data_7HEC
# 
_entry.id   7HEC 
# 
_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   7HEC         pdb_00007hec 10.2210/pdb7hec/pdb 
WWPDB D_1001407366 ?            ?                   
# 
_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                        7HEC 
_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)-3-phenyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butan-1-ol' 282.340   1   ?                      ? ? 
?                                                                                    
4 water       nat water                                                                   18.015    421 ?                      ? ? 
?                                                                                    
# 
_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)-3-phenyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butan-1-ol' A1A9O 
4 water                                                                   HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A9O non-polymer         . '(2S,3R)-3-phenyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butan-1-ol' ? 'C16 H18 N4 O'   282.340 
ALA   'L-peptide linking' y ALANINE                                                                 ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                              ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                         ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                               ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                         ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                 ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                               ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                   ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                              ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                 ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                  ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                              ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                           ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                 ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                  ? 'C3 H7 N O3'     105.093 
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 A1A9O 1   202 201  A1A9O LA1 A . 
E 4 HOH   1   301 196  HOH   HOH A . 
E 4 HOH   2   302 292  HOH   HOH A . 
E 4 HOH   3   303 153  HOH   HOH A . 
E 4 HOH   4   304 11   HOH   HOH A . 
E 4 HOH   5   305 625  HOH   HOH A . 
E 4 HOH   6   306 209  HOH   HOH A . 
E 4 HOH   7   307 86   HOH   HOH A . 
E 4 HOH   8   308 229  HOH   HOH A . 
E 4 HOH   9   309 405  HOH   HOH A . 
E 4 HOH   10  310 1289 HOH   HOH A . 
E 4 HOH   11  311 109  HOH   HOH A . 
E 4 HOH   12  312 17   HOH   HOH A . 
E 4 HOH   13  313 247  HOH   HOH A . 
E 4 HOH   14  314 661  HOH   HOH A . 
E 4 HOH   15  315 1275 HOH   HOH A . 
E 4 HOH   16  316 76   HOH   HOH A . 
E 4 HOH   17  317 409  HOH   HOH A . 
E 4 HOH   18  318 136  HOH   HOH A . 
E 4 HOH   19  319 236  HOH   HOH A . 
E 4 HOH   20  320 8    HOH   HOH A . 
E 4 HOH   21  321 630  HOH   HOH A . 
E 4 HOH   22  322 151  HOH   HOH A . 
E 4 HOH   23  323 124  HOH   HOH A . 
E 4 HOH   24  324 1295 HOH   HOH A . 
E 4 HOH   25  325 1283 HOH   HOH A . 
E 4 HOH   26  326 15   HOH   HOH A . 
E 4 HOH   27  327 964  HOH   HOH A . 
E 4 HOH   28  328 1301 HOH   HOH A . 
E 4 HOH   29  329 192  HOH   HOH A . 
E 4 HOH   30  330 241  HOH   HOH A . 
E 4 HOH   31  331 469  HOH   HOH A . 
E 4 HOH   32  332 105  HOH   HOH A . 
E 4 HOH   33  333 225  HOH   HOH A . 
E 4 HOH   34  334 78   HOH   HOH A . 
E 4 HOH   35  335 164  HOH   HOH A . 
E 4 HOH   36  336 96   HOH   HOH A . 
E 4 HOH   37  337 57   HOH   HOH A . 
E 4 HOH   38  338 195  HOH   HOH A . 
E 4 HOH   39  339 140  HOH   HOH A . 
E 4 HOH   40  340 21   HOH   HOH A . 
E 4 HOH   41  341 662  HOH   HOH A . 
E 4 HOH   42  342 1300 HOH   HOH A . 
E 4 HOH   43  343 337  HOH   HOH A . 
E 4 HOH   44  344 296  HOH   HOH A . 
E 4 HOH   45  345 39   HOH   HOH A . 
E 4 HOH   46  346 393  HOH   HOH A . 
E 4 HOH   47  347 18   HOH   HOH A . 
E 4 HOH   48  348 93   HOH   HOH A . 
E 4 HOH   49  349 165  HOH   HOH A . 
E 4 HOH   50  350 320  HOH   HOH A . 
E 4 HOH   51  351 42   HOH   HOH A . 
E 4 HOH   52  352 92   HOH   HOH A . 
E 4 HOH   53  353 2    HOH   HOH A . 
E 4 HOH   54  354 66   HOH   HOH A . 
E 4 HOH   55  355 1290 HOH   HOH A . 
E 4 HOH   56  356 162  HOH   HOH A . 
E 4 HOH   57  357 33   HOH   HOH A . 
E 4 HOH   58  358 102  HOH   HOH A . 
E 4 HOH   59  359 1310 HOH   HOH A . 
E 4 HOH   60  360 36   HOH   HOH A . 
E 4 HOH   61  361 169  HOH   HOH A . 
E 4 HOH   62  362 354  HOH   HOH A . 
E 4 HOH   63  363 19   HOH   HOH A . 
E 4 HOH   64  364 139  HOH   HOH A . 
E 4 HOH   65  365 81   HOH   HOH A . 
E 4 HOH   66  366 155  HOH   HOH A . 
E 4 HOH   67  367 45   HOH   HOH A . 
E 4 HOH   68  368 159  HOH   HOH A . 
E 4 HOH   69  369 5    HOH   HOH A . 
E 4 HOH   70  370 396  HOH   HOH A . 
E 4 HOH   71  371 939  HOH   HOH A . 
E 4 HOH   72  372 148  HOH   HOH A . 
E 4 HOH   73  373 138  HOH   HOH A . 
E 4 HOH   74  374 1308 HOH   HOH A . 
E 4 HOH   75  375 186  HOH   HOH A . 
E 4 HOH   76  376 281  HOH   HOH A . 
E 4 HOH   77  377 278  HOH   HOH A . 
E 4 HOH   78  378 46   HOH   HOH A . 
E 4 HOH   79  379 9    HOH   HOH A . 
E 4 HOH   80  380 35   HOH   HOH A . 
E 4 HOH   81  381 56   HOH   HOH A . 
E 4 HOH   82  382 134  HOH   HOH A . 
E 4 HOH   83  383 3    HOH   HOH A . 
E 4 HOH   84  384 24   HOH   HOH A . 
E 4 HOH   85  385 62   HOH   HOH A . 
E 4 HOH   86  386 26   HOH   HOH A . 
E 4 HOH   87  387 461  HOH   HOH A . 
E 4 HOH   88  388 140  HOH   HOH A . 
E 4 HOH   89  389 366  HOH   HOH A . 
E 4 HOH   90  390 218  HOH   HOH A . 
E 4 HOH   91  391 49   HOH   HOH A . 
E 4 HOH   92  392 7    HOH   HOH A . 
E 4 HOH   93  393 154  HOH   HOH A . 
E 4 HOH   94  394 27   HOH   HOH A . 
E 4 HOH   95  395 70   HOH   HOH A . 
E 4 HOH   96  396 115  HOH   HOH A . 
E 4 HOH   97  397 85   HOH   HOH A . 
E 4 HOH   98  398 34   HOH   HOH A . 
E 4 HOH   99  399 132  HOH   HOH A . 
E 4 HOH   100 400 116  HOH   HOH A . 
E 4 HOH   101 401 6    HOH   HOH A . 
E 4 HOH   102 402 303  HOH   HOH A . 
E 4 HOH   103 403 351  HOH   HOH A . 
E 4 HOH   104 404 83   HOH   HOH A . 
E 4 HOH   105 405 1309 HOH   HOH A . 
E 4 HOH   106 406 58   HOH   HOH A . 
E 4 HOH   107 407 74   HOH   HOH A . 
E 4 HOH   108 408 1315 HOH   HOH A . 
E 4 HOH   109 409 12   HOH   HOH A . 
E 4 HOH   110 410 67   HOH   HOH A . 
E 4 HOH   111 411 8    HOH   HOH A . 
E 4 HOH   112 412 25   HOH   HOH A . 
E 4 HOH   113 413 333  HOH   HOH A . 
E 4 HOH   114 414 121  HOH   HOH A . 
E 4 HOH   115 415 7    HOH   HOH A . 
E 4 HOH   116 416 381  HOH   HOH A . 
E 4 HOH   117 417 199  HOH   HOH A . 
E 4 HOH   118 418 1313 HOH   HOH A . 
E 4 HOH   119 419 3    HOH   HOH A . 
E 4 HOH   120 420 123  HOH   HOH A . 
E 4 HOH   121 421 68   HOH   HOH A . 
E 4 HOH   122 422 5    HOH   HOH A . 
E 4 HOH   123 423 397  HOH   HOH A . 
E 4 HOH   124 424 53   HOH   HOH A . 
E 4 HOH   125 425 125  HOH   HOH A . 
E 4 HOH   126 426 156  HOH   HOH A . 
E 4 HOH   127 427 1068 HOH   HOH A . 
E 4 HOH   128 428 1279 HOH   HOH A . 
E 4 HOH   129 429 95   HOH   HOH A . 
E 4 HOH   130 430 582  HOH   HOH A . 
E 4 HOH   131 431 122  HOH   HOH A . 
E 4 HOH   132 432 51   HOH   HOH A . 
E 4 HOH   133 433 1222 HOH   HOH A . 
E 4 HOH   134 434 1296 HOH   HOH A . 
E 4 HOH   135 435 1238 HOH   HOH A . 
E 4 HOH   136 436 16   HOH   HOH A . 
E 4 HOH   137 437 4    HOH   HOH A . 
E 4 HOH   138 438 493  HOH   HOH A . 
E 4 HOH   139 439 71   HOH   HOH A . 
E 4 HOH   140 440 212  HOH   HOH A . 
E 4 HOH   141 441 80   HOH   HOH A . 
E 4 HOH   142 442 40   HOH   HOH A . 
E 4 HOH   143 443 94   HOH   HOH A . 
E 4 HOH   144 444 188  HOH   HOH A . 
E 4 HOH   145 445 73   HOH   HOH A . 
E 4 HOH   146 446 952  HOH   HOH A . 
E 4 HOH   147 447 1286 HOH   HOH A . 
E 4 HOH   148 448 944  HOH   HOH A . 
E 4 HOH   149 449 1094 HOH   HOH A . 
E 4 HOH   150 450 79   HOH   HOH A . 
E 4 HOH   151 451 97   HOH   HOH A . 
E 4 HOH   152 452 104  HOH   HOH A . 
E 4 HOH   153 453 576  HOH   HOH A . 
E 4 HOH   154 454 6    HOH   HOH A . 
E 4 HOH   155 455 1189 HOH   HOH A . 
E 4 HOH   156 456 330  HOH   HOH A . 
E 4 HOH   157 457 107  HOH   HOH A . 
E 4 HOH   158 458 1134 HOH   HOH A . 
E 4 HOH   159 459 1119 HOH   HOH A . 
E 4 HOH   160 460 509  HOH   HOH A . 
E 4 HOH   161 461 726  HOH   HOH A . 
E 4 HOH   162 462 163  HOH   HOH A . 
E 4 HOH   163 463 408  HOH   HOH A . 
E 4 HOH   164 464 756  HOH   HOH A . 
E 4 HOH   165 465 1276 HOH   HOH A . 
E 4 HOH   166 466 361  HOH   HOH A . 
E 4 HOH   167 467 126  HOH   HOH A . 
E 4 HOH   168 468 319  HOH   HOH A . 
E 4 HOH   169 469 280  HOH   HOH A . 
E 4 HOH   170 470 556  HOH   HOH A . 
E 4 HOH   171 471 801  HOH   HOH A . 
E 4 HOH   172 472 1307 HOH   HOH A . 
E 4 HOH   173 473 63   HOH   HOH A . 
E 4 HOH   174 474 250  HOH   HOH A . 
E 4 HOH   175 475 342  HOH   HOH A . 
E 4 HOH   176 476 12   HOH   HOH A . 
E 4 HOH   177 477 135  HOH   HOH A . 
E 4 HOH   178 478 1287 HOH   HOH A . 
E 4 HOH   179 479 1306 HOH   HOH A . 
E 4 HOH   180 480 370  HOH   HOH A . 
E 4 HOH   181 481 202  HOH   HOH A . 
E 4 HOH   182 482 224  HOH   HOH A . 
E 4 HOH   183 483 695  HOH   HOH A . 
E 4 HOH   184 484 674  HOH   HOH A . 
E 4 HOH   185 485 919  HOH   HOH A . 
E 4 HOH   186 486 267  HOH   HOH A . 
E 4 HOH   187 487 711  HOH   HOH A . 
E 4 HOH   188 488 309  HOH   HOH A . 
E 4 HOH   189 489 1314 HOH   HOH A . 
E 4 HOH   190 490 318  HOH   HOH A . 
E 4 HOH   191 491 1299 HOH   HOH A . 
E 4 HOH   192 492 315  HOH   HOH A . 
E 4 HOH   193 493 805  HOH   HOH A . 
E 4 HOH   194 494 331  HOH   HOH A . 
E 4 HOH   195 495 326  HOH   HOH A . 
E 4 HOH   196 496 263  HOH   HOH A . 
E 4 HOH   197 497 941  HOH   HOH A . 
E 4 HOH   198 498 521  HOH   HOH A . 
E 4 HOH   199 499 152  HOH   HOH A . 
E 4 HOH   200 500 208  HOH   HOH A . 
E 4 HOH   201 501 4    HOH   HOH A . 
E 4 HOH   202 502 180  HOH   HOH A . 
E 4 HOH   203 503 1071 HOH   HOH A . 
E 4 HOH   204 504 350  HOH   HOH A . 
E 4 HOH   205 505 356  HOH   HOH A . 
E 4 HOH   206 506 363  HOH   HOH A . 
E 4 HOH   207 507 313  HOH   HOH A . 
E 4 HOH   208 508 371  HOH   HOH A . 
E 4 HOH   209 509 10   HOH   HOH A . 
E 4 HOH   210 510 1284 HOH   HOH A . 
E 4 HOH   211 511 185  HOH   HOH A . 
E 4 HOH   212 512 429  HOH   HOH A . 
E 4 HOH   213 513 1    HOH   HOH A . 
E 4 HOH   214 514 70   HOH   HOH A . 
E 4 HOH   215 515 376  HOH   HOH A . 
E 4 HOH   216 516 772  HOH   HOH A . 
E 4 HOH   217 517 2    HOH   HOH A . 
E 4 HOH   218 518 1074 HOH   HOH A . 
E 4 HOH   219 519 346  HOH   HOH A . 
E 4 HOH   220 520 1292 HOH   HOH A . 
E 4 HOH   221 521 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 531  HOH   HOH B . 
F 4 HOH   3   203 549  HOH   HOH B . 
F 4 HOH   4   204 358  HOH   HOH B . 
F 4 HOH   5   205 364  HOH   HOH B . 
F 4 HOH   6   206 758  HOH   HOH B . 
F 4 HOH   7   207 1249 HOH   HOH B . 
F 4 HOH   8   208 900  HOH   HOH B . 
F 4 HOH   9   209 353  HOH   HOH B . 
F 4 HOH   10  210 240  HOH   HOH B . 
F 4 HOH   11  211 343  HOH   HOH B . 
F 4 HOH   12  212 398  HOH   HOH B . 
F 4 HOH   13  213 120  HOH   HOH B . 
F 4 HOH   14  214 232  HOH   HOH B . 
F 4 HOH   15  215 50   HOH   HOH B . 
F 4 HOH   16  216 264  HOH   HOH B . 
F 4 HOH   17  217 452  HOH   HOH B . 
F 4 HOH   18  218 743  HOH   HOH B . 
F 4 HOH   19  219 1312 HOH   HOH B . 
F 4 HOH   20  220 654  HOH   HOH B . 
F 4 HOH   21  221 1140 HOH   HOH B . 
F 4 HOH   22  222 131  HOH   HOH B . 
F 4 HOH   23  223 444  HOH   HOH B . 
F 4 HOH   24  224 54   HOH   HOH B . 
F 4 HOH   25  225 332  HOH   HOH B . 
F 4 HOH   26  226 166  HOH   HOH B . 
F 4 HOH   27  227 1278 HOH   HOH B . 
F 4 HOH   28  228 723  HOH   HOH B . 
F 4 HOH   29  229 75   HOH   HOH B . 
F 4 HOH   30  230 282  HOH   HOH B . 
F 4 HOH   31  231 205  HOH   HOH B . 
F 4 HOH   32  232 325  HOH   HOH B . 
F 4 HOH   33  233 82   HOH   HOH B . 
F 4 HOH   34  234 60   HOH   HOH B . 
F 4 HOH   35  235 128  HOH   HOH B . 
F 4 HOH   36  236 127  HOH   HOH B . 
F 4 HOH   37  237 272  HOH   HOH B . 
F 4 HOH   38  238 300  HOH   HOH B . 
F 4 HOH   39  239 1    HOH   HOH B . 
F 4 HOH   40  240 181  HOH   HOH B . 
F 4 HOH   41  241 110  HOH   HOH B . 
F 4 HOH   42  242 252  HOH   HOH B . 
F 4 HOH   43  243 276  HOH   HOH B . 
F 4 HOH   44  244 14   HOH   HOH B . 
F 4 HOH   45  245 144  HOH   HOH B . 
F 4 HOH   46  246 143  HOH   HOH B . 
F 4 HOH   47  247 9    HOH   HOH B . 
F 4 HOH   48  248 69   HOH   HOH B . 
F 4 HOH   49  249 133  HOH   HOH B . 
F 4 HOH   50  250 30   HOH   HOH B . 
F 4 HOH   51  251 172  HOH   HOH B . 
F 4 HOH   52  252 52   HOH   HOH B . 
F 4 HOH   53  253 391  HOH   HOH B . 
F 4 HOH   54  254 31   HOH   HOH B . 
F 4 HOH   55  255 129  HOH   HOH B . 
F 4 HOH   56  256 41   HOH   HOH B . 
F 4 HOH   57  257 271  HOH   HOH B . 
F 4 HOH   58  258 347  HOH   HOH B . 
F 4 HOH   59  259 10   HOH   HOH B . 
F 4 HOH   60  260 47   HOH   HOH B . 
F 4 HOH   61  261 150  HOH   HOH B . 
F 4 HOH   62  262 103  HOH   HOH B . 
F 4 HOH   63  263 231  HOH   HOH B . 
F 4 HOH   64  264 72   HOH   HOH B . 
F 4 HOH   65  265 416  HOH   HOH B . 
F 4 HOH   66  266 59   HOH   HOH B . 
F 4 HOH   67  267 243  HOH   HOH B . 
F 4 HOH   68  268 11   HOH   HOH B . 
F 4 HOH   69  269 117  HOH   HOH B . 
F 4 HOH   70  270 61   HOH   HOH B . 
F 4 HOH   71  271 242  HOH   HOH B . 
F 4 HOH   72  272 302  HOH   HOH B . 
F 4 HOH   73  273 77   HOH   HOH B . 
F 4 HOH   74  274 114  HOH   HOH B . 
F 4 HOH   75  275 175  HOH   HOH B . 
F 4 HOH   76  276 1277 HOH   HOH B . 
F 4 HOH   77  277 84   HOH   HOH B . 
F 4 HOH   78  278 20   HOH   HOH B . 
F 4 HOH   79  279 43   HOH   HOH B . 
F 4 HOH   80  280 147  HOH   HOH B . 
F 4 HOH   81  281 221  HOH   HOH B . 
F 4 HOH   82  282 287  HOH   HOH B . 
F 4 HOH   83  283 1066 HOH   HOH B . 
F 4 HOH   84  284 220  HOH   HOH B . 
F 4 HOH   85  285 1106 HOH   HOH B . 
F 4 HOH   86  286 137  HOH   HOH B . 
F 4 HOH   87  287 88   HOH   HOH B . 
F 4 HOH   88  288 1305 HOH   HOH B . 
F 4 HOH   89  289 22   HOH   HOH B . 
F 4 HOH   90  290 235  HOH   HOH B . 
F 4 HOH   91  291 216  HOH   HOH B . 
F 4 HOH   92  292 13   HOH   HOH B . 
F 4 HOH   93  293 106  HOH   HOH B . 
F 4 HOH   94  294 387  HOH   HOH B . 
F 4 HOH   95  295 99   HOH   HOH B . 
F 4 HOH   96  296 160  HOH   HOH B . 
F 4 HOH   97  297 142  HOH   HOH B . 
F 4 HOH   98  298 635  HOH   HOH B . 
F 4 HOH   99  299 112  HOH   HOH B . 
F 4 HOH   100 300 141  HOH   HOH B . 
F 4 HOH   101 301 89   HOH   HOH B . 
F 4 HOH   102 302 118  HOH   HOH B . 
F 4 HOH   103 303 316  HOH   HOH B . 
F 4 HOH   104 304 311  HOH   HOH B . 
F 4 HOH   105 305 341  HOH   HOH B . 
F 4 HOH   106 306 299  HOH   HOH B . 
F 4 HOH   107 307 215  HOH   HOH B . 
F 4 HOH   108 308 101  HOH   HOH B . 
F 4 HOH   109 309 1126 HOH   HOH B . 
F 4 HOH   110 310 297  HOH   HOH B . 
F 4 HOH   111 311 37   HOH   HOH B . 
F 4 HOH   112 312 38   HOH   HOH B . 
F 4 HOH   113 313 32   HOH   HOH B . 
F 4 HOH   114 314 48   HOH   HOH B . 
F 4 HOH   115 315 1274 HOH   HOH B . 
F 4 HOH   116 316 170  HOH   HOH B . 
F 4 HOH   117 317 161  HOH   HOH B . 
F 4 HOH   118 318 23   HOH   HOH B . 
F 4 HOH   119 319 28   HOH   HOH B . 
F 4 HOH   120 320 1291 HOH   HOH B . 
F 4 HOH   121 321 44   HOH   HOH B . 
F 4 HOH   122 322 91   HOH   HOH B . 
F 4 HOH   123 323 100  HOH   HOH B . 
F 4 HOH   124 324 704  HOH   HOH B . 
F 4 HOH   125 325 1285 HOH   HOH B . 
F 4 HOH   126 326 177  HOH   HOH B . 
F 4 HOH   127 327 197  HOH   HOH B . 
F 4 HOH   128 328 182  HOH   HOH B . 
F 4 HOH   129 329 1294 HOH   HOH B . 
F 4 HOH   130 330 29   HOH   HOH B . 
F 4 HOH   131 331 334  HOH   HOH B . 
F 4 HOH   132 332 98   HOH   HOH B . 
F 4 HOH   133 333 55   HOH   HOH B . 
F 4 HOH   134 334 207  HOH   HOH B . 
F 4 HOH   135 335 717  HOH   HOH B . 
F 4 HOH   136 336 234  HOH   HOH B . 
F 4 HOH   137 337 339  HOH   HOH B . 
F 4 HOH   138 338 65   HOH   HOH B . 
F 4 HOH   139 339 619  HOH   HOH B . 
F 4 HOH   140 340 445  HOH   HOH B . 
F 4 HOH   141 341 1293 HOH   HOH B . 
F 4 HOH   142 342 178  HOH   HOH B . 
F 4 HOH   143 343 362  HOH   HOH B . 
F 4 HOH   144 344 960  HOH   HOH B . 
F 4 HOH   145 345 90   HOH   HOH B . 
F 4 HOH   146 346 1304 HOH   HOH B . 
F 4 HOH   147 347 463  HOH   HOH B . 
F 4 HOH   148 348 623  HOH   HOH B . 
F 4 HOH   149 349 191  HOH   HOH B . 
F 4 HOH   150 350 335  HOH   HOH B . 
F 4 HOH   151 351 1046 HOH   HOH B . 
F 4 HOH   152 352 304  HOH   HOH B . 
F 4 HOH   153 353 203  HOH   HOH B . 
F 4 HOH   154 354 1280 HOH   HOH B . 
F 4 HOH   155 355 290  HOH   HOH B . 
F 4 HOH   156 356 541  HOH   HOH B . 
F 4 HOH   157 357 87   HOH   HOH B . 
F 4 HOH   158 358 479  HOH   HOH B . 
F 4 HOH   159 359 389  HOH   HOH B . 
F 4 HOH   160 360 1077 HOH   HOH B . 
F 4 HOH   161 361 718  HOH   HOH B . 
F 4 HOH   162 362 283  HOH   HOH B . 
F 4 HOH   163 363 1072 HOH   HOH B . 
F 4 HOH   164 364 1316 HOH   HOH B . 
F 4 HOH   165 365 898  HOH   HOH B . 
F 4 HOH   166 366 291  HOH   HOH B . 
F 4 HOH   167 367 373  HOH   HOH B . 
F 4 HOH   168 368 615  HOH   HOH B . 
F 4 HOH   169 369 1303 HOH   HOH B . 
F 4 HOH   170 370 667  HOH   HOH B . 
F 4 HOH   171 371 340  HOH   HOH B . 
F 4 HOH   172 372 190  HOH   HOH B . 
F 4 HOH   173 373 310  HOH   HOH B . 
F 4 HOH   174 374 149  HOH   HOH B . 
F 4 HOH   175 375 431  HOH   HOH B . 
F 4 HOH   176 376 1173 HOH   HOH B . 
F 4 HOH   177 377 183  HOH   HOH B . 
F 4 HOH   178 378 1163 HOH   HOH B . 
F 4 HOH   179 379 1000 HOH   HOH B . 
F 4 HOH   180 380 418  HOH   HOH B . 
F 4 HOH   181 381 1311 HOH   HOH B . 
F 4 HOH   182 382 176  HOH   HOH B . 
F 4 HOH   183 383 424  HOH   HOH B . 
F 4 HOH   184 384 1298 HOH   HOH B . 
F 4 HOH   185 385 491  HOH   HOH B . 
F 4 HOH   186 386 981  HOH   HOH B . 
F 4 HOH   187 387 248  HOH   HOH B . 
F 4 HOH   188 388 265  HOH   HOH B . 
F 4 HOH   189 389 470  HOH   HOH B . 
F 4 HOH   190 390 184  HOH   HOH B . 
F 4 HOH   191 391 360  HOH   HOH B . 
F 4 HOH   192 392 355  HOH   HOH B . 
F 4 HOH   193 393 410  HOH   HOH B . 
F 4 HOH   194 394 274  HOH   HOH B . 
F 4 HOH   195 395 314  HOH   HOH B . 
F 4 HOH   196 396 566  HOH   HOH B . 
F 4 HOH   197 397 157  HOH   HOH B . 
F 4 HOH   198 398 792  HOH   HOH B . 
F 4 HOH   199 399 321  HOH   HOH B . 
F 4 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HEC 
_cell.length_a           88.789 
_cell.length_b           88.789 
_cell.length_c           39.586 
_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                         7HEC 
_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          7HEC 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.79 
_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                     7HEC 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.390 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165635 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.600 
_reflns.pdbx_Rmerge_I_obs            0.050 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.700 
_reflns.B_iso_Wilson_estimate        11.850 
_reflns.pdbx_redundancy              6.300 
_reflns.pdbx_Rrim_I_all              0.054 
_reflns.pdbx_Rpim_I_all              0.021 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1045217 
_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  ? 33542 7643 ? 2.039 ? ? ? 4.400 ? 0.500  ? ? ? ? ? ? 92.900 2.316 1.073 0.328 
1 2 5.480 44.390 ? 7462  1096 ? 0.026 ? ? ? 6.800 ? 52.600 ? ? ? ? ? ? 99.900 0.028 0.011 1.000 
# 
_refine.entry_id                                 7HEC 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.3900 
_refine.pdbx_ls_sigma_F                          1.330 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.4100 
_refine.ls_number_reflns_obs                     165236 
_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                          0.1454 
_refine.ls_R_factor_R_work                       0.1447 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1588 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7962 
_refine.ls_number_reflns_R_work                  157274 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.1297 
_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                            0.1200 
_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                                67.880 
_refine.B_iso_min                                8.470 
_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                        44.3900 
_refine_hist.pdbx_number_atoms_ligand         46 
_refine_hist.number_atoms_solvent             421 
_refine_hist.number_atoms_total               3009 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           16.44 
_refine_hist.pdbx_B_iso_mean_solvent          30.43 
_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 86.0000  4551 . 0.4358 0.3912 . 235 0.0000 4786 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 98.0000  5149 . 0.3684 0.3954 . 226 0.0000 5375 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5237 . 0.3243 0.3159 . 252 0.0000 5489 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5192 . 0.2876 0.2721 . 275 0.0000 5467 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5201 . 0.2657 0.2792 . 323 0.0000 5524 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5259 . 0.2455 0.2640 . 250 0.0000 5509 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5252 . 0.2130 0.2378 . 268 0.0000 5520 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5245 . 0.1919 0.2126 . 249 0.0000 5494 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5225 . 0.1783 0.1903 . 280 0.0000 5505 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 5283 . 0.1594 0.1770 . 241 0.0000 5524 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 5267 . 0.1490 0.1777 . 250 0.0000 5517 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 5282 . 0.1387 0.1730 . 281 0.0000 5563 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5173 . 0.1314 0.1624 . 287 0.0000 5460 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5332 . 0.1239 0.1428 . 235 0.0000 5567 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5190 . 0.1258 0.1468 . 262 0.0000 5452 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5300 . 0.1266 0.1414 . 272 0.0000 5572 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5257 . 0.1263 0.1405 . 285 0.0000 5542 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5199 . 0.1316 0.1494 . 276 0.0000 5475 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5287 . 0.1273 0.1617 . 252 0.0000 5539 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5260 . 0.1251 0.1576 . 264 0.0000 5524 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5308 . 0.1182 0.1255 . 257 0.0000 5565 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5225 . 0.1148 0.1284 . 276 0.0000 5501 . 'X-RAY DIFFRACTION' 
1.5500 1.6300  30 100.0000 5290 . 0.1149 0.1326 . 261 0.0000 5551 . 'X-RAY DIFFRACTION' 
1.6300 1.7100  30 100.0000 5315 . 0.1219 0.1426 . 270 0.0000 5585 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5284 . 0.1310 0.1456 . 250 0.0000 5534 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5287 . 0.1305 0.1354 . 281 0.0000 5568 . 'X-RAY DIFFRACTION' 
1.9600 2.1600  30 100.0000 5292 . 0.1361 0.1410 . 287 0.0000 5579 . 'X-RAY DIFFRACTION' 
2.1600 2.4700  30 100.0000 5308 . 0.1348 0.1392 . 288 0.0000 5596 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5333 . 0.1481 0.1595 . 260 0.0000 5593 . 'X-RAY DIFFRACTION' 
3.1100 44.3900 30 100.0000 5491 . 0.1501 0.1716 . 269 0.0000 5760 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HEC 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003669' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HEC 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HEC A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HEC 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 7HEC SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HEC MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HEC SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HEC MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? 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 LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HEC 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 HH A TYR 42 ? B 1_555 OD1 B ASP 67 ? ? 2_654 1.57 
2 1 O  A ASP 66 ? ? 1_555 HG  B SER 1  ? B 2_655 1.59 
# 
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 ? ? 55.56 -133.84 
2 1 HIS B 86 ? ? 57.59 -128.10 
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 519 ? 5.96 . 
2 1 O ? A HOH 520 ? 5.98 . 
3 1 O ? A HOH 521 ? 7.65 . 
4 1 O ? B HOH 400 ? 6.24 . 
# 
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 
A1A9O N2   N Y N 1   
A1A9O C3   C Y N 2   
A1A9O C6   C Y N 3   
A1A9O C9   C N S 4   
A1A9O C12  C Y N 5   
A1A9O C14  C Y N 6   
A1A9O C1   C N N 7   
A1A9O C10  C N N 8   
A1A9O C11  C Y N 9   
A1A9O C13  C Y N 10  
A1A9O C15  C Y N 11  
A1A9O C16  C Y N 12  
A1A9O C2   C N R 13  
A1A9O C4   C Y N 14  
A1A9O C5   C Y N 15  
A1A9O C7   C Y N 16  
A1A9O C8   C Y N 17  
A1A9O N1   N N N 18  
A1A9O N3   N Y N 19  
A1A9O N4   N Y N 20  
A1A9O O1   O N N 21  
A1A9O H8   H N N 22  
A1A9O H2   H N N 23  
A1A9O H15  H N N 24  
A1A9O H4   H N N 25  
A1A9O H5   H N N 26  
A1A9O H3   H N N 27  
A1A9O H11  H N N 28  
A1A9O H12  H N N 29  
A1A9O H16  H N N 30  
A1A9O H17  H N N 31  
A1A9O H1   H N N 32  
A1A9O H6   H N N 33  
A1A9O H7   H N N 34  
A1A9O H9   H N N 35  
A1A9O H10  H N N 36  
A1A9O H14  H N N 37  
A1A9O H18  H N N 38  
A1A9O H13  H N N 39  
ALA   N    N N N 40  
ALA   CA   C N S 41  
ALA   C    C N N 42  
ALA   O    O N N 43  
ALA   CB   C N N 44  
ALA   OXT  O N N 45  
ALA   H    H N N 46  
ALA   H2   H N N 47  
ALA   HA   H N N 48  
ALA   HB1  H N N 49  
ALA   HB2  H N N 50  
ALA   HB3  H N N 51  
ALA   HXT  H N N 52  
ARG   N    N N N 53  
ARG   CA   C N S 54  
ARG   C    C N N 55  
ARG   O    O N N 56  
ARG   CB   C N N 57  
ARG   CG   C N N 58  
ARG   CD   C N N 59  
ARG   NE   N N N 60  
ARG   CZ   C N N 61  
ARG   NH1  N N N 62  
ARG   NH2  N N N 63  
ARG   OXT  O N N 64  
ARG   H    H N N 65  
ARG   H2   H N N 66  
ARG   HA   H N N 67  
ARG   HB2  H N N 68  
ARG   HB3  H N N 69  
ARG   HG2  H N N 70  
ARG   HG3  H N N 71  
ARG   HD2  H N N 72  
ARG   HD3  H N N 73  
ARG   HE   H N N 74  
ARG   HH11 H N N 75  
ARG   HH12 H N N 76  
ARG   HH21 H N N 77  
ARG   HH22 H N N 78  
ARG   HXT  H N N 79  
ASN   N    N N N 80  
ASN   CA   C N S 81  
ASN   C    C N N 82  
ASN   O    O N N 83  
ASN   CB   C N N 84  
ASN   CG   C N N 85  
ASN   OD1  O N N 86  
ASN   ND2  N N N 87  
ASN   OXT  O N N 88  
ASN   H    H N N 89  
ASN   H2   H N N 90  
ASN   HA   H N N 91  
ASN   HB2  H N N 92  
ASN   HB3  H N N 93  
ASN   HD21 H N N 94  
ASN   HD22 H N N 95  
ASN   HXT  H N N 96  
ASP   N    N N N 97  
ASP   CA   C N S 98  
ASP   C    C N N 99  
ASP   O    O N N 100 
ASP   CB   C N N 101 
ASP   CG   C N N 102 
ASP   OD1  O N N 103 
ASP   OD2  O N N 104 
ASP   OXT  O N N 105 
ASP   H    H N N 106 
ASP   H2   H N N 107 
ASP   HA   H N N 108 
ASP   HB2  H N N 109 
ASP   HB3  H N N 110 
ASP   HD2  H N N 111 
ASP   HXT  H N N 112 
CYS   N    N N N 113 
CYS   CA   C N R 114 
CYS   C    C N N 115 
CYS   O    O N N 116 
CYS   CB   C N N 117 
CYS   SG   S N N 118 
CYS   OXT  O N N 119 
CYS   H    H N N 120 
CYS   H2   H N N 121 
CYS   HA   H N N 122 
CYS   HB2  H N N 123 
CYS   HB3  H N N 124 
CYS   HG   H N N 125 
CYS   HXT  H N N 126 
GLN   N    N N N 127 
GLN   CA   C N S 128 
GLN   C    C N N 129 
GLN   O    O N N 130 
GLN   CB   C N N 131 
GLN   CG   C N N 132 
GLN   CD   C N N 133 
GLN   OE1  O N N 134 
GLN   NE2  N N N 135 
GLN   OXT  O N N 136 
GLN   H    H N N 137 
GLN   H2   H N N 138 
GLN   HA   H N N 139 
GLN   HB2  H N N 140 
GLN   HB3  H N N 141 
GLN   HG2  H N N 142 
GLN   HG3  H N N 143 
GLN   HE21 H N N 144 
GLN   HE22 H N N 145 
GLN   HXT  H N N 146 
GLU   N    N N N 147 
GLU   CA   C N S 148 
GLU   C    C N N 149 
GLU   O    O N N 150 
GLU   CB   C N N 151 
GLU   CG   C N N 152 
GLU   CD   C N N 153 
GLU   OE1  O N N 154 
GLU   OE2  O N N 155 
GLU   OXT  O N N 156 
GLU   H    H N N 157 
GLU   H2   H N N 158 
GLU   HA   H N N 159 
GLU   HB2  H N N 160 
GLU   HB3  H N N 161 
GLU   HG2  H N N 162 
GLU   HG3  H N N 163 
GLU   HE2  H N N 164 
GLU   HXT  H N N 165 
GLY   N    N N N 166 
GLY   CA   C N N 167 
GLY   C    C N N 168 
GLY   O    O N N 169 
GLY   OXT  O N N 170 
GLY   H    H N N 171 
GLY   H2   H N N 172 
GLY   HA2  H N N 173 
GLY   HA3  H N N 174 
GLY   HXT  H N N 175 
HIS   N    N N N 176 
HIS   CA   C N S 177 
HIS   C    C N N 178 
HIS   O    O N N 179 
HIS   CB   C N N 180 
HIS   CG   C Y N 181 
HIS   ND1  N Y N 182 
HIS   CD2  C Y N 183 
HIS   CE1  C Y N 184 
HIS   NE2  N Y N 185 
HIS   OXT  O N N 186 
HIS   H    H N N 187 
HIS   H2   H N N 188 
HIS   HA   H N N 189 
HIS   HB2  H N N 190 
HIS   HB3  H N N 191 
HIS   HD1  H N N 192 
HIS   HD2  H N N 193 
HIS   HE1  H N N 194 
HIS   HE2  H N N 195 
HIS   HXT  H N N 196 
HOH   O    O N N 197 
HOH   H1   H N N 198 
HOH   H2   H N N 199 
ILE   N    N N N 200 
ILE   CA   C N S 201 
ILE   C    C N N 202 
ILE   O    O N N 203 
ILE   CB   C N S 204 
ILE   CG1  C N N 205 
ILE   CG2  C N N 206 
ILE   CD1  C N N 207 
ILE   OXT  O N N 208 
ILE   H    H N N 209 
ILE   H2   H N N 210 
ILE   HA   H N N 211 
ILE   HB   H N N 212 
ILE   HG12 H N N 213 
ILE   HG13 H N N 214 
ILE   HG21 H N N 215 
ILE   HG22 H N N 216 
ILE   HG23 H N N 217 
ILE   HD11 H N N 218 
ILE   HD12 H N N 219 
ILE   HD13 H N N 220 
ILE   HXT  H N N 221 
LEU   N    N N N 222 
LEU   CA   C N S 223 
LEU   C    C N N 224 
LEU   O    O N N 225 
LEU   CB   C N N 226 
LEU   CG   C N N 227 
LEU   CD1  C N N 228 
LEU   CD2  C N N 229 
LEU   OXT  O N N 230 
LEU   H    H N N 231 
LEU   H2   H N N 232 
LEU   HA   H N N 233 
LEU   HB2  H N N 234 
LEU   HB3  H N N 235 
LEU   HG   H N N 236 
LEU   HD11 H N N 237 
LEU   HD12 H N N 238 
LEU   HD13 H N N 239 
LEU   HD21 H N N 240 
LEU   HD22 H N N 241 
LEU   HD23 H N N 242 
LEU   HXT  H N N 243 
LYS   N    N N N 244 
LYS   CA   C N S 245 
LYS   C    C N N 246 
LYS   O    O N N 247 
LYS   CB   C N N 248 
LYS   CG   C N N 249 
LYS   CD   C N N 250 
LYS   CE   C N N 251 
LYS   NZ   N N N 252 
LYS   OXT  O N N 253 
LYS   H    H N N 254 
LYS   H2   H N N 255 
LYS   HA   H N N 256 
LYS   HB2  H N N 257 
LYS   HB3  H N N 258 
LYS   HG2  H N N 259 
LYS   HG3  H N N 260 
LYS   HD2  H N N 261 
LYS   HD3  H N N 262 
LYS   HE2  H N N 263 
LYS   HE3  H N N 264 
LYS   HZ1  H N N 265 
LYS   HZ2  H N N 266 
LYS   HZ3  H N N 267 
LYS   HXT  H N N 268 
MET   N    N N N 269 
MET   CA   C N S 270 
MET   C    C N N 271 
MET   O    O N N 272 
MET   CB   C N N 273 
MET   CG   C N N 274 
MET   SD   S N N 275 
MET   CE   C N N 276 
MET   OXT  O N N 277 
MET   H    H N N 278 
MET   H2   H N N 279 
MET   HA   H N N 280 
MET   HB2  H N N 281 
MET   HB3  H N N 282 
MET   HG2  H N N 283 
MET   HG3  H N N 284 
MET   HE1  H N N 285 
MET   HE2  H N N 286 
MET   HE3  H N N 287 
MET   HXT  H N N 288 
PHE   N    N N N 289 
PHE   CA   C N S 290 
PHE   C    C N N 291 
PHE   O    O N N 292 
PHE   CB   C N N 293 
PHE   CG   C Y N 294 
PHE   CD1  C Y N 295 
PHE   CD2  C Y N 296 
PHE   CE1  C Y N 297 
PHE   CE2  C Y N 298 
PHE   CZ   C Y N 299 
PHE   OXT  O N N 300 
PHE   H    H N N 301 
PHE   H2   H N N 302 
PHE   HA   H N N 303 
PHE   HB2  H N N 304 
PHE   HB3  H N N 305 
PHE   HD1  H N N 306 
PHE   HD2  H N N 307 
PHE   HE1  H N N 308 
PHE   HE2  H N N 309 
PHE   HZ   H N N 310 
PHE   HXT  H N N 311 
PRO   N    N N N 312 
PRO   CA   C N S 313 
PRO   C    C N N 314 
PRO   O    O N N 315 
PRO   CB   C N N 316 
PRO   CG   C N N 317 
PRO   CD   C N N 318 
PRO   OXT  O N N 319 
PRO   H    H N N 320 
PRO   HA   H N N 321 
PRO   HB2  H N N 322 
PRO   HB3  H N N 323 
PRO   HG2  H N N 324 
PRO   HG3  H N N 325 
PRO   HD2  H N N 326 
PRO   HD3  H N N 327 
PRO   HXT  H N N 328 
SER   N    N N N 329 
SER   CA   C N S 330 
SER   C    C N N 331 
SER   O    O N N 332 
SER   CB   C N N 333 
SER   OG   O N N 334 
SER   OXT  O N N 335 
SER   H    H N N 336 
SER   H2   H N N 337 
SER   HA   H N N 338 
SER   HB2  H N N 339 
SER   HB3  H N N 340 
SER   HG   H N N 341 
SER   HXT  H N N 342 
TFA   C1   C N N 343 
TFA   C2   C N N 344 
TFA   O    O N N 345 
TFA   F1   F N N 346 
TFA   F2   F N N 347 
TFA   F3   F N N 348 
TFA   OXT  O N N 349 
TFA   HXT  H N N 350 
THR   N    N N N 351 
THR   CA   C N S 352 
THR   C    C N N 353 
THR   O    O N N 354 
THR   CB   C N R 355 
THR   OG1  O N N 356 
THR   CG2  C N N 357 
THR   OXT  O N N 358 
THR   H    H N N 359 
THR   H2   H N N 360 
THR   HA   H N N 361 
THR   HB   H N N 362 
THR   HG1  H N N 363 
THR   HG21 H N N 364 
THR   HG22 H N N 365 
THR   HG23 H N N 366 
THR   HXT  H N N 367 
TYR   N    N N N 368 
TYR   CA   C N S 369 
TYR   C    C N N 370 
TYR   O    O N N 371 
TYR   CB   C N N 372 
TYR   CG   C Y N 373 
TYR   CD1  C Y N 374 
TYR   CD2  C Y N 375 
TYR   CE1  C Y N 376 
TYR   CE2  C Y N 377 
TYR   CZ   C Y N 378 
TYR   OH   O N N 379 
TYR   OXT  O N N 380 
TYR   H    H N N 381 
TYR   H2   H N N 382 
TYR   HA   H N N 383 
TYR   HB2  H N N 384 
TYR   HB3  H N N 385 
TYR   HD1  H N N 386 
TYR   HD2  H N N 387 
TYR   HE1  H N N 388 
TYR   HE2  H N N 389 
TYR   HH   H N N 390 
TYR   HXT  H N N 391 
VAL   N    N N N 392 
VAL   CA   C N S 393 
VAL   C    C N N 394 
VAL   O    O N N 395 
VAL   CB   C N N 396 
VAL   CG1  C N N 397 
VAL   CG2  C N N 398 
VAL   OXT  O N N 399 
VAL   H    H N N 400 
VAL   H2   H N N 401 
VAL   HA   H N N 402 
VAL   HB   H N N 403 
VAL   HG11 H N N 404 
VAL   HG12 H N N 405 
VAL   HG13 H N N 406 
VAL   HG21 H N N 407 
VAL   HG22 H N N 408 
VAL   HG23 H N N 409 
VAL   HXT  H N N 410 
# 
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 
A1A9O C7  C6   doub Y N 1   
A1A9O C7  C8   sing Y N 2   
A1A9O C6  C5   sing Y N 3   
A1A9O C8  C3   doub Y N 4   
A1A9O C10 O1   sing N N 5   
A1A9O C10 C9   sing N N 6   
A1A9O C5  C4   doub Y N 7   
A1A9O C3  C4   sing Y N 8   
A1A9O C3  C2   sing N N 9   
A1A9O C1  C2   sing N N 10  
A1A9O C9  C2   sing N N 11  
A1A9O C9  N1   sing N N 12  
A1A9O N1  C11  sing N N 13  
A1A9O C11 C14  doub Y N 14  
A1A9O C11 N2   sing Y N 15  
A1A9O C15 C14  sing Y N 16  
A1A9O C15 C16  doub Y N 17  
A1A9O C14 C13  sing Y N 18  
A1A9O N2  C12  doub Y N 19  
A1A9O C16 N4   sing Y N 20  
A1A9O C13 N4   sing Y N 21  
A1A9O C13 N3   doub Y N 22  
A1A9O C12 N3   sing Y N 23  
A1A9O C6  H8   sing N N 24  
A1A9O C9  H2   sing N N 25  
A1A9O C12 H15  sing N N 26  
A1A9O C1  H4   sing N N 27  
A1A9O C1  H5   sing N N 28  
A1A9O C1  H3   sing N N 29  
A1A9O C10 H11  sing N N 30  
A1A9O C10 H12  sing N N 31  
A1A9O C15 H16  sing N N 32  
A1A9O C16 H17  sing N N 33  
A1A9O C2  H1   sing N N 34  
A1A9O C4  H6   sing N N 35  
A1A9O C5  H7   sing N N 36  
A1A9O C7  H9   sing N N 37  
A1A9O C8  H10  sing N N 38  
A1A9O N1  H14  sing N N 39  
A1A9O N4  H18  sing N N 40  
A1A9O O1  H13  sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
GLN   N   CA   sing N N 124 
GLN   N   H    sing N N 125 
GLN   N   H2   sing N N 126 
GLN   CA  C    sing N N 127 
GLN   CA  CB   sing N N 128 
GLN   CA  HA   sing N N 129 
GLN   C   O    doub N N 130 
GLN   C   OXT  sing N N 131 
GLN   CB  CG   sing N N 132 
GLN   CB  HB2  sing N N 133 
GLN   CB  HB3  sing N N 134 
GLN   CG  CD   sing N N 135 
GLN   CG  HG2  sing N N 136 
GLN   CG  HG3  sing N N 137 
GLN   CD  OE1  doub N N 138 
GLN   CD  NE2  sing N N 139 
GLN   NE2 HE21 sing N N 140 
GLN   NE2 HE22 sing N N 141 
GLN   OXT HXT  sing N N 142 
GLU   N   CA   sing N N 143 
GLU   N   H    sing N N 144 
GLU   N   H2   sing N N 145 
GLU   CA  C    sing N N 146 
GLU   CA  CB   sing N N 147 
GLU   CA  HA   sing N N 148 
GLU   C   O    doub N N 149 
GLU   C   OXT  sing N N 150 
GLU   CB  CG   sing N N 151 
GLU   CB  HB2  sing N N 152 
GLU   CB  HB3  sing N N 153 
GLU   CG  CD   sing N N 154 
GLU   CG  HG2  sing N N 155 
GLU   CG  HG3  sing N N 156 
GLU   CD  OE1  doub N N 157 
GLU   CD  OE2  sing N N 158 
GLU   OE2 HE2  sing N N 159 
GLU   OXT HXT  sing N N 160 
GLY   N   CA   sing N N 161 
GLY   N   H    sing N N 162 
GLY   N   H2   sing N N 163 
GLY   CA  C    sing N N 164 
GLY   CA  HA2  sing N N 165 
GLY   CA  HA3  sing N N 166 
GLY   C   O    doub N N 167 
GLY   C   OXT  sing N N 168 
GLY   OXT HXT  sing N N 169 
HIS   N   CA   sing N N 170 
HIS   N   H    sing N N 171 
HIS   N   H2   sing N N 172 
HIS   CA  C    sing N N 173 
HIS   CA  CB   sing N N 174 
HIS   CA  HA   sing N N 175 
HIS   C   O    doub N N 176 
HIS   C   OXT  sing N N 177 
HIS   CB  CG   sing N N 178 
HIS   CB  HB2  sing N N 179 
HIS   CB  HB3  sing N N 180 
HIS   CG  ND1  sing Y N 181 
HIS   CG  CD2  doub Y N 182 
HIS   ND1 CE1  doub Y N 183 
HIS   ND1 HD1  sing N N 184 
HIS   CD2 NE2  sing Y N 185 
HIS   CD2 HD2  sing N N 186 
HIS   CE1 NE2  sing Y N 187 
HIS   CE1 HE1  sing N N 188 
HIS   NE2 HE2  sing N N 189 
HIS   OXT HXT  sing N N 190 
HOH   O   H1   sing N N 191 
HOH   O   H2   sing N N 192 
ILE   N   CA   sing N N 193 
ILE   N   H    sing N N 194 
ILE   N   H2   sing N N 195 
ILE   CA  C    sing N N 196 
ILE   CA  CB   sing N N 197 
ILE   CA  HA   sing N N 198 
ILE   C   O    doub N N 199 
ILE   C   OXT  sing N N 200 
ILE   CB  CG1  sing N N 201 
ILE   CB  CG2  sing N N 202 
ILE   CB  HB   sing N N 203 
ILE   CG1 CD1  sing N N 204 
ILE   CG1 HG12 sing N N 205 
ILE   CG1 HG13 sing N N 206 
ILE   CG2 HG21 sing N N 207 
ILE   CG2 HG22 sing N N 208 
ILE   CG2 HG23 sing N N 209 
ILE   CD1 HD11 sing N N 210 
ILE   CD1 HD12 sing N N 211 
ILE   CD1 HD13 sing N N 212 
ILE   OXT HXT  sing N N 213 
LEU   N   CA   sing N N 214 
LEU   N   H    sing N N 215 
LEU   N   H2   sing N N 216 
LEU   CA  C    sing N N 217 
LEU   CA  CB   sing N N 218 
LEU   CA  HA   sing N N 219 
LEU   C   O    doub N N 220 
LEU   C   OXT  sing N N 221 
LEU   CB  CG   sing N N 222 
LEU   CB  HB2  sing N N 223 
LEU   CB  HB3  sing N N 224 
LEU   CG  CD1  sing N N 225 
LEU   CG  CD2  sing N N 226 
LEU   CG  HG   sing N N 227 
LEU   CD1 HD11 sing N N 228 
LEU   CD1 HD12 sing N N 229 
LEU   CD1 HD13 sing N N 230 
LEU   CD2 HD21 sing N N 231 
LEU   CD2 HD22 sing N N 232 
LEU   CD2 HD23 sing N N 233 
LEU   OXT HXT  sing N N 234 
LYS   N   CA   sing N N 235 
LYS   N   H    sing N N 236 
LYS   N   H2   sing N N 237 
LYS   CA  C    sing N N 238 
LYS   CA  CB   sing N N 239 
LYS   CA  HA   sing N N 240 
LYS   C   O    doub N N 241 
LYS   C   OXT  sing N N 242 
LYS   CB  CG   sing N N 243 
LYS   CB  HB2  sing N N 244 
LYS   CB  HB3  sing N N 245 
LYS   CG  CD   sing N N 246 
LYS   CG  HG2  sing N N 247 
LYS   CG  HG3  sing N N 248 
LYS   CD  CE   sing N N 249 
LYS   CD  HD2  sing N N 250 
LYS   CD  HD3  sing N N 251 
LYS   CE  NZ   sing N N 252 
LYS   CE  HE2  sing N N 253 
LYS   CE  HE3  sing N N 254 
LYS   NZ  HZ1  sing N N 255 
LYS   NZ  HZ2  sing N N 256 
LYS   NZ  HZ3  sing N N 257 
LYS   OXT HXT  sing N N 258 
MET   N   CA   sing N N 259 
MET   N   H    sing N N 260 
MET   N   H2   sing N N 261 
MET   CA  C    sing N N 262 
MET   CA  CB   sing N N 263 
MET   CA  HA   sing N N 264 
MET   C   O    doub N N 265 
MET   C   OXT  sing N N 266 
MET   CB  CG   sing N N 267 
MET   CB  HB2  sing N N 268 
MET   CB  HB3  sing N N 269 
MET   CG  SD   sing N N 270 
MET   CG  HG2  sing N N 271 
MET   CG  HG3  sing N N 272 
MET   SD  CE   sing N N 273 
MET   CE  HE1  sing N N 274 
MET   CE  HE2  sing N N 275 
MET   CE  HE3  sing N N 276 
MET   OXT HXT  sing N N 277 
PHE   N   CA   sing N N 278 
PHE   N   H    sing N N 279 
PHE   N   H2   sing N N 280 
PHE   CA  C    sing N N 281 
PHE   CA  CB   sing N N 282 
PHE   CA  HA   sing N N 283 
PHE   C   O    doub N N 284 
PHE   C   OXT  sing N N 285 
PHE   CB  CG   sing N N 286 
PHE   CB  HB2  sing N N 287 
PHE   CB  HB3  sing N N 288 
PHE   CG  CD1  doub Y N 289 
PHE   CG  CD2  sing Y N 290 
PHE   CD1 CE1  sing Y N 291 
PHE   CD1 HD1  sing N N 292 
PHE   CD2 CE2  doub Y N 293 
PHE   CD2 HD2  sing N N 294 
PHE   CE1 CZ   doub Y N 295 
PHE   CE1 HE1  sing N N 296 
PHE   CE2 CZ   sing Y N 297 
PHE   CE2 HE2  sing N N 298 
PHE   CZ  HZ   sing N N 299 
PHE   OXT HXT  sing N N 300 
PRO   N   CA   sing N N 301 
PRO   N   CD   sing N N 302 
PRO   N   H    sing N N 303 
PRO   CA  C    sing N N 304 
PRO   CA  CB   sing N N 305 
PRO   CA  HA   sing N N 306 
PRO   C   O    doub N N 307 
PRO   C   OXT  sing N N 308 
PRO   CB  CG   sing N N 309 
PRO   CB  HB2  sing N N 310 
PRO   CB  HB3  sing N N 311 
PRO   CG  CD   sing N N 312 
PRO   CG  HG2  sing N N 313 
PRO   CG  HG3  sing N N 314 
PRO   CD  HD2  sing N N 315 
PRO   CD  HD3  sing N N 316 
PRO   OXT HXT  sing N N 317 
SER   N   CA   sing N N 318 
SER   N   H    sing N N 319 
SER   N   H2   sing N N 320 
SER   CA  C    sing N N 321 
SER   CA  CB   sing N N 322 
SER   CA  HA   sing N N 323 
SER   C   O    doub N N 324 
SER   C   OXT  sing N N 325 
SER   CB  OG   sing N N 326 
SER   CB  HB2  sing N N 327 
SER   CB  HB3  sing N N 328 
SER   OG  HG   sing N N 329 
SER   OXT HXT  sing N N 330 
TFA   C1  C2   sing N N 331 
TFA   C1  O    doub N N 332 
TFA   C1  OXT  sing N N 333 
TFA   C2  F1   sing N N 334 
TFA   C2  F2   sing N N 335 
TFA   C2  F3   sing N N 336 
TFA   OXT HXT  sing N N 337 
THR   N   CA   sing N N 338 
THR   N   H    sing N N 339 
THR   N   H2   sing N N 340 
THR   CA  C    sing N N 341 
THR   CA  CB   sing N N 342 
THR   CA  HA   sing N N 343 
THR   C   O    doub N N 344 
THR   C   OXT  sing N N 345 
THR   CB  OG1  sing N N 346 
THR   CB  CG2  sing N N 347 
THR   CB  HB   sing N N 348 
THR   OG1 HG1  sing N N 349 
THR   CG2 HG21 sing N N 350 
THR   CG2 HG22 sing N N 351 
THR   CG2 HG23 sing N N 352 
THR   OXT HXT  sing N N 353 
TYR   N   CA   sing N N 354 
TYR   N   H    sing N N 355 
TYR   N   H2   sing N N 356 
TYR   CA  C    sing N N 357 
TYR   CA  CB   sing N N 358 
TYR   CA  HA   sing N N 359 
TYR   C   O    doub N N 360 
TYR   C   OXT  sing N N 361 
TYR   CB  CG   sing N N 362 
TYR   CB  HB2  sing N N 363 
TYR   CB  HB3  sing N N 364 
TYR   CG  CD1  doub Y N 365 
TYR   CG  CD2  sing Y N 366 
TYR   CD1 CE1  sing Y N 367 
TYR   CD1 HD1  sing N N 368 
TYR   CD2 CE2  doub Y N 369 
TYR   CD2 HD2  sing N N 370 
TYR   CE1 CZ   doub Y N 371 
TYR   CE1 HE1  sing N N 372 
TYR   CE2 CZ   sing Y N 373 
TYR   CE2 HE2  sing N N 374 
TYR   CZ  OH   sing N N 375 
TYR   OH  HH   sing N N 376 
TYR   OXT HXT  sing N N 377 
VAL   N   CA   sing N N 378 
VAL   N   H    sing N N 379 
VAL   N   H2   sing N N 380 
VAL   CA  C    sing N N 381 
VAL   CA  CB   sing N N 382 
VAL   CA  HA   sing N N 383 
VAL   C   O    doub N N 384 
VAL   C   OXT  sing N N 385 
VAL   CB  CG1  sing N N 386 
VAL   CB  CG2  sing N N 387 
VAL   CB  HB   sing N N 388 
VAL   CG1 HG11 sing N N 389 
VAL   CG1 HG12 sing N N 390 
VAL   CG1 HG13 sing N N 391 
VAL   CG2 HG21 sing N N 392 
VAL   CG2 HG22 sing N N 393 
VAL   CG2 HG23 sing N N 394 
VAL   OXT HXT  sing N N 395 
# 
_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                    7HEC 
_atom_sites.fract_transf_matrix[1][1]   0.011263 
_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]   0.011263 
_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]   0.025261 
_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 
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    . VAL   A 1 3   ? 19.585 -16.165 22.296  1.00 55.21 ?  3   VAL   A N    1 
ATOM   2    C CA   . VAL   A 1 3   ? 18.639 -15.071 22.481  1.00 54.61 ?  3   VAL   A CA   1 
ATOM   3    C C    . VAL   A 1 3   ? 19.303 -13.737 22.161  1.00 52.39 ?  3   VAL   A C    1 
ATOM   4    O O    . VAL   A 1 3   ? 20.425 -13.474 22.593  1.00 53.01 ?  3   VAL   A O    1 
ATOM   5    C CB   . VAL   A 1 3   ? 18.043 -15.079 23.904  1.00 55.69 ?  3   VAL   A CB   1 
ATOM   6    C CG1  . VAL   A 1 3   ? 17.036 -13.948 24.071  1.00 55.99 ?  3   VAL   A CG1  1 
ATOM   7    C CG2  . VAL   A 1 3   ? 17.392 -16.424 24.198  1.00 56.02 ?  3   VAL   A CG2  1 
ATOM   8    H HA   . VAL   A 1 3   ? 17.904 -15.183 21.862  1.00 65.53 ?  3   VAL   A HA   1 
ATOM   9    H HB   . VAL   A 1 3   ? 18.755 -14.944 24.550  1.00 66.83 ?  3   VAL   A HB   1 
ATOM   10   H HG11 . VAL   A 1 3   ? 16.551 -14.076 24.902  1.00 67.19 ?  3   VAL   A HG11 1 
ATOM   11   H HG12 . VAL   A 1 3   ? 17.508 -13.101 24.093  1.00 67.19 ?  3   VAL   A HG12 1 
ATOM   12   H HG13 . VAL   A 1 3   ? 16.417 -13.964 23.324  1.00 67.19 ?  3   VAL   A HG13 1 
ATOM   13   H HG21 . VAL   A 1 3   ? 16.956 -16.381 25.064  1.00 67.23 ?  3   VAL   A HG21 1 
ATOM   14   H HG22 . VAL   A 1 3   ? 16.738 -16.614 23.507  1.00 67.23 ?  3   VAL   A HG22 1 
ATOM   15   H HG23 . VAL   A 1 3   ? 18.076 -17.111 24.205  1.00 67.23 ?  3   VAL   A HG23 1 
ATOM   16   N N    . ASN   A 1 4   ? 18.605 -12.903 21.392  1.00 48.96 ?  4   ASN   A N    1 
ATOM   17   C CA   . ASN   A 1 4   ? 19.054 -11.553 21.076  1.00 45.15 ?  4   ASN   A CA   1 
ATOM   18   C C    . ASN   A 1 4   ? 17.906 -10.578 21.321  1.00 41.75 ?  4   ASN   A C    1 
ATOM   19   O O    . ASN   A 1 4   ? 16.797 -10.973 21.695  1.00 41.57 ?  4   ASN   A O    1 
ATOM   20   C CB   . ASN   A 1 4   ? 19.608 -11.457 19.647  1.00 44.38 ?  4   ASN   A CB   1 
ATOM   21   C CG   . ASN   A 1 4   ? 18.601 -11.868 18.597  1.00 43.43 ?  4   ASN   A CG   1 
ATOM   22   O OD1  . ASN   A 1 4   ? 17.481 -11.360 18.563  1.00 43.00 ?  4   ASN   A OD1  1 
ATOM   23   N ND2  . ASN   A 1 4   ? 18.995 -12.799 17.733  1.00 43.09 ?  4   ASN   A ND2  1 
ATOM   24   H H    . ASN   A 1 4   ? 17.847 -13.104 21.036  1.00 58.75 ?  4   ASN   A H    1 
ATOM   25   H HA   . ASN   A 1 4   ? 19.775 -11.323 21.676  1.00 54.18 ?  4   ASN   A HA   1 
ATOM   26   H HB2  . ASN   A 1 4   ? 19.867 -10.538 19.470  1.00 53.26 ?  4   ASN   A HB2  1 
ATOM   27   H HB3  . ASN   A 1 4   ? 20.379 -12.039 19.568  1.00 53.26 ?  4   ASN   A HB3  1 
ATOM   28   H HD21 . ASN   A 1 4   ? 18.461 -13.068 17.115  1.00 51.71 ?  4   ASN   A HD21 1 
ATOM   29   H HD22 . ASN   A 1 4   ? 19.787 -13.132 17.790  1.00 51.71 ?  4   ASN   A HD22 1 
ATOM   30   N N    . SER   A 1 5   ? 18.175 -9.290  21.106  1.00 38.31 ?  5   SER   A N    1 
ATOM   31   C CA   . SER   A 1 5   ? 17.256 -8.224  21.485  1.00 34.94 ?  5   SER   A CA   1 
ATOM   32   C C    . SER   A 1 5   ? 16.377 -7.739  20.333  1.00 30.91 ?  5   SER   A C    1 
ATOM   33   O O    . SER   A 1 5   ? 15.658 -6.748  20.496  1.00 31.10 ?  5   SER   A O    1 
ATOM   34   C CB   . SER   A 1 5   ? 18.025 -7.050  22.098  1.00 35.96 ?  5   SER   A CB   1 
ATOM   35   O OG   . SER   A 1 5   ? 18.904 -6.466  21.153  1.00 36.53 ?  5   SER   A OG   1 
ATOM   36   H H    . SER   A 1 5   ? 18.898 -9.009  20.732  1.00 45.98 ?  5   SER   A H    1 
ATOM   37   H HA   . SER   A 1 5   ? 16.668 -8.564  22.174  1.00 41.93 ?  5   SER   A HA   1 
ATOM   38   H HB2  . SER   A 1 5   ? 17.392 -6.377  22.395  1.00 43.15 ?  5   SER   A HB2  1 
ATOM   39   H HB3  . SER   A 1 5   ? 18.542 -7.370  22.857  1.00 43.15 ?  5   SER   A HB3  1 
ATOM   40   H HG   . SER   A 1 5   ? 19.322 -5.825  21.507  1.00 43.84 ?  5   SER   A HG   1 
ATOM   41   N N    . PHE   A 1 6   ? 16.410 -8.403  19.181  1.00 26.28 ?  6   PHE   A N    1 
ATOM   42   C CA   . PHE   A 1 6   ? 15.506 -8.040  18.095  1.00 22.33 ?  6   PHE   A CA   1 
ATOM   43   C C    . PHE   A 1 6   ? 14.074 -8.402  18.480  1.00 22.47 ?  6   PHE   A C    1 
ATOM   44   O O    . PHE   A 1 6   ? 13.807 -9.518  18.929  1.00 24.28 ?  6   PHE   A O    1 
ATOM   45   C CB   . PHE   A 1 6   ? 15.910 -8.766  16.817  1.00 20.43 ?  6   PHE   A CB   1 
ATOM   46   C CG   . PHE   A 1 6   ? 17.200 -8.263  16.218  1.00 19.20 ?  6   PHE   A CG   1 
ATOM   47   C CD1  . PHE   A 1 6   ? 17.228 -7.078  15.508  1.00 18.70 ?  6   PHE   A CD1  1 
ATOM   48   C CD2  . PHE   A 1 6   ? 18.378 -8.978  16.363  1.00 19.78 ?  6   PHE   A CD2  1 
ATOM   49   C CE1  . PHE   A 1 6   ? 18.406 -6.610  14.952  1.00 18.84 ?  6   PHE   A CE1  1 
ATOM   50   C CE2  . PHE   A 1 6   ? 19.559 -8.518  15.806  1.00 19.89 ?  6   PHE   A CE2  1 
ATOM   51   C CZ   . PHE   A 1 6   ? 19.571 -7.330  15.102  1.00 19.24 ?  6   PHE   A CZ   1 
ATOM   52   H H    . PHE   A 1 6   ? 16.938 -9.061  19.009  1.00 31.55 ?  6   PHE   A H    1 
ATOM   53   H HA   . PHE   A 1 6   ? 15.550 -7.089  17.948  1.00 26.80 ?  6   PHE   A HA   1 
ATOM   54   H HB2  . PHE   A 1 6   ? 16.017 -9.712  17.016  1.00 24.52 ?  6   PHE   A HB2  1 
ATOM   55   H HB3  . PHE   A 1 6   ? 15.206 -8.650  16.161  1.00 24.52 ?  6   PHE   A HB3  1 
ATOM   56   H HD1  . PHE   A 1 6   ? 16.444 -6.589  15.404  1.00 22.44 ?  6   PHE   A HD1  1 
ATOM   57   H HD2  . PHE   A 1 6   ? 18.370 -9.781  16.841  1.00 23.74 ?  6   PHE   A HD2  1 
ATOM   58   H HE1  . PHE   A 1 6   ? 18.414 -5.811  14.476  1.00 22.61 ?  6   PHE   A HE1  1 
ATOM   59   H HE2  . PHE   A 1 6   ? 20.344 -9.005  15.913  1.00 23.87 ?  6   PHE   A HE2  1 
ATOM   60   H HZ   . PHE   A 1 6   ? 20.363 -7.017  14.730  1.00 23.09 ?  6   PHE   A HZ   1 
ATOM   61   N N    A SER   A 1 7   ? 13.135 -7.484  18.237  0.72 21.76 ?  7   SER   A N    1 
ATOM   62   N N    B SER   A 1 7   ? 13.169 -7.434  18.349  0.28 21.94 ?  7   SER   A N    1 
ATOM   63   C CA   A SER   A 1 7   ? 11.754 -7.653  18.679  0.72 21.93 ?  7   SER   A CA   1 
ATOM   64   C CA   B SER   A 1 7   ? 11.839 -7.502  18.937  0.28 21.65 ?  7   SER   A CA   1 
ATOM   65   C C    A SER   A 1 7   ? 10.770 -7.409  17.539  0.72 19.51 ?  7   SER   A C    1 
ATOM   66   C C    B SER   A 1 7   ? 10.790 -7.250  17.866  0.28 20.50 ?  7   SER   A C    1 
ATOM   67   O O    A SER   A 1 7   ? 10.989 -6.538  16.692  0.72 19.60 ?  7   SER   A O    1 
ATOM   68   O O    B SER   A 1 7   ? 10.933 -6.340  17.045  0.28 20.56 ?  7   SER   A O    1 
ATOM   69   C CB   A SER   A 1 7   ? 11.444 -6.694  19.837  0.72 24.41 ?  7   SER   A CB   1 
ATOM   70   C CB   B SER   A 1 7   ? 11.695 -6.452  20.051  0.28 22.14 ?  7   SER   A CB   1 
ATOM   71   O OG   A SER   A 1 7   ? 10.125 -6.884  20.316  0.72 26.42 ?  7   SER   A OG   1 
ATOM   72   O OG   B SER   A 1 7   ? 10.334 -6.191  20.343  0.28 22.63 ?  7   SER   A OG   1 
ATOM   73   H H    A SER   A 1 7   ? 13.280 -6.755  17.805  0.72 26.12 ?  7   SER   A H    1 
ATOM   74   H H    B SER   A 1 7   ? 13.307 -6.712  17.904  0.28 26.34 ?  7   SER   A H    1 
ATOM   75   H HA   A SER   A 1 7   ? 11.628 -8.558  18.998  0.72 26.32 ?  7   SER   A HA   1 
ATOM   76   H HA   B SER   A 1 7   ? 11.687 -8.378  19.324  0.28 25.99 ?  7   SER   A HA   1 
ATOM   77   H HB2  A SER   A 1 7   ? 12.068 -6.862  20.562  0.72 29.30 ?  7   SER   A HB2  1 
ATOM   78   H HB2  B SER   A 1 7   ? 12.127 -6.783  20.856  0.28 26.58 ?  7   SER   A HB2  1 
ATOM   79   H HB3  A SER   A 1 7   ? 11.543 -5.780  19.524  0.72 29.30 ?  7   SER   A HB3  1 
ATOM   80   H HB3  B SER   A 1 7   ? 12.121 -5.629  19.765  0.28 26.58 ?  7   SER   A HB3  1 
ATOM   81   H HG   A SER   A 1 7   ? 9.970  -6.348  20.944  0.72 31.71 ?  7   SER   A HG   1 
ATOM   82   H HG   B SER   A 1 7   ? 10.274 -5.611  20.949  0.28 27.16 ?  7   SER   A HG   1 
ATOM   83   N N    A GLY   A 1 8   ? 9.678  -8.178  17.528  0.72 17.79 ?  8   GLY   A N    1 
ATOM   84   N N    B GLY   A 1 8   ? 9.735  -8.062  17.879  0.28 19.31 ?  8   GLY   A N    1 
ATOM   85   C CA   A GLY   A 1 8   ? 8.591  -7.937  16.599  0.72 16.95 ?  8   GLY   A CA   1 
ATOM   86   C CA   B GLY   A 1 8   ? 8.636  -7.884  16.957  0.28 18.14 ?  8   GLY   A CA   1 
ATOM   87   C C    A GLY   A 1 8   ? 8.803  -8.437  15.189  0.72 15.82 ?  8   GLY   A C    1 
ATOM   88   C C    B GLY   A 1 8   ? 8.870  -8.408  15.562  0.28 16.49 ?  8   GLY   A C    1 
ATOM   89   O O    A GLY   A 1 8   ? 8.080  -8.013  14.281  0.72 16.20 ?  8   GLY   A O    1 
ATOM   90   O O    B GLY   A 1 8   ? 8.061  -8.124  14.671  0.28 16.58 ?  8   GLY   A O    1 
ATOM   91   H H    A GLY   A 1 8   ? 9.553  -8.845  18.057  0.72 21.35 ?  8   GLY   A H    1 
ATOM   92   H H    B GLY   A 1 8   ? 9.637  -8.727  18.416  0.28 23.17 ?  8   GLY   A H    1 
ATOM   93   H HA2  A GLY   A 1 8   ? 7.788  -8.352  16.954  0.72 20.34 ?  8   GLY   A HA2  1 
ATOM   94   H HA2  B GLY   A 1 8   ? 7.854  -8.333  17.306  0.28 21.78 ?  8   GLY   A HA2  1 
ATOM   95   H HA3  A GLY   A 1 8   ? 8.432  -6.980  16.553  0.72 20.34 ?  8   GLY   A HA3  1 
ATOM   96   H HA3  B GLY   A 1 8   ? 8.436  -6.938  16.886  0.28 21.78 ?  8   GLY   A HA3  1 
ATOM   97   N N    A TYR   A 1 9   ? 9.768  -9.329  14.969  0.72 14.52 ?  9   TYR   A N    1 
ATOM   98   N N    B TYR   A 1 9   ? 9.942  -9.163  15.335  0.28 15.32 ?  9   TYR   A N    1 
ATOM   99   C CA   A TYR   A 1 9   ? 10.037 -9.863  13.640  0.72 13.22 ?  9   TYR   A CA   1 
ATOM   100  C CA   B TYR   A 1 9   ? 10.216 -9.687  14.006  0.28 14.33 ?  9   TYR   A CA   1 
ATOM   101  C C    A TYR   A 1 9   ? 9.176  -11.089 13.360  0.72 12.64 ?  9   TYR   A C    1 
ATOM   102  C C    B TYR   A 1 9   ? 9.382  -10.929 13.725  0.28 14.00 ?  9   TYR   A C    1 
ATOM   103  O O    A TYR   A 1 9   ? 8.915  -11.907 14.248  0.72 14.44 ?  9   TYR   A O    1 
ATOM   104  O O    B TYR   A 1 9   ? 9.160  -11.764 14.607  0.28 15.11 ?  9   TYR   A O    1 
ATOM   105  C CB   A TYR   A 1 9   ? 11.512 -10.257 13.488  0.72 13.37 ?  9   TYR   A CB   1 
ATOM   106  C CB   B TYR   A 1 9   ? 11.705 -9.997  13.837  0.28 14.16 ?  9   TYR   A CB   1 
ATOM   107  C CG   A TYR   A 1 9   ? 12.449 -9.086  13.357  0.72 14.38 ?  9   TYR   A CG   1 
ATOM   108  C CG   B TYR   A 1 9   ? 12.528 -8.758  13.565  0.28 14.00 ?  9   TYR   A CG   1 
ATOM   109  C CD1  A TYR   A 1 9   ? 12.802 -8.336  14.469  0.72 14.66 ?  9   TYR   A CD1  1 
ATOM   110  C CD1  B TYR   A 1 9   ? 12.760 -7.828  14.567  0.28 14.09 ?  9   TYR   A CD1  1 
ATOM   111  C CD2  A TYR   A 1 9   ? 12.967 -8.722  12.122  0.72 14.85 ?  9   TYR   A CD2  1 
ATOM   112  C CD2  B TYR   A 1 9   ? 13.053 -8.508  12.303  0.28 13.45 ?  9   TYR   A CD2  1 
ATOM   113  C CE1  A TYR   A 1 9   ? 13.644 -7.253  14.357  0.72 15.46 ?  9   TYR   A CE1  1 
ATOM   114  C CE1  B TYR   A 1 9   ? 13.496 -6.686  14.325  0.28 13.56 ?  9   TYR   A CE1  1 
ATOM   115  C CE2  A TYR   A 1 9   ? 13.809 -7.643  11.999  0.72 15.20 ?  9   TYR   A CE2  1 
ATOM   116  C CE2  B TYR   A 1 9   ? 13.792 -7.366  12.050  0.28 13.05 ?  9   TYR   A CE2  1 
ATOM   117  C CZ   A TYR   A 1 9   ? 14.146 -6.911  13.120  0.72 15.61 ?  9   TYR   A CZ   1 
ATOM   118  C CZ   B TYR   A 1 9   ? 14.010 -6.462  13.066  0.28 13.07 ?  9   TYR   A CZ   1 
ATOM   119  O OH   A TYR   A 1 9   ? 14.984 -5.832  12.995  0.72 17.24 ?  9   TYR   A OH   1 
ATOM   120  O OH   B TYR   A 1 9   ? 14.741 -5.324  12.823  0.28 13.21 ?  9   TYR   A OH   1 
ATOM   121  H H    A TYR   A 1 9   ? 10.276 -9.645  15.579  0.72 17.43 ?  9   TYR   A H    1 
ATOM   122  H H    B TYR   A 1 9   ? 10.528 -9.379  15.932  0.28 18.38 ?  9   TYR   A H    1 
ATOM   123  H HA   A TYR   A 1 9   ? 9.831  -9.185  12.972  0.72 15.88 ?  9   TYR   A HA   1 
ATOM   124  H HA   B TYR   A 1 9   ? 9.979  -9.014  13.352  0.28 17.21 ?  9   TYR   A HA   1 
ATOM   125  H HB2  A TYR   A 1 9   ? 11.778 -10.775 14.263  0.72 16.05 ?  9   TYR   A HB2  1 
ATOM   126  H HB2  B TYR   A 1 9   ? 12.039 -10.414 14.647  0.28 17.00 ?  9   TYR   A HB2  1 
ATOM   127  H HB3  A TYR   A 1 9   ? 11.593 -10.797 12.687  0.72 16.05 ?  9   TYR   A HB3  1 
ATOM   128  H HB3  B TYR   A 1 9   ? 11.813 -10.603 13.086  0.28 17.00 ?  9   TYR   A HB3  1 
ATOM   129  H HD1  A TYR   A 1 9   ? 12.454 -8.565  15.304  0.72 17.60 ?  9   TYR   A HD1  1 
ATOM   130  H HD1  B TYR   A 1 9   ? 12.412 -7.978  15.417  0.28 16.91 ?  9   TYR   A HD1  1 
ATOM   131  H HD2  A TYR   A 1 9   ? 12.739 -9.218  11.366  0.72 17.83 ?  9   TYR   A HD2  1 
ATOM   132  H HD2  B TYR   A 1 9   ? 12.906 -9.119  11.617  0.28 16.15 ?  9   TYR   A HD2  1 
ATOM   133  H HE1  A TYR   A 1 9   ? 13.877 -6.762  15.111  0.72 18.55 ?  9   TYR   A HE1  1 
ATOM   134  H HE1  B TYR   A 1 9   ? 13.646 -6.073  15.006  0.28 16.28 ?  9   TYR   A HE1  1 
ATOM   135  H HE2  A TYR   A 1 9   ? 14.161 -7.416  11.167  0.72 18.24 ?  9   TYR   A HE2  1 
ATOM   136  H HE2  B TYR   A 1 9   ? 14.145 -7.210  11.201  0.28 15.66 ?  9   TYR   A HE2  1 
ATOM   137  H HH   A TYR   A 1 9   ? 15.124 -5.491  13.748  0.72 20.69 ?  9   TYR   A HH   1 
ATOM   138  H HH   B TYR   A 1 9   ? 14.820 -4.872  13.528  0.28 15.86 ?  9   TYR   A HH   1 
ATOM   139  N N    A LEU   A 1 10  ? 8.743  -11.208 12.111  0.72 12.05 ?  10  LEU   A N    1 
ATOM   140  N N    B LEU   A 1 10  ? 8.917  -11.036 12.484  0.28 13.31 ?  10  LEU   A N    1 
ATOM   141  C CA   A LEU   A 1 10  ? 8.166  -12.447 11.609  0.72 11.78 ?  10  LEU   A CA   1 
ATOM   142  C CA   B LEU   A 1 10  ? 8.202  -12.211 12.010  0.28 13.50 ?  10  LEU   A CA   1 
ATOM   143  C C    A LEU   A 1 10  ? 9.301  -13.382 11.191  0.72 12.01 ?  10  LEU   A C    1 
ATOM   144  C C    B LEU   A 1 10  ? 9.231  -13.205 11.485  0.28 12.73 ?  10  LEU   A C    1 
ATOM   145  O O    A LEU   A 1 10  ? 10.282 -12.950 10.580  0.72 12.60 ?  10  LEU   A O    1 
ATOM   146  O O    B LEU   A 1 10  ? 10.042 -12.866 10.616  0.28 12.80 ?  10  LEU   A O    1 
ATOM   147  C CB   A LEU   A 1 10  ? 7.279  -12.133 10.406  0.72 12.26 ?  10  LEU   A CB   1 
ATOM   148  C CB   B LEU   A 1 10  ? 7.232  -11.820 10.897  0.28 13.99 ?  10  LEU   A CB   1 
ATOM   149  C CG   A LEU   A 1 10  ? 6.620  -13.314 9.695   0.72 15.10 ?  10  LEU   A CG   1 
ATOM   150  C CG   B LEU   A 1 10  ? 6.461  -12.973 10.261  0.28 15.00 ?  10  LEU   A CG   1 
ATOM   151  C CD1  A LEU   A 1 10  ? 5.584  -13.960 10.587  0.72 16.74 ?  10  LEU   A CD1  1 
ATOM   152  C CD1  B LEU   A 1 10  ? 5.453  -13.540 11.246  0.28 15.82 ?  10  LEU   A CD1  1 
ATOM   153  C CD2  A LEU   A 1 10  ? 6.005  -12.884 8.371   0.72 16.67 ?  10  LEU   A CD2  1 
ATOM   154  C CD2  B LEU   A 1 10  ? 5.779  -12.486 9.000   0.28 15.99 ?  10  LEU   A CD2  1 
ATOM   155  H H    A LEU   A 1 10  ? 8.770  -10.576 11.520  0.72 14.46 ?  10  LEU   A H    1 
ATOM   156  H H    B LEU   A 1 10  ? 9.016  -10.427 11.884  0.28 15.98 ?  10  LEU   A H    1 
ATOM   157  H HA   A LEU   A 1 10  ? 7.631  -12.871 12.301  0.72 14.14 ?  10  LEU   A HA   1 
ATOM   158  H HA   B LEU   A 1 10  ? 7.702  -12.617 12.737  0.28 16.20 ?  10  LEU   A HA   1 
ATOM   159  H HB2  A LEU   A 1 10  ? 6.565  -11.549 10.698  0.72 14.72 ?  10  LEU   A HB2  1 
ATOM   160  H HB2  B LEU   A 1 10  ? 6.575  -11.200 11.259  0.28 16.79 ?  10  LEU   A HB2  1 
ATOM   161  H HB3  A LEU   A 1 10  ? 7.820  -11.675 9.745   0.72 14.72 ?  10  LEU   A HB3  1 
ATOM   162  H HB3  B LEU   A 1 10  ? 7.732  -11.381 10.191  0.28 16.79 ?  10  LEU   A HB3  1 
ATOM   163  H HG   A LEU   A 1 10  ? 7.297  -13.985 9.500   0.72 18.13 ?  10  LEU   A HG   1 
ATOM   164  H HG   B LEU   A 1 10  ? 7.079  -13.682 10.016  0.28 18.01 ?  10  LEU   A HG   1 
ATOM   165  H HD11 A LEU   A 1 10  ? 5.210  -14.733 10.134  0.72 20.09 ?  10  LEU   A HD11 1 
ATOM   166  H HD11 B LEU   A 1 10  ? 4.981  -14.275 10.826  0.28 18.98 ?  10  LEU   A HD11 1 
ATOM   167  H HD12 A LEU   A 1 10  ? 6.006  -14.238 11.416  0.72 20.09 ?  10  LEU   A HD12 1 
ATOM   168  H HD12 B LEU   A 1 10  ? 5.923  -13.856 12.035  0.28 18.98 ?  10  LEU   A HD12 1 
ATOM   169  H HD13 A LEU   A 1 10  ? 4.884  -13.316 10.775  0.72 20.09 ?  10  LEU   A HD13 1 
ATOM   170  H HD13 B LEU   A 1 10  ? 4.828  -12.841 11.493  0.28 18.98 ?  10  LEU   A HD13 1 
ATOM   171  H HD21 A LEU   A 1 10  ? 5.597  -13.658 7.949   0.72 20.01 ?  10  LEU   A HD21 1 
ATOM   172  H HD21 B LEU   A 1 10  ? 5.285  -13.220 8.607   0.28 19.19 ?  10  LEU   A HD21 1 
ATOM   173  H HD22 A LEU   A 1 10  ? 5.335  -12.208 8.544   0.72 20.01 ?  10  LEU   A HD22 1 
ATOM   174  H HD22 B LEU   A 1 10  ? 5.177  -11.763 9.231   0.28 19.19 ?  10  LEU   A HD22 1 
ATOM   175  H HD23 A LEU   A 1 10  ? 6.704  -12.527 7.803   0.72 20.01 ?  10  LEU   A HD23 1 
ATOM   176  H HD23 B LEU   A 1 10  ? 6.455  -12.170 8.381   0.28 19.19 ?  10  LEU   A HD23 1 
ATOM   177  N N    A LYS   A 1 11  ? 9.175  -14.664 11.535  0.72 11.86 ?  11  LYS   A N    1 
ATOM   178  N N    B LYS   A 1 11  ? 9.205  -14.421 12.017  0.28 12.18 ?  11  LYS   A N    1 
ATOM   179  C CA   A LYS   A 1 11  ? 10.183 -15.668 11.208  0.72 12.26 ?  11  LYS   A CA   1 
ATOM   180  C CA   B LYS   A 1 11  ? 10.135 -15.452 11.578  0.28 12.05 ?  11  LYS   A CA   1 
ATOM   181  C C    A LYS   A 1 11  ? 9.848  -16.276 9.852   0.72 12.31 ?  11  LYS   A C    1 
ATOM   182  C C    B LYS   A 1 11  ? 9.724  -15.941 10.195  0.28 11.08 ?  11  LYS   A C    1 
ATOM   183  O O    A LYS   A 1 11  ? 8.788  -16.885 9.693   0.72 14.28 ?  11  LYS   A O    1 
ATOM   184  O O    B LYS   A 1 11  ? 8.589  -16.387 9.997   0.28 11.08 ?  11  LYS   A O    1 
ATOM   185  C CB   A LYS   A 1 11  ? 10.214 -16.740 12.301  0.72 12.78 ?  11  LYS   A CB   1 
ATOM   186  C CB   B LYS   A 1 11  ? 10.145 -16.602 12.584  0.28 12.29 ?  11  LYS   A CB   1 
ATOM   187  C CG   A LYS   A 1 11  ? 11.236 -17.847 12.116  0.72 13.42 ?  11  LYS   A CG   1 
ATOM   188  C CG   B LYS   A 1 11  ? 11.204 -17.668 12.325  0.28 12.62 ?  11  LYS   A CG   1 
ATOM   189  C CD   A LYS   A 1 11  ? 11.315 -18.679 13.398  0.72 14.05 ?  11  LYS   A CD   1 
ATOM   190  C CD   B LYS   A 1 11  ? 11.227 -18.702 13.449  0.28 13.17 ?  11  LYS   A CD   1 
ATOM   191  C CE   A LYS   A 1 11  ? 12.293 -19.843 13.302  0.72 14.35 ?  11  LYS   A CE   1 
ATOM   192  C CE   B LYS   A 1 11  ? 12.251 -19.806 13.205  0.28 13.36 ?  11  LYS   A CE   1 
ATOM   193  N NZ   A LYS   A 1 11  ? 13.676 -19.403 12.977  0.72 14.57 ?  11  LYS   A NZ   1 
ATOM   194  N NZ   B LYS   A 1 11  ? 13.650 -19.293 13.152  0.28 13.37 ?  11  LYS   A NZ   1 
ATOM   195  H H    A LYS   A 1 11  ? 8.493  -14.985 11.955  0.72 14.24 ?  11  LYS   A H    1 
ATOM   196  H H    B LYS   A 1 11  ? 8.658  -14.667 12.630  0.28 14.62 ?  11  LYS   A H    1 
ATOM   197  H HA   A LYS   A 1 11  ? 11.055 -15.248 11.155  0.72 14.72 ?  11  LYS   A HA   1 
ATOM   198  H HA   B LYS   A 1 11  ? 11.025 -15.076 11.519  0.28 14.46 ?  11  LYS   A HA   1 
ATOM   199  H HB2  A LYS   A 1 11  ? 10.409 -16.304 13.146  0.72 15.34 ?  11  LYS   A HB2  1 
ATOM   200  H HB2  B LYS   A 1 11  ? 10.306 -16.232 13.467  0.28 14.75 ?  11  LYS   A HB2  1 
ATOM   201  H HB3  A LYS   A 1 11  ? 9.339  -17.154 12.347  0.72 15.34 ?  11  LYS   A HB3  1 
ATOM   202  H HB3  B LYS   A 1 11  ? 9.277  -17.033 12.565  0.28 14.75 ?  11  LYS   A HB3  1 
ATOM   203  H HG2  A LYS   A 1 11  ? 10.961 -18.427 11.387  0.72 16.11 ?  11  LYS   A HG2  1 
ATOM   204  H HG2  B LYS   A 1 11  ? 11.002 -18.126 11.495  0.28 15.15 ?  11  LYS   A HG2  1 
ATOM   205  H HG3  A LYS   A 1 11  ? 12.107 -17.465 11.942  0.72 16.11 ?  11  LYS   A HG3  1 
ATOM   206  H HG3  B LYS   A 1 11  ? 12.077 -17.252 12.277  0.28 15.15 ?  11  LYS   A HG3  1 
ATOM   207  H HD2  A LYS   A 1 11  ? 11.597 -18.109 14.129  0.72 16.86 ?  11  LYS   A HD2  1 
ATOM   208  H HD2  B LYS   A 1 11  ? 11.452 -18.262 14.283  0.28 15.81 ?  11  LYS   A HD2  1 
ATOM   209  H HD3  A LYS   A 1 11  ? 10.433 -19.047 13.590  0.72 16.86 ?  11  LYS   A HD3  1 
ATOM   210  H HD3  B LYS   A 1 11  ? 10.351 -19.117 13.518  0.28 15.81 ?  11  LYS   A HD3  1 
ATOM   211  H HE2  A LYS   A 1 11  ? 12.319 -20.309 14.153  0.72 17.23 ?  11  LYS   A HE2  1 
ATOM   212  H HE2  B LYS   A 1 11  ? 12.198 -20.456 13.924  0.28 16.03 ?  11  LYS   A HE2  1 
ATOM   213  H HE3  A LYS   A 1 11  ? 12.000 -20.449 12.603  0.72 17.23 ?  11  LYS   A HE3  1 
ATOM   214  H HE3  B LYS   A 1 11  ? 12.060 -20.237 12.356  0.28 16.03 ?  11  LYS   A HE3  1 
ATOM   215  H HZ1  A LYS   A 1 11  ? 14.210 -20.111 12.887  0.72 17.50 ?  11  LYS   A HZ1  1 
ATOM   216  H HZ1  B LYS   A 1 11  ? 14.217 -19.965 13.011  0.28 16.05 ?  11  LYS   A HZ1  1 
ATOM   217  H HZ2  A LYS   A 1 11  ? 13.679 -18.942 12.216  0.72 17.50 ?  11  LYS   A HZ2  1 
ATOM   218  H HZ2  B LYS   A 1 11  ? 13.733 -18.702 12.491  0.28 16.05 ?  11  LYS   A HZ2  1 
ATOM   219  H HZ3  A LYS   A 1 11  ? 13.994 -18.886 13.628  0.72 17.50 ?  11  LYS   A HZ3  1 
ATOM   220  H HZ3  B LYS   A 1 11  ? 13.858 -18.897 13.922  0.28 16.05 ?  11  LYS   A HZ3  1 
ATOM   221  N N    A LEU   A 1 12  ? 10.746 -16.125 8.876   0.72 11.45 ?  12  LEU   A N    1 
ATOM   222  N N    B LEU   A 1 12  ? 10.633 -15.830 9.228   0.28 11.12 ?  12  LEU   A N    1 
ATOM   223  C CA   A LEU   A 1 12  ? 10.490 -16.706 7.561   0.72 11.58 ?  12  LEU   A CA   1 
ATOM   224  C CA   B LEU   A 1 12  ? 10.388 -16.342 7.884   0.28 11.06 ?  12  LEU   A CA   1 
ATOM   225  C C    A LEU   A 1 12  ? 11.081 -18.103 7.417   0.72 11.90 ?  12  LEU   A C    1 
ATOM   226  C C    B LEU   A 1 12  ? 10.951 -17.740 7.675   0.28 11.09 ?  12  LEU   A C    1 
ATOM   227  O O    A LEU   A 1 12  ? 10.454 -18.982 6.812   0.72 12.55 ?  12  LEU   A O    1 
ATOM   228  O O    B LEU   A 1 12  ? 10.277 -18.594 7.089   0.28 11.30 ?  12  LEU   A O    1 
ATOM   229  C CB   A LEU   A 1 12  ? 11.052 -15.813 6.452   0.72 11.83 ?  12  LEU   A CB   1 
ATOM   230  C CB   B LEU   A 1 12  ? 10.978 -15.399 6.831   0.28 11.66 ?  12  LEU   A CB   1 
ATOM   231  C CG   A LEU   A 1 12  ? 10.397 -14.449 6.250   0.72 12.71 ?  12  LEU   A CG   1 
ATOM   232  C CG   B LEU   A 1 12  ? 10.298 -14.038 6.692   0.28 12.02 ?  12  LEU   A CG   1 
ATOM   233  C CD1  A LEU   A 1 12  ? 11.154 -13.675 5.191   0.72 13.12 ?  12  LEU   A CD1  1 
ATOM   234  C CD1  B LEU   A 1 12  ? 10.934 -13.248 5.559   0.28 12.41 ?  12  LEU   A CD1  1 
ATOM   235  C CD2  A LEU   A 1 12  ? 8.927  -14.593 5.868   0.72 14.02 ?  12  LEU   A CD2  1 
ATOM   236  C CD2  B LEU   A 1 12  ? 8.805  -14.210 6.456   0.28 11.63 ?  12  LEU   A CD2  1 
ATOM   237  H H    A LEU   A 1 12  ? 11.500 -15.704 8.948   0.72 13.74 ?  12  LEU   A H    1 
ATOM   238  H H    B LEU   A 1 12  ? 11.399 -15.442 9.323   0.28 13.35 ?  12  LEU   A H    1 
ATOM   239  H HA   A LEU   A 1 12  ? 9.534  -16.779 7.436   0.72 13.90 ?  12  LEU   A HA   1 
ATOM   240  H HA   B LEU   A 1 12  ? 9.430  -16.384 7.740   0.28 13.28 ?  12  LEU   A HA   1 
ATOM   241  H HB2  A LEU   A 1 12  ? 11.989 -15.659 6.640   0.72 14.20 ?  12  LEU   A HB2  1 
ATOM   242  H HB2  B LEU   A 1 12  ? 11.908 -15.234 7.051   0.28 13.99 ?  12  LEU   A HB2  1 
ATOM   243  H HB3  A LEU   A 1 12  ? 10.970 -16.299 5.615   0.72 14.20 ?  12  LEU   A HB3  1 
ATOM   244  H HB3  B LEU   A 1 12  ? 10.924 -15.834 5.966   0.28 13.99 ?  12  LEU   A HB3  1 
ATOM   245  H HG   A LEU   A 1 12  ? 10.444 -13.951 7.080   0.72 15.26 ?  12  LEU   A HG   1 
ATOM   246  H HG   B LEU   A 1 12  ? 10.421 -13.533 7.513   0.28 14.42 ?  12  LEU   A HG   1 
ATOM   247  H HD11 A LEU   A 1 12  ? 10.731 -12.814 5.067   0.72 15.75 ?  12  LEU   A HD11 1 
ATOM   248  H HD11 B LEU   A 1 12  ? 10.495 -12.385 5.489   0.28 14.90 ?  12  LEU   A HD11 1 
ATOM   249  H HD12 A LEU   A 1 12  ? 12.072 -13.557 5.484   0.72 15.75 ?  12  LEU   A HD12 1 
ATOM   250  H HD12 B LEU   A 1 12  ? 11.877 -13.125 5.748   0.28 14.90 ?  12  LEU   A HD12 1 
ATOM   251  H HD13 A LEU   A 1 12  ? 11.136 -14.178 4.360   0.72 15.75 ?  12  LEU   A HD13 1 
ATOM   252  H HD13 B LEU   A 1 12  ? 10.825 -13.742 4.731   0.28 14.90 ?  12  LEU   A HD13 1 
ATOM   253  H HD21 A LEU   A 1 12  ? 8.566  -13.719 5.658   0.72 16.83 ?  12  LEU   A HD21 1 
ATOM   254  H HD21 B LEU   A 1 12  ? 8.438  -13.377 6.126   0.28 13.96 ?  12  LEU   A HD21 1 
ATOM   255  H HD22 A LEU   A 1 12  ? 8.858  -15.174 5.091   0.72 16.83 ?  12  LEU   A HD22 1 
ATOM   256  H HD22 B LEU   A 1 12  ? 8.670  -14.916 5.805   0.28 13.96 ?  12  LEU   A HD22 1 
ATOM   257  H HD23 A LEU   A 1 12  ? 8.440  -14.983 6.611   0.72 16.83 ?  12  LEU   A HD23 1 
ATOM   258  H HD23 B LEU   A 1 12  ? 8.381  -14.450 7.296   0.28 13.96 ?  12  LEU   A HD23 1 
ATOM   259  N N    A THR   A 1 13  ? 12.291 -18.308 7.932   0.72 12.28 ?  13  THR   A N    1 
ATOM   260  N N    B THR   A 1 13  ? 12.174 -17.986 8.135   0.28 11.27 ?  13  THR   A N    1 
ATOM   261  C CA   A THR   A 1 13  ? 12.986 -19.587 7.855   0.72 12.76 ?  13  THR   A CA   1 
ATOM   262  C CA   B THR   A 1 13  ? 12.820 -19.286 8.003   0.28 11.69 ?  13  THR   A CA   1 
ATOM   263  C C    A THR   A 1 13  ? 13.746 -19.794 9.159   0.72 12.89 ?  13  THR   A C    1 
ATOM   264  C C    B THR   A 1 13  ? 13.604 -19.572 9.280   0.28 12.28 ?  13  THR   A C    1 
ATOM   265  O O    A THR   A 1 13  ? 13.654 -18.996 10.097  0.72 12.89 ?  13  THR   A O    1 
ATOM   266  O O    B THR   A 1 13  ? 13.496 -18.859 10.283  0.28 12.67 ?  13  THR   A O    1 
ATOM   267  C CB   A THR   A 1 13  ? 13.967 -19.638 6.676   0.72 13.53 ?  13  THR   A CB   1 
ATOM   268  C CB   B THR   A 1 13  ? 13.752 -19.329 6.783   0.28 11.74 ?  13  THR   A CB   1 
ATOM   269  O OG1  A THR   A 1 13  ? 15.043 -18.734 6.931   0.72 13.86 ?  13  THR   A OG1  1 
ATOM   270  O OG1  B THR   A 1 13  ? 14.811 -18.386 6.968   0.28 11.74 ?  13  THR   A OG1  1 
ATOM   271  C CG2  A THR   A 1 13  ? 13.299 -19.273 5.361   0.72 14.72 ?  13  THR   A CG2  1 
ATOM   272  C CG2  B THR   A 1 13  ? 13.008 -19.023 5.485   0.28 12.35 ?  13  THR   A CG2  1 
ATOM   273  H H    A THR   A 1 13  ? 12.747 -17.703 8.331   0.72 14.74 ?  13  THR   A H    1 
ATOM   274  H H    B THR   A 1 13  ? 12.659 -17.394 8.525   0.28 13.53 ?  13  THR   A H    1 
ATOM   275  H HA   A THR   A 1 13  ? 12.344 -20.309 7.749   0.72 15.32 ?  13  THR   A HA   1 
ATOM   276  H HA   B THR   A 1 13  ? 12.144 -19.970 7.896   0.28 14.03 ?  13  THR   A HA   1 
ATOM   277  H HB   A THR   A 1 13  ? 14.326 -20.537 6.590   0.72 16.24 ?  13  THR   A HB   1 
ATOM   278  H HB   B THR   A 1 13  ? 14.133 -20.215 6.704   0.28 14.10 ?  13  THR   A HB   1 
ATOM   279  H HG1  A THR   A 1 13  ? 15.590 -18.745 6.283   0.72 16.64 ?  13  THR   A HG1  1 
ATOM   280  H HG1  B THR   A 1 13  ? 15.327 -18.395 6.302   0.28 14.09 ?  13  THR   A HG1  1 
ATOM   281  H HG21 A THR   A 1 13  ? 13.912 -19.430 4.623   0.72 17.67 ?  13  THR   A HG21 1 
ATOM   282  H HG21 B THR   A 1 13  ? 13.612 -19.115 4.727   0.28 14.82 ?  13  THR   A HG21 1 
ATOM   283  H HG22 A THR   A 1 13  ? 12.508 -19.818 5.231   0.72 17.67 ?  13  THR   A HG22 1 
ATOM   284  H HG22 B THR   A 1 13  ? 12.270 -19.644 5.371   0.28 14.82 ?  13  THR   A HG22 1 
ATOM   285  H HG23 A THR   A 1 13  ? 13.044 -18.340 5.366   0.72 17.67 ?  13  THR   A HG23 1 
ATOM   286  H HG23 B THR   A 1 13  ? 12.661 -18.120 5.501   0.28 14.82 ?  13  THR   A HG23 1 
ATOM   287  N N    A ASP   A 1 14  ? 14.550 -20.855 9.201   0.72 13.67 ?  14  ASP   A N    1 
ATOM   288  N N    B ASP   A 1 14  ? 14.420 -20.624 9.220   0.28 12.79 ?  14  ASP   A N    1 
ATOM   289  C CA   A ASP   A 1 14  ? 15.388 -21.092 10.368  0.72 14.53 ?  14  ASP   A CA   1 
ATOM   290  C CA   B ASP   A 1 14  ? 15.257 -21.008 10.351  0.28 13.58 ?  14  ASP   A CA   1 
ATOM   291  C C    A ASP   A 1 14  ? 16.172 -19.844 10.765  0.72 14.04 ?  14  ASP   A C    1 
ATOM   292  C C    B ASP   A 1 14  ? 16.237 -19.909 10.738  0.28 13.08 ?  14  ASP   A C    1 
ATOM   293  O O    A ASP   A 1 14  ? 16.334 -19.558 11.957  0.72 14.88 ?  14  ASP   A O    1 
ATOM   294  O O    B ASP   A 1 14  ? 16.628 -19.814 11.908  0.28 12.79 ?  14  ASP   A O    1 
ATOM   295  C CB   A ASP   A 1 14  ? 16.352 -22.237 10.079  0.72 17.20 ?  14  ASP   A CB   1 
ATOM   296  C CB   B ASP   A 1 14  ? 16.022 -22.283 9.997   0.28 15.28 ?  14  ASP   A CB   1 
ATOM   297  C CG   A ASP   A 1 14  ? 17.295 -22.477 11.223  0.72 21.34 ?  14  ASP   A CG   1 
ATOM   298  C CG   B ASP   A 1 14  ? 16.933 -22.747 11.108  0.28 16.74 ?  14  ASP   A CG   1 
ATOM   299  O OD1  A ASP   A 1 14  ? 16.831 -22.908 12.297  0.72 22.89 ?  14  ASP   A OD1  1 
ATOM   300  O OD1  B ASP   A 1 14  ? 16.410 -23.084 12.191  0.28 17.04 ?  14  ASP   A OD1  1 
ATOM   301  O OD2  A ASP   A 1 14  ? 18.496 -22.204 11.054  0.72 23.68 -1 14  ASP   A OD2  1 
ATOM   302  O OD2  B ASP   A 1 14  ? 18.163 -22.796 10.895  0.28 17.65 -1 14  ASP   A OD2  1 
ATOM   303  H H    A ASP   A 1 14  ? 14.636 -21.443 8.577   0.72 16.40 ?  14  ASP   A H    1 
ATOM   304  H H    B ASP   A 1 14  ? 14.500 -21.127 8.533   0.28 15.35 ?  14  ASP   A H    1 
ATOM   305  H HA   A ASP   A 1 14  ? 14.832 -21.354 11.120  0.72 17.44 ?  14  ASP   A HA   1 
ATOM   306  H HA   B ASP   A 1 14  ? 14.694 -21.193 11.117  0.28 16.31 ?  14  ASP   A HA   1 
ATOM   307  H HB2  A ASP   A 1 14  ? 15.836 -23.052 9.901   0.72 20.64 ?  14  ASP   A HB2  1 
ATOM   308  H HB2  B ASP   A 1 14  ? 15.391 -23.000 9.847   0.28 18.35 ?  14  ASP   A HB2  1 
ATOM   309  H HB3  A ASP   A 1 14  ? 16.891 -22.023 9.304   0.72 20.64 ?  14  ASP   A HB3  1 
ATOM   310  H HB3  B ASP   A 1 14  ? 16.545 -22.125 9.194   0.28 18.35 ?  14  ASP   A HB3  1 
ATOM   311  N N    . ASN   A 1 15  ? 16.655 -19.076 9.780   1.00 13.21 ?  15  ASN   A N    1 
ATOM   312  C CA   . ASN   A 1 15  ? 17.647 -18.035 10.043  1.00 13.71 ?  15  ASN   A CA   1 
ATOM   313  C C    . ASN   A 1 15  ? 17.278 -16.640 9.548   1.00 13.99 ?  15  ASN   A C    1 
ATOM   314  O O    . ASN   A 1 15  ? 18.050 -15.707 9.796   1.00 15.31 ?  15  ASN   A O    1 
ATOM   315  C CB   . ASN   A 1 15  ? 19.020 -18.431 9.460   1.00 13.37 ?  15  ASN   A CB   1 
ATOM   316  C CG   . ASN   A 1 15  ? 19.006 -18.525 7.952   1.00 13.52 ?  15  ASN   A CG   1 
ATOM   317  O OD1  . ASN   A 1 15  ? 18.280 -19.342 7.379   1.00 14.69 ?  15  ASN   A OD1  1 
ATOM   318  N ND2  . ASN   A 1 15  ? 19.801 -17.686 7.295   1.00 13.71 ?  15  ASN   A ND2  1 
ATOM   319  H H    A ASN   A 1 15  ? 16.418 -19.136 8.959   0.72 15.86 ?  15  ASN   A H    1 
ATOM   320  H H    B ASN   A 1 15  ? 16.373 -19.090 8.972   0.28 15.86 ?  15  ASN   A H    1 
ATOM   321  H HA   . ASN   A 1 15  ? 17.770 -17.966 11.000  1.00 16.45 ?  15  ASN   A HA   1 
ATOM   322  H HB2  . ASN   A 1 15  ? 19.681 -17.762 9.718   1.00 16.05 ?  15  ASN   A HB2  1 
ATOM   323  H HB3  . ASN   A 1 15  ? 19.282 -19.298 9.814   1.00 16.05 ?  15  ASN   A HB3  1 
ATOM   324  H HD21 . ASN   A 1 15  ? 19.827 -17.697 6.435   1.00 16.46 ?  15  ASN   A HD21 1 
ATOM   325  H HD22 . ASN   A 1 15  ? 20.293 -17.118 7.726   1.00 16.46 ?  15  ASN   A HD22 1 
ATOM   326  N N    . VAL   A 1 16  ? 16.143 -16.460 8.872   1.00 13.40 ?  16  VAL   A N    1 
ATOM   327  C CA   . VAL   A 1 16  ? 15.758 -15.177 8.292   1.00 13.05 ?  16  VAL   A CA   1 
ATOM   328  C C    . VAL   A 1 16  ? 14.483 -14.673 8.960   1.00 12.55 ?  16  VAL   A C    1 
ATOM   329  O O    . VAL   A 1 16  ? 13.485 -15.402 9.051   1.00 12.96 ?  16  VAL   A O    1 
ATOM   330  C CB   . VAL   A 1 16  ? 15.582 -15.260 6.766   1.00 13.68 ?  16  VAL   A CB   1 
ATOM   331  C CG1  . VAL   A 1 16  ? 15.140 -13.904 6.197   1.00 14.61 ?  16  VAL   A CG1  1 
ATOM   332  C CG2  . VAL   A 1 16  ? 16.866 -15.730 6.093   1.00 14.42 ?  16  VAL   A CG2  1 
ATOM   333  H H    . VAL   A 1 16  ? 15.567 -17.085 8.743   1.00 16.08 ?  16  VAL   A H    1 
ATOM   334  H HA   . VAL   A 1 16  ? 16.464 -14.534 8.473   1.00 15.67 ?  16  VAL   A HA   1 
ATOM   335  H HB   . VAL   A 1 16  ? 14.890 -15.908 6.571   1.00 16.42 ?  16  VAL   A HB   1 
ATOM   336  H HG11 . VAL   A 1 16  ? 15.224 -13.933 5.232   1.00 17.54 ?  16  VAL   A HG11 1 
ATOM   337  H HG12 . VAL   A 1 16  ? 14.213 -13.749 6.442   1.00 17.54 ?  16  VAL   A HG12 1 
ATOM   338  H HG13 . VAL   A 1 16  ? 15.704 -13.210 6.562   1.00 17.54 ?  16  VAL   A HG13 1 
ATOM   339  H HG21 . VAL   A 1 16  ? 16.740 -15.719 5.132   1.00 17.31 ?  16  VAL   A HG21 1 
ATOM   340  H HG22 . VAL   A 1 16  ? 17.592 -15.135 6.338   1.00 17.31 ?  16  VAL   A HG22 1 
ATOM   341  H HG23 . VAL   A 1 16  ? 17.068 -16.633 6.389   1.00 17.31 ?  16  VAL   A HG23 1 
ATOM   342  N N    A TYR   A 1 17  ? 14.530 -13.421 9.400   0.72 12.38 ?  17  TYR   A N    1 
ATOM   343  N N    B TYR   A 1 17  ? 14.522 -13.405 9.396   0.28 12.32 ?  17  TYR   A N    1 
ATOM   344  C CA   A TYR   A 1 17  ? 13.452 -12.737 10.092  0.72 12.43 ?  17  TYR   A CA   1 
ATOM   345  C CA   B TYR   A 1 17  ? 13.448 -12.726 10.116  0.28 12.17 ?  17  TYR   A CA   1 
ATOM   346  C C    A TYR   A 1 17  ? 13.176 -11.428 9.365   0.72 12.63 ?  17  TYR   A C    1 
ATOM   347  C C    B TYR   A 1 17  ? 13.194 -11.368 9.467   0.28 11.83 ?  17  TYR   A C    1 
ATOM   348  O O    A TYR   A 1 17  ? 14.080 -10.868 8.744   0.72 12.98 ?  17  TYR   A O    1 
ATOM   349  O O    B TYR   A 1 17  ? 14.086 -10.798 8.837   0.28 11.95 ?  17  TYR   A O    1 
ATOM   350  C CB   A TYR   A 1 17  ? 13.876 -12.463 11.538  0.72 13.27 ?  17  TYR   A CB   1 
ATOM   351  C CB   B TYR   A 1 17  ? 13.837 -12.499 11.587  0.28 12.70 ?  17  TYR   A CB   1 
ATOM   352  C CG   A TYR   A 1 17  ? 14.050 -13.731 12.345  0.72 14.14 ?  17  TYR   A CG   1 
ATOM   353  C CG   B TYR   A 1 17  ? 14.098 -13.763 12.381  0.28 13.22 ?  17  TYR   A CG   1 
ATOM   354  C CD1  A TYR   A 1 17  ? 15.210 -14.497 12.254  0.72 15.34 ?  17  TYR   A CD1  1 
ATOM   355  C CD1  B TYR   A 1 17  ? 15.299 -14.452 12.261  0.28 13.74 ?  17  TYR   A CD1  1 
ATOM   356  C CD2  A TYR   A 1 17  ? 13.037 -14.178 13.179  0.72 14.83 ?  17  TYR   A CD2  1 
ATOM   357  C CD2  B TYR   A 1 17  ? 13.146 -14.258 13.262  0.28 13.76 ?  17  TYR   A CD2  1 
ATOM   358  C CE1  A TYR   A 1 17  ? 15.354 -15.675 12.985  0.72 15.83 ?  17  TYR   A CE1  1 
ATOM   359  C CE1  B TYR   A 1 17  ? 15.539 -15.606 12.987  0.28 14.31 ?  17  TYR   A CE1  1 
ATOM   360  C CE2  A TYR   A 1 17  ? 13.168 -15.351 13.910  0.72 15.43 ?  17  TYR   A CE2  1 
ATOM   361  C CE2  B TYR   A 1 17  ? 13.377 -15.414 13.994  0.28 14.19 ?  17  TYR   A CE2  1 
ATOM   362  C CZ   A TYR   A 1 17  ? 14.326 -16.095 13.816  0.72 15.66 ?  17  TYR   A CZ   1 
ATOM   363  C CZ   B TYR   A 1 17  ? 14.576 -16.083 13.853  0.28 14.32 ?  17  TYR   A CZ   1 
ATOM   364  O OH   A TYR   A 1 17  ? 14.437 -17.253 14.554  0.72 16.18 ?  17  TYR   A OH   1 
ATOM   365  O OH   B TYR   A 1 17  ? 14.812 -17.229 14.581  0.28 14.65 ?  17  TYR   A OH   1 
ATOM   366  H H    A TYR   A 1 17  ? 15.227 -12.918 9.300   0.72 14.87 ?  17  TYR   A H    1 
ATOM   367  H H    B TYR   A 1 17  ? 15.206 -12.889 9.273   0.28 14.79 ?  17  TYR   A H    1 
ATOM   368  H HA   A TYR   A 1 17  ? 12.655 -13.290 10.085  0.72 14.93 ?  17  TYR   A HA   1 
ATOM   369  H HA   B TYR   A 1 17  ? 12.632 -13.244 10.076  0.28 14.61 ?  17  TYR   A HA   1 
ATOM   370  H HB2  A TYR   A 1 17  ? 14.722 -11.990 11.533  0.72 15.93 ?  17  TYR   A HB2  1 
ATOM   371  H HB2  B TYR   A 1 17  ? 14.647 -11.965 11.616  0.28 15.24 ?  17  TYR   A HB2  1 
ATOM   372  H HB3  A TYR   A 1 17  ? 13.197 -11.925 11.965  0.72 15.93 ?  17  TYR   A HB3  1 
ATOM   373  H HB3  B TYR   A 1 17  ? 13.118 -12.022 12.027  0.28 15.24 ?  17  TYR   A HB3  1 
ATOM   374  H HD1  A TYR   A 1 17  ? 15.904 -14.221 11.694  0.72 18.41 ?  17  TYR   A HD1  1 
ATOM   375  H HD1  B TYR   A 1 17  ? 15.951 -14.137 11.679  0.28 16.49 ?  17  TYR   A HD1  1 
ATOM   376  H HD2  A TYR   A 1 17  ? 12.252 -13.688 13.249  0.72 17.80 ?  17  TYR   A HD2  1 
ATOM   377  H HD2  B TYR   A 1 17  ? 12.335 -13.810 13.360  0.28 16.52 ?  17  TYR   A HD2  1 
ATOM   378  H HE1  A TYR   A 1 17  ? 16.141 -16.178 12.921  0.72 19.00 ?  17  TYR   A HE1  1 
ATOM   379  H HE1  B TYR   A 1 17  ? 16.347 -16.060 12.897  0.28 17.18 ?  17  TYR   A HE1  1 
ATOM   380  H HE2  A TYR   A 1 17  ? 12.481 -15.631 14.469  0.72 18.52 ?  17  TYR   A HE2  1 
ATOM   381  H HE2  B TYR   A 1 17  ? 12.726 -15.732 14.579  0.28 17.04 ?  17  TYR   A HE2  1 
ATOM   382  H HH   A TYR   A 1 17  ? 13.690 -17.465 14.871  0.72 19.42 ?  17  TYR   A HH   1 
ATOM   383  H HH   B TYR   A 1 17  ? 15.558 -17.553 14.376  0.28 17.59 ?  17  TYR   A HH   1 
ATOM   384  N N    A ILE   A 1 18  ? 11.932 -10.930 9.430   0.72 12.52 ?  18  ILE   A N    1 
ATOM   385  N N    B ILE   A 1 18  ? 11.976 -10.829 9.632   0.28 11.42 ?  18  ILE   A N    1 
ATOM   386  C CA   A ILE   A 1 18  ? 11.549 -9.748  8.658   0.72 12.06 ?  18  ILE   A CA   1 
ATOM   387  C CA   B ILE   A 1 18  ? 11.593 -9.591  8.953   0.28 11.03 ?  18  ILE   A CA   1 
ATOM   388  C C    A ILE   A 1 18  ? 10.563 -8.883  9.438   0.72 12.41 ?  18  ILE   A C    1 
ATOM   389  C C    B ILE   A 1 18  ? 10.684 -8.729  9.826   0.28 10.59 ?  18  ILE   A C    1 
ATOM   390  O O    A ILE   A 1 18  ? 9.727  -9.386  10.194  0.72 12.60 ?  18  ILE   A O    1 
ATOM   391  O O    B ILE   A 1 18  ? 9.880  -9.235  10.617  0.28 11.07 ?  18  ILE   A O    1 
ATOM   392  C CB   A ILE   A 1 18  ? 11.008 -10.152 7.265   0.72 12.05 ?  18  ILE   A CB   1 
ATOM   393  C CB   B ILE   A 1 18  ? 10.927 -9.893  7.592   0.28 10.86 ?  18  ILE   A CB   1 
ATOM   394  C CG1  A ILE   A 1 18  ? 10.980 -8.951  6.322   0.72 12.07 ?  18  ILE   A CG1  1 
ATOM   395  C CG1  B ILE   A 1 18  ? 10.881 -8.640  6.715   0.28 11.92 ?  18  ILE   A CG1  1 
ATOM   396  C CG2  A ILE   A 1 18  ? 9.646  -10.851 7.380   0.72 12.04 ?  18  ILE   A CG2  1 
ATOM   397  C CG2  B ILE   A 1 18  ? 9.533  -10.479 7.793   0.28 11.49 ?  18  ILE   A CG2  1 
ATOM   398  C CD1  A ILE   A 1 18  ? 10.755 -9.335  4.893   0.72 12.96 ?  18  ILE   A CD1  1 
ATOM   399  C CD1  B ILE   A 1 18  ? 10.419 -8.918  5.304   0.28 13.14 ?  18  ILE   A CD1  1 
ATOM   400  H H    A ILE   A 1 18  ? 11.306 -11.268 9.914   0.72 15.03 ?  18  ILE   A H    1 
ATOM   401  H H    B ILE   A 1 18  ? 11.357 -11.169 10.121  0.28 13.71 ?  18  ILE   A H    1 
ATOM   402  H HA   A ILE   A 1 18  ? 12.347 -9.224  8.508   0.72 14.47 ?  18  ILE   A HA   1 
ATOM   403  H HA   B ILE   A 1 18  ? 12.399 -9.078  8.776   0.28 13.24 ?  18  ILE   A HA   1 
ATOM   404  H HB   A ILE   A 1 18  ? 11.627 -10.801 6.888   0.72 14.47 ?  18  ILE   A HB   1 
ATOM   405  H HB   B ILE   A 1 18  ? 11.468 -10.552 7.140   0.28 13.04 ?  18  ILE   A HB   1 
ATOM   406  H HG12 A ILE   A 1 18  ? 10.269 -8.356  6.591   0.72 14.49 ?  18  ILE   A HG12 1 
ATOM   407  H HG12 B ILE   A 1 18  ? 10.270 -7.997  7.106   0.28 14.31 ?  18  ILE   A HG12 1 
ATOM   408  H HG13 A ILE   A 1 18  ? 11.837 -8.494  6.374   0.72 14.49 ?  18  ILE   A HG13 1 
ATOM   409  H HG13 B ILE   A 1 18  ? 11.773 -8.256  6.664   0.28 14.31 ?  18  ILE   A HG13 1 
ATOM   410  H HG21 A ILE   A 1 18  ? 9.409  -11.234 6.517   0.72 14.45 ?  18  ILE   A HG21 1 
ATOM   411  H HG21 B ILE   A 1 18  ? 9.230  -10.864 6.954   0.28 13.79 ?  18  ILE   A HG21 1 
ATOM   412  H HG22 A ILE   A 1 18  ? 9.702  -11.557 8.044   0.72 14.45 ?  18  ILE   A HG22 1 
ATOM   413  H HG22 B ILE   A 1 18  ? 9.575  -11.168 8.474   0.28 13.79 ?  18  ILE   A HG22 1 
ATOM   414  H HG23 A ILE   A 1 18  ? 8.974  -10.203 7.644   0.72 14.45 ?  18  ILE   A HG23 1 
ATOM   415  H HG23 B ILE   A 1 18  ? 8.924  -9.777  8.071   0.28 13.79 ?  18  ILE   A HG23 1 
ATOM   416  H HD11 A ILE   A 1 18  ? 10.810 -8.536  4.340   0.72 15.56 ?  18  ILE   A HD11 1 
ATOM   417  H HD11 B ILE   A 1 18  ? 10.492 -8.104  4.780   0.28 15.78 ?  18  ILE   A HD11 1 
ATOM   418  H HD12 A ILE   A 1 18  ? 11.431 -9.970  4.621   0.72 15.56 ?  18  ILE   A HD12 1 
ATOM   419  H HD12 B ILE   A 1 18  ? 10.982 -9.609  4.918   0.28 15.78 ?  18  ILE   A HD12 1 
ATOM   420  H HD13 A ILE   A 1 18  ? 9.872  -9.730  4.808   0.72 15.56 ?  18  ILE   A HD13 1 
ATOM   421  H HD13 B ILE   A 1 18  ? 9.497  -9.216  5.326   0.28 15.78 ?  18  ILE   A HD13 1 
ATOM   422  N N    A LYS   A 1 19  ? 10.646 -7.566  9.222   0.72 12.52 ?  19  LYS   A N    1 
ATOM   423  N N    B LYS   A 1 19  ? 10.802 -7.408  9.650   0.28 10.41 ?  19  LYS   A N    1 
ATOM   424  C CA   A LYS   A 1 19  ? 9.834  -6.607  9.961   0.72 12.87 ?  19  LYS   A CA   1 
ATOM   425  C CA   B LYS   A 1 19  ? 10.010 -6.437  10.395  0.28 11.52 ?  19  LYS   A CA   1 
ATOM   426  C C    A LYS   A 1 19  ? 9.667  -5.342  9.129   0.72 13.14 ?  19  LYS   A C    1 
ATOM   427  C C    B LYS   A 1 19  ? 9.810  -5.190  9.541   0.28 12.07 ?  19  LYS   A C    1 
ATOM   428  O O    A LYS   A 1 19  ? 10.565 -4.966  8.372   0.72 13.29 ?  19  LYS   A O    1 
ATOM   429  O O    B LYS   A 1 19  ? 10.713 -4.785  8.806   0.28 12.09 ?  19  LYS   A O    1 
ATOM   430  C CB   A LYS   A 1 19  ? 10.537 -6.262  11.281  0.72 14.65 ?  19  LYS   A CB   1 
ATOM   431  C CB   B LYS   A 1 19  ? 10.711 -6.057  11.707  0.28 12.51 ?  19  LYS   A CB   1 
ATOM   432  C CG   A LYS   A 1 19  ? 9.807  -5.296  12.204  0.72 16.20 ?  19  LYS   A CG   1 
ATOM   433  C CG   B LYS   A 1 19  ? 9.887  -5.191  12.640  0.28 13.78 ?  19  LYS   A CG   1 
ATOM   434  C CD   A LYS   A 1 19  ? 10.677 -5.017  13.426  0.72 18.10 ?  19  LYS   A CD   1 
ATOM   435  C CD   B LYS   A 1 19  ? 10.718 -4.770  13.836  0.28 15.26 ?  19  LYS   A CD   1 
ATOM   436  C CE   A LYS   A 1 19  ? 10.030 -4.073  14.420  0.72 19.37 ?  19  LYS   A CE   1 
ATOM   437  C CE   B LYS   A 1 19  ? 9.917  -3.933  14.811  0.28 16.40 ?  19  LYS   A CE   1 
ATOM   438  N NZ   A LYS   A 1 19  ? 10.924 -3.847  15.595  0.72 19.59 ?  19  LYS   A NZ   1 
ATOM   439  N NZ   B LYS   A 1 19  ? 10.766 -3.465  15.936  0.28 16.77 ?  19  LYS   A NZ   1 
ATOM   440  H H    A LYS   A 1 19  ? 11.175 -7.209  8.643   0.72 15.03 ?  19  LYS   A H    1 
ATOM   441  H H    B LYS   A 1 19  ? 11.349 -7.039  9.090   0.28 12.50 ?  19  LYS   A H    1 
ATOM   442  H HA   A LYS   A 1 19  ? 8.961  -6.993  10.147  0.72 15.46 ?  19  LYS   A HA   1 
ATOM   443  H HA   B LYS   A 1 19  ? 9.144  -6.811  10.605  0.28 13.83 ?  19  LYS   A HA   1 
ATOM   444  H HB2  A LYS   A 1 19  ? 10.670 -7.089  11.774  0.72 17.58 ?  19  LYS   A HB2  1 
ATOM   445  H HB2  B LYS   A 1 19  ? 10.925 -6.869  12.192  0.28 15.02 ?  19  LYS   A HB2  1 
ATOM   446  H HB3  A LYS   A 1 19  ? 11.395 -5.872  11.070  0.72 17.58 ?  19  LYS   A HB3  1 
ATOM   447  H HB3  B LYS   A 1 19  ? 11.526 -5.572  11.504  0.28 15.02 ?  19  LYS   A HB3  1 
ATOM   448  H HG2  A LYS   A 1 19  ? 9.642  -4.462  11.740  0.72 19.45 ?  19  LYS   A HG2  1 
ATOM   449  H HG2  B LYS   A 1 19  ? 9.595  -4.394  12.174  0.28 16.54 ?  19  LYS   A HG2  1 
ATOM   450  H HG3  A LYS   A 1 19  ? 8.971  -5.694  12.500  0.72 19.45 ?  19  LYS   A HG3  1 
ATOM   451  H HG3  B LYS   A 1 19  ? 9.123  -5.697  12.962  0.28 16.54 ?  19  LYS   A HG3  1 
ATOM   452  H HD2  A LYS   A 1 19  ? 10.855 -5.854  13.884  0.72 21.73 ?  19  LYS   A HD2  1 
ATOM   453  H HD2  B LYS   A 1 19  ? 11.025 -5.563  14.303  0.28 18.32 ?  19  LYS   A HD2  1 
ATOM   454  H HD3  A LYS   A 1 19  ? 11.511 -4.617  13.134  0.72 21.73 ?  19  LYS   A HD3  1 
ATOM   455  H HD3  B LYS   A 1 19  ? 11.475 -4.246  13.531  0.28 18.32 ?  19  LYS   A HD3  1 
ATOM   456  H HE2  A LYS   A 1 19  ? 9.866  -3.215  13.994  0.72 23.25 ?  19  LYS   A HE2  1 
ATOM   457  H HE2  B LYS   A 1 19  ? 9.563  -3.157  14.349  0.28 19.68 ?  19  LYS   A HE2  1 
ATOM   458  H HE3  A LYS   A 1 19  ? 9.198  -4.454  14.739  0.72 23.25 ?  19  LYS   A HE3  1 
ATOM   459  H HE3  B LYS   A 1 19  ? 9.194  -4.469  15.173  0.28 19.68 ?  19  LYS   A HE3  1 
ATOM   460  H HZ1  A LYS   A 1 19  ? 10.534 -3.294  16.173  0.72 23.51 ?  19  LYS   A HZ1  1 
ATOM   461  H HZ1  B LYS   A 1 19  ? 10.282 -2.975  16.499  0.28 20.13 ?  19  LYS   A HZ1  1 
ATOM   462  H HZ2  A LYS   A 1 19  ? 11.090 -4.621  16.002  0.72 23.51 ?  19  LYS   A HZ2  1 
ATOM   463  H HZ2  B LYS   A 1 19  ? 11.103 -4.163  16.375  0.28 20.13 ?  19  LYS   A HZ2  1 
ATOM   464  H HZ3  A LYS   A 1 19  ? 11.693 -3.490  15.327  0.72 23.51 ?  19  LYS   A HZ3  1 
ATOM   465  H HZ3  B LYS   A 1 19  ? 11.437 -2.969  15.625  0.28 20.13 ?  19  LYS   A HZ3  1 
ATOM   466  N N    A ASN   A 1 20  ? 8.508  -4.689  9.261   0.72 13.88 ?  20  ASN   A N    1 
ATOM   467  N N    B ASN   A 1 20  ? 8.624  -4.589  9.645   0.28 13.03 ?  20  ASN   A N    1 
ATOM   468  C CA   A ASN   A 1 20  ? 8.323  -3.344  8.715   0.72 15.39 ?  20  ASN   A CA   1 
ATOM   469  C CA   B ASN   A 1 20  ? 8.291  -3.342  8.950   0.28 14.04 ?  20  ASN   A CA   1 
ATOM   470  C C    A ASN   A 1 20  ? 8.965  -2.361  9.686   0.72 16.08 ?  20  ASN   A C    1 
ATOM   471  C C    B ASN   A 1 20  ? 8.823  -2.183  9.784   0.28 14.53 ?  20  ASN   A C    1 
ATOM   472  O O    A ASN   A 1 20  ? 8.465  -2.161  10.800  0.72 17.00 ?  20  ASN   A O    1 
ATOM   473  O O    B ASN   A 1 20  ? 8.144  -1.666  10.674  0.28 14.93 ?  20  ASN   A O    1 
ATOM   474  C CB   A ASN   A 1 20  ? 6.834  -3.053  8.512   0.72 16.63 ?  20  ASN   A CB   1 
ATOM   475  C CB   B ASN   A 1 20  ? 6.778  -3.247  8.759   0.28 14.59 ?  20  ASN   A CB   1 
ATOM   476  C CG   A ASN   A 1 20  ? 6.549  -1.603  8.123   0.72 18.41 ?  20  ASN   A CG   1 
ATOM   477  C CG   B ASN   A 1 20  ? 6.329  -1.959  8.068   0.28 15.17 ?  20  ASN   A CG   1 
ATOM   478  O OD1  A ASN   A 1 20  ? 5.544  -1.038  8.544   0.72 21.40 ?  20  ASN   A OD1  1 
ATOM   479  O OD1  B ASN   A 1 20  ? 5.214  -1.483  8.299   0.28 15.75 ?  20  ASN   A OD1  1 
ATOM   480  N ND2  A ASN   A 1 20  ? 7.422  -1.003  7.321   0.72 18.13 ?  20  ASN   A ND2  1 
ATOM   481  N ND2  B ASN   A 1 20  ? 7.178  -1.401  7.214   0.28 15.89 ?  20  ASN   A ND2  1 
ATOM   482  H H    A ASN   A 1 20  ? 7.812  -5.013  9.658   0.72 16.66 ?  20  ASN   A H    1 
ATOM   483  H H    B ASN   A 1 20  ? 7.982  -4.902  10.117  0.28 15.65 ?  20  ASN   A H    1 
ATOM   484  H HA   A ASN   A 1 20  ? 8.769  -3.281  7.862   0.72 18.48 ?  20  ASN   A HA   1 
ATOM   485  H HA   B ASN   A 1 20  ? 8.725  -3.331  8.083   0.28 16.85 ?  20  ASN   A HA   1 
ATOM   486  H HB2  A ASN   A 1 20  ? 6.495  -3.625  7.804   0.72 19.96 ?  20  ASN   A HB2  1 
ATOM   487  H HB2  B ASN   A 1 20  ? 6.484  -3.989  8.228   0.28 17.51 ?  20  ASN   A HB2  1 
ATOM   488  H HB3  A ASN   A 1 20  ? 6.360  -3.242  9.339   0.72 19.96 ?  20  ASN   A HB3  1 
ATOM   489  H HB3  B ASN   A 1 20  ? 6.357  -3.287  9.630   0.28 17.51 ?  20  ASN   A HB3  1 
ATOM   490  H HD21 A ASN   A 1 20  ? 7.292  -0.188  7.081   0.72 21.76 ?  20  ASN   A HD21 1 
ATOM   491  H HD21 B ASN   A 1 20  ? 6.962  -0.672  6.816   0.28 19.07 ?  20  ASN   A HD21 1 
ATOM   492  H HD22 A ASN   A 1 20  ? 8.116  -1.428  7.044   0.72 21.76 ?  20  ASN   A HD22 1 
ATOM   493  H HD22 B ASN   A 1 20  ? 7.941  -1.763  7.061   0.28 19.07 ?  20  ASN   A HD22 1 
ATOM   494  N N    A ALA   A 1 21  ? 10.089 -1.769  9.288   0.72 16.17 ?  21  ALA   A N    1 
ATOM   495  N N    B ALA   A 1 21  ? 10.055 -1.767  9.491   0.28 14.75 ?  21  ALA   A N    1 
ATOM   496  C CA   A ALA   A 1 21  ? 10.808 -0.901  10.206  0.72 16.27 ?  21  ALA   A CA   1 
ATOM   497  C CA   B ALA   A 1 21  ? 10.704 -0.728  10.278  0.28 14.84 ?  21  ALA   A CA   1 
ATOM   498  C C    A ALA   A 1 21  ? 11.755 -0.000  9.434   0.72 16.02 ?  21  ALA   A C    1 
ATOM   499  C C    B ALA   A 1 21  ? 11.832 -0.103  9.470   0.28 14.34 ?  21  ALA   A C    1 
ATOM   500  O O    A ALA   A 1 21  ? 12.202 -0.338  8.333   0.72 15.75 ?  21  ALA   A O    1 
ATOM   501  O O    B ALA   A 1 21  ? 12.388 -0.728  8.565   0.28 14.21 ?  21  ALA   A O    1 
ATOM   502  C CB   A ALA   A 1 21  ? 11.596 -1.709  11.238  0.72 16.93 ?  21  ALA   A CB   1 
ATOM   503  C CB   B ALA   A 1 21  ? 11.244 -1.292  11.598  0.28 15.46 ?  21  ALA   A CB   1 
ATOM   504  H H    A ALA   A 1 21  ? 10.441 -1.853  8.510   0.72 19.41 ?  21  ALA   A H    1 
ATOM   505  H H    B ALA   A 1 21  ? 10.532 -2.067  8.841   0.28 17.71 ?  21  ALA   A H    1 
ATOM   506  H HA   A ALA   A 1 21  ? 10.167 -0.343  10.679  0.72 19.53 ?  21  ALA   A HA   1 
ATOM   507  H HA   B ALA   A 1 21  ? 10.059 -0.035  10.488  0.28 17.82 ?  21  ALA   A HA   1 
ATOM   508  H HB1  A ALA   A 1 21  ? 12.034 -1.095  11.843  0.72 20.32 ?  21  ALA   A HB1  1 
ATOM   509  H HB1  B ALA   A 1 21  ? 11.675 -0.580  12.096  0.28 18.56 ?  21  ALA   A HB1  1 
ATOM   510  H HB2  A ALA   A 1 21  ? 10.978 -2.276  11.731  0.72 20.32 ?  21  ALA   A HB2  1 
ATOM   511  H HB2  B ALA   A 1 21  ? 10.506 -1.656  12.115  0.28 18.56 ?  21  ALA   A HB2  1 
ATOM   512  H HB3  A ALA   A 1 21  ? 12.249 -2.254  10.778  0.72 20.32 ?  21  ALA   A HB3  1 
ATOM   513  H HB3  B ALA   A 1 21  ? 11.886 -1.994  11.404  0.28 18.56 ?  21  ALA   A HB3  1 
ATOM   514  N N    A ASP   A 1 22  ? 12.034 1.154   10.039  0.72 16.50 ?  22  ASP   A N    1 
ATOM   515  N N    B ASP   A 1 22  ? 12.138 1.151   9.799   0.28 14.33 ?  22  ASP   A N    1 
ATOM   516  C CA   A ASP   A 1 22  ? 13.075 2.067   9.588   0.72 16.51 ?  22  ASP   A CA   1 
ATOM   517  C CA   B ASP   A 1 22  ? 13.316 1.826   9.268   0.28 14.49 ?  22  ASP   A CA   1 
ATOM   518  C C    A ASP   A 1 22  ? 14.403 1.585   10.160  0.72 15.24 ?  22  ASP   A C    1 
ATOM   519  C C    B ASP   A 1 22  ? 14.563 1.206   9.889   0.28 13.54 ?  22  ASP   A C    1 
ATOM   520  O O    A ASP   A 1 22  ? 14.588 1.574   11.382  0.72 15.72 ?  22  ASP   A O    1 
ATOM   521  O O    B ASP   A 1 22  ? 14.664 1.090   11.114  0.28 13.66 ?  22  ASP   A O    1 
ATOM   522  C CB   A ASP   A 1 22  ? 12.737 3.467   10.100  0.72 18.37 ?  22  ASP   A CB   1 
ATOM   523  C CB   B ASP   A 1 22  ? 13.234 3.310   9.635   0.28 15.64 ?  22  ASP   A CB   1 
ATOM   524  C CG   A ASP   A 1 22  ? 13.737 4.520   9.660   0.72 20.44 ?  22  ASP   A CG   1 
ATOM   525  C CG   B ASP   A 1 22  ? 14.255 4.168   8.912   0.28 16.24 ?  22  ASP   A CG   1 
ATOM   526  O OD1  A ASP   A 1 22  ? 14.868 4.174   9.274   0.72 21.05 ?  22  ASP   A OD1  1 
ATOM   527  O OD1  B ASP   A 1 22  ? 15.299 3.636   8.485   0.28 15.39 ?  22  ASP   A OD1  1 
ATOM   528  O OD2  A ASP   A 1 22  ? 13.390 5.718   9.716   0.72 22.31 -1 22  ASP   A OD2  1 
ATOM   529  O OD2  B ASP   A 1 22  ? 14.012 5.389   8.787   0.28 17.46 -1 22  ASP   A OD2  1 
ATOM   530  H H    A ASP   A 1 22  ? 11.602 1.443   10.728  0.72 19.80 ?  22  ASP   A H    1 
ATOM   531  H H    B ASP   A 1 22  ? 11.660 1.639   10.321  0.28 17.20 ?  22  ASP   A H    1 
ATOM   532  H HA   A ASP   A 1 22  ? 13.119 2.078   8.619   0.72 19.82 ?  22  ASP   A HA   1 
ATOM   533  H HA   B ASP   A 1 22  ? 13.348 1.729   8.299   0.28 17.39 ?  22  ASP   A HA   1 
ATOM   534  H HB2  A ASP   A 1 22  ? 11.864 3.728   9.762   0.72 22.05 ?  22  ASP   A HB2  1 
ATOM   535  H HB2  B ASP   A 1 22  ? 12.357 3.645   9.407   0.28 18.77 ?  22  ASP   A HB2  1 
ATOM   536  H HB3  A ASP   A 1 22  ? 12.720 3.451   11.072  0.72 22.05 ?  22  ASP   A HB3  1 
ATOM   537  H HB3  B ASP   A 1 22  ? 13.394 3.403   10.585  0.28 18.77 ?  22  ASP   A HB3  1 
ATOM   538  N N    A ILE   A 1 23  ? 15.319 1.175   9.279   0.72 14.64 ?  23  ILE   A N    1 
ATOM   539  N N    B ILE   A 1 23  ? 15.512 0.790   9.045   0.28 13.23 ?  23  ILE   A N    1 
ATOM   540  C CA   A ILE   A 1 23  ? 16.564 0.550   9.721   0.72 14.04 ?  23  ILE   A CA   1 
ATOM   541  C CA   B ILE   A 1 23  ? 16.732 0.166   9.552   0.28 12.73 ?  23  ILE   A CA   1 
ATOM   542  C C    A ILE   A 1 23  ? 17.375 1.490   10.606  0.72 13.87 ?  23  ILE   A C    1 
ATOM   543  C C    B ILE   A 1 23  ? 17.483 1.125   10.464  0.28 13.30 ?  23  ILE   A C    1 
ATOM   544  O O    A ILE   A 1 23  ? 18.099 1.037   11.503  0.72 14.63 ?  23  ILE   A O    1 
ATOM   545  O O    B ILE   A 1 23  ? 18.152 0.698   11.414  0.28 13.20 ?  23  ILE   A O    1 
ATOM   546  C CB   A ILE   A 1 23  ? 17.362 0.033   8.504   0.72 13.59 ?  23  ILE   A CB   1 
ATOM   547  C CB   B ILE   A 1 23  ? 17.611 -0.357  8.393   0.28 12.08 ?  23  ILE   A CB   1 
ATOM   548  C CG1  A ILE   A 1 23  ? 18.494 -0.894  8.953   0.72 13.45 ?  23  ILE   A CG1  1 
ATOM   549  C CG1  B ILE   A 1 23  ? 18.721 -1.265  8.936   0.28 11.86 ?  23  ILE   A CG1  1 
ATOM   550  C CG2  A ILE   A 1 23  ? 17.884 1.195   7.658   0.72 14.05 ?  23  ILE   A CG2  1 
ATOM   551  C CG2  B ILE   A 1 23  ? 18.204 0.794   7.584   0.28 11.83 ?  23  ILE   A CG2  1 
ATOM   552  C CD1  A ILE   A 1 23  ? 19.188 -1.597  7.803   0.72 13.42 ?  23  ILE   A CD1  1 
ATOM   553  C CD1  B ILE   A 1 23  ? 19.580 -1.907  7.858   0.28 11.79 ?  23  ILE   A CD1  1 
ATOM   554  H H    A ILE   A 1 23  ? 15.234 1.244   8.429   0.72 17.58 ?  23  ILE   A H    1 
ATOM   555  H H    B ILE   A 1 23  ? 15.475 0.859   8.198   0.28 15.88 ?  23  ILE   A H    1 
ATOM   556  H HA   A ILE   A 1 23  ? 16.337 -0.221  10.260  0.72 16.86 ?  23  ILE   A HA   1 
ATOM   557  H HA   B ILE   A 1 23  ? 16.477 -0.600  10.084  0.28 15.28 ?  23  ILE   A HA   1 
ATOM   558  H HB   A ILE   A 1 23  ? 16.757 -0.484  7.952   0.72 16.31 ?  23  ILE   A HB   1 
ATOM   559  H HB   B ILE   A 1 23  ? 17.054 -0.887  7.803   0.28 14.50 ?  23  ILE   A HB   1 
ATOM   560  H HG12 A ILE   A 1 23  ? 19.161 -0.375  9.427   0.72 16.14 ?  23  ILE   A HG12 1 
ATOM   561  H HG12 B ILE   A 1 23  ? 19.307 -0.743  9.505   0.28 14.24 ?  23  ILE   A HG12 1 
ATOM   562  H HG13 A ILE   A 1 23  ? 18.129 -1.576  9.539   0.72 16.14 ?  23  ILE   A HG13 1 
ATOM   563  H HG13 B ILE   A 1 23  ? 18.317 -1.981  9.453   0.28 14.24 ?  23  ILE   A HG13 1 
ATOM   564  H HG21 A ILE   A 1 23  ? 18.234 0.847   6.821   0.72 16.86 ?  23  ILE   A HG21 1 
ATOM   565  H HG21 B ILE   A 1 23  ? 18.583 0.439   6.761   0.28 14.20 ?  23  ILE   A HG21 1 
ATOM   566  H HG22 A ILE   A 1 23  ? 17.150 1.806   7.473   0.72 16.86 ?  23  ILE   A HG22 1 
ATOM   567  H HG22 B ILE   A 1 23  ? 17.502 1.427   7.376   0.28 14.20 ?  23  ILE   A HG22 1 
ATOM   568  H HG23 A ILE   A 1 23  ? 18.582 1.658   8.142   0.72 16.86 ?  23  ILE   A HG23 1 
ATOM   569  H HG23 B ILE   A 1 23  ? 18.898 1.225   8.105   0.28 14.20 ?  23  ILE   A HG23 1 
ATOM   570  H HD11 A ILE   A 1 23  ? 19.831 -2.227  8.160   0.72 16.11 ?  23  ILE   A HD11 1 
ATOM   571  H HD11 B ILE   A 1 23  ? 20.185 -2.544  8.273   0.28 14.15 ?  23  ILE   A HD11 1 
ATOM   572  H HD12 A ILE   A 1 23  ? 18.522 -2.067  7.275   0.72 16.11 ?  23  ILE   A HD12 1 
ATOM   573  H HD12 B ILE   A 1 23  ? 19.004 -2.365  7.226   0.28 14.15 ?  23  ILE   A HD12 1 
ATOM   574  H HD13 A ILE   A 1 23  ? 19.637 -0.936  7.255   0.72 16.11 ?  23  ILE   A HD13 1 
ATOM   575  H HD13 B ILE   A 1 23  ? 20.088 -1.218  7.404   0.28 14.15 ?  23  ILE   A HD13 1 
ATOM   576  N N    A VAL   A 1 24  ? 17.260 2.803   10.387  0.72 14.45 ?  24  VAL   A N    1 
ATOM   577  N N    B VAL   A 1 24  ? 17.369 2.430   10.206  0.28 14.81 ?  24  VAL   A N    1 
ATOM   578  C CA   A VAL   A 1 24  ? 17.940 3.765   11.253  0.72 15.74 ?  24  VAL   A CA   1 
ATOM   579  C CA   B VAL   A 1 24  ? 18.003 3.425   11.065  0.28 15.95 ?  24  VAL   A CA   1 
ATOM   580  C C    A VAL   A 1 24  ? 17.412 3.660   12.676  0.72 16.50 ?  24  VAL   A C    1 
ATOM   581  C C    B VAL   A 1 24  ? 17.388 3.397   12.458  0.28 16.70 ?  24  VAL   A C    1 
ATOM   582  O O    A VAL   A 1 24  ? 18.180 3.553   13.642  0.72 17.07 ?  24  VAL   A O    1 
ATOM   583  O O    B VAL   A 1 24  ? 18.098 3.469   13.469  0.28 17.27 ?  24  VAL   A O    1 
ATOM   584  C CB   A VAL   A 1 24  ? 17.783 5.192   10.696  0.72 17.12 ?  24  VAL   A CB   1 
ATOM   585  C CB   B VAL   A 1 24  ? 17.907 4.819   10.415  0.28 16.76 ?  24  VAL   A CB   1 
ATOM   586  C CG1  A VAL   A 1 24  ? 18.266 6.227   11.713  0.72 17.99 ?  24  VAL   A CG1  1 
ATOM   587  C CG1  B VAL   A 1 24  ? 18.459 5.887   11.344  0.28 17.65 ?  24  VAL   A CG1  1 
ATOM   588  C CG2  A VAL   A 1 24  ? 18.529 5.330   9.381   0.72 18.28 ?  24  VAL   A CG2  1 
ATOM   589  C CG2  B VAL   A 1 24  ? 18.640 4.829   9.079   0.28 16.66 ?  24  VAL   A CG2  1 
ATOM   590  H H    A VAL   A 1 24  ? 16.805 3.157   9.747   0.72 17.34 ?  24  VAL   A H    1 
ATOM   591  H H    B VAL   A 1 24  ? 16.930 2.761   9.546   0.28 17.78 ?  24  VAL   A H    1 
ATOM   592  H HA   A VAL   A 1 24  ? 18.886 3.559   11.269  0.72 18.89 ?  24  VAL   A HA   1 
ATOM   593  H HA   B VAL   A 1 24  ? 18.942 3.208   11.155  0.28 19.15 ?  24  VAL   A HA   1 
ATOM   594  H HB   A VAL   A 1 24  ? 16.844 5.363   10.520  0.72 20.55 ?  24  VAL   A HB   1 
ATOM   595  H HB   B VAL   A 1 24  ? 16.975 5.025   10.242  0.28 20.12 ?  24  VAL   A HB   1 
ATOM   596  H HG11 A VAL   A 1 24  ? 18.424 7.067   11.255  0.72 21.59 ?  24  VAL   A HG11 1 
ATOM   597  H HG11 B VAL   A 1 24  ? 18.593 6.704   10.838  0.28 21.19 ?  24  VAL   A HG11 1 
ATOM   598  H HG12 A VAL   A 1 24  ? 17.586 6.344   12.393  0.72 21.59 ?  24  VAL   A HG12 1 
ATOM   599  H HG12 B VAL   A 1 24  ? 17.823 6.044   12.059  0.28 21.19 ?  24  VAL   A HG12 1 
ATOM   600  H HG13 A VAL   A 1 24  ? 19.091 5.910   12.114  0.72 21.59 ?  24  VAL   A HG13 1 
ATOM   601  H HG13 B VAL   A 1 24  ? 19.303 5.582   11.708  0.28 21.19 ?  24  VAL   A HG13 1 
ATOM   602  H HG21 A VAL   A 1 24  ? 18.309 6.186   8.979   0.72 21.94 ?  24  VAL   A HG21 1 
ATOM   603  H HG21 B VAL   A 1 24  ? 18.602 5.723   8.704   0.28 20.00 ?  24  VAL   A HG21 1 
ATOM   604  H HG22 A VAL   A 1 24  ? 19.484 5.285   9.553   0.72 21.94 ?  24  VAL   A HG22 1 
ATOM   605  H HG22 B VAL   A 1 24  ? 19.565 4.572   9.225   0.28 20.00 ?  24  VAL   A HG22 1 
ATOM   606  H HG23 A VAL   A 1 24  ? 18.266 4.611   8.786   0.72 21.94 ?  24  VAL   A HG23 1 
ATOM   607  H HG23 B VAL   A 1 24  ? 18.213 4.199   8.478   0.28 20.00 ?  24  VAL   A HG23 1 
ATOM   608  N N    A GLU   A 1 25  ? 16.087 3.701   12.826  0.72 17.35 ?  25  GLU   A N    1 
ATOM   609  N N    B GLU   A 1 25  ? 16.060 3.282   12.536  0.28 17.10 ?  25  GLU   A N    1 
ATOM   610  C CA   A GLU   A 1 25  ? 15.495 3.626   14.157  0.72 18.86 ?  25  GLU   A CA   1 
ATOM   611  C CA   B GLU   A 1 25  ? 15.399 3.229   13.836  0.28 17.85 ?  25  GLU   A CA   1 
ATOM   612  C C    A GLU   A 1 25  ? 15.737 2.264   14.795  0.72 17.84 ?  25  GLU   A C    1 
ATOM   613  C C    B GLU   A 1 25  ? 15.668 1.903   14.543  0.28 17.64 ?  25  GLU   A C    1 
ATOM   614  O O    A GLU   A 1 25  ? 15.968 2.174   16.006  0.72 18.71 ?  25  GLU   A O    1 
ATOM   615  O O    B GLU   A 1 25  ? 15.846 1.871   15.766  0.28 17.82 ?  25  GLU   A O    1 
ATOM   616  C CB   A GLU   A 1 25  ? 14.004 3.963   14.085  0.72 21.66 ?  25  GLU   A CB   1 
ATOM   617  C CB   B GLU   A 1 25  ? 13.897 3.474   13.671  0.28 18.93 ?  25  GLU   A CB   1 
ATOM   618  C CG   A GLU   A 1 25  ? 13.744 5.418   13.716  0.72 24.80 ?  25  GLU   A CG   1 
ATOM   619  C CG   B GLU   A 1 25  ? 13.563 4.855   13.122  0.28 20.79 ?  25  GLU   A CG   1 
ATOM   620  C CD   A GLU   A 1 25  ? 14.527 6.393   14.583  0.72 27.39 ?  25  GLU   A CD   1 
ATOM   621  C CD   B GLU   A 1 25  ? 14.025 5.971   14.035  0.28 22.44 ?  25  GLU   A CD   1 
ATOM   622  O OE1  A GLU   A 1 25  ? 14.573 6.195   15.817  0.72 28.19 ?  25  GLU   A OE1  1 
ATOM   623  O OE1  B GLU   A 1 25  ? 14.006 5.772   15.269  0.28 23.20 ?  25  GLU   A OE1  1 
ATOM   624  O OE2  A GLU   A 1 25  ? 15.117 7.344   14.027  0.72 28.81 -1 25  GLU   A OE2  1 
ATOM   625  O OE2  B GLU   A 1 25  ? 14.406 7.042   13.520  0.28 23.09 -1 25  GLU   A OE2  1 
ATOM   626  H H    A GLU   A 1 25  ? 15.518 3.781   12.182  0.72 20.82 ?  25  GLU   A H    1 
ATOM   627  H H    B GLU   A 1 25  ? 15.530 3.239   11.860  0.28 20.52 ?  25  GLU   A H    1 
ATOM   628  H HA   A GLU   A 1 25  ? 15.923 4.282   14.724  0.72 22.64 ?  25  GLU   A HA   1 
ATOM   629  H HA   B GLU   A 1 25  ? 15.754 3.936   14.394  0.28 21.43 ?  25  GLU   A HA   1 
ATOM   630  H HB2  A GLU   A 1 25  ? 13.579 3.408   13.409  0.72 26.00 ?  25  GLU   A HB2  1 
ATOM   631  H HB2  B GLU   A 1 25  ? 13.535 2.817   13.058  0.28 22.72 ?  25  GLU   A HB2  1 
ATOM   632  H HB3  A GLU   A 1 25  ? 13.594 3.801   14.949  0.72 26.00 ?  25  GLU   A HB3  1 
ATOM   633  H HB3  B GLU   A 1 25  ? 13.468 3.389   14.537  0.28 22.72 ?  25  GLU   A HB3  1 
ATOM   634  H HG2  A GLU   A 1 25  ? 14.015 5.564   12.797  0.72 29.76 ?  25  GLU   A HG2  1 
ATOM   635  H HG2  B GLU   A 1 25  ? 13.995 4.967   12.260  0.28 24.95 ?  25  GLU   A HG2  1 
ATOM   636  H HG3  A GLU   A 1 25  ? 12.797 5.608   13.818  0.72 29.76 ?  25  GLU   A HG3  1 
ATOM   637  H HG3  B GLU   A 1 25  ? 12.602 4.936   13.025  0.28 24.95 ?  25  GLU   A HG3  1 
ATOM   638  N N    A GLU   A 1 26  ? 15.703 1.195   13.995  0.72 17.63 ?  26  GLU   A N    1 
ATOM   639  N N    B GLU   A 1 26  ? 15.702 0.798   13.793  0.28 17.38 ?  26  GLU   A N    1 
ATOM   640  C CA   A GLU   A 1 26  ? 15.999 -0.134  14.523  0.72 17.30 ?  26  GLU   A CA   1 
ATOM   641  C CA   B GLU   A 1 26  ? 16.066 -0.482  14.391  0.28 17.34 ?  26  GLU   A CA   1 
ATOM   642  C C    A GLU   A 1 26  ? 17.426 -0.207  15.053  0.72 16.75 ?  26  GLU   A C    1 
ATOM   643  C C    B GLU   A 1 26  ? 17.490 -0.462  14.925  0.28 16.54 ?  26  GLU   A C    1 
ATOM   644  O O    A GLU   A 1 26  ? 17.667 -0.695  16.163  0.72 17.05 ?  26  GLU   A O    1 
ATOM   645  O O    B GLU   A 1 26  ? 17.779 -1.095  15.947  0.28 16.28 ?  26  GLU   A O    1 
ATOM   646  C CB   A GLU   A 1 26  ? 15.790 -1.187  13.435  0.72 18.50 ?  26  GLU   A CB   1 
ATOM   647  C CB   B GLU   A 1 26  ? 15.912 -1.610  13.370  0.28 18.30 ?  26  GLU   A CB   1 
ATOM   648  C CG   A GLU   A 1 26  ? 14.372 -1.685  13.290  0.72 21.78 ?  26  GLU   A CG   1 
ATOM   649  C CG   B GLU   A 1 26  ? 14.477 -1.998  13.086  0.28 19.04 ?  26  GLU   A CG   1 
ATOM   650  C CD   A GLU   A 1 26  ? 13.918 -2.524  14.471  0.72 23.76 ?  26  GLU   A CD   1 
ATOM   651  C CD   B GLU   A 1 26  ? 13.767 -2.565  14.290  0.28 19.18 ?  26  GLU   A CD   1 
ATOM   652  O OE1  A GLU   A 1 26  ? 14.395 -3.673  14.641  0.72 24.07 ?  26  GLU   A OE1  1 
ATOM   653  O OE1  B GLU   A 1 26  ? 14.287 -3.521  14.907  0.28 19.93 ?  26  GLU   A OE1  1 
ATOM   654  O OE2  A GLU   A 1 26  ? 13.084 -2.017  15.235  0.72 24.98 -1 26  GLU   A OE2  1 
ATOM   655  O OE2  B GLU   A 1 26  ? 12.685 -2.041  14.616  0.28 17.72 -1 26  GLU   A OE2  1 
ATOM   656  H H    A GLU   A 1 26  ? 15.516 1.219   13.155  0.72 21.17 ?  26  GLU   A H    1 
ATOM   657  H H    B GLU   A 1 26  ? 15.520 0.764   12.956  0.28 20.86 ?  26  GLU   A H    1 
ATOM   658  H HA   A GLU   A 1 26  ? 15.393 -0.323  15.253  0.72 20.77 ?  26  GLU   A HA   1 
ATOM   659  H HA   B GLU   A 1 26  ? 15.477 -0.665  15.137  0.28 20.82 ?  26  GLU   A HA   1 
ATOM   660  H HB2  A GLU   A 1 26  ? 16.056 -0.809  12.582  0.72 22.20 ?  26  GLU   A HB2  1 
ATOM   661  H HB2  B GLU   A 1 26  ? 16.310 -1.328  12.530  0.28 21.97 ?  26  GLU   A HB2  1 
ATOM   662  H HB3  A GLU   A 1 26  ? 16.348 -1.952  13.640  0.72 22.20 ?  26  GLU   A HB3  1 
ATOM   663  H HB3  B GLU   A 1 26  ? 16.375 -2.398  13.700  0.28 21.97 ?  26  GLU   A HB3  1 
ATOM   664  H HG2  A GLU   A 1 26  ? 13.781 -0.917  13.207  0.72 26.14 ?  26  GLU   A HG2  1 
ATOM   665  H HG2  B GLU   A 1 26  ? 13.985 -1.213  12.809  0.28 22.85 ?  26  GLU   A HG2  1 
ATOM   666  H HG3  A GLU   A 1 26  ? 14.308 -2.235  12.496  0.72 26.14 ?  26  GLU   A HG3  1 
ATOM   667  H HG3  B GLU   A 1 26  ? 14.460 -2.672  12.393  0.28 22.85 ?  26  GLU   A HG3  1 
ATOM   668  N N    . ALA   A 1 27  ? 18.393 0.257   14.257  1.00 15.92 ?  27  ALA   A N    1 
ATOM   669  C CA   . ALA   A 1 27  ? 19.781 0.255   14.704  1.00 16.23 ?  27  ALA   A CA   1 
ATOM   670  C C    . ALA   A 1 27  ? 19.947 1.058   15.987  1.00 18.19 ?  27  ALA   A C    1 
ATOM   671  O O    . ALA   A 1 27  ? 20.620 0.614   16.925  1.00 18.11 ?  27  ALA   A O    1 
ATOM   672  C CB   . ALA   A 1 27  ? 20.695 0.792   13.601  1.00 15.36 ?  27  ALA   A CB   1 
ATOM   673  H H    A ALA   A 1 27  ? 18.272 0.570   13.463  0.72 19.10 ?  27  ALA   A H    1 
ATOM   674  H H    B ALA   A 1 27  ? 18.230 0.744   13.565  0.28 19.10 ?  27  ALA   A H    1 
ATOM   675  H HA   . ALA   A 1 27  ? 20.047 -0.654  14.888  1.00 19.48 ?  27  ALA   A HA   1 
ATOM   676  H HB1  . ALA   A 1 27  ? 21.615 0.784   13.919  1.00 18.44 ?  27  ALA   A HB1  1 
ATOM   677  H HB2  . ALA   A 1 27  ? 20.616 0.225   12.817  1.00 18.44 ?  27  ALA   A HB2  1 
ATOM   678  H HB3  . ALA   A 1 27  ? 20.434 1.700   13.379  1.00 18.44 ?  27  ALA   A HB3  1 
ATOM   679  N N    A LYS   A 1 28  ? 19.336 2.242   16.057  0.72 19.75 ?  28  LYS   A N    1 
ATOM   680  N N    B LYS   A 1 28  ? 19.328 2.242   16.052  0.28 20.30 ?  28  LYS   A N    1 
ATOM   681  C CA   A LYS   A 1 28  ? 19.481 3.063   17.254  0.72 22.37 ?  28  LYS   A CA   1 
ATOM   682  C CA   B LYS   A 1 28  ? 19.428 3.072   17.249  0.28 22.80 ?  28  LYS   A CA   1 
ATOM   683  C C    A LYS   A 1 28  ? 18.919 2.365   18.486  0.72 23.37 ?  28  LYS   A C    1 
ATOM   684  C C    B LYS   A 1 28  ? 18.889 2.354   18.479  0.28 24.25 ?  28  LYS   A C    1 
ATOM   685  O O    A LYS   A 1 28  ? 19.443 2.546   19.590  0.72 25.03 ?  28  LYS   A O    1 
ATOM   686  O O    B LYS   A 1 28  ? 19.408 2.545   19.585  0.28 24.86 ?  28  LYS   A O    1 
ATOM   687  C CB   A LYS   A 1 28  ? 18.836 4.435   17.045  0.72 24.39 ?  28  LYS   A CB   1 
ATOM   688  C CB   B LYS   A 1 28  ? 18.690 4.397   17.034  0.28 23.93 ?  28  LYS   A CB   1 
ATOM   689  C CG   A LYS   A 1 28  ? 19.684 5.365   16.190  0.72 26.57 ?  28  LYS   A CG   1 
ATOM   690  C CG   B LYS   A 1 28  ? 19.337 5.301   15.990  0.28 25.13 ?  28  LYS   A CG   1 
ATOM   691  C CD   A LYS   A 1 28  ? 19.213 6.806   16.266  0.72 29.46 ?  28  LYS   A CD   1 
ATOM   692  C CD   B LYS   A 1 28  ? 18.771 6.716   16.019  0.28 26.64 ?  28  LYS   A CD   1 
ATOM   693  C CE   A LYS   A 1 28  ? 17.912 7.001   15.518  0.72 31.43 ?  28  LYS   A CE   1 
ATOM   694  C CE   B LYS   A 1 28  ? 17.431 6.810   15.310  0.28 27.77 ?  28  LYS   A CE   1 
ATOM   695  N NZ   A LYS   A 1 28  ? 17.531 8.438   15.456  0.72 32.76 ?  28  LYS   A NZ   1 
ATOM   696  N NZ   B LYS   A 1 28  ? 16.988 8.226   15.160  0.28 28.38 ?  28  LYS   A NZ   1 
ATOM   697  H H    A LYS   A 1 28  ? 18.848 2.586   15.439  0.72 23.71 ?  28  LYS   A H    1 
ATOM   698  H H    B LYS   A 1 28  ? 18.855 2.583   15.422  0.28 24.36 ?  28  LYS   A H    1 
ATOM   699  H HA   A LYS   A 1 28  ? 20.423 3.209   17.419  0.72 26.85 ?  28  LYS   A HA   1 
ATOM   700  H HA   B LYS   A 1 28  ? 20.359 3.278   17.414  0.28 27.36 ?  28  LYS   A HA   1 
ATOM   701  H HB2  A LYS   A 1 28  ? 17.982 4.323   16.603  0.72 29.27 ?  28  LYS   A HB2  1 
ATOM   702  H HB2  B LYS   A 1 28  ? 17.785 4.210   16.741  0.28 28.72 ?  28  LYS   A HB2  1 
ATOM   703  H HB3  A LYS   A 1 28  ? 18.709 4.863   17.908  0.72 29.27 ?  28  LYS   A HB3  1 
ATOM   704  H HB3  B LYS   A 1 28  ? 18.669 4.886   17.872  0.28 28.72 ?  28  LYS   A HB3  1 
ATOM   705  H HG2  A LYS   A 1 28  ? 20.603 5.333   16.498  0.72 31.89 ?  28  LYS   A HG2  1 
ATOM   706  H HG2  B LYS   A 1 28  ? 20.289 5.355   16.162  0.28 30.16 ?  28  LYS   A HG2  1 
ATOM   707  H HG3  A LYS   A 1 28  ? 19.632 5.080   15.265  0.72 31.89 ?  28  LYS   A HG3  1 
ATOM   708  H HG3  B LYS   A 1 28  ? 19.177 4.932   15.107  0.28 30.16 ?  28  LYS   A HG3  1 
ATOM   709  H HD2  A LYS   A 1 28  ? 19.070 7.050   17.194  0.72 35.35 ?  28  LYS   A HD2  1 
ATOM   710  H HD2  B LYS   A 1 28  ? 18.645 6.992   16.941  0.28 31.98 ?  28  LYS   A HD2  1 
ATOM   711  H HD3  A LYS   A 1 28  ? 19.883 7.384   15.867  0.72 35.35 ?  28  LYS   A HD3  1 
ATOM   712  H HD3  B LYS   A 1 28  ? 19.390 7.317   15.574  0.28 31.98 ?  28  LYS   A HD3  1 
ATOM   713  H HE2  A LYS   A 1 28  ? 18.012 6.673   14.611  0.72 37.72 ?  28  LYS   A HE2  1 
ATOM   714  H HE2  B LYS   A 1 28  ? 17.509 6.421   14.425  0.28 33.33 ?  28  LYS   A HE2  1 
ATOM   715  H HE3  A LYS   A 1 28  ? 17.205 6.518   15.974  0.72 37.72 ?  28  LYS   A HE3  1 
ATOM   716  H HE3  B LYS   A 1 28  ? 16.762 6.336   15.828  0.28 33.33 ?  28  LYS   A HE3  1 
ATOM   717  H HZ1  A LYS   A 1 28  ? 16.766 8.531   15.013  0.72 39.32 ?  28  LYS   A HZ1  1 
ATOM   718  H HZ1  B LYS   A 1 28  ? 16.203 8.258   14.743  0.28 34.06 ?  28  LYS   A HZ1  1 
ATOM   719  H HZ2  A LYS   A 1 28  ? 17.431 8.762   16.279  0.72 39.32 ?  28  LYS   A HZ2  1 
ATOM   720  H HZ2  B LYS   A 1 28  ? 16.906 8.606   15.961  0.28 34.06 ?  28  LYS   A HZ2  1 
ATOM   721  H HZ3  A LYS   A 1 28  ? 18.166 8.902   15.038  0.72 39.32 ?  28  LYS   A HZ3  1 
ATOM   722  H HZ3  B LYS   A 1 28  ? 17.587 8.683   14.684  0.28 34.06 ?  28  LYS   A HZ3  1 
ATOM   723  N N    A LYS   A 1 29  ? 17.878 1.550   18.317  0.72 23.41 ?  29  LYS   A N    1 
ATOM   724  N N    B LYS   A 1 29  ? 17.860 1.523   18.311  0.28 25.28 ?  29  LYS   A N    1 
ATOM   725  C CA   A LYS   A 1 29  ? 17.281 0.851   19.452  0.72 25.23 ?  29  LYS   A CA   1 
ATOM   726  C CA   B LYS   A 1 29  ? 17.256 0.835   19.448  0.28 26.65 ?  29  LYS   A CA   1 
ATOM   727  C C    A LYS   A 1 29  ? 18.094 -0.382  19.840  0.72 24.86 ?  29  LYS   A C    1 
ATOM   728  C C    B LYS   A 1 29  ? 18.056 -0.402  19.841  0.28 25.65 ?  29  LYS   A C    1 
ATOM   729  O O    A LYS   A 1 29  ? 18.383 -0.598  21.023  0.72 26.08 ?  29  LYS   A O    1 
ATOM   730  O O    B LYS   A 1 29  ? 18.307 -0.637  21.029  0.28 26.18 ?  29  LYS   A O    1 
ATOM   731  C CB   A LYS   A 1 29  ? 15.842 0.452   19.115  0.72 27.89 ?  29  LYS   A CB   1 
ATOM   732  C CB   B LYS   A 1 29  ? 15.814 0.447   19.107  0.28 28.95 ?  29  LYS   A CB   1 
ATOM   733  C CG   A LYS   A 1 29  ? 15.101 -0.239  20.248  0.72 31.14 ?  29  LYS   A CG   1 
ATOM   734  C CG   B LYS   A 1 29  ? 15.044 -0.188  20.255  0.28 31.05 ?  29  LYS   A CG   1 
ATOM   735  C CD   A LYS   A 1 29  ? 14.755 0.736   21.360  0.72 34.09 ?  29  LYS   A CD   1 
ATOM   736  C CD   B LYS   A 1 29  ? 14.685 0.838   21.315  0.28 32.82 ?  29  LYS   A CD   1 
ATOM   737  C CE   A LYS   A 1 29  ? 13.896 0.077   22.428  0.72 36.01 ?  29  LYS   A CE   1 
ATOM   738  C CE   B LYS   A 1 29  ? 13.797 0.234   22.391  0.28 34.06 ?  29  LYS   A CE   1 
ATOM   739  N NZ   A LYS   A 1 29  ? 13.485 1.045   23.480  0.72 37.15 ?  29  LYS   A NZ   1 
ATOM   740  N NZ   B LYS   A 1 29  ? 13.398 1.241   23.411  0.28 34.75 ?  29  LYS   A NZ   1 
ATOM   741  H H    A LYS   A 1 29  ? 17.500 1.386   17.562  0.72 28.09 ?  29  LYS   A H    1 
ATOM   742  H H    B LYS   A 1 29  ? 17.495 1.344   17.553  0.28 30.34 ?  29  LYS   A H    1 
ATOM   743  H HA   A LYS   A 1 29  ? 17.255 1.445   20.216  0.72 30.28 ?  29  LYS   A HA   1 
ATOM   744  H HA   B LYS   A 1 29  ? 17.234 1.434   20.209  0.28 31.99 ?  29  LYS   A HA   1 
ATOM   745  H HB2  A LYS   A 1 29  ? 15.342 1.252   18.886  0.72 33.47 ?  29  LYS   A HB2  1 
ATOM   746  H HB2  B LYS   A 1 29  ? 15.333 1.246   18.839  0.28 34.75 ?  29  LYS   A HB2  1 
ATOM   747  H HB3  A LYS   A 1 29  ? 15.853 -0.154  18.359  0.72 33.47 ?  29  LYS   A HB3  1 
ATOM   748  H HB3  B LYS   A 1 29  ? 15.827 -0.188  18.375  0.28 34.75 ?  29  LYS   A HB3  1 
ATOM   749  H HG2  A LYS   A 1 29  ? 14.275 -0.614  19.906  0.72 37.37 ?  29  LYS   A HG2  1 
ATOM   750  H HG2  B LYS   A 1 29  ? 14.222 -0.571  19.912  0.28 37.26 ?  29  LYS   A HG2  1 
ATOM   751  H HG3  A LYS   A 1 29  ? 15.655 -0.944  20.621  0.72 37.37 ?  29  LYS   A HG3  1 
ATOM   752  H HG3  B LYS   A 1 29  ? 15.586 -0.879  20.669  0.28 37.26 ?  29  LYS   A HG3  1 
ATOM   753  H HD2  A LYS   A 1 29  ? 15.572 1.050   21.777  0.72 40.92 ?  29  LYS   A HD2  1 
ATOM   754  H HD2  B LYS   A 1 29  ? 15.496 1.162   21.736  0.28 39.39 ?  29  LYS   A HD2  1 
ATOM   755  H HD3  A LYS   A 1 29  ? 14.259 1.482   20.987  0.72 40.92 ?  29  LYS   A HD3  1 
ATOM   756  H HD3  B LYS   A 1 29  ? 14.205 1.572   20.900  0.28 39.39 ?  29  LYS   A HD3  1 
ATOM   757  H HE2  A LYS   A 1 29  ? 13.095 -0.283  22.015  0.72 43.21 ?  29  LYS   A HE2  1 
ATOM   758  H HE2  B LYS   A 1 29  ? 12.991 -0.116  21.979  0.28 40.88 ?  29  LYS   A HE2  1 
ATOM   759  H HE3  A LYS   A 1 29  ? 14.403 -0.635  22.850  0.72 43.21 ?  29  LYS   A HE3  1 
ATOM   760  H HE3  B LYS   A 1 29  ? 14.280 -0.478  22.839  0.28 40.88 ?  29  LYS   A HE3  1 
ATOM   761  H HZ1  A LYS   A 1 29  ? 12.984 0.635   24.091  0.72 44.58 ?  29  LYS   A HZ1  1 
ATOM   762  H HZ1  B LYS   A 1 29  ? 12.880 0.861   24.027  0.28 41.71 ?  29  LYS   A HZ1  1 
ATOM   763  H HZ2  A LYS   A 1 29  ? 14.204 1.387   23.877  0.72 44.58 ?  29  LYS   A HZ2  1 
ATOM   764  H HZ2  B LYS   A 1 29  ? 14.121 1.575   23.808  0.28 41.71 ?  29  LYS   A HZ2  1 
ATOM   765  H HZ3  A LYS   A 1 29  ? 13.012 1.707   23.117  0.72 44.58 ?  29  LYS   A HZ3  1 
ATOM   766  H HZ3  B LYS   A 1 29  ? 12.948 1.904   23.024  0.28 41.71 ?  29  LYS   A HZ3  1 
ATOM   767  N N    . VAL   A 1 30  ? 18.454 -1.208  18.857  1.00 24.20 ?  30  VAL   A N    1 
ATOM   768  C CA   . VAL   A 1 30  ? 19.111 -2.479  19.152  1.00 23.39 ?  30  VAL   A CA   1 
ATOM   769  C C    . VAL   A 1 30  ? 20.614 -2.323  19.379  1.00 22.30 ?  30  VAL   A C    1 
ATOM   770  O O    . VAL   A 1 30  ? 21.199 -3.052  20.188  1.00 22.68 ?  30  VAL   A O    1 
ATOM   771  C CB   . VAL   A 1 30  ? 18.802 -3.473  18.018  1.00 24.22 ?  30  VAL   A CB   1 
ATOM   772  C CG1  . VAL   A 1 30  ? 19.548 -4.783  18.221  1.00 25.02 ?  30  VAL   A CG1  1 
ATOM   773  C CG2  . VAL   A 1 30  ? 17.299 -3.717  17.920  1.00 24.89 ?  30  VAL   A CG2  1 
ATOM   774  H H    A VAL   A 1 30  ? 18.322 -1.062  18.019  0.72 29.05 ?  30  VAL   A H    1 
ATOM   775  H H    B VAL   A 1 30  ? 18.347 -1.049  18.018  0.28 29.05 ?  30  VAL   A H    1 
ATOM   776  H HA   . VAL   A 1 30  ? 18.725 -2.842  19.961  1.00 28.08 ?  30  VAL   A HA   1 
ATOM   777  H HB   . VAL   A 1 30  ? 19.095 -3.095  17.175  1.00 29.06 ?  30  VAL   A HB   1 
ATOM   778  H HG11 . VAL   A 1 30  ? 19.170 -5.455  17.630  1.00 30.03 ?  30  VAL   A HG11 1 
ATOM   779  H HG12 . VAL   A 1 30  ? 20.484 -4.652  18.015  1.00 30.03 ?  30  VAL   A HG12 1 
ATOM   780  H HG13 . VAL   A 1 30  ? 19.444 -5.064  19.144  1.00 30.03 ?  30  VAL   A HG13 1 
ATOM   781  H HG21 . VAL   A 1 30  ? 17.130 -4.395  17.245  1.00 29.87 ?  30  VAL   A HG21 1 
ATOM   782  H HG22 . VAL   A 1 30  ? 16.971 -4.023  18.781  1.00 29.87 ?  30  VAL   A HG22 1 
ATOM   783  H HG23 . VAL   A 1 30  ? 16.857 -2.890  17.674  1.00 29.87 ?  30  VAL   A HG23 1 
ATOM   784  N N    . LYS   A 1 31  ? 21.260 -1.387  18.693  1.00 20.98 ?  31  LYS   A N    1 
ATOM   785  C CA   . LYS   A 1 31  ? 22.715 -1.298  18.649  1.00 21.69 ?  31  LYS   A CA   1 
ATOM   786  C C    . LYS   A 1 31  ? 23.317 -2.663  18.301  1.00 19.28 ?  31  LYS   A C    1 
ATOM   787  O O    . LYS   A 1 31  ? 24.092 -3.228  19.079  1.00 20.23 ?  31  LYS   A O    1 
ATOM   788  C CB   . LYS   A 1 31  ? 23.295 -0.757  19.949  1.00 26.76 ?  31  LYS   A CB   1 
ATOM   789  C CG   . LYS   A 1 31  ? 22.590 0.490   20.460  1.00 32.90 ?  31  LYS   A CG   1 
ATOM   790  C CD   . LYS   A 1 31  ? 23.580 1.553   20.915  1.00 37.66 ?  31  LYS   A CD   1 
ATOM   791  C CE   . LYS   A 1 31  ? 22.906 2.599   21.793  1.00 40.81 ?  31  LYS   A CE   1 
ATOM   792  N NZ   . LYS   A 1 31  ? 21.754 3.262   21.120  1.00 42.35 ?  31  LYS   A NZ   1 
ATOM   793  H H    . LYS   A 1 31  ? 20.866 -0.771  18.238  1.00 25.18 ?  31  LYS   A H    1 
ATOM   794  H HA   . LYS   A 1 31  ? 22.958 -0.681  17.940  1.00 26.03 ?  31  LYS   A HA   1 
ATOM   795  H HB2  . LYS   A 1 31  ? 23.226 -1.440  20.630  1.00 32.12 ?  31  LYS   A HB2  1 
ATOM   796  H HB3  . LYS   A 1 31  ? 24.228 -0.531  19.802  1.00 32.12 ?  31  LYS   A HB3  1 
ATOM   797  H HG2  . LYS   A 1 31  ? 22.048 0.867   19.749  1.00 39.48 ?  31  LYS   A HG2  1 
ATOM   798  H HG3  . LYS   A 1 31  ? 22.032 0.252   21.217  1.00 39.48 ?  31  LYS   A HG3  1 
ATOM   799  H HD2  . LYS   A 1 31  ? 24.288 1.134   21.429  1.00 45.19 ?  31  LYS   A HD2  1 
ATOM   800  H HD3  . LYS   A 1 31  ? 23.950 2.000   20.137  1.00 45.19 ?  31  LYS   A HD3  1 
ATOM   801  H HE2  . LYS   A 1 31  ? 22.576 2.170   22.598  1.00 48.97 ?  31  LYS   A HE2  1 
ATOM   802  H HE3  . LYS   A 1 31  ? 23.553 3.284   22.023  1.00 48.97 ?  31  LYS   A HE3  1 
ATOM   803  H HZ1  . LYS   A 1 31  ? 21.397 3.873   21.660  1.00 50.82 ?  31  LYS   A HZ1  1 
ATOM   804  H HZ2  . LYS   A 1 31  ? 22.027 3.661   20.373  1.00 50.82 ?  31  LYS   A HZ2  1 
ATOM   805  H HZ3  . LYS   A 1 31  ? 21.133 2.658   20.915  1.00 50.82 ?  31  LYS   A HZ3  1 
ATOM   806  N N    . PRO   A 1 32  ? 22.974 -3.212  17.142  1.00 16.96 ?  32  PRO   A N    1 
ATOM   807  C CA   . PRO   A 1 32  ? 23.444 -4.551  16.789  1.00 17.27 ?  32  PRO   A CA   1 
ATOM   808  C C    . PRO   A 1 32  ? 24.944 -4.563  16.577  1.00 17.18 ?  32  PRO   A C    1 
ATOM   809  O O    . PRO   A 1 32  ? 25.581 -3.531  16.354  1.00 17.37 ?  32  PRO   A O    1 
ATOM   810  C CB   . PRO   A 1 32  ? 22.715 -4.838  15.473  1.00 17.49 ?  32  PRO   A CB   1 
ATOM   811  C CG   . PRO   A 1 32  ? 22.531 -3.475  14.869  1.00 16.24 ?  32  PRO   A CG   1 
ATOM   812  C CD   . PRO   A 1 32  ? 22.238 -2.581  16.036  1.00 16.11 ?  32  PRO   A CD   1 
ATOM   813  H HA   . PRO   A 1 32  ? 23.198 -5.202  17.461  1.00 20.73 ?  32  PRO   A HA   1 
ATOM   814  H HB2  . PRO   A 1 32  ? 23.265 -5.405  14.903  1.00 20.99 ?  32  PRO   A HB2  1 
ATOM   815  H HB3  . PRO   A 1 32  ? 21.861 -5.263  15.655  1.00 20.99 ?  32  PRO   A HB3  1 
ATOM   816  H HG2  . PRO   A 1 32  ? 23.343 -3.212  14.413  1.00 19.49 ?  32  PRO   A HG2  1 
ATOM   817  H HG3  . PRO   A 1 32  ? 21.781 -3.501  14.248  1.00 19.49 ?  32  PRO   A HG3  1 
ATOM   818  H HD2  . PRO   A 1 32  ? 22.580 -1.692  15.853  1.00 19.33 ?  32  PRO   A HD2  1 
ATOM   819  H HD3  . PRO   A 1 32  ? 21.289 -2.573  16.216  1.00 19.33 ?  32  PRO   A HD3  1 
ATOM   820  N N    . THR   A 1 33  ? 25.506 -5.769  16.619  1.00 17.03 ?  33  THR   A N    1 
ATOM   821  C CA   . THR   A 1 33  ? 26.915 -5.928  16.291  1.00 17.27 ?  33  THR   A CA   1 
ATOM   822  C C    . THR   A 1 33  ? 27.202 -5.465  14.869  1.00 15.61 ?  33  THR   A C    1 
ATOM   823  O O    . THR   A 1 33  ? 28.232 -4.822  14.616  1.00 15.92 ?  33  THR   A O    1 
ATOM   824  C CB   . THR   A 1 33  ? 27.324 -7.387  16.485  1.00 19.02 ?  33  THR   A CB   1 
ATOM   825  O OG1  . THR   A 1 33  ? 26.999 -7.788  17.818  1.00 21.13 ?  33  THR   A OG1  1 
ATOM   826  C CG2  . THR   A 1 33  ? 28.817 -7.570  16.256  1.00 20.36 ?  33  THR   A CG2  1 
ATOM   827  H H    . THR   A 1 33  ? 25.098 -6.499  16.822  1.00 20.44 ?  33  THR   A H    1 
ATOM   828  H HA   . THR   A 1 33  ? 27.447 -5.389  16.897  1.00 20.73 ?  33  THR   A HA   1 
ATOM   829  H HB   . THR   A 1 33  ? 26.846 -7.952  15.855  1.00 22.82 ?  33  THR   A HB   1 
ATOM   830  H HG1  . THR   A 1 33  ? 27.413 -7.311  18.375  1.00 25.36 ?  33  THR   A HG1  1 
ATOM   831  H HG21 . THR   A 1 33  ? 29.087 -8.465  16.524  1.00 24.44 ?  33  THR   A HG21 1 
ATOM   832  H HG22 . THR   A 1 33  ? 29.028 -7.447  15.320  1.00 24.44 ?  33  THR   A HG22 1 
ATOM   833  H HG23 . THR   A 1 33  ? 29.313 -6.924  16.783  1.00 24.44 ?  33  THR   A HG23 1 
ATOM   834  N N    . VAL   A 1 34  ? 26.304 -5.774  13.932  1.00 14.31 ?  34  VAL   A N    1 
ATOM   835  C CA   . VAL   A 1 34  ? 26.497 -5.444  12.524  1.00 12.76 ?  34  VAL   A CA   1 
ATOM   836  C C    . VAL   A 1 34  ? 25.198 -4.885  11.956  1.00 12.10 ?  34  VAL   A C    1 
ATOM   837  O O    . VAL   A 1 34  ? 24.159 -5.556  11.997  1.00 12.83 ?  34  VAL   A O    1 
ATOM   838  C CB   . VAL   A 1 34  ? 26.946 -6.653  11.682  1.00 13.60 ?  34  VAL   A CB   1 
ATOM   839  C CG1  . VAL   A 1 34  ? 27.119 -6.249  10.222  1.00 13.52 ?  34  VAL   A CG1  1 
ATOM   840  C CG2  . VAL   A 1 34  ? 28.229 -7.256  12.240  1.00 15.20 ?  34  VAL   A CG2  1 
ATOM   841  H H    . VAL   A 1 34  ? 25.561 -6.179  14.093  1.00 17.18 ?  34  VAL   A H    1 
ATOM   842  H HA   . VAL   A 1 34  ? 27.176 -4.753  12.446  1.00 15.32 ?  34  VAL   A HA   1 
ATOM   843  H HB   . VAL   A 1 34  ? 26.253 -7.331  11.726  1.00 16.33 ?  34  VAL   A HB   1 
ATOM   844  H HG11 . VAL   A 1 34  ? 27.617 -6.945  9.765   1.00 16.23 ?  34  VAL   A HG11 1 
ATOM   845  H HG12 . VAL   A 1 34  ? 26.247 -6.143  9.814   1.00 16.23 ?  34  VAL   A HG12 1 
ATOM   846  H HG13 . VAL   A 1 34  ? 27.611 -5.413  10.184  1.00 16.23 ?  34  VAL   A HG13 1 
ATOM   847  H HG21 . VAL   A 1 34  ? 28.501 -7.993  11.672  1.00 18.25 ?  34  VAL   A HG21 1 
ATOM   848  H HG22 . VAL   A 1 34  ? 28.918 -6.574  12.253  1.00 18.25 ?  34  VAL   A HG22 1 
ATOM   849  H HG23 . VAL   A 1 34  ? 28.063 -7.576  13.142  1.00 18.25 ?  34  VAL   A HG23 1 
ATOM   850  N N    . VAL   A 1 35  ? 25.261 -3.670  11.407  1.00 11.58 ?  35  VAL   A N    1 
ATOM   851  C CA   . VAL   A 1 35  ? 24.230 -3.151  10.515  1.00 10.97 ?  35  VAL   A CA   1 
ATOM   852  C C    . VAL   A 1 35  ? 24.789 -3.155  9.100   1.00 10.79 ?  35  VAL   A C    1 
ATOM   853  O O    . VAL   A 1 35  ? 25.935 -2.751  8.875   1.00 11.34 ?  35  VAL   A O    1 
ATOM   854  C CB   . VAL   A 1 35  ? 23.708 -1.756  10.929  1.00 11.77 ?  35  VAL   A CB   1 
ATOM   855  C CG1  . VAL   A 1 35  ? 24.788 -0.668  10.832  1.00 12.55 ?  35  VAL   A CG1  1 
ATOM   856  C CG2  . VAL   A 1 35  ? 22.477 -1.390  10.097  1.00 12.45 ?  35  VAL   A CG2  1 
ATOM   857  H H    . VAL   A 1 35  ? 25.898 -3.111  11.542  1.00 13.91 ?  35  VAL   A H    1 
ATOM   858  H HA   . VAL   A 1 35  ? 23.468 -3.755  10.535  1.00 13.17 ?  35  VAL   A HA   1 
ATOM   859  H HB   . VAL   A 1 35  ? 23.414 -1.794  11.851  1.00 14.13 ?  35  VAL   A HB   1 
ATOM   860  H HG11 . VAL   A 1 35  ? 24.431 0.169   11.181  1.00 15.06 ?  35  VAL   A HG11 1 
ATOM   861  H HG12 . VAL   A 1 35  ? 25.555 -0.939  11.358  1.00 15.06 ?  35  VAL   A HG12 1 
ATOM   862  H HG13 . VAL   A 1 35  ? 25.046 -0.550  9.905   1.00 15.06 ?  35  VAL   A HG13 1 
ATOM   863  H HG21 . VAL   A 1 35  ? 22.122 -0.543  10.403  1.00 14.95 ?  35  VAL   A HG21 1 
ATOM   864  H HG22 . VAL   A 1 35  ? 22.739 -1.315  9.160   1.00 14.95 ?  35  VAL   A HG22 1 
ATOM   865  H HG23 . VAL   A 1 35  ? 21.809 -2.086  10.193  1.00 14.95 ?  35  VAL   A HG23 1 
ATOM   866  N N    . VAL   A 1 36  ? 23.978 -3.615  8.151   1.00 10.08 ?  36  VAL   A N    1 
ATOM   867  C CA   . VAL   A 1 36  ? 24.350 -3.630  6.742   1.00 9.89  ?  36  VAL   A CA   1 
ATOM   868  C C    . VAL   A 1 36  ? 23.890 -2.338  6.082   1.00 10.35 ?  36  VAL   A C    1 
ATOM   869  O O    . VAL   A 1 36  ? 22.727 -1.932  6.219   1.00 10.73 ?  36  VAL   A O    1 
ATOM   870  C CB   . VAL   A 1 36  ? 23.747 -4.847  6.022   1.00 9.87  ?  36  VAL   A CB   1 
ATOM   871  C CG1  . VAL   A 1 36  ? 24.013 -4.770  4.535   1.00 10.63 ?  36  VAL   A CG1  1 
ATOM   872  C CG2  . VAL   A 1 36  ? 24.298 -6.135  6.602   1.00 10.90 ?  36  VAL   A CG2  1 
ATOM   873  H H    . VAL   A 1 36  ? 23.188 -3.937  8.301   1.00 12.10 ?  36  VAL   A H    1 
ATOM   874  H HA   . VAL   A 1 36  ? 25.318 -3.685  6.669   1.00 11.88 ?  36  VAL   A HA   1 
ATOM   875  H HB   . VAL   A 1 36  ? 22.788 -4.844  6.151   1.00 11.85 ?  36  VAL   A HB   1 
ATOM   876  H HG11 . VAL   A 1 36  ? 23.874 -5.644  4.141   1.00 12.76 ?  36  VAL   A HG11 1 
ATOM   877  H HG12 . VAL   A 1 36  ? 23.405 -4.127  4.132   1.00 12.76 ?  36  VAL   A HG12 1 
ATOM   878  H HG13 . VAL   A 1 36  ? 24.932 -4.487  4.391   1.00 12.76 ?  36  VAL   A HG13 1 
ATOM   879  H HG21 . VAL   A 1 36  ? 23.919 -6.891  6.124   1.00 13.09 ?  36  VAL   A HG21 1 
ATOM   880  H HG22 . VAL   A 1 36  ? 25.268 -6.141  6.502   1.00 13.09 ?  36  VAL   A HG22 1 
ATOM   881  H HG23 . VAL   A 1 36  ? 24.068 -6.191  7.543   1.00 13.09 ?  36  VAL   A HG23 1 
ATOM   882  N N    . ASN   A 1 37  ? 24.801 -1.711  5.341   1.00 9.73  ?  37  ASN   A N    1 
ATOM   883  C CA   . ASN   A 1 37  ? 24.479 -0.590  4.475   1.00 9.49  ?  37  ASN   A CA   1 
ATOM   884  C C    . ASN   A 1 37  ? 24.344 -1.053  3.035   1.00 9.35  ?  37  ASN   A C    1 
ATOM   885  O O    . ASN   A 1 37  ? 25.125 -1.885  2.556   1.00 10.00 ?  37  ASN   A O    1 
ATOM   886  C CB   . ASN   A 1 37  ? 25.554 0.492   4.559   1.00 9.87  ?  37  ASN   A CB   1 
ATOM   887  C CG   . ASN   A 1 37  ? 25.233 1.691   3.703   1.00 10.07 ?  37  ASN   A CG   1 
ATOM   888  O OD1  . ASN   A 1 37  ? 24.062 2.030   3.511   1.00 10.71 ?  37  ASN   A OD1  1 
ATOM   889  N ND2  . ASN   A 1 37  ? 26.270 2.344   3.186   1.00 10.55 ?  37  ASN   A ND2  1 
ATOM   890  H H    . ASN   A 1 37  ? 25.637 -1.919  5.332   1.00 11.68 ?  37  ASN   A H    1 
ATOM   891  H HA   . ASN   A 1 37  ? 23.638 -0.197  4.759   1.00 11.39 ?  37  ASN   A HA   1 
ATOM   892  H HB2  . ASN   A 1 37  ? 25.636 0.794   5.482   1.00 11.85 ?  37  ASN   A HB2  1 
ATOM   893  H HB3  . ASN   A 1 37  ? 26.403 0.123   4.261   1.00 11.85 ?  37  ASN   A HB3  1 
ATOM   894  H HD21 . ASN   A 1 37  ? 26.138 3.035   2.690   1.00 12.66 ?  37  ASN   A HD21 1 
ATOM   895  H HD22 . ASN   A 1 37  ? 27.069 2.084   3.343   1.00 12.66 ?  37  ASN   A HD22 1 
ATOM   896  N N    . ALA   A 1 38  ? 23.335 -0.508  2.350   1.00 10.02 ?  38  ALA   A N    1 
ATOM   897  C CA   . ALA   A 1 38  ? 23.143 -0.682  0.909   1.00 10.34 ?  38  ALA   A CA   1 
ATOM   898  C C    . ALA   A 1 38  ? 24.041 0.324   0.183   1.00 10.25 ?  38  ALA   A C    1 
ATOM   899  O O    . ALA   A 1 38  ? 23.614 1.400   -0.246  1.00 10.39 ?  38  ALA   A O    1 
ATOM   900  C CB   . ALA   A 1 38  ? 21.673 -0.486  0.554   1.00 11.59 ?  38  ALA   A CB   1 
ATOM   901  H H    . ALA   A 1 38  ? 22.735 -0.010  2.715   1.00 12.04 ?  38  ALA   A H    1 
ATOM   902  H HA   . ALA   A 1 38  ? 23.409 -1.578  0.652   1.00 12.42 ?  38  ALA   A HA   1 
