159 ? 45.946 -42.349 -6.810  0.72 26.30 ?  159 ASN   B HB3  1 
ATOM   6513 H  HB3  B ASN   B 1 159 ? 45.945 -42.316 -6.905  0.28 23.71 ?  159 ASN   B HB3  1 
ATOM   6514 H  HD21 A ASN   B 1 159 ? 49.402 -43.273 -7.666  0.72 29.61 ?  159 ASN   B HD21 1 
ATOM   6515 H  HD21 B ASN   B 1 159 ? 49.384 -43.272 -7.757  0.28 25.39 ?  159 ASN   B HD21 1 
ATOM   6516 H  HD22 A ASN   B 1 159 ? 48.921 -42.442 -6.528  0.72 29.61 ?  159 ASN   B HD22 1 
ATOM   6517 H  HD22 B ASN   B 1 159 ? 48.892 -42.480 -6.596  0.28 25.39 ?  159 ASN   B HD22 1 
ATOM   6518 N  N    . LEU   B 1 160 ? 44.910 -38.968 -6.819  1.00 18.58 ?  160 LEU   B N    1 
ATOM   6519 C  CA   . LEU   B 1 160 ? 43.781 -38.235 -6.258  1.00 17.87 ?  160 LEU   B CA   1 
ATOM   6520 C  C    . LEU   B 1 160 ? 42.983 -37.568 -7.365  1.00 17.01 ?  160 LEU   B C    1 
ATOM   6521 O  O    . LEU   B 1 160 ? 41.746 -37.572 -7.337  1.00 16.61 ?  160 LEU   B O    1 
ATOM   6522 C  CB   . LEU   B 1 160 ? 44.247 -37.208 -5.229  1.00 17.54 ?  160 LEU   B CB   1 
ATOM   6523 C  CG   . LEU   B 1 160 ? 43.117 -36.315 -4.694  1.00 17.24 ?  160 LEU   B CG   1 
ATOM   6524 C  CD1  . LEU   B 1 160 ? 42.005 -37.145 -4.068  1.00 18.06 ?  160 LEU   B CD1  1 
ATOM   6525 C  CD2  . LEU   B 1 160 ? 43.666 -35.308 -3.696  1.00 17.59 ?  160 LEU   B CD2  1 
ATOM   6526 H  H    A LEU   B 1 160 ? 45.681 -38.608 -6.693  0.72 22.35 ?  160 LEU   B H    1 
ATOM   6527 H  H    B LEU   B 1 160 ? 45.685 -38.632 -6.655  0.28 22.35 ?  160 LEU   B H    1 
ATOM   6528 H  HA   . LEU   B 1 160 ? 43.196 -38.866 -5.815  1.00 21.49 ?  160 LEU   B HA   1 
ATOM   6529 H  HB2  . LEU   B 1 160 ? 44.643 -37.683 -4.477  1.00 21.09 ?  160 LEU   B HB2  1 
ATOM   6530 H  HB3  . LEU   B 1 160 ? 44.919 -36.636 -5.639  1.00 21.09 ?  160 LEU   B HB3  1 
ATOM   6531 H  HG   . LEU   B 1 160 ? 42.738 -35.820 -5.433  1.00 20.73 ?  160 LEU   B HG   1 
ATOM   6532 H  HD11 . LEU   B 1 160 ? 41.376 -36.550 -3.637  1.00 21.72 ?  160 LEU   B HD11 1 
ATOM   6533 H  HD12 . LEU   B 1 160 ? 41.556 -37.656 -4.762  1.00 21.72 ?  160 LEU   B HD12 1 
ATOM   6534 H  HD13 . LEU   B 1 160 ? 42.391 -37.751 -3.412  1.00 21.72 ?  160 LEU   B HD13 1 
ATOM   6535 H  HD21 . LEU   B 1 160 ? 42.942 -34.733 -3.407  1.00 21.16 ?  160 LEU   B HD21 1 
ATOM   6536 H  HD22 . LEU   B 1 160 ? 44.037 -35.784 -2.938  1.00 21.16 ?  160 LEU   B HD22 1 
ATOM   6537 H  HD23 . LEU   B 1 160 ? 44.356 -34.781 -4.129  1.00 21.16 ?  160 LEU   B HD23 1 
ATOM   6538 N  N    . TYR   B 1 161 ? 43.675 -36.992 -8.352  1.00 17.28 ?  161 TYR   B N    1 
ATOM   6539 C  CA   . TYR   B 1 161 ? 43.000 -36.426 -9.515  1.00 17.34 ?  161 TYR   B CA   1 
ATOM   6540 C  C    . TYR   B 1 161 ? 42.053 -37.446 -10.134 1.00 16.97 ?  161 TYR   B C    1 
ATOM   6541 O  O    . TYR   B 1 161 ? 40.880 -37.151 -10.391 1.00 16.81 ?  161 TYR   B O    1 
ATOM   6542 C  CB   . TYR   B 1 161 ? 44.040 -35.955 -10.540 1.00 17.74 ?  161 TYR   B CB   1 
ATOM   6543 C  CG   . TYR   B 1 161 ? 43.458 -35.482 -11.854 1.00 18.09 ?  161 TYR   B CG   1 
ATOM   6544 C  CD1  . TYR   B 1 161 ? 43.068 -34.159 -12.021 1.00 18.18 ?  161 TYR   B CD1  1 
ATOM   6545 C  CD2  . TYR   B 1 161 ? 43.284 -36.357 -12.922 1.00 18.58 ?  161 TYR   B CD2  1 
ATOM   6546 C  CE1  . TYR   B 1 161 ? 42.529 -33.719 -13.209 1.00 19.42 ?  161 TYR   B CE1  1 
ATOM   6547 C  CE2  . TYR   B 1 161 ? 42.740 -35.924 -14.115 1.00 19.83 ?  161 TYR   B CE2  1 
ATOM   6548 C  CZ   . TYR   B 1 161 ? 42.368 -34.602 -14.253 1.00 19.84 ?  161 TYR   B CZ   1 
ATOM   6549 O  OH   . TYR   B 1 161 ? 41.823 -34.162 -15.436 1.00 21.82 ?  161 TYR   B OH   1 
ATOM   6550 H  H    . TYR   B 1 161 ? 44.529 -36.926 -8.377  1.00 20.79 ?  161 TYR   B H    1 
ATOM   6551 H  HA   . TYR   B 1 161 ? 42.477 -35.657 -9.242  1.00 20.86 ?  161 TYR   B HA   1 
ATOM   6552 H  HB2  . TYR   B 1 161 ? 44.537 -35.212 -10.159 1.00 21.34 ?  161 TYR   B HB2  1 
ATOM   6553 H  HB3  . TYR   B 1 161 ? 44.644 -36.685 -10.735 1.00 21.34 ?  161 TYR   B HB3  1 
ATOM   6554 H  HD1  . TYR   B 1 161 ? 43.177 -33.553 -11.322 1.00 21.87 ?  161 TYR   B HD1  1 
ATOM   6555 H  HD2  . TYR   B 1 161 ? 43.531 -37.249 -12.834 1.00 22.34 ?  161 TYR   B HD2  1 
ATOM   6556 H  HE1  . TYR   B 1 161 ? 42.276 -32.824 -13.304 1.00 23.36 ?  161 TYR   B HE1  1 
ATOM   6557 H  HE2  . TYR   B 1 161 ? 42.628 -36.517 -14.823 1.00 23.84 ?  161 TYR   B HE2  1 
ATOM   6558 H  HH   . TYR   B 1 161 ? 41.775 -34.799 -15.985 1.00 26.23 ?  161 TYR   B HH   1 
ATOM   6559 N  N    . ASP   B 1 162 ? 42.548 -38.663 -10.367 1.00 17.70 ?  162 ASP   B N    1 
ATOM   6560 C  CA   . ASP   B 1 162 ? 41.717 -39.696 -10.975 1.00 18.15 ?  162 ASP   B CA   1 
ATOM   6561 C  C    . ASP   B 1 162 ? 40.516 -40.033 -10.098 1.00 17.46 ?  162 ASP   B C    1 
ATOM   6562 O  O    . ASP   B 1 162 ? 39.410 -40.246 -10.607 1.00 17.95 ?  162 ASP   B O    1 
ATOM   6563 C  CB   . ASP   B 1 162 ? 42.545 -40.960 -11.225 1.00 19.63 ?  162 ASP   B CB   1 
ATOM   6564 C  CG   . ASP   B 1 162 ? 43.544 -40.807 -12.358 1.00 21.00 ?  162 ASP   B CG   1 
ATOM   6565 O  OD1  . ASP   B 1 162 ? 43.414 -39.866 -13.165 1.00 21.47 ?  162 ASP   B OD1  1 
ATOM   6566 O  OD2  . ASP   B 1 162 ? 44.442 -41.669 -12.462 1.00 22.60 -1 162 ASP   B OD2  1 
ATOM   6567 H  H    . ASP   B 1 162 ? 43.351 -38.904 -10.191 1.00 21.29 ?  162 ASP   B H    1 
ATOM   6568 H  HA   . ASP   B 1 162 ? 41.385 -39.377 -11.827 1.00 21.82 ?  162 ASP   B HA   1 
ATOM   6569 H  HB2  . ASP   B 1 162 ? 43.046 -41.174 -10.425 1.00 23.61 ?  162 ASP   B HB2  1 
ATOM   6570 H  HB3  . ASP   B 1 162 ? 41.949 -41.686 -11.455 1.00 23.61 ?  162 ASP   B HB3  1 
ATOM   6571 N  N    . LYS   B 1 163 ? 40.717 -40.115 -8.781  1.00 17.03 ?  163 LYS   B N    1 
ATOM   6572 C  CA   . LYS   B 1 163 ? 39.598 -40.393 -7.886  1.00 17.76 ?  163 LYS   B CA   1 
ATOM   6573 C  C    . LYS   B 1 163 ? 38.556 -39.280 -7.944  1.00 16.54 ?  163 LYS   B C    1 
ATOM   6574 O  O    . LYS   B 1 163 ? 37.345 -39.546 -7.943  1.00 17.03 ?  163 LYS   B O    1 
ATOM   6575 C  CB   . LYS   B 1 163 ? 40.094 -40.578 -6.454  1.00 21.01 ?  163 LYS   B CB   1 
ATOM   6576 C  CG   . LYS   B 1 163 ? 39.004 -41.055 -5.516  1.00 27.05 ?  163 LYS   B CG   1 
ATOM   6577 C  CD   . LYS   B 1 163 ? 39.485 -41.213 -4.086  1.00 32.62 ?  163 LYS   B CD   1 
ATOM   6578 C  CE   . LYS   B 1 163 ? 38.403 -41.862 -3.233  1.00 36.69 ?  163 LYS   B CE   1 
ATOM   6579 N  NZ   . LYS   B 1 163 ? 38.608 -41.630 -1.777  1.00 39.79 ?  163 LYS   B NZ   1 
ATOM   6580 H  H    . LYS   B 1 163 ? 41.480 -40.011 -8.391  1.00 20.48 ?  163 LYS   B H    1 
ATOM   6581 H  HA   . LYS   B 1 163 ? 39.174 -41.215 -8.165  1.00 21.36 ?  163 LYS   B HA   1 
ATOM   6582 H  HB2  . LYS   B 1 163 ? 40.806 -41.239 -6.448  1.00 25.26 ?  163 LYS   B HB2  1 
ATOM   6583 H  HB3  . LYS   B 1 163 ? 40.427 -39.731 -6.120  1.00 25.26 ?  163 LYS   B HB3  1 
ATOM   6584 H  HG2  . LYS   B 1 163 ? 38.280 -40.412 -5.518  1.00 32.51 ?  163 LYS   B HG2  1 
ATOM   6585 H  HG3  . LYS   B 1 163 ? 38.682 -41.919 -5.823  1.00 32.51 ?  163 LYS   B HG3  1 
ATOM   6586 H  HD2  . LYS   B 1 163 ? 40.271 -41.783 -4.070  1.00 39.20 ?  163 LYS   B HD2  1 
ATOM   6587 H  HD3  . LYS   B 1 163 ? 39.690 -40.342 -3.715  1.00 39.20 ?  163 LYS   B HD3  1 
ATOM   6588 H  HE2  . LYS   B 1 163 ? 37.537 -41.503 -3.482  1.00 44.08 ?  163 LYS   B HE2  1 
ATOM   6589 H  HE3  . LYS   B 1 163 ? 38.415 -42.819 -3.387  1.00 44.08 ?  163 LYS   B HE3  1 
ATOM   6590 H  HZ1  . LYS   B 1 163 ? 37.956 -42.021 -1.313  1.00 47.80 ?  163 LYS   B HZ1  1 
ATOM   6591 H  HZ2  . LYS   B 1 163 ? 39.389 -41.971 -1.524  1.00 47.80 ?  163 LYS   B HZ2  1 
ATOM   6592 H  HZ3  . LYS   B 1 163 ? 38.602 -40.757 -1.605  1.00 47.80 ?  163 LYS   B HZ3  1 
ATOM   6593 N  N    . LEU   B 1 164 ? 39.013 -38.027 -7.996  1.00 15.19 ?  164 LEU   B N    1 
ATOM   6594 C  CA   . LEU   B 1 164 ? 38.101 -36.888 -8.046  1.00 14.99 ?  164 LEU   B CA   1 
ATOM   6595 C  C    . LEU   B 1 164 ? 37.309 -36.870 -9.349  1.00 15.07 ?  164 LEU   B C    1 
ATOM   6596 O  O    . LEU   B 1 164 ? 36.085 -36.675 -9.344  1.00 16.14 ?  164 LEU   B O    1 
ATOM   6597 C  CB   . LEU   B 1 164 ? 38.900 -35.595 -7.888  1.00 14.52 ?  164 LEU   B CB   1 
ATOM   6598 C  CG   . LEU   B 1 164 ? 39.437 -35.326 -6.488  1.00 15.21 ?  164 LEU   B CG   1 
ATOM   6599 C  CD1  . LEU   B 1 164 ? 40.531 -34.263 -6.553  1.00 15.03 ?  164 LEU   B CD1  1 
ATOM   6600 C  CD2  . LEU   B 1 164 ? 38.330 -34.878 -5.557  1.00 17.17 ?  164 LEU   B CD2  1 
ATOM   6601 H  H    . LEU   B 1 164 ? 39.853 -37.808 -8.003  1.00 18.28 ?  164 LEU   B H    1 
ATOM   6602 H  HA   . LEU   B 1 164 ? 37.479 -36.949 -7.313  1.00 18.03 ?  164 LEU   B HA   1 
ATOM   6603 H  HB2  . LEU   B 1 164 ? 39.664 -35.626 -8.491  1.00 17.47 ?  164 LEU   B HB2  1 
ATOM   6604 H  HB3  . LEU   B 1 164 ? 38.332 -34.849 -8.130  1.00 17.47 ?  164 LEU   B HB3  1 
ATOM   6605 H  HG   . LEU   B 1 164 ? 39.832 -36.134 -6.132  1.00 18.30 ?  164 LEU   B HG   1 
ATOM   6606 H  HD11 . LEU   B 1 164 ? 40.864 -34.087 -5.655  1.00 18.08 ?  164 LEU   B HD11 1 
ATOM   6607 H  HD12 . LEU   B 1 164 ? 41.263 -34.586 -7.110  1.00 18.08 ?  164 LEU   B HD12 1 
ATOM   6608 H  HD13 . LEU   B 1 164 ? 40.169 -33.447 -6.933  1.00 18.08 ?  164 LEU   B HD13 1 
ATOM   6609 H  HD21 . LEU   B 1 164 ? 38.707 -34.664 -4.691  1.00 20.65 ?  164 LEU   B HD21 1 
ATOM   6610 H  HD22 . LEU   B 1 164 ? 37.895 -34.096 -5.932  1.00 20.65 ?  164 LEU   B HD22 1 
ATOM   6611 H  HD23 . LEU   B 1 164 ? 37.687 -35.601 -5.468  1.00 20.65 ?  164 LEU   B HD23 1 
ATOM   6612 N  N    . VAL   B 1 165 ? 37.996 -37.038 -10.481 1.00 16.50 ?  165 VAL   B N    1 
ATOM   6613 C  CA   . VAL   B 1 165 ? 37.330 -36.975 -11.777 1.00 18.18 ?  165 VAL   B CA   1 
ATOM   6614 C  C    . VAL   B 1 165 ? 36.405 -38.169 -11.951 1.00 20.23 ?  165 VAL   B C    1 
ATOM   6615 O  O    . VAL   B 1 165 ? 35.237 -38.025 -12.335 1.00 21.70 ?  165 VAL   B O    1 
ATOM   6616 C  CB   . VAL   B 1 165 ? 38.365 -36.904 -12.914 1.00 19.12 ?  165 VAL   B CB   1 
ATOM   6617 C  CG1  . VAL   B 1 165 ? 37.687 -37.027 -14.257 1.00 20.50 ?  165 VAL   B CG1  1 
ATOM   6618 C  CG2  . VAL   B 1 165 ? 39.157 -35.613 -12.835 1.00 18.79 ?  165 VAL   B CG2  1 
ATOM   6619 H  H    . VAL   B 1 165 ? 38.847 -37.178 -10.524 1.00 19.85 ?  165 VAL   B H    1 
ATOM   6620 H  HA   . VAL   B 1 165 ? 36.793 -36.172 -11.819 1.00 21.87 ?  165 VAL   B HA   1 
ATOM   6621 H  HB   . VAL   B 1 165 ? 38.994 -37.636 -12.822 1.00 23.00 ?  165 VAL   B HB   1 
ATOM   6622 H  HG11 . VAL   B 1 165 ? 38.287 -36.711 -14.947 1.00 24.64 ?  165 VAL   B HG11 1 
ATOM   6623 H  HG12 . VAL   B 1 165 ? 37.475 -37.963 -14.413 1.00 24.64 ?  165 VAL   B HG12 1 
ATOM   6624 H  HG13 . VAL   B 1 165 ? 36.876 -36.501 -14.251 1.00 24.64 ?  165 VAL   B HG13 1 
ATOM   6625 H  HG21 . VAL   B 1 165 ? 39.791 -35.581 -13.571 1.00 22.60 ?  165 VAL   B HG21 1 
ATOM   6626 H  HG22 . VAL   B 1 165 ? 38.545 -34.860 -12.899 1.00 22.60 ?  165 VAL   B HG22 1 
ATOM   6627 H  HG23 . VAL   B 1 165 ? 39.633 -35.579 -11.990 1.00 22.60 ?  165 VAL   B HG23 1 
ATOM   6628 N  N    . SER   B 1 166 ? 36.922 -39.370 -11.676 1.00 21.06 ?  166 SER   B N    1 
ATOM   6629 C  CA   . SER   B 1 166 ? 36.172 -40.582 -11.966 1.00 22.14 ?  166 SER   B CA   1 
ATOM   6630 C  C    . SER   B 1 166 ? 34.917 -40.677 -11.114 1.00 22.49 ?  166 SER   B C    1 
ATOM   6631 O  O    . SER   B 1 166 ? 33.947 -41.303 -11.535 1.00 23.95 ?  166 SER   B O    1 
ATOM   6632 C  CB   . SER   B 1 166 ? 37.045 -41.834 -11.800 1.00 23.38 ?  166 SER   B CB   1 
ATOM   6633 O  OG   . SER   B 1 166 ? 37.403 -42.051 -10.445 1.00 23.53 ?  166 SER   B OG   1 
ATOM   6634 H  H    . SER   B 1 166 ? 37.702 -39.508 -11.329 1.00 25.32 ?  166 SER   B H    1 
ATOM   6635 H  HA   . SER   B 1 166 ? 35.893 -40.556 -12.894 1.00 26.62 ?  166 SER   B HA   1 
ATOM   6636 H  HB2  . SER   B 1 166 ? 36.552 -42.608 -12.118 1.00 28.11 ?  166 SER   B HB2  1 
ATOM   6637 H  HB3  . SER   B 1 166 ? 37.853 -41.726 -12.331 1.00 28.11 ?  166 SER   B HB3  1 
ATOM   6638 H  HG   . SER   B 1 166 ? 37.852 -41.398 -10.163 1.00 28.29 ?  166 SER   B HG   1 
ATOM   6639 N  N    . SER   B 1 167 ? 34.901 -40.063 -9.934  1.00 21.00 ?  167 SER   B N    1 
ATOM   6640 C  CA   . SER   B 1 167 ? 33.751 -40.121 -9.039  1.00 20.63 ?  167 SER   B CA   1 
ATOM   6641 C  C    . SER   B 1 167 ? 32.834 -38.901 -9.132  1.00 20.22 ?  167 SER   B C    1 
ATOM   6642 O  O    . SER   B 1 167 ? 31.756 -38.909 -8.529  1.00 20.70 ?  167 SER   B O    1 
ATOM   6643 C  CB   . SER   B 1 167 ? 34.208 -40.306 -7.586  1.00 20.29 ?  167 SER   B CB   1 
ATOM   6644 O  OG   . SER   B 1 167 ? 34.887 -39.149 -7.113  1.00 20.02 ?  167 SER   B OG   1 
ATOM   6645 H  H    . SER   B 1 167 ? 35.551 -39.605 -9.629  1.00 25.25 ?  167 SER   B H    1 
ATOM   6646 H  HA   . SER   B 1 167 ? 33.216 -40.897 -9.273  1.00 24.80 ?  167 SER   B HA   1 
ATOM   6647 H  HB2  . SER   B 1 167 ? 33.428 -40.473 -7.030  1.00 24.40 ?  167 SER   B HB2  1 
ATOM   6648 H  HB3  . SER   B 1 167 ? 34.806 -41.074 -7.543  1.00 24.40 ?  167 SER   B HB3  1 
ATOM   6649 H  HG   . SER   B 1 167 ? 35.563 -39.010 -7.585  1.00 24.08 ?  167 SER   B HG   1 
ATOM   6650 N  N    . PHE   B 1 168 ? 33.209 -37.862 -9.878  1.00 19.74 ?  168 PHE   B N    1 
ATOM   6651 C  CA   . PHE   B 1 168 ? 32.371 -36.662 -9.936  1.00 18.86 ?  168 PHE   B CA   1 
ATOM   6652 C  C    . PHE   B 1 168 ? 31.064 -36.921 -10.681 1.00 16.33 ?  168 PHE   B C    1 
ATOM   6653 O  O    . PHE   B 1 168 ? 30.015 -36.334 -10.348 1.00 16.93 ?  168 PHE   B O    1 
ATOM   6654 C  CB   . PHE   B 1 168 ? 33.131 -35.517 -10.601 1.00 19.55 ?  168 PHE   B CB   1 
ATOM   6655 C  CG   . PHE   B 1 168 ? 32.317 -34.274 -10.744 1.00 19.31 ?  168 PHE   B CG   1 
ATOM   6656 C  CD1  . PHE   B 1 168 ? 31.978 -33.527 -9.623  1.00 20.38 ?  168 PHE   B CD1  1 
ATOM   6657 C  CD2  . PHE   B 1 168 ? 31.877 -33.854 -11.982 1.00 18.42 ?  168 PHE   B CD2  1 
ATOM   6658 C  CE1  . PHE   B 1 168 ? 31.208 -32.384 -9.733  1.00 20.64 ?  168 PHE   B CE1  1 
ATOM   6659 C  CE2  . PHE   B 1 168 ? 31.123 -32.690 -12.107 1.00 19.85 ?  168 PHE   B CE2  1 
ATOM   6660 C  CZ   . PHE   B 1 168 ? 30.783 -31.953 -10.977 1.00 19.93 ?  168 PHE   B CZ   1 
ATOM   6661 H  H    . PHE   B 1 168 ? 33.928 -37.823 -10.347 1.00 23.74 ?  168 PHE   B H    1 
ATOM   6662 H  HA   . PHE   B 1 168 ? 32.147 -36.389 -9.036  1.00 22.68 ?  168 PHE   B HA   1 
ATOM   6663 H  HB2  . PHE   B 1 168 ? 33.909 -35.302 -10.063 1.00 23.51 ?  168 PHE   B HB2  1 
ATOM   6664 H  HB3  . PHE   B 1 168 ? 33.408 -35.790 -11.488 1.00 23.51 ?  168 PHE   B HB3  1 
ATOM   6665 H  HD1  . PHE   B 1 168 ? 32.259 -33.813 -8.784  1.00 24.51 ?  168 PHE   B HD1  1 
ATOM   6666 H  HD2  . PHE   B 1 168 ? 32.105 -34.332 -12.742 1.00 22.15 ?  168 PHE   B HD2  1 
ATOM   6667 H  HE1  . PHE   B 1 168 ? 30.989 -31.896 -8.971  1.00 24.81 ?  168 PHE   B HE1  1 
ATOM   6668 H  HE2  . PHE   B 1 168 ? 30.831 -32.409 -12.947 1.00 23.87 ?  168 PHE   B HE2  1 
ATOM   6669 H  HZ   . PHE   B 1 168 ? 30.266 -31.181 -11.057 1.00 23.97 ?  168 PHE   B HZ   1 
ATOM   6670 N  N    . LEU   B 1 169 ? 31.109 -37.800 -11.680 1.00 16.61 ?  169 LEU   B N    1 
ATOM   6671 C  CA   . LEU   B 1 169 ? 29.936 -38.122 -12.484 1.00 18.74 ?  169 LEU   B CA   1 
ATOM   6672 C  C    . LEU   B 1 169 ? 29.915 -39.561 -12.972 1.00 21.77 ?  169 LEU   B C    1 
ATOM   6673 O  O    . LEU   B 1 169 ? 29.003 -39.971 -13.691 1.00 24.34 ?  169 LEU   B O    1 
ATOM   6674 C  CB   . LEU   B 1 169 ? 29.864 -37.197 -13.697 1.00 20.63 ?  169 LEU   B CB   1 
ATOM   6675 C  CG   . LEU   B 1 169 ? 28.613 -36.328 -13.798 1.00 23.59 ?  169 LEU   B CG   1 
ATOM   6676 C  CD1  . LEU   B 1 169 ? 28.545 -35.687 -15.168 1.00 24.43 ?  169 LEU   B CD1  1 
ATOM   6677 C  CD2  . LEU   B 1 169 ? 27.352 -37.125 -13.515 1.00 23.48 ?  169 LEU   B CD2  1 
ATOM   6678 O  OXT  . LEU   B 1 169 ? 30.814 -40.337 -12.671 1.00 22.64 -1 169 LEU   B OXT  1 
ATOM   6679 H  H    . LEU   B 1 169 ? 31.818 -38.223 -11.922 1.00 19.98 ?  169 LEU   B H    1 
ATOM   6680 H  HA   . LEU   B 1 169 ? 29.150 -37.975 -11.939 1.00 22.54 ?  169 LEU   B HA   1 
ATOM   6681 H  HB2  . LEU   B 1 169 ? 30.629 -36.599 -13.677 1.00 24.80 ?  169 LEU   B HB2  1 
ATOM   6682 H  HB3  . LEU   B 1 169 ? 29.901 -37.738 -14.502 1.00 24.80 ?  169 LEU   B HB3  1 
ATOM   6683 H  HG   . LEU   B 1 169 ? 28.669 -35.615 -13.140 1.00 28.36 ?  169 LEU   B HG   1 
ATOM   6684 H  HD11 . LEU   B 1 169 ? 27.763 -35.114 -15.209 1.00 29.36 ?  169 LEU   B HD11 1 
ATOM   6685 H  HD12 . LEU   B 1 169 ? 29.348 -35.162 -15.308 1.00 29.36 ?  169 LEU   B HD12 1 
ATOM   6686 H  HD13 . LEU   B 1 169 ? 28.482 -36.385 -15.837 1.00 29.36 ?  169 LEU   B HD13 1 
ATOM   6687 H  HD21 . LEU   B 1 169 ? 26.602 -36.703 -13.955 1.00 28.22 ?  169 LEU   B HD21 1 
ATOM   6688 H  HD22 . LEU   B 1 169 ? 27.470 -38.029 -13.853 1.00 28.22 ?  169 LEU   B HD22 1 
ATOM   6689 H  HD23 . LEU   B 1 169 ? 27.205 -37.150 -12.557 1.00 28.22 ?  169 LEU   B HD23 1 
HETATM 6690 C  C1   T TFA   C 2 .   ? 12.094 -1.263  1.462   0.30 12.74 ?  201 TFA   A C1   1 
HETATM 6691 C  C2   T TFA   C 2 .   ? 12.711 -1.698  0.108   0.30 14.83 ?  201 TFA   A C2   1 
HETATM 6692 O  O    T TFA   C 2 .   ? 12.832 -1.517  2.425   0.30 10.69 ?  201 TFA   A O    1 
HETATM 6693 F  F1   T TFA   C 2 .   ? 12.810 -3.039  0.074   0.30 16.16 ?  201 TFA   A F1   1 
HETATM 6694 F  F2   T TFA   C 2 .   ? 11.979 -1.348  -0.961  0.30 15.26 ?  201 TFA   A F2   1 
HETATM 6695 F  F3   T TFA   C 2 .   ? 13.928 -1.189  -0.102  0.30 15.72 ?  201 TFA   A F3   1 
HETATM 6696 O  OXT  T TFA   C 2 .   ? 10.979 -0.736  1.402   0.30 13.51 ?  201 TFA   A OXT  1 
HETATM 6697 N  N2   B A1A8D D 3 .   ? 14.326 -0.340  4.306   0.28 15.08 ?  202 A1A8D A N2   1 
HETATM 6698 C  C3   B A1A8D D 3 .   ? 13.705 -0.834  1.568   0.28 18.52 ?  202 A1A8D A C3   1 
HETATM 6699 C  C6   B A1A8D D 3 .   ? 14.608 -0.100  5.608   0.28 14.65 ?  202 A1A8D A C6   1 
HETATM 6700 C  C9   B A1A8D D 3 .   ? 15.358 3.249   3.365   0.28 11.98 ?  202 A1A8D A C9   1 
HETATM 6701 C  C1   B A1A8D D 3 .   ? 15.264 -0.476  -0.453  0.28 19.15 ?  202 A1A8D A C1   1 
HETATM 6702 C  C10  B A1A8D D 3 .   ? 15.775 4.035   4.448   0.28 11.64 ?  202 A1A8D A C10  1 
HETATM 6703 C  C2   B A1A8D D 3 .   ? 14.819 -1.439  0.637   0.28 19.14 ?  202 A1A8D A C2   1 
HETATM 6704 C  C4   B A1A8D D 3 .   ? 12.372 -0.669  0.807   0.28 19.13 ?  202 A1A8D A C4   1 
HETATM 6705 C  C5   B A1A8D D 3 .   ? 14.521 0.693   3.411   0.28 15.15 ?  202 A1A8D A C5   1 
HETATM 6706 C  C7   B A1A8D D 3 .   ? 15.244 2.021   5.264   0.28 12.28 ?  202 A1A8D A C7   1 
HETATM 6707 C  C8   B A1A8D D 3 .   ? 15.008 1.947   3.881   0.28 12.88 ?  202 A1A8D A C8   1 
HETATM 6708 N  N1   B A1A8D D 3 .   ? 14.227 0.434   2.092   0.28 17.22 ?  202 A1A8D A N1   1 
HETATM 6709 N  N3   B A1A8D D 3 .   ? 15.059 1.019   6.176   0.28 13.50 ?  202 A1A8D A N3   1 
HETATM 6710 N  N4   B A1A8D D 3 .   ? 15.703 3.270   5.622   0.28 10.74 ?  202 A1A8D A N4   1 
HETATM 6711 O  O1   B A1A8D D 3 .   ? 15.939 -1.658  1.460   0.28 19.59 ?  202 A1A8D A O1   1 
HETATM 6712 O  O2   B A1A8D D 3 .   ? 11.447 -0.147  1.716   0.28 19.27 ?  202 A1A8D A O2   1 
HETATM 6713 H  H2   B A1A8D D 3 .   ? 13.545 -1.553  2.398   0.28 22.27 ?  202 A1A8D A H2   1 
HETATM 6714 H  H11  B A1A8D D 3 .   ? 14.450 -0.914  6.341   0.28 17.63 ?  202 A1A8D A H11  1 
HETATM 6715 H  H12  B A1A8D D 3 .   ? 15.322 3.620   2.379   0.28 14.43 ?  202 A1A8D A H12  1 
HETATM 6716 H  H4   B A1A8D D 3 .   ? 16.069 -0.886  -1.075  0.28 23.03 ?  202 A1A8D A H4   1 
HETATM 6717 H  H3   B A1A8D D 3 .   ? 15.651 0.470   -0.034  0.28 23.03 ?  202 A1A8D A H3   1 
HETATM 6718 H  H5   B A1A8D D 3 .   ? 14.464 -0.187  -1.118  0.28 23.03 ?  202 A1A8D A H5   1 
HETATM 6719 H  H13  B A1A8D D 3 .   ? 16.120 5.055   4.497   0.28 14.02 ?  202 A1A8D A H13  1 
HETATM 6720 H  H1   B A1A8D D 3 .   ? 14.467 -2.388  0.165   0.28 23.02 ?  202 A1A8D A H1   1 
HETATM 6721 H  H7   B A1A8D D 3 .   ? 12.020 -1.655  0.437   0.28 23.00 ?  202 A1A8D A H7   1 
HETATM 6722 H  H8   B A1A8D D 3 .   ? 12.480 -0.035  -0.086  0.28 23.00 ?  202 A1A8D A H8   1 
HETATM 6723 H  H10  B A1A8D D 3 .   ? 14.388 1.196   1.435   0.28 20.71 ?  202 A1A8D A H10  1 
HETATM 6724 H  H14  B A1A8D D 3 .   ? 15.948 3.559   6.550   0.28 12.94 ?  202 A1A8D A H14  1 
HETATM 6725 H  H6   B A1A8D D 3 .   ? 16.451 -2.341  1.036   0.28 23.55 ?  202 A1A8D A H6   1 
HETATM 6726 H  H9   B A1A8D D 3 .   ? 10.613 -0.078  1.255   0.28 23.17 ?  202 A1A8D A H9   1 
HETATM 6727 CL CL   B CL    E 4 .   ? 15.815 2.814   -1.211  0.28 16.68 ?  203 CL    A CL   1 
HETATM 6728 O  O    . HOH   F 5 .   ? 7.927  -12.584 -0.847  1.00 21.90 ?  301 HOH   A O    1 
HETATM 6729 O  O    . HOH   F 5 .   ? 14.694 -4.702  20.510  1.00 42.81 ?  302 HOH   A O    1 
HETATM 6730 O  O    . HOH   F 5 .   ? 17.137 -18.046 15.011  1.00 27.15 ?  303 HOH   A O    1 
HETATM 6731 O  O    . HOH   F 5 .   ? 18.578 -2.375  -16.413 1.00 45.67 ?  304 HOH   A O    1 
HETATM 6732 O  O    . HOH   F 5 .   ? 8.841  -11.982 17.197  1.00 49.75 ?  305 HOH   A O    1 
HETATM 6733 O  O    A HOH   F 5 .   ? 4.667  3.919   0.635   0.72 22.22 ?  306 HOH   A O    1 
HETATM 6734 O  O    . HOH   F 5 .   ? 34.301 -1.859  12.515  1.00 38.17 ?  307 HOH   A O    1 
HETATM 6735 O  O    . HOH   F 5 .   ? 7.626  -6.328  -6.654  1.00 39.10 ?  308 HOH   A O    1 
HETATM 6736 O  O    . HOH   F 5 .   ? 11.707 -10.848 -10.069 1.00 44.12 ?  309 HOH   A O    1 
HETATM 6737 O  O    . HOH   F 5 .   ? 14.456 -24.661 11.585  1.00 36.68 ?  310 HOH   A O    1 
HETATM 6738 O  O    . HOH   F 5 .   ? 28.885 0.440   -9.721  1.00 22.52 ?  311 HOH   A O    1 
HETATM 6739 O  O    . HOH   F 5 .   ? 15.076 -12.227 18.638  1.00 40.99 ?  312 HOH   A O    1 
HETATM 6740 O  O    B HOH   F 5 .   ? 15.016 -2.926  3.486   0.28 16.60 ?  313 HOH   A O    1 
HETATM 6741 O  O    . HOH   F 5 .   ? 0.725  -4.442  0.123   1.00 34.39 ?  314 HOH   A O    1 
HETATM 6742 O  O    . HOH   F 5 .   ? 28.167 -6.276  19.612  1.00 40.56 ?  315 HOH   A O    1 
HETATM 6743 O  O    B HOH   F 5 .   ? 8.423  4.079   1.423   0.28 24.14 ?  316 HOH   A O    1 
HETATM 6744 O  O    . HOH   F 5 .   ? 18.945 -21.958 7.032   1.00 33.20 ?  317 HOH   A O    1 
HETATM 6745 O  O    . HOH   F 5 .   ? 14.715 -13.933 16.718  1.00 26.22 ?  318 HOH   A O    1 
HETATM 6746 O  O    . HOH   F 5 .   ? 42.418 10.530  5.140   1.00 20.61 ?  319 HOH   A O    1 
HETATM 6747 O  O    B HOH   F 5 .   ? 4.926  4.280   0.854   0.28 34.60 ?  320 HOH   A O    1 
HETATM 6748 O  O    . HOH   F 5 .   ? 30.874 6.216   -12.277 1.00 27.86 ?  321 HOH   A O    1 
HETATM 6749 O  O    . HOH   F 5 .   ? 30.220 -13.307 -8.519  1.00 22.52 ?  322 HOH   A O    1 
HETATM 6750 O  O    . HOH   F 5 .   ? 36.138 -5.112  -0.517  1.00 31.58 ?  323 HOH   A O    1 
HETATM 6751 O  O    . HOH   F 5 .   ? 14.101 -4.524  -11.887 1.00 32.38 ?  324 HOH   A O    1 
HETATM 6752 O  O    . HOH   F 5 .   ? 27.880 0.816   -7.133  1.00 14.41 ?  325 HOH   A O    1 
HETATM 6753 O  O    . HOH   F 5 .   ? 9.184  -10.106 19.438  1.00 41.43 ?  326 HOH   A O    1 
HETATM 6754 O  O    . HOH   F 5 .   ? 14.973 3.972   17.660  1.00 39.69 ?  327 HOH   A O    1 
HETATM 6755 O  O    . HOH   F 5 .   ? 13.258 -1.459  -6.679  1.00 17.56 ?  328 HOH   A O    1 
HETATM 6756 O  O    . HOH   F 5 .   ? 11.954 0.362   14.803  1.00 34.51 ?  329 HOH   A O    1 
HETATM 6757 O  O    . HOH   F 5 .   ? 19.895 -12.566 -8.850  1.00 26.32 ?  330 HOH   A O    1 
HETATM 6758 O  O    . HOH   F 5 .   ? 22.695 12.487  1.651   1.00 14.74 ?  331 HOH   A O    1 
HETATM 6759 O  O    . HOH   F 5 .   ? 21.247 -2.319  -2.324  1.00 16.50 ?  332 HOH   A O    1 
HETATM 6760 O  O    . HOH   F 5 .   ? 16.984 -19.263 4.912   1.00 15.37 ?  333 HOH   A O    1 
HETATM 6761 O  O    . HOH   F 5 .   ? 33.986 -1.045  -8.905  1.00 28.20 ?  334 HOH   A O    1 
HETATM 6762 O  O    . HOH   F 5 .   ? 37.501 2.823   10.246  1.00 28.28 ?  335 HOH   A O    1 
HETATM 6763 O  O    A HOH   F 5 .   ? 6.932  -8.160  11.866  0.72 18.69 ?  336 HOH   A O    1 
HETATM 6764 O  O    . HOH   F 5 .   ? 26.472 -19.327 -1.751  1.00 14.70 ?  337 HOH   A O    1 
HETATM 6765 O  O    A HOH   F 5 .   ? 14.613 -3.650  3.111   0.72 15.87 ?  338 HOH   A O    1 
HETATM 6766 O  O    . HOH   F 5 .   ? -0.418 -2.960  3.000   1.00 40.12 ?  339 HOH   A O    1 
HETATM 6767 O  O    . HOH   F 5 .   ? 38.240 10.134  7.135   1.00 40.70 ?  340 HOH   A O    1 
HETATM 6768 O  O    . HOH   F 5 .   ? 31.025 -18.113 7.825   1.00 20.69 ?  341 HOH   A O    1 
HETATM 6769 O  O    A HOH   F 5 .   ? 14.254 0.577   6.814   0.72 24.21 ?  342 HOH   A O    1 
HETATM 6770 O  O    . HOH   F 5 .   ? 38.548 4.983   6.971   1.00 16.06 ?  343 HOH   A O    1 
HETATM 6771 O  O    . HOH   F 5 .   ? 27.294 13.760  2.843   1.00 29.55 ?  344 HOH   A O    1 
HETATM 6772 O  O    . HOH   F 5 .   ? 18.676 -19.349 13.585  1.00 38.04 ?  345 HOH   A O    1 
HETATM 6773 O  O    . HOH   F 5 .   ? 9.894  -21.362 5.701   1.00 19.32 ?  346 HOH   A O    1 
HETATM 6774 O  O    . HOH   F 5 .   ? 28.318 -0.143  -13.399 1.00 35.57 ?  347 HOH   A O    1 
HETATM 6775 O  O    . HOH   F 5 .   ? 20.610 -19.723 -5.047  1.00 25.79 ?  348 HOH   A O    1 
HETATM 6776 O  O    . HOH   F 5 .   ? 44.292 7.122   6.416   1.00 26.97 ?  349 HOH   A O    1 
HETATM 6777 O  O    A HOH   F 5 .   ? 3.582  -9.463  9.750   0.72 24.93 ?  350 HOH   A O    1 
HETATM 6778 O  O    . HOH   F 5 .   ? 13.535 -15.256 -7.468  1.00 26.54 ?  351 HOH   A O    1 
HETATM 6779 O  O    . HOH   F 5 .   ? 26.809 11.400  1.674   1.00 16.17 ?  352 HOH   A O    1 
HETATM 6780 O  O    . HOH   F 5 .   ? 22.281 5.367   19.003  1.00 42.39 ?  353 HOH   A O    1 
HETATM 6781 O  O    . HOH   F 5 .   ? 39.718 -1.036  -5.175  1.00 21.28 ?  354 HOH   A O    1 
HETATM 6782 O  O    . HOH   F 5 .   ? 22.176 -19.280 11.400  1.00 35.20 ?  355 HOH   A O    1 
HETATM 6783 O  O    . HOH   F 5 .   ? 28.610 -10.607 -14.004 1.00 40.93 ?  356 HOH   A O    1 
HETATM 6784 O  O    . HOH   F 5 .   ? 42.508 4.264   5.390   1.00 31.21 ?  357 HOH   A O    1 
HETATM 6785 O  O    . HOH   F 5 .   ? 31.664 8.211   14.836  1.00 24.16 ?  358 HOH   A O    1 
HETATM 6786 O  O    . HOH   F 5 .   ? 24.005 -2.121  -2.071  1.00 10.65 ?  359 HOH   A O    1 
HETATM 6787 O  O    . HOH   F 5 .   ? 11.699 -10.733 17.049  1.00 28.11 ?  360 HOH   A O    1 
HETATM 6788 O  O    . HOH   F 5 .   ? 17.141 -17.792 -5.016  1.00 26.84 ?  361 HOH   A O    1 
HETATM 6789 O  O    . HOH   F 5 .   ? -0.716 -8.490  2.106   1.00 47.18 ?  362 HOH   A O    1 
HETATM 6790 O  O    . HOH   F 5 .   ? 35.764 -12.657 6.849   1.00 15.88 ?  363 HOH   A O    1 
HETATM 6791 O  O    . HOH   F 5 .   ? 30.776 3.088   8.287   1.00 12.10 ?  364 HOH   A O    1 
HETATM 6792 O  O    . HOH   F 5 .   ? 14.324 -21.251 -4.185  1.00 29.22 ?  365 HOH   A O    1 
HETATM 6793 O  O    A HOH   F 5 .   ? 8.172  -21.395 4.007   0.72 36.18 ?  366 HOH   A O    1 
HETATM 6794 O  O    . HOH   F 5 .   ? 25.673 -0.825  -7.351  1.00 15.92 ?  367 HOH   A O    1 
HETATM 6795 O  O    . HOH   F 5 .   ? 33.650 -7.154  4.306   1.00 16.70 ?  368 HOH   A O    1 
HETATM 6796 O  O    B HOH   F 5 .   ? 11.027 2.453   11.929  0.28 22.96 ?  369 HOH   A O    1 
HETATM 6797 O  O    . HOH   F 5 .   ? 37.285 11.984  4.947   1.00 30.05 ?  370 HOH   A O    1 
HETATM 6798 O  O    . HOH   F 5 .   ? 37.229 -2.828  9.716   1.00 41.05 ?  371 HOH   A O    1 
HETATM 6799 O  O    . HOH   F 5 .   ? 15.472 11.874  7.900   1.00 39.38 ?  372 HOH   A O    1 
HETATM 6800 O  O    . HOH   F 5 .   ? 31.072 -13.943 -2.443  1.00 14.14 ?  373 HOH   A O    1 
HETATM 6801 O  O    . HOH   F 5 .   ? 27.408 -6.079  -13.973 1.00 36.71 ?  374 HOH   A O    1 
HETATM 6802 O  O    . HOH   F 5 .   ? 43.912 8.443   -3.065  1.00 27.38 ?  375 HOH   A O    1 
HETATM 6803 O  O    . HOH   F 5 .   ? 43.327 7.797   2.692   1.00 26.92 ?  376 HOH   A O    1 
HETATM 6804 O  O    A HOH   F 5 .   ? 11.043 -0.377  1.949   0.42 23.68 ?  377 HOH   A O    1 
HETATM 6805 O  O    . HOH   F 5 .   ? 13.935 -4.906  17.424  1.00 26.87 ?  378 HOH   A O    1 
HETATM 6806 O  O    . HOH   F 5 .   ? 18.534 9.397   9.041   1.00 22.13 ?  379 HOH   A O    1 
HETATM 6807 O  O    . HOH   F 5 .   ? 21.862 -21.900 8.427   1.00 29.23 ?  380 HOH   A O    1 
HETATM 6808 O  O    T HOH   F 5 .   ? 15.383 -0.417  2.400   0.30 14.10 ?  381 HOH   A O    1 
HETATM 6809 O  O    . HOH   F 5 .   ? 14.514 -0.540  -12.125 1.00 24.87 ?  382 HOH   A O    1 
HETATM 6810 O  O    . HOH   F 5 .   ? 31.856 -9.352  -6.646  1.00 22.63 ?  383 HOH   A O    1 
HETATM 6811 O  O    . HOH   F 5 .   ? 24.664 -17.489 12.741  1.00 24.57 ?  384 HOH   A O    1 
HETATM 6812 O  O    . HOH   F 5 .   ? 27.469 -10.601 14.083  1.00 17.82 ?  385 HOH   A O    1 
HETATM 6813 O  O    A HOH   F 5 .   ? 17.471 -1.709  0.454   0.72 19.62 ?  386 HOH   A O    1 
HETATM 6814 O  O    . HOH   F 5 .   ? 6.704  -3.229  12.829  1.00 29.23 ?  387 HOH   A O    1 
HETATM 6815 O  O    . HOH   F 5 .   ? 24.364 3.565   -1.804  1.00 14.72 ?  388 HOH   A O    1 
HETATM 6816 O  O    . HOH   F 5 .   ? 22.653 -11.916 21.820  1.00 47.11 ?  389 HOH   A O    1 
HETATM 6817 O  O    . HOH   F 5 .   ? 31.785 -7.309  -9.839  1.00 21.93 ?  390 HOH   A O    1 
HETATM 6818 O  O    . HOH   F 5 .   ? 15.785 2.110   24.699  1.00 44.04 ?  391 HOH   A O    1 
HETATM 6819 O  O    . HOH   F 5 .   ? 16.514 -22.071 1.022   1.00 28.38 ?  392 HOH   A O    1 
HETATM 6820 O  O    . HOH   F 5 .   ? 15.200 -21.539 14.246  1.00 18.55 ?  393 HOH   A O    1 
HETATM 6821 O  O    B HOH   F 5 .   ? 22.586 5.644   -1.868  0.28 17.95 ?  394 HOH   A O    1 
HETATM 6822 O  O    . HOH   F 5 .   ? 21.295 3.030   -0.259  1.00 13.31 ?  395 HOH   A O    1 
HETATM 6823 O  O    . HOH   F 5 .   ? 24.215 -7.743  14.465  1.00 17.43 ?  396 HOH   A O    1 
HETATM 6824 O  O    . HOH   F 5 .   ? 32.764 -9.238  5.987   1.00 20.05 ?  397 HOH   A O    1 
HETATM 6825 O  O    . HOH   F 5 .   ? 21.184 10.254  15.079  1.00 35.16 ?  398 HOH   A O    1 
HETATM 6826 O  O    . HOH   F 5 .   ? 30.673 1.905   16.705  1.00 21.71 ?  399 HOH   A O    1 
HETATM 6827 O  O    . HOH   F 5 .   ? 37.539 -2.023  5.808   1.00 27.12 ?  400 HOH   A O    1 
HETATM 6828 O  O    . HOH   F 5 .   ? 27.340 2.329   18.715  1.00 31.04 ?  401 HOH   A O    1 
HETATM 6829 O  O    . HOH   F 5 .   ? 18.874 -0.723  -1.667  1.00 14.82 ?  402 HOH   A O    1 
HETATM 6830 O  O    . HOH   F 5 .   ? 20.553 -20.014 2.801   1.00 18.50 ?  403 HOH   A O    1 
HETATM 6831 O  O    A HOH   F 5 .   ? 15.778 -0.941  5.283   0.72 22.46 ?  404 HOH   A O    1 
HETATM 6832 O  O    . HOH   F 5 .   ? 24.526 1.985   -7.030  1.00 20.99 ?  405 HOH   A O    1 
HETATM 6833 O  O    . HOH   F 5 .   ? 23.436 11.360  4.094   1.00 12.57 ?  406 HOH   A O    1 
HETATM 6834 O  O    . HOH   F 5 .   ? 15.155 -8.077  -9.782  1.00 23.72 ?  407 HOH   A O    1 
HETATM 6835 O  O    . HOH   F 5 .   ? 30.044 -10.096 13.016  1.00 22.91 ?  408 HOH   A O    1 
HETATM 6836 O  O    . HOH   F 5 .   ? 23.874 -15.710 -9.118  1.00 37.40 ?  409 HOH   A O    1 
HETATM 6837 O  O    . HOH   F 5 .   ? 19.495 -11.066 24.035  1.00 70.23 ?  410 HOH   A O    1 
HETATM 6838 O  O    A HOH   F 5 .   ? 20.068 4.549   -7.535  0.72 17.83 ?  411 HOH   A O    1 
HETATM 6839 O  O    . HOH   F 5 .   ? 40.869 -8.274  -6.761  1.00 35.34 ?  412 HOH   A O    1 
HETATM 6840 O  O    . HOH   F 5 .   ? 26.904 4.139   -0.652  1.00 12.75 ?  413 HOH   A O    1 
HETATM 6841 O  O    . HOH   F 5 .   ? 14.054 -23.040 7.446   1.00 19.04 ?  414 HOH   A O    1 
HETATM 6842 O  O    . HOH   F 5 .   ? 38.079 -1.344  -1.944  1.00 19.23 ?  415 HOH   A O    1 
HETATM 6843 O  O    . HOH   F 5 .   ? 21.747 -13.829 -8.132  1.00 41.13 ?  416 HOH   A O    1 
HETATM 6844 O  O    B HOH   F 5 .   ? 11.889 -1.676  -3.023  0.28 14.79 ?  417 HOH   A O    1 
HETATM 6845 O  O    . HOH   F 5 .   ? 23.918 -20.279 -1.323  1.00 16.86 ?  418 HOH   A O    1 
HETATM 6846 O  O    . HOH   F 5 .   ? 16.183 16.663  8.636   1.00 33.70 ?  419 HOH   A O    1 
HETATM 6847 O  O    . HOH   F 5 .   ? 15.995 6.881   2.982   1.00 21.25 ?  420 HOH   A O    1 
HETATM 6848 O  O    . HOH   F 5 .   ? 30.324 -12.910 13.530  1.00 20.64 ?  421 HOH   A O    1 
HETATM 6849 O  O    . HOH   F 5 .   ? 32.497 -10.646 3.210   1.00 31.61 ?  422 HOH   A O    1 
HETATM 6850 O  O    . HOH   F 5 .   ? 41.567 1.518   4.982   1.00 38.51 ?  423 HOH   A O    1 
HETATM 6851 O  O    . HOH   F 5 .   ? 35.050 -5.231  -3.085  1.00 18.19 ?  424 HOH   A O    1 
HETATM 6852 O  O    A HOH   F 5 .   ? 24.062 3.966   -4.907  0.72 20.26 ?  425 HOH   A O    1 
HETATM 6853 O  O    . HOH   F 5 .   ? 32.653 -4.352  -9.889  1.00 28.24 ?  426 HOH   A O    1 
HETATM 6854 O  O    . HOH   F 5 .   ? 36.710 -4.963  5.383   1.00 24.90 ?  427 HOH   A O    1 
HETATM 6855 O  O    A HOH   F 5 .   ? 11.017 1.554   12.767  0.72 22.00 ?  428 HOH   A O    1 
HETATM 6856 O  O    . HOH   F 5 .   ? 5.279  2.797   4.948   1.00 30.44 ?  429 HOH   A O    1 
HETATM 6857 O  O    . HOH   F 5 .   ? 10.379 -13.727 -1.672  1.00 17.35 ?  430 HOH   A O    1 
HETATM 6858 O  O    B HOH   F 5 .   ? 16.284 7.623   8.995   0.28 22.01 ?  431 HOH   A O    1 
HETATM 6859 O  O    A HOH   F 5 .   ? 6.449  -5.604  11.196  0.72 19.57 ?  432 HOH   A O    1 
HETATM 6860 O  O    . HOH   F 5 .   ? 22.570 8.140   18.363  1.00 45.42 ?  433 HOH   A O    1 
HETATM 6861 O  O    . HOH   F 5 .   ? 44.953 -0.559  3.048   1.00 42.40 ?  434 HOH   A O    1 
HETATM 6862 O  O    . HOH   F 5 .   ? 16.206 -14.209 20.163  1.00 49.72 ?  435 HOH   A O    1 
HETATM 6863 O  O    . HOH   F 5 .   ? 37.708 -8.823  -3.450  1.00 25.21 ?  436 HOH   A O    1 
HETATM 6864 O  O    . HOH   F 5 .   ? 27.053 -3.145  19.363  1.00 37.19 ?  437 HOH   A O    1 
HETATM 6865 O  O    . HOH   F 5 .   ? 21.295 -9.203  21.332  1.00 51.06 ?  438 HOH   A O    1 
HETATM 6866 O  O    . HOH   F 5 .   ? 10.372 -22.244 -1.161  1.00 51.27 ?  439 HOH   A O    1 
HETATM 6867 O  O    . HOH   F 5 .   ? 23.521 -8.005  17.108  1.00 22.51 ?  440 HOH   A O    1 
HETATM 6868 O  O    A HOH   F 5 .   ? 16.231 2.952   -1.428  0.72 15.41 ?  441 HOH   A O    1 
HETATM 6869 O  O    . HOH   F 5 .   ? 23.337 -20.930 1.348   1.00 19.02 ?  442 HOH   A O    1 
HETATM 6870 O  O    B HOH   F 5 .   ? 23.220 7.883   -3.180  0.28 24.94 ?  443 HOH   A O    1 
HETATM 6871 O  O    . HOH   F 5 .   ? 18.404 -16.000 16.310  1.00 36.68 ?  444 HOH   A O    1 
HETATM 6872 O  O    B HOH   F 5 .   ? 11.409 2.912   1.953   0.28 20.96 ?  445 HOH   A O    1 
HETATM 6873 O  O    . HOH   F 5 .   ? 34.397 -8.066  -0.518  1.00 29.56 ?  446 HOH   A O    1 
HETATM 6874 O  O    . HOH   F 5 .   ? 20.591 -17.746 24.784  1.00 57.67 ?  447 HOH   A O    1 
HETATM 6875 O  O    . HOH   F 5 .   ? 18.463 4.921   -15.103 1.00 48.45 ?  448 HOH   A O    1 
HETATM 6876 O  O    A HOH   F 5 .   ? 14.004 -0.335  3.476   0.42 37.82 ?  449 HOH   A O    1 
HETATM 6877 O  O    . HOH   F 5 .   ? 9.460  -16.272 -1.984  1.00 44.90 ?  450 HOH   A O    1 
HETATM 6878 O  O    . HOH   F 5 .   ? 18.792 1.953   -0.669  1.00 13.43 ?  451 HOH   A O    1 
HETATM 6879 O  O    . HOH   F 5 .   ? 30.559 14.760  2.767   1.00 18.57 ?  452 HOH   A O    1 
HETATM 6880 O  O    A HOH   F 5 .   ? 23.171 7.519   -3.226  0.72 28.75 ?  453 HOH   A O    1 
HETATM 6881 O  O    . HOH   F 5 .   ? 31.326 -12.796 0.036   1.00 20.30 ?  454 HOH   A O    1 
HETATM 6882 O  O    . HOH   F 5 .   ? -1.438 -4.898  7.662   1.00 46.31 ?  455 HOH   A O    1 
HETATM 6883 O  O    . HOH   F 5 .   ? 21.501 -14.736 17.934  1.00 52.55 ?  456 HOH   A O    1 
HETATM 6884 O  O    B HOH   F 5 .   ? 12.973 2.439   -0.076  0.28 18.87 ?  457 HOH   A O    1 
HETATM 6885 O  O    . HOH   F 5 .   ? 29.809 -16.064 10.751  1.00 36.14 ?  458 HOH   A O    1 
HETATM 6886 O  O    . HOH   F 5 .   ? 27.721 7.009   -6.508  1.00 36.34 ?  459 HOH   A O    1 
HETATM 6887 O  O    . HOH   F 5 .   ? 25.369 8.226   -4.837  1.00 27.41 ?  460 HOH   A O    1 
HETATM 6888 O  O    . HOH   F 5 .   ? 32.426 -15.909 10.868  1.00 31.21 ?  461 HOH   A O    1 
HETATM 6889 O  O    . HOH   F 5 .   ? 29.773 -1.926  -12.729 1.00 46.01 ?  462 HOH   A O    1 
HETATM 6890 O  O    . HOH   F 5 .   ? 19.879 -17.354 -5.020  1.00 24.54 ?  463 HOH   A O    1 
HETATM 6891 O  O    . HOH   F 5 .   ? 24.846 5.663   20.749  1.00 50.76 ?  464 HOH   A O    1 
HETATM 6892 O  O    . HOH   F 5 .   ? 23.208 -22.386 -3.305  1.00 35.00 ?  465 HOH   A O    1 
HETATM 6893 O  O    . HOH   F 5 .   ? 24.566 14.622  7.831   1.00 35.30 ?  466 HOH   A O    1 
HETATM 6894 O  O    . HOH   F 5 .   ? 15.709 -21.485 3.701   1.00 23.94 ?  467 HOH   A O    1 
HETATM 6895 O  O    . HOH   F 5 .   ? 26.882 11.588  -1.304  1.00 31.47 ?  468 HOH   A O    1 
HETATM 6896 O  O    B HOH   F 5 .   ? 11.458 0.640   -1.961  0.28 21.44 ?  469 HOH   A O    1 
HETATM 6897 O  O    . HOH   F 5 .   ? 39.605 -7.004  -3.471  1.00 47.51 ?  470 HOH   A O    1 
HETATM 6898 O  O    . HOH   F 5 .   ? 18.732 10.821  11.334  1.00 32.15 ?  471 HOH   A O    1 
HETATM 6899 O  O    . HOH   F 5 .   ? 27.456 -11.332 16.647  1.00 37.94 ?  472 HOH   A O    1 
HETATM 6900 O  O    . HOH   F 5 .   ? 11.960 -13.467 16.389  1.00 54.27 ?  473 HOH   A O    1 
HETATM 6901 O  O    A HOH   F 5 .   ? 21.935 5.273   -5.825  0.72 29.04 ?  474 HOH   A O    1 
HETATM 6902 O  O    . HOH   F 5 .   ? 23.464 13.699  5.544   1.00 18.60 ?  475 HOH   A O    1 
HETATM 6903 O  O    . HOH   F 5 .   ? 11.084 -15.028 -6.106  1.00 33.59 ?  476 HOH   A O    1 
HETATM 6904 O  O    . HOH   F 5 .   ? 12.258 1.651   17.336  1.00 39.16 ?  477 HOH   A O    1 
HETATM 6905 O  O    . HOH   F 5 .   ? 18.103 -16.192 -8.838  1.00 42.49 ?  478 HOH   A O    1 
HETATM 6906 O  O    . HOH   F 5 .   ? 25.811 10.769  -3.704  1.00 24.13 ?  479 HOH   A O    1 
HETATM 6907 O  O    . HOH   F 5 .   ? 16.823 -20.524 16.141  1.00 29.36 ?  480 HOH   A O    1 
HETATM 6908 O  O    . HOH   F 5 .   ? 28.813 8.973   17.515  1.00 37.45 ?  481 HOH   A O    1 
HETATM 6909 O  O    . HOH   F 5 .   ? 13.986 -10.363 -10.896 1.00 33.02 ?  482 HOH   A O    1 
HETATM 6910 O  O    . HOH   F 5 .   ? 15.693 -17.143 -6.997  1.00 31.17 ?  483 HOH   A O    1 
HETATM 6911 O  O    . HOH   F 5 .   ? 35.170 7.489   12.251  1.00 45.30 ?  484 HOH   A O    1 
HETATM 6912 O  O    . HOH   F 5 .   ? 41.010 -3.944  -0.384  1.00 38.94 ?  485 HOH   A O    1 
HETATM 6913 O  O    . HOH   F 5 .   ? 17.374 -18.713 19.827  1.00 52.10 ?  486 HOH   A O    1 
HETATM 6914 O  O    B HOH   F 5 .   ? 10.734 -1.499  -5.598  0.28 17.67 ?  487 HOH   A O    1 
HETATM 6915 O  O    . HOH   F 5 .   ? 20.519 -16.049 -7.369  1.00 29.58 ?  488 HOH   A O    1 
HETATM 6916 O  O    . HOH   F 5 .   ? 23.121 11.826  -4.024  1.00 19.34 ?  489 HOH   A O    1 
HETATM 6917 O  O    . HOH   F 5 .   ? 30.906 0.742   19.145  1.00 39.81 ?  490 HOH   A O    1 
HETATM 6918 O  O    . HOH   F 5 .   ? 23.190 -12.857 19.339  1.00 48.37 ?  491 HOH   A O    1 
HETATM 6919 O  O    . HOH   F 5 .   ? 44.492 10.434  -1.600  1.00 30.55 ?  492 HOH   A O    1 
HETATM 6920 O  O    . HOH   F 5 .   ? 41.696 9.379   -3.960  1.00 31.25 ?  493 HOH   A O    1 
HETATM 6921 O  O    . HOH   F 5 .   ? 28.556 -4.712  -12.286 1.00 37.88 ?  494 HOH   A O    1 
HETATM 6922 O  O    . HOH   F 5 .   ? 39.168 2.410   7.448   1.00 31.98 ?  495 HOH   A O    1 
HETATM 6923 O  O    . HOH   F 5 .   ? 31.413 -0.593  -10.571 1.00 29.94 ?  496 HOH   A O    1 
HETATM 6924 O  O    . HOH   F 5 .   ? 28.669 -7.930  -15.247 1.00 49.16 ?  497 HOH   A O    1 
HETATM 6925 O  O    . HOH   F 5 .   ? 18.469 -23.193 1.897   1.00 46.70 ?  498 HOH   A O    1 
HETATM 6926 O  O    . HOH   F 5 .   ? 16.013 -6.835  -11.868 1.00 45.73 ?  499 HOH   A O    1 
HETATM 6927 O  O    . HOH   F 5 .   ? 20.018 -22.365 4.261   1.00 29.39 ?  500 HOH   A O    1 
HETATM 6928 O  O    . HOH   F 5 .   ? 13.927 -25.236 8.924   1.00 33.68 ?  501 HOH   A O    1 
HETATM 6929 O  O    . HOH   F 5 .   ? 40.520 -0.287  -7.834  1.00 32.86 ?  502 HOH   A O    1 
HETATM 6930 O  O    . HOH   F 5 .   ? 30.640 5.840   -14.731 1.00 35.26 ?  503 HOH   A O    1 
HETATM 6931 O  O    B HOH   F 5 .   ? 10.328 5.613   10.823  0.28 28.39 ?  504 HOH   A O    1 
HETATM 6932 O  O    . HOH   F 5 .   ? 16.161 -23.371 5.752   1.00 27.77 ?  505 HOH   A O    1 
HETATM 6933 O  O    B HOH   F 5 .   ? 5.819  6.849   1.486   0.28 28.95 ?  506 HOH   A O    1 
HETATM 6934 O  O    . HOH   F 5 .   ? 30.724 -5.792  -11.858 1.00 46.38 ?  507 HOH   A O    1 
HETATM 6935 O  O    . HOH   F 5 .   ? 37.379 -6.647  7.614   1.00 24.93 ?  508 HOH   A O    1 
HETATM 6936 O  O    . HOH   F 5 .   ? 23.176 -23.792 1.606   1.00 32.79 ?  509 HOH   A O    1 
HETATM 6937 O  O    . HOH   F 5 .   ? 39.519 -0.003  6.612   1.00 28.52 ?  510 HOH   A O    1 
HETATM 6938 O  O    . HOH   F 5 .   ? 28.965 14.401  0.862   1.00 47.17 ?  511 HOH   A O    1 
HETATM 6939 O  O    . HOH   F 5 .   ? 8.038  -3.064  -5.757  1.00 50.76 ?  512 HOH   A O    1 
HETATM 6940 O  O    . HOH   F 5 .   ? 38.002 13.945  6.686   1.00 42.94 ?  513 HOH   A O    1 
HETATM 6941 O  O    . HOH   F 5 .   ? 14.821 8.354   4.980   1.00 41.89 ?  514 HOH   A O    1 
HETATM 6942 O  O    . HOH   F 5 .   ? 22.025 -24.029 4.484   1.00 26.71 ?  515 HOH   A O    1 
HETATM 6943 O  O    . HOH   F 5 .   ? 36.450 -6.490  10.203  1.00 43.82 ?  516 HOH   A O    1 
HETATM 6944 O  O    T HOH   F 5 .   ? 11.895 -2.145  -3.639  0.30 11.61 ?  517 HOH   A O    1 
HETATM 6945 O  O    . HOH   F 5 .   ? 17.362 -6.664  -14.161 1.00 42.37 ?  518 HOH   A O    1 
HETATM 6946 O  O    B HOH   F 5 .   ? 8.279  7.371   2.386   0.28 28.59 ?  519 HOH   A O    1 
HETATM 6947 O  O    . HOH   F 5 .   ? 24.070 9.020   -7.202  1.00 37.19 ?  520 HOH   A O    1 
HETATM 6948 O  O    . HOH   F 5 .   ? 16.293 -21.156 18.750  1.00 36.19 ?  521 HOH   A O    1 
HETATM 6949 O  O    . HOH   F 5 .   ? 15.805 -12.301 27.386  1.00 44.48 ?  522 HOH   A O    1 
HETATM 6950 O  O    . HOH   F 5 .   ? 14.697 -22.752 19.844  1.00 34.01 ?  523 HOH   A O    1 
HETATM 6951 O  O    . HOH   G 5 .   ? 29.851 -22.429 5.541   1.00 20.40 ?  201 HOH   B O    1 
HETATM 6952 O  O    . HOH   G 5 .   ? 41.717 -35.913 -17.257 1.00 31.16 ?  202 HOH   B O    1 
HETATM 6953 O  O    . HOH   G 5 .   ? 27.862 -41.716 -15.166 1.00 36.25 ?  203 HOH   B O    1 
HETATM 6954 O  O    . HOH   G 5 .   ? 49.336 -22.697 -19.755 1.00 45.33 ?  204 HOH   B O    1 
HETATM 6955 O  O    . HOH   G 5 .   ? 27.732 -29.164 -1.846  1.00 36.34 ?  205 HOH   B O    1 
HETATM 6956 O  O    . HOH   G 5 .   ? 59.135 -18.736 6.794   1.00 37.02 ?  206 HOH   B O    1 
HETATM 6957 O  O    . HOH   G 5 .   ? 52.949 -13.443 -20.259 1.00 33.67 ?  207 HOH   B O    1 
HETATM 6958 O  O    . HOH   G 5 .   ? 48.070 -6.921  15.558  1.00 33.48 ?  208 HOH   B O    1 
HETATM 6959 O  O    . HOH   G 5 .   ? 54.461 -9.404  -8.725  1.00 18.64 ?  209 HOH   B O    1 
HETATM 6960 O  O    . HOH   G 5 .   ? 30.199 -40.969 -8.086  1.00 17.60 ?  210 HOH   B O    1 
HETATM 6961 O  O    . HOH   G 5 .   ? 29.933 -26.302 4.098   1.00 27.32 ?  211 HOH   B O    1 
HETATM 6962 O  O    . HOH   G 5 .   ? 56.344 -19.715 7.252   1.00 32.14 ?  212 HOH   B O    1 
HETATM 6963 O  O    . HOH   G 5 .   ? 41.343 -7.766  5.467   1.00 38.37 ?  213 HOH   B O    1 
HETATM 6964 O  O    . HOH   G 5 .   ? 44.424 -7.227  2.040   1.00 35.47 ?  214 HOH   B O    1 
HETATM 6965 O  O    . HOH   G 5 .   ? 38.040 -39.446 -0.178  1.00 41.54 ?  215 HOH   B O    1 
HETATM 6966 O  O    . HOH   G 5 .   ? 30.944 -28.782 4.370   1.00 28.19 ?  216 HOH   B O    1 
HETATM 6967 O  O    . HOH   G 5 .   ? 58.189 -12.967 8.408   1.00 32.20 ?  217 HOH   B O    1 
HETATM 6968 O  O    . HOH   G 5 .   ? 57.108 -26.880 -7.636  1.00 38.34 ?  218 HOH   B O    1 
HETATM 6969 O  O    . HOH   G 5 .   ? 50.176 -3.392  7.162   1.00 35.99 ?  219 HOH   B O    1 
HETATM 6970 O  O    . HOH   G 5 .   ? 55.325 -16.495 -14.336 1.00 32.57 ?  220 HOH   B O    1 
HETATM 6971 O  O    . HOH   G 5 .   ? 57.707 -24.441 5.052   1.00 36.46 ?  221 HOH   B O    1 
HETATM 6972 O  O    . HOH   G 5 .   ? 47.404 -7.337  -3.844  1.00 38.98 ?  222 HOH   B O    1 
HETATM 6973 O  O    . HOH   G 5 .   ? 50.743 -6.112  0.150   1.00 26.88 ?  223 HOH   B O    1 
HETATM 6974 O  O    . HOH   G 5 .   ? 48.539 -36.506 -15.486 1.00 43.69 ?  224 HOH   B O    1 
HETATM 6975 O  O    . HOH   G 5 .   ? 56.665 -30.752 -7.744  1.00 32.38 ?  225 HOH   B O    1 
HETATM 6976 O  O    . HOH   G 5 .   ? 34.533 -36.389 -7.180  1.00 19.10 ?  226 HOH   B O    1 
HETATM 6977 O  O    . HOH   G 5 .   ? 41.491 -39.139 -14.894 1.00 22.55 ?  227 HOH   B O    1 
HETATM 6978 O  O    . HOH   G 5 .   ? 34.903 -24.670 13.853  1.00 32.40 ?  228 HOH   B O    1 
HETATM 6979 O  O    . HOH   G 5 .   ? 29.791 -34.156 -0.426  1.00 33.91 ?  229 HOH   B O    1 
HETATM 6980 O  O    . HOH   G 5 .   ? 57.376 -16.264 -12.221 1.00 18.85 ?  230 HOH   B O    1 
HETATM 6981 O  O    . HOH   G 5 .   ? 51.651 -6.487  4.392   1.00 19.49 ?  231 HOH   B O    1 
HETATM 6982 O  O    . HOH   G 5 .   ? 25.438 -25.953 -1.281  1.00 33.31 ?  232 HOH   B O    1 
HETATM 6983 O  O    . HOH   G 5 .   ? 40.625 -16.058 14.126  1.00 23.29 ?  233 HOH   B O    1 
HETATM 6984 O  O    . HOH   G 5 .   ? 41.380 -9.633  13.066  1.00 22.71 ?  234 HOH   B O    1 
HETATM 6985 O  O    . HOH   G 5 .   ? 32.772 -43.752 -11.304 1.00 21.45 ?  235 HOH   B O    1 
HETATM 6986 O  O    . HOH   G 5 .   ? 39.296 -10.897 6.135   1.00 25.94 ?  236 HOH   B O    1 
HETATM 6987 O  O    . HOH   G 5 .   ? 44.903 -43.538 -10.530 1.00 28.09 ?  237 HOH   B O    1 
HETATM 6988 O  O    . HOH   G 5 .   ? 35.072 -7.997  -2.985  1.00 17.98 ?  238 HOH   B O    1 
HETATM 6989 O  O    . HOH   G 5 .   ? 37.008 -19.776 -18.155 1.00 40.69 ?  239 HOH   B O    1 
HETATM 6990 O  O    . HOH   G 5 .   ? 50.726 -12.968 -0.464  1.00 12.10 ?  240 HOH   B O    1 
HETATM 6991 O  O    . HOH   G 5 .   ? 42.548 -25.364 2.666   1.00 15.50 ?  241 HOH   B O    1 
HETATM 6992 O  O    . HOH   G 5 .   ? 45.127 -35.013 6.842   1.00 39.56 ?  242 HOH   B O    1 
HETATM 6993 O  O    . HOH   G 5 .   ? 38.447 -11.052 -2.245  1.00 19.78 ?  243 HOH   B O    1 
HETATM 6994 O  O    . HOH   G 5 .   ? 43.047 -43.229 -8.223  1.00 28.75 ?  244 HOH   B O    1 
HETATM 6995 O  O    . HOH   G 5 .   ? 44.510 -27.752 -0.707  1.00 21.70 ?  245 HOH   B O    1 
HETATM 6996 O  O    . HOH   G 5 .   ? 43.132 -32.372 -17.068 1.00 24.10 ?  246 HOH   B O    1 
HETATM 6997 O  O    . HOH   G 5 .   ? 36.013 -43.337 -8.444  1.00 34.28 ?  247 HOH   B O    1 
HETATM 6998 O  O    . HOH   G 5 .   ? 46.377 -1.544  13.233  1.00 28.65 ?  248 HOH   B O    1 
HETATM 6999 O  O    . HOH   G 5 .   ? 42.629 -22.863 3.869   1.00 12.14 ?  249 HOH   B O    1 
HETATM 7000 O  O    . HOH   G 5 .   ? 39.496 -11.121 0.350   1.00 17.13 ?  250 HOH   B O    1 
HETATM 7001 O  O    . HOH   G 5 .   ? 28.358 -19.661 -13.069 1.00 24.47 ?  251 HOH   B O    1 
HETATM 7002 O  O    . HOH   G 5 .   ? 57.615 -24.355 -3.803  1.00 21.12 ?  252 HOH   B O    1 
HETATM 7003 O  O    . HOH   G 5 .   ? 41.848 -23.520 9.301   1.00 18.11 ?  253 HOH   B O    1 
HETATM 7004 O  O    . HOH   G 5 .   ? 40.314 -12.748 -11.502 1.00 15.17 ?  254 HOH   B O    1 
HETATM 7005 O  O    . HOH   G 5 .   ? 34.226 -18.460 11.440  1.00 26.07 ?  255 HOH   B O    1 
HETATM 7006 O  O    . HOH   G 5 .   ? 58.174 -10.637 -4.041  1.00 20.50 ?  256 HOH   B O    1 
HETATM 7007 O  O    . HOH   G 5 .   ? 51.545 -13.831 11.030  1.00 26.41 ?  257 HOH   B O    1 
HETATM 7008 O  O    . HOH   G 5 .   ? 29.708 -25.196 -10.791 1.00 16.94 ?  258 HOH   B O    1 
HETATM 7009 O  O    . HOH   G 5 .   ? 27.117 -31.807 -9.931  1.00 20.68 ?  259 HOH   B O    1 
HETATM 7010 O  O    . HOH   G 5 .   ? 38.915 -11.975 12.379  1.00 34.75 ?  260 HOH   B O    1 
HETATM 7011 O  O    . HOH   G 5 .   ? 33.518 -16.991 8.095   1.00 20.36 ?  261 HOH   B O    1 
HETATM 7012 O  O    . HOH   G 5 .   ? 30.860 -15.731 2.698   1.00 14.29 ?  262 HOH   B O    1 
HETATM 7013 O  O    . HOH   G 5 .   ? 31.788 -17.894 -14.488 1.00 30.98 ?  263 HOH   B O    1 
HETATM 7014 O  O    . HOH   G 5 .   ? 47.910 -24.493 -17.794 1.00 32.22 ?  264 HOH   B O    1 
HETATM 7015 O  O    . HOH   G 5 .   ? 28.447 -30.854 -14.742 1.00 29.92 ?  265 HOH   B O    1 
HETATM 7016 O  O    . HOH   G 5 .   ? 57.481 -9.220  1.410   1.00 20.14 ?  266 HOH   B O    1 
HETATM 7017 O  O    . HOH   G 5 .   ? 42.334 -9.936  9.362   1.00 20.83 ?  267 HOH   B O    1 
HETATM 7018 O  O    . HOH   G 5 .   ? 34.471 -12.793 2.619   1.00 25.63 ?  268 HOH   B O    1 
HETATM 7019 O  O    . HOH   G 5 .   ? 48.012 -22.778 5.851   1.00 17.37 ?  269 HOH   B O    1 
HETATM 7020 O  O    . HOH   G 5 .   ? 49.710 -0.460  10.197  1.00 31.00 ?  270 HOH   B O    1 
HETATM 7021 O  O    . HOH   G 5 .   ? 50.943 -39.949 -8.286  1.00 35.25 ?  271 HOH   B O    1 
HETATM 7022 O  O    . HOH   G 5 .   ? 28.262 -34.334 -9.409  1.00 19.15 ?  272 HOH   B O    1 
HETATM 7023 O  O    . HOH   G 5 .   ? 43.356 -15.769 -12.164 1.00 14.27 ?  273 HOH   B O    1 
HETATM 7024 O  O    . HOH   G 5 .   ? 49.293 -28.695 -6.900  1.00 15.50 ?  274 HOH   B O    1 
HETATM 7025 O  O    . HOH   G 5 .   ? 56.940 -8.625  8.425   1.00 19.86 ?  275 HOH   B O    1 
HETATM 7026 O  O    . HOH   G 5 .   ? 42.388 -34.691 3.785   1.00 27.23 ?  276 HOH   B O    1 
HETATM 7027 O  O    . HOH   G 5 .   ? 46.584 -31.245 -4.800  1.00 25.31 ?  277 HOH   B O    1 
HETATM 7028 O  O    . HOH   G 5 .   ? 27.950 -22.882 -7.965  1.00 17.88 ?  278 HOH   B O    1 
HETATM 7029 O  O    . HOH   G 5 .   ? 56.168 -23.510 -14.734 1.00 27.00 ?  279 HOH   B O    1 
HETATM 7030 O  O    . HOH   G 5 .   ? 30.458 -42.249 -10.590 1.00 29.22 ?  280 HOH   B O    1 
HETATM 7031 O  O    . HOH   G 5 .   ? 42.834 -20.234 -20.727 1.00 38.90 ?  281 HOH   B O    1 
HETATM 7032 O  O    . HOH   G 5 .   ? 59.770 -15.266 8.138   1.00 31.79 ?  282 HOH   B O    1 
HETATM 7033 O  O    . HOH   G 5 .   ? 34.910 -33.341 -19.191 1.00 32.59 ?  283 HOH   B O    1 
HETATM 7034 O  O    . HOH   G 5 .   ? 41.138 -5.550  11.530  1.00 44.10 ?  284 HOH   B O    1 
HETATM 7035 O  O    . HOH   G 5 .   ? 48.404 -25.040 3.115   1.00 13.86 ?  285 HOH   B O    1 
HETATM 7036 O  O    . HOH   G 5 .   ? 45.300 -33.358 -15.941 1.00 24.27 ?  286 HOH   B O    1 
HETATM 7037 O  O    . HOH   G 5 .   ? 27.547 -26.658 -15.616 1.00 32.72 ?  287 HOH   B O    1 
HETATM 7038 O  O    . HOH   G 5 .   ? 52.492 -10.383 13.009  1.00 21.81 ?  288 HOH   B O    1 
