data_7HD9
# 
_entry.id   7HD9 
# 
_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   7HD9         pdb_00007hd9 10.2210/pdb7hd9/pdb 
WWPDB D_1001407327 ?            ?                   
# 
_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                        7HD9 
_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 '[(1S,3S,4R)-2-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-2-azabicyclo[2.2.1]heptan-3-yl]methanol' 244.292   1   ? ? ? ? 
3 water       nat water                                                                                     18.015    426 ? ? ? ? 
# 
_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 '[(1S,3S,4R)-2-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-2-azabicyclo[2.2.1]heptan-3-yl]methanol' A1A7W 
3 water                                                                                     HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A7W non-polymer         . '[(1S,3S,4R)-2-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-2-azabicyclo[2.2.1]heptan-3-yl]methanol' ? 
'C13 H16 N4 O'   244.292 
ALA   'L-peptide linking' y ALANINE                                                                                   ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                  ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                           ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                  ? 
'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                 ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                           ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                   ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                 ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                     ? 'H2 O' 
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                   ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                    ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                             ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                   ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                    ? 
'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                 ? 
'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                                                  ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                    ? 
'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1A7W 1   201 201  A1A7W LA1 A . 
D 3 HOH   1   301 292  HOH   HOH A . 
D 3 HOH   2   302 393  HOH   HOH A . 
D 3 HOH   3   303 26   HOH   HOH A . 
D 3 HOH   4   304 109  HOH   HOH A . 
D 3 HOH   5   305 625  HOH   HOH A . 
D 3 HOH   6   306 209  HOH   HOH A . 
D 3 HOH   7   307 153  HOH   HOH A . 
D 3 HOH   8   308 229  HOH   HOH A . 
D 3 HOH   9   309 132  HOH   HOH A . 
D 3 HOH   10  310 192  HOH   HOH A . 
D 3 HOH   11  311 196  HOH   HOH A . 
D 3 HOH   12  312 1295 HOH   HOH A . 
D 3 HOH   13  313 1301 HOH   HOH A . 
D 3 HOH   14  314 1283 HOH   HOH A . 
D 3 HOH   15  315 493  HOH   HOH A . 
D 3 HOH   16  316 661  HOH   HOH A . 
D 3 HOH   17  317 124  HOH   HOH A . 
D 3 HOH   18  318 76   HOH   HOH A . 
D 3 HOH   19  319 136  HOH   HOH A . 
D 3 HOH   20  320 461  HOH   HOH A . 
D 3 HOH   21  321 74   HOH   HOH A . 
D 3 HOH   22  322 151  HOH   HOH A . 
D 3 HOH   23  323 93   HOH   HOH A . 
D 3 HOH   24  324 1296 HOH   HOH A . 
D 3 HOH   25  325 236  HOH   HOH A . 
D 3 HOH   26  326 281  HOH   HOH A . 
D 3 HOH   27  327 164  HOH   HOH A . 
D 3 HOH   28  328 140  HOH   HOH A . 
D 3 HOH   29  329 105  HOH   HOH A . 
D 3 HOH   30  330 630  HOH   HOH A . 
D 3 HOH   31  331 169  HOH   HOH A . 
D 3 HOH   32  332 247  HOH   HOH A . 
D 3 HOH   33  333 36   HOH   HOH A . 
D 3 HOH   34  334 396  HOH   HOH A . 
D 3 HOH   35  335 469  HOH   HOH A . 
D 3 HOH   36  336 10   HOH   HOH A . 
D 3 HOH   37  337 241  HOH   HOH A . 
D 3 HOH   38  338 165  HOH   HOH A . 
D 3 HOH   39  339 42   HOH   HOH A . 
D 3 HOH   40  340 18   HOH   HOH A . 
D 3 HOH   41  341 57   HOH   HOH A . 
D 3 HOH   42  342 662  HOH   HOH A . 
D 3 HOH   43  343 9    HOH   HOH A . 
D 3 HOH   44  344 964  HOH   HOH A . 
D 3 HOH   45  345 337  HOH   HOH A . 
D 3 HOH   46  346 366  HOH   HOH A . 
D 3 HOH   47  347 81   HOH   HOH A . 
D 3 HOH   48  348 102  HOH   HOH A . 
D 3 HOH   49  349 218  HOH   HOH A . 
D 3 HOH   50  350 12   HOH   HOH A . 
D 3 HOH   51  351 225  HOH   HOH A . 
D 3 HOH   52  352 33   HOH   HOH A . 
D 3 HOH   53  353 92   HOH   HOH A . 
D 3 HOH   54  354 155  HOH   HOH A . 
D 3 HOH   55  355 1300 HOH   HOH A . 
D 3 HOH   56  356 354  HOH   HOH A . 
D 3 HOH   57  357 381  HOH   HOH A . 
D 3 HOH   58  358 66   HOH   HOH A . 
D 3 HOH   59  359 56   HOH   HOH A . 
D 3 HOH   60  360 19   HOH   HOH A . 
D 3 HOH   61  361 320  HOH   HOH A . 
D 3 HOH   62  362 139  HOH   HOH A . 
D 3 HOH   63  363 21   HOH   HOH A . 
D 3 HOH   64  364 1134 HOH   HOH A . 
D 3 HOH   65  365 86   HOH   HOH A . 
D 3 HOH   66  366 46   HOH   HOH A . 
D 3 HOH   67  367 5    HOH   HOH A . 
D 3 HOH   68  368 5    HOH   HOH A . 
D 3 HOH   69  369 17   HOH   HOH A . 
D 3 HOH   70  370 7    HOH   HOH A . 
D 3 HOH   71  371 138  HOH   HOH A . 
D 3 HOH   72  372 85   HOH   HOH A . 
D 3 HOH   73  373 2    HOH   HOH A . 
D 3 HOH   74  374 1290 HOH   HOH A . 
D 3 HOH   75  375 159  HOH   HOH A . 
D 3 HOH   76  376 405  HOH   HOH A . 
D 3 HOH   77  377 939  HOH   HOH A . 
D 3 HOH   78  378 162  HOH   HOH A . 
D 3 HOH   79  379 1275 HOH   HOH A . 
D 3 HOH   80  380 45   HOH   HOH A . 
D 3 HOH   81  381 4    HOH   HOH A . 
D 3 HOH   82  382 27   HOH   HOH A . 
D 3 HOH   83  383 2    HOH   HOH A . 
D 3 HOH   84  384 409  HOH   HOH A . 
D 3 HOH   85  385 134  HOH   HOH A . 
D 3 HOH   86  386 14   HOH   HOH A . 
D 3 HOH   87  387 1309 HOH   HOH A . 
D 3 HOH   88  388 195  HOH   HOH A . 
D 3 HOH   89  389 35   HOH   HOH A . 
D 3 HOH   90  390 212  HOH   HOH A . 
D 3 HOH   91  391 39   HOH   HOH A . 
D 3 HOH   92  392 49   HOH   HOH A . 
D 3 HOH   93  393 3    HOH   HOH A . 
D 3 HOH   94  394 296  HOH   HOH A . 
D 3 HOH   95  395 186  HOH   HOH A . 
D 3 HOH   96  396 24   HOH   HOH A . 
D 3 HOH   97  397 12   HOH   HOH A . 
D 3 HOH   98  398 83   HOH   HOH A . 
D 3 HOH   99  399 67   HOH   HOH A . 
D 3 HOH   100 400 154  HOH   HOH A . 
D 3 HOH   101 401 148  HOH   HOH A . 
D 3 HOH   102 402 8    HOH   HOH A . 
D 3 HOH   103 403 6    HOH   HOH A . 
D 3 HOH   104 404 34   HOH   HOH A . 
D 3 HOH   105 405 1315 HOH   HOH A . 
D 3 HOH   106 406 68   HOH   HOH A . 
D 3 HOH   107 407 58   HOH   HOH A . 
D 3 HOH   108 408 1289 HOH   HOH A . 
D 3 HOH   109 409 4    HOH   HOH A . 
D 3 HOH   110 410 116  HOH   HOH A . 
D 3 HOH   111 411 51   HOH   HOH A . 
D 3 HOH   112 412 78   HOH   HOH A . 
D 3 HOH   113 413 70   HOH   HOH A . 
D 3 HOH   114 414 303  HOH   HOH A . 
D 3 HOH   115 415 278  HOH   HOH A . 
D 3 HOH   116 416 96   HOH   HOH A . 
D 3 HOH   117 417 17   HOH   HOH A . 
D 3 HOH   118 418 333  HOH   HOH A . 
D 3 HOH   119 419 1313 HOH   HOH A . 
D 3 HOH   120 420 1308 HOH   HOH A . 
D 3 HOH   121 421 1094 HOH   HOH A . 
D 3 HOH   122 422 121  HOH   HOH A . 
D 3 HOH   123 423 1068 HOH   HOH A . 
D 3 HOH   124 424 123  HOH   HOH A . 
D 3 HOH   125 425 7    HOH   HOH A . 
D 3 HOH   126 426 25   HOH   HOH A . 
D 3 HOH   127 427 1310 HOH   HOH A . 
D 3 HOH   128 428 53   HOH   HOH A . 
D 3 HOH   129 429 122  HOH   HOH A . 
D 3 HOH   130 430 582  HOH   HOH A . 
D 3 HOH   131 431 199  HOH   HOH A . 
D 3 HOH   132 432 156  HOH   HOH A . 
D 3 HOH   133 433 115  HOH   HOH A . 
D 3 HOH   134 434 397  HOH   HOH A . 
D 3 HOH   135 435 125  HOH   HOH A . 
D 3 HOH   136 436 95   HOH   HOH A . 
D 3 HOH   137 437 351  HOH   HOH A . 
D 3 HOH   138 438 342  HOH   HOH A . 
D 3 HOH   139 439 1279 HOH   HOH A . 
D 3 HOH   140 440 15   HOH   HOH A . 
D 3 HOH   141 441 1    HOH   HOH A . 
D 3 HOH   142 442 16   HOH   HOH A . 
D 3 HOH   143 443 80   HOH   HOH A . 
D 3 HOH   144 444 1189 HOH   HOH A . 
D 3 HOH   145 445 71   HOH   HOH A . 
D 3 HOH   146 446 1222 HOH   HOH A . 
D 3 HOH   147 447 1238 HOH   HOH A . 
D 3 HOH   148 448 73   HOH   HOH A . 
D 3 HOH   149 449 944  HOH   HOH A . 
D 3 HOH   150 450 94   HOH   HOH A . 
D 3 HOH   151 451 104  HOH   HOH A . 
D 3 HOH   152 452 40   HOH   HOH A . 
D 3 HOH   153 453 188  HOH   HOH A . 
D 3 HOH   154 454 97   HOH   HOH A . 
D 3 HOH   155 455 952  HOH   HOH A . 
D 3 HOH   156 456 79   HOH   HOH A . 
D 3 HOH   157 457 3    HOH   HOH A . 
D 3 HOH   158 458 19   HOH   HOH A . 
D 3 HOH   159 459 1286 HOH   HOH A . 
D 3 HOH   160 460 576  HOH   HOH A . 
D 3 HOH   161 461 330  HOH   HOH A . 
D 3 HOH   162 462 107  HOH   HOH A . 
D 3 HOH   163 463 509  HOH   HOH A . 
D 3 HOH   164 464 726  HOH   HOH A . 
D 3 HOH   165 465 163  HOH   HOH A . 
D 3 HOH   166 466 1119 HOH   HOH A . 
D 3 HOH   167 467 408  HOH   HOH A . 
D 3 HOH   168 468 756  HOH   HOH A . 
D 3 HOH   169 469 319  HOH   HOH A . 
D 3 HOH   170 470 1276 HOH   HOH A . 
D 3 HOH   171 471 6    HOH   HOH A . 
D 3 HOH   172 472 361  HOH   HOH A . 
D 3 HOH   173 473 63   HOH   HOH A . 
D 3 HOH   174 474 126  HOH   HOH A . 
D 3 HOH   175 475 1307 HOH   HOH A . 
D 3 HOH   176 476 556  HOH   HOH A . 
D 3 HOH   177 477 801  HOH   HOH A . 
D 3 HOH   178 478 250  HOH   HOH A . 
D 3 HOH   179 479 521  HOH   HOH A . 
D 3 HOH   180 480 370  HOH   HOH A . 
D 3 HOH   181 481 280  HOH   HOH A . 
D 3 HOH   182 482 711  HOH   HOH A . 
D 3 HOH   183 483 135  HOH   HOH A . 
D 3 HOH   184 484 1287 HOH   HOH A . 
D 3 HOH   185 485 224  HOH   HOH A . 
D 3 HOH   186 486 1306 HOH   HOH A . 
D 3 HOH   187 487 674  HOH   HOH A . 
D 3 HOH   188 488 202  HOH   HOH A . 
D 3 HOH   189 489 919  HOH   HOH A . 
D 3 HOH   190 490 695  HOH   HOH A . 
D 3 HOH   191 491 326  HOH   HOH A . 
D 3 HOH   192 492 318  HOH   HOH A . 
D 3 HOH   193 493 267  HOH   HOH A . 
D 3 HOH   194 494 1314 HOH   HOH A . 
D 3 HOH   195 495 331  HOH   HOH A . 
D 3 HOH   196 496 315  HOH   HOH A . 
D 3 HOH   197 497 1299 HOH   HOH A . 
D 3 HOH   198 498 309  HOH   HOH A . 
D 3 HOH   199 499 941  HOH   HOH A . 
D 3 HOH   200 500 805  HOH   HOH A . 
D 3 HOH   201 501 263  HOH   HOH A . 
D 3 HOH   202 502 152  HOH   HOH A . 
D 3 HOH   203 503 208  HOH   HOH A . 
D 3 HOH   204 504 356  HOH   HOH A . 
D 3 HOH   205 505 11   HOH   HOH A . 
D 3 HOH   206 506 8    HOH   HOH A . 
D 3 HOH   207 507 350  HOH   HOH A . 
D 3 HOH   208 508 1071 HOH   HOH A . 
D 3 HOH   209 509 180  HOH   HOH A . 
D 3 HOH   210 510 13   HOH   HOH A . 
D 3 HOH   211 511 363  HOH   HOH A . 
D 3 HOH   212 512 1284 HOH   HOH A . 
D 3 HOH   213 513 371  HOH   HOH A . 
D 3 HOH   214 514 313  HOH   HOH A . 
D 3 HOH   215 515 18   HOH   HOH A . 
D 3 HOH   216 516 185  HOH   HOH A . 
D 3 HOH   217 517 429  HOH   HOH A . 
D 3 HOH   218 518 772  HOH   HOH A . 
D 3 HOH   219 519 376  HOH   HOH A . 
D 3 HOH   220 520 1074 HOH   HOH A . 
D 3 HOH   221 521 1292 HOH   HOH A . 
D 3 HOH   222 522 346  HOH   HOH A . 
D 3 HOH   223 523 16   HOH   HOH A . 
D 3 HOH   224 524 1078 HOH   HOH A . 
E 3 HOH   1   201 64   HOH   HOH B . 
E 3 HOH   2   202 549  HOH   HOH B . 
E 3 HOH   3   203 240  HOH   HOH B . 
E 3 HOH   4   204 364  HOH   HOH B . 
E 3 HOH   5   205 1249 HOH   HOH B . 
E 3 HOH   6   206 900  HOH   HOH B . 
E 3 HOH   7   207 120  HOH   HOH B . 
E 3 HOH   8   208 232  HOH   HOH B . 
E 3 HOH   9   209 452  HOH   HOH B . 
E 3 HOH   10  210 654  HOH   HOH B . 
E 3 HOH   11  211 531  HOH   HOH B . 
E 3 HOH   12  212 358  HOH   HOH B . 
E 3 HOH   13  213 353  HOH   HOH B . 
E 3 HOH   14  214 398  HOH   HOH B . 
E 3 HOH   15  215 264  HOH   HOH B . 
E 3 HOH   16  216 758  HOH   HOH B . 
E 3 HOH   17  217 50   HOH   HOH B . 
E 3 HOH   18  218 444  HOH   HOH B . 
E 3 HOH   19  219 205  HOH   HOH B . 
E 3 HOH   20  220 75   HOH   HOH B . 
E 3 HOH   21  221 15   HOH   HOH B . 
E 3 HOH   22  222 166  HOH   HOH B . 
E 3 HOH   23  223 332  HOH   HOH B . 
E 3 HOH   24  224 743  HOH   HOH B . 
E 3 HOH   25  225 54   HOH   HOH B . 
E 3 HOH   26  226 276  HOH   HOH B . 
E 3 HOH   27  227 391  HOH   HOH B . 
E 3 HOH   28  228 325  HOH   HOH B . 
E 3 HOH   29  229 82   HOH   HOH B . 
E 3 HOH   30  230 131  HOH   HOH B . 
E 3 HOH   31  231 172  HOH   HOH B . 
E 3 HOH   32  232 343  HOH   HOH B . 
E 3 HOH   33  233 723  HOH   HOH B . 
E 3 HOH   34  234 127  HOH   HOH B . 
E 3 HOH   35  235 110  HOH   HOH B . 
E 3 HOH   36  236 181  HOH   HOH B . 
E 3 HOH   37  237 133  HOH   HOH B . 
E 3 HOH   38  238 1140 HOH   HOH B . 
E 3 HOH   39  239 1278 HOH   HOH B . 
E 3 HOH   40  240 282  HOH   HOH B . 
E 3 HOH   41  241 60   HOH   HOH B . 
E 3 HOH   42  242 300  HOH   HOH B . 
E 3 HOH   43  243 41   HOH   HOH B . 
E 3 HOH   44  244 69   HOH   HOH B . 
E 3 HOH   45  245 272  HOH   HOH B . 
E 3 HOH   46  246 1    HOH   HOH B . 
E 3 HOH   47  247 52   HOH   HOH B . 
E 3 HOH   48  248 9    HOH   HOH B . 
E 3 HOH   49  249 14   HOH   HOH B . 
E 3 HOH   50  250 30   HOH   HOH B . 
E 3 HOH   51  251 144  HOH   HOH B . 
E 3 HOH   52  252 72   HOH   HOH B . 
E 3 HOH   53  253 128  HOH   HOH B . 
E 3 HOH   54  254 129  HOH   HOH B . 
E 3 HOH   55  255 31   HOH   HOH B . 
E 3 HOH   56  256 59   HOH   HOH B . 
E 3 HOH   57  257 1312 HOH   HOH B . 
E 3 HOH   58  258 62   HOH   HOH B . 
E 3 HOH   59  259 302  HOH   HOH B . 
E 3 HOH   60  260 1305 HOH   HOH B . 
E 3 HOH   61  261 47   HOH   HOH B . 
E 3 HOH   62  262 231  HOH   HOH B . 
E 3 HOH   63  263 10   HOH   HOH B . 
E 3 HOH   64  264 221  HOH   HOH B . 
E 3 HOH   65  265 150  HOH   HOH B . 
E 3 HOH   66  266 243  HOH   HOH B . 
E 3 HOH   67  267 242  HOH   HOH B . 
E 3 HOH   68  268 143  HOH   HOH B . 
E 3 HOH   69  269 20   HOH   HOH B . 
E 3 HOH   70  270 175  HOH   HOH B . 
E 3 HOH   71  271 84   HOH   HOH B . 
E 3 HOH   72  272 103  HOH   HOH B . 
E 3 HOH   73  273 61   HOH   HOH B . 
E 3 HOH   74  274 220  HOH   HOH B . 
E 3 HOH   75  275 11   HOH   HOH B . 
E 3 HOH   76  276 117  HOH   HOH B . 
E 3 HOH   77  277 114  HOH   HOH B . 
E 3 HOH   78  278 287  HOH   HOH B . 
E 3 HOH   79  279 22   HOH   HOH B . 
E 3 HOH   80  280 271  HOH   HOH B . 
E 3 HOH   81  281 1285 HOH   HOH B . 
E 3 HOH   82  282 347  HOH   HOH B . 
E 3 HOH   83  283 147  HOH   HOH B . 
E 3 HOH   84  284 416  HOH   HOH B . 
E 3 HOH   85  285 43   HOH   HOH B . 
E 3 HOH   86  286 252  HOH   HOH B . 
E 3 HOH   87  287 1066 HOH   HOH B . 
E 3 HOH   88  288 1277 HOH   HOH B . 
E 3 HOH   89  289 77   HOH   HOH B . 
E 3 HOH   90  290 88   HOH   HOH B . 
E 3 HOH   91  291 106  HOH   HOH B . 
E 3 HOH   92  292 89   HOH   HOH B . 
E 3 HOH   93  293 13   HOH   HOH B . 
E 3 HOH   94  294 235  HOH   HOH B . 
E 3 HOH   95  295 137  HOH   HOH B . 
E 3 HOH   96  296 387  HOH   HOH B . 
E 3 HOH   97  297 311  HOH   HOH B . 
E 3 HOH   98  298 316  HOH   HOH B . 
E 3 HOH   99  299 99   HOH   HOH B . 
E 3 HOH   100 300 299  HOH   HOH B . 
E 3 HOH   101 301 38   HOH   HOH B . 
E 3 HOH   102 302 1106 HOH   HOH B . 
E 3 HOH   103 303 112  HOH   HOH B . 
E 3 HOH   104 304 182  HOH   HOH B . 
E 3 HOH   105 305 216  HOH   HOH B . 
E 3 HOH   106 306 160  HOH   HOH B . 
E 3 HOH   107 307 297  HOH   HOH B . 
E 3 HOH   108 308 32   HOH   HOH B . 
E 3 HOH   109 309 142  HOH   HOH B . 
E 3 HOH   110 310 215  HOH   HOH B . 
E 3 HOH   111 311 635  HOH   HOH B . 
E 3 HOH   112 312 37   HOH   HOH B . 
E 3 HOH   113 313 170  HOH   HOH B . 
E 3 HOH   114 314 118  HOH   HOH B . 
E 3 HOH   115 315 341  HOH   HOH B . 
E 3 HOH   116 316 101  HOH   HOH B . 
E 3 HOH   117 317 48   HOH   HOH B . 
E 3 HOH   118 318 44   HOH   HOH B . 
E 3 HOH   119 319 91   HOH   HOH B . 
E 3 HOH   120 320 207  HOH   HOH B . 
E 3 HOH   121 321 1274 HOH   HOH B . 
E 3 HOH   122 322 197  HOH   HOH B . 
E 3 HOH   123 323 23   HOH   HOH B . 
E 3 HOH   124 324 177  HOH   HOH B . 
E 3 HOH   125 325 1294 HOH   HOH B . 
E 3 HOH   126 326 28   HOH   HOH B . 
E 3 HOH   127 327 29   HOH   HOH B . 
E 3 HOH   128 328 141  HOH   HOH B . 
E 3 HOH   129 329 100  HOH   HOH B . 
E 3 HOH   130 330 334  HOH   HOH B . 
E 3 HOH   131 331 1291 HOH   HOH B . 
E 3 HOH   132 332 98   HOH   HOH B . 
E 3 HOH   133 333 717  HOH   HOH B . 
E 3 HOH   134 334 1126 HOH   HOH B . 
E 3 HOH   135 335 704  HOH   HOH B . 
E 3 HOH   136 336 161  HOH   HOH B . 
E 3 HOH   137 337 55   HOH   HOH B . 
E 3 HOH   138 338 445  HOH   HOH B . 
E 3 HOH   139 339 234  HOH   HOH B . 
E 3 HOH   140 340 1293 HOH   HOH B . 
E 3 HOH   141 341 65   HOH   HOH B . 
E 3 HOH   142 342 362  HOH   HOH B . 
E 3 HOH   143 343 339  HOH   HOH B . 
E 3 HOH   144 344 619  HOH   HOH B . 
E 3 HOH   145 345 178  HOH   HOH B . 
E 3 HOH   146 346 87   HOH   HOH B . 
E 3 HOH   147 347 90   HOH   HOH B . 
E 3 HOH   148 348 463  HOH   HOH B . 
E 3 HOH   149 349 1304 HOH   HOH B . 
E 3 HOH   150 350 960  HOH   HOH B . 
E 3 HOH   151 351 191  HOH   HOH B . 
E 3 HOH   152 352 1280 HOH   HOH B . 
E 3 HOH   153 353 1046 HOH   HOH B . 
E 3 HOH   154 354 335  HOH   HOH B . 
E 3 HOH   155 355 203  HOH   HOH B . 
E 3 HOH   156 356 623  HOH   HOH B . 
E 3 HOH   157 357 304  HOH   HOH B . 
E 3 HOH   158 358 541  HOH   HOH B . 
E 3 HOH   159 359 290  HOH   HOH B . 
E 3 HOH   160 360 1077 HOH   HOH B . 
E 3 HOH   161 361 718  HOH   HOH B . 
E 3 HOH   162 362 389  HOH   HOH B . 
E 3 HOH   163 363 1072 HOH   HOH B . 
E 3 HOH   164 364 283  HOH   HOH B . 
E 3 HOH   165 365 479  HOH   HOH B . 
E 3 HOH   166 366 291  HOH   HOH B . 
E 3 HOH   167 367 898  HOH   HOH B . 
E 3 HOH   168 368 373  HOH   HOH B . 
E 3 HOH   169 369 340  HOH   HOH B . 
E 3 HOH   170 370 615  HOH   HOH B . 
E 3 HOH   171 371 1316 HOH   HOH B . 
E 3 HOH   172 372 667  HOH   HOH B . 
E 3 HOH   173 373 1303 HOH   HOH B . 
E 3 HOH   174 374 190  HOH   HOH B . 
E 3 HOH   175 375 310  HOH   HOH B . 
E 3 HOH   176 376 1173 HOH   HOH B . 
E 3 HOH   177 377 431  HOH   HOH B . 
E 3 HOH   178 378 149  HOH   HOH B . 
E 3 HOH   179 379 183  HOH   HOH B . 
E 3 HOH   180 380 1000 HOH   HOH B . 
E 3 HOH   181 381 418  HOH   HOH B . 
E 3 HOH   182 382 1311 HOH   HOH B . 
E 3 HOH   183 383 1163 HOH   HOH B . 
E 3 HOH   184 384 424  HOH   HOH B . 
E 3 HOH   185 385 176  HOH   HOH B . 
E 3 HOH   186 386 491  HOH   HOH B . 
E 3 HOH   187 387 265  HOH   HOH B . 
E 3 HOH   188 388 1298 HOH   HOH B . 
E 3 HOH   189 389 981  HOH   HOH B . 
E 3 HOH   190 390 470  HOH   HOH B . 
E 3 HOH   191 391 248  HOH   HOH B . 
E 3 HOH   192 392 184  HOH   HOH B . 
E 3 HOH   193 393 360  HOH   HOH B . 
E 3 HOH   194 394 410  HOH   HOH B . 
E 3 HOH   195 395 355  HOH   HOH B . 
E 3 HOH   196 396 314  HOH   HOH B . 
E 3 HOH   197 397 566  HOH   HOH B . 
E 3 HOH   198 398 274  HOH   HOH B . 
E 3 HOH   199 399 157  HOH   HOH B . 
E 3 HOH   200 400 321  HOH   HOH B . 
E 3 HOH   201 401 792  HOH   HOH B . 