ATOM   903  H HB1  . ALA   A 1 38  ? 21.531 -0.744  -0.369  1.00 13.92 ?  38  ALA   A HB1  1 
ATOM   904  H HB2  . ALA   A 1 38  ? 21.128 -1.041  1.139   1.00 13.92 ?  38  ALA   A HB2  1 
ATOM   905  H HB3  . ALA   A 1 38  ? 21.440 0.446   0.679   1.00 13.92 ?  38  ALA   A HB3  1 
ATOM   906  N N    A ALA   A 1 39  ? 25.312 -0.047  0.050   0.72 10.07 ?  39  ALA   A N    1 
ATOM   907  N N    B ALA   A 1 39  ? 25.313 -0.035  0.053   0.28 10.45 ?  39  ALA   A N    1 
ATOM   908  C CA   A ALA   A 1 39  ? 26.353 0.838   -0.441  0.72 10.25 ?  39  ALA   A CA   1 
ATOM   909  C CA   B ALA   A 1 39  ? 26.321 0.896   -0.426  0.28 10.86 ?  39  ALA   A CA   1 
ATOM   910  C C    A ALA   A 1 39  ? 26.455 0.799   -1.964  0.72 10.29 ?  39  ALA   A C    1 
ATOM   911  C C    B ALA   A 1 39  ? 26.536 0.765   -1.930  0.28 10.28 ?  39  ALA   A C    1 
ATOM   912  O O    A ALA   A 1 39  ? 25.931 -0.096  -2.633  0.72 10.73 ?  39  ALA   A O    1 
ATOM   913  O O    B ALA   A 1 39  ? 26.156 -0.229  -2.556  0.28 9.27  ?  39  ALA   A O    1 
ATOM   914  C CB   A ALA   A 1 39  ? 27.692 0.439   0.184   0.72 10.98 ?  39  ALA   A CB   1 
ATOM   915  C CB   B ALA   A 1 39  ? 27.642 0.655   0.305   0.28 11.94 ?  39  ALA   A CB   1 
ATOM   916  H H    A ALA   A 1 39  ? 25.597 -0.836  0.249   0.72 12.09 ?  39  ALA   A H    1 
ATOM   917  H H    B ALA   A 1 39  ? 25.615 -0.821  0.235   0.28 12.55 ?  39  ALA   A H    1 
ATOM   918  H HA   A ALA   A 1 39  ? 26.145 1.748   -0.170  0.72 12.30 ?  39  ALA   A HA   1 
ATOM   919  H HA   B ALA   A 1 39  ? 26.031 1.801   -0.240  0.28 13.04 ?  39  ALA   A HA   1 
ATOM   920  H HB1  A ALA   A 1 39  ? 28.379 1.039   -0.145  0.72 13.18 ?  39  ALA   A HB1  1 
ATOM   921  H HB1  B ALA   A 1 39  ? 28.301 1.285   -0.023  0.28 14.34 ?  39  ALA   A HB1  1 
ATOM   922  H HB2  A ALA   A 1 39  ? 27.623 0.518   1.152   0.72 13.18 ?  39  ALA   A HB2  1 
ATOM   923  H HB2  B ALA   A 1 39  ? 27.503 0.786   1.257   0.28 14.34 ?  39  ALA   A HB2  1 
ATOM   924  H HB3  A ALA   A 1 39  ? 27.895 -0.472  -0.061  0.72 13.18 ?  39  ALA   A HB3  1 
ATOM   925  H HB3  B ALA   A 1 39  ? 27.936 -0.253  0.136   0.28 14.34 ?  39  ALA   A HB3  1 
ATOM   926  N N    . ASN   A 1 40  ? 27.158 1.794   -2.505  1.00 10.69 ?  40  ASN   A N    1 
ATOM   927  C CA   . ASN   A 1 40  ? 27.680 1.754   -3.864  1.00 10.71 ?  40  ASN   A CA   1 
ATOM   928  C C    . ASN   A 1 40  ? 29.207 1.625   -3.812  1.00 10.33 ?  40  ASN   A C    1 
ATOM   929  O O    . ASN   A 1 40  ? 29.824 1.722   -2.750  1.00 10.55 ?  40  ASN   A O    1 
ATOM   930  C CB   . ASN   A 1 40  ? 27.206 2.946   -4.712  1.00 11.62 ?  40  ASN   A CB   1 
ATOM   931  C CG   . ASN   A 1 40  ? 27.592 4.282   -4.126  1.00 12.57 ?  40  ASN   A CG   1 
ATOM   932  O OD1  . ASN   A 1 40  ? 28.765 4.539   -3.832  1.00 13.30 ?  40  ASN   A OD1  1 
ATOM   933  N ND2  . ASN   A 1 40  ? 26.595 5.150   -3.956  1.00 13.60 ?  40  ASN   A ND2  1 
ATOM   934  H H    A ASN   A 1 40  ? 27.361 2.514   -2.087  0.72 12.83 ?  40  ASN   A H    1 
ATOM   935  H H    B ASN   A 1 40  ? 27.303 2.539   -2.109  0.28 12.83 ?  40  ASN   A H    1 
ATOM   936  H HA   . ASN   A 1 40  ? 27.345 0.950   -4.297  1.00 12.86 ?  40  ASN   A HA   1 
ATOM   937  H HB2  . ASN   A 1 40  ? 27.597 2.879   -5.596  1.00 13.96 ?  40  ASN   A HB2  1 
ATOM   938  H HB3  . ASN   A 1 40  ? 26.237 2.915   -4.778  1.00 13.96 ?  40  ASN   A HB3  1 
ATOM   939  H HD21 . ASN   A 1 40  ? 26.756 5.933   -3.630  1.00 16.33 ?  40  ASN   A HD21 1 
ATOM   940  H HD22 . ASN   A 1 40  ? 25.792 4.936   -4.175  1.00 16.33 ?  40  ASN   A HD22 1 
ATOM   941  N N    A VAL   A 1 41  ? 29.834 1.384   -4.969  0.72 10.92 ?  41  VAL   A N    1 
ATOM   942  N N    B VAL   A 1 41  ? 29.781 1.372   -4.993  0.28 11.11 ?  41  VAL   A N    1 
ATOM   943  C CA   A VAL   A 1 41  ? 31.266 1.063   -4.975  0.72 11.43 ?  41  VAL   A CA   1 
ATOM   944  C CA   B VAL   A 1 41  ? 31.207 1.080   -5.110  0.28 11.79 ?  41  VAL   A CA   1 
ATOM   945  C C    A VAL   A 1 41  ? 32.134 2.211   -4.492  0.72 11.02 ?  41  VAL   A C    1 
ATOM   946  C C    B VAL   A 1 41  ? 32.052 2.250   -4.636  0.28 11.89 ?  41  VAL   A C    1 
ATOM   947  O O    A VAL   A 1 41  ? 33.279 1.975   -4.089  0.72 11.88 ?  41  VAL   A O    1 
ATOM   948  O O    B VAL   A 1 41  ? 33.199 2.063   -4.211  0.28 12.37 ?  41  VAL   A O    1 
ATOM   949  C CB   A VAL   A 1 41  ? 31.779 0.564   -6.344  0.72 12.08 ?  41  VAL   A CB   1 
ATOM   950  C CB   B VAL   A 1 41  ? 31.558 0.679   -6.558  0.28 12.31 ?  41  VAL   A CB   1 
ATOM   951  C CG1  A VAL   A 1 41  ? 31.060 -0.719  -6.757  0.72 13.24 ?  41  VAL   A CG1  1 
ATOM   952  C CG1  B VAL   A 1 41  ? 30.945 -0.673  -6.901  0.28 13.01 ?  41  VAL   A CG1  1 
ATOM   953  C CG2  A VAL   A 1 41  ? 31.676 1.647   -7.420  0.72 12.02 ?  41  VAL   A CG2  1 
ATOM   954  C CG2  B VAL   A 1 41  ? 31.104 1.751   -7.550  0.28 12.80 ?  41  VAL   A CG2  1 
ATOM   955  H H    A VAL   A 1 41  ? 29.464 1.388   -5.743  0.72 13.11 ?  41  VAL   A H    1 
ATOM   956  H H    B VAL   A 1 41  ? 29.352 1.352   -5.740  0.28 13.34 ?  41  VAL   A H    1 
ATOM   957  H HA   A VAL   A 1 41  ? 31.412 0.338   -4.348  0.72 13.72 ?  41  VAL   A HA   1 
ATOM   958  H HA   B VAL   A 1 41  ? 31.408 0.319   -4.544  0.28 14.15 ?  41  VAL   A HA   1 
ATOM   959  H HB   A VAL   A 1 41  ? 32.719 0.337   -6.257  0.72 14.50 ?  41  VAL   A HB   1 
ATOM   960  H HB   B VAL   A 1 41  ? 32.520 0.593   -6.633  0.28 14.77 ?  41  VAL   A HB   1 
ATOM   961  H HG11 A VAL   A 1 41  ? 31.406 -1.021  -7.612  0.72 15.90 ?  41  VAL   A HG11 1 
ATOM   962  H HG11 B VAL   A 1 41  ? 31.231 -0.934  -7.790  0.28 15.61 ?  41  VAL   A HG11 1 
ATOM   963  H HG12 A VAL   A 1 41  ? 31.209 -1.400  -6.082  0.72 15.90 ?  41  VAL   A HG12 1 
ATOM   964  H HG12 B VAL   A 1 41  ? 31.243 -1.329  -6.252  0.28 15.61 ?  41  VAL   A HG12 1 
ATOM   965  H HG13 A VAL   A 1 41  ? 30.108 -0.538  -6.835  0.72 15.90 ?  41  VAL   A HG13 1 
ATOM   966  H HG13 B VAL   A 1 41  ? 29.978 -0.598  -6.873  0.28 15.61 ?  41  VAL   A HG13 1 
ATOM   967  H HG21 A VAL   A 1 41  ? 31.888 1.257   -8.284  0.72 14.43 ?  41  VAL   A HG21 1 
ATOM   968  H HG21 B VAL   A 1 41  ? 31.444 1.529   -8.430  0.28 15.36 ?  41  VAL   A HG21 1 
ATOM   969  H HG22 A VAL   A 1 41  ? 30.774 1.997   -7.427  0.72 14.43 ?  41  VAL   A HG22 1 
ATOM   970  H HG22 B VAL   A 1 41  ? 30.134 1.779   -7.572  0.28 15.36 ?  41  VAL   A HG22 1 
ATOM   971  H HG23 A VAL   A 1 41  ? 32.308 2.353   -7.214  0.72 14.43 ?  41  VAL   A HG23 1 
ATOM   972  H HG23 B VAL   A 1 41  ? 31.453 2.610   -7.268  0.28 15.36 ?  41  VAL   A HG23 1 
ATOM   973  N N    A TYR   A 1 42  ? 31.634 3.449   -4.552  0.72 11.16 ?  42  TYR   A N    1 
ATOM   974  N N    B TYR   A 1 42  ? 31.521 3.469   -4.720  0.28 11.59 ?  42  TYR   A N    1 
ATOM   975  C CA   A TYR   A 1 42  ? 32.380 4.631   -4.135  0.72 10.87 ?  42  TYR   A CA   1 
ATOM   976  C CA   B TYR   A 1 42  ? 32.251 4.659   -4.306  0.28 11.61 ?  42  TYR   A CA   1 
ATOM   977  C C    A TYR   A 1 42  ? 32.136 4.994   -2.678  0.72 10.85 ?  42  TYR   A C    1 
ATOM   978  C C    B TYR   A 1 42  ? 31.954 5.070   -2.872  0.28 11.10 ?  42  TYR   A C    1 
ATOM   979  O O    A TYR   A 1 42  ? 32.715 5.970   -2.181  0.72 11.52 ?  42  TYR   A O    1 
ATOM   980  O O    B TYR   A 1 42  ? 32.480 6.091   -2.413  0.28 11.33 ?  42  TYR   A O    1 
ATOM   981  C CB   A TYR   A 1 42  ? 32.019 5.824   -5.039  0.72 11.66 ?  42  TYR   A CB   1 
ATOM   982  C CB   B TYR   A 1 42  ? 31.947 5.824   -5.255  0.28 12.26 ?  42  TYR   A CB   1 
ATOM   983  C CG   A TYR   A 1 42  ? 32.172 5.522   -6.520  0.72 12.93 ?  42  TYR   A CG   1 
ATOM   984  C CG   B TYR   A 1 42  ? 32.233 5.495   -6.700  0.28 12.69 ?  42  TYR   A CG   1 
ATOM   985  C CD1  A TYR   A 1 42  ? 33.422 5.321   -7.083  0.72 13.63 ?  42  TYR   A CD1  1 
ATOM   986  C CD1  B TYR   A 1 42  ? 33.532 5.288   -7.141  0.28 13.17 ?  42  TYR   A CD1  1 
ATOM   987  C CD2  A TYR   A 1 42  ? 31.061 5.416   -7.350  0.72 14.67 ?  42  TYR   A CD2  1 
ATOM   988  C CD2  B TYR   A 1 42  ? 31.201 5.376   -7.621  0.28 13.03 ?  42  TYR   A CD2  1 
ATOM   989  C CE1  A TYR   A 1 42  ? 33.564 5.024   -8.431  0.72 13.93 ?  42  TYR   A CE1  1 
ATOM   990  C CE1  B TYR   A 1 42  ? 33.796 4.973   -8.460  0.28 13.44 ?  42  TYR   A CE1  1 
ATOM   991  C CE2  A TYR   A 1 42  ? 31.196 5.132   -8.701  0.72 15.42 ?  42  TYR   A CE2  1 
ATOM   992  C CE2  B TYR   A 1 42  ? 31.456 5.066   -8.942  0.28 13.35 ?  42  TYR   A CE2  1 
ATOM   993  C CZ   A TYR   A 1 42  ? 32.451 4.933   -9.234  0.72 15.19 ?  42  TYR   A CZ   1 
ATOM   994  C CZ   B TYR   A 1 42  ? 32.754 4.866   -9.356  0.28 13.65 ?  42  TYR   A CZ   1 
ATOM   995  O OH   A TYR   A 1 42  ? 32.595 4.647   -10.572 0.72 16.56 ?  42  TYR   A OH   1 
ATOM   996  O OH   B TYR   A 1 42  ? 33.006 4.554   -10.671 0.28 14.61 ?  42  TYR   A OH   1 
ATOM   997  H H    A TYR   A 1 42  ? 30.843 3.630   -4.839  0.72 13.40 ?  42  TYR   A H    1 
ATOM   998  H H    B TYR   A 1 42  ? 30.730 3.629   -5.023  0.28 13.92 ?  42  TYR   A H    1 
ATOM   999  H HA   A TYR   A 1 42  ? 33.327 4.463   -4.249  0.72 13.05 ?  42  TYR   A HA   1 
ATOM   1000 H HA   B TYR   A 1 42  ? 33.197 4.472   -4.369  0.28 13.94 ?  42  TYR   A HA   1 
ATOM   1001 H HB2  A TYR   A 1 42  ? 31.093 6.076   -4.882  0.72 13.99 ?  42  TYR   A HB2  1 
ATOM   1002 H HB2  B TYR   A 1 42  ? 31.007 6.056   -5.181  0.28 14.72 ?  42  TYR   A HB2  1 
ATOM   1003 H HB3  A TYR   A 1 42  ? 32.600 6.574   -4.829  0.72 13.99 ?  42  TYR   A HB3  1 
ATOM   1004 H HB3  B TYR   A 1 42  ? 32.496 6.582   -5.006  0.28 14.72 ?  42  TYR   A HB3  1 
ATOM   1005 H HD1  A TYR   A 1 42  ? 34.180 5.378   -6.546  0.72 16.36 ?  42  TYR   A HD1  1 
ATOM   1006 H HD1  B TYR   A 1 42  ? 34.237 5.358   -6.536  0.28 15.81 ?  42  TYR   A HD1  1 
ATOM   1007 H HD2  A TYR   A 1 42  ? 30.214 5.552   -6.996  0.72 17.61 ?  42  TYR   A HD2  1 
ATOM   1008 H HD2  B TYR   A 1 42  ? 30.323 5.511   -7.341  0.28 15.65 ?  42  TYR   A HD2  1 
ATOM   1009 H HE1  A TYR   A 1 42  ? 34.412 4.894   -8.796  0.72 16.72 ?  42  TYR   A HE1  1 
ATOM   1010 H HE1  B TYR   A 1 42  ? 34.673 4.841   -8.743  0.28 16.13 ?  42  TYR   A HE1  1 
ATOM   1011 H HE2  A TYR   A 1 42  ? 30.443 5.069   -9.247  0.72 18.51 ?  42  TYR   A HE2  1 
ATOM   1012 H HE2  B TYR   A 1 42  ? 30.754 4.995   -9.549  0.28 16.03 ?  42  TYR   A HE2  1 
ATOM   1013 H HH   A TYR   A 1 42  ? 33.413 4.546   -10.763 0.72 19.88 ?  42  TYR   A HH   1 
ATOM   1014 H HH   B TYR   A 1 42  ? 33.780 4.240   -10.745 0.28 17.54 ?  42  TYR   A HH   1 
ATOM   1015 N N    A LEU   A 1 43  ? 31.279 4.237   -1.995  0.72 10.84 ?  43  LEU   A N    1 
ATOM   1016 N N    B LEU   A 1 43  ? 31.125 4.305   -2.161  0.28 10.70 ?  43  LEU   A N    1 
ATOM   1017 C CA   A LEU   A 1 43  ? 30.818 4.577   -0.653  0.72 10.43 ?  43  LEU   A CA   1 
ATOM   1018 C CA   B LEU   A 1 43  ? 30.717 4.628   -0.795  0.28 10.64 ?  43  LEU   A CA   1 
ATOM   1019 C C    A LEU   A 1 43  ? 30.343 6.026   -0.570  0.72 10.16 ?  43  LEU   A C    1 
ATOM   1020 C C    B LEU   A 1 43  ? 30.233 6.072   -0.676  0.28 11.15 ?  43  LEU   A C    1 
ATOM   1021 O O    A LEU   A 1 43  ? 30.616 6.733   0.405   0.72 11.46 ?  43  LEU   A O    1 
ATOM   1022 O O    B LEU   A 1 43  ? 30.463 6.747   0.330   0.28 11.87 ?  43  LEU   A O    1 
ATOM   1023 C CB   A LEU   A 1 43  ? 31.863 4.280   0.421   0.72 10.93 ?  43  LEU   A CB   1 
ATOM   1024 C CB   B LEU   A 1 43  ? 31.811 4.311   0.227   0.28 10.77 ?  43  LEU   A CB   1 
ATOM   1025 C CG   A LEU   A 1 43  ? 32.368 2.833   0.535   0.72 11.30 ?  43  LEU   A CG   1 
ATOM   1026 C CG   B LEU   A 1 43  ? 32.268 2.847   0.287   0.28 10.86 ?  43  LEU   A CG   1 
ATOM   1027 C CD1  A LEU   A 1 43  ? 33.391 2.735   1.657   0.72 11.99 ?  43  LEU   A CD1  1 
ATOM   1028 C CD1  B LEU   A 1 43  ? 33.368 2.668   1.326   0.28 10.89 ?  43  LEU   A CD1  1 
ATOM   1029 C CD2  A LEU   A 1 43  ? 31.241 1.834   0.755   0.72 12.00 ?  43  LEU   A CD2  1 
ATOM   1030 C CD2  B LEU   A 1 43  ? 31.100 1.910   0.572   0.28 11.03 ?  43  LEU   A CD2  1 
ATOM   1031 H H    A LEU   A 1 43  ? 30.946 3.498   -2.295  0.72 13.01 ?  43  LEU   A H    1 
ATOM   1032 H H    B LEU   A 1 43  ? 30.777 3.574   -2.453  0.28 12.84 ?  43  LEU   A H    1 
ATOM   1033 H HA   A LEU   A 1 43  ? 30.050 4.017   -0.456  0.72 12.52 ?  43  LEU   A HA   1 
ATOM   1034 H HA   B LEU   A 1 43  ? 29.959 4.069   -0.574  0.28 12.77 ?  43  LEU   A HA   1 
ATOM   1035 H HB2  A LEU   A 1 43  ? 32.634 4.843   0.257   0.72 13.12 ?  43  LEU   A HB2  1 
ATOM   1036 H HB2  B LEU   A 1 43  ? 32.590 4.849   0.024   0.28 12.93 ?  43  LEU   A HB2  1 
ATOM   1037 H HB3  A LEU   A 1 43  ? 31.477 4.509   1.281   0.72 13.12 ?  43  LEU   A HB3  1 
ATOM   1038 H HB3  B LEU   A 1 43  ? 31.480 4.542   1.110   0.28 12.93 ?  43  LEU   A HB3  1 
ATOM   1039 H HG   A LEU   A 1 43  ? 32.822 2.598   -0.291  0.72 13.56 ?  43  LEU   A HG   1 
ATOM   1040 H HG   B LEU   A 1 43  ? 32.640 2.604   -0.575  0.28 13.04 ?  43  LEU   A HG   1 
ATOM   1041 H HD11 A LEU   A 1 43  ? 33.708 1.820   1.718   0.72 14.39 ?  43  LEU   A HD11 1 
ATOM   1042 H HD11 B LEU   A 1 43  ? 33.642 1.737   1.340   0.28 13.08 ?  43  LEU   A HD11 1 
ATOM   1043 H HD12 A LEU   A 1 43  ? 34.135 3.329   1.463   0.72 14.39 ?  43  LEU   A HD12 1 
ATOM   1044 H HD12 B LEU   A 1 43  ? 34.123 3.231   1.090   0.28 13.08 ?  43  LEU   A HD12 1 
ATOM   1045 H HD13 A LEU   A 1 43  ? 32.971 2.997   2.491   0.72 14.39 ?  43  LEU   A HD13 1 
ATOM   1046 H HD13 B LEU   A 1 43  ? 33.025 2.924   2.197   0.28 13.08 ?  43  LEU   A HD13 1 
ATOM   1047 H HD21 A LEU   A 1 43  ? 31.627 0.954   0.889   0.72 14.41 ?  43  LEU   A HD21 1 
ATOM   1048 H HD21 B LEU   A 1 43  ? 31.446 1.022   0.753   0.28 13.24 ?  43  LEU   A HD21 1 
ATOM   1049 H HD22 A LEU   A 1 43  ? 30.738 2.100   1.537   0.72 14.41 ?  43  LEU   A HD22 1 
ATOM   1050 H HD22 B LEU   A 1 43  ? 30.613 2.239   1.343   0.28 13.24 ?  43  LEU   A HD22 1 
ATOM   1051 H HD23 A LEU   A 1 43  ? 30.672 1.832   -0.028  0.72 14.41 ?  43  LEU   A HD23 1 
ATOM   1052 H HD23 B LEU   A 1 43  ? 30.519 1.888   -0.203  0.28 13.24 ?  43  LEU   A HD23 1 
ATOM   1053 N N    A LYS   A 1 44  ? 29.606 6.463   -1.596  0.72 10.54 ?  44  LYS   A N    1 
ATOM   1054 N N    B LYS   A 1 44  ? 29.534 6.540   -1.710  0.28 11.44 ?  44  LYS   A N    1 
ATOM   1055 C CA   A LYS   A 1 44  ? 28.959 7.774   -1.597  0.72 10.94 ?  44  LYS   A CA   1 
ATOM   1056 C CA   B LYS   A 1 44  ? 28.877 7.845   -1.691  0.28 12.08 ?  44  LYS   A CA   1 
ATOM   1057 C C    A LYS   A 1 44  ? 27.527 7.586   -1.113  0.72 10.45 ?  44  LYS   A C    1 
ATOM   1058 C C    B LYS   A 1 44  ? 27.476 7.635   -1.137  0.28 11.19 ?  44  LYS   A C    1 
ATOM   1059 O O    A LYS   A 1 44  ? 26.673 7.063   -1.836  0.72 11.34 ?  44  LYS   A O    1 
ATOM   1060 O O    B LYS   A 1 44  ? 26.584 7.149   -1.837  0.28 11.59 ?  44  LYS   A O    1 
ATOM   1061 C CB   A LYS   A 1 44  ? 29.026 8.420   -2.974  0.72 12.78 ?  44  LYS   A CB   1 
ATOM   1062 C CB   B LYS   A 1 44  ? 28.827 8.442   -3.093  0.28 14.33 ?  44  LYS   A CB   1 
ATOM   1063 C CG   A LYS   A 1 44  ? 30.413 8.906   -3.366  0.72 16.07 ?  44  LYS   A CG   1 
ATOM   1064 C CG   B LYS   A 1 44  ? 30.172 8.893   -3.638  0.28 16.68 ?  44  LYS   A CG   1 
ATOM   1065 C CD   A LYS   A 1 44  ? 31.077 9.758   -2.286  0.72 21.53 ?  44  LYS   A CD   1 
ATOM   1066 C CD   B LYS   A 1 44  ? 30.824 9.948   -2.754  0.28 19.08 ?  44  LYS   A CD   1 
ATOM   1067 C CE   A LYS   A 1 44  ? 32.397 10.326  -2.777  0.72 24.57 ?  44  LYS   A CE   1 
ATOM   1068 C CE   B LYS   A 1 44  ? 32.175 10.361  -3.309  0.28 20.81 ?  44  LYS   A CE   1 
ATOM   1069 N NZ   A LYS   A 1 44  ? 33.233 10.853  -1.665  0.72 25.73 ?  44  LYS   A NZ   1 
ATOM   1070 N NZ   B LYS   A 1 44  ? 33.041 10.989  -2.273  0.28 21.93 ?  44  LYS   A NZ   1 
ATOM   1071 H H    A LYS   A 1 44  ? 29.465 6.007   -2.317  0.72 12.65 ?  44  LYS   A H    1 
ATOM   1072 H H    B LYS   A 1 44  ? 29.418 6.106   -2.442  0.28 13.73 ?  44  LYS   A H    1 
ATOM   1073 H HA   A LYS   A 1 44  ? 29.405 8.340   -0.951  0.72 13.13 ?  44  LYS   A HA   1 
ATOM   1074 H HA   B LYS   A 1 44  ? 29.350 8.445   -1.096  0.28 14.50 ?  44  LYS   A HA   1 
ATOM   1075 H HB2  A LYS   A 1 44  ? 28.739 7.775   -3.637  0.72 15.34 ?  44  LYS   A HB2  1 
ATOM   1076 H HB2  B LYS   A 1 44  ? 28.473 7.774   -3.700  0.28 17.20 ?  44  LYS   A HB2  1 
ATOM   1077 H HB3  A LYS   A 1 44  ? 28.429 9.187   -2.983  0.72 15.34 ?  44  LYS   A HB3  1 
ATOM   1078 H HB3  B LYS   A 1 44  ? 28.241 9.214   -3.079  0.28 17.20 ?  44  LYS   A HB3  1 
ATOM   1079 H HG2  A LYS   A 1 44  ? 30.982 8.140   -3.534  0.72 19.29 ?  44  LYS   A HG2  1 
ATOM   1080 H HG2  B LYS   A 1 44  ? 30.768 8.130   -3.689  0.28 20.03 ?  44  LYS   A HG2  1 
ATOM   1081 H HG3  A LYS   A 1 44  ? 30.342 9.449   -4.169  0.72 19.29 ?  44  LYS   A HG3  1 
ATOM   1082 H HG3  B LYS   A 1 44  ? 30.045 9.277   -4.521  0.28 20.03 ?  44  LYS   A HG3  1 
ATOM   1083 H HD2  A LYS   A 1 44  ? 30.485 10.491  -2.048  0.72 25.85 ?  44  LYS   A HD2  1 
ATOM   1084 H HD2  B LYS   A 1 44  ? 30.252 10.730  -2.712  0.28 22.90 ?  44  LYS   A HD2  1 
ATOM   1085 H HD3  A LYS   A 1 44  ? 31.259 9.205   -1.509  0.72 25.85 ?  44  LYS   A HD3  1 
ATOM   1086 H HD3  B LYS   A 1 44  ? 30.965 9.585   -1.865  0.28 22.90 ?  44  LYS   A HD3  1 
ATOM   1087 H HE2  A LYS   A 1 44  ? 32.897 9.623   -3.222  0.72 29.48 ?  44  LYS   A HE2  1 
ATOM   1088 H HE2  B LYS   A 1 44  ? 32.633 9.575   -3.648  0.28 24.98 ?  44  LYS   A HE2  1 
ATOM   1089 H HE3  A LYS   A 1 44  ? 32.219 11.051  -3.395  0.72 29.48 ?  44  LYS   A HE3  1 
ATOM   1090 H HE3  B LYS   A 1 44  ? 32.042 11.004  -4.021  0.28 24.98 ?  44  LYS   A HE3  1 
ATOM   1091 H HZ1  A LYS   A 1 44  ? 33.996 11.179  -1.987  0.72 30.88 ?  44  LYS   A HZ1  1 
ATOM   1092 H HZ1  B LYS   A 1 44  ? 33.824 11.219  -2.630  0.28 26.32 ?  44  LYS   A HZ1  1 
ATOM   1093 H HZ2  A LYS   A 1 44  ? 32.797 11.506  -1.242  0.72 30.88 ?  44  LYS   A HZ2  1 
ATOM   1094 H HZ2  B LYS   A 1 44  ? 32.647 11.717  -1.948  0.28 26.32 ?  44  LYS   A HZ2  1 
ATOM   1095 H HZ3  A LYS   A 1 44  ? 33.415 10.205  -1.085  0.72 30.88 ?  44  LYS   A HZ3  1 
ATOM   1096 H HZ3  B LYS   A 1 44  ? 33.186 10.416  -1.607  0.28 26.32 ?  44  LYS   A HZ3  1 
ATOM   1097 N N    . HIS   A 1 45  ? 27.278 7.992   0.130   1.00 10.66 ?  45  HIS   A N    1 
ATOM   1098 C CA   . HIS   A 1 45  ? 26.039 7.658   0.828   1.00 10.61 ?  45  HIS   A CA   1 
ATOM   1099 C C    . HIS   A 1 45  ? 25.021 8.785   0.653   1.00 11.50 ?  45  HIS   A C    1 
ATOM   1100 O O    . HIS   A 1 45  ? 24.729 9.550   1.568   1.00 13.31 ?  45  HIS   A O    1 
ATOM   1101 C CB   . HIS   A 1 45  ? 26.332 7.403   2.295   1.00 10.59 ?  45  HIS   A CB   1 
ATOM   1102 C CG   . HIS   A 1 45  ? 27.443 6.431   2.527   1.00 10.06 ?  45  HIS   A CG   1 
ATOM   1103 N ND1  . HIS   A 1 45  ? 27.438 5.143   2.024   1.00 10.66 ?  45  HIS   A ND1  1 
ATOM   1104 C CD2  . HIS   A 1 45  ? 28.606 6.583   3.204   1.00 10.66 ?  45  HIS   A CD2  1 
ATOM   1105 C CE1  . HIS   A 1 45  ? 28.557 4.547   2.399   1.00 10.41 ?  45  HIS   A CE1  1 
ATOM   1106 N NE2  . HIS   A 1 45  ? 29.284 5.397   3.109   1.00 10.65 ?  45  HIS   A NE2  1 
ATOM   1107 H H    A HIS   A 1 45  ? 27.819 8.469   0.603   0.72 12.80 ?  45  HIS   A H    1 
ATOM   1108 H H    B HIS   A 1 45  ? 27.845 8.427   0.612   0.28 12.80 ?  45  HIS   A H    1 
ATOM   1109 H HA   . HIS   A 1 45  ? 25.661 6.849   0.449   1.00 12.73 ?  45  HIS   A HA   1 
ATOM   1110 H HB2  . HIS   A 1 45  ? 26.568 8.242   2.720   1.00 12.71 ?  45  HIS   A HB2  1 
ATOM   1111 H HB3  . HIS   A 1 45  ? 25.527 7.044   2.717   1.00 12.71 ?  45  HIS   A HB3  1 
ATOM   1112 H HD2  . HIS   A 1 45  ? 28.895 7.352   3.647   1.00 12.80 ?  45  HIS   A HD2  1 
ATOM   1113 H HE1  . HIS   A 1 45  ? 28.791 3.670   2.206   1.00 12.50 ?  45  HIS   A HE1  1 
ATOM   1114 H HE2  . HIS   A 1 45  ? 30.051 5.228   3.462   1.00 12.78 ?  45  HIS   A HE2  1 
ATOM   1115 N N    A GLY   A 1 46  ? 24.414 8.829   -0.529  0.72 12.43 ?  46  GLY   A N    1 
ATOM   1116 N N    B GLY   A 1 46  ? 24.511 8.902   -0.569  0.28 11.73 ?  46  GLY   A N    1 
ATOM   1117 C CA   A GLY   A 1 46  ? 23.558 9.947   -0.882  0.72 12.99 ?  46  GLY   A CA   1 
ATOM   1118 C CA   B GLY   A 1 46  ? 23.752 10.080  -0.950  0.28 11.76 ?  46  GLY   A CA   1 
ATOM   1119 C C    A GLY   A 1 46  ? 22.081 9.783   -0.575  0.72 13.10 ?  46  GLY   A C    1 
ATOM   1120 C C    B GLY   A 1 46  ? 22.270 10.025  -0.633  0.28 11.63 ?  46  GLY   A C    1 
ATOM   1121 O O    A GLY   A 1 46  ? 21.425 10.737  -0.139  0.72 13.94 ?  46  GLY   A O    1 
ATOM   1122 O O    B GLY   A 1 46  ? 21.638 11.062  -0.406  0.28 11.97 ?  46  GLY   A O    1 
ATOM   1123 H H    A GLY   A 1 46  ? 24.477 8.226   -1.136  0.72 14.93 ?  46  GLY   A H    1 
ATOM   1124 H H    B GLY   A 1 46  ? 24.593 8.314   -1.189  0.28 14.08 ?  46  GLY   A H    1 
ATOM   1125 H HA2  A GLY   A 1 46  ? 23.860 10.737  -0.407  0.72 15.59 ?  46  GLY   A HA2  1 
ATOM   1126 H HA2  B GLY   A 1 46  ? 24.136 10.855  -0.505  0.28 14.12 ?  46  GLY   A HA2  1 
ATOM   1127 H HA3  A GLY   A 1 46  ? 23.650 10.122  -1.832  0.72 15.59 ?  46  GLY   A HA3  1 
ATOM   1128 H HA3  B GLY   A 1 46  ? 23.841 10.211  -1.905  0.28 14.12 ?  46  GLY   A HA3  1 
ATOM   1129 N N    A GLY   A 1 47  ? 21.536 8.591   -0.806  0.72 12.77 ?  47  GLY   A N    1 
ATOM   1130 N N    B GLY   A 1 47  ? 21.705 8.827   -0.642  0.28 11.18 ?  47  GLY   A N    1 
ATOM   1131 C CA   A GLY   A 1 47  ? 20.105 8.386   -0.721  0.72 12.46 ?  47  GLY   A CA   1 
ATOM   1132 C CA   B GLY   A 1 47  ? 20.286 8.655   -0.407  0.28 11.57 ?  47  GLY   A CA   1 
ATOM   1133 C C    A GLY   A 1 47  ? 19.776 6.968   -0.302  0.72 11.94 ?  47  GLY   A C    1 
ATOM   1134 C C    B GLY   A 1 47  ? 19.971 7.194   -0.173  0.28 11.66 ?  47  GLY   A C    1 
ATOM   1135 O O    A GLY   A 1 47  ? 20.663 6.147   -0.048  0.72 11.97 ?  47  GLY   A O    1 
ATOM   1136 O O    B GLY   A 1 47  ? 20.865 6.347   -0.108  0.28 12.35 ?  47  GLY   A O    1 
ATOM   1137 H H    A GLY   A 1 47  ? 21.981 7.879   -1.000  0.72 15.33 ?  47  GLY   A H    1 
ATOM   1138 H H    B GLY   A 1 47  ? 22.124 8.096   -0.784  0.28 13.42 ?  47  GLY   A H    1 
ATOM   1139 H HA2  A GLY   A 1 47  ? 19.722 8.994   -0.071  0.72 14.95 ?  47  GLY   A HA2  1 
ATOM   1140 H HA2  B GLY   A 1 47  ? 20.005 9.175   0.367   0.28 13.88 ?  47  GLY   A HA2  1 
ATOM   1141 H HA3  A GLY   A 1 47  ? 19.697 8.554   -1.585  0.72 14.95 ?  47  GLY   A HA3  1 
ATOM   1142 H HA3  B GLY   A 1 47  ? 19.786 8.962   -1.182  0.28 13.88 ?  47  GLY   A HA3  1 
ATOM   1143 N N    A GLY   A 1 48  ? 18.481 6.673   -0.249  0.72 12.24 ?  48  GLY   A N    1 
ATOM   1144 N N    B GLY   A 1 48  ? 18.679 6.903   -0.055  0.28 12.27 ?  48  GLY   A N    1 
ATOM   1145 C CA   A GLY   A 1 48  ? 18.061 5.368   0.208   0.72 12.59 ?  48  GLY   A CA   1 
ATOM   1146 C CA   B GLY   A 1 48  ? 18.258 5.537   0.188   0.28 12.18 ?  48  GLY   A CA   1 
ATOM   1147 C C    A GLY   A 1 48  ? 18.584 5.090   1.603   0.72 11.86 ?  48  GLY   A C    1 
ATOM   1148 C C    B GLY   A 1 48  ? 18.633 5.077   1.587   0.28 11.38 ?  48  GLY   A C    1 
ATOM   1149 O O    A GLY   A 1 48  ? 18.793 6.001   2.418   0.72 12.27 ?  48  GLY   A O    1 
ATOM   1150 O O    B GLY   A 1 48  ? 18.618 5.847   2.554   0.28 11.40 ?  48  GLY   A O    1 
ATOM   1151 H H    A GLY   A 1 48  ? 17.839 7.209   -0.449  0.72 14.69 ?  48  GLY   A H    1 
ATOM   1152 H H    B GLY   A 1 48  ? 18.045 7.475   -0.107  0.28 14.73 ?  48  GLY   A H    1 
ATOM   1153 H HA2  A GLY   A 1 48  ? 17.092 5.313   0.223   0.72 15.11 ?  48  GLY   A HA2  1 
ATOM   1154 H HA2  B GLY   A 1 48  ? 17.298 5.469   0.083   0.28 14.62 ?  48  GLY   A HA2  1 
ATOM   1155 H HA3  A GLY   A 1 48  ? 18.404 4.684   -0.387  0.72 15.11 ?  48  GLY   A HA3  1 
ATOM   1156 H HA3  B GLY   A 1 48  ? 18.684 4.944   -0.452  0.28 14.62 ?  48  GLY   A HA3  1 
ATOM   1157 N N    A VAL   A 1 49  ? 18.804 3.803   1.880   0.72 11.12 ?  49  VAL   A N    1 
ATOM   1158 N N    B VAL   A 1 49  ? 18.972 3.790   1.691   0.28 10.99 ?  49  VAL   A N    1 
ATOM   1159 C CA   A VAL   A 1 49  ? 19.329 3.382   3.177   0.72 11.41 ?  49  VAL   A CA   1 
ATOM   1160 C CA   B VAL   A 1 49  ? 19.484 3.254   2.950   0.28 10.09 ?  49  VAL   A CA   1 
ATOM   1161 C C    A VAL   A 1 49  ? 20.642 4.089   3.494   0.72 10.39 ?  49  VAL   A C    1 
ATOM   1162 C C    B VAL   A 1 49  ? 20.766 3.970   3.349   0.28 9.34  ?  49  VAL   A C    1 
ATOM   1163 O O    A VAL   A 1 49  ? 20.858 4.538   4.625   0.72 10.92 ?  49  VAL   A O    1 
ATOM   1164 O O    B VAL   A 1 49  ? 20.955 4.329   4.517   0.28 9.66  ?  49  VAL   A O    1 
ATOM   1165 C CB   A VAL   A 1 49  ? 19.476 1.849   3.216   0.72 12.16 ?  49  VAL   A CB   1 
ATOM   1166 C CB   B VAL   A 1 49  ? 19.707 1.734   2.833   0.28 9.46  ?  49  VAL   A CB   1 
ATOM   1167 C CG1  A VAL   A 1 49  ? 20.300 1.412   4.417   0.72 12.11 ?  49  VAL   A CG1  1 
ATOM   1168 C CG1  B VAL   A 1 49  ? 20.533 1.220   4.011   0.28 9.83  ?  49  VAL   A CG1  1 
ATOM   1169 C CG2  A VAL   A 1 49  ? 18.102 1.193   3.244   0.72 14.20 ?  49  VAL   A CG2  1 
ATOM   1170 C CG2  B VAL   A 1 49  ? 18.385 0.997   2.748   0.28 9.07  ?  49  VAL   A CG2  1 
ATOM   1171 H H    A VAL   A 1 49  ? 18.657 3.150   1.336   0.72 13.35 ?  49  VAL   A H    1 
ATOM   1172 H H    B VAL   A 1 49  ? 18.924 3.214   1.056   0.28 13.20 ?  49  VAL   A H    1 
ATOM   1173 H HA   A VAL   A 1 49  ? 18.698 3.629   3.867   0.72 13.70 ?  49  VAL   A HA   1 
ATOM   1174 H HA   B VAL   A 1 49  ? 18.827 3.402   3.650   0.28 12.12 ?  49  VAL   A HA   1 
ATOM   1175 H HB   A VAL   A 1 49  ? 19.936 1.549   2.415   0.72 14.60 ?  49  VAL   A HB   1 
ATOM   1176 H HB   B VAL   A 1 49  ? 20.205 1.554   2.022   0.28 11.36 ?  49  VAL   A HB   1 
ATOM   1177 H HG11 A VAL   A 1 49  ? 20.144 0.469   4.578   0.72 14.53 ?  49  VAL   A HG11 1 
ATOM   1178 H HG11 B VAL   A 1 49  ? 20.416 0.260   4.081   0.28 11.80 ?  49  VAL   A HG11 1 
ATOM   1179 H HG12 A VAL   A 1 49  ? 21.239 1.564   4.231   0.72 14.53 ?  49  VAL   A HG12 1 
ATOM   1180 H HG12 B VAL   A 1 49  ? 21.470 1.426   3.860   0.28 11.80 ?  49  VAL   A HG12 1 
ATOM   1181 H HG13 A VAL   A 1 49  ? 20.024 1.929   5.190   0.72 14.53 ?  49  VAL   A HG13 1 
ATOM   1182 H HG13 B VAL   A 1 49  ? 20.224 1.649   4.824   0.28 11.80 ?  49  VAL   A HG13 1 
ATOM   1183 H HG21 A VAL   A 1 49  ? 18.210 0.229   3.263   0.72 17.05 ?  49  VAL   A HG21 1 
ATOM   1184 H HG21 B VAL   A 1 49  ? 18.556 0.048   2.636   0.28 10.89 ?  49  VAL   A HG21 1 
ATOM   1185 H HG22 A VAL   A 1 49  ? 17.629 1.488   4.039   0.72 17.05 ?  49  VAL   A HG22 1 
ATOM   1186 H HG22 B VAL   A 1 49  ? 17.886 1.147   3.566   0.28 10.89 ?  49  VAL   A HG22 1 
ATOM   1187 H HG23 A VAL   A 1 49  ? 17.612 1.456   2.450   0.72 17.05 ?  49  VAL   A HG23 1 
ATOM   1188 H HG23 B VAL   A 1 49  ? 17.885 1.334   1.988   0.28 10.89 ?  49  VAL   A HG23 1 
ATOM   1189 N N    A ALA   A 1 50  ? 21.549 4.160   2.514   0.72 9.98  ?  50  ALA   A N    1 
ATOM   1190 N N    B ALA   A 1 50  ? 21.678 4.159   2.392   0.28 9.12  ?  50  ALA   A N    1 
ATOM   1191 C CA   A ALA   A 1 50  ? 22.872 4.721   2.773   0.72 10.12 ?  50  ALA   A CA   1 
ATOM   1192 C CA   B ALA   A 1 50  ? 22.976 4.744   2.710   0.28 9.62  ?  50  ALA   A CA   1 
ATOM   1193 C C    A ALA   A 1 50  ? 22.776 6.180   3.195   0.72 9.88  ?  50  ALA   A C    1 
ATOM   1194 C C    B ALA   A 1 50  ? 22.846 6.199   3.142   0.28 9.78  ?  50  ALA   A C    1 
ATOM   1195 O O    A ALA   A 1 50  ? 23.404 6.598   4.175   0.72 10.37 ?  50  ALA   A O    1 
ATOM   1196 O O    B ALA   A 1 50  ? 23.509 6.631   4.092   0.28 9.99  ?  50  ALA   A O    1 
ATOM   1197 C CB   A ALA   A 1 50  ? 23.749 4.593   1.527   0.72 10.21 ?  50  ALA   A CB   1 
ATOM   1198 C CB   B ALA   A 1 50  ? 23.916 4.618   1.510   0.28 9.59  ?  50  ALA   A CB   1 
ATOM   1199 H H    A ALA   A 1 50  ? 21.427 3.898   1.699   0.72 11.98 ?  50  ALA   A H    1 
ATOM   1200 H H    B ALA   A 1 50  ? 21.567 3.950   1.566   0.28 10.95 ?  50  ALA   A H    1 
ATOM   1201 H HA   A ALA   A 1 50  ? 23.295 4.231   3.492   0.72 12.15 ?  50  ALA   A HA   1 
ATOM   1202 H HA   B ALA   A 1 50  ? 23.368 4.255   3.446   0.28 11.55 ?  50  ALA   A HA   1 
ATOM   1203 H HB1  A ALA   A 1 50  ? 24.624 4.973   1.715   0.72 12.26 ?  50  ALA   A HB1  1 
ATOM   1204 H HB1  B ALA   A 1 50  ? 24.772 5.015   1.738   0.28 11.52 ?  50  ALA   A HB1  1 
ATOM   1205 H HB2  A ALA   A 1 50  ? 23.839 3.657   1.297   0.72 12.26 ?  50  ALA   A HB2  1 
ATOM   1206 H HB2  B ALA   A 1 50  ? 24.034 3.679   1.296   0.28 11.52 ?  50  ALA   A HB2  1 
ATOM   1207 H HB3  A ALA   A 1 50  ? 23.333 5.077   0.795   0.72 12.26 ?  50  ALA   A HB3  1 
ATOM   1208 H HB3  B ALA   A 1 50  ? 23.528 5.084   0.752   0.28 11.52 ?  50  ALA   A HB3  1 
ATOM   1209 N N    . GLY   A 1 51  ? 22.008 6.975   2.455   1.00 10.19 ?  51  GLY   A N    1 
ATOM   1210 C CA   . GLY   A 1 51  ? 21.845 8.364   2.834   1.00 10.64 ?  51  GLY   A CA   1 
ATOM   1211 C C    . GLY   A 1 51  ? 21.246 8.507   4.217   1.00 10.59 ?  51  GLY   A C    1 
ATOM   1212 O O    . GLY   A 1 51  ? 21.635 9.393   4.983   1.00 11.16 ?  51  GLY   A O    1 
ATOM   1213 H H    A GLY   A 1 51  ? 21.584 6.735   1.742   0.72 12.24 ?  51  GLY   A H    1 
ATOM   1214 H H    B GLY   A 1 51  ? 21.541 6.722   1.775   0.28 12.24 ?  51  GLY   A H    1 
ATOM   1215 H HA2  . GLY   A 1 51  ? 22.706 8.807   2.822   1.00 12.77 ?  51  GLY   A HA2  1 
ATOM   1216 H HA3  . GLY   A 1 51  ? 21.261 8.808   2.198   1.00 12.77 ?  51  GLY   A HA3  1 
ATOM   1217 N N    . ALA   A 1 52  ? 20.289 7.636   4.554   1.00 10.77 ?  52  ALA   A N    1 
ATOM   1218 C CA   . ALA   A 1 52  ? 19.645 7.685   5.862   1.00 11.47 ?  52  ALA   A CA   1 
ATOM   1219 C C    . ALA   A 1 52  ? 20.605 7.279   6.979   1.00 10.78 ?  52  ALA   A C    1 
ATOM   1220 O O    . ALA   A 1 52  ? 20.684 7.948   8.016   1.00 11.85 ?  52  ALA   A O    1 
ATOM   1221 C CB   . ALA   A 1 52  ? 18.393 6.803   5.859   1.00 13.04 ?  52  ALA   A CB   1 
ATOM   1222 H H    . ALA   A 1 52  ? 20.008 6.996   4.044   1.00 12.92 ?  52  ALA   A H    1 
ATOM   1223 H HA   . ALA   A 1 52  ? 19.363 8.592   6.032   1.00 13.77 ?  52  ALA   A HA   1 
ATOM   1224 H HB1  . ALA   A 1 52  ? 17.969 6.852   6.731   1.00 15.65 ?  52  ALA   A HB1  1 
ATOM   1225 H HB2  . ALA   A 1 52  ? 17.780 7.125   5.178   1.00 15.65 ?  52  ALA   A HB2  1 
ATOM   1226 H HB3  . ALA   A 1 52  ? 18.646 5.886   5.667   1.00 15.65 ?  52  ALA   A HB3  1 
ATOM   1227 N N    A LEU   A 1 53  ? 21.330 6.173   6.803   0.72 10.73 ?  53  LEU   A N    1 
ATOM   1228 N N    B LEU   A 1 53  ? 21.351 6.185   6.779   0.28 10.45 ?  53  LEU   A N    1 
ATOM   1229 C CA   A LEU   A 1 53  ? 22.305 5.785   7.819   0.72 11.18 ?  53  LEU   A CA   1 
ATOM   1230 C CA   B LEU   A 1 53  ? 22.316 5.745   7.786   0.28 10.39 ?  53  LEU   A CA   1 
ATOM   1231 C C    A LEU   A 1 53  ? 23.337 6.886   8.012   0.72 10.57 ?  53  LEU   A C    1 
ATOM   1232 C C    B LEU   A 1 53  ? 23.409 6.786   7.996   0.28 10.03 ?  53  LEU   A C    1 
ATOM   1233 O O    A LEU   A 1 53  ? 23.624 7.299   9.142   0.72 11.28 ?  53  LEU   A O    1 
ATOM   1234 O O    B LEU   A 1 53  ? 23.834 7.032   9.130   0.28 9.94  ?  53  LEU   A O    1 
ATOM   1235 C CB   A LEU   A 1 53  ? 22.989 4.465   7.450   0.72 11.41 ?  53  LEU   A CB   1 
ATOM   1236 C CB   B LEU   A 1 53  ? 22.942 4.407   7.377   0.28 10.40 ?  53  LEU   A CB   1 
ATOM   1237 C CG   A LEU   A 1 53  ? 22.113 3.205   7.466   0.72 12.61 ?  53  LEU   A CG   1 
ATOM   1238 C CG   B LEU   A 1 53  ? 22.129 3.121   7.561   0.28 10.17 ?  53  LEU   A CG   1 
ATOM   1239 C CD1  A LEU   A 1 53  ? 22.907 2.014   6.964   0.72 12.74 ?  53  LEU   A CD1  1 
ATOM   1240 C CD1  B LEU   A 1 53  ? 22.773 1.973   6.797   0.28 10.61 ?  53  LEU   A CD1  1 
ATOM   1241 C CD2  A LEU   A 1 53  ? 21.552 2.928   8.857   0.72 13.50 ?  53  LEU   A CD2  1 
ATOM   1242 C CD2  B LEU   A 1 53  ? 22.001 2.757   9.030   0.28 9.46  ?  53  LEU   A CD2  1 
ATOM   1243 H H    A LEU   A 1 53  ? 21.282 5.645   6.121   0.72 12.88 ?  53  LEU   A H    1 
ATOM   1244 H H    B LEU   A 1 53  ? 21.321 5.689   6.075   0.28 12.54 ?  53  LEU   A H    1 
ATOM   1245 H HA   A LEU   A 1 53  ? 21.845 5.656   8.661   0.72 13.42 ?  53  LEU   A HA   1 
ATOM   1246 H HA   B LEU   A 1 53  ? 21.857 5.614   8.630   0.28 12.47 ?  53  LEU   A HA   1 
ATOM   1247 H HB2  A LEU   A 1 53  ? 23.348 4.546   6.553   0.72 13.69 ?  53  LEU   A HB2  1 
ATOM   1248 H HB2  B LEU   A 1 53  ? 23.166 4.459   6.436   0.28 12.49 ?  53  LEU   A HB2  1 
ATOM   1249 H HB3  A LEU   A 1 53  ? 23.714 4.311   8.074   0.72 13.69 ?  53  LEU   A HB3  1 
ATOM   1250 H HB3  B LEU   A 1 53  ? 23.756 4.291   7.890   0.28 12.49 ?  53  LEU   A HB3  1 
ATOM   1251 H HG   A LEU   A 1 53  ? 21.363 3.335   6.863   0.72 15.14 ?  53  LEU   A HG   1 
ATOM   1252 H HG   B LEU   A 1 53  ? 21.237 3.251   7.202   0.28 12.20 ?  53  LEU   A HG   1 
ATOM   1253 H HD11 A LEU   A 1 53  ? 22.335 1.226   6.980   0.72 15.29 ?  53  LEU   A HD11 1 
ATOM   1254 H HD11 B LEU   A 1 53  ? 22.246 1.169   6.933   0.28 12.73 ?  53  LEU   A HD11 1 
ATOM   1255 H HD12 A LEU   A 1 53  ? 23.198 2.189   6.057   0.72 15.29 ?  53  LEU   A HD12 1 
ATOM   1256 H HD12 B LEU   A 1 53  ? 22.799 2.196   5.855   0.28 12.73 ?  53  LEU   A HD12 1 
ATOM   1257 H HD13 A LEU   A 1 53  ? 23.671 1.878   7.542   0.72 15.29 ?  53  LEU   A HD13 1 
ATOM   1258 H HD13 B LEU   A 1 53  ? 23.673 1.838   7.132   0.28 12.73 ?  53  LEU   A HD13 1 
ATOM   1259 H HD21 A LEU   A 1 53  ? 21.084 2.077   8.846   0.72 16.21 ?  53  LEU   A HD21 1 
ATOM   1260 H HD21 B LEU   A 1 53  ? 21.463 1.952   9.110   0.28 11.36 ?  53  LEU   A HD21 1 
ATOM   1261 H HD22 A LEU   A 1 53  ? 22.281 2.896   9.492   0.72 16.21 ?  53  LEU   A HD22 1 
ATOM   1262 H HD22 B LEU   A 1 53  ? 22.885 2.601   9.393   0.28 11.36 ?  53  LEU   A HD22 1 
ATOM   1263 H HD23 A LEU   A 1 53  ? 20.934 3.638   9.096   0.72 16.21 ?  53  LEU   A HD23 1 
ATOM   1264 H HD23 B LEU   A 1 53  ? 21.572 3.489   9.497   0.28 11.36 ?  53  LEU   A HD23 1 
ATOM   1265 N N    . ASN   A 1 54  ? 23.888 7.396   6.914   1.00 10.27 ?  54  ASN   A N    1 
ATOM   1266 C CA   . ASN   A 1 54  ? 24.937 8.397   7.041   1.00 10.38 ?  54  ASN   A CA   1 
ATOM   1267 C C    . ASN   A 1 54  ? 24.426 9.644   7.764   1.00 10.40 ?  54  ASN   A C    1 
ATOM   1268 O O    . ASN   A 1 54  ? 25.115 10.198  8.633   1.00 10.93 ?  54  ASN   A O    1 
ATOM   1269 C CB   . ASN   A 1 54  ? 25.498 8.748   5.675   1.00 10.33 ?  54  ASN   A CB   1 
ATOM   1270 C CG   . ASN   A 1 54  ? 26.516 9.854   5.772   1.00 10.52 ?  54  ASN   A CG   1 
ATOM   1271 O OD1  . ASN   A 1 54  ? 27.522 9.717   6.480   1.00 10.73 ?  54  ASN   A OD1  1 
ATOM   1272 N ND2  . ASN   A 1 54  ? 26.252 10.972  5.118   1.00 11.66 ?  54  ASN   A ND2  1 
ATOM   1273 H H    A ASN   A 1 54  ? 23.673 7.183   6.107   0.72 12.32 ?  54  ASN   A H    1 
ATOM   1274 H H    B ASN   A 1 54  ? 23.618 7.249   6.109   0.28 12.32 ?  54  ASN   A H    1 
ATOM   1275 H HA   . ASN   A 1 54  ? 25.654 8.023   7.571   1.00 12.46 ?  54  ASN   A HA   1 
ATOM   1276 H HB2  . ASN   A 1 54  ? 25.935 7.959   5.300   1.00 12.40 ?  54  ASN   A HB2  1 
ATOM   1277 H HB3  . ASN   A 1 54  ? 24.780 9.035   5.094   1.00 12.40 ?  54  ASN   A HB3  1 
ATOM   1278 H HD21 . ASN   A 1 54  ? 26.801 11.631  5.156   1.00 14.00 ?  54  ASN   A HD21 1 
ATOM   1279 H HD22 . ASN   A 1 54  ? 25.533 11.035  4.650   1.00 14.00 ?  54  ASN   A HD22 1 
ATOM   1280 N N    A LYS   A 1 55  ? 23.217 10.098  7.415   0.72 11.01 ?  55  LYS   A N    1 
ATOM   1281 N N    B LYS   A 1 55  ? 23.212 10.092  7.427   0.28 10.85 ?  55  LYS   A N    1 
ATOM   1282 C CA   A LYS   A 1 55  ? 22.625 11.250  8.083   0.72 11.65 ?  55  LYS   A CA   1 
ATOM   1283 C CA   B LYS   A 1 55  ? 22.643 11.261  8.090   0.28 11.41 ?  55  LYS   A CA   1 
ATOM   1284 C C    A LYS   A 1 55  ? 22.547 11.017  9.586   0.72 11.73 ?  55  LYS   A C    1 
ATOM   1285 C C    B LYS   A 1 55  ? 22.512 11.030  9.591   0.28 11.67 ?  55  LYS   A C    1 
ATOM   1286 O O    A LYS   A 1 55  ? 22.854 11.915  10.379  0.72 12.65 ?  55  LYS   A O    1 
ATOM   1287 O O    B LYS   A 1 55  ? 22.741 11.945  10.391  0.28 12.01 ?  55  LYS   A O    1 
ATOM   1288 C CB   A LYS   A 1 55  ? 21.242 11.526  7.482   0.72 12.83 ?  55  LYS   A CB   1 
ATOM   1289 C CB   B LYS   A 1 55  ? 21.291 11.607  7.456   0.28 11.99 ?  55  LYS   A CB   1 
ATOM   1290 C CG   A LYS   A 1 55  ? 20.497 12.715  8.069   0.72 14.77 ?  55  LYS   A CG   1 
ATOM   1291 C CG   B LYS   A 1 55  ? 20.526 12.729  8.147   0.28 13.23 ?  55  LYS   A CG   1 
ATOM   1292 C CD   A LYS   A 1 55  ? 19.144 12.883  7.376   0.72 16.26 ?  55  LYS   A CD   1 
ATOM   1293 C CD   B LYS   A 1 55  ? 19.257 13.081  7.374   0.28 14.18 ?  55  LYS   A CD   1 
ATOM   1294 C CE   A LYS   A 1 55  ? 18.322 14.020  7.968   0.72 18.06 ?  55  LYS   A CE   1 
ATOM   1295 C CE   B LYS   A 1 55  ? 18.328 13.974  8.183   0.28 15.36 ?  55  LYS   A CE   1 
ATOM   1296 N NZ   A LYS   A 1 55  ? 16.963 14.080  7.354   0.72 18.88 ?  55  LYS   A NZ   1 
ATOM   1297 N NZ   B LYS   A 1 55  ? 17.056 14.254  7.457   0.28 15.93 ?  55  LYS   A NZ   1 
ATOM   1298 H H    A LYS   A 1 55  ? 22.717 9.749   6.803   0.72 13.22 ?  55  LYS   A H    1 
ATOM   1299 H H    B LYS   A 1 55  ? 22.702 9.738   6.828   0.28 13.02 ?  55  LYS   A H    1 
ATOM   1300 H HA   A LYS   A 1 55  ? 23.181 12.027  7.928   0.72 13.99 ?  55  LYS   A HA   1 
ATOM   1301 H HA   B LYS   A 1 55  ? 23.235 12.015  7.956   0.28 13.69 ?  55  LYS   A HA   1 
ATOM   1302 H HB2  A LYS   A 1 55  ? 21.345 11.693  6.533   0.72 15.40 ?  55  LYS   A HB2  1 
ATOM   1303 H HB2  B LYS   A 1 55  ? 21.442 11.883  6.538   0.28 14.40 ?  55  LYS   A HB2  1 
ATOM   1304 H HB3  A LYS   A 1 55  ? 20.684 10.743  7.615   0.72 15.40 ?  55  LYS   A HB3  1 
ATOM   1305 H HB3  B LYS   A 1 55  ? 20.728 10.819  7.471   0.28 14.40 ?  55  LYS   A HB3  1 
ATOM   1306 H HG2  A LYS   A 1 55  ? 20.338 12.565  9.015   0.72 17.73 ?  55  LYS   A HG2  1 
ATOM   1307 H HG2  B LYS   A 1 55  ? 20.267 12.444  9.037   0.28 15.88 ?  55  LYS   A HG2  1 
ATOM   1308 H HG3  A LYS   A 1 55  ? 21.014 13.522  7.934   0.72 17.73 ?  55  LYS   A HG3  1 
ATOM   1309 H HG3  B LYS   A 1 55  ? 21.084 13.520  8.195   0.28 15.88 ?  55  LYS   A HG3  1 
ATOM   1310 H HD2  A LYS   A 1 55  ? 19.293 13.073  6.437   0.72 19.52 ?  55  LYS   A HD2  1 
ATOM   1311 H HD2  B LYS   A 1 55  ? 19.502 13.553  6.562   0.28 17.02 ?  55  LYS   A HD2  1 
ATOM   1312 H HD3  A LYS   A 1 55  ? 18.635 12.061  7.472   0.72 19.52 ?  55  LYS   A HD3  1 
ATOM   1313 H HD3  B LYS   A 1 55  ? 18.782 12.264  7.155   0.28 17.02 ?  55  LYS   A HD3  1 
ATOM   1314 H HE2  A LYS   A 1 55  ? 18.223 13.879  8.923   0.72 21.68 ?  55  LYS   A HE2  1 
ATOM   1315 H HE2  B LYS   A 1 55  ? 18.109 13.531  9.018   0.28 18.44 ?  55  LYS   A HE2  1 
ATOM   1316 H HE3  A LYS   A 1 55  ? 18.775 14.862  7.799   0.72 21.68 ?  55  LYS   A HE3  1 
ATOM   1317 H HE3  B LYS   A 1 55  ? 18.770 14.819  8.358   0.28 18.44 ?  55  LYS   A HE3  1 
ATOM   1318 H HZ1  A LYS   A 1 55  ? 16.402 14.499  7.904   0.72 22.66 ?  55  LYS   A HZ1  1 
ATOM   1319 H HZ1  B LYS   A 1 55  ? 16.531 14.776  7.952   0.28 19.12 ?  55  LYS   A HZ1  1 
ATOM   1320 H HZ2  A LYS   A 1 55  ? 16.996 14.525  6.584   0.72 22.66 ?  55  LYS   A HZ2  1 
ATOM   1321 H HZ2  B LYS   A 1 55  ? 17.227 14.665  6.687   0.28 19.12 ?  55  LYS   A HZ2  1 
ATOM   1322 H HZ3  A LYS   A 1 55  ? 16.659 13.258  7.204   0.72 22.66 ?  55  LYS   A HZ3  1 
ATOM   1323 H HZ3  B LYS   A 1 55  ? 16.626 13.492  7.288   0.28 19.12 ?  55  LYS   A HZ3  1 
ATOM   1324 N N    . ALA   A 1 56  ? 22.149 9.808   9.995   1.00 11.86 ?  56  ALA   A N    1 
ATOM   1325 C CA   . ALA   A 1 56  ? 22.034 9.486   11.412  1.00 12.77 ?  56  ALA   A CA   1 
ATOM   1326 C C    . ALA   A 1 56  ? 23.376 9.518   12.135  1.00 12.44 ?  56  ALA   A C    1 
ATOM   1327 O O    . ALA   A 1 56  ? 23.398 9.706   13.354  1.00 13.87 ?  56  ALA   A O    1 
ATOM   1328 C CB   . ALA   A 1 56  ? 21.347 8.125   11.590  1.00 13.66 ?  56  ALA   A CB   1 
ATOM   1329 H H    A ALA   A 1 56  ? 21.945 9.162   9.466   0.72 14.24 ?  56  ALA   A H    1 
ATOM   1330 H H    B ALA   A 1 56  ? 21.965 9.157   9.465   0.28 14.24 ?  56  ALA   A H    1 
ATOM   1331 H HA   . ALA   A 1 56  ? 21.470 10.143  11.833  1.00 15.33 ?  56  ALA   A HA   1 
ATOM   1332 H HB1  . ALA   A 1 56  ? 21.279 7.924   12.538  1.00 16.40 ?  56  ALA   A HB1  1 
ATOM   1333 H HB2  . ALA   A 1 56  ? 20.461 8.164   11.197  1.00 16.40 ?  56  ALA   A HB2  1 
ATOM   1334 H HB3  . ALA   A 1 56  ? 21.873 7.438   11.147  1.00 16.40 ?  56  ALA   A HB3  1 
ATOM   1335 N N    . THR   A 1 57  ? 24.488 9.332   11.419  1.00 11.72 ?  57  THR   A N    1 
ATOM   1336 C CA   . THR   A 1 57  ? 25.827 9.456   11.995  1.00 11.72 ?  57  THR   A CA   1 
ATOM   1337 C C    . THR   A 1 57  ? 26.380 10.871  11.913  1.00 12.25 ?  57  THR   A C    1 
ATOM   1338 O O    . THR   A 1 57  ? 27.567 11.077  12.201  1.00 12.87 ?  57  THR   A O    1 
ATOM   1339 C CB   . THR   A 1 57  ? 26.837 8.505   11.326  1.00 11.94 ?  57  THR   A CB   1 
ATOM   1340 O OG1  . THR   A 1 57  ? 27.214 9.001   10.030  1.00 11.62 ?  57  THR   A OG1  1 
ATOM   1341 C CG2  . THR   A 1 57  ? 26.297 7.090   11.223  1.00 11.77 ?  57  THR   A CG2  1 
ATOM   1342 H H    . THR   A 1 57  ? 24.493 9.105   10.587  1.00 14.07 ?  57  THR   A H    1 
ATOM   1343 H HA   . THR   A 1 57  ? 25.780 9.203   12.935  1.00 14.07 ?  57  THR   A HA   1 
ATOM   1344 H HB   . THR   A 1 57  ? 27.636 8.462   11.884  1.00 14.33 ?  57  THR   A HB   1 
ATOM   1345 H HG1  . THR   A 1 57  ? 26.534 9.061   9.542   1.00 13.95 ?  57  THR   A HG1  1 
ATOM   1346 H HG21 . THR   A 1 57  ? 26.908 6.536   10.710  1.00 14.13 ?  57  THR   A HG21 1 
ATOM   1347 H HG22 . THR   A 1 57  ? 26.194 6.704   12.107  1.00 14.13 ?  57  THR   A HG22 1 
ATOM   1348 H HG23 . THR   A 1 57  ? 25.435 7.091   10.782  1.00 14.13 ?  57  THR   A HG23 1 
ATOM   1349 N N    . ASN   A 1 58  ? 25.566 11.847  11.512  1.00 12.78 ?  58  ASN   A N    1 
ATOM   1350 C CA   . ASN   A 1 58  ? 26.028 13.227  11.410  1.00 13.77 ?  58  ASN   A CA   1 
ATOM   1351 C C    . ASN   A 1 58  ? 27.181 13.345  10.407  1.00 12.88 ?  58  ASN   A C    1 
ATOM   1352 O O    . ASN   A 1 58  ? 28.078 14.173  10.566  1.00 13.34 ?  58  ASN   A O    1 
ATOM   1353 C CB   . ASN   A 1 58  ? 26.393 13.768  12.805  1.00 16.57 ?  58  ASN   A CB   1 
ATOM   1354 C CG   . ASN   A 1 58  ? 26.805 15.221  12.801  1.00 20.56 ?  58  ASN   A CG   1 
ATOM   1355 O OD1  . ASN   A 1 58  ? 26.182 16.044  12.140  1.00 22.41 ?  58  ASN   A OD1  1 
ATOM   1356 N ND2  . ASN   A 1 58  ? 27.857 15.550  13.557  1.00 21.95 ?  58  ASN   A ND2  1 
ATOM   1357 H H    . ASN   A 1 58  ? 24.741 11.727  11.283  1.00 15.34 ?  58  ASN   A H    1 
ATOM   1358 H HA   . ASN   A 1 58  ? 25.293 13.761  11.077  1.00 16.53 ?  58  ASN   A HA   1 
ATOM   1359 H HB2  . ASN   A 1 58  ? 25.616 13.678  13.391  1.00 19.89 ?  58  ASN   A HB2  1 
ATOM   1360 H HB3  . ASN   A 1 58  ? 27.129 13.257  13.167  1.00 19.89 ?  58  ASN   A HB3  1 
ATOM   1361 H HD21 . ASN   A 1 58  ? 28.125 16.369  13.590  1.00 26.34 ?  58  ASN   A HD21 1 
ATOM   1362 H HD22 . ASN   A 1 58  ? 28.261 14.947  14.010  1.00 26.34 ?  58  ASN   A HD22 1 
ATOM   1363 N N    . ASN   A 1 59  ? 27.155 12.530  9.349   1.00 11.62 ?  59  ASN   A N    1 
ATOM   1364 C CA   . ASN   A 1 59  ? 28.137 12.504  8.256   1.00 11.32 ?  59  ASN   A CA   1 
ATOM   1365 C C    . ASN   A 1 59  ? 29.453 11.822  8.644   1.00 11.15 ?  59  ASN   A C    1 
ATOM   1366 O O    . ASN   A 1 59  ? 30.377 11.785  7.821   1.00 11.32 ?  59  ASN   A O    1 
ATOM   1367 C CB   . ASN   A 1 59  ? 28.424 13.891  7.648   1.00 11.75 ?  59  ASN   A CB   1 
ATOM   1368 C CG   . ASN   A 1 59  ? 28.784 13.822  6.181   1.00 12.07 ?  59  ASN   A CG   1 
ATOM   1369 O OD1  . ASN   A 1 59  ? 28.075 13.202  5.383   1.00 12.09 ?  59  ASN   A OD1  1 
ATOM   1370 N ND2  . ASN   A 1 59  ? 29.877 14.477  5.809   1.00 12.74 ?  59  ASN   A ND2  1 
ATOM   1371 H H    . ASN   A 1 59  ? 26.534 11.947  9.230   1.00 13.95 ?  59  ASN   A H    1 
ATOM   1372 H HA   . ASN   A 1 59  ? 27.756 11.974  7.544   1.00 13.58 ?  59  ASN   A HA   1 
ATOM   1373 H HB2  . ASN   A 1 59  ? 27.634 14.450  7.731   1.00 14.10 ?  59  ASN   A HB2  1 
ATOM   1374 H HB3  . ASN   A 1 59  ? 29.168 14.301  8.116   1.00 14.10 ?  59  ASN   A HB3  1 
ATOM   1375 H HD21 . ASN   A 1 59  ? 30.128 14.470  4.987   1.00 15.30 ?  59  ASN   A HD21 1 
ATOM   1376 H HD22 . ASN   A 1 59  ? 30.351 14.900  6.396   1.00 15.30 ?  59  ASN   A HD22 1 
ATOM   1377 N N    . ALA   A 1 60  ? 29.577 11.278  9.854   1.00 11.18 ?  60  ALA   A N    1 
ATOM   1378 C CA   . ALA   A 1 60  ? 30.813 10.590  10.213  1.00 11.31 ?  60  ALA   A CA   1 
ATOM   1379 C C    . ALA   A 1 60  ? 31.033 9.355   9.349   1.00 11.19 ?  60  ALA   A C    1 
ATOM   1380 O O    . ALA   A 1 60  ? 32.176 9.029   9.018   1.00 11.62 ?  60  ALA   A O    1 
ATOM   1381 C CB   . ALA   A 1 60  ? 30.803 10.219  11.695  1.00 11.73 ?  60  ALA   A CB   1 
ATOM   1382 H H    . ALA   A 1 60  ? 28.976 11.288  10.471  1.00 13.42 ?  60  ALA   A H    1 
ATOM   1383 H HA   . ALA   A 1 60  ? 31.559 11.193  10.065  1.00 13.58 ?  60  ALA   A HA   1 
ATOM   1384 H HB1  . ALA   A 1 60  ? 31.632 9.766   11.915  1.00 14.08 ?  60  ALA   A HB1  1 
ATOM   1385 H HB2  . ALA   A 1 60  ? 30.722 11.032  12.223  1.00 14.08 ?  60  ALA   A HB2  1 
ATOM   1386 H HB3  . ALA   A 1 60  ? 30.049 9.636   11.871  1.00 14.08 ?  60  ALA   A HB3  1 
ATOM   1387 N N    . MET   A 1 61  ? 29.960 8.667   8.961   1.00 10.77 ?  61  MET   A N    1 
ATOM   1388 C CA   . MET   A 1 61  ? 30.096 7.526   8.060   1.00 10.77 ?  61  MET   A CA   1 
ATOM   1389 C C    . MET   A 1 61  ? 30.736 7.947   6.738   1.00 10.48 ?  61  MET   A C    1 
ATOM   1390 O O    . MET   A 1 61  ? 31.622 7.259   6.217   1.00 10.99 ?  61  MET   A O    1 
ATOM   1391 C CB   . MET   A 1 61  ? 28.733 6.867   7.838   1.00 10.72 ?  61  MET   A CB   1 
ATOM   1392 C CG   . MET   A 1 61  ? 28.751 5.694   6.868   1.00 11.13 ?  61  MET   A CG   1 
ATOM   1393 S SD   . MET   A 1 61  ? 27.121 4.947   6.660   1.00 12.30 ?  61  MET   A SD   1 
ATOM   1394 C CE   . MET   A 1 61  ? 26.991 4.038   8.206   1.00 13.88 ?  61  MET   A CE   1 
ATOM   1395 H H    . MET   A 1 61  ? 29.151 8.841   9.200   1.00 12.93 ?  61  MET   A H    1 
ATOM   1396 H HA   . MET   A 1 61  ? 30.670 6.869   8.483   1.00 12.93 ?  61  MET   A HA   1 
ATOM   1397 H HB2  . MET   A 1 61  ? 28.405 6.541   8.691   1.00 12.86 ?  61  MET   A HB2  1 
ATOM   1398 H HB3  . MET   A 1 61  ? 28.121 7.532   7.487   1.00 12.86 ?  61  MET   A HB3  1 
ATOM   1399 H HG2  . MET   A 1 61  ? 29.039 5.997   5.995   1.00 13.37 ?  61  MET   A HG2  1 
ATOM   1400 H HG3  . MET   A 1 61  ? 29.346 5.008   7.201   1.00 13.37 ?  61  MET   A HG3  1 
ATOM   1401 H HE1  . MET   A 1 61  ? 26.150 3.553   8.222   1.00 16.67 ?  61  MET   A HE1  1 
ATOM   1402 H HE2  . MET   A 1 61  ? 27.732 3.413   8.267   1.00 16.67 ?  61  MET   A HE2  1 
ATOM   1403 H HE3  . MET   A 1 61  ? 27.026 4.663   8.948   1.00 16.67 ?  61  MET   A HE3  1 
ATOM   1404 N N    . GLN   A 1 62  ? 30.290 9.075   6.176   1.00 10.47 ?  62  GLN   A N    1 
ATOM   1405 C CA   . GLN   A 1 62  ? 30.854 9.555   4.918   1.00 10.85 ?  62  GLN   A CA   1 
ATOM   1406 C C    . GLN   A 1 62  ? 32.325 9.927   5.067   1.00 10.95 ?  62  GLN   A C    1 
ATOM   1407 O O    . GLN   A 1 62  ? 33.136 9.614   4.188   1.00 11.14 ?  62  GLN   A O    1 
ATOM   1408 C CB   . GLN   A 1 62  ? 30.053 10.739  4.383   1.00 10.80 ?  62  GLN   A CB   1 
ATOM   1409 C CG   . GLN   A 1 62  ? 30.441 11.102  2.959   1.00 10.93 ?  62  GLN   A CG   1 
ATOM   1410 C CD   . GLN   A 1 62  ? 30.105 9.974   2.006   1.00 11.07 ?  62  GLN   A CD   1 
ATOM   1411 O OE1  . GLN   A 1 62  ? 28.922 9.671   1.793   1.00 11.74 ?  62  GLN   A OE1  1 
ATOM   1412 N NE2  . GLN   A 1 62  ? 31.124 9.303   1.479   1.00 11.60 ?  62  GLN   A NE2  1 
ATOM   1413 H H    . GLN   A 1 62  ? 29.665 9.567   6.502   1.00 12.57 ?  62  GLN   A H    1 
ATOM   1414 H HA   . GLN   A 1 62  ? 30.800 8.836   4.270   1.00 13.03 ?  62  GLN   A HA   1 
ATOM   1415 H HB2  . GLN   A 1 62  ? 29.110 10.512  4.392   1.00 12.97 ?  62  GLN   A HB2  1 
ATOM   1416 H HB3  . GLN   A 1 62  ? 30.215 11.510  4.948   1.00 12.97 ?  62  GLN   A HB3  1 
ATOM   1417 H HG2  . GLN   A 1 62  ? 29.945 11.886  2.687   1.00 13.12 ?  62  GLN   A HG2  1 
ATOM   1418 H HG3  . GLN   A 1 62  ? 31.394 11.268  2.918   1.00 13.12 ?  62  GLN   A HG3  1 
ATOM   1419 H HE21 . GLN   A 1 62  ? 31.933 9.533   1.667   1.00 13.92 ?  62  GLN   A HE21 1 
ATOM   1420 H HE22 . GLN   A 1 62  ? 30.977 8.651   0.941   1.00 13.92 ?  62  GLN   A HE22 1 
ATOM   1421 N N    . VAL   A 1 63  ? 32.690 10.607  6.161   1.00 11.59 ?  63  VAL   A N    1 
ATOM   1422 C CA   . VAL   A 1 63  ? 34.086 11.000  6.372   1.00 12.17 ?  63  VAL   A CA   1 
ATOM   1423 C C    . VAL   A 1 63  ? 34.983 9.764   6.431   1.00 11.65 ?  63  VAL   A C    1 
ATOM   1424 O O    . VAL   A 1 63  ? 36.039 9.697   5.781   1.00 12.15 ?  63  VAL   A O    1 
ATOM   1425 C CB   . VAL   A 1 63  ? 34.197 11.876  7.635   1.00 13.71 ?  63  VAL   A CB   1 
ATOM   1426 C CG1  . VAL   A 1 63  ? 35.645 12.127  7.993   1.00 15.71 ?  63  VAL   A CG1  1 
ATOM   1427 C CG2  . VAL   A 1 63  ? 33.459 13.196  7.430   1.00 14.06 ?  63  VAL   A CG2  1 
ATOM   1428 H H    . VAL   A 1 63  ? 32.148 10.848  6.790   1.00 13.91 ?  63  VAL   A H    1 
ATOM   1429 H HA   . VAL   A 1 63  ? 34.367 11.534  5.619   1.00 14.61 ?  63  VAL   A HA   1 
ATOM   1430 H HB   . VAL   A 1 63  ? 33.782 11.413  8.381   1.00 16.45 ?  63  VAL   A HB   1 
ATOM   1431 H HG11 . VAL   A 1 63  ? 35.689 12.859  8.626   1.00 18.85 ?  63  VAL   A HG11 1 
ATOM   1432 H HG12 . VAL   A 1 63  ? 36.019 11.324  8.386   1.00 18.85 ?  63  VAL   A HG12 1 
ATOM   1433 H HG13 . VAL   A 1 63  ? 36.130 12.360  7.185   1.00 18.85 ?  63  VAL   A HG13 1 
ATOM   1434 H HG21 . VAL   A 1 63  ? 33.551 13.737  8.229   1.00 16.87 ?  63  VAL   A HG21 1 
ATOM   1435 H HG22 . VAL   A 1 63  ? 33.845 13.657  6.670   1.00 16.87 ?  63  VAL   A HG22 1 
ATOM   1436 H HG23 . VAL   A 1 63  ? 32.521 13.010  7.263   1.00 16.87 ?  63  VAL   A HG23 1 
ATOM   1437 N N    . GLU   A 1 64  ? 34.563 8.758   7.202   1.00 11.57 ?  64  GLU   A N    1 
ATOM   1438 C CA   . GLU   A 1 64  ? 35.321 7.515   7.292   1.00 11.50 ?  64  GLU   A CA   1 
ATOM   1439 C C    . GLU   A 1 64  ? 35.407 6.828   5.934   1.00 11.21 ?  64  GLU   A C    1 
ATOM   1440 O O    . GLU   A 1 64  ? 36.455 6.282   5.555   1.00 11.71 ?  64  GLU   A O    1 
ATOM   1441 C CB   . GLU   A 1 64  ? 34.629 6.605   8.306   1.00 12.07 ?  64  GLU   A CB   1 
ATOM   1442 C CG   . GLU   A 1 64  ? 35.283 5.260   8.465   1.00 12.54 ?  64  GLU   A CG   1 
ATOM   1443 C CD   . GLU   A 1 64  ? 34.402 4.264   9.193   1.00 13.31 ?  64  GLU   A CD   1 
ATOM   1444 O OE1  . GLU   A 1 64  ? 33.164 4.355   9.054   1.00 13.83 ?  64  GLU   A OE1  1 
ATOM   1445 O OE2  . GLU   A 1 64  ? 34.950 3.371   9.882   1.00 13.85 -1 64  GLU   A OE2  1 
ATOM   1446 H H    . GLU   A 1 64  ? 33.838 8.765   7.667   1.00 13.89 ?  64  GLU   A H    1 
ATOM   1447 H HA   . GLU   A 1 64  ? 36.218 7.708   7.608   1.00 13.80 ?  64  GLU   A HA   1 
ATOM   1448 H HB2  . GLU   A 1 64  ? 34.639 7.045   9.177   1.00 14.49 ?  64  GLU   A HB2  1 
ATOM   1449 H HB3  . GLU   A 1 64  ? 33.712 6.467   8.025   1.00 14.49 ?  64  GLU   A HB3  1 
ATOM   1450 H HG2  . GLU   A 1 64  ? 35.489 4.893   7.589   1.00 15.06 ?  64  GLU   A HG2  1 
ATOM   1451 H HG3  . GLU   A 1 64  ? 36.101 5.368   8.974   1.00 15.06 ?  64  GLU   A HG3  1 
ATOM   1452 N N    . SER   A 1 65  ? 34.291 6.824   5.200   1.00 10.93 ?  65  SER   A N    1 
ATOM   1453 C CA   . SER   A 1 65  ? 34.238 6.165   3.899   1.00 10.81 ?  65  SER   A CA   1 
ATOM   1454 C C    . SER   A 1 65  ? 35.161 6.835   2.890   1.00 11.27 ?  65  SER   A C    1 
ATOM   1455 O O    . SER   A 1 65  ? 35.801 6.153   2.080   1.00 11.94 ?  65  SER   A O    1 
ATOM   1456 C CB   . SER   A 1 65  ? 32.802 6.175   3.371   1.00 11.07 ?  65  SER   A CB   1 
ATOM   1457 O OG   . SER   A 1 65  ? 31.950 5.360   4.164   1.00 11.45 ?  65  SER   A OG   1 
ATOM   1458 H H    . SER   A 1 65  ? 33.556 7.201   5.434   1.00 13.12 ?  65  SER   A H    1 
ATOM   1459 H HA   . SER   A 1 65  ? 34.520 5.245   3.995   1.00 12.98 ?  65  SER   A HA   1 
ATOM   1460 H HB2  . SER   A 1 65  ? 32.465 7.082   3.383   1.00 13.28 ?  65  SER   A HB2  1 
ATOM   1461 H HB3  . SER   A 1 65  ? 32.803 5.835   2.462   1.00 13.28 ?  65  SER   A HB3  1 
ATOM   1462 H HG   . SER   A 1 65  ? 31.943 5.641   4.959   1.00 13.74 ?  65  SER   A HG   1 
ATOM   1463 N N    . ASP   A 1 66  ? 35.240 8.170   2.913   1.00 11.25 ?  66  ASP   A N    1 
ATOM   1464 C CA   . ASP   A 1 66  ? 36.102 8.868   1.966   1.00 11.96 ?  66  ASP   A CA   1 
ATOM   1465 C C    . ASP   A 1 66  ? 37.563 8.506   2.200   1.00 12.22 ?  66  ASP   A C    1 
ATOM   1466 O O    . ASP   A 1 66  ? 38.334 8.331   1.247   1.00 13.08 ?  66  ASP   A O    1 
ATOM   1467 C CB   . ASP   A 1 66  ? 35.885 10.375  2.081   1.00 13.21 ?  66  ASP   A CB   1 
ATOM   1468 C CG   . ASP   A 1 66  ? 34.548 10.837  1.481   1.00 15.21 ?  66  ASP   A CG   1 
ATOM   1469 O OD1  . ASP   A 1 66  ? 33.830 10.044  0.833   1.00 15.34 ?  66  ASP   A OD1  1 
ATOM   1470 O OD2  . ASP   A 1 66  ? 34.244 12.036  1.629   1.00 18.36 -1 66  ASP   A OD2  1 
ATOM   1471 H H    . ASP   A 1 66  ? 34.803 8.685   3.453   1.00 13.51 ?  66  ASP   A H    1 
ATOM   1472 H HA   . ASP   A 1 66  ? 35.863 8.602   1.068   1.00 14.36 ?  66  ASP   A HA   1 
ATOM   1473 H HB2  . ASP   A 1 66  ? 35.896 10.630  3.018   1.00 15.85 ?  66  ASP   A HB2  1 
ATOM   1474 H HB3  . ASP   A 1 66  ? 36.603 10.834  1.609   1.00 15.85 ?  66  ASP   A HB3  1 
ATOM   1475 N N    . ASP   A 1 67  ? 37.963 8.375   3.464   1.00 12.36 ?  67  ASP   A N    1 
ATOM   1476 C CA   . ASP   A 1 67  ? 39.315 7.918   3.762   1.00 13.35 ?  67  ASP   A CA   1 
ATOM   1477 C C    . ASP   A 1 67  ? 39.532 6.481   3.291   1.00 12.91 ?  67  ASP   A C    1 
ATOM   1478 O O    . ASP   A 1 67  ? 40.592 6.156   2.743   1.00 13.54 ?  67  ASP   A O    1 
ATOM   1479 C CB   . ASP   A 1 67  ? 39.589 8.055   5.258   1.00 14.57 ?  67  ASP   A CB   1 
ATOM   1480 C CG   . ASP   A 1 67  ? 40.884 7.392   5.677   1.00 15.70 ?  67  ASP   A CG   1 
ATOM   1481 O OD1  . ASP   A 1 67  ? 41.964 8.012   5.526   1.00 18.62 ?  67  ASP   A OD1  1 
ATOM   1482 O OD2  . ASP   A 1 67  ? 40.824 6.237   6.156   1.00 15.40 -1 67  ASP   A OD2  1 
ATOM   1483 H H    . ASP   A 1 67  ? 37.480 8.538   4.152   1.00 14.84 ?  67  ASP   A H    1 
ATOM   1484 H HA   . ASP   A 1 67  ? 39.949 8.477   3.287   1.00 16.03 ?  67  ASP   A HA   1 
ATOM   1485 H HB2  . ASP   A 1 67  ? 39.651 8.993   5.479   1.00 17.49 ?  67  ASP   A HB2  1 
ATOM   1486 H HB3  . ASP   A 1 67  ? 38.865 7.637   5.749   1.00 17.49 ?  67  ASP   A HB3  1 
ATOM   1487 N N    . TYR   A 1 68  ? 38.542 5.601   3.493   1.00 12.71 ?  68  TYR   A N    1 
ATOM   1488 C CA   . TYR   A 1 68  ? 38.652 4.223   3.011   1.00 12.68 ?  68  TYR   A CA   1 
ATOM   1489 C C    . TYR   A 1 68  ? 38.890 4.181   1.502   1.00 12.30 ?  68  TYR   A C    1 
ATOM   1490 O O    . TYR   A 1 68  ? 39.768 3.449   1.021   1.00 12.88 ?  68  TYR   A O    1 
ATOM   1491 C CB   . TYR   A 1 68  ? 37.398 3.410   3.380   1.00 13.04 ?  68  TYR   A CB   1 
ATOM   1492 C CG   . TYR   A 1 68  ? 37.427 2.025   2.752   1.00 14.71 ?  68  TYR   A CG   1 
ATOM   1493 C CD1  . TYR   A 1 68  ? 36.968 1.829   1.453   1.00 16.16 ?  68  TYR   A CD1  1 
ATOM   1494 C CD2  . TYR   A 1 68  ? 37.963 0.938   3.423   1.00 16.62 ?  68  TYR   A CD2  1 
ATOM   1495 C CE1  . TYR   A 1 68  ? 37.031 0.603   0.841   1.00 17.53 ?  68  TYR   A CE1  1 
ATOM   1496 C CE2  . TYR   A 1 68  ? 38.027 -0.322  2.811   1.00 17.21 ?  68  TYR   A CE2  1 
ATOM   1497 C CZ   . TYR   A 1 68  ? 37.565 -0.466  1.521   1.00 17.87 ?  68  TYR   A CZ   1 
ATOM   1498 O OH   . TYR   A 1 68  ? 37.644 -1.684  0.900   1.00 18.77 ?  68  TYR   A OH   1 
ATOM   1499 H H    . TYR   A 1 68  ? 37.804 5.775   3.902   1.00 15.25 ?  68  TYR   A H    1 
ATOM   1500 H HA   . TYR   A 1 68  ? 39.410 3.802   3.442   1.00 15.22 ?  68  TYR   A HA   1 
ATOM   1501 H HB2  . TYR   A 1 68  ? 37.357 3.301   4.342   1.00 15.65 ?  68  TYR   A HB2  1 
ATOM   1502 H HB3  . TYR   A 1 68  ? 36.608 3.872   3.059   1.00 15.65 ?  68  TYR   A HB3  1 
ATOM   1503 H HD1  . TYR   A 1 68  ? 36.616 2.554   0.983   1.00 19.40 ?  68  TYR   A HD1  1 
ATOM   1504 H HD2  . TYR   A 1 68  ? 38.292 1.045   4.281   1.00 19.95 ?  68  TYR   A HD2  1 
ATOM   1505 H HE1  . TYR   A 1 68  ? 36.710 0.501   -0.027  1.00 21.04 ?  68  TYR   A HE1  1 
ATOM   1506 H HE2  . TYR   A 1 68  ? 38.389 -1.048  3.257   1.00 20.66 ?  68  TYR   A HE2  1 
ATOM   1507 H HH   . TYR   A 1 68  ? 37.974 -2.248  1.430   1.00 22.53 ?  68  TYR   A HH   1 
ATOM   1508 N N    . ILE   A 1 69  ? 38.110 4.952   0.734   1.00 12.04 ?  69  ILE   A N    1 
ATOM   1509 C CA   . ILE   A 1 69  ? 38.249 4.941   -0.722  1.00 11.96 ?  69  ILE   A CA   1 
ATOM   1510 C C    . ILE   A 1 69  ? 39.585 5.544   -1.152  1.00 12.27 ?  69  ILE   A C    1 
ATOM   1511 O O    . ILE   A 1 69  ? 40.230 5.059   -2.090  1.00 12.61 ?  69  ILE   A O    1 
ATOM   1512 C CB   . ILE   A 1 69  ? 37.052 5.654   -1.384  1.00 13.35 ?  69  ILE   A CB   1 
ATOM   1513 C CG1  . ILE   A 1 69  ? 35.740 4.920   -1.101  1.00 13.39 ?  69  ILE   A CG1  1 
ATOM   1514 C CG2  . ILE   A 1 69  ? 37.285 5.838   -2.892  1.00 14.71 ?  69  ILE   A CG2  1 
ATOM   1515 C CD1  . ILE   A 1 69  ? 35.568 3.625   -1.872  1.00 14.18 ?  69  ILE   A CD1  1 
ATOM   1516 H H    . ILE   A 1 69  ? 37.508 5.486   1.032   1.00 14.45 ?  69  ILE   A H    1 
ATOM   1517 H HA   . ILE   A 1 69  ? 38.242 4.019   -1.020  1.00 14.36 ?  69  ILE   A HA   1 
ATOM   1518 H HB   . ILE   A 1 69  ? 36.982 6.535   -0.990  1.00 16.03 ?  69  ILE   A HB   1 
ATOM   1519 H HG12 . ILE   A 1 69  ? 35.704 4.703   -0.155  1.00 16.07 ?  69  ILE   A HG12 1 
ATOM   1520 H HG13 . ILE   A 1 69  ? 35.003 5.502   -1.331  1.00 16.07 ?  69  ILE   A HG13 1 
ATOM   1521 H HG21 . ILE   A 1 69  ? 36.440 6.058   -3.317  1.00 17.65 ?  69  ILE   A HG21 1 
ATOM   1522 H HG22 . ILE   A 1 69  ? 37.916 6.568   -3.028  1.00 17.65 ?  69  ILE   A HG22 1 
ATOM   1523 H HG23 . ILE   A 1 69  ? 37.640 5.020   -3.264  1.00 17.65 ?  69  ILE   A HG23 1 
ATOM   1524 H HD11 . ILE   A 1 69  ? 34.770 3.177   -1.552  1.00 17.02 ?  69  ILE   A HD11 1 
ATOM   1525 H HD12 . ILE   A 1 69  ? 35.473 3.832   -2.816  1.00 17.02 ?  69  ILE   A HD12 1 
ATOM   1526 H HD13 . ILE   A 1 69  ? 36.343 3.064   -1.730  1.00 17.02 ?  69  ILE   A HD13 1 
ATOM   1527 N N    . ALA   A 1 70  ? 40.008 6.625   -0.498  1.00 12.88 ?  70  ALA   A N    1 
ATOM   1528 C CA   . ALA   A 1 70  ? 41.288 7.229   -0.848  1.00 13.61 ?  70  ALA   A CA   1 
ATOM   1529 C C    . ALA   A 1 70  ? 42.436 6.244   -0.674  1.00 13.93 ?  70  ALA   A C    1 
ATOM   1530 O O    . ALA   A 1 70  ? 43.407 6.282   -1.434  1.00 15.83 ?  70  ALA   A O    1 
ATOM   1531 C CB   . ALA   A 1 70  ? 41.529 8.484   -0.005  1.00 14.52 ?  70  ALA   A CB   1 
ATOM   1532 H H    . ALA   A 1 70  ? 39.579 7.021   0.136   1.00 15.46 ?  70  ALA   A H    1 
ATOM   1533 H HA   . ALA   A 1 70  ? 41.261 7.504   -1.779  1.00 16.33 ?  70  ALA   A HA   1 
ATOM   1534 H HB1  . ALA   A 1 70  ? 42.389 8.868   -0.252  1.00 17.43 ?  70  ALA   A HB1  1 
ATOM   1535 H HB2  . ALA   A 1 70  ? 40.823 9.123   -0.169  1.00 17.43 ?  70  ALA   A HB2  1 
ATOM   1536 H HB3  . ALA   A 1 70  ? 41.543 8.235   0.934   1.00 17.43 ?  70  ALA   A HB3  1 
ATOM   1537 N N    . THR   A 1 71  ? 42.336 5.350   0.309   1.00 13.33 ?  71  THR   A N    1 
ATOM   1538 C CA   . THR   A 1 71  ? 43.384 4.368   0.559   1.00 14.77 ?  71  THR   A CA   1 
ATOM   1539 C C    . THR   A 1 71  ? 43.263 3.147   -0.344  1.00 14.92 ?  71  THR   A C    1 
ATOM   1540 O O    . THR   A 1 71  ? 44.277 2.639   -0.842  1.00 17.10 ?  71  THR   A O    1 
ATOM   1541 C CB   . THR   A 1 71  ? 43.310 3.917   2.014   1.00 16.63 ?  71  THR   A CB   1 
ATOM   1542 O OG1  . THR   A 1 71  ? 43.562 5.038   2.865   1.00 17.96 ?  71  THR   A OG1  1 
ATOM   1543 C CG2  . THR   A 1 71  ? 44.323 2.817   2.301   1.00 18.15 ?  71  THR   A CG2  1 
ATOM   1544 H H    . THR   A 1 71  ? 41.663 5.287   0.836   1.00 16.00 ?  71  THR   A H    1 
ATOM   1545 H HA   . THR   A 1 71  ? 44.249 4.773   0.401   1.00 17.73 ?  71  THR   A HA   1 
ATOM   1546 H HB   . THR   A 1 71  ? 42.419 3.556   2.183   1.00 19.97 ?  71  THR   A HB   1 
ATOM   1547 H HG1  . THR   A 1 71  ? 43.499 4.793   3.666   1.00 21.55 ?  71  THR   A HG1  1 
ATOM   1548 H HG21 . THR   A 1 71  ? 44.450 2.733   3.258   1.00 21.78 ?  71  THR   A HG21 1 
ATOM   1549 H HG22 . THR   A 1 71  ? 44.017 1.968   1.948   1.00 21.78 ?  71  THR   A HG22 1 
ATOM   1550 H HG23 . THR   A 1 71  ? 45.176 3.041   1.892   1.00 21.78 ?  71  THR   A HG23 1 
ATOM   1551 N N    . ASN   A 1 72  ? 42.042 2.636   -0.531  1.00 14.22 ?  72  ASN   A N    1 
ATOM   1552 C CA   . ASN   A 1 72  ? 41.821 1.311   -1.098  1.00 14.31 ?  72  ASN   A CA   1 
ATOM   1553 C C    . ASN   A 1 72  ? 41.200 1.302   -2.483  1.00 14.32 ?  72  ASN   A C    1 
ATOM   1554 O O    . ASN   A 1 72  ? 41.205 0.247   -3.129  1.00 15.13 ?  72  ASN   A O    1 
ATOM   1555 C CB   . ASN   A 1 72  ? 40.927 0.488   -0.163  1.00 15.02 ?  72  ASN   A CB   1 
ATOM   1556 C CG   . ASN   A 1 72  ? 41.535 0.330   1.205   1.00 15.98 ?  72  ASN   A CG   1 
ATOM   1557 O OD1  . ASN   A 1 72  ? 41.088 0.940   2.174   1.00 18.02 ?  72  ASN   A OD1  1 
ATOM   1558 N ND2  . ASN   A 1 72  ? 42.580 -0.462  1.288   1.00 16.42 ?  72  ASN   A ND2  1 
ATOM   1559 H H    . ASN   A 1 72  ? 41.312 3.050   -0.336  1.00 17.07 ?  72  ASN   A H    1 
ATOM   1560 H HA   . ASN   A 1 72  ? 42.675 0.859   -1.164  1.00 17.18 ?  72  ASN   A HA   1 
ATOM   1561 H HB2  . ASN   A 1 72  ? 40.073 0.930   -0.067  1.00 18.03 ?  72  ASN   A HB2  1 
ATOM   1562 H HB3  . ASN   A 1 72  ? 40.807 -0.399  -0.540  1.00 18.03 ?  72  ASN   A HB3  1 
ATOM   1563 H HD21 . ASN   A 1 72  ? 42.970 -0.581  2.048   1.00 19.71 ?  72  ASN   A HD21 1 
ATOM   1564 H HD22 . ASN   A 1 72  ? 42.876 -0.865  0.589   1.00 19.71 ?  72  ASN   A HD22 1 
ATOM   1565 N N    . GLY   A 1 73  ? 40.652 2.415   -2.948  1.00 14.12 ?  73  GLY   A N    1 
ATOM   1566 C CA   . GLY   A 1 73  ? 39.919 2.422   -4.188  1.00 13.84 ?  73  GLY   A CA   1 
ATOM   1567 C C    . GLY   A 1 73  ? 38.522 1.849   -4.019  1.00 13.41 ?  73  GLY   A C    1 
ATOM   1568 O O    . GLY   A 1 73  ? 38.130 1.392   -2.937  1.00 13.85 ?  73  GLY   A O    1 
ATOM   1569 H H    . GLY   A 1 73  ? 40.698 3.189   -2.566  1.00 16.95 ?  73  GLY   A H    1 
ATOM   1570 H HA2  . GLY   A 1 73  ? 39.846 3.334   -4.517  1.00 16.61 ?  73  GLY   A HA2  1 
ATOM   1571 H HA3  . GLY   A 1 73  ? 40.395 1.896   -4.852  1.00 16.61 ?  73  GLY   A HA3  1 
ATOM   1572 N N    . PRO   A 1 74  ? 37.742 1.872   -5.098  1.00 13.72 ?  74  PRO   A N    1 
ATOM   1573 C CA   . PRO   A 1 74  ? 36.343 1.439   -5.018  1.00 13.72 ?  74  PRO   A CA   1 
ATOM   1574 C C    . PRO   A 1 74  ? 36.191 -0.044  -4.702  1.00 12.75 ?  74  PRO   A C    1 
ATOM   1575 O O    . PRO   A 1 74  ? 37.061 -0.873  -4.989  1.00 13.57 ?  74  PRO   A O    1 
ATOM   1576 C CB   . PRO   A 1 74  ? 35.803 1.743   -6.422  1.00 15.27 ?  74  PRO   A CB   1 
ATOM   1577 C CG   . PRO   A 1 74  ? 36.756 2.716   -7.023  1.00 18.01 ?  74  PRO   A CG   1 
ATOM   1578 C CD   . PRO   A 1 74  ? 38.090 2.372   -6.439  1.00 15.32 ?  74  PRO   A CD   1 
ATOM   1579 H HA   . PRO   A 1 74  ? 35.863 1.970   -4.360  1.00 16.47 ?  74  PRO   A HA   1 
ATOM   1580 H HB2  . PRO   A 1 74  ? 35.773 0.922   -6.937  1.00 18.33 ?  74  PRO   A HB2  1 
ATOM   1581 H HB3  . PRO   A 1 74  ? 34.916 2.132   -6.347  1.00 18.33 ?  74  PRO   A HB3  1 
ATOM   1582 H HG2  . PRO   A 1 74  ? 36.771 2.611   -7.987  1.00 21.62 ?  74  PRO   A HG2  1 
ATOM   1583 H HG3  . PRO   A 1 74  ? 36.505 3.620   -6.780  1.00 21.62 ?  74  PRO   A HG3  1 
ATOM   1584 H HD2  . PRO   A 1 74  ? 38.526 1.677   -6.963  1.00 18.38 ?  74  PRO   A HD2  1 
ATOM   1585 H HD3  . PRO   A 1 74  ? 38.648 3.169   -6.383  1.00 18.38 ?  74  PRO   A HD3  1 
ATOM   1586 N N    . LEU   A 1 75  ? 35.045 -0.370  -4.113  1.00 12.11 ?  75  LEU   A N    1 
ATOM   1587 C CA   . LEU   A 1 75  ? 34.647 -1.760  -3.964  1.00 11.71 ?  75  LEU   A CA   1 
ATOM   1588 C C    . LEU   A 1 75  ? 34.254 -2.332  -5.323  1.00 12.34 ?  75  LEU   A C    1 
ATOM   1589 O O    . LEU   A 1 75  ? 34.133 -1.614  -6.320  1.00 13.82 ?  75  LEU   A O    1 
ATOM   1590 C CB   . LEU   A 1 75  ? 33.460 -1.874  -3.008  1.00 11.65 ?  75  LEU   A CB   1 
ATOM   1591 C CG   . LEU   A 1 75  ? 33.667 -1.449  -1.556  1.00 13.40 ?  75  LEU   A CG   1 
ATOM   1592 C CD1  . LEU   A 1 75  ? 32.382 -1.643  -0.751  1.00 15.36 ?  75  LEU   A CD1  1 
ATOM   1593 C CD2  . LEU   A 1 75  ? 34.820 -2.149  -0.893  1.00 16.84 ?  75  LEU   A CD2  1 
ATOM   1594 H H    . LEU   A 1 75  ? 34.481 0.200   -3.799  1.00 14.54 ?  75  LEU   A H    1 
ATOM   1595 H HA   . LEU   A 1 75  ? 35.387 -2.272  -3.612  1.00 14.06 ?  75  LEU   A HA   1 
ATOM   1596 H HB2  . LEU   A 1 75  ? 32.738 -1.334  -3.360  1.00 13.99 ?  75  LEU   A HB2  1 
ATOM   1597 H HB3  . LEU   A 1 75  ? 33.184 -2.804  -2.991  1.00 13.99 ?  75  LEU   A HB3  1 
ATOM   1598 H HG   . LEU   A 1 75  ? 33.872 -0.498  -1.547  1.00 16.09 ?  75  LEU   A HG   1 
ATOM   1599 H HD11 . LEU   A 1 75  ? 32.540 -1.360  0.164   1.00 18.44 ?  75  LEU   A HD11 1 
ATOM   1600 H HD12 . LEU   A 1 75  ? 31.683 -1.100  -1.148  1.00 18.44 ?  75  LEU   A HD12 1 
ATOM   1601 H HD13 . LEU   A 1 75  ? 32.136 -2.576  -0.775  1.00 18.44 ?  75  LEU   A HD13 1 
ATOM   1602 H HD21 . LEU   A 1 75  ? 34.870 -1.874  0.036   1.00 20.21 ?  75  LEU   A HD21 1 
ATOM   1603 H HD22 . LEU   A 1 75  ? 34.687 -3.106  -0.949  1.00 20.21 ?  75  LEU   A HD22 1 
ATOM   1604 H HD23 . LEU   A 1 75  ? 35.647 -1.905  -1.349  1.00 20.21 ?  75  LEU   A HD23 1 
ATOM   1605 N N    . LYS   A 1 76  ? 34.058 -3.652  -5.347  1.00 12.51 ?  76  LYS   A N    1 
ATOM   1606 C CA   . LYS   A 1 76  ? 33.455 -4.357  -6.473  1.00 13.17 ?  76  LYS   A CA   1 
ATOM   1607 C C    . LYS   A 1 76  ? 31.945 -4.445  -6.274  1.00 11.96 ?  76  LYS   A C    1 
ATOM   1608 O O    . LYS   A 1 76  ? 31.466 -4.574  -5.151  1.00 11.72 ?  76  LYS   A O    1 
ATOM   1609 C CB   . LYS   A 1 76  ? 33.996 -5.796  -6.550  1.00 15.33 ?  76  LYS   A CB   1 
ATOM   1610 C CG   . LYS   A 1 76  ? 35.506 -5.907  -6.724  1.00 16.84 ?  76  LYS   A CG   1 
ATOM   1611 C CD   . LYS   A 1 76  ? 36.011 -7.323  -6.528  1.00 18.07 ?  76  LYS   A CD   1 
ATOM   1612 C CE   . LYS   A 1 76  ? 37.511 -7.399  -6.728  1.00 20.36 ?  76  LYS   A CE   1 
ATOM   1613 N NZ   . LYS   A 1 76  ? 38.035 -8.753  -6.474  1.00 21.32 ?  76  LYS   A NZ   1 
ATOM   1614 H H    . LYS   A 1 76  ? 34.269 -4.176  -4.695  1.00 15.02 ?  76  LYS   A H    1 
ATOM   1615 H HA   . LYS   A 1 76  ? 33.648 -3.891  -7.305  1.00 15.81 ?  76  LYS   A HA   1 
ATOM   1616 H HB2  . LYS   A 1 76  ? 33.760 -6.253  -5.730  1.00 18.40 ?  76  LYS   A HB2  1 
ATOM   1617 H HB3  . LYS   A 1 76  ? 33.581 -6.236  -7.305  1.00 18.40 ?  76  LYS   A HB3  1 
ATOM   1618 H HG2  . LYS   A 1 76  ? 35.744 -5.622  -7.620  1.00 20.22 ?  76  LYS   A HG2  1 
ATOM   1619 H HG3  . LYS   A 1 76  ? 35.944 -5.339  -6.069  1.00 20.22 ?  76  LYS   A HG3  1 
ATOM   1620 H HD2  . LYS   A 1 76  ? 35.805 -7.617  -5.626  1.00 21.69 ?  76  LYS   A HD2  1 
ATOM   1621 H HD3  . LYS   A 1 76  ? 35.585 -7.908  -7.176  1.00 21.69 ?  76  LYS   A HD3  1 
ATOM   1622 H HE2  . LYS   A 1 76  ? 37.721 -7.156  -7.642  1.00 24.44 ?  76  LYS   A HE2  1 
ATOM   1623 H HE3  . LYS   A 1 76  ? 37.943 -6.788  -6.110  1.00 24.44 ?  76  LYS   A HE3  1 
ATOM   1624 H HZ1  . LYS   A 1 76  ? 38.915 -8.774  -6.599  1.00 25.59 ?  76  LYS   A HZ1  1 
ATOM   1625 H HZ2  . LYS   A 1 76  ? 37.856 -9.004  -5.638  1.00 25.59 ?  76  LYS   A HZ2  1 
ATOM   1626 H HZ3  . LYS   A 1 76  ? 37.654 -9.340  -7.033  1.00 25.59 ?  76  LYS   A HZ3  1 
ATOM   1627 N N    . VAL   A 1 77  ? 31.190 -4.410  -7.376  1.00 12.26 ?  77  VAL   A N    1 
ATOM   1628 C CA   . VAL   A 1 77  ? 29.784 -4.795  -7.289  1.00 12.20 ?  77  VAL   A CA   1 
ATOM   1629 C C    . VAL   A 1 77  ? 29.717 -6.250  -6.847  1.00 11.85 ?  77  VAL   A C    1 
ATOM   1630 O O    . VAL   A 1 77  ? 30.367 -7.122  -7.433  1.00 12.29 ?  77  VAL   A O    1 
ATOM   1631 C CB   . VAL   A 1 77  ? 29.058 -4.573  -8.623  1.00 13.23 ?  77  VAL   A CB   1 
ATOM   1632 C CG1  . VAL   A 1 77  ? 27.592 -5.012  -8.510  1.00 14.12 ?  77  VAL   A CG1  1 
ATOM   1633 C CG2  . VAL   A 1 77  ? 29.138 -3.113  -9.037  1.00 15.04 ?  77  VAL   A CG2  1 
ATOM   1634 H H    . VAL   A 1 77  ? 31.465 -4.172  -8.154  1.00 14.71 ?  77  VAL   A H    1 
ATOM   1635 H HA   . VAL   A 1 77  ? 29.350 -4.252  -6.611  1.00 14.64 ?  77  VAL   A HA   1 
ATOM   1636 H HB   . VAL   A 1 77  ? 29.486 -5.107  -9.310  1.00 15.88 ?  77  VAL   A HB   1 
ATOM   1637 H HG11 . VAL   A 1 77  ? 27.113 -4.709  -9.294  1.00 16.94 ?  77  VAL   A HG11 1 
ATOM   1638 H HG12 . VAL   A 1 77  ? 27.553 -5.978  -8.447  1.00 16.94 ?  77  VAL   A HG12 1 
ATOM   1639 H HG13 . VAL   A 1 77  ? 27.206 -4.613  -7.712  1.00 16.94 ?  77  VAL   A HG13 1 
ATOM   1640 H HG21 . VAL   A 1 77  ? 28.629 -2.990  -9.852  1.00 18.05 ?  77  VAL   A HG21 1 
ATOM   1641 H HG22 . VAL   A 1 77  ? 28.766 -2.565  -8.327  1.00 18.05 ?  77  VAL   A HG22 1 
ATOM   1642 H HG23 . VAL   A 1 77  ? 30.066 -2.875  -9.185  1.00 18.05 ?  77  VAL   A HG23 1 
ATOM   1643 N N    . GLY   A 1 78  ? 28.935 -6.516  -5.799  1.00 11.45 ?  78  GLY   A N    1 
ATOM   1644 C CA   . GLY   A 1 78  ? 28.909 -7.804  -5.145  1.00 11.67 ?  78  GLY   A CA   1 
ATOM   1645 C C    . GLY   A 1 78  ? 29.822 -7.899  -3.943  1.00 10.91 ?  78  GLY   A C    1 
ATOM   1646 O O    . GLY   A 1 78  ? 29.764 -8.903  -3.216  1.00 11.90 ?  78  GLY   A O    1 
ATOM   1647 H H    . GLY   A 1 78  ? 28.394 -5.940  -5.450  1.00 13.75 ?  78  GLY   A H    1 
ATOM   1648 H HA2  . GLY   A 1 78  ? 28.004 -7.993  -4.854  1.00 14.01 ?  78  GLY   A HA2  1 
ATOM   1649 H HA3  . GLY   A 1 78  ? 29.172 -8.487  -5.783  1.00 14.01 ?  78  GLY   A HA3  1 
ATOM   1650 N N    . GLY   A 1 79  ? 30.681 -6.899  -3.726  1.00 11.05 ?  79  GLY   A N    1 
ATOM   1651 C CA   . GLY   A 1 79  ? 31.641 -6.917  -2.647  1.00 11.51 ?  79  GLY   A CA   1 
ATOM   1652 C C    . GLY   A 1 79  ? 31.199 -6.121  -1.433  1.00 10.97 ?  79  GLY   A C    1 
ATOM   1653 O O    . GLY   A 1 79  ? 30.079 -5.609  -1.351  1.00 11.57 ?  79  GLY   A O    1 
ATOM   1654 H H    . GLY   A 1 79  ? 30.724 -6.185  -4.210  1.00 13.27 ?  79  GLY   A H    1 
ATOM   1655 H HA2  . GLY   A 1 79  ? 31.793 -7.842  -2.376  1.00 13.82 ?  79  GLY   A HA2  1 
ATOM   1656 H HA3  . GLY   A 1 79  ? 32.485 -6.559  -2.965  1.00 13.82 ?  79  GLY   A HA3  1 
ATOM   1657 N N    . SER   A 1 80  ? 32.111 -6.028  -0.465  1.00 11.74 ?  80  SER   A N    1 
ATOM   1658 C CA   . SER   A 1 80  ? 31.796 -5.399  0.809   1.00 11.22 ?  80  SER   A CA   1 
ATOM   1659 C C    . SER   A 1 80  ? 33.067 -4.954  1.510   1.00 11.01 ?  80  SER   A C    1 
ATOM   1660 O O    . SER   A 1 80  ? 34.177 -5.390  1.182   1.00 12.55 ?  80  SER   A O    1 
ATOM   1661 C CB   . SER   A 1 80  ? 31.040 -6.366  1.726   1.00 12.28 ?  80  SER   A CB   1 
ATOM   1662 O OG   . SER   A 1 80  ? 31.866 -7.411  2.213   1.00 14.08 ?  80  SER   A OG   1 
ATOM   1663 H H    . SER   A 1 80  ? 32.923 -6.310  -0.529  1.00 14.09 ?  80  SER   A H    1 
ATOM   1664 H HA   . SER   A 1 80  ? 31.241 -4.619  0.637   1.00 13.47 ?  80  SER   A HA   1 
ATOM   1665 H HB2  . SER   A 1 80  ? 30.693 -5.863  2.478   1.00 14.74 ?  80  SER   A HB2  1 
ATOM   1666 H HB3  . SER   A 1 80  ? 30.305 -6.752  1.223   1.00 14.74 ?  80  SER   A HB3  1 
ATOM   1667 H HG   . SER   A 1 80  ? 32.173 -7.852  1.563   1.00 16.91 ?  80  SER   A HG   1 
ATOM   1668 N N    . CYS   A 1 81  ? 32.877 -4.106  2.519   1.00 10.98 ?  81  CYS   A N    1 
ATOM   1669 C CA   . CYS   A 1 81  ? 33.926 -3.824  3.485   1.00 11.21 ?  81  CYS   A CA   1 
ATOM   1670 C C    . CYS   A 1 81  ? 33.285 -3.589  4.845   1.00 11.12 ?  81  CYS   A C    1 
ATOM   1671 O O    . CYS   A 1 81  ? 32.122 -3.188  4.934   1.00 12.19 ?  81  CYS   A O    1 
ATOM   1672 C CB   . CYS   A 1 81  ? 34.803 -2.632  3.070   1.00 12.13 ?  81  CYS   A CB   1 
ATOM   1673 S SG   . CYS   A 1 81  ? 33.914 -1.053  3.080   1.00 12.03 ?  81  CYS   A SG   1 
ATOM   1674 H H    . CYS   A 1 81  ? 32.141 -3.677  2.665   1.00 13.18 ?  81  CYS   A H    1 
ATOM   1675 H HA   . CYS   A 1 81  ? 34.499 -4.599  3.557   1.00 13.46 ?  81  CYS   A HA   1 
ATOM   1676 H HB2  . CYS   A 1 81  ? 35.553 -2.564  3.687   1.00 14.56 ?  81  CYS   A HB2  1 
ATOM   1677 H HB3  . CYS   A 1 81  ? 35.138 -2.787  2.169   1.00 14.56 ?  81  CYS   A HB3  1 
ATOM   1678 H HG   . CYS   A 1 81  ? 34.665 -0.176  2.747   1.00 14.44 ?  81  CYS   A HG   1 
ATOM   1679 N N    . VAL   A 1 82  ? 34.055 -3.843  5.902   1.00 11.17 ?  82  VAL   A N    1 
ATOM   1680 C CA   . VAL   A 1 82  ? 33.628 -3.598  7.274   1.00 11.87 ?  82  VAL   A CA   1 
ATOM   1681 C C    . VAL   A 1 82  ? 34.229 -2.285  7.745   1.00 12.04 ?  82  VAL   A C    1 
ATOM   1682 O O    . VAL   A 1 82  ? 35.455 -2.112  7.725   1.00 12.71 ?  82  VAL   A O    1 
ATOM   1683 C CB   . VAL   A 1 82  ? 34.050 -4.739  8.210   1.00 13.23 ?  82  VAL   A CB   1 
ATOM   1684 C CG1  . VAL   A 1 82  ? 33.606 -4.435  9.635   1.00 14.82 ?  82  VAL   A CG1  1 
ATOM   1685 C CG2  . VAL   A 1 82  ? 33.487 -6.069  7.738   1.00 14.29 ?  82  VAL   A CG2  1 
ATOM   1686 H H    . VAL   A 1 82  ? 34.852 -4.176  5.846   1.00 13.41 ?  82  VAL   A H    1 
ATOM   1687 H HA   . VAL   A 1 82  ? 32.660 -3.518  7.297   1.00 14.25 ?  82  VAL   A HA   1 
ATOM   1688 H HB   . VAL   A 1 82  ? 35.015 -4.801  8.210   1.00 15.88 ?  82  VAL   A HB   1 
ATOM   1689 H HG11 . VAL   A 1 82  ? 33.680 -5.242  10.167  1.00 17.79 ?  82  VAL   A HG11 1 
ATOM   1690 H HG12 . VAL   A 1 82  ? 34.172 -3.741  10.009  1.00 17.79 ?  82  VAL   A HG12 1 
ATOM   1691 H HG13 . VAL   A 1 82  ? 32.680 -4.134  9.623   1.00 17.79 ?  82  VAL   A HG13 1 
ATOM   1692 H HG21 . VAL   A 1 82  ? 33.734 -6.758  8.373   1.00 17.16 ?  82  VAL   A HG21 1 
ATOM   1693 H HG22 . VAL   A 1 82  ? 32.520 -6.002  7.682   1.00 17.16 ?  82  VAL   A HG22 1 
ATOM   1694 H HG23 . VAL   A 1 82  ? 33.854 -6.274  6.865   1.00 17.16 ?  82  VAL   A HG23 1 
ATOM   1695 N N    . LEU   A 1 83  ? 33.374 -1.360  8.170   1.00 11.36 ?  83  LEU   A N    1 
ATOM   1696 C CA   . LEU   A 1 83  ? 33.796 -0.096  8.751   1.00 11.42 ?  83  LEU   A CA   1 
ATOM   1697 C C    . LEU   A 1 83  ? 33.081 0.085   10.086  1.00 11.69 ?  83  LEU   A C    1 
ATOM   1698 O O    . LEU   A 1 83  ? 32.358 -0.804  10.554  1.00 12.01 ?  83  LEU   A O    1 
ATOM   1699 C CB   . LEU   A 1 83  ? 33.554 1.061   7.771   1.00 12.33 ?  83  LEU   A CB   1 
ATOM   1700 C CG   . LEU   A 1 83  ? 34.454 1.066   6.529   1.00 12.82 ?  83  LEU   A CG   1 
ATOM   1701 C CD1  . LEU   A 1 83  ? 34.015 2.119   5.531   1.00 13.95 ?  83  LEU   A CD1  1 
ATOM   1702 C CD2  . LEU   A 1 83  ? 35.928 1.266   6.913   1.00 13.68 ?  83  LEU   A CD2  1 
ATOM   1703 H H    . LEU   A 1 83  ? 32.518 -1.445  8.126   1.00 13.63 ?  83  LEU   A H    1 
ATOM   1704 H HA   . LEU   A 1 83  ? 34.749 -0.133  8.927   1.00 13.71 ?  83  LEU   A HA   1 
ATOM   1705 H HB2  . LEU   A 1 83  ? 32.637 1.021   7.460   1.00 14.80 ?  83  LEU   A HB2  1 
ATOM   1706 H HB3  . LEU   A 1 83  ? 33.701 1.900   8.236   1.00 14.80 ?  83  LEU   A HB3  1 
ATOM   1707 H HG   . LEU   A 1 83  ? 34.383 0.202   6.097   1.00 15.39 ?  83  LEU   A HG   1 
ATOM   1708 H HD11 . LEU   A 1 83  ? 34.608 2.087   4.762   1.00 16.74 ?  83  LEU   A HD11 1 
ATOM   1709 H HD12 . LEU   A 1 83  ? 33.107 1.934   5.259   1.00 16.74 ?  83  LEU   A HD12 1 
ATOM   1710 H HD13 . LEU   A 1 83  ? 34.068 2.992   5.952   1.00 16.74 ?  83  LEU   A HD13 1 
ATOM   1711 H HD21 . LEU   A 1 83  ? 36.448 1.416   6.106   1.00 16.43 ?  83  LEU   A HD21 1 
ATOM   1712 H HD22 . LEU   A 1 83  ? 36.005 2.033   7.501   1.00 16.43 ?  83  LEU   A HD22 1 
ATOM   1713 H HD23 . LEU   A 1 83  ? 36.252 0.470   7.366   1.00 16.43 ?  83  LEU   A HD23 1 
ATOM   1714 N N    . SER   A 1 84  ? 33.305 1.237   10.719  1.00 12.00 ?  84  SER   A N    1 
ATOM   1715 C CA   . SER   A 1 84  ? 32.660 1.497   11.995  1.00 12.40 ?  84  SER   A CA   1 
ATOM   1716 C C    . SER   A 1 84  ? 31.143 1.579   11.846  1.00 12.10 ?  84  SER   A C    1 
ATOM   1717 O O    . SER   A 1 84  ? 30.618 2.044   10.836  1.00 12.23 ?  84  SER   A O    1 
ATOM   1718 C CB   . SER   A 1 84  ? 33.157 2.819   12.570  1.00 13.24 ?  84  SER   A CB   1 
ATOM   1719 O OG   . SER   A 1 84  ? 32.519 3.097   13.800  1.00 14.05 ?  84  SER   A OG   1 
ATOM   1720 H H    . SER   A 1 84  ? 33.810 1.877   10.425  1.00 14.41 ?  84  SER   A H    1 
ATOM   1721 H HA   . SER   A 1 84  ? 32.881 0.788   12.615  1.00 14.88 ?  84  SER   A HA   1 
ATOM   1722 H HB2  . SER   A 1 84  ? 34.118 2.766   12.712  1.00 15.89 ?  84  SER   A HB2  1 
ATOM   1723 H HB3  . SER   A 1 84  ? 32.959 3.535   11.942  1.00 15.89 ?  84  SER   A HB3  1 
ATOM   1724 H HG   . SER   A 1 84  ? 32.801 3.827   14.112  1.00 16.86 ?  84  SER   A HG   1 
ATOM   1725 N N    . GLY   A 1 85  ? 30.438 1.169   12.895  1.00 13.05 ?  85  GLY   A N    1 
ATOM   1726 C CA   . GLY   A 1 85  ? 29.015 1.409   12.988  1.00 13.62 ?  85  GLY   A CA   1 
ATOM   1727 C C    . GLY   A 1 85  ? 28.648 2.724   13.636  1.00 13.32 ?  85  GLY   A C    1 
ATOM   1728 O O    . GLY   A 1 85  ? 27.458 3.040   13.753  1.00 13.86 ?  85  GLY   A O    1 
ATOM   1729 H H    . GLY   A 1 85  ? 30.774 0.742   13.567  1.00 15.66 ?  85  GLY   A H    1 
ATOM   1730 H HA2  . GLY   A 1 85  ? 28.639 1.391   12.095  1.00 16.35 ?  85  GLY   A HA2  1 
ATOM   1731 H HA3  . GLY   A 1 85  ? 28.611 0.695   13.500  1.00 16.35 ?  85  GLY   A HA3  1 
ATOM   1732 N N    . HIS   A 1 86  ? 29.635 3.496   14.078  1.00 13.11 ?  86  HIS   A N    1 
ATOM   1733 C CA   . HIS   A 1 86  ? 29.406 4.833   14.642  1.00 13.44 ?  86  HIS   A CA   1 
ATOM   1734 C C    . HIS   A 1 86  ? 28.414 4.711   15.793  1.00 14.35 ?  86  HIS   A C    1 
ATOM   1735 O O    . HIS   A 1 86  ? 28.592 3.831   16.652  1.00 15.26 ?  86  HIS   A O    1 
ATOM   1736 C CB   . HIS   A 1 86  ? 29.035 5.820   13.539  1.00 13.30 ?  86  HIS   A CB   1 
ATOM   1737 C CG   . HIS   A 1 86  ? 30.091 5.915   12.497  1.00 13.44 ?  86  HIS   A CG   1 
ATOM   1738 N ND1  . HIS   A 1 86  ? 31.183 6.746   12.625  1.00 14.77 ?  86  HIS   A ND1  1 
ATOM   1739 C CD2  . HIS   A 1 86  ? 30.269 5.223   11.351  1.00 13.06 ?  86  HIS   A CD2  1 
ATOM   1740 C CE1  . HIS   A 1 86  ? 31.975 6.576   11.581  1.00 14.40 ?  86  HIS   A CE1  1 
ATOM   1741 N NE2  . HIS   A 1 86  ? 31.449 5.652   10.800  1.00 13.43 ?  86  HIS   A NE2  1 
ATOM   1742 H H    . HIS   A 1 86  ? 30.462 3.270   14.075  1.00 15.73 ?  86  HIS   A H    1 
ATOM   1743 H HA   . HIS   A 1 86  ? 30.239 5.146   15.022  1.00 16.14 ?  86  HIS   A HA   1 
ATOM   1744 H HB2  . HIS   A 1 86  ? 28.212 5.539   13.110  1.00 15.96 ?  86  HIS   A HB2  1 
ATOM   1745 H HB3  . HIS   A 1 86  ? 28.918 6.709   13.923  1.00 15.96 ?  86  HIS   A HB3  1 
ATOM   1746 H HD2  . HIS   A 1 86  ? 29.702 4.564   11.004  1.00 15.68 ?  86  HIS   A HD2  1 
ATOM   1747 H HE1  . HIS   A 1 86  ? 32.768 7.031   11.406  1.00 17.28 ?  86  HIS   A HE1  1 
ATOM   1748 H HE2  . HIS   A 1 86  ? 31.780 5.371   10.046  1.00 16.12 ?  86  HIS   A HE2  1 
ATOM   1749 N N    . ASN   A 1 87  ? 27.407 5.569   15.865  1.00 15.08 ?  87  ASN   A N    1 
ATOM   1750 C CA   . ASN   A 1 87  ? 26.426 5.559   16.934  1.00 16.14 ?  87  ASN   A CA   1 
ATOM   1751 C C    . ASN   A 1 87  ? 25.307 4.557   16.703  1.00 17.46 ?  87  ASN   A C    1 
ATOM   1752 O O    . ASN   A 1 87  ? 24.395 4.477   17.530  1.00 19.76 ?  87  ASN   A O    1 
ATOM   1753 C CB   . ASN   A 1 87  ? 25.826 6.964   17.093  1.00 17.01 ?  87  ASN   A CB   1 
ATOM   1754 C CG   . ASN   A 1 87  ? 25.320 7.540   15.776  1.00 17.82 ?  87  ASN   A CG   1 
ATOM   1755 O OD1  . ASN   A 1 87  ? 25.968 7.428   14.739  1.00 18.49 ?  87  ASN   A OD1  1 
ATOM   1756 N ND2  . ASN   A 1 87  ? 24.158 8.162   15.818  1.00 18.79 ?  87  ASN   A ND2  1 
ATOM   1757 H H    . ASN   A 1 87  ? 27.263 6.183   15.287  1.00 18.10 ?  87  ASN   A H    1 
ATOM   1758 H HA   . ASN   A 1 87  ? 26.859 5.325   17.774  1.00 19.37 ?  87  ASN   A HA   1 
ATOM   1759 H HB2  . ASN   A 1 87  ? 25.076 6.920   17.715  1.00 20.41 ?  87  ASN   A HB2  1 
ATOM   1760 H HB3  . ASN   A 1 87  ? 26.506 7.559   17.444  1.00 20.41 ?  87  ASN   A HB3  1 
ATOM   1761 H HD21 . ASN   A 1 87  ? 23.832 8.501   15.101  1.00 22.55 ?  87  ASN   A HD21 1 
ATOM   1762 H HD22 . ASN   A 1 87  ? 23.732 8.230   16.563  1.00 22.55 ?  87  ASN   A HD22 1 
ATOM   1763 N N    . LEU   A 1 88  ? 25.358 3.788   15.619  1.00 16.25 ?  88  LEU   A N    1 
ATOM   1764 C CA   . LEU   A 1 88  ? 24.250 2.924   15.228  1.00 16.09 ?  88  LEU   A CA   1 
ATOM   1765 C C    . LEU   A 1 88  ? 24.470 1.448   15.534  1.00 15.37 ?  88  LEU   A C    1 
ATOM   1766 O O    . LEU   A 1 88  ? 23.491 0.717   15.717  1.00 16.98 ?  88  LEU   A O    1 
ATOM   1767 C CB   . LEU   A 1 88  ? 23.994 3.075   13.728  1.00 16.80 ?  88  LEU   A CB   1 
ATOM   1768 C CG   . LEU   A 1 88  ? 23.695 4.495   13.244  1.00 18.29 ?  88  LEU   A CG   1 
ATOM   1769 C CD1  . LEU   A 1 88  ? 23.541 4.506   11.735  1.00 18.39 ?  88  LEU   A CD1  1 
ATOM   1770 C CD2  . LEU   A 1 88  ? 22.450 5.053   13.917  1.00 19.91 ?  88  LEU   A CD2  1 
ATOM   1771 H H    . LEU   A 1 88  ? 26.032 3.749   15.094  1.00 19.50 ?  88  LEU   A H    1 
ATOM   1772 H HA   . LEU   A 1 88  ? 23.448 3.210   15.697  1.00 19.31 ?  88  LEU   A HA   1 
ATOM   1773 H HB2  . LEU   A 1 88  ? 24.774 2.766   13.249  1.00 20.16 ?  88  LEU   A HB2  1 
ATOM   1774 H HB3  . LEU   A 1 88  ? 23.228 2.527   13.492  1.00 20.16 ?  88  LEU   A HB3  1 
ATOM   1775 H HG   . LEU   A 1 88  ? 24.441 5.072   13.468  1.00 21.95 ?  88  LEU   A HG   1 
ATOM   1776 H HD11 . LEU   A 1 88  ? 23.375 5.416   11.439  1.00 22.08 ?  88  LEU   A HD11 1 
ATOM   1777 H HD12 . LEU   A 1 88  ? 24.358 4.173   11.331  1.00 22.08 ?  88  LEU   A HD12 1 
ATOM   1778 H HD13 . LEU   A 1 88  ? 22.795 3.938   11.489  1.00 22.08 ?  88  LEU   A HD13 1 
ATOM   1779 H HD21 . LEU   A 1 88  ? 22.222 5.901   13.505  1.00 23.89 ?  88  LEU   A HD21 1 
ATOM   1780 H HD22 . LEU   A 1 88  ? 21.723 4.423   13.804  1.00 23.89 ?  88  LEU   A HD22 1 
ATOM   1781 H HD23 . LEU   A 1 88  ? 22.636 5.182   14.860  1.00 23.89 ?  88  LEU   A HD23 1 
ATOM   1782 N N    . ALA   A 1 89  ? 25.720 0.997   15.578  1.00 14.54 ?  89  ALA   A N    1 
ATOM   1783 C CA   . ALA   A 1 89  ? 26.059 -0.415  15.679  1.00 14.42 ?  89  ALA   A CA   1 
ATOM   1784 C C    . ALA   A 1 89  ? 27.545 -0.490  15.989  1.00 15.20 ?  89  ALA   A C    1 
ATOM   1785 O O    . ALA   A 1 89  ? 28.263 0.503   15.869  1.00 15.73 ?  89  ALA   A O    1 
ATOM   1786 C CB   . ALA   A 1 89  ? 25.765 -1.131  14.361  1.00 14.28 ?  89  ALA   A CB   1 
ATOM   1787 H H    . ALA   A 1 89  ? 26.408 1.514   15.538  1.00 17.45 ?  89  ALA   A H    1 
ATOM   1788 H HA   . ALA   A 1 89  ? 25.553 -0.827  16.399  1.00 17.31 ?  89  ALA   A HA   1 
ATOM   1789 H HB1  . ALA   A 1 89  ? 26.018 -2.065  14.452  1.00 17.15 ?  89  ALA   A HB1  1 
ATOM   1790 H HB2  . ALA   A 1 89  ? 24.815 -1.067  14.170  1.00 17.15 ?  89  ALA   A HB2  1 
ATOM   1791 H HB3  . ALA   A 1 89  ? 26.277 -0.717  13.655  1.00 17.15 ?  89  ALA   A HB3  1 
ATOM   1792 N N    . LYS   A 1 90  ? 28.019 -1.671  16.381  1.00 15.82 ?  90  LYS   A N    1 
ATOM   1793 C CA   . LYS   A 1 90  ? 29.464 -1.830  16.518  1.00 16.69 ?  90  LYS   A CA   1 
ATOM   1794 C C    . LYS   A 1 90  ? 30.159 -1.640  15.172  1.00 15.30 ?  90  LYS   A C    1 
ATOM   1795 O O    . LYS   A 1 90  ? 31.098 -0.838  15.044  1.00 16.81 ?  90  LYS   A O    1 
ATOM   1796 C CB   . LYS   A 1 90  ? 29.802 -3.190  17.131  1.00 19.14 ?  90  LYS   A CB   1 
ATOM   1797 C CG   . LYS   A 1 90  ? 31.281 -3.343  17.464  1.00 23.78 ?  90  LYS   A CG   1 
ATOM   1798 C CD   . LYS   A 1 90  ? 31.526 -4.570  18.327  1.00 28.94 ?  90  LYS   A CD   1 
ATOM   1799 C CE   . LYS   A 1 90  ? 32.942 -4.598  18.881  1.00 32.89 ?  90  LYS   A CE   1 
ATOM   1800 N NZ   . LYS   A 1 90  ? 33.955 -4.938  17.846  1.00 35.10 ?  90  LYS   A NZ   1 
ATOM   1801 H H    . LYS   A 1 90  ? 27.542 -2.357  16.567  1.00 18.99 ?  90  LYS   A H    1 
ATOM   1802 H HA   . LYS   A 1 90  ? 29.796 -1.146  17.116  1.00 20.04 ?  90  LYS   A HA   1 
ATOM   1803 H HB2  . LYS   A 1 90  ? 29.295 -3.298  17.954  1.00 22.98 ?  90  LYS   A HB2  1 
ATOM   1804 H HB3  . LYS   A 1 90  ? 29.561 -3.889  16.503  1.00 22.98 ?  90  LYS   A HB3  1 
ATOM   1805 H HG2  . LYS   A 1 90  ? 31.786 -3.442  16.643  1.00 28.54 ?  90  LYS   A HG2  1 
ATOM   1806 H HG3  . LYS   A 1 90  ? 31.581 -2.561  17.954  1.00 28.54 ?  90  LYS   A HG3  1 
ATOM   1807 H HD2  . LYS   A 1 90  ? 30.908 -4.564  19.076  1.00 34.73 ?  90  LYS   A HD2  1 
ATOM   1808 H HD3  . LYS   A 1 90  ? 31.393 -5.369  17.793  1.00 34.73 ?  90  LYS   A HD3  1 
ATOM   1809 H HE2  . LYS   A 1 90  ? 33.159 -3.722  19.237  1.00 39.47 ?  90  LYS   A HE2  1 
ATOM   1810 H HE3  . LYS   A 1 90  ? 32.994 -5.265  19.584  1.00 39.47 ?  90  LYS   A HE3  1 
ATOM   1811 H HZ1  . LYS   A 1 90  ? 34.767 -4.964  18.212  1.00 42.13 ?  90  LYS   A HZ1  1 
ATOM   1812 H HZ2  . LYS   A 1 90  ? 33.773 -5.735  17.492  1.00 42.13 ?  90  LYS   A HZ2  1 
ATOM   1813 H HZ3  . LYS   A 1 90  ? 33.949 -4.327  17.200  1.00 42.13 ?  90  LYS   A HZ3  1 
ATOM   1814 N N    . HIS   A 1 91  ? 29.685 -2.354  14.149  1.00 13.42 ?  91  HIS   A N    1 
ATOM   1815 C CA   . HIS   A 1 91  ? 30.260 -2.338  12.818  1.00 12.92 ?  91  HIS   A CA   1 
ATOM   1816 C C    . HIS   A 1 91  ? 29.175 -2.060  11.795  1.00 11.78 ?  91  HIS   A C    1 
ATOM   1817 O O    . HIS   A 1 91  ? 28.008 -2.411  11.995  1.00 12.34 ?  91  HIS   A O    1 
ATOM   1818 C CB   . HIS   A 1 91  ? 30.858 -3.707  12.452  1.00 15.30 ?  91  HIS   A CB   1 
ATOM   1819 C CG   . HIS   A 1 91  ? 31.837 -4.236  13.450  1.00 20.05 ?  91  HIS   A CG   1 
ATOM   1820 N ND1  . HIS   A 1 91  ? 33.117 -3.741  13.573  1.00 22.16 ?  91  HIS   A ND1  1 
ATOM   1821 C CD2  . HIS   A 1 91  ? 31.730 -5.231  14.361  1.00 21.82 ?  91  HIS   A CD2  1 
ATOM   1822 C CE1  . HIS   A 1 91  ? 33.755 -4.406  14.521  1.00 23.11 ?  91  HIS   A CE1  1 
ATOM   1823 N NE2  . HIS   A 1 91  ? 32.935 -5.317  15.015  1.00 23.23 ?  91  HIS   A NE2  1 
ATOM   1824 H H    . HIS   A 1 91  ? 29.001 -2.888  14.216  1.00 16.11 ?  91  HIS   A H    1 
ATOM   1825 H HA   . HIS   A 1 91  ? 30.947 -1.661  12.757  1.00 15.51 ?  91  HIS   A HA   1 
ATOM   1826 H HB2  . HIS   A 1 91  ? 30.139 -4.355  12.377  1.00 18.37 ?  91  HIS   A HB2  1 
ATOM   1827 H HB3  . HIS   A 1 91  ? 31.317 -3.629  11.601  1.00 18.37 ?  91  HIS   A HB3  1 
ATOM   1828 H HD1  . HIS   A 1 91  ? 33.452 -3.100  13.103  1.00 26.60 ?  91  HIS   A HD1  1 
ATOM   1829 H HD2  . HIS   A 1 91  ? 30.985 -5.759  14.518  1.00 26.19 ?  91  HIS   A HD2  1 
ATOM   1830 H HE1  . HIS   A 1 91  ? 34.635 -4.253  14.794  1.00 27.74 ?  91  HIS   A HE1  1 
ATOM   1831 N N    . CYS   A 1 92  ? 29.580 -1.466  10.678  1.00 11.50 ?  92  CYS   A N    1 
ATOM   1832 C CA   . CYS   A 1 92  ? 28.745 -1.382  9.489   1.00 11.27 ?  92  CYS   A CA   1 
ATOM   1833 C C    . CYS   A 1 92  ? 29.392 -2.211  8.386   1.00 10.98 ?  92  CYS   A C    1 
ATOM   1834 O O    . CYS   A 1 92  ? 30.552 -1.964  8.017   1.00 11.66 ?  92  CYS   A O    1 
ATOM   1835 C CB   . CYS   A 1 92  ? 28.545 0.063   9.026   1.00 11.48 ?  92  CYS   A CB   1 
ATOM   1836 S SG   . CYS   A 1 92  ? 27.519 0.170   7.516   1.00 11.27 ?  92  CYS   A SG   1 
ATOM   1837 H H    . CYS   A 1 92  ? 30.354 -1.095  10.584  1.00 13.81 ?  92  CYS   A H    1 
ATOM   1838 H HA   . CYS   A 1 92  ? 27.876 -1.759  9.684   1.00 13.53 ?  92  CYS   A HA   1 
ATOM   1839 H HB2  . CYS   A 1 92  ? 28.098 0.565   9.726   1.00 13.78 ?  92  CYS   A HB2  1 
ATOM   1840 H HB3  . CYS   A 1 92  ? 29.406 0.460   8.829   1.00 13.78 ?  92  CYS   A HB3  1 
ATOM   1841 H HG   . CYS   A 1 92  ? 27.391 1.321   7.220   1.00 13.52 ?  92  CYS   A HG   1 
ATOM   1842 N N    . LEU   A 1 93  ? 28.649 -3.192  7.873   1.00 10.70 ?  93  LEU   A N    1 
ATOM   1843 C CA   . LEU   A 1 93  ? 29.051 -3.951  6.694   1.00 10.35 ?  93  LEU   A CA   1 
ATOM   1844 C C    . LEU   A 1 93  ? 28.460 -3.257  5.473   1.00 9.72  ?  93  LEU   A C    1 
ATOM   1845 O O    . LEU   A 1 93  ? 27.247 -3.313  5.245   1.00 10.02 ?  93  LEU   A O    1 
ATOM   1846 C CB   . LEU   A 1 93  ? 28.565 -5.395  6.799   1.00 10.96 ?  93  LEU   A CB   1 
ATOM   1847 C CG   . LEU   A 1 93  ? 28.956 -6.299  5.629   1.00 11.09 ?  93  LEU   A CG   1 
ATOM   1848 C CD1  . LEU   A 1 93  ? 30.462 -6.554  5.621   1.00 12.22 ?  93  LEU   A CD1  1 
ATOM   1849 C CD2  . LEU   A 1 93  ? 28.184 -7.619  5.661   1.00 12.08 ?  93  LEU   A CD2  1 
ATOM   1850 H H    . LEU   A 1 93  ? 27.892 -3.436  8.206   1.00 12.85 ?  93  LEU   A H    1 
ATOM   1851 H HA   . LEU   A 1 93  ? 30.012 -3.944  6.621   1.00 12.43 ?  93  LEU   A HA   1 
ATOM   1852 H HB2  . LEU   A 1 93  ? 28.934 -5.780  7.610   1.00 13.16 ?  93  LEU   A HB2  1 
ATOM   1853 H HB3  . LEU   A 1 93  ? 27.596 -5.391  6.856   1.00 13.16 ?  93  LEU   A HB3  1 
ATOM   1854 H HG   . LEU   A 1 93  ? 28.739 -5.849  4.805   1.00 13.31 ?  93  LEU   A HG   1 
ATOM   1855 H HD11 . LEU   A 1 93  ? 30.677 -7.172  4.907   1.00 14.67 ?  93  LEU   A HD11 1 
ATOM   1856 H HD12 . LEU   A 1 93  ? 30.931 -5.716  5.489   1.00 14.67 ?  93  LEU   A HD12 1 
ATOM   1857 H HD13 . LEU   A 1 93  ? 30.725 -6.942  6.479   1.00 14.67 ?  93  LEU   A HD13 1 
ATOM   1858 H HD21 . LEU   A 1 93  ? 28.467 -8.163  4.905   1.00 14.50 ?  93  LEU   A HD21 1 
ATOM   1859 H HD22 . LEU   A 1 93  ? 28.379 -8.083  6.490   1.00 14.50 ?  93  LEU   A HD22 1 
ATOM   1860 H HD23 . LEU   A 1 93  ? 27.238 -7.431  5.597   1.00 14.50 ?  93  LEU   A HD23 1 
ATOM   1861 N N    . HIS   A 1 94  ? 29.305 -2.566  4.713   1.00 9.79  ?  94  HIS   A N    1 
ATOM   1862 C CA   . HIS   A 1 94  ? 28.883 -1.891  3.488   1.00 9.67  ?  94  HIS   A CA   1 
ATOM   1863 C C    . HIS   A 1 94  ? 28.890 -2.927  2.379   1.00 9.83  ?  94  HIS   A C    1 
ATOM   1864 O O    . HIS   A 1 94  ? 29.959 -3.441  2.036   1.00 11.34 ?  94  HIS   A O    1 
ATOM   1865 C CB   . HIS   A 1 94  ? 29.850 -0.754  3.159   1.00 10.00 ?  94  HIS   A CB   1 
ATOM   1866 C CG   . HIS   A 1 94  ? 29.835 0.342   4.171   1.00 9.83  ?  94  HIS   A CG   1 
ATOM   1867 N ND1  . HIS   A 1 94  ? 28.967 1.413   4.109   1.00 10.07 ?  94  HIS   A ND1  1 
ATOM   1868 C CD2  . HIS   A 1 94  ? 30.572 0.508   5.292   1.00 10.63 ?  94  HIS   A CD2  1 
ATOM   1869 C CE1  . HIS   A 1 94  ? 29.180 2.191   5.154   1.00 10.16 ?  94  HIS   A CE1  1 
ATOM   1870 N NE2  . HIS   A 1 94  ? 30.148 1.666   5.887   1.00 10.68 ?  94  HIS   A NE2  1 
ATOM   1871 H H    . HIS   A 1 94  ? 30.145 -2.471  4.886   1.00 11.76 ?  94  HIS   A H    1 
ATOM   1872 H HA   . HIS   A 1 94  ? 27.984 -1.534  3.592   1.00 11.60 ?  94  HIS   A HA   1 
ATOM   1873 H HB2  . HIS   A 1 94  ? 30.747 -1.110  3.117   1.00 12.01 ?  94  HIS   A HB2  1 
ATOM   1874 H HB3  . HIS   A 1 94  ? 29.600 -0.371  2.302   1.00 12.01 ?  94  HIS   A HB3  1 
ATOM   1875 H HD2  . HIS   A 1 94  ? 31.236 -0.053  5.605   1.00 12.76 ?  94  HIS   A HD2  1 
ATOM   1876 H HE1  . HIS   A 1 94  ? 28.718 2.983   5.336   1.00 12.19 ?  94  HIS   A HE1  1 
ATOM   1877 H HE2  . HIS   A 1 94  ? 30.455 2.009   6.611   1.00 12.82 ?  94  HIS   A HE2  1 
ATOM   1878 N N    . VAL   A 1 95  ? 27.720 -3.242  1.822   1.00 9.30  ?  95  VAL   A N    1 
ATOM   1879 C CA   . VAL   A 1 95  ? 27.578 -4.282  0.806   1.00 9.93  ?  95  VAL   A CA   1 
ATOM   1880 C C    . VAL   A 1 95  ? 27.032 -3.649  -0.462  1.00 9.43  ?  95  VAL   A C    1 
ATOM   1881 O O    . VAL   A 1 95  ? 26.029 -2.924  -0.410  1.00 10.15 ?  95  VAL   A O    1 
ATOM   1882 C CB   . VAL   A 1 95  ? 26.649 -5.419  1.263   1.00 10.51 ?  95  VAL   A CB   1 
ATOM   1883 C CG1  . VAL   A 1 95  ? 26.534 -6.461  0.163   1.00 11.08 ?  95  VAL   A CG1  1 
ATOM   1884 C CG2  . VAL   A 1 95  ? 27.157 -6.037  2.549   1.00 10.60 ?  95  VAL   A CG2  1 
ATOM   1885 H H    . VAL   A 1 95  ? 26.973 -2.861  2.026   1.00 11.17 ?  95  VAL   A H    1 
ATOM   1886 H HA   . VAL   A 1 95  ? 28.447 -4.657  0.606   1.00 11.92 ?  95  VAL   A HA   1 
ATOM   1887 H HB   . VAL   A 1 95  ? 25.767 -5.063  1.430   1.00 12.61 ?  95  VAL   A HB   1 
ATOM   1888 H HG11 . VAL   A 1 95  ? 26.150 -7.275  0.536   1.00 13.30 ?  95  VAL   A HG11 1 
ATOM   1889 H HG12 . VAL   A 1 95  ? 25.964 -6.125  -0.543  1.00 13.30 ?  95  VAL   A HG12 1 
ATOM   1890 H HG13 . VAL   A 1 95  ? 27.420 -6.656  -0.189  1.00 13.30 ?  95  VAL   A HG13 1 
ATOM   1891 H HG21 . VAL   A 1 95  ? 26.597 -6.794  2.778   1.00 12.73 ?  95  VAL   A HG21 1 
ATOM   1892 H HG22 . VAL   A 1 95  ? 28.074 -6.327  2.423   1.00 12.73 ?  95  VAL   A HG22 1 
ATOM   1893 H HG23 . VAL   A 1 95  ? 27.116 -5.370  3.254   1.00 12.73 ?  95  VAL   A HG23 1 
ATOM   1894 N N    . VAL   A 1 96  ? 27.669 -3.935  -1.600  1.00 9.53  ?  96  VAL   A N    1 
ATOM   1895 C CA   . VAL   A 1 96  ? 27.262 -3.378  -2.884  1.00 10.25 ?  96  VAL   A CA   1 
ATOM   1896 C C    . VAL   A 1 96  ? 26.450 -4.422  -3.645  1.00 10.39 ?  96  VAL   A C    1 
ATOM   1897 O O    . VAL   A 1 96  ? 27.000 -5.366  -4.220  1.00 11.32 ?  96  VAL   A O    1 
ATOM   1898 C CB   . VAL   A 1 96  ? 28.455 -2.908  -3.714  1.00 10.67 ?  96  VAL   A CB   1 
ATOM   1899 C CG1  . VAL   A 1 96  ? 27.951 -2.271  -4.984  1.00 11.02 ?  96  VAL   A CG1  1 
ATOM   1900 C CG2  . VAL   A 1 96  ? 29.321 -1.943  -2.919  1.00 11.44 ?  96  VAL   A CG2  1 
ATOM   1901 H H    . VAL   A 1 96  ? 28.360 -4.451  -1.647  1.00 11.44 ?  96  VAL   A H    1 
ATOM   1902 H HA   . VAL   A 1 96  ? 26.694 -2.610  -2.725  1.00 12.31 ?  96  VAL   A HA   1 
ATOM   1903 H HB   . VAL   A 1 96  ? 29.000 -3.671  -3.954  1.00 12.81 ?  96  VAL   A HB   1 
ATOM   1904 H HG11 . VAL   A 1 96  ? 28.688 -1.792  -5.405  1.00 13.23 ?  96  VAL   A HG11 1 
ATOM   1905 H HG12 . VAL   A 1 96  ? 27.624 -2.958  -5.578  1.00 13.23 ?  96  VAL   A HG12 1 
ATOM   1906 H HG13 . VAL   A 1 96  ? 27.243 -1.646  -4.765  1.00 13.23 ?  96  VAL   A HG13 1 
ATOM   1907 H HG21 . VAL   A 1 96  ? 30.024 -1.598  -3.488  1.00 13.73 ?  96  VAL   A HG21 1 
ATOM   1908 H HG22 . VAL   A 1 96  ? 28.768 -1.210  -2.596  1.00 13.73 ?  96  VAL   A HG22 1 
ATOM   1909 H HG23 . VAL   A 1 96  ? 29.710 -2.413  -2.161  1.00 13.73 ?  96  VAL   A HG23 1 
ATOM   1910 N N    . GLY   A 1 97  ? 25.133 -4.255  -3.666  1.00 10.53 ?  97  GLY   A N    1 
ATOM   1911 C CA   . GLY   A 1 97  ? 24.307 -5.005  -4.578  1.00 11.40 ?  97  GLY   A CA   1 
ATOM   1912 C C    . GLY   A 1 97  ? 24.306 -4.359  -5.948  1.00 11.32 ?  97  GLY   A C    1 
ATOM   1913 O O    . GLY   A 1 97  ? 24.587 -3.164  -6.090  1.00 12.13 ?  97  GLY   A O    1 
ATOM   1914 H H    . GLY   A 1 97  ? 24.696 -3.707  -3.156  1.00 12.64 ?  97  GLY   A H    1 
ATOM   1915 H HA2  . GLY   A 1 97  ? 24.652 -5.908  -4.648  1.00 13.68 ?  97  GLY   A HA2  1 
ATOM   1916 H HA3  . GLY   A 1 97  ? 23.398 -5.044  -4.237  1.00 13.68 ?  97  GLY   A HA3  1 
ATOM   1917 N N    . PRO   A 1 98  ? 23.983 -5.118  -6.989  1.00 11.43 ?  98  PRO   A N    1 
ATOM   1918 C CA   . PRO   A 1 98  ? 23.879 -4.509  -8.319  1.00 12.60 ?  98  PRO   A CA   1 
ATOM   1919 C C    . PRO   A 1 98  ? 22.753 -3.483  -8.383  1.00 12.85 ?  98  PRO   A C    1 
ATOM   1920 O O    . PRO   A 1 98  ? 21.678 -3.661  -7.802  1.00 12.87 ?  98  PRO   A O    1 
ATOM   1921 C CB   . PRO   A 1 98  ? 23.602 -5.706  -9.235  1.00 12.85 ?  98  PRO   A CB   1 
ATOM   1922 C CG   . PRO   A 1 98  ? 22.955 -6.720  -8.341  1.00 12.97 ?  98  PRO   A CG   1 
ATOM   1923 C CD   . PRO   A 1 98  ? 23.663 -6.559  -7.011  1.00 11.76 ?  98  PRO   A CD   1 
ATOM   1924 H HA   . PRO   A 1 98  ? 24.718 -4.092  -8.562  1.00 15.12 ?  98  PRO   A HA   1 
ATOM   1925 H HB2  . PRO   A 1 98  ? 22.998 -5.433  -9.944  1.00 15.42 ?  98  PRO   A HB2  1 
ATOM   1926 H HB3  . PRO   A 1 98  ? 24.435 -6.038  -9.595  1.00 15.42 ?  98  PRO   A HB3  1 
ATOM   1927 H HG2  . PRO   A 1 98  ? 22.009 -6.525  -8.253  1.00 15.57 ?  98  PRO   A HG2  1 
ATOM   1928 H HG3  . PRO   A 1 98  ? 23.096 -7.607  -8.700  1.00 15.57 ?  98  PRO   A HG3  1 
ATOM   1929 H HD2  . PRO   A 1 98  ? 23.063 -6.792  -6.279  1.00 14.11 ?  98  PRO   A HD2  1 
ATOM   1930 H HD3  . PRO   A 1 98  ? 24.473 -7.089  -6.988  1.00 14.11 ?  98  PRO   A HD3  1 
ATOM   1931 N N    A ASN   A 1 99  ? 23.027 -2.363  -9.058  0.72 13.54 ?  99  ASN   A N    1 
ATOM   1932 N N    B ASN   A 1 99  ? 23.003 -2.431  -9.148  0.28 13.93 ?  99  ASN   A N    1 
ATOM   1933 C CA   A ASN   A 1 99  ? 22.056 -1.285  -9.245  0.72 14.57 ?  99  ASN   A CA   1 
ATOM   1934 C CA   B ASN   A 1 99  ? 22.000 -1.432  -9.474  0.28 15.14 ?  99  ASN   A CA   1 
ATOM   1935 C C    A ASN   A 1 99  ? 21.501 -1.398  -10.662 0.72 15.47 ?  99  ASN   A C    1 
ATOM   1936 C C    B ASN   A 1 99  ? 21.401 -1.783  -10.830 0.28 16.05 ?  99  ASN   A C    1 
ATOM   1937 O O    A ASN   A 1 99  ? 22.182 -1.059  -11.637 0.72 16.42 ?  99  ASN   A O    1 
ATOM   1938 O O    B ASN   A 1 99  ? 22.104 -1.774  -11.847 0.28 15.95 ?  99  ASN   A O    1 
ATOM   1939 C CB   A ASN   A 1 99  ? 22.692 0.086   -8.997  0.72 14.43 ?  99  ASN   A CB   1 
ATOM   1940 C CB   B ASN   A 1 99  ? 22.637 -0.047  -9.509  0.28 16.35 ?  99  ASN   A CB   1 
ATOM   1941 C CG   A ASN   A 1 99  ? 21.667 1.231   -8.990  0.72 14.66 ?  99  ASN   A CG   1 
ATOM   1942 C CG   B ASN   A 1 99  ? 21.613 1.060   -9.593  0.28 17.21 ?  99  ASN   A CG   1 
ATOM   1943 O OD1  A ASN   A 1 99  ? 20.670 1.191   -9.711  0.72 15.16 ?  99  ASN   A OD1  1 
ATOM   1944 O OD1  B ASN   A 1 99  ? 20.668 0.990   -10.378 0.28 17.46 ?  99  ASN   A OD1  1 
ATOM   1945 N ND2  A ASN   A 1 99  ? 21.930 2.263   -8.185  0.72 15.06 ?  99  ASN   A ND2  1 
ATOM   1946 N ND2  B ASN   A 1 99  ? 21.788 2.086   -8.768  0.28 17.37 ?  99  ASN   A ND2  1 
ATOM   1947 H H    A ASN   A 1 99  ? 23.791 -2.197  -9.414  0.72 16.26 ?  99  ASN   A H    1 
ATOM   1948 H H    B ASN   A 1 99  ? 23.774 -2.271  -9.495  0.28 16.72 ?  99  ASN   A H    1 
ATOM   1949 H HA   A ASN   A 1 99  ? 21.324 -1.397  -8.608  0.72 17.49 ?  99  ASN   A HA   1 
ATOM   1950 H HA   B ASN   A 1 99  ? 21.299 -1.443  -8.803  0.28 18.18 ?  99  ASN   A HA   1 
ATOM   1951 H HB2  A ASN   A 1 99  ? 23.140 0.083   -8.138  0.72 17.32 ?  99  ASN   A HB2  1 
ATOM   1952 H HB2  B ASN   A 1 99  ? 23.155 0.080   -8.701  0.28 19.63 ?  99  ASN   A HB2  1 
ATOM   1953 H HB3  A ASN   A 1 99  ? 23.333 0.264   -9.704  0.72 17.32 ?  99  ASN   A HB3  1 
ATOM   1954 H HB3  B ASN   A 1 99  ? 23.214 0.007   -10.281 0.28 19.63 ?  99  ASN   A HB3  1 
ATOM   1955 H HD21 A ASN   A 1 99  ? 21.388 2.932   -8.149  0.72 18.08 ?  99  ASN   A HD21 1 
ATOM   1956 H HD21 B ASN   A 1 99  ? 21.231 2.740   -8.769  0.28 20.85 ?  99  ASN   A HD21 1 
ATOM   1957 H HD22 A ASN   A 1 99  ? 22.640 2.259   -7.701  0.72 18.08 ?  99  ASN   A HD22 1 
ATOM   1958 H HD22 B ASN   A 1 99  ? 22.462 2.096   -8.231  0.28 20.85 ?  99  ASN   A HD22 1 
ATOM   1959 N N    A VAL   A 1 100 ? 20.262 -1.888  -10.763 0.72 16.36 ?  100 VAL   A N    1 
ATOM   1960 N N    B VAL   A 1 100 ? 20.107 -2.103  -10.835 0.28 17.75 ?  100 VAL   A N    1 
ATOM   1961 C CA   A VAL   A 1 100 ? 19.618 -2.082  -12.059 0.72 18.24 ?  100 VAL   A CA   1 
ATOM   1962 C CA   B VAL   A 1 100 ? 19.431 -2.468  -12.075 0.28 19.66 ?  100 VAL   A CA   1 
ATOM   1963 C C    A VAL   A 1 100 ? 19.495 -0.765  -12.810 0.72 18.16 ?  100 VAL   A C    1 
ATOM   1964 C C    B VAL   A 1 100 ? 19.270 -1.252  -12.976 0.28 20.94 ?  100 VAL   A C    1 
ATOM   1965 O O    A VAL   A 1 100 ? 19.559 -0.737  -14.045 0.72 19.47 ?  100 VAL   A O    1 
ATOM   1966 O O    B VAL   A 1 100 ? 19.347 -1.360  -14.206 0.28 21.41 ?  100 VAL   A O    1 
ATOM   1967 C CB   A VAL   A 1 100 ? 18.257 -2.784  -11.869 0.72 19.81 ?  100 VAL   A CB   1 
ATOM   1968 C CB   B VAL   A 1 100 ? 18.085 -3.147  -11.762 0.28 20.35 ?  100 VAL   A CB   1 
ATOM   1969 C CG1  A VAL   A 1 100 ? 17.533 -2.943  -13.200 0.72 20.68 ?  100 VAL   A CG1  1 
ATOM   1970 C CG1  B VAL   A 1 100 ? 17.281 -3.373  -13.035 0.28 20.59 ?  100 VAL   A CG1  1 
ATOM   1971 C CG2  A VAL   A 1 100 ? 18.460 -4.136  -11.207 0.72 20.70 ?  100 VAL   A CG2  1 
ATOM   1972 C CG2  B VAL   A 1 100 ? 18.329 -4.461  -11.045 0.28 20.79 ?  100 VAL   A CG2  1 
ATOM   1973 H H    A VAL   A 1 100 ? 19.770 -2.116  -10.087 0.72 19.64 ?  100 VAL   A H    1 
ATOM   1974 H H    B VAL   A 1 100 ? 19.604 -2.116  -10.138 0.28 21.30 ?  100 VAL   A H    1 
ATOM   1975 H HA   A VAL   A 1 100 ? 20.173 -2.665  -12.592 0.72 21.89 ?  100 VAL   A HA   1 
ATOM   1976 H HA   B VAL   A 1 100 ? 19.980 -3.109  -12.551 0.28 23.60 ?  100 VAL   A HA   1 
ATOM   1977 H HB   A VAL   A 1 100 ? 17.698 -2.246  -11.288 0.72 23.78 ?  100 VAL   A HB   1 
ATOM   1978 H HB   B VAL   A 1 100 ? 17.568 -2.573  -11.175 0.28 24.43 ?  100 VAL   A HB   1 
ATOM   1979 H HG11 A VAL   A 1 100 ? 16.777 -3.540  -13.079 0.72 24.82 ?  100 VAL   A HG11 1 
ATOM   1980 H HG11 B VAL   A 1 100 ? 16.554 -3.986  -12.842 0.28 24.72 ?  100 VAL   A HG11 1 
ATOM   1981 H HG12 A VAL   A 1 100 ? 17.221 -2.075  -13.500 0.72 24.82 ?  100 VAL   A HG12 1 
ATOM   1982 H HG12 B VAL   A 1 100 ? 16.922 -2.525  -13.341 0.28 24.72 ?  100 VAL   A HG12 1 
ATOM   1983 H HG13 A VAL   A 1 100 ? 18.146 -3.319  -13.851 0.72 24.82 ?  100 VAL   A HG13 1 
ATOM   1984 H HG13 B VAL   A 1 100 ? 17.861 -3.753  -13.712 0.28 24.72 ?  100 VAL   A HG13 1 
ATOM   1985 H HG21 A VAL   A 1 100 ? 17.611 -4.604  -11.176 0.72 24.84 ?  100 VAL   A HG21 1 
ATOM   1986 H HG21 B VAL   A 1 100 ? 17.487 -4.929  -10.950 0.28 24.95 ?  100 VAL   A HG21 1 
ATOM   1987 H HG22 A VAL   A 1 100 ? 19.101 -4.648  -11.725 0.72 24.84 ?  100 VAL   A HG22 1 
ATOM   1988 H HG22 B VAL   A 1 100 ? 18.948 -4.993  -11.570 0.28 24.95 ?  100 VAL   A HG22 1 
ATOM   1989 H HG23 A VAL   A 1 100 ? 18.795 -4.001  -10.307 0.72 24.84 ?  100 VAL   A HG23 1 
ATOM   1990 H HG23 B VAL   A 1 100 ? 18.710 -4.276  -10.172 0.28 24.95 ?  100 VAL   A HG23 1 
ATOM   1991 N N    A ASN   A 1 101 ? 19.323 0.344   -12.096 0.72 19.39 ?  101 ASN   A N    1 
ATOM   1992 N N    B ASN   A 1 101 ? 19.038 -0.077  -12.383 0.28 21.85 ?  101 ASN   A N    1 
ATOM   1993 C CA   A ASN   A 1 101 ? 19.249 1.631   -12.777 0.72 21.35 ?  101 ASN   A CA   1 
ATOM   1994 C CA   B ASN   A 1 101 ? 18.969 1.147   -13.173 0.28 22.58 ?  101 ASN   A CA   1 
ATOM   1995 C C    A ASN   A 1 101 ? 20.594 2.077   -13.348 0.72 23.42 ?  101 ASN   A C    1 
ATOM   1996 C C    B ASN   A 1 101 ? 20.300 1.437   -13.854 0.28 23.46 ?  101 ASN   A C    1 
ATOM   1997 O O    A ASN   A 1 101 ? 20.641 3.116   -14.020 0.72 25.09 ?  101 ASN   A O    1 
ATOM   1998 O O    B ASN   A 1 101 ? 20.324 1.970   -14.970 0.28 22.83 ?  101 ASN   A O    1 
ATOM   1999 C CB   A ASN   A 1 101 ? 18.606 2.666   -11.850 0.72 21.49 ?  101 ASN   A CB   1 
ATOM   2000 C CB   B ASN   A 1 101 ? 18.543 2.316   -12.282 0.28 22.21 ?  101 ASN   A CB   1 
ATOM   2001 C CG   A ASN   A 1 101 ? 17.217 2.235   -11.390 0.72 21.38 ?  101 ASN   A CG   1 
ATOM   2002 C CG   B ASN   A 1 101 ? 17.254 2.033   -11.530 0.28 21.82 ?  101 ASN   A CG   1 
ATOM   2003 O OD1  A ASN   A 1 101 ? 16.429 1.704   -12.177 0.72 21.65 ?  101 ASN   A OD1  1 
ATOM   2004 O OD1  B ASN   A 1 101 ? 16.302 1.486   -12.088 0.28 21.44 ?  101 ASN   A OD1  1 
ATOM   2005 N ND2  A ASN   A 1 101 ? 16.922 2.431   -10.110 0.72 21.50 ?  101 ASN   A ND2  1 
ATOM   2006 N ND2  B ASN   A 1 101 ? 17.222 2.395   -10.253 0.28 21.99 ?  101 ASN   A ND2  1 
ATOM   2007 H H    A ASN   A 1 101 ? 19.237 0.382   -11.243 0.72 23.28 ?  101 ASN   A H    1 
ATOM   2008 H H    B ASN   A 1 101 ? 18.916 0.035   -11.539 0.28 26.23 ?  101 ASN   A H    1 
ATOM   2009 H HA   A ASN   A 1 101 ? 18.662 1.537   -13.536 0.72 25.63 ?  101 ASN   A HA   1 
ATOM   2010 H HA   B ASN   A 1 101 ? 18.299 1.046   -13.865 0.28 27.10 ?  101 ASN   A HA   1 
ATOM   2011 H HB2  A ASN   A 1 101 ? 19.163 2.790   -11.066 0.72 25.80 ?  101 ASN   A HB2  1 
ATOM   2012 H HB2  B ASN   A 1 101 ? 19.236 2.494   -11.627 0.28 26.66 ?  101 ASN   A HB2  1 
ATOM   2013 H HB3  A ASN   A 1 101 ? 18.521 3.513   -12.328 0.72 25.80 ?  101 ASN   A HB3  1 
ATOM   2014 H HB3  B ASN   A 1 101 ? 18.401 3.105   -12.833 0.28 26.66 ?  101 ASN   A HB3  1 
ATOM   2015 H HD21 A ASN   A 1 101 ? 16.150 2.204   -9.810  0.72 25.80 ?  101 ASN   A HD21 1 
ATOM   2016 H HD21 B ASN   A 1 101 ? 16.513 2.260   -9.786  0.28 26.40 ?  101 ASN   A HD21 1 
ATOM   2017 H HD22 A ASN   A 1 101 ? 17.496 2.802   -9.588  0.72 25.80 ?  101 ASN   A HD22 1 
ATOM   2018 H HD22 B ASN   A 1 101 ? 17.907 2.772   -9.895  0.28 26.40 ?  101 ASN   A HD22 1 
ATOM   2019 N N    A LYS   A 1 102 ? 21.662 1.295   -13.135 0.72 25.42 ?  102 LYS   A N    1 
ATOM   2020 N N    B LYS   A 1 102 ? 21.413 1.093   -13.204 0.28 25.46 ?  102 LYS   A N    1 
ATOM   2021 C CA   A LYS   A 1 102 ? 22.956 1.497   -13.778 0.72 26.54 ?  102 LYS   A CA   1 
ATOM   2022 C CA   B LYS   A 1 102 ? 22.727 1.195   -13.827 0.28 26.74 ?  102 LYS   A CA   1 
ATOM   2023 C C    A LYS   A 1 102 ? 23.285 0.416   -14.798 0.72 26.96 ?  102 LYS   A C    1 
ATOM   2024 C C    B LYS   A 1 102 ? 23.024 0.030   -14.764 0.28 26.68 ?  102 LYS   A C    1 
ATOM   2025 O O    A LYS   A 1 102 ? 24.355 0.477   -15.412 0.72 27.80 ?  102 LYS   A O    1 
ATOM   2026 O O    B LYS   A 1 102 ? 24.091 0.011   -15.385 0.28 26.79 ?  102 LYS   A O    1 
ATOM   2027 C CB   A LYS   A 1 102 ? 24.083 1.530   -12.735 0.72 27.65 ?  102 LYS   A CB   1 
ATOM   2028 C CB   B LYS   A 1 102 ? 23.823 1.272   -12.760 0.28 27.79 ?  102 LYS   A CB   1 
ATOM   2029 C CG   A LYS   A 1 102 ? 23.992 2.649   -11.722 0.72 28.74 ?  102 LYS   A CG   1 
ATOM   2030 C CG   B LYS   A 1 102 ? 23.813 2.552   -11.936 0.28 28.56 ?  102 LYS   A CG   1 
ATOM   2031 C CD   A LYS   A 1 102 ? 25.169 2.581   -10.757 0.72 29.97 ?  102 LYS   A CD   1 
ATOM   2032 C CD   B LYS   A 1 102 ? 24.806 2.489   -10.783 0.28 29.27 ?  102 LYS   A CD   1 
ATOM   2033 C CE   A LYS   A 1 102 ? 25.113 3.687   -9.718  0.72 31.07 ?  102 LYS   A CE   1 
ATOM   2034 C CE   B LYS   A 1 102 ? 24.724 3.735   -9.915  0.28 29.80 ?  102 LYS   A CE   1 
ATOM   2035 N NZ   A LYS   A 1 102 ? 26.223 3.567   -8.727  0.72 31.56 ?  102 LYS   A NZ   1 
ATOM   2036 N NZ   B LYS   A 1 102 ? 25.332 3.530   -8.570  0.28 30.12 ?  102 LYS   A NZ   1 
ATOM   2037 H H    A LYS   A 1 102 ? 21.656 0.605   -12.617 0.72 30.51 ?  102 LYS   A H    1 
ATOM   2038 H H    B LYS   A 1 102 ? 21.428 0.793   -12.396 0.28 30.55 ?  102 LYS   A H    1 
ATOM   2039 H HA   A LYS   A 1 102 ? 22.957 2.340   -14.245 0.72 31.86 ?  102 LYS   A HA   1 
ATOM   2040 H HA   B LYS   A 1 102 ? 22.759 2.019   -14.336 0.28 32.10 ?  102 LYS   A HA   1 
ATOM   2041 H HB2  A LYS   A 1 102 ? 24.079 0.692   -12.247 0.72 33.19 ?  102 LYS   A HB2  1 
ATOM   2042 H HB2  B LYS   A 1 102 ? 23.726 0.519   -12.160 0.28 33.36 ?  102 LYS   A HB2  1 
ATOM   2043 H HB3  A LYS   A 1 102 ? 24.932 1.626   -13.200 0.72 33.19 ?  102 LYS   A HB3  1 
ATOM   2044 H HB3  B LYS   A 1 102 ? 24.682 1.220   -13.201 0.28 33.36 ?  102 LYS   A HB3  1 
ATOM   2045 H HG2  A LYS   A 1 102 ? 24.016 3.503   -12.181 0.72 34.49 ?  102 LYS   A HG2  1 
ATOM   2046 H HG2  B LYS   A 1 102 ? 24.059 3.299   -12.506 0.28 34.28 ?  102 LYS   A HG2  1 
ATOM   2047 H HG3  A LYS   A 1 102 ? 23.170 2.558   -11.215 0.72 34.49 ?  102 LYS   A HG3  1 
ATOM   2048 H HG3  B LYS   A 1 102 ? 22.928 2.690   -11.566 0.28 34.28 ?  102 LYS   A HG3  1 
ATOM   2049 H HD2  A LYS   A 1 102 ? 25.153 1.728   -10.295 0.72 35.97 ?  102 LYS   A HD2  1 
ATOM   2050 H HD2  B LYS   A 1 102 ? 24.611 1.718   -10.228 0.28 35.12 ?  102 LYS   A HD2  1 
ATOM   2051 H HD3  A LYS   A 1 102 ? 25.996 2.675   -11.257 0.72 35.97 ?  102 LYS   A HD3  1 
ATOM   2052 H HD3  B LYS   A 1 102 ? 25.707 2.425   -11.139 0.28 35.12 ?  102 LYS   A HD3  1 
ATOM   2053 H HE2  A LYS   A 1 102 ? 25.193 4.546   -10.163 0.72 37.29 ?  102 LYS   A HE2  1 
ATOM   2054 H HE2  B LYS   A 1 102 ? 25.199 4.459   -10.353 0.28 35.77 ?  102 LYS   A HE2  1 
ATOM   2055 H HE3  A LYS   A 1 102 ? 24.270 3.634   -9.242  0.72 37.29 ?  102 LYS   A HE3  1 
ATOM   2056 H HE3  B LYS   A 1 102 ? 23.792 3.974   -9.791  0.28 35.77 ?  102 LYS   A HE3  1 
ATOM   2057 H HZ1  A LYS   A 1 102 ? 26.169 4.223   -8.130  0.72 37.88 ?  102 LYS   A HZ1  1 
ATOM   2058 H HZ1  B LYS   A 1 102 ? 25.267 4.277   -8.090  0.28 36.15 ?  102 LYS   A HZ1  1 
ATOM   2059 H HZ2  A LYS   A 1 102 ? 26.167 2.785   -8.305  0.72 37.88 ?  102 LYS   A HZ2  1 
ATOM   2060 H HZ2  B LYS   A 1 102 ? 24.910 2.873   -8.143  0.28 36.15 ?  102 LYS   A HZ2  1 
ATOM   2061 H HZ3  A LYS   A 1 102 ? 27.008 3.616   -9.143  0.72 37.88 ?  102 LYS   A HZ3  1 
ATOM   2062 H HZ3  B LYS   A 1 102 ? 26.191 3.315   -8.655  0.28 36.15 ?  102 LYS   A HZ3  1 
ATOM   2063 N N    A GLY   A 1 103 ? 22.418 -0.580  -14.979 0.72 27.66 ?  103 GLY   A N    1 
ATOM   2064 N N    B GLY   A 1 103 ? 22.124 -0.946  -14.865 0.28 26.51 ?  103 GLY   A N    1 
ATOM   2065 C CA   A GLY   A 1 103 ? 22.674 -1.653  -15.922 0.72 27.61 ?  103 GLY   A CA   1 
ATOM   2066 C CA   B GLY   A 1 103 ? 22.305 -2.056  -15.779 0.28 25.79 ?  103 GLY   A CA   1 
ATOM   2067 C C    A GLY   A 1 103 ? 23.540 -2.778  -15.400 0.72 27.88 ?  103 GLY   A C    1 
ATOM   2068 C C    B GLY   A 1 103 ? 23.220 -3.156  -15.291 0.28 25.15 ?  103 GLY   A C    1 
ATOM   2069 O O    A GLY   A 1 103 ? 24.175 -3.473  -16.198 0.72 28.96 ?  103 GLY   A O    1 
ATOM   2070 O O    B GLY   A 1 103 ? 23.606 -4.018  -16.089 0.28 24.95 ?  103 GLY   A O    1 
ATOM   2071 H H    A GLY   A 1 103 ? 21.676 -0.664  -14.558 0.72 33.20 ?  103 GLY   A H    1 
ATOM   2072 H H    B GLY   A 1 103 ? 21.397 -0.982  -14.407 0.28 31.82 ?  103 GLY   A H    1 
ATOM   2073 H HA2  A GLY   A 1 103 ? 21.823 -2.027  -16.217 0.72 33.14 ?  103 GLY   A HA2  1 
ATOM   2074 H HA2  B GLY   A 1 103 ? 21.442 -2.454  -15.957 0.28 30.95 ?  103 GLY   A HA2  1 
ATOM   2075 H HA3  A GLY   A 1 103 ? 23.121 -1.292  -16.702 0.72 33.14 ?  103 GLY   A HA3  1 
ATOM   2076 H HA3  B GLY   A 1 103 ? 22.657 -1.712  -16.617 0.28 30.95 ?  103 GLY   A HA3  1 
ATOM   2077 N N    A GLU   A 1 104 ? 23.586 -2.986  -14.088 0.72 25.95 ?  104 GLU   A N    1 
ATOM   2078 N N    B GLU   A 1 104 ? 23.569 -3.168  -14.009 0.28 24.53 ?  104 GLU   A N    1 
ATOM   2079 C CA   A GLU   A 1 104 ? 24.455 -3.988  -13.487 0.72 24.34 ?  104 GLU   A CA   1 
ATOM   2080 C CA   B GLU   A 1 104 ? 24.520 -4.140  -13.492 0.28 23.83 ?  104 GLU   A CA   1 
ATOM   2081 C C    A GLU   A 1 104 ? 23.757 -5.343  -13.384 0.72 24.45 ?  104 GLU   A C    1 
ATOM   2082 C C    B GLU   A 1 104 ? 23.870 -5.515  -13.340 0.28 23.93 ?  104 GLU   A C    1 
ATOM   2083 O O    A GLU   A 1 104 ? 22.530 -5.430  -13.282 0.72 25.04 ?  104 GLU   A O    1 
ATOM   2084 O O    B GLU   A 1 104 ? 22.676 -5.638  -13.050 0.28 23.67 ?  104 GLU   A O    1 
ATOM   2085 C CB   A GLU   A 1 104 ? 24.946 -3.493  -12.122 0.72 22.21 ?  104 GLU   A CB   1 
ATOM   2086 C CB   B GLU   A 1 104 ? 25.096 -3.646  -12.163 0.28 23.16 ?  104 GLU   A CB   1 
ATOM   2087 C CG   A GLU   A 1 104 ? 25.832 -2.246  -12.274 0.72 21.47 ?  104 GLU   A CG   1 
ATOM   2088 C CG   B GLU   A 1 104 ? 25.877 -2.340  -12.316 0.28 22.95 ?  104 GLU   A CG   1 
ATOM   2089 C CD   A GLU   A 1 104 ? 26.203 -1.530  -10.983 0.72 20.53 ?  104 GLU   A CD   1 
ATOM   2090 C CD   B GLU   A 1 104 ? 26.137 -1.631  -10.999 0.28 22.67 ?  104 GLU   A CD   1 
ATOM   2091 O OE1  A GLU   A 1 104 ? 25.616 -1.813  -9.915  0.72 18.59 ?  104 GLU   A OE1  1 
ATOM   2092 O OE1  B GLU   A 1 104 ? 25.659 -2.106  -9.949  0.28 22.40 ?  104 GLU   A OE1  1 
ATOM   2093 O OE2  A GLU   A 1 104 ? 27.093 -0.649  -11.067 0.72 21.32 -1 104 GLU   A OE2  1 
ATOM   2094 O OE2  B GLU   A 1 104 ? 26.818 -0.584  -11.021 0.28 22.75 -1 104 GLU   A OE2  1 
ATOM   2095 H H    A GLU   A 1 104 ? 23.118 -2.547  -13.519 0.72 31.14 ?  104 GLU   A H    1 
ATOM   2096 H H    B GLU   A 1 104 ? 23.267 -2.619  -13.418 0.28 29.44 ?  104 GLU   A H    1 
ATOM   2097 H HA   A GLU   A 1 104 ? 25.229 -4.104  -14.055 0.72 29.21 ?  104 GLU   A HA   1 
ATOM   2098 H HA   B GLU   A 1 104 ? 25.257 -4.221  -14.118 0.28 28.60 ?  104 GLU   A HA   1 
ATOM   2099 H HB2  A GLU   A 1 104 ? 24.180 -3.265  -11.573 0.72 26.66 ?  104 GLU   A HB2  1 
ATOM   2100 H HB2  B GLU   A 1 104 ? 24.371 -3.490  -11.539 0.28 27.80 ?  104 GLU   A HB2  1 
ATOM   2101 H HB3  A GLU   A 1 104 ? 25.467 -4.193  -11.701 0.72 26.66 ?  104 GLU   A HB3  1 
ATOM   2102 H HB3  B GLU   A 1 104 ? 25.702 -4.317  -11.810 0.28 27.80 ?  104 GLU   A HB3  1 
ATOM   2103 H HG2  A GLU   A 1 104 ? 26.658 -2.511  -12.700 0.72 25.77 ?  104 GLU   A HG2  1 
ATOM   2104 H HG2  B GLU   A 1 104 ? 26.735 -2.532  -12.729 0.28 27.54 ?  104 GLU   A HG2  1 
ATOM   2105 H HG3  A GLU   A 1 104 ? 25.364 -1.606  -12.831 0.72 25.77 ?  104 GLU   A HG3  1 
ATOM   2106 H HG3  B GLU   A 1 104 ? 25.373 -1.732  -12.880 0.28 27.54 ?  104 GLU   A HG3  1 
ATOM   2107 N N    A ASP   A 1 105 ? 24.565 -6.405  -13.403 0.72 25.17 ?  105 ASP   A N    1 
ATOM   2108 N N    B ASP   A 1 105 ? 24.681 -6.552  -13.542 0.28 24.66 ?  105 ASP   A N    1 
ATOM   2109 C CA   A ASP   A 1 105 ? 24.064 -7.768  -13.565 0.72 26.48 ?  105 ASP   A CA   1 
ATOM   2110 C CA   B ASP   A 1 105 ? 24.194 -7.927  -13.584 0.28 25.52 ?  105 ASP   A CA   1 
ATOM   2111 C C    A ASP   A 1 105 ? 23.383 -8.253  -12.287 0.72 23.79 ?  105 ASP   A C    1 
ATOM   2112 C C    B ASP   A 1 105 ? 23.458 -8.277  -12.298 0.28 25.10 ?  105 ASP   A C    1 
ATOM   2113 O O    A ASP   A 1 105 ? 24.024 -8.369  -11.240 0.72 21.38 ?  105 ASP   A O    1 
ATOM   2114 O O    B ASP   A 1 105 ? 24.039 -8.247  -11.210 0.28 24.69 ?  105 ASP   A O    1 
ATOM   2115 C CB   A ASP   A 1 105 ? 25.233 -8.685  -13.922 0.72 30.35 ?  105 ASP   A CB   1 
ATOM   2116 C CB   B ASP   A 1 105 ? 25.386 -8.865  -13.781 0.28 26.70 ?  105 ASP   A CB   1 
ATOM   2117 C CG   A ASP   A 1 105 ? 24.797 -10.101 -14.225 0.72 33.43 ?  105 ASP   A CG   1 
ATOM   2118 C CG   B ASP   A 1 105 ? 24.996 -10.333 -13.772 0.28 27.63 ?  105 ASP   A CG   1 
ATOM   2119 O OD1  A ASP   A 1 105 ? 23.575 -10.346 -14.288 0.72 34.18 ?  105 ASP   A OD1  1 
ATOM   2120 O OD1  B ASP   A 1 105 ? 23.793 -10.644 -13.899 0.28 27.70 ?  105 ASP   A OD1  1 
ATOM   2121 O OD2  A ASP   A 1 105 ? 25.681 -10.967 -14.407 0.72 34.99 -1 105 ASP   A OD2  1 
ATOM   2122 O OD2  B ASP   A 1 105 ? 25.905 -11.181 -13.632 0.28 28.24 -1 105 ASP   A OD2  1 
ATOM   2123 H H    A ASP   A 1 105 ? 25.423 -6.361  -13.325 0.72 30.21 ?  105 ASP   A H    1 
ATOM   2124 H H    B ASP   A 1 105 ? 25.527 -6.480  -13.655 0.28 29.60 ?  105 ASP   A H    1 
ATOM   2125 H HA   A ASP   A 1 105 ? 23.421 -7.799  -14.287 0.72 31.78 ?  105 ASP   A HA   1 
ATOM   2126 H HA   B ASP   A 1 105 ? 23.580 -8.031  -14.328 0.28 30.63 ?  105 ASP   A HA   1 
ATOM   2127 H HB2  A ASP   A 1 105 ? 25.674 -8.344  -14.717 0.72 36.42 ?  105 ASP   A HB2  1 
ATOM   2128 H HB2  B ASP   A 1 105 ? 25.801 -8.666  -14.634 0.28 32.04 ?  105 ASP   A HB2  1 
ATOM   2129 H HB3  A ASP   A 1 105 ? 25.861 -8.707  -13.181 0.72 36.42 ?  105 ASP   A HB3  1 
ATOM   2130 H HB3  B ASP   A 1 105 ? 26.018 -8.723  -13.061 0.28 32.04 ?  105 ASP   A HB3  1 
ATOM   2131 N N    A ILE   A 1 106 ? 22.091 -8.579  -12.386 0.72 23.34 ?  106 ILE   A N    1 
ATOM   2132 N N    B ILE   A 1 106 ? 22.174 -8.623  -12.429 0.28 25.02 ?  106 ILE   A N    1 
ATOM   2133 C CA   A ILE   A 1 106 ? 21.326 -9.009  -11.221 0.72 22.73 ?  106 ILE   A CA   1 
ATOM   2134 C CA   B ILE   A 1 106 ? 21.381 -8.979  -11.260 0.28 24.97 ?  106 ILE   A CA   1 
ATOM   2135 C C    A ILE   A 1 106 ? 21.871 -10.296 -10.626 0.72 21.50 ?  106 ILE   A C    1 
ATOM   2136 C C    B ILE   A 1 106 ? 21.865 -10.275 -10.626 0.28 24.46 ?  106 ILE   A C    1 
ATOM   2137 O O    A ILE   A 1 106 ? 21.677 -10.549 -9.434  0.72 20.83 ?  106 ILE   A O    1 
ATOM   2138 O O    B ILE   A 1 106 ? 21.615 -10.508 -9.438  0.28 24.14 ?  106 ILE   A O    1 
ATOM   2139 C CB   A ILE   A 1 106 ? 19.821 -9.119  -11.562 0.72 24.41 ?  106 ILE   A CB   1 
ATOM   2140 C CB   B ILE   A 1 106 ? 19.878 -9.027  -11.605 0.28 25.72 ?  106 ILE   A CB   1 
ATOM   2141 C CG1  A ILE   A 1 106 ? 18.980 -9.242  -10.289 0.72 24.98 ?  106 ILE   A CG1  1 
ATOM   2142 C CG1  B ILE   A 1 106 ? 19.031 -9.025  -10.330 0.28 26.10 ?  106 ILE   A CG1  1 
ATOM   2143 C CG2  A ILE   A 1 106 ? 19.561 -10.308 -12.469 0.72 25.35 ?  106 ILE   A CG2  1 
ATOM   2144 C CG2  B ILE   A 1 106 ? 19.557 -10.259 -12.435 0.28 25.97 ?  106 ILE   A CG2  1 
ATOM   2145 C CD1  A ILE   A 1 106 ? 19.053 -8.031  -9.385  0.72 25.27 ?  106 ILE   A CD1  1 
ATOM   2146 C CD1  B ILE   A 1 106 ? 19.321 -7.863  -9.405  0.28 26.28 ?  106 ILE   A CD1  1 
ATOM   2147 H H    A ILE   A 1 106 ? 21.644 -8.558  -13.115 0.72 28.01 ?  106 ILE   A H    1 
ATOM   2148 H H    B ILE   A 1 106 ? 21.748 -8.649  -13.172 0.28 30.03 ?  106 ILE   A H    1 
ATOM   2149 H HA   A ILE   A 1 106 ? 21.423 -8.335  -10.539 0.72 27.29 ?  106 ILE   A HA   1 
ATOM   2150 H HA   B ILE   A 1 106 ? 21.511 -8.283  -10.603 0.28 29.96 ?  106 ILE   A HA   1 
ATOM   2151 H HB   A ILE   A 1 106 ? 19.558 -8.312  -12.029 0.72 29.29 ?  106 ILE   A HB   1 
ATOM   2152 H HB   B ILE   A 1 106 ? 19.653 -8.239  -12.125 0.28 30.87 ?  106 ILE   A HB   1 
ATOM   2153 H HG12 A ILE   A 1 106 ? 18.052 -9.363  -10.539 0.72 29.98 ?  106 ILE   A HG12 1 
ATOM   2154 H HG12 B ILE   A 1 106 ? 18.093 -8.977  -10.577 0.28 31.32 ?  106 ILE   A HG12 1 
ATOM   2155 H HG13 A ILE   A 1 106 ? 19.286 -10.008 -9.779  0.72 29.98 ?  106 ILE   A HG13 1 
ATOM   2156 H HG13 B ILE   A 1 106 ? 19.200 -9.844  -9.840  0.28 31.32 ?  106 ILE   A HG13 1 
ATOM   2157 H HG21 A ILE   A 1 106 ? 18.664 -10.235 -12.827 0.72 30.42 ?  106 ILE   A HG21 1 
ATOM   2158 H HG21 B ILE   A 1 106 ? 18.673 -10.157 -12.821 0.28 31.17 ?  106 ILE   A HG21 1 
ATOM   2159 H HG22 A ILE   A 1 106 ? 20.210 -10.300 -13.188 0.72 30.42 ?  106 ILE   A HG22 1 
ATOM   2160 H HG22 B ILE   A 1 106 ? 20.219 -10.343 -13.138 0.28 31.17 ?  106 ILE   A HG22 1 
ATOM   2161 H HG23 A ILE   A 1 106 ? 19.648 -11.123 -11.951 0.72 30.42 ?  106 ILE   A HG23 1 
ATOM   2162 H HG23 B ILE   A 1 106 ? 19.580 -11.041 -11.862 0.28 31.17 ?  106 ILE   A HG23 1 
ATOM   2163 H HD11 A ILE   A 1 106 ? 18.335 -8.077  -8.737  0.72 30.33 ?  106 ILE   A HD11 1 
ATOM   2164 H HD11 B ILE   A 1 106 ? 18.563 -7.732  -8.819  0.28 31.54 ?  106 ILE   A HD11 1 
ATOM   2165 H HD12 A ILE   A 1 106 ? 19.910 -8.026  -8.928  0.72 30.33 ?  106 ILE   A HD12 1 
ATOM   2166 H HD12 B ILE   A 1 106 ? 20.113 -8.067  -8.883  0.28 31.54 ?  106 ILE   A HD12 1 
ATOM   2167 H HD13 A ILE   A 1 106 ? 18.961 -7.229  -9.924  0.72 30.33 ?  106 ILE   A HD13 1 
ATOM   2168 H HD13 B ILE   A 1 106 ? 19.471 -7.067  -9.939  0.28 31.54 ?  106 ILE   A HD13 1 
ATOM   2169 N N    A GLN   A 1 107 ? 22.571 -11.112 -11.426 0.72 22.39 ?  107 GLN   A N    1 
ATOM   2170 N N    B GLN   A 1 107 ? 22.563 -11.126 -11.384 0.28 24.52 ?  107 GLN   A N    1 
ATOM   2171 C CA   A GLN   A 1 107 ? 23.195 -12.322 -10.899 0.72 25.21 ?  107 GLN   A CA   1 
ATOM   2172 C CA   B GLN   A 1 107 ? 23.134 -12.334 -10.802 0.28 24.84 ?  107 GLN   A CA   1 
ATOM   2173 C C    A GLN   A 1 107 ? 24.166 -12.010 -9.769  0.72 23.09 ?  107 GLN   A C    1 
ATOM   2174 C C    B GLN   A 1 107 ? 24.175 -12.015 -9.739  0.28 22.50 ?  107 GLN   A C    1 
ATOM   2175 O O    A GLN   A 1 107 ? 24.385 -12.859 -8.899  0.72 24.90 ?  107 GLN   A O    1 
ATOM   2176 O O    B GLN   A 1 107 ? 24.474 -12.873 -8.901  0.28 23.36 ?  107 GLN   A O    1 
ATOM   2177 C CB   A GLN   A 1 107 ? 23.913 -13.074 -12.027 0.72 29.68 ?  107 GLN   A CB   1 
ATOM   2178 C CB   B GLN   A 1 107 ? 23.736 -13.219 -11.897 0.28 27.40 ?  107 GLN   A CB   1 
ATOM   2179 C CG   A GLN   A 1 107 ? 23.050 -13.312 -13.262 0.72 34.49 ?  107 GLN   A CG   1 
ATOM   2180 C CG   B GLN   A 1 107 ? 22.740 -13.617 -12.977 0.28 29.99 ?  107 GLN   A CG   1 
ATOM   2181 C CD   A GLN   A 1 107 ? 21.801 -14.110 -12.954 0.72 38.52 ?  107 GLN   A CD   1 
ATOM   2182 C CD   B GLN   A 1 107 ? 21.457 -14.190 -12.403 0.28 32.28 ?  107 GLN   A CD   1 
ATOM   2183 O OE1  A GLN   A 1 107 ? 21.864 -15.156 -12.307 0.72 40.04 ?  107 GLN   A OE1  1 
ATOM   2184 O OE1  B GLN   A 1 107 ? 21.484 -15.116 -11.593 0.28 33.09 ?  107 GLN   A OE1  1 
ATOM   2185 N NE2  A GLN   A 1 107 ? 20.654 -13.616 -13.411 0.72 39.97 ?  107 GLN   A NE2  1 
ATOM   2186 N NE2  B GLN   A 1 107 ? 20.325 -13.629 -12.812 0.28 33.12 ?  107 GLN   A NE2  1 
ATOM   2187 H H    A GLN   A 1 107 ? 22.708 -10.982 -12.263 0.72 26.87 ?  107 GLN   A H    1 
ATOM   2188 H H    B GLN   A 1 107 ? 22.715 -11.026 -12.224 0.28 29.43 ?  107 GLN   A H    1 
ATOM   2189 H HA   A GLN   A 1 107 ? 22.514 -12.910 -10.545 0.72 30.26 ?  107 GLN   A HA   1 
ATOM   2190 H HA   B GLN   A 1 107 ? 22.428 -12.836 -10.371 0.28 29.82 ?  107 GLN   A HA   1 
ATOM   2191 H HB2  A GLN   A 1 107 ? 24.689 -12.564 -12.308 0.72 35.62 ?  107 GLN   A HB2  1 
ATOM   2192 H HB2  B GLN   A 1 107 ? 24.462 -12.741 -12.328 0.28 32.89 ?  107 GLN   A HB2  1 
ATOM   2193 H HB3  A GLN   A 1 107 ? 24.197 -13.945 -11.701 0.72 35.62 ?  107 GLN   A HB3  1 
ATOM   2194 H HB3  B GLN   A 1 107 ? 24.074 -14.035 -11.495 0.28 32.89 ?  107 GLN   A HB3  1 
ATOM   2195 H HG2  A GLN   A 1 107 ? 22.776 -12.459 -13.633 0.72 41.39 ?  107 GLN   A HG2  1 
ATOM   2196 H HG2  B GLN   A 1 107 ? 22.513 -12.832 -13.500 0.28 35.99 ?  107 GLN   A HG2  1 
ATOM   2197 H HG3  A GLN   A 1 107 ? 23.565 -13.805 -13.918 0.72 41.39 ?  107 GLN   A HG3  1 
ATOM   2198 H HG3  B GLN   A 1 107 ? 23.142 -14.291 -13.547 0.28 35.99 ?  107 GLN   A HG3  1 
ATOM   2199 H HE21 A GLN   A 1 107 ? 20.649 -12.882 -13.858 0.72 47.97 ?  107 GLN   A HE21 1 
ATOM   2200 H HE21 B GLN   A 1 107 ? 20.346 -12.981 -13.377 0.28 39.75 ?  107 GLN   A HE21 1 
ATOM   2201 H HE22 A GLN   A 1 107 ? 19.916 -14.032 -13.260 0.72 47.97 ?  107 GLN   A HE22 1 
ATOM   2202 H HE22 B GLN   A 1 107 ? 19.572 -13.916 -12.513 0.28 39.75 ?  107 GLN   A HE22 1 
ATOM   2203 N N    . LEU   A 1 108 ? 24.724 -10.798 -9.741  1.00 19.53 ?  108 LEU   A N    1 
ATOM   2204 C CA   . LEU   A 1 108 ? 25.645 -10.401 -8.690  1.00 15.91 ?  108 LEU   A CA   1 
ATOM   2205 C C    . LEU   A 1 108 ? 24.948 -10.238 -7.349  1.00 14.01 ?  108 LEU   A C    1 
ATOM   2206 O O    . LEU   A 1 108 ? 25.631 -10.075 -6.336  1.00 14.18 ?  108 LEU   A O    1 
ATOM   2207 C CB   . LEU   A 1 108 ? 26.369 -9.106  -9.079  1.00 15.56 ?  108 LEU   A CB   1 
ATOM   2208 C CG   . LEU   A 1 108 ? 27.354 -9.298  -10.233 1.00 17.24 ?  108 LEU   A CG   1 
ATOM   2209 C CD1  . LEU   A 1 108 ? 27.825 -7.961  -10.776 1.00 18.09 ?  108 LEU   A CD1  1 
ATOM   2210 C CD2  . LEU   A 1 108 ? 28.545 -10.136 -9.787  1.00 19.28 ?  108 LEU   A CD2  1 
ATOM   2211 H H    A LEU   A 1 108 ? 24.571 -10.188 -10.320 0.72 23.44 ?  108 LEU   A H    1 
ATOM   2212 H H    B LEU   A 1 108 ? 24.581 -10.200 -10.335 0.28 23.44 ?  108 LEU   A H    1 
ATOM   2213 H HA   . LEU   A 1 108 ? 26.312 -11.094 -8.579  1.00 19.09 ?  108 LEU   A HA   1 
ATOM   2214 H HB2  . LEU   A 1 108 ? 25.711 -8.449  -9.356  1.00 18.67 ?  108 LEU   A HB2  1 
ATOM   2215 H HB3  . LEU   A 1 108 ? 26.864 -8.778  -8.314  1.00 18.67 ?  108 LEU   A HB3  1 
ATOM   2216 H HG   . LEU   A 1 108 ? 26.910 -9.774  -10.953 1.00 20.70 ?  108 LEU   A HG   1 
ATOM   2217 H HD11 . LEU   A 1 108 ? 28.427 -8.118  -11.524 1.00 21.71 ?  108 LEU   A HD11 1 
ATOM   2218 H HD12 . LEU   A 1 108 ? 27.058 -7.451  -11.072 1.00 21.71 ?  108 LEU   A HD12 1 
ATOM   2219 H HD13 . LEU   A 1 108 ? 28.293 -7.482  -10.074 1.00 21.71 ?  108 LEU   A HD13 1 
ATOM   2220 H HD21 . LEU   A 1 108 ? 29.234 -10.086 -10.463 1.00 23.14 ?  108 LEU   A HD21 1 
ATOM   2221 H HD22 . LEU   A 1 108 ? 28.875 -9.784  -8.946  1.00 23.14 ?  108 LEU   A HD22 1 
ATOM   2222 H HD23 . LEU   A 1 108 ? 28.256 -11.055 -9.670  1.00 23.14 ?  108 LEU   A HD23 1 
ATOM   2223 N N    . LEU   A 1 109 ? 23.615 -10.289 -7.309  1.00 13.35 ?  109 LEU   A N    1 
ATOM   2224 C CA   . LEU   A 1 109 ? 22.920 -10.158 -6.036  1.00 12.38 ?  109 LEU   A CA   1 
ATOM   2225 C C    . LEU   A 1 109 ? 23.262 -11.311 -5.098  1.00 11.93 ?  109 LEU   A C    1 
ATOM   2226 O O    . LEU   A 1 109 ? 23.391 -11.110 -3.885  1.00 12.18 ?  109 LEU   A O    1 
ATOM   2227 C CB   . LEU   A 1 109 ? 21.413 -10.071 -6.279  1.00 12.99 ?  109 LEU   A CB   1 
ATOM   2228 C CG   . LEU   A 1 109 ? 20.529 -9.788  -5.067  1.00 13.22 ?  109 LEU   A CG   1 
ATOM   2229 C CD1  . LEU   A 1 109 ? 21.002 -8.535  -4.336  1.00 13.34 ?  109 LEU   A CD1  1 
ATOM   2230 C CD2  . LEU   A 1 109 ? 19.071 -9.639  -5.489  1.00 14.32 ?  109 LEU   A CD2  1 
ATOM   2231 H H    . LEU   A 1 109 ? 23.100 -10.395 -7.987  1.00 16.02 ?  109 LEU   A H    1 
ATOM   2232 H HA   . LEU   A 1 109 ? 23.205 -9.336  -5.606  1.00 14.86 ?  109 LEU   A HA   1 
ATOM   2233 H HB2  . LEU   A 1 109 ? 21.254 -9.358  -6.919  1.00 15.59 ?  109 LEU   A HB2  1 
ATOM   2234 H HB3  . LEU   A 1 109 ? 21.117 -10.911 -6.655  1.00 15.59 ?  109 LEU   A HB3  1 
ATOM   2235 H HG   . LEU   A 1 109 ? 20.586 -10.531 -4.451  1.00 15.87 ?  109 LEU   A HG   1 
ATOM   2236 H HD11 . LEU   A 1 109 ? 20.324 -8.264  -3.699  1.00 16.01 ?  109 LEU   A HD11 1 
ATOM   2237 H HD12 . LEU   A 1 109 ? 21.832 -8.731  -3.874  1.00 16.01 ?  109 LEU   A HD12 1 
ATOM   2238 H HD13 . LEU   A 1 109 ? 21.145 -7.824  -4.985  1.00 16.01 ?  109 LEU   A HD13 1 
ATOM   2239 H HD21 . LEU   A 1 109 ? 18.544 -9.365  -4.721  1.00 17.19 ?  109 LEU   A HD21 1 
ATOM   2240 H HD22 . LEU   A 1 109 ? 19.007 -8.972  -6.189  1.00 17.19 ?  109 LEU   A HD22 1 
ATOM   2241 H HD23 . LEU   A 1 109 ? 18.749 -10.495 -5.819  1.00 17.19 ?  109 LEU   A HD23 1 
ATOM   2242 N N    . LYS   A 1 110 ? 23.412 -12.527 -5.632  1.00 11.43 ?  110 LYS   A N    1 
ATOM   2243 C CA   . LYS   A 1 110 ? 23.786 -13.646 -4.773  1.00 11.73 ?  110 LYS   A CA   1 
ATOM   2244 C C    . LYS   A 1 110 ? 25.169 -13.430 -4.169  1.00 11.16 ?  110 LYS   A C    1 
ATOM   2245 O O    . LYS   A 1 110 ? 25.362 -13.628 -2.968  1.00 11.32 ?  110 LYS   A O    1 
ATOM   2246 C CB   . LYS   A 1 110 ? 23.699 -14.972 -5.531  1.00 12.62 ?  110 LYS   A CB   1 
ATOM   2247 C CG   . LYS   A 1 110 ? 23.907 -16.177 -4.619  1.00 12.79 ?  110 LYS   A CG   1 
ATOM   2248 C CD   . LYS   A 1 110 ? 23.658 -17.508 -5.323  1.00 13.40 ?  110 LYS   A CD   1 
ATOM   2249 C CE   . LYS   A 1 110 ? 23.772 -18.684 -4.365  1.00 14.42 ?  110 LYS   A CE   1 
ATOM   2250 N NZ   . LYS   A 1 110 ? 22.593 -18.803 -3.463  1.00 14.73 ?  110 LYS   A NZ   1 
ATOM   2251 H H    . LYS   A 1 110 ? 23.307 -12.724 -6.460  1.00 13.73 ?  110 LYS   A H    1 
ATOM   2252 H HA   . LYS   A 1 110 ? 23.150 -13.693 -4.038  1.00 14.08 ?  110 LYS   A HA   1 
ATOM   2253 H HB2  . LYS   A 1 110 ? 22.820 -15.052 -5.934  1.00 15.15 ?  110 LYS   A HB2  1 
ATOM   2254 H HB3  . LYS   A 1 110 ? 24.384 -14.993 -6.216  1.00 15.15 ?  110 LYS   A HB3  1 
ATOM   2255 H HG2  . LYS   A 1 110 ? 24.823 -16.173 -4.294  1.00 15.35 ?  110 LYS   A HG2  1 
ATOM   2256 H HG3  . LYS   A 1 110 ? 23.294 -16.114 -3.869  1.00 15.35 ?  110 LYS   A HG3  1 
ATOM   2257 H HD2  . LYS   A 1 110 ? 22.769 -17.510 -5.700  1.00 16.09 ?  110 LYS   A HD2  1 
ATOM   2258 H HD3  . LYS   A 1 110 ? 24.323 -17.626 -6.021  1.00 16.09 ?  110 LYS   A HD3  1 
ATOM   2259 H HE2  . LYS   A 1 110 ? 23.842 -19.507 -4.873  1.00 17.31 ?  110 LYS   A HE2  1 
ATOM   2260 H HE3  . LYS   A 1 110 ? 24.560 -18.571 -3.807  1.00 17.31 ?  110 LYS   A HE3  1 
ATOM   2261 H HZ1  . LYS   A 1 110 ? 22.687 -19.497 -2.917  1.00 17.68 ?  110 LYS   A HZ1  1 
ATOM   2262 H HZ2  . LYS   A 1 110 ? 22.504 -18.061 -2.974  1.00 17.68 ?  110 LYS   A HZ2  1 
ATOM   2263 H HZ3  . LYS   A 1 110 ? 21.849 -18.915 -3.945  1.00 17.68 ?  110 LYS   A HZ3  1 
ATOM   2264 N N    . SER   A 1 111 ? 26.129 -12.984 -4.980  1.00 11.45 ?  111 SER   A N    1 
ATOM   2265 C CA   . SER   A 1 111 ? 27.456 -12.676 -4.458  1.00 11.48 ?  111 SER   A CA   1 