HETATM 7039 O  O    . HOH   G 5 .   ? 57.181 -12.055 12.352  1.00 37.14 ?  289 HOH   B O    1 
HETATM 7040 O  O    . HOH   G 5 .   ? 42.727 -12.255 -18.477 1.00 27.90 ?  290 HOH   B O    1 
HETATM 7041 O  O    . HOH   G 5 .   ? 48.696 -20.036 5.951   1.00 14.14 ?  291 HOH   B O    1 
HETATM 7042 O  O    . HOH   G 5 .   ? 36.818 -12.756 -1.495  1.00 26.80 ?  292 HOH   B O    1 
HETATM 7043 O  O    . HOH   G 5 .   ? 51.199 -37.550 -9.668  1.00 27.55 ?  293 HOH   B O    1 
HETATM 7044 O  O    . HOH   G 5 .   ? 46.873 -29.540 9.867   1.00 31.59 ?  294 HOH   B O    1 
HETATM 7045 O  O    . HOH   G 5 .   ? 47.061 -33.958 -4.626  1.00 18.12 ?  295 HOH   B O    1 
HETATM 7046 O  O    . HOH   G 5 .   ? 49.927 -24.669 5.834   1.00 34.21 ?  296 HOH   B O    1 
HETATM 7047 O  O    . HOH   G 5 .   ? 44.611 -27.458 2.026   1.00 15.53 ?  297 HOH   B O    1 
HETATM 7048 O  O    . HOH   G 5 .   ? 33.482 -15.288 -13.930 1.00 21.47 ?  298 HOH   B O    1 
HETATM 7049 O  O    . HOH   G 5 .   ? 52.574 -35.618 -8.684  1.00 29.87 ?  299 HOH   B O    1 
HETATM 7050 O  O    . HOH   G 5 .   ? 37.520 -18.095 13.133  1.00 31.98 ?  300 HOH   B O    1 
HETATM 7051 O  O    . HOH   G 5 .   ? 42.286 -9.909  -14.879 1.00 36.85 ?  301 HOH   B O    1 
HETATM 7052 O  O    . HOH   G 5 .   ? 45.865 -40.382 -3.615  1.00 30.52 ?  302 HOH   B O    1 
HETATM 7053 O  O    . HOH   G 5 .   ? 35.075 -33.565 4.557   1.00 30.74 ?  303 HOH   B O    1 
HETATM 7054 O  O    . HOH   G 5 .   ? 37.326 -35.671 7.281   1.00 33.60 ?  304 HOH   B O    1 
HETATM 7055 O  O    . HOH   G 5 .   ? 53.449 -30.206 4.507   1.00 18.90 ?  305 HOH   B O    1 
HETATM 7056 O  O    . HOH   G 5 .   ? 40.232 -10.838 -9.506  1.00 17.40 ?  306 HOH   B O    1 
HETATM 7057 O  O    . HOH   G 5 .   ? 32.815 -34.594 -5.851  1.00 17.65 ?  307 HOH   B O    1 
HETATM 7058 O  O    . HOH   G 5 .   ? 44.036 -29.351 -4.654  1.00 23.37 ?  308 HOH   B O    1 
HETATM 7059 O  O    . HOH   G 5 .   ? 52.483 -29.221 -13.064 1.00 24.72 ?  309 HOH   B O    1 
HETATM 7060 O  O    . HOH   G 5 .   ? 52.990 -15.988 -12.750 1.00 27.35 ?  310 HOH   B O    1 
HETATM 7061 O  O    . HOH   G 5 .   ? 25.931 -21.479 -3.488  1.00 16.82 ?  311 HOH   B O    1 
HETATM 7062 O  O    . HOH   G 5 .   ? 57.644 -22.080 3.153   1.00 28.90 ?  312 HOH   B O    1 
HETATM 7063 O  O    . HOH   G 5 .   ? 43.211 -21.420 10.685  1.00 16.57 ?  313 HOH   B O    1 
HETATM 7064 O  O    . HOH   G 5 .   ? 37.848 -10.238 -10.743 1.00 17.66 ?  314 HOH   B O    1 
HETATM 7065 O  O    . HOH   G 5 .   ? 62.692 -13.559 4.780   1.00 26.80 ?  315 HOH   B O    1 
HETATM 7066 O  O    . HOH   G 5 .   ? 51.372 -33.021 -10.824 1.00 40.97 ?  316 HOH   B O    1 
HETATM 7067 O  O    . HOH   G 5 .   ? 53.635 -12.571 -22.198 1.00 31.84 ?  317 HOH   B O    1 
HETATM 7068 O  O    . HOH   G 5 .   ? 26.333 -21.036 -6.226  1.00 16.66 ?  318 HOH   B O    1 
HETATM 7069 O  O    . HOH   G 5 .   ? 51.687 -5.987  -7.877  1.00 46.79 ?  319 HOH   B O    1 
HETATM 7070 O  O    . HOH   G 5 .   ? 37.083 -30.565 -21.007 1.00 30.92 ?  320 HOH   B O    1 
HETATM 7071 O  O    . HOH   G 5 .   ? 41.741 -8.058  1.409   1.00 24.64 ?  321 HOH   B O    1 
HETATM 7072 O  O    . HOH   G 5 .   ? 45.678 -36.256 -16.092 1.00 36.17 ?  322 HOH   B O    1 
HETATM 7073 O  O    . HOH   G 5 .   ? 38.328 -12.755 7.935   1.00 18.86 ?  323 HOH   B O    1 
HETATM 7074 O  O    . HOH   G 5 .   ? 62.845 -20.208 -0.762  1.00 37.32 ?  324 HOH   B O    1 
HETATM 7075 O  O    . HOH   G 5 .   ? 48.113 -32.591 -16.681 1.00 43.49 ?  325 HOH   B O    1 
HETATM 7076 O  O    . HOH   G 5 .   ? 38.374 -9.362  -13.265 1.00 27.62 ?  326 HOH   B O    1 
HETATM 7077 O  O    . HOH   G 5 .   ? 43.483 -15.354 18.172  1.00 28.10 ?  327 HOH   B O    1 
HETATM 7078 O  O    . HOH   G 5 .   ? 36.718 -12.414 4.318   1.00 18.40 ?  328 HOH   B O    1 
HETATM 7079 O  O    . HOH   G 5 .   ? 44.611 -24.584 9.594   1.00 20.33 ?  329 HOH   B O    1 
HETATM 7080 O  O    . HOH   G 5 .   ? 44.083 -1.754  7.639   1.00 44.11 ?  330 HOH   B O    1 
HETATM 7081 O  O    . HOH   G 5 .   ? 43.117 -34.579 0.110   1.00 21.38 ?  331 HOH   B O    1 
HETATM 7082 O  O    . HOH   G 5 .   ? 59.939 -17.185 -10.507 1.00 34.21 ?  332 HOH   B O    1 
HETATM 7083 O  O    . HOH   G 5 .   ? 48.562 -11.996 -14.084 1.00 27.18 ?  333 HOH   B O    1 
HETATM 7084 O  O    . HOH   G 5 .   ? 33.650 -31.195 11.097  1.00 35.41 ?  334 HOH   B O    1 
HETATM 7085 O  O    . HOH   G 5 .   ? 47.214 -24.509 8.171   1.00 25.85 ?  335 HOH   B O    1 
HETATM 7086 O  O    . HOH   G 5 .   ? 27.831 -14.761 -9.471  1.00 36.67 ?  336 HOH   B O    1 
HETATM 7087 O  O    . HOH   G 5 .   ? 42.799 -43.491 -14.344 1.00 42.54 ?  337 HOH   B O    1 
HETATM 7088 O  O    . HOH   G 5 .   ? 41.280 -24.542 15.871  1.00 44.13 ?  338 HOH   B O    1 
HETATM 7089 O  O    . HOH   G 5 .   ? 47.460 -27.424 2.030   1.00 15.11 ?  339 HOH   B O    1 
HETATM 7090 O  O    . HOH   G 5 .   ? 36.989 -15.087 -16.511 1.00 39.05 ?  340 HOH   B O    1 
HETATM 7091 O  O    . HOH   G 5 .   ? 46.809 -19.890 12.282  1.00 29.95 ?  341 HOH   B O    1 
HETATM 7092 O  O    . HOH   G 5 .   ? 39.528 -23.557 -20.346 1.00 36.85 ?  342 HOH   B O    1 
HETATM 7093 O  O    . HOH   G 5 .   ? 38.419 -12.236 -16.244 1.00 43.99 ?  343 HOH   B O    1 
HETATM 7094 O  O    . HOH   G 5 .   ? 37.049 -45.160 -9.711  1.00 37.93 ?  344 HOH   B O    1 
HETATM 7095 O  O    . HOH   G 5 .   ? 28.872 -42.912 -12.294 1.00 38.56 ?  345 HOH   B O    1 
HETATM 7096 O  O    . HOH   G 5 .   ? 32.999 -14.689 1.072   1.00 19.86 ?  346 HOH   B O    1 
HETATM 7097 O  O    . HOH   G 5 .   ? 39.793 -44.251 -11.186 1.00 40.60 ?  347 HOH   B O    1 
HETATM 7098 O  O    . HOH   G 5 .   ? 33.652 -9.718  -8.810  1.00 32.32 ?  348 HOH   B O    1 
HETATM 7099 O  O    . HOH   G 5 .   ? 40.400 -43.470 -9.096  1.00 26.85 ?  349 HOH   B O    1 
HETATM 7100 O  O    . HOH   G 5 .   ? 27.761 -26.598 -0.544  1.00 30.12 ?  350 HOH   B O    1 
HETATM 7101 O  O    . HOH   G 5 .   ? 38.551 -22.297 15.054  1.00 40.65 ?  351 HOH   B O    1 
HETATM 7102 O  O    . HOH   G 5 .   ? 44.147 -37.329 -17.826 1.00 33.79 ?  352 HOH   B O    1 
HETATM 7103 O  O    . HOH   G 5 .   ? 55.631 -8.261  10.811  1.00 24.53 ?  353 HOH   B O    1 
HETATM 7104 O  O    . HOH   G 5 .   ? 34.574 -10.324 7.624   1.00 24.56 ?  354 HOH   B O    1 
HETATM 7105 O  O    . HOH   G 5 .   ? 62.609 -20.103 -4.817  1.00 42.75 ?  355 HOH   B O    1 
HETATM 7106 O  O    . HOH   G 5 .   ? 56.564 -7.272  3.080   1.00 26.77 ?  356 HOH   B O    1 
HETATM 7107 O  O    . HOH   G 5 .   ? 23.181 -23.659 6.869   1.00 35.95 ?  357 HOH   B O    1 
HETATM 7108 O  O    . HOH   G 5 .   ? 34.015 -7.799  11.488  1.00 39.59 ?  358 HOH   B O    1 
HETATM 7109 O  O    . HOH   G 5 .   ? 36.114 -8.470  -9.707  1.00 35.78 ?  359 HOH   B O    1 
HETATM 7110 O  O    . HOH   G 5 .   ? 43.182 -12.674 -21.209 1.00 38.29 ?  360 HOH   B O    1 
HETATM 7111 O  O    . HOH   G 5 .   ? 61.470 -19.911 1.667   1.00 35.65 ?  361 HOH   B O    1 
HETATM 7112 O  O    . HOH   G 5 .   ? 56.886 -21.593 -16.339 1.00 39.09 ?  362 HOH   B O    1 
HETATM 7113 O  O    . HOH   G 5 .   ? 40.223 -8.847  9.915   1.00 37.10 ?  363 HOH   B O    1 
HETATM 7114 O  O    . HOH   G 5 .   ? 27.152 -25.925 -11.375 1.00 34.33 ?  364 HOH   B O    1 
HETATM 7115 O  O    . HOH   G 5 .   ? 54.152 -5.748  3.001   1.00 35.64 ?  365 HOH   B O    1 
HETATM 7116 O  O    . HOH   G 5 .   ? 40.189 -11.344 -13.940 1.00 33.44 ?  366 HOH   B O    1 
HETATM 7117 O  O    . HOH   G 5 .   ? 48.342 -26.509 8.822   1.00 39.77 ?  367 HOH   B O    1 
HETATM 7118 O  O    . HOH   G 5 .   ? 32.587 -23.608 14.091  1.00 39.57 ?  368 HOH   B O    1 
HETATM 7119 O  O    . HOH   G 5 .   ? 58.964 -10.450 9.165   1.00 40.24 ?  369 HOH   B O    1 
HETATM 7120 O  O    . HOH   G 5 .   ? 36.193 -8.709  8.997   1.00 38.12 ?  370 HOH   B O    1 
HETATM 7121 O  O    . HOH   G 5 .   ? 39.852 -7.015  7.874   1.00 38.89 ?  371 HOH   B O    1 
HETATM 7122 O  O    . HOH   G 5 .   ? 41.773 -10.053 -17.452 1.00 54.95 ?  372 HOH   B O    1 
HETATM 7123 O  O    . HOH   G 5 .   ? 56.002 -7.785  -0.605  1.00 34.75 ?  373 HOH   B O    1 
HETATM 7124 O  O    . HOH   G 5 .   ? 41.839 -6.743  -4.868  1.00 45.42 ?  374 HOH   B O    1 
HETATM 7125 O  O    . HOH   G 5 .   ? 52.044 -12.899 13.377  1.00 28.85 ?  375 HOH   B O    1 
HETATM 7126 O  O    . HOH   G 5 .   ? 63.027 -12.397 6.966   1.00 37.41 ?  376 HOH   B O    1 
HETATM 7127 O  O    . HOH   G 5 .   ? 36.538 -22.864 13.283  1.00 28.25 ?  377 HOH   B O    1 
HETATM 7128 O  O    . HOH   G 5 .   ? 37.985 -10.543 10.093  1.00 28.84 ?  378 HOH   B O    1 
HETATM 7129 O  O    . HOH   G 5 .   ? 42.612 -17.070 -23.128 1.00 41.75 ?  379 HOH   B O    1 
HETATM 7130 O  O    . HOH   G 5 .   ? 44.037 -5.589  -3.515  1.00 43.18 ?  380 HOH   B O    1 
HETATM 7131 O  O    . HOH   G 5 .   ? 40.130 -7.648  3.188   1.00 38.15 ?  381 HOH   B O    1 
HETATM 7132 O  O    . HOH   G 5 .   ? 39.647 -14.055 15.703  1.00 49.53 ?  382 HOH   B O    1 
HETATM 7133 O  O    . HOH   G 5 .   ? 52.839 -29.919 7.181   1.00 23.63 ?  383 HOH   B O    1 
HETATM 7134 O  O    . HOH   G 5 .   ? 60.475 -22.300 2.822   1.00 47.13 ?  384 HOH   B O    1 
HETATM 7135 O  O    . HOH   G 5 .   ? 46.757 -5.386  2.915   1.00 37.95 ?  385 HOH   B O    1 
HETATM 7136 O  O    . HOH   G 5 .   ? 25.799 -18.941 -11.851 1.00 38.24 ?  386 HOH   B O    1 
HETATM 7137 O  O    . HOH   G 5 .   ? 23.905 -20.870 -7.632  1.00 28.85 ?  387 HOH   B O    1 
HETATM 7138 O  O    . HOH   G 5 .   ? 35.422 -33.777 7.417   1.00 42.65 ?  388 HOH   B O    1 
HETATM 7139 O  O    . HOH   G 5 .   ? 40.912 -9.791  15.818  1.00 45.78 ?  389 HOH   B O    1 
HETATM 7140 O  O    . HOH   G 5 .   ? 35.268 -20.336 13.343  1.00 31.65 ?  390 HOH   B O    1 
HETATM 7141 O  O    . HOH   G 5 .   ? 40.699 -6.632  -0.851  1.00 25.77 ?  391 HOH   B O    1 
HETATM 7142 O  O    . HOH   G 5 .   ? 44.078 -31.743 -3.799  1.00 37.33 ?  392 HOH   B O    1 
HETATM 7143 O  O    . HOH   G 5 .   ? 27.999 -27.106 2.298   1.00 30.60 ?  393 HOH   B O    1 
HETATM 7144 O  O    . HOH   G 5 .   ? 26.606 -27.936 -13.428 1.00 35.41 ?  394 HOH   B O    1 
HETATM 7145 O  O    . HOH   G 5 .   ? 24.597 -20.609 -10.482 1.00 36.43 ?  395 HOH   B O    1 
HETATM 7146 O  O    . HOH   G 5 .   ? 50.640 -30.825 8.719   1.00 29.42 ?  396 HOH   B O    1 
HETATM 7147 O  O    . HOH   G 5 .   ? 26.833 -30.658 -12.625 1.00 29.05 ?  397 HOH   B O    1 
HETATM 7148 O  O    . HOH   G 5 .   ? 34.371 -33.527 9.635   1.00 35.45 ?  398 HOH   B O    1 
HETATM 7149 O  O    . HOH   G 5 .   ? 57.517 -6.450  -2.305  1.00 33.64 ?  399 HOH   B O    1 
HETATM 7150 O  O    . HOH   G 5 .   ? 45.730 -20.099 15.213  1.00 44.67 ?  400 HOH   B O    1 
HETATM 7151 O  O    . HOH   G 5 .   ? 40.856 -11.755 -22.270 1.00 40.78 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   A VAL   A 3   ? 0.6947 0.6991 0.7547 -0.0029 -0.0202 0.0754  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.6923 0.6957 0.7269 -0.0057 -0.0160 0.0519  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.6917 0.6961 0.7464 -0.0039 -0.0195 0.0744  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.6893 0.6931 0.7218 -0.0064 -0.0158 0.0529  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.6750 0.6817 0.7201 -0.0089 -0.0200 0.0734  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.6740 0.6800 0.7056 -0.0104 -0.0176 0.0613  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.6780 0.6849 0.7316 -0.0078 -0.0216 0.0757  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.6773 0.6830 0.7151 -0.0096 -0.0188 0.0619  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.7021 0.7048 0.7565 -0.0012 -0.0175 0.0742  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.6984 0.7009 0.7275 -0.0040 -0.0133 0.0466  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.7059 0.7077 0.7586 -0.0003 -0.0169 0.0743  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.7017 0.7035 0.7287 -0.0033 -0.0125 0.0443  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.7053 0.7074 0.7589 -0.0002 -0.0166 0.0748  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.7012 0.7032 0.7287 -0.0032 -0.0123 0.0447  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.6521 0.6615 0.6742 -0.0157 -0.0174 0.0692  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.6043 0.6198 0.5898 -0.0286 -0.0132 0.0701  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.5400 0.5694 0.5317 -0.0431 0.0007  0.0460  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.5426 0.5714 0.5306 -0.0435 -0.0022 0.0496  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.6168 0.6255 0.5553 -0.0278 -0.0219 0.0939  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.6265 0.6294 0.5228 -0.0283 -0.0293 0.1150  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.6310 0.6305 0.5107 -0.0287 -0.0335 0.1235  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.6289 0.6307 0.5146 -0.0282 -0.0309 0.1243  4   ASN   A ND2 
46   N  N   A SER   A 5   ? 0.4996 0.5444 0.4945 -0.0589 0.0147  0.0331  5   SER   A N   
47   N  N   B SER   A 5   ? 0.5105 0.5378 0.5044 -0.0428 0.0040  0.0328  5   SER   A N   
48   C  CA  A SER   A 5   ? 0.4564 0.5174 0.4562 -0.0739 0.0313  0.0208  5   SER   A CA  
49   C  CA  B SER   A 5   ? 0.4788 0.5046 0.4740 -0.0428 0.0087  0.0202  5   SER   A CA  
50   C  C   A SER   A 5   ? 0.4062 0.4780 0.3985 -0.0877 0.0497  0.0176  5   SER   A C   
51   C  C   B SER   A 5   ? 0.4411 0.4645 0.4214 -0.0425 0.0132  0.0127  5   SER   A C   
52   O  O   A SER   A 5   ? 0.4107 0.4841 0.3974 -0.0826 0.0542  0.0119  5   SER   A O   
53   O  O   B SER   A 5   ? 0.4431 0.4670 0.4231 -0.0413 0.0137  0.0108  5   SER   A O   
54   C  CB  A SER   A 5   ? 0.4627 0.5275 0.4761 -0.0753 0.0310  0.0131  5   SER   A CB  
55   C  CB  B SER   A 5   ? 0.4836 0.5100 0.4931 -0.0433 0.0098  0.0163  5   SER   A CB  
56   O  OG  A SER   A 5   ? 0.4664 0.5329 0.4869 -0.0757 0.0322  0.0087  5   SER   A OG  
57   O  OG  B SER   A 5   ? 0.4864 0.5129 0.5035 -0.0435 0.0107  0.0140  5   SER   A OG  
68   N  N   A PHE   A 6   ? 0.3482 0.4306 0.3367 -0.1064 0.0647  0.0240  6   PHE   A N   
69   N  N   B PHE   A 6   ? 0.3994 0.4209 0.3640 -0.0434 0.0181  0.0088  6   PHE   A N   
70   C  CA  A PHE   A 6   ? 0.2948 0.3824 0.2747 -0.1190 0.0737  0.0401  6   PHE   A CA  
71   C  CA  B PHE   A 6   ? 0.3584 0.3771 0.3087 -0.0436 0.0235  0.0077  6   PHE   A CA  
72   C  C   A PHE   A 6   ? 0.2820 0.3772 0.2677 -0.1210 0.0813  0.0317  6   PHE   A C   
73   C  C   B PHE   A 6   ? 0.3432 0.3602 0.2929 -0.0453 0.0304  0.0023  6   PHE   A C   
74   O  O   A PHE   A 6   ? 0.2885 0.3865 0.2847 -0.1211 0.0898  0.0447  6   PHE   A O   
75   O  O   B PHE   A 6   ? 0.3441 0.3603 0.2829 -0.0473 0.0292  0.0055  6   PHE   A O   
76   C  CB  A PHE   A 6   ? 0.2680 0.3417 0.2431 -0.1149 0.0535  0.0592  6   PHE   A CB  
77   C  CB  B PHE   A 6   ? 0.3356 0.3519 0.2758 -0.0397 0.0192  0.0097  6   PHE   A CB  
78   C  CG  A PHE   A 6   ? 0.2467 0.3119 0.2221 -0.1032 0.0378  0.0597  6   PHE   A CG  
79   C  CG  B PHE   A 6   ? 0.3143 0.3295 0.2513 -0.0365 0.0157  0.0106  6   PHE   A CG  
80   C  CD1 A PHE   A 6   ? 0.2387 0.2995 0.2166 -0.0931 0.0186  0.0545  6   PHE   A CD1 
81   C  CD1 B PHE   A 6   ? 0.3052 0.3197 0.2397 -0.0341 0.0115  0.0109  6   PHE   A CD1 
82   C  CD2 A PHE   A 6   ? 0.2516 0.3063 0.2345 -0.0841 0.0325  0.0585  6   PHE   A CD2 
83   C  CD2 B PHE   A 6   ? 0.3072 0.3205 0.2465 -0.0321 0.0162  0.0104  6   PHE   A CD2 
84   C  CE1 A PHE   A 6   ? 0.2349 0.2926 0.2201 -0.0886 0.0156  0.0526  6   PHE   A CE1 
85   C  CE1 B PHE   A 6   ? 0.2994 0.3135 0.2352 -0.0331 0.0125  0.0108  6   PHE   A CE1 
86   C  CE2 A PHE   A 6   ? 0.2475 0.3009 0.2435 -0.0785 0.0246  0.0479  6   PHE   A CE2 
87   C  CE2 B PHE   A 6   ? 0.3013 0.3144 0.2426 -0.0309 0.0156  0.0087  6   PHE   A CE2 
88   C  CZ  A PHE   A 6   ? 0.2404 0.2931 0.2333 -0.0835 0.0195  0.0486  6   PHE   A CZ  
89   C  CZ  B PHE   A 6   ? 0.2982 0.3118 0.2368 -0.0318 0.0133  0.0084  6   PHE   A CZ  
108  N  N   A SER   A 7   ? 0.2589 0.3609 0.2433 -0.1204 0.0823  0.0141  7   SER   A N   
109  N  N   B SER   A 7   ? 0.3273 0.3426 0.2925 -0.0449 0.0340  -0.0066 7   SER   A N   
110  C  CA  A SER   A 7   ? 0.2587 0.3552 0.2450 -0.1071 0.0697  -0.0147 7   SER   A CA  
111  C  CA  B SER   A 7   ? 0.3147 0.3282 0.2980 -0.0428 0.0306  -0.0179 7   SER   A CA  
112  C  C   A SER   A 7   ? 0.2415 0.3149 0.2058 -0.0985 0.0681  -0.0193 7   SER   A C   
113  C  C   B SER   A 7   ? 0.2978 0.3109 0.2772 -0.0426 0.0324  -0.0158 7   SER   A C   
114  O  O   A SER   A 7   ? 0.2504 0.3058 0.2006 -0.1025 0.0687  -0.0199 7   SER   A O   
115  O  O   B SER   A 7   ? 0.3011 0.3129 0.2792 -0.0414 0.0281  -0.0146 7   SER   A O   
116  C  CB  A SER   A 7   ? 0.2789 0.3817 0.2808 -0.0962 0.0670  -0.0211 7   SER   A CB  
117  C  CB  B SER   A 7   ? 0.3175 0.3307 0.3186 -0.0428 0.0270  -0.0272 7   SER   A CB  
118  O  OG  A SER   A 7   ? 0.2923 0.3858 0.3113 -0.0864 0.0618  -0.0250 7   SER   A OG  
119  O  OG  B SER   A 7   ? 0.3188 0.3319 0.3353 -0.0425 0.0204  -0.0335 7   SER   A OG  
130  N  N   A GLY   A 8   ? 0.2195 0.2842 0.1882 -0.0881 0.0569  -0.0234 8   GLY   A N   
131  N  N   B GLY   A 8   ? 0.2810 0.2945 0.2528 -0.0430 0.0369  -0.0127 8   GLY   A N   
132  C  CA  A GLY   A 8   ? 0.2028 0.2555 0.1927 -0.0680 0.0485  -0.0167 8   GLY   A CA  
133  C  CA  B GLY   A 8   ? 0.2624 0.2755 0.2278 -0.0438 0.0394  -0.0095 8   GLY   A CA  
134  C  C   A GLY   A 8   ? 0.1798 0.2336 0.1831 -0.0453 0.0433  -0.0121 8   GLY   A C   
135  C  C   B GLY   A 8   ? 0.2441 0.2573 0.2062 -0.0441 0.0404  -0.0066 8   GLY   A C   
136  O  O   A GLY   A 8   ? 0.1849 0.2361 0.1989 -0.0269 0.0364  -0.0212 8   GLY   A O   
137  O  O   B GLY   A 8   ? 0.2429 0.2585 0.2010 -0.0428 0.0465  -0.0131 8   GLY   A O   
144  N  N   A TYR   A 9   ? 0.1584 0.2164 0.1789 -0.0312 0.0354  0.0069  9   TYR   A N   
145  N  N   B TYR   A 9   ? 0.2258 0.2374 0.1964 -0.0407 0.0304  -0.0007 9   TYR   A N   
146  C  CA  A TYR   A 9   ? 0.1500 0.1946 0.1603 -0.0380 0.0244  0.0073  9   TYR   A CA  
147  C  CA  B TYR   A 9   ? 0.2119 0.2188 0.1864 -0.0332 0.0288  0.0065  9   TYR   A CA  
148  C  C   A TYR   A 9   ? 0.1514 0.1764 0.1629 -0.0293 0.0299  0.0249  9   TYR   A C   
149  C  C   B TYR   A 9   ? 0.2044 0.1996 0.1757 -0.0297 0.0277  0.0092  9   TYR   A C   
150  O  O   A TYR   A 9   ? 0.1744 0.1890 0.1795 -0.0249 0.0282  0.0155  9   TYR   A O   
151  O  O   B TYR   A 9   ? 0.2117 0.2012 0.1899 -0.0301 0.0215  0.0110  9   TYR   A O   
152  C  CB  A TYR   A 9   ? 0.1462 0.2126 0.1676 -0.0260 0.0228  0.0082  9   TYR   A CB  
153  C  CB  B TYR   A 9   ? 0.2027 0.2196 0.1913 -0.0300 0.0233  0.0044  9   TYR   A CB  
154  C  CG  A TYR   A 9   ? 0.1453 0.2214 0.1792 -0.0198 0.0332  -0.0023 9   TYR   A CG  
155  C  CG  B TYR   A 9   ? 0.1940 0.2205 0.1873 -0.0282 0.0243  0.0018  9   TYR   A CG  
156  C  CD1 A TYR   A 9   ? 0.1510 0.2345 0.1951 -0.0319 0.0372  -0.0127 9   TYR   A CD1 
157  C  CD1 B TYR   A 9   ? 0.1957 0.2253 0.1911 -0.0291 0.0249  -0.0006 9   TYR   A CD1 
158  C  CD2 A TYR   A 9   ? 0.1427 0.2142 0.1817 -0.0119 0.0227  0.0041  9   TYR   A CD2 
159  C  CD2 B TYR   A 9   ? 0.1894 0.2199 0.1828 -0.0266 0.0189  0.0021  9   TYR   A CD2 
160  C  CE1 A TYR   A 9   ? 0.1600 0.2375 0.2151 -0.0340 0.0377  -0.0227 9   TYR   A CE1 
161  C  CE1 B TYR   A 9   ? 0.1966 0.2271 0.1990 -0.0306 0.0233  -0.0035 9   TYR   A CE1 
162  C  CE2 A TYR   A 9   ? 0.1454 0.2217 0.1958 -0.0177 0.0303  -0.0057 9   TYR   A CE2 
163  C  CE2 B TYR   A 9   ? 0.1894 0.2239 0.1922 -0.0263 0.0225  0.0019  9   TYR   A CE2 
164  C  CZ  A TYR   A 9   ? 0.1481 0.2351 0.2195 -0.0367 0.0488  -0.0115 9   TYR   A CZ  
165  C  CZ  B TYR   A 9   ? 0.1948 0.2281 0.2050 -0.0287 0.0276  0.0019  9   TYR   A CZ  
166  O  OH  A TYR   A 9   ? 0.1545 0.2502 0.2441 -0.0573 0.0556  -0.0114 9   TYR   A OH  
167  O  OH  B TYR   A 9   ? 0.2038 0.2358 0.2239 -0.0314 0.0320  0.0068  9   TYR   A OH  
186  N  N   A LEU   A 10  ? 0.1508 0.1595 0.1656 -0.0276 0.0141  0.0208  10  LEU   A N   
187  N  N   B LEU   A 10  ? 0.1956 0.1862 0.1617 -0.0250 0.0264  0.0095  10  LEU   A N   
188  C  CA  A LEU   A 10  ? 0.1431 0.1568 0.1668 -0.0251 0.0192  0.0277  10  LEU   A CA  
189  C  CA  B LEU   A 10  ? 0.1885 0.1809 0.1638 -0.0214 0.0234  0.0044  10  LEU   A CA  
190  C  C   A LEU   A 10  ? 0.1382 0.1488 0.1715 -0.0214 0.0184  0.0345  10  LEU   A C   
191  C  C   B LEU   A 10  ? 0.1800 0.1718 0.1569 -0.0225 0.0163  0.0151  10  LEU   A C   
192  O  O   A LEU   A 10  ? 0.1439 0.1428 0.1909 -0.0191 0.0325  0.0354  10  LEU   A O   
193  O  O   B LEU   A 10  ? 0.1797 0.1699 0.1523 -0.0227 0.0235  0.0240  10  LEU   A O   
194  C  CB  A LEU   A 10  ? 0.1484 0.1569 0.1862 -0.0251 0.0134  0.0358  10  LEU   A CB  
195  C  CB  B LEU   A 10  ? 0.1902 0.1812 0.1780 -0.0211 0.0181  -0.0020 10  LEU   A CB  
196  C  CG  A LEU   A 10  ? 0.1720 0.1670 0.2411 -0.0136 0.0026  0.0251  10  LEU   A CG  
197  C  CG  B LEU   A 10  ? 0.1949 0.1848 0.1976 -0.0158 0.0029  -0.0098 10  LEU   A CG  
198  C  CD1 A LEU   A 10  ? 0.1878 0.1710 0.2710 -0.0234 0.0141  0.0175  10  LEU   A CD1 
199  C  CD1 B LEU   A 10  ? 0.1990 0.1892 0.2103 -0.0222 -0.0041 -0.0146 10  LEU   A CD1 
200  C  CD2 A LEU   A 10  ? 0.1895 0.1881 0.2588 -0.0042 0.0030  0.0143  10  LEU   A CD2 
201  C  CD2 B LEU   A 10  ? 0.2023 0.1885 0.2124 -0.0098 -0.0040 -0.0113 10  LEU   A CD2 
224  N  N   A LYS   A 11  ? 0.1494 0.1513 0.1777 -0.0251 0.0206  0.0368  11  LYS   A N   
225  N  N   B LYS   A 11  ? 0.1809 0.1646 0.1599 -0.0272 -0.0001 0.0141  11  LYS   A N   
226  C  CA  A LYS   A 11  ? 0.1468 0.1481 0.1880 -0.0324 0.0229  0.0342  11  LYS   A CA  
227  C  CA  B LYS   A 11  ? 0.1810 0.1586 0.1623 -0.0224 0.0043  0.0156  11  LYS   A CA  
228  C  C   A LYS   A 11  ? 0.1364 0.1501 0.1879 -0.0282 0.0289  0.0214  11  LYS   A C   
229  C  C   B LYS   A 11  ? 0.1666 0.1455 0.1582 -0.0235 0.0066  0.0062  11  LYS   A C   
230  O  O   A LYS   A 11  ? 0.1441 0.1736 0.2210 -0.0524 0.0314  -0.0009 11  LYS   A O   
231  O  O   B LYS   A 11  ? 0.1626 0.1396 0.1679 -0.0252 0.0126  -0.0168 11  LYS   A O   
232  C  CB  A LYS   A 11  ? 0.1540 0.1487 0.1880 -0.0361 0.0162  0.0206  11  LYS   A CB  
233  C  CB  B LYS   A 11  ? 0.1905 0.1554 0.1637 -0.0197 0.0010  0.0128  11  LYS   A CB  
234  C  CG  A LYS   A 11  ? 0.1701 0.1425 0.1876 -0.0363 0.0213  0.0255  11  LYS   A CG  
235  C  CG  B LYS   A 11  ? 0.1988 0.1572 0.1596 -0.0161 0.0040  0.0205  11  LYS   A CG  
236  C  CD  A LYS   A 11  ? 0.1877 0.1522 0.1861 -0.0357 0.0144  0.0281  11  LYS   A CD  
237  C  CD  B LYS   A 11  ? 0.2049 0.1656 0.1610 -0.0145 0.0077  0.0263  11  LYS   A CD  
238  C  CE  A LYS   A 11  ? 0.1974 0.1508 0.1893 -0.0261 0.0136  0.0317  11  LYS   A CE  
239  C  CE  B LYS   A 11  ? 0.2071 0.1680 0.1595 -0.0098 0.0109  0.0327  11  LYS   A CE  
240  N  NZ  A LYS   A 11  ? 0.1968 0.1476 0.1941 -0.0109 -0.0022 0.0210  11  LYS   A NZ  
241  N  NZ  B LYS   A 11  ? 0.2049 0.1679 0.1506 -0.0036 0.0099  0.0379  11  LYS   A NZ  
268  N  N   A LEU   A 12  ? 0.1275 0.1448 0.1792 -0.0277 0.0209  0.0211  12  LEU   A N   
269  N  N   B LEU   A 12  ? 0.1583 0.1534 0.1582 -0.0070 0.0029  0.0010  12  LEU   A N   
270  C  CA  A LEU   A 12  ? 0.1314 0.1483 0.1773 -0.0210 0.0129  0.0251  12  LEU   A CA  
271  C  CA  B LEU   A 12  ? 0.1558 0.1602 0.1668 -0.0009 0.0074  0.0024  12  LEU   A CA  
272  C  C   A LEU   A 12  ? 0.1364 0.1386 0.1841 -0.0210 0.0144  0.0307  12  LEU   A C   
273  C  C   B LEU   A 12  ? 0.1534 0.1657 0.1688 0.0018  0.0186  0.0064  12  LEU   A C   
274  O  O   A LEU   A 12  ? 0.1394 0.1406 0.1827 -0.0127 0.0213  0.0135  12  LEU   A O   
275  O  O   B LEU   A 12  ? 0.1555 0.1659 0.1631 0.0117  0.0140  0.0018  12  LEU   A O   
276  C  CB  A LEU   A 12  ? 0.1362 0.1442 0.1811 -0.0144 0.0016  0.0270  12  LEU   A CB  
277  C  CB  B LEU   A 12  ? 0.1566 0.1656 0.1789 -0.0006 0.0086  0.0010  12  LEU   A CB  
278  C  CG  A LEU   A 12  ? 0.1458 0.1549 0.2007 -0.0060 0.0097  0.0222  12  LEU   A CG  
279  C  CG  B LEU   A 12  ? 0.1572 0.1693 0.1948 0.0018  0.0130  -0.0020 12  LEU   A CG  
280  C  CD1 A LEU   A 12  ? 0.1578 0.1572 0.1911 0.0081  0.0226  0.0350  12  LEU   A CD1 
281  C  CD1 B LEU   A 12  ? 0.1585 0.1738 0.2074 0.0049  0.0172  -0.0001 12  LEU   A CD1 
282  C  CD2 A LEU   A 12  ? 0.1505 0.1626 0.2292 -0.0028 0.0030  0.0199  12  LEU   A CD2 
283  C  CD2 B LEU   A 12  ? 0.1588 0.1743 0.2004 0.0007  0.0134  -0.0086 12  LEU   A CD2 
306  N  N   A THR   A 13  ? 0.1337 0.1349 0.1999 -0.0193 0.0069  0.0300  13  THR   A N   
307  N  N   B THR   A 13  ? 0.1511 0.1658 0.1827 0.0001  0.0213  0.0140  13  THR   A N   
308  C  CA  A THR   A 13  ? 0.1341 0.1407 0.2056 -0.0172 0.0173  0.0356  13  THR   A CA  
309  C  CA  B THR   A 13  ? 0.1482 0.1681 0.1865 0.0000  0.0267  0.0218  13  THR   A CA  
310  C  C   A THR   A 13  ? 0.1340 0.1445 0.2173 -0.0215 0.0121  0.0492  13  THR   A C   
311  C  C   B THR   A 13  ? 0.1527 0.1764 0.1910 -0.0107 0.0247  0.0198  13  THR   A C   
312  O  O   A THR   A 13  ? 0.1423 0.1494 0.2248 -0.0207 0.0095  0.0481  13  THR   A O   
313  O  O   B THR   A 13  ? 0.1597 0.1806 0.1965 -0.0145 0.0196  0.0220  13  THR   A O   
314  C  CB  A THR   A 13  ? 0.1363 0.1531 0.2184 -0.0103 0.0109  0.0480  13  THR   A CB  
315  C  CB  B THR   A 13  ? 0.1412 0.1711 0.1953 0.0098  0.0252  0.0328  13  THR   A CB  
316  O  OG1 A THR   A 13  ? 0.1373 0.1510 0.2277 -0.0180 0.0002  0.0524  13  THR   A OG1 
317  O  OG1 B THR   A 13  ? 0.1336 0.1738 0.2068 0.0092  0.0400  0.0391  13  THR   A OG1 
318  C  CG2 A THR   A 13  ? 0.1413 0.1795 0.2290 -0.0111 0.0254  0.0375  13  THR   A CG2 
319  C  CG2 B THR   A 13  ? 0.1418 0.1756 0.2031 0.0210  0.0199  0.0343  13  THR   A CG2 
334  N  N   A ASP   A 14  ? 0.1397 0.1468 0.2353 -0.0280 0.0005  0.0645  14  ASP   A N   
335  N  N   B ASP   A 14  ? 0.1530 0.1790 0.1975 -0.0138 0.0145  0.0209  14  ASP   A N   
336  C  CA  A ASP   A 14  ? 0.1485 0.1647 0.2463 -0.0259 -0.0068 0.0696  14  ASP   A CA  
337  C  CA  B ASP   A 14  ? 0.1515 0.1794 0.2001 -0.0144 0.0134  0.0261  14  ASP   A CA  
338  C  C   A ASP   A 14  ? 0.1490 0.1675 0.2265 -0.0224 -0.0096 0.0650  14  ASP   A C   
339  C  C   B ASP   A 14  ? 0.1408 0.1642 0.1779 -0.0071 0.0098  0.0332  14  ASP   A C   
340  O  O   A ASP   A 14  ? 0.1598 0.1720 0.2273 -0.0277 -0.0039 0.0549  14  ASP   A O   
341  O  O   B ASP   A 14  ? 0.1423 0.1636 0.1781 -0.0011 0.0162  0.0274  14  ASP   A O   
342  C  CB  A ASP   A 14  ? 0.1676 0.1863 0.2991 -0.0355 -0.0229 0.0849  14  ASP   A CB  
343  C  CB  B ASP   A 14  ? 0.1629 0.1976 0.2358 -0.0196 0.0084  0.0294  14  ASP   A CB  
344  C  CG  A ASP   A 14  ? 0.1915 0.2380 0.3751 -0.0400 -0.0307 0.0719  14  ASP   A CG  
345  C  CG  B ASP   A 14  ? 0.1656 0.2213 0.2708 -0.0322 0.0047  0.0251  14  ASP   A CG  
346  O  OD1 A ASP   A 14  ? 0.2022 0.2611 0.4023 -0.0275 -0.0526 0.0678  14  ASP   A OD1 
347  O  OD1 B ASP   A 14  ? 0.1701 0.2256 0.2810 -0.0377 0.0087  0.0263  14  ASP   A OD1 
348  O  OD2 A ASP   A 14  ? 0.2070 0.2654 0.4115 -0.0418 -0.0425 0.0504  14  ASP   A OD2 
349  O  OD2 B ASP   A 14  ? 0.1653 0.2369 0.2915 -0.0341 -0.0044 0.0172  14  ASP   A OD2 
358  N  N   A ASN   A 15  ? 0.1408 0.1602 0.2296 -0.0262 0.0031  0.0682  15  ASN   A N   
359  N  N   B ASN   A 15  ? 0.1283 0.1501 0.1654 -0.0108 0.0021  0.0470  15  ASN   A N   
360  C  CA  A ASN   A 15  ? 0.1457 0.1598 0.2383 -0.0227 -0.0097 0.0538  15  ASN   A CA  
361  C  CA  B ASN   A 15  ? 0.1282 0.1489 0.1801 -0.0128 0.0002  0.0354  15  ASN   A CA  
362  C  C   A ASN   A 15  ? 0.1396 0.1505 0.2288 -0.0233 0.0004  0.0416  15  ASN   A C   
363  C  C   B ASN   A 15  ? 0.1323 0.1514 0.1914 -0.0104 0.0138  0.0352  15  ASN   A C   
364  O  O   A ASN   A 15  ? 0.1363 0.1499 0.2175 -0.0236 0.0046  0.0348  15  ASN   A O   
365  O  O   B ASN   A 15  ? 0.1339 0.1564 0.2062 -0.0077 0.0259  0.0287  15  ASN   A O   
366  C  CB  A ASN   A 15  ? 0.1444 0.1600 0.2435 -0.0143 0.0000  0.0578  15  ASN   A CB  
367  C  CB  B ASN   A 15  ? 0.1206 0.1427 0.1765 -0.0188 0.0026  0.0243  15  ASN   A CB  
368  C  CG  A ASN   A 15  ? 0.1463 0.1708 0.2453 -0.0086 0.0133  0.0445  15  ASN   A CG  
369  C  CG  B ASN   A 15  ? 0.1242 0.1499 0.1859 -0.0172 0.0093  0.0058  15  ASN   A CG  
370  O  OD1 A ASN   A 15  ? 0.1558 0.1716 0.2440 -0.0204 0.0220  0.0437  15  ASN   A OD1 
371  O  OD1 B ASN   A 15  ? 0.1327 0.1496 0.1892 -0.0213 0.0096  -0.0050 15  ASN   A OD1 
372  N  ND2 A ASN   A 15  ? 0.1485 0.1804 0.2303 -0.0111 0.0176  0.0545  15  ASN   A ND2 
373  N  ND2 B ASN   A 15  ? 0.1220 0.1552 0.1748 -0.0191 0.0103  0.0036  15  ASN   A ND2 
386  N  N   A VAL   A 16  ? 0.1426 0.1419 0.2357 -0.0143 0.0101  0.0420  16  VAL   A N   
387  N  N   B VAL   A 16  ? 0.1349 0.1500 0.1885 -0.0091 0.0154  0.0463  16  VAL   A N   
388  C  CA  A VAL   A 16  ? 0.1339 0.1454 0.2357 -0.0146 0.0152  0.0400  16  VAL   A CA  
389  C  CA  B VAL   A 16  ? 0.1361 0.1525 0.1793 -0.0084 0.0198  0.0496  16  VAL   A CA  
390  C  C   A VAL   A 16  ? 0.1336 0.1414 0.2181 -0.0172 0.0051  0.0355  16  VAL   A C   
391  C  C   B VAL   A 16  ? 0.1341 0.1594 0.1721 -0.0106 0.0179  0.0453  16  VAL   A C   
392  O  O   A VAL   A 16  ? 0.1278 0.1365 0.2242 -0.0213 0.0150  0.0205  16  VAL   A O   
393  O  O   B VAL   A 16  ? 0.1290 0.1540 0.1759 -0.0072 0.0268  0.0427  16  VAL   A O   
394  C  CB  A VAL   A 16  ? 0.1418 0.1661 0.2396 0.0086  0.0381  0.0420  16  VAL   A CB  
395  C  CB  B VAL   A 16  ? 0.1443 0.1546 0.1730 0.0056  0.0326  0.0501  16  VAL   A CB  
396  C  CG1 A VAL   A 16  ? 0.1564 0.1755 0.2422 0.0172  0.0401  0.0427  16  VAL   A CG1 
397  C  CG1 B VAL   A 16  ? 0.1522 0.1535 0.1744 0.0150  0.0312  0.0512  16  VAL   A CG1 
398  C  CG2 A VAL   A 16  ? 0.1481 0.1756 0.2520 0.0149  0.0470  0.0410  16  VAL   A CG2 
399  C  CG2 B VAL   A 16  ? 0.1467 0.1589 0.1818 0.0078  0.0347  0.0472  16  VAL   A CG2 
418  N  N   A TYR   A 17  ? 0.1341 0.1356 0.2054 -0.0145 0.0180  0.0388  17  TYR   A N   
419  N  N   B TYR   A 17  ? 0.1368 0.1611 0.1603 -0.0166 0.0131  0.0381  17  TYR   A N   
420  C  CA  A TYR   A 17  ? 0.1357 0.1390 0.1910 -0.0245 0.0139  0.0331  17  TYR   A CA  
421  C  CA  B TYR   A 17  ? 0.1354 0.1597 0.1413 -0.0244 0.0033  0.0300  17  TYR   A CA  
422  C  C   A TYR   A 17  ? 0.1346 0.1320 0.1803 -0.0169 0.0119  0.0218  17  TYR   A C   
423  C  C   B TYR   A 17  ? 0.1386 0.1614 0.1400 -0.0305 0.0068  0.0230  17  TYR   A C   
424  O  O   A TYR   A 17  ? 0.1272 0.1303 0.1698 -0.0158 0.0118  0.0294  17  TYR   A O   
425  O  O   B TYR   A 17  ? 0.1355 0.1588 0.1337 -0.0395 0.0006  0.0210  17  TYR   A O   
426  C  CB  A TYR   A 17  ? 0.1544 0.1428 0.1912 -0.0267 0.0013  0.0406  17  TYR   A CB  
427  C  CB  B TYR   A 17  ? 0.1435 0.1632 0.1511 -0.0171 -0.0070 0.0307  17  TYR   A CB  
428  C  CG  A TYR   A 17  ? 0.1752 0.1641 0.2114 -0.0359 -0.0210 0.0461  17  TYR   A CG  
429  C  CG  B TYR   A 17  ? 0.1527 0.1694 0.1557 -0.0124 -0.0142 0.0272  17  TYR   A CG  
430  C  CD1 A TYR   A 17  ? 0.1876 0.1708 0.2327 -0.0275 -0.0327 0.0455  17  TYR   A CD1 
431  C  CD1 B TYR   A 17  ? 0.1600 0.1699 0.1646 -0.0009 -0.0165 0.0337  17  TYR   A CD1 
432  C  CD2 A TYR   A 17  ? 0.1835 0.1734 0.1952 -0.0482 -0.0302 0.0619  17  TYR   A CD2 
433  C  CD2 B TYR   A 17  ? 0.1550 0.1731 0.1577 -0.0111 -0.0117 0.0278  17  TYR   A CD2 
434  C  CE1 A TYR   A 17  ? 0.1915 0.1733 0.2386 -0.0320 -0.0420 0.0498  17  TYR   A CE1 
435  C  CE1 B TYR   A 17  ? 0.1656 0.1737 0.1731 0.0022  -0.0080 0.0373  17  TYR   A CE1 
436  C  CE2 A TYR   A 17  ? 0.1915 0.1740 0.2132 -0.0461 -0.0461 0.0493  17  TYR   A CE2 
437  C  CE2 B TYR   A 17  ? 0.1598 0.1727 0.1655 -0.0024 -0.0054 0.0295  17  TYR   A CE2 
438  C  CZ  A TYR   A 17  ? 0.1985 0.1706 0.2276 -0.0390 -0.0497 0.0536  17  TYR   A CZ  
439  C  CZ  B TYR   A 17  ? 0.1591 0.1728 0.1696 0.0040  -0.0087 0.0367  17  TYR   A CZ  
440  O  OH  A TYR   A 17  ? 0.2127 0.1672 0.2395 -0.0320 -0.0441 0.0486  17  TYR   A OH  
441  O  OH  B TYR   A 17  ? 0.1527 0.1740 0.1770 0.0117  -0.0043 0.0404  17  TYR   A OH  
460  N  N   A ILE   A 18  ? 0.1388 0.1357 0.1700 -0.0162 0.0195  0.0365  18  ILE   A N   
461  N  N   B ILE   A 18  ? 0.1410 0.1665 0.1348 -0.0283 0.0118  0.0192  18  ILE   A N   
462  C  CA  A ILE   A 18  ? 0.1459 0.1319 0.1697 -0.0087 0.0219  0.0262  18  ILE   A CA  
463  C  CA  B ILE   A 18  ? 0.1419 0.1675 0.1251 -0.0200 0.0215  0.0084  18  ILE   A CA  
464  C  C   A ILE   A 18  ? 0.1448 0.1442 0.1779 -0.0227 0.0172  0.0229  18  ILE   A C   
465  C  C   B ILE   A 18  ? 0.1409 0.1795 0.1215 -0.0194 0.0159  0.0025  18  ILE   A C   
466  O  O   A ILE   A 18  ? 0.1413 0.1576 0.1808 -0.0266 0.0223  0.0329  18  ILE   A O   
467  O  O   B ILE   A 18  ? 0.1346 0.1870 0.1310 -0.0210 0.0240  0.0054  18  ILE   A O   
468  C  CB  A ILE   A 18  ? 0.1523 0.1346 0.1537 0.0056  0.0239  0.0341  18  ILE   A CB  
469  C  CB  B ILE   A 18  ? 0.1432 0.1561 0.1194 -0.0169 0.0249  0.0117  18  ILE   A CB  
470  C  CG1 A ILE   A 18  ? 0.1548 0.1462 0.1639 0.0187  0.0083  0.0272  18  ILE   A CG1 
471  C  CG1 B ILE   A 18  ? 0.1571 0.1639 0.1313 -0.0167 0.0285  0.0157  18  ILE   A CG1 
472  C  CG2 A ILE   A 18  ? 0.1571 0.1402 0.1649 -0.0003 0.0218  0.0188  18  ILE   A CG2 
473  C  CG2 B ILE   A 18  ? 0.1472 0.1576 0.1195 -0.0188 0.0258  0.0065  18  ILE   A CG2 
474  C  CD1 A ILE   A 18  ? 0.1800 0.1690 0.1880 0.0209  0.0104  0.0296  18  ILE   A CD1 
475  C  CD1 B ILE   A 18  ? 0.1670 0.1689 0.1524 -0.0171 0.0254  0.0065  18  ILE   A CD1 
498  N  N   A LYS   A 19  ? 0.1447 0.1418 0.1623 -0.0181 0.0357  0.0217  19  LYS   A N   
499  N  N   B LYS   A 19  ? 0.1472 0.1847 0.1343 -0.0142 0.0163  -0.0069 19  LYS   A N   
500  C  CA  A LYS   A 19  ? 0.1604 0.1589 0.1767 -0.0166 0.0394  0.0228  19  LYS   A CA  
501  C  CA  B LYS   A 19  ? 0.1595 0.1950 0.1493 -0.0043 0.0131  -0.0132 19  LYS   A CA  
502  C  C   A LYS   A 19  ? 0.1481 0.1501 0.1887 -0.0111 0.0361  0.0316  19  LYS   A C   
503  C  C   B LYS   A 19  ? 0.1671 0.1978 0.1530 0.0086  0.0189  -0.0175 19  LYS   A C   
504  O  O   A LYS   A 19  ? 0.1482 0.1486 0.2005 -0.0031 0.0327  0.0442  19  LYS   A O   
505  O  O   B LYS   A 19  ? 0.1685 0.1918 0.1507 0.0053  0.0217  -0.0117 19  LYS   A O   
506  C  CB  A LYS   A 19  ? 0.1760 0.1802 0.1958 -0.0227 0.0346  0.0173  19  LYS   A CB  
507  C  CB  B LYS   A 19  ? 0.1572 0.2024 0.1583 -0.0087 0.0203  -0.0159 19  LYS   A CB  
508  C  CG  A LYS   A 19  ? 0.2049 0.1966 0.2017 -0.0255 0.0277  0.0028  19  LYS   A CG  
509  C  CG  B LYS   A 19  ? 0.1669 0.2126 0.1663 -0.0117 0.0186  -0.0173 19  LYS   A CG  
510  C  CD  A LYS   A 19  ? 0.2278 0.2192 0.2139 -0.0310 0.0296  0.0011  19  LYS   A CD  
511  C  CD  B LYS   A 19  ? 0.1770 0.2205 0.1743 -0.0191 0.0136  -0.0142 19  LYS   A CD  
512  C  CE  A LYS   A 19  ? 0.2436 0.2332 0.2205 -0.0420 0.0255  0.0001  19  LYS   A CE  
513  C  CE  B LYS   A 19  ? 0.1825 0.2276 0.1805 -0.0244 0.0134  -0.0139 19  LYS   A CE  
514  N  NZ  A LYS   A 19  ? 0.2570 0.2489 0.2229 -0.0444 0.0290  -0.0107 19  LYS   A NZ  
515  N  NZ  B LYS   A 19  ? 0.1854 0.2303 0.1802 -0.0325 0.0182  -0.0142 19  LYS   A NZ  
542  N  N   A ASN   A 20  ? 0.1520 0.1505 0.2063 -0.0138 0.0366  0.0352  20  ASN   A N   
543  N  N   B ASN   A 20  ? 0.1798 0.2106 0.1723 0.0182  0.0221  -0.0245 20  ASN   A N   
544  C  CA  A ASN   A 20  ? 0.1638 0.1739 0.2226 0.0056  0.0526  0.0306  20  ASN   A CA  
545  C  CA  B ASN   A 20  ? 0.1926 0.2240 0.2027 0.0195  0.0176  -0.0228 20  ASN   A CA  
546  C  C   A ASN   A 20  ? 0.1872 0.1793 0.2404 -0.0024 0.0724  0.0119  20  ASN   A C   
547  C  C   B ASN   A 20  ? 0.2005 0.2196 0.2095 0.0108  0.0222  -0.0327 20  ASN   A C   
548  O  O   A ASN   A 20  ? 0.2143 0.1933 0.2549 -0.0228 0.0783  -0.0108 20  ASN   A O   
549  O  O   B ASN   A 20  ? 0.2103 0.2254 0.2144 -0.0000 0.0205  -0.0448 20  ASN   A O   
550  C  CB  A ASN   A 20  ? 0.1683 0.1910 0.2359 0.0195  0.0591  0.0514  20  ASN   A CB  
551  C  CB  B ASN   A 20  ? 0.2021 0.2384 0.2222 0.0284  0.0122  -0.0183 20  ASN   A CB  
552  C  CG  A ASN   A 20  ? 0.1813 0.2031 0.2691 0.0375  0.0596  0.0741  20  ASN   A CG  
553  C  CG  B ASN   A 20  ? 0.2149 0.2509 0.2435 0.0360  0.0092  -0.0105 20  ASN   A CG  
554  O  OD1 A ASN   A 20  ? 0.2088 0.2159 0.3111 0.0553  0.0683  0.0578  20  ASN   A OD1 
555  O  OD1 B ASN   A 20  ? 0.2266 0.2560 0.2456 0.0407  0.0014  -0.0099 20  ASN   A OD1 
556  N  ND2 A ASN   A 20  ? 0.1740 0.1953 0.2905 0.0371  0.0454  0.0914  20  ASN   A ND2 
557  N  ND2 B ASN   A 20  ? 0.2160 0.2540 0.2558 0.0380  0.0088  -0.0028 20  ASN   A ND2 
570  N  N   A ALA   A 21  ? 0.1863 0.1774 0.2500 0.0036  0.0562  0.0093  21  ALA   A N   
571  N  N   B ALA   A 21  ? 0.2025 0.2118 0.2160 0.0077  0.0200  -0.0262 21  ALA   A N   
572  C  CA  A ALA   A 21  ? 0.1911 0.1737 0.2554 0.0003  0.0535  0.0192  21  ALA   A CA  
573  C  CA  B ALA   A 21  ? 0.2032 0.2039 0.2134 0.0002  0.0298  -0.0153 21  ALA   A CA  
574  C  C   A ALA   A 21  ? 0.1779 0.1746 0.2600 0.0012  0.0406  0.0367  21  ALA   A C   
575  C  C   B ALA   A 21  ? 0.1950 0.1928 0.2056 0.0044  0.0467  -0.0038 21  ALA   A C   
576  O  O   A ALA   A 21  ? 0.1764 0.1755 0.2614 0.0057  0.0257  0.0482  21  ALA   A O   
577  O  O   B ALA   A 21  ? 0.1979 0.1881 0.2089 0.0141  0.0518  -0.0056 21  ALA   A O   
578  C  CB  A ALA   A 21  ? 0.2104 0.1854 0.2681 -0.0073 0.0394  0.0236  21  ALA   A CB  
579  C  CB  B ALA   A 21  ? 0.2099 0.2044 0.2307 -0.0034 0.0266  -0.0139 21  ALA   A CB  
590  N  N   A ASP   A 22  ? 0.1804 0.1742 0.2809 -0.0064 0.0360  0.0445  22  ASP   A N   
591  N  N   B ASP   A 22  ? 0.1872 0.1844 0.2053 -0.0044 0.0521  0.0104  22  ASP   A N   
592  C  CA  A ASP   A 22  ? 0.1866 0.1777 0.2677 -0.0016 0.0241  0.0410  22  ASP   A CA  
593  C  CA  B ASP   A 22  ? 0.1824 0.1750 0.2033 -0.0100 0.0444  0.0212  22  ASP   A CA  
594  C  C   A ASP   A 22  ? 0.1729 0.1830 0.2141 -0.0085 0.0297  0.0319  22  ASP   A C   
595  C  C   B ASP   A 22  ? 0.1706 0.1688 0.1838 -0.0206 0.0467  0.0191  22  ASP   A C   
596  O  O   A ASP   A 22  ? 0.1776 0.1960 0.2168 -0.0097 0.0294  0.0236  22  ASP   A O   
597  O  O   B ASP   A 22  ? 0.1692 0.1703 0.1876 -0.0259 0.0423  0.0019  22  ASP   A O   
598  C  CB  A ASP   A 22  ? 0.2050 0.1835 0.3253 0.0006  0.0147  0.0293  22  ASP   A CB  
599  C  CB  B ASP   A 22  ? 0.1886 0.1756 0.2237 -0.0066 0.0373  0.0244  22  ASP   A CB  
600  C  CG  A ASP   A 22  ? 0.2202 0.1906 0.3819 -0.0025 -0.0077 0.0365  22  ASP   A CG  
601  C  CG  B ASP   A 22  ? 0.1923 0.1732 0.2374 -0.0058 0.0303  0.0276  22  ASP   A CG  
602  O  OD1 A ASP   A 22  ? 0.2154 0.1847 0.4045 -0.0210 -0.0267 0.0494  22  ASP   A OD1 
603  O  OD1 B ASP   A 22  ? 0.1924 0.1658 0.2368 -0.0011 0.0342  0.0288  22  ASP   A OD1 
604  O  OD2 A ASP   A 22  ? 0.2441 0.2053 0.4187 0.0112  -0.0028 0.0331  22  ASP   A OD2 
605  O  OD2 B ASP   A 22  ? 0.1936 0.1797 0.2424 -0.0091 0.0294  0.0236  22  ASP   A OD2 
614  N  N   A ILE   A 23  ? 0.1701 0.1760 0.1924 -0.0019 0.0283  0.0248  23  ILE   A N   
615  N  N   B ILE   A 23  ? 0.1649 0.1651 0.1770 -0.0181 0.0452  0.0240  23  ILE   A N   
616  C  CA  A ILE   A 23  ? 0.1706 0.1704 0.1746 -0.0033 0.0283  0.0258  23  ILE   A CA  
617  C  CA  B ILE   A 23  ? 0.1620 0.1704 0.1598 -0.0150 0.0344  0.0268  23  ILE   A CA  
618  C  C   A ILE   A 23  ? 0.1675 0.1769 0.1722 0.0016  0.0441  0.0185  23  ILE   A C   
619  C  C   B ILE   A 23  ? 0.1667 0.1770 0.1698 -0.0189 0.0305  0.0153  23  ILE   A C   
620  O  O   A ILE   A 23  ? 0.1765 0.1865 0.1766 0.0002  0.0410  0.0048  23  ILE   A O   
621  O  O   B ILE   A 23  ? 0.1637 0.1718 0.1715 -0.0157 0.0249  0.0138  23  ILE   A O   
622  C  CB  A ILE   A 23  ? 0.1857 0.1717 0.1578 -0.0030 0.0264  0.0190  23  ILE   A CB  
623  C  CB  B ILE   A 23  ? 0.1606 0.1660 0.1434 -0.0097 0.0228  0.0353  23  ILE   A CB  
624  C  CG1 A ILE   A 23  ? 0.1983 0.1759 0.1612 0.0033  0.0215  0.0159  23  ILE   A CG1 
625  C  CG1 B ILE   A 23  ? 0.1619 0.1612 0.1398 -0.0086 0.0143  0.0315  23  ILE   A CG1 
626  C  CG2 A ILE   A 23  ? 0.1822 0.1701 0.1556 -0.0039 0.0301  0.0198  23  ILE   A CG2 
627  C  CG2 B ILE   A 23  ? 0.1598 0.1656 0.1390 -0.0084 0.0179  0.0388  23  ILE   A CG2 
628  C  CD1 A ILE   A 23  ? 0.2069 0.1764 0.1760 0.0011  0.0086  0.0073  23  ILE   A CD1 
629  C  CD1 B ILE   A 23  ? 0.1555 0.1593 0.1401 -0.0033 0.0036  0.0224  23  ILE   A CD1 
652  N  N   A VAL   A 24  ? 0.1746 0.1849 0.1916 -0.0082 0.0381  0.0151  24  VAL   A N   
653  N  N   B VAL   A 24  ? 0.1751 0.1852 0.1894 -0.0249 0.0341  0.0058  24  VAL   A N   
654  C  CA  A VAL   A 24  ? 0.1875 0.1963 0.2134 -0.0188 0.0365  0.0013  24  VAL   A CA  
655  C  CA  B VAL   A 24  ? 0.1863 0.1920 0.2003 -0.0301 0.0372  0.0011  24  VAL   A CA  
656  C  C   A VAL   A 24  ? 0.1969 0.2127 0.2152 -0.0285 0.0322  -0.0020 24  VAL   A C   
657  C  C   B VAL   A 24  ? 0.1938 0.2092 0.2030 -0.0321 0.0387  -0.0072 24  VAL   A C   
658  O  O   A VAL   A 24  ? 0.2107 0.2182 0.2192 -0.0279 0.0340  -0.0040 24  VAL   A O   
659  O  O   B VAL   A 24  ? 0.2002 0.2146 0.2144 -0.0277 0.0391  -0.0048 24  VAL   A O   
660  C  CB  A VAL   A 24  ? 0.1916 0.2000 0.2363 -0.0152 0.0488  0.0038  24  VAL   A CB  
661  C  CB  B VAL   A 24  ? 0.1902 0.1890 0.2164 -0.0271 0.0352  0.0029  24  VAL   A CB  
662  C  CG1 A VAL   A 24  ? 0.1972 0.2064 0.2481 -0.0064 0.0408  -0.0128 24  VAL   A CG1 
663  C  CG1 B VAL   A 24  ? 0.1976 0.1934 0.2306 -0.0218 0.0340  0.0018  24  VAL   A CG1 
664  C  CG2 A VAL   A 24  ? 0.2070 0.2067 0.2482 -0.0153 0.0681  0.0219  24  VAL   A CG2 
665  C  CG2 B VAL   A 24  ? 0.1921 0.1830 0.2139 -0.0293 0.0355  -0.0006 24  VAL   A CG2 
684  N  N   A GLU   A 25  ? 0.2022 0.2364 0.2144 -0.0364 0.0449  -0.0131 25  GLU   A N   
685  N  N   B GLU   A 25  ? 0.1973 0.2216 0.2017 -0.0343 0.0469  -0.0135 25  GLU   A N   
686  C  CA  A GLU   A 25  ? 0.2174 0.2638 0.2193 -0.0302 0.0545  -0.0228 25  GLU   A CA  
687  C  CA  B GLU   A 25  ? 0.2089 0.2378 0.2123 -0.0371 0.0429  -0.0178 25  GLU   A CA  
688  C  C   A GLU   A 25  ? 0.2034 0.2664 0.1887 -0.0417 0.0577  -0.0196 25  GLU   A C   
689  C  C   B GLU   A 25  ? 0.2106 0.2448 0.1996 -0.0363 0.0455  -0.0193 25  GLU   A C   
690  O  O   A GLU   A 25  ? 0.2080 0.2736 0.2013 -0.0449 0.0497  -0.0176 25  GLU   A O   
691  O  O   B GLU   A 25  ? 0.2138 0.2459 0.2019 -0.0369 0.0494  -0.0227 25  GLU   A O   
692  C  CB  A GLU   A 25  ? 0.2447 0.2936 0.2617 -0.0212 0.0553  -0.0220 25  GLU   A CB  
693  C  CB  B GLU   A 25  ? 0.2185 0.2434 0.2409 -0.0398 0.0372  -0.0190 25  GLU   A CB  
694  C  CG  A GLU   A 25  ? 0.2777 0.3193 0.3272 -0.0193 0.0379  -0.0269 25  GLU   A CG  
695  C  CG  B GLU   A 25  ? 0.2321 0.2524 0.2833 -0.0399 0.0300  -0.0189 25  GLU   A CG  
696  C  CD  A GLU   A 25  ? 0.3037 0.3420 0.3855 -0.0198 0.0246  -0.0271 25  GLU   A CD  
697  C  CD  B GLU   A 25  ? 0.2406 0.2608 0.3198 -0.0416 0.0188  -0.0173 25  GLU   A CD  
698  O  OE1 A GLU   A 25  ? 0.3147 0.3505 0.3991 -0.0182 0.0114  -0.0349 25  GLU   A OE1 
699  O  OE1 B GLU   A 25  ? 0.2445 0.2653 0.3397 -0.0402 0.0132  -0.0172 25  GLU   A OE1 
700  O  OE2 A GLU   A 25  ? 0.3116 0.3521 0.4178 -0.0214 0.0202  -0.0325 25  GLU   A OE2 
701  O  OE2 B GLU   A 25  ? 0.2472 0.2642 0.3339 -0.0422 0.0161  -0.0140 25  GLU   A OE2 
714  N  N   A GLU   A 26  ? 0.1901 0.2614 0.1940 -0.0568 0.0683  -0.0163 26  GLU   A N   
715  N  N   B GLU   A 26  ? 0.2127 0.2477 0.1898 -0.0373 0.0495  -0.0191 26  GLU   A N   
716  C  CA  A GLU   A 26  ? 0.2040 0.2645 0.1836 -0.0690 0.0626  -0.0107 26  GLU   A CA  
717  C  CA  B GLU   A 26  ? 0.2209 0.2534 0.1927 -0.0328 0.0472  -0.0193 26  GLU   A CA  
718  C  C   A GLU   A 26  ? 0.2042 0.2517 0.1630 -0.0642 0.0530  -0.0035 26  GLU   A C   
719  C  C   B GLU   A 26  ? 0.2279 0.2555 0.1861 -0.0243 0.0429  -0.0096 26  GLU   A C   
720  O  O   A GLU   A 26  ? 0.2147 0.2522 0.1584 -0.0694 0.0494  -0.0045 26  GLU   A O   
721  O  O   B GLU   A 26  ? 0.2273 0.2526 0.1796 -0.0228 0.0497  -0.0064 26  GLU   A O   
722  C  CB  A GLU   A 26  ? 0.2279 0.2740 0.2224 -0.0822 0.0582  0.0005  26  GLU   A CB  
723  C  CB  B GLU   A 26  ? 0.2258 0.2572 0.2053 -0.0376 0.0420  -0.0257 26  GLU   A CB  
724  C  CG  A GLU   A 26  ? 0.2559 0.2926 0.3032 -0.0898 0.0562  -0.0061 26  GLU   A CG  
725  C  CG  B GLU   A 26  ? 0.2301 0.2604 0.2151 -0.0432 0.0529  -0.0296 26  GLU   A CG  
726  C  CD  A GLU   A 26  ? 0.2765 0.3073 0.3536 -0.1023 0.0737  -0.0049 26  GLU   A CD  
727  C  CD  B GLU   A 26  ? 0.2357 0.2648 0.2140 -0.0521 0.0683  -0.0337 26  GLU   A CD  
728  O  OE1 A GLU   A 26  ? 0.2774 0.3327 0.3641 -0.0926 0.0919  -0.0268 26  GLU   A OE1 
729  O  OE1 B GLU   A 26  ? 0.2325 0.2823 0.2118 -0.0459 0.0772  -0.0448 26  GLU   A OE1 
730  O  OE2 A GLU   A 26  ? 0.3045 0.3111 0.3740 -0.1041 0.0663  0.0018  26  GLU   A OE2 
731  O  OE2 B GLU   A 26  ? 0.2430 0.2580 0.1860 -0.0612 0.0848  -0.0356 26  GLU   A OE2 
744  N  N   A ALA   A 27  ? 0.1852 0.2368 0.1558 -0.0699 0.0526  0.0041  27  ALA   A N   
745  N  N   B ALA   A 27  ? 0.2343 0.2595 0.1846 -0.0190 0.0343  -0.0035 27  ALA   A N   
746  C  CA  A ALA   A 27  ? 0.1951 0.2467 0.1529 -0.0614 0.0416  -0.0007 27  ALA   A CA  
747  C  CA  B ALA   A 27  ? 0.2472 0.2714 0.1857 -0.0149 0.0246  -0.0002 27  ALA   A CA  
748  C  C   A ALA   A 27  ? 0.2217 0.2671 0.1615 -0.0703 0.0465  -0.0133 27  ALA   A C   
749  C  C   B ALA   A 27  ? 0.2676 0.2910 0.2068 -0.0155 0.0189  -0.0052 27  ALA   A C   
750  O  O   A ALA   A 27  ? 0.2266 0.2646 0.1633 -0.0749 0.0318  -0.0110 27  ALA   A O   
751  O  O   B ALA   A 27  ? 0.2673 0.2893 0.2036 -0.0151 0.0138  -0.0065 27  ALA   A O   
752  C  CB  A ALA   A 27  ? 0.1797 0.2359 0.1536 -0.0600 0.0386  0.0079  27  ALA   A CB  
753  C  CB  B ALA   A 27  ? 0.2422 0.2668 0.1790 -0.0151 0.0235  0.0038  27  ALA   A CB  
764  N  N   A LYS   A 28  ? 0.2552 0.2949 0.1805 -0.0696 0.0399  -0.0432 28  LYS   A N   
765  N  N   B LYS   A 28  ? 0.2915 0.3133 0.2358 -0.0170 0.0148  -0.0130 28  LYS   A N   
766  C  CA  A LYS   A 28  ? 0.2965 0.3344 0.2241 -0.0600 0.0410  -0.0568 28  LYS   A CA  
767  C  CA  B LYS   A 28  ? 0.3171 0.3386 0.2723 -0.0179 0.0131  -0.0180 28  LYS   A CA  
768  C  C   A LYS   A 28  ? 0.3155 0.3653 0.2115 -0.0645 0.0585  -0.0447 28  LYS   A C   
769  C  C   B LYS   A 28  ? 0.3325 0.3584 0.2751 -0.0270 0.0203  -0.0137 28  LYS   A C   
770  O  O   A LYS   A 28  ? 0.3237 0.3745 0.2434 -0.0615 0.0401  -0.0466 28  LYS   A O   
771  O  O   B LYS   A 28  ? 0.3362 0.3613 0.2815 -0.0253 0.0146  -0.0159 28  LYS   A O   
772  C  CB  A LYS   A 28  ? 0.3199 0.3493 0.2896 -0.0418 0.0298  -0.0688 28  LYS   A CB  
773  C  CB  B LYS   A 28  ? 0.3285 0.3459 0.3097 -0.0108 0.0070  -0.0237 28  LYS   A CB  
774  C  CG  A LYS   A 28  ? 0.3395 0.3606 0.3512 -0.0269 0.0258  -0.0743 28  LYS   A CG  
775  C  CG  B LYS   A 28  ? 0.3393 0.3522 0.3474 -0.0056 0.0033  -0.0269 28  LYS   A CG  
776  C  CD  A LYS   A 28  ? 0.3573 0.3758 0.4209 -0.0152 0.0173  -0.0739 28  LYS   A CD  
777  C  CD  B LYS   A 28  ? 0.3500 0.3606 0.3887 -0.0017 -0.0006 -0.0281 28  LYS   A CD  
778  C  CE  A LYS   A 28  ? 0.3694 0.3862 0.4699 -0.0072 0.0109  -0.0761 28  LYS   A CE  
779  C  CE  B LYS   A 28  ? 0.3582 0.3666 0.4192 0.0003  -0.0033 -0.0295 28  LYS   A CE  
780  N  NZ  A LYS   A 28  ? 0.3763 0.3915 0.5003 -0.0012 0.0099  -0.0790 28  LYS   A NZ  
781  N  NZ  B LYS   A 28  ? 0.3628 0.3697 0.4369 0.0021  -0.0047 -0.0314 28  LYS   A NZ  
808  N  N   A LYS   A 29  ? 0.3238 0.3861 0.1923 -0.0727 0.0937  -0.0219 29  LYS   A N   
809  N  N   B LYS   A 29  ? 0.3432 0.3747 0.2802 -0.0388 0.0352  -0.0047 29  LYS   A N   
810  C  CA  A LYS   A 29  ? 0.3440 0.4098 0.2238 -0.0748 0.1080  -0.0024 29  LYS   A CA  
811  C  CA  B LYS   A 29  ? 0.3546 0.3909 0.2924 -0.0498 0.0490  0.0033  29  LYS   A CA  
812  C  C   A LYS   A 29  ? 0.3494 0.4066 0.2088 -0.0795 0.0945  0.0121  29  LYS   A C   
813  C  C   B LYS   A 29  ? 0.3508 0.3934 0.2518 -0.0684 0.0633  0.0124  29  LYS   A C   
814  O  O   A LYS   A 29  ? 0.3636 0.4193 0.2253 -0.0712 0.0849  0.0102  29  LYS   A O   
815  O  O   B LYS   A 29  ? 0.3560 0.3982 0.2560 -0.0661 0.0622  0.0143  29  LYS   A O   
816  C  CB  A LYS   A 29  ? 0.3589 0.4352 0.2880 -0.0672 0.1173  0.0022  29  LYS   A CB  
817  C  CB  B LYS   A 29  ? 0.3678 0.4031 0.3429 -0.0415 0.0463  0.0029  29  LYS   A CB  
818  C  CG  A LYS   A 29  ? 0.3776 0.4575 0.3581 -0.0581 0.1154  0.0032  29  LYS   A CG  
819  C  CG  B LYS   A 29  ? 0.3810 0.4141 0.3912 -0.0339 0.0430  0.0026  29  LYS   A CG  
820  C  CD  A LYS   A 29  ? 0.3949 0.4755 0.4257 -0.0503 0.1088  0.0012  29  LYS   A CD  
821  C  CD  B LYS   A 29  ? 0.3918 0.4228 0.4341 -0.0277 0.0398  0.0024  29  LYS   A CD  
822  C  CE  A LYS   A 29  ? 0.4063 0.4879 0.4725 -0.0451 0.1064  -0.0019 29  LYS   A CE  
823  C  CE  B LYS   A 29  ? 0.3990 0.4289 0.4648 -0.0236 0.0384  0.0012  29  LYS   A CE  
824  N  NZ  A LYS   A 29  ? 0.4110 0.4947 0.5013 -0.0419 0.1037  -0.0044 29  LYS   A NZ  
825  N  NZ  B LYS   A 29  ? 0.4031 0.4326 0.4826 -0.0216 0.0373  0.0011  29  LYS   A NZ  
852  N  N   . VAL   A 30  ? 0.3404 0.3901 0.2103 -0.0899 0.0802  0.0183  30  VAL   A N   
853  C  CA  . VAL   A 30  ? 0.3349 0.3748 0.1784 -0.1114 0.0507  0.0399  30  VAL   A CA  
854  C  C   . VAL   A 30  ? 0.3380 0.3608 0.1421 -0.1123 0.0308  0.0490  30  VAL   A C   
855  O  O   . VAL   A 30  ? 0.3486 0.3628 0.1508 -0.1126 0.0210  0.0436  30  VAL   A O   
856  C  CB  . VAL   A 30  ? 0.3277 0.3656 0.2156 -0.1288 0.0249  0.0376  30  VAL   A CB  
857  C  CG1 . VAL   A 30  ? 0.3307 0.3643 0.2358 -0.1302 0.0115  0.0348  30  VAL   A CG1 
858  C  CG2 . VAL   A 30  ? 0.3248 0.3662 0.2360 -0.1373 0.0329  0.0372  30  VAL   A CG2 
869  N  N   . LYS   A 31  ? 0.3324 0.3469 0.1348 -0.1183 0.0078  0.0448  31  LYS   A N   
870  C  CA  . LYS   A 31  ? 0.3499 0.3500 0.1564 -0.1054 -0.0147 0.0418  31  LYS   A CA  
871  C  C   . LYS   A 31  ? 0.3101 0.3214 0.1252 -0.0795 -0.0198 0.0700  31  LYS   A C   
872  O  O   . LYS   A 31  ? 0.3164 0.3363 0.1507 -0.0808 -0.0319 0.0821  31  LYS   A O   
873  C  CB  . LYS   A 31  ? 0.4077 0.3869 0.2749 -0.1011 -0.0298 0.0161  31  LYS   A CB  