E 3 HOH   202 402 558  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           7HD9 
_cell.length_a           88.873 
_cell.length_b           88.873 
_cell.length_c           39.440 
_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                         7HD9 
_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          7HD9 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.67 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HD9 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.440 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   156262 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.800 
_reflns.pdbx_Rmerge_I_obs            0.061 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        11.500 
_reflns.B_iso_Wilson_estimate        11.930 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.066 
_reflns.pdbx_Rpim_I_all              0.026 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1004218 
_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 1.020 1.040  ? 41150 7428 ? 1.650 ? ? ? 5.500 ? 0.700  ? ? ? ? ? ? 96.000 1.821 0.755 0.496 
1 2 5.590 44.440 ? 7123  1038 ? 0.031 ? ? ? 6.900 ? 41.600 ? ? ? ? ? ? 99.900 0.033 0.012 0.999 
# 
_refine.entry_id                                 7HD9 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             44.4400 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.7500 
_refine.ls_number_reflns_obs                     156157 
_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                          0.1499 
_refine.ls_R_factor_R_work                       0.1492 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1631 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7533 
_refine.ls_number_reflns_R_work                  148624 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.0761 
_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                            0.1500 
_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                                78.290 
_refine.B_iso_min                                8.570 
_refine.pdbx_overall_phase_error                 17.8800 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0200 
_refine_hist.d_res_low                        44.4400 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.number_atoms_solvent             426 
_refine_hist.number_atoms_total               3002 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           12.73 
_refine_hist.pdbx_B_iso_mean_solvent          31.52 
_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 
1.0200 1.0300  30 94.0000  4724 . 0.4877 0.4904 . 197 0.0000 4921 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 4937 . 0.4173 0.4125 . 281 0.0000 5218 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 4893 . 0.3485 0.3613 . 276 0.0000 5169 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 4923 . 0.3049 0.3342 . 277 0.0000 5200 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 4912 . 0.2651 0.3063 . 243 0.0000 5155 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 4965 . 0.2361 0.2703 . 226 0.0000 5191 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 100.0000 4895 . 0.2072 0.2332 . 272 0.0000 5167 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5010 . 0.1910 0.2167 . 218 0.0000 5228 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 4919 . 0.1773 0.2137 . 240 0.0000 5159 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 4960 . 0.1577 0.1872 . 259 0.0000 5219 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 4929 . 0.1471 0.1751 . 251 0.0000 5180 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 4875 . 0.1415 0.1697 . 268 0.0000 5143 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5057 . 0.1366 0.1638 . 221 0.0000 5278 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 4915 . 0.1402 0.1754 . 243 0.0000 5158 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 4911 . 0.1436 0.1611 . 252 0.0000 5163 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 4968 . 0.1412 0.1654 . 270 0.0000 5238 . 'X-RAY DIFFRACTION' 
1.3200 1.3500  30 100.0000 4949 . 0.1440 0.1670 . 239 0.0000 5188 . 'X-RAY DIFFRACTION' 
1.3500 1.3800  30 100.0000 4923 . 0.1335 0.1658 . 265 0.0000 5188 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 4985 . 0.1252 0.1561 . 239 0.0000 5224 . 'X-RAY DIFFRACTION' 
1.4300 1.4700  30 100.0000 4971 . 0.1207 0.1403 . 244 0.0000 5215 . 'X-RAY DIFFRACTION' 
1.4700 1.5200  30 100.0000 4971 . 0.1170 0.1184 . 245 0.0000 5216 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 4958 . 0.1193 0.1337 . 261 0.0000 5219 . 'X-RAY DIFFRACTION' 
1.5900 1.6600  30 100.0000 4935 . 0.1199 0.1353 . 268 0.0000 5203 . 'X-RAY DIFFRACTION' 
1.6600 1.7400  30 100.0000 5035 . 0.1262 0.1479 . 200 0.0000 5235 . 'X-RAY DIFFRACTION' 
1.7400 1.8500  30 100.0000 4944 . 0.1277 0.1404 . 286 0.0000 5230 . 'X-RAY DIFFRACTION' 
1.8500 2.0000  30 100.0000 4992 . 0.1350 0.1294 . 251 0.0000 5243 . 'X-RAY DIFFRACTION' 
2.0000 2.2000  30 100.0000 4946 . 0.1370 0.1444 . 288 0.0000 5234 . 'X-RAY DIFFRACTION' 
2.2000 2.5200  30 100.0000 5015 . 0.1384 0.1436 . 248 0.0000 5263 . 'X-RAY DIFFRACTION' 
2.5200 3.1700  30 100.0000 5026 . 0.1523 0.1682 . 253 0.0000 5279 . 'X-RAY DIFFRACTION' 
3.1700 44.4400 30 100.0000 5181 . 0.1540 0.1681 . 252 0.0000 5433 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HD9 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003713' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HD9 
_struct_keywords.pdbx_keywords   'Viral Protein, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HD9 A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HD9 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 7HD9 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HD9 MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HD9 SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HD9 MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D 
2 1 B,E   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HD9 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 56.07 -132.87 
2 1 HIS A 86  ? ? 55.53 -132.87 
3 1 SER A 128 ? B 71.74 -0.21   
4 1 ALA A 134 ? B 2.65  129.44  
5 1 HIS B 86  ? ? 57.56 -127.79 
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 521 ? 5.85 . 
2 1 O ? A HOH 522 ? 5.93 . 
3 1 O B A HOH 523 ? 5.96 . 
4 1 O ? A HOH 524 ? 7.61 . 
5 1 O ? B HOH 402 ? 6.56 . 
# 
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 
A1A7W N2   N Y N 1   
A1A7W C3   C N R 2   
A1A7W C6   C N S 3   
A1A7W C9   C Y N 4   
A1A7W C12  C Y N 5   
A1A7W C1   C N N 6   
A1A7W C10  C Y N 7   
A1A7W C11  C Y N 8   
A1A7W C13  C N N 9   
A1A7W C2   C N S 10  
A1A7W C4   C N N 11  
A1A7W C5   C N N 12  
A1A7W C7   C Y N 13  
A1A7W C8   C Y N 14  
A1A7W N1   N N N 15  
A1A7W N3   N Y N 16  
A1A7W N4   N Y N 17  
A1A7W O1   O N N 18  
A1A7W H13  H N N 19  
A1A7W H2   H N N 20  
A1A7W H3   H N N 21  
A1A7W H11  H N N 22  
A1A7W H14  H N N 23  
A1A7W H5   H N N 24  
A1A7W H6   H N N 25  
A1A7W H12  H N N 26  
A1A7W H15  H N N 27  
A1A7W H16  H N N 28  
A1A7W H1   H N N 29  
A1A7W H8   H N N 30  
A1A7W H7   H N N 31  
A1A7W H9   H N N 32  
A1A7W H10  H N N 33  
A1A7W H4   H N N 34  
ALA   N    N N N 35  
ALA   CA   C N S 36  
ALA   C    C N N 37  
ALA   O    O N N 38  
ALA   CB   C N N 39  
ALA   OXT  O N N 40  
ALA   H    H N N 41  
ALA   H2   H N N 42  
ALA   HA   H N N 43  
ALA   HB1  H N N 44  
ALA   HB2  H N N 45  
ALA   HB3  H N N 46  
ALA   HXT  H N N 47  
ARG   N    N N N 48  
ARG   CA   C N S 49  
ARG   C    C N N 50  
ARG   O    O N N 51  
ARG   CB   C N N 52  
ARG   CG   C N N 53  
ARG   CD   C N N 54  
ARG   NE   N N N 55  
ARG   CZ   C N N 56  
ARG   NH1  N N N 57  
ARG   NH2  N N N 58  
ARG   OXT  O N N 59  
ARG   H    H N N 60  
ARG   H2   H N N 61  
ARG   HA   H N N 62  
ARG   HB2  H N N 63  
ARG   HB3  H N N 64  
ARG   HG2  H N N 65  
ARG   HG3  H N N 66  
ARG   HD2  H N N 67  
ARG   HD3  H N N 68  
ARG   HE   H N N 69  
ARG   HH11 H N N 70  
ARG   HH12 H N N 71  
ARG   HH21 H N N 72  
ARG   HH22 H N N 73  
ARG   HXT  H N N 74  
ASN   N    N N N 75  
ASN   CA   C N S 76  
ASN   C    C N N 77  
ASN   O    O N N 78  
ASN   CB   C N N 79  
ASN   CG   C N N 80  
ASN   OD1  O N N 81  
ASN   ND2  N N N 82  
ASN   OXT  O N N 83  
ASN   H    H N N 84  
ASN   H2   H N N 85  
ASN   HA   H N N 86  
ASN   HB2  H N N 87  
ASN   HB3  H N N 88  
ASN   HD21 H N N 89  
ASN   HD22 H N N 90  
ASN   HXT  H N N 91  
ASP   N    N N N 92  
ASP   CA   C N S 93  
ASP   C    C N N 94  
ASP   O    O N N 95  
ASP   CB   C N N 96  
ASP   CG   C N N 97  
ASP   OD1  O N N 98  
ASP   OD2  O N N 99  
ASP   OXT  O N N 100 
ASP   H    H N N 101 
ASP   H2   H N N 102 
ASP   HA   H N N 103 
ASP   HB2  H N N 104 
ASP   HB3  H N N 105 
ASP   HD2  H N N 106 
ASP   HXT  H N N 107 
CYS   N    N N N 108 
CYS   CA   C N R 109 
CYS   C    C N N 110 
CYS   O    O N N 111 
CYS   CB   C N N 112 
CYS   SG   S N N 113 
CYS   OXT  O N N 114 
CYS   H    H N N 115 
CYS   H2   H N N 116 
CYS   HA   H N N 117 
CYS   HB2  H N N 118 
CYS   HB3  H N N 119 
CYS   HG   H N N 120 
CYS   HXT  H N N 121 
GLN   N    N N N 122 
GLN   CA   C N S 123 
GLN   C    C N N 124 
GLN   O    O N N 125 
GLN   CB   C N N 126 
GLN   CG   C N N 127 
GLN   CD   C N N 128 
GLN   OE1  O N N 129 
GLN   NE2  N N N 130 
GLN   OXT  O N N 131 
GLN   H    H N N 132 
GLN   H2   H N N 133 
GLN   HA   H N N 134 
GLN   HB2  H N N 135 
GLN   HB3  H N N 136 
GLN   HG2  H N N 137 
GLN   HG3  H N N 138 
GLN   HE21 H N N 139 
GLN   HE22 H N N 140 
GLN   HXT  H N N 141 
GLU   N    N N N 142 
GLU   CA   C N S 143 
GLU   C    C N N 144 
GLU   O    O N N 145 
GLU   CB   C N N 146 
GLU   CG   C N N 147 
GLU   CD   C N N 148 
GLU   OE1  O N N 149 
GLU   OE2  O N N 150 
GLU   OXT  O N N 151 
GLU   H    H N N 152 
GLU   H2   H N N 153 
GLU   HA   H N N 154 
GLU   HB2  H N N 155 
GLU   HB3  H N N 156 
GLU   HG2  H N N 157 
GLU   HG3  H N N 158 
GLU   HE2  H N N 159 
GLU   HXT  H N N 160 
GLY   N    N N N 161 
GLY   CA   C N N 162 
GLY   C    C N N 163 
GLY   O    O N N 164 
GLY   OXT  O N N 165 
GLY   H    H N N 166 
GLY   H2   H N N 167 
GLY   HA2  H N N 168 
GLY   HA3  H N N 169 
GLY   HXT  H N N 170 
HIS   N    N N N 171 
HIS   CA   C N S 172 
HIS   C    C N N 173 
HIS   O    O N N 174 
HIS   CB   C N N 175 
HIS   CG   C Y N 176 
HIS   ND1  N Y N 177 
HIS   CD2  C Y N 178 
HIS   CE1  C Y N 179 
HIS   NE2  N Y N 180 
HIS   OXT  O N N 181 
HIS   H    H N N 182 
HIS   H2   H N N 183 
HIS   HA   H N N 184 
HIS   HB2  H N N 185 
HIS   HB3  H N N 186 
HIS   HD1  H N N 187 
HIS   HD2  H N N 188 
HIS   HE1  H N N 189 
HIS   HE2  H N N 190 
HIS   HXT  H N N 191 
HOH   O    O N N 192 
HOH   H1   H N N 193 
HOH   H2   H N N 194 
ILE   N    N N N 195 
ILE   CA   C N S 196 
ILE   C    C N N 197 
ILE   O    O N N 198 
ILE   CB   C N S 199 
ILE   CG1  C N N 200 
ILE   CG2  C N N 201 
ILE   CD1  C N N 202 
ILE   OXT  O N N 203 
ILE   H    H N N 204 
ILE   H2   H N N 205 
ILE   HA   H N N 206 
ILE   HB   H N N 207 
ILE   HG12 H N N 208 
ILE   HG13 H N N 209 
ILE   HG21 H N N 210 
ILE   HG22 H N N 211 
ILE   HG23 H N N 212 
ILE   HD11 H N N 213 
ILE   HD12 H N N 214 
ILE   HD13 H N N 215 
ILE   HXT  H N N 216 
LEU   N    N N N 217 
LEU   CA   C N S 218 
LEU   C    C N N 219 
LEU   O    O N N 220 
LEU   CB   C N N 221 
LEU   CG   C N N 222 
LEU   CD1  C N N 223 
LEU   CD2  C N N 224 
LEU   OXT  O N N 225 
LEU   H    H N N 226 
LEU   H2   H N N 227 
LEU   HA   H N N 228 
LEU   HB2  H N N 229 
LEU   HB3  H N N 230 
LEU   HG   H N N 231 
LEU   HD11 H N N 232 
LEU   HD12 H N N 233 
LEU   HD13 H N N 234 
LEU   HD21 H N N 235 
LEU   HD22 H N N 236 
LEU   HD23 H N N 237 
LEU   HXT  H N N 238 
LYS   N    N N N 239 
LYS   CA   C N S 240 
LYS   C    C N N 241 
LYS   O    O N N 242 
LYS   CB   C N N 243 
LYS   CG   C N N 244 
LYS   CD   C N N 245 
LYS   CE   C N N 246 
LYS   NZ   N N N 247 
LYS   OXT  O N N 248 
LYS   H    H N N 249 
LYS   H2   H N N 250 
LYS   HA   H N N 251 
LYS   HB2  H N N 252 
LYS   HB3  H N N 253 
LYS   HG2  H N N 254 
LYS   HG3  H N N 255 
LYS   HD2  H N N 256 
LYS   HD3  H N N 257 
LYS   HE2  H N N 258 
LYS   HE3  H N N 259 
LYS   HZ1  H N N 260 
LYS   HZ2  H N N 261 
LYS   HZ3  H N N 262 
LYS   HXT  H N N 263 
MET   N    N N N 264 
MET   CA   C N S 265 
MET   C    C N N 266 
MET   O    O N N 267 
MET   CB   C N N 268 
MET   CG   C N N 269 
MET   SD   S N N 270 
MET   CE   C N N 271 
MET   OXT  O N N 272 
MET   H    H N N 273 
MET   H2   H N N 274 
MET   HA   H N N 275 
MET   HB2  H N N 276 
MET   HB3  H N N 277 
MET   HG2  H N N 278 
MET   HG3  H N N 279 
MET   HE1  H N N 280 
MET   HE2  H N N 281 
MET   HE3  H N N 282 
MET   HXT  H N N 283 
PHE   N    N N N 284 
PHE   CA   C N S 285 
PHE   C    C N N 286 
PHE   O    O N N 287 
PHE   CB   C N N 288 
PHE   CG   C Y N 289 
PHE   CD1  C Y N 290 
PHE   CD2  C Y N 291 
PHE   CE1  C Y N 292 
PHE   CE2  C Y N 293 
PHE   CZ   C Y N 294 
PHE   OXT  O N N 295 
PHE   H    H N N 296 
PHE   H2   H N N 297 
PHE   HA   H N N 298 
PHE   HB2  H N N 299 
PHE   HB3  H N N 300 
PHE   HD1  H N N 301 
PHE   HD2  H N N 302 
PHE   HE1  H N N 303 
PHE   HE2  H N N 304 
PHE   HZ   H N N 305 
PHE   HXT  H N N 306 
PRO   N    N N N 307 
PRO   CA   C N S 308 
PRO   C    C N N 309 
PRO   O    O N N 310 
PRO   CB   C N N 311 
PRO   CG   C N N 312 
PRO   CD   C N N 313 
PRO   OXT  O N N 314 
PRO   H    H N N 315 
PRO   HA   H N N 316 
PRO   HB2  H N N 317 
PRO   HB3  H N N 318 
PRO   HG2  H N N 319 
PRO   HG3  H N N 320 
PRO   HD2  H N N 321 
PRO   HD3  H N N 322 
PRO   HXT  H N N 323 
SER   N    N N N 324 
SER   CA   C N S 325 
SER   C    C N N 326 
SER   O    O N N 327 
SER   CB   C N N 328 
SER   OG   O N N 329 
SER   OXT  O N N 330 
SER   H    H N N 331 
SER   H2   H N N 332 
SER   HA   H N N 333 
SER   HB2  H N N 334 
SER   HB3  H N N 335 
SER   HG   H N N 336 
SER   HXT  H N N 337 
THR   N    N N N 338 
THR   CA   C N S 339 
THR   C    C N N 340 
THR   O    O N N 341 
THR   CB   C N R 342 
THR   OG1  O N N 343 
THR   CG2  C N N 344 
THR   OXT  O N N 345 
THR   H    H N N 346 
THR   H2   H N N 347 
THR   HA   H N N 348 
THR   HB   H N N 349 
THR   HG1  H N N 350 
THR   HG21 H N N 351 
THR   HG22 H N N 352 
THR   HG23 H N N 353 
THR   HXT  H N N 354 
TYR   N    N N N 355 
TYR   CA   C N S 356 
TYR   C    C N N 357 
TYR   O    O N N 358 
TYR   CB   C N N 359 
TYR   CG   C Y N 360 
TYR   CD1  C Y N 361 
TYR   CD2  C Y N 362 
TYR   CE1  C Y N 363 
TYR   CE2  C Y N 364 
TYR   CZ   C Y N 365 
TYR   OH   O N N 366 
TYR   OXT  O N N 367 
TYR   H    H N N 368 
TYR   H2   H N N 369 
TYR   HA   H N N 370 
TYR   HB2  H N N 371 
TYR   HB3  H N N 372 
TYR   HD1  H N N 373 
TYR   HD2  H N N 374 
TYR   HE1  H N N 375 
TYR   HE2  H N N 376 
TYR   HH   H N N 377 
TYR   HXT  H N N 378 
VAL   N    N N N 379 
VAL   CA   C N S 380 
VAL   C    C N N 381 
VAL   O    O N N 382 
VAL   CB   C N N 383 
VAL   CG1  C N N 384 
VAL   CG2  C N N 385 
VAL   OXT  O N N 386 
VAL   H    H N N 387 
VAL   H2   H N N 388 
VAL   HA   H N N 389 
VAL   HB   H N N 390 
VAL   HG11 H N N 391 
VAL   HG12 H N N 392 
VAL   HG13 H N N 393 
VAL   HG21 H N N 394 
VAL   HG22 H N N 395 
VAL   HG23 H N N 396 
VAL   HXT  H N N 397 
# 
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 
A1A7W C4  C3   sing N N 1   
A1A7W C4  C5   sing N N 2   
A1A7W C3  C13  sing N N 3   
A1A7W C3  C2   sing N N 4   
A1A7W C5  C6   sing N N 5   
A1A7W O1  C1   sing N N 6   
A1A7W C13 C6   sing N N 7   
A1A7W C1  C2   sing N N 8   
A1A7W C6  N1   sing N N 9   
A1A7W C2  N1   sing N N 10  
A1A7W N1  C7   sing N N 11  
A1A7W C7  N4   doub Y N 12  
A1A7W C7  C8   sing Y N 13  
A1A7W C9  C8   sing Y N 14  
A1A7W C9  C10  doub Y N 15  
A1A7W N4  C12  sing Y N 16  
A1A7W C8  C11  doub Y N 17  
A1A7W C10 N2   sing Y N 18  
A1A7W C12 N3   doub Y N 19  
A1A7W C11 N2   sing Y N 20  
A1A7W C11 N3   sing Y N 21  
A1A7W N2  H13  sing N N 22  
A1A7W C3  H2   sing N N 23  
A1A7W C6  H3   sing N N 24  
A1A7W C9  H11  sing N N 25  
A1A7W C12 H14  sing N N 26  
A1A7W C1  H5   sing N N 27  
A1A7W C1  H6   sing N N 28  
A1A7W C10 H12  sing N N 29  
A1A7W C13 H15  sing N N 30  
A1A7W C13 H16  sing N N 31  
A1A7W C2  H1   sing N N 32  
A1A7W C4  H8   sing N N 33  
A1A7W C4  H7   sing N N 34  
A1A7W C5  H9   sing N N 35  
A1A7W C5  H10  sing N N 36  
A1A7W O1  H4   sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
GLN   N   CA   sing N N 120 
GLN   N   H    sing N N 121 
GLN   N   H2   sing N N 122 
GLN   CA  C    sing N N 123 
GLN   CA  CB   sing N N 124 
GLN   CA  HA   sing N N 125 
GLN   C   O    doub N N 126 
GLN   C   OXT  sing N N 127 
GLN   CB  CG   sing N N 128 
GLN   CB  HB2  sing N N 129 
GLN   CB  HB3  sing N N 130 
GLN   CG  CD   sing N N 131 
GLN   CG  HG2  sing N N 132 
GLN   CG  HG3  sing N N 133 
GLN   CD  OE1  doub N N 134 
GLN   CD  NE2  sing N N 135 
GLN   NE2 HE21 sing N N 136 
GLN   NE2 HE22 sing N N 137 
GLN   OXT HXT  sing N N 138 
GLU   N   CA   sing N N 139 
GLU   N   H    sing N N 140 
GLU   N   H2   sing N N 141 
GLU   CA  C    sing N N 142 
GLU   CA  CB   sing N N 143 
GLU   CA  HA   sing N N 144 
GLU   C   O    doub N N 145 
GLU   C   OXT  sing N N 146 
GLU   CB  CG   sing N N 147 
GLU   CB  HB2  sing N N 148 
GLU   CB  HB3  sing N N 149 
GLU   CG  CD   sing N N 150 
GLU   CG  HG2  sing N N 151 
GLU   CG  HG3  sing N N 152 
GLU   CD  OE1  doub N N 153 
GLU   CD  OE2  sing N N 154 
GLU   OE2 HE2  sing N N 155 
GLU   OXT HXT  sing N N 156 
GLY   N   CA   sing N N 157 
GLY   N   H    sing N N 158 
GLY   N   H2   sing N N 159 
GLY   CA  C    sing N N 160 
GLY   CA  HA2  sing N N 161 
GLY   CA  HA3  sing N N 162 
GLY   C   O    doub N N 163 
GLY   C   OXT  sing N N 164 
GLY   OXT HXT  sing N N 165 
HIS   N   CA   sing N N 166 
HIS   N   H    sing N N 167 
HIS   N   H2   sing N N 168 
HIS   CA  C    sing N N 169 
HIS   CA  CB   sing N N 170 
HIS   CA  HA   sing N N 171 
HIS   C   O    doub N N 172 
HIS   C   OXT  sing N N 173 
HIS   CB  CG   sing N N 174 
HIS   CB  HB2  sing N N 175 
HIS   CB  HB3  sing N N 176 
HIS   CG  ND1  sing Y N 177 
HIS   CG  CD2  doub Y N 178 
HIS   ND1 CE1  doub Y N 179 
HIS   ND1 HD1  sing N N 180 
HIS   CD2 NE2  sing Y N 181 
HIS   CD2 HD2  sing N N 182 
HIS   CE1 NE2  sing Y N 183 
HIS   CE1 HE1  sing N N 184 
HIS   NE2 HE2  sing N N 185 
HIS   OXT HXT  sing N N 186 
HOH   O   H1   sing N N 187 
HOH   O   H2   sing N N 188 
ILE   N   CA   sing N N 189 
ILE   N   H    sing N N 190 
ILE   N   H2   sing N N 191 
ILE   CA  C    sing N N 192 
ILE   CA  CB   sing N N 193 
ILE   CA  HA   sing N N 194 
ILE   C   O    doub N N 195 
ILE   C   OXT  sing N N 196 
ILE   CB  CG1  sing N N 197 
ILE   CB  CG2  sing N N 198 