ATOM   2266 C C    . SER   A 1 111 ? 27.388 -11.631 -3.352  1.00 10.97 ?  111 SER   A C    1 
ATOM   2267 O O    . SER   A 1 111 ? 28.087 -11.735 -2.340  1.00 11.58 ?  111 SER   A O    1 
ATOM   2268 C CB   . SER   A 1 111 ? 28.352 -12.186 -5.592  1.00 12.80 ?  111 SER   A CB   1 
ATOM   2269 O OG   . SER   A 1 111 ? 28.459 -13.180 -6.599  1.00 15.09 ?  111 SER   A OG   1 
ATOM   2270 H H    . SER   A 1 111 ? 26.032 -12.853 -5.822  1.00 13.75 ?  111 SER   A H    1 
ATOM   2271 H HA   . SER   A 1 111 ? 27.847 -13.485 -4.090  1.00 13.78 ?  111 SER   A HA   1 
ATOM   2272 H HB2  . SER   A 1 111 ? 27.961 -11.390 -5.983  1.00 15.37 ?  111 SER   A HB2  1 
ATOM   2273 H HB3  . SER   A 1 111 ? 29.231 -11.985 -5.237  1.00 15.37 ?  111 SER   A HB3  1 
ATOM   2274 H HG   . SER   A 1 111 ? 28.971 -12.900 -7.216  1.00 18.11 ?  111 SER   A HG   1 
ATOM   2275 N N    . ALA   A 1 112 ? 26.549 -10.610 -3.533  1.00 11.29 ?  112 ALA   A N    1 
ATOM   2276 C CA   . ALA   A 1 112 ? 26.410 -9.574  -2.514  1.00 11.36 ?  112 ALA   A CA   1 
ATOM   2277 C C    . ALA   A 1 112 ? 25.928 -10.172 -1.193  1.00 11.29 ?  112 ALA   A C    1 
ATOM   2278 O O    . ALA   A 1 112 ? 26.467 -9.869  -0.122  1.00 11.39 ?  112 ALA   A O    1 
ATOM   2279 C CB   . ALA   A 1 112 ? 25.454 -8.484  -3.005  1.00 11.98 ?  112 ALA   A CB   1 
ATOM   2280 H H    . ALA   A 1 112 ? 26.057 -10.494 -4.226  1.00 13.55 ?  112 ALA   A H    1 
ATOM   2281 H HA   . ALA   A 1 112 ? 27.273 -9.159  -2.356  1.00 13.64 ?  112 ALA   A HA   1 
ATOM   2282 H HB1  . ALA   A 1 112 ? 25.384 -7.787  -2.325  1.00 14.38 ?  112 ALA   A HB1  1 
ATOM   2283 H HB2  . ALA   A 1 112 ? 25.801 -8.099  -3.826  1.00 14.38 ?  112 ALA   A HB2  1 
ATOM   2284 H HB3  . ALA   A 1 112 ? 24.579 -8.871  -3.165  1.00 14.38 ?  112 ALA   A HB3  1 
ATOM   2285 N N    . TYR   A 1 113 ? 24.890 -11.012 -1.246  1.00 11.27 ?  113 TYR   A N    1 
ATOM   2286 C CA   . TYR   A 1 113 ? 24.375 -11.617 -0.020  1.00 10.94 ?  113 TYR   A CA   1 
ATOM   2287 C C    . TYR   A 1 113 ? 25.377 -12.569 0.632   1.00 10.42 ?  113 TYR   A C    1 
ATOM   2288 O O    . TYR   A 1 113 ? 25.334 -12.751 1.851   1.00 11.22 ?  113 TYR   A O    1 
ATOM   2289 C CB   . TYR   A 1 113 ? 23.051 -12.340 -0.296  1.00 11.56 ?  113 TYR   A CB   1 
ATOM   2290 C CG   . TYR   A 1 113 ? 21.832 -11.447 -0.209  1.00 11.05 ?  113 TYR   A CG   1 
ATOM   2291 C CD1  . TYR   A 1 113 ? 21.473 -10.857 0.993   1.00 11.09 ?  113 TYR   A CD1  1 
ATOM   2292 C CD2  . TYR   A 1 113 ? 21.023 -11.223 -1.313  1.00 11.15 ?  113 TYR   A CD2  1 
ATOM   2293 C CE1  . TYR   A 1 113 ? 20.342 -10.062 1.095   1.00 11.44 ?  113 TYR   A CE1  1 
ATOM   2294 C CE2  . TYR   A 1 113 ? 19.873 -10.420 -1.218  1.00 11.37 ?  113 TYR   A CE2  1 
ATOM   2295 C CZ   . TYR   A 1 113 ? 19.550 -9.850  -0.011  1.00 11.42 ?  113 TYR   A CZ   1 
ATOM   2296 O OH   . TYR   A 1 113 ? 18.426 -9.060  0.117   1.00 12.02 ?  113 TYR   A OH   1 
ATOM   2297 H H    . TYR   A 1 113 ? 24.473 -11.234 -1.966  1.00 13.53 ?  113 TYR   A H    1 
ATOM   2298 H HA   . TYR   A 1 113 ? 24.196 -10.911 0.615   1.00 13.14 ?  113 TYR   A HA   1 
ATOM   2299 H HB2  . TYR   A 1 113 ? 23.078 -12.709 -1.191  1.00 13.88 ?  113 TYR   A HB2  1 
ATOM   2300 H HB3  . TYR   A 1 113 ? 22.945 -13.048 0.353   1.00 13.88 ?  113 TYR   A HB3  1 
ATOM   2301 H HD1  . TYR   A 1 113 ? 22.002 -11.001 1.747   1.00 13.31 ?  113 TYR   A HD1  1 
ATOM   2302 H HD2  . TYR   A 1 113 ? 21.238 -11.617 -2.127  1.00 13.39 ?  113 TYR   A HD2  1 
ATOM   2303 H HE1  . TYR   A 1 113 ? 20.121 -9.673  1.910   1.00 13.73 ?  113 TYR   A HE1  1 
ATOM   2304 H HE2  . TYR   A 1 113 ? 19.334 -10.274 -1.965  1.00 13.65 ?  113 TYR   A HE2  1 
ATOM   2305 H HH   . TYR   A 1 113 ? 18.030 -9.009  -0.627  1.00 14.43 ?  113 TYR   A HH   1 
ATOM   2306 N N    . GLU   A 1 114 ? 26.277 -13.184 -0.148  1.00 11.02 ?  114 GLU   A N    1 
ATOM   2307 C CA   . GLU   A 1 114 ? 27.265 -14.084 0.445   1.00 11.06 ?  114 GLU   A CA   1 
ATOM   2308 C C    . GLU   A 1 114 ? 28.117 -13.376 1.495   1.00 11.24 ?  114 GLU   A C    1 
ATOM   2309 O O    . GLU   A 1 114 ? 28.596 -14.015 2.442   1.00 11.33 ?  114 GLU   A O    1 
ATOM   2310 C CB   . GLU   A 1 114 ? 28.135 -14.724 -0.645  1.00 11.22 ?  114 GLU   A CB   1 
ATOM   2311 C CG   . GLU   A 1 114 ? 27.371 -15.771 -1.437  1.00 11.45 ?  114 GLU   A CG   1 
ATOM   2312 C CD   . GLU   A 1 114 ? 28.086 -16.311 -2.666  1.00 12.13 ?  114 GLU   A CD   1 
ATOM   2313 O OE1  . GLU   A 1 114 ? 29.047 -15.689 -3.153  1.00 12.28 ?  114 GLU   A OE1  1 
ATOM   2314 O OE2  . GLU   A 1 114 ? 27.643 -17.373 -3.159  1.00 13.25 -1 114 GLU   A OE2  1 
ATOM   2315 H H    . GLU   A 1 114 ? 26.341 -13.084 -1.011  1.00 13.22 ?  114 GLU   A H    1 
ATOM   2316 H HA   . GLU   A 1 114 ? 26.792 -14.795 0.886   1.00 13.28 ?  114 GLU   A HA   1 
ATOM   2317 H HB2  . GLU   A 1 114 ? 28.432 -14.041 -1.271  1.00 13.47 ?  114 GLU   A HB2  1 
ATOM   2318 H HB3  . GLU   A 1 114 ? 28.896 -15.159 -0.239  1.00 13.47 ?  114 GLU   A HB3  1 
ATOM   2319 H HG2  . GLU   A 1 114 ? 27.184 -16.524 -0.855  1.00 13.75 ?  114 GLU   A HG2  1 
ATOM   2320 H HG3  . GLU   A 1 114 ? 26.528 -15.383 -1.736  1.00 13.75 ?  114 GLU   A HG3  1 
ATOM   2321 N N    . ASN   A 1 115 ? 28.309 -12.058 1.362   1.00 10.89 ?  115 ASN   A N    1 
ATOM   2322 C CA   . ASN   A 1 115 ? 29.073 -11.330 2.372   1.00 11.53 ?  115 ASN   A CA   1 
ATOM   2323 C C    . ASN   A 1 115 ? 28.453 -11.460 3.760   1.00 11.27 ?  115 ASN   A C    1 
ATOM   2324 O O    . ASN   A 1 115 ? 29.166 -11.388 4.770   1.00 11.50 ?  115 ASN   A O    1 
ATOM   2325 C CB   . ASN   A 1 115 ? 29.188 -9.852  2.002   1.00 11.55 ?  115 ASN   A CB   1 
ATOM   2326 C CG   . ASN   A 1 115 ? 29.977 -9.635  0.737   1.00 12.47 ?  115 ASN   A CG   1 
ATOM   2327 O OD1  . ASN   A 1 115 ? 31.196 -9.742  0.747   1.00 15.76 ?  115 ASN   A OD1  1 
ATOM   2328 N ND2  . ASN   A 1 115 ? 29.298 -9.333  -0.357  1.00 12.04 ?  115 ASN   A ND2  1 
ATOM   2329 H H    . ASN   A 1 115 ? 28.008 -11.569 0.719   1.00 13.07 ?  115 ASN   A H    1 
ATOM   2330 H HA   . ASN   A 1 115 ? 29.967 -11.698 2.414   1.00 13.84 ?  115 ASN   A HA   1 
ATOM   2331 H HB2  . ASN   A 1 115 ? 28.299 -9.486  1.878   1.00 13.87 ?  115 ASN   A HB2  1 
ATOM   2332 H HB3  . ASN   A 1 115 ? 29.639 -9.381  2.725   1.00 13.87 ?  115 ASN   A HB3  1 
ATOM   2333 H HD21 . ASN   A 1 115 ? 29.710 -9.203  -1.100  1.00 14.45 ?  115 ASN   A HD21 1 
ATOM   2334 H HD22 . ASN   A 1 115 ? 28.437 -9.290  -0.332  1.00 14.45 ?  115 ASN   A HD22 1 
ATOM   2335 N N    . PHE   A 1 116 ? 27.127 -11.619 3.840   1.00 11.11 ?  116 PHE   A N    1 
ATOM   2336 C CA   . PHE   A 1 116 ? 26.480 -11.723 5.147   1.00 10.93 ?  116 PHE   A CA   1 
ATOM   2337 C C    . PHE   A 1 116 ? 26.959 -12.956 5.913   1.00 11.10 ?  116 PHE   A C    1 
ATOM   2338 O O    . PHE   A 1 116 ? 26.878 -12.981 7.143   1.00 11.82 ?  116 PHE   A O    1 
ATOM   2339 C CB   . PHE   A 1 116 ? 24.949 -11.850 5.013   1.00 11.27 ?  116 PHE   A CB   1 
ATOM   2340 C CG   . PHE   A 1 116 ? 24.193 -10.600 4.547   1.00 10.76 ?  116 PHE   A CG   1 
ATOM   2341 C CD1  . PHE   A 1 116 ? 24.773 -9.574  3.811   1.00 11.06 ?  116 PHE   A CD1  1 
ATOM   2342 C CD2  . PHE   A 1 116 ? 22.835 -10.492 4.859   1.00 11.60 ?  116 PHE   A CD2  1 
ATOM   2343 C CE1  . PHE   A 1 116 ? 24.010 -8.495  3.389   1.00 11.31 ?  116 PHE   A CE1  1 
ATOM   2344 C CE2  . PHE   A 1 116 ? 22.072 -9.424  4.448   1.00 11.61 ?  116 PHE   A CE2  1 
ATOM   2345 C CZ   . PHE   A 1 116 ? 22.648 -8.421  3.715   1.00 11.17 ?  116 PHE   A CZ   1 
ATOM   2346 H H    . PHE   A 1 116 ? 26.590 -11.661 3.166   1.00 13.33 ?  116 PHE   A H    1 
ATOM   2347 H HA   . PHE   A 1 116 ? 26.675 -10.931 5.673   1.00 13.13 ?  116 PHE   A HA   1 
ATOM   2348 H HB2  . PHE   A 1 116 ? 24.760 -12.556 4.373   1.00 13.53 ?  116 PHE   A HB2  1 
ATOM   2349 H HB3  . PHE   A 1 116 ? 24.590 -12.100 5.878   1.00 13.53 ?  116 PHE   A HB3  1 
ATOM   2350 H HD1  . PHE   A 1 116 ? 25.670 -9.632  3.581   1.00 13.28 ?  116 PHE   A HD1  1 
ATOM   2351 H HD2  . PHE   A 1 116 ? 22.429 -11.182 5.344   1.00 13.92 ?  116 PHE   A HD2  1 
ATOM   2352 H HE1  . PHE   A 1 116 ? 24.405 -7.811  2.900   1.00 13.58 ?  116 PHE   A HE1  1 
ATOM   2353 H HE2  . PHE   A 1 116 ? 21.170 -9.387  4.676   1.00 13.94 ?  116 PHE   A HE2  1 
ATOM   2354 H HZ   . PHE   A 1 116 ? 22.142 -7.689  3.451   1.00 13.41 ?  116 PHE   A HZ   1 
ATOM   2355 N N    . ASN   A 1 117 ? 27.386 -14.007 5.205   1.00 11.42 ?  117 ASN   A N    1 
ATOM   2356 C CA   . ASN   A 1 117 ? 27.756 -15.252 5.873   1.00 11.79 ?  117 ASN   A CA   1 
ATOM   2357 C C    . ASN   A 1 117 ? 29.016 -15.134 6.709   1.00 12.16 ?  117 ASN   A C    1 
ATOM   2358 O O    . ASN   A 1 117 ? 29.317 -16.057 7.478   1.00 13.07 ?  117 ASN   A O    1 
ATOM   2359 C CB   . ASN   A 1 117 ? 27.869 -16.383 4.857   1.00 12.17 ?  117 ASN   A CB   1 
ATOM   2360 C CG   . ASN   A 1 117 ? 26.518 -16.762 4.315   1.00 11.79 ?  117 ASN   A CG   1 
ATOM   2361 O OD1  . ASN   A 1 117 ? 25.540 -16.787 5.062   1.00 12.45 ?  117 ASN   A OD1  1 
ATOM   2362 N ND2  . ASN   A 1 117 ? 26.438 -17.025 3.025   1.00 11.61 ?  117 ASN   A ND2  1 
ATOM   2363 H H    . ASN   A 1 117 ? 27.451 -14.024 4.344   1.00 13.71 ?  117 ASN   A H    1 
ATOM   2364 H HA   . ASN   A 1 117 ? 27.030 -15.485 6.477   1.00 14.16 ?  117 ASN   A HA   1 
ATOM   2365 H HB2  . ASN   A 1 117 ? 28.424 -16.093 4.117   1.00 14.61 ?  117 ASN   A HB2  1 
ATOM   2366 H HB3  . ASN   A 1 117 ? 28.250 -17.158 5.288   1.00 14.61 ?  117 ASN   A HB3  1 
ATOM   2367 H HD21 . ASN   A 1 117 ? 25.685 -17.235 2.679   1.00 13.94 ?  117 ASN   A HD21 1 
ATOM   2368 H HD22 . ASN   A 1 117 ? 27.146 -16.982 2.536   1.00 13.94 ?  117 ASN   A HD22 1 
ATOM   2369 N N    . GLN   A 1 118 ? 29.743 -14.026 6.593   1.00 12.15 ?  118 GLN   A N    1 
ATOM   2370 C CA   . GLN   A 1 118 ? 30.923 -13.793 7.413   1.00 12.60 ?  118 GLN   A CA   1 
ATOM   2371 C C    . GLN   A 1 118 ? 30.584 -13.221 8.786   1.00 12.61 ?  118 GLN   A C    1 
ATOM   2372 O O    . GLN   A 1 118 ? 31.499 -12.932 9.567   1.00 14.34 ?  118 GLN   A O    1 
ATOM   2373 C CB   . GLN   A 1 118 ? 31.918 -12.896 6.669   1.00 13.00 ?  118 GLN   A CB   1 
ATOM   2374 C CG   . GLN   A 1 118 ? 32.387 -13.485 5.348   1.00 13.35 ?  118 GLN   A CG   1 
ATOM   2375 C CD   . GLN   A 1 118 ? 33.223 -14.741 5.529   1.00 13.75 ?  118 GLN   A CD   1 
ATOM   2376 O OE1  . GLN   A 1 118 ? 34.087 -14.803 6.416   1.00 14.45 ?  118 GLN   A OE1  1 
ATOM   2377 N NE2  . GLN   A 1 118 ? 32.982 -15.746 4.682   1.00 13.60 ?  118 GLN   A NE2  1 
ATOM   2378 H H    . GLN   A 1 118 ? 29.563 -13.379 6.046   1.00 14.58 ?  118 GLN   A H    1 
ATOM   2379 H HA   . GLN   A 1 118 ? 31.353 -14.648 7.560   1.00 15.13 ?  118 GLN   A HA   1 
ATOM   2380 H HB2  . GLN   A 1 118 ? 31.494 -12.044 6.487   1.00 15.61 ?  118 GLN   A HB2  1 
ATOM   2381 H HB3  . GLN   A 1 118 ? 32.696 -12.767 7.233   1.00 15.61 ?  118 GLN   A HB3  1 
ATOM   2382 H HG2  . GLN   A 1 118 ? 31.612 -13.708 4.805   1.00 16.03 ?  118 GLN   A HG2  1 
ATOM   2383 H HG3  . GLN   A 1 118 ? 32.933 -12.828 4.886   1.00 16.03 ?  118 GLN   A HG3  1 
ATOM   2384 H HE21 . GLN   A 1 118 ? 32.368 -15.666 4.074   1.00 16.32 ?  118 GLN   A HE21 1 
ATOM   2385 H HE22 . GLN   A 1 118 ? 33.422 -16.482 4.740   1.00 16.32 ?  118 GLN   A HE22 1 
ATOM   2386 N N    . HIS   A 1 119 ? 29.297 -13.071 9.102   1.00 12.51 ?  119 HIS   A N    1 
ATOM   2387 C CA   . HIS   A 1 119 ? 28.846 -12.462 10.347  1.00 12.74 ?  119 HIS   A CA   1 
ATOM   2388 C C    . HIS   A 1 119 ? 27.705 -13.280 10.930  1.00 12.68 ?  119 HIS   A C    1 
ATOM   2389 O O    . HIS   A 1 119 ? 26.751 -13.610 10.221  1.00 13.35 ?  119 HIS   A O    1 
ATOM   2390 C CB   . HIS   A 1 119 ? 28.395 -11.025 10.071  1.00 13.23 ?  119 HIS   A CB   1 
ATOM   2391 C CG   . HIS   A 1 119 ? 29.483 -10.210 9.469   1.00 14.89 ?  119 HIS   A CG   1 
ATOM   2392 N ND1  . HIS   A 1 119 ? 30.449 -9.599  10.235  1.00 17.47 ?  119 HIS   A ND1  1 
ATOM   2393 C CD2  . HIS   A 1 119 ? 29.831 -10.003 8.178   1.00 15.89 ?  119 HIS   A CD2  1 
ATOM   2394 C CE1  . HIS   A 1 119 ? 31.324 -9.012  9.438   1.00 17.71 ?  119 HIS   A CE1  1 
ATOM   2395 N NE2  . HIS   A 1 119 ? 30.980 -9.251  8.185   1.00 17.31 ?  119 HIS   A NE2  1 
ATOM   2396 H H    . HIS   A 1 119 ? 28.644 -13.334 8.601   1.00 15.02 ?  119 HIS   A H    1 
ATOM   2397 H HA   . HIS   A 1 119 ? 29.578 -12.449 10.985  1.00 15.29 ?  119 HIS   A HA   1 
ATOM   2398 H HB2  . HIS   A 1 119 ? 27.649 -11.046 9.453   1.00 15.88 ?  119 HIS   A HB2  1 
ATOM   2399 H HB3  . HIS   A 1 119 ? 28.132 -10.615 10.906  1.00 15.88 ?  119 HIS   A HB3  1 
ATOM   2400 H HD2  . HIS   A 1 119 ? 29.378 -10.316 7.424   1.00 19.07 ?  119 HIS   A HD2  1 
ATOM   2401 H HE1  . HIS   A 1 119 ? 32.058 -8.511  9.709   1.00 21.25 ?  119 HIS   A HE1  1 
ATOM   2402 H HE2  . HIS   A 1 119 ? 31.387 -8.954  7.486   1.00 20.78 ?  119 HIS   A HE2  1 
ATOM   2403 N N    . GLU   A 1 120 ? 27.796 -13.592 12.224  1.00 13.59 ?  120 GLU   A N    1 
ATOM   2404 C CA   . GLU   A 1 120 ? 26.836 -14.516 12.826  1.00 15.53 ?  120 GLU   A CA   1 
ATOM   2405 C C    . GLU   A 1 120 ? 25.420 -13.948 12.881  1.00 14.45 ?  120 GLU   A C    1 
ATOM   2406 O O    . GLU   A 1 120 ? 24.447 -14.710 12.759  1.00 14.80 ?  120 GLU   A O    1 
ATOM   2407 C CB   . GLU   A 1 120 ? 27.306 -14.917 14.225  1.00 20.82 ?  120 GLU   A CB   1 
ATOM   2408 C CG   . GLU   A 1 120 ? 28.501 -15.855 14.221  1.00 28.59 ?  120 GLU   A CG   1 
ATOM   2409 C CD   . GLU   A 1 120 ? 28.690 -16.557 15.548  1.00 35.76 ?  120 GLU   A CD   1 
ATOM   2410 O OE1  . GLU   A 1 120 ? 28.259 -16.001 16.581  1.00 37.93 ?  120 GLU   A OE1  1 
ATOM   2411 O OE2  . GLU   A 1 120 ? 29.266 -17.665 15.557  1.00 39.80 -1 120 GLU   A OE2  1 
ATOM   2412 H H    . GLU   A 1 120 ? 28.397 -13.289 12.764  1.00 16.31 ?  120 GLU   A H    1 
ATOM   2413 H HA   . GLU   A 1 120 ? 26.811 -15.321 12.294  1.00 18.64 ?  120 GLU   A HA   1 
ATOM   2414 H HB2  . GLU   A 1 120 ? 27.564 -14.125 14.721  1.00 24.99 ?  120 GLU   A HB2  1 
ATOM   2415 H HB3  . GLU   A 1 120 ? 26.582 -15.371 14.687  1.00 24.99 ?  120 GLU   A HB3  1 
ATOM   2416 H HG2  . GLU   A 1 120 ? 28.383 -16.526 13.528  1.00 34.32 ?  120 GLU   A HG2  1 
ATOM   2417 H HG3  . GLU   A 1 120 ? 29.311 -15.350 14.061  1.00 34.32 ?  120 GLU   A HG3  1 
ATOM   2418 N N    . VAL   A 1 121 ? 25.287 -12.638 13.094  1.00 14.06 ?  121 VAL   A N    1 
ATOM   2419 C CA   . VAL   A 1 121 ? 23.995 -11.967 13.217  1.00 14.13 ?  121 VAL   A CA   1 
ATOM   2420 C C    . VAL   A 1 121 ? 24.106 -10.585 12.580  1.00 12.61 ?  121 VAL   A C    1 
ATOM   2421 O O    . VAL   A 1 121 ? 25.070 -9.854  12.829  1.00 13.56 ?  121 VAL   A O    1 
ATOM   2422 C CB   . VAL   A 1 121 ? 23.561 -11.820 14.694  1.00 16.96 ?  121 VAL   A CB   1 
ATOM   2423 C CG1  . VAL   A 1 121 ? 22.176 -11.190 14.787  1.00 17.45 ?  121 VAL   A CG1  1 
ATOM   2424 C CG2  . VAL   A 1 121 ? 23.582 -13.153 15.425  1.00 19.29 ?  121 VAL   A CG2  1 
ATOM   2425 H H    . VAL   A 1 121 ? 25.954 -12.100 13.180  1.00 16.88 ?  121 VAL   A H    1 
ATOM   2426 H HA   . VAL   A 1 121 ? 23.319 -12.481 12.750  1.00 16.96 ?  121 VAL   A HA   1 
ATOM   2427 H HB   . VAL   A 1 121 ? 24.180 -11.231 15.148  1.00 20.35 ?  121 VAL   A HB   1 
ATOM   2428 H HG11 . VAL   A 1 121 ? 21.859 -11.251 15.704  1.00 20.95 ?  121 VAL   A HG11 1 
ATOM   2429 H HG12 . VAL   A 1 121 ? 22.230 -10.261 14.519  1.00 20.95 ?  121 VAL   A HG12 1 
ATOM   2430 H HG13 . VAL   A 1 121 ? 21.569 -11.671 14.200  1.00 20.95 ?  121 VAL   A HG13 1 
ATOM   2431 H HG21 . VAL   A 1 121 ? 23.232 -13.029 16.326  1.00 23.15 ?  121 VAL   A HG21 1 
ATOM   2432 H HG22 . VAL   A 1 121 ? 23.023 -13.789 14.947  1.00 23.15 ?  121 VAL   A HG22 1 
ATOM   2433 H HG23 . VAL   A 1 121 ? 24.491 -13.480 15.470  1.00 23.15 ?  121 VAL   A HG23 1 
ATOM   2434 N N    . LEU   A 1 122 ? 23.094 -10.200 11.795  1.00 12.22 ?  122 LEU   A N    1 
ATOM   2435 C CA   . LEU   A 1 122 ? 23.094 -8.902  11.127  1.00 11.96 ?  122 LEU   A CA   1 
ATOM   2436 C C    . LEU   A 1 122 ? 21.700 -8.299  11.096  1.00 11.92 ?  122 LEU   A C    1 
ATOM   2437 O O    . LEU   A 1 122 ? 20.704 -9.015  10.962  1.00 13.00 ?  122 LEU   A O    1 
ATOM   2438 C CB   . LEU   A 1 122 ? 23.517 -8.997  9.652   1.00 13.33 ?  122 LEU   A CB   1 
ATOM   2439 C CG   . LEU   A 1 122 ? 24.725 -9.851  9.288   1.00 13.18 ?  122 LEU   A CG   1 
ATOM   2440 C CD1  . LEU   A 1 122 ? 24.325 -11.296 9.051   1.00 14.04 ?  122 LEU   A CD1  1 
ATOM   2441 C CD2  . LEU   A 1 122 ? 25.420 -9.274  8.066   1.00 12.91 ?  122 LEU   A CD2  1 
ATOM   2442 H H    . LEU   A 1 122 ? 22.391 -10.675 11.633  1.00 14.67 ?  122 LEU   A H    1 
ATOM   2443 H HA   . LEU   A 1 122 ? 23.693 -8.291  11.588  1.00 14.35 ?  122 LEU   A HA   1 
ATOM   2444 H HB2  . LEU   A 1 122 ? 22.774 -9.356  9.154   1.00 16.00 ?  122 LEU   A HB2  1 
ATOM   2445 H HB3  . LEU   A 1 122 ? 23.714 -8.104  9.342   1.00 16.00 ?  122 LEU   A HB3  1 
ATOM   2446 H HG   . LEU   A 1 122 ? 25.366 -9.840  10.019  1.00 15.82 ?  122 LEU   A HG   1 
ATOM   2447 H HD11 . LEU   A 1 122 ? 25.107 -11.808 8.788   1.00 16.85 ?  122 LEU   A HD11 1 
ATOM   2448 H HD12 . LEU   A 1 122 ? 23.956 -11.660 9.871   1.00 16.85 ?  122 LEU   A HD12 1 
ATOM   2449 H HD13 . LEU   A 1 122 ? 23.659 -11.328 8.346   1.00 16.85 ?  122 LEU   A HD13 1 
ATOM   2450 H HD21 . LEU   A 1 122 ? 26.166 -9.847  7.815   1.00 15.50 ?  122 LEU   A HD21 1 
ATOM   2451 H HD22 . LEU   A 1 122 ? 24.787 -9.222  7.333   1.00 15.50 ?  122 LEU   A HD22 1 
ATOM   2452 H HD23 . LEU   A 1 122 ? 25.752 -8.384  8.277   1.00 15.50 ?  122 LEU   A HD23 1 
ATOM   2453 N N    A LEU   A 1 123 ? 21.645 -6.970  11.191  0.72 11.71 ?  123 LEU   A N    1 
ATOM   2454 N N    B LEU   A 1 123 ? 21.652 -6.970  11.215  0.28 11.91 ?  123 LEU   A N    1 
ATOM   2455 C CA   A LEU   A 1 123 ? 20.479 -6.171  10.816  0.72 11.25 ?  123 LEU   A CA   1 
ATOM   2456 C CA   B LEU   A 1 123 ? 20.476 -6.166  10.897  0.28 11.93 ?  123 LEU   A CA   1 
ATOM   2457 C C    A LEU   A 1 123 ? 20.716 -5.667  9.401   0.72 10.41 ?  123 LEU   A C    1 
ATOM   2458 C C    B LEU   A 1 123 ? 20.718 -5.596  9.504   0.28 11.37 ?  123 LEU   A C    1 
ATOM   2459 O O    A LEU   A 1 123 ? 21.801 -5.151  9.115   0.72 10.33 ?  123 LEU   A O    1 
ATOM   2460 O O    B LEU   A 1 123 ? 21.617 -4.770  9.321   0.28 11.04 ?  123 LEU   A O    1 
ATOM   2461 C CB   A LEU   A 1 123 ? 20.356 -4.976  11.761  0.72 11.70 ?  123 LEU   A CB   1 
ATOM   2462 C CB   B LEU   A 1 123 ? 20.318 -5.041  11.921  0.28 12.36 ?  123 LEU   A CB   1 
ATOM   2463 C CG   A LEU   A 1 123 ? 19.273 -3.951  11.427  0.72 12.93 ?  123 LEU   A CG   1 
ATOM   2464 C CG   B LEU   A 1 123 ? 19.368 -3.900  11.537  0.28 12.26 ?  123 LEU   A CG   1 
ATOM   2465 C CD1  A LEU   A 1 123 ? 17.892 -4.592  11.439  0.72 13.60 ?  123 LEU   A CD1  1 
ATOM   2466 C CD1  B LEU   A 1 123 ? 17.916 -4.368  11.495  0.28 12.27 ?  123 LEU   A CD1  1 
ATOM   2467 C CD2  A LEU   A 1 123 ? 19.336 -2.781  12.405  0.72 13.36 ?  123 LEU   A CD2  1 
ATOM   2468 C CD2  B LEU   A 1 123 ? 19.532 -2.712  12.477  0.28 12.27 ?  123 LEU   A CD2  1 
ATOM   2469 H H    A LEU   A 1 123 ? 22.302 -6.491  11.478  0.72 14.06 ?  123 LEU   A H    1 
ATOM   2470 H H    B LEU   A 1 123 ? 22.318 -6.490  11.477  0.28 14.30 ?  123 LEU   A H    1 
ATOM   2471 H HA   A LEU   A 1 123 ? 19.671 -6.707  10.849  0.72 13.51 ?  123 LEU   A HA   1 
ATOM   2472 H HA   B LEU   A 1 123 ? 19.677 -6.714  10.890  0.28 14.32 ?  123 LEU   A HA   1 
ATOM   2473 H HB2  A LEU   A 1 123 ? 20.161 -5.312  12.651  0.72 14.04 ?  123 LEU   A HB2  1 
ATOM   2474 H HB2  B LEU   A 1 123 ? 19.984 -5.426  12.750  0.28 14.84 ?  123 LEU   A HB2  1 
ATOM   2475 H HB3  A LEU   A 1 123 ? 21.199 -4.506  11.771  0.72 14.04 ?  123 LEU   A HB3  1 
ATOM   2476 H HB3  B LEU   A 1 123 ? 21.189 -4.645  12.083  0.28 14.84 ?  123 LEU   A HB3  1 
ATOM   2477 H HG   A LEU   A 1 123 ? 19.427 -3.595  10.538  0.72 15.53 ?  123 LEU   A HG   1 
ATOM   2478 H HG   B LEU   A 1 123 ? 19.593 -3.585  10.651  0.28 14.72 ?  123 LEU   A HG   1 
ATOM   2479 H HD11 A LEU   A 1 123 ? 17.220 -3.907  11.305  0.72 16.32 ?  123 LEU   A HD11 1 
ATOM   2480 H HD11 B LEU   A 1 123 ? 17.350 -3.620  11.250  0.28 14.73 ?  123 LEU   A HD11 1 
ATOM   2481 H HD12 A LEU   A 1 123 ? 17.843 -5.249  10.726  0.72 16.32 ?  123 LEU   A HD12 1 
ATOM   2482 H HD12 B LEU   A 1 123 ? 17.831 -5.077  10.837  0.28 14.73 ?  123 LEU   A HD12 1 
ATOM   2483 H HD13 A LEU   A 1 123 ? 17.753 -5.027  12.297  0.72 16.32 ?  123 LEU   A HD13 1 
ATOM   2484 H HD13 B LEU   A 1 123 ? 17.664 -4.700  12.372  0.28 14.73 ?  123 LEU   A HD13 1 
ATOM   2485 H HD21 A LEU   A 1 123 ? 18.644 -2.139  12.183  0.72 16.04 ?  123 LEU   A HD21 1 
ATOM   2486 H HD21 B LEU   A 1 123 ? 18.917 -2.011  12.208  0.28 14.73 ?  123 LEU   A HD21 1 
ATOM   2487 H HD22 A LEU   A 1 123 ? 19.194 -3.117  13.308  0.72 16.04 ?  123 LEU   A HD22 1 
ATOM   2488 H HD22 B LEU   A 1 123 ? 19.333 -2.996  13.383  0.28 14.73 ?  123 LEU   A HD22 1 
ATOM   2489 H HD23 A LEU   A 1 123 ? 20.208 -2.364  12.344  0.72 16.04 ?  123 LEU   A HD23 1 
ATOM   2490 H HD23 B LEU   A 1 123 ? 20.445 -2.391  12.423  0.28 14.73 ?  123 LEU   A HD23 1 
ATOM   2491 N N    A ALA   A 1 124 ? 19.719 -5.785  8.519   0.72 9.90  ?  124 ALA   A N    1 
ATOM   2492 N N    B ALA   A 1 124 ? 19.932 -6.032  8.528   0.28 11.00 ?  124 ALA   A N    1 
ATOM   2493 C CA   A ALA   A 1 124 ? 19.996 -5.506  7.116   0.72 10.07 ?  124 ALA   A CA   1 
ATOM   2494 C CA   B ALA   A 1 124 ? 20.195 -5.737  7.129   0.28 11.32 ?  124 ALA   A CA   1 
ATOM   2495 C C    A ALA   A 1 124 ? 18.759 -5.080  6.335   0.72 9.92  ?  124 ALA   A C    1 
ATOM   2496 C C    B ALA   A 1 124 ? 18.977 -5.155  6.434   0.28 10.83 ?  124 ALA   A C    1 
ATOM   2497 O O    A ALA   A 1 124 ? 17.633 -5.471  6.678   0.72 10.72 ?  124 ALA   A O    1 
ATOM   2498 O O    B ALA   A 1 124 ? 17.840 -5.337  6.885   0.28 10.81 ?  124 ALA   A O    1 
ATOM   2499 C CB   A ALA   A 1 124 ? 20.606 -6.736  6.432   0.72 10.74 ?  124 ALA   A CB   1 
ATOM   2500 C CB   B ALA   A 1 124 ? 20.633 -6.999  6.372   0.28 11.76 ?  124 ALA   A CB   1 
ATOM   2501 H H    A ALA   A 1 124 ? 18.907 -6.012  8.702   0.72 11.88 ?  124 ALA   A H    1 
ATOM   2502 H H    B ALA   A 1 124 ? 19.232 -6.515  8.652   0.28 13.20 ?  124 ALA   A H    1 
ATOM   2503 H HA   A ALA   A 1 124 ? 20.651 -4.795  7.074   0.72 12.09 ?  124 ALA   A HA   1 
ATOM   2504 H HA   B ALA   A 1 124 ? 20.914 -5.093  7.081   0.28 13.59 ?  124 ALA   A HA   1 
ATOM   2505 H HB1  A ALA   A 1 124 ? 20.789 -6.525  5.504   0.72 12.89 ?  124 ALA   A HB1  1 
ATOM   2506 H HB1  B ALA   A 1 124 ? 20.803 -6.770  5.443   0.28 14.12 ?  124 ALA   A HB1  1 
ATOM   2507 H HB2  A ALA   A 1 124 ? 21.440 -6.967  6.884   0.72 12.89 ?  124 ALA   A HB2  1 
ATOM   2508 H HB2  B ALA   A 1 124 ? 21.442 -7.349  6.777   0.28 14.12 ?  124 ALA   A HB2  1 
ATOM   2509 H HB3  A ALA   A 1 124 ? 19.986 -7.475  6.493   0.72 12.89 ?  124 ALA   A HB3  1 
ATOM   2510 H HB3  B ALA   A 1 124 ? 19.925 -7.661  6.423   0.28 14.12 ?  124 ALA   A HB3  1 
ATOM   2511 N N    A PRO   A 1 125 ? 18.948 -4.329  5.253   0.72 10.02 ?  125 PRO   A N    1 
ATOM   2512 N N    B PRO   A 1 125 ? 19.188 -4.449  5.316   0.28 10.20 ?  125 PRO   A N    1 
ATOM   2513 C CA   A PRO   A 1 125 ? 17.895 -4.107  4.263   0.72 10.29 ?  125 PRO   A CA   1 
ATOM   2514 C CA   B PRO   A 1 125 ? 18.075 -4.045  4.456   0.28 10.72 ?  125 PRO   A CA   1 
ATOM   2515 C C    A PRO   A 1 125 ? 17.970 -5.174  3.176   0.72 10.21 ?  125 PRO   A C    1 
ATOM   2516 C C    B PRO   A 1 125 ? 17.932 -5.036  3.313   0.28 11.61 ?  125 PRO   A C    1 
ATOM   2517 O O    A PRO   A 1 125 ? 18.947 -5.921  3.065   0.72 10.38 ?  125 PRO   A O    1 
ATOM   2518 O O    B PRO   A 1 125 ? 18.740 -5.963  3.200   0.28 11.85 ?  125 PRO   A O    1 
ATOM   2519 C CB   A PRO   A 1 125 ? 18.308 -2.756  3.666   0.72 10.67 ?  125 PRO   A CB   1 
ATOM   2520 C CB   B PRO   A 1 125 ? 18.545 -2.683  3.939   0.28 10.18 ?  125 PRO   A CB   1 
ATOM   2521 C CG   A PRO   A 1 125 ? 19.822 -2.888  3.600   0.72 11.13 ?  125 PRO   A CG   1 
ATOM   2522 C CG   B PRO   A 1 125 ? 20.039 -2.896  3.757   0.28 9.90  ?  125 PRO   A CG   1 
ATOM   2523 C CD   A PRO   A 1 125 ? 20.199 -3.635  4.876   0.72 10.60 ?  125 PRO   A CD   1 
ATOM   2524 C CD   B PRO   A 1 125 ? 20.467 -3.904  4.821   0.28 9.45  ?  125 PRO   A CD   1 
ATOM   2525 H HA   A PRO   A 1 125 ? 17.009 -4.071  4.666   0.72 12.36 ?  125 PRO   A HA   1 
ATOM   2526 H HA   B PRO   A 1 125 ? 17.243 -3.962  4.951   0.28 12.87 ?  125 PRO   A HA   1 
ATOM   2527 H HB2  A PRO   A 1 125 ? 17.915 -2.651  2.782   0.72 12.81 ?  125 PRO   A HB2  1 
ATOM   2528 H HB2  B PRO   A 1 125 ? 18.114 -2.476  3.094   0.28 12.22 ?  125 PRO   A HB2  1 
ATOM   2529 H HB3  A PRO   A 1 125 ? 18.033 -2.036  4.257   0.72 12.81 ?  125 PRO   A HB3  1 
ATOM   2530 H HB3  B PRO   A 1 125 ? 18.367 -1.994  4.601   0.28 12.22 ?  125 PRO   A HB3  1 
ATOM   2531 H HG2  A PRO   A 1 125 ? 20.072 -3.401  2.814   0.72 13.36 ?  125 PRO   A HG2  1 
ATOM   2532 H HG2  B PRO   A 1 125 ? 20.209 -3.246  2.868   0.28 11.88 ?  125 PRO   A HG2  1 
ATOM   2533 H HG3  A PRO   A 1 125 ? 20.224 -2.006  3.579   0.72 13.36 ?  125 PRO   A HG3  1 
ATOM   2534 H HG3  B PRO   A 1 125 ? 20.504 -2.053  3.882   0.28 11.88 ?  125 PRO   A HG3  1 
ATOM   2535 H HD2  A PRO   A 1 125 ? 20.906 -4.269  4.703   0.72 12.72 ?  125 PRO   A HD2  1 
ATOM   2536 H HD2  B PRO   A 1 125 ? 21.010 -4.603  4.421   0.28 11.34 ?  125 PRO   A HD2  1 
ATOM   2537 H HD3  A PRO   A 1 125 ? 20.451 -3.000  5.572   0.72 12.72 ?  125 PRO   A HD3  1 
ATOM   2538 H HD3  B PRO   A 1 125 ? 20.940 -3.454  5.537   0.28 11.34 ?  125 PRO   A HD3  1 
ATOM   2539 N N    A LEU   A 1 126 ? 16.920 -5.215  2.358   0.72 10.27 ?  126 LEU   A N    1 
ATOM   2540 N N    B LEU   A 1 126 ? 16.931 -4.852  2.457   0.28 12.37 ?  126 LEU   A N    1 
ATOM   2541 C CA   A LEU   A 1 126 ? 16.932 -6.036  1.156   0.72 10.15 ?  126 LEU   A CA   1 
ATOM   2542 C CA   B LEU   A 1 126 ? 16.768 -5.695  1.276   0.28 12.76 ?  126 LEU   A CA   1 
ATOM   2543 C C    A LEU   A 1 126 ? 17.862 -5.419  0.112   0.72 10.29 ?  126 LEU   A C    1 
ATOM   2544 C C    B LEU   A 1 126 ? 17.705 -5.187  0.185   0.28 12.07 ?  126 LEU   A C    1 
ATOM   2545 O O    A LEU   A 1 126 ? 17.633 -4.304  -0.368  0.72 11.67 ?  126 LEU   A O    1 
ATOM   2546 O O    B LEU   A 1 126 ? 17.457 -4.136  -0.416  0.28 12.29 ?  126 LEU   A O    1 
ATOM   2547 C CB   A LEU   A 1 126 ? 15.521 -6.166  0.598   0.72 10.73 ?  126 LEU   A CB   1 
ATOM   2548 C CB   B LEU   A 1 126 ? 15.318 -5.632  0.810   0.28 14.78 ?  126 LEU   A CB   1 
ATOM   2549 C CG   A LEU   A 1 126 ? 14.596 -7.080  1.398   0.72 11.85 ?  126 LEU   A CG   1 
ATOM   2550 C CG   B LEU   A 1 126 ? 14.759 -6.841  0.064   0.28 16.54 ?  126 LEU   A CG   1 
ATOM   2551 C CD1  A LEU   A 1 126 ? 13.163 -6.930  0.909   0.72 13.27 ?  126 LEU   A CD1  1 
ATOM   2552 C CD1  B LEU   A 1 126 ? 14.792 -8.069  0.950   0.28 16.91 ?  126 LEU   A CD1  1 
ATOM   2553 C CD2  A LEU   A 1 126 ? 15.068 -8.539  1.308   0.72 11.93 ?  126 LEU   A CD2  1 
ATOM   2554 C CD2  B LEU   A 1 126 ? 13.343 -6.552  -0.397  0.28 17.02 ?  126 LEU   A CD2  1 
ATOM   2555 H H    A LEU   A 1 126 ? 16.194 -4.771  2.470   0.72 12.33 ?  126 LEU   A H    1 
ATOM   2556 H H    B LEU   A 1 126 ? 16.320 -4.246  2.542   0.28 14.85 ?  126 LEU   A H    1 
ATOM   2557 H HA   A LEU   A 1 126 ? 17.265 -6.924  1.373   0.72 12.19 ?  126 LEU   A HA   1 
ATOM   2558 H HA   B LEU   A 1 126 ? 17.001 -6.612  1.493   0.28 15.31 ?  126 LEU   A HA   1 
ATOM   2559 H HB2  A LEU   A 1 126 ? 15.114 -5.290  0.578   0.72 12.88 ?  126 LEU   A HB2  1 
ATOM   2560 H HB2  B LEU   A 1 126 ? 14.759 -5.499  1.590   0.28 17.75 ?  126 LEU   A HB2  1 
ATOM   2561 H HB3  A LEU   A 1 126 ? 15.574 -6.525  -0.302  0.72 12.88 ?  126 LEU   A HB3  1 
ATOM   2562 H HB3  B LEU   A 1 126 ? 15.227 -4.867  0.220   0.28 17.75 ?  126 LEU   A HB3  1 
ATOM   2563 H HG   A LEU   A 1 126 ? 14.619 -6.821  2.331   0.72 14.22 ?  126 LEU   A HG   1 
ATOM   2564 H HG   B LEU   A 1 126 ? 15.305 -7.010  -0.719  0.28 19.85 ?  126 LEU   A HG   1 
ATOM   2565 H HD11 A LEU   A 1 126 ? 12.589 -7.522  1.422   0.72 15.93 ?  126 LEU   A HD11 1 
ATOM   2566 H HD11 B LEU   A 1 126 ? 14.261 -8.767  0.539   0.28 20.29 ?  126 LEU   A HD11 1 
ATOM   2567 H HD12 A LEU   A 1 126 ? 12.885 -6.012  1.026   0.72 15.93 ?  126 LEU   A HD12 1 
ATOM   2568 H HD12 B LEU   A 1 126 ? 15.710 -8.365  1.046   0.28 20.29 ?  126 LEU   A HD12 1 
ATOM   2569 H HD13 A LEU   A 1 126 ? 13.125 -7.173  -0.032  0.72 15.93 ?  126 LEU   A HD13 1 
ATOM   2570 H HD13 B LEU   A 1 126 ? 14.423 -7.839  1.818   0.28 20.29 ?  126 LEU   A HD13 1 
ATOM   2571 H HD21 A LEU   A 1 126 ? 14.383 -9.120  1.677   0.72 14.32 ?  126 LEU   A HD21 1 
ATOM   2572 H HD21 B LEU   A 1 126 ? 12.941 -7.374  -0.717  0.28 20.43 ?  126 LEU   A HD21 1 
ATOM   2573 H HD22 A LEU   A 1 126 ? 15.224 -8.766  0.377   0.72 14.32 ?  126 LEU   A HD22 1 
ATOM   2574 H HD22 B LEU   A 1 126 ? 12.832 -6.206  0.352   0.28 20.43 ?  126 LEU   A HD22 1 
ATOM   2575 H HD23 A LEU   A 1 126 ? 15.891 -8.639  1.813   0.72 14.32 ?  126 LEU   A HD23 1 
ATOM   2576 H HD23 B LEU   A 1 126 ? 13.368 -5.895  -1.110  0.28 20.43 ?  126 LEU   A HD23 1 
ATOM   2577 N N    A LEU   A 1 127 ? 18.909 -6.155  -0.248  0.72 10.43 ?  127 LEU   A N    1 
ATOM   2578 N N    B LEU   A 1 127 ? 18.775 -5.932  -0.089  0.28 11.72 ?  127 LEU   A N    1 
ATOM   2579 C CA   A LEU   A 1 127 ? 19.893 -5.655  -1.196  0.72 10.32 ?  127 LEU   A CA   1 
ATOM   2580 C CA   B LEU   A 1 127 ? 19.801 -5.442  -1.000  0.28 11.57 ?  127 LEU   A CA   1 
ATOM   2581 C C    A LEU   A 1 127 ? 19.275 -5.479  -2.575  0.72 9.90  ?  127 LEU   A C    1 
ATOM   2582 C C    B LEU   A 1 127 ? 19.251 -5.281  -2.405  0.28 11.45 ?  127 LEU   A C    1 
ATOM   2583 O O    A LEU   A 1 127 ? 18.446 -6.278  -3.022  0.72 10.42 ?  127 LEU   A O    1 
ATOM   2584 O O    B LEU   A 1 127 ? 18.425 -6.074  -2.866  0.28 12.04 ?  127 LEU   A O    1 
ATOM   2585 C CB   A LEU   A 1 127 ? 21.076 -6.619  -1.287  0.72 11.33 ?  127 LEU   A CB   1 
ATOM   2586 C CB   B LEU   A 1 127 ? 20.997 -6.390  -1.042  0.28 11.53 ?  127 LEU   A CB   1 
ATOM   2587 C CG   A LEU   A 1 127 ? 21.860 -6.894  -0.005  0.72 12.16 ?  127 LEU   A CG   1 
ATOM   2588 C CG   B LEU   A 1 127 ? 21.827 -6.432  0.241   0.28 11.38 ?  127 LEU   A CG   1 
ATOM   2589 C CD1  A LEU   A 1 127 ? 22.971 -7.878  -0.294  0.72 12.24 ?  127 LEU   A CD1  1 
ATOM   2590 C CD1  B LEU   A 1 127 ? 23.030 -7.346  0.077   0.28 11.89 ?  127 LEU   A CD1  1 
ATOM   2591 C CD2  A LEU   A 1 127 ? 22.433 -5.618  0.557   0.72 12.64 ?  127 LEU   A CD2  1 
ATOM   2592 C CD2  B LEU   A 1 127 ? 22.263 -5.031  0.662   0.28 11.67 ?  127 LEU   A CD2  1 
ATOM   2593 H H    A LEU   A 1 127 ? 19.077 -6.950  0.053   0.72 12.52 ?  127 LEU   A H    1 
ATOM   2594 H H    B LEU   A 1 127 ? 18.927 -6.718  0.227   0.28 14.08 ?  127 LEU   A H    1 
ATOM   2595 H HA   A LEU   A 1 127 ? 20.223 -4.798  -0.891  0.72 12.38 ?  127 LEU   A HA   1 
ATOM   2596 H HA   B LEU   A 1 127 ? 20.095 -4.573  -0.703  0.28 13.89 ?  127 LEU   A HA   1 
ATOM   2597 H HB2  A LEU   A 1 127 ? 20.748 -7.472  -1.608  0.72 13.61 ?  127 LEU   A HB2  1 
ATOM   2598 H HB2  B LEU   A 1 127 ? 20.670 -7.287  -1.222  0.28 13.85 ?  127 LEU   A HB2  1 
ATOM   2599 H HB3  A LEU   A 1 127 ? 21.709 -6.258  -1.928  0.72 13.61 ?  127 LEU   A HB3  1 
ATOM   2600 H HB3  B LEU   A 1 127 ? 21.580 -6.110  -1.770  0.28 13.85 ?  127 LEU   A HB3  1 
ATOM   2601 H HG   A LEU   A 1 127 ? 21.268 -7.293  0.661   0.72 14.60 ?  127 LEU   A HG   1 
ATOM   2602 H HG   B LEU   A 1 127 ? 21.274 -6.797  0.947   0.28 13.67 ?  127 LEU   A HG   1 
ATOM   2603 H HD11 A LEU   A 1 127 ? 23.452 -8.067  0.530   0.72 14.70 ?  127 LEU   A HD11 1 
ATOM   2604 H HD11 B LEU   A 1 127 ? 23.562 -7.310  0.887   0.28 14.28 ?  127 LEU   A HD11 1 
ATOM   2605 H HD12 A LEU   A 1 127 ? 22.590 -8.698  -0.647  0.72 14.70 ?  127 LEU   A HD12 1 
ATOM   2606 H HD12 B LEU   A 1 127 ? 22.721 -8.253  -0.077  0.28 14.28 ?  127 LEU   A HD12 1 
ATOM   2607 H HD13 A LEU   A 1 127 ? 23.575 -7.487  -0.944  0.72 14.70 ?  127 LEU   A HD13 1 
ATOM   2608 H HD13 B LEU   A 1 127 ? 23.557 -7.043  -0.679  0.28 14.28 ?  127 LEU   A HD13 1 
ATOM   2609 H HD21 A LEU   A 1 127 ? 23.009 -5.833  1.306   0.72 15.18 ?  127 LEU   A HD21 1 
ATOM   2610 H HD21 B LEU   A 1 127 ? 22.969 -5.109  1.319   0.28 14.01 ?  127 LEU   A HD21 1 
ATOM   2611 H HD22 A LEU   A 1 127 ? 22.943 -5.175  -0.138  0.72 15.18 ?  127 LEU   A HD22 1 
ATOM   2612 H HD22 B LEU   A 1 127 ? 22.582 -4.553  -0.118  0.28 14.01 ?  127 LEU   A HD22 1 
ATOM   2613 H HD23 A LEU   A 1 127 ? 21.705 -5.049  0.849   0.72 15.18 ?  127 LEU   A HD23 1 
ATOM   2614 H HD23 B LEU   A 1 127 ? 21.501 -4.568  1.045   0.28 14.01 ?  127 LEU   A HD23 1 
ATOM   2615 N N    A SER   A 1 128 ? 19.709 -4.428  -3.257  0.72 10.02 ?  128 SER   A N    1 
ATOM   2616 N N    B SER   A 1 128 ? 19.720 -4.239  -3.086  0.28 11.17 ?  128 SER   A N    1 
ATOM   2617 C CA   A SER   A 1 128 ? 19.302 -4.045  -4.605  0.72 10.63 ?  128 SER   A CA   1 
ATOM   2618 C CA   B SER   A 1 128 ? 19.379 -3.937  -4.466  0.28 11.42 ?  128 SER   A CA   1 
ATOM   2619 C C    A SER   A 1 128 ? 17.845 -3.591  -4.707  0.72 10.84 ?  128 SER   A C    1 
ATOM   2620 C C    B SER   A 1 128 ? 17.926 -3.512  -4.626  0.28 11.80 ?  128 SER   A C    1 
ATOM   2621 O O    A SER   A 1 128 ? 17.409 -3.246  -5.805  0.72 12.60 ?  128 SER   A O    1 
ATOM   2622 O O    B SER   A 1 128 ? 17.490 -3.270  -5.754  0.28 12.16 ?  128 SER   A O    1 
ATOM   2623 C CB   A SER   A 1 128 ? 19.626 -5.102  -5.673  0.72 11.13 ?  128 SER   A CB   1 
ATOM   2624 C CB   B SER   A 1 128 ? 19.727 -5.087  -5.420  0.28 10.97 ?  128 SER   A CB   1 
ATOM   2625 O OG   A SER   A 1 128 ? 21.027 -5.364  -5.724  0.72 12.03 ?  128 SER   A OG   1 
ATOM   2626 O OG   B SER   A 1 128 ? 21.134 -5.173  -5.592  0.28 10.75 ?  128 SER   A OG   1 
ATOM   2627 H H    A SER   A 1 128 ? 20.309 -3.897  -2.938  0.72 12.03 ?  128 SER   A H    1 
ATOM   2628 H H    B SER   A 1 128 ? 20.262 -3.655  -2.751  0.28 13.40 ?  128 SER   A H    1 
ATOM   2629 H HA   A SER   A 1 128 ? 19.834 -3.272  -4.835  0.72 12.76 ?  128 SER   A HA   1 
ATOM   2630 H HA   B SER   A 1 128 ? 19.911 -3.179  -4.743  0.28 13.71 ?  128 SER   A HA   1 
ATOM   2631 H HB2  A SER   A 1 128 ? 19.156 -5.920  -5.465  0.72 13.36 ?  128 SER   A HB2  1 
ATOM   2632 H HB2  B SER   A 1 128 ? 19.398 -5.918  -5.041  0.28 13.17 ?  128 SER   A HB2  1 
ATOM   2633 H HB3  A SER   A 1 128 ? 19.334 -4.764  -6.540  0.72 13.36 ?  128 SER   A HB3  1 
ATOM   2634 H HB3  B SER   A 1 128 ? 19.318 -4.923  -6.278  0.28 13.17 ?  128 SER   A HB3  1 
ATOM   2635 H HG   A SER   A 1 128 ? 21.442 -4.658  -5.914  0.72 14.44 ?  128 SER   A HG   1 
ATOM   2636 H HG   B SER   A 1 128 ? 21.423 -4.438  -5.885  0.28 12.90 ?  128 SER   A HG   1 
ATOM   2637 N N    A ALA   A 1 129 ? 17.101 -3.549  -3.603  0.72 11.56 ?  129 ALA   A N    1 
ATOM   2638 N N    B ALA   A 1 129 ? 17.175 -3.391  -3.534  0.28 12.17 ?  129 ALA   A N    1 
ATOM   2639 C CA   A ALA   A 1 129 ? 15.724 -3.069  -3.612  0.72 12.24 ?  129 ALA   A CA   1 
ATOM   2640 C CA   B ALA   A 1 129 ? 15.809 -2.898  -3.582  0.28 12.34 ?  129 ALA   A CA   1 
ATOM   2641 C C    A ALA   A 1 129 ? 15.714 -1.539  -3.546  0.72 11.99 ?  129 ALA   A C    1 
ATOM   2642 C C    B ALA   A 1 129 ? 15.805 -1.370  -3.571  0.28 11.82 ?  129 ALA   A C    1 
ATOM   2643 O O    A ALA   A 1 129 ? 16.755 -0.880  -3.647  0.72 12.25 ?  129 ALA   A O    1 
ATOM   2644 O O    B ALA   A 1 129 ? 16.852 -0.716  -3.517  0.28 11.29 ?  129 ALA   A O    1 
ATOM   2645 C CB   A ALA   A 1 129 ? 14.926 -3.728  -2.489  0.72 13.51 ?  129 ALA   A CB   1 
ATOM   2646 C CB   B ALA   A 1 129 ? 14.992 -3.476  -2.427  0.28 12.86 ?  129 ALA   A CB   1 
ATOM   2647 H H    A ALA   A 1 129 ? 17.380 -3.796  -2.824  0.72 13.88 ?  129 ALA   A H    1 
ATOM   2648 H H    B ALA   A 1 129 ? 17.449 -3.592  -2.745  0.28 14.61 ?  129 ALA   A H    1 
ATOM   2649 H HA   A ALA   A 1 129 ? 15.319 -3.328  -4.448  0.72 14.69 ?  129 ALA   A HA   1 
ATOM   2650 H HA   B ALA   A 1 129 ? 15.405 -3.188  -4.407  0.28 14.81 ?  129 ALA   A HA   1 
ATOM   2651 H HB1  A ALA   A 1 129 ? 14.016 -3.398  -2.516  0.72 16.21 ?  129 ALA   A HB1  1 
ATOM   2652 H HB1  B ALA   A 1 129 ? 14.113 -3.065  -2.427  0.28 15.44 ?  129 ALA   A HB1  1 
ATOM   2653 H HB2  A ALA   A 1 129 ? 14.937 -4.689  -2.618  0.72 16.21 ?  129 ALA   A HB2  1 
ATOM   2654 H HB2  B ALA   A 1 129 ? 14.907 -4.435  -2.548  0.28 15.44 ?  129 ALA   A HB2  1 
ATOM   2655 H HB3  A ALA   A 1 129 ? 15.335 -3.506  -1.636  0.72 16.21 ?  129 ALA   A HB3  1 
ATOM   2656 H HB3  B ALA   A 1 129 ? 15.443 -3.288  -1.588  0.28 15.44 ?  129 ALA   A HB3  1 
ATOM   2657 N N    A GLY   A 1 130 ? 14.522 -0.955  -3.412  0.72 12.50 ?  130 GLY   A N    1 
ATOM   2658 N N    B GLY   A 1 130 ? 14.610 -0.793  -3.636  0.28 12.02 ?  130 GLY   A N    1 
ATOM   2659 C CA   A GLY   A 1 130 ? 14.414 0.493   -3.344  0.72 12.87 ?  130 GLY   A CA   1 
ATOM   2660 C CA   B GLY   A 1 130 ? 14.500 0.656   -3.638  0.28 12.14 ?  130 GLY   A CA   1 
ATOM   2661 C C    A GLY   A 1 130 ? 14.997 1.141   -4.581  0.72 12.08 ?  130 GLY   A C    1 
ATOM   2662 C C    B GLY   A 1 130 ? 15.197 1.254   -4.841  0.28 12.04 ?  130 GLY   A C    1 
ATOM   2663 O O    A GLY   A 1 130 ? 14.767 0.695   -5.710  0.72 11.97 ?  130 GLY   A O    1 
ATOM   2664 O O    B GLY   A 1 130 ? 14.988 0.831   -5.984  0.28 12.32 ?  130 GLY   A O    1 
ATOM   2665 H H    A GLY   A 1 130 ? 13.771 -1.372  -3.372  0.72 15.00 ?  130 GLY   A H    1 
ATOM   2666 H H    B GLY   A 1 130 ? 13.862 -1.213  -3.679  0.28 14.43 ?  130 GLY   A H    1 
ATOM   2667 H HA2  A GLY   A 1 130 ? 13.477 0.749   -3.269  0.72 15.45 ?  130 GLY   A HA2  1 
ATOM   2668 H HA2  B GLY   A 1 130 ? 13.563 0.911   -3.662  0.28 14.58 ?  130 GLY   A HA2  1 
ATOM   2669 H HA3  A GLY   A 1 130 ? 14.890 0.823   -2.573  0.72 15.45 ?  130 GLY   A HA3  1 
ATOM   2670 H HA3  B GLY   A 1 130 ? 14.903 1.018   -2.836  0.28 14.58 ?  130 GLY   A HA3  1 
ATOM   2671 N N    A ILE   A 1 131 ? 15.768 2.215   -4.370  0.72 12.53 ?  131 ILE   A N    1 
ATOM   2672 N N    B ILE   A 1 131 ? 16.052 2.248   -4.585  0.28 11.77 ?  131 ILE   A N    1 
ATOM   2673 C CA   A ILE   A 1 131 ? 16.316 2.983   -5.484  0.72 11.91 ?  131 ILE   A CA   1 
ATOM   2674 C CA   B ILE   A 1 131 ? 16.676 3.005   -5.666  0.28 11.81 ?  131 ILE   A CA   1 
ATOM   2675 C C    A ILE   A 1 131 ? 17.363 2.224   -6.291  0.72 11.76 ?  131 ILE   A C    1 
ATOM   2676 C C    B ILE   A 1 131 ? 17.672 2.195   -6.481  0.28 11.89 ?  131 ILE   A C    1 
ATOM   2677 O O    A ILE   A 1 131 ? 17.780 2.722   -7.345  0.72 12.42 ?  131 ILE   A O    1 
ATOM   2678 O O    B ILE   A 1 131 ? 18.128 2.678   -7.525  0.28 12.37 ?  131 ILE   A O    1 
ATOM   2679 C CB   A ILE   A 1 131 ? 16.828 4.371   -5.036  0.72 13.28 ?  131 ILE   A CB   1 
ATOM   2680 C CB   B ILE   A 1 131 ? 17.313 4.321   -5.167  0.28 12.09 ?  131 ILE   A CB   1 
ATOM   2681 C CG1  A ILE   A 1 131 ? 18.042 4.250   -4.107  0.72 14.79 ?  131 ILE   A CG1  1 
ATOM   2682 C CG1  B ILE   A 1 131 ? 18.535 4.051   -4.282  0.28 12.64 ?  131 ILE   A CG1  1 
ATOM   2683 C CG2  A ILE   A 1 131 ? 15.701 5.161   -4.370  0.72 14.14 ?  131 ILE   A CG2  1 
ATOM   2684 C CG2  B ILE   A 1 131 ? 16.283 5.163   -4.421  0.28 12.19 ?  131 ILE   A CG2  1 
ATOM   2685 C CD1  A ILE   A 1 131 ? 18.679 5.592   -3.750  0.72 16.31 ?  131 ILE   A CD1  1 
ATOM   2686 C CD1  B ILE   A 1 131 ? 19.208 5.322   -3.774  0.28 13.45 ?  131 ILE   A CD1  1 
ATOM   2687 H H    A ILE   A 1 131 ? 15.967 2.526   -3.594  0.72 15.04 ?  131 ILE   A H    1 
ATOM   2688 H H    B ILE   A 1 131 ? 16.273 2.504   -3.795  0.28 14.13 ?  131 ILE   A H    1 
ATOM   2689 H HA   A ILE   A 1 131 ? 15.591 3.159   -6.098  0.72 14.30 ?  131 ILE   A HA   1 
ATOM   2690 H HA   B ILE   A 1 131 ? 15.975 3.258   -6.278  0.28 14.18 ?  131 ILE   A HA   1 
ATOM   2691 H HB   A ILE   A 1 131 ? 17.103 4.862   -5.825  0.72 15.94 ?  131 ILE   A HB   1 
ATOM   2692 H HB   B ILE   A 1 131 ? 17.605 4.824   -5.942  0.28 14.51 ?  131 ILE   A HB   1 
ATOM   2693 H HG12 A ILE   A 1 131 ? 17.763 3.823   -3.281  0.72 17.76 ?  131 ILE   A HG12 1 
ATOM   2694 H HG12 B ILE   A 1 131 ? 18.258 3.535   -3.512  0.28 15.17 ?  131 ILE   A HG12 1 
ATOM   2695 H HG13 A ILE   A 1 131 ? 18.718 3.710   -4.543  0.72 17.76 ?  131 ILE   A HG13 1 
ATOM   2696 H HG13 B ILE   A 1 131 ? 19.194 3.559   -4.794  0.28 15.17 ?  131 ILE   A HG13 1 
ATOM   2697 H HG21 A ILE   A 1 131 ? 15.994 6.074   -4.224  0.72 16.97 ?  131 ILE   A HG21 1 
ATOM   2698 H HG21 B ILE   A 1 131 ? 16.635 6.058   -4.295  0.28 14.64 ?  131 ILE   A HG21 1 
ATOM   2699 H HG22 A ILE   A 1 131 ? 14.925 5.153   -4.953  0.72 16.97 ?  131 ILE   A HG22 1 
ATOM   2700 H HG22 B ILE   A 1 131 ? 15.469 5.201   -4.948  0.28 14.64 ?  131 ILE   A HG22 1 
ATOM   2701 H HG23 A ILE   A 1 131 ? 15.480 4.744   -3.522  0.72 16.97 ?  131 ILE   A HG23 1 
ATOM   2702 H HG23 B ILE   A 1 131 ? 16.102 4.752   -3.562  0.28 14.64 ?  131 ILE   A HG23 1 
ATOM   2703 H HD11 A ILE   A 1 131 ? 19.494 5.431   -3.247  0.72 19.57 ?  131 ILE   A HD11 1 
ATOM   2704 H HD11 B ILE   A 1 131 ? 20.050 5.088   -3.352  0.28 16.15 ?  131 ILE   A HD11 1 
ATOM   2705 H HD12 A ILE   A 1 131 ? 18.885 6.072   -4.567  0.72 19.57 ?  131 ILE   A HD12 1 
ATOM   2706 H HD12 B ILE   A 1 131 ? 19.370 5.919   -4.523  0.28 16.15 ?  131 ILE   A HD12 1 
ATOM   2707 H HD13 A ILE   A 1 131 ? 18.057 6.107   -3.212  0.72 19.57 ?  131 ILE   A HD13 1 
ATOM   2708 H HD13 B ILE   A 1 131 ? 18.626 5.757   -3.129  0.28 16.15 ?  131 ILE   A HD13 1 
ATOM   2709 N N    A PHE   A 1 132 ? 17.804 1.039   -5.839  0.72 11.93 ?  132 PHE   A N    1 
ATOM   2710 N N    B PHE   A 1 132 ? 18.026 0.982   -6.046  0.28 11.67 ?  132 PHE   A N    1 
ATOM   2711 C CA   A PHE   A 1 132 ? 18.672 0.201   -6.663  0.72 11.72 ?  132 PHE   A CA   1 
ATOM   2712 C CA   B PHE   A 1 132 ? 18.934 0.156   -6.834  0.28 12.05 ?  132 PHE   A CA   1 
ATOM   2713 C C    A PHE   A 1 132 ? 17.910 -0.558  -7.749  0.72 12.27 ?  132 PHE   A C    1 
ATOM   2714 C C    B PHE   A 1 132 ? 18.228 -0.596  -7.960  0.28 13.00 ?  132 PHE   A C    1 
ATOM   2715 O O    A PHE   A 1 132 ? 18.538 -1.200  -8.596  0.72 13.31 ?  132 PHE   A O    1 
ATOM   2716 O O    B PHE   A 1 132 ? 18.907 -1.149  -8.834  0.28 13.94 ?  132 PHE   A O    1 
ATOM   2717 C CB   A PHE   A 1 132 ? 19.478 -0.778  -5.803  0.72 11.55 ?  132 PHE   A CB   1 
ATOM   2718 C CB   B PHE   A 1 132 ? 19.720 -0.802  -5.934  0.28 11.41 ?  132 PHE   A CB   1 
ATOM   2719 C CG   A PHE   A 1 132 ? 20.717 -0.186  -5.163  0.72 11.30 ?  132 PHE   A CG   1 
ATOM   2720 C CG   B PHE   A 1 132 ? 20.894 -0.162  -5.225  0.28 11.42 ?  132 PHE   A CG   1 
ATOM   2721 C CD1  A PHE   A 1 132 ? 20.634 0.854   -4.251  0.72 13.01 ?  132 PHE   A CD1  1 
ATOM   2722 C CD1  B PHE   A 1 132 ? 20.711 0.888   -4.338  0.28 12.14 ?  132 PHE   A CD1  1 
ATOM   2723 C CD2  A PHE   A 1 132 ? 21.965 -0.730  -5.424  0.72 12.25 ?  132 PHE   A CD2  1 
ATOM   2724 C CD2  B PHE   A 1 132 ? 22.181 -0.636  -5.428  0.28 11.77 ?  132 PHE   A CD2  1 
ATOM   2725 C CE1  A PHE   A 1 132 ? 21.780 1.363   -3.643  0.72 13.53 ?  132 PHE   A CE1  1 
ATOM   2726 C CE1  B PHE   A 1 132 ? 21.794 1.461   -3.681  0.28 12.43 ?  132 PHE   A CE1  1 
ATOM   2727 C CE2  A PHE   A 1 132 ? 23.111 -0.226  -4.820  0.72 13.30 ?  132 PHE   A CE2  1 
ATOM   2728 C CE2  B PHE   A 1 132 ? 23.264 -0.068  -4.774  0.28 12.14 ?  132 PHE   A CE2  1 
ATOM   2729 C CZ   A PHE   A 1 132 ? 23.013 0.825   -3.928  0.72 13.42 ?  132 PHE   A CZ   1 
ATOM   2730 C CZ   B PHE   A 1 132 ? 23.067 0.982   -3.900  0.28 12.21 ?  132 PHE   A CZ   1 
ATOM   2731 H H    A PHE   A 1 132 ? 17.612 0.706   -5.064  0.72 14.32 ?  132 PHE   A H    1 
ATOM   2732 H H    B PHE   A 1 132 ? 17.757 0.620   -5.307  0.28 14.01 ?  132 PHE   A H    1 
ATOM   2733 H HA   A PHE   A 1 132 ? 19.312 0.781   -7.102  0.72 14.07 ?  132 PHE   A HA   1 
ATOM   2734 H HA   B PHE   A 1 132 ? 19.582 0.743   -7.246  0.28 14.47 ?  132 PHE   A HA   1 
ATOM   2735 H HB2  A PHE   A 1 132 ? 18.910 -1.107  -5.087  0.72 13.86 ?  132 PHE   A HB2  1 
ATOM   2736 H HB2  B PHE   A 1 132 ? 19.126 -1.149  -5.252  0.28 13.69 ?  132 PHE   A HB2  1 
ATOM   2737 H HB3  A PHE   A 1 132 ? 19.761 -1.521  -6.359  0.72 13.86 ?  132 PHE   A HB3  1 
ATOM   2738 H HB3  B PHE   A 1 132 ? 20.065 -1.532  -6.474  0.28 13.69 ?  132 PHE   A HB3  1 
ATOM   2739 H HD1  A PHE   A 1 132 ? 19.807 1.223   -4.050  0.72 15.61 ?  132 PHE   A HD1  1 
ATOM   2740 H HD1  B PHE   A 1 132 ? 19.857 1.218   -4.184  0.28 14.58 ?  132 PHE   A HD1  1 
ATOM   2741 H HD2  A PHE   A 1 132 ? 22.044 -1.441  -6.023  0.72 14.71 ?  132 PHE   A HD2  1 
ATOM   2742 H HD2  B PHE   A 1 132 ? 22.323 -1.345  -6.014  0.28 14.13 ?  132 PHE   A HD2  1 
ATOM   2743 H HE1  A PHE   A 1 132 ? 21.711 2.074   -3.046  0.72 16.24 ?  132 PHE   A HE1  1 
ATOM   2744 H HE1  B PHE   A 1 132 ? 21.660 2.171   -3.093  0.28 14.92 ?  132 PHE   A HE1  1 
ATOM   2745 H HE2  A PHE   A 1 132 ? 23.944 -0.592  -5.021  0.72 15.97 ?  132 PHE   A HE2  1 
ATOM   2746 H HE2  B PHE   A 1 132 ? 24.123 -0.394  -4.927  0.28 14.58 ?  132 PHE   A HE2  1 
ATOM   2747 H HZ   A PHE   A 1 132 ? 23.776 1.173   -3.529  0.72 16.10 ?  132 PHE   A HZ   1 
ATOM   2748 H HZ   B PHE   A 1 132 ? 23.794 1.367   -3.464  0.28 14.66 ?  132 PHE   A HZ   1 
ATOM   2749 N N    A GLY   A 1 133 ? 16.579 -0.521  -7.742  0.72 12.02 ?  133 GLY   A N    1 
ATOM   2750 N N    B GLY   A 1 133 ? 16.893 -0.638  -7.962  0.28 12.85 ?  133 GLY   A N    1 
ATOM   2751 C CA   A GLY   A 1 133 ? 15.804 -0.880  -8.912  0.72 12.92 ?  133 GLY   A CA   1 
ATOM   2752 C CA   B GLY   A 1 133 ? 16.123 -1.009  -9.129  0.28 13.31 ?  133 GLY   A CA   1 
ATOM   2753 C C    A GLY   A 1 133 ? 15.496 -2.346  -9.131  0.72 13.60 ?  133 GLY   A C    1 
ATOM   2754 C C    B GLY   A 1 133 ? 15.593 -2.430  -9.149  0.28 13.94 ?  133 GLY   A C    1 
ATOM   2755 O O    A GLY   A 1 133 ? 14.927 -2.672  -10.180 0.72 14.74 ?  133 GLY   A O    1 
ATOM   2756 O O    B GLY   A 1 133 ? 14.630 -2.700  -9.878  0.28 14.58 ?  133 GLY   A O    1 
ATOM   2757 H H    A GLY   A 1 133 ? 16.104 -0.286  -7.064  0.72 14.43 ?  133 GLY   A H    1 
ATOM   2758 H H    B GLY   A 1 133 ? 16.409 -0.456  -7.275  0.28 15.42 ?  133 GLY   A H    1 
ATOM   2759 H HA2  A GLY   A 1 133 ? 14.957 -0.414  -8.873  0.72 15.51 ?  133 GLY   A HA2  1 
ATOM   2760 H HA2  B GLY   A 1 133 ? 15.355 -0.424  -9.189  0.28 15.98 ?  133 GLY   A HA2  1 
ATOM   2761 H HA3  A GLY   A 1 133 ? 16.275 -0.573  -9.702  0.72 15.51 ?  133 GLY   A HA3  1 
ATOM   2762 H HA3  B GLY   A 1 133 ? 16.669 -0.864  -9.919  0.28 15.98 ?  133 GLY   A HA3  1 
ATOM   2763 N N    A ALA   A 1 134 ? 15.848 -3.241  -8.207  0.72 13.00 ?  134 ALA   A N    1 
ATOM   2764 N N    B ALA   A 1 134 ? 16.172 -3.337  -8.366  0.28 13.86 ?  134 ALA   A N    1 
ATOM   2765 C CA   A ALA   A 1 134 ? 15.488 -4.641  -8.370  0.72 13.31 ?  134 ALA   A CA   1 
ATOM   2766 C CA   B ALA   A 1 134 ? 15.836 -4.747  -8.492  0.28 14.12 ?  134 ALA   A CA   1 
ATOM   2767 C C    A ALA   A 1 134 ? 14.139 -4.933  -7.715  0.72 13.42 ?  134 ALA   A C    1 
ATOM   2768 C C    B ALA   A 1 134 ? 14.453 -5.036  -7.913  0.28 14.61 ?  134 ALA   A C    1 
ATOM   2769 O O    A ALA   A 1 134 ? 13.618 -4.147  -6.920  0.72 15.44 ?  134 ALA   A O    1 
ATOM   2770 O O    B ALA   A 1 134 ? 13.883 -4.246  -7.157  0.28 15.35 ?  134 ALA   A O    1 
ATOM   2771 C CB   A ALA   A 1 134 ? 16.560 -5.565  -7.794  0.72 14.00 ?  134 ALA   A CB   1 
ATOM   2772 C CB   B ALA   A 1 134 ? 16.885 -5.611  -7.791  0.28 14.39 ?  134 ALA   A CB   1 
ATOM   2773 H H    A ALA   A 1 134 ? 16.298 -3.062  -7.488  0.72 15.61 ?  134 ALA   A H    1 
ATOM   2774 H H    B ALA   A 1 134 ? 16.749 -3.158  -7.753  0.28 16.64 ?  134 ALA   A H    1 
ATOM   2775 H HA   A ALA   A 1 134 ? 15.408 -4.833  -9.314  0.72 15.98 ?  134 ALA   A HA   1 
ATOM   2776 H HA   B ALA   A 1 134 ? 15.825 -4.988  -9.429  0.28 16.94 ?  134 ALA   A HA   1 
ATOM   2777 H HB1  A ALA   A 1 134 ? 16.294 -6.484  -7.941  0.72 16.81 ?  134 ALA   A HB1  1 
ATOM   2778 H HB1  B ALA   A 1 134 ? 16.643 -6.545  -7.895  0.28 17.28 ?  134 ALA   A HB1  1 
ATOM   2779 H HB2  A ALA   A 1 134 ? 17.401 -5.387  -8.248  0.72 16.81 ?  134 ALA   A HB2  1 
ATOM   2780 H HB2  B ALA   A 1 134 ? 17.751 -5.447  -8.198  0.28 17.28 ?  134 ALA   A HB2  1 
ATOM   2781 H HB3  A ALA   A 1 134 ? 16.654 -5.391  -6.846  0.72 16.81 ?  134 ALA   A HB3  1 
ATOM   2782 H HB3  B ALA   A 1 134 ? 16.912 -5.377  -6.851  0.28 17.28 ?  134 ALA   A HB3  1 
ATOM   2783 N N    A ASP   A 1 135 ? 13.575 -6.081  -8.072  0.72 13.87 ?  135 ASP   A N    1 
ATOM   2784 N N    B ASP   A 1 135 ? 13.921 -6.197  -8.279  0.28 14.82 ?  135 ASP   A N    1 
ATOM   2785 C CA   A ASP   A 1 135 ? 12.328 -6.552  -7.477  0.72 15.70 ?  135 ASP   A CA   1 
ATOM   2786 C CA   B ASP   A 1 135 ? 12.622 -6.628  -7.780  0.28 15.40 ?  135 ASP   A CA   1 
ATOM   2787 C C    A ASP   A 1 135 ? 12.592 -7.007  -6.047  0.72 15.07 ?  135 ASP   A C    1 
ATOM   2788 C C    B ASP   A 1 135 ? 12.754 -7.031  -6.318  0.28 14.78 ?  135 ASP   A C    1 
ATOM   2789 O O    A ASP   A 1 135 ? 13.373 -7.946  -5.844  0.72 14.61 ?  135 ASP   A O    1 
ATOM   2790 O O    B ASP   A 1 135 ? 13.573 -7.902  -5.997  0.28 14.50 ?  135 ASP   A O    1 
ATOM   2791 C CB   A ASP   A 1 135 ? 11.828 -7.727  -8.311  0.72 18.33 ?  135 ASP   A CB   1 
ATOM   2792 C CB   B ASP   A 1 135 ? 12.116 -7.802  -8.610  0.28 17.41 ?  135 ASP   A CB   1 
ATOM   2793 C CG   A ASP   A 1 135 ? 10.534 -8.326  -7.791  0.72 20.79 ?  135 ASP   A CG   1 
ATOM   2794 C CG   B ASP   A 1 135 ? 10.898 -8.474  -7.994  0.28 19.12 ?  135 ASP   A CG   1 
ATOM   2795 O OD1  A ASP   A 1 135 ? 10.025 -7.873  -6.746  0.72 20.61 ?  135 ASP   A OD1  1 
ATOM   2796 O OD1  B ASP   A 1 135 ? 9.936  -7.759  -7.647  0.28 19.73 ?  135 ASP   A OD1  1 
ATOM   2797 O OD2  A ASP   A 1 135 ? 10.025 -9.255  -8.453  0.72 23.67 -1 135 ASP   A OD2  1 
ATOM   2798 O OD2  B ASP   A 1 135 ? 10.899 -9.717  -7.862  0.28 20.03 -1 135 ASP   A OD2  1 
ATOM   2799 H H    A ASP   A 1 135 ? 13.892 -6.611  -8.668  0.72 16.65 ?  135 ASP   A H    1 
ATOM   2800 H H    B ASP   A 1 135 ? 14.295 -6.757  -8.813  0.28 17.79 ?  135 ASP   A H    1 
ATOM   2801 H HA   A ASP   A 1 135 ? 11.659 -5.844  -7.495  0.72 18.84 ?  135 ASP   A HA   1 
ATOM   2802 H HA   B ASP   A 1 135 ? 11.991 -5.899  -7.862  0.28 18.48 ?  135 ASP   A HA   1 
ATOM   2803 H HB2  A ASP   A 1 135 ? 11.665 -7.428  -9.217  0.72 22.00 ?  135 ASP   A HB2  1 
ATOM   2804 H HB2  B ASP   A 1 135 ? 11.872 -7.477  -9.493  0.28 20.90 ?  135 ASP   A HB2  1 
ATOM   2805 H HB3  A ASP   A 1 135 ? 12.501 -8.424  -8.305  0.72 22.00 ?  135 ASP   A HB3  1 
ATOM   2806 H HB3  B ASP   A 1 135 ? 12.820 -8.463  -8.683  0.28 20.90 ?  135 ASP   A HB3  1 
ATOM   2807 N N    A PRO   A 1 136 ? 11.991 -6.380  -5.033  0.72 14.88 ?  136 PRO   A N    1 
ATOM   2808 N N    B PRO   A 1 136 ? 11.985 -6.435  -5.404  0.28 14.46 ?  136 PRO   A N    1 
ATOM   2809 C CA   A PRO   A 1 136 ? 12.250 -6.823  -3.652  0.72 14.70 ?  136 PRO   A CA   1 
ATOM   2810 C CA   B PRO   A 1 136 ? 12.185 -6.734  -3.978  0.28 14.26 ?  136 PRO   A CA   1 
ATOM   2811 C C    A PRO   A 1 136 ? 11.828 -8.255  -3.366  0.72 13.92 ?  136 PRO   A C    1 
ATOM   2812 C C    B PRO   A 1 136 ? 11.777 -8.143  -3.583  0.28 14.54 ?  136 PRO   A C    1 
ATOM   2813 O O    A PRO   A 1 136 ? 12.421 -8.892  -2.486  0.72 13.54 ?  136 PRO   A O    1 
ATOM   2814 O O    B PRO   A 1 136 ? 12.388 -8.714  -2.672  0.28 14.49 ?  136 PRO   A O    1 
ATOM   2815 C CB   A PRO   A 1 136 ? 11.473 -5.805  -2.804  0.72 16.00 ?  136 PRO   A CB   1 
ATOM   2816 C CB   B PRO   A 1 136 ? 11.343 -5.660  -3.276  0.28 14.21 ?  136 PRO   A CB   1 
ATOM   2817 C CG   A PRO   A 1 136 ? 10.441 -5.252  -3.727  0.72 17.05 ?  136 PRO   A CG   1 
ATOM   2818 C CG   B PRO   A 1 136 ? 10.279 -5.321  -4.272  0.28 14.61 ?  136 PRO   A CG   1 
ATOM   2819 C CD   A PRO   A 1 136 ? 11.076 -5.227  -5.079  0.72 15.86 ?  136 PRO   A CD   1 
ATOM   2820 C CD   B PRO   A 1 136 ? 10.921 -5.441  -5.622  0.28 14.71 ?  136 PRO   A CD   1 
ATOM   2821 H HA   A PRO   A 1 136 ? 13.197 -6.734  -3.452  0.72 17.64 ?  136 PRO   A HA   1 
ATOM   2822 H HA   B PRO   A 1 136 ? 13.117 -6.604  -3.737  0.28 17.11 ?  136 PRO   A HA   1 
ATOM   2823 H HB2  A PRO   A 1 136 ? 11.057 -6.258  -2.053  0.72 19.21 ?  136 PRO   A HB2  1 
ATOM   2824 H HB2  B PRO   A 1 136 ? 10.955 -6.018  -2.464  0.28 17.06 ?  136 PRO   A HB2  1 
ATOM   2825 H HB3  A PRO   A 1 136 ? 12.075 -5.110  -2.498  0.72 19.21 ?  136 PRO   A HB3  1 
ATOM   2826 H HB3  B PRO   A 1 136 ? 11.894 -4.882  -3.082  0.28 17.06 ?  136 PRO   A HB3  1 
ATOM   2827 H HG2  A PRO   A 1 136 ? 9.661  -5.828  -3.733  0.72 20.46 ?  136 PRO   A HG2  1 
ATOM   2828 H HG2  B PRO   A 1 136 ? 9.548  -5.949  -4.188  0.28 17.54 ?  136 PRO   A HG2  1 
ATOM   2829 H HG3  A PRO   A 1 136 ? 10.202 -4.354  -3.451  0.72 20.46 ?  136 PRO   A HG3  1 
ATOM   2830 H HG3  B PRO   A 1 136 ? 9.973  -4.414  -4.124  0.28 17.54 ?  136 PRO   A HG3  1 
ATOM   2831 H HD2  A PRO   A 1 136 ? 10.403 -5.356  -5.770  0.72 19.04 ?  136 PRO   A HD2  1 
ATOM   2832 H HD2  B PRO   A 1 136 ? 10.284 -5.769  -6.276  0.28 17.65 ?  136 PRO   A HD2  1 
ATOM   2833 H HD3  A PRO   A 1 136 ? 11.567 -4.401  -5.214  0.72 19.04 ?  136 PRO   A HD3  1 
ATOM   2834 H HD3  B PRO   A 1 136 ? 11.307 -4.594  -5.897  0.28 17.65 ?  136 PRO   A HD3  1 
ATOM   2835 N N    A ILE   A 1 137 ? 10.811 -8.773  -4.063  0.72 14.01 ?  137 ILE   A N    1 
ATOM   2836 N N    B ILE   A 1 137 ? 10.762 -8.722  -4.230  0.28 14.83 ?  137 ILE   A N    1 
ATOM   2837 C CA   A ILE   A 1 137 ? 10.429 -10.172 -3.886  0.72 14.44 ?  137 ILE   A CA   1 
ATOM   2838 C CA   B ILE   A 1 137 ? 10.410 -10.112 -3.950  0.28 15.09 ?  137 ILE   A CA   1 
ATOM   2839 C C    A ILE   A 1 137 ? 11.578 -11.082 -4.297  0.72 13.80 ?  137 ILE   A C    1 
ATOM   2840 C C    B ILE   A 1 137 ? 11.582 -11.023 -4.284  0.28 14.36 ?  137 ILE   A C    1 
ATOM   2841 O O    A ILE   A 1 137 ? 11.882 -12.074 -3.620  0.72 13.98 ?  137 ILE   A O    1 
ATOM   2842 O O    B ILE   A 1 137 ? 11.900 -11.961 -3.542  0.28 14.35 ?  137 ILE   A O    1 
ATOM   2843 C CB   A ILE   A 1 137 ? 9.131  -10.483 -4.660  0.72 16.01 ?  137 ILE   A CB   1 
ATOM   2844 C CB   B ILE   A 1 137 ? 9.138  -10.509 -4.725  0.28 16.44 ?  137 ILE   A CB   1 
ATOM   2845 C CG1  A ILE   A 1 137 ? 7.967  -9.625  -4.145  0.72 18.13 ?  137 ILE   A CG1  1 
ATOM   2846 C CG1  B ILE   A 1 137 ? 7.945  -9.664  -4.273  0.28 17.77 ?  137 ILE   A CG1  1 
ATOM   2847 C CG2  A ILE   A 1 137 ? 8.788  -11.969 -4.553  0.72 16.79 ?  137 ILE   A CG2  1 
ATOM   2848 C CG2  B ILE   A 1 137 ? 8.846  -11.992 -4.549  0.28 16.77 ?  137 ILE   A CG2  1 
ATOM   2849 C CD1  A ILE   A 1 137 ? 6.678  -9.802  -4.929  0.72 18.92 ?  137 ILE   A CD1  1 
ATOM   2850 C CD1  B ILE   A 1 137 ? 7.506  -8.647  -5.297  0.28 18.60 ?  137 ILE   A CD1  1 
ATOM   2851 H H    A ILE   A 1 137 ? 10.333 -8.340  -4.632  0.72 16.82 ?  137 ILE   A H    1 
ATOM   2852 H H    B ILE   A 1 137 ? 10.277 -8.337  -4.829  0.28 17.80 ?  137 ILE   A H    1 
ATOM   2853 H HA   A ILE   A 1 137 ? 10.258 -10.334 -2.951  0.72 17.33 ?  137 ILE   A HA   1 
ATOM   2854 H HA   B ILE   A 1 137 ? 10.224 -10.202 -3.006  0.28 18.11 ?  137 ILE   A HA   1 
ATOM   2855 H HB   A ILE   A 1 137 ? 9.271  -10.272 -5.595  0.72 19.22 ?  137 ILE   A HB   1 
ATOM   2856 H HB   B ILE   A 1 137 ? 9.290  -10.339 -5.667  0.28 19.73 ?  137 ILE   A HB   1 
ATOM   2857 H HG12 A ILE   A 1 137 ? 7.792  -9.857  -3.220  0.72 21.77 ?  137 ILE   A HG12 1 
ATOM   2858 H HG12 B ILE   A 1 137 ? 7.193  -10.249 -4.095  0.28 21.34 ?  137 ILE   A HG12 1 
ATOM   2859 H HG13 A ILE   A 1 137 ? 8.222  -8.687  -4.204  0.72 21.77 ?  137 ILE   A HG13 1 
ATOM   2860 H HG13 B ILE   A 1 137 ? 8.188  -9.185  -3.466  0.28 21.34 ?  137 ILE   A HG13 1 
ATOM   2861 H HG21 A ILE   A 1 137 ? 7.916  -12.137 -4.943  0.72 20.15 ?  137 ILE   A HG21 1 
ATOM   2862 H HG21 B ILE   A 1 137 ? 7.959  -12.181 -4.895  0.28 20.12 ?  137 ILE   A HG21 1 
ATOM   2863 H HG22 A ILE   A 1 137 ? 9.456  -12.481 -5.030  0.72 20.15 ?  137 ILE   A HG22 1 
ATOM   2864 H HG22 B ILE   A 1 137 ? 9.505  -12.506 -5.041  0.28 20.12 ?  137 ILE   A HG22 1 
ATOM   2865 H HG23 A ILE   A 1 137 ? 8.781  -12.219 -3.618  0.72 20.15 ?  137 ILE   A HG23 1 
ATOM   2866 H HG23 B ILE   A 1 137 ? 8.887  -12.212 -3.606  0.28 20.12 ?  137 ILE   A HG23 1 
ATOM   2867 H HD11 A ILE   A 1 137 ? 5.968  -10.053 -4.317  0.72 22.71 ?  137 ILE   A HD11 1 
ATOM   2868 H HD11 B ILE   A 1 137 ? 6.948  -7.983  -4.862  0.28 22.33 ?  137 ILE   A HD11 1 
ATOM   2869 H HD12 A ILE   A 1 137 ? 6.470  -8.965  -5.362  0.72 22.71 ?  137 ILE   A HD12 1 
ATOM   2870 H HD12 B ILE   A 1 137 ? 8.290  -8.222  -5.676  0.28 22.33 ?  137 ILE   A HD12 1 
ATOM   2871 H HD13 A ILE   A 1 137 ? 6.797  -10.491 -5.601  0.72 22.71 ?  137 ILE   A HD13 1 
ATOM   2872 H HD13 B ILE   A 1 137 ? 7.005  -9.097  -5.995  0.28 22.33 ?  137 ILE   A HD13 1 
ATOM   2873 N N    . HIS   A 1 138 ? 12.237 -10.756 -5.413  1.00 14.15 ?  138 HIS   A N    1 
ATOM   2874 C CA   . HIS   A 1 138 ? 13.410 -11.519 -5.817  1.00 14.06 ?  138 HIS   A CA   1 
ATOM   2875 C C    . HIS   A 1 138 ? 14.549 -11.368 -4.813  1.00 13.26 ?  138 HIS   A C    1 
ATOM   2876 O O    . HIS   A 1 138 ? 15.217 -12.352 -4.468  1.00 13.67 ?  138 HIS   A O    1 
ATOM   2877 C CB   . HIS   A 1 138 ? 13.832 -11.075 -7.215  1.00 14.91 ?  138 HIS   A CB   1 
ATOM   2878 C CG   . HIS   A 1 138 ? 15.100 -11.709 -7.679  1.00 15.67 ?  138 HIS   A CG   1 
ATOM   2879 N ND1  . HIS   A 1 138 ? 15.209 -13.061 -7.923  1.00 17.35 ?  138 HIS   A ND1  1 
ATOM   2880 C CD2  . HIS   A 1 138 ? 16.321 -11.181 -7.922  1.00 15.97 ?  138 HIS   A CD2  1 
ATOM   2881 C CE1  . HIS   A 1 138 ? 16.443 -13.337 -8.308  1.00 17.74 ?  138 HIS   A CE1  1 
ATOM   2882 N NE2  . HIS   A 1 138 ? 17.138 -12.214 -8.318  1.00 16.71 ?  138 HIS   A NE2  1 
ATOM   2883 H H    A HIS   A 1 138 ? 12.028 -10.105 -5.944  0.72 16.99 ?  138 HIS   A H    1 
ATOM   2884 H H    B HIS   A 1 138 ? 12.015 -10.134 -5.973  0.28 16.99 ?  138 HIS   A H    1 
ATOM   2885 H HA   . HIS   A 1 138 ? 13.171 -12.456 -5.868  1.00 16.88 ?  138 HIS   A HA   1 
ATOM   2886 H HB2  . HIS   A 1 138 ? 13.129 -11.314 -7.850  1.00 17.89 ?  138 HIS   A HB2  1 
ATOM   2887 H HB3  . HIS   A 1 138 ? 13.959 -10.115 -7.221  1.00 17.89 ?  138 HIS   A HB3  1 
ATOM   2888 H HD1  . HIS   A 1 138 ? 14.570 -13.637 -7.843  1.00 20.82 ?  138 HIS   A HD1  1 
ATOM   2889 H HD2  . HIS   A 1 138 ? 16.557 -10.288 -7.846  1.00 19.17 ?  138 HIS   A HD2  1 
ATOM   2890 H HE1  . HIS   A 1 138 ? 16.763 -14.181 -8.533  1.00 21.29 ?  138 HIS   A HE1  1 
ATOM   2891 N N    . SER   A 1 139 ? 14.792 -10.148 -4.337  1.00 12.87 ?  139 SER   A N    1 
ATOM   2892 C CA   . SER   A 1 139 ? 15.858 -9.953  -3.362  1.00 12.81 ?  139 SER   A CA   1 
ATOM   2893 C C    . SER   A 1 139 ? 15.635 -10.798 -2.112  1.00 12.15 ?  139 SER   A C    1 
ATOM   2894 O O    . SER   A 1 139 ? 16.583 -11.388 -1.578  1.00 12.32 ?  139 SER   A O    1 
ATOM   2895 C CB   . SER   A 1 139 ? 15.994 -8.473  -3.009  1.00 12.65 ?  139 SER   A CB   1 
ATOM   2896 O OG   . SER   A 1 139 ? 17.072 -8.310  -2.103  1.00 13.09 ?  139 SER   A OG   1 
ATOM   2897 H H    . SER   A 1 139 ? 14.364 -9.434  -4.557  1.00 15.45 ?  139 SER   A H    1 
ATOM   2898 H HA   . SER   A 1 139 ? 16.696 -10.232 -3.762  1.00 15.38 ?  139 SER   A HA   1 
ATOM   2899 H HB2  . SER   A 1 139 ? 16.173 -7.961  -3.818  1.00 15.18 ?  139 SER   A HB2  1 
ATOM   2900 H HB3  . SER   A 1 139 ? 15.171 -8.163  -2.597  1.00 15.18 ?  139 SER   A HB3  1 
ATOM   2901 H HG   . SER   A 1 139 ? 17.159 -7.496  -1.899  1.00 15.72 ?  139 SER   A HG   1 
ATOM   2902 N N    . LEU   A 1 140 ? 14.395 -10.859 -1.622  1.00 12.17 ?  140 LEU   A N    1 
ATOM   2903 C CA   . LEU   A 1 140 ? 14.117 -11.673 -0.442  1.00 11.86 ?  140 LEU   A CA   1 
ATOM   2904 C C    . LEU   A 1 140 ? 14.387 -13.148 -0.717  1.00 12.13 ?  140 LEU   A C    1 
ATOM   2905 O O    . LEU   A 1 140 ? 14.939 -13.859 0.135   1.00 12.88 ?  140 LEU   A O    1 
ATOM   2906 C CB   . LEU   A 1 140 ? 12.678 -11.442 0.022   1.00 12.44 ?  140 LEU   A CB   1 
ATOM   2907 C CG   . LEU   A 1 140 ? 12.220 -12.274 1.218   1.00 12.82 ?  140 LEU   A CG   1 
ATOM   2908 C CD1  . LEU   A 1 140 ? 13.124 -12.094 2.433   1.00 13.49 ?  140 LEU   A CD1  1 
ATOM   2909 C CD2  . LEU   A 1 140 ? 10.766 -11.958 1.574   1.00 13.77 ?  140 LEU   A CD2  1 
ATOM   2910 H H    . LEU   A 1 140 ? 13.713 -10.441 -1.944  1.00 14.61 ?  140 LEU   A H    1 
ATOM   2911 H HA   . LEU   A 1 140 ? 14.704 -11.394 0.273   1.00 14.24 ?  140 LEU   A HA   1 
ATOM   2912 H HB2  . LEU   A 1 140 ? 12.579 -10.513 0.265   1.00 14.94 ?  140 LEU   A HB2  1 
ATOM   2913 H HB3  . LEU   A 1 140 ? 12.082 -11.652 -0.715  1.00 14.94 ?  140 LEU   A HB3  1 
ATOM   2914 H HG   . LEU   A 1 140 ? 12.249 -13.213 0.972   1.00 15.39 ?  140 LEU   A HG   1 
ATOM   2915 H HD11 . LEU   A 1 140 ? 12.747 -12.583 3.183   1.00 16.19 ?  140 LEU   A HD11 1 
ATOM   2916 H HD12 . LEU   A 1 140 ? 14.005 -12.449 2.223   1.00 16.19 ?  140 LEU   A HD12 1 
ATOM   2917 H HD13 . LEU   A 1 140 ? 13.186 -11.155 2.646   1.00 16.19 ?  140 LEU   A HD13 1 
ATOM   2918 H HD21 . LEU   A 1 140 ? 10.499 -12.507 2.336   1.00 16.53 ?  140 LEU   A HD21 1 
ATOM   2919 H HD22 . LEU   A 1 140 ? 10.690 -11.021 1.806   1.00 16.53 ?  140 LEU   A HD22 1 
ATOM   2920 H HD23 . LEU   A 1 140 ? 10.199 -12.161 0.814   1.00 16.53 ?  140 LEU   A HD23 1 
ATOM   2921 N N    . ARG   A 1 141 ? 14.005 -13.625 -1.906  1.00 12.37 ?  141 ARG   A N    1 
ATOM   2922 C CA   . ARG   A 1 141 ? 14.245 -15.017 -2.267  1.00 13.63 ?  141 ARG   A CA   1 
ATOM   2923 C C    . ARG   A 1 141 ? 15.740 -15.322 -2.283  1.00 13.07 ?  141 ARG   A C    1 
ATOM   2924 O O    . ARG   A 1 141 ? 16.192 -16.331 -1.726  1.00 13.24 ?  141 ARG   A O    1 
ATOM   2925 C CB   . ARG   A 1 141 ? 13.623 -15.285 -3.639  1.00 15.47 ?  141 ARG   A CB   1 
ATOM   2926 C CG   . ARG   A 1 141 ? 13.620 -16.734 -4.075  1.00 18.43 ?  141 ARG   A CG   1 
ATOM   2927 C CD   . ARG   A 1 141 ? 12.583 -17.499 -3.317  1.00 20.58 ?  141 ARG   A CD   1 
ATOM   2928 N NE   . ARG   A 1 141 ? 13.186 -18.283 -2.253  1.00 21.36 ?  141 ARG   A NE   1 
ATOM   2929 C CZ   . ARG   A 1 141 ? 12.500 -18.836 -1.261  1.00 21.91 ?  141 ARG   A CZ   1 
ATOM   2930 N NH1  . ARG   A 1 141 ? 11.213 -18.584 -1.085  1.00 21.08 ?  141 ARG   A NH1  1 
ATOM   2931 N NH2  . ARG   A 1 141 ? 13.124 -19.656 -0.421  1.00 23.27 ?  141 ARG   A NH2  1 
ATOM   2932 H H    . ARG   A 1 141 ? 13.608 -13.162 -2.518  1.00 14.85 ?  141 ARG   A H    1 
ATOM   2933 H HA   . ARG   A 1 141 ? 13.823 -15.598 -1.620  1.00 16.37 ?  141 ARG   A HA   1 
ATOM   2934 H HB2  . ARG   A 1 141 ? 12.704 -14.975 -3.629  1.00 18.57 ?  141 ARG   A HB2  1 
ATOM   2935 H HB3  . ARG   A 1 141 ? 14.122 -14.783 -4.304  1.00 18.57 ?  141 ARG   A HB3  1 
ATOM   2936 H HG2  . ARG   A 1 141 ? 13.415 -16.789 -5.023  1.00 22.12 ?  141 ARG   A HG2  1 
ATOM   2937 H HG3  . ARG   A 1 141 ? 14.490 -17.132 -3.897  1.00 22.12 ?  141 ARG   A HG3  1 
ATOM   2938 H HD2  . ARG   A 1 141 ? 11.954 -16.881 -2.909  1.00 24.70 ?  141 ARG   A HD2  1 
ATOM   2939 H HD3  . ARG   A 1 141 ? 12.114 -18.097 -3.923  1.00 24.70 ?  141 ARG   A HD3  1 
ATOM   2940 H HE   . ARG   A 1 141 ? 14.010 -18.506 -2.338  1.00 25.64 ?  141 ARG   A HE   1 
ATOM   2941 H HH11 . ARG   A 1 141 ? 10.792 -18.067 -1.628  1.00 25.30 ?  141 ARG   A HH11 1 
ATOM   2942 H HH12 . ARG   A 1 141 ? 10.787 -18.950 -0.430  1.00 25.30 ?  141 ARG   A HH12 1 
ATOM   2943 H HH21 . ARG   A 1 141 ? 13.960 -19.825 -0.524  1.00 27.93 ?  141 ARG   A HH21 1 
ATOM   2944 H HH22 . ARG   A 1 141 ? 12.693 -20.009 0.238   1.00 27.93 ?  141 ARG   A HH22 1 
ATOM   2945 N N    . VAL   A 1 142 ? 16.532 -14.455 -2.920  1.00 12.60 ?  142 VAL   A N    1 
ATOM   2946 C CA   . VAL   A 1 142 ? 17.979 -14.664 -2.947  1.00 12.59 ?  142 VAL   A CA   1 
ATOM   2947 C C    . VAL   A 1 142 ? 18.547 -14.648 -1.534  1.00 11.96 ?  142 VAL   A C    1 
ATOM   2948 O O    . VAL   A 1 142 ? 19.409 -15.465 -1.187  1.00 12.53 ?  142 VAL   A O    1 
ATOM   2949 C CB   . VAL   A 1 142 ? 18.676 -13.645 -3.869  1.00 12.70 ?  142 VAL   A CB   1 
ATOM   2950 C CG1  . VAL   A 1 142 ? 20.190 -13.851 -3.815  1.00 13.15 ?  142 VAL   A CG1  1 
ATOM   2951 C CG2  . VAL   A 1 142 ? 18.187 -13.788 -5.298  1.00 14.56 ?  142 VAL   A CG2  1 
ATOM   2952 H H    . VAL   A 1 142 ? 16.263 -13.742 -3.330  1.00 15.13 ?  142 VAL   A H    1 
ATOM   2953 H HA   . VAL   A 1 142 ? 18.149 -15.537 -3.315  1.00 15.11 ?  142 VAL   A HA   1 
ATOM   2954 H HB   . VAL   A 1 142 ? 18.485 -12.739 -3.569  1.00 15.25 ?  142 VAL   A HB   1 
ATOM   2955 H HG11 . VAL   A 1 142 ? 20.603 -13.367 -4.550  1.00 15.79 ?  142 VAL   A HG11 1 
ATOM   2956 H HG12 . VAL   A 1 142 ? 20.531 -13.509 -2.971  1.00 15.79 ?  142 VAL   A HG12 1 
ATOM   2957 H HG13 . VAL   A 1 142 ? 20.384 -14.796 -3.892  1.00 15.79 ?  142 VAL   A HG13 1 
ATOM   2958 H HG21 . VAL   A 1 142 ? 18.662 -13.151 -5.857  1.00 17.48 ?  142 VAL   A HG21 1 
ATOM   2959 H HG22 . VAL   A 1 142 ? 18.372 -14.691 -5.598  1.00 17.48 ?  142 VAL   A HG22 1 
ATOM   2960 H HG23 . VAL   A 1 142 ? 17.239 -13.611 -5.322  1.00 17.48 ?  142 VAL   A HG23 1 
ATOM   2961 N N    . CYS   A 1 143 ? 18.083 -13.717 -0.699  1.00 11.95 ?  143 CYS   A N    1 
ATOM   2962 C CA   . CYS   A 1 143 ? 18.539 -13.667 0.687   1.00 11.87 ?  143 CYS   A CA   1 
ATOM   2963 C C    . CYS   A 1 143 ? 18.315 -15.010 1.380   1.00 12.00 ?  143 CYS   A C    1 
ATOM   2964 O O    . CYS   A 1 143 ? 19.237 -15.596 1.955   1.00 12.12 ?  143 CYS   A O    1 
ATOM   2965 C CB   . CYS   A 1 143 ? 17.799 -12.556 1.427   1.00 12.46 ?  143 CYS   A CB   1 
ATOM   2966 S SG   . CYS   A 1 143 ? 18.298 -12.377 3.154   1.00 12.95 ?  143 CYS   A SG   1 
ATOM   2967 H H    . CYS   A 1 143 ? 17.504 -13.118 -0.904  1.00 14.35 ?  143 CYS   A H    1 
ATOM   2968 H HA   . CYS   A 1 143 ? 19.489 -13.473 0.706   1.00 14.24 ?  143 CYS   A HA   1 
ATOM   2969 H HB2  . CYS   A 1 143 ? 17.961 -11.717 0.976   1.00 14.96 ?  143 CYS   A HB2  1 
ATOM   2970 H HB3  . CYS   A 1 143 ? 16.851 -12.757 1.414   1.00 14.96 ?  143 CYS   A HB3  1 
ATOM   2971 H HG   . CYS   A 1 143 ? 17.727 -11.432 3.618   1.00 15.55 ?  143 CYS   A HG   1 
ATOM   2972 N N    . VAL   A 1 144 ? 17.087 -15.518 1.321   1.00 12.58 ?  144 VAL   A N    1 
ATOM   2973 C CA   . VAL   A 1 144 ? 16.750 -16.750 2.025   1.00 13.87 ?  144 VAL   A CA   1 
ATOM   2974 C C    . VAL   A 1 144 ? 17.565 -17.918 1.496   1.00 13.45 ?  144 VAL   A C    1 
ATOM   2975 O O    . VAL   A 1 144 ? 17.933 -18.827 2.254   1.00 14.27 ?  144 VAL   A O    1 
ATOM   2976 C CB   . VAL   A 1 144 ? 15.231 -16.991 1.917   1.00 17.15 ?  144 VAL   A CB   1 
ATOM   2977 C CG1  . VAL   A 1 144 ? 14.872 -18.429 2.236   1.00 19.34 ?  144 VAL   A CG1  1 
ATOM   2978 C CG2  . VAL   A 1 144 ? 14.488 -15.997 2.814   1.00 16.82 ?  144 VAL   A CG2  1 
ATOM   2979 H H    . VAL   A 1 144 ? 16.434 -15.163 0.883   1.00 15.10 ?  144 VAL   A H    1 
ATOM   2980 H HA   . VAL   A 1 144 ? 16.958 -16.639 2.960   1.00 16.65 ?  144 VAL   A HA   1 
ATOM   2981 H HB   . VAL   A 1 144 ? 14.949 -16.812 1.000   1.00 20.58 ?  144 VAL   A HB   1 
ATOM   2982 H HG11 . VAL   A 1 144 ? 13.921 -18.480 2.428   1.00 23.22 ?  144 VAL   A HG11 1 
ATOM   2983 H HG12 . VAL   A 1 144 ? 15.082 -18.985 1.470   1.00 23.22 ?  144 VAL   A HG12 1 
ATOM   2984 H HG13 . VAL   A 1 144 ? 15.380 -18.713 3.009   1.00 23.22 ?  144 VAL   A HG13 1 
ATOM   2985 H HG21 . VAL   A 1 144 ? 13.531 -16.151 2.743   1.00 20.19 ?  144 VAL   A HG21 1 
ATOM   2986 H HG22 . VAL   A 1 144 ? 14.775 -16.120 3.731   1.00 20.19 ?  144 VAL   A HG22 1 
ATOM   2987 H HG23 . VAL   A 1 144 ? 14.692 -15.089 2.525   1.00 20.19 ?  144 VAL   A HG23 1 
ATOM   2988 N N    . ASP   A 1 145 ? 17.829 -17.938 0.189   1.00 13.80 ?  145 ASP   A N    1 
ATOM   2989 C CA   . ASP   A 1 145 ? 18.539 -19.044 -0.444  1.00 14.33 ?  145 ASP   A CA   1 
ATOM   2990 C C    . ASP   A 1 145 ? 20.060 -18.899 -0.395  1.00 14.14 ?  145 ASP   A C    1 
ATOM   2991 O O    . ASP   A 1 145 ? 20.765 -19.798 -0.865  1.00 16.38 ?  145 ASP   A O    1 
ATOM   2992 C CB   . ASP   A 1 145 ? 18.089 -19.192 -1.902  1.00 16.10 ?  145 ASP   A CB   1 
ATOM   2993 C CG   . ASP   A 1 145 ? 16.635 -19.617 -2.029  1.00 18.50 ?  145 ASP   A CG   1 
ATOM   2994 O OD1  . ASP   A 1 145 ? 16.075 -20.158 -1.051  1.00 18.56 ?  145 ASP   A OD1  1 
ATOM   2995 O OD2  . ASP   A 1 145 ? 16.052 -19.404 -3.112  1.00 19.99 -1 145 ASP   A OD2  1 
ATOM   2996 H H    . ASP   A 1 145 ? 17.586 -17.320 -0.363  1.00 16.56 ?  145 ASP   A H    1 
ATOM   2997 H HA   . ASP   A 1 145 ? 18.304 -19.863 0.018   1.00 17.21 ?  145 ASP   A HA   1 
ATOM   2998 H HB2  . ASP   A 1 145 ? 18.198 -18.343 -2.357  1.00 19.33 ?  145 ASP   A HB2  1 
ATOM   2999 H HB3  . ASP   A 1 145 ? 18.632 -19.872 -2.331  1.00 19.33 ?  145 ASP   A HB3  1 
ATOM   3000 N N    . THR   A 1 146 ? 20.583 -17.806 0.158   1.00 12.48 ?  146 THR   A N    1 
ATOM   3001 C CA   . THR   A 1 146 ? 22.023 -17.556 0.175   1.00 12.28 ?  146 THR   A CA   1 
ATOM   3002 C C    . THR   A 1 146 ? 22.576 -17.377 1.578   1.00 12.07 ?  146 THR   A C    1 
ATOM   3003 O O    . THR   A 1 146 ? 23.654 -17.907 1.886   1.00 13.20 ?  146 THR   A O    1 
ATOM   3004 C CB   . THR   A 1 146 ? 22.354 -16.307 -0.666  1.00 12.24 ?  146 THR   A CB   1 
ATOM   3005 O OG1  . THR   A 1 146 ? 21.821 -16.471 -1.979  1.00 12.82 ?  146 THR   A OG1  1 
ATOM   3006 C CG2  . THR   A 1 146 ? 23.855 -16.077 -0.760  1.00 12.93 ?  146 THR   A CG2  1 
ATOM   3007 H H    . THR   A 1 146 ? 20.117 -17.179 0.520   1.00 14.99 ?  146 THR   A H    1 
ATOM   3008 H HA   . THR   A 1 146 ? 22.479 -18.310 -0.224  1.00 14.75 ?  146 THR   A HA   1 
ATOM   3009 H HB   . THR   A 1 146 ? 21.960 -15.524 -0.247  1.00 14.70 ?  146 THR   A HB   1 
ATOM   3010 H HG1  . THR   A 1 146 ? 20.981 -16.529 -1.938  1.00 15.39 ?  146 THR   A HG1  1 
ATOM   3011 H HG21 . THR   A 1 146 ? 24.044 -15.401 -1.426  1.00 15.52 ?  146 THR   A HG21 1 
ATOM   3012 H HG22 . THR   A 1 146 ? 24.204 -15.786 0.096   1.00 15.52 ?  146 THR   A HG22 1 
ATOM   3013 H HG23 . THR   A 1 146 ? 24.296 -16.904 -1.017  1.00 15.52 ?  146 THR   A HG23 1 
ATOM   3014 N N    . VAL   A 1 147 ? 21.899 -16.595 2.414   1.00 11.95 ?  147 VAL   A N    1 
ATOM   3015 C CA   . VAL   A 1 147 ? 22.387 -16.296 3.751   1.00 12.29 ?  147 VAL   A CA   1 
ATOM   3016 C C    . VAL   A 1 147 ? 22.065 -17.464 4.669   1.00 12.63 ?  147 VAL   A C    1 
ATOM   3017 O O    . VAL   A 1 147 ? 20.927 -17.942 4.715   1.00 13.09 ?  147 VAL   A O    1 
ATOM   3018 C CB   . VAL   A 1 147 ? 21.771 -14.990 4.271   1.00 12.49 ?  147 VAL   A CB   1 
ATOM   3019 C CG1  . VAL   A 1 147 ? 22.315 -14.677 5.649   1.00 13.56 ?  147 VAL   A CG1  1 
ATOM   3020 C CG2  . VAL   A 1 147 ? 22.039 -13.846 3.302   1.00 12.76 ?  147 VAL   A CG2  1 
ATOM   3021 H H    . VAL   A 1 147 ? 21.139 -16.230 2.230   1.00 14.35 ?  147 VAL   A H    1 
ATOM   3022 H HA   . VAL   A 1 147 ? 23.350 -16.188 3.718   1.00 14.75 ?  147 VAL   A HA   1 
ATOM   3023 H HB   . VAL   A 1 147 ? 20.814 -15.100 4.349   1.00 15.00 ?  147 VAL   A HB   1 
ATOM   3024 H HG11 . VAL   A 1 147 ? 22.072 -13.772 5.886   1.00 16.28 ?  147 VAL   A HG11 1 
ATOM   3025 H HG12 . VAL   A 1 147 ? 21.934 -15.301 6.289   1.00 16.28 ?  147 VAL   A HG12 1 
ATOM   3026 H HG13 . VAL   A 1 147 ? 23.282 -14.769 5.635   1.00 16.28 ?  147 VAL   A HG13 1 
ATOM   3027 H HG21 . VAL   A 1 147 ? 21.716 -13.020 3.696   1.00 15.32 ?  147 VAL   A HG21 1 
ATOM   3028 H HG22 . VAL   A 1 147 ? 22.992 -13.786 3.140   1.00 15.32 ?  147 VAL   A HG22 1 
ATOM   3029 H HG23 . VAL   A 1 147 ? 21.570 -14.023 2.473   1.00 15.32 ?  147 VAL   A HG23 1 
ATOM   3030 N N    . ARG   A 1 148 ? 23.085 -17.940 5.381   1.00 13.06 ?  148 ARG   A N    1 
ATOM   3031 C CA   . ARG   A 1 148 ? 22.954 -19.017 6.347   1.00 12.94 ?  148 ARG   A CA   1 
ATOM   3032 C C    . ARG   A 1 148 ? 23.079 -18.542 7.783   1.00 13.44 ?  148 ARG   A C    1 
ATOM   3033 O O    . ARG   A 1 148 ? 22.673 -19.269 8.696   1.00 15.09 ?  148 ARG   A O    1 
ATOM   3034 C CB   . ARG   A 1 148 ? 23.997 -20.110 6.069   1.00 13.38 ?  148 ARG   A CB   1 
ATOM   3035 C CG   . ARG   A 1 148 ? 23.836 -20.759 4.704   1.00 14.89 ?  148 ARG   A CG   1 
ATOM   3036 C CD   . ARG   A 1 148 ? 24.927 -21.787 4.412   1.00 16.07 ?  148 ARG   A CD   1 
ATOM   3037 N NE   . ARG   A 1 148 ? 26.266 -21.208 4.441   1.00 15.81 ?  148 ARG   A NE   1 
ATOM   3038 C CZ   . ARG   A 1 148 ? 26.782 -20.468 3.468   1.00 15.19 ?  148 ARG   A CZ   1 
ATOM   3039 N NH1  . ARG   A 1 148 ? 26.111 -20.229 2.353   1.00 15.60 ?  148 ARG   A NH1  1 
ATOM   3040 N NH2  . ARG   A 1 148 ? 27.998 -19.940 3.622   1.00 15.53 ?  148 ARG   A NH2  1 
ATOM   3041 H H    . ARG   A 1 148 ? 23.896 -17.640 5.307   1.00 15.68 ?  148 ARG   A H    1 
ATOM   3042 H HA   . ARG   A 1 148 ? 22.083 -19.416 6.242   1.00 15.54 ?  148 ARG   A HA   1 
ATOM   3043 H HB2  . ARG   A 1 148 ? 24.885 -19.731 6.113   1.00 16.07 ?  148 ARG   A HB2  1 
ATOM   3044 H HB3  . ARG   A 1 148 ? 23.903 -20.813 6.735   1.00 16.07 ?  148 ARG   A HB3  1 
ATOM   3045 H HG2  . ARG   A 1 148 ? 22.977 -21.205 4.663   1.00 17.88 ?  148 ARG   A HG2  1 
ATOM   3046 H HG3  . ARG   A 1 148 ? 23.883 -20.067 4.022   1.00 17.88 ?  148 ARG   A HG3  1 
ATOM   3047 H HD2  . ARG   A 1 148 ? 24.888 -22.487 5.081   1.00 19.29 ?  148 ARG   A HD2  1 
ATOM   3048 H HD3  . ARG   A 1 148 ? 24.778 -22.165 3.529   1.00 19.29 ?  148 ARG   A HD3  1 
ATOM   3049 H HE   . ARG   A 1 148 ? 26.753 -21.359 5.130   1.00 18.98 ?  148 ARG   A HE   1 
ATOM   3050 H HH11 . ARG   A 1 148 ? 25.324 -20.552 2.242   1.00 18.72 ?  148 ARG   A HH11 1 
ATOM   3051 H HH12 . ARG   A 1 148 ? 26.462 -19.736 1.738   1.00 18.72 ?  148 ARG   A HH12 1 
ATOM   3052 H HH21 . ARG   A 1 148 ? 28.440 -20.085 4.344   1.00 18.64 ?  148 ARG   A HH21 1 
ATOM   3053 H HH22 . ARG   A 1 148 ? 28.339 -19.452 3.000   1.00 18.64 ?  148 ARG   A HH22 1 
ATOM   3054 N N    . THR   A 1 149 ? 23.634 -17.353 7.998   1.00 13.52 ?  149 THR   A N    1 
ATOM   3055 C CA   . THR   A 1 149 ? 23.711 -16.749 9.315   1.00 13.62 ?  149 THR   A CA   1 
ATOM   3056 C C    . THR   A 1 149 ? 22.390 -16.041 9.624   1.00 13.03 ?  149 THR   A C    1 
ATOM   3057 O O    . THR   A 1 149 ? 21.450 -16.039 8.819   1.00 13.60 ?  149 THR   A O    1 
ATOM   3058 C CB   . THR   A 1 149 ? 24.914 -15.816 9.374   1.00 13.95 ?  149 THR   A CB   1 
ATOM   3059 O OG1  . THR   A 1 149 ? 24.792 -14.879 8.301   1.00 14.01 ?  149 THR   A OG1  1 
ATOM   3060 C CG2  . THR   A 1 149 ? 26.224 -16.610 9.247   1.00 14.36 ?  149 THR   A CG2  1 
ATOM   3061 H H    . THR   A 1 149 ? 23.981 -16.865 7.377   1.00 16.23 ?  149 THR   A H    1 
ATOM   3062 H HA   . THR   A 1 149 ? 23.837 -17.450 9.974   1.00 16.35 ?  149 THR   A HA   1 
ATOM   3063 H HB   . THR   A 1 149 ? 24.911 -15.344 10.218  1.00 16.75 ?  149 THR   A HB   1 
ATOM   3064 H HG1  . THR   A 1 149 ? 25.448 -14.355 8.303   1.00 16.82 ?  149 THR   A HG1  1 
ATOM   3065 H HG21 . THR   A 1 149 ? 26.982 -16.010 9.302   1.00 17.24 ?  149 THR   A HG21 1 
ATOM   3066 H HG22 . THR   A 1 149 ? 26.288 -17.266 9.963   1.00 17.24 ?  149 THR   A HG22 1 
ATOM   3067 H HG23 . THR   A 1 149 ? 26.253 -17.077 8.395   1.00 17.24 ?  149 THR   A HG23 1 
ATOM   3068 N N    . ASN   A 1 150 ? 22.270 -15.502 10.832  1.00 13.13 ?  150 ASN   A N    1 
ATOM   3069 C CA   . ASN   A 1 150 ? 20.989 -14.985 11.315  1.00 13.64 ?  150 ASN   A CA   1 
ATOM   3070 C C    . ASN   A 1 150 ? 20.806 -13.544 10.860  1.00 13.05 ?  150 ASN   A C    1 
ATOM   3071 O O    . ASN   A 1 150 ? 21.557 -12.652 11.278  1.00 14.59 ?  150 ASN   A O    1 
ATOM   3072 C CB   . ASN   A 1 150 ? 20.929 -15.098 12.832  1.00 16.14 ?  150 ASN   A CB   1 
ATOM   3073 C CG   . ASN   A 1 150 ? 20.817 -16.528 13.293  1.00 20.65 ?  150 ASN   A CG   1 
ATOM   3074 O OD1  . ASN   A 1 150 ? 20.213 -17.359 12.613  1.00 21.78 ?  150 ASN   A OD1  1 
ATOM   3075 N ND2  . ASN   A 1 150 ? 21.407 -16.835 14.444  1.00 23.34 ?  150 ASN   A ND2  1 
ATOM   3076 H H    . ASN   A 1 150 ? 22.915 -15.430 11.395  1.00 15.76 ?  150 ASN   A H    1 
ATOM   3077 H HA   . ASN   A 1 150 ? 20.266 -15.524 10.946  1.00 16.37 ?  150 ASN   A HA   1 
ATOM   3078 H HB2  . ASN   A 1 150 ? 21.737 -14.725 13.215  1.00 19.37 ?  150 ASN   A HB2  1 
ATOM   3079 H HB3  . ASN   A 1 150 ? 20.150 -14.623 13.160  1.00 19.37 ?  150 ASN   A HB3  1 
ATOM   3080 H HD21 . ASN   A 1 150 ? 21.374 -17.643 14.751  1.00 28.01 ?  150 ASN   A HD21 1 
ATOM   3081 H HD22 . ASN   A 1 150 ? 21.820 -16.230 14.895  1.00 28.01 ?  150 ASN   A HD22 1 
ATOM   3082 N N    . VAL   A 1 151 ? 19.812 -13.311 10.009  1.00 12.74 ?  151 VAL   A N    1 
ATOM   3083 C CA   . VAL   A 1 151 ? 19.606 -12.003 9.404   1.00 12.64 ?  151 VAL   A CA   1 
ATOM   3084 C C    . VAL   A 1 151 ? 18.221 -11.485 9.765   1.00 12.40 ?  151 VAL   A C    1 
ATOM   3085 O O    . VAL   A 1 151 ? 17.213 -12.195 9.615   1.00 13.92 ?  151 VAL   A O    1 
ATOM   3086 C CB   . VAL   A 1 151 ? 19.890 -12.010 7.887   1.00 13.89 ?  151 VAL   A CB   1 
ATOM   3087 C CG1  . VAL   A 1 151 ? 19.062 -13.050 7.150   1.00 15.34 ?  151 VAL   A CG1  1 
ATOM   3088 C CG2  . VAL   A 1 151 ? 19.704 -10.607 7.294   1.00 14.04 ?  151 VAL   A CG2  1 
ATOM   3089 H H    . VAL   A 1 151 ? 19.241 -13.906 9.763   1.00 15.29 ?  151 VAL   A H    1 
ATOM   3090 H HA   . VAL   A 1 151 ? 20.249 -11.392 9.795   1.00 15.17 ?  151 VAL   A HA   1 
ATOM   3091 H HB   . VAL   A 1 151 ? 20.823 -12.251 7.752   1.00 16.68 ?  151 VAL   A HB   1 
ATOM   3092 H HG11 . VAL   A 1 151 ? 19.257 -13.006 6.201   1.00 18.41 ?  151 VAL   A HG11 1 
ATOM   3093 H HG12 . VAL   A 1 151 ? 19.287 -13.936 7.488   1.00 18.41 ?  151 VAL   A HG12 1 
ATOM   3094 H HG13 . VAL   A 1 151 ? 18.119 -12.874 7.301   1.00 18.41 ?  151 VAL   A HG13 1 
ATOM   3095 H HG21 . VAL   A 1 151 ? 20.014 -10.609 6.371   1.00 16.86 ?  151 VAL   A HG21 1 
ATOM   3096 H HG22 . VAL   A 1 151 ? 18.762 -10.374 7.319   1.00 16.86 ?  151 VAL   A HG22 1 
ATOM   3097 H HG23 . VAL   A 1 151 ? 20.219 -9.973  7.812   1.00 16.86 ?  151 VAL   A HG23 1 
ATOM   3098 N N    . TYR   A 1 152 ? 18.201 -10.239 10.249  1.00 12.63 ?  152 TYR   A N    1 
ATOM   3099 C CA   . TYR   A 1 152 ? 17.003 -9.507  10.633  1.00 12.30 ?  152 TYR   A CA   1 
ATOM   3100 C C    . TYR   A 1 152 ? 16.814 -8.402  9.606   1.00 11.79 ?  152 TYR   A C    1 
ATOM   3101 O O    . TYR   A 1 152 ? 17.593 -7.444  9.565   1.00 12.25 ?  152 TYR   A O    1 
ATOM   3102 C CB   . TYR   A 1 152 ? 17.173 -8.960  12.047  1.00 12.92 ?  152 TYR   A CB   1 
ATOM   3103 C CG   . TYR   A 1 152 ? 17.129 -10.080 13.049  1.00 13.44 ?  152 TYR   A CG   1 
ATOM   3104 C CD1  . TYR   A 1 152 ? 18.258 -10.836 13.330  1.00 15.01 ?  152 TYR   A CD1  1 
ATOM   3105 C CD2  . TYR   A 1 152 ? 15.943 -10.430 13.678  1.00 14.12 ?  152 TYR   A CD2  1 
ATOM   3106 C CE1  . TYR   A 1 152 ? 18.218 -11.892 14.218  1.00 16.48 ?  152 TYR   A CE1  1 
ATOM   3107 C CE2  . TYR   A 1 152 ? 15.890 -11.494 14.575  1.00 15.86 ?  152 TYR   A CE2  1 
ATOM   3108 C CZ   . TYR   A 1 152 ? 17.033 -12.218 14.842  1.00 16.82 ?  152 TYR   A CZ   1 
ATOM   3109 O OH   . TYR   A 1 152 ? 16.990 -13.280 15.726  1.00 19.34 ?  152 TYR   A OH   1 
ATOM   3110 H H    . TYR   A 1 152 ? 18.921 -9.771  10.352  1.00 15.16 ?  152 TYR   A H    1 
ATOM   3111 H HA   . TYR   A 1 152 ? 16.237 -10.099 10.608  1.00 14.77 ?  152 TYR   A HA   1 
ATOM   3112 H HB2  . TYR   A 1 152 ? 18.033 -8.520  12.120  1.00 15.51 ?  152 TYR   A HB2  1 
ATOM   3113 H HB3  . TYR   A 1 152 ? 16.455 -8.342  12.242  1.00 15.51 ?  152 TYR   A HB3  1 
ATOM   3114 H HD1  . TYR   A 1 152 ? 19.060 -10.622 12.907  1.00 18.02 ?  152 TYR   A HD1  1 
ATOM   3115 H HD2  . TYR   A 1 152 ? 15.165 -9.944  13.496  1.00 16.95 ?  152 TYR   A HD2  1 
ATOM   3116 H HE1  . TYR   A 1 152 ? 18.987 -12.375 14.398  1.00 19.78 ?  152 TYR   A HE1  1 
ATOM   3117 H HE2  . TYR   A 1 152 ? 15.088 -11.707 14.997  1.00 19.04 ?  152 TYR   A HE2  1 
ATOM   3118 H HH   . TYR   A 1 152 ? 16.213 -13.354 16.037  1.00 23.22 ?  152 TYR   A HH   1 
ATOM   3119 N N    A LEU   A 1 153 ? 15.820 -8.587  8.738   0.72 11.89 ?  153 LEU   A N    1 
ATOM   3120 N N    B LEU   A 1 153 ? 15.768 -8.508  8.797   0.28 11.55 ?  153 LEU   A N    1 
ATOM   3121 C CA   A LEU   A 1 153 ? 15.562 -7.703  7.608   0.72 11.59 ?  153 LEU   A CA   1 
ATOM   3122 C CA   B LEU   A 1 153 ? 15.521 -7.552  7.725   0.28 11.06 ?  153 LEU   A CA   1 
ATOM   3123 C C    A LEU   A 1 153 ? 14.557 -6.629  7.991   0.72 11.80 ?  153 LEU   A C    1 
ATOM   3124 C C    B LEU   A 1 153 ? 14.551 -6.479  8.202   0.28 11.22 ?  153 LEU   A C    1 
ATOM   3125 O O    A LEU   A 1 153 ? 13.461 -6.938  8.474   0.72 13.31 ?  153 LEU   A O    1 
ATOM   3126 O O    B LEU   A 1 153 ? 13.421 -6.787  8.597   0.28 12.08 ?  153 LEU   A O    1 
ATOM   3127 C CB   A LEU   A 1 153 ? 14.988 -8.506  6.439   0.72 11.75 ?  153 LEU   A CB   1 
ATOM   3128 C CB   B LEU   A 1 153 ? 14.960 -8.259  6.494   0.28 11.10 ?  153 LEU   A CB   1 
ATOM   3129 C CG   A LEU   A 1 153 ? 15.942 -9.496  5.768   0.72 11.87 ?  153 LEU   A CG   1 
ATOM   3130 C CG   B LEU   A 1 153 ? 15.850 -9.354  5.901   0.28 11.51 ?  153 LEU   A CG   1 
ATOM   3131 C CD1  A LEU   A 1 153 ? 15.171 -10.427 4.843   0.72 12.34 ?  153 LEU   A CD1  1 
ATOM   3132 C CD1  B LEU   A 1 153 ? 15.074 -10.129 4.850   0.28 11.90 ?  153 LEU   A CD1  1 
ATOM   3133 C CD2  A LEU   A 1 153 ? 17.013 -8.745  4.995   0.72 12.10 ?  153 LEU   A CD2  1 
ATOM   3134 C CD2  B LEU   A 1 153 ? 17.137 -8.779  5.316   0.28 11.97 ?  153 LEU   A CD2  1 
ATOM   3135 H H    A LEU   A 1 153 ? 15.263 -9.244  8.790   0.72 14.28 ?  153 LEU   A H    1 
ATOM   3136 H H    B LEU   A 1 153 ? 15.173 -9.129  8.853   0.28 13.87 ?  153 LEU   A H    1 
ATOM   3137 H HA   A LEU   A 1 153 ? 16.388 -7.289  7.328   0.72 13.91 ?  153 LEU   A HA   1 
ATOM   3138 H HA   B LEU   A 1 153 ? 16.351 -7.120  7.483   0.28 13.27 ?  153 LEU   A HA   1 
ATOM   3139 H HB2  A LEU   A 1 153 ? 14.226 -9.016  6.761   0.72 14.10 ?  153 LEU   A HB2  1 
ATOM   3140 H HB2  B LEU   A 1 153 ? 14.116 -8.669  6.736   0.28 13.33 ?  153 LEU   A HB2  1 
ATOM   3141 H HB3  A LEU   A 1 153 ? 14.694 -7.886  5.756   0.72 14.10 ?  153 LEU   A HB3  1 
ATOM   3142 H HB3  B LEU   A 1 153 ? 14.813 -7.595  5.804   0.28 13.33 ?  153 LEU   A HB3  1 
ATOM   3143 H HG   A LEU   A 1 153 ? 16.378 -10.037 6.450   0.72 14.25 ?  153 LEU   A HG   1 
ATOM   3144 H HG   B LEU   A 1 153 ? 16.098 -9.971  6.607   0.28 13.81 ?  153 LEU   A HG   1 
ATOM   3145 H HD11 A LEU   A 1 153 ? 15.754 -11.149 4.564   0.72 14.81 ?  153 LEU   A HD11 1 
ATOM   3146 H HD11 B LEU   A 1 153 ? 15.644 -10.823 4.487   0.28 14.29 ?  153 LEU   A HD11 1 
ATOM   3147 H HD12 A LEU   A 1 153 ? 14.407 -10.782 5.318   0.72 14.81 ?  153 LEU   A HD12 1 
ATOM   3148 H HD12 B LEU   A 1 153 ? 14.292 -10.525 5.266   0.28 14.29 ?  153 LEU   A HD12 1 
ATOM   3149 H HD13 A LEU   A 1 153 ? 14.876 -9.921  4.069   0.72 14.81 ?  153 LEU   A HD13 1 
ATOM   3150 H HD13 B LEU   A 1 153 ? 14.802 -9.519  4.146   0.28 14.29 ?  153 LEU   A HD13 1 
ATOM   3151 H HD21 A LEU   A 1 153 ? 17.577 -9.385  4.542   0.72 14.52 ?  153 LEU   A HD21 1 
ATOM   3152 H HD21 B LEU   A 1 153 ? 17.653 -9.500  4.923   0.28 14.37 ?  153 LEU   A HD21 1 
ATOM   3153 H HD22 A LEU   A 1 153 ? 16.578 -8.165  4.354   0.72 14.52 ?  153 LEU   A HD22 1 
ATOM   3154 H HD22 B LEU   A 1 153 ? 16.911 -8.125  4.638   0.28 14.37 ?  153 LEU   A HD22 1 
ATOM   3155 H HD23 A LEU   A 1 153 ? 17.535 -8.221  5.621   0.72 14.52 ?  153 LEU   A HD23 1 
ATOM   3156 H HD23 B LEU   A 1 153 ? 17.648 -8.357  6.026   0.28 14.37 ?  153 LEU   A HD23 1 
ATOM   3157 N N    A ALA   A 1 154 ? 14.920 -5.377  7.737   0.72 11.49 ?  154 ALA   A N    1 
ATOM   3158 N N    B ALA   A 1 154 ? 14.995 -5.225  8.160   0.28 10.27 ?  154 ALA   A N    1 
ATOM   3159 C CA   A ALA   A 1 154 ? 14.058 -4.225  7.964   0.72 11.42 ?  154 ALA   A CA   1 
ATOM   3160 C CA   B ALA   A 1 154 ? 14.145 -4.073  8.430   0.28 10.80 ?  154 ALA   A CA   1 
ATOM   3161 C C    A ALA   A 1 154 ? 13.569 -3.719  6.613   0.72 11.07 ?  154 ALA   A C    1 
ATOM   3162 C C    B ALA   A 1 154 ? 13.677 -3.517  7.091   0.28 10.63 ?  154 ALA   A C    1 
ATOM   3163 O O    A ALA   A 1 154 ? 14.374 -3.328  5.764   0.72 12.14 ?  154 ALA   A O    1 
ATOM   3164 O O    B ALA   A 1 154 ? 14.500 -3.124  6.258   0.28 10.45 ?  154 ALA   A O    1 
ATOM   3165 C CB   A ALA   A 1 154 ? 14.825 -3.126  8.698   0.72 12.40 ?  154 ALA   A CB   1 
ATOM   3166 C CB   B ALA   A 1 154 ? 14.911 -3.010  9.220   0.28 10.96 ?  154 ALA   A CB   1 
ATOM   3167 H H    A ALA   A 1 154 ? 15.689 -5.167  7.404   0.72 13.79 ?  154 ALA   A H    1 
ATOM   3168 H H    B ALA   A 1 154 ? 15.807 -5.006  7.963   0.28 12.33 ?  154 ALA   A H    1 
ATOM   3169 H HA   A ALA   A 1 154 ? 13.295 -4.491  8.501   0.72 13.71 ?  154 ALA   A HA   1 
ATOM   3170 H HA   B ALA   A 1 154 ? 13.372 -4.341  8.943   0.28 12.97 ?  154 ALA   A HA   1 
ATOM   3171 H HB1  A ALA   A 1 154 ? 14.233 -2.372  8.843   0.72 14.89 ?  154 ALA   A HB1  1 
ATOM   3172 H HB1  B ALA   A 1 154 ? 14.326 -2.254  9.391   0.28 13.16 ?  154 ALA   A HB1  1 
ATOM   3173 H HB2  A ALA   A 1 154 ? 15.138 -3.470  9.551   0.72 14.89 ?  154 ALA   A HB2  1 
ATOM   3174 H HB2  B ALA   A 1 154 ? 15.206 -3.394  10.062  0.28 13.16 ?  154 ALA   A HB2  1 
ATOM   3175 H HB3  A ALA   A 1 154 ? 15.583 -2.853  8.156   0.72 14.89 ?  154 ALA   A HB3  1 
ATOM   3176 H HB3  B ALA   A 1 154 ? 15.681 -2.721  8.704   0.28 13.16 ?  154 ALA   A HB3  1 
ATOM   3177 N N    A VAL   A 1 155 ? 12.254 -3.723  6.422   0.42 8.47  ?  155 VAL   A N    1 
ATOM   3178 N N    B VAL   A 1 155 ? 12.364 -3.508  6.875   0.28 10.47 ?  155 VAL   A N    1 
ATOM   3179 C CA   A VAL   A 1 155 ? 11.610 -3.259  5.197   0.42 11.01 ?  155 VAL   A CA   1 
ATOM   3180 C CA   B VAL   A 1 155 ? 11.765 -3.016  5.638   0.28 11.51 ?  155 VAL   A CA   1 
ATOM   3181 C CA   T VAL   A 1 155 ? 11.615 -3.297  5.226   0.30 13.39 ?  155 VAL   A CA   1 
ATOM   3182 C C    A VAL   A 1 155 ? 10.878 -1.967  5.537   0.42 12.48 ?  155 VAL   A C    1 
ATOM   3183 C C    B VAL   A 1 155 ? 11.036 -1.710  5.932   0.28 12.84 ?  155 VAL   A C    1 
ATOM   3184 C C    T VAL   A 1 155 ? 11.002 -1.930  5.535   0.30 13.15 ?  155 VAL   A C    1 
ATOM   3185 O O    A VAL   A 1 155 ? 9.884  -1.989  6.273   0.42 12.84 ?  155 VAL   A O    1 
ATOM   3186 O O    B VAL   A 1 155 ? 10.092 -1.682  6.731   0.28 12.98 ?  155 VAL   A O    1 
ATOM   3187 O O    T VAL   A 1 155 ? 10.157 -1.803  6.420   0.30 13.38 ?  155 VAL   A O    1 
ATOM   3188 C CB   A VAL   A 1 155 ? 10.649 -4.316  4.631   0.42 11.75 ?  155 VAL   A CB   1 
ATOM   3189 C CB   B VAL   A 1 155 ? 10.829 -4.058  5.010   0.28 11.81 ?  155 VAL   A CB   1 
ATOM   3190 C CB   T VAL   A 1 155 ? 10.570 -4.313  4.722   0.30 13.45 ?  155 VAL   A CB   1 
ATOM   3191 C CG1  A VAL   A 1 155 ? 10.012 -3.825  3.339   0.42 12.23 ?  155 VAL   A CG1  1 
ATOM   3192 C CG1  B VAL   A 1 155 ? 10.055 -3.445  3.855   0.28 11.64 ?  155 VAL   A CG1  1 
ATOM   3193 C CG1  T VAL   A 1 155 ? 9.891  -3.801  3.463   0.30 13.58 ?  155 VAL   A CG1  1 
ATOM   3194 C CG2  A VAL   A 1 155 ? 11.372 -5.641  4.405   0.42 13.20 ?  155 VAL   A CG2  1 
ATOM   3195 C CG2  B VAL   A 1 155 ? 11.636 -5.267  4.545   0.28 12.42 ?  155 VAL   A CG2  1 
ATOM   3196 C CG2  T VAL   A 1 155 ? 11.222 -5.668  4.464   0.30 13.93 ?  155 VAL   A CG2  1 
ATOM   3197 H H    A VAL   A 1 155 ? 11.695 -4.019  7.008   0.42 10.17 ?  155 VAL   A H    1 
ATOM   3198 H H    B VAL   A 1 155 ? 11.789 -3.793  7.443   0.28 12.57 ?  155 VAL   A H    1 
ATOM   3199 H HA   A VAL   A 1 155 ? 12.285 -3.068  4.530   0.42 13.21 ?  155 VAL   A HA   1 
ATOM   3200 H HA   B VAL   A 1 155 ? 12.471 -2.827  4.999   0.28 13.82 ?  155 VAL   A HA   1 
ATOM   3201 H HB   A VAL   A 1 155 ? 9.937  -4.472  5.274   0.42 14.10 ?  155 VAL   A HB   1 
ATOM   3202 H HB   B VAL   A 1 155 ? 10.193 -4.357  5.679   0.28 14.18 ?  155 VAL   A HB   1 
ATOM   3203 H HB   T VAL   A 1 155 ? 9.893  -4.432  5.406   0.30 16.14 ?  155 VAL   A HB   1 
ATOM   3204 H HG11 A VAL   A 1 155 ? 9.509  -4.555  2.941   0.42 14.69 ?  155 VAL   A HG11 1 
ATOM   3205 H HG11 B VAL   A 1 155 ? 9.682  -4.159  3.316   0.28 13.97 ?  155 VAL   A HG11 1 
ATOM   3206 H HG11 T VAL   A 1 155 ? 9.343  -4.512  3.093   0.30 16.30 ?  155 VAL   A HG11 1 
ATOM   3207 H HG12 A VAL   A 1 155 ? 9.417  -3.087  3.539   0.42 14.69 ?  155 VAL   A HG12 1 
ATOM   3208 H HG12 B VAL   A 1 155 ? 9.342  -2.891  4.208   0.28 13.97 ?  155 VAL   A HG12 1 
ATOM   3209 H HG12 T VAL   A 1 155 ? 9.337  -3.040  3.688   0.30 16.30 ?  155 VAL   A HG12 1 
ATOM   3210 H HG13 A VAL   A 1 155 ? 10.711 -3.538  2.734   0.42 14.69 ?  155 VAL   A HG13 1 
ATOM   3211 H HG13 B VAL   A 1 155 ? 10.661 -2.909  3.320   0.28 13.97 ?  155 VAL   A HG13 1 
ATOM   3212 H HG13 T VAL   A 1 155 ? 10.571 -3.542  2.822   0.30 16.30 ?  155 VAL   A HG13 1 
ATOM   3213 H HG21 A VAL   A 1 155 ? 10.769 -6.260  3.966   0.42 15.85 ?  155 VAL   A HG21 1 
ATOM   3214 H HG21 B VAL   A 1 155 ? 11.034 -5.910  4.138   0.28 14.91 ?  155 VAL   A HG21 1 
ATOM   3215 H HG21 T VAL   A 1 155 ? 10.547 -6.289  4.151   0.30 16.72 ?  155 VAL   A HG21 1 
ATOM   3216 H HG22 A VAL   A 1 155 ? 12.149 -5.483  3.845   0.42 15.85 ?  155 VAL   A HG22 1 
ATOM   3217 H HG22 B VAL   A 1 155 ? 12.296 -4.976  3.897   0.28 14.91 ?  155 VAL   A HG22 1 
ATOM   3218 H HG22 T VAL   A 1 155 ? 11.912 -5.562  3.788   0.30 16.72 ?  155 VAL   A HG22 1 
ATOM   3219 H HG23 A VAL   A 1 155 ? 11.650 -6.001  5.262   0.42 15.85 ?  155 VAL   A HG23 1 
ATOM   3220 H HG23 B VAL   A 1 155 ? 12.078 -5.667  5.311   0.28 14.91 ?  155 VAL   A HG23 1 
ATOM   3221 H HG23 T VAL   A 1 155 ? 11.617 -5.993  5.288   0.30 16.72 ?  155 VAL   A HG23 1 
ATOM   3222 N N    A PHE   A 1 156 ? 11.359 -0.843  4.993   0.42 14.68 ?  156 PHE   A N    1 
ATOM   3223 N N    B PHE   A 1 156 ? 11.479 -0.632  5.279   0.28 13.95 ?  156 PHE   A N    1 
ATOM   3224 N N    T PHE   A 1 156 ? 11.446 -0.912  4.791   0.30 13.57 ?  156 PHE   A N    1 
ATOM   3225 C CA   A PHE   A 1 156 ? 10.844 0.467   5.399   0.42 17.25 ?  156 PHE   A CA   1 
ATOM   3226 C CA   B PHE   A 1 156 ? 10.904 0.692   5.509   0.28 15.81 ?  156 PHE   A CA   1 
ATOM   3227 C CA   T PHE   A 1 156 ? 11.040 0.464   5.074   0.30 14.07 ?  156 PHE   A CA   1 
ATOM   3228 C C    A PHE   A 1 156 ? 9.385  0.654   5.001   0.42 17.79 ?  156 PHE   A C    1 
ATOM   3229 C C    B PHE   A 1 156 ? 9.457  0.761   5.034   0.28 16.04 ?  156 PHE   A C    1 
ATOM   3230 C C    T PHE   A 1 156 ? 9.578  0.703   4.721   0.30 15.06 ?  156 PHE   A C    1 
ATOM   3231 O O    A PHE   A 1 156 ? 8.592  1.210   5.772   0.42 18.57 ?  156 PHE   A O    1 
ATOM   3232 O O    B PHE   A 1 156 ? 8.561  1.152   5.791   0.28 16.81 ?  156 PHE   A O    1 
ATOM   3233 O O    T PHE   A 1 156 ? 8.861  1.400   5.449   0.30 15.46 ?  156 PHE   A O    1 
ATOM   3234 C CB   A PHE   A 1 156 ? 11.708 1.580   4.798   0.42 18.93 ?  156 PHE   A CB   1 
ATOM   3235 C CB   B PHE   A 1 156 ? 11.756 1.733   4.777   0.28 17.40 ?  156 PHE   A CB   1 
ATOM   3236 C CB   T PHE   A 1 156 ? 11.932 1.424   4.284   0.30 13.24 ?  156 PHE   A CB   1 
ATOM   3237 C CG   A PHE   A 1 156 ? 11.200 2.969   5.096   0.42 20.43 ?  156 PHE   A CG   1 
ATOM   3238 C CG   B PHE   A 1 156 ? 11.332 3.162   5.012   0.28 18.57 ?  156 PHE   A CG   1 
ATOM   3239 C CG   T PHE   A 1 156 ? 11.596 2.881   4.486   0.30 13.09 ?  156 PHE   A CG   1 
ATOM   3240 C CD1  A PHE   A 1 156 ? 11.088 3.406   6.406   0.42 20.85 ?  156 PHE   A CD1  1 
ATOM   3241 C CD1  B PHE   A 1 156 ? 10.335 3.746   4.244   0.28 19.16 ?  156 PHE   A CD1  1 
ATOM   3242 C CD1  T PHE   A 1 156 ? 11.986 3.535   5.645   0.30 13.92 ?  156 PHE   A CD1  1 
ATOM   3243 C CD2  A PHE   A 1 156 ? 10.847 3.835   4.072   0.42 21.24 ?  156 PHE   A CD2  1 
ATOM   3244 C CD2  B PHE   A 1 156 ? 11.959 3.930   5.981   0.28 18.96 ?  156 PHE   A CD2  1 
ATOM   3245 C CD2  T PHE   A 1 156 ? 10.906 3.597   3.517   0.30 13.40 ?  156 PHE   A CD2  1 
ATOM   3246 C CE1  A PHE   A 1 156 ? 10.625 4.676   6.692   0.42 21.43 ?  156 PHE   A CE1  1 
ATOM   3247 C CE1  B PHE   A 1 156 ? 9.954  5.062   4.456   0.28 19.31 ?  156 PHE   A CE1  1 
ATOM   3248 C CE1  T PHE   A 1 156 ? 11.687 4.870   5.841   0.30 14.64 ?  156 PHE   A CE1  1 
ATOM   3249 C CE2  A PHE   A 1 156 ? 10.381 5.111   4.352   0.42 21.97 ?  156 PHE   A CE2  1 
ATOM   3250 C CE2  B PHE   A 1 156 ? 11.586 5.246   6.196   0.28 19.43 ?  156 PHE   A CE2  1 
ATOM   3251 C CE2  T PHE   A 1 156 ? 10.606 4.937   3.705   0.30 14.19 ?  156 PHE   A CE2  1 
ATOM   3252 C CZ   A PHE   A 1 156 ? 10.273 5.532   5.665   0.42 22.04 ?  156 PHE   A CZ   1 
ATOM   3253 C CZ   B PHE   A 1 156 ? 10.585 5.813   5.432   0.28 19.47 ?  156 PHE   A CZ   1 
ATOM   3254 C CZ   T PHE   A 1 156 ? 10.999 5.575   4.869   0.30 14.41 ?  156 PHE   A CZ   1 
ATOM   3255 H H    A PHE   A 1 156 ? 11.977 -0.819  4.394   0.42 17.62 ?  156 PHE   A H    1 
ATOM   3256 H H    B PHE   A 1 156 ? 12.121 -0.643  4.703   0.28 16.75 ?  156 PHE   A H    1 
ATOM   3257 H H    T PHE   A 1 156 ? 11.982 -0.998  4.125   0.30 16.29 ?  156 PHE   A H    1 
ATOM   3258 H HA   A PHE   A 1 156 ? 10.905 0.537   6.362   0.42 20.70 ?  156 PHE   A HA   1 
ATOM   3259 H HA   B PHE   A 1 156 ? 10.927 0.892   6.457   0.28 18.98 ?  156 PHE   A HA   1 
ATOM   3260 H HA   T PHE   A 1 156 ? 11.163 0.640   6.020   0.30 16.89 ?  156 PHE   A HA   1 
ATOM   3261 H HB2  A PHE   A 1 156 ? 12.609 1.509   5.156   0.42 22.72 ?  156 PHE   A HB2  1 
ATOM   3262 H HB2  B PHE   A 1 156 ? 12.676 1.646   5.071   0.28 20.89 ?  156 PHE   A HB2  1 
ATOM   3263 H HB2  T PHE   A 1 156 ? 12.853 1.289   4.557   0.30 15.89 ?  156 PHE   A HB2  1 
ATOM   3264 H HB3  A PHE   A 1 156 ? 11.733 1.473   3.833   0.42 22.72 ?  156 PHE   A HB3  1 
ATOM   3265 H HB3  B PHE   A 1 156 ? 11.701 1.561   3.825   0.28 20.89 ?  156 PHE   A HB3  1 
ATOM   3266 H HB3  T PHE   A 1 156 ? 11.837 1.226   3.339   0.30 15.89 ?  156 PHE   A HB3  1 
ATOM   3267 H HD1  A PHE   A 1 156 ? 11.325 2.833   7.101   0.42 25.02 ?  156 PHE   A HD1  1 
ATOM   3268 H HD1  B PHE   A 1 156 ? 9.908  3.246   3.587   0.28 23.00 ?  156 PHE   A HD1  1 
ATOM   3269 H HD1  T PHE   A 1 156 ? 12.448 3.063   6.305   0.30 16.71 ?  156 PHE   A HD1  1 
ATOM   3270 H HD2  A PHE   A 1 156 ? 10.919 3.555   3.188   0.42 25.50 ?  156 PHE   A HD2  1 
ATOM   3271 H HD2  B PHE   A 1 156 ? 12.634 3.552   6.498   0.28 22.75 ?  156 PHE   A HD2  1 
ATOM   3272 H HD2  T PHE   A 1 156 ? 10.641 3.168   2.737   0.30 16.08 ?  156 PHE   A HD2  1 
ATOM   3273 H HE1  A PHE   A 1 156 ? 10.554 4.955   7.578   0.42 25.72 ?  156 PHE   A HE1  1 
ATOM   3274 H HE1  B PHE   A 1 156 ? 9.279  5.440   3.939   0.28 23.17 ?  156 PHE   A HE1  1 
ATOM   3275 H HE1  T PHE   A 1 156 ? 11.950 5.293   6.628   0.30 17.57 ?  156 PHE   A HE1  1 
ATOM   3276 H HE2  A PHE   A 1 156 ? 10.146 5.684   3.658   0.42 26.37 ?  156 PHE   A HE2  1 
ATOM   3277 H HE2  B PHE   A 1 156 ? 12.010 5.746   6.854   0.28 23.33 ?  156 PHE   A HE2  1 
ATOM   3278 H HE2  T PHE   A 1 156 ? 10.139 5.402   3.056   0.30 17.04 ?  156 PHE   A HE2  1 
ATOM   3279 H HZ   A PHE   A 1 156 ? 9.962  6.387   5.859   0.42 26.45 ?  156 PHE   A HZ   1 
ATOM   3280 H HZ   B PHE   A 1 156 ? 10.331 6.695   5.577   0.28 23.37 ?  156 PHE   A HZ   1 
ATOM   3281 H HZ   T PHE   A 1 156 ? 10.794 6.468   5.004   0.30 17.30 ?  156 PHE   A HZ   1 
ATOM   3282 N N    A ASP   A 1 157 ? 9.018  0.215   3.804   0.42 17.67 ?  157 ASP   A N    1 
ATOM   3283 N N    B ASP   A 1 157 ? 9.216  0.393   3.779   0.28 15.26 ?  157 ASP   A N    1 
ATOM   3284 N N    T ASP   A 1 157 ? 9.128  0.149   3.602   0.30 15.81 ?  157 ASP   A N    1 
ATOM   3285 C CA   A ASP   A 1 157 ? 7.705  0.498   3.239   0.42 18.67 ?  157 ASP   A CA   1 
ATOM   3286 C CA   B ASP   A 1 157 ? 7.930  0.627   3.133   0.28 15.39 ?  157 ASP   A CA   1 
ATOM   3287 C CA   T ASP   A 1 157 ? 7.819  0.455   3.043   0.30 16.68 ?  157 ASP   A CA   1 
ATOM   3288 C C    A ASP   A 1 157 ? 6.704  -0.544  3.731   0.42 19.03 ?  157 ASP   A C    1 
ATOM   3289 C C    B ASP   A 1 157 ? 6.895  -0.374  3.641   0.28 15.59 ?  157 ASP   A C    1 
ATOM   3290 C C    T ASP   A 1 157 ? 6.786  -0.519  3.600   0.30 17.41 ?  157 ASP   A C    1 
ATOM   3291 O O    A ASP   A 1 157 ? 6.834  -1.734  3.421   0.42 18.56 ?  157 ASP   A O    1 
ATOM   3292 O O    B ASP   A 1 157 ? 7.087  -1.590  3.528   0.28 15.47 ?  157 ASP   A O    1 
ATOM   3293 O O    T ASP   A 1 157 ? 6.877  -1.730  3.366   0.30 17.03 ?  157 ASP   A O    1 
ATOM   3294 C CB   A ASP   A 1 157 ? 7.799  0.486   1.715   0.42 19.55 ?  157 ASP   A CB   1 
ATOM   3295 C CB   B ASP   A 1 157 ? 8.109  0.514   1.621   0.28 15.36 ?  157 ASP   A CB   1 
ATOM   3296 C CB   T ASP   A 1 157 ? 7.902  0.335   1.524   0.30 16.96 ?  157 ASP   A CB   1 
ATOM   3297 C CG   A ASP   A 1 157 ? 6.509  0.914   1.047   0.42 20.63 ?  157 ASP   A CG   1 
ATOM   3298 C CG   B ASP   A 1 157 ? 6.882  0.937   0.860   0.28 15.35 ?  157 ASP   A CG   1 
ATOM   3299 C CG   T ASP   A 1 157 ? 6.760  1.019   0.825   0.30 16.62 ?  157 ASP   A CG   1 
ATOM   3300 O OD1  A ASP   A 1 157 ? 6.130  2.094   1.178   0.42 21.67 ?  157 ASP   A OD1  1 
ATOM   3301 O OD1  B ASP   A 1 157 ? 5.804  0.362   1.122   0.28 15.07 ?  157 ASP   A OD1  1 
ATOM   3302 O OD1  T ASP   A 1 157 ? 5.666  0.421   0.771   0.30 16.93 ?  157 ASP   A OD1  1 
ATOM   3303 O OD2  A ASP   A 1 157 ? 5.865  0.065   0.392   0.42 20.57 -1 157 ASP   A OD2  1 
ATOM   3304 O OD2  B ASP   A 1 157 ? 6.988  1.843   0.007   0.28 15.80 -1 157 ASP   A OD2  1 
ATOM   3305 O OD2  T ASP   A 1 157 ? 6.951  2.155   0.343   0.30 16.02 -1 157 ASP   A OD2  1 
ATOM   3306 H H    A ASP   A 1 157 ? 9.526  -0.261  3.293   0.42 21.21 ?  157 ASP   A H    1 
ATOM   3307 H H    B ASP   A 1 157 ? 9.797  0.006   3.270   0.28 18.32 ?  157 ASP   A H    1 
ATOM   3308 H H    T ASP   A 1 157 ? 9.580  -0.416  3.135   0.30 18.98 ?  157 ASP   A H    1 
ATOM   3309 H HA   A ASP   A 1 157 ? 7.415  1.377   3.529   0.42 22.41 ?  157 ASP   A HA   1 
ATOM   3310 H HA   B ASP   A 1 157 ? 7.625  1.525   3.340   0.28 18.47 ?  157 ASP   A HA   1 
ATOM   3311 H HA   T ASP   A 1 157 ? 7.566  1.363   3.277   0.30 20.02 ?  157 ASP   A HA   1 
ATOM   3312 H HB2  A ASP   A 1 157 ? 8.538  1.065   1.444   0.42 23.46 ?  157 ASP   A HB2  1 
ATOM   3313 H HB2  B ASP   A 1 157 ? 8.851  1.075   1.345   0.28 18.44 ?  157 ASP   A HB2  1 
ATOM   3314 H HB2  T ASP   A 1 157 ? 8.734  0.724   1.220   0.30 20.35 ?  157 ASP   A HB2  1 
ATOM   3315 H HB3  A ASP   A 1 157 ? 7.976  -0.418  1.418   0.42 23.46 ?  157 ASP   A HB3  1 
ATOM   3316 H HB3  B ASP   A 1 157 ? 8.292  -0.411  1.391   0.28 18.44 ?  157 ASP   A HB3  1 
ATOM   3317 H HB3  T ASP   A 1 157 ? 7.874  -0.604  1.286   0.30 20.35 ?  157 ASP   A HB3  1 
ATOM   3318 N N    A LYS   A 1 158 ? 5.707  -0.093  4.501   0.42 20.44 ?  158 LYS   A N    1 
ATOM   3319 N N    B LYS   A 1 158 ? 5.789  0.139   4.189   0.28 16.23 ?  158 LYS   A N    1 
ATOM   3320 N N    T LYS   A 1 158 ? 5.801  0.012   4.331   0.30 19.00 ?  158 LYS   A N    1 
ATOM   3321 C CA   A LYS   A 1 158 ? 4.731  -1.020  5.071   0.42 21.47 ?  158 LYS   A CA   1 
ATOM   3322 C CA   B LYS   A 1 158 ? 4.793  -0.742  4.793   0.28 16.87 ?  158 LYS   A CA   1 
ATOM   3323 C CA   T LYS   A 1 158 ? 4.801  -0.852  4.953   0.30 20.58 ?  158 LYS   A CA   1 
ATOM   3324 C C    A LYS   A 1 158 ? 3.969  -1.759  3.979   0.42 20.72 ?  158 LYS   A C    1 
ATOM   3325 C C    B LYS   A 1 158 ? 4.062  -1.563  3.737   0.28 16.84 ?  158 LYS   A C    1 
ATOM   3326 C C    T LYS   A 1 158 ? 4.026  -1.645  3.908   0.30 20.46 ?  158 LYS   A C    1 
ATOM   3327 O O    A LYS   A 1 158 ? 3.749  -2.973  4.078   0.42 20.96 ?  158 LYS   A O    1 
ATOM   3328 O O    B LYS   A 1 158 ? 3.847  -2.767  3.917   0.28 17.08 ?  158 LYS   A O    1 
ATOM   3329 O O    T LYS   A 1 158 ? 3.782  -2.845  4.083   0.30 20.69 ?  158 LYS   A O    1 
ATOM   3330 C CB   A LYS   A 1 158 ? 3.763  -0.272  5.991   0.42 23.07 ?  158 LYS   A CB   1 
ATOM   3331 C CB   B LYS   A 1 158 ? 3.793  0.064   5.623   0.28 18.02 ?  158 LYS   A CB   1 
ATOM   3332 C CB   T LYS   A 1 158 ? 3.848  -0.031  5.824   0.30 22.38 ?  158 LYS   A CB   1 
ATOM   3333 C CG   A LYS   A 1 158 ? 2.518  -1.067  6.404   0.42 24.65 ?  158 LYS   A CG   1 
ATOM   3334 C CG   B LYS   A 1 158 ? 2.628  -0.774  6.139   0.28 18.90 ?  158 LYS   A CG   1 
ATOM   3335 C CG   T LYS   A 1 158 ? 2.620  -0.802  6.309   0.30 23.95 ?  158 LYS   A CG   1 
ATOM   3336 C CD   A LYS   A 1 158 ? 2.857  -2.339  7.181   0.42 25.57 ?  158 LYS   A CD   1 
ATOM   3337 C CD   B LYS   A 1 158 ? 1.591  0.063   6.858   0.28 19.42 ?  158 LYS   A CD   1 
ATOM   3338 C CD   T LYS   A 1 158 ? 2.999  -2.020  7.145   0.30 25.15 ?  158 LYS   A CD   1 
ATOM   3339 C CE   A LYS   A 1 158 ? 1.589  -3.027  7.685   0.42 25.95 ?  158 LYS   A CE   1 
ATOM   3340 C CE   B LYS   A 1 158 ? 0.388  -0.778  7.255   0.28 19.59 ?  158 LYS   A CE   1 
ATOM   3341 C CE   T LYS   A 1 158 ? 1.767  -2.827  7.539   0.30 25.95 ?  158 LYS   A CE   1 
ATOM   3342 N NZ   A LYS   A 1 158 ? 1.852  -4.357  8.310   0.42 25.96 ?  158 LYS   A NZ   1 
ATOM   3343 N NZ   B LYS   A 1 158 ? -0.295 -1.382  6.075   0.28 19.47 ?  158 LYS   A NZ   1 
ATOM   3344 N NZ   T LYS   A 1 158 ? 2.104  -4.033  8.348   0.30 26.31 ?  158 LYS   A NZ   1 
ATOM   3345 H H    A LYS   A 1 158 ? 5.582  0.732   4.702   0.42 24.54 ?  158 LYS   A H    1 
ATOM   3346 H H    B LYS   A 1 158 ? 5.596  0.975   4.212   0.28 19.48 ?  158 LYS   A H    1 
ATOM   3347 H H    T LYS   A 1 158 ? 5.694  0.853   4.476   0.30 22.80 ?  158 LYS   A H    1 
ATOM   3348 H HA   A LYS   A 1 158 ? 5.200  -1.679  5.605   0.42 25.77 ?  158 LYS   A HA   1 
ATOM   3349 H HA   B LYS   A 1 158 ? 5.246  -1.358  5.392   0.28 20.24 ?  158 LYS   A HA   1 
ATOM   3350 H HA   T LYS   A 1 158 ? 5.255  -1.485  5.530   0.30 24.70 ?  158 LYS   A HA   1 
ATOM   3351 H HB2  A LYS   A 1 158 ? 4.235  -0.023  6.802   0.42 27.69 ?  158 LYS   A HB2  1 
ATOM   3352 H HB2  B LYS   A 1 158 ? 4.254  0.440   6.393   0.28 21.63 ?  158 LYS   A HB2  1 
ATOM   3353 H HB2  T LYS   A 1 158 ? 4.329  0.277   6.610   0.30 26.86 ?  158 LYS   A HB2  1 
ATOM   3354 H HB3  A LYS   A 1 158 ? 3.461  0.529   5.536   0.42 27.69 ?  158 LYS   A HB3  1 
ATOM   3355 H HB3  B LYS   A 1 158 ? 3.431  0.777   5.076   0.28 21.63 ?  158 LYS   A HB3  1 
ATOM   3356 H HB3  T LYS   A 1 158 ? 3.535  0.732   5.314   0.30 26.86 ?  158 LYS   A HB3  1 
ATOM   3357 H HG2  A LYS   A 1 158 ? 1.971  -0.509  6.976   0.42 29.58 ?  158 LYS   A HG2  1 
ATOM   3358 H HG2  B LYS   A 1 158 ? 2.186  -1.210  5.395   0.28 22.69 ?  158 LYS   A HG2  1 
ATOM   3359 H HG2  T LYS   A 1 158 ? 2.082  -0.218  6.863   0.30 28.74 ?  158 LYS   A HG2  1 
ATOM   3360 H HG3  A LYS   A 1 158 ? 2.013  -1.317  5.614   0.42 29.58 ?  158 LYS   A HG3  1 
ATOM   3361 H HG3  B LYS   A 1 158 ? 2.968  -1.440  6.759   0.28 22.69 ?  158 LYS   A HG3  1 
ATOM   3362 H HG3  T LYS   A 1 158 ? 2.098  -1.103  5.547   0.30 28.74 ?  158 LYS   A HG3  1 
ATOM   3363 H HD2  A LYS   A 1 158 ? 3.329  -2.956  6.601   0.42 30.69 ?  158 LYS   A HD2  1 
ATOM   3364 H HD2  B LYS   A 1 158 ? 1.985  0.437   7.661   0.28 23.31 ?  158 LYS   A HD2  1 
ATOM   3365 H HD2  T LYS   A 1 158 ? 3.585  -2.598  6.633   0.30 30.19 ?  158 LYS   A HD2  1 
ATOM   3366 H HD3  A LYS   A 1 158 ? 3.405  -2.111  7.948   0.42 30.69 ?  158 LYS   A HD3  1 
ATOM   3367 H HD3  B LYS   A 1 158 ? 1.290  0.772   6.268   0.28 23.31 ?  158 LYS   A HD3  1 
ATOM   3368 H HD3  T LYS   A 1 158 ? 3.442  -1.727  7.957   0.30 30.19 ?  158 LYS   A HD3  1 
ATOM   3369 H HE2  A LYS   A 1 158 ? 1.167  -2.462  8.351   0.42 31.14 ?  158 LYS   A HE2  1 
ATOM   3370 H HE2  B LYS   A 1 158 ? 0.684  -1.498  7.833   0.28 23.51 ?  158 LYS   A HE2  1 
ATOM   3371 H HE2  T LYS   A 1 158 ? 1.176  -2.267  8.067   0.30 31.15 ?  158 LYS   A HE2  1 
ATOM   3372 H HE3  A LYS   A 1 158 ? 0.986  -3.163  6.937   0.42 31.14 ?  158 LYS   A HE3  1 
ATOM   3373 H HE3  B LYS   A 1 158 ? -0.250 -0.216  7.719   0.28 23.51 ?  158 LYS   A HE3  1 
ATOM   3374 H HE3  T LYS   A 1 158 ? 1.312  -3.123  6.734   0.30 31.15 ?  158 LYS   A HE3  1 
ATOM   3375 H HZ1  A LYS   A 1 158 ? 1.088  -4.719  8.588   0.42 31.15 ?  158 LYS   A HZ1  1 
ATOM   3376 H HZ1  B LYS   A 1 158 ? -1.037 -1.799  6.335   0.28 23.37 ?  158 LYS   A HZ1  1 
ATOM   3377 H HZ1  T LYS   A 1 158 ? 1.361  -4.477  8.558   0.30 31.58 ?  158 LYS   A HZ1  1 
ATOM   3378 H HZ2  A LYS   A 1 158 ? 2.231  -4.902  7.717   0.42 31.15 ?  158 LYS   A HZ2  1 
ATOM   3379 H HZ2  B LYS   A 1 158 ? -0.511 -0.746  5.490   0.28 23.37 ?  158 LYS   A HZ2  1 
ATOM   3380 H HZ2  T LYS   A 1 158 ? 2.640  -4.571  7.883   0.30 31.58 ?  158 LYS   A HZ2  1 
ATOM   3381 H HZ3  A LYS   A 1 158 ? 2.397  -4.263  9.007   0.42 31.15 ?  158 LYS   A HZ3  1 
ATOM   3382 H HZ3  B LYS   A 1 158 ? 0.243  -1.970  5.678   0.28 23.37 ?  158 LYS   A HZ3  1 
ATOM   3383 H HZ3  T LYS   A 1 158 ? 2.517  -3.791  9.098   0.30 31.58 ?  158 LYS   A HZ3  1 
ATOM   3384 N N    A ASN   A 1 159 ? 3.554  -1.049  2.931   0.42 20.58 ?  159 ASN   A N    1 
ATOM   3385 N N    B ASN   A 1 159 ? 3.654  -0.930  2.637   0.28 17.52 ?  159 ASN   A N    1 
ATOM   3386 N N    T ASN   A 1 159 ? 3.623  -0.998  2.822   0.30 20.77 ?  159 ASN   A N    1 
ATOM   3387 C CA   A ASN   A 1 159 ? 2.865  -1.725  1.839   0.42 19.90 ?  159 ASN   A CA   1 
ATOM   3388 C CA   B ASN   A 1 159 ? 2.932  -1.668  1.607   0.28 18.20 ?  159 ASN   A CA   1 
ATOM   3389 C CA   T ASN   A 1 159 ? 2.885  -1.693  1.775   0.30 20.83 ?  159 ASN   A CA   1 
ATOM   3390 C C    A ASN   A 1 159 ? 3.751  -2.805  1.223   0.42 18.72 ?  159 ASN   A C    1 
ATOM   3391 C C    B ASN   A 1 159 ? 3.793  -2.766  0.996   0.28 17.70 ?  159 ASN   A C    1 
ATOM   3392 C C    T ASN   A 1 159 ? 3.720  -2.806  1.144   0.30 20.41 ?  159 ASN   A C    1 
ATOM   3393 O O    A ASN   A 1 159 ? 3.297  -3.931  0.983   0.42 17.63 ?  159 ASN   A O    1 
ATOM   3394 O O    B ASN   A 1 159 ? 3.280  -3.834  0.644   0.28 17.64 ?  159 ASN   A O    1 
ATOM   3395 O O    T ASN   A 1 159 ? 3.200  -3.875  0.830   0.30 20.15 ?  159 ASN   A O    1 
ATOM   3396 C CB   A ASN   A 1 159 ? 2.377  -0.702  0.808   0.42 21.46 ?  159 ASN   A CB   1 
ATOM   3397 C CB   B ASN   A 1 159 ? 2.407  -0.706  0.540   0.28 19.97 ?  159 ASN   A CB   1 
ATOM   3398 C CB   T ASN   A 1 159 ? 2.377  -0.708  0.718   0.30 21.93 ?  159 ASN   A CB   1 
ATOM   3399 C CG   A ASN   A 1 159 ? 1.135  0.046   1.275   0.42 23.45 ?  159 ASN   A CG   1 
ATOM   3400 C CG   B ASN   A 1 159 ? 1.211  0.097   1.020   0.28 21.60 ?  159 ASN   A CG   1 
ATOM   3401 C CG   T ASN   A 1 159 ? 1.167  0.079   1.193   0.30 23.22 ?  159 ASN   A CG   1 
ATOM   3402 O OD1  A ASN   A 1 159 ? 0.304  -0.508  1.994   0.42 24.74 ?  159 ASN   A OD1  1 
ATOM   3403 O OD1  B ASN   A 1 159 ? 0.392  -0.397  1.793   0.28 22.59 ?  159 ASN   A OD1  1 
ATOM   3404 O OD1  T ASN   A 1 159 ? 0.370  -0.413  1.990   0.30 24.06 ?  159 ASN   A OD1  1 
ATOM   3405 N ND2  A ASN   A 1 159 ? 1.005  1.307   0.868   0.42 24.22 ?  159 ASN   A ND2  1 
ATOM   3406 N ND2  B ASN   A 1 159 ? 1.106  1.340   0.565   0.28 22.22 ?  159 ASN   A ND2  1 
ATOM   3407 N ND2  T ASN   A 1 159 ? 1.025  1.306   0.706   0.30 23.75 ?  159 ASN   A ND2  1 
ATOM   3408 H H    A ASN   A 1 159 ? 3.662  -0.200  2.830   0.42 24.70 ?  159 ASN   A H    1 
ATOM   3409 H H    B ASN   A 1 159 ? 3.782  -0.099  2.472   0.28 21.03 ?  159 ASN   A H    1 
ATOM   3410 H H    T ASN   A 1 159 ? 3.756  -0.161  2.673   0.30 24.93 ?  159 ASN   A H    1 
ATOM   3411 H HA   A ASN   A 1 159 ? 2.082  -2.164  2.196   0.42 23.89 ?  159 ASN   A HA   1 
ATOM   3412 H HA   B ASN   A 1 159 ? 2.165  -2.096  2.016   0.28 21.84 ?  159 ASN   A HA   1 
ATOM   3413 H HA   T ASN   A 1 159 ? 2.112  -2.114  2.174   0.30 25.00 ?  159 ASN   A HA   1 
ATOM   3414 H HB2  A ASN   A 1 159 ? 3.071  -0.044  0.648   0.42 25.76 ?  159 ASN   A HB2  1 
ATOM   3415 H HB2  B ASN   A 1 159 ? 3.108  -0.080  0.302   0.28 23.97 ?  159 ASN   A HB2  1 
ATOM   3416 H HB2  T ASN   A 1 159 ? 3.080  -0.075  0.506   0.30 26.32 ?  159 ASN   A HB2  1 
ATOM   3417 H HB3  A ASN   A 1 159 ? 2.153  -1.157  -0.018  0.42 25.76 ?  159 ASN   A HB3  1 
ATOM   3418 H HB3  B ASN   A 1 159 ? 2.134  -1.215  -0.240  0.28 23.97 ?  159 ASN   A HB3  1 
ATOM   3419 H HB3  T ASN   A 1 159 ? 2.122  -1.201  -0.079  0.30 26.32 ?  159 ASN   A HB3  1 
ATOM   3420 H HD21 A ASN   A 1 159 ? 0.319  1.770   1.105   0.42 29.07 ?  159 ASN   A HD21 1 
ATOM   3421 H HD21 B ASN   A 1 159 ? 0.442  1.831   0.809   0.28 26.68 ?  159 ASN   A HD21 1 
ATOM   3422 H HD21 T ASN   A 1 159 ? 0.354  1.787   0.945   0.30 28.50 ?  159 ASN   A HD21 1 
ATOM   3423 H HD22 A ASN   A 1 159 ? 1.608  1.661   0.367   0.42 29.07 ?  159 ASN   A HD22 1 
ATOM   3424 H HD22 B ASN   A 1 159 ? 1.699  1.651   0.029   0.28 26.68 ?  159 ASN   A HD22 1 
ATOM   3425 H HD22 T ASN   A 1 159 ? 1.603  1.617   0.153   0.30 28.50 ?  159 ASN   A HD22 1 
ATOM   3426 N N    A LEU   A 1 160 ? 5.035  -2.508  1.019   0.42 17.78 ?  160 LEU   A N    1 
ATOM   3427 N N    B LEU   A 1 160 ? 5.101  -2.540  0.879   0.28 16.77 ?  160 LEU   A N    1 
ATOM   3428 N N    T LEU   A 1 160 ? 5.017  -2.570  0.980   0.30 19.98 ?  160 LEU   A N    1 
ATOM   3429 C CA   A LEU   A 1 160 ? 5.930  -3.519  0.467   0.42 17.18 ?  160 LEU   A CA   1 
ATOM   3430 C CA   B LEU   A 1 160 ? 5.976  -3.593  0.374   0.28 16.18 ?  160 LEU   A CA   1 
ATOM   3431 C CA   T LEU   A 1 160 ? 5.898  -3.601  0.441   0.30 19.56 ?  160 LEU   A CA   1 
ATOM   3432 C C    A LEU   A 1 160 ? 6.088  -4.695  1.422   0.42 16.00 ?  160 LEU   A C    1 
ATOM   3433 C C    B LEU   A 1 160 ? 6.194  -4.680  1.422   0.28 14.76 ?  160 LEU   A C    1 
ATOM   3434 O O    A LEU   A 1 160 ? 6.075  -5.857  0.998   0.42 15.55 ?  160 LEU   A O    1 
ATOM   3435 O O    B LEU   A 1 160 ? 6.229  -5.871  1.090   0.28 14.41 ?  160 LEU   A O    1 
ATOM   3436 C CB   A LEU   A 1 160 ? 7.285  -2.898  0.143   0.42 17.34 ?  160 LEU   A CB   1 
ATOM   3437 C CB   B LEU   A 1 160 ? 7.303  -2.992  -0.085  0.28 16.90 ?  160 LEU   A CB   1 
ATOM   3438 C CB   T LEU   A 1 160 ? 7.266  -3.019  0.095   0.30 19.06 ?  160 LEU   A CB   1 
ATOM   3439 C CG   A LEU   A 1 160 ? 8.343  -3.919  -0.271  0.42 17.82 ?  160 LEU   A CG   1 
ATOM   3440 C CG   B LEU   A 1 160 ? 8.294  -3.939  -0.758  0.28 17.97 ?  160 LEU   A CG   1 
ATOM   3441 C CG   T LEU   A 1 160 ? 8.316  -4.055  -0.306  0.30 18.89 ?  160 LEU   A CG   1 
ATOM   3442 C CD1  A LEU   A 1 160 ? 7.866  -4.723  -1.463  0.42 18.28 ?  160 LEU   A CD1  1 
ATOM   3443 C CD1  B LEU   A 1 160 ? 7.629  -4.711  -1.883  0.28 18.56 ?  160 LEU   A CD1  1 
ATOM   3444 C CD1  T LEU   A 1 160 ? 7.874  -4.827  -1.533  0.30 19.18 ?  160 LEU   A CD1  1 
ATOM   3445 C CD2  A LEU   A 1 160 ? 9.649  -3.225  -0.586  0.42 17.73 ?  160 LEU   A CD2  1 
ATOM   3446 C CD2  B LEU   A 1 160 ? 9.471  -3.140  -1.284  0.28 18.03 ?  160 LEU   A CD2  1 
ATOM   3447 C CD2  T LEU   A 1 160 ? 9.652  -3.383  -0.551  0.30 18.57 ?  160 LEU   A CD2  1 
ATOM   3448 H H    A LEU   A 1 160 ? 5.405  -1.750  1.206   0.42 21.34 ?  160 LEU   A H    1 
ATOM   3449 H H    B LEU   A 1 160 ? 5.493  -1.800  1.078   0.28 20.13 ?  160 LEU   A H    1 
ATOM   3450 H H    T LEU   A 1 160 ? 5.412  -1.829  1.177   0.30 23.98 ?  160 LEU   A H    1 
ATOM   3451 H HA   A LEU   A 1 160 ? 5.549  -3.849  -0.356  0.42 20.62 ?  160 LEU   A HA   1 
ATOM   3452 H HA   B LEU   A 1 160 ? 5.547  -3.996  -0.398  0.28 19.42 ?  160 LEU   A HA   1 
ATOM   3453 H HB2  A LEU   A 1 160 ? 7.180  -2.259  -0.586  0.42 20.81 ?  160 LEU   A HB2  1 
ATOM   3454 H HB2  B LEU   A 1 160 ? 7.113  -2.282  -0.719  0.28 20.28 ?  160 LEU   A HB2  1 
ATOM   3455 H HB2  T LEU   A 1 160 ? 7.166  -2.386  -0.638  0.30 22.88 ?  160 LEU   A HB2  1 
ATOM   3456 H HB3  A LEU   A 1 160 ? 7.616  -2.441  0.932   0.42 20.81 ?  160 LEU   A HB3  1 
ATOM   3457 H HB3  B LEU   A 1 160 ? 7.748  -2.617  0.690   0.28 20.28 ?  160 LEU   A HB3  1 
ATOM   3458 H HB3  T LEU   A 1 160 ? 7.612  -2.564  0.877   0.30 22.88 ?  160 LEU   A HB3  1 
ATOM   3459 H HG   A LEU   A 1 160 ? 8.508  -4.529  0.462   0.42 21.40 ?  160 LEU   A HG   1 
ATOM   3460 H HG   B LEU   A 1 160 ? 8.626  -4.575  -0.105  0.28 21.57 ?  160 LEU   A HG   1 
ATOM   3461 H HG   T LEU   A 1 160 ? 8.430  -4.683  0.423   0.30 22.68 ?  160 LEU   A HG   1 
ATOM   3462 H HD11 A LEU   A 1 160 ? 8.586  -5.291  -1.765  0.42 21.94 ?  160 LEU   A HD11 1 
ATOM   3463 H HD11 B LEU   A 1 160 ? 8.308  -5.192  -2.379  0.28 22.27 ?  160 LEU   A HD11 1 
ATOM   3464 H HD11 T LEU   A 1 160 ? 8.593  -5.412  -1.813  0.30 23.02 ?  160 LEU   A HD11 1 
ATOM   3465 H HD12 A LEU   A 1 160 ? 7.107  -5.266  -1.196  0.42 21.94 ?  160 LEU   A HD12 1 
ATOM   3466 H HD12 B LEU   A 1 160 ? 6.993  -5.338  -1.503  0.28 22.27 ?  160 LEU   A HD12 1 
ATOM   3467 H HD12 T LEU   A 1 160 ? 7.089  -5.351  -1.309  0.30 23.02 ?  160 LEU   A HD12 1 
ATOM   3468 H HD13 A LEU   A 1 160 ? 7.602  -4.112  -2.170  0.42 21.94 ?  160 LEU   A HD13 1 
ATOM   3469 H HD13 B LEU   A 1 160 ? 7.171  -4.086  -2.467  0.28 22.27 ?  160 LEU   A HD13 1 
ATOM   3470 H HD13 T LEU   A 1 160 ? 7.662  -4.199  -2.241  0.30 23.02 ?  160 LEU   A HD13 1 
ATOM   3471 H HD21 A LEU   A 1 160 ? 10.307 -3.891  -0.844  0.42 21.28 ?  160 LEU   A HD21 1 
ATOM   3472 H HD21 B LEU   A 1 160 ? 10.151 -3.752  -1.605  0.28 21.64 ?  160 LEU   A HD21 1 
ATOM   3473 H HD21 T LEU   A 1 160 ? 10.303 -4.057  -0.803  0.30 22.29 ?  160 LEU   A HD21 1 
ATOM   3474 H HD22 A LEU   A 1 160 ? 9.510  -2.599  -1.315  0.42 21.28 ?  160 LEU   A HD22 1 
ATOM   3475 H HD22 B LEU   A 1 160 ? 9.167  -2.572  -2.010  0.28 21.64 ?  160 LEU   A HD22 1 
ATOM   3476 H HD22 T LEU   A 1 160 ? 9.554  -2.736  -1.268  0.30 22.29 ?  160 LEU   A HD22 1 
ATOM   3477 H HD23 A LEU   A 1 160 ? 9.954  -2.749  0.203   0.42 21.28 ?  160 LEU   A HD23 1 
ATOM   3478 H HD23 B LEU   A 1 160 ? 9.828  -2.595  -0.565  0.28 21.64 ?  160 LEU   A HD23 1 
ATOM   3479 H HD23 T LEU   A 1 160 ? 9.936  -2.935  0.261   0.30 22.29 ?  160 LEU   A HD23 1 
ATOM   3480 N N    A TYR   A 1 161 ? 6.239  -4.412  2.715   0.72 16.37 ?  161 TYR   A N    1 
ATOM   3481 N N    B TYR   A 1 161 ? 6.346  -4.293  2.692   0.28 14.23 ?  161 TYR   A N    1 
ATOM   3482 C CA   A TYR   A 1 161 ? 6.370  -5.472  3.706   0.72 16.24 ?  161 TYR   A CA   1 
ATOM   3483 C CA   B TYR   A 1 161 ? 6.435  -5.289  3.756   0.28 13.65 ?  161 TYR   A CA   1 
ATOM   3484 C C    A TYR   A 1 161 ? 5.223  -6.474  3.606   0.72 16.75 ?  161 TYR   A C    1 
ATOM   3485 C C    B TYR   A 1 161 ? 5.213  -6.198  3.752   0.28 13.93 ?  161 TYR   A C    1 
ATOM   3486 O O    A TYR   A 1 161 ? 5.442  -7.691  3.573   0.72 16.12 ?  161 TYR   A O    1 
ATOM   3487 O O    B TYR   A 1 161 ? 5.334  -7.427  3.815   0.28 13.75 ?  161 TYR   A O    1 
ATOM   3488 C CB   A TYR   A 1 161 ? 6.426  -4.856  5.103   0.72 16.12 ?  161 TYR   A CB   1 
ATOM   3489 C CB   B TYR   A 1 161 ? 6.587  -4.612  5.120   0.28 13.22 ?  161 TYR   A CB   1 
ATOM   3490 C CG   A TYR   A 1 161 ? 6.350  -5.889  6.190   0.72 15.35 ?  161 TYR   A CG   1 
ATOM   3491 C CG   B TYR   A 1 161 ? 6.454  -5.583  6.282   0.28 12.75 ?  161 TYR   A CG   1 
ATOM   3492 C CD1  A TYR   A 1 161 ? 7.477  -6.597  6.578   0.72 15.06 ?  161 TYR   A CD1  1 
ATOM   3493 C CD1  B TYR   A 1 161 ? 7.548  -6.313  6.734   0.28 13.07 ?  161 TYR   A CD1  1 
ATOM   3494 C CD2  A TYR   A 1 161 ? 5.146  -6.173  6.821   0.72 14.93 ?  161 TYR   A CD2  1 
ATOM   3495 C CD2  B TYR   A 1 161 ? 5.235  -5.769  6.930   0.28 12.84 ?  161 TYR   A CD2  1 
ATOM   3496 C CE1  A TYR   A 1 161 ? 7.412  -7.554  7.558   0.72 14.44 ?  161 TYR   A CE1  1 
ATOM   3497 C CE1  B TYR   A 1 161 ? 7.433  -7.202  7.794   0.28 13.45 ?  161 TYR   A CE1  1 
ATOM   3498 C CE2  A TYR   A 1 161 ? 5.070  -7.133  7.803   0.72 14.26 ?  161 TYR   A CE2  1 
ATOM   3499 C CE2  B TYR   A 1 161 ? 5.112  -6.654  7.992   0.28 13.55 ?  161 TYR   A CE2  1 
ATOM   3500 C CZ   A TYR   A 1 161 ? 6.207  -7.818  8.169   0.72 14.08 ?  161 TYR   A CZ   1 
ATOM   3501 C CZ   B TYR   A 1 161 ? 6.214  -7.367  8.417   0.28 14.06 ?  161 TYR   A CZ   1 
ATOM   3502 O OH   A TYR   A 1 161 ? 6.146  -8.772  9.150   0.72 14.62 ?  161 TYR   A OH   1 
ATOM   3503 O OH   B TYR   A 1 161 ? 6.095  -8.249  9.469   0.28 15.36 ?  161 TYR   A OH   1 
ATOM   3504 H H    A TYR   A 1 161 ? 6.255  -3.618  3.045   0.72 19.64 ?  161 TYR   A H    1 
ATOM   3505 H H    B TYR   A 1 161 ? 6.398  -3.475  2.952   0.28 17.08 ?  161 TYR   A H    1 
ATOM   3506 H HA   A TYR   A 1 161 ? 7.195  -5.951  3.554   0.72 19.49 ?  161 TYR   A HA   1 
ATOM   3507 H HA   B TYR   A 1 161 ? 7.220  -5.836  3.606   0.28 16.39 ?  161 TYR   A HA   1 
ATOM   3508 H HB2  A TYR   A 1 161 ? 7.266  -4.380  5.202   0.72 19.35 ?  161 TYR   A HB2  1 
ATOM   3509 H HB2  B TYR   A 1 161 ? 7.465  -4.200  5.173   0.28 15.86 ?  161 TYR   A HB2  1 
ATOM   3510 H HB3  A TYR   A 1 161 ? 5.681  -4.246  5.214   0.72 19.35 ?  161 TYR   A HB3  1 
ATOM   3511 H HB3  B TYR   A 1 161 ? 5.900  -3.932  5.215   0.28 15.86 ?  161 TYR   A HB3  1 
ATOM   3512 H HD1  A TYR   A 1 161 ? 8.290  -6.423  6.164   0.72 18.08 ?  161 TYR   A HD1  1 
ATOM   3513 H HD1  B TYR   A 1 161 ? 8.371  -6.205  6.319   0.28 15.69 ?  161 TYR   A HD1  1 
ATOM   3514 H HD2  A TYR   A 1 161 ? 4.373  -5.715  6.574   0.72 17.92 ?  161 TYR   A HD2  1 
ATOM   3515 H HD2  B TYR   A 1 161 ? 4.489  -5.287  6.653   0.28 15.42 ?  161 TYR   A HD2  1 
ATOM   3516 H HE1  A TYR   A 1 161 ? 8.175  -8.023  7.809   0.72 17.33 ?  161 TYR   A HE1  1 
ATOM   3517 H HE1  B TYR   A 1 161 ? 8.175  -7.684  8.086   0.28 16.15 ?  161 TYR   A HE1  1 
ATOM   3518 H HE2  A TYR   A 1 161 ? 4.253  -7.315  8.221   0.72 17.11 ?  161 TYR   A HE2  1 
ATOM   3519 H HE2  B TYR   A 1 161 ? 4.290  -6.764  8.419   0.28 16.27 ?  161 TYR   A HE2  1 
ATOM   3520 H HH   A TYR   A 1 161 ? 6.900  -9.121  9.270   0.72 17.55 ?  161 TYR   A HH   1 
ATOM   3521 H HH   B TYR   A 1 161 ? 6.831  -8.614  9.632   0.28 18.43 ?  161 TYR   A HH   1 
ATOM   3522 N N    A ASP   A 1 162 ? 3.983  -5.978  3.566   0.72 17.43 ?  162 ASP   A N    1 
ATOM   3523 N N    B ASP   A 1 162 ? 4.018  -5.606  3.686   0.28 14.20 ?  162 ASP   A N    1 
ATOM   3524 C CA   A ASP   A 1 162 ? 2.833  -6.879  3.496   0.72 18.11 ?  162 ASP   A CA   1 
ATOM   3525 C CA   B ASP   A 1 162 ? 2.802  -6.414  3.654   0.28 14.82 ?  162 ASP   A CA   1 
ATOM   3526 C C    A ASP   A 1 162 ? 2.873  -7.720  2.228   0.72 18.30 ?  162 ASP   A C    1 
ATOM   3527 C C    B ASP   A 1 162 ? 2.823  -7.389  2.484   0.28 15.49 ?  162 ASP   A C    1 
ATOM   3528 O O    A ASP   A 1 162 ? 2.514  -8.904  2.246   0.72 18.40 ?  162 ASP   A O    1 
ATOM   3529 O O    B ASP   A 1 162 ? 2.481  -8.568  2.639   0.28 15.66 ?  162 ASP   A O    1 
ATOM   3530 C CB   A ASP   A 1 162 ? 1.525  -6.086  3.559   0.72 19.36 ?  162 ASP   A CB   1 
ATOM   3531 C CB   B ASP   A 1 162 ? 1.567  -5.514  3.569   0.28 15.00 ?  162 ASP   A CB   1 
ATOM   3532 C CG   A ASP   A 1 162 ? 1.250  -5.503  4.931   0.72 20.81 ?  162 ASP   A CG   1 
ATOM   3533 C CG   B ASP   A 1 162 ? 1.314  -4.729  4.842   0.28 14.58 ?  162 ASP   A CG   1 
ATOM   3534 O OD1  A ASP   A 1 162 ? 1.872  -5.951  5.915   0.72 21.79 ?  162 ASP   A OD1  1 
ATOM   3535 O OD1  B ASP   A 1 162 ? 1.825  -5.132  5.908   0.28 14.68 ?  162 ASP   A OD1  1 
ATOM   3536 O OD2  A ASP   A 1 162 ? 0.375  -4.614  5.025   0.72 21.81 -1 162 ASP   A OD2  1 
ATOM   3537 O OD2  B ASP   A 1 162 ? 0.587  -3.710  4.776   0.28 14.69 -1 162 ASP   A OD2  1 
ATOM   3538 H H    A ASP   A 1 162 ? 3.782  -5.146  3.581   0.72 20.93 ?  162 ASP   A H    1 
ATOM   3539 H H    B ASP   A 1 162 ? 3.888  -4.756  3.660   0.28 17.05 ?  162 ASP   A H    1 
ATOM   3540 H HA   A ASP   A 1 162 ? 2.850  -7.485  4.253   0.72 21.74 ?  162 ASP   A HA   1 
ATOM   3541 H HA   B ASP   A 1 162 ? 2.748  -6.931  4.471   0.28 17.79 ?  162 ASP   A HA   1 
ATOM   3542 H HB2  A ASP   A 1 162 ? 1.566  -5.355  2.924   0.72 23.24 ?  162 ASP   A HB2  1 
ATOM   3543 H HB2  B ASP   A 1 162 ? 1.688  -4.880  2.848   0.28 18.01 ?  162 ASP   A HB2  1 
ATOM   3544 H HB3  A ASP   A 1 162 ? 0.784  -6.673  3.345   0.72 23.24 ?  162 ASP   A HB3  1 
ATOM   3545 H HB3  B ASP   A 1 162 ? 0.789  -6.066  3.405   0.28 18.01 ?  162 ASP   A HB3  1 
ATOM   3546 N N    A LYS   A 1 163 ? 3.301  -7.124  1.115   0.72 19.33 ?  163 LYS   A N    1 
ATOM   3547 N N    B LYS   A 1 163 ? 3.219  -6.914  1.301   0.28 16.43 ?  163 LYS   A N    1 
ATOM   3548 C CA   A LYS   A 1 163 ? 3.404  -7.879  -0.128  0.72 19.93 ?  163 LYS   A CA   1 
ATOM   3549 C CA   B LYS   A 1 163 ? 3.276  -7.792  0.138   0.28 17.65 ?  163 LYS   A CA   1 
ATOM   3550 C C    A LYS   A 1 163 ? 4.470  -8.967  -0.027  0.72 19.03 ?  163 LYS   A C    1 
ATOM   3551 C C    B LYS   A 1 163 ? 4.416  -8.796  0.241   0.28 17.03 ?  163 LYS   A C    1 
ATOM   3552 O O    A LYS   A 1 163 ? 4.285  -10.077 -0.536  0.72 19.49 ?  163 LYS   A O    1 
ATOM   3553 O O    B LYS   A 1 163 ? 4.276  -9.933  -0.219  0.28 16.77 ?  163 LYS   A O    1 
ATOM   3554 C CB   A LYS   A 1 163 ? 3.700  -6.929  -1.290  0.72 22.36 ?  163 LYS   A CB   1 
ATOM   3555 C CB   B LYS   A 1 163 ? 3.396  -6.963  -1.141  0.28 20.01 ?  163 LYS   A CB   1 
ATOM   3556 C CG   A LYS   A 1 163 ? 3.768  -7.622  -2.637  0.72 25.86 ?  163 LYS   A CG   1 
ATOM   3557 C CG   B LYS   A 1 163 ? 3.513  -7.778  -2.420  0.28 22.44 ?  163 LYS   A CG   1 
ATOM   3558 C CD   A LYS   A 1 163 ? 4.189  -6.669  -3.740  0.72 29.35 ?  163 LYS   A CD   1 
ATOM   3559 C CD   B LYS   A 1 163 ? 3.545  -6.859  -3.627  0.28 24.57 ?  163 LYS   A CD   1 
ATOM   3560 C CE   A LYS   A 1 163 ? 4.104  -7.345  -5.099  0.72 32.05 ?  163 LYS   A CE   1 
ATOM   3561 C CE   B LYS   A 1 163 ? 3.885  -7.602  -4.907  0.28 26.20 ?  163 LYS   A CE   1 
ATOM   3562 N NZ   A LYS   A 1 163 ? 4.760  -6.548  -6.170  0.72 33.53 ?  163 LYS   A NZ   1 
ATOM   3563 N NZ   B LYS   A 1 163 ? 4.032  -6.660  -6.054  0.28 27.03 ?  163 LYS   A NZ   1 
ATOM   3564 H H    A LYS   A 1 163 ? 3.536  -6.295  1.057   0.72 23.20 ?  163 LYS   A H    1 
ATOM   3565 H H    B LYS   A 1 163 ? 3.453  -6.100  1.147   0.28 19.72 ?  163 LYS   A H    1 
ATOM   3566 H HA   A LYS   A 1 163 ? 2.552  -8.303  -0.305  0.72 23.92 ?  163 LYS   A HA   1 
ATOM   3567 H HA   B LYS   A 1 163 ? 2.452  -8.295  0.084   0.28 21.19 ?  163 LYS   A HA   1 
ATOM   3568 H HB2  A LYS   A 1 163 ? 2.996  -6.257  -1.339  0.72 26.84 ?  163 LYS   A HB2  1 
ATOM   3569 H HB2  B LYS   A 1 163 ? 2.606  -6.406  -1.224  0.28 24.02 ?  163 LYS   A HB2  1 
ATOM   3570 H HB3  A LYS   A 1 163 ? 4.553  -6.494  -1.136  0.72 26.84 ?  163 LYS   A HB3  1 
ATOM   3571 H HB3  B LYS   A 1 163 ? 4.184  -6.404  -1.079  0.28 24.02 ?  163 LYS   A HB3  1 
ATOM   3572 H HG2  A LYS   A 1 163 ? 4.418  -8.340  -2.597  0.72 31.04 ?  163 LYS   A HG2  1 
ATOM   3573 H HG2  B LYS   A 1 163 ? 4.336  -8.292  -2.408  0.28 26.93 ?  163 LYS   A HG2  1 
ATOM   3574 H HG3  A LYS   A 1 163 ? 2.891  -7.975  -2.857  0.72 31.04 ?  163 LYS   A HG3  1 
ATOM   3575 H HG3  B LYS   A 1 163 ? 2.746  -8.368  -2.502  0.28 26.93 ?  163 LYS   A HG3  1 
ATOM   3576 H HD2  A LYS   A 1 163 ? 3.597  -5.900  -3.744  0.72 35.23 ?  163 LYS   A HD2  1 
ATOM   3577 H HD2  B LYS   A 1 163 ? 2.672  -6.451  -3.739  0.28 29.50 ?  163 LYS   A HD2  1 
ATOM   3578 H HD3  A LYS   A 1 163 ? 5.105  -6.389  -3.591  0.72 35.23 ?  163 LYS   A HD3  1 
ATOM   3579 H HD3  B LYS   A 1 163 ? 4.218  -6.175  -3.487  0.28 29.50 ?  163 LYS   A HD3  1 
ATOM   3580 H HE2  A LYS   A 1 163 ? 4.531  -8.214  -5.051  0.72 38.47 ?  163 LYS   A HE2  1 
ATOM   3581 H HE2  B LYS   A 1 163 ? 4.723  -8.076  -4.790  0.28 31.45 ?  163 LYS   A HE2  1 
ATOM   3582 H HE3  A LYS   A 1 163 ? 3.172  -7.453  -5.337  0.72 38.47 ?  163 LYS   A HE3  1 
ATOM   3583 H HE3  B LYS   A 1 163 ? 3.173  -8.225  -5.115  0.28 31.45 ?  163 LYS   A HE3  1 
ATOM   3584 H HZ1  A LYS   A 1 163 ? 4.692  -6.973  -6.949  0.72 40.24 ?  163 LYS   A HZ1  1 
ATOM   3585 H HZ1  B LYS   A 1 163 ? 4.232  -7.110  -6.795  0.28 32.44 ?  163 LYS   A HZ1  1 
ATOM   3586 H HZ2  A LYS   A 1 163 ? 4.365  -5.753  -6.239  0.72 40.24 ?  163 LYS   A HZ2  1 
ATOM   3587 H HZ2  B LYS   A 1 163 ? 3.272  -6.215  -6.182  0.28 32.44 ?  163 LYS   A HZ2  1 
ATOM   3588 H HZ3  A LYS   A 1 163 ? 5.620  -6.428  -5.978  0.72 40.24 ?  163 LYS   A HZ3  1 
ATOM   3589 H HZ3  B LYS   A 1 163 ? 4.684  -6.076  -5.886  0.28 32.44 ?  163 LYS   A HZ3  1 
ATOM   3590 N N    A LEU   A 1 164 ? 5.597  -8.664  0.623   0.72 16.82 ?  164 LEU   A N    1 
ATOM   3591 N N    B LEU   A 1 164 ? 5.547  -8.405  0.834   0.28 16.20 ?  164 LEU   A N    1 
ATOM   3592 C CA   A LEU   A 1 164 ? 6.666  -9.651  0.766   0.72 15.92 ?  164 LEU   A CA   1 
ATOM   3593 C CA   B LEU   A 1 164 ? 6.658  -9.342  0.975   0.28 15.49 ?  164 LEU   A CA   1 
ATOM   3594 C C    A LEU   A 1 164 ? 6.224  -10.819 1.641   0.72 16.04 ?  164 LEU   A C    1 
ATOM   3595 C C    B LEU   A 1 164 ? 6.263  -10.543 1.825   0.28 15.27 ?  164 LEU   A C    1 
ATOM   3596 O O    A LEU   A 1 164 ? 6.517  -11.980 1.332   0.72 16.16 ?  164 LEU   A O    1 
ATOM   3597 O O    B LEU   A 1 164 ? 6.592  -11.688 1.490   0.28 15.50 ?  164 LEU   A O    1 
ATOM   3598 C CB   A LEU   A 1 164 ? 7.901  -8.990  1.372   0.72 15.75 ?  164 LEU   A CB   1 
ATOM   3599 C CB   B LEU   A 1 164 ? 7.871  -8.634  1.578   0.28 15.23 ?  164 LEU   A CB   1 
ATOM   3600 C CG   A LEU   A 1 164 ? 8.637  -7.982  0.489   0.72 16.01 ?  164 LEU   A CG   1 
ATOM   3601 C CG   B LEU   A 1 164 ? 8.762  -7.870  0.596   0.28 15.61 ?  164 LEU   A CG   1 
ATOM   3602 C CD1  A LEU   A 1 164 ? 9.521  -7.089  1.342   0.72 15.14 ?  164 LEU   A CD1  1 
ATOM   3603 C CD1  B LEU   A 1 164 ? 9.783  -7.044  1.355   0.28 15.82 ?  164 LEU   A CD1  1 
ATOM   3604 C CD2  A LEU   A 1 164 ? 9.462  -8.697  -0.565  0.72 16.32 ?  164 LEU   A CD2  1 
ATOM   3605 C CD2  B LEU   A 1 164 ? 9.456  -8.821  -0.372  0.28 15.46 ?  164 LEU   A CD2  1 
ATOM   3606 H H    A LEU   A 1 164 ? 5.765  -7.898  0.983   0.72 20.19 ?  164 LEU   A H    1 
ATOM   3607 H H    B LEU   A 1 164 ? 5.692  -7.617  1.157   0.28 19.45 ?  164 LEU   A H    1 
ATOM   3608 H HA   A LEU   A 1 164 ? 6.901  -9.993  -0.111  0.72 19.11 ?  164 LEU   A HA   1 
ATOM   3609 H HA   B LEU   A 1 164 ? 6.909  -9.664  0.097   0.28 18.59 ?  164 LEU   A HA   1 
ATOM   3610 H HB2  A LEU   A 1 164 ? 7.634  -8.524  2.175   0.72 18.90 ?  164 LEU   A HB2  1 
ATOM   3611 H HB2  B LEU   A 1 164 ? 7.558  -7.994  2.237   0.28 18.28 ?  164 LEU   A HB2  1 
ATOM   3612 H HB3  A LEU   A 1 164 ? 8.536  -9.687  1.595   0.72 18.90 ?  164 LEU   A HB3  1 
ATOM   3613 H HB3  B LEU   A 1 164 ? 8.427  -9.298  2.012   0.28 18.28 ?  164 LEU   A HB3  1 
ATOM   3614 H HG   A LEU   A 1 164 ? 7.988  -7.419  0.036   0.72 19.22 ?  164 LEU   A HG   1 
ATOM   3615 H HG   B LEU   A 1 164 ? 8.213  -7.263  0.077   0.28 18.74 ?  164 LEU   A HG   1 
ATOM   3616 H HD11 A LEU   A 1 164 ? 9.983  -6.459  0.768   0.72 18.17 ?  164 LEU   A HD11 1 
ATOM   3617 H HD11 B LEU   A 1 164 ? 10.338 -6.567  0.719   0.28 18.98 ?  164 LEU   A HD11 1 
ATOM   3618 H HD12 A LEU   A 1 164 ? 8.966  -6.611  1.979   0.72 18.17 ?  164 LEU   A HD12 1 
ATOM   3619 H HD12 B LEU   A 1 164 ? 9.317  -6.415  1.926   0.28 18.98 ?  164 LEU   A HD12 1 
ATOM   3620 H HD13 A LEU   A 1 164 ? 10.164 -7.641  1.814   0.72 18.17 ?  164 LEU   A HD13 1 
ATOM   3621 H HD13 B LEU   A 1 164 ? 10.330 -7.638  1.893   0.28 18.98 ?  164 LEU   A HD13 1 
ATOM   3622 H HD21 A LEU   A 1 164 ? 9.918  -8.036  -1.110  0.72 19.59 ?  164 LEU   A HD21 1 
ATOM   3623 H HD21 B LEU   A 1 164 ? 10.136 -8.332  -0.862  0.28 18.56 ?  164 LEU   A HD21 1 
ATOM   3624 H HD22 A LEU   A 1 164 ? 10.111 -9.267  -0.124  0.72 19.59 ?  164 LEU   A HD22 1 
ATOM   3625 H HD22 B LEU   A 1 164 ? 9.865  -9.542  0.131   0.28 18.56 ?  164 LEU   A HD22 1 
ATOM   3626 H HD23 A LEU   A 1 164 ? 8.872  -9.231  -1.118  0.72 19.59 ?  164 LEU   A HD23 1 
ATOM   3627 H HD23 B LEU   A 1 164 ? 8.800  -9.180  -0.990  0.28 18.56 ?  164 LEU   A HD23 1 
ATOM   3628 N N    A VAL   A 1 165 ? 5.552  -10.524 2.753   0.72 15.79 ?  165 VAL   A N    1 
ATOM   3629 N N    B VAL   A 1 165 ? 5.557  -10.302 2.930   0.28 14.98 ?  165 VAL   A N    1 