874  C  CG  . LYS   A 31  ? 0.4609 0.4304 0.4191 -0.0910 -0.0420 -0.0026 31  LYS   A CG  
875  C  CD  . LYS   A 31  ? 0.5076 0.4699 0.5277 -0.0810 -0.0543 -0.0191 31  LYS   A CD  
876  C  CE  . LYS   A 31  ? 0.5438 0.4960 0.5977 -0.0735 -0.0638 -0.0319 31  LYS   A CE  
877  N  NZ  . LYS   A 31  ? 0.5599 0.5046 0.6354 -0.0696 -0.0690 -0.0394 31  LYS   A NZ  
891  N  N   . PRO   A 32  ? 0.2705 0.2871 0.1088 -0.0767 -0.0119 0.0559  32  PRO   A N   
892  C  CA  . PRO   A 32  ? 0.2571 0.2636 0.1545 -0.0717 -0.0143 0.0656  32  PRO   A CA  
893  C  C   . PRO   A 32  ? 0.2515 0.2565 0.1645 -0.0592 -0.0217 0.0654  32  PRO   A C   
894  O  O   . PRO   A 32  ? 0.2453 0.2475 0.1665 -0.0587 -0.0400 0.0665  32  PRO   A O   
895  C  CB  . PRO   A 32  ? 0.2488 0.2655 0.1575 -0.0671 -0.0182 0.0505  32  PRO   A CB  
896  C  CG  . PRO   A 32  ? 0.2474 0.2713 0.0960 -0.0606 -0.0285 0.0379  32  PRO   A CG  
897  C  CD  . PRO   A 32  ? 0.2515 0.2751 0.0992 -0.0680 -0.0167 0.0388  32  PRO   A CD  
905  N  N   . THR   A 33  ? 0.2607 0.2542 0.1518 -0.0509 -0.0206 0.0725  33  THR   A N   
906  C  CA  . THR   A 33  ? 0.2590 0.2478 0.1580 -0.0416 -0.0338 0.0707  33  THR   A CA  
907  C  C   . THR   A 33  ? 0.2290 0.2274 0.1507 -0.0436 -0.0318 0.0539  33  THR   A C   
908  O  O   . THR   A 33  ? 0.2204 0.2273 0.1702 -0.0438 -0.0482 0.0567  33  THR   A O   
909  C  CB  . THR   A 33  ? 0.2835 0.2704 0.1808 -0.0306 -0.0414 0.0850  33  THR   A CB  
910  O  OG1 . THR   A 33  ? 0.3064 0.2816 0.2029 -0.0168 -0.0332 0.0992  33  THR   A OG1 
911  C  CG2 . THR   A 33  ? 0.2852 0.2826 0.2096 -0.0235 -0.0495 0.0767  33  THR   A CG2 
919  N  N   . VAL   A 34  ? 0.2057 0.2084 0.1381 -0.0459 -0.0266 0.0486  34  VAL   A N   
920  C  CA  . VAL   A 34  ? 0.1831 0.1873 0.1336 -0.0350 -0.0151 0.0435  34  VAL   A CA  
921  C  C   . VAL   A 34  ? 0.1722 0.1781 0.1256 -0.0256 -0.0015 0.0345  34  VAL   A C   
922  O  O   . VAL   A 34  ? 0.1734 0.1834 0.1565 -0.0343 -0.0031 0.0450  34  VAL   A O   
923  C  CB  . VAL   A 34  ? 0.1831 0.1847 0.1649 -0.0310 -0.0086 0.0327  34  VAL   A CB  
924  C  CG1 . VAL   A 34  ? 0.1840 0.1847 0.1627 -0.0251 -0.0002 0.0189  34  VAL   A CG1 
925  C  CG2 . VAL   A 34  ? 0.1849 0.2014 0.1923 -0.0254 -0.0213 0.0317  34  VAL   A CG2 
935  N  N   . VAL   A 35  ? 0.1602 0.1641 0.1233 -0.0304 -0.0101 0.0283  35  VAL   A N   
936  C  CA  . VAL   A 35  ? 0.1561 0.1614 0.1154 -0.0275 -0.0010 0.0244  35  VAL   A CA  
937  C  C   . VAL   A 35  ? 0.1447 0.1483 0.1124 -0.0199 0.0026  0.0238  35  VAL   A C   
938  O  O   . VAL   A 35  ? 0.1355 0.1635 0.1400 -0.0254 0.0133  0.0220  35  VAL   A O   
939  C  CB  . VAL   A 35  ? 0.1574 0.1666 0.1244 -0.0193 0.0093  0.0107  35  VAL   A CB  
940  C  CG1 . VAL   A 35  ? 0.1716 0.1738 0.1473 -0.0064 0.0058  0.0013  35  VAL   A CG1 
941  C  CG2 . VAL   A 35  ? 0.1587 0.1726 0.1588 -0.0169 0.0118  0.0023  35  VAL   A CG2 
951  N  N   . VAL   A 36  ? 0.1337 0.1438 0.1109 -0.0255 0.0035  0.0242  36  VAL   A N   
952  C  CA  . VAL   A 36  ? 0.1321 0.1343 0.1202 -0.0139 -0.0027 0.0141  36  VAL   A CA  
953  C  C   . VAL   A 36  ? 0.1224 0.1386 0.1291 -0.0195 0.0030  0.0156  36  VAL   A C   
954  O  O   . VAL   A 36  ? 0.1317 0.1383 0.1465 -0.0099 0.0174  0.0183  36  VAL   A O   
955  C  CB  . VAL   A 36  ? 0.1323 0.1280 0.1316 -0.0133 0.0012  0.0152  36  VAL   A CB  
956  C  CG1 . VAL   A 36  ? 0.1353 0.1342 0.1373 -0.0149 0.0036  0.0054  36  VAL   A CG1 
957  C  CG2 . VAL   A 36  ? 0.1418 0.1324 0.1524 -0.0123 -0.0055 0.0251  36  VAL   A CG2 
967  N  N   . ASN   A 37  ? 0.1228 0.1287 0.1161 -0.0080 0.0028  0.0191  37  ASN   A N   
968  C  CA  . ASN   A 37  ? 0.1209 0.1287 0.1149 -0.0028 0.0090  0.0170  37  ASN   A CA  
969  C  C   . ASN   A 37  ? 0.1193 0.1238 0.1220 -0.0027 0.0115  0.0239  37  ASN   A C   
970  O  O   . ASN   A 37  ? 0.1335 0.1313 0.1171 0.0056  0.0161  0.0129  37  ASN   A O   
971  C  CB  . ASN   A 37  ? 0.1217 0.1270 0.1235 -0.0021 0.0050  0.0147  37  ASN   A CB  
972  C  CG  . ASN   A 37  ? 0.1196 0.1304 0.1309 -0.0009 0.0035  0.0136  37  ASN   A CG  
973  O  OD1 . ASN   A 37  ? 0.1231 0.1267 0.1549 -0.0022 0.0048  0.0178  37  ASN   A OD1 
974  N  ND2 . ASN   A 37  ? 0.1241 0.1248 0.1487 -0.0036 0.0075  0.0271  37  ASN   A ND2 
981  N  N   A ALA   A 38  ? 0.1160 0.1311 0.1276 -0.0023 0.0158  0.0153  38  ALA   A N   
982  N  N   B ALA   A 38  ? 0.1223 0.1310 0.1264 -0.0030 0.0013  0.0170  38  ALA   A N   
983  C  CA  A ALA   A 38  ? 0.1230 0.1316 0.1200 -0.0056 0.0060  0.0068  38  ALA   A CA  
984  C  CA  B ALA   A 38  ? 0.1293 0.1361 0.1353 -0.0050 -0.0137 0.0111  38  ALA   A CA  
985  C  C   A ALA   A 38  ? 0.1232 0.1340 0.1158 -0.0020 0.0042  -0.0009 38  ALA   A C   
986  C  C   B ALA   A 38  ? 0.1260 0.1314 0.1373 -0.0034 -0.0228 0.0076  38  ALA   A C   
987  O  O   A ALA   A 38  ? 0.1206 0.1242 0.1265 -0.0024 -0.0031 -0.0091 38  ALA   A O   
988  O  O   B ALA   A 38  ? 0.1183 0.1219 0.1449 -0.0053 -0.0366 0.0129  38  ALA   A O   
989  C  CB  A ALA   A 38  ? 0.1312 0.1500 0.1401 -0.0175 0.0020  0.0048  38  ALA   A CB  
990  C  CB  B ALA   A 38  ? 0.1352 0.1416 0.1447 -0.0063 -0.0190 -0.0001 38  ALA   A CB  
1001 N  N   A ALA   A 39  ? 0.1216 0.1325 0.1289 0.0020  0.0145  0.0117  39  ALA   A N   
1002 N  N   B ALA   A 39  ? 0.1308 0.1343 0.1411 -0.0038 -0.0145 0.0087  39  ALA   A N   
1003 C  CA  A ALA   A 39  ? 0.1177 0.1248 0.1232 -0.0002 0.0157  0.0094  39  ALA   A CA  
1004 C  CA  B ALA   A 39  ? 0.1364 0.1381 0.1333 -0.0060 -0.0055 0.0088  39  ALA   A CA  
1005 C  C   A ALA   A 39  ? 0.1213 0.1261 0.1259 0.0009  0.0056  0.0067  39  ALA   A C   
1006 C  C   B ALA   A 39  ? 0.1327 0.1346 0.1198 -0.0073 0.0072  0.0127  39  ALA   A C   
1007 O  O   A ALA   A 39  ? 0.1336 0.1248 0.1318 -0.0019 0.0032  0.0121  39  ALA   A O   
1008 O  O   B ALA   A 39  ? 0.1362 0.1359 0.1231 -0.0101 0.0124  0.0106  39  ALA   A O   
1009 C  CB  A ALA   A 39  ? 0.1186 0.1272 0.1457 0.0005  -0.0013 0.0025  39  ALA   A CB  
1010 C  CB  B ALA   A 39  ? 0.1466 0.1428 0.1439 -0.0031 -0.0115 -0.0008 39  ALA   A CB  
1021 N  N   A ASN   A 40  ? 0.1220 0.1300 0.1298 -0.0037 0.0149  0.0081  40  ASN   A N   
1022 N  N   B ASN   A 40  ? 0.1339 0.1317 0.1160 -0.0066 0.0157  0.0195  40  ASN   A N   
1023 C  CA  A ASN   A 40  ? 0.1240 0.1224 0.1396 -0.0030 0.0057  0.0011  40  ASN   A CA  
1024 C  CA  B ASN   A 40  ? 0.1363 0.1256 0.1243 -0.0036 0.0034  0.0234  40  ASN   A CA  
1025 C  C   A ASN   A 40  ? 0.1228 0.1163 0.1131 -0.0049 0.0138  0.0173  40  ASN   A C   
1026 C  C   B ASN   A 40  ? 0.1348 0.1255 0.1189 -0.0013 0.0082  0.0381  40  ASN   A C   
1027 O  O   A ASN   A 40  ? 0.1233 0.1247 0.1232 -0.0096 0.0104  0.0153  40  ASN   A O   
1028 O  O   B ASN   A 40  ? 0.1309 0.1277 0.1284 0.0026  0.0002  0.0397  40  ASN   A O   
1029 C  CB  A ASN   A 40  ? 0.1368 0.1351 0.1484 0.0078  -0.0032 0.0049  40  ASN   A CB  
1030 C  CB  B ASN   A 40  ? 0.1510 0.1257 0.1424 -0.0048 0.0025  0.0120  40  ASN   A CB  
1031 C  CG  A ASN   A 40  ? 0.1475 0.1422 0.1623 0.0079  0.0011  0.0145  40  ASN   A CG  
1032 C  CG  B ASN   A 40  ? 0.1555 0.1280 0.1556 -0.0078 0.0026  0.0050  40  ASN   A CG  
1033 O  OD1 A ASN   A 40  ? 0.1584 0.1410 0.1749 0.0032  -0.0064 0.0115  40  ASN   A OD1 
1034 O  OD1 B ASN   A 40  ? 0.1595 0.1275 0.1672 -0.0113 0.0014  -0.0003 40  ASN   A OD1 
1035 N  ND2 A ASN   A 40  ? 0.1547 0.1535 0.1710 0.0078  0.0145  0.0006  40  ASN   A ND2 
1036 N  ND2 B ASN   A 40  ? 0.1574 0.1358 0.1595 -0.0128 0.0172  -0.0018 40  ASN   A ND2 
1049 N  N   A VAL   A 41  ? 0.1287 0.1247 0.1181 -0.0028 0.0067  0.0130  41  VAL   A N   
1050 N  N   B VAL   A 41  ? 0.1366 0.1330 0.1172 0.0003  0.0091  0.0414  41  VAL   A N   
1051 C  CA  A VAL   A 41  ? 0.1324 0.1318 0.1339 -0.0021 0.0180  0.0136  41  VAL   A CA  
1052 C  CA  B VAL   A 41  ? 0.1397 0.1367 0.1192 0.0037  0.0146  0.0386  41  VAL   A CA  
1053 C  C   A VAL   A 41  ? 0.1287 0.1236 0.1451 0.0015  0.0233  0.0143  41  VAL   A C   
1054 C  C   B VAL   A 41  ? 0.1415 0.1366 0.1239 0.0004  0.0161  0.0351  41  VAL   A C   
1055 O  O   A VAL   A 41  ? 0.1345 0.1148 0.1644 0.0038  0.0106  0.0065  41  VAL   A O   
1056 O  O   B VAL   A 41  ? 0.1501 0.1313 0.1296 0.0025  0.0064  0.0245  41  VAL   A O   
1057 C  CB  A VAL   A 41  ? 0.1368 0.1313 0.1468 0.0030  0.0192  0.0130  41  VAL   A CB  
1058 C  CB  B VAL   A 41  ? 0.1430 0.1421 0.1276 0.0089  0.0250  0.0408  41  VAL   A CB  
1059 C  CG1 A VAL   A 41  ? 0.1444 0.1406 0.1508 0.0064  0.0061  0.0050  41  VAL   A CG1 
1060 C  CG1 B VAL   A 41  ? 0.1546 0.1430 0.1352 0.0086  0.0273  0.0326  41  VAL   A CG1 
1061 C  CG2 A VAL   A 41  ? 0.1466 0.1393 0.1419 -0.0051 0.0312  0.0102  41  VAL   A CG2 
1062 C  CG2 B VAL   A 41  ? 0.1434 0.1496 0.1397 0.0121  0.0218  0.0380  41  VAL   A CG2 
1081 N  N   A TYR   A 42  ? 0.1201 0.1191 0.1594 -0.0020 0.0265  0.0184  42  TYR   A N   
1082 N  N   B TYR   A 42  ? 0.1391 0.1391 0.1355 0.0021  0.0144  0.0388  42  TYR   A N   
1083 C  CA  A TYR   A 42  ? 0.1261 0.1137 0.1688 -0.0070 0.0272  0.0197  42  TYR   A CA  
1084 C  CA  B TYR   A 42  ? 0.1388 0.1405 0.1371 0.0013  0.0162  0.0371  42  TYR   A CA  
1085 C  C   A TYR   A 42  ? 0.1184 0.1177 0.1674 -0.0051 0.0241  0.0194  42  TYR   A C   
1086 C  C   B TYR   A 42  ? 0.1390 0.1428 0.1330 0.0010  0.0136  0.0430  42  TYR   A C   
1087 O  O   A TYR   A 42  ? 0.1211 0.1205 0.1876 -0.0148 0.0184  -0.0008 42  TYR   A O   
1088 O  O   B TYR   A 42  ? 0.1382 0.1482 0.1428 -0.0036 0.0103  0.0370  42  TYR   A O   
1089 C  CB  A TYR   A 42  ? 0.1462 0.1268 0.1673 -0.0039 0.0318  0.0199  42  TYR   A CB  
1090 C  CB  B TYR   A 42  ? 0.1472 0.1416 0.1404 0.0060  0.0136  0.0379  42  TYR   A CB  
1091 C  CG  A TYR   A 42  ? 0.1616 0.1361 0.1589 -0.0049 0.0251  0.0321  42  TYR   A CG  
1092 C  CG  B TYR   A 42  ? 0.1550 0.1464 0.1393 0.0127  0.0069  0.0365  42  TYR   A CG  
1093 C  CD1 A TYR   A 42  ? 0.1690 0.1535 0.1708 -0.0134 0.0307  0.0342  42  TYR   A CD1 
1094 C  CD1 B TYR   A 42  ? 0.1554 0.1487 0.1365 0.0126  0.0113  0.0437  42  TYR   A CD1 
1095 C  CD2 A TYR   A 42  ? 0.1719 0.1572 0.1824 0.0044  0.0135  0.0291  42  TYR   A CD2 
1096 C  CD2 B TYR   A 42  ? 0.1661 0.1592 0.1514 0.0161  0.0031  0.0303  42  TYR   A CD2 
1097 C  CE1 A TYR   A 42  ? 0.1788 0.1651 0.1659 -0.0128 0.0286  0.0290  42  TYR   A CE1 
1098 C  CE1 B TYR   A 42  ? 0.1579 0.1559 0.1414 0.0123  0.0158  0.0346  42  TYR   A CE1 
1099 C  CE2 A TYR   A 42  ? 0.1843 0.1711 0.1921 -0.0086 0.0124  0.0350  42  TYR   A CE2 
1100 C  CE2 B TYR   A 42  ? 0.1713 0.1659 0.1530 0.0158  0.0088  0.0287  42  TYR   A CE2 
1101 C  CZ  A TYR   A 42  ? 0.1946 0.1758 0.1694 -0.0160 0.0279  0.0334  42  TYR   A CZ  
1102 C  CZ  B TYR   A 42  ? 0.1675 0.1651 0.1389 0.0136  0.0138  0.0272  42  TYR   A CZ  
1103 O  OH  A TYR   A 42  ? 0.2093 0.1940 0.1904 -0.0222 0.0198  0.0239  42  TYR   A OH  
1104 O  OH  B TYR   A 42  ? 0.1702 0.1762 0.1399 0.0080  0.0150  0.0212  42  TYR   A OH  
1123 N  N   A LEU   A 43  ? 0.1232 0.1207 0.1499 -0.0060 0.0153  0.0066  43  LEU   A N   
1124 N  N   B LEU   A 43  ? 0.1327 0.1383 0.1283 0.0017  0.0018  0.0430  43  LEU   A N   
1125 C  CA  A LEU   A 43  ? 0.1189 0.1185 0.1529 -0.0074 0.0138  0.0040  43  LEU   A CA  
1126 C  CA  B LEU   A 43  ? 0.1326 0.1350 0.1333 -0.0037 -0.0022 0.0325  43  LEU   A CA  
1127 C  C   A LEU   A 43  ? 0.1150 0.1284 0.1461 -0.0009 0.0122  0.0017  43  LEU   A C   
1128 C  C   B LEU   A 43  ? 0.1322 0.1352 0.1294 -0.0081 -0.0046 0.0255  43  LEU   A C   
1129 O  O   A LEU   A 43  ? 0.1333 0.1360 0.1696 0.0078  -0.0032 0.0036  43  LEU   A O   
1130 O  O   B LEU   A 43  ? 0.1283 0.1316 0.1265 -0.0178 -0.0173 0.0209  43  LEU   A O   
1131 C  CB  A LEU   A 43  ? 0.1301 0.1190 0.1547 -0.0093 0.0072  -0.0005 43  LEU   A CB  
1132 C  CB  B LEU   A 43  ? 0.1289 0.1318 0.1383 -0.0029 -0.0009 0.0290  43  LEU   A CB  
1133 C  CG  A LEU   A 43  ? 0.1324 0.1203 0.1620 -0.0066 0.0007  0.0039  43  LEU   A CG  
1134 C  CG  B LEU   A 43  ? 0.1239 0.1297 0.1406 -0.0000 0.0013  0.0281  43  LEU   A CG  
1135 C  CD1 A LEU   A 43  ? 0.1407 0.1311 0.1809 -0.0040 -0.0073 0.0182  43  LEU   A CD1 
1136 C  CD1 B LEU   A 43  ? 0.1269 0.1344 0.1469 0.0012  0.0012  0.0326  43  LEU   A CD1 
1137 C  CD2 A LEU   A 43  ? 0.1446 0.1235 0.1661 -0.0049 -0.0006 0.0112  43  LEU   A CD2 
1138 C  CD2 B LEU   A 43  ? 0.1270 0.1233 0.1410 0.0035  0.0034  0.0428  43  LEU   A CD2 
1161 N  N   A LYS   A 44  ? 0.1288 0.1280 0.1381 -0.0016 0.0083  0.0128  44  LYS   A N   
1162 N  N   B LYS   A 44  ? 0.1388 0.1392 0.1373 0.0014  -0.0018 0.0253  44  LYS   A N   
1163 C  CA  A LYS   A 44  ? 0.1392 0.1260 0.1394 -0.0084 0.0182  0.0213  44  LYS   A CA  
1164 C  CA  B LYS   A 44  ? 0.1484 0.1420 0.1458 0.0046  0.0026  0.0212  44  LYS   A CA  
1165 C  C   A LYS   A 44  ? 0.1300 0.1277 0.1343 0.0033  0.0073  0.0094  44  LYS   A C   
1166 C  C   B LYS   A 44  ? 0.1388 0.1336 0.1283 0.0050  0.0028  0.0111  44  LYS   A C   
1167 O  O   A LYS   A 44  ? 0.1350 0.1418 0.1619 0.0023  0.0029  0.0024  44  LYS   A O   
1168 O  O   B LYS   A 44  ? 0.1456 0.1375 0.1282 0.0075  0.0047  -0.0052 44  LYS   A O   
1169 C  CB  A LYS   A 44  ? 0.1652 0.1437 0.1795 -0.0056 0.0282  0.0312  44  LYS   A CB  
1170 C  CB  B LYS   A 44  ? 0.1679 0.1621 0.1954 0.0107  0.0097  0.0156  44  LYS   A CB  
1171 C  CG  A LYS   A 44  ? 0.2001 0.1679 0.2315 -0.0124 0.0472  0.0469  44  LYS   A CG  
1172 C  CG  B LYS   A 44  ? 0.1848 0.1854 0.2465 0.0144  0.0129  0.0182  44  LYS   A CG  
1173 C  CD  A LYS   A 44  ? 0.2402 0.2215 0.3394 -0.0128 0.0381  0.0349  44  LYS   A CD  
1174 C  CD  B LYS   A 44  ? 0.2028 0.2135 0.3032 0.0119  0.0079  0.0193  44  LYS   A CD  
1175 C  CE  A LYS   A 44  ? 0.2570 0.2518 0.4061 -0.0059 0.0296  0.0332  44  LYS   A CE  
1176 C  CE  B LYS   A 44  ? 0.2088 0.2268 0.3397 0.0130  0.0047  0.0298  44  LYS   A CE  
1177 N  NZ  A LYS   A 44  ? 0.2612 0.2699 0.4350 -0.0003 0.0236  0.0348  44  LYS   A NZ  
1178 N  NZ  B LYS   A 44  ? 0.2166 0.2356 0.3653 0.0106  0.0059  0.0361  44  LYS   A NZ  
1205 N  N   . HIS   A 45  ? 0.1281 0.1290 0.1318 0.0001  0.0016  0.0174  45  HIS   A N   
1206 C  CA  . HIS   A 45  ? 0.1257 0.1274 0.1437 0.0007  -0.0050 0.0153  45  HIS   A CA  
1207 C  C   . HIS   A 45  ? 0.1300 0.1378 0.1492 0.0060  0.0007  0.0182  45  HIS   A C   
1208 O  O   . HIS   A 45  ? 0.1498 0.1548 0.1886 0.0282  -0.0069 -0.0079 45  HIS   A O   
1209 C  CB  . HIS   A 45  ? 0.1251 0.1244 0.1392 -0.0003 -0.0030 0.0104  45  HIS   A CB  
1210 C  CG  . HIS   A 45  ? 0.1235 0.1241 0.1256 -0.0092 -0.0006 0.0103  45  HIS   A CG  
1211 N  ND1 . HIS   A 45  ? 0.1160 0.1298 0.1516 -0.0071 -0.0036 0.0205  45  HIS   A ND1 
1212 C  CD2 . HIS   A 45  ? 0.1227 0.1302 0.1320 -0.0095 -0.0028 0.0175  45  HIS   A CD2 
1213 C  CE1 . HIS   A 45  ? 0.1239 0.1358 0.1287 -0.0092 -0.0016 0.0208  45  HIS   A CE1 
1214 N  NE2 . HIS   A 45  ? 0.1245 0.1360 0.1369 -0.0034 -0.0025 0.0204  45  HIS   A NE2 
1223 N  N   A GLY   A 46  ? 0.1472 0.1393 0.1702 0.0062  -0.0222 0.0261  46  GLY   A N   
1224 N  N   B GLY   A 46  ? 0.1396 0.1406 0.1528 0.0112  -0.0132 0.0180  46  GLY   A N   
1225 C  CA  A GLY   A 46  ? 0.1524 0.1493 0.1903 0.0084  -0.0204 0.0286  46  GLY   A CA  
1226 C  CA  B GLY   A 46  ? 0.1457 0.1438 0.1549 0.0133  -0.0181 0.0153  46  GLY   A CA  
1227 C  C   A GLY   A 46  ? 0.1546 0.1470 0.1974 0.0187  -0.0236 0.0324  46  GLY   A C   
1228 C  C   B GLY   A 46  ? 0.1508 0.1417 0.1486 0.0199  -0.0212 0.0119  46  GLY   A C   
1229 O  O   A GLY   A 46  ? 0.1501 0.1543 0.2399 0.0149  -0.0389 0.0123  46  GLY   A O   
1230 O  O   B GLY   A 46  ? 0.1526 0.1420 0.1682 0.0160  -0.0264 0.0106  46  GLY   A O   
1237 N  N   A GLY   A 47  ? 0.1559 0.1472 0.1732 0.0171  -0.0243 0.0185  47  GLY   A N   
1238 N  N   B GLY   A 47  ? 0.1495 0.1410 0.1413 0.0243  -0.0195 -0.0004 47  GLY   A N   
1239 C  CA  A GLY   A 47  ? 0.1527 0.1479 0.1673 0.0164  -0.0393 -0.0030 47  GLY   A CA  
1240 C  CA  B GLY   A 47  ? 0.1520 0.1443 0.1427 0.0258  -0.0233 -0.0076 47  GLY   A CA  
1241 C  C   A GLY   A 47  ? 0.1504 0.1363 0.1691 0.0157  -0.0414 -0.0028 47  GLY   A C   
1242 C  C   B GLY   A 47  ? 0.1511 0.1432 0.1357 0.0264  -0.0171 -0.0162 47  GLY   A C   
1243 O  O   A GLY   A 47  ? 0.1522 0.1328 0.1695 0.0195  -0.0418 0.0088  47  GLY   A O   
1244 O  O   B GLY   A 47  ? 0.1532 0.1415 0.1374 0.0298  -0.0141 -0.0056 47  GLY   A O   
1251 N  N   A GLY   A 48  ? 0.1442 0.1370 0.1718 0.0159  -0.0459 -0.0034 48  GLY   A N   
1252 N  N   B GLY   A 48  ? 0.1521 0.1496 0.1526 0.0188  -0.0161 -0.0147 48  GLY   A N   
1253 C  CA  A GLY   A 48  ? 0.1431 0.1345 0.1892 0.0078  -0.0421 -0.0131 48  GLY   A CA  
1254 C  CA  B GLY   A 48  ? 0.1491 0.1435 0.1586 0.0171  -0.0095 -0.0135 48  GLY   A CA  
1255 C  C   A GLY   A 48  ? 0.1283 0.1322 0.1703 -0.0047 -0.0195 -0.0068 48  GLY   A C   
1256 C  C   B GLY   A 48  ? 0.1416 0.1413 0.1544 0.0084  0.0058  -0.0039 48  GLY   A C   
1257 O  O   A GLY   A 48  ? 0.1381 0.1342 0.1685 -0.0047 -0.0163 -0.0033 48  GLY   A O   
1258 O  O   B GLY   A 48  ? 0.1499 0.1444 0.1534 0.0022  0.0154  -0.0080 48  GLY   A O   
1265 N  N   A VAL   A 49  ? 0.1248 0.1326 0.1749 -0.0070 -0.0113 -0.0063 49  VAL   A N   
1266 N  N   B VAL   A 49  ? 0.1300 0.1372 0.1497 0.0054  0.0035  0.0048  49  VAL   A N   
1267 C  CA  A VAL   A 49  ? 0.1379 0.1311 0.1616 -0.0094 0.0114  -0.0085 49  VAL   A CA  
1268 C  CA  B VAL   A 49  ? 0.1217 0.1341 0.1412 0.0030  0.0070  0.0148  49  VAL   A CA  
1269 C  C   A VAL   A 49  ? 0.1301 0.1204 0.1284 0.0051  0.0106  -0.0054 49  VAL   A C   
1270 C  C   B VAL   A 49  ? 0.1159 0.1237 0.1304 0.0071  0.0092  0.0108  49  VAL   A C   
1271 O  O   A VAL   A 49  ? 0.1326 0.1292 0.1379 -0.0022 0.0188  -0.0029 49  VAL   A O   
1272 O  O   B VAL   A 49  ? 0.1161 0.1114 0.1331 0.0107  0.0082  0.0088  49  VAL   A O   
1273 C  CB  A VAL   A 49  ? 0.1545 0.1391 0.1731 -0.0163 0.0177  -0.0139 49  VAL   A CB  
1274 C  CB  B VAL   A 49  ? 0.1210 0.1311 0.1369 0.0051  0.0049  0.0158  49  VAL   A CB  
1275 C  CG1 A VAL   A 49  ? 0.1594 0.1299 0.1652 -0.0021 0.0223  -0.0073 49  VAL   A CG1 
1276 C  CG1 B VAL   A 49  ? 0.1204 0.1304 0.1414 0.0128  -0.0030 0.0142  49  VAL   A CG1 
1277 C  CG2 A VAL   A 49  ? 0.1692 0.1494 0.2245 -0.0290 0.0138  -0.0121 49  VAL   A CG2 
1278 C  CG2 B VAL   A 49  ? 0.1235 0.1369 0.1309 0.0042  0.0143  0.0197  49  VAL   A CG2 
1297 N  N   A ALA   A 50  ? 0.1273 0.1224 0.1282 -0.0019 -0.0089 0.0032  50  ALA   A N   
1298 N  N   B ALA   A 50  ? 0.1148 0.1232 0.1256 0.0065  0.0064  0.0112  50  ALA   A N   
1299 C  CA  A ALA   A 50  ? 0.1211 0.1225 0.1312 -0.0074 -0.0030 0.0125  50  ALA   A CA  
1300 C  CA  B ALA   A 50  ? 0.1172 0.1246 0.1336 -0.0009 0.0013  0.0094  50  ALA   A CA  
1301 C  C   A ALA   A 50  ? 0.1208 0.1287 0.1249 -0.0090 -0.0069 0.0049  50  ALA   A C   
1302 C  C   B ALA   A 50  ? 0.1204 0.1255 0.1344 -0.0021 -0.0027 0.0069  50  ALA   A C   
1303 O  O   A ALA   A 50  ? 0.1194 0.1273 0.1495 -0.0003 -0.0025 0.0031  50  ALA   A O   
1304 O  O   B ALA   A 50  ? 0.1189 0.1258 0.1467 0.0016  -0.0007 0.0061  50  ALA   A O   
1305 C  CB  A ALA   A 50  ? 0.1186 0.1238 0.1225 -0.0080 0.0063  0.0064  50  ALA   A CB  
1306 C  CB  B ALA   A 50  ? 0.1173 0.1284 0.1379 -0.0039 0.0053  -0.0008 50  ALA   A CB  
1317 N  N   . GLY   A 51  ? 0.1253 0.1207 0.1459 0.0011  -0.0091 0.0052  51  GLY   A N   
1318 C  CA  . GLY   A 51  ? 0.1357 0.1183 0.1435 0.0062  -0.0131 0.0051  51  GLY   A CA  
1319 C  C   . GLY   A 51  ? 0.1230 0.1330 0.1422 0.0089  -0.0061 -0.0062 51  GLY   A C   
1320 O  O   . GLY   A 51  ? 0.1274 0.1388 0.1611 0.0016  -0.0095 -0.0086 51  GLY   A O   
1325 N  N   . ALA   A 52  ? 0.1194 0.1421 0.1449 0.0029  0.0002  -0.0112 52  ALA   A N   
1326 C  CA  . ALA   A 52  ? 0.1239 0.1534 0.1586 0.0003  0.0068  -0.0143 52  ALA   A CA  
1327 C  C   . ALA   A 52  ? 0.1228 0.1478 0.1341 -0.0115 0.0057  -0.0097 52  ALA   A C   
1328 O  O   . ALA   A 52  ? 0.1324 0.1558 0.1475 -0.0053 0.0050  -0.0108 52  ALA   A O   
1329 C  CB  . ALA   A 52  ? 0.1319 0.1856 0.1735 -0.0136 -0.0010 0.0034  52  ALA   A CB  
1335 N  N   A LEU   A 53  ? 0.1215 0.1468 0.1418 -0.0099 0.0032  -0.0029 53  LEU   A N   
1336 N  N   B LEU   A 53  ? 0.1212 0.1454 0.1345 -0.0061 0.0057  -0.0012 53  LEU   A N   
1337 C  CA  A LEU   A 53  ? 0.1339 0.1513 0.1241 -0.0095 0.0002  0.0023  53  LEU   A CA  
1338 C  CA  B LEU   A 53  ? 0.1251 0.1449 0.1247 -0.0020 0.0065  0.0057  53  LEU   A CA  
1339 C  C   A LEU   A 53  ? 0.1298 0.1499 0.1050 -0.0017 0.0028  0.0003  53  LEU   A C   
1340 C  C   B LEU   A 53  ? 0.1269 0.1439 0.1165 -0.0004 0.0080  0.0026  53  LEU   A C   
1341 O  O   A LEU   A 53  ? 0.1406 0.1547 0.1196 -0.0075 -0.0060 -0.0010 53  LEU   A O   
1342 O  O   B LEU   A 53  ? 0.1346 0.1424 0.1247 -0.0061 0.0108  0.0034  53  LEU   A O   
1343 C  CB  A LEU   A 53  ? 0.1488 0.1523 0.1258 -0.0168 0.0032  0.0022  53  LEU   A CB  
1344 C  CB  B LEU   A 53  ? 0.1277 0.1391 0.1248 0.0001  0.0074  0.0088  53  LEU   A CB  
1345 C  CG  A LEU   A 53  ? 0.1691 0.1551 0.1449 -0.0215 0.0028  0.0036  53  LEU   A CG  
1346 C  CG  B LEU   A 53  ? 0.1290 0.1316 0.1166 0.0017  0.0011  0.0107  53  LEU   A CG  
1347 C  CD1 A LEU   A 53  ? 0.1869 0.1633 0.1541 -0.0147 0.0057  -0.0003 53  LEU   A CD1 
1348 C  CD1 B LEU   A 53  ? 0.1408 0.1351 0.1267 0.0059  0.0025  0.0142  53  LEU   A CD1 
1349 C  CD2 A LEU   A 53  ? 0.1763 0.1722 0.1552 -0.0194 -0.0020 0.0102  53  LEU   A CD2 
1350 C  CD2 B LEU   A 53  ? 0.1244 0.1299 0.1099 0.0023  -0.0004 0.0059  53  LEU   A CD2 
1373 N  N   . ASN   A 54  ? 0.1246 0.1406 0.1209 -0.0014 -0.0045 0.0063  54  ASN   A N   
1374 C  CA  . ASN   A 54  ? 0.1177 0.1348 0.1341 -0.0008 -0.0052 0.0009  54  ASN   A CA  
1375 C  C   . ASN   A 54  ? 0.1346 0.1391 0.1239 -0.0111 -0.0001 0.0040  54  ASN   A C   
1376 O  O   . ASN   A 54  ? 0.1340 0.1468 0.1431 -0.0091 -0.0045 -0.0063 54  ASN   A O   
1377 C  CB  . ASN   A 54  ? 0.1176 0.1335 0.1377 -0.0074 -0.0092 0.0004  54  ASN   A CB  
1378 C  CG  . ASN   A 54  ? 0.1200 0.1367 0.1384 -0.0001 -0.0037 0.0000  54  ASN   A CG  
1379 O  OD1 . ASN   A 54  ? 0.1221 0.1383 0.1442 0.0005  -0.0089 0.0034  54  ASN   A OD1 
1380 N  ND2 . ASN   A 54  ? 0.1298 0.1438 0.1541 -0.0117 -0.0146 0.0142  54  ASN   A ND2 
1388 N  N   . LYS   A 55  ? 0.1301 0.1413 0.1396 -0.0056 -0.0020 -0.0053 55  LYS   A N   
1389 C  CA  . LYS   A 55  ? 0.1396 0.1501 0.1486 0.0043  -0.0085 -0.0160 55  LYS   A CA  
1390 C  C   . LYS   A 55  ? 0.1335 0.1609 0.1456 -0.0026 0.0006  -0.0247 55  LYS   A C   
1391 O  O   . LYS   A 55  ? 0.1430 0.1735 0.1580 0.0058  -0.0071 -0.0292 55  LYS   A O   
1392 C  CB  . LYS   A 55  ? 0.1449 0.1587 0.1637 0.0104  -0.0063 -0.0196 55  LYS   A CB  
1393 C  CG  . LYS   A 55  ? 0.1565 0.1910 0.1816 0.0299  -0.0178 -0.0307 55  LYS   A CG  
1394 C  CD  . LYS   A 55  ? 0.1689 0.2244 0.1956 0.0400  -0.0204 -0.0326 55  LYS   A CD  
1395 C  CE  . LYS   A 55  ? 0.1902 0.2539 0.2195 0.0480  -0.0236 -0.0297 55  LYS   A CE  
1396 N  NZ  . LYS   A 55  ? 0.1976 0.2674 0.2319 0.0551  -0.0243 -0.0227 55  LYS   A NZ  
1410 N  N   . ALA   A 56  ? 0.1394 0.1662 0.1504 -0.0077 -0.0029 -0.0193 56  ALA   A N   
1411 C  CA  . ALA   A 56  ? 0.1547 0.1858 0.1461 -0.0117 0.0021  -0.0200 56  ALA   A CA  
1412 C  C   . ALA   A 56  ? 0.1538 0.1929 0.1192 -0.0101 0.0041  -0.0232 56  ALA   A C   
1413 O  O   . ALA   A 56  ? 0.1606 0.2278 0.1387 0.0051  0.0127  -0.0158 56  ALA   A O   
1414 C  CB  . ALA   A 56  ? 0.1549 0.2066 0.1435 -0.0179 0.0101  -0.0051 56  ALA   A CB  
1420 N  N   . THR   A 57  ? 0.1375 0.1703 0.1259 -0.0102 0.0089  -0.0181 57  THR   A N   
1421 C  CA  . THR   A 57  ? 0.1457 0.1675 0.1305 -0.0142 -0.0051 -0.0185 57  THR   A CA  
1422 C  C   . THR   A 57  ? 0.1473 0.1771 0.1402 -0.0058 -0.0070 -0.0182 57  THR   A C   
1423 O  O   . THR   A 57  ? 0.1408 0.1789 0.1681 -0.0138 -0.0148 -0.0216 57  THR   A O   
1424 C  CB  . THR   A 57  ? 0.1403 0.1688 0.1353 -0.0131 0.0003  -0.0100 57  THR   A CB  
1425 O  OG1 . THR   A 57  ? 0.1300 0.1627 0.1421 -0.0078 -0.0034 -0.0070 57  THR   A OG1 
1426 C  CG2 . THR   A 57  ? 0.1434 0.1668 0.1321 -0.0062 -0.0025 0.0042  57  THR   A CG2 
1434 N  N   . ASN   A 58  ? 0.1443 0.1716 0.1672 -0.0063 0.0023  -0.0296 58  ASN   A N   
1435 C  CA  . ASN   A 58  ? 0.1630 0.1659 0.1830 -0.0093 0.0057  -0.0366 58  ASN   A CA  
1436 C  C   . ASN   A 58  ? 0.1432 0.1510 0.1680 -0.0018 0.0010  -0.0218 58  ASN   A C   
1437 O  O   . ASN   A 58  ? 0.1470 0.1658 0.1826 -0.0175 -0.0007 -0.0237 58  ASN   A O   
1438 C  CB  . ASN   A 58  ? 0.2070 0.1793 0.2176 -0.0120 0.0347  -0.0469 58  ASN   A CB  
1439 C  CG  . ASN   A 58  ? 0.2506 0.2053 0.2845 -0.0102 0.0290  -0.0282 58  ASN   A CG  
1440 O  OD1 . ASN   A 58  ? 0.2790 0.2014 0.3216 0.0183  0.0578  -0.0252 58  ASN   A OD1 
1441 N  ND2 . ASN   A 58  ? 0.2599 0.2151 0.3028 -0.0130 0.0125  -0.0303 58  ASN   A ND2 
1448 N  N   . ASN   A 59  ? 0.1306 0.1419 0.1564 -0.0045 -0.0121 -0.0121 59  ASN   A N   
1449 C  CA  . ASN   A 59  ? 0.1299 0.1322 0.1521 -0.0036 -0.0067 -0.0093 59  ASN   A CA  
1450 C  C   . ASN   A 59  ? 0.1351 0.1372 0.1393 -0.0063 -0.0066 -0.0052 59  ASN   A C   
1451 O  O   . ASN   A 59  ? 0.1335 0.1383 0.1515 -0.0047 0.0008  0.0043  59  ASN   A O   
1452 C  CB  . ASN   A 59  ? 0.1374 0.1334 0.1560 0.0014  -0.0185 -0.0166 59  ASN   A CB  
1453 C  CG  . ASN   A 59  ? 0.1395 0.1403 0.1598 -0.0001 -0.0254 0.0002  59  ASN   A CG  
1454 O  OD1 . ASN   A 59  ? 0.1508 0.1437 0.1531 -0.0079 -0.0205 0.0011  59  ASN   A OD1 
1455 N  ND2 . ASN   A 59  ? 0.1488 0.1436 0.1744 -0.0110 -0.0191 0.0074  59  ASN   A ND2 
1462 N  N   . ALA   A 60  ? 0.1300 0.1439 0.1370 -0.0031 -0.0017 0.0018  60  ALA   A N   
1463 C  CA  . ALA   A 60  ? 0.1291 0.1437 0.1542 -0.0020 -0.0077 0.0029  60  ALA   A CA  
1464 C  C   . ALA   A 60  ? 0.1260 0.1368 0.1596 -0.0058 -0.0071 0.0006  60  ALA   A C   
1465 O  O   . ALA   A 60  ? 0.1214 0.1383 0.1783 -0.0035 -0.0101 -0.0052 60  ALA   A O   
1466 C  CB  . ALA   A 60  ? 0.1422 0.1551 0.1577 0.0023  -0.0169 -0.0154 60  ALA   A CB  
1472 N  N   . MET   A 61  ? 0.1226 0.1327 0.1494 -0.0064 -0.0019 -0.0051 61  MET   A N   
1473 C  CA  . MET   A 61  ? 0.1269 0.1318 0.1348 -0.0067 0.0071  0.0046  61  MET   A CA  
1474 C  C   . MET   A 61  ? 0.1222 0.1293 0.1499 -0.0075 -0.0065 -0.0069 61  MET   A C   
1475 O  O   . MET   A 61  ? 0.1274 0.1278 0.1610 -0.0051 0.0059  0.0054  61  MET   A O   
1476 C  CB  . MET   A 61  ? 0.1314 0.1331 0.1268 -0.0032 0.0011  0.0044  61  MET   A CB  
1477 C  CG  . MET   A 61  ? 0.1284 0.1387 0.1522 -0.0033 -0.0006 0.0026  61  MET   A CG  
1478 S  SD  . MET   A 61  ? 0.1316 0.1413 0.1859 -0.0113 -0.0005 -0.0149 61  MET   A SD  
1479 C  CE  . MET   A 61  ? 0.1479 0.1565 0.2023 -0.0164 0.0173  -0.0109 61  MET   A CE  
1489 N  N   . GLN   A 62  ? 0.1221 0.1243 0.1537 -0.0114 -0.0064 -0.0035 62  GLN   A N   
1490 C  CA  . GLN   A 62  ? 0.1248 0.1226 0.1568 -0.0020 0.0042  0.0067  62  GLN   A CA  
1491 C  C   . GLN   A 62  ? 0.1299 0.1137 0.1559 0.0006  0.0055  0.0062  62  GLN   A C   
1492 O  O   . GLN   A 62  ? 0.1320 0.1296 0.1520 -0.0016 0.0038  0.0010  62  GLN   A O   
1493 C  CB  . GLN   A 62  ? 0.1239 0.1216 0.1552 -0.0025 0.0009  0.0022  62  GLN   A CB  
1494 C  CG  . GLN   A 62  ? 0.1279 0.1198 0.1543 -0.0076 -0.0011 0.0161  62  GLN   A CG  
1495 C  CD  . GLN   A 62  ? 0.1328 0.1274 0.1546 0.0001  0.0042  0.0164  62  GLN   A CD  
1496 O  OE1 . GLN   A 62  ? 0.1352 0.1432 0.1624 -0.0021 0.0016  0.0061  62  GLN   A OE1 
1497 N  NE2 . GLN   A 62  ? 0.1393 0.1300 0.1705 0.0044  -0.0009 -0.0008 62  GLN   A NE2 
1506 N  N   . VAL   A 63  ? 0.1212 0.1233 0.1709 -0.0034 0.0095  -0.0145 63  VAL   A N   
1507 C  CA  . VAL   A 63  ? 0.1228 0.1335 0.1909 -0.0129 0.0029  -0.0115 63  VAL   A CA  
1508 C  C   . VAL   A 63  ? 0.1136 0.1314 0.1750 -0.0138 -0.0069 -0.0112 63  VAL   A C   
1509 O  O   . VAL   A 63  ? 0.1172 0.1328 0.1912 -0.0120 0.0007  -0.0059 63  VAL   A O   
1510 C  CB  . VAL   A 63  ? 0.1379 0.1533 0.2217 -0.0163 0.0004  -0.0324 63  VAL   A CB  
1511 C  CG1 . VAL   A 63  ? 0.1498 0.1746 0.2632 -0.0131 -0.0084 -0.0537 63  VAL   A CG1 
1512 C  CG2 . VAL   A 63  ? 0.1464 0.1430 0.2372 -0.0145 0.0111  -0.0249 63  VAL   A CG2 
1522 N  N   . GLU   A 64  ? 0.1238 0.1397 0.1629 -0.0058 -0.0020 -0.0090 64  GLU   A N   
1523 C  CA  . GLU   A 64  ? 0.1207 0.1397 0.1703 -0.0084 -0.0097 -0.0012 64  GLU   A CA  
1524 C  C   . GLU   A 64  ? 0.1139 0.1309 0.1655 -0.0100 0.0023  0.0034  64  GLU   A C   
1525 O  O   . GLU   A 64  ? 0.1261 0.1396 0.1705 -0.0035 0.0002  -0.0011 64  GLU   A O   
1526 C  CB  . GLU   A 64  ? 0.1306 0.1485 0.1740 -0.0093 -0.0019 0.0011  64  GLU   A CB  
1527 C  CG  . GLU   A 64  ? 0.1421 0.1501 0.1809 -0.0113 -0.0025 -0.0004 64  GLU   A CG  
1528 C  CD  . GLU   A 64  ? 0.1513 0.1616 0.1851 -0.0165 0.0051  0.0036  64  GLU   A CD  
1529 O  OE1 . GLU   A 64  ? 0.1534 0.1734 0.2155 -0.0223 0.0135  0.0078  64  GLU   A OE1 
1530 O  OE2 . GLU   A 64  ? 0.1684 0.1656 0.1828 -0.0219 -0.0093 0.0129  64  GLU   A OE2 
1537 N  N   . SER   A 65  ? 0.1117 0.1318 0.1572 0.0008  -0.0033 0.0013  65  SER   A N   
1538 C  CA  . SER   A 65  ? 0.1212 0.1278 0.1502 -0.0073 -0.0043 -0.0020 65  SER   A CA  
1539 C  C   . SER   A 65  ? 0.1216 0.1350 0.1551 -0.0060 -0.0057 -0.0025 65  SER   A C   
1540 O  O   . SER   A 65  ? 0.1356 0.1383 0.1689 -0.0007 0.0127  0.0017  65  SER   A O   
1541 C  CB  . SER   A 65  ? 0.1256 0.1262 0.1490 -0.0066 0.0051  0.0087  65  SER   A CB  
1542 O  OG  . SER   A 65  ? 0.1223 0.1396 0.1586 -0.0087 -0.0040 0.0152  65  SER   A OG  
1548 N  N   . ASP   A 66  ? 0.1224 0.1275 0.1656 -0.0081 0.0090  0.0052  66  ASP   A N   
1549 C  CA  . ASP   A 66  ? 0.1356 0.1388 0.1818 -0.0034 0.0047  0.0194  66  ASP   A CA  
1550 C  C   . ASP   A 66  ? 0.1284 0.1373 0.1886 -0.0067 0.0090  0.0216  66  ASP   A C   
1551 O  O   . ASP   A 66  ? 0.1350 0.1503 0.2052 -0.0038 0.0295  0.0261  66  ASP   A O   
1552 C  CB  . ASP   A 66  ? 0.1420 0.1485 0.2085 0.0078  0.0137  0.0374  66  ASP   A CB  
1553 C  CG  . ASP   A 66  ? 0.1679 0.1605 0.2347 0.0005  -0.0010 0.0555  66  ASP   A CG  
1554 O  OD1 . ASP   A 66  ? 0.1632 0.1948 0.2098 -0.0075 -0.0083 0.0532  66  ASP   A OD1 
1555 O  OD2 . ASP   A 66  ? 0.1852 0.1773 0.3150 0.0221  -0.0155 0.0311  66  ASP   A OD2 
1560 N  N   . ASP   A 67  ? 0.1205 0.1377 0.1986 -0.0071 0.0040  0.0231  67  ASP   A N   
1561 C  CA  . ASP   A 67  ? 0.1261 0.1547 0.2055 -0.0033 -0.0037 0.0277  67  ASP   A CA  
1562 C  C   . ASP   A 67  ? 0.1285 0.1559 0.1977 -0.0006 0.0094  0.0273  67  ASP   A C   
1563 O  O   . ASP   A 67  ? 0.1260 0.1650 0.2241 0.0023  0.0239  0.0380  67  ASP   A O   
1564 C  CB  . ASP   A 67  ? 0.1346 0.1671 0.2365 -0.0029 -0.0176 0.0310  67  ASP   A CB  
1565 C  CG  . ASP   A 67  ? 0.1296 0.1839 0.2721 -0.0091 -0.0240 0.0425  67  ASP   A CG  
1566 O  OD1 . ASP   A 67  ? 0.1339 0.2029 0.3528 -0.0128 -0.0324 0.0552  67  ASP   A OD1 
1567 O  OD2 . ASP   A 67  ? 0.1348 0.1880 0.2591 0.0019  -0.0178 0.0364  67  ASP   A OD2 
1572 N  N   . TYR   A 68  ? 0.1297 0.1426 0.1909 0.0038  0.0163  0.0292  68  TYR   A N   
1573 C  CA  . TYR   A 68  ? 0.1391 0.1396 0.1900 0.0045  0.0236  0.0278  68  TYR   A CA  
1574 C  C   . TYR   A 68  ? 0.1318 0.1411 0.1944 0.0020  0.0228  0.0221  68  TYR   A C   
1575 O  O   . TYR   A 68  ? 0.1393 0.1442 0.2030 0.0068  0.0303  0.0212  68  TYR   A O   
1576 C  CB  . TYR   A 68  ? 0.1446 0.1402 0.2018 0.0079  0.0375  0.0326  68  TYR   A CB  
1577 C  CG  . TYR   A 68  ? 0.1463 0.1567 0.2341 0.0053  0.0414  0.0359  68  TYR   A CG  
1578 C  CD1 . TYR   A 68  ? 0.1580 0.1649 0.2637 -0.0175 0.0438  -0.0028 68  TYR   A CD1 
1579 C  CD2 . TYR   A 68  ? 0.1713 0.1601 0.2713 0.0146  0.0516  0.0438  68  TYR   A CD2 
1580 C  CE1 . TYR   A 68  ? 0.1634 0.1728 0.2969 -0.0176 0.0506  -0.0158 68  TYR   A CE1 
1581 C  CE2 . TYR   A 68  ? 0.1701 0.1621 0.2944 0.0053  0.0661  0.0193  68  TYR   A CE2 
1582 C  CZ  . TYR   A 68  ? 0.1694 0.1672 0.3107 -0.0151 0.0546  -0.0080 68  TYR   A CZ  
1583 O  OH  . TYR   A 68  ? 0.1963 0.1649 0.3271 -0.0115 0.0332  -0.0294 68  TYR   A OH  
1593 N  N   . ILE   A 69  ? 0.1240 0.1322 0.1909 0.0024  0.0202  0.0204  69  ILE   A N   
1594 C  CA  . ILE   A 69  ? 0.1373 0.1375 0.1806 0.0022  0.0158  0.0077  69  ILE   A CA  
1595 C  C   . ILE   A 69  ? 0.1383 0.1396 0.1755 0.0072  0.0189  0.0148  69  ILE   A C   
1596 O  O   . ILE   A 69  ? 0.1449 0.1453 0.1732 -0.0005 0.0212  0.0181  69  ILE   A O   
1597 C  CB  . ILE   A 69  ? 0.1411 0.1567 0.1789 0.0069  0.0166  0.0034  69  ILE   A CB  
1598 C  CG1 . ILE   A 69  ? 0.1432 0.1645 0.1879 0.0079  0.0167  -0.0158 69  ILE   A CG1 
1599 C  CG2 . ILE   A 69  ? 0.1643 0.1737 0.1860 0.0148  0.0057  -0.0069 69  ILE   A CG2 
1600 C  CD1 . ILE   A 69  ? 0.1441 0.1776 0.2035 -0.0049 0.0138  -0.0159 69  ILE   A CD1 
1612 N  N   . ALA   A 70  ? 0.1429 0.1426 0.1784 -0.0009 0.0226  0.0225  70  ALA   A N   
1613 C  CA  . ALA   A 70  ? 0.1451 0.1555 0.1995 -0.0171 0.0327  0.0292  70  ALA   A CA  
1614 C  C   . ALA   A 70  ? 0.1386 0.1682 0.1920 -0.0084 0.0256  0.0240  70  ALA   A C   
1615 O  O   . ALA   A 70  ? 0.1617 0.2026 0.2223 0.0145  0.0452  0.0430  70  ALA   A O   
1616 C  CB  . ALA   A 70  ? 0.1505 0.1484 0.2240 -0.0145 0.0251  0.0212  70  ALA   A CB  
1622 N  N   . THR   A 71  ? 0.1350 0.1670 0.1901 -0.0016 0.0185  0.0283  71  THR   A N   
1623 C  CA  . THR   A 71  ? 0.1438 0.1820 0.2227 0.0071  0.0199  0.0332  71  THR   A CA  
1624 C  C   . THR   A 71  ? 0.1357 0.1761 0.2503 0.0172  0.0330  0.0236  71  THR   A C   
1625 O  O   . THR   A 71  ? 0.1436 0.2033 0.2870 0.0148  0.0442  0.0060  71  THR   A O   
1626 C  CB  . THR   A 71  ? 0.1714 0.2127 0.2530 0.0202  -0.0123 0.0414  71  THR   A CB  
1627 O  OG1 . THR   A 71  ? 0.2007 0.2318 0.2616 0.0116  -0.0366 0.0342  71  THR   A OG1 
1628 C  CG2 . THR   A 71  ? 0.1806 0.2296 0.2811 0.0289  -0.0249 0.0454  71  THR   A CG2 
1636 N  N   . ASN   A 72  ? 0.1429 0.1592 0.2221 0.0116  0.0229  0.0280  72  ASN   A N   
1637 C  CA  . ASN   A 72  ? 0.1489 0.1563 0.2210 0.0168  0.0338  0.0274  72  ASN   A CA  
1638 C  C   . ASN   A 72  ? 0.1599 0.1565 0.2109 0.0141  0.0520  0.0213  72  ASN   A C   
1639 O  O   . ASN   A 72  ? 0.1777 0.1566 0.2410 0.0162  0.0491  0.0064  72  ASN   A O   
1640 C  CB  . ASN   A 72  ? 0.1687 0.1647 0.2292 0.0135  0.0356  0.0278  72  ASN   A CB  
1641 C  CG  . ASN   A 72  ? 0.1933 0.1749 0.2434 0.0227  0.0341  0.0350  72  ASN   A CG  
1642 O  OD1 . ASN   A 72  ? 0.2099 0.2074 0.2690 0.0258  0.0426  0.0353  72  ASN   A OD1 
1643 N  ND2 . ASN   A 72  ? 0.2088 0.1724 0.2492 0.0552  0.0177  0.0224  72  ASN   A ND2 
1650 N  N   . GLY   A 73  ? 0.1641 0.1554 0.1956 0.0057  0.0453  0.0174  73  GLY   A N   
1651 C  CA  . GLY   A 73  ? 0.1645 0.1473 0.1818 -0.0061 0.0411  0.0110  73  GLY   A CA  
1652 C  C   . GLY   A 73  ? 0.1666 0.1417 0.1635 0.0032  0.0524  0.0286  73  GLY   A C   
1653 O  O   . GLY   A 73  ? 0.1674 0.1474 0.1928 0.0111  0.0403  0.0329  73  GLY   A O   
1657 N  N   . PRO   A 74  ? 0.1773 0.1474 0.1799 -0.0102 0.0460  0.0172  74  PRO   A N   
1658 C  CA  . PRO   A 74  ? 0.1694 0.1469 0.1938 0.0024  0.0432  0.0146  74  PRO   A CA  
1659 C  C   . PRO   A 74  ? 0.1603 0.1291 0.1847 0.0010  0.0343  0.0073  74  PRO   A C   
1660 O  O   . PRO   A 74  ? 0.1688 0.1357 0.2119 0.0014  0.0408  -0.0026 74  PRO   A O   
1661 C  CB  . PRO   A 74  ? 0.1852 0.1721 0.2184 0.0023  0.0406  0.0255  74  PRO   A CB  
1662 C  CG  . PRO   A 74  ? 0.2141 0.2089 0.2587 -0.0217 0.0336  0.0147  74  PRO   A CG  
1663 C  CD  . PRO   A 74  ? 0.1967 0.1848 0.2064 -0.0236 0.0283  0.0006  74  PRO   A CD  
1671 N  N   . LEU   A 75  ? 0.1584 0.1242 0.1684 -0.0022 0.0262  0.0062  75  LEU   A N   
1672 C  CA  . LEU   A 75  ? 0.1588 0.1242 0.1539 -0.0001 0.0076  0.0090  75  LEU   A CA  
1673 C  C   . LEU   A 75  ? 0.1687 0.1362 0.1448 0.0075  0.0120  0.0154  75  LEU   A C   
1674 O  O   . LEU   A 75  ? 0.2020 0.1540 0.1526 0.0114  0.0078  0.0088  75  LEU   A O   
1675 C  CB  . LEU   A 75  ? 0.1611 0.1294 0.1536 -0.0088 0.0124  0.0159  75  LEU   A CB  
1676 C  CG  . LEU   A 75  ? 0.1784 0.1682 0.1634 -0.0364 0.0062  0.0119  75  LEU   A CG  
1677 C  CD1 . LEU   A 75  ? 0.1914 0.2190 0.1781 -0.0331 -0.0004 0.0018  75  LEU   A CD1 
1678 C  CD2 . LEU   A 75  ? 0.2141 0.2077 0.2171 -0.0097 -0.0024 0.0138  75  LEU   A CD2 
1690 N  N   . LYS   A 76  ? 0.1693 0.1355 0.1722 -0.0056 0.0090  0.0018  76  LYS   A N   
1691 C  CA  . LYS   A 76  ? 0.1649 0.1574 0.1814 -0.0082 0.0159  -0.0068 76  LYS   A CA  
1692 C  C   . LYS   A 76  ? 0.1614 0.1396 0.1405 -0.0057 0.0152  0.0125  76  LYS   A C   
1693 O  O   . LYS   A 76  ? 0.1669 0.1347 0.1477 -0.0045 0.0153  0.0126  76  LYS   A O   
1694 C  CB  . LYS   A 76  ? 0.1655 0.1791 0.2215 0.0008  0.0152  -0.0339 76  LYS   A CB  
1695 C  CG  . LYS   A 76  ? 0.1789 0.1733 0.2674 0.0068  0.0122  -0.0327 76  LYS   A CG  
1696 C  CD  . LYS   A 76  ? 0.1879 0.1750 0.3057 0.0047  -0.0023 -0.0399 76  LYS   A CD  
1697 C  CE  . LYS   A 76  ? 0.2084 0.1964 0.3575 0.0017  0.0021  -0.0436 76  LYS   A CE  
1698 N  NZ  . LYS   A 76  ? 0.2123 0.1892 0.3990 -0.0139 -0.0039 -0.0512 76  LYS   A NZ  
1712 N  N   . VAL   A 77  ? 0.1747 0.1462 0.1493 -0.0027 0.0266  0.0133  77  VAL   A N   
1713 C  CA  . VAL   A 77  ? 0.1700 0.1478 0.1453 0.0036  0.0180  0.0104  77  VAL   A CA  
1714 C  C   . VAL   A 77  ? 0.1661 0.1448 0.1351 0.0065  0.0147  0.0086  77  VAL   A C   
1715 O  O   . VAL   A 77  ? 0.1710 0.1485 0.1488 0.0097  0.0305  -0.0035 77  VAL   A O   
1716 C  CB  . VAL   A 77  ? 0.1874 0.1633 0.1561 0.0014  0.0179  0.0179  77  VAL   A CB  
1717 C  CG1 . VAL   A 77  ? 0.1812 0.1771 0.1695 0.0127  0.0041  0.0059  77  VAL   A CG1 
1718 C  CG2 . VAL   A 77  ? 0.2157 0.1735 0.1791 -0.0023 0.0052  0.0203  77  VAL   A CG2 
1728 N  N   . GLY   A 78  ? 0.1578 0.1388 0.1356 0.0019  0.0214  0.0048  78  GLY   A N   
1729 C  CA  . GLY   A 78  ? 0.1569 0.1348 0.1569 0.0006  0.0218  0.0151  78  GLY   A CA  
1730 C  C   . GLY   A 78  ? 0.1477 0.1281 0.1519 0.0043  0.0251  0.0132  78  GLY   A C   
1731 O  O   . GLY   A 78  ? 0.1463 0.1383 0.1751 0.0036  0.0209  0.0253  78  GLY   A O   
1735 N  N   . GLY   A 79  ? 0.1500 0.1257 0.1476 0.0000  0.0176  0.0174  79  GLY   A N   
1736 C  CA  . GLY   A 79  ? 0.1482 0.1339 0.1613 0.0008  0.0210  0.0143  79  GLY   A CA  
1737 C  C   . GLY   A 79  ? 0.1375 0.1318 0.1506 0.0001  0.0093  0.0070  79  GLY   A C   
1738 O  O   . GLY   A 79  ? 0.1359 0.1374 0.1637 0.0179  0.0062  0.0083  79  GLY   A O   
1742 N  N   . SER   A 80  ? 0.1311 0.1451 0.1634 0.0015  0.0133  0.0001  80  SER   A N   
1743 C  CA  . SER   A 80  ? 0.1266 0.1377 0.1542 -0.0034 0.0080  0.0013  80  SER   A CA  
1744 C  C   . SER   A 80  ? 0.1271 0.1357 0.1486 -0.0038 0.0050  0.0099  80  SER   A C   
1745 O  O   . SER   A 80  ? 0.1279 0.1598 0.1909 0.0087  0.0134  -0.0007 80  SER   A O   
1746 C  CB  . SER   A 80  ? 0.1445 0.1352 0.1896 -0.0060 0.0171  0.0063  80  SER   A CB  
1747 O  OG  . SER   A 80  ? 0.1664 0.1332 0.2272 0.0029  -0.0004 0.0284  80  SER   A OG  
1753 N  N   . CYS   A 81  ? 0.1215 0.1331 0.1545 -0.0047 -0.0011 0.0109  81  CYS   A N   
1754 C  CA  . CYS   A 81  ? 0.1215 0.1419 0.1510 -0.0049 -0.0064 0.0245  81  CYS   A CA  
1755 C  C   . CYS   A 81  ? 0.1257 0.1342 0.1494 -0.0112 -0.0022 0.0271  81  CYS   A C   
1756 O  O   . CYS   A 81  ? 0.1204 0.1661 0.1748 -0.0007 0.0017  0.0388  81  CYS   A O   
1757 C  CB  . CYS   A 81  ? 0.1285 0.1431 0.1721 -0.0079 -0.0004 0.0291  81  CYS   A CB  
1758 S  SG  . CYS   A 81  ? 0.1423 0.1349 0.1713 -0.0137 0.0026  0.0173  81  CYS   A SG  
1764 N  N   . VAL   A 82  ? 0.1278 0.1406 0.1596 -0.0034 -0.0128 0.0226  82  VAL   A N   
1765 C  CA  . VAL   A 82  ? 0.1419 0.1498 0.1586 -0.0008 -0.0058 0.0309  82  VAL   A CA  
1766 C  C   . VAL   A 82  ? 0.1383 0.1564 0.1656 -0.0016 -0.0157 0.0303  82  VAL   A C   
1767 O  O   . VAL   A 82  ? 0.1307 0.1591 0.1936 -0.0008 -0.0081 0.0064  82  VAL   A O   
1768 C  CB  . VAL   A 82  ? 0.1713 0.1651 0.1673 0.0018  0.0027  0.0354  82  VAL   A CB  
1769 C  CG1 . VAL   A 82  ? 0.1915 0.1783 0.1880 0.0069  0.0092  0.0421  82  VAL   A CG1 
1770 C  CG2 . VAL   A 82  ? 0.1761 0.1701 0.1988 -0.0020 -0.0043 0.0332  82  VAL   A CG2 
1780 N  N   . LEU   A 83  ? 0.1327 0.1535 0.1550 -0.0114 -0.0074 0.0179  83  LEU   A N   
1781 C  CA  . LEU   A 83  ? 0.1357 0.1509 0.1413 -0.0089 -0.0065 0.0126  83  LEU   A CA  
1782 C  C   . LEU   A 83  ? 0.1380 0.1516 0.1405 -0.0132 -0.0151 0.0199  83  LEU   A C   
1783 O  O   . LEU   A 83  ? 0.1484 0.1571 0.1559 -0.0176 -0.0159 0.0285  83  LEU   A O   
1784 C  CB  . LEU   A 83  ? 0.1474 0.1526 0.1428 -0.0133 -0.0091 0.0206  83  LEU   A CB  
1785 C  CG  . LEU   A 83  ? 0.1585 0.1638 0.1520 -0.0144 0.0013  0.0091  83  LEU   A CG  
1786 C  CD1 . LEU   A 83  ? 0.1707 0.1640 0.1601 -0.0246 0.0004  0.0218  83  LEU   A CD1 
1787 C  CD2 . LEU   A 83  ? 0.1485 0.1829 0.1743 -0.0173 0.0089  0.0210  83  LEU   A CD2 
1799 N  N   . SER   A 84  ? 0.1575 0.1599 0.1449 -0.0180 -0.0129 0.0267  84  SER   A N   
1800 C  CA  . SER   A 84  ? 0.1661 0.1654 0.1272 -0.0151 -0.0134 0.0238  84  SER   A CA  
1801 C  C   . SER   A 84  ? 0.1669 0.1662 0.1274 -0.0208 -0.0025 0.0204  84  SER   A C   
1802 O  O   . SER   A 84  ? 0.1646 0.1763 0.1270 -0.0132 -0.0114 0.0194  84  SER   A O   
1803 C  CB  . SER   A 84  ? 0.1729 0.1896 0.1457 -0.0137 -0.0117 0.0121  84  SER   A CB  
1804 O  OG  . SER   A 84  ? 0.1761 0.2064 0.1579 -0.0138 -0.0217 0.0003  84  SER   A OG  
1810 N  N   . GLY   A 85  ? 0.1816 0.1798 0.1396 -0.0254 0.0073  0.0177  85  GLY   A N   
1811 C  CA  . GLY   A 85  ? 0.1841 0.1890 0.1580 -0.0274 0.0116  0.0001  85  GLY   A CA  
1812 C  C   . GLY   A 85  ? 0.1755 0.1925 0.1366 -0.0239 -0.0059 0.0099  85  GLY   A C   
1813 O  O   . GLY   A 85  ? 0.1768 0.2029 0.1463 -0.0352 0.0112  -0.0097 85  GLY   A O   
1817 N  N   . HIS   A 86  ? 0.1735 0.1832 0.1286 -0.0232 -0.0086 0.0101  86  HIS   A N   
1818 C  CA  . HIS   A 86  ? 0.1949 0.1936 0.1220 -0.0272 -0.0019 0.0145  86  HIS   A CA  
1819 C  C   . HIS   A 86  ? 0.2172 0.2097 0.1149 -0.0328 -0.0104 0.0074  86  HIS   A C   
1820 O  O   . HIS   A 86  ? 0.2299 0.2362 0.1263 -0.0230 0.0092  0.0084  86  HIS   A O   
1821 C  CB  . HIS   A 86  ? 0.1962 0.1839 0.1299 -0.0193 0.0055  0.0109  86  HIS   A CB  
1822 C  CG  . HIS   A 86  ? 0.1877 0.1850 0.1371 -0.0108 0.0012  0.0163  86  HIS   A CG  
1823 N  ND1 . HIS   A 86  ? 0.1956 0.1837 0.1707 -0.0181 -0.0026 0.0147  86  HIS   A ND1 
1824 C  CD2 . HIS   A 86  ? 0.1885 0.1830 0.1288 0.0021  0.0100  0.0207  86  HIS   A CD2 
1825 C  CE1 . HIS   A 86  ? 0.1870 0.1865 0.1689 -0.0131 0.0183  0.0209  86  HIS   A CE1 
1826 N  NE2 . HIS   A 86  ? 0.1892 0.1825 0.1468 0.0037  0.0178  0.0341  86  HIS   A NE2 
1834 N  N   . ASN   A 87  ? 0.2293 0.2181 0.1324 -0.0274 0.0129  -0.0066 87  ASN   A N   
1835 C  CA  . ASN   A 87  ? 0.2514 0.2270 0.1380 -0.0232 0.0315  -0.0156 87  ASN   A CA  
1836 C  C   . ASN   A 87  ? 0.2495 0.2445 0.1659 -0.0266 0.0559  -0.0009 87  ASN   A C   
1837 O  O   . ASN   A 87  ? 0.2717 0.2606 0.2098 -0.0434 0.0821  -0.0107 87  ASN   A O   
1838 C  CB  . ASN   A 87  ? 0.2677 0.2295 0.1540 -0.0105 0.0345  -0.0156 87  ASN   A CB  
1839 C  CG  . ASN   A 87  ? 0.2773 0.2387 0.1562 -0.0027 0.0501  -0.0053 87  ASN   A CG  
1840 O  OD1 . ASN   A 87  ? 0.2912 0.2323 0.1679 0.0135  0.0497  -0.0001 87  ASN   A OD1 
1841 N  ND2 . ASN   A 87  ? 0.2797 0.2669 0.1744 -0.0064 0.0509  0.0052  87  ASN   A ND2 
1848 N  N   . LEU   A 88  ? 0.2192 0.2316 0.1604 -0.0308 0.0281  0.0093  88  LEU   A N   
1849 C  CA  . LEU   A 88  ? 0.1984 0.2275 0.1731 -0.0332 0.0350  0.0189  88  LEU   A CA  
1850 C  C   . LEU   A 88  ? 0.1949 0.2294 0.1622 -0.0330 0.0286  0.0339  88  LEU   A C   
1851 O  O   . LEU   A 88  ? 0.2020 0.2359 0.1969 -0.0276 0.0342  0.0519  88  LEU   A O   
1852 C  CB  . LEU   A 88  ? 0.1972 0.2327 0.1814 -0.0336 -0.0009 0.0322  88  LEU   A CB  
1853 C  CG  . LEU   A 88  ? 0.2141 0.2438 0.2096 -0.0321 -0.0079 0.0400  88  LEU   A CG  
1854 C  CD1 . LEU   A 88  ? 0.2281 0.2520 0.2102 -0.0385 -0.0057 0.0332  88  LEU   A CD1 
1855 C  CD2 . LEU   A 88  ? 0.2275 0.2577 0.2499 -0.0222 -0.0001 0.0236  88  LEU   A CD2 
1867 N  N   . ALA   A 89  ? 0.1940 0.2211 0.1544 -0.0316 0.0119  0.0120  89  ALA   A N   
1868 C  CA  . ALA   A 89  ? 0.2040 0.2197 0.1394 -0.0296 0.0010  0.0263  89  ALA   A CA  
1869 C  C   . ALA   A 89  ? 0.2097 0.2235 0.1437 -0.0218 -0.0131 0.0223  89  ALA   A C   
1870 O  O   . ALA   A 89  ? 0.1987 0.2183 0.1770 -0.0309 -0.0133 -0.0069 89  ALA   A O   
1871 C  CB  . ALA   A 89  ? 0.1959 0.2140 0.1322 -0.0328 -0.0039 0.0238  89  ALA   A CB  
1877 N  N   . LYS   A 90  ? 0.2171 0.2391 0.1417 -0.0308 -0.0215 0.0310  90  LYS   A N   
1878 C  CA  . LYS   A 90  ? 0.2294 0.2562 0.1456 -0.0248 -0.0359 0.0315  90  LYS   A CA  
1879 C  C   . LYS   A 90  ? 0.2024 0.2355 0.1461 -0.0276 -0.0338 0.0170  90  LYS   A C   
1880 O  O   . LYS   A 90  ? 0.2054 0.2527 0.1819 -0.0288 -0.0420 0.0121  90  LYS   A O   
1881 C  CB  . LYS   A 90  ? 0.2652 0.2954 0.1862 -0.0243 -0.0456 0.0558  90  LYS   A CB  
1882 C  CG  . LYS   A 90  ? 0.3187 0.3384 0.2955 -0.0270 -0.0439 0.0596  90  LYS   A CG  
1883 C  CD  . LYS   A 90  ? 0.3759 0.3905 0.4040 -0.0321 -0.0308 0.0625  90  LYS   A CD  
1884 C  CE  . LYS   A 90  ? 0.4172 0.4276 0.4898 -0.0350 -0.0181 0.0580  90  LYS   A CE  
1885 N  NZ  . LYS   A 90  ? 0.4415 0.4415 0.5436 -0.0364 -0.0114 0.0543  90  LYS   A NZ  
1899 N  N   . HIS   A 91  ? 0.1888 0.2038 0.1200 -0.0278 -0.0353 0.0247  91  HIS   A N   
1900 C  CA  . HIS   A 91  ? 0.1797 0.1862 0.1344 -0.0203 -0.0306 0.0256  91  HIS   A CA  
1901 C  C   . HIS   A 91  ? 0.1579 0.1725 0.1177 -0.0189 -0.0186 0.0278  91  HIS   A C   
1902 O  O   . HIS   A 91  ? 0.1529 0.1843 0.1461 -0.0265 -0.0055 0.0289  91  HIS   A O   
1903 C  CB  . HIS   A 91  ? 0.1968 0.2145 0.1882 0.0005  -0.0467 0.0264  91  HIS   A CB  
1904 C  CG  . HIS   A 91  ? 0.2396 0.2633 0.2517 0.0146  -0.0744 0.0169  91  HIS   A CG  
1905 N  ND1 . HIS   A 91  ? 0.2524 0.2908 0.2999 0.0188  -0.0796 -0.0072 91  HIS   A ND1 
1906 C  CD2 . HIS   A 91  ? 0.2635 0.2835 0.2752 0.0236  -0.0884 0.0281  91  HIS   A CD2 
1907 C  CE1 . HIS   A 91  ? 0.2641 0.2995 0.3130 0.0240  -0.0776 0.0060  91  HIS   A CE1 
1908 N  NE2 . HIS   A 91  ? 0.2740 0.2983 0.3034 0.0308  -0.0871 0.0154  91  HIS   A NE2 
1916 N  N   . CYS   A 92  ? 0.1487 0.1642 0.1272 -0.0194 -0.0146 0.0259  92  CYS   A N   
1917 C  CA  . CYS   A 92  ? 0.1403 0.1538 0.1376 -0.0155 -0.0030 0.0216  92  CYS   A CA  
1918 C  C   . CYS   A 92  ? 0.1373 0.1468 0.1347 -0.0160 0.0011  0.0244  92  CYS   A C   
1919 O  O   . CYS   A 92  ? 0.1405 0.1527 0.1582 -0.0184 0.0017  0.0238  92  CYS   A O   
1920 C  CB  . CYS   A 92  ? 0.1429 0.1584 0.1449 -0.0113 -0.0018 0.0154  92  CYS   A CB  
1921 S  SG  . CYS   A 92  ? 0.1428 0.1450 0.1373 -0.0140 -0.0054 0.0166  92  CYS   A SG  
1927 N  N   . LEU   A 93  ? 0.1382 0.1362 0.1397 -0.0149 0.0080  0.0177  93  LEU   A N   
1928 C  CA  . LEU   A 93  ? 0.1251 0.1340 0.1413 -0.0085 -0.0015 0.0181  93  LEU   A CA  
1929 C  C   . LEU   A 93  ? 0.1260 0.1247 0.1369 -0.0034 0.0046  0.0132  93  LEU   A C   
1930 O  O   . LEU   A 93  ? 0.1170 0.1348 0.1410 -0.0063 0.0001  0.0145  93  LEU   A O   
1931 C  CB  . LEU   A 93  ? 0.1295 0.1376 0.1555 -0.0033 -0.0076 0.0260  93  LEU   A CB  
1932 C  CG  . LEU   A 93  ? 0.1362 0.1358 0.1541 -0.0062 -0.0007 0.0225  93  LEU   A CG  
1933 C  CD1 . LEU   A 93  ? 0.1430 0.1430 0.1825 -0.0045 0.0082  0.0186  93  LEU   A CD1 
1934 C  CD2 . LEU   A 93  ? 0.1512 0.1340 0.1717 -0.0061 -0.0044 0.0182  93  LEU   A CD2 
1946 N  N   . HIS   A 94  ? 0.1177 0.1226 0.1364 -0.0065 0.0015  0.0203  94  HIS   A N   
1947 C  CA  . HIS   A 94  ? 0.1173 0.1242 0.1331 -0.0043 -0.0006 0.0146  94  HIS   A CA  
1948 C  C   . HIS   A 94  ? 0.1150 0.1231 0.1415 -0.0065 0.0026  0.0105  94  HIS   A C   
1949 O  O   . HIS   A 94  ? 0.1182 0.1411 0.1729 0.0013  0.0021  -0.0065 94  HIS   A O   
1950 C  CB  . HIS   A 94  ? 0.1116 0.1176 0.1431 -0.0065 -0.0062 0.0168  94  HIS   A CB  
1951 C  CG  . HIS   A 94  ? 0.1203 0.1206 0.1257 -0.0063 -0.0051 0.0211  94  HIS   A CG  
1952 N  ND1 . HIS   A 94  ? 0.1221 0.1226 0.1371 -0.0048 0.0005  0.0176  94  HIS   A ND1 
1953 C  CD2 . HIS   A 94  ? 0.1281 0.1338 0.1357 -0.0061 -0.0085 0.0136  94  HIS   A CD2 
1954 C  CE1 . HIS   A 94  ? 0.1272 0.1280 0.1415 -0.0075 -0.0051 0.0125  94  HIS   A CE1 
1955 N  NE2 . HIS   A 94  ? 0.1285 0.1309 0.1488 -0.0104 -0.0095 0.0085  94  HIS   A NE2 
1963 N  N   . VAL   A 95  ? 0.1142 0.1172 0.1283 -0.0024 0.0077  0.0096  95  VAL   A N   
1964 C  CA  . VAL   A 95  ? 0.1262 0.1195 0.1250 -0.0054 0.0122  0.0188  95  VAL   A CA  
1965 C  C   . VAL   A 95  ? 0.1275 0.1206 0.1155 -0.0152 0.0070  0.0073  95  VAL   A C   
1966 O  O   . VAL   A 95  ? 0.1300 0.1332 0.1342 0.0048  0.0071  0.0088  95  VAL   A O   
1967 C  CB  . VAL   A 95  ? 0.1250 0.1238 0.1483 -0.0114 0.0057  0.0114  95  VAL   A CB  
1968 C  CG1 . VAL   A 95  ? 0.1401 0.1262 0.1577 -0.0151 0.0025  0.0047  95  VAL   A CG1 
1969 C  CG2 . VAL   A 95  ? 0.1295 0.1292 0.1475 -0.0119 0.0121  0.0233  95  VAL   A CG2 
1979 N  N   . VAL   A 96  ? 0.1263 0.1227 0.1111 -0.0030 0.0101  0.0098  96  VAL   A N   
1980 C  CA  . VAL   A 96  ? 0.1376 0.1228 0.1281 -0.0001 0.0101  0.0200  96  VAL   A CA  
1981 C  C   . VAL   A 96  ? 0.1387 0.1312 0.1354 -0.0047 0.0128  0.0189  96  VAL   A C   
1982 O  O   . VAL   A 96  ? 0.1453 0.1387 0.1574 -0.0085 0.0236  0.0013  96  VAL   A O   
1983 C  CB  . VAL   A 96  ? 0.1384 0.1324 0.1327 -0.0041 0.0242  0.0190  96  VAL   A CB  
1984 C  CG1 . VAL   A 96  ? 0.1508 0.1422 0.1235 -0.0052 0.0138  0.0154  96  VAL   A CG1 
1985 C  CG2 . VAL   A 96  ? 0.1398 0.1387 0.1590 -0.0157 0.0199  0.0131  96  VAL   A CG2 
1995 N  N   . GLY   A 97  ? 0.1334 0.1338 0.1345 -0.0094 0.0082  0.0069  97  GLY   A N   
1996 C  CA  . GLY   A 97  ? 0.1480 0.1439 0.1353 -0.0048 0.0035  0.0184  97  GLY   A CA  
1997 C  C   . GLY   A 97  ? 0.1472 0.1605 0.1222 -0.0106 0.0017  0.0115  97  GLY   A C   
1998 O  O   . GLY   A 97  ? 0.1589 0.1538 0.1499 -0.0104 0.0034  0.0172  97  GLY   A O   
2002 N  N   A PRO   A 98  ? 0.1526 0.1694 0.1126 -0.0045 -0.0037 0.0160  98  PRO   A N   