ILE   CB  HB   sing N N 199 
ILE   CG1 CD1  sing N N 200 
ILE   CG1 HG12 sing N N 201 
ILE   CG1 HG13 sing N N 202 
ILE   CG2 HG21 sing N N 203 
ILE   CG2 HG22 sing N N 204 
ILE   CG2 HG23 sing N N 205 
ILE   CD1 HD11 sing N N 206 
ILE   CD1 HD12 sing N N 207 
ILE   CD1 HD13 sing N N 208 
ILE   OXT HXT  sing N N 209 
LEU   N   CA   sing N N 210 
LEU   N   H    sing N N 211 
LEU   N   H2   sing N N 212 
LEU   CA  C    sing N N 213 
LEU   CA  CB   sing N N 214 
LEU   CA  HA   sing N N 215 
LEU   C   O    doub N N 216 
LEU   C   OXT  sing N N 217 
LEU   CB  CG   sing N N 218 
LEU   CB  HB2  sing N N 219 
LEU   CB  HB3  sing N N 220 
LEU   CG  CD1  sing N N 221 
LEU   CG  CD2  sing N N 222 
LEU   CG  HG   sing N N 223 
LEU   CD1 HD11 sing N N 224 
LEU   CD1 HD12 sing N N 225 
LEU   CD1 HD13 sing N N 226 
LEU   CD2 HD21 sing N N 227 
LEU   CD2 HD22 sing N N 228 
LEU   CD2 HD23 sing N N 229 
LEU   OXT HXT  sing N N 230 
LYS   N   CA   sing N N 231 
LYS   N   H    sing N N 232 
LYS   N   H2   sing N N 233 
LYS   CA  C    sing N N 234 
LYS   CA  CB   sing N N 235 
LYS   CA  HA   sing N N 236 
LYS   C   O    doub N N 237 
LYS   C   OXT  sing N N 238 
LYS   CB  CG   sing N N 239 
LYS   CB  HB2  sing N N 240 
LYS   CB  HB3  sing N N 241 
LYS   CG  CD   sing N N 242 
LYS   CG  HG2  sing N N 243 
LYS   CG  HG3  sing N N 244 
LYS   CD  CE   sing N N 245 
LYS   CD  HD2  sing N N 246 
LYS   CD  HD3  sing N N 247 
LYS   CE  NZ   sing N N 248 
LYS   CE  HE2  sing N N 249 
LYS   CE  HE3  sing N N 250 
LYS   NZ  HZ1  sing N N 251 
LYS   NZ  HZ2  sing N N 252 
LYS   NZ  HZ3  sing N N 253 
LYS   OXT HXT  sing N N 254 
MET   N   CA   sing N N 255 
MET   N   H    sing N N 256 
MET   N   H2   sing N N 257 
MET   CA  C    sing N N 258 
MET   CA  CB   sing N N 259 
MET   CA  HA   sing N N 260 
MET   C   O    doub N N 261 
MET   C   OXT  sing N N 262 
MET   CB  CG   sing N N 263 
MET   CB  HB2  sing N N 264 
MET   CB  HB3  sing N N 265 
MET   CG  SD   sing N N 266 
MET   CG  HG2  sing N N 267 
MET   CG  HG3  sing N N 268 
MET   SD  CE   sing N N 269 
MET   CE  HE1  sing N N 270 
MET   CE  HE2  sing N N 271 
MET   CE  HE3  sing N N 272 
MET   OXT HXT  sing N N 273 
PHE   N   CA   sing N N 274 
PHE   N   H    sing N N 275 
PHE   N   H2   sing N N 276 
PHE   CA  C    sing N N 277 
PHE   CA  CB   sing N N 278 
PHE   CA  HA   sing N N 279 
PHE   C   O    doub N N 280 
PHE   C   OXT  sing N N 281 
PHE   CB  CG   sing N N 282 
PHE   CB  HB2  sing N N 283 
PHE   CB  HB3  sing N N 284 
PHE   CG  CD1  doub Y N 285 
PHE   CG  CD2  sing Y N 286 
PHE   CD1 CE1  sing Y N 287 
PHE   CD1 HD1  sing N N 288 
PHE   CD2 CE2  doub Y N 289 
PHE   CD2 HD2  sing N N 290 
PHE   CE1 CZ   doub Y N 291 
PHE   CE1 HE1  sing N N 292 
PHE   CE2 CZ   sing Y N 293 
PHE   CE2 HE2  sing N N 294 
PHE   CZ  HZ   sing N N 295 
PHE   OXT HXT  sing N N 296 
PRO   N   CA   sing N N 297 
PRO   N   CD   sing N N 298 
PRO   N   H    sing N N 299 
PRO   CA  C    sing N N 300 
PRO   CA  CB   sing N N 301 
PRO   CA  HA   sing N N 302 
PRO   C   O    doub N N 303 
PRO   C   OXT  sing N N 304 
PRO   CB  CG   sing N N 305 
PRO   CB  HB2  sing N N 306 
PRO   CB  HB3  sing N N 307 
PRO   CG  CD   sing N N 308 
PRO   CG  HG2  sing N N 309 
PRO   CG  HG3  sing N N 310 
PRO   CD  HD2  sing N N 311 
PRO   CD  HD3  sing N N 312 
PRO   OXT HXT  sing N N 313 
SER   N   CA   sing N N 314 
SER   N   H    sing N N 315 
SER   N   H2   sing N N 316 
SER   CA  C    sing N N 317 
SER   CA  CB   sing N N 318 
SER   CA  HA   sing N N 319 
SER   C   O    doub N N 320 
SER   C   OXT  sing N N 321 
SER   CB  OG   sing N N 322 
SER   CB  HB2  sing N N 323 
SER   CB  HB3  sing N N 324 
SER   OG  HG   sing N N 325 
SER   OXT HXT  sing N N 326 
THR   N   CA   sing N N 327 
THR   N   H    sing N N 328 
THR   N   H2   sing N N 329 
THR   CA  C    sing N N 330 
THR   CA  CB   sing N N 331 
THR   CA  HA   sing N N 332 
THR   C   O    doub N N 333 
THR   C   OXT  sing N N 334 
THR   CB  OG1  sing N N 335 
THR   CB  CG2  sing N N 336 
THR   CB  HB   sing N N 337 
THR   OG1 HG1  sing N N 338 
THR   CG2 HG21 sing N N 339 
THR   CG2 HG22 sing N N 340 
THR   CG2 HG23 sing N N 341 
THR   OXT HXT  sing N N 342 
TYR   N   CA   sing N N 343 
TYR   N   H    sing N N 344 
TYR   N   H2   sing N N 345 
TYR   CA  C    sing N N 346 
TYR   CA  CB   sing N N 347 
TYR   CA  HA   sing N N 348 
TYR   C   O    doub N N 349 
TYR   C   OXT  sing N N 350 
TYR   CB  CG   sing N N 351 
TYR   CB  HB2  sing N N 352 
TYR   CB  HB3  sing N N 353 
TYR   CG  CD1  doub Y N 354 
TYR   CG  CD2  sing Y N 355 
TYR   CD1 CE1  sing Y N 356 
TYR   CD1 HD1  sing N N 357 
TYR   CD2 CE2  doub Y N 358 
TYR   CD2 HD2  sing N N 359 
TYR   CE1 CZ   doub Y N 360 
TYR   CE1 HE1  sing N N 361 
TYR   CE2 CZ   sing Y N 362 
TYR   CE2 HE2  sing N N 363 
TYR   CZ  OH   sing N N 364 
TYR   OH  HH   sing N N 365 
TYR   OXT HXT  sing N N 366 
VAL   N   CA   sing N N 367 
VAL   N   H    sing N N 368 
VAL   N   H2   sing N N 369 
VAL   CA  C    sing N N 370 
VAL   CA  CB   sing N N 371 
VAL   CA  HA   sing N N 372 
VAL   C   O    doub N N 373 
VAL   C   OXT  sing N N 374 
VAL   CB  CG1  sing N N 375 
VAL   CB  CG2  sing N N 376 
VAL   CB  HB   sing N N 377 
VAL   CG1 HG11 sing N N 378 
VAL   CG1 HG12 sing N N 379 
VAL   CG1 HG13 sing N N 380 
VAL   CG2 HG21 sing N N 381 
VAL   CG2 HG22 sing N N 382 
VAL   CG2 HG23 sing N N 383 
VAL   OXT HXT  sing N N 384 
# 
_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                    7HD9 
_atom_sites.fract_transf_matrix[1][1]   0.011252 
_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]   0.011252 
_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]   0.025355 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.740 -16.182 22.237  0.42 58.43 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.664 -15.791 22.293  0.58 59.16 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.761 -15.113 22.391  0.42 58.01 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.681 -14.734 22.497  0.58 58.66 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.406 -13.760 22.105  0.42 56.13 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.307 -13.373 22.203  0.58 56.50 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.506 -13.476 22.581  0.42 56.45 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.415 -13.082 22.654  0.58 56.91 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.117 -15.141 23.793  0.42 59.13 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.090 -14.786 23.920  0.58 59.90 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.096 -14.021 23.935  0.42 59.52 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.041 -13.700 24.100  0.58 60.31 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.470 -16.494 24.055  0.42 59.61 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.496 -16.161 24.202  0.58 60.39 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.054 -15.242 21.744  0.42 69.61 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.951 -14.864 21.875  0.58 70.39 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.805 -15.005 24.463  0.42 70.96 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.798 -14.630 24.565  0.58 71.88 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.578 -14.168 24.742  0.42 71.42 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.573 -13.849 24.936  0.58 72.37 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.562 -13.172 23.992  0.42 71.42 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.479 -12.835 24.117  0.58 72.37 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.511 -14.028 23.161  0.42 71.42 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.415 -13.741 23.360  0.58 72.37 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 17.019 -16.467 24.914  0.42 71.53 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.057 -16.144 25.067  0.58 72.47 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.830 -16.679 23.351  0.42 71.53 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.852 -16.373 23.509  0.58 72.47 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.158 -17.177 24.065  0.42 71.53 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.208 -16.820 24.205  0.58 72.47 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.721 -12.932 21.319  0.42 53.42 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.593 -12.543 21.443  0.58 53.39 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.162 -11.574 21.028  0.42 50.29 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 19.050 -11.202 21.096  0.58 49.88 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 18.008 -10.607 21.279  0.42 47.20 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.933 -10.200 21.373  0.58 46.58 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.898 -11.008 21.642  0.42 47.43 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.843 -10.560 21.828  0.58 46.85 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.727 -11.449 19.606  0.42 49.98 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.549 -11.130 19.646  0.58 49.36 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.733 -11.860 18.539  0.42 49.55 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.508 -11.581 18.645  0.58 48.76 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.584 -11.420 18.538  0.42 49.27 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.365 -11.125 18.669  0.58 48.46 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.177 -12.710 17.619  0.42 49.36 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.900 -12.488 17.758  0.58 48.50 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.979 -13.143 20.937  0.42 64.10 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.822 -12.742 21.116  0.58 64.07 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.876 -11.347 21.639  0.42 60.35 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.799 -10.980 21.664  0.58 59.86 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 19.975 -10.523 19.446  0.42 59.97 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.787 -10.211 19.439  0.58 59.23 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.507 -12.018 19.525  0.42 59.97 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.326 -11.701 19.549  0.58 59.23 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.656 -12.974 16.988  0.42 59.23 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.349 -12.777 17.166  0.58 58.20 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.987 -12.998 17.655  0.42 59.23 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.708 -12.786 17.776  0.58 58.20 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.278 -9.317  21.077  0.42 43.60 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.210 -8.927  21.089  0.58 42.76 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.353 -8.253  21.446  0.42 39.91 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.321 -7.831  21.455  0.58 38.97 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.495 -7.769  20.281  0.42 35.61 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.444 -7.353  20.301  0.58 34.13 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.810 -6.749  20.415  0.42 35.77 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.763 -6.331  20.440  0.58 34.29 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 18.116 -7.078  22.061  0.42 40.31 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 18.123 -6.659  22.027  0.58 39.67 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 19.134 -6.619  21.189  0.42 40.59 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 18.915 -6.045  21.028  0.58 40.22 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 19.005 -9.034  20.717  0.42 52.32 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 18.918 -8.675  20.672  0.58 51.31 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.755 -8.593  22.128  0.42 47.89 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.731 -8.141  22.157  0.58 46.76 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.494 -6.351  22.231  0.42 48.37 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.506 -6.004  22.392  0.58 47.60 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.521 -7.366  22.896  0.42 48.37 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.706 -6.987  22.730  0.58 47.60 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.544 -5.975  21.541  0.42 48.70 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.343 -5.400  21.356  0.58 48.27 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.515 -8.464  19.146  0.42 31.13 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.444 -8.055  19.171  0.58 29.09 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.626 -8.112  18.045  0.42 26.68 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.495 -7.745  18.111  0.58 24.49 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 14.194 -8.502  18.394  0.42 25.19 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 14.088 -8.104  18.573  0.58 24.25 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.934 -9.634  18.812  0.42 25.48 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 13.885 -9.110  19.256  0.58 25.40 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 16.062 -8.823  16.767  0.42 24.04 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 15.840 -8.527  16.845  0.58 21.16 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.328 -8.275  16.166  0.42 21.77 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 17.143 -8.111  16.205  0.58 18.77 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.320 -7.080  15.466  0.42 20.75 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.217 -6.965  15.431  0.58 17.79 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.524 -8.964  16.288  0.42 21.27 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.286 -8.876  16.368  0.58 19.17 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.483 -6.576  14.908  0.42 20.27 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.411 -6.581  14.841  0.58 17.37 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.689 -8.465  15.731  0.42 21.10 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.480 -8.498  15.779  0.58 19.31 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.667 -7.271  15.040  0.42 20.56 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.541 -7.351  15.013  0.58 18.37 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 17.032 -9.133  18.988  0.42 37.36 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 16.974 -8.710  18.998  0.58 34.91 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.659 -7.155  17.896  0.42 32.02 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.523 -6.798  17.914  0.58 29.39 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 16.210 -9.761  16.968  0.42 28.85 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 15.904 -9.469  17.068  0.58 25.39 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.358 -8.736  16.108  0.42 28.85 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 15.132 -8.392  16.194  0.58 25.39 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.525 -6.607  15.375  0.42 24.90 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.455 -6.442  15.313  0.58 21.35 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.543 -9.770  16.754  0.42 25.53 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.248 -9.651  16.885  0.58 23.01 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.466 -5.770  14.443  0.42 24.32 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.446 -5.808  14.326  0.58 20.85 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.485 -8.936  15.823  0.42 25.32 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.240 -9.019  15.899  0.58 23.17 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.449 -6.934  14.666  0.42 24.67 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.341 -7.096  14.618  0.58 22.04 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.262 -7.569  18.204  0.42 23.68 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 13.112 -7.275  18.205  0.58 23.15 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.890 -7.727  18.669  0.42 22.96 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 11.758 -7.409  18.725  0.58 23.75 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.904 -7.447  17.542  0.42 21.25 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 10.735 -7.300  17.603  0.58 21.82 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 11.123 -6.555  16.718  0.42 21.38 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 10.867 -6.463  16.705  0.58 21.65 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.612 -6.770  19.838  0.42 23.80 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.475 -6.333  19.781  0.58 26.07 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.231 -6.737  20.157  0.42 24.70 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 10.778 -6.881  20.886  0.58 28.27 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.408 -6.827  17.796  0.42 28.41 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 13.213 -6.625  17.649  0.58 27.78 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.756 -8.636  18.980  0.42 27.55 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 11.656 -8.278  19.141  0.58 28.50 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 12.112 -7.069  20.617  0.42 28.56 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 12.317 -5.965  20.091  0.58 31.29 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.902 -5.877  19.589  0.42 28.56 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 10.934 -5.634  19.382  0.58 31.29 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 10.102 -6.208  20.798  0.42 29.64 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 10.628 -6.284  21.457  0.58 33.92 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.818  -8.221  17.514  0.42 20.03 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 9.713  -8.150  17.663  0.58 21.03 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.715  -7.962  16.608  0.42 18.59 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 8.600  -8.052  16.743  0.58 20.31 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.892  -8.454  15.189  0.42 17.25 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 8.857  -8.571  15.351  0.58 19.01 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 8.163  -8.007  14.298  0.42 17.64 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 8.058  -8.291  14.450  0.58 19.10 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.699  -8.903  18.020  0.42 24.03 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 9.649  -8.796  18.228  0.58 25.23 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.913  -8.372  16.977  0.42 22.31 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 7.852  -8.550  17.099  0.58 24.38 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.563  -7.007  16.566  0.42 22.31 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.338  -7.122  16.668  0.58 24.38 ?  8   GLY   A HA3  1 