ATOM   3630 C CA   A VAL   A 1 165 ? 5.045  -11.582 3.625   0.72 15.95 ?  165 VAL   A CA   1 
ATOM   3631 C CA   B VAL   A 1 165 ? 5.152  -11.404 3.798   0.28 15.06 ?  165 VAL   A CA   1 
ATOM   3632 C C    A VAL   A 1 165 ? 4.022  -12.431 2.885   0.72 16.28 ?  165 VAL   A C    1 
ATOM   3633 C C    B VAL   A 1 165 ? 4.096  -12.266 3.121   0.28 14.81 ?  165 VAL   A C    1 
ATOM   3634 O O    A VAL   A 1 165 ? 4.131  -13.662 2.826   0.72 15.99 ?  165 VAL   A O    1 
ATOM   3635 O O    B VAL   A 1 165 ? 4.145  -13.501 3.188   0.28 14.56 ?  165 VAL   A O    1 
ATOM   3636 C CB   A VAL   A 1 165 ? 4.452  -10.972 4.909   0.72 16.55 ?  165 VAL   A CB   1 
ATOM   3637 C CB   B VAL   A 1 165 ? 4.669  -10.870 5.159   0.28 15.43 ?  165 VAL   A CB   1 
ATOM   3638 C CG1  A VAL   A 1 165 ? 3.694  -12.026 5.710   0.72 16.66 ?  165 VAL   A CG1  1 
ATOM   3639 C CG1  B VAL   A 1 165 ? 3.971  -11.975 5.944   0.28 15.42 ?  165 VAL   A CG1  1 
ATOM   3640 C CG2  A VAL   A 1 165 ? 5.547  -10.324 5.748   0.72 17.12 ?  165 VAL   A CG2  1 
ATOM   3641 C CG2  B VAL   A 1 165 ? 5.836  -10.307 5.950   0.28 15.70 ?  165 VAL   A CG2  1 
ATOM   3642 H H    A VAL   A 1 165 ? 5.378  -9.728  3.020   0.72 18.95 ?  165 VAL   A H    1 
ATOM   3643 H H    B VAL   A 1 165 ? 5.308  -9.521  3.193   0.28 17.98 ?  165 VAL   A H    1 
ATOM   3644 H HA   A VAL   A 1 165 ? 5.783  -12.157 3.885   0.72 19.14 ?  165 VAL   A HA   1 
ATOM   3645 H HA   B VAL   A 1 165 ? 5.928  -11.961 3.965   0.28 18.08 ?  165 VAL   A HA   1 
ATOM   3646 H HB   A VAL   A 1 165 ? 3.824  -10.275 4.663   0.72 19.87 ?  165 VAL   A HB   1 
ATOM   3647 H HB   B VAL   A 1 165 ? 4.030  -10.153 5.012   0.28 18.53 ?  165 VAL   A HB   1 
ATOM   3648 H HG11 A VAL   A 1 165 ? 3.576  -11.705 6.618   0.72 19.99 ?  165 VAL   A HG11 1 
ATOM   3649 H HG11 B VAL   A 1 165 ? 3.929  -11.717 6.877   0.28 18.51 ?  165 VAL   A HG11 1 
ATOM   3650 H HG12 A VAL   A 1 165 ? 2.828  -12.173 5.299   0.72 19.99 ?  165 VAL   A HG12 1 
ATOM   3651 H HG12 B VAL   A 1 165 ? 3.073  -12.094 5.595   0.28 18.51 ?  165 VAL   A HG12 1 
ATOM   3652 H HG13 A VAL   A 1 165 ? 4.207  -12.847 5.715   0.72 19.99 ?  165 VAL   A HG13 1 
ATOM   3653 H HG13 B VAL   A 1 165 ? 4.477  -12.796 5.850   0.28 18.51 ?  165 VAL   A HG13 1 
ATOM   3654 H HG21 A VAL   A 1 165 ? 5.153  -9.953  6.554   0.72 20.54 ?  165 VAL   A HG21 1 
ATOM   3655 H HG21 B VAL   A 1 165 ? 5.510  -9.971  6.799   0.28 18.85 ?  165 VAL   A HG21 1 
ATOM   3656 H HG22 A VAL   A 1 165 ? 6.208  -10.994 5.982   0.72 20.54 ?  165 VAL   A HG22 1 
ATOM   3657 H HG22 B VAL   A 1 165 ? 6.484  -11.013 6.099   0.28 18.85 ?  165 VAL   A HG22 1 
ATOM   3658 H HG23 A VAL   A 1 165 ? 5.966  -9.614  5.232   0.72 20.54 ?  165 VAL   A HG23 1 
ATOM   3659 H HG23 B VAL   A 1 165 ? 6.242  -9.586  5.442   0.28 18.85 ?  165 VAL   A HG23 1 
ATOM   3660 N N    A SER   A 1 166 ? 3.012  -11.781 2.306   0.72 17.11 ?  166 SER   A N    1 
ATOM   3661 N N    B SER   A 1 166 ? 3.120  -11.637 2.464   0.28 15.04 ?  166 SER   A N    1 
ATOM   3662 C CA   A SER   A 1 166 ? 1.904  -12.521 1.715   0.72 18.03 ?  166 SER   A CA   1 
ATOM   3663 C CA   B SER   A 1 166 ? 1.975  -12.384 1.956   0.28 15.50 ?  166 SER   A CA   1 
ATOM   3664 C C    A SER   A 1 166 ? 2.360  -13.359 0.533   0.72 19.06 ?  166 SER   A C    1 
ATOM   3665 C C    B SER   A 1 166 ? 2.306  -13.226 0.730   0.28 16.35 ?  166 SER   A C    1 
ATOM   3666 O O    A SER   A 1 166 ? 1.751  -14.396 0.238   0.72 21.18 ?  166 SER   A O    1 
ATOM   3667 O O    B SER   A 1 166 ? 1.530  -14.129 0.396   0.28 17.24 ?  166 SER   A O    1 
ATOM   3668 C CB   A SER   A 1 166 ? 0.796  -11.555 1.284   0.72 18.95 ?  166 SER   A CB   1 
ATOM   3669 C CB   B SER   A 1 166 ? 0.833  -11.433 1.606   0.28 15.98 ?  166 SER   A CB   1 
ATOM   3670 O OG   A SER   A 1 166 ? 0.167  -10.956 2.406   0.72 19.50 ?  166 SER   A OG   1 
ATOM   3671 O OG   B SER   A 1 166 ? 1.114  -10.739 0.404   0.28 16.09 ?  166 SER   A OG   1 
ATOM   3672 H H    A SER   A 1 166 ? 2.947  -10.930 2.248   0.72 20.53 ?  166 SER   A H    1 
ATOM   3673 H H    B SER   A 1 166 ? 3.092  -10.787 2.319   0.28 18.06 ?  166 SER   A H    1 
ATOM   3674 H HA   A SER   A 1 166 ? 1.530  -13.124 2.376   0.72 21.64 ?  166 SER   A HA   1 
ATOM   3675 H HA   B SER   A 1 166 ? 1.660  -12.976 2.657   0.28 18.61 ?  166 SER   A HA   1 
ATOM   3676 H HB2  A SER   A 1 166 ? 1.178  -10.866 0.718   0.72 22.75 ?  166 SER   A HB2  1 
ATOM   3677 H HB2  B SER   A 1 166 ? 0.019  -11.948 1.488   0.28 19.18 ?  166 SER   A HB2  1 
ATOM   3678 H HB3  A SER   A 1 166 ? 0.117  -12.045 0.798   0.72 22.75 ?  166 SER   A HB3  1 
ATOM   3679 H HB3  B SER   A 1 166 ? 0.718  -10.795 2.328   0.28 19.18 ?  166 SER   A HB3  1 
ATOM   3680 H HG   A SER   A 1 166 ? -0.414 -10.405 2.157   0.72 23.41 ?  166 SER   A HG   1 
ATOM   3681 H HG   B SER   A 1 166 ? 1.826  -10.298 0.488   0.28 19.31 ?  166 SER   A HG   1 
ATOM   3682 N N    A SER   A 1 167 ? 3.422  -12.940 -0.151  0.72 17.97 ?  167 SER   A N    1 
ATOM   3683 N N    B SER   A 1 167 ? 3.413  -12.949 0.039   0.28 16.79 ?  167 SER   A N    1 
ATOM   3684 C CA   A SER   A 1 167 ? 3.914  -13.657 -1.316  0.72 18.93 ?  167 SER   A CA   1 
ATOM   3685 C CA   B SER   A 1 167 ? 3.780  -13.686 -1.166  0.28 17.90 ?  167 SER   A CA   1 
ATOM   3686 C C    A SER   A 1 167 ? 5.050  -14.618 -0.989  0.72 19.29 ?  167 SER   A C    1 
ATOM   3687 C C    B SER   A 1 167 ? 4.989  -14.593 -0.960  0.28 18.45 ?  167 SER   A C    1 
ATOM   3688 O O    A SER   A 1 167 ? 5.541  -15.299 -1.895  0.72 20.47 ?  167 SER   A O    1 
ATOM   3689 O O    B SER   A 1 167 ? 5.480  -15.191 -1.923  0.28 19.11 ?  167 SER   A O    1 
ATOM   3690 C CB   A SER   A 1 167 ? 4.355  -12.670 -2.411  0.72 19.28 ?  167 SER   A CB   1 
ATOM   3691 C CB   B SER   A 1 167 ? 4.028  -12.721 -2.329  0.28 18.52 ?  167 SER   A CB   1 
ATOM   3692 O OG   A SER   A 1 167 ? 5.422  -11.849 -1.958  0.72 19.51 ?  167 SER   A OG   1 
ATOM   3693 O OG   B SER   A 1 167 ? 5.151  -11.892 -2.078  0.28 19.02 ?  167 SER   A OG   1 
ATOM   3694 H H    A SER   A 1 167 ? 3.876  -12.231 0.046   0.72 21.57 ?  167 SER   A H    1 
ATOM   3695 H H    B SER   A 1 167 ? 3.969  -12.326 0.252   0.28 20.16 ?  167 SER   A H    1 
ATOM   3696 H HA   A SER   A 1 167 ? 3.185  -14.176 -1.680  0.72 22.72 ?  167 SER   A HA   1 
ATOM   3697 H HA   B SER   A 1 167 ? 3.032  -14.245 -1.415  0.28 21.48 ?  167 SER   A HA   1 
ATOM   3698 H HB2  A SER   A 1 167 ? 4.654  -13.172 -3.185  0.72 23.14 ?  167 SER   A HB2  1 
ATOM   3699 H HB2  B SER   A 1 167 ? 4.192  -13.238 -3.132  0.28 22.23 ?  167 SER   A HB2  1 
ATOM   3700 H HB3  A SER   A 1 167 ? 3.592  -12.113 -2.662  0.72 23.14 ?  167 SER   A HB3  1 
ATOM   3701 H HB3  B SER   A 1 167 ? 3.239  -12.166 -2.449  0.28 22.23 ?  167 SER   A HB3  1 
ATOM   3702 H HG   A SER   A 1 167 ? 5.158  -11.387 -1.300  0.72 23.42 ?  167 SER   A HG   1 
ATOM   3703 H HG   B SER   A 1 167 ? 5.015  -11.428 -1.390  0.28 22.82 ?  167 SER   A HG   1 
ATOM   3704 N N    . PHE   A 1 168 ? 5.476  -14.705 0.271   1.00 18.32 ?  168 PHE   A N    1 
ATOM   3705 C CA   . PHE   A 1 168 ? 6.650  -15.517 0.573   1.00 18.95 ?  168 PHE   A CA   1 
ATOM   3706 C C    . PHE   A 1 168 ? 6.342  -16.999 0.443   1.00 21.55 ?  168 PHE   A C    1 
ATOM   3707 O O    . PHE   A 1 168 ? 5.347  -17.494 0.988   1.00 23.06 ?  168 PHE   A O    1 
ATOM   3708 C CB   . PHE   A 1 168 ? 7.161  -15.246 1.984   1.00 17.71 ?  168 PHE   A CB   1 
ATOM   3709 C CG   . PHE   A 1 168 ? 8.425  -15.994 2.299   1.00 16.96 ?  168 PHE   A CG   1 
ATOM   3710 C CD1  . PHE   A 1 168 ? 9.611  -15.628 1.697   1.00 17.35 ?  168 PHE   A CD1  1 
ATOM   3711 C CD2  . PHE   A 1 168 ? 8.429  -17.082 3.156   1.00 17.00 ?  168 PHE   A CD2  1 
ATOM   3712 C CE1  . PHE   A 1 168 ? 10.777 -16.316 1.957   1.00 16.93 ?  168 PHE   A CE1  1 
ATOM   3713 C CE2  . PHE   A 1 168 ? 9.604  -17.769 3.425   1.00 17.02 ?  168 PHE   A CE2  1 
ATOM   3714 C CZ   . PHE   A 1 168 ? 10.775 -17.382 2.823   1.00 16.79 ?  168 PHE   A CZ   1 
ATOM   3715 H H    A PHE   A 1 168 ? 5.118  -14.311 0.947   0.72 21.99 ?  168 PHE   A H    1 
ATOM   3716 H H    B PHE   A 1 168 ? 5.150  -14.298 0.955   0.28 21.99 ?  168 PHE   A H    1 
ATOM   3717 H HA   . PHE   A 1 168 ? 7.358  -15.293 -0.055  1.00 22.74 ?  168 PHE   A HA   1 
ATOM   3718 H HB2  . PHE   A 1 168 ? 7.341  -14.299 2.081   1.00 21.26 ?  168 PHE   A HB2  1 
ATOM   3719 H HB3  . PHE   A 1 168 ? 6.482  -15.522 2.621   1.00 21.26 ?  168 PHE   A HB3  1 
ATOM   3720 H HD1  . PHE   A 1 168 ? 9.628  -14.905 1.112   1.00 20.83 ?  168 PHE   A HD1  1 
ATOM   3721 H HD2  . PHE   A 1 168 ? 7.639  -17.349 3.568   1.00 20.40 ?  168 PHE   A HD2  1 
ATOM   3722 H HE1  . PHE   A 1 168 ? 11.578 -16.054 1.553   1.00 20.32 ?  168 PHE   A HE1  1 
ATOM   3723 H HE2  . PHE   A 1 168 ? 9.598  -18.497 4.007   1.00 20.42 ?  168 PHE   A HE2  1 
ATOM   3724 H HZ   . PHE   A 1 168 ? 11.568 -17.844 2.996   1.00 20.15 ?  168 PHE   A HZ   1 
ATOM   3725 N N    A LEU   A 1 169 ? 7.222  -17.721 -0.245  0.72 23.56 ?  169 LEU   A N    1 
ATOM   3726 N N    B LEU   A 1 169 ? 7.208  -17.710 -0.275  0.28 24.38 ?  169 LEU   A N    1 
ATOM   3727 C CA   A LEU   A 1 169 ? 7.038  -19.151 -0.405  0.72 28.15 ?  169 LEU   A CA   1 
ATOM   3728 C CA   B LEU   A 1 169 ? 7.000  -19.123 -0.548  0.28 27.76 ?  169 LEU   A CA   1 
ATOM   3729 C C    A LEU   A 1 169 ? 7.887  -19.897 0.615   0.72 29.27 ?  169 LEU   A C    1 
ATOM   3730 C C    B LEU   A 1 169 ? 7.880  -19.976 0.357   0.28 28.81 ?  169 LEU   A C    1 
ATOM   3731 O O    A LEU   A 1 169 ? 7.359  -20.402 1.607   0.72 29.77 ?  169 LEU   A O    1 
ATOM   3732 O O    B LEU   A 1 169 ? 7.391  -20.594 1.303   0.28 29.15 ?  169 LEU   A O    1 
ATOM   3733 C CB   A LEU   A 1 169 ? 7.378  -19.586 -1.833  0.72 30.52 ?  169 LEU   A CB   1 
ATOM   3734 C CB   B LEU   A 1 169 ? 7.294  -19.422 -2.020  0.28 29.50 ?  169 LEU   A CB   1 
ATOM   3735 C CG   A LEU   A 1 169 ? 7.086  -21.053 -2.162  0.72 32.53 ?  169 LEU   A CG   1 
ATOM   3736 C CG   B LEU   A 1 169 ? 6.963  -20.829 -2.522  0.28 30.95 ?  169 LEU   A CG   1 
ATOM   3737 C CD1  A LEU   A 1 169 ? 5.671  -21.430 -1.748  0.72 33.34 ?  169 LEU   A CD1  1 
ATOM   3738 C CD1  B LEU   A 1 169 ? 5.519  -21.184 -2.212  0.28 31.54 ?  169 LEU   A CD1  1 
ATOM   3739 C CD2  A LEU   A 1 169 ? 7.297  -21.323 -3.645  0.72 33.10 ?  169 LEU   A CD2  1 
ATOM   3740 C CD2  B LEU   A 1 169 ? 7.233  -20.937 -4.016  0.28 31.40 ?  169 LEU   A CD2  1 
ATOM   3741 O OXT  A LEU   A 1 169 ? 9.108  -19.994 0.486   0.72 28.81 -1 169 LEU   A OXT  1 
ATOM   3742 O OXT  B LEU   A 1 169 ? 9.094  -20.058 0.173   0.28 29.03 -1 169 LEU   A OXT  1 
ATOM   3743 H H    A LEU   A 1 169 ? 7.932  -17.406 -0.620  0.72 28.28 ?  169 LEU   A H    1 
ATOM   3744 H H    B LEU   A 1 169 ? 7.933  -17.390 -0.616  0.28 29.26 ?  169 LEU   A H    1 
ATOM   3745 H HA   A LEU   A 1 169 ? 6.113  -19.369 -0.231  0.72 33.78 ?  169 LEU   A HA   1 
ATOM   3746 H HA   B LEU   A 1 169 ? 6.077  -19.347 -0.367  0.28 33.32 ?  169 LEU   A HA   1 
ATOM   3747 H HB2  A LEU   A 1 169 ? 6.861  -19.043 -2.450  0.72 36.63 ?  169 LEU   A HB2  1 
ATOM   3748 H HB2  B LEU   A 1 169 ? 6.783  -18.800 -2.562  0.28 35.40 ?  169 LEU   A HB2  1 
ATOM   3749 H HB3  A LEU   A 1 169 ? 8.323  -19.437 -1.987  0.72 36.63 ?  169 LEU   A HB3  1 
ATOM   3750 H HB3  B LEU   A 1 169 ? 8.240  -19.279 -2.176  0.28 35.40 ?  169 LEU   A HB3  1 
ATOM   3751 H HG   A LEU   A 1 169 ? 7.702  -21.615 -1.668  0.72 39.04 ?  169 LEU   A HG   1 
ATOM   3752 H HG   B LEU   A 1 169 ? 7.534  -21.470 -2.070  0.28 37.15 ?  169 LEU   A HG   1 
ATOM   3753 H HD11 A LEU   A 1 169 ? 5.435  -22.273 -2.163  0.72 40.02 ?  169 LEU   A HD11 1 
ATOM   3754 H HD11 B LEU   A 1 169 ? 5.282  -21.992 -2.693  0.28 37.85 ?  169 LEU   A HD11 1 
ATOM   3755 H HD12 A LEU   A 1 169 ? 5.637  -21.517 -0.782  0.72 40.02 ?  169 LEU   A HD12 1 
ATOM   3756 H HD12 B LEU   A 1 169 ? 5.427  -21.328 -1.257  0.28 37.85 ?  169 LEU   A HD12 1 
ATOM   3757 H HD13 A LEU   A 1 169 ? 5.061  -20.734 -2.040  0.72 40.02 ?  169 LEU   A HD13 1 
ATOM   3758 H HD13 B LEU   A 1 169 ? 4.948  -20.452 -2.495  0.28 37.85 ?  169 LEU   A HD13 1 
ATOM   3759 H HD21 A LEU   A 1 169 ? 7.113  -22.259 -3.825  0.72 39.73 ?  169 LEU   A HD21 1 
ATOM   3760 H HD21 B LEU   A 1 169 ? 7.021  -21.836 -4.312  0.28 37.69 ?  169 LEU   A HD21 1 
ATOM   3761 H HD22 A LEU   A 1 169 ? 6.691  -20.764 -4.157  0.72 39.73 ?  169 LEU   A HD22 1 
ATOM   3762 H HD22 B LEU   A 1 169 ? 6.676  -20.295 -4.485  0.28 37.69 ?  169 LEU   A HD22 1 
ATOM   3763 H HD23 A LEU   A 1 169 ? 8.215  -21.115 -3.877  0.72 39.73 ?  169 LEU   A HD23 1 
ATOM   3764 H HD23 B LEU   A 1 169 ? 8.169  -20.746 -4.183  0.28 37.69 ?  169 LEU   A HD23 1 
ATOM   3765 N N    A SER   B 1 1   ? 50.780 -9.239  -23.745 0.72 28.60 ?  1   SER   B N    1 
ATOM   3766 N N    B SER   B 1 1   ? 50.682 -9.211  -23.721 0.28 27.27 ?  1   SER   B N    1 
ATOM   3767 C CA   A SER   B 1 1   ? 51.272 -10.282 -22.825 0.72 28.61 ?  1   SER   B CA   1 
ATOM   3768 C CA   B SER   B 1 1   ? 51.193 -10.229 -22.780 0.28 27.10 ?  1   SER   B CA   1 
ATOM   3769 C C    A SER   B 1 1   ? 50.198 -11.331 -22.571 0.72 27.55 ?  1   SER   B C    1 
ATOM   3770 C C    B SER   B 1 1   ? 50.142 -11.304 -22.540 0.28 26.36 ?  1   SER   B C    1 
ATOM   3771 O O    A SER   B 1 1   ? 49.007 -11.128 -22.850 0.72 27.32 ?  1   SER   B O    1 
ATOM   3772 O O    B SER   B 1 1   ? 48.979 -11.161 -22.927 0.28 26.07 ?  1   SER   B O    1 
ATOM   3773 C CB   A SER   B 1 1   ? 51.727 -9.669  -21.503 0.72 29.53 ?  1   SER   B CB   1 
ATOM   3774 C CB   B SER   B 1 1   ? 51.586 -9.581  -21.456 0.28 27.59 ?  1   SER   B CB   1 
ATOM   3775 O OG   A SER   B 1 1   ? 50.623 -9.429  -20.652 0.72 31.49 ?  1   SER   B OG   1 
ATOM   3776 O OG   B SER   B 1 1   ? 50.457 -9.440  -20.614 0.28 28.45 ?  1   SER   B OG   1 
ATOM   3777 H H1   A SER   B 1 1   ? 50.666 -9.595  -24.550 0.72 34.32 ?  1   SER   B H1   1 
ATOM   3778 H H1   B SER   B 1 1   ? 51.369 -8.758  -24.054 0.28 32.73 ?  1   SER   B H1   1 
ATOM   3779 H H2   A SER   B 1 1   ? 50.010 -8.925  -23.440 0.72 34.32 ?  1   SER   B H2   1 
ATOM   3780 H H2   B SER   B 1 1   ? 50.242 -9.618  -24.375 0.28 32.73 ?  1   SER   B H2   1 
ATOM   3781 H H3   A SER   B 1 1   ? 51.380 -8.585  -23.785 0.72 34.32 ?  1   SER   B H3   1 
ATOM   3782 H H3   B SER   B 1 1   ? 50.140 -8.662  -23.285 0.28 32.73 ?  1   SER   B H3   1 
ATOM   3783 H HA   A SER   B 1 1   ? 52.033 -10.714 -23.237 0.72 34.34 ?  1   SER   B HA   1 
ATOM   3784 H HA   B SER   B 1 1   ? 51.977 -10.638 -23.169 0.28 32.53 ?  1   SER   B HA   1 
ATOM   3785 H HB2  A SER   B 1 1   ? 52.335 -10.286 -21.068 0.72 35.44 ?  1   SER   B HB2  1 
ATOM   3786 H HB2  B SER   B 1 1   ? 52.248 -10.141 -21.024 0.28 33.11 ?  1   SER   B HB2  1 
ATOM   3787 H HB3  A SER   B 1 1   ? 52.179 -8.828  -21.680 0.72 35.44 ?  1   SER   B HB3  1 
ATOM   3788 H HB3  B SER   B 1 1   ? 51.957 -8.702  -21.630 0.28 33.11 ?  1   SER   B HB3  1 
ATOM   3789 H HG   A SER   B 1 1   ? 50.848 -8.895  -20.042 0.72 37.79 ?  1   SER   B HG   1 
ATOM   3790 H HG   B SER   B 1 1   ? 50.598 -8.833  -20.053 0.28 34.14 ?  1   SER   B HG   1 
ATOM   3791 N N    A MET   B 1 2   ? 50.642 -12.455 -22.028 0.72 26.81 ?  2   MET   B N    1 
ATOM   3792 N N    B MET   B 1 2   ? 50.567 -12.380 -21.886 0.28 25.92 ?  2   MET   B N    1 
ATOM   3793 C CA   A MET   B 1 2   ? 49.819 -13.643 -21.856 0.72 26.70 ?  2   MET   B CA   1 
ATOM   3794 C CA   B MET   B 1 2   ? 49.756 -13.578 -21.705 0.28 25.50 ?  2   MET   B CA   1 
ATOM   3795 C C    A MET   B 1 2   ? 49.576 -13.830 -20.365 0.72 24.20 ?  2   MET   B C    1 
ATOM   3796 C C    B MET   B 1 2   ? 49.490 -13.757 -20.217 0.28 23.74 ?  2   MET   B C    1 
ATOM   3797 O O    A MET   B 1 2   ? 50.515 -14.086 -19.605 0.72 24.25 ?  2   MET   B O    1 
ATOM   3798 O O    B MET   B 1 2   ? 50.398 -14.114 -19.458 0.28 23.90 ?  2   MET   B O    1 
ATOM   3799 C CB   A MET   B 1 2   ? 50.550 -14.839 -22.453 0.72 30.66 ?  2   MET   B CB   1 
ATOM   3800 C CB   B MET   B 1 2   ? 50.501 -14.780 -22.270 0.28 27.26 ?  2   MET   B CB   1 
ATOM   3801 C CG   A MET   B 1 2   ? 49.699 -16.082 -22.648 0.72 34.21 ?  2   MET   B CG   1 
ATOM   3802 C CG   B MET   B 1 2   ? 49.617 -15.909 -22.771 0.28 28.69 ?  2   MET   B CG   1 
ATOM   3803 S SD   A MET   B 1 2   ? 50.546 -17.294 -23.680 0.72 37.65 ?  2   MET   B SD   1 
ATOM   3804 S SD   B MET   B 1 2   ? 50.529 -17.016 -23.852 0.28 30.05 ?  2   MET   B SD   1 
ATOM   3805 C CE   A MET   B 1 2   ? 51.086 -16.235 -25.015 0.72 37.92 ?  2   MET   B CE   1 
ATOM   3806 C CE   B MET   B 1 2   ? 51.457 -15.827 -24.804 0.28 30.25 ?  2   MET   B CE   1 
ATOM   3807 H H    A MET   B 1 2   ? 51.449 -12.562 -21.741 0.72 32.18 ?  2   MET   B H    1 
ATOM   3808 H H    B MET   B 1 2   ? 51.350 -12.446 -21.536 0.28 31.11 ?  2   MET   B H    1 
ATOM   3809 H HA   A MET   B 1 2   ? 48.977 -13.537 -22.322 0.72 32.04 ?  2   MET   B HA   1 
ATOM   3810 H HA   B MET   B 1 2   ? 48.922 -13.490 -22.191 0.28 30.61 ?  2   MET   B HA   1 
ATOM   3811 H HB2  A MET   B 1 2   ? 50.895 -14.553 -23.310 0.72 36.79 ?  2   MET   B HB2  1 
ATOM   3812 H HB2  B MET   B 1 2   ? 51.047 -14.437 -22.988 0.28 32.72 ?  2   MET   B HB2  1 
ATOM   3813 H HB3  A MET   B 1 2   ? 51.285 -15.090 -21.877 0.72 36.79 ?  2   MET   B HB3  1 
ATOM   3814 H HB3  B MET   B 1 2   ? 51.070 -15.164 -21.594 0.28 32.72 ?  2   MET   B HB3  1 
ATOM   3815 H HG2  A MET   B 1 2   ? 49.518 -16.483 -21.780 0.72 41.05 ?  2   MET   B HG2  1 
ATOM   3816 H HG2  B MET   B 1 2   ? 49.292 -16.423 -22.012 0.28 34.44 ?  2   MET   B HG2  1 
ATOM   3817 H HG3  A MET   B 1 2   ? 48.870 -15.846 -23.090 0.72 41.05 ?  2   MET   B HG3  1 
ATOM   3818 H HG3  B MET   B 1 2   ? 48.874 -15.553 -23.275 0.28 34.44 ?  2   MET   B HG3  1 
ATOM   3819 H HE1  A MET   B 1 2   ? 51.226 -16.777 -25.795 0.72 45.51 ?  2   MET   B HE1  1 
ATOM   3820 H HE1  B MET   B 1 2   ? 51.686 -16.246 -25.625 0.28 36.31 ?  2   MET   B HE1  1 
ATOM   3821 H HE2  A MET   B 1 2   ? 50.391 -15.575 -25.182 0.72 45.51 ?  2   MET   B HE2  1 
ATOM   3822 H HE2  B MET   B 1 2   ? 50.900 -15.046 -24.975 0.28 36.31 ?  2   MET   B HE2  1 
ATOM   3823 H HE3  A MET   B 1 2   ? 51.913 -15.783 -24.766 0.72 45.51 ?  2   MET   B HE3  1 
ATOM   3824 H HE3  B MET   B 1 2   ? 52.261 -15.565 -24.315 0.28 36.31 ?  2   MET   B HE3  1 
ATOM   3825 N N    A VAL   B 1 3   ? 48.324 -13.669 -19.946 0.72 21.65 ?  3   VAL   B N    1 
ATOM   3826 N N    B VAL   B 1 3   ? 48.256 -13.492 -19.800 0.28 21.77 ?  3   VAL   B N    1 
ATOM   3827 C CA   A VAL   B 1 3   ? 47.914 -13.923 -18.573 0.72 20.65 ?  3   VAL   B CA   1 
ATOM   3828 C CA   B VAL   B 1 3   ? 47.821 -13.758 -18.437 0.28 20.25 ?  3   VAL   B CA   1 
ATOM   3829 C C    A VAL   B 1 3   ? 46.679 -14.814 -18.596 0.72 19.06 ?  3   VAL   B C    1 
ATOM   3830 C C    B VAL   B 1 3   ? 46.567 -14.618 -18.475 0.28 18.52 ?  3   VAL   B C    1 
ATOM   3831 O O    A VAL   B 1 3   ? 45.967 -14.908 -19.599 0.72 19.28 ?  3   VAL   B O    1 
ATOM   3832 O O    B VAL   B 1 3   ? 45.735 -14.504 -19.379 0.28 18.22 ?  3   VAL   B O    1 
ATOM   3833 C CB   A VAL   B 1 3   ? 47.638 -12.619 -17.792 0.72 22.28 ?  3   VAL   B CB   1 
ATOM   3834 C CB   B VAL   B 1 3   ? 47.571 -12.468 -17.627 0.28 20.69 ?  3   VAL   B CB   1 
ATOM   3835 C CG1  A VAL   B 1 3   ? 48.910 -11.770 -17.693 0.72 22.69 ?  3   VAL   B CG1  1 
ATOM   3836 C CG1  B VAL   B 1 3   ? 48.850 -11.647 -17.520 0.28 20.83 ?  3   VAL   B CG1  1 
ATOM   3837 C CG2  A VAL   B 1 3   ? 46.516 -11.834 -18.449 0.72 23.26 ?  3   VAL   B CG2  1 
ATOM   3838 C CG2  B VAL   B 1 3   ? 46.449 -11.655 -18.250 0.28 20.99 ?  3   VAL   B CG2  1 
ATOM   3839 H H    A VAL   B 1 3   ? 47.683 -13.404 -20.453 0.72 25.98 ?  3   VAL   B H    1 
ATOM   3840 H H    B VAL   B 1 3   ? 47.652 -13.143 -20.303 0.28 26.13 ?  3   VAL   B H    1 
ATOM   3841 H HA   A VAL   B 1 3   ? 48.623 -14.401 -18.113 0.72 24.78 ?  3   VAL   B HA   1 
ATOM   3842 H HA   B VAL   B 1 3   ? 48.514 -14.262 -17.985 0.28 24.30 ?  3   VAL   B HA   1 
ATOM   3843 H HB   A VAL   B 1 3   ? 47.363 -12.845 -16.890 0.72 26.75 ?  3   VAL   B HB   1 
ATOM   3844 H HB   B VAL   B 1 3   ? 47.299 -12.716 -16.730 0.28 24.84 ?  3   VAL   B HB   1 
ATOM   3845 H HG11 A VAL   B 1 3   ? 48.712 -10.966 -17.188 0.72 27.23 ?  3   VAL   B HG11 1 
ATOM   3846 H HG11 B VAL   B 1 3   ? 48.671 -10.854 -16.992 0.28 25.00 ?  3   VAL   B HG11 1 
ATOM   3847 H HG12 A VAL   B 1 3   ? 49.597 -12.285 -17.242 0.72 27.23 ?  3   VAL   B HG12 1 
ATOM   3848 H HG12 B VAL   B 1 3   ? 49.534 -12.184 -17.090 0.28 25.00 ?  3   VAL   B HG12 1 
ATOM   3849 H HG13 A VAL   B 1 3   ? 49.202 -11.537 -18.588 0.72 27.23 ?  3   VAL   B HG13 1 
ATOM   3850 H HG13 B VAL   B 1 3   ? 49.139 -11.395 -18.411 0.28 25.00 ?  3   VAL   B HG13 1 
ATOM   3851 H HG21 A VAL   B 1 3   ? 46.453 -10.964 -18.029 0.72 27.92 ?  3   VAL   B HG21 1 
ATOM   3852 H HG21 B VAL   B 1 3   ? 46.412 -10.790 -17.817 0.28 25.19 ?  3   VAL   B HG21 1 
ATOM   3853 H HG22 A VAL   B 1 3   ? 46.711 -11.734 -19.394 0.72 27.92 ?  3   VAL   B HG22 1 
ATOM   3854 H HG22 B VAL   B 1 3   ? 46.626 -11.546 -19.197 0.28 25.19 ?  3   VAL   B HG22 1 
ATOM   3855 H HG23 A VAL   B 1 3   ? 45.683 -12.319 -18.333 0.72 27.92 ?  3   VAL   B HG23 1 
ATOM   3856 H HG23 B VAL   B 1 3   ? 45.609 -12.125 -18.124 0.28 25.19 ?  3   VAL   B HG23 1 
ATOM   3857 N N    . ASN   B 1 4   ? 46.435 -15.483 -17.470 1.00 17.13 ?  4   ASN   B N    1 
ATOM   3858 C CA   . ASN   B 1 4   ? 45.298 -16.395 -17.355 1.00 15.97 ?  4   ASN   B CA   1 
ATOM   3859 C C    . ASN   B 1 4   ? 45.242 -17.364 -18.534 1.00 16.50 ?  4   ASN   B C    1 
ATOM   3860 O O    . ASN   B 1 4   ? 44.179 -17.633 -19.090 1.00 17.11 ?  4   ASN   B O    1 
ATOM   3861 C CB   . ASN   B 1 4   ? 43.977 -15.634 -17.198 1.00 15.78 ?  4   ASN   B CB   1 
ATOM   3862 C CG   . ASN   B 1 4   ? 43.931 -14.817 -15.925 1.00 14.64 ?  4   ASN   B CG   1 
ATOM   3863 O OD1  . ASN   B 1 4   ? 44.214 -15.329 -14.843 1.00 14.45 ?  4   ASN   B OD1  1 
ATOM   3864 N ND2  . ASN   B 1 4   ? 43.590 -13.540 -16.046 1.00 15.43 ?  4   ASN   B ND2  1 
ATOM   3865 H H    A ASN   B 1 4   ? 46.919 -15.431 -16.762 0.72 20.56 ?  4   ASN   B H    1 
ATOM   3866 H H    B ASN   B 1 4   ? 47.004 -15.557 -16.830 0.28 20.56 ?  4   ASN   B H    1 
ATOM   3867 H HA   . ASN   B 1 4   ? 45.423 -16.927 -16.553 1.00 19.17 ?  4   ASN   B HA   1 
ATOM   3868 H HB2  . ASN   B 1 4   ? 43.863 -15.033 -17.948 1.00 18.95 ?  4   ASN   B HB2  1 
ATOM   3869 H HB3  . ASN   B 1 4   ? 43.246 -16.276 -17.174 1.00 18.95 ?  4   ASN   B HB3  1 
ATOM   3870 H HD21 . ASN   B 1 4   ? 43.552 -13.034 -15.347 1.00 18.52 ?  4   ASN   B HD21 1 
ATOM   3871 H HD22 . ASN   B 1 4   ? 43.407 -13.211 -16.819 1.00 18.52 ?  4   ASN   B HD22 1 
ATOM   3872 N N    . SER   B 1 5   ? 46.403 -17.891 -18.923 1.00 17.51 ?  5   SER   B N    1 
ATOM   3873 C CA   . SER   B 1 5   ? 46.495 -18.807 -20.060 1.00 19.74 ?  5   SER   B CA   1 
ATOM   3874 C C    . SER   B 1 5   ? 46.488 -20.243 -19.544 1.00 21.50 ?  5   SER   B C    1 
ATOM   3875 O O    . SER   B 1 5   ? 47.499 -20.938 -19.515 1.00 24.09 ?  5   SER   B O    1 
ATOM   3876 C CB   . SER   B 1 5   ? 47.743 -18.508 -20.886 1.00 21.21 ?  5   SER   B CB   1 
ATOM   3877 O OG   . SER   B 1 5   ? 48.921 -18.685 -20.116 1.00 24.47 ?  5   SER   B OG   1 
ATOM   3878 H H    . SER   B 1 5   ? 47.159 -17.741 -18.538 1.00 21.02 ?  5   SER   B H    1 
ATOM   3879 H HA   . SER   B 1 5   ? 45.723 -18.686 -20.633 1.00 23.69 ?  5   SER   B HA   1 
ATOM   3880 H HB2  . SER   B 1 5   ? 47.762 -19.105 -21.654 1.00 25.46 ?  5   SER   B HB2  1 
ATOM   3881 H HB3  . SER   B 1 5   ? 47.691 -17.590 -21.188 1.00 25.46 ?  5   SER   B HB3  1 
ATOM   3882 H HG   . SER   B 1 5   ? 48.992 -19.487 -19.880 1.00 29.37 ?  5   SER   B HG   1 
ATOM   3883 N N    . PHE   B 1 6   ? 45.306 -20.666 -19.109 1.00 21.81 ?  6   PHE   B N    1 
ATOM   3884 C CA   . PHE   B 1 6   ? 45.112 -22.012 -18.589 1.00 21.35 ?  6   PHE   B CA   1 
ATOM   3885 C C    . PHE   B 1 6   ? 45.049 -23.000 -19.745 1.00 24.74 ?  6   PHE   B C    1 
ATOM   3886 O O    . PHE   B 1 6   ? 44.389 -22.738 -20.754 1.00 26.58 ?  6   PHE   B O    1 
ATOM   3887 C CB   . PHE   B 1 6   ? 43.818 -22.064 -17.779 1.00 19.30 ?  6   PHE   B CB   1 
ATOM   3888 C CG   . PHE   B 1 6   ? 43.841 -21.203 -16.548 1.00 17.07 ?  6   PHE   B CG   1 
ATOM   3889 C CD1  . PHE   B 1 6   ? 44.353 -21.696 -15.362 1.00 16.16 ?  6   PHE   B CD1  1 
ATOM   3890 C CD2  . PHE   B 1 6   ? 43.358 -19.902 -16.576 1.00 16.54 ?  6   PHE   B CD2  1 
ATOM   3891 C CE1  . PHE   B 1 6   ? 44.368 -20.918 -14.218 1.00 15.81 ?  6   PHE   B CE1  1 
ATOM   3892 C CE2  . PHE   B 1 6   ? 43.385 -19.110 -15.437 1.00 17.07 ?  6   PHE   B CE2  1 
ATOM   3893 C CZ   . PHE   B 1 6   ? 43.895 -19.614 -14.259 1.00 15.95 ?  6   PHE   B CZ   1 
ATOM   3894 H H    . PHE   B 1 6   ? 44.595 -20.190 -19.107 1.00 26.17 ?  6   PHE   B H    1 
ATOM   3895 H HA   . PHE   B 1 6   ? 45.851 -22.255 -18.014 1.00 25.63 ?  6   PHE   B HA   1 
ATOM   3896 H HB2  . PHE   B 1 6   ? 43.085 -21.760 -18.340 1.00 23.17 ?  6   PHE   B HB2  1 
ATOM   3897 H HB3  . PHE   B 1 6   ? 43.658 -22.978 -17.499 1.00 23.17 ?  6   PHE   B HB3  1 
ATOM   3898 H HD1  . PHE   B 1 6   ? 44.680 -22.565 -15.329 1.00 19.39 ?  6   PHE   B HD1  1 
ATOM   3899 H HD2  . PHE   B 1 6   ? 43.012 -19.559 -17.367 1.00 19.86 ?  6   PHE   B HD2  1 
ATOM   3900 H HE1  . PHE   B 1 6   ? 44.725 -21.256 -13.426 1.00 18.98 ?  6   PHE   B HE1  1 
ATOM   3901 H HE2  . PHE   B 1 6   ? 43.054 -18.239 -15.466 1.00 20.49 ?  6   PHE   B HE2  1 
ATOM   3902 H HZ   . PHE   B 1 6   ? 43.912 -19.089 -13.491 1.00 19.15 ?  6   PHE   B HZ   1 
ATOM   3903 N N    . SER   B 1 7   ? 45.752 -24.125 -19.603 1.00 25.48 ?  7   SER   B N    1 
ATOM   3904 C CA   . SER   B 1 7   ? 45.840 -25.122 -20.660 1.00 28.13 ?  7   SER   B CA   1 
ATOM   3905 C C    . SER   B 1 7   ? 45.799 -26.522 -20.065 1.00 27.06 ?  7   SER   B C    1 
ATOM   3906 O O    . SER   B 1 7   ? 46.389 -26.780 -19.012 1.00 28.21 ?  7   SER   B O    1 
ATOM   3907 C CB   . SER   B 1 7   ? 47.131 -24.945 -21.472 1.00 31.31 ?  7   SER   B CB   1 
ATOM   3908 O OG   . SER   B 1 7   ? 47.126 -25.769 -22.624 1.00 33.38 ?  7   SER   B OG   1 
ATOM   3909 H H    . SER   B 1 7   ? 46.200 -24.330 -18.893 1.00 30.58 ?  7   SER   B H    1 
ATOM   3910 H HA   . SER   B 1 7   ? 45.087 -25.026 -21.259 1.00 33.76 ?  7   SER   B HA   1 
ATOM   3911 H HB2  . SER   B 1 7   ? 47.202 -24.019 -21.751 1.00 37.58 ?  7   SER   B HB2  1 
ATOM   3912 H HB3  . SER   B 1 7   ? 47.890 -25.180 -20.914 1.00 37.58 ?  7   SER   B HB3  1 
ATOM   3913 H HG   . SER   B 1 7   ? 47.842 -25.665 -23.053 1.00 40.06 ?  7   SER   B HG   1 
ATOM   3914 N N    . GLY   B 1 8   ? 45.100 -27.424 -20.752 1.00 26.92 ?  8   GLY   B N    1 
ATOM   3915 C CA   . GLY   B 1 8   ? 45.076 -28.816 -20.360 1.00 26.36 ?  8   GLY   B CA   1 
ATOM   3916 C C    . GLY   B 1 8   ? 44.100 -29.156 -19.262 1.00 24.73 ?  8   GLY   B C    1 
ATOM   3917 O O    . GLY   B 1 8   ? 44.214 -30.233 -18.664 1.00 26.13 ?  8   GLY   B O    1 
ATOM   3918 H H    . GLY   B 1 8   ? 44.636 -27.244 -21.449 1.00 32.31 ?  8   GLY   B H    1 
ATOM   3919 H HA2  . GLY   B 1 8   ? 44.846 -29.354 -21.132 1.00 31.64 ?  8   GLY   B HA2  1 
ATOM   3920 H HA3  . GLY   B 1 8   ? 45.959 -29.077 -20.061 1.00 31.64 ?  8   GLY   B HA3  1 
ATOM   3921 N N    . TYR   B 1 9   ? 43.128 -28.288 -18.985 1.00 22.80 ?  9   TYR   B N    1 
ATOM   3922 C CA   . TYR   B 1 9   ? 42.164 -28.558 -17.932 1.00 20.49 ?  9   TYR   B CA   1 
ATOM   3923 C C    . TYR   B 1 9   ? 40.986 -29.355 -18.458 1.00 19.91 ?  9   TYR   B C    1 
ATOM   3924 O O    . TYR   B 1 9   ? 40.585 -29.229 -19.618 1.00 21.87 ?  9   TYR   B O    1 
ATOM   3925 C CB   . TYR   B 1 9   ? 41.648 -27.269 -17.298 1.00 19.74 ?  9   TYR   B CB   1 
ATOM   3926 C CG   . TYR   B 1 9   ? 42.665 -26.640 -16.380 1.00 19.03 ?  9   TYR   B CG   1 
ATOM   3927 C CD1  . TYR   B 1 9   ? 43.767 -25.977 -16.896 1.00 19.69 ?  9   TYR   B CD1  1 
ATOM   3928 C CD2  . TYR   B 1 9   ? 42.542 -26.732 -15.001 1.00 18.26 ?  9   TYR   B CD2  1 
ATOM   3929 C CE1  . TYR   B 1 9   ? 44.716 -25.416 -16.068 1.00 19.89 ?  9   TYR   B CE1  1 
ATOM   3930 C CE2  . TYR   B 1 9   ? 43.485 -26.172 -14.161 1.00 18.55 ?  9   TYR   B CE2  1 
ATOM   3931 C CZ   . TYR   B 1 9   ? 44.571 -25.511 -14.704 1.00 19.55 ?  9   TYR   B CZ   1 
ATOM   3932 O OH   . TYR   B 1 9   ? 45.524 -24.955 -13.887 1.00 20.08 ?  9   TYR   B OH   1 
ATOM   3933 H H    . TYR   B 1 9   ? 42.990 -27.553 -19.410 1.00 27.37 ?  9   TYR   B H    1 
ATOM   3934 H HA   . TYR   B 1 9   ? 42.588 -29.081 -17.239 1.00 24.59 ?  9   TYR   B HA   1 
ATOM   3935 H HB2  . TYR   B 1 9   ? 41.429 -26.627 -17.994 1.00 23.69 ?  9   TYR   B HB2  1 
ATOM   3936 H HB3  . TYR   B 1 9   ? 40.865 -27.476 -16.773 1.00 23.69 ?  9   TYR   B HB3  1 
ATOM   3937 H HD1  . TYR   B 1 9   ? 43.871 -25.910 -17.818 1.00 23.63 ?  9   TYR   B HD1  1 
ATOM   3938 H HD2  . TYR   B 1 9   ? 41.809 -27.178 -14.636 1.00 21.92 ?  9   TYR   B HD2  1 
ATOM   3939 H HE1  . TYR   B 1 9   ? 45.444 -24.971 -16.427 1.00 23.88 ?  9   TYR   B HE1  1 
ATOM   3940 H HE2  . TYR   B 1 9   ? 43.381 -26.239 -13.236 1.00 22.26 ?  9   TYR   B HE2  1 
ATOM   3941 H HH   . TYR   B 1 9   ? 46.113 -24.583 -14.349 1.00 24.10 ?  9   TYR   B HH   1 
ATOM   3942 N N    . LEU   B 1 10  ? 40.437 -30.185 -17.578 1.00 17.99 ?  10  LEU   B N    1 
ATOM   3943 C CA   . LEU   B 1 10  ? 39.231 -30.950 -17.846 1.00 17.80 ?  10  LEU   B CA   1 
ATOM   3944 C C    . LEU   B 1 10  ? 38.042 -30.181 -17.286 1.00 17.30 ?  10  LEU   B C    1 
ATOM   3945 O O    . LEU   B 1 10  ? 38.054 -29.766 -16.122 1.00 16.98 ?  10  LEU   B O    1 
ATOM   3946 C CB   . LEU   B 1 10  ? 39.334 -32.323 -17.183 1.00 18.47 ?  10  LEU   B CB   1 
ATOM   3947 C CG   . LEU   B 1 10  ? 38.171 -33.257 -17.486 1.00 20.51 ?  10  LEU   B CG   1 
ATOM   3948 C CD1  . LEU   B 1 10  ? 38.243 -33.755 -18.923 1.00 22.30 ?  10  LEU   B CD1  1 
ATOM   3949 C CD2  . LEU   B 1 10  ? 38.149 -34.412 -16.505 1.00 22.03 ?  10  LEU   B CD2  1 
ATOM   3950 H H    . LEU   B 1 10  ? 40.754 -30.319 -16.782 1.00 21.59 ?  10  LEU   B H    1 
ATOM   3951 H HA   . LEU   B 1 10  ? 39.116 -31.066 -18.796 1.00 21.37 ?  10  LEU   B HA   1 
ATOM   3952 H HB2  . LEU   B 1 10  ? 40.148 -32.757 -17.488 1.00 22.17 ?  10  LEU   B HB2  1 
ATOM   3953 H HB3  . LEU   B 1 10  ? 39.373 -32.206 -16.218 1.00 22.17 ?  10  LEU   B HB3  1 
ATOM   3954 H HG   . LEU   B 1 10  ? 37.339 -32.769 -17.385 1.00 24.61 ?  10  LEU   B HG   1 
ATOM   3955 H HD11 . LEU   B 1 10  ? 37.526 -34.391 -19.071 1.00 26.77 ?  10  LEU   B HD11 1 
ATOM   3956 H HD12 . LEU   B 1 10  ? 38.143 -33.000 -19.524 1.00 26.77 ?  10  LEU   B HD12 1 
ATOM   3957 H HD13 . LEU   B 1 10  ? 39.101 -34.182 -19.066 1.00 26.77 ?  10  LEU   B HD13 1 
ATOM   3958 H HD21 . LEU   B 1 10  ? 37.406 -34.993 -16.724 1.00 26.44 ?  10  LEU   B HD21 1 
ATOM   3959 H HD22 . LEU   B 1 10  ? 38.984 -34.895 -16.572 1.00 26.44 ?  10  LEU   B HD22 1 
ATOM   3960 H HD23 . LEU   B 1 10  ? 38.039 -34.056 -15.609 1.00 26.44 ?  10  LEU   B HD23 1 
ATOM   3961 N N    . LYS   B 1 11  ? 37.022 -29.997 -18.113 1.00 18.65 ?  11  LYS   B N    1 
ATOM   3962 C CA   . LYS   B 1 11  ? 35.824 -29.282 -17.698 1.00 20.65 ?  11  LYS   B CA   1 
ATOM   3963 C C    . LYS   B 1 11  ? 34.943 -30.206 -16.864 1.00 19.78 ?  11  LYS   B C    1 
ATOM   3964 O O    . LYS   B 1 11  ? 34.566 -31.291 -17.320 1.00 21.86 ?  11  LYS   B O    1 
ATOM   3965 C CB   . LYS   B 1 11  ? 35.079 -28.802 -18.943 1.00 24.77 ?  11  LYS   B CB   1 
ATOM   3966 C CG   . LYS   B 1 11  ? 33.900 -27.887 -18.677 1.00 28.68 ?  11  LYS   B CG   1 
ATOM   3967 C CD   . LYS   B 1 11  ? 33.159 -27.587 -19.974 1.00 31.89 ?  11  LYS   B CD   1 
ATOM   3968 C CE   . LYS   B 1 11  ? 32.142 -26.474 -19.799 1.00 34.17 ?  11  LYS   B CE   1 
ATOM   3969 N NZ   . LYS   B 1 11  ? 32.799 -25.159 -19.586 1.00 35.45 ?  11  LYS   B NZ   1 
ATOM   3970 H H    . LYS   B 1 11  ? 36.996 -30.287 -18.923 1.00 22.39 ?  11  LYS   B H    1 
ATOM   3971 H HA   . LYS   B 1 11  ? 36.070 -28.515 -17.163 1.00 24.79 ?  11  LYS   B HA   1 
ATOM   3972 H HB2  . LYS   B 1 11  ? 35.703 -28.316 -19.505 1.00 29.73 ?  11  LYS   B HB2  1 
ATOM   3973 H HB3  . LYS   B 1 11  ? 34.746 -29.576 -19.422 1.00 29.73 ?  11  LYS   B HB3  1 
ATOM   3974 H HG2  . LYS   B 1 11  ? 33.283 -28.321 -18.067 1.00 34.43 ?  11  LYS   B HG2  1 
ATOM   3975 H HG3  . LYS   B 1 11  ? 34.216 -27.050 -18.304 1.00 34.43 ?  11  LYS   B HG3  1 
ATOM   3976 H HD2  . LYS   B 1 11  ? 33.799 -27.310 -20.650 1.00 38.28 ?  11  LYS   B HD2  1 
ATOM   3977 H HD3  . LYS   B 1 11  ? 32.691 -28.385 -20.266 1.00 38.28 ?  11  LYS   B HD3  1 
ATOM   3978 H HE2  . LYS   B 1 11  ? 31.594 -26.416 -20.598 1.00 41.01 ?  11  LYS   B HE2  1 
ATOM   3979 H HE3  . LYS   B 1 11  ? 31.589 -26.670 -19.027 1.00 41.01 ?  11  LYS   B HE3  1 
ATOM   3980 H HZ1  . LYS   B 1 11  ? 32.184 -24.521 -19.508 1.00 42.55 ?  11  LYS   B HZ1  1 
ATOM   3981 H HZ2  . LYS   B 1 11  ? 33.291 -25.181 -18.845 1.00 42.55 ?  11  LYS   B HZ2  1 
ATOM   3982 H HZ3  . LYS   B 1 11  ? 33.327 -24.968 -20.278 1.00 42.55 ?  11  LYS   B HZ3  1 
ATOM   3983 N N    . LEU   B 1 12  ? 34.611 -29.780 -15.644 1.00 18.07 ?  12  LEU   B N    1 
ATOM   3984 C CA   . LEU   B 1 12  ? 33.654 -30.491 -14.800 1.00 17.55 ?  12  LEU   B CA   1 
ATOM   3985 C C    . LEU   B 1 12  ? 32.263 -29.885 -14.884 1.00 17.36 ?  12  LEU   B C    1 
ATOM   3986 O O    . LEU   B 1 12  ? 31.274 -30.604 -15.050 1.00 18.03 ?  12  LEU   B O    1 
ATOM   3987 C CB   . LEU   B 1 12  ? 34.120 -30.503 -13.339 1.00 16.82 ?  12  LEU   B CB   1 
ATOM   3988 C CG   . LEU   B 1 12  ? 35.453 -31.197 -13.066 1.00 16.73 ?  12  LEU   B CG   1 
ATOM   3989 C CD1  . LEU   B 1 12  ? 35.808 -31.146 -11.591 1.00 16.76 ?  12  LEU   B CD1  1 
ATOM   3990 C CD2  . LEU   B 1 12  ? 35.434 -32.635 -13.566 1.00 17.57 ?  12  LEU   B CD2  1 
ATOM   3991 H H    . LEU   B 1 12  ? 34.928 -29.068 -15.284 1.00 21.69 ?  12  LEU   B H    1 
ATOM   3992 H HA   . LEU   B 1 12  ? 33.585 -31.405 -15.104 1.00 21.06 ?  12  LEU   B HA   1 
ATOM   3993 H HB2  . LEU   B 1 12  ? 34.203 -29.586 -13.038 1.00 20.19 ?  12  LEU   B HB2  1 
ATOM   3994 H HB3  . LEU   B 1 12  ? 33.444 -30.956 -12.811 1.00 20.19 ?  12  LEU   B HB3  1 
ATOM   3995 H HG   . LEU   B 1 12  ? 36.149 -30.728 -13.550 1.00 20.08 ?  12  LEU   B HG   1 
ATOM   3996 H HD11 . LEU   B 1 12  ? 36.662 -31.591 -11.455 1.00 20.11 ?  12  LEU   B HD11 1 
ATOM   3997 H HD12 . LEU   B 1 12  ? 35.875 -30.219 -11.311 1.00 20.11 ?  12  LEU   B HD12 1 
ATOM   3998 H HD13 . LEU   B 1 12  ? 35.119 -31.596 -11.079 1.00 20.11 ?  12  LEU   B HD13 1 
ATOM   3999 H HD21 . LEU   B 1 12  ? 36.230 -33.090 -13.249 1.00 21.09 ?  12  LEU   B HD21 1 
ATOM   4000 H HD22 . LEU   B 1 12  ? 34.641 -33.078 -13.226 1.00 21.09 ?  12  LEU   B HD22 1 
ATOM   4001 H HD23 . LEU   B 1 12  ? 35.420 -32.632 -14.537 1.00 21.09 ?  12  LEU   B HD23 1 
ATOM   4002 N N    . THR   B 1 13  ? 32.176 -28.564 -14.763 1.00 17.20 ?  13  THR   B N    1 
ATOM   4003 C CA   . THR   B 1 13  ? 30.947 -27.817 -14.969 1.00 17.38 ?  13  THR   B CA   1 
ATOM   4004 C C    . THR   B 1 13  ? 31.272 -26.616 -15.850 1.00 19.45 ?  13  THR   B C    1 
ATOM   4005 O O    . THR   B 1 13  ? 32.413 -26.422 -16.283 1.00 20.21 ?  13  THR   B O    1 
ATOM   4006 C CB   . THR   B 1 13  ? 30.341 -27.351 -13.640 1.00 16.96 ?  13  THR   B CB   1 
ATOM   4007 O OG1  . THR   B 1 13  ? 31.178 -26.329 -13.089 1.00 16.73 ?  13  THR   B OG1  1 
ATOM   4008 C CG2  . THR   B 1 13  ? 30.227 -28.506 -12.647 1.00 17.72 ?  13  THR   B CG2  1 
ATOM   4009 H H    . THR   B 1 13  ? 32.844 -28.058 -14.554 1.00 20.65 ?  13  THR   B H    1 
ATOM   4010 H HA   . THR   B 1 13  ? 30.298 -28.373 -15.421 1.00 20.86 ?  13  THR   B HA   1 
ATOM   4011 H HB   . THR   B 1 13  ? 29.452 -26.988 -13.796 1.00 20.35 ?  13  THR   B HB   1 
ATOM   4012 H HG1  . THR   B 1 13  ? 30.876 -25.563 -13.286 1.00 20.08 ?  13  THR   B HG1  1 
ATOM   4013 H HG21 . THR   B 1 13  ? 29.715 -28.230 -11.871 1.00 21.27 ?  13  THR   B HG21 1 
ATOM   4014 H HG22 . THR   B 1 13  ? 29.780 -29.257 -13.067 1.00 21.27 ?  13  THR   B HG22 1 
ATOM   4015 H HG23 . THR   B 1 13  ? 31.110 -28.785 -12.360 1.00 21.27 ?  13  THR   B HG23 1 
ATOM   4016 N N    A ASP   B 1 14  ? 30.256 -25.792 -16.106 0.72 20.35 ?  14  ASP   B N    1 
ATOM   4017 N N    B ASP   B 1 14  ? 30.260 -25.779 -16.096 0.28 20.28 ?  14  ASP   B N    1 
ATOM   4018 C CA   A ASP   B 1 14  ? 30.460 -24.626 -16.959 0.72 21.90 ?  14  ASP   B CA   1 
ATOM   4019 C CA   B ASP   B 1 14  ? 30.450 -24.620 -16.964 0.28 21.17 ?  14  ASP   B CA   1 
ATOM   4020 C C    A ASP   B 1 14  ? 31.561 -23.717 -16.431 0.72 19.82 ?  14  ASP   B C    1 
ATOM   4021 C C    B ASP   B 1 14  ? 31.447 -23.617 -16.403 0.28 19.30 ?  14  ASP   B C    1 
ATOM   4022 O O    A ASP   B 1 14  ? 32.218 -23.025 -17.218 0.72 21.37 ?  14  ASP   B O    1 
ATOM   4023 O O    B ASP   B 1 14  ? 31.885 -22.727 -17.140 0.28 19.63 ?  14  ASP   B O    1 
ATOM   4024 C CB   A ASP   B 1 14  ? 29.150 -23.851 -17.113 0.72 25.79 ?  14  ASP   B CB   1 
ATOM   4025 C CB   B ASP   B 1 14  ? 29.119 -23.909 -17.209 0.28 23.87 ?  14  ASP   B CB   1 
ATOM   4026 C CG   A ASP   B 1 14  ? 28.186 -24.516 -18.068 0.72 29.77 ?  14  ASP   B CG   1 
ATOM   4027 C CG   B ASP   B 1 14  ? 28.252 -24.636 -18.218 0.28 26.21 ?  14  ASP   B CG   1 
ATOM   4028 O OD1  A ASP   B 1 14  ? 28.555 -25.525 -18.714 0.72 31.03 ?  14  ASP   B OD1  1 
ATOM   4029 O OD1  B ASP   B 1 14  ? 28.814 -25.256 -19.146 0.28 26.98 ?  14  ASP   B OD1  1 
ATOM   4030 O OD2  A ASP   B 1 14  ? 27.042 -24.030 -18.167 0.72 31.33 -1 14  ASP   B OD2  1 
ATOM   4031 O OD2  B ASP   B 1 14  ? 27.012 -24.595 -18.083 0.28 26.96 -1 14  ASP   B OD2  1 
ATOM   4032 H H    A ASP   B 1 14  ? 29.458 -25.873 -15.792 0.72 24.42 ?  14  ASP   B H    1 
ATOM   4033 H H    B ASP   B 1 14  ? 29.466 -25.858 -15.775 0.28 24.34 ?  14  ASP   B H    1 
ATOM   4034 H HA   A ASP   B 1 14  ? 30.729 -24.919 -17.839 0.72 26.28 ?  14  ASP   B HA   1 
ATOM   4035 H HA   B ASP   B 1 14  ? 30.782 -24.927 -17.822 0.28 25.41 ?  14  ASP   B HA   1 
ATOM   4036 H HB2  A ASP   B 1 14  ? 28.697 -23.800 -16.258 0.72 30.95 ?  14  ASP   B HB2  1 
ATOM   4037 H HB2  B ASP   B 1 14  ? 28.630 -23.855 -16.372 0.28 28.65 ?  14  ASP   B HB2  1 
ATOM   4038 H HB3  A ASP   B 1 14  ? 29.333 -22.959 -17.447 0.72 30.95 ?  14  ASP   B HB3  1 
ATOM   4039 H HB3  B ASP   B 1 14  ? 29.299 -23.009 -17.540 0.28 28.65 ?  14  ASP   B HB3  1 
ATOM   4040 N N    . ASN   B 1 15  ? 31.791 -23.712 -15.116 1.00 17.50 ?  15  ASN   B N    1 
ATOM   4041 C CA   . ASN   B 1 15  ? 32.753 -22.791 -14.516 1.00 15.22 ?  15  ASN   B CA   1 
ATOM   4042 C C    . ASN   B 1 15  ? 33.846 -23.442 -13.679 1.00 14.06 ?  15  ASN   B C    1 
ATOM   4043 O O    . ASN   B 1 15  ? 34.689 -22.713 -13.146 1.00 14.77 ?  15  ASN   B O    1 
ATOM   4044 C CB   . ASN   B 1 15  ? 32.038 -21.738 -13.656 1.00 15.55 ?  15  ASN   B CB   1 
ATOM   4045 C CG   . ASN   B 1 15  ? 31.417 -22.336 -12.416 1.00 15.13 ?  15  ASN   B CG   1 
ATOM   4046 O OD1  . ASN   B 1 15  ? 30.474 -23.128 -12.506 1.00 16.87 ?  15  ASN   B OD1  1 
ATOM   4047 N ND2  . ASN   B 1 15  ? 31.937 -21.984 -11.256 1.00 14.57 ?  15  ASN   B ND2  1 
ATOM   4048 H H    A ASN   B 1 15  ? 31.404 -24.238 -14.553 0.72 21.00 ?  15  ASN   B H    1 
ATOM   4049 H H    B ASN   B 1 15  ? 31.451 -24.280 -14.565 0.28 21.00 ?  15  ASN   B H    1 
ATOM   4050 H HA   . ASN   B 1 15  ? 33.198 -22.312 -15.223 1.00 18.27 ?  15  ASN   B HA   1 
ATOM   4051 H HB2  . ASN   B 1 15  ? 32.686 -21.064 -13.375 1.00 18.66 ?  15  ASN   B HB2  1 
ATOM   4052 H HB3  . ASN   B 1 15  ? 31.335 -21.316 -14.175 1.00 18.66 ?  15  ASN   B HB3  1 
ATOM   4053 H HD21 . ASN   B 1 15  ? 31.612 -22.295 -10.520 1.00 17.49 ?  15  ASN   B HD21 1 
ATOM   4054 H HD22 . ASN   B 1 15  ? 32.602 -21.432 -11.223 1.00 17.49 ?  15  ASN   B HD22 1 
ATOM   4055 N N    . VAL   B 1 16  ? 33.863 -24.768 -13.532 1.00 14.09 ?  16  VAL   B N    1 
ATOM   4056 C CA   . VAL   B 1 16  ? 34.863 -25.462 -12.725 1.00 13.63 ?  16  VAL   B CA   1 
ATOM   4057 C C    . VAL   B 1 16  ? 35.655 -26.399 -13.622 1.00 14.02 ?  16  VAL   B C    1 
ATOM   4058 O O    . VAL   B 1 16  ? 35.077 -27.277 -14.281 1.00 15.22 ?  16  VAL   B O    1 
ATOM   4059 C CB   . VAL   B 1 16  ? 34.230 -26.224 -11.547 1.00 14.16 ?  16  VAL   B CB   1 
ATOM   4060 C CG1  . VAL   B 1 16  ? 35.311 -26.963 -10.757 1.00 14.05 ?  16  VAL   B CG1  1 
ATOM   4061 C CG2  . VAL   B 1 16  ? 33.445 -25.269 -10.651 1.00 14.79 ?  16  VAL   B CG2  1 
ATOM   4062 H H    . VAL   B 1 16  ? 33.291 -25.300 -13.901 1.00 16.92 ?  16  VAL   B H    1 
ATOM   4063 H HA   . VAL   B 1 16  ? 35.477 -24.809 -12.355 1.00 16.36 ?  16  VAL   B HA   1 
ATOM   4064 H HB   . VAL   B 1 16  ? 33.612 -26.886 -11.897 1.00 17.00 ?  16  VAL   B HB   1 
ATOM   4065 H HG11 . VAL   B 1 16  ? 34.934 -27.260 -9.913  1.00 16.87 ?  16  VAL   B HG11 1 
ATOM   4066 H HG12 . VAL   B 1 16  ? 35.618 -27.725 -11.268 1.00 16.87 ?  16  VAL   B HG12 1 
ATOM   4067 H HG13 . VAL   B 1 16  ? 36.048 -26.353 -10.588 1.00 16.87 ?  16  VAL   B HG13 1 
ATOM   4068 H HG21 . VAL   B 1 16  ? 33.102 -25.764 -9.891  1.00 17.75 ?  16  VAL   B HG21 1 
ATOM   4069 H HG22 . VAL   B 1 16  ? 34.033 -24.563 -10.351 1.00 17.75 ?  16  VAL   B HG22 1 
ATOM   4070 H HG23 . VAL   B 1 16  ? 32.709 -24.895 -11.161 1.00 17.75 ?  16  VAL   B HG23 1 
ATOM   4071 N N    . TYR   B 1 17  ? 36.980 -26.234 -13.600 1.00 14.31 ?  17  TYR   B N    1 
ATOM   4072 C CA   . TYR   B 1 17  ? 37.927 -26.987 -14.411 1.00 14.70 ?  17  TYR   B CA   1 
ATOM   4073 C C    . TYR   B 1 17  ? 38.980 -27.596 -13.497 1.00 13.65 ?  17  TYR   B C    1 
ATOM   4074 O O    . TYR   B 1 17  ? 39.254 -27.066 -12.418 1.00 14.25 ?  17  TYR   B O    1 
ATOM   4075 C CB   . TYR   B 1 17  ? 38.635 -26.063 -15.409 1.00 17.09 ?  17  TYR   B CB   1 
ATOM   4076 C CG   . TYR   B 1 17  ? 37.710 -25.290 -16.314 1.00 20.35 ?  17  TYR   B CG   1 
ATOM   4077 C CD1  . TYR   B 1 17  ? 37.131 -24.096 -15.900 1.00 21.72 ?  17  TYR   B CD1  1 
ATOM   4078 C CD2  . TYR   B 1 17  ? 37.420 -25.751 -17.589 1.00 22.62 ?  17  TYR   B CD2  1 
ATOM   4079 C CE1  . TYR   B 1 17  ? 36.281 -23.386 -16.731 1.00 23.54 ?  17  TYR   B CE1  1 
ATOM   4080 C CE2  . TYR   B 1 17  ? 36.578 -25.049 -18.428 1.00 24.17 ?  17  TYR   B CE2  1 
ATOM   4081 C CZ   . TYR   B 1 17  ? 36.009 -23.869 -17.994 1.00 24.65 ?  17  TYR   B CZ   1 
ATOM   4082 O OH   . TYR   B 1 17  ? 35.171 -23.169 -18.827 1.00 26.24 ?  17  TYR   B OH   1 
ATOM   4083 H H    . TYR   B 1 17  ? 37.376 -25.658 -13.090 1.00 17.17 ?  17  TYR   B H    1 
ATOM   4084 H HA   . TYR   B 1 17  ? 37.465 -27.696 -14.892 1.00 17.64 ?  17  TYR   B HA   1 
ATOM   4085 H HB2  . TYR   B 1 17  ? 39.174 -25.427 -14.916 1.00 20.51 ?  17  TYR   B HB2  1 
ATOM   4086 H HB3  . TYR   B 1 17  ? 39.201 -26.606 -15.974 1.00 20.51 ?  17  TYR   B HB3  1 
ATOM   4087 H HD1  . TYR   B 1 17  ? 37.314 -23.771 -15.049 1.00 26.07 ?  17  TYR   B HD1  1 
ATOM   4088 H HD2  . TYR   B 1 17  ? 37.796 -26.546 -17.886 1.00 27.15 ?  17  TYR   B HD2  1 
ATOM   4089 H HE1  . TYR   B 1 17  ? 35.899 -22.588 -16.442 1.00 28.25 ?  17  TYR   B HE1  1 
ATOM   4090 H HE2  . TYR   B 1 17  ? 36.387 -25.372 -19.281 1.00 29.00 ?  17  TYR   B HE2  1 
ATOM   4091 H HH   . TYR   B 1 17  ? 35.085 -23.565 -19.562 1.00 31.50 ?  17  TYR   B HH   1 
ATOM   4092 N N    . ILE   B 1 18  ? 39.593 -28.700 -13.929 1.00 13.82 ?  18  ILE   B N    1 
ATOM   4093 C CA   . ILE   B 1 18  ? 40.527 -29.419 -13.067 1.00 13.75 ?  18  ILE   B CA   1 
ATOM   4094 C C    . ILE   B 1 18  ? 41.691 -29.969 -13.883 1.00 14.51 ?  18  ILE   B C    1 
ATOM   4095 O O    . ILE   B 1 18  ? 41.531 -30.361 -15.044 1.00 16.07 ?  18  ILE   B O    1 
ATOM   4096 C CB   . ILE   B 1 18  ? 39.775 -30.519 -12.271 1.00 14.51 ?  18  ILE   B CB   1 
ATOM   4097 C CG1  . ILE   B 1 18  ? 40.636 -31.073 -11.132 1.00 14.80 ?  18  ILE   B CG1  1 
ATOM   4098 C CG2  . ILE   B 1 18  ? 39.270 -31.633 -13.202 1.00 15.07 ?  18  ILE   B CG2  1 
ATOM   4099 C CD1  . ILE   B 1 18  ? 39.825 -31.868 -10.104 1.00 16.22 ?  18  ILE   B CD1  1 
ATOM   4100 H H    . ILE   B 1 18  ? 39.487 -29.050 -14.706 1.00 16.59 ?  18  ILE   B H    1 
ATOM   4101 H HA   . ILE   B 1 18  ? 40.886 -28.801 -12.415 1.00 16.50 ?  18  ILE   B HA   1 
ATOM   4102 H HB   . ILE   B 1 18  ? 38.995 -30.113 -11.863 1.00 17.42 ?  18  ILE   B HB   1 
ATOM   4103 H HG12 . ILE   B 1 18  ? 41.310 -31.661 -11.497 1.00 17.76 ?  18  ILE   B HG12 1 
ATOM   4104 H HG13 . ILE   B 1 18  ? 41.055 -30.332 -10.665 1.00 17.76 ?  18  ILE   B HG13 1 
ATOM   4105 H HG21 . ILE   B 1 18  ? 38.690 -32.228 -12.699 1.00 18.09 ?  18  ILE   B HG21 1 
ATOM   4106 H HG22 . ILE   B 1 18  ? 38.775 -31.228 -13.930 1.00 18.09 ?  18  ILE   B HG22 1 
ATOM   4107 H HG23 . ILE   B 1 18  ? 40.028 -32.126 -13.548 1.00 18.09 ?  18  ILE   B HG23 1 
ATOM   4108 H HD11 . ILE   B 1 18  ? 40.417 -32.159 -9.390  1.00 19.47 ?  18  ILE   B HD11 1 
ATOM   4109 H HD12 . ILE   B 1 18  ? 39.127 -31.300 -9.739  1.00 19.47 ?  18  ILE   B HD12 1 
ATOM   4110 H HD13 . ILE   B 1 18  ? 39.431 -32.640 -10.539 1.00 19.47 ?  18  ILE   B HD13 1 
ATOM   4111 N N    . LYS   B 1 19  ? 42.872 -30.002 -13.259 1.00 14.87 ?  19  LYS   B N    1 
ATOM   4112 C CA   . LYS   B 1 19  ? 44.085 -30.478 -13.912 1.00 15.36 ?  19  LYS   B CA   1 
ATOM   4113 C C    . LYS   B 1 19  ? 44.977 -31.160 -12.886 1.00 15.50 ?  19  LYS   B C    1 
ATOM   4114 O O    . LYS   B 1 19  ? 45.054 -30.729 -11.734 1.00 15.25 ?  19  LYS   B O    1 
ATOM   4115 C CB   . LYS   B 1 19  ? 44.857 -29.313 -14.547 1.00 16.55 ?  19  LYS   B CB   1 
ATOM   4116 C CG   . LYS   B 1 19  ? 46.064 -29.720 -15.375 1.00 18.51 ?  19  LYS   B CG   1 
ATOM   4117 C CD   . LYS   B 1 19  ? 46.804 -28.492 -15.887 1.00 20.47 ?  19  LYS   B CD   1 
ATOM   4118 C CE   . LYS   B 1 19  ? 47.964 -28.873 -16.786 1.00 22.44 ?  19  LYS   B CE   1 
ATOM   4119 N NZ   . LYS   B 1 19  ? 48.744 -27.690 -17.232 1.00 23.70 ?  19  LYS   B NZ   1 
ATOM   4120 H H    . LYS   B 1 19  ? 42.986 -29.747 -12.441 1.00 17.85 ?  19  LYS   B H    1 
ATOM   4121 H HA   . LYS   B 1 19  ? 43.848 -31.114 -14.603 1.00 18.43 ?  19  LYS   B HA   1 
ATOM   4122 H HB2  . LYS   B 1 19  ? 44.251 -28.827 -15.129 1.00 19.86 ?  19  LYS   B HB2  1 
ATOM   4123 H HB3  . LYS   B 1 19  ? 45.164 -28.726 -13.836 1.00 19.86 ?  19  LYS   B HB3  1 
ATOM   4124 H HG2  . LYS   B 1 19  ? 46.668 -30.241 -14.826 1.00 22.22 ?  19  LYS   B HG2  1 
ATOM   4125 H HG3  . LYS   B 1 19  ? 45.763 -30.241 -16.137 1.00 22.22 ?  19  LYS   B HG3  1 
ATOM   4126 H HD2  . LYS   B 1 19  ? 46.190 -27.937 -16.395 1.00 24.57 ?  19  LYS   B HD2  1 
ATOM   4127 H HD3  . LYS   B 1 19  ? 47.154 -27.994 -15.129 1.00 24.57 ?  19  LYS   B HD3  1 
ATOM   4128 H HE2  . LYS   B 1 19  ? 48.558 -29.465 -16.299 1.00 26.93 ?  19  LYS   B HE2  1 
ATOM   4129 H HE3  . LYS   B 1 19  ? 47.616 -29.324 -17.573 1.00 26.93 ?  19  LYS   B HE3  1 
ATOM   4130 H HZ1  . LYS   B 1 19  ? 49.384 -27.944 -17.797 1.00 28.45 ?  19  LYS   B HZ1  1 
ATOM   4131 H HZ2  . LYS   B 1 19  ? 48.209 -27.110 -17.645 1.00 28.45 ?  19  LYS   B HZ2  1 
ATOM   4132 H HZ3  . LYS   B 1 19  ? 49.118 -27.290 -16.532 1.00 28.45 ?  19  LYS   B HZ3  1 
ATOM   4133 N N    . ASN   B 1 20  ? 45.662 -32.214 -13.318 1.00 16.46 ?  20  ASN   B N    1 
ATOM   4134 C CA   . ASN   B 1 20  ? 46.692 -32.847 -12.501 1.00 17.45 ?  20  ASN   B CA   1 
ATOM   4135 C C    . ASN   B 1 20  ? 47.960 -32.022 -12.691 1.00 17.74 ?  20  ASN   B C    1 
ATOM   4136 O O    . ASN   B 1 20  ? 48.600 -32.087 -13.746 1.00 19.70 ?  20  ASN   B O    1 
ATOM   4137 C CB   . ASN   B 1 20  ? 46.868 -34.298 -12.942 1.00 19.08 ?  20  ASN   B CB   1 
ATOM   4138 C CG   . ASN   B 1 20  ? 48.033 -34.997 -12.263 1.00 20.66 ?  20  ASN   B CG   1 
ATOM   4139 O OD1  . ASN   B 1 20  ? 48.704 -35.836 -12.877 1.00 23.05 ?  20  ASN   B OD1  1 
ATOM   4140 N ND2  . ASN   B 1 20  ? 48.269 -34.683 -10.998 1.00 20.24 ?  20  ASN   B ND2  1 
ATOM   4141 H H    . ASN   B 1 20  ? 45.548 -32.580 -14.088 1.00 19.76 ?  20  ASN   B H    1 
ATOM   4142 H HA   . ASN   B 1 20  ? 46.418 -32.828 -11.567 1.00 20.94 ?  20  ASN   B HA   1 
ATOM   4143 H HB2  . ASN   B 1 20  ? 46.060 -34.792 -12.729 1.00 22.90 ?  20  ASN   B HB2  1 
ATOM   4144 H HB3  . ASN   B 1 20  ? 47.021 -34.314 -13.898 1.00 22.90 ?  20  ASN   B HB3  1 
ATOM   4145 H HD21 . ASN   B 1 20  ? 48.923 -35.048 -10.581 1.00 24.29 ?  20  ASN   B HD21 1 
ATOM   4146 H HD22 . ASN   B 1 20  ? 47.778 -34.098 -10.595 1.00 24.29 ?  20  ASN   B HD22 1 
ATOM   4147 N N    . ALA   B 1 21  ? 48.313 -31.219 -11.683 1.00 17.52 ?  21  ALA   B N    1 
ATOM   4148 C CA   . ALA   B 1 21  ? 49.419 -30.288 -11.836 1.00 18.63 ?  21  ALA   B CA   1 
ATOM   4149 C C    . ALA   B 1 21  ? 49.881 -29.793 -10.475 1.00 17.29 ?  21  ALA   B C    1 
ATOM   4150 O O    . ALA   B 1 21  ? 49.138 -29.823 -9.490  1.00 17.11 ?  21  ALA   B O    1 
ATOM   4151 C CB   . ALA   B 1 21  ? 49.021 -29.107 -12.722 1.00 20.18 ?  21  ALA   B CB   1 
ATOM   4152 H H    . ALA   B 1 21  ? 47.925 -31.200 -10.907 1.00 21.03 ?  21  ALA   B H    1 
ATOM   4153 H HA   . ALA   B 1 21  ? 50.158 -30.752 -12.255 1.00 22.36 ?  21  ALA   B HA   1 
ATOM   4154 H HB1  . ALA   B 1 21  ? 49.801 -28.555 -12.860 1.00 24.22 ?  21  ALA   B HB1  1 
ATOM   4155 H HB2  . ALA   B 1 21  ? 48.699 -29.452 -13.568 1.00 24.22 ?  21  ALA   B HB2  1 
ATOM   4156 H HB3  . ALA   B 1 21  ? 48.321 -28.604 -12.278 1.00 24.22 ?  21  ALA   B HB3  1 
ATOM   4157 N N    . ASP   B 1 22  ? 51.138 -29.345 -10.453 1.00 16.65 ?  22  ASP   B N    1 
ATOM   4158 C CA   . ASP   B 1 22  ? 51.747 -28.649 -9.325  1.00 15.80 ?  22  ASP   B CA   1 
ATOM   4159 C C    . ASP   B 1 22  ? 51.337 -27.179 -9.406  1.00 14.57 ?  22  ASP   B C    1 
ATOM   4160 O O    . ASP   B 1 22  ? 51.642 -26.506 -10.394 1.00 14.94 ?  22  ASP   B O    1 
ATOM   4161 C CB   . ASP   B 1 22  ? 53.264 -28.821 -9.475  1.00 17.28 ?  22  ASP   B CB   1 
ATOM   4162 C CG   . ASP   B 1 22  ? 54.086 -28.064 -8.443  1.00 19.18 ?  22  ASP   B CG   1 
ATOM   4163 O OD1  . ASP   B 1 22  ? 53.711 -26.954 -8.034  1.00 19.21 ?  22  ASP   B OD1  1 
ATOM   4164 O OD2  . ASP   B 1 22  ? 55.165 -28.574 -8.070  1.00 21.62 -1 22  ASP   B OD2  1 
ATOM   4165 H H    . ASP   B 1 22  ? 51.682 -29.442 -11.116 1.00 19.99 ?  22  ASP   B H    1 
ATOM   4166 H HA   . ASP   B 1 22  ? 51.453 -29.034 -8.482  1.00 18.97 ?  22  ASP   B HA   1 
ATOM   4167 H HB2  . ASP   B 1 22  ? 53.488 -29.757 -9.394  1.00 20.74 ?  22  ASP   B HB2  1 
ATOM   4168 H HB3  . ASP   B 1 22  ? 53.532 -28.486 -10.344 1.00 20.74 ?  22  ASP   B HB3  1 
ATOM   4169 N N    . ILE   B 1 23  ? 50.629 -26.685 -8.382  1.00 13.87 ?  23  ILE   B N    1 
ATOM   4170 C CA   . ILE   B 1 23  ? 50.032 -25.350 -8.449  1.00 13.09 ?  23  ILE   B CA   1 
ATOM   4171 C C    . ILE   B 1 23  ? 51.086 -24.258 -8.585  1.00 12.81 ?  23  ILE   B C    1 
ATOM   4172 O O    . ILE   B 1 23  ? 50.818 -23.216 -9.193  1.00 12.42 ?  23  ILE   B O    1 
ATOM   4173 C CB   . ILE   B 1 23  ? 49.089 -25.109 -7.253  1.00 13.67 ?  23  ILE   B CB   1 
ATOM   4174 C CG1  . ILE   B 1 23  ? 48.252 -23.846 -7.464  1.00 14.29 ?  23  ILE   B CG1  1 
ATOM   4175 C CG2  . ILE   B 1 23  ? 49.857 -25.068 -5.947  1.00 14.57 ?  23  ILE   B CG2  1 
ATOM   4176 C CD1  . ILE   B 1 23  ? 47.140 -23.660 -6.433  1.00 14.76 ?  23  ILE   B CD1  1 
ATOM   4177 H H    . ILE   B 1 23  ? 50.485 -27.104 -7.646  1.00 16.65 ?  23  ILE   B H    1 
ATOM   4178 H HA   . ILE   B 1 23  ? 49.489 -25.311 -9.250  1.00 15.71 ?  23  ILE   B HA   1 
ATOM   4179 H HB   . ILE   B 1 23  ? 48.474 -25.859 -7.214  1.00 16.41 ?  23  ILE   B HB   1 
ATOM   4180 H HG12 . ILE   B 1 23  ? 48.838 -23.072 -7.413  1.00 17.15 ?  23  ILE   B HG12 1 
ATOM   4181 H HG13 . ILE   B 1 23  ? 47.841 -23.883 -8.345  1.00 17.15 ?  23  ILE   B HG13 1 
ATOM   4182 H HG21 . ILE   B 1 23  ? 49.226 -25.069 -5.213  1.00 17.49 ?  23  ILE   B HG21 1 
ATOM   4183 H HG22 . ILE   B 1 23  ? 50.428 -25.849 -5.896  1.00 17.49 ?  23  ILE   B HG22 1 
ATOM   4184 H HG23 . ILE   B 1 23  ? 50.394 -24.262 -5.924  1.00 17.49 ?  23  ILE   B HG23 1 
ATOM   4185 H HD11 . ILE   B 1 23  ? 46.614 -22.885 -6.676  1.00 17.72 ?  23  ILE   B HD11 1 
ATOM   4186 H HD12 . ILE   B 1 23  ? 46.583 -24.454 -6.432  1.00 17.72 ?  23  ILE   B HD12 1 
ATOM   4187 H HD13 . ILE   B 1 23  ? 47.540 -23.534 -5.561  1.00 17.72 ?  23  ILE   B HD13 1 
ATOM   4188 N N    . VAL   B 1 24  ? 52.282 -24.462 -8.023  1.00 13.35 ?  24  VAL   B N    1 
ATOM   4189 C CA   . VAL   B 1 24  ? 53.362 -23.488 -8.189  1.00 14.19 ?  24  VAL   B CA   1 
ATOM   4190 C C    . VAL   B 1 24  ? 53.814 -23.438 -9.642  1.00 14.05 ?  24  VAL   B C    1 
ATOM   4191 O O    . VAL   B 1 24  ? 53.956 -22.358 -10.232 1.00 14.34 ?  24  VAL   B O    1 
ATOM   4192 C CB   . VAL   B 1 24  ? 54.538 -23.808 -7.244  1.00 15.04 ?  24  VAL   B CB   1 
ATOM   4193 C CG1  . VAL   B 1 24  ? 55.750 -22.925 -7.563  1.00 15.76 ?  24  VAL   B CG1  1 
ATOM   4194 C CG2  . VAL   B 1 24  ? 54.124 -23.632 -5.800  1.00 16.02 ?  24  VAL   B CG2  1 
ATOM   4195 H H    . VAL   B 1 24  ? 52.493 -25.150 -7.549  1.00 16.02 ?  24  VAL   B H    1 
ATOM   4196 H HA   . VAL   B 1 24  ? 53.032 -22.613 -7.952  1.00 17.03 ?  24  VAL   B HA   1 
ATOM   4197 H HB   . VAL   B 1 24  ? 54.805 -24.736 -7.362  1.00 18.05 ?  24  VAL   B HB   1 
ATOM   4198 H HG11 . VAL   B 1 24  ? 56.355 -22.933 -6.803  1.00 18.91 ?  24  VAL   B HG11 1 
ATOM   4199 H HG12 . VAL   B 1 24  ? 56.201 -23.278 -8.344  1.00 18.91 ?  24  VAL   B HG12 1 
ATOM   4200 H HG13 . VAL   B 1 24  ? 55.443 -22.021 -7.730  1.00 18.91 ?  24  VAL   B HG13 1 
ATOM   4201 H HG21 . VAL   B 1 24  ? 54.851 -23.916 -5.223  1.00 19.22 ?  24  VAL   B HG21 1 
ATOM   4202 H HG22 . VAL   B 1 24  ? 53.924 -22.697 -5.643  1.00 19.22 ?  24  VAL   B HG22 1 
ATOM   4203 H HG23 . VAL   B 1 24  ? 53.337 -24.174 -5.628  1.00 19.22 ?  24  VAL   B HG23 1 
ATOM   4204 N N    . GLU   B 1 25  ? 54.075 -24.606 -10.235 1.00 15.07 ?  25  GLU   B N    1 
ATOM   4205 C CA   . GLU   B 1 25  ? 54.471 -24.632 -11.637 1.00 16.28 ?  25  GLU   B CA   1 
ATOM   4206 C C    . GLU   B 1 25  ? 53.364 -24.085 -12.525 1.00 15.03 ?  25  GLU   B C    1 
ATOM   4207 O O    . GLU   B 1 25  ? 53.630 -23.366 -13.496 1.00 15.98 ?  25  GLU   B O    1 
ATOM   4208 C CB   . GLU   B 1 25  ? 54.869 -26.049 -12.044 1.00 20.09 ?  25  GLU   B CB   1 
ATOM   4209 C CG   . GLU   B 1 25  ? 56.177 -26.491 -11.403 1.00 25.97 ?  25  GLU   B CG   1 
ATOM   4210 C CD   . GLU   B 1 25  ? 57.286 -25.448 -11.518 1.00 31.47 ?  25  GLU   B CD   1 
ATOM   4211 O OE1  . GLU   B 1 25  ? 57.646 -25.079 -12.657 1.00 33.53 ?  25  GLU   B OE1  1 
ATOM   4212 O OE2  . GLU   B 1 25  ? 57.785 -24.977 -10.468 1.00 33.34 -1 25  GLU   B OE2  1 
ATOM   4213 H H    . GLU   B 1 25  ? 54.024 -25.378 -9.856  1.00 18.09 ?  25  GLU   B H    1 
ATOM   4214 H HA   . GLU   B 1 25  ? 55.226 -24.044 -11.756 1.00 19.54 ?  25  GLU   B HA   1 
ATOM   4215 H HB2  . GLU   B 1 25  ? 54.173 -26.669 -11.765 1.00 24.11 ?  25  GLU   B HB2  1 
ATOM   4216 H HB3  . GLU   B 1 25  ? 54.975 -26.085 -13.008 1.00 24.11 ?  25  GLU   B HB3  1 
ATOM   4217 H HG2  . GLU   B 1 25  ? 56.026 -26.651 -10.463 1.00 31.17 ?  25  GLU   B HG2  1 
ATOM   4218 H HG3  . GLU   B 1 25  ? 56.482 -27.298 -11.842 1.00 31.17 ?  25  GLU   B HG3  1 
ATOM   4219 N N    . GLU   B 1 26  ? 52.111 -24.406 -12.198 1.00 14.25 ?  26  GLU   B N    1 
ATOM   4220 C CA   . GLU   B 1 26  ? 50.984 -23.871 -12.955 1.00 15.04 ?  26  GLU   B CA   1 
ATOM   4221 C C    . GLU   B 1 26  ? 50.939 -22.355 -12.871 1.00 14.26 ?  26  GLU   B C    1 
ATOM   4222 O O    . GLU   B 1 26  ? 50.738 -21.678 -13.882 1.00 15.56 ?  26  GLU   B O    1 
ATOM   4223 C CB   . GLU   B 1 26  ? 49.669 -24.450 -12.434 1.00 16.97 ?  26  GLU   B CB   1 
ATOM   4224 C CG   . GLU   B 1 26  ? 49.231 -25.737 -13.101 1.00 20.63 ?  26  GLU   B CG   1 
ATOM   4225 C CD   . GLU   B 1 26  ? 49.002 -25.604 -14.602 1.00 22.24 ?  26  GLU   B CD   1 
ATOM   4226 O OE1  . GLU   B 1 26  ? 48.039 -24.936 -15.041 1.00 22.80 ?  26  GLU   B OE1  1 
ATOM   4227 O OE2  . GLU   B 1 26  ? 49.791 -26.201 -15.344 1.00 24.25 -1 26  GLU   B OE2  1 
ATOM   4228 H H    . GLU   B 1 26  ? 51.886 -24.938 -11.554 1.00 17.11 ?  26  GLU   B H    1 
ATOM   4229 H HA   . GLU   B 1 26  ? 51.077 -24.116 -13.885 1.00 18.05 ?  26  GLU   B HA   1 
ATOM   4230 H HB2  . GLU   B 1 26  ? 49.760 -24.633 -11.484 1.00 20.36 ?  26  GLU   B HB2  1 
ATOM   4231 H HB3  . GLU   B 1 26  ? 48.963 -23.796 -12.569 1.00 20.36 ?  26  GLU   B HB3  1 
ATOM   4232 H HG2  . GLU   B 1 26  ? 49.926 -26.393 -12.979 1.00 24.76 ?  26  GLU   B HG2  1 
ATOM   4233 H HG3  . GLU   B 1 26  ? 48.404 -26.036 -12.693 1.00 24.76 ?  26  GLU   B HG3  1 
ATOM   4234 N N    . ALA   B 1 27  ? 51.084 -21.807 -11.662 1.00 13.31 ?  27  ALA   B N    1 
ATOM   4235 C CA   . ALA   B 1 27  ? 51.048 -20.356 -11.511 1.00 13.52 ?  27  ALA   B CA   1 
ATOM   4236 C C    . ALA   B 1 27  ? 52.119 -19.692 -12.369 1.00 14.74 ?  27  ALA   B C    1 
ATOM   4237 O O    . ALA   B 1 27  ? 51.855 -18.691 -13.053 1.00 15.66 ?  27  ALA   B O    1 
ATOM   4238 C CB   . ALA   B 1 27  ? 51.199 -19.975 -10.038 1.00 13.86 ?  27  ALA   B CB   1 
ATOM   4239 H H    . ALA   B 1 27  ? 51.195 -22.246 -10.926 1.00 15.98 ?  27  ALA   B H    1 
ATOM   4240 H HA   . ALA   B 1 27  ? 50.188 -20.032 -11.809 1.00 16.23 ?  27  ALA   B HA   1 
ATOM   4241 H HB1  . ALA   B 1 27  ? 51.165 -19.007 -9.956  1.00 16.64 ?  27  ALA   B HB1  1 
ATOM   4242 H HB2  . ALA   B 1 27  ? 50.467 -20.370 -9.532  1.00 16.64 ?  27  ALA   B HB2  1 
ATOM   4243 H HB3  . ALA   B 1 27  ? 52.045 -20.306 -9.705  1.00 16.64 ?  27  ALA   B HB3  1 
ATOM   4244 N N    . LYS   B 1 28  ? 53.336 -20.239 -12.357 1.00 16.31 ?  28  LYS   B N    1 
ATOM   4245 C CA   . LYS   B 1 28  ? 54.409 -19.620 -13.126 1.00 18.22 ?  28  LYS   B CA   1 
ATOM   4246 C C    . LYS   B 1 28  ? 54.156 -19.706 -14.624 1.00 18.96 ?  28  LYS   B C    1 
ATOM   4247 O O    . LYS   B 1 28  ? 54.571 -18.811 -15.370 1.00 20.22 ?  28  LYS   B O    1 
ATOM   4248 C CB   . LYS   B 1 28  ? 55.768 -20.213 -12.740 1.00 21.49 ?  28  LYS   B CB   1 
ATOM   4249 C CG   . LYS   B 1 28  ? 56.166 -19.887 -11.306 1.00 25.02 ?  28  LYS   B CG   1 
ATOM   4250 C CD   . LYS   B 1 28  ? 57.592 -20.298 -10.968 1.00 29.95 ?  28  LYS   B CD   1 
ATOM   4251 C CE   . LYS   B 1 28  ? 57.706 -21.782 -10.711 1.00 33.68 ?  28  LYS   B CE   1 
ATOM   4252 N NZ   . LYS   B 1 28  ? 59.058 -22.141 -10.196 1.00 35.49 ?  28  LYS   B NZ   1 
ATOM   4253 H H    . LYS   B 1 28  ? 53.562 -20.946 -11.923 1.00 19.58 ?  28  LYS   B H    1 
ATOM   4254 H HA   . LYS   B 1 28  ? 54.436 -18.677 -12.907 1.00 21.87 ?  28  LYS   B HA   1 
ATOM   4255 H HB2  . LYS   B 1 28  ? 55.734 -21.175 -12.829 1.00 25.79 ?  28  LYS   B HB2  1 
ATOM   4256 H HB3  . LYS   B 1 28  ? 56.451 -19.847 -13.328 1.00 25.79 ?  28  LYS   B HB3  1 
ATOM   4257 H HG2  . LYS   B 1 28  ? 56.087 -18.928 -11.171 1.00 30.03 ?  28  LYS   B HG2  1 
ATOM   4258 H HG3  . LYS   B 1 28  ? 55.566 -20.353 -10.704 1.00 30.03 ?  28  LYS   B HG3  1 
ATOM   4259 H HD2  . LYS   B 1 28  ? 58.170 -20.071 -11.713 1.00 35.95 ?  28  LYS   B HD2  1 
ATOM   4260 H HD3  . LYS   B 1 28  ? 57.874 -19.826 -10.169 1.00 35.95 ?  28  LYS   B HD3  1 
ATOM   4261 H HE2  . LYS   B 1 28  ? 57.048 -22.045 -10.047 1.00 40.42 ?  28  LYS   B HE2  1 
ATOM   4262 H HE3  . LYS   B 1 28  ? 57.557 -22.265 -11.539 1.00 40.42 ?  28  LYS   B HE3  1 
ATOM   4263 H HZ1  . LYS   B 1 28  ? 59.107 -23.017 -10.049 1.00 42.59 ?  28  LYS   B HZ1  1 
ATOM   4264 H HZ2  . LYS   B 1 28  ? 59.680 -21.911 -10.789 1.00 42.59 ?  28  LYS   B HZ2  1 
ATOM   4265 H HZ3  . LYS   B 1 28  ? 59.217 -21.711 -9.432  1.00 42.59 ?  28  LYS   B HZ3  1 
ATOM   4266 N N    . LYS   B 1 29  ? 53.450 -20.740 -15.081 1.00 20.05 ?  29  LYS   B N    1 
ATOM   4267 C CA   . LYS   B 1 29  ? 53.173 -20.887 -16.504 1.00 22.60 ?  29  LYS   B CA   1 
ATOM   4268 C C    . LYS   B 1 29  ? 51.926 -20.126 -16.945 1.00 21.68 ?  29  LYS   B C    1 
ATOM   4269 O O    . LYS   B 1 29  ? 51.930 -19.504 -18.013 1.00 22.94 ?  29  LYS   B O    1 
ATOM   4270 C CB   . LYS   B 1 29  ? 53.037 -22.370 -16.861 1.00 27.12 ?  29  LYS   B CB   1 
ATOM   4271 C CG   . LYS   B 1 29  ? 52.911 -22.640 -18.349 1.00 31.39 ?  29  LYS   B CG   1 
ATOM   4272 C CD   . LYS   B 1 29  ? 53.162 -24.107 -18.669 1.00 34.77 ?  29  LYS   B CD   1 
ATOM   4273 C CE   . LYS   B 1 29  ? 52.052 -25.002 -18.141 1.00 37.12 ?  29  LYS   B CE   1 
ATOM   4274 N NZ   . LYS   B 1 29  ? 52.311 -26.441 -18.437 1.00 38.34 ?  29  LYS   B NZ   1 
ATOM   4275 H H    . LYS   B 1 29  ? 53.115 -21.366 -14.583 1.00 24.06 ?  29  LYS   B H    1 
ATOM   4276 H HA   . LYS   B 1 29  ? 53.920 -20.532 -17.000 1.00 27.13 ?  29  LYS   B HA   1 
ATOM   4277 H HB2  . LYS   B 1 29  ? 53.829 -22.837 -16.546 1.00 32.55 ?  29  LYS   B HB2  1 
ATOM   4278 H HB3  . LYS   B 1 29  ? 52.250 -22.728 -16.429 1.00 32.55 ?  29  LYS   B HB3  1 
ATOM   4279 H HG2  . LYS   B 1 29  ? 52.013 -22.414 -18.639 1.00 37.67 ?  29  LYS   B HG2  1 
ATOM   4280 H HG3  . LYS   B 1 29  ? 53.564 -22.106 -18.830 1.00 37.67 ?  29  LYS   B HG3  1 
ATOM   4281 H HD2  . LYS   B 1 29  ? 53.212 -24.220 -19.630 1.00 41.72 ?  29  LYS   B HD2  1 
ATOM   4282 H HD3  . LYS   B 1 29  ? 53.996 -24.385 -18.256 1.00 41.72 ?  29  LYS   B HD3  1 
ATOM   4283 H HE2  . LYS   B 1 29  ? 51.986 -24.900 -17.179 1.00 44.55 ?  29  LYS   B HE2  1 
ATOM   4284 H HE3  . LYS   B 1 29  ? 51.214 -24.752 -18.562 1.00 44.55 ?  29  LYS   B HE3  1 
ATOM   4285 H HZ1  . LYS   B 1 29  ? 51.647 -26.942 -18.120 1.00 46.01 ?  29  LYS   B HZ1  1 
ATOM   4286 H HZ2  . LYS   B 1 29  ? 52.370 -26.564 -19.317 1.00 46.01 ?  29  LYS   B HZ2  1 
ATOM   4287 H HZ3  . LYS   B 1 29  ? 53.074 -26.697 -18.058 1.00 46.01 ?  29  LYS   B HZ3  1 
ATOM   4288 N N    . VAL   B 1 30  ? 50.859 -20.175 -16.141 1.00 19.98 ?  30  VAL   B N    1 
ATOM   4289 C CA   . VAL   B 1 30  ? 49.570 -19.582 -16.506 1.00 20.18 ?  30  VAL   B CA   1 
ATOM   4290 C C    . VAL   B 1 30  ? 49.569 -18.067 -16.350 1.00 19.27 ?  30  VAL   B C    1 
ATOM   4291 O O    . VAL   B 1 30  ? 48.827 -17.359 -17.050 1.00 20.65 ?  30  VAL   B O    1 
ATOM   4292 C CB   . VAL   B 1 30  ? 48.466 -20.210 -15.630 1.00 21.13 ?  30  VAL   B CB   1 
ATOM   4293 C CG1  . VAL   B 1 30  ? 47.175 -19.404 -15.708 1.00 21.32 ?  30  VAL   B CG1  1 
ATOM   4294 C CG2  . VAL   B 1 30  ? 48.226 -21.664 -16.022 1.00 22.07 ?  30  VAL   B CG2  1 
ATOM   4295 H H    . VAL   B 1 30  ? 50.844 -20.579 -15.370 1.00 23.98 ?  30  VAL   B H    1 
ATOM   4296 H HA   . VAL   B 1 30  ? 49.368 -19.806 -17.427 1.00 24.22 ?  30  VAL   B HA   1 
ATOM   4297 H HB   . VAL   B 1 30  ? 48.755 -20.209 -14.703 1.00 25.36 ?  30  VAL   B HB   1 
ATOM   4298 H HG11 . VAL   B 1 30  ? 46.432 -19.988 -15.479 1.00 25.58 ?  30  VAL   B HG11 1 
ATOM   4299 H HG12 . VAL   B 1 30  ? 47.217 -18.671 -15.077 1.00 25.58 ?  30  VAL   B HG12 1 
ATOM   4300 H HG13 . VAL   B 1 30  ? 47.058 -19.077 -16.608 1.00 25.58 ?  30  VAL   B HG13 1 
ATOM   4301 H HG21 . VAL   B 1 30  ? 47.535 -22.042 -15.448 1.00 26.49 ?  30  VAL   B HG21 1 
ATOM   4302 H HG22 . VAL   B 1 30  ? 47.932 -21.698 -16.948 1.00 26.49 ?  30  VAL   B HG22 1 
ATOM   4303 H HG23 . VAL   B 1 30  ? 49.048 -22.163 -15.916 1.00 26.49 ?  30  VAL   B HG23 1 
ATOM   4304 N N    . LYS   B 1 31  ? 50.347 -17.560 -15.408 1.00 18.81 ?  31  LYS   B N    1 
ATOM   4305 C CA   . LYS   B 1 31  ? 50.369 -16.149 -15.049 1.00 19.58 ?  31  LYS   B CA   1 
ATOM   4306 C C    . LYS   B 1 31  ? 48.966 -15.678 -14.664 1.00 17.24 ?  31  LYS   B C    1 
ATOM   4307 O O    . LYS   B 1 31  ? 48.426 -14.751 -15.284 1.00 18.22 ?  31  LYS   B O    1 
ATOM   4308 C CB   . LYS   B 1 31  ? 51.001 -15.333 -16.182 1.00 23.02 ?  31  LYS   B CB   1 
ATOM   4309 C CG   . LYS   B 1 31  ? 52.425 -15.795 -16.516 1.00 26.80 ?  31  LYS   B CG   1 
ATOM   4310 C CD   . LYS   B 1 31  ? 53.002 -15.058 -17.706 1.00 30.80 ?  31  LYS   B CD   1 
ATOM   4311 C CE   . LYS   B 1 31  ? 54.478 -15.360 -17.864 1.00 33.79 ?  31  LYS   B CE   1 
ATOM   4312 N NZ   . LYS   B 1 31  ? 55.247 -14.956 -16.654 1.00 35.16 ?  31  LYS   B NZ   1 
ATOM   4313 H H    . LYS   B 1 31  ? 50.896 -18.040 -14.955 1.00 22.58 ?  31  LYS   B H    1 
ATOM   4314 H HA   . LYS   B 1 31  ? 50.927 -16.057 -14.272 1.00 23.50 ?  31  LYS   B HA   1 
ATOM   4315 H HB2  . LYS   B 1 31  ? 50.462 -15.423 -16.983 1.00 27.63 ?  31  LYS   B HB2  1 
ATOM   4316 H HB3  . LYS   B 1 31  ? 51.044 -14.406 -15.908 1.00 27.63 ?  31  LYS   B HB3  1 
ATOM   4317 H HG2  . LYS   B 1 31  ? 52.993 -15.635 -15.748 1.00 32.16 ?  31  LYS   B HG2  1 
ATOM   4318 H HG3  . LYS   B 1 31  ? 52.412 -16.743 -16.727 1.00 32.16 ?  31  LYS   B HG3  1 
ATOM   4319 H HD2  . LYS   B 1 31  ? 52.540 -15.343 -18.510 1.00 36.97 ?  31  LYS   B HD2  1 
ATOM   4320 H HD3  . LYS   B 1 31  ? 52.893 -14.106 -17.571 1.00 36.97 ?  31  LYS   B HD3  1 
ATOM   4321 H HE2  . LYS   B 1 31  ? 54.599 -16.314 -17.997 1.00 40.56 ?  31  LYS   B HE2  1 
ATOM   4322 H HE3  . LYS   B 1 31  ? 54.825 -14.868 -18.624 1.00 40.56 ?  31  LYS   B HE3  1 
ATOM   4323 H HZ1  . LYS   B 1 31  ? 56.120 -15.002 -16.818 1.00 42.19 ?  31  LYS   B HZ1  1 
ATOM   4324 H HZ2  . LYS   B 1 31  ? 55.039 -14.121 -16.427 1.00 42.19 ?  31  LYS   B HZ2  1 
ATOM   4325 H HZ3  . LYS   B 1 31  ? 55.053 -15.496 -15.973 1.00 42.19 ?  31  LYS   B HZ3  1 
ATOM   4326 N N    . PRO   B 1 32  ? 48.354 -16.279 -13.639 1.00 14.69 ?  32  PRO   B N    1 
ATOM   4327 C CA   . PRO   B 1 32  ? 46.975 -15.923 -13.283 1.00 13.75 ?  32  PRO   B CA   1 
ATOM   4328 C C    . PRO   B 1 32  ? 46.890 -14.578 -12.578 1.00 13.68 ?  32  PRO   B C    1 
ATOM   4329 O O    . PRO   B 1 32  ? 47.811 -14.150 -11.877 1.00 15.10 ?  32  PRO   B O    1 
ATOM   4330 C CB   . PRO   B 1 32  ? 46.576 -17.047 -12.320 1.00 14.07 ?  32  PRO   B CB   1 
ATOM   4331 C CG   . PRO   B 1 32  ? 47.876 -17.405 -11.650 1.00 14.12 ?  32  PRO   B CG   1 
ATOM   4332 C CD   . PRO   B 1 32  ? 48.933 -17.263 -12.702 1.00 14.57 ?  32  PRO   B CD   1 
ATOM   4333 H HA   . PRO   B 1 32  ? 46.399 -15.933 -14.066 1.00 16.51 ?  32  PRO   B HA   1 
ATOM   4334 H HB2  . PRO   B 1 32  ? 45.929 -16.716 -11.675 1.00 16.89 ?  32  PRO   B HB2  1 
ATOM   4335 H HB3  . PRO   B 1 32  ? 46.218 -17.800 -12.816 1.00 16.89 ?  32  PRO   B HB3  1 
ATOM   4336 H HG2  . PRO   B 1 32  ? 48.047 -16.795 -10.912 1.00 16.95 ?  32  PRO   B HG2  1 
ATOM   4337 H HG3  . PRO   B 1 32  ? 47.842 -18.321 -11.329 1.00 16.95 ?  32  PRO   B HG3  1 
ATOM   4338 H HD2  . PRO   B 1 32  ? 49.752 -16.915 -12.313 1.00 17.49 ?  32  PRO   B HD2  1 
ATOM   4339 H HD3  . PRO   B 1 32  ? 49.080 -18.107 -13.148 1.00 17.49 ?  32  PRO   B HD3  1 
ATOM   4340 N N    . THR   B 1 33  ? 45.735 -13.926 -12.747 1.00 13.41 ?  33  THR   B N    1 
ATOM   4341 C CA   . THR   B 1 33  ? 45.438 -12.750 -11.939 1.00 13.67 ?  33  THR   B CA   1 
ATOM   4342 C C    . THR   B 1 33  ? 45.389 -13.104 -10.458 1.00 13.33 ?  33  THR   B C    1 
ATOM   4343 O O    . THR   B 1 33  ? 45.865 -12.329 -9.615  1.00 14.29 ?  33  THR   B O    1 
ATOM   4344 C CB   . THR   B 1 33  ? 44.121 -12.112 -12.392 1.00 14.31 ?  33  THR   B CB   1 
ATOM   4345 O OG1  . THR   B 1 33  ? 44.166 -11.855 -13.798 1.00 14.47 ?  33  THR   B OG1  1 
ATOM   4346 C CG2  . THR   B 1 33  ? 43.860 -10.811 -11.644 1.00 15.49 ?  33  THR   B CG2  1 
ATOM   4347 H H    . THR   B 1 33  ? 45.117 -14.143 -13.308 1.00 16.10 ?  33  THR   B H    1 
ATOM   4348 H HA   . THR   B 1 33  ? 46.140 -12.096 -12.064 1.00 16.41 ?  33  THR   B HA   1 
ATOM   4349 H HB   . THR   B 1 33  ? 43.385 -12.722 -12.205 1.00 17.17 ?  33  THR   B HB   1 
ATOM   4350 H HG1  . THR   B 1 33  ? 43.446 -11.490 -14.049 1.00 17.37 ?  33  THR   B HG1  1 
ATOM   4351 H HG21 . THR   B 1 33  ? 43.101 -10.352 -12.032 1.00 18.60 ?  33  THR   B HG21 1 
ATOM   4352 H HG22 . THR   B 1 33  ? 43.673 -10.996 -10.709 1.00 18.60 ?  33  THR   B HG22 1 
ATOM   4353 H HG23 . THR   B 1 33  ? 44.640 -10.237 -11.702 1.00 18.60 ?  33  THR   B HG23 1 
ATOM   4354 N N    . VAL   B 1 34  ? 44.837 -14.272 -10.118 1.00 12.17 ?  34  VAL   B N    1 
ATOM   4355 C CA   . VAL   B 1 34  ? 44.652 -14.670 -8.726  1.00 11.87 ?  34  VAL   B CA   1 
ATOM   4356 C C    . VAL   B 1 34  ? 45.084 -16.118 -8.561  1.00 11.16 ?  34  VAL   B C    1 
ATOM   4357 O O    . VAL   B 1 34  ? 44.562 -17.008 -9.246  1.00 11.81 ?  34  VAL   B O    1 
ATOM   4358 C CB   . VAL   B 1 34  ? 43.182 -14.530 -8.274  1.00 13.01 ?  34  VAL   B CB   1 
ATOM   4359 C CG1  . VAL   B 1 34  ? 43.022 -14.986 -6.827  1.00 13.79 ?  34  VAL   B CG1  1 
ATOM   4360 C CG2  . VAL   B 1 34  ? 42.678 -13.102 -8.464  1.00 14.03 ?  34  VAL   B CG2  1 
ATOM   4361 H H    . VAL   B 1 34  ? 44.571 -14.862 -10.683 1.00 14.61 ?  34  VAL   B H    1 
ATOM   4362 H HA   . VAL   B 1 34  ? 45.207 -14.116 -8.149  1.00 14.25 ?  34  VAL   B HA   1 
ATOM   4363 H HB   . VAL   B 1 34  ? 42.636 -15.106 -8.826  1.00 15.61 ?  34  VAL   B HB   1 
ATOM   4364 H HG11 . VAL   B 1 34  ? 42.165 -14.673 -6.490  1.00 16.55 ?  34  VAL   B HG11 1 
ATOM   4365 H HG12 . VAL   B 1 34  ? 43.052 -15.955 -6.791  1.00 16.55 ?  34  VAL   B HG12 1 
ATOM   4366 H HG13 . VAL   B 1 34  ? 43.739 -14.611 -6.291  1.00 16.55 ?  34  VAL   B HG13 1 
ATOM   4367 H HG21 . VAL   B 1 34  ? 41.761 -13.045 -8.148  1.00 16.85 ?  34  VAL   B HG21 1 
ATOM   4368 H HG22 . VAL   B 1 34  ? 43.240 -12.494 -7.960  1.00 16.85 ?  34  VAL   B HG22 1 
ATOM   4369 H HG23 . VAL   B 1 34  ? 42.713 -12.876 -9.409  1.00 16.85 ?  34  VAL   B HG23 1 
ATOM   4370 N N    . VAL   B 1 35  ? 45.994 -16.367 -7.622  1.00 10.80 ?  35  VAL   B N    1 
ATOM   4371 C CA   . VAL   B 1 35  ? 46.229 -17.712 -7.107  1.00 10.62 ?  35  VAL   B CA   1 
ATOM   4372 C C    . VAL   B 1 35  ? 45.689 -17.774 -5.685  1.00 10.27 ?  35  VAL   B C    1 
ATOM   4373 O O    . VAL   B 1 35  ? 45.902 -16.850 -4.895  1.00 10.65 ?  35  VAL   B O    1 
ATOM   4374 C CB   . VAL   B 1 35  ? 47.713 -18.130 -7.191  1.00 11.19 ?  35  VAL   B CB   1 
ATOM   4375 C CG1  . VAL   B 1 35  ? 48.615 -17.290 -6.275  1.00 11.94 ?  35  VAL   B CG1  1 
ATOM   4376 C CG2  . VAL   B 1 35  ? 47.850 -19.632 -6.882  1.00 11.84 ?  35  VAL   B CG2  1 
ATOM   4377 H H    . VAL   B 1 35  ? 46.499 -15.767 -7.268  1.00 12.97 ?  35  VAL   B H    1 
ATOM   4378 H HA   . VAL   B 1 35  ? 45.714 -18.342 -7.635  1.00 12.74 ?  35  VAL   B HA   1 
ATOM   4379 H HB   . VAL   B 1 35  ? 48.012 -17.998 -8.104  1.00 13.43 ?  35  VAL   B HB   1 
ATOM   4380 H HG11 . VAL   B 1 35  ? 49.537 -17.523 -6.449  1.00 14.33 ?  35  VAL   B HG11 1 
ATOM   4381 H HG12 . VAL   B 1 35  ? 48.462 -16.354 -6.462  1.00 14.33 ?  35  VAL   B HG12 1 
ATOM   4382 H HG13 . VAL   B 1 35  ? 48.390 -17.486 -5.350  1.00 14.33 ?  35  VAL   B HG13 1 
ATOM   4383 H HG21 . VAL   B 1 35  ? 48.772 -19.899 -6.989  1.00 14.21 ?  35  VAL   B HG21 1 
ATOM   4384 H HG22 . VAL   B 1 35  ? 47.558 -19.800 -5.969  1.00 14.21 ?  35  VAL   B HG22 1 
ATOM   4385 H HG23 . VAL   B 1 35  ? 47.286 -20.139 -7.498  1.00 14.21 ?  35  VAL   B HG23 1 
ATOM   4386 N N    . VAL   B 1 36  ? 44.961 -18.846 -5.371  1.00 10.28 ?  36  VAL   B N    1 
ATOM   4387 C CA   . VAL   B 1 36  ? 44.419 -19.049 -4.036  1.00 10.14 ?  36  VAL   B CA   1 
ATOM   4388 C C    . VAL   B 1 36  ? 45.428 -19.810 -3.183  1.00 9.90  ?  36  VAL   B C    1 
ATOM   4389 O O    . VAL   B 1 36  ? 45.973 -20.840 -3.607  1.00 10.92 ?  36  VAL   B O    1 
ATOM   4390 C CB   . VAL   B 1 36  ? 43.086 -19.811 -4.109  1.00 10.72 ?  36  VAL   B CB   1 
ATOM   4391 C CG1  . VAL   B 1 36  ? 42.583 -20.175 -2.719  1.00 11.33 ?  36  VAL   B CG1  1 
ATOM   4392 C CG2  . VAL   B 1 36  ? 42.059 -18.984 -4.865  1.00 11.35 ?  36  VAL   B CG2  1 
ATOM   4393 H H    . VAL   B 1 36  ? 44.769 -19.478 -5.921  1.00 12.34 ?  36  VAL   B H    1 
ATOM   4394 H HA   . VAL   B 1 36  ? 44.251 -18.188 -3.619  1.00 12.17 ?  36  VAL   B HA   1 
ATOM   4395 H HB   . VAL   B 1 36  ? 43.222 -20.636 -4.601  1.00 12.87 ?  36  VAL   B HB   1 
ATOM   4396 H HG11 . VAL   B 1 36  ? 41.644 -20.411 -2.778  1.00 13.60 ?  36  VAL   B HG11 1 
ATOM   4397 H HG12 . VAL   B 1 36  ? 43.092 -20.926 -2.382  1.00 13.60 ?  36  VAL   B HG12 1 
ATOM   4398 H HG13 . VAL   B 1 36  ? 42.692 -19.407 -2.136  1.00 13.60 ?  36  VAL   B HG13 1 
ATOM   4399 H HG21 . VAL   B 1 36  ? 41.213 -19.460 -4.877  1.00 13.63 ?  36  VAL   B HG21 1 
ATOM   4400 H HG22 . VAL   B 1 36  ? 41.951 -18.129 -4.420  1.00 13.63 ?  36  VAL   B HG22 1 
ATOM   4401 H HG23 . VAL   B 1 36  ? 42.370 -18.845 -5.775  1.00 13.63 ?  36  VAL   B HG23 1 
ATOM   4402 N N    . ASN   B 1 37  ? 45.648 -19.317 -1.963  1.00 10.32 ?  37  ASN   B N    1 
ATOM   4403 C CA   . ASN   B 1 37  ? 46.400 -20.042 -0.952  1.00 10.35 ?  37  ASN   B CA   1 
ATOM   4404 C C    . ASN   B 1 37  ? 45.452 -20.716 0.031   1.00 10.36 ?  37  ASN   B C    1 
ATOM   4405 O O    . ASN   B 1 37  ? 44.437 -20.142 0.438   1.00 10.85 ?  37  ASN   B O    1 
ATOM   4406 C CB   . ASN   B 1 37  ? 47.327 -19.095 -0.189  1.00 10.43 ?  37  ASN   B CB   1 
ATOM   4407 C CG   . ASN   B 1 37  ? 48.185 -19.814 0.821   1.00 11.07 ?  37  ASN   B CG   1 
ATOM   4408 O OD1  . ASN   B 1 37  ? 48.535 -20.984 0.634   1.00 11.58 ?  37  ASN   B OD1  1 
ATOM   4409 N ND2  . ASN   B 1 37  ? 48.538 -19.120 1.901   1.00 10.96 ?  37  ASN   B ND2  1 
ATOM   4410 H H    . ASN   B 1 37  ? 45.361 -18.550 -1.691  1.00 12.39 ?  37  ASN   B H    1 
ATOM   4411 H HA   . ASN   B 1 37  ? 46.937 -20.730 -1.372  1.00 12.43 ?  37  ASN   B HA   1 
ATOM   4412 H HB2  . ASN   B 1 37  ? 47.918 -18.658 -0.821  1.00 12.52 ?  37  ASN   B HB2  1 
ATOM   4413 H HB3  . ASN   B 1 37  ? 46.797 -18.438 0.284   1.00 12.52 ?  37  ASN   B HB3  1 
ATOM   4414 H HD21 . ASN   B 1 37  ? 49.033 -19.485 2.506   1.00 13.16 ?  37  ASN   B HD21 1 
ATOM   4415 H HD22 . ASN   B 1 37  ? 48.280 -18.311 1.999   1.00 13.16 ?  37  ASN   B HD22 1 
ATOM   4416 N N    . ALA   B 1 38  ? 45.803 -21.945 0.409   1.00 10.78 ?  38  ALA   B N    1 
ATOM   4417 C CA   . ALA   B 1 38  ? 45.152 -22.691 1.488   1.00 10.94 ?  38  ALA   B CA   1 
ATOM   4418 C C    . ALA   B 1 38  ? 45.734 -22.202 2.813   1.00 11.20 ?  38  ALA   B C    1 
ATOM   4419 O O    . ALA   B 1 38  ? 46.639 -22.806 3.401   1.00 11.92 ?  38  ALA   B O    1 
ATOM   4420 C CB   . ALA   B 1 38  ? 45.376 -24.187 1.295   1.00 12.15 ?  38  ALA   B CB   1 
ATOM   4421 H H    . ALA   B 1 38  ? 46.453 -22.380 0.054   1.00 12.94 ?  38  ALA   B H    1 
ATOM   4422 H HA   . ALA   B 1 38  ? 44.198 -22.512 1.482   1.00 13.13 ?  38  ALA   B HA   1 
ATOM   4423 H HB1  . ALA   B 1 38  ? 44.929 -24.667 2.017   1.00 14.59 ?  38  ALA   B HB1  1 
ATOM   4424 H HB2  . ALA   B 1 38  ? 44.992 -24.453 0.443   1.00 14.59 ?  38  ALA   B HB2  1 
ATOM   4425 H HB3  . ALA   B 1 38  ? 46.321 -24.372 1.310   1.00 14.59 ?  38  ALA   B HB3  1 
ATOM   4426 N N    . ALA   B 1 39  ? 45.210 -21.063 3.273   1.00 10.90 ?  39  ALA   B N    1 
ATOM   4427 C CA   . ALA   B 1 39  ? 45.758 -20.331 4.403   1.00 11.22 ?  39  ALA   B CA   1 
ATOM   4428 C C    . ALA   B 1 39  ? 45.141 -20.782 5.724   1.00 11.26 ?  39  ALA   B C    1 
ATOM   4429 O O    . ALA   B 1 39  ? 44.114 -21.460 5.770   1.00 12.29 ?  39  ALA   B O    1 
ATOM   4430 C CB   . ALA   B 1 39  ? 45.522 -18.828 4.210   1.00 11.72 ?  39  ALA   B CB   1 
ATOM   4431 H H    . ALA   B 1 39  ? 44.515 -20.691 2.930   1.00 13.08 ?  39  ALA   B H    1 
ATOM   4432 H HA   . ALA   B 1 39  ? 46.709 -20.483 4.451   1.00 13.47 ?  39  ALA   B HA   1 
ATOM   4433 H HB1  . ALA   B 1 39  ? 45.889 -18.350 4.970   1.00 14.06 ?  39  ALA   B HB1  1 
ATOM   4434 H HB2  . ALA   B 1 39  ? 45.966 -18.543 3.395   1.00 14.06 ?  39  ALA   B HB2  1 
ATOM   4435 H HB3  . ALA   B 1 39  ? 44.569 -18.660 4.142   1.00 14.06 ?  39  ALA   B HB3  1 
ATOM   4436 N N    . ASN   B 1 40  ? 45.784 -20.368 6.812   1.00 12.00 ?  40  ASN   B N    1 
ATOM   4437 C CA   . ASN   B 1 40  ? 45.220 -20.410 8.154   1.00 12.47 ?  40  ASN   B CA   1 
ATOM   4438 C C    . ASN   B 1 40  ? 45.043 -18.981 8.675   1.00 12.58 ?  40  ASN   B C    1 
ATOM   4439 O O    . ASN   B 1 40  ? 45.454 -18.002 8.041   1.00 12.33 ?  40  ASN   B O    1 
ATOM   4440 C CB   . ASN   B 1 40  ? 46.072 -21.279 9.094   1.00 13.64 ?  40  ASN   B CB   1 
ATOM   4441 C CG   . ASN   B 1 40  ? 47.534 -20.872 9.116   1.00 14.59 ?  40  ASN   B CG   1 
ATOM   4442 O OD1  . ASN   B 1 40  ? 47.856 -19.693 9.172   1.00 16.60 ?  40  ASN   B OD1  1 
ATOM   4443 N ND2  . ASN   B 1 40  ? 48.425 -21.848 9.075   1.00 14.57 ?  40  ASN   B ND2  1 
ATOM   4444 H H    . ASN   B 1 40  ? 46.581 -20.057 6.794   1.00 14.41 ?  40  ASN   B H    1 
ATOM   4445 H HA   . ASN   B 1 40  ? 44.335 -20.809 8.110   1.00 14.96 ?  40  ASN   B HA   1 
ATOM   4446 H HB2  . ASN   B 1 40  ? 45.725 -21.201 9.996   1.00 16.37 ?  40  ASN   B HB2  1 
ATOM   4447 H HB3  . ASN   B 1 40  ? 46.023 -22.201 8.797   1.00 16.37 ?  40  ASN   B HB3  1 
ATOM   4448 H HD21 . ASN   B 1 40  ? 49.266 -21.663 9.089   1.00 17.49 ?  40  ASN   B HD21 1 
ATOM   4449 H HD22 . ASN   B 1 40  ? 48.165 -22.666 9.040   1.00 17.49 ?  40  ASN   B HD22 1 
ATOM   4450 N N    . VAL   B 1 41  ? 44.394 -18.854 9.834   1.00 12.88 ?  41  VAL   B N    1 
ATOM   4451 C CA   . VAL   B 1 41  ? 43.936 -17.534 10.278  1.00 13.48 ?  41  VAL   B CA   1 
ATOM   4452 C C    . VAL   B 1 41  ? 45.088 -16.580 10.580  1.00 13.47 ?  41  VAL   B C    1 
ATOM   4453 O O    . VAL   B 1 41  ? 44.909 -15.361 10.506  1.00 13.49 ?  41  VAL   B O    1 
ATOM   4454 C CB   . VAL   B 1 41  ? 42.959 -17.617 11.467  1.00 14.88 ?  41  VAL   B CB   1 
ATOM   4455 C CG1  . VAL   B 1 41  ? 41.665 -18.310 11.060  1.00 15.32 ?  41  VAL   B CG1  1 
ATOM   4456 C CG2  . VAL   B 1 41  ? 43.613 -18.299 12.655  1.00 15.87 ?  41  VAL   B CG2  1 
ATOM   4457 H H    . VAL   B 1 41  ? 44.215 -19.496 10.368  1.00 15.46 ?  41  VAL   B H    1 
ATOM   4458 H HA   . VAL   B 1 41  ? 43.440 -17.136 9.547   1.00 16.18 ?  41  VAL   B HA   1 
ATOM   4459 H HB   . VAL   B 1 41  ? 42.729 -16.715 11.742  1.00 17.86 ?  41  VAL   B HB   1 
ATOM   4460 H HG11 . VAL   B 1 41  ? 41.059 -18.316 11.818  1.00 18.39 ?  41  VAL   B HG11 1 
ATOM   4461 H HG12 . VAL   B 1 41  ? 41.268 -17.826 10.321  1.00 18.39 ?  41  VAL   B HG12 1 
ATOM   4462 H HG13 . VAL   B 1 41  ? 41.868 -19.219 10.791  1.00 18.39 ?  41  VAL   B HG13 1 
ATOM   4463 H HG21 . VAL   B 1 41  ? 42.982 -18.337 13.386  1.00 19.05 ?  41  VAL   B HG21 1 
ATOM   4464 H HG22 . VAL   B 1 41  ? 43.877 -19.198 12.397  1.00 19.05 ?  41  VAL   B HG22 1 
ATOM   4465 H HG23 . VAL   B 1 41  ? 44.397 -17.791 12.919  1.00 19.05 ?  41  VAL   B HG23 1 
ATOM   4466 N N    . TYR   B 1 42  ? 46.260 -17.093 10.955  1.00 13.70 ?  42  TYR   B N    1 
ATOM   4467 C CA   . TYR   B 1 42  ? 47.416 -16.247 11.226  1.00 14.26 ?  42  TYR   B CA   1 
ATOM   4468 C C    . TYR   B 1 42  ? 48.382 -16.176 10.046  1.00 13.42 ?  42  TYR   B C    1 
ATOM   4469 O O    . TYR   B 1 42  ? 49.472 -15.606 10.177  1.00 14.59 ?  42  TYR   B O    1 
ATOM   4470 C CB   . TYR   B 1 42  ? 48.111 -16.658 12.530  1.00 16.03 ?  42  TYR   B CB   1 
ATOM   4471 C CG   . TYR   B 1 42  ? 47.501 -15.987 13.757  1.00 16.46 ?  42  TYR   B CG   1 
ATOM   4472 C CD1  . TYR   B 1 42  ? 47.703 -14.633 13.998  1.00 16.00 ?  42  TYR   B CD1  1 
ATOM   4473 C CD2  . TYR   B 1 42  ? 46.725 -16.693 14.659  1.00 18.31 ?  42  TYR   B CD2  1 
ATOM   4474 C CE1  . TYR   B 1 42  ? 47.153 -14.003 15.099  1.00 17.17 ?  42  TYR   B CE1  1 
ATOM   4475 C CE2  . TYR   B 1 42  ? 46.171 -16.072 15.771  1.00 18.59 ?  42  TYR   B CE2  1 
ATOM   4476 C CZ   . TYR   B 1 42  ? 46.386 -14.724 15.983  1.00 19.02 ?  42  TYR   B CZ   1 
ATOM   4477 O OH   . TYR   B 1 42  ? 45.847 -14.085 17.082  1.00 22.00 ?  42  TYR   B OH   1 
ATOM   4478 H H    . TYR   B 1 42  ? 46.409 -17.939 11.052  1.00 16.45 ?  42  TYR   B H    1 
ATOM   4479 H HA   . TYR   B 1 42  ? 47.088 -15.349 11.365  1.00 17.12 ?  42  TYR   B HA   1 
ATOM   4480 H HB2  . TYR   B 1 42  ? 48.036 -17.617 12.645  1.00 19.25 ?  42  TYR   B HB2  1 
ATOM   4481 H HB3  . TYR   B 1 42  ? 49.047 -16.402 12.481  1.00 19.25 ?  42  TYR   B HB3  1 
ATOM   4482 H HD1  . TYR   B 1 42  ? 48.222 -14.137 13.397  1.00 19.21 ?  42  TYR   B HD1  1 
ATOM   4483 H HD2  . TYR   B 1 42  ? 46.575 -17.602 14.516  1.00 21.97 ?  42  TYR   B HD2  1 
ATOM   4484 H HE1  . TYR   B 1 42  ? 47.303 -13.096 15.236  1.00 20.60 ?  42  TYR   B HE1  1 
ATOM   4485 H HE2  . TYR   B 1 42  ? 45.650 -16.562 16.365  1.00 22.31 ?  42  TYR   B HE2  1 
ATOM   4486 H HH   . TYR   B 1 42  ? 46.064 -13.276 17.071  1.00 26.41 ?  42  TYR   B HH   1 
ATOM   4487 N N    . LEU   B 1 43  ? 47.981 -16.689 8.885   1.00 12.33 ?  43  LEU   B N    1 
ATOM   4488 C CA   . LEU   B 1 43  ? 48.793 -16.619 7.677   1.00 12.25 ?  43  LEU   B CA   1 
ATOM   4489 C C    . LEU   B 1 43  ? 50.206 -17.125 7.936   1.00 12.16 ?  43  LEU   B C    1 
ATOM   4490 O O    . LEU   B 1 43  ? 51.186 -16.531 7.486   1.00 13.03 ?  43  LEU   B O    1 
ATOM   4491 C CB   . LEU   B 1 43  ? 48.811 -15.216 7.065   1.00 12.24 ?  43  LEU   B CB   1 
ATOM   4492 C CG   . LEU   B 1 43  ? 47.455 -14.601 6.692   1.00 12.34 ?  43  LEU   B CG   1 
ATOM   4493 C CD1  . LEU   B 1 43  ? 47.661 -13.200 6.114   1.00 13.90 ?  43  LEU   B CD1  1 
ATOM   4494 C CD2  . LEU   B 1 43  ? 46.693 -15.490 5.715   1.00 12.71 ?  43  LEU   B CD2  1 
ATOM   4495 H H    . LEU   B 1 43  ? 47.233 -17.100 8.773   1.00 14.80 ?  43  LEU   B H    1 
ATOM   4496 H HA   . LEU   B 1 43  ? 48.395 -17.211 7.015   1.00 14.71 ?  43  LEU   B HA   1 
ATOM   4497 H HB2  . LEU   B 1 43  ? 49.233 -14.617 7.698   1.00 14.69 ?  43  LEU   B HB2  1 
ATOM   4498 H HB3  . LEU   B 1 43  ? 49.338 -15.251 6.252   1.00 14.69 ?  43  LEU   B HB3  1 
ATOM   4499 H HG   . LEU   B 1 43  ? 46.920 -14.512 7.495   1.00 14.81 ?  43  LEU   B HG   1 
ATOM   4500 H HD11 . LEU   B 1 43  ? 46.797 -12.822 5.886   1.00 16.69 ?  43  LEU   B HD11 1 
ATOM   4501 H HD12 . LEU   B 1 43  ? 48.097 -12.644 6.782   1.00 16.69 ?  43  LEU   B HD12 1 
ATOM   4502 H HD13 . LEU   B 1 43  ? 48.216 -13.261 5.323   1.00 16.69 ?  43  LEU   B HD13 1 
ATOM   4503 H HD21 . LEU   B 1 43  ? 45.890 -15.027 5.425   1.00 15.26 ?  43  LEU   B HD21 1 
ATOM   4504 H HD22 . LEU   B 1 43  ? 47.259 -15.678 4.950   1.00 15.26 ?  43  LEU   B HD22 1 
ATOM   4505 H HD23 . LEU   B 1 43  ? 46.454 -16.317 6.161   1.00 15.26 ?  43  LEU   B HD23 1 
ATOM   4506 N N    . LYS   B 1 44  ? 50.306 -18.248 8.649   1.00 12.46 ?  44  LYS   B N    1 
ATOM   4507 C CA   . LYS   B 1 44  ? 51.574 -18.927 8.884   1.00 13.10 ?  44  LYS   B CA   1 
ATOM   4508 C C    . LYS   B 1 44  ? 51.688 -20.048 7.859   1.00 12.59 ?  44  LYS   B C    1 
ATOM   4509 O O    . LYS   B 1 44  ? 50.992 -21.064 7.952   1.00 13.86 ?  44  LYS   B O    1 
ATOM   4510 C CB   . LYS   B 1 44  ? 51.639 -19.443 10.320  1.00 14.96 ?  44  LYS   B CB   1 
ATOM   4511 C CG   . LYS   B 1 44  ? 51.813 -18.338 11.353  1.00 17.65 ?  44  LYS   B CG   1 
ATOM   4512 C CD   . LYS   B 1 44  ? 52.986 -17.440 10.960  1.00 20.67 ?  44  LYS   B CD   1 
ATOM   4513 C CE   . LYS   B 1 44  ? 53.543 -16.649 12.116  1.00 23.54 ?  44  LYS   B CE   1 
ATOM   4514 N NZ   . LYS   B 1 44  ? 54.693 -15.801 11.720  1.00 24.79 ?  44  LYS   B NZ   1 
ATOM   4515 H H    . LYS   B 1 44  ? 49.633 -18.632 9.022   1.00 14.96 ?  44  LYS   B H    1 
ATOM   4516 H HA   . LYS   B 1 44  ? 52.304 -18.309 8.723   1.00 15.73 ?  44  LYS   B HA   1 
ATOM   4517 H HB2  . LYS   B 1 44  ? 50.811 -19.910 10.524  1.00 17.96 ?  44  LYS   B HB2  1 
ATOM   4518 H HB3  . LYS   B 1 44  ? 52.388 -20.049 10.403  1.00 17.96 ?  44  LYS   B HB3  1 
ATOM   4519 H HG2  . LYS   B 1 44  ? 51.008 -17.802 11.395  1.00 21.19 ?  44  LYS   B HG2  1 
ATOM   4520 H HG3  . LYS   B 1 44  ? 52.005 -18.736 12.220  1.00 21.19 ?  44  LYS   B HG3  1 
ATOM   4521 H HD2  . LYS   B 1 44  ? 53.693 -17.998 10.591  1.00 24.81 ?  44  LYS   B HD2  1 
ATOM   4522 H HD3  . LYS   B 1 44  ? 52.679 -16.812 10.286  1.00 24.81 ?  44  LYS   B HD3  1 
ATOM   4523 H HE2  . LYS   B 1 44  ? 52.857 -16.050 12.419  1.00 28.25 ?  44  LYS   B HE2  1 
ATOM   4524 H HE3  . LYS   B 1 44  ? 53.819 -17.255 12.828  1.00 28.25 ?  44  LYS   B HE3  1 
ATOM   4525 H HZ1  . LYS   B 1 44  ? 54.994 -15.349 12.425  1.00 29.75 ?  44  LYS   B HZ1  1 
ATOM   4526 H HZ2  . LYS   B 1 44  ? 55.349 -16.303 11.394  1.00 29.75 ?  44  LYS   B HZ2  1 
ATOM   4527 H HZ3  . LYS   B 1 44  ? 54.436 -15.219 11.094  1.00 29.75 ?  44  LYS   B HZ3  1 
ATOM   4528 N N    . HIS   B 1 45  ? 52.544 -19.838 6.860   1.00 12.46 ?  45  HIS   B N    1 
ATOM   4529 C CA   . HIS   B 1 45  ? 52.569 -20.670 5.659   1.00 12.37 ?  45  HIS   B CA   1 
ATOM   4530 C C    . HIS   B 1 45  ? 53.591 -21.792 5.823   1.00 14.54 ?  45  HIS   B C    1 
ATOM   4531 O O    . HIS   B 1 45  ? 54.652 -21.810 5.208   1.00 16.95 ?  45  HIS   B O    1 
ATOM   4532 C CB   . HIS   B 1 45  ? 52.876 -19.816 4.438   1.00 12.74 ?  45  HIS   B CB   1 
ATOM   4533 C CG   . HIS   B 1 45  ? 52.006 -18.612 4.326   1.00 12.26 ?  45  HIS   B CG   1 
ATOM   4534 N ND1  . HIS   B 1 45  ? 50.628 -18.685 4.294   1.00 12.45 ?  45  HIS   B ND1  1 
ATOM   4535 C CD2  . HIS   B 1 45  ? 52.323 -17.298 4.258   1.00 13.31 ?  45  HIS   B CD2  1 
ATOM   4536 C CE1  . HIS   B 1 45  ? 50.140 -17.461 4.191   1.00 12.28 ?  45  HIS   B CE1  1 
ATOM   4537 N NE2  . HIS   B 1 45  ? 51.144 -16.601 4.167   1.00 13.00 ?  45  HIS   B NE2  1 
ATOM   4538 H H    . HIS   B 1 45  ? 53.113 -19.196 6.850   1.00 14.96 ?  45  HIS   B H    1 
ATOM   4539 H HA   . HIS   B 1 45  ? 51.688 -21.069 5.531   1.00 14.85 ?  45  HIS   B HA   1 
ATOM   4540 H HB2  . HIS   B 1 45  ? 53.796 -19.519 4.489   1.00 15.30 ?  45  HIS   B HB2  1 
ATOM   4541 H HB3  . HIS   B 1 45  ? 52.747 -20.356 3.639   1.00 15.30 ?  45  HIS   B HB3  1 
ATOM   4542 H HD2  . HIS   B 1 45  ? 53.179 -16.932 4.267   1.00 15.97 ?  45  HIS   B HD2  1 
ATOM   4543 H HE1  . HIS   B 1 45  ? 49.237 -17.243 4.135   1.00 14.75 ?  45  HIS   B HE1  1 
ATOM   4544 H HE2  . HIS   B 1 45  ? 51.067 -15.747 4.114   1.00 15.60 ?  45  HIS   B HE2  1 
ATOM   4545 N N    A GLY   B 1 46  ? 53.227 -22.759 6.659   0.72 15.72 ?  46  GLY   B N    1 
ATOM   4546 N N    B GLY   B 1 46  ? 53.235 -22.745 6.676   0.28 15.56 ?  46  GLY   B N    1 
ATOM   4547 C CA   A GLY   B 1 46  ? 54.149 -23.818 7.030   0.72 17.34 ?  46  GLY   B CA   1 
ATOM   4548 C CA   B GLY   B 1 46  ? 54.148 -23.816 7.013   0.28 16.70 ?  46  GLY   B CA   1 
ATOM   4549 C C    A GLY   B 1 46  ? 54.192 -25.034 6.124   0.72 18.94 ?  46  GLY   B C    1 
ATOM   4550 C C    B GLY   B 1 46  ? 54.170 -24.953 6.010   0.28 17.88 ?  46  GLY   B C    1 
ATOM   4551 O O    A GLY   B 1 46  ? 55.270 -25.458 5.693   0.72 22.18 ?  46  GLY   B O    1 
ATOM   4552 O O    B GLY   B 1 46  ? 55.193 -25.209 5.368   0.28 18.72 ?  46  GLY   B O    1 
ATOM   4553 H H    A GLY   B 1 46  ? 52.454 -22.811 7.040   0.72 18.87 ?  46  GLY   B H    1 
ATOM   4554 H H    B GLY   B 1 46  ? 52.469 -22.786 7.075   0.28 18.67 ?  46  GLY   B H    1 
ATOM   4555 H HA2  A GLY   B 1 46  ? 55.042 -23.446 7.074   0.72 20.82 ?  46  GLY   B HA2  1 
ATOM   4556 H HA2  B GLY   B 1 46  ? 55.044 -23.453 7.078   0.28 20.04 ?  46  GLY   B HA2  1 
ATOM   4557 H HA3  A GLY   B 1 46  ? 53.914 -24.134 7.916   0.72 20.82 ?  46  GLY   B HA3  1 
ATOM   4558 H HA3  B GLY   B 1 46  ? 53.905 -24.172 7.883   0.28 20.04 ?  46  GLY   B HA3  1 
ATOM   4559 N N    . GLY   B 1 47  ? 53.035 -25.633 5.851   1.00 18.49 ?  47  GLY   B N    1 
ATOM   4560 C CA   . GLY   B 1 47  ? 52.976 -26.894 5.140   1.00 16.29 ?  47  GLY   B CA   1 
ATOM   4561 C C    . GLY   B 1 47  ? 52.063 -26.865 3.928   1.00 13.96 ?  47  GLY   B C    1 
ATOM   4562 O O    . GLY   B 1 47  ? 51.408 -25.863 3.636   1.00 14.18 ?  47  GLY   B O    1 
ATOM   4563 H H    A GLY   B 1 47  ? 52.266 -25.338 6.099   0.72 22.20 ?  47  GLY   B H    1 
ATOM   4564 H H    B GLY   B 1 47  ? 52.273 -25.373 6.155   0.28 22.20 ?  47  GLY   B H    1 
ATOM   4565 H HA2  . GLY   B 1 47  ? 53.866 -27.144 4.843   1.00 19.55 ?  47  GLY   B HA2  1 
ATOM   4566 H HA3  . GLY   B 1 47  ? 52.660 -27.586 5.746   1.00 19.55 ?  47  GLY   B HA3  1 
ATOM   4567 N N    . GLY   B 1 48  ? 52.027 -28.000 3.232   1.00 13.62 ?  48  GLY   B N    1 
ATOM   4568 C CA   . GLY   B 1 48  ? 51.099 -28.152 2.127   1.00 12.94 ?  48  GLY   B CA   1 
ATOM   4569 C C    . GLY   B 1 48  ? 51.235 -27.041 1.111   1.00 12.23 ?  48  GLY   B C    1 
ATOM   4570 O O    . GLY   B 1 48  ? 52.334 -26.578 0.795   1.00 13.09 ?  48  GLY   B O    1 
ATOM   4571 H H    . GLY   B 1 48  ? 52.535 -28.675 3.372   1.00 16.35 ?  48  GLY   B H    1 
ATOM   4572 H HA2  . GLY   B 1 48  ? 51.259 -29.000 1.685   1.00 15.53 ?  48  GLY   B HA2  1 
ATOM   4573 H HA3  . GLY   B 1 48  ? 50.190 -28.148 2.466   1.00 15.53 ?  48  GLY   B HA3  1 
ATOM   4574 N N    . VAL   B 1 49  ? 50.091 -26.609 0.578   1.00 12.28 ?  49  VAL   B N    1 
ATOM   4575 C CA   . VAL   B 1 49  ? 50.072 -25.582 -0.462  1.00 12.32 ?  49  VAL   B CA   1 
ATOM   4576 C C    . VAL   B 1 49  ? 50.728 -24.292 0.026   1.00 11.36 ?  49  VAL   B C    1 
ATOM   4577 O O    . VAL   B 1 49  ? 51.521 -23.674 -0.693  1.00 12.32 ?  49  VAL   B O    1 
ATOM   4578 C CB   . VAL   B 1 49  ? 48.628 -25.336 -0.941  1.00 13.84 ?  49  VAL   B CB   1 
ATOM   4579 C CG1  . VAL   B 1 49  ? 48.549 -24.095 -1.822  1.00 14.15 ?  49  VAL   B CG1  1 
ATOM   4580 C CG2  . VAL   B 1 49  ? 48.087 -26.556 -1.685  1.00 15.37 ?  49  VAL   B CG2  1 
ATOM   4581 H H    . VAL   B 1 49  ? 49.307 -26.893 0.802   1.00 14.74 ?  49  VAL   B H    1 
ATOM   4582 H HA   . VAL   B 1 49  ? 50.577 -25.900 -1.224  1.00 14.79 ?  49  VAL   B HA   1 
ATOM   4583 H HB   . VAL   B 1 49  ? 48.058 -25.186 -0.171  1.00 16.61 ?  49  VAL   B HB   1 
ATOM   4584 H HG11 . VAL   B 1 49  ? 47.716 -24.110 -2.321  1.00 16.98 ?  49  VAL   B HG11 1 
ATOM   4585 H HG12 . VAL   B 1 49  ? 48.576 -23.302 -1.259  1.00 16.98 ?  49  VAL   B HG12 1 
ATOM   4586 H HG13 . VAL   B 1 49  ? 49.300 -24.091 -2.435  1.00 16.98 ?  49  VAL   B HG13 1 
ATOM   4587 H HG21 . VAL   B 1 49  ? 47.177 -26.374 -1.974  1.00 18.45 ?  49  VAL   B HG21 1 
ATOM   4588 H HG22 . VAL   B 1 49  ? 48.649 -26.729 -2.458  1.00 18.45 ?  49  VAL   B HG22 1 
ATOM   4589 H HG23 . VAL   B 1 49  ? 48.098 -27.319 -1.089  1.00 18.45 ?  49  VAL   B HG23 1 
ATOM   4590 N N    . ALA   B 1 50  ? 50.386 -23.849 1.234   1.00 11.35 ?  50  ALA   B N    1 
ATOM   4591 C CA   . ALA   B 1 50  ? 50.908 -22.571 1.712   1.00 11.20 ?  50  ALA   B CA   1 
ATOM   4592 C C    . ALA   B 1 50  ? 52.429 -22.602 1.823   1.00 11.82 ?  50  ALA   B C    1 
ATOM   4593 O O    . ALA   B 1 50  ? 53.113 -21.634 1.463   1.00 11.74 ?  50  ALA   B O    1 
ATOM   4594 C CB   . ALA   B 1 50  ? 50.272 -22.213 3.054   1.00 11.87 ?  50  ALA   B CB   1 
ATOM   4595 H H    . ALA   B 1 50  ? 49.864 -24.257 1.784   1.00 13.63 ?  50  ALA   B H    1 
ATOM   4596 H HA   . ALA   B 1 50  ? 50.676 -21.878 1.082   1.00 13.45 ?  50  ALA   B HA   1 
ATOM   4597 H HB1  . ALA   B 1 50  ? 50.627 -21.360 3.358   1.00 14.25 ?  50  ALA   B HB1  1 
ATOM   4598 H HB2  . ALA   B 1 50  ? 49.309 -22.142 2.940   1.00 14.25 ?  50  ALA   B HB2  1 
ATOM   4599 H HB3  . ALA   B 1 50  ? 50.475 -22.904 3.702   1.00 14.25 ?  50  ALA   B HB3  1 
ATOM   4600 N N    . GLY   B 1 51  ? 52.980 -23.697 2.336   1.00 12.24 ?  51  GLY   B N    1 
ATOM   4601 C CA   . GLY   B 1 51  ? 54.424 -23.797 2.406   1.00 12.78 ?  51  GLY   B CA   1 
ATOM   4602 C C    . GLY   B 1 51  ? 55.069 -23.742 1.037   1.00 12.71 ?  51  GLY   B C    1 
ATOM   4603 O O    . GLY   B 1 51  ? 56.116 -23.111 0.859   1.00 13.58 ?  51  GLY   B O    1 
ATOM   4604 H H    . GLY   B 1 51  ? 52.553 -24.381 2.637   1.00 14.69 ?  51  GLY   B H    1 
ATOM   4605 H HA2  . GLY   B 1 51  ? 54.778 -23.066 2.935   1.00 15.35 ?  51  GLY   B HA2  1 
ATOM   4606 H HA3  . GLY   B 1 51  ? 54.676 -24.634 2.828   1.00 15.35 ?  51  GLY   B HA3  1 
ATOM   4607 N N    . ALA   B 1 52  ? 54.462 -24.411 0.056   1.00 12.19 ?  52  ALA   B N    1 
ATOM   4608 C CA   . ALA   B 1 52  ? 55.021 -24.420 -1.290  1.00 12.76 ?  52  ALA   B CA   1 
ATOM   4609 C C    . ALA   B 1 52  ? 54.939 -23.041 -1.939  1.00 11.99 ?  52  ALA   B C    1 
ATOM   4610 O O    . ALA   B 1 52  ? 55.906 -22.587 -2.568  1.00 13.08 ?  52  ALA   B O    1 
ATOM   4611 C CB   . ALA   B 1 52  ? 54.315 -25.466 -2.150  1.00 13.39 ?  52  ALA   B CB   1 
ATOM   4612 H H    . ALA   B 1 52  ? 53.731 -24.860 0.141   1.00 14.64 ?  52  ALA   B H    1 
ATOM   4613 H HA   . ALA   B 1 52  ? 55.956 -24.664 -1.238  1.00 15.32 ?  52  ALA   B HA   1 
ATOM   4614 H HB1  . ALA   B 1 52  ? 54.705 -25.456 -3.042  1.00 16.07 ?  52  ALA   B HB1  1 
ATOM   4615 H HB2  . ALA   B 1 52  ? 54.442 -26.341 -1.748  1.00 16.07 ?  52  ALA   B HB2  1 
ATOM   4616 H HB3  . ALA   B 1 52  ? 53.373 -25.256 -2.199  1.00 16.07 ?  52  ALA   B HB3  1 
ATOM   4617 N N    . LEU   B 1 53  ? 53.796 -22.362 -1.815  1.00 11.82 ?  53  LEU   B N    1 
ATOM   4618 C CA   . LEU   B 1 53  ? 53.688 -21.022 -2.386  1.00 12.03 ?  53  LEU   B CA   1 
ATOM   4619 C C    . LEU   B 1 53  ? 54.695 -20.079 -1.739  1.00 11.86 ?  53  LEU   B C    1 
ATOM   4620 O O    . LEU   B 1 53  ? 55.399 -19.329 -2.425  1.00 12.54 ?  53  LEU   B O    1 
ATOM   4621 C CB   . LEU   B 1 53  ? 52.267 -20.476 -2.216  1.00 12.75 ?  53  LEU   B CB   1 
ATOM   4622 C CG   . LEU   B 1 53  ? 51.134 -21.209 -2.942  1.00 12.77 ?  53  LEU   B CG   1 
ATOM   4623 C CD1  . LEU   B 1 53  ? 49.794 -20.587 -2.602  1.00 14.52 ?  53  LEU   B CD1  1 
ATOM   4624 C CD2  . LEU   B 1 53  ? 51.350 -21.211 -4.453  1.00 14.98 ?  53  LEU   B CD2  1 
ATOM   4625 H H    . LEU   B 1 53  ? 53.092 -22.642 -1.410  1.00 14.19 ?  53  LEU   B H    1 
ATOM   4626 H HA   . LEU   B 1 53  ? 53.888 -21.067 -3.337  1.00 14.44 ?  53  LEU   B HA   1 
ATOM   4627 H HB2  . LEU   B 1 53  ? 52.053 -20.490 -1.274  1.00 15.30 ?  53  LEU   B HB2  1 
ATOM   4628 H HB3  . LEU   B 1 53  ? 52.259 -19.561 -2.535  1.00 15.30 ?  53  LEU   B HB3  1 
ATOM   4629 H HG   . LEU   B 1 53  ? 51.116 -22.130 -2.644  1.00 15.33 ?  53  LEU   B HG   1 
ATOM   4630 H HD11 . LEU   B 1 53  ? 49.092 -21.069 -3.070  1.00 17.43 ?  53  LEU   B HD11 1 
ATOM   4631 H HD12 . LEU   B 1 53  ? 49.650 -20.648 -1.643  1.00 17.43 ?  53  LEU   B HD12 1 
ATOM   4632 H HD13 . LEU   B 1 53  ? 49.794 -19.657 -2.877  1.00 17.43 ?  53  LEU   B HD13 1 
ATOM   4633 H HD21 . LEU   B 1 53  ? 50.624 -21.697 -4.874  1.00 17.98 ?  53  LEU   B HD21 1 
ATOM   4634 H HD22 . LEU   B 1 53  ? 51.362 -20.296 -4.772  1.00 17.98 ?  53  LEU   B HD22 1 
ATOM   4635 H HD23 . LEU   B 1 53  ? 52.195 -21.644 -4.653  1.00 17.98 ?  53  LEU   B HD23 1 
ATOM   4636 N N    . ASN   B 1 54  ? 54.786 -20.107 -0.412  1.00 11.74 ?  54  ASN   B N    1 
ATOM   4637 C CA   . ASN   B 1 54  ? 55.699 -19.193 0.260   1.00 12.49 ?  54  ASN   B CA   1 
ATOM   4638 C C    . ASN   B 1 54  ? 57.144 -19.470 -0.139  1.00 12.71 ?  54  ASN   B C    1 
ATOM   4639 O O    . ASN   B 1 54  ? 57.921 -18.534 -0.373  1.00 13.01 ?  54  ASN   B O    1 
ATOM   4640 C CB   . ASN   B 1 54  ? 55.536 -19.275 1.771   1.00 13.57 ?  54  ASN   B CB   1 
ATOM   4641 C CG   . ASN   B 1 54  ? 56.510 -18.365 2.488   1.00 13.45 ?  54  ASN   B CG   1 
ATOM   4642 O OD1  . ASN   B 1 54  ? 56.540 -17.157 2.240   1.00 13.53 ?  54  ASN   B OD1  1 
ATOM   4643 N ND2  . ASN   B 1 54  ? 57.337 -18.939 3.351   1.00 14.85 ?  54  ASN   B ND2  1 
ATOM   4644 H H    . ASN   B 1 54  ? 54.340 -20.629 0.104   1.00 14.09 ?  54  ASN   B H    1 
ATOM   4645 H HA   . ASN   B 1 54  ? 55.485 -18.287 -0.012  1.00 15.00 ?  54  ASN   B HA   1 
ATOM   4646 H HB2  . ASN   B 1 54  ? 54.637 -19.003 2.011   1.00 16.29 ?  54  ASN   B HB2  1 
ATOM   4647 H HB3  . ASN   B 1 54  ? 55.703 -20.183 2.061   1.00 16.29 ?  54  ASN   B HB3  1 
ATOM   4648 H HD21 . ASN   B 1 54  ? 57.914 -18.463 3.779   1.00 17.83 ?  54  ASN   B HD21 1 
ATOM   4649 H HD22 . ASN   B 1 54  ? 57.295 -19.787 3.488   1.00 17.83 ?  54  ASN   B HD22 1 
ATOM   4650 N N    . LYS   B 1 55  ? 57.525 -20.748 -0.206  1.00 13.31 ?  55  LYS   B N    1 
ATOM   4651 C CA   . LYS   B 1 55  ? 58.880 -21.093 -0.624  1.00 14.56 ?  55  LYS   B CA   1 
ATOM   4652 C C    . LYS   B 1 55  ? 59.176 -20.561 -2.019  1.00 14.02 ?  55  LYS   B C    1 
ATOM   4653 O O    . LYS   B 1 55  ? 60.275 -20.054 -2.275  1.00 14.58 ?  55  LYS   B O    1 
ATOM   4654 C CB   . LYS   B 1 55  ? 59.076 -22.608 -0.567  1.00 16.23 ?  55  LYS   B CB   1 
ATOM   4655 C CG   . LYS   B 1 55  ? 60.454 -23.071 -1.005  1.00 20.47 ?  55  LYS   B CG   1 
ATOM   4656 C CD   . LYS   B 1 55  ? 60.620 -24.570 -0.815  1.00 24.06 ?  55  LYS   B CD   1 
ATOM   4657 C CE   . LYS   B 1 55  ? 60.736 -24.949 0.661   1.00 27.30 ?  55  LYS   B CE   1 
ATOM   4658 N NZ   . LYS   B 1 55  ? 61.071 -26.384 0.845   1.00 29.02 ?  55  LYS   B NZ   1 
ATOM   4659 H H    . LYS   B 1 55  ? 57.019 -21.421 -0.022  1.00 15.98 ?  55  LYS   B H    1 
ATOM   4660 H HA   . LYS   B 1 55  ? 59.507 -20.685 -0.013  1.00 17.48 ?  55  LYS   B HA   1 
ATOM   4661 H HB2  . LYS   B 1 55  ? 58.938 -22.898 0.348   1.00 19.48 ?  55  LYS   B HB2  1 
ATOM   4662 H HB3  . LYS   B 1 55  ? 58.423 -23.029 -1.147  1.00 19.48 ?  55  LYS   B HB3  1 
ATOM   4663 H HG2  . LYS   B 1 55  ? 60.578 -22.870 -1.945  1.00 24.57 ?  55  LYS   B HG2  1 
ATOM   4664 H HG3  . LYS   B 1 55  ? 61.128 -22.619 -0.472  1.00 24.57 ?  55  LYS   B HG3  1 
ATOM   4665 H HD2  . LYS   B 1 55  ? 59.849 -25.030 -1.183  1.00 28.87 ?  55  LYS   B HD2  1 
ATOM   4666 H HD3  . LYS   B 1 55  ? 61.430 -24.864 -1.264  1.00 28.87 ?  55  LYS   B HD3  1 
ATOM   4667 H HE2  . LYS   B 1 55  ? 61.438 -24.413 1.068   1.00 32.76 ?  55  LYS   B HE2  1 
ATOM   4668 H HE3  . LYS   B 1 55  ? 59.888 -24.771 1.100   1.00 32.76 ?  55  LYS   B HE3  1 
ATOM   4669 H HZ1  . LYS   B 1 55  ? 61.096 -26.578 1.713   1.00 34.83 ?  55  LYS   B HZ1  1 
ATOM   4670 H HZ2  . LYS   B 1 55  ? 60.451 -26.888 0.453   1.00 34.83 ?  55  LYS   B HZ2  1 
ATOM   4671 H HZ3  . LYS   B 1 55  ? 61.861 -26.559 0.482   1.00 34.83 ?  55  LYS   B HZ3  1 
ATOM   4672 N N    . ALA   B 1 56  ? 58.202 -20.642 -2.931  1.00 13.64 ?  56  ALA   B N    1 
ATOM   4673 C CA   . ALA   B 1 56  ? 58.429 -20.139 -4.281  1.00 14.52 ?  56  ALA   B CA   1 
ATOM   4674 C C    . ALA   B 1 56  ? 58.706 -18.642 -4.280  1.00 14.08 ?  56  ALA   B C    1 
ATOM   4675 O O    . ALA   B 1 56  ? 59.435 -18.144 -5.150  1.00 15.34 ?  56  ALA   B O    1 
ATOM   4676 C CB   . ALA   B 1 56  ? 57.237 -20.469 -5.178  1.00 15.21 ?  56  ALA   B CB   1 
ATOM   4677 H H    . ALA   B 1 56  ? 57.413 -20.963 -2.794  1.00 16.38 ?  56  ALA   B H    1 
ATOM   4678 H HA   . ALA   B 1 56  ? 59.205 -20.577 -4.650  1.00 17.42 ?  56  ALA   B HA   1 
ATOM   4679 H HB1  . ALA   B 1 56  ? 57.410 -20.134 -6.074  1.00 18.26 ?  56  ALA   B HB1  1 
ATOM   4680 H HB2  . ALA   B 1 56  ? 57.123 -21.434 -5.206  1.00 18.26 ?  56  ALA   B HB2  1 
ATOM   4681 H HB3  . ALA   B 1 56  ? 56.439 -20.053 -4.819  1.00 18.26 ?  56  ALA   B HB3  1 
ATOM   4682 N N    . THR   B 1 57  ? 58.139 -17.909 -3.318  1.00 13.81 ?  57  THR   B N    1 
ATOM   4683 C CA   . THR   B 1 57  ? 58.378 -16.474 -3.192  1.00 13.94 ?  57  THR   B CA   1 
ATOM   4684 C C    . THR   B 1 57  ? 59.628 -16.149 -2.382  1.00 14.78 ?  57  THR   B C    1 
ATOM   4685 O O    . THR   B 1 57  ? 59.867 -14.974 -2.075  1.00 15.37 ?  57  THR   B O    1 
ATOM   4686 C CB   . THR   B 1 57  ? 57.175 -15.745 -2.556  1.00 12.97 ?  57  THR   B CB   1 
ATOM   4687 O OG1  . THR   B 1 57  ? 57.148 -15.959 -1.137  1.00 13.46 ?  57  THR   B OG1  1 
ATOM   4688 C CG2  . THR   B 1 57  ? 55.854 -16.157 -3.200  1.00 13.49 ?  57  THR   B CG2  1 
ATOM   4689 H H    . THR   B 1 57  ? 57.595 -18.224 -2.725  1.00 16.58 ?  57  THR   B H    1 
ATOM   4690 H HA   . THR   B 1 57  ? 58.501 -16.110 -4.081  1.00 16.74 ?  57  THR   B HA   1 
ATOM   4691 H HB   . THR   B 1 57  ? 57.284 -14.794 -2.720  1.00 15.57 ?  57  THR   B HB   1 
ATOM   4692 H HG1  . THR   B 1 57  ? 57.066 -16.780 -0.977  1.00 16.16 ?  57  THR   B HG1  1 
ATOM   4693 H HG21 . THR   B 1 57  ? 55.128 -15.632 -2.835  1.00 16.19 ?  57  THR   B HG21 1 
ATOM   4694 H HG22 . THR   B 1 57  ? 55.893 -16.018 -4.161  1.00 16.19 ?  57  THR   B HG22 1 
ATOM   4695 H HG23 . THR   B 1 57  ? 55.680 -17.096 -3.029  1.00 16.19 ?  57  THR   B HG23 1 
ATOM   4696 N N    . ASN   B 1 58  ? 60.423 -17.153 -2.018  1.00 15.19 ?  58  ASN   B N    1 
ATOM   4697 C CA   . ASN   B 1 58  ? 61.624 -16.930 -1.216  1.00 18.18 ?  58  ASN   B CA   1 
ATOM   4698 C C    . ASN   B 1 58  ? 61.290 -16.218 0.096   1.00 16.16 ?  58  ASN   B C    1 
ATOM   4699 O O    . ASN   B 1 58  ? 62.035 -15.350 0.563   1.00 16.70 ?  58  ASN   B O    1 
ATOM   4700 C CB   . ASN   B 1 58  ? 62.705 -16.181 -2.003  1.00 26.19 ?  58  ASN   B CB   1 
ATOM   4701 C CG   . ASN   B 1 58  ? 64.080 -16.315 -1.375  1.00 35.30 ?  58  ASN   B CG   1 
ATOM   4702 O OD1  . ASN   B 1 58  ? 64.394 -17.329 -0.752  1.00 38.15 ?  58  ASN   B OD1  1 
ATOM   4703 N ND2  . ASN   B 1 58  ? 64.908 -15.288 -1.536  1.00 41.16 ?  58  ASN   B ND2  1 
ATOM   4704 H H    . ASN   B 1 58  ? 60.288 -17.981 -2.220  1.00 18.24 ?  58  ASN   B H    1 
ATOM   4705 H HA   . ASN   B 1 58  ? 61.993 -17.798 -0.990  1.00 21.82 ?  58  ASN   B HA   1 
ATOM   4706 H HB2  . ASN   B 1 58  ? 62.750 -16.540 -2.906  1.00 31.43 ?  58  ASN   B HB2  1 
ATOM   4707 H HB3  . ASN   B 1 58  ? 62.483 -15.239 -2.032  1.00 31.43 ?  58  ASN   B HB3  1 
ATOM   4708 H HD21 . ASN   B 1 58  ? 65.701 -15.317 -1.201  1.00 49.40 ?  58  ASN   B HD21 1 
ATOM   4709 H HD22 . ASN   B 1 58  ? 64.653 -14.595 -1.975  1.00 49.40 ?  58  ASN   B HD22 1 
ATOM   4710 N N    . ASN   B 1 59  ? 60.164 -16.603 0.703   1.00 15.06 ?  59  ASN   B N    1 
ATOM   4711 C CA   . ASN   B 1 59  ? 59.687 -16.137 2.008   1.00 14.92 ?  59  ASN   B CA   1 
ATOM   4712 C C    . ASN   B 1 59  ? 59.095 -14.728 1.959   1.00 14.23 ?  59  ASN   B C    1 
ATOM   4713 O O    . ASN   B 1 59  ? 58.656 -14.230 3.002   1.00 14.24 ?  59  ASN   B O    1 
ATOM   4714 C CB   . ASN   B 1 59  ? 60.759 -16.207 3.112   1.00 16.34 ?  59  ASN   B CB   1 
ATOM   4715 C CG   . ASN   B 1 59  ? 60.168 -16.373 4.493   1.00 17.76 ?  59  ASN   B CG   1 
ATOM   4716 O OD1  . ASN   B 1 59  ? 59.342 -17.256 4.719   1.00 17.51 ?  59  ASN   B OD1  1 
ATOM   4717 N ND2  . ASN   B 1 59  ? 60.587 -15.527 5.427   1.00 18.31 ?  59  ASN   B ND2  1 
ATOM   4718 H H    . ASN   B 1 59  ? 59.624 -17.180 0.353   1.00 18.07 ?  59  ASN   B H    1 
ATOM   4719 H HA   . ASN   B 1 59  ? 58.977 -16.737 2.285   1.00 17.91 ?  59  ASN   B HA   1 
ATOM   4720 H HB2  . ASN   B 1 59  ? 61.341 -16.968 2.951   1.00 19.61 ?  59  ASN   B HB2  1 
ATOM   4721 H HB3  . ASN   B 1 59  ? 61.274 -15.389 3.112   1.00 19.61 ?  59  ASN   B HB3  1 
ATOM   4722 H HD21 . ASN   B 1 59  ? 60.280 -15.583 6.232   1.00 21.98 ?  59  ASN   B HD21 1 
ATOM   4723 H HD22 . ASN   B 1 59  ? 61.167 -14.926 5.232   1.00 21.98 ?  59  ASN   B HD22 1 
ATOM   4724 N N    . ALA   B 1 60  ? 59.035 -14.081 0.792   1.00 14.29 ?  60  ALA   B N    1 
ATOM   4725 C CA   . ALA   B 1 60  ? 58.435 -12.752 0.720   1.00 14.06 ?  60  ALA   B CA   1 
ATOM   4726 C C    . ALA   B 1 60  ? 56.964 -12.780 1.117   1.00 13.06 ?  60  ALA   B C    1 
ATOM   4727 O O    . ALA   B 1 60  ? 56.456 -11.832 1.732   1.00 13.55 ?  60  ALA   B O    1 
ATOM   4728 C CB   . ALA   B 1 60  ? 58.602 -12.181 -0.687  1.00 15.21 ?  60  ALA   B CB   1 
ATOM   4729 H H    . ALA   B 1 60  ? 59.329 -14.392 0.046   1.00 17.15 ?  60  ALA   B H    1 
ATOM   4730 H HA   . ALA   B 1 60  ? 58.898 -12.173 1.342   1.00 16.88 ?  60  ALA   B HA   1 
ATOM   4731 H HB1  . ALA   B 1 60  ? 58.203 -11.302 -0.714  1.00 18.25 ?  60  ALA   B HB1  1 
ATOM   4732 H HB2  . ALA   B 1 60  ? 59.551 -12.124 -0.891  1.00 18.25 ?  60  ALA   B HB2  1 
ATOM   4733 H HB3  . ALA   B 1 60  ? 58.164 -12.770 -1.320  1.00 18.25 ?  60  ALA   B HB3  1 
ATOM   4734 N N    . MET   B 1 61  ? 56.259 -13.858 0.769   1.00 12.66 ?  61  MET   B N    1 
ATOM   4735 C CA   . MET   B 1 61  ? 54.861 -13.978 1.160   1.00 12.29 ?  61  MET   B CA   1 
ATOM   4736 C C    . MET   B 1 61  ? 54.715 -13.991 2.682   1.00 12.34 ?  61  MET   B C    1 
ATOM   4737 O O    . MET   B 1 61  ? 53.818 -13.340 3.234   1.00 12.38 ?  61  MET   B O    1 
ATOM   4738 C CB   . MET   B 1 61  ? 54.280 -15.248 0.530   1.00 12.39 ?  61  MET   B CB   1 
ATOM   4739 C CG   . MET   B 1 61  ? 52.834 -15.541 0.927   1.00 11.99 ?  61  MET   B CG   1 
ATOM   4740 S SD   . MET   B 1 61  ? 52.191 -17.045 0.170   1.00 12.86 ?  61  MET   B SD   1 
ATOM   4741 C CE   . MET   B 1 61  ? 51.937 -16.469 -1.506  1.00 14.30 ?  61  MET   B CE   1 
ATOM   4742 H H    . MET   B 1 61  ? 56.563 -14.530 0.317   1.00 15.20 ?  61  MET   B H    1 
ATOM   4743 H HA   . MET   B 1 61  ? 54.368 -13.225 0.799   1.00 14.76 ?  61  MET   B HA   1 
ATOM   4744 H HB2  . MET   B 1 61  ? 54.302 -15.160 -0.437  1.00 14.88 ?  61  MET   B HB2  1 
ATOM   4745 H HB3  . MET   B 1 61  ? 54.815 -16.009 0.801   1.00 14.88 ?  61  MET   B HB3  1 
ATOM   4746 H HG2  . MET   B 1 61  ? 52.779 -15.648 1.892   1.00 14.39 ?  61  MET   B HG2  1 
ATOM   4747 H HG3  . MET   B 1 61  ? 52.269 -14.797 0.650   1.00 14.39 ?  61  MET   B HG3  1 
ATOM   4748 H HE1  . MET   B 1 61  ? 51.560 -17.188 -2.036  1.00 17.17 ?  61  MET   B HE1  1 
ATOM   4749 H HE2  . MET   B 1 61  ? 51.321 -15.714 -1.494  1.00 17.17 ?  61  MET   B HE2  1 
ATOM   4750 H HE3  . MET   B 1 61  ? 52.787 -16.191 -1.878  1.00 17.17 ?  61  MET   B HE3  1 
ATOM   4751 N N    . GLN   B 1 62  ? 55.594 -14.713 3.382   1.00 12.46 ?  62  GLN   B N    1 
ATOM   4752 C CA   . GLN   B 1 62  ? 55.494 -14.769 4.838   1.00 12.89 ?  62  GLN   B CA   1 
ATOM   4753 C C    . GLN   B 1 62  ? 55.776 -13.410 5.469   1.00 12.98 ?  62  GLN   B C    1 
ATOM   4754 O O    . GLN   B 1 62  ? 55.087 -13.007 6.412   1.00 13.63 ?  62  GLN   B O    1 
ATOM   4755 C CB   . GLN   B 1 62  ? 56.451 -15.816 5.405   1.00 12.88 ?  62  GLN   B CB   1 
ATOM   4756 C CG   . GLN   B 1 62  ? 56.223 -16.091 6.884   1.00 13.04 ?  62  GLN   B CG   1 
ATOM   4757 C CD   . GLN   B 1 62  ? 54.848 -16.678 7.127   1.00 12.85 ?  62  GLN   B CD   1 
ATOM   4758 O OE1  . GLN   B 1 62  ? 54.586 -17.826 6.762   1.00 13.34 ?  62  GLN   B OE1  1 
ATOM   4759 N NE2  . GLN   B 1 62  ? 53.944 -15.884 7.699   1.00 13.29 ?  62  GLN   B NE2  1 
ATOM   4760 H H    . GLN   B 1 62  ? 56.234 -15.174 3.042   1.00 14.96 ?  62  GLN   B H    1 
ATOM   4761 H HA   . GLN   B 1 62  ? 54.588 -15.027 5.078   1.00 15.47 ?  62  GLN   B HA   1 
ATOM   4762 H HB2  . GLN   B 1 62  ? 56.336 -16.648 4.924   1.00 15.46 ?  62  GLN   B HB2  1 
ATOM   4763 H HB3  . GLN   B 1 62  ? 57.364 -15.497 5.299   1.00 15.46 ?  62  GLN   B HB3  1 
ATOM   4764 H HG2  . GLN   B 1 62  ? 56.885 -16.732 7.194   1.00 15.65 ?  62  GLN   B HG2  1 
ATOM   4765 H HG3  . GLN   B 1 62  ? 56.299 -15.265 7.384   1.00 15.65 ?  62  GLN   B HG3  1 
ATOM   4766 H HE21 . GLN   B 1 62  ? 54.161 -15.082 7.927   1.00 15.95 ?  62  GLN   B HE21 1 
ATOM   4767 H HE22 . GLN   B 1 62  ? 53.150 -16.173 7.848   1.00 15.95 ?  62  GLN   B HE22 1 
ATOM   4768 N N    . VAL   B 1 63  ? 56.791 -12.696 4.978   1.00 13.54 ?  63  VAL   B N    1 
ATOM   4769 C CA   . VAL   B 1 63  ? 57.097 -11.378 5.531   1.00 14.70 ?  63  VAL   B CA   1 
ATOM   4770 C C    . VAL   B 1 63  ? 55.905 -10.444 5.352   1.00 13.71 ?  63  VAL   B C    1 
ATOM   4771 O O    . VAL   B 1 63  ? 55.491 -9.740  6.285   1.00 14.63 ?  63  VAL   B O    1 
ATOM   4772 C CB   . VAL   B 1 63  ? 58.387 -10.823 4.904   1.00 15.96 ?  63  VAL   B CB   1 
ATOM   4773 C CG1  . VAL   B 1 63  ? 58.615 -9.381  5.340   1.00 16.60 ?  63  VAL   B CG1  1 
ATOM   4774 C CG2  . VAL   B 1 63  ? 59.570 -11.698 5.302   1.00 16.51 ?  63  VAL   B CG2  1 
ATOM   4775 H H    . VAL   B 1 63  ? 57.299 -12.949 4.329   1.00 16.26 ?  63  VAL   B H    1 
ATOM   4776 H HA   . VAL   B 1 63  ? 57.253 -11.478 6.478   1.00 17.65 ?  63  VAL   B HA   1 
ATOM   4777 H HB   . VAL   B 1 63  ? 58.317 -10.848 3.936   1.00 19.16 ?  63  VAL   B HB   1 
ATOM   4778 H HG11 . VAL   B 1 63  ? 59.533 -9.136  5.150   1.00 19.92 ?  63  VAL   B HG11 1 
ATOM   4779 H HG12 . VAL   B 1 63  ? 58.009 -8.806  4.852   1.00 19.92 ?  63  VAL   B HG12 1 
ATOM   4780 H HG13 . VAL   B 1 63  ? 58.447 -9.314  6.294   1.00 19.92 ?  63  VAL   B HG13 1 
ATOM   4781 H HG21 . VAL   B 1 63  ? 60.382 -11.326 4.922   1.00 19.82 ?  63  VAL   B HG21 1 
ATOM   4782 H HG22 . VAL   B 1 63  ? 59.639 -11.711 6.273   1.00 19.82 ?  63  VAL   B HG22 1 
ATOM   4783 H HG23 . VAL   B 1 63  ? 59.430 -12.598 4.971   1.00 19.82 ?  63  VAL   B HG23 1 
ATOM   4784 N N    . GLU   B 1 64  ? 55.334 -10.429 4.147   1.00 13.49 ?  64  GLU   B N    1 
ATOM   4785 C CA   . GLU   B 1 64  ? 54.166 -9.592  3.877   1.00 13.11 ?  64  GLU   B CA   1 
ATOM   4786 C C    . GLU   B 1 64  ? 52.987 -9.995  4.756   1.00 12.45 ?  64  GLU   B C    1 
ATOM   4787 O O    . GLU   B 1 64  ? 52.239 -9.136  5.253   1.00 13.28 ?  64  GLU   B O    1 
ATOM   4788 C CB   . GLU   B 1 64  ? 53.798 -9.745  2.400   1.00 13.49 ?  64  GLU   B CB   1 
ATOM   4789 C CG   . GLU   B 1 64  ? 52.540 -9.006  1.965   1.00 13.39 ?  64  GLU   B CG   1 
ATOM   4790 C CD   . GLU   B 1 64  ? 52.009 -9.504  0.628   1.00 14.17 ?  64  GLU   B CD   1 
ATOM   4791 O OE1  . GLU   B 1 64  ? 52.191 -10.713 0.311   1.00 14.65 ?  64  GLU   B OE1  1 
ATOM   4792 O OE2  . GLU   B 1 64  ? 51.385 -8.691  -0.098  1.00 14.88 -1 64  GLU   B OE2  1 
ATOM   4793 H H    . GLU   B 1 64  ? 55.606 -10.888 3.465   1.00 16.20 ?  64  GLU   B H    1 
ATOM   4794 H HA   . GLU   B 1 64  ? 54.381 -8.664  4.049   1.00 15.73 ?  64  GLU   B HA   1 
ATOM   4795 H HB2  . GLU   B 1 64  ? 54.527 -9.402  1.858   1.00 16.20 ?  64  GLU   B HB2  1 
ATOM   4796 H HB3  . GLU   B 1 64  ? 53.662 -10.682 2.208   1.00 16.20 ?  64  GLU   B HB3  1 
ATOM   4797 H HG2  . GLU   B 1 64  ? 51.836 -9.131  2.624   1.00 16.07 ?  64  GLU   B HG2  1 
ATOM   4798 H HG3  . GLU   B 1 64  ? 52.738 -8.060  1.874   1.00 16.07 ?  64  GLU   B HG3  1 
ATOM   4799 N N    . SER   B 1 65  ? 52.802 -11.304 4.943   1.00 12.30 ?  65  SER   B N    1 
ATOM   4800 C CA   . SER   B 1 65  ? 51.694 -11.814 5.740   1.00 12.55 ?  65  SER   B CA   1 
ATOM   4801 C C    . SER   B 1 65  ? 51.826 -11.416 7.205   1.00 12.82 ?  65  SER   B C    1 
ATOM   4802 O O    . SER   B 1 65  ? 50.826 -11.053 7.843   1.00 13.12 ?  65  SER   B O    1 
ATOM   4803 C CB   . SER   B 1 65  ? 51.614 -13.336 5.606   1.00 12.77 ?  65  SER   B CB   1 
ATOM   4804 O OG   . SER   B 1 65  ? 51.271 -13.732 4.286   1.00 13.19 ?  65  SER   B OG   1 
ATOM   4805 H H    . SER   B 1 65  ? 53.309 -11.924 4.618   1.00 14.76 ?  65  SER   B H    1 
ATOM   4806 H HA   . SER   B 1 65  ? 50.863 -11.442 5.402   1.00 15.07 ?  65  SER   B HA   1 
ATOM   4807 H HB2  . SER   B 1 65  ? 52.474 -13.718 5.829   1.00 15.33 ?  65  SER   B HB2  1 
ATOM   4808 H HB3  . SER   B 1 65  ? 50.935 -13.669 6.218   1.00 15.33 ?  65  SER   B HB3  1 
ATOM   4809 H HG   . SER   B 1 65  ? 51.842 -13.439 3.739   1.00 15.84 ?  65  SER   B HG   1 
ATOM   4810 N N    . ASP   B 1 66  ? 53.035 -11.512 7.769   1.00 12.85 ?  66  ASP   B N    1 
ATOM   4811 C CA   . ASP   B 1 66  ? 53.223 -11.127 9.166   1.00 13.11 ?  66  ASP   B CA   1 
ATOM   4812 C C    . ASP   B 1 66  ? 52.908 -9.651  9.369   1.00 13.37 ?  66  ASP   B C    1 
ATOM   4813 O O    . ASP   B 1 66  ? 52.333 -9.264  10.393  1.00 14.07 ?  66  ASP   B O    1 
ATOM   4814 C CB   . ASP   B 1 66  ? 54.652 -11.439 9.619   1.00 14.61 ?  66  ASP   B CB   1 
ATOM   4815 C CG   . ASP   B 1 66  ? 54.922 -12.934 9.765   1.00 16.53 ?  66  ASP   B CG   1 
ATOM   4816 O OD1  . ASP   B 1 66  ? 53.972 -13.741 9.686   1.00 17.38 ?  66  ASP   B OD1  1 
ATOM   4817 O OD2  . ASP   B 1 66  ? 56.099 -13.307 9.968   1.00 19.40 -1 66  ASP   B OD2  1 
ATOM   4818 H H    . ASP   B 1 66  ? 53.741 -11.797 7.375   1.00 15.43 ?  66  ASP   B H    1 
ATOM   4819 H HA   . ASP   B 1 66  ? 52.616 -11.632 9.724   1.00 15.73 ?  66  ASP   B HA   1 
ATOM   4820 H HB2  . ASP   B 1 66  ? 55.276 -11.093 8.964   1.00 17.53 ?  66  ASP   B HB2  1 
ATOM   4821 H HB3  . ASP   B 1 66  ? 54.810 -11.016 10.481  1.00 17.53 ?  66  ASP   B HB3  1 
ATOM   4822 N N    . ASP   B 1 67  ? 53.288 -8.807  8.407   1.00 13.37 ?  67  ASP   B N    1 
ATOM   4823 C CA   . ASP   B 1 67  ? 52.941 -7.396  8.494   1.00 14.13 ?  67  ASP   B CA   1 
ATOM   4824 C C    . ASP   B 1 67  ? 51.429 -7.191  8.413   1.00 13.92 ?  67  ASP   B C    1 
ATOM   4825 O O    . ASP   B 1 67  ? 50.868 -6.383  9.160   1.00 14.54 ?  67  ASP   B O    1 
ATOM   4826 C CB   . ASP   B 1 67  ? 53.656 -6.623  7.393   1.00 15.39 ?  67  ASP   B CB   1 
ATOM   4827 C CG   . ASP   B 1 67  ? 53.227 -5.178  7.349   1.00 16.59 ?  67  ASP   B CG   1 
ATOM   4828 O OD1  . ASP   B 1 67  ? 53.707 -4.367  8.174   1.00 17.68 ?  67  ASP   B OD1  1 
ATOM   4829 O OD2  . ASP   B 1 67  ? 52.375 -4.866  6.505   1.00 17.76 -1 67  ASP   B OD2  1 
ATOM   4830 H H    . ASP   B 1 67  ? 53.745 -9.026  7.710   1.00 16.05 ?  67  ASP   B H    1 
ATOM   4831 H HA   . ASP   B 1 67  ? 53.249 -7.047  9.343   1.00 16.96 ?  67  ASP   B HA   1 
ATOM   4832 H HB2  . ASP   B 1 67  ? 54.616 -6.647  7.552   1.00 18.47 ?  67  ASP   B HB2  1 
ATOM   4833 H HB3  . ASP   B 1 67  ? 53.459 -7.035  6.532   1.00 18.47 ?  67  ASP   B HB3  1 
ATOM   4834 N N    . TYR   B 1 68  ? 50.748 -7.924  7.525   1.00 13.46 ?  68  TYR   B N    1 
ATOM   4835 C CA   . TYR   B 1 68  ? 49.290 -7.841  7.452   1.00 14.32 ?  68  TYR   B CA   1 
ATOM   4836 C C    . TYR   B 1 68  ? 48.652 -8.182  8.794   1.00 13.89 ?  68  TYR   B C    1 
ATOM   4837 O O    . TYR   B 1 68  ? 47.718 -7.503  9.240   1.00 14.84 ?  68  TYR   B O    1 
ATOM   4838 C CB   . TYR   B 1 68  ? 48.755 -8.768  6.355   1.00 15.16 ?  68  TYR   B CB   1 
ATOM   4839 C CG   . TYR   B 1 68  ? 47.247 -8.920  6.406   1.00 16.25 ?  68  TYR   B CG   1 
ATOM   4840 C CD1  . TYR   B 1 68  ? 46.653 -9.874  7.228   1.00 17.47 ?  68  TYR   B CD1  1 
ATOM   4841 C CD2  . TYR   B 1 68  ? 46.419 -8.083  5.678   1.00 17.51 ?  68  TYR   B CD2  1 
ATOM   4842 C CE1  . TYR   B 1 68  ? 45.286 -9.995  7.314   1.00 18.53 ?  68  TYR   B CE1  1 
ATOM   4843 C CE2  . TYR   B 1 68  ? 45.036 -8.213  5.745   1.00 17.93 ?  68  TYR   B CE2  1 
ATOM   4844 C CZ   . TYR   B 1 68  ? 44.490 -9.164  6.569   1.00 18.58 ?  68  TYR   B CZ   1 
ATOM   4845 O OH   . TYR   B 1 68  ? 43.124 -9.285  6.660   1.00 20.03 ?  68  TYR   B OH   1 
ATOM   4846 H H    . TYR   B 1 68  ? 51.105 -8.477  6.966   1.00 16.16 ?  68  TYR   B H    1 
ATOM   4847 H HA   . TYR   B 1 68  ? 49.044 -6.933  7.231   1.00 17.19 ?  68  TYR   B HA   1 
ATOM   4848 H HB2  . TYR   B 1 68  ? 48.984 -8.397  5.492   1.00 18.20 ?  68  TYR   B HB2  1 
ATOM   4849 H HB3  . TYR   B 1 68  ? 49.147 -9.646  6.461   1.00 18.20 ?  68  TYR   B HB3  1 
ATOM   4850 H HD1  . TYR   B 1 68  ? 47.190 -10.442 7.736   1.00 20.97 ?  68  TYR   B HD1  1 
ATOM   4851 H HD2  . TYR   B 1 68  ? 46.791 -7.432  5.135   1.00 21.02 ?  68  TYR   B HD2  1 
ATOM   4852 H HE1  . TYR   B 1 68  ? 44.901 -10.655 7.855   1.00 22.25 ?  68  TYR   B HE1  1 
ATOM   4853 H HE2  . TYR   B 1 68  ? 44.481 -7.649  5.255   1.00 21.52 ?  68  TYR   B HE2  1 
ATOM   4854 H HH   . TYR   B 1 68  ? 42.735 -8.738  6.146   1.00 24.04 ?  68  TYR   B HH   1 
ATOM   4855 N N    . ILE   B 1 69  ? 49.131 -9.249  9.441   1.00 13.72 ?  69  ILE   B N    1 
ATOM   4856 C CA   . ILE   B 1 69  ? 48.572 -9.678  10.720  1.00 14.50 ?  69  ILE   B CA   1 
ATOM   4857 C C    . ILE   B 1 69  ? 48.829 -8.636  11.799  1.00 14.20 ?  69  ILE   B C    1 
ATOM   4858 O O    . ILE   B 1 69  ? 47.964 -8.364  12.637  1.00 14.50 ?  69  ILE   B O    1 
ATOM   4859 C CB   . ILE   B 1 69  ? 49.149 -11.055 11.108  1.00 15.24 ?  69  ILE   B CB   1 
ATOM   4860 C CG1  . ILE   B 1 69  ? 48.617 -12.152 10.178  1.00 15.78 ?  69  ILE   B CG1  1 
ATOM   4861 C CG2  . ILE   B 1 69  ? 48.860 -11.379 12.568  1.00 16.34 ?  69  ILE   B CG2  1 
ATOM   4862 C CD1  . ILE   B 1 69  ? 47.139 -12.454 10.331  1.00 15.97 ?  69  ILE   B CD1  1 
ATOM   4863 H H    . ILE   B 1 69  ? 49.775 -9.743  9.159   1.00 16.47 ?  69  ILE   B H    1 
ATOM   4864 H HA   . ILE   B 1 69  ? 47.614 -9.776  10.627  1.00 17.41 ?  69  ILE   B HA   1 
ATOM   4865 H HB   . ILE   B 1 69  ? 50.114 -11.016 11.001  1.00 18.29 ?  69  ILE   B HB   1 
ATOM   4866 H HG12 . ILE   B 1 69  ? 48.770 -11.876 9.261   1.00 18.94 ?  69  ILE   B HG12 1 
ATOM   4867 H HG13 . ILE   B 1 69  ? 49.106 -12.971 10.357  1.00 18.94 ?  69  ILE   B HG13 1 
ATOM   4868 H HG21 . ILE   B 1 69  ? 48.999 -12.329 12.711  1.00 19.62 ?  69  ILE   B HG21 1 
ATOM   4869 H HG22 . ILE   B 1 69  ? 49.463 -10.872 13.134  1.00 19.62 ?  69  ILE   B HG22 1 
ATOM   4870 H HG23 . ILE   B 1 69  ? 47.940 -11.148 12.766  1.00 19.62 ?  69  ILE   B HG23 1 
ATOM   4871 H HD11 . ILE   B 1 69  ? 46.905 -13.173 9.726   1.00 19.16 ?  69  ILE   B HD11 1 
ATOM   4872 H HD12 . ILE   B 1 69  ? 46.962 -12.723 11.246  1.00 19.16 ?  69  ILE   B HD12 1 
ATOM   4873 H HD13 . ILE   B 1 69  ? 46.628 -11.660 10.114  1.00 19.16 ?  69  ILE   B HD13 1 
ATOM   4874 N N    . ALA   B 1 70  ? 50.024 -8.047  11.816  1.00 14.25 ?  70  ALA   B N    1 
ATOM   4875 C CA   . ALA   B 1 70  ? 50.309 -7.011  12.805  1.00 14.13 ?  70  ALA   B CA   1 
ATOM   4876 C C    . ALA   B 1 70  ? 49.314 -5.865  12.699  1.00 14.17 ?  70  ALA   B C    1 
ATOM   4877 O O    . ALA   B 1 70  ? 48.869 -5.322  13.714  1.00 14.50 ?  70  ALA   B O    1 
ATOM   4878 C CB   . ALA   B 1 70  ? 51.737 -6.497  12.634  1.00 14.65 ?  70  ALA   B CB   1 
ATOM   4879 H H    . ALA   B 1 70  ? 50.665 -8.223  11.281  1.00 17.11 ?  70  ALA   B H    1 
ATOM   4880 H HA   . ALA   B 1 70  ? 50.232 -7.388  13.694  1.00 16.96 ?  70  ALA   B HA   1 
ATOM   4881 H HB1  . ALA   B 1 70  ? 51.920 -5.834  13.319  1.00 17.59 ?  70  ALA   B HB1  1 
ATOM   4882 H HB2  . ALA   B 1 70  ? 52.352 -7.243  12.726  1.00 17.59 ?  70  ALA   B HB2  1 
ATOM   4883 H HB3  . ALA   B 1 70  ? 51.830 -6.100  11.755  1.00 17.59 ?  70  ALA   B HB3  1 
ATOM   4884 N N    . THR   B 1 71  ? 48.945 -5.493  11.475  1.00 14.63 ?  71  THR   B N    1 
ATOM   4885 C CA   . THR   B 1 71  ? 48.051 -4.358  11.263  1.00 15.75 ?  71  THR   B CA   1 
ATOM   4886 C C    . THR   B 1 71  ? 46.583 -4.723  11.467  1.00 16.30 ?  71  THR   B C    1 
ATOM   4887 O O    . THR   B 1 71  ? 45.803 -3.905  11.975  1.00 17.85 ?  71  THR   B O    1 
ATOM   4888 C CB   . THR   B 1 71  ? 48.276 -3.789  9.858   1.00 17.55 ?  71  THR   B CB   1 
ATOM   4889 O OG1  . THR   B 1 71  ? 49.610 -3.274  9.763   1.00 19.81 ?  71  THR   B OG1  1 
ATOM   4890 C CG2  . THR   B 1 71  ? 47.275 -2.684  9.532   1.00 18.66 ?  71  THR   B CG2  1 
ATOM   4891 H H    . THR   B 1 71  ? 49.201 -5.874  10.752  1.00 17.56 ?  71  THR   B H    1 
ATOM   4892 H HA   . THR   B 1 71  ? 48.273 -3.657  11.896  1.00 18.91 ?  71  THR   B HA   1 
ATOM   4893 H HB   . THR   B 1 71  ? 48.172 -4.492  9.201   1.00 21.06 ?  71  THR   B HB   1 
ATOM   4894 H HG1  . THR   B 1 71  ? 49.746 -2.943  8.997   1.00 23.78 ?  71  THR   B HG1  1 
ATOM   4895 H HG21 . THR   B 1 71  ? 47.581 -2.173  8.763   1.00 22.40 ?  71  THR   B HG21 1 
ATOM   4896 H HG22 . THR   B 1 71  ? 46.409 -3.067  9.328   1.00 22.40 ?  71  THR   B HG22 1 
ATOM   4897 H HG23 . THR   B 1 71  ? 47.187 -2.081  10.288  1.00 22.40 ?  71  THR   B HG23 1 
ATOM   4898 N N    . ASN   B 1 72  ? 46.186 -5.936  11.074  1.00 15.98 ?  72  ASN   B N    1 
ATOM   4899 C CA   . ASN   B 1 72  ? 44.781 -6.295  10.949  1.00 16.44 ?  72  ASN   B CA   1 
ATOM   4900 C C    . ASN   B 1 72  ? 44.315 -7.397  11.887  1.00 16.85 ?  72  ASN   B C    1 
ATOM   4901 O O    . ASN   B 1 72  ? 43.099 -7.559  12.057  1.00 18.04 ?  72  ASN   B O    1 
ATOM   4902 C CB   . ASN   B 1 72  ? 44.471 -6.722  9.505   1.00 17.39 ?  72  ASN   B CB   1 
ATOM   4903 C CG   . ASN   B 1 72  ? 44.746 -5.622  8.514   1.00 18.36 ?  72  ASN   B CG   1 
ATOM   4904 O OD1  . ASN   B 1 72  ? 45.758 -5.631  7.807   1.00 19.30 ?  72  ASN   B OD1  1 
ATOM   4905 N ND2  . ASN   B 1 72  ? 43.866 -4.640  8.481   1.00 20.03 ?  72  ASN   B ND2  1 
ATOM   4906 H H    . ASN   B 1 72  ? 46.727 -6.576  10.872  1.00 19.18 ?  72  ASN   B H    1 
ATOM   4907 H HA   . ASN   B 1 72  ? 44.249 -5.510  11.140  1.00 19.73 ?  72  ASN   B HA   1 
ATOM   4908 H HB2  . ASN   B 1 72  ? 45.029 -7.482  9.274   1.00 20.87 ?  72  ASN   B HB2  1 
ATOM   4909 H HB3  . ASN   B 1 72  ? 43.536 -6.962  9.442   1.00 20.87 ?  72  ASN   B HB3  1 
ATOM   4910 H HD21 . ASN   B 1 72  ? 43.970 -3.984  7.933   1.00 24.04 ?  72  ASN   B HD21 1 
ATOM   4911 H HD22 . ASN   B 1 72  ? 43.171 -4.664  8.991   1.00 24.04 ?  72  ASN   B HD22 1 
ATOM   4912 N N    . GLY   B 1 73  ? 45.223 -8.151  12.499  1.00 16.46 ?  73  GLY   B N    1 
ATOM   4913 C CA   . GLY   B 1 73  ? 44.834 -9.291  13.293  1.00 16.07 ?  73  GLY   B CA   1 
ATOM   4914 C C    . GLY   B 1 73  ? 44.458 -10.472 12.423  1.00 14.68 ?  73  GLY   B C    1 
ATOM   4915 O O    . GLY   B 1 73  ? 44.444 -10.387 11.192  1.00 14.35 ?  73  GLY   B O    1 
ATOM   4916 H H    . GLY   B 1 73  ? 46.076 -8.017  12.469  1.00 19.76 ?  73  GLY   B H    1 
ATOM   4917 H HA2  . GLY   B 1 73  ? 45.570 -9.552  13.870  1.00 19.28 ?  73  GLY   B HA2  1 
ATOM   4918 H HA3  . GLY   B 1 73  ? 44.075 -9.057  13.848  1.00 19.28 ?  73  GLY   B HA3  1 
ATOM   4919 N N    . PRO   B 1 74  ? 44.147 -11.599 13.060  1.00 15.02 ?  74  PRO   B N    1 
ATOM   4920 C CA   . PRO   B 1 74  ? 43.894 -12.833 12.313  1.00 14.41 ?  74  PRO   B CA   1 
ATOM   4921 C C    . PRO   B 1 74  ? 42.593 -12.778 11.524  1.00 13.54 ?  74  PRO   B C    1 
ATOM   4922 O O    . PRO   B 1 74  ? 41.648 -12.045 11.846  1.00 14.69 ?  74  PRO   B O    1 
ATOM   4923 C CB   . PRO   B 1 74  ? 43.823 -13.899 13.414  1.00 15.65 ?  74  PRO   B CB   1 
ATOM   4924 C CG   . PRO   B 1 74  ? 43.393 -13.152 14.633  1.00 17.18 ?  74  PRO   B CG   1 
ATOM   4925 C CD   . PRO   B 1 74  ? 44.051 -11.807 14.516  1.00 16.62 ?  74  PRO   B CD   1 
ATOM   4926 H HA   . PRO   B 1 74  ? 44.638 -13.025 11.715  1.00 17.30 ?  74  PRO   B HA   1 
ATOM   4927 H HB2  . PRO   B 1 74  ? 43.171 -14.575 13.171  1.00 18.78 ?  74  PRO   B HB2  1 
ATOM   4928 H HB3  . PRO   B 1 74  ? 44.699 -14.296 13.542  1.00 18.78 ?  74  PRO   B HB3  1 
ATOM   4929 H HG2  . PRO   B 1 74  ? 42.426 -13.066 14.633  1.00 20.62 ?  74  PRO   B HG2  1 
ATOM   4930 H HG3  . PRO   B 1 74  ? 43.698 -13.620 15.423  1.00 20.62 ?  74  PRO   B HG3  1 
ATOM   4931 H HD2  . PRO   B 1 74  ? 43.493 -11.123 14.926  1.00 19.95 ?  74  PRO   B HD2  1 
ATOM   4932 H HD3  . PRO   B 1 74  ? 44.936 -11.826 14.910  1.00 19.95 ?  74  PRO   B HD3  1 
ATOM   4933 N N    . LEU   B 1 75  ? 42.561 -13.591 10.470  1.00 12.78 ?  75  LEU   B N    1 
ATOM   4934 C CA   . LEU   B 1 75  ? 41.348 -13.807 9.704   1.00 13.08 ?  75  LEU   B CA   1 
ATOM   4935 C C    . LEU   B 1 75  ? 40.374 -14.668 10.508  1.00 13.41 ?  75  LEU   B C    1 
ATOM   4936 O O    . LEU   B 1 75  ? 40.714 -15.229 11.550  1.00 14.57 ?  75  LEU   B O    1 
ATOM   4937 C CB   . LEU   B 1 75  ? 41.669 -14.522 8.390   1.00 13.11 ?  75  LEU   B CB   1 
ATOM   4938 C CG   . LEU   B 1 75  ? 42.520 -13.772 7.360   1.00 14.91 ?  75  LEU   B CG   1 
ATOM   4939 C CD1  . LEU   B 1 75  ? 42.704 -14.599 6.087   1.00 16.24 ?  75  LEU   B CD1  1 
ATOM   4940 C CD2  . LEU   B 1 75  ? 41.940 -12.420 7.030   1.00 18.12 ?  75  LEU   B CD2  1 
ATOM   4941 H H    . LEU   B 1 75  ? 43.239 -14.037 10.173  1.00 15.34 ?  75  LEU   B H    1 
ATOM   4942 H HA   . LEU   B 1 75  ? 40.925 -12.958 9.504   1.00 15.71 ?  75  LEU   B HA   1 
ATOM   4943 H HB2  . LEU   B 1 75  ? 42.144 -15.343 8.600   1.00 15.74 ?  75  LEU   B HB2  1 
ATOM   4944 H HB3  . LEU   B 1 75  ? 40.833 -14.746 7.952   1.00 15.74 ?  75  LEU   B HB3  1 
ATOM   4945 H HG   . LEU   B 1 75  ? 43.401 -13.626 7.738   1.00 17.90 ?  75  LEU   B HG   1 
ATOM   4946 H HD11 . LEU   B 1 75  ? 43.251 -14.095 5.459   1.00 19.49 ?  75  LEU   B HD11 1 
ATOM   4947 H HD12 . LEU   B 1 75  ? 43.146 -15.433 6.310   1.00 19.49 ?  75  LEU   B HD12 1 
ATOM   4948 H HD13 . LEU   B 1 75  ? 41.836 -14.777 5.695   1.00 19.49 ?  75  LEU   B HD13 1 
ATOM   4949 H HD21 . LEU   B 1 75  ? 42.449 -12.026 6.305   1.00 21.75 ?  75  LEU   B HD21 1 
ATOM   4950 H HD22 . LEU   B 1 75  ? 41.015 -12.531 6.765   1.00 21.75 ?  75  LEU   B HD22 1 
ATOM   4951 H HD23 . LEU   B 1 75  ? 41.994 -11.853 7.817   1.00 21.75 ?  75  LEU   B HD23 1 
ATOM   4952 N N    . LYS   B 1 76  ? 39.142 -14.768 10.003  1.00 14.83 ?  76  LYS   B N    1 
ATOM   4953 C CA   . LYS   B 1 76  ? 38.161 -15.734 10.482  1.00 16.04 ?  76  LYS   B CA   1 
ATOM   4954 C C    . LYS   B 1 76  ? 38.249 -17.004 9.639   1.00 14.38 ?  76  LYS   B C    1 
ATOM   4955 O O    . LYS   B 1 76  ? 38.520 -16.943 8.441   1.00 14.18 ?  76  LYS   B O    1 
ATOM   4956 C CB   . LYS   B 1 76  ? 36.739 -15.172 10.317  1.00 18.65 ?  76  LYS   B CB   1 
ATOM   4957 C CG   . LYS   B 1 76  ? 36.465 -13.785 10.920  1.00 20.89 ?  76  LYS   B CG   1 
ATOM   4958 C CD   . LYS   B 1 76  ? 35.046 -13.282 10.588  1.00 22.11 ?  76  LYS   B CD   1 
ATOM   4959 C CE   . LYS   B 1 76  ? 34.788 -11.900 11.174  1.00 24.24 ?  76  LYS   B CE   1 
ATOM   4960 N NZ   . LYS   B 1 76  ? 33.468 -11.334 10.771  1.00 24.98 ?  76  LYS   B NZ   1 
ATOM   4961 H H    . LYS   B 1 76  ? 38.848 -14.274 9.366   1.00 17.80 ?  76  LYS   B H    1 
ATOM   4962 H HA   . LYS   B 1 76  ? 38.321 -15.956 11.413  1.00 19.25 ?  76  LYS   B HA   1 
ATOM   4963 H HB2  . LYS   B 1 76  ? 36.545 -15.116 9.368   1.00 22.39 ?  76  LYS   B HB2  1 
ATOM   4964 H HB3  . LYS   B 1 76  ? 36.119 -15.791 10.734  1.00 22.39 ?  76  LYS   B HB3  1 
ATOM   4965 H HG2  . LYS   B 1 76  ? 36.555 -13.835 11.884  1.00 25.07 ?  76  LYS   B HG2  1 
ATOM   4966 H HG3  . LYS   B 1 76  ? 37.107 -13.151 10.557  1.00 25.07 ?  76  LYS   B HG3  1 
ATOM   4967 H HD2  . LYS   B 1 76  ? 34.946 -13.230 9.624   1.00 26.53 ?  76  LYS   B HD2  1 
ATOM   4968 H HD3  . LYS   B 1 76  ? 34.398 -13.899 10.959  1.00 26.53 ?  76  LYS   B HD3  1 
ATOM   4969 H HE2  . LYS   B 1 76  ? 34.807 -11.961 12.141  1.00 29.10 ?  76  LYS   B HE2  1 
ATOM   4970 H HE3  . LYS   B 1 76  ? 35.481 -11.294 10.866  1.00 29.10 ?  76  LYS   B HE3  1 
ATOM   4971 H HZ1  . LYS   B 1 76  ? 33.424 -11.258 9.885   1.00 29.98 ?  76  LYS   B HZ1  1 
ATOM   4972 H HZ2  . LYS   B 1 76  ? 32.809 -11.866 11.048  1.00 29.98 ?  76  LYS   B HZ2  1 
ATOM   4973 H HZ3  . LYS   B 1 76  ? 33.358 -10.528 11.135  1.00 29.98 ?  76  LYS   B HZ3  1 
ATOM   4974 N N    . VAL   B 1 77  ? 37.998 -18.162 10.261  1.00 15.02 ?  77  VAL   B N    1 
ATOM   4975 C CA   . VAL   B 1 77  ? 37.785 -19.371 9.470   1.00 15.24 ?  77  VAL   B CA   1 
ATOM   4976 C C    . VAL   B 1 77  ? 36.593 -19.134 8.555   1.00 14.09 ?  77  VAL   B C    1 
ATOM   4977 O O    . VAL   B 1 77  ? 35.528 -18.689 9.003   1.00 14.08 ?  77  VAL   B O    1 
ATOM   4978 C CB   . VAL   B 1 77  ? 37.580 -20.596 10.373  1.00 16.48 ?  77  VAL   B CB   1 
ATOM   4979 C CG1  . VAL   B 1 77  ? 37.291 -21.825 9.522   1.00 17.32 ?  77  VAL   B CG1  1 
ATOM   4980 C CG2  . VAL   B 1 77  ? 38.809 -20.827 11.253  1.00 17.99 ?  77  VAL   B CG2  1 
ATOM   4981 H H    . VAL   B 1 77  ? 37.945 -18.268 11.108  1.00 18.03 ?  77  VAL   B H    1 
ATOM   4982 H HA   . VAL   B 1 77  ? 38.561 -19.529 8.913   1.00 18.29 ?  77  VAL   B HA   1 
ATOM   4983 H HB   . VAL   B 1 77  ? 36.814 -20.441 10.950  1.00 19.79 ?  77  VAL   B HB   1 
ATOM   4984 H HG11 . VAL   B 1 77  ? 37.357 -22.614 10.080  1.00 20.79 ?  77  VAL   B HG11 1 
ATOM   4985 H HG12 . VAL   B 1 77  ? 36.392 -21.756 9.156   1.00 20.79 ?  77  VAL   B HG12 1 
ATOM   4986 H HG13 . VAL   B 1 77  ? 37.938 -21.871 8.804   1.00 20.79 ?  77  VAL   B HG13 1 
ATOM   4987 H HG21 . VAL   B 1 77  ? 38.668 -21.626 11.779  1.00 21.60 ?  77  VAL   B HG21 1 
ATOM   4988 H HG22 . VAL   B 1 77  ? 39.584 -20.932 10.682  1.00 21.60 ?  77  VAL   B HG22 1 
ATOM   4989 H HG23 . VAL   B 1 77  ? 38.924 -20.060 11.834  1.00 21.60 ?  77  VAL   B HG23 1 
ATOM   4990 N N    . GLY   B 1 78  ? 36.773 -19.407 7.263   1.00 13.50 ?  78  GLY   B N    1 
ATOM   4991 C CA   . GLY   B 1 78  ? 35.793 -19.084 6.254   1.00 13.16 ?  78  GLY   B CA   1 
ATOM   4992 C C    . GLY   B 1 78  ? 36.037 -17.767 5.553   1.00 12.43 ?  78  GLY   B C    1 