2003 N  N   B PRO   A 98  ? 0.1582 0.1572 0.1257 -0.0063 -0.0020 0.0134  98  PRO   A N   
2004 C  CA  A PRO   A 98  ? 0.1573 0.1959 0.1178 -0.0094 0.0000  0.0083  98  PRO   A CA  
2005 C  CA  B PRO   A 98  ? 0.1680 0.1628 0.1310 -0.0097 -0.0044 0.0058  98  PRO   A CA  
2006 C  C   A PRO   A 98  ? 0.1553 0.2057 0.1062 -0.0197 0.0059  0.0193  98  PRO   A C   
2007 C  C   B PRO   A 98  ? 0.1841 0.1520 0.1283 -0.0115 -0.0095 0.0141  98  PRO   A C   
2008 O  O   A PRO   A 98  ? 0.1522 0.1910 0.1375 -0.0133 0.0079  0.0225  98  PRO   A O   
2009 O  O   B PRO   A 98  ? 0.1814 0.1419 0.1563 -0.0089 -0.0026 0.0141  98  PRO   A O   
2010 C  CB  A PRO   A 98  ? 0.1708 0.2044 0.1199 0.0035  -0.0074 -0.0038 98  PRO   A CB  
2011 C  CB  B PRO   A 98  ? 0.1714 0.1667 0.1314 -0.0042 -0.0034 0.0084  98  PRO   A CB  
2012 C  CG  A PRO   A 98  ? 0.1758 0.1928 0.1295 0.0017  -0.0046 -0.0110 98  PRO   A CG  
2013 C  CG  B PRO   A 98  ? 0.1761 0.1648 0.1343 -0.0061 -0.0020 0.0087  98  PRO   A CG  
2014 C  CD  A PRO   A 98  ? 0.1611 0.1708 0.1264 -0.0006 -0.0031 0.0045  98  PRO   A CD  
2015 C  CD  B PRO   A 98  ? 0.1653 0.1560 0.1293 -0.0051 -0.0015 0.0133  98  PRO   A CD  
2030 N  N   A ASN   A 99  ? 0.1594 0.2295 0.1090 -0.0172 0.0143  0.0309  99  ASN   A N   
2031 N  N   B ASN   A 99  ? 0.2066 0.1508 0.1013 -0.0066 -0.0147 0.0217  99  ASN   A N   
2032 C  CA  A ASN   A 99  ? 0.1852 0.2455 0.1193 -0.0207 0.0032  0.0396  99  ASN   A CA  
2033 C  CA  B ASN   A 99  ? 0.2291 0.1489 0.0896 -0.0023 -0.0111 0.0380  99  ASN   A CA  
2034 C  C   A ASN   A 99  ? 0.2062 0.2757 0.1136 -0.0389 0.0021  0.0473  99  ASN   A C   
2035 C  C   B ASN   A 99  ? 0.2436 0.1493 0.1017 -0.0019 -0.0188 0.0404  99  ASN   A C   
2036 O  O   A ASN   A 99  ? 0.2150 0.2916 0.1323 -0.0357 -0.0019 0.0303  99  ASN   A O   
2037 O  O   B ASN   A 99  ? 0.2489 0.1270 0.1069 0.0063  -0.0215 0.0197  99  ASN   A O   
2038 C  CB  A ASN   A 99  ? 0.1833 0.2358 0.1266 -0.0187 -0.0049 0.0479  99  ASN   A CB  
2039 C  CB  B ASN   A 99  ? 0.2362 0.1446 0.0981 -0.0019 0.0006  0.0375  99  ASN   A CB  
2040 C  CG  A ASN   A 99  ? 0.1825 0.2314 0.1443 -0.0114 -0.0105 0.0397  99  ASN   A CG  
2041 C  CG  B ASN   A 99  ? 0.2429 0.1493 0.1110 -0.0051 0.0057  0.0399  99  ASN   A CG  
2042 O  OD1 A ASN   A 99  ? 0.1959 0.2406 0.1493 0.0031  -0.0090 0.0208  99  ASN   A OD1 
2043 O  OD1 B ASN   A 99  ? 0.2475 0.1575 0.1036 -0.0022 0.0055  0.0413  99  ASN   A OD1 
2044 N  ND2 A ASN   A 99  ? 0.1817 0.2296 0.1653 -0.0094 -0.0157 0.0541  99  ASN   A ND2 
2045 N  ND2 B ASN   A 99  ? 0.2450 0.1515 0.1452 0.0005  -0.0045 0.0239  99  ASN   A ND2 
2058 N  N   A VAL   A 100 ? 0.2281 0.2909 0.1229 -0.0609 -0.0223 0.0456  100 VAL   A N   
2059 N  N   B VAL   A 100 ? 0.2517 0.1761 0.1352 -0.0062 -0.0248 0.0478  100 VAL   A N   
2060 C  CA  A VAL   A 100 ? 0.2594 0.3113 0.1544 -0.0716 -0.0354 0.0510  100 VAL   A CA  
2061 C  CA  B VAL   A 100 ? 0.2590 0.1943 0.1740 -0.0101 -0.0240 0.0450  100 VAL   A CA  
2062 C  C   A VAL   A 100 ? 0.2722 0.3250 0.1617 -0.0746 -0.0443 0.0777  100 VAL   A C   
2063 C  C   B VAL   A 100 ? 0.2615 0.1960 0.1734 -0.0110 -0.0357 0.0405  100 VAL   A C   
2064 O  O   A VAL   A 100 ? 0.2799 0.3312 0.1787 -0.0711 -0.0214 0.0811  100 VAL   A O   
2065 O  O   B VAL   A 100 ? 0.2630 0.1913 0.1731 -0.0147 -0.0348 0.0329  100 VAL   A O   
2066 C  CB  A VAL   A 100 ? 0.2807 0.3174 0.2050 -0.0805 -0.0403 0.0374  100 VAL   A CB  
2067 C  CB  B VAL   A 100 ? 0.2639 0.2116 0.2122 -0.0074 -0.0174 0.0316  100 VAL   A CB  
2068 C  CG1 A VAL   A 100 ? 0.2804 0.3197 0.2295 -0.0875 -0.0356 0.0369  100 VAL   A CG1 
2069 C  CG1 B VAL   A 100 ? 0.2645 0.2116 0.2279 -0.0092 -0.0113 0.0309  100 VAL   A CG1 
2070 C  CG2 A VAL   A 100 ? 0.2933 0.3195 0.2083 -0.0825 -0.0343 0.0306  100 VAL   A CG2 
2071 C  CG2 B VAL   A 100 ? 0.2668 0.2207 0.2249 -0.0060 -0.0146 0.0235  100 VAL   A CG2 
2090 N  N   A ASN   A 101 ? 0.2783 0.3317 0.1916 -0.0820 -0.0530 0.1049  101 ASN   A N   
2091 N  N   B ASN   A 101 ? 0.2623 0.2017 0.1792 -0.0082 -0.0450 0.0409  101 ASN   A N   
2092 C  CA  A ASN   A 101 ? 0.3010 0.3414 0.2162 -0.0861 -0.0541 0.1235  101 ASN   A CA  
2093 C  CA  B ASN   A 101 ? 0.2671 0.2074 0.1885 -0.0061 -0.0411 0.0402  101 ASN   A CA  
2094 C  C   A ASN   A 101 ? 0.3277 0.3700 0.2428 -0.0907 -0.0201 0.1451  101 ASN   A C   
2095 C  C   B ASN   A 101 ? 0.2818 0.2231 0.1909 -0.0022 -0.0256 0.0561  101 ASN   A C   
2096 O  O   A ASN   A 101 ? 0.3407 0.3771 0.2855 -0.0891 -0.0135 0.1373  101 ASN   A O   
2097 O  O   B ASN   A 101 ? 0.2877 0.2262 0.1764 -0.0016 -0.0218 0.0719  101 ASN   A O   
2098 C  CB  A ASN   A 101 ? 0.2991 0.3245 0.2191 -0.0862 -0.0775 0.1115  101 ASN   A CB  
2099 C  CB  B ASN   A 101 ? 0.2581 0.2003 0.1958 -0.0121 -0.0407 0.0301  101 ASN   A CB  
2100 C  CG  A ASN   A 101 ? 0.2994 0.3092 0.2245 -0.0843 -0.0862 0.0937  101 ASN   A CG  
2101 C  CG  B ASN   A 101 ? 0.2521 0.2026 0.2122 -0.0173 -0.0410 0.0268  101 ASN   A CG  
2102 O  OD1 A ASN   A 101 ? 0.2975 0.3106 0.2464 -0.0697 -0.0863 0.0696  101 ASN   A OD1 
2103 O  OD1 B ASN   A 101 ? 0.2555 0.2083 0.2195 -0.0257 -0.0363 0.0233  101 ASN   A OD1 
2104 N  ND2 A ASN   A 101 ? 0.3020 0.3010 0.2283 -0.0896 -0.0791 0.0960  101 ASN   A ND2 
2105 N  ND2 B ASN   A 101 ? 0.2488 0.2020 0.2289 -0.0129 -0.0359 0.0190  101 ASN   A ND2 
2118 N  N   A LYS   A 102 ? 0.3353 0.3953 0.2668 -0.0968 -0.0031 0.1442  102 LYS   A N   
2119 N  N   B LYS   A 102 ? 0.2921 0.2412 0.2228 -0.0032 -0.0090 0.0525  102 LYS   A N   
2120 C  CA  A LYS   A 102 ? 0.3492 0.4191 0.2772 -0.0944 -0.0054 0.1304  102 LYS   A CA  
2121 C  CA  B LYS   A 102 ? 0.3036 0.2573 0.2387 -0.0073 0.0033  0.0498  102 LYS   A CA  
2122 C  C   A LYS   A 102 ? 0.3567 0.4358 0.2637 -0.0851 -0.0050 0.1196  102 LYS   A C   
2123 C  C   B LYS   A 102 ? 0.3027 0.2566 0.2238 -0.0079 0.0007  0.0633  102 LYS   A C   
2124 O  O   A LYS   A 102 ? 0.3628 0.4467 0.2709 -0.0783 -0.0019 0.1098  102 LYS   A O   
2125 O  O   B LYS   A 102 ? 0.3033 0.2508 0.2122 -0.0127 0.0032  0.0769  102 LYS   A O   
2126 C  CB  A LYS   A 102 ? 0.3625 0.4269 0.3141 -0.0960 -0.0151 0.1161  102 LYS   A CB  
2127 C  CB  B LYS   A 102 ? 0.3170 0.2739 0.2818 -0.0129 0.0099  0.0279  102 LYS   A CB  
2128 C  CG  A LYS   A 102 ? 0.3744 0.4330 0.3485 -0.0963 -0.0273 0.0965  102 LYS   A CG  
2129 C  CG  B LYS   A 102 ? 0.3282 0.2878 0.3245 -0.0169 0.0134  0.0104  102 LYS   A CG  
2130 C  CD  A LYS   A 102 ? 0.3874 0.4404 0.3851 -0.0946 -0.0381 0.0720  102 LYS   A CD  
2131 C  CD  B LYS   A 102 ? 0.3385 0.3008 0.3628 -0.0202 0.0177  -0.0001 102 LYS   A CD  
2132 C  CE  A LYS   A 102 ? 0.3990 0.4462 0.4162 -0.0917 -0.0444 0.0568  102 LYS   A CE  
2133 C  CE  B LYS   A 102 ? 0.3447 0.3107 0.3897 -0.0226 0.0180  -0.0084 102 LYS   A CE  
2134 N  NZ  A LYS   A 102 ? 0.4043 0.4479 0.4309 -0.0938 -0.0468 0.0473  102 LYS   A NZ  
2135 N  NZ  B LYS   A 102 ? 0.3479 0.3162 0.4038 -0.0235 0.0204  -0.0084 102 LYS   A NZ  
2162 N  N   A GLY   A 103 ? 0.3571 0.4451 0.2723 -0.0759 -0.0115 0.0963  103 GLY   A N   
2163 N  N   B GLY   A 103 ? 0.3001 0.2618 0.2190 -0.0065 -0.0089 0.0613  103 GLY   A N   
2164 C  CA  A GLY   A 103 ? 0.3585 0.4512 0.2680 -0.0627 -0.0099 0.0777  103 GLY   A CA  
2165 C  CA  B GLY   A 103 ? 0.2966 0.2639 0.2128 -0.0103 -0.0148 0.0638  103 GLY   A CA  
2166 C  C   A GLY   A 103 ? 0.3535 0.4557 0.2664 -0.0531 -0.0016 0.0609  103 GLY   A C   
2167 C  C   B GLY   A 103 ? 0.2898 0.2628 0.1987 -0.0138 -0.0164 0.0663  103 GLY   A C   
2168 O  O   A GLY   A 103 ? 0.3642 0.4623 0.2822 -0.0499 -0.0006 0.0524  103 GLY   A O   
2169 O  O   B GLY   A 103 ? 0.2898 0.2610 0.1926 -0.0172 -0.0185 0.0759  103 GLY   A O   
2176 N  N   A GLU   A 104 ? 0.3332 0.4490 0.2293 -0.0506 0.0064  0.0502  104 GLU   A N   
2177 N  N   B GLU   A 104 ? 0.2830 0.2626 0.1921 -0.0098 -0.0231 0.0592  104 GLU   A N   
2178 C  CA  A GLU   A 104 ? 0.3064 0.4375 0.1980 -0.0569 0.0116  0.0411  104 GLU   A CA  
2179 C  CA  B GLU   A 104 ? 0.2744 0.2601 0.1837 -0.0104 -0.0268 0.0467  104 GLU   A CA  
2180 C  C   A GLU   A 104 ? 0.3047 0.4439 0.1925 -0.0558 0.0169  0.0185  104 GLU   A C   
2181 C  C   B GLU   A 104 ? 0.2713 0.2587 0.1879 -0.0018 -0.0216 0.0363  104 GLU   A C   
2182 O  O   A GLU   A 104 ? 0.3000 0.4451 0.2085 -0.0579 0.0058  0.0153  104 GLU   A O   
2183 O  O   B GLU   A 104 ? 0.2686 0.2467 0.1891 -0.0022 -0.0224 0.0467  104 GLU   A O   
2184 C  CB  A GLU   A 104 ? 0.2765 0.4183 0.1759 -0.0647 0.0181  0.0623  104 GLU   A CB  
2185 C  CB  B GLU   A 104 ? 0.2709 0.2617 0.1837 -0.0176 -0.0291 0.0455  104 GLU   A CB  
2186 C  CG  A GLU   A 104 ? 0.2556 0.3998 0.1760 -0.0659 0.0121  0.0776  104 GLU   A CG  
2187 C  CG  B GLU   A 104 ? 0.2724 0.2683 0.1999 -0.0216 -0.0344 0.0425  104 GLU   A CG  
2188 C  CD  A GLU   A 104 ? 0.2327 0.3833 0.1679 -0.0704 0.0154  0.0898  104 GLU   A CD  
2189 C  CD  B GLU   A 104 ? 0.2730 0.2722 0.2098 -0.0237 -0.0375 0.0399  104 GLU   A CD  
2190 O  OE1 A GLU   A 104 ? 0.2132 0.3640 0.1377 -0.0650 0.0050  0.0851  104 GLU   A OE1 
2191 O  OE1 B GLU   A 104 ? 0.2745 0.2744 0.2160 -0.0232 -0.0374 0.0378  104 GLU   A OE1 
2192 O  OE2 A GLU   A 104 ? 0.2410 0.3810 0.2016 -0.0731 0.0157  0.1073  104 GLU   A OE2 
2193 O  OE2 B GLU   A 104 ? 0.2760 0.2730 0.2177 -0.0249 -0.0395 0.0392  104 GLU   A OE2 
2206 N  N   A ASP   A 105 ? 0.3078 0.4486 0.2008 -0.0529 0.0297  -0.0077 105 ASP   A N   
2207 N  N   B ASP   A 105 ? 0.2772 0.2716 0.2099 0.0022  -0.0154 0.0163  105 ASP   A N   
2208 C  CA  A ASP   A 105 ? 0.3063 0.4516 0.2278 -0.0469 0.0367  -0.0373 105 ASP   A CA  
2209 C  CA  B ASP   A 105 ? 0.2819 0.2856 0.2422 0.0081  -0.0086 -0.0078 105 ASP   A CA  
2210 C  C   A ASP   A 105 ? 0.2715 0.4335 0.1877 -0.0589 0.0245  -0.0589 105 ASP   A C   
2211 C  C   B ASP   A 105 ? 0.2828 0.2907 0.2418 0.0018  -0.0061 -0.0148 105 ASP   A C   
2212 O  O   A ASP   A 105 ? 0.2508 0.4279 0.1412 -0.0657 0.0196  -0.0839 105 ASP   A O   
2213 O  O   B ASP   A 105 ? 0.2782 0.2930 0.2306 0.0025  -0.0050 -0.0179 105 ASP   A O   
2214 C  CB  A ASP   A 105 ? 0.3365 0.4706 0.2976 -0.0313 0.0478  -0.0445 105 ASP   A CB  
2215 C  CB  B ASP   A 105 ? 0.2847 0.2937 0.2762 0.0190  -0.0059 -0.0237 105 ASP   A CB  
2216 C  CG  A ASP   A 105 ? 0.3597 0.4852 0.3610 -0.0181 0.0514  -0.0514 105 ASP   A CG  
2217 C  CG  B ASP   A 105 ? 0.2879 0.2989 0.3072 0.0293  -0.0041 -0.0363 105 ASP   A CG  
2218 O  OD1 A ASP   A 105 ? 0.3660 0.4911 0.3751 -0.0173 0.0508  -0.0606 105 ASP   A OD1 
2219 O  OD1 B ASP   A 105 ? 0.2889 0.2984 0.3068 0.0287  -0.0074 -0.0437 105 ASP   A OD1 
2220 O  OD2 A ASP   A 105 ? 0.3720 0.4908 0.3980 -0.0131 0.0542  -0.0464 105 ASP   A OD2 
2221 O  OD2 B ASP   A 105 ? 0.2897 0.3017 0.3286 0.0349  -0.0046 -0.0352 105 ASP   A OD2 
2230 N  N   A ILE   A 106 ? 0.2554 0.4186 0.2062 -0.0644 0.0040  -0.0604 106 ILE   A N   
2231 N  N   B ILE   A 106 ? 0.2857 0.2923 0.2526 -0.0025 -0.0088 -0.0151 106 ILE   A N   
2232 C  CA  A ILE   A 106 ? 0.2322 0.3996 0.2299 -0.0761 -0.0155 -0.0711 106 ILE   A CA  
2233 C  CA  B ILE   A 106 ? 0.2879 0.2955 0.2674 -0.0113 -0.0108 -0.0171 106 ILE   A CA  
2234 C  C   A ILE   A 106 ? 0.2189 0.3730 0.2459 -0.0925 -0.0162 -0.0871 106 ILE   A C   
2235 C  C   B ILE   A 106 ? 0.2867 0.2882 0.2656 -0.0143 -0.0040 -0.0159 106 ILE   A C   
2236 O  O   A ILE   A 106 ? 0.1979 0.3613 0.2516 -0.0972 0.0047  -0.0878 106 ILE   A O   
2237 O  O   B ILE   A 106 ? 0.2825 0.2866 0.2650 -0.0144 -0.0010 -0.0174 106 ILE   A O   
2238 C  CB  A ILE   A 106 ? 0.2335 0.4110 0.2760 -0.0619 -0.0275 -0.0428 106 ILE   A CB  
2239 C  CB  B ILE   A 106 ? 0.2937 0.3082 0.2932 -0.0164 -0.0184 -0.0118 106 ILE   A CB  
2240 C  CG1 A ILE   A 106 ? 0.2178 0.4118 0.2993 -0.0478 -0.0267 -0.0189 106 ILE   A CG1 
2241 C  CG1 B ILE   A 106 ? 0.2950 0.3153 0.3111 -0.0170 -0.0205 -0.0045 106 ILE   A CG1 
2242 C  CG2 A ILE   A 106 ? 0.2436 0.4165 0.2900 -0.0609 -0.0371 -0.0420 106 ILE   A CG2 
2243 C  CG2 B ILE   A 106 ? 0.2962 0.3114 0.2973 -0.0182 -0.0216 -0.0128 106 ILE   A CG2 
2244 C  CD1 A ILE   A 106 ? 0.2083 0.4081 0.3126 -0.0374 -0.0114 -0.0063 106 ILE   A CD1 
2245 C  CD1 B ILE   A 106 ? 0.2970 0.3170 0.3220 -0.0151 -0.0192 -0.0016 106 ILE   A CD1 
2268 N  N   A GLN   A 107 ? 0.2383 0.3575 0.2763 -0.0921 -0.0031 -0.0967 107 GLN   A N   
2269 N  N   B GLN   A 107 ? 0.2892 0.2799 0.2718 -0.0154 0.0038  -0.0115 107 GLN   A N   
2270 C  CA  A GLN   A 107 ? 0.2674 0.3379 0.3426 -0.0787 0.0130  -0.0958 107 GLN   A CA  
2271 C  CA  B GLN   A 107 ? 0.2930 0.2753 0.2948 -0.0174 0.0109  -0.0107 107 GLN   A CA  
2272 C  C   A GLN   A 107 ? 0.2380 0.2833 0.3179 -0.0667 0.0353  -0.0791 107 GLN   A C   
2273 C  C   B GLN   A 107 ? 0.2664 0.2435 0.2606 -0.0131 0.0211  -0.0011 107 GLN   A C   
2274 O  O   A GLN   A 107 ? 0.2485 0.2797 0.3751 -0.0598 0.0490  -0.0764 107 GLN   A O   
2275 O  O   B GLN   A 107 ? 0.2674 0.2389 0.2590 -0.0122 0.0248  -0.0058 107 GLN   A O   
2276 C  CB  A GLN   A 107 ? 0.3172 0.3715 0.4350 -0.0826 0.0051  -0.0967 107 GLN   A CB  
2277 C  CB  B GLN   A 107 ? 0.3209 0.3034 0.3546 -0.0252 0.0045  -0.0131 107 GLN   A CB  
2278 C  CG  A GLN   A 107 ? 0.3664 0.4112 0.5366 -0.0805 -0.0017 -0.0848 107 GLN   A CG  
2279 C  CG  B GLN   A 107 ? 0.3451 0.3272 0.4172 -0.0314 -0.0021 -0.0097 107 GLN   A CG  
2280 C  CD  A GLN   A 107 ? 0.4056 0.4356 0.6226 -0.0777 -0.0040 -0.0715 107 GLN   A CD  
2281 C  CD  B GLN   A 107 ? 0.3659 0.3486 0.4713 -0.0345 -0.0058 -0.0048 107 GLN   A CD  
2282 O  OE1 A GLN   A 107 ? 0.4208 0.4445 0.6568 -0.0768 -0.0040 -0.0669 107 GLN   A OE1 
2283 O  OE1 B GLN   A 107 ? 0.3732 0.3572 0.4883 -0.0360 -0.0058 -0.0015 107 GLN   A OE1 
2284 N  NE2 A GLN   A 107 ? 0.4184 0.4412 0.6515 -0.0780 -0.0065 -0.0701 107 GLN   A NE2 
2285 N  NE2 B GLN   A 107 ? 0.3722 0.3554 0.4888 -0.0353 -0.0100 -0.0038 107 GLN   A NE2 
2302 N  N   A LEU   A 108 ? 0.1996 0.2307 0.2524 -0.0624 0.0363  -0.0728 108 LEU   A N   
2303 N  N   B LEU   A 108 ? 0.2388 0.2185 0.2348 -0.0133 0.0247  0.0044  108 LEU   A N   
2304 C  CA  A LEU   A 108 ? 0.1821 0.1927 0.2171 -0.0288 0.0383  -0.0320 108 LEU   A CA  
2305 C  CA  B LEU   A 108 ? 0.2121 0.1954 0.2147 -0.0079 0.0260  0.0082  108 LEU   A CA  
2306 C  C   A LEU   A 108 ? 0.1658 0.1518 0.2101 -0.0163 0.0296  -0.0009 108 LEU   A C   
2307 C  C   B LEU   A 108 ? 0.1844 0.1673 0.2072 -0.0046 0.0247  0.0132  108 LEU   A C   
2308 O  O   A LEU   A 108 ? 0.1605 0.1503 0.2242 -0.0082 0.0327  0.0042  108 LEU   A O   
2309 O  O   B LEU   A 108 ? 0.1846 0.1682 0.2107 -0.0022 0.0297  0.0150  108 LEU   A O   
2310 C  CB  A LEU   A 108 ? 0.1869 0.2022 0.2030 -0.0295 0.0492  -0.0262 108 LEU   A CB  
2311 C  CB  B LEU   A 108 ? 0.2145 0.2047 0.2081 -0.0118 0.0271  0.0031  108 LEU   A CB  
2312 C  CG  A LEU   A 108 ? 0.2032 0.2254 0.2250 -0.0236 0.0568  -0.0309 108 LEU   A CG  
2313 C  CG  B LEU   A 108 ? 0.2200 0.2169 0.2175 -0.0134 0.0280  -0.0053 108 LEU   A CG  
2314 C  CD1 A LEU   A 108 ? 0.2195 0.2293 0.2320 -0.0335 0.0619  -0.0262 108 LEU   A CD1 
2315 C  CD1 B LEU   A 108 ? 0.2258 0.2191 0.2212 -0.0183 0.0326  -0.0068 108 LEU   A CD1 
2316 C  CD2 A LEU   A 108 ? 0.2061 0.2467 0.2695 -0.0121 0.0524  -0.0232 108 LEU   A CD2 
2317 C  CD2 B LEU   A 108 ? 0.2206 0.2270 0.2345 -0.0107 0.0254  -0.0041 108 LEU   A CD2 
2340 N  N   . LEU   A 109 ? 0.1585 0.1502 0.2091 -0.0015 0.0232  0.0144  109 LEU   A N   
2341 C  CA  . LEU   A 109 ? 0.1518 0.1418 0.1915 -0.0034 0.0121  0.0166  109 LEU   A CA  
2342 C  C   . LEU   A 109 ? 0.1384 0.1359 0.1773 -0.0125 0.0120  0.0077  109 LEU   A C   
2343 O  O   . LEU   A 109 ? 0.1472 0.1303 0.1961 -0.0067 0.0041  0.0048  109 LEU   A O   
2344 C  CB  . LEU   A 109 ? 0.1524 0.1461 0.2152 0.0091  0.0108  0.0316  109 LEU   A CB  
2345 C  CG  . LEU   A 109 ? 0.1451 0.1586 0.2275 0.0033  0.0113  0.0362  109 LEU   A CG  
2346 C  CD1 . LEU   A 109 ? 0.1560 0.1502 0.2407 -0.0044 0.0164  0.0213  109 LEU   A CD1 
2347 C  CD2 . LEU   A 109 ? 0.1450 0.1803 0.2505 -0.0014 0.0122  0.0389  109 LEU   A CD2 
2360 N  N   . LYS   A 110 ? 0.1431 0.1340 0.1791 -0.0079 0.0091  0.0076  110 LYS   A N   
2361 C  CA  . LYS   A 110 ? 0.1414 0.1283 0.1881 -0.0109 0.0051  0.0163  110 LYS   A CA  
2362 C  C   . LYS   A 110 ? 0.1410 0.1243 0.1719 -0.0097 0.0031  0.0000  110 LYS   A C   
2363 O  O   . LYS   A 110 ? 0.1328 0.1263 0.1890 -0.0089 0.0086  -0.0023 110 LYS   A O   
2364 C  CB  . LYS   A 110 ? 0.1463 0.1329 0.2124 -0.0102 -0.0024 -0.0018 110 LYS   A CB  
2365 C  CG  . LYS   A 110 ? 0.1486 0.1323 0.2195 -0.0048 -0.0050 -0.0043 110 LYS   A CG  
2366 C  CD  . LYS   A 110 ? 0.1531 0.1395 0.2377 -0.0115 -0.0083 -0.0090 110 LYS   A CD  
2367 C  CE  . LYS   A 110 ? 0.1607 0.1462 0.2613 -0.0125 0.0146  -0.0127 110 LYS   A CE  
2368 N  NZ  . LYS   A 110 ? 0.1590 0.1464 0.2740 -0.0218 0.0259  -0.0095 110 LYS   A NZ  
2382 N  N   . SER   A 111 ? 0.1369 0.1311 0.1712 -0.0034 0.0063  0.0010  111 SER   A N   
2383 C  CA  . SER   A 111 ? 0.1292 0.1360 0.1832 -0.0022 0.0101  0.0015  111 SER   A CA  
2384 C  C   . SER   A 111 ? 0.1276 0.1310 0.1749 -0.0113 0.0078  0.0078  111 SER   A C   
2385 O  O   . SER   A 111 ? 0.1400 0.1223 0.1931 -0.0066 0.0167  0.0105  111 SER   A O   
2386 C  CB  . SER   A 111 ? 0.1450 0.1555 0.1971 -0.0040 0.0221  -0.0096 111 SER   A CB  
2387 O  OG  . SER   A 111 ? 0.1965 0.1750 0.2070 -0.0036 0.0283  -0.0187 111 SER   A OG  
2393 N  N   . ALA   A 112 ? 0.1336 0.1249 0.1846 -0.0064 0.0163  0.0081  112 ALA   A N   
2394 C  CA  . ALA   A 112 ? 0.1375 0.1219 0.1754 -0.0105 0.0198  0.0002  112 ALA   A CA  
2395 C  C   . ALA   A 112 ? 0.1299 0.1130 0.1912 -0.0079 0.0115  0.0036  112 ALA   A C   
2396 O  O   . ALA   A 112 ? 0.1325 0.1180 0.2015 -0.0148 0.0183  0.0069  112 ALA   A O   
2397 C  CB  . ALA   A 112 ? 0.1446 0.1304 0.1763 -0.0079 0.0165  0.0070  112 ALA   A CB  
2403 N  N   . TYR   A 113 ? 0.1217 0.1257 0.1949 -0.0065 0.0161  0.0125  113 TYR   A N   
2404 C  CA  . TYR   A 113 ? 0.1204 0.1206 0.1820 -0.0063 0.0175  0.0150  113 TYR   A CA  
2405 C  C   . TYR   A 113 ? 0.1185 0.1215 0.1653 -0.0122 0.0169  0.0096  113 TYR   A C   
2406 O  O   . TYR   A 113 ? 0.1251 0.1261 0.1836 -0.0054 0.0247  0.0103  113 TYR   A O   
2407 C  CB  . TYR   A 113 ? 0.1247 0.1295 0.1912 -0.0055 0.0031  0.0228  113 TYR   A CB  
2408 C  CG  . TYR   A 113 ? 0.1272 0.1321 0.1759 -0.0117 0.0152  0.0244  113 TYR   A CG  
2409 C  CD1 . TYR   A 113 ? 0.1283 0.1369 0.1767 -0.0042 0.0121  0.0287  113 TYR   A CD1 
2410 C  CD2 . TYR   A 113 ? 0.1313 0.1345 0.1739 -0.0112 0.0107  0.0187  113 TYR   A CD2 
2411 C  CE1 . TYR   A 113 ? 0.1315 0.1443 0.1823 -0.0084 0.0137  0.0302  113 TYR   A CE1 
2412 C  CE2 . TYR   A 113 ? 0.1307 0.1461 0.1814 -0.0084 0.0066  0.0200  113 TYR   A CE2 
2413 C  CZ  . TYR   A 113 ? 0.1286 0.1460 0.1772 0.0036  0.0140  0.0273  113 TYR   A CZ  
2414 O  OH  . TYR   A 113 ? 0.1269 0.1519 0.1888 0.0102  0.0133  0.0265  113 TYR   A OH  
2424 N  N   . GLU   A 114 ? 0.1225 0.1211 0.1778 -0.0084 0.0141  0.0148  114 GLU   A N   
2425 C  CA  . GLU   A 114 ? 0.1314 0.1194 0.1914 -0.0044 0.0068  0.0181  114 GLU   A CA  
2426 C  C   . GLU   A 114 ? 0.1230 0.1250 0.1913 -0.0025 0.0181  0.0185  114 GLU   A C   
2427 O  O   . GLU   A 114 ? 0.1353 0.1236 0.1891 -0.0054 0.0100  0.0112  114 GLU   A O   
2428 C  CB  . GLU   A 114 ? 0.1316 0.1192 0.1877 -0.0072 0.0084  0.0155  114 GLU   A CB  
2429 C  CG  . GLU   A 114 ? 0.1349 0.1238 0.1995 0.0018  0.0113  0.0068  114 GLU   A CG  
2430 C  CD  . GLU   A 114 ? 0.1445 0.1229 0.2067 -0.0027 0.0021  0.0072  114 GLU   A CD  
2431 O  OE1 . GLU   A 114 ? 0.1446 0.1254 0.2145 -0.0125 0.0159  -0.0043 114 GLU   A OE1 
2432 O  OE2 . GLU   A 114 ? 0.1608 0.1303 0.2291 -0.0126 0.0127  -0.0138 114 GLU   A OE2 
2439 N  N   . ASN   A 115 ? 0.1235 0.1266 0.1774 -0.0079 0.0149  0.0101  115 ASN   A N   
2440 C  CA  . ASN   A 115 ? 0.1234 0.1296 0.1842 -0.0072 0.0166  0.0151  115 ASN   A CA  
2441 C  C   . ASN   A 115 ? 0.1283 0.1252 0.1795 -0.0127 0.0061  0.0082  115 ASN   A C   
2442 O  O   . ASN   A 115 ? 0.1334 0.1331 0.1787 -0.0084 0.0134  0.0207  115 ASN   A O   
2443 C  CB  . ASN   A 115 ? 0.1357 0.1384 0.1848 -0.0134 0.0138  0.0158  115 ASN   A CB  
2444 C  CG  . ASN   A 115 ? 0.1350 0.1541 0.1900 -0.0182 0.0252  0.0146  115 ASN   A CG  
2445 O  OD1 . ASN   A 115 ? 0.1397 0.2542 0.2218 -0.0164 0.0310  0.0269  115 ASN   A OD1 
2446 N  ND2 . ASN   A 115 ? 0.1364 0.1359 0.1816 -0.0140 0.0270  0.0174  115 ASN   A ND2 
2453 N  N   . PHE   A 116 ? 0.1253 0.1259 0.1844 0.0002  0.0170  0.0232  116 PHE   A N   
2454 C  CA  . PHE   A 116 ? 0.1269 0.1340 0.1671 -0.0007 0.0166  0.0214  116 PHE   A CA  
2455 C  C   . PHE   A 116 ? 0.1247 0.1445 0.1716 -0.0099 0.0131  0.0253  116 PHE   A C   
2456 O  O   . PHE   A 116 ? 0.1304 0.1475 0.1809 0.0005  0.0152  0.0327  116 PHE   A O   
2457 C  CB  . PHE   A 116 ? 0.1252 0.1255 0.1849 -0.0035 0.0226  0.0222  116 PHE   A CB  
2458 C  CG  . PHE   A 116 ? 0.1317 0.1293 0.1776 -0.0070 0.0167  0.0152  116 PHE   A CG  
2459 C  CD1 . PHE   A 116 ? 0.1342 0.1259 0.1722 -0.0097 0.0170  0.0149  116 PHE   A CD1 
2460 C  CD2 . PHE   A 116 ? 0.1360 0.1343 0.1839 -0.0087 0.0233  0.0141  116 PHE   A CD2 
2461 C  CE1 . PHE   A 116 ? 0.1348 0.1244 0.1889 -0.0169 0.0147  0.0075  116 PHE   A CE1 
2462 C  CE2 . PHE   A 116 ? 0.1377 0.1312 0.1939 -0.0077 0.0192  0.0069  116 PHE   A CE2 
2463 C  CZ  . PHE   A 116 ? 0.1379 0.1142 0.1735 -0.0061 0.0113  0.0133  116 PHE   A CZ  
2473 N  N   . ASN   A 117 ? 0.1249 0.1306 0.1976 -0.0068 0.0131  0.0244  117 ASN   A N   
2474 C  CA  . ASN   A 117 ? 0.1278 0.1295 0.2037 -0.0041 0.0161  0.0271  117 ASN   A CA  
2475 C  C   . ASN   A 117 ? 0.1280 0.1415 0.2068 -0.0046 0.0183  0.0252  117 ASN   A C   
2476 O  O   . ASN   A 117 ? 0.1386 0.1470 0.2335 -0.0089 -0.0036 0.0421  117 ASN   A O   
2477 C  CB  . ASN   A 117 ? 0.1249 0.1339 0.1980 -0.0015 0.0130  0.0309  117 ASN   A CB  
2478 C  CG  . ASN   A 117 ? 0.1266 0.1367 0.1986 -0.0067 0.0180  0.0284  117 ASN   A CG  
2479 O  OD1 . ASN   A 117 ? 0.1291 0.1559 0.2113 -0.0160 0.0149  0.0210  117 ASN   A OD1 
2480 N  ND2 . ASN   A 117 ? 0.1258 0.1328 0.1999 -0.0037 0.0100  0.0263  117 ASN   A ND2 
2487 N  N   . GLN   A 118 ? 0.1270 0.1406 0.2103 -0.0069 0.0023  0.0342  118 GLN   A N   
2488 C  CA  . GLN   A 118 ? 0.1346 0.1527 0.2155 -0.0064 -0.0001 0.0275  118 GLN   A CA  
2489 C  C   . GLN   A 118 ? 0.1381 0.1586 0.1990 -0.0077 -0.0002 0.0355  118 GLN   A C   
2490 O  O   . GLN   A 118 ? 0.1358 0.1894 0.2275 -0.0046 -0.0091 0.0154  118 GLN   A O   
2491 C  CB  . GLN   A 118 ? 0.1341 0.1503 0.2312 -0.0045 0.0121  0.0244  118 GLN   A CB  
2492 C  CG  . GLN   A 118 ? 0.1276 0.1509 0.2241 -0.0039 0.0090  0.0304  118 GLN   A CG  
2493 C  CD  . GLN   A 118 ? 0.1272 0.1583 0.2376 -0.0016 0.0116  0.0258  118 GLN   A CD  
2494 O  OE1 . GLN   A 118 ? 0.1321 0.1685 0.2527 0.0110  0.0038  0.0137  118 GLN   A OE1 
2495 N  NE2 . GLN   A 118 ? 0.1364 0.1550 0.2428 0.0043  0.0088  0.0269  118 GLN   A NE2 
2504 N  N   . HIS   A 119 ? 0.1442 0.1516 0.1908 -0.0020 0.0076  0.0353  119 HIS   A N   
2505 C  CA  . HIS   A 119 ? 0.1509 0.1609 0.1916 -0.0008 0.0054  0.0425  119 HIS   A CA  
2506 C  C   . HIS   A 119 ? 0.1573 0.1685 0.1915 -0.0053 0.0126  0.0405  119 HIS   A C   
2507 O  O   . HIS   A 119 ? 0.1580 0.1790 0.2047 -0.0236 0.0040  0.0441  119 HIS   A O   
2508 C  CB  . HIS   A 119 ? 0.1549 0.1557 0.2179 -0.0057 0.0219  0.0417  119 HIS   A CB  
2509 C  CG  . HIS   A 119 ? 0.1556 0.1584 0.2568 0.0022  0.0099  0.0510  119 HIS   A CG  
2510 N  ND1 . HIS   A 119 ? 0.1676 0.1809 0.3147 -0.0133 0.0082  0.0349  119 HIS   A ND1 
2511 C  CD2 . HIS   A 119 ? 0.1654 0.1675 0.2737 0.0122  0.0280  0.0681  119 HIS   A CD2 
2512 C  CE1 . HIS   A 119 ? 0.1637 0.1787 0.3204 -0.0151 0.0249  0.0585  119 HIS   A CE1 
2513 N  NE2 . HIS   A 119 ? 0.1752 0.1746 0.3106 -0.0009 0.0388  0.0723  119 HIS   A NE2 
2521 N  N   . GLU   A 120 ? 0.1679 0.1928 0.1968 -0.0072 0.0011  0.0710  120 GLU   A N   
2522 C  CA  . GLU   A 120 ? 0.1927 0.2292 0.2235 0.0007  0.0027  0.1080  120 GLU   A CA  
2523 C  C   . GLU   A 120 ? 0.1670 0.2133 0.1975 -0.0088 0.0008  0.0930  120 GLU   A C   
2524 O  O   . GLU   A 120 ? 0.1640 0.2069 0.2043 -0.0136 -0.0007 0.0867  120 GLU   A O   
2525 C  CB  . GLU   A 120 ? 0.2705 0.3041 0.2897 0.0188  0.0086  0.1534  120 GLU   A CB  
2526 C  CG  . GLU   A 120 ? 0.3734 0.3884 0.4085 0.0304  0.0089  0.1515  120 GLU   A CG  
2527 C  CD  . GLU   A 120 ? 0.4559 0.4546 0.5281 0.0379  0.0150  0.1369  120 GLU   A CD  
2528 O  OE1 . GLU   A 120 ? 0.4835 0.4778 0.5532 0.0404  0.0162  0.1318  120 GLU   A OE1 
2529 O  OE2 . GLU   A 120 ? 0.5176 0.5176 0.5854 0.0400  0.0179  0.1295  120 GLU   A OE2 
2536 N  N   . VAL   A 121 ? 0.1622 0.2146 0.1723 -0.0088 0.0059  0.0694  121 VAL   A N   
2537 C  CA  . VAL   A 121 ? 0.1720 0.2182 0.1568 -0.0128 0.0138  0.0720  121 VAL   A CA  
2538 C  C   . VAL   A 121 ? 0.1615 0.1987 0.1413 -0.0232 0.0052  0.0520  121 VAL   A C   
2539 O  O   . VAL   A 121 ? 0.1675 0.2003 0.1728 -0.0305 -0.0069 0.0449  121 VAL   A O   
2540 C  CB  . VAL   A 121 ? 0.2131 0.2558 0.1939 0.0006  0.0262  0.0774  121 VAL   A CB  
2541 C  CG1 . VAL   A 121 ? 0.2150 0.2734 0.2011 0.0044  0.0358  0.0790  121 VAL   A CG1 
2542 C  CG2 . VAL   A 121 ? 0.2381 0.2736 0.2333 -0.0111 0.0256  0.0673  121 VAL   A CG2 
2552 N  N   . LEU   A 122 ? 0.1522 0.1756 0.1538 -0.0230 0.0096  0.0495  122 LEU   A N   
2553 C  CA  . LEU   A 122 ? 0.1551 0.1604 0.1567 -0.0237 0.0224  0.0404  122 LEU   A CA  
2554 C  C   . LEU   A 122 ? 0.1522 0.1607 0.1629 -0.0262 0.0083  0.0356  122 LEU   A C   
2555 O  O   . LEU   A 122 ? 0.1516 0.1687 0.1976 -0.0294 0.0090  0.0416  122 LEU   A O   
2556 C  CB  . LEU   A 122 ? 0.1726 0.1597 0.1893 -0.0071 0.0147  0.0530  122 LEU   A CB  
2557 C  CG  . LEU   A 122 ? 0.1740 0.1671 0.1919 -0.0095 0.0258  0.0383  122 LEU   A CG  
2558 C  CD1 . LEU   A 122 ? 0.1885 0.1671 0.2095 -0.0177 0.0252  0.0445  122 LEU   A CD1 
2559 C  CD2 . LEU   A 122 ? 0.1700 0.1586 0.1862 -0.0070 0.0314  0.0295  122 LEU   A CD2 
2571 N  N   A LEU   A 123 ? 0.1444 0.1564 0.1552 -0.0261 0.0014  0.0311  123 LEU   A N   
2572 N  N   B LEU   A 123 ? 0.1509 0.1557 0.1577 -0.0228 0.0038  0.0257  123 LEU   A N   
2573 C  CA  A LEU   A 123 ? 0.1412 0.1572 0.1421 -0.0293 0.0105  0.0344  123 LEU   A CA  
2574 C  CA  B LEU   A 123 ? 0.1515 0.1534 0.1546 -0.0202 0.0041  0.0183  123 LEU   A CA  
2575 C  C   A LEU   A 123 ? 0.1381 0.1441 0.1313 -0.0177 0.0055  0.0368  123 LEU   A C   
2576 C  C   B LEU   A 123 ? 0.1497 0.1463 0.1399 -0.0106 0.0041  0.0141  123 LEU   A C   
2577 O  O   A LEU   A 123 ? 0.1288 0.1435 0.1417 -0.0219 0.0102  0.0235  123 LEU   A O   
2578 O  O   B LEU   A 123 ? 0.1486 0.1448 0.1311 -0.0059 0.0098  0.0027  123 LEU   A O   
2579 C  CB  A LEU   A 123 ? 0.1558 0.1722 0.1324 -0.0270 0.0277  0.0316  123 LEU   A CB  
2580 C  CB  B LEU   A 123 ? 0.1573 0.1575 0.1612 -0.0216 0.0031  0.0168  123 LEU   A CB  
2581 C  CG  A LEU   A 123 ? 0.1620 0.1867 0.1470 -0.0186 0.0197  0.0194  123 LEU   A CG  
2582 C  CG  B LEU   A 123 ? 0.1574 0.1603 0.1544 -0.0237 0.0037  0.0192  123 LEU   A CG  
2583 C  CD1 A LEU   A 123 ? 0.1679 0.1906 0.1640 -0.0033 0.0156  0.0105  123 LEU   A CD1 
2584 C  CD1 B LEU   A 123 ? 0.1600 0.1596 0.1586 -0.0208 0.0060  0.0172  123 LEU   A CD1 
2585 C  CD2 A LEU   A 123 ? 0.1740 0.1915 0.1586 -0.0173 0.0149  0.0126  123 LEU   A CD2 
2586 C  CD2 B LEU   A 123 ? 0.1617 0.1616 0.1556 -0.0238 0.0011  0.0178  123 LEU   A CD2 
2609 N  N   A ALA   A 124 ? 0.1340 0.1313 0.1288 -0.0114 0.0090  0.0341  124 ALA   A N   
2610 N  N   B ALA   A 124 ? 0.1462 0.1392 0.1358 -0.0100 0.0013  0.0118  124 ALA   A N   
2611 C  CA  A ALA   A 124 ? 0.1281 0.1311 0.1395 -0.0120 0.0036  0.0358  124 ALA   A CA  
2612 C  CA  B ALA   A 124 ? 0.1450 0.1414 0.1303 -0.0152 -0.0114 0.0157  124 ALA   A CA  
2613 C  C   A ALA   A 124 ? 0.1204 0.1377 0.1496 -0.0127 0.0111  0.0351  124 ALA   A C   
2614 C  C   B ALA   A 124 ? 0.1404 0.1434 0.1177 -0.0154 -0.0093 0.0204  124 ALA   A C   
2615 O  O   A ALA   A 124 ? 0.1185 0.1456 0.1767 -0.0188 0.0142  0.0357  124 ALA   A O   
2616 O  O   B ALA   A 124 ? 0.1416 0.1459 0.1227 -0.0090 -0.0100 0.0237  124 ALA   A O   
2617 C  CB  A ALA   A 124 ? 0.1300 0.1272 0.1709 -0.0074 0.0047  0.0218  124 ALA   A CB  
2618 C  CB  B ALA   A 124 ? 0.1514 0.1420 0.1467 -0.0152 -0.0069 0.0124  124 ALA   A CB  
2629 N  N   A PRO   A 125 ? 0.1132 0.1328 0.1585 -0.0109 0.0085  0.0345  125 PRO   A N   
2630 N  N   B PRO   A 125 ? 0.1286 0.1357 0.0992 -0.0118 -0.0098 0.0319  125 PRO   A N   
2631 C  CA  A PRO   A 125 ? 0.1262 0.1354 0.1673 -0.0135 0.0012  0.0247  125 PRO   A CA  
2632 C  CA  B PRO   A 125 ? 0.1314 0.1385 0.1076 -0.0141 -0.0072 0.0244  125 PRO   A CA  
2633 C  C   A PRO   A 125 ? 0.1221 0.1340 0.1624 -0.0062 0.0102  0.0310  125 PRO   A C   
2634 C  C   B PRO   A 125 ? 0.1386 0.1487 0.1182 -0.0103 -0.0034 0.0158  125 PRO   A C   
2635 O  O   A PRO   A 125 ? 0.1268 0.1364 0.1721 0.0005  0.0073  0.0250  125 PRO   A O   
2636 O  O   B PRO   A 125 ? 0.1414 0.1539 0.1251 -0.0096 -0.0070 0.0173  125 PRO   A O   
2637 C  CB  A PRO   A 125 ? 0.1379 0.1392 0.1528 -0.0171 0.0007  0.0169  125 PRO   A CB  
2638 C  CB  B PRO   A 125 ? 0.1249 0.1327 0.1005 -0.0151 -0.0109 0.0292  125 PRO   A CB  
2639 C  CG  A PRO   A 125 ? 0.1453 0.1385 0.1646 -0.0196 0.0026  0.0260  125 PRO   A CG  
2640 C  CG  B PRO   A 125 ? 0.1203 0.1261 0.1043 -0.0118 -0.0055 0.0312  125 PRO   A CG  
2641 C  CD  A PRO   A 125 ? 0.1258 0.1453 0.1634 -0.0135 0.0138  0.0226  125 PRO   A CD  
2642 C  CD  B PRO   A 125 ? 0.1200 0.1235 0.0989 -0.0106 0.0038  0.0297  125 PRO   A CD  
2657 N  N   A LEU   A 126 ? 0.1164 0.1350 0.1644 0.0013  0.0127  0.0181  126 LEU   A N   
2658 N  N   B LEU   A 126 ? 0.1417 0.1489 0.1300 -0.0087 -0.0051 0.0075  126 LEU   A N   
2659 C  CA  A LEU   A 126 ? 0.1242 0.1304 0.1804 0.0020  0.0114  0.0235  126 LEU   A CA  
2660 C  CA  B LEU   A 126 ? 0.1406 0.1409 0.1384 -0.0066 0.0054  -0.0003 126 LEU   A CA  
2661 C  C   A LEU   A 126 ? 0.1364 0.1283 0.1752 0.0007  -0.0023 0.0168  126 LEU   A C   
2662 C  C   B LEU   A 126 ? 0.1459 0.1297 0.1432 0.0028  0.0198  -0.0033 126 LEU   A C   
2663 O  O   A LEU   A 126 ? 0.1461 0.1279 0.1926 0.0074  0.0174  0.0219  126 LEU   A O   
2664 O  O   B LEU   A 126 ? 0.1616 0.1256 0.1725 0.0028  0.0339  0.0068  126 LEU   A O   
2665 C  CB  A LEU   A 126 ? 0.1328 0.1414 0.1920 -0.0048 0.0032  0.0145  126 LEU   A CB  
2666 C  CB  B LEU   A 126 ? 0.1385 0.1519 0.1587 -0.0109 0.0050  -0.0073 126 LEU   A CB  
2667 C  CG  A LEU   A 126 ? 0.1385 0.1611 0.2189 -0.0045 0.0119  0.0137  126 LEU   A CG  
2668 C  CG  B LEU   A 126 ? 0.1351 0.1562 0.1658 -0.0113 0.0107  -0.0186 126 LEU   A CG  
2669 C  CD1 A LEU   A 126 ? 0.1475 0.1803 0.2476 -0.0069 0.0113  0.0205  126 LEU   A CD1 
2670 C  CD1 B LEU   A 126 ? 0.1355 0.1588 0.1789 -0.0128 0.0075  -0.0217 126 LEU   A CD1 
2671 C  CD2 A LEU   A 126 ? 0.1527 0.1498 0.2159 -0.0138 0.0231  0.0217  126 LEU   A CD2 
2672 C  CD2 B LEU   A 126 ? 0.1355 0.1574 0.1678 -0.0114 0.0107  -0.0193 126 LEU   A CD2 
2695 N  N   A LEU   A 127 ? 0.1358 0.1350 0.1492 0.0012  0.0015  0.0187  127 LEU   A N   
2696 N  N   B LEU   A 127 ? 0.1374 0.1325 0.1306 0.0073  0.0191  0.0091  127 LEU   A N   
2697 C  CA  A LEU   A 127 ? 0.1363 0.1398 0.1358 -0.0065 0.0001  0.0090  127 LEU   A CA  
2698 C  CA  B LEU   A 127 ? 0.1328 0.1409 0.1298 0.0051  0.0167  0.0140  127 LEU   A CA  
2699 C  C   A LEU   A 127 ? 0.1323 0.1334 0.1344 -0.0025 -0.0007 0.0102  127 LEU   A C   
2700 C  C   B LEU   A 127 ? 0.1336 0.1417 0.1300 0.0013  0.0130  0.0040  127 LEU   A C   
2701 O  O   A LEU   A 127 ? 0.1333 0.1286 0.1475 -0.0135 -0.0049 0.0138  127 LEU   A O   
2702 O  O   B LEU   A 127 ? 0.1379 0.1432 0.1413 -0.0028 0.0214  0.0002  127 LEU   A O   
2703 C  CB  A LEU   A 127 ? 0.1400 0.1462 0.1528 0.0052  0.0032  0.0112  127 LEU   A CB  
2704 C  CB  B LEU   A 127 ? 0.1285 0.1504 0.1341 0.0044  0.0126  0.0166  127 LEU   A CB  
2705 C  CG  A LEU   A 127 ? 0.1475 0.1493 0.1639 0.0110  0.0054  0.0193  127 LEU   A CG  
2706 C  CG  B LEU   A 127 ? 0.1257 0.1591 0.1361 0.0076  0.0007  0.0233  127 LEU   A CG  
2707 C  CD1 A LEU   A 127 ? 0.1545 0.1415 0.1863 0.0070  0.0007  0.0114  127 LEU   A CD1 
2708 C  CD1 B LEU   A 127 ? 0.1273 0.1646 0.1495 0.0102  0.0073  0.0288  127 LEU   A CD1 
2709 C  CD2 A LEU   A 127 ? 0.1579 0.1508 0.1928 0.0178  -0.0080 0.0166  127 LEU   A CD2 
2710 C  CD2 B LEU   A 127 ? 0.1304 0.1642 0.1312 0.0097  -0.0124 0.0181  127 LEU   A CD2 
2733 N  N   A SER   A 128 ? 0.1418 0.1349 0.1364 -0.0113 -0.0011 0.0157  128 SER   A N   
2734 N  N   B SER   A 128 ? 0.1326 0.1420 0.1344 -0.0051 0.0021  0.0095  128 SER   A N   
2735 C  CA  A SER   A 128 ? 0.1530 0.1368 0.1389 -0.0091 0.0050  0.0170  128 SER   A CA  
2736 C  CA  B SER   A 128 ? 0.1329 0.1403 0.1364 -0.0099 -0.0122 0.0159  128 SER   A CA  
2737 C  C   A SER   A 128 ? 0.1602 0.1383 0.1422 -0.0006 -0.0012 0.0178  128 SER   A C   
2738 C  C   B SER   A 128 ? 0.1332 0.1336 0.1422 -0.0107 -0.0314 0.0249  128 SER   A C   
2739 O  O   A SER   A 128 ? 0.1773 0.1620 0.1577 0.0021  0.0049  0.0072  128 SER   A O   
2740 O  O   B SER   A 128 ? 0.1325 0.1357 0.1489 -0.0135 -0.0334 0.0298  128 SER   A O   
2741 C  CB  A SER   A 128 ? 0.1530 0.1519 0.1418 -0.0082 0.0013  0.0212  128 SER   A CB  
2742 C  CB  B SER   A 128 ? 0.1296 0.1478 0.1287 -0.0164 -0.0150 0.0149  128 SER   A CB  
2743 O  OG  A SER   A 128 ? 0.1557 0.1649 0.1552 -0.0048 0.0109  0.0166  128 SER   A OG  
2744 O  OG  B SER   A 128 ? 0.1233 0.1540 0.1389 -0.0194 -0.0020 0.0145  128 SER   A OG  
2755 N  N   A ALA   A 129 ? 0.1520 0.1453 0.1751 -0.0034 -0.0039 0.0329  129 ALA   A N   
2756 N  N   B ALA   A 129 ? 0.1348 0.1361 0.1600 -0.0098 -0.0334 0.0315  129 ALA   A N   
2757 C  CA  A ALA   A 129 ? 0.1445 0.1544 0.1790 0.0014  -0.0032 0.0393  129 ALA   A CA  
2758 C  CA  B ALA   A 129 ? 0.1401 0.1425 0.1701 -0.0052 -0.0246 0.0296  129 ALA   A CA  
2759 C  C   A ALA   A 129 ? 0.1483 0.1520 0.1700 0.0010  -0.0071 0.0212  129 ALA   A C   
2760 C  C   B ALA   A 129 ? 0.1488 0.1434 0.1700 -0.0074 -0.0168 0.0183  129 ALA   A C   
2761 O  O   A ALA   A 129 ? 0.1570 0.1590 0.1742 -0.0062 -0.0018 0.0252  129 ALA   A O   
2762 O  O   B ALA   A 129 ? 0.1504 0.1440 0.1604 -0.0112 -0.0121 0.0203  129 ALA   A O   
2763 C  CB  A ALA   A 129 ? 0.1468 0.1774 0.1932 0.0090  0.0051  0.0584  129 ALA   A CB  
2764 C  CB  B ALA   A 129 ? 0.1423 0.1549 0.1728 0.0012  -0.0233 0.0330  129 ALA   A CB  
2775 N  N   A GLY   A 130 ? 0.1506 0.1474 0.1761 -0.0008 -0.0035 0.0118  130 GLY   A N   
2776 N  N   B GLY   A 130 ? 0.1585 0.1474 0.1728 -0.0078 -0.0159 0.0191  130 GLY   A N   
2777 C  CA  A GLY   A 130 ? 0.1732 0.1500 0.1853 -0.0002 0.0031  0.0089  130 GLY   A CA  
2778 C  CA  B GLY   A 130 ? 0.1718 0.1525 0.1870 -0.0059 -0.0246 0.0163  130 GLY   A CA  
2779 C  C   A GLY   A 130 ? 0.1720 0.1468 0.1633 -0.0003 -0.0026 0.0111  130 GLY   A C   
2780 C  C   B GLY   A 130 ? 0.1748 0.1543 0.1826 -0.0059 -0.0393 0.0168  130 GLY   A C   
2781 O  O   A GLY   A 130 ? 0.1713 0.1384 0.1515 -0.0080 -0.0069 0.0137  130 GLY   A O   
2782 O  O   B GLY   A 130 ? 0.1815 0.1561 0.1914 -0.0045 -0.0409 0.0232  130 GLY   A O   
2789 N  N   A ILE   A 131 ? 0.1859 0.1453 0.1706 -0.0070 -0.0048 0.0075  131 ILE   A N   
2790 N  N   B ILE   A 131 ? 0.1740 0.1483 0.1746 -0.0068 -0.0408 0.0219  131 ILE   A N   
2791 C  CA  A ILE   A 131 ? 0.1927 0.1486 0.1551 -0.0154 -0.0189 0.0134  131 ILE   A CA  
2792 C  CA  B ILE   A 131 ? 0.1737 0.1453 0.1671 -0.0017 -0.0487 0.0251  131 ILE   A CA  
2793 C  C   A ILE   A 131 ? 0.1835 0.1503 0.1440 -0.0211 -0.0111 0.0235  131 ILE   A C   
2794 C  C   B ILE   A 131 ? 0.1718 0.1490 0.1642 -0.0011 -0.0450 0.0270  131 ILE   A C   
2795 O  O   A ILE   A 131 ? 0.1975 0.1556 0.1610 -0.0137 -0.0111 0.0262  131 ILE   A O   
2796 O  O   B ILE   A 131 ? 0.1793 0.1535 0.1746 0.0034  -0.0472 0.0256  131 ILE   A O   
2797 C  CB  A ILE   A 131 ? 0.2062 0.1593 0.1699 -0.0225 -0.0261 0.0000  131 ILE   A CB  
2798 C  CB  B ILE   A 131 ? 0.1732 0.1483 0.1785 0.0024  -0.0523 0.0150  131 ILE   A CB  
2799 C  CG1 A ILE   A 131 ? 0.2101 0.1828 0.1844 -0.0306 -0.0323 -0.0022 131 ILE   A CG1 
2800 C  CG1 B ILE   A 131 ? 0.1750 0.1587 0.1887 0.0102  -0.0514 0.0117  131 ILE   A CG1 
2801 C  CG2 A ILE   A 131 ? 0.2179 0.1476 0.1893 -0.0145 -0.0248 -0.0095 131 ILE   A CG2 
2802 C  CG2 B ILE   A 131 ? 0.1699 0.1469 0.1827 -0.0013 -0.0537 0.0022  131 ILE   A CG2 
2803 C  CD1 A ILE   A 131 ? 0.2155 0.1901 0.2081 -0.0267 -0.0381 -0.0047 131 ILE   A CD1 
2804 C  CD1 B ILE   A 131 ? 0.1804 0.1650 0.1933 0.0092  -0.0510 0.0054  131 ILE   A CD1 
2827 N  N   A PHE   A 132 ? 0.1755 0.1463 0.1520 -0.0141 -0.0027 0.0214  132 PHE   A N   
2828 N  N   B PHE   A 132 ? 0.1680 0.1495 0.1686 0.0004  -0.0368 0.0252  132 PHE   A N   
2829 C  CA  A PHE   A 132 ? 0.1764 0.1523 0.1402 -0.0189 0.0023  0.0132  132 PHE   A CA  
2830 C  CA  B PHE   A 132 ? 0.1712 0.1539 0.1736 -0.0073 -0.0273 0.0195  132 PHE   A CA  
2831 C  C   A PHE   A 132 ? 0.1757 0.1634 0.1454 -0.0221 -0.0051 0.0124  132 PHE   A C   
2832 C  C   B PHE   A 132 ? 0.1765 0.1670 0.1799 -0.0100 -0.0253 0.0237  132 PHE   A C   
2833 O  O   A PHE   A 132 ? 0.1784 0.1704 0.1565 -0.0280 -0.0086 0.0186  132 PHE   A O   
2834 O  O   B PHE   A 132 ? 0.1823 0.1801 0.1801 -0.0220 -0.0162 0.0342  132 PHE   A O   
2835 C  CB  A PHE   A 132 ? 0.1719 0.1466 0.1368 -0.0147 -0.0103 0.0171  132 PHE   A CB  
2836 C  CB  B PHE   A 132 ? 0.1645 0.1454 0.1567 -0.0125 -0.0212 0.0184  132 PHE   A CB  
2837 C  CG  A PHE   A 132 ? 0.1727 0.1493 0.1451 -0.0043 -0.0145 0.0157  132 PHE   A CG  
2838 C  CG  B PHE   A 132 ? 0.1637 0.1428 0.1512 -0.0112 -0.0168 0.0039  132 PHE   A CG  
2839 C  CD1 A PHE   A 132 ? 0.1711 0.1650 0.1759 0.0076  -0.0230 0.0021  132 PHE   A CD1 
2840 C  CD1 B PHE   A 132 ? 0.1627 0.1509 0.1628 -0.0037 -0.0109 -0.0079 132 PHE   A CD1 
2841 C  CD2 A PHE   A 132 ? 0.1714 0.1572 0.1494 -0.0063 -0.0059 0.0139  132 PHE   A CD2 
2842 C  CD2 B PHE   A 132 ? 0.1638 0.1423 0.1511 -0.0085 -0.0161 -0.0066 132 PHE   A CD2 
2843 C  CE1 A PHE   A 132 ? 0.1725 0.1695 0.1829 0.0009  -0.0308 -0.0070 132 PHE   A CE1 
2844 C  CE1 B PHE   A 132 ? 0.1626 0.1533 0.1627 -0.0046 -0.0116 -0.0147 132 PHE   A CE1 
2845 C  CE2 A PHE   A 132 ? 0.1667 0.1628 0.1645 0.0007  -0.0165 0.0166  132 PHE   A CE2 
2846 C  CE2 B PHE   A 132 ? 0.1595 0.1500 0.1624 -0.0033 -0.0148 -0.0102 132 PHE   A CE2 
2847 C  CZ  A PHE   A 132 ? 0.1638 0.1650 0.1774 -0.0034 -0.0319 0.0115  132 PHE   A CZ  
2848 C  CZ  B PHE   A 132 ? 0.1588 0.1524 0.1643 -0.0056 -0.0143 -0.0114 132 PHE   A CZ  
2867 N  N   A GLY   A 133 ? 0.1763 0.1668 0.1461 -0.0168 -0.0231 0.0165  133 GLY   A N   
2868 N  N   B GLY   A 133 ? 0.1778 0.1671 0.1758 -0.0076 -0.0267 0.0201  133 GLY   A N   
2869 C  CA  A GLY   A 133 ? 0.1833 0.1795 0.1507 -0.0153 -0.0291 0.0055  133 GLY   A CA  
2870 C  CA  B GLY   A 133 ? 0.1773 0.1702 0.1775 -0.0038 -0.0249 0.0109  133 GLY   A CA  
2871 C  C   A GLY   A 133 ? 0.1899 0.1862 0.1582 -0.0200 -0.0439 -0.0008 133 GLY   A C   
2872 C  C   B GLY   A 133 ? 0.1781 0.1754 0.1789 -0.0002 -0.0241 -0.0023 133 GLY   A C   
2873 O  O   A GLY   A 133 ? 0.2017 0.1966 0.1658 -0.0172 -0.0405 -0.0221 133 GLY   A O   
2874 O  O   B GLY   A 133 ? 0.1797 0.1843 0.1771 0.0031  -0.0196 -0.0184 133 GLY   A O   
2881 N  N   A ALA   A 134 ? 0.1903 0.1763 0.1637 -0.0252 -0.0339 0.0016  134 ALA   A N   
2882 N  N   B ALA   A 134 ? 0.1792 0.1695 0.1837 0.0015  -0.0192 -0.0033 134 ALA   A N   
2883 C  CA  A ALA   A 134 ? 0.1925 0.1797 0.1897 -0.0207 -0.0317 0.0002  134 ALA   A CA  
2884 C  CA  B ALA   A 134 ? 0.1800 0.1670 0.1883 0.0009  -0.0159 -0.0031 134 ALA   A CA  
2885 C  C   A ALA   A 134 ? 0.1925 0.1841 0.1879 -0.0212 -0.0262 0.0066  134 ALA   A C   
2886 C  C   B ALA   A 134 ? 0.1819 0.1648 0.1814 -0.0053 -0.0160 0.0018  134 ALA   A C   
2887 O  O   A ALA   A 134 ? 0.2000 0.1918 0.2076 -0.0292 -0.0112 0.0052  134 ALA   A O   
2888 O  O   B ALA   A 134 ? 0.1826 0.1649 0.1950 -0.0126 -0.0045 -0.0024 134 ALA   A O   
2889 C  CB  A ALA   A 134 ? 0.1977 0.1756 0.2149 -0.0165 -0.0304 -0.0033 134 ALA   A CB  
2890 C  CB  B ALA   A 134 ? 0.1808 0.1637 0.1997 0.0043  -0.0124 -0.0045 134 ALA   A CB  
2901 N  N   A ASP   A 135 ? 0.1946 0.1778 0.2057 -0.0203 -0.0308 0.0094  135 ASP   A N   
2902 N  N   B ASP   A 135 ? 0.1888 0.1671 0.1846 -0.0115 -0.0274 0.0105  135 ASP   A N   
2903 C  CA  A ASP   A 135 ? 0.1917 0.1861 0.2392 -0.0268 -0.0364 0.0179  135 ASP   A CA  
2904 C  CA  B ASP   A 135 ? 0.1877 0.1697 0.1972 -0.0158 -0.0323 0.0073  135 ASP   A CA  
2905 C  C   A ASP   A 135 ? 0.1738 0.1723 0.2477 -0.0222 -0.0223 0.0380  135 ASP   A C   
2906 C  C   B ASP   A 135 ? 0.1799 0.1671 0.1939 -0.0136 -0.0315 0.0033  135 ASP   A C   
2907 O  O   A ASP   A 135 ? 0.1657 0.1699 0.2605 -0.0144 -0.0160 0.0457  135 ASP   A O   
2908 O  O   B ASP   A 135 ? 0.1775 0.1648 0.1950 -0.0129 -0.0321 0.0084  135 ASP   A O   
2909 C  CB  A ASP   A 135 ? 0.2156 0.2115 0.2745 -0.0422 -0.0511 0.0058  135 ASP   A CB  
2910 C  CB  B ASP   A 135 ? 0.1946 0.1781 0.2097 -0.0210 -0.0346 0.0030  135 ASP   A CB  
2911 C  CG  A ASP   A 135 ? 0.2333 0.2341 0.3056 -0.0595 -0.0559 0.0019  135 ASP   A CG  
2912 C  CG  B ASP   A 135 ? 0.1984 0.1895 0.2264 -0.0213 -0.0305 0.0017  135 ASP   A CG  
2913 O  OD1 A ASP   A 135 ? 0.2277 0.2429 0.3029 -0.0703 -0.0650 0.0199  135 ASP   A OD1 
2914 O  OD1 B ASP   A 135 ? 0.1948 0.1860 0.2306 -0.0197 -0.0316 0.0023  135 ASP   A OD1 
2915 O  OD2 A ASP   A 135 ? 0.2644 0.2548 0.3488 -0.0592 -0.0333 -0.0074 135 ASP   A OD2 
2916 O  OD2 B ASP   A 135 ? 0.2018 0.2004 0.2440 -0.0211 -0.0318 -0.0008 135 ASP   A OD2 
2925 N  N   A PRO   A 136 ? 0.1573 0.1629 0.2508 -0.0120 -0.0147 0.0511  136 PRO   A N   
2926 N  N   B PRO   A 136 ? 0.1739 0.1644 0.1945 -0.0118 -0.0253 -0.0057 136 PRO   A N   
2927 C  CA  A PRO   A 136 ? 0.1514 0.1627 0.2572 -0.0154 -0.0039 0.0331  136 PRO   A CA  
2928 C  CA  B PRO   A 136 ? 0.1704 0.1698 0.1928 -0.0129 -0.0161 -0.0123 136 PRO   A CA  
2929 C  C   A PRO   A 136 ? 0.1288 0.1568 0.2474 -0.0043 -0.0001 0.0240  136 PRO   A C   
2930 C  C   B PRO   A 136 ? 0.1577 0.1719 0.1771 -0.0082 -0.0130 -0.0097 136 PRO   A C   
2931 O  O   A PRO   A 136 ? 0.1290 0.1606 0.2426 -0.0081 0.0048  0.0278  136 PRO   A O   
2932 O  O   B PRO   A 136 ? 0.1564 0.1671 0.1562 -0.0000 -0.0028 -0.0133 136 PRO   A O   
2933 C  CB  A PRO   A 136 ? 0.1634 0.1594 0.2744 -0.0200 -0.0110 0.0275  136 PRO   A CB  
2934 C  CB  B PRO   A 136 ? 0.1798 0.1701 0.2086 -0.0134 -0.0190 -0.0149 136 PRO   A CB  
2935 C  CG  A PRO   A 136 ? 0.1718 0.1645 0.2833 -0.0154 -0.0174 0.0351  136 PRO   A CG  
2936 C  CG  B PRO   A 136 ? 0.1866 0.1681 0.2173 -0.0122 -0.0242 -0.0130 136 PRO   A CG  
2937 C  CD  A PRO   A 136 ? 0.1698 0.1649 0.2680 -0.0109 -0.0137 0.0531  136 PRO   A CD  
2938 C  CD  B PRO   A 136 ? 0.1766 0.1637 0.2046 -0.0120 -0.0248 -0.0092 136 PRO   A CD  
2953 N  N   A ILE   A 137 ? 0.1288 0.1550 0.2599 -0.0036 -0.0119 0.0301  137 ILE   A N   
2954 N  N   B ILE   A 137 ? 0.1545 0.1728 0.1920 -0.0085 -0.0186 -0.0040 137 ILE   A N   
2955 C  CA  A ILE   A 137 ? 0.1374 0.1556 0.2630 -0.0170 -0.0157 0.0312  137 ILE   A CA  
2956 C  CA  B ILE   A 137 ? 0.1570 0.1784 0.1994 -0.0092 -0.0141 0.0000  137 ILE   A CA  
2957 C  C   A ILE   A 137 ? 0.1389 0.1593 0.2416 -0.0178 -0.0200 0.0293  137 ILE   A C   
2958 C  C   B ILE   A 137 ? 0.1525 0.1832 0.1933 -0.0131 -0.0023 0.0027  137 ILE   A C   
2959 O  O   A ILE   A 137 ? 0.1496 0.1572 0.2422 -0.0165 -0.0147 0.0236  137 ILE   A O   
2960 O  O   B ILE   A 137 ? 0.1483 0.1872 0.1912 -0.0184 0.0028  0.0057  137 ILE   A O   
2961 C  CB  A ILE   A 137 ? 0.1489 0.1688 0.2861 -0.0186 -0.0291 0.0319  137 ILE   A CB  
2962 C  CB  B ILE   A 137 ? 0.1645 0.1759 0.2156 -0.0053 -0.0278 0.0037  137 ILE   A CB  
2963 C  CG1 A ILE   A 137 ? 0.1633 0.1920 0.3181 -0.0140 -0.0250 0.0343  137 ILE   A CG1 
2964 C  CG1 B ILE   A 137 ? 0.1738 0.1772 0.2327 -0.0015 -0.0385 0.0088  137 ILE   A CG1 
2965 C  CG2 A ILE   A 137 ? 0.1607 0.1689 0.2916 -0.0232 -0.0280 0.0195  137 ILE   A CG2 
2966 C  CG2 B ILE   A 137 ? 0.1692 0.1731 0.2212 -0.0018 -0.0295 0.0045  137 ILE   A CG2 
2967 C  CD1 A ILE   A 137 ? 0.1799 0.2068 0.3344 -0.0092 -0.0180 0.0316  137 ILE   A CD1 
2968 C  CD1 B ILE   A 137 ? 0.1791 0.1749 0.2423 -0.0007 -0.0434 0.0155  137 ILE   A CD1 
2991 N  N   A HIS   A 138 ? 0.1359 0.1796 0.2326 -0.0146 -0.0095 0.0300  138 HIS   A N   
2992 N  N   B HIS   A 138 ? 0.1476 0.1866 0.1932 -0.0122 0.0087  -0.0007 138 HIS   A N   
2993 C  CA  A HIS   A 138 ? 0.1417 0.1941 0.2176 -0.0160 -0.0044 0.0268  138 HIS   A CA  
2994 C  CA  B HIS   A 138 ? 0.1468 0.1841 0.1909 -0.0122 0.0100  0.0074  138 HIS   A CA  
2995 C  C   A HIS   A 138 ? 0.1363 0.1855 0.2099 -0.0123 -0.0024 0.0274  138 HIS   A C   
2996 C  C   B HIS   A 138 ? 0.1416 0.1785 0.1960 -0.0113 0.0090  0.0205  138 HIS   A C   
2997 O  O   A HIS   A 138 ? 0.1451 0.1880 0.2062 -0.0140 0.0005  0.0210  138 HIS   A O   
2998 O  O   B HIS   A 138 ? 0.1482 0.1811 0.1981 -0.0128 0.0123  0.0186  138 HIS   A O   
2999 C  CB  A HIS   A 138 ? 0.1644 0.2167 0.2123 -0.0167 -0.0157 0.0184  138 HIS   A CB  
3000 C  CB  B HIS   A 138 ? 0.1479 0.1891 0.1843 -0.0069 0.0125  -0.0058 138 HIS   A CB  
3001 C  CG  A HIS   A 138 ? 0.1880 0.2276 0.2209 -0.0204 -0.0140 0.0159  138 HIS   A CG  
3002 C  CG  B HIS   A 138 ? 0.1562 0.1916 0.1901 -0.0063 0.0110  -0.0130 138 HIS   A CG  
3003 N  ND1 A HIS   A 138 ? 0.2040 0.2382 0.2376 -0.0242 -0.0071 0.0051  138 HIS   A ND1 
3004 N  ND1 B HIS   A 138 ? 0.1640 0.1954 0.2028 -0.0052 0.0105  -0.0209 138 HIS   A ND1 
3005 C  CD2 A HIS   A 138 ? 0.1959 0.2353 0.2249 -0.0119 -0.0138 0.0155  138 HIS   A CD2 
3006 C  CD2 B HIS   A 138 ? 0.1589 0.1913 0.1909 -0.0012 0.0153  -0.0157 138 HIS   A CD2 
3007 C  CE1 A HIS   A 138 ? 0.2100 0.2440 0.2442 -0.0147 -0.0112 0.0059  138 HIS   A CE1 
3008 C  CE1 B HIS   A 138 ? 0.1648 0.1927 0.2034 -0.0008 0.0114  -0.0205 138 HIS   A CE1 
3009 N  NE2 A HIS   A 138 ? 0.2036 0.2426 0.2254 -0.0103 -0.0088 0.0074  138 HIS   A NE2 
3010 N  NE2 B HIS   A 138 ? 0.1624 0.1916 0.1960 0.0011  0.0151  -0.0227 138 HIS   A NE2 
3025 N  N   . SER   A 139 ? 0.1326 0.1708 0.2076 -0.0090 -0.0048 0.0332  139 SER   A N   
3026 C  CA  . SER   A 139 ? 0.1311 0.1634 0.1987 -0.0099 0.0030  0.0395  139 SER   A CA  
3027 C  C   . SER   A 139 ? 0.1323 0.1559 0.1927 -0.0099 0.0069  0.0244  139 SER   A C   
3028 O  O   . SER   A 139 ? 0.1274 0.1545 0.2055 -0.0130 0.0040  0.0281  139 SER   A O   
3029 C  CB  . SER   A 139 ? 0.1301 0.1675 0.1926 -0.0162 -0.0053 0.0300  139 SER   A CB  
3030 O  OG  . SER   A 139 ? 0.1403 0.1643 0.2033 -0.0213 -0.0102 0.0438  139 SER   A OG  
3037 N  N   . LEU   A 140 ? 0.1258 0.1618 0.1970 -0.0088 0.0126  0.0391  140 LEU   A N   
3038 C  CA  . LEU   A 140 ? 0.1245 0.1547 0.1935 -0.0112 0.0051  0.0350  140 LEU   A CA  
3039 C  C   . LEU   A 140 ? 0.1200 0.1648 0.1958 -0.0178 0.0053  0.0343  140 LEU   A C   
3040 O  O   . LEU   A 140 ? 0.1295 0.1662 0.2144 -0.0108 -0.0005 0.0367  140 LEU   A O   
3041 C  CB  . LEU   A 140 ? 0.1331 0.1647 0.2051 -0.0091 0.0060  0.0346  140 LEU   A CB  
3042 C  CG  . LEU   A 140 ? 0.1331 0.1811 0.2164 -0.0209 0.0106  0.0431  140 LEU   A CG  
3043 C  CD1 . LEU   A 140 ? 0.1406 0.1883 0.2211 -0.0123 0.0088  0.0473  140 LEU   A CD1 
3044 C  CD2 . LEU   A 140 ? 0.1402 0.1968 0.2231 -0.0151 0.0150  0.0468  140 LEU   A CD2 
3056 N  N   . ARG   A 141 ? 0.1283 0.1678 0.2075 -0.0092 -0.0020 0.0313  141 ARG   A N   
3057 C  CA  . ARG   A 141 ? 0.1406 0.1777 0.2240 -0.0218 -0.0059 0.0144  141 ARG   A CA  
3058 C  C   . ARG   A 141 ? 0.1405 0.1586 0.2100 -0.0219 -0.0013 0.0128  141 ARG   A C   
3059 O  O   . ARG   A 141 ? 0.1393 0.1565 0.2365 -0.0202 0.0056  0.0107  141 ARG   A O   
3060 C  CB  . ARG   A 141 ? 0.1509 0.2093 0.2525 -0.0289 -0.0029 -0.0092 141 ARG   A CB  
3061 C  CG  . ARG   A 141 ? 0.1910 0.2484 0.2927 -0.0331 0.0151  -0.0167 141 ARG   A CG  
3062 C  CD  . ARG   A 141 ? 0.2306 0.2768 0.3290 -0.0410 0.0177  -0.0222 141 ARG   A CD  
3063 N  NE  . ARG   A 141 ? 0.2189 0.3015 0.3461 -0.0474 0.0071  -0.0188 141 ARG   A NE  
3064 C  CZ  . ARG   A 141 ? 0.2215 0.3228 0.3521 -0.0636 0.0176  -0.0097 141 ARG   A CZ  
3065 N  NH1 . ARG   A 141 ? 0.2060 0.3253 0.3357 -0.0815 0.0415  -0.0284 141 ARG   A NH1 
3066 N  NH2 . ARG   A 141 ? 0.2239 0.3361 0.3731 -0.0608 0.0028  0.0027  141 ARG   A NH2 
3080 N  N   . VAL   A 142 ? 0.1374 0.1578 0.1935 -0.0143 0.0004  0.0044  142 VAL   A N   
3081 C  CA  . VAL   A 142 ? 0.1381 0.1547 0.1977 -0.0111 0.0183  -0.0001 142 VAL   A CA  
3082 C  C   . VAL   A 142 ? 0.1251 0.1490 0.1939 -0.0186 0.0041  0.0064  142 VAL   A C   
3083 O  O   . VAL   A 142 ? 0.1305 0.1530 0.2150 -0.0038 0.0089  0.0184  142 VAL   A O   
3084 C  CB  . VAL   A 142 ? 0.1517 0.1616 0.1963 -0.0146 0.0205  0.0090  142 VAL   A CB  
3085 C  CG1 . VAL   A 142 ? 0.1497 0.1529 0.1953 -0.0184 0.0263  0.0032  142 VAL   A CG1 
3086 C  CG2 . VAL   A 142 ? 0.1601 0.1795 0.2086 -0.0123 0.0195  0.0112  142 VAL   A CG2 
3096 N  N   . CYS   A 143 ? 0.1301 0.1459 0.1829 -0.0156 0.0056  0.0112  143 CYS   A N   
3097 C  CA  . CYS   A 143 ? 0.1287 0.1465 0.1968 -0.0138 0.0112  0.0198  143 CYS   A CA  
3098 C  C   . CYS   A 143 ? 0.1280 0.1487 0.2121 -0.0136 0.0080  0.0299  143 CYS   A C   
3099 O  O   . CYS   A 143 ? 0.1282 0.1466 0.2113 -0.0072 0.0089  0.0329  143 CYS   A O   
3100 C  CB  . CYS   A 143 ? 0.1354 0.1473 0.2080 -0.0094 0.0116  0.0322  143 CYS   A CB  
3101 S  SG  . CYS   A 143 ? 0.1544 0.1584 0.1980 0.0010  0.0145  0.0201  143 CYS   A SG  
3107 N  N   . VAL   A 144 ? 0.1242 0.1514 0.2263 -0.0114 0.0123  0.0330  144 VAL   A N   
3108 C  CA  . VAL   A 144 ? 0.1290 0.1618 0.2558 -0.0173 0.0226  0.0361  144 VAL   A CA  
3109 C  C   . VAL   A 144 ? 0.1354 0.1487 0.2548 -0.0258 -0.0004 0.0297  144 VAL   A C   
3110 O  O   . VAL   A 144 ? 0.1520 0.1528 0.2583 -0.0100 -0.0058 0.0365  144 VAL   A O   
3111 C  CB  . VAL   A 144 ? 0.1555 0.1847 0.3109 -0.0053 0.0457  0.0403  144 VAL   A CB  