ATOM   157  N N    A TYR   A 1 9   ? 9.837  -9.356  14.942  0.42 15.52 ?  9   TYR   A N    1 
ATOM   158  N N    B TYR   A 1 9   ? 9.934  -9.320  15.140  0.58 17.58 ?  9   TYR   A N    1 
ATOM   159  C CA   A TYR   A 1 9   ? 10.070 -9.875  13.604  0.42 14.22 ?  9   TYR   A CA   1 
ATOM   160  C CA   B TYR   A 1 9   ? 10.217 -9.850  13.818  0.58 16.07 ?  9   TYR   A CA   1 
ATOM   161  C C    A TYR   A 1 9   ? 9.199  -11.097 13.339  0.42 13.99 ?  9   TYR   A C    1 
ATOM   162  C C    B TYR   A 1 9   ? 9.385  -11.095 13.540  0.58 15.88 ?  9   TYR   A C    1 
ATOM   163  O O    A TYR   A 1 9   ? 8.894  -11.882 14.239  0.42 15.25 ?  9   TYR   A O    1 
ATOM   164  O O    B TYR   A 1 9   ? 9.095  -11.897 14.432  0.58 17.34 ?  9   TYR   A O    1 
ATOM   165  C CB   A TYR   A 1 9   ? 11.542 -10.268 13.415  0.42 13.79 ?  9   TYR   A CB   1 
ATOM   166  C CB   B TYR   A 1 9   ? 11.705 -10.178 13.660  0.58 15.49 ?  9   TYR   A CB   1 
ATOM   167  C CG   A TYR   A 1 9   ? 12.489 -9.095  13.295  0.42 14.14 ?  9   TYR   A CG   1 
ATOM   168  C CG   B TYR   A 1 9   ? 12.552 -8.953  13.392  0.58 15.15 ?  9   TYR   A CG   1 
ATOM   169  C CD1  A TYR   A 1 9   ? 12.826 -8.341  14.408  0.42 14.85 ?  9   TYR   A CD1  1 
ATOM   170  C CD1  B TYR   A 1 9   ? 12.852 -8.064  14.413  0.58 15.92 ?  9   TYR   A CD1  1 
ATOM   171  C CD2  A TYR   A 1 9   ? 13.042 -8.744  12.070  0.42 13.77 ?  9   TYR   A CD2  1 
ATOM   172  C CD2  B TYR   A 1 9   ? 13.021 -8.673  12.116  0.58 14.33 ?  9   TYR   A CD2  1 
ATOM   173  C CE1  A TYR   A 1 9   ? 13.680 -7.264  14.309  0.42 14.99 ?  9   TYR   A CE1  1 
ATOM   174  C CE1  B TYR   A 1 9   ? 13.605 -6.934  14.176  0.58 15.78 ?  9   TYR   A CE1  1 
ATOM   175  C CE2  A TYR   A 1 9   ? 13.899 -7.669  11.960  0.42 14.22 ?  9   TYR   A CE2  1 
ATOM   176  C CE2  B TYR   A 1 9   ? 13.777 -7.547  11.868  0.58 14.48 ?  9   TYR   A CE2  1 
ATOM   177  C CZ   A TYR   A 1 9   ? 14.212 -6.935  13.083  0.42 15.12 ?  9   TYR   A CZ   1 
ATOM   178  C CZ   B TYR   A 1 9   ? 14.060 -6.680  12.900  0.58 15.11 ?  9   TYR   A CZ   1 
ATOM   179  O OH   A TYR   A 1 9   ? 15.066 -5.867  12.977  0.42 16.40 ?  9   TYR   A OH   1 
ATOM   180  O OH   B TYR   A 1 9   ? 14.807 -5.557  12.645  0.58 15.33 ?  9   TYR   A OH   1 
ATOM   181  H H    A TYR   A 1 9   ? 10.361 -9.688  15.538  0.42 18.63 ?  9   TYR   A H    1 
ATOM   182  H H    B TYR   A 1 9   ? 10.513 -9.535  15.744  0.58 21.10 ?  9   TYR   A H    1 
ATOM   183  H HA   A TYR   A 1 9   ? 9.847  -9.196  12.950  0.42 17.07 ?  9   TYR   A HA   1 
ATOM   184  H HA   B TYR   A 1 9   ? 9.988  -9.182  13.158  0.58 19.28 ?  9   TYR   A HA   1 
ATOM   185  H HB2  A TYR   A 1 9   ? 11.824 -10.805 14.173  0.42 16.54 ?  9   TYR   A HB2  1 
ATOM   186  H HB2  B TYR   A 1 9   ? 12.024 -10.601 14.473  0.58 18.59 ?  9   TYR   A HB2  1 
ATOM   187  H HB3  A TYR   A 1 9   ? 11.611 -10.788 12.600  0.42 16.54 ?  9   TYR   A HB3  1 
ATOM   188  H HB3  B TYR   A 1 9   ? 11.805 -10.786 12.910  0.58 18.59 ?  9   TYR   A HB3  1 
ATOM   189  H HD1  A TYR   A 1 9   ? 12.458 -8.561  15.235  0.42 17.82 ?  9   TYR   A HD1  1 
ATOM   190  H HD1  B TYR   A 1 9   ? 12.533 -8.237  15.275  0.58 19.10 ?  9   TYR   A HD1  1 
ATOM   191  H HD2  A TYR   A 1 9   ? 12.829 -9.239  11.312  0.42 16.52 ?  9   TYR   A HD2  1 
ATOM   192  H HD2  B TYR   A 1 9   ? 12.824 -9.254  11.417  0.58 17.20 ?  9   TYR   A HD2  1 
ATOM   193  H HE1  A TYR   A 1 9   ? 13.896 -6.764  15.061  0.42 17.99 ?  9   TYR   A HE1  1 
ATOM   194  H HE1  B TYR   A 1 9   ? 13.801 -6.350  14.870  0.58 18.94 ?  9   TYR   A HE1  1 
ATOM   195  H HE2  A TYR   A 1 9   ? 14.268 -7.441  11.134  0.42 17.06 ?  9   TYR   A HE2  1 
ATOM   196  H HE2  B TYR   A 1 9   ? 14.092 -7.369  11.009  0.58 17.38 ?  9   TYR   A HE2  1 
ATOM   197  H HH   A TYR   A 1 9   ? 15.174 -5.511  13.729  0.42 19.68 ?  9   TYR   A HH   1 
ATOM   198  H HH   B TYR   A 1 9   ? 14.922 -5.122  13.354  0.58 18.39 ?  9   TYR   A HH   1 
ATOM   199  N N    A LEU   A 1 10  ? 8.795  -11.239 12.082  0.42 13.58 ?  10  LEU   A N    1 
ATOM   200  N N    B LEU   A 1 10  ? 9.019  -11.246 12.273  0.58 15.29 ?  10  LEU   A N    1 
ATOM   201  C CA   A LEU   A 1 10  ? 8.245  -12.493 11.593  0.42 13.77 ?  10  LEU   A CA   1 
ATOM   202  C CA   B LEU   A 1 10  ? 8.339  -12.428 11.772  0.58 15.50 ?  10  LEU   A CA   1 
ATOM   203  C C    A LEU   A 1 10  ? 9.396  -13.418 11.215  0.42 12.80 ?  10  LEU   A C    1 
ATOM   204  C C    B LEU   A 1 10  ? 9.385  -13.394 11.228  0.58 15.09 ?  10  LEU   A C    1 
ATOM   205  O O    A LEU   A 1 10  ? 10.422 -12.973 10.696  0.42 11.24 ?  10  LEU   A O    1 
ATOM   206  O O    B LEU   A 1 10  ? 10.226 -13.013 10.408  0.58 14.09 ?  10  LEU   A O    1 
ATOM   207  C CB   A LEU   A 1 10  ? 7.388  -12.221 10.360  0.42 15.52 ?  10  LEU   A CB   1 
ATOM   208  C CB   B LEU   A 1 10  ? 7.385  -12.006 10.656  0.58 16.20 ?  10  LEU   A CB   1 
ATOM   209  C CG   A LEU   A 1 10  ? 6.713  -13.424 9.711   0.42 17.49 ?  10  LEU   A CG   1 
ATOM   210  C CG   B LEU   A 1 10  ? 6.568  -13.095 9.970   0.58 17.92 ?  10  LEU   A CG   1 
ATOM   211  C CD1  A LEU   A 1 10  ? 5.629  -13.977 10.608  0.42 18.48 ?  10  LEU   A CD1  1 
ATOM   212  C CD1  B LEU   A 1 10  ? 5.684  -13.787 10.973  0.58 19.55 ?  10  LEU   A CD1  1 
ATOM   213  C CD2  A LEU   A 1 10  ? 6.144  -13.021 8.374   0.42 18.17 ?  10  LEU   A CD2  1 
ATOM   214  C CD2  B LEU   A 1 10  ? 5.732  -12.484 8.861   0.58 18.90 ?  10  LEU   A CD2  1 
ATOM   215  H H    A LEU   A 1 10  ? 8.819  -10.609 11.490  0.42 16.30 ?  10  LEU   A H    1 
ATOM   216  H H    B LEU   A 1 10  ? 9.165  -10.656 11.666  0.58 18.35 ?  10  LEU   A H    1 
ATOM   217  H HA   A LEU   A 1 10  ? 7.699  -12.908 12.282  0.42 16.52 ?  10  LEU   A HA   1 
ATOM   218  H HA   B LEU   A 1 10  ? 7.835  -12.853 12.484  0.58 18.60 ?  10  LEU   A HA   1 
ATOM   219  H HB2  A LEU   A 1 10  ? 6.685  -11.601 10.604  0.42 18.63 ?  10  LEU   A HB2  1 
ATOM   220  H HB2  B LEU   A 1 10  ? 6.749  -11.370 11.023  0.58 19.44 ?  10  LEU   A HB2  1 
ATOM   221  H HB3  A LEU   A 1 10  ? 7.953  -11.815 9.684   0.42 18.63 ?  10  LEU   A HB3  1 
ATOM   222  H HB3  B LEU   A 1 10  ? 7.906  -11.566 9.965   0.58 19.44 ?  10  LEU   A HB3  1 
ATOM   223  H HG   A LEU   A 1 10  ? 7.371  -14.122 9.561   0.42 20.98 ?  10  LEU   A HG   1 
ATOM   224  H HG   B LEU   A 1 10  ? 7.167  -13.751 9.576   0.58 21.51 ?  10  LEU   A HG   1 
ATOM   225  H HD11 A LEU   A 1 10  ? 5.303  -14.811 10.235  0.42 22.18 ?  10  LEU   A HD11 1 
ATOM   226  H HD11 B LEU   A 1 10  ? 5.269  -14.556 10.553  0.58 23.46 ?  10  LEU   A HD11 1 
ATOM   227  H HD12 A LEU   A 1 10  ? 5.995  -14.132 11.492  0.42 22.18 ?  10  LEU   A HD12 1 
ATOM   228  H HD12 B LEU   A 1 10  ? 6.219  -14.070 11.727  0.58 23.46 ?  10  LEU   A HD12 1 
ATOM   229  H HD13 A LEU   A 1 10  ? 4.905  -13.333 10.661  0.42 22.18 ?  10  LEU   A HD13 1 
ATOM   230  H HD13 B LEU   A 1 10  ? 5.005  -13.162 11.270  0.58 23.46 ?  10  LEU   A HD13 1 
ATOM   231  H HD21 A LEU   A 1 10  ? 5.706  -13.789 7.978   0.42 21.80 ?  10  LEU   A HD21 1 
ATOM   232  H HD21 B LEU   A 1 10  ? 5.219  -13.185 8.431   0.58 22.67 ?  10  LEU   A HD21 1 
ATOM   233  H HD22 A LEU   A 1 10  ? 5.506  -12.305 8.511   0.42 21.80 ?  10  LEU   A HD22 1 
ATOM   234  H HD22 B LEU   A 1 10  ? 5.134  -11.825 9.247   0.58 22.67 ?  10  LEU   A HD22 1 
ATOM   235  H HD23 A LEU   A 1 10  ? 6.868  -12.719 7.806   0.42 21.80 ?  10  LEU   A HD23 1 
ATOM   236  H HD23 B LEU   A 1 10  ? 6.321  -12.061 8.218   0.58 22.67 ?  10  LEU   A HD23 1 
ATOM   237  N N    A LYS   A 1 11  ? 9.225  -14.711 11.473  0.42 13.34 ?  11  LYS   A N    1 
ATOM   238  N N    B LYS   A 1 11  ? 9.340  -14.638 11.694  0.58 15.50 ?  11  LYS   A N    1 
ATOM   239  C CA   A LYS   A 1 11  ? 10.271 -15.699 11.229  0.42 13.68 ?  11  LYS   A CA   1 
ATOM   240  C CA   B LYS   A 1 11  ? 10.284 -15.652 11.247  0.58 15.13 ?  11  LYS   A CA   1 
ATOM   241  C C    A LYS   A 1 11  ? 9.977  -16.361 9.888   0.42 13.96 ?  11  LYS   A C    1 
ATOM   242  C C    B LYS   A 1 11  ? 9.876  -16.144 9.865   0.58 14.14 ?  11  LYS   A C    1 
ATOM   243  O O    A LYS   A 1 11  ? 9.003  -17.110 9.761   0.42 14.69 ?  11  LYS   A O    1 
ATOM   244  O O    B LYS   A 1 11  ? 8.725  -16.541 9.659   0.58 14.27 ?  11  LYS   A O    1 
ATOM   245  C CB   A LYS   A 1 11  ? 10.319 -16.718 12.368  0.42 13.54 ?  11  LYS   A CB   1 
ATOM   246  C CB   B LYS   A 1 11  ? 10.277 -16.810 12.244  0.58 15.42 ?  11  LYS   A CB   1 
ATOM   247  C CG   A LYS   A 1 11  ? 11.393 -17.793 12.236  0.42 13.14 ?  11  LYS   A CG   1 
ATOM   248  C CG   B LYS   A 1 11  ? 11.279 -17.916 11.984  0.58 15.52 ?  11  LYS   A CG   1 
ATOM   249  C CD   A LYS   A 1 11  ? 11.471 -18.642 13.502  0.42 12.74 ?  11  LYS   A CD   1 
ATOM   250  C CD   B LYS   A 1 11  ? 11.309 -18.850 13.182  0.58 15.93 ?  11  LYS   A CD   1 
ATOM   251  C CE   A LYS   A 1 11  ? 12.480 -19.783 13.372  0.42 12.71 ?  11  LYS   A CE   1 
ATOM   252  C CE   B LYS   A 1 11  ? 12.334 -19.960 13.030  0.58 15.77 ?  11  LYS   A CE   1 
ATOM   253  N NZ   A LYS   A 1 11  ? 13.862 -19.293 13.118  0.42 12.70 ?  11  LYS   A NZ   1 
ATOM   254  N NZ   B LYS   A 1 11  ? 13.715 -19.430 12.894  0.58 15.93 ?  11  LYS   A NZ   1 
ATOM   255  H H    A LYS   A 1 11  ? 8.494  -15.042 11.782  0.42 16.01 ?  11  LYS   A H    1 
ATOM   256  H H    B LYS   A 1 11  ? 8.767  -14.914 12.272  0.58 18.60 ?  11  LYS   A H    1 
ATOM   257  H HA   A LYS   A 1 11  ? 11.129 -15.249 11.174  0.42 16.42 ?  11  LYS   A HA   1 
ATOM   258  H HA   B LYS   A 1 11  ? 11.176 -15.270 11.200  0.58 18.16 ?  11  LYS   A HA   1 
ATOM   259  H HB2  A LYS   A 1 11  ? 10.485 -16.237 13.196  0.42 16.25 ?  11  LYS   A HB2  1 
ATOM   260  H HB2  B LYS   A 1 11  ? 10.463 -16.449 13.125  0.58 18.51 ?  11  LYS   A HB2  1 
ATOM   261  H HB3  A LYS   A 1 11  ? 9.461  -17.161 12.417  0.42 16.25 ?  11  LYS   A HB3  1 
ATOM   262  H HB3  B LYS   A 1 11  ? 9.396  -17.208 12.235  0.58 18.51 ?  11  LYS   A HB3  1 
ATOM   263  H HG2  A LYS   A 1 11  ? 11.176 -18.370 11.490  0.42 15.76 ?  11  LYS   A HG2  1 
ATOM   264  H HG2  B LYS   A 1 11  ? 11.017 -18.417 11.197  0.58 18.63 ?  11  LYS   A HG2  1 
ATOM   265  H HG3  A LYS   A 1 11  ? 12.255 -17.369 12.098  0.42 15.76 ?  11  LYS   A HG3  1 
ATOM   266  H HG3  B LYS   A 1 11  ? 12.165 -17.531 11.865  0.58 18.63 ?  11  LYS   A HG3  1 
ATOM   267  H HD2  A LYS   A 1 11  ? 11.739 -18.082 14.248  0.42 15.29 ?  11  LYS   A HD2  1 
ATOM   268  H HD2  B LYS   A 1 11  ? 11.526 -18.340 13.977  0.58 19.11 ?  11  LYS   A HD2  1 
ATOM   269  H HD3  A LYS   A 1 11  ? 10.596 -19.030 13.679  0.42 15.29 ?  11  LYS   A HD3  1 
ATOM   270  H HD3  B LYS   A 1 11  ? 10.432 -19.260 13.280  0.58 19.11 ?  11  LYS   A HD3  1 
ATOM   271  H HE2  A LYS   A 1 11  ? 12.490 -20.294 14.197  0.42 15.25 ?  11  LYS   A HE2  1 
ATOM   272  H HE2  B LYS   A 1 11  ? 12.304 -20.528 13.816  0.58 18.92 ?  11  LYS   A HE2  1 
ATOM   273  H HE3  A LYS   A 1 11  ? 12.221 -20.352 12.631  0.42 15.25 ?  11  LYS   A HE3  1 
ATOM   274  H HE3  B LYS   A 1 11  ? 12.128 -20.474 12.236  0.58 18.92 ?  11  LYS   A HE3  1 
ATOM   275  H HZ1  A LYS   A 1 11  ? 14.421 -19.981 13.049  0.42 15.24 ?  11  LYS   A HZ1  1 
ATOM   276  H HZ1  B LYS   A 1 11  ? 14.290 -20.101 12.798  0.58 19.11 ?  11  LYS   A HZ1  1 
ATOM   277  H HZ2  A LYS   A 1 11  ? 13.884 -18.825 12.361  0.42 15.24 ?  11  LYS   A HZ2  1 
ATOM   278  H HZ2  B LYS   A 1 11  ? 13.769 -18.897 12.183  0.58 19.11 ?  11  LYS   A HZ2  1 
ATOM   279  H HZ3  A LYS   A 1 11  ? 14.127 -18.770 13.788  0.42 15.24 ?  11  LYS   A HZ3  1 
ATOM   280  H HZ3  B LYS   A 1 11  ? 13.935 -18.963 13.620  0.58 19.11 ?  11  LYS   A HZ3  1 
ATOM   281  N N    A LEU   A 1 12  ? 10.808 -16.073 8.883   0.42 13.59 ?  12  LEU   A N    1 
ATOM   282  N N    B LEU   A 1 12  ? 10.809 -16.113 8.914   0.58 14.09 ?  12  LEU   A N    1 
ATOM   283  C CA   A LEU   A 1 12  ? 10.596 -16.663 7.565   0.42 13.65 ?  12  LEU   A CA   1 
ATOM   284  C CA   B LEU   A 1 12  ? 10.565 -16.660 7.583   0.58 14.76 ?  12  LEU   A CA   1 
ATOM   285  C C    A LEU   A 1 12  ? 11.167 -18.072 7.487   0.42 13.49 ?  12  LEU   A C    1 
ATOM   286  C C    B LEU   A 1 12  ? 11.176 -18.038 7.382   0.58 14.40 ?  12  LEU   A C    1 
ATOM   287  O O    A LEU   A 1 12  ? 10.513 -18.984 6.970   0.42 13.93 ?  12  LEU   A O    1 
ATOM   288  O O    B LEU   A 1 12  ? 10.565 -18.880 6.718   0.58 14.02 ?  12  LEU   A O    1 
ATOM   289  C CB   A LEU   A 1 12  ? 11.215 -15.789 6.473   0.42 14.10 ?  12  LEU   A CB   1 
ATOM   290  C CB   B LEU   A 1 12  ? 11.101 -15.726 6.497   0.58 15.90 ?  12  LEU   A CB   1 
ATOM   291  C CG   A LEU   A 1 12  ? 10.527 -14.459 6.168   0.42 15.02 ?  12  LEU   A CG   1 
ATOM   292  C CG   B LEU   A 1 12  ? 10.479 -14.334 6.443   0.58 17.27 ?  12  LEU   A CG   1 
ATOM   293  C CD1  A LEU   A 1 12  ? 11.355 -13.669 5.162   0.42 15.56 ?  12  LEU   A CD1  1 
ATOM   294  C CD1  B LEU   A 1 12  ? 11.016 -13.568 5.244   0.58 17.93 ?  12  LEU   A CD1  1 
ATOM   295  C CD2  A LEU   A 1 12  ? 9.103  -14.673 5.659   0.42 15.05 ?  12  LEU   A CD2  1 
ATOM   296  C CD2  B LEU   A 1 12  ? 8.959  -14.431 6.399   0.58 17.70 ?  12  LEU   A CD2  1 
ATOM   297  H H    A LEU   A 1 12  ? 11.493 -15.552 8.939   0.42 16.31 ?  12  LEU   A H    1 
ATOM   298  H H    B LEU   A 1 12  ? 11.594 -15.773 9.017   0.58 16.91 ?  12  LEU   A H    1 
ATOM   299  H HA   A LEU   A 1 12  ? 9.645  -16.722 7.402   0.42 16.38 ?  12  LEU   A HA   1 
ATOM   300  H HA   B LEU   A 1 12  ? 9.610  -16.751 7.458   0.58 17.71 ?  12  LEU   A HA   1 
ATOM   301  H HB2  A LEU   A 1 12  ? 12.126 -15.584 6.730   0.42 16.92 ?  12  LEU   A HB2  1 
ATOM   302  H HB2  B LEU   A 1 12  ? 12.054 -15.614 6.637   0.58 19.08 ?  12  LEU   A HB2  1 
ATOM   303  H HB3  A LEU   A 1 12  ? 11.223 -16.302 5.649   0.42 16.92 ?  12  LEU   A HB3  1 
ATOM   304  H HB3  B LEU   A 1 12  ? 10.949 -16.146 5.637   0.58 19.08 ?  12  LEU   A HB3  1 
ATOM   305  H HG   A LEU   A 1 12  ? 10.473 -13.939 6.982   0.42 18.02 ?  12  LEU   A HG   1 
ATOM   306  H HG   B LEU   A 1 12  ? 10.727 -13.846 7.244   0.58 20.73 ?  12  LEU   A HG   1 
ATOM   307  H HD11 A LEU   A 1 12  ? 10.894 -12.842 4.954   0.42 18.67 ?  12  LEU   A HD11 1 
ATOM   308  H HD11 B LEU   A 1 12  ? 10.610 -12.688 5.222   0.58 21.51 ?  12  LEU   A HD11 1 
ATOM   309  H HD12 A LEU   A 1 12  ? 12.222 -13.477 5.552   0.42 18.67 ?  12  LEU   A HD12 1 
ATOM   310  H HD12 B LEU   A 1 12  ? 11.981 -13.485 5.328   0.58 21.51 ?  12  LEU   A HD12 1 
ATOM   311  H HD13 A LEU   A 1 12  ? 11.464 -14.199 4.357   0.42 18.67 ?  12  LEU   A HD13 1 
ATOM   312  H HD13 B LEU   A 1 12  ? 10.797 -14.055 4.434   0.58 21.51 ?  12  LEU   A HD13 1 
ATOM   313  H HD21 A LEU   A 1 12  ? 8.693  -13.813 5.498   0.42 18.06 ?  12  LEU   A HD21 1 
ATOM   314  H HD21 B LEU   A 1 12  ? 8.595  -13.565 6.163   0.58 21.24 ?  12  LEU   A HD21 1 
ATOM   315  H HD22 A LEU   A 1 12  ? 9.139  -15.180 4.835   0.42 18.06 ?  12  LEU   A HD22 1 
ATOM   316  H HD22 B LEU   A 1 12  ? 8.705  -15.092 5.737   0.58 21.24 ?  12  LEU   A HD22 1 
ATOM   317  H HD23 A LEU   A 1 12  ? 8.592  -15.162 6.325   0.42 18.06 ?  12  LEU   A HD23 1 
ATOM   318  H HD23 B LEU   A 1 12  ? 8.635  -14.699 7.275   0.58 21.24 ?  12  LEU   A HD23 1 
ATOM   319  N N    A THR   A 1 13  ? 12.389 -18.262 7.977   0.42 12.91 ?  13  THR   A N    1 
ATOM   320  N N    B THR   A 1 13  ? 12.382 -18.264 7.900   0.58 14.07 ?  13  THR   A N    1 
ATOM   321  C CA   A THR   A 1 13  ? 13.083 -19.539 7.882   0.42 13.16 ?  13  THR   A CA   1 
ATOM   322  C CA   B THR   A 1 13  ? 13.065 -19.550 7.827   0.58 14.68 ?  13  THR   A CA   1 
ATOM   323  C C    A THR   A 1 13  ? 13.844 -19.774 9.178   0.42 13.00 ?  13  THR   A C    1 
ATOM   324  C C    B THR   A 1 13  ? 13.824 -19.757 9.131   0.58 14.58 ?  13  THR   A C    1 
ATOM   325  O O    A THR   A 1 13  ? 13.729 -19.015 10.144  0.42 13.38 ?  13  THR   A O    1 
ATOM   326  O O    B THR   A 1 13  ? 13.731 -18.956 10.065  0.58 14.64 ?  13  THR   A O    1 
ATOM   327  C CB   A THR   A 1 13  ? 14.065 -19.564 6.705   0.42 13.62 ?  13  THR   A CB   1 
ATOM   328  C CB   B THR   A 1 13  ? 14.043 -19.623 6.646   0.58 15.20 ?  13  THR   A CB   1 
ATOM   329  O OG1  A THR   A 1 13  ? 15.106 -18.614 6.947   0.42 13.72 ?  13  THR   A OG1  1 
ATOM   330  O OG1  B THR   A 1 13  ? 15.116 -18.707 6.874   0.58 15.30 ?  13  THR   A OG1  1 
ATOM   331  C CG2  A THR   A 1 13  ? 13.375 -19.244 5.385   0.42 14.22 ?  13  THR   A CG2  1 
ATOM   332  C CG2  B THR   A 1 13  ? 13.367 -19.305 5.317   0.58 16.06 ?  13  THR   A CG2  1 
ATOM   333  H H    A THR   A 1 13  ? 12.850 -17.647 8.374   0.42 15.49 ?  13  THR   A H    1 
ATOM   334  H H    B THR   A 1 13  ? 12.849 -17.657 8.298   0.58 16.88 ?  13  THR   A H    1 
ATOM   335  H HA   A THR   A 1 13  ? 12.442 -20.253 7.767   0.42 15.79 ?  13  THR   A HA   1 
ATOM   336  H HA   B THR   A 1 13  ? 12.415 -20.255 7.725   0.58 17.62 ?  13  THR   A HA   1 
ATOM   337  H HB   A THR   A 1 13  ? 14.459 -20.448 6.636   0.42 16.34 ?  13  THR   A HB   1 
ATOM   338  H HB   B THR   A 1 13  ? 14.406 -20.520 6.586   0.58 18.24 ?  13  THR   A HB   1 
ATOM   339  H HG1  A THR   A 1 13  ? 15.803 -19.005 7.211   0.42 16.47 ?  13  THR   A HG1  1 
ATOM   340  H HG1  B THR   A 1 13  ? 15.728 -19.078 7.317   0.58 18.36 ?  13  THR   A HG1  1 
ATOM   341  H HG21 A THR   A 1 13  ? 14.009 -19.328 4.652   0.42 17.07 ?  13  THR   A HG21 1 
ATOM   342  H HG21 B THR   A 1 13  ? 14.002 -19.415 4.587   0.58 19.27 ?  13  THR   A HG21 1 
ATOM   343  H HG22 A THR   A 1 13  ? 12.644 -19.865 5.237   0.42 17.07 ?  13  THR   A HG22 1 
ATOM   344  H HG22 B THR   A 1 13  ? 12.623 -19.911 5.175   0.58 19.27 ?  13  THR   A HG22 1 
ATOM   345  H HG23 A THR   A 1 13  ? 13.028 -18.342 5.399   0.42 17.07 ?  13  THR   A HG23 1 
ATOM   346  H HG23 B THR   A 1 13  ? 13.042 -18.395 5.317   0.58 19.27 ?  13  THR   A HG23 1 
ATOM   347  N N    A ASP   A 1 14  ? 14.661 -20.826 9.177   0.42 13.24 ?  14  ASP   A N    1 
ATOM   348  N N    B ASP   A 1 14  ? 14.613 -20.831 9.176   0.58 15.21 ?  14  ASP   A N    1 
ATOM   349  C CA   A ASP   A 1 14  ? 15.484 -21.116 10.337  0.42 13.40 ?  14  ASP   A CA   1 