ATOM   4993 O O    . GLY   B 1 78  ? 35.356 -17.481 4.561   1.00 12.92 ?  78  GLY   B O    1 
ATOM   4994 H H    . GLY   B 1 78  ? 37.478 -19.788 6.947   1.00 16.21 ?  78  GLY   B H    1 
ATOM   4995 H HA2  . GLY   B 1 78  ? 35.782 -19.780 5.584   1.00 15.80 ?  78  GLY   B HA2  1 
ATOM   4996 H HA3  . GLY   B 1 78  ? 34.915 -19.041 6.665   1.00 15.80 ?  78  GLY   B HA3  1 
ATOM   4997 N N    . GLY   B 1 79  ? 36.996 -16.970 6.032   1.00 12.46 ?  79  GLY   B N    1 
ATOM   4998 C CA   . GLY   B 1 79  ? 37.289 -15.671 5.464   1.00 12.49 ?  79  GLY   B CA   1 
ATOM   4999 C C    . GLY   B 1 79  ? 38.530 -15.687 4.578   1.00 11.81 ?  79  GLY   B C    1 
ATOM   5000 O O    . GLY   B 1 79  ? 39.146 -16.722 4.330   1.00 12.28 ?  79  GLY   B O    1 
ATOM   5001 H H    . GLY   B 1 79  ? 37.503 -17.171 6.693   1.00 14.96 ?  79  GLY   B H    1 
ATOM   5002 H HA2  . GLY   B 1 79  ? 36.534 -15.368 4.930   1.00 14.99 ?  79  GLY   B HA2  1 
ATOM   5003 H HA3  . GLY   B 1 79  ? 37.435 -15.030 6.176   1.00 14.99 ?  79  GLY   B HA3  1 
ATOM   5004 N N    . SER   B 1 80  ? 38.893 -14.493 4.097   1.00 12.04 ?  80  SER   B N    1 
ATOM   5005 C CA   . SER   B 1 80  ? 40.007 -14.358 3.166   1.00 11.90 ?  80  SER   B CA   1 
ATOM   5006 C C    . SER   B 1 80  ? 40.586 -12.949 3.226   1.00 11.63 ?  80  SER   B C    1 
ATOM   5007 O O    . SER   B 1 80  ? 39.966 -12.016 3.741   1.00 13.00 ?  80  SER   B O    1 
ATOM   5008 C CB   . SER   B 1 80  ? 39.565 -14.648 1.725   1.00 12.22 ?  80  SER   B CB   1 
ATOM   5009 O OG   . SER   B 1 80  ? 38.725 -13.621 1.220   1.00 12.95 ?  80  SER   B OG   1 
ATOM   5010 H H    . SER   B 1 80  ? 38.513 -13.748 4.297   1.00 14.45 ?  80  SER   B H    1 
ATOM   5011 H HA   . SER   B 1 80  ? 40.697 -14.989 3.411   1.00 14.28 ?  80  SER   B HA   1 
ATOM   5012 H HB2  . SER   B 1 80  ? 40.349 -14.707 1.158   1.00 14.67 ?  80  SER   B HB2  1 
ATOM   5013 H HB3  . SER   B 1 80  ? 39.079 -15.487 1.706   1.00 14.67 ?  80  SER   B HB3  1 
ATOM   5014 H HG   . SER   B 1 80  ? 38.032 -13.557 1.703   1.00 15.54 ?  80  SER   B HG   1 
ATOM   5015 N N    . CYS   B 1 81  ? 41.773 -12.802 2.641   1.00 11.41 ?  81  CYS   B N    1 
ATOM   5016 C CA   . CYS   B 1 81  ? 42.321 -11.490 2.330   1.00 11.78 ?  81  CYS   B CA   1 
ATOM   5017 C C    . CYS   B 1 81  ? 43.092 -11.578 1.021   1.00 11.13 ?  81  CYS   B C    1 
ATOM   5018 O O    . CYS   B 1 81  ? 43.605 -12.639 0.647   1.00 11.82 ?  81  CYS   B O    1 
ATOM   5019 C CB   . CYS   B 1 81  ? 43.214 -10.938 3.451   1.00 12.34 ?  81  CYS   B CB   1 
ATOM   5020 S SG   . CYS   B 1 81  ? 44.734 -11.874 3.710   1.00 12.96 ?  81  CYS   B SG   1 
ATOM   5021 H H    . CYS   B 1 81  ? 42.284 -13.455 2.405   1.00 13.69 ?  81  CYS   B H    1 
ATOM   5022 H HA   . CYS   B 1 81  ? 41.587 -10.866 2.202   1.00 14.15 ?  81  CYS   B HA   1 
ATOM   5023 H HB2  . CYS   B 1 81  ? 43.463 -10.027 3.236   1.00 14.81 ?  81  CYS   B HB2  1 
ATOM   5024 H HB3  . CYS   B 1 81  ? 42.710 -10.950 4.285   1.00 14.81 ?  81  CYS   B HB3  1 
ATOM   5025 H HG   . CYS   B 1 81  ? 45.359 -11.376 4.610   1.00 15.56 ?  81  CYS   B HG   1 
ATOM   5026 N N    . VAL   B 1 82  ? 43.198 -10.438 0.347   1.00 11.30 ?  82  VAL   B N    1 
ATOM   5027 C CA   . VAL   B 1 82  ? 43.964 -10.312 -0.889  1.00 11.67 ?  82  VAL   B CA   1 
ATOM   5028 C C    . VAL   B 1 82  ? 45.305 -9.669  -0.566  1.00 11.99 ?  82  VAL   B C    1 
ATOM   5029 O O    . VAL   B 1 82  ? 45.354 -8.552  -0.031  1.00 13.00 ?  82  VAL   B O    1 
ATOM   5030 C CB   . VAL   B 1 82  ? 43.216 -9.475  -1.938  1.00 13.12 ?  82  VAL   B CB   1 
ATOM   5031 C CG1  . VAL   B 1 82  ? 44.061 -9.332  -3.198  1.00 14.37 ?  82  VAL   B CG1  1 
ATOM   5032 C CG2  . VAL   B 1 82  ? 41.863 -10.079 -2.255  1.00 14.05 ?  82  VAL   B CG2  1 
ATOM   5033 H H    . VAL   B 1 82  ? 42.816 -9.699  0.587   1.00 13.57 ?  82  VAL   B H    1 
ATOM   5034 H HA   . VAL   B 1 82  ? 44.126 -11.191 -1.259  1.00 14.01 ?  82  VAL   B HA   1 
ATOM   5035 H HB   . VAL   B 1 82  ? 43.065 -8.587  -1.584  1.00 15.74 ?  82  VAL   B HB   1 
ATOM   5036 H HG11 . VAL   B 1 82  ? 43.499 -9.013  -3.923  1.00 17.24 ?  82  VAL   B HG11 1 
ATOM   5037 H HG12 . VAL   B 1 82  ? 44.775 -8.692  -3.033  1.00 17.24 ?  82  VAL   B HG12 1 
ATOM   5038 H HG13 . VAL   B 1 82  ? 44.438 -10.195 -3.429  1.00 17.24 ?  82  VAL   B HG13 1 
ATOM   5039 H HG21 . VAL   B 1 82  ? 41.431 -9.555  -2.948  1.00 16.87 ?  82  VAL   B HG21 1 
ATOM   5040 H HG22 . VAL   B 1 82  ? 41.986 -10.994 -2.565  1.00 16.87 ?  82  VAL   B HG22 1 
ATOM   5041 H HG23 . VAL   B 1 82  ? 41.317 -10.078 -1.452  1.00 16.87 ?  82  VAL   B HG23 1 
ATOM   5042 N N    . LEU   B 1 83  ? 46.385 -10.358 -0.926  1.00 11.54 ?  83  LEU   B N    1 
ATOM   5043 C CA   . LEU   B 1 83  ? 47.741 -9.839  -0.807  1.00 11.46 ?  83  LEU   B CA   1 
ATOM   5044 C C    . LEU   B 1 83  ? 48.448 -9.976  -2.159  1.00 11.50 ?  83  LEU   B C    1 
ATOM   5045 O O    . LEU   B 1 83  ? 47.846 -10.392 -3.155  1.00 11.67 ?  83  LEU   B O    1 
ATOM   5046 C CB   . LEU   B 1 83  ? 48.493 -10.515 0.345   1.00 12.07 ?  83  LEU   B CB   1 
ATOM   5047 C CG   . LEU   B 1 83  ? 47.982 -10.152 1.746   1.00 13.28 ?  83  LEU   B CG   1 
ATOM   5048 C CD1  . LEU   B 1 83  ? 48.608 -11.027 2.811   1.00 13.98 ?  83  LEU   B CD1  1 
ATOM   5049 C CD2  . LEU   B 1 83  ? 48.200 -8.667  2.067   1.00 14.25 ?  83  LEU   B CD2  1 
ATOM   5050 H H    . LEU   B 1 83  ? 46.352 -11.156 -1.247  1.00 13.85 ?  83  LEU   B H    1 
ATOM   5051 H HA   . LEU   B 1 83  ? 47.683 -8.894  -0.605  1.00 13.75 ?  83  LEU   B HA   1 
ATOM   5052 H HB2  . LEU   B 1 83  ? 48.422 -11.474 0.242   1.00 14.48 ?  83  LEU   B HB2  1 
ATOM   5053 H HB3  . LEU   B 1 83  ? 49.427 -10.249 0.295   1.00 14.48 ?  83  LEU   B HB3  1 
ATOM   5054 H HG   . LEU   B 1 83  ? 47.028 -10.314 1.765   1.00 15.94 ?  83  LEU   B HG   1 
ATOM   5055 H HD11 . LEU   B 1 83  ? 48.252 -10.774 3.678   1.00 16.79 ?  83  LEU   B HD11 1 
ATOM   5056 H HD12 . LEU   B 1 83  ? 48.386 -11.957 2.626   1.00 16.79 ?  83  LEU   B HD12 1 
ATOM   5057 H HD13 . LEU   B 1 83  ? 49.568 -10.910 2.799   1.00 16.79 ?  83  LEU   B HD13 1 
ATOM   5058 H HD21 . LEU   B 1 83  ? 47.998 -8.516  3.003   1.00 17.11 ?  83  LEU   B HD21 1 
ATOM   5059 H HD22 . LEU   B 1 83  ? 49.122 -8.435  1.883   1.00 17.11 ?  83  LEU   B HD22 1 
ATOM   5060 H HD23 . LEU   B 1 83  ? 47.607 -8.134  1.512   1.00 17.11 ?  83  LEU   B HD23 1 
ATOM   5061 N N    . SER   B 1 84  ? 49.726 -9.601  -2.212  1.00 12.67 ?  84  SER   B N    1 
ATOM   5062 C CA   . SER   B 1 84  ? 50.461 -9.716  -3.462  1.00 12.87 ?  84  SER   B CA   1 
ATOM   5063 C C    . SER   B 1 84  ? 50.616 -11.174 -3.879  1.00 11.78 ?  84  SER   B C    1 
ATOM   5064 O O    . SER   B 1 84  ? 50.717 -12.075 -3.050  1.00 12.00 ?  84  SER   B O    1 
ATOM   5065 C CB   . SER   B 1 84  ? 51.856 -9.113  -3.310  1.00 14.86 ?  84  SER   B CB   1 
ATOM   5066 O OG   . SER   B 1 84  ? 52.599 -9.311  -4.497  1.00 16.11 ?  84  SER   B OG   1 
ATOM   5067 H H    . SER   B 1 84  ? 50.174 -9.272  -1.554  1.00 15.21 ?  84  SER   B H    1 
ATOM   5068 H HA   . SER   B 1 84  ? 49.993 -9.243  -4.166  1.00 15.45 ?  84  SER   B HA   1 
ATOM   5069 H HB2  . SER   B 1 84  ? 51.773 -8.158  -3.134  1.00 17.84 ?  84  SER   B HB2  1 
ATOM   5070 H HB3  . SER   B 1 84  ? 52.317 -9.544  -2.575  1.00 17.84 ?  84  SER   B HB3  1 
ATOM   5071 H HG   . SER   B 1 84  ? 53.365 -8.964  -4.419  1.00 19.33 ?  84  SER   B HG   1 
ATOM   5072 N N    . GLY   B 1 85  ? 50.668 -11.396 -5.187  1.00 13.00 ?  85  GLY   B N    1 
ATOM   5073 C CA   . GLY   B 1 85  ? 51.024 -12.684 -5.729  1.00 13.66 ?  85  GLY   B CA   1 
ATOM   5074 C C    . GLY   B 1 85  ? 52.496 -12.875 -6.032  1.00 13.04 ?  85  GLY   B C    1 
ATOM   5075 O O    . GLY   B 1 85  ? 52.877 -13.952 -6.495  1.00 13.38 ?  85  GLY   B O    1 
ATOM   5076 H H    . GLY   B 1 85  ? 50.516 -10.805 -5.782  1.00 15.60 ?  85  GLY   B H    1 
ATOM   5077 H HA2  . GLY   B 1 85  ? 50.759 -13.378 -5.100  1.00 16.40 ?  85  GLY   B HA2  1 
ATOM   5078 H HA3  . GLY   B 1 85  ? 50.534 -12.827 -6.550  1.00 16.40 ?  85  GLY   B HA3  1 
ATOM   5079 N N    . HIS   B 1 86  ? 53.348 -11.877 -5.806  1.00 12.65 ?  86  HIS   B N    1 
ATOM   5080 C CA   . HIS   B 1 86  ? 54.811 -12.048 -5.888  1.00 12.84 ?  86  HIS   B CA   1 
ATOM   5081 C C    . HIS   B 1 86  ? 55.180 -12.556 -7.279  1.00 13.12 ?  86  HIS   B C    1 
ATOM   5082 O O    . HIS   B 1 86  ? 54.788 -11.936 -8.281  1.00 13.69 ?  86  HIS   B O    1 
ATOM   5083 C CB   . HIS   B 1 86  ? 55.307 -12.890 -4.714  1.00 13.34 ?  86  HIS   B CB   1 
ATOM   5084 C CG   . HIS   B 1 86  ? 54.991 -12.287 -3.386  1.00 13.66 ?  86  HIS   B CG   1 
ATOM   5085 N ND1  . HIS   B 1 86  ? 55.815 -11.371 -2.768  1.00 14.71 ?  86  HIS   B ND1  1 
ATOM   5086 C CD2  . HIS   B 1 86  ? 53.914 -12.434 -2.578  1.00 13.80 ?  86  HIS   B CD2  1 
ATOM   5087 C CE1  . HIS   B 1 86  ? 55.258 -10.984 -1.635  1.00 14.76 ?  86  HIS   B CE1  1 
ATOM   5088 N NE2  . HIS   B 1 86  ? 54.102 -11.609 -1.498  1.00 14.05 ?  86  HIS   B NE2  1 
ATOM   5089 H H    . HIS   B 1 86  ? 53.107 -11.082 -5.600  1.00 15.19 ?  86  HIS   B H    1 
ATOM   5090 H HA   . HIS   B 1 86  ? 55.217 -11.176 -5.790  1.00 15.42 ?  86  HIS   B HA   1 
ATOM   5091 H HB2  . HIS   B 1 86  ? 54.897 -13.767 -4.752  1.00 16.02 ?  86  HIS   B HB2  1 
ATOM   5092 H HB3  . HIS   B 1 86  ? 56.275 -12.978 -4.774  1.00 16.02 ?  86  HIS   B HB3  1 
ATOM   5093 H HD2  . HIS   B 1 86  ? 53.171 -12.980 -2.737  1.00 16.56 ?  86  HIS   B HD2  1 
ATOM   5094 H HE1  . HIS   B 1 86  ? 55.621 -10.386 -1.025  1.00 17.71 ?  86  HIS   B HE1  1 
ATOM   5095 H HE2  . HIS   B 1 86  ? 53.560 -11.531 -0.831  1.00 16.86 ?  86  HIS   B HE2  1 
ATOM   5096 N N    . ASN   B 1 87  ? 55.945 -13.639 -7.392  1.00 13.42 ?  87  ASN   B N    1 
ATOM   5097 C CA   . ASN   B 1 87  ? 56.338 -14.207 -8.672  1.00 14.33 ?  87  ASN   B CA   1 
ATOM   5098 C C    . ASN   B 1 87  ? 55.358 -15.253 -9.174  1.00 13.74 ?  87  ASN   B C    1 
ATOM   5099 O O    . ASN   B 1 87  ? 55.676 -15.964 -10.134 1.00 15.49 ?  87  ASN   B O    1 
ATOM   5100 C CB   . ASN   B 1 87  ? 57.734 -14.830 -8.557  1.00 16.01 ?  87  ASN   B CB   1 
ATOM   5101 C CG   . ASN   B 1 87  ? 57.793 -15.954 -7.524  1.00 16.57 ?  87  ASN   B CG   1 
ATOM   5102 O OD1  . ASN   B 1 87  ? 57.161 -15.882 -6.468  1.00 16.06 ?  87  ASN   B OD1  1 
ATOM   5103 N ND2  . ASN   B 1 87  ? 58.531 -17.018 -7.847  1.00 18.73 ?  87  ASN   B ND2  1 
ATOM   5104 H H    . ASN   B 1 87  ? 56.254 -14.077 -6.721  1.00 16.11 ?  87  ASN   B H    1 
ATOM   5105 H HA   . ASN   B 1 87  ? 56.380 -13.497 -9.330  1.00 17.20 ?  87  ASN   B HA   1 
ATOM   5106 H HB2  . ASN   B 1 87  ? 57.987 -15.196 -9.421  1.00 19.22 ?  87  ASN   B HB2  1 
ATOM   5107 H HB3  . ASN   B 1 87  ? 58.364 -14.144 -8.290  1.00 19.22 ?  87  ASN   B HB3  1 
ATOM   5108 H HD21 . ASN   B 1 87  ? 58.596 -17.677 -7.303  1.00 22.48 ?  87  ASN   B HD21 1 
ATOM   5109 H HD22 . ASN   B 1 87  ? 58.952 -17.039 -8.601  1.00 22.48 ?  87  ASN   B HD22 1 
ATOM   5110 N N    . LEU   B 1 88  ? 54.180 -15.356 -8.558  1.00 12.84 ?  88  LEU   B N    1 
ATOM   5111 C CA   . LEU   B 1 88  ? 53.203 -16.388 -8.889  1.00 13.11 ?  88  LEU   B CA   1 
ATOM   5112 C C    . LEU   B 1 88  ? 51.969 -15.871 -9.609  1.00 12.70 ?  88  LEU   B C    1 
ATOM   5113 O O    . LEU   B 1 88  ? 51.361 -16.624 -10.379 1.00 14.53 ?  88  LEU   B O    1 
ATOM   5114 C CB   . LEU   B 1 88  ? 52.732 -17.080 -7.608  1.00 13.94 ?  88  LEU   B CB   1 
ATOM   5115 C CG   . LEU   B 1 88  ? 53.843 -17.749 -6.812  1.00 16.13 ?  88  LEU   B CG   1 
ATOM   5116 C CD1  . LEU   B 1 88  ? 53.337 -18.148 -5.436  1.00 17.75 ?  88  LEU   B CD1  1 
ATOM   5117 C CD2  . LEU   B 1 88  ? 54.368 -18.952 -7.574  1.00 19.22 ?  88  LEU   B CD2  1 
ATOM   5118 H H    . LEU   B 1 88  ? 53.919 -14.833 -7.919  1.00 15.41 ?  88  LEU   B H    1 
ATOM   5119 H HA   . LEU   B 1 88  ? 53.619 -17.049 -9.454  1.00 15.74 ?  88  LEU   B HA   1 
ATOM   5120 H HB2  . LEU   B 1 88  ? 52.309 -16.426 -7.031  1.00 16.73 ?  88  LEU   B HB2  1 
ATOM   5121 H HB3  . LEU   B 1 88  ? 52.087 -17.768 -7.846  1.00 16.73 ?  88  LEU   B HB3  1 
ATOM   5122 H HG   . LEU   B 1 88  ? 54.573 -17.122 -6.695  1.00 19.36 ?  88  LEU   B HG   1 
ATOM   5123 H HD11 . LEU   B 1 88  ? 53.965 -18.769 -5.036  1.00 21.31 ?  88  LEU   B HD11 1 
ATOM   5124 H HD12 . LEU   B 1 88  ? 53.257 -17.354 -4.886  1.00 21.31 ?  88  LEU   B HD12 1 
ATOM   5125 H HD13 . LEU   B 1 88  ? 52.470 -18.572 -5.535  1.00 21.31 ?  88  LEU   B HD13 1 
ATOM   5126 H HD21 . LEU   B 1 88  ? 55.003 -19.424 -7.014  1.00 23.07 ?  88  LEU   B HD21 1 
ATOM   5127 H HD22 . LEU   B 1 88  ? 53.625 -19.532 -7.796  1.00 23.07 ?  88  LEU   B HD22 1 
ATOM   5128 H HD23 . LEU   B 1 88  ? 54.805 -18.646 -8.384  1.00 23.07 ?  88  LEU   B HD23 1 
ATOM   5129 N N    . ALA   B 1 89  ? 51.560 -14.634 -9.345  1.00 12.12 ?  89  ALA   B N    1 
ATOM   5130 C CA   . ALA   B 1 89  ? 50.266 -14.136 -9.792  1.00 11.66 ?  89  ALA   B CA   1 
ATOM   5131 C C    . ALA   B 1 89  ? 50.239 -12.644 -9.510  1.00 12.15 ?  89  ALA   B C    1 
ATOM   5132 O O    . ALA   B 1 89  ? 51.081 -12.126 -8.775  1.00 13.12 ?  89  ALA   B O    1 
ATOM   5133 C CB   . ALA   B 1 89  ? 49.121 -14.811 -9.038  1.00 12.29 ?  89  ALA   B CB   1 
ATOM   5134 H H    . ALA   B 1 89  ? 52.012 -14.053 -8.893  1.00 14.55 ?  89  ALA   B H    1 
ATOM   5135 H HA   . ALA   B 1 89  ? 50.157 -14.281 -10.744 1.00 14.00 ?  89  ALA   B HA   1 
ATOM   5136 H HB1  . ALA   B 1 89  ? 48.276 -14.471 -9.378  1.00 14.75 ?  89  ALA   B HB1  1 
ATOM   5137 H HB2  . ALA   B 1 89  ? 49.172 -15.769 -9.189  1.00 14.75 ?  89  ALA   B HB2  1 
ATOM   5138 H HB3  . ALA   B 1 89  ? 49.204 -14.617 -8.096  1.00 14.75 ?  89  ALA   B HB3  1 
ATOM   5139 N N    . LYS   B 1 90  ? 49.245 -11.954 -10.070 1.00 13.04 ?  90  LYS   B N    1 
ATOM   5140 C CA   . LYS   B 1 90  ? 49.052 -10.566 -9.664  1.00 13.03 ?  90  LYS   B CA   1 
ATOM   5141 C C    . LYS   B 1 90  ? 48.739 -10.495 -8.174  1.00 12.99 ?  90  LYS   B C    1 
ATOM   5142 O O    . LYS   B 1 90  ? 49.379 -9.743  -7.423  1.00 14.35 ?  90  LYS   B O    1 
ATOM   5143 C CB   . LYS   B 1 90  ? 47.964 -9.910  -10.513 1.00 15.10 ?  90  LYS   B CB   1 
ATOM   5144 C CG   . LYS   B 1 90  ? 47.675 -8.464  -10.150 1.00 15.65 ?  90  LYS   B CG   1 
ATOM   5145 C CD   . LYS   B 1 90  ? 48.889 -7.577  -10.229 1.00 18.86 ?  90  LYS   B CD   1 
ATOM   5146 C CE   . LYS   B 1 90  ? 48.457 -6.145  -10.007 1.00 21.21 ?  90  LYS   B CE   1 
ATOM   5147 N NZ   . LYS   B 1 90  ? 49.618 -5.233  -9.876  1.00 21.23 ?  90  LYS   B NZ   1 
ATOM   5148 H H    . LYS   B 1 90  ? 48.691 -12.258 -10.657 1.00 15.66 ?  90  LYS   B H    1 
ATOM   5149 H HA   . LYS   B 1 90  ? 49.874 -10.089 -9.816  1.00 15.64 ?  90  LYS   B HA   1 
ATOM   5150 H HB2  . LYS   B 1 90  ? 48.243 -9.928  -11.446 1.00 18.12 ?  90  LYS   B HB2  1 
ATOM   5151 H HB3  . LYS   B 1 90  ? 47.138 -10.412 -10.417 1.00 18.12 ?  90  LYS   B HB3  1 
ATOM   5152 H HG2  . LYS   B 1 90  ? 47.006 -8.112  -10.764 1.00 18.78 ?  90  LYS   B HG2  1 
ATOM   5153 H HG3  . LYS   B 1 90  ? 47.331 -8.429  -9.242  1.00 18.78 ?  90  LYS   B HG3  1 
ATOM   5154 H HD2  . LYS   B 1 90  ? 49.521 -7.822  -9.534  1.00 22.64 ?  90  LYS   B HD2  1 
ATOM   5155 H HD3  . LYS   B 1 90  ? 49.294 -7.650  -11.106 1.00 22.64 ?  90  LYS   B HD3  1 
ATOM   5156 H HE2  . LYS   B 1 90  ? 47.928 -5.843  -10.764 1.00 25.46 ?  90  LYS   B HE2  1 
ATOM   5157 H HE3  . LYS   B 1 90  ? 47.937 -6.082  -9.191  1.00 25.46 ?  90  LYS   B HE3  1 
ATOM   5158 H HZ1  . LYS   B 1 90  ? 49.343 -4.394  -9.748  1.00 25.49 ?  90  LYS   B HZ1  1 
ATOM   5159 H HZ2  . LYS   B 1 90  ? 50.124 -5.476  -9.184  1.00 25.49 ?  90  LYS   B HZ2  1 
ATOM   5160 H HZ3  . LYS   B 1 90  ? 50.115 -5.259  -10.616 1.00 25.49 ?  90  LYS   B HZ3  1 
ATOM   5161 N N    . HIS   B 1 91  ? 47.781 -11.312 -7.727  1.00 11.46 ?  91  HIS   B N    1 
ATOM   5162 C CA   . HIS   B 1 91  ? 47.321 -11.339 -6.352  1.00 11.78 ?  91  HIS   B CA   1 
ATOM   5163 C C    . HIS   B 1 91  ? 47.314 -12.767 -5.834  1.00 10.88 ?  91  HIS   B C    1 
ATOM   5164 O O    . HIS   B 1 91  ? 47.087 -13.721 -6.587  1.00 11.47 ?  91  HIS   B O    1 
ATOM   5165 C CB   . HIS   B 1 91  ? 45.870 -10.855 -6.238  1.00 13.42 ?  91  HIS   B CB   1 
ATOM   5166 C CG   . HIS   B 1 91  ? 45.664 -9.444  -6.672  1.00 16.86 ?  91  HIS   B CG   1 
ATOM   5167 N ND1  . HIS   B 1 91  ? 46.274 -8.373  -6.054  1.00 19.41 ?  91  HIS   B ND1  1 
ATOM   5168 C CD2  . HIS   B 1 91  ? 44.883 -8.924  -7.644  1.00 19.23 ?  91  HIS   B CD2  1 
ATOM   5169 C CE1  . HIS   B 1 91  ? 45.895 -7.252  -6.643  1.00 20.44 ?  91  HIS   B CE1  1 
ATOM   5170 N NE2  . HIS   B 1 91  ? 45.043 -7.559  -7.606  1.00 20.49 ?  91  HIS   B NE2  1 
ATOM   5171 H H    . HIS   B 1 91  ? 47.369 -11.882 -8.222  1.00 13.76 ?  91  HIS   B H    1 
ATOM   5172 H HA   . HIS   B 1 91  ? 47.893 -10.784 -5.788  1.00 14.14 ?  91  HIS   B HA   1 
ATOM   5173 H HB2  . HIS   B 1 91  ? 45.311 -11.419 -6.792  1.00 16.11 ?  91  HIS   B HB2  1 
ATOM   5174 H HB3  . HIS   B 1 91  ? 45.589 -10.924 -5.310  1.00 16.11 ?  91  HIS   B HB3  1 
ATOM   5175 H HD1  . HIS   B 1 91  ? 46.825 -8.429  -5.391  1.00 23.29 ?  91  HIS   B HD1  1 
ATOM   5176 H HD2  . HIS   B 1 91  ? 44.347 -9.392  -8.237  1.00 23.08 ?  91  HIS   B HD2  1 
ATOM   5177 H HE1  . HIS   B 1 91  ? 46.176 -6.395  -6.408  1.00 24.54 ?  91  HIS   B HE1  1 
ATOM   5178 N N    . CYS   B 1 92  ? 47.509 -12.899 -4.529  1.00 10.93 ?  92  CYS   B N    1 
ATOM   5179 C CA   . CYS   B 1 92  ? 47.205 -14.134 -3.816  1.00 10.55 ?  92  CYS   B CA   1 
ATOM   5180 C C    . CYS   B 1 92  ? 45.985 -13.898 -2.934  1.00 10.22 ?  92  CYS   B C    1 
ATOM   5181 O O    . CYS   B 1 92  ? 45.986 -13.002 -2.081  1.00 11.22 ?  92  CYS   B O    1 
ATOM   5182 C CB   . CYS   B 1 92  ? 48.381 -14.590 -2.960  1.00 11.33 ?  92  CYS   B CB   1 
ATOM   5183 S SG   . CYS   B 1 92  ? 48.035 -16.133 -2.070  1.00 11.47 ?  92  CYS   B SG   1 
ATOM   5184 H H    . CYS   B 1 92  ? 47.834 -12.280 -4.017  1.00 13.12 ?  92  CYS   B H    1 
ATOM   5185 H HA   . CYS   B 1 92  ? 47.004 -14.833 -4.458  1.00 12.66 ?  92  CYS   B HA   1 
ATOM   5186 H HB2  . CYS   B 1 92  ? 49.151 -14.732 -3.526  1.00 13.60 ?  92  CYS   B HB2  1 
ATOM   5187 H HB3  . CYS   B 1 92  ? 48.572 -13.902 -2.301  1.00 13.60 ?  92  CYS   B HB3  1 
ATOM   5188 H HG   . CYS   B 1 92  ? 49.011 -16.438 -1.437  1.00 13.77 ?  92  CYS   B HG   1 
ATOM   5189 N N    . LEU   B 1 93  ? 44.949 -14.704 -3.143  1.00 10.29 ?  93  LEU   B N    1 
ATOM   5190 C CA   . LEU   B 1 93  ? 43.773 -14.725 -2.282  1.00 10.67 ?  93  LEU   B CA   1 
ATOM   5191 C C    . LEU   B 1 93  ? 43.997 -15.790 -1.216  1.00 9.95  ?  93  LEU   B C    1 
ATOM   5192 O O    . LEU   B 1 93  ? 43.952 -16.993 -1.510  1.00 10.68 ?  93  LEU   B O    1 
ATOM   5193 C CB   . LEU   B 1 93  ? 42.515 -15.020 -3.095  1.00 11.00 ?  93  LEU   B CB   1 
ATOM   5194 C CG   . LEU   B 1 93  ? 41.212 -15.033 -2.289  1.00 11.60 ?  93  LEU   B CG   1 
ATOM   5195 C CD1  . LEU   B 1 93  ? 40.859 -13.644 -1.793  1.00 12.02 ?  93  LEU   B CD1  1 
ATOM   5196 C CD2  . LEU   B 1 93  ? 40.083 -15.626 -3.116  1.00 11.83 ?  93  LEU   B CD2  1 
ATOM   5197 H H    . LEU   B 1 93  ? 44.905 -15.273 -3.798  1.00 12.35 ?  93  LEU   B H    1 
ATOM   5198 H HA   . LEU   B 1 93  ? 43.673 -13.861 -1.854  1.00 12.80 ?  93  LEU   B HA   1 
ATOM   5199 H HB2  . LEU   B 1 93  ? 42.425 -14.336 -3.782  1.00 13.20 ?  93  LEU   B HB2  1 
ATOM   5200 H HB3  . LEU   B 1 93  ? 42.613 -15.886 -3.513  1.00 13.20 ?  93  LEU   B HB3  1 
ATOM   5201 H HG   . LEU   B 1 93  ? 41.333 -15.601 -1.515  1.00 13.92 ?  93  LEU   B HG   1 
ATOM   5202 H HD11 . LEU   B 1 93  ? 40.003 -13.679 -1.345  1.00 14.43 ?  93  LEU   B HD11 1 
ATOM   5203 H HD12 . LEU   B 1 93  ? 41.547 -13.345 -1.178  1.00 14.43 ?  93  LEU   B HD12 1 
ATOM   5204 H HD13 . LEU   B 1 93  ? 40.812 -13.041 -2.554  1.00 14.43 ?  93  LEU   B HD13 1 
ATOM   5205 H HD21 . LEU   B 1 93  ? 39.270 -15.621 -2.589  1.00 14.20 ?  93  LEU   B HD21 1 
ATOM   5206 H HD22 . LEU   B 1 93  ? 39.962 -15.089 -3.917  1.00 14.20 ?  93  LEU   B HD22 1 
ATOM   5207 H HD23 . LEU   B 1 93  ? 40.313 -16.536 -3.362  1.00 14.20 ?  93  LEU   B HD23 1 
ATOM   5208 N N    . HIS   B 1 94  ? 44.274 -15.352 0.008   1.00 10.06 ?  94  HIS   B N    1 
ATOM   5209 C CA   . HIS   B 1 94  ? 44.495 -16.258 1.128   1.00 10.22 ?  94  HIS   B CA   1 
ATOM   5210 C C    . HIS   B 1 94  ? 43.133 -16.616 1.708   1.00 10.39 ?  94  HIS   B C    1 
ATOM   5211 O O    . HIS   B 1 94  ? 42.464 -15.748 2.270   1.00 12.10 ?  94  HIS   B O    1 
ATOM   5212 C CB   . HIS   B 1 94  ? 45.370 -15.584 2.185   1.00 10.58 ?  94  HIS   B CB   1 
ATOM   5213 C CG   . HIS   B 1 94  ? 46.754 -15.281 1.713   1.00 10.78 ?  94  HIS   B CG   1 
ATOM   5214 N ND1  . HIS   B 1 94  ? 47.782 -16.194 1.803   1.00 11.04 ?  94  HIS   B ND1  1 
ATOM   5215 C CD2  . HIS   B 1 94  ? 47.262 -14.176 1.115   1.00 10.91 ?  94  HIS   B CD2  1 
ATOM   5216 C CE1  . HIS   B 1 94  ? 48.869 -15.647 1.289   1.00 10.65 ?  94  HIS   B CE1  1 
ATOM   5217 N NE2  . HIS   B 1 94  ? 48.584 -14.427 0.867   1.00 11.40 ?  94  HIS   B NE2  1 
ATOM   5218 H H    . HIS   B 1 94  ? 44.343 -14.517 0.215   1.00 12.08 ?  94  HIS   B H    1 
ATOM   5219 H HA   . HIS   B 1 94  ? 44.931 -17.066 0.816   1.00 12.27 ?  94  HIS   B HA   1 
ATOM   5220 H HB2  . HIS   B 1 94  ? 44.955 -14.750 2.446   1.00 12.70 ?  94  HIS   B HB2  1 
ATOM   5221 H HB3  . HIS   B 1 94  ? 45.438 -16.176 2.950   1.00 12.70 ?  94  HIS   B HB3  1 
ATOM   5222 H HD2  . HIS   B 1 94  ? 46.801 -13.399 0.916   1.00 13.10 ?  94  HIS   B HD2  1 
ATOM   5223 H HE1  . HIS   B 1 94  ? 49.702 -16.063 1.239   1.00 12.79 ?  94  HIS   B HE1  1 
ATOM   5224 H HE2  . HIS   B 1 94  ? 49.137 -13.889 0.500   1.00 13.69 ?  94  HIS   B HE2  1 
ATOM   5225 N N    . VAL   B 1 95  ? 42.701 -17.871 1.554   1.00 10.38 ?  95  VAL   B N    1 
ATOM   5226 C CA   . VAL   B 1 95  ? 41.376 -18.314 1.988   1.00 10.82 ?  95  VAL   B CA   1 
ATOM   5227 C C    . VAL   B 1 95  ? 41.546 -19.350 3.086   1.00 11.03 ?  95  VAL   B C    1 
ATOM   5228 O O    . VAL   B 1 95  ? 42.312 -20.306 2.925   1.00 11.47 ?  95  VAL   B O    1 
ATOM   5229 C CB   . VAL   B 1 95  ? 40.562 -18.918 0.828   1.00 10.87 ?  95  VAL   B CB   1 
ATOM   5230 C CG1  . VAL   B 1 95  ? 39.183 -19.368 1.309   1.00 12.05 ?  95  VAL   B CG1  1 
ATOM   5231 C CG2  . VAL   B 1 95  ? 40.437 -17.933 -0.316  1.00 11.17 ?  95  VAL   B CG2  1 
ATOM   5232 H H    . VAL   B 1 95  ? 43.166 -18.497 1.194   1.00 12.46 ?  95  VAL   B H    1 
ATOM   5233 H HA   . VAL   B 1 95  ? 40.878 -17.561 2.351   1.00 12.98 ?  95  VAL   B HA   1 
ATOM   5234 H HB   . VAL   B 1 95  ? 41.024 -19.698 0.495   1.00 13.05 ?  95  VAL   B HB   1 
ATOM   5235 H HG11 . VAL   B 1 95  ? 38.625 -19.567 0.534   1.00 14.46 ?  95  VAL   B HG11 1 
ATOM   5236 H HG12 . VAL   B 1 95  ? 39.274 -20.164 1.854   1.00 14.46 ?  95  VAL   B HG12 1 
ATOM   5237 H HG13 . VAL   B 1 95  ? 38.774 -18.656 1.826   1.00 14.46 ?  95  VAL   B HG13 1 
ATOM   5238 H HG21 . VAL   B 1 95  ? 39.866 -18.319 -1.000  1.00 13.41 ?  95  VAL   B HG21 1 
ATOM   5239 H HG22 . VAL   B 1 95  ? 40.042 -17.112 0.018   1.00 13.41 ?  95  VAL   B HG22 1 
ATOM   5240 H HG23 . VAL   B 1 95  ? 41.317 -17.759 -0.675  1.00 13.41 ?  95  VAL   B HG23 1 
ATOM   5241 N N    . VAL   B 1 96  ? 40.810 -19.180 4.182   1.00 11.34 ?  96  VAL   B N    1 
ATOM   5242 C CA   . VAL   B 1 96  ? 40.889 -20.094 5.321   1.00 11.73 ?  96  VAL   B CA   1 
ATOM   5243 C C    . VAL   B 1 96  ? 39.702 -21.056 5.272   1.00 12.31 ?  96  VAL   B C    1 
ATOM   5244 O O    . VAL   B 1 96  ? 38.582 -20.701 5.649   1.00 12.85 ?  96  VAL   B O    1 
ATOM   5245 C CB   . VAL   B 1 96  ? 40.945 -19.347 6.657   1.00 12.43 ?  96  VAL   B CB   1 
ATOM   5246 C CG1  . VAL   B 1 96  ? 41.131 -20.339 7.801   1.00 13.13 ?  96  VAL   B CG1  1 
ATOM   5247 C CG2  . VAL   B 1 96  ? 42.055 -18.304 6.661   1.00 13.08 ?  96  VAL   B CG2  1 
ATOM   5248 H H    . VAL   B 1 96  ? 40.251 -18.538 4.297   1.00 13.61 ?  96  VAL   B H    1 
ATOM   5249 H HA   . VAL   B 1 96  ? 41.701 -20.622 5.249   1.00 14.08 ?  96  VAL   B HA   1 
ATOM   5250 H HB   . VAL   B 1 96  ? 40.102 -18.890 6.801   1.00 14.92 ?  96  VAL   B HB   1 
ATOM   5251 H HG11 . VAL   B 1 96  ? 41.318 -19.848 8.620   1.00 15.76 ?  96  VAL   B HG11 1 
ATOM   5252 H HG12 . VAL   B 1 96  ? 40.325 -20.863 7.909   1.00 15.76 ?  96  VAL   B HG12 1 
ATOM   5253 H HG13 . VAL   B 1 96  ? 41.882 -20.923 7.595   1.00 15.76 ?  96  VAL   B HG13 1 
ATOM   5254 H HG21 . VAL   B 1 96  ? 42.108 -17.897 7.543   1.00 15.70 ?  96  VAL   B HG21 1 
ATOM   5255 H HG22 . VAL   B 1 96  ? 42.896 -18.731 6.444   1.00 15.70 ?  96  VAL   B HG22 1 
ATOM   5256 H HG23 . VAL   B 1 96  ? 41.849 -17.622 6.000   1.00 15.70 ?  96  VAL   B HG23 1 
ATOM   5257 N N    . GLY   B 1 97  ? 39.938 -22.289 4.835   1.00 11.92 ?  97  GLY   B N    1 
ATOM   5258 C CA   . GLY   B 1 97  ? 38.965 -23.345 4.995   1.00 12.87 ?  97  GLY   B CA   1 
ATOM   5259 C C    . GLY   B 1 97  ? 39.087 -23.956 6.374   1.00 13.56 ?  97  GLY   B C    1 
ATOM   5260 O O    . GLY   B 1 97  ? 40.121 -23.820 7.040   1.00 14.00 ?  97  GLY   B O    1 
ATOM   5261 H H    . GLY   B 1 97  ? 40.667 -22.533 4.442   1.00 14.31 ?  97  GLY   B H    1 
ATOM   5262 H HA2  . GLY   B 1 97  ? 38.074 -22.978 4.878   1.00 15.45 ?  97  GLY   B HA2  1 
ATOM   5263 H HA3  . GLY   B 1 97  ? 39.112 -24.029 4.322   1.00 15.45 ?  97  GLY   B HA3  1 
ATOM   5264 N N    . PRO   B 1 98  ? 38.037 -24.637 6.836   1.00 14.25 ?  98  PRO   B N    1 
ATOM   5265 C CA   . PRO   B 1 98  ? 38.128 -25.331 8.123   1.00 15.13 ?  98  PRO   B CA   1 
ATOM   5266 C C    . PRO   B 1 98  ? 39.153 -26.453 8.077   1.00 14.74 ?  98  PRO   B C    1 
ATOM   5267 O O    . PRO   B 1 98  ? 39.257 -27.189 7.097   1.00 15.14 ?  98  PRO   B O    1 
ATOM   5268 C CB   . PRO   B 1 98  ? 36.708 -25.875 8.328   1.00 15.50 ?  98  PRO   B CB   1 
ATOM   5269 C CG   . PRO   B 1 98  ? 36.148 -26.003 6.956   1.00 15.13 ?  98  PRO   B CG   1 
ATOM   5270 C CD   . PRO   B 1 98  ? 36.719 -24.826 6.205   1.00 14.52 ?  98  PRO   B CD   1 
ATOM   5271 H HA   . PRO   B 1 98  ? 38.353 -24.710 8.827   1.00 18.16 ?  98  PRO   B HA   1 
ATOM   5272 H HB2  . PRO   B 1 98  ? 36.751 -26.742 8.763   1.00 18.61 ?  98  PRO   B HB2  1 
ATOM   5273 H HB3  . PRO   B 1 98  ? 36.193 -25.248 8.852   1.00 18.61 ?  98  PRO   B HB3  1 
ATOM   5274 H HG2  . PRO   B 1 98  ? 36.441 -26.840 6.556   1.00 18.16 ?  98  PRO   B HG2  1 
ATOM   5275 H HG3  . PRO   B 1 98  ? 35.182 -25.958 6.989   1.00 18.16 ?  98  PRO   B HG3  1 
ATOM   5276 H HD2  . PRO   B 1 98  ? 36.811 -25.036 5.259   1.00 17.43 ?  98  PRO   B HD2  1 
ATOM   5277 H HD3  . PRO   B 1 98  ? 36.170 -24.036 6.339   1.00 17.43 ?  98  PRO   B HD3  1 
ATOM   5278 N N    . ASN   B 1 99  ? 39.905 -26.586 9.162   1.00 15.53 ?  99  ASN   B N    1 
ATOM   5279 C CA   . ASN   B 1 99  ? 40.882 -27.661 9.320   1.00 16.17 ?  99  ASN   B CA   1 
ATOM   5280 C C    . ASN   B 1 99  ? 40.249 -28.745 10.193  1.00 18.37 ?  99  ASN   B C    1 
ATOM   5281 O O    . ASN   B 1 99  ? 40.164 -28.602 11.416  1.00 19.59 ?  99  ASN   B O    1 
ATOM   5282 C CB   . ASN   B 1 99  ? 42.156 -27.107 9.942   1.00 16.88 ?  99  ASN   B CB   1 
ATOM   5283 C CG   . ASN   B 1 99  ? 43.282 -28.116 9.954   1.00 17.99 ?  99  ASN   B CG   1 
ATOM   5284 O OD1  . ASN   B 1 99  ? 43.049 -29.304 10.132  1.00 18.72 ?  99  ASN   B OD1  1 
ATOM   5285 N ND2  . ASN   B 1 99  ? 44.505 -27.649 9.754   1.00 18.18 ?  99  ASN   B ND2  1 
ATOM   5286 H H    . ASN   B 1 99  ? 39.872 -26.050 9.833   1.00 18.64 ?  99  ASN   B H    1 
ATOM   5287 H HA   . ASN   B 1 99  ? 41.096 -28.044 8.456   1.00 19.41 ?  99  ASN   B HA   1 
ATOM   5288 H HB2  . ASN   B 1 99  ? 42.444 -26.336 9.438   1.00 20.26 ?  99  ASN   B HB2  1 
ATOM   5289 H HB3  . ASN   B 1 99  ? 41.967 -26.854 10.863  1.00 20.26 ?  99  ASN   B HB3  1 
ATOM   5290 H HD21 . ASN   B 1 99  ? 45.175 -28.186 9.750   1.00 21.82 ?  99  ASN   B HD21 1 
ATOM   5291 H HD22 . ASN   B 1 99  ? 44.623 -26.807 9.631   1.00 21.82 ?  99  ASN   B HD22 1 
ATOM   5292 N N    A VAL   B 1 100 ? 39.784 -29.823 9.553   0.72 20.58 ?  100 VAL   B N    1 
ATOM   5293 N N    B VAL   B 1 100 ? 39.795 -29.824 9.549   0.28 20.62 ?  100 VAL   B N    1 
ATOM   5294 C CA   A VAL   B 1 100 ? 39.163 -30.925 10.288  0.72 23.47 ?  100 VAL   B CA   1 
ATOM   5295 C CA   B VAL   B 1 100 ? 39.172 -30.932 10.271  0.28 23.02 ?  100 VAL   B CA   1 
ATOM   5296 C C    A VAL   B 1 100 ? 40.166 -31.603 11.213  0.72 23.66 ?  100 VAL   B C    1 
ATOM   5297 C C    B VAL   B 1 100 ? 40.167 -31.598 11.210  0.28 23.65 ?  100 VAL   B C    1 
ATOM   5298 O O    A VAL   B 1 100 ? 39.788 -32.142 12.259  0.72 24.19 ?  100 VAL   B O    1 
ATOM   5299 O O    B VAL   B 1 100 ? 39.786 -32.109 12.270  0.28 23.95 ?  100 VAL   B O    1 
ATOM   5300 C CB   A VAL   B 1 100 ? 38.515 -31.926 9.310   0.72 26.26 ?  100 VAL   B CB   1 
ATOM   5301 C CB   B VAL   B 1 100 ? 38.554 -31.934 9.273   0.28 24.73 ?  100 VAL   B CB   1 
ATOM   5302 C CG1  A VAL   B 1 100 ? 38.010 -33.155 10.053  0.72 27.28 ?  100 VAL   B CG1  1 
ATOM   5303 C CG1  B VAL   B 1 100 ? 38.040 -33.171 9.997   0.28 25.32 ?  100 VAL   B CG1  1 
ATOM   5304 C CG2  A VAL   B 1 100 ? 37.379 -31.265 8.545   0.72 27.12 ?  100 VAL   B CG2  1 
ATOM   5305 C CG2  B VAL   B 1 100 ? 37.434 -31.272 8.487   0.28 25.30 ?  100 VAL   B CG2  1 
ATOM   5306 H H    A VAL   B 1 100 ? 39.800 -29.928 8.697   0.72 24.71 ?  100 VAL   B H    1 
ATOM   5307 H H    B VAL   B 1 100 ? 39.830 -29.933 8.696   0.28 24.75 ?  100 VAL   B H    1 
ATOM   5308 H HA   A VAL   B 1 100 ? 38.450 -30.561 10.838  0.72 28.17 ?  100 VAL   B HA   1 
ATOM   5309 H HA   B VAL   B 1 100 ? 38.449 -30.579 10.811  0.28 27.63 ?  100 VAL   B HA   1 
ATOM   5310 H HB   A VAL   B 1 100 ? 39.181 -32.219 8.670   0.72 31.51 ?  100 VAL   B HB   1 
ATOM   5311 H HB   B VAL   B 1 100 ? 39.235 -32.218 8.645   0.28 29.68 ?  100 VAL   B HB   1 
ATOM   5312 H HG11 A VAL   B 1 100 ? 37.425 -33.659 9.464   0.72 32.75 ?  100 VAL   B HG11 1 
ATOM   5313 H HG11 B VAL   B 1 100 ? 37.470 -33.674 9.393   0.28 30.38 ?  100 VAL   B HG11 1 
ATOM   5314 H HG12 A VAL   B 1 100 ? 38.765 -33.705 10.314  0.72 32.75 ?  100 VAL   B HG12 1 
ATOM   5315 H HG12 B VAL   B 1 100 ? 38.794 -33.718 10.267  0.28 30.38 ?  100 VAL   B HG12 1 
ATOM   5316 H HG13 A VAL   B 1 100 ? 37.518 -32.870 10.839  0.72 32.75 ?  100 VAL   B HG13 1 
ATOM   5317 H HG13 B VAL   B 1 100 ? 37.532 -32.894 10.775  0.28 30.38 ?  100 VAL   B HG13 1 
ATOM   5318 H HG21 A VAL   B 1 100 ? 36.982 -31.918 7.946   0.72 32.55 ?  100 VAL   B HG21 1 
ATOM   5319 H HG21 B VAL   B 1 100 ? 37.044 -31.925 7.884   0.28 30.36 ?  100 VAL   B HG21 1 
ATOM   5320 H HG22 A VAL   B 1 100 ? 36.713 -30.952 9.178   0.72 32.55 ?  100 VAL   B HG22 1 
ATOM   5321 H HG22 B VAL   B 1 100 ? 36.761 -30.951 9.107   0.28 30.36 ?  100 VAL   B HG22 1 
ATOM   5322 H HG23 A VAL   B 1 100 ? 37.732 -30.521 8.037   0.72 32.55 ?  100 VAL   B HG23 1 
ATOM   5323 H HG23 B VAL   B 1 100 ? 37.800 -30.531 7.981   0.28 30.36 ?  100 VAL   B HG23 1 
ATOM   5324 N N    . ASN   B 1 101 ? 41.449 -31.617 10.840  1.00 24.02 ?  101 ASN   B N    1 
ATOM   5325 C CA   . ASN   B 1 101 ? 42.480 -32.160 11.724  1.00 26.06 ?  101 ASN   B CA   1 
ATOM   5326 C C    . ASN   B 1 101 ? 42.661 -31.331 12.989  1.00 28.04 ?  101 ASN   B C    1 
ATOM   5327 O O    . ASN   B 1 101 ? 43.290 -31.813 13.940  1.00 29.46 ?  101 ASN   B O    1 
ATOM   5328 C CB   . ASN   B 1 101 ? 43.813 -32.284 10.980  1.00 26.22 ?  101 ASN   B CB   1 
ATOM   5329 C CG   . ASN   B 1 101 ? 43.819 -33.429 9.987   1.00 25.70 ?  101 ASN   B CG   1 
ATOM   5330 O OD1  . ASN   B 1 101 ? 43.171 -34.447 10.204  1.00 26.90 ?  101 ASN   B OD1  1 
ATOM   5331 N ND2  . ASN   B 1 101 ? 44.544 -33.263 8.888   1.00 24.89 ?  101 ASN   B ND2  1 
ATOM   5332 H H    A ASN   B 1 101 ? 41.739 -31.338 10.079  0.72 28.83 ?  101 ASN   B H    1 
ATOM   5333 H H    B ASN   B 1 101 ? 41.742 -31.330 10.083  0.28 28.83 ?  101 ASN   B H    1 
ATOM   5334 H HA   . ASN   B 1 101 ? 42.212 -33.047 11.995  1.00 31.28 ?  101 ASN   B HA   1 
ATOM   5335 H HB2  . ASN   B 1 101 ? 43.990 -31.467 10.490  1.00 31.47 ?  101 ASN   B HB2  1 
ATOM   5336 H HB3  . ASN   B 1 101 ? 44.521 -32.442 11.626  1.00 31.47 ?  101 ASN   B HB3  1 
ATOM   5337 H HD21 . ASN   B 1 101 ? 44.580 -33.888 8.297   1.00 29.88 ?  101 ASN   B HD21 1 
ATOM   5338 H HD22 . ASN   B 1 101 ? 44.978 -32.531 8.766   1.00 29.88 ?  101 ASN   B HD22 1 
ATOM   5339 N N    . LYS   B 1 102 ? 42.134 -30.105 13.018  1.00 30.26 ?  102 LYS   B N    1 
ATOM   5340 C CA   . LYS   B 1 102 ? 42.103 -29.271 14.212  1.00 32.91 ?  102 LYS   B CA   1 
ATOM   5341 C C    . LYS   B 1 102 ? 40.723 -29.230 14.857  1.00 32.46 ?  102 LYS   B C    1 
ATOM   5342 O O    . LYS   B 1 102 ? 40.506 -28.439 15.779  1.00 33.56 ?  102 LYS   B O    1 
ATOM   5343 C CB   . LYS   B 1 102 ? 42.528 -27.841 13.873  1.00 36.11 ?  102 LYS   B CB   1 
ATOM   5344 C CG   . LYS   B 1 102 ? 43.984 -27.665 13.488  1.00 39.37 ?  102 LYS   B CG   1 
ATOM   5345 C CD   . LYS   B 1 102 ? 44.219 -26.240 13.012  1.00 42.32 ?  102 LYS   B CD   1 
ATOM   5346 C CE   . LYS   B 1 102 ? 45.688 -25.943 12.777  1.00 44.60 ?  102 LYS   B CE   1 
ATOM   5347 N NZ   . LYS   B 1 102 ? 45.880 -24.545 12.290  1.00 45.98 ?  102 LYS   B NZ   1 
ATOM   5348 H H    . LYS   B 1 102 ? 41.771 -29.726 12.336  1.00 36.32 ?  102 LYS   B H    1 
ATOM   5349 H HA   . LYS   B 1 102 ? 42.731 -29.621 14.861  1.00 39.50 ?  102 LYS   B HA   1 
ATOM   5350 H HB2  . LYS   B 1 102 ? 41.990 -27.529 13.129  1.00 43.33 ?  102 LYS   B HB2  1 
ATOM   5351 H HB3  . LYS   B 1 102 ? 42.363 -27.279 14.648  1.00 43.33 ?  102 LYS   B HB3  1 
ATOM   5352 H HG2  . LYS   B 1 102 ? 44.549 -27.830 14.260  1.00 47.25 ?  102 LYS   B HG2  1 
ATOM   5353 H HG3  . LYS   B 1 102 ? 44.207 -28.273 12.766  1.00 47.25 ?  102 LYS   B HG3  1 
ATOM   5354 H HD2  . LYS   B 1 102 ? 43.746 -26.103 12.176  1.00 50.79 ?  102 LYS   B HD2  1 
ATOM   5355 H HD3  . LYS   B 1 102 ? 43.890 -25.623 13.685  1.00 50.79 ?  102 LYS   B HD3  1 
ATOM   5356 H HE2  . LYS   B 1 102 ? 46.174 -26.046 13.610  1.00 53.53 ?  102 LYS   B HE2  1 
ATOM   5357 H HE3  . LYS   B 1 102 ? 46.036 -26.551 12.106  1.00 53.53 ?  102 LYS   B HE3  1 
ATOM   5358 H HZ1  . LYS   B 1 102 ? 46.744 -24.385 12.157  1.00 55.19 ?  102 LYS   B HZ1  1 
ATOM   5359 H HZ2  . LYS   B 1 102 ? 45.442 -24.428 11.524  1.00 55.19 ?  102 LYS   B HZ2  1 
ATOM   5360 H HZ3  . LYS   B 1 102 ? 45.568 -23.968 12.892  1.00 55.19 ?  102 LYS   B HZ3  1 
ATOM   5361 N N    . GLY   B 1 103 ? 39.782 -30.042 14.381  1.00 31.56 ?  103 GLY   B N    1 
ATOM   5362 C CA   . GLY   B 1 103 ? 38.451 -30.083 14.954  1.00 31.10 ?  103 GLY   B CA   1 
ATOM   5363 C C    . GLY   B 1 103 ? 37.518 -28.985 14.498  1.00 30.09 ?  103 GLY   B C    1 
ATOM   5364 O O    . GLY   B 1 103 ? 36.437 -28.833 15.079  1.00 30.66 ?  103 GLY   B O    1 
ATOM   5365 H H    . GLY   B 1 103 ? 39.893 -30.581 13.723  1.00 37.88 ?  103 GLY   B H    1 
ATOM   5366 H HA2  . GLY   B 1 103 ? 38.040 -30.932 14.731  1.00 37.32 ?  103 GLY   B HA2  1 
ATOM   5367 H HA3  . GLY   B 1 103 ? 38.523 -30.032 15.921  1.00 37.32 ?  103 GLY   B HA3  1 
ATOM   5368 N N    A GLU   B 1 104 ? 37.897 -28.215 13.482  0.72 28.57 ?  104 GLU   B N    1 
ATOM   5369 N N    B GLU   B 1 104 ? 37.888 -28.219 13.478  0.28 29.40 ?  104 GLU   B N    1 
ATOM   5370 C CA   A GLU   B 1 104 ? 37.071 -27.113 13.018  0.72 26.89 ?  104 GLU   B CA   1 
ATOM   5371 C CA   B GLU   B 1 104 ? 37.042 -27.134 13.007  0.28 28.43 ?  104 GLU   B CA   1 
ATOM   5372 C C    A GLU   B 1 104 ? 35.891 -27.634 12.198  0.72 27.73 ?  104 GLU   B C    1 
ATOM   5373 C C    B GLU   B 1 104 ? 35.885 -27.673 12.171  0.28 28.40 ?  104 GLU   B C    1 
ATOM   5374 O O    A GLU   B 1 104 ? 35.929 -28.725 11.622  0.72 28.86 ?  104 GLU   B O    1 
ATOM   5375 O O    B GLU   B 1 104 ? 35.971 -28.745 11.564  0.28 28.74 ?  104 GLU   B O    1 
ATOM   5376 C CB   A GLU   B 1 104 ? 37.919 -26.117 12.224  0.72 25.39 ?  104 GLU   B CB   1 
ATOM   5377 C CB   B GLU   B 1 104 ? 37.873 -26.127 12.212  0.28 27.62 ?  104 GLU   B CB   1 
ATOM   5378 C CG   A GLU   B 1 104 ? 39.014 -25.492 13.079  0.72 24.02 ?  104 GLU   B CG   1 
ATOM   5379 C CG   B GLU   B 1 104 ? 38.946 -25.463 13.065  0.28 26.88 ?  104 GLU   B CG   1 
ATOM   5380 C CD   A GLU   B 1 104 ? 39.957 -24.587 12.314  0.72 22.45 ?  104 GLU   B CD   1 
ATOM   5381 C CD   B GLU   B 1 104 ? 39.901 -24.601 12.266  0.28 26.21 ?  104 GLU   B CD   1 
ATOM   5382 O OE1  A GLU   B 1 104 ? 39.974 -24.613 11.063  0.72 20.70 ?  104 GLU   B OE1  1 
ATOM   5383 O OE1  B GLU   B 1 104 ? 39.823 -24.605 11.019  0.28 25.69 ?  104 GLU   B OE1  1 
ATOM   5384 O OE2  A GLU   B 1 104 ? 40.695 -23.843 12.991  0.72 22.95 -1 104 GLU   B OE2  1 
ATOM   5385 O OE2  B GLU   B 1 104 ? 40.736 -23.917 12.893  0.28 26.31 -1 104 GLU   B OE2  1 
ATOM   5386 H H    A GLU   B 1 104 ? 38.635 -28.309 13.049  0.72 34.29 ?  104 GLU   B H    1 
ATOM   5387 H H    B GLU   B 1 104 ? 38.628 -28.302 13.048  0.28 35.28 ?  104 GLU   B H    1 
ATOM   5388 H HA   A GLU   B 1 104 ? 36.715 -26.645 13.790  0.72 32.27 ?  104 GLU   B HA   1 
ATOM   5389 H HA   B GLU   B 1 104 ? 36.667 -26.673 13.773  0.28 34.12 ?  104 GLU   B HA   1 
ATOM   5390 H HB2  A GLU   B 1 104 ? 38.342 -26.576 11.483  0.72 30.47 ?  104 GLU   B HB2  1 
ATOM   5391 H HB2  B GLU   B 1 104 ? 38.312 -26.584 11.478  0.28 33.14 ?  104 GLU   B HB2  1 
ATOM   5392 H HB3  A GLU   B 1 104 ? 37.350 -25.403 11.895  0.72 30.47 ?  104 GLU   B HB3  1 
ATOM   5393 H HB3  B GLU   B 1 104 ? 37.288 -25.432 11.870  0.28 33.14 ?  104 GLU   B HB3  1 
ATOM   5394 H HG2  A GLU   B 1 104 ? 38.606 -24.958 13.780  0.72 28.83 ?  104 GLU   B HG2  1 
ATOM   5395 H HG2  B GLU   B 1 104 ? 38.516 -24.900 13.729  0.28 32.26 ?  104 GLU   B HG2  1 
ATOM   5396 H HG3  A GLU   B 1 104 ? 39.551 -26.195 13.477  0.72 28.83 ?  104 GLU   B HG3  1 
ATOM   5397 H HG3  B GLU   B 1 104 ? 39.467 -26.152 13.509  0.28 32.26 ?  104 GLU   B HG3  1 
ATOM   5398 N N    A ASP   B 1 105 ? 34.829 -26.831 12.158  0.72 27.58 ?  105 ASP   B N    1 
ATOM   5399 N N    B ASP   B 1 105 ? 34.793 -26.911 12.147  0.28 27.96 ?  105 ASP   B N    1 
ATOM   5400 C CA   A ASP   B 1 105 ? 33.545 -27.274 11.628  0.72 28.22 ?  105 ASP   B CA   1 
ATOM   5401 C CA   B ASP   B 1 105 ? 33.536 -27.390 11.583  0.28 27.81 ?  105 ASP   B CA   1 
ATOM   5402 C C    A ASP   B 1 105 ? 33.592 -27.325 10.104  0.72 26.22 ?  105 ASP   B C    1 
ATOM   5403 C C    B ASP   B 1 105 ? 33.609 -27.403 10.060  0.28 26.87 ?  105 ASP   B C    1 
ATOM   5404 O O    A ASP   B 1 105 ? 33.731 -26.290 9.444   0.72 25.23 ?  105 ASP   B O    1 
ATOM   5405 O O    B ASP   B 1 105 ? 33.814 -26.361 9.429   0.28 26.52 ?  105 ASP   B O    1 
ATOM   5406 C CB   A ASP   B 1 105 ? 32.440 -26.331 12.100  0.72 31.62 ?  105 ASP   B CB   1 
ATOM   5407 C CB   B ASP   B 1 105 ? 32.388 -26.500 12.057  0.28 28.62 ?  105 ASP   B CB   1 
ATOM   5408 C CG   A ASP   B 1 105 ? 31.058 -26.793 11.678  0.72 34.49 ?  105 ASP   B CG   1 
ATOM   5409 C CG   B ASP   B 1 105 ? 31.025 -27.097 11.751  0.28 29.31 ?  105 ASP   B CG   1 
ATOM   5410 O OD1  A ASP   B 1 105 ? 30.945 -27.890 11.091  0.72 34.69 ?  105 ASP   B OD1  1 
ATOM   5411 O OD1  B ASP   B 1 105 ? 30.967 -28.103 11.013  0.28 29.35 ?  105 ASP   B OD1  1 
ATOM   5412 O OD2  A ASP   B 1 105 ? 30.082 -26.054 11.932  0.72 36.21 -1 105 ASP   B OD2  1 
ATOM   5413 O OD2  B ASP   B 1 105 ? 30.012 -26.570 12.260  0.28 29.49 -1 105 ASP   B OD2  1 
ATOM   5414 H H    A ASP   B 1 105 ? 34.832 -26.014 12.427  0.72 33.10 ?  105 ASP   B H    1 
ATOM   5415 H H    B ASP   B 1 105 ? 34.757 -26.110 12.450  0.28 33.55 ?  105 ASP   B H    1 
ATOM   5416 H HA   A ASP   B 1 105 ? 33.350 -28.164 11.958  0.72 33.87 ?  105 ASP   B HA   1 
ATOM   5417 H HA   B ASP   B 1 105 ? 33.363 -28.293 11.890  0.28 33.38 ?  105 ASP   B HA   1 
ATOM   5418 H HB2  A ASP   B 1 105 ? 32.470 -26.271 13.070  0.72 37.95 ?  105 ASP   B HB2  1 
ATOM   5419 H HB2  B ASP   B 1 105 ? 32.451 -26.383 13.019  0.28 34.35 ?  105 ASP   B HB2  1 
ATOM   5420 H HB3  A ASP   B 1 105 ? 32.584 -25.454 11.711  0.72 37.95 ?  105 ASP   B HB3  1 
ATOM   5421 H HB3  B ASP   B 1 105 ? 32.454 -25.634 11.617  0.28 34.35 ?  105 ASP   B HB3  1 
ATOM   5422 N N    A ILE   B 1 106 ? 33.452 -28.532 9.548   0.72 25.86 ?  106 ILE   B N    1 
ATOM   5423 N N    B ILE   B 1 106 ? 33.428 -28.589 9.471   0.28 26.32 ?  106 ILE   B N    1 
ATOM   5424 C CA   A ILE   B 1 106 ? 33.447 -28.715 8.101   0.72 24.88 ?  106 ILE   B CA   1 
ATOM   5425 C CA   B ILE   B 1 106 ? 33.441 -28.734 8.020   0.28 25.86 ?  106 ILE   B CA   1 
ATOM   5426 C C    A ILE   B 1 106 ? 32.347 -27.899 7.427   0.72 23.55 ?  106 ILE   B C    1 
ATOM   5427 C C    B ILE   B 1 106 ? 32.340 -27.914 7.358   0.28 25.28 ?  106 ILE   B C    1 
ATOM   5428 O O    A ILE   B 1 106 ? 32.452 -27.577 6.240   0.72 22.47 ?  106 ILE   B O    1 
ATOM   5429 O O    B ILE   B 1 106 ? 32.428 -27.611 6.164   0.28 24.93 ?  106 ILE   B O    1 
ATOM   5430 C CB   A ILE   B 1 106 ? 33.357 -30.225 7.773   0.72 26.00 ?  106 ILE   B CB   1 
ATOM   5431 C CB   B ILE   B 1 106 ? 33.354 -30.233 7.648   0.28 26.20 ?  106 ILE   B CB   1 
ATOM   5432 C CG1  A ILE   B 1 106 ? 33.608 -30.480 6.287   0.72 26.57 ?  106 ILE   B CG1  1 
ATOM   5433 C CG1  B ILE   B 1 106 ? 33.617 -30.446 6.155   0.28 26.37 ?  106 ILE   B CG1  1 
ATOM   5434 C CG2  A ILE   B 1 106 ? 32.003 -30.789 8.191   0.72 27.04 ?  106 ILE   B CG2  1 
ATOM   5435 C CG2  B ILE   B 1 106 ? 31.997 -30.806 8.037   0.28 26.54 ?  106 ILE   B CG2  1 
ATOM   5436 C CD1  A ILE   B 1 106 ? 34.967 -30.019 5.821   0.72 26.69 ?  106 ILE   B CD1  1 
ATOM   5437 C CD1  B ILE   B 1 106 ? 34.977 -29.970 5.705   0.28 26.47 ?  106 ILE   B CD1  1 
ATOM   5438 H H    A ILE   B 1 106 ? 33.363 -29.259 9.996   0.72 31.03 ?  106 ILE   B H    1 
ATOM   5439 H H    B ILE   B 1 106 ? 33.304 -29.324 9.896   0.28 31.59 ?  106 ILE   B H    1 
ATOM   5440 H HA   A ILE   B 1 106 ? 34.292 -28.395 7.761   0.72 29.86 ?  106 ILE   B HA   1 
ATOM   5441 H HA   B ILE   B 1 106 ? 34.286 -28.398 7.693   0.28 31.04 ?  106 ILE   B HA   1 
ATOM   5442 H HB   A ILE   B 1 106 ? 34.042 -30.689 8.280   0.72 31.20 ?  106 ILE   B HB   1 
ATOM   5443 H HB   B ILE   B 1 106 ? 34.035 -30.709 8.145   0.28 31.45 ?  106 ILE   B HB   1 
ATOM   5444 H HG12 A ILE   B 1 106 ? 33.549 -31.436 6.118   0.72 31.89 ?  106 ILE   B HG12 1 
ATOM   5445 H HG12 B ILE   B 1 106 ? 33.560 -31.397 5.961   0.28 31.65 ?  106 ILE   B HG12 1 
ATOM   5446 H HG13 A ILE   B 1 106 ? 32.940 -30.013 5.766   0.72 31.89 ?  106 ILE   B HG13 1 
ATOM   5447 H HG13 B ILE   B 1 106 ? 32.949 -29.967 5.643   0.28 31.65 ?  106 ILE   B HG13 1 
ATOM   5448 H HG21 A ILE   B 1 106 ? 32.019 -31.755 8.094   0.72 32.45 ?  106 ILE   B HG21 1 
ATOM   5449 H HG21 B ILE   B 1 106 ? 32.017 -31.769 7.920   0.28 31.86 ?  106 ILE   B HG21 1 
ATOM   5450 H HG22 A ILE   B 1 106 ? 31.836 -30.555 9.118   0.72 32.45 ?  106 ILE   B HG22 1 
ATOM   5451 H HG22 B ILE   B 1 106 ? 31.818 -30.590 8.966   0.28 31.86 ?  106 ILE   B HG22 1 
ATOM   5452 H HG23 A ILE   B 1 106 ? 31.313 -30.412 7.625   0.72 32.45 ?  106 ILE   B HG23 1 
ATOM   5453 H HG23 B ILE   B 1 106 ? 31.313 -30.418 7.470   0.28 31.86 ?  106 ILE   B HG23 1 
ATOM   5454 H HD11 A ILE   B 1 106 ? 35.163 -30.429 4.965   0.72 32.03 ?  106 ILE   B HD11 1 
ATOM   5455 H HD11 B ILE   B 1 106 ? 35.171 -30.349 4.835   0.28 31.77 ?  106 ILE   B HD11 1 
ATOM   5456 H HD12 A ILE   B 1 106 ? 34.960 -29.053 5.731   0.72 32.03 ?  106 ILE   B HD12 1 
ATOM   5457 H HD12 B ILE   B 1 106 ? 34.971 -29.002 5.650   0.28 31.77 ?  106 ILE   B HD12 1 
ATOM   5458 H HD13 A ILE   B 1 106 ? 35.634 -30.287 6.475   0.72 32.03 ?  106 ILE   B HD13 1 
ATOM   5459 H HD13 B ILE   B 1 106 ? 35.642 -30.263 6.348   0.28 31.77 ?  106 ILE   B HD13 1 
ATOM   5460 N N    A GLN   B 1 107 ? 31.288 -27.547 8.160   0.72 24.01 ?  107 GLN   B N    1 
ATOM   5461 N N    B GLN   B 1 107 ? 31.300 -27.543 8.109   0.28 25.34 ?  107 GLN   B N    1 
ATOM   5462 C CA   A GLN   B 1 107 ? 30.216 -26.740 7.584   0.72 24.46 ?  107 GLN   B CA   1 
ATOM   5463 C CA   B GLN   B 1 107 ? 30.219 -26.739 7.549   0.28 25.34 ?  107 GLN   B CA   1 
ATOM   5464 C C    A GLN   B 1 107 ? 30.710 -25.391 7.072   0.72 22.60 ?  107 GLN   B C    1 
ATOM   5465 C C    B GLN   B 1 107 ? 30.699 -25.370 7.080   0.28 23.10 ?  107 GLN   B C    1 
ATOM   5466 O O    A GLN   B 1 107 ? 30.076 -24.812 6.185   0.72 23.41 ?  107 GLN   B O    1 
ATOM   5467 O O    B GLN   B 1 107 ? 30.034 -24.749 6.244   0.28 23.50 ?  107 GLN   B O    1 
ATOM   5468 C CB   A GLN   B 1 107 ? 29.106 -26.540 8.621   0.72 28.31 ?  107 GLN   B CB   1 
ATOM   5469 C CB   B GLN   B 1 107 ? 29.102 -26.585 8.586   0.28 27.86 ?  107 GLN   B CB   1 
ATOM   5470 C CG   A GLN   B 1 107 ? 27.786 -26.018 8.057   0.72 32.44 ?  107 GLN   B CG   1 
ATOM   5471 C CG   B GLN   B 1 107 ? 27.778 -26.069 8.032   0.28 30.31 ?  107 GLN   B CG   1 
ATOM   5472 C CD   A GLN   B 1 107 ? 27.737 -24.503 7.964   0.72 35.57 ?  107 GLN   B CD   1 
ATOM   5473 C CD   B GLN   B 1 107 ? 27.677 -24.556 8.056   0.28 32.24 ?  107 GLN   B CD   1 
ATOM   5474 O OE1  A GLN   B 1 107 ? 28.581 -23.805 8.529   0.72 36.71 ?  107 GLN   B OE1  1 
ATOM   5475 O OE1  B GLN   B 1 107 ? 28.525 -23.872 8.632   0.28 32.90 ?  107 GLN   B OE1  1 
ATOM   5476 N NE2  A GLN   B 1 107 ? 26.740 -23.985 7.249   0.72 36.67 ?  107 GLN   B NE2  1 
ATOM   5477 N NE2  B GLN   B 1 107 ? 26.632 -24.023 7.430   0.28 32.95 ?  107 GLN   B NE2  1 
ATOM   5478 H H    A GLN   B 1 107 ? 31.170 -27.762 8.978   0.72 28.82 ?  107 GLN   B H    1 
ATOM   5479 H H    B GLN   B 1 107 ? 31.195 -27.747 8.935   0.28 30.41 ?  107 GLN   B H    1 
ATOM   5480 H HA   A GLN   B 1 107 ? 29.835 -27.222 6.831   0.72 29.36 ?  107 GLN   B HA   1 
ATOM   5481 H HA   B GLN   B 1 107 ? 29.847 -27.203 6.783   0.28 30.41 ?  107 GLN   B HA   1 
ATOM   5482 H HB2  A GLN   B 1 107 ? 28.926 -27.391 9.043   0.72 33.98 ?  107 GLN   B HB2  1 
ATOM   5483 H HB2  B GLN   B 1 107 ? 28.931 -27.450 8.983   0.28 33.44 ?  107 GLN   B HB2  1 
ATOM   5484 H HB3  A GLN   B 1 107 ? 29.417 -25.905 9.284   0.72 33.98 ?  107 GLN   B HB3  1 
ATOM   5485 H HB3  B GLN   B 1 107 ? 29.397 -25.966 9.272   0.28 33.44 ?  107 GLN   B HB3  1 
ATOM   5486 H HG2  A GLN   B 1 107 ? 27.657 -26.373 7.165   0.72 38.93 ?  107 GLN   B HG2  1 
ATOM   5487 H HG2  B GLN   B 1 107 ? 27.683 -26.360 7.112   0.28 36.37 ?  107 GLN   B HG2  1 
ATOM   5488 H HG3  A GLN   B 1 107 ? 27.060 -26.309 8.636   0.72 38.93 ?  107 GLN   B HG3  1 
ATOM   5489 H HG3  B GLN   B 1 107 ? 27.050 -26.429 8.568   0.28 36.37 ?  107 GLN   B HG3  1 
ATOM   5490 H HE21 A GLN   B 1 107 ? 26.168 -24.504 6.867   0.72 44.01 ?  107 GLN   B HE21 1 
ATOM   5491 H HE21 B GLN   B 1 107 ? 26.060 -24.532 7.037   0.28 39.55 ?  107 GLN   B HE21 1 
ATOM   5492 H HE22 A GLN   B 1 107 ? 26.662 -23.132 7.169   0.72 44.01 ?  107 GLN   B HE22 1 
ATOM   5493 H HE22 B GLN   B 1 107 ? 26.528 -23.170 7.418   0.28 39.55 ?  107 GLN   B HE22 1 
ATOM   5494 N N    . LEU   B 1 108 ? 31.835 -24.888 7.587   1.00 20.71 ?  108 LEU   B N    1 
ATOM   5495 C CA   . LEU   B 1 108 ? 32.370 -23.590 7.175   1.00 18.28 ?  108 LEU   B CA   1 
ATOM   5496 C C    . LEU   B 1 108 ? 33.025 -23.610 5.802   1.00 16.13 ?  108 LEU   B C    1 
ATOM   5497 O O    . LEU   B 1 108 ? 33.463 -22.552 5.321   1.00 15.58 ?  108 LEU   B O    1 
ATOM   5498 C CB   . LEU   B 1 108 ? 33.366 -23.084 8.215   1.00 18.90 ?  108 LEU   B CB   1 
ATOM   5499 C CG   . LEU   B 1 108 ? 32.727 -22.647 9.530   1.00 20.46 ?  108 LEU   B CG   1 
ATOM   5500 C CD1  . LEU   B 1 108 ? 33.754 -22.595 10.644  1.00 20.82 ?  108 LEU   B CD1  1 
ATOM   5501 C CD2  . LEU   B 1 108 ? 32.070 -21.290 9.357   1.00 22.09 ?  108 LEU   B CD2  1 
ATOM   5502 H H    A LEU   B 1 108 ? 32.301 -25.280 8.189   0.72 24.86 ?  108 LEU   B H    1 
ATOM   5503 H H    B LEU   B 1 108 ? 32.306 -25.291 8.178   0.28 24.86 ?  108 LEU   B H    1 
ATOM   5504 H HA   . LEU   B 1 108 ? 31.638 -22.957 7.135   1.00 21.94 ?  108 LEU   B HA   1 
ATOM   5505 H HB2  . LEU   B 1 108 ? 33.992 -23.795 8.415   1.00 22.68 ?  108 LEU   B HB2  1 
ATOM   5506 H HB3  . LEU   B 1 108 ? 33.835 -22.322 7.848   1.00 22.68 ?  108 LEU   B HB3  1 
ATOM   5507 H HG   . LEU   B 1 108 ? 32.037 -23.285 9.783   1.00 24.56 ?  108 LEU   B HG   1 
ATOM   5508 H HD11 . LEU   B 1 108 ? 33.314 -22.329 11.469  1.00 24.99 ?  108 LEU   B HD11 1 
ATOM   5509 H HD12 . LEU   B 1 108 ? 34.150 -23.473 10.750  1.00 24.99 ?  108 LEU   B HD12 1 
ATOM   5510 H HD13 . LEU   B 1 108 ? 34.437 -21.947 10.413  1.00 24.99 ?  108 LEU   B HD13 1 
ATOM   5511 H HD21 . LEU   B 1 108 ? 31.717 -20.997 10.211  1.00 26.52 ?  108 LEU   B HD21 1 
ATOM   5512 H HD22 . LEU   B 1 108 ? 32.733 -20.659 9.038   1.00 26.52 ?  108 LEU   B HD22 1 
ATOM   5513 H HD23 . LEU   B 1 108 ? 31.349 -21.366 8.711   1.00 26.52 ?  108 LEU   B HD23 1 
ATOM   5514 N N    . LEU   B 1 109 ? 33.096 -24.777 5.164   1.00 15.21 ?  109 LEU   B N    1 
ATOM   5515 C CA   . LEU   B 1 109 ? 33.731 -24.881 3.859   1.00 13.88 ?  109 LEU   B CA   1 
ATOM   5516 C C    . LEU   B 1 109 ? 32.970 -24.093 2.801   1.00 13.29 ?  109 LEU   B C    1 
ATOM   5517 O O    . LEU   B 1 109 ? 33.584 -23.502 1.906   1.00 13.39 ?  109 LEU   B O    1 
ATOM   5518 C CB   . LEU   B 1 109 ? 33.847 -26.358 3.477   1.00 14.30 ?  109 LEU   B CB   1 
ATOM   5519 C CG   . LEU   B 1 109 ? 34.632 -26.692 2.214   1.00 14.40 ?  109 LEU   B CG   1 
ATOM   5520 C CD1  . LEU   B 1 109 ? 36.006 -26.032 2.240   1.00 14.39 ?  109 LEU   B CD1  1 
ATOM   5521 C CD2  . LEU   B 1 109 ? 34.764 -28.204 2.079   1.00 15.27 ?  109 LEU   B CD2  1 
ATOM   5522 H H    . LEU   B 1 109 ? 32.787 -25.521 5.461   1.00 18.25 ?  109 LEU   B H    1 
ATOM   5523 H HA   . LEU   B 1 109 ? 34.624 -24.515 3.910   1.00 16.67 ?  109 LEU   B HA   1 
ATOM   5524 H HB2  . LEU   B 1 109 ? 34.281 -26.826 4.206   1.00 17.17 ?  109 LEU   B HB2  1 
ATOM   5525 H HB3  . LEU   B 1 109 ? 32.954 -26.715 3.353   1.00 17.17 ?  109 LEU   B HB3  1 
ATOM   5526 H HG   . LEU   B 1 109 ? 34.151 -26.368 1.435   1.00 17.28 ?  109 LEU   B HG   1 
ATOM   5527 H HD11 . LEU   B 1 109 ? 36.550 -26.402 1.524   1.00 17.27 ?  109 LEU   B HD11 1 
ATOM   5528 H HD12 . LEU   B 1 109 ? 35.899 -25.078 2.113   1.00 17.27 ?  109 LEU   B HD12 1 
ATOM   5529 H HD13 . LEU   B 1 109 ? 36.425 -26.212 3.096   1.00 17.27 ?  109 LEU   B HD13 1 
ATOM   5530 H HD21 . LEU   B 1 109 ? 35.335 -28.409 1.319   1.00 18.33 ?  109 LEU   B HD21 1 
ATOM   5531 H HD22 . LEU   B 1 109 ? 35.156 -28.563 2.890   1.00 18.33 ?  109 LEU   B HD22 1 
ATOM   5532 H HD23 . LEU   B 1 109 ? 33.883 -28.591 1.940   1.00 18.33 ?  109 LEU   B HD23 1 
ATOM   5533 N N    . LYS   B 1 110 ? 31.636 -24.055 2.885   1.00 13.27 ?  110 LYS   B N    1 
ATOM   5534 C CA   . LYS   B 1 110 ? 30.879 -23.294 1.896   1.00 12.99 ?  110 LYS   B CA   1 
ATOM   5535 C C    . LYS   B 1 110 ? 31.216 -21.805 1.984   1.00 12.80 ?  110 LYS   B C    1 
ATOM   5536 O O    . LYS   B 1 110 ? 31.477 -21.159 0.967   1.00 12.55 ?  110 LYS   B O    1 
ATOM   5537 C CB   . LYS   B 1 110 ? 29.374 -23.538 2.044   1.00 13.68 ?  110 LYS   B CB   1 
ATOM   5538 C CG   . LYS   B 1 110 ? 28.566 -22.916 0.907   1.00 13.86 ?  110 LYS   B CG   1 
ATOM   5539 C CD   . LYS   B 1 110 ? 27.103 -23.349 0.924   1.00 14.62 ?  110 LYS   B CD   1 
ATOM   5540 C CE   . LYS   B 1 110 ? 26.347 -22.807 -0.290  1.00 15.49 ?  110 LYS   B CE   1 
ATOM   5541 N NZ   . LYS   B 1 110 ? 26.665 -23.535 -1.545  1.00 15.70 ?  110 LYS   B NZ   1 
ATOM   5542 H H    . LYS   B 1 110 ? 31.162 -24.456 3.475   1.00 15.93 ?  110 LYS   B H    1 
ATOM   5543 H HA   . LYS   B 1 110 ? 31.134 -23.597 1.006   1.00 15.59 ?  110 LYS   B HA   1 
ATOM   5544 H HB2  . LYS   B 1 110 ? 29.205 -24.497 2.038   1.00 16.42 ?  110 LYS   B HB2  1 
ATOM   5545 H HB3  . LYS   B 1 110 ? 29.068 -23.153 2.877   1.00 16.42 ?  110 LYS   B HB3  1 
ATOM   5546 H HG2  . LYS   B 1 110 ? 28.587 -21.949 0.991   1.00 16.63 ?  110 LYS   B HG2  1 
ATOM   5547 H HG3  . LYS   B 1 110 ? 28.943 -23.185 0.056   1.00 16.63 ?  110 LYS   B HG3  1 
ATOM   5548 H HD2  . LYS   B 1 110 ? 27.050 -24.321 0.903   1.00 17.55 ?  110 LYS   B HD2  1 
ATOM   5549 H HD3  . LYS   B 1 110 ? 26.670 -23.011 1.726   1.00 17.55 ?  110 LYS   B HD3  1 
ATOM   5550 H HE2  . LYS   B 1 110 ? 25.394 -22.884 -0.133  1.00 18.60 ?  110 LYS   B HE2  1 
ATOM   5551 H HE3  . LYS   B 1 110 ? 26.588 -21.875 -0.416  1.00 18.60 ?  110 LYS   B HE3  1 
ATOM   5552 H HZ1  . LYS   B 1 110 ? 26.212 -23.188 -2.225  1.00 18.84 ?  110 LYS   B HZ1  1 
ATOM   5553 H HZ2  . LYS   B 1 110 ? 27.539 -23.476 -1.719  1.00 18.84 ?  110 LYS   B HZ2  1 
ATOM   5554 H HZ3  . LYS   B 1 110 ? 26.449 -24.396 -1.461  1.00 18.84 ?  110 LYS   B HZ3  1 
ATOM   5555 N N    . SER   B 1 111 ? 31.238 -21.254 3.202   1.00 13.35 ?  111 SER   B N    1 
ATOM   5556 C CA   . SER   B 1 111 ? 31.627 -19.855 3.377   1.00 13.14 ?  111 SER   B CA   1 
ATOM   5557 C C    . SER   B 1 111 ? 33.006 -19.594 2.788   1.00 12.90 ?  111 SER   B C    1 
ATOM   5558 O O    . SER   B 1 111 ? 33.230 -18.559 2.143   1.00 12.97 ?  111 SER   B O    1 
ATOM   5559 C CB   . SER   B 1 111 ? 31.624 -19.493 4.861   1.00 14.54 ?  111 SER   B CB   1 
ATOM   5560 O OG   . SER   B 1 111 ? 30.315 -19.503 5.387   1.00 15.94 ?  111 SER   B OG   1 
ATOM   5561 H H    . SER   B 1 111 ? 31.042 -21.670 3.926   1.00 16.03 ?  111 SER   B H    1 
ATOM   5562 H HA   . SER   B 1 111 ? 30.993 -19.289 2.921   1.00 15.77 ?  111 SER   B HA   1 
ATOM   5563 H HB2  . SER   B 1 111 ? 32.160 -20.141 5.347   1.00 17.45 ?  111 SER   B HB2  1 
ATOM   5564 H HB3  . SER   B 1 111 ? 31.995 -18.607 4.970   1.00 17.45 ?  111 SER   B HB3  1 
ATOM   5565 H HG   . SER   B 1 111 ? 30.328 -19.305 6.209   1.00 19.14 ?  111 SER   B HG   1 
ATOM   5566 N N    . ALA   B 1 112 ? 33.947 -20.512 3.014   1.00 12.86 ?  112 ALA   B N    1 
ATOM   5567 C CA   . ALA   B 1 112 ? 35.293 -20.346 2.475   1.00 12.51 ?  112 ALA   B CA   1 
ATOM   5568 C C    . ALA   B 1 112 ? 35.264 -20.252 0.952   1.00 11.74 ?  112 ALA   B C    1 
ATOM   5569 O O    . ALA   B 1 112 ? 35.892 -19.365 0.360   1.00 12.18 ?  112 ALA   B O    1 
ATOM   5570 C CB   . ALA   B 1 112 ? 36.196 -21.487 2.955   1.00 12.99 ?  112 ALA   B CB   1 
ATOM   5571 H H    . ALA   B 1 112 ? 33.837 -21.231 3.481   1.00 15.44 ?  112 ALA   B H    1 
ATOM   5572 H HA   . ALA   B 1 112 ? 35.664 -19.517 2.814   1.00 15.01 ?  112 ALA   B HA   1 
ATOM   5573 H HB1  . ALA   B 1 112 ? 37.088 -21.356 2.591   1.00 15.59 ?  112 ALA   B HB1  1 
ATOM   5574 H HB2  . ALA   B 1 112 ? 36.235 -21.472 3.926   1.00 15.59 ?  112 ALA   B HB2  1 
ATOM   5575 H HB3  . ALA   B 1 112 ? 35.834 -22.330 2.650   1.00 15.59 ?  112 ALA   B HB3  1 
ATOM   5576 N N    . TYR   B 1 113 ? 34.529 -21.157 0.295   1.00 11.83 ?  113 TYR   B N    1 
ATOM   5577 C CA   . TYR   B 1 113 ? 34.456 -21.107 -1.161  1.00 11.43 ?  113 TYR   B CA   1 
ATOM   5578 C C    . TYR   B 1 113 ? 33.743 -19.857 -1.675  1.00 11.51 ?  113 TYR   B C    1 
ATOM   5579 O O    . TYR   B 1 113 ? 34.013 -19.423 -2.799  1.00 11.44 ?  113 TYR   B O    1 
ATOM   5580 C CB   . TYR   B 1 113 ? 33.780 -22.364 -1.711  1.00 11.75 ?  113 TYR   B CB   1 
ATOM   5581 C CG   . TYR   B 1 113 ? 34.739 -23.517 -1.971  1.00 12.30 ?  113 TYR   B CG   1 
ATOM   5582 C CD1  . TYR   B 1 113 ? 35.740 -23.408 -2.926  1.00 12.73 ?  113 TYR   B CD1  1 
ATOM   5583 C CD2  . TYR   B 1 113 ? 34.636 -24.710 -1.270  1.00 12.39 ?  113 TYR   B CD2  1 
ATOM   5584 C CE1  . TYR   B 1 113 ? 36.620 -24.440 -3.175  1.00 12.74 ?  113 TYR   B CE1  1 
ATOM   5585 C CE2  . TYR   B 1 113 ? 35.509 -25.763 -1.515  1.00 12.99 ?  113 TYR   B CE2  1 
ATOM   5586 C CZ   . TYR   B 1 113 ? 36.494 -25.624 -2.475  1.00 12.69 ?  113 TYR   B CZ   1 
ATOM   5587 O OH   . TYR   B 1 113 ? 37.381 -26.639 -2.750  1.00 13.53 ?  113 TYR   B OH   1 
ATOM   5588 H H    . TYR   B 1 113 ? 34.067 -21.789 0.666   1.00 14.21 ?  113 TYR   B H    1 
ATOM   5589 H HA   . TYR   B 1 113 ? 35.356 -21.088 -1.501  1.00 13.72 ?  113 TYR   B HA   1 
ATOM   5590 H HB2  . TYR   B 1 113 ? 33.115 -22.677 -1.074  1.00 14.10 ?  113 TYR   B HB2  1 
ATOM   5591 H HB3  . TYR   B 1 113 ? 33.344 -22.145 -2.551  1.00 14.10 ?  113 TYR   B HB3  1 
ATOM   5592 H HD1  . TYR   B 1 113 ? 35.828 -22.611 -3.409  1.00 15.28 ?  113 TYR   B HD1  1 
ATOM   5593 H HD2  . TYR   B 1 113 ? 33.962 -24.808 -0.637  1.00 14.87 ?  113 TYR   B HD2  1 
ATOM   5594 H HE1  . TYR   B 1 113 ? 37.282 -24.346 -3.825  1.00 15.29 ?  113 TYR   B HE1  1 
ATOM   5595 H HE2  . TYR   B 1 113 ? 35.418 -26.561 -1.047  1.00 15.60 ?  113 TYR   B HE2  1 
ATOM   5596 H HH   . TYR   B 1 113 ? 37.205 -27.310 -2.274  1.00 16.25 ?  113 TYR   B HH   1 
ATOM   5597 N N    . GLU   B 1 114 ? 32.826 -19.273 -0.892  1.00 11.55 ?  114 GLU   B N    1 
ATOM   5598 C CA   . GLU   B 1 114 ? 32.141 -18.066 -1.350  1.00 11.34 ?  114 GLU   B CA   1 
ATOM   5599 C C    . GLU   B 1 114 ? 33.125 -16.942 -1.650  1.00 11.21 ?  114 GLU   B C    1 
ATOM   5600 O O    . GLU   B 1 114 ? 32.843 -16.080 -2.488  1.00 11.63 ?  114 GLU   B O    1 
ATOM   5601 C CB   . GLU   B 1 114 ? 31.076 -17.638 -0.333  1.00 12.10 ?  114 GLU   B CB   1 
ATOM   5602 C CG   . GLU   B 1 114 ? 29.861 -18.564 -0.392  1.00 12.26 ?  114 GLU   B CG   1 
ATOM   5603 C CD   . GLU   B 1 114 ? 28.835 -18.378 0.718   1.00 12.34 ?  114 GLU   B CD   1 
ATOM   5604 O OE1  . GLU   B 1 114 ? 29.128 -17.750 1.761   1.00 12.54 ?  114 GLU   B OE1  1 
ATOM   5605 O OE2  . GLU   B 1 114 ? 27.712 -18.910 0.546   1.00 13.35 -1 114 GLU   B OE2  1 
ATOM   5606 H H    . GLU   B 1 114 ? 32.578 -19.559 -0.114  1.00 13.87 ?  114 GLU   B H    1 
ATOM   5607 H HA   . GLU   B 1 114 ? 31.684 -18.270 -2.172  1.00 13.61 ?  114 GLU   B HA   1 
ATOM   5608 H HB2  . GLU   B 1 114 ? 31.446 -17.678 0.564   1.00 14.53 ?  114 GLU   B HB2  1 
ATOM   5609 H HB3  . GLU   B 1 114 ? 30.780 -16.738 -0.536  1.00 14.53 ?  114 GLU   B HB3  1 
ATOM   5610 H HG2  . GLU   B 1 114 ? 29.413 -18.424 -1.237  1.00 14.71 ?  114 GLU   B HG2  1 
ATOM   5611 H HG3  . GLU   B 1 114 ? 30.180 -19.483 -0.342  1.00 14.71 ?  114 GLU   B HG3  1 
ATOM   5612 N N    . ASN   B 1 115 ? 34.289 -16.940 -0.998  1.00 11.29 ?  115 ASN   B N    1 
ATOM   5613 C CA   . ASN   B 1 115 ? 35.278 -15.907 -1.296  1.00 11.07 ?  115 ASN   B CA   1 
ATOM   5614 C C    . ASN   B 1 115 ? 35.690 -15.928 -2.760  1.00 10.91 ?  115 ASN   B C    1 
ATOM   5615 O O    . ASN   B 1 115 ? 36.076 -14.888 -3.316  1.00 11.60 ?  115 ASN   B O    1 
ATOM   5616 C CB   . ASN   B 1 115 ? 36.519 -16.078 -0.413  1.00 11.85 ?  115 ASN   B CB   1 
ATOM   5617 C CG   . ASN   B 1 115 ? 36.251 -15.815 1.045   1.00 12.34 ?  115 ASN   B CG   1 
ATOM   5618 O OD1  . ASN   B 1 115 ? 36.242 -14.668 1.487   1.00 14.06 ?  115 ASN   B OD1  1 
ATOM   5619 N ND2  . ASN   B 1 115 ? 36.081 -16.883 1.818   1.00 12.60 ?  115 ASN   B ND2  1 
ATOM   5620 H H    . ASN   B 1 115 ? 34.526 -17.507 -0.388  1.00 13.55 ?  115 ASN   B H    1 
ATOM   5621 H HA   . ASN   B 1 115 ? 34.898 -15.039 -1.105  1.00 13.29 ?  115 ASN   B HA   1 
ATOM   5622 H HB2  . ASN   B 1 115 ? 36.852 -16.984 -0.500  1.00 14.23 ?  115 ASN   B HB2  1 
ATOM   5623 H HB3  . ASN   B 1 115 ? 37.201 -15.448 -0.703  1.00 14.23 ?  115 ASN   B HB3  1 
ATOM   5624 H HD21 . ASN   B 1 115 ? 35.933 -16.787 2.660   1.00 15.13 ?  115 ASN   B HD21 1 
ATOM   5625 H HD22 . ASN   B 1 115 ? 36.112 -17.673 1.476   1.00 15.13 ?  115 ASN   B HD22 1 
ATOM   5626 N N    . PHE   B 1 116 ? 35.666 -17.107 -3.393  1.00 10.73 ?  116 PHE   B N    1 
ATOM   5627 C CA   . PHE   B 1 116 ? 36.095 -17.205 -4.783  1.00 11.26 ?  116 PHE   B CA   1 
ATOM   5628 C C    . PHE   B 1 116 ? 35.198 -16.377 -5.699  1.00 11.05 ?  116 PHE   B C    1 
ATOM   5629 O O    . PHE   B 1 116 ? 35.635 -15.949 -6.771  1.00 11.38 ?  116 PHE   B O    1 
ATOM   5630 C CB   . PHE   B 1 116 ? 36.056 -18.656 -5.294  1.00 10.87 ?  116 PHE   B CB   1 
ATOM   5631 C CG   . PHE   B 1 116 ? 37.131 -19.600 -4.750  1.00 10.70 ?  116 PHE   B CG   1 
ATOM   5632 C CD1  . PHE   B 1 116 ? 37.786 -19.411 -3.544  1.00 11.99 ?  116 PHE   B CD1  1 
ATOM   5633 C CD2  . PHE   B 1 116 ? 37.438 -20.736 -5.489  1.00 11.12 ?  116 PHE   B CD2  1 
ATOM   5634 C CE1  . PHE   B 1 116 ? 38.722 -20.348 -3.095  1.00 11.81 ?  116 PHE   B CE1  1 
ATOM   5635 C CE2  . PHE   B 1 116 ? 38.363 -21.671 -5.046  1.00 11.42 ?  116 PHE   B CE2  1 
ATOM   5636 C CZ   . PHE   B 1 116 ? 39.005 -21.479 -3.854  1.00 11.47 ?  116 PHE   B CZ   1 
ATOM   5637 H H    . PHE   B 1 116 ? 35.406 -17.856 -3.042  1.00 12.88 ?  116 PHE   B H    1 
ATOM   5638 H HA   . PHE   B 1 116 ? 37.005 -16.883 -4.866  1.00 13.52 ?  116 PHE   B HA   1 
ATOM   5639 H HB2  . PHE   B 1 116 ? 35.187 -19.036 -5.060  1.00 13.05 ?  116 PHE   B HB2  1 
ATOM   5640 H HB3  . PHE   B 1 116 ? 36.140 -18.643 -6.261  1.00 13.05 ?  116 PHE   B HB3  1 
ATOM   5641 H HD1  . PHE   B 1 116 ? 37.587 -18.665 -3.025  1.00 14.40 ?  116 PHE   B HD1  1 
ATOM   5642 H HD2  . PHE   B 1 116 ? 36.994 -20.888 -6.292  1.00 13.36 ?  116 PHE   B HD2  1 
ATOM   5643 H HE1  . PHE   B 1 116 ? 39.165 -20.210 -2.290  1.00 14.18 ?  116 PHE   B HE1  1 
ATOM   5644 H HE2  . PHE   B 1 116 ? 38.557 -22.416 -5.563  1.00 13.71 ?  116 PHE   B HE2  1 
ATOM   5645 H HZ   . PHE   B 1 116 ? 39.647 -22.086 -3.564  1.00 13.77 ?  116 PHE   B HZ   1 
ATOM   5646 N N    . ASN   B 1 117 ? 33.926 -16.176 -5.320  1.00 11.43 ?  117 ASN   B N    1 
ATOM   5647 C CA   . ASN   B 1 117 ? 32.979 -15.470 -6.187  1.00 11.49 ?  117 ASN   B CA   1 
ATOM   5648 C C    . ASN   B 1 117 ? 33.294 -13.990 -6.333  1.00 11.76 ?  117 ASN   B C    1 
ATOM   5649 O O    . ASN   B 1 117 ? 32.703 -13.332 -7.191  1.00 12.97 ?  117 ASN   B O    1 
ATOM   5650 C CB   . ASN   B 1 117 ? 31.555 -15.689 -5.693  1.00 11.87 ?  117 ASN   B CB   1 
ATOM   5651 C CG   . ASN   B 1 117 ? 31.103 -17.102 -5.944  1.00 11.91 ?  117 ASN   B CG   1 
ATOM   5652 O OD1  . ASN   B 1 117 ? 31.456 -17.691 -6.967  1.00 12.79 ?  117 ASN   B OD1  1 
ATOM   5653 N ND2  . ASN   B 1 117 ? 30.362 -17.673 -5.008  1.00 12.13 ?  117 ASN   B ND2  1 
ATOM   5654 H H    . ASN   B 1 117 ? 33.596 -16.438 -4.565  1.00 13.73 ?  117 ASN   B H    1 
ATOM   5655 H HA   . ASN   B 1 117 ? 33.038 -15.866 -7.065  1.00 13.79 ?  117 ASN   B HA   1 
ATOM   5656 H HB2  . ASN   B 1 117 ? 31.514 -15.522 -4.734  1.00 14.25 ?  117 ASN   B HB2  1 
ATOM   5657 H HB3  . ASN   B 1 117 ? 30.957 -15.084 -6.160  1.00 14.25 ?  117 ASN   B HB3  1 
ATOM   5658 H HD21 . ASN   B 1 117 ? 30.076 -18.478 -5.112  1.00 14.56 ?  117 ASN   B HD21 1 
ATOM   5659 H HD22 . ASN   B 1 117 ? 30.139 -17.230 -4.301  1.00 14.56 ?  117 ASN   B HD22 1 
ATOM   5660 N N    . GLN   B 1 118 ? 34.232 -13.467 -5.555  1.00 11.38 ?  118 GLN   B N    1 
ATOM   5661 C CA   . GLN   B 1 118 ? 34.661 -12.079 -5.698  1.00 12.21 ?  118 GLN   B CA   1 
ATOM   5662 C C    . GLN   B 1 118 ? 35.732 -11.890 -6.766  1.00 12.44 ?  118 GLN   B C    1 
ATOM   5663 O O    . GLN   B 1 118 ? 36.202 -10.763 -6.947  1.00 13.61 ?  118 GLN   B O    1 
ATOM   5664 C CB   . GLN   B 1 118 ? 35.145 -11.544 -4.347  1.00 12.65 ?  118 GLN   B CB   1 
ATOM   5665 C CG   . GLN   B 1 118 ? 34.063 -11.585 -3.276  1.00 12.67 ?  118 GLN   B CG   1 
ATOM   5666 C CD   . GLN   B 1 118 ? 32.885 -10.677 -3.605  1.00 12.88 ?  118 GLN   B CD   1 
ATOM   5667 O OE1  . GLN   B 1 118 ? 33.068 -9.533  -4.039  1.00 13.55 ?  118 GLN   B OE1  1 
ATOM   5668 N NE2  . GLN   B 1 118 ? 31.674 -11.175 -3.397  1.00 13.28 ?  118 GLN   B NE2  1 
ATOM   5669 H H    . GLN   B 1 118 ? 34.652 -13.894 -4.932  1.00 13.67 ?  118 GLN   B H    1 
ATOM   5670 H HA   . GLN   B 1 118 ? 33.896 -11.550 -5.967  1.00 14.65 ?  118 GLN   B HA   1 
ATOM   5671 H HB2  . GLN   B 1 118 ? 35.894 -12.072 -4.042  1.00 15.19 ?  118 GLN   B HB2  1 
ATOM   5672 H HB3  . GLN   B 1 118 ? 35.419 -10.613 -4.455  1.00 15.19 ?  118 GLN   B HB3  1 
ATOM   5673 H HG2  . GLN   B 1 118 ? 33.733 -12.493 -3.197  1.00 15.21 ?  118 GLN   B HG2  1 
ATOM   5674 H HG3  . GLN   B 1 118 ? 34.444 -11.296 -2.430  1.00 15.21 ?  118 GLN   B HG3  1 
ATOM   5675 H HE21 . GLN   B 1 118 ? 31.588 -11.975 -3.089  1.00 15.94 ?  118 GLN   B HE21 1 
ATOM   5676 H HE22 . GLN   B 1 118 ? 30.986 -10.698 -3.563  1.00 15.94 ?  118 GLN   B HE22 1 
ATOM   5677 N N    . HIS   B 1 119 ? 36.096 -12.945 -7.496  1.00 11.53 ?  119 HIS   B N    1 
ATOM   5678 C CA   . HIS   B 1 119 ? 37.132 -12.893 -8.520  1.00 11.89 ?  119 HIS   B CA   1 
ATOM   5679 C C    . HIS   B 1 119 ? 36.652 -13.624 -9.759  1.00 12.07 ?  119 HIS   B C    1 
ATOM   5680 O O    . HIS   B 1 119 ? 36.144 -14.740 -9.656  1.00 12.69 ?  119 HIS   B O    1 
ATOM   5681 C CB   . HIS   B 1 119 ? 38.415 -13.524 -7.980  1.00 12.46 ?  119 HIS   B CB   1 
ATOM   5682 C CG   . HIS   B 1 119 ? 38.886 -12.841 -6.743  1.00 13.84 ?  119 HIS   B CG   1 
ATOM   5683 N ND1  . HIS   B 1 119 ? 39.678 -11.713 -6.778  1.00 15.48 ?  119 HIS   B ND1  1 
ATOM   5684 C CD2  . HIS   B 1 119 ? 38.575 -13.048 -5.442  1.00 14.92 ?  119 HIS   B CD2  1 
ATOM   5685 C CE1  . HIS   B 1 119 ? 39.869 -11.283 -5.544  1.00 16.58 ?  119 HIS   B CE1  1 
ATOM   5686 N NE2  . HIS   B 1 119 ? 39.208 -12.071 -4.716  1.00 16.76 ?  119 HIS   B NE2  1 
ATOM   5687 H H    . HIS   B 1 119 ? 35.737 -13.728 -7.418  1.00 13.84 ?  119 HIS   B H    1 
ATOM   5688 H HA   . HIS   B 1 119 ? 37.308 -11.968 -8.759  1.00 14.28 ?  119 HIS   B HA   1 
ATOM   5689 H HB2  . HIS   B 1 119 ? 38.250 -14.454 -7.777  1.00 14.96 ?  119 HIS   B HB2  1 
ATOM   5690 H HB3  . HIS   B 1 119 ? 39.111 -13.445 -8.655  1.00 14.96 ?  119 HIS   B HB3  1 
ATOM   5691 H HD2  . HIS   B 1 119 ? 38.040 -13.735 -5.106  1.00 17.91 ?  119 HIS   B HD2  1 
ATOM   5692 H HE1  . HIS   B 1 119 ? 40.395 -10.561 -5.294  1.00 19.91 ?  119 HIS   B HE1  1 
ATOM   5693 H HE2  . HIS   B 1 119 ? 39.202 -12.009 -3.856  1.00 20.12 ?  119 HIS   B HE2  1 
ATOM   5694 N N    . GLU   B 1 120 ? 36.809 -13.008 -10.929 1.00 12.80 ?  120 GLU   B N    1 
ATOM   5695 C CA   . GLU   B 1 120 ? 36.220 -13.594 -12.129 1.00 13.93 ?  120 GLU   B CA   1 
ATOM   5696 C C    . GLU   B 1 120 ? 36.896 -14.894 -12.543 1.00 12.66 ?  120 GLU   B C    1 
ATOM   5697 O O    . GLU   B 1 120 ? 36.231 -15.765 -13.119 1.00 12.91 ?  120 GLU   B O    1 
ATOM   5698 C CB   . GLU   B 1 120 ? 36.223 -12.587 -13.276 1.00 18.63 ?  120 GLU   B CB   1 
ATOM   5699 C CG   . GLU   B 1 120 ? 35.273 -11.426 -13.048 1.00 24.89 ?  120 GLU   B CG   1 
ATOM   5700 C CD   . GLU   B 1 120 ? 35.123 -10.548 -14.269 1.00 30.96 ?  120 GLU   B CD   1 
ATOM   5701 O OE1  . GLU   B 1 120 ? 36.118 -10.376 -15.007 1.00 33.11 ?  120 GLU   B OE1  1 
ATOM   5702 O OE2  . GLU   B 1 120 ? 34.007 -10.035 -14.491 1.00 33.87 -1 120 GLU   B OE2  1 
ATOM   5703 H H    . GLU   B 1 120 ? 37.229 -12.266 -11.058 1.00 15.36 ?  120 GLU   B H    1 
ATOM   5704 H HA   . GLU   B 1 120 ? 35.297 -13.808 -11.942 1.00 16.72 ?  120 GLU   B HA   1 
ATOM   5705 H HB2  . GLU   B 1 120 ? 37.111 -12.221 -13.383 1.00 22.36 ?  120 GLU   B HB2  1 
ATOM   5706 H HB3  . GLU   B 1 120 ? 35.946 -13.033 -14.094 1.00 22.36 ?  120 GLU   B HB3  1 
ATOM   5707 H HG2  . GLU   B 1 120 ? 34.391 -11.769 -12.827 1.00 29.87 ?  120 GLU   B HG2  1 
ATOM   5708 H HG3  . GLU   B 1 120 ? 35.605 -10.876 -12.322 1.00 29.87 ?  120 GLU   B HG3  1 
ATOM   5709 N N    . VAL   B 1 121 ? 38.198 -15.035 -12.283 1.00 12.33 ?  121 VAL   B N    1 
ATOM   5710 C CA   . VAL   B 1 121 ? 38.944 -16.243 -12.630 1.00 12.06 ?  121 VAL   B CA   1 
ATOM   5711 C C    . VAL   B 1 121 ? 40.052 -16.449 -11.604 1.00 11.64 ?  121 VAL   B C    1 
ATOM   5712 O O    . VAL   B 1 121 ? 40.725 -15.490 -11.204 1.00 12.44 ?  121 VAL   B O    1 
ATOM   5713 C CB   . VAL   B 1 121 ? 39.463 -16.194 -14.087 1.00 14.17 ?  121 VAL   B CB   1 
ATOM   5714 C CG1  . VAL   B 1 121 ? 40.328 -14.965 -14.338 1.00 15.49 ?  121 VAL   B CG1  1 
ATOM   5715 C CG2  . VAL   B 1 121 ? 40.210 -17.468 -14.437 1.00 15.78 ?  121 VAL   B CG2  1 
ATOM   5716 H H    . VAL   B 1 121 ? 38.683 -14.432 -11.906 1.00 14.81 ?  121 VAL   B H    1 
ATOM   5717 H HA   . VAL   B 1 121 ? 38.338 -16.996 -12.570 1.00 14.48 ?  121 VAL   B HA   1 
ATOM   5718 H HB   . VAL   B 1 121 ? 38.699 -16.137 -14.686 1.00 17.01 ?  121 VAL   B HB   1 
ATOM   5719 H HG11 . VAL   B 1 121 ? 40.643 -14.979 -15.256 1.00 18.59 ?  121 VAL   B HG11 1 
ATOM   5720 H HG12 . VAL   B 1 121 ? 39.797 -14.168 -14.184 1.00 18.59 ?  121 VAL   B HG12 1 
ATOM   5721 H HG13 . VAL   B 1 121 ? 41.084 -14.981 -13.730 1.00 18.59 ?  121 VAL   B HG13 1 
ATOM   5722 H HG21 . VAL   B 1 121 ? 40.413 -17.468 -15.388 1.00 18.94 ?  121 VAL   B HG21 1 
ATOM   5723 H HG22 . VAL   B 1 121 ? 41.037 -17.503 -13.929 1.00 18.94 ?  121 VAL   B HG22 1 
ATOM   5724 H HG23 . VAL   B 1 121 ? 39.656 -18.233 -14.221 1.00 18.94 ?  121 VAL   B HG23 1 
ATOM   5725 N N    . LEU   B 1 122 ? 40.233 -17.705 -11.168 1.00 11.44 ?  122 LEU   B N    1 
ATOM   5726 C CA   . LEU   B 1 122 ? 41.220 -18.055 -10.147 1.00 11.35 ?  122 LEU   B CA   1 
ATOM   5727 C C    . LEU   B 1 122 ? 41.872 -19.387 -10.469 1.00 11.28 ?  122 LEU   B C    1 
ATOM   5728 O O    . LEU   B 1 122 ? 41.211 -20.305 -10.967 1.00 12.26 ?  122 LEU   B O    1 
ATOM   5729 C CB   . LEU   B 1 122 ? 40.573 -18.278 -8.768  1.00 13.04 ?  122 LEU   B CB   1 
ATOM   5730 C CG   . LEU   B 1 122 ? 39.529 -17.263 -8.288  1.00 12.89 ?  122 LEU   B CG   1 
ATOM   5731 C CD1  . LEU   B 1 122 ? 38.133 -17.618 -8.768  1.00 13.79 ?  122 LEU   B CD1  1 
ATOM   5732 C CD2  . LEU   B 1 122 ? 39.567 -17.149 -6.774  1.00 12.47 ?  122 LEU   B CD2  1 
ATOM   5733 H H    . LEU   B 1 122 ? 39.789 -18.385 -11.459 1.00 13.74 ?  122 LEU   B H    1 
ATOM   5734 H HA   . LEU   B 1 122 ? 41.900 -17.364 -10.080 1.00 13.63 ?  122 LEU   B HA   1 
ATOM   5735 H HB2  . LEU   B 1 122 ? 40.139 -19.142 -8.779  1.00 15.65 ?  122 LEU   B HB2  1 
ATOM   5736 H HB3  . LEU   B 1 122 ? 41.281 -18.284 -8.106  1.00 15.65 ?  122 LEU   B HB3  1 
ATOM   5737 H HG   . LEU   B 1 122 ? 39.751 -16.392 -8.650  1.00 15.48 ?  122 LEU   B HG   1 
ATOM   5738 H HD11 . LEU   B 1 122 ? 37.500 -16.982 -8.393  1.00 16.55 ?  122 LEU   B HD11 1 
ATOM   5739 H HD12 . LEU   B 1 122 ? 38.110 -17.565 -9.738  1.00 16.55 ?  122 LEU   B HD12 1 
ATOM   5740 H HD13 . LEU   B 1 122 ? 37.914 -18.513 -8.478  1.00 16.55 ?  122 LEU   B HD13 1 
ATOM   5741 H HD21 . LEU   B 1 122 ? 38.880 -16.528 -6.484  1.00 14.97 ?  122 LEU   B HD21 1 
ATOM   5742 H HD22 . LEU   B 1 122 ? 39.408 -18.023 -6.385  1.00 14.97 ?  122 LEU   B HD22 1 
ATOM   5743 H HD23 . LEU   B 1 122 ? 40.441 -16.822 -6.504  1.00 14.97 ?  122 LEU   B HD23 1 
ATOM   5744 N N    . LEU   B 1 123 ? 43.159 -19.494 -10.117 1.00 10.86 ?  123 LEU   B N    1 
ATOM   5745 C CA   . LEU   B 1 123 ? 43.871 -20.764 -9.996  1.00 11.45 ?  123 LEU   B CA   1 
ATOM   5746 C C    . LEU   B 1 123 ? 43.842 -21.158 -8.523  1.00 10.74 ?  123 LEU   B C    1 
ATOM   5747 O O    . LEU   B 1 123 ? 44.200 -20.335 -7.671  1.00 11.14 ?  123 LEU   B O    1 
ATOM   5748 C CB   . LEU   B 1 123 ? 45.320 -20.580 -10.459 1.00 11.53 ?  123 LEU   B CB   1 
ATOM   5749 C CG   . LEU   B 1 123 ? 46.261 -21.765 -10.208 1.00 11.89 ?  123 LEU   B CG   1 
ATOM   5750 C CD1  . LEU   B 1 123 ? 45.851 -23.011 -11.001 1.00 12.36 ?  123 LEU   B CD1  1 
ATOM   5751 C CD2  . LEU   B 1 123 ? 47.683 -21.362 -10.561 1.00 13.03 ?  123 LEU   B CD2  1 
ATOM   5752 H H    . LEU   B 1 123 ? 43.658 -18.816 -9.925  1.00 13.04 ?  123 LEU   B H    1 
ATOM   5753 H HA   . LEU   B 1 123 ? 43.436 -21.453 -10.528 1.00 13.74 ?  123 LEU   B HA   1 
ATOM   5754 H HB2  . LEU   B 1 123 ? 45.314 -20.419 -11.415 1.00 13.84 ?  123 LEU   B HB2  1 
ATOM   5755 H HB3  . LEU   B 1 123 ? 45.691 -19.817 -10.000 1.00 13.84 ?  123 LEU   B HB3  1 
ATOM   5756 H HG   . LEU   B 1 123 ? 46.247 -21.993 -9.266  1.00 14.28 ?  123 LEU   B HG   1 
ATOM   5757 H HD11 . LEU   B 1 123 ? 46.485 -23.719 -10.818 1.00 14.84 ?  123 LEU   B HD11 1 
ATOM   5758 H HD12 . LEU   B 1 123 ? 44.962 -23.277 -10.723 1.00 14.84 ?  123 LEU   B HD12 1 
ATOM   5759 H HD13 . LEU   B 1 123 ? 45.855 -22.794 -11.945 1.00 14.84 ?  123 LEU   B HD13 1 
ATOM   5760 H HD21 . LEU   B 1 123 ? 48.272 -22.114 -10.401 1.00 15.64 ?  123 LEU   B HD21 1 
ATOM   5761 H HD22 . LEU   B 1 123 ? 47.714 -21.107 -11.495 1.00 15.64 ?  123 LEU   B HD22 1 
ATOM   5762 H HD23 . LEU   B 1 123 ? 47.943 -20.611 -10.003 1.00 15.64 ?  123 LEU   B HD23 1 
ATOM   5763 N N    . ALA   B 1 124 ? 43.412 -22.389 -8.213  1.00 10.74 ?  124 ALA   B N    1 
ATOM   5764 C CA   . ALA   B 1 124 ? 43.153 -22.707 -6.818  1.00 10.90 ?  124 ALA   B CA   1 
ATOM   5765 C C    . ALA   B 1 124 ? 43.419 -24.167 -6.484  1.00 10.74 ?  124 ALA   B C    1 
ATOM   5766 O O    . ALA   B 1 124 ? 43.295 -25.044 -7.353  1.00 11.39 ?  124 ALA   B O    1 
ATOM   5767 C CB   . ALA   B 1 124 ? 41.696 -22.385 -6.460  1.00 11.30 ?  124 ALA   B CB   1 
ATOM   5768 H H    . ALA   B 1 124 ? 43.259 -23.031 -8.772  1.00 12.89 ?  124 ALA   B H    1 
ATOM   5769 H HA   . ALA   B 1 124 ? 43.726 -22.154 -6.270  1.00 13.08 ?  124 ALA   B HA   1 
ATOM   5770 H HB1  . ALA   B 1 124 ? 41.538 -22.597 -5.528  1.00 13.57 ?  124 ALA   B HB1  1 
ATOM   5771 H HB2  . ALA   B 1 124 ? 41.535 -21.436 -6.613  1.00 13.57 ?  124 ALA   B HB2  1 
ATOM   5772 H HB3  . ALA   B 1 124 ? 41.104 -22.909 -7.024  1.00 13.57 ?  124 ALA   B HB3  1 
ATOM   5773 N N    . PRO   B 1 125 ? 43.717 -24.458 -5.219  1.00 10.92 ?  125 PRO   B N    1 
ATOM   5774 C CA   . PRO   B 1 125 ? 43.652 -25.823 -4.699  1.00 11.47 ?  125 PRO   B CA   1 
ATOM   5775 C C    . PRO   B 1 125 ? 42.252 -26.096 -4.153  1.00 11.63 ?  125 PRO   B C    1 
ATOM   5776 O O    . PRO   B 1 125 ? 41.457 -25.179 -3.941  1.00 12.33 ?  125 PRO   B O    1 
ATOM   5777 C CB   . PRO   B 1 125 ? 44.639 -25.752 -3.529  1.00 12.76 ?  125 PRO   B CB   1 
ATOM   5778 C CG   . PRO   B 1 125 ? 44.376 -24.363 -2.954  1.00 12.61 ?  125 PRO   B CG   1 
ATOM   5779 C CD   . PRO   B 1 125 ? 44.047 -23.489 -4.157  1.00 11.77 ?  125 PRO   B CD   1 
ATOM   5780 H HA   . PRO   B 1 125 ? 43.926 -26.489 -5.349  1.00 13.77 ?  125 PRO   B HA   1 
ATOM   5781 H HB2  . PRO   B 1 125 ? 44.438 -26.437 -2.873  1.00 15.31 ?  125 PRO   B HB2  1 
ATOM   5782 H HB3  . PRO   B 1 125 ? 45.550 -25.824 -3.848  1.00 15.31 ?  125 PRO   B HB3  1 
ATOM   5783 H HG2  . PRO   B 1 125 ? 43.618 -24.389 -2.343  1.00 15.14 ?  125 PRO   B HG2  1 
ATOM   5784 H HG3  . PRO   B 1 125 ? 45.166 -24.031 -2.496  1.00 15.14 ?  125 PRO   B HG3  1 
ATOM   5785 H HD2  . PRO   B 1 125 ? 43.288 -22.914 -3.973  1.00 14.13 ?  125 PRO   B HD2  1 
ATOM   5786 H HD3  . PRO   B 1 125 ? 44.829 -22.960 -4.414  1.00 14.13 ?  125 PRO   B HD3  1 
ATOM   5787 N N    . LEU   B 1 126 ? 41.987 -27.374 -3.872  1.00 12.47 ?  126 LEU   B N    1 
ATOM   5788 C CA   . LEU   B 1 126 ? 40.768 -27.746 -3.161  1.00 12.97 ?  126 LEU   B CA   1 
ATOM   5789 C C    . LEU   B 1 126 ? 40.878 -27.345 -1.697  1.00 12.85 ?  126 LEU   B C    1 
ATOM   5790 O O    . LEU   B 1 126 ? 41.762 -27.813 -0.974  1.00 14.46 ?  126 LEU   B O    1 
ATOM   5791 C CB   . LEU   B 1 126 ? 40.518 -29.246 -3.276  1.00 14.40 ?  126 LEU   B CB   1 
ATOM   5792 C CG   . LEU   B 1 126 ? 39.990 -29.724 -4.629  1.00 14.90 ?  126 LEU   B CG   1 
ATOM   5793 C CD1  . LEU   B 1 126 ? 40.050 -31.235 -4.729  1.00 16.80 ?  126 LEU   B CD1  1 
ATOM   5794 C CD2  . LEU   B 1 126 ? 38.569 -29.238 -4.857  1.00 15.41 ?  126 LEU   B CD2  1 
ATOM   5795 H H    . LEU   B 1 126 ? 42.499 -28.039 -4.069  1.00 14.97 ?  126 LEU   B H    1 
ATOM   5796 H HA   . LEU   B 1 126 ? 40.016 -27.274 -3.551  1.00 15.57 ?  126 LEU   B HA   1 
ATOM   5797 H HB2  . LEU   B 1 126 ? 41.352 -29.707 -3.105  1.00 17.29 ?  126 LEU   B HB2  1 
ATOM   5798 H HB3  . LEU   B 1 126 ? 39.864 -29.497 -2.603  1.00 17.29 ?  126 LEU   B HB3  1 
ATOM   5799 H HG   . LEU   B 1 126 ? 40.551 -29.353 -5.330  1.00 17.89 ?  126 LEU   B HG   1 
ATOM   5800 H HD11 . LEU   B 1 126 ? 39.711 -31.506 -5.596  1.00 20.17 ?  126 LEU   B HD11 1 
ATOM   5801 H HD12 . LEU   B 1 126 ? 40.968 -31.524 -4.625  1.00 20.17 ?  126 LEU   B HD12 1 
ATOM   5802 H HD13 . LEU   B 1 126 ? 39.500 -31.618 -4.026  1.00 20.17 ?  126 LEU   B HD13 1 
ATOM   5803 H HD21 . LEU   B 1 126 ? 38.220 -29.653 -5.660  1.00 18.50 ?  126 LEU   B HD21 1 
ATOM   5804 H HD22 . LEU   B 1 126 ? 38.025 -29.482 -4.093  1.00 18.50 ?  126 LEU   B HD22 1 
ATOM   5805 H HD23 . LEU   B 1 126 ? 38.575 -28.272 -4.962  1.00 18.50 ?  126 LEU   B HD23 1 
ATOM   5806 N N    . LEU   B 1 127 ? 39.953 -26.507 -1.246  1.00 12.54 ?  127 LEU   B N    1 
ATOM   5807 C CA   . LEU   B 1 127 ? 40.001 -26.017 0.120   1.00 13.12 ?  127 LEU   B CA   1 
ATOM   5808 C C    . LEU   B 1 127 ? 39.729 -27.139 1.115   1.00 12.84 ?  127 LEU   B C    1 
ATOM   5809 O O    . LEU   B 1 127 ? 38.907 -28.033 0.885   1.00 13.22 ?  127 LEU   B O    1 
ATOM   5810 C CB   . LEU   B 1 127 ? 38.981 -24.897 0.320   1.00 13.88 ?  127 LEU   B CB   1 
ATOM   5811 C CG   . LEU   B 1 127 ? 39.164 -23.625 -0.511  1.00 14.39 ?  127 LEU   B CG   1 
ATOM   5812 C CD1  . LEU   B 1 127 ? 38.045 -22.657 -0.178  1.00 14.59 ?  127 LEU   B CD1  1 
ATOM   5813 C CD2  . LEU   B 1 127 ? 40.523 -22.987 -0.275  1.00 14.92 ?  127 LEU   B CD2  1 
ATOM   5814 H H    . LEU   B 1 127 ? 39.290 -26.200 -1.712  1.00 15.06 ?  127 LEU   B H    1 
ATOM   5815 H HA   . LEU   B 1 127 ? 40.885 -25.651 0.298   1.00 15.75 ?  127 LEU   B HA   1 
ATOM   5816 H HB2  . LEU   B 1 127 ? 38.100 -25.247 0.110   1.00 16.66 ?  127 LEU   B HB2  1 
ATOM   5817 H HB3  . LEU   B 1 127 ? 39.001 -24.628 1.252   1.00 16.66 ?  127 LEU   B HB3  1 
ATOM   5818 H HG   . LEU   B 1 127 ? 39.084 -23.839 -1.452  1.00 17.28 ?  127 LEU   B HG   1 
ATOM   5819 H HD11 . LEU   B 1 127 ? 38.158 -21.842 -0.699  1.00 17.51 ?  127 LEU   B HD11 1 
ATOM   5820 H HD12 . LEU   B 1 127 ? 37.191 -23.063 -0.389  1.00 17.51 ?  127 LEU   B HD12 1 
ATOM   5821 H HD13 . LEU   B 1 127 ? 38.081 -22.440 0.770   1.00 17.51 ?  127 LEU   B HD13 1 
ATOM   5822 H HD21 . LEU   B 1 127 ? 40.561 -22.131 -0.734  1.00 17.91 ?  127 LEU   B HD21 1 
ATOM   5823 H HD22 . LEU   B 1 127 ? 40.651 -22.854 0.678   1.00 17.91 ?  127 LEU   B HD22 1 
ATOM   5824 H HD23 . LEU   B 1 127 ? 41.209 -23.577 -0.622  1.00 17.91 ?  127 LEU   B HD23 1 
ATOM   5825 N N    . SER   B 1 128 ? 40.416 -27.060 2.244   1.00 12.83 ?  128 SER   B N    1 
ATOM   5826 C CA   . SER   B 1 128 ? 40.299 -27.976 3.369   1.00 13.35 ?  128 SER   B CA   1 
ATOM   5827 C C    . SER   B 1 128 ? 40.795 -29.383 3.053   1.00 14.43 ?  128 SER   B C    1 
ATOM   5828 O O    . SER   B 1 128 ? 40.706 -30.259 3.912   1.00 15.77 ?  128 SER   B O    1 
ATOM   5829 C CB   . SER   B 1 128 ? 38.897 -27.984 3.998   1.00 13.82 ?  128 SER   B CB   1 
ATOM   5830 O OG   . SER   B 1 128 ? 38.575 -26.713 4.555   1.00 14.35 ?  128 SER   B OG   1 
ATOM   5831 H H    . SER   B 1 128 ? 40.996 -26.443 2.387   1.00 15.41 ?  128 SER   B H    1 
ATOM   5832 H HA   . SER   B 1 128 ? 40.885 -27.641 4.054   1.00 16.02 ?  128 SER   B HA   1 
ATOM   5833 H HB2  . SER   B 1 128 ? 38.239 -28.216 3.325   1.00 16.59 ?  128 SER   B HB2  1 
ATOM   5834 H HB3  . SER   B 1 128 ? 38.878 -28.657 4.712   1.00 16.59 ?  128 SER   B HB3  1 
ATOM   5835 H HG   . SER   B 1 128 ? 39.138 -26.513 5.147   1.00 17.22 ?  128 SER   B HG   1 
ATOM   5836 N N    . ALA   B 1 129 ? 41.363 -29.609 1.867   1.00 15.57 ?  129 ALA   B N    1 
ATOM   5837 C CA   . ALA   B 1 129 ? 41.907 -30.910 1.513   1.00 16.38 ?  129 ALA   B CA   1 
ATOM   5838 C C    . ALA   B 1 129 ? 43.304 -31.084 2.100   1.00 15.48 ?  129 ALA   B C    1 
ATOM   5839 O O    . ALA   B 1 129 ? 43.863 -30.185 2.742   1.00 14.96 ?  129 ALA   B O    1 
ATOM   5840 C CB   . ALA   B 1 129 ? 41.950 -31.075 -0.004  1.00 18.65 ?  129 ALA   B CB   1 
ATOM   5841 H H    . ALA   B 1 129 ? 41.442 -29.022 1.243   1.00 18.69 ?  129 ALA   B H    1 
ATOM   5842 H HA   . ALA   B 1 129 ? 41.339 -31.606 1.874   1.00 19.66 ?  129 ALA   B HA   1 
ATOM   5843 H HB1  . ALA   B 1 129 ? 42.306 -31.954 -0.218  1.00 22.38 ?  129 ALA   B HB1  1 
ATOM   5844 H HB2  . ALA   B 1 129 ? 41.052 -30.988 -0.356  1.00 22.38 ?  129 ALA   B HB2  1 
ATOM   5845 H HB3  . ALA   B 1 129 ? 42.523 -30.388 -0.381  1.00 22.38 ?  129 ALA   B HB3  1 
ATOM   5846 N N    . GLY   B 1 130 ? 43.873 -32.263 1.860   1.00 15.61 ?  130 GLY   B N    1 
ATOM   5847 C CA   . GLY   B 1 130 ? 45.260 -32.499 2.218   1.00 15.96 ?  130 GLY   B CA   1 
ATOM   5848 C C    . GLY   B 1 130 ? 45.473 -32.405 3.711   1.00 16.02 ?  130 GLY   B C    1 
ATOM   5849 O O    . GLY   B 1 130 ? 44.779 -33.054 4.509   1.00 16.84 ?  130 GLY   B O    1 
ATOM   5850 H H    . GLY   B 1 130 ? 43.484 -32.932 1.484   1.00 18.74 ?  130 GLY   B H    1 
ATOM   5851 H HA2  . GLY   B 1 130 ? 45.529 -33.384 1.923   1.00 19.16 ?  130 GLY   B HA2  1 
ATOM   5852 H HA3  . GLY   B 1 130 ? 45.828 -31.844 1.781   1.00 19.16 ?  130 GLY   B HA3  1 
ATOM   5853 N N    . ILE   B 1 131 ? 46.446 -31.574 4.102   1.00 16.45 ?  131 ILE   B N    1 
ATOM   5854 C CA   . ILE   B 1 131 ? 46.801 -31.445 5.508   1.00 17.17 ?  131 ILE   B CA   1 
ATOM   5855 C C    . ILE   B 1 131 ? 45.685 -30.842 6.343   1.00 16.40 ?  131 ILE   B C    1 
ATOM   5856 O O    . ILE   B 1 131 ? 45.759 -30.901 7.574   1.00 18.13 ?  131 ILE   B O    1 
ATOM   5857 C CB   . ILE   B 1 131 ? 48.121 -30.668 5.708   1.00 19.12 ?  131 ILE   B CB   1 
ATOM   5858 C CG1  . ILE   B 1 131 ? 47.954 -29.185 5.343   1.00 20.31 ?  131 ILE   B CG1  1 
ATOM   5859 C CG2  . ILE   B 1 131 ? 49.239 -31.305 4.888   1.00 20.14 ?  131 ILE   B CG2  1 
ATOM   5860 C CD1  . ILE   B 1 131 ? 49.178 -28.334 5.652   1.00 21.35 ?  131 ILE   B CD1  1 
ATOM   5861 H H    . ILE   B 1 131 ? 46.911 -31.078 3.574   1.00 19.75 ?  131 ILE   B H    1 
ATOM   5862 H HA   . ILE   B 1 131 ? 46.943 -32.335 5.856   1.00 20.61 ?  131 ILE   B HA   1 
ATOM   5863 H HB   . ILE   B 1 131 ? 48.359 -30.723 6.647   1.00 22.95 ?  131 ILE   B HB   1 
ATOM   5864 H HG12 . ILE   B 1 131 ? 47.773 -29.120 4.393   1.00 24.38 ?  131 ILE   B HG12 1 
ATOM   5865 H HG13 . ILE   B 1 131 ? 47.208 -28.814 5.843   1.00 24.38 ?  131 ILE   B HG13 1 
ATOM   5866 H HG21 . ILE   B 1 131 ? 50.080 -30.907 5.149   1.00 24.18 ?  131 ILE   B HG21 1 
ATOM   5867 H HG22 . ILE   B 1 131 ? 49.247 -32.256 5.060   1.00 24.18 ?  131 ILE   B HG22 1 
ATOM   5868 H HG23 . ILE   B 1 131 ? 49.065 -31.137 3.948   1.00 24.18 ?  131 ILE   B HG23 1 
ATOM   5869 H HD11 . ILE   B 1 131 ? 48.961 -27.403 5.491   1.00 25.63 ?  131 ILE   B HD11 1 
ATOM   5870 H HD12 . ILE   B 1 131 ? 49.423 -28.462 6.582   1.00 25.63 ?  131 ILE   B HD12 1 
ATOM   5871 H HD13 . ILE   B 1 131 ? 49.907 -28.610 5.076   1.00 25.63 ?  131 ILE   B HD13 1 
ATOM   5872 N N    . PHE   B 1 132 ? 44.655 -30.262 5.712   1.00 15.29 ?  132 PHE   B N    1 
ATOM   5873 C CA   . PHE   B 1 132 ? 43.493 -29.759 6.439   1.00 15.70 ?  132 PHE   B CA   1 
ATOM   5874 C C    . PHE   B 1 132 ? 42.472 -30.852 6.768   1.00 16.90 ?  132 PHE   B C    1 
ATOM   5875 O O    . PHE   B 1 132 ? 41.569 -30.607 7.576   1.00 18.52 ?  132 PHE   B O    1 
ATOM   5876 C CB   . PHE   B 1 132 ? 42.819 -28.621 5.658   1.00 14.81 ?  132 PHE   B CB   1 
ATOM   5877 C CG   . PHE   B 1 132 ? 43.519 -27.282 5.774   1.00 14.51 ?  132 PHE   B CG   1 
ATOM   5878 C CD1  . PHE   B 1 132 ? 44.808 -27.099 5.295   1.00 15.97 ?  132 PHE   B CD1  1 
ATOM   5879 C CD2  . PHE   B 1 132 ? 42.856 -26.189 6.314   1.00 14.24 ?  132 PHE   B CD2  1 
ATOM   5880 C CE1  . PHE   B 1 132 ? 45.433 -25.860 5.391   1.00 16.48 ?  132 PHE   B CE1  1 
ATOM   5881 C CE2  . PHE   B 1 132 ? 43.468 -24.948 6.399   1.00 14.85 ?  132 PHE   B CE2  1 
ATOM   5882 C CZ   . PHE   B 1 132 ? 44.761 -24.788 5.943   1.00 16.09 ?  132 PHE   B CZ   1 
ATOM   5883 H H    . PHE   B 1 132 ? 44.603 -30.152 4.857   1.00 18.35 ?  132 PHE   B H    1 
ATOM   5884 H HA   . PHE   B 1 132 ? 43.798 -29.388 7.277   1.00 18.84 ?  132 PHE   B HA   1 
ATOM   5885 H HB2  . PHE   B 1 132 ? 42.804 -28.858 4.719   1.00 17.78 ?  132 PHE   B HB2  1 
ATOM   5886 H HB3  . PHE   B 1 132 ? 41.912 -28.510 5.985   1.00 17.78 ?  132 PHE   B HB3  1 
ATOM   5887 H HD1  . PHE   B 1 132 ? 45.266 -27.821 4.927   1.00 19.17 ?  132 PHE   B HD1  1 
ATOM   5888 H HD2  . PHE   B 1 132 ? 41.987 -26.293 6.626   1.00 17.09 ?  132 PHE   B HD2  1 
ATOM   5889 H HE1  . PHE   B 1 132 ? 46.303 -25.754 5.080   1.00 19.78 ?  132 PHE   B HE1  1 
ATOM   5890 H HE2  . PHE   B 1 132 ? 43.017 -24.227 6.780   1.00 17.83 ?  132 PHE   B HE2  1 
ATOM   5891 H HZ   . PHE   B 1 132 ? 45.178 -23.955 6.009   1.00 19.31 ?  132 PHE   B HZ   1 
ATOM   5892 N N    . GLY   B 1 133 ? 42.573 -32.042 6.163   1.00 16.66 ?  133 GLY   B N    1 
ATOM   5893 C CA   . GLY   B 1 133 ? 41.870 -33.215 6.652   1.00 17.67 ?  133 GLY   B CA   1 
ATOM   5894 C C    . GLY   B 1 133 ? 40.476 -33.484 6.113   1.00 17.78 ?  133 GLY   B C    1 
ATOM   5895 O O    . GLY   B 1 133 ? 39.896 -34.512 6.472   1.00 19.60 ?  133 GLY   B O    1 
ATOM   5896 H H    . GLY   B 1 133 ? 43.050 -32.185 5.461   1.00 20.00 ?  133 GLY   B H    1 
ATOM   5897 H HA2  . GLY   B 1 133 ? 42.410 -33.995 6.454   1.00 21.21 ?  133 GLY   B HA2  1 
ATOM   5898 H HA3  . GLY   B 1 133 ? 41.801 -33.144 7.617   1.00 21.21 ?  133 GLY   B HA3  1 
ATOM   5899 N N    . ALA   B 1 134 ? 39.907 -32.614 5.287   1.00 17.05 ?  134 ALA   B N    1 
ATOM   5900 C CA   . ALA   B 1 134 ? 38.584 -32.901 4.750   1.00 17.06 ?  134 ALA   B CA   1 
ATOM   5901 C C    . ALA   B 1 134 ? 38.673 -33.887 3.591   1.00 17.10 ?  134 ALA   B C    1 
ATOM   5902 O O    . ALA   B 1 134 ? 39.724 -34.066 2.968   1.00 18.20 ?  134 ALA   B O    1 
ATOM   5903 C CB   . ALA   B 1 134 ? 37.898 -31.617 4.283   1.00 17.29 ?  134 ALA   B CB   1 
ATOM   5904 H H    . ALA   B 1 134 ? 40.253 -31.866 5.030   1.00 20.47 ?  134 ALA   B H    1 
ATOM   5905 H HA   . ALA   B 1 134 ? 38.036 -33.294 5.449   1.00 20.48 ?  134 ALA   B HA   1 
ATOM   5906 H HB1  . ALA   B 1 134 ? 37.015 -31.835 3.945   1.00 20.75 ?  134 ALA   B HB1  1 
ATOM   5907 H HB2  . ALA   B 1 134 ? 37.822 -31.005 5.033   1.00 20.75 ?  134 ALA   B HB2  1 
ATOM   5908 H HB3  . ALA   B 1 134 ? 38.430 -31.212 3.580   1.00 20.75 ?  134 ALA   B HB3  1 
ATOM   5909 N N    . ASP   B 1 135 ? 37.544 -34.521 3.304   1.00 17.26 ?  135 ASP   B N    1 
ATOM   5910 C CA   . ASP   B 1 135 ? 37.447 -35.410 2.158   1.00 18.06 ?  135 ASP   B CA   1 
ATOM   5911 C C    . ASP   B 1 135 ? 37.547 -34.575 0.889   1.00 16.88 ?  135 ASP   B C    1 
ATOM   5912 O O    . ASP   B 1 135 ? 36.698 -33.700 0.668   1.00 16.54 ?  135 ASP   B O    1 
ATOM   5913 C CB   . ASP   B 1 135 ? 36.106 -36.136 2.211   1.00 20.00 ?  135 ASP   B CB   1 
ATOM   5914 C CG   . ASP   B 1 135 ? 35.921 -37.127 1.080   1.00 22.03 ?  135 ASP   B CG   1 
ATOM   5915 O OD1  . ASP   B 1 135 ? 36.774 -37.180 0.168   1.00 21.59 ?  135 ASP   B OD1  1 
ATOM   5916 O OD2  . ASP   B 1 135 ? 34.917 -37.876 1.121   1.00 25.01 -1 135 ASP   B OD2  1 
ATOM   5917 H H    . ASP   B 1 135 ? 36.814 -34.444 3.752   1.00 20.72 ?  135 ASP   B H    1 
ATOM   5918 H HA   . ASP   B 1 135 ? 38.164 -36.064 2.190   1.00 21.68 ?  135 ASP   B HA   1 
ATOM   5919 H HB2  . ASP   B 1 135 ? 36.049 -36.626 3.044   1.00 24.01 ?  135 ASP   B HB2  1 
ATOM   5920 H HB3  . ASP   B 1 135 ? 35.395 -35.485 2.152   1.00 24.01 ?  135 ASP   B HB3  1 
ATOM   5921 N N    . PRO   B 1 136 ? 38.551 -34.790 0.038   1.00 17.08 ?  136 PRO   B N    1 
ATOM   5922 C CA   . PRO   B 1 136 ? 38.653 -33.963 -1.174  1.00 16.14 ?  136 PRO   B CA   1 
ATOM   5923 C C    . PRO   B 1 136 ? 37.462 -34.107 -2.100  1.00 15.71 ?  136 PRO   B C    1 
ATOM   5924 O O    . PRO   B 1 136 ? 37.139 -33.159 -2.822  1.00 14.85 ?  136 PRO   B O    1 
ATOM   5925 C CB   . PRO   B 1 136 ? 39.963 -34.438 -1.823  1.00 17.27 ?  136 PRO   B CB   1 
ATOM   5926 C CG   . PRO   B 1 136 ? 40.172 -35.822 -1.281  1.00 18.50 ?  136 PRO   B CG   1 
ATOM   5927 C CD   . PRO   B 1 136 ? 39.633 -35.781 0.122   1.00 17.99 ?  136 PRO   B CD   1 
ATOM   5928 H HA   . PRO   B 1 136 ? 38.747 -33.027 -0.938  1.00 19.38 ?  136 PRO   B HA   1 
ATOM   5929 H HB2  . PRO   B 1 136 ? 39.867 -34.458 -2.791  1.00 20.73 ?  136 PRO   B HB2  1 
ATOM   5930 H HB3  . PRO   B 1 136 ? 40.690 -33.852 -1.564  1.00 20.73 ?  136 PRO   B HB3  1 
ATOM   5931 H HG2  . PRO   B 1 136 ? 39.679 -36.467 -1.815  1.00 22.20 ?  136 PRO   B HG2  1 
ATOM   5932 H HG3  . PRO   B 1 136 ? 41.119 -36.038 -1.275  1.00 22.20 ?  136 PRO   B HG3  1 
ATOM   5933 H HD2  . PRO   B 1 136 ? 39.276 -36.647 0.376   1.00 21.59 ?  136 PRO   B HD2  1 
ATOM   5934 H HD3  . PRO   B 1 136 ? 40.317 -35.482 0.744   1.00 21.59 ?  136 PRO   B HD3  1 
ATOM   5935 N N    . ILE   B 1 137 ? 36.803 -35.271 -2.105  1.00 16.15 ?  137 ILE   B N    1 
ATOM   5936 C CA   . ILE   B 1 137 ? 35.584 -35.437 -2.894  1.00 16.28 ?  137 ILE   B CA   1 
ATOM   5937 C C    . ILE   B 1 137 ? 34.508 -34.470 -2.416  1.00 16.24 ?  137 ILE   B C    1 
ATOM   5938 O O    . ILE   B 1 137 ? 33.790 -33.859 -3.219  1.00 15.85 ?  137 ILE   B O    1 
ATOM   5939 C CB   . ILE   B 1 137 ? 35.112 -36.905 -2.833  1.00 18.31 ?  137 ILE   B CB   1 
ATOM   5940 C CG1  . ILE   B 1 137 ? 36.114 -37.810 -3.554  1.00 20.66 ?  137 ILE   B CG1  1 
ATOM   5941 C CG2  . ILE   B 1 137 ? 33.718 -37.053 -3.432  1.00 19.02 ?  137 ILE   B CG2  1 
ATOM   5942 C CD1  . ILE   B 1 137 ? 35.764 -39.288 -3.499  1.00 23.10 ?  137 ILE   B CD1  1 
ATOM   5943 H H    . ILE   B 1 137 ? 37.040 -35.973 -1.671  1.00 19.38 ?  137 ILE   B H    1 
ATOM   5944 H HA   . ILE   B 1 137 ? 35.776 -35.232 -3.824  1.00 19.54 ?  137 ILE   B HA   1 
ATOM   5945 H HB   . ILE   B 1 137 ? 35.070 -37.176 -1.907  1.00 21.97 ?  137 ILE   B HB   1 
ATOM   5946 H HG12 . ILE   B 1 137 ? 36.156 -37.554 -4.489  1.00 24.80 ?  137 ILE   B HG12 1 
ATOM   5947 H HG13 . ILE   B 1 137 ? 36.985 -37.701 -3.143  1.00 24.80 ?  137 ILE   B HG13 1 
ATOM   5948 H HG21 . ILE   B 1 137 ? 33.453 -37.988 -3.413  1.00 22.83 ?  137 ILE   B HG21 1 
ATOM   5949 H HG22 . ILE   B 1 137 ? 33.084 -36.541 -2.911  1.00 22.83 ?  137 ILE   B HG22 1 
ATOM   5950 H HG23 . ILE   B 1 137 ? 33.730 -36.737 -4.348  1.00 22.83 ?  137 ILE   B HG23 1 
ATOM   5951 H HD11 . ILE   B 1 137 ? 36.443 -39.776 -3.985  1.00 27.73 ?  137 ILE   B HD11 1 
ATOM   5952 H HD12 . ILE   B 1 137 ? 35.741 -39.577 -2.573  1.00 27.73 ?  137 ILE   B HD12 1 
ATOM   5953 H HD13 . ILE   B 1 137 ? 34.902 -39.438 -3.917  1.00 27.73 ?  137 ILE   B HD13 1 
ATOM   5954 N N    . HIS   B 1 138 ? 34.378 -34.317 -1.101  1.00 16.45 ?  138 HIS   B N    1 
ATOM   5955 C CA   . HIS   B 1 138 ? 33.429 -33.352 -0.565  1.00 16.83 ?  138 HIS   B CA   1 
ATOM   5956 C C    . HIS   B 1 138 ? 33.849 -31.925 -0.888  1.00 15.87 ?  138 HIS   B C    1 
ATOM   5957 O O    . HIS   B 1 138 ? 33.005 -31.080 -1.198  1.00 16.19 ?  138 HIS   B O    1 
ATOM   5958 C CB   . HIS   B 1 138 ? 33.320 -33.527 0.941   1.00 18.05 ?  138 HIS   B CB   1 
ATOM   5959 C CG   . HIS   B 1 138 ? 32.388 -32.550 1.580   1.00 19.15 ?  138 HIS   B CG   1 
ATOM   5960 N ND1  . HIS   B 1 138 ? 31.049 -32.486 1.261   1.00 20.54 ?  138 HIS   B ND1  1 
ATOM   5961 C CD2  . HIS   B 1 138 ? 32.604 -31.576 2.495   1.00 19.69 ?  138 HIS   B CD2  1 
ATOM   5962 C CE1  . HIS   B 1 138 ? 30.476 -31.527 1.965   1.00 20.61 ?  138 HIS   B CE1  1 
ATOM   5963 N NE2  . HIS   B 1 138 ? 31.397 -30.962 2.726   1.00 20.22 ?  138 HIS   B NE2  1 
ATOM   5964 H H    . HIS   B 1 138 ? 34.826 -34.752 -0.512  1.00 19.75 ?  138 HIS   B H    1 
ATOM   5965 H HA   . HIS   B 1 138 ? 32.554 -33.515 -0.958  1.00 20.21 ?  138 HIS   B HA   1 
ATOM   5966 H HB2  . HIS   B 1 138 ? 32.989 -34.417 1.132   1.00 21.67 ?  138 HIS   B HB2  1 
ATOM   5967 H HB3  . HIS   B 1 138 ? 34.194 -33.403 1.336   1.00 21.67 ?  138 HIS   B HB3  1 
ATOM   5968 H HD2  . HIS   B 1 138 ? 33.408 -31.369 2.905   1.00 23.64 ?  138 HIS   B HD2  1 
ATOM   5969 H HE1  . HIS   B 1 138 ? 29.571 -31.296 1.935   1.00 24.74 ?  138 HIS   B HE1  1 
ATOM   5970 H HE2  . HIS   B 1 138 ? 31.256 -30.312 3.274   1.00 24.26 ?  138 HIS   B HE2  1 
ATOM   5971 N N    . SER   B 1 139 ? 35.144 -31.627 -0.810  1.00 15.31 ?  139 SER   B N    1 
ATOM   5972 C CA   . SER   B 1 139 ? 35.582 -30.276 -1.128  1.00 14.53 ?  139 SER   B CA   1 
ATOM   5973 C C    . SER   B 1 139 ? 35.242 -29.923 -2.566  1.00 13.72 ?  139 SER   B C    1 
ATOM   5974 O O    . SER   B 1 139 ? 34.795 -28.804 -2.842  1.00 13.63 ?  139 SER   B O    1 
ATOM   5975 C CB   . SER   B 1 139 ? 37.079 -30.144 -0.874  1.00 14.77 ?  139 SER   B CB   1 
ATOM   5976 O OG   . SER   B 1 139 ? 37.488 -28.807 -1.116  1.00 15.00 ?  139 SER   B OG   1 
ATOM   5977 H H    . SER   B 1 139 ? 35.763 -32.175 -0.593  1.00 18.38 ?  139 SER   B H    1 
ATOM   5978 H HA   . SER   B 1 139 ? 35.120 -29.653 -0.557  1.00 17.44 ?  139 SER   B HA   1 
ATOM   5979 H HB2  . SER   B 1 139 ? 37.263 -30.374 0.050   1.00 17.73 ?  139 SER   B HB2  1 
ATOM   5980 H HB3  . SER   B 1 139 ? 37.561 -30.740 -1.469  1.00 17.73 ?  139 SER   B HB3  1 
ATOM   5981 H HG   . SER   B 1 139 ? 38.317 -28.731 -0.972  1.00 18.00 ?  139 SER   B HG   1 
ATOM   5982 N N    . LEU   B 1 140 ? 35.429 -30.869 -3.493  1.00 13.20 ?  140 LEU   B N    1 
ATOM   5983 C CA   . LEU   B 1 140 ? 35.069 -30.620 -4.883  1.00 13.23 ?  140 LEU   B CA   1 
ATOM   5984 C C    . LEU   B 1 140 ? 33.566 -30.390 -5.019  1.00 13.54 ?  140 LEU   B C    1 
ATOM   5985 O O    . LEU   B 1 140 ? 33.129 -29.505 -5.760  1.00 13.65 ?  140 LEU   B O    1 
ATOM   5986 C CB   . LEU   B 1 140 ? 35.539 -31.783 -5.762  1.00 13.38 ?  140 LEU   B CB   1 
ATOM   5987 C CG   . LEU   B 1 140 ? 35.179 -31.681 -7.238  1.00 13.90 ?  140 LEU   B CG   1 
ATOM   5988 C CD1  . LEU   B 1 140 ? 35.742 -30.395 -7.842  1.00 14.87 ?  140 LEU   B CD1  1 
ATOM   5989 C CD2  . LEU   B 1 140 ? 35.676 -32.906 -7.983  1.00 14.74 ?  140 LEU   B CD2  1 
ATOM   5990 H H    . LEU   B 1 140 ? 35.754 -31.653 -3.345  1.00 15.84 ?  140 LEU   B H    1 
ATOM   5991 H HA   . LEU   B 1 140 ? 35.523 -29.819 -5.186  1.00 15.88 ?  140 LEU   B HA   1 
ATOM   5992 H HB2  . LEU   B 1 140 ? 36.506 -31.842 -5.707  1.00 16.06 ?  140 LEU   B HB2  1 
ATOM   5993 H HB3  . LEU   B 1 140 ? 35.146 -32.603 -5.428  1.00 16.06 ?  140 LEU   B HB3  1 
ATOM   5994 H HG   . LEU   B 1 140 ? 34.214 -31.649 -7.324  1.00 16.69 ?  140 LEU   B HG   1 
ATOM   5995 H HD11 . LEU   B 1 140 ? 35.615 -30.421 -8.803  1.00 17.85 ?  140 LEU   B HD11 1 
ATOM   5996 H HD12 . LEU   B 1 140 ? 35.268 -29.636 -7.467  1.00 17.85 ?  140 LEU   B HD12 1 
ATOM   5997 H HD13 . LEU   B 1 140 ? 36.685 -30.336 -7.632  1.00 17.85 ?  140 LEU   B HD13 1 
ATOM   5998 H HD21 . LEU   B 1 140 ? 35.431 -32.819 -8.920  1.00 17.69 ?  140 LEU   B HD21 1 
ATOM   5999 H HD22 . LEU   B 1 140 ? 36.634 -32.965 -7.892  1.00 17.69 ?  140 LEU   B HD22 1 
ATOM   6000 H HD23 . LEU   B 1 140 ? 35.251 -33.692 -7.605  1.00 17.69 ?  140 LEU   B HD23 1 
ATOM   6001 N N    . ARG   B 1 141 ? 32.765 -31.183 -4.305  1.00 13.73 ?  141 ARG   B N    1 
ATOM   6002 C CA   . ARG   B 1 141 ? 31.313 -31.010 -4.287  1.00 15.05 ?  141 ARG   B CA   1 
ATOM   6003 C C    . ARG   B 1 141 ? 30.931 -29.600 -3.859  1.00 14.29 ?  141 ARG   B C    1 
ATOM   6004 O O    . ARG   B 1 141 ? 30.128 -28.924 -4.520  1.00 14.59 ?  141 ARG   B O    1 
ATOM   6005 C CB   . ARG   B 1 141 ? 30.733 -32.039 -3.306  1.00 16.37 ?  141 ARG   B CB   1 
ATOM   6006 C CG   . ARG   B 1 141 ? 29.267 -31.920 -2.962  1.00 18.28 ?  141 ARG   B CG   1 
ATOM   6007 C CD   . ARG   B 1 141 ? 28.458 -32.565 -4.014  1.00 20.21 ?  141 ARG   B CD   1 
ATOM   6008 N NE   . ARG   B 1 141 ? 28.202 -31.663 -5.125  1.00 21.06 ?  141 ARG   B NE   1 
ATOM   6009 C CZ   . ARG   B 1 141 ? 28.211 -32.019 -6.402  1.00 20.74 ?  141 ARG   B CZ   1 
ATOM   6010 N NH1  . ARG   B 1 141 ? 28.656 -33.205 -6.790  1.00 20.34 ?  141 ARG   B NH1  1 
ATOM   6011 N NH2  . ARG   B 1 141 ? 27.756 -31.165 -7.314  1.00 21.39 ?  141 ARG   B NH2  1 
ATOM   6012 H H    . ARG   B 1 141 ? 33.043 -31.834 -3.819  1.00 16.48 ?  141 ARG   B H    1 
ATOM   6013 H HA   . ARG   B 1 141 ? 30.948 -31.181 -5.167  1.00 18.07 ?  141 ARG   B HA   1 
ATOM   6014 H HB2  . ARG   B 1 141 ? 30.877 -32.927 -3.677  1.00 19.65 ?  141 ARG   B HB2  1 
ATOM   6015 H HB3  . ARG   B 1 141 ? 31.224 -31.972 -2.473  1.00 19.65 ?  141 ARG   B HB3  1 
ATOM   6016 H HG2  . ARG   B 1 141 ? 29.102 -32.364 -2.117  1.00 21.94 ?  141 ARG   B HG2  1 
ATOM   6017 H HG3  . ARG   B 1 141 ? 29.013 -30.981 -2.900  1.00 21.94 ?  141 ARG   B HG3  1 
ATOM   6018 H HD2  . ARG   B 1 141 ? 28.929 -33.351 -4.343  1.00 24.26 ?  141 ARG   B HD2  1 
ATOM   6019 H HD3  . ARG   B 1 141 ? 27.610 -32.833 -3.635  1.00 24.26 ?  141 ARG   B HD3  1 
ATOM   6020 H HE   . ARG   B 1 141 ? 28.003 -30.849 -4.938  1.00 25.28 ?  141 ARG   B HE   1 
ATOM   6021 H HH11 . ARG   B 1 141 ? 28.939 -33.778 -6.213  1.00 24.41 ?  141 ARG   B HH11 1 
ATOM   6022 H HH12 . ARG   B 1 141 ? 28.659 -33.410 -7.624  1.00 24.41 ?  141 ARG   B HH12 1 
ATOM   6023 H HH21 . ARG   B 1 141 ? 27.474 -30.388 -7.074  1.00 25.68 ?  141 ARG   B HH21 1 
ATOM   6024 H HH22 . ARG   B 1 141 ? 27.779 -31.374 -8.149  1.00 25.68 ?  141 ARG   B HH22 1 
ATOM   6025 N N    . VAL   B 1 142 ? 31.480 -29.149 -2.735  1.00 14.05 ?  142 VAL   B N    1 
ATOM   6026 C CA   . VAL   B 1 142 ? 31.139 -27.817 -2.251  1.00 13.88 ?  142 VAL   B CA   1 
ATOM   6027 C C    . VAL   B 1 142 ? 31.614 -26.756 -3.237  1.00 13.71 ?  142 VAL   B C    1 
ATOM   6028 O O    . VAL   B 1 142 ? 30.917 -25.768 -3.488  1.00 14.24 ?  142 VAL   B O    1 
ATOM   6029 C CB   . VAL   B 1 142 ? 31.681 -27.590 -0.828  1.00 14.41 ?  142 VAL   B CB   1 
ATOM   6030 C CG1  . VAL   B 1 142 ? 31.368 -26.163 -0.364  1.00 14.45 ?  142 VAL   B CG1  1 
ATOM   6031 C CG2  . VAL   B 1 142 ? 31.089 -28.606 0.135   1.00 14.92 ?  142 VAL   B CG2  1 
ATOM   6032 H H    . VAL   B 1 142 ? 32.042 -29.582 -2.246  1.00 16.86 ?  142 VAL   B H    1 
ATOM   6033 H HA   . VAL   B 1 142 ? 30.177 -27.750 -2.201  1.00 16.66 ?  142 VAL   B HA   1 
ATOM   6034 H HB   . VAL   B 1 142 ? 32.645 -27.702 -0.829  1.00 17.30 ?  142 VAL   B HB   1 
ATOM   6035 H HG11 . VAL   B 1 142 ? 31.545 -26.093 0.586   1.00 17.35 ?  142 VAL   B HG11 1 
ATOM   6036 H HG12 . VAL   B 1 142 ? 31.932 -25.538 -0.850  1.00 17.35 ?  142 VAL   B HG12 1 
ATOM   6037 H HG13 . VAL   B 1 142 ? 30.434 -25.971 -0.541  1.00 17.35 ?  142 VAL   B HG13 1 
ATOM   6038 H HG21 . VAL   B 1 142 ? 31.409 -28.416 1.029   1.00 17.91 ?  142 VAL   B HG21 1 
ATOM   6039 H HG22 . VAL   B 1 142 ? 30.122 -28.537 0.106   1.00 17.91 ?  142 VAL   B HG22 1 
ATOM   6040 H HG23 . VAL   B 1 142 ? 31.366 -29.494 -0.137  1.00 17.91 ?  142 VAL   B HG23 1 
ATOM   6041 N N    . CYS   B 1 143 ? 32.797 -26.950 -3.820  1.00 13.23 ?  143 CYS   B N    1 
ATOM   6042 C CA   . CYS   B 1 143 ? 33.295 -26.008 -4.819  1.00 12.94 ?  143 CYS   B CA   1 
ATOM   6043 C C    . CYS   B 1 143 ? 32.296 -25.860 -5.960  1.00 12.84 ?  143 CYS   B C    1 
ATOM   6044 O O    . CYS   B 1 143 ? 31.886 -24.750 -6.316  1.00 13.17 ?  143 CYS   B O    1 
ATOM   6045 C CB   . CYS   B 1 143 ? 34.649 -26.495 -5.346  1.00 13.70 ?  143 CYS   B CB   1 
ATOM   6046 S SG   . CYS   B 1 143 ? 35.407 -25.393 -6.566  1.00 13.68 ?  143 CYS   B SG   1 
ATOM   6047 H H    . CYS   B 1 143 ? 33.328 -27.607 -3.656  1.00 15.88 ?  143 CYS   B H    1 
ATOM   6048 H HA   . CYS   B 1 143 ? 33.428 -25.140 -4.412  1.00 15.53 ?  143 CYS   B HA   1 
ATOM   6049 H HB2  . CYS   B 1 143 ? 35.272 -26.580 -4.603  1.00 16.44 ?  143 CYS   B HB2  1 
ATOM   6050 H HB3  . CYS   B 1 143 ? 34.533 -27.360 -5.766  1.00 16.44 ?  143 CYS   B HB3  1 
ATOM   6051 H HG   . CYS   B 1 143 ? 36.479 -25.827 -6.891  1.00 16.42 ?  143 CYS   B HG   1 
ATOM   6052 N N    . VAL   B 1 144 ? 31.887 -26.983 -6.547  1.00 13.69 ?  144 VAL   B N    1 
ATOM   6053 C CA   . VAL   B 1 144 ? 30.985 -26.928 -7.692  1.00 14.27 ?  144 VAL   B CA   1 
ATOM   6054 C C    . VAL   B 1 144 ? 29.644 -26.315 -7.318  1.00 14.75 ?  144 VAL   B C    1 
ATOM   6055 O O    . VAL   B 1 144 ? 29.031 -25.604 -8.125  1.00 15.93 ?  144 VAL   B O    1 
ATOM   6056 C CB   . VAL   B 1 144 ? 30.828 -28.342 -8.271  1.00 17.27 ?  144 VAL   B CB   1 
ATOM   6057 C CG1  . VAL   B 1 144 ? 29.565 -28.462 -9.120  1.00 20.21 ?  144 VAL   B CG1  1 
ATOM   6058 C CG2  . VAL   B 1 144 ? 32.081 -28.743 -9.049  1.00 17.07 ?  144 VAL   B CG2  1 
ATOM   6059 H H    . VAL   B 1 144 ? 32.120 -27.776 -6.311  1.00 16.43 ?  144 VAL   B H    1 
ATOM   6060 H HA   . VAL   B 1 144 ? 31.378 -26.376 -8.381  1.00 17.13 ?  144 VAL   B HA   1 
ATOM   6061 H HB   . VAL   B 1 144 ? 30.738 -28.969 -7.535  1.00 20.73 ?  144 VAL   B HB   1 
ATOM   6062 H HG11 . VAL   B 1 144 ? 29.645 -29.245 -9.691  1.00 24.26 ?  144 VAL   B HG11 1 
ATOM   6063 H HG12 . VAL   B 1 144 ? 28.799 -28.560 -8.536  1.00 24.26 ?  144 VAL   B HG12 1 
ATOM   6064 H HG13 . VAL   B 1 144 ? 29.475 -27.668 -9.667  1.00 24.26 ?  144 VAL   B HG13 1 
ATOM   6065 H HG21 . VAL   B 1 144 ? 31.965 -29.640 -9.403  1.00 20.49 ?  144 VAL   B HG21 1 
ATOM   6066 H HG22 . VAL   B 1 144 ? 32.212 -28.117 -9.781  1.00 20.49 ?  144 VAL   B HG22 1 
ATOM   6067 H HG23 . VAL   B 1 144 ? 32.845 -28.718 -8.454  1.00 20.49 ?  144 VAL   B HG23 1 
ATOM   6068 N N    . ASP   B 1 145 ? 29.175 -26.558 -6.098  1.00 14.79 ?  145 ASP   B N    1 
ATOM   6069 C CA   . ASP   B 1 145 ? 27.865 -26.094 -5.670  1.00 15.56 ?  145 ASP   B CA   1 
ATOM   6070 C C    . ASP   B 1 145 ? 27.896 -24.672 -5.126  1.00 15.06 ?  145 ASP   B C    1 
ATOM   6071 O O    . ASP   B 1 145 ? 26.838 -24.124 -4.800  1.00 16.90 ?  145 ASP   B O    1 
ATOM   6072 C CB   . ASP   B 1 145 ? 27.282 -27.013 -4.588  1.00 17.30 ?  145 ASP   B CB   1 
ATOM   6073 C CG   . ASP   B 1 145 ? 26.921 -28.390 -5.099  1.00 19.15 ?  145 ASP   B CG   1 
ATOM   6074 O OD1  . ASP   B 1 145 ? 26.815 -28.584 -6.328  1.00 19.57 ?  145 ASP   B OD1  1 
ATOM   6075 O OD2  . ASP   B 1 145 ? 26.733 -29.275 -4.244  1.00 21.14 -1 145 ASP   B OD2  1 
ATOM   6076 H H    . ASP   B 1 145 ? 29.610 -26.986 -5.493  1.00 17.76 ?  145 ASP   B H    1 
ATOM   6077 H HA   . ASP   B 1 145 ? 27.268 -26.093 -6.430  1.00 18.67 ?  145 ASP   B HA   1 
ATOM   6078 H HB2  . ASP   B 1 145 ? 27.931 -27.127 -3.887  1.00 20.77 ?  145 ASP   B HB2  1 
ATOM   6079 H HB3  . ASP   B 1 145 ? 26.473 -26.603 -4.238  1.00 20.77 ?  145 ASP   B HB3  1 
ATOM   6080 N N    . THR   B 1 146 ? 29.070 -24.060 -5.009  1.00 13.47 ?  146 THR   B N    1 
ATOM   6081 C CA   . THR   B 1 146 ? 29.202 -22.734 -4.404  1.00 13.05 ?  146 THR   B CA   1 
ATOM   6082 C C    . THR   B 1 146 ? 29.832 -21.699 -5.319  1.00 12.86 ?  146 THR   B C    1 
ATOM   6083 O O    . THR   B 1 146 ? 29.378 -20.540 -5.354  1.00 13.21 ?  146 THR   B O    1 
ATOM   6084 C CB   . THR   B 1 146 ? 30.033 -22.835 -3.114  1.00 13.52 ?  146 THR   B CB   1 
ATOM   6085 O OG1  . THR   B 1 146 ? 29.454 -23.821 -2.250  1.00 13.81 ?  146 THR   B OG1  1 
ATOM   6086 C CG2  . THR   B 1 146 ? 30.110 -21.490 -2.408  1.00 13.88 ?  146 THR   B CG2  1 
ATOM   6087 H H    . THR   B 1 146 ? 29.823 -24.390 -5.271  1.00 16.17 ?  146 THR   B H    1 
ATOM   6088 H HA   . THR   B 1 146 ? 28.327 -22.408 -4.161  1.00 15.67 ?  146 THR   B HA   1 
ATOM   6089 H HB   . THR   B 1 146 ? 30.940 -23.099 -3.340  1.00 16.22 ?  146 THR   B HB   1 
ATOM   6090 H HG1  . THR   B 1 146 ? 29.484 -24.579 -2.624  1.00 16.57 ?  146 THR   B HG1  1 
ATOM   6091 H HG21 . THR   B 1 146 ? 30.444 -21.610 -1.506  1.00 16.66 ?  146 THR   B HG21 1 
ATOM   6092 H HG22 . THR   B 1 146 ? 30.713 -20.896 -2.887  1.00 16.66 ?  146 THR   B HG22 1 
ATOM   6093 H HG23 . THR   B 1 146 ? 29.232 -21.086 -2.370  1.00 16.66 ?  146 THR   B HG23 1 
ATOM   6094 N N    . VAL   B 1 147 ? 30.895 -22.067 -6.023  1.00 12.73 ?  147 VAL   B N    1 
ATOM   6095 C CA   . VAL   B 1 147 ? 31.619 -21.121 -6.858  1.00 12.43 ?  147 VAL   B CA   1 
ATOM   6096 C C    . VAL   B 1 147 ? 30.888 -20.991 -8.181  1.00 12.53 ?  147 VAL   B C    1 
ATOM   6097 O O    . VAL   B 1 147 ? 30.524 -21.998 -8.807  1.00 13.56 ?  147 VAL   B O    1 
ATOM   6098 C CB   . VAL   B 1 147 ? 33.073 -21.583 -7.064  1.00 12.49 ?  147 VAL   B CB   1 
ATOM   6099 C CG1  . VAL   B 1 147 ? 33.841 -20.567 -7.883  1.00 12.69 ?  147 VAL   B CG1  1 
ATOM   6100 C CG2  . VAL   B 1 147 ? 33.752 -21.792 -5.722  1.00 12.93 ?  147 VAL   B CG2  1 
ATOM   6101 H H    . VAL   B 1 147 ? 31.225 -22.868 -6.039  1.00 15.28 ?  147 VAL   B H    1 
ATOM   6102 H HA   . VAL   B 1 147 ? 31.641 -20.254 -6.426  1.00 14.92 ?  147 VAL   B HA   1 
ATOM   6103 H HB   . VAL   B 1 147 ? 33.082 -22.430 -7.546  1.00 14.99 ?  147 VAL   B HB   1 
ATOM   6104 H HG11 . VAL   B 1 147 ? 34.782 -20.793 -7.873  1.00 15.23 ?  147 VAL   B HG11 1 
ATOM   6105 H HG12 . VAL   B 1 147 ? 33.507 -20.573 -8.794  1.00 15.23 ?  147 VAL   B HG12 1 
ATOM   6106 H HG13 . VAL   B 1 147 ? 33.708 -19.687 -7.491  1.00 15.23 ?  147 VAL   B HG13 1 
ATOM   6107 H HG21 . VAL   B 1 147 ? 34.692 -21.986 -5.870  1.00 15.52 ?  147 VAL   B HG21 1 
ATOM   6108 H HG22 . VAL   B 1 147 ? 33.660 -20.984 -5.197  1.00 15.52 ?  147 VAL   B HG22 1 
ATOM   6109 H HG23 . VAL   B 1 147 ? 33.330 -22.536 -5.266  1.00 15.52 ?  147 VAL   B HG23 1 
ATOM   6110 N N    . ARG   B 1 148 ? 30.676 -19.745 -8.602  1.00 12.55 ?  148 ARG   B N    1 
ATOM   6111 C CA   . ARG   B 1 148 ? 30.055 -19.428 -9.877  1.00 12.88 ?  148 ARG   B CA   1 
ATOM   6112 C C    . ARG   B 1 148 ? 31.013 -18.759 -10.852 1.00 12.92 ?  148 ARG   B C    1 
ATOM   6113 O O    . ARG   B 1 148 ? 30.725 -18.736 -12.051 1.00 14.16 ?  148 ARG   B O    1 
ATOM   6114 C CB   . ARG   B 1 148 ? 28.820 -18.539 -9.659  1.00 13.04 ?  148 ARG   B CB   1 
ATOM   6115 C CG   . ARG   B 1 148 ? 27.745 -19.246 -8.846  1.00 14.04 ?  148 ARG   B CG   1 
ATOM   6116 C CD   . ARG   B 1 148 ? 26.536 -18.358 -8.537  1.00 14.89 ?  148 ARG   B CD   1 
ATOM   6117 N NE   . ARG   B 1 148 ? 26.916 -17.159 -7.804  1.00 14.84 ?  148 ARG   B NE   1 
ATOM   6118 C CZ   . ARG   B 1 148 ? 27.220 -17.129 -6.514  1.00 13.99 ?  148 ARG   B CZ   1 
ATOM   6119 N NH1  . ARG   B 1 148 ? 27.153 -18.216 -5.759  1.00 14.10 ?  148 ARG   B NH1  1 
ATOM   6120 N NH2  . ARG   B 1 148 ? 27.619 -15.982 -5.969  1.00 13.86 ?  148 ARG   B NH2  1 
ATOM   6121 H H    . ARG   B 1 148 ? 30.894 -19.044 -8.144  1.00 15.07 ?  148 ARG   B H    1 
ATOM   6122 H HA   . ARG   B 1 148 ? 29.755 -20.251 -10.282 1.00 15.47 ?  148 ARG   B HA   1 
ATOM   6123 H HB2  . ARG   B 1 148 ? 29.080 -17.738 -9.177  1.00 15.66 ?  148 ARG   B HB2  1 
ATOM   6124 H HB3  . ARG   B 1 148 ? 28.441 -18.304 -10.519 1.00 15.66 ?  148 ARG   B HB3  1 
ATOM   6125 H HG2  . ARG   B 1 148 ? 27.428 -20.017 -9.348  1.00 16.85 ?  148 ARG   B HG2  1 
ATOM   6126 H HG3  . ARG   B 1 148 ? 28.124 -19.537 -8.003  1.00 16.85 ?  148 ARG   B HG3  1 
ATOM   6127 H HD2  . ARG   B 1 148 ? 26.122 -18.086 -9.371  1.00 17.87 ?  148 ARG   B HD2  1 
ATOM   6128 H HD3  . ARG   B 1 148 ? 25.903 -18.861 -7.999  1.00 17.87 ?  148 ARG   B HD3  1 
ATOM   6129 H HE   . ARG   B 1 148 ? 26.952 -16.423 -8.237  1.00 17.81 ?  148 ARG   B HE   1 
ATOM   6130 H HH11 . ARG   B 1 148 ? 26.895 -18.967 -6.095  1.00 16.92 ?  148 ARG   B HH11 1 
ATOM   6131 H HH12 . ARG   B 1 148 ? 27.352 -18.174 -4.920  1.00 16.92 ?  148 ARG   B HH12 1 
ATOM   6132 H HH21 . ARG   B 1 148 ? 27.674 -15.277 -6.453  1.00 16.64 ?  148 ARG   B HH21 1 
ATOM   6133 H HH22 . ARG   B 1 148 ? 27.823 -15.951 -5.134  1.00 16.64 ?  148 ARG   B HH22 1 
ATOM   6134 N N    . THR   B 1 149 ? 32.121 -18.203 -10.367 1.00 12.66 ?  149 THR   B N    1 
ATOM   6135 C CA   . THR   B 1 149 ? 33.162 -17.641 -11.213 1.00 12.85 ?  149 THR   B CA   1 
ATOM   6136 C C    . THR   B 1 149 ? 34.048 -18.779 -11.729 1.00 12.67 ?  149 THR   B C    1 
ATOM   6137 O O    . THR   B 1 149 ? 33.856 -19.950 -11.391 1.00 13.12 ?  149 THR   B O    1 
ATOM   6138 C CB   . THR   B 1 149 ? 33.935 -16.588 -10.426 1.00 13.11 ?  149 THR   B CB   1 
ATOM   6139 O OG1  . THR   B 1 149 ? 34.398 -17.184 -9.213  1.00 13.09 ?  149 THR   B OG1  1 
ATOM   6140 C CG2  . THR   B 1 149 ? 33.045 -15.389 -10.114 1.00 13.94 ?  149 THR   B CG2  1 
ATOM   6141 H H    . THR   B 1 149 ? 32.289 -18.139 -9.529  1.00 15.19 ?  149 THR   B H    1 
ATOM   6142 H HA   . THR   B 1 149 ? 32.752 -17.205 -11.977 1.00 15.42 ?  149 THR   B HA   1 
ATOM   6143 H HB   . THR   B 1 149 ? 34.693 -16.288 -10.947 1.00 15.73 ?  149 THR   B HB   1 
ATOM   6144 H HG1  . THR   B 1 149 ? 34.824 -16.616 -8.756  1.00 15.72 ?  149 THR   B HG1  1 
ATOM   6145 H HG21 . THR   B 1 149 ? 33.551 -14.721 -9.627  1.00 16.74 ?  149 THR   B HG21 1 
ATOM   6146 H HG22 . THR   B 1 149 ? 32.715 -15.000 -10.937 1.00 16.74 ?  149 THR   B HG22 1 
ATOM   6147 H HG23 . THR   B 1 149 ? 32.290 -15.669 -9.572  1.00 16.74 ?  149 THR   B HG23 1 
ATOM   6148 N N    . ASN   B 1 150 ? 35.021 -18.454 -12.573 1.00 12.92 ?  150 ASN   B N    1 
ATOM   6149 C CA   . ASN   B 1 150 ? 35.789 -19.481 -13.270 1.00 13.11 ?  150 ASN   B CA   1 
ATOM   6150 C C    . ASN   B 1 150 ? 36.955 -19.932 -12.397 1.00 12.70 ?  150 ASN   B C    1 
ATOM   6151 O O    . ASN   B 1 150 ? 37.883 -19.158 -12.135 1.00 13.20 ?  150 ASN   B O    1 
ATOM   6152 C CB   . ASN   B 1 150 ? 36.266 -18.951 -14.615 1.00 14.67 ?  150 ASN   B CB   1 
ATOM   6153 C CG   . ASN   B 1 150 ? 35.130 -18.737 -15.565 1.00 17.76 ?  150 ASN   B CG   1 
ATOM   6154 O OD1  . ASN   B 1 150 ? 34.237 -19.570 -15.654 1.00 18.85 ?  150 ASN   B OD1  1 
ATOM   6155 N ND2  . ASN   B 1 150 ? 35.127 -17.607 -16.252 1.00 19.76 ?  150 ASN   B ND2  1 
ATOM   6156 H H    . ASN   B 1 150 ? 35.268 -17.644 -12.753 1.00 15.50 ?  150 ASN   B H    1 
ATOM   6157 H HA   . ASN   B 1 150 ? 35.213 -20.246 -13.434 1.00 15.73 ?  150 ASN   B HA   1 
ATOM   6158 H HB2  . ASN   B 1 150 ? 36.710 -18.098 -14.481 1.00 17.60 ?  150 ASN   B HB2  1 
ATOM   6159 H HB3  . ASN   B 1 150 ? 36.877 -19.589 -15.010 1.00 17.60 ?  150 ASN   B HB3  1 
ATOM   6160 H HD21 . ASN   B 1 150 ? 34.494 -17.439 -16.813 1.00 23.72 ?  150 ASN   B HD21 1 
ATOM   6161 H HD22 . ASN   B 1 150 ? 35.769 -17.041 -16.153 1.00 23.72 ?  150 ASN   B HD22 1 
ATOM   6162 N N    . VAL   B 1 151 ? 36.913 -21.184 -11.950 1.00 12.48 ?  151 VAL   B N    1 
ATOM   6163 C CA   . VAL   B 1 151 ? 37.927 -21.719 -11.056 1.00 12.50 ?  151 VAL   B CA   1 
ATOM   6164 C C    . VAL   B 1 151 ? 38.635 -22.886 -11.730 1.00 12.29 ?  151 VAL   B C    1 
ATOM   6165 O O    . VAL   B 1 151 ? 37.997 -23.824 -12.232 1.00 13.21 ?  151 VAL   B O    1 
ATOM   6166 C CB   . VAL   B 1 151 ? 37.364 -22.055 -9.662  1.00 13.84 ?  151 VAL   B CB   1 
ATOM   6167 C CG1  . VAL   B 1 151 ? 36.206 -23.045 -9.748  1.00 14.96 ?  151 VAL   B CG1  1 
ATOM   6168 C CG2  . VAL   B 1 151 ? 38.470 -22.557 -8.749  1.00 14.58 ?  151 VAL   B CG2  1 
ATOM   6169 H H    . VAL   B 1 151 ? 36.291 -21.748 -12.156 1.00 14.98 ?  151 VAL   B H    1 
ATOM   6170 H HA   . VAL   B 1 151 ? 38.592 -21.025 -10.923 1.00 15.01 ?  151 VAL   B HA   1 
ATOM   6171 H HB   . VAL   B 1 151 ? 37.012 -21.237 -9.270  1.00 16.62 ?  151 VAL   B HB   1 
ATOM   6172 H HG11 . VAL   B 1 151 ? 35.879 -23.237 -8.854  1.00 17.96 ?  151 VAL   B HG11 1 
ATOM   6173 H HG12 . VAL   B 1 151 ? 35.490 -22.660 -10.282 1.00 17.96 ?  151 VAL   B HG12 1 
ATOM   6174 H HG13 . VAL   B 1 151 ? 36.517 -23.866 -10.166 1.00 17.96 ?  151 VAL   B HG13 1 
ATOM   6175 H HG21 . VAL   B 1 151 ? 38.124 -22.623 -7.844  1.00 17.50 ?  151 VAL   B HG21 1 
ATOM   6176 H HG22 . VAL   B 1 151 ? 38.764 -23.427 -9.055  1.00 17.50 ?  151 VAL   B HG22 1 
ATOM   6177 H HG23 . VAL   B 1 151 ? 39.209 -21.927 -8.773  1.00 17.50 ?  151 VAL   B HG23 1 
ATOM   6178 N N    . TYR   B 1 152 ? 39.965 -22.792 -11.749 1.00 11.68 ?  152 TYR   B N    1 
ATOM   6179 C CA   . TYR   B 1 152 ? 40.872 -23.774 -12.327 1.00 11.91 ?  152 TYR   B CA   1 
ATOM   6180 C C    . TYR   B 1 152 ? 41.589 -24.455 -11.167 1.00 11.56 ?  152 TYR   B C    1 
ATOM   6181 O O    . TYR   B 1 152 ? 42.438 -23.843 -10.513 1.00 12.08 ?  152 TYR   B O    1 
ATOM   6182 C CB   . TYR   B 1 152 ? 41.844 -23.067 -13.275 1.00 12.91 ?  152 TYR   B CB   1 
ATOM   6183 C CG   . TYR   B 1 152 ? 41.166 -22.599 -14.544 1.00 13.49 ?  152 TYR   B CG   1 
ATOM   6184 C CD1  . TYR   B 1 152 ? 40.489 -21.385 -14.603 1.00 13.84 ?  152 TYR   B CD1  1 
ATOM   6185 C CD2  . TYR   B 1 152 ? 41.164 -23.404 -15.671 1.00 14.54 ?  152 TYR   B CD2  1 
ATOM   6186 C CE1  . TYR   B 1 152 ? 39.846 -20.984 -15.762 1.00 15.19 ?  152 TYR   B CE1  1 
ATOM   6187 C CE2  . TYR   B 1 152 ? 40.532 -23.016 -16.831 1.00 15.49 ?  152 TYR   B CE2  1 
ATOM   6188 C CZ   . TYR   B 1 152 ? 39.868 -21.808 -16.877 1.00 15.54 ?  152 TYR   B CZ   1 
ATOM   6189 O OH   . TYR   B 1 152 ? 39.242 -21.439 -18.041 1.00 18.00 ?  152 TYR   B OH   1 
ATOM   6190 H H    . TYR   B 1 152 ? 40.393 -22.127 -11.399 1.00 14.02 ?  152 TYR   B H    1 
ATOM   6191 H HA   . TYR   B 1 152 ? 40.365 -24.438 -12.824 1.00 14.30 ?  152 TYR   B HA   1 
ATOM   6192 H HB2  . TYR   B 1 152 ? 42.211 -22.290 -12.824 1.00 15.50 ?  152 TYR   B HB2  1 
ATOM   6193 H HB3  . TYR   B 1 152 ? 42.554 -23.678 -13.517 1.00 15.50 ?  152 TYR   B HB3  1 
ATOM   6194 H HD1  . TYR   B 1 152 ? 40.466 -20.834 -13.853 1.00 16.62 ?  152 TYR   B HD1  1 
ATOM   6195 H HD2  . TYR   B 1 152 ? 41.607 -24.225 -15.645 1.00 17.46 ?  152 TYR   B HD2  1 
ATOM   6196 H HE1  . TYR   B 1 152 ? 39.404 -20.168 -15.795 1.00 18.24 ?  152 TYR   B HE1  1 
ATOM   6197 H HE2  . TYR   B 1 152 ? 40.554 -23.568 -17.578 1.00 18.60 ?  152 TYR   B HE2  1 
ATOM   6198 H HH   . TYR   B 1 152 ? 38.891 -20.682 -17.943 1.00 21.61 ?  152 TYR   B HH   1 
ATOM   6199 N N    . LEU   B 1 153 ? 41.222 -25.710 -10.896 1.00 11.87 ?  153 LEU   B N    1 
ATOM   6200 C CA   . LEU   B 1 153 ? 41.734 -26.459 -9.758  1.00 11.67 ?  153 LEU   B CA   1 
ATOM   6201 C C    . LEU   B 1 153 ? 42.967 -27.262 -10.149 1.00 12.06 ?  153 LEU   B C    1 
ATOM   6202 O O    . LEU   B 1 153 ? 42.954 -27.992 -11.143 1.00 13.20 ?  153 LEU   B O    1 
ATOM   6203 C CB   . LEU   B 1 153 ? 40.652 -27.410 -9.239  1.00 11.86 ?  153 LEU   B CB   1 
ATOM   6204 C CG   . LEU   B 1 153 ? 39.390 -26.757 -8.680  1.00 13.18 ?  153 LEU   B CG   1 
ATOM   6205 C CD1  . LEU   B 1 153 ? 38.289 -27.796 -8.528  1.00 13.82 ?  153 LEU   B CD1  1 
ATOM   6206 C CD2  . LEU   B 1 153 ? 39.688 -26.098 -7.341  1.00 13.42 ?  153 LEU   B CD2  1 
ATOM   6207 H H    . LEU   B 1 153 ? 40.650 -26.155 -11.371 1.00 14.25 ?  153 LEU   B H    1 
ATOM   6208 H HA   . LEU   B 1 153 ? 41.962 -25.842 -9.049  1.00 14.01 ?  153 LEU   B HA   1 
ATOM   6209 H HB2  . LEU   B 1 153 ? 40.372 -27.987 -9.967  1.00 14.24 ?  153 LEU   B HB2  1 
ATOM   6210 H HB3  . LEU   B 1 153 ? 41.032 -27.949 -8.528  1.00 14.24 ?  153 LEU   B HB3  1 
ATOM   6211 H HG   . LEU   B 1 153 ? 39.078 -26.068 -9.290  1.00 15.83 ?  153 LEU   B HG   1 
ATOM   6212 H HD11 . LEU   B 1 153 ? 37.483 -27.355 -8.210  1.00 16.59 ?  153 LEU   B HD11 1 
ATOM   6213 H HD12 . LEU   B 1 153 ? 38.125 -28.203 -9.389  1.00 16.59 ?  153 LEU   B HD12 1 
ATOM   6214 H HD13 . LEU   B 1 153 ? 38.576 -28.463 -7.887  1.00 16.59 ?  153 LEU   B HD13 1 
ATOM   6215 H HD21 . LEU   B 1 153 ? 38.872 -25.720 -6.979  1.00 16.11 ?  153 LEU   B HD21 1 
ATOM   6216 H HD22 . LEU   B 1 153 ? 40.041 -26.767 -6.731  1.00 16.11 ?  153 LEU   B HD22 1 
ATOM   6217 H HD23 . LEU   B 1 153 ? 40.346 -25.396 -7.472  1.00 16.11 ?  153 LEU   B HD23 1 
ATOM   6218 N N    . ALA   B 1 154 ? 44.018 -27.148 -9.343  1.00 12.15 ?  154 ALA   B N    1 
ATOM   6219 C CA   . ALA   B 1 154 ? 45.249 -27.908 -9.525  1.00 13.43 ?  154 ALA   B CA   1 
ATOM   6220 C C    . ALA   B 1 154 ? 45.315 -28.988 -8.454  1.00 14.09 ?  154 ALA   B C    1 
ATOM   6221 O O    . ALA   B 1 154 ? 45.240 -28.689 -7.255  1.00 15.54 ?  154 ALA   B O    1 
ATOM   6222 C CB   . ALA   B 1 154 ? 46.466 -26.991 -9.440  1.00 14.60 ?  154 ALA   B CB   1 
ATOM   6223 H H    . ALA   B 1 154 ? 44.036 -26.617 -8.662  1.00 14.59 ?  154 ALA   B H    1 
ATOM   6224 H HA   . ALA   B 1 154 ? 45.242 -28.331 -10.393 1.00 16.12 ?  154 ALA   B HA   1 
ATOM   6225 H HB1  . ALA   B 1 154 ? 47.270 -27.518 -9.561  1.00 17.53 ?  154 ALA   B HB1  1 
ATOM   6226 H HB2  . ALA   B 1 154 ? 46.406 -26.315 -10.135 1.00 17.53 ?  154 ALA   B HB2  1 
ATOM   6227 H HB3  . ALA   B 1 154 ? 46.483 -26.561 -8.567  1.00 17.53 ?  154 ALA   B HB3  1 
ATOM   6228 N N    . VAL   B 1 155 ? 45.431 -30.238 -8.889  1.00 13.27 ?  155 VAL   B N    1 
ATOM   6229 C CA   . VAL   B 1 155 ? 45.539 -31.385 -7.997  1.00 13.51 ?  155 VAL   B CA   1 
ATOM   6230 C C    . VAL   B 1 155 ? 46.883 -32.055 -8.271  1.00 13.42 ?  155 VAL   B C    1 
ATOM   6231 O O    . VAL   B 1 155 ? 47.122 -32.552 -9.379  1.00 15.18 ?  155 VAL   B O    1 
ATOM   6232 C CB   . VAL   B 1 155 ? 44.384 -32.378 -8.204  1.00 15.06 ?  155 VAL   B CB   1 
ATOM   6233 C CG1  . VAL   B 1 155 ? 44.560 -33.581 -7.303  1.00 15.03 ?  155 VAL   B CG1  1 
ATOM   6234 C CG2  . VAL   B 1 155 ? 43.045 -31.692 -7.944  1.00 15.95 ?  155 VAL   B CG2  1 
ATOM   6235 H H    . VAL   B 1 155 ? 45.462 -30.454 -9.723  1.00 15.93 ?  155 VAL   B H    1 
ATOM   6236 H HA   . VAL   B 1 155 ? 45.526 -31.085 -7.075  1.00 16.22 ?  155 VAL   B HA   1 
ATOM   6237 H HB   . VAL   B 1 155 ? 44.390 -32.680 -9.126  1.00 18.07 ?  155 VAL   B HB   1 
ATOM   6238 H HG11 . VAL   B 1 155 ? 43.730 -34.081 -7.278  1.00 18.04 ?  155 VAL   B HG11 1 
ATOM   6239 H HG12 . VAL   B 1 155 ? 45.271 -34.143 -7.657  1.00 18.04 ?  155 VAL   B HG12 1 
ATOM   6240 H HG13 . VAL   B 1 155 ? 44.791 -33.279 -6.411  1.00 18.04 ?  155 VAL   B HG13 1 
ATOM   6241 H HG21 . VAL   B 1 155 ? 42.335 -32.347 -8.039  1.00 19.14 ?  155 VAL   B HG21 1 
ATOM   6242 H HG22 . VAL   B 1 155 ? 43.045 -31.333 -7.043  1.00 19.14 ?  155 VAL   B HG22 1 
ATOM   6243 H HG23 . VAL   B 1 155 ? 42.923 -30.977 -8.586  1.00 19.14 ?  155 VAL   B HG23 1 
ATOM   6244 N N    . PHE   B 1 156 ? 47.749 -32.088 -7.256  1.00 13.87 ?  156 PHE   B N    1 
ATOM   6245 C CA   . PHE   B 1 156 ? 49.128 -32.545 -7.453  1.00 15.01 ?  156 PHE   B CA   1 
ATOM   6246 C C    . PHE   B 1 156 ? 49.223 -34.044 -7.741  1.00 15.84 ?  156 PHE   B C    1 
ATOM   6247 O O    . PHE   B 1 156 ? 49.950 -34.468 -8.651  1.00 17.90 ?  156 PHE   B O    1 
ATOM   6248 C CB   . PHE   B 1 156 ? 49.955 -32.183 -6.221  1.00 15.16 ?  156 PHE   B CB   1 
ATOM   6249 C CG   . PHE   B 1 156 ? 51.382 -32.640 -6.285  1.00 15.75 ?  156 PHE   B CG   1 
ATOM   6250 C CD1  . PHE   B 1 156 ? 52.256 -32.099 -7.209  1.00 17.22 ?  156 PHE   B CD1  1 
ATOM   6251 C CD2  . PHE   B 1 156 ? 51.851 -33.599 -5.408  1.00 16.32 ?  156 PHE   B CD2  1 
ATOM   6252 C CE1  . PHE   B 1 156 ? 53.577 -32.510 -7.262  1.00 18.09 ?  156 PHE   B CE1  1 
ATOM   6253 C CE2  . PHE   B 1 156 ? 53.172 -34.012 -5.458  1.00 17.58 ?  156 PHE   B CE2  1 
ATOM   6254 C CZ   . PHE   B 1 156 ? 54.025 -33.471 -6.392  1.00 18.04 ?  156 PHE   B CZ   1 
ATOM   6255 H H    . PHE   B 1 156 ? 47.562 -31.863 -6.448  1.00 16.65 ?  156 PHE   B H    1 
ATOM   6256 H HA   . PHE   B 1 156 ? 49.502 -32.076 -8.209  1.00 18.02 ?  156 PHE   B HA   1 
ATOM   6257 H HB2  . PHE   B 1 156 ? 49.958 -31.218 -6.125  1.00 18.20 ?  156 PHE   B HB2  1 
ATOM   6258 H HB3  . PHE   B 1 156 ? 49.549 -32.589 -5.439  1.00 18.20 ?  156 PHE   B HB3  1 
ATOM   6259 H HD1  . PHE   B 1 156 ? 51.955 -31.447 -7.803  1.00 20.67 ?  156 PHE   B HD1  1 
ATOM   6260 H HD2  . PHE   B 1 156 ? 51.271 -33.972 -4.781  1.00 19.59 ?  156 PHE   B HD2  1 
ATOM   6261 H HE1  . PHE   B 1 156 ? 54.156 -32.141 -7.893  1.00 21.71 ?  156 PHE   B HE1  1 
ATOM   6262 H HE2  . PHE   B 1 156 ? 53.476 -34.669 -4.869  1.00 21.10 ?  156 PHE   B HE2  1 
ATOM   6263 H HZ   . PHE   B 1 156 ? 54.911 -33.751 -6.426  1.00 21.66 ?  156 PHE   B HZ   1 
ATOM   6264 N N    . ASP   B 1 157 ? 48.550 -34.867 -6.944  1.00 16.33 ?  157 ASP   B N    1 
ATOM   6265 C CA   . ASP   B 1 157 ? 48.701 -36.315 -7.040  1.00 17.93 ?  157 ASP   B CA   1 
ATOM   6266 C C    . ASP   B 1 157 ? 47.790 -36.861 -8.134  1.00 18.07 ?  157 ASP   B C    1 
ATOM   6267 O O    . ASP   B 1 157 ? 46.562 -36.746 -8.038  1.00 17.25 ?  157 ASP   B O    1 
ATOM   6268 C CB   . ASP   B 1 157 ? 48.332 -36.930 -5.695  1.00 19.37 ?  157 ASP   B CB   1 
ATOM   6269 C CG   . ASP   B 1 157 ? 48.472 -38.440 -5.676  1.00 21.46 ?  157 ASP   B CG   1 
ATOM   6270 O OD1  . ASP   B 1 157 ? 48.818 -39.047 -6.719  1.00 21.97 ?  157 ASP   B OD1  1 
ATOM   6271 O OD2  . ASP   B 1 157 ? 48.252 -39.018 -4.596  1.00 23.45 -1 157 ASP   B OD2  1 
ATOM   6272 H H    . ASP   B 1 157 ? 48.007 -34.613 -6.335  1.00 19.60 ?  157 ASP   B H    1 
ATOM   6273 H HA   . ASP   B 1 157 ? 49.623 -36.546 -7.249  1.00 21.52 ?  157 ASP   B HA   1 
ATOM   6274 H HB2  . ASP   B 1 157 ? 48.901 -36.547 -5.012  1.00 23.25 ?  157 ASP   B HB2  1 
ATOM   6275 H HB3  . ASP   B 1 157 ? 47.402 -36.720 -5.504  1.00 23.25 ?  157 ASP   B HB3  1 
ATOM   6276 N N    . LYS   B 1 158 ? 48.389 -37.480 -9.160  1.00 19.21 ?  158 LYS   B N    1 
ATOM   6277 C CA   . LYS   B 1 158 ? 47.615 -38.088 -10.244 1.00 20.04 ?  158 LYS   B CA   1 
ATOM   6278 C C    . LYS   B 1 158 ? 46.556 -39.054 -9.715  1.00 19.77 ?  158 LYS   B C    1 
ATOM   6279 O O    . LYS   B 1 158 ? 45.448 -39.138 -10.262 1.00 19.50 ?  158 LYS   B O    1 
ATOM   6280 C CB   . LYS   B 1 158 ? 48.562 -38.798 -11.222 1.00 21.76 ?  158 LYS   B CB   1 
ATOM   6281 C CG   . LYS   B 1 158 ? 47.886 -39.712 -12.239 1.00 23.50 ?  158 LYS   B CG   1 
ATOM   6282 C CD   . LYS   B 1 158 ? 47.034 -38.945 -13.228 1.00 25.52 ?  158 LYS   B CD   1 
ATOM   6283 C CE   . LYS   B 1 158 ? 46.446 -39.879 -14.275 1.00 27.23 ?  158 LYS   B CE   1 
ATOM   6284 N NZ   . LYS   B 1 158 ? 45.370 -39.224 -15.073 1.00 27.43 ?  158 LYS   B NZ   1 
ATOM   6285 H H    . LYS   B 1 158 ? 49.246 -37.564 -9.251  1.00 23.05 ?  158 LYS   B H    1 
ATOM   6286 H HA   . LYS   B 1 158 ? 47.163 -37.387 -10.739 1.00 24.06 ?  158 LYS   B HA   1 
ATOM   6287 H HB2  . LYS   B 1 158 ? 49.054 -38.125 -11.726 1.00 26.11 ?  158 LYS   B HB2  1 
ATOM   6288 H HB3  . LYS   B 1 158 ? 49.188 -39.338 -10.715 1.00 26.11 ?  158 LYS   B HB3  1 
ATOM   6289 H HG2  . LYS   B 1 158 ? 48.573 -40.179 -12.742 1.00 28.21 ?  158 LYS   B HG2  1 
ATOM   6290 H HG3  . LYS   B 1 158 ? 47.325 -40.361 -11.785 1.00 28.21 ?  158 LYS   B HG3  1 
ATOM   6291 H HD2  . LYS   B 1 158 ? 46.305 -38.512 -12.758 1.00 30.64 ?  158 LYS   B HD2  1 
ATOM   6292 H HD3  . LYS   B 1 158 ? 47.582 -38.286 -13.682 1.00 30.64 ?  158 LYS   B HD3  1 
ATOM   6293 H HE2  . LYS   B 1 158 ? 47.144 -40.158 -14.885 1.00 32.68 ?  158 LYS   B HE2  1 
ATOM   6294 H HE3  . LYS   B 1 158 ? 46.061 -40.653 -13.832 1.00 32.68 ?  158 LYS   B HE3  1 
ATOM   6295 H HZ1  . LYS   B 1 158 ? 45.045 -39.794 -15.674 1.00 32.92 ?  158 LYS   B HZ1  1 
ATOM   6296 H HZ2  . LYS   B 1 158 ? 44.709 -38.961 -14.537 1.00 32.92 ?  158 LYS   B HZ2  1 
ATOM   6297 H HZ3  . LYS   B 1 158 ? 45.697 -38.512 -15.496 1.00 32.92 ?  158 LYS   B HZ3  1 
ATOM   6298 N N    . ASN   B 1 159 ? 46.879 -39.815 -8.668  1.00 20.13 ?  159 ASN   B N    1 
ATOM   6299 C CA   . ASN   B 1 159 ? 45.922 -40.797 -8.166  1.00 20.64 ?  159 ASN   B CA   1 
ATOM   6300 C C    . ASN   B 1 159 ? 44.724 -40.125 -7.491  1.00 19.45 ?  159 ASN   B C    1 
ATOM   6301 O O    . ASN   B 1 159 ? 43.592 -40.619 -7.589  1.00 19.90 ?  159 ASN   B O    1 
ATOM   6302 C CB   . ASN   B 1 159 ? 46.624 -41.776 -7.232  1.00 22.41 ?  159 ASN   B CB   1 
ATOM   6303 C CG   . ASN   B 1 159 ? 47.652 -42.626 -7.954  1.00 24.61 ?  159 ASN   B CG   1 
ATOM   6304 O OD1  . ASN   B 1 159 ? 47.399 -43.125 -9.057  1.00 25.25 ?  159 ASN   B OD1  1 
ATOM   6305 N ND2  . ASN   B 1 159 ? 48.819 -42.801 -7.337  1.00 25.61 ?  159 ASN   B ND2  1 
ATOM   6306 H H    . ASN   B 1 159 ? 47.629 -39.780 -8.252  1.00 24.16 ?  159 ASN   B H    1 
ATOM   6307 H HA   . ASN   B 1 159 ? 45.589 -41.305 -8.923  1.00 24.77 ?  159 ASN   B HA   1 
ATOM   6308 H HB2  . ASN   B 1 159 ? 47.082 -41.284 -6.535  1.00 26.90 ?  159 ASN   B HB2  1 
ATOM   6309 H HB3  . ASN   B 1 159 ? 45.966 -42.373 -6.847  1.00 26.90 ?  159 ASN   B HB3  1 
ATOM   6310 H HD21 . ASN   B 1 159 ? 49.437 -43.279 -7.704  1.00 30.74 ?  159 ASN   B HD21 1 
ATOM   6311 H HD22 . ASN   B 1 159 ? 48.955 -42.452 -6.563  1.00 30.74 ?  159 ASN   B HD22 1 
ATOM   6312 N N    . LEU   B 1 160 ? 44.941 -38.998 -6.804  1.00 18.57 ?  160 LEU   B N    1 
ATOM   6313 C CA   . LEU   B 1 160 ? 43.806 -38.261 -6.262  1.00 17.58 ?  160 LEU   B CA   1 
ATOM   6314 C C    . LEU   B 1 160 ? 43.015 -37.597 -7.378  1.00 16.72 ?  160 LEU   B C    1 
ATOM   6315 O O    . LEU   B 1 160 ? 41.779 -37.604 -7.362  1.00 16.03 ?  160 LEU   B O    1 
ATOM   6316 C CB   . LEU   B 1 160 ? 44.268 -37.227 -5.232  1.00 17.16 ?  160 LEU   B CB   1 
ATOM   6317 C CG   . LEU   B 1 160 ? 43.138 -36.331 -4.696  1.00 16.79 ?  160 LEU   B CG   1 
ATOM   6318 C CD1  . LEU   B 1 160 ? 42.018 -37.165 -4.083  1.00 17.71 ?  160 LEU   B CD1  1 
ATOM   6319 C CD2  . LEU   B 1 160 ? 43.668 -35.331 -3.687  1.00 16.96 ?  160 LEU   B CD2  1 
ATOM   6320 H H    . LEU   B 1 160 ? 45.715 -38.653 -6.648  1.00 22.29 ?  160 LEU   B H    1 
ATOM   6321 H HA   . LEU   B 1 160 ? 43.217 -38.887 -5.821  1.00 21.10 ?  160 LEU   B HA   1 
ATOM   6322 H HB2  . LEU   B 1 160 ? 44.664 -37.700 -4.480  1.00 20.60 ?  160 LEU   B HB2  1 
ATOM   6323 H HB3  . LEU   B 1 160 ? 44.938 -36.655 -5.643  1.00 20.60 ?  160 LEU   B HB3  1 
ATOM   6324 H HG   . LEU   B 1 160 ? 42.765 -35.832 -5.434  1.00 20.15 ?  160 LEU   B HG   1 
ATOM   6325 H HD11 . LEU   B 1 160 ? 41.390 -36.573 -3.649  1.00 21.25 ?  160 LEU   B HD11 1 
ATOM   6326 H HD12 . LEU   B 1 160 ? 41.572 -37.667 -4.785  1.00 21.25 ?  160 LEU   B HD12 1 
ATOM   6327 H HD13 . LEU   B 1 160 ? 42.400 -37.780 -3.432  1.00 21.25 ?  160 LEU   B HD13 1 
ATOM   6328 H HD21 . LEU   B 1 160 ? 42.936 -34.771 -3.390  1.00 20.36 ?  160 LEU   B HD21 1 
ATOM   6329 H HD22 . LEU   B 1 160 ? 44.047 -35.811 -2.933  1.00 20.36 ?  160 LEU   B HD22 1 
ATOM   6330 H HD23 . LEU   B 1 160 ? 44.352 -34.788 -4.110  1.00 20.36 ?  160 LEU   B HD23 1 
ATOM   6331 N N    . TYR   B 1 161 ? 43.711 -37.024 -8.362  1.00 16.66 ?  161 TYR   B N    1 
ATOM   6332 C CA   . TYR   B 1 161 ? 43.037 -36.458 -9.525  1.00 16.62 ?  161 TYR   B CA   1 
ATOM   6333 C C    . TYR   B 1 161 ? 42.095 -37.482 -10.149 1.00 16.60 ?  161 TYR   B C    1 
ATOM   6334 O O    . TYR   B 1 161 ? 40.923 -37.190 -10.412 1.00 16.57 ?  161 TYR   B O    1 
ATOM   6335 C CB   . TYR   B 1 161 ? 44.078 -35.976 -10.543 1.00 17.33 ?  161 TYR   B CB   1 
ATOM   6336 C CG   . TYR   B 1 161 ? 43.499 -35.510 -11.857 1.00 17.98 ?  161 TYR   B CG   1 
ATOM   6337 C CD1  . TYR   B 1 161 ? 43.101 -34.188 -12.026 1.00 17.89 ?  161 TYR   B CD1  1 
ATOM   6338 C CD2  . TYR   B 1 161 ? 43.336 -36.386 -12.926 1.00 18.61 ?  161 TYR   B CD2  1 
ATOM   6339 C CE1  . TYR   B 1 161 ? 42.572 -33.754 -13.215 1.00 18.78 ?  161 TYR   B CE1  1 
ATOM   6340 C CE2  . TYR   B 1 161 ? 42.800 -35.956 -14.120 1.00 19.59 ?  161 TYR   B CE2  1 
ATOM   6341 C CZ   . TYR   B 1 161 ? 42.419 -34.639 -14.258 1.00 19.43 ?  161 TYR   B CZ   1 
ATOM   6342 O OH   . TYR   B 1 161 ? 41.880 -34.199 -15.442 1.00 21.57 ?  161 TYR   B OH   1 
ATOM   6343 H H    . TYR   B 1 161 ? 44.567 -36.956 -8.387  1.00 19.99 ?  161 TYR   B H    1 
ATOM   6344 H HA   . TYR   B 1 161 ? 42.508 -35.693 -9.253  1.00 19.95 ?  161 TYR   B HA   1 
ATOM   6345 H HB2  . TYR   B 1 161 ? 44.566 -35.229 -10.160 1.00 20.80 ?  161 TYR   B HB2  1 
ATOM   6346 H HB3  . TYR   B 1 161 ? 44.689 -36.702 -10.737 1.00 20.80 ?  161 TYR   B HB3  1 
ATOM   6347 H HD1  . TYR   B 1 161 ? 43.202 -33.579 -11.329 1.00 21.48 ?  161 TYR   B HD1  1 
ATOM   6348 H HD2  . TYR   B 1 161 ? 43.590 -37.276 -12.837 1.00 22.34 ?  161 TYR   B HD2  1 
ATOM   6349 H HE1  . TYR   B 1 161 ? 42.313 -32.863 -13.313 1.00 22.55 ?  161 TYR   B HE1  1 
ATOM   6350 H HE2  . TYR   B 1 161 ? 42.695 -36.552 -14.830 1.00 23.51 ?  161 TYR   B HE2  1 
ATOM   6351 H HH   . TYR   B 1 161 ? 41.842 -34.831 -15.994 1.00 25.88 ?  161 TYR   B HH   1 
ATOM   6352 N N    . ASP   B 1 162 ? 42.591 -38.701 -10.372 1.00 16.99 ?  162 ASP   B N    1 
ATOM   6353 C CA   . ASP   B 1 162 ? 41.766 -39.742 -10.982 1.00 17.62 ?  162 ASP   B CA   1 
ATOM   6354 C C    . ASP   B 1 162 ? 40.558 -40.077 -10.115 1.00 16.89 ?  162 ASP   B C    1 
ATOM   6355 O O    . ASP   B 1 162 ? 39.456 -40.295 -10.632 1.00 17.11 ?  162 ASP   B O    1 