3112 C  CG1 . VAL   A 144 ? 0.1768 0.2049 0.3494 -0.0134 0.0254  0.0371  144 VAL   A CG1 
3113 C  CG2 . VAL   A 144 ? 0.1434 0.1905 0.3163 -0.0092 0.0505  0.0521  144 VAL   A CG2 
3123 N  N   . ASP   A 145 ? 0.1433 0.1402 0.2581 -0.0195 0.0066  0.0186  145 ASP   A N   
3124 C  CA  . ASP   A 145 ? 0.1565 0.1441 0.2636 -0.0217 0.0006  0.0138  145 ASP   A CA  
3125 C  C   . ASP   A 145 ? 0.1522 0.1429 0.2580 -0.0175 0.0046  0.0014  145 ASP   A C   
3126 O  O   . ASP   A 145 ? 0.1631 0.1555 0.3166 -0.0200 0.0007  -0.0289 145 ASP   A O   
3127 C  CB  . ASP   A 145 ? 0.1638 0.1757 0.2853 -0.0257 -0.0149 0.0104  145 ASP   A CB  
3128 C  CG  . ASP   A 145 ? 0.1788 0.2140 0.3187 -0.0459 -0.0263 0.0209  145 ASP   A CG  
3129 O  OD1 . ASP   A 145 ? 0.1724 0.2339 0.3291 -0.0544 -0.0188 0.0241  145 ASP   A OD1 
3130 O  OD2 . ASP   A 145 ? 0.2027 0.2385 0.3293 -0.0526 -0.0504 0.0213  145 ASP   A OD2 
3135 N  N   . THR   A 146 ? 0.1343 0.1376 0.2167 -0.0141 0.0130  0.0115  146 THR   A N   
3136 C  CA  . THR   A 146 ? 0.1341 0.1378 0.2012 -0.0064 0.0107  0.0080  146 THR   A CA  
3137 C  C   . THR   A 146 ? 0.1293 0.1313 0.2081 0.0030  0.0125  0.0206  146 THR   A C   
3138 O  O   . THR   A 146 ? 0.1423 0.1468 0.2258 0.0044  0.0038  0.0145  146 THR   A O   
3139 C  CB  . THR   A 146 ? 0.1298 0.1417 0.2069 -0.0020 0.0096  0.0176  146 THR   A CB  
3140 O  OG1 . THR   A 146 ? 0.1275 0.1590 0.2172 -0.0025 0.0046  0.0114  146 THR   A OG1 
3141 C  CG2 . THR   A 146 ? 0.1342 0.1442 0.2254 -0.0050 0.0067  0.0190  146 THR   A CG2 
3149 N  N   . VAL   A 147 ? 0.1270 0.1367 0.2047 0.0008  0.0160  0.0163  147 VAL   A N   
3150 C  CA  . VAL   A 147 ? 0.1302 0.1424 0.2133 -0.0089 0.0316  0.0291  147 VAL   A CA  
3151 C  C   . VAL   A 147 ? 0.1332 0.1382 0.2356 -0.0120 0.0237  0.0364  147 VAL   A C   
3152 O  O   . VAL   A 147 ? 0.1356 0.1440 0.2402 -0.0169 0.0173  0.0346  147 VAL   A O   
3153 C  CB  . VAL   A 147 ? 0.1449 0.1445 0.2030 -0.0130 0.0247  0.0301  147 VAL   A CB  
3154 C  CG1 . VAL   A 147 ? 0.1743 0.1531 0.2065 -0.0083 0.0247  0.0354  147 VAL   A CG1 
3155 C  CG2 . VAL   A 147 ? 0.1483 0.1452 0.1967 -0.0140 0.0121  0.0196  147 VAL   A CG2 
3165 N  N   . ARG   A 148 ? 0.1340 0.1422 0.2369 -0.0114 0.0234  0.0513  148 ARG   A N   
3166 C  CA  . ARG   A 148 ? 0.1423 0.1455 0.2302 -0.0133 0.0190  0.0560  148 ARG   A CA  
3167 C  C   . ARG   A 148 ? 0.1528 0.1475 0.2266 -0.0160 0.0168  0.0690  148 ARG   A C   
3168 O  O   . ARG   A 148 ? 0.1775 0.1658 0.2562 -0.0207 0.0242  0.0543  148 ARG   A O   
3169 C  CB  . ARG   A 148 ? 0.1489 0.1490 0.2529 -0.0075 0.0279  0.0538  148 ARG   A CB  
3170 C  CG  . ARG   A 148 ? 0.1615 0.1486 0.2848 -0.0103 0.0451  0.0357  148 ARG   A CG  
3171 C  CD  . ARG   A 148 ? 0.1773 0.1451 0.3002 -0.0100 0.0552  0.0519  148 ARG   A CD  
3172 N  NE  . ARG   A 148 ? 0.1711 0.1508 0.2971 0.0087  0.0573  0.0541  148 ARG   A NE  
3173 C  CZ  . ARG   A 148 ? 0.1720 0.1399 0.2794 0.0032  0.0469  0.0458  148 ARG   A CZ  
3174 N  NH1 . ARG   A 148 ? 0.1740 0.1402 0.2917 -0.0081 0.0495  0.0212  148 ARG   A NH1 
3175 N  NH2 . ARG   A 148 ? 0.1633 0.1566 0.2789 0.0155  0.0477  0.0500  148 ARG   A NH2 
3189 N  N   . THR   A 149 ? 0.1505 0.1605 0.2187 -0.0178 0.0040  0.0577  149 THR   A N   
3190 C  CA  . THR   A 149 ? 0.1465 0.1637 0.2146 -0.0148 0.0052  0.0535  149 THR   A CA  
3191 C  C   . THR   A 149 ? 0.1442 0.1595 0.2059 -0.0223 0.0075  0.0543  149 THR   A C   
3192 O  O   . THR   A 149 ? 0.1474 0.1683 0.2271 -0.0220 0.0116  0.0526  149 THR   A O   
3193 C  CB  . THR   A 149 ? 0.1473 0.1751 0.2158 -0.0160 0.0062  0.0452  149 THR   A CB  
3194 O  OG1 . THR   A 149 ? 0.1511 0.1623 0.2296 -0.0263 0.0055  0.0416  149 THR   A OG1 
3195 C  CG2 . THR   A 149 ? 0.1466 0.1851 0.2315 -0.0111 -0.0065 0.0358  149 THR   A CG2 
3203 N  N   . ASN   A 150 ? 0.1467 0.1656 0.2037 -0.0130 -0.0022 0.0656  150 ASN   A N   
3204 C  CA  . ASN   A 150 ? 0.1611 0.1766 0.2049 -0.0164 0.0045  0.0597  150 ASN   A CA  
3205 C  C   . ASN   A 150 ? 0.1443 0.1652 0.2014 -0.0217 0.0028  0.0526  150 ASN   A C   
3206 O  O   . ASN   A 150 ? 0.1531 0.1767 0.2331 -0.0174 -0.0116 0.0517  150 ASN   A O   
3207 C  CB  . ASN   A 150 ? 0.2014 0.2016 0.2332 -0.0224 0.0263  0.0772  150 ASN   A CB  
3208 C  CG  . ASN   A 150 ? 0.2572 0.2344 0.3009 -0.0182 0.0094  0.0803  150 ASN   A CG  
3209 O  OD1 . ASN   A 150 ? 0.2811 0.2456 0.3213 -0.0245 0.0123  0.0942  150 ASN   A OD1 
3210 N  ND2 . ASN   A 150 ? 0.2882 0.2567 0.3332 -0.0103 -0.0036 0.0772  150 ASN   A ND2 
3217 N  N   . VAL   A 151 ? 0.1480 0.1517 0.1995 -0.0221 0.0021  0.0453  151 VAL   A N   
3218 C  CA  . VAL   A 151 ? 0.1522 0.1533 0.1901 -0.0209 0.0070  0.0404  151 VAL   A CA  
3219 C  C   . VAL   A 151 ? 0.1423 0.1488 0.2025 -0.0293 0.0036  0.0473  151 VAL   A C   
3220 O  O   . VAL   A 151 ? 0.1510 0.1603 0.2373 -0.0207 0.0094  0.0436  151 VAL   A O   
3221 C  CB  . VAL   A 151 ? 0.1799 0.1724 0.1937 -0.0096 0.0112  0.0398  151 VAL   A CB  
3222 C  CG1 . VAL   A 151 ? 0.1774 0.1918 0.2200 -0.0109 0.0058  0.0406  151 VAL   A CG1 
3223 C  CG2 . VAL   A 151 ? 0.1905 0.1693 0.1996 -0.0024 0.0244  0.0310  151 VAL   A CG2 
3233 N  N   . TYR   A 152 ? 0.1388 0.1561 0.1995 -0.0267 0.0061  0.0430  152 TYR   A N   
3234 C  CA  . TYR   A 152 ? 0.1419 0.1625 0.1716 -0.0247 0.0087  0.0445  152 TYR   A CA  
3235 C  C   . TYR   A 152 ? 0.1372 0.1542 0.1721 -0.0212 0.0190  0.0401  152 TYR   A C   
3236 O  O   . TYR   A 152 ? 0.1508 0.1499 0.1888 -0.0253 0.0209  0.0353  152 TYR   A O   
3237 C  CB  . TYR   A 152 ? 0.1601 0.1712 0.1830 -0.0208 0.0251  0.0452  152 TYR   A CB  
3238 C  CG  . TYR   A 152 ? 0.1698 0.1957 0.1842 -0.0230 0.0283  0.0541  152 TYR   A CG  
3239 C  CD1 . TYR   A 152 ? 0.1800 0.2191 0.2000 -0.0120 0.0301  0.0647  152 TYR   A CD1 
3240 C  CD2 . TYR   A 152 ? 0.1786 0.2133 0.1778 -0.0328 0.0215  0.0524  152 TYR   A CD2 
3241 C  CE1 . TYR   A 152 ? 0.2143 0.2339 0.2186 -0.0100 0.0162  0.0749  152 TYR   A CE1 
3242 C  CE2 . TYR   A 152 ? 0.2065 0.2296 0.1906 -0.0344 0.0248  0.0590  152 TYR   A CE2 
3243 C  CZ  . TYR   A 152 ? 0.2300 0.2344 0.2031 -0.0222 0.0168  0.0869  152 TYR   A CZ  
3244 O  OH  . TYR   A 152 ? 0.2610 0.2535 0.2474 -0.0128 0.0185  0.0992  152 TYR   A OH  
3254 N  N   A LEU   A 153 ? 0.1344 0.1484 0.1840 -0.0205 0.0221  0.0481  153 LEU   A N   
3255 N  N   B LEU   A 153 ? 0.1421 0.1602 0.1578 -0.0192 0.0099  0.0371  153 LEU   A N   
3256 C  CA  A LEU   A 153 ? 0.1279 0.1388 0.1939 -0.0150 0.0247  0.0410  153 LEU   A CA  
3257 C  CA  B LEU   A 153 ? 0.1421 0.1608 0.1419 -0.0072 0.0060  0.0259  153 LEU   A CA  
3258 C  C   A LEU   A 153 ? 0.1343 0.1416 0.1975 -0.0112 0.0292  0.0326  153 LEU   A C   
3259 C  C   B LEU   A 153 ? 0.1478 0.1681 0.1376 -0.0016 0.0053  0.0189  153 LEU   A C   
3260 O  O   A LEU   A 153 ? 0.1440 0.1492 0.2184 -0.0174 0.0438  0.0239  153 LEU   A O   
3261 O  O   B LEU   A 153 ? 0.1506 0.1738 0.1512 -0.0046 0.0102  0.0149  153 LEU   A O   
3262 C  CB  A LEU   A 153 ? 0.1281 0.1349 0.2077 -0.0146 0.0207  0.0361  153 LEU   A CB  
3263 C  CB  B LEU   A 153 ? 0.1397 0.1572 0.1466 0.0032  0.0018  0.0267  153 LEU   A CB  
3264 C  CG  A LEU   A 153 ? 0.1315 0.1351 0.1997 -0.0095 0.0204  0.0264  153 LEU   A CG  
3265 C  CG  B LEU   A 153 ? 0.1437 0.1572 0.1528 0.0112  -0.0001 0.0264  153 LEU   A CG  
3266 C  CD1 A LEU   A 153 ? 0.1484 0.1263 0.2001 -0.0042 0.0031  0.0306  153 LEU   A CD1 
3267 C  CD1 B LEU   A 153 ? 0.1479 0.1559 0.1698 0.0195  -0.0009 0.0268  153 LEU   A CD1 
3268 C  CD2 A LEU   A 153 ? 0.1394 0.1458 0.1828 -0.0176 0.0279  0.0013  153 LEU   A CD2 
3269 C  CD2 B LEU   A 153 ? 0.1478 0.1613 0.1557 0.0082  0.0015  0.0178  153 LEU   A CD2 
3292 N  N   A ALA   A 154 ? 0.1315 0.1371 0.1904 -0.0140 0.0312  0.0326  154 ALA   A N   
3293 N  N   B ALA   A 154 ? 0.1504 0.1669 0.1269 0.0022  0.0077  0.0120  154 ALA   A N   
3294 C  CA  A ALA   A 154 ? 0.1410 0.1415 0.1793 -0.0127 0.0270  0.0214  154 ALA   A CA  
3295 C  CA  B ALA   A 154 ? 0.1585 0.1655 0.1415 0.0049  0.0008  0.0042  154 ALA   A CA  
3296 C  C   A ALA   A 154 ? 0.1383 0.1295 0.1694 -0.0058 0.0255  0.0258  154 ALA   A C   
3297 C  C   B ALA   A 154 ? 0.1606 0.1689 0.1375 0.0061  -0.0061 0.0060  154 ALA   A C   
3298 O  O   A ALA   A 154 ? 0.1531 0.1456 0.1688 -0.0125 0.0240  0.0228  154 ALA   A O   
3299 O  O   B ALA   A 154 ? 0.1654 0.1687 0.1174 0.0014  -0.0072 0.0109  154 ALA   A O   
3300 C  CB  A ALA   A 154 ? 0.1484 0.1526 0.1800 -0.0027 0.0220  0.0141  154 ALA   A CB  
3301 C  CB  B ALA   A 154 ? 0.1619 0.1634 0.1511 0.0049  -0.0073 -0.0047 154 ALA   A CB  
3312 N  N   A VAL   A 155 ? 0.1211 0.1021 0.1347 0.0035  0.0299  0.0417  155 VAL   A N   
3313 N  N   B VAL   A 155 ? 0.1644 0.1721 0.1506 0.0097  -0.0137 0.0137  155 VAL   A N   
3314 C  CA  A VAL   A 155 ? 0.1417 0.1235 0.1836 0.0030  0.0181  0.0449  155 VAL   A CA  
3315 C  CA  B VAL   A 155 ? 0.1848 0.1898 0.1778 0.0060  -0.0233 0.0190  155 VAL   A CA  
3316 C  CA  T VAL   A 155 ? 0.1607 0.1695 0.1921 -0.0137 0.0340  0.0557  155 VAL   A CA  
3317 C  C   A VAL   A 155 ? 0.1472 0.1421 0.2108 0.0225  0.0300  0.0566  155 VAL   A C   
3318 C  C   B VAL   A 155 ? 0.2050 0.2055 0.2141 0.0179  -0.0232 0.0266  155 VAL   A C   
3319 C  C   T VAL   A 155 ? 0.1633 0.1732 0.1893 0.0005  0.0411  0.0615  155 VAL   A C   
3320 O  O   A VAL   A 155 ? 0.1404 0.1497 0.2378 0.0265  0.0396  0.0532  155 VAL   A O   
3321 O  O   B VAL   A 155 ? 0.2016 0.2025 0.2242 0.0247  -0.0172 0.0336  155 VAL   A O   
3322 O  O   T VAL   A 155 ? 0.1525 0.1780 0.1895 0.0014  0.0495  0.0610  155 VAL   A O   
3323 C  CB  A VAL   A 155 ? 0.1526 0.1307 0.2012 0.0050  -0.0069 0.0370  155 VAL   A CB  
3324 C  CB  B VAL   A 155 ? 0.1819 0.1894 0.1814 -0.0042 -0.0264 0.0164  155 VAL   A CB  
3325 C  CB  T VAL   A 155 ? 0.1576 0.1721 0.1964 -0.0152 0.0251  0.0472  155 VAL   A CB  
3326 C  CG1 A VAL   A 155 ? 0.1645 0.1496 0.2177 0.0028  -0.0163 0.0338  155 VAL   A CG1 
3327 C  CG1 B VAL   A 155 ? 0.1814 0.1889 0.1900 -0.0137 -0.0369 0.0138  155 VAL   A CG1 
3328 C  CG1 T VAL   A 155 ? 0.1601 0.1809 0.2033 -0.0161 0.0212  0.0470  155 VAL   A CG1 
3329 C  CG2 A VAL   A 155 ? 0.1636 0.1393 0.2173 0.0138  -0.0257 0.0314  155 VAL   A CG2 
3330 C  CG2 B VAL   A 155 ? 0.1769 0.1868 0.1771 -0.0101 -0.0166 0.0161  155 VAL   A CG2 
3331 C  CG2 T VAL   A 155 ? 0.1630 0.1767 0.2053 -0.0082 0.0134  0.0418  155 VAL   A CG2 
3357 N  N   A PHE   A 156 ? 0.1533 0.1552 0.2370 0.0302  0.0355  0.0692  156 PHE   A N   
3358 N  N   B PHE   A 156 ? 0.2267 0.2191 0.2327 0.0228  -0.0236 0.0241  156 PHE   A N   
3359 N  N   T PHE   A 156 ? 0.1777 0.1725 0.1996 0.0082  0.0385  0.0669  156 PHE   A N   
3360 C  CA  A PHE   A 156 ? 0.1694 0.1614 0.2680 0.0391  0.0375  0.0736  156 PHE   A CA  
3361 C  CA  B PHE   A 156 ? 0.2448 0.2337 0.2570 0.0305  -0.0212 0.0232  156 PHE   A CA  
3362 C  CA  T PHE   A 156 ? 0.1994 0.1717 0.1993 0.0128  0.0384  0.0697  156 PHE   A CA  
3363 C  C   A PHE   A 156 ? 0.1686 0.1632 0.2671 0.0481  0.0479  0.0888  156 PHE   A C   
3364 C  C   B PHE   A 156 ? 0.2533 0.2417 0.2696 0.0373  -0.0195 0.0337  156 PHE   A C   
3365 C  C   T PHE   A 156 ? 0.1987 0.1800 0.2083 0.0152  0.0480  0.0766  156 PHE   A C   
3366 O  O   A PHE   A 156 ? 0.1752 0.1680 0.2774 0.0324  0.0627  0.0746  156 PHE   A O   
3367 O  O   B PHE   A 156 ? 0.2601 0.2443 0.2783 0.0363  -0.0190 0.0381  156 PHE   A O   
3368 O  O   T PHE   A 156 ? 0.2085 0.1842 0.2202 0.0143  0.0485  0.0564  156 PHE   A O   
3369 C  CB  A PHE   A 156 ? 0.1892 0.1697 0.2845 0.0323  0.0257  0.0774  156 PHE   A CB  
3370 C  CB  B PHE   A 156 ? 0.2531 0.2417 0.2715 0.0305  -0.0183 0.0145  156 PHE   A CB  
3371 C  CB  T PHE   A 156 ? 0.2115 0.1605 0.1809 0.0165  0.0356  0.0675  156 PHE   A CB  
3372 C  CG  A PHE   A 156 ? 0.2139 0.1762 0.2964 0.0264  0.0153  0.0693  156 PHE   A CG  
3373 C  CG  B PHE   A 156 ? 0.2611 0.2496 0.2822 0.0287  -0.0084 0.0012  156 PHE   A CG  
3374 C  CG  T PHE   A 156 ? 0.2220 0.1586 0.1669 0.0233  0.0336  0.0682  156 PHE   A CG  
3375 C  CD1 A PHE   A 156 ? 0.2239 0.1791 0.2944 0.0289  0.0243  0.0610  156 PHE   A CD1 
3376 C  CD1 B PHE   A 156 ? 0.2647 0.2528 0.2863 0.0271  -0.0015 -0.0057 156 PHE   A CD1 
3377 C  CD1 T PHE   A 156 ? 0.2278 0.1634 0.1808 0.0256  0.0242  0.0606  156 PHE   A CD1 
3378 C  CD2 A PHE   A 156 ? 0.2290 0.1862 0.3012 0.0316  0.0099  0.0697  156 PHE   A CD2 
3379 C  CD2 B PHE   A 156 ? 0.2616 0.2546 0.2826 0.0248  -0.0051 -0.0042 156 PHE   A CD2 
3380 C  CD2 T PHE   A 156 ? 0.2278 0.1561 0.1755 0.0270  0.0311  0.0651  156 PHE   A CD2 
3381 C  CE1 A PHE   A 156 ? 0.2398 0.1867 0.3029 0.0302  0.0277  0.0484  156 PHE   A CE1 
3382 C  CE1 B PHE   A 156 ? 0.2655 0.2544 0.2863 0.0279  0.0035  -0.0053 156 PHE   A CE1 
3383 C  CE1 T PHE   A 156 ? 0.2335 0.1644 0.1984 0.0294  0.0191  0.0465  156 PHE   A CE1 
3384 C  CE2 A PHE   A 156 ? 0.2435 0.1949 0.3086 0.0323  0.0155  0.0529  156 PHE   A CE2 
3385 C  CE2 B PHE   A 156 ? 0.2621 0.2568 0.2777 0.0261  0.0001  -0.0028 156 PHE   A CE2 
3386 C  CE2 T PHE   A 156 ? 0.2348 0.1598 0.1864 0.0260  0.0259  0.0569  156 PHE   A CE2 
3387 C  CZ  A PHE   A 156 ? 0.2461 0.1956 0.3053 0.0313  0.0280  0.0470  156 PHE   A CZ  
3388 C  CZ  B PHE   A 156 ? 0.2643 0.2554 0.2809 0.0296  0.0029  -0.0023 156 PHE   A CZ  
3389 C  CZ  T PHE   A 156 ? 0.2339 0.1575 0.1983 0.0234  0.0207  0.0482  156 PHE   A CZ  
3417 N  N   A ASP   A 157 ? 0.1801 0.1820 0.2735 0.0576  0.0378  0.0957  157 ASP   A N   
3418 N  N   B ASP   A 157 ? 0.2550 0.2484 0.2659 0.0415  -0.0198 0.0366  157 ASP   A N   
3419 N  N   T ASP   A 157 ? 0.1909 0.1960 0.2201 0.0192  0.0467  0.0887  157 ASP   A N   
3420 C  CA  A ASP   A 157 ? 0.2044 0.2131 0.2868 0.0602  0.0278  0.0953  157 ASP   A CA  
3421 C  CA  B ASP   A 157 ? 0.2581 0.2611 0.2711 0.0415  -0.0190 0.0412  157 ASP   A CA  
3422 C  CA  T ASP   A 157 ? 0.1941 0.2165 0.2314 0.0284  0.0412  0.0900  157 ASP   A CA  
3423 C  C   A ASP   A 157 ? 0.1947 0.2349 0.2923 0.0654  0.0350  0.1002  157 ASP   A C   
3424 C  C   B ASP   A 157 ? 0.2501 0.2687 0.2711 0.0472  -0.0159 0.0494  157 ASP   A C   
3425 C  C   T ASP   A 157 ? 0.1974 0.2377 0.2420 0.0342  0.0485  0.0948  157 ASP   A C   
3426 O  O   A ASP   A 157 ? 0.1860 0.2309 0.2885 0.0674  0.0419  0.1052  157 ASP   A O   
3427 O  O   B ASP   A 157 ? 0.2480 0.2684 0.2696 0.0479  -0.0143 0.0485  157 ASP   A O   
3428 O  O   T ASP   A 157 ? 0.1890 0.2366 0.2422 0.0356  0.0567  0.0960  157 ASP   A O   
3429 C  CB  A ASP   A 157 ? 0.2290 0.2209 0.3020 0.0653  0.0162  0.0848  157 ASP   A CB  
3430 C  CB  B ASP   A 157 ? 0.2659 0.2661 0.2800 0.0364  -0.0190 0.0372  157 ASP   A CB  
3431 C  CB  T ASP   A 157 ? 0.1930 0.2149 0.2384 0.0365  0.0271  0.0812  157 ASP   A CB  
3432 C  CG  A ASP   A 157 ? 0.2505 0.2286 0.3252 0.0694  0.0061  0.0800  157 ASP   A CG  
3433 C  CG  B ASP   A 157 ? 0.2722 0.2699 0.2949 0.0313  -0.0195 0.0373  157 ASP   A CG  
3434 C  CG  T ASP   A 157 ? 0.1868 0.2071 0.2427 0.0459  0.0172  0.0790  157 ASP   A CG  
3435 O  OD1 A ASP   A 157 ? 0.2670 0.2321 0.3412 0.0649  -0.0036 0.0732  157 ASP   A OD1 
3436 O  OD1 B ASP   A 157 ? 0.2781 0.2732 0.3043 0.0267  -0.0195 0.0354  157 ASP   A OD1 
3437 O  OD1 T ASP   A 157 ? 0.1821 0.1972 0.2624 0.0487  0.0194  0.0635  157 ASP   A OD1 
3438 O  OD2 A ASP   A 157 ? 0.2474 0.2241 0.3340 0.0684  0.0163  0.0901  157 ASP   A OD2 
3439 O  OD2 B ASP   A 157 ? 0.2717 0.2694 0.3003 0.0294  -0.0178 0.0390  157 ASP   A OD2 
3440 O  OD2 T ASP   A 157 ? 0.1803 0.2053 0.2240 0.0485  0.0108  0.0889  157 ASP   A OD2 
3453 N  N   A LYS   A 158 ? 0.1981 0.2605 0.3044 0.0635  0.0416  0.0899  158 LYS   A N   
3454 N  N   B LYS   A 158 ? 0.2457 0.2764 0.2735 0.0494  -0.0158 0.0543  158 LYS   A N   
3455 N  N   T LYS   A 158 ? 0.2120 0.2602 0.2565 0.0344  0.0492  0.0851  158 LYS   A N   
3456 C  CA  A LYS   A 158 ? 0.1954 0.2835 0.3163 0.0697  0.0495  0.0803  158 LYS   A CA  
3457 C  CA  B LYS   A 158 ? 0.2463 0.2878 0.2770 0.0468  -0.0029 0.0533  158 LYS   A CA  
3458 C  CA  T LYS   A 158 ? 0.2262 0.2811 0.2816 0.0389  0.0446  0.0682  158 LYS   A CA  
3459 C  C   A LYS   A 158 ? 0.1778 0.2980 0.2986 0.0763  0.0305  0.0874  158 LYS   A C   
3460 C  C   B LYS   A 158 ? 0.2289 0.2914 0.2558 0.0471  -0.0101 0.0540  158 LYS   A C   
3461 C  C   T LYS   A 158 ? 0.2258 0.2898 0.2746 0.0428  0.0293  0.0637  158 LYS   A C   
3462 O  O   A LYS   A 158 ? 0.1746 0.3054 0.3000 0.0647  0.0414  0.0799  158 LYS   A O   
3463 O  O   B LYS   A 158 ? 0.2203 0.2940 0.2383 0.0429  -0.0078 0.0537  158 LYS   A O   
3464 O  O   T LYS   A 158 ? 0.2236 0.2934 0.2747 0.0408  0.0294  0.0566  158 LYS   A O   
3465 C  CB  A LYS   A 158 ? 0.2150 0.2916 0.3467 0.0672  0.0725  0.0729  158 LYS   A CB  
3466 C  CB  B LYS   A 158 ? 0.2633 0.2995 0.3047 0.0417  0.0131  0.0510  158 LYS   A CB  
3467 C  CB  T LYS   A 158 ? 0.2447 0.2924 0.3187 0.0371  0.0542  0.0583  158 LYS   A CB  
3468 C  CG  A LYS   A 158 ? 0.2387 0.3010 0.3772 0.0633  0.0841  0.0724  158 LYS   A CG  
3469 C  CG  B LYS   A 158 ? 0.2782 0.3105 0.3350 0.0368  0.0268  0.0534  158 LYS   A CG  
3470 C  CG  T LYS   A 158 ? 0.2629 0.3031 0.3543 0.0353  0.0592  0.0542  158 LYS   A CG  
3471 C  CD  A LYS   A 158 ? 0.2559 0.3095 0.4016 0.0579  0.1009  0.0770  158 LYS   A CD  
3472 C  CD  B LYS   A 158 ? 0.2905 0.3187 0.3620 0.0325  0.0378  0.0592  158 LYS   A CD  
3473 C  CD  T LYS   A 158 ? 0.2778 0.3119 0.3885 0.0361  0.0635  0.0541  158 LYS   A CD  
3474 C  CE  A LYS   A 158 ? 0.2665 0.3142 0.4141 0.0504  0.1143  0.0881  158 LYS   A CE  
3475 C  CE  B LYS   A 158 ? 0.2962 0.3222 0.3808 0.0330  0.0458  0.0666  158 LYS   A CE  
3476 C  CE  T LYS   A 158 ? 0.2886 0.3170 0.4127 0.0361  0.0647  0.0572  158 LYS   A CE  
3477 N  NZ  A LYS   A 158 ? 0.2700 0.3150 0.4186 0.0454  0.1244  0.0933  158 LYS   A NZ  
3478 N  NZ  B LYS   A 158 ? 0.2980 0.3225 0.3921 0.0333  0.0499  0.0695  158 LYS   A NZ  
3479 N  NZ  T LYS   A 158 ? 0.2943 0.3192 0.4251 0.0370  0.0661  0.0577  158 LYS   A NZ  
3519 N  N   A ASN   A 159 ? 0.1726 0.3056 0.3032 0.0800  0.0122  0.0890  159 ASN   A N   
3520 N  N   B ASN   A 159 ? 0.2261 0.2954 0.2617 0.0504  -0.0160 0.0491  159 ASN   A N   
3521 N  N   T ASN   A 159 ? 0.2310 0.2935 0.2842 0.0419  0.0193  0.0598  159 ASN   A N   
3522 C  CA  A ASN   A 159 ? 0.1768 0.3126 0.2965 0.0739  -0.0005 0.0946  159 ASN   A CA  
3523 C  CA  B ASN   A 159 ? 0.2271 0.3005 0.2693 0.0483  -0.0131 0.0431  159 ASN   A CA  
3524 C  CA  T ASN   A 159 ? 0.2406 0.2968 0.2861 0.0357  0.0134  0.0590  159 ASN   A CA  
3525 C  C   A ASN   A 159 ? 0.1568 0.3129 0.2670 0.0614  0.0058  0.0979  159 ASN   A C   
3526 C  C   B ASN   A 159 ? 0.2113 0.3019 0.2523 0.0437  -0.0008 0.0452  159 ASN   A C   
3527 C  C   T ASN   A 159 ? 0.2441 0.2983 0.2738 0.0266  0.0231  0.0527  159 ASN   A C   
3528 O  O   A ASN   A 159 ? 0.1415 0.3173 0.2545 0.0655  -0.0030 0.0888  159 ASN   A O   
3529 O  O   B ASN   A 159 ? 0.1995 0.3096 0.2460 0.0449  0.0020  0.0406  159 ASN   A O   
3530 O  O   T ASN   A 159 ? 0.2448 0.2992 0.2675 0.0260  0.0244  0.0448  159 ASN   A O   
3531 C  CB  A ASN   A 159 ? 0.1939 0.3200 0.3263 0.0736  -0.0113 0.0977  159 ASN   A CB  
3532 C  CB  B ASN   A 159 ? 0.2418 0.3037 0.3030 0.0496  -0.0217 0.0342  159 ASN   A CB  
3533 C  CB  T ASN   A 159 ? 0.2450 0.2996 0.3083 0.0357  0.0025  0.0655  159 ASN   A CB  
3534 C  CG  A ASN   A 159 ? 0.2138 0.3275 0.3665 0.0680  -0.0095 0.0920  159 ASN   A CG  
3535 C  CG  B ASN   A 159 ? 0.2564 0.3059 0.3362 0.0463  -0.0278 0.0227  159 ASN   A CG  
3536 C  CG  T ASN   A 159 ? 0.2510 0.3023 0.3366 0.0345  -0.0021 0.0678  159 ASN   A CG  
3537 O  OD1 A ASN   A 159 ? 0.2172 0.3335 0.3854 0.0648  0.0037  0.0890  159 ASN   A OD1 
3538 O  OD1 B ASN   A 159 ? 0.2627 0.3052 0.3483 0.0449  -0.0332 0.0217  159 ASN   A OD1 
3539 O  OD1 T ASN   A 159 ? 0.2509 0.3059 0.3504 0.0337  0.0072  0.0685  159 ASN   A OD1 
3540 N  ND2 A ASN   A 159 ? 0.2186 0.3304 0.3799 0.0671  -0.0168 0.0876  159 ASN   A ND2 
3541 N  ND2 B ASN   A 159 ? 0.2597 0.3073 0.3511 0.0435  -0.0288 0.0137  159 ASN   A ND2 
3542 N  ND2 T ASN   A 159 ? 0.2518 0.3034 0.3436 0.0344  -0.0109 0.0688  159 ASN   A ND2 
3561 N  N   A LEU   A 160 ? 0.1476 0.2998 0.2581 0.0498  -0.0018 0.1143  160 LEU   A N   
3562 N  N   B LEU   A 160 ? 0.2044 0.2918 0.2425 0.0373  -0.0010 0.0594  160 LEU   A N   
3563 N  N   T LEU   A 160 ? 0.2446 0.2941 0.2750 0.0183  0.0214  0.0552  160 LEU   A N   
3564 C  CA  A LEU   A 160 ? 0.1415 0.2831 0.2473 0.0269  0.0142  0.1244  160 LEU   A CA  
3565 C  CA  B LEU   A 160 ? 0.2000 0.2794 0.2352 0.0283  0.0071  0.0655  160 LEU   A CA  
3566 C  CA  T LEU   A 160 ? 0.2461 0.2869 0.2717 0.0064  0.0248  0.0600  160 LEU   A CA  
3567 C  C   A LEU   A 160 ? 0.1214 0.2792 0.2354 0.0179  0.0239  0.1162  160 LEU   A C   
3568 C  C   B LEU   A 160 ? 0.1855 0.2724 0.2200 0.0171  0.0132  0.0678  160 LEU   A C   
3569 O  O   A LEU   A 160 ? 0.1059 0.2878 0.2439 0.0120  0.0206  0.1095  160 LEU   A O   
3570 O  O   B LEU   A 160 ? 0.1777 0.2782 0.2247 0.0154  0.0113  0.0666  160 LEU   A O   
3571 C  CB  A LEU   A 160 ? 0.1551 0.2742 0.2431 0.0142  0.0151  0.1288  160 LEU   A CB  
3572 C  CB  B LEU   A 160 ? 0.2108 0.2749 0.2450 0.0281  0.0077  0.0620  160 LEU   A CB  
3573 C  CB  T LEU   A 160 ? 0.2465 0.2806 0.2662 -0.0043 0.0276  0.0621  160 LEU   A CB  
3574 C  CG  A LEU   A 160 ? 0.1703 0.2739 0.2609 -0.0053 0.0235  0.1089  160 LEU   A CG  
3575 C  CG  B LEU   A 160 ? 0.2222 0.2729 0.2626 0.0234  0.0108  0.0490  160 LEU   A CG  
3576 C  CG  T LEU   A 160 ? 0.2487 0.2778 0.2675 -0.0163 0.0317  0.0553  160 LEU   A CG  
3577 C  CD1 A LEU   A 160 ? 0.1829 0.2810 0.2723 -0.0090 0.0225  0.0979  160 LEU   A CD1 
3578 C  CD1 B LEU   A 160 ? 0.2264 0.2714 0.2678 0.0166  0.0159  0.0432  160 LEU   A CD1 
3579 C  CD1 T LEU   A 160 ? 0.2529 0.2811 0.2713 -0.0182 0.0311  0.0503  160 LEU   A CD1 
3580 C  CD2 A LEU   A 160 ? 0.1746 0.2680 0.2649 -0.0104 0.0288  0.0990  160 LEU   A CD2 
3581 C  CD2 B LEU   A 160 ? 0.2257 0.2721 0.2679 0.0239  0.0126  0.0447  160 LEU   A CD2 
3582 C  CD2 T LEU   A 160 ? 0.2485 0.2728 0.2643 -0.0206 0.0353  0.0528  160 LEU   A CD2 
3615 N  N   A TYR   A 161 ? 0.1333 0.2657 0.2579 0.0153  0.0299  0.1052  161 TYR   A N   
3616 N  N   B TYR   A 161 ? 0.1853 0.2590 0.2145 0.0105  0.0205  0.0658  161 TYR   A N   
3617 C  CA  A TYR   A 161 ? 0.1436 0.2514 0.2522 0.0114  0.0278  0.0947  161 TYR   A CA  
3618 C  CA  B TYR   A 161 ? 0.1857 0.2493 0.2080 0.0053  0.0248  0.0599  161 TYR   A CA  
3619 C  C   A TYR   A 161 ? 0.1418 0.2664 0.2545 0.0082  0.0230  0.0819  161 TYR   A C   
3620 C  C   B TYR   A 161 ? 0.1839 0.2606 0.2167 -0.0010 0.0246  0.0500  161 TYR   A C   
3621 O  O   A TYR   A 161 ? 0.1379 0.2681 0.2380 0.0009  0.0235  0.0754  161 TYR   A O   
3622 O  O   B TYR   A 161 ? 0.1800 0.2613 0.2084 -0.0029 0.0262  0.0375  161 TYR   A O   
3623 C  CB  A TYR   A 161 ? 0.1509 0.2269 0.2546 0.0070  0.0346  0.0847  161 TYR   A CB  
3624 C  CB  B TYR   A 161 ? 0.1864 0.2309 0.2021 0.0066  0.0269  0.0589  161 TYR   A CB  
3625 C  CG  A TYR   A 161 ? 0.1469 0.2087 0.2570 0.0051  0.0268  0.0618  161 TYR   A CG  
3626 C  CG  B TYR   A 161 ? 0.1828 0.2122 0.1995 0.0074  0.0290  0.0550  161 TYR   A CG  
3627 C  CD1 A TYR   A 161 ? 0.1454 0.2003 0.2633 0.0047  0.0269  0.0458  161 TYR   A CD1 
3628 C  CD1 B TYR   A 161 ? 0.1850 0.2039 0.2035 0.0084  0.0260  0.0476  161 TYR   A CD1 
3629 C  CD2 A TYR   A 161 ? 0.1463 0.2035 0.2565 0.0100  0.0128  0.0529  161 TYR   A CD2 
3630 C  CD2 B TYR   A 161 ? 0.1833 0.2044 0.2044 0.0084  0.0308  0.0572  161 TYR   A CD2 
3631 C  CE1 A TYR   A 161 ? 0.1480 0.1871 0.2614 0.0055  0.0172  0.0486  161 TYR   A CE1 
3632 C  CE1 B TYR   A 161 ? 0.1878 0.2022 0.2096 0.0087  0.0242  0.0457  161 TYR   A CE1 
3633 C  CE2 A TYR   A 161 ? 0.1509 0.1892 0.2591 0.0049  0.0133  0.0538  161 TYR   A CE2 
3634 C  CE2 B TYR   A 161 ? 0.1881 0.2033 0.2151 0.0037  0.0325  0.0556  161 TYR   A CE2 
3635 C  CZ  A TYR   A 161 ? 0.1576 0.1814 0.2549 0.0014  0.0066  0.0549  161 TYR   A CZ  
3636 C  CZ  B TYR   A 161 ? 0.1953 0.2016 0.2210 0.0052  0.0281  0.0509  161 TYR   A CZ  
3637 O  OH  A TYR   A 161 ? 0.1793 0.1711 0.2692 -0.0037 -0.0088 0.0633  161 TYR   A OH  
3638 O  OH  B TYR   A 161 ? 0.2090 0.2032 0.2459 0.0026  0.0232  0.0462  161 TYR   A OH  
3657 N  N   A ASP   A 162 ? 0.1425 0.2836 0.2617 0.0153  0.0362  0.0802  162 ASP   A N   
3658 N  N   B ASP   A 162 ? 0.1844 0.2704 0.2265 -0.0035 0.0298  0.0560  162 ASP   A N   
3659 C  CA  A ASP   A 162 ? 0.1401 0.3124 0.2761 0.0062  0.0446  0.0652  162 ASP   A CA  
3660 C  CA  B ASP   A 162 ? 0.1924 0.2855 0.2529 -0.0043 0.0196  0.0419  162 ASP   A CA  
3661 C  C   A ASP   A 162 ? 0.1293 0.3309 0.2761 -0.0034 0.0391  0.0626  162 ASP   A C   
3662 C  C   B ASP   A 162 ? 0.1895 0.2883 0.2514 -0.0040 0.0116  0.0367  162 ASP   A C   
3663 O  O   A ASP   A 162 ? 0.1337 0.3368 0.2982 -0.0099 0.0310  0.0557  162 ASP   A O   
3664 O  O   B ASP   A 162 ? 0.1888 0.2927 0.2616 -0.0035 0.0101  0.0360  162 ASP   A O   
3665 C  CB  A ASP   A 162 ? 0.1485 0.3220 0.2941 0.0095  0.0602  0.0515  162 ASP   A CB  
3666 C  CB  B ASP   A 162 ? 0.2048 0.2971 0.2845 -0.0052 0.0156  0.0277  162 ASP   A CB  
3667 C  CG  A ASP   A 162 ? 0.1620 0.3355 0.3181 0.0120  0.0612  0.0383  162 ASP   A CG  
3668 C  CG  B ASP   A 162 ? 0.2179 0.3070 0.3116 -0.0048 0.0093  0.0150  162 ASP   A CG  
3669 O  OD1 A ASP   A 162 ? 0.1720 0.3402 0.3270 0.0018  0.0602  0.0426  162 ASP   A OD1 
3670 O  OD1 B ASP   A 162 ? 0.2281 0.3101 0.3292 -0.0026 0.0088  0.0170  162 ASP   A OD1 
3671 O  OD2 A ASP   A 162 ? 0.1760 0.3386 0.3503 0.0238  0.0479  0.0214  162 ASP   A OD2 
3672 O  OD2 B ASP   A 162 ? 0.2184 0.3103 0.3155 -0.0052 0.0040  0.0038  162 ASP   A OD2 
3681 N  N   A LYS   A 163 ? 0.1471 0.3450 0.2800 -0.0001 0.0121  0.0591  163 LYS   A N   
3682 N  N   B LYS   A 163 ? 0.1939 0.2871 0.2478 -0.0023 0.0023  0.0315  163 LYS   A N   
3683 C  CA  A LYS   A 163 ? 0.1549 0.3535 0.2821 -0.0005 -0.0021 0.0511  163 LYS   A CA  
3684 C  CA  B LYS   A 163 ? 0.1959 0.2837 0.2487 0.0001  -0.0002 0.0276  163 LYS   A CA  
3685 C  C   A LYS   A 163 ? 0.1456 0.3486 0.2683 -0.0098 0.0113  0.0623  163 LYS   A C   
3686 C  C   B LYS   A 163 ? 0.1870 0.2763 0.2356 0.0046  0.0041  0.0269  163 LYS   A C   
3687 O  O   A LYS   A 163 ? 0.1393 0.3570 0.2701 -0.0131 0.0019  0.0631  163 LYS   A O   
3688 O  O   B LYS   A 163 ? 0.1847 0.2789 0.2451 0.0079  -0.0044 0.0314  163 LYS   A O   
3689 C  CB  A LYS   A 163 ? 0.1854 0.3660 0.3061 0.0151  -0.0213 0.0380  163 LYS   A CB  
3690 C  CB  B LYS   A 163 ? 0.2119 0.2908 0.2732 0.0011  -0.0099 0.0222  163 LYS   A CB  
3691 C  CG  A LYS   A 163 ? 0.2244 0.3785 0.3504 0.0161  -0.0180 0.0290  163 LYS   A CG  
3692 C  CG  B LYS   A 163 ? 0.2276 0.2980 0.3036 -0.0002 -0.0100 0.0167  163 LYS   A CG  
3693 C  CD  A LYS   A 163 ? 0.2559 0.3885 0.4033 0.0159  -0.0143 0.0233  163 LYS   A CD  
3694 C  CD  B LYS   A 163 ? 0.2411 0.3051 0.3347 -0.0013 -0.0124 0.0113  163 LYS   A CD  
3695 C  CE  A LYS   A 163 ? 0.2810 0.3956 0.4456 0.0148  -0.0065 0.0250  163 LYS   A CE  
3696 C  CE  B LYS   A 163 ? 0.2514 0.3097 0.3610 -0.0009 -0.0139 0.0041  163 LYS   A CE  
3697 N  NZ  A LYS   A 163 ? 0.2952 0.3995 0.4702 0.0121  -0.0039 0.0264  163 LYS   A NZ  
3698 N  NZ  B LYS   A 163 ? 0.2580 0.3118 0.3764 -0.0015 -0.0130 0.0010  163 LYS   A NZ  
3725 N  N   A LEU   A 164 ? 0.1310 0.3239 0.2492 -0.0264 0.0153  0.0624  164 LEU   A N   
3726 N  N   B LEU   A 164 ? 0.1770 0.2694 0.2169 -0.0007 0.0097  0.0217  164 LEU   A N   
3727 C  CA  A LEU   A 164 ? 0.1424 0.2986 0.2317 -0.0412 0.0206  0.0606  164 LEU   A CA  
3728 C  CA  B LEU   A 164 ? 0.1709 0.2619 0.1989 -0.0029 0.0157  0.0138  164 LEU   A CA  
3729 C  C   A LEU   A 164 ? 0.1564 0.2971 0.2237 -0.0446 0.0223  0.0492  164 LEU   A C   
3730 C  C   B LEU   A 164 ? 0.1705 0.2648 0.1990 -0.0098 0.0192  0.0083  164 LEU   A C   
3731 O  O   A LEU   A 164 ? 0.1622 0.3051 0.2130 -0.0492 0.0447  0.0340  164 LEU   A O   
3732 O  O   B LEU   A 164 ? 0.1722 0.2686 0.1956 -0.0154 0.0268  0.0022  164 LEU   A O   
3733 C  CB  A LEU   A 164 ? 0.1452 0.2798 0.2227 -0.0432 0.0240  0.0631  164 LEU   A CB  
3734 C  CB  B LEU   A 164 ? 0.1694 0.2531 0.1831 0.0016  0.0179  0.0080  164 LEU   A CB  
3735 C  CG  A LEU   A 164 ? 0.1542 0.2679 0.2189 -0.0401 0.0184  0.0559  164 LEU   A CG  
3736 C  CG  B LEU   A 164 ? 0.1725 0.2454 0.1804 0.0059  0.0122  0.0053  164 LEU   A CG  
3737 C  CD1 A LEU   A 164 ? 0.1496 0.2613 0.2169 -0.0270 0.0089  0.0595  164 LEU   A CD1 
3738 C  CD1 B LEU   A 164 ? 0.1748 0.2431 0.1808 0.0084  0.0117  0.0013  164 LEU   A CD1 
3739 C  CD2 A LEU   A 164 ? 0.1636 0.2672 0.2092 -0.0404 0.0151  0.0459  164 LEU   A CD2 
3740 C  CD2 B LEU   A 164 ? 0.1690 0.2412 0.1739 0.0042  0.0109  0.0048  164 LEU   A CD2 
3763 N  N   A VAL   A 165 ? 0.1470 0.2854 0.2228 -0.0475 0.0237  0.0551  165 VAL   A N   
3764 N  N   B VAL   A 165 ? 0.1654 0.2634 0.2010 -0.0149 0.0170  0.0072  165 VAL   A N   
3765 C  CA  A VAL   A 165 ? 0.1553 0.2780 0.2043 -0.0484 0.0292  0.0496  165 VAL   A CA  
3766 C  CA  B VAL   A 165 ? 0.1688 0.2648 0.2078 -0.0153 0.0168  0.0050  165 VAL   A CA  
3767 C  C   A VAL   A 165 ? 0.1478 0.2898 0.2055 -0.0409 0.0312  0.0420  165 VAL   A C   
3768 C  C   B VAL   A 165 ? 0.1642 0.2668 0.2040 -0.0150 0.0266  -0.0003 165 VAL   A C   
3769 O  O   A VAL   A 165 ? 0.1458 0.2867 0.2034 -0.0350 0.0408  0.0393  165 VAL   A O   
3770 O  O   B VAL   A 165 ? 0.1672 0.2684 0.1956 -0.0135 0.0271  -0.0046 165 VAL   A O   
3771 C  CB  A VAL   A 165 ? 0.1692 0.2664 0.2069 -0.0526 0.0299  0.0418  165 VAL   A CB  
3772 C  CB  B VAL   A 165 ? 0.1744 0.2650 0.2160 -0.0162 0.0070  0.0015  165 VAL   A CB  
3773 C  CG1 A VAL   A 165 ? 0.1790 0.2658 0.2088 -0.0552 0.0339  0.0308  165 VAL   A CG1 
3774 C  CG1 B VAL   A 165 ? 0.1771 0.2670 0.2234 -0.0179 0.0043  -0.0024 165 VAL   A CG1 
3775 C  CG2 A VAL   A 165 ? 0.1722 0.2659 0.2074 -0.0494 0.0154  0.0480  165 VAL   A CG2 
3776 C  CG2 B VAL   A 165 ? 0.1787 0.2644 0.2213 -0.0156 0.0020  -0.0028 165 VAL   A CG2 
3795 N  N   A SER   A 166 ? 0.1413 0.3051 0.2246 -0.0310 0.0256  0.0295  166 SER   A N   
3796 N  N   B SER   A 166 ? 0.1508 0.2681 0.2123 -0.0167 0.0379  -0.0013 166 SER   A N   
3797 C  CA  A SER   A 166 ? 0.1467 0.3277 0.2405 -0.0256 0.0237  0.0222  166 SER   A CA  
3798 C  CA  B SER   A 166 ? 0.1442 0.2718 0.2150 -0.0188 0.0393  -0.0027 166 SER   A CA  
3799 C  C   A SER   A 166 ? 0.1479 0.3511 0.2427 -0.0232 0.0187  0.0198  166 SER   A C   
3800 C  C   B SER   A 166 ? 0.1586 0.2799 0.2178 -0.0273 0.0389  -0.0008 166 SER   A C   
3801 O  O   A SER   A 166 ? 0.1683 0.3670 0.2674 -0.0360 0.0362  -0.0041 166 SER   A O   
3802 O  O   B SER   A 166 ? 0.1644 0.2869 0.2218 -0.0378 0.0459  -0.0080 166 SER   A O   
3803 C  CB  A SER   A 166 ? 0.1704 0.3334 0.2658 -0.0183 0.0249  0.0196  166 SER   A CB  
3804 C  CB  B SER   A 166 ? 0.1286 0.2689 0.2225 -0.0061 0.0339  -0.0097 166 SER   A CB  
3805 O  OG  A SER   A 166 ? 0.1992 0.3399 0.2945 -0.0172 0.0254  0.0271  166 SER   A OG  
3806 O  OG  B SER   A 166 ? 0.1222 0.2675 0.2350 -0.0001 0.0148  -0.0043 166 SER   A OG  
3817 N  N   A SER   A 167 ? 0.1488 0.3529 0.2033 0.0013  0.0021  0.0371  167 SER   A N   
3818 N  N   B SER   A 167 ? 0.1777 0.2814 0.2408 -0.0214 0.0275  0.0082  167 SER   A N   
3819 C  CA  A SER   A 167 ? 0.1682 0.3550 0.2091 0.0086  -0.0156 0.0279  167 SER   A CA  
3820 C  CA  B SER   A 167 ? 0.1933 0.2801 0.2598 -0.0194 0.0252  0.0176  167 SER   A CA  
3821 C  C   A SER   A 167 ? 0.1696 0.3439 0.2103 0.0181  -0.0036 0.0238  167 SER   A C   
3822 C  C   B SER   A 167 ? 0.1927 0.2788 0.2644 -0.0150 0.0314  0.0205  167 SER   A C   
3823 O  O   A SER   A 167 ? 0.1786 0.3487 0.2182 0.0221  -0.0018 0.0188  167 SER   A O   
3824 O  O   B SER   A 167 ? 0.2103 0.2867 0.2859 -0.0172 0.0258  0.0182  167 SER   A O   
3825 C  CB  A SER   A 167 ? 0.1715 0.3639 0.2263 0.0055  -0.0063 0.0257  167 SER   A CB  
3826 C  CB  B SER   A 167 ? 0.2094 0.2817 0.2828 -0.0177 0.0120  0.0160  167 SER   A CB  
3827 O  OG  A SER   A 167 ? 0.1617 0.3700 0.2239 0.0046  0.0140  0.0328  167 SER   A OG  
3828 O  OG  B SER   A 167 ? 0.2202 0.2839 0.2983 -0.0188 0.0024  0.0167  167 SER   A OG  
3839 N  N   A PHE   A 168 ? 0.1598 0.3265 0.2207 0.0246  0.0104  0.0269  168 PHE   A N   
3840 N  N   B PHE   A 168 ? 0.1741 0.2705 0.2410 -0.0118 0.0402  0.0279  168 PHE   A N   
3841 C  CA  A PHE   A 168 ? 0.1689 0.3142 0.2437 0.0131  0.0219  0.0309  168 PHE   A CA  
3842 C  CA  B PHE   A 168 ? 0.1637 0.2679 0.2169 -0.0099 0.0440  0.0323  168 PHE   A CA  
3843 C  C   A PHE   A 168 ? 0.1811 0.3187 0.2858 0.0017  0.0499  0.0211  168 PHE   A C   
3844 C  C   B PHE   A 168 ? 0.1612 0.2661 0.2138 -0.0127 0.0435  0.0318  168 PHE   A C   
3845 O  O   A PHE   A 168 ? 0.1936 0.3250 0.3273 -0.0103 0.0533  0.0319  168 PHE   A O   
3846 O  O   B PHE   A 168 ? 0.1467 0.2639 0.1983 -0.0120 0.0507  0.0364  168 PHE   A O   
3847 C  CB  A PHE   A 168 ? 0.1696 0.3035 0.2253 0.0020  0.0111  0.0323  168 PHE   A CB  
3848 C  CB  B PHE   A 168 ? 0.1669 0.2673 0.2126 -0.0088 0.0359  0.0384  168 PHE   A CB  
3849 C  CG  A PHE   A 168 ? 0.1671 0.2965 0.2133 -0.0075 0.0070  0.0295  168 PHE   A CG  
3850 C  CG  B PHE   A 168 ? 0.1703 0.2646 0.2135 -0.0056 0.0265  0.0465  168 PHE   A CG  
3851 C  CD1 A PHE   A 168 ? 0.1625 0.2969 0.2121 -0.0133 0.0017  0.0327  168 PHE   A CD1 
3852 C  CD1 B PHE   A 168 ? 0.1728 0.2655 0.2167 -0.0049 0.0253  0.0526  168 PHE   A CD1 
3853 C  CD2 A PHE   A 168 ? 0.1645 0.2907 0.2019 -0.0117 0.0187  0.0205  168 PHE   A CD2 
3854 C  CD2 B PHE   A 168 ? 0.1704 0.2625 0.2111 -0.0005 0.0161  0.0495  168 PHE   A CD2 
3855 C  CE1 A PHE   A 168 ? 0.1509 0.2898 0.1948 -0.0144 -0.0041 0.0290  168 PHE   A CE1 
3856 C  CE1 B PHE   A 168 ? 0.1724 0.2646 0.2203 -0.0026 0.0208  0.0566  168 PHE   A CE1 
3857 C  CE2 A PHE   A 168 ? 0.1705 0.2827 0.1970 -0.0135 0.0110  0.0228  168 PHE   A CE2 
3858 C  CE2 B PHE   A 168 ? 0.1737 0.2612 0.2165 0.0037  0.0076  0.0536  168 PHE   A CE2 
3859 C  CZ  A PHE   A 168 ? 0.1597 0.2840 0.1895 -0.0186 0.0029  0.0268  168 PHE   A CZ  
3860 C  CZ  B PHE   A 168 ? 0.1753 0.2621 0.2201 0.0008  0.0151  0.0541  168 PHE   A CZ  
3879 N  N   A LEU   A 169 ? 0.2055 0.3194 0.3138 -0.0029 0.0558  0.0031  169 LEU   A N   
3880 N  N   B LEU   A 169 ? 0.1716 0.2677 0.2284 -0.0127 0.0349  0.0314  169 LEU   A N   
3881 C  CA  A LEU   A 169 ? 0.2417 0.3275 0.3577 -0.0009 0.0439  -0.0056 169 LEU   A CA  
3882 C  CA  B LEU   A 169 ? 0.1888 0.2741 0.2474 -0.0154 0.0249  0.0236  169 LEU   A CA  
3883 C  C   A LEU   A 169 ? 0.2343 0.3201 0.3695 -0.0025 0.0572  0.0082  169 LEU   A C   
3884 C  C   B LEU   A 169 ? 0.1993 0.2802 0.2597 -0.0078 0.0185  0.0190  169 LEU   A C   
3885 O  O   A LEU   A 169 ? 0.2395 0.3194 0.3803 0.0049  0.0485  0.0067  169 LEU   A O   
3886 O  O   B LEU   A 169 ? 0.1973 0.2829 0.2624 -0.0075 0.0109  0.0163  169 LEU   A O   
3887 C  CB  A LEU   A 169 ? 0.2722 0.3429 0.3697 0.0002  0.0321  -0.0223 169 LEU   A CB  
3888 C  CB  B LEU   A 169 ? 0.1946 0.2755 0.2500 -0.0240 0.0188  0.0233  169 LEU   A CB  
3889 C  CG  A LEU   A 169 ? 0.3008 0.3538 0.3808 -0.0014 0.0207  -0.0431 169 LEU   A CG  
3890 C  CG  B LEU   A 169 ? 0.1974 0.2752 0.2571 -0.0309 0.0163  0.0237  169 LEU   A CG  
3891 C  CD1 A LEU   A 169 ? 0.3123 0.3566 0.3863 -0.0008 0.0153  -0.0474 169 LEU   A CD1 
3892 C  CD1 B LEU   A 169 ? 0.1973 0.2774 0.2695 -0.0341 0.0100  0.0239  169 LEU   A CD1 
3893 C  CD2 A LEU   A 169 ? 0.3090 0.3592 0.3800 -0.0040 0.0221  -0.0485 169 LEU   A CD2 
3894 C  CD2 B LEU   A 169 ? 0.2029 0.2750 0.2578 -0.0360 0.0171  0.0222  169 LEU   A CD2 
3895 O  OXT A LEU   A 169 ? 0.2199 0.3205 0.3633 -0.0086 0.0779  0.0152  169 LEU   A OXT 
3896 O  OXT B LEU   A 169 ? 0.2143 0.2852 0.2726 -0.0080 0.0137  0.0188  169 LEU   A OXT 
3919 N  N   A SER   B 1   ? 0.3591 0.3360 0.3463 -0.1226 -0.0784 0.0399  1   SER   B N   
3920 N  N   B SER   B 1   ? 0.3378 0.3309 0.3418 -0.0643 -0.0458 0.0190  1   SER   B N   
3921 C  CA  A SER   B 1   ? 0.3476 0.3415 0.3529 -0.1279 -0.0891 0.0375  1   SER   B CA  
3922 C  CA  B SER   B 1   ? 0.3329 0.3328 0.3413 -0.0649 -0.0468 0.0190  1   SER   B CA  
3923 C  C   A SER   B 1   ? 0.3190 0.3430 0.3403 -0.1297 -0.0961 0.0557  1   SER   B C   
3924 C  C   B SER   B 1   ? 0.3207 0.3335 0.3326 -0.0631 -0.0498 0.0293  1   SER   B C   
3925 O  O   A SER   B 1   ? 0.3305 0.3458 0.3256 -0.1233 -0.0907 0.0510  1   SER   B O   
3926 O  O   B SER   B 1   ? 0.3242 0.3336 0.3242 -0.0624 -0.0498 0.0263  1   SER   B O   
3927 C  CB  A SER   B 1   ? 0.3614 0.3402 0.3713 -0.1281 -0.0801 0.0223  1   SER   B CB  
3928 C  CB  B SER   B 1   ? 0.3384 0.3322 0.3492 -0.0656 -0.0410 0.0094  1   SER   B CB  
3929 O  OG  A SER   B 1   ? 0.3798 0.3533 0.4185 -0.1206 -0.0671 0.0179  1   SER   B OG  
3930 O  OG  B SER   B 1   ? 0.3451 0.3365 0.3680 -0.0653 -0.0364 0.0048  1   SER   B OG  
3945 N  N   A MET   B 2   ? 0.2892 0.3393 0.3356 -0.1303 -0.0943 0.0999  2   MET   B N   
3946 N  N   B MET   B 2   ? 0.3074 0.3334 0.3270 -0.0602 -0.0494 0.0501  2   MET   B N   
3947 C  CA  A MET   B 2   ? 0.2738 0.3419 0.3548 -0.1072 -0.0902 0.1194  2   MET   B CA  
3948 C  CA  B MET   B 2   ? 0.2948 0.3322 0.3254 -0.0517 -0.0477 0.0658  2   MET   B CA  
3949 C  C   A MET   B 2   ? 0.2406 0.3248 0.3348 -0.0813 -0.0985 0.1427  2   MET   B C   
3950 C  C   B MET   B 2   ? 0.2730 0.3169 0.3016 -0.0478 -0.0434 0.0731  2   MET   B C   
3951 O  O   A MET   B 2   ? 0.2309 0.3381 0.3399 -0.0644 -0.1131 0.1440  2   MET   B O   
3952 O  O   B MET   B 2   ? 0.2733 0.3218 0.3040 -0.0446 -0.0395 0.0696  2   MET   B O   
3953 C  CB  A MET   B 2   ? 0.3036 0.3732 0.4313 -0.0884 -0.0692 0.0896  2   MET   B CB  
3954 C  CB  B MET   B 2   ? 0.3062 0.3478 0.3572 -0.0413 -0.0482 0.0682  2   MET   B CB  
3955 C  CG  A MET   B 2   ? 0.3343 0.4006 0.5043 -0.0652 -0.0477 0.0717  2   MET   B CG  
3956 C  CG  B MET   B 2   ? 0.3157 0.3607 0.3825 -0.0306 -0.0488 0.0772  2   MET   B CG  
3957 S  SD  A MET   B 2   ? 0.3663 0.4279 0.5746 -0.0437 -0.0322 0.0563  2   MET   B SD  
3958 S  SD  B MET   B 2   ? 0.3258 0.3745 0.4039 -0.0193 -0.0524 0.0870  2   MET   B SD  
3959 C  CE  A MET   B 2   ? 0.3682 0.4303 0.5737 -0.0435 -0.0228 0.0562  2   MET   B CE  
3960 C  CE  B MET   B 2   ? 0.3257 0.3751 0.4107 -0.0200 -0.0491 0.0810  2   MET   B CE  
3979 N  N   A VAL   B 3   ? 0.2152 0.2887 0.3102 -0.0843 -0.0853 0.1594  3   VAL   B N   
3980 N  N   B VAL   B 3   ? 0.2500 0.2947 0.2779 -0.0499 -0.0423 0.0850  3   VAL   B N   
3981 C  CA  A VAL   B 3   ? 0.2050 0.2596 0.3081 -0.0740 -0.0789 0.1382  3   VAL   B CA  
3982 C  CA  B VAL   B 3   ? 0.2293 0.2725 0.2630 -0.0483 -0.0428 0.0853  3   VAL   B CA  
3983 C  C   A VAL   B 3   ? 0.1886 0.2491 0.2700 -0.0655 -0.0748 0.1181  3   VAL   B C   
3984 C  C   B VAL   B 3   ? 0.2042 0.2539 0.2366 -0.0500 -0.0517 0.0939  3   VAL   B C   
3985 O  O   A VAL   B 3   ? 0.1901 0.2552 0.2851 -0.0660 -0.0755 0.1212  3   VAL   B O   
3986 O  O   B VAL   B 3   ? 0.2034 0.2596 0.2283 -0.0364 -0.0550 0.1049  3   VAL   B O   
3987 C  CB  A VAL   B 3   ? 0.2208 0.2566 0.3547 -0.0753 -0.0682 0.1165  3   VAL   B CB  
3988 C  CB  B VAL   B 3   ? 0.2354 0.2703 0.2779 -0.0477 -0.0337 0.0768  3   VAL   B CB  
3989 C  CG1 A VAL   B 3   ? 0.2304 0.2507 0.3731 -0.0800 -0.0642 0.1104  3   VAL   B CG1 
3990 C  CG1 B VAL   B 3   ? 0.2388 0.2683 0.2863 -0.0487 -0.0304 0.0721  3   VAL   B CG1 
3991 C  CG2 A VAL   B 3   ? 0.2253 0.2628 0.3739 -0.0683 -0.0551 0.1181  3   VAL   B CG2 
3992 C  CG2 B VAL   B 3   ? 0.2370 0.2710 0.2844 -0.0461 -0.0296 0.0774  3   VAL   B CG2 
4011 N  N   . ASN   B 4   ? 0.1819 0.2284 0.2296 -0.0627 -0.0591 0.0933  4   ASN   B N   
4012 C  CA  . ASN   B 4   ? 0.1831 0.2246 0.1955 -0.0590 -0.0512 0.0584  4   ASN   B CA  
4013 C  C   . ASN   B 4   ? 0.1882 0.2365 0.1903 -0.0566 -0.0478 0.0432  4   ASN   B C   
4014 O  O   . ASN   B 4   ? 0.1897 0.2420 0.2126 -0.0560 -0.0317 0.0172  4   ASN   B O   
4015 C  CB  . ASN   B 4   ? 0.1814 0.2218 0.1759 -0.0515 -0.0609 0.0416  4   ASN   B CB  
4016 C  CG  . ASN   B 4   ? 0.1837 0.1975 0.1660 -0.0535 -0.0565 0.0398  4   ASN   B CG  
4017 O  OD1 . ASN   B 4   ? 0.1924 0.1802 0.1758 -0.0503 -0.0511 0.0357  4   ASN   B OD1 
4018 N  ND2 . ASN   B 4   ? 0.2083 0.2003 0.1872 -0.0305 -0.0372 0.0320  4   ASN   B ND2 
4026 N  N   . SER   B 5   ? 0.2010 0.2557 0.2085 -0.0522 -0.0379 0.0370  5   SER   B N   
4027 C  CA  . SER   B 5   ? 0.2273 0.2909 0.2235 -0.0459 -0.0212 0.0352  5   SER   B CA  
4028 C  C   . SER   B 5   ? 0.2478 0.2976 0.2570 -0.0674 0.0113  0.0383  5   SER   B C   
4029 O  O   . SER   B 5   ? 0.2674 0.2941 0.3347 -0.0621 0.0552  0.0391  5   SER   B O   
4030 C  CB  . SER   B 5   ? 0.2403 0.3111 0.2407 -0.0350 -0.0058 0.0474  5   SER   B CB  
4031 O  OG  . SER   B 5   ? 0.2632 0.3322 0.2932 -0.0208 -0.0008 0.0559  5   SER   B OG  
4037 N  N   . PHE   B 6   ? 0.2698 0.3198 0.2328 -0.0733 0.0255  0.0422  6   PHE   B N   
4038 C  CA  . PHE   B 6   ? 0.2823 0.3253 0.1975 -0.0950 0.0329  0.0225  6   PHE   B CA  
4039 C  C   . PHE   B 6   ? 0.3376 0.3600 0.2458 -0.1039 0.0688  -0.0025 6   PHE   B C   
4040 O  O   . PHE   B 6   ? 0.3528 0.3884 0.2793 -0.0994 0.0560  -0.0172 6   PHE   B O   
4041 C  CB  . PHE   B 6   ? 0.2509 0.3014 0.1754 -0.0837 0.0059  0.0139  6   PHE   B CB  
4042 C  CG  . PHE   B 6   ? 0.2206 0.2661 0.1680 -0.0733 -0.0058 0.0117  6   PHE   B CG  
4043 C  CD1 . PHE   B 6   ? 0.2196 0.2328 0.1546 -0.0646 -0.0148 0.0119  6   PHE   B CD1 
4044 C  CD2 . PHE   B 6   ? 0.1958 0.2587 0.1695 -0.0646 -0.0042 0.0424  6   PHE   B CD2 
4045 C  CE1 . PHE   B 6   ? 0.2128 0.2056 0.1676 -0.0576 -0.0162 0.0112  6   PHE   B CE1 
4046 C  CE2 . PHE   B 6   ? 0.1973 0.2424 0.1979 -0.0499 -0.0001 0.0377  6   PHE   B CE2 
4047 C  CZ  . PHE   B 6   ? 0.2004 0.2167 0.1868 -0.0479 -0.0101 0.0162  6   PHE   B CZ  
4057 N  N   . SER   B 7   ? 0.3779 0.3551 0.2725 -0.1270 0.1072  -0.0264 7   SER   B N   
4058 C  CA  . SER   B 7   ? 0.4216 0.3798 0.3371 -0.1266 0.1317  -0.0380 7   SER   B CA  
4059 C  C   . SER   B 7   ? 0.4167 0.3519 0.3248 -0.1289 0.1494  -0.0585 7   SER   B C   
4060 O  O   . SER   B 7   ? 0.4277 0.3440 0.3537 -0.1337 0.1438  -0.0655 7   SER   B O   
4061 C  CB  . SER   B 7   ? 0.4509 0.4123 0.4097 -0.1262 0.1484  -0.0259 7   SER   B CB  
4062 O  OG  . SER   B 7   ? 0.4520 0.4145 0.4665 -0.1271 0.1563  -0.0163 7   SER   B OG  
4068 N  N   . GLY   B 8   ? 0.4088 0.3335 0.3207 -0.1129 0.1522  -0.0726 8   GLY   B N   
4069 C  CA  . GLY   B 8   ? 0.3918 0.3136 0.3194 -0.1042 0.1536  -0.0781 8   GLY   B CA  
4070 C  C   . GLY   B 8   ? 0.3667 0.2833 0.3082 -0.1006 0.1525  -0.0718 8   GLY   B C   
4071 O  O   . GLY   B 8   ? 0.3798 0.2908 0.3483 -0.0887 0.1521  -0.0819 8   GLY   B O   
4075 N  N   . TYR   B 9   ? 0.3432 0.2585 0.2776 -0.0871 0.1159  -0.0792 9   TYR   B N   
4076 C  CA  . TYR   B 9   ? 0.3165 0.2282 0.2470 -0.0749 0.0833  -0.0625 9   TYR   B CA  
4077 C  C   . TYR   B 9   ? 0.3093 0.2211 0.2280 -0.0664 0.0487  -0.0472 9   TYR   B C   
4078 O  O   . TYR   B 9   ? 0.3218 0.2443 0.2690 -0.0653 0.0484  -0.0346 9   TYR   B O   
4079 C  CB  . TYR   B 9   ? 0.3066 0.2063 0.2486 -0.0662 0.0752  -0.0569 9   TYR   B CB  
4080 C  CG  . TYR   B 9   ? 0.2954 0.1889 0.2458 -0.0705 0.0681  -0.0597 9   TYR   B CG  
4081 C  CD1 . TYR   B 9   ? 0.2962 0.1914 0.2605 -0.0842 0.0742  -0.0510 9   TYR   B CD1 
4082 C  CD2 . TYR   B 9   ? 0.2819 0.1857 0.2299 -0.0619 0.0643  -0.0657 9   TYR   B CD2 
4083 C  CE1 . TYR   B 9   ? 0.2926 0.2003 0.2585 -0.0862 0.0783  -0.0655 9   TYR   B CE1 
4084 C  CE2 . TYR   B 9   ? 0.2856 0.1824 0.2433 -0.0612 0.0623  -0.0603 9   TYR   B CE2 
4085 C  CZ  . TYR   B 9   ? 0.2871 0.1993 0.2544 -0.0764 0.0707  -0.0686 9   TYR   B CZ  
4086 O  OH  . TYR   B 9   ? 0.2870 0.2082 0.2712 -0.0853 0.0675  -0.0839 9   TYR   B OH  
4096 N  N   . LEU   B 10  ? 0.2897 0.1919 0.2060 -0.0618 0.0262  -0.0434 10  LEU   B N   
4097 C  CA  . LEU   B 10  ? 0.2929 0.1952 0.2052 -0.0717 -0.0080 -0.0381 10  LEU   B CA  
4098 C  C   . LEU   B 10  ? 0.2724 0.1966 0.2089 -0.0679 -0.0230 -0.0337 10  LEU   B C   
4099 O  O   . LEU   B 10  ? 0.2460 0.1956 0.2109 -0.0525 -0.0121 -0.0251 10  LEU   B O   
4100 C  CB  . LEU   B 10  ? 0.3147 0.1900 0.2302 -0.0809 -0.0266 -0.0161 10  LEU   B CB  
4101 C  CG  . LEU   B 10  ? 0.3402 0.1979 0.2658 -0.0730 -0.0542 -0.0050 10  LEU   B CG  
4102 C  CD1 . LEU   B 10  ? 0.3554 0.2052 0.2851 -0.0699 -0.0520 -0.0047 10  LEU   B CD1 
4103 C  CD2 . LEU   B 10  ? 0.3490 0.2049 0.2990 -0.0722 -0.0521 0.0117  10  LEU   B CD2 
4115 N  N   . LYS   B 11  ? 0.2881 0.2239 0.2130 -0.0702 -0.0293 -0.0256 11  LYS   B N   
4116 C  CA  . LYS   B 11  ? 0.3111 0.2493 0.2520 -0.0558 -0.0319 -0.0323 11  LYS   B CA  
4117 C  C   . LYS   B 11  ? 0.2915 0.2264 0.2555 -0.0741 -0.0331 -0.0434 11  LYS   B C   
4118 O  O   . LYS   B 11  ? 0.3061 0.2446 0.2897 -0.0892 -0.0323 -0.0733 11  LYS   B O   
4119 C  CB  . LYS   B 11  ? 0.3476 0.3003 0.3142 -0.0321 -0.0350 -0.0323 11  LYS   B CB  
4120 C  CG  . LYS   B 11  ? 0.3795 0.3346 0.3876 -0.0181 -0.0366 -0.0333 11  LYS   B CG  
4121 C  CD  . LYS   B 11  ? 0.4048 0.3577 0.4522 -0.0068 -0.0358 -0.0327 11  LYS   B CD  
4122 C  CE  . LYS   B 11  ? 0.4222 0.3735 0.4983 -0.0040 -0.0354 -0.0330 11  LYS   B CE  
4123 N  NZ  . LYS   B 11  ? 0.4318 0.3836 0.5218 -0.0040 -0.0366 -0.0314 11  LYS   B NZ  
4137 N  N   . LEU   B 12  ? 0.2550 0.2044 0.2477 -0.0635 -0.0270 -0.0402 12  LEU   B N   
4138 C  CA  . LEU   B 12  ? 0.2379 0.1811 0.2695 -0.0551 -0.0171 -0.0387 12  LEU   B CA  
4139 C  C   . LEU   B 12  ? 0.2225 0.1835 0.2829 -0.0526 -0.0345 -0.0355 12  LEU   B C   
4140 O  O   . LEU   B 12  ? 0.2189 0.1843 0.2999 -0.0570 -0.0484 -0.0261 12  LEU   B O   
4141 C  CB  . LEU   B 12  ? 0.2394 0.1609 0.2725 -0.0418 -0.0090 -0.0384 12  LEU   B CB  
4142 C  CG  . LEU   B 12  ? 0.2390 0.1608 0.2654 -0.0433 -0.0071 -0.0249 12  LEU   B CG  
4143 C  CD1 . LEU   B 12  ? 0.2485 0.1640 0.2531 -0.0235 -0.0067 -0.0073 12  LEU   B CD1 
4144 C  CD2 . LEU   B 12  ? 0.2412 0.1656 0.2765 -0.0468 -0.0021 -0.0275 12  LEU   B CD2 
4156 N  N   . THR   B 13  ? 0.2065 0.1867 0.2772 -0.0534 -0.0358 -0.0421 13  THR   B N   
4157 C  CA  . THR   B 13  ? 0.2041 0.1947 0.2694 -0.0615 -0.0553 -0.0228 13  THR   B CA  
4158 C  C   . THR   B 13  ? 0.2525 0.2148 0.2859 -0.0696 -0.0725 -0.0112 13  THR   B C   
4159 O  O   . THR   B 13  ? 0.2729 0.2138 0.2982 -0.0714 -0.0383 -0.0207 13  THR   B O   
4160 C  CB  . THR   B 13  ? 0.1914 0.1981 0.2725 -0.0522 -0.0502 -0.0123 13  THR   B CB  
4161 O  OG1 . THR   B 13  ? 0.1818 0.1915 0.2827 -0.0429 -0.0364 -0.0183 13  THR   B OG1 
4162 C  CG2 . THR   B 13  ? 0.2020 0.2048 0.2761 -0.0458 -0.0413 -0.0025 13  THR   B CG2 
4170 N  N   A ASP   B 14  ? 0.2691 0.2272 0.2934 -0.0738 -0.1077 -0.0029 14  ASP   B N   
4171 N  N   B ASP   B 14  ? 0.2636 0.2242 0.2959 -0.0677 -0.0795 -0.0052 14  ASP   B N   
4172 C  CA  A ASP   B 14  ? 0.2863 0.2431 0.3193 -0.0728 -0.1117 0.0143  14  ASP   B CA  
4173 C  CA  B ASP   B 14  ? 0.2733 0.2338 0.3106 -0.0643 -0.0776 0.0039  14  ASP   B CA  
4174 C  C   A ASP   B 14  ? 0.2750 0.2262 0.2779 -0.0749 -0.0949 0.0190  14  ASP   B C   
4175 C  C   B ASP   B 14  ? 0.2587 0.2177 0.2750 -0.0635 -0.0792 0.0080  14  ASP   B C   
4176 O  O   A ASP   B 14  ? 0.3020 0.2423 0.2840 -0.0757 -0.0913 0.0366  14  ASP   B O   
4177 O  O   B ASP   B 14  ? 0.2676 0.2179 0.2730 -0.0594 -0.0802 0.0095  14  ASP   B O   
4178 C  CB  A ASP   B 14  ? 0.3079 0.2783 0.3960 -0.0688 -0.1234 0.0150  14  ASP   B CB  
4179 C  CB  B ASP   B 14  ? 0.2933 0.2578 0.3631 -0.0603 -0.0715 0.0047  14  ASP   B CB  
4180 C  CG  A ASP   B 14  ? 0.3333 0.3095 0.4706 -0.0616 -0.1185 0.0024  14  ASP   B CG  
4181 C  CG  B ASP   B 14  ? 0.3120 0.2778 0.4099 -0.0557 -0.0642 0.0000  14  ASP   B CG  
4182 O  OD1 A ASP   B 14  ? 0.3476 0.3196 0.4888 -0.0651 -0.1195 -0.0120 14  ASP   B OD1 
4183 O  OD1 B ASP   B 14  ? 0.3187 0.2860 0.4227 -0.0553 -0.0613 -0.0046 14  ASP   B OD1 
4184 O  OD2 A ASP   B 14  ? 0.3375 0.3218 0.5066 -0.0600 -0.1112 0.0046  14  ASP   B OD2 
4185 O  OD2 B ASP   B 14  ? 0.3179 0.2831 0.4278 -0.0579 -0.0627 0.0004  14  ASP   B OD2 
4194 N  N   . ASN   B 15  ? 0.2354 0.1998 0.2520 -0.0600 -0.0797 0.0139  15  ASN   B N   
4195 C  CA  . ASN   B 15  ? 0.1869 0.1755 0.2362 -0.0412 -0.0564 0.0023  15  ASN   B CA  
4196 C  C   . ASN   B 15  ? 0.1690 0.1598 0.2202 -0.0259 -0.0508 -0.0031 15  ASN   B C   
4197 O  O   . ASN   B 15  ? 0.1743 0.1532 0.2364 -0.0251 -0.0530 -0.0108 15  ASN   B O   
4198 C  CB  . ASN   B 15  ? 0.1796 0.1688 0.2585 -0.0234 -0.0551 0.0058  15  ASN   B CB  
4199 C  CG  . ASN   B 15  ? 0.1654 0.1673 0.2636 -0.0312 -0.0301 0.0098  15  ASN   B CG  
4200 O  OD1 . ASN   B 15  ? 0.1707 0.1954 0.2899 -0.0446 -0.0357 0.0143  15  ASN   B OD1 
4201 N  ND2 . ASN   B 15  ? 0.1625 0.1441 0.2480 -0.0201 -0.0066 -0.0063 15  ASN   B ND2 
4209 N  N   . VAL   B 16  ? 0.1730 0.1474 0.2226 -0.0337 -0.0513 0.0006  16  VAL   B N   
4210 C  CA  . VAL   B 16  ? 0.1757 0.1518 0.2078 -0.0294 -0.0395 -0.0193 16  VAL   B CA  
4211 C  C   . VAL   B 16  ? 0.1732 0.1633 0.2014 -0.0341 -0.0335 -0.0123 16  VAL   B C   
4212 O  O   . VAL   B 16  ? 0.1761 0.1764 0.2200 -0.0311 -0.0310 -0.0333 16  VAL   B O   
4213 C  CB  . VAL   B 16  ? 0.1802 0.1534 0.2186 -0.0200 -0.0222 -0.0225 16  VAL   B CB  
4214 C  CG1 . VAL   B 16  ? 0.1872 0.1505 0.2177 -0.0067 -0.0207 -0.0096 16  VAL   B CG1 
4215 C  CG2 . VAL   B 16  ? 0.1861 0.1604 0.2376 -0.0094 -0.0138 -0.0183 16  VAL   B CG2 
4225 N  N   . TYR   B 17  ? 0.1792 0.1750 0.2061 -0.0334 -0.0306 -0.0196 17  TYR   B N   
4226 C  CA  . TYR   B 17  ? 0.1893 0.1862 0.2028 -0.0440 -0.0271 -0.0012 17  TYR   B CA  
4227 C  C   . TYR   B 17  ? 0.1813 0.1546 0.1942 -0.0475 -0.0201 -0.0067 17  TYR   B C   
4228 O  O   . TYR   B 17  ? 0.1762 0.1661 0.1999 -0.0378 -0.0289 -0.0323 17  TYR   B O   
4229 C  CB  . TYR   B 17  ? 0.2194 0.2286 0.2313 -0.0291 -0.0302 0.0309  17  TYR   B CB  
4230 C  CG  . TYR   B 17  ? 0.2485 0.2753 0.2727 -0.0225 -0.0491 0.0385  17  TYR   B CG  
4231 C  CD1 . TYR   B 17  ? 0.2675 0.2937 0.2885 -0.0191 -0.0646 0.0515  17  TYR   B CD1 