ATOM   350  C CA   B ASP   A 1 14  ? 15.453 -21.090 10.336  0.58 15.83 ?  14  ASP   A CA   1 
ATOM   351  C C    A ASP   A 1 14  ? 16.365 -19.934 10.723  0.42 12.95 ?  14  ASP   A C    1 
ATOM   352  C C    B ASP   A 1 14  ? 16.248 -19.850 10.736  0.58 14.39 ?  14  ASP   A C    1 
ATOM   353  O O    A ASP   A 1 14  ? 16.697 -19.776 11.903  0.42 13.17 ?  14  ASP   A O    1 
ATOM   354  O O    B ASP   A 1 14  ? 16.369 -19.542 11.927  0.58 15.32 ?  14  ASP   A O    1 
ATOM   355  C CB   A ASP   A 1 14  ? 16.366 -22.325 10.059  0.42 15.27 ?  14  ASP   A CB   1 
ATOM   356  C CB   B ASP   A 1 14  ? 16.398 -22.252 10.019  0.58 19.18 ?  14  ASP   A CB   1 
ATOM   357  C CG   A ASP   A 1 14  ? 17.276 -22.620 11.208  0.42 17.40 ?  14  ASP   A CG   1 
ATOM   358  C CG   B ASP   A 1 14  ? 17.323 -22.594 11.175  0.58 23.16 ?  14  ASP   A CG   1 
ATOM   359  O OD1  A ASP   A 1 14  ? 16.775 -23.162 12.216  0.42 17.51 ?  14  ASP   A OD1  1 
ATOM   360  O OD1  B ASP   A 1 14  ? 16.956 -22.333 12.341  0.58 24.68 ?  14  ASP   A OD1  1 
ATOM   361  O OD2  A ASP   A 1 14  ? 18.464 -22.259 11.125  0.42 18.46 -1 14  ASP   A OD2  1 
ATOM   362  O OD2  B ASP   A 1 14  ? 18.421 -23.127 10.915  0.58 24.71 -1 14  ASP   A OD2  1 
ATOM   363  H H    A ASP   A 1 14  ? 14.762 -21.371 8.523   0.42 15.88 ?  14  ASP   A H    1 
ATOM   364  H H    B ASP   A 1 14  ? 14.692 -21.404 8.543   0.58 18.25 ?  14  ASP   A H    1 
ATOM   365  H HA   A ASP   A 1 14  ? 14.918 -21.330 11.093  0.42 16.08 ?  14  ASP   A HA   1 
ATOM   366  H HA   B ASP   A 1 14  ? 14.891 -21.350 11.084  0.58 18.99 ?  14  ASP   A HA   1 
ATOM   367  H HB2  A ASP   A 1 14  ? 15.803 -23.110 9.916   0.42 18.32 ?  14  ASP   A HB2  1 
ATOM   368  H HB2  B ASP   A 1 14  ? 15.862 -23.043 9.815   0.58 23.02 ?  14  ASP   A HB2  1 
ATOM   369  H HB3  A ASP   A 1 14  ? 16.905 -22.164 9.269   0.42 18.32 ?  14  ASP   A HB3  1 
ATOM   370  H HB3  B ASP   A 1 14  ? 16.938 -22.019 9.250   0.58 23.02 ?  14  ASP   A HB3  1 
ATOM   371  N N    . ASN   A 1 15  ? 16.769 -19.107 9.755   1.00 13.02 ?  15  ASN   A N    1 
ATOM   372  C CA   . ASN   A 1 15  ? 17.750 -18.058 10.017  1.00 13.12 ?  15  ASN   A CA   1 
ATOM   373  C C    . ASN   A 1 15  ? 17.389 -16.672 9.495   1.00 13.36 ?  15  ASN   A C    1 
ATOM   374  O O    . ASN   A 1 15  ? 18.160 -15.736 9.724   1.00 14.76 ?  15  ASN   A O    1 
ATOM   375  C CB   . ASN   A 1 15  ? 19.122 -18.460 9.451   1.00 13.28 ?  15  ASN   A CB   1 
ATOM   376  C CG   . ASN   A 1 15  ? 19.127 -18.536 7.945   1.00 13.56 ?  15  ASN   A CG   1 
ATOM   377  O OD1  . ASN   A 1 15  ? 18.420 -19.362 7.354   1.00 15.13 ?  15  ASN   A OD1  1 
ATOM   378  N ND2  . ASN   A 1 15  ? 19.920 -17.672 7.306   1.00 13.92 ?  15  ASN   A ND2  1 
ATOM   379  H H    A ASN   A 1 15  ? 16.482 -19.129 8.951   0.42 15.62 ?  15  ASN   A H    1 
ATOM   380  H H    B ASN   A 1 15  ? 16.567 -19.196 8.931   0.58 15.62 ?  15  ASN   A H    1 
ATOM   381  H HA   . ASN   A 1 15  ? 17.858 -17.971 10.980  1.00 15.74 ?  15  ASN   A HA   1 
ATOM   382  H HB2  . ASN   A 1 15  ? 19.782 -17.794 9.726   1.00 15.94 ?  15  ASN   A HB2  1 
ATOM   383  H HB3  . ASN   A 1 15  ? 19.369 -19.328 9.801   1.00 15.94 ?  15  ASN   A HB3  1 
ATOM   384  H HD21 . ASN   A 1 15  ? 19.948 -17.670 6.448   1.00 16.70 ?  15  ASN   A HD21 1 
ATOM   385  H HD22 . ASN   A 1 15  ? 20.389 -17.101 7.751   1.00 16.70 ?  15  ASN   A HD22 1 
ATOM   386  N N    A VAL   A 1 16  ? 16.257 -16.509 8.811   0.42 13.14 ?  16  VAL   A N    1 
ATOM   387  N N    B VAL   A 1 16  ? 16.249 -16.502 8.827   0.58 13.66 ?  16  VAL   A N    1 
ATOM   388  C CA   A VAL   A 1 16  ? 15.860 -15.231 8.224   0.42 12.86 ?  16  VAL   A CA   1 
ATOM   389  C CA   B VAL   A 1 16  ? 15.845 -15.215 8.263   0.58 13.72 ?  16  VAL   A CA   1 
ATOM   390  C C    A VAL   A 1 16  ? 14.580 -14.739 8.888   0.42 12.31 ?  16  VAL   A C    1 
ATOM   391  C C    B VAL   A 1 16  ? 14.589 -14.719 8.968   0.58 13.46 ?  16  VAL   A C    1 
ATOM   392  O O    A VAL   A 1 16  ? 13.572 -15.455 8.932   0.42 12.34 ?  16  VAL   A O    1 
ATOM   393  O O    B VAL   A 1 16  ? 13.605 -15.456 9.112   0.58 13.59 ?  16  VAL   A O    1 
ATOM   394  C CB   A VAL   A 1 16  ? 15.683 -15.322 6.697   0.42 13.49 ?  16  VAL   A CB   1 
ATOM   395  C CB   B VAL   A 1 16  ? 15.634 -15.296 6.741   0.58 14.38 ?  16  VAL   A CB   1 
ATOM   396  C CG1  A VAL   A 1 16  ? 15.264 -13.965 6.130   0.42 13.91 ?  16  VAL   A CG1  1 
ATOM   397  C CG1  B VAL   A 1 16  ? 15.191 -13.939 6.187   0.58 14.86 ?  16  VAL   A CG1  1 
ATOM   398  C CG2  A VAL   A 1 16  ? 16.966 -15.803 6.036   0.42 14.27 ?  16  VAL   A CG2  1 
ATOM   399  C CG2  B VAL   A 1 16  ? 16.908 -15.771 6.048   0.58 15.35 ?  16  VAL   A CG2  1 
ATOM   400  H H    A VAL   A 1 16  ? 15.692 -17.142 8.674   0.42 15.77 ?  16  VAL   A H    1 
ATOM   401  H H    B VAL   A 1 16  ? 15.682 -17.134 8.690   0.58 16.39 ?  16  VAL   A H    1 
ATOM   402  H HA   A VAL   A 1 16  ? 16.554 -14.578 8.399   0.42 15.43 ?  16  VAL   A HA   1 
ATOM   403  H HA   B VAL   A 1 16  ? 16.553 -14.572 8.428   0.58 16.46 ?  16  VAL   A HA   1 
ATOM   404  H HB   A VAL   A 1 16  ? 14.986 -15.964 6.496   0.42 16.19 ?  16  VAL   A HB   1 
ATOM   405  H HB   B VAL   A 1 16  ? 14.937 -15.941 6.557   0.58 17.25 ?  16  VAL   A HB   1 
ATOM   406  H HG11 A VAL   A 1 16  ? 15.348 -13.990 5.165   0.42 16.69 ?  16  VAL   A HG11 1 
ATOM   407  H HG11 B VAL   A 1 16  ? 15.250 -13.965 5.220   0.58 17.83 ?  16  VAL   A HG11 1 
ATOM   408  H HG12 A VAL   A 1 16  ? 14.344 -13.789 6.378   0.42 16.69 ?  16  VAL   A HG12 1 
ATOM   409  H HG12 B VAL   A 1 16  ? 14.278 -13.770 6.460   0.58 17.83 ?  16  VAL   A HG12 1 
ATOM   410  H HG13 A VAL   A 1 16  ? 15.845 -13.279 6.495   0.42 16.69 ?  16  VAL   A HG13 1 
ATOM   411  H HG13 B VAL   A 1 16  ? 15.778 -13.250 6.535   0.58 17.83 ?  16  VAL   A HG13 1 
ATOM   412  H HG21 A VAL   A 1 16  ? 16.848 -15.796 5.074   0.42 17.13 ?  16  VAL   A HG21 1 
ATOM   413  H HG21 B VAL   A 1 16  ? 16.767 -15.765 5.089   0.58 18.42 ?  16  VAL   A HG21 1 
ATOM   414  H HG22 A VAL   A 1 16  ? 17.692 -15.209 6.285   0.42 17.13 ?  16  VAL   A HG22 1 
ATOM   415  H HG22 B VAL   A 1 16  ? 17.638 -15.174 6.277   0.58 18.42 ?  16  VAL   A HG22 1 
ATOM   416  H HG23 A VAL   A 1 16  ? 17.162 -16.704 6.339   0.42 17.13 ?  16  VAL   A HG23 1 
ATOM   417  H HG23 B VAL   A 1 16  ? 17.117 -16.672 6.345   0.58 18.42 ?  16  VAL   A HG23 1 
ATOM   418  N N    A TYR   A 1 17  ? 14.625 -13.499 9.366   0.42 11.79 ?  17  TYR   A N    1 
ATOM   419  N N    B TYR   A 1 17  ? 14.625 -13.451 9.370   0.58 13.02 ?  17  TYR   A N    1 
ATOM   420  C CA   A TYR   A 1 17  ? 13.525 -12.805 10.017  0.42 12.17 ?  17  TYR   A CA   1 
ATOM   421  C CA   B TYR   A 1 17  ? 13.556 -12.775 10.088  0.58 12.93 ?  17  TYR   A CA   1 
ATOM   422  C C    A TYR   A 1 17  ? 13.252 -11.502 9.269   0.42 11.90 ?  17  TYR   A C    1 
ATOM   423  C C    B TYR   A 1 17  ? 13.271 -11.450 9.397   0.58 12.98 ?  17  TYR   A C    1 
ATOM   424  O O    A TYR   A 1 17  ? 14.100 -11.022 8.511   0.42 11.73 ?  17  TYR   A O    1 
ATOM   425  O O    B TYR   A 1 17  ? 14.186 -10.817 8.863   0.58 12.93 ?  17  TYR   A O    1 
ATOM   426  C CB   A TYR   A 1 17  ? 13.898 -12.507 11.478  0.42 13.07 ?  17  TYR   A CB   1 
ATOM   427  C CB   B TYR   A 1 17  ? 14.002 -12.510 11.524  0.58 13.36 ?  17  TYR   A CB   1 
ATOM   428  C CG   A TYR   A 1 17  ? 14.157 -13.756 12.302  0.42 14.41 ?  17  TYR   A CG   1 
ATOM   429  C CG   B TYR   A 1 17  ? 14.154 -13.770 12.329  0.58 14.77 ?  17  TYR   A CG   1 
ATOM   430  C CD1  A TYR   A 1 17  ? 15.367 -14.443 12.214  0.42 15.02 ?  17  TYR   A CD1  1 
ATOM   431  C CD1  B TYR   A 1 17  ? 15.321 -14.526 12.274  0.58 15.56 ?  17  TYR   A CD1  1 
ATOM   432  C CD2  A TYR   A 1 17  ? 13.184 -14.256 13.160  0.42 15.20 ?  17  TYR   A CD2  1 
ATOM   433  C CD2  B TYR   A 1 17  ? 13.117 -14.222 13.129  0.58 15.19 ?  17  TYR   A CD2  1 
ATOM   434  C CE1  A TYR   A 1 17  ? 15.597 -15.594 12.958  0.42 15.61 ?  17  TYR   A CE1  1 
ATOM   435  C CE1  B TYR   A 1 17  ? 15.447 -15.701 13.001  0.58 16.04 ?  17  TYR   A CE1  1 
ATOM   436  C CE2  A TYR   A 1 17  ? 13.406 -15.408 13.909  0.42 15.90 ?  17  TYR   A CE2  1 
ATOM   437  C CE2  B TYR   A 1 17  ? 13.233 -15.392 13.860  0.58 15.95 ?  17  TYR   A CE2  1 
ATOM   438  C CZ   A TYR   A 1 17  ? 14.616 -16.070 13.804  0.42 16.14 ?  17  TYR   A CZ   1 
ATOM   439  C CZ   B TYR   A 1 17  ? 14.399 -16.127 13.797  0.58 16.02 ?  17  TYR   A CZ   1 
ATOM   440  O OH   A TYR   A 1 17  ? 14.845 -17.212 14.547  0.42 16.94 ?  17  TYR   A OH   1 
ATOM   441  O OH   B TYR   A 1 17  ? 14.509 -17.292 14.528  0.58 16.40 ?  17  TYR   A OH   1 
ATOM   442  H H    A TYR   A 1 17  ? 15.334 -13.009 9.312   0.42 14.15 ?  17  TYR   A H    1 
ATOM   443  H H    B TYR   A 1 17  ? 15.301 -12.928 9.222   0.58 15.62 ?  17  TYR   A H    1 
ATOM   444  H HA   A TYR   A 1 17  ? 12.733 -13.364 9.993   0.42 14.60 ?  17  TYR   A HA   1 
ATOM   445  H HA   B TYR   A 1 17  ? 12.754 -13.318 10.094  0.58 15.52 ?  17  TYR   A HA   1 
ATOM   446  H HB2  A TYR   A 1 17  ? 14.701 -11.963 11.490  0.42 15.68 ?  17  TYR   A HB2  1 
ATOM   447  H HB2  B TYR   A 1 17  ? 14.859 -12.062 11.509  0.58 16.04 ?  17  TYR   A HB2  1 
ATOM   448  H HB3  A TYR   A 1 17  ? 13.167 -12.022 11.888  0.42 15.68 ?  17  TYR   A HB3  1 
ATOM   449  H HB3  B TYR   A 1 17  ? 13.341 -11.958 11.961  0.58 16.04 ?  17  TYR   A HB3  1 
ATOM   450  H HD1  A TYR   A 1 17  ? 16.030 -14.130 11.646  0.42 18.02 ?  17  TYR   A HD1  1 
ATOM   451  H HD1  B TYR   A 1 17  ? 16.026 -14.243 11.735  0.58 18.67 ?  17  TYR   A HD1  1 
ATOM   452  H HD2  A TYR   A 1 17  ? 12.367 -13.816 13.232  0.42 18.24 ?  17  TYR   A HD2  1 
ATOM   453  H HD2  B TYR   A 1 17  ? 12.327 -13.735 13.173  0.58 18.23 ?  17  TYR   A HD2  1 
ATOM   454  H HE1  A TYR   A 1 17  ? 16.410 -16.046 12.893  0.42 18.73 ?  17  TYR   A HE1  1 
ATOM   455  H HE1  B TYR   A 1 17  ? 16.236 -16.194 12.961  0.58 19.25 ?  17  TYR   A HE1  1 
ATOM   456  H HE2  A TYR   A 1 17  ? 12.744 -15.731 14.481  0.42 19.08 ?  17  TYR   A HE2  1 
ATOM   457  H HE2  B TYR   A 1 17  ? 12.529 -15.678 14.396  0.58 19.14 ?  17  TYR   A HE2  1 
ATOM   458  H HH   A TYR   A 1 17  ? 15.605 -17.525 14.380  0.42 20.33 ?  17  TYR   A HH   1 
ATOM   459  H HH   B TYR   A 1 17  ? 13.761 -17.496 14.843  0.58 19.68 ?  17  TYR   A HH   1 
ATOM   460  N N    A ILE   A 1 18  ? 12.069 -10.914 9.484   0.42 11.91 ?  18  ILE   A N    1 
ATOM   461  N N    B ILE   A 1 18  ? 12.002 -11.021 9.401   0.58 13.13 ?  18  ILE   A N    1 
ATOM   462  C CA   A ILE   A 1 18  ? 11.656 -9.731  8.721   0.42 12.18 ?  18  ILE   A CA   1 
ATOM   463  C CA   B ILE   A 1 18  ? 11.601 -9.837  8.643   0.58 13.69 ?  18  ILE   A CA   1 
ATOM   464  C C    A ILE   A 1 18  ? 10.690 -8.887  9.549   0.42 12.68 ?  18  ILE   A C    1 
ATOM   465  C C    B ILE   A 1 18  ? 10.635 -8.968  9.439   0.58 14.63 ?  18  ILE   A C    1 
ATOM   466  O O    A ILE   A 1 18  ? 9.854  -9.418  10.284  0.42 13.59 ?  18  ILE   A O    1 
ATOM   467  O O    B ILE   A 1 18  ? 9.854  -9.460  10.259  0.58 15.57 ?  18  ILE   A O    1 
ATOM   468  C CB   A ILE   A 1 18  ? 11.087 -10.137 7.343   0.42 12.94 ?  18  ILE   A CB   1 
ATOM   469  C CB   B ILE   A 1 18  ? 11.004 -10.261 7.287   0.58 14.33 ?  18  ILE   A CB   1 
ATOM   470  C CG1  A ILE   A 1 18  ? 10.952 -8.918  6.431   0.42 14.38 ?  18  ILE   A CG1  1 
ATOM   471  C CG1  B ILE   A 1 18  ? 10.971 -9.096  6.305   0.58 14.93 ?  18  ILE   A CG1  1 
ATOM   472  C CG2  A ILE   A 1 18  ? 9.766  -10.893 7.491   0.42 13.41 ?  18  ILE   A CG2  1 
ATOM   473  C CG2  B ILE   A 1 18  ? 9.630  -10.891 7.482   0.58 15.05 ?  18  ILE   A CG2  1 
ATOM   474  C CD1  A ILE   A 1 18  ? 10.746 -9.286  4.979   0.42 16.17 ?  18  ILE   A CD1  1 
ATOM   475  C CD1  B ILE   A 1 18  ? 10.700 -9.544  4.894   0.58 16.54 ?  18  ILE   A CD1  1 
ATOM   476  H H    A ILE   A 1 18  ? 11.500 -11.174 10.074  0.42 14.29 ?  18  ILE   A H    1 
ATOM   477  H H    B ILE   A 1 18  ? 11.355 -11.414 9.821   0.58 15.76 ?  18  ILE   A H    1 
ATOM   478  H HA   A ILE   A 1 18  ? 12.438 -9.190  8.556   0.42 14.62 ?  18  ILE   A HA   1 
ATOM   479  H HA   B ILE   A 1 18  ? 12.400 -9.311  8.466   0.58 16.43 ?  18  ILE   A HA   1 
ATOM   480  H HB   A ILE   A 1 18  ? 11.722 -10.739 6.928   0.42 15.53 ?  18  ILE   A HB   1 
ATOM   481  H HB   B ILE   A 1 18  ? 11.584 -10.937 6.915   0.58 17.20 ?  18  ILE   A HB   1 
ATOM   482  H HG12 A ILE   A 1 18  ? 10.191 -8.387  6.714   0.42 17.25 ?  18  ILE   A HG12 1 
ATOM   483  H HG12 B ILE   A 1 18  ? 10.269 -8.477  6.560   0.58 17.92 ?  18  ILE   A HG12 1 
ATOM   484  H HG13 A ILE   A 1 18  ? 11.764 -8.387  6.488   0.42 17.25 ?  18  ILE   A HG13 1 
ATOM   485  H HG13 B ILE   A 1 18  ? 11.830 -8.644  6.312   0.58 17.92 ?  18  ILE   A HG13 1 
ATOM   486  H HG21 A ILE   A 1 18  ? 9.505  -11.247 6.624   0.42 16.09 ?  18  ILE   A HG21 1 
ATOM   487  H HG21 B ILE   A 1 18  ? 9.371  -11.329 6.658   0.58 18.07 ?  18  ILE   A HG21 1 
ATOM   488  H HG22 A ILE   A 1 18  ? 9.889  -11.621 8.119   0.42 16.09 ?  18  ILE   A HG22 1 
ATOM   489  H HG22 B ILE   A 1 18  ? 9.683  -11.540 8.201   0.58 18.07 ?  18  ILE   A HG22 1 
ATOM   490  H HG23 A ILE   A 1 18  ? 9.084  -10.285 7.816   0.42 16.09 ?  18  ILE   A HG23 1 
ATOM   491  H HG23 B ILE   A 1 18  ? 8.992  -10.198 7.707   0.58 18.07 ?  18  ILE   A HG23 1 
ATOM   492  H HD11 A ILE   A 1 18  ? 10.720 -8.477  4.445   0.42 19.40 ?  18  ILE   A HD11 1 
ATOM   493  H HD11 B ILE   A 1 18  ? 10.766 -8.779  4.301   0.58 19.85 ?  18  ILE   A HD11 1 
ATOM   494  H HD12 A ILE   A 1 18  ? 11.479 -9.851  4.689   0.42 19.40 ?  18  ILE   A HD12 1 
ATOM   495  H HD12 B ILE   A 1 18  ? 11.356 -10.212 4.646   0.58 19.85 ?  18  ILE   A HD12 1 
ATOM   496  H HD13 A ILE   A 1 18  ? 9.906  -9.766  4.892   0.42 19.40 ?  18  ILE   A HD13 1 
ATOM   497  H HD13 B ILE   A 1 18  ? 9.808  -9.920  4.850   0.58 19.85 ?  18  ILE   A HD13 1 
ATOM   498  N N    A LYS   A 1 19  ? 10.801 -7.560  9.411   0.42 12.49 ?  19  LYS   A N    1 
ATOM   499  N N    B LYS   A 1 19  ? 10.679 -7.661  9.169   0.58 14.23 ?  19  LYS   A N    1 
ATOM   500  C CA   A LYS   A 1 19  ? 10.012 -6.612  10.189  0.42 12.80 ?  19  LYS   A CA   1 
ATOM   501  C CA   B LYS   A 1 19  ? 9.843  -6.684  9.858   0.58 14.34 ?  19  LYS   A CA   1 
ATOM   502  C C    A LYS   A 1 19  ? 9.821  -5.342  9.371   0.42 12.28 ?  19  LYS   A C    1 
ATOM   503  C C    B LYS   A 1 19  ? 9.650  -5.474  8.954   0.58 13.64 ?  19  LYS   A C    1 
ATOM   504  O O    A LYS   A 1 19  ? 10.727 -4.932  8.642   0.42 12.69 ?  19  LYS   A O    1 
ATOM   505  O O    B LYS   A 1 19  ? 10.554 -5.110  8.198   0.58 13.23 ?  19  LYS   A O    1 
ATOM   506  C CB   A LYS   A 1 19  ? 10.744 -6.278  11.497  0.42 13.38 ?  19  LYS   A CB   1 
ATOM   507  C CB   B LYS   A 1 19  ? 10.518 -6.238  11.164  0.58 14.73 ?  19  LYS   A CB   1 
ATOM   508  C CG   A LYS   A 1 19  ? 10.063 -5.281  12.416  0.42 14.05 ?  19  LYS   A CG   1 
ATOM   509  C CG   B LYS   A 1 19  ? 9.701  -5.319  12.065  0.58 16.17 ?  19  LYS   A CG   1 
ATOM   510  C CD   A LYS   A 1 19  ? 10.990 -4.955  13.580  0.42 14.90 ?  19  LYS   A CD   1 
ATOM   511  C CD   B LYS   A 1 19  ? 10.503 -4.998  13.323  0.58 17.51 ?  19  LYS   A CD   1 
ATOM   512  C CE   A LYS   A 1 19  ? 10.319 -4.097  14.629  0.42 15.29 ?  19  LYS   A CE   1 
ATOM   513  C CE   B LYS   A 1 19  ? 9.774  -4.066  14.276  0.58 18.01 ?  19  LYS   A CE   1 
ATOM   514  N NZ   A LYS   A 1 19  ? 11.217 -3.904  15.801  0.42 15.51 ?  19  LYS   A NZ   1 
ATOM   515  N NZ   B LYS   A 1 19  ? 10.666 -3.651  15.398  0.58 18.28 ?  19  LYS   A NZ   1 
ATOM   516  H H    A LYS   A 1 19  ? 11.344 -7.171  8.864   0.42 14.99 ?  19  LYS   A H    1 
ATOM   517  H H    B LYS   A 1 19  ? 11.200 -7.317  8.579   0.58 17.08 ?  19  LYS   A H    1 
ATOM   518  H HA   A LYS   A 1 19  ? 9.142  -6.981  10.399  0.42 15.36 ?  19  LYS   A HA   1 
ATOM   519  H HA   B LYS   A 1 19  ? 8.982  -7.085  10.064  0.58 17.20 ?  19  LYS   A HA   1 
ATOM   520  H HB2  A LYS   A 1 19  ? 10.846 -7.101  12.003  0.42 16.06 ?  19  LYS   A HB2  1 
ATOM   521  H HB2  B LYS   A 1 19  ? 10.731 -7.031  11.683  0.58 17.67 ?  19  LYS   A HB2  1 
ATOM   522  H HB3  A LYS   A 1 19  ? 11.618 -5.921  11.282  0.42 16.06 ?  19  LYS   A HB3  1 
ATOM   523  H HB3  B LYS   A 1 19  ? 11.334 -5.772  10.938  0.58 17.67 ?  19  LYS   A HB3  1 
ATOM   524  H HG2  A LYS   A 1 19  ? 9.877  -4.460  11.934  0.42 16.86 ?  19  LYS   A HG2  1 
ATOM   525  H HG2  B LYS   A 1 19  ? 9.510  -4.489  11.599  0.58 19.41 ?  19  LYS   A HG2  1 
ATOM   526  H HG3  A LYS   A 1 19  ? 9.245  -5.664  12.770  0.42 16.86 ?  19  LYS   A HG3  1 
ATOM   527  H HG3  B LYS   A 1 19  ? 8.877  -5.760  12.328  0.58 19.41 ?  19  LYS   A HG3  1 
ATOM   528  H HD2  A LYS   A 1 19  ? 11.269 -5.783  14.002  0.42 17.88 ?  19  LYS   A HD2  1 
ATOM   529  H HD2  B LYS   A 1 19  ? 10.691 -5.823  13.797  0.58 21.01 ?  19  LYS   A HD2  1 
ATOM   530  H HD3  A LYS   A 1 19  ? 11.763 -4.475  13.244  0.42 17.88 ?  19  LYS   A HD3  1 
ATOM   531  H HD3  B LYS   A 1 19  ? 11.335 -4.569  13.064  0.58 21.01 ?  19  LYS   A HD3  1 
ATOM   532  H HE2  A LYS   A 1 19  ? 10.116 -3.227  14.249  0.42 18.34 ?  19  LYS   A HE2  1 
ATOM   533  H HE2  B LYS   A 1 19  ? 9.495  -3.269  13.799  0.58 21.61 ?  19  LYS   A HE2  1 
ATOM   534  H HE3  A LYS   A 1 19  ? 9.507  -4.533  14.930  0.42 18.34 ?  19  LYS   A HE3  1 
ATOM   535  H HE3  B LYS   A 1 19  ? 9.006  -4.523  14.651  0.58 21.61 ?  19  LYS   A HE3  1 
ATOM   536  H HZ1  A LYS   A 1 19  ? 10.803 -3.414  16.419  0.42 18.61 ?  19  LYS   A HZ1  1 
ATOM   537  H HZ1  B LYS   A 1 19  ? 10.230 -3.108  15.952  0.58 21.94 ?  19  LYS   A HZ1  1 
ATOM   538  H HZ2  A LYS   A 1 19  ? 11.432 -4.692  16.151  0.42 18.61 ?  19  LYS   A HZ2  1 
ATOM   539  H HZ2  B LYS   A 1 19  ? 10.940 -4.368  15.852  0.58 21.94 ?  19  LYS   A HZ2  1 
ATOM   540  H HZ3  A LYS   A 1 19  ? 11.959 -3.484  15.549  0.42 18.61 ?  19  LYS   A HZ3  1 
ATOM   541  H HZ3  B LYS   A 1 19  ? 11.380 -3.224  15.079  0.58 21.94 ?  19  LYS   A HZ3  1 
ATOM   542  N N    A ASN   A 1 20  ? 8.641  -4.728  9.483   0.42 12.85 ?  20  ASN   A N    1 
ATOM   543  N N    B ASN   A 1 20  ? 8.464  -4.866  9.023   0.58 14.19 ?  20  ASN   A N    1 
ATOM   544  C CA   A ASN   A 1 20  ? 8.426  -3.397  8.921   0.42 12.55 ?  20  ASN   A CA   1 
ATOM   545  C CA   B ASN   A 1 20  ? 8.221  -3.586  8.356   0.58 14.85 ?  20  ASN   A CA   1 
ATOM   546  C C    A ASN   A 1 20  ? 9.068  -2.393  9.866   0.42 12.96 ?  20  ASN   A C    1 
ATOM   547  C C    B ASN   A 1 20  ? 8.793  -2.496  9.253   0.58 15.22 ?  20  ASN   A C    1 