ATOM   6356 C CB   . ASP   B 1 162 ? 42.599 -41.005 -11.223 1.00 19.01 ?  162 ASP   B CB   1 
ATOM   6357 C CG   . ASP   B 1 162 ? 43.609 -40.847 -12.347 1.00 20.54 ?  162 ASP   B CG   1 
ATOM   6358 O OD1  . ASP   B 1 162 ? 43.481 -39.902 -13.149 1.00 20.94 ?  162 ASP   B OD1  1 
ATOM   6359 O OD2  . ASP   B 1 162 ? 44.520 -41.698 -12.445 1.00 22.41 -1 162 ASP   B OD2  1 
ATOM   6360 H H    . ASP   B 1 162 ? 43.391 -38.946 -10.186 1.00 20.40 ?  162 ASP   B H    1 
ATOM   6361 H HA   . ASP   B 1 162 ? 41.438 -39.430 -11.839 1.00 21.14 ?  162 ASP   B HA   1 
ATOM   6362 H HB2  . ASP   B 1 162 ? 43.091 -41.218 -10.417 1.00 22.82 ?  162 ASP   B HB2  1 
ATOM   6363 H HB3  . ASP   B 1 162 ? 42.007 -41.736 -11.456 1.00 22.82 ?  162 ASP   B HB3  1 
ATOM   6364 N N    A LYS   B 1 163 ? 40.748 -40.144 -8.796  0.72 16.17 ?  163 LYS   B N    1 
ATOM   6365 N N    B LYS   B 1 163 ? 40.742 -40.123 -8.793  0.28 17.26 ?  163 LYS   B N    1 
ATOM   6366 C CA   A LYS   B 1 163 ? 39.625 -40.422 -7.909  0.72 16.47 ?  163 LYS   B CA   1 
ATOM   6367 C CA   B LYS   B 1 163 ? 39.622 -40.424 -7.906  0.28 17.93 ?  163 LYS   B CA   1 
ATOM   6368 C C    A LYS   B 1 163 ? 38.578 -39.317 -7.986  0.72 15.49 ?  163 LYS   B C    1 
ATOM   6369 C C    B LYS   B 1 163 ? 38.579 -39.311 -7.935  0.28 16.29 ?  163 LYS   B C    1 
ATOM   6370 O O    A LYS   B 1 163 ? 37.369 -39.594 -8.015  0.72 16.25 ?  163 LYS   B O    1 
ATOM   6371 O O    B LYS   B 1 163 ? 37.373 -39.581 -7.875  0.28 16.60 ?  163 LYS   B O    1 
ATOM   6372 C CB   A LYS   B 1 163 ? 40.113 -40.592 -6.472  0.72 19.06 ?  163 LYS   B CB   1 
ATOM   6373 C CB   B LYS   B 1 163 ? 40.124 -40.648 -6.479  0.28 20.65 ?  163 LYS   B CB   1 
ATOM   6374 C CG   A LYS   B 1 163 ? 39.035 -41.130 -5.551  0.72 23.65 ?  163 LYS   B CG   1 
ATOM   6375 C CG   B LYS   B 1 163 ? 39.047 -41.164 -5.543  0.28 23.66 ?  163 LYS   B CG   1 
ATOM   6376 C CD   A LYS   B 1 163 ? 39.455 -41.160 -4.095  0.72 27.94 ?  163 LYS   B CD   1 
ATOM   6377 C CD   B LYS   B 1 163 ? 39.536 -41.291 -4.113  0.28 26.63 ?  163 LYS   B CD   1 
ATOM   6378 C CE   A LYS   B 1 163 ? 38.379 -41.831 -3.250  0.72 30.65 ?  163 LYS   B CE   1 
ATOM   6379 C CE   B LYS   B 1 163 ? 38.483 -41.968 -3.251  0.28 28.79 ?  163 LYS   B CE   1 
ATOM   6380 N NZ   A LYS   B 1 163 ? 38.531 -41.554 -1.795  0.72 32.30 ?  163 LYS   B NZ   1 
ATOM   6381 N NZ   B LYS   B 1 163 ? 38.683 -41.702 -1.801  0.28 29.68 ?  163 LYS   B NZ   1 
ATOM   6382 H H    A LYS   B 1 163 ? 41.507 -40.034 -8.401  0.72 19.41 ?  163 LYS   B H    1 
ATOM   6383 H H    B LYS   B 1 163 ? 41.495 -39.989 -8.394  0.28 20.71 ?  163 LYS   B H    1 
ATOM   6384 H HA   A LYS   B 1 163 ? 39.209 -41.250 -8.184  0.72 19.77 ?  163 LYS   B HA   1 
ATOM   6385 H HA   B LYS   B 1 163 ? 39.197 -41.241 -8.203  0.28 21.52 ?  163 LYS   B HA   1 
ATOM   6386 H HB2  A LYS   B 1 163 ? 40.856 -41.220 -6.462  0.72 22.88 ?  163 LYS   B HB2  1 
ATOM   6387 H HB2  B LYS   B 1 163 ? 40.842 -41.303 -6.495  0.28 24.79 ?  163 LYS   B HB2  1 
ATOM   6388 H HB3  A LYS   B 1 163 ? 40.402 -39.734 -6.128  0.72 22.88 ?  163 LYS   B HB3  1 
ATOM   6389 H HB3  B LYS   B 1 163 ? 40.452 -39.809 -6.122  0.28 24.79 ?  163 LYS   B HB3  1 
ATOM   6390 H HG2  A LYS   B 1 163 ? 38.248 -40.569 -5.622  0.72 28.39 ?  163 LYS   B HG2  1 
ATOM   6391 H HG2  B LYS   B 1 163 ? 38.297 -40.550 -5.549  0.28 28.40 ?  163 LYS   B HG2  1 
ATOM   6392 H HG3  A LYS   B 1 163 ? 38.817 -42.039 -5.818  0.72 28.39 ?  163 LYS   B HG3  1 
ATOM   6393 H HG3  B LYS   B 1 163 ? 38.761 -42.042 -5.842  0.28 28.40 ?  163 LYS   B HG3  1 
ATOM   6394 H HD2  A LYS   B 1 163 ? 40.277 -41.669 -4.006  0.72 33.53 ?  163 LYS   B HD2  1 
ATOM   6395 H HD2  B LYS   B 1 163 ? 40.343 -41.830 -4.093  0.28 31.96 ?  163 LYS   B HD2  1 
ATOM   6396 H HD3  A LYS   B 1 163 ? 39.580 -40.254 -3.776  0.72 33.53 ?  163 LYS   B HD3  1 
ATOM   6397 H HD3  B LYS   B 1 163 ? 39.710 -40.408 -3.751  0.28 31.96 ?  163 LYS   B HD3  1 
ATOM   6398 H HE2  A LYS   B 1 163 ? 37.506 -41.517 -3.532  0.72 36.79 ?  163 LYS   B HE2  1 
ATOM   6399 H HE2  B LYS   B 1 163 ? 37.606 -41.637 -3.502  0.28 34.55 ?  163 LYS   B HE2  1 
ATOM   6400 H HE3  A LYS   B 1 163 ? 38.435 -42.790 -3.377  0.72 36.79 ?  163 LYS   B HE3  1 
ATOM   6401 H HE3  B LYS   B 1 163 ? 38.527 -42.927 -3.391  0.28 34.55 ?  163 LYS   B HE3  1 
ATOM   6402 H HZ1  A LYS   B 1 163 ? 37.883 -41.961 -1.340  0.72 38.77 ?  163 LYS   B HZ1  1 
ATOM   6403 H HZ1  B LYS   B 1 163 ? 38.050 -42.111 -1.328  0.28 35.62 ?  163 LYS   B HZ1  1 
ATOM   6404 H HZ2  A LYS   B 1 163 ? 39.318 -41.854 -1.511  0.72 38.77 ?  163 LYS   B HZ2  1 
ATOM   6405 H HZ2  B LYS   B 1 163 ? 39.478 -42.005 -1.544  0.28 35.62 ?  163 LYS   B HZ2  1 
ATOM   6406 H HZ3  A LYS   B 1 163 ? 38.483 -40.678 -1.646  0.72 38.77 ?  163 LYS   B HZ3  1 
ATOM   6407 H HZ3  B LYS   B 1 163 ? 38.641 -40.827 -1.645  0.28 35.62 ?  163 LYS   B HZ3  1 
ATOM   6408 N N    . LEU   B 1 164 ? 39.029 -38.057 -8.020  1.00 14.65 ?  164 LEU   B N    1 
ATOM   6409 C CA   . LEU   B 1 164 ? 38.112 -36.923 -8.073  1.00 14.45 ?  164 LEU   B CA   1 
ATOM   6410 C C    . LEU   B 1 164 ? 37.333 -36.908 -9.383  1.00 14.70 ?  164 LEU   B C    1 
ATOM   6411 O O    . LEU   B 1 164 ? 36.108 -36.718 -9.388  1.00 15.84 ?  164 LEU   B O    1 
ATOM   6412 C CB   . LEU   B 1 164 ? 38.913 -35.627 -7.913  1.00 14.02 ?  164 LEU   B CB   1 
ATOM   6413 C CG   . LEU   B 1 164 ? 39.446 -35.349 -6.511  1.00 15.13 ?  164 LEU   B CG   1 
ATOM   6414 C CD1  . LEU   B 1 164 ? 40.523 -34.271 -6.561  1.00 15.17 ?  164 LEU   B CD1  1 
ATOM   6415 C CD2  . LEU   B 1 164 ? 38.326 -34.934 -5.574  1.00 16.73 ?  164 LEU   B CD2  1 
ATOM   6416 H H    A LEU   B 1 164 ? 39.865 -37.837 -8.011  0.72 17.58 ?  164 LEU   B H    1 
ATOM   6417 H H    B LEU   B 1 164 ? 39.866 -37.839 -8.050  0.28 17.58 ?  164 LEU   B H    1 
ATOM   6418 H HA   . LEU   B 1 164 ? 37.484 -36.986 -7.345  1.00 17.35 ?  164 LEU   B HA   1 
ATOM   6419 H HB2  . LEU   B 1 164 ? 39.679 -35.661 -8.515  1.00 16.82 ?  164 LEU   B HB2  1 
ATOM   6420 H HB3  . LEU   B 1 164 ? 38.345 -34.883 -8.161  1.00 16.82 ?  164 LEU   B HB3  1 
ATOM   6421 H HG   . LEU   B 1 164 ? 39.855 -36.156 -6.162  1.00 18.17 ?  164 LEU   B HG   1 
ATOM   6422 H HD11 . LEU   B 1 164 ? 40.847 -34.103 -5.661  1.00 18.20 ?  164 LEU   B HD11 1 
ATOM   6423 H HD12 . LEU   B 1 164 ? 41.257 -34.578 -7.121  1.00 18.20 ?  164 LEU   B HD12 1 
ATOM   6424 H HD13 . LEU   B 1 164 ? 40.145 -33.459 -6.933  1.00 18.20 ?  164 LEU   B HD13 1 
ATOM   6425 H HD21 . LEU   B 1 164 ? 38.704 -34.703 -4.712  1.00 20.08 ?  164 LEU   B HD21 1 
ATOM   6426 H HD22 . LEU   B 1 164 ? 37.866 -34.169 -5.951  1.00 20.08 ?  164 LEU   B HD22 1 
ATOM   6427 H HD23 . LEU   B 1 164 ? 37.709 -35.677 -5.476  1.00 20.08 ?  164 LEU   B HD23 1 
ATOM   6428 N N    . VAL   B 1 165 ? 38.029 -37.075 -10.508 1.00 16.30 ?  165 VAL   B N    1 
ATOM   6429 C CA   . VAL   B 1 165 ? 37.374 -37.013 -11.810 1.00 17.55 ?  165 VAL   B CA   1 
ATOM   6430 C C    . VAL   B 1 165 ? 36.450 -38.207 -11.995 1.00 19.27 ?  165 VAL   B C    1 
ATOM   6431 O O    . VAL   B 1 165 ? 35.289 -38.067 -12.403 1.00 20.36 ?  165 VAL   B O    1 
ATOM   6432 C CB   . VAL   B 1 165 ? 38.420 -36.929 -12.938 1.00 18.46 ?  165 VAL   B CB   1 
ATOM   6433 C CG1  . VAL   B 1 165 ? 37.754 -37.042 -14.295 1.00 19.83 ?  165 VAL   B CG1  1 
ATOM   6434 C CG2  . VAL   B 1 165 ? 39.208 -35.636 -12.836 1.00 18.26 ?  165 VAL   B CG2  1 
ATOM   6435 H H    . VAL   B 1 165 ? 38.880 -37.220 -10.544 1.00 19.56 ?  165 VAL   B H    1 
ATOM   6436 H HA   . VAL   B 1 165 ? 36.835 -36.213 -11.852 1.00 21.07 ?  165 VAL   B HA   1 
ATOM   6437 H HB   . VAL   B 1 165 ? 39.048 -37.663 -12.848 1.00 22.16 ?  165 VAL   B HB   1 
ATOM   6438 H HG11 . VAL   B 1 165 ? 38.373 -36.746 -14.978 1.00 23.80 ?  165 VAL   B HG11 1 
ATOM   6439 H HG12 . VAL   B 1 165 ? 37.518 -37.973 -14.451 1.00 23.80 ?  165 VAL   B HG12 1 
ATOM   6440 H HG13 . VAL   B 1 165 ? 36.958 -36.493 -14.303 1.00 23.80 ?  165 VAL   B HG13 1 
ATOM   6441 H HG21 . VAL   B 1 165 ? 39.844 -35.589 -13.570 1.00 21.91 ?  165 VAL   B HG21 1 
ATOM   6442 H HG22 . VAL   B 1 165 ? 38.595 -34.884 -12.885 1.00 21.91 ?  165 VAL   B HG22 1 
ATOM   6443 H HG23 . VAL   B 1 165 ? 39.684 -35.616 -11.989 1.00 21.91 ?  165 VAL   B HG23 1 
ATOM   6444 N N    . SER   B 1 166 ? 36.957 -39.406 -11.696 1.00 19.99 ?  166 SER   B N    1 
ATOM   6445 C CA   . SER   B 1 166 ? 36.198 -40.614 -11.984 1.00 21.28 ?  166 SER   B CA   1 
ATOM   6446 C C    . SER   B 1 166 ? 34.940 -40.704 -11.136 1.00 21.53 ?  166 SER   B C    1 
ATOM   6447 O O    . SER   B 1 166 ? 33.967 -41.319 -11.567 1.00 23.32 ?  166 SER   B O    1 
ATOM   6448 C CB   . SER   B 1 166 ? 37.063 -41.870 -11.821 1.00 22.14 ?  166 SER   B CB   1 
ATOM   6449 O OG   . SER   B 1 166 ? 37.432 -42.082 -10.470 1.00 21.95 ?  166 SER   B OG   1 
ATOM   6450 H H    . SER   B 1 166 ? 37.734 -39.545 -11.343 1.00 24.00 ?  166 SER   B H    1 
ATOM   6451 H HA   . SER   B 1 166 ? 35.921 -40.588 -12.913 1.00 25.54 ?  166 SER   B HA   1 
ATOM   6452 H HB2  . SER   B 1 166 ? 36.561 -42.640 -12.132 1.00 26.57 ?  166 SER   B HB2  1 
ATOM   6453 H HB3  . SER   B 1 166 ? 37.868 -41.769 -12.359 1.00 26.57 ?  166 SER   B HB3  1 
ATOM   6454 H HG   . SER   B 1 166 ? 37.886 -41.433 -10.193 1.00 26.35 ?  166 SER   B HG   1 
ATOM   6455 N N    . SER   B 1 167 ? 34.924 -40.109 -9.945  1.00 20.17 ?  167 SER   B N    1 
ATOM   6456 C CA   . SER   B 1 167 ? 33.764 -40.162 -9.062  1.00 19.52 ?  167 SER   B CA   1 
ATOM   6457 C C    . SER   B 1 167 ? 32.848 -38.941 -9.164  1.00 19.07 ?  167 SER   B C    1 
ATOM   6458 O O    . SER   B 1 167 ? 31.768 -38.943 -8.561  1.00 19.36 ?  167 SER   B O    1 
ATOM   6459 C CB   . SER   B 1 167 ? 34.203 -40.347 -7.602  1.00 19.52 ?  167 SER   B CB   1 
ATOM   6460 O OG   . SER   B 1 167 ? 34.877 -39.187 -7.126  1.00 19.11 ?  167 SER   B OG   1 
ATOM   6461 H H    . SER   B 1 167 ? 35.582 -39.671 -9.625  1.00 24.21 ?  167 SER   B H    1 
ATOM   6462 H HA   . SER   B 1 167 ? 33.233 -40.942 -9.302  1.00 23.43 ?  167 SER   B HA   1 
ATOM   6463 H HB2  . SER   B 1 167 ? 33.417 -40.511 -7.055  1.00 23.43 ?  167 SER   B HB2  1 
ATOM   6464 H HB3  . SER   B 1 167 ? 34.800 -41.118 -7.549  1.00 23.43 ?  167 SER   B HB3  1 
ATOM   6465 H HG   . SER   B 1 167 ? 35.562 -39.054 -7.594  1.00 22.94 ?  167 SER   B HG   1 
ATOM   6466 N N    . PHE   B 1 168 ? 33.229 -37.908 -9.918  1.00 18.80 ?  168 PHE   B N    1 
ATOM   6467 C CA   . PHE   B 1 168 ? 32.397 -36.706 -9.986  1.00 18.33 ?  168 PHE   B CA   1 
ATOM   6468 C C    . PHE   B 1 168 ? 31.080 -36.970 -10.711 1.00 15.88 ?  168 PHE   B C    1 
ATOM   6469 O O    . PHE   B 1 168 ? 30.040 -36.373 -10.368 1.00 16.74 ?  168 PHE   B O    1 
ATOM   6470 C CB   . PHE   B 1 168 ? 33.162 -35.576 -10.675 1.00 19.24 ?  168 PHE   B CB   1 
ATOM   6471 C CG   . PHE   B 1 168 ? 32.365 -34.320 -10.806 1.00 19.04 ?  168 PHE   B CG   1 
ATOM   6472 C CD1  . PHE   B 1 168 ? 32.038 -33.584 -9.677  1.00 20.49 ?  168 PHE   B CD1  1 
ATOM   6473 C CD2  . PHE   B 1 168 ? 31.918 -33.884 -12.038 1.00 18.47 ?  168 PHE   B CD2  1 
ATOM   6474 C CE1  . PHE   B 1 168 ? 31.281 -32.434 -9.772  1.00 20.86 ?  168 PHE   B CE1  1 
ATOM   6475 C CE2  . PHE   B 1 168 ? 31.173 -32.718 -12.146 1.00 19.65 ?  168 PHE   B CE2  1 
ATOM   6476 C CZ   . PHE   B 1 168 ? 30.851 -31.991 -11.008 1.00 20.08 ?  168 PHE   B CZ   1 
ATOM   6477 H H    . PHE   B 1 168 ? 33.947 -37.881 -10.387 1.00 22.56 ?  168 PHE   B H    1 
ATOM   6478 H HA   . PHE   B 1 168 ? 32.185 -36.420 -9.085  1.00 22.00 ?  168 PHE   B HA   1 
ATOM   6479 H HB2  . PHE   B 1 168 ? 33.954 -35.373 -10.155 1.00 23.10 ?  168 PHE   B HB2  1 
ATOM   6480 H HB3  . PHE   B 1 168 ? 33.413 -35.864 -11.565 1.00 23.10 ?  168 PHE   B HB3  1 
ATOM   6481 H HD1  . PHE   B 1 168 ? 32.322 -33.881 -8.843  1.00 24.59 ?  168 PHE   B HD1  1 
ATOM   6482 H HD2  . PHE   B 1 168 ? 32.133 -34.363 -12.804 1.00 22.17 ?  168 PHE   B HD2  1 
ATOM   6483 H HE1  . PHE   B 1 168 ? 31.072 -31.950 -9.006  1.00 25.04 ?  168 PHE   B HE1  1 
ATOM   6484 H HE2  . PHE   B 1 168 ? 30.879 -32.426 -12.981 1.00 23.59 ?  168 PHE   B HE2  1 
ATOM   6485 H HZ   . PHE   B 1 168 ? 30.344 -31.213 -11.079 1.00 24.10 ?  168 PHE   B HZ   1 
ATOM   6486 N N    . LEU   B 1 169 ? 31.109 -37.846 -11.713 1.00 16.23 ?  169 LEU   B N    1 
ATOM   6487 C CA   . LEU   B 1 169 ? 29.934 -38.146 -12.523 1.00 18.77 ?  169 LEU   B CA   1 
ATOM   6488 C C    . LEU   B 1 169 ? 29.925 -39.580 -13.040 1.00 21.29 ?  169 LEU   B C    1 
ATOM   6489 O O    . LEU   B 1 169 ? 29.014 -39.985 -13.768 1.00 23.56 ?  169 LEU   B O    1 
ATOM   6490 C CB   . LEU   B 1 169 ? 29.860 -37.190 -13.714 1.00 21.07 ?  169 LEU   B CB   1 
ATOM   6491 C CG   . LEU   B 1 169 ? 28.596 -36.336 -13.810 1.00 24.34 ?  169 LEU   B CG   1 
ATOM   6492 C CD1  . LEU   B 1 169 ? 28.556 -35.628 -15.149 1.00 25.50 ?  169 LEU   B CD1  1 
ATOM   6493 C CD2  . LEU   B 1 169 ? 27.345 -37.171 -13.606 1.00 24.40 ?  169 LEU   B CD2  1 
ATOM   6494 O OXT  . LEU   B 1 169 ? 30.830 -40.358 -12.755 1.00 22.15 -1 169 LEU   B OXT  1 
ATOM   6495 H H    . LEU   B 1 169 ? 31.813 -38.281 -11.956 1.00 19.48 ?  169 LEU   B H    1 
ATOM   6496 H HA   . LEU   B 1 169 ? 29.148 -38.014 -11.977 1.00 22.53 ?  169 LEU   B HA   1 
ATOM   6497 H HB2  . LEU   B 1 169 ? 30.615 -36.581 -13.670 1.00 25.29 ?  169 LEU   B HB2  1 
ATOM   6498 H HB3  . LEU   B 1 169 ? 29.915 -37.710 -14.532 1.00 25.29 ?  169 LEU   B HB3  1 
ATOM   6499 H HG   . LEU   B 1 169 ? 28.621 -35.656 -13.117 1.00 29.22 ?  169 LEU   B HG   1 
ATOM   6500 H HD11 . LEU   B 1 169 ? 27.763 -35.070 -15.186 1.00 30.61 ?  169 LEU   B HD11 1 
ATOM   6501 H HD12 . LEU   B 1 169 ? 29.351 -35.080 -15.240 1.00 30.61 ?  169 LEU   B HD12 1 
ATOM   6502 H HD13 . LEU   B 1 169 ? 28.528 -36.292 -15.854 1.00 30.61 ?  169 LEU   B HD13 1 
ATOM   6503 H HD21 . LEU   B 1 169 ? 26.594 -36.722 -14.019 1.00 29.28 ?  169 LEU   B HD21 1 
ATOM   6504 H HD22 . LEU   B 1 169 ? 27.479 -38.041 -14.017 1.00 29.28 ?  169 LEU   B HD22 1 
ATOM   6505 H HD23 . LEU   B 1 169 ? 27.190 -37.276 -12.655 1.00 29.28 ?  169 LEU   B HD23 1 
HETATM 6506 C C1   T TFA   C 2 .   ? 12.150 -1.263  1.479   0.30 11.13 ?  201 TFA   A C1   1 
HETATM 6507 C C2   T TFA   C 2 .   ? 12.768 -1.728  0.134   0.30 13.60 ?  201 TFA   A C2   1 
HETATM 6508 O O    T TFA   C 2 .   ? 12.845 -1.547  2.462   0.30 9.49  ?  201 TFA   A O    1 
HETATM 6509 F F1   T TFA   C 2 .   ? 12.804 -3.072  0.098   0.30 14.63 ?  201 TFA   A F1   1 
HETATM 6510 F F2   T TFA   C 2 .   ? 12.061 -1.341  -0.938  0.30 14.22 ?  201 TFA   A F2   1 
HETATM 6511 F F3   T TFA   C 2 .   ? 14.009 -1.268  -0.068  0.30 15.09 ?  201 TFA   A F3   1 
HETATM 6512 O OXT  T TFA   C 2 .   ? 11.075 -0.668  1.390   0.30 11.40 ?  201 TFA   A OXT  1 
HETATM 6513 N N2   B A1A9O D 3 .   ? 14.782 -0.148  4.092   0.28 14.37 ?  202 A1A9O A N2   1 
HETATM 6514 C C3   B A1A9O D 3 .   ? 12.118 0.183   0.456   0.28 17.64 ?  202 A1A9O A C3   1 
HETATM 6515 C C6   B A1A9O D 3 .   ? 10.489 1.951   -1.102  0.28 18.36 ?  202 A1A9O A C6   1 
HETATM 6516 C C9   B A1A9O D 3 .   ? 14.595 -0.449  1.207   0.28 16.26 ?  202 A1A9O A C9   1 
HETATM 6517 C C12  B A1A9O D 3 .   ? 14.863 -0.064  5.473   0.28 14.41 ?  202 A1A9O A C12  1 
HETATM 6518 C C14  B A1A9O D 3 .   ? 15.272 2.213   3.952   0.28 13.28 ?  202 A1A9O A C14  1 
HETATM 6519 C C1   B A1A9O D 3 .   ? 12.747 -2.276  0.874   0.28 16.93 ?  202 A1A9O A C1   1 
HETATM 6520 C C10  B A1A9O D 3 .   ? 15.112 -0.366  -0.273  0.28 16.92 ?  202 A1A9O A C10  1 
HETATM 6521 C C11  B A1A9O D 3 .   ? 14.977 0.962   3.309   0.28 13.98 ?  202 A1A9O A C11  1 
HETATM 6522 C C13  B A1A9O D 3 .   ? 15.324 2.140   5.386   0.28 12.99 ?  202 A1A9O A C13  1 
HETATM 6523 C C15  B A1A9O D 3 .   ? 15.558 3.608   3.625   0.28 13.11 ?  202 A1A9O A C15  1 
HETATM 6524 C C16  B A1A9O D 3 .   ? 15.752 4.293   4.820   0.28 12.24 ?  202 A1A9O A C16  1 
HETATM 6525 C C2   B A1A9O D 3 .   ? 13.012 -0.797  1.300   0.28 17.10 ?  202 A1A9O A C2   1 
HETATM 6526 C C4   B A1A9O D 3 .   ? 11.756 1.473   0.929   0.28 18.24 ?  202 A1A9O A C4   1 
HETATM 6527 C C5   B A1A9O D 3 .   ? 10.954 2.349   0.164   0.28 18.38 ?  202 A1A9O A C5   1 
HETATM 6528 C C7   B A1A9O D 3 .   ? 10.836 0.682   -1.596  0.28 18.22 ?  202 A1A9O A C7   1 
HETATM 6529 C C8   B A1A9O D 3 .   ? 11.640 -0.183  -0.824  0.28 17.71 ?  202 A1A9O A C8   1 
HETATM 6530 N N1   B A1A9O D 3 .   ? 14.891 0.827   1.887   0.28 14.87 ?  202 A1A9O A N1   1 
HETATM 6531 N N3   B A1A9O D 3 .   ? 15.122 1.043   6.169   0.28 13.93 ?  202 A1A9O A N3   1 
HETATM 6532 N N4   B A1A9O D 3 .   ? 15.614 3.389   5.845   0.28 11.77 ?  202 A1A9O A N4   1 
HETATM 6533 O O1   B A1A9O D 3 .   ? 16.491 -0.086  -0.248  0.28 17.47 ?  202 A1A9O A O1   1 
HETATM 6534 H H8   B A1A9O D 3 .   ? 9.853  2.640   -1.713  0.28 22.03 ?  202 A1A9O A H8   1 
HETATM 6535 H H2   B A1A9O D 3 .   ? 15.103 -1.301  1.742   0.28 19.52 ?  202 A1A9O A H2   1 
HETATM 6536 H H15  B A1A9O D 3 .   ? 14.690 -0.988  6.071   0.28 17.30 ?  202 A1A9O A H15  1 
HETATM 6537 H H4   B A1A9O D 3 .   ? 11.677 -2.515  0.750   0.28 20.32 ?  202 A1A9O A H4   1 
HETATM 6538 H H5   B A1A9O D 3 .   ? 13.139 -3.009  1.599   0.28 20.32 ?  202 A1A9O A H5   1 
HETATM 6539 H H3   B A1A9O D 3 .   ? 13.207 -2.572  -0.101  0.28 20.32 ?  202 A1A9O A H3   1 
HETATM 6540 H H11  B A1A9O D 3 .   ? 14.930 -1.297  -0.826  0.28 20.31 ?  202 A1A9O A H11  1 
HETATM 6541 H H12  B A1A9O D 3 .   ? 14.547 0.437   -0.788  0.28 20.31 ?  202 A1A9O A H12  1 
HETATM 6542 H H16  B A1A9O D 3 .   ? 15.615 4.102   2.671   0.28 15.74 ?  202 A1A9O A H16  1 
HETATM 6543 H H17  B A1A9O D 3 .   ? 15.981 5.322   5.115   0.28 14.69 ?  202 A1A9O A H17  1 
HETATM 6544 H H1   B A1A9O D 3 .   ? 12.742 -0.727  2.397   0.28 20.53 ?  202 A1A9O A H1   1 
HETATM 6545 H H6   B A1A9O D 3 .   ? 12.101 1.823   1.928   0.28 21.90 ?  202 A1A9O A H6   1 
HETATM 6546 H H7   B A1A9O D 3 .   ? 10.671 3.368   0.556   0.28 22.06 ?  202 A1A9O A H7   1 
HETATM 6547 H H9   B A1A9O D 3 .   ? 10.466 0.365   -2.605  0.28 21.87 ?  202 A1A9O A H9   1 
HETATM 6548 H H10  B A1A9O D 3 .   ? 11.891 -1.183  -1.241  0.28 21.25 ?  202 A1A9O A H10  1 
HETATM 6549 H H14  B A1A9O D 3 .   ? 15.039 1.649   1.291   0.28 17.85 ?  202 A1A9O A H14  1 
HETATM 6550 H H18  B A1A9O D 3 .   ? 15.704 3.641   6.860   0.28 14.13 ?  202 A1A9O A H18  1 
HETATM 6551 H H13  B A1A9O D 3 .   ? 16.858 -0.097  -1.147  0.28 20.97 ?  202 A1A9O A H13  1 
HETATM 6552 O O    . HOH   E 4 .   ? 4.759  3.739   0.607   1.00 22.77 ?  301 HOH   A O    1 
HETATM 6553 O O    . HOH   E 4 .   ? 14.741 -4.654  20.514  1.00 45.50 ?  302 HOH   A O    1 
HETATM 6554 O O    . HOH   E 4 .   ? 17.063 -17.987 15.066  1.00 25.79 ?  303 HOH   A O    1 
HETATM 6555 O O    B HOH   E 4 .   ? 15.028 6.982   7.181   0.28 18.77 ?  304 HOH   A O    1 
HETATM 6556 O O    . HOH   E 4 .   ? 34.342 -1.863  12.485  1.00 38.16 ?  305 HOH   A O    1 
HETATM 6557 O O    . HOH   E 4 .   ? 15.103 -12.188 18.714  1.00 37.94 ?  306 HOH   A O    1 
HETATM 6558 O O    . HOH   E 4 .   ? 6.884  -7.986  11.855  1.00 18.02 ?  307 HOH   A O    1 
HETATM 6559 O O    . HOH   E 4 .   ? 11.981 0.392   14.799  1.00 32.70 ?  308 HOH   A O    1 
HETATM 6560 O O    . HOH   E 4 .   ? 8.821  -12.093 17.113  1.00 45.18 ?  309 HOH   A O    1 
HETATM 6561 O O    . HOH   E 4 .   ? 18.593 -2.385  -16.433 1.00 47.46 ?  310 HOH   A O    1 
HETATM 6562 O O    . HOH   E 4 .   ? 28.954 0.498   -9.699  1.00 21.52 ?  311 HOH   A O    1 
HETATM 6563 O O    . HOH   E 4 .   ? 21.269 -2.311  -2.317  1.00 15.70 ?  312 HOH   A O    1 
HETATM 6564 O O    . HOH   E 4 .   ? 0.710  -4.185  0.164   1.00 29.07 ?  313 HOH   A O    1 
HETATM 6565 O O    . HOH   E 4 .   ? 9.180  -10.086 19.408  1.00 38.11 ?  314 HOH   A O    1 
HETATM 6566 O O    . HOH   E 4 .   ? 14.435 -24.674 11.616  1.00 39.35 ?  315 HOH   A O    1 
HETATM 6567 O O    . HOH   E 4 .   ? 42.474 10.554  5.218   1.00 20.78 ?  316 HOH   A O    1 
HETATM 6568 O O    A HOH   E 4 .   ? -0.485 -3.057  3.096   0.72 31.68 ?  317 HOH   A O    1 
HETATM 6569 O O    . HOH   E 4 .   ? 14.653 -13.939 16.722  1.00 25.10 ?  318 HOH   A O    1 
HETATM 6570 O O    . HOH   E 4 .   ? 36.154 -5.088  -0.528  1.00 31.11 ?  319 HOH   A O    1 
HETATM 6571 O O    B HOH   E 4 .   ? 18.377 -1.787  0.468   0.28 19.72 ?  320 HOH   A O    1 
HETATM 6572 O O    . HOH   E 4 .   ? 18.661 -19.390 13.538  1.00 37.56 ?  321 HOH   A O    1 
HETATM 6573 O O    . HOH   E 4 .   ? 19.870 -12.460 -8.974  1.00 24.73 ?  322 HOH   A O    1 
HETATM 6574 O O    . HOH   E 4 .   ? 30.224 -13.326 -8.585  1.00 21.18 ?  323 HOH   A O    1 
HETATM 6575 O O    . HOH   E 4 .   ? 28.172 -6.300  19.688  1.00 41.13 ?  324 HOH   A O    1 
HETATM 6576 O O    . HOH   E 4 .   ? 15.034 4.020   17.693  1.00 39.61 ?  325 HOH   A O    1 
HETATM 6577 O O    . HOH   E 4 .   ? 26.452 -19.330 -1.784  1.00 14.31 ?  326 HOH   A O    1 
HETATM 6578 O O    . HOH   E 4 .   ? 28.288 -0.089  -13.396 1.00 34.79 ?  327 HOH   A O    1 
HETATM 6579 O O    . HOH   E 4 .   ? 11.698 -10.845 -10.155 1.00 45.48 ?  328 HOH   A O    1 
HETATM 6580 O O    . HOH   E 4 .   ? 14.173 -4.553  -11.930 1.00 32.70 ?  329 HOH   A O    1 
HETATM 6581 O O    . HOH   E 4 .   ? 27.317 13.789  2.881   1.00 30.35 ?  330 HOH   A O    1 
HETATM 6582 O O    . HOH   E 4 .   ? 38.276 10.105  7.201   1.00 37.29 ?  331 HOH   A O    1 
HETATM 6583 O O    . HOH   E 4 .   ? 7.896  -12.519 -0.903  1.00 19.61 ?  332 HOH   A O    1 
HETATM 6584 O O    . HOH   E 4 .   ? 34.020 -1.047  -8.938  1.00 27.43 ?  333 HOH   A O    1 
HETATM 6585 O O    . HOH   E 4 .   ? 20.071 4.527   -7.536  1.00 18.63 ?  334 HOH   A O    1 
HETATM 6586 O O    . HOH   E 4 .   ? 37.549 2.816   10.259  1.00 30.64 ?  335 HOH   A O    1 
HETATM 6587 O O    . HOH   E 4 .   ? 15.169 -8.067  -9.746  1.00 23.23 ?  336 HOH   A O    1 
HETATM 6588 O O    . HOH   E 4 .   ? 9.812  -21.339 5.698   1.00 18.88 ?  337 HOH   A O    1 
HETATM 6589 O O    . HOH   E 4 .   ? 14.536 -0.539  -12.132 1.00 21.61 ?  338 HOH   A O    1 
HETATM 6590 O O    . HOH   E 4 .   ? 30.993 -18.133 7.799   1.00 19.55 ?  339 HOH   A O    1 
HETATM 6591 O O    A HOH   E 4 .   ? 14.628 -3.631  3.099   0.72 14.35 ?  340 HOH   A O    1 
HETATM 6592 O O    . HOH   E 4 .   ? 7.957  -21.464 4.013   1.00 47.46 ?  341 HOH   A O    1 
HETATM 6593 O O    . HOH   E 4 .   ? 22.308 5.399   18.972  1.00 39.93 ?  342 HOH   A O    1 
HETATM 6594 O O    . HOH   E 4 .   ? 18.857 -21.950 6.980   1.00 32.96 ?  343 HOH   A O    1 
HETATM 6595 O O    . HOH   E 4 .   ? 15.496 11.885  7.931   1.00 37.57 ?  344 HOH   A O    1 
HETATM 6596 O O    . HOH   E 4 .   ? 13.229 -1.482  -6.648  1.00 16.69 ?  345 HOH   A O    1 
HETATM 6597 O O    A HOH   E 4 .   ? 3.585  -9.436  9.724   0.72 25.37 ?  346 HOH   A O    1 
HETATM 6598 O O    . HOH   E 4 .   ? 22.705 12.485  1.638   1.00 15.05 ?  347 HOH   A O    1 
HETATM 6599 O O    . HOH   E 4 .   ? 26.855 11.421  1.661   1.00 16.94 ?  348 HOH   A O    1 
HETATM 6600 O O    . HOH   E 4 .   ? 44.355 7.109   6.434   1.00 27.15 ?  349 HOH   A O    1 
HETATM 6601 O O    . HOH   E 4 .   ? 20.609 -19.717 -5.074  1.00 26.77 ?  350 HOH   A O    1 
HETATM 6602 O O    . HOH   E 4 .   ? 38.573 4.967   6.985   1.00 16.20 ?  351 HOH   A O    1 
HETATM 6603 O O    . HOH   E 4 .   ? 39.765 -1.027  -5.176  1.00 20.89 ?  352 HOH   A O    1 
HETATM 6604 O O    . HOH   E 4 .   ? 24.032 -2.083  -2.073  1.00 10.70 ?  353 HOH   A O    1 
HETATM 6605 O O    . HOH   E 4 .   ? 35.744 -12.677 6.869   1.00 16.07 ?  354 HOH   A O    1 
HETATM 6606 O O    . HOH   E 4 .   ? -0.640 -8.361  2.107   1.00 43.75 ?  355 HOH   A O    1 
HETATM 6607 O O    . HOH   E 4 .   ? 37.321 11.978  4.987   1.00 32.70 ?  356 HOH   A O    1 
HETATM 6608 O O    A HOH   E 4 .   ? 14.269 0.595   6.804   0.72 17.47 ?  357 HOH   A O    1 
HETATM 6609 O O    . HOH   E 4 .   ? 31.701 8.205   14.885  1.00 23.80 ?  358 HOH   A O    1 
HETATM 6610 O O    . HOH   E 4 .   ? 28.563 -10.638 -14.013 1.00 43.89 ?  359 HOH   A O    1 
HETATM 6611 O O    A HOH   E 4 .   ? 17.491 -1.691  0.446   0.72 18.77 ?  360 HOH   A O    1 
HETATM 6612 O O    . HOH   E 4 .   ? 14.317 -21.188 -4.260  1.00 30.44 ?  361 HOH   A O    1 
HETATM 6613 O O    . HOH   E 4 .   ? 42.575 4.268   5.387   1.00 30.91 ?  362 HOH   A O    1 
HETATM 6614 O O    . HOH   E 4 .   ? 31.059 -13.935 -2.480  1.00 14.14 ?  363 HOH   A O    1 
HETATM 6615 O O    . HOH   E 4 .   ? 17.127 -17.767 -5.050  1.00 26.48 ?  364 HOH   A O    1 
HETATM 6616 O O    . HOH   E 4 .   ? 31.809 -9.339  -6.660  1.00 22.78 ?  365 HOH   A O    1 
HETATM 6617 O O    . HOH   E 4 .   ? 13.537 -15.209 -7.495  1.00 25.95 ?  366 HOH   A O    1 
HETATM 6618 O O    . HOH   E 4 .   ? 33.646 -7.150  4.309   1.00 17.27 ?  367 HOH   A O    1 
HETATM 6619 O O    . HOH   E 4 .   ? 43.965 8.443   -3.077  1.00 27.80 ?  368 HOH   A O    1 
HETATM 6620 O O    . HOH   E 4 .   ? 30.806 3.098   8.279   1.00 12.12 ?  369 HOH   A O    1 
HETATM 6621 O O    . HOH   E 4 .   ? 22.169 -19.254 11.423  1.00 34.55 ?  370 HOH   A O    1 
HETATM 6622 O O    . HOH   E 4 .   ? 37.238 -2.808  9.733   1.00 40.64 ?  371 HOH   A O    1 
HETATM 6623 O O    . HOH   E 4 .   ? 13.909 -4.904  17.464  1.00 26.96 ?  372 HOH   A O    1 
HETATM 6624 O O    . HOH   E 4 .   ? 21.874 -21.923 8.443   1.00 29.00 ?  373 HOH   A O    1 
HETATM 6625 O O    . HOH   E 4 .   ? 27.366 -5.956  -13.974 1.00 37.90 ?  374 HOH   A O    1 
HETATM 6626 O O    . HOH   E 4 .   ? 16.475 -22.045 0.958   1.00 27.08 ?  375 HOH   A O    1 
HETATM 6627 O O    . HOH   E 4 .   ? 31.013 6.183   -12.279 1.00 29.20 ?  376 HOH   A O    1 
HETATM 6628 O O    . HOH   E 4 .   ? 16.152 16.601  8.665   1.00 32.60 ?  377 HOH   A O    1 
HETATM 6629 O O    . HOH   E 4 .   ? 27.463 -10.598 14.056  1.00 17.53 ?  378 HOH   A O    1 
HETATM 6630 O O    B HOH   E 4 .   ? 14.980 -2.947  3.515   0.28 15.48 ?  379 HOH   A O    1 
HETATM 6631 O O    . HOH   E 4 .   ? 24.216 -7.746  14.447  1.00 17.10 ?  380 HOH   A O    1 
HETATM 6632 O O    . HOH   E 4 .   ? 18.593 9.490   9.046   1.00 21.43 ?  381 HOH   A O    1 
HETATM 6633 O O    . HOH   E 4 .   ? 31.726 -7.274  -9.871  1.00 21.56 ?  382 HOH   A O    1 
HETATM 6634 O O    B HOH   E 4 .   ? 7.441  1.614   -2.743  0.28 26.67 ?  383 HOH   A O    1 
HETATM 6635 O O    . HOH   E 4 .   ? 6.392  -5.442  11.101  1.00 18.35 ?  384 HOH   A O    1 
HETATM 6636 O O    . HOH   E 4 .   ? 33.501 -16.982 8.073   1.00 19.48 ?  385 HOH   A O    1 
HETATM 6637 O O    . HOH   E 4 .   ? 25.682 -0.754  -7.323  1.00 15.35 ?  386 HOH   A O    1 
HETATM 6638 O O    . HOH   E 4 .   ? 22.631 -11.939 21.799  1.00 44.91 ?  387 HOH   A O    1 
HETATM 6639 O O    T HOH   E 4 .   ? 15.402 -0.399  2.390   0.30 11.49 ?  388 HOH   A O    1 
HETATM 6640 O O    . HOH   E 4 .   ? 21.246 10.338  15.042  1.00 34.09 ?  389 HOH   A O    1 
HETATM 6641 O O    . HOH   E 4 .   ? 43.390 7.835   2.692   1.00 25.48 ?  390 HOH   A O    1 
HETATM 6642 O O    . HOH   E 4 .   ? 16.963 -19.250 4.898   1.00 15.13 ?  391 HOH   A O    1 
HETATM 6643 O O    B HOH   E 4 .   ? 19.230 -0.592  -2.017  0.28 26.11 ?  392 HOH   A O    1 
HETATM 6644 O O    . HOH   E 4 .   ? 24.656 -17.517 12.740  1.00 24.83 ?  393 HOH   A O    1 
HETATM 6645 O O    . HOH   E 4 .   ? 24.411 3.606   -1.804  1.00 15.22 ?  394 HOH   A O    1 
HETATM 6646 O O    . HOH   E 4 .   ? 11.634 -10.659 17.021  1.00 24.26 ?  395 HOH   A O    1 
HETATM 6647 O O    A HOH   E 4 .   ? 11.062 -0.354  1.936   0.42 20.79 ?  396 HOH   A O    1 
HETATM 6648 O O    A HOH   E 4 .   ? 24.583 2.062   -6.978  0.72 15.12 ?  397 HOH   A O    1 
HETATM 6649 O O    . HOH   E 4 .   ? 14.027 -23.044 7.483   1.00 17.89 ?  398 HOH   A O    1 
HETATM 6650 O O    . HOH   E 4 .   ? 10.974 1.764   12.594  1.00 23.80 ?  399 HOH   A O    1 
HETATM 6651 O O    . HOH   E 4 .   ? 37.523 -2.018  5.791   1.00 26.16 ?  400 HOH   A O    1 
HETATM 6652 O O    . HOH   E 4 .   ? 21.351 3.105   -0.312  1.00 14.03 ?  401 HOH   A O    1 
HETATM 6653 O O    A HOH   E 4 .   ? 15.794 -0.924  5.274   0.72 17.92 ?  402 HOH   A O    1 
HETATM 6654 O O    . HOH   E 4 .   ? 6.648  -3.122  12.753  1.00 27.20 ?  403 HOH   A O    1 
HETATM 6655 O O    . HOH   E 4 .   ? 30.676 1.904   16.716  1.00 20.98 ?  404 HOH   A O    1 
HETATM 6656 O O    . HOH   E 4 .   ? 10.358 -22.177 -1.233  1.00 46.35 ?  405 HOH   A O    1 
HETATM 6657 O O    . HOH   E 4 .   ? 32.771 -9.254  5.981   1.00 20.00 ?  406 HOH   A O    1 
HETATM 6658 O O    . HOH   E 4 .   ? 15.171 -21.528 14.222  1.00 17.89 ?  407 HOH   A O    1 
HETATM 6659 O O    . HOH   E 4 .   ? 27.352 2.338   18.731  1.00 29.44 ?  408 HOH   A O    1 
HETATM 6660 O O    . HOH   E 4 .   ? 23.468 11.379  4.073   1.00 12.39 ?  409 HOH   A O    1 
HETATM 6661 O O    . HOH   E 4 .   ? 20.539 -20.016 2.772   1.00 18.03 ?  410 HOH   A O    1 
HETATM 6662 O O    . HOH   E 4 .   ? 27.946 0.838   -7.132  1.00 14.21 ?  411 HOH   A O    1 
HETATM 6663 O O    . HOH   E 4 .   ? 23.896 -20.267 -1.363  1.00 16.20 ?  412 HOH   A O    1 
HETATM 6664 O O    . HOH   E 4 .   ? 21.758 -13.758 -8.154  1.00 39.93 ?  413 HOH   A O    1 
HETATM 6665 O O    . HOH   E 4 .   ? 30.026 -10.082 13.039  1.00 21.80 ?  414 HOH   A O    1 
HETATM 6666 O O    . HOH   E 4 .   ? 15.956 6.862   2.994   1.00 17.98 ?  415 HOH   A O    1 
HETATM 6667 O O    . HOH   E 4 .   ? 5.422  2.888   4.977   1.00 33.66 ?  416 HOH   A O    1 
HETATM 6668 O O    . HOH   E 4 .   ? 23.886 -15.695 -9.145  1.00 34.84 ?  417 HOH   A O    1 
HETATM 6669 O O    . HOH   E 4 .   ? 15.850 2.110   24.758  1.00 45.38 ?  418 HOH   A O    1 
HETATM 6670 O O    . HOH   E 4 .   ? 26.929 4.184   -0.667  1.00 12.76 ?  419 HOH   A O    1 
HETATM 6671 O O    . HOH   E 4 .   ? 30.304 -12.915 13.518  1.00 19.48 ?  420 HOH   A O    1 
HETATM 6672 O O    . HOH   E 4 .   ? 38.125 -1.360  -1.944  1.00 20.22 ?  421 HOH   A O    1 
HETATM 6673 O O    B HOH   E 4 .   ? 8.270  4.223   1.071   0.28 23.12 ?  422 HOH   A O    1 
HETATM 6674 O O    . HOH   E 4 .   ? 41.590 1.538   4.987   1.00 36.58 ?  423 HOH   A O    1 
HETATM 6675 O O    . HOH   E 4 .   ? 35.036 -5.223  -3.088  1.00 17.71 ?  424 HOH   A O    1 
HETATM 6676 O O    . HOH   E 4 .   ? 32.622 -4.295  -9.927  1.00 28.60 ?  425 HOH   A O    1 
HETATM 6677 O O    . HOH   E 4 .   ? 32.517 -10.646 3.201   1.00 32.21 ?  426 HOH   A O    1 
HETATM 6678 O O    . HOH   E 4 .   ? 40.916 -8.248  -6.737  1.00 37.56 ?  427 HOH   A O    1 
HETATM 6679 O O    . HOH   E 4 .   ? 44.929 -0.669  3.039   1.00 41.98 ?  428 HOH   A O    1 
HETATM 6680 O O    . HOH   E 4 .   ? 36.720 -4.987  5.379   1.00 24.36 ?  429 HOH   A O    1 
HETATM 6681 O O    . HOH   E 4 .   ? 16.182 -14.120 20.232  1.00 50.90 ?  430 HOH   A O    1 
HETATM 6682 O O    . HOH   E 4 .   ? 24.036 3.931   -4.809  1.00 22.21 ?  431 HOH   A O    1 
HETATM 6683 O O    . HOH   E 4 .   ? 10.330 -13.689 -1.682  1.00 16.66 ?  432 HOH   A O    1 
HETATM 6684 O O    . HOH   E 4 .   ? 22.632 8.159   18.387  1.00 46.53 ?  433 HOH   A O    1 
HETATM 6685 O O    . HOH   E 4 .   ? 19.470 -11.068 24.091  1.00 67.88 ?  434 HOH   A O    1 
HETATM 6686 O O    . HOH   E 4 .   ? 18.527 4.917   -15.143 1.00 46.29 ?  435 HOH   A O    1 
HETATM 6687 O O    . HOH   E 4 .   ? 18.895 1.990   -0.706  1.00 13.76 ?  436 HOH   A O    1 
HETATM 6688 O O    A HOH   E 4 .   ? 18.955 -0.646  -1.621  0.72 12.69 ?  437 HOH   A O    1 
HETATM 6689 O O    . HOH   E 4 .   ? 7.619  -5.855  -6.822  1.00 45.56 ?  438 HOH   A O    1 
HETATM 6690 O O    . HOH   E 4 .   ? 23.547 -8.016  17.131  1.00 21.55 ?  439 HOH   A O    1 
HETATM 6691 O O    . HOH   E 4 .   ? 27.120 -3.165  19.342  1.00 36.71 ?  440 HOH   A O    1 
HETATM 6692 O O    . HOH   E 4 .   ? 23.315 -20.926 1.314   1.00 18.60 ?  441 HOH   A O    1 
HETATM 6693 O O    A HOH   E 4 .   ? 16.257 2.972   -1.435  0.72 12.75 ?  442 HOH   A O    1 
HETATM 6694 O O    . HOH   E 4 .   ? 34.402 -8.095  -0.545  1.00 27.15 ?  443 HOH   A O    1 
HETATM 6695 O O    . HOH   E 4 .   ? 23.182 7.557   -3.205  1.00 34.12 ?  444 HOH   A O    1 
HETATM 6696 O O    . HOH   E 4 .   ? 37.691 -8.804  -3.404  1.00 24.40 ?  445 HOH   A O    1 
HETATM 6697 O O    . HOH   E 4 .   ? 9.414  -16.223 -1.956  1.00 36.58 ?  446 HOH   A O    1 
HETATM 6698 O O    . HOH   E 4 .   ? 21.261 -9.152  21.334  1.00 49.64 ?  447 HOH   A O    1 
HETATM 6699 O O    . HOH   E 4 .   ? 18.409 -15.971 16.330  1.00 38.13 ?  448 HOH   A O    1 
HETATM 6700 O O    . HOH   E 4 .   ? -1.393 -4.855  7.577   1.00 49.01 ?  449 HOH   A O    1 
HETATM 6701 O O    A HOH   E 4 .   ? 14.022 -0.315  3.465   0.42 29.51 ?  450 HOH   A O    1 
HETATM 6702 O O    . HOH   E 4 .   ? 30.609 14.774  2.795   1.00 18.92 ?  451 HOH   A O    1 
HETATM 6703 O O    . HOH   E 4 .   ? 31.320 -12.775 0.007   1.00 20.09 ?  452 HOH   A O    1 
HETATM 6704 O O    . HOH   E 4 .   ? 21.489 -14.681 17.978  1.00 53.58 ?  453 HOH   A O    1 
HETATM 6705 O O    B HOH   E 4 .   ? 16.287 2.979   -0.889  0.28 18.64 ?  454 HOH   A O    1 
HETATM 6706 O O    . HOH   E 4 .   ? 20.597 -17.770 24.818  1.00 52.73 ?  455 HOH   A O    1 
HETATM 6707 O O    . HOH   E 4 .   ? 29.790 -16.053 10.702  1.00 34.68 ?  456 HOH   A O    1 
HETATM 6708 O O    . HOH   E 4 .   ? 25.397 8.213   -4.818  1.00 32.27 ?  457 HOH   A O    1 
HETATM 6709 O O    . HOH   E 4 .   ? 29.768 -1.959  -12.741 1.00 45.68 ?  458 HOH   A O    1 
HETATM 6710 O O    . HOH   E 4 .   ? 27.832 7.145   -6.441  1.00 37.09 ?  459 HOH   A O    1 
HETATM 6711 O O    . HOH   E 4 .   ? 32.463 -15.944 10.874  1.00 34.77 ?  460 HOH   A O    1 
HETATM 6712 O O    . HOH   E 4 .   ? 24.847 5.639   20.772  1.00 51.99 ?  461 HOH   A O    1 
HETATM 6713 O O    . HOH   E 4 .   ? 19.845 -17.327 -5.063  1.00 23.73 ?  462 HOH   A O    1 
HETATM 6714 O O    . HOH   E 4 .   ? 23.124 -22.345 -3.354  1.00 36.02 ?  463 HOH   A O    1 
HETATM 6715 O O    . HOH   E 4 .   ? 24.628 14.673  7.833   1.00 38.81 ?  464 HOH   A O    1 
HETATM 6716 O O    . HOH   E 4 .   ? 12.003 -13.350 16.403  1.00 49.15 ?  465 HOH   A O    1 
HETATM 6717 O O    . HOH   E 4 .   ? 26.911 11.669  -1.384  1.00 32.90 ?  466 HOH   A O    1 
HETATM 6718 O O    . HOH   E 4 .   ? 15.713 -21.499 3.701   1.00 24.50 ?  467 HOH   A O    1 
HETATM 6719 O O    . HOH   E 4 .   ? 18.777 10.926  11.303  1.00 32.45 ?  468 HOH   A O    1 
HETATM 6720 O O    . HOH   E 4 .   ? 21.854 5.179   -5.717  1.00 31.46 ?  469 HOH   A O    1 
HETATM 6721 O O    . HOH   E 4 .   ? 39.617 -7.012  -3.452  1.00 45.72 ?  470 HOH   A O    1 
HETATM 6722 O O    . HOH   E 4 .   ? 27.493 -11.395 16.617  1.00 36.83 ?  471 HOH   A O    1 
HETATM 6723 O O    . HOH   E 4 .   ? 12.344 1.585   17.341  1.00 41.74 ?  472 HOH   A O    1 
HETATM 6724 O O    . HOH   E 4 .   ? 23.504 13.738  5.495   1.00 18.66 ?  473 HOH   A O    1 
HETATM 6725 O O    . HOH   E 4 .   ? 25.786 10.794  -3.778  1.00 26.56 ?  474 HOH   A O    1 
HETATM 6726 O O    . HOH   E 4 .   ? 10.973 -15.012 -6.152  1.00 35.21 ?  475 HOH   A O    1 
HETATM 6727 O O    B HOH   E 4 .   ? 6.571  3.987   3.470   0.28 21.04 ?  476 HOH   A O    1 
HETATM 6728 O O    . HOH   E 4 .   ? 23.089 11.805  -4.084  1.00 18.64 ?  477 HOH   A O    1 
HETATM 6729 O O    . HOH   E 4 .   ? 28.862 9.037   17.468  1.00 38.42 ?  478 HOH   A O    1 
HETATM 6730 O O    . HOH   E 4 .   ? 35.227 7.420   12.256  1.00 43.35 ?  479 HOH   A O    1 
HETATM 6731 O O    . HOH   E 4 .   ? 18.054 -16.225 -8.814  1.00 41.59 ?  480 HOH   A O    1 
HETATM 6732 O O    . HOH   E 4 .   ? 16.807 -20.531 16.135  1.00 29.52 ?  481 HOH   A O    1 
HETATM 6733 O O    . HOH   E 4 .   ? 15.658 -17.111 -7.012  1.00 30.52 ?  482 HOH   A O    1 
HETATM 6734 O O    . HOH   E 4 .   ? 17.372 -18.703 19.821  1.00 51.62 ?  483 HOH   A O    1 
HETATM 6735 O O    . HOH   E 4 .   ? 40.920 -3.976  -0.386  1.00 38.29 ?  484 HOH   A O    1 
HETATM 6736 O O    . HOH   E 4 .   ? 30.857 0.720   19.183  1.00 39.34 ?  485 HOH   A O    1 
HETATM 6737 O O    . HOH   E 4 .   ? 13.962 -10.313 -10.885 1.00 31.94 ?  486 HOH   A O    1 
HETATM 6738 O O    . HOH   E 4 .   ? 16.022 -6.750  -11.907 1.00 40.65 ?  487 HOH   A O    1 
HETATM 6739 O O    . HOH   E 4 .   ? 41.736 9.293   -4.081  1.00 31.30 ?  488 HOH   A O    1 
HETATM 6740 O O    . HOH   E 4 .   ? 28.656 -7.931  -15.313 1.00 47.31 ?  489 HOH   A O    1 
HETATM 6741 O O    . HOH   E 4 .   ? 44.552 10.477  -1.572  1.00 34.03 ?  490 HOH   A O    1 
HETATM 6742 O O    . HOH   E 4 .   ? 23.251 -12.869 19.335  1.00 46.53 ?  491 HOH   A O    1 
HETATM 6743 O O    . HOH   E 4 .   ? 31.459 -0.571  -10.571 1.00 30.98 ?  492 HOH   A O    1 
HETATM 6744 O O    . HOH   E 4 .   ? 18.375 -23.201 1.945   1.00 40.53 ?  493 HOH   A O    1 
HETATM 6745 O O    . HOH   E 4 .   ? 39.154 2.397   7.547   1.00 32.82 ?  494 HOH   A O    1 
HETATM 6746 O O    . HOH   E 4 .   ? 20.478 -16.079 -7.373  1.00 28.33 ?  495 HOH   A O    1 
HETATM 6747 O O    . HOH   E 4 .   ? 40.570 -0.257  -7.808  1.00 35.27 ?  496 HOH   A O    1 
HETATM 6748 O O    . HOH   E 4 .   ? 13.966 -25.266 8.876   1.00 31.54 ?  497 HOH   A O    1 
HETATM 6749 O O    . HOH   E 4 .   ? 28.590 -4.664  -12.309 1.00 36.11 ?  498 HOH   A O    1 
HETATM 6750 O O    . HOH   E 4 .   ? 20.004 -22.329 4.164   1.00 28.47 ?  499 HOH   A O    1 
HETATM 6751 O O    . HOH   E 4 .   ? 16.143 -23.392 5.729   1.00 27.47 ?  500 HOH   A O    1 
HETATM 6752 O O    B HOH   E 4 .   ? 6.956  -1.419  -3.230  0.28 33.32 ?  501 HOH   A O    1 
HETATM 6753 O O    . HOH   E 4 .   ? 37.366 -6.640  7.581   1.00 26.86 ?  502 HOH   A O    1 
HETATM 6754 O O    . HOH   E 4 .   ? 30.716 -5.835  -11.887 1.00 47.56 ?  503 HOH   A O    1 
HETATM 6755 O O    . HOH   E 4 .   ? 23.075 -23.751 1.644   1.00 31.47 ?  504 HOH   A O    1 
HETATM 6756 O O    . HOH   E 4 .   ? 30.732 5.817   -14.730 1.00 36.35 ?  505 HOH   A O    1 
HETATM 6757 O O    . HOH   E 4 .   ? 39.524 0.014   6.584   1.00 31.04 ?  506 HOH   A O    1 
HETATM 6758 O O    . HOH   E 4 .   ? 38.031 13.895  6.765   1.00 48.98 ?  507 HOH   A O    1 
HETATM 6759 O O    . HOH   E 4 .   ? 29.005 14.397  0.881   1.00 49.24 ?  508 HOH   A O    1 
HETATM 6760 O O    B HOH   E 4 .   ? 14.676 8.029   4.846   0.28 21.79 ?  509 HOH   A O    1 
HETATM 6761 O O    . HOH   E 4 .   ? 8.059  -3.020  -5.808  1.00 49.04 ?  510 HOH   A O    1 
HETATM 6762 O O    . HOH   E 4 .   ? 21.992 -24.025 4.463   1.00 27.30 ?  511 HOH   A O    1 
HETATM 6763 O O    . HOH   E 4 .   ? 36.457 -6.530  10.153  1.00 45.01 ?  512 HOH   A O    1 
HETATM 6764 O O    B HOH   E 4 .   ? 9.584  -1.581  -4.640  0.28 23.54 ?  513 HOH   A O    1 
HETATM 6765 O O    T HOH   E 4 .   ? 11.918 -2.119  -3.653  0.30 11.74 ?  514 HOH   A O    1 
HETATM 6766 O O    A HOH   E 4 .   ? 14.851 8.673   4.898   0.72 46.99 ?  515 HOH   A O    1 
HETATM 6767 O O    . HOH   E 4 .   ? 17.325 -6.552  -14.227 1.00 38.35 ?  516 HOH   A O    1 
HETATM 6768 O O    B HOH   E 4 .   ? 9.499  1.053   -5.030  0.28 18.22 ?  517 HOH   A O    1 
HETATM 6769 O O    . HOH   E 4 .   ? 24.080 9.017   -7.235  1.00 37.92 ?  518 HOH   A O    1 
HETATM 6770 O O    . HOH   E 4 .   ? 16.397 -21.127 18.808  1.00 38.53 ?  519 HOH   A O    1 
HETATM 6771 O O    . HOH   E 4 .   ? 15.874 -12.242 27.463  1.00 45.28 ?  520 HOH   A O    1 
HETATM 6772 O O    . HOH   E 4 .   ? 14.738 -22.793 19.864  1.00 37.25 ?  521 HOH   A O    1 
HETATM 6773 O O    . HOH   F 4 .   ? 29.812 -22.418 5.487   1.00 20.70 ?  201 HOH   B O    1 
HETATM 6774 O O    . HOH   F 4 .   ? 52.877 -13.417 -20.292 1.00 35.49 ?  202 HOH   B O    1 
HETATM 6775 O O    . HOH   F 4 .   ? 41.787 -36.008 -17.248 1.00 31.42 ?  203 HOH   B O    1 
HETATM 6776 O O    . HOH   F 4 .   ? 48.094 -6.889  15.592  1.00 36.94 ?  204 HOH   B O    1 
HETATM 6777 O O    . HOH   F 4 .   ? 59.165 -18.731 6.815   1.00 36.26 ?  205 HOH   B O    1 
HETATM 6778 O O    . HOH   F 4 .   ? 41.363 -7.793  5.497   1.00 38.72 ?  206 HOH   B O    1 
HETATM 6779 O O    . HOH   F 4 .   ? 37.938 -39.458 -0.202  1.00 40.88 ?  207 HOH   B O    1 
HETATM 6780 O O    . HOH   F 4 .   ? 49.429 -22.657 -19.753 1.00 48.13 ?  208 HOH   B O    1 
HETATM 6781 O O    . HOH   F 4 .   ? 50.233 -3.333  7.227   1.00 38.99 ?  209 HOH   B O    1 
HETATM 6782 O O    . HOH   F 4 .   ? 27.686 -29.189 -1.801  1.00 38.28 ?  210 HOH   B O    1 
HETATM 6783 O O    . HOH   F 4 .   ? 55.413 -16.541 -14.349 1.00 36.81 ?  211 HOH   B O    1 
HETATM 6784 O O    . HOH   F 4 .   ? 27.823 -41.886 -15.145 1.00 34.72 ?  212 HOH   B O    1 
HETATM 6785 O O    . HOH   F 4 .   ? 54.494 -9.364  -8.768  1.00 19.39 ?  213 HOH   B O    1 
HETATM 6786 O O    . HOH   F 4 .   ? 29.888 -26.297 4.014   1.00 28.68 ?  214 HOH   B O    1 
HETATM 6787 O O    . HOH   F 4 .   ? 30.213 -41.025 -8.101  1.00 17.05 ?  215 HOH   B O    1 
HETATM 6788 O O    . HOH   F 4 .   ? 58.203 -12.928 8.418   1.00 33.38 ?  216 HOH   B O    1 
HETATM 6789 O O    . HOH   F 4 .   ? 57.706 -24.446 5.050   1.00 33.09 ?  217 HOH   B O    1 
HETATM 6790 O O    . HOH   F 4 .   ? 56.367 -19.721 7.269   1.00 34.19 ?  218 HOH   B O    1 
HETATM 6791 O O    . HOH   F 4 .   ? 48.576 -36.446 -15.456 1.00 44.41 ?  219 HOH   B O    1 
HETATM 6792 O O    . HOH   F 4 .   ? 47.366 -7.349  -3.848  1.00 39.37 ?  220 HOH   B O    1 
HETATM 6793 O O    . HOH   F 4 .   ? 57.184 -26.882 -7.620  1.00 42.52 ?  221 HOH   B O    1 
HETATM 6794 O O    . HOH   F 4 .   ? 50.771 -6.102  0.161   1.00 28.24 ?  222 HOH   B O    1 
HETATM 6795 O O    . HOH   F 4 .   ? 44.469 -7.208  2.117   1.00 33.86 ?  223 HOH   B O    1 
HETATM 6796 O O    . HOH   F 4 .   ? 57.406 -16.251 -12.175 1.00 18.68 ?  224 HOH   B O    1 
HETATM 6797 O O    . HOH   F 4 .   ? 56.708 -30.759 -7.744  1.00 33.13 ?  225 HOH   B O    1 
HETATM 6798 O O    . HOH   F 4 .   ? 45.002 -43.534 -10.531 1.00 26.90 ?  226 HOH   B O    1 
HETATM 6799 O O    . HOH   F 4 .   ? 37.112 -19.783 -18.086 1.00 37.43 ?  227 HOH   B O    1 
HETATM 6800 O O    . HOH   F 4 .   ? 45.108 -34.920 6.834   1.00 38.88 ?  228 HOH   B O    1 
HETATM 6801 O O    . HOH   F 4 .   ? 34.540 -36.377 -7.217  1.00 17.92 ?  229 HOH   B O    1 
HETATM 6802 O O    . HOH   F 4 .   ? 35.967 -43.277 -8.538  1.00 30.83 ?  230 HOH   B O    1 
HETATM 6803 O O    . HOH   F 4 .   ? 30.849 -28.797 4.296   1.00 27.01 ?  231 HOH   B O    1 
HETATM 6804 O O    . HOH   F 4 .   ? 46.406 -1.588  13.264  1.00 29.58 ?  232 HOH   B O    1 
HETATM 6805 O O    . HOH   F 4 .   ? 41.521 -39.211 -14.909 1.00 22.30 ?  233 HOH   B O    1 
HETATM 6806 O O    . HOH   F 4 .   ? 51.681 -6.486  4.421   1.00 20.79 ?  234 HOH   B O    1 
HETATM 6807 O O    . HOH   F 4 .   ? 40.620 -16.035 14.158  1.00 24.72 ?  235 HOH   B O    1 
HETATM 6808 O O    . HOH   F 4 .   ? 41.344 -9.644  13.114  1.00 23.42 ?  236 HOH   B O    1 
HETATM 6809 O O    . HOH   F 4 .   ? 39.297 -10.918 6.152   1.00 26.86 ?  237 HOH   B O    1 
HETATM 6810 O O    . HOH   F 4 .   ? 25.405 -25.954 -1.322  1.00 33.44 ?  238 HOH   B O    1 
HETATM 6811 O O    . HOH   F 4 .   ? 50.725 -12.982 -0.468  1.00 12.59 ?  239 HOH   B O    1 
HETATM 6812 O O    . HOH   F 4 .   ? 28.398 -19.698 -13.129 1.00 24.12 ?  240 HOH   B O    1 
HETATM 6813 O O    . HOH   F 4 .   ? 35.084 -8.001  -2.990  1.00 18.24 ?  241 HOH   B O    1 
HETATM 6814 O O    . HOH   F 4 .   ? 48.072 -24.551 -17.758 1.00 29.65 ?  242 HOH   B O    1 
HETATM 6815 O O    . HOH   F 4 .   ? 29.800 -34.228 -0.458  1.00 35.52 ?  243 HOH   B O    1 
HETATM 6816 O O    . HOH   F 4 .   ? 42.554 -25.376 2.648   1.00 15.25 ?  244 HOH   B O    1 
HETATM 6817 O O    . HOH   F 4 .   ? 34.210 -18.512 11.413  1.00 24.13 ?  245 HOH   B O    1 
HETATM 6818 O O    . HOH   F 4 .   ? 43.216 -32.423 -17.068 1.00 23.53 ?  246 HOH   B O    1 
HETATM 6819 O O    . HOH   F 4 .   ? 42.626 -22.881 3.852   1.00 11.77 ?  247 HOH   B O    1 
HETATM 6820 O O    . HOH   F 4 .   ? 32.812 -43.808 -11.317 1.00 20.77 ?  248 HOH   B O    1 
HETATM 6821 O O    . HOH   F 4 .   ? 44.505 -27.784 -0.709  1.00 22.92 ?  249 HOH   B O    1 
HETATM 6822 O O    . HOH   F 4 .   ? 39.472 -11.110 0.350   1.00 16.82 ?  250 HOH   B O    1 
HETATM 6823 O O    . HOH   F 4 .   ? 34.875 -24.673 13.879  1.00 30.02 ?  251 HOH   B O    1 
HETATM 6824 O O    . HOH   F 4 .   ? 57.604 -24.383 -3.802  1.00 22.06 ?  252 HOH   B O    1 
HETATM 6825 O O    . HOH   F 4 .   ? 50.970 -39.930 -8.213  1.00 34.64 ?  253 HOH   B O    1 
HETATM 6826 O O    . HOH   F 4 .   ? 40.314 -12.757 -11.495 1.00 15.32 ?  254 HOH   B O    1 
HETATM 6827 O O    . HOH   F 4 .   ? 43.094 -43.273 -8.246  1.00 30.24 ?  255 HOH   B O    1 
HETATM 6828 O O    . HOH   F 4 .   ? 38.471 -11.069 -2.229  1.00 19.66 ?  256 HOH   B O    1 
HETATM 6829 O O    . HOH   F 4 .   ? 31.769 -17.918 -14.504 1.00 31.17 ?  257 HOH   B O    1 
HETATM 6830 O O    . HOH   F 4 .   ? 38.913 -12.001 12.417  1.00 35.43 ?  258 HOH   B O    1 
HETATM 6831 O O    . HOH   F 4 .   ? 30.831 -15.734 2.681   1.00 13.84 ?  259 HOH   B O    1 
HETATM 6832 O O    . HOH   F 4 .   ? 29.722 -25.231 -10.822 1.00 16.69 ?  260 HOH   B O    1 
HETATM 6833 O O    . HOH   F 4 .   ? 58.179 -10.638 -4.072  1.00 20.79 ?  261 HOH   B O    1 
HETATM 6834 O O    . HOH   F 4 .   ? 27.143 -31.845 -9.960  1.00 20.73 ?  262 HOH   B O    1 
HETATM 6835 O O    . HOH   F 4 .   ? 51.544 -13.881 11.080  1.00 27.53 ?  263 HOH   B O    1 
HETATM 6836 O O    . HOH   F 4 .   ? 41.871 -23.530 9.300   1.00 17.49 ?  264 HOH   B O    1 
HETATM 6837 O O    . HOH   F 4 .   ? 42.917 -20.347 -20.813 1.00 36.97 ?  265 HOH   B O    1 
HETATM 6838 O O    . HOH   F 4 .   ? 47.999 -22.786 5.859   1.00 17.37 ?  266 HOH   B O    1 
HETATM 6839 O O    . HOH   F 4 .   ? 28.490 -30.856 -14.769 1.00 30.49 ?  267 HOH   B O    1 
HETATM 6840 O O    . HOH   F 4 .   ? 43.351 -15.789 -12.161 1.00 14.35 ?  268 HOH   B O    1 
HETATM 6841 O O    . HOH   F 4 .   ? 42.321 -9.908  9.408   1.00 21.52 ?  269 HOH   B O    1 
HETATM 6842 O O    . HOH   F 4 .   ? 57.494 -9.231  1.450   1.00 19.82 ?  270 HOH   B O    1 
HETATM 6843 O O    . HOH   F 4 .   ? 56.163 -23.512 -14.729 1.00 27.22 ?  271 HOH   B O    1 
HETATM 6844 O O    . HOH   F 4 .   ? 49.746 -0.486  10.214  1.00 30.47 ?  272 HOH   B O    1 
HETATM 6845 O O    . HOH   F 4 .   ? 28.274 -34.380 -9.417  1.00 20.36 ?  273 HOH   B O    1 
HETATM 6846 O O    . HOH   F 4 .   ? 46.615 -31.250 -4.804  1.00 22.80 ?  274 HOH   B O    1 
HETATM 6847 O O    . HOH   F 4 .   ? 34.450 -12.791 2.626   1.00 25.12 ?  275 HOH   B O    1 
HETATM 6848 O O    . HOH   F 4 .   ? 34.937 -33.376 -19.205 1.00 33.43 ?  276 HOH   B O    1 
HETATM 6849 O O    . HOH   F 4 .   ? 56.934 -8.640  8.466   1.00 19.43 ?  277 HOH   B O    1 
HETATM 6850 O O    . HOH   F 4 .   ? 49.316 -28.704 -6.876  1.00 15.55 ?  278 HOH   B O    1 
HETATM 6851 O O    . HOH   F 4 .   ? 27.946 -22.900 -8.004  1.00 17.77 ?  279 HOH   B O    1 
HETATM 6852 O O    . HOH   F 4 .   ? 42.384 -34.736 3.768   1.00 25.89 ?  280 HOH   B O    1 
HETATM 6853 O O    . HOH   F 4 .   ? 30.561 -42.255 -10.629 1.00 29.97 ?  281 HOH   B O    1 
HETATM 6854 O O    . HOH   F 4 .   ? 46.837 -29.584 9.877   1.00 32.51 ?  282 HOH   B O    1 
HETATM 6855 O O    . HOH   F 4 .   ? 36.772 -12.785 -1.492  1.00 27.32 ?  283 HOH   B O    1 
HETATM 6856 O O    . HOH   F 4 .   ? 49.941 -24.662 5.790   1.00 33.14 ?  284 HOH   B O    1 
HETATM 6857 O O    . HOH   F 4 .   ? 57.099 -12.080 12.362  1.00 39.59 ?  285 HOH   B O    1 
HETATM 6858 O O    . HOH   F 4 .   ? 51.228 -37.604 -9.589  1.00 25.96 ?  286 HOH   B O    1 
HETATM 6859 O O    . HOH   F 4 .   ? 52.544 -10.409 13.023  1.00 23.02 ?  287 HOH   B O    1 
HETATM 6860 O O    . HOH   F 4 .   ? 41.140 -5.520  11.529  1.00 46.75 ?  288 HOH   B O    1 
HETATM 6861 O O    . HOH   F 4 .   ? 48.411 -25.064 3.130   1.00 13.59 ?  289 HOH   B O    1 
HETATM 6862 O O    . HOH   F 4 .   ? 27.549 -26.679 -15.650 1.00 33.29 ?  290 HOH   B O    1 
HETATM 6863 O O    . HOH   F 4 .   ? 59.775 -15.288 8.185   1.00 32.09 ?  291 HOH   B O    1 
HETATM 6864 O O    . HOH   F 4 .   ? 48.703 -20.039 5.964   1.00 14.57 ?  292 HOH   B O    1 
HETATM 6865 O O    . HOH   F 4 .   ? 33.507 -15.315 -13.964 1.00 21.65 ?  293 HOH   B O    1 
HETATM 6866 O O    . HOH   F 4 .   ? 42.273 -9.962  -14.882 1.00 38.95 ?  294 HOH   B O    1 
HETATM 6867 O O    . HOH   F 4 .   ? 45.380 -33.409 -15.947 1.00 23.76 ?  295 HOH   B O    1 
HETATM 6868 O O    . HOH   F 4 .   ? 42.706 -12.287 -18.510 1.00 29.48 ?  296 HOH   B O    1 
HETATM 6869 O O    . HOH   F 4 .   ? 44.021 -29.357 -4.706  1.00 24.59 ?  297 HOH   B O    1 
HETATM 6870 O O    . HOH   F 4 .   ? 37.327 -35.669 7.215   1.00 32.17 ?  298 HOH   B O    1 
HETATM 6871 O O    . HOH   F 4 .   ? 44.604 -27.461 2.008   1.00 15.76 ?  299 HOH   B O    1 
HETATM 6872 O O    . HOH   F 4 .   ? 57.665 -22.102 3.117   1.00 28.99 ?  300 HOH   B O    1 
HETATM 6873 O O    . HOH   F 4 .   ? 47.086 -33.956 -4.589  1.00 18.18 ?  301 HOH   B O    1 
HETATM 6874 O O    . HOH   F 4 .   ? 52.533 -29.248 -13.023 1.00 24.58 ?  302 HOH   B O    1 
HETATM 6875 O O    . HOH   F 4 .   ? 52.620 -35.672 -8.620  1.00 29.63 ?  303 HOH   B O    1 
HETATM 6876 O O    . HOH   F 4 .   ? 37.496 -18.166 13.151  1.00 30.99 ?  304 HOH   B O    1 
HETATM 6877 O O    . HOH   F 4 .   ? 43.502 -15.406 18.253  1.00 32.64 ?  305 HOH   B O    1 
HETATM 6878 O O    . HOH   F 4 .   ? 45.883 -40.410 -3.558  1.00 29.92 ?  306 HOH   B O    1 
HETATM 6879 O O    . HOH   F 4 .   ? 53.142 -16.070 -12.721 1.00 28.94 ?  307 HOH   B O    1 
HETATM 6880 O O    . HOH   F 4 .   ? 53.466 -30.201 4.546   1.00 18.83 ?  308 HOH   B O    1 
HETATM 6881 O O    . HOH   F 4 .   ? 41.229 -24.493 15.812  1.00 44.80 ?  309 HOH   B O    1 
HETATM 6882 O O    . HOH   F 4 .   ? 35.024 -33.594 4.514   1.00 29.07 ?  310 HOH   B O    1 
HETATM 6883 O O    . HOH   F 4 .   ? 37.853 -10.257 -10.758 1.00 17.40 ?  311 HOH   B O    1 
HETATM 6884 O O    . HOH   F 4 .   ? 25.928 -21.491 -3.537  1.00 16.71 ?  312 HOH   B O    1 
HETATM 6885 O O    . HOH   F 4 .   ? 40.237 -10.830 -9.548  1.00 17.05 ?  313 HOH   B O    1 
HETATM 6886 O O    . HOH   F 4 .   ? 32.807 -34.600 -5.914  1.00 17.40 ?  314 HOH   B O    1 
HETATM 6887 O O    . HOH   F 4 .   ? 51.376 -32.948 -10.760 1.00 41.11 ?  315 HOH   B O    1 
HETATM 6888 O O    . HOH   F 4 .   ? 62.694 -13.557 4.727   1.00 27.78 ?  316 HOH   B O    1 
HETATM 6889 O O    . HOH   F 4 .   ? 59.952 -17.130 -10.454 1.00 34.06 ?  317 HOH   B O    1 
HETATM 6890 O O    . HOH   F 4 .   ? 43.189 -21.430 10.696  1.00 16.14 ?  318 HOH   B O    1 
HETATM 6891 O O    . HOH   F 4 .   ? 26.325 -21.030 -6.237  1.00 16.62 ?  319 HOH   B O    1 
HETATM 6892 O O    . HOH   F 4 .   ? 48.093 -32.614 -16.636 1.00 41.19 ?  320 HOH   B O    1 
HETATM 6893 O O    . HOH   F 4 .   ? 38.321 -12.753 7.963   1.00 18.50 ?  321 HOH   B O    1 
HETATM 6894 O O    . HOH   F 4 .   ? 41.733 -8.060  1.401   1.00 25.63 ?  322 HOH   B O    1 
HETATM 6895 O O    . HOH   F 4 .   ? 44.574 -24.630 9.604   1.00 19.71 ?  323 HOH   B O    1 
HETATM 6896 O O    . HOH   F 4 .   ? 62.863 -20.170 -0.767  1.00 38.18 ?  324 HOH   B O    1 
HETATM 6897 O O    . HOH   F 4 .   ? 51.742 -5.942  -7.876  1.00 49.92 ?  325 HOH   B O    1 
HETATM 6898 O O    . HOH   F 4 .   ? 37.187 -30.586 -21.053 1.00 32.00 ?  326 HOH   B O    1 
HETATM 6899 O O    . HOH   F 4 .   ? 53.641 -12.603 -22.222 1.00 34.35 ?  327 HOH   B O    1 
HETATM 6900 O O    . HOH   F 4 .   ? 38.361 -9.359  -13.276 1.00 27.27 ?  328 HOH   B O    1 
HETATM 6901 O O    . HOH   F 4 .   ? 44.167 -1.772  7.614   1.00 45.57 ?  329 HOH   B O    1 
HETATM 6902 O O    . HOH   F 4 .   ? 36.716 -12.417 4.326   1.00 18.48 ?  330 HOH   B O    1 
HETATM 6903 O O    . HOH   F 4 .   ? 27.916 -14.792 -9.414  1.00 34.74 ?  331 HOH   B O    1 
HETATM 6904 O O    . HOH   F 4 .   ? 47.173 -24.505 8.212   1.00 25.94 ?  332 HOH   B O    1 
HETATM 6905 O O    . HOH   F 4 .   ? 43.134 -34.640 0.076   1.00 20.09 ?  333 HOH   B O    1 
HETATM 6906 O O    . HOH   F 4 .   ? 48.575 -11.930 -13.865 1.00 27.55 ?  334 HOH   B O    1 
HETATM 6907 O O    . HOH   F 4 .   ? 33.549 -31.217 11.094  1.00 34.22 ?  335 HOH   B O    1 
HETATM 6908 O O    . HOH   F 4 .   ? 42.877 -43.489 -14.372 1.00 46.48 ?  336 HOH   B O    1 
HETATM 6909 O O    . HOH   F 4 .   ? 39.460 -23.551 -20.309 1.00 36.97 ?  337 HOH   B O    1 
HETATM 6910 O O    . HOH   F 4 .   ? 47.464 -27.427 2.048   1.00 15.02 ?  338 HOH   B O    1 
HETATM 6911 O O    . HOH   F 4 .   ? 46.847 -19.871 12.275  1.00 31.14 ?  339 HOH   B O    1 
HETATM 6912 O O    . HOH   F 4 .   ? 45.711 -36.284 -16.112 1.00 34.62 ?  340 HOH   B O    1 
HETATM 6913 O O    . HOH   F 4 .   ? 37.006 -15.108 -16.516 1.00 40.50 ?  341 HOH   B O    1 
HETATM 6914 O O    . HOH   F 4 .   ? 37.077 -45.220 -9.763  1.00 38.38 ?  342 HOH   B O    1 
HETATM 6915 O O    . HOH   F 4 .   ? 28.880 -42.935 -12.312 1.00 40.67 ?  343 HOH   B O    1 
HETATM 6916 O O    . HOH   F 4 .   ? 38.456 -12.278 -16.278 1.00 41.87 ?  344 HOH   B O    1 
HETATM 6917 O O    . HOH   F 4 .   ? 32.996 -14.690 1.058   1.00 19.23 ?  345 HOH   B O    1 
HETATM 6918 O O    . HOH   F 4 .   ? 38.559 -22.325 15.035  1.00 39.71 ?  346 HOH   B O    1 
HETATM 6919 O O    . HOH   F 4 .   ? 39.793 -44.315 -11.223 1.00 39.60 ?  347 HOH   B O    1 
HETATM 6920 O O    . HOH   F 4 .   ? 33.750 -9.414  -8.815  1.00 33.03 ?  348 HOH   B O    1 
HETATM 6921 O O    . HOH   F 4 .   ? 40.421 -43.508 -9.084  1.00 27.85 ?  349 HOH   B O    1 
HETATM 6922 O O    . HOH   F 4 .   ? 27.740 -26.613 -0.606  1.00 31.00 ?  350 HOH   B O    1 
HETATM 6923 O O    . HOH   F 4 .   ? 62.559 -20.204 -4.842  1.00 43.36 ?  351 HOH   B O    1 
HETATM 6924 O O    . HOH   F 4 .   ? 55.633 -8.250  10.867  1.00 25.36 ?  352 HOH   B O    1 
HETATM 6925 O O    . HOH   F 4 .   ? 23.182 -23.666 6.830   1.00 35.35 ?  353 HOH   B O    1 
HETATM 6926 O O    . HOH   F 4 .   ? 44.170 -37.323 -17.782 1.00 32.44 ?  354 HOH   B O    1 
HETATM 6927 O O    . HOH   F 4 .   ? 56.556 -7.267  3.151   1.00 27.16 ?  355 HOH   B O    1 
HETATM 6928 O O    . HOH   F 4 .   ? 36.071 -8.568  -9.713  1.00 35.73 ?  356 HOH   B O    1 
HETATM 6929 O O    . HOH   F 4 .   ? 34.617 -10.320 7.566   1.00 24.79 ?  357 HOH   B O    1 
HETATM 6930 O O    . HOH   F 4 .   ? 43.197 -12.692 -21.166 1.00 40.95 ?  358 HOH   B O    1 
HETATM 6931 O O    . HOH   F 4 .   ? 61.487 -19.909 1.641   1.00 36.10 ?  359 HOH   B O    1 
HETATM 6932 O O    . HOH   F 4 .   ? 34.110 -7.734  11.429  1.00 39.78 ?  360 HOH   B O    1 
HETATM 6933 O O    . HOH   F 4 .   ? 56.918 -21.533 -16.350 1.00 42.83 ?  361 HOH   B O    1 
HETATM 6934 O O    . HOH   F 4 .   ? 40.238 -8.861  9.930   1.00 40.10 ?  362 HOH   B O    1 
HETATM 6935 O O    . HOH   F 4 .   ? 27.150 -25.977 -11.428 1.00 33.87 ?  363 HOH   B O    1 
HETATM 6936 O O    . HOH   F 4 .   ? 54.174 -5.724  3.063   1.00 36.61 ?  364 HOH   B O    1 
HETATM 6937 O O    . HOH   F 4 .   ? 32.498 -23.638 14.125  1.00 39.39 ?  365 HOH   B O    1 
HETATM 6938 O O    . HOH   F 4 .   ? 40.112 -11.352 -13.939 1.00 32.22 ?  366 HOH   B O    1 
HETATM 6939 O O    . HOH   F 4 .   ? 58.911 -10.393 9.263   1.00 37.22 ?  367 HOH   B O    1 
HETATM 6940 O O    . HOH   F 4 .   ? 48.368 -26.558 8.840   1.00 40.40 ?  368 HOH   B O    1 
HETATM 6941 O O    . HOH   F 4 .   ? 41.828 -10.068 -17.421 1.00 53.77 ?  369 HOH   B O    1 
HETATM 6942 O O    . HOH   F 4 .   ? 39.848 -7.042  7.862   1.00 41.71 ?  370 HOH   B O    1 
HETATM 6943 O O    . HOH   F 4 .   ? 36.163 -8.694  8.989   1.00 39.09 ?  371 HOH   B O    1 
HETATM 6944 O O    . HOH   F 4 .   ? 56.079 -7.799  -0.579  1.00 36.46 ?  372 HOH   B O    1 
HETATM 6945 O O    . HOH   F 4 .   ? 52.045 -12.902 13.376  1.00 32.02 ?  373 HOH   B O    1 
HETATM 6946 O O    . HOH   F 4 .   ? 38.019 -10.630 10.117  1.00 31.10 ?  374 HOH   B O    1 
HETATM 6947 O O    . HOH   F 4 .   ? 63.024 -12.372 6.972   1.00 37.43 ?  375 HOH   B O    1 
HETATM 6948 O O    . HOH   F 4 .   ? 41.800 -6.711  -4.839  1.00 45.81 ?  376 HOH   B O    1 
HETATM 6949 O O    . HOH   F 4 .   ? 36.473 -22.831 13.302  1.00 26.04 ?  377 HOH   B O    1 
HETATM 6950 O O    . HOH   F 4 .   ? 44.078 -5.576  -3.535  1.00 44.12 ?  378 HOH   B O    1 
HETATM 6951 O O    . HOH   F 4 .   ? 42.690 -17.194 -23.172 1.00 45.47 ?  379 HOH   B O    1 
HETATM 6952 O O    . HOH   F 4 .   ? 40.081 -7.629  3.264   1.00 36.06 ?  380 HOH   B O    1 
HETATM 6953 O O    . HOH   F 4 .   ? 39.673 -14.079 15.711  1.00 50.78 ?  381 HOH   B O    1 
HETATM 6954 O O    . HOH   F 4 .   ? 52.837 -29.897 7.205   1.00 24.05 ?  382 HOH   B O    1 
HETATM 6955 O O    . HOH   F 4 .   ? 60.481 -22.212 2.854   1.00 48.41 ?  383 HOH   B O    1 
HETATM 6956 O O    . HOH   F 4 .   ? 40.970 -9.855  15.819  1.00 43.35 ?  384 HOH   B O    1 
HETATM 6957 O O    . HOH   F 4 .   ? 46.784 -5.391  2.921   1.00 41.06 ?  385 HOH   B O    1 
HETATM 6958 O O    . HOH   F 4 .   ? 25.799 -18.835 -11.897 1.00 38.27 ?  386 HOH   B O    1 
HETATM 6959 O O    . HOH   F 4 .   ? 23.894 -20.839 -7.676  1.00 27.45 ?  387 HOH   B O    1 
HETATM 6960 O O    . HOH   F 4 .   ? 35.317 -20.329 13.364  1.00 30.56 ?  388 HOH   B O    1 
HETATM 6961 O O    . HOH   F 4 .   ? 35.359 -33.730 7.326   1.00 40.17 ?  389 HOH   B O    1 
HETATM 6962 O O    . HOH   F 4 .   ? 40.701 -6.637  -0.844  1.00 25.34 ?  390 HOH   B O    1 
HETATM 6963 O O    . HOH   F 4 .   ? 44.059 -31.837 -3.864  1.00 32.65 ?  391 HOH   B O    1 
HETATM 6964 O O    . HOH   F 4 .   ? 26.643 -28.014 -13.527 1.00 36.84 ?  392 HOH   B O    1 
HETATM 6965 O O    . HOH   F 4 .   ? 27.896 -27.101 2.181   1.00 30.46 ?  393 HOH   B O    1 
HETATM 6966 O O    . HOH   F 4 .   ? 24.618 -20.645 -10.509 1.00 38.06 ?  394 HOH   B O    1 
HETATM 6967 O O    . HOH   F 4 .   ? 50.622 -30.807 8.723   1.00 29.12 ?  395 HOH   B O    1 
HETATM 6968 O O    . HOH   F 4 .   ? 34.374 -33.495 9.637   1.00 35.51 ?  396 HOH   B O    1 
HETATM 6969 O O    . HOH   F 4 .   ? 26.854 -30.685 -12.642 1.00 28.81 ?  397 HOH   B O    1 
HETATM 6970 O O    . HOH   F 4 .   ? 45.753 -20.281 15.202  1.00 52.73 ?  398 HOH   B O    1 
HETATM 6971 O O    . HOH   F 4 .   ? 57.662 -6.515  -2.346  1.00 34.67 ?  399 HOH   B O    1 
HETATM 6972 O O    . HOH   F 4 .   ? 40.964 -11.789 -22.336 1.00 39.58 ?  400 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . VAL   A 3   ? 0.6681 0.6806 0.7492 0.0001  -0.0387 0.1107  3   VAL   A N   
2    C CA  . VAL   A 3   ? 0.6642 0.6768 0.7338 -0.0022 -0.0384 0.1106  3   VAL   A CA  
3    C C   . VAL   A 3   ? 0.6427 0.6606 0.6872 -0.0150 -0.0410 0.1180  3   VAL   A C   
4    O O   . VAL   A 3   ? 0.6463 0.6637 0.7040 -0.0131 -0.0438 0.1223  3   VAL   A O   
5    C CB  . VAL   A 3   ? 0.6777 0.6864 0.7519 0.0054  -0.0343 0.1044  3   VAL   A CB  
6    C CG1 . VAL   A 3   ? 0.6822 0.6894 0.7558 0.0080  -0.0328 0.1024  3   VAL   A CG1 
7    C CG2 . VAL   A 3   ? 0.6820 0.6894 0.7571 0.0082  -0.0321 0.1024  3   VAL   A CG2 
16   N N   . ASN   A 4   ? 0.6133 0.6378 0.6090 -0.0307 -0.0396 0.1223  4   ASN   A N   
17   C CA  . ASN   A 4   ? 0.5819 0.6126 0.5210 -0.0485 -0.0371 0.1230  4   ASN   A CA  
18   C C   . ASN   A 4   ? 0.5384 0.5850 0.4629 -0.0631 -0.0258 0.0946  4   ASN   A C   
19   O O   . ASN   A 4   ? 0.5402 0.5868 0.4523 -0.0637 -0.0281 0.1001  4   ASN   A O   
20   C CB  . ASN   A 4   ? 0.5903 0.6126 0.4834 -0.0525 -0.0460 0.1500  4   ASN   A CB  
21   C CG  . ASN   A 4   ? 0.5956 0.6100 0.4445 -0.0567 -0.0536 0.1770  4   ASN   A CG  
22   O OD1 . ASN   A 4   ? 0.5992 0.6081 0.4267 -0.0580 -0.0582 0.1867  4   ASN   A OD1 
23   N ND2 . ASN   A 4   ? 0.5958 0.6087 0.4328 -0.0577 -0.0555 0.1904  4   ASN   A ND2 
30   N N   . SER   A 5   ? 0.4907 0.5519 0.4130 -0.0785 -0.0145 0.0596  5   SER   A N   
31   C CA  . SER   A 5   ? 0.4411 0.5178 0.3686 -0.0920 -0.0009 0.0251  5   SER   A CA  
32   C C   . SER   A 5   ? 0.3893 0.4738 0.3114 -0.0984 0.0134  -0.0008 5   SER   A C   
33   O O   . SER   A 5   ? 0.3930 0.4822 0.3066 -0.0890 0.0135  -0.0205 5   SER   A O   
34   C CB  . SER   A 5   ? 0.4464 0.5272 0.3926 -0.0968 0.0012  0.0168  5   SER   A CB  
35   O OG  . SER   A 5   ? 0.4502 0.5325 0.4053 -0.0999 0.0030  0.0105  5   SER   A OG  
41   N N   . PHE   A 6   ? 0.3300 0.4184 0.2503 -0.1135 0.0308  -0.0014 6   PHE   A N   
42   C CA  . PHE   A 6   ? 0.2813 0.3645 0.2026 -0.1151 0.0421  0.0136  6   PHE   A CA  
43   C C   . PHE   A 6   ? 0.2761 0.3564 0.2212 -0.1116 0.0606  0.0141  6   PHE   A C   
44   O O   . PHE   A 6   ? 0.2857 0.3708 0.2660 -0.1132 0.0590  0.0313  6   PHE   A O   
45   C CB  . PHE   A 6   ? 0.2617 0.3272 0.1873 -0.0977 0.0248  0.0283  6   PHE   A CB  
46   C CG  . PHE   A 6   ? 0.2454 0.3015 0.1826 -0.0798 0.0131  0.0335  6   PHE   A CG  
47   C CD1 . PHE   A 6   ? 0.2352 0.2900 0.1852 -0.0694 0.0115  0.0428  6   PHE   A CD1 
48   C CD2 . PHE   A 6   ? 0.2515 0.2928 0.2072 -0.0646 0.0141  0.0376  6   PHE   A CD2 
49   C CE1 . PHE   A 6   ? 0.2337 0.2821 0.2000 -0.0664 0.0122  0.0417  6   PHE   A CE1 
50   C CE2 . PHE   A 6   ? 0.2481 0.2870 0.2207 -0.0591 0.0089  0.0259  6   PHE   A CE2 
51   C CZ  . PHE   A 6   ? 0.2383 0.2824 0.2102 -0.0635 0.0030  0.0254  6   PHE   A CZ  
61   N N   A SER   A 7   ? 0.2655 0.3467 0.2147 -0.1136 0.0646  -0.0008 7   SER   A N   
62   N N   B SER   A 7   ? 0.2686 0.3380 0.2272 -0.1044 0.0626  -0.0005 7   SER   A N   
63   C CA  A SER   A 7   ? 0.2660 0.3409 0.2261 -0.1009 0.0585  -0.0240 7   SER   A CA  
64   C CA  B SER   A 7   ? 0.2660 0.3196 0.2370 -0.0923 0.0597  -0.0163 7   SER   A CA  
65   C C   A SER   A 7   ? 0.2493 0.3077 0.1843 -0.0898 0.0656  -0.0202 7   SER   A C   
66   C C   B SER   A 7   ? 0.2570 0.2983 0.2238 -0.0769 0.0669  -0.0096 7   SER   A C   
67   O O   A SER   A 7   ? 0.2620 0.3017 0.1812 -0.0943 0.0711  -0.0167 7   SER   A O   
68   O O   B SER   A 7   ? 0.2600 0.2976 0.2236 -0.0778 0.0683  -0.0121 7   SER   A O   
69   C CB  A SER   A 7   ? 0.2858 0.3680 0.2738 -0.0891 0.0626  -0.0272 7   SER   A CB  
70   C CB  B SER   A 7   ? 0.2703 0.3209 0.2502 -0.0963 0.0563  -0.0276 7   SER   A CB  
71   O OG  A SER   A 7   ? 0.3032 0.3839 0.3169 -0.0824 0.0598  -0.0266 7   SER   A OG  
72   O OG  B SER   A 7   ? 0.2737 0.3204 0.2656 -0.0997 0.0553  -0.0315 7   SER   A OG  
83   N N   A GLY   A 8   ? 0.2216 0.2799 0.1744 -0.0741 0.0624  -0.0274 8   GLY   A N   
84   N N   B GLY   A 8   ? 0.2441 0.2773 0.2121 -0.0636 0.0702  -0.0042 8   GLY   A N   
85   C CA  A GLY   A 8   ? 0.2079 0.2500 0.1860 -0.0511 0.0542  -0.0133 8   GLY   A CA  
86   C CA  B GLY   A 8   ? 0.2317 0.2529 0.2047 -0.0534 0.0591  0.0018  8   GLY   A CA  
87   C C   A GLY   A 8   ? 0.1858 0.2265 0.1888 -0.0353 0.0410  -0.0042 8   GLY   A C   
88   C C   B GLY   A 8   ? 0.2136 0.2305 0.1825 -0.0460 0.0479  0.0056  8   GLY   A C   
89   O O   A GLY   A 8   ? 0.1927 0.2242 0.1986 -0.0163 0.0386  -0.0141 8   GLY   A O   
90   O O   B GLY   A 8   ? 0.2174 0.2280 0.1846 -0.0418 0.0536  0.0077  8   GLY   A O   
97   N N   A TYR   A 9   ? 0.1615 0.2098 0.1803 -0.0321 0.0352  -0.0012 9   TYR   A N   
98   N N   B TYR   A 9   ? 0.1931 0.2139 0.1749 -0.0388 0.0263  0.0115  9   TYR   A N   
99   C CA  A TYR   A 9   ? 0.1514 0.1931 0.1580 -0.0355 0.0215  0.0019  9   TYR   A CA  
100  C CA  B TYR   A 9   ? 0.1795 0.1974 0.1677 -0.0316 0.0165  0.0175  9   TYR   A CA  
101  C C   A TYR   A 9   ? 0.1495 0.1784 0.1522 -0.0284 0.0275  0.0280  9   TYR   A C   
102  C C   B TYR   A 9   ? 0.1751 0.1903 0.1665 -0.0276 0.0107  0.0175  9   TYR   A C   
103  O O   A TYR   A 9   ? 0.1727 0.1989 0.1771 -0.0313 0.0074  0.0334  9   TYR   A O   
104  O O   B TYR   A 9   ? 0.1821 0.2025 0.1895 -0.0319 0.0039  0.0251  9   TYR   A O   
105  C CB  A TYR   A 9   ? 0.1439 0.2019 0.1622 -0.0315 0.0218  -0.0056 9   TYR   A CB  
106  C CB  B TYR   A 9   ? 0.1697 0.1958 0.1725 -0.0271 0.0127  0.0173  9   TYR   A CB  
107  C CG  A TYR   A 9   ? 0.1537 0.2086 0.1840 -0.0214 0.0300  -0.0137 9   TYR   A CG  
108  C CG  B TYR   A 9   ? 0.1636 0.1943 0.1739 -0.0200 0.0134  0.0189  9   TYR   A CG  
109  C CD1 A TYR   A 9   ? 0.1583 0.2054 0.1935 -0.0326 0.0406  -0.0125 9   TYR   A CD1 
110  C CD1 B TYR   A 9   ? 0.1638 0.1919 0.1796 -0.0179 0.0179  0.0182  9   TYR   A CD1 
111  C CD2 A TYR   A 9   ? 0.1520 0.2090 0.2034 -0.0126 0.0269  0.0018  9   TYR   A CD2 
112  C CD2 B TYR   A 9   ? 0.1576 0.1901 0.1635 -0.0144 0.0111  0.0245  9   TYR   A CD2 
113  C CE1 A TYR   A 9   ? 0.1630 0.2116 0.2126 -0.0259 0.0446  -0.0177 9   TYR   A CE1 
114  C CE1 B TYR   A 9   ? 0.1576 0.1855 0.1722 -0.0176 0.0209  0.0187  9   TYR   A CE1 
115  C CE2 A TYR   A 9   ? 0.1571 0.2131 0.2072 -0.0147 0.0287  -0.0053 9   TYR   A CE2 
116  C CE2 B TYR   A 9   ? 0.1541 0.1870 0.1546 -0.0120 0.0199  0.0210  9   TYR   A CE2 
117  C CZ  A TYR   A 9   ? 0.1582 0.2151 0.2199 -0.0307 0.0457  -0.0085 9   TYR   A CZ  
118  C CZ  B TYR   A 9   ? 0.1485 0.1810 0.1671 -0.0139 0.0304  0.0169  9   TYR   A CZ  
119  O OH  A TYR   A 9   ? 0.1743 0.2225 0.2582 -0.0379 0.0414  -0.0039 9   TYR   A OH  
120  O OH  B TYR   A 9   ? 0.1390 0.1771 0.1859 -0.0164 0.0401  0.0215  9   TYR   A OH  
139  N N   A LEU   A 10  ? 0.1497 0.1596 0.1485 -0.0281 0.0171  0.0175  10  LEU   A N   
140  N N   B LEU   A 10  ? 0.1725 0.1781 0.1553 -0.0219 0.0065  0.0079  10  LEU   A N   
141  C CA  A LEU   A 10  ? 0.1429 0.1565 0.1481 -0.0243 0.0154  0.0308  10  LEU   A CA  
142  C CA  B LEU   A 10  ? 0.1730 0.1727 0.1671 -0.0195 0.0097  0.0029  10  LEU   A CA  
143  C C   A LEU   A 10  ? 0.1399 0.1507 0.1658 -0.0230 0.0190  0.0324  10  LEU   A C   
144  C C   B LEU   A 10  ? 0.1662 0.1620 0.1554 -0.0199 0.0024  0.0116  10  LEU   A C   
145  O O   A LEU   A 10  ? 0.1422 0.1454 0.1911 -0.0188 0.0362  0.0397  10  LEU   A O   
146  O O   B LEU   A 10  ? 0.1645 0.1588 0.1631 -0.0190 0.0072  0.0268  10  LEU   A O   
147  C CB  A LEU   A 10  ? 0.1441 0.1593 0.1624 -0.0156 0.0067  0.0355  10  LEU   A CB  
148  C CB  B LEU   A 10  ? 0.1766 0.1736 0.1814 -0.0193 0.0062  0.0052  10  LEU   A CB  
149  C CG  A LEU   A 10  ? 0.1728 0.1712 0.2299 -0.0015 -0.0240 0.0382  10  LEU   A CG  
150  C CG  B LEU   A 10  ? 0.1845 0.1809 0.2046 -0.0103 -0.0012 0.0053  10  LEU   A CG  
151  C CD1 A LEU   A 10  ? 0.1971 0.1795 0.2595 -0.0156 -0.0134 0.0373  10  LEU   A CD1 
152  C CD1 B LEU   A 10  ? 0.1904 0.1847 0.2258 -0.0163 0.0015  0.0089  10  LEU   A CD1 
153  C CD2 A LEU   A 10  ? 0.1886 0.1941 0.2507 0.0087  -0.0068 0.0225  10  LEU   A CD2 
154  C CD2 B LEU   A 10  ? 0.1952 0.1894 0.2230 -0.0010 -0.0131 -0.0019 10  LEU   A CD2 
177  N N   A LYS   A 11  ? 0.1457 0.1494 0.1554 -0.0267 0.0148  0.0314  11  LYS   A N   
178  N N   B LYS   A 11  ? 0.1662 0.1545 0.1420 -0.0263 -0.0052 0.0118  11  LYS   A N   
179  C CA  A LYS   A 11  ? 0.1462 0.1463 0.1733 -0.0357 0.0129  0.0285  11  LYS   A CA  
180  C CA  B LYS   A 11  ? 0.1652 0.1462 0.1463 -0.0245 -0.0015 0.0174  11  LYS   A CA  
181  C C   A LYS   A 11  ? 0.1437 0.1529 0.1712 -0.0280 0.0164  0.0166  11  LYS   A C   
182  C C   B LYS   A 11  ? 0.1495 0.1262 0.1454 -0.0257 0.0089  0.0115  11  LYS   A C   
183  O O   A LYS   A 11  ? 0.1549 0.1828 0.2048 -0.0553 0.0248  -0.0031 11  LYS   A O   
184  O O   B LYS   A 11  ? 0.1469 0.1119 0.1621 -0.0225 0.0180  -0.0190 11  LYS   A O   
185  C CB  A LYS   A 11  ? 0.1554 0.1474 0.1826 -0.0342 0.0142  0.0183  11  LYS   A CB  
186  C CB  B LYS   A 11  ? 0.1759 0.1453 0.1459 -0.0243 -0.0033 0.0111  11  LYS   A CB  
187  C CG  A LYS   A 11  ? 0.1712 0.1514 0.1873 -0.0248 0.0133  0.0285  11  LYS   A CG  
188  C CG  B LYS   A 11  ? 0.1852 0.1474 0.1470 -0.0212 -0.0035 0.0209  11  LYS   A CG  
189  C CD  A LYS   A 11  ? 0.1855 0.1563 0.1919 -0.0246 0.0053  0.0353  11  LYS   A CD  
190  C CD  B LYS   A 11  ? 0.1922 0.1526 0.1555 -0.0185 -0.0016 0.0277  11  LYS   A CD  
191  C CE  A LYS   A 11  ? 0.1988 0.1541 0.1923 -0.0213 0.0039  0.0376  11  LYS   A CE  
192  C CE  B LYS   A 11  ? 0.1971 0.1527 0.1576 -0.0161 0.0013  0.0339  11  LYS   A CE  
193  N NZ  A LYS   A 11  ? 0.1974 0.1553 0.2011 -0.0130 -0.0047 0.0339  11  LYS   A NZ  
194  N NZ  B LYS   A 11  ? 0.1968 0.1540 0.1571 -0.0131 0.0041  0.0389  11  LYS   A NZ  
221  N N   A LEU   A 12  ? 0.1375 0.1400 0.1574 -0.0218 0.0145  0.0197  12  LEU   A N   
222  N N   B LEU   A 12  ? 0.1368 0.1328 0.1531 -0.0136 0.0043  0.0073  12  LEU   A N   
223  C CA  A LEU   A 12  ? 0.1422 0.1497 0.1480 -0.0184 0.0106  0.0275  12  LEU   A CA  
224  C CA  B LEU   A 12  ? 0.1324 0.1405 0.1473 -0.0076 0.0115  0.0047  12  LEU   A CA  
225  C C   A LEU   A 12  ? 0.1439 0.1461 0.1620 -0.0259 0.0143  0.0291  12  LEU   A C   
226  C C   B LEU   A 12  ? 0.1286 0.1454 0.1476 -0.0128 0.0192  0.0029  12  LEU   A C   
227  O O   A LEU   A 12  ? 0.1543 0.1457 0.1768 -0.0193 0.0101  0.0107  12  LEU   A O   
228  O O   B LEU   A 12  ? 0.1320 0.1485 0.1488 -0.0068 0.0160  0.0051  12  LEU   A O   
229  C CB  A LEU   A 12  ? 0.1520 0.1495 0.1481 -0.0183 0.0056  0.0191  12  LEU   A CB  
230  C CB  B LEU   A 12  ? 0.1426 0.1447 0.1555 -0.0025 0.0126  0.0019  12  LEU   A CB  
231  C CG  A LEU   A 12  ? 0.1586 0.1540 0.1705 -0.0086 0.0194  0.0183  12  LEU   A CG  
232  C CG  B LEU   A 12  ? 0.1490 0.1461 0.1615 0.0016  0.0134  -0.0006 12  LEU   A CG  
233  C CD1 A LEU   A 12  ? 0.1726 0.1522 0.1736 0.0080  0.0254  0.0283  12  LEU   A CD1 
234  C CD1 B LEU   A 12  ? 0.1507 0.1495 0.1714 0.0059  0.0247  -0.0044 12  LEU   A CD1 
235  C CD2 A LEU   A 12  ? 0.1612 0.1715 0.2000 -0.0109 0.0155  0.0145  12  LEU   A CD2 
236  C CD2 B LEU   A 12  ? 0.1461 0.1448 0.1508 0.0029  0.0067  -0.0086 12  LEU   A CD2 
259  N N   A THR   A 13  ? 0.1427 0.1396 0.1842 -0.0223 0.0074  0.0204  13  THR   A N   
260  N N   B THR   A 13  ? 0.1289 0.1442 0.1552 -0.0218 0.0113  -0.0003 13  THR   A N   
261  C CA  A THR   A 13  ? 0.1454 0.1426 0.1969 -0.0146 0.0185  0.0198  13  THR   A CA  
262  C CA  B THR   A 13  ? 0.1342 0.1494 0.1604 -0.0240 0.0128  0.0016  13  THR   A CA  
263  C C   A THR   A 13  ? 0.1440 0.1428 0.2030 -0.0211 0.0102  0.0361  13  THR   A C   
264  C C   B THR   A 13  ? 0.1416 0.1593 0.1656 -0.0285 0.0134  0.0074  13  THR   A C   
265  O O   A THR   A 13  ? 0.1469 0.1469 0.1959 -0.0154 0.0093  0.0310  13  THR   A O   
266  O O   B THR   A 13  ? 0.1481 0.1671 0.1662 -0.0355 0.0063  0.0163  13  THR   A O   
267  C CB  A THR   A 13  ? 0.1465 0.1576 0.2099 -0.0130 0.0193  0.0282  13  THR   A CB  
268  C CB  B THR   A 13  ? 0.1309 0.1560 0.1592 -0.0155 0.0165  0.0071  13  THR   A CB  
269  O OG1 A THR   A 13  ? 0.1484 0.1532 0.2253 -0.0053 0.0080  0.0336  13  THR   A OG1 
270  O OG1 B THR   A 13  ? 0.1240 0.1586 0.1632 -0.0177 0.0334  0.0125  13  THR   A OG1 
271  C CG2 A THR   A 13  ? 0.1534 0.1728 0.2330 -0.0060 0.0297  0.0194  13  THR   A CG2 
272  C CG2 B THR   A 13  ? 0.1340 0.1643 0.1709 -0.0109 0.0145  0.0068  13  THR   A CG2 
287  N N   A ASP   A 14  ? 0.1511 0.1438 0.2244 -0.0233 0.0058  0.0525  14  ASP   A N   
288  N N   B ASP   A 14  ? 0.1455 0.1618 0.1785 -0.0253 0.0080  0.0073  14  ASP   A N   
289  C CA  A ASP   A 14  ? 0.1509 0.1597 0.2415 -0.0234 -0.0010 0.0703  14  ASP   A CA  
290  C CA  B ASP   A 14  ? 0.1489 0.1711 0.1961 -0.0159 -0.0003 0.0229  14  ASP   A CA  
291  C C   A ASP   A 14  ? 0.1438 0.1694 0.2203 -0.0236 -0.0119 0.0648  14  ASP   A C   
292  C C   B ASP   A 14  ? 0.1411 0.1676 0.1882 -0.0104 -0.0095 0.0382  14  ASP   A C   
293  O O   A ASP   A 14  ? 0.1579 0.1757 0.2319 -0.0344 -0.0128 0.0659  14  ASP   A O   
294  O O   B ASP   A 14  ? 0.1402 0.1705 0.1755 0.0003  -0.0165 0.0345  14  ASP   A O   
295  C CB  A ASP   A 14  ? 0.1605 0.1828 0.3102 -0.0289 -0.0016 0.0851  14  ASP   A CB  
296  C CB  B ASP   A 14  ? 0.1591 0.1874 0.2342 -0.0129 -0.0045 0.0271  14  ASP   A CB  
297  C CG  A ASP   A 14  ? 0.1812 0.2308 0.3989 -0.0307 -0.0045 0.0800  14  ASP   A CG  
298  C CG  B ASP   A 14  ? 0.1632 0.2055 0.2675 -0.0181 -0.0023 0.0290  14  ASP   A CG  
299  O OD1 A ASP   A 14  ? 0.1937 0.2535 0.4227 -0.0154 -0.0266 0.0812  14  ASP   A OD1 
300  O OD1 B ASP   A 14  ? 0.1642 0.2101 0.2733 -0.0187 0.0041  0.0328  14  ASP   A OD1 
301  O OD2 A ASP   A 14  ? 0.2036 0.2563 0.4398 -0.0411 -0.0172 0.0636  14  ASP   A OD2 
302  O OD2 B ASP   A 14  ? 0.1663 0.2171 0.2872 -0.0251 -0.0105 0.0288  14  ASP   A OD2 
311  N N   . ASN   A 15  ? 0.1382 0.1584 0.2054 -0.0205 0.0001  0.0568  15  ASN   A N   
312  C CA  . ASN   A 15  ? 0.1390 0.1624 0.2193 -0.0202 -0.0058 0.0483  15  ASN   A CA  
313  C C   . ASN   A 15  ? 0.1372 0.1609 0.2333 -0.0189 0.0032  0.0462  15  ASN   A C   
314  O O   . ASN   A 15  ? 0.1450 0.1622 0.2745 -0.0263 -0.0216 0.0452  15  ASN   A O   
315  C CB  . ASN   A 15  ? 0.1337 0.1660 0.2082 -0.0121 -0.0054 0.0425  15  ASN   A CB  
316  C CG  . ASN   A 15  ? 0.1366 0.1664 0.2108 -0.0150 0.0056  0.0304  15  ASN   A CG  
317  O OD1 . ASN   A 15  ? 0.1525 0.1657 0.2399 -0.0249 0.0013  0.0350  15  ASN   A OD1 
318  N ND2 . ASN   A 15  ? 0.1397 0.1827 0.1985 -0.0162 0.0146  0.0289  15  ASN   A ND2 
326  N N   . VAL   A 16  ? 0.1346 0.1559 0.2184 -0.0165 0.0037  0.0414  16  VAL   A N   
327  C CA  . VAL   A 16  ? 0.1366 0.1604 0.1990 -0.0115 0.0051  0.0461  16  VAL   A CA  
328  C C   . VAL   A 16  ? 0.1331 0.1598 0.1837 -0.0147 0.0046  0.0329  16  VAL   A C   
329  O O   . VAL   A 16  ? 0.1278 0.1553 0.2095 -0.0184 0.0135  0.0314  16  VAL   A O   
330  C CB  . VAL   A 16  ? 0.1504 0.1707 0.1986 -0.0014 0.0251  0.0427  16  VAL   A CB  
331  C CG1 . VAL   A 16  ? 0.1693 0.1811 0.2048 0.0059  0.0208  0.0529  16  VAL   A CG1 
332  C CG2 . VAL   A 16  ? 0.1611 0.1773 0.2094 0.0029  0.0316  0.0398  16  VAL   A CG2 
342  N N   A TYR   A 17  ? 0.1359 0.1472 0.1874 -0.0134 0.0079  0.0300  17  TYR   A N   
343  N N   B TYR   A 17  ? 0.1337 0.1606 0.1739 -0.0126 0.0067  0.0306  17  TYR   A N   
344  C CA  A TYR   A 17  ? 0.1410 0.1452 0.1862 -0.0193 0.0053  0.0388  17  TYR   A CA  
345  C CA  B TYR   A 17  ? 0.1339 0.1651 0.1632 -0.0137 0.0087  0.0336  17  TYR   A CA  
346  C C   A TYR   A 17  ? 0.1393 0.1488 0.1919 -0.0136 0.0058  0.0405  17  TYR   A C   
347  C C   B TYR   A 17  ? 0.1286 0.1684 0.1526 -0.0227 0.0119  0.0367  17  TYR   A C   
348  O O   A TYR   A 17  ? 0.1390 0.1485 0.2058 -0.0119 0.0192  0.0458  17  TYR   A O   
349  O O   B TYR   A 17  ? 0.1254 0.1718 0.1568 -0.0257 0.0127  0.0510  17  TYR   A O   
350  C CB  A TYR   A 17  ? 0.1586 0.1445 0.2012 -0.0348 -0.0024 0.0433  17  TYR   A CB  
351  C CB  B TYR   A 17  ? 0.1427 0.1687 0.1710 -0.0080 0.0074  0.0330  17  TYR   A CB  
352  C CG  A TYR   A 17  ? 0.1855 0.1572 0.1943 -0.0426 -0.0171 0.0292  17  TYR   A CG  
353  C CG  B TYR   A 17  ? 0.1560 0.1762 0.1701 -0.0011 0.0032  0.0309  17  TYR   A CG  
354  C CD1 A TYR   A 17  ? 0.2040 0.1657 0.2131 -0.0278 -0.0242 0.0334  17  TYR   A CD1 
355  C CD1 B TYR   A 17  ? 0.1642 0.1778 0.1800 0.0104  0.0005  0.0386  17  TYR   A CD1 
356  C CD2 A TYR   A 17  ? 0.2023 0.1683 0.1929 -0.0566 -0.0196 0.0402  17  TYR   A CD2 
357  C CD2 B TYR   A 17  ? 0.1642 0.1836 0.1751 -0.0038 -0.0024 0.0328  17  TYR   A CD2 
358  C CE1 A TYR   A 17  ? 0.2143 0.1705 0.2165 -0.0384 -0.0378 0.0337  17  TYR   A CE1 
359  C CE1 B TYR   A 17  ? 0.1708 0.1826 0.1903 0.0108  -0.0051 0.0458  17  TYR   A CE1 
360  C CE2 A TYR   A 17  ? 0.2177 0.1716 0.1970 -0.0555 -0.0406 0.0341  17  TYR   A CE2 
361  C CE2 B TYR   A 17  ? 0.1704 0.1860 0.1828 0.0020  -0.0080 0.0383  17  TYR   A CE2 
362  C CZ  A TYR   A 17  ? 0.2280 0.1682 0.1987 -0.0494 -0.0486 0.0400  17  TYR   A CZ  
363  C CZ  B TYR   A 17  ? 0.1735 0.1853 0.1853 0.0083  -0.0166 0.0513  17  TYR   A CZ  
364  O OH  A TYR   A 17  ? 0.2494 0.1691 0.1963 -0.0471 -0.0452 0.0341  17  TYR   A OH  
365  O OH  B TYR   A 17  ? 0.1747 0.1882 0.1937 0.0147  -0.0213 0.0603  17  TYR   A OH  
384  N N   A ILE   A 18  ? 0.1419 0.1513 0.1824 -0.0177 0.0058  0.0472  18  ILE   A N   
385  N N   B ILE   A 18  ? 0.1252 0.1666 0.1421 -0.0308 0.0183  0.0265  18  ILE   A N   
386  C CA  A ILE   A 18  ? 0.1457 0.1429 0.1695 -0.0111 0.0103  0.0330  18  ILE   A CA  
387  C CA  B ILE   A 18  ? 0.1219 0.1629 0.1343 -0.0253 0.0257  0.0171  18  ILE   A CA  
388  C C   A ILE   A 18  ? 0.1449 0.1512 0.1753 -0.0215 0.0070  0.0326  18  ILE   A C   
389  C C   B ILE   A 18  ? 0.1187 0.1650 0.1185 -0.0273 0.0083  0.0125  18  ILE   A C   
390  O O   A ILE   A 18  ? 0.1410 0.1697 0.1681 -0.0302 0.0191  0.0372  18  ILE   A O   
391  O O   B ILE   A 18  ? 0.1188 0.1708 0.1312 -0.0328 0.0105  0.0120  18  ILE   A O   
392  C CB  A ILE   A 18  ? 0.1576 0.1361 0.1642 0.0009  0.0128  0.0342  18  ILE   A CB  
393  C CB  B ILE   A 18  ? 0.1255 0.1583 0.1289 -0.0182 0.0440  0.0185  18  ILE   A CB  
394  C CG1 A ILE   A 18  ? 0.1640 0.1440 0.1507 0.0117  0.0088  0.0246  18  ILE   A CG1 
395  C CG1 B ILE   A 18  ? 0.1409 0.1632 0.1489 -0.0185 0.0545  0.0167  18  ILE   A CG1 
396  C CG2 A ILE   A 18  ? 0.1646 0.1376 0.1553 0.0028  0.0112  0.0197  18  ILE   A CG2 
397  C CG2 B ILE   A 18  ? 0.1319 0.1654 0.1391 -0.0161 0.0440  0.0162  18  ILE   A CG2 
398  C CD1 A ILE   A 18  ? 0.1785 0.1613 0.1526 0.0311  0.0105  0.0246  18  ILE   A CD1 
399  C CD1 B ILE   A 18  ? 0.1534 0.1731 0.1729 -0.0156 0.0557  0.0058  18  ILE   A CD1 
422  N N   A LYS   A 19  ? 0.1514 0.1521 0.1723 -0.0126 0.0265  0.0275  19  LYS   A N   
423  N N   B LYS   A 19  ? 0.1252 0.1638 0.1066 -0.0174 0.0254  0.0059  19  LYS   A N   
424  C CA  A LYS   A 19  ? 0.1662 0.1636 0.1594 -0.0094 0.0296  0.0328  19  LYS   A CA  
425  C CA  B LYS   A 19  ? 0.1398 0.1755 0.1225 -0.0057 0.0326  -0.0099 19  LYS   A CA  
426  C C   A LYS   A 19  ? 0.1611 0.1550 0.1832 -0.0060 0.0339  0.0345  19  LYS   A C   
427  C C   B LYS   A 19  ? 0.1413 0.1728 0.1444 0.0039  0.0333  -0.0112 19  LYS   A C   
428  O O   A LYS   A 19  ? 0.1614 0.1530 0.1904 -0.0072 0.0349  0.0459  19  LYS   A O   
429  O O   B LYS   A 19  ? 0.1400 0.1685 0.1510 0.0011  0.0315  -0.0094 19  LYS   A O   
430  C CB  A LYS   A 19  ? 0.1937 0.1902 0.1726 -0.0144 0.0336  0.0232  19  LYS   A CB  
431  C CB  B LYS   A 19  ? 0.1524 0.1885 0.1344 -0.0055 0.0339  -0.0273 19  LYS   A CB  
432  C CG  A LYS   A 19  ? 0.2268 0.2081 0.1807 -0.0187 0.0383  0.0237  19  LYS   A CG  
433  C CG  B LYS   A 19  ? 0.1794 0.2022 0.1418 -0.0041 0.0368  -0.0330 19  LYS   A CG  
434  C CD  A LYS   A 19  ? 0.2558 0.2267 0.2052 -0.0221 0.0496  0.0089  19  LYS   A CD  
435  C CD  B LYS   A 19  ? 0.2050 0.2155 0.1593 -0.0042 0.0344  -0.0320 19  LYS   A CD  
436  C CE  A LYS   A 19  ? 0.2791 0.2365 0.2202 -0.0258 0.0568  -0.0023 19  LYS   A CE  
437  C CE  B LYS   A 19  ? 0.2231 0.2262 0.1736 -0.0095 0.0305  -0.0312 19  LYS   A CE  
438  N NZ  A LYS   A 19  ? 0.2883 0.2387 0.2173 -0.0316 0.0734  -0.0177 19  LYS   A NZ  
439  N NZ  B LYS   A 19  ? 0.2312 0.2301 0.1758 -0.0115 0.0365  -0.0365 19  LYS   A NZ  
466  N N   A ASN   A 20  ? 0.1610 0.1581 0.2082 -0.0101 0.0358  0.0458  20  ASN   A N   
467  N N   B ASN   A 20  ? 0.1470 0.1777 0.1705 0.0103  0.0345  -0.0163 20  ASN   A N   
468  C CA  A ASN   A 20  ? 0.1747 0.1667 0.2435 0.0040  0.0573  0.0453  20  ASN   A CA  
469  C CA  B ASN   A 20  ? 0.1511 0.1841 0.1983 0.0164  0.0341  -0.0133 20  ASN   A CA  
470  C C   A ASN   A 20  ? 0.1909 0.1691 0.2511 -0.0035 0.0731  0.0325  20  ASN   A C   
471  C C   B ASN   A 20  ? 0.1676 0.1813 0.2033 0.0152  0.0426  -0.0179 20  ASN   A C   
472  O O   A ASN   A 20  ? 0.2089 0.1734 0.2635 -0.0124 0.0717  0.0166  20  ASN   A O   
473  O O   B ASN   A 20  ? 0.1754 0.1789 0.2130 0.0248  0.0532  -0.0192 20  ASN   A O   
474  C CB  A ASN   A 20  ? 0.1834 0.1751 0.2733 0.0139  0.0621  0.0606  20  ASN   A CB  
475  C CB  B ASN   A 20  ? 0.1413 0.1905 0.2225 0.0220  0.0270  -0.0041 20  ASN   A CB  
476  C CG  A ASN   A 20  ? 0.2017 0.1818 0.3161 0.0267  0.0666  0.0582  20  ASN   A CG  
477  C CG  B ASN   A 20  ? 0.1359 0.1911 0.2495 0.0275  0.0243  -0.0017 20  ASN   A CG  
478  O OD1 A ASN   A 20  ? 0.2317 0.1984 0.3831 0.0308  0.0800  0.0522  20  ASN   A OD1 
479  O OD1 B ASN   A 20  ? 0.1357 0.1838 0.2790 0.0262  0.0363  -0.0166 20  ASN   A OD1 
480  N ND2 A ASN   A 20  ? 0.2092 0.1679 0.3116 0.0208  0.0521  0.0746  20  ASN   A ND2 
481  N ND2 B ASN   A 20  ? 0.1449 0.1960 0.2626 0.0250  0.0100  0.0190  20  ASN   A ND2 
494  N N   A ALA   A 21  ? 0.1922 0.1725 0.2497 -0.0016 0.0592  0.0241  21  ALA   A N   
495  N N   B ALA   A 21  ? 0.1748 0.1803 0.2055 0.0098  0.0294  -0.0187 21  ALA   A N   
496  C CA  A ALA   A 21  ? 0.1936 0.1769 0.2475 -0.0050 0.0585  0.0176  21  ALA   A CA  
497  C CA  B ALA   A 21  ? 0.1809 0.1775 0.2056 0.0020  0.0347  -0.0163 21  ALA   A CA  
498  C C   A ALA   A 21  ? 0.1806 0.1787 0.2494 -0.0051 0.0544  0.0275  21  ALA   A C   
499  C C   B ALA   A 21  ? 0.1763 0.1705 0.1979 -0.0035 0.0504  -0.0078 21  ALA   A C   
500  O O   A ALA   A 21  ? 0.1771 0.1779 0.2435 0.0081  0.0443  0.0402  21  ALA   A O   
501  O O   B ALA   A 21  ? 0.1756 0.1579 0.2063 0.0019  0.0528  -0.0120 21  ALA   A O   
502  C CB  A ALA   A 21  ? 0.2106 0.1797 0.2528 -0.0133 0.0607  0.0178  21  ALA   A CB  
503  C CB  B ALA   A 21  ? 0.1858 0.1777 0.2240 0.0057  0.0326  -0.0179 21  ALA   A CB  
514  N N   A ASP   A 22  ? 0.1849 0.1765 0.2654 -0.0099 0.0470  0.0302  22  ASP   A N   
515  N N   B ASP   A 22  ? 0.1792 0.1722 0.1929 -0.0104 0.0558  0.0072  22  ASP   A N   
516  C CA  A ASP   A 22  ? 0.1898 0.1744 0.2631 -0.0059 0.0424  0.0358  22  ASP   A CA  
517  C CA  B ASP   A 22  ? 0.1853 0.1710 0.1943 -0.0113 0.0529  0.0152  22  ASP   A CA  
518  C C   A ASP   A 22  ? 0.1783 0.1784 0.2224 -0.0070 0.0397  0.0332  22  ASP   A C   
519  C C   B ASP   A 22  ? 0.1747 0.1669 0.1728 -0.0227 0.0531  0.0162  22  ASP   A C   
520  O O   A ASP   A 22  ? 0.1794 0.1829 0.2349 -0.0077 0.0361  0.0241  22  ASP   A O   
521  O O   B ASP   A 22  ? 0.1751 0.1686 0.1753 -0.0271 0.0460  0.0113  22  ASP   A O   
522  C CB  A ASP   A 22  ? 0.2093 0.1783 0.3103 -0.0080 0.0314  0.0303  22  ASP   A CB  
523  C CB  B ASP   A 22  ? 0.2013 0.1738 0.2191 0.0001  0.0519  0.0072  22  ASP   A CB  
524  C CG  A ASP   A 22  ? 0.2263 0.1912 0.3594 -0.0111 0.0048  0.0355  22  ASP   A CG  
525  C CG  B ASP   A 22  ? 0.2122 0.1717 0.2332 0.0034  0.0533  0.0037  22  ASP   A CG  
526  O OD1 A ASP   A 22  ? 0.2184 0.1945 0.3868 -0.0304 -0.0103 0.0473  22  ASP   A OD1 
527  O OD1 B ASP   A 22  ? 0.2122 0.1542 0.2186 -0.0003 0.0537  -0.0091 22  ASP   A OD1 
528  O OD2 A ASP   A 22  ? 0.2514 0.2029 0.3932 -0.0002 0.0067  0.0212  22  ASP   A OD2 
529  O OD2 B ASP   A 22  ? 0.2205 0.1855 0.2574 0.0049  0.0605  0.0090  22  ASP   A OD2 
538  N N   A ILE   A 23  ? 0.1794 0.1808 0.1962 -0.0039 0.0364  0.0254  23  ILE   A N   
539  N N   B ILE   A 23  ? 0.1694 0.1666 0.1667 -0.0238 0.0433  0.0136  23  ILE   A N   
540  C CA  A ILE   A 23  ? 0.1750 0.1786 0.1801 -0.0029 0.0322  0.0210  23  ILE   A CA  
541  C CA  B ILE   A 23  ? 0.1623 0.1676 0.1538 -0.0274 0.0256  0.0141  23  ILE   A CA  
542  C C   A ILE   A 23  ? 0.1740 0.1841 0.1688 -0.0028 0.0468  0.0161  23  ILE   A C   
543  C C   B ILE   A 23  ? 0.1667 0.1770 0.1618 -0.0372 0.0266  0.0060  23  ILE   A C   
544  O O   A ILE   A 23  ? 0.1871 0.1942 0.1745 -0.0022 0.0355  -0.0016 23  ILE   A O   
545  O O   B ILE   A 23  ? 0.1655 0.1731 0.1629 -0.0356 0.0280  -0.0006 23  ILE   A O   
546  C CB  A ILE   A 23  ? 0.1830 0.1667 0.1665 0.0023  0.0239  0.0207  23  ILE   A CB  
547  C CB  B ILE   A 23  ? 0.1571 0.1649 0.1371 -0.0157 0.0180  0.0186  23  ILE   A CB  
548  C CG1 A ILE   A 23  ? 0.1851 0.1661 0.1598 0.0070  0.0145  0.0153  23  ILE   A CG1 
549  C CG1 B ILE   A 23  ? 0.1614 0.1667 0.1225 -0.0141 0.0090  0.0126  23  ILE   A CG1 
550  C CG2 A ILE   A 23  ? 0.1907 0.1705 0.1725 0.0046  0.0261  0.0337  23  ILE   A CG2 
551  C CG2 B ILE   A 23  ? 0.1522 0.1631 0.1342 -0.0030 0.0178  0.0168  23  ILE   A CG2 
552  C CD1 A ILE   A 23  ? 0.1860 0.1700 0.1540 0.0043  -0.0013 0.0044  23  ILE   A CD1 
553  C CD1 B ILE   A 23  ? 0.1581 0.1673 0.1223 -0.0101 0.0027  0.0071  23  ILE   A CD1 
576  N N   A VAL   A 24  ? 0.1803 0.1872 0.1813 -0.0101 0.0513  0.0121  24  VAL   A N   
577  N N   B VAL   A 24  ? 0.1800 0.1919 0.1908 -0.0439 0.0267  0.0075  24  VAL   A N   
578  C CA  A VAL   A 24  ? 0.1976 0.1962 0.2042 -0.0234 0.0482  -0.0065 24  VAL   A CA  
579  C CA  B VAL   A 24  ? 0.1974 0.2034 0.2054 -0.0440 0.0311  0.0080  24  VAL   A CA  
580  C C   A VAL   A 24  ? 0.2040 0.2118 0.2110 -0.0344 0.0367  -0.0133 24  VAL   A C   
581  C C   B VAL   A 24  ? 0.2049 0.2191 0.2106 -0.0435 0.0362  -0.0016 24  VAL   A C   
582  O O   A VAL   A 24  ? 0.2150 0.2159 0.2175 -0.0248 0.0422  -0.0167 24  VAL   A O   
583  O O   B VAL   A 24  ? 0.2114 0.2238 0.2209 -0.0372 0.0409  0.0019  24  VAL   A O   
584  C CB  A VAL   A 24  ? 0.2090 0.1989 0.2426 -0.0220 0.0526  -0.0084 24  VAL   A CB  
585  C CB  B VAL   A 24  ? 0.2085 0.2039 0.2246 -0.0395 0.0261  0.0125  24  VAL   A CB  
586  C CG1 A VAL   A 24  ? 0.2150 0.2044 0.2640 -0.0158 0.0534  -0.0215 24  VAL   A CG1 
587  C CG1 B VAL   A 24  ? 0.2183 0.2112 0.2412 -0.0343 0.0211  0.0098  24  VAL   A CG1 
588  C CG2 A VAL   A 24  ? 0.2226 0.2109 0.2611 -0.0153 0.0670  0.0055  24  VAL   A CG2 
589  C CG2 B VAL   A 24  ? 0.2111 0.1978 0.2241 -0.0413 0.0274  0.0141  24  VAL   A CG2 
608  N N   A GLU   A 25  ? 0.2074 0.2367 0.2149 -0.0404 0.0508  -0.0241 25  GLU   A N   
609  N N   B GLU   A 25  ? 0.2070 0.2322 0.2104 -0.0454 0.0462  -0.0143 25  GLU   A N   
610  C CA  A GLU   A 25  ? 0.2246 0.2690 0.2229 -0.0294 0.0590  -0.0297 25  GLU   A CA  
611  C CA  B GLU   A 25  ? 0.2148 0.2453 0.2182 -0.0521 0.0461  -0.0182 25  GLU   A CA  
612  C C   A GLU   A 25  ? 0.2139 0.2734 0.1903 -0.0388 0.0687  -0.0299 25  GLU   A C   
613  C C   B GLU   A 25  ? 0.2168 0.2516 0.2017 -0.0520 0.0552  -0.0198 25  GLU   A C   
614  O O   A GLU   A 25  ? 0.2139 0.2862 0.2109 -0.0404 0.0649  -0.0279 25  GLU   A O   
615  O O   B GLU   A 25  ? 0.2200 0.2542 0.2028 -0.0513 0.0546  -0.0294 25  GLU   A O   
616  C CB  A GLU   A 25  ? 0.2517 0.2998 0.2716 -0.0208 0.0577  -0.0210 25  GLU   A CB  
617  C CB  B GLU   A 25  ? 0.2230 0.2529 0.2434 -0.0537 0.0412  -0.0198 25  GLU   A CB  
618  C CG  A GLU   A 25  ? 0.2810 0.3239 0.3372 -0.0206 0.0375  -0.0217 25  GLU   A CG  
619  C CG  B GLU   A 25  ? 0.2373 0.2651 0.2875 -0.0533 0.0307  -0.0178 25  GLU   A CG  
620  C CD  A GLU   A 25  ? 0.3042 0.3442 0.3925 -0.0205 0.0212  -0.0178 25  GLU   A CD  
621  C CD  B GLU   A 25  ? 0.2468 0.2772 0.3285 -0.0531 0.0177  -0.0152 25  GLU   A CD  
622  O OE1 A GLU   A 25  ? 0.3143 0.3535 0.4032 -0.0172 0.0068  -0.0236 25  GLU   A OE1 
623  O OE1 B GLU   A 25  ? 0.2512 0.2819 0.3483 -0.0537 0.0138  -0.0130 25  GLU   A OE1 
624  O OE2 A GLU   A 25  ? 0.3126 0.3525 0.4296 -0.0218 0.0162  -0.0236 25  GLU   A OE2 
625  O OE2 B GLU   A 25  ? 0.2505 0.2835 0.3435 -0.0508 0.0152  -0.0116 25  GLU   A OE2 
638  N N   A GLU   A 26  ? 0.2079 0.2660 0.1961 -0.0601 0.0697  -0.0278 26  GLU   A N   
639  N N   B GLU   A 26  ? 0.2133 0.2512 0.1958 -0.0581 0.0650  -0.0197 26  GLU   A N   
640  C CA  A GLU   A 26  ? 0.2195 0.2663 0.1716 -0.0714 0.0626  -0.0198 26  GLU   A CA  
641  C CA  B GLU   A 26  ? 0.2170 0.2536 0.1884 -0.0618 0.0649  -0.0158 26  GLU   A CA  
642  C C   A GLU   A 26  ? 0.2191 0.2529 0.1646 -0.0683 0.0472  -0.0149 26  GLU   A C   
643  C C   B GLU   A 26  ? 0.2112 0.2446 0.1725 -0.0638 0.0608  -0.0157 26  GLU   A C   
644  O O   A GLU   A 26  ? 0.2343 0.2518 0.1617 -0.0740 0.0459  -0.0152 26  GLU   A O   
645  O O   B GLU   A 26  ? 0.2157 0.2402 0.1625 -0.0643 0.0738  -0.0154 26  GLU   A O   
646  C CB  A GLU   A 26  ? 0.2383 0.2729 0.1915 -0.0835 0.0513  -0.0099 26  GLU   A CB  
647  C CB  B GLU   A 26  ? 0.2279 0.2630 0.2046 -0.0625 0.0535  -0.0164 26  GLU   A CB  
648  C CG  A GLU   A 26  ? 0.2663 0.2905 0.2707 -0.0897 0.0473  -0.0199 26  GLU   A CG  
649  C CG  B GLU   A 26  ? 0.2378 0.2690 0.2167 -0.0660 0.0561  -0.0166 26  GLU   A CG  
650  C CD  A GLU   A 26  ? 0.2856 0.3013 0.3157 -0.0995 0.0656  -0.0220 26  GLU   A CD  
651  C CD  B GLU   A 26  ? 0.2453 0.2734 0.2100 -0.0741 0.0615  -0.0170 26  GLU   A CD  
652  O OE1 A GLU   A 26  ? 0.2811 0.3259 0.3075 -0.0894 0.0979  -0.0554 26  GLU   A OE1 
653  O OE1 B GLU   A 26  ? 0.2504 0.2917 0.2151 -0.0699 0.0709  -0.0204 26  GLU   A OE1 
654  O OE2 A GLU   A 26  ? 0.3083 0.3017 0.3392 -0.1052 0.0553  -0.0073 26  GLU   A OE2 
655  O OE2 B GLU   A 26  ? 0.2470 0.2659 0.1604 -0.0806 0.0702  -0.0205 26  GLU   A OE2 
668  N N   . ALA   A 27  ? 0.1998 0.2402 0.1647 -0.0663 0.0467  -0.0123 27  ALA   A N   
669  C CA  . ALA   A 27  ? 0.2058 0.2521 0.1586 -0.0581 0.0410  -0.0110 27  ALA   A CA  
670  C C   . ALA   A 27  ? 0.2453 0.2766 0.1692 -0.0629 0.0500  -0.0248 27  ALA   A C   
671  O O   . ALA   A 27  ? 0.2437 0.2690 0.1753 -0.0671 0.0298  -0.0162 27  ALA   A O   
672  C CB  . ALA   A 27  ? 0.1785 0.2422 0.1631 -0.0565 0.0282  -0.0096 27  ALA   A CB  
679  N N   A LYS   A 28  ? 0.2781 0.2930 0.1795 -0.0619 0.0491  -0.0580 28  LYS   A N   
680  N N   B LYS   A 28  ? 0.2762 0.2960 0.1990 -0.0570 0.0416  -0.0303 28  LYS   A N   
681  C CA  A LYS   A 28  ? 0.3153 0.3248 0.2099 -0.0555 0.0482  -0.0772 28  LYS   A CA  
682  C CA  B LYS   A 28  ? 0.3072 0.3206 0.2384 -0.0493 0.0321  -0.0348 28  LYS   A CA  
683  C C   A LYS   A 28  ? 0.3339 0.3532 0.2008 -0.0645 0.0661  -0.0575 28  LYS   A C   
684  C C   B LYS   A 28  ? 0.3290 0.3428 0.2495 -0.0525 0.0383  -0.0280 28  LYS   A C   
685  O O   A LYS   A 28  ? 0.3422 0.3628 0.2461 -0.0635 0.0416  -0.0545 28  LYS   A O   
686  O O   B LYS   A 28  ? 0.3331 0.3475 0.2639 -0.0508 0.0299  -0.0282 28  LYS   A O   
687  C CB  A LYS   A 28  ? 0.3335 0.3347 0.2584 -0.0392 0.0381  -0.0988 28  LYS   A CB  
688  C CB  B LYS   A 28  ? 0.3152 0.3249 0.2693 -0.0393 0.0198  -0.0413 28  LYS   A CB  
689  C CG  A LYS   A 28  ? 0.3493 0.3438 0.3164 -0.0282 0.0296  -0.1028 28  LYS   A CG  
690  C CG  B LYS   A 28  ? 0.3226 0.3286 0.3035 -0.0310 0.0113  -0.0417 28  LYS   A CG  
691  C CD  A LYS   A 28  ? 0.3636 0.3606 0.3950 -0.0197 0.0145  -0.0969 28  LYS   A CD  
692  C CD  B LYS   A 28  ? 0.3312 0.3350 0.3461 -0.0240 0.0028  -0.0406 28  LYS   A CD  
693  C CE  A LYS   A 28  ? 0.3738 0.3716 0.4489 -0.0160 0.0014  -0.0981 28  LYS   A CE  
694  C CE  B LYS   A 28  ? 0.3377 0.3381 0.3795 -0.0215 -0.0014 -0.0400 28  LYS   A CE  
695  N NZ  A LYS   A 28  ? 0.3828 0.3777 0.4843 -0.0133 -0.0031 -0.0991 28  LYS   A NZ  
696  N NZ  B LYS   A 28  ? 0.3407 0.3395 0.3981 -0.0198 -0.0043 -0.0410 28  LYS   A NZ  
723  N N   A LYS   A 29  ? 0.3432 0.3721 0.1741 -0.0752 0.1008  -0.0329 29  LYS   A N   
724  N N   B LYS   A 29  ? 0.3452 0.3597 0.2555 -0.0585 0.0525  -0.0182 29  LYS   A N   
725  C CA  A LYS   A 29  ? 0.3623 0.3960 0.2004 -0.0778 0.1242  -0.0149 29  LYS   A CA  
726  C CA  B LYS   A 29  ? 0.3631 0.3771 0.2723 -0.0630 0.0662  -0.0101 29  LYS   A CA  
727  C C   A LYS   A 29  ? 0.3678 0.3902 0.1866 -0.0839 0.1074  -0.0087 29  LYS   A C   
728  C C   B LYS   A 29  ? 0.3647 0.3775 0.2325 -0.0770 0.0782  -0.0058 29  LYS   A C   
729  O O   A LYS   A 29  ? 0.3806 0.4016 0.2088 -0.0778 0.0958  -0.0108 29  LYS   A O   
730  O O   B LYS   A 29  ? 0.3702 0.3817 0.2430 -0.0746 0.0752  -0.0048 29  LYS   A O   
731  C CB  A LYS   A 29  ? 0.3750 0.4269 0.2577 -0.0681 0.1532  -0.0057 29  LYS   A CB  
732  C CB  B LYS   A 29  ? 0.3775 0.3936 0.3290 -0.0526 0.0650  -0.0065 29  LYS   A CB  
733  C CG  A LYS   A 29  ? 0.3937 0.4518 0.3375 -0.0586 0.1538  -0.0022 29  LYS   A CG  
734  C CG  B LYS   A 29  ? 0.3913 0.4071 0.3813 -0.0436 0.0624  -0.0046 29  LYS   A CG  
735  C CD  A LYS   A 29  ? 0.4102 0.4713 0.4138 -0.0511 0.1484  -0.0008 29  LYS   A CD  
736  C CD  B LYS   A 29  ? 0.4022 0.4178 0.4272 -0.0367 0.0598  -0.0024 29  LYS   A CD  
737  C CE  A LYS   A 29  ? 0.4208 0.4846 0.4627 -0.0456 0.1470  0.0001  29  LYS   A CE  
738  C CE  B LYS   A 29  ? 0.4095 0.4254 0.4591 -0.0320 0.0588  -0.0013 29  LYS   A CE  
739  N NZ  A LYS   A 29  ? 0.4262 0.4921 0.4931 -0.0419 0.1445  -0.0015 29  LYS   A NZ  
740  N NZ  B LYS   A 29  ? 0.4133 0.4293 0.4779 -0.0295 0.0578  -0.0008 29  LYS   A NZ  
767  N N   . VAL   A 30  ? 0.3584 0.3726 0.1886 -0.0935 0.0943  -0.0034 30  VAL   A N   
768  C CA  . VAL   A 30  ? 0.3538 0.3553 0.1798 -0.1165 0.0632  0.0201  30  VAL   A CA  
769  C C   . VAL   A 30  ? 0.3574 0.3422 0.1477 -0.1178 0.0402  0.0262  30  VAL   A C   
770  O O   . VAL   A 30  ? 0.3645 0.3436 0.1537 -0.1208 0.0318  0.0303  30  VAL   A O   
771  C CB  . VAL   A 30  ? 0.3502 0.3480 0.2219 -0.1316 0.0340  0.0243  30  VAL   A CB  
772  C CG1 . VAL   A 30  ? 0.3559 0.3488 0.2461 -0.1306 0.0187  0.0277  30  VAL   A CG1 
773  C CG2 . VAL   A 30  ? 0.3476 0.3485 0.2494 -0.1395 0.0364  0.0251  30  VAL   A CG2 
784  N N   . LYS   A 31  ? 0.3465 0.3220 0.1288 -0.1177 0.0186  0.0169  31  LYS   A N   
785  C CA  . LYS   A 31  ? 0.3572 0.3243 0.1425 -0.1012 -0.0118 0.0123  31  LYS   A CA  
786  C C   . LYS   A 31  ? 0.3230 0.2967 0.1128 -0.0748 -0.0134 0.0533  31  LYS   A C   
787  O O   . LYS   A 31  ? 0.3297 0.3105 0.1283 -0.0701 -0.0300 0.0684  31  LYS   A O   
788  C CB  . LYS   A 31  ? 0.4036 0.3613 0.2519 -0.0946 -0.0370 -0.0133 31  LYS   A CB  
789  C CG  . LYS   A 31  ? 0.4551 0.3995 0.3953 -0.0836 -0.0577 -0.0271 31  LYS   A CG  
790  C CD  . LYS   A 31  ? 0.4936 0.4328 0.5044 -0.0737 -0.0753 -0.0399 31  LYS   A CD  
791  C CE  . LYS   A 31  ? 0.5204 0.4571 0.5729 -0.0669 -0.0873 -0.0503 31  LYS   A CE  
792  N NZ  . LYS   A 31  ? 0.5351 0.4653 0.6086 -0.0637 -0.0935 -0.0579 31  LYS   A NZ  
806  N N   . PRO   A 32  ? 0.2796 0.2598 0.1051 -0.0769 -0.0044 0.0386  32  PRO   A N   
807  C CA  . PRO   A 32  ? 0.2660 0.2427 0.1474 -0.0705 -0.0194 0.0482  32  PRO   A CA  
808  C C   . PRO   A 32  ? 0.2583 0.2418 0.1528 -0.0594 -0.0271 0.0578  32  PRO   A C   
809  O O   . PRO   A 32  ? 0.2549 0.2403 0.1648 -0.0583 -0.0372 0.0519  32  PRO   A O   
810  C CB  . PRO   A 32  ? 0.2575 0.2485 0.1586 -0.0683 -0.0159 0.0371  32  PRO   A CB  
811  C CG  . PRO   A 32  ? 0.2514 0.2531 0.1126 -0.0627 -0.0271 0.0241  32  PRO   A CG  
812  C CD  . PRO   A 32  ? 0.2556 0.2517 0.1047 -0.0709 -0.0131 0.0324  32  PRO   A CD  
820  N N   . THR   A 33  ? 0.2624 0.2396 0.1449 -0.0553 -0.0312 0.0585  33  THR   A N   
821  C CA  . THR   A 33  ? 0.2601 0.2423 0.1539 -0.0447 -0.0440 0.0573  33  THR   A CA  
822  C C   . THR   A 33  ? 0.2278 0.2170 0.1484 -0.0470 -0.0394 0.0415  33  THR   A C   
823  O O   . THR   A 33  ? 0.2231 0.2229 0.1587 -0.0431 -0.0539 0.0535  33  THR   A O   
824  C CB  . THR   A 33  ? 0.2895 0.2698 0.1632 -0.0312 -0.0499 0.0870  33  THR   A CB  
825  O OG1 . THR   A 33  ? 0.3130 0.2892 0.2007 -0.0141 -0.0395 0.0983  33  THR   A OG1 
826  C CG2 . THR   A 33  ? 0.2949 0.2789 0.1998 -0.0268 -0.0551 0.0903  33  THR   A CG2 
834  N N   . VAL   A 34  ? 0.2086 0.2007 0.1343 -0.0454 -0.0348 0.0333  34  VAL   A N   
835  C CA  . VAL   A 34  ? 0.1846 0.1866 0.1136 -0.0322 -0.0199 0.0391  34  VAL   A CA  
836  C C   . VAL   A 34  ? 0.1746 0.1758 0.1095 -0.0276 -0.0094 0.0303  34  VAL   A C   
837  O O   . VAL   A 34  ? 0.1709 0.1795 0.1373 -0.0347 -0.0064 0.0342  34  VAL   A O   
838  C CB  . VAL   A 34  ? 0.1864 0.1849 0.1456 -0.0268 -0.0162 0.0257  34  VAL   A CB  
839  C CG1 . VAL   A 34  ? 0.1907 0.1820 0.1411 -0.0286 0.0050  0.0068  34  VAL   A CG1 
840  C CG2 . VAL   A 34  ? 0.1973 0.2030 0.1772 -0.0160 -0.0218 0.0303  34  VAL   A CG2 
850  N N   . VAL   A 35  ? 0.1599 0.1654 0.1148 -0.0312 -0.0092 0.0237  35  VAL   A N   
851  C CA  . VAL   A 35  ? 0.1504 0.1605 0.1060 -0.0267 -0.0065 0.0110  35  VAL   A CA  
852  C C   . VAL   A 35  ? 0.1423 0.1466 0.1210 -0.0264 -0.0009 0.0175  35  VAL   A C   
853  O O   . VAL   A 35  ? 0.1365 0.1619 0.1325 -0.0266 0.0094  0.0095  35  VAL   A O   
854  C CB  . VAL   A 35  ? 0.1551 0.1649 0.1271 -0.0183 0.0071  0.0075  35  VAL   A CB  
855  C CG1 . VAL   A 35  ? 0.1682 0.1716 0.1369 -0.0138 0.0031  -0.0045 35  VAL   A CG1 
856  C CG2 . VAL   A 35  ? 0.1490 0.1608 0.1632 -0.0118 0.0150  0.0032  35  VAL   A CG2 
866  N N   . VAL   A 36  ? 0.1266 0.1446 0.1118 -0.0173 0.0048  0.0232  36  VAL   A N   
867  C CA  . VAL   A 36  ? 0.1242 0.1382 0.1136 -0.0129 0.0064  0.0126  36  VAL   A CA  
868  C C   . VAL   A 36  ? 0.1263 0.1430 0.1240 -0.0147 0.0055  0.0143  36  VAL   A C   
869  O O   . VAL   A 36  ? 0.1309 0.1392 0.1378 -0.0079 0.0188  0.0111  36  VAL   A O   
870  C CB  . VAL   A 36  ? 0.1276 0.1324 0.1152 -0.0103 -0.0033 0.0163  36  VAL   A CB  
871  C CG1 . VAL   A 36  ? 0.1359 0.1352 0.1329 -0.0159 0.0026  0.0011  36  VAL   A CG1 
872  C CG2 . VAL   A 36  ? 0.1404 0.1388 0.1351 -0.0125 0.0023  0.0209  36  VAL   A CG2 
882  N N   . ASN   A 37  ? 0.1229 0.1283 0.1185 -0.0010 0.0061  0.0141  37  ASN   A N   
883  C CA  . ASN   A 37  ? 0.1244 0.1217 0.1143 -0.0001 0.0098  0.0103  37  ASN   A CA  
884  C C   . ASN   A 37  ? 0.1261 0.1175 0.1117 -0.0033 0.0082  0.0218  37  ASN   A C   
885  O O   . ASN   A 37  ? 0.1402 0.1323 0.1074 0.0068  0.0105  0.0070  37  ASN   A O   
886  C CB  . ASN   A 37  ? 0.1277 0.1229 0.1246 0.0033  0.0018  0.0056  37  ASN   A CB  
887  C CG  . ASN   A 37  ? 0.1257 0.1228 0.1342 0.0029  0.0090  0.0077  37  ASN   A CG  
888  O OD1 . ASN   A 37  ? 0.1271 0.1237 0.1561 -0.0016 0.0079  0.0149  37  ASN   A OD1 
889  N ND2 . ASN   A 37  ? 0.1348 0.1292 0.1367 -0.0040 0.0038  0.0265  37  ASN   A ND2 
896  N N   . ALA   A 38  ? 0.1242 0.1276 0.1291 -0.0024 0.0075  0.0142  38  ALA   A N   
897  C CA  . ALA   A 38  ? 0.1351 0.1340 0.1238 -0.0022 -0.0062 0.0109  38  ALA   A CA  
898  C C   . ALA   A 38  ? 0.1301 0.1393 0.1200 0.0049  -0.0051 0.0028  38  ALA   A C   
899  O O   . ALA   A 38  ? 0.1301 0.1372 0.1274 0.0069  -0.0017 0.0083  38  ALA   A O   
900  C CB  . ALA   A 38  ? 0.1311 0.1693 0.1401 -0.0107 -0.0048 0.0015  38  ALA   A CB  
906  N N   A ALA   A 39  ? 0.1228 0.1269 0.1330 0.0034  0.0045  0.0055  39  ALA   A N   
907  N N   B ALA   A 39  ? 0.1310 0.1378 0.1284 -0.0024 0.0020  0.0095  39  ALA   A N   
908  C CA  A ALA   A 39  ? 0.1314 0.1295 0.1285 0.0037  0.0097  -0.0010 39  ALA   A CA  
909  C CA  B ALA   A 39  ? 0.1379 0.1412 0.1337 -0.0085 0.0074  0.0127  39  ALA   A CA  
910  C C   A ALA   A 39  ? 0.1300 0.1282 0.1326 0.0043  0.0016  0.0015  39  ALA   A C   
911  C C   B ALA   A 39  ? 0.1349 0.1347 0.1209 -0.0091 0.0113  0.0127  39  ALA   A C   
912  O O   A ALA   A 39  ? 0.1366 0.1287 0.1425 0.0047  0.0060  0.0044  39  ALA   A O   
913  O O   B ALA   A 39  ? 0.1281 0.1289 0.0951 -0.0119 0.0150  0.0223  39  ALA   A O   
914  C CB  A ALA   A 39  ? 0.1359 0.1414 0.1397 -0.0008 0.0005  -0.0038 39  ALA   A CB  
915  C CB  B ALA   A 39  ? 0.1445 0.1514 0.1579 -0.0134 0.0025  0.0065  39  ALA   A CB  
926  N N   . ASN   A 40  ? 0.1404 0.1360 0.1298 -0.0090 0.0227  0.0077  40  ASN   A N   
927  C CA  . ASN   A 40  ? 0.1426 0.1347 0.1296 -0.0028 0.0144  0.0022  40  ASN   A CA  
928  C C   . ASN   A 40  ? 0.1540 0.1256 0.1130 -0.0042 0.0206  0.0081  40  ASN   A C   
929  O O   . ASN   A 40  ? 0.1437 0.1276 0.1294 -0.0064 0.0236  0.0158  40  ASN   A O   
930  C CB  . ASN   A 40  ? 0.1568 0.1426 0.1423 -0.0012 0.0032  0.0085  40  ASN   A CB  
931  C CG  . ASN   A 40  ? 0.1675 0.1333 0.1769 0.0009  -0.0025 0.0158  40  ASN   A CG  
932  O OD1 . ASN   A 40  ? 0.1778 0.1402 0.1872 0.0029  0.0065  0.0082  40  ASN   A OD1 
933  N ND2 . ASN   A 40  ? 0.1679 0.1493 0.1997 0.0040  -0.0050 -0.0111 40  ASN   A ND2 
941  N N   A VAL   A 41  ? 0.1641 0.1248 0.1261 -0.0036 0.0255  0.0124  41  VAL   A N   
942  N N   B VAL   A 41  ? 0.1626 0.1342 0.1253 -0.0028 0.0315  0.0189  41  VAL   A N   
943  C CA  A VAL   A 41  ? 0.1622 0.1287 0.1433 -0.0002 0.0283  0.0041  41  VAL   A CA  
944  C CA  B VAL   A 41  ? 0.1638 0.1458 0.1383 0.0002  0.0383  0.0252  41  VAL   A CA  
945  C C   A VAL   A 41  ? 0.1520 0.1255 0.1413 0.0022  0.0294  0.0113  41  VAL   A C   
946  C C   B VAL   A 41  ? 0.1601 0.1511 0.1404 0.0050  0.0400  0.0277  41  VAL   A C   
947  O O   A VAL   A 41  ? 0.1542 0.1171 0.1802 0.0051  0.0208  0.0049  41  VAL   A O   
948  O O   B VAL   A 41  ? 0.1619 0.1538 0.1543 0.0050  0.0407  0.0235  41  VAL   A O   
949  C CB  A VAL   A 41  ? 0.1703 0.1415 0.1470 -0.0059 0.0339  0.0037  41  VAL   A CB  
950  C CB  B VAL   A 41  ? 0.1641 0.1540 0.1496 -0.0026 0.0460  0.0287  41  VAL   A CB  
951  C CG1 A VAL   A 41  ? 0.1857 0.1517 0.1657 -0.0013 0.0343  -0.0006 41  VAL   A CG1 
952  C CG1 B VAL   A 41  ? 0.1734 0.1593 0.1614 -0.0050 0.0534  0.0221  41  VAL   A CG1 
953  C CG2 A VAL   A 41  ? 0.1742 0.1481 0.1343 -0.0080 0.0498  0.0029  41  VAL   A CG2 
954  C CG2 B VAL   A 41  ? 0.1645 0.1637 0.1580 0.0002  0.0377  0.0301  41  VAL   A CG2 
973  N N   A TYR   A 42  ? 0.1434 0.1223 0.1585 -0.0107 0.0309  0.0154  42  TYR   A N   
974  N N   B TYR   A 42  ? 0.1538 0.1494 0.1372 0.0058  0.0343  0.0383  42  TYR   A N   
975  C CA  A TYR   A 42  ? 0.1416 0.1177 0.1538 -0.0103 0.0304  0.0175  42  TYR   A CA  
976  C CA  B TYR   A 42  ? 0.1528 0.1496 0.1389 0.0012  0.0325  0.0340  42  TYR   A CA  
977  C C   A TYR   A 42  ? 0.1272 0.1174 0.1677 -0.0066 0.0253  0.0156  42  TYR   A C   
978  C C   B TYR   A 42  ? 0.1489 0.1501 0.1228 0.0026  0.0263  0.0439  42  TYR   A C   
979  O O   A TYR   A 42  ? 0.1225 0.1222 0.1930 -0.0169 0.0154  0.0025  42  TYR   A O   
980  O O   B TYR   A 42  ? 0.1439 0.1546 0.1322 0.0004  0.0249  0.0336  42  TYR   A O   
981  C CB  A TYR   A 42  ? 0.1644 0.1295 0.1490 -0.0037 0.0332  0.0222  42  TYR   A CB  
982  C CB  B TYR   A 42  ? 0.1608 0.1522 0.1530 -0.0038 0.0362  0.0261  42  TYR   A CB  
983  C CG  A TYR   A 42  ? 0.1882 0.1417 0.1614 0.0041  0.0254  0.0348  42  TYR   A CG  
984  C CG  B TYR   A 42  ? 0.1700 0.1564 0.1556 -0.0066 0.0383  0.0194  42  TYR   A CG  
985  C CD1 A TYR   A 42  ? 0.1984 0.1531 0.1664 -0.0055 0.0322  0.0369  42  TYR   A CD1 
986  C CD1 B TYR   A 42  ? 0.1773 0.1620 0.1610 -0.0113 0.0344  0.0084  42  TYR   A CD1 
987  C CD2 A TYR   A 42  ? 0.2052 0.1676 0.1845 0.0061  0.0248  0.0275  42  TYR   A CD2 
988  C CD2 B TYR   A 42  ? 0.1760 0.1650 0.1542 -0.0055 0.0404  0.0111  42  TYR   A CD2 
989  C CE1 A TYR   A 42  ? 0.2020 0.1664 0.1609 -0.0094 0.0443  0.0327  42  TYR   A CE1 
990  C CE1 B TYR   A 42  ? 0.1823 0.1659 0.1624 -0.0134 0.0348  -0.0029 42  TYR   A CE1 
991  C CE2 A TYR   A 42  ? 0.2148 0.1816 0.1894 -0.0032 0.0358  0.0279  42  TYR   A CE2 
992  C CE2 B TYR   A 42  ? 0.1789 0.1682 0.1603 -0.0134 0.0416  0.0126  42  TYR   A CE2 
993  C CZ  A TYR   A 42  ? 0.2149 0.1823 0.1800 -0.0128 0.0479  0.0262  42  TYR   A CZ  
994  C CZ  B TYR   A 42  ? 0.1843 0.1706 0.1637 -0.0146 0.0397  -0.0023 42  TYR   A CZ  
995  O OH  A TYR   A 42  ? 0.2208 0.2055 0.2029 -0.0239 0.0459  0.0150  42  TYR   A OH  
996  O OH  B TYR   A 42  ? 0.1923 0.1822 0.1806 -0.0160 0.0289  -0.0080 42  TYR   A OH  
1015 N N   A LEU   A 43  ? 0.1304 0.1234 0.1580 -0.0086 0.0160  -0.0012 43  LEU   A N   
1016 N N   B LEU   A 43  ? 0.1441 0.1469 0.1155 0.0061  0.0139  0.0359  43  LEU   A N   
1017 C CA  A LEU   A 43  ? 0.1278 0.1252 0.1431 -0.0106 0.0155  0.0039  43  LEU   A CA  
1018 C CA  B LEU   A 43  ? 0.1416 0.1435 0.1191 0.0063  0.0039  0.0289  43  LEU   A CA  
1019 C C   A LEU   A 43  ? 0.1230 0.1259 0.1370 -0.0016 0.0077  0.0013  43  LEU   A C   
1020 C C   B LEU   A 43  ? 0.1432 0.1450 0.1354 0.0081  -0.0014 0.0242  43  LEU   A C   
1021 O O   A LEU   A 43  ? 0.1399 0.1311 0.1645 0.0025  -0.0056 -0.0100 43  LEU   A O   
1022 O O   B LEU   A 43  ? 0.1537 0.1483 0.1491 0.0034  -0.0033 0.0209  43  LEU   A O   
1023 C CB  A LEU   A 43  ? 0.1405 0.1222 0.1526 -0.0089 0.0193  0.0053  43  LEU   A CB  
1024 C CB  B LEU   A 43  ? 0.1424 0.1382 0.1287 0.0048  0.0001  0.0220  43  LEU   A CB  
1025 C CG  A LEU   A 43  ? 0.1402 0.1254 0.1636 -0.0030 0.0140  0.0083  43  LEU   A CG  
1026 C CG  B LEU   A 43  ? 0.1399 0.1368 0.1359 0.0038  -0.0044 0.0125  43  LEU   A CG  
1027 C CD1 A LEU   A 43  ? 0.1448 0.1306 0.1801 -0.0024 -0.0027 0.0108  43  LEU   A CD1 
1028 C CD1 B LEU   A 43  ? 0.1412 0.1371 0.1356 0.0004  -0.0106 0.0143  43  LEU   A CD1 
1029 C CD2 A LEU   A 43  ? 0.1516 0.1308 0.1736 -0.0062 0.0164  0.0193  43  LEU   A CD2 
1030 C CD2 B LEU   A 43  ? 0.1469 0.1352 0.1370 0.0019  -0.0005 0.0169  43  LEU   A CD2 
1053 N N   A LYS   A 44  ? 0.1381 0.1259 0.1363 -0.0030 0.0119  0.0134  44  LYS   A N   
1054 N N   B LYS   A 44  ? 0.1454 0.1474 0.1418 0.0115  -0.0023 0.0204  44  LYS   A N   
1055 C CA  A LYS   A 44  ? 0.1486 0.1264 0.1405 -0.0041 0.0172  0.0162  44  LYS   A CA  
1056 C CA  B LYS   A 44  ? 0.1526 0.1518 0.1548 0.0095  0.0006  0.0155  44  LYS   A CA  
1057 C C   A LYS   A 44  ? 0.1327 0.1297 0.1348 0.0007  0.0041  0.0075  44  LYS   A C   
1058 C C   B LYS   A 44  ? 0.1388 0.1422 0.1442 0.0065  0.0009  0.0121  44  LYS   A C   
1059 O O   A LYS   A 44  ? 0.1397 0.1415 0.1498 0.0035  0.0039  -0.0019 44  LYS   A O   
1060 O O   B LYS   A 44  ? 0.1426 0.1494 0.1482 0.0070  0.0044  0.0050  44  LYS   A O   
1061 C CB  A LYS   A 44  ? 0.1759 0.1379 0.1717 -0.0068 0.0295  0.0353  44  LYS   A CB  
1062 C CB  B LYS   A 44  ? 0.1751 0.1720 0.1973 0.0117  0.0077  0.0136  44  LYS   A CB  
1063 C CG  A LYS   A 44  ? 0.2082 0.1715 0.2308 -0.0132 0.0411  0.0464  44  LYS   A CG  
1064 C CG  B LYS   A 44  ? 0.1954 0.1918 0.2468 0.0114  0.0145  0.0151  44  LYS   A CG  
1065 C CD  A LYS   A 44  ? 0.2463 0.2302 0.3417 -0.0142 0.0230  0.0378  44  LYS   A CD  
1066 C CD  B LYS   A 44  ? 0.2153 0.2150 0.2946 0.0017  0.0070  0.0168  44  LYS   A CD  
1067 C CE  A LYS   A 44  ? 0.2655 0.2607 0.4072 -0.0163 0.0162  0.0373  44  LYS   A CE  
1068 C CE  B LYS   A 44  ? 0.2280 0.2331 0.3295 -0.0052 0.0019  0.0195  44  LYS   A CE  
1069 N NZ  A LYS   A 44  ? 0.2718 0.2749 0.4308 -0.0159 0.0131  0.0457  44  LYS   A NZ  
1070 N NZ  B LYS   A 44  ? 0.2376 0.2446 0.3509 -0.0147 0.0030  0.0172  44  LYS   A NZ  
1097 N N   . HIS   A 45  ? 0.1278 0.1313 0.1460 0.0016  0.0028  0.0176  45  HIS   A N   
1098 C CA  . HIS   A 45  ? 0.1308 0.1284 0.1438 0.0017  -0.0057 0.0137  45  HIS   A CA  
1099 C C   . HIS   A 45  ? 0.1367 0.1413 0.1589 0.0062  0.0019  0.0155  45  HIS   A C   
1100 O O   . HIS   A 45  ? 0.1556 0.1552 0.1949 0.0266  0.0007  -0.0048 45  HIS   A O   
1101 C CB  . HIS   A 45  ? 0.1302 0.1264 0.1456 -0.0027 -0.0010 0.0056  45  HIS   A CB  
1102 C CG  . HIS   A 45  ? 0.1285 0.1270 0.1266 -0.0070 0.0017  0.0062  45  HIS   A CG  
1103 N ND1 . HIS   A 45  ? 0.1291 0.1308 0.1452 -0.0021 0.0001  0.0119  45  HIS   A ND1 
1104 C CD2 . HIS   A 45  ? 0.1237 0.1347 0.1467 -0.0126 -0.0029 0.0209  45  HIS   A CD2 
1105 C CE1 . HIS   A 45  ? 0.1274 0.1387 0.1295 -0.0043 -0.0047 0.0197  45  HIS   A CE1 
1106 N NE2 . HIS   A 45  ? 0.1227 0.1407 0.1411 -0.0045 0.0028  0.0244  45  HIS   A NE2 
1115 N N   A GLY   A 46  ? 0.1519 0.1477 0.1728 0.0113  -0.0116 0.0196  46  GLY   A N   
1116 N N   B GLY   A 46  ? 0.1402 0.1412 0.1641 0.0122  -0.0088 0.0241  46  GLY   A N   
1117 C CA  A GLY   A 46  ? 0.1538 0.1552 0.1844 0.0103  -0.0072 0.0220  46  GLY   A CA  
1118 C CA  B GLY   A 46  ? 0.1413 0.1387 0.1669 0.0118  -0.0157 0.0314  46  GLY   A CA  
1119 C C   A GLY   A 46  ? 0.1569 0.1511 0.1895 0.0158  -0.0039 0.0308  46  GLY   A C   
1120 C C   B GLY   A 46  ? 0.1448 0.1282 0.1687 0.0149  -0.0247 0.0425  46  GLY   A C   
1121 O O   A GLY   A 46  ? 0.1597 0.1588 0.2110 0.0092  -0.0145 0.0157  46  GLY   A O   
1122 O O   B GLY   A 46  ? 0.1490 0.1192 0.1868 0.0246  -0.0343 0.0666  46  GLY   A O   
1129 N N   A GLY   A 47  ? 0.1627 0.1483 0.1742 0.0200  -0.0106 0.0076  47  GLY   A N   
1130 N N   B GLY   A 47  ? 0.1404 0.1289 0.1555 0.0109  -0.0362 0.0259  47  GLY   A N   
1131 C CA  A GLY   A 47  ? 0.1588 0.1490 0.1655 0.0171  -0.0323 -0.0111 47  GLY   A CA  
1132 C CA  B GLY   A 47  ? 0.1448 0.1330 0.1616 0.0107  -0.0449 0.0159  47  GLY   A CA  
1133 C C   A GLY   A 47  ? 0.1497 0.1423 0.1617 0.0153  -0.0326 -0.0051 47  GLY   A C   
1134 C C   B GLY   A 47  ? 0.1469 0.1369 0.1592 0.0139  -0.0343 0.0042  47  GLY   A C   
1135 O O   A GLY   A 47  ? 0.1468 0.1366 0.1714 0.0186  -0.0366 0.0100  47  GLY   A O   
1136 O O   B GLY   A 47  ? 0.1481 0.1429 0.1784 0.0214  -0.0298 0.0084  47  GLY   A O   
1143 N N   A GLY   A 48  ? 0.1450 0.1452 0.1747 0.0104  -0.0455 -0.0143 48  GLY   A N   
1144 N N   B GLY   A 48  ? 0.1476 0.1437 0.1750 0.0112  -0.0242 -0.0036 48  GLY   A N   
1145 C CA  A GLY   A 48  ? 0.1412 0.1416 0.1955 0.0027  -0.0384 -0.0237 48  GLY   A CA  
1146 C CA  B GLY   A 48  ? 0.1425 0.1420 0.1782 0.0098  -0.0143 -0.0067 48  GLY   A CA  
1147 C C   A GLY   A 48  ? 0.1364 0.1397 0.1744 0.0072  -0.0085 -0.0096 48  GLY   A C   
1148 C C   B GLY   A 48  ? 0.1377 0.1363 0.1585 0.0086  0.0011  -0.0047 48  GLY   A C   
1149 O O   A GLY   A 48  ? 0.1469 0.1366 0.1826 0.0077  -0.0065 -0.0107 48  GLY   A O   
1150 O O   B GLY   A 48  ? 0.1458 0.1306 0.1570 0.0073  -0.0011 -0.0143 48  GLY   A O   
1157 N N   A VAL   A 49  ? 0.1195 0.1309 0.1720 -0.0019 -0.0061 -0.0117 49  VAL   A N   
1158 N N   B VAL   A 49  ? 0.1266 0.1334 0.1577 0.0001  0.0037  -0.0004 49  VAL   A N   
1159 C CA  A VAL   A 49  ? 0.1391 0.1313 0.1632 -0.0059 0.0171  -0.0079 49  VAL   A CA  
1160 C CA  B VAL   A 49  ? 0.1146 0.1296 0.1394 -0.0012 0.0143  0.0022  49  VAL   A CA  
1161 C C   A VAL   A 49  ? 0.1400 0.1217 0.1331 -0.0001 0.0090  -0.0036 49  VAL   A C   
1162 C C   B VAL   A 49  ? 0.1138 0.1237 0.1173 0.0049  0.0175  0.0045  49  VAL   A C   
1163 O O   A VAL   A 49  ? 0.1496 0.1302 0.1351 -0.0065 0.0188  -0.0070 49  VAL   A O   
1164 O O   B VAL   A 49  ? 0.1163 0.1171 0.1337 0.0062  0.0146  -0.0022 49  VAL   A O   
1165 C CB  A VAL   A 49  ? 0.1587 0.1385 0.1649 -0.0080 0.0234  -0.0125 49  VAL   A CB  
1166 C CB  B VAL   A 49  ? 0.1106 0.1225 0.1264 -0.0006 0.0135  -0.0079 49  VAL   A CB  
1167 C CG1 A VAL   A 49  ? 0.1712 0.1328 0.1560 -0.0033 0.0277  -0.0096 49  VAL   A CG1 
1168 C CG1 B VAL   A 49  ? 0.1178 0.1239 0.1317 0.0049  0.0202  -0.0059 49  VAL   A CG1 
1169 C CG2 A VAL   A 49  ? 0.1764 0.1534 0.2099 -0.0249 0.0223  -0.0126 49  VAL   A CG2 
1170 C CG2 B VAL   A 49  ? 0.1133 0.1245 0.1070 -0.0061 0.0229  -0.0089 49  VAL   A CG2 
1189 N N   A ALA   A 50  ? 0.1388 0.1213 0.1191 -0.0076 -0.0067 0.0009  50  ALA   A N   
1190 N N   B ALA   A 50  ? 0.1191 0.1236 0.1039 0.0099  0.0156  0.0008  50  ALA   A N   
1191 C CA  A ALA   A 50  ? 0.1313 0.1218 0.1315 -0.0129 -0.0072 0.0125  50  ALA   A CA  
1192 C CA  B ALA   A 50  ? 0.1250 0.1245 0.1161 0.0051  0.0018  0.0096  50  ALA   A CA  
1193 C C   A ALA   A 50  ? 0.1232 0.1250 0.1273 -0.0119 -0.0023 0.0009  50  ALA   A C   
1194 C C   B ALA   A 50  ? 0.1242 0.1225 0.1249 0.0032  0.0018  0.0057  50  ALA   A C   
1195 O O   A ALA   A 50  ? 0.1210 0.1307 0.1426 -0.0046 -0.0028 0.0010  50  ALA   A O   
1196 O O   B ALA   A 50  ? 0.1196 0.1213 0.1386 0.0102  0.0028  0.0078  50  ALA   A O   
1197 C CB  A ALA   A 50  ? 0.1287 0.1262 0.1331 -0.0111 0.0013  -0.0027 50  ALA   A CB  
1198 C CB  B ALA   A 50  ? 0.1271 0.1250 0.1124 0.0041  0.0101  0.0091  50  ALA   A CB  
1209 N N   . GLY   A 51  ? 0.1293 0.1211 0.1369 0.0050  -0.0089 0.0040  51  GLY   A N   
1210 C CA  . GLY   A 51  ? 0.1401 0.1208 0.1433 0.0097  -0.0132 -0.0008 51  GLY   A CA  
1211 C C   . GLY   A 51  ? 0.1285 0.1261 0.1477 0.0077  -0.0039 -0.0104 51  GLY   A C   
1212 O O   . GLY   A 51  ? 0.1324 0.1351 0.1567 0.0000  -0.0067 -0.0122 51  GLY   A O   
1217 N N   . ALA   A 52  ? 0.1269 0.1399 0.1423 0.0015  -0.0006 -0.0165 52  ALA   A N   
1218 C CA  . ALA   A 52  ? 0.1250 0.1495 0.1613 0.0016  0.0039  -0.0195 52  ALA   A CA  
1219 C C   . ALA   A 52  ? 0.1231 0.1476 0.1389 -0.0032 0.0169  -0.0083 52  ALA   A C   
1220 O O   . ALA   A 52  ? 0.1380 0.1545 0.1577 -0.0003 0.0099  -0.0158 52  ALA   A O   
1221 C CB  . ALA   A 52  ? 0.1393 0.1770 0.1790 -0.0069 -0.0026 -0.0088 52  ALA   A CB  
1227 N N   A LEU   A 53  ? 0.1251 0.1451 0.1373 -0.0086 -0.0013 -0.0057 53  LEU   A N   
1228 N N   B LEU   A 53  ? 0.1241 0.1431 0.1298 -0.0026 0.0124  -0.0010 53  LEU   A N   
1229 C CA  A LEU   A 53  ? 0.1407 0.1474 0.1367 -0.0049 0.0011  0.0018  53  LEU   A CA  
1230 C CA  B LEU   A 53  ? 0.1299 0.1408 0.1240 0.0005  0.0154  0.0045  53  LEU   A CA  
1231 C C   A LEU   A 53  ? 0.1398 0.1444 0.1176 0.0027  -0.0004 -0.0005 53  LEU   A C   
1232 C C   B LEU   A 53  ? 0.1295 0.1397 0.1119 0.0007  0.0132  -0.0011 53  LEU   A C   
1233 O O   A LEU   A 53  ? 0.1518 0.1445 0.1324 -0.0057 -0.0051 -0.0038 53  LEU   A O   
1234 O O   B LEU   A 53  ? 0.1261 0.1396 0.1120 -0.0094 0.0131  -0.0035 53  LEU   A O   
1235 C CB  A LEU   A 53  ? 0.1509 0.1498 0.1327 -0.0113 -0.0006 0.0008  53  LEU   A CB  
1236 C CB  B LEU   A 53  ? 0.1343 0.1371 0.1237 0.0008  0.0159  0.0090  53  LEU   A CB  
1237 C CG  A LEU   A 53  ? 0.1673 0.1574 0.1546 -0.0211 0.0012  0.0011  53  LEU   A CG  
1238 C CG  B LEU   A 53  ? 0.1369 0.1334 0.1159 -0.0011 0.0143  0.0126  53  LEU   A CG  
1239 C CD1 A LEU   A 53  ? 0.1748 0.1660 0.1431 -0.0098 -0.0060 -0.0123 53  LEU   A CD1 
1240 C CD1 B LEU   A 53  ? 0.1430 0.1382 0.1217 0.0086  0.0099  0.0202  53  LEU   A CD1 
1241 C CD2 A LEU   A 53  ? 0.1751 0.1707 0.1672 -0.0231 -0.0005 0.0137  53  LEU   A CD2 
1242 C CD2 B LEU   A 53  ? 0.1323 0.1305 0.0966 0.0004  0.0172  0.0045  53  LEU   A CD2 
1265 N N   . ASN   A 54  ? 0.1309 0.1383 0.1208 -0.0004 0.0053  0.0041  54  ASN   A N   
1266 C CA  . ASN   A 54  ? 0.1196 0.1358 0.1391 -0.0014 0.0004  -0.0009 54  ASN   A CA  
1267 C C   . ASN   A 54  ? 0.1306 0.1393 0.1254 -0.0024 -0.0018 -0.0061 54  ASN   A C   
1268 O O   . ASN   A 54  ? 0.1308 0.1482 0.1362 -0.0021 -0.0063 -0.0144 54  ASN   A O   
1269 C CB  . ASN   A 54  ? 0.1172 0.1329 0.1425 -0.0061 -0.0014 -0.0006 54  ASN   A CB  
1270 C CG  . ASN   A 54  ? 0.1255 0.1373 0.1369 0.0031  -0.0083 -0.0030 54  ASN   A CG  
1271 O OD1 . ASN   A 54  ? 0.1269 0.1393 0.1416 -0.0026 -0.0054 0.0004  54  ASN   A OD1 
1272 N ND2 . ASN   A 54  ? 0.1263 0.1447 0.1721 -0.0059 -0.0177 0.0120  54  ASN   A ND2 
1280 N N   A LYS   A 55  ? 0.1313 0.1429 0.1440 -0.0018 -0.0046 -0.0128 55  LYS   A N   
1281 N N   B LYS   A 55  ? 0.1343 0.1419 0.1359 0.0011  -0.0029 -0.0085 55  LYS   A N   
1282 C CA  A LYS   A 55  ? 0.1387 0.1514 0.1527 0.0053  -0.0089 -0.0191 55  LYS   A CA  
1283 C CA  B LYS   A 55  ? 0.1407 0.1466 0.1461 0.0073  -0.0057 -0.0094 55  LYS   A CA  
1284 C C   A LYS   A 55  ? 0.1409 0.1547 0.1500 -0.0043 0.0009  -0.0245 55  LYS   A C   
1285 C C   B LYS   A 55  ? 0.1428 0.1539 0.1467 -0.0027 -0.0021 -0.0171 55  LYS   A C   
1286 O O   A LYS   A 55  ? 0.1503 0.1676 0.1627 0.0019  -0.0023 -0.0290 55  LYS   A O   
1287 O O   B LYS   A 55  ? 0.1464 0.1602 0.1499 -0.0011 -0.0093 -0.0205 55  LYS   A O   
1288 C CB  A LYS   A 55  ? 0.1477 0.1630 0.1768 0.0104  -0.0126 -0.0307 55  LYS   A CB  
1289 C CB  B LYS   A 55  ? 0.1456 0.1473 0.1628 0.0164  -0.0067 -0.0066 55  LYS   A CB  
1290 C CG  A LYS   A 55  ? 0.1673 0.1967 0.1973 0.0211  -0.0254 -0.0327 55  LYS   A CG  
1291 C CG  B LYS   A 55  ? 0.1553 0.1602 0.1872 0.0255  -0.0106 -0.0124 55  LYS   A CG  
1292 C CD  A LYS   A 55  ? 0.1836 0.2355 0.1988 0.0324  -0.0221 -0.0282 55  LYS   A CD  
1293 C CD  B LYS   A 55  ? 0.1639 0.1741 0.2006 0.0347  -0.0061 -0.0157 55  LYS   A CD  
1294 C CE  A LYS   A 55  ? 0.2045 0.2710 0.2109 0.0456  -0.0332 -0.0318 55  LYS   A CE  
1295 C CE  B LYS   A 55  ? 0.1778 0.1882 0.2176 0.0445  -0.0030 -0.0254 55  LYS   A CE  
1296 N NZ  A LYS   A 55  ? 0.2129 0.2815 0.2230 0.0559  -0.0376 -0.0253 55  LYS   A NZ  
1297 N NZ  B LYS   A 55  ? 0.1833 0.1950 0.2270 0.0530  -0.0013 -0.0315 55  LYS   A NZ  
1324 N N   . ALA   A 56  ? 0.1438 0.1613 0.1454 -0.0120 0.0102  -0.0189 56  ALA   A N   
1325 C CA  . ALA   A 56  ? 0.1569 0.1818 0.1465 -0.0146 0.0169  -0.0165 56  ALA   A CA  
1326 C C   . ALA   A 56  ? 0.1579 0.1929 0.1219 -0.0148 0.0074  -0.0285 56  ALA   A C   
1327 O O   . ALA   A 56  ? 0.1630 0.2260 0.1382 0.0003  0.0137  -0.0226 56  ALA   A O   
1328 C CB  . ALA   A 56  ? 0.1633 0.2039 0.1519 -0.0261 0.0188  -0.0082 56  ALA   A CB  
1335 N N   . THR   A 57  ? 0.1448 0.1722 0.1283 -0.0138 0.0067  -0.0255 57  THR   A N   
1336 C CA  . THR   A 57  ? 0.1460 0.1656 0.1336 -0.0156 0.0040  -0.0090 57  THR   A CA  
1337 C C   . THR   A 57  ? 0.1458 0.1716 0.1482 -0.0091 -0.0014 -0.0181 57  THR   A C   
1338 O O   . THR   A 57  ? 0.1453 0.1782 0.1657 -0.0133 -0.0096 -0.0284 57  THR   A O   
1339 C CB  . THR   A 57  ? 0.1460 0.1665 0.1411 -0.0060 0.0084  -0.0113 57  THR   A CB  
1340 O OG1 . THR   A 57  ? 0.1376 0.1650 0.1391 -0.0054 0.0030  -0.0130 57  THR   A OG1 
1341 C CG2 . THR   A 57  ? 0.1498 0.1673 0.1300 -0.0076 -0.0001 -0.0044 57  THR   A CG2 
1349 N N   . ASN   A 58  ? 0.1423 0.1717 0.1715 -0.0067 0.0107  -0.0372 58  ASN   A N   
1350 C CA  . ASN   A 58  ? 0.1683 0.1649 0.1899 -0.0183 0.0117  -0.0448 58  ASN   A CA  
1351 C C   . ASN   A 58  ? 0.1471 0.1523 0.1902 -0.0045 0.0023  -0.0312 58  ASN   A C   
1352 O O   . ASN   A 58  ? 0.1482 0.1666 0.1919 -0.0156 -0.0038 -0.0320 58  ASN   A O   
1353 C CB  . ASN   A 58  ? 0.2178 0.1843 0.2276 -0.0206 0.0432  -0.0571 58  ASN   A CB  
1354 C CG  . ASN   A 58  ? 0.2630 0.2059 0.3123 -0.0205 0.0470  -0.0440 58  ASN   A CG  
1355 O OD1 . ASN   A 58  ? 0.2942 0.1987 0.3587 0.0212  0.0806  -0.0375 58  ASN   A OD1 
1356 N ND2 . ASN   A 58  ? 0.2742 0.2229 0.3369 -0.0273 0.0340  -0.0440 58  ASN   A ND2 
1363 N N   . ASN   A 59  ? 0.1335 0.1452 0.1628 -0.0102 -0.0090 -0.0174 59  ASN   A N   
1364 C CA  . ASN   A 59  ? 0.1328 0.1329 0.1642 -0.0074 -0.0072 -0.0105 59  ASN   A CA  
1365 C C   . ASN   A 59  ? 0.1336 0.1417 0.1483 -0.0049 -0.0135 -0.0102 59  ASN   A C   
1366 O O   . ASN   A 59  ? 0.1343 0.1424 0.1536 -0.0098 -0.0033 -0.0007 59  ASN   A O   
1367 C CB  . ASN   A 59  ? 0.1381 0.1346 0.1737 -0.0047 -0.0108 -0.0156 59  ASN   A CB  
1368 C CG  . ASN   A 59  ? 0.1396 0.1420 0.1770 0.0006  -0.0240 -0.0011 59  ASN   A CG  
1369 O OD1 . ASN   A 59  ? 0.1536 0.1401 0.1657 -0.0068 -0.0222 0.0033  59  ASN   A OD1 
1370 N ND2 . ASN   A 59  ? 0.1475 0.1499 0.1867 -0.0105 -0.0173 0.0021  59  ASN   A ND2 
1377 N N   . ALA   A 60  ? 0.1319 0.1475 0.1453 -0.0038 -0.0086 -0.0062 60  ALA   A N   
1378 C CA  . ALA   A 60  ? 0.1322 0.1460 0.1516 0.0005  -0.0136 -0.0057 60  ALA   A CA  
1379 C C   . ALA   A 60  ? 0.1296 0.1436 0.1517 -0.0007 -0.0057 -0.0027 60  ALA   A C   
1380 O O   . ALA   A 60  ? 0.1264 0.1409 0.1742 -0.0046 -0.0055 -0.0108 60  ALA   A O   
1381 C CB  . ALA   A 60  ? 0.1399 0.1577 0.1480 -0.0051 -0.0178 -0.0151 60  ALA   A CB  
1387 N N   . MET   A 61  ? 0.1265 0.1362 0.1464 -0.0018 -0.0060 -0.0076 61  MET   A N   
1388 C CA  . MET   A 61  ? 0.1299 0.1312 0.1482 -0.0059 0.0034  0.0027  61  MET   A CA  
1389 C C   . MET   A 61  ? 0.1236 0.1255 0.1491 -0.0042 -0.0023 -0.0078 61  MET   A C   
1390 O O   . MET   A 61  ? 0.1332 0.1256 0.1589 -0.0046 0.0077  -0.0045 61  MET   A O   
1391 C CB  . MET   A 61  ? 0.1371 0.1368 0.1332 -0.0047 -0.0035 -0.0080 61  MET   A CB  
1392 C CG  . MET   A 61  ? 0.1373 0.1447 0.1411 0.0019  0.0015  -0.0012 61  MET   A CG  
1393 S SD  . MET   A 61  ? 0.1378 0.1422 0.1873 -0.0123 -0.0005 -0.0182 61  MET   A SD  
1394 C CE  . MET   A 61  ? 0.1646 0.1592 0.2038 -0.0118 0.0204  -0.0118 61  MET   A CE  
1404 N N   . GLN   A 62  ? 0.1224 0.1245 0.1509 -0.0066 0.0005  -0.0051 62  GLN   A N   
1405 C CA  . GLN   A 62  ? 0.1316 0.1238 0.1570 -0.0041 0.0059  0.0000  62  GLN   A CA  
1406 C C   . GLN   A 62  ? 0.1344 0.1187 0.1629 -0.0006 0.0068  0.0015  62  GLN   A C   
1407 O O   . GLN   A 62  ? 0.1331 0.1372 0.1530 -0.0017 0.0027  0.0009  62  GLN   A O   
1408 C CB  . GLN   A 62  ? 0.1299 0.1190 0.1615 0.0006  -0.0035 -0.0013 62  GLN   A CB  
1409 C CG  . GLN   A 62  ? 0.1350 0.1221 0.1582 -0.0040 -0.0025 0.0149  62  GLN   A CG  
1410 C CD  . GLN   A 62  ? 0.1421 0.1261 0.1523 -0.0041 0.0064  0.0090  62  GLN   A CD  
1411 O OE1 . GLN   A 62  ? 0.1433 0.1382 0.1644 -0.0034 0.0037  0.0020  62  GLN   A OE1 
1412 N NE2 . GLN   A 62  ? 0.1469 0.1270 0.1666 0.0023  0.0000  -0.0111 62  GLN   A NE2 
1421 N N   . VAL   A 63  ? 0.1312 0.1301 0.1790 -0.0093 0.0060  -0.0173 63  VAL   A N   
1422 C CA  . VAL   A 63  ? 0.1289 0.1401 0.1934 -0.0210 -0.0005 -0.0152 63  VAL   A CA  
1423 C C   . VAL   A 63  ? 0.1220 0.1438 0.1770 -0.0155 -0.0039 -0.0145 63  VAL   A C   
1424 O O   . VAL   A 63  ? 0.1265 0.1381 0.1969 -0.0186 0.0013  -0.0115 63  VAL   A O   
1425 C CB  . VAL   A 63  ? 0.1437 0.1597 0.2173 -0.0145 -0.0064 -0.0400 63  VAL   A CB  
1426 C CG1 . VAL   A 63  ? 0.1561 0.1788 0.2618 -0.0187 -0.0162 -0.0574 63  VAL   A CG1 
1427 C CG2 . VAL   A 63  ? 0.1459 0.1528 0.2354 -0.0117 0.0162  -0.0337 63  VAL   A CG2 
1437 N N   . GLU   A 64  ? 0.1265 0.1475 0.1657 -0.0051 -0.0012 -0.0091 64  GLU   A N   
1438 C CA  . GLU   A 64  ? 0.1257 0.1424 0.1689 -0.0070 -0.0043 -0.0053 64  GLU   A CA  
1439 C C   . GLU   A 64  ? 0.1215 0.1351 0.1694 -0.0092 0.0026  -0.0003 64  GLU   A C   
1440 O O   . GLU   A 64  ? 0.1291 0.1395 0.1761 -0.0013 0.0006  -0.0020 64  GLU   A O   
1441 C CB  . GLU   A 64  ? 0.1360 0.1510 0.1716 -0.0095 0.0021  -0.0050 64  GLU   A CB  
1442 C CG  . GLU   A 64  ? 0.1400 0.1516 0.1850 -0.0089 0.0030  0.0006  64  GLU   A CG  
1443 C CD  . GLU   A 64  ? 0.1512 0.1624 0.1920 -0.0119 0.0061  -0.0075 64  GLU   A CD  
1444 O OE1 . GLU   A 64  ? 0.1521 0.1672 0.2062 -0.0261 0.0146  -0.0047 64  GLU   A OE1 
1445 O OE2 . GLU   A 64  ? 0.1693 0.1655 0.1914 -0.0267 -0.0070 0.0062  64  GLU   A OE2 
1452 N N   . SER   A 65  ? 0.1152 0.1382 0.1618 0.0000  -0.0008 -0.0023 65  SER   A N   
1453 C CA  . SER   A 65  ? 0.1227 0.1263 0.1618 -0.0044 -0.0057 -0.0092 65  SER   A CA  
1454 C C   . SER   A 65  ? 0.1258 0.1319 0.1706 -0.0007 -0.0079 -0.0018 65  SER   A C   
1455 O O   . SER   A 65  ? 0.1330 0.1377 0.1829 0.0056  0.0110  -0.0055 65  SER   A O   
1456 C CB  . SER   A 65  ? 0.1256 0.1353 0.1595 -0.0126 0.0026  0.0033  65  SER   A CB  
1457 O OG  . SER   A 65  ? 0.1242 0.1495 0.1613 -0.0123 -0.0010 0.0102  65  SER   A OG  
1463 N N   . ASP   A 66  ? 0.1292 0.1302 0.1680 -0.0049 0.0136  0.0024  66  ASP   A N   
1464 C CA  . ASP   A 66  ? 0.1368 0.1434 0.1744 -0.0021 0.0091  0.0191  66  ASP   A CA  
1465 C C   . ASP   A 66  ? 0.1301 0.1407 0.1935 -0.0044 0.0077  0.0200  66  ASP   A C   
1466 O O   . ASP   A 66  ? 0.1394 0.1543 0.2033 -0.0026 0.0248  0.0189  66  ASP   A O   
1467 C CB  . ASP   A 66  ? 0.1433 0.1560 0.2025 0.0077  0.0179  0.0328  66  ASP   A CB  
1468 C CG  . ASP   A 66  ? 0.1711 0.1693 0.2373 -0.0004 0.0129  0.0486  66  ASP   A CG  
1469 O OD1 . ASP   A 66  ? 0.1739 0.1996 0.2093 -0.0080 -0.0024 0.0579  66  ASP   A OD1 
1470 O OD2 . ASP   A 66  ? 0.1924 0.1801 0.3252 0.0242  -0.0128 0.0187  66  ASP   A OD2 
1475 N N   . ASP   A 67  ? 0.1264 0.1394 0.2038 -0.0023 0.0034  0.0197  67  ASP   A N   
1476 C CA  . ASP   A 67  ? 0.1330 0.1640 0.2103 -0.0021 -0.0029 0.0228  67  ASP   A CA  
1477 C C   . ASP   A 67  ? 0.1307 0.1603 0.1994 0.0054  0.0128  0.0219  67  ASP   A C   
1478 O O   . ASP   A 67  ? 0.1303 0.1681 0.2160 0.0060  0.0279  0.0279  67  ASP   A O   
1479 C CB  . ASP   A 67  ? 0.1401 0.1710 0.2424 -0.0059 -0.0177 0.0312  67  ASP   A CB  
1480 C CG  . ASP   A 67  ? 0.1407 0.1810 0.2750 -0.0096 -0.0320 0.0340  67  ASP   A CG  
1481 O OD1 . ASP   A 67  ? 0.1458 0.1981 0.3635 -0.0134 -0.0431 0.0492  67  ASP   A OD1 
1482 O OD2 . ASP   A 67  ? 0.1442 0.1830 0.2578 0.0026  -0.0166 0.0251  67  ASP   A OD2 
1487 N N   . TYR   A 68  ? 0.1332 0.1514 0.1982 0.0052  0.0209  0.0324  68  TYR   A N   
1488 C CA  . TYR   A 68  ? 0.1469 0.1418 0.1930 0.0065  0.0278  0.0245  68  TYR   A CA  
1489 C C   . TYR   A 68  ? 0.1388 0.1421 0.1866 -0.0005 0.0303  0.0157  68  TYR   A C   
1490 O O   . TYR   A 68  ? 0.1440 0.1483 0.1969 0.0054  0.0362  0.0161  68  TYR   A O   
1491 C CB  . TYR   A 68  ? 0.1507 0.1403 0.2043 0.0076  0.0455  0.0287  68  TYR   A CB  
1492 C CG  . TYR   A 68  ? 0.1539 0.1576 0.2474 0.0073  0.0558  0.0298  68  TYR   A CG  
1493 C CD1 . TYR   A 68  ? 0.1657 0.1724 0.2761 -0.0159 0.0486  -0.0098 68  TYR   A CD1 
1494 C CD2 . TYR   A 68  ? 0.1760 0.1638 0.2918 0.0162  0.0610  0.0376  68  TYR   A CD2 
1495 C CE1 . TYR   A 68  ? 0.1681 0.1808 0.3172 -0.0190 0.0661  -0.0139 68  TYR   A CE1 
1496 C CE2 . TYR   A 68  ? 0.1725 0.1698 0.3118 0.0073  0.0728  0.0156  68  TYR   A CE2 
1497 C CZ  . TYR   A 68  ? 0.1763 0.1734 0.3295 -0.0182 0.0607  -0.0143 68  TYR   A CZ  
1498 O OH  . TYR   A 68  ? 0.2004 0.1717 0.3412 -0.0084 0.0279  -0.0356 68  TYR   A OH  
1508 N N   . ILE   A 69  ? 0.1287 0.1373 0.1913 0.0036  0.0222  0.0195  69  ILE   A N   
1509 C CA  . ILE   A 69  ? 0.1393 0.1376 0.1777 0.0037  0.0179  0.0081  69  ILE   A CA  
1510 C C   . ILE   A 69  ? 0.1463 0.1446 0.1752 0.0037  0.0221  0.0159  69  ILE   A C   
1511 O O   . ILE   A 69  ? 0.1547 0.1506 0.1740 -0.0050 0.0255  0.0154  69  ILE   A O   
1512 C CB  . ILE   A 69  ? 0.1517 0.1616 0.1941 0.0045  0.0130  0.0011  69  ILE   A CB  
1513 C CG1 . ILE   A 69  ? 0.1495 0.1692 0.1899 0.0031  0.0172  -0.0139 69  ILE   A CG1 
1514 C CG2 . ILE   A 69  ? 0.1718 0.1863 0.2007 0.0121  -0.0049 0.0002  69  ILE   A CG2 
1515 C CD1 . ILE   A 69  ? 0.1471 0.1786 0.2131 -0.0040 0.0118  -0.0111 69  ILE   A CD1 
1527 N N   . ALA   A 70  ? 0.1489 0.1441 0.1963 -0.0072 0.0268  0.0182  70  ALA   A N   
1528 C CA  . ALA   A 70  ? 0.1534 0.1567 0.2069 -0.0153 0.0342  0.0253  70  ALA   A CA  
1529 C C   . ALA   A 70  ? 0.1518 0.1728 0.2049 -0.0109 0.0340  0.0230  70  ALA   A C   
1530 O O   . ALA   A 70  ? 0.1669 0.2044 0.2302 0.0050  0.0493  0.0378  70  ALA   A O   
1531 C CB  . ALA   A 70  ? 0.1516 0.1533 0.2469 -0.0126 0.0253  0.0148  70  ALA   A CB  
1537 N N   . THR   A 71  ? 0.1435 0.1707 0.1924 -0.0013 0.0248  0.0250  71  THR   A N   
1538 C CA  . THR   A 71  ? 0.1515 0.1846 0.2250 0.0116  0.0219  0.0177  71  THR   A CA  
1539 C C   . THR   A 71  ? 0.1471 0.1740 0.2458 0.0146  0.0420  0.0201  71  THR   A C   
1540 O O   . THR   A 71  ? 0.1530 0.1973 0.2993 0.0082  0.0459  -0.0087 71  THR   A O   
1541 C CB  . THR   A 71  ? 0.1771 0.2084 0.2465 0.0181  -0.0122 0.0301  71  THR   A CB  
1542 O OG1 . THR   A 71  ? 0.2027 0.2298 0.2497 0.0058  -0.0299 0.0244  71  THR   A OG1 
1543 C CG2 . THR   A 71  ? 0.1904 0.2248 0.2744 0.0242  -0.0220 0.0465  71  THR   A CG2 
1551 N N   . ASN   A 72  ? 0.1541 0.1589 0.2272 0.0128  0.0340  0.0241  72  ASN   A N   
1552 C CA  . ASN   A 72  ? 0.1589 0.1620 0.2229 0.0156  0.0426  0.0268  72  ASN   A CA  
1553 C C   . ASN   A 72  ? 0.1658 0.1590 0.2193 0.0064  0.0519  0.0129  72  ASN   A C   
1554 O O   . ASN   A 72  ? 0.1825 0.1571 0.2353 0.0126  0.0457  0.0037  72  ASN   A O   
1555 C CB  . ASN   A 72  ? 0.1718 0.1696 0.2294 0.0172  0.0348  0.0291  72  ASN   A CB  
1556 C CG  . ASN   A 72  ? 0.1967 0.1834 0.2270 0.0259  0.0270  0.0327  72  ASN   A CG  
1557 O OD1 . ASN   A 72  ? 0.2180 0.2142 0.2525 0.0257  0.0382  0.0313  72  ASN   A OD1 
1558 N ND2 . ASN   A 72  ? 0.2080 0.1808 0.2349 0.0497  0.0066  0.0124  72  ASN   A ND2 
1565 N N   . GLY   A 73  ? 0.1648 0.1580 0.2138 0.0041  0.0486  0.0035  73  GLY   A N   
1566 C CA  . GLY   A 73  ? 0.1655 0.1542 0.2061 -0.0047 0.0405  0.0067  73  GLY   A CA  
1567 C C   . GLY   A 73  ? 0.1687 0.1472 0.1937 0.0012  0.0523  0.0135  73  GLY   A C   
1568 O O   . GLY   A 73  ? 0.1716 0.1556 0.1992 0.0102  0.0429  0.0208  73  GLY   A O   
1572 N N   . PRO   A 74  ? 0.1780 0.1508 0.1923 -0.0139 0.0539  0.0147  74  PRO   A N   
1573 C CA  . PRO   A 74  ? 0.1745 0.1448 0.2020 -0.0015 0.0493  0.0240  74  PRO   A CA  
1574 C C   . PRO   A 74  ? 0.1634 0.1326 0.1885 0.0029  0.0388  0.0105  74  PRO   A C   
1575 O O   . PRO   A 74  ? 0.1719 0.1358 0.2081 0.0018  0.0350  -0.0071 74  PRO   A O   
1576 C CB  . PRO   A 74  ? 0.1898 0.1726 0.2178 -0.0027 0.0505  0.0296  74  PRO   A CB  
1577 C CG  . PRO   A 74  ? 0.2150 0.2095 0.2600 -0.0242 0.0365  0.0059  74  PRO   A CG  
1578 C CD  . PRO   A 74  ? 0.1961 0.1805 0.2053 -0.0276 0.0446  -0.0031 74  PRO   A CD  
1586 N N   . LEU   A 75  ? 0.1675 0.1278 0.1649 -0.0001 0.0257  0.0061  75  LEU   A N   
1587 C CA  . LEU   A 75  ? 0.1668 0.1231 0.1551 -0.0008 0.0137  0.0076  75  LEU   A CA  
1588 C C   . LEU   A 75  ? 0.1773 0.1408 0.1507 0.0084  0.0165  0.0140  75  LEU   A C   
1589 O O   . LEU   A 75  ? 0.2074 0.1544 0.1633 0.0101  0.0102  0.0051  75  LEU   A O   
1590 C CB  . LEU   A 75  ? 0.1706 0.1342 0.1379 -0.0096 0.0103  0.0198  75  LEU   A CB  
1591 C CG  . LEU   A 75  ? 0.1842 0.1680 0.1570 -0.0329 0.0077  0.0124  75  LEU   A CG  
1592 C CD1 . LEU   A 75  ? 0.1958 0.2151 0.1728 -0.0396 0.0053  -0.0082 75  LEU   A CD1 
1593 C CD2 . LEU   A 75  ? 0.2112 0.2070 0.2217 -0.0128 0.0105  0.0222  75  LEU   A CD2 