4232 C  CD2 . TYR   B 17  ? 0.2720 0.3025 0.3022 -0.0098 -0.0589 0.0398  17  TYR   B CD2 
4233 C  CE1 . TYR   B 17  ? 0.2866 0.3223 0.3085 -0.0086 -0.0773 0.0458  17  TYR   B CE1 
4234 C  CE2 . TYR   B 17  ? 0.2909 0.3264 0.3242 0.0035  -0.0762 0.0472  17  TYR   B CE2 
4235 C  CZ  . TYR   B 17  ? 0.3006 0.3365 0.3248 0.0055  -0.0858 0.0475  17  TYR   B CZ  
4236 O  OH  . TYR   B 17  ? 0.3167 0.3506 0.3411 0.0149  -0.0955 0.0489  17  TYR   B OH  
4246 N  N   . ILE   B 18  ? 0.1891 0.1582 0.1941 -0.0345 -0.0039 -0.0180 18  ILE   B N   
4247 C  CA  . ILE   B 18  ? 0.1884 0.1526 0.1982 -0.0392 -0.0046 -0.0243 18  ILE   B CA  
4248 C  C   . ILE   B 18  ? 0.2010 0.1596 0.1963 -0.0507 -0.0091 -0.0376 18  ILE   B C   
4249 O  O   . ILE   B 18  ? 0.2205 0.1749 0.2057 -0.0433 0.0020  -0.0425 18  ILE   B O   
4250 C  CB  . ILE   B 18  ? 0.1976 0.1553 0.2114 -0.0434 -0.0081 -0.0219 18  ILE   B CB  
4251 C  CG1 . ILE   B 18  ? 0.1957 0.1602 0.2204 -0.0442 -0.0022 -0.0141 18  ILE   B CG1 
4252 C  CG2 . ILE   B 18  ? 0.2077 0.1634 0.2126 -0.0376 -0.0143 -0.0146 18  ILE   B CG2 
4253 C  CD1 . ILE   B 18  ? 0.2043 0.1882 0.2405 -0.0450 -0.0279 0.0124  18  ILE   B CD1 
4265 N  N   . LYS   B 19  ? 0.2058 0.1578 0.2116 -0.0275 0.0293  -0.0410 19  LYS   B N   
4266 C  CA  . LYS   B 19  ? 0.2152 0.1619 0.2345 -0.0277 0.0341  -0.0451 19  LYS   B CA  
4267 C  C   . LYS   B 19  ? 0.1983 0.1604 0.2483 -0.0268 0.0362  -0.0553 19  LYS   B C   
4268 O  O   . LYS   B 19  ? 0.1935 0.1635 0.2255 -0.0200 0.0281  -0.0458 19  LYS   B O   
4269 C  CB  . LYS   B 19  ? 0.2415 0.1865 0.2462 -0.0344 0.0437  -0.0349 19  LYS   B CB  
4270 C  CG  . LYS   B 19  ? 0.2686 0.2098 0.2729 -0.0465 0.0542  -0.0365 19  LYS   B CG  
4271 C  CD  . LYS   B 19  ? 0.2996 0.2408 0.2849 -0.0523 0.0640  -0.0350 19  LYS   B CD  
4272 C  CE  . LYS   B 19  ? 0.3285 0.2658 0.3075 -0.0523 0.0569  -0.0357 19  LYS   B CE  
4273 N  NZ  . LYS   B 19  ? 0.3441 0.2821 0.3156 -0.0558 0.0611  -0.0341 19  LYS   B NZ  
4287 N  N   . ASN   B 20  ? 0.1944 0.1713 0.2839 -0.0204 0.0372  -0.0675 20  ASN   B N   
4288 C  CA  . ASN   B 20  ? 0.1979 0.1858 0.3079 -0.0160 0.0418  -0.0826 20  ASN   B CA  
4289 C  C   . ASN   B 20  ? 0.1970 0.2062 0.3010 -0.0234 0.0530  -0.0958 20  ASN   B C   
4290 O  O   . ASN   B 20  ? 0.2189 0.2402 0.3183 -0.0369 0.0552  -0.0931 20  ASN   B O   
4291 C  CB  . ASN   B 20  ? 0.2315 0.1902 0.3395 0.0103  0.0295  -0.0871 20  ASN   B CB  
4292 C  CG  . ASN   B 20  ? 0.2588 0.2003 0.3616 0.0409  0.0275  -0.0929 20  ASN   B CG  
4293 O  OD1 . ASN   B 20  ? 0.2899 0.2295 0.3868 0.0528  0.0227  -0.0918 20  ASN   B OD1 
4294 N  ND2 . ASN   B 20  ? 0.2472 0.2012 0.3557 0.0421  0.0183  -0.0854 20  ASN   B ND2 
4301 N  N   . ALA   B 21  ? 0.1970 0.1926 0.2989 -0.0268 0.0537  -0.0775 21  ALA   B N   
4302 C  CA  . ALA   B 21  ? 0.2070 0.2020 0.3052 -0.0338 0.0444  -0.0583 21  ALA   B CA  
4303 C  C   . ALA   B 21  ? 0.2065 0.1725 0.2864 -0.0250 0.0518  -0.0458 21  ALA   B C   
4304 O  O   . ALA   B 21  ? 0.2114 0.1609 0.2836 -0.0329 0.0447  -0.0347 21  ALA   B O   
4305 C  CB  . ALA   B 21  ? 0.2233 0.2314 0.3122 -0.0453 0.0510  -0.0454 21  ALA   B CB  
4311 N  N   . ASP   B 22  ? 0.1950 0.1609 0.2751 -0.0269 0.0436  -0.0353 22  ASP   B N   
4312 C  CA  . ASP   B 22  ? 0.1913 0.1528 0.2555 -0.0117 0.0377  -0.0226 22  ASP   B CA  
4313 C  C   . ASP   B 22  ? 0.1829 0.1528 0.2150 -0.0166 0.0216  -0.0132 22  ASP   B C   
4314 O  O   . ASP   B 22  ? 0.1843 0.1561 0.2125 -0.0126 0.0134  -0.0157 22  ASP   B O   
4315 C  CB  . ASP   B 22  ? 0.2014 0.1608 0.2948 -0.0038 0.0356  -0.0093 22  ASP   B CB  
4316 C  CG  . ASP   B 22  ? 0.2062 0.1806 0.3358 0.0056  0.0140  -0.0079 22  ASP   B CG  
4317 O  OD1 . ASP   B 22  ? 0.2174 0.1739 0.3333 0.0034  -0.0111 -0.0090 22  ASP   B OD1 
4318 O  OD2 . ASP   B 22  ? 0.2141 0.2131 0.3921 0.0115  -0.0053 -0.0217 22  ASP   B OD2 
4323 N  N   . ILE   B 23  ? 0.1837 0.1466 0.1940 -0.0119 0.0037  0.0150  23  ILE   B N   
4324 C  CA  . ILE   B 23  ? 0.1772 0.1425 0.1772 -0.0093 -0.0040 0.0082  23  ILE   B CA  
4325 C  C   . ILE   B 23  ? 0.1647 0.1421 0.1751 -0.0052 -0.0113 0.0034  23  ILE   B C   
4326 O  O   . ILE   B 23  ? 0.1569 0.1446 0.1657 -0.0077 -0.0086 0.0056  23  ILE   B O   
4327 C  CB  . ILE   B 23  ? 0.1683 0.1443 0.1964 -0.0241 -0.0007 0.0114  23  ILE   B CB  
4328 C  CG1 . ILE   B 23  ? 0.1726 0.1600 0.2086 -0.0147 0.0051  0.0250  23  ILE   B CG1 
4329 C  CG2 . ILE   B 23  ? 0.1760 0.1702 0.2073 -0.0170 -0.0005 0.0026  23  ILE   B CG2 
4330 C  CD1 . ILE   B 23  ? 0.1749 0.1714 0.2159 -0.0126 0.0062  0.0243  23  ILE   B CD1 
4342 N  N   . VAL   B 24  ? 0.1687 0.1432 0.1844 -0.0060 -0.0066 0.0015  24  VAL   B N   
4343 C  CA  . VAL   B 24  ? 0.1621 0.1505 0.2046 -0.0095 -0.0200 -0.0004 24  VAL   B CA  
4344 C  C   . VAL   B 24  ? 0.1623 0.1554 0.2110 -0.0155 -0.0102 0.0031  24  VAL   B C   
4345 O  O   . VAL   B 24  ? 0.1598 0.1657 0.2227 -0.0173 -0.0050 0.0153  24  VAL   B O   
4346 C  CB  . VAL   B 24  ? 0.1710 0.1674 0.2179 0.0051  -0.0244 -0.0049 24  VAL   B CB  
4347 C  CG1 . VAL   B 24  ? 0.1712 0.1754 0.2453 -0.0050 -0.0322 -0.0044 24  VAL   B CG1 
4348 C  CG2 . VAL   B 24  ? 0.1828 0.1948 0.2244 0.0063  -0.0281 -0.0130 24  VAL   B CG2 
4358 N  N   . GLU   B 25  ? 0.1828 0.1651 0.2063 -0.0149 -0.0027 0.0007  25  GLU   B N   
4359 C  CA  . GLU   B 25  ? 0.1978 0.1961 0.2244 -0.0006 0.0175  -0.0065 25  GLU   B CA  
4360 C  C   . GLU   B 25  ? 0.1874 0.1935 0.1951 -0.0128 0.0192  0.0028  25  GLU   B C   
4361 O  O   . GLU   B 25  ? 0.1868 0.2039 0.2158 -0.0115 0.0218  0.0056  25  GLU   B O   
4362 C  CB  . GLU   B 25  ? 0.2376 0.2493 0.2928 0.0243  0.0277  -0.0102 25  GLU   B CB  
4363 C  CG  . GLU   B 25  ? 0.2759 0.3223 0.4037 0.0307  0.0190  -0.0134 25  GLU   B CG  
4364 C  CD  . GLU   B 25  ? 0.3294 0.3800 0.4959 0.0276  0.0096  -0.0131 25  GLU   B CD  
4365 O  OE1 . GLU   B 25  ? 0.3548 0.3985 0.5287 0.0321  0.0120  -0.0096 25  GLU   B OE1 
4366 O  OE2 . GLU   B 25  ? 0.3500 0.3960 0.5275 0.0269  0.0017  -0.0201 25  GLU   B OE2 
4373 N  N   A GLU   B 26  ? 0.1825 0.1804 0.1771 -0.0297 0.0132  0.0014  26  GLU   B N   
4374 N  N   B GLU   B 26  ? 0.1863 0.1919 0.1893 -0.0227 0.0142  0.0043  26  GLU   B N   
4375 C  CA  A GLU   B 26  ? 0.1788 0.1928 0.1871 -0.0407 -0.0083 -0.0016 26  GLU   B CA  
4376 C  CA  B GLU   B 26  ? 0.1875 0.1970 0.1952 -0.0307 0.0055  0.0058  26  GLU   B CA  
4377 C  C   A GLU   B 26  ? 0.1640 0.1900 0.1589 -0.0294 0.0013  0.0112  26  GLU   B C   
4378 C  C   B GLU   B 26  ? 0.1712 0.1883 0.1733 -0.0267 0.0050  0.0133  26  GLU   B C   
4379 O  O   A GLU   B 26  ? 0.1868 0.2124 0.1676 -0.0245 -0.0023 0.0210  26  GLU   B O   
4380 O  O   B GLU   B 26  ? 0.1815 0.1983 0.1774 -0.0239 0.0019  0.0175  26  GLU   B O   
4381 C  CB  A GLU   B 26  ? 0.2102 0.2123 0.2186 -0.0515 -0.0020 0.0153  26  GLU   B CB  
4382 C  CB  B GLU   B 26  ? 0.2107 0.2113 0.2212 -0.0375 0.0116  0.0106  26  GLU   B CB  
4383 C  CG  A GLU   B 26  ? 0.2528 0.2490 0.2815 -0.0522 0.0124  0.0029  26  GLU   B CG  
4384 C  CG  B GLU   B 26  ? 0.2363 0.2325 0.2578 -0.0415 0.0209  0.0054  26  GLU   B CG  
4385 C  CD  A GLU   B 26  ? 0.2763 0.2708 0.3113 -0.0666 0.0252  -0.0292 26  GLU   B CD  
4386 C  CD  B GLU   B 26  ? 0.2521 0.2483 0.2779 -0.0533 0.0345  -0.0057 26  GLU   B CD  
4387 O  OE1 A GLU   B 26  ? 0.2909 0.2563 0.3203 -0.0771 0.0608  -0.0383 26  GLU   B OE1 
4388 O  OE1 B GLU   B 26  ? 0.2625 0.2427 0.2738 -0.0593 0.0636  -0.0005 26  GLU   B OE1 
4389 O  OE2 A GLU   B 26  ? 0.2824 0.3038 0.3498 -0.0609 0.0207  -0.0294 26  GLU   B OE2 
4390 O  OE2 B GLU   B 26  ? 0.2542 0.2666 0.3070 -0.0536 0.0324  -0.0020 26  GLU   B OE2 
4403 N  N   . ALA   B 27  ? 0.1530 0.1717 0.1652 -0.0240 0.0033  0.0195  27  ALA   B N   
4404 C  CA  . ALA   B 27  ? 0.1517 0.1672 0.1896 -0.0159 -0.0003 0.0261  27  ALA   B CA  
4405 C  C   . ALA   B 27  ? 0.1558 0.1797 0.2175 -0.0188 0.0089  0.0420  27  ALA   B C   
4406 O  O   . ALA   B 27  ? 0.1679 0.1881 0.2282 -0.0078 0.0070  0.0461  27  ALA   B O   
4407 C  CB  . ALA   B 27  ? 0.1709 0.1550 0.1901 -0.0200 0.0013  0.0213  27  ALA   B CB  
4414 N  N   . LYS   B 28  ? 0.1549 0.1974 0.2647 -0.0211 0.0187  0.0568  28  LYS   B N   
4415 C  CA  . LYS   B 28  ? 0.1696 0.2403 0.2860 -0.0149 0.0513  0.0893  28  LYS   B CA  
4416 C  C   . LYS   B 28  ? 0.1978 0.2591 0.2753 -0.0045 0.0629  0.0771  28  LYS   B C   
4417 O  O   . LYS   B 28  ? 0.2247 0.2613 0.2848 -0.0073 0.0641  0.0757  28  LYS   B O   
4418 C  CB  . LYS   B 28  ? 0.1955 0.2809 0.3355 0.0003  0.0784  0.1067  28  LYS   B CB  
4419 C  CG  . LYS   B 28  ? 0.2363 0.3378 0.3776 0.0110  0.0815  0.1183  28  LYS   B CG  
4420 C  CD  . LYS   B 28  ? 0.2934 0.4042 0.4354 0.0162  0.0963  0.1171  28  LYS   B CD  
4421 C  CE  . LYS   B 28  ? 0.3334 0.4478 0.4801 0.0222  0.1018  0.1207  28  LYS   B CE  
4422 N  NZ  . LYS   B 28  ? 0.3765 0.4708 0.5032 0.0276  0.1022  0.1240  28  LYS   B NZ  
4436 N  N   . LYS   B 29  ? 0.2154 0.2842 0.2742 0.0159  0.0656  0.0620  29  LYS   B N   
4437 C  CA  . LYS   B 29  ? 0.2615 0.3218 0.2994 0.0146  0.0631  0.0624  29  LYS   B CA  
4438 C  C   . LYS   B 29  ? 0.2534 0.3225 0.2569 0.0120  0.0450  0.0748  29  LYS   B C   
4439 O  O   . LYS   B 29  ? 0.2698 0.3444 0.2676 0.0192  0.0444  0.0821  29  LYS   B O   
4440 C  CB  . LYS   B 29  ? 0.3199 0.3600 0.3866 0.0135  0.0595  0.0487  29  LYS   B CB  
4441 C  CG  . LYS   B 29  ? 0.3695 0.3898 0.4756 0.0117  0.0601  0.0445  29  LYS   B CG  
4442 C  CD  . LYS   B 29  ? 0.4147 0.4137 0.5464 0.0079  0.0665  0.0366  29  LYS   B CD  
4443 C  CE  . LYS   B 29  ? 0.4457 0.4306 0.5956 0.0040  0.0731  0.0311  29  LYS   B CE  
4444 N  NZ  . LYS   B 29  ? 0.4566 0.4373 0.6247 0.0015  0.0750  0.0283  29  LYS   B NZ  
4458 N  N   . VAL   B 30  ? 0.2213 0.3027 0.2352 -0.0023 0.0272  0.0734  30  VAL   B N   
4459 C  CA  . VAL   B 30  ? 0.2051 0.2908 0.2731 -0.0197 -0.0084 0.0784  30  VAL   B CA  
4460 C  C   . VAL   B 30  ? 0.1866 0.2832 0.2676 -0.0198 -0.0027 0.0983  30  VAL   B C   
4461 O  O   . VAL   B 30  ? 0.1981 0.2999 0.2736 -0.0100 -0.0013 0.1135  30  VAL   B O   
4462 C  CB  . VAL   B 30  ? 0.2132 0.2844 0.3154 -0.0387 -0.0348 0.0728  30  VAL   B CB  
4463 C  CG1 . VAL   B 30  ? 0.2198 0.2910 0.3161 -0.0395 -0.0276 0.0702  30  VAL   B CG1 
4464 C  CG2 . VAL   B 30  ? 0.2268 0.2830 0.3308 -0.0463 -0.0451 0.0591  30  VAL   B CG2 
4474 N  N   . LYS   B 31  ? 0.1770 0.2429 0.3019 -0.0351 -0.0031 0.1010  31  LYS   B N   
4475 C  CA  . LYS   B 31  ? 0.1631 0.2313 0.3382 -0.0458 -0.0118 0.1050  31  LYS   B CA  
4476 C  C   . LYS   B 31  ? 0.1582 0.1941 0.2852 -0.0403 -0.0317 0.0914  31  LYS   B C   
4477 O  O   . LYS   B 31  ? 0.1671 0.2116 0.3006 -0.0328 -0.0237 0.1056  31  LYS   B O   
4478 C  CB  . LYS   B 31  ? 0.1810 0.2800 0.3997 -0.0362 0.0138  0.1190  31  LYS   B CB  
4479 C  CG  . LYS   B 31  ? 0.2205 0.3292 0.4451 -0.0364 0.0315  0.1144  31  LYS   B CG  
4480 C  CD  . LYS   B 31  ? 0.2603 0.3780 0.4858 -0.0299 0.0321  0.1006  31  LYS   B CD  
4481 C  CE  . LYS   B 31  ? 0.2813 0.4069 0.5224 -0.0261 0.0262  0.0908  31  LYS   B CE  
4482 N  NZ  . LYS   B 31  ? 0.2979 0.4255 0.5362 -0.0176 0.0171  0.0802  31  LYS   B NZ  
4496 N  N   . PRO   B 32  ? 0.1709 0.1612 0.2268 -0.0377 -0.0443 0.0542  32  PRO   B N   
4497 C  CA  . PRO   B 32  ? 0.1801 0.1564 0.1809 -0.0358 -0.0434 0.0281  32  PRO   B CA  
4498 C  C   . PRO   B 32  ? 0.1910 0.1498 0.1811 -0.0384 -0.0563 0.0364  32  PRO   B C   
4499 O  O   . PRO   B 32  ? 0.2069 0.1493 0.2233 -0.0441 -0.0755 0.0399  32  PRO   B O   
4500 C  CB  . PRO   B 32  ? 0.1906 0.1523 0.1775 -0.0391 -0.0358 0.0232  32  PRO   B CB  
4501 C  CG  . PRO   B 32  ? 0.2088 0.1380 0.1884 -0.0362 -0.0479 0.0251  32  PRO   B CG  
4502 C  CD  . PRO   B 32  ? 0.1934 0.1455 0.2098 -0.0292 -0.0598 0.0297  32  PRO   B CD  
4510 N  N   . THR   B 33  ? 0.1925 0.1374 0.1781 -0.0335 -0.0543 0.0238  33  THR   B N   
4511 C  CA  . THR   B 33  ? 0.1974 0.1440 0.1729 -0.0370 -0.0452 0.0321  33  THR   B CA  
4512 C  C   . THR   B 33  ? 0.1978 0.1350 0.1665 -0.0336 -0.0475 0.0192  33  THR   B C   
4513 O  O   . THR   B 33  ? 0.2202 0.1365 0.1811 -0.0454 -0.0568 0.0211  33  THR   B O   
4514 C  CB  . THR   B 33  ? 0.2078 0.1549 0.1847 -0.0218 -0.0510 0.0323  33  THR   B CB  
4515 O  OG1 . THR   B 33  ? 0.1954 0.1638 0.1852 -0.0254 -0.0479 0.0397  33  THR   B OG1 
4516 C  CG2 . THR   B 33  ? 0.2357 0.1573 0.2035 -0.0164 -0.0538 0.0232  33  THR   B CG2 
4524 N  N   . VAL   B 34  ? 0.1819 0.1345 0.1502 -0.0368 -0.0379 0.0202  34  VAL   B N   
4525 C  CA  . VAL   B 34  ? 0.1710 0.1326 0.1438 -0.0287 -0.0354 0.0080  34  VAL   B CA  
4526 C  C   . VAL   B 34  ? 0.1539 0.1279 0.1309 -0.0234 -0.0224 0.0056  34  VAL   B C   
4527 O  O   . VAL   B 34  ? 0.1731 0.1320 0.1374 -0.0215 -0.0351 0.0056  34  VAL   B O   
4528 C  CB  . VAL   B 34  ? 0.1792 0.1400 0.1833 -0.0100 -0.0267 0.0068  34  VAL   B CB  
4529 C  CG1 . VAL   B 34  ? 0.1779 0.1559 0.1834 -0.0090 -0.0128 -0.0006 34  VAL   B CG1 
4530 C  CG2 . VAL   B 34  ? 0.1801 0.1485 0.2173 -0.0122 -0.0267 0.0109  34  VAL   B CG2 
4540 N  N   . VAL   B 35  ? 0.1432 0.1259 0.1317 -0.0267 -0.0187 0.0075  35  VAL   B N   
4541 C  CA  . VAL   B 35  ? 0.1404 0.1213 0.1274 -0.0217 -0.0075 0.0059  35  VAL   B CA  
4542 C  C   . VAL   B 35  ? 0.1319 0.1183 0.1320 -0.0181 -0.0136 0.0060  35  VAL   B C   
4543 O  O   . VAL   B 35  ? 0.1365 0.1255 0.1431 -0.0229 0.0001  -0.0002 35  VAL   B O   
4544 C  CB  . VAL   B 35  ? 0.1435 0.1423 0.1375 -0.0186 0.0055  0.0051  35  VAL   B CB  
4545 C  CG1 . VAL   B 35  ? 0.1364 0.1550 0.1589 -0.0221 0.0046  0.0069  35  VAL   B CG1 
4546 C  CG2 . VAL   B 35  ? 0.1463 0.1436 0.1599 -0.0090 -0.0020 0.0013  35  VAL   B CG2 
4556 N  N   . VAL   B 36  ? 0.1336 0.1216 0.1261 -0.0158 -0.0138 0.0103  36  VAL   B N   
4557 C  CA  . VAL   B 36  ? 0.1290 0.1196 0.1326 -0.0148 -0.0077 0.0020  36  VAL   B CA  
4558 C  C   . VAL   B 36  ? 0.1259 0.1218 0.1197 -0.0147 -0.0024 0.0006  36  VAL   B C   
4559 O  O   . VAL   B 36  ? 0.1351 0.1299 0.1495 -0.0107 -0.0013 -0.0063 36  VAL   B O   
4560 C  CB  . VAL   B 36  ? 0.1325 0.1279 0.1383 -0.0151 -0.0034 0.0040  36  VAL   B CB  
4561 C  CG1 . VAL   B 36  ? 0.1314 0.1373 0.1572 -0.0231 -0.0083 0.0086  36  VAL   B CG1 
4562 C  CG2 . VAL   B 36  ? 0.1365 0.1326 0.1458 -0.0145 -0.0160 0.0083  36  VAL   B CG2 
4572 N  N   . ASN   B 37  ? 0.1330 0.1226 0.1227 -0.0024 -0.0051 0.0040  37  ASN   B N   
4573 C  CA  . ASN   B 37  ? 0.1302 0.1272 0.1313 -0.0007 -0.0138 0.0026  37  ASN   B CA  
4574 C  C   . ASN   B 37  ? 0.1291 0.1282 0.1407 0.0011  -0.0162 0.0011  37  ASN   B C   
4575 O  O   . ASN   B 37  ? 0.1410 0.1338 0.1379 0.0005  -0.0002 0.0069  37  ASN   B O   
4576 C  CB  . ASN   B 37  ? 0.1296 0.1334 0.1246 -0.0004 -0.0165 0.0030  37  ASN   B CB  
4577 C  CG  . ASN   B 37  ? 0.1413 0.1316 0.1353 -0.0025 -0.0077 0.0029  37  ASN   B CG  
4578 O  OD1 . ASN   B 37  ? 0.1437 0.1313 0.1562 0.0097  -0.0147 0.0016  37  ASN   B OD1 
4579 N  ND2 . ASN   B 37  ? 0.1439 0.1288 0.1343 0.0009  -0.0194 0.0011  37  ASN   B ND2 
4586 N  N   . ALA   B 38  ? 0.1406 0.1235 0.1400 0.0063  0.0061  0.0013  38  ALA   B N   
4587 C  CA  . ALA   B 38  ? 0.1491 0.1295 0.1472 0.0032  -0.0006 0.0133  38  ALA   B CA  
4588 C  C   . ALA   B 38  ? 0.1443 0.1282 0.1421 -0.0028 0.0025  0.0122  38  ALA   B C   
4589 O  O   . ALA   B 38  ? 0.1576 0.1384 0.1549 0.0042  -0.0028 0.0067  38  ALA   B O   
4590 C  CB  . ALA   B 38  ? 0.1715 0.1446 0.1571 -0.0081 0.0050  0.0082  38  ALA   B CB  
4596 N  N   . ALA   B 39  ? 0.1470 0.1286 0.1287 0.0053  -0.0030 0.0039  39  ALA   B N   
4597 C  CA  . ALA   B 39  ? 0.1584 0.1344 0.1275 0.0030  -0.0093 0.0073  39  ALA   B CA  
4598 C  C   . ALA   B 39  ? 0.1655 0.1442 0.1085 0.0079  -0.0041 0.0012  39  ALA   B C   
4599 O  O   . ALA   B 39  ? 0.1632 0.1443 0.1471 -0.0027 -0.0013 0.0089  39  ALA   B O   
4600 C  CB  . ALA   B 39  ? 0.1580 0.1381 0.1504 -0.0058 -0.0044 0.0037  39  ALA   B CB  
4606 N  N   . ASN   B 40  ? 0.1655 0.1613 0.1114 -0.0015 0.0012  -0.0018 40  ASN   B N   
4607 C  CA  . ASN   B 40  ? 0.1724 0.1686 0.1322 0.0014  -0.0056 -0.0081 40  ASN   B CA  
4608 C  C   . ASN   B 40  ? 0.1706 0.1652 0.1246 0.0050  -0.0074 -0.0042 40  ASN   B C   
4609 O  O   . ASN   B 40  ? 0.1671 0.1532 0.1414 0.0064  -0.0109 -0.0010 40  ASN   B O   
4610 C  CB  . ASN   B 40  ? 0.1862 0.1666 0.1573 0.0125  -0.0093 0.0127  40  ASN   B CB  
4611 C  CG  . ASN   B 40  ? 0.1918 0.1710 0.1907 0.0084  -0.0244 0.0173  40  ASN   B CG  
4612 O  OD1 . ASN   B 40  ? 0.1886 0.1665 0.2767 0.0030  -0.0363 0.0172  40  ASN   B OD1 
4613 N  ND2 . ASN   B 40  ? 0.1947 0.1709 0.1822 0.0056  -0.0174 0.0199  40  ASN   B ND2 
4620 N  N   . VAL   B 41  ? 0.1838 0.1690 0.1255 0.0138  0.0097  -0.0072 41  VAL   B N   
4621 C  CA  . VAL   B 41  ? 0.1920 0.1814 0.1305 0.0070  0.0038  -0.0079 41  VAL   B CA  
4622 C  C   . VAL   B 41  ? 0.1888 0.1785 0.1315 0.0181  -0.0010 -0.0075 41  VAL   B C   
4623 O  O   . VAL   B 41  ? 0.1870 0.1756 0.1482 0.0154  -0.0071 -0.0125 41  VAL   B O   
4624 C  CB  . VAL   B 41  ? 0.2064 0.1994 0.1575 -0.0056 0.0274  -0.0191 41  VAL   B CB  
4625 C  CG1 . VAL   B 41  ? 0.2017 0.2025 0.1799 -0.0101 0.0358  -0.0204 41  VAL   B CG1 
4626 C  CG2 . VAL   B 41  ? 0.2194 0.2190 0.1715 -0.0167 0.0228  -0.0145 41  VAL   B CG2 
4636 N  N   . TYR   B 42  ? 0.1965 0.1789 0.1381 0.0174  -0.0182 0.0014  42  TYR   B N   
4637 C  CA  . TYR   B 42  ? 0.2000 0.1835 0.1361 0.0214  -0.0218 -0.0091 42  TYR   B CA  
4638 C  C   . TYR   B 42  ? 0.1792 0.1671 0.1455 0.0235  -0.0256 -0.0109 42  TYR   B C   
4639 O  O   . TYR   B 42  ? 0.1777 0.1796 0.1824 0.0144  -0.0248 -0.0184 42  TYR   B O   
4640 C  CB  . TYR   B 42  ? 0.2223 0.2084 0.1544 0.0141  -0.0299 0.0046  42  TYR   B CB  
4641 C  CG  . TYR   B 42  ? 0.2228 0.2265 0.1482 0.0014  -0.0302 0.0186  42  TYR   B CG  
4642 C  CD1 . TYR   B 42  ? 0.2182 0.2270 0.1284 -0.0026 -0.0085 0.0088  42  TYR   B CD1 
4643 C  CD2 . TYR   B 42  ? 0.2349 0.2418 0.1887 0.0004  -0.0181 0.0235  42  TYR   B CD2 
4644 C  CE1 . TYR   B 42  ? 0.2305 0.2462 0.1291 0.0047  -0.0098 0.0027  42  TYR   B CE1 
4645 C  CE2 . TYR   B 42  ? 0.2333 0.2546 0.1874 0.0037  0.0094  0.0346  42  TYR   B CE2 
4646 C  CZ  . TYR   B 42  ? 0.2453 0.2658 0.1639 0.0198  0.0135  0.0155  42  TYR   B CZ  
4647 O  OH  . TYR   B 42  ? 0.2769 0.2897 0.2080 0.0330  0.0196  0.0282  42  TYR   B OH  
4657 N  N   . LEU   B 43  ? 0.1691 0.1517 0.1301 0.0088  -0.0190 -0.0122 43  LEU   B N   
4658 C  CA  . LEU   B 43  ? 0.1678 0.1534 0.1286 0.0012  -0.0180 -0.0008 43  LEU   B CA  
4659 C  C   . LEU   B 43  ? 0.1719 0.1543 0.1387 0.0018  -0.0206 -0.0009 43  LEU   B C   
4660 O  O   . LEU   B 43  ? 0.1707 0.1554 0.1685 0.0079  -0.0237 0.0055  43  LEU   B O   
4661 C  CB  . LEU   B 43  ? 0.1616 0.1506 0.1483 -0.0064 -0.0262 -0.0101 43  LEU   B CB  
4662 C  CG  . LEU   B 43  ? 0.1707 0.1477 0.1577 -0.0002 -0.0262 -0.0041 43  LEU   B CG  
4663 C  CD1 . LEU   B 43  ? 0.1811 0.1529 0.1947 0.0013  -0.0400 -0.0040 43  LEU   B CD1 
4664 C  CD2 . LEU   B 43  ? 0.1683 0.1496 0.1625 -0.0121 -0.0277 -0.0018 43  LEU   B CD2 
4676 N  N   . LYS   B 44  ? 0.1722 0.1515 0.1500 0.0047  -0.0094 -0.0043 44  LYS   B N   
4677 C  CA  . LYS   B 44  ? 0.1824 0.1628 0.1518 0.0059  -0.0111 0.0069  44  LYS   B CA  
4678 C  C   . LYS   B 44  ? 0.1733 0.1542 0.1477 0.0122  -0.0158 0.0019  44  LYS   B C   
4679 O  O   . LYS   B 44  ? 0.1935 0.1567 0.1699 0.0035  -0.0096 -0.0022 44  LYS   B O   
4680 C  CB  . LYS   B 44  ? 0.2071 0.1863 0.1698 0.0153  -0.0316 0.0026  44  LYS   B CB  
4681 C  CG  . LYS   B 44  ? 0.2480 0.2167 0.2005 0.0114  -0.0606 0.0075  44  LYS   B CG  
4682 C  CD  . LYS   B 44  ? 0.2876 0.2406 0.2697 -0.0007 -0.0655 0.0014  44  LYS   B CD  
4683 C  CE  . LYS   B 44  ? 0.3184 0.2652 0.3237 -0.0052 -0.0690 0.0164  44  LYS   B CE  
4684 N  NZ  . LYS   B 44  ? 0.3259 0.2741 0.3516 -0.0044 -0.0768 0.0312  44  LYS   B NZ  
4698 N  N   . HIS   B 45  ? 0.1651 0.1615 0.1447 0.0059  -0.0133 0.0123  45  HIS   B N   
4699 C  CA  . HIS   B 45  ? 0.1663 0.1492 0.1484 0.0108  -0.0086 -0.0004 45  HIS   B CA  
4700 C  C   . HIS   B 45  ? 0.1894 0.1731 0.1890 0.0176  -0.0183 -0.0049 45  HIS   B C   
4701 O  O   . HIS   B 45  ? 0.2037 0.2035 0.2389 0.0428  0.0119  -0.0037 45  HIS   B O   
4702 C  CB  . HIS   B 45  ? 0.1556 0.1572 0.1587 -0.0010 -0.0084 -0.0064 45  HIS   B CB  
4703 C  CG  . HIS   B 45  ? 0.1616 0.1549 0.1560 -0.0060 -0.0062 -0.0015 45  HIS   B CG  
4704 N  ND1 . HIS   B 45  ? 0.1665 0.1476 0.1496 -0.0036 -0.0170 -0.0078 45  HIS   B ND1 
4705 C  CD2 . HIS   B 45  ? 0.1725 0.1568 0.1626 -0.0116 -0.0143 0.0022  45  HIS   B CD2 
4706 C  CE1 . HIS   B 45  ? 0.1754 0.1368 0.1365 -0.0055 -0.0217 -0.0099 45  HIS   B CE1 
4707 N  NE2 . HIS   B 45  ? 0.1780 0.1470 0.1572 -0.0023 -0.0210 -0.0036 45  HIS   B NE2 
4715 N  N   A GLY   B 46  ? 0.1993 0.1681 0.2173 0.0181  -0.0391 0.0035  46  GLY   B N   
4716 N  N   B GLY   B 46  ? 0.2000 0.1791 0.2073 0.0170  -0.0277 0.0024  46  GLY   B N   
4717 C  CA  A GLY   B 46  ? 0.2139 0.1852 0.2578 0.0222  -0.0407 0.0082  46  GLY   B CA  
4718 C  CA  B GLY   B 46  ? 0.2091 0.1928 0.2305 0.0173  -0.0292 0.0082  46  GLY   B CA  
4719 C  C   A GLY   B 46  ? 0.2136 0.1993 0.3000 0.0278  -0.0384 0.0070  46  GLY   B C   
4720 C  C   B GLY   B 46  ? 0.2138 0.2057 0.2589 0.0181  -0.0289 0.0120  46  GLY   B C   
4721 O  O   A GLY   B 46  ? 0.2173 0.2130 0.3846 0.0327  -0.0180 -0.0249 46  GLY   B O   
4722 O  O   B GLY   B 46  ? 0.2177 0.2137 0.2745 0.0203  -0.0281 0.0172  46  GLY   B O   
4729 N  N   . GLY   B 47  ? 0.2147 0.2133 0.2786 0.0093  -0.0186 0.0010  47  GLY   B N   
4730 C  CA  . GLY   B 47  ? 0.2056 0.1842 0.2344 0.0006  -0.0171 0.0080  47  GLY   B CA  
4731 C  C   . GLY   B 47  ? 0.1814 0.1617 0.1980 -0.0002 -0.0037 0.0067  47  GLY   B C   
4732 O  O   . GLY   B 47  ? 0.1952 0.1445 0.2086 0.0024  -0.0107 0.0089  47  GLY   B O   
4737 N  N   . GLY   B 48  ? 0.1618 0.1494 0.1985 0.0038  -0.0145 0.0189  48  GLY   B N   
4738 C  CA  . GLY   B 48  ? 0.1582 0.1439 0.1910 -0.0014 -0.0103 0.0083  48  GLY   B CA  
4739 C  C   . GLY   B 48  ? 0.1520 0.1426 0.1709 0.0025  0.0003  0.0055  48  GLY   B C   
4740 O  O   . GLY   B 48  ? 0.1474 0.1448 0.2075 0.0070  -0.0091 0.0000  48  GLY   B O   
4744 N  N   . VAL   B 49  ? 0.1531 0.1466 0.1704 0.0088  -0.0049 0.0088  49  VAL   B N   
4745 C  CA  . VAL   B 49  ? 0.1546 0.1514 0.1612 0.0097  -0.0186 -0.0062 49  VAL   B CA  
4746 C  C   . VAL   B 49  ? 0.1445 0.1440 0.1491 0.0144  -0.0096 0.0032  49  VAL   B C   
4747 O  O   . VAL   B 49  ? 0.1549 0.1475 0.1628 0.0046  -0.0045 0.0042  49  VAL   B O   
4748 C  CB  . VAL   B 49  ? 0.1552 0.1674 0.1859 -0.0004 -0.0278 -0.0074 49  VAL   B CB  
4749 C  CG1 . VAL   B 49  ? 0.1504 0.1747 0.1800 0.0086  -0.0230 -0.0048 49  VAL   B CG1 
4750 C  CG2 . VAL   B 49  ? 0.1725 0.1877 0.2164 -0.0080 -0.0423 -0.0065 49  VAL   B CG2 
4760 N  N   . ALA   B 50  ? 0.1408 0.1409 0.1514 0.0046  -0.0054 0.0025  50  ALA   B N   
4761 C  CA  . ALA   B 50  ? 0.1420 0.1341 0.1510 0.0072  -0.0094 0.0002  50  ALA   B CA  
4762 C  C   . ALA   B 50  ? 0.1528 0.1362 0.1469 0.0049  -0.0106 0.0011  50  ALA   B C   
4763 O  O   . ALA   B 50  ? 0.1512 0.1405 0.1465 0.0072  -0.0030 -0.0011 50  ALA   B O   
4764 C  CB  . ALA   B 50  ? 0.1475 0.1316 0.1541 0.0035  -0.0043 0.0063  50  ALA   B CB  
4770 N  N   . GLY   B 51  ? 0.1528 0.1484 0.1639 0.0113  -0.0155 0.0027  51  GLY   B N   
4771 C  CA  . GLY   B 51  ? 0.1518 0.1548 0.1773 0.0164  -0.0179 0.0065  51  GLY   B CA  
4772 C  C   . GLY   B 51  ? 0.1528 0.1472 0.1766 0.0183  -0.0128 0.0062  51  GLY   B C   
4773 O  O   . GLY   B 51  ? 0.1506 0.1564 0.2003 0.0086  -0.0123 -0.0001 51  GLY   B O   
4777 N  N   . ALA   B 52  ? 0.1523 0.1436 0.1653 0.0170  -0.0089 0.0057  52  ALA   B N   
4778 C  CA  . ALA   B 52  ? 0.1553 0.1499 0.1713 0.0155  -0.0016 -0.0061 52  ALA   B CA  
4779 C  C   . ALA   B 52  ? 0.1438 0.1525 0.1601 0.0078  -0.0013 -0.0076 52  ALA   B C   
4780 O  O   . ALA   B 52  ? 0.1462 0.1570 0.1796 0.0110  -0.0058 -0.0003 52  ALA   B O   
4781 C  CB  . ALA   B 52  ? 0.1712 0.1509 0.1812 0.0037  0.0015  -0.0053 52  ALA   B CB  
4787 N  N   . LEU   B 53  ? 0.1379 0.1477 0.1622 0.0149  0.0001  -0.0037 53  LEU   B N   
4788 C  CA  . LEU   B 53  ? 0.1392 0.1538 0.1525 0.0083  -0.0100 -0.0011 53  LEU   B CA  
4789 C  C   . LEU   B 53  ? 0.1468 0.1479 0.1468 0.0085  0.0005  0.0038  53  LEU   B C   
4790 O  O   . LEU   B 53  ? 0.1530 0.1541 0.1682 -0.0006 0.0008  0.0118  53  LEU   B O   
4791 C  CB  . LEU   B 53  ? 0.1392 0.1556 0.1752 0.0068  -0.0025 0.0148  53  LEU   B CB  
4792 C  CG  . LEU   B 53  ? 0.1363 0.1691 0.1758 0.0022  -0.0039 0.0211  53  LEU   B CG  
4793 C  CD1 . LEU   B 53  ? 0.1470 0.1935 0.2018 0.0114  -0.0057 0.0060  53  LEU   B CD1 
4794 C  CD2 . LEU   B 53  ? 0.1496 0.2014 0.2002 -0.0069 -0.0149 -0.0146 53  LEU   B CD2 
4806 N  N   . ASN   B 54  ? 0.1454 0.1383 0.1483 0.0071  -0.0059 0.0018  54  ASN   B N   
4807 C  CA  . ASN   B 54  ? 0.1493 0.1497 0.1577 0.0028  -0.0102 -0.0096 54  ASN   B CA  
4808 C  C   . ASN   B 54  ? 0.1471 0.1542 0.1767 0.0008  0.0031  -0.0033 54  ASN   B C   
4809 O  O   . ASN   B 54  ? 0.1413 0.1614 0.1938 -0.0052 0.0005  -0.0056 54  ASN   B O   
4810 C  CB  . ASN   B 54  ? 0.1538 0.1628 0.1658 0.0032  -0.0093 -0.0023 54  ASN   B CB  
4811 C  CG  . ASN   B 54  ? 0.1525 0.1710 0.1656 0.0019  -0.0150 0.0004  54  ASN   B CG  
4812 O  OD1 . ASN   B 54  ? 0.1456 0.1697 0.1850 0.0003  -0.0183 -0.0164 54  ASN   B OD1 
4813 N  ND2 . ASN   B 54  ? 0.1663 0.1870 0.2017 -0.0001 -0.0336 0.0111  54  ASN   B ND2 
4820 N  N   . LYS   B 55  ? 0.1445 0.1587 0.1945 0.0108  -0.0005 -0.0059 55  LYS   B N   
4821 C  CA  . LYS   B 55  ? 0.1475 0.1733 0.2069 0.0157  -0.0042 -0.0046 55  LYS   B CA  
4822 C  C   . LYS   B 55  ? 0.1462 0.1700 0.2059 0.0161  0.0053  -0.0061 55  LYS   B C   
4823 O  O   . LYS   B 55  ? 0.1417 0.1880 0.2254 0.0128  0.0082  -0.0006 55  LYS   B O   
4824 C  CB  . LYS   B 55  ? 0.1582 0.1809 0.2507 0.0267  0.0093  0.0082  55  LYS   B CB  
4825 C  CG  . LYS   B 55  ? 0.2010 0.2136 0.3277 0.0348  0.0302  0.0239  55  LYS   B CG  
4826 C  CD  . LYS   B 55  ? 0.2442 0.2369 0.3923 0.0456  0.0458  0.0382  55  LYS   B CD  
4827 C  CE  . LYS   B 55  ? 0.2717 0.2568 0.4518 0.0457  0.0591  0.0439  55  LYS   B CE  
4828 N  NZ  . LYS   B 55  ? 0.2766 0.2698 0.4831 0.0417  0.0447  0.0538  55  LYS   B NZ  
4842 N  N   . ALA   B 56  ? 0.1437 0.1738 0.1907 0.0077  0.0038  -0.0134 56  ALA   B N   
4843 C  CA  . ALA   B 56  ? 0.1569 0.1881 0.1909 0.0041  0.0088  -0.0100 56  ALA   B CA  
4844 C  C   . ALA   B 56  ? 0.1577 0.1835 0.1857 0.0040  0.0132  -0.0071 56  ALA   B C   
4845 O  O   . ALA   B 56  ? 0.1722 0.1943 0.2100 0.0042  0.0310  0.0031  56  ALA   B O   
4846 C  CB  . ALA   B 56  ? 0.1757 0.2077 0.1905 -0.0110 0.0063  -0.0125 56  ALA   B CB  
4852 N  N   . THR   B 57  ? 0.1534 0.1752 0.1946 0.0025  0.0219  -0.0016 57  THR   B N   
4853 C  CA  . THR   B 57  ? 0.1550 0.1768 0.1965 -0.0016 0.0228  0.0042  57  THR   B CA  
4854 C  C   . THR   B 57  ? 0.1532 0.1826 0.2156 0.0042  0.0234  0.0014  57  THR   B C   
4855 O  O   . THR   B 57  ? 0.1638 0.1810 0.2181 -0.0152 0.0137  0.0037  57  THR   B O   
4856 C  CB  . THR   B 57  ? 0.1633 0.1602 0.1699 -0.0006 0.0188  0.0070  57  THR   B CB  
4857 O  OG1 . THR   B 57  ? 0.1632 0.1521 0.1976 -0.0056 0.0153  0.0029  57  THR   B OG1 
4858 C  CG2 . THR   B 57  ? 0.1548 0.1626 0.1735 -0.0012 0.0166  0.0099  57  THR   B CG2 
4866 N  N   . ASN   B 58  ? 0.1403 0.2026 0.2388 -0.0134 0.0095  -0.0149 58  ASN   B N   
4867 C  CA  . ASN   B 58  ? 0.1693 0.2533 0.2786 -0.0292 0.0384  -0.0047 58  ASN   B CA  
4868 C  C   . ASN   B 58  ? 0.1498 0.2202 0.2313 -0.0191 0.0030  -0.0062 58  ASN   B C   
4869 O  O   . ASN   B 58  ? 0.1571 0.2279 0.2433 -0.0186 0.0046  -0.0126 58  ASN   B O   
4870 C  CB  . ASN   B 58  ? 0.2725 0.3486 0.3980 -0.0419 0.0746  0.0035  58  ASN   B CB  
4871 C  CG  . ASN   B 58  ? 0.3931 0.4317 0.5486 -0.0424 0.0852  0.0206  58  ASN   B CG  
4872 O  OD1 . ASN   B 58  ? 0.4242 0.4555 0.5998 -0.0431 0.0870  0.0253  58  ASN   B OD1 
4873 N  ND2 . ASN   B 58  ? 0.5162 0.5162 0.6042 -0.0441 0.0902  0.0260  58  ASN   B ND2 
4880 N  N   . ASN   B 59  ? 0.1492 0.2029 0.2090 -0.0106 -0.0039 -0.0049 59  ASN   B N   
4881 C  CA  . ASN   B 59  ? 0.1486 0.2053 0.2034 -0.0097 -0.0214 0.0005  59  ASN   B CA  
4882 C  C   . ASN   B 59  ? 0.1459 0.1966 0.2014 -0.0137 -0.0149 -0.0079 59  ASN   B C   
4883 O  O   . ASN   B 59  ? 0.1499 0.1943 0.1981 -0.0126 -0.0113 -0.0025 59  ASN   B O   
4884 C  CB  . ASN   B 59  ? 0.1631 0.2286 0.2234 -0.0056 -0.0299 0.0006  59  ASN   B CB  
4885 C  CG  . ASN   B 59  ? 0.1737 0.2442 0.2374 -0.0010 -0.0446 0.0014  59  ASN   B CG  
4886 O  OD1 . ASN   B 59  ? 0.1753 0.2471 0.2331 0.0048  -0.0247 0.0151  59  ASN   B OD1 
4887 N  ND2 . ASN   B 59  ? 0.1778 0.2523 0.2543 -0.0078 -0.0456 -0.0041 59  ASN   B ND2 
4894 N  N   . ALA   B 60  ? 0.1455 0.1842 0.1979 -0.0127 -0.0019 -0.0092 60  ALA   B N   
4895 C  CA  . ALA   B 60  ? 0.1550 0.1747 0.1972 -0.0208 -0.0020 -0.0012 60  ALA   B CA  
4896 C  C   . ALA   B 60  ? 0.1599 0.1626 0.1810 -0.0143 -0.0081 -0.0010 60  ALA   B C   
4897 O  O   . ALA   B 60  ? 0.1626 0.1638 0.1947 -0.0189 0.0010  -0.0127 60  ALA   B O   
4898 C  CB  . ALA   B 60  ? 0.1719 0.1797 0.2234 -0.0185 0.0107  0.0012  60  ALA   B CB  
4904 N  N   . MET   B 61  ? 0.1513 0.1521 0.1746 -0.0104 -0.0035 0.0055  61  MET   B N   
4905 C  CA  . MET   B 61  ? 0.1443 0.1497 0.1698 -0.0096 -0.0099 0.0034  61  MET   B CA  
4906 C  C   . MET   B 61  ? 0.1507 0.1436 0.1686 -0.0143 -0.0109 0.0104  61  MET   B C   
4907 O  O   . MET   B 61  ? 0.1505 0.1477 0.1578 -0.0045 -0.0074 -0.0112 61  MET   B O   
4908 C  CB  . MET   B 61  ? 0.1392 0.1494 0.1692 0.0057  -0.0049 -0.0067 61  MET   B CB  
4909 C  CG  . MET   B 61  ? 0.1406 0.1518 0.1622 0.0045  -0.0036 0.0000  61  MET   B CG  
4910 S  SD  . MET   B 61  ? 0.1432 0.1541 0.1824 -0.0031 -0.0059 -0.0094 61  MET   B SD  
4911 C  CE  . MET   B 61  ? 0.1535 0.1797 0.1950 -0.0020 0.0037  -0.0262 61  MET   B CE  
4921 N  N   . GLN   B 62  ? 0.1490 0.1524 0.1620 -0.0056 -0.0157 0.0028  62  GLN   B N   
4922 C  CA  . GLN   B 62  ? 0.1530 0.1576 0.1689 0.0003  -0.0170 -0.0055 62  GLN   B CA  
4923 C  C   . GLN   B 62  ? 0.1538 0.1640 0.1725 -0.0021 -0.0229 -0.0089 62  GLN   B C   
4924 O  O   . GLN   B 62  ? 0.1683 0.1655 0.1818 -0.0024 -0.0294 -0.0180 62  GLN   B O   
4925 C  CB  . GLN   B 62  ? 0.1570 0.1631 0.1664 0.0021  -0.0099 -0.0004 62  GLN   B CB  
4926 C  CG  . GLN   B 62  ? 0.1633 0.1686 0.1672 -0.0000 -0.0265 -0.0099 62  GLN   B CG  
4927 C  CD  . GLN   B 62  ? 0.1616 0.1665 0.1582 0.0048  -0.0273 0.0042  62  GLN   B CD  
4928 O  OE1 . GLN   B 62  ? 0.1631 0.1626 0.1768 0.0037  -0.0268 -0.0091 62  GLN   B OE1 
4929 N  NE2 . GLN   B 62  ? 0.1629 0.1740 0.1682 0.0056  -0.0270 -0.0076 62  GLN   B NE2 
4938 N  N   . VAL   B 63  ? 0.1509 0.1657 0.1927 -0.0070 -0.0235 -0.0143 63  VAL   B N   
4939 C  CA  . VAL   B 63  ? 0.1630 0.1698 0.2123 -0.0088 -0.0281 -0.0089 63  VAL   B CA  
4940 C  C   . VAL   B 63  ? 0.1653 0.1607 0.1889 -0.0160 -0.0330 -0.0168 63  VAL   B C   
4941 O  O   . VAL   B 63  ? 0.1741 0.1581 0.2049 -0.0116 -0.0391 -0.0122 63  VAL   B O   
4942 C  CB  . VAL   B 63  ? 0.1603 0.1869 0.2491 -0.0149 -0.0261 -0.0115 63  VAL   B CB  
4943 C  CG1 . VAL   B 63  ? 0.1695 0.1919 0.2583 -0.0246 -0.0202 -0.0114 63  VAL   B CG1 
4944 C  CG2 . VAL   B 63  ? 0.1535 0.2071 0.2621 -0.0118 -0.0353 -0.0182 63  VAL   B CG2 
4954 N  N   . GLU   B 64  ? 0.1643 0.1549 0.1801 -0.0097 -0.0236 -0.0106 64  GLU   B N   
4955 C  CA  . GLU   B 64  ? 0.1648 0.1462 0.1735 -0.0132 -0.0288 -0.0040 64  GLU   B CA  
4956 C  C   . GLU   B 64  ? 0.1546 0.1450 0.1656 -0.0070 -0.0268 -0.0150 64  GLU   B C   
4957 O  O   . GLU   B 64  ? 0.1676 0.1577 0.1682 -0.0110 -0.0244 -0.0168 64  GLU   B O   
4958 C  CB  . GLU   B 64  ? 0.1630 0.1533 0.1731 -0.0157 -0.0191 0.0007  64  GLU   B CB  
4959 C  CG  . GLU   B 64  ? 0.1664 0.1576 0.1740 -0.0248 -0.0256 -0.0123 64  GLU   B CG  
4960 C  CD  . GLU   B 64  ? 0.1732 0.1711 0.1856 -0.0318 -0.0244 -0.0040 64  GLU   B CD  
4961 O  OE1 . GLU   B 64  ? 0.1758 0.1853 0.1947 -0.0316 -0.0205 -0.0293 64  GLU   B OE1 
4962 O  OE2 . GLU   B 64  ? 0.1895 0.1808 0.1874 -0.0341 -0.0375 -0.0096 64  GLU   B OE2 
4969 N  N   . SER   B 65  ? 0.1585 0.1436 0.1595 -0.0082 -0.0169 -0.0211 65  SER   B N   
4970 C  CA  . SER   B 65  ? 0.1567 0.1427 0.1620 -0.0034 -0.0209 -0.0189 65  SER   B CA  
4971 C  C   . SER   B 65  ? 0.1564 0.1472 0.1605 -0.0029 -0.0259 -0.0213 65  SER   B C   
4972 O  O   . SER   B 65  ? 0.1630 0.1527 0.1711 -0.0017 -0.0218 -0.0223 65  SER   B O   
4973 C  CB  . SER   B 65  ? 0.1612 0.1469 0.1656 -0.0115 -0.0147 -0.0127 65  SER   B CB  
4974 O  OG  . SER   B 65  ? 0.1639 0.1477 0.1670 -0.0132 -0.0145 -0.0226 65  SER   B OG  
4980 N  N   . ASP   B 66  ? 0.1703 0.1548 0.1669 -0.0057 -0.0293 -0.0240 66  ASP   B N   
4981 C  CA  . ASP   B 66  ? 0.1751 0.1591 0.1552 -0.0006 -0.0406 -0.0175 66  ASP   B CA  
4982 C  C   . ASP   B 66  ? 0.1808 0.1616 0.1533 -0.0047 -0.0268 -0.0205 66  ASP   B C   
4983 O  O   . ASP   B 66  ? 0.1854 0.1696 0.1659 0.0040  -0.0245 -0.0252 66  ASP   B O   
4984 C  CB  . ASP   B 66  ? 0.1894 0.1734 0.1823 0.0072  -0.0451 -0.0135 66  ASP   B CB  
4985 C  CG  . ASP   B 66  ? 0.2206 0.1887 0.2115 0.0221  -0.0496 -0.0039 66  ASP   B CG  
4986 O  OD1 . ASP   B 66  ? 0.2470 0.1815 0.2109 0.0136  -0.0480 0.0030  66  ASP   B OD1 
4987 O  OD2 . ASP   B 66  ? 0.2413 0.2147 0.2705 0.0467  -0.0486 -0.0104 66  ASP   B OD2 
4992 N  N   . ASP   B 67  ? 0.1780 0.1554 0.1586 -0.0094 -0.0268 -0.0205 67  ASP   B N   
4993 C  CA  . ASP   B 67  ? 0.1922 0.1481 0.1691 -0.0075 -0.0279 -0.0151 67  ASP   B CA  
4994 C  C   . ASP   B 67  ? 0.1861 0.1492 0.1799 0.0014  -0.0287 -0.0139 67  ASP   B C   
4995 O  O   . ASP   B 67  ? 0.1890 0.1587 0.1891 0.0033  -0.0186 -0.0230 67  ASP   B O   
4996 C  CB  . ASP   B 67  ? 0.2135 0.1612 0.1893 -0.0184 -0.0390 -0.0103 67  ASP   B CB  
4997 C  CG  . ASP   B 67  ? 0.2492 0.1714 0.1908 -0.0112 -0.0678 -0.0155 67  ASP   B CG  
4998 O  OD1 . ASP   B 67  ? 0.2748 0.1806 0.2049 -0.0110 -0.0663 -0.0128 67  ASP   B OD1 
4999 O  OD2 . ASP   B 67  ? 0.2595 0.1767 0.2117 0.0036  -0.0762 -0.0103 67  ASP   B OD2 
5004 N  N   . TYR   B 68  ? 0.1796 0.1493 0.1778 0.0055  -0.0456 -0.0218 68  TYR   B N   
5005 C  CA  . TYR   B 68  ? 0.1778 0.1693 0.1838 0.0096  -0.0427 -0.0342 68  TYR   B CA  
5006 C  C   . TYR   B 68  ? 0.1680 0.1645 0.1820 0.0015  -0.0383 -0.0406 68  TYR   B C   
5007 O  O   . TYR   B 68  ? 0.1769 0.1761 0.1987 0.0074  -0.0348 -0.0532 68  TYR   B O   
5008 C  CB  . TYR   B 68  ? 0.1825 0.1912 0.1915 0.0104  -0.0446 -0.0380 68  TYR   B CB  
5009 C  CG  . TYR   B 68  ? 0.1938 0.2059 0.2064 0.0163  -0.0344 -0.0528 68  TYR   B CG  
5010 C  CD1 . TYR   B 68  ? 0.1968 0.2086 0.2361 -0.0034 -0.0352 -0.0640 68  TYR   B CD1 
5011 C  CD2 . TYR   B 68  ? 0.1973 0.2274 0.2162 0.0214  -0.0455 -0.0430 68  TYR   B CD2 
5012 C  CE1 . TYR   B 68  ? 0.2005 0.2231 0.2483 0.0007  -0.0313 -0.0664 68  TYR   B CE1 
5013 C  CE2 . TYR   B 68  ? 0.1963 0.2310 0.2226 0.0211  -0.0340 -0.0597 68  TYR   B CE2 
5014 C  CZ  . TYR   B 68  ? 0.1921 0.2290 0.2452 0.0082  -0.0334 -0.0647 68  TYR   B CZ  
5015 O  OH  . TYR   B 68  ? 0.1813 0.2466 0.2726 0.0037  -0.0254 -0.0407 68  TYR   B OH  
5025 N  N   . ILE   B 69  ? 0.1716 0.1576 0.1790 0.0064  -0.0287 -0.0328 69  ILE   B N   
5026 C  CA  . ILE   B 69  ? 0.1763 0.1624 0.1849 0.0010  -0.0195 -0.0341 69  ILE   B CA  
5027 C  C   . ILE   B 69  ? 0.1713 0.1611 0.1740 0.0093  -0.0322 -0.0287 69  ILE   B C   
5028 O  O   . ILE   B 69  ? 0.1773 0.1736 0.1718 0.0078  -0.0168 -0.0312 69  ILE   B O   
5029 C  CB  . ILE   B 69  ? 0.1839 0.1683 0.2041 -0.0004 0.0003  -0.0280 69  ILE   B CB  
5030 C  CG1 . ILE   B 69  ? 0.1859 0.1765 0.2146 -0.0058 0.0070  -0.0326 69  ILE   B CG1 
5031 C  CG2 . ILE   B 69  ? 0.1960 0.1736 0.2120 0.0011  -0.0034 -0.0206 69  ILE   B CG2 
5032 C  CD1 . ILE   B 69  ? 0.1754 0.1837 0.2235 -0.0173 0.0102  -0.0386 69  ILE   B CD1 
5044 N  N   . ALA   B 70  ? 0.1712 0.1605 0.1759 0.0070  -0.0358 -0.0263 70  ALA   B N   
5045 C  CA  . ALA   B 70  ? 0.1758 0.1634 0.1705 0.0006  -0.0371 -0.0268 70  ALA   B CA  
5046 C  C   . ALA   B 70  ? 0.1821 0.1654 0.1818 -0.0012 -0.0425 -0.0356 70  ALA   B C   
5047 O  O   . ALA   B 70  ? 0.1930 0.1627 0.1885 0.0018  -0.0353 -0.0359 70  ALA   B O   
5048 C  CB  . ALA   B 70  ? 0.1817 0.1818 0.1751 0.0033  -0.0417 -0.0278 70  ALA   B CB  
5054 N  N   . THR   B 71  ? 0.1914 0.1669 0.1907 0.0004  -0.0559 -0.0356 71  THR   B N   
5055 C  CA  . THR   B 71  ? 0.2028 0.1738 0.2145 0.0083  -0.0695 -0.0337 71  THR   B CA  
5056 C  C   . THR   B 71  ? 0.1995 0.1771 0.2420 0.0291  -0.0647 -0.0484 71  THR   B C   
5057 O  O   . THR   B 71  ? 0.2136 0.1803 0.2771 0.0296  -0.0515 -0.0621 71  THR   B O   
5058 C  CB  . THR   B 71  ? 0.2306 0.1925 0.2363 0.0021  -0.0753 -0.0152 71  THR   B CB  
5059 O  OG1 . THR   B 71  ? 0.2470 0.2193 0.2733 -0.0158 -0.0700 0.0092  71  THR   B OG1 
5060 C  CG2 . THR   B 71  ? 0.2501 0.1857 0.2574 0.0019  -0.0629 -0.0000 71  THR   B CG2 
5068 N  N   . ASN   B 72  ? 0.1834 0.1794 0.2326 0.0177  -0.0611 -0.0688 72  ASN   B N   
5069 C  CA  . ASN   B 72  ? 0.1839 0.1894 0.2350 0.0198  -0.0436 -0.0774 72  ASN   B CA  
5070 C  C   . ASN   B 72  ? 0.1850 0.1992 0.2374 0.0065  -0.0283 -0.0753 72  ASN   B C   
5071 O  O   . ASN   B 72  ? 0.1847 0.2176 0.2717 0.0112  -0.0110 -0.0721 72  ASN   B O   
5072 C  CB  . ASN   B 72  ? 0.1903 0.2059 0.2485 0.0124  -0.0612 -0.0617 72  ASN   B CB  
5073 C  CG  . ASN   B 72  ? 0.2035 0.2205 0.2573 0.0267  -0.0646 -0.0411 72  ASN   B CG  
5074 O  OD1 . ASN   B 72  ? 0.2297 0.2390 0.2631 0.0172  -0.0454 -0.0443 72  ASN   B OD1 
5075 N  ND2 . ASN   B 72  ? 0.2181 0.2309 0.2965 0.0425  -0.0495 -0.0066 72  ASN   B ND2 
5082 N  N   . GLY   B 73  ? 0.1894 0.2020 0.2157 -0.0021 -0.0365 -0.0643 73  GLY   B N   
5083 C  CA  . GLY   B 73  ? 0.1847 0.2109 0.1953 -0.0070 -0.0185 -0.0553 73  GLY   B CA  
5084 C  C   . GLY   B 73  ? 0.1748 0.2087 0.1441 -0.0016 -0.0190 -0.0465 73  GLY   B C   
5085 O  O   . GLY   B 73  ? 0.1710 0.1906 0.1650 0.0051  -0.0166 -0.0356 73  GLY   B O   
5089 N  N   . PRO   B 74  ? 0.1798 0.2197 0.1423 0.0035  -0.0326 -0.0346 74  PRO   B N   
5090 C  CA  . PRO   B 74  ? 0.1736 0.2197 0.1327 0.0098  -0.0185 -0.0235 74  PRO   B CA  
5091 C  C   . PRO   B 74  ? 0.1630 0.2029 0.1427 0.0080  -0.0133 -0.0186 74  PRO   B C   
5092 O  O   . PRO   B 74  ? 0.1676 0.2043 0.1784 0.0055  -0.0056 -0.0296 74  PRO   B O   
5093 C  CB  . PRO   B 74  ? 0.1904 0.2361 0.1396 0.0048  -0.0238 -0.0143 74  PRO   B CB  
5094 C  CG  . PRO   B 74  ? 0.2122 0.2443 0.1710 0.0041  -0.0216 -0.0092 74  PRO   B CG  
5095 C  CD  . PRO   B 74  ? 0.2089 0.2359 0.1626 0.0029  -0.0187 -0.0224 74  PRO   B CD  
5103 N  N   . LEU   B 75  ? 0.1593 0.1880 0.1387 0.0070  -0.0208 -0.0216 75  LEU   B N   
5104 C  CA  . LEU   B 75  ? 0.1662 0.1864 0.1411 0.0052  -0.0138 -0.0047 75  LEU   B CA  
5105 C  C   . LEU   B 75  ? 0.1717 0.1999 0.1457 0.0078  -0.0061 -0.0058 75  LEU   B C   
5106 O  O   . LEU   B 75  ? 0.1869 0.2075 0.1569 -0.0037 -0.0083 -0.0023 75  LEU   B O   
5107 C  CB  . LEU   B 75  ? 0.1714 0.1871 0.1291 -0.0127 -0.0249 0.0059  75  LEU   B CB  
5108 C  CG  . LEU   B 75  ? 0.2091 0.2028 0.1518 -0.0338 -0.0123 0.0028  75  LEU   B CG  
5109 C  CD1 . LEU   B 75  ? 0.2451 0.2232 0.1685 -0.0431 0.0132  0.0041  75  LEU   B CD1 
5110 C  CD2 . LEU   B 75  ? 0.2427 0.2258 0.2235 -0.0224 0.0007  0.0101  75  LEU   B CD2 
5122 N  N   . LYS   B 76  ? 0.1687 0.2182 0.1701 0.0082  0.0017  0.0042  76  LYS   B N   
5123 C  CA  . LYS   B 76  ? 0.1824 0.2276 0.2003 -0.0012 0.0264  -0.0003 76  LYS   B CA  
5124 C  C   . LYS   B 76  ? 0.1780 0.2080 0.1677 0.0004  0.0169  0.0178  76  LYS   B C   
5125 O  O   . LYS   B 76  ? 0.1807 0.1914 0.1744 -0.0026 0.0110  0.0187  76  LYS   B O   
5126 C  CB  . LYS   B 76  ? 0.1977 0.2361 0.2629 -0.0081 0.0474  -0.0282 76  LYS   B CB  
5127 C  CG  . LYS   B 76  ? 0.2110 0.2572 0.3106 0.0020  0.0315  -0.0350 76  LYS   B CG  
5128 C  CD  . LYS   B 76  ? 0.2158 0.2656 0.3484 0.0073  0.0236  -0.0543 76  LYS   B CD  
5129 C  CE  . LYS   B 76  ? 0.2231 0.2798 0.3980 0.0116  0.0110  -0.0649 76  LYS   B CE  
5130 N  NZ  . LYS   B 76  ? 0.2238 0.2848 0.4173 0.0084  -0.0065 -0.0815 76  LYS   B NZ  
5144 N  N   . VAL   B 77  ? 0.1849 0.2200 0.1712 0.0096  0.0139  0.0258  77  VAL   B N   
5145 C  CA  . VAL   B 77  ? 0.1892 0.2110 0.1830 0.0122  0.0226  0.0506  77  VAL   B CA  
5146 C  C   . VAL   B 77  ? 0.1724 0.1892 0.1764 0.0138  0.0288  0.0394  77  VAL   B C   
5147 O  O   . VAL   B 77  ? 0.1794 0.1864 0.1770 0.0212  0.0340  0.0308  77  VAL   B O   
5148 C  CB  . VAL   B 77  ? 0.2007 0.2221 0.2191 0.0137  0.0366  0.0694  77  VAL   B CB  
5149 C  CG1 . VAL   B 77  ? 0.2025 0.2132 0.2482 0.0042  0.0350  0.0747  77  VAL   B CG1 
5150 C  CG2 . VAL   B 77  ? 0.2129 0.2423 0.2444 0.0127  0.0255  0.0725  77  VAL   B CG2 
5160 N  N   . GLY   B 78  ? 0.1658 0.1738 0.1722 0.0095  0.0169  0.0344  78  GLY   B N   
5161 C  CA  . GLY   B 78  ? 0.1658 0.1679 0.1706 0.0113  0.0317  0.0197  78  GLY   B CA  
5162 C  C   . GLY   B 78  ? 0.1595 0.1628 0.1543 0.0067  0.0210  0.0205  78  GLY   B C   
5163 O  O   . GLY   B 78  ? 0.1595 0.1627 0.1755 0.0166  0.0233  0.0234  78  GLY   B O   
5167 N  N   . GLY   B 79  ? 0.1526 0.1693 0.1603 0.0071  0.0144  0.0120  79  GLY   B N   
5168 C  CA  . GLY   B 79  ? 0.1519 0.1576 0.1567 0.0121  0.0076  0.0086  79  GLY   B CA  
5169 C  C   . GLY   B 79  ? 0.1421 0.1502 0.1609 0.0120  0.0123  0.0075  79  GLY   B C   
5170 O  O   . GLY   B 79  ? 0.1510 0.1505 0.1719 0.0083  0.0206  0.0161  79  GLY   B O   
5174 N  N   . SER   B 80  ? 0.1440 0.1430 0.1634 0.0056  0.0206  0.0080  80  SER   B N   
5175 C  CA  . SER   B 80  ? 0.1359 0.1453 0.1538 0.0039  0.0056  0.0093  80  SER   B CA  
5176 C  C   . SER   B 80  ? 0.1431 0.1393 0.1518 0.0088  -0.0022 -0.0005 80  SER   B C   
5177 O  O   . SER   B 80  ? 0.1586 0.1406 0.1925 0.0091  0.0080  -0.0046 80  SER   B O   
5178 C  CB  . SER   B 80  ? 0.1438 0.1477 0.1639 -0.0016 0.0004  0.0094  80  SER   B CB  
5179 O  OG  . SER   B 80  ? 0.1544 0.1595 0.1828 -0.0052 -0.0118 0.0138  80  SER   B OG  
5185 N  N   . CYS   B 81  ? 0.1420 0.1301 0.1653 0.0013  -0.0015 -0.0060 81  CYS   B N   
5186 C  CA  . CYS   B 81  ? 0.1436 0.1275 0.1647 0.0036  -0.0109 -0.0104 81  CYS   B CA  
5187 C  C   . CYS   B 81  ? 0.1453 0.1242 0.1362 0.0008  -0.0117 0.0002  81  CYS   B C   
5188 O  O   . CYS   B 81  ? 0.1645 0.1264 0.1615 0.0058  -0.0013 -0.0050 81  CYS   B O   
5189 C  CB  . CYS   B 81  ? 0.1572 0.1410 0.1650 -0.0011 -0.0120 -0.0037 81  CYS   B CB  
5190 S  SG  . CYS   B 81  ? 0.1614 0.1587 0.1626 -0.0043 -0.0250 -0.0097 81  CYS   B SG  
5196 N  N   . VAL   B 82  ? 0.1434 0.1244 0.1590 -0.0010 -0.0110 -0.0048 82  VAL   B N   
5197 C  CA  . VAL   B 82  ? 0.1497 0.1292 0.1545 -0.0043 -0.0108 0.0040  82  VAL   B CA  
5198 C  C   . VAL   B 82  ? 0.1589 0.1240 0.1623 -0.0033 -0.0116 -0.0009 82  VAL   B C   
5199 O  O   . VAL   B 82  ? 0.1654 0.1279 0.1922 -0.0049 -0.0094 -0.0160 82  VAL   B O   
5200 C  CB  . VAL   B 82  ? 0.1559 0.1523 0.1747 -0.0018 -0.0123 0.0087  82  VAL   B CB  
5201 C  CG1 . VAL   B 82  ? 0.1758 0.1682 0.1830 0.0021  -0.0138 0.0209  82  VAL   B CG1 
5202 C  CG2 . VAL   B 82  ? 0.1610 0.1668 0.1786 -0.0068 -0.0270 0.0084  82  VAL   B CG2 
5212 N  N   . LEU   B 83  ? 0.1465 0.1250 0.1548 -0.0150 -0.0185 -0.0101 83  LEU   B N   
5213 C  CA  . LEU   B 83  ? 0.1497 0.1320 0.1441 -0.0160 -0.0191 -0.0058 83  LEU   B CA  
5214 C  C   . LEU   B 83  ? 0.1512 0.1289 0.1407 -0.0184 -0.0230 0.0015  83  LEU   B C   
5215 O  O   . LEU   B 83  ? 0.1535 0.1358 0.1386 -0.0224 -0.0170 0.0039  83  LEU   B O   
5216 C  CB  . LEU   B 83  ? 0.1585 0.1456 0.1519 -0.0151 -0.0233 -0.0093 83  LEU   B CB  
5217 C  CG  . LEU   B 83  ? 0.1733 0.1683 0.1569 -0.0192 -0.0119 -0.0056 83  LEU   B CG  
5218 C  CD1 . LEU   B 83  ? 0.1901 0.1758 0.1620 -0.0201 -0.0150 0.0022  83  LEU   B CD1 
5219 C  CD2 . LEU   B 83  ? 0.1907 0.1699 0.1711 -0.0100 -0.0070 -0.0272 83  LEU   B CD2 
5231 N  N   . SER   B 84  ? 0.1573 0.1371 0.1696 -0.0211 -0.0219 -0.0006 84  SER   B N   
5232 C  CA  . SER   B 84  ? 0.1575 0.1565 0.1557 -0.0243 -0.0184 0.0146  84  SER   B CA  
5233 C  C   . SER   B 84  ? 0.1460 0.1754 0.1183 -0.0193 -0.0145 0.0184  84  SER   B C   
5234 O  O   . SER   B 84  ? 0.1520 0.1608 0.1242 -0.0165 -0.0083 -0.0007 84  SER   B O   
5235 C  CB  . SER   B 84  ? 0.1770 0.1601 0.2051 -0.0318 0.0054  0.0134  84  SER   B CB  
5236 O  OG  . SER   B 84  ? 0.1764 0.1804 0.2481 -0.0378 0.0023  0.0256  84  SER   B OG  
5242 N  N   . GLY   B 85  ? 0.1468 0.1962 0.1413 -0.0294 -0.0143 0.0208  85  GLY   B N   
5243 C  CA  . GLY   B 85  ? 0.1516 0.2054 0.1571 -0.0386 -0.0022 -0.0063 85  GLY   B CA  
5244 C  C   . GLY   B 85  ? 0.1491 0.1856 0.1435 -0.0411 0.0002  0.0055  85  GLY   B C   
5245 O  O   . GLY   B 85  ? 0.1599 0.1828 0.1541 -0.0484 0.0165  -0.0078 85  GLY   B O   
5249 N  N   . HIS   B 86  ? 0.1484 0.1713 0.1650 -0.0317 -0.0179 0.0157  86  HIS   B N   
5250 C  CA  . HIS   B 86  ? 0.1499 0.1676 0.1645 -0.0304 -0.0219 0.0147  86  HIS   B CA  
5251 C  C   . HIS   B 86  ? 0.1497 0.1780 0.1492 -0.0442 -0.0154 0.0302  86  HIS   B C   
5252 O  O   . HIS   B 86  ? 0.1646 0.1915 0.1632 -0.0341 0.0065  0.0284  86  HIS   B O   
5253 C  CB  . HIS   B 86  ? 0.1579 0.1709 0.1649 -0.0219 -0.0243 0.0042  86  HIS   B CB  
5254 C  CG  . HIS   B 86  ? 0.1600 0.1801 0.1649 -0.0126 -0.0210 0.0096  86  HIS   B CG  
5255 N  ND1 . HIS   B 86  ? 0.1734 0.2016 0.1836 -0.0236 -0.0264 -0.0080 86  HIS   B ND1 
5256 C  CD2 . HIS   B 86  ? 0.1615 0.1787 0.1714 -0.0129 -0.0237 0.0086  86  HIS   B CD2 
5257 C  CE1 . HIS   B 86  ? 0.1795 0.1990 0.1752 -0.0195 -0.0144 -0.0201 86  HIS   B CE1 
5258 N  NE2 . HIS   B 86  ? 0.1738 0.1884 0.1642 -0.0048 -0.0152 -0.0038 86  HIS   B NE2 
5266 N  N   . ASN   B 87  ? 0.1518 0.1823 0.1597 -0.0344 -0.0020 0.0229  87  ASN   B N   
5267 C  CA  . ASN   B 87  ? 0.1635 0.1993 0.1698 -0.0295 0.0222  0.0226  87  ASN   B CA  
5268 C  C   . ASN   B 87  ? 0.1736 0.1857 0.1602 -0.0288 0.0341  0.0166  87  ASN   B C   
5269 O  O   . ASN   B 87  ? 0.1984 0.1933 0.1953 -0.0206 0.0468  0.0066  87  ASN   B O   
5270 C  CB  . ASN   B 87  ? 0.1616 0.2380 0.2079 -0.0218 0.0262  0.0119  87  ASN   B CB  
5271 C  CG  . ASN   B 87  ? 0.1675 0.2561 0.2111 0.0120  0.0265  0.0273  87  ASN   B CG  
5272 O  OD1 . ASN   B 87  ? 0.1620 0.2443 0.1972 0.0106  0.0461  0.0407  87  ASN   B OD1 
5273 N  ND2 . ASN   B 87  ? 0.2022 0.2660 0.2528 0.0127  0.0350  0.0266  87  ASN   B ND2 
5280 N  N   . LEU   B 88  ? 0.1618 0.1711 0.1430 -0.0312 0.0072  0.0118  88  LEU   B N   
5281 C  CA  . LEU   B 88  ? 0.1753 0.1643 0.1462 -0.0331 -0.0029 -0.0028 88  LEU   B CA  
5282 C  C   . LEU   B 88  ? 0.1776 0.1620 0.1466 -0.0398 -0.0032 -0.0020 88  LEU   B C   
5283 O  O   . LEU   B 88  ? 0.2008 0.1727 0.1799 -0.0249 -0.0271 -0.0041 88  LEU   B O   
5284 C  CB  . LEU   B 88  ? 0.1865 0.1673 0.1651 -0.0422 -0.0086 0.0129  88  LEU   B CB  
5285 C  CG  . LEU   B 88  ? 0.2236 0.2003 0.1829 -0.0355 -0.0267 0.0287  88  LEU   B CG  
5286 C  CD1 . LEU   B 88  ? 0.2382 0.2324 0.1979 -0.0423 -0.0242 0.0524  88  LEU   B CD1 
5287 C  CD2 . LEU   B 88  ? 0.2589 0.2264 0.2387 0.0035  -0.0515 0.0007  88  LEU   B CD2 
5299 N  N   . ALA   B 89  ? 0.1592 0.1559 0.1418 -0.0350 0.0122  -0.0034 89  ALA   B N   
5300 C  CA  . ALA   B 89  ? 0.1568 0.1530 0.1266 -0.0372 0.0071  0.0099  89  ALA   B CA  
5301 C  C   . ALA   B 89  ? 0.1659 0.1557 0.1332 -0.0398 0.0124  0.0055  89  ALA   B C   
5302 O  O   . ALA   B 89  ? 0.1497 0.1649 0.1771 -0.0398 0.0133  -0.0286 89  ALA   B O   
5303 C  CB  . ALA   B 89  ? 0.1510 0.1482 0.1418 -0.0327 0.0029  0.0198  89  ALA   B CB  
5309 N  N   . LYS   B 90  ? 0.2015 0.1451 0.1443 -0.0438 -0.0076 0.0070  90  LYS   B N   
5310 C  CA  . LYS   B 90  ? 0.2158 0.1417 0.1365 -0.0400 -0.0110 0.0091  90  LYS   B CA  
5311 C  C   . LYS   B 90  ? 0.1975 0.1319 0.1466 -0.0409 -0.0148 -0.0018 90  LYS   B C   
5312 O  O   . LYS   B 90  ? 0.2068 0.1499 0.1662 -0.0564 -0.0044 0.0030  90  LYS   B O   
5313 C  CB  . LYS   B 90  ? 0.2349 0.1534 0.1676 -0.0389 -0.0061 0.0204  90  LYS   B CB  
5314 C  CG  . LYS   B 90  ? 0.2388 0.1602 0.1768 -0.0218 0.0237  0.0151  90  LYS   B CG  
5315 C  CD  . LYS   B 90  ? 0.2666 0.1837 0.2300 -0.0122 0.0390  0.0016  90  LYS   B CD  
5316 C  CE  . LYS   B 90  ? 0.2775 0.1969 0.2739 -0.0218 0.0517  -0.0127 90  LYS   B CE  
5317 N  NZ  . LYS   B 90  ? 0.2836 0.1880 0.2606 -0.0330 0.0709  -0.0169 90  LYS   B NZ  
5331 N  N   . HIS   B 91  ? 0.1637 0.1250 0.1352 -0.0303 -0.0102 0.0064  91  HIS   B N   
5332 C  CA  . HIS   B 91  ? 0.1552 0.1280 0.1483 -0.0206 -0.0102 0.0021  91  HIS   B CA  
5333 C  C   . HIS   B 91  ? 0.1443 0.1316 0.1275 -0.0258 -0.0075 0.0029  91  HIS   B C   
5334 O  O   . HIS   B 91  ? 0.1615 0.1358 0.1259 -0.0279 -0.0209 0.0036  91  HIS   B O   
5335 C  CB  . HIS   B 91  ? 0.1766 0.1304 0.1845 -0.0092 -0.0089 0.0149  91  HIS   B CB  
5336 C  CG  . HIS   B 91  ? 0.2188 0.1477 0.2489 0.0026  0.0195  0.0201  91  HIS   B CG  
5337 N  ND1 . HIS   B 91  ? 0.2454 0.1549 0.3113 0.0023  0.0267  0.0107  91  HIS   B ND1 
5338 C  CD2 . HIS   B 91  ? 0.2296 0.1800 0.3000 0.0179  0.0091  0.0538  91  HIS   B CD2 
5339 C  CE1 . HIS   B 91  ? 0.2471 0.1688 0.3334 0.0185  0.0286  0.0157  91  HIS   B CE1 
5340 N  NE2 . HIS   B 91  ? 0.2405 0.1850 0.3320 0.0318  0.0238  0.0586  91  HIS   B NE2 
5348 N  N   . CYS   B 92  ? 0.1431 0.1312 0.1282 -0.0269 -0.0162 -0.0019 92  CYS   B N   
5349 C  CA  . CYS   B 92  ? 0.1420 0.1300 0.1281 -0.0223 -0.0072 0.0006  92  CYS   B CA  
5350 C  C   . CYS   B 92  ? 0.1373 0.1235 0.1226 -0.0130 -0.0055 0.0007  92  CYS   B C   
5351 O  O   . CYS   B 92  ? 0.1447 0.1336 0.1413 -0.0158 -0.0021 0.0011  92  CYS   B O   
5352 C  CB  . CYS   B 92  ? 0.1440 0.1390 0.1344 -0.0153 -0.0054 0.0039  92  CYS   B CB  