ATOM   548  O O    A ASN   A 1 20  ? 8.586  -2.188  10.985  0.42 12.75 ?  20  ASN   A O    1 
ATOM   549  O O    B ASN   A 1 20  ? 8.169  -2.096  10.240  0.58 16.68 ?  20  ASN   A O    1 
ATOM   550  C CB   A ASN   A 1 20  ? 6.936  -3.119  8.734   0.42 12.84 ?  20  ASN   A CB   1 
ATOM   551  C CB   B ASN   A 1 20  ? 6.729  -3.381  8.109   0.58 15.51 ?  20  ASN   A CB   1 
ATOM   552  C CG   A ASN   A 1 20  ? 6.644  -1.663  8.380   0.42 13.93 ?  20  ASN   A CG   1 
ATOM   553  C CG   B ASN   A 1 20  ? 6.395  -1.974  7.643   0.58 16.60 ?  20  ASN   A CG   1 
ATOM   554  O OD1  A ASN   A 1 20  ? 5.753  -1.043  8.963   0.42 16.17 ?  20  ASN   A OD1  1 
ATOM   555  O OD1  B ASN   A 1 20  ? 5.433  -1.353  8.125   0.58 18.10 ?  20  ASN   A OD1  1 
ATOM   556  N ND2  A ASN   A 1 20  ? 7.401  -1.109  7.433   0.42 13.96 ?  20  ASN   A ND2  1 
ATOM   557  N ND2  B ASN   A 1 20  ? 7.176  -1.466  6.691   0.58 16.62 ?  20  ASN   A ND2  1 
ATOM   558  H H    A ASN   A 1 20  ? 7.950  -5.057  9.878   0.42 15.42 ?  20  ASN   A H    1 
ATOM   559  H H    B ASN   A 1 20  ? 7.783  -5.186  9.450   0.58 17.03 ?  20  ASN   A H    1 
ATOM   560  H HA   A ASN   A 1 20  ? 8.858  -3.331  8.059   0.42 15.06 ?  20  ASN   A HA   1 
ATOM   561  H HA   B ASN   A 1 20  ? 8.685  -3.579  7.504   0.58 17.82 ?  20  ASN   A HA   1 
ATOM   562  H HB2  A ASN   A 1 20  ? 6.597  -3.680  8.014   0.42 15.40 ?  20  ASN   A HB2  1 
ATOM   563  H HB2  B ASN   A 1 20  ? 6.433  -3.989  7.420   0.58 18.61 ?  20  ASN   A HB2  1 
ATOM   564  H HB3  A ASN   A 1 20  ? 6.464  -3.319  9.556   0.42 15.40 ?  20  ASN   A HB3  1 
ATOM   565  H HB3  B ASN   A 1 20  ? 6.249  -3.556  8.935   0.58 18.61 ?  20  ASN   A HB3  1 
ATOM   566  H HD21 A ASN   A 1 20  ? 7.262  -0.294  7.193   0.42 16.75 ?  20  ASN   A HD21 1 
ATOM   567  H HD21 B ASN   A 1 20  ? 7.036  -0.670  6.404   0.58 19.95 ?  20  ASN   A HD21 1 
ATOM   568  H HD22 A ASN   A 1 20  ? 8.024  -1.566  7.057   0.42 16.75 ?  20  ASN   A HD22 1 
ATOM   569  H HD22 B ASN   A 1 20  ? 7.814  -1.939  6.358   0.58 19.95 ?  20  ASN   A HD22 1 
ATOM   570  N N    A ALA   A 1 21  ? 10.173 -1.787  9.439   0.42 13.32 ?  21  ALA   A N    1 
ATOM   571  N N    B ALA   A 1 21  ? 9.994  -2.024  8.924   0.58 14.70 ?  21  ALA   A N    1 
ATOM   572  C CA   A ALA   A 1 21  ? 10.882 -0.874  10.319  0.42 13.72 ?  21  ALA   A CA   1 
ATOM   573  C CA   B ALA   A 1 21  ? 10.670 -1.052  9.772   0.58 14.66 ?  21  ALA   A CA   1 
ATOM   574  C C    A ALA   A 1 21  ? 11.844 -0.024  9.510   0.42 14.26 ?  21  ALA   A C    1 
ATOM   575  C C    B ALA   A 1 21  ? 11.730 -0.319  8.967   0.58 13.09 ?  21  ALA   A C    1 
ATOM   576  O O    A ALA   A 1 21  ? 12.313 -0.430  8.444   0.42 14.99 ?  21  ALA   A O    1 
ATOM   577  O O    B ALA   A 1 21  ? 12.201 -0.808  7.938   0.58 12.59 ?  21  ALA   A O    1 
ATOM   578  C CB   A ALA   A 1 21  ? 11.652 -1.640  11.395  0.42 14.38 ?  21  ALA   A CB   1 
ATOM   579  C CB   B ALA   A 1 21  ? 11.315 -1.723  10.988  0.58 16.39 ?  21  ALA   A CB   1 
ATOM   580  H H    A ALA   A 1 21  ? 10.525 -1.888  8.658   0.42 15.98 ?  21  ALA   A H    1 
ATOM   581  H H    B ALA   A 1 21  ? 10.426 -2.252  8.216   0.58 17.65 ?  21  ALA   A H    1 
ATOM   582  H HA   A ALA   A 1 21  ? 10.243 -0.282  10.752  0.42 16.47 ?  21  ALA   A HA   1 
ATOM   583  H HA   B ALA   A 1 21  ? 10.014 -0.410  10.087  0.58 17.59 ?  21  ALA   A HA   1 
ATOM   584  H HB1  A ALA   A 1 21  ? 12.013 -1.001  12.023  0.42 17.26 ?  21  ALA   A HB1  1 
ATOM   585  H HB1  B ALA   A 1 21  ? 11.749 -1.041  11.523  0.58 19.66 ?  21  ALA   A HB1  1 
ATOM   586  H HB2  A ALA   A 1 21  ? 11.036 -2.239  11.845  0.42 17.26 ?  21  ALA   A HB2  1 
ATOM   587  H HB2  B ALA   A 1 21  ? 10.624 -2.163  11.510  0.58 19.66 ?  21  ALA   A HB2  1 
ATOM   588  H HB3  A ALA   A 1 21  ? 12.360 -2.146  10.972  0.42 17.26 ?  21  ALA   A HB3  1 
ATOM   589  H HB3  B ALA   A 1 21  ? 11.964 -2.372  10.683  0.58 19.66 ?  21  ALA   A HB3  1 
ATOM   590  N N    A ASP   A 1 22  ? 12.110 1.170   10.034  0.42 14.53 ?  22  ASP   A N    1 
ATOM   591  N N    B ASP   A 1 22  ? 12.087 0.870   9.462   0.58 12.76 ?  22  ASP   A N    1 
ATOM   592  C CA   A ASP   A 1 22  ? 13.173 2.031   9.537   0.42 14.84 ?  22  ASP   A CA   1 
ATOM   593  C CA   B ASP   A 1 22  ? 13.197 1.658   8.935   0.58 12.35 ?  22  ASP   A CA   1 
ATOM   594  C C    A ASP   A 1 22  ? 14.495 1.521   10.094  0.42 14.45 ?  22  ASP   A C    1 
ATOM   595  C C    B ASP   A 1 22  ? 14.491 1.153   9.572   0.58 11.79 ?  22  ASP   A C    1 
ATOM   596  O O    A ASP   A 1 22  ? 14.698 1.514   11.313  0.42 14.64 ?  22  ASP   A O    1 
ATOM   597  O O    B ASP   A 1 22  ? 14.622 1.162   10.801  0.58 12.33 ?  22  ASP   A O    1 
ATOM   598  C CB   A ASP   A 1 22  ? 12.917 3.458   10.014  0.42 16.59 ?  22  ASP   A CB   1 
ATOM   599  C CB   B ASP   A 1 22  ? 12.961 3.126   9.295   0.58 13.46 ?  22  ASP   A CB   1 
ATOM   600  C CG   A ASP   A 1 22  ? 13.937 4.449   9.482   0.42 17.79 ?  22  ASP   A CG   1 
ATOM   601  C CG   B ASP   A 1 22  ? 13.980 4.070   8.677   0.58 14.00 ?  22  ASP   A CG   1 
ATOM   602  O OD1  A ASP   A 1 22  ? 14.950 4.020   8.897   0.42 17.55 ?  22  ASP   A OD1  1 
ATOM   603  O OD1  B ASP   A 1 22  ? 15.122 3.639   8.397   0.58 13.24 ?  22  ASP   A OD1  1 
ATOM   604  O OD2  A ASP   A 1 22  ? 13.715 5.667   9.643   0.42 19.13 -1 22  ASP   A OD2  1 
ATOM   605  O OD2  B ASP   A 1 22  ? 13.629 5.254   8.475   0.58 16.65 -1 22  ASP   A OD2  1 
ATOM   606  H H    A ASP   A 1 22  ? 11.668 1.514   10.688  0.42 17.44 ?  22  ASP   A H    1 
ATOM   607  H H    B ASP   A 1 22  ? 11.678 1.248   10.123  0.58 15.32 ?  22  ASP   A H    1 
ATOM   608  H HA   A ASP   A 1 22  ? 13.202 2.012   8.567   0.42 17.81 ?  22  ASP   A HA   1 
ATOM   609  H HA   B ASP   A 1 22  ? 13.247 1.553   7.973   0.58 14.82 ?  22  ASP   A HA   1 
ATOM   610  H HB2  A ASP   A 1 22  ? 12.044 3.741   9.707   0.42 19.91 ?  22  ASP   A HB2  1 
ATOM   611  H HB2  B ASP   A 1 22  ? 12.089 3.386   8.978   0.58 16.15 ?  22  ASP   A HB2  1 
ATOM   612  H HB3  A ASP   A 1 22  ? 12.943 3.469   10.988  0.42 19.91 ?  22  ASP   A HB3  1 
ATOM   613  H HB3  B ASP   A 1 22  ? 13.011 3.217   10.260  0.58 16.15 ?  22  ASP   A HB3  1 
ATOM   614  N N    A ILE   A 1 23  ? 15.391 1.086   9.204   0.42 13.57 ?  23  ILE   A N    1 
ATOM   615  N N    B ILE   A 1 23  ? 15.446 0.704   8.745   0.58 11.99 ?  23  ILE   A N    1 
ATOM   616  C CA   A ILE   A 1 23  ? 16.649 0.488   9.642   0.42 13.27 ?  23  ILE   A CA   1 
ATOM   617  C CA   B ILE   A 1 23  ? 16.689 0.135   9.269   0.58 11.77 ?  23  ILE   A CA   1 
ATOM   618  C C    A ILE   A 1 23  ? 17.441 1.452   10.513  0.42 13.05 ?  23  ILE   A C    1 
ATOM   619  C C    B ILE   A 1 23  ? 17.402 1.120   10.187  0.58 11.96 ?  23  ILE   A C    1 
ATOM   620  O O    A ILE   A 1 23  ? 18.183 1.028   11.407  0.42 13.29 ?  23  ILE   A O    1 
ATOM   621  O O    B ILE   A 1 23  ? 18.061 0.715   11.152  0.58 12.22 ?  23  ILE   A O    1 
ATOM   622  C CB   A ILE   A 1 23  ? 17.457 -0.016  8.426   0.42 12.91 ?  23  ILE   A CB   1 
ATOM   623  C CB   B ILE   A 1 23  ? 17.609 -0.380  8.133   0.58 11.66 ?  23  ILE   A CB   1 
ATOM   624  C CG1  A ILE   A 1 23  ? 18.622 -0.902  8.883   0.42 13.02 ?  23  ILE   A CG1  1 
ATOM   625  C CG1  B ILE   A 1 23  ? 18.656 -1.348  8.702   0.58 11.82 ?  23  ILE   A CG1  1 
ATOM   626  C CG2  A ILE   A 1 23  ? 17.934 1.152   7.565   0.42 13.17 ?  23  ILE   A CG2  1 
ATOM   627  C CG2  B ILE   A 1 23  ? 18.284 0.775   7.393   0.58 11.85 ?  23  ILE   A CG2  1 
ATOM   628  C CD1  A ILE   A 1 23  ? 19.312 -1.625  7.742   0.42 13.26 ?  23  ILE   A CD1  1 
ATOM   629  C CD1  B ILE   A 1 23  ? 19.580 -1.958  7.655   0.58 11.68 ?  23  ILE   A CD1  1 
ATOM   630  H H    A ILE   A 1 23  ? 15.293 1.126   8.353   0.42 16.28 ?  23  ILE   A H    1 
ATOM   631  H H    B ILE   A 1 23  ? 15.395 0.706   7.895   0.58 14.39 ?  23  ILE   A H    1 
ATOM   632  H HA   A ILE   A 1 23  ? 16.446 -0.285  10.188  0.42 15.93 ?  23  ILE   A HA   1 
ATOM   633  H HA   B ILE   A 1 23  ? 16.460 -0.642  9.804   0.58 14.13 ?  23  ILE   A HA   1 
ATOM   634  H HB   A ILE   A 1 23  ? 16.869 -0.560  7.885   0.42 15.49 ?  23  ILE   A HB   1 
ATOM   635  H HB   B ILE   A 1 23  ? 17.068 -0.874  7.496   0.58 13.99 ?  23  ILE   A HB   1 
ATOM   636  H HG12 A ILE   A 1 23  ? 19.284 -0.352  9.329   0.42 15.63 ?  23  ILE   A HG12 1 
ATOM   637  H HG12 B ILE   A 1 23  ? 19.210 -0.876  9.341   0.58 14.19 ?  23  ILE   A HG12 1 
ATOM   638  H HG13 A ILE   A 1 23  ? 18.284 -1.574  9.497   0.42 15.63 ?  23  ILE   A HG13 1 
ATOM   639  H HG13 B ILE   A 1 23  ? 18.199 -2.083  9.147   0.58 14.19 ?  23  ILE   A HG13 1 
ATOM   640  H HG21 A ILE   A 1 23  ? 18.301 0.805   6.735   0.42 15.80 ?  23  ILE   A HG21 1 
ATOM   641  H HG21 B ILE   A 1 23  ? 18.676 0.439   6.566   0.58 14.22 ?  23  ILE   A HG21 1 
ATOM   642  H HG22 A ILE   A 1 23  ? 17.178 1.730   7.372   0.42 15.80 ?  23  ILE   A HG22 1 
ATOM   643  H HG22 B ILE   A 1 23  ? 17.623 1.449   7.192   0.58 14.22 ?  23  ILE   A HG22 1 
ATOM   644  H HG23 A ILE   A 1 23  ? 18.615 1.648   8.045   0.42 15.80 ?  23  ILE   A HG23 1 
ATOM   645  H HG23 B ILE   A 1 23  ? 18.983 1.149   7.953   0.58 14.22 ?  23  ILE   A HG23 1 
ATOM   646  H HD11 A ILE   A 1 23  ? 19.990 -2.215  8.107   0.42 15.91 ?  23  ILE   A HD11 1 
ATOM   647  H HD11 B ILE   A 1 23  ? 20.137 -2.634  8.078   0.58 14.01 ?  23  ILE   A HD11 1 
ATOM   648  H HD12 A ILE   A 1 23  ? 18.653 -2.141  7.252   0.42 15.91 ?  23  ILE   A HD12 1 
ATOM   649  H HD12 B ILE   A 1 23  ? 19.044 -2.363  6.957   0.58 14.01 ?  23  ILE   A HD12 1 
ATOM   650  H HD13 A ILE   A 1 23  ? 19.723 -0.970  7.157   0.42 15.91 ?  23  ILE   A HD13 1 
ATOM   651  H HD13 B ILE   A 1 23  ? 20.139 -1.259  7.282   0.58 14.01 ?  23  ILE   A HD13 1 
ATOM   652  N N    A VAL   A 1 24  ? 17.293 2.757   10.281  0.42 13.50 ?  24  VAL   A N    1 
ATOM   653  N N    B VAL   A 1 24  ? 17.276 2.421   9.918   0.58 12.48 ?  24  VAL   A N    1 
ATOM   654  C CA   A VAL   A 1 24  ? 17.963 3.743   11.124  0.42 14.49 ?  24  VAL   A CA   1 
ATOM   655  C CA   B VAL   A 1 24  ? 17.933 3.418   10.757  0.58 13.75 ?  24  VAL   A CA   1 
ATOM   656  C C    A VAL   A 1 24  ? 17.443 3.658   12.553  0.42 15.40 ?  24  VAL   A C    1 
ATOM   657  C C    B VAL   A 1 24  ? 17.341 3.413   12.159  0.58 14.36 ?  24  VAL   A C    1 
ATOM   658  O O    A VAL   A 1 24  ? 18.218 3.571   13.514  0.42 15.31 ?  24  VAL   A O    1 
ATOM   659  O O    B VAL   A 1 24  ? 18.070 3.475   13.157  0.58 15.75 ?  24  VAL   A O    1 
ATOM   660  C CB   A VAL   A 1 24  ? 17.787 5.154   10.538  0.42 14.78 ?  24  VAL   A CB   1 
ATOM   661  C CB   B VAL   A 1 24  ? 17.852 4.807   10.101  0.58 14.55 ?  24  VAL   A CB   1 
ATOM   662  C CG1  A VAL   A 1 24  ? 18.257 6.210   11.531  0.42 14.83 ?  24  VAL   A CG1  1 
ATOM   663  C CG1  B VAL   A 1 24  ? 18.560 5.838   10.961  0.58 15.94 ?  24  VAL   A CG1  1 
ATOM   664  C CG2  A VAL   A 1 24  ? 18.532 5.273   9.217   0.42 15.12 ?  24  VAL   A CG2  1 
ATOM   665  C CG2  B VAL   A 1 24  ? 18.440 4.766   8.702   0.58 14.66 ?  24  VAL   A CG2  1 
ATOM   666  H H    A VAL   A 1 24  ? 16.814 3.094   9.652   0.42 16.20 ?  24  VAL   A H    1 
ATOM   667  H H    B VAL   A 1 24  ? 16.817 2.743   9.269   0.58 14.97 ?  24  VAL   A H    1 
ATOM   668  H HA   A VAL   A 1 24  ? 18.911 3.551   11.143  0.42 17.39 ?  24  VAL   A HA   1 
ATOM   669  H HA   B VAL   A 1 24  ? 18.868 3.184   10.839  0.58 16.50 ?  24  VAL   A HA   1 
ATOM   670  H HB   A VAL   A 1 24  ? 16.847 5.312   10.361  0.42 17.74 ?  24  VAL   A HB   1 
ATOM   671  H HB   B VAL   A 1 24  ? 16.921 5.067   10.028  0.58 17.46 ?  24  VAL   A HB   1 
ATOM   672  H HG11 A VAL   A 1 24  ? 18.404 7.044   11.058  0.42 17.80 ?  24  VAL   A HG11 1 
ATOM   673  H HG11 B VAL   A 1 24  ? 18.655 6.657   10.453  0.58 19.13 ?  24  VAL   A HG11 1 
ATOM   674  H HG12 A VAL   A 1 24  ? 17.575 6.333   12.210  0.42 17.80 ?  24  VAL   A HG12 1 
ATOM   675  H HG12 B VAL   A 1 24  ? 18.030 6.004   11.758  0.58 19.13 ?  24  VAL   A HG12 1 
ATOM   676  H HG13 A VAL   A 1 24  ? 19.085 5.912   11.939  0.42 17.80 ?  24  VAL   A HG13 1 
ATOM   677  H HG13 B VAL   A 1 24  ? 19.432 5.497   11.208  0.58 19.13 ?  24  VAL   A HG13 1 
ATOM   678  H HG21 A VAL   A 1 24  ? 18.274 6.100   8.780   0.42 18.14 ?  24  VAL   A HG21 1 
ATOM   679  H HG21 B VAL   A 1 24  ? 18.493 5.668   8.356   0.58 17.60 ?  24  VAL   A HG21 1 
ATOM   680  H HG22 A VAL   A 1 24  ? 19.487 5.279   9.392   0.42 18.14 ?  24  VAL   A HG22 1 
ATOM   681  H HG22 B VAL   A 1 24  ? 19.327 4.374   8.746   0.58 17.60 ?  24  VAL   A HG22 1 
ATOM   682  H HG23 A VAL   A 1 24  ? 18.304 4.517   8.654   0.42 18.14 ?  24  VAL   A HG23 1 
ATOM   683  H HG23 B VAL   A 1 24  ? 17.868 4.225   8.135   0.58 17.60 ?  24  VAL   A HG23 1 
ATOM   684  N N    A GLU   A 1 25  ? 16.119 3.703   12.713  0.42 16.31 ?  25  GLU   A N    1 
ATOM   685  N N    B GLU   A 1 25  ? 16.010 3.336   12.260  0.58 14.73 ?  25  GLU   A N    1 
ATOM   686  C CA   A GLU   A 1 25  ? 15.534 3.622   14.047  0.42 17.71 ?  25  GLU   A CA   1 
ATOM   687  C CA   B GLU   A 1 25  ? 15.365 3.291   13.570  0.58 15.34 ?  25  GLU   A CA   1 
ATOM   688  C C    A GLU   A 1 25  ? 15.744 2.251   14.675  0.42 16.75 ?  25  GLU   A C    1 
ATOM   689  C C    B GLU   A 1 25  ? 15.640 1.969   14.276  0.58 14.78 ?  25  GLU   A C    1 
ATOM   690  O O    A GLU   A 1 25  ? 15.917 2.154   15.895  0.42 17.29 ?  25  GLU   A O    1 
ATOM   691  O O    B GLU   A 1 25  ? 15.856 1.945   15.493  0.58 15.94 ?  25  GLU   A O    1 
ATOM   692  C CB   A GLU   A 1 25  ? 14.050 3.986   13.995  0.42 20.04 ?  25  GLU   A CB   1 
ATOM   693  C CB   B GLU   A 1 25  ? 13.861 3.547   13.434  0.58 17.07 ?  25  GLU   A CB   1 
ATOM   694  C CG   A GLU   A 1 25  ? 13.797 5.451   13.649  0.42 22.39 ?  25  GLU   A CG   1 
ATOM   695  C CG   B GLU   A 1 25  ? 13.525 4.948   12.948  0.58 20.37 ?  25  GLU   A CG   1 
ATOM   696  C CD   A GLU   A 1 25  ? 14.601 6.414   14.514  0.42 24.22 ?  25  GLU   A CD   1 
ATOM   697  C CD   B GLU   A 1 25  ? 14.125 6.028   13.818  0.58 23.64 ?  25  GLU   A CD   1 
ATOM   698  O OE1  A GLU   A 1 25  ? 14.749 6.151   15.728  0.42 24.61 ?  25  GLU   A OE1  1 
ATOM   699  O OE1  B GLU   A 1 25  ? 14.137 5.852   15.057  0.58 25.30 ?  25  GLU   A OE1  1 
ATOM   700  O OE2  A GLU   A 1 25  ? 15.099 7.426   13.977  0.42 25.48 -1 25  GLU   A OE2  1 
ATOM   701  O OE2  B GLU   A 1 25  ? 14.582 7.047   13.264  0.58 24.79 -1 25  GLU   A OE2  1 
ATOM   702  H H    A GLU   A 1 25  ? 15.549 3.790   12.075  0.42 19.58 ?  25  GLU   A H    1 
ATOM   703  H H    B GLU   A 1 25  ? 15.465 3.311   11.594  0.58 17.68 ?  25  GLU   A H    1 
ATOM   704  H HA   A GLU   A 1 25  ? 15.982 4.261   14.620  0.42 21.25 ?  25  GLU   A HA   1 
ATOM   705  H HA   B GLU   A 1 25  ? 15.737 3.987   14.125  0.58 18.41 ?  25  GLU   A HA   1 
ATOM   706  H HB2  A GLU   A 1 25  ? 13.615 3.440   13.317  0.42 24.05 ?  25  GLU   A HB2  1 
ATOM   707  H HB2  B GLU   A 1 25  ? 13.487 2.920   12.796  0.58 20.49 ?  25  GLU   A HB2  1 
ATOM   708  H HB3  A GLU   A 1 25  ? 13.650 3.811   14.861  0.42 24.05 ?  25  GLU   A HB3  1 
ATOM   709  H HB3  B GLU   A 1 25  ? 13.440 3.426   14.300  0.58 20.49 ?  25  GLU   A HB3  1 
ATOM   710  H HG2  A GLU   A 1 25  ? 14.050 5.603   12.726  0.42 26.87 ?  25  GLU   A HG2  1 
ATOM   711  H HG2  B GLU   A 1 25  ? 13.863 5.063   12.047  0.58 24.44 ?  25  GLU   A HG2  1 
ATOM   712  H HG3  A GLU   A 1 25  ? 12.854 5.644   13.772  0.42 26.87 ?  25  GLU   A HG3  1 
ATOM   713  H HG3  B GLU   A 1 25  ? 12.568 5.077   12.969  0.58 24.44 ?  25  GLU   A HG3  1 
ATOM   714  N N    A GLU   A 1 26  ? 15.739 1.185   13.870  0.42 15.89 ?  26  GLU   A N    1 
ATOM   715  N N    B GLU   A 1 26  ? 15.629 0.860   13.535  0.58 14.57 ?  26  GLU   A N    1 
ATOM   716  C CA   A GLU   A 1 26  ? 16.045 -0.140  14.402  0.42 15.78 ?  26  GLU   A CA   1 
ATOM   717  C CA   B GLU   A 1 26  ? 16.000 -0.421  14.129  0.58 14.74 ?  26  GLU   A CA   1 
ATOM   718  C C    A GLU   A 1 26  ? 17.459 -0.186  14.964  0.42 15.11 ?  26  GLU   A C    1 
ATOM   719  C C    B GLU   A 1 26  ? 17.421 -0.373  14.679  0.58 13.71 ?  26  GLU   A C    1 
ATOM   720  O O    A GLU   A 1 26  ? 17.676 -0.633  16.096  0.42 14.75 ?  26  GLU   A O    1 
ATOM   721  O O    B GLU   A 1 26  ? 17.691 -0.896  15.766  0.58 14.20 ?  26  GLU   A O    1 
ATOM   722  C CB   A GLU   A 1 26  ? 15.890 -1.202  13.312  0.42 16.78 ?  26  GLU   A CB   1 
ATOM   723  C CB   B GLU   A 1 26  ? 15.862 -1.543  13.097  0.58 16.74 ?  26  GLU   A CB   1 
ATOM   724  C CG   A GLU   A 1 26  ? 14.499 -1.764  13.147  0.42 18.93 ?  26  GLU   A CG   1 
ATOM   725  C CG   B GLU   A 1 26  ? 14.436 -1.966  12.818  0.58 18.48 ?  26  GLU   A CG   1 
ATOM   726  C CD   A GLU   A 1 26  ? 14.059 -2.616  14.329  0.42 20.25 ?  26  GLU   A CD   1 
ATOM   727  C CD   B GLU   A 1 26  ? 13.759 -2.541  14.044  0.58 19.72 ?  26  GLU   A CD   1 
ATOM   728  O OE1  A GLU   A 1 26  ? 14.405 -3.819  14.385  0.42 20.54 ?  26  GLU   A OE1  1 
ATOM   729  O OE1  B GLU   A 1 26  ? 14.320 -3.480  14.651  0.58 20.39 ?  26  GLU   A OE1  1 
ATOM   730  O OE2  A GLU   A 1 26  ? 13.367 -2.076  15.208  0.42 20.44 -1 26  GLU   A OE2  1 
ATOM   731  O OE2  B GLU   A 1 26  ? 12.678 -2.038  14.407  0.58 19.00 -1 26  GLU   A OE2  1 
ATOM   732  H H    A GLU   A 1 26  ? 15.569 1.207   13.028  0.42 19.07 ?  26  GLU   A H    1 
ATOM   733  H H    B GLU   A 1 26  ? 15.414 0.819   12.703  0.58 17.48 ?  26  GLU   A H    1 
ATOM   734  H HA   A GLU   A 1 26  ? 15.428 -0.343  15.120  0.42 18.93 ?  26  GLU   A HA   1 
ATOM   735  H HA   B GLU   A 1 26  ? 15.403 -0.617  14.866  0.58 17.69 ?  26  GLU   A HA   1 
ATOM   736  H HB2  A GLU   A 1 26  ? 16.151 -0.809  12.464  0.42 20.14 ?  26  GLU   A HB2  1 
ATOM   737  H HB2  B GLU   A 1 26  ? 16.248 -1.245  12.256  0.58 20.09 ?  26  GLU   A HB2  1 
ATOM   738  H HB3  A GLU   A 1 26  ? 16.482 -1.940  13.522  0.42 20.14 ?  26  GLU   A HB3  1 
ATOM   739  H HB3  B GLU   A 1 26  ? 16.345 -2.325  13.414  0.58 20.09 ?  26  GLU   A HB3  1 
ATOM   740  H HG2  A GLU   A 1 26  ? 13.887 -1.019  13.041  0.42 22.72 ?  26  GLU   A HG2  1 
ATOM   741  H HG2  B GLU   A 1 26  ? 13.927 -1.195  12.522  0.58 22.18 ?  26  GLU   A HG2  1 
ATOM   742  H HG3  A GLU   A 1 26  ? 14.481 -2.326  12.360  0.42 22.72 ?  26  GLU   A HG3  1 
ATOM   743  H HG3  B GLU   A 1 26  ? 14.430 -2.653  12.135  0.58 22.18 ?  26  GLU   A HG3  1 
ATOM   744  N N    A ALA   A 1 27  ? 18.441 0.268   14.179  0.42 14.95 ?  27  ALA   A N    1 
ATOM   745  N N    B ALA   A 1 27  ? 18.341 0.261   13.949  0.58 12.80 ?  27  ALA   A N    1 