1605 N N   . LYS   A 76  ? 0.1732 0.1358 0.1666 -0.0021 0.0161  -0.0034 76  LYS   A N   
1606 C CA  . LYS   A 76  ? 0.1706 0.1619 0.1680 -0.0049 0.0192  -0.0191 76  LYS   A CA  
1607 C C   . LYS   A 76  ? 0.1639 0.1430 0.1477 -0.0022 0.0186  -0.0016 76  LYS   A C   
1608 O O   . LYS   A 76  ? 0.1667 0.1388 0.1399 0.0017  0.0187  0.0097  76  LYS   A O   
1609 C CB  . LYS   A 76  ? 0.1710 0.1892 0.2222 0.0060  0.0207  -0.0505 76  LYS   A CB  
1610 C CG  . LYS   A 76  ? 0.1815 0.1815 0.2770 0.0114  0.0168  -0.0408 76  LYS   A CG  
1611 C CD  . LYS   A 76  ? 0.1876 0.1757 0.3232 0.0132  0.0007  -0.0451 76  LYS   A CD  
1612 C CE  . LYS   A 76  ? 0.2065 0.1915 0.3756 -0.0002 0.0054  -0.0564 76  LYS   A CE  
1613 N NZ  . LYS   A 76  ? 0.2121 0.1878 0.4102 -0.0144 0.0024  -0.0669 76  LYS   A NZ  
1627 N N   . VAL   A 77  ? 0.1749 0.1425 0.1483 0.0002  0.0279  0.0060  77  VAL   A N   
1628 C CA  . VAL   A 77  ? 0.1734 0.1498 0.1402 0.0082  0.0168  0.0107  77  VAL   A CA  
1629 C C   . VAL   A 77  ? 0.1684 0.1451 0.1368 0.0092  0.0129  0.0036  77  VAL   A C   
1630 O O   . VAL   A 77  ? 0.1766 0.1481 0.1421 0.0147  0.0305  -0.0069 77  VAL   A O   
1631 C CB  . VAL   A 77  ? 0.1868 0.1651 0.1506 0.0086  0.0190  0.0195  77  VAL   A CB  
1632 C CG1 . VAL   A 77  ? 0.1853 0.1830 0.1680 0.0170  0.0064  0.0041  77  VAL   A CG1 
1633 C CG2 . VAL   A 77  ? 0.2145 0.1761 0.1807 0.0034  0.0103  0.0183  77  VAL   A CG2 
1643 N N   . GLY   A 78  ? 0.1637 0.1370 0.1346 0.0093  0.0245  0.0079  78  GLY   A N   
1644 C CA  . GLY   A 78  ? 0.1638 0.1373 0.1425 0.0010  0.0262  0.0089  78  GLY   A CA  
1645 C C   . GLY   A 78  ? 0.1510 0.1332 0.1304 0.0058  0.0296  0.0060  78  GLY   A C   
1646 O O   . GLY   A 78  ? 0.1464 0.1411 0.1649 0.0021  0.0221  0.0241  78  GLY   A O   
1650 N N   . GLY   A 79  ? 0.1556 0.1257 0.1387 0.0002  0.0137  0.0103  79  GLY   A N   
1651 C CA  . GLY   A 79  ? 0.1525 0.1339 0.1510 -0.0013 0.0156  0.0067  79  GLY   A CA  
1652 C C   . GLY   A 79  ? 0.1406 0.1311 0.1450 -0.0000 0.0156  -0.0011 79  GLY   A C   
1653 O O   . GLY   A 79  ? 0.1417 0.1370 0.1607 0.0176  0.0165  -0.0007 79  GLY   A O   
1657 N N   . SER   A 80  ? 0.1349 0.1442 0.1668 -0.0014 0.0159  -0.0054 80  SER   A N   
1658 C CA  . SER   A 80  ? 0.1348 0.1331 0.1583 -0.0048 0.0108  0.0031  80  SER   A CA  
1659 C C   . SER   A 80  ? 0.1329 0.1378 0.1477 -0.0078 0.0100  0.0123  80  SER   A C   
1660 O O   . SER   A 80  ? 0.1295 0.1583 0.1889 0.0056  0.0106  -0.0030 80  SER   A O   
1661 C CB  . SER   A 80  ? 0.1478 0.1362 0.1826 -0.0048 0.0129  0.0091  80  SER   A CB  
1662 O OG  . SER   A 80  ? 0.1744 0.1402 0.2205 0.0043  -0.0057 0.0220  80  SER   A OG  
1668 N N   . CYS   A 81  ? 0.1255 0.1396 0.1520 0.0012  0.0012  0.0135  81  CYS   A N   
1669 C CA  . CYS   A 81  ? 0.1273 0.1480 0.1506 -0.0092 -0.0047 0.0190  81  CYS   A CA  
1670 C C   . CYS   A 81  ? 0.1262 0.1395 0.1569 -0.0077 0.0004  0.0299  81  CYS   A C   
1671 O O   . CYS   A 81  ? 0.1274 0.1650 0.1708 0.0014  0.0006  0.0308  81  CYS   A O   
1672 C CB  . CYS   A 81  ? 0.1376 0.1528 0.1704 -0.0141 0.0015  0.0192  81  CYS   A CB  
1673 S SG  . CYS   A 81  ? 0.1460 0.1400 0.1712 -0.0128 0.0025  0.0128  81  CYS   A SG  
1679 N N   . VAL   A 82  ? 0.1262 0.1420 0.1561 -0.0004 -0.0058 0.0168  82  VAL   A N   
1680 C CA  . VAL   A 82  ? 0.1393 0.1552 0.1566 -0.0049 -0.0038 0.0229  82  VAL   A CA  
1681 C C   . VAL   A 82  ? 0.1361 0.1589 0.1625 -0.0082 -0.0111 0.0242  82  VAL   A C   
1682 O O   . VAL   A 82  ? 0.1361 0.1624 0.1843 -0.0085 -0.0060 -0.0021 82  VAL   A O   
1683 C CB  . VAL   A 82  ? 0.1691 0.1663 0.1674 0.0016  0.0013  0.0295  82  VAL   A CB  
1684 C CG1 . VAL   A 82  ? 0.1895 0.1787 0.1950 0.0038  0.0031  0.0262  82  VAL   A CG1 
1685 C CG2 . VAL   A 82  ? 0.1751 0.1706 0.1973 -0.0020 -0.0048 0.0242  82  VAL   A CG2 
1695 N N   . LEU   A 83  ? 0.1279 0.1510 0.1526 -0.0096 -0.0128 0.0117  83  LEU   A N   
1696 C CA  . LEU   A 83  ? 0.1368 0.1503 0.1468 -0.0079 -0.0119 0.0077  83  LEU   A CA  
1697 C C   . LEU   A 83  ? 0.1406 0.1568 0.1469 -0.0094 -0.0127 0.0088  83  LEU   A C   
1698 O O   . LEU   A 83  ? 0.1454 0.1595 0.1516 -0.0196 -0.0046 0.0164  83  LEU   A O   
1699 C CB  . LEU   A 83  ? 0.1453 0.1591 0.1641 -0.0117 -0.0130 0.0124  83  LEU   A CB  
1700 C CG  . LEU   A 83  ? 0.1547 0.1693 0.1633 -0.0146 0.0074  0.0025  83  LEU   A CG  
1701 C CD1 . LEU   A 83  ? 0.1709 0.1770 0.1821 -0.0275 0.0041  0.0243  83  LEU   A CD1 
1702 C CD2 . LEU   A 83  ? 0.1553 0.1844 0.1803 -0.0103 0.0193  0.0065  83  LEU   A CD2 
1714 N N   . SER   A 84  ? 0.1551 0.1616 0.1392 -0.0144 -0.0105 0.0142  84  SER   A N   
1715 C CA  . SER   A 84  ? 0.1654 0.1667 0.1390 -0.0168 -0.0161 0.0140  84  SER   A CA  
1716 C C   . SER   A 84  ? 0.1694 0.1627 0.1278 -0.0201 0.0003  0.0103  84  SER   A C   
1717 O O   . SER   A 84  ? 0.1629 0.1728 0.1292 -0.0130 -0.0053 0.0066  84  SER   A O   
1718 C CB  . SER   A 84  ? 0.1683 0.1891 0.1456 -0.0188 -0.0108 0.0016  84  SER   A CB  
1719 O OG  . SER   A 84  ? 0.1758 0.2084 0.1495 -0.0169 -0.0157 -0.0064 84  SER   A OG  
1725 N N   . GLY   A 85  ? 0.1828 0.1802 0.1326 -0.0219 0.0045  0.0078  85  GLY   A N   
1726 C CA  . GLY   A 85  ? 0.1822 0.1879 0.1475 -0.0217 0.0092  -0.0041 85  GLY   A CA  
1727 C C   . GLY   A 85  ? 0.1764 0.1939 0.1356 -0.0218 -0.0058 -0.0024 85  GLY   A C   
1728 O O   . GLY   A 85  ? 0.1773 0.2029 0.1466 -0.0341 0.0135  -0.0113 85  GLY   A O   
1732 N N   . HIS   A 86  ? 0.1787 0.1873 0.1320 -0.0202 -0.0070 0.0010  86  HIS   A N   
1733 C CA  . HIS   A 86  ? 0.1948 0.1901 0.1258 -0.0248 -0.0069 -0.0004 86  HIS   A CA  
1734 C C   . HIS   A 86  ? 0.2149 0.2033 0.1269 -0.0255 -0.0125 0.0033  86  HIS   A C   
1735 O O   . HIS   A 86  ? 0.2194 0.2273 0.1333 -0.0196 0.0026  -0.0024 86  HIS   A O   
1736 C CB  . HIS   A 86  ? 0.1931 0.1804 0.1318 -0.0131 0.0055  -0.0012 86  HIS   A CB  
1737 C CG  . HIS   A 86  ? 0.1851 0.1832 0.1425 -0.0058 0.0024  0.0047  86  HIS   A CG  
1738 N ND1 . HIS   A 86  ? 0.1920 0.1801 0.1892 -0.0180 0.0011  0.0031  86  HIS   A ND1 
1739 C CD2 . HIS   A 86  ? 0.1857 0.1758 0.1348 0.0039  0.0130  0.0104  86  HIS   A CD2 
1740 C CE1 . HIS   A 86  ? 0.1882 0.1824 0.1764 -0.0101 0.0188  0.0114  86  HIS   A CE1 
1741 N NE2 . HIS   A 86  ? 0.1870 0.1749 0.1484 0.0017  0.0150  0.0242  86  HIS   A NE2 
1749 N N   . ASN   A 87  ? 0.2285 0.2083 0.1361 -0.0243 0.0180  -0.0053 87  ASN   A N   
1750 C CA  . ASN   A 87  ? 0.2451 0.2236 0.1444 -0.0169 0.0434  -0.0155 87  ASN   A CA  
1751 C C   . ASN   A 87  ? 0.2432 0.2403 0.1800 -0.0267 0.0638  -0.0036 87  ASN   A C   
1752 O O   . ASN   A 87  ? 0.2659 0.2604 0.2245 -0.0387 0.0921  -0.0200 87  ASN   A O   
1753 C CB  . ASN   A 87  ? 0.2659 0.2266 0.1536 -0.0062 0.0450  -0.0265 87  ASN   A CB  
1754 C CG  . ASN   A 87  ? 0.2775 0.2374 0.1621 0.0023  0.0599  -0.0162 87  ASN   A CG  
1755 O OD1 . ASN   A 87  ? 0.2953 0.2389 0.1683 0.0225  0.0535  -0.0039 87  ASN   A OD1 
1756 N ND2 . ASN   A 87  ? 0.2793 0.2635 0.1710 0.0019  0.0581  -0.0140 87  ASN   A ND2 
1763 N N   . LEU   A 88  ? 0.2190 0.2268 0.1716 -0.0319 0.0341  0.0082  88  LEU   A N   
1764 C CA  . LEU   A 88  ? 0.1989 0.2256 0.1868 -0.0345 0.0300  0.0253  88  LEU   A CA  
1765 C C   . LEU   A 88  ? 0.1956 0.2324 0.1560 -0.0374 0.0295  0.0350  88  LEU   A C   
1766 O O   . LEU   A 88  ? 0.2052 0.2376 0.2022 -0.0340 0.0319  0.0493  88  LEU   A O   
1767 C CB  . LEU   A 88  ? 0.2013 0.2331 0.2038 -0.0394 -0.0060 0.0375  88  LEU   A CB  
1768 C CG  . LEU   A 88  ? 0.2175 0.2487 0.2289 -0.0342 -0.0131 0.0360  88  LEU   A CG  
1769 C CD1 . LEU   A 88  ? 0.2281 0.2541 0.2166 -0.0323 -0.0193 0.0236  88  LEU   A CD1 
1770 C CD2 . LEU   A 88  ? 0.2275 0.2582 0.2706 -0.0284 -0.0044 0.0268  88  LEU   A CD2 
1782 N N   . ALA   A 89  ? 0.1931 0.2212 0.1381 -0.0330 0.0202  0.0057  89  ALA   A N   
1783 C CA  . ALA   A 89  ? 0.2031 0.2186 0.1262 -0.0261 0.0101  0.0121  89  ALA   A CA  
1784 C C   . ALA   A 89  ? 0.2133 0.2236 0.1407 -0.0247 -0.0049 0.0127  89  ALA   A C   
1785 O O   . ALA   A 89  ? 0.2074 0.2179 0.1722 -0.0286 -0.0104 -0.0124 89  ALA   A O   
1786 C CB  . ALA   A 89  ? 0.2001 0.2156 0.1270 -0.0209 0.0048  0.0226  89  ALA   A CB  
1792 N N   . LYS   A 90  ? 0.2263 0.2389 0.1360 -0.0384 -0.0241 0.0160  90  LYS   A N   
1793 C CA  . LYS   A 90  ? 0.2353 0.2526 0.1463 -0.0293 -0.0353 0.0175  90  LYS   A CA  
1794 C C   . LYS   A 90  ? 0.2069 0.2343 0.1402 -0.0240 -0.0333 0.0032  90  LYS   A C   
1795 O O   . LYS   A 90  ? 0.2120 0.2487 0.1781 -0.0247 -0.0357 -0.0120 90  LYS   A O   
1796 C CB  . LYS   A 90  ? 0.2608 0.2881 0.1785 -0.0257 -0.0469 0.0424  90  LYS   A CB  
1797 C CG  . LYS   A 90  ? 0.3017 0.3223 0.2796 -0.0232 -0.0472 0.0467  90  LYS   A CG  
1798 C CD  . LYS   A 90  ? 0.3497 0.3618 0.3879 -0.0265 -0.0304 0.0487  90  LYS   A CD  
1799 C CE  . LYS   A 90  ? 0.3834 0.3952 0.4709 -0.0291 -0.0157 0.0438  90  LYS   A CE  
1800 N NZ  . LYS   A 90  ? 0.4004 0.4085 0.5248 -0.0298 -0.0076 0.0377  90  LYS   A NZ  
1814 N N   . HIS   A 91  ? 0.1894 0.2052 0.1153 -0.0240 -0.0375 0.0215  91  HIS   A N   
1815 C CA  . HIS   A 91  ? 0.1788 0.1844 0.1276 -0.0191 -0.0339 0.0191  91  HIS   A CA  
1816 C C   . HIS   A 91  ? 0.1617 0.1702 0.1157 -0.0162 -0.0158 0.0208  91  HIS   A C   
1817 O O   . HIS   A 91  ? 0.1594 0.1837 0.1257 -0.0225 -0.0033 0.0223  91  HIS   A O   
1818 C CB  . HIS   A 91  ? 0.1922 0.2081 0.1811 0.0034  -0.0436 0.0240  91  HIS   A CB  
1819 C CG  . HIS   A 91  ? 0.2429 0.2608 0.2580 0.0166  -0.0692 0.0081  91  HIS   A CG  
1820 N ND1 . HIS   A 91  ? 0.2550 0.2894 0.2976 0.0242  -0.0807 -0.0121 91  HIS   A ND1 
1821 C CD2 . HIS   A 91  ? 0.2681 0.2809 0.2800 0.0253  -0.0888 0.0151  91  HIS   A CD2 
1822 C CE1 . HIS   A 91  ? 0.2676 0.2975 0.3130 0.0248  -0.0831 0.0030  91  HIS   A CE1 
1823 N NE2 . HIS   A 91  ? 0.2802 0.2971 0.3052 0.0295  -0.0958 0.0106  91  HIS   A NE2 
1831 N N   . CYS   A 92  ? 0.1484 0.1603 0.1283 -0.0201 -0.0113 0.0219  92  CYS   A N   
1832 C CA  . CYS   A 92  ? 0.1414 0.1560 0.1308 -0.0127 -0.0053 0.0157  92  CYS   A CA  
1833 C C   . CYS   A 92  ? 0.1342 0.1528 0.1302 -0.0148 0.0020  0.0110  92  CYS   A C   
1834 O O   . CYS   A 92  ? 0.1397 0.1570 0.1466 -0.0206 -0.0052 0.0062  92  CYS   A O   
1835 C CB  . CYS   A 92  ? 0.1418 0.1542 0.1400 -0.0051 -0.0058 0.0144  92  CYS   A CB  
1836 S SG  . CYS   A 92  ? 0.1438 0.1424 0.1419 -0.0126 -0.0045 0.0099  92  CYS   A SG  
1842 N N   . LEU   A 93  ? 0.1371 0.1374 0.1321 -0.0148 0.0026  0.0112  93  LEU   A N   
1843 C CA  . LEU   A 93  ? 0.1264 0.1335 0.1334 -0.0096 -0.0032 0.0119  93  LEU   A CA  
1844 C C   . LEU   A 93  ? 0.1254 0.1282 0.1158 -0.0037 0.0041  0.0043  93  LEU   A C   
1845 O O   . LEU   A 93  ? 0.1240 0.1352 0.1217 -0.0049 -0.0013 0.0105  93  LEU   A O   
1846 C CB  . LEU   A 93  ? 0.1291 0.1384 0.1490 -0.0056 -0.0097 0.0203  93  LEU   A CB  
1847 C CG  . LEU   A 93  ? 0.1388 0.1371 0.1453 -0.0092 -0.0014 0.0187  93  LEU   A CG  
1848 C CD1 . LEU   A 93  ? 0.1464 0.1395 0.1784 -0.0023 0.0104  0.0059  93  LEU   A CD1 
1849 C CD2 . LEU   A 93  ? 0.1503 0.1369 0.1716 -0.0104 -0.0068 0.0144  93  LEU   A CD2 
1861 N N   . HIS   A 94  ? 0.1157 0.1241 0.1323 -0.0022 0.0073  0.0140  94  HIS   A N   
1862 C CA  . HIS   A 94  ? 0.1179 0.1233 0.1261 -0.0043 0.0023  0.0175  94  HIS   A CA  
1863 C C   . HIS   A 94  ? 0.1207 0.1171 0.1356 -0.0040 0.0027  0.0065  94  HIS   A C   
1864 O O   . HIS   A 94  ? 0.1276 0.1400 0.1631 -0.0005 0.0016  -0.0097 94  HIS   A O   
1865 C CB  . HIS   A 94  ? 0.1201 0.1234 0.1365 -0.0025 -0.0019 0.0134  94  HIS   A CB  
1866 C CG  . HIS   A 94  ? 0.1253 0.1207 0.1274 -0.0058 -0.0016 0.0158  94  HIS   A CG  
1867 N ND1 . HIS   A 94  ? 0.1276 0.1208 0.1340 -0.0034 0.0026  0.0132  94  HIS   A ND1 
1868 C CD2 . HIS   A 94  ? 0.1281 0.1343 0.1415 -0.0041 -0.0069 0.0073  94  HIS   A CD2 
1869 C CE1 . HIS   A 94  ? 0.1335 0.1258 0.1266 -0.0063 -0.0085 0.0067  94  HIS   A CE1 
1870 N NE2 . HIS   A 94  ? 0.1338 0.1276 0.1444 -0.0091 -0.0021 0.0059  94  HIS   A NE2 
1878 N N   . VAL   A 95  ? 0.1156 0.1176 0.1203 -0.0026 0.0060  0.0028  95  VAL   A N   
1879 C CA  . VAL   A 95  ? 0.1257 0.1219 0.1297 -0.0064 0.0078  0.0117  95  VAL   A CA  
1880 C C   . VAL   A 95  ? 0.1242 0.1125 0.1216 -0.0108 0.0031  0.0083  95  VAL   A C   
1881 O O   . VAL   A 95  ? 0.1321 0.1325 0.1210 0.0076  0.0084  0.0044  95  VAL   A O   
1882 C CB  . VAL   A 95  ? 0.1292 0.1262 0.1438 -0.0112 0.0088  0.0110  95  VAL   A CB  
1883 C CG1 . VAL   A 95  ? 0.1420 0.1294 0.1495 -0.0144 0.0067  -0.0023 95  VAL   A CG1 
1884 C CG2 . VAL   A 95  ? 0.1341 0.1282 0.1406 -0.0166 0.0077  0.0196  95  VAL   A CG2 
1894 N N   . VAL   A 96  ? 0.1315 0.1191 0.1115 -0.0064 0.0079  0.0049  96  VAL   A N   
1895 C CA  . VAL   A 96  ? 0.1381 0.1270 0.1244 0.0010  0.0087  0.0143  96  VAL   A CA  
1896 C C   . VAL   A 96  ? 0.1398 0.1331 0.1220 0.0026  0.0138  0.0160  96  VAL   A C   
1897 O O   . VAL   A 96  ? 0.1441 0.1381 0.1479 -0.0009 0.0188  -0.0039 96  VAL   A O   
1898 C CB  . VAL   A 96  ? 0.1421 0.1322 0.1311 -0.0033 0.0241  0.0129  96  VAL   A CB  
1899 C CG1 . VAL   A 96  ? 0.1521 0.1440 0.1228 -0.0044 0.0215  0.0131  96  VAL   A CG1 
1900 C CG2 . VAL   A 96  ? 0.1405 0.1388 0.1553 -0.0136 0.0151  0.0103  96  VAL   A CG2 
1910 N N   . GLY   A 97  ? 0.1378 0.1308 0.1315 -0.0033 0.0093  0.0137  97  GLY   A N   
1911 C CA  . GLY   A 97  ? 0.1504 0.1450 0.1376 -0.0046 -0.0012 0.0129  97  GLY   A CA  
1912 C C   . GLY   A 97  ? 0.1515 0.1612 0.1173 -0.0077 0.0028  0.0119  97  GLY   A C   
1913 O O   . GLY   A 97  ? 0.1646 0.1574 0.1389 -0.0075 0.0084  0.0185  97  GLY   A O   
1917 N N   . PRO   A 98  ? 0.1504 0.1674 0.1166 0.0001  0.0014  0.0180  98  PRO   A N   
1918 C CA  . PRO   A 98  ? 0.1628 0.1880 0.1279 -0.0081 0.0039  0.0082  98  PRO   A CA  
1919 C C   . PRO   A 98  ? 0.1732 0.2022 0.1128 -0.0130 -0.0004 0.0253  98  PRO   A C   
1920 O O   . PRO   A 98  ? 0.1669 0.1817 0.1403 -0.0083 -0.0003 0.0258  98  PRO   A O   
1921 C CB  . PRO   A 98  ? 0.1754 0.1975 0.1152 -0.0018 -0.0010 -0.0078 98  PRO   A CB  
1922 C CG  . PRO   A 98  ? 0.1746 0.1866 0.1315 0.0035  -0.0005 -0.0170 98  PRO   A CG  
1923 C CD  . PRO   A 98  ? 0.1611 0.1634 0.1222 0.0035  0.0014  0.0017  98  PRO   A CD  
1931 N N   A ASN   A 99  ? 0.1756 0.2225 0.1165 -0.0139 0.0117  0.0430  99  ASN   A N   
1932 N N   B ASN   A 99  ? 0.1898 0.2101 0.1294 -0.0067 -0.0077 0.0463  99  ASN   A N   
1933 C CA  A ASN   A 99  ? 0.1943 0.2355 0.1238 -0.0173 -0.0003 0.0609  99  ASN   A CA  
1934 C CA  B ASN   A 99  ? 0.2113 0.2151 0.1489 -0.0006 -0.0216 0.0652  99  ASN   A CA  
1935 C C   A ASN   A 99  ? 0.2062 0.2692 0.1124 -0.0360 0.0060  0.0651  99  ASN   A C   
1936 C C   B ASN   A 99  ? 0.2310 0.2208 0.1579 -0.0064 -0.0223 0.0663  99  ASN   A C   
1937 O O   A ASN   A 99  ? 0.2181 0.2813 0.1243 -0.0348 0.0000  0.0567  99  ASN   A O   
1938 O O   B ASN   A 99  ? 0.2354 0.2077 0.1630 -0.0060 -0.0335 0.0569  99  ASN   A O   
1939 C CB  A ASN   A 99  ? 0.1950 0.2223 0.1308 -0.0167 -0.0106 0.0627  99  ASN   A CB  
1940 C CB  B ASN   A 99  ? 0.2132 0.2209 0.1873 0.0034  -0.0351 0.0708  99  ASN   A CB  
1941 C CG  A ASN   A 99  ? 0.1998 0.2173 0.1399 -0.0125 -0.0327 0.0405  99  ASN   A CG  
1942 C CG  B ASN   A 99  ? 0.2142 0.2262 0.2134 0.0060  -0.0465 0.0788  99  ASN   A CG  
1943 O OD1 A ASN   A 99  ? 0.2134 0.2267 0.1358 -0.0027 -0.0355 0.0293  99  ASN   A OD1 
1944 O OD1 B ASN   A 99  ? 0.2228 0.2329 0.2078 -0.0030 -0.0493 0.0821  99  ASN   A OD1 
1945 N ND2 A ASN   A 99  ? 0.1989 0.2142 0.1591 -0.0099 -0.0302 0.0399  99  ASN   A ND2 
1946 N ND2 B ASN   A 99  ? 0.2096 0.2284 0.2219 0.0183  -0.0558 0.0758  99  ASN   A ND2 
1959 N N   A VAL   A 100 ? 0.2157 0.2853 0.1207 -0.0561 -0.0229 0.0541  100 VAL   A N   
1960 N N   B VAL   A 100 ? 0.2477 0.2435 0.1832 -0.0148 -0.0196 0.0661  100 VAL   A N   
1961 C CA  A VAL   A 100 ? 0.2386 0.3065 0.1477 -0.0660 -0.0255 0.0502  100 VAL   A CA  
1962 C CA  B VAL   A 100 ? 0.2648 0.2686 0.2136 -0.0239 -0.0144 0.0605  100 VAL   A CA  
1963 C C   A VAL   A 100 ? 0.2392 0.3203 0.1305 -0.0811 -0.0328 0.0737  100 VAL   A C   
1964 C C   B VAL   A 100 ? 0.2790 0.2912 0.2256 -0.0285 -0.0207 0.0705  100 VAL   A C   
1965 O O   A VAL   A 100 ? 0.2475 0.3286 0.1635 -0.0811 -0.0123 0.0689  100 VAL   A O   
1966 O O   B VAL   A 100 ? 0.2823 0.2995 0.2316 -0.0332 -0.0202 0.0649  100 VAL   A O   
1967 C CB  A VAL   A 100 ? 0.2638 0.3063 0.1827 -0.0704 -0.0338 0.0454  100 VAL   A CB  
1968 C CB  B VAL   A 100 ? 0.2699 0.2722 0.2311 -0.0249 -0.0120 0.0459  100 VAL   A CB  
1969 C CG1 A VAL   A 100 ? 0.2662 0.3113 0.2082 -0.0715 -0.0291 0.0408  100 VAL   A CG1 
1970 C CG1 B VAL   A 100 ? 0.2687 0.2733 0.2404 -0.0271 -0.0087 0.0428  100 VAL   A CG1 
1971 C CG2 A VAL   A 100 ? 0.2812 0.3086 0.1966 -0.0715 -0.0351 0.0436  100 VAL   A CG2 
1972 C CG2 B VAL   A 100 ? 0.2751 0.2750 0.2398 -0.0258 -0.0133 0.0363  100 VAL   A CG2 
1991 N N   A ASN   A 101 ? 0.2437 0.3301 0.1631 -0.0881 -0.0410 0.1017  101 ASN   A N   
1992 N N   B ASN   A 101 ? 0.2874 0.3031 0.2398 -0.0252 -0.0293 0.0826  101 ASN   A N   
1993 C CA  A ASN   A 101 ? 0.2725 0.3472 0.1916 -0.0889 -0.0473 0.1191  101 ASN   A CA  
1994 C CA  B ASN   A 101 ? 0.2950 0.3125 0.2504 -0.0245 -0.0365 0.0913  101 ASN   A CA  
1995 C C   A ASN   A 101 ? 0.2980 0.3745 0.2172 -0.0893 -0.0219 0.1461  101 ASN   A C   
1996 C C   B ASN   A 101 ? 0.3063 0.3288 0.2564 -0.0234 -0.0263 0.1101  101 ASN   A C   
1997 O O   A ASN   A 101 ? 0.3180 0.3777 0.2575 -0.0886 -0.0232 0.1354  101 ASN   A O   
1998 O O   B ASN   A 101 ? 0.3067 0.3229 0.2377 -0.0246 -0.0254 0.1335  101 ASN   A O   
1999 C CB  A ASN   A 101 ? 0.2805 0.3374 0.1987 -0.0822 -0.0651 0.1076  101 ASN   A CB  
2000 C CB  B ASN   A 101 ? 0.2923 0.3026 0.2490 -0.0279 -0.0479 0.0792  101 ASN   A CB  
2001 C CG  A ASN   A 101 ? 0.2883 0.3256 0.1984 -0.0820 -0.0668 0.0824  101 ASN   A CG  
2002 C CG  B ASN   A 101 ? 0.2904 0.2937 0.2450 -0.0307 -0.0500 0.0636  101 ASN   A CG  
2003 O OD1 A ASN   A 101 ? 0.2889 0.3319 0.2019 -0.0733 -0.0583 0.0460  101 ASN   A OD1 
2004 O OD1 B ASN   A 101 ? 0.2868 0.2900 0.2378 -0.0314 -0.0496 0.0523  101 ASN   A OD1 
2005 N ND2 A ASN   A 101 ? 0.2961 0.3129 0.2079 -0.0873 -0.0643 0.0875  101 ASN   A ND2 
2006 N ND2 B ASN   A 101 ? 0.2935 0.2902 0.2519 -0.0325 -0.0498 0.0595  101 ASN   A ND2 
2019 N N   A LYS   A 102 ? 0.3005 0.4115 0.2540 -0.1012 0.0010  0.1472  102 LYS   A N   
2020 N N   B LYS   A 102 ? 0.3183 0.3505 0.2984 -0.0232 -0.0110 0.0923  102 LYS   A N   
2021 C CA  A LYS   A 102 ? 0.3125 0.4409 0.2552 -0.1012 0.0054  0.1468  102 LYS   A CA  
2022 C CA  B LYS   A 102 ? 0.3292 0.3676 0.3193 -0.0243 0.0004  0.0749  102 LYS   A CA  
2023 C C   A LYS   A 102 ? 0.3239 0.4672 0.2332 -0.0877 0.0181  0.1381  102 LYS   A C   
2024 C C   B LYS   A 102 ? 0.3319 0.3741 0.3079 -0.0252 0.0067  0.0746  102 LYS   A C   
2025 O O   A LYS   A 102 ? 0.3297 0.4833 0.2433 -0.0822 0.0323  0.1235  102 LYS   A O   
2026 O O   B LYS   A 102 ? 0.3334 0.3782 0.3065 -0.0269 0.0103  0.0802  102 LYS   A O   
2027 C CB  A LYS   A 102 ? 0.3193 0.4438 0.2875 -0.1083 -0.0039 0.1359  102 LYS   A CB  
2028 C CB  B LYS   A 102 ? 0.3366 0.3771 0.3424 -0.0254 0.0069  0.0581  102 LYS   A CB  
2029 C CG  A LYS   A 102 ? 0.3288 0.4470 0.3161 -0.1104 -0.0191 0.1179  102 LYS   A CG  
2030 C CG  B LYS   A 102 ? 0.3429 0.3842 0.3580 -0.0274 0.0116  0.0427  102 LYS   A CG  
2031 C CD  A LYS   A 102 ? 0.3408 0.4511 0.3471 -0.1117 -0.0324 0.0943  102 LYS   A CD  
2032 C CD  B LYS   A 102 ? 0.3494 0.3910 0.3715 -0.0284 0.0160  0.0279  102 LYS   A CD  
2033 C CE  A LYS   A 102 ? 0.3537 0.4556 0.3714 -0.1087 -0.0444 0.0784  102 LYS   A CE  
2034 C CE  B LYS   A 102 ? 0.3539 0.3968 0.3817 -0.0280 0.0181  0.0158  102 LYS   A CE  
2035 N NZ  A LYS   A 102 ? 0.3582 0.4555 0.3856 -0.1139 -0.0449 0.0675  102 LYS   A NZ  
2036 N NZ  B LYS   A 102 ? 0.3568 0.4009 0.3869 -0.0275 0.0210  0.0070  102 LYS   A NZ  
2063 N N   A GLY   A 103 ? 0.3273 0.4794 0.2444 -0.0742 0.0085  0.1124  103 GLY   A N   
2064 N N   B GLY   A 103 ? 0.3309 0.3759 0.3006 -0.0221 0.0043  0.0643  103 GLY   A N   
2065 C CA  A GLY   A 103 ? 0.3301 0.4862 0.2328 -0.0605 0.0142  0.0921  103 GLY   A CA  
2066 C CA  B GLY   A 103 ? 0.3279 0.3735 0.2786 -0.0214 0.0046  0.0593  103 GLY   A CA  
2067 C C   A GLY   A 103 ? 0.3304 0.4919 0.2371 -0.0515 0.0279  0.0695  103 GLY   A C   
2068 C C   B GLY   A 103 ? 0.3242 0.3709 0.2605 -0.0223 0.0044  0.0524  103 GLY   A C   
2069 O O   A GLY   A 103 ? 0.3424 0.5015 0.2565 -0.0473 0.0330  0.0518  103 GLY   A O   
2070 O O   B GLY   A 103 ? 0.3221 0.3707 0.2552 -0.0266 0.0081  0.0549  103 GLY   A O   
2077 N N   A GLU   A 104 ? 0.3139 0.4823 0.1896 -0.0505 0.0340  0.0612  104 GLU   A N   
2078 N N   B GLU   A 104 ? 0.3214 0.3675 0.2431 -0.0176 -0.0031 0.0415  104 GLU   A N   
2079 C CA  A GLU   A 104 ? 0.2930 0.4698 0.1620 -0.0546 0.0358  0.0407  104 GLU   A CA  
2080 C CA  B GLU   A 104 ? 0.3157 0.3620 0.2276 -0.0156 -0.0104 0.0299  104 GLU   A CA  
2081 C C   A GLU   A 104 ? 0.2957 0.4783 0.1551 -0.0556 0.0428  0.0156  104 GLU   A C   
2082 C C   B GLU   A 104 ? 0.3170 0.3640 0.2281 -0.0139 -0.0085 0.0163  104 GLU   A C   
2083 O O   A GLU   A 104 ? 0.2864 0.4816 0.1833 -0.0599 0.0275  0.0085  104 GLU   A O   
2084 O O   B GLU   A 104 ? 0.3138 0.3598 0.2256 -0.0144 -0.0111 0.0187  104 GLU   A O   
2085 C CB  A GLU   A 104 ? 0.2625 0.4372 0.1443 -0.0587 0.0389  0.0588  104 GLU   A CB  
2086 C CB  B GLU   A 104 ? 0.3069 0.3549 0.2182 -0.0146 -0.0179 0.0346  104 GLU   A CB  
2087 C CG  A GLU   A 104 ? 0.2438 0.4184 0.1537 -0.0616 0.0280  0.0729  104 GLU   A CG  
2088 C CG  B GLU   A 104 ? 0.3017 0.3493 0.2208 -0.0114 -0.0268 0.0399  104 GLU   A CG  
2089 C CD  A GLU   A 104 ? 0.2237 0.3946 0.1617 -0.0635 0.0259  0.0778  104 GLU   A CD  
2090 C CD  B GLU   A 104 ? 0.2968 0.3443 0.2202 -0.0080 -0.0325 0.0442  104 GLU   A CD  
2091 O OE1 A GLU   A 104 ? 0.1993 0.3765 0.1307 -0.0621 0.0123  0.0707  104 GLU   A OE1 
2092 O OE1 B GLU   A 104 ? 0.2943 0.3410 0.2159 -0.0063 -0.0365 0.0489  104 GLU   A OE1 
2093 O OE2 A GLU   A 104 ? 0.2386 0.3893 0.1821 -0.0678 0.0173  0.1004  104 GLU   A OE2 
2094 O OE2 B GLU   A 104 ? 0.2971 0.3433 0.2242 -0.0067 -0.0366 0.0439  104 GLU   A OE2 
2107 N N   A ASP   A 105 ? 0.3094 0.4812 0.1658 -0.0529 0.0547  -0.0143 105 ASP   A N   
2108 N N   B ASP   A 105 ? 0.3234 0.3708 0.2427 -0.0139 -0.0043 -0.0022 105 ASP   A N   
2109 C CA  A ASP   A 105 ? 0.3150 0.4784 0.2127 -0.0449 0.0579  -0.0470 105 ASP   A CA  
2110 C CA  B ASP   A 105 ? 0.3273 0.3767 0.2657 -0.0124 -0.0004 -0.0209 105 ASP   A CA  
2111 C C   A ASP   A 105 ? 0.2776 0.4547 0.1716 -0.0551 0.0438  -0.0683 105 ASP   A C   
2112 C C   B ASP   A 105 ? 0.3205 0.3741 0.2592 -0.0188 0.0017  -0.0257 105 ASP   A C   
2113 O O   A ASP   A 105 ? 0.2500 0.4180 0.1445 -0.0515 0.0360  -0.0883 105 ASP   A O   
2114 O O   B ASP   A 105 ? 0.3168 0.3755 0.2457 -0.0200 0.0014  -0.0309 105 ASP   A O   
2115 C CB  A ASP   A 105 ? 0.3504 0.5033 0.2994 -0.0311 0.0703  -0.0570 105 ASP   A CB  
2116 C CB  B ASP   A 105 ? 0.3357 0.3829 0.2957 -0.0067 0.0001  -0.0353 105 ASP   A CB  
2117 C CG  A ASP   A 105 ? 0.3799 0.5200 0.3703 -0.0184 0.0735  -0.0671 105 ASP   A CG  
2118 C CG  B ASP   A 105 ? 0.3419 0.3876 0.3204 -0.0023 -0.0040 -0.0482 105 ASP   A CG  
2119 O OD1 A ASP   A 105 ? 0.3890 0.5269 0.3830 -0.0176 0.0728  -0.0787 105 ASP   A OD1 
2120 O OD1 B ASP   A 105 ? 0.3445 0.3883 0.3195 -0.0024 -0.0072 -0.0561 105 ASP   A OD1 
2121 O OD2 A ASP   A 105 ? 0.3960 0.5259 0.4075 -0.0140 0.0769  -0.0634 105 ASP   A OD2 
2122 O OD2 B ASP   A 105 ? 0.3451 0.3908 0.3373 -0.0032 -0.0101 -0.0495 105 ASP   A OD2 
2131 N N   A ILE   A 106 ? 0.2644 0.4392 0.1833 -0.0634 0.0198  -0.0676 106 ILE   A N   
2132 N N   B ILE   A 106 ? 0.3165 0.3678 0.2664 -0.0244 -0.0003 -0.0291 106 ILE   A N   
2133 C CA  A ILE   A 106 ? 0.2409 0.4212 0.2016 -0.0790 -0.0035 -0.0811 106 ILE   A CA  
2134 C CA  B ILE   A 106 ? 0.3106 0.3604 0.2776 -0.0322 -0.0019 -0.0364 106 ILE   A CA  
2135 C C   A ILE   A 106 ? 0.2251 0.3914 0.2003 -0.0991 0.0009  -0.1032 106 ILE   A C   
2136 C C   B ILE   A 106 ? 0.3034 0.3472 0.2788 -0.0392 0.0078  -0.0499 106 ILE   A C   
2137 O O   A ILE   A 106 ? 0.2022 0.3774 0.2116 -0.1053 0.0205  -0.1022 106 ILE   A O   
2138 O O   B ILE   A 106 ? 0.2999 0.3436 0.2738 -0.0379 0.0094  -0.0553 106 ILE   A O   
2139 C CB  A ILE   A 106 ? 0.2406 0.4314 0.2552 -0.0690 -0.0339 -0.0540 106 ILE   A CB  
2140 C CB  B ILE   A 106 ? 0.3129 0.3663 0.2982 -0.0314 -0.0130 -0.0249 106 ILE   A CB  
2141 C CG1 A ILE   A 106 ? 0.2293 0.4301 0.2896 -0.0570 -0.0406 -0.0328 106 ILE   A CG1 
2142 C CG1 B ILE   A 106 ? 0.3113 0.3666 0.3137 -0.0293 -0.0180 -0.0159 106 ILE   A CG1 
2143 C CG2 A ILE   A 106 ? 0.2522 0.4373 0.2736 -0.0670 -0.0390 -0.0487 106 ILE   A CG2 
2144 C CG2 B ILE   A 106 ? 0.3157 0.3691 0.3021 -0.0316 -0.0156 -0.0224 106 ILE   A CG2 
2145 C CD1 A ILE   A 106 ? 0.2264 0.4271 0.3067 -0.0442 -0.0307 -0.0233 106 ILE   A CD1 
2146 C CD1 B ILE   A 106 ? 0.3114 0.3652 0.3219 -0.0261 -0.0179 -0.0119 106 ILE   A CD1 
2169 N N   A GLN   A 107 ? 0.2445 0.3757 0.2305 -0.0968 0.0097  -0.1183 107 GLN   A N   
2170 N N   B GLN   A 107 ? 0.3002 0.3361 0.2953 -0.0446 0.0193  -0.0576 107 GLN   A N   
2171 C CA  A GLN   A 107 ? 0.2735 0.3567 0.3279 -0.0770 0.0362  -0.1120 107 GLN   A CA  
2172 C CA  B GLN   A 107 ? 0.2959 0.3221 0.3258 -0.0455 0.0338  -0.0665 107 GLN   A CA  
2173 C C   A GLN   A 107 ? 0.2494 0.3037 0.3244 -0.0654 0.0589  -0.0851 107 GLN   A C   
2174 C C   B GLN   A 107 ? 0.2612 0.2885 0.3053 -0.0512 0.0502  -0.0688 107 GLN   A C   
2175 O O   A GLN   A 107 ? 0.2566 0.2980 0.3914 -0.0549 0.0664  -0.0799 107 GLN   A O   
2176 O O   B GLN   A 107 ? 0.2667 0.2875 0.3333 -0.0477 0.0522  -0.0653 107 GLN   A O   
2177 C CB  A GLN   A 107 ? 0.3169 0.3857 0.4249 -0.0777 0.0233  -0.1150 107 GLN   A CB  
2178 C CB  B GLN   A 107 ? 0.3227 0.3398 0.3787 -0.0435 0.0245  -0.0629 107 GLN   A CB  
2179 C CG  A GLN   A 107 ? 0.3635 0.4172 0.5296 -0.0720 0.0151  -0.1050 107 GLN   A CG  
2180 C CG  B GLN   A 107 ? 0.3467 0.3567 0.4359 -0.0411 0.0165  -0.0570 107 GLN   A CG  
2181 C CD  A GLN   A 107 ? 0.4000 0.4423 0.6212 -0.0670 0.0127  -0.0894 107 GLN   A CD  
2182 C CD  B GLN   A 107 ? 0.3676 0.3724 0.4866 -0.0371 0.0105  -0.0493 107 GLN   A CD  
2183 O OE1 A GLN   A 107 ? 0.4135 0.4501 0.6578 -0.0652 0.0122  -0.0864 107 GLN   A OE1 
2184 O OE1 B GLN   A 107 ? 0.3750 0.3780 0.5041 -0.0360 0.0103  -0.0447 107 GLN   A OE1 
2185 N NE2 A GLN   A 107 ? 0.4129 0.4528 0.6530 -0.0662 0.0101  -0.0861 107 GLN   A NE2 
2186 N NE2 B GLN   A 107 ? 0.3748 0.3783 0.5054 -0.0365 0.0077  -0.0506 107 GLN   A NE2 
2203 N N   . LEU   A 108 ? 0.2215 0.2550 0.2654 -0.0580 0.0588  -0.0788 108 LEU   A N   
2204 C CA  . LEU   A 108 ? 0.1909 0.1948 0.2186 -0.0212 0.0486  -0.0341 108 LEU   A CA  
2205 C C   . LEU   A 108 ? 0.1677 0.1524 0.2123 -0.0088 0.0378  -0.0020 108 LEU   A C   
2206 O O   . LEU   A 108 ? 0.1628 0.1553 0.2206 0.0043  0.0409  0.0093  108 LEU   A O   
2207 C CB  . LEU   A 108 ? 0.1920 0.2030 0.1960 -0.0243 0.0467  -0.0173 108 LEU   A CB  
2208 C CG  . LEU   A 108 ? 0.2103 0.2275 0.2173 -0.0255 0.0578  -0.0178 108 LEU   A CG  
2209 C CD1 . LEU   A 108 ? 0.2339 0.2370 0.2165 -0.0336 0.0599  -0.0081 108 LEU   A CD1 
2210 C CD2 . LEU   A 108 ? 0.2174 0.2482 0.2668 -0.0170 0.0589  -0.0076 108 LEU   A CD2 
2223 N N   . LEU   A 109 ? 0.1527 0.1519 0.2025 -0.0000 0.0336  0.0131  109 LEU   A N   
2224 C CA  . LEU   A 109 ? 0.1462 0.1418 0.1824 0.0007  0.0180  0.0106  109 LEU   A CA  
2225 C C   . LEU   A 109 ? 0.1417 0.1385 0.1731 -0.0069 0.0185  -0.0006 109 LEU   A C   
2226 O O   . LEU   A 109 ? 0.1505 0.1293 0.1830 -0.0026 0.0049  -0.0004 109 LEU   A O   
2227 C CB  . LEU   A 109 ? 0.1579 0.1492 0.1865 0.0086  0.0061  0.0238  109 LEU   A CB  
2228 C CG  . LEU   A 109 ? 0.1480 0.1566 0.1977 0.0082  0.0088  0.0292  109 LEU   A CG  
2229 C CD1 . LEU   A 109 ? 0.1524 0.1489 0.2054 0.0060  0.0218  0.0072  109 LEU   A CD1 
2230 C CD2 . LEU   A 109 ? 0.1419 0.1768 0.2254 0.0069  0.0019  0.0278  109 LEU   A CD2 
2242 N N   . LYS   A 110 ? 0.1366 0.1396 0.1583 -0.0018 0.0072  -0.0002 110 LYS   A N   
2243 C CA  . LYS   A 110 ? 0.1401 0.1335 0.1722 -0.0053 0.0023  0.0082  110 LYS   A CA  
2244 C C   . LYS   A 110 ? 0.1409 0.1303 0.1527 -0.0072 0.0027  -0.0008 110 LYS   A C   
2245 O O   . LYS   A 110 ? 0.1333 0.1283 0.1686 -0.0062 0.0102  -0.0050 110 LYS   A O   
2246 C CB  . LYS   A 110 ? 0.1456 0.1391 0.1948 0.0027  -0.0110 -0.0068 110 LYS   A CB  
2247 C CG  . LYS   A 110 ? 0.1520 0.1334 0.2005 0.0029  -0.0101 -0.0038 110 LYS   A CG  
2248 C CD  . LYS   A 110 ? 0.1550 0.1434 0.2108 -0.0079 -0.0052 -0.0126 110 LYS   A CD  
2249 C CE  . LYS   A 110 ? 0.1612 0.1511 0.2356 -0.0061 0.0070  -0.0120 110 LYS   A CE  
2250 N NZ  . LYS   A 110 ? 0.1636 0.1500 0.2461 -0.0162 0.0190  -0.0023 110 LYS   A NZ  
2264 N N   . SER   A 111 ? 0.1401 0.1307 0.1643 -0.0038 0.0045  0.0060  111 SER   A N   
2265 C CA  . SER   A 111 ? 0.1336 0.1379 0.1647 -0.0026 0.0062  0.0019  111 SER   A CA  
2266 C C   . SER   A 111 ? 0.1327 0.1278 0.1564 -0.0074 0.0117  0.0021  111 SER   A C   
2267 O O   . SER   A 111 ? 0.1492 0.1261 0.1647 -0.0046 0.0092  0.0071  111 SER   A O   
2268 C CB  . SER   A 111 ? 0.1485 0.1586 0.1794 0.0009  0.0251  -0.0163 111 SER   A CB  
2269 O OG  . SER   A 111 ? 0.2031 0.1809 0.1894 0.0032  0.0310  -0.0175 111 SER   A OG  
2275 N N   . ALA   A 112 ? 0.1351 0.1214 0.1724 -0.0006 0.0173  0.0057  112 ALA   A N   
2276 C CA  . ALA   A 112 ? 0.1390 0.1222 0.1703 -0.0008 0.0256  -0.0020 112 ALA   A CA  
2277 C C   . ALA   A 112 ? 0.1323 0.1174 0.1792 -0.0003 0.0128  -0.0021 112 ALA   A C   
2278 O O   . ALA   A 112 ? 0.1346 0.1191 0.1789 -0.0101 0.0135  0.0054  112 ALA   A O   
2279 C CB  . ALA   A 112 ? 0.1480 0.1268 0.1802 -0.0047 0.0251  0.0025  112 ALA   A CB  
2285 N N   . TYR   A 113 ? 0.1285 0.1262 0.1735 -0.0032 0.0150  0.0064  113 TYR   A N   
2286 C CA  . TYR   A 113 ? 0.1262 0.1231 0.1665 -0.0032 0.0162  0.0061  113 TYR   A CA  
2287 C C   . TYR   A 113 ? 0.1217 0.1171 0.1571 -0.0077 0.0125  0.0021  113 TYR   A C   
2288 O O   . TYR   A 113 ? 0.1276 0.1284 0.1703 -0.0053 0.0135  0.0019  113 TYR   A O   
2289 C CB  . TYR   A 113 ? 0.1300 0.1358 0.1736 -0.0090 0.0049  0.0150  113 TYR   A CB  
2290 C CG  . TYR   A 113 ? 0.1282 0.1341 0.1577 -0.0078 0.0130  0.0133  113 TYR   A CG  
2291 C CD1 . TYR   A 113 ? 0.1312 0.1373 0.1527 -0.0030 0.0105  0.0196  113 TYR   A CD1 
2292 C CD2 . TYR   A 113 ? 0.1335 0.1396 0.1507 -0.0096 0.0067  0.0156  113 TYR   A CD2 
2293 C CE1 . TYR   A 113 ? 0.1320 0.1464 0.1562 -0.0048 0.0081  0.0278  113 TYR   A CE1 
2294 C CE2 . TYR   A 113 ? 0.1274 0.1439 0.1608 -0.0090 0.0111  0.0120  113 TYR   A CE2 
2295 C CZ  . TYR   A 113 ? 0.1333 0.1416 0.1589 0.0020  0.0159  0.0249  113 TYR   A CZ  
2296 O OH  . TYR   A 113 ? 0.1329 0.1459 0.1779 0.0088  0.0154  0.0251  113 TYR   A OH  
2306 N N   . GLU   A 114 ? 0.1267 0.1206 0.1712 -0.0030 0.0156  0.0090  114 GLU   A N   
2307 C CA  . GLU   A 114 ? 0.1293 0.1124 0.1786 0.0029  0.0094  0.0094  114 GLU   A CA  
2308 C C   . GLU   A 114 ? 0.1245 0.1228 0.1799 0.0035  0.0148  0.0136  114 GLU   A C   
2309 O O   . GLU   A 114 ? 0.1334 0.1228 0.1742 -0.0030 0.0011  0.0066  114 GLU   A O   
2310 C CB  . GLU   A 114 ? 0.1317 0.1188 0.1758 -0.0052 0.0081  0.0118  114 GLU   A CB  
2311 C CG  . GLU   A 114 ? 0.1351 0.1239 0.1760 -0.0033 0.0147  0.0001  114 GLU   A CG  
2312 C CD  . GLU   A 114 ? 0.1457 0.1256 0.1895 -0.0072 0.0050  -0.0026 114 GLU   A CD  
2313 O OE1 . GLU   A 114 ? 0.1450 0.1263 0.1953 -0.0114 0.0201  -0.0053 114 GLU   A OE1 
2314 O OE2 . GLU   A 114 ? 0.1616 0.1333 0.2086 -0.0126 0.0093  -0.0092 114 GLU   A OE2 
2321 N N   . ASN   A 115 ? 0.1291 0.1260 0.1586 -0.0056 0.0067  0.0065  115 ASN   A N   
2322 C CA  . ASN   A 115 ? 0.1289 0.1342 0.1750 -0.0084 0.0113  0.0112  115 ASN   A CA  
2323 C C   . ASN   A 115 ? 0.1336 0.1289 0.1655 -0.0133 0.0021  0.0105  115 ASN   A C   
2324 O O   . ASN   A 115 ? 0.1354 0.1411 0.1602 -0.0071 0.0087  0.0154  115 ASN   A O   
2325 C CB  . ASN   A 115 ? 0.1360 0.1338 0.1691 -0.0177 0.0184  0.0076  115 ASN   A CB  
2326 C CG  . ASN   A 115 ? 0.1370 0.1560 0.1807 -0.0185 0.0224  0.0119  115 ASN   A CG  
2327 O OD1 . ASN   A 115 ? 0.1393 0.2529 0.2068 -0.0188 0.0268  0.0274  115 ASN   A OD1 
2328 N ND2 . ASN   A 115 ? 0.1418 0.1347 0.1809 -0.0151 0.0308  0.0092  115 ASN   A ND2 
2335 N N   . PHE   A 116 ? 0.1256 0.1296 0.1668 -0.0048 0.0114  0.0163  116 PHE   A N   
2336 C CA  . PHE   A 116 ? 0.1237 0.1377 0.1541 0.0014  0.0151  0.0114  116 PHE   A CA  
2337 C C   . PHE   A 116 ? 0.1209 0.1423 0.1587 -0.0043 0.0191  0.0183  116 PHE   A C   
2338 O O   . PHE   A 116 ? 0.1325 0.1439 0.1728 -0.0034 0.0162  0.0239  116 PHE   A O   
2339 C CB  . PHE   A 116 ? 0.1298 0.1322 0.1661 -0.0040 0.0115  0.0162  116 PHE   A CB  
2340 C CG  . PHE   A 116 ? 0.1284 0.1297 0.1507 -0.0130 0.0144  0.0123  116 PHE   A CG  
2341 C CD1 . PHE   A 116 ? 0.1351 0.1290 0.1561 -0.0106 0.0138  0.0107  116 PHE   A CD1 
2342 C CD2 . PHE   A 116 ? 0.1338 0.1329 0.1740 -0.0100 0.0163  0.0151  116 PHE   A CD2 
2343 C CE1 . PHE   A 116 ? 0.1385 0.1230 0.1684 -0.0140 0.0125  0.0065  116 PHE   A CE1 
2344 C CE2 . PHE   A 116 ? 0.1377 0.1244 0.1791 -0.0047 0.0204  0.0085  116 PHE   A CE2 
2345 C CZ  . PHE   A 116 ? 0.1422 0.1188 0.1635 -0.0021 0.0100  0.0076  116 PHE   A CZ  
2355 N N   . ASN   A 117 ? 0.1293 0.1344 0.1703 -0.0044 0.0099  0.0204  117 ASN   A N   
2356 C CA  . ASN   A 117 ? 0.1267 0.1302 0.1912 -0.0035 0.0138  0.0205  117 ASN   A CA  
2357 C C   . ASN   A 117 ? 0.1270 0.1386 0.1963 -0.0022 0.0148  0.0220  117 ASN   A C   
2358 O O   . ASN   A 117 ? 0.1409 0.1434 0.2122 -0.0057 -0.0076 0.0330  117 ASN   A O   
2359 C CB  . ASN   A 117 ? 0.1322 0.1349 0.1955 -0.0046 0.0086  0.0329  117 ASN   A CB  
2360 C CG  . ASN   A 117 ? 0.1286 0.1356 0.1839 -0.0046 0.0147  0.0268  117 ASN   A CG  
2361 O OD1 . ASN   A 117 ? 0.1295 0.1555 0.1880 -0.0142 0.0130  0.0165  117 ASN   A OD1 
2362 N ND2 . ASN   A 117 ? 0.1255 0.1338 0.1818 -0.0058 0.0105  0.0193  117 ASN   A ND2 
2369 N N   . GLN   A 118 ? 0.1282 0.1405 0.1929 -0.0122 -0.0056 0.0285  118 GLN   A N   
2370 C CA  . GLN   A 118 ? 0.1366 0.1499 0.1924 -0.0086 -0.0037 0.0258  118 GLN   A CA  
2371 C C   . GLN   A 118 ? 0.1347 0.1593 0.1854 -0.0149 0.0008  0.0292  118 GLN   A C   
2372 O O   . GLN   A 118 ? 0.1351 0.1913 0.2186 -0.0039 -0.0148 0.0072  118 GLN   A O   
2373 C CB  . GLN   A 118 ? 0.1359 0.1521 0.2062 -0.0030 0.0026  0.0228  118 GLN   A CB  
2374 C CG  . GLN   A 118 ? 0.1332 0.1554 0.2187 -0.0042 0.0113  0.0223  118 GLN   A CG  
2375 C CD  . GLN   A 118 ? 0.1319 0.1654 0.2252 0.0005  0.0078  0.0180  118 GLN   A CD  
2376 O OE1 . GLN   A 118 ? 0.1372 0.1712 0.2405 0.0067  -0.0026 0.0102  118 GLN   A OE1 
2377 N NE2 . GLN   A 118 ? 0.1433 0.1610 0.2124 0.0058  0.0123  0.0274  118 GLN   A NE2 
2386 N N   . HIS   A 119 ? 0.1379 0.1572 0.1803 -0.0096 0.0011  0.0293  119 HIS   A N   
2387 C CA  . HIS   A 119 ? 0.1408 0.1667 0.1765 -0.0046 0.0013  0.0352  119 HIS   A CA  
2388 C C   . HIS   A 119 ? 0.1532 0.1695 0.1590 -0.0041 -0.0016 0.0357  119 HIS   A C   
2389 O O   . HIS   A 119 ? 0.1607 0.1805 0.1662 -0.0269 -0.0088 0.0372  119 HIS   A O   
2390 C CB  . HIS   A 119 ? 0.1477 0.1650 0.1900 -0.0076 0.0108  0.0295  119 HIS   A CB  
2391 C CG  . HIS   A 119 ? 0.1510 0.1707 0.2442 -0.0011 0.0131  0.0446  119 HIS   A CG  
2392 N ND1 . HIS   A 119 ? 0.1648 0.1900 0.3091 -0.0133 0.0089  0.0258  119 HIS   A ND1 
2393 C CD2 . HIS   A 119 ? 0.1642 0.1788 0.2607 0.0112  0.0273  0.0653  119 HIS   A CD2 
2394 C CE1 . HIS   A 119 ? 0.1667 0.1884 0.3177 -0.0142 0.0232  0.0518  119 HIS   A CE1 
2395 N NE2 . HIS   A 119 ? 0.1741 0.1830 0.3005 -0.0027 0.0477  0.0688  119 HIS   A NE2 
2403 N N   . GLU   A 120 ? 0.1658 0.1899 0.1605 -0.0049 -0.0096 0.0470  120 GLU   A N   
2404 C CA  . GLU   A 120 ? 0.1886 0.2160 0.1854 -0.0027 -0.0061 0.0887  120 GLU   A CA  
2405 C C   . GLU   A 120 ? 0.1670 0.2102 0.1720 -0.0138 0.0023  0.0869  120 GLU   A C   
2406 O O   . GLU   A 120 ? 0.1691 0.2033 0.1899 -0.0137 -0.0038 0.0769  120 GLU   A O   
2407 C CB  . GLU   A 120 ? 0.2547 0.2816 0.2549 0.0107  -0.0024 0.1455  120 GLU   A CB  
2408 C CG  . GLU   A 120 ? 0.3513 0.3583 0.3769 0.0241  -0.0019 0.1604  120 GLU   A CG  
2409 C CD  . GLU   A 120 ? 0.4289 0.4221 0.5078 0.0360  0.0071  0.1471  120 GLU   A CD  
2410 O OE1 . GLU   A 120 ? 0.4547 0.4460 0.5403 0.0389  0.0101  0.1407  120 GLU   A OE1 
2411 O OE2 . GLU   A 120 ? 0.4728 0.4728 0.5667 0.0395  0.0088  0.1424  120 GLU   A OE2 
2418 N N   . VAL   A 121 ? 0.1616 0.2100 0.1627 -0.0106 0.0013  0.0654  121 VAL   A N   
2419 C CA  . VAL   A 121 ? 0.1723 0.2140 0.1505 -0.0135 0.0187  0.0639  121 VAL   A CA  
2420 C C   . VAL   A 121 ? 0.1560 0.1947 0.1283 -0.0197 0.0076  0.0459  121 VAL   A C   
2421 O O   . VAL   A 121 ? 0.1618 0.1982 0.1552 -0.0299 -0.0092 0.0447  121 VAL   A O   
2422 C CB  . VAL   A 121 ? 0.2083 0.2461 0.1899 0.0032  0.0275  0.0719  121 VAL   A CB  
2423 C CG1 . VAL   A 121 ? 0.2104 0.2623 0.1904 0.0119  0.0332  0.0771  121 VAL   A CG1 
2424 C CG2 . VAL   A 121 ? 0.2347 0.2653 0.2328 -0.0062 0.0247  0.0524  121 VAL   A CG2 
2434 N N   . LEU   A 122 ? 0.1459 0.1775 0.1410 -0.0182 0.0039  0.0430  122 LEU   A N   
2435 C CA  . LEU   A 122 ? 0.1552 0.1624 0.1366 -0.0183 0.0194  0.0376  122 LEU   A CA  
2436 C C   . LEU   A 122 ? 0.1494 0.1591 0.1445 -0.0215 0.0085  0.0307  122 LEU   A C   
2437 O O   . LEU   A 122 ? 0.1496 0.1707 0.1735 -0.0260 0.0044  0.0319  122 LEU   A O   
2438 C CB  . LEU   A 122 ? 0.1703 0.1598 0.1764 -0.0083 0.0079  0.0504  122 LEU   A CB  
2439 C CG  . LEU   A 122 ? 0.1684 0.1636 0.1687 -0.0067 0.0125  0.0254  122 LEU   A CG  
2440 C CD1 . LEU   A 122 ? 0.1937 0.1668 0.1728 -0.0166 0.0148  0.0276  122 LEU   A CD1 
2441 C CD2 . LEU   A 122 ? 0.1624 0.1583 0.1699 -0.0091 0.0166  0.0320  122 LEU   A CD2 
2453 N N   A LEU   A 123 ? 0.1492 0.1572 0.1384 -0.0242 0.0026  0.0293  123 LEU   A N   
2454 N N   B LEU   A 123 ? 0.1527 0.1567 0.1433 -0.0192 0.0040  0.0183  123 LEU   A N   
2455 C CA  A LEU   A 123 ? 0.1467 0.1558 0.1250 -0.0283 0.0057  0.0267  123 LEU   A CA  
2456 C CA  B LEU   A 123 ? 0.1551 0.1554 0.1427 -0.0175 0.0046  0.0058  123 LEU   A CA  
2457 C C   A LEU   A 123 ? 0.1414 0.1400 0.1143 -0.0215 0.0019  0.0243  123 LEU   A C   
2458 C C   B LEU   A 123 ? 0.1565 0.1471 0.1284 -0.0120 0.0033  -0.0037 123 LEU   A C   
2459 O O   A LEU   A 123 ? 0.1254 0.1370 0.1302 -0.0159 0.0118  0.0210  123 LEU   A O   
2460 O O   B LEU   A 123 ? 0.1583 0.1389 0.1223 -0.0111 -0.0027 -0.0209 123 LEU   A O   
2461 C CB  A LEU   A 123 ? 0.1607 0.1722 0.1117 -0.0265 0.0218  0.0290  123 LEU   A CB  
2462 C CB  B LEU   A 123 ? 0.1596 0.1620 0.1481 -0.0195 0.0039  0.0028  123 LEU   A CB  
2463 C CG  A LEU   A 123 ? 0.1676 0.1871 0.1368 -0.0195 0.0184  0.0102  123 LEU   A CG  
2464 C CG  B LEU   A 123 ? 0.1585 0.1654 0.1421 -0.0226 0.0100  0.0057  123 LEU   A CG  
2465 C CD1 A LEU   A 123 ? 0.1714 0.1912 0.1541 -0.0199 0.0155  -0.0017 123 LEU   A CD1 
2466 C CD1 B LEU   A 123 ? 0.1615 0.1626 0.1421 -0.0246 0.0113  0.0059  123 LEU   A CD1 
2467 C CD2 A LEU   A 123 ? 0.1760 0.1946 0.1371 -0.0166 0.0083  0.0088  123 LEU   A CD2 
2468 C CD2 B LEU   A 123 ? 0.1579 0.1684 0.1399 -0.0252 0.0097  0.0108  123 LEU   A CD2 
2491 N N   A ALA   A 124 ? 0.1375 0.1283 0.1103 -0.0168 0.0016  0.0242  124 ALA   A N   
2492 N N   B ALA   A 124 ? 0.1515 0.1424 0.1240 -0.0079 0.0104  -0.0041 124 ALA   A N   
2493 C CA  A ALA   A 124 ? 0.1323 0.1285 0.1217 -0.0054 -0.0036 0.0285  124 ALA   A CA  
2494 C CA  B ALA   A 124 ? 0.1509 0.1471 0.1321 -0.0111 -0.0019 0.0084  124 ALA   A CA  
2495 C C   A ALA   A 124 ? 0.1214 0.1324 0.1232 -0.0085 0.0084  0.0254  124 ALA   A C   
2496 C C   B ALA   A 124 ? 0.1476 0.1468 0.1170 -0.0109 -0.0064 0.0124  124 ALA   A C   
2497 O O   A ALA   A 124 ? 0.1187 0.1370 0.1516 -0.0194 0.0177  0.0284  124 ALA   A O   
2498 O O   B ALA   A 124 ? 0.1520 0.1517 0.1069 -0.0066 -0.0140 0.0186  124 ALA   A O   
2499 C CB  A ALA   A 124 ? 0.1321 0.1235 0.1523 -0.0092 0.0029  0.0176  124 ALA   A CB  
2500 C CB  B ALA   A 124 ? 0.1558 0.1457 0.1454 -0.0170 0.0059  0.0082  124 ALA   A CB  
2511 N N   A PRO   A 125 ? 0.1181 0.1319 0.1306 -0.0062 0.0102  0.0304  125 PRO   A N   
2512 N N   B PRO   A 125 ? 0.1382 0.1374 0.1120 -0.0067 -0.0120 0.0182  125 PRO   A N   
2513 C CA  A PRO   A 125 ? 0.1255 0.1329 0.1326 -0.0055 0.0049  0.0217  125 PRO   A CA  
2514 C CA  B PRO   A 125 ? 0.1410 0.1432 0.1230 -0.0091 -0.0095 0.0149  125 PRO   A CA  
2515 C C   A PRO   A 125 ? 0.1214 0.1311 0.1356 -0.0020 0.0127  0.0250  125 PRO   A C   
2516 C C   B PRO   A 125 ? 0.1524 0.1543 0.1345 -0.0086 -0.0092 0.0098  125 PRO   A C   
2517 O O   A PRO   A 125 ? 0.1270 0.1303 0.1371 0.0031  0.0092  0.0191  125 PRO   A O   
2518 O O   B PRO   A 125 ? 0.1542 0.1590 0.1370 -0.0123 -0.0059 0.0164  125 PRO   A O   
2519 C CB  A PRO   A 125 ? 0.1394 0.1340 0.1322 -0.0144 0.0103  0.0199  125 PRO   A CB  
2520 C CB  B PRO   A 125 ? 0.1315 0.1371 0.1182 -0.0093 -0.0157 0.0165  125 PRO   A CB  
2521 C CG  A PRO   A 125 ? 0.1420 0.1364 0.1446 -0.0163 0.0089  0.0314  125 PRO   A CG  
2522 C CG  B PRO   A 125 ? 0.1218 0.1313 0.1228 -0.0085 -0.0105 0.0208  125 PRO   A CG  
2523 C CD  A PRO   A 125 ? 0.1258 0.1381 0.1387 -0.0092 0.0192  0.0255  125 PRO   A CD  
2524 C CD  B PRO   A 125 ? 0.1226 0.1248 0.1116 -0.0076 -0.0073 0.0268  125 PRO   A CD  
2539 N N   A LEU   A 126 ? 0.1180 0.1342 0.1380 -0.0008 0.0178  0.0219  126 LEU   A N   
2540 N N   B LEU   A 126 ? 0.1612 0.1593 0.1496 -0.0058 -0.0106 -0.0016 126 LEU   A N   
2541 C CA  A LEU   A 126 ? 0.1186 0.1307 0.1365 0.0004  0.0112  0.0171  126 LEU   A CA  
2542 C CA  B LEU   A 126 ? 0.1616 0.1626 0.1604 -0.0035 -0.0082 -0.0004 126 LEU   A CA  
2543 C C   A LEU   A 126 ? 0.1245 0.1233 0.1432 0.0071  -0.0005 0.0128  126 LEU   A C   
2544 C C   B LEU   A 126 ? 0.1526 0.1523 0.1536 0.0010  -0.0030 -0.0033 126 LEU   A C   
2545 O O   A LEU   A 126 ? 0.1402 0.1329 0.1701 0.0133  0.0263  0.0272  126 LEU   A O   
2546 O O   B LEU   A 126 ? 0.1601 0.1546 0.1524 -0.0096 -0.0033 0.0068  126 LEU   A O   
2547 C CB  A LEU   A 126 ? 0.1234 0.1375 0.1466 -0.0072 0.0046  0.0102  126 LEU   A CB  
2548 C CB  B LEU   A 126 ? 0.1746 0.1822 0.2048 -0.0093 -0.0163 0.0053  126 LEU   A CB  
2549 C CG  A LEU   A 126 ? 0.1279 0.1641 0.1581 -0.0215 0.0102  0.0084  126 LEU   A CG  
2550 C CG  B LEU   A 126 ? 0.1870 0.1963 0.2452 -0.0096 -0.0259 0.0136  126 LEU   A CG  
2551 C CD1 A LEU   A 126 ? 0.1349 0.1821 0.1873 -0.0261 0.0043  0.0185  126 LEU   A CD1 
2552 C CD1 B LEU   A 126 ? 0.1864 0.1992 0.2568 -0.0103 -0.0310 0.0157  126 LEU   A CD1 
2553 C CD2 A LEU   A 126 ? 0.1364 0.1614 0.1554 -0.0235 0.0063  0.0296  126 LEU   A CD2 
2554 C CD2 B LEU   A 126 ? 0.1920 0.2011 0.2537 -0.0083 -0.0293 0.0147  126 LEU   A CD2 
2577 N N   A LEU   A 127 ? 0.1280 0.1319 0.1364 0.0050  0.0064  0.0148  127 LEU   A N   
2578 N N   B LEU   A 127 ? 0.1443 0.1481 0.1531 0.0127  0.0016  -0.0008 127 LEU   A N   
2579 C CA  A LEU   A 127 ? 0.1294 0.1395 0.1231 -0.0013 0.0011  0.0111  127 LEU   A CA  
2580 C CA  B LEU   A 127 ? 0.1390 0.1541 0.1466 0.0109  0.0011  0.0060  127 LEU   A CA  
2581 C C   A LEU   A 127 ? 0.1205 0.1307 0.1248 -0.0026 -0.0006 0.0045  127 LEU   A C   
2582 C C   B LEU   A 127 ? 0.1385 0.1523 0.1441 0.0026  0.0078  0.0050  127 LEU   A C   
2583 O O   A LEU   A 127 ? 0.1315 0.1282 0.1363 -0.0131 -0.0010 0.0066  127 LEU   A O   
2584 O O   B LEU   A 127 ? 0.1463 0.1534 0.1578 -0.0014 0.0136  0.0131  127 LEU   A O   
2585 C CB  A LEU   A 127 ? 0.1424 0.1561 0.1322 0.0108  0.0114  0.0056  127 LEU   A CB  
2586 C CB  B LEU   A 127 ? 0.1359 0.1666 0.1357 0.0166  -0.0036 0.0054  127 LEU   A CB  
2587 C CG  A LEU   A 127 ? 0.1527 0.1590 0.1504 0.0111  0.0069  0.0081  127 LEU   A CG  
2588 C CG  B LEU   A 127 ? 0.1290 0.1760 0.1275 0.0201  -0.0171 0.0053  127 LEU   A CG  
2589 C CD1 A LEU   A 127 ? 0.1558 0.1447 0.1647 0.0090  0.0100  0.0039  127 LEU   A CD1 
2590 C CD1 B LEU   A 127 ? 0.1315 0.1786 0.1418 0.0230  -0.0087 0.0077  127 LEU   A CD1 
2591 C CD2 A LEU   A 127 ? 0.1655 0.1549 0.1600 0.0310  0.0043  0.0047  127 LEU   A CD2 
2592 C CD2 B LEU   A 127 ? 0.1309 0.1887 0.1240 0.0239  -0.0241 0.0060  127 LEU   A CD2 
2615 N N   A SER   A 128 ? 0.1302 0.1278 0.1226 -0.0038 0.0024  0.0102  128 SER   A N   
2616 N N   B SER   A 128 ? 0.1357 0.1516 0.1370 -0.0025 0.0125  0.0089  128 SER   A N   
2617 C CA  A SER   A 128 ? 0.1468 0.1358 0.1211 -0.0019 0.0072  0.0145  128 SER   A CA  
2618 C CA  B SER   A 128 ? 0.1383 0.1529 0.1428 -0.0071 0.0062  0.0151  128 SER   A CA  
2619 C C   A SER   A 128 ? 0.1507 0.1394 0.1216 0.0071  -0.0130 0.0186  128 SER   A C   
2620 C C   B SER   A 128 ? 0.1453 0.1505 0.1526 -0.0058 0.0063  0.0158  128 SER   A C   
2621 O O   A SER   A 128 ? 0.1714 0.1567 0.1506 0.0054  -0.0150 0.0153  128 SER   A O   
2622 O O   B SER   A 128 ? 0.1482 0.1538 0.1602 -0.0027 -0.0034 0.0104  128 SER   A O   
2623 C CB  A SER   A 128 ? 0.1499 0.1504 0.1225 -0.0100 0.0075  0.0114  128 SER   A CB  
2624 C CB  B SER   A 128 ? 0.1310 0.1562 0.1298 -0.0103 -0.0031 0.0102  128 SER   A CB  
2625 O OG  A SER   A 128 ? 0.1545 0.1584 0.1441 -0.0077 0.0148  0.0139  128 SER   A OG  
2626 O OG  B SER   A 128 ? 0.1235 0.1564 0.1285 -0.0108 -0.0066 0.0011  128 SER   A OG  
2637 N N   A ALA   A 129 ? 0.1440 0.1446 0.1507 0.0085  -0.0097 0.0228  129 ALA   A N   
2638 N N   B ALA   A 129 ? 0.1488 0.1511 0.1625 -0.0085 0.0129  0.0175  129 ALA   A N   
2639 C CA  A ALA   A 129 ? 0.1399 0.1476 0.1775 0.0083  -0.0014 0.0346  129 ALA   A CA  
2640 C CA  B ALA   A 129 ? 0.1529 0.1515 0.1643 -0.0094 0.0098  0.0187  129 ALA   A CA  
2641 C C   A ALA   A 129 ? 0.1478 0.1520 0.1558 0.0109  -0.0003 0.0168  129 ALA   A C   
2642 C C   B ALA   A 129 ? 0.1525 0.1465 0.1502 -0.0148 -0.0021 0.0041  129 ALA   A C   
2643 O O   A ALA   A 129 ? 0.1580 0.1578 0.1496 0.0058  -0.0063 0.0242  129 ALA   A O   
2644 O O   B ALA   A 129 ? 0.1516 0.1430 0.1344 -0.0248 -0.0040 -0.0019 129 ALA   A O   
2645 C CB  A ALA   A 129 ? 0.1390 0.1613 0.2128 0.0085  0.0126  0.0438  129 ALA   A CB  
2646 C CB  B ALA   A 129 ? 0.1585 0.1569 0.1734 -0.0055 0.0193  0.0258  129 ALA   A CB  
2657 N N   A GLY   A 130 ? 0.1529 0.1498 0.1721 0.0065  0.0101  0.0182  130 GLY   A N   
2658 N N   B GLY   A 130 ? 0.1592 0.1466 0.1511 -0.0117 -0.0063 0.0119  130 GLY   A N   
2659 C CA  A GLY   A 130 ? 0.1694 0.1520 0.1675 0.0047  0.0136  0.0140  130 GLY   A CA  
2660 C CA  B GLY   A 130 ? 0.1659 0.1451 0.1504 -0.0128 -0.0088 0.0108  130 GLY   A CA  
2661 C C   A GLY   A 130 ? 0.1617 0.1515 0.1456 0.0029  0.0094  0.0117  130 GLY   A C   
2662 C C   B GLY   A 130 ? 0.1656 0.1464 0.1454 -0.0084 -0.0198 0.0113  130 GLY   A C   
2663 O O   A GLY   A 130 ? 0.1611 0.1443 0.1496 0.0046  -0.0037 0.0151  130 GLY   A O   
2664 O O   B GLY   A 130 ? 0.1685 0.1471 0.1527 -0.0014 -0.0225 0.0157  130 GLY   A O   
2671 N N   A ILE   A 131 ? 0.1738 0.1495 0.1527 0.0038  0.0126  0.0150  131 ILE   A N   
2672 N N   B ILE   A 131 ? 0.1618 0.1435 0.1420 -0.0124 -0.0142 0.0182  131 ILE   A N   
2673 C CA  A ILE   A 131 ? 0.1768 0.1492 0.1265 -0.0013 -0.0016 0.0110  131 ILE   A CA  
2674 C CA  B ILE   A 131 ? 0.1628 0.1393 0.1468 -0.0097 -0.0268 0.0179  131 ILE   A CA  
2675 C C   A ILE   A 131 ? 0.1672 0.1550 0.1246 0.0011  0.0019  0.0198  131 ILE   A C   
2676 C C   B ILE   A 131 ? 0.1642 0.1384 0.1491 -0.0104 -0.0199 0.0211  131 ILE   A C   
2677 O O   A ILE   A 131 ? 0.1747 0.1600 0.1371 0.0071  -0.0009 0.0220  131 ILE   A O   
2678 O O   B ILE   A 131 ? 0.1679 0.1397 0.1626 -0.0162 -0.0106 0.0230  131 ILE   A O   
2679 C CB  A ILE   A 131 ? 0.1872 0.1634 0.1539 -0.0071 -0.0010 -0.0033 131 ILE   A CB  
2680 C CB  B ILE   A 131 ? 0.1588 0.1454 0.1551 -0.0090 -0.0359 0.0055  131 ILE   A CB  
2681 C CG1 A ILE   A 131 ? 0.1912 0.1988 0.1721 -0.0145 -0.0115 -0.0133 131 ILE   A CG1 
2682 C CG1 B ILE   A 131 ? 0.1551 0.1589 0.1661 -0.0058 -0.0354 0.0020  131 ILE   A CG1 
2683 C CG2 A ILE   A 131 ? 0.1966 0.1518 0.1889 0.0010  0.0084  -0.0111 131 ILE   A CG2 
2684 C CG2 B ILE   A 131 ? 0.1576 0.1446 0.1611 -0.0114 -0.0292 -0.0055 131 ILE   A CG2 
2685 C CD1 A ILE   A 131 ? 0.1909 0.2146 0.2141 -0.0135 -0.0291 -0.0251 131 ILE   A CD1 
2686 C CD1 B ILE   A 131 ? 0.1582 0.1654 0.1876 -0.0031 -0.0348 -0.0027 131 ILE   A CD1 
2709 N N   A PHE   A 132 ? 0.1625 0.1504 0.1402 0.0011  0.0033  0.0197  132 PHE   A N   
2710 N N   B PHE   A 132 ? 0.1562 0.1355 0.1517 0.0010  -0.0173 0.0183  132 PHE   A N   
2711 C CA  A PHE   A 132 ? 0.1634 0.1546 0.1274 -0.0051 0.0089  0.0108  132 PHE   A CA  
2712 C CA  B PHE   A 132 ? 0.1591 0.1384 0.1603 0.0009  -0.0136 0.0137  132 PHE   A CA  
2713 C C   A PHE   A 132 ? 0.1638 0.1713 0.1310 -0.0072 0.0092  0.0042  132 PHE   A C   
2714 C C   B PHE   A 132 ? 0.1676 0.1532 0.1732 0.0034  -0.0143 0.0144  132 PHE   A C   
2715 O O   A PHE   A 132 ? 0.1691 0.1900 0.1464 -0.0092 0.0106  0.0051  132 PHE   A O   
2716 O O   B PHE   A 132 ? 0.1795 0.1669 0.1834 0.0036  -0.0087 0.0176  132 PHE   A O   
2717 C CB  A PHE   A 132 ? 0.1665 0.1502 0.1221 0.0025  0.0033  0.0174  132 PHE   A CB  
2718 C CB  B PHE   A 132 ? 0.1542 0.1369 0.1423 -0.0049 -0.0054 0.0230  132 PHE   A CB  
2719 C CG  A PHE   A 132 ? 0.1711 0.1548 0.1035 0.0089  0.0042  0.0150  132 PHE   A CG  
2720 C CG  B PHE   A 132 ? 0.1603 0.1409 0.1326 -0.0087 -0.0035 0.0097  132 PHE   A CG  
2721 C CD1 A PHE   A 132 ? 0.1714 0.1647 0.1581 0.0154  -0.0014 -0.0030 132 PHE   A CD1 
2722 C CD1 B PHE   A 132 ? 0.1617 0.1482 0.1515 -0.0052 -0.0023 -0.0020 132 PHE   A CD1 
2723 C CD2 A PHE   A 132 ? 0.1697 0.1657 0.1301 0.0051  -0.0071 0.0102  132 PHE   A CD2 
2724 C CD2 B PHE   A 132 ? 0.1618 0.1466 0.1387 -0.0084 -0.0116 -0.0066 132 PHE   A CD2 
2725 C CE1 A PHE   A 132 ? 0.1762 0.1677 0.1701 0.0109  -0.0104 -0.0048 132 PHE   A CE1 
2726 C CE1 B PHE   A 132 ? 0.1657 0.1505 0.1561 -0.0082 -0.0070 -0.0086 132 PHE   A CE1 
2727 C CE2 A PHE   A 132 ? 0.1736 0.1713 0.1605 0.0065  -0.0126 0.0147  132 PHE   A CE2 
2728 C CE2 B PHE   A 132 ? 0.1624 0.1521 0.1468 -0.0060 -0.0120 -0.0097 132 PHE   A CE2 
2729 C CZ  A PHE   A 132 ? 0.1712 0.1717 0.1668 0.0033  -0.0174 0.0054  132 PHE   A CZ  
2730 C CZ  B PHE   A 132 ? 0.1626 0.1506 0.1508 -0.0103 -0.0117 -0.0129 132 PHE   A CZ  
2749 N N   A GLY   A 133 ? 0.1674 0.1703 0.1190 -0.0023 -0.0108 0.0060  133 GLY   A N   
2750 N N   B GLY   A 133 ? 0.1670 0.1539 0.1672 0.0021  -0.0167 0.0152  133 GLY   A N   
2751 C CA  A GLY   A 133 ? 0.1774 0.1830 0.1304 -0.0085 -0.0126 0.0053  133 GLY   A CA  
2752 C CA  B GLY   A 133 ? 0.1706 0.1626 0.1725 0.0062  -0.0187 0.0115  133 GLY   A CA  
2753 C C   A GLY   A 133 ? 0.1856 0.1928 0.1383 -0.0203 -0.0278 -0.0008 133 GLY   A C   
2754 C C   B GLY   A 133 ? 0.1743 0.1744 0.1809 0.0098  -0.0198 0.0022  133 GLY   A C   
2755 O O   A GLY   A 133 ? 0.2073 0.2096 0.1430 -0.0216 -0.0293 -0.0095 133 GLY   A O   
2756 O O   B GLY   A 133 ? 0.1812 0.1822 0.1906 0.0136  -0.0197 -0.0123 133 GLY   A O   
2763 N N   A ALA   A 134 ? 0.1773 0.1779 0.1388 -0.0172 -0.0169 -0.0070 134 ALA   A N   
2764 N N   B ALA   A 134 ? 0.1712 0.1745 0.1809 0.0150  -0.0136 0.0047  134 ALA   A N   
2765 C CA  A ALA   A 134 ? 0.1694 0.1761 0.1602 -0.0158 -0.0257 -0.0101 134 ALA   A CA  
2766 C CA  B ALA   A 134 ? 0.1700 0.1814 0.1848 0.0130  -0.0150 0.0074  134 ALA   A CA  
2767 C C   A ALA   A 134 ? 0.1694 0.1761 0.1645 -0.0106 -0.0179 0.0053  134 ALA   A C   
2768 C C   B ALA   A 134 ? 0.1719 0.1873 0.1959 0.0031  -0.0019 0.0163  134 ALA   A C   
2769 O O   A ALA   A 134 ? 0.1914 0.1857 0.2096 -0.0057 0.0153  0.0017  134 ALA   A O   
2770 O O   B ALA   A 134 ? 0.1794 0.1904 0.2134 -0.0025 0.0042  0.0168  134 ALA   A O   
2771 C CB  A ALA   A 134 ? 0.1729 0.1692 0.1899 -0.0096 -0.0239 -0.0173 134 ALA   A CB  
2772 C CB  B ALA   A 134 ? 0.1745 0.1821 0.1903 0.0209  -0.0200 0.0076  134 ALA   A CB  
2783 N N   A ASP   A 135 ? 0.1711 0.1813 0.1746 -0.0240 -0.0251 0.0238  135 ASP   A N   
2784 N N   B ASP   A 135 ? 0.1707 0.1926 0.1999 0.0017  0.0028  0.0182  135 ASP   A N   
2785 C CA  A ASP   A 135 ? 0.1750 0.2044 0.2169 -0.0315 -0.0372 0.0340  135 ASP   A CA  
2786 C CA  B ASP   A 135 ? 0.1745 0.2018 0.2087 0.0003  -0.0048 0.0239  135 ASP   A CA  
2787 C C   A ASP   A 135 ? 0.1642 0.1905 0.2180 -0.0206 -0.0197 0.0430  135 ASP   A C   
2788 C C   B ASP   A 135 ? 0.1689 0.1984 0.1942 -0.0059 -0.0043 0.0206  135 ASP   A C   
2789 O O   A ASP   A 135 ? 0.1669 0.1779 0.2104 -0.0206 -0.0181 0.0456  135 ASP   A O   
2790 O O   B ASP   A 135 ? 0.1663 0.1900 0.1946 -0.0095 -0.0073 0.0215  135 ASP   A O   
2791 C CB  A ASP   A 135 ? 0.2005 0.2456 0.2504 -0.0563 -0.0639 0.0286  135 ASP   A CB  
2792 C CB  B ASP   A 135 ? 0.1909 0.2177 0.2528 -0.0005 -0.0129 0.0309  135 ASP   A CB  
2793 C CG  A ASP   A 135 ? 0.2150 0.2839 0.2911 -0.0700 -0.0858 0.0273  135 ASP   A CG  
2794 C CG  B ASP   A 135 ? 0.2011 0.2310 0.2943 0.0035  -0.0181 0.0389  135 ASP   A CG  
2795 O OD1 A ASP   A 135 ? 0.2137 0.2965 0.2730 -0.0779 -0.0887 0.0636  135 ASP   A OD1 
2796 O OD1 B ASP   A 135 ? 0.2075 0.2325 0.3096 0.0062  -0.0093 0.0427  135 ASP   A OD1 
2797 O OD2 A ASP   A 135 ? 0.2450 0.3049 0.3496 -0.0736 -0.0671 0.0213  135 ASP   A OD2 
2798 O OD2 B ASP   A 135 ? 0.2043 0.2411 0.3155 0.0045  -0.0219 0.0473  135 ASP   A OD2 
2807 N N   A PRO   A 136 ? 0.1550 0.1880 0.2226 -0.0018 -0.0147 0.0541  136 PRO   A N   
2808 N N   B PRO   A 136 ? 0.1651 0.2008 0.1834 -0.0081 -0.0080 0.0195  136 PRO   A N   
2809 C CA  A PRO   A 136 ? 0.1477 0.1811 0.2296 -0.0046 -0.0086 0.0383  136 PRO   A CA  
2810 C CA  B PRO   A 136 ? 0.1611 0.1986 0.1819 -0.0095 -0.0114 0.0146  136 PRO   A CA  
2811 C C   A PRO   A 136 ? 0.1306 0.1773 0.2209 0.0008  -0.0031 0.0350  136 PRO   A C   
2812 C C   B PRO   A 136 ? 0.1588 0.1974 0.1963 -0.0078 -0.0080 0.0156  136 PRO   A C   
2813 O O   A PRO   A 136 ? 0.1278 0.1790 0.2077 -0.0019 0.0058  0.0376  136 PRO   A O   
2814 O O   B PRO   A 136 ? 0.1601 0.1915 0.1990 -0.0092 -0.0033 0.0166  136 PRO   A O   
2815 C CB  A PRO   A 136 ? 0.1682 0.1849 0.2548 0.0007  -0.0071 0.0381  136 PRO   A CB  
2816 C CB  B PRO   A 136 ? 0.1661 0.1986 0.1753 -0.0088 -0.0138 0.0203  136 PRO   A CB  
2817 C CG  A PRO   A 136 ? 0.1803 0.1940 0.2736 0.0131  -0.0122 0.0447  136 PRO   A CG  
2818 C CG  B PRO   A 136 ? 0.1717 0.2034 0.1802 -0.0072 -0.0176 0.0164  136 PRO   A CG  
2819 C CD  A PRO   A 136 ? 0.1659 0.1872 0.2494 0.0133  -0.0133 0.0641  136 PRO   A CD  
2820 C CD  B PRO   A 136 ? 0.1704 0.2035 0.1849 -0.0056 -0.0115 0.0169  136 PRO   A CD  
2835 N N   A ILE   A 137 ? 0.1341 0.1765 0.2218 -0.0047 -0.0084 0.0368  137 ILE   A N   
2836 N N   B ILE   A 137 ? 0.1595 0.2012 0.2027 -0.0103 -0.0088 0.0130  137 ILE   A N   
2837 C CA  A ILE   A 137 ? 0.1397 0.1896 0.2192 -0.0163 -0.0140 0.0343  137 ILE   A CA  
2838 C CA  B ILE   A 137 ? 0.1615 0.2074 0.2044 -0.0137 -0.0107 0.0153  137 ILE   A CA  
2839 C C   A ILE   A 137 ? 0.1401 0.1851 0.1993 -0.0166 -0.0185 0.0300  137 ILE   A C   
2840 C C   B ILE   A 137 ? 0.1524 0.2002 0.1932 -0.0177 -0.0101 0.0209  137 ILE   A C   
2841 O O   A ILE   A 137 ? 0.1456 0.1804 0.2051 -0.0128 -0.0096 0.0219  137 ILE   A O   
2842 O O   B ILE   A 137 ? 0.1524 0.2007 0.1921 -0.0210 -0.0034 0.0203  137 ILE   A O   
2843 C CB  A ILE   A 137 ? 0.1469 0.2144 0.2471 -0.0181 -0.0317 0.0373  137 ILE   A CB  
2844 C CB  B ILE   A 137 ? 0.1741 0.2215 0.2291 -0.0122 -0.0172 0.0127  137 ILE   A CB  
2845 C CG1 A ILE   A 137 ? 0.1599 0.2445 0.2846 -0.0051 -0.0434 0.0368  137 ILE   A CG1 
2846 C CG1 B ILE   A 137 ? 0.1869 0.2366 0.2519 -0.0068 -0.0180 0.0105  137 ILE   A CG1 
2847 C CG2 A ILE   A 137 ? 0.1580 0.2160 0.2640 -0.0249 -0.0303 0.0277  137 ILE   A CG2 
2848 C CG2 B ILE   A 137 ? 0.1781 0.2228 0.2361 -0.0140 -0.0193 0.0094  137 ILE   A CG2 
2849 C CD1 A ILE   A 137 ? 0.1658 0.2576 0.2955 0.0039  -0.0431 0.0434  137 ILE   A CD1 
2850 C CD1 B ILE   A 137 ? 0.1970 0.2442 0.2656 -0.0032 -0.0123 0.0099  137 ILE   A CD1 
2873 N N   . HIS   A 138 ? 0.1464 0.1978 0.1935 -0.0171 -0.0078 0.0270  138 HIS   A N   
2874 C CA  . HIS   A 138 ? 0.1530 0.2002 0.1810 -0.0143 0.0012  0.0137  138 HIS   A CA  
2875 C C   . HIS   A 138 ? 0.1420 0.1842 0.1775 -0.0101 0.0026  0.0216  138 HIS   A C   
2876 O O   . HIS   A 138 ? 0.1524 0.1851 0.1819 -0.0058 0.0039  0.0203  138 HIS   A O   
2877 C CB  . HIS   A 138 ? 0.1694 0.2205 0.1765 -0.0138 -0.0056 0.0093  138 HIS   A CB  
2878 C CG  . HIS   A 138 ? 0.1870 0.2322 0.1763 -0.0241 -0.0099 -0.0001 138 HIS   A CG  
2879 N ND1 . HIS   A 138 ? 0.2024 0.2454 0.2114 -0.0265 -0.0016 -0.0108 138 HIS   A ND1 
2880 C CD2 . HIS   A 138 ? 0.1849 0.2415 0.1806 -0.0190 -0.0116 0.0090  138 HIS   A CD2 
2881 C CE1 . HIS   A 138 ? 0.2058 0.2531 0.2150 -0.0145 -0.0086 -0.0110 138 HIS   A CE1 
2882 N NE2 . HIS   A 138 ? 0.1940 0.2523 0.1885 -0.0133 0.0019  -0.0011 138 HIS   A NE2 
2891 N N   . SER   A 139 ? 0.1378 0.1739 0.1772 -0.0089 -0.0031 0.0257  139 SER   A N   
2892 C CA  . SER   A 139 ? 0.1321 0.1730 0.1816 -0.0086 0.0040  0.0304  139 SER   A CA  
2893 C C   . SER   A 139 ? 0.1320 0.1576 0.1721 -0.0082 0.0111  0.0202  139 SER   A C   
2894 O O   . SER   A 139 ? 0.1276 0.1535 0.1870 -0.0153 0.0061  0.0243  139 SER   A O   
2895 C CB  . SER   A 139 ? 0.1330 0.1680 0.1795 -0.0152 -0.0048 0.0302  139 SER   A CB  
2896 O OG  . SER   A 139 ? 0.1408 0.1665 0.1902 -0.0197 -0.0099 0.0384  139 SER   A OG  
2902 N N   . LEU   A 140 ? 0.1302 0.1628 0.1694 -0.0068 0.0080  0.0318  140 LEU   A N   
2903 C CA  . LEU   A 140 ? 0.1313 0.1568 0.1626 -0.0077 0.0080  0.0224  140 LEU   A CA  
2904 C C   . LEU   A 140 ? 0.1232 0.1642 0.1737 -0.0150 0.0023  0.0302  140 LEU   A C   
2905 O O   . LEU   A 140 ? 0.1317 0.1658 0.1921 -0.0078 0.0033  0.0312  140 LEU   A O   
2906 C CB  . LEU   A 140 ? 0.1332 0.1621 0.1773 -0.0104 0.0071  0.0231  140 LEU   A CB  
2907 C CG  . LEU   A 140 ? 0.1320 0.1751 0.1800 -0.0205 0.0145  0.0363  140 LEU   A CG  
2908 C CD1 . LEU   A 140 ? 0.1394 0.1780 0.1952 -0.0135 0.0028  0.0285  140 LEU   A CD1 
2909 C CD2 . LEU   A 140 ? 0.1338 0.1959 0.1935 -0.0180 0.0149  0.0401  140 LEU   A CD2 
2921 N N   . ARG   A 141 ? 0.1310 0.1704 0.1686 -0.0103 -0.0001 0.0259  141 ARG   A N   
2922 C CA  . ARG   A 141 ? 0.1428 0.1796 0.1957 -0.0169 -0.0053 0.0064  141 ARG   A CA  
2923 C C   . ARG   A 141 ? 0.1466 0.1626 0.1875 -0.0165 -0.0033 0.0032  141 ARG   A C   
2924 O O   . ARG   A 141 ? 0.1429 0.1619 0.1982 -0.0195 0.0074  0.0046  141 ARG   A O   
2925 C CB  . ARG   A 141 ? 0.1565 0.2046 0.2267 -0.0247 -0.0042 -0.0154 141 ARG   A CB  
2926 C CG  . ARG   A 141 ? 0.1942 0.2431 0.2630 -0.0271 0.0171  -0.0221 141 ARG   A CG  
2927 C CD  . ARG   A 141 ? 0.2221 0.2654 0.2944 -0.0349 0.0179  -0.0342 141 ARG   A CD  
2928 N NE  . ARG   A 141 ? 0.2180 0.2842 0.3094 -0.0349 0.0043  -0.0311 141 ARG   A NE  
2929 C CZ  . ARG   A 141 ? 0.2164 0.3039 0.3120 -0.0483 0.0099  -0.0207 141 ARG   A CZ  
2930 N NH1 . ARG   A 141 ? 0.2010 0.3063 0.2935 -0.0591 0.0328  -0.0390 141 ARG   A NH1 
2931 N NH2 . ARG   A 141 ? 0.2259 0.3186 0.3398 -0.0422 -0.0080 -0.0007 141 ARG   A NH2 
2945 N N   . VAL   A 142 ? 0.1365 0.1597 0.1826 -0.0164 0.0045  -0.0033 142 VAL   A N   
2946 C CA  . VAL   A 142 ? 0.1417 0.1565 0.1800 -0.0069 0.0168  0.0014  142 VAL   A CA  
2947 C C   . VAL   A 142 ? 0.1240 0.1505 0.1800 -0.0136 0.0098  0.0080  142 VAL   A C   
2948 O O   . VAL   A 142 ? 0.1287 0.1519 0.1955 -0.0014 0.0126  0.0120  142 VAL   A O   
2949 C CB  . VAL   A 142 ? 0.1447 0.1570 0.1809 -0.0088 0.0196  0.0021  142 VAL   A CB  
2950 C CG1 . VAL   A 142 ? 0.1488 0.1513 0.1995 -0.0191 0.0258  0.0014  142 VAL   A CG1 
2951 C CG2 . VAL   A 142 ? 0.1619 0.1785 0.2127 -0.0077 0.0196  0.0050  142 VAL   A CG2 
2961 N N   . CYS   A 143 ? 0.1300 0.1507 0.1735 -0.0174 0.0073  0.0097  143 CYS   A N   
2962 C CA  . CYS   A 143 ? 0.1268 0.1504 0.1737 -0.0141 0.0079  0.0181  143 CYS   A CA  
2963 C C   . CYS   A 143 ? 0.1322 0.1466 0.1772 -0.0140 0.0046  0.0269  143 CYS   A C   
2964 O O   . CYS   A 143 ? 0.1312 0.1480 0.1813 -0.0047 0.0050  0.0231  143 CYS   A O   
2965 C CB  . CYS   A 143 ? 0.1365 0.1521 0.1849 -0.0089 0.0201  0.0245  143 CYS   A CB  
2966 S SG  . CYS   A 143 ? 0.1546 0.1610 0.1765 0.0041  0.0130  0.0155  143 CYS   A SG  
2972 N N   . VAL   A 144 ? 0.1294 0.1531 0.1954 -0.0116 0.0128  0.0323  144 VAL   A N   
2973 C CA  . VAL   A 144 ? 0.1345 0.1611 0.2314 -0.0195 0.0200  0.0320  144 VAL   A CA  
2974 C C   . VAL   A 144 ? 0.1366 0.1529 0.2217 -0.0199 -0.0063 0.0261  144 VAL   A C   
2975 O O   . VAL   A 144 ? 0.1529 0.1596 0.2297 -0.0082 -0.0082 0.0300  144 VAL   A O   
2976 C CB  . VAL   A 144 ? 0.1603 0.1843 0.3070 -0.0050 0.0368  0.0356  144 VAL   A CB  
2977 C CG1 . VAL   A 144 ? 0.1794 0.2038 0.3519 -0.0158 0.0148  0.0456  144 VAL   A CG1 
2978 C CG2 . VAL   A 144 ? 0.1431 0.1885 0.3073 -0.0035 0.0367  0.0410  144 VAL   A CG2 
2988 N N   . ASP   A 145 ? 0.1426 0.1512 0.2304 -0.0199 0.0012  0.0161  145 ASP   A N   
2989 C CA  . ASP   A 145 ? 0.1571 0.1526 0.2350 -0.0240 -0.0042 0.0008  145 ASP   A CA  
2990 C C   . ASP   A 145 ? 0.1536 0.1449 0.2387 -0.0120 0.0012  -0.0025 145 ASP   A C   
2991 O O   . ASP   A 145 ? 0.1699 0.1478 0.3045 -0.0117 0.0001  -0.0325 145 ASP   A O   
2992 C CB  . ASP   A 145 ? 0.1710 0.1844 0.2565 -0.0300 -0.0114 0.0011  145 ASP   A CB  
2993 C CG  . ASP   A 145 ? 0.1886 0.2272 0.2871 -0.0439 -0.0240 0.0164  145 ASP   A CG  
2994 O OD1 . ASP   A 145 ? 0.1791 0.2375 0.2885 -0.0578 -0.0227 0.0159  145 ASP   A OD1 
2995 O OD2 . ASP   A 145 ? 0.2075 0.2523 0.2998 -0.0549 -0.0403 0.0189  145 ASP   A OD2 
3000 N N   . THR   A 146 ? 0.1350 0.1442 0.1951 -0.0174 0.0089  0.0039  146 THR   A N   
3001 C CA  . THR   A 146 ? 0.1371 0.1399 0.1898 -0.0076 0.0035  0.0001  146 THR   A CA  
3002 C C   . THR   A 146 ? 0.1333 0.1342 0.1912 0.0015  0.0055  0.0087  146 THR   A C   
3003 O O   . THR   A 146 ? 0.1466 0.1488 0.2060 0.0066  0.0001  0.0100  146 THR   A O   
3004 C CB  . THR   A 146 ? 0.1312 0.1425 0.1915 -0.0047 0.0018  0.0156  146 THR   A CB  
3005 O OG1 . THR   A 146 ? 0.1344 0.1585 0.1943 0.0018  0.0001  0.0099  146 THR   A OG1 
3006 C CG2 . THR   A 146 ? 0.1353 0.1448 0.2112 -0.0072 0.0098  0.0096  146 THR   A CG2 
3014 N N   . VAL   A 147 ? 0.1281 0.1363 0.1897 -0.0010 0.0082  0.0113  147 VAL   A N   
3015 C CA  . VAL   A 147 ? 0.1291 0.1430 0.1946 -0.0079 0.0234  0.0188  147 VAL   A CA  
3016 C C   . VAL   A 147 ? 0.1340 0.1426 0.2033 -0.0087 0.0196  0.0253  147 VAL   A C   
3017 O O   . VAL   A 147 ? 0.1382 0.1496 0.2096 -0.0175 0.0080  0.0274  147 VAL   A O   
3018 C CB  . VAL   A 147 ? 0.1388 0.1429 0.1930 -0.0132 0.0259  0.0186  147 VAL   A CB  
3019 C CG1 . VAL   A 147 ? 0.1665 0.1431 0.2056 -0.0105 0.0187  0.0248  147 VAL   A CG1 
3020 C CG2 . VAL   A 147 ? 0.1528 0.1473 0.1847 -0.0178 0.0116  0.0112  147 VAL   A CG2 
3030 N N   . ARG   A 148 ? 0.1376 0.1471 0.2117 -0.0173 0.0170  0.0376  148 ARG   A N   
3031 C CA  . ARG   A 148 ? 0.1438 0.1453 0.2026 -0.0165 0.0030  0.0419  148 ARG   A CA  
3032 C C   . ARG   A 148 ? 0.1490 0.1518 0.2100 -0.0191 0.0063  0.0572  148 ARG   A C   
3033 O O   . ARG   A 148 ? 0.1797 0.1654 0.2281 -0.0226 0.0131  0.0505  148 ARG   A O   
3034 C CB  . ARG   A 148 ? 0.1485 0.1422 0.2179 -0.0093 0.0176  0.0347  148 ARG   A CB  
3035 C CG  . ARG   A 148 ? 0.1676 0.1473 0.2510 -0.0134 0.0294  0.0336  148 ARG   A CG  
3036 C CD  . ARG   A 148 ? 0.1819 0.1508 0.2781 -0.0042 0.0384  0.0483  148 ARG   A CD  
3037 N NE  . ARG   A 148 ? 0.1726 0.1551 0.2729 0.0104  0.0460  0.0496  148 ARG   A NE  
3038 C CZ  . ARG   A 148 ? 0.1712 0.1438 0.2623 0.0034  0.0465  0.0421  148 ARG   A CZ  
3039 N NH1 . ARG   A 148 ? 0.1751 0.1447 0.2728 -0.0031 0.0415  0.0227  148 ARG   A NH1 
3040 N NH2 . ARG   A 148 ? 0.1611 0.1564 0.2727 0.0141  0.0544  0.0463  148 ARG   A NH2 
3054 N N   . THR   A 149 ? 0.1524 0.1599 0.2013 -0.0187 0.0000  0.0424  149 THR   A N   
3055 C CA  . THR   A 149 ? 0.1517 0.1609 0.2051 -0.0155 0.0087  0.0438  149 THR   A CA  
3056 C C   . THR   A 149 ? 0.1455 0.1626 0.1872 -0.0227 0.0091  0.0504  149 THR   A C   
3057 O O   . THR   A 149 ? 0.1449 0.1742 0.1978 -0.0257 0.0025  0.0502  149 THR   A O   
3058 C CB  . THR   A 149 ? 0.1510 0.1770 0.2023 -0.0150 0.0067  0.0402  149 THR   A CB  
3059 O OG1 . THR   A 149 ? 0.1541 0.1642 0.2141 -0.0258 0.0063  0.0319  149 THR   A OG1 
3060 C CG2 . THR   A 149 ? 0.1453 0.1871 0.2133 -0.0058 -0.0084 0.0327  149 THR   A CG2 
3068 N N   . ASN   A 150 ? 0.1499 0.1639 0.1852 -0.0078 -0.0026 0.0549  150 ASN   A N   
3069 C CA  . ASN   A 150 ? 0.1634 0.1734 0.1814 -0.0117 0.0092  0.0491  150 ASN   A CA  
3070 C C   . ASN   A 150 ? 0.1466 0.1653 0.1840 -0.0161 -0.0007 0.0475  150 ASN   A C   
3071 O O   . ASN   A 150 ? 0.1536 0.1776 0.2231 -0.0182 -0.0162 0.0411  150 ASN   A O   
3072 C CB  . ASN   A 150 ? 0.1970 0.1970 0.2191 -0.0205 0.0312  0.0676  150 ASN   A CB  
3073 C CG  . ASN   A 150 ? 0.2572 0.2360 0.2915 -0.0210 0.0108  0.0740  150 ASN   A CG  
3074 O OD1 . ASN   A 150 ? 0.2817 0.2437 0.3020 -0.0330 0.0099  0.0974  150 ASN   A OD1 
3075 N ND2 . ASN   A 150 ? 0.2922 0.2614 0.3333 -0.0103 -0.0071 0.0708  150 ASN   A ND2 
3082 N N   . VAL   A 151 ? 0.1464 0.1551 0.1825 -0.0146 0.0001  0.0417  151 VAL   A N   
3083 C CA  . VAL   A 151 ? 0.1490 0.1563 0.1748 -0.0103 0.0071  0.0444  151 VAL   A CA  
3084 C C   . VAL   A 151 ? 0.1344 0.1500 0.1869 -0.0245 0.0064  0.0440  151 VAL   A C   
3085 O O   . VAL   A 151 ? 0.1477 0.1635 0.2175 -0.0220 0.0109  0.0370  151 VAL   A O   
3086 C CB  . VAL   A 151 ? 0.1715 0.1748 0.1816 0.0035  0.0111  0.0460  151 VAL   A CB  
3087 C CG1 . VAL   A 151 ? 0.1712 0.1982 0.2134 -0.0079 0.0014  0.0282  151 VAL   A CG1 
3088 C CG2 . VAL   A 151 ? 0.1821 0.1780 0.1734 -0.0000 0.0175  0.0394  151 VAL   A CG2 
3098 N N   . TYR   A 152 ? 0.1386 0.1514 0.1900 -0.0235 0.0070  0.0339  152 TYR   A N   
3099 C CA  . TYR   A 152 ? 0.1460 0.1562 0.1653 -0.0219 0.0041  0.0324  152 TYR   A CA  
3100 C C   . TYR   A 152 ? 0.1363 0.1554 0.1565 -0.0188 0.0151  0.0331  152 TYR   A C   
3101 O O   . TYR   A 152 ? 0.1478 0.1551 0.1624 -0.0270 0.0142  0.0331  152 TYR   A O   
3102 C CB  . TYR   A 152 ? 0.1638 0.1665 0.1607 -0.0201 0.0154  0.0350  152 TYR   A CB  
3103 C CG  . TYR   A 152 ? 0.1702 0.1857 0.1547 -0.0186 0.0229  0.0423  152 TYR   A CG  
3104 C CD1 . TYR   A 152 ? 0.1808 0.2095 0.1801 -0.0098 0.0291  0.0517  152 TYR   A CD1 
3105 C CD2 . TYR   A 152 ? 0.1806 0.2023 0.1536 -0.0335 0.0151  0.0393  152 TYR   A CD2 
3106 C CE1 . TYR   A 152 ? 0.2119 0.2284 0.1859 -0.0029 0.0062  0.0655  152 TYR   A CE1 
3107 C CE2 . TYR   A 152 ? 0.2058 0.2210 0.1758 -0.0354 0.0184  0.0483  152 TYR   A CE2 
3108 C CZ  . TYR   A 152 ? 0.2296 0.2282 0.1812 -0.0213 0.0083  0.0790  152 TYR   A CZ  
3109 O OH  . TYR   A 152 ? 0.2648 0.2517 0.2184 -0.0207 0.0134  0.0951  152 TYR   A OH  
3119 N N   A LEU   A 153 ? 0.1344 0.1501 0.1674 -0.0237 0.0188  0.0329  153 LEU   A N   
3120 N N   B LEU   A 153 ? 0.1396 0.1519 0.1474 -0.0216 0.0084  0.0346  153 LEU   A N   
3121 C CA  A LEU   A 153 ? 0.1288 0.1431 0.1684 -0.0116 0.0171  0.0345  153 LEU   A CA  
3122 C CA  B LEU   A 153 ? 0.1388 0.1461 0.1352 -0.0151 0.0068  0.0322  153 LEU   A CA  
3123 C C   A LEU   A 153 ? 0.1358 0.1431 0.1694 -0.0130 0.0285  0.0280  153 LEU   A C   
3124 C C   B LEU   A 153 ? 0.1424 0.1505 0.1334 -0.0137 0.0122  0.0255  153 LEU   A C   
3125 O O   A LEU   A 153 ? 0.1432 0.1527 0.2097 -0.0112 0.0363  0.0170  153 LEU   A O   
3126 O O   B LEU   A 153 ? 0.1483 0.1607 0.1499 -0.0160 0.0336  0.0276  153 LEU   A O   
3127 C CB  A LEU   A 153 ? 0.1214 0.1425 0.1826 -0.0147 0.0144  0.0296  153 LEU   A CB  
3128 C CB  B LEU   A 153 ? 0.1355 0.1471 0.1392 -0.0082 0.0049  0.0377  153 LEU   A CB  
3129 C CG  A LEU   A 153 ? 0.1277 0.1443 0.1789 -0.0114 0.0266  0.0171  153 LEU   A CG  
3130 C CG  B LEU   A 153 ? 0.1440 0.1557 0.1375 -0.0032 0.0095  0.0313  153 LEU   A CG  
3131 C CD1 A LEU   A 153 ? 0.1376 0.1423 0.1889 -0.0060 0.0102  0.0216  153 LEU   A CD1 
3132 C CD1 B LEU   A 153 ? 0.1477 0.1587 0.1458 0.0013  0.0098  0.0286  153 LEU   A CD1 
3133 C CD2 A LEU   A 153 ? 0.1354 0.1502 0.1740 -0.0174 0.0174  0.0008  153 LEU   A CD2 
3134 C CD2 B LEU   A 153 ? 0.1500 0.1642 0.1407 -0.0052 0.0062  0.0252  153 LEU   A CD2 
3157 N N   A ALA   A 154 ? 0.1349 0.1396 0.1620 -0.0105 0.0232  0.0314  154 ALA   A N   
3158 N N   B ALA   A 154 ? 0.1392 0.1463 0.1046 -0.0104 0.0078  0.0150  154 ALA   A N   
3159 C CA  A ALA   A 154 ? 0.1414 0.1438 0.1487 -0.0114 0.0210  0.0206  154 ALA   A CA  
3160 C CA  B ALA   A 154 ? 0.1435 0.1511 0.1159 -0.0086 0.0021  0.0037  154 ALA   A CA  
3161 C C   A ALA   A 154 ? 0.1386 0.1397 0.1424 -0.0072 0.0181  0.0248  154 ALA   A C   
3162 C C   B ALA   A 154 ? 0.1410 0.1533 0.1097 -0.0120 -0.0045 0.0081  154 ALA   A C   
3163 O O   A ALA   A 154 ? 0.1454 0.1568 0.1589 -0.0130 0.0195  0.0226  154 ALA   A O   
3164 O O   B ALA   A 154 ? 0.1458 0.1587 0.0925 -0.0131 -0.0020 0.0142  154 ALA   A O   
3165 C CB  A ALA   A 154 ? 0.1613 0.1563 0.1536 -0.0034 0.0177  0.0155  154 ALA   A CB  
3166 C CB  B ALA   A 154 ? 0.1498 0.1502 0.1164 -0.0097 -0.0107 -0.0095 154 ALA   A CB  
3177 N N   A VAL   A 155 ? 0.1163 0.1059 0.0996 0.0041  0.0220  0.0340  155 VAL   A N   
3178 N N   B VAL   A 155 ? 0.1373 0.1421 0.1186 -0.0118 -0.0071 0.0077  155 VAL   A N   
3179 C CA  A VAL   A 155 ? 0.1316 0.1286 0.1581 0.0011  0.0226  0.0369  155 VAL   A CA  
3180 C CA  B VAL   A 155 ? 0.1533 0.1506 0.1336 -0.0091 -0.0129 0.0030  155 VAL   A CA  
3181 C CA  T VAL   A 155 ? 0.1669 0.1671 0.1747 -0.0044 0.0268  0.0227  155 VAL   A CA  
3182 C C   A VAL   A 155 ? 0.1448 0.1389 0.1907 0.0085  0.0267  0.0484  155 VAL   A C   
3183 C C   B VAL   A 155 ? 0.1611 0.1623 0.1643 0.0019  -0.0207 0.0096  155 VAL   A C   
3184 C C   T VAL   A 155 ? 0.1727 0.1649 0.1621 0.0082  0.0348  0.0282  155 VAL   A C   
3185 O O   A VAL   A 155 ? 0.1402 0.1332 0.2145 0.0106  0.0320  0.0349  155 VAL   A O   
3186 O O   B VAL   A 155 ? 0.1633 0.1704 0.1596 0.0030  -0.0234 -0.0097 155 VAL   A O   
3187 O O   T VAL   A 155 ? 0.1714 0.1707 0.1662 0.0140  0.0345  0.0154  155 VAL   A O   
3188 C CB  A VAL   A 155 ? 0.1490 0.1366 0.1607 0.0065  0.0053  0.0277  155 VAL   A CB  
3189 C CB  B VAL   A 155 ? 0.1624 0.1510 0.1353 -0.0026 -0.0164 -0.0043 155 VAL   A CB  
3190 C CB  T VAL   A 155 ? 0.1679 0.1690 0.1740 -0.0080 0.0109  0.0173  155 VAL   A CB  
3191 C CG1 A VAL   A 155 ? 0.1619 0.1443 0.1586 0.0100  -0.0065 0.0234  155 VAL   A CG1 
3192 C CG1 B VAL   A 155 ? 0.1599 0.1486 0.1337 -0.0012 -0.0175 -0.0005 155 VAL   A CG1 
3193 C CG1 T VAL   A 155 ? 0.1744 0.1727 0.1689 -0.0046 0.0088  0.0150  155 VAL   A CG1 
3194 C CG2 A VAL   A 155 ? 0.1672 0.1429 0.1916 0.0105  -0.0108 0.0282  155 VAL   A CG2 
3195 C CG2 B VAL   A 155 ? 0.1774 0.1533 0.1413 0.0001  -0.0196 -0.0075 155 VAL   A CG2 
3196 C CG2 T VAL   A 155 ? 0.1696 0.1714 0.1884 -0.0107 -0.0019 0.0185  155 VAL   A CG2 
3222 N N   A PHE   A 156 ? 0.1675 0.1573 0.2330 0.0168  0.0316  0.0683  156 PHE   A N   
3223 N N   B PHE   A 156 ? 0.1684 0.1653 0.1965 0.0103  -0.0210 0.0301  156 PHE   A N   
3224 N N   T PHE   A 156 ? 0.1860 0.1588 0.1707 0.0132  0.0453  0.0473  156 PHE   A N   
3225 C CA  A PHE   A 156 ? 0.1959 0.1760 0.2834 0.0294  0.0309  0.0690  156 PHE   A CA  
3226 C CA  B PHE   A 156 ? 0.1836 0.1759 0.2413 0.0196  -0.0121 0.0408  156 PHE   A CA  
3227 C CA  T PHE   A 156 ? 0.2051 0.1529 0.1765 0.0172  0.0498  0.0571  156 PHE   A CA  
3228 C C   A PHE   A 156 ? 0.2003 0.1797 0.2960 0.0445  0.0409  0.0732  156 PHE   A C   
3229 C C   B PHE   A 156 ? 0.1781 0.1857 0.2456 0.0216  0.0053  0.0508  156 PHE   A C   
3230 C C   T PHE   A 156 ? 0.2041 0.1689 0.1994 0.0192  0.0621  0.0631  156 PHE   A C   
3231 O O   A PHE   A 156 ? 0.2103 0.1876 0.3079 0.0402  0.0496  0.0667  156 PHE   A O   
3232 O O   B PHE   A 156 ? 0.1880 0.1925 0.2583 0.0186  0.0198  0.0507  156 PHE   A O   
3233 O O   T PHE   A 156 ? 0.2085 0.1742 0.2045 0.0218  0.0669  0.0509  156 PHE   A O   
3234 C CB  A PHE   A 156 ? 0.2172 0.1932 0.3089 0.0214  0.0231  0.0679  156 PHE   A CB  
3235 C CB  B PHE   A 156 ? 0.2017 0.1867 0.2727 0.0174  -0.0183 0.0393  156 PHE   A CB  
3236 C CB  T PHE   A 156 ? 0.2129 0.1332 0.1568 0.0158  0.0468  0.0518  156 PHE   A CB  
3237 C CG  A PHE   A 156 ? 0.2392 0.2074 0.3295 0.0247  0.0156  0.0560  156 PHE   A CG  
3238 C CG  B PHE   A 156 ? 0.2188 0.1938 0.2929 0.0215  -0.0269 0.0275  156 PHE   A CG  
3239 C CG  T PHE   A 156 ? 0.2219 0.1241 0.1514 0.0177  0.0376  0.0574  156 PHE   A CG  
3240 C CD1 A PHE   A 156 ? 0.2462 0.2096 0.3364 0.0315  0.0174  0.0507  156 PHE   A CD1 
3241 C CD1 B PHE   A 156 ? 0.2235 0.2043 0.3001 0.0206  -0.0260 0.0177  156 PHE   A CD1 
3242 C CD1 T PHE   A 156 ? 0.2271 0.1299 0.1721 0.0205  0.0270  0.0439  156 PHE   A CD1 
3243 C CD2 A PHE   A 156 ? 0.2488 0.2223 0.3361 0.0322  0.0095  0.0475  156 PHE   A CD2 
3244 C CD2 B PHE   A 156 ? 0.2245 0.1958 0.3001 0.0255  -0.0300 0.0186  156 PHE   A CD2 
3245 C CD2 T PHE   A 156 ? 0.2256 0.1207 0.1628 0.0192  0.0369  0.0727  156 PHE   A CD2 
3246 C CE1 A PHE   A 156 ? 0.2540 0.2151 0.3450 0.0361  0.0187  0.0449  156 PHE   A CE1 
3247 C CE1 B PHE   A 156 ? 0.2264 0.2047 0.3025 0.0217  -0.0274 0.0093  156 PHE   A CE1 
3248 C CE1 T PHE   A 156 ? 0.2307 0.1305 0.1950 0.0193  0.0292  0.0344  156 PHE   A CE1 
3249 C CE2 A PHE   A 156 ? 0.2590 0.2301 0.3458 0.0364  0.0102  0.0331  156 PHE   A CE2 
3250 C CE2 B PHE   A 156 ? 0.2295 0.2004 0.3085 0.0245  -0.0290 0.0067  156 PHE   A CE2 
3251 C CE2 T PHE   A 156 ? 0.2316 0.1263 0.1814 0.0170  0.0339  0.0584  156 PHE   A CE2 
3252 C CZ  A PHE   A 156 ? 0.2616 0.2270 0.3489 0.0378  0.0172  0.0343  156 PHE   A CZ  
3253 C CZ  B PHE   A 156 ? 0.2304 0.2017 0.3076 0.0243  -0.0236 0.0054  156 PHE   A CZ  
3254 C CZ  T PHE   A 156 ? 0.2305 0.1211 0.1960 0.0127  0.0368  0.0423  156 PHE   A CZ  
3282 N N   A ASP   A 157 ? 0.1960 0.1831 0.2923 0.0548  0.0414  0.0758  157 ASP   A N   
3283 N N   B ASP   A 157 ? 0.1610 0.1874 0.2314 0.0205  0.0042  0.0519  157 ASP   A N   
3284 N N   T ASP   A 157 ? 0.1939 0.1830 0.2239 0.0153  0.0540  0.0741  157 ASP   A N   
3285 C CA  A ASP   A 157 ? 0.2083 0.2043 0.2966 0.0567  0.0397  0.0796  157 ASP   A CA  
3286 C CA  B ASP   A 157 ? 0.1607 0.1983 0.2257 0.0192  0.0078  0.0600  157 ASP   A CA  
3287 C CA  T ASP   A 157 ? 0.1941 0.2023 0.2372 0.0212  0.0451  0.0781  157 ASP   A CA  
3288 C C   A ASP   A 157 ? 0.1977 0.2220 0.3035 0.0507  0.0425  0.0923  157 ASP   A C   
3289 C C   B ASP   A 157 ? 0.1580 0.2113 0.2231 0.0348  0.0159  0.0738  157 ASP   A C   
3290 C C   T ASP   A 157 ? 0.1923 0.2226 0.2466 0.0254  0.0452  0.0872  157 ASP   A C   
3291 O O   A ASP   A 157 ? 0.1856 0.2204 0.2992 0.0437  0.0387  0.0916  157 ASP   A O   
3292 O O   B ASP   A 157 ? 0.1565 0.2085 0.2227 0.0400  0.0124  0.0755  157 ASP   A O   
3293 O O   T ASP   A 157 ? 0.1797 0.2216 0.2456 0.0208  0.0454  0.0869  157 ASP   A O   
3294 C CB  A ASP   A 157 ? 0.2277 0.2131 0.3019 0.0655  0.0352  0.0715  157 ASP   A CB  
3295 C CB  B ASP   A 157 ? 0.1603 0.1965 0.2270 0.0065  -0.0011 0.0592  157 ASP   A CB  
3296 C CB  T ASP   A 157 ? 0.1940 0.2024 0.2479 0.0266  0.0356  0.0759  157 ASP   A CB  
3297 C CG  A ASP   A 157 ? 0.2452 0.2210 0.3178 0.0681  0.0312  0.0691  157 ASP   A CG  
3298 C CG  B ASP   A 157 ? 0.1548 0.1914 0.2369 0.0022  -0.0084 0.0632  157 ASP   A CG  
3299 C CG  T ASP   A 157 ? 0.1860 0.1906 0.2547 0.0337  0.0241  0.0777  157 ASP   A CG  
3300 O OD1 A ASP   A 157 ? 0.2606 0.2275 0.3351 0.0648  0.0270  0.0608  157 ASP   A OD1 
3301 O OD1 B ASP   A 157 ? 0.1467 0.1808 0.2451 -0.0051 -0.0163 0.0515  157 ASP   A OD1 
3302 O OD1 T ASP   A 157 ? 0.1830 0.1896 0.2705 0.0332  0.0195  0.0634  157 ASP   A OD1 
3303 O OD2 A ASP   A 157 ? 0.2431 0.2194 0.3189 0.0694  0.0355  0.0773  157 ASP   A OD2 
3304 O OD2 B ASP   A 157 ? 0.1577 0.1978 0.2450 0.0090  -0.0055 0.0673  157 ASP   A OD2 
3305 O OD2 T ASP   A 157 ? 0.1785 0.1822 0.2478 0.0450  0.0244  0.0826  157 ASP   A OD2 
3318 N N   A LYS   A 158 ? 0.2104 0.2451 0.3213 0.0446  0.0564  0.0896  158 LYS   A N   
3319 N N   B LYS   A 158 ? 0.1646 0.2269 0.2253 0.0373  0.0295  0.0741  158 LYS   A N   
3320 N N   T LYS   A 158 ? 0.2108 0.2462 0.2648 0.0279  0.0495  0.0800  158 LYS   A N   
3321 C CA  A LYS   A 158 ? 0.2102 0.2703 0.3354 0.0444  0.0702  0.0827  158 LYS   A CA  
3322 C CA  B LYS   A 158 ? 0.1651 0.2414 0.2343 0.0414  0.0324  0.0659  158 LYS   A CA  
3323 C CA  T LYS   A 158 ? 0.2235 0.2702 0.2883 0.0330  0.0498  0.0679  158 LYS   A CA  
3324 C C   A LYS   A 158 ? 0.1905 0.2791 0.3177 0.0466  0.0593  0.0941  158 LYS   A C   
3325 C C   B LYS   A 158 ? 0.1612 0.2450 0.2337 0.0482  0.0225  0.0780  158 LYS   A C   
3326 C C   T LYS   A 158 ? 0.2194 0.2760 0.2818 0.0337  0.0382  0.0714  158 LYS   A C   
3327 O O   A LYS   A 158 ? 0.1880 0.2865 0.3218 0.0394  0.0615  0.0959  158 LYS   A O   
3328 O O   B LYS   A 158 ? 0.1609 0.2513 0.2369 0.0413  0.0316  0.0771  158 LYS   A O   
3329 O O   T LYS   A 158 ? 0.2192 0.2805 0.2864 0.0316  0.0374  0.0716  158 LYS   A O   
3330 C CB  A LYS   A 158 ? 0.2315 0.2820 0.3632 0.0392  0.0916  0.0784  158 LYS   A CB  
3331 C CB  B LYS   A 158 ? 0.1775 0.2497 0.2575 0.0332  0.0416  0.0492  158 LYS   A CB  
3332 C CB  T LYS   A 158 ? 0.2434 0.2840 0.3229 0.0345  0.0608  0.0597  158 LYS   A CB  
3333 C CG  A LYS   A 158 ? 0.2562 0.2949 0.3853 0.0364  0.1028  0.0754  158 LYS   A CG  
3334 C CG  B LYS   A 158 ? 0.1890 0.2562 0.2731 0.0260  0.0465  0.0355  158 LYS   A CG  
3335 C CG  T LYS   A 158 ? 0.2624 0.2962 0.3513 0.0362  0.0682  0.0546  158 LYS   A CG  
3336 C CD  A LYS   A 158 ? 0.2734 0.3032 0.3950 0.0368  0.1170  0.0785  158 LYS   A CD  
3337 C CD  B LYS   A 158 ? 0.1961 0.2580 0.2838 0.0256  0.0512  0.0262  158 LYS   A CD  
3338 C CD  T LYS   A 158 ? 0.2772 0.3042 0.3742 0.0401  0.0742  0.0546  158 LYS   A CD  
3339 C CE  A LYS   A 158 ? 0.2838 0.3059 0.3962 0.0330  0.1246  0.0879  158 LYS   A CE  
3340 C CE  B LYS   A 158 ? 0.1998 0.2566 0.2880 0.0255  0.0480  0.0217  158 LYS   A CE  
3341 C CE  T LYS   A 158 ? 0.2882 0.3089 0.3890 0.0418  0.0748  0.0567  158 LYS   A CE  
3342 N NZ  A LYS   A 158 ? 0.2853 0.3059 0.3951 0.0286  0.1312  0.0933  158 LYS   A NZ  
3343 N NZ  B LYS   A 158 ? 0.2006 0.2532 0.2861 0.0260  0.0465  0.0203  158 LYS   A NZ  
3344 N NZ  T LYS   A 158 ? 0.2941 0.3110 0.3946 0.0443  0.0750  0.0575  158 LYS   A NZ  
3384 N N   A ASN   A 159 ? 0.1823 0.2807 0.3189 0.0453  0.0394  0.0945  159 ASN   A N   
3385 N N   B ASN   A 159 ? 0.1673 0.2478 0.2508 0.0505  0.0108  0.0737  159 ASN   A N   
3386 N N   T ASN   A 159 ? 0.2212 0.2787 0.2892 0.0305  0.0272  0.0666  159 ASN   A N   
3387 C CA  A ASN   A 159 ? 0.1746 0.2800 0.3016 0.0395  0.0164  0.1108  159 ASN   A CA  
3388 C CA  B ASN   A 159 ? 0.1761 0.2520 0.2634 0.0447  0.0039  0.0750  159 ASN   A CA  
3389 C CA  T ASN   A 159 ? 0.2245 0.2802 0.2866 0.0232  0.0187  0.0730  159 ASN   A CA  
3390 C C   A ASN   A 159 ? 0.1569 0.2773 0.2771 0.0266  0.0090  0.0999  159 ASN   A C   
3391 C C   B ASN   A 159 ? 0.1704 0.2512 0.2509 0.0332  0.0097  0.0591  159 ASN   A C   
3392 C C   T ASN   A 159 ? 0.2232 0.2796 0.2727 0.0113  0.0231  0.0649  159 ASN   A C   
3393 O O   A ASN   A 159 ? 0.1337 0.2779 0.2584 0.0299  -0.0191 0.0819  159 ASN   A O   
3394 O O   B ASN   A 159 ? 0.1667 0.2517 0.2520 0.0279  0.0087  0.0400  159 ASN   A O   
3395 O O   T ASN   A 159 ? 0.2205 0.2808 0.2642 0.0091  0.0197  0.0521  159 ASN   A O   
3396 C CB  A ASN   A 159 ? 0.1924 0.2885 0.3347 0.0388  0.0111  0.1208  159 ASN   A CB  
3397 C CB  B ASN   A 159 ? 0.1956 0.2606 0.3026 0.0468  -0.0032 0.0814  159 ASN   A CB  
3398 C CB  T ASN   A 159 ? 0.2336 0.2855 0.3142 0.0250  0.0101  0.0802  159 ASN   A CB  
3399 C CG  A ASN   A 159 ? 0.2108 0.3012 0.3790 0.0350  0.0122  0.1147  159 ASN   A CG  
3400 C CG  B ASN   A 159 ? 0.2121 0.2691 0.3394 0.0474  -0.0041 0.0791  159 ASN   A CG  
3401 C CG  T ASN   A 159 ? 0.2429 0.2922 0.3469 0.0254  0.0057  0.0800  159 ASN   A CG  
3402 O OD1 A ASN   A 159 ? 0.2221 0.3134 0.4044 0.0346  0.0221  0.1093  159 ASN   A OD1 
3403 O OD1 B ASN   A 159 ? 0.2193 0.2789 0.3601 0.0484  0.0099  0.0726  159 ASN   A OD1 
3404 O OD1 T ASN   A 159 ? 0.2483 0.3003 0.3657 0.0271  0.0124  0.0770  159 ASN   A OD1 
3405 N ND2 A ASN   A 159 ? 0.2176 0.3046 0.3980 0.0319  0.0094  0.1085  159 ASN   A ND2 
3406 N ND2 B ASN   A 159 ? 0.2180 0.2712 0.3552 0.0463  -0.0104 0.0766  159 ASN   A ND2 
3407 N ND2 T ASN   A 159 ? 0.2467 0.2942 0.3613 0.0241  0.0007  0.0774  159 ASN   A ND2 
3426 N N   A LEU   A 160 ? 0.1505 0.2646 0.2603 0.0218  0.0038  0.1108  160 LEU   A N   
3427 N N   B LEU   A 160 ? 0.1622 0.2438 0.2310 0.0330  0.0018  0.0635  160 LEU   A N   
3428 N N   T LEU   A 160 ? 0.2199 0.2732 0.2660 0.0046  0.0223  0.0697  160 LEU   A N   
3429 C CA  A LEU   A 160 ? 0.1542 0.2545 0.2438 0.0097  0.0220  0.1088  160 LEU   A CA  
3430 C CA  B LEU   A 160 ? 0.1626 0.2382 0.2139 0.0245  0.0095  0.0590  160 LEU   A CA  
3431 C CA  T LEU   A 160 ? 0.2220 0.2665 0.2546 -0.0048 0.0294  0.0763  160 LEU   A CA  
3432 C C   A LEU   A 160 ? 0.1364 0.2469 0.2248 0.0068  0.0293  0.0985  160 LEU   A C   
3433 C C   B LEU   A 160 ? 0.1484 0.2251 0.1871 0.0186  0.0177  0.0558  160 LEU   A C   
3434 O O   A LEU   A 160 ? 0.1222 0.2508 0.2179 0.0016  0.0268  0.0991  160 LEU   A O   
3435 O O   B LEU   A 160 ? 0.1380 0.2281 0.1814 0.0189  0.0122  0.0588  160 LEU   A O   
3436 C CB  A LEU   A 160 ? 0.1660 0.2557 0.2371 0.0035  0.0228  0.1115  160 LEU   A CB  
3437 C CB  B LEU   A 160 ? 0.1748 0.2481 0.2192 0.0197  0.0005  0.0522  160 LEU   A CB  
3438 C CB  T LEU   A 160 ? 0.2216 0.2623 0.2403 -0.0131 0.0324  0.0826  160 LEU   A CB  
3439 C CG  A LEU   A 160 ? 0.1733 0.2615 0.2424 -0.0024 0.0199  0.0963  160 LEU   A CG  
3440 C CG  B LEU   A 160 ? 0.1850 0.2596 0.2383 0.0156  -0.0050 0.0335  160 LEU   A CG  
3441 C CG  T LEU   A 160 ? 0.2218 0.2612 0.2349 -0.0201 0.0347  0.0801  160 LEU   A CG  
3442 C CD1 A LEU   A 160 ? 0.1767 0.2659 0.2519 -0.0079 0.0216  0.0811  160 LEU   A CD1 
3443 C CD1 B LEU   A 160 ? 0.1924 0.2654 0.2473 0.0119  -0.0011 0.0262  160 LEU   A CD1 
3444 C CD1 T LEU   A 160 ? 0.2236 0.2649 0.2403 -0.0201 0.0347  0.0697  160 LEU   A CD1 
3445 C CD2 A LEU   A 160 ? 0.1743 0.2610 0.2384 -0.0029 0.0195  0.0949  160 LEU   A CD2 
3446 C CD2 B LEU   A 160 ? 0.1838 0.2604 0.2407 0.0170  -0.0097 0.0266  160 LEU   A CD2 
3447 C CD2 T LEU   A 160 ? 0.2207 0.2570 0.2279 -0.0244 0.0377  0.0837  160 LEU   A CD2 
3480 N N   A TYR   A 161 ? 0.1459 0.2326 0.2433 0.0085  0.0286  0.0911  161 TYR   A N   
3481 N N   B TYR   A 161 ? 0.1529 0.2075 0.1803 0.0120  0.0214  0.0476  161 TYR   A N   
3482 C CA  A TYR   A 161 ? 0.1511 0.2234 0.2425 0.0025  0.0261  0.0826  161 TYR   A CA  
3483 C CA  B TYR   A 161 ? 0.1579 0.1936 0.1673 0.0034  0.0234  0.0344  161 TYR   A CA  
3484 C C   A TYR   A 161 ? 0.1554 0.2365 0.2446 0.0036  0.0175  0.0811  161 TYR   A C   
3485 C C   B TYR   A 161 ? 0.1622 0.1964 0.1706 -0.0074 0.0241  0.0255  161 TYR   A C   
3486 O O   A TYR   A 161 ? 0.1497 0.2379 0.2247 -0.0018 0.0158  0.0760  161 TYR   A O   
3487 O O   B TYR   A 161 ? 0.1607 0.1973 0.1645 -0.0057 0.0318  0.0217  161 TYR   A O   
3488 C CB  A TYR   A 161 ? 0.1597 0.2112 0.2418 -0.0055 0.0358  0.0658  161 TYR   A CB  
3489 C CB  B TYR   A 161 ? 0.1629 0.1821 0.1571 0.0072  0.0284  0.0304  161 TYR   A CB  
3490 C CG  A TYR   A 161 ? 0.1585 0.1958 0.2290 -0.0028 0.0217  0.0438  161 TYR   A CG  
3491 C CG  B TYR   A 161 ? 0.1614 0.1695 0.1535 0.0136  0.0350  0.0245  161 TYR   A CG  
3492 C CD1 A TYR   A 161 ? 0.1582 0.1875 0.2265 -0.0051 0.0183  0.0312  161 TYR   A CD1 
3493 C CD1 B TYR   A 161 ? 0.1659 0.1666 0.1641 0.0137  0.0293  0.0212  161 TYR   A CD1 
3494 C CD2 A TYR   A 161 ? 0.1576 0.1859 0.2238 0.0019  0.0184  0.0436  161 TYR   A CD2 
3495 C CD2 B TYR   A 161 ? 0.1630 0.1631 0.1619 0.0111  0.0403  0.0287  161 TYR   A CD2 
3496 C CE1 A TYR   A 161 ? 0.1515 0.1752 0.2219 0.0015  0.0113  0.0352  161 TYR   A CE1 
3497 C CE1 B TYR   A 161 ? 0.1698 0.1665 0.1748 0.0143  0.0311  0.0207  161 TYR   A CE1 
3498 C CE2 A TYR   A 161 ? 0.1557 0.1670 0.2190 -0.0065 0.0110  0.0435  161 TYR   A CE2 
3499 C CE2 B TYR   A 161 ? 0.1701 0.1662 0.1786 0.0069  0.0418  0.0303  161 TYR   A CE2 
3500 C CZ  A TYR   A 161 ? 0.1588 0.1643 0.2119 -0.0021 0.0010  0.0411  161 TYR   A CZ  
3501 C CZ  B TYR   A 161 ? 0.1785 0.1663 0.1893 0.0095  0.0351  0.0292  161 TYR   A CZ  
3502 O OH  A TYR   A 161 ? 0.1758 0.1570 0.2228 -0.0005 -0.0035 0.0408  161 TYR   A OH  
3503 O OH  B TYR   A 161 ? 0.1935 0.1692 0.2208 0.0096  0.0335  0.0307  161 TYR   A OH  
3522 N N   A ASP   A 162 ? 0.1519 0.2487 0.2618 0.0109  0.0275  0.0836  162 ASP   A N   
3523 N N   B ASP   A 162 ? 0.1622 0.1995 0.1780 -0.0147 0.0243  0.0244  162 ASP   A N   
3524 C CA  A ASP   A 162 ? 0.1473 0.2689 0.2720 0.0094  0.0417  0.0739  162 ASP   A CA  
3525 C CA  B ASP   A 162 ? 0.1669 0.2063 0.1897 -0.0101 0.0215  0.0180  162 ASP   A CA  
3526 C C   A ASP   A 162 ? 0.1426 0.2918 0.2608 0.0040  0.0317  0.0708  162 ASP   A C   
3527 C C   B ASP   A 162 ? 0.1756 0.2206 0.1924 -0.0174 0.0201  0.0107  162 ASP   A C   
3528 O O   A ASP   A 162 ? 0.1441 0.2933 0.2618 0.0019  0.0234  0.0481  162 ASP   A O   
3529 O O   B ASP   A 162 ? 0.1781 0.2198 0.1971 -0.0164 0.0212  -0.0044 162 ASP   A O   
3530 C CB  A ASP   A 162 ? 0.1543 0.2731 0.3083 0.0125  0.0470  0.0612  162 ASP   A CB  
3531 C CB  B ASP   A 162 ? 0.1635 0.2007 0.2057 0.0023  0.0226  0.0212  162 ASP   A CB  
3532 C CG  A ASP   A 162 ? 0.1704 0.2836 0.3366 0.0113  0.0509  0.0465  162 ASP   A CG  
3533 C CG  B ASP   A 162 ? 0.1611 0.1886 0.2042 0.0087  0.0281  0.0332  162 ASP   A CG  
3534 O OD1 A ASP   A 162 ? 0.1888 0.2901 0.3491 0.0055  0.0548  0.0450  162 ASP   A OD1 
3535 O OD1 B ASP   A 162 ? 0.1632 0.1825 0.2121 0.0171  0.0289  0.0346  162 ASP   A OD1 
3536 O OD2 A ASP   A 162 ? 0.1857 0.2867 0.3563 0.0131  0.0577  0.0343  162 ASP   A OD2 
3537 O OD2 B ASP   A 162 ? 0.1655 0.1875 0.2053 0.0116  0.0259  0.0436  162 ASP   A OD2 
3546 N N   A LYS   A 163 ? 0.1501 0.3146 0.2697 0.0001  0.0107  0.0695  163 LYS   A N   
3547 N N   B LYS   A 163 ? 0.1859 0.2410 0.1973 -0.0200 0.0184  0.0084  163 LYS   A N   
3548 C CA  A LYS   A 163 ? 0.1618 0.3344 0.2612 -0.0025 0.0026  0.0648  163 LYS   A CA  
3549 C CA  B LYS   A 163 ? 0.1979 0.2594 0.2134 -0.0210 0.0151  0.0130  163 LYS   A CA  
3550 C C   A LYS   A 163 ? 0.1539 0.3262 0.2430 -0.0144 0.0149  0.0619  163 LYS   A C   
3551 C C   B LYS   A 163 ? 0.1936 0.2527 0.2007 -0.0206 0.0197  0.0115  163 LYS   A C   
3552 O O   A LYS   A 163 ? 0.1441 0.3408 0.2555 -0.0227 0.0101  0.0518  163 LYS   A O   
3553 O O   B LYS   A 163 ? 0.1907 0.2537 0.1930 -0.0221 0.0193  -0.0047 163 LYS   A O   
3554 C CB  A LYS   A 163 ? 0.2005 0.3588 0.2903 0.0209  -0.0187 0.0665  163 LYS   A CB  
3555 C CB  B LYS   A 163 ? 0.2202 0.2822 0.2578 -0.0166 0.0073  0.0196  163 LYS   A CB  
3556 C CG  A LYS   A 163 ? 0.2476 0.3817 0.3533 0.0260  -0.0141 0.0625  163 LYS   A CG  
3557 C CG  B LYS   A 163 ? 0.2422 0.3002 0.3101 -0.0158 0.0045  0.0228  163 LYS   A CG  
3558 C CD  A LYS   A 163 ? 0.2929 0.4004 0.4220 0.0270  -0.0097 0.0590  163 LYS   A CD  
3559 C CD  B LYS   A 163 ? 0.2609 0.3155 0.3574 -0.0148 0.0027  0.0240  163 LYS   A CD  
3560 C CE  A LYS   A 163 ? 0.3254 0.4127 0.4798 0.0254  -0.0030 0.0592  163 LYS   A CE  
3561 C CE  B LYS   A 163 ? 0.2736 0.3275 0.3945 -0.0135 0.0000  0.0238  163 LYS   A CE  
3562 N NZ  A LYS   A 163 ? 0.3409 0.4202 0.5130 0.0233  -0.0001 0.0594  163 LYS   A NZ  
3563 N NZ  B LYS   A 163 ? 0.2804 0.3350 0.4117 -0.0120 -0.0008 0.0271  163 LYS   A NZ  
3590 N N   A LEU   A 164 ? 0.1331 0.2935 0.2126 -0.0199 0.0163  0.0565  164 LEU   A N   
3591 N N   B LEU   A 164 ? 0.1833 0.2389 0.1935 -0.0181 0.0176  0.0202  164 LEU   A N   
3592 C CA  A LEU   A 164 ? 0.1443 0.2689 0.1916 -0.0307 0.0308  0.0508  164 LEU   A CA  
3593 C CA  B LEU   A 164 ? 0.1808 0.2277 0.1800 -0.0183 0.0183  0.0202  164 LEU   A CA  
3594 C C   A LEU   A 164 ? 0.1555 0.2668 0.1871 -0.0313 0.0267  0.0400  164 LEU   A C   
3595 C C   B LEU   A 164 ? 0.1773 0.2214 0.1815 -0.0219 0.0188  0.0190  164 LEU   A C   
3596 O O   A LEU   A 164 ? 0.1626 0.2621 0.1895 -0.0395 0.0395  0.0213  164 LEU   A O   
3597 O O   B LEU   A 164 ? 0.1792 0.2177 0.1922 -0.0281 0.0253  0.0214  164 LEU   A O   
3598 C CB  A LEU   A 164 ? 0.1414 0.2531 0.2039 -0.0322 0.0285  0.0513  164 LEU   A CB  
3599 C CB  B LEU   A 164 ? 0.1782 0.2230 0.1774 -0.0112 0.0185  0.0188  164 LEU   A CB  
3600 C CG  A LEU   A 164 ? 0.1494 0.2433 0.2158 -0.0264 0.0133  0.0490  164 LEU   A CG  
3601 C CG  B LEU   A 164 ? 0.1826 0.2229 0.1877 -0.0057 0.0212  0.0272  164 LEU   A CG  
3602 C CD1 A LEU   A 164 ? 0.1345 0.2301 0.2106 -0.0241 0.0058  0.0651  164 LEU   A CD1 
3603 C CD1 B LEU   A 164 ? 0.1813 0.2215 0.1982 -0.0018 0.0192  0.0312  164 LEU   A CD1 
3604 C CD2 A LEU   A 164 ? 0.1652 0.2459 0.2090 -0.0284 0.0356  0.0388  164 LEU   A CD2 
3605 C CD2 B LEU   A 164 ? 0.1859 0.2245 0.1771 -0.0072 0.0364  0.0323  164 LEU   A CD2 
3628 N N   A VAL   A 165 ? 0.1486 0.2699 0.1813 -0.0273 0.0252  0.0511  165 VAL   A N   
3629 N N   B VAL   A 165 ? 0.1672 0.2212 0.1809 -0.0229 0.0162  0.0194  165 VAL   A N   
3630 C CA  A VAL   A 165 ? 0.1586 0.2746 0.1727 -0.0290 0.0237  0.0579  165 VAL   A CA  
3631 C CA  B VAL   A 165 ? 0.1644 0.2239 0.1840 -0.0182 0.0124  0.0213  165 VAL   A CA  
3632 C C   A VAL   A 165 ? 0.1562 0.2845 0.1779 -0.0241 0.0239  0.0586  165 VAL   A C   
3633 C C   B VAL   A 165 ? 0.1563 0.2239 0.1826 -0.0194 0.0151  0.0242  165 VAL   A C   
3634 O O   A VAL   A 165 ? 0.1520 0.2828 0.1729 -0.0291 0.0316  0.0435  165 VAL   A O   
3635 O O   B VAL   A 165 ? 0.1581 0.2189 0.1764 -0.0225 0.0155  0.0165  165 VAL   A O   
3636 C CB  A VAL   A 165 ? 0.1763 0.2678 0.1848 -0.0373 0.0257  0.0587  165 VAL   A CB  
3637 C CB  B VAL   A 165 ? 0.1688 0.2263 0.1913 -0.0117 0.0081  0.0187  165 VAL   A CB  
3638 C CG1 A VAL   A 165 ? 0.1819 0.2706 0.1805 -0.0415 0.0303  0.0482  165 VAL   A CG1 
3639 C CG1 B VAL   A 165 ? 0.1709 0.2269 0.1880 -0.0111 0.0068  0.0078  165 VAL   A CG1 
3640 C CG2 A VAL   A 165 ? 0.1850 0.2606 0.2048 -0.0330 0.0190  0.0716  165 VAL   A CG2 
3641 C CG2 B VAL   A 165 ? 0.1688 0.2257 0.2021 -0.0093 0.0020  0.0173  165 VAL   A CG2 
3660 N N   A SER   A 166 ? 0.1477 0.2945 0.2078 -0.0193 0.0124  0.0533  166 SER   A N   
3661 N N   B SER   A 166 ? 0.1413 0.2330 0.1974 -0.0217 0.0195  0.0289  166 SER   A N   
3662 C CA  A SER   A 166 ? 0.1513 0.3094 0.2242 -0.0207 0.0238  0.0420  166 SER   A CA  
3663 C CA  B SER   A 166 ? 0.1388 0.2456 0.2045 -0.0211 0.0197  0.0225  166 SER   A CA  
3664 C C   A SER   A 166 ? 0.1543 0.3264 0.2435 -0.0181 0.0106  0.0213  166 SER   A C   
3665 C C   B SER   A 166 ? 0.1485 0.2609 0.2116 -0.0184 0.0070  0.0122  166 SER   A C   
3666 O O   A SER   A 166 ? 0.1751 0.3403 0.2893 -0.0287 0.0240  -0.0133 166 SER   A O   
3667 O O   B SER   A 166 ? 0.1547 0.2643 0.2362 -0.0242 0.0098  -0.0045 166 SER   A O   
3668 C CB  A SER   A 166 ? 0.1633 0.3099 0.2469 -0.0132 0.0210  0.0406  166 SER   A CB  
3669 C CB  B SER   A 166 ? 0.1352 0.2461 0.2260 -0.0189 0.0112  0.0187  166 SER   A CB  
3670 O OG  A SER   A 166 ? 0.1741 0.3095 0.2575 -0.0071 0.0219  0.0559  166 SER   A OG  
3671 O OG  B SER   A 166 ? 0.1295 0.2467 0.2353 -0.0166 0.0016  0.0253  166 SER   A OG  
3682 N N   A SER   A 167 ? 0.1544 0.3265 0.2019 0.0024  -0.0017 0.0331  167 SER   A N   
3683 N N   B SER   A 167 ? 0.1606 0.2759 0.2016 -0.0077 0.0009  0.0229  167 SER   A N   
3684 C CA  A SER   A 167 ? 0.1767 0.3316 0.2111 0.0101  -0.0081 0.0213  167 SER   A CA  
3685 C CA  B SER   A 167 ? 0.1786 0.2949 0.2065 0.0000  -0.0005 0.0243  167 SER   A CA  
3686 C C   A SER   A 167 ? 0.1865 0.3264 0.2199 0.0172  0.0127  0.0199  167 SER   A C   
3687 C C   B SER   A 167 ? 0.1837 0.3060 0.2112 0.0112  0.0131  0.0221  167 SER   A C   
3688 O O   A SER   A 167 ? 0.2052 0.3296 0.2429 0.0236  -0.0021 0.0266  167 SER   A O   
3689 O O   B SER   A 167 ? 0.1964 0.3065 0.2233 0.0119  0.0081  0.0252  167 SER   A O   
3690 C CB  A SER   A 167 ? 0.1808 0.3412 0.2106 0.0136  -0.0046 0.0200  167 SER   A CB  
3691 C CB  B SER   A 167 ? 0.1898 0.3030 0.2109 -0.0017 -0.0020 0.0300  167 SER   A CB  
3692 O OG  A SER   A 167 ? 0.1810 0.3473 0.2132 0.0094  0.0199  0.0215  167 SER   A OG  
3693 O OG  B SER   A 167 ? 0.1977 0.3076 0.2172 -0.0020 0.0028  0.0360  167 SER   A OG  
3704 N N   . PHE   A 168 ? 0.1760 0.3166 0.2036 0.0247  0.0177  0.0205  168 PHE   A N   
3705 C CA  . PHE   A 168 ? 0.1755 0.3227 0.2217 0.0165  0.0271  0.0153  168 PHE   A CA  
3706 C C   . PHE   A 168 ? 0.1997 0.3488 0.2701 -0.0041 0.0688  0.0038  168 PHE   A C   
3707 O O   . PHE   A 168 ? 0.2017 0.3501 0.3242 -0.0205 0.0724  0.0227  168 PHE   A O   
3708 C CB  . PHE   A 168 ? 0.1748 0.3042 0.1940 0.0149  0.0061  0.0202  168 PHE   A CB  
3709 C CG  . PHE   A 168 ? 0.1689 0.2853 0.1903 0.0053  -0.0008 0.0253  168 PHE   A CG  
3710 C CD1 . PHE   A 168 ? 0.1706 0.2856 0.2032 -0.0066 -0.0030 0.0343  168 PHE   A CD1 
3711 C CD2 . PHE   A 168 ? 0.1699 0.2743 0.2016 0.0028  0.0122  0.0174  168 PHE   A CD2 
3712 C CE1 . PHE   A 168 ? 0.1587 0.2786 0.2060 -0.0146 0.0004  0.0380  168 PHE   A CE1 
3713 C CE2 . PHE   A 168 ? 0.1753 0.2634 0.2078 -0.0033 0.0138  0.0280  168 PHE   A CE2 
3714 C CZ  . PHE   A 168 ? 0.1656 0.2672 0.2051 -0.0099 0.0057  0.0344  168 PHE   A CZ  
3725 N N   A LEU   A 169 ? 0.2360 0.3616 0.2976 -0.0228 0.0675  -0.0202 169 LEU   A N   
3726 N N   B LEU   A 169 ? 0.2420 0.3646 0.3198 -0.0082 0.0497  -0.0037 169 LEU   A N   
3727 C CA  A LEU   A 169 ? 0.3066 0.3849 0.3780 -0.0263 0.0279  -0.0246 169 LEU   A CA  
3728 C CA  B LEU   A 169 ? 0.2903 0.3823 0.3823 -0.0080 0.0201  -0.0039 169 LEU   A CA  
3729 C C   A LEU   A 169 ? 0.3184 0.3860 0.4076 -0.0306 0.0180  -0.0071 169 LEU   A C   
3730 C C   B LEU   A 169 ? 0.3012 0.3866 0.4068 -0.0098 0.0064  0.0053  169 LEU   A C   
3731 O O   A LEU   A 169 ? 0.3269 0.3875 0.4167 -0.0282 0.0163  -0.0086 169 LEU   A O   
3732 O O   B LEU   A 169 ? 0.3058 0.3887 0.4129 -0.0106 0.0010  0.0061  169 LEU   A O   
3733 C CB  A LEU   A 169 ? 0.3483 0.4027 0.4086 -0.0301 0.0053  -0.0441 169 LEU   A CB  
3734 C CB  B LEU   A 169 ? 0.3192 0.3930 0.4086 -0.0091 0.0081  -0.0135 169 LEU   A CB  
3735 C CG  A LEU   A 169 ? 0.3831 0.4171 0.4357 -0.0353 -0.0127 -0.0639 169 LEU   A CG  
3736 C CG  B LEU   A 169 ? 0.3426 0.4020 0.4315 -0.0112 -0.0010 -0.0242 169 LEU   A CG  
3737 C CD1 A LEU   A 169 ? 0.3951 0.4205 0.4513 -0.0368 -0.0213 -0.0682 169 LEU   A CD1 
3738 C CD1 B LEU   A 169 ? 0.3515 0.4050 0.4416 -0.0126 -0.0042 -0.0276 169 LEU   A CD1 
3739 C CD2 A LEU   A 169 ? 0.3956 0.4233 0.4388 -0.0380 -0.0149 -0.0722 169 LEU   A CD2 
3740 C CD2 B LEU   A 169 ? 0.3502 0.4053 0.4375 -0.0124 -0.0029 -0.0271 169 LEU   A CD2 
3741 O OXT A LEU   A 169 ? 0.3049 0.3847 0.4052 -0.0369 0.0169  0.0039  169 LEU   A OXT 
3742 O OXT B LEU   A 169 ? 0.3005 0.3875 0.4150 -0.0103 0.0046  0.0092  169 LEU   A OXT 
3765 N N   A SER   B 1   ? 0.3775 0.3591 0.3498 -0.1110 -0.0837 0.0449  1   SER   B N   
3766 N N   B SER   B 1   ? 0.3432 0.3447 0.3484 -0.0663 -0.0555 0.0240  1   SER   B N   
3767 C CA  A SER   B 1   ? 0.3680 0.3634 0.3557 -0.1149 -0.0889 0.0415  1   SER   B CA  
3768 C CA  B SER   B 1   ? 0.3383 0.3456 0.3459 -0.0671 -0.0563 0.0237  1   SER   B CA  
3769 C C   A SER   B 1   ? 0.3423 0.3664 0.3380 -0.1134 -0.0913 0.0619  1   SER   B C   
3770 C C   B SER   B 1   ? 0.3252 0.3447 0.3316 -0.0649 -0.0602 0.0341  1   SER   B C   
3771 O O   A SER   B 1   ? 0.3532 0.3702 0.3145 -0.1036 -0.0796 0.0629  1   SER   B O   
3772 O O   B SER   B 1   ? 0.3270 0.3453 0.3183 -0.0639 -0.0622 0.0327  1   SER   B O   
3773 C CB  A SER   B 1   ? 0.3814 0.3625 0.3780 -0.1140 -0.0816 0.0215  1   SER   B CB  
3774 C CB  B SER   B 1   ? 0.3445 0.3461 0.3576 -0.0673 -0.0501 0.0127  1   SER   B CB  
3775 O OG  A SER   B 1   ? 0.3965 0.3721 0.4280 -0.1117 -0.0687 0.0137  1   SER   B OG  
3776 O OG  B SER   B 1   ? 0.3508 0.3507 0.3795 -0.0680 -0.0451 0.0073  1   SER   B OG  
3791 N N   A MET   B 2   ? 0.3149 0.3621 0.3418 -0.1168 -0.0894 0.0971  2   MET   B N   
3792 N N   B MET   B 2   ? 0.3131 0.3418 0.3300 -0.0618 -0.0563 0.0518  2   MET   B N   
3793 C CA  A MET   B 2   ? 0.2933 0.3619 0.3592 -0.0973 -0.0887 0.1190  2   MET   B CA  
3794 C CA  B MET   B 2   ? 0.3013 0.3387 0.3291 -0.0519 -0.0516 0.0650  2   MET   B CA  
3795 C C   A MET   B 2   ? 0.2540 0.3365 0.3290 -0.0777 -0.0986 0.1449  2   MET   B C   
3796 C C   B MET   B 2   ? 0.2800 0.3207 0.3013 -0.0463 -0.0471 0.0709  2   MET   B C   
3797 O O   A MET   B 2   ? 0.2434 0.3460 0.3319 -0.0687 -0.1082 0.1467  2   MET   B O   
3798 O O   B MET   B 2   ? 0.2806 0.3252 0.3023 -0.0439 -0.0431 0.0691  2   MET   B O   
3799 C CB  A MET   B 2   ? 0.3235 0.3959 0.4455 -0.0757 -0.0668 0.0936  2   MET   B CB  
3800 C CB  B MET   B 2   ? 0.3134 0.3550 0.3676 -0.0420 -0.0485 0.0669  2   MET   B CB  
3801 C CG  A MET   B 2   ? 0.3513 0.4244 0.5240 -0.0518 -0.0458 0.0784  2   MET   B CG  
3802 C CG  B MET   B 2   ? 0.3232 0.3690 0.3980 -0.0316 -0.0455 0.0745  2   MET   B CG  
3803 S SD  A MET   B 2   ? 0.3780 0.4514 0.6010 -0.0322 -0.0337 0.0641  2   MET   B SD  
3804 S SD  B MET   B 2   ? 0.3330 0.3834 0.4255 -0.0219 -0.0472 0.0815  2   MET   B SD  
3805 C CE  A MET   B 2   ? 0.3803 0.4578 0.6027 -0.0300 -0.0240 0.0635  2   MET   B CE  
3806 C CE  B MET   B 2   ? 0.3336 0.3847 0.4313 -0.0217 -0.0435 0.0753  2   MET   B CE  
3825 N N   A VAL   B 3   ? 0.2271 0.2962 0.2992 -0.0768 -0.0934 0.1623  3   VAL   B N   
3826 N N   B VAL   B 3   ? 0.2581 0.2961 0.2730 -0.0458 -0.0466 0.0771  3   VAL   B N   
3827 C CA  A VAL   B 3   ? 0.2178 0.2679 0.2988 -0.0641 -0.0798 0.1366  3   VAL   B CA  
3828 C CA  B VAL   B 3   ? 0.2394 0.2734 0.2564 -0.0425 -0.0433 0.0729  3   VAL   B CA  
3829 C C   A VAL   B 3   ? 0.2027 0.2494 0.2723 -0.0601 -0.0649 0.1119  3   VAL   B C   
3830 C C   B VAL   B 3   ? 0.2169 0.2540 0.2328 -0.0435 -0.0450 0.0761  3   VAL   B C   
3831 O O   A VAL   B 3   ? 0.1977 0.2482 0.2868 -0.0651 -0.0699 0.1178  3   VAL   B O   
3832 O O   B VAL   B 3   ? 0.2152 0.2592 0.2180 -0.0316 -0.0482 0.0776  3   VAL   B O   
3833 C CB  A VAL   B 3   ? 0.2317 0.2643 0.3506 -0.0632 -0.0656 0.1181  3   VAL   B CB  
3834 C CB  B VAL   B 3   ? 0.2448 0.2697 0.2717 -0.0408 -0.0356 0.0643  3   VAL   B CB  
3835 C CG1 A VAL   B 3   ? 0.2354 0.2595 0.3673 -0.0631 -0.0654 0.1116  3   VAL   B CG1 
3836 C CG1 B VAL   B 3   ? 0.2463 0.2673 0.2779 -0.0414 -0.0340 0.0609  3   VAL   B CG1 
3837 C CG2 A VAL   B 3   ? 0.2369 0.2728 0.3741 -0.0590 -0.0577 0.1165  3   VAL   B CG2 
3838 C CG2 B VAL   B 3   ? 0.2472 0.2710 0.2793 -0.0388 -0.0347 0.0628  3   VAL   B CG2 
3857 N N   . ASN   B 4   ? 0.1973 0.2264 0.2270 -0.0560 -0.0519 0.0774  4   ASN   B N   
3858 C CA  . ASN   B 4   ? 0.1932 0.2190 0.1946 -0.0566 -0.0416 0.0385  4   ASN   B CA  
3859 C C   . ASN   B 4   ? 0.2028 0.2354 0.1888 -0.0554 -0.0279 0.0283  4   ASN   B C   
3860 O O   . ASN   B 4   ? 0.2042 0.2403 0.2056 -0.0522 -0.0252 0.0098  4   ASN   B O   
3861 C CB  . ASN   B 4   ? 0.1891 0.2136 0.1969 -0.0508 -0.0582 0.0320  4   ASN   B CB  
3862 C CG  . ASN   B 4   ? 0.1836 0.1923 0.1805 -0.0457 -0.0528 0.0326  4   ASN   B CG  
3863 O OD1 . ASN   B 4   ? 0.1882 0.1760 0.1846 -0.0429 -0.0544 0.0295  4   ASN   B OD1 
3864 N ND2 . ASN   B 4   ? 0.2044 0.1977 0.1840 -0.0237 -0.0439 0.0279  4   ASN   B ND2 
3872 N N   . SER   B 5   ? 0.2155 0.2527 0.1971 -0.0559 -0.0181 0.0309  5   SER   B N   
3873 C CA  . SER   B 5   ? 0.2435 0.2879 0.2185 -0.0519 0.0001  0.0336  5   SER   B CA  
3874 C C   . SER   B 5   ? 0.2592 0.2955 0.2622 -0.0723 0.0279  0.0323  5   SER   B C   
3875 O O   . SER   B 5   ? 0.2768 0.2924 0.3460 -0.0665 0.0643  0.0291  5   SER   B O   
3876 C CB  . SER   B 5   ? 0.2594 0.3119 0.2347 -0.0422 0.0098  0.0450  5   SER   B CB  
3877 O OG  . SER   B 5   ? 0.2845 0.3461 0.2992 -0.0312 0.0145  0.0483  5   SER   B OG  
3883 N N   . PHE   B 6   ? 0.2748 0.3144 0.2393 -0.0768 0.0380  0.0349  6   PHE   B N   
3884 C CA  . PHE   B 6   ? 0.2829 0.3195 0.2088 -0.0942 0.0384  0.0174  6   PHE   B CA  
3885 C C   . PHE   B 6   ? 0.3360 0.3526 0.2514 -0.0989 0.0633  -0.0094 6   PHE   B C   
3886 O O   . PHE   B 6   ? 0.3503 0.3838 0.2757 -0.0903 0.0484  -0.0297 6   PHE   B O   
3887 C CB  . PHE   B 6   ? 0.2504 0.2947 0.1882 -0.0833 0.0190  0.0165  6   PHE   B CB  
3888 C CG  . PHE   B 6   ? 0.2175 0.2584 0.1728 -0.0750 0.0054  0.0121  6   PHE   B CG  
3889 C CD1 . PHE   B 6   ? 0.2210 0.2281 0.1647 -0.0654 -0.0098 0.0084  6   PHE   B CD1 
3890 C CD2 . PHE   B 6   ? 0.1949 0.2548 0.1789 -0.0602 0.0057  0.0368  6   PHE   B CD2 
3891 C CE1 . PHE   B 6   ? 0.2149 0.2096 0.1762 -0.0520 -0.0144 0.0101  6   PHE   B CE1 
3892 C CE2 . PHE   B 6   ? 0.2019 0.2394 0.2073 -0.0465 0.0011  0.0337  6   PHE   B CE2 
3893 C CZ  . PHE   B 6   ? 0.2042 0.2151 0.1868 -0.0474 -0.0126 0.0151  6   PHE   B CZ  
3903 N N   . SER   B 7   ? 0.3731 0.3368 0.2581 -0.1190 0.0933  -0.0333 7   SER   B N   
3904 C CA  . SER   B 7   ? 0.4081 0.3525 0.3081 -0.1169 0.1175  -0.0356 7   SER   B CA  
3905 C C   . SER   B 7   ? 0.4079 0.3308 0.2893 -0.1205 0.1361  -0.0495 7   SER   B C   
3906 O O   . SER   B 7   ? 0.4180 0.3296 0.3243 -0.1221 0.1316  -0.0537 7   SER   B O   
3907 C CB  . SER   B 7   ? 0.4334 0.3789 0.3774 -0.1107 0.1281  -0.0317 7   SER   B CB  
3908 O OG  . SER   B 7   ? 0.4503 0.3864 0.4316 -0.1094 0.1314  -0.0217 7   SER   B OG  
3914 N N   . GLY   B 8   ? 0.4051 0.3209 0.2969 -0.1041 0.1416  -0.0587 8   GLY   B N   
3915 C CA  . GLY   B 8   ? 0.3909 0.3038 0.3069 -0.0950 0.1384  -0.0697 8   GLY   B CA  
3916 C C   . GLY   B 8   ? 0.3679 0.2752 0.2964 -0.0903 0.1422  -0.0675 8   GLY   B C   
3917 O O   . GLY   B 8   ? 0.3758 0.2804 0.3366 -0.0791 0.1483  -0.0760 8   GLY   B O   
3921 N N   . TYR   B 9   ? 0.3506 0.2521 0.2638 -0.0773 0.1121  -0.0751 9   TYR   B N   
3922 C CA  . TYR   B 9   ? 0.3265 0.2244 0.2277 -0.0607 0.0841  -0.0598 9   TYR   B CA  
3923 C C   . TYR   B 9   ? 0.3194 0.2230 0.2139 -0.0545 0.0509  -0.0456 9   TYR   B C   
3924 O O   . TYR   B 9   ? 0.3355 0.2440 0.2513 -0.0597 0.0492  -0.0275 9   TYR   B O   
3925 C CB  . TYR   B 9   ? 0.3148 0.1988 0.2363 -0.0576 0.0778  -0.0514 9   TYR   B CB  
3926 C CG  . TYR   B 9   ? 0.2991 0.1802 0.2436 -0.0620 0.0732  -0.0566 9   TYR   B CG  
3927 C CD1 . TYR   B 9   ? 0.3006 0.1870 0.2605 -0.0747 0.0745  -0.0530 9   TYR   B CD1 
3928 C CD2 . TYR   B 9   ? 0.2823 0.1747 0.2369 -0.0573 0.0690  -0.0528 9   TYR   B CD2 
3929 C CE1 . TYR   B 9   ? 0.2953 0.1914 0.2692 -0.0788 0.0789  -0.0611 9   TYR   B CE1 
3930 C CE2 . TYR   B 9   ? 0.2842 0.1697 0.2507 -0.0594 0.0703  -0.0511 9   TYR   B CE2 
3931 C CZ  . TYR   B 9   ? 0.2891 0.1887 0.2653 -0.0694 0.0741  -0.0697 9   TYR   B CZ  
3932 O OH  . TYR   B 9   ? 0.2877 0.1994 0.2759 -0.0836 0.0763  -0.0804 9   TYR   B OH  
3942 N N   . LEU   B 10  ? 0.2953 0.1954 0.1927 -0.0504 0.0251  -0.0435 10  LEU   B N   
3943 C CA  . LEU   B 10  ? 0.2900 0.1886 0.1977 -0.0633 -0.0089 -0.0421 10  LEU   B CA  
3944 C C   . LEU   B 10  ? 0.2678 0.1899 0.1997 -0.0660 -0.0229 -0.0411 10  LEU   B C   
3945 O O   . LEU   B 10  ? 0.2514 0.1872 0.2066 -0.0463 -0.0101 -0.0304 10  LEU   B O   
3946 C CB  . LEU   B 10  ? 0.2993 0.1876 0.2150 -0.0671 -0.0367 -0.0165 10  LEU   B CB  
3947 C CG  . LEU   B 10  ? 0.3184 0.1999 0.2608 -0.0617 -0.0680 -0.0052 10  LEU   B CG  
3948 C CD1 . LEU   B 10  ? 0.3346 0.2178 0.2950 -0.0535 -0.0651 -0.0017 10  LEU   B CD1 
3949 C CD2 . LEU   B 10  ? 0.3278 0.2084 0.3007 -0.0635 -0.0611 0.0093  10  LEU   B CD2 
3961 N N   . LYS   B 11  ? 0.2840 0.2215 0.2031 -0.0567 -0.0269 -0.0306 11  LYS   B N   
3962 C CA  . LYS   B 11  ? 0.3016 0.2518 0.2312 -0.0442 -0.0509 -0.0380 11  LYS   B CA  
3963 C C   . LYS   B 11  ? 0.2823 0.2332 0.2362 -0.0646 -0.0497 -0.0470 11  LYS   B C   
3964 O O   . LYS   B 11  ? 0.2996 0.2513 0.2796 -0.0785 -0.0401 -0.0784 11  LYS   B O   
3965 C CB  . LYS   B 11  ? 0.3379 0.3034 0.2997 -0.0175 -0.0590 -0.0311 11  LYS   B CB  
3966 C CG  . LYS   B 11  ? 0.3717 0.3392 0.3790 -0.0013 -0.0602 -0.0288 11  LYS   B CG  
3967 C CD  . LYS   B 11  ? 0.3976 0.3639 0.4504 0.0077  -0.0613 -0.0301 11  LYS   B CD  
3968 C CE  . LYS   B 11  ? 0.4168 0.3802 0.5012 0.0085  -0.0610 -0.0333 11  LYS   B CE  
3969 N NZ  . LYS   B 11  ? 0.4279 0.3900 0.5291 0.0083  -0.0624 -0.0322 11  LYS   B NZ  
3983 N N   . LEU   B 12  ? 0.2428 0.2062 0.2377 -0.0606 -0.0436 -0.0377 12  LEU   B N   
3984 C CA  . LEU   B 12  ? 0.2265 0.1827 0.2575 -0.0487 -0.0363 -0.0281 12  LEU   B CA  
3985 C C   . LEU   B 12  ? 0.2146 0.1823 0.2628 -0.0469 -0.0486 -0.0338 12  LEU   B C   
3986 O O   . LEU   B 12  ? 0.2149 0.1849 0.2851 -0.0575 -0.0549 -0.0264 12  LEU   B O   
3987 C CB  . LEU   B 12  ? 0.2280 0.1605 0.2505 -0.0334 -0.0294 -0.0254 12  LEU   B CB  
3988 C CG  . LEU   B 12  ? 0.2277 0.1564 0.2514 -0.0342 -0.0122 -0.0203 12  LEU   B CG  
3989 C CD1 . LEU   B 12  ? 0.2354 0.1589 0.2424 -0.0196 -0.0056 -0.0075 12  LEU   B CD1 
3990 C CD2 . LEU   B 12  ? 0.2348 0.1626 0.2702 -0.0349 -0.0142 -0.0314 12  LEU   B CD2 
4002 N N   . THR   B 13  ? 0.2031 0.1818 0.2687 -0.0473 -0.0411 -0.0463 13  THR   B N   
4003 C CA  . THR   B 13  ? 0.2096 0.1907 0.2601 -0.0490 -0.0482 -0.0336 13  THR   B CA  
4004 C C   . THR   B 13  ? 0.2512 0.2094 0.2784 -0.0606 -0.0641 -0.0217 13  THR   B C   
4005 O O   . THR   B 13  ? 0.2685 0.2102 0.2893 -0.0582 -0.0297 -0.0236 13  THR   B O   
4006 C CB  . THR   B 13  ? 0.1939 0.1875 0.2629 -0.0504 -0.0439 -0.0239 13  THR   B CB  
4007 O OG1 . THR   B 13  ? 0.1856 0.1833 0.2666 -0.0426 -0.0342 -0.0247 13  THR   B OG1 
4008 C CG2 . THR   B 13  ? 0.2016 0.1962 0.2757 -0.0487 -0.0395 -0.0018 13  THR   B CG2 
4016 N N   A ASP   B 14  ? 0.2644 0.2244 0.2842 -0.0703 -0.1037 -0.0065 14  ASP   B N   
4017 N N   B ASP   B 14  ? 0.2600 0.2211 0.2894 -0.0615 -0.0724 -0.0108 14  ASP   B N   
4018 C CA  A ASP   B 14  ? 0.2769 0.2407 0.3143 -0.0710 -0.1108 0.0148  14  ASP   B CA  
4019 C CA  B ASP   B 14  ? 0.2667 0.2324 0.3053 -0.0598 -0.0723 0.0011  14  ASP   B CA  
4020 C C   A ASP   B 14  ? 0.2625 0.2202 0.2704 -0.0807 -0.0890 0.0089  14  ASP   B C   
4021 C C   B ASP   B 14  ? 0.2492 0.2132 0.2708 -0.0646 -0.0717 0.0012  14  ASP   B C   
4022 O O   A ASP   B 14  ? 0.2928 0.2380 0.2810 -0.0772 -0.0815 0.0280  14  ASP   B O   
4023 O O   B ASP   B 14  ? 0.2578 0.2141 0.2741 -0.0607 -0.0697 0.0025  14  ASP   B O   
4024 C CB  A ASP   B 14  ? 0.3018 0.2784 0.3996 -0.0658 -0.1281 0.0182  14  ASP   B CB  
4025 C CB  B ASP   B 14  ? 0.2881 0.2609 0.3578 -0.0534 -0.0696 0.0056  14  ASP   B CB  
4026 C CG  A ASP   B 14  ? 0.3336 0.3109 0.4866 -0.0598 -0.1209 0.0079  14  ASP   B CG  
4027 C CG  B ASP   B 14  ? 0.3082 0.2828 0.4049 -0.0472 -0.0634 0.0042  14  ASP   B CG  
4028 O OD1 A ASP   B 14  ? 0.3533 0.3204 0.5055 -0.0659 -0.1200 -0.0078 14  ASP   B OD1 
4029 O OD1 B ASP   B 14  ? 0.3157 0.2938 0.4155 -0.0444 -0.0584 0.0018  14  ASP   B OD1 
4030 O OD2 A ASP   B 14  ? 0.3363 0.3275 0.5265 -0.0562 -0.1169 0.0111  14  ASP   B OD2 
4031 O OD2 B ASP   B 14  ? 0.3132 0.2880 0.4232 -0.0509 -0.0659 0.0052  14  ASP   B OD2 
4040 N N   . ASN   B 15  ? 0.2259 0.1963 0.2427 -0.0608 -0.0734 0.0075  15  ASN   B N   
4041 C CA  . ASN   B 15  ? 0.1834 0.1692 0.2256 -0.0381 -0.0492 -0.0004 15  ASN   B CA  
4042 C C   . ASN   B 15  ? 0.1666 0.1558 0.2119 -0.0195 -0.0363 -0.0012 15  ASN   B C   
4043 O O   . ASN   B 15  ? 0.1673 0.1589 0.2351 -0.0207 -0.0417 -0.0168 15  ASN   B O   
4044 C CB  . ASN   B 15  ? 0.1766 0.1732 0.2409 -0.0172 -0.0426 -0.0047 15  ASN   B CB  
4045 C CG  . ASN   B 15  ? 0.1657 0.1701 0.2389 -0.0253 -0.0228 -0.0028 15  ASN   B CG  
4046 O OD1 . ASN   B 15  ? 0.1728 0.1995 0.2686 -0.0444 -0.0320 0.0050  15  ASN   B OD1 
4047 N ND2 . ASN   B 15  ? 0.1712 0.1429 0.2394 -0.0105 -0.0016 -0.0154 15  ASN   B ND2 
4055 N N   . VAL   B 16  ? 0.1725 0.1507 0.2122 -0.0249 -0.0464 -0.0037 16  VAL   B N   
4056 C CA  . VAL   B 16  ? 0.1735 0.1494 0.1949 -0.0250 -0.0336 -0.0217 16  VAL   B CA  
4057 C C   . VAL   B 16  ? 0.1739 0.1598 0.1989 -0.0375 -0.0277 -0.0116 16  VAL   B C   
4058 O O   . VAL   B 16  ? 0.1812 0.1736 0.2235 -0.0360 -0.0228 -0.0285 16  VAL   B O   
4059 C CB  . VAL   B 16  ? 0.1801 0.1463 0.2116 -0.0143 -0.0157 -0.0135 16  VAL   B CB  
4060 C CG1 . VAL   B 16  ? 0.1916 0.1420 0.2003 -0.0037 -0.0203 -0.0093 16  VAL   B CG1 
4061 C CG2 . VAL   B 16  ? 0.1745 0.1561 0.2311 -0.0119 -0.0041 -0.0208 16  VAL   B CG2 
4071 N N   . TYR   B 17  ? 0.1766 0.1665 0.2004 -0.0329 -0.0288 -0.0213 17  TYR   B N   
4072 C CA  . TYR   B 17  ? 0.1850 0.1785 0.1949 -0.0351 -0.0253 0.0043  17  TYR   B CA  
4073 C C   . TYR   B 17  ? 0.1713 0.1520 0.1954 -0.0386 -0.0192 -0.0073 17  TYR   B C   
4074 O O   . TYR   B 17  ? 0.1707 0.1636 0.2070 -0.0310 -0.0270 -0.0315 17  TYR   B O   
4075 C CB  . TYR   B 17  ? 0.2192 0.2204 0.2096 -0.0219 -0.0267 0.0445  17  TYR   B CB  
4076 C CG  . TYR   B 17  ? 0.2503 0.2690 0.2541 -0.0159 -0.0417 0.0468  17  TYR   B CG  
4077 C CD1 . TYR   B 17  ? 0.2687 0.2805 0.2762 -0.0135 -0.0554 0.0563  17  TYR   B CD1 
4078 C CD2 . TYR   B 17  ? 0.2758 0.2985 0.2851 -0.0067 -0.0474 0.0408  17  TYR   B CD2 
4079 C CE1 . TYR   B 17  ? 0.2915 0.3049 0.2980 -0.0043 -0.0661 0.0462  17  TYR   B CE1 
4080 C CE2 . TYR   B 17  ? 0.2944 0.3171 0.3067 0.0070  -0.0658 0.0470  17  TYR   B CE2 
4081 C CZ  . TYR   B 17  ? 0.3042 0.3225 0.3098 0.0086  -0.0796 0.0496  17  TYR   B CZ  
4082 O OH  . TYR   B 17  ? 0.3200 0.3429 0.3341 0.0202  -0.0910 0.0466  17  TYR   B OH  
4092 N N   . ILE   B 18  ? 0.1867 0.1551 0.1833 -0.0345 -0.0096 -0.0236 18  ILE   B N   
4093 C CA  . ILE   B 18  ? 0.1912 0.1529 0.1781 -0.0364 -0.0127 -0.0231 18  ILE   B CA  
4094 C C   . ILE   B 18  ? 0.2080 0.1585 0.1847 -0.0468 -0.0123 -0.0282 18  ILE   B C   
4095 O O   . ILE   B 18  ? 0.2310 0.1691 0.2106 -0.0450 0.0014  -0.0391 18  ILE   B O   
4096 C CB  . ILE   B 18  ? 0.1990 0.1579 0.1944 -0.0438 -0.0112 -0.0209 18  ILE   B CB  
4097 C CG1 . ILE   B 18  ? 0.2049 0.1588 0.1986 -0.0450 -0.0093 -0.0024 18  ILE   B CG1 
4098 C CG2 . ILE   B 18  ? 0.2050 0.1656 0.2020 -0.0479 -0.0128 -0.0152 18  ILE   B CG2 
4099 C CD1 . ILE   B 18  ? 0.2111 0.1851 0.2202 -0.0356 -0.0225 0.0178  18  ILE   B CD1 
4111 N N   . LYS   B 19  ? 0.2069 0.1555 0.2027 -0.0309 0.0262  -0.0348 19  LYS   B N   
4112 C CA  . LYS   B 19  ? 0.2121 0.1557 0.2156 -0.0248 0.0368  -0.0384 19  LYS   B CA  
4113 C C   . LYS   B 19  ? 0.1960 0.1569 0.2359 -0.0246 0.0361  -0.0447 19  LYS   B C   
4114 O O   . LYS   B 19  ? 0.1898 0.1596 0.2299 -0.0181 0.0217  -0.0440 19  LYS   B O   
4115 C CB  . LYS   B 19  ? 0.2354 0.1722 0.2211 -0.0244 0.0455  -0.0231 19  LYS   B CB  
4116 C CG  . LYS   B 19  ? 0.2607 0.1934 0.2493 -0.0313 0.0526  -0.0243 19  LYS   B CG  
4117 C CD  . LYS   B 19  ? 0.2906 0.2197 0.2674 -0.0439 0.0583  -0.0142 19  LYS   B CD  
4118 C CE  . LYS   B 19  ? 0.3192 0.2467 0.2868 -0.0483 0.0591  -0.0118 19  LYS   B CE  
4119 N NZ  . LYS   B 19  ? 0.3391 0.2652 0.2963 -0.0521 0.0642  -0.0030 19  LYS   B NZ  
4133 N N   . ASN   B 20  ? 0.1894 0.1730 0.2631 -0.0207 0.0444  -0.0574 20  ASN   B N   
4134 C CA  . ASN   B 20  ? 0.1905 0.1854 0.2871 -0.0134 0.0381  -0.0738 20  ASN   B CA  
4135 C C   . ASN   B 20  ? 0.1895 0.2041 0.2805 -0.0187 0.0512  -0.0854 20  ASN   B C   
4136 O O   . ASN   B 20  ? 0.2065 0.2407 0.3013 -0.0340 0.0477  -0.0813 20  ASN   B O   
4137 C CB  . ASN   B 20  ? 0.2187 0.1897 0.3164 0.0083  0.0286  -0.0717 20  ASN   B CB  
4138 C CG  . ASN   B 20  ? 0.2488 0.1957 0.3404 0.0367  0.0280  -0.0837 20  ASN   B CG  
4139 O OD1 . ASN   B 20  ? 0.2807 0.2256 0.3694 0.0507  0.0228  -0.0862 20  ASN   B OD1 
4140 N ND2 . ASN   B 20  ? 0.2387 0.1947 0.3355 0.0424  0.0135  -0.0737 20  ASN   B ND2 
4147 N N   . ALA   B 21  ? 0.1927 0.1867 0.2864 -0.0281 0.0518  -0.0686 21  ALA   B N   
4148 C CA  . ALA   B 21  ? 0.2057 0.1973 0.3049 -0.0304 0.0383  -0.0534 21  ALA   B CA  
4149 C C   . ALA   B 21  ? 0.2033 0.1679 0.2857 -0.0211 0.0483  -0.0425 21  ALA   B C   
4150 O O   . ALA   B 21  ? 0.2002 0.1600 0.2898 -0.0283 0.0403  -0.0366 21  ALA   B O   
4151 C CB  . ALA   B 21  ? 0.2226 0.2269 0.3171 -0.0451 0.0375  -0.0379 21  ALA   B CB  
4157 N N   . ASP   B 22  ? 0.1952 0.1584 0.2791 -0.0242 0.0405  -0.0373 22  ASP   B N   
4158 C CA  . ASP   B 22  ? 0.1890 0.1497 0.2617 -0.0111 0.0360  -0.0267 22  ASP   B CA  
4159 C C   . ASP   B 22  ? 0.1805 0.1519 0.2210 -0.0190 0.0229  -0.0129 22  ASP   B C   
4160 O O   . ASP   B 22  ? 0.1842 0.1544 0.2291 -0.0119 0.0158  -0.0072 22  ASP   B O   
4161 C CB  . ASP   B 22  ? 0.1956 0.1659 0.2951 -0.0027 0.0323  -0.0152 22  ASP   B CB  
4162 C CG  . ASP   B 22  ? 0.1975 0.1852 0.3460 0.0028  0.0066  -0.0076 22  ASP   B CG  
4163 O OD1 . ASP   B 22  ? 0.2100 0.1763 0.3437 0.0048  -0.0179 -0.0078 22  ASP   B OD1 
4164 O OD2 . ASP   B 22  ? 0.2059 0.2142 0.4012 0.0151  -0.0159 -0.0176 22  ASP   B OD2 
4169 N N   . ILE   B 23  ? 0.1810 0.1463 0.1998 -0.0074 0.0057  0.0143  23  ILE   B N   
4170 C CA  . ILE   B 23  ? 0.1720 0.1497 0.1758 -0.0089 0.0012  0.0056  23  ILE   B CA  
4171 C C   . ILE   B 23  ? 0.1598 0.1499 0.1770 -0.0046 -0.0074 0.0033  23  ILE   B C   
4172 O O   . ILE   B 23  ? 0.1557 0.1455 0.1707 -0.0086 -0.0036 0.0073  23  ILE   B O   
4173 C CB  . ILE   B 23  ? 0.1647 0.1571 0.1976 -0.0164 0.0001  0.0117  23  ILE   B CB  
4174 C CG1 . ILE   B 23  ? 0.1703 0.1581 0.2144 -0.0122 0.0100  0.0240  23  ILE   B CG1 
4175 C CG2 . ILE   B 23  ? 0.1715 0.1798 0.2024 -0.0150 0.0032  0.0054  23  ILE   B CG2 
4176 C CD1 . ILE   B 23  ? 0.1772 0.1680 0.2156 -0.0080 0.0098  0.0133  23  ILE   B CD1 
4188 N N   . VAL   B 24  ? 0.1640 0.1464 0.1967 -0.0099 -0.0119 0.0003  24  VAL   B N   
4189 C CA  . VAL   B 24  ? 0.1636 0.1572 0.2182 -0.0041 -0.0213 -0.0048 24  VAL   B CA  
4190 C C   . VAL   B 24  ? 0.1583 0.1554 0.2202 -0.0052 -0.0103 0.0022  24  VAL   B C   
4191 O O   . VAL   B 24  ? 0.1556 0.1620 0.2273 -0.0121 -0.0017 0.0141  24  VAL   B O   
4192 C CB  . VAL   B 24  ? 0.1766 0.1741 0.2208 0.0035  -0.0274 0.0029  24  VAL   B CB  
4193 C CG1 . VAL   B 24  ? 0.1743 0.1735 0.2510 -0.0049 -0.0284 0.0067  24  VAL   B CG1 
4194 C CG2 . VAL   B 24  ? 0.1854 0.1965 0.2266 0.0075  -0.0282 -0.0076 24  VAL   B CG2 
4204 N N   . GLU   B 25  ? 0.1820 0.1669 0.2237 -0.0055 -0.0013 0.0074  25  GLU   B N   
4205 C CA  . GLU   B 25  ? 0.1943 0.1905 0.2339 0.0002  0.0131  -0.0023 25  GLU   B CA  
4206 C C   . GLU   B 25  ? 0.1870 0.1868 0.1973 -0.0093 0.0177  -0.0018 25  GLU   B C   
4207 O O   . GLU   B 25  ? 0.1930 0.2031 0.2110 -0.0072 0.0200  0.0087  25  GLU   B O   
4208 C CB  . GLU   B 25  ? 0.2345 0.2359 0.2930 0.0188  0.0192  -0.0120 25  GLU   B CB  
4209 C CG  . GLU   B 25  ? 0.2776 0.2995 0.4097 0.0306  0.0081  -0.0164 25  GLU   B CG  
4210 C CD  . GLU   B 25  ? 0.3296 0.3615 0.5047 0.0273  0.0003  -0.0164 25  GLU   B CD  
4211 O OE1 . GLU   B 25  ? 0.3519 0.3849 0.5372 0.0327  0.0051  -0.0141 25  GLU   B OE1 
4212 O OE2 . GLU   B 25  ? 0.3472 0.3810 0.5384 0.0257  -0.0064 -0.0225 25  GLU   B OE2 
4219 N N   . GLU   B 26  ? 0.1851 0.1731 0.1834 -0.0274 0.0132  -0.0012 26  GLU   B N   
4220 C CA  . GLU   B 26  ? 0.1857 0.1895 0.1963 -0.0361 -0.0097 0.0035  26  GLU   B CA  
4221 C C   . GLU   B 26  ? 0.1675 0.1845 0.1897 -0.0264 0.0008  0.0175  26  GLU   B C   
4222 O O   . GLU   B 26  ? 0.1930 0.2120 0.1862 -0.0241 -0.0038 0.0212  26  GLU   B O   
4223 C CB  . GLU   B 26  ? 0.2142 0.2115 0.2190 -0.0477 -0.0056 0.0198  26  GLU   B CB  
4224 C CG  . GLU   B 26  ? 0.2573 0.2522 0.2744 -0.0514 0.0121  -0.0025 26  GLU   B CG  
4225 C CD  . GLU   B 26  ? 0.2823 0.2745 0.2880 -0.0747 0.0296  -0.0425 26  GLU   B CD  
4226 O OE1 . GLU   B 26  ? 0.3032 0.2589 0.3041 -0.0851 0.0824  -0.0406 26  GLU   B OE1 
4227 O OE2 . GLU   B 26  ? 0.2844 0.3185 0.3185 -0.0667 0.0263  -0.0306 26  GLU   B OE2 
4234 N N   . ALA   B 27  ? 0.1495 0.1691 0.1871 -0.0204 0.0092  0.0212  27  ALA   B N   
4235 C CA  . ALA   B 27  ? 0.1524 0.1710 0.1902 -0.0115 0.0039  0.0299  27  ALA   B CA  
4236 C C   . ALA   B 27  ? 0.1624 0.1781 0.2196 -0.0082 0.0135  0.0386  27  ALA   B C   
4237 O O   . ALA   B 27  ? 0.1732 0.1849 0.2371 0.0045  0.0174  0.0473  27  ALA   B O   
4238 C CB  . ALA   B 27  ? 0.1737 0.1555 0.1976 -0.0124 0.0053  0.0269  27  ALA   B CB  
4244 N N   . LYS   B 28  ? 0.1586 0.1990 0.2621 -0.0182 0.0189  0.0602  28  LYS   B N   
4245 C CA  . LYS   B 28  ? 0.1705 0.2345 0.2873 -0.0089 0.0450  0.0939  28  LYS   B CA  
4246 C C   . LYS   B 28  ? 0.1925 0.2528 0.2750 -0.0011 0.0618  0.0830  28  LYS   B C   
4247 O O   . LYS   B 28  ? 0.2222 0.2610 0.2849 -0.0049 0.0674  0.0814  28  LYS   B O   
4248 C CB  . LYS   B 28  ? 0.1965 0.2735 0.3465 0.0047  0.0680  0.1165  28  LYS   B CB  
4249 C CG  . LYS   B 28  ? 0.2299 0.3308 0.3899 0.0163  0.0832  0.1324  28  LYS   B CG  
4250 C CD  . LYS   B 28  ? 0.2856 0.3981 0.4544 0.0249  0.1012  0.1328  28  LYS   B CD  
4251 C CE  . LYS   B 28  ? 0.3298 0.4457 0.5042 0.0359  0.1058  0.1378  28  LYS   B CE  
4252 N NZ  . LYS   B 28  ? 0.3606 0.4598 0.5281 0.0443  0.1074  0.1444  28  LYS   B NZ  
4266 N N   . LYS   B 29  ? 0.2044 0.2782 0.2790 0.0187  0.0620  0.0630  29  LYS   B N   
4267 C CA  . LYS   B 29  ? 0.2524 0.3117 0.2948 0.0216  0.0643  0.0626  29  LYS   B CA  
4268 C C   . LYS   B 29  ? 0.2490 0.3172 0.2575 0.0228  0.0505  0.0746  29  LYS   B C   
4269 O O   . LYS   B 29  ? 0.2681 0.3378 0.2656 0.0316  0.0514  0.0819  29  LYS   B O   
4270 C CB  . LYS   B 29  ? 0.3128 0.3477 0.3699 0.0225  0.0630  0.0484  29  LYS   B CB  
4271 C CG  . LYS   B 29  ? 0.3623 0.3786 0.4516 0.0191  0.0677  0.0428  29  LYS   B CG  
4272 C CD  . LYS   B 29  ? 0.4029 0.4010 0.5171 0.0125  0.0783  0.0343  29  LYS   B CD  
4273 C CE  . LYS   B 29  ? 0.4317 0.4158 0.5628 0.0079  0.0885  0.0304  29  LYS   B CE  
4274 N NZ  . LYS   B 29  ? 0.4434 0.4247 0.5886 0.0066  0.0932  0.0271  29  LYS   B NZ  
4288 N N   . VAL   B 30  ? 0.2187 0.2980 0.2425 0.0135  0.0379  0.0719  30  VAL   B N   
4289 C CA  . VAL   B 30  ? 0.2056 0.2851 0.2758 -0.0018 0.0028  0.0757  30  VAL   B CA  
4290 C C   . VAL   B 30  ? 0.1885 0.2806 0.2629 -0.0069 0.0094  0.1020  30  VAL   B C   
4291 O O   . VAL   B 30  ? 0.2079 0.2982 0.2785 -0.0051 0.0103  0.1167  30  VAL   B O   
4292 C CB  . VAL   B 30  ? 0.2134 0.2763 0.3133 -0.0156 -0.0261 0.0708  30  VAL   B CB  
4293 C CG1 . VAL   B 30  ? 0.2185 0.2819 0.3095 -0.0156 -0.0179 0.0673  30  VAL   B CG1 
4294 C CG2 . VAL   B 30  ? 0.2266 0.2758 0.3363 -0.0235 -0.0366 0.0508  30  VAL   B CG2 
4304 N N   . LYS   B 31  ? 0.1731 0.2441 0.2976 -0.0188 0.0086  0.1080  31  LYS   B N   
4305 C CA  . LYS   B 31  ? 0.1647 0.2414 0.3379 -0.0375 0.0051  0.1049  31  LYS   B CA  
4306 C C   . LYS   B 31  ? 0.1572 0.1976 0.3002 -0.0389 -0.0187 0.0835  31  LYS   B C   
4307 O O   . LYS   B 31  ? 0.1687 0.2098 0.3138 -0.0249 -0.0142 0.1011  31  LYS   B O   
4308 C CB  . LYS   B 31  ? 0.1849 0.2960 0.3937 -0.0343 0.0275  0.1219  31  LYS   B CB  
4309 C CG  . LYS   B 31  ? 0.2261 0.3502 0.4419 -0.0344 0.0431  0.1169  31  LYS   B CG  
4310 C CD  . LYS   B 31  ? 0.2761 0.4055 0.4886 -0.0290 0.0354  0.0986  31  LYS   B CD  
4311 C CE  . LYS   B 31  ? 0.3139 0.4402 0.5299 -0.0270 0.0253  0.0835  31  LYS   B CE  
4312 N NZ  . LYS   B 31  ? 0.3333 0.4569 0.5455 -0.0205 0.0152  0.0717  31  LYS   B NZ  
4326 N N   . PRO   B 32  ? 0.1683 0.1616 0.2282 -0.0362 -0.0384 0.0475  32  PRO   B N   
4327 C CA  . PRO   B 32  ? 0.1826 0.1584 0.1815 -0.0340 -0.0379 0.0320  32  PRO   B CA  
4328 C C   . PRO   B 32  ? 0.1901 0.1493 0.1803 -0.0368 -0.0538 0.0409  32  PRO   B C   
4329 O O   . PRO   B 32  ? 0.1986 0.1571 0.2182 -0.0396 -0.0695 0.0306  32  PRO   B O   
4330 C CB  . PRO   B 32  ? 0.1948 0.1554 0.1845 -0.0369 -0.0277 0.0117  32  PRO   B CB  
4331 C CG  . PRO   B 32  ? 0.2098 0.1446 0.1823 -0.0273 -0.0496 0.0265  32  PRO   B CG  
4332 C CD  . PRO   B 32  ? 0.1937 0.1510 0.2089 -0.0249 -0.0552 0.0284  32  PRO   B CD  
4340 N N   . THR   B 33  ? 0.1939 0.1393 0.1763 -0.0305 -0.0497 0.0294  33  THR   B N   
4341 C CA  . THR   B 33  ? 0.1959 0.1481 0.1754 -0.0306 -0.0430 0.0365  33  THR   B CA  
4342 C C   . THR   B 33  ? 0.1944 0.1376 0.1744 -0.0314 -0.0413 0.0228  33  THR   B C   
4343 O O   . THR   B 33  ? 0.2202 0.1401 0.1826 -0.0376 -0.0491 0.0177  33  THR   B O   
4344 C CB  . THR   B 33  ? 0.2075 0.1548 0.1814 -0.0190 -0.0546 0.0321  33  THR   B CB  
4345 O OG1 . THR   B 33  ? 0.1964 0.1666 0.1867 -0.0209 -0.0504 0.0335  33  THR   B OG1 
4346 C CG2 . THR   B 33  ? 0.2330 0.1606 0.1950 -0.0104 -0.0484 0.0197  33  THR   B CG2 
4354 N N   . VAL   B 34  ? 0.1787 0.1351 0.1485 -0.0347 -0.0420 0.0151  34  VAL   B N   
4355 C CA  . VAL   B 34  ? 0.1672 0.1332 0.1505 -0.0217 -0.0292 0.0071  34  VAL   B CA  
4356 C C   . VAL   B 34  ? 0.1572 0.1309 0.1359 -0.0295 -0.0207 0.0109  34  VAL   B C   
4357 O O   . VAL   B 34  ? 0.1743 0.1361 0.1384 -0.0286 -0.0331 0.0076  34  VAL   B O   
4358 C CB  . VAL   B 34  ? 0.1754 0.1416 0.1772 -0.0047 -0.0290 -0.0012 34  VAL   B CB  
4359 C CG1 . VAL   B 34  ? 0.1745 0.1600 0.1894 -0.0036 -0.0220 -0.0067 34  VAL   B CG1 
4360 C CG2 . VAL   B 34  ? 0.1802 0.1494 0.2036 -0.0050 -0.0295 0.0064  34  VAL   B CG2 
4370 N N   . VAL   B 35  ? 0.1467 0.1299 0.1338 -0.0244 -0.0124 0.0101  35  VAL   B N   
4371 C CA  . VAL   B 35  ? 0.1422 0.1259 0.1353 -0.0200 -0.0034 0.0096  35  VAL   B CA  
4372 C C   . VAL   B 35  ? 0.1377 0.1226 0.1298 -0.0152 -0.0121 0.0049  35  VAL   B C   
4373 O O   . VAL   B 35  ? 0.1408 0.1300 0.1339 -0.0219 -0.0018 -0.0074 35  VAL   B O   
4374 C CB  . VAL   B 35  ? 0.1413 0.1429 0.1409 -0.0219 0.0036  0.0026  35  VAL   B CB  
4375 C CG1 . VAL   B 35  ? 0.1392 0.1570 0.1575 -0.0210 0.0012  -0.0036 35  VAL   B CG1 
4376 C CG2 . VAL   B 35  ? 0.1428 0.1436 0.1634 -0.0080 -0.0012 -0.0019 35  VAL   B CG2 
4386 N N   . VAL   B 36  ? 0.1359 0.1213 0.1333 -0.0223 -0.0058 0.0036  36  VAL   B N   
4387 C CA  . VAL   B 36  ? 0.1330 0.1130 0.1391 -0.0149 -0.0062 0.0042  36  VAL   B CA  
4388 C C   . VAL   B 36  ? 0.1314 0.1180 0.1268 -0.0091 -0.0078 0.0016  36  VAL   B C   
4389 O O   . VAL   B 36  ? 0.1390 0.1330 0.1429 -0.0116 -0.0026 -0.0059 36  VAL   B O   
4390 C CB  . VAL   B 36  ? 0.1358 0.1244 0.1471 -0.0160 -0.0077 0.0072  36  VAL   B CB  
4391 C CG1 . VAL   B 36  ? 0.1339 0.1355 0.1609 -0.0230 -0.0051 0.0012  36  VAL   B CG1 
4392 C CG2 . VAL   B 36  ? 0.1416 0.1332 0.1564 -0.0129 -0.0127 0.0037  36  VAL   B CG2 
4402 N N   . ASN   B 37  ? 0.1370 0.1257 0.1294 -0.0005 -0.0050 0.0033  37  ASN   B N   
4403 C CA  . ASN   B 37  ? 0.1385 0.1246 0.1303 0.0010  -0.0052 0.0064  37  ASN   B CA  
4404 C C   . ASN   B 37  ? 0.1315 0.1283 0.1338 0.0095  -0.0075 0.0093  37  ASN   B C   
4405 O O   . ASN   B 37  ? 0.1426 0.1390 0.1306 0.0054  -0.0029 0.0091  37  ASN   B O   
4406 C CB  . ASN   B 37  ? 0.1363 0.1304 0.1297 -0.0064 -0.0202 0.0059  37  ASN   B CB  
4407 C CG  . ASN   B 37  ? 0.1426 0.1354 0.1427 0.0011  -0.0101 0.0022  37  ASN   B CG  
4408 O OD1 . ASN   B 37  ? 0.1500 0.1358 0.1541 0.0046  -0.0132 0.0079  37  ASN   B OD1 
4409 N ND2 . ASN   B 37  ? 0.1455 0.1280 0.1430 0.0026  -0.0156 0.0049  37  ASN   B ND2 
4416 N N   . ALA   B 38  ? 0.1414 0.1271 0.1410 0.0079  0.0066  0.0043  38  ALA   B N   
4417 C CA  . ALA   B 38  ? 0.1462 0.1283 0.1411 0.0039  0.0034  0.0044  38  ALA   B CA  
4418 C C   . ALA   B 38  ? 0.1479 0.1319 0.1455 0.0019  0.0013  0.0077  38  ALA   B C   
4419 O O   . ALA   B 38  ? 0.1603 0.1388 0.1539 0.0066  -0.0007 0.0101  38  ALA   B O   
4420 C CB  . ALA   B 38  ? 0.1653 0.1420 0.1545 -0.0012 0.0134  0.0086  38  ALA   B CB  
4426 N N   . ALA   B 39  ? 0.1518 0.1281 0.1341 0.0064  -0.0034 0.0035  39  ALA   B N   
4427 C CA  . ALA   B 39  ? 0.1538 0.1351 0.1374 0.0034  -0.0103 0.0025  39  ALA   B CA  
4428 C C   . ALA   B 39  ? 0.1537 0.1406 0.1334 0.0124  -0.0042 0.0038  39  ALA   B C   
4429 O O   . ALA   B 39  ? 0.1583 0.1544 0.1543 0.0029  -0.0023 0.0070  39  ALA   B O   
4430 C CB  . ALA   B 39  ? 0.1530 0.1416 0.1506 -0.0043 -0.0068 -0.0030 39  ALA   B CB  
4436 N N   . ASN   B 40  ? 0.1615 0.1651 0.1293 0.0001  0.0005  -0.0103 40  ASN   B N   
4437 C CA  . ASN   B 40  ? 0.1652 0.1665 0.1419 0.0022  -0.0097 -0.0108 40  ASN   B CA  
4438 C C   . ASN   B 40  ? 0.1716 0.1716 0.1347 0.0044  -0.0078 -0.0079 40  ASN   B C   
4439 O O   . ASN   B 40  ? 0.1693 0.1628 0.1362 0.0061  -0.0090 0.0017  40  ASN   B O   
4440 C CB  . ASN   B 40  ? 0.1786 0.1633 0.1763 0.0092  -0.0112 0.0066  40  ASN   B CB  
4441 C CG  . ASN   B 40  ? 0.1807 0.1775 0.1962 0.0032  -0.0238 0.0101  40  ASN   B CG  
4442 O OD1 . ASN   B 40  ? 0.1793 0.1768 0.2746 0.0013  -0.0407 0.0083  40  ASN   B OD1 
4443 N ND2 . ASN   B 40  ? 0.1847 0.1735 0.1955 0.0048  -0.0152 0.0148  40  ASN   B ND2 
4450 N N   . VAL   B 41  ? 0.1821 0.1774 0.1300 0.0136  -0.0003 -0.0103 41  VAL   B N   
4451 C CA  . VAL   B 41  ? 0.1814 0.1899 0.1408 0.0107  -0.0030 -0.0126 41  VAL   B CA  
4452 C C   . VAL   B 41  ? 0.1824 0.1896 0.1399 0.0182  -0.0063 -0.0190 41  VAL   B C   
4453 O O   . VAL   B 41  ? 0.1797 0.1864 0.1466 0.0162  -0.0112 -0.0165 41  VAL   B O   
4454 C CB  . VAL   B 41  ? 0.1969 0.2049 0.1635 -0.0050 0.0246  -0.0204 41  VAL   B CB  
4455 C CG1 . VAL   B 41  ? 0.1977 0.2100 0.1744 -0.0126 0.0327  -0.0137 41  VAL   B CG1 
4456 C CG2 . VAL   B 41  ? 0.2103 0.2271 0.1656 -0.0133 0.0225  -0.0190 41  VAL   B CG2 
4466 N N   . TYR   B 42  ? 0.1887 0.1875 0.1445 0.0141  -0.0228 0.0020  42  TYR   B N   
4467 C CA  . TYR   B 42  ? 0.1927 0.1927 0.1565 0.0138  -0.0309 -0.0135 42  TYR   B CA  
4468 C C   . TYR   B 42  ? 0.1786 0.1673 0.1640 0.0144  -0.0236 -0.0094 42  TYR   B C   
4469 O O   . TYR   B 42  ? 0.1828 0.1746 0.1968 0.0085  -0.0277 -0.0148 42  TYR   B O   
4470 C CB  . TYR   B 42  ? 0.2172 0.2181 0.1740 0.0123  -0.0351 0.0023  42  TYR   B CB  
4471 C CG  . TYR   B 42  ? 0.2181 0.2401 0.1672 -0.0007 -0.0299 0.0091  42  TYR   B CG  
4472 C CD1 . TYR   B 42  ? 0.2174 0.2394 0.1511 -0.0003 -0.0166 0.0010  42  TYR   B CD1 
4473 C CD2 . TYR   B 42  ? 0.2324 0.2545 0.2087 0.0005  -0.0119 0.0162  42  TYR   B CD2 
4474 C CE1 . TYR   B 42  ? 0.2300 0.2564 0.1658 0.0052  -0.0115 0.0060  42  TYR   B CE1 
4475 C CE2 . TYR   B 42  ? 0.2377 0.2662 0.2023 0.0032  0.0144  0.0310  42  TYR   B CE2 
4476 C CZ  . TYR   B 42  ? 0.2495 0.2763 0.1968 0.0199  0.0148  0.0167  42  TYR   B CZ  
4477 O OH  . TYR   B 42  ? 0.2882 0.3064 0.2415 0.0366  0.0220  0.0315  42  TYR   B OH  
4487 N N   . LEU   B 43  ? 0.1654 0.1524 0.1508 0.0067  -0.0145 -0.0033 43  LEU   B N   
4488 C CA  . LEU   B 43  ? 0.1654 0.1580 0.1421 0.0036  -0.0089 0.0081  43  LEU   B CA  
4489 C C   . LEU   B 43  ? 0.1696 0.1563 0.1360 0.0028  -0.0189 -0.0004 43  LEU   B C   
4490 O O   . LEU   B 43  ? 0.1643 0.1632 0.1677 0.0068  -0.0174 0.0036  43  LEU   B O   
4491 C CB  . LEU   B 43  ? 0.1587 0.1551 0.1510 0.0030  -0.0232 -0.0083 43  LEU   B CB  
4492 C CG  . LEU   B 43  ? 0.1656 0.1488 0.1544 0.0022  -0.0322 -0.0088 43  LEU   B CG  
4493 C CD1 . LEU   B 43  ? 0.1744 0.1534 0.2004 0.0022  -0.0428 -0.0076 43  LEU   B CD1 
4494 C CD2 . LEU   B 43  ? 0.1661 0.1476 0.1693 -0.0113 -0.0290 -0.0049 43  LEU   B CD2 
4506 N N   . LYS   B 44  ? 0.1656 0.1567 0.1511 0.0098  -0.0120 -0.0064 44  LYS   B N   
4507 C CA  . LYS   B 44  ? 0.1806 0.1651 0.1520 0.0069  -0.0090 0.0120  44  LYS   B CA  
4508 C C   . LYS   B 44  ? 0.1695 0.1569 0.1520 0.0107  -0.0147 0.0087  44  LYS   B C   
4509 O O   . LYS   B 44  ? 0.1877 0.1586 0.1802 0.0005  -0.0060 0.0035  44  LYS   B O   
4510 C CB  . LYS   B 44  ? 0.2098 0.1825 0.1762 0.0146  -0.0303 0.0116  44  LYS   B CB  
4511 C CG  . LYS   B 44  ? 0.2479 0.2132 0.2096 0.0121  -0.0585 0.0121  44  LYS   B CG  
4512 C CD  . LYS   B 44  ? 0.2815 0.2374 0.2665 -0.0030 -0.0681 0.0057  44  LYS   B CD  
4513 C CE  . LYS   B 44  ? 0.3127 0.2672 0.3144 -0.0119 -0.0711 0.0148  44  LYS   B CE  