5353 S  SG  . CYS   B 92  ? 0.1422 0.1365 0.1404 -0.0097 -0.0104 0.0048  92  CYS   B SG  
5359 N  N   . LEU   B 93  ? 0.1290 0.1244 0.1342 -0.0145 -0.0081 -0.0028 93  LEU   B N   
5360 C  CA  . LEU   B 93  ? 0.1321 0.1260 0.1350 -0.0047 -0.0150 0.0071  93  LEU   B CA  
5361 C  C   . LEU   B 93  ? 0.1237 0.1223 0.1262 -0.0065 -0.0065 0.0042  93  LEU   B C   
5362 O  O   . LEU   B 93  ? 0.1358 0.1231 0.1389 -0.0055 -0.0072 0.0036  93  LEU   B O   
5363 C  CB  . LEU   B 93  ? 0.1362 0.1247 0.1508 0.0015  -0.0097 0.0073  93  LEU   B CB  
5364 C  CG  . LEU   B 93  ? 0.1329 0.1384 0.1647 -0.0030 -0.0028 0.0134  93  LEU   B CG  
5365 C  CD1 . LEU   B 93  ? 0.1426 0.1494 0.1599 0.0059  0.0017  0.0033  93  LEU   B CD1 
5366 C  CD2 . LEU   B 93  ? 0.1307 0.1408 0.1790 -0.0018 -0.0143 0.0056  93  LEU   B CD2 
5378 N  N   . HIS   B 94  ? 0.1348 0.1195 0.1197 -0.0076 -0.0083 0.0028  94  HIS   B N   
5379 C  CA  . HIS   B 94  ? 0.1346 0.1208 0.1248 -0.0017 -0.0070 0.0068  94  HIS   B CA  
5380 C  C   . HIS   B 94  ? 0.1293 0.1229 0.1498 -0.0051 -0.0085 0.0083  94  HIS   B C   
5381 O  O   . HIS   B 94  ? 0.1334 0.1331 0.1846 -0.0074 0.0139  -0.0044 94  HIS   B O   
5382 C  CB  . HIS   B 94  ? 0.1326 0.1327 0.1344 -0.0007 -0.0105 0.0005  94  HIS   B CB  
5383 C  CG  . HIS   B 94  ? 0.1396 0.1242 0.1386 -0.0058 -0.0180 0.0015  94  HIS   B CG  
5384 N  ND1 . HIS   B 94  ? 0.1431 0.1332 0.1374 -0.0056 -0.0188 0.0017  94  HIS   B ND1 
5385 C  CD2 . HIS   B 94  ? 0.1415 0.1312 0.1346 -0.0012 -0.0130 0.0082  94  HIS   B CD2 
5386 C  CE1 . HIS   B 94  ? 0.1488 0.1325 0.1391 -0.0115 -0.0199 0.0051  94  HIS   B CE1 
5387 N  NE2 . HIS   B 94  ? 0.1378 0.1344 0.1479 -0.0149 -0.0185 0.0023  94  HIS   B NE2 
5395 N  N   . VAL   B 95  ? 0.1252 0.1260 0.1488 -0.0037 0.0005  0.0044  95  VAL   B N   
5396 C  CA  . VAL   B 95  ? 0.1290 0.1312 0.1376 -0.0020 0.0009  0.0174  95  VAL   B CA  
5397 C  C   . VAL   B 95  ? 0.1390 0.1365 0.1336 -0.0027 0.0121  0.0087  95  VAL   B C   
5398 O  O   . VAL   B 95  ? 0.1404 0.1329 0.1611 0.0062  0.0069  0.0137  95  VAL   B O   
5399 C  CB  . VAL   B 95  ? 0.1354 0.1290 0.1465 -0.0061 -0.0049 0.0091  95  VAL   B CB  
5400 C  CG1 . VAL   B 95  ? 0.1444 0.1450 0.1677 -0.0090 0.0016  0.0165  95  VAL   B CG1 
5401 C  CG2 . VAL   B 95  ? 0.1395 0.1284 0.1479 0.0012  -0.0087 0.0043  95  VAL   B CG2 
5411 N  N   . VAL   B 96  ? 0.1515 0.1313 0.1440 0.0094  0.0140  0.0185  96  VAL   B N   
5412 C  CA  . VAL   B 96  ? 0.1546 0.1451 0.1375 0.0095  0.0127  0.0176  96  VAL   B CA  
5413 C  C   . VAL   B 96  ? 0.1578 0.1485 0.1586 0.0062  0.0166  0.0186  96  VAL   B C   
5414 O  O   . VAL   B 96  ? 0.1576 0.1530 0.1752 0.0025  0.0184  0.0060  96  VAL   B O   
5415 C  CB  . VAL   B 96  ? 0.1627 0.1678 0.1393 0.0104  0.0106  0.0112  96  VAL   B CB  
5416 C  CG1 . VAL   B 96  ? 0.1608 0.1890 0.1573 0.0179  0.0100  0.0119  96  VAL   B CG1 
5417 C  CG2 . VAL   B 96  ? 0.1684 0.1763 0.1584 0.0031  0.0113  0.0039  96  VAL   B CG2 
5427 N  N   . GLY   B 97  ? 0.1611 0.1510 0.1441 0.0027  0.0131  0.0189  97  GLY   B N   
5428 C  CA  . GLY   B 97  ? 0.1781 0.1549 0.1502 0.0019  0.0142  0.0203  97  GLY   B CA  
5429 C  C   . GLY   B 97  ? 0.2002 0.1622 0.1631 0.0100  0.0122  0.0191  97  GLY   B C   
5430 O  O   . GLY   B 97  ? 0.2142 0.1701 0.1623 0.0051  0.0050  0.0085  97  GLY   B O   
5434 N  N   . PRO   B 98  ? 0.2139 0.1669 0.1797 0.0097  0.0449  0.0378  98  PRO   B N   
5435 C  CA  . PRO   B 98  ? 0.2293 0.1872 0.1822 0.0215  0.0557  0.0340  98  PRO   B CA  
5436 C  C   . PRO   B 98  ? 0.2449 0.1867 0.1528 0.0395  0.0530  0.0552  98  PRO   B C   
5437 O  O   . PRO   B 98  ? 0.2343 0.1838 0.1768 0.0268  0.0520  0.0478  98  PRO   B O   
5438 C  CB  . PRO   B 98  ? 0.2187 0.1951 0.2043 0.0170  0.0648  0.0416  98  PRO   B CB  
5439 C  CG  . PRO   B 98  ? 0.2134 0.1872 0.2081 0.0104  0.0563  0.0522  98  PRO   B CG  
5440 C  CD  . PRO   B 98  ? 0.2000 0.1743 0.1992 0.0139  0.0515  0.0491  98  PRO   B CD  
5448 N  N   . ASN   B 99  ? 0.2594 0.2072 0.1651 0.0545  0.0515  0.0378  99  ASN   B N   
5449 C  CA  . ASN   B 99  ? 0.2785 0.2182 0.1794 0.0639  0.0490  0.0585  99  ASN   B CA  
5450 C  C   . ASN   B 99  ? 0.3068 0.2556 0.2146 0.0626  0.0716  0.0882  99  ASN   B C   
5451 O  O   . ASN   B 99  ? 0.3184 0.2638 0.2221 0.0627  0.0663  0.0862  99  ASN   B O   
5452 C  CB  . ASN   B 99  ? 0.2871 0.2116 0.1909 0.0625  0.0344  0.0502  99  ASN   B CB  
5453 C  CG  . ASN   B 99  ? 0.2903 0.2191 0.2129 0.0538  0.0242  0.0388  99  ASN   B CG  
5454 O  OD1 . ASN   B 99  ? 0.2900 0.2169 0.2418 0.0582  0.0306  0.0486  99  ASN   B OD1 
5455 N  ND2 . ASN   B 99  ? 0.2884 0.2181 0.2125 0.0558  -0.0029 0.0314  99  ASN   B ND2 
5462 N  N   A VAL   B 100 ? 0.3233 0.2668 0.2625 0.0489  0.0793  0.1140  100 VAL   B N   
5463 N  N   B VAL   B 100 ? 0.3290 0.2705 0.2609 0.0536  0.0620  0.0990  100 VAL   B N   
5464 C  CA  A VAL   B 100 ? 0.3498 0.2846 0.3177 0.0363  0.0738  0.1280  100 VAL   B CA  
5465 C  CA  B VAL   B 100 ? 0.3542 0.2868 0.3051 0.0443  0.0493  0.1053  100 VAL   B CA  
5466 C  C   A VAL   B 100 ? 0.3738 0.2906 0.3072 0.0423  0.0661  0.1422  100 VAL   B C   
5467 C  C   B VAL   B 100 ? 0.3747 0.2926 0.3068 0.0470  0.0463  0.1254  100 VAL   B C   
5468 O  O   A VAL   B 100 ? 0.3837 0.3054 0.3129 0.0372  0.0756  0.1337  100 VAL   B O   
5469 O  O   B VAL   B 100 ? 0.3795 0.3006 0.3097 0.0437  0.0475  0.1205  100 VAL   B O   
5470 C  CB  A VAL   B 100 ? 0.3564 0.2994 0.3837 0.0131  0.0701  0.1349  100 VAL   B CB  
5471 C  CB  B VAL   B 100 ? 0.3595 0.2979 0.3453 0.0313  0.0402  0.0958  100 VAL   B CB  
5472 C  CG1 A VAL   B 100 ? 0.3606 0.3048 0.4079 0.0099  0.0685  0.1346  100 VAL   B CG1 
5473 C  CG1 B VAL   B 100 ? 0.3621 0.3020 0.3588 0.0290  0.0375  0.0930  100 VAL   B CG1 
5474 C  CG2 A VAL   B 100 ? 0.3560 0.3041 0.3958 0.0033  0.0753  0.1450  100 VAL   B CG2 
5475 C  CG2 B VAL   B 100 ? 0.3605 0.3017 0.3569 0.0267  0.0385  0.0942  100 VAL   B CG2 
5494 N  N   . ASN   B 101 ? 0.3906 0.2944 0.3081 0.0532  0.0435  0.1430  101 ASN   B N   
5495 C  CA  . ASN   B 101 ? 0.4318 0.3118 0.3221 0.0616  0.0222  0.1490  101 ASN   B CA  
5496 C  C   . ASN   B 101 ? 0.4756 0.3546 0.3257 0.0629  0.0105  0.1586  101 ASN   B C   
5497 O  O   . ASN   B 101 ? 0.4781 0.3665 0.3471 0.0695  0.0142  0.1283  101 ASN   B O   
5498 C  CB  . ASN   B 101 ? 0.4295 0.2926 0.3332 0.0593  0.0220  0.1292  101 ASN   B CB  
5499 C  CG  . ASN   B 101 ? 0.4253 0.2709 0.3329 0.0571  0.0246  0.1298  101 ASN   B CG  
5500 O  OD1 . ASN   B 101 ? 0.4274 0.2713 0.3591 0.0441  0.0458  0.1190  101 ASN   B OD1 
5501 N  ND2 . ASN   B 101 ? 0.4218 0.2664 0.3312 0.0602  0.0199  0.1145  101 ASN   B ND2 
5509 N  N   . LYS   B 102 ? 0.5142 0.3958 0.3565 0.0506  0.0124  0.1525  102 LYS   B N   
5510 C  CA  . LYS   B 102 ? 0.5503 0.4430 0.3971 0.0351  0.0192  0.1264  102 LYS   B CA  
5511 C  C   . LYS   B 102 ? 0.5447 0.4421 0.3769 0.0327  0.0275  0.1342  102 LYS   B C   
5512 O  O   . LYS   B 102 ? 0.5541 0.4458 0.3816 0.0333  0.0144  0.1359  102 LYS   B O   
5513 C  CB  . LYS   B 102 ? 0.5862 0.4889 0.4661 0.0243  0.0267  0.0808  102 LYS   B CB  
5514 C  CG  . LYS   B 102 ? 0.6151 0.5328 0.5374 0.0154  0.0337  0.0381  102 LYS   B CG  
5515 C  CD  . LYS   B 102 ? 0.6403 0.5672 0.6064 0.0088  0.0413  0.0038  102 LYS   B CD  
5516 C  CE  . LYS   B 102 ? 0.6588 0.5883 0.6610 0.0032  0.0467  -0.0200 102 LYS   B CE  
5517 N  NZ  . LYS   B 102 ? 0.6674 0.6042 0.6928 -0.0000 0.0484  -0.0330 102 LYS   B NZ  
5531 N  N   . GLY   B 103 ? 0.5248 0.4330 0.3720 0.0291  0.0488  0.1278  103 GLY   B N   
5532 C  CA  . GLY   B 103 ? 0.5021 0.4224 0.3805 0.0281  0.0672  0.1069  103 GLY   B CA  
5533 C  C   . GLY   B 103 ? 0.4756 0.4071 0.3736 0.0246  0.0829  0.0862  103 GLY   B C   
5534 O  O   . GLY   B 103 ? 0.4814 0.4135 0.3829 0.0232  0.0864  0.0878  103 GLY   B O   
5538 N  N   A GLU   B 104 ? 0.4578 0.3910 0.3531 0.0269  0.1028  0.0739  104 GLU   B N   
5539 N  N   B GLU   B 104 ? 0.4590 0.3992 0.3704 0.0205  0.0713  0.0674  104 GLU   B N   
5540 C  CA  A GLU   B 104 ? 0.4380 0.3745 0.3321 0.0341  0.1149  0.0572  104 GLU   B CA  
5541 C  CA  B GLU   B 104 ? 0.4409 0.3900 0.3631 0.0175  0.0589  0.0457  104 GLU   B CA  
5542 C  C   A GLU   B 104 ? 0.4410 0.3786 0.3407 0.0164  0.1527  0.0639  104 GLU   B C   
5543 C  C   B GLU   B 104 ? 0.4355 0.3899 0.3739 0.0110  0.0655  0.0386  104 GLU   B C   
5544 O  O   A GLU   B 104 ? 0.4413 0.3821 0.3592 0.0124  0.1551  0.0640  104 GLU   B O   
5545 O  O   B GLU   B 104 ? 0.4356 0.3904 0.3802 0.0100  0.0662  0.0374  104 GLU   B O   
5546 C  CB  A GLU   B 104 ? 0.4203 0.3526 0.3186 0.0582  0.0775  0.0269  104 GLU   B CB  
5547 C  CB  B GLU   B 104 ? 0.4298 0.3801 0.3470 0.0204  0.0390  0.0285  104 GLU   B CB  
5548 C  CG  A GLU   B 104 ? 0.4053 0.3352 0.3010 0.0800  0.0361  -0.0069 104 GLU   B CG  
5549 C  CG  B GLU   B 104 ? 0.4206 0.3720 0.3317 0.0226  0.0188  0.0100  104 GLU   B CG  
5550 C  CD  A GLU   B 104 ? 0.3907 0.3182 0.2728 0.0993  0.0033  -0.0271 104 GLU   B CD  
5551 C  CD  B GLU   B 104 ? 0.4132 0.3646 0.3165 0.0234  0.0028  -0.0030 104 GLU   B CD  
5552 O  OE1 A GLU   B 104 ? 0.3745 0.2997 0.2324 0.1179  0.0054  -0.0333 104 GLU   B OE1 
5553 O  OE1 B GLU   B 104 ? 0.4092 0.3601 0.3045 0.0229  0.0013  -0.0055 104 GLU   B OE1 
5554 O  OE2 A GLU   B 104 ? 0.3914 0.3233 0.2755 0.0959  -0.0227 -0.0378 104 GLU   B OE2 
5555 O  OE2 B GLU   B 104 ? 0.4115 0.3636 0.3144 0.0238  -0.0077 -0.0103 104 GLU   B OE2 
5568 N  N   A ASP   B 105 ? 0.4383 0.3793 0.3334 0.0052  0.1837  0.0687  105 ASP   B N   
5569 N  N   B ASP   B 105 ? 0.4287 0.3887 0.3764 0.0059  0.0706  0.0326  105 ASP   B N   
5570 C  CA  A ASP   B 105 ? 0.4395 0.3803 0.3538 -0.0030 0.2008  0.0545  105 ASP   B CA  
5571 C  CA  B ASP   B 105 ? 0.4230 0.3866 0.3851 0.0015  0.0729  0.0226  105 ASP   B CA  
5572 C  C   A ASP   B 105 ? 0.4194 0.3504 0.3261 -0.0156 0.2078  0.0530  105 ASP   B C   
5573 C  C   B ASP   B 105 ? 0.4122 0.3761 0.3663 -0.0026 0.0745  0.0163  105 ASP   B C   
5574 O  O   A ASP   B 105 ? 0.4044 0.3440 0.3177 -0.0152 0.2013  0.0531  105 ASP   B O   
5575 O  O   B ASP   B 105 ? 0.4116 0.3752 0.3590 -0.0025 0.0772  0.0165  105 ASP   B O   
5576 C  CB  A ASP   B 105 ? 0.4564 0.4061 0.4231 0.0057  0.1972  0.0316  105 ASP   B CB  
5577 C  CB  B ASP   B 105 ? 0.4260 0.3936 0.4139 0.0027  0.0732  0.0178  105 ASP   B CB  
5578 C  CG  A ASP   B 105 ? 0.4669 0.4246 0.4851 0.0107  0.1997  0.0169  105 ASP   B CG  
5579 C  CG  B ASP   B 105 ? 0.4276 0.3978 0.4404 0.0027  0.0746  0.0156  105 ASP   B CG  
5580 O  OD1 A ASP   B 105 ? 0.4647 0.4285 0.4893 0.0050  0.2156  0.0225  105 ASP   B OD1 
5581 O  OD1 B ASP   B 105 ? 0.4269 0.3989 0.4464 0.0007  0.0764  0.0167  105 ASP   B OD1 
5582 O  OD2 A ASP   B 105 ? 0.4728 0.4344 0.5225 0.0189  0.1876  0.0028  105 ASP   B OD2 
5583 O  OD2 B ASP   B 105 ? 0.4274 0.3996 0.4508 0.0032  0.0751  0.0145  105 ASP   B OD2 
5592 N  N   A ILE   B 106 ? 0.4102 0.3244 0.3330 -0.0245 0.1979  0.0509  106 ILE   B N   
5593 N  N   B ILE   B 106 ? 0.4011 0.3656 0.3562 -0.0050 0.0711  0.0118  106 ILE   B N   
5594 C  CA  A ILE   B 106 ? 0.3879 0.2951 0.3446 -0.0391 0.1979  0.0412  106 ILE   B CA  
5595 C  CA  B ILE   B 106 ? 0.3879 0.3553 0.3511 -0.0079 0.0703  0.0064  106 ILE   B CA  
5596 C  C   A ILE   B 106 ? 0.3552 0.2846 0.3358 -0.0323 0.1989  0.0226  106 ILE   B C   
5597 C  C   B ILE   B 106 ? 0.3706 0.3484 0.3470 -0.0065 0.0713  0.0004  106 ILE   B C   
5598 O  O   A ILE   B 106 ? 0.3451 0.2609 0.3424 -0.0355 0.1965  0.0194  106 ILE   B O   
5599 O  O   B ILE   B 106 ? 0.3692 0.3444 0.3450 -0.0081 0.0674  -0.0032 106 ILE   B O   
5600 C  CB  A ILE   B 106 ? 0.4019 0.2847 0.3623 -0.0528 0.1882  0.0478  106 ILE   B CB  
5601 C  CB  B ILE   B 106 ? 0.3921 0.3543 0.3512 -0.0114 0.0680  0.0068  106 ILE   B CB  
5602 C  CG1 A ILE   B 106 ? 0.4071 0.2864 0.3679 -0.0452 0.1775  0.0375  106 ILE   B CG1 
5603 C  CG1 B ILE   B 106 ? 0.3932 0.3536 0.3505 -0.0104 0.0648  0.0065  106 ILE   B CG1 
5604 C  CG2 A ILE   B 106 ? 0.4082 0.2851 0.3853 -0.0621 0.1835  0.0532  106 ILE   B CG2 
5605 C  CG2 B ILE   B 106 ? 0.3945 0.3562 0.3564 -0.0135 0.0680  0.0068  106 ILE   B CG2 
5606 C  CD1 A ILE   B 106 ? 0.4098 0.2881 0.3583 -0.0387 0.1752  0.0358  106 ILE   B CD1 
5607 C  CD1 B ILE   B 106 ? 0.3939 0.3529 0.3492 -0.0092 0.0631  0.0064  106 ILE   B CD1 
5630 N  N   A GLN   B 107 ? 0.3383 0.3019 0.3438 -0.0282 0.1877  0.0183  107 GLN   B N   
5631 N  N   B GLN   B 107 ? 0.3555 0.3464 0.3535 -0.0050 0.0749  0.0000  107 GLN   B N   
5632 C  CA  A GLN   B 107 ? 0.3185 0.3166 0.3588 -0.0282 0.1653  0.0178  107 GLN   B CA  
5633 C  CA  B GLN   B 107 ? 0.3393 0.3419 0.3612 -0.0038 0.0764  0.0029  107 GLN   B CA  
5634 C  C   A GLN   B 107 ? 0.2859 0.2934 0.3281 -0.0198 0.1346  0.0085  107 GLN   B C   
5635 C  C   B GLN   B 107 ? 0.3036 0.3123 0.3260 -0.0008 0.0891  0.0024  107 GLN   B C   
5636 O  O   A GLN   B 107 ? 0.2764 0.2895 0.3581 -0.0170 0.1069  -0.0098 107 GLN   B O   
5637 O  O   B GLN   B 107 ? 0.3024 0.3144 0.3328 0.0009  0.0790  -0.0043 107 GLN   B O   
5638 C  CB  A GLN   B 107 ? 0.3490 0.3574 0.4251 -0.0267 0.1413  0.0198  107 GLN   B CB  
5639 C  CB  B GLN   B 107 ? 0.3604 0.3659 0.4105 -0.0036 0.0622  0.0044  107 GLN   B CB  
5640 C  CG  A GLN   B 107 ? 0.3802 0.3941 0.4916 -0.0206 0.1049  0.0186  107 GLN   B CG  
5641 C  CG  B GLN   B 107 ? 0.3786 0.3865 0.4584 -0.0021 0.0465  0.0055  107 GLN   B CG  
5642 C  CD  A GLN   B 107 ? 0.4031 0.4208 0.5419 -0.0183 0.0783  0.0201  107 GLN   B CD  
5643 C  CD  B GLN   B 107 ? 0.3927 0.4020 0.4971 -0.0022 0.0344  0.0069  107 GLN   B CD  
5644 O  OE1 A GLN   B 107 ? 0.4114 0.4311 0.5600 -0.0162 0.0733  0.0176  107 GLN   B OE1 
5645 O  OE1 B GLN   B 107 ? 0.3979 0.4079 0.5104 -0.0020 0.0323  0.0067  107 GLN   B OE1 
5646 N  NE2 A GLN   B 107 ? 0.4127 0.4288 0.5587 -0.0161 0.0667  0.0239  107 GLN   B NE2 
5647 N  NE2 B GLN   B 107 ? 0.3982 0.4068 0.5108 -0.0015 0.0294  0.0085  107 GLN   B NE2 
5664 N  N   . LEU   B 108 ? 0.2668 0.2795 0.2947 0.0055  0.1083  0.0073  108 LEU   B N   
5665 C  CA  . LEU   B 108 ? 0.2379 0.2487 0.2540 0.0236  0.0803  0.0228  108 LEU   B CA  
5666 C  C   . LEU   B 108 ? 0.1940 0.2034 0.2349 0.0271  0.0554  0.0290  108 LEU   B C   
5667 O  O   . LEU   B 108 ? 0.1903 0.1907 0.2310 0.0240  0.0455  0.0275  108 LEU   B O   
5668 C  CB  . LEU   B 108 ? 0.2561 0.2680 0.2434 0.0265  0.0762  0.0265  108 LEU   B CB  
5669 C  CG  . LEU   B 108 ? 0.2694 0.2955 0.2490 0.0285  0.0742  0.0029  108 LEU   B CG  
5670 C  CD1 . LEU   B 108 ? 0.2781 0.3095 0.2449 0.0213  0.0742  0.0029  108 LEU   B CD1 
5671 C  CD2 . LEU   B 108 ? 0.2831 0.3076 0.2613 0.0374  0.0661  -0.0122 108 LEU   B CD2 
5684 N  N   . LEU   B 109 ? 0.1814 0.1813 0.2324 0.0137  0.0502  0.0192  109 LEU   B N   
5685 C  CA  . LEU   B 109 ? 0.1615 0.1512 0.2496 0.0066  0.0437  0.0269  109 LEU   B CA  
5686 C  C   . LEU   B 109 ? 0.1494 0.1372 0.2485 0.0005  0.0345  0.0178  109 LEU   B C   
5687 O  O   . LEU   B 109 ? 0.1475 0.1375 0.2391 0.0007  0.0311  0.0307  109 LEU   B O   
5688 C  CB  . LEU   B 109 ? 0.1693 0.1430 0.2535 0.0063  0.0290  0.0367  109 LEU   B CB  
5689 C  CG  . LEU   B 109 ? 0.1654 0.1399 0.2528 0.0048  0.0200  0.0250  109 LEU   B CG  
5690 C  CD1 . LEU   B 109 ? 0.1619 0.1496 0.2323 0.0147  0.0252  0.0296  109 LEU   B CD1 
5691 C  CD2 . LEU   B 109 ? 0.1759 0.1437 0.2684 0.0076  0.0180  0.0273  109 LEU   B CD2 
5703 N  N   . LYS   B 110 ? 0.1495 0.1427 0.2415 -0.0058 0.0367  0.0227  110 LYS   B N   
5704 C  CA  . LYS   B 110 ? 0.1476 0.1367 0.2369 -0.0026 0.0308  0.0140  110 LYS   B CA  
5705 C  C   . LYS   B 110 ? 0.1403 0.1381 0.2267 0.0004  0.0362  0.0081  110 LYS   B C   
5706 O  O   . LYS   B 110 ? 0.1361 0.1412 0.2254 -0.0097 0.0309  0.0092  110 LYS   B O   
5707 C  CB  . LYS   B 110 ? 0.1474 0.1389 0.2568 -0.0045 0.0293  0.0148  110 LYS   B CB  
5708 C  CG  . LYS   B 110 ? 0.1473 0.1409 0.2634 -0.0022 0.0147  0.0204  110 LYS   B CG  
5709 C  CD  . LYS   B 110 ? 0.1506 0.1360 0.2712 -0.0092 0.0175  0.0146  110 LYS   B CD  
5710 C  CE  . LYS   B 110 ? 0.1511 0.1489 0.2970 -0.0064 0.0147  0.0050  110 LYS   B CE  
5711 N  NZ  . LYS   B 110 ? 0.1528 0.1705 0.2893 0.0045  0.0054  -0.0020 110 LYS   B NZ  
5725 N  N   . SER   B 111 ? 0.1479 0.1372 0.2457 -0.0056 0.0319  0.0116  111 SER   B N   
5726 C  CA  . SER   B 111 ? 0.1542 0.1433 0.2266 -0.0030 0.0224  0.0188  111 SER   B CA  
5727 C  C   . SER   B 111 ? 0.1489 0.1321 0.2112 -0.0026 0.0207  0.0059  111 SER   B C   
5728 O  O   . SER   B 111 ? 0.1455 0.1353 0.2273 -0.0034 0.0163  0.0082  111 SER   B O   
5729 C  CB  . SER   B 111 ? 0.1623 0.1668 0.2372 -0.0055 0.0394  0.0213  111 SER   B CB  
5730 O  OG  . SER   B 111 ? 0.1819 0.1949 0.2429 0.0065  0.0470  0.0308  111 SER   B OG  
5736 N  N   . ALA   B 112 ? 0.1396 0.1391 0.2184 0.0048  0.0308  0.0178  112 ALA   B N   
5737 C  CA  . ALA   B 112 ? 0.1403 0.1459 0.2004 -0.0002 0.0113  0.0055  112 ALA   B CA  
5738 C  C   . ALA   B 112 ? 0.1318 0.1386 0.1920 -0.0037 0.0121  0.0047  112 ALA   B C   
5739 O  O   . ALA   B 112 ? 0.1303 0.1362 0.2079 -0.0064 0.0146  0.0052  112 ALA   B O   
5740 C  CB  . ALA   B 112 ? 0.1420 0.1479 0.2043 0.0032  0.0109  0.0124  112 ALA   B CB  
5746 N  N   . TYR   B 113 ? 0.1307 0.1242 0.2062 -0.0018 0.0139  0.0045  113 TYR   B N   
5747 C  CA  . TYR   B 113 ? 0.1261 0.1216 0.1994 -0.0049 0.0125  -0.0004 113 TYR   B CA  
5748 C  C   . TYR   B 113 ? 0.1233 0.1173 0.1922 -0.0110 0.0129  0.0076  113 TYR   B C   
5749 O  O   . TYR   B 113 ? 0.1284 0.1227 0.1861 -0.0070 0.0082  0.0007  113 TYR   B O   
5750 C  CB  . TYR   B 113 ? 0.1351 0.1213 0.2052 -0.0067 0.0169  0.0089  113 TYR   B CB  
5751 C  CG  . TYR   B 113 ? 0.1319 0.1236 0.2256 -0.0030 0.0172  0.0147  113 TYR   B CG  
5752 C  CD1 . TYR   B 113 ? 0.1388 0.1255 0.2291 -0.0030 0.0189  0.0163  113 TYR   B CD1 
5753 C  CD2 . TYR   B 113 ? 0.1450 0.1224 0.2167 -0.0067 0.0120  0.0128  113 TYR   B CD2 
5754 C  CE1 . TYR   B 113 ? 0.1397 0.1299 0.2228 -0.0027 0.0254  0.0040  113 TYR   B CE1 
5755 C  CE2 . TYR   B 113 ? 0.1526 0.1159 0.2230 -0.0002 0.0147  0.0148  113 TYR   B CE2 
5756 C  CZ  . TYR   B 113 ? 0.1420 0.1254 0.2268 0.0038  0.0129  0.0092  113 TYR   B CZ  
5757 O  OH  . TYR   B 113 ? 0.1465 0.1196 0.2517 0.0093  0.0265  0.0063  113 TYR   B OH  
5767 N  N   . GLU   B 114 ? 0.1247 0.1130 0.2096 -0.0035 0.0168  0.0065  114 GLU   B N   
5768 C  CA  . GLU   B 114 ? 0.1255 0.1169 0.2097 0.0015  0.0111  0.0037  114 GLU   B CA  
5769 C  C   . GLU   B 114 ? 0.1256 0.1216 0.1989 -0.0037 0.0097  0.0080  114 GLU   B C   
5770 O  O   . GLU   B 114 ? 0.1245 0.1211 0.2031 -0.0008 -0.0024 0.0081  114 GLU   B O   
5771 C  CB  . GLU   B 114 ? 0.1292 0.1228 0.2192 -0.0023 0.0153  0.0088  114 GLU   B CB  
5772 C  CG  . GLU   B 114 ? 0.1320 0.1255 0.2106 -0.0049 0.0125  0.0102  114 GLU   B CG  
5773 C  CD  . GLU   B 114 ? 0.1316 0.1329 0.2287 -0.0081 0.0085  0.0088  114 GLU   B CD  
5774 O  OE1 . GLU   B 114 ? 0.1263 0.1468 0.2234 -0.0112 0.0227  0.0115  114 GLU   B OE1 
5775 O  OE2 . GLU   B 114 ? 0.1265 0.1460 0.2426 -0.0195 0.0165  0.0075  114 GLU   B OE2 
5782 N  N   . ASN   B 115 ? 0.1276 0.1140 0.1951 -0.0056 0.0012  0.0100  115 ASN   B N   
5783 C  CA  . ASN   B 115 ? 0.1321 0.1214 0.1735 -0.0066 0.0068  0.0118  115 ASN   B CA  
5784 C  C   . ASN   B 115 ? 0.1238 0.1194 0.1805 -0.0126 0.0012  0.0034  115 ASN   B C   
5785 O  O   . ASN   B 115 ? 0.1329 0.1244 0.1875 -0.0125 0.0031  0.0035  115 ASN   B O   
5786 C  CB  . ASN   B 115 ? 0.1350 0.1337 0.1835 -0.0126 0.0088  0.0050  115 ASN   B CB  
5787 C  CG  . ASN   B 115 ? 0.1438 0.1403 0.1853 0.0009  0.0045  -0.0005 115 ASN   B CG  
5788 O  OD1 . ASN   B 115 ? 0.1880 0.1529 0.2008 0.0004  0.0196  -0.0112 115 ASN   B OD1 
5789 N  ND2 . ASN   B 115 ? 0.1433 0.1508 0.1830 -0.0055 0.0074  0.0043  115 ASN   B ND2 
5796 N  N   . PHE   B 116 ? 0.1251 0.1221 0.1658 -0.0061 0.0022  0.0019  116 PHE   B N   
5797 C  CA  . PHE   B 116 ? 0.1308 0.1275 0.1757 -0.0091 -0.0003 0.0040  116 PHE   B CA  
5798 C  C   . PHE   B 116 ? 0.1308 0.1150 0.1742 -0.0119 -0.0005 0.0042  116 PHE   B C   
5799 O  O   . PHE   B 116 ? 0.1321 0.1245 0.1868 -0.0039 -0.0052 0.0058  116 PHE   B O   
5800 C  CB  . PHE   B 116 ? 0.1271 0.1198 0.1673 -0.0057 -0.0096 0.0032  116 PHE   B CB  
5801 C  CG  . PHE   B 116 ? 0.1222 0.1186 0.1695 -0.0094 0.0014  0.0044  116 PHE   B CG  
5802 C  CD1 . PHE   B 116 ? 0.1304 0.1280 0.1856 -0.0048 0.0030  0.0046  116 PHE   B CD1 
5803 C  CD2 . PHE   B 116 ? 0.1310 0.1318 0.1661 -0.0080 0.0038  -0.0016 116 PHE   B CD2 
5804 C  CE1 . PHE   B 116 ? 0.1344 0.1312 0.1781 -0.0058 -0.0028 0.0084  116 PHE   B CE1 
5805 C  CE2 . PHE   B 116 ? 0.1363 0.1295 0.1715 -0.0001 0.0035  0.0038  116 PHE   B CE2 
5806 C  CZ  . PHE   B 116 ? 0.1289 0.1338 0.1706 0.0001  -0.0066 0.0049  116 PHE   B CZ  
5816 N  N   . ASN   B 117 ? 0.1267 0.1182 0.1890 -0.0047 -0.0068 0.0059  117 ASN   B N   
5817 C  CA  . ASN   B 117 ? 0.1350 0.1266 0.1885 -0.0013 -0.0048 0.0061  117 ASN   B CA  
5818 C  C   . ASN   B 117 ? 0.1368 0.1238 0.2023 -0.0009 -0.0070 0.0068  117 ASN   B C   
5819 O  O   . ASN   B 117 ? 0.1425 0.1272 0.2376 -0.0057 -0.0299 0.0098  117 ASN   B O   
5820 C  CB  . ASN   B 117 ? 0.1359 0.1274 0.1893 -0.0010 -0.0070 0.0028  117 ASN   B CB  
5821 C  CG  . ASN   B 117 ? 0.1282 0.1286 0.2042 0.0015  -0.0008 -0.0059 117 ASN   B CG  
5822 O  OD1 . ASN   B 117 ? 0.1483 0.1290 0.2181 -0.0169 0.0036  -0.0062 117 ASN   B OD1 
5823 N  ND2 . ASN   B 117 ? 0.1362 0.1280 0.2025 -0.0020 -0.0012 0.0010  117 ASN   B ND2 
5830 N  N   . GLN   B 118 ? 0.1384 0.1184 0.1911 -0.0114 -0.0153 0.0014  118 GLN   B N   
5831 C  CA  . GLN   B 118 ? 0.1417 0.1205 0.2081 -0.0021 -0.0098 -0.0024 118 GLN   B CA  
5832 C  C   . GLN   B 118 ? 0.1446 0.1201 0.2065 -0.0034 -0.0047 -0.0025 118 GLN   B C   
5833 O  O   . GLN   B 118 ? 0.1646 0.1190 0.2454 -0.0094 0.0050  0.0080  118 GLN   B O   
5834 C  CB  . GLN   B 118 ? 0.1474 0.1275 0.2197 0.0011  -0.0125 -0.0025 118 GLN   B CB  
5835 C  CG  . GLN   B 118 ? 0.1574 0.1298 0.2118 0.0036  -0.0026 -0.0091 118 GLN   B CG  
5836 C  CD  . GLN   B 118 ? 0.1616 0.1256 0.2128 0.0029  -0.0036 -0.0159 118 GLN   B CD  
5837 O  OE1 . GLN   B 118 ? 0.1732 0.1215 0.2325 0.0032  0.0080  0.0025  118 GLN   B OE1 
5838 N  NE2 . GLN   B 118 ? 0.1688 0.1284 0.2152 0.0017  -0.0021 0.0032  118 GLN   B NE2 
5847 N  N   . HIS   B 119 ? 0.1438 0.1273 0.1760 -0.0093 -0.0068 0.0034  119 HIS   B N   
5848 C  CA  . HIS   B 119 ? 0.1549 0.1366 0.1709 -0.0037 -0.0107 0.0128  119 HIS   B CA  
5849 C  C   . HIS   B 119 ? 0.1560 0.1386 0.1621 -0.0063 -0.0260 0.0072  119 HIS   B C   
5850 O  O   . HIS   B 119 ? 0.1649 0.1366 0.1898 -0.0292 -0.0203 0.0109  119 HIS   B O   
5851 C  CB  . HIS   B 119 ? 0.1582 0.1466 0.1825 -0.0054 -0.0160 0.0019  119 HIS   B CB  
5852 C  CG  . HIS   B 119 ? 0.1597 0.1707 0.1975 0.0061  -0.0340 -0.0187 119 HIS   B CG  
5853 N  ND1 . HIS   B 119 ? 0.1719 0.1852 0.2303 0.0012  -0.0414 -0.0358 119 HIS   B ND1 
5854 C  CD2 . HIS   B 119 ? 0.1791 0.1890 0.2075 0.0370  -0.0440 -0.0206 119 HIS   B CD2 
5855 C  CE1 . HIS   B 119 ? 0.1909 0.2011 0.2372 0.0145  -0.0488 -0.0491 119 HIS   B CE1 
5856 N  NE2 . HIS   B 119 ? 0.1931 0.2119 0.2222 0.0319  -0.0455 -0.0354 119 HIS   B NE2 
5864 N  N   . GLU   B 120 ? 0.1745 0.1384 0.1663 -0.0114 -0.0364 0.0153  120 GLU   B N   
5865 C  CA  . GLU   B 120 ? 0.2099 0.1537 0.1769 -0.0069 -0.0423 0.0315  120 GLU   B CA  
5866 C  C   . GLU   B 120 ? 0.1822 0.1434 0.1700 -0.0167 -0.0319 0.0275  120 GLU   B C   
5867 O  O   . GLU   B 120 ? 0.1732 0.1550 0.1810 -0.0159 -0.0366 0.0160  120 GLU   B O   
5868 C  CB  . GLU   B 120 ? 0.2822 0.1991 0.2627 0.0199  -0.0768 0.0537  120 GLU   B CB  
5869 C  CG  . GLU   B 120 ? 0.3436 0.2750 0.3628 0.0323  -0.0983 0.0730  120 GLU   B CG  
5870 C  CD  . GLU   B 120 ? 0.3956 0.3539 0.4701 0.0356  -0.1058 0.0799  120 GLU   B CD  
5871 O  OE1 . GLU   B 120 ? 0.4204 0.3835 0.5065 0.0320  -0.1026 0.0887  120 GLU   B OE1 
5872 O  OE2 . GLU   B 120 ? 0.4231 0.3902 0.5225 0.0374  -0.1045 0.0730  120 GLU   B OE2 
5879 N  N   . VAL   B 121 ? 0.1656 0.1402 0.1736 -0.0236 -0.0204 0.0193  121 VAL   B N   
5880 C  CA  . VAL   B 121 ? 0.1620 0.1490 0.1542 -0.0232 -0.0243 0.0124  121 VAL   B CA  
5881 C  C   . VAL   B 121 ? 0.1570 0.1431 0.1518 -0.0266 -0.0200 0.0139  121 VAL   B C   
5882 O  O   . VAL   B 121 ? 0.1650 0.1407 0.1765 -0.0299 -0.0300 0.0095  121 VAL   B O   
5883 C  CB  . VAL   B 121 ? 0.1923 0.1905 0.1660 -0.0065 -0.0276 0.0191  121 VAL   B CB  
5884 C  CG1 . VAL   B 121 ? 0.1933 0.2004 0.2006 -0.0188 -0.0155 0.0217  121 VAL   B CG1 
5885 C  CG2 . VAL   B 121 ? 0.2199 0.2158 0.1708 0.0006  -0.0244 0.0024  121 VAL   B CG2 
5895 N  N   . LEU   B 122 ? 0.1516 0.1383 0.1472 -0.0205 -0.0204 0.0045  122 LEU   B N   
5896 C  CA  . LEU   B 122 ? 0.1436 0.1492 0.1254 -0.0207 -0.0211 0.0087  122 LEU   B CA  
5897 C  C   . LEU   B 122 ? 0.1438 0.1329 0.1433 -0.0270 -0.0158 0.0094  122 LEU   B C   
5898 O  O   . LEU   B 122 ? 0.1561 0.1345 0.1825 -0.0331 -0.0200 0.0031  122 LEU   B O   
5899 C  CB  . LEU   B 122 ? 0.1683 0.1564 0.1678 -0.0039 -0.0268 0.0122  122 LEU   B CB  
5900 C  CG  . LEU   B 122 ? 0.1521 0.1609 0.1824 -0.0149 -0.0114 0.0132  122 LEU   B CG  
5901 C  CD1 . LEU   B 122 ? 0.1598 0.1896 0.1861 -0.0195 -0.0118 0.0052  122 LEU   B CD1 
5902 C  CD2 . LEU   B 122 ? 0.1587 0.1556 0.1678 -0.0092 -0.0091 -0.0063 122 LEU   B CD2 
5914 N  N   . LEU   B 123 ? 0.1440 0.1246 0.1374 -0.0242 -0.0117 0.0077  123 LEU   B N   
5915 C  CA  . LEU   B 123 ? 0.1492 0.1267 0.1394 -0.0242 -0.0140 -0.0006 123 LEU   B CA  
5916 C  C   . LEU   B 123 ? 0.1433 0.1226 0.1425 -0.0223 -0.0105 -0.0012 123 LEU   B C   
5917 O  O   . LEU   B 123 ? 0.1508 0.1275 0.1429 -0.0307 -0.0154 0.0025  123 LEU   B O   
5918 C  CB  . LEU   B 123 ? 0.1494 0.1328 0.1498 -0.0233 -0.0040 -0.0021 123 LEU   B CB  
5919 C  CG  . LEU   B 123 ? 0.1466 0.1345 0.1706 -0.0173 -0.0025 0.0036  123 LEU   B CG  
5920 C  CD1 . LEU   B 123 ? 0.1573 0.1388 0.1749 -0.0170 0.0058  -0.0075 123 LEU   B CD1 
5921 C  CD2 . LEU   B 123 ? 0.1536 0.1449 0.1845 -0.0143 -0.0025 0.0176  123 LEU   B CD2 
5933 N  N   . ALA   B 124 ? 0.1419 0.1234 0.1427 -0.0206 0.0000  -0.0043 124 ALA   B N   
5934 C  CA  . ALA   B 124 ? 0.1358 0.1238 0.1550 -0.0153 -0.0065 -0.0088 124 ALA   B CA  
5935 C  C   . ALA   B 124 ? 0.1311 0.1203 0.1421 -0.0169 -0.0136 0.0030  124 ALA   B C   
5936 O  O   . ALA   B 124 ? 0.1398 0.1245 0.1620 -0.0151 -0.0145 0.0012  124 ALA   B O   
5937 C  CB  . ALA   B 124 ? 0.1406 0.1287 0.1702 -0.0065 0.0026  -0.0012 124 ALA   B CB  
5943 N  N   . PRO   B 125 ? 0.1422 0.1242 0.1396 -0.0132 -0.0135 0.0103  125 PRO   B N   
5944 C  CA  . PRO   B 125 ? 0.1489 0.1259 0.1596 -0.0160 -0.0106 0.0232  125 PRO   B CA  
5945 C  C   . PRO   B 125 ? 0.1430 0.1251 0.1692 -0.0159 -0.0084 0.0073  125 PRO   B C   
5946 O  O   . PRO   B 125 ? 0.1454 0.1249 0.1926 -0.0123 -0.0024 0.0122  125 PRO   B O   
5947 C  CB  . PRO   B 125 ? 0.1475 0.1510 0.1797 -0.0184 -0.0178 0.0352  125 PRO   B CB  
5948 C  CG  . PRO   B 125 ? 0.1590 0.1584 0.1616 -0.0284 -0.0186 0.0177  125 PRO   B CG  
5949 C  CD  . PRO   B 125 ? 0.1524 0.1370 0.1452 -0.0270 -0.0060 0.0113  125 PRO   B CD  
5957 N  N   . LEU   B 126 ? 0.1491 0.1196 0.1967 -0.0163 0.0098  0.0114  126 LEU   B N   
5958 C  CA  . LEU   B 126 ? 0.1564 0.1305 0.1980 -0.0136 0.0195  0.0146  126 LEU   B CA  
5959 C  C   . LEU   B 126 ? 0.1546 0.1372 0.2035 0.0022  0.0246  0.0231  126 LEU   B C   
5960 O  O   . LEU   B 126 ? 0.1765 0.1613 0.2252 0.0118  -0.0023 0.0032  126 LEU   B O   
5961 C  CB  . LEU   B 126 ? 0.1746 0.1336 0.2233 -0.0195 0.0209  0.0128  126 LEU   B CB  
5962 C  CG  . LEU   B 126 ? 0.1894 0.1419 0.2395 -0.0235 0.0251  -0.0115 126 LEU   B CG  
5963 C  CD1 . LEU   B 126 ? 0.2032 0.1506 0.2921 -0.0181 0.0155  -0.0162 126 LEU   B CD1 
5964 C  CD2 . LEU   B 126 ? 0.1917 0.1521 0.2412 -0.0272 0.0163  -0.0133 126 LEU   B CD2 
5976 N  N   . LEU   B 127 ? 0.1515 0.1221 0.2207 0.0020  0.0291  0.0106  127 LEU   B N   
5977 C  CA  . LEU   B 127 ? 0.1457 0.1357 0.2234 -0.0045 0.0341  0.0171  127 LEU   B CA  
5978 C  C   . LEU   B 127 ? 0.1429 0.1310 0.2217 0.0007  0.0233  0.0190  127 LEU   B C   
5979 O  O   . LEU   B 127 ? 0.1447 0.1345 0.2428 -0.0161 0.0153  0.0158  127 LEU   B O   
5980 C  CB  . LEU   B 127 ? 0.1589 0.1357 0.2372 0.0013  0.0315  0.0248  127 LEU   B CB  
5981 C  CG  . LEU   B 127 ? 0.1722 0.1370 0.2438 0.0045  0.0290  0.0207  127 LEU   B CG  
5982 C  CD1 . LEU   B 127 ? 0.1801 0.1342 0.2396 0.0047  0.0258  0.0075  127 LEU   B CD1 
5983 C  CD2 . LEU   B 127 ? 0.1698 0.1442 0.2652 -0.0078 0.0279  0.0354  127 LEU   B CD2 
5995 N  N   . SER   B 128 ? 0.1450 0.1299 0.2202 -0.0008 0.0098  0.0165  128 SER   B N   
5996 C  CA  . SER   B 128 ? 0.1637 0.1396 0.2176 0.0059  0.0032  0.0220  128 SER   B CA  
5997 C  C   . SER   B 128 ? 0.1777 0.1441 0.2429 0.0070  -0.0173 0.0220  128 SER   B C   
5998 O  O   . SER   B 128 ? 0.1890 0.1473 0.2779 0.0032  -0.0134 0.0311  128 SER   B O   
5999 C  CB  . SER   B 128 ? 0.1752 0.1392 0.2180 0.0051  0.0043  0.0343  128 SER   B CB  
6000 O  OG  . SER   B 128 ? 0.1780 0.1574 0.2215 0.0107  0.0113  0.0320  128 SER   B OG  
6006 N  N   . ALA   B 129 ? 0.1896 0.1481 0.2653 0.0219  -0.0077 0.0076  129 ALA   B N   
6007 C  CA  . ALA   B 129 ? 0.2022 0.1552 0.2783 0.0311  -0.0055 0.0003  129 ALA   B CA  
6008 C  C   . ALA   B 129 ? 0.1971 0.1505 0.2673 0.0178  0.0109  0.0075  129 ALA   B C   
6009 O  O   . ALA   B 129 ? 0.1822 0.1546 0.2554 0.0118  0.0018  0.0098  129 ALA   B O   
6010 C  CB  . ALA   B 129 ? 0.2224 0.1797 0.3155 0.0344  0.0082  -0.0098 129 ALA   B CB  
6016 N  N   . GLY   B 130 ? 0.1933 0.1458 0.2648 0.0281  0.0140  -0.0024 130 GLY   B N   
6017 C  CA  . GLY   B 130 ? 0.1998 0.1567 0.2721 0.0231  0.0357  -0.0077 130 GLY   B CA  
6018 C  C   . GLY   B 130 ? 0.2051 0.1584 0.2645 0.0205  0.0232  0.0017  130 GLY   B C   
6019 O  O   . GLY   B 130 ? 0.2200 0.1703 0.2724 0.0167  0.0102  0.0102  130 GLY   B O   
6023 N  N   . ILE   B 131 ? 0.2016 0.1745 0.2668 0.0329  0.0186  -0.0016 131 ILE   B N   
6024 C  CA  . ILE   B 131 ? 0.2141 0.1858 0.2674 0.0281  0.0082  0.0133  131 ILE   B CA  
6025 C  C   . ILE   B 131 ? 0.2262 0.1737 0.2297 0.0185  0.0072  0.0227  131 ILE   B C   
6026 O  O   . ILE   B 131 ? 0.2521 0.1906 0.2365 0.0190  -0.0153 0.0204  131 ILE   B O   
6027 C  CB  . ILE   B 131 ? 0.2132 0.2209 0.3073 0.0291  0.0023  0.0223  131 ILE   B CB  
6028 C  CG1 . ILE   B 131 ? 0.2177 0.2369 0.3243 0.0064  0.0094  0.0306  131 ILE   B CG1 
6029 C  CG2 . ILE   B 131 ? 0.2130 0.2394 0.3317 0.0366  0.0067  0.0212  131 ILE   B CG2 
6030 C  CD1 . ILE   B 131 ? 0.2236 0.2536 0.3386 -0.0138 -0.0011 0.0370  131 ILE   B CD1 
6042 N  N   . PHE   B 132 ? 0.2113 0.1594 0.2269 0.0150  0.0227  0.0221  132 PHE   B N   
6043 C  CA  . PHE   B 132 ? 0.2228 0.1604 0.2282 0.0105  0.0404  0.0145  132 PHE   B CA  
6044 C  C   . PHE   B 132 ? 0.2432 0.1787 0.2481 0.0129  0.0517  0.0092  132 PHE   B C   
6045 O  O   . PHE   B 132 ? 0.2621 0.1989 0.2686 0.0063  0.0637  0.0197  132 PHE   B O   
6046 C  CB  . PHE   B 132 ? 0.2103 0.1608 0.2098 0.0126  0.0472  0.0164  132 PHE   B CB  
6047 C  CG  . PHE   B 132 ? 0.2020 0.1654 0.2065 0.0165  0.0369  0.0202  132 PHE   B CG  
6048 C  CD1 . PHE   B 132 ? 0.2082 0.1691 0.2354 0.0129  0.0306  0.0209  132 PHE   B CD1 
6049 C  CD2 . PHE   B 132 ? 0.2002 0.1710 0.1936 0.0217  0.0318  0.0304  132 PHE   B CD2 
6050 C  CE1 . PHE   B 132 ? 0.2105 0.1730 0.2462 0.0098  0.0248  0.0212  132 PHE   B CE1 
6051 C  CE2 . PHE   B 132 ? 0.2096 0.1804 0.1970 0.0188  0.0188  0.0282  132 PHE   B CE2 
6052 C  CZ  . PHE   B 132 ? 0.2086 0.1754 0.2255 0.0124  0.0053  0.0333  132 PHE   B CZ  
6062 N  N   . GLY   B 133 ? 0.2359 0.1696 0.2502 0.0082  0.0410  0.0308  133 GLY   B N   
6063 C  CA  . GLY   B 133 ? 0.2478 0.1807 0.2630 -0.0160 0.0378  0.0433  133 GLY   B CA  
6064 C  C   . GLY   B 133 ? 0.2538 0.1887 0.2643 -0.0316 0.0459  0.0457  133 GLY   B C   
6065 O  O   . GLY   B 133 ? 0.2725 0.2022 0.3115 -0.0465 0.0476  0.0597  133 GLY   B O   
6069 N  N   . ALA   B 134 ? 0.2347 0.1867 0.2483 -0.0279 0.0448  0.0227  134 ALA   B N   
6070 C  CA  . ALA   B 134 ? 0.2287 0.1828 0.2592 -0.0192 0.0578  0.0112  134 ALA   B CA  
6071 C  C   . ALA   B 134 ? 0.2376 0.1720 0.2634 -0.0138 0.0495  0.0294  134 ALA   B C   
6072 O  O   . ALA   B 134 ? 0.2419 0.1898 0.2799 -0.0034 0.0374  0.0219  134 ALA   B O   
6073 C  CB  . ALA   B 134 ? 0.2299 0.1859 0.2832 -0.0079 0.0475  0.0071  134 ALA   B CB  
6079 N  N   . ASP   B 135 ? 0.2538 0.1681 0.2706 -0.0193 0.0283  0.0347  135 ASP   B N   
6080 C  CA  . ASP   B 135 ? 0.2679 0.1599 0.2927 -0.0186 0.0125  0.0392  135 ASP   B CA  
6081 C  C   . ASP   B 135 ? 0.2473 0.1458 0.2793 -0.0066 0.0110  0.0340  135 ASP   B C   
6082 O  O   . ASP   B 135 ? 0.2435 0.1414 0.2868 -0.0031 0.0095  0.0289  135 ASP   B O   
6083 C  CB  . ASP   B 135 ? 0.2943 0.1731 0.3183 -0.0393 0.0098  0.0413  135 ASP   B CB  
6084 C  CG  . ASP   B 135 ? 0.3181 0.1740 0.3551 -0.0590 0.0074  0.0359  135 ASP   B CG  
6085 O  OD1 . ASP   B 135 ? 0.3217 0.1604 0.3571 -0.0417 -0.0037 0.0317  135 ASP   B OD1 
6086 O  OD2 . ASP   B 135 ? 0.3388 0.2099 0.4053 -0.0733 0.0074  0.0184  135 ASP   B OD2 
6091 N  N   . PRO   B 136 ? 0.2341 0.1562 0.2875 0.0118  -0.0021 0.0257  136 PRO   B N   
6092 C  CA  . PRO   B 136 ? 0.2084 0.1474 0.2902 0.0176  -0.0021 0.0123  136 PRO   B CA  
6093 C  C   . PRO   B 136 ? 0.1881 0.1366 0.2973 0.0127  -0.0009 0.0133  136 PRO   B C   
6094 O  O   . PRO   B 136 ? 0.1689 0.1352 0.2870 0.0096  0.0073  0.0135  136 PRO   B O   
6095 C  CB  . PRO   B 136 ? 0.2151 0.1725 0.3016 0.0283  -0.0111 0.0041  136 PRO   B CB  
6096 C  CG  . PRO   B 136 ? 0.2334 0.1759 0.3174 0.0328  -0.0026 0.0063  136 PRO   B CG  
6097 C  CD  . PRO   B 136 ? 0.2403 0.1703 0.3055 0.0347  0.0001  0.0124  136 PRO   B CD  
6105 N  N   . ILE   B 137 ? 0.2003 0.1302 0.3051 0.0140  -0.0088 0.0076  137 ILE   B N   
6106 C  CA  . ILE   B 137 ? 0.2058 0.1262 0.3141 -0.0019 0.0022  0.0074  137 ILE   B CA  
6107 C  C   . ILE   B 137 ? 0.1971 0.1337 0.2991 -0.0074 0.0159  0.0159  137 ILE   B C   
6108 O  O   . ILE   B 137 ? 0.1850 0.1372 0.2970 -0.0093 0.0162  0.0114  137 ILE   B O   
6109 C  CB  . ILE   B 137 ? 0.2323 0.1404 0.3514 -0.0056 0.0013  0.0132  137 ILE   B CB  
6110 C  CG1 . ILE   B 137 ? 0.2593 0.1553 0.3969 0.0062  0.0071  0.0031  137 ILE   B CG1 
6111 C  CG2 . ILE   B 137 ? 0.2332 0.1457 0.3556 -0.0340 0.0009  0.0179  137 ILE   B CG2 
6112 C  CD1 . ILE   B 137 ? 0.2817 0.1759 0.4316 0.0173  0.0018  0.0076  137 ILE   B CD1 
6124 N  N   . HIS   B 138 ? 0.2032 0.1310 0.2995 -0.0103 0.0301  0.0147  138 HIS   B N   
6125 C  CA  . HIS   B 138 ? 0.2117 0.1466 0.2954 -0.0088 0.0441  0.0187  138 HIS   B CA  
6126 C  C   . HIS   B 138 ? 0.1911 0.1425 0.2826 -0.0072 0.0367  0.0271  138 HIS   B C   
6127 O  O   . HIS   B 138 ? 0.1797 0.1478 0.3000 -0.0060 0.0400  0.0375  138 HIS   B O   
6128 C  CB  . HIS   B 138 ? 0.2372 0.1579 0.3024 -0.0116 0.0644  0.0198  138 HIS   B CB  
6129 C  CG  . HIS   B 138 ? 0.2634 0.1746 0.3093 -0.0119 0.0784  0.0380  138 HIS   B CG  
6130 N  ND1 . HIS   B 138 ? 0.2743 0.1927 0.3359 -0.0066 0.0844  0.0289  138 HIS   B ND1 
6131 C  CD2 . HIS   B 138 ? 0.2795 0.1815 0.3014 -0.0111 0.0841  0.0341  138 HIS   B CD2 
6132 C  CE1 . HIS   B 138 ? 0.2771 0.1870 0.3300 -0.0061 0.0866  0.0302  138 HIS   B CE1 
6133 N  NE2 . HIS   B 138 ? 0.2832 0.1777 0.3070 -0.0009 0.0928  0.0258  138 HIS   B NE2 
6141 N  N   . SER   B 139 ? 0.1910 0.1296 0.2779 0.0044  0.0305  0.0151  139 SER   B N   
6142 C  CA  . SER   B 139 ? 0.1845 0.1254 0.2639 0.0001  0.0267  0.0067  139 SER   B CA  
6143 C  C   . SER   B 139 ? 0.1595 0.1189 0.2647 -0.0030 0.0208  0.0088  139 SER   B C   
6144 O  O   . SER   B 139 ? 0.1595 0.1218 0.2693 -0.0034 0.0071  0.0080  139 SER   B O   
6145 C  CB  . SER   B 139 ? 0.1947 0.1285 0.2722 0.0027  0.0101  0.0035  139 SER   B CB  
6146 O  OG  . SER   B 139 ? 0.1902 0.1235 0.2719 -0.0032 -0.0049 0.0166  139 SER   B OG  
6152 N  N   . LEU   B 140 ? 0.1597 0.1169 0.2547 -0.0057 0.0257  0.0027  140 LEU   B N   
6153 C  CA  . LEU   B 140 ? 0.1513 0.1218 0.2591 -0.0069 0.0129  0.0074  140 LEU   B CA  
6154 C  C   . LEU   B 140 ? 0.1507 0.1200 0.2735 -0.0049 0.0063  -0.0078 140 LEU   B C   
6155 O  O   . LEU   B 140 ? 0.1470 0.1273 0.2721 -0.0030 0.0041  0.0041  140 LEU   B O   
6156 C  CB  . LEU   B 140 ? 0.1470 0.1166 0.2644 -0.0096 0.0161  -0.0052 140 LEU   B CB  
6157 C  CG  . LEU   B 140 ? 0.1547 0.1261 0.2706 -0.0117 0.0020  0.0072  140 LEU   B CG  
6158 C  CD1 . LEU   B 140 ? 0.1625 0.1372 0.2736 -0.0094 0.0077  0.0087  140 LEU   B CD1 
6159 C  CD2 . LEU   B 140 ? 0.1737 0.1349 0.2893 -0.0125 0.0031  -0.0137 140 LEU   B CD2 
6171 N  N   . ARG   B 141 ? 0.1408 0.1211 0.2887 -0.0131 0.0092  -0.0017 141 ARG   B N   
6172 C  CA  . ARG   B 141 ? 0.1434 0.1235 0.3292 -0.0176 0.0263  0.0009  141 ARG   B CA  
6173 C  C   . ARG   B 141 ? 0.1418 0.1253 0.3131 -0.0168 0.0201  -0.0003 141 ARG   B C   
6174 O  O   . ARG   B 141 ? 0.1455 0.1280 0.3017 -0.0160 0.0166  -0.0112 141 ARG   B O   
6175 C  CB  . ARG   B 141 ? 0.1636 0.1350 0.3420 -0.0216 0.0313  -0.0006 141 ARG   B CB  
6176 C  CG  . ARG   B 141 ? 0.1957 0.1617 0.3508 -0.0196 0.0390  0.0047  141 ARG   B CG  
6177 C  CD  . ARG   B 141 ? 0.2389 0.1883 0.3537 -0.0113 0.0224  -0.0124 141 ARG   B CD  
6178 N  NE  . ARG   B 141 ? 0.2603 0.1863 0.3411 -0.0293 0.0280  -0.0227 141 ARG   B NE  
6179 C  CZ  . ARG   B 141 ? 0.2726 0.1728 0.3218 -0.0271 0.0336  -0.0340 141 ARG   B CZ  
6180 N  NH1 . ARG   B 141 ? 0.2833 0.1622 0.3217 -0.0251 0.0277  -0.0297 141 ARG   B NH1 
6181 N  NH2 . ARG   B 141 ? 0.2815 0.1851 0.3294 -0.0174 0.0171  -0.0296 141 ARG   B NH2 
6195 N  N   . VAL   B 142 ? 0.1461 0.1211 0.3001 -0.0149 0.0231  -0.0038 142 VAL   B N   
6196 C  CA  . VAL   B 142 ? 0.1449 0.1231 0.2859 -0.0112 0.0224  -0.0001 142 VAL   B CA  
6197 C  C   . VAL   B 142 ? 0.1410 0.1177 0.2828 -0.0072 0.0118  -0.0021 142 VAL   B C   
6198 O  O   . VAL   B 142 ? 0.1471 0.1172 0.2987 -0.0043 0.0158  -0.0003 142 VAL   B O   
6199 C  CB  . VAL   B 142 ? 0.1571 0.1330 0.2845 -0.0003 0.0251  0.0130  142 VAL   B CB  
6200 C  CG1 . VAL   B 142 ? 0.1522 0.1377 0.2793 0.0042  0.0307  0.0122  142 VAL   B CG1 
6201 C  CG2 . VAL   B 142 ? 0.1789 0.1302 0.2891 0.0051  0.0147  0.0177  142 VAL   B CG2 
6211 N  N   . CYS   B 143 ? 0.1334 0.1225 0.2629 -0.0033 0.0073  0.0085  143 CYS   B N   
6212 C  CA  . CYS   B 143 ? 0.1337 0.1235 0.2648 -0.0116 0.0111  0.0050  143 CYS   B CA  
6213 C  C   . CYS   B 143 ? 0.1349 0.1242 0.2554 -0.0082 0.0139  -0.0043 143 CYS   B C   
6214 O  O   . CYS   B 143 ? 0.1371 0.1292 0.2542 -0.0081 0.0066  -0.0018 143 CYS   B O   
6215 C  CB  . CYS   B 143 ? 0.1446 0.1255 0.2589 -0.0099 0.0040  0.0025  143 CYS   B CB  
6216 S  SG  . CYS   B 143 ? 0.1434 0.1470 0.2367 -0.0052 0.0079  0.0061  143 CYS   B SG  
6222 N  N   . VAL   B 144 ? 0.1353 0.1262 0.2700 -0.0077 0.0039  -0.0130 144 VAL   B N   
6223 C  CA  . VAL   B 144 ? 0.1409 0.1316 0.2958 -0.0169 -0.0079 -0.0199 144 VAL   B CA  
6224 C  C   . VAL   B 144 ? 0.1406 0.1383 0.2947 -0.0116 -0.0106 -0.0036 144 VAL   B C   
6225 O  O   . VAL   B 144 ? 0.1490 0.1602 0.3066 -0.0015 -0.0043 0.0166  144 VAL   B O   
6226 C  CB  . VAL   B 144 ? 0.1655 0.1492 0.3532 -0.0196 -0.0193 -0.0372 144 VAL   B CB  
6227 C  CG1 . VAL   B 144 ? 0.1929 0.1923 0.3840 -0.0130 -0.0237 -0.0339 144 VAL   B CG1 
6228 C  CG2 . VAL   B 144 ? 0.1814 0.1529 0.3428 -0.0083 -0.0245 -0.0356 144 VAL   B CG2 
6238 N  N   . ASP   B 145 ? 0.1438 0.1317 0.3108 -0.0130 -0.0005 -0.0150 145 ASP   B N   
6239 C  CA  . ASP   B 145 ? 0.1422 0.1365 0.3319 -0.0076 0.0074  -0.0134 145 ASP   B CA  
6240 C  C   . ASP   B 145 ? 0.1374 0.1388 0.3101 -0.0072 0.0110  -0.0139 145 ASP   B C   
6241 O  O   . ASP   B 145 ? 0.1386 0.1539 0.3632 -0.0135 0.0176  -0.0259 145 ASP   B O   
6242 C  CB  . ASP   B 145 ? 0.1543 0.1439 0.3758 -0.0160 0.0200  -0.0019 145 ASP   B CB  
6243 C  CG  . ASP   B 145 ? 0.1708 0.1435 0.4195 -0.0259 0.0303  -0.0067 145 ASP   B CG  
6244 O  OD1 . ASP   B 145 ? 0.1776 0.1508 0.4257 -0.0274 0.0015  -0.0151 145 ASP   B OD1 
6245 O  OD2 . ASP   B 145 ? 0.2028 0.1482 0.4627 -0.0287 0.0552  -0.0008 145 ASP   B OD2 
6250 N  N   . THR   B 146 ? 0.1286 0.1262 0.2692 -0.0117 0.0068  -0.0050 146 THR   B N   
6251 C  CA  . THR   B 146 ? 0.1376 0.1227 0.2532 -0.0078 0.0118  0.0023  146 THR   B CA  
6252 C  C   . THR   B 146 ? 0.1392 0.1234 0.2432 -0.0051 0.0024  0.0020  146 THR   B C   
6253 O  O   . THR   B 146 ? 0.1407 0.1267 0.2523 -0.0082 -0.0018 0.0031  146 THR   B O   
6254 C  CB  . THR   B 146 ? 0.1418 0.1239 0.2618 -0.0033 0.0196  0.0046  146 THR   B CB  
6255 O  OG1 . THR   B 146 ? 0.1434 0.1233 0.2712 -0.0067 0.0206  0.0121  146 THR   B OG1 
6256 C  CG2 . THR   B 146 ? 0.1514 0.1313 0.2635 -0.0039 0.0163  0.0019  146 THR   B CG2 
6264 N  N   . VAL   B 147 ? 0.1458 0.1273 0.2223 -0.0080 0.0145  -0.0004 147 VAL   B N   
6265 C  CA  . VAL   B 147 ? 0.1431 0.1259 0.2210 -0.0124 -0.0039 -0.0002 147 VAL   B CA  
6266 C  C   . VAL   B 147 ? 0.1344 0.1262 0.2390 -0.0171 -0.0116 -0.0029 147 VAL   B C   
6267 O  O   . VAL   B 147 ? 0.1459 0.1374 0.2490 -0.0195 -0.0308 -0.0079 147 VAL   B O   
6268 C  CB  . VAL   B 147 ? 0.1486 0.1349 0.2008 -0.0081 -0.0074 0.0015  147 VAL   B CB  
6269 C  CG1 . VAL   B 147 ? 0.1475 0.1533 0.1989 -0.0157 -0.0020 0.0084  147 VAL   B CG1 
6270 C  CG2 . VAL   B 147 ? 0.1586 0.1282 0.2165 -0.0081 0.0012  -0.0021 147 VAL   B CG2 
6280 N  N   . ARG   B 148 ? 0.1355 0.1298 0.2313 -0.0096 -0.0184 -0.0031 148 ARG   B N   
6281 C  CA  . ARG   B 148 ? 0.1398 0.1374 0.2200 -0.0079 -0.0251 -0.0114 148 ARG   B CA  
6282 C  C   . ARG   B 148 ? 0.1494 0.1462 0.2088 -0.0053 -0.0235 -0.0085 148 ARG   B C   
6283 O  O   . ARG   B 148 ? 0.1671 0.1769 0.2094 -0.0227 -0.0360 -0.0049 148 ARG   B O   
6284 C  CB  . ARG   B 148 ? 0.1481 0.1460 0.2212 -0.0063 -0.0292 -0.0134 148 ARG   B CB  
6285 C  CG  . ARG   B 148 ? 0.1450 0.1625 0.2336 -0.0104 -0.0271 -0.0294 148 ARG   B CG  
6286 C  CD  . ARG   B 148 ? 0.1545 0.1778 0.2441 0.0040  -0.0260 -0.0294 148 ARG   B CD  
6287 N  NE  . ARG   B 148 ? 0.1603 0.1745 0.2439 0.0204  -0.0274 -0.0291 148 ARG   B NE  
6288 C  CZ  . ARG   B 148 ? 0.1463 0.1619 0.2297 0.0137  -0.0223 -0.0185 148 ARG   B CZ  
6289 N  NH1 . ARG   B 148 ? 0.1385 0.1685 0.2334 -0.0014 -0.0046 -0.0209 148 ARG   B NH1 
6290 N  NH2 . ARG   B 148 ? 0.1686 0.1490 0.2193 0.0135  -0.0112 -0.0153 148 ARG   B NH2 
6304 N  N   . THR   B 149 ? 0.1477 0.1393 0.2091 -0.0130 -0.0299 -0.0036 149 THR   B N   
6305 C  CA  . THR   B 149 ? 0.1519 0.1428 0.2046 -0.0184 -0.0287 0.0039  149 THR   B CA  
6306 C  C   . THR   B 149 ? 0.1521 0.1387 0.1943 -0.0183 -0.0315 0.0026  149 THR   B C   
6307 O  O   . THR   B 149 ? 0.1612 0.1404 0.2085 -0.0215 -0.0141 0.0037  149 THR   B O   
6308 C  CB  . THR   B 149 ? 0.1589 0.1372 0.2088 -0.0183 -0.0276 -0.0030 149 THR   B CB  
6309 O  OG1 . THR   B 149 ? 0.1611 0.1438 0.1949 -0.0262 -0.0346 0.0050  149 THR   B OG1 
6310 C  CG2 . THR   B 149 ? 0.1699 0.1422 0.2183 -0.0114 -0.0210 -0.0005 149 THR   B CG2 
6318 N  N   . ASN   B 150 ? 0.1603 0.1392 0.1946 -0.0197 -0.0361 0.0029  150 ASN   B N   
6319 C  CA  . ASN   B 150 ? 0.1691 0.1538 0.1838 -0.0271 -0.0319 -0.0028 150 ASN   B CA  
6320 C  C   . ASN   B 150 ? 0.1594 0.1495 0.1764 -0.0184 -0.0288 -0.0035 150 ASN   B C   
6321 O  O   . ASN   B 150 ? 0.1672 0.1456 0.2000 -0.0255 -0.0389 -0.0025 150 ASN   B O   
6322 C  CB  . ASN   B 150 ? 0.1932 0.1864 0.1989 -0.0279 -0.0449 0.0105  150 ASN   B CB  
6323 C  CG  . ASN   B 150 ? 0.2197 0.2237 0.2342 -0.0279 -0.0466 0.0215  150 ASN   B CG  
6324 O  OD1 . ASN   B 150 ? 0.2274 0.2385 0.2468 -0.0360 -0.0586 0.0178  150 ASN   B OD1 
6325 N  ND2 . ASN   B 150 ? 0.2337 0.2460 0.2717 -0.0177 -0.0524 0.0598  150 ASN   B ND2 
6332 N  N   . VAL   B 151 ? 0.1491 0.1471 0.1803 -0.0220 -0.0274 -0.0011 151 VAL   B N   
6333 C  CA  . VAL   B 151 ? 0.1536 0.1492 0.1846 -0.0275 -0.0176 -0.0027 151 VAL   B CA  
6334 C  C   . VAL   B 151 ? 0.1554 0.1404 0.1781 -0.0334 -0.0239 -0.0043 151 VAL   B C   
6335 O  O   . VAL   B 151 ? 0.1604 0.1488 0.2019 -0.0306 -0.0134 -0.0110 151 VAL   B O   
6336 C  CB  . VAL   B 151 ? 0.1691 0.1597 0.1962 -0.0121 -0.0170 -0.0006 151 VAL   B CB  
6337 C  CG1 . VAL   B 151 ? 0.1752 0.1673 0.2216 -0.0215 -0.0056 -0.0120 151 VAL   B CG1 
6338 C  CG2 . VAL   B 151 ? 0.1830 0.1738 0.1789 -0.0004 -0.0207 0.0128  151 VAL   B CG2 
6348 N  N   . TYR   B 152 ? 0.1506 0.1293 0.1768 -0.0245 -0.0210 -0.0070 152 TYR   B N   
6349 C  CA  . TYR   B 152 ? 0.1522 0.1466 0.1645 -0.0310 -0.0165 -0.0117 152 TYR   B CA  
6350 C  C   . TYR   B 152 ? 0.1502 0.1319 0.1549 -0.0220 -0.0133 -0.0131 152 TYR   B C   
6351 O  O   . TYR   B 152 ? 0.1532 0.1357 0.1680 -0.0228 -0.0156 -0.0027 152 TYR   B O   
6352 C  CB  . TYR   B 152 ? 0.1670 0.1641 0.1686 -0.0317 -0.0109 0.0016  152 TYR   B CB  
6353 C  CG  . TYR   B 152 ? 0.1823 0.1694 0.1628 -0.0390 -0.0116 -0.0018 152 TYR   B CG  
6354 C  CD1 . TYR   B 152 ? 0.1949 0.1830 0.1547 -0.0319 -0.0195 0.0068  152 TYR   B CD1 
6355 C  CD2 . TYR   B 152 ? 0.2064 0.1875 0.1696 -0.0408 -0.0075 -0.0121 152 TYR   B CD2 
6356 C  CE1 . TYR   B 152 ? 0.2129 0.2056 0.1814 -0.0296 -0.0320 0.0168  152 TYR   B CE1 
6357 C  CE2 . TYR   B 152 ? 0.2180 0.2112 0.1674 -0.0412 -0.0143 -0.0193 152 TYR   B CE2 
6358 C  CZ  . TYR   B 152 ? 0.2214 0.2262 0.1652 -0.0358 -0.0373 0.0091  152 TYR   B CZ  
6359 O  OH  . TYR   B 152 ? 0.2441 0.2665 0.1947 -0.0241 -0.0385 0.0087  152 TYR   B OH  
6369 N  N   . LEU   B 153 ? 0.1515 0.1301 0.1759 -0.0256 -0.0118 -0.0064 153 LEU   B N   
6370 C  CA  . LEU   B 153 ? 0.1559 0.1251 0.1584 -0.0228 -0.0024 -0.0144 153 LEU   B CA  
6371 C  C   . LEU   B 153 ? 0.1592 0.1268 0.1702 -0.0264 -0.0037 -0.0167 153 LEU   B C   
6372 O  O   . LEU   B 153 ? 0.1679 0.1489 0.1850 -0.0178 -0.0076 -0.0304 153 LEU   B O   
6373 C  CB  . LEU   B 153 ? 0.1580 0.1263 0.1806 -0.0226 -0.0047 -0.0062 153 LEU   B CB  
6374 C  CG  . LEU   B 153 ? 0.1516 0.1374 0.2097 -0.0283 -0.0060 -0.0071 153 LEU   B CG  
6375 C  CD1 . LEU   B 153 ? 0.1612 0.1510 0.2118 -0.0279 0.0067  0.0037  153 LEU   B CD1 
6376 C  CD2 . LEU   B 153 ? 0.1531 0.1543 0.2141 -0.0340 0.0074  0.0026  153 LEU   B CD2 
6388 N  N   . ALA   B 154 ? 0.1496 0.1288 0.1838 -0.0088 -0.0144 -0.0149 154 ALA   B N   
6389 C  CA  . ALA   B 154 ? 0.1599 0.1411 0.2070 -0.0023 -0.0164 -0.0217 154 ALA   B CA  
6390 C  C   . ALA   B 154 ? 0.1723 0.1429 0.2195 0.0023  -0.0185 -0.0283 154 ALA   B C   
6391 O  O   . ALA   B 154 ? 0.2062 0.1449 0.2315 0.0049  -0.0044 -0.0072 154 ALA   B O   
6392 C  CB  . ALA   B 154 ? 0.1546 0.1550 0.2214 -0.0006 -0.0099 -0.0281 154 ALA   B CB  
6398 N  N   . VAL   B 155 ? 0.1399 0.1342 0.2313 -0.0023 -0.0008 -0.0206 155 VAL   B N   
6399 C  CA  . VAL   B 155 ? 0.1375 0.1331 0.2342 -0.0018 -0.0085 -0.0160 155 VAL   B CA  
6400 C  C   . VAL   B 155 ? 0.1385 0.1291 0.2353 -0.0066 -0.0080 -0.0280 155 VAL   B C   
6401 O  O   . VAL   B 155 ? 0.1623 0.1481 0.2725 0.0030  -0.0096 -0.0443 155 VAL   B O   
6402 C  CB  . VAL   B 155 ? 0.1433 0.1527 0.2640 -0.0064 -0.0129 0.0015  155 VAL   B CB  
6403 C  CG1 . VAL   B 155 ? 0.1522 0.1487 0.2616 -0.0113 -0.0128 0.0017  155 VAL   B CG1 
6404 C  CG2 . VAL   B 155 ? 0.1443 0.1652 0.2837 -0.0126 -0.0127 0.0349  155 VAL   B CG2 
6414 N  N   . PHE   B 156 ? 0.1292 0.1447 0.2536 0.0030  -0.0018 -0.0199 156 PHE   B N   
6415 C  CA  . PHE   B 156 ? 0.1390 0.1512 0.2801 0.0067  0.0010  -0.0233 156 PHE   B CA  
6416 C  C   . PHE   B 156 ? 0.1434 0.1623 0.3160 0.0158  -0.0070 -0.0370 156 PHE   B C   
6417 O  O   . PHE   B 156 ? 0.1684 0.1848 0.3408 0.0254  -0.0019 -0.0482 156 PHE   B O   
6418 C  CB  . PHE   B 156 ? 0.1450 0.1461 0.2737 0.0006  -0.0100 -0.0143 156 PHE   B CB  
6419 C  CG  . PHE   B 156 ? 0.1468 0.1610 0.2852 0.0012  -0.0057 0.0009  156 PHE   B CG  
6420 C  CD1 . PHE   B 156 ? 0.1513 0.1891 0.3216 0.0030  0.0043  0.0334  156 PHE   B CD1 
6421 C  CD2 . PHE   B 156 ? 0.1555 0.1717 0.2833 0.0115  -0.0177 0.0044  156 PHE   B CD2 
6422 C  CE1 . PHE   B 156 ? 0.1517 0.2006 0.3362 0.0043  -0.0013 0.0344  156 PHE   B CE1 
6423 C  CE2 . PHE   B 156 ? 0.1634 0.1966 0.3145 0.0168  -0.0142 0.0119  156 PHE   B CE2 
6424 C  CZ  . PHE   B 156 ? 0.1521 0.2011 0.3347 0.0164  -0.0177 0.0218  156 PHE   B CZ  
6434 N  N   . ASP   B 157 ? 0.1480 0.1507 0.3340 0.0152  -0.0215 -0.0221 157 ASP   B N   
6435 C  CA  . ASP   B 157 ? 0.1628 0.1590 0.3597 0.0142  -0.0279 -0.0273 157 ASP   B CA  
6436 C  C   . ASP   B 157 ? 0.1653 0.1569 0.3572 0.0073  -0.0208 -0.0515 157 ASP   B C   
6437 O  O   . ASP   B 157 ? 0.1426 0.1562 0.3618 0.0065  -0.0173 -0.0332 157 ASP   B O   
6438 C  CB  . ASP   B 157 ? 0.1956 0.1759 0.3755 0.0121  -0.0528 -0.0128 157 ASP   B CB  
6439 C  CG  . ASP   B 157 ? 0.2315 0.1879 0.3955 0.0082  -0.0504 -0.0133 157 ASP   B CG  
6440 O  OD1 . ASP   B 157 ? 0.2330 0.1774 0.4119 0.0161  -0.0477 -0.0123 157 ASP   B OD1 
6441 O  OD2 . ASP   B 157 ? 0.2592 0.2140 0.4149 0.0050  -0.0368 -0.0070 157 ASP   B OD2 
6446 N  N   A LYS   B 158 ? 0.1606 0.1810 0.3725 0.0071  0.0000  -0.0812 158 LYS   B N   
6447 N  N   B LYS   B 158 ? 0.1808 0.1840 0.3367 0.0076  -0.0109 -0.0574 158 LYS   B N   
6448 C  CA  A LYS   B 158 ? 0.1738 0.1968 0.3817 0.0083  0.0058  -0.0944 158 LYS   B CA  
6449 C  CA  B LYS   B 158 ? 0.2029 0.2056 0.3223 0.0091  -0.0078 -0.0587 158 LYS   B CA  
6450 C  C   A LYS   B 158 ? 0.1727 0.1828 0.3958 0.0090  -0.0090 -0.0852 158 LYS   B C   
6451 C  C   B LYS   B 158 ? 0.2024 0.2032 0.3102 0.0102  -0.0138 -0.0557 158 LYS   B C   
6452 O  O   A LYS   B 158 ? 0.1730 0.1753 0.4041 -0.0069 -0.0087 -0.0858 158 LYS   B O   
6453 O  O   B LYS   B 158 ? 0.2044 0.2038 0.3005 0.0057  -0.0116 -0.0556 158 LYS   B O   
6454 C  CB  A LYS   B 158 ? 0.2031 0.2372 0.3760 0.0134  0.0187  -0.1159 158 LYS   B CB  
6455 C  CB  B LYS   B 158 ? 0.2286 0.2298 0.3273 0.0115  -0.0011 -0.0628 158 LYS   B CB  