ATOM   746  C CA   A ALA   A 1 27  ? 19.829 0.192   14.623  0.42 15.50 ?  27  ALA   A CA   1 
ATOM   747  C CA   B ALA   A 1 27  ? 19.720 0.346   14.420  0.58 13.03 ?  27  ALA   A CA   1 
ATOM   748  C C    A ALA   A 1 27  ? 20.046 1.004   15.894  0.42 16.97 ?  27  ALA   A C    1 
ATOM   749  C C    B ALA   A 1 27  ? 19.811 1.182   15.692  0.58 13.63 ?  27  ALA   A C    1 
ATOM   750  O O    A ALA   A 1 27  ? 20.734 0.552   16.817  0.42 17.14 ?  27  ALA   A O    1 
ATOM   751  O O    B ALA   A 1 27  ? 20.450 0.776   16.669  0.58 14.20 ?  27  ALA   A O    1 
ATOM   752  C CB   A ALA   A 1 27  ? 20.775 0.647   13.508  0.42 14.87 ?  27  ALA   A CB   1 
ATOM   753  C CB   B ALA   A 1 27  ? 20.623 0.918   13.324  0.58 12.85 ?  27  ALA   A CB   1 
ATOM   754  H H    A ALA   A 1 27  ? 18.330 0.620   13.399  0.42 17.94 ?  27  ALA   A H    1 
ATOM   755  H H    B ALA   A 1 27  ? 18.187 0.646   13.193  0.58 15.36 ?  27  ALA   A H    1 
ATOM   756  H HA   A ALA   A 1 27  ? 20.037 -0.730  14.824  0.42 18.60 ?  27  ALA   A HA   1 
ATOM   757  H HA   B ALA   A 1 27  ? 20.032 -0.544  14.624  0.58 15.63 ?  27  ALA   A HA   1 
ATOM   758  H HB1  A ALA   A 1 27  ? 21.691 0.586   13.825  0.42 17.85 ?  27  ALA   A HB1  1 
ATOM   759  H HB1  B ALA   A 1 27  ? 21.531 0.963   13.658  0.58 15.42 ?  27  ALA   A HB1  1 
ATOM   760  H HB2  A ALA   A 1 27  ? 20.656 0.068   12.736  0.42 17.85 ?  27  ALA   A HB2  1 
ATOM   761  H HB2  B ALA   A 1 27  ? 20.582 0.342   12.545  0.58 15.42 ?  27  ALA   A HB2  1 
ATOM   762  H HB3  A ALA   A 1 27  ? 20.569 1.563   13.266  0.42 17.85 ?  27  ALA   A HB3  1 
ATOM   763  H HB3  B ALA   A 1 27  ? 20.313 1.810   13.090  0.58 15.42 ?  27  ALA   A HB3  1 
ATOM   764  N N    A LYS   A 1 28  ? 19.460 2.203   15.968  0.42 19.10 ?  28  LYS   A N    1 
ATOM   765  N N    B LYS   A 1 28  ? 19.164 2.350   15.704  0.58 15.27 ?  28  LYS   A N    1 
ATOM   766  C CA   A LYS   A 1 28  ? 19.626 3.021   17.165  0.42 21.74 ?  28  LYS   A CA   1 
ATOM   767  C CA   B LYS   A 1 28  ? 19.224 3.209   16.884  0.58 17.58 ?  28  LYS   A CA   1 
ATOM   768  C C    A LYS   A 1 28  ? 19.071 2.324   18.400  0.42 22.81 ?  28  LYS   A C    1 
ATOM   769  C C    B LYS   A 1 28  ? 18.658 2.515   18.117  0.58 18.96 ?  28  LYS   A C    1 
ATOM   770  O O    A LYS   A 1 28  ? 19.634 2.457   19.492  0.42 23.69 ?  28  LYS   A O    1 
ATOM   771  O O    B LYS   A 1 28  ? 19.167 2.703   19.228  0.58 20.63 ?  28  LYS   A O    1 
ATOM   772  C CB   A LYS   A 1 28  ? 18.988 4.399   16.966  0.42 23.81 ?  28  LYS   A CB   1 
ATOM   773  C CB   B LYS   A 1 28  ? 18.505 4.532   16.618  0.58 19.87 ?  28  LYS   A CB   1 
ATOM   774  C CG   A LYS   A 1 28  ? 19.818 5.330   16.093  0.42 25.87 ?  28  LYS   A CG   1 
ATOM   775  C CG   B LYS   A 1 28  ? 19.326 5.491   15.783  0.58 22.72 ?  28  LYS   A CG   1 
ATOM   776  C CD   A LYS   A 1 28  ? 19.331 6.768   16.159  0.42 27.73 ?  28  LYS   A CD   1 
ATOM   777  C CD   B LYS   A 1 28  ? 18.795 6.909   15.843  0.58 26.22 ?  28  LYS   A CD   1 
ATOM   778  C CE   A LYS   A 1 28  ? 18.019 6.949   15.421  0.42 29.00 ?  28  LYS   A CE   1 
ATOM   779  C CE   B LYS   A 1 28  ? 17.647 7.114   14.879  0.58 28.64 ?  28  LYS   A CE   1 
ATOM   780  N NZ   A LYS   A 1 28  ? 17.628 8.385   15.356  0.42 29.59 ?  28  LYS   A NZ   1 
ATOM   781  N NZ   B LYS   A 1 28  ? 17.312 8.558   14.734  0.58 29.74 ?  28  LYS   A NZ   1 
ATOM   782  H H    A LYS   A 1 28  ? 18.972 2.554   15.355  0.42 22.92 ?  28  LYS   A H    1 
ATOM   783  H H    B LYS   A 1 28  ? 18.694 2.666   15.052  0.58 18.32 ?  28  LYS   A H    1 
ATOM   784  H HA   A LYS   A 1 28  ? 20.571 3.161   17.319  0.42 26.08 ?  28  LYS   A HA   1 
ATOM   785  H HA   B LYS   A 1 28  ? 20.148 3.415   17.072  0.58 21.09 ?  28  LYS   A HA   1 
ATOM   786  H HB2  A LYS   A 1 28  ? 18.124 4.293   16.540  0.42 28.57 ?  28  LYS   A HB2  1 
ATOM   787  H HB2  B LYS   A 1 28  ? 17.679 4.361   16.141  0.58 23.84 ?  28  LYS   A HB2  1 
ATOM   788  H HB3  A LYS   A 1 28  ? 18.880 4.829   17.829  0.42 28.57 ?  28  LYS   A HB3  1 
ATOM   789  H HB3  B LYS   A 1 28  ? 18.314 4.967   17.464  0.58 23.84 ?  28  LYS   A HB3  1 
ATOM   790  H HG2  A LYS   A 1 28  ? 20.740 5.312   16.393  0.42 31.05 ?  28  LYS   A HG2  1 
ATOM   791  H HG2  B LYS   A 1 28  ? 20.237 5.497   16.113  0.58 27.26 ?  28  LYS   A HG2  1 
ATOM   792  H HG3  A LYS   A 1 28  ? 19.761 5.036   15.170  0.42 31.05 ?  28  LYS   A HG3  1 
ATOM   793  H HG3  B LYS   A 1 28  ? 19.307 5.200   14.859  0.58 27.26 ?  28  LYS   A HG3  1 
ATOM   794  H HD2  A LYS   A 1 28  ? 19.193 7.018   17.087  0.42 33.27 ?  28  LYS   A HD2  1 
ATOM   795  H HD2  B LYS   A 1 28  ? 18.477 7.096   16.742  0.58 31.46 ?  28  LYS   A HD2  1 
ATOM   796  H HD3  A LYS   A 1 28  ? 19.990 7.350   15.750  0.42 33.27 ?  28  LYS   A HD3  1 
ATOM   797  H HD3  B LYS   A 1 28  ? 19.506 7.525   15.606  0.58 31.46 ?  28  LYS   A HD3  1 
ATOM   798  H HE2  A LYS   A 1 28  ? 18.113 6.618   14.514  0.42 34.81 ?  28  LYS   A HE2  1 
ATOM   799  H HE2  B LYS   A 1 28  ? 17.896 6.769   14.007  0.58 34.37 ?  28  LYS   A HE2  1 
ATOM   800  H HE3  A LYS   A 1 28  ? 17.320 6.464   15.886  0.42 34.81 ?  28  LYS   A HE3  1 
ATOM   801  H HE3  B LYS   A 1 28  ? 16.863 6.651   15.213  0.58 34.37 ?  28  LYS   A HE3  1 
ATOM   802  H HZ1  A LYS   A 1 28  ? 16.857 8.471   14.920  0.42 35.51 ?  28  LYS   A HZ1  1 
ATOM   803  H HZ1  B LYS   A 1 28  ? 16.637 8.657   14.164  0.58 35.69 ?  28  LYS   A HZ1  1 
ATOM   804  H HZ2  A LYS   A 1 28  ? 17.533 8.712   16.178  0.42 35.51 ?  28  LYS   A HZ2  1 
ATOM   805  H HZ2  B LYS   A 1 28  ? 17.078 8.897   15.523  0.58 35.69 ?  28  LYS   A HZ2  1 
ATOM   806  H HZ3  A LYS   A 1 28  ? 18.255 8.852   14.930  0.42 35.51 ?  28  LYS   A HZ3  1 
ATOM   807  H HZ3  B LYS   A 1 28  ? 18.019 9.004   14.426  0.58 35.69 ?  28  LYS   A HZ3  1 
ATOM   808  N N    A LYS   A 1 29  ? 17.988 1.561   18.244  0.42 23.21 ?  29  LYS   A N    1 
ATOM   809  N N    B LYS   A 1 29  ? 17.604 1.717   17.947  0.58 18.70 ?  29  LYS   A N    1 
ATOM   810  C CA   A LYS   A 1 29  ? 17.388 0.869   19.381  0.42 24.21 ?  29  LYS   A CA   1 
ATOM   811  C CA   B LYS   A 1 29  ? 16.980 1.053   19.088  0.58 19.91 ?  29  LYS   A CA   1 
ATOM   812  C C    A LYS   A 1 29  ? 18.199 -0.365  19.769  0.42 22.91 ?  29  LYS   A C    1 
ATOM   813  C C    B LYS   A 1 29  ? 17.789 -0.154  19.545  0.58 18.86 ?  29  LYS   A C    1 
ATOM   814  O O    A LYS   A 1 29  ? 18.533 -0.556  20.944  0.42 23.49 ?  29  LYS   A O    1 
ATOM   815  O O    B LYS   A 1 29  ? 17.991 -0.357  20.747  0.58 20.21 ?  29  LYS   A O    1 
ATOM   816  C CB   A LYS   A 1 29  ? 15.949 0.474   19.037  0.42 26.60 ?  29  LYS   A CB   1 
ATOM   817  C CB   B LYS   A 1 29  ? 15.562 0.613   18.722  0.58 22.31 ?  29  LYS   A CB   1 
ATOM   818  C CG   A LYS   A 1 29  ? 15.216 -0.261  20.149  0.42 28.97 ?  29  LYS   A CG   1 
ATOM   819  C CG   B LYS   A 1 29  ? 14.840 -0.146  19.830  0.58 26.05 ?  29  LYS   A CG   1 
ATOM   820  C CD   A LYS   A 1 29  ? 14.877 0.670   21.300  0.42 31.04 ?  29  LYS   A CD   1 
ATOM   821  C CD   B LYS   A 1 29  ? 14.524 0.759   21.008  0.58 29.27 ?  29  LYS   A CD   1 
ATOM   822  C CE   A LYS   A 1 29  ? 13.996 -0.023  22.329  0.42 32.58 ?  29  LYS   A CE   1 
ATOM   823  C CE   B LYS   A 1 29  ? 13.735 0.023   22.078  0.58 31.63 ?  29  LYS   A CE   1 
ATOM   824  N NZ   A LYS   A 1 29  ? 13.523 0.920   23.379  0.42 33.37 ?  29  LYS   A NZ   1 
ATOM   825  N NZ   B LYS   A 1 29  ? 13.352 0.926   23.196  0.58 32.88 ?  29  LYS   A NZ   1 
ATOM   826  H H    A LYS   A 1 29  ? 17.593 1.423   17.493  0.42 27.85 ?  29  LYS   A H    1 
ATOM   827  H H    B LYS   A 1 29  ? 17.227 1.552   17.190  0.58 22.44 ?  29  LYS   A H    1 
ATOM   828  H HA   A LYS   A 1 29  ? 17.359 1.470   20.142  0.42 29.06 ?  29  LYS   A HA   1 
ATOM   829  H HA   B LYS   A 1 29  ? 16.922 1.676   19.830  0.58 23.90 ?  29  LYS   A HA   1 
ATOM   830  H HB2  A LYS   A 1 29  ? 15.443 1.279   18.836  0.42 31.93 ?  29  LYS   A HB2  1 
ATOM   831  H HB2  B LYS   A 1 29  ? 15.033 1.399   18.517  0.58 26.77 ?  29  LYS   A HB2  1 
ATOM   832  H HB3  A LYS   A 1 29  ? 15.961 -0.105  18.259  0.42 31.93 ?  29  LYS   A HB3  1 
ATOM   833  H HB3  B LYS   A 1 29  ? 15.603 0.032   17.948  0.58 26.77 ?  29  LYS   A HB3  1 
ATOM   834  H HG2  A LYS   A 1 29  ? 14.387 -0.620  19.798  0.42 34.76 ?  29  LYS   A HG2  1 
ATOM   835  H HG2  B LYS   A 1 29  ? 14.003 -0.491  19.484  0.58 31.26 ?  29  LYS   A HG2  1 
ATOM   836  H HG3  A LYS   A 1 29  ? 15.770 -0.981  20.491  0.42 34.76 ?  29  LYS   A HG3  1 
ATOM   837  H HG3  B LYS   A 1 29  ? 15.393 -0.880  20.147  0.58 31.26 ?  29  LYS   A HG3  1 
ATOM   838  H HD2  A LYS   A 1 29  ? 15.695 0.950   21.739  0.42 37.25 ?  29  LYS   A HD2  1 
ATOM   839  H HD2  B LYS   A 1 29  ? 15.353 1.073   21.404  0.58 35.12 ?  29  LYS   A HD2  1 
ATOM   840  H HD3  A LYS   A 1 29  ? 14.398 1.441   20.958  0.42 37.25 ?  29  LYS   A HD3  1 
ATOM   841  H HD3  B LYS   A 1 29  ? 13.994 1.511   20.700  0.58 35.12 ?  29  LYS   A HD3  1 
ATOM   842  H HE2  A LYS   A 1 29  ? 13.219 -0.396  21.884  0.42 39.09 ?  29  LYS   A HE2  1 
ATOM   843  H HE2  B LYS   A 1 29  ? 12.924 -0.337  21.686  0.58 37.95 ?  29  LYS   A HE2  1 
ATOM   844  H HE3  A LYS   A 1 29  ? 14.504 -0.727  22.761  0.42 39.09 ?  29  LYS   A HE3  1 
ATOM   845  H HE3  B LYS   A 1 29  ? 14.279 -0.695  22.440  0.58 37.95 ?  29  LYS   A HE3  1 
ATOM   846  H HZ1  A LYS   A 1 29  ? 13.011 0.489   23.966  0.42 40.05 ?  29  LYS   A HZ1  1 
ATOM   847  H HZ1  B LYS   A 1 29  ? 12.892 0.473   23.809  0.58 39.46 ?  29  LYS   A HZ1  1 
ATOM   848  H HZ2  A LYS   A 1 29  ? 14.219 1.273   23.806  0.42 40.05 ?  29  LYS   A HZ2  1 
ATOM   849  H HZ2  B LYS   A 1 29  ? 14.082 1.266   23.575  0.58 39.46 ?  29  LYS   A HZ2  1 
ATOM   850  H HZ3  A LYS   A 1 29  ? 13.049 1.575   23.008  0.42 40.05 ?  29  LYS   A HZ3  1 
ATOM   851  H HZ3  B LYS   A 1 29  ? 12.848 1.592   22.889  0.58 39.46 ?  29  LYS   A HZ3  1 
ATOM   852  N N    A VAL   A 1 30  ? 18.521 -1.211  18.792  0.42 21.35 ?  30  VAL   A N    1 
ATOM   853  N N    B VAL   A 1 30  ? 18.236 -0.978  18.600  0.58 17.87 ?  30  VAL   A N    1 
ATOM   854  C CA   A VAL   A 1 30  ? 19.170 -2.485  19.083  0.42 20.17 ?  30  VAL   A CA   1 
ATOM   855  C CA   B VAL   A 1 30  ? 18.883 -2.239  18.944  0.58 17.17 ?  30  VAL   A CA   1 
ATOM   856  C C    A VAL   A 1 30  ? 20.677 -2.329  19.287  0.42 18.79 ?  30  VAL   A C    1 
ATOM   857  C C    B VAL   A 1 30  ? 20.386 -2.081  19.177  0.58 16.66 ?  30  VAL   A C    1 
ATOM   858  O O    A VAL   A 1 30  ? 21.276 -3.062  20.083  0.42 19.29 ?  30  VAL   A O    1 
ATOM   859  O O    B VAL   A 1 30  ? 20.958 -2.791  20.010  0.58 17.50 ?  30  VAL   A O    1 
ATOM   860  C CB   A VAL   A 1 30  ? 18.855 -3.491  17.961  0.42 20.81 ?  30  VAL   A CB   1 
ATOM   861  C CB   B VAL   A 1 30  ? 18.593 -3.282  17.848  0.58 17.70 ?  30  VAL   A CB   1 
ATOM   862  C CG1  A VAL   A 1 30  ? 19.621 -4.791  18.169  0.42 21.28 ?  30  VAL   A CG1  1 
ATOM   863  C CG1  B VAL   A 1 30  ? 19.335 -4.582  18.126  0.58 18.65 ?  30  VAL   A CG1  1 
ATOM   864  C CG2  A VAL   A 1 30  ? 17.357 -3.751  17.884  0.42 21.49 ?  30  VAL   A CG2  1 
ATOM   865  C CG2  B VAL   A 1 30  ? 17.092 -3.531  17.729  0.58 18.39 ?  30  VAL   A CG2  1 
ATOM   866  H H    A VAL   A 1 30  ? 18.365 -1.072  17.959  0.42 25.62 ?  30  VAL   A H    1 
ATOM   867  H H    B VAL   A 1 30  ? 18.169 -0.834  17.750  0.58 21.44 ?  30  VAL   A H    1 
ATOM   868  H HA   A VAL   A 1 30  ? 18.793 -2.839  19.903  0.42 24.20 ?  30  VAL   A HA   1 
ATOM   869  H HA   B VAL   A 1 30  ? 18.483 -2.568  19.765  0.58 20.60 ?  30  VAL   A HA   1 
ATOM   870  H HB   A VAL   A 1 30  ? 19.136 -3.113  17.113  0.42 24.97 ?  30  VAL   A HB   1 
ATOM   871  H HB   B VAL   A 1 30  ? 18.906 -2.941  16.997  0.58 21.24 ?  30  VAL   A HB   1 
ATOM   872  H HG11 A VAL   A 1 30  ? 19.241 -5.475  17.594  0.42 25.53 ?  30  VAL   A HG11 1 
ATOM   873  H HG11 B VAL   A 1 30  ? 18.936 -5.294  17.600  0.58 22.39 ?  30  VAL   A HG11 1 
ATOM   874  H HG12 A VAL   A 1 30  ? 20.554 -4.653  17.943  0.42 25.53 ?  30  VAL   A HG12 1 
ATOM   875  H HG12 B VAL   A 1 30  ? 20.267 -4.475  17.881  0.58 22.39 ?  30  VAL   A HG12 1 
ATOM   876  H HG13 A VAL   A 1 30  ? 19.539 -5.061  19.097  0.42 25.53 ?  30  VAL   A HG13 1 
ATOM   877  H HG13 B VAL   A 1 30  ? 19.261 -4.791  19.069  0.58 22.39 ?  30  VAL   A HG13 1 
ATOM   878  H HG21 A VAL   A 1 30  ? 17.189 -4.421  17.204  0.42 25.79 ?  30  VAL   A HG21 1 
ATOM   879  H HG21 B VAL   A 1 30  ? 16.939 -4.225  17.068  0.58 22.07 ?  30  VAL   A HG21 1 
ATOM   880  H HG22 A VAL   A 1 30  ? 17.049 -4.069  18.747  0.42 25.79 ?  30  VAL   A HG22 1 
ATOM   881  H HG22 B VAL   A 1 30  ? 16.751 -3.815  18.592  0.58 22.07 ?  30  VAL   A HG22 1 
ATOM   882  H HG23 A VAL   A 1 30  ? 16.905 -2.925  17.654  0.42 25.79 ?  30  VAL   A HG23 1 
ATOM   883  H HG23 B VAL   A 1 30  ? 16.658 -2.710  17.453  0.58 22.07 ?  30  VAL   A HG23 1 
ATOM   884  N N    A LYS   A 1 31  ? 21.310 -1.391  18.590  0.42 17.38 ?  31  LYS   A N    1 
ATOM   885  N N    B LYS   A 1 31  ? 21.032 -1.158  18.470  0.58 15.98 ?  31  LYS   A N    1 
ATOM   886  C CA   A LYS   A 1 31  ? 22.764 -1.292  18.533  0.42 17.43 ?  31  LYS   A CA   1 
ATOM   887  C CA   B LYS   A 1 31  ? 22.485 -1.046  18.446  0.58 16.70 ?  31  LYS   A CA   1 
ATOM   888  C C    A LYS   A 1 31  ? 23.382 -2.651  18.187  0.42 15.55 ?  31  LYS   A C    1 
ATOM   889  C C    B LYS   A 1 31  ? 23.119 -2.415  18.190  0.58 15.39 ?  31  LYS   A C    1 
ATOM   890  O O    A LYS   A 1 31  ? 24.168 -3.200  18.964  0.42 15.93 ?  31  LYS   A O    1 
ATOM   891  O O    B LYS   A 1 31  ? 23.880 -2.923  19.023  0.58 16.43 ?  31  LYS   A O    1 
ATOM   892  C CB   A LYS   A 1 31  ? 23.350 -0.741  19.826  0.42 20.95 ?  31  LYS   A CB   1 
ATOM   893  C CB   B LYS   A 1 31  ? 23.029 -0.414  19.720  0.58 20.07 ?  31  LYS   A CB   1 
ATOM   894  C CG   A LYS   A 1 31  ? 22.666 0.518   20.333  0.42 24.81 ?  31  LYS   A CG   1 
ATOM   895  C CG   B LYS   A 1 31  ? 22.319 0.870   20.120  0.58 24.79 ?  31  LYS   A CG   1 
ATOM   896  C CD   A LYS   A 1 31  ? 23.676 1.559   20.793  0.42 27.94 ?  31  LYS   A CD   1 
ATOM   897  C CD   B LYS   A 1 31  ? 23.280 1.861   20.754  0.58 28.64 ?  31  LYS   A CD   1 
ATOM   898  C CE   A LYS   A 1 31  ? 23.029 2.601   21.695  0.42 30.03 ?  31  LYS   A CE   1 
ATOM   899  C CE   B LYS   A 1 31  ? 22.543 2.893   21.588  0.58 31.19 ?  31  LYS   A CE   1 
ATOM   900  N NZ   A LYS   A 1 31  ? 21.846 3.253   21.068  0.42 30.94 ?  31  LYS   A NZ   1 
ATOM   901  N NZ   B LYS   A 1 31  ? 21.333 3.421   20.900  0.58 32.79 ?  31  LYS   A NZ   1 
ATOM   902  H H    A LYS   A 1 31  ? 20.909 -0.786  18.132  0.42 20.86 ?  31  LYS   A H    1 
ATOM   903  H H    B LYS   A 1 31  ? 20.628 -0.562  17.990  0.58 19.18 ?  31  LYS   A H    1 
ATOM   904  H HA   A LYS   A 1 31  ? 22.998 -0.676  17.827  0.42 20.91 ?  31  LYS   A HA   1 
ATOM   905  H HA   B LYS   A 1 31  ? 22.722 -0.464  17.713  0.58 20.05 ?  31  LYS   A HA   1 
ATOM   906  H HB2  A LYS   A 1 31  ? 23.278 -1.420  20.514  0.42 25.14 ?  31  LYS   A HB2  1 
ATOM   907  H HB2  B LYS   A 1 31  ? 22.933 -1.040  20.450  0.58 24.08 ?  31  LYS   A HB2  1 
ATOM   908  H HB3  A LYS   A 1 31  ? 24.287 -0.529  19.676  0.42 25.14 ?  31  LYS   A HB3  1 
ATOM   909  H HB3  B LYS   A 1 31  ? 23.965 -0.200  19.584  0.58 24.08 ?  31  LYS   A HB3  1 
ATOM   910  H HG2  A LYS   A 1 31  ? 22.136 0.904   19.619  0.42 29.78 ?  31  LYS   A HG2  1 
ATOM   911  H HG2  B LYS   A 1 31  ? 21.931 1.284   19.333  0.58 29.75 ?  31  LYS   A HG2  1 
ATOM   912  H HG3  A LYS   A 1 31  ? 22.100 0.292   21.088  0.42 29.78 ?  31  LYS   A HG3  1 
ATOM   913  H HG3  B LYS   A 1 31  ? 21.625 0.665   20.768  0.58 29.75 ?  31  LYS   A HG3  1 
ATOM   914  H HD2  A LYS   A 1 31  ? 24.384 1.123   21.291  0.42 33.53 ?  31  LYS   A HD2  1 
ATOM   915  H HD2  B LYS   A 1 31  ? 23.897 1.384   21.333  0.58 34.37 ?  31  LYS   A HD2  1 
ATOM   916  H HD3  A LYS   A 1 31  ? 24.042 2.014   20.017  0.42 33.53 ?  31  LYS   A HD3  1 
ATOM   917  H HD3  B LYS   A 1 31  ? 23.769 2.326   20.056  0.58 34.37 ?  31  LYS   A HD3  1 
ATOM   918  H HE2  A LYS   A 1 31  ? 22.734 2.172   22.513  0.42 36.04 ?  31  LYS   A HE2  1 
ATOM   919  H HE2  B LYS   A 1 31  ? 22.267 2.483   22.420  0.58 37.43 ?  31  LYS   A HE2  1 
ATOM   920  H HE3  A LYS   A 1 31  ? 23.678 3.292   21.898  0.42 36.04 ?  31  LYS   A HE3  1 
ATOM   921  H HE3  B LYS   A 1 31  ? 23.137 3.638   21.767  0.58 37.43 ?  31  LYS   A HE3  1 
ATOM   922  H HZ1  A LYS   A 1 31  ? 21.510 3.868   21.618  0.42 37.13 ?  31  LYS   A HZ1  1 
ATOM   923  H HZ1  B LYS   A 1 31  ? 20.980 4.085   21.376  0.58 39.35 ?  31  LYS   A HZ1  1 
ATOM   924  H HZ2  A LYS   A 1 31  ? 22.083 3.647   20.306  0.42 37.13 ?  31  LYS   A HZ2  1 
ATOM   925  H HZ2  B LYS   A 1 31  ? 21.552 3.727   20.094  0.58 39.35 ?  31  LYS   A HZ2  1 
ATOM   926  H HZ3  A LYS   A 1 31  ? 21.218 2.646   20.897  0.42 37.13 ?  31  LYS   A HZ3  1 
ATOM   927  H HZ3  B LYS   A 1 31  ? 20.727 2.776   20.811  0.58 39.35 ?  31  LYS   A HZ3  1 
ATOM   928  N N    A PRO   A 1 32  ? 23.048 -3.210  17.027  0.42 14.27 ?  32  PRO   A N    1 
ATOM   929  N N    B PRO   A 1 32  ? 22.832 -3.027  17.046  0.58 13.99 ?  32  PRO   A N    1 
ATOM   930  C CA   A PRO   A 1 32  ? 23.525 -4.553  16.689  0.42 14.61 ?  32  PRO   A CA   1 
ATOM   931  C CA   B PRO   A 1 32  ? 23.327 -4.377  16.774  0.58 14.33 ?  32  PRO   A CA   1 
ATOM   932  C C    A PRO   A 1 32  ? 25.025 -4.573  16.458  0.42 14.31 ?  32  PRO   A C    1 
ATOM   933  C C    B PRO   A 1 32  ? 24.833 -4.380  16.567  0.58 14.15 ?  32  PRO   A C    1 
ATOM   934  O O    A PRO   A 1 32  ? 25.660 -3.552  16.183  0.42 13.88 ?  32  PRO   A O    1 
ATOM   935  O O    B PRO   A 1 32  ? 25.482 -3.343  16.414  0.58 14.60 ?  32  PRO   A O    1 
ATOM   936  C CB   A PRO   A 1 32  ? 22.782 -4.862  15.386  0.42 15.23 ?  32  PRO   A CB   1 
ATOM   937  C CB   B PRO   A 1 32  ? 22.605 -4.735  15.474  0.58 14.68 ?  32  PRO   A CB   1 
ATOM   938  C CG   A PRO   A 1 32  ? 22.601 -3.521  14.753  0.42 14.77 ?  32  PRO   A CG   1 
ATOM   939  C CG   B PRO   A 1 32  ? 22.461 -3.419  14.776  0.58 14.47 ?  32  PRO   A CG   1 
ATOM   940  C CD   A PRO   A 1 32  ? 22.320 -2.591  15.907  0.42 13.73 ?  32  PRO   A CD   1 
ATOM   941  C CD   B PRO   A 1 32  ? 22.126 -2.459  15.884  0.58 13.65 ?  32  PRO   A CD   1 
ATOM   942  H HA   A PRO   A 1 32  ? 23.278 -5.194  17.377  0.42 17.53 ?  32  PRO   A HA   1 
ATOM   943  H HA   B PRO   A 1 32  ? 23.072 -4.992  17.482  0.58 17.19 ?  32  PRO   A HA   1 
ATOM   944  H HB2  A PRO   A 1 32  ? 23.326 -5.442  14.829  0.42 18.27 ?  32  PRO   A HB2  1 