4514 N NZ  . LYS   B 44  ? 0.3246 0.2777 0.3397 -0.0122 -0.0777 0.0312  44  LYS   B NZ  
4528 N N   . HIS   B 45  ? 0.1638 0.1603 0.1495 -0.0004 -0.0109 0.0175  45  HIS   B N   
4529 C CA  . HIS   B 45  ? 0.1688 0.1513 0.1500 0.0025  -0.0091 0.0006  45  HIS   B CA  
4530 C C   . HIS   B 45  ? 0.1898 0.1761 0.1867 0.0189  -0.0227 -0.0068 45  HIS   B C   
4531 O O   . HIS   B 45  ? 0.2032 0.2069 0.2340 0.0408  0.0067  -0.0041 45  HIS   B O   
4532 C CB  . HIS   B 45  ? 0.1610 0.1558 0.1673 -0.0015 -0.0105 -0.0040 45  HIS   B CB  
4533 C CG  . HIS   B 45  ? 0.1642 0.1534 0.1482 -0.0090 -0.0082 0.0050  45  HIS   B CG  
4534 N ND1 . HIS   B 45  ? 0.1634 0.1490 0.1607 -0.0027 -0.0212 -0.0060 45  HIS   B ND1 
4535 C CD2 . HIS   B 45  ? 0.1746 0.1621 0.1688 -0.0148 -0.0174 0.0054  45  HIS   B CD2 
4536 C CE1 . HIS   B 45  ? 0.1750 0.1389 0.1528 -0.0007 -0.0273 -0.0082 45  HIS   B CE1 
4537 N NE2 . HIS   B 45  ? 0.1775 0.1506 0.1658 -0.0007 -0.0201 -0.0055 45  HIS   B NE2 
4545 N N   A GLY   B 46  ? 0.2071 0.1725 0.2177 0.0192  -0.0415 0.0118  46  GLY   B N   
4546 N N   B GLY   B 46  ? 0.2003 0.1822 0.2086 0.0180  -0.0316 0.0058  46  GLY   B N   
4547 C CA  A GLY   B 46  ? 0.2190 0.1802 0.2597 0.0173  -0.0471 0.0120  46  GLY   B CA  
4548 C CA  B GLY   B 46  ? 0.2088 0.1924 0.2333 0.0160  -0.0364 0.0119  46  GLY   B CA  
4549 C C   A GLY   B 46  ? 0.2134 0.1957 0.3107 0.0289  -0.0391 0.0061  46  GLY   B C   
4550 C C   B GLY   B 46  ? 0.2101 0.2057 0.2635 0.0195  -0.0340 0.0145  46  GLY   B C   
4551 O O   A GLY   B 46  ? 0.2264 0.2112 0.4052 0.0385  -0.0134 -0.0186 46  GLY   B O   
4552 O O   B GLY   B 46  ? 0.2165 0.2181 0.2767 0.0225  -0.0345 0.0249  46  GLY   B O   
4559 N N   . GLY   B 47  ? 0.2076 0.2109 0.2842 0.0123  -0.0217 0.0027  47  GLY   B N   
4560 C CA  . GLY   B 47  ? 0.1949 0.1810 0.2430 0.0097  -0.0185 0.0099  47  GLY   B CA  
4561 C C   . GLY   B 47  ? 0.1772 0.1593 0.1941 0.0089  0.0044  0.0100  47  GLY   B C   
4562 O O   . GLY   B 47  ? 0.1885 0.1465 0.2040 0.0056  -0.0077 0.0128  47  GLY   B O   
4567 N N   . GLY   B 48  ? 0.1619 0.1505 0.2051 0.0073  -0.0073 0.0168  48  GLY   B N   
4568 C CA  . GLY   B 48  ? 0.1611 0.1449 0.1857 -0.0014 -0.0058 0.0091  48  GLY   B CA  
4569 C C   . GLY   B 48  ? 0.1550 0.1384 0.1712 0.0000  0.0024  0.0053  48  GLY   B C   
4570 O O   . GLY   B 48  ? 0.1496 0.1477 0.1998 0.0067  -0.0041 0.0053  48  GLY   B O   
4574 N N   . VAL   B 49  ? 0.1577 0.1460 0.1631 0.0155  -0.0009 0.0113  49  VAL   B N   
4575 C CA  . VAL   B 49  ? 0.1556 0.1545 0.1579 0.0139  -0.0136 -0.0038 49  VAL   B CA  
4576 C C   . VAL   B 49  ? 0.1469 0.1479 0.1370 0.0089  -0.0044 0.0024  49  VAL   B C   
4577 O O   . VAL   B 49  ? 0.1540 0.1544 0.1598 0.0074  0.0030  0.0107  49  VAL   B O   
4578 C CB  . VAL   B 49  ? 0.1622 0.1660 0.1977 0.0036  -0.0267 0.0002  49  VAL   B CB  
4579 C CG1 . VAL   B 49  ? 0.1654 0.1792 0.1930 0.0062  -0.0419 -0.0013 49  VAL   B CG1 
4580 C CG2 . VAL   B 49  ? 0.1774 0.1795 0.2271 -0.0014 -0.0446 -0.0059 49  VAL   B CG2 
4590 N N   . ALA   B 50  ? 0.1409 0.1461 0.1443 -0.0008 -0.0023 0.0041  50  ALA   B N   
4591 C CA  . ALA   B 50  ? 0.1383 0.1376 0.1496 0.0037  -0.0051 0.0040  50  ALA   B CA  
4592 C C   . ALA   B 50  ? 0.1513 0.1432 0.1545 0.0040  -0.0034 0.0027  50  ALA   B C   
4593 O O   . ALA   B 50  ? 0.1494 0.1433 0.1534 0.0038  -0.0044 0.0030  50  ALA   B O   
4594 C CB  . ALA   B 50  ? 0.1482 0.1428 0.1600 0.0072  -0.0083 0.0127  50  ALA   B CB  
4600 N N   . GLY   B 51  ? 0.1436 0.1529 0.1683 0.0126  -0.0071 0.0091  51  GLY   B N   
4601 C CA  . GLY   B 51  ? 0.1483 0.1603 0.1772 0.0219  -0.0156 0.0159  51  GLY   B CA  
4602 C C   . GLY   B 51  ? 0.1476 0.1522 0.1831 0.0189  -0.0196 0.0105  51  GLY   B C   
4603 O O   . GLY   B 51  ? 0.1504 0.1636 0.2019 0.0092  -0.0173 -0.0012 51  GLY   B O   
4607 N N   . ALA   B 52  ? 0.1400 0.1488 0.1745 0.0183  -0.0075 0.0140  52  ALA   B N   
4608 C CA  . ALA   B 52  ? 0.1536 0.1605 0.1708 0.0215  0.0070  -0.0020 52  ALA   B CA  
4609 C C   . ALA   B 52  ? 0.1445 0.1558 0.1555 0.0131  0.0006  -0.0031 52  ALA   B C   
4610 O O   . ALA   B 52  ? 0.1465 0.1625 0.1881 0.0130  0.0048  0.0049  52  ALA   B O   
4611 C CB  . ALA   B 52  ? 0.1730 0.1612 0.1746 0.0040  0.0051  -0.0023 52  ALA   B CB  
4617 N N   . LEU   B 53  ? 0.1441 0.1493 0.1557 0.0189  0.0004  -0.0001 53  LEU   B N   
4618 C CA  . LEU   B 53  ? 0.1345 0.1554 0.1671 0.0131  -0.0060 0.0028  53  LEU   B CA  
4619 C C   . LEU   B 53  ? 0.1426 0.1487 0.1594 0.0133  -0.0005 0.0099  53  LEU   B C   
4620 O O   . LEU   B 53  ? 0.1478 0.1569 0.1716 -0.0034 -0.0013 0.0145  53  LEU   B O   
4621 C CB  . LEU   B 53  ? 0.1411 0.1620 0.1813 0.0056  -0.0088 0.0171  53  LEU   B CB  
4622 C CG  . LEU   B 53  ? 0.1400 0.1689 0.1764 0.0046  -0.0014 0.0240  53  LEU   B CG  
4623 C CD1 . LEU   B 53  ? 0.1517 0.1913 0.2087 0.0099  -0.0062 0.0087  53  LEU   B CD1 
4624 C CD2 . LEU   B 53  ? 0.1603 0.1994 0.2095 -0.0088 -0.0055 -0.0117 53  LEU   B CD2 
4636 N N   . ASN   B 54  ? 0.1475 0.1447 0.1538 0.0082  -0.0087 0.0047  54  ASN   B N   
4637 C CA  . ASN   B 54  ? 0.1529 0.1544 0.1673 0.0034  -0.0097 -0.0009 54  ASN   B CA  
4638 C C   . ASN   B 54  ? 0.1468 0.1579 0.1782 0.0027  0.0003  0.0001  54  ASN   B C   
4639 O O   . ASN   B 54  ? 0.1423 0.1631 0.1890 -0.0047 -0.0038 0.0009  54  ASN   B O   
4640 C CB  . ASN   B 54  ? 0.1584 0.1737 0.1835 0.0061  -0.0087 0.0064  54  ASN   B CB  
4641 C CG  . ASN   B 54  ? 0.1568 0.1780 0.1762 0.0029  -0.0138 0.0040  54  ASN   B CG  
4642 O OD1 . ASN   B 54  ? 0.1551 0.1758 0.1830 -0.0014 -0.0154 -0.0095 54  ASN   B OD1 
4643 N ND2 . ASN   B 54  ? 0.1675 0.1893 0.2074 -0.0026 -0.0328 0.0123  54  ASN   B ND2 
4650 N N   . LYS   B 55  ? 0.1451 0.1588 0.2019 0.0122  -0.0031 0.0029  55  LYS   B N   
4651 C CA  . LYS   B 55  ? 0.1523 0.1719 0.2291 0.0168  -0.0039 0.0111  55  LYS   B CA  
4652 C C   . LYS   B 55  ? 0.1462 0.1676 0.2190 0.0133  0.0097  -0.0004 55  LYS   B C   
4653 O O   . LYS   B 55  ? 0.1412 0.1855 0.2271 0.0097  0.0061  -0.0013 55  LYS   B O   
4654 C CB  . LYS   B 55  ? 0.1643 0.1919 0.2606 0.0289  0.0079  0.0267  55  LYS   B CB  
4655 C CG  . LYS   B 55  ? 0.2118 0.2191 0.3470 0.0328  0.0226  0.0386  55  LYS   B CG  
4656 C CD  . LYS   B 55  ? 0.2465 0.2455 0.4220 0.0431  0.0403  0.0512  55  LYS   B CD  
4657 C CE  . LYS   B 55  ? 0.2728 0.2713 0.4931 0.0445  0.0533  0.0529  55  LYS   B CE  
4658 N NZ  . LYS   B 55  ? 0.2838 0.2901 0.5288 0.0444  0.0338  0.0631  55  LYS   B NZ  
4672 N N   . ALA   B 56  ? 0.1469 0.1751 0.1964 0.0099  0.0017  -0.0128 56  ALA   B N   
4673 C CA  . ALA   B 56  ? 0.1623 0.1967 0.1925 0.0009  0.0046  -0.0090 56  ALA   B CA  
4674 C C   . ALA   B 56  ? 0.1594 0.1916 0.1838 0.0025  0.0184  0.0003  56  ALA   B C   
4675 O O   . ALA   B 56  ? 0.1706 0.2069 0.2053 0.0049  0.0288  0.0048  56  ALA   B O   
4676 C CB  . ALA   B 56  ? 0.1751 0.2123 0.1905 -0.0128 0.0005  0.0025  56  ALA   B CB  
4682 N N   . THR   B 57  ? 0.1548 0.1846 0.1855 0.0000  0.0149  0.0026  57  THR   B N   
4683 C CA  . THR   B 57  ? 0.1628 0.1778 0.1892 -0.0011 0.0129  0.0085  57  THR   B CA  
4684 C C   . THR   B 57  ? 0.1616 0.1849 0.2150 0.0002  0.0171  0.0106  57  THR   B C   
4685 O O   . THR   B 57  ? 0.1700 0.1935 0.2204 -0.0186 0.0135  0.0120  57  THR   B O   
4686 C CB  . THR   B 57  ? 0.1686 0.1584 0.1658 0.0006  0.0148  0.0204  57  THR   B CB  
4687 O OG1 . THR   B 57  ? 0.1643 0.1611 0.1860 -0.0047 0.0132  0.0107  57  THR   B OG1 
4688 C CG2 . THR   B 57  ? 0.1613 0.1656 0.1856 -0.0057 0.0117  0.0138  57  THR   B CG2 
4696 N N   . ASN   B 58  ? 0.1479 0.2010 0.2284 -0.0167 0.0089  -0.0108 58  ASN   B N   
4697 C CA  . ASN   B 58  ? 0.1651 0.2498 0.2758 -0.0307 0.0287  0.0029  58  ASN   B CA  
4698 C C   . ASN   B 58  ? 0.1464 0.2276 0.2402 -0.0233 -0.0033 0.0019  58  ASN   B C   
4699 O O   . ASN   B 58  ? 0.1551 0.2379 0.2417 -0.0253 -0.0015 -0.0086 58  ASN   B O   
4700 C CB  . ASN   B 58  ? 0.2580 0.3293 0.4077 -0.0518 0.0590  0.0193  58  ASN   B CB  
4701 C CG  . ASN   B 58  ? 0.3715 0.4051 0.5648 -0.0574 0.0706  0.0408  58  ASN   B CG  
4702 O OD1 . ASN   B 58  ? 0.3974 0.4299 0.6221 -0.0594 0.0731  0.0467  58  ASN   B OD1 
4703 N ND2 . ASN   B 58  ? 0.4739 0.4739 0.6160 -0.0609 0.0767  0.0475  58  ASN   B ND2 
4710 N N   . ASN   B 59  ? 0.1519 0.2133 0.2070 -0.0155 -0.0146 0.0072  59  ASN   B N   
4711 C CA  . ASN   B 59  ? 0.1587 0.2105 0.1977 -0.0184 -0.0174 0.0082  59  ASN   B CA  
4712 C C   . ASN   B 59  ? 0.1512 0.2000 0.1893 -0.0219 -0.0166 -0.0004 59  ASN   B C   
4713 O O   . ASN   B 59  ? 0.1512 0.2048 0.1850 -0.0173 -0.0066 -0.0002 59  ASN   B O   
4714 C CB  . ASN   B 59  ? 0.1680 0.2301 0.2228 -0.0128 -0.0279 0.0129  59  ASN   B CB  
4715 C CG  . ASN   B 59  ? 0.1792 0.2502 0.2454 -0.0119 -0.0351 0.0110  59  ASN   B CG  
4716 O OD1 . ASN   B 59  ? 0.1763 0.2568 0.2322 -0.0084 -0.0202 0.0211  59  ASN   B OD1 
4717 N ND2 . ASN   B 59  ? 0.1872 0.2571 0.2514 -0.0212 -0.0364 0.0114  59  ASN   B ND2 
4724 N N   . ALA   B 60  ? 0.1528 0.1898 0.2002 -0.0172 -0.0041 0.0002  60  ALA   B N   
4725 C CA  . ALA   B 60  ? 0.1569 0.1799 0.1974 -0.0205 -0.0049 0.0066  60  ALA   B CA  
4726 C C   . ALA   B 60  ? 0.1551 0.1685 0.1727 -0.0151 -0.0056 0.0065  60  ALA   B C   
4727 O O   . ALA   B 60  ? 0.1604 0.1649 0.1895 -0.0195 0.0025  -0.0017 60  ALA   B O   
4728 C CB  . ALA   B 60  ? 0.1751 0.1768 0.2259 -0.0125 -0.0022 0.0034  60  ALA   B CB  
4734 N N   . MET   B 61  ? 0.1474 0.1592 0.1746 -0.0129 0.0007  0.0033  61  MET   B N   
4735 C CA  . MET   B 61  ? 0.1505 0.1477 0.1689 -0.0097 -0.0108 0.0061  61  MET   B CA  
4736 C C   . MET   B 61  ? 0.1603 0.1439 0.1648 -0.0103 -0.0142 0.0095  61  MET   B C   
4737 O O   . MET   B 61  ? 0.1593 0.1462 0.1651 -0.0017 -0.0084 -0.0081 61  MET   B O   
4738 C CB  . MET   B 61  ? 0.1491 0.1559 0.1659 -0.0024 -0.0108 0.0016  61  MET   B CB  
4739 C CG  . MET   B 61  ? 0.1433 0.1509 0.1612 -0.0079 -0.0114 0.0033  61  MET   B CG  
4740 S SD  . MET   B 61  ? 0.1463 0.1557 0.1866 -0.0037 -0.0066 -0.0086 61  MET   B SD  
4741 C CE  . MET   B 61  ? 0.1553 0.1764 0.2117 0.0028  -0.0119 -0.0242 61  MET   B CE  
4751 N N   . GLN   B 62  ? 0.1544 0.1556 0.1635 -0.0067 -0.0187 0.0022  62  GLN   B N   
4752 C CA  . GLN   B 62  ? 0.1629 0.1608 0.1660 -0.0024 -0.0185 0.0014  62  GLN   B CA  
4753 C C   . GLN   B 62  ? 0.1589 0.1667 0.1674 -0.0053 -0.0309 -0.0053 62  GLN   B C   
4754 O O   . GLN   B 62  ? 0.1715 0.1695 0.1768 -0.0053 -0.0342 -0.0120 62  GLN   B O   
4755 C CB  . GLN   B 62  ? 0.1663 0.1606 0.1624 -0.0021 -0.0147 0.0045  62  GLN   B CB  
4756 C CG  . GLN   B 62  ? 0.1644 0.1647 0.1664 -0.0004 -0.0266 0.0006  62  GLN   B CG  
4757 C CD  . GLN   B 62  ? 0.1645 0.1641 0.1596 0.0037  -0.0279 0.0064  62  GLN   B CD  
4758 O OE1 . GLN   B 62  ? 0.1677 0.1606 0.1785 -0.0031 -0.0227 -0.0015 62  GLN   B OE1 
4759 N NE2 . GLN   B 62  ? 0.1660 0.1704 0.1686 -0.0005 -0.0263 -0.0048 62  GLN   B NE2 
4768 N N   . VAL   B 63  ? 0.1551 0.1668 0.1926 -0.0108 -0.0242 -0.0118 63  VAL   B N   
4769 C CA  . VAL   B 63  ? 0.1702 0.1685 0.2199 -0.0201 -0.0334 -0.0087 63  VAL   B CA  
4770 C C   . VAL   B 63  ? 0.1719 0.1536 0.1954 -0.0233 -0.0364 -0.0167 63  VAL   B C   
4771 O O   . VAL   B 63  ? 0.1858 0.1599 0.2104 -0.0188 -0.0511 -0.0166 63  VAL   B O   
4772 C CB  . VAL   B 63  ? 0.1687 0.1858 0.2519 -0.0248 -0.0344 -0.0079 63  VAL   B CB  
4773 C CG1 . VAL   B 63  ? 0.1764 0.1842 0.2700 -0.0304 -0.0301 -0.0049 63  VAL   B CG1 
4774 C CG2 . VAL   B 63  ? 0.1632 0.2032 0.2610 -0.0161 -0.0324 -0.0060 63  VAL   B CG2 
4784 N N   . GLU   B 64  ? 0.1644 0.1525 0.1957 -0.0144 -0.0287 -0.0152 64  GLU   B N   
4785 C CA  . GLU   B 64  ? 0.1692 0.1466 0.1822 -0.0126 -0.0322 -0.0023 64  GLU   B CA  
4786 C C   . GLU   B 64  ? 0.1606 0.1491 0.1632 -0.0048 -0.0320 -0.0077 64  GLU   B C   
4787 O O   . GLU   B 64  ? 0.1688 0.1571 0.1787 -0.0095 -0.0255 -0.0143 64  GLU   B O   
4788 C CB  . GLU   B 64  ? 0.1711 0.1522 0.1894 -0.0164 -0.0289 -0.0023 64  GLU   B CB  
4789 C CG  . GLU   B 64  ? 0.1729 0.1596 0.1761 -0.0231 -0.0381 -0.0131 64  GLU   B CG  
4790 C CD  . GLU   B 64  ? 0.1787 0.1746 0.1851 -0.0299 -0.0290 0.0008  64  GLU   B CD  
4791 O OE1 . GLU   B 64  ? 0.1729 0.1883 0.1956 -0.0331 -0.0205 -0.0166 64  GLU   B OE1 
4792 O OE2 . GLU   B 64  ? 0.1929 0.1927 0.1799 -0.0388 -0.0439 -0.0032 64  GLU   B OE2 
4799 N N   . SER   B 65  ? 0.1601 0.1434 0.1637 -0.0120 -0.0192 -0.0131 65  SER   B N   
4800 C CA  . SER   B 65  ? 0.1638 0.1440 0.1692 -0.0017 -0.0234 -0.0151 65  SER   B CA  
4801 C C   . SER   B 65  ? 0.1657 0.1536 0.1678 -0.0014 -0.0324 -0.0151 65  SER   B C   
4802 O O   . SER   B 65  ? 0.1670 0.1613 0.1703 -0.0002 -0.0232 -0.0230 65  SER   B O   
4803 C CB  . SER   B 65  ? 0.1686 0.1491 0.1676 -0.0109 -0.0238 -0.0065 65  SER   B CB  
4804 O OG  . SER   B 65  ? 0.1692 0.1541 0.1781 -0.0110 -0.0224 -0.0142 65  SER   B OG  
4810 N N   . ASP   B 66  ? 0.1752 0.1573 0.1558 0.0010  -0.0286 -0.0102 66  ASP   B N   
4811 C CA  . ASP   B 66  ? 0.1810 0.1689 0.1481 0.0014  -0.0349 -0.0115 66  ASP   B CA  
4812 C C   . ASP   B 66  ? 0.1903 0.1712 0.1463 -0.0055 -0.0240 -0.0213 66  ASP   B C   
4813 O O   . ASP   B 66  ? 0.1964 0.1786 0.1595 -0.0009 -0.0329 -0.0252 66  ASP   B O   
4814 C CB  . ASP   B 66  ? 0.1946 0.1799 0.1806 0.0135  -0.0439 -0.0164 66  ASP   B CB  
4815 C CG  . ASP   B 66  ? 0.2225 0.1979 0.2076 0.0175  -0.0613 -0.0013 66  ASP   B CG  
4816 O OD1 . ASP   B 66  ? 0.2450 0.1957 0.2195 0.0089  -0.0568 0.0089  66  ASP   B OD1 
4817 O OD2 . ASP   B 66  ? 0.2413 0.2213 0.2743 0.0327  -0.0630 0.0094  66  ASP   B OD2 
4822 N N   . ASP   B 67  ? 0.1837 0.1661 0.1582 -0.0084 -0.0194 -0.0216 67  ASP   B N   
4823 C CA  . ASP   B 67  ? 0.2006 0.1634 0.1730 -0.0082 -0.0222 -0.0113 67  ASP   B CA  
4824 C C   . ASP   B 67  ? 0.1911 0.1564 0.1813 -0.0015 -0.0275 -0.0194 67  ASP   B C   
4825 O O   . ASP   B 67  ? 0.1957 0.1632 0.1935 -0.0016 -0.0200 -0.0273 67  ASP   B O   
4826 C CB  . ASP   B 67  ? 0.2211 0.1737 0.1898 -0.0157 -0.0459 -0.0123 67  ASP   B CB  
4827 C CG  . ASP   B 67  ? 0.2565 0.1745 0.1992 -0.0127 -0.0705 -0.0173 67  ASP   B CG  
4828 O OD1 . ASP   B 67  ? 0.2799 0.1791 0.2128 -0.0123 -0.0637 -0.0184 67  ASP   B OD1 
4829 O OD2 . ASP   B 67  ? 0.2755 0.1794 0.2200 0.0010  -0.0758 -0.0151 67  ASP   B OD2 
4834 N N   . TYR   B 68  ? 0.1812 0.1556 0.1747 0.0020  -0.0400 -0.0247 68  TYR   B N   
4835 C CA  . TYR   B 68  ? 0.1808 0.1710 0.1925 0.0077  -0.0407 -0.0321 68  TYR   B CA  
4836 C C   . TYR   B 68  ? 0.1707 0.1709 0.1860 0.0055  -0.0354 -0.0397 68  TYR   B C   
4837 O O   . TYR   B 68  ? 0.1796 0.1821 0.2022 0.0083  -0.0353 -0.0573 68  TYR   B O   
4838 C CB  . TYR   B 68  ? 0.1894 0.1916 0.1952 0.0107  -0.0500 -0.0528 68  TYR   B CB  
4839 C CG  . TYR   B 68  ? 0.1988 0.2137 0.2049 0.0194  -0.0382 -0.0705 68  TYR   B CG  
4840 C CD1 . TYR   B 68  ? 0.2000 0.2215 0.2424 -0.0041 -0.0385 -0.0770 68  TYR   B CD1 
4841 C CD2 . TYR   B 68  ? 0.1972 0.2360 0.2320 0.0248  -0.0523 -0.0638 68  TYR   B CD2 
4842 C CE1 . TYR   B 68  ? 0.2004 0.2376 0.2662 -0.0020 -0.0338 -0.0801 68  TYR   B CE1 
4843 C CE2 . TYR   B 68  ? 0.1952 0.2409 0.2450 0.0199  -0.0427 -0.0883 68  TYR   B CE2 
4844 C CZ  . TYR   B 68  ? 0.1942 0.2474 0.2644 0.0046  -0.0424 -0.0852 68  TYR   B CZ  
4845 O OH  . TYR   B 68  ? 0.1926 0.2710 0.2973 -0.0010 -0.0339 -0.0610 68  TYR   B OH  
4855 N N   . ILE   B 69  ? 0.1708 0.1611 0.1893 0.0060  -0.0356 -0.0341 69  ILE   B N   
4856 C CA  . ILE   B 69  ? 0.1816 0.1697 0.1997 -0.0047 -0.0258 -0.0397 69  ILE   B CA  
4857 C C   . ILE   B 69  ? 0.1810 0.1686 0.1899 0.0062  -0.0433 -0.0314 69  ILE   B C   
4858 O O   . ILE   B 69  ? 0.1833 0.1797 0.1879 0.0082  -0.0258 -0.0369 69  ILE   B O   
4859 C CB  . ILE   B 69  ? 0.1911 0.1743 0.2137 -0.0073 0.0046  -0.0362 69  ILE   B CB  
4860 C CG1 . ILE   B 69  ? 0.1895 0.1797 0.2304 -0.0068 0.0063  -0.0372 69  ILE   B CG1 
4861 C CG2 . ILE   B 69  ? 0.2102 0.1803 0.2305 -0.0037 0.0051  -0.0294 69  ILE   B CG2 
4862 C CD1 . ILE   B 69  ? 0.1808 0.1805 0.2453 -0.0156 0.0031  -0.0405 69  ILE   B CD1 
4874 N N   . ALA   B 70  ? 0.1817 0.1679 0.1919 0.0034  -0.0463 -0.0329 70  ALA   B N   
4875 C CA  . ALA   B 70  ? 0.1842 0.1725 0.1801 0.0036  -0.0457 -0.0190 70  ALA   B CA  
4876 C C   . ALA   B 70  ? 0.1840 0.1674 0.1869 0.0009  -0.0446 -0.0429 70  ALA   B C   
4877 O O   . ALA   B 70  ? 0.1863 0.1718 0.1928 0.0033  -0.0365 -0.0413 70  ALA   B O   
4878 C CB  . ALA   B 70  ? 0.1916 0.1831 0.1821 0.0001  -0.0494 -0.0211 70  ALA   B CB  
4884 N N   . THR   B 71  ? 0.1940 0.1716 0.1903 0.0007  -0.0519 -0.0340 71  THR   B N   
4885 C CA  . THR   B 71  ? 0.2124 0.1763 0.2098 0.0097  -0.0662 -0.0382 71  THR   B CA  
4886 C C   . THR   B 71  ? 0.2106 0.1773 0.2316 0.0272  -0.0682 -0.0537 71  THR   B C   
4887 O O   . THR   B 71  ? 0.2200 0.1778 0.2803 0.0280  -0.0640 -0.0695 71  THR   B O   
4888 C CB  . THR   B 71  ? 0.2358 0.1980 0.2329 0.0012  -0.0785 -0.0181 71  THR   B CB  
4889 O OG1 . THR   B 71  ? 0.2502 0.2244 0.2782 -0.0192 -0.0765 -0.0004 71  THR   B OG1 
4890 C CG2 . THR   B 71  ? 0.2508 0.1969 0.2615 0.0100  -0.0643 0.0067  71  THR   B CG2 
4898 N N   . ASN   B 72  ? 0.1979 0.1851 0.2243 0.0194  -0.0660 -0.0720 72  ASN   B N   
4899 C CA  . ASN   B 72  ? 0.1959 0.1985 0.2301 0.0167  -0.0557 -0.0752 72  ASN   B CA  
4900 C C   . ASN   B 72  ? 0.1929 0.2081 0.2391 0.0048  -0.0273 -0.0745 72  ASN   B C   
4901 O O   . ASN   B 72  ? 0.1934 0.2216 0.2706 0.0044  -0.0056 -0.0792 72  ASN   B O   
4902 C CB  . ASN   B 72  ? 0.2013 0.2152 0.2442 0.0191  -0.0638 -0.0619 72  ASN   B CB  
4903 C CG  . ASN   B 72  ? 0.2167 0.2304 0.2504 0.0328  -0.0590 -0.0399 72  ASN   B CG  
4904 O OD1 . ASN   B 72  ? 0.2375 0.2475 0.2484 0.0200  -0.0391 -0.0460 72  ASN   B OD1 
4905 N ND2 . ASN   B 72  ? 0.2319 0.2363 0.2929 0.0507  -0.0519 -0.0068 72  ASN   B ND2 
4912 N N   . GLY   B 73  ? 0.1944 0.2120 0.2191 -0.0022 -0.0358 -0.0678 73  GLY   B N   
4913 C CA  . GLY   B 73  ? 0.1879 0.2200 0.2025 -0.0017 -0.0285 -0.0566 73  GLY   B CA  
4914 C C   . GLY   B 73  ? 0.1857 0.2151 0.1571 0.0038  -0.0277 -0.0542 73  GLY   B C   
4915 O O   . GLY   B 73  ? 0.1756 0.1991 0.1706 0.0097  -0.0216 -0.0373 73  GLY   B O   
4919 N N   . PRO   B 74  ? 0.1883 0.2244 0.1581 0.0034  -0.0317 -0.0422 74  PRO   B N   
4920 C CA  . PRO   B 74  ? 0.1792 0.2208 0.1476 0.0068  -0.0219 -0.0272 74  PRO   B CA  
4921 C C   . PRO   B 74  ? 0.1691 0.2008 0.1448 0.0070  -0.0146 -0.0179 74  PRO   B C   
4922 O O   . PRO   B 74  ? 0.1748 0.1992 0.1843 0.0076  -0.0106 -0.0337 74  PRO   B O   
4923 C CB  . PRO   B 74  ? 0.1961 0.2423 0.1561 -0.0001 -0.0251 -0.0233 74  PRO   B CB  
4924 C CG  . PRO   B 74  ? 0.2167 0.2516 0.1845 0.0043  -0.0180 -0.0169 74  PRO   B CG  
4925 C CD  . PRO   B 74  ? 0.2096 0.2406 0.1813 0.0080  -0.0181 -0.0310 74  PRO   B CD  
4933 N N   . LEU   B 75  ? 0.1667 0.1881 0.1307 0.0087  -0.0191 -0.0208 75  LEU   B N   
4934 C CA  . LEU   B 75  ? 0.1701 0.1873 0.1397 0.0017  -0.0197 -0.0032 75  LEU   B CA  
4935 C C   . LEU   B 75  ? 0.1740 0.1996 0.1360 0.0072  -0.0105 -0.0116 75  LEU   B C   
4936 O O   . LEU   B 75  ? 0.1859 0.2158 0.1519 0.0040  -0.0087 -0.0041 75  LEU   B O   
4937 C CB  . LEU   B 75  ? 0.1807 0.1866 0.1309 -0.0120 -0.0209 0.0097  75  LEU   B CB  
4938 C CG  . LEU   B 75  ? 0.2076 0.1984 0.1606 -0.0306 -0.0090 0.0016  75  LEU   B CG  
4939 C CD1 . LEU   B 75  ? 0.2410 0.2094 0.1665 -0.0415 0.0125  -0.0038 75  LEU   B CD1 
4940 C CD2 . LEU   B 75  ? 0.2421 0.2211 0.2255 -0.0216 0.0079  0.0126  75  LEU   B CD2 
4952 N N   . LYS   B 76  ? 0.1719 0.2204 0.1712 -0.0050 -0.0066 0.0003  76  LYS   B N   
4953 C CA  . LYS   B 76  ? 0.1826 0.2280 0.1988 -0.0098 0.0113  -0.0047 76  LYS   B CA  
4954 C C   . LYS   B 76  ? 0.1771 0.2082 0.1611 -0.0028 0.0030  0.0117  76  LYS   B C   
4955 O O   . LYS   B 76  ? 0.1767 0.1943 0.1679 -0.0029 -0.0011 0.0193  76  LYS   B O   
4956 C CB  . LYS   B 76  ? 0.1967 0.2411 0.2709 -0.0148 0.0346  -0.0358 76  LYS   B CB  
4957 C CG  . LYS   B 76  ? 0.2090 0.2636 0.3209 -0.0056 0.0265  -0.0412 76  LYS   B CG  
4958 C CD  . LYS   B 76  ? 0.2081 0.2743 0.3574 0.0071  0.0186  -0.0587 76  LYS   B CD  
4959 C CE  . LYS   B 76  ? 0.2202 0.2919 0.4090 0.0112  0.0031  -0.0661 76  LYS   B CE  
4960 N NZ  . LYS   B 76  ? 0.2233 0.2987 0.4269 0.0128  -0.0202 -0.0852 76  LYS   B NZ  
4974 N N   . VAL   B 77  ? 0.1833 0.2197 0.1677 0.0087  0.0100  0.0214  77  VAL   B N   
4975 C CA  . VAL   B 77  ? 0.1859 0.2115 0.1815 0.0141  0.0175  0.0469  77  VAL   B CA  
4976 C C   . VAL   B 77  ? 0.1667 0.1933 0.1753 0.0160  0.0202  0.0339  77  VAL   B C   
4977 O O   . VAL   B 77  ? 0.1734 0.1904 0.1711 0.0262  0.0244  0.0257  77  VAL   B O   
4978 C CB  . VAL   B 77  ? 0.1940 0.2216 0.2107 0.0120  0.0256  0.0578  77  VAL   B CB  
4979 C CG1 . VAL   B 77  ? 0.1986 0.2129 0.2466 0.0045  0.0276  0.0633  77  VAL   B CG1 
4980 C CG2 . VAL   B 77  ? 0.2086 0.2391 0.2360 0.0086  0.0110  0.0676  77  VAL   B CG2 
4990 N N   . GLY   B 78  ? 0.1628 0.1763 0.1740 0.0123  0.0173  0.0260  78  GLY   B N   
4991 C CA  . GLY   B 78  ? 0.1622 0.1679 0.1699 0.0140  0.0210  0.0174  78  GLY   B CA  
4992 C C   . GLY   B 78  ? 0.1567 0.1638 0.1519 0.0087  0.0197  0.0121  78  GLY   B C   
4993 O O   . GLY   B 78  ? 0.1634 0.1627 0.1649 0.0140  0.0101  0.0158  78  GLY   B O   
4997 N N   . GLY   B 79  ? 0.1522 0.1660 0.1553 0.0084  0.0061  0.0091  79  GLY   B N   
4998 C CA  . GLY   B 79  ? 0.1565 0.1565 0.1614 0.0101  0.0054  0.0064  79  GLY   B CA  
4999 C C   . GLY   B 79  ? 0.1451 0.1524 0.1513 0.0145  0.0065  -0.0042 79  GLY   B C   
5000 O O   . GLY   B 79  ? 0.1494 0.1508 0.1665 0.0113  0.0110  0.0128  79  GLY   B O   
5004 N N   . SER   B 80  ? 0.1453 0.1478 0.1643 0.0069  0.0126  0.0004  80  SER   B N   
5005 C CA  . SER   B 80  ? 0.1392 0.1462 0.1666 0.0044  0.0045  -0.0016 80  SER   B CA  
5006 C C   . SER   B 80  ? 0.1438 0.1434 0.1547 0.0063  -0.0043 0.0049  80  SER   B C   
5007 O O   . SER   B 80  ? 0.1569 0.1451 0.1919 0.0111  0.0008  -0.0042 80  SER   B O   
5008 C CB  . SER   B 80  ? 0.1483 0.1480 0.1682 -0.0045 0.0041  0.0065  80  SER   B CB  
5009 O OG  . SER   B 80  ? 0.1531 0.1619 0.1769 -0.0014 -0.0117 0.0105  80  SER   B OG  
5015 N N   . CYS   B 81  ? 0.1426 0.1296 0.1613 0.0036  -0.0071 0.0004  81  CYS   B N   
5016 C CA  . CYS   B 81  ? 0.1510 0.1323 0.1644 0.0031  -0.0115 0.0035  81  CYS   B CA  
5017 C C   . CYS   B 81  ? 0.1411 0.1299 0.1519 0.0021  -0.0206 0.0001  81  CYS   B C   
5018 O O   . CYS   B 81  ? 0.1657 0.1279 0.1553 0.0084  -0.0034 -0.0083 81  CYS   B O   
5019 C CB  . CYS   B 81  ? 0.1646 0.1463 0.1578 -0.0003 -0.0169 0.0068  81  CYS   B CB  
5020 S SG  . CYS   B 81  ? 0.1641 0.1612 0.1672 -0.0026 -0.0253 -0.0123 81  CYS   B SG  
5026 N N   . VAL   B 82  ? 0.1453 0.1249 0.1592 -0.0002 -0.0107 -0.0073 82  VAL   B N   
5027 C CA  . VAL   B 82  ? 0.1566 0.1311 0.1557 -0.0026 -0.0084 0.0057  82  VAL   B CA  
5028 C C   . VAL   B 82  ? 0.1659 0.1278 0.1617 0.0012  -0.0085 -0.0062 82  VAL   B C   
5029 O O   . VAL   B 82  ? 0.1721 0.1275 0.1943 -0.0009 -0.0147 -0.0137 82  VAL   B O   
5030 C CB  . VAL   B 82  ? 0.1683 0.1491 0.1809 -0.0049 -0.0130 0.0139  82  VAL   B CB  
5031 C CG1 . VAL   B 82  ? 0.1826 0.1722 0.1910 0.0055  -0.0124 0.0280  82  VAL   B CG1 
5032 C CG2 . VAL   B 82  ? 0.1774 0.1640 0.1926 -0.0090 -0.0262 0.0099  82  VAL   B CG2 
5042 N N   . LEU   B 83  ? 0.1550 0.1231 0.1604 -0.0133 -0.0170 -0.0081 83  LEU   B N   
5043 C CA  . LEU   B 83  ? 0.1546 0.1294 0.1513 -0.0122 -0.0188 -0.0070 83  LEU   B CA  
5044 C C   . LEU   B 83  ? 0.1522 0.1303 0.1544 -0.0151 -0.0161 -0.0043 83  LEU   B C   
5045 O O   . LEU   B 83  ? 0.1530 0.1427 0.1476 -0.0201 -0.0141 0.0057  83  LEU   B O   
5046 C CB  . LEU   B 83  ? 0.1630 0.1420 0.1534 -0.0188 -0.0268 -0.0055 83  LEU   B CB  
5047 C CG  . LEU   B 83  ? 0.1781 0.1660 0.1603 -0.0201 -0.0073 -0.0081 83  LEU   B CG  
5048 C CD1 . LEU   B 83  ? 0.1880 0.1701 0.1732 -0.0125 -0.0185 -0.0016 83  LEU   B CD1 
5049 C CD2 . LEU   B 83  ? 0.1964 0.1698 0.1754 -0.0138 -0.0114 -0.0280 83  LEU   B CD2 
5061 N N   . SER   B 84  ? 0.1600 0.1413 0.1802 -0.0279 -0.0136 -0.0015 84  SER   B N   
5062 C CA  . SER   B 84  ? 0.1578 0.1587 0.1724 -0.0325 -0.0195 0.0228  84  SER   B CA  
5063 C C   . SER   B 84  ? 0.1454 0.1739 0.1282 -0.0225 -0.0212 0.0191  84  SER   B C   
5064 O O   . SER   B 84  ? 0.1567 0.1654 0.1337 -0.0198 -0.0151 0.0060  84  SER   B O   
5065 C CB  . SER   B 84  ? 0.1798 0.1657 0.2192 -0.0277 0.0075  0.0219  84  SER   B CB  
5066 O OG  . SER   B 84  ? 0.1770 0.1831 0.2518 -0.0377 0.0091  0.0339  84  SER   B OG  
5072 N N   . GLY   B 85  ? 0.1503 0.1974 0.1461 -0.0267 -0.0240 0.0204  85  GLY   B N   
5073 C CA  . GLY   B 85  ? 0.1499 0.2005 0.1687 -0.0359 -0.0037 -0.0083 85  GLY   B CA  
5074 C C   . GLY   B 85  ? 0.1535 0.1852 0.1567 -0.0399 -0.0055 0.0039  85  GLY   B C   
5075 O O   . GLY   B 85  ? 0.1597 0.1853 0.1634 -0.0544 0.0080  -0.0044 85  GLY   B O   
5079 N N   . HIS   B 86  ? 0.1515 0.1664 0.1629 -0.0277 -0.0140 0.0167  86  HIS   B N   
5080 C CA  . HIS   B 86  ? 0.1532 0.1680 0.1667 -0.0313 -0.0179 0.0222  86  HIS   B CA  
5081 C C   . HIS   B 86  ? 0.1536 0.1818 0.1629 -0.0420 -0.0051 0.0375  86  HIS   B C   
5082 O O   . HIS   B 86  ? 0.1672 0.1921 0.1610 -0.0329 0.0051  0.0322  86  HIS   B O   
5083 C CB  . HIS   B 86  ? 0.1614 0.1679 0.1776 -0.0210 -0.0269 0.0083  86  HIS   B CB  
5084 C CG  . HIS   B 86  ? 0.1679 0.1787 0.1722 -0.0179 -0.0271 0.0161  86  HIS   B CG  
5085 N ND1 . HIS   B 86  ? 0.1781 0.1966 0.1843 -0.0267 -0.0378 0.0050  86  HIS   B ND1 
5086 C CD2 . HIS   B 86  ? 0.1624 0.1819 0.1800 -0.0094 -0.0298 0.0168  86  HIS   B CD2 
5087 C CE1 . HIS   B 86  ? 0.1864 0.1944 0.1799 -0.0181 -0.0117 -0.0232 86  HIS   B CE1 
5088 N NE2 . HIS   B 86  ? 0.1778 0.1856 0.1703 -0.0052 -0.0122 0.0049  86  HIS   B NE2 
5096 N N   . ASN   B 87  ? 0.1594 0.1833 0.1674 -0.0384 -0.0026 0.0283  87  ASN   B N   
5097 C CA  . ASN   B 87  ? 0.1635 0.2031 0.1779 -0.0328 0.0216  0.0268  87  ASN   B CA  
5098 C C   . ASN   B 87  ? 0.1708 0.1890 0.1623 -0.0329 0.0298  0.0196  87  ASN   B C   
5099 O O   . ASN   B 87  ? 0.1938 0.2024 0.1924 -0.0259 0.0485  0.0120  87  ASN   B O   
5100 C CB  . ASN   B 87  ? 0.1632 0.2408 0.2044 -0.0273 0.0171  0.0149  87  ASN   B CB  
5101 C CG  . ASN   B 87  ? 0.1684 0.2592 0.2019 0.0085  0.0257  0.0345  87  ASN   B CG  
5102 O OD1 . ASN   B 87  ? 0.1673 0.2474 0.1956 0.0053  0.0452  0.0480  87  ASN   B OD1 
5103 N ND2 . ASN   B 87  ? 0.2043 0.2719 0.2352 0.0160  0.0317  0.0302  87  ASN   B ND2 
5110 N N   . LEU   B 88  ? 0.1557 0.1788 0.1531 -0.0321 0.0147  0.0124  88  LEU   B N   
5111 C CA  . LEU   B 88  ? 0.1691 0.1756 0.1534 -0.0263 0.0081  -0.0014 88  LEU   B CA  
5112 C C   . LEU   B 88  ? 0.1718 0.1665 0.1444 -0.0295 -0.0025 0.0001  88  LEU   B C   
5113 O O   . LEU   B 88  ? 0.1998 0.1731 0.1791 -0.0183 -0.0267 -0.0059 88  LEU   B O   
5114 C CB  . LEU   B 88  ? 0.1769 0.1813 0.1713 -0.0311 -0.0029 0.0211  88  LEU   B CB  
5115 C CG  . LEU   B 88  ? 0.2140 0.2047 0.1940 -0.0283 -0.0246 0.0347  88  LEU   B CG  
5116 C CD1 . LEU   B 88  ? 0.2317 0.2379 0.2050 -0.0415 -0.0140 0.0540  88  LEU   B CD1 
5117 C CD2 . LEU   B 88  ? 0.2503 0.2263 0.2538 0.0165  -0.0529 0.0124  88  LEU   B CD2 
5129 N N   . ALA   B 89  ? 0.1638 0.1561 0.1405 -0.0328 0.0200  0.0040  89  ALA   B N   
5130 C CA  . ALA   B 89  ? 0.1629 0.1524 0.1276 -0.0342 0.0069  0.0056  89  ALA   B CA  
5131 C C   . ALA   B 89  ? 0.1708 0.1591 0.1319 -0.0357 0.0097  0.0079  89  ALA   B C   
5132 O O   . ALA   B 89  ? 0.1534 0.1699 0.1752 -0.0400 0.0109  -0.0253 89  ALA   B O   
5133 C CB  . ALA   B 89  ? 0.1615 0.1483 0.1570 -0.0336 0.0076  0.0131  89  ALA   B CB  
5139 N N   . LYS   B 90  ? 0.2028 0.1490 0.1437 -0.0425 -0.0097 0.0120  90  LYS   B N   
5140 C CA  . LYS   B 90  ? 0.2170 0.1419 0.1361 -0.0416 -0.0104 0.0088  90  LYS   B CA  
5141 C C   . LYS   B 90  ? 0.1985 0.1397 0.1553 -0.0433 -0.0112 0.0058  90  LYS   B C   
5142 O O   . LYS   B 90  ? 0.2100 0.1568 0.1783 -0.0585 -0.0097 0.0042  90  LYS   B O   
5143 C CB  . LYS   B 90  ? 0.2407 0.1488 0.1841 -0.0294 -0.0075 0.0198  90  LYS   B CB  
5144 C CG  . LYS   B 90  ? 0.2466 0.1639 0.1841 -0.0142 0.0247  0.0155  90  LYS   B CG  
5145 C CD  . LYS   B 90  ? 0.2814 0.1919 0.2432 -0.0113 0.0442  -0.0088 90  LYS   B CD  
5146 C CE  . LYS   B 90  ? 0.2944 0.2092 0.3022 -0.0238 0.0551  -0.0208 90  LYS   B CE  
5147 N NZ  . LYS   B 90  ? 0.3044 0.2019 0.3005 -0.0414 0.0741  -0.0243 90  LYS   B NZ  
5161 N N   . HIS   B 91  ? 0.1684 0.1299 0.1373 -0.0306 -0.0131 0.0080  91  HIS   B N   
5162 C CA  . HIS   B 91  ? 0.1580 0.1362 0.1533 -0.0199 -0.0124 0.0031  91  HIS   B CA  
5163 C C   . HIS   B 91  ? 0.1511 0.1333 0.1290 -0.0254 -0.0083 0.0095  91  HIS   B C   
5164 O O   . HIS   B 91  ? 0.1676 0.1397 0.1286 -0.0275 -0.0210 -0.0001 91  HIS   B O   
5165 C CB  . HIS   B 91  ? 0.1800 0.1357 0.1941 -0.0085 -0.0120 0.0148  91  HIS   B CB  
5166 C CG  . HIS   B 91  ? 0.2229 0.1539 0.2639 0.0031  0.0258  0.0221  91  HIS   B CG  
5167 N ND1 . HIS   B 91  ? 0.2536 0.1596 0.3242 0.0078  0.0299  0.0138  91  HIS   B ND1 
5168 C CD2 . HIS   B 91  ? 0.2347 0.1823 0.3137 0.0142  0.0157  0.0561  91  HIS   B CD2 
5169 C CE1 . HIS   B 91  ? 0.2567 0.1789 0.3411 0.0269  0.0311  0.0189  91  HIS   B CE1 
5170 N NE2 . HIS   B 91  ? 0.2449 0.1893 0.3443 0.0318  0.0317  0.0602  91  HIS   B NE2 
5178 N N   . CYS   B 92  ? 0.1490 0.1274 0.1391 -0.0239 -0.0161 0.0024  92  CYS   B N   
5179 C CA  . CYS   B 92  ? 0.1438 0.1249 0.1321 -0.0179 -0.0137 0.0014  92  CYS   B CA  
5180 C C   . CYS   B 92  ? 0.1372 0.1204 0.1306 -0.0140 0.0003  0.0029  92  CYS   B C   
5181 O O   . CYS   B 92  ? 0.1475 0.1289 0.1498 -0.0138 -0.0031 -0.0049 92  CYS   B O   
5182 C CB  . CYS   B 92  ? 0.1464 0.1406 0.1436 -0.0130 -0.0031 0.0040  92  CYS   B CB  
5183 S SG  . CYS   B 92  ? 0.1437 0.1389 0.1532 -0.0114 -0.0115 0.0040  92  CYS   B SG  
5189 N N   . LEU   B 93  ? 0.1329 0.1277 0.1304 -0.0102 -0.0054 -0.0070 93  LEU   B N   
5190 C CA  . LEU   B 93  ? 0.1343 0.1279 0.1430 -0.0018 -0.0110 0.0035  93  LEU   B CA  
5191 C C   . LEU   B 93  ? 0.1278 0.1227 0.1275 0.0013  -0.0067 0.0071  93  LEU   B C   
5192 O O   . LEU   B 93  ? 0.1385 0.1226 0.1447 -0.0046 -0.0070 0.0002  93  LEU   B O   
5193 C CB  . LEU   B 93  ? 0.1368 0.1288 0.1523 0.0008  -0.0079 -0.0002 93  LEU   B CB  
5194 C CG  . LEU   B 93  ? 0.1353 0.1396 0.1657 -0.0033 -0.0025 0.0089  93  LEU   B CG  
5195 C CD1 . LEU   B 93  ? 0.1384 0.1519 0.1665 0.0049  0.0028  -0.0022 93  LEU   B CD1 
5196 C CD2 . LEU   B 93  ? 0.1339 0.1462 0.1693 -0.0062 -0.0124 0.0025  93  LEU   B CD2 
5208 N N   . HIS   B 94  ? 0.1334 0.1236 0.1253 -0.0047 -0.0083 0.0038  94  HIS   B N   
5209 C CA  . HIS   B 94  ? 0.1366 0.1202 0.1317 -0.0008 -0.0042 -0.0004 94  HIS   B CA  
5210 C C   . HIS   B 94  ? 0.1321 0.1196 0.1432 -0.0040 -0.0028 0.0041  94  HIS   B C   
5211 O O   . HIS   B 94  ? 0.1380 0.1317 0.1902 -0.0056 0.0138  -0.0123 94  HIS   B O   
5212 C CB  . HIS   B 94  ? 0.1334 0.1279 0.1405 0.0024  -0.0044 0.0031  94  HIS   B CB  
5213 C CG  . HIS   B 94  ? 0.1394 0.1270 0.1432 -0.0076 -0.0199 -0.0036 94  HIS   B CG  
5214 N ND1 . HIS   B 94  ? 0.1426 0.1343 0.1427 -0.0057 -0.0260 0.0024  94  HIS   B ND1 
5215 C CD2 . HIS   B 94  ? 0.1380 0.1308 0.1460 -0.0025 -0.0153 0.0041  94  HIS   B CD2 
5216 C CE1 . HIS   B 94  ? 0.1458 0.1345 0.1246 -0.0103 -0.0195 0.0082  94  HIS   B CE1 
5217 N NE2 . HIS   B 94  ? 0.1378 0.1413 0.1540 -0.0160 -0.0172 0.0061  94  HIS   B NE2 
5225 N N   . VAL   B 95  ? 0.1267 0.1229 0.1445 -0.0023 -0.0035 0.0000  95  VAL   B N   
5226 C CA  . VAL   B 95  ? 0.1325 0.1353 0.1432 0.0003  0.0038  0.0082  95  VAL   B CA  
5227 C C   . VAL   B 95  ? 0.1414 0.1324 0.1452 -0.0005 0.0065  0.0104  95  VAL   B C   
5228 O O   . VAL   B 95  ? 0.1438 0.1281 0.1639 0.0059  0.0048  0.0122  95  VAL   B O   
5229 C CB  . VAL   B 95  ? 0.1349 0.1342 0.1440 -0.0028 -0.0110 0.0035  95  VAL   B CB  
5230 C CG1 . VAL   B 95  ? 0.1450 0.1519 0.1609 -0.0082 -0.0040 0.0114  95  VAL   B CG1 
5231 C CG2 . VAL   B 95  ? 0.1469 0.1315 0.1460 0.0013  -0.0044 0.0040  95  VAL   B CG2 
5241 N N   . VAL   B 96  ? 0.1496 0.1415 0.1396 0.0117  0.0042  0.0134  96  VAL   B N   
5242 C CA  . VAL   B 96  ? 0.1547 0.1490 0.1418 0.0080  0.0037  0.0170  96  VAL   B CA  
5243 C C   . VAL   B 96  ? 0.1596 0.1522 0.1560 0.0130  0.0088  0.0205  96  VAL   B C   
5244 O O   . VAL   B 96  ? 0.1571 0.1546 0.1767 0.0032  0.0183  0.0078  96  VAL   B O   
5245 C CB  . VAL   B 96  ? 0.1624 0.1691 0.1407 0.0097  0.0077  0.0100  96  VAL   B CB  
5246 C CG1 . VAL   B 96  ? 0.1579 0.1851 0.1559 0.0233  0.0079  -0.0005 96  VAL   B CG1 
5247 C CG2 . VAL   B 96  ? 0.1697 0.1708 0.1564 0.0005  0.0047  0.0042  96  VAL   B CG2 
5257 N N   . GLY   B 97  ? 0.1596 0.1505 0.1427 0.0063  0.0089  0.0256  97  GLY   B N   
5258 C CA  . GLY   B 97  ? 0.1729 0.1528 0.1632 -0.0034 0.0131  0.0228  97  GLY   B CA  
5259 C C   . GLY   B 97  ? 0.1911 0.1622 0.1621 0.0020  0.0074  0.0213  97  GLY   B C   
5260 O O   . GLY   B 97  ? 0.2028 0.1698 0.1594 0.0037  0.0074  0.0084  97  GLY   B O   
5264 N N   . PRO   B 98  ? 0.1979 0.1685 0.1752 0.0040  0.0284  0.0297  98  PRO   B N   
5265 C CA  . PRO   B 98  ? 0.2097 0.1841 0.1810 0.0146  0.0364  0.0221  98  PRO   B CA  
5266 C C   . PRO   B 98  ? 0.2179 0.1856 0.1565 0.0251  0.0370  0.0398  98  PRO   B C   
5267 O O   . PRO   B 98  ? 0.2102 0.1793 0.1856 0.0221  0.0327  0.0403  98  PRO   B O   
5268 C CB  . PRO   B 98  ? 0.1977 0.1836 0.2077 0.0118  0.0478  0.0256  98  PRO   B CB  
5269 C CG  . PRO   B 98  ? 0.1902 0.1831 0.2015 0.0050  0.0395  0.0387  98  PRO   B CG  
5270 C CD  . PRO   B 98  ? 0.1795 0.1753 0.1970 0.0009  0.0340  0.0359  98  PRO   B CD  
5278 N N   . ASN   B 99  ? 0.2245 0.2005 0.1650 0.0407  0.0351  0.0214  99  ASN   B N   
5279 C CA  . ASN   B 99  ? 0.2450 0.2055 0.1639 0.0504  0.0283  0.0374  99  ASN   B CA  
5280 C C   . ASN   B 99  ? 0.2758 0.2381 0.1838 0.0463  0.0564  0.0659  99  ASN   B C   
5281 O O   . ASN   B 99  ? 0.2931 0.2465 0.2048 0.0472  0.0410  0.0696  99  ASN   B O   
5282 C CB  . ASN   B 99  ? 0.2590 0.2039 0.1782 0.0463  0.0127  0.0312  99  ASN   B CB  
5283 C CG  . ASN   B 99  ? 0.2664 0.2128 0.2045 0.0406  0.0027  0.0206  99  ASN   B CG  
5284 O OD1 . ASN   B 99  ? 0.2705 0.2143 0.2264 0.0427  -0.0000 0.0277  99  ASN   B OD1 
5285 N ND2 . ASN   B 99  ? 0.2642 0.2114 0.2152 0.0462  -0.0210 0.0293  99  ASN   B ND2 
5292 N N   A VAL   B 100 ? 0.2922 0.2475 0.2424 0.0321  0.0600  0.0909  100 VAL   B N   
5293 N N   B VAL   B 100 ? 0.2977 0.2521 0.2336 0.0389  0.0491  0.0795  100 VAL   B N   
5294 C CA  A VAL   B 100 ? 0.3223 0.2680 0.3015 0.0195  0.0630  0.1015  100 VAL   B CA  
5295 C CA  B VAL   B 100 ? 0.3250 0.2697 0.2801 0.0310  0.0431  0.0871  100 VAL   B CA  
5296 C C   A VAL   B 100 ? 0.3443 0.2716 0.2831 0.0272  0.0663  0.1182  100 VAL   B C   
5297 C C   B VAL   B 100 ? 0.3443 0.2739 0.2805 0.0344  0.0461  0.1075  100 VAL   B C   
5298 O O   A VAL   B 100 ? 0.3527 0.2842 0.2821 0.0248  0.0791  0.1119  100 VAL   B O   
5299 O O   B VAL   B 100 ? 0.3486 0.2810 0.2805 0.0322  0.0482  0.1037  100 VAL   B O   
5300 C CB  A VAL   B 100 ? 0.3347 0.2870 0.3759 -0.0030 0.0587  0.1056  100 VAL   B CB  
5301 C CB  B VAL   B 100 ? 0.3336 0.2827 0.3232 0.0185  0.0353  0.0805  100 VAL   B CB  
5302 C CG1 A VAL   B 100 ? 0.3410 0.2925 0.4032 -0.0057 0.0586  0.1055  100 VAL   B CG1 
5303 C CG1 B VAL   B 100 ? 0.3373 0.2865 0.3381 0.0163  0.0339  0.0786  100 VAL   B CG1 
5304 C CG2 A VAL   B 100 ? 0.3379 0.2939 0.3987 -0.0109 0.0605  0.1139  100 VAL   B CG2 
5305 C CG2 B VAL   B 100 ? 0.3360 0.2875 0.3377 0.0143  0.0335  0.0805  100 VAL   B CG2 
5324 N N   . ASN   B 101 ? 0.3579 0.2734 0.2812 0.0419  0.0462  0.1250  101 ASN   B N   
5325 C CA  . ASN   B 101 ? 0.3957 0.2954 0.2992 0.0563  0.0203  0.1290  101 ASN   B CA  
5326 C C   . ASN   B 101 ? 0.4389 0.3352 0.2913 0.0592  -0.0011 0.1449  101 ASN   B C   
5327 O O   . ASN   B 101 ? 0.4453 0.3532 0.3209 0.0673  -0.0013 0.1144  101 ASN   B O   
5328 C CB  . ASN   B 101 ? 0.3928 0.2816 0.3219 0.0572  0.0231  0.1036  101 ASN   B CB  
5329 C CG  . ASN   B 101 ? 0.3896 0.2681 0.3189 0.0579  0.0199  0.1049  101 ASN   B CG  
5330 O OD1 . ASN   B 101 ? 0.3949 0.2710 0.3564 0.0531  0.0381  0.0922  101 ASN   B OD1 
5331 N ND2 . ASN   B 101 ? 0.3813 0.2591 0.3054 0.0581  0.0129  0.0964  101 ASN   B ND2 
5339 N N   . LYS   B 102 ? 0.4722 0.3680 0.3097 0.0438  0.0051  0.1397  102 LYS   B N   
5340 C CA  . LYS   B 102 ? 0.5037 0.4097 0.3371 0.0287  0.0121  0.1184  102 LYS   B CA  
5341 C C   . LYS   B 102 ? 0.5012 0.4109 0.3211 0.0300  0.0239  0.1261  102 LYS   B C   
5342 O O   . LYS   B 102 ? 0.5123 0.4180 0.3450 0.0310  0.0089  0.1151  102 LYS   B O   
5343 C CB  . LYS   B 102 ? 0.5331 0.4467 0.3921 0.0143  0.0234  0.0780  102 LYS   B CB  
5344 C CG  . LYS   B 102 ? 0.5584 0.4777 0.4596 0.0038  0.0363  0.0361  102 LYS   B CG  
5345 C CD  . LYS   B 102 ? 0.5788 0.5027 0.5266 -0.0045 0.0493  0.0039  102 LYS   B CD  
5346 C CE  . LYS   B 102 ? 0.5921 0.5206 0.5819 -0.0116 0.0596  -0.0182 102 LYS   B CE  
5347 N NZ  . LYS   B 102 ? 0.5992 0.5321 0.6159 -0.0145 0.0641  -0.0310 102 LYS   B NZ  
5361 N N   . GLY   B 103 ? 0.4838 0.4018 0.3135 0.0287  0.0508  0.1261  103 GLY   B N   
5362 C CA  . GLY   B 103 ? 0.4639 0.3930 0.3247 0.0289  0.0727  0.1059  103 GLY   B CA  
5363 C C   . GLY   B 103 ? 0.4401 0.3792 0.3238 0.0256  0.0877  0.0829  103 GLY   B C   
5364 O O   . GLY   B 103 ? 0.4471 0.3886 0.3291 0.0221  0.0920  0.0801  103 GLY   B O   
5368 N N   A GLU   B 104 ? 0.4221 0.3613 0.3020 0.0285  0.1072  0.0720  104 GLU   B N   
5369 N N   B GLU   B 104 ? 0.4230 0.3689 0.3249 0.0221  0.0744  0.0655  104 GLU   B N   
5370 C CA  A GLU   B 104 ? 0.4037 0.3455 0.2723 0.0356  0.1169  0.0591  104 GLU   B CA  
5371 C CA  B GLU   B 104 ? 0.4049 0.3582 0.3169 0.0196  0.0597  0.0455  104 GLU   B CA  
5372 C C   A GLU   B 104 ? 0.4108 0.3523 0.2904 0.0203  0.1433  0.0589  104 GLU   B C   
5373 C C   B GLU   B 104 ? 0.3977 0.3561 0.3253 0.0136  0.0656  0.0382  104 GLU   B C   
5374 O O   A GLU   B 104 ? 0.4156 0.3565 0.3245 0.0177  0.1391  0.0539  104 GLU   B O   
5375 O O   B GLU   B 104 ? 0.3990 0.3571 0.3360 0.0132  0.0649  0.0352  104 GLU   B O   
5376 C CB  A GLU   B 104 ? 0.3856 0.3230 0.2559 0.0559  0.0798  0.0329  104 GLU   B CB  
5377 C CB  B GLU   B 104 ? 0.3961 0.3491 0.3041 0.0215  0.0378  0.0291  104 GLU   B CB  
5378 C CG  A GLU   B 104 ? 0.3707 0.3069 0.2352 0.0728  0.0341  -0.0038 104 GLU   B CG  
5379 C CG  B GLU   B 104 ? 0.3887 0.3417 0.2908 0.0222  0.0150  0.0097  104 GLU   B CG  
5380 C CD  A GLU   B 104 ? 0.3570 0.2900 0.2060 0.0850  -0.0076 -0.0140 104 GLU   B CD  
5381 C CD  B GLU   B 104 ? 0.3829 0.3345 0.2786 0.0209  -0.0038 -0.0024 104 GLU   B CD  
5382 O OE1 A GLU   B 104 ? 0.3368 0.2706 0.1791 0.0952  -0.0038 -0.0086 104 GLU   B OE1 
5383 O OE1 B GLU   B 104 ? 0.3780 0.3289 0.2692 0.0183  -0.0043 -0.0033 104 GLU   B OE1 
5384 O OE2 A GLU   B 104 ? 0.3638 0.3002 0.2079 0.0782  -0.0393 -0.0281 104 GLU   B OE2 
5385 O OE2 B GLU   B 104 ? 0.3837 0.3357 0.2803 0.0207  -0.0165 -0.0111 104 GLU   B OE2 
5398 N N   A ASP   B 105 ? 0.4083 0.3551 0.2846 0.0076  0.1673  0.0679  105 ASP   B N   
5399 N N   B ASP   B 105 ? 0.3880 0.3528 0.3214 0.0078  0.0719  0.0363  105 ASP   B N   
5400 C CA  A ASP   B 105 ? 0.4090 0.3584 0.3048 -0.0023 0.1900  0.0528  105 ASP   B CA  
5401 C CA  B ASP   B 105 ? 0.3799 0.3493 0.3276 0.0021  0.0775  0.0285  105 ASP   B CA  
5402 C C   A ASP   B 105 ? 0.3856 0.3262 0.2843 -0.0132 0.1857  0.0457  105 ASP   B C   
5403 C C   B ASP   B 105 ? 0.3705 0.3385 0.3118 -0.0022 0.0768  0.0194  105 ASP   B C   
5404 O O   A ASP   B 105 ? 0.3667 0.3202 0.2717 -0.0091 0.1770  0.0475  105 ASP   B O   
5405 O O   B ASP   B 105 ? 0.3682 0.3364 0.3031 -0.0009 0.0797  0.0196  105 ASP   B O   
5406 C CB  A ASP   B 105 ? 0.4276 0.3888 0.3851 0.0066  0.1923  0.0275  105 ASP   B CB  
5407 C CB  B ASP   B 105 ? 0.3796 0.3548 0.3529 0.0033  0.0817  0.0267  105 ASP   B CB  
5408 C CG  A ASP   B 105 ? 0.4407 0.4101 0.4594 0.0098  0.1977  0.0090  105 ASP   B CG  
5409 C CG  B ASP   B 105 ? 0.3784 0.3570 0.3783 0.0022  0.0870  0.0271  105 ASP   B CG  
5410 O OD1 A ASP   B 105 ? 0.4390 0.4165 0.4627 0.0034  0.2171  0.0120  105 ASP   B OD1 
5411 O OD1 B ASP   B 105 ? 0.3760 0.3588 0.3806 -0.0013 0.0923  0.0272  105 ASP   B OD1 
5412 O OD2 A ASP   B 105 ? 0.4487 0.4202 0.5069 0.0163  0.1846  -0.0046 105 ASP   B OD2 
5413 O OD2 B ASP   B 105 ? 0.3768 0.3570 0.3869 0.0014  0.0904  0.0312  105 ASP   B OD2 
5422 N N   A ILE   B 106 ? 0.3797 0.2971 0.3057 -0.0222 0.1738  0.0425  106 ILE   B N   
5423 N N   B ILE   B 106 ? 0.3628 0.3290 0.3082 -0.0051 0.0701  0.0132  106 ILE   B N   
5424 C CA  A ILE   B 106 ? 0.3611 0.2664 0.3177 -0.0375 0.1773  0.0356  106 ILE   B CA  
5425 C CA  B ILE   B 106 ? 0.3525 0.3204 0.3098 -0.0087 0.0690  0.0070  106 ILE   B CA  
5426 C C   A ILE   B 106 ? 0.3271 0.2583 0.3095 -0.0320 0.1738  0.0117  106 ILE   B C   
5427 C C   B ILE   B 106 ? 0.3365 0.3171 0.3070 -0.0064 0.0675  -0.0011 106 ILE   B C   
5428 O O   A ILE   B 106 ? 0.3163 0.2310 0.3066 -0.0371 0.1669  -0.0025 106 ILE   B O   
5429 O O   B ILE   B 106 ? 0.3331 0.3117 0.3024 -0.0097 0.0616  -0.0061 106 ILE   B O   
5430 C CB  A ILE   B 106 ? 0.3841 0.2576 0.3461 -0.0504 0.1644  0.0388  106 ILE   B CB  
5431 C CB  B ILE   B 106 ? 0.3595 0.3189 0.3171 -0.0143 0.0669  0.0077  106 ILE   B CB  
5432 C CG1 A ILE   B 106 ? 0.3942 0.2579 0.3575 -0.0415 0.1538  0.0291  106 ILE   B CG1 
5433 C CG1 B ILE   B 106 ? 0.3624 0.3181 0.3215 -0.0135 0.0637  0.0068  106 ILE   B CG1 
5434 C CG2 A ILE   B 106 ? 0.3940 0.2643 0.3690 -0.0582 0.1604  0.0432  106 ILE   B CG2 
5435 C CG2 B ILE   B 106 ? 0.3626 0.3216 0.3243 -0.0168 0.0668  0.0079  106 ILE   B CG2 
5436 C CD1 A ILE   B 106 ? 0.3993 0.2607 0.3542 -0.0346 0.1536  0.0302  106 ILE   B CD1 
5437 C CD1 B ILE   B 106 ? 0.3640 0.3182 0.3235 -0.0123 0.0631  0.0076  106 ILE   B CD1 
5460 N N   A GLN   B 107 ? 0.3116 0.2819 0.3187 -0.0276 0.1647  0.0164  107 GLN   B N   
5461 N N   B GLN   B 107 ? 0.3253 0.3200 0.3174 -0.0029 0.0683  -0.0016 107 GLN   B N   
5462 C CA  A GLN   B 107 ? 0.2941 0.3017 0.3337 -0.0242 0.1496  0.0169  107 GLN   B CA  
5463 C CA  B GLN   B 107 ? 0.3130 0.3198 0.3299 0.0002  0.0686  0.0015  107 GLN   B CA  
5464 C C   A GLN   B 107 ? 0.2661 0.2808 0.3118 -0.0103 0.1110  0.0063  107 GLN   B C   
5465 C C   B GLN   B 107 ? 0.2818 0.2937 0.3022 0.0051  0.0744  -0.0002 107 GLN   B C   
5466 O O   A GLN   B 107 ? 0.2548 0.2782 0.3564 -0.0028 0.0800  -0.0081 107 GLN   B O   
5467 O O   B GLN   B 107 ? 0.2808 0.2962 0.3159 0.0065  0.0628  -0.0057 107 GLN   B O   
5468 C CB  A GLN   B 107 ? 0.3245 0.3443 0.4069 -0.0250 0.1318  0.0209  107 GLN   B CB  
5469 C CB  B GLN   B 107 ? 0.3342 0.3444 0.3800 -0.0001 0.0581  0.0035  107 GLN   B CB  
5470 C CG  A GLN   B 107 ? 0.3592 0.3841 0.4893 -0.0179 0.0915  0.0197  107 GLN   B CG  
5471 C CG  B GLN   B 107 ? 0.3536 0.3661 0.4318 0.0016  0.0431  0.0053  107 GLN   B CG  
5472 C CD  A GLN   B 107 ? 0.3839 0.4130 0.5547 -0.0157 0.0635  0.0217  107 GLN   B CD  
5473 C CD  B GLN   B 107 ? 0.3682 0.3820 0.4748 0.0019  0.0318  0.0076  107 GLN   B CD  
5474 O OE1 A GLN   B 107 ? 0.3915 0.4238 0.5795 -0.0121 0.0601  0.0185  107 GLN   B OE1 
5475 O OE1 B GLN   B 107 ? 0.3727 0.3880 0.4893 0.0028  0.0310  0.0076  107 GLN   B OE1 
5476 N NE2 A GLN   B 107 ? 0.3947 0.4224 0.5764 -0.0137 0.0513  0.0271  107 GLN   B NE2 
5477 N NE2 B GLN   B 107 ? 0.3743 0.3872 0.4905 0.0028  0.0271  0.0099  107 GLN   B NE2 
5494 N N   . LEU   B 108 ? 0.2500 0.2625 0.2744 0.0128  0.0880  0.0027  108 LEU   B N   
5495 C CA  . LEU   B 108 ? 0.2300 0.2312 0.2333 0.0286  0.0638  0.0219  108 LEU   B CA  
5496 C C   . LEU   B 108 ? 0.1959 0.1956 0.2213 0.0250  0.0394  0.0336  108 LEU   B C   
5497 O O   . LEU   B 108 ? 0.1983 0.1855 0.2081 0.0242  0.0309  0.0258  108 LEU   B O   
5498 C CB  . LEU   B 108 ? 0.2480 0.2476 0.2225 0.0234  0.0659  0.0302  108 LEU   B CB  
5499 C CG  . LEU   B 108 ? 0.2663 0.2811 0.2301 0.0215  0.0583  0.0049  108 LEU   B CG  
5500 C CD1 . LEU   B 108 ? 0.2754 0.2972 0.2186 0.0093  0.0649  0.0108  108 LEU   B CD1 
5501 C CD2 . LEU   B 108 ? 0.2855 0.2968 0.2571 0.0347  0.0427  -0.0123 108 LEU   B CD2 
5514 N N   . LEU   B 109 ? 0.1790 0.1794 0.2195 0.0174  0.0397  0.0248  109 LEU   B N   
5515 C CA  . LEU   B 109 ? 0.1615 0.1510 0.2150 0.0109  0.0400  0.0350  109 LEU   B CA  
5516 C C   . LEU   B 109 ? 0.1485 0.1362 0.2205 0.0007  0.0321  0.0167  109 LEU   B C   
5517 O O   . LEU   B 109 ? 0.1512 0.1368 0.2210 0.0055  0.0282  0.0333  109 LEU   B O   
5518 C CB  . LEU   B 109 ? 0.1747 0.1425 0.2263 0.0127  0.0214  0.0429  109 LEU   B CB  
5519 C CG  . LEU   B 109 ? 0.1719 0.1408 0.2343 0.0029  0.0223  0.0227  109 LEU   B CG  
5520 C CD1 . LEU   B 109 ? 0.1589 0.1563 0.2315 0.0174  0.0242  0.0250  109 LEU   B CD1 
5521 C CD2 . LEU   B 109 ? 0.1805 0.1491 0.2507 0.0053  0.0158  0.0157  109 LEU   B CD2 
5533 N N   . LYS   B 110 ? 0.1506 0.1406 0.2130 -0.0073 0.0278  0.0201  110 LYS   B N   
5534 C CA  . LYS   B 110 ? 0.1474 0.1372 0.2089 -0.0024 0.0217  0.0186  110 LYS   B CA  
5535 C C   . LYS   B 110 ? 0.1443 0.1394 0.2027 -0.0011 0.0271  0.0088  110 LYS   B C   
5536 O O   . LYS   B 110 ? 0.1414 0.1414 0.1941 -0.0045 0.0196  0.0069  110 LYS   B O   
5537 C CB  . LYS   B 110 ? 0.1532 0.1395 0.2270 -0.0023 0.0296  0.0144  110 LYS   B CB  
5538 C CG  . LYS   B 110 ? 0.1506 0.1366 0.2393 -0.0040 0.0129  0.0125  110 LYS   B CG  
5539 C CD  . LYS   B 110 ? 0.1617 0.1410 0.2529 -0.0086 0.0179  0.0192  110 LYS   B CD  
5540 C CE  . LYS   B 110 ? 0.1604 0.1563 0.2719 -0.0048 0.0198  0.0043  110 LYS   B CE  
5541 N NZ  . LYS   B 110 ? 0.1575 0.1639 0.2750 -0.0012 0.0020  0.0038  110 LYS   B NZ  
5555 N N   . SER   B 111 ? 0.1473 0.1395 0.2205 -0.0063 0.0244  0.0173  111 SER   B N   
5556 C CA  . SER   B 111 ? 0.1508 0.1470 0.2015 0.0048  0.0288  0.0123  111 SER   B CA  
5557 C C   . SER   B 111 ? 0.1543 0.1364 0.1993 0.0011  0.0109  0.0044  111 SER   B C   
5558 O O   . SER   B 111 ? 0.1475 0.1398 0.2053 0.0008  0.0113  0.0103  111 SER   B O   
5559 C CB  . SER   B 111 ? 0.1642 0.1687 0.2194 0.0096  0.0407  0.0208  111 SER   B CB  
5560 O OG  . SER   B 111 ? 0.1851 0.2009 0.2198 0.0065  0.0402  0.0214  111 SER   B OG  
5566 N N   . ALA   B 112 ? 0.1418 0.1394 0.2075 0.0097  0.0223  0.0220  112 ALA   B N   
5567 C CA  . ALA   B 112 ? 0.1429 0.1445 0.1878 0.0035  0.0096  0.0054  112 ALA   B CA  
5568 C C   . ALA   B 112 ? 0.1284 0.1425 0.1751 0.0010  0.0123  0.0053  112 ALA   B C   
5569 O O   . ALA   B 112 ? 0.1286 0.1415 0.1926 -0.0005 0.0081  -0.0020 112 ALA   B O   
5570 C CB  . ALA   B 112 ? 0.1432 0.1445 0.2059 0.0104  0.0088  0.0094  112 ALA   B CB  
5576 N N   . TYR   B 113 ? 0.1271 0.1285 0.1941 -0.0006 0.0139  0.0077  113 TYR   B N   
5577 C CA  . TYR   B 113 ? 0.1244 0.1276 0.1823 -0.0043 0.0116  0.0020  113 TYR   B CA  
5578 C C   . TYR   B 113 ? 0.1226 0.1270 0.1878 -0.0053 0.0135  0.0046  113 TYR   B C   
5579 O O   . TYR   B 113 ? 0.1301 0.1279 0.1766 -0.0048 0.0047  -0.0055 113 TYR   B O   
5580 C CB  . TYR   B 113 ? 0.1301 0.1180 0.1982 -0.0025 0.0205  0.0119  113 TYR   B CB  
5581 C CG  . TYR   B 113 ? 0.1368 0.1285 0.2020 -0.0036 0.0156  0.0105  113 TYR   B CG  
5582 C CD1 . TYR   B 113 ? 0.1396 0.1277 0.2162 -0.0022 0.0089  0.0155  113 TYR   B CD1 
5583 C CD2 . TYR   B 113 ? 0.1414 0.1278 0.2014 -0.0038 0.0129  0.0090  113 TYR   B CD2 
5584 C CE1 . TYR   B 113 ? 0.1405 0.1329 0.2106 0.0004  0.0134  -0.0012 113 TYR   B CE1 
5585 C CE2 . TYR   B 113 ? 0.1436 0.1266 0.2234 -0.0015 0.0107  0.0146  113 TYR   B CE2 
5586 C CZ  . TYR   B 113 ? 0.1349 0.1228 0.2247 0.0080  0.0090  0.0109  113 TYR   B CZ  
5587 O OH  . TYR   B 113 ? 0.1483 0.1219 0.2440 0.0084  0.0172  0.0102  113 TYR   B OH  
5597 N N   . GLU   B 114 ? 0.1256 0.1203 0.1930 0.0006  0.0101  0.0012  114 GLU   B N   
5598 C CA  . GLU   B 114 ? 0.1256 0.1209 0.1845 0.0039  0.0071  -0.0007 114 GLU   B CA  
5599 C C   . GLU   B 114 ? 0.1251 0.1228 0.1782 -0.0049 0.0039  0.0004  114 GLU   B C   
5600 O O   . GLU   B 114 ? 0.1300 0.1259 0.1860 0.0021  -0.0004 0.0102  114 GLU   B O   
5601 C CB  . GLU   B 114 ? 0.1260 0.1318 0.2020 -0.0020 0.0045  0.0022  114 GLU   B CB  
5602 C CG  . GLU   B 114 ? 0.1376 0.1280 0.2001 -0.0029 0.0124  0.0105  114 GLU   B CG  
5603 C CD  . GLU   B 114 ? 0.1366 0.1342 0.1981 -0.0091 0.0098  0.0022  114 GLU   B CD  
5604 O OE1 . GLU   B 114 ? 0.1303 0.1465 0.1996 -0.0088 0.0178  0.0023  114 GLU   B OE1 
5605 O OE2 . GLU   B 114 ? 0.1334 0.1534 0.2205 -0.0215 0.0079  0.0051  114 GLU   B OE2 
5612 N N   . ASN   B 115 ? 0.1278 0.1129 0.1883 -0.0059 -0.0010 0.0028  115 ASN   B N   
5613 C CA  . ASN   B 115 ? 0.1270 0.1236 0.1700 -0.0057 0.0014  0.0037  115 ASN   B CA  
5614 C C   . ASN   B 115 ? 0.1278 0.1204 0.1662 -0.0102 0.0035  0.0004  115 ASN   B C   
5615 O O   . ASN   B 115 ? 0.1414 0.1283 0.1710 -0.0111 0.0015  0.0019  115 ASN   B O   
5616 C CB  . ASN   B 115 ? 0.1384 0.1415 0.1705 -0.0067 0.0027  -0.0009 115 ASN   B CB  
5617 C CG  . ASN   B 115 ? 0.1530 0.1438 0.1720 0.0015  0.0053  0.0004  115 ASN   B CG  
5618 O OD1 . ASN   B 115 ? 0.1967 0.1554 0.1820 0.0006  0.0116  -0.0106 115 ASN   B OD1 
5619 N ND2 . ASN   B 115 ? 0.1488 0.1584 0.1716 -0.0016 0.0030  0.0042  115 ASN   B ND2 
5626 N N   . PHE   B 116 ? 0.1271 0.1265 0.1542 -0.0009 0.0024  -0.0012 116 PHE   B N   
5627 C CA  . PHE   B 116 ? 0.1370 0.1282 0.1628 -0.0050 0.0045  -0.0019 116 PHE   B CA  
5628 C C   . PHE   B 116 ? 0.1371 0.1131 0.1698 -0.0115 0.0079  0.0072  116 PHE   B C   
5629 O O   . PHE   B 116 ? 0.1317 0.1248 0.1759 -0.0030 -0.0019 0.0049  116 PHE   B O   
5630 C CB  . PHE   B 116 ? 0.1345 0.1181 0.1605 -0.0050 -0.0071 0.0011  116 PHE   B CB  
5631 C CG  . PHE   B 116 ? 0.1287 0.1205 0.1573 -0.0034 0.0008  -0.0031 116 PHE   B CG  
5632 C CD1 . PHE   B 116 ? 0.1388 0.1252 0.1917 -0.0025 -0.0074 0.0055  116 PHE   B CD1 
5633 C CD2 . PHE   B 116 ? 0.1330 0.1325 0.1572 -0.0009 -0.0006 -0.0018 116 PHE   B CD2 
5634 C CE1 . PHE   B 116 ? 0.1369 0.1265 0.1853 -0.0074 -0.0120 0.0033  116 PHE   B CE1 
5635 C CE2 . PHE   B 116 ? 0.1326 0.1318 0.1695 -0.0001 0.0022  0.0013  116 PHE   B CE2 
5636 C CZ  . PHE   B 116 ? 0.1231 0.1290 0.1836 -0.0033 -0.0099 -0.0019 116 PHE   B CZ  
5646 N N   . ASN   B 117 ? 0.1347 0.1165 0.1832 -0.0073 -0.0009 0.0052  117 ASN   B N   
5647 C CA  . ASN   B 117 ? 0.1387 0.1191 0.1788 -0.0052 -0.0085 0.0038  117 ASN   B CA  
5648 C C   . ASN   B 117 ? 0.1367 0.1220 0.1882 0.0042  -0.0020 0.0007  117 ASN   B C   
5649 O O   . ASN   B 117 ? 0.1453 0.1251 0.2222 -0.0046 -0.0269 0.0018  117 ASN   B O   
5650 C CB  . ASN   B 117 ? 0.1396 0.1271 0.1845 -0.0059 -0.0033 -0.0017 117 ASN   B CB  
5651 C CG  . ASN   B 117 ? 0.1322 0.1258 0.1945 -0.0020 -0.0050 -0.0058 117 ASN   B CG  
5652 O OD1 . ASN   B 117 ? 0.1555 0.1283 0.2021 -0.0122 0.0050  -0.0039 117 ASN   B OD1 
5653 N ND2 . ASN   B 117 ? 0.1361 0.1289 0.1959 -0.0006 -0.0029 -0.0044 117 ASN   B ND2 
5660 N N   . GLN   B 118 ? 0.1363 0.1184 0.1779 -0.0072 -0.0101 0.0005  118 GLN   B N   
5661 C CA  . GLN   B 118 ? 0.1465 0.1235 0.1939 -0.0013 -0.0085 0.0050  118 GLN   B CA  
5662 C C   . GLN   B 118 ? 0.1467 0.1250 0.2010 -0.0038 -0.0065 -0.0028 118 GLN   B C   
5663 O O   . GLN   B 118 ? 0.1632 0.1241 0.2298 -0.0083 0.0073  0.0034  118 GLN   B O   
5664 C CB  . GLN   B 118 ? 0.1504 0.1304 0.2000 0.0024  -0.0123 -0.0019 118 GLN   B CB  
5665 C CG  . GLN   B 118 ? 0.1588 0.1239 0.1987 0.0070  -0.0050 -0.0154 118 GLN   B CG  
5666 C CD  . GLN   B 118 ? 0.1658 0.1241 0.1993 -0.0007 -0.0104 -0.0164 118 GLN   B CD  
5667 O OE1 . GLN   B 118 ? 0.1715 0.1268 0.2166 0.0058  0.0131  0.0018  118 GLN   B OE1 
5668 N NE2 . GLN   B 118 ? 0.1722 0.1268 0.2056 0.0010  -0.0100 -0.0032 118 GLN   B NE2 
5677 N N   . HIS   B 119 ? 0.1460 0.1249 0.1670 -0.0075 -0.0094 0.0062  119 HIS   B N   
5678 C CA  . HIS   B 119 ? 0.1549 0.1389 0.1581 -0.0058 -0.0139 0.0096  119 HIS   B CA  
5679 C C   . HIS   B 119 ? 0.1586 0.1364 0.1638 -0.0103 -0.0277 0.0141  119 HIS   B C   
5680 O O   . HIS   B 119 ? 0.1634 0.1393 0.1793 -0.0266 -0.0155 0.0087  119 HIS   B O   
5681 C CB  . HIS   B 119 ? 0.1561 0.1512 0.1662 -0.0001 -0.0180 0.0001  119 HIS   B CB  
5682 C CG  . HIS   B 119 ? 0.1626 0.1725 0.1908 0.0099  -0.0279 -0.0148 119 HIS   B CG  
5683 N ND1 . HIS   B 119 ? 0.1758 0.1870 0.2254 0.0084  -0.0475 -0.0326 119 HIS   B ND1 
5684 C CD2 . HIS   B 119 ? 0.1812 0.1902 0.1956 0.0361  -0.0390 -0.0311 119 HIS   B CD2 
5685 C CE1 . HIS   B 119 ? 0.1939 0.2044 0.2319 0.0219  -0.0571 -0.0508 119 HIS   B CE1 
5686 N NE2 . HIS   B 119 ? 0.1986 0.2168 0.2214 0.0348  -0.0451 -0.0404 119 HIS   B NE2 
5694 N N   . GLU   B 120 ? 0.1755 0.1389 0.1717 -0.0083 -0.0365 0.0107  120 GLU   B N   
5695 C CA  . GLU   B 120 ? 0.1943 0.1544 0.1805 -0.0029 -0.0416 0.0241  120 GLU   B CA  
5696 C C   . GLU   B 120 ? 0.1762 0.1467 0.1582 -0.0129 -0.0306 0.0203  120 GLU   B C   
5697 O O   . GLU   B 120 ? 0.1757 0.1571 0.1578 -0.0109 -0.0301 0.0154  120 GLU   B O   
5698 C CB  . GLU   B 120 ? 0.2648 0.1874 0.2555 0.0236  -0.0713 0.0429  120 GLU   B CB  
5699 C CG  . GLU   B 120 ? 0.3261 0.2600 0.3597 0.0352  -0.0913 0.0644  120 GLU   B CG  
5700 C CD  . GLU   B 120 ? 0.3727 0.3332 0.4706 0.0364  -0.1001 0.0782  120 GLU   B CD  
5701 O OE1 . GLU   B 120 ? 0.3928 0.3578 0.5074 0.0305  -0.0957 0.0905  120 GLU   B OE1 
5702 O OE2 . GLU   B 120 ? 0.3963 0.3626 0.5280 0.0365  -0.0990 0.0718  120 GLU   B OE2 
5709 N N   . VAL   B 121 ? 0.1664 0.1381 0.1641 -0.0195 -0.0109 0.0143  121 VAL   B N   
5710 C CA  . VAL   B 121 ? 0.1591 0.1519 0.1473 -0.0159 -0.0133 0.0177  121 VAL   B CA  
5711 C C   . VAL   B 121 ? 0.1518 0.1473 0.1434 -0.0201 -0.0099 0.0097  121 VAL   B C   
5712 O O   . VAL   B 121 ? 0.1649 0.1437 0.1642 -0.0313 -0.0213 0.0042  121 VAL   B O   
5713 C CB  . VAL   B 121 ? 0.1849 0.1903 0.1634 -0.0020 -0.0205 0.0147  121 VAL   B CB  
5714 C CG1 . VAL   B 121 ? 0.1870 0.2025 0.1989 -0.0115 -0.0068 0.0119  121 VAL   B CG1 
5715 C CG2 . VAL   B 121 ? 0.2143 0.2186 0.1665 0.0118  -0.0169 -0.0025 121 VAL   B CG2 
5725 N N   . LEU   B 122 ? 0.1503 0.1390 0.1455 -0.0106 -0.0155 0.0063  122 LEU   B N   
5726 C CA  . LEU   B 122 ? 0.1427 0.1507 0.1379 -0.0185 -0.0122 0.0095  122 LEU   B CA  
5727 C C   . LEU   B 122 ? 0.1417 0.1383 0.1485 -0.0238 -0.0163 0.0054  122 LEU   B C   
5728 O O   . LEU   B 122 ? 0.1511 0.1343 0.1802 -0.0273 -0.0203 -0.0023 122 LEU   B O   
5729 C CB  . LEU   B 122 ? 0.1689 0.1530 0.1736 -0.0036 -0.0208 0.0081  122 LEU   B CB  
5730 C CG  . LEU   B 122 ? 0.1523 0.1649 0.1726 -0.0128 -0.0023 0.0040  122 LEU   B CG  
5731 C CD1 . LEU   B 122 ? 0.1522 0.1853 0.1865 -0.0146 -0.0199 0.0004  122 LEU   B CD1 
5732 C CD2 . LEU   B 122 ? 0.1555 0.1651 0.1533 -0.0073 0.0047  -0.0132 122 LEU   B CD2 
5744 N N   . LEU   B 123 ? 0.1429 0.1245 0.1452 -0.0230 -0.0142 0.0063  123 LEU   B N   
5745 C CA  . LEU   B 123 ? 0.1501 0.1330 0.1518 -0.0231 -0.0212 0.0041  123 LEU   B CA  
5746 C C   . LEU   B 123 ? 0.1412 0.1286 0.1383 -0.0251 -0.0212 0.0020  123 LEU   B C   
5747 O O   . LEU   B 123 ? 0.1507 0.1343 0.1384 -0.0295 -0.0150 0.0037  123 LEU   B O   
5748 C CB  . LEU   B 123 ? 0.1498 0.1336 0.1546 -0.0218 -0.0094 0.0021  123 LEU   B CB  
5749 C CG  . LEU   B 123 ? 0.1413 0.1377 0.1729 -0.0165 -0.0074 0.0058  123 LEU   B CG  
5750 C CD1 . LEU   B 123 ? 0.1504 0.1376 0.1815 -0.0160 -0.0019 -0.0146 123 LEU   B CD1 
5751 C CD2 . LEU   B 123 ? 0.1550 0.1434 0.1968 -0.0117 -0.0023 0.0227  123 LEU   B CD2 
5763 N N   . ALA   B 124 ? 0.1414 0.1238 0.1428 -0.0188 -0.0038 0.0001  124 ALA   B N   
5764 C CA  . ALA   B 124 ? 0.1304 0.1253 0.1584 -0.0149 -0.0066 -0.0007 124 ALA   B CA  
5765 C C   . ALA   B 124 ? 0.1298 0.1250 0.1532 -0.0184 -0.0024 0.0024  124 ALA   B C   
5766 O O   . ALA   B 124 ? 0.1448 0.1275 0.1606 -0.0130 -0.0079 -0.0036 124 ALA   B O   
5767 C CB  . ALA   B 124 ? 0.1386 0.1319 0.1590 -0.0057 0.0052  -0.0023 124 ALA   B CB  
5773 N N   . PRO   B 125 ? 0.1383 0.1284 0.1480 -0.0128 -0.0113 0.0142  125 PRO   B N   
5774 C CA  . PRO   B 125 ? 0.1495 0.1295 0.1568 -0.0152 -0.0119 0.0197  125 PRO   B CA  
5775 C C   . PRO   B 125 ? 0.1437 0.1232 0.1750 -0.0133 -0.0039 0.0142  125 PRO   B C   
5776 O O   . PRO   B 125 ? 0.1465 0.1207 0.2011 -0.0120 -0.0042 0.0122  125 PRO   B O   
5777 C CB  . PRO   B 125 ? 0.1504 0.1518 0.1825 -0.0189 -0.0135 0.0285  125 PRO   B CB  
5778 C CG  . PRO   B 125 ? 0.1553 0.1558 0.1682 -0.0312 -0.0222 0.0204  125 PRO   B CG  
5779 C CD  . PRO   B 125 ? 0.1494 0.1382 0.1596 -0.0292 -0.0124 0.0040  125 PRO   B CD  
5787 N N   . LEU   B 126 ? 0.1513 0.1213 0.2011 -0.0198 0.0096  0.0129  126 LEU   B N   
5788 C CA  . LEU   B 126 ? 0.1586 0.1297 0.2046 -0.0102 0.0222  0.0158  126 LEU   B CA  
5789 C C   . LEU   B 126 ? 0.1509 0.1398 0.1975 0.0011  0.0212  0.0159  126 LEU   B C   
5790 O O   . LEU   B 126 ? 0.1729 0.1647 0.2118 0.0187  -0.0053 -0.0058 126 LEU   B O   
5791 C CB  . LEU   B 126 ? 0.1797 0.1352 0.2323 -0.0149 0.0271  0.0056  126 LEU   B CB  
5792 C CG  . LEU   B 126 ? 0.1907 0.1438 0.2318 -0.0202 0.0279  -0.0093 126 LEU   B CG  
5793 C CD1 . LEU   B 126 ? 0.2046 0.1551 0.2787 -0.0186 0.0196  -0.0163 126 LEU   B CD1 
5794 C CD2 . LEU   B 126 ? 0.1878 0.1537 0.2441 -0.0225 0.0241  -0.0045 126 LEU   B CD2 
5806 N N   . LEU   B 127 ? 0.1474 0.1276 0.2015 0.0033  0.0193  0.0102  127 LEU   B N   
5807 C CA  . LEU   B 127 ? 0.1497 0.1339 0.2149 -0.0014 0.0268  0.0177  127 LEU   B CA  
5808 C C   . LEU   B 127 ? 0.1423 0.1326 0.2129 -0.0016 0.0185  0.0169  127 LEU   B C   
5809 O O   . LEU   B 127 ? 0.1429 0.1388 0.2207 -0.0121 0.0116  0.0218  127 LEU   B O   
5810 C CB  . LEU   B 127 ? 0.1626 0.1351 0.2296 -0.0040 0.0204  0.0195  127 LEU   B CB  
5811 C CG  . LEU   B 127 ? 0.1716 0.1321 0.2431 0.0001  0.0259  0.0192  127 LEU   B CG  
5812 C CD1 . LEU   B 127 ? 0.1820 0.1337 0.2386 0.0077  0.0195  0.0086  127 LEU   B CD1 
5813 C CD2 . LEU   B 127 ? 0.1737 0.1462 0.2469 -0.0088 0.0255  0.0259  127 LEU   B CD2 
5825 N N   . SER   B 128 ? 0.1418 0.1322 0.2136 0.0005  0.0031  0.0117  128 SER   B N   
5826 C CA  . SER   B 128 ? 0.1655 0.1400 0.2017 0.0100  0.0031  0.0181  128 SER   B CA  
5827 C C   . SER   B 128 ? 0.1794 0.1457 0.2232 0.0146  -0.0193 0.0118  128 SER   B C   
5828 O O   . SER   B 128 ? 0.1935 0.1473 0.2584 0.0107  -0.0154 0.0315  128 SER   B O   
5829 C CB  . SER   B 128 ? 0.1765 0.1409 0.2078 0.0091  0.0083  0.0322  128 SER   B CB  
5830 O OG  . SER   B 128 ? 0.1832 0.1566 0.2052 0.0124  0.0128  0.0336  128 SER   B OG  
5836 N N   . ALA   B 129 ? 0.1871 0.1540 0.2505 0.0321  -0.0126 -0.0012 129 ALA   B N   
5837 C CA  . ALA   B 129 ? 0.1991 0.1600 0.2634 0.0329  -0.0165 -0.0106 129 ALA   B CA  
5838 C C   . ALA   B 129 ? 0.1859 0.1535 0.2489 0.0206  0.0034  -0.0043 129 ALA   B C   
5839 O O   . ALA   B 129 ? 0.1755 0.1563 0.2364 0.0177  -0.0020 0.0071  129 ALA   B O   
5840 C CB  . ALA   B 129 ? 0.2247 0.1840 0.2999 0.0387  -0.0093 -0.0117 129 ALA   B CB  
5846 N N   . GLY   B 130 ? 0.1837 0.1508 0.2586 0.0295  0.0051  -0.0074 130 GLY   B N   
5847 C CA  . GLY   B 130 ? 0.1861 0.1579 0.2623 0.0272  0.0334  -0.0050 130 GLY   B CA  
5848 C C   . GLY   B 130 ? 0.1886 0.1627 0.2574 0.0206  0.0168  0.0100  130 GLY   B C   
5849 O O   . GLY   B 130 ? 0.2040 0.1732 0.2626 0.0163  0.0175  0.0120  130 GLY   B O   
5853 N N   . ILE   B 131 ? 0.1828 0.1768 0.2655 0.0342  0.0035  0.0138  131 ILE   B N   
5854 C CA  . ILE   B 131 ? 0.2037 0.1858 0.2630 0.0322  -0.0117 0.0201  131 ILE   B CA  
5855 C C   . ILE   B 131 ? 0.2160 0.1806 0.2263 0.0216  -0.0050 0.0272  131 ILE   B C   
5856 O O   . ILE   B 131 ? 0.2493 0.1987 0.2409 0.0255  -0.0233 0.0263  131 ILE   B O   
5857 C CB  . ILE   B 131 ? 0.2022 0.2167 0.3076 0.0312  -0.0142 0.0309  131 ILE   B CB  
5858 C CG1 . ILE   B 131 ? 0.2063 0.2376 0.3279 0.0062  -0.0077 0.0344  131 ILE   B CG1 
5859 C CG2 . ILE   B 131 ? 0.2034 0.2326 0.3293 0.0344  -0.0109 0.0227  131 ILE   B CG2 
5860 C CD1 . ILE   B 131 ? 0.2114 0.2559 0.3440 -0.0142 -0.0100 0.0385  131 ILE   B CD1 
5872 N N   . PHE   B 132 ? 0.1997 0.1614 0.2198 0.0165  0.0135  0.0274  132 PHE   B N   
5873 C CA  . PHE   B 132 ? 0.2097 0.1648 0.2220 0.0091  0.0390  0.0201  132 PHE   B CA  
5874 C C   . PHE   B 132 ? 0.2301 0.1793 0.2327 0.0107  0.0431  0.0201  132 PHE   B C   
5875 O O   . PHE   B 132 ? 0.2477 0.2032 0.2526 0.0057  0.0570  0.0282  132 PHE   B O   
5876 C CB  . PHE   B 132 ? 0.1918 0.1624 0.2086 0.0080  0.0414  0.0237  132 PHE   B CB  
5877 C CG  . PHE   B 132 ? 0.1898 0.1658 0.1956 0.0158  0.0357  0.0208  132 PHE   B CG  
5878 C CD1 . PHE   B 132 ? 0.1979 0.1694 0.2395 0.0076  0.0269  0.0220  132 PHE   B CD1 
5879 C CD2 . PHE   B 132 ? 0.1894 0.1681 0.1835 0.0207  0.0221  0.0253  132 PHE   B CD2 
5880 C CE1 . PHE   B 132 ? 0.2025 0.1720 0.2516 0.0030  0.0213  0.0229  132 PHE   B CE1 
5881 C CE2 . PHE   B 132 ? 0.1974 0.1759 0.1910 0.0170  0.0067  0.0195  132 PHE   B CE2 
5882 C CZ  . PHE   B 132 ? 0.1999 0.1766 0.2348 0.0031  0.0013  0.0261  132 PHE   B CZ  
5892 N N   . GLY   B 133 ? 0.2266 0.1700 0.2366 0.0047  0.0258  0.0491  133 GLY   B N   
5893 C CA  . GLY   B 133 ? 0.2343 0.1838 0.2532 -0.0145 0.0195  0.0488  133 GLY   B CA  
5894 C C   . GLY   B 133 ? 0.2379 0.1905 0.2470 -0.0303 0.0260  0.0456  133 GLY   B C   
5895 O O   . GLY   B 133 ? 0.2558 0.2035 0.2856 -0.0395 0.0284  0.0517  133 GLY   B O   
5899 N N   . ALA   B 134 ? 0.2214 0.1906 0.2360 -0.0299 0.0264  0.0307  134 ALA   B N   
5900 C CA  . ALA   B 134 ? 0.2161 0.1841 0.2481 -0.0189 0.0346  0.0159  134 ALA   B CA  
5901 C C   . ALA   B 134 ? 0.2220 0.1785 0.2491 -0.0134 0.0342  0.0355  134 ALA   B C   
5902 O O   . ALA   B 134 ? 0.2278 0.1992 0.2646 0.0008  0.0259  0.0232  134 ALA   B O   
5903 C CB  . ALA   B 134 ? 0.2116 0.1760 0.2691 -0.0082 0.0351  0.0066  134 ALA   B CB  
5909 N N   . ASP   B 135 ? 0.2370 0.1733 0.2456 -0.0149 0.0171  0.0414  135 ASP   B N   
5910 C CA  . ASP   B 135 ? 0.2525 0.1677 0.2661 -0.0124 0.0035  0.0421  135 ASP   B CA  
5911 C C   . ASP   B 135 ? 0.2343 0.1524 0.2545 -0.0033 0.0026  0.0287  135 ASP   B C   
5912 O O   . ASP   B 135 ? 0.2217 0.1518 0.2551 -0.0025 0.0031  0.0271  135 ASP   B O   
5913 C CB  . ASP   B 135 ? 0.2831 0.1794 0.2975 -0.0331 0.0036  0.0485  135 ASP   B CB  
5914 C CG  . ASP   B 135 ? 0.3095 0.1812 0.3463 -0.0576 0.0055  0.0358  135 ASP   B CG  
5915 O OD1 . ASP   B 135 ? 0.3194 0.1602 0.3405 -0.0421 -0.0079 0.0313  135 ASP   B OD1 
5916 O OD2 . ASP   B 135 ? 0.3311 0.2190 0.4000 -0.0752 0.0061  0.0144  135 ASP   B OD2 
5921 N N   . PRO   B 136 ? 0.2277 0.1571 0.2643 0.0161  -0.0120 0.0236  136 PRO   B N   
5922 C CA  . PRO   B 136 ? 0.2054 0.1438 0.2642 0.0108  -0.0130 0.0094  136 PRO   B CA  
5923 C C   . PRO   B 136 ? 0.1856 0.1397 0.2716 0.0084  -0.0099 0.0055  136 PRO   B C   
5924 O O   . PRO   B 136 ? 0.1654 0.1391 0.2597 0.0107  0.0045  0.0046  136 PRO   B O   
5925 C CB  . PRO   B 136 ? 0.2150 0.1656 0.2757 0.0236  -0.0193 -0.0043 136 PRO   B CB  
5926 C CG  . PRO   B 136 ? 0.2367 0.1741 0.2920 0.0266  -0.0059 -0.0054 136 PRO   B CG  
5927 C CD  . PRO   B 136 ? 0.2349 0.1647 0.2838 0.0358  -0.0003 0.0041  136 PRO   B CD  
5935 N N   . ILE   B 137 ? 0.1947 0.1324 0.2864 0.0134  -0.0063 0.0062  137 ILE   B N   
5936 C CA  . ILE   B 137 ? 0.1969 0.1272 0.2944 -0.0028 0.0005  0.0054  137 ILE   B CA  
5937 C C   . ILE   B 137 ? 0.1913 0.1341 0.2917 -0.0096 0.0097  0.0195  137 ILE   B C   
5938 O O   . ILE   B 137 ? 0.1804 0.1380 0.2836 -0.0119 0.0085  0.0100  137 ILE   B O   
5939 C CB  . ILE   B 137 ? 0.2177 0.1382 0.3397 -0.0035 -0.0053 0.0122  137 ILE   B CB  
5940 C CG1 . ILE   B 137 ? 0.2438 0.1562 0.3850 0.0036  -0.0029 -0.0002 137 ILE   B CG1 
5941 C CG2 . ILE   B 137 ? 0.2218 0.1408 0.3600 -0.0253 -0.0062 0.0151  137 ILE   B CG2 
5942 C CD1 . ILE   B 137 ? 0.2677 0.1854 0.4247 0.0216  -0.0074 0.0093  137 ILE   B CD1 
5954 N N   . HIS   B 138 ? 0.1982 0.1317 0.2952 -0.0032 0.0211  0.0228  138 HIS   B N   
5955 C CA  . HIS   B 138 ? 0.2092 0.1427 0.2877 -0.0054 0.0346  0.0193  138 HIS   B CA  
5956 C C   . HIS   B 138 ? 0.1942 0.1388 0.2701 -0.0117 0.0337  0.0204  138 HIS   B C   
5957 O O   . HIS   B 138 ? 0.1826 0.1442 0.2882 0.0020  0.0350  0.0330  138 HIS   B O   
5958 C CB  . HIS   B 138 ? 0.2313 0.1554 0.2992 -0.0071 0.0506  0.0112  138 HIS   B CB  
5959 C CG  . HIS   B 138 ? 0.2506 0.1733 0.3036 -0.0076 0.0757  0.0350  138 HIS   B CG  
5960 N ND1 . HIS   B 138 ? 0.2574 0.1953 0.3277 -0.0012 0.0884  0.0261  138 HIS   B ND1 
5961 C CD2 . HIS   B 138 ? 0.2661 0.1841 0.2980 -0.0091 0.0790  0.0346  138 HIS   B CD2 
5962 C CE1 . HIS   B 138 ? 0.2624 0.1990 0.3217 -0.0026 0.0922  0.0351  138 HIS   B CE1 
5963 N NE2 . HIS   B 138 ? 0.2730 0.1884 0.3067 0.0025  0.0862  0.0268  138 HIS   B NE2 
5971 N N   . SER   B 139 ? 0.1909 0.1326 0.2582 -0.0069 0.0244  0.0132  139 SER   B N   
5972 C CA  . SER   B 139 ? 0.1835 0.1260 0.2425 -0.0032 0.0242  0.0038  139 SER   B CA  
5973 C C   . SER   B 139 ? 0.1609 0.1188 0.2416 -0.0010 0.0211  0.0030  139 SER   B C   
5974 O O   . SER   B 139 ? 0.1598 0.1207 0.2374 0.0037  0.0027  0.0034  139 SER   B O   
5975 C CB  . SER   B 139 ? 0.1851 0.1257 0.2504 0.0024  0.0103  0.0011  139 SER   B CB  
5976 O OG  . SER   B 139 ? 0.1869 0.1276 0.2554 0.0002  -0.0071 0.0123  139 SER   B OG  
5982 N N   . LEU   B 140 ? 0.1551 0.1139 0.2325 -0.0039 0.0178  -0.0048 140 LEU   B N   
5983 C CA  . LEU   B 140 ? 0.1532 0.1221 0.2274 -0.0029 0.0054  0.0076  140 LEU   B CA  
5984 C C   . LEU   B 140 ? 0.1417 0.1244 0.2483 -0.0042 0.0031  -0.0023 140 LEU   B C   
5985 O O   . LEU   B 140 ? 0.1460 0.1294 0.2433 -0.0039 0.0047  0.0094  140 LEU   B O   
5986 C CB  . LEU   B 140 ? 0.1446 0.1214 0.2425 -0.0032 0.0146  -0.0047 140 LEU   B CB  
5987 C CG  . LEU   B 140 ? 0.1582 0.1263 0.2437 -0.0107 0.0064  0.0049  140 LEU   B CG  
5988 C CD1 . LEU   B 140 ? 0.1646 0.1363 0.2642 -0.0115 0.0054  0.0050  140 LEU   B CD1 
5989 C CD2 . LEU   B 140 ? 0.1773 0.1379 0.2447 -0.0098 -0.0013 -0.0045 140 LEU   B CD2 
6001 N N   . ARG   B 141 ? 0.1408 0.1241 0.2566 -0.0104 0.0062  -0.0032 141 ARG   B N   
6002 C CA  . ARG   B 141 ? 0.1463 0.1271 0.2986 -0.0130 0.0259  -0.0030 141 ARG   B CA  
6003 C C   . ARG   B 141 ? 0.1366 0.1263 0.2801 -0.0134 0.0177  -0.0016 141 ARG   B C   
6004 O O   . ARG   B 141 ? 0.1450 0.1263 0.2830 -0.0156 0.0070  -0.0179 141 ARG   B O   
6005 C CB  . ARG   B 141 ? 0.1640 0.1328 0.3252 -0.0173 0.0382  -0.0070 141 ARG   B CB  
6006 C CG  . ARG   B 141 ? 0.2003 0.1585 0.3358 -0.0169 0.0423  -0.0033 141 ARG   B CG  
6007 C CD  . ARG   B 141 ? 0.2447 0.1831 0.3403 -0.0163 0.0316  -0.0127 141 ARG   B CD  
6008 N NE  . ARG   B 141 ? 0.2725 0.1837 0.3442 -0.0390 0.0355  -0.0206 141 ARG   B NE  
6009 C CZ  . ARG   B 141 ? 0.2845 0.1681 0.3353 -0.0343 0.0509  -0.0293 141 ARG   B CZ  
6010 N NH1 . ARG   B 141 ? 0.2938 0.1565 0.3225 -0.0347 0.0447  -0.0196 141 ARG   B NH1 
6011 N NH2 . ARG   B 141 ? 0.2892 0.1774 0.3464 -0.0216 0.0453  -0.0230 141 ARG   B NH2 
6025 N N   . VAL   B 142 ? 0.1430 0.1210 0.2696 -0.0085 0.0176  -0.0083 142 VAL   B N   
6026 C CA  . VAL   B 142 ? 0.1393 0.1270 0.2612 -0.0054 0.0212  -0.0113 142 VAL   B CA  
6027 C C   . VAL   B 142 ? 0.1363 0.1237 0.2608 -0.0039 0.0174  -0.0108 142 VAL   B C   
6028 O O   . VAL   B 142 ? 0.1486 0.1196 0.2727 0.0022  0.0137  -0.0063 142 VAL   B O   
6029 C CB  . VAL   B 142 ? 0.1509 0.1340 0.2626 0.0006  0.0229  0.0077  142 VAL   B CB  
6030 C CG1 . VAL   B 142 ? 0.1482 0.1316 0.2692 0.0102  0.0217  0.0082  142 VAL   B CG1 
6031 C CG2 . VAL   B 142 ? 0.1655 0.1410 0.2603 -0.0008 0.0145  0.0091  142 VAL   B CG2 
6041 N N   . CYS   B 143 ? 0.1348 0.1268 0.2409 -0.0002 0.0072  0.0079  143 CYS   B N   
6042 C CA  . CYS   B 143 ? 0.1314 0.1241 0.2362 -0.0042 0.0089  0.0014  143 CYS   B CA  
6043 C C   . CYS   B 143 ? 0.1255 0.1263 0.2361 -0.0043 0.0073  -0.0021 143 CYS   B C   
6044 O O   . CYS   B 143 ? 0.1345 0.1276 0.2384 -0.0021 -0.0031 -0.0017 143 CYS   B O   
6045 C CB  . CYS   B 143 ? 0.1408 0.1372 0.2425 -0.0040 0.0073  -0.0094 143 CYS   B CB  
6046 S SG  . CYS   B 143 ? 0.1456 0.1457 0.2284 -0.0056 0.0084  0.0041  143 CYS   B SG  
6052 N N   . VAL   B 144 ? 0.1382 0.1247 0.2572 -0.0103 0.0049  -0.0098 144 VAL   B N   
6053 C CA  . VAL   B 144 ? 0.1422 0.1274 0.2725 -0.0128 -0.0017 -0.0196 144 VAL   B CA  
6054 C C   . VAL   B 144 ? 0.1444 0.1321 0.2839 -0.0125 -0.0065 0.0030  144 VAL   B C   
6055 O O   . VAL   B 144 ? 0.1481 0.1533 0.3040 -0.0018 -0.0117 0.0195  144 VAL   B O   
6056 C CB  . VAL   B 144 ? 0.1649 0.1553 0.3360 -0.0142 -0.0135 -0.0315 144 VAL   B CB  
6057 C CG1 . VAL   B 144 ? 0.1941 0.2051 0.3688 -0.0112 -0.0236 -0.0332 144 VAL   B CG1 
6058 C CG2 . VAL   B 144 ? 0.1785 0.1507 0.3194 -0.0023 -0.0276 -0.0430 144 VAL   B CG2 
6068 N N   . ASP   B 145 ? 0.1389 0.1301 0.2931 -0.0068 0.0002  -0.0161 145 ASP   B N   
6069 C CA  . ASP   B 145 ? 0.1418 0.1347 0.3146 -0.0072 0.0148  -0.0080 145 ASP   B CA  
6070 C C   . ASP   B 145 ? 0.1420 0.1377 0.2926 -0.0078 0.0112  -0.0073 145 ASP   B C   
6071 O O   . ASP   B 145 ? 0.1461 0.1554 0.3406 -0.0129 0.0123  -0.0239 145 ASP   B O   
6072 C CB  . ASP   B 145 ? 0.1569 0.1453 0.3552 -0.0135 0.0314  -0.0036 145 ASP   B CB  
6073 C CG  . ASP   B 145 ? 0.1774 0.1459 0.4042 -0.0218 0.0403  -0.0136 145 ASP   B CG  
6074 O OD1 . ASP   B 145 ? 0.1777 0.1489 0.4171 -0.0227 0.0028  -0.0262 145 ASP   B OD1 
6075 O OD2 . ASP   B 145 ? 0.2050 0.1551 0.4430 -0.0304 0.0639  -0.0083 145 ASP   B OD2 
6080 N N   . THR   B 146 ? 0.1331 0.1250 0.2536 -0.0140 0.0032  -0.0052 146 THR   B N   
6081 C CA  . THR   B 146 ? 0.1356 0.1360 0.2244 -0.0090 0.0052  -0.0101 146 THR   B CA  
6082 C C   . THR   B 146 ? 0.1352 0.1300 0.2235 -0.0035 0.0029  0.0033  146 THR   B C   
6083 O O   . THR   B 146 ? 0.1397 0.1334 0.2289 -0.0039 0.0031  -0.0003 146 THR   B O   
6084 C CB  . THR   B 146 ? 0.1472 0.1300 0.2363 -0.0062 0.0214  -0.0059 146 THR   B CB  
6085 O OG1 . THR   B 146 ? 0.1497 0.1287 0.2462 -0.0084 0.0252  0.0085  146 THR   B OG1 
6086 C CG2 . THR   B 146 ? 0.1610 0.1231 0.2433 -0.0059 0.0126  -0.0060 146 THR   B CG2 
6094 N N   . VAL   B 147 ? 0.1415 0.1320 0.2101 -0.0021 0.0111  0.0058  147 VAL   B N   
6095 C CA  . VAL   B 147 ? 0.1392 0.1281 0.2051 -0.0082 -0.0013 0.0039  147 VAL   B CA  
6096 C C   . VAL   B 147 ? 0.1350 0.1314 0.2097 -0.0117 -0.0094 -0.0026 147 VAL   B C   
6097 O O   . VAL   B 147 ? 0.1505 0.1420 0.2229 -0.0176 -0.0326 -0.0115 147 VAL   B O   
6098 C CB  . VAL   B 147 ? 0.1459 0.1375 0.1912 -0.0083 -0.0091 -0.0010 147 VAL   B CB  
6099 C CG1 . VAL   B 147 ? 0.1449 0.1502 0.1871 -0.0190 -0.0036 0.0029  147 VAL   B CG1 
6100 C CG2 . VAL   B 147 ? 0.1504 0.1399 0.2009 -0.0106 0.0004  0.0020  147 VAL   B CG2 
6110 N N   . ARG   B 148 ? 0.1418 0.1295 0.2055 -0.0096 -0.0169 -0.0078 148 ARG   B N   
6111 C CA  . ARG   B 148 ? 0.1465 0.1399 0.2030 -0.0058 -0.0211 -0.0103 148 ARG   B CA  
6112 C C   . ARG   B 148 ? 0.1507 0.1487 0.1917 -0.0087 -0.0194 -0.0052 148 ARG   B C   
6113 O O   . ARG   B 148 ? 0.1689 0.1755 0.1938 -0.0206 -0.0304 -0.0030 148 ARG   B O   
6114 C CB  . ARG   B 148 ? 0.1491 0.1446 0.2019 -0.0035 -0.0294 -0.0194 148 ARG   B CB  
6115 C CG  . ARG   B 148 ? 0.1487 0.1606 0.2240 -0.0120 -0.0246 -0.0340 148 ARG   B CG  
6116 C CD  . ARG   B 148 ? 0.1533 0.1801 0.2323 0.0043  -0.0218 -0.0365 148 ARG   B CD  
6117 N NE  . ARG   B 148 ? 0.1580 0.1768 0.2289 0.0200  -0.0310 -0.0305 148 ARG   B NE  
6118 C CZ  . ARG   B 148 ? 0.1517 0.1706 0.2093 0.0100  -0.0189 -0.0240 148 ARG   B CZ  
6119 N NH1 . ARG   B 148 ? 0.1433 0.1788 0.2136 0.0003  0.0022  -0.0154 148 ARG   B NH1 
6120 N NH2 . ARG   B 148 ? 0.1801 0.1583 0.1882 0.0109  -0.0169 -0.0132 148 ARG   B NH2 
6134 N N   . THR   B 149 ? 0.1493 0.1388 0.1928 -0.0091 -0.0183 -0.0050 149 THR   B N   
6135 C CA  . THR   B 149 ? 0.1556 0.1465 0.1860 -0.0132 -0.0259 0.0030  149 THR   B CA  
6136 C C   . THR   B 149 ? 0.1539 0.1419 0.1855 -0.0171 -0.0265 0.0039  149 THR   B C   
6137 O O   . THR   B 149 ? 0.1575 0.1414 0.1995 -0.0207 -0.0075 -0.0011 149 THR   B O   
6138 C CB  . THR   B 149 ? 0.1613 0.1423 0.1943 -0.0163 -0.0266 0.0054  149 THR   B CB  
6139 O OG1 . THR   B 149 ? 0.1589 0.1505 0.1881 -0.0268 -0.0328 0.0021  149 THR   B OG1 
6140 C CG2 . THR   B 149 ? 0.1731 0.1416 0.2151 -0.0115 -0.0178 -0.0030 149 THR   B CG2 
6148 N N   . ASN   B 150 ? 0.1604 0.1411 0.1892 -0.0153 -0.0346 0.0048  150 ASN   B N   
6149 C CA  . ASN   B 150 ? 0.1681 0.1562 0.1737 -0.0133 -0.0238 -0.0065 150 ASN   B CA  
6150 C C   . ASN   B 150 ? 0.1564 0.1503 0.1760 -0.0107 -0.0149 -0.0055 150 ASN   B C   
6151 O O   . ASN   B 150 ? 0.1624 0.1435 0.1958 -0.0257 -0.0331 -0.0024 150 ASN   B O   
6152 C CB  . ASN   B 150 ? 0.1888 0.1862 0.1823 -0.0171 -0.0384 0.0090  150 ASN   B CB  
6153 C CG  . ASN   B 150 ? 0.2140 0.2300 0.2309 -0.0158 -0.0439 0.0223  150 ASN   B CG  
6154 O OD1 . ASN   B 150 ? 0.2239 0.2471 0.2453 -0.0283 -0.0596 0.0219  150 ASN   B OD1 
6155 N ND2 . ASN   B 150 ? 0.2258 0.2502 0.2749 -0.0025 -0.0483 0.0635  150 ASN   B ND2 
6162 N N   . VAL   B 151 ? 0.1506 0.1467 0.1768 -0.0148 -0.0222 -0.0017 151 VAL   B N   
6163 C CA  . VAL   B 151 ? 0.1518 0.1487 0.1745 -0.0228 -0.0235 -0.0060 151 VAL   B CA  
6164 C C   . VAL   B 151 ? 0.1549 0.1406 0.1713 -0.0306 -0.0242 -0.0030 151 VAL   B C   
6165 O O   . VAL   B 151 ? 0.1616 0.1463 0.1939 -0.0245 -0.0148 -0.0113 151 VAL   B O   
6166 C CB  . VAL   B 151 ? 0.1687 0.1654 0.1918 -0.0058 -0.0152 -0.0056 151 VAL   B CB  
6167 C CG1 . VAL   B 151 ? 0.1796 0.1696 0.2194 -0.0155 -0.0089 -0.0108 151 VAL   B CG1 
6168 C CG2 . VAL   B 151 ? 0.1884 0.1806 0.1848 0.0115  -0.0140 0.0047  151 VAL   B CG2 
6178 N N   . TYR   B 152 ? 0.1474 0.1310 0.1654 -0.0227 -0.0151 -0.0102 152 TYR   B N   
6179 C CA  . TYR   B 152 ? 0.1535 0.1455 0.1536 -0.0278 -0.0166 -0.0075 152 TYR   B CA  
6180 C C   . TYR   B 152 ? 0.1479 0.1356 0.1558 -0.0218 -0.0102 -0.0068 152 TYR   B C   
6181 O O   . TYR   B 152 ? 0.1553 0.1378 0.1658 -0.0252 -0.0102 0.0012  152 TYR   B O   
6182 C CB  . TYR   B 152 ? 0.1649 0.1575 0.1683 -0.0224 -0.0125 0.0074  152 TYR   B CB  
6183 C CG  . TYR   B 152 ? 0.1787 0.1676 0.1662 -0.0307 -0.0138 0.0039  152 TYR   B CG  
6184 C CD1 . TYR   B 152 ? 0.1864 0.1776 0.1620 -0.0224 -0.0271 0.0038  152 TYR   B CD1 
6185 C CD2 . TYR   B 152 ? 0.1996 0.1829 0.1701 -0.0345 -0.0062 -0.0057 152 TYR   B CD2 
6186 C CE1 . TYR   B 152 ? 0.2064 0.1977 0.1732 -0.0224 -0.0282 0.0163  152 TYR   B CE1 
6187 C CE2 . TYR   B 152 ? 0.2082 0.2024 0.1780 -0.0346 -0.0103 -0.0137 152 TYR   B CE2 
6188 C CZ  . TYR   B 152 ? 0.2125 0.2194 0.1587 -0.0260 -0.0440 0.0111  152 TYR   B CZ  
6189 O OH  . TYR   B 152 ? 0.2352 0.2565 0.1924 -0.0137 -0.0407 0.0144  152 TYR   B OH  
6199 N N   . LEU   B 153 ? 0.1543 0.1304 0.1663 -0.0329 -0.0103 -0.0053 153 LEU   B N   
6200 C CA  . LEU   B 153 ? 0.1579 0.1277 0.1577 -0.0233 -0.0067 -0.0067 153 LEU   B CA  
6201 C C   . LEU   B 153 ? 0.1613 0.1321 0.1650 -0.0253 -0.0077 -0.0188 153 LEU   B C   
6202 O O   . LEU   B 153 ? 0.1687 0.1498 0.1830 -0.0143 -0.0111 -0.0349 153 LEU   B O   
6203 C CB  . LEU   B 153 ? 0.1563 0.1272 0.1673 -0.0220 -0.0055 -0.0072 153 LEU   B CB  
6204 C CG  . LEU   B 153 ? 0.1595 0.1428 0.1987 -0.0202 -0.0048 -0.0076 153 LEU   B CG  
6205 C CD1 . LEU   B 153 ? 0.1603 0.1593 0.2054 -0.0279 0.0026  -0.0003 153 LEU   B CD1 
6206 C CD2 . LEU   B 153 ? 0.1526 0.1580 0.1993 -0.0226 0.0126  0.0055  153 LEU   B CD2 
6218 N N   . ALA   B 154 ? 0.1546 0.1305 0.1768 -0.0057 -0.0189 -0.0145 154 ALA   B N   
6219 C CA  . ALA   B 154 ? 0.1682 0.1420 0.2002 0.0033  -0.0174 -0.0229 154 ALA   B CA  
6220 C C   . ALA   B 154 ? 0.1840 0.1455 0.2057 0.0110  -0.0303 -0.0313 154 ALA   B C   
6221 O O   . ALA   B 154 ? 0.2158 0.1479 0.2266 0.0055  -0.0164 -0.0154 154 ALA   B O   
6222 C CB  . ALA   B 154 ? 0.1635 0.1608 0.2305 0.0013  -0.0171 -0.0316 154 ALA   B CB  
6228 N N   . VAL   B 155 ? 0.1502 0.1378 0.2163 0.0002  -0.0011 -0.0197 155 VAL   B N   
6229 C CA  . VAL   B 155 ? 0.1412 0.1380 0.2340 0.0018  -0.0087 -0.0087 155 VAL   B CA  
6230 C C   . VAL   B 155 ? 0.1418 0.1397 0.2283 -0.0050 -0.0104 -0.0185 155 VAL   B C   
6231 O O   . VAL   B 155 ? 0.1605 0.1525 0.2637 0.0039  -0.0124 -0.0417 155 VAL   B O   
6232 C CB  . VAL   B 155 ? 0.1469 0.1509 0.2743 0.0007  -0.0207 0.0042  155 VAL   B CB  
6233 C CG1 . VAL   B 155 ? 0.1556 0.1514 0.2641 -0.0047 -0.0167 -0.0078 155 VAL   B CG1 
6234 C CG2 . VAL   B 155 ? 0.1463 0.1622 0.2975 -0.0047 -0.0119 0.0323  155 VAL   B CG2 
6244 N N   . PHE   B 156 ? 0.1307 0.1484 0.2479 0.0067  -0.0063 -0.0134 156 PHE   B N   
6245 C CA  . PHE   B 156 ? 0.1376 0.1522 0.2806 0.0060  -0.0100 -0.0154 156 PHE   B CA  
6246 C C   . PHE   B 156 ? 0.1307 0.1652 0.3059 0.0135  -0.0154 -0.0410 156 PHE   B C   
6247 O O   . PHE   B 156 ? 0.1562 0.1842 0.3397 0.0262  -0.0021 -0.0466 156 PHE   B O   
6248 C CB  . PHE   B 156 ? 0.1448 0.1510 0.2803 0.0034  -0.0093 -0.0158 156 PHE   B CB  
6249 C CG  . PHE   B 156 ? 0.1449 0.1595 0.2939 -0.0021 -0.0122 0.0026  156 PHE   B CG  
6250 C CD1 . PHE   B 156 ? 0.1475 0.1840 0.3229 0.0023  -0.0038 0.0423  156 PHE   B CD1 
6251 C CD2 . PHE   B 156 ? 0.1519 0.1717 0.2966 0.0103  -0.0231 0.0061  156 PHE   B CD2 
6252 C CE1 . PHE   B 156 ? 0.1512 0.1995 0.3366 -0.0002 -0.0078 0.0430  156 PHE   B CE1 
6253 C CE2 . PHE   B 156 ? 0.1579 0.1918 0.3183 0.0135  -0.0182 0.0087  156 PHE   B CE2 
6254 C CZ  . PHE   B 156 ? 0.1468 0.2025 0.3363 0.0159  -0.0237 0.0231  156 PHE   B CZ  
6264 N N   . ASP   B 157 ? 0.1381 0.1544 0.3279 0.0171  -0.0216 -0.0232 157 ASP   B N   
6265 C CA  . ASP   B 157 ? 0.1497 0.1645 0.3672 0.0126  -0.0233 -0.0254 157 ASP   B CA  
6266 C C   . ASP   B 157 ? 0.1533 0.1569 0.3763 0.0065  -0.0259 -0.0459 157 ASP   B C   
6267 O O   . ASP   B 157 ? 0.1453 0.1548 0.3553 0.0054  -0.0261 -0.0326 157 ASP   B O   
6268 C CB  . ASP   B 157 ? 0.1773 0.1770 0.3816 0.0034  -0.0439 -0.0133 157 ASP   B CB  
6269 C CG  . ASP   B 157 ? 0.2163 0.1863 0.4127 0.0006  -0.0303 -0.0097 157 ASP   B CG  
6270 O OD1 . ASP   B 157 ? 0.2283 0.1769 0.4296 0.0136  -0.0261 -0.0037 157 ASP   B OD1 
6271 O OD2 . ASP   B 157 ? 0.2460 0.2098 0.4353 -0.0021 -0.0173 -0.0082 157 ASP   B OD2 
6276 N N   . LYS   B 158 ? 0.1607 0.1828 0.3862 0.0070  -0.0095 -0.0670 158 LYS   B N   
6277 C CA  . LYS   B 158 ? 0.1734 0.1946 0.3936 0.0073  0.0000  -0.0832 158 LYS   B CA  
6278 C C   . LYS   B 158 ? 0.1731 0.1794 0.3986 0.0103  -0.0065 -0.0814 158 LYS   B C   
6279 O O   . LYS   B 158 ? 0.1700 0.1787 0.3923 -0.0029 -0.0052 -0.0822 158 LYS   B O   
6280 C CB  . LYS   B 158 ? 0.1955 0.2348 0.3964 0.0047  0.0070  -0.1039 158 LYS   B CB  
6281 C CG  . LYS   B 158 ? 0.2245 0.2713 0.3972 0.0100  0.0171  -0.1168 158 LYS   B CG  
6282 C CD  . LYS   B 158 ? 0.2482 0.3134 0.4082 0.0081  0.0295  -0.1033 158 LYS   B CD  
6283 C CE  . LYS   B 158 ? 0.2682 0.3433 0.4230 0.0108  0.0280  -0.0973 158 LYS   B CE  
6284 N NZ  . LYS   B 158 ? 0.2653 0.3571 0.4199 0.0078  0.0222  -0.0959 158 LYS   B NZ  
6298 N N   . ASN   B 159 ? 0.1760 0.1704 0.4184 0.0060  -0.0175 -0.0712 159 ASN   B N   
6299 C CA  . ASN   B 159 ? 0.1874 0.1642 0.4325 0.0200  -0.0341 -0.0547 159 ASN   B CA  
6300 C C   . ASN   B 159 ? 0.1695 0.1526 0.4170 0.0170  -0.0481 -0.0445 159 ASN   B C   
6301 O O   . ASN   B 159 ? 0.1734 0.1477 0.4350 0.0037  -0.0569 -0.0313 159 ASN   B O   
6302 C CB  . ASN   B 159 ? 0.2092 0.1766 0.4656 0.0301  -0.0369 -0.0447 159 ASN   B CB  
6303 C CG  . ASN   B 159 ? 0.2369 0.1993 0.4988 0.0341  -0.0475 -0.0546 159 ASN   B CG  
6304 O OD1 . ASN   B 159 ? 0.2508 0.2067 0.5018 0.0403  -0.0439 -0.0689 159 ASN   B OD1 
6305 N ND2 . ASN   B 159 ? 0.2415 0.2110 0.5207 0.0329  -0.0523 -0.0497 159 ASN   B ND2 
6312 N N   . LEU   B 160 ? 0.1641 0.1541 0.3873 0.0127  -0.0377 -0.0388 160 LEU   B N   
6313 C CA  . LEU   B 160 ? 0.1650 0.1567 0.3462 0.0122  -0.0339 -0.0238 160 LEU   B CA  
6314 C C   . LEU   B 160 ? 0.1598 0.1481 0.3272 0.0053  -0.0198 -0.0313 160 LEU   B C   
6315 O O   . LEU   B 160 ? 0.1505 0.1468 0.3118 0.0001  -0.0230 -0.0270 160 LEU   B O   
6316 C CB  . LEU   B 160 ? 0.1615 0.1668 0.3238 0.0066  -0.0387 -0.0110 160 LEU   B CB  
6317 C CG  . LEU   B 160 ? 0.1585 0.1844 0.2950 0.0167  -0.0336 -0.0073 160 LEU   B CG  
6318 C CD1 . LEU   B 160 ? 0.1762 0.2071 0.2894 0.0039  -0.0207 -0.0138 160 LEU   B CD1 
6319 C CD2 . LEU   B 160 ? 0.1673 0.1866 0.2905 0.0324  -0.0260 -0.0150 160 LEU   B CD2 
6331 N N   . TYR   B 161 ? 0.1488 0.1564 0.3276 -0.0024 -0.0043 -0.0479 161 TYR   B N   
6332 C CA  . TYR   B 161 ? 0.1553 0.1533 0.3227 -0.0116 0.0115  -0.0470 161 TYR   B CA  
6333 C C   . TYR   B 161 ? 0.1645 0.1523 0.3140 -0.0071 0.0153  -0.0403 161 TYR   B C   
6334 O O   . TYR   B 161 ? 0.1736 0.1504 0.3058 -0.0150 -0.0006 -0.0318 161 TYR   B O   
6335 C CB  . TYR   B 161 ? 0.1682 0.1658 0.3245 -0.0192 0.0300  -0.0512 161 TYR   B CB  
6336 C CG  . TYR   B 161 ? 0.1936 0.1678 0.3217 -0.0228 0.0400  -0.0612 161 TYR   B CG  
6337 C CD1 . TYR   B 161 ? 0.1985 0.1608 0.3206 -0.0369 0.0415  -0.0571 161 TYR   B CD1 
6338 C CD2 . TYR   B 161 ? 0.2164 0.1742 0.3167 -0.0217 0.0317  -0.0661 161 TYR   B CD2 
6339 C CE1 . TYR   B 161 ? 0.2165 0.1810 0.3163 -0.0407 0.0360  -0.0580 161 TYR   B CE1 
6340 C CE2 . TYR   B 161 ? 0.2358 0.1908 0.3177 -0.0252 0.0365  -0.0602 161 TYR   B CE2 
6341 C CZ  . TYR   B 161 ? 0.2334 0.1951 0.3097 -0.0403 0.0284  -0.0469 161 TYR   B CZ  
6342 O OH  . TYR   B 161 ? 0.2650 0.2185 0.3359 -0.0378 0.0255  -0.0355 161 TYR   B OH  
6352 N N   . ASP   B 162 ? 0.1690 0.1507 0.3260 -0.0050 -0.0039 -0.0491 162 ASP   B N   
6353 C CA  . ASP   B 162 ? 0.1779 0.1585 0.3329 -0.0061 -0.0057 -0.0499 162 ASP   B CA  
6354 C C   . ASP   B 162 ? 0.1743 0.1454 0.3219 -0.0112 -0.0099 -0.0406 162 ASP   B C   
6355 O O   . ASP   B 162 ? 0.1746 0.1520 0.3237 -0.0110 -0.0252 -0.0303 162 ASP   B O   
6356 C CB  . ASP   B 162 ? 0.1919 0.1712 0.3593 0.0019  -0.0118 -0.0749 162 ASP   B CB  
6357 C CG  . ASP   B 162 ? 0.1973 0.1972 0.3859 0.0082  -0.0092 -0.0876 162 ASP   B CG  
6358 O OD1 . ASP   B 162 ? 0.1999 0.2178 0.3779 0.0024  0.0035  -0.0789 162 ASP   B OD1 
6359 O OD2 . ASP   B 162 ? 0.2114 0.2201 0.4201 0.0225  0.0038  -0.0829 162 ASP   B OD2 
6364 N N   A LYS   B 163 ? 0.1744 0.1280 0.3120 -0.0071 -0.0229 -0.0289 163 LYS   B N   
6365 N N   B LYS   B 163 ? 0.1836 0.1554 0.3167 -0.0113 -0.0156 -0.0270 163 LYS   B N   
6366 C CA  A LYS   B 163 ? 0.1813 0.1379 0.3066 -0.0145 -0.0220 -0.0039 163 LYS   B CA  
6367 C CA  B LYS   B 163 ? 0.1935 0.1728 0.3149 -0.0142 -0.0159 -0.0109 163 LYS   B CA  
6368 C C   A LYS   B 163 ? 0.1535 0.1369 0.2982 -0.0228 -0.0221 -0.0049 163 LYS   B C   
6369 C C   B LYS   B 163 ? 0.1664 0.1533 0.2991 -0.0170 -0.0181 -0.0051 163 LYS   B C   
6370 O O   A LYS   B 163 ? 0.1488 0.1480 0.3207 -0.0266 -0.0175 -0.0083 163 LYS   B O   
6371 O O   B LYS   B 163 ? 0.1661 0.1560 0.3087 -0.0165 -0.0169 0.0016  163 LYS   B O   
6372 C CB  A LYS   B 163 ? 0.2214 0.1648 0.3380 -0.0155 -0.0288 0.0037  163 LYS   B CB  
6373 C CB  B LYS   B 163 ? 0.2298 0.2120 0.3429 -0.0155 -0.0178 -0.0066 163 LYS   B CB  
6374 C CG  A LYS   B 163 ? 0.2853 0.2296 0.3837 -0.0224 -0.0163 0.0101  163 LYS   B CG  
6375 C CG  B LYS   B 163 ? 0.2683 0.2540 0.3766 -0.0175 -0.0134 -0.0025 163 LYS   B CG  
6376 C CD  A LYS   B 163 ? 0.3440 0.2800 0.4374 -0.0319 -0.0107 0.0013  163 LYS   B CD  
6377 C CD  B LYS   B 163 ? 0.3041 0.2926 0.4151 -0.0204 -0.0106 -0.0036 163 LYS   B CD  
6378 C CE  A LYS   B 163 ? 0.3805 0.3155 0.4687 -0.0383 -0.0043 0.0009  163 LYS   B CE  
6379 C CE  B LYS   B 163 ? 0.3293 0.3209 0.4436 -0.0232 -0.0074 -0.0031 163 LYS   B CE  
6380 N NZ  A LYS   B 163 ? 0.4003 0.3368 0.4903 -0.0424 -0.0003 -0.0038 163 LYS   B NZ  
6381 N NZ  B LYS   B 163 ? 0.3386 0.3274 0.4616 -0.0247 -0.0054 -0.0042 163 LYS   B NZ  
6408 N N   . LEU   B 164 ? 0.1428 0.1341 0.2797 -0.0176 -0.0205 -0.0070 164 LEU   B N   
6409 C CA  . LEU   B 164 ? 0.1464 0.1375 0.2653 -0.0059 -0.0268 -0.0035 164 LEU   B CA  
6410 C C   . LEU   B 164 ? 0.1507 0.1374 0.2703 -0.0149 -0.0316 0.0049  164 LEU   B C   
6411 O O   . LEU   B 164 ? 0.1531 0.1565 0.2924 -0.0150 -0.0272 0.0036  164 LEU   B O   
6412 C CB  . LEU   B 164 ? 0.1428 0.1330 0.2568 -0.0091 -0.0294 -0.0090 164 LEU   B CB  
6413 C CG  . LEU   B 164 ? 0.1508 0.1538 0.2704 -0.0041 -0.0156 -0.0027 164 LEU   B CG  
6414 C CD1 . LEU   B 164 ? 0.1537 0.1539 0.2686 -0.0072 -0.0240 -0.0156 164 LEU   B CD1 
6415 C CD2 . LEU   B 164 ? 0.1672 0.1904 0.2778 -0.0075 -0.0008 -0.0207 164 LEU   B CD2 
6428 N N   . VAL   B 165 ? 0.1795 0.1482 0.2916 -0.0158 -0.0343 -0.0039 165 VAL   B N   
6429 C CA  . VAL   B 165 ? 0.2087 0.1599 0.2984 -0.0285 -0.0528 -0.0008 165 VAL   B CA  
6430 C C   . VAL   B 165 ? 0.2333 0.1717 0.3271 -0.0348 -0.0838 -0.0133 165 VAL   B C   
6431 O O   . VAL   B 165 ? 0.2547 0.1833 0.3355 -0.0379 -0.0839 -0.0064 165 VAL   B O   
6432 C CB  . VAL   B 165 ? 0.2301 0.1743 0.2970 -0.0122 -0.0249 -0.0109 165 VAL   B CB  
6433 C CG1 . VAL   B 165 ? 0.2453 0.1809 0.3272 -0.0120 -0.0162 -0.0085 165 VAL   B CG1 
6434 C CG2 . VAL   B 165 ? 0.2250 0.1791 0.2896 -0.0110 -0.0182 -0.0132 165 VAL   B CG2 
6444 N N   . SER   B 166 ? 0.2414 0.1571 0.3612 -0.0314 -0.0866 -0.0353 166 SER   B N   
6445 C CA  . SER   B 166 ? 0.2387 0.1588 0.4109 -0.0295 -0.0723 -0.0374 166 SER   B CA  
6446 C C   . SER   B 166 ? 0.2252 0.1653 0.4275 -0.0401 -0.0663 -0.0145 166 SER   B C   
6447 O O   . SER   B 166 ? 0.2331 0.1901 0.4630 -0.0562 -0.0736 -0.0321 166 SER   B O   
6448 C CB  . SER   B 166 ? 0.2399 0.1695 0.4317 -0.0209 -0.0644 -0.0450 166 SER   B CB  
6449 O OG  . SER   B 166 ? 0.2323 0.1668 0.4351 -0.0174 -0.0638 -0.0205 166 SER   B OG  
6455 N N   . SER   B 167 ? 0.2044 0.1626 0.3992 -0.0351 -0.0712 0.0220  167 SER   B N   
6456 C CA  . SER   B 167 ? 0.1952 0.1713 0.3752 -0.0316 -0.0560 0.0281  167 SER   B CA  
6457 C C   . SER   B 167 ? 0.1903 0.1779 0.3565 -0.0492 -0.0480 0.0531  167 SER   B C   
6458 O O   . SER   B 167 ? 0.1970 0.1858 0.3529 -0.0498 -0.0425 0.0577  167 SER   B O   
6459 C CB  . SER   B 167 ? 0.1914 0.1794 0.3709 -0.0325 -0.0338 0.0170  167 SER   B CB  
6460 O OG  . SER   B 167 ? 0.1879 0.1888 0.3494 -0.0248 -0.0118 0.0191  167 SER   B OG  
6466 N N   . PHE   B 168 ? 0.1865 0.1778 0.3498 -0.0442 -0.0388 0.0595  168 PHE   B N   
6467 C CA  . PHE   B 168 ? 0.1952 0.1778 0.3233 -0.0424 -0.0316 0.0340  168 PHE   B CA  
6468 C C   . PHE   B 168 ? 0.1763 0.1638 0.2633 -0.0188 -0.0183 0.0140  168 PHE   B C   
6469 O O   . PHE   B 168 ? 0.2076 0.1584 0.2699 0.0052  -0.0161 -0.0041 168 PHE   B O   
6470 C CB  . PHE   B 168 ? 0.2132 0.1835 0.3344 -0.0534 -0.0379 0.0452  168 PHE   B CB  
6471 C CG  . PHE   B 168 ? 0.2382 0.1659 0.3193 -0.0539 -0.0403 0.0237  168 PHE   B CG  
6472 C CD1 . PHE   B 168 ? 0.2734 0.1713 0.3338 -0.0447 -0.0462 0.0177  168 PHE   B CD1 
6473 C CD2 . PHE   B 168 ? 0.2269 0.1569 0.3179 -0.0459 -0.0446 0.0143  168 PHE   B CD2 
6474 C CE1 . PHE   B 168 ? 0.2852 0.1767 0.3307 -0.0327 -0.0425 0.0225  168 PHE   B CE1 
6475 C CE2 . PHE   B 168 ? 0.2572 0.1622 0.3272 -0.0290 -0.0524 0.0136  168 PHE   B CE2 
6476 C CZ  . PHE   B 168 ? 0.2721 0.1623 0.3285 -0.0164 -0.0572 0.0284  168 PHE   B CZ  
6486 N N   . LEU   B 169 ? 0.1815 0.1807 0.2545 -0.0004 0.0001  0.0033  169 LEU   B N   
6487 C CA  . LEU   B 169 ? 0.2078 0.2126 0.2926 -0.0089 -0.0024 -0.0272 169 LEU   B CA  
6488 C C   . LEU   B 169 ? 0.2347 0.2338 0.3405 0.0020  -0.0065 -0.0545 169 LEU   B C   
6489 O O   . LEU   B 169 ? 0.2570 0.2507 0.3874 0.0008  -0.0033 -0.0747 169 LEU   B O   
6490 C CB  . LEU   B 169 ? 0.2286 0.2576 0.3145 -0.0189 -0.0053 -0.0019 169 LEU   B CB  
6491 C CG  . LEU   B 169 ? 0.2719 0.2945 0.3585 -0.0083 0.0031  0.0028  169 LEU   B CG  
6492 C CD1 . LEU   B 169 ? 0.2905 0.3149 0.3637 -0.0112 0.0014  0.0193  169 LEU   B CD1 
6493 C CD2 . LEU   B 169 ? 0.2677 0.3003 0.3589 0.0065  0.0203  -0.0148 169 LEU   B CD2 
6494 O OXT . LEU   B 169 ? 0.2536 0.2505 0.3375 0.0290  0.0016  -0.0532 169 LEU   B OXT 
6506 C C1  T TFA   C .   ? 0.1418 0.1521 0.1290 -0.0023 0.0320  0.0219  201 TFA   A C1  
6507 C C2  T TFA   C .   ? 0.1702 0.1835 0.1630 -0.0158 0.0229  -0.0020 201 TFA   A C2  
6508 O O   T TFA   C .   ? 0.1145 0.1274 0.1188 -0.0039 0.0283  0.0345  201 TFA   A O   
6509 F F1  T TFA   C .   ? 0.1789 0.1948 0.1822 -0.0106 0.0137  -0.0130 201 TFA   A F1  
6510 F F2  T TFA   C .   ? 0.1843 0.1901 0.1659 -0.0173 0.0320  0.0083  201 TFA   A F2  
6511 F F3  T TFA   C .   ? 0.1838 0.2003 0.1892 -0.0312 0.0292  -0.0080 201 TFA   A F3  
6512 O OXT T TFA   C .   ? 0.1466 0.1476 0.1390 0.0214  0.0354  0.0244  201 TFA   A OXT 
6513 N N2  B A1A9O D .   ? 0.1711 0.1953 0.1796 0.0066  -0.0145 -0.0190 202 A1A9O A N2  
6514 C C3  B A1A9O D .   ? 0.2035 0.2290 0.2378 -0.0318 0.0271  -0.0010 202 A1A9O A C3  
6515 C C6  B A1A9O D .   ? 0.2106 0.2420 0.2449 -0.0390 0.0382  0.0026  202 A1A9O A C6  
6516 C C9  B A1A9O D .   ? 0.1926 0.2043 0.2210 -0.0214 0.0103  -0.0023 202 A1A9O A C9  
6517 C C12 B A1A9O D .   ? 0.1700 0.1983 0.1793 0.0110  -0.0119 -0.0042 202 A1A9O A C12 
6518 C C14 B A1A9O D .   ? 0.1522 0.1906 0.1619 0.0033  -0.0187 0.0042  202 A1A9O A C14 
6519 C C1  B A1A9O D .   ? 0.1948 0.2177 0.2309 -0.0302 0.0142  0.0049  202 A1A9O A C1  
6520 C C10 B A1A9O D .   ? 0.2009 0.2129 0.2291 -0.0193 0.0220  -0.0025 202 A1A9O A C10 
6521 C C11 B A1A9O D .   ? 0.1637 0.1942 0.1731 -0.0023 -0.0168 -0.0021 202 A1A9O A C11 
6522 C C13 B A1A9O D .   ? 0.1512 0.1842 0.1580 0.0107  -0.0295 0.0062  202 A1A9O A C13 
6523 C C15 B A1A9O D .   ? 0.1451 0.1904 0.1626 -0.0024 -0.0133 0.0106  202 A1A9O A C15 
6524 C C16 B A1A9O D .   ? 0.1315 0.1773 0.1562 -0.0064 -0.0341 0.0203  202 A1A9O A C16 
6525 C C2  B A1A9O D .   ? 0.1964 0.2182 0.2353 -0.0278 0.0149  -0.0020 202 A1A9O A C2  
6526 C C4  B A1A9O D .   ? 0.2087 0.2377 0.2468 -0.0323 0.0327  -0.0060 202 A1A9O A C4  
6527 C C5  B A1A9O D .   ? 0.2124 0.2417 0.2442 -0.0378 0.0388  0.0033  202 A1A9O A C5  
6528 C C7  B A1A9O D .   ? 0.2110 0.2385 0.2429 -0.0352 0.0324  0.0051  202 A1A9O A C7  
6529 C C8  B A1A9O D .   ? 0.2067 0.2320 0.2341 -0.0341 0.0331  -0.0001 202 A1A9O A C8  
6530 N N1  B A1A9O D .   ? 0.1759 0.1931 0.1959 -0.0173 -0.0082 0.0011  202 A1A9O A N1  
6531 N N3  B A1A9O D .   ? 0.1670 0.1946 0.1679 0.0112  -0.0169 0.0044  202 A1A9O A N3  
6532 N N4  B A1A9O D .   ? 0.1340 0.1688 0.1442 0.0069  -0.0422 0.0286  202 A1A9O A N4  
6533 O O1  B A1A9O D .   ? 0.2052 0.2176 0.2409 -0.0205 0.0401  0.0031  202 A1A9O A O1  
6552 O O   . HOH   E .   ? 0.2555 0.2319 0.3776 -0.0186 -0.0188 0.0621  301 HOH   A O   
6553 O O   . HOH   E .   ? 0.4188 0.8173 0.4928 -0.1184 0.0267  0.1097  302 HOH   A O   
6554 O O   . HOH   E .   ? 0.2730 0.2700 0.4368 -0.0169 -0.1092 0.1161  303 HOH   A O   
6555 O O   B HOH   E .   ? 0.2379 0.2460 0.2292 -0.0841 0.0138  -0.0131 304 HOH   A O   
6556 O O   . HOH   E .   ? 0.6569 0.4377 0.3553 0.1549  -0.1565 0.0552  305 HOH   A O   
6557 O O   . HOH   E .   ? 0.5556 0.3722 0.5138 -0.0685 0.1414  0.1139  306 HOH   A O   
6558 O O   . HOH   E .   ? 0.2140 0.2306 0.2401 -0.0243 0.0435  0.0418  307 HOH   A O   
6559 O O   . HOH   E .   ? 0.4574 0.3366 0.4484 -0.0349 0.1180  -0.0319 308 HOH   A O   
6560 O O   . HOH   E .   ? 0.6505 0.5984 0.4676 -0.1014 0.0223  0.2248  309 HOH   A O   
6561 O O   . HOH   E .   ? 0.7652 0.6311 0.4068 -0.1040 0.0079  0.2465  310 HOH   A O   
6562 O O   . HOH   E .   ? 0.3015 0.3320 0.1842 -0.0449 0.0440  0.0537  311 HOH   A O   
6563 O O   . HOH   E .   ? 0.1624 0.1774 0.2568 0.0078  -0.0255 -0.0560 312 HOH   A O   
6564 O O   . HOH   E .   ? 0.2560 0.4418 0.4066 0.0100  -0.0606 0.0296  313 HOH   A O   
6565 O O   . HOH   E .   ? 0.4768 0.5034 0.4678 -0.0536 0.1195  0.2465  314 HOH   A O   
6566 O O   . HOH   E .   ? 0.5650 0.3906 0.5394 0.0127  0.1646  -0.1518 315 HOH   A O   
6567 O O   . HOH   E .   ? 0.2167 0.1962 0.3765 -0.0457 -0.0003 -0.0293 316 HOH   A O   
6568 O O   A HOH   E .   ? 0.2297 0.4523 0.5215 0.0694  0.0522  0.0662  317 HOH   A O   
6569 O O   . HOH   E .   ? 0.3566 0.3184 0.2789 -0.1152 0.0075  0.0783  318 HOH   A O   
6570 O O   . HOH   E .   ? 0.4580 0.3687 0.3555 -0.1125 0.1612  -0.0020 319 HOH   A O   
6571 O O   B HOH   E .   ? 0.2491 0.2453 0.2549 -0.0290 -0.0186 -0.0792 320 HOH   A O   
6572 O O   . HOH   E .   ? 0.5226 0.4647 0.4397 -0.1785 -0.1104 0.2367  321 HOH   A O   
6573 O O   . HOH   E .   ? 0.1957 0.3680 0.3760 -0.0434 0.0390  -0.1043 322 HOH   A O   
6574 O O   . HOH   E .   ? 0.1895 0.2901 0.3249 0.0273  -0.0078 -0.0120 323 HOH   A O   
6575 O O   . HOH   E .   ? 0.6564 0.5549 0.3514 -0.0132 -0.0632 0.1197  324 HOH   A O   
6576 O O   . HOH   E .   ? 0.4485 0.4744 0.5823 0.1363  0.1459  -0.1119 325 HOH   A O   
6577 O O   . HOH   E .   ? 0.1577 0.1624 0.2236 -0.0183 0.0047  -0.0033 326 HOH   A O   
6578 O O   . HOH   E .   ? 0.5244 0.5351 0.2624 -0.1155 0.1063  0.1144  327 HOH   A O   
6579 O O   . HOH   E .   ? 0.6028 0.6281 0.4972 -0.1194 -0.1267 -0.0696 328 HOH   A O   
6580 O O   . HOH   E .   ? 0.5809 0.3351 0.3264 -0.0830 -0.0901 -0.0102 329 HOH   A O   
6581 O O   . HOH   E .   ? 0.4506 0.2233 0.4793 0.0313  -0.1665 0.0407  330 HOH   A O   
6582 O O   . HOH   E .   ? 0.5356 0.4256 0.4558 -0.0442 -0.0407 -0.0925 331 HOH   A O   
6583 O O   . HOH   E .   ? 0.1543 0.3515 0.2395 -0.0048 0.0265  0.0470  332 HOH   A O   
6584 O O   . HOH   E .   ? 0.3284 0.4576 0.2561 -0.0217 0.0473  0.0196  333 HOH   A O   
6585 O O   . HOH   E .   ? 0.2181 0.2330 0.2566 0.0107  -0.0034 0.0633  334 HOH   A O   
6586 O O   . HOH   E .   ? 0.2319 0.5219 0.4103 -0.0203 -0.0527 0.2201  335 HOH   A O   
6587 O O   . HOH   E .   ? 0.2872 0.2861 0.3094 0.0162  -0.0404 -0.0626 336 HOH   A O   
6588 O O   . HOH   E .   ? 0.2469 0.2162 0.2541 -0.0197 -0.0074 -0.0210 337 HOH   A O   
6589 O O   . HOH   E .   ? 0.2994 0.2970 0.2245 -0.0020 -0.0478 0.0188  338 HOH   A O   
6590 O O   . HOH   E .   ? 0.2461 0.2282 0.2686 0.0250  0.0353  0.0349  339 HOH   A O   
6591 O O   A HOH   E .   ? 0.1458 0.2076 0.1919 0.0353  0.0415  0.0419  340 HOH   A O   
6592 O O   . HOH   E .   ? 0.8084 0.4120 0.5828 -0.0837 -0.1372 0.0403  341 HOH   A O   
6593 O O   . HOH   E .   ? 0.5317 0.4531 0.5324 0.0652  0.2296  -0.0750 342 HOH   A O   
6594 O O   . HOH   E .   ? 0.4874 0.2225 0.5424 0.0630  0.0140  0.0103  343 HOH   A O   
6595 O O   . HOH   E .   ? 0.3399 0.5530 0.5348 0.1152  0.0241  0.1511  344 HOH   A O   
6596 O O   . HOH   E .   ? 0.2230 0.1761 0.2351 -0.0143 -0.0456 -0.0036 345 HOH   A O   
6597 O O   A HOH   E .   ? 0.2334 0.2989 0.4318 0.0196  0.1285  0.1535  346 HOH   A O   
6598 O O   . HOH   E .   ? 0.1822 0.1743 0.2152 0.0196  -0.0172 0.0259  347 HOH   A O   
6599 O O   . HOH   E .   ? 0.2208 0.1775 0.2453 0.0235  -0.0266 -0.0003 348 HOH   A O   
6600 O O   . HOH   E .   ? 0.2369 0.4352 0.3594 0.1013  -0.0836 -0.0168 349 HOH   A O   
6601 O O   . HOH   E .   ? 0.3016 0.3501 0.3653 -0.0910 -0.0663 -0.0410 350 HOH   A O   
6602 O O   . HOH   E .   ? 0.1518 0.2310 0.2327 -0.0011 -0.0117 0.0573  351 HOH   A O   
6603 O O   . HOH   E .   ? 0.2054 0.2066 0.3817 0.0217  0.0935  -0.0008 352 HOH   A O   
6604 O O   . HOH   E .   ? 0.1421 0.1319 0.1325 -0.0046 0.0135  0.0075  353 HOH   A O   
6605 O O   . HOH   E .   ? 0.1561 0.1940 0.2606 0.0068  -0.0085 0.0127  354 HOH   A O   
6606 O O   . HOH   E .   ? 0.5511 0.4414 0.6698 0.1158  -0.0979 -0.0301 355 HOH   A O   
6607 O O   . HOH   E .   ? 0.4960 0.2872 0.4594 -0.1562 0.1710  -0.0382 356 HOH   A O   
6608 O O   A HOH   E .   ? 0.1876 0.2472 0.2288 0.0253  0.0306  0.0144  357 HOH   A O   
6609 O O   . HOH   E .   ? 0.3080 0.3524 0.2439 -0.0894 -0.0112 -0.0724 358 HOH   A O   
6610 O O   . HOH   E .   ? 0.6255 0.6201 0.4222 0.1983  -0.0799 -0.0134 359 HOH   A O   
6611 O O   A HOH   E .   ? 0.3742 0.1662 0.1727 0.0265  0.0053  0.0127  360 HOH   A O   
6612 O O   . HOH   E .   ? 0.2948 0.3417 0.5201 -0.0771 -0.1092 -0.0946 361 HOH   A O   
6613 O O   . HOH   E .   ? 0.3642 0.4375 0.3729 0.1917  0.0788  0.0483  362 HOH   A O   
6614 O O   . HOH   E .   ? 0.1588 0.1371 0.2415 -0.0096 0.0207  -0.0087 363 HOH   A O   
6615 O O   . HOH   E .   ? 0.2735 0.4104 0.3224 -0.0480 0.0671  0.0089  364 HOH   A O   
6616 O O   . HOH   E .   ? 0.4032 0.2204 0.2418 0.1229  0.0520  0.0238  365 HOH   A O   
6617 O O   . HOH   E .   ? 0.3440 0.3037 0.3381 -0.0951 0.0025  -0.0280 366 HOH   A O   
6618 O O   . HOH   E .   ? 0.2032 0.2008 0.2523 -0.0365 0.0055  0.0413  367 HOH   A O   
6619 O O   . HOH   E .   ? 0.2799 0.4528 0.3235 0.0668  0.0936  0.1983  368 HOH   A O   
6620 O O   . HOH   E .   ? 0.1517 0.1542 0.1547 -0.0042 -0.0083 -0.0003 369 HOH   A O   
6621 O O   . HOH   E .   ? 0.6036 0.3851 0.3240 0.0196  0.0256  0.1337  370 HOH   A O   
6622 O O   . HOH   E .   ? 0.3543 0.7235 0.4662 -0.0493 -0.1407 0.0529  371 HOH   A O   
6623 O O   . HOH   E .   ? 0.3082 0.3632 0.3531 -0.1268 0.0813  -0.0327 372 HOH   A O   
6624 O O   . HOH   E .   ? 0.3771 0.2540 0.4707 -0.1225 0.0642  0.0363  373 HOH   A O   
6625 O O   . HOH   E .   ? 0.3674 0.6498 0.4227 -0.0506 0.0124  0.1649  374 HOH   A O   
6626 O O   . HOH   E .   ? 0.3207 0.2521 0.4559 -0.0617 -0.0257 0.0232  375 HOH   A O   
6627 O O   . HOH   E .   ? 0.5115 0.2868 0.3112 -0.1200 0.0661  0.0261  376 HOH   A O   
6628 O O   . HOH   E .   ? 0.4517 0.4352 0.3516 0.1535  -0.0776 -0.1385 377 HOH   A O   
6629 O O   . HOH   E .   ? 0.2057 0.2202 0.2400 -0.0317 -0.0527 0.0376  378 HOH   A O   
6630 O O   B HOH   E .   ? 0.1917 0.1856 0.2107 -0.0196 -0.0528 -0.0257 379 HOH   A O   
6631 O O   . HOH   E .   ? 0.2625 0.2068 0.1804 -0.0649 0.0005  0.0310  380 HOH   A O   
6632 O O   . HOH   E .   ? 0.2027 0.2584 0.3530 0.0264  0.0805  -0.0592 381 HOH   A O   
6633 O O   . HOH   E .   ? 0.3099 0.2731 0.2363 0.0280  0.0789  -0.0009 382 HOH   A O   
6634 O O   B HOH   E .   ? 0.4808 0.3455 0.1869 0.0118  -0.0278 0.0181  383 HOH   A O   
6635 O O   . HOH   E .   ? 0.1850 0.2323 0.2797 -0.0270 0.0711  0.0396  384 HOH   A O   
6636 O O   . HOH   E .   ? 0.1789 0.2762 0.2852 0.0378  0.0397  0.0857  385 HOH   A O   
6637 O O   . HOH   E .   ? 0.1827 0.2166 0.1838 -0.0144 0.0098  0.0542  386 HOH   A O   
6638 O O   . HOH   E .   ? 0.5593 0.5276 0.6194 -0.0764 0.0469  0.1473  387 HOH   A O   
6639 O O   T HOH   E .   ? 0.0985 0.1133 0.2248 -0.0148 0.0259  0.0348  388 HOH   A O   
6640 O O   . HOH   E .   ? 0.3033 0.6750 0.3169 0.1148  0.0299  -0.1187 389 HOH   A O   
6641 O O   . HOH   E .   ? 0.2198 0.4237 0.3246 -0.0192 -0.0032 0.0796  390 HOH   A O   
6642 O O   . HOH   E .   ? 0.1690 0.1869 0.2188 -0.0211 0.0045  0.0341  391 HOH   A O   
6643 O O   B HOH   E .   ? 0.3862 0.3075 0.2984 0.0485  -0.0376 0.0435  392 HOH   A O   
6644 O O   . HOH   E .   ? 0.3265 0.2733 0.3436 -0.0056 -0.0313 0.0852  393 HOH   A O   
6645 O O   . HOH   E .   ? 0.2069 0.1973 0.1741 0.0067  0.0118  0.0154  394 HOH   A O   
6646 O O   . HOH   E .   ? 0.3256 0.3449 0.2512 -0.0242 -0.0368 0.0157  395 HOH   A O   
6647 O O   A HOH   E .   ? 0.2882 0.2452 0.2564 0.1010  0.0707  0.0655  396 HOH   A O   
6648 O O   A HOH   E .   ? 0.1857 0.1788 0.2102 -0.0019 -0.0351 0.0173  397 HOH   A O   
6649 O O   . HOH   E .   ? 0.2391 0.1805 0.2601 -0.0050 0.0039  0.0292  398 HOH   A O   
6650 O O   . HOH   E .   ? 0.2729 0.3362 0.2951 -0.0300 0.0841  -0.0543 399 HOH   A O   
6651 O O   . HOH   E .   ? 0.2622 0.3809 0.3508 -0.0335 0.0862  -0.0864 400 HOH   A O   
6652 O O   . HOH   E .   ? 0.1680 0.1716 0.1936 0.0150  -0.0264 -0.0334 401 HOH   A O   
6653 O O   A HOH   E .   ? 0.1846 0.1901 0.3062 -0.0215 0.0411  -0.0114 402 HOH   A O   
6654 O O   . HOH   E .   ? 0.3225 0.3480 0.3630 -0.0739 0.1381  0.0195  403 HOH   A O   
6655 O O   . HOH   E .   ? 0.3030 0.2751 0.2191 -0.0648 -0.0863 0.0206  404 HOH   A O   
6656 O O   . HOH   E .   ? 0.5499 0.6248 0.5865 -0.0106 0.1012  0.0710  405 HOH   A O   
6657 O O   . HOH   E .   ? 0.1872 0.2010 0.3718 0.0379  0.0983  0.1034  406 HOH   A O   
6658 O O   . HOH   E .   ? 0.1924 0.2244 0.2631 -0.0051 -0.0251 0.0738  407 HOH   A O   
6659 O O   . HOH   E .   ? 0.4831 0.4265 0.2090 -0.0028 0.1031  0.0886  408 HOH   A O   
6660 O O   . HOH   E .   ? 0.1404 0.1478 0.1826 0.0004  -0.0190 0.0043  409 HOH   A O   
6661 O O   . HOH   E .   ? 0.2261 0.1731 0.2858 0.0006  -0.0238 0.0063  410 HOH   A O   
6662 O O   . HOH   E .   ? 0.2061 0.1734 0.1604 -0.0086 0.0201  0.0119  411 HOH   A O   
6663 O O   . HOH   E .   ? 0.1583 0.1758 0.2813 -0.0040 -0.0021 0.0144  412 HOH   A O   
6664 O O   . HOH   E .   ? 0.3430 0.6454 0.5288 0.0877  0.1279  0.0759  413 HOH   A O   
6665 O O   . HOH   E .   ? 0.1992 0.2654 0.3637 -0.0223 -0.0219 -0.0036 414 HOH   A O   
6666 O O   . HOH   E .   ? 0.2035 0.1946 0.2850 0.0238  -0.0474 0.0215  415 HOH   A O   
6667 O O   . HOH   E .   ? 0.4694 0.4320 0.3778 0.1925  -0.0046 -0.0741 416 HOH   A O   
6668 O O   . HOH   E .   ? 0.5451 0.2738 0.5048 0.0444  0.0576  -0.0033 417 HOH   A O   
6669 O O   . HOH   E .   ? 0.6012 0.6149 0.5083 0.0640  0.1198  0.0799  418 HOH   A O   
6670 O O   . HOH   E .   ? 0.1802 0.1424 0.1623 -0.0205 0.0126  -0.0046 419 HOH   A O   
6671 O O   . HOH   E .   ? 0.2062 0.2987 0.2353 -0.0131 -0.0532 0.0408  420 HOH   A O   
6672 O O   . HOH   E .   ? 0.2633 0.2140 0.2910 -0.0669 -0.0174 0.0696  421 HOH   A O   
6673 O O   B HOH   E .   ? 0.3231 0.2569 0.2984 0.0732  -0.0560 -0.0675 422 HOH   A O   
6674 O O   . HOH   E .   ? 0.4413 0.5855 0.3631 -0.0620 0.0083  0.1272  423 HOH   A O   
6675 O O   . HOH   E .   ? 0.3285 0.1333 0.2111 0.0054  -0.0343 0.0127  424 HOH   A O   
6676 O O   . HOH   E .   ? 0.2820 0.6187 0.1858 -0.0382 0.0404  0.0304  425 HOH   A O   
6677 O O   . HOH   E .   ? 0.4351 0.2323 0.5563 -0.0860 -0.2303 0.1169  426 HOH   A O   
6678 O O   . HOH   E .   ? 0.3294 0.3622 0.7355 0.0022  0.1285  -0.0563 427 HOH   A O   
6679 O O   . HOH   E .   ? 0.6837 0.3942 0.5171 0.2020  -0.0705 0.1582  428 HOH   A O   
6680 O O   . HOH   E .   ? 0.2375 0.4139 0.2743 0.1558  -0.0018 0.0049  429 HOH   A O   
6681 O O   . HOH   E .   ? 0.6316 0.6474 0.6548 -0.1263 -0.0839 -0.0892 430 HOH   A O   
6682 O O   . HOH   E .   ? 0.2045 0.2411 0.3984 0.0206  -0.0360 -0.0508 431 HOH   A O   
6683 O O   . HOH   E .   ? 0.1689 0.1942 0.2700 -0.0102 0.0061  0.0307  432 HOH   A O   
6684 O O   . HOH   E .   ? 0.6136 0.7201 0.4341 0.0761  0.2714  -0.0695 433 HOH   A O   
6685 O O   . HOH   E .   ? 0.9233 0.9098 0.7459 -0.0221 -0.0058 -0.0532 434 HOH   A O   
6686 O O   . HOH   E .   ? 0.5951 0.7418 0.4218 0.2092  -0.0856 0.1851  435 HOH   A O   
6687 O O   . HOH   E .   ? 0.1940 0.1556 0.1734 -0.0001 -0.0181 -0.0076 436 HOH   A O   
6688 O O   A HOH   E .   ? 0.1635 0.1444 0.1742 0.0068  -0.0350 0.0032  437 HOH   A O   
6689 O O   . HOH   E .   ? 0.3396 0.7500 0.6414 -0.0538 -0.1251 0.0041  438 HOH   A O   
6690 O O   . HOH   E .   ? 0.3505 0.2901 0.1781 -0.0730 0.0233  0.0580  439 HOH   A O   
6691 O O   . HOH   E .   ? 0.4966 0.5001 0.3982 -0.0353 -0.1389 0.0297  440 HOH   A O   
6692 O O   . HOH   E .   ? 0.2628 0.1706 0.2734 0.0083  0.0039  0.0147  441 HOH   A O   
6693 O O   A HOH   E .   ? 0.1703 0.1375 0.1768 0.0126  -0.0484 -0.0168 442 HOH   A O   
6694 O O   . HOH   E .   ? 0.3689 0.3472 0.3157 0.1969  -0.0380 -0.0379 443 HOH   A O   
6695 O O   . HOH   E .   ? 0.3223 0.3988 0.5752 -0.0085 0.1526  -0.1572 444 HOH   A O   
6696 O O   . HOH   E .   ? 0.1953 0.2334 0.4984 -0.0292 -0.0882 0.0739  445 HOH   A O   
6697 O O   . HOH   E .   ? 0.5381 0.2895 0.5624 0.0378  0.1205  -0.0750 446 HOH   A O   
6698 O O   . HOH   E .   ? 0.5993 0.6116 0.6751 -0.1484 -0.0376 -0.1272 447 HOH   A O   
6699 O O   . HOH   E .   ? 0.5143 0.4569 0.4776 -0.0997 -0.1102 -0.1287 448 HOH   A O   
6700 O O   . HOH   E .   ? 0.8552 0.4983 0.5087 0.0314  0.1843  0.1496  449 HOH   A O   
6701 O O   A HOH   E .   ? 0.5429 0.2554 0.3229 -0.0223 0.0716  0.1177  450 HOH   A O   
6702 O O   . HOH   E .   ? 0.2374 0.2036 0.2778 0.0153  0.0234  0.0263  451 HOH   A O   
6703 O O   . HOH   E .   ? 0.2309 0.2744 0.2579 -0.0031 -0.0232 -0.0507 452 HOH   A O   
6704 O O   . HOH   E .   ? 0.6925 0.5441 0.7994 0.0744  -0.1111 0.2002  453 HOH   A O   
6705 O O   B HOH   E .   ? 0.2157 0.1996 0.2928 -0.0031 0.0943  0.1059  454 HOH   A O   
6706 O O   . HOH   E .   ? 0.6941 0.7126 0.5969 0.1043  -0.1301 -0.0002 455 HOH   A O   
6707 O O   . HOH   E .   ? 0.5429 0.3451 0.4299 -0.0082 0.0255  0.0587  456 HOH   A O   
6708 O O   . HOH   E .   ? 0.3782 0.4534 0.3946 0.1780  -0.0583 0.0731  457 HOH   A O   
6709 O O   . HOH   E .   ? 0.6606 0.5803 0.4949 -0.0903 0.1095  0.0728  458 HOH   A O   
6710 O O   . HOH   E .   ? 0.4862 0.4929 0.4302 0.1000  -0.0056 0.0528  459 HOH   A O   
6711 O O   . HOH   E .   ? 0.4573 0.3533 0.5106 0.0251  0.0053  0.0196  460 HOH   A O   
6712 O O   . HOH   E .   ? 0.7096 0.7703 0.4954 0.0910  -0.1052 -0.0172 461 HOH   A O   
6713 O O   . HOH   E .   ? 0.2927 0.2597 0.3492 -0.0395 0.0393  -0.0706 462 HOH   A O   
6714 O O   . HOH   E .   ? 0.3387 0.4899 0.5401 -0.1388 0.1093  -0.1560 463 HOH   A O   
6715 O O   . HOH   E .   ? 0.4781 0.5055 0.4909 0.1047  -0.0328 0.1520  464 HOH   A O   
6716 O O   . HOH   E .   ? 0.6666 0.6042 0.5966 0.0744  0.1780  0.1853  465 HOH   A O   
6717 O O   . HOH   E .   ? 0.2991 0.5165 0.4343 -0.0652 0.0101  -0.0071 466 HOH   A O   
6718 O O   . HOH   E .   ? 0.2570 0.3007 0.3731 -0.0964 0.0550  -0.0428 467 HOH   A O   
6719 O O   . HOH   E .   ? 0.2789 0.4438 0.5101 0.0617  0.0091  -0.1885 468 HOH   A O   
6720 O O   . HOH   E .   ? 0.3041 0.2639 0.6273 0.0685  -0.1623 -0.0698 469 HOH   A O   
6721 O O   . HOH   E .   ? 0.6717 0.3763 0.6893 0.0832  0.0188  0.2181  470 HOH   A O   
6722 O O   . HOH   E .   ? 0.4292 0.5969 0.3734 -0.1075 -0.0866 0.2240  471 HOH   A O   
6723 O O   . HOH   E .   ? 0.6000 0.4944 0.4915 0.0341  0.1498  0.0418  472 HOH   A O   
6724 O O   . HOH   E .   ? 0.2758 0.1745 0.2585 0.0258  -0.0876 -0.0220 473 HOH   A O   
6725 O O   . HOH   E .   ? 0.3330 0.2789 0.3975 0.0044  0.1095  -0.0107 474 HOH   A O   
6726 O O   . HOH   E .   ? 0.4176 0.5261 0.3939 0.0317  -0.0441 -0.0781 475 HOH   A O   
6727 O O   B HOH   E .   ? 0.2302 0.1832 0.3859 -0.0768 -0.0444 0.1011  476 HOH   A O   
6728 O O   . HOH   E .   ? 0.2378 0.2223 0.2483 0.0071  0.0126  0.0043  477 HOH   A O   
6729 O O   . HOH   E .   ? 0.4476 0.4640 0.5482 -0.1891 -0.0310 -0.0238 478 HOH   A O   
6730 O O   . HOH   E .   ? 0.4964 0.5939 0.5568 -0.1656 -0.1145 -0.0271 479 HOH   A O   
6731 O O   . HOH   E .   ? 0.5327 0.5675 0.4799 0.1214  -0.0903 -0.0839 480 HOH   A O   
6732 O O   . HOH   E .   ? 0.5044 0.2780 0.3394 -0.0879 -0.1340 0.0579  481 HOH   A O   
6733 O O   . HOH   E .   ? 0.4051 0.4802 0.2742 -0.0012 0.0044  -0.0096 482 HOH   A O   
6734 O O   . HOH   E .   ? 0.7038 0.5704 0.6872 -0.1395 0.0352  -0.1054 483 HOH   A O   
6735 O O   . HOH   E .   ? 0.5766 0.4316 0.4465 0.0057  0.0171  -0.1316 484 HOH   A O   
6736 O O   . HOH   E .   ? 0.8063 0.3716 0.3166 -0.0189 -0.1364 0.0438  485 HOH   A O   
6737 O O   . HOH   E .   ? 0.4283 0.4711 0.3142 -0.0543 -0.0347 -0.0223 486 HOH   A O   
6738 O O   . HOH   E .   ? 0.5830 0.5056 0.4558 -0.0780 -0.0788 -0.0598 487 HOH   A O   
6739 O O   . HOH   E .   ? 0.2845 0.5417 0.3631 0.1257  0.1102  0.2344  488 HOH   A O   
6740 O O   . HOH   E .   ? 0.5373 0.5973 0.6630 0.1137  0.1647  -0.1173 489 HOH   A O   
6741 O O   . HOH   E .   ? 0.3300 0.4376 0.5253 0.0546  0.1834  0.1388  490 HOH   A O   
6742 O O   . HOH   E .   ? 0.6277 0.7098 0.4304 -0.0648 0.1320  0.1236  491 HOH   A O   
6743 O O   . HOH   E .   ? 0.4824 0.4054 0.2894 -0.1167 0.1554  -0.0669 492 HOH   A O   
6744 O O   . HOH   E .   ? 0.4802 0.4870 0.5729 0.0113  -0.0951 0.0665  493 HOH   A O   
6745 O O   . HOH   E .   ? 0.2561 0.2654 0.7255 -0.0162 -0.1286 0.0431  494 HOH   A O   
6746 O O   . HOH   E .   ? 0.2875 0.4711 0.3177 -0.0171 -0.0278 -0.1014 495 HOH   A O   
6747 O O   . HOH   E .   ? 0.5171 0.3351 0.4880 -0.0227 0.2711  0.0368  496 HOH   A O   
6748 O O   . HOH   E .   ? 0.4196 0.3090 0.4697 -0.1111 -0.0046 0.1085  497 HOH   A O   
6749 O O   . HOH   E .   ? 0.5693 0.3813 0.4215 -0.0192 0.1096  -0.0320 498 HOH   A O   
6750 O O   . HOH   E .   ? 0.2907 0.2416 0.5496 0.0101  0.0384  0.1196  499 HOH   A O   
6751 O O   . HOH   E .   ? 0.2589 0.3152 0.4697 0.0067  0.0887  -0.0717 500 HOH   A O   
6752 O O   B HOH   E .   ? 0.3143 0.5007 0.4511 0.1059  0.0498  0.0709  501 HOH   A O   
6753 O O   . HOH   E .   ? 0.2750 0.3955 0.3503 0.0919  -0.0426 0.0707  502 HOH   A O   
6754 O O   . HOH   E .   ? 0.4529 0.8166 0.5375 -0.1038 -0.0602 0.2589  503 HOH   A O   
6755 O O   . HOH   E .   ? 0.4699 0.2833 0.4425 -0.1490 0.0164  0.0556  504 HOH   A O   
6756 O O   . HOH   E .   ? 0.6586 0.2753 0.4473 -0.0621 0.0372  0.0624  505 HOH   A O   
6757 O O   . HOH   E .   ? 0.3029 0.4341 0.4423 0.0771  -0.0196 0.0181  506 HOH   A O   
6758 O O   . HOH   E .   ? 0.8143 0.4736 0.5731 0.0750  -0.0292 0.0114  507 HOH   A O   
6759 O O   . HOH   E .   ? 0.6024 0.7342 0.5343 0.0900  -0.0757 0.0354  508 HOH   A O   
6760 O O   B HOH   E .   ? 0.2310 0.3043 0.2927 0.0218  0.0419  0.0664  509 HOH   A O   
6761 O O   . HOH   E .   ? 0.6875 0.6448 0.5310 0.1198  -0.1455 0.0552  510 HOH   A O   
6762 O O   . HOH   E .   ? 0.2722 0.2565 0.5085 0.0234  0.0588  0.0760  511 HOH   A O   
6763 O O   . HOH   E .   ? 0.5422 0.6867 0.4815 0.3161  0.0237  0.1415  512 HOH   A O   
6764 O O   B HOH   E .   ? 0.3614 0.2056 0.3276 0.0047  -0.0877 0.0838  513 HOH   A O   
6765 O O   T HOH   E .   ? 0.1056 0.1253 0.2154 -0.0296 -0.0272 0.0656  514 HOH   A O   
6766 O O   A HOH   E .   ? 0.4677 0.8955 0.4221 0.1492  0.0766  0.0140  515 HOH   A O   
6767 O O   . HOH   E .   ? 0.4607 0.5679 0.4284 -0.0403 -0.0287 -0.1414 516 HOH   A O   
6768 O O   B HOH   E .   ? 0.2351 0.2039 0.2531 -0.0042 -0.0611 0.0017  517 HOH   A O   
6769 O O   . HOH   E .   ? 0.2729 0.7161 0.4518 0.0543  0.0557  -0.0419 518 HOH   A O   
6770 O O   . HOH   E .   ? 0.5417 0.5083 0.4140 0.1534  -0.0354 0.1316  519 HOH   A O   
6771 O O   . HOH   E .   ? 0.4917 0.6780 0.5508 -0.0661 -0.0949 0.0118  520 HOH   A O   
6772 O O   . HOH   E .   ? 0.3219 0.5000 0.5934 -0.0205 -0.1010 0.2998  521 HOH   A O   
6773 O O   . HOH   F .   ? 0.2497 0.2285 0.3082 0.0240  0.0772  0.0328  201 HOH   B O   
6774 O O   . HOH   F .   ? 0.3482 0.4978 0.5025 -0.0911 0.0247  -0.1573 202 HOH   B O   
6775 O O   . HOH   F .   ? 0.4685 0.3355 0.3898 -0.0524 0.0204  -0.1336 203 HOH   B O   
6776 O O   . HOH   F .   ? 0.5016 0.6060 0.2958 0.0863  -0.0466 -0.1489 204 HOH   B O   
6777 O O   . HOH   F .   ? 0.2899 0.6853 0.4024 0.0539  0.0369  0.2428  205 HOH   B O   
6778 O O   . HOH   F .   ? 0.5126 0.5628 0.3959 0.2721  -0.1143 -0.0272 206 HOH   B O   
6779 O O   . HOH   F .   ? 0.7005 0.3554 0.4973 0.0617  0.1473  0.0256  207 HOH   B O   
6780 O O   . HOH   F .   ? 0.6137 0.5886 0.6266 0.1741  0.0749  -0.0182 208 HOH   B O   
6781 O O   . HOH   F .   ? 0.5170 0.5893 0.3752 0.3141  -0.0702 -0.0037 209 HOH   B O   
6782 O O   . HOH   F .   ? 0.3478 0.4417 0.6650 -0.0887 0.0406  -0.0823 210 HOH   B O   
6783 O O   . HOH   F .   ? 0.6456 0.2962 0.4566 -0.1782 0.0448  0.0559  211 HOH   B O   
6784 O O   . HOH   F .   ? 0.2782 0.5154 0.5258 -0.0094 0.1440  -0.1998 212 HOH   B O   
6785 O O   . HOH   F .   ? 0.1878 0.2402 0.3086 -0.0028 0.0025  -0.0428 213 HOH   B O   
6786 O O   . HOH   F .   ? 0.2967 0.2064 0.5865 0.0316  0.2000  0.0928  214 HOH   B O   
6787 O O   . HOH   F .   ? 0.1619 0.1910 0.2950 -0.0146 0.0009  0.0045  215 HOH   B O   
6788 O O   . HOH   F .   ? 0.5357 0.3619 0.3707 -0.0240 -0.1097 0.0534  216 HOH   B O   
6789 O O   . HOH   F .   ? 0.3289 0.5147 0.4138 0.1548  0.0501  0.0094  217 HOH   B O   
6790 O O   . HOH   F .   ? 0.2894 0.3129 0.6970 0.0655  -0.1025 0.0376  218 HOH   B O   
6791 O O   . HOH   F .   ? 0.6744 0.5004 0.5125 0.1678  -0.0056 -0.1165 219 HOH   B O   
6792 O O   . HOH   F .   ? 0.4665 0.4056 0.6237 0.0479  -0.0937 0.2528  220 HOH   B O   
6793 O O   . HOH   F .   ? 0.5049 0.4797 0.6308 0.0248  -0.1648 -0.1036 221 HOH   B O   
6794 O O   . HOH   F .   ? 0.5257 0.2262 0.3211 -0.0059 -0.1030 0.0136  222 HOH   B O   
6795 O O   . HOH   F .   ? 0.4346 0.4554 0.3964 0.0207  0.0852  -0.1738 223 HOH   B O   
6796 O O   . HOH   F .   ? 0.2491 0.1908 0.2698 -0.0274 0.1010  -0.0045 224 HOH   B O   
6797 O O   . HOH   F .   ? 0.3477 0.4381 0.4731 0.0319  -0.1017 0.0587  225 HOH   B O   
6798 O O   . HOH   F .   ? 0.3689 0.2590 0.3943 0.0792  -0.0576 -0.0701 226 HOH   B O   
6799 O O   . HOH   F .   ? 0.4172 0.6529 0.3523 0.2405  0.0209  0.0065  227 HOH   B O   
6800 O O   . HOH   F .   ? 0.5399 0.6238 0.3137 0.0771  -0.0042 0.1155  228 HOH   B O   
6801 O O   . HOH   F .   ? 0.1766 0.2058 0.2985 -0.0123 0.0023  0.0093  229 HOH   B O   
6802 O O   . HOH   F .   ? 0.2916 0.2773 0.6025 -0.0265 0.0426  0.0290  230 HOH   B O   
6803 O O   . HOH   F .   ? 0.3406 0.2296 0.4560 0.0009  0.1618  0.0256  231 HOH   B O   
6804 O O   . HOH   F .   ? 0.3423 0.3291 0.4526 0.0654  -0.1054 -0.1776 232 HOH   B O   
6805 O O   . HOH   F .   ? 0.2318 0.2202 0.3952 -0.0399 0.0006  -0.0504 233 HOH   B O   
6806 O O   . HOH   F .   ? 0.3594 0.1950 0.2357 0.0257  -0.0811 -0.0122 234 HOH   B O   
6807 O O   . HOH   F .   ? 0.3829 0.3298 0.2266 0.0417  0.0766  0.0485  235 HOH   B O   
6808 O O   . HOH   F .   ? 0.2850 0.2739 0.3311 0.0446  0.0077  -0.1076 236 HOH   B O   
6809 O O   . HOH   F .   ? 0.2651 0.4330 0.3224 -0.0848 0.0440  -0.0815 237 HOH   B O   
6810 O O   . HOH   F .   ? 0.5581 0.3137 0.3988 -0.2294 -0.0438 0.0179  238 HOH   B O   
6811 O O   . HOH   F .   ? 0.1519 0.1511 0.1755 -0.0155 -0.0054 -0.0007 239 HOH   B O   
6812 O O   . HOH   F .   ? 0.2243 0.3602 0.3321 -0.0419 -0.0637 -0.0418 240 HOH   B O   
6813 O O   . HOH   F .   ? 0.2136 0.1402 0.3392 0.0144  -0.0573 -0.0180 241 HOH   B O   
6814 O O   . HOH   F .   ? 0.4480 0.3415 0.3370 -0.0945 0.0625  -0.0806 242 HOH   B O   
6815 O O   . HOH   F .   ? 0.3867 0.4242 0.5386 -0.1591 -0.0114 0.1070  243 HOH   B O   
6816 O O   . HOH   F .   ? 0.1638 0.1572 0.2582 -0.0015 0.0059  -0.0101 244 HOH   B O   
6817 O O   . HOH   F .   ? 0.3167 0.3801 0.2200 0.0540  0.0692  0.0240  245 HOH   B O   
6818 O O   . HOH   F .   ? 0.3298 0.2309 0.3334 -0.0207 0.0176  -0.0494 246 HOH   B O   
6819 O O   . HOH   F .   ? 0.1481 0.1336 0.1655 -0.0022 -0.0081 0.0063  247 HOH   B O   
6820 O O   . HOH   F .   ? 0.2167 0.2345 0.3379 -0.0452 0.0138  -0.0274 248 HOH   B O   
6821 O O   . HOH   F .   ? 0.2195 0.3871 0.2644 -0.0324 -0.0198 0.0568  249 HOH   B O   
6822 O O   . HOH   F .   ? 0.2355 0.1980 0.2055 -0.0331 -0.0574 0.0123  250 HOH   B O   
6823 O O   . HOH   F .   ? 0.5454 0.3355 0.2597 -0.0257 0.0558  -0.0169 251 HOH   B O   
6824 O O   . HOH   F .   ? 0.3012 0.2243 0.3127 0.0816  0.0782  -0.0003 252 HOH   B O   
6825 O O   . HOH   F .   ? 0.2509 0.4518 0.6135 0.1386  -0.0490 -0.1028 253 HOH   B O   
6826 O O   . HOH   F .   ? 0.2091 0.1535 0.2196 -0.0272 -0.0366 0.0249  254 HOH   B O   
6827 O O   . HOH   F .   ? 0.3306 0.1793 0.6389 -0.0173 -0.1317 -0.0293 255 HOH   B O   
6828 O O   . HOH   F .   ? 0.2593 0.2210 0.2669 0.0859  -0.0848 -0.0677 256 HOH   B O   
6829 O O   . HOH   F .   ? 0.3331 0.4819 0.3695 -0.0490 -0.1024 0.1306  257 HOH   B O   
6830 O O   . HOH   F .   ? 0.2456 0.4760 0.6245 0.0277  0.0504  -0.1014 258 HOH   B O   
6831 O O   . HOH   F .   ? 0.1486 0.1768 0.2005 -0.0115 0.0074  0.0058  259 HOH   B O   
6832 O O   . HOH   F .   ? 0.1622 0.1757 0.2964 -0.0172 -0.0169 0.0076  260 HOH   B O   
6833 O O   . HOH   F .   ? 0.2346 0.3300 0.2252 -0.0568 0.0265  0.0495  261 HOH   B O   
6834 O O   . HOH   F .   ? 0.2252 0.1919 0.3705 -0.0138 -0.0586 -0.0448 262 HOH   B O   
6835 O O   . HOH   F .   ? 0.3008 0.4276 0.3176 -0.0948 -0.0320 -0.0483 263 HOH   B O   
6836 O O   . HOH   F .   ? 0.2559 0.2169 0.1918 0.0001  -0.0130 -0.0024 264 HOH   B O   
6837 O O   . HOH   F .   ? 0.4805 0.6662 0.2582 -0.0240 -0.0514 0.0485  265 HOH   B O   
6838 O O   . HOH   F .   ? 0.2207 0.2250 0.2141 0.0083  -0.0020 0.0013  266 HOH   B O   
6839 O O   . HOH   F .   ? 0.2139 0.4314 0.5134 -0.0400 -0.0290 -0.1507 267 HOH   B O   
6840 O O   . HOH   F .   ? 0.1885 0.1861 0.1707 -0.0456 -0.0380 0.0131  268 HOH   B O   
6841 O O   . HOH   F .   ? 0.2617 0.3075 0.2486 -0.0510 -0.0770 0.0069  269 HOH   B O   
6842 O O   . HOH   F .   ? 0.2561 0.2113 0.2856 -0.0565 0.0100  -0.0113 270 HOH   B O   
6843 O O   . HOH   F .   ? 0.2462 0.3936 0.3944 0.0309  0.1174  0.0166  271 HOH   B O   
6844 O O   . HOH   F .   ? 0.4077 0.2881 0.4619 -0.0045 -0.1244 -0.0405 272 HOH   B O   
6845 O O   . HOH   F .   ? 0.1819 0.1392 0.4525 -0.0059 -0.0211 -0.0179 273 HOH   B O   
6846 O O   . HOH   F .   ? 0.2479 0.3798 0.2387 0.1195  -0.0324 -0.0505 274 HOH   B O   
6847 O O   . HOH   F .   ? 0.2389 0.3715 0.3440 -0.0591 0.0537  -0.1260 275 HOH   B O   
6848 O O   . HOH   F .   ? 0.3165 0.3616 0.5922 0.0214  0.0474  -0.0001 276 HOH   B O   
6849 O O   . HOH   F .   ? 0.2361 0.2568 0.2452 -0.0384 -0.0706 -0.0279 277 HOH   B O   
6850 O O   . HOH   F .   ? 0.2029 0.1540 0.2339 -0.0267 -0.0148 0.0091  278 HOH   B O   
6851 O O   . HOH   F .   ? 0.1632 0.1645 0.3477 -0.0126 0.0078  -0.0009 279 HOH   B O   
6852 O O   . HOH   F .   ? 0.2840 0.2085 0.4913 0.0154  0.0581  0.0433  280 HOH   B O   
6853 O O   . HOH   F .   ? 0.4566 0.4018 0.2801 0.0685  -0.0040 -0.1154 281 HOH   B O   
6854 O O   . HOH   F .   ? 0.3533 0.4023 0.4795 0.1172  -0.0769 -0.1303 282 HOH   B O   
6855 O O   . HOH   F .   ? 0.3816 0.2288 0.4276 -0.0962 -0.2132 0.0962  283 HOH   B O   
6856 O O   . HOH   F .   ? 0.5741 0.3711 0.3141 0.2534  0.1107  0.0918  284 HOH   B O   
6857 O O   . HOH   F .   ? 0.4696 0.4981 0.5366 0.0390  -0.1483 -0.0142 285 HOH   B O   
6858 O O   . HOH   F .   ? 0.1719 0.3219 0.4927 0.0262  0.0103  -0.1344 286 HOH   B O   
6859 O O   . HOH   F .   ? 0.3531 0.2955 0.2259 0.0397  -0.0691 -0.0115 287 HOH   B O   
6860 O O   . HOH   F .   ? 0.2963 0.7408 0.7390 0.1628  -0.0793 -0.1032 288 HOH   B O   
6861 O O   . HOH   F .   ? 0.1699 0.1573 0.1890 0.0014  0.0016  0.0033  289 HOH   B O   
6862 O O   . HOH   F .   ? 0.2703 0.4818 0.5127 -0.0881 -0.1236 0.0912  290 HOH   B O   
6863 O O   . HOH   F .   ? 0.2621 0.7034 0.2540 0.0657  -0.0282 -0.0390 291 HOH   B O   
6864 O O   . HOH   F .   ? 0.1676 0.2219 0.1639 -0.0161 -0.0189 0.0078  292 HOH   B O   
6865 O O   . HOH   F .   ? 0.2479 0.2616 0.3129 0.0158  -0.0902 0.0205  293 HOH   B O   
6866 O O   . HOH   F .   ? 0.3437 0.7591 0.3771 0.1550  -0.0619 0.1378  294 HOH   B O   
6867 O O   . HOH   F .   ? 0.3217 0.2756 0.3054 -0.0122 -0.0023 -0.1354 295 HOH   B O   
6868 O O   . HOH   F .   ? 0.4739 0.3890 0.2572 0.1276  -0.0861 0.0399  296 HOH   B O   
6869 O O   . HOH   F .   ? 0.3571 0.2023 0.3750 0.0756  0.1299  0.0446  297 HOH   B O   
6870 O O   . HOH   F .   ? 0.4406 0.3208 0.4609 -0.0554 0.0123  0.1027  298 HOH   B O   
6871 O O   . HOH   F .   ? 0.1795 0.1719 0.2472 0.0107  -0.0005 0.0183  299 HOH   B O   
6872 O O   . HOH   F .   ? 0.2796 0.3522 0.4699 -0.0584 -0.1448 0.1143  300 HOH   B O   
6873 O O   . HOH   F .   ? 0.1763 0.2130 0.3015 0.0200  0.0003  0.0164  301 HOH   B O   
6874 O O   . HOH   F .   ? 0.2806 0.2889 0.3644 -0.0398 0.0939  -0.0786 302 HOH   B O   
6875 O O   . HOH   F .   ? 0.2046 0.2703 0.6512 0.0429  -0.0417 -0.1114 303 HOH   B O   
6876 O O   . HOH   F .   ? 0.4606 0.4797 0.2371 0.0222  0.0921  0.0661  304 HOH   B O   
6877 O O   . HOH   F .   ? 0.4869 0.5088 0.2442 0.1452  -0.0623 -0.0129 305 HOH   B O   
6878 O O   . HOH   F .   ? 0.3286 0.2852 0.5230 -0.0409 -0.0962 0.1191  306 HOH   B O   
6879 O O   . HOH   F .   ? 0.5302 0.3168 0.2527 -0.1789 0.0738  -0.0167 307 HOH   B O   
6880 O O   . HOH   F .   ? 0.2105 0.1690 0.3361 0.0341  -0.0907 0.0008  308 HOH   B O   
6881 O O   . HOH   F .   ? 0.6321 0.5545 0.5158 -0.1072 -0.0127 0.1529  309 HOH   B O   
6882 O O   . HOH   F .   ? 0.3107 0.3705 0.4234 -0.1386 0.1118  -0.0725 310 HOH   B O   
6883 O O   . HOH   F .   ? 0.2532 0.1467 0.2611 -0.0122 -0.0181 0.0330  311 HOH   B O   
6884 O O   . HOH   F .   ? 0.1665 0.1560 0.3126 0.0152  -0.0061 -0.0042 312 HOH   B O   
6885 O O   . HOH   F .   ? 0.2188 0.1688 0.2601 -0.0276 -0.0342 -0.0011 313 HOH   B O   
6886 O O   . HOH   F .   ? 0.1593 0.1945 0.3075 -0.0216 -0.0078 0.0035  314 HOH   B O   
6887 O O   . HOH   F .   ? 0.3523 0.4298 0.7799 -0.0099 -0.0904 0.2316  315 HOH   B O   
6888 O O   . HOH   F .   ? 0.2210 0.3215 0.5131 -0.0174 -0.0349 -0.0306 316 HOH   B O   
6889 O O   . HOH   F .   ? 0.4455 0.3291 0.5195 0.1004  0.2018  0.1834  317 HOH   B O   
6890 O O   . HOH   F .   ? 0.2237 0.1986 0.1910 -0.0081 0.0233  0.0174  318 HOH   B O   
6891 O O   . HOH   F .   ? 0.1655 0.1633 0.3024 -0.0187 -0.0151 -0.0102 319 HOH   B O   
6892 O O   . HOH   F .   ? 0.6380 0.4298 0.4971 0.1272  0.1474  0.0335  320 HOH   B O   
6893 O O   . HOH   F .   ? 0.1807 0.2864 0.2357 -0.0102 -0.0195 0.0652  321 HOH   B O   
6894 O O   . HOH   F .   ? 0.4342 0.2501 0.2894 0.1696  0.1138  0.0480  322 HOH   B O   
6895 O O   . HOH   F .   ? 0.2810 0.2256 0.2424 0.0224  -0.0234 0.0280  323 HOH   B O   
6896 O O   . HOH   F .   ? 0.4469 0.4072 0.5967 0.0733  -0.0034 0.0891  324 HOH   B O   
6897 O O   . HOH   F .   ? 0.6639 0.6942 0.5385 0.3388  -0.0089 -0.0170 325 HOH   B O   
6898 O O   . HOH   F .   ? 0.4442 0.4973 0.2744 0.0676  -0.0431 -0.0712 326 HOH   B O   
6899 O O   . HOH   F .   ? 0.2193 0.6094 0.4766 -0.0759 -0.0229 -0.0532 327 HOH   B O   
6900 O O   . HOH   F .   ? 0.4828 0.2623 0.2910 0.0076  0.0273  0.0909  328 HOH   B O   
6901 O O   . HOH   F .   ? 0.6203 0.4781 0.6329 0.0930  -0.0800 0.1620  329 HOH   B O   
6902 O O   . HOH   F .   ? 0.1968 0.2091 0.2963 0.0358  0.0411  0.0175  330 HOH   B O   
6903 O O   . HOH   F .   ? 0.8128 0.2135 0.2937 0.0254  -0.0623 -0.0027 331 HOH   B O   
6904 O O   . HOH   F .   ? 0.2723 0.1999 0.5135 0.0078  0.0196  0.0321  332 HOH   B O   
6905 O O   . HOH   F .   ? 0.1912 0.2849 0.2873 0.0328  -0.0263 -0.0566 333 HOH   B O   
6906 O O   . HOH   F .   ? 0.2327 0.2452 0.5690 -0.0595 -0.0102 0.1410  334 HOH   B O   
6907 O O   . HOH   F .   ? 0.5421 0.3783 0.3799 -0.0129 0.1180  0.1144  335 HOH   B O   
6908 O O   . HOH   F .   ? 0.6420 0.4974 0.6267 -0.0549 -0.0490 -0.1078 336 HOH   B O   
6909 O O   . HOH   F .   ? 0.5038 0.5369 0.3639 0.0054  -0.1049 0.0260  337 HOH   B O   
6910 O O   . HOH   F .   ? 0.1774 0.1523 0.2409 0.0050  -0.0181 0.0081  338 HOH   B O   
6911 O O   . HOH   F .   ? 0.5120 0.3334 0.3378 0.0726  -0.1222 -0.0840 339 HOH   B O   
6912 O O   . HOH   F .   ? 0.5211 0.3544 0.4400 0.0367  0.0731  -0.1482 340 HOH   B O   
6913 O O   . HOH   F .   ? 0.4430 0.7192 0.3765 -0.0227 -0.0305 0.1921  341 HOH   B O   
6914 O O   . HOH   F .   ? 0.3990 0.6419 0.4174 -0.1121 -0.0956 -0.0795 342 HOH   B O   
6915 O O   . HOH   F .   ? 0.1961 0.6809 0.6681 -0.0203 -0.0955 0.0035  343 HOH   B O   
6916 O O   . HOH   F .   ? 0.7347 0.5699 0.2864 0.0438  -0.0561 0.0958  344 HOH   B O   
6917 O O   . HOH   F .   ? 0.2145 0.2082 0.3080 -0.0024 0.0522  -0.0162 345 HOH   B O   
6918 O O   . HOH   F .   ? 0.5629 0.5213 0.4245 -0.1255 0.0775  0.0935  346 HOH   B O   
6919 O O   . HOH   F .   ? 0.4214 0.5024 0.5808 -0.0162 -0.1061 0.0904  347 HOH   B O   
6920 O O   . HOH   F .   ? 0.2571 0.6165 0.3815 0.1694  -0.0456 -0.1548 348 HOH   B O   
6921 O O   . HOH   F .   ? 0.2888 0.2369 0.5324 -0.0172 -0.0984 -0.0580 349 HOH   B O   
6922 O O   . HOH   F .   ? 0.2233 0.4143 0.5404 0.0264  0.0427  0.0006  350 HOH   B O   
6923 O O   . HOH   F .   ? 0.4518 0.5908 0.6047 0.0256  -0.0083 -0.0790 351 HOH   B O   
6924 O O   . HOH   F .   ? 0.3902 0.2264 0.3470 -0.0831 0.0423  -0.0803 352 HOH   B O   
6925 O O   . HOH   F .   ? 0.4608 0.3348 0.5474 -0.1060 0.1219  0.0752  353 HOH   B O   
6926 O O   . HOH   F .   ? 0.3568 0.4114 0.4643 -0.1310 0.0332  -0.0392 354 HOH   B O   
6927 O O   . HOH   F .   ? 0.3784 0.2887 0.3648 -0.0925 -0.0120 -0.0470 355 HOH   B O   
6928 O O   . HOH   F .   ? 0.5348 0.3782 0.4447 0.0565  0.1337  -0.0721 356 HOH   B O   
6929 O O   . HOH   F .   ? 0.3254 0.2024 0.4141 0.0476  -0.1274 -0.0542 357 HOH   B O   
6930 O O   . HOH   F .   ? 0.5257 0.4884 0.5419 -0.0682 -0.0413 -0.0272 358 HOH   B O   
6931 O O   . HOH   F .   ? 0.5402 0.3314 0.5002 -0.0193 -0.1702 -0.0405 359 HOH   B O   
6932 O O   . HOH   F .   ? 0.4652 0.5119 0.5344 0.1585  -0.1286 0.1789  360 HOH   B O   
6933 O O   . HOH   F .   ? 0.5111 0.4451 0.6712 -0.0188 0.0407  0.1514  361 HOH   B O   
6934 O O   . HOH   F .   ? 0.5032 0.7060 0.3145 0.2544  0.0192  0.0446  362 HOH   B O   
6935 O O   . HOH   F .   ? 0.2349 0.3534 0.6985 -0.0719 -0.0642 -0.0837 363 HOH   B O   
6936 O O   . HOH   F .   ? 0.5331 0.3070 0.5510 -0.1489 -0.0279 0.0187  364 HOH   B O   
6937 O O   . HOH   F .   ? 0.6075 0.4475 0.4417 0.0888  0.0859  0.0612  365 HOH   B O   
6938 O O   . HOH   F .   ? 0.6475 0.2329 0.3439 -0.0164 0.0107  0.0524  366 HOH   B O   
6939 O O   . HOH   F .   ? 0.4840 0.5715 0.3586 0.1563  -0.1311 0.0594  367 HOH   B O   
6940 O O   . HOH   F .   ? 0.5017 0.5527 0.4804 -0.0881 -0.0633 -0.1065 368 HOH   B O   
6941 O O   . HOH   F .   ? 0.7363 0.7972 0.5094 0.2752  -0.1244 0.0987  369 HOH   B O   
6942 O O   . HOH   F .   ? 0.4573 0.5860 0.5417 0.2861  0.1058  0.1554  370 HOH   B O   
6943 O O   . HOH   F .   ? 0.5255 0.3783 0.5813 0.0994  -0.1469 0.0101  371 HOH   B O   
6944 O O   . HOH   F .   ? 0.6946 0.3706 0.3202 -0.1191 -0.1080 -0.0629 372 HOH   B O   
6945 O O   . HOH   F .   ? 0.4066 0.3881 0.4220 0.0641  -0.1360 -0.0421 373 HOH   B O   
6946 O O   . HOH   F .   ? 0.2346 0.5130 0.4341 0.0041  -0.0400 -0.0810 374 HOH   B O   
6947 O O   . HOH   F .   ? 0.4375 0.5101 0.4744 -0.0814 -0.0555 0.0429  375 HOH   B O   
6948 O O   . HOH   F .   ? 0.4378 0.6709 0.6317 0.1346  0.0242  0.2642  376 HOH   B O   
6949 O O   . HOH   F .   ? 0.3201 0.4337 0.2357 0.0445  0.0308  -0.0134 377 HOH   B O   
6950 O O   . HOH   F .   ? 0.7349 0.3987 0.5427 -0.0973 -0.0674 0.0032  378 HOH   B O   
6951 O O   . HOH   F .   ? 0.5650 0.7294 0.4330 -0.1401 0.0199  -0.1495 379 HOH   B O   
6952 O O   . HOH   F .   ? 0.4018 0.4432 0.5251 0.1593  0.0023  -0.0029 380 HOH   B O   
6953 O O   . HOH   F .   ? 0.6220 0.6785 0.6287 -0.0198 0.2196  0.1780  381 HOH   B O   
6954 O O   . HOH   F .   ? 0.3272 0.2587 0.3280 0.0094  0.0184  0.0352  382 HOH   B O   
6955 O O   . HOH   F .   ? 0.4229 0.8397 0.5770 0.0529  0.1965  0.1094  383 HOH   B O   
6956 O O   . HOH   F .   ? 0.6874 0.5791 0.3806 0.2419  0.0566  0.0662  384 HOH   B O   
6957 O O   . HOH   F .   ? 0.6684 0.4451 0.4467 0.1265  0.0868  -0.0400 385 HOH   B O   
6958 O O   . HOH   F .   ? 0.5122 0.4614 0.4806 0.0065  -0.0699 -0.0403 386 HOH   B O   
6959 O O   . HOH   F .   ? 0.2364 0.4347 0.3720 -0.0682 -0.0981 -0.0187 387 HOH   B O   
6960 O O   . HOH   F .   ? 0.4779 0.3590 0.3245 0.0039  0.0588  -0.0263 388 HOH   B O   
6961 O O   . HOH   F .   ? 0.5598 0.4162 0.5505 -0.0510 -0.0156 -0.0080 389 HOH   B O   
6962 O O   . HOH   F .   ? 0.3645 0.2348 0.3633 0.0618  -0.0406 -0.0018 390 HOH   B O   
6963 O O   . HOH   F .   ? 0.4161 0.4205 0.4038 -0.0035 0.0549  0.0286  391 HOH   B O   
6964 O O   . HOH   F .   ? 0.2466 0.4849 0.6683 -0.1487 -0.0393 -0.0017 392 HOH   B O   
6965 O O   . HOH   F .   ? 0.3840 0.2434 0.5299 -0.0381 0.0671  0.0668  393 HOH   B O   
6966 O O   . HOH   F .   ? 0.4711 0.6097 0.3653 0.1749  -0.0462 -0.1085 394 HOH   B O   
6967 O O   . HOH   F .   ? 0.3193 0.3596 0.4276 0.0357  0.0005  -0.0522 395 HOH   B O   
6968 O O   . HOH   F .   ? 0.4593 0.4346 0.4553 0.0439  0.1061  0.0708  396 HOH   B O   
6969 O O   . HOH   F .   ? 0.2116 0.3011 0.5820 -0.0534 -0.0892 0.0358  397 HOH   B O   
6970 O O   . HOH   F .   ? 0.5914 0.6742 0.7380 0.1484  -0.1079 0.2224  398 HOH   B O   
6971 O O   . HOH   F .   ? 0.5754 0.4255 0.3162 -0.2255 -0.0314 0.1121  399 HOH   B O   
6972 O O   . HOH   F .   ? 0.5341 0.5936 0.3760 0.1728  0.0106  -0.0330 400 HOH   B O   
# 