6456 C  CG  A LYS   B 158 ? 0.2355 0.2809 0.3825 0.0168  0.0236  -0.1144 158 LYS   B CG  
6457 C  CG  B LYS   B 158 ? 0.2519 0.2507 0.3409 0.0130  0.0039  -0.0620 158 LYS   B CG  
6458 C  CD  A LYS   B 158 ? 0.2561 0.3206 0.3873 0.0132  0.0256  -0.1074 158 LYS   B CD  
6459 C  CD  B LYS   B 158 ? 0.2692 0.2714 0.3552 0.0126  0.0080  -0.0593 158 LYS   B CD  
6460 C  CE  A LYS   B 158 ? 0.2747 0.3497 0.3996 0.0121  0.0222  -0.0995 158 LYS   B CE  
6461 C  CE  B LYS   B 158 ? 0.2826 0.2865 0.3704 0.0132  0.0095  -0.0554 158 LYS   B CE  
6462 N  NZ  A LYS   B 158 ? 0.2759 0.3649 0.4022 0.0065  0.0184  -0.0952 158 LYS   B NZ  
6463 N  NZ  B LYS   B 158 ? 0.2873 0.2933 0.3776 0.0120  0.0102  -0.0533 158 LYS   B NZ  
6490 N  N   A ASN   B 159 ? 0.1734 0.1698 0.4115 0.0092  -0.0239 -0.0700 159 ASN   B N   
6491 N  N   B ASN   B 159 ? 0.1992 0.1979 0.3205 0.0099  -0.0220 -0.0486 159 ASN   B N   
6492 C  CA  A ASN   B 159 ? 0.1896 0.1644 0.4226 0.0171  -0.0428 -0.0517 159 ASN   B CA  
6493 C  CA  B ASN   B 159 ? 0.1989 0.1920 0.3362 0.0133  -0.0313 -0.0423 159 ASN   B CA  
6494 C  C   A ASN   B 159 ? 0.1711 0.1535 0.4146 0.0104  -0.0542 -0.0399 159 ASN   B C   
6495 C  C   B ASN   B 159 ? 0.1801 0.1723 0.3599 0.0123  -0.0397 -0.0388 159 ASN   B C   
6496 O  O   A ASN   B 159 ? 0.1749 0.1452 0.4357 -0.0051 -0.0592 -0.0230 159 ASN   B O   
6497 O  O   B ASN   B 159 ? 0.1813 0.1681 0.3621 0.0103  -0.0371 -0.0329 159 ASN   B O   
6498 C  CB  A ASN   B 159 ? 0.2107 0.1798 0.4408 0.0283  -0.0456 -0.0459 159 ASN   B CB  
6499 C  CB  B ASN   B 159 ? 0.2104 0.2046 0.3342 0.0170  -0.0325 -0.0371 159 ASN   B CB  
6500 C  CG  A ASN   B 159 ? 0.2408 0.2023 0.4616 0.0255  -0.0518 -0.0583 159 ASN   B CG  
6501 C  CG  B ASN   B 159 ? 0.2250 0.2186 0.3405 0.0179  -0.0345 -0.0377 159 ASN   B CG  
6502 O  OD1 A ASN   B 159 ? 0.2573 0.2070 0.4694 0.0297  -0.0471 -0.0688 159 ASN   B OD1 
6503 O  OD1 B ASN   B 159 ? 0.2314 0.2238 0.3426 0.0214  -0.0327 -0.0373 159 ASN   B OD1 
6504 N  ND2 A ASN   B 159 ? 0.2464 0.2148 0.4747 0.0253  -0.0558 -0.0551 159 ASN   B ND2 
6505 N  ND2 B ASN   B 159 ? 0.2296 0.2252 0.3476 0.0195  -0.0355 -0.0358 159 ASN   B ND2 
6518 N  N   . LEU   B 160 ? 0.1630 0.1581 0.3850 0.0099  -0.0454 -0.0351 160 LEU   B N   
6519 C  CA  . LEU   B 160 ? 0.1583 0.1571 0.3636 0.0131  -0.0388 -0.0249 160 LEU   B CA  
6520 C  C   . LEU   B 160 ? 0.1521 0.1411 0.3531 0.0020  -0.0260 -0.0318 160 LEU   B C   
6521 O  O   . LEU   B 160 ? 0.1439 0.1450 0.3422 -0.0013 -0.0288 -0.0183 160 LEU   B O   
6522 C  CB  . LEU   B 160 ? 0.1549 0.1659 0.3456 0.0037  -0.0324 -0.0065 160 LEU   B CB  
6523 C  CG  . LEU   B 160 ? 0.1554 0.1804 0.3192 0.0061  -0.0322 0.0034  160 LEU   B CG  
6524 C  CD1 . LEU   B 160 ? 0.1692 0.1988 0.3184 -0.0061 -0.0142 0.0061  160 LEU   B CD1 
6525 C  CD2 . LEU   B 160 ? 0.1614 0.1838 0.3231 0.0211  -0.0301 -0.0110 160 LEU   B CD2 
6538 N  N   . TYR   B 161 ? 0.1498 0.1511 0.3558 -0.0062 -0.0031 -0.0434 161 TYR   B N   
6539 C  CA  . TYR   B 161 ? 0.1608 0.1508 0.3474 -0.0127 0.0096  -0.0449 161 TYR   B CA  
6540 C  C   . TYR   B 161 ? 0.1641 0.1452 0.3356 -0.0130 0.0116  -0.0397 161 TYR   B C   
6541 O  O   . TYR   B 161 ? 0.1653 0.1437 0.3296 -0.0195 0.0020  -0.0368 161 TYR   B O   
6542 C  CB  . TYR   B 161 ? 0.1726 0.1609 0.3406 -0.0240 0.0257  -0.0547 161 TYR   B CB  
6543 C  CG  . TYR   B 161 ? 0.1972 0.1611 0.3293 -0.0263 0.0356  -0.0651 161 TYR   B CG  
6544 C  CD1 . TYR   B 161 ? 0.2027 0.1617 0.3264 -0.0393 0.0366  -0.0641 161 TYR   B CD1 
6545 C  CD2 . TYR   B 161 ? 0.2165 0.1688 0.3205 -0.0244 0.0342  -0.0625 161 TYR   B CD2 
6546 C  CE1 . TYR   B 161 ? 0.2211 0.1858 0.3312 -0.0424 0.0363  -0.0574 161 TYR   B CE1 
6547 C  CE2 . TYR   B 161 ? 0.2354 0.1888 0.3293 -0.0320 0.0351  -0.0590 161 TYR   B CE2 
6548 C  CZ  . TYR   B 161 ? 0.2361 0.1929 0.3248 -0.0497 0.0246  -0.0538 161 TYR   B CZ  
6549 O  OH  . TYR   B 161 ? 0.2656 0.2184 0.3450 -0.0471 0.0269  -0.0504 161 TYR   B OH  
6559 N  N   . ASP   B 162 ? 0.1715 0.1474 0.3538 -0.0103 0.0002  -0.0563 162 ASP   B N   
6560 C  CA  . ASP   B 162 ? 0.1794 0.1542 0.3559 -0.0030 -0.0028 -0.0544 162 ASP   B CA  
6561 C  C   . ASP   B 162 ? 0.1739 0.1460 0.3434 -0.0107 -0.0065 -0.0480 162 ASP   B C   
6562 O  O   . ASP   B 162 ? 0.1816 0.1507 0.3495 -0.0215 -0.0178 -0.0328 162 ASP   B O   
6563 C  CB  . ASP   B 162 ? 0.1990 0.1714 0.3756 -0.0019 -0.0100 -0.0729 162 ASP   B CB  
6564 C  CG  . ASP   B 162 ? 0.2049 0.1942 0.3989 0.0078  -0.0142 -0.0926 162 ASP   B CG  
6565 O  OD1 . ASP   B 162 ? 0.2055 0.2155 0.3948 -0.0005 0.0035  -0.0824 162 ASP   B OD1 
6566 O  OD2 . ASP   B 162 ? 0.2159 0.2150 0.4279 0.0277  -0.0106 -0.0879 162 ASP   B OD2 
6571 N  N   . LYS   B 163 ? 0.1725 0.1351 0.3394 -0.0044 -0.0229 -0.0313 163 LYS   B N   
6572 C  CA  . LYS   B 163 ? 0.1869 0.1462 0.3416 -0.0132 -0.0184 -0.0083 163 LYS   B CA  
6573 C  C   . LYS   B 163 ? 0.1542 0.1447 0.3295 -0.0162 -0.0194 -0.0025 163 LYS   B C   
6574 O  O   . LYS   B 163 ? 0.1504 0.1489 0.3479 -0.0208 -0.0176 -0.0015 163 LYS   B O   
6575 C  CB  . LYS   B 163 ? 0.2375 0.1805 0.3801 -0.0097 -0.0252 0.0127  163 LYS   B CB  
6576 C  CG  . LYS   B 163 ? 0.3213 0.2644 0.4421 -0.0142 -0.0095 0.0181  163 LYS   B CG  
6577 C  CD  . LYS   B 163 ? 0.3880 0.3459 0.5056 -0.0218 -0.0064 0.0134  163 LYS   B CD  
6578 C  CE  . LYS   B 163 ? 0.4408 0.4034 0.5499 -0.0272 -0.0022 0.0136  163 LYS   B CE  
6579 N  NZ  . LYS   B 163 ? 0.4731 0.4609 0.5780 -0.0301 -0.0007 0.0097  163 LYS   B NZ  
6593 N  N   . LEU   B 164 ? 0.1442 0.1343 0.2987 -0.0155 -0.0149 -0.0048 164 LEU   B N   
6594 C  CA  . LEU   B 164 ? 0.1492 0.1365 0.2837 -0.0098 -0.0234 -0.0041 164 LEU   B CA  
6595 C  C   . LEU   B 164 ? 0.1539 0.1340 0.2845 -0.0161 -0.0252 0.0005  164 LEU   B C   
6596 O  O   . LEU   B 164 ? 0.1563 0.1549 0.3022 -0.0157 -0.0254 0.0007  164 LEU   B O   
6597 C  CB  . LEU   B 164 ? 0.1472 0.1319 0.2725 -0.0122 -0.0247 -0.0084 164 LEU   B CB  
6598 C  CG  . LEU   B 164 ? 0.1546 0.1472 0.2763 -0.0105 -0.0121 0.0006  164 LEU   B CG  
6599 C  CD1 . LEU   B 164 ? 0.1545 0.1495 0.2669 -0.0160 -0.0183 -0.0078 164 LEU   B CD1 
6600 C  CD2 . LEU   B 164 ? 0.1738 0.1826 0.2958 -0.0096 0.0093  -0.0170 164 LEU   B CD2 
6612 N  N   . VAL   B 165 ? 0.1842 0.1440 0.2988 -0.0243 -0.0365 -0.0072 165 VAL   B N   
6613 C  CA  . VAL   B 165 ? 0.2248 0.1556 0.3105 -0.0345 -0.0584 -0.0051 165 VAL   B CA  
6614 C  C   . VAL   B 165 ? 0.2558 0.1641 0.3489 -0.0433 -0.0863 -0.0027 165 VAL   B C   
6615 O  O   . VAL   B 165 ? 0.2776 0.1858 0.3612 -0.0480 -0.0959 0.0041  165 VAL   B O   
6616 C  CB  . VAL   B 165 ? 0.2463 0.1732 0.3071 -0.0134 -0.0312 -0.0190 165 VAL   B CB  
6617 C  CG1 . VAL   B 165 ? 0.2644 0.1837 0.3307 -0.0122 -0.0202 -0.0114 165 VAL   B CG1 
6618 C  CG2 . VAL   B 165 ? 0.2416 0.1793 0.2932 -0.0075 -0.0170 -0.0140 165 VAL   B CG2 
6628 N  N   . SER   B 166 ? 0.2699 0.1525 0.3777 -0.0425 -0.0953 -0.0258 166 SER   B N   
6629 C  CA  . SER   B 166 ? 0.2640 0.1552 0.4221 -0.0382 -0.0789 -0.0335 166 SER   B CA  
6630 C  C   . SER   B 166 ? 0.2445 0.1679 0.4420 -0.0432 -0.0764 -0.0082 166 SER   B C   
6631 O  O   . SER   B 166 ? 0.2475 0.1895 0.4731 -0.0566 -0.0891 -0.0343 166 SER   B O   
6632 C  CB  . SER   B 166 ? 0.2649 0.1734 0.4502 -0.0254 -0.0731 -0.0365 166 SER   B CB  
6633 O  OG  . SER   B 166 ? 0.2541 0.1746 0.4654 -0.0219 -0.0772 -0.0232 166 SER   B OG  
6639 N  N   . SER   B 167 ? 0.2226 0.1605 0.4150 -0.0431 -0.0802 0.0309  167 SER   B N   
6640 C  CA  . SER   B 167 ? 0.2172 0.1715 0.3951 -0.0406 -0.0607 0.0313  167 SER   B CA  
6641 C  C   . SER   B 167 ? 0.2108 0.1817 0.3758 -0.0562 -0.0576 0.0491  167 SER   B C   
6642 O  O   . SER   B 167 ? 0.2100 0.1972 0.3792 -0.0630 -0.0560 0.0493  167 SER   B O   
6643 C  CB  . SER   B 167 ? 0.2062 0.1780 0.3867 -0.0364 -0.0258 0.0341  167 SER   B CB  
6644 O  OG  . SER   B 167 ? 0.1998 0.1889 0.3721 -0.0276 -0.0086 0.0359  167 SER   B OG  
6650 N  N   . PHE   B 168 ? 0.2068 0.1805 0.3629 -0.0505 -0.0396 0.0533  168 PHE   B N   
6651 C  CA  . PHE   B 168 ? 0.2094 0.1746 0.3325 -0.0529 -0.0317 0.0288  168 PHE   B CA  
6652 C  C   . PHE   B 168 ? 0.1786 0.1580 0.2839 -0.0316 -0.0152 0.0124  168 PHE   B C   
6653 O  O   . PHE   B 168 ? 0.2107 0.1505 0.2822 -0.0008 -0.0123 -0.0007 168 PHE   B O   
6654 C  CB  . PHE   B 168 ? 0.2261 0.1811 0.3357 -0.0549 -0.0440 0.0394  168 PHE   B CB  
6655 C  CG  . PHE   B 168 ? 0.2475 0.1667 0.3196 -0.0559 -0.0460 0.0154  168 PHE   B CG  
6656 C  CD1 . PHE   B 168 ? 0.2762 0.1723 0.3258 -0.0509 -0.0524 0.0148  168 PHE   B CD1 
6657 C  CD2 . PHE   B 168 ? 0.2312 0.1586 0.3101 -0.0543 -0.0411 0.0160  168 PHE   B CD2 
6658 C  CE1 . PHE   B 168 ? 0.2873 0.1813 0.3156 -0.0404 -0.0398 0.0258  168 PHE   B CE1 
6659 C  CE2 . PHE   B 168 ? 0.2646 0.1684 0.3211 -0.0387 -0.0412 0.0109  168 PHE   B CE2 
6660 C  CZ  . PHE   B 168 ? 0.2777 0.1640 0.3157 -0.0288 -0.0447 0.0299  168 PHE   B CZ  
6670 N  N   . LEU   B 169 ? 0.1851 0.1675 0.2785 -0.0034 -0.0057 -0.0023 169 LEU   B N   
6671 C  CA  . LEU   B 169 ? 0.2078 0.1966 0.3078 -0.0067 0.0026  -0.0276 169 LEU   B CA  
6672 C  C   . LEU   B 169 ? 0.2392 0.2285 0.3593 0.0061  0.0026  -0.0514 169 LEU   B C   
6673 O  O   . LEU   B 169 ? 0.2622 0.2514 0.4113 -0.0032 0.0017  -0.0646 169 LEU   B O   
6674 C  CB  . LEU   B 169 ? 0.2270 0.2386 0.3181 -0.0152 0.0004  0.0028  169 LEU   B CB  
6675 C  CG  . LEU   B 169 ? 0.2663 0.2764 0.3538 -0.0034 0.0023  0.0067  169 LEU   B CG  
6676 C  CD1 . LEU   B 169 ? 0.2804 0.2924 0.3553 -0.0048 -0.0040 0.0234  169 LEU   B CD1 
6677 C  CD2 . LEU   B 169 ? 0.2573 0.2838 0.3509 0.0153  0.0220  -0.0062 169 LEU   B CD2 
6678 O  OXT . LEU   B 169 ? 0.2588 0.2485 0.3530 0.0390  0.0139  -0.0551 169 LEU   B OXT 
6690 C  C1  T TFA   C .   ? 0.1573 0.1774 0.1494 -0.0134 0.0202  0.0119  201 TFA   A C1  
6691 C  C2  T TFA   C .   ? 0.1829 0.1920 0.1887 -0.0214 0.0079  -0.0056 201 TFA   A C2  
6692 O  O   T TFA   C .   ? 0.1324 0.1580 0.1156 -0.0198 0.0213  0.0166  201 TFA   A O   
6693 F  F1  T TFA   C .   ? 0.1982 0.1992 0.2168 -0.0151 -0.0088 -0.0128 201 TFA   A F1  
6694 F  F2  T TFA   C .   ? 0.1864 0.1991 0.1945 -0.0205 0.0015  0.0026  201 TFA   A F2  
6695 F  F3  T TFA   C .   ? 0.1942 0.1993 0.2036 -0.0369 0.0277  -0.0125 201 TFA   A F3  
6696 O  OXT T TFA   C .   ? 0.1623 0.1799 0.1712 0.0063  0.0245  0.0093  201 TFA   A OXT 
6697 N  N2  B A1A8D D .   ? 0.2050 0.1855 0.1824 0.0119  -0.0071 0.0314  202 A1A8D A N2  
6698 C  C3  B A1A8D D .   ? 0.2295 0.2265 0.2478 0.0200  -0.0144 0.0159  202 A1A8D A C3  
6699 C  C6  B A1A8D D .   ? 0.1965 0.1790 0.1810 0.0050  -0.0071 0.0385  202 A1A8D A C6  
6700 C  C9  B A1A8D D .   ? 0.1440 0.1770 0.1342 0.0305  0.0182  0.0487  202 A1A8D A C9  
6701 C  C1  B A1A8D D .   ? 0.2386 0.2355 0.2534 0.0295  -0.0122 0.0214  202 A1A8D A C1  
6702 C  C10 B A1A8D D .   ? 0.1231 0.1666 0.1526 0.0160  0.0024  0.0511  202 A1A8D A C10 
6703 C  C2  B A1A8D D .   ? 0.2370 0.2337 0.2566 0.0241  -0.0156 0.0159  202 A1A8D A C2  
6704 C  C4  B A1A8D D .   ? 0.2304 0.2307 0.2656 0.0165  -0.0138 0.0105  202 A1A8D A C4  
6705 C  C5  B A1A8D D .   ? 0.2015 0.1936 0.1806 0.0167  -0.0108 0.0312  202 A1A8D A C5  
6706 C  C7  B A1A8D D .   ? 0.1582 0.1587 0.1496 0.0128  -0.0036 0.0458  202 A1A8D A C7  
6707 C  C8  B A1A8D D .   ? 0.1668 0.1759 0.1467 0.0226  0.0005  0.0450  202 A1A8D A C8  
6708 N  N1  B A1A8D D .   ? 0.2226 0.2132 0.2186 0.0206  -0.0177 0.0225  202 A1A8D A N1  
6709 N  N3  B A1A8D D .   ? 0.1802 0.1693 0.1633 0.0057  -0.0052 0.0422  202 A1A8D A N3  
6710 N  N4  B A1A8D D .   ? 0.1267 0.1448 0.1366 0.0119  -0.0039 0.0541  202 A1A8D A N4  
6711 O  O1  B A1A8D D .   ? 0.2401 0.2351 0.2689 0.0214  -0.0172 0.0146  202 A1A8D A O1  
6712 O  O2  B A1A8D D .   ? 0.2281 0.2308 0.2731 0.0145  -0.0140 0.0098  202 A1A8D A O2  
6727 CL CL  B CL    E .   ? 0.1764 0.1669 0.2905 -0.0152 -0.0064 -0.0300 203 CL    A CL  
6728 O  O   . HOH   F .   ? 0.1596 0.4247 0.2478 -0.0091 0.0320  0.0559  301 HOH   A O   
6729 O  O   . HOH   F .   ? 0.4055 0.7385 0.4825 -0.1185 0.0211  0.0754  302 HOH   A O   
6730 O  O   . HOH   F .   ? 0.2845 0.2800 0.4671 -0.0277 -0.1026 0.1316  303 HOH   A O   
6731 O  O   . HOH   F .   ? 0.7693 0.5791 0.3869 -0.1498 0.0019  0.1983  304 HOH   A O   
6732 O  O   . HOH   F .   ? 0.7478 0.6166 0.5257 -0.1168 0.0537  0.2201  305 HOH   A O   
6733 O  O   A HOH   F .   ? 0.2664 0.2187 0.3591 -0.0193 -0.0224 0.0474  306 HOH   A O   
6734 O  O   . HOH   F .   ? 0.5888 0.5074 0.3542 0.2144  -0.1308 0.0588  307 HOH   A O   
6735 O  O   . HOH   F .   ? 0.3049 0.6342 0.5466 -0.0460 -0.0671 0.1848  308 HOH   A O   
6736 O  O   . HOH   F .   ? 0.5617 0.6200 0.4948 -0.1328 -0.1062 -0.1045 309 HOH   A O   
6737 O  O   . HOH   F .   ? 0.4817 0.3792 0.5327 0.1029  0.1513  -0.1158 310 HOH   A O   
6738 O  O   . HOH   F .   ? 0.3176 0.3528 0.1853 -0.0404 0.0565  0.0477  311 HOH   A O   
6739 O  O   . HOH   F .   ? 0.5755 0.4320 0.5500 -0.0763 0.1620  0.1333  312 HOH   A O   
6740 O  O   B HOH   F .   ? 0.1778 0.2261 0.2268 -0.0197 -0.0406 -0.0390 313 HOH   A O   
6741 O  O   . HOH   F .   ? 0.3029 0.6282 0.3757 -0.0034 -0.0454 0.0766  314 HOH   A O   
6742 O  O   . HOH   F .   ? 0.5990 0.5501 0.3918 -0.0439 -0.0257 0.1242  315 HOH   A O   
6743 O  O   B HOH   F .   ? 0.3824 0.2651 0.2696 0.0897  -0.0768 0.0332  316 HOH   A O   
6744 O  O   . HOH   F .   ? 0.5373 0.1931 0.5311 0.0543  0.0168  0.0040  317 HOH   A O   
6745 O  O   . HOH   F .   ? 0.3575 0.3312 0.3077 -0.1343 0.0088  0.0819  318 HOH   A O   
6746 O  O   . HOH   F .   ? 0.2096 0.1829 0.3907 -0.0465 0.0036  -0.0267 319 HOH   A O   
6747 O  O   B HOH   F .   ? 0.3944 0.5446 0.3758 0.0606  -0.0044 0.0533  320 HOH   A O   
6748 O  O   . HOH   F .   ? 0.4975 0.2668 0.2944 -0.0977 0.0177  0.0487  321 HOH   A O   
6749 O  O   . HOH   F .   ? 0.1757 0.3681 0.3117 0.0498  -0.0085 0.0112  322 HOH   A O   
6750 O  O   . HOH   F .   ? 0.3926 0.4139 0.3935 -0.0646 0.1777  0.0460  323 HOH   A O   
6751 O  O   . HOH   F .   ? 0.5491 0.3415 0.3396 -0.0941 -0.0994 0.0158  324 HOH   A O   
6752 O  O   . HOH   F .   ? 0.2094 0.1676 0.1707 -0.0112 0.0234  0.0221  325 HOH   A O   
6753 O  O   . HOH   F .   ? 0.6600 0.4522 0.4620 -0.0783 0.1520  0.1887  326 HOH   A O   
6754 O  O   . HOH   F .   ? 0.4469 0.5104 0.5507 0.1773  0.0899  -0.0932 327 HOH   A O   
6755 O  O   . HOH   F .   ? 0.2190 0.1794 0.2687 -0.0148 -0.0525 -0.0047 328 HOH   A O   
6756 O  O   . HOH   F .   ? 0.4559 0.3584 0.4967 -0.0161 0.1294  -0.0304 329 HOH   A O   
6757 O  O   . HOH   F .   ? 0.2003 0.3605 0.4393 -0.0398 0.0428  -0.1204 330 HOH   A O   
6758 O  O   . HOH   F .   ? 0.1772 0.1675 0.2153 0.0167  -0.0270 0.0255  331 HOH   A O   
6759 O  O   . HOH   F .   ? 0.1529 0.1953 0.2788 0.0082  -0.0325 -0.0670 332 HOH   A O   
6760 O  O   . HOH   F .   ? 0.1675 0.1727 0.2437 -0.0173 0.0127  0.0403  333 HOH   A O   
6761 O  O   . HOH   F .   ? 0.3491 0.4484 0.2740 -0.0385 0.0523  0.0233  334 HOH   A O   
6762 O  O   . HOH   F .   ? 0.2253 0.4513 0.3978 -0.0468 -0.0747 0.1833  335 HOH   A O   
6763 O  O   A HOH   F .   ? 0.2109 0.2328 0.2663 -0.0323 0.0507  0.0545  336 HOH   A O   
6764 O  O   . HOH   F .   ? 0.1546 0.1567 0.2472 -0.0215 0.0086  0.0110  337 HOH   A O   
6765 O  O   A HOH   F .   ? 0.1623 0.2100 0.2307 0.0362  0.0390  0.0512  338 HOH   A O   
6766 O  O   . HOH   F .   ? 0.2951 0.5425 0.6866 0.0673  0.1034  0.0583  339 HOH   A O   
6767 O  O   . HOH   F .   ? 0.5099 0.6336 0.4028 0.0667  0.0211  -0.0932 340 HOH   A O   
6768 O  O   . HOH   F .   ? 0.2484 0.2207 0.3170 0.0368  0.0393  0.0532  341 HOH   A O   
6769 O  O   A HOH   F .   ? 0.2436 0.4180 0.2582 0.1128  0.0343  -0.0294 342 HOH   A O   
6770 O  O   . HOH   F .   ? 0.1525 0.2209 0.2369 -0.0021 -0.0104 0.0678  343 HOH   A O   
6771 O  O   . HOH   F .   ? 0.4576 0.1973 0.4678 0.0093  -0.1797 0.0464  344 HOH   A O   
6772 O  O   . HOH   F .   ? 0.5372 0.4171 0.4909 -0.1857 -0.0705 0.2175  345 HOH   A O   
6773 O  O   . HOH   F .   ? 0.2574 0.2084 0.2684 -0.0189 0.0169  -0.0122 346 HOH   A O   
6774 O  O   . HOH   F .   ? 0.5268 0.5355 0.2892 -0.1288 0.1397  0.0959  347 HOH   A O   
6775 O  O   . HOH   F .   ? 0.2531 0.3633 0.3636 -0.0657 -0.0361 -0.0384 348 HOH   A O   
6776 O  O   . HOH   F .   ? 0.2425 0.4102 0.3721 0.0993  -0.0775 -0.0139 349 HOH   A O   
6777 O  O   A HOH   F .   ? 0.2258 0.3256 0.3957 -0.0014 0.0918  0.1606  350 HOH   A O   
6778 O  O   . HOH   F .   ? 0.3284 0.3002 0.3797 -0.0863 0.0104  -0.0322 351 HOH   A O   
6779 O  O   . HOH   F .   ? 0.1992 0.1688 0.2462 0.0243  -0.0211 0.0024  352 HOH   A O   
6780 O  O   . HOH   F .   ? 0.5656 0.5607 0.4844 0.0422  0.2012  -0.0857 353 HOH   A O   
6781 O  O   . HOH   F .   ? 0.1986 0.1977 0.4123 0.0113  0.1050  -0.0131 354 HOH   A O   
6782 O  O   . HOH   F .   ? 0.5961 0.4065 0.3350 0.0459  0.0175  0.1491  355 HOH   A O   
6783 O  O   . HOH   F .   ? 0.5255 0.6380 0.3915 0.2261  -0.0153 -0.0293 356 HOH   A O   
6784 O  O   . HOH   F .   ? 0.3678 0.3962 0.4219 0.1672  0.0756  0.0461  357 HOH   A O   
6785 O  O   . HOH   F .   ? 0.3097 0.3758 0.2325 -0.0905 -0.0173 -0.0728 358 HOH   A O   
6786 O  O   . HOH   F .   ? 0.1330 0.1298 0.1420 -0.0053 0.0146  0.0101  359 HOH   A O   
6787 O  O   . HOH   F .   ? 0.4615 0.3458 0.2607 -0.0723 0.0253  0.0159  360 HOH   A O   
6788 O  O   . HOH   F .   ? 0.2632 0.4102 0.3465 -0.0406 0.0669  0.0020  361 HOH   A O   
6789 O  O   . HOH   F .   ? 0.6500 0.5392 0.6036 -0.0067 -0.1012 -0.0106 362 HOH   A O   
6790 O  O   . HOH   F .   ? 0.1476 0.2010 0.2548 0.0077  -0.0091 0.0157  363 HOH   A O   
6791 O  O   . HOH   F .   ? 0.1477 0.1530 0.1592 -0.0052 -0.0167 -0.0041 364 HOH   A O   
6792 O  O   . HOH   F .   ? 0.2755 0.3234 0.5115 -0.0505 -0.0902 -0.0806 365 HOH   A O   
6793 O  O   A HOH   F .   ? 0.5930 0.3049 0.4769 -0.0603 -0.1176 0.0714  366 HOH   A O   
6794 O  O   . HOH   F .   ? 0.1745 0.2328 0.1978 -0.0185 -0.0014 0.0738  367 HOH   A O   
6795 O  O   . HOH   F .   ? 0.1860 0.1942 0.2543 -0.0342 0.0082  0.0295  368 HOH   A O   
6796 O  O   B HOH   F .   ? 0.3014 0.3859 0.1852 -0.0499 -0.0048 -0.0111 369 HOH   A O   
6797 O  O   . HOH   F .   ? 0.4580 0.2628 0.4211 -0.1513 0.1568  -0.0458 370 HOH   A O   
6798 O  O   . HOH   F .   ? 0.3874 0.6917 0.4808 -0.0754 -0.1451 0.0721  371 HOH   A O   
6799 O  O   . HOH   F .   ? 0.3943 0.5354 0.5666 0.0798  -0.0223 0.1525  372 HOH   A O   
6800 O  O   . HOH   F .   ? 0.1573 0.1375 0.2423 -0.0124 0.0235  -0.0090 373 HOH   A O   
6801 O  O   . HOH   F .   ? 0.3565 0.6538 0.3846 -0.0726 0.0219  0.1281  374 HOH   A O   
6802 O  O   . HOH   F .   ? 0.2722 0.4385 0.3296 0.0725  0.0878  0.1841  375 HOH   A O   
6803 O  O   . HOH   F .   ? 0.2906 0.4034 0.3287 -0.0686 -0.0470 0.0937  376 HOH   A O   
6804 O  O   A HOH   F .   ? 0.2441 0.3305 0.3251 0.1098  0.0282  0.1502  377 HOH   A O   
6805 O  O   . HOH   F .   ? 0.3057 0.3463 0.3690 -0.1341 0.0986  -0.0277 378 HOH   A O   
6806 O  O   . HOH   F .   ? 0.2064 0.2756 0.3588 0.0333  0.0815  -0.0544 379 HOH   A O   
6807 O  O   . HOH   F .   ? 0.4118 0.2470 0.4519 -0.1269 0.0820  0.0304  380 HOH   A O   
6808 O  O   T HOH   F .   ? 0.1384 0.1209 0.2766 -0.0252 0.0235  0.0396  381 HOH   A O   
6809 O  O   . HOH   F .   ? 0.3460 0.3567 0.2421 -0.0641 -0.0955 0.0495  382 HOH   A O   
6810 O  O   . HOH   F .   ? 0.3902 0.2155 0.2540 0.1116  0.0569  0.0234  383 HOH   A O   
6811 O  O   . HOH   F .   ? 0.3300 0.2684 0.3352 -0.0135 -0.0268 0.0880  384 HOH   A O   
6812 O  O   . HOH   F .   ? 0.1989 0.2357 0.2426 -0.0302 -0.0432 0.0497  385 HOH   A O   
6813 O  O   A HOH   F .   ? 0.3666 0.1618 0.2171 0.0246  0.0302  0.0013  386 HOH   A O   
6814 O  O   . HOH   F .   ? 0.3156 0.3543 0.4405 -0.0473 0.1430  -0.0065 387 HOH   A O   
6815 O  O   . HOH   F .   ? 0.1885 0.1862 0.1845 0.0040  0.0099  0.0184  388 HOH   A O   
6816 O  O   . HOH   F .   ? 0.5977 0.5498 0.6425 -0.1056 -0.0246 0.1234  389 HOH   A O   
6817 O  O   . HOH   F .   ? 0.3071 0.3113 0.2149 0.0182  0.0702  0.0105  390 HOH   A O   
6818 O  O   . HOH   F .   ? 0.5326 0.5958 0.5450 0.0316  0.0989  -0.0517 391 HOH   A O   
6819 O  O   . HOH   F .   ? 0.3212 0.2476 0.5095 -0.0613 -0.0328 0.0131  392 HOH   A O   
6820 O  O   . HOH   F .   ? 0.1969 0.2209 0.2871 -0.0168 -0.0226 0.0923  393 HOH   A O   
6821 O  O   B HOH   F .   ? 0.2185 0.2928 0.1707 0.1375  0.0440  0.0806  394 HOH   A O   
6822 O  O   . HOH   F .   ? 0.1446 0.1762 0.1851 0.0081  -0.0264 -0.0283 395 HOH   A O   
6823 O  O   . HOH   F .   ? 0.2625 0.2097 0.1902 -0.0609 0.0070  0.0393  396 HOH   A O   
6824 O  O   . HOH   F .   ? 0.1887 0.1850 0.3883 0.0352  0.1020  0.0947  397 HOH   A O   
6825 O  O   . HOH   F .   ? 0.2972 0.6604 0.3785 0.1279  0.0528  -0.0644 398 HOH   A O   
6826 O  O   . HOH   F .   ? 0.3204 0.2667 0.2378 -0.0680 -0.1062 0.0313  399 HOH   A O   
6827 O  O   . HOH   F .   ? 0.2535 0.4200 0.3570 -0.0252 0.0971  -0.0858 400 HOH   A O   
6828 O  O   . HOH   F .   ? 0.5183 0.4553 0.2059 0.0091  0.1030  0.0876  401 HOH   A O   
6829 O  O   . HOH   F .   ? 0.1659 0.1676 0.2295 0.0015  -0.0303 0.0009  402 HOH   A O   
6830 O  O   . HOH   F .   ? 0.2216 0.1789 0.3023 0.0059  -0.0287 0.0042  403 HOH   A O   
6831 O  O   A HOH   F .   ? 0.2705 0.2201 0.3628 -0.0528 0.0665  -0.0302 404 HOH   A O   
6832 O  O   . HOH   F .   ? 0.2050 0.2153 0.3773 -0.0001 -0.0644 0.0444  405 HOH   A O   
6833 O  O   . HOH   F .   ? 0.1351 0.1479 0.1946 -0.0008 -0.0196 0.0064  406 HOH   A O   
6834 O  O   . HOH   F .   ? 0.2504 0.2928 0.3581 -0.0047 -0.0179 -0.0727 407 HOH   A O   
6835 O  O   . HOH   F .   ? 0.1907 0.2740 0.4058 -0.0040 -0.0173 0.0158  408 HOH   A O   
6836 O  O   . HOH   F .   ? 0.6012 0.3378 0.4822 0.1364  -0.0143 -0.0153 409 HOH   A O   
6837 O  O   . HOH   F .   ? 0.9176 0.9433 0.8074 0.0108  0.0127  -0.0244 410 HOH   A O   
6838 O  O   A HOH   F .   ? 0.2198 0.2093 0.2486 -0.0031 0.0023  0.0510  411 HOH   A O   
6839 O  O   . HOH   F .   ? 0.2823 0.3596 0.7009 -0.0282 0.0864  -0.0447 412 HOH   A O   
6840 O  O   . HOH   F .   ? 0.1708 0.1419 0.1718 -0.0239 0.0154  0.0029  413 HOH   A O   
6841 O  O   . HOH   F .   ? 0.2477 0.1855 0.2901 -0.0043 0.0205  0.0345  414 HOH   A O   
6842 O  O   . HOH   F .   ? 0.2514 0.2068 0.2725 -0.0555 -0.0025 0.0576  415 HOH   A O   
6843 O  O   . HOH   F .   ? 0.3962 0.6258 0.5408 0.0872  0.0821  0.0423  416 HOH   A O   
6844 O  O   B HOH   F .   ? 0.1559 0.1083 0.2978 -0.0115 0.0433  -0.0353 417 HOH   A O   
6845 O  O   . HOH   F .   ? 0.1500 0.1671 0.3234 -0.0037 0.0041  0.0265  418 HOH   A O   
6846 O  O   . HOH   F .   ? 0.4375 0.4767 0.3664 0.1723  -0.1090 -0.1671 419 HOH   A O   
6847 O  O   . HOH   F .   ? 0.2479 0.2021 0.3576 0.0200  -0.1041 0.0230  420 HOH   A O   
6848 O  O   . HOH   F .   ? 0.2144 0.2981 0.2718 -0.0220 -0.0529 0.0623  421 HOH   A O   
6849 O  O   . HOH   F .   ? 0.4055 0.2249 0.5707 -0.0781 -0.2277 0.1050  422 HOH   A O   
6850 O  O   . HOH   F .   ? 0.4640 0.6461 0.3531 -0.0772 -0.0009 0.1556  423 HOH   A O   
6851 O  O   . HOH   F .   ? 0.3373 0.1315 0.2222 0.0062  -0.0475 0.0082  424 HOH   A O   
6852 O  O   A HOH   F .   ? 0.1967 0.2271 0.3459 0.0147  -0.0420 -0.0656 425 HOH   A O   
6853 O  O   . HOH   F .   ? 0.2745 0.6208 0.1778 -0.0190 0.0369  0.0262  426 HOH   A O   
6854 O  O   . HOH   F .   ? 0.2312 0.4334 0.2817 0.1556  0.0057  0.0389  427 HOH   A O   
6855 O  O   A HOH   F .   ? 0.2593 0.2809 0.2959 -0.0357 0.0849  -0.0241 428 HOH   A O   
6856 O  O   . HOH   F .   ? 0.3877 0.3287 0.4402 0.1136  0.0532  0.0167  429 HOH   A O   
6857 O  O   . HOH   F .   ? 0.1639 0.2092 0.2861 -0.0175 0.0057  0.0443  430 HOH   A O   
6858 O  O   B HOH   F .   ? 0.1953 0.2570 0.3840 0.0049  0.0052  -0.0263 431 HOH   A O   
6859 O  O   A HOH   F .   ? 0.1546 0.2620 0.3270 -0.0236 0.0725  0.0435  432 HOH   A O   
6860 O  O   . HOH   F .   ? 0.5638 0.7027 0.4592 0.0640  0.2658  -0.0723 433 HOH   A O   
6861 O  O   . HOH   F .   ? 0.6621 0.4259 0.5229 0.2014  -0.0733 0.1603  434 HOH   A O   
6862 O  O   . HOH   F .   ? 0.5896 0.6470 0.6525 -0.1143 -0.0794 -0.0557 435 HOH   A O   
6863 O  O   . HOH   F .   ? 0.1902 0.2159 0.5517 -0.0339 -0.0941 0.0705  436 HOH   A O   
6864 O  O   . HOH   F .   ? 0.5510 0.4521 0.4099 -0.0180 -0.1542 0.0093  437 HOH   A O   
6865 O  O   . HOH   F .   ? 0.6655 0.6132 0.6614 -0.1471 -0.0167 -0.1314 438 HOH   A O   
6866 O  O   . HOH   F .   ? 0.6610 0.6757 0.6116 -0.0911 0.0154  0.0237  439 HOH   A O   
6867 O  O   . HOH   F .   ? 0.3693 0.2870 0.1990 -0.0973 -0.0006 0.0703  440 HOH   A O   
6868 O  O   A HOH   F .   ? 0.1647 0.1810 0.2397 -0.0292 -0.0135 0.0057  441 HOH   A O   
6869 O  O   . HOH   F .   ? 0.2637 0.1636 0.2955 0.0059  0.0076  0.0096  442 HOH   A O   
6870 O  O   B HOH   F .   ? 0.2733 0.3415 0.3327 0.0788  0.0060  0.0054  443 HOH   A O   
6871 O  O   . HOH   F .   ? 0.4101 0.4774 0.5063 -0.0968 -0.0836 -0.1242 444 HOH   A O   
6872 O  O   B HOH   F .   ? 0.3084 0.2047 0.2835 0.0194  -0.0593 0.0754  445 HOH   A O   
6873 O  O   . HOH   F .   ? 0.4075 0.3691 0.3466 0.2196  -0.0463 -0.0412 446 HOH   A O   
6874 O  O   . HOH   F .   ? 0.7713 0.7621 0.6576 0.0979  -0.0891 -0.0190 447 HOH   A O   
6875 O  O   . HOH   F .   ? 0.5879 0.7893 0.4637 0.1884  -0.0937 0.2051  448 HOH   A O   
6876 O  O   A HOH   F .   ? 0.5938 0.4565 0.3867 0.0048  0.1073  0.0880  449 HOH   A O   
6877 O  O   . HOH   F .   ? 0.5516 0.5155 0.6388 0.0750  0.0568  -0.1334 450 HOH   A O   
6878 O  O   . HOH   F .   ? 0.1736 0.1589 0.1778 -0.0067 -0.0163 -0.0177 451 HOH   A O   
6879 O  O   . HOH   F .   ? 0.2198 0.2009 0.2849 0.0149  0.0187  0.0227  452 HOH   A O   
6880 O  O   A HOH   F .   ? 0.2867 0.3161 0.4895 0.0053  0.1243  -0.1095 453 HOH   A O   
6881 O  O   . HOH   F .   ? 0.2147 0.2815 0.2750 -0.0072 -0.0095 -0.0563 454 HOH   A O   
6882 O  O   . HOH   F .   ? 0.6877 0.5321 0.5397 0.0216  0.0941  0.2613  455 HOH   A O   
6883 O  O   . HOH   F .   ? 0.6758 0.5482 0.7727 0.0623  -0.1104 0.1844  456 HOH   A O   
6884 O  O   B HOH   F .   ? 0.3183 0.1850 0.2138 -0.0363 0.0172  0.0491  457 HOH   A O   
6885 O  O   . HOH   F .   ? 0.5747 0.4182 0.3800 0.0441  0.0357  0.0120  458 HOH   A O   
6886 O  O   . HOH   F .   ? 0.3948 0.4941 0.4918 0.0946  -0.0245 0.1012  459 HOH   A O   
6887 O  O   . HOH   F .   ? 0.3125 0.3910 0.3379 0.1337  -0.0191 0.0653  460 HOH   A O   
6888 O  O   . HOH   F .   ? 0.3996 0.3538 0.4326 0.0321  0.0786  0.0493  461 HOH   A O   
6889 O  O   . HOH   F .   ? 0.6271 0.6292 0.4920 -0.0788 0.0974  0.0989  462 HOH   A O   
6890 O  O   . HOH   F .   ? 0.2839 0.2757 0.3729 -0.0507 0.0339  -0.0815 463 HOH   A O   
6891 O  O   . HOH   F .   ? 0.7315 0.7084 0.4889 0.0438  -0.0855 -0.0296 464 HOH   A O   
6892 O  O   . HOH   F .   ? 0.3266 0.4693 0.5339 -0.1535 0.1235  -0.1769 465 HOH   A O   
6893 O  O   . HOH   F .   ? 0.3778 0.4954 0.4681 0.0674  -0.0601 0.1317  466 HOH   A O   
6894 O  O   . HOH   F .   ? 0.2771 0.2627 0.3696 -0.0894 0.0450  -0.0249 467 HOH   A O   
6895 O  O   . HOH   F .   ? 0.3224 0.4596 0.4137 -0.0731 -0.0071 -0.0142 468 HOH   A O   
6896 O  O   B HOH   F .   ? 0.2770 0.2470 0.2908 0.0837  0.0949  0.0069  469 HOH   A O   
6897 O  O   . HOH   F .   ? 0.7113 0.3535 0.7403 0.0552  0.0745  0.2414  470 HOH   A O   
6898 O  O   . HOH   F .   ? 0.2777 0.4211 0.5227 0.0329  0.0257  -0.1652 471 HOH   A O   
6899 O  O   . HOH   F .   ? 0.4022 0.6434 0.3959 -0.1047 -0.1049 0.2266  472 HOH   A O   
6900 O  O   . HOH   F .   ? 0.7229 0.6509 0.6882 0.0761  0.1841  0.2315  473 HOH   A O   
6901 O  O   A HOH   F .   ? 0.2942 0.2599 0.5494 0.0855  -0.1942 -0.0931 474 HOH   A O   
6902 O  O   . HOH   F .   ? 0.2715 0.1824 0.2526 0.0295  -0.0760 -0.0252 475 HOH   A O   
6903 O  O   . HOH   F .   ? 0.4039 0.5094 0.3629 0.0274  -0.0548 -0.0495 476 HOH   A O   
6904 O  O   . HOH   F .   ? 0.5192 0.4873 0.4813 0.0060  0.0695  0.0387  477 HOH   A O   
6905 O  O   . HOH   F .   ? 0.5335 0.5741 0.5067 0.1075  -0.0547 -0.0778 478 HOH   A O   
6906 O  O   . HOH   F .   ? 0.2909 0.2389 0.3871 0.0172  0.0742  -0.0017 479 HOH   A O   
6907 O  O   . HOH   F .   ? 0.4973 0.2633 0.3552 -0.0576 -0.1301 0.0695  480 HOH   A O   
6908 O  O   . HOH   F .   ? 0.4532 0.4552 0.5145 -0.1934 -0.0503 -0.0019 481 HOH   A O   
6909 O  O   . HOH   F .   ? 0.4617 0.4273 0.3657 -0.0214 -0.0617 -0.0278 482 HOH   A O   
6910 O  O   . HOH   F .   ? 0.4181 0.4769 0.2892 0.0106  -0.0014 -0.0074 483 HOH   A O   
6911 O  O   . HOH   F .   ? 0.5518 0.6001 0.5694 -0.1626 -0.1366 0.0212  484 HOH   A O   
6912 O  O   . HOH   F .   ? 0.5861 0.4518 0.4415 -0.0312 -0.0020 -0.1224 485 HOH   A O   
6913 O  O   . HOH   F .   ? 0.6826 0.6064 0.6906 -0.0375 0.0345  -0.0466 486 HOH   A O   
6914 O  O   B HOH   F .   ? 0.1800 0.1866 0.3047 0.0321  -0.0127 0.0767  487 HOH   A O   
6915 O  O   . HOH   F .   ? 0.3108 0.4507 0.3624 -0.0240 -0.0321 -0.0708 488 HOH   A O   
6916 O  O   . HOH   F .   ? 0.2449 0.2259 0.2639 0.0180  -0.0019 0.0001  489 HOH   A O   
6917 O  O   . HOH   F .   ? 0.7835 0.3905 0.3385 -0.0499 -0.1032 0.0180  490 HOH   A O   
6918 O  O   . HOH   F .   ? 0.6665 0.6746 0.4966 -0.0662 0.1679  0.1104  491 HOH   A O   
6919 O  O   . HOH   F .   ? 0.2924 0.3939 0.4742 0.0038  0.1305  0.0993  492 HOH   A O   
6920 O  O   . HOH   F .   ? 0.2621 0.5499 0.3756 0.1048  0.0954  0.2478  493 HOH   A O   
6921 O  O   . HOH   F .   ? 0.5788 0.3907 0.4697 -0.0170 0.1075  -0.0153 494 HOH   A O   
6922 O  O   . HOH   F .   ? 0.2592 0.2463 0.7094 -0.0033 -0.1299 0.0177  495 HOH   A O   
6923 O  O   . HOH   F .   ? 0.4582 0.3933 0.2863 -0.1092 0.1435  -0.0653 496 HOH   A O   
6924 O  O   . HOH   F .   ? 0.5834 0.5866 0.6980 0.1014  0.2157  -0.1104 497 HOH   A O   
6925 O  O   . HOH   F .   ? 0.5736 0.6240 0.5768 0.0942  -0.1317 0.0431  498 HOH   A O   
6926 O  O   . HOH   F .   ? 0.6832 0.5444 0.5101 -0.1046 -0.1064 -0.0865 499 HOH   A O   
6927 O  O   . HOH   F .   ? 0.3110 0.2204 0.5854 0.0023  0.0637  0.0917  500 HOH   A O   
6928 O  O   . HOH   F .   ? 0.4403 0.3751 0.4642 -0.1010 0.0499  0.1161  501 HOH   A O   
6929 O  O   . HOH   F .   ? 0.4653 0.3274 0.4558 -0.0009 0.2300  0.0282  502 HOH   A O   
6930 O  O   . HOH   F .   ? 0.6323 0.2436 0.4637 -0.0726 0.1018  0.0498  503 HOH   A O   
6931 O  O   B HOH   F .   ? 0.3740 0.4000 0.3047 0.1156  0.0042  -0.0614 504 HOH   A O   
6932 O  O   . HOH   F .   ? 0.2501 0.3026 0.5024 -0.0016 0.0858  -0.0515 505 HOH   A O   
6933 O  O   B HOH   F .   ? 0.3888 0.3583 0.3530 0.0902  0.0645  0.1239  506 HOH   A O   
6934 O  O   . HOH   F .   ? 0.3994 0.7949 0.5679 -0.0508 -0.0449 0.2256  507 HOH   A O   
6935 O  O   . HOH   F .   ? 0.2396 0.3487 0.3588 0.0525  -0.0404 0.0724  508 HOH   A O   
6936 O  O   . HOH   F .   ? 0.4990 0.2925 0.4545 -0.1744 0.0008  0.0405  509 HOH   A O   
6937 O  O   . HOH   F .   ? 0.2725 0.3987 0.4124 0.0346  -0.0440 0.0073  510 HOH   A O   
6938 O  O   . HOH   F .   ? 0.5566 0.7103 0.5254 0.0789  -0.0989 0.0373  511 HOH   A O   
6939 O  O   . HOH   F .   ? 0.7447 0.6674 0.5164 0.0952  -0.1445 0.0196  512 HOH   A O   
6940 O  O   . HOH   F .   ? 0.6898 0.4062 0.5355 0.0762  0.0318  0.1350  513 HOH   A O   
6941 O  O   . HOH   F .   ? 0.2874 0.8463 0.4579 0.0603  0.0886  -0.0140 514 HOH   A O   
6942 O  O   . HOH   F .   ? 0.2999 0.2396 0.4752 0.0184  0.0441  0.0702  515 HOH   A O   
6943 O  O   . HOH   F .   ? 0.5224 0.6540 0.4886 0.2882  0.0059  0.1275  516 HOH   A O   
6944 O  O   T HOH   F .   ? 0.1357 0.1019 0.2035 -0.0174 0.0055  0.0072  517 HOH   A O   
6945 O  O   . HOH   F .   ? 0.5540 0.5906 0.4653 -0.0787 -0.0863 -0.1296 518 HOH   A O   
6946 O  O   B HOH   F .   ? 0.3639 0.3752 0.3472 0.0726  0.0623  0.0385  519 HOH   A O   
6947 O  O   . HOH   F .   ? 0.2668 0.7417 0.4046 0.0729  0.0218  -0.0385 520 HOH   A O   
6948 O  O   . HOH   F .   ? 0.4469 0.4689 0.4593 0.0966  -0.0126 0.1351  521 HOH   A O   
6949 O  O   . HOH   F .   ? 0.4609 0.6792 0.5498 -0.0771 -0.0380 0.0757  522 HOH   A O   
6950 O  O   . HOH   F .   ? 0.3013 0.4458 0.5452 -0.0259 -0.0824 0.2606  523 HOH   A O   
6951 O  O   . HOH   G .   ? 0.2237 0.2169 0.3344 0.0114  0.0779  0.0324  201 HOH   B O   
6952 O  O   . HOH   G .   ? 0.4505 0.3523 0.3810 -0.0473 0.0140  -0.1267 202 HOH   B O   
6953 O  O   . HOH   G .   ? 0.3096 0.5475 0.5201 -0.0073 0.1717  -0.1860 203 HOH   B O   
6954 O  O   . HOH   G .   ? 0.6029 0.5786 0.5407 0.2162  0.0155  0.0222  204 HOH   B O   
6955 O  O   . HOH   G .   ? 0.3761 0.3494 0.6553 -0.0639 0.0581  -0.0313 205 HOH   B O   
6956 O  O   . HOH   G .   ? 0.3227 0.6950 0.3887 0.0529  0.0073  0.2394  206 HOH   B O   
6957 O  O   . HOH   G .   ? 0.3625 0.4157 0.5013 -0.0918 0.0121  -0.1322 207 HOH   B O   
6958 O  O   . HOH   G .   ? 0.4066 0.5771 0.2884 0.0485  -0.0178 -0.1232 208 HOH   B O   
6959 O  O   . HOH   G .   ? 0.1826 0.2291 0.2967 -0.0136 0.0219  -0.0313 209 HOH   B O   
6960 O  O   . HOH   G .   ? 0.1662 0.2037 0.2987 -0.0214 -0.0031 0.0077  210 HOH   B O   
6961 O  O   . HOH   G .   ? 0.2914 0.2019 0.5449 0.0060  0.1815  0.0541  211 HOH   B O   
6962 O  O   . HOH   G .   ? 0.2808 0.2801 0.6603 0.0659  -0.1211 0.0536  212 HOH   B O   
6963 O  O   . HOH   G .   ? 0.4404 0.6313 0.3863 0.2843  -0.0901 -0.0147 213 HOH   B O   
6964 O  O   . HOH   G .   ? 0.4856 0.4465 0.4157 0.0388  0.1061  -0.1529 214 HOH   B O   
6965 O  O   . HOH   G .   ? 0.7531 0.3541 0.4712 0.0632  0.1508  0.0015  215 HOH   B O   
6966 O  O   . HOH   G .   ? 0.3300 0.2247 0.5163 -0.0010 0.1960  0.0352  216 HOH   B O   
6967 O  O   . HOH   G .   ? 0.4850 0.3477 0.3906 -0.0091 -0.1375 0.0370  217 HOH   B O   
6968 O  O   . HOH   G .   ? 0.3905 0.4436 0.6226 -0.0220 -0.1653 -0.0772 218 HOH   B O   
6969 O  O   . HOH   G .   ? 0.4403 0.5284 0.3986 0.2478  -0.0394 0.0347  219 HOH   B O   
6970 O  O   . HOH   G .   ? 0.5199 0.3100 0.4078 -0.1609 -0.0055 0.0063  220 HOH   B O   
6971 O  O   . HOH   G .   ? 0.3476 0.5282 0.5095 0.2309  0.0285  -0.0375 221 HOH   B O   
6972 O  O   . HOH   G .   ? 0.5041 0.3934 0.5837 0.0588  -0.1045 0.2428  222 HOH   B O   
6973 O  O   . HOH   G .   ? 0.5033 0.2078 0.3102 -0.0067 -0.0920 0.0176  223 HOH   B O   
6974 O  O   . HOH   G .   ? 0.7366 0.4313 0.4922 0.1536  -0.0305 -0.1048 224 HOH   B O   
6975 O  O   . HOH   G .   ? 0.3314 0.4212 0.4776 0.0729  -0.0625 0.0229  225 HOH   B O   
6976 O  O   . HOH   G .   ? 0.1798 0.2230 0.3228 -0.0132 0.0098  -0.0047 226 HOH   B O   
6977 O  O   . HOH   G .   ? 0.2175 0.2280 0.4114 -0.0390 0.0140  -0.0514 227 HOH   B O   
6978 O  O   . HOH   G .   ? 0.5981 0.3613 0.2716 0.0190  0.1256  -0.0236 228 HOH   B O   
6979 O  O   . HOH   G .   ? 0.4144 0.3797 0.4944 -0.1693 0.0100  0.0687  229 HOH   B O   
6980 O  O   . HOH   G .   ? 0.2537 0.1826 0.2801 -0.0304 0.1101  -0.0039 230 HOH   B O   
6981 O  O   . HOH   G .   ? 0.3506 0.1791 0.2107 0.0185  -0.0701 -0.0118 231 HOH   B O   
6982 O  O   . HOH   G .   ? 0.5208 0.3237 0.4212 -0.2321 -0.0055 0.0243  232 HOH   B O   
6983 O  O   . HOH   G .   ? 0.3509 0.3106 0.2234 0.0310  0.0583  0.0422  233 HOH   B O   
6984 O  O   . HOH   G .   ? 0.2714 0.2652 0.3262 0.0430  0.0157  -0.0991 234 HOH   B O   
6985 O  O   . HOH   G .   ? 0.2164 0.2753 0.3234 -0.0659 0.0174  -0.0321 235 HOH   B O   
6986 O  O   . HOH   G .   ? 0.2755 0.3854 0.3249 -0.0882 0.0204  0.0018  236 HOH   B O   
6987 O  O   . HOH   G .   ? 0.3847 0.2635 0.4191 0.0668  -0.0468 -0.0561 237 HOH   B O   
6988 O  O   . HOH   G .   ? 0.2032 0.1392 0.3406 0.0102  -0.0495 -0.0138 238 HOH   B O   
6989 O  O   . HOH   G .   ? 0.4561 0.6830 0.4070 0.2445  0.0491  0.0023  239 HOH   B O   
6990 O  O   . HOH   G .   ? 0.1502 0.1426 0.1669 -0.0119 -0.0056 -0.0080 240 HOH   B O   
6991 O  O   . HOH   G .   ? 0.1600 0.1488 0.2801 -0.0050 0.0070  -0.0097 241 HOH   B O   
6992 O  O   . HOH   G .   ? 0.6174 0.5527 0.3330 0.0855  -0.0357 -0.0131 242 HOH   B O   
6993 O  O   . HOH   G .   ? 0.2458 0.2212 0.2844 0.0773  -0.0831 -0.0640 243 HOH   B O   
6994 O  O   . HOH   G .   ? 0.3099 0.1774 0.6050 -0.0146 -0.1081 -0.0343 244 HOH   B O   
6995 O  O   . HOH   G .   ? 0.2166 0.3648 0.2430 -0.0290 -0.0218 0.0523  245 HOH   B O   
6996 O  O   . HOH   G .   ? 0.3298 0.2523 0.3334 -0.0387 0.0343  -0.0628 246 HOH   B O   
6997 O  O   . HOH   G .   ? 0.3554 0.3695 0.5776 0.0173  0.0235  -0.0129 247 HOH   B O   
6998 O  O   . HOH   G .   ? 0.3720 0.2779 0.4389 0.0518  -0.0966 -0.1503 248 HOH   B O   
6999 O  O   . HOH   G .   ? 0.1499 0.1343 0.1770 -0.0051 -0.0063 0.0100  249 HOH   B O   
7000 O  O   . HOH   G .   ? 0.2202 0.1991 0.2314 -0.0330 -0.0416 0.0137  250 HOH   B O   
7001 O  O   . HOH   G .   ? 0.2190 0.3659 0.3449 -0.0403 -0.0560 -0.0527 251 HOH   B O   
7002 O  O   . HOH   G .   ? 0.2894 0.2286 0.2842 0.0871  0.0674  -0.0029 252 HOH   B O   
7003 O  O   . HOH   G .   ? 0.2712 0.2150 0.2020 0.0153  -0.0113 0.0044  253 HOH   B O   
7004 O  O   . HOH   G .   ? 0.2095 0.1512 0.2157 -0.0251 -0.0390 0.0291  254 HOH   B O   
7005 O  O   . HOH   G .   ? 0.3356 0.4089 0.2459 0.0311  0.0829  0.0092  255 HOH   B O   
7006 O  O   . HOH   G .   ? 0.2329 0.3168 0.2293 -0.0640 0.0247  0.0360  256 HOH   B O   
7007 O  O   . HOH   G .   ? 0.2884 0.4002 0.3148 -0.0744 -0.0374 -0.0579 257 HOH   B O   
7008 O  O   . HOH   G .   ? 0.1677 0.1665 0.3095 -0.0282 -0.0122 0.0104  258 HOH   B O   
7009 O  O   . HOH   G .   ? 0.2125 0.1944 0.3787 -0.0032 -0.0459 -0.0266 259 HOH   B O   
7010 O  O   . HOH   G .   ? 0.2880 0.4609 0.5713 0.0200  -0.0023 -0.1346 260 HOH   B O   
7011 O  O   . HOH   G .   ? 0.1944 0.2768 0.3025 0.0439  0.0535  0.1084  261 HOH   B O   
7012 O  O   . HOH   G .   ? 0.1435 0.1707 0.2287 -0.0068 0.0156  0.0166  262 HOH   B O   
7013 O  O   . HOH   G .   ? 0.3145 0.4955 0.3669 -0.0355 -0.1092 0.0962  263 HOH   B O   
7014 O  O   . HOH   G .   ? 0.4533 0.3856 0.3851 -0.1008 0.1205  -0.1143 264 HOH   B O   
7015 O  O   . HOH   G .   ? 0.2059 0.4253 0.5055 -0.0293 -0.0292 -0.1522 265 HOH   B O   
7016 O  O   . HOH   G .   ? 0.2593 0.2022 0.3037 -0.0630 0.0247  -0.0132 266 HOH   B O   
7017 O  O   . HOH   G .   ? 0.2684 0.2819 0.2413 -0.0442 -0.0789 0.0224  267 HOH   B O   
7018 O  O   . HOH   G .   ? 0.2392 0.3868 0.3477 -0.0758 0.0599  -0.1472 268 HOH   B O   
7019 O  O   . HOH   G .   ? 0.2343 0.2144 0.2114 0.0096  -0.0045 -0.0128 269 HOH   B O   
7020 O  O   . HOH   G .   ? 0.4202 0.2985 0.4591 -0.0136 -0.1057 -0.0543 270 HOH   B O   
7021 O  O   . HOH   G .   ? 0.2708 0.5417 0.5268 0.1640  -0.0539 -0.1143 271 HOH   B O   
7022 O  O   . HOH   G .   ? 0.1886 0.1467 0.3925 -0.0081 -0.0294 -0.0104 272 HOH   B O   
7023 O  O   . HOH   G .   ? 0.1860 0.1844 0.1719 -0.0457 -0.0425 0.0146  273 HOH   B O   
7024 O  O   . HOH   G .   ? 0.2089 0.1526 0.2273 -0.0262 -0.0176 0.0191  274 HOH   B O   
7025 O  O   . HOH   G .   ? 0.2452 0.2672 0.2422 -0.0416 -0.0748 -0.0429 275 HOH   B O   
7026 O  O   . HOH   G .   ? 0.3065 0.2114 0.5166 0.0260  0.0403  0.0637  276 HOH   B O   
7027 O  O   . HOH   G .   ? 0.2870 0.4325 0.2420 0.1787  -0.0553 -0.0667 277 HOH   B O   
7028 O  O   . HOH   G .   ? 0.1610 0.1589 0.3595 -0.0142 0.0157  -0.0082 278 HOH   B O   
7029 O  O   . HOH   G .   ? 0.2556 0.3869 0.3835 0.0279  0.1163  0.0202  279 HOH   B O   
7030 O  O   . HOH   G .   ? 0.4531 0.3580 0.2990 0.0446  0.0020  -0.0728 280 HOH   B O   
7031 O  O   . HOH   G .   ? 0.5733 0.6293 0.2754 -0.0266 -0.1136 0.0571  281 HOH   B O   
7032 O  O   . HOH   G .   ? 0.2638 0.6754 0.2686 0.0648  -0.0334 -0.0498 282 HOH   B O   
7033 O  O   . HOH   G .   ? 0.4013 0.3282 0.5086 -0.0600 0.0241  -0.0196 283 HOH   B O   
7034 O  O   . HOH   G .   ? 0.2798 0.6750 0.7207 0.1079  -0.0909 -0.0928 284 HOH   B O   
7035 O  O   . HOH   G .   ? 0.1731 0.1525 0.2011 -0.0001 -0.0019 0.0006  285 HOH   B O   
7036 O  O   . HOH   G .   ? 0.3282 0.3037 0.2901 -0.0438 0.0220  -0.1364 286 HOH   B O   
7037 O  O   . HOH   G .   ? 0.2824 0.4822 0.4786 -0.0889 -0.1221 0.0940  287 HOH   B O   
7038 O  O   . HOH   G .   ? 0.3397 0.2641 0.2247 0.0057  -0.0760 -0.0014 288 HOH   B O   
7039 O  O   . HOH   G .   ? 0.4205 0.5200 0.4707 -0.0041 -0.1425 0.0535  289 HOH   B O   
7040 O  O   . HOH   G .   ? 0.4236 0.3834 0.2532 0.0917  -0.0694 0.0531  290 HOH   B O   
7041 O  O   . HOH   G .   ? 0.1717 0.2089 0.1565 -0.0163 -0.0175 0.0074  291 HOH   B O   
7042 O  O   . HOH   G .   ? 0.3859 0.2237 0.4086 -0.0943 -0.2064 0.0862  292 HOH   B O   
7043 O  O   . HOH   G .   ? 0.1744 0.3634 0.5092 0.0359  -0.0027 -0.1544 293 HOH   B O   
7044 O  O   . HOH   G .   ? 0.3538 0.3725 0.4740 0.1351  -0.0611 -0.1148 294 HOH   B O   
7045 O  O   . HOH   G .   ? 0.1821 0.1987 0.3077 0.0151  -0.0103 0.0050  295 HOH   B O   
7046 O  O   . HOH   G .   ? 0.5980 0.3794 0.3223 0.2630  0.1186  0.0815  296 HOH   B O   
7047 O  O   . HOH   G .   ? 0.1734 0.1620 0.2546 0.0106  0.0102  0.0207  297 HOH   B O   
7048 O  O   . HOH   G .   ? 0.2522 0.2686 0.2950 0.0109  -0.0713 0.0330  298 HOH   B O   
7049 O  O   . HOH   G .   ? 0.2047 0.3087 0.6217 0.0459  -0.0397 -0.1303 299 HOH   B O   
7050 O  O   . HOH   G .   ? 0.4652 0.4975 0.2524 0.0391  0.0985  0.1104  300 HOH   B O   
7051 O  O   . HOH   G .   ? 0.3398 0.6975 0.3628 0.1699  -0.0238 0.1177  301 HOH   B O   
7052 O  O   . HOH   G .   ? 0.3263 0.2986 0.5347 -0.0264 -0.0970 0.1171  302 HOH   B O   
7053 O  O   . HOH   G .   ? 0.4106 0.3545 0.4029 -0.1585 0.1371  -0.0428 303 HOH   B O   
7054 O  O   . HOH   G .   ? 0.4460 0.3879 0.4429 -0.0851 0.0301  0.1335  304 HOH   B O   
7055 O  O   . HOH   G .   ? 0.2123 0.1656 0.3402 0.0389  -0.0874 -0.0026 305 HOH   B O   
7056 O  O   . HOH   G .   ? 0.2121 0.1664 0.2826 -0.0257 -0.0303 0.0028  306 HOH   B O   
7057 O  O   . HOH   G .   ? 0.1625 0.1924 0.3159 -0.0292 -0.0116 0.0134  307 HOH   B O   
7058 O  O   . HOH   G .   ? 0.3318 0.1936 0.3625 0.0713  0.1067  0.0522  308 HOH   B O   
7059 O  O   . HOH   G .   ? 0.3030 0.2888 0.3473 -0.0397 0.1211  -0.0694 309 HOH   B O   
7060 O  O   . HOH   G .   ? 0.4968 0.2986 0.2436 -0.1756 0.0556  -0.0229 310 HOH   B O   
7061 O  O   . HOH   G .   ? 0.1635 0.1553 0.3202 0.0040  -0.0007 -0.0009 311 HOH   B O   
7062 O  O   . HOH   G .   ? 0.2692 0.3494 0.4796 -0.0466 -0.1457 0.1280  312 HOH   B O   
7063 O  O   . HOH   G .   ? 0.2261 0.1992 0.2043 -0.0090 0.0229  0.0228  313 HOH   B O   
7064 O  O   . HOH   G .   ? 0.2445 0.1535 0.2730 -0.0177 -0.0311 0.0388  314 HOH   B O   
7065 O  O   . HOH   G .   ? 0.2204 0.3006 0.4972 -0.0192 -0.0506 -0.0007 315 HOH   B O   
7066 O  O   . HOH   G .   ? 0.3428 0.4670 0.7467 -0.0260 -0.0913 0.2355  316 HOH   B O   
7067 O  O   . HOH   G .   ? 0.2307 0.5351 0.4441 -0.0529 -0.0242 -0.0434 317 HOH   B O   
7068 O  O   . HOH   G .   ? 0.1605 0.1637 0.3086 -0.0132 -0.0121 -0.0101 318 HOH   B O   
7069 O  O   . HOH   G .   ? 0.6025 0.6705 0.5050 0.3053  -0.0002 -0.0145 319 HOH   B O   
7070 O  O   . HOH   G .   ? 0.4846 0.4088 0.2815 0.0301  -0.0513 -0.0575 320 HOH   B O   
7071 O  O   . HOH   G .   ? 0.4290 0.2343 0.2731 0.1524  0.1078  0.0361  321 HOH   B O   
7072 O  O   . HOH   G .   ? 0.5323 0.3587 0.4831 0.0319  0.1312  -0.1349 322 HOH   B O   
7073 O  O   . HOH   G .   ? 0.1692 0.3012 0.2462 -0.0207 -0.0217 0.0750  323 HOH   B O   
7074 O  O   . HOH   G .   ? 0.4597 0.4139 0.5446 0.0634  -0.0083 0.0549  324 HOH   B O   
7075 O  O   . HOH   G .   ? 0.6650 0.4819 0.5054 0.1172  0.1574  0.0601  325 HOH   B O   
7076 O  O   . HOH   G .   ? 0.4646 0.2571 0.3278 0.0287  0.0571  0.0888  326 HOH   B O   
7077 O  O   . HOH   G .   ? 0.4347 0.4000 0.2329 0.1079  -0.0633 -0.0186 327 HOH   B O   
7078 O  O   . HOH   G .   ? 0.1985 0.2055 0.2950 0.0275  0.0448  0.0206  328 HOH   B O   
7079 O  O   . HOH   G .   ? 0.3063 0.2213 0.2449 0.0216  -0.0185 0.0304  329 HOH   B O   
7080 O  O   . HOH   G .   ? 0.5496 0.4773 0.6490 0.1025  -0.0772 0.1813  330 HOH   B O   
7081 O  O   . HOH   G .   ? 0.1819 0.2936 0.3368 0.0443  -0.0197 -0.0685 331 HOH   B O   
7082 O  O   . HOH   G .   ? 0.4363 0.3127 0.5507 0.1242  0.2141  0.1565  332 HOH   B O   
7083 O  O   . HOH   G .   ? 0.2218 0.2420 0.5690 -0.0493 0.0027  0.1415  333 HOH   B O   
7084 O  O   . HOH   G .   ? 0.5764 0.3856 0.3836 0.0324  0.1109  0.1324  334 HOH   B O   
7085 O  O   . HOH   G .   ? 0.2726 0.2002 0.5093 -0.0035 0.0115  0.0455  335 HOH   B O   
7086 O  O   . HOH   G .   ? 0.8424 0.2199 0.3309 0.0350  -0.0816 0.0078  336 HOH   B O   
7087 O  O   . HOH   G .   ? 0.5754 0.4440 0.5968 -0.0713 -0.0723 -0.1332 337 HOH   B O   
7088 O  O   . HOH   G .   ? 0.6116 0.5161 0.5490 -0.1054 -0.0577 0.1287  338 HOH   B O   
7089 O  O   . HOH   G .   ? 0.1811 0.1474 0.2458 0.0097  -0.0204 0.0079  339 HOH   B O   
7090 O  O   . HOH   G .   ? 0.4206 0.6708 0.3925 -0.0454 -0.0789 0.1844  340 HOH   B O   
7091 O  O   . HOH   G .   ? 0.5041 0.3149 0.3190 0.0446  -0.1360 -0.0547 341 HOH   B O   
7092 O  O   . HOH   G .   ? 0.4546 0.5585 0.3869 0.0143  -0.0992 0.0137  342 HOH   B O   
7093 O  O   . HOH   G .   ? 0.6674 0.6890 0.3149 0.0026  -0.0495 0.1300  343 HOH   B O   
7094 O  O   . HOH   G .   ? 0.4441 0.5948 0.4024 -0.0926 -0.0869 -0.0673 344 HOH   B O   
7095 O  O   . HOH   G .   ? 0.2667 0.5482 0.6502 -0.0118 -0.0626 0.0540  345 HOH   B O   
7096 O  O   . HOH   G .   ? 0.2061 0.2060 0.3425 -0.0082 0.0734  -0.0095 346 HOH   B O   
7097 O  O   . HOH   G .   ? 0.4443 0.5233 0.5750 0.0087  -0.1006 0.0450  347 HOH   B O   
7098 O  O   . HOH   G .   ? 0.2589 0.6526 0.3165 0.1725  -0.0634 -0.1453 348 HOH   B O   
7099 O  O   . HOH   G .   ? 0.2782 0.2353 0.5068 -0.0318 -0.0911 -0.0551 349 HOH   B O   
7100 O  O   . HOH   G .   ? 0.2293 0.3957 0.5196 0.0147  0.0430  0.0188  350 HOH   B O   
7101 O  O   . HOH   G .   ? 0.4759 0.5792 0.4893 -0.1189 0.0412  0.1143  351 HOH   B O   
7102 O  O   . HOH   G .   ? 0.3396 0.4761 0.4682 -0.1526 0.0222  -0.0607 352 HOH   B O   
7103 O  O   . HOH   G .   ? 0.3732 0.2143 0.3446 -0.0583 0.0144  -0.0693 353 HOH   B O   
7104 O  O   . HOH   G .   ? 0.3061 0.1884 0.4389 0.0464  -0.1131 -0.0586 354 HOH   B O   
7105 O  O   . HOH   G .   ? 0.4718 0.5378 0.6147 0.0256  0.0391  -0.0732 355 HOH   B O   
7106 O  O   . HOH   G .   ? 0.3561 0.2853 0.3759 -0.0968 0.0098  -0.0765 356 HOH   B O   
7107 O  O   . HOH   G .   ? 0.4715 0.3324 0.5620 -0.1129 0.1426  0.0838  357 HOH   B O   
7108 O  O   . HOH   G .   ? 0.4707 0.5500 0.4837 0.1785  -0.1195 0.1446  358 HOH   B O   
7109 O  O   . HOH   G .   ? 0.5765 0.3644 0.4187 0.0447  0.1601  -0.0490 359 HOH   B O   
7110 O  O   . HOH   G .   ? 0.4801 0.4794 0.4953 -0.0569 -0.0389 0.0013  360 HOH   B O   
7111 O  O   . HOH   G .   ? 0.5159 0.3480 0.4907 -0.0063 -0.1569 -0.0527 361 HOH   B O   
7112 O  O   . HOH   G .   ? 0.4987 0.3913 0.5953 0.0773  0.1008  0.1051  362 HOH   B O   
7113 O  O   . HOH   G .   ? 0.4635 0.6500 0.2960 0.2303  0.0003  0.0379  363 HOH   B O   
7114 O  O   . HOH   G .   ? 0.2171 0.4090 0.6784 -0.0807 -0.0645 -0.0624 364 HOH   B O   
7115 O  O   . HOH   G .   ? 0.4836 0.3010 0.5696 -0.1333 -0.0599 0.0196  365 HOH   B O   
7116 O  O   . HOH   G .   ? 0.6417 0.2287 0.4002 -0.0174 0.0063  0.0756  366 HOH   B O   
7117 O  O   . HOH   G .   ? 0.5024 0.5735 0.4351 -0.0711 -0.0529 -0.1116 367 HOH   B O   
7118 O  O   . HOH   G .   ? 0.6293 0.4414 0.4329 0.1090  0.0492  0.0376  368 HOH   B O   
7119 O  O   . HOH   G .   ? 0.5712 0.5942 0.3635 0.1594  -0.1597 0.0765  369 HOH   B O   
7120 O  O   . HOH   G .   ? 0.5492 0.3667 0.5324 0.1310  -0.1284 0.0258  370 HOH   B O   
7121 O  O   . HOH   G .   ? 0.4072 0.5543 0.5163 0.2373  0.0842  0.1408  371 HOH   B O   
7122 O  O   . HOH   G .   ? 0.7614 0.7722 0.5542 0.2482  -0.1420 0.0662  372 HOH   B O   
7123 O  O   . HOH   G .   ? 0.5937 0.4275 0.2992 -0.0904 -0.0927 -0.0826 373 HOH   B O   
7124 O  O   . HOH   G .   ? 0.4460 0.7008 0.5788 0.1342  0.0585  0.2673  374 HOH   B O   
7125 O  O   . HOH   G .   ? 0.4290 0.3176 0.3495 0.0829  -0.1402 -0.0473 375 HOH   B O   
7126 O  O   . HOH   G .   ? 0.4564 0.4849 0.4800 -0.0824 -0.0461 0.0333  376 HOH   B O   
7127 O  O   . HOH   G .   ? 0.3490 0.4910 0.2336 0.0153  0.0561  0.0350  377 HOH   B O   
7128 O  O   . HOH   G .   ? 0.2359 0.4224 0.4373 0.0385  -0.0521 -0.0588 378 HOH   B O   
7129 O  O   . HOH   G .   ? 0.5274 0.6597 0.3991 -0.1407 0.0084  -0.1525 379 HOH   B O   
7130 O  O   . HOH   G .   ? 0.7288 0.3928 0.5189 -0.0855 -0.0529 0.0053  380 HOH   B O   
7131 O  O   . HOH   G .   ? 0.3887 0.5174 0.5435 0.0777  0.0001  -0.0287 381 HOH   B O   
7132 O  O   . HOH   G .   ? 0.5389 0.6700 0.6729 -0.0319 0.2266  0.1498  382 HOH   B O   
7133 O  O   . HOH   G .   ? 0.2971 0.2668 0.3339 0.0081  0.0199  0.0320  383 HOH   B O   
7134 O  O   . HOH   G .   ? 0.4245 0.7831 0.5833 0.0911  0.1987  0.0588  384 HOH   B O   
7135 O  O   . HOH   G .   ? 0.6217 0.4226 0.3977 0.0890  0.0712  -0.0796 385 HOH   B O   
7136 O  O   . HOH   G .   ? 0.4977 0.5142 0.4410 0.0533  -0.0616 -0.0811 386 HOH   B O   
7137 O  O   . HOH   G .   ? 0.2386 0.4280 0.4297 -0.0728 -0.0930 -0.0313 387 HOH   B O   
7138 O  O   . HOH   G .   ? 0.6139 0.4629 0.5437 -0.0848 0.0557  -0.0330 388 HOH   B O   
7139 O  O   . HOH   G .   ? 0.7042 0.5801 0.4552 0.2170  -0.0294 0.0216  389 HOH   B O   
7140 O  O   . HOH   G .   ? 0.4760 0.3838 0.3428 0.0235  0.0594  -0.0144 390 HOH   B O   
7141 O  O   . HOH   G .   ? 0.3877 0.2378 0.3536 0.0727  -0.0221 0.0214  391 HOH   B O   
7142 O  O   . HOH   G .   ? 0.5536 0.4589 0.4061 0.0667  0.0643  0.0726  392 HOH   B O   
7143 O  O   . HOH   G .   ? 0.4396 0.2373 0.4856 -0.0616 0.0486  0.0506  393 HOH   B O   
7144 O  O   . HOH   G .   ? 0.2624 0.4756 0.6073 -0.1545 -0.0467 0.0080  394 HOH   B O   
7145 O  O   . HOH   G .   ? 0.4380 0.5447 0.4016 0.0957  0.0080  -0.0779 395 HOH   B O   
7146 O  O   . HOH   G .   ? 0.3397 0.3895 0.3889 0.0045  0.0352  -0.0882 396 HOH   B O   
7147 O  O   . HOH   G .   ? 0.1980 0.2968 0.6090 -0.0540 -0.0607 0.0208  397 HOH   B O   
7148 O  O   . HOH   G .   ? 0.4434 0.4524 0.4511 0.0591  0.0964  0.0540  398 HOH   B O   
7149 O  O   . HOH   G .   ? 0.5325 0.4357 0.3100 -0.2242 -0.0569 0.0989  399 HOH   B O   
7150 O  O   . HOH   G .   ? 0.5160 0.5652 0.6160 0.0776  -0.1224 0.1840  400 HOH   B O   
7151 O  O   . HOH   G .   ? 0.5814 0.5838 0.3841 0.1702  -0.0191 -0.0532 401 HOH   B O   
# 