ATOM   945  H HB2  B PRO   A 1 32  ? 23.146 -5.349  14.956  0.58 17.62 ?  32  PRO   A HB2  1 
ATOM   946  H HB3  A PRO   A 1 32  ? 21.926 -5.276  15.584  0.42 18.27 ?  32  PRO   A HB3  1 
ATOM   947  H HB3  B PRO   A 1 32  ? 21.734 -5.121  15.671  0.58 17.62 ?  32  PRO   A HB3  1 
ATOM   948  H HG2  A PRO   A 1 32  ? 23.414 -3.267  14.293  0.42 17.73 ?  32  PRO   A HG2  1 
ATOM   949  H HG2  B PRO   A 1 32  ? 23.298 -3.183  14.351  0.58 17.36 ?  32  PRO   A HG2  1 
ATOM   950  H HG3  A PRO   A 1 32  ? 21.850 -3.552  14.140  0.42 17.73 ?  32  PRO   A HG3  1 
ATOM   951  H HG3  B PRO   A 1 32  ? 21.742 -3.471  14.127  0.58 17.36 ?  32  PRO   A HG3  1 
ATOM   952  H HD2  A PRO   A 1 32  ? 22.673 -1.709  15.713  0.42 16.48 ?  32  PRO   A HD2  1 
ATOM   953  H HD2  B PRO   A 1 32  ? 22.467 -1.576  15.670  0.58 16.38 ?  32  PRO   A HD2  1 
ATOM   954  H HD3  A PRO   A 1 32  ? 21.369 -2.565  16.089  0.42 16.48 ?  32  PRO   A HD3  1 
ATOM   955  H HD3  B PRO   A 1 32  ? 21.165 -2.442  16.031  0.58 16.38 ?  32  PRO   A HD3  1 
ATOM   956  N N    A THR   A 1 33  ? 25.589 -5.778  16.551  0.42 14.79 ?  33  THR   A N    1 
ATOM   957  N N    B THR   A 1 33  ? 25.386 -5.589  16.535  0.58 14.20 ?  33  THR   A N    1 
ATOM   958  C CA   A THR   A 1 33  ? 26.994 -5.954  16.209  0.42 15.19 ?  33  THR   A CA   1 
ATOM   959  C CA   B THR   A 1 33  ? 26.808 -5.741  16.254  0.58 14.35 ?  33  THR   A CA   1 
ATOM   960  C C    A THR   A 1 33  ? 27.274 -5.515  14.776  0.42 14.19 ?  33  THR   A C    1 
ATOM   961  C C    B THR   A 1 33  ? 27.137 -5.300  14.832  0.58 13.12 ?  33  THR   A C    1 
ATOM   962  O O    A THR   A 1 33  ? 28.359 -4.992  14.493  0.42 14.06 ?  33  THR   A O    1 
ATOM   963  O O    B THR   A 1 33  ? 28.131 -4.600  14.602  0.58 12.58 ?  33  THR   A O    1 
ATOM   964  C CB   A THR   A 1 33  ? 27.399 -7.418  16.408  0.42 16.74 ?  33  THR   A CB   1 
ATOM   965  C CB   B THR   A 1 33  ? 27.221 -7.194  16.480  0.58 15.86 ?  33  THR   A CB   1 
ATOM   966  O OG1  A THR   A 1 33  ? 27.146 -7.816  17.760  0.42 18.30 ?  33  THR   A OG1  1 
ATOM   967  O OG1  B THR   A 1 33  ? 26.871 -7.583  17.813  0.58 17.98 ?  33  THR   A OG1  1 
ATOM   968  C CG2  A THR   A 1 33  ? 28.873 -7.617  16.112  0.42 17.10 ?  33  THR   A CG2  1 
ATOM   969  C CG2  B THR   A 1 33  ? 28.718 -7.366  16.274  0.58 16.78 ?  33  THR   A CG2  1 
ATOM   970  H H    A THR   A 1 33  ? 25.185 -6.495  16.801  0.42 17.74 ?  33  THR   A H    1 
ATOM   971  H H    B THR   A 1 33  ? 24.961 -6.323  16.672  0.58 17.04 ?  33  THR   A H    1 
ATOM   972  H HA   A THR   A 1 33  ? 27.533 -5.406  16.802  0.42 18.23 ?  33  THR   A HA   1 
ATOM   973  H HA   B THR   A 1 33  ? 27.311 -5.186  16.873  0.58 17.22 ?  33  THR   A HA   1 
ATOM   974  H HB   A THR   A 1 33  ? 26.884 -7.979  15.808  0.42 20.09 ?  33  THR   A HB   1 
ATOM   975  H HB   B THR   A 1 33  ? 26.753 -7.764  15.844  0.58 19.03 ?  33  THR   A HB   1 
ATOM   976  H HG1  A THR   A 1 33  ? 27.574 -7.324  18.290  0.42 21.96 ?  33  THR   A HG1  1 
ATOM   977  H HG1  B THR   A 1 33  ? 27.281 -7.101  18.368  0.58 21.57 ?  33  THR   A HG1  1 
ATOM   978  H HG21 A THR   A 1 33  ? 29.149 -8.501  16.403  0.42 20.52 ?  33  THR   A HG21 1 
ATOM   979  H HG21 B THR   A 1 33  ? 28.993 -8.248  16.568  0.58 20.13 ?  33  THR   A HG21 1 
ATOM   980  H HG22 A THR   A 1 33  ? 29.037 -7.533  15.162  0.42 20.52 ?  33  THR   A HG22 1 
ATOM   981  H HG22 B THR   A 1 33  ? 28.941 -7.265  15.334  0.58 20.13 ?  33  THR   A HG22 1 
ATOM   982  H HG23 A THR   A 1 33  ? 29.398 -6.954  16.587  0.42 20.52 ?  33  THR   A HG23 1 
ATOM   983  H HG23 B THR   A 1 33  ? 29.201 -6.699  16.786  0.58 20.13 ?  33  THR   A HG23 1 
ATOM   984  N N    . VAL   A 1 34  ? 26.318 -5.713  13.865  1.00 12.48 ?  34  VAL   A N    1 
ATOM   985  C CA   . VAL   A 1 34  ? 26.510 -5.389  12.455  1.00 11.90 ?  34  VAL   A CA   1 
ATOM   986  C C    . VAL   A 1 34  ? 25.214 -4.838  11.882  1.00 11.11 ?  34  VAL   A C    1 
ATOM   987  O O    . VAL   A 1 34  ? 24.179 -5.511  11.922  1.00 11.96 ?  34  VAL   A O    1 
ATOM   988  C CB   . VAL   A 1 34  ? 26.972 -6.603  11.625  1.00 12.25 ?  34  VAL   A CB   1 
ATOM   989  C CG1  . VAL   A 1 34  ? 27.165 -6.208  10.179  1.00 12.36 ?  34  VAL   A CG1  1 
ATOM   990  C CG2  . VAL   A 1 34  ? 28.255 -7.230  12.188  1.00 13.70 ?  34  VAL   A CG2  1 
ATOM   991  H H    A VAL   A 1 34  ? 25.544 -6.044  14.047  0.42 14.97 ?  34  VAL   A H    1 
ATOM   992  H H    B VAL   A 1 34  ? 25.626 -6.205  14.012  0.58 14.97 ?  34  VAL   A H    1 
ATOM   993  H HA   . VAL   A 1 34  ? 27.188 -4.701  12.378  1.00 14.28 ?  34  VAL   A HA   1 
ATOM   994  H HB   . VAL   A 1 34  ? 26.277 -7.280  11.659  1.00 14.69 ?  34  VAL   A HB   1 
ATOM   995  H HG11 . VAL   A 1 34  ? 27.668 -6.904  9.726   1.00 14.84 ?  34  VAL   A HG11 1 
ATOM   996  H HG12 . VAL   A 1 34  ? 26.301 -6.097  9.757   1.00 14.84 ?  34  VAL   A HG12 1 
ATOM   997  H HG13 . VAL   A 1 34  ? 27.662 -5.372  10.143  1.00 14.84 ?  34  VAL   A HG13 1 
ATOM   998  H HG21 . VAL   A 1 34  ? 28.537 -7.951  11.599  1.00 16.44 ?  34  VAL   A HG21 1 
ATOM   999  H HG22 . VAL   A 1 34  ? 28.945 -6.554  12.238  1.00 16.44 ?  34  VAL   A HG22 1 
ATOM   1000 H HG23 . VAL   A 1 34  ? 28.074 -7.586  13.074  1.00 16.44 ?  34  VAL   A HG23 1 
ATOM   1001 N N    . VAL   A 1 35  ? 25.281 -3.643  11.300  1.00 10.64 ?  35  VAL   A N    1 
ATOM   1002 C CA   . VAL   A 1 35  ? 24.241 -3.138  10.412  1.00 10.28 ?  35  VAL   A CA   1 
ATOM   1003 C C    . VAL   A 1 35  ? 24.795 -3.148  8.995   1.00 9.94  ?  35  VAL   A C    1 
ATOM   1004 O O    . VAL   A 1 35  ? 25.940 -2.744  8.769   1.00 10.62 ?  35  VAL   A O    1 
ATOM   1005 C CB   . VAL   A 1 35  ? 23.714 -1.744  10.817  1.00 11.32 ?  35  VAL   A CB   1 
ATOM   1006 C CG1  . VAL   A 1 35  ? 24.788 -0.655  10.692  1.00 11.86 ?  35  VAL   A CG1  1 
ATOM   1007 C CG2  . VAL   A 1 35  ? 22.480 -1.382  9.993   1.00 12.10 ?  35  VAL   A CG2  1 
ATOM   1008 H H    . VAL   A 1 35  ? 25.938 -3.098  11.398  1.00 12.77 ?  35  VAL   A H    1 
ATOM   1009 H HA   . VAL   A 1 35  ? 23.489 -3.749  10.436  1.00 12.34 ?  35  VAL   A HA   1 
ATOM   1010 H HB   . VAL   A 1 35  ? 23.443 -1.775  11.742  1.00 13.59 ?  35  VAL   A HB   1 
ATOM   1011 H HG11 . VAL   A 1 35  ? 24.442 0.178   11.053  1.00 14.23 ?  35  VAL   A HG11 1 
ATOM   1012 H HG12 . VAL   A 1 35  ? 25.576 -0.925  11.194  1.00 14.23 ?  35  VAL   A HG12 1 
ATOM   1013 H HG13 . VAL   A 1 35  ? 25.022 -0.534  9.757   1.00 14.23 ?  35  VAL   A HG13 1 
ATOM   1014 H HG21 . VAL   A 1 35  ? 22.134 -0.529  10.299  1.00 14.52 ?  35  VAL   A HG21 1 
ATOM   1015 H HG22 . VAL   A 1 35  ? 22.731 -1.314  9.054   1.00 14.52 ?  35  VAL   A HG22 1 
ATOM   1016 H HG23 . VAL   A 1 35  ? 21.812 -2.072  10.105  1.00 14.52 ?  35  VAL   A HG23 1 
ATOM   1017 N N    . VAL   A 1 36  ? 23.987 -3.612  8.043   1.00 9.28  ?  36  VAL   A N    1 
ATOM   1018 C CA   . VAL   A 1 36  ? 24.368 -3.628  6.635   1.00 9.16  ?  36  VAL   A CA   1 
ATOM   1019 C C    . VAL   A 1 36  ? 23.911 -2.341  5.959   1.00 9.36  ?  36  VAL   A C    1 
ATOM   1020 O O    . VAL   A 1 36  ? 22.749 -1.938  6.088   1.00 9.91  ?  36  VAL   A O    1 
ATOM   1021 C CB   . VAL   A 1 36  ? 23.774 -4.855  5.922   1.00 9.33  ?  36  VAL   A CB   1 
ATOM   1022 C CG1  . VAL   A 1 36  ? 24.039 -4.795  4.440   1.00 10.10 ?  36  VAL   A CG1  1 
ATOM   1023 C CG2  . VAL   A 1 36  ? 24.318 -6.142  6.520   1.00 10.32 ?  36  VAL   A CG2  1 
ATOM   1024 H H    . VAL   A 1 36  ? 23.195 -3.928  8.191   1.00 11.13 ?  36  VAL   A H    1 
ATOM   1025 H HA   . VAL   A 1 36  ? 25.339 -3.688  6.573   1.00 10.99 ?  36  VAL   A HA   1 
ATOM   1026 H HB   . VAL   A 1 36  ? 22.814 -4.854  6.053   1.00 11.20 ?  36  VAL   A HB   1 
ATOM   1027 H HG11 . VAL   A 1 36  ? 23.902 -5.676  4.061   1.00 12.12 ?  36  VAL   A HG11 1 
ATOM   1028 H HG12 . VAL   A 1 36  ? 23.426 -4.162  4.035   1.00 12.12 ?  36  VAL   A HG12 1 
ATOM   1029 H HG13 . VAL   A 1 36  ? 24.955 -4.511  4.297   1.00 12.12 ?  36  VAL   A HG13 1 
ATOM   1030 H HG21 . VAL   A 1 36  ? 23.934 -6.900  6.045   1.00 12.38 ?  36  VAL   A HG21 1 
ATOM   1031 H HG22 . VAL   A 1 36  ? 25.284 -6.154  6.428   1.00 12.38 ?  36  VAL   A HG22 1 
ATOM   1032 H HG23 . VAL   A 1 36  ? 24.074 -6.188  7.458   1.00 12.38 ?  36  VAL   A HG23 1 
ATOM   1033 N N    . ASN   A 1 37  ? 24.825 -1.713  5.222   1.00 9.01  ?  37  ASN   A N    1 
ATOM   1034 C CA   . ASN   A 1 37  ? 24.498 -0.601  4.347   1.00 8.93  ?  37  ASN   A CA   1 
ATOM   1035 C C    . ASN   A 1 37  ? 24.385 -1.090  2.911   1.00 9.07  ?  37  ASN   A C    1 
ATOM   1036 O O    . ASN   A 1 37  ? 25.180 -1.924  2.458   1.00 9.45  ?  37  ASN   A O    1 
ATOM   1037 C CB   . ASN   A 1 37  ? 25.570 0.486   4.425   1.00 9.62  ?  37  ASN   A CB   1 
ATOM   1038 C CG   . ASN   A 1 37  ? 25.237 1.673   3.564   1.00 9.98  ?  37  ASN   A CG   1 
ATOM   1039 O OD1  . ASN   A 1 37  ? 24.060 1.999   3.366   1.00 10.43 ?  37  ASN   A OD1  1 
ATOM   1040 N ND2  . ASN   A 1 37  ? 26.268 2.331   3.045   1.00 10.31 ?  37  ASN   A ND2  1 
ATOM   1041 H H    . ASN   A 1 37  ? 25.664 -1.924  5.216   1.00 10.81 ?  37  ASN   A H    1 
ATOM   1042 H HA   . ASN   A 1 37  ? 23.656 -0.214  4.617   1.00 10.72 ?  37  ASN   A HA   1 
ATOM   1043 H HB2  . ASN   A 1 37  ? 25.650 0.793   5.342   1.00 11.54 ?  37  ASN   A HB2  1 
ATOM   1044 H HB3  . ASN   A 1 37  ? 26.423 0.117   4.127   1.00 11.54 ?  37  ASN   A HB3  1 
ATOM   1045 H HD21 . ASN   A 1 37  ? 26.132 3.013   2.534   1.00 12.38 ?  37  ASN   A HD21 1 
ATOM   1046 H HD22 . ASN   A 1 37  ? 27.072 2.075   3.194   1.00 12.38 ?  37  ASN   A HD22 1 
ATOM   1047 N N    A ALA   A 1 38  ? 23.369 -0.562  2.223   0.42 9.44  ?  38  ALA   A N    1 
ATOM   1048 N N    B ALA   A 1 38  ? 23.376 -0.598  2.192   0.58 9.55  ?  38  ALA   A N    1 
ATOM   1049 C CA   A ALA   A 1 38  ? 23.181 -0.679  0.779   0.42 9.53  ?  38  ALA   A CA   1 
ATOM   1050 C CA   B ALA   A 1 38  ? 23.239 -0.880  0.761   0.58 10.09 ?  38  ALA   A CA   1 
ATOM   1051 C C    A ALA   A 1 38  ? 24.099 0.336   0.101   0.42 9.71  ?  38  ALA   A C    1 
ATOM   1052 C C    B ALA   A 1 38  ? 24.033 0.177   0.003   0.58 10.01 ?  38  ALA   A C    1 
ATOM   1053 O O    A ALA   A 1 38  ? 23.704 1.449   -0.257  0.42 9.17  ?  38  ALA   A O    1 
ATOM   1054 O O    B ALA   A 1 38  ? 23.512 1.226   -0.386  0.58 10.57 ?  38  ALA   A O    1 
ATOM   1055 C CB   A ALA   A 1 38  ? 21.718 -0.420  0.430   0.42 9.59  ?  38  ALA   A CB   1 
ATOM   1056 C CB   B ALA   A 1 38  ? 21.775 -0.912  0.339   0.58 10.60 ?  38  ALA   A CB   1 
ATOM   1057 H H    A ALA   A 1 38  ? 22.745 -0.103  2.601   0.42 11.33 ?  38  ALA   A H    1 
ATOM   1058 H H    B ALA   A 1 38  ? 22.757 -0.091  2.513   0.58 11.46 ?  38  ALA   A H    1 
ATOM   1059 H HA   A ALA   A 1 38  ? 23.422 -1.568  0.486   0.42 11.43 ?  38  ALA   A HA   1 
ATOM   1060 H HA   B ALA   A 1 38  ? 23.628 -1.747  0.571   0.58 12.11 ?  38  ALA   A HA   1 
ATOM   1061 H HB1  A ALA   A 1 38  ? 21.605 -0.489  -0.530  0.42 11.51 ?  38  ALA   A HB1  1 
ATOM   1062 H HB1  B ALA   A 1 38  ? 21.728 -1.104  -0.614  0.58 12.71 ?  38  ALA   A HB1  1 
ATOM   1063 H HB2  A ALA   A 1 38  ? 21.162 -1.075  0.879   0.42 11.51 ?  38  ALA   A HB2  1 
ATOM   1064 H HB2  B ALA   A 1 38  ? 21.316 -1.606  0.836   0.58 12.71 ?  38  ALA   A HB2  1 
ATOM   1065 H HB3  A ALA   A 1 38  ? 21.475 0.475   0.726   0.42 11.51 ?  38  ALA   A HB3  1 
ATOM   1066 H HB3  B ALA   A 1 38  ? 21.373 -0.050  0.521   0.58 12.71 ?  38  ALA   A HB3  1 
ATOM   1067 N N    A ALA   A 1 39  ? 25.359 -0.059  -0.061  0.42 10.22 ?  39  ALA   A N    1 
ATOM   1068 N N    B ALA   A 1 39  ? 25.319 -0.102  -0.199  0.58 10.40 ?  39  ALA   A N    1 
ATOM   1069 C CA   A ALA   A 1 39  ? 26.417 0.824   -0.523  0.42 10.14 ?  39  ALA   A CA   1 
ATOM   1070 C CA   B ALA   A 1 39  ? 26.266 0.882   -0.691  0.58 10.07 ?  39  ALA   A CA   1 
ATOM   1071 C C    A ALA   A 1 39  ? 26.566 0.780   -2.041  0.42 9.98  ?  39  ALA   A C    1 
ATOM   1072 C C    B ALA   A 1 39  ? 26.417 0.803   -2.205  0.58 9.72  ?  39  ALA   A C    1 
ATOM   1073 O O    A ALA   A 1 39  ? 26.055 -0.112  -2.724  0.42 11.01 ?  39  ALA   A O    1 
ATOM   1074 O O    B ALA   A 1 39  ? 25.991 -0.154  -2.858  0.58 10.41 ?  39  ALA   A O    1 
ATOM   1075 C CB   A ALA   A 1 39  ? 27.744 0.417   0.123   0.42 10.24 ?  39  ALA   A CB   1 
ATOM   1076 C CB   B ALA   A 1 39  ? 27.625 0.670   -0.023  0.58 11.29 ?  39  ALA   A CB   1 
ATOM   1077 H H    A ALA   A 1 39  ? 25.631 -0.859  0.101   0.42 12.26 ?  39  ALA   A H    1 
ATOM   1078 H H    B ALA   A 1 39  ? 25.670 -0.879  -0.049  0.58 12.48 ?  39  ALA   A H    1 
ATOM   1079 H HA   A ALA   A 1 39  ? 26.218 1.737   -0.259  0.42 12.17 ?  39  ALA   A HA   1 
ATOM   1080 H HA   B ALA   A 1 39  ? 25.949 1.766   -0.456  0.58 12.08 ?  39  ALA   A HA   1 
ATOM   1081 H HB1  A ALA   A 1 39  ? 28.445 1.013   -0.193  0.42 12.29 ?  39  ALA   A HB1  1 
ATOM   1082 H HB1  B ALA   A 1 39  ? 28.248 1.335   -0.358  0.58 13.55 ?  39  ALA   A HB1  1 
ATOM   1083 H HB2  A ALA   A 1 39  ? 27.665 0.489   1.088   0.42 12.29 ?  39  ALA   A HB2  1 
ATOM   1084 H HB2  B ALA   A 1 39  ? 27.526 0.770   0.940   0.58 13.55 ?  39  ALA   A HB2  1 
ATOM   1085 H HB3  A ALA   A 1 39  ? 27.952 -0.496  -0.125  0.42 12.29 ?  39  ALA   A HB3  1 
ATOM   1086 H HB3  B ALA   A 1 39  ? 27.948 -0.220  -0.230  0.58 13.55 ?  39  ALA   A HB3  1 
ATOM   1087 N N    A ASN   A 1 40  ? 27.292 1.765   -2.567  0.42 9.96  ?  40  ASN   A N    1 
ATOM   1088 N N    B ASN   A 1 40  ? 27.029 1.841   -2.767  0.58 9.30  ?  40  ASN   A N    1 
ATOM   1089 C CA   A ASN   A 1 40  ? 27.844 1.715   -3.914  0.42 10.42 ?  40  ASN   A CA   1 
ATOM   1090 C CA   B ASN   A 1 40  ? 27.581 1.774   -4.112  0.58 9.31  ?  40  ASN   A CA   1 
ATOM   1091 C C    A ASN   A 1 40  ? 29.366 1.602   -3.836  0.42 9.98  ?  40  ASN   A C    1 
ATOM   1092 C C    B ASN   A 1 40  ? 29.100 1.625   -4.021  0.58 8.81  ?  40  ASN   A C    1 
ATOM   1093 O O    A ASN   A 1 40  ? 29.965 1.727   -2.763  0.42 10.15 ?  40  ASN   A O    1 
ATOM   1094 O O    B ASN   A 1 40  ? 29.685 1.706   -2.939  0.58 8.89  ?  40  ASN   A O    1 
ATOM   1095 C CB   A ASN   A 1 40  ? 27.400 2.921   -4.762  0.42 11.47 ?  40  ASN   A CB   1 
ATOM   1096 C CB   B ASN   A 1 40  ? 27.167 2.986   -4.961  0.58 10.06 ?  40  ASN   A CB   1 
ATOM   1097 C CG   A ASN   A 1 40  ? 27.758 4.254   -4.132  0.42 12.71 ?  40  ASN   A CG   1 
ATOM   1098 C CG   B ASN   A 1 40  ? 27.548 4.307   -4.331  0.58 10.11 ?  40  ASN   A CG   1 
ATOM   1099 O OD1  A ASN   A 1 40  ? 28.929 4.532   -3.862  0.42 12.46 ?  40  ASN   A OD1  1 
ATOM   1100 O OD1  B ASN   A 1 40  ? 28.716 4.536   -4.007  0.58 11.08 ?  40  ASN   A OD1  1 
ATOM   1101 N ND2  A ASN   A 1 40  ? 26.748 5.097   -3.917  0.42 13.93 ?  40  ASN   A ND2  1 
ATOM   1102 N ND2  B ASN   A 1 40  ? 26.565 5.193   -4.171  0.58 11.66 ?  40  ASN   A ND2  1 
ATOM   1103 H H    A ASN   A 1 40  ? 27.484 2.493   -2.149  0.42 11.95 ?  40  ASN   A H    1 
ATOM   1104 H H    B ASN   A 1 40  ? 27.135 2.603   -2.381  0.58 11.16 ?  40  ASN   A H    1 
ATOM   1105 H HA   A ASN   A 1 40  ? 27.512 0.920   -4.354  0.42 12.51 ?  40  ASN   A HA   1 
ATOM   1106 H HA   B ASN   A 1 40  ? 27.229 0.981   -4.548  0.58 11.17 ?  40  ASN   A HA   1 
ATOM   1107 H HB2  A ASN   A 1 40  ? 27.831 2.871   -5.635  0.42 13.76 ?  40  ASN   A HB2  1 
ATOM   1108 H HB2  B ASN   A 1 40  ? 27.608 2.927   -5.824  0.58 12.07 ?  40  ASN   A HB2  1 
ATOM   1109 H HB3  A ASN   A 1 40  ? 26.436 2.893   -4.876  0.42 13.76 ?  40  ASN   A HB3  1 
ATOM   1110 H HB3  B ASN   A 1 40  ? 26.204 2.974   -5.082  0.58 12.07 ?  40  ASN   A HB3  1 
ATOM   1111 H HD21 A ASN   A 1 40  ? 26.898 5.873   -3.576  0.42 16.72 ?  40  ASN   A HD21 1 
ATOM   1112 H HD21 B ASN   A 1 40  ? 26.731 5.961   -3.818  0.58 13.99 ?  40  ASN   A HD21 1 
ATOM   1113 H HD22 A ASN   A 1 40  ? 25.944 4.868   -4.122  0.42 16.72 ?  40  ASN   A HD22 1 
ATOM   1114 H HD22 B ASN   A 1 40  ? 25.764 4.996   -4.412  0.58 13.99 ?  40  ASN   A HD22 1 
ATOM   1115 N N    A VAL   A 1 41  ? 29.990 1.351   -4.991  0.42 10.26 ?  41  VAL   A N    1 
ATOM   1116 N N    B VAL   A 1 41  ? 29.737 1.385   -5.170  0.58 9.45  ?  41  VAL   A N    1 
ATOM   1117 C CA   A VAL   A 1 41  ? 31.418 1.024   -5.015  0.42 10.95 ?  41  VAL   A CA   1 
ATOM   1118 C CA   B VAL   A 1 41  ? 31.161 1.059   -5.166  0.58 9.98  ?  41  VAL   A CA   1 
ATOM   1119 C C    A VAL   A 1 41  ? 32.271 2.172   -4.497  0.42 10.65 ?  41  VAL   A C    1 
ATOM   1120 C C    B VAL   A 1 41  ? 32.029 2.208   -4.673  0.58 10.11 ?  41  VAL   A C    1 
ATOM   1121 O O    A VAL   A 1 41  ? 33.375 1.949   -3.983  0.42 11.27 ?  41  VAL   A O    1 
ATOM   1122 O O    B VAL   A 1 41  ? 33.182 1.979   -4.293  0.58 10.19 ?  41  VAL   A O    1 
ATOM   1123 C CB   A VAL   A 1 41  ? 31.883 0.560   -6.415  0.42 11.32 ?  41  VAL   A CB   1 
ATOM   1124 C CB   B VAL   A 1 41  ? 31.670 0.569   -6.541  0.58 11.72 ?  41  VAL   A CB   1 
ATOM   1125 C CG1  A VAL   A 1 41  ? 31.210 -0.748  -6.803  0.42 10.95 ?  41  VAL   A CG1  1 
ATOM   1126 C CG1  B VAL   A 1 41  ? 30.932 -0.684  -6.987  0.58 13.19 ?  41  VAL   A CG1  1 
ATOM   1127 C CG2  A VAL   A 1 41  ? 31.645 1.631   -7.472  0.42 12.42 ?  41  VAL   A CG2  1 
ATOM   1128 C CG2  B VAL   A 1 41  ? 31.599 1.670   -7.594  0.58 12.56 ?  41  VAL   A CG2  1 
ATOM   1129 H H    A VAL   A 1 41  ? 29.614 1.360   -5.760  0.42 12.32 ?  41  VAL   A H    1 
ATOM   1130 H H    B VAL   A 1 41  ? 29.365 1.392   -5.946  0.58 11.34 ?  41  VAL   A H    1 
ATOM   1131 H HA   A VAL   A 1 41  ? 31.567 0.284   -4.414  0.42 13.14 ?  41  VAL   A HA   1 
ATOM   1132 H HA   B VAL   A 1 41  ? 31.288 0.324   -4.549  0.58 11.97 ?  41  VAL   A HA   1 
ATOM   1133 H HB   A VAL   A 1 41  ? 32.840 0.390   -6.385  0.42 13.59 ?  41  VAL   A HB   1 
ATOM   1134 H HB   B VAL   A 1 41  ? 32.603 0.327   -6.443  0.58 14.06 ?  41  VAL   A HB   1 
ATOM   1135 H HG11 A VAL   A 1 41  ? 31.540 -1.036  -7.670  0.42 13.14 ?  41  VAL   A HG11 1 
ATOM   1136 H HG11 B VAL   A 1 41  ? 31.269 -0.959  -7.855  0.58 15.82 ?  41  VAL   A HG11 1 
ATOM   1137 H HG12 A VAL   A 1 41  ? 31.410 -1.422  -6.135  0.42 13.14 ?  41  VAL   A HG12 1 
ATOM   1138 H HG12 B VAL   A 1 41  ? 31.083 -1.390  -6.338  0.58 15.82 ?  41  VAL   A HG12 1 
ATOM   1139 H HG13 A VAL   A 1 41  ? 30.249 -0.607  -6.850  0.42 13.14 ?  41  VAL   A HG13 1 
ATOM   1140 H HG13 B VAL   A 1 41  ? 29.983 -0.492  -7.049  0.58 15.82 ?  41  VAL   A HG13 1 
ATOM   1141 H HG21 A VAL   A 1 41  ? 31.927 1.290   -8.338  0.42 14.90 ?  41  VAL   A HG21 1 
ATOM   1142 H HG21 B VAL   A 1 41  ? 31.819 1.287   -8.461  0.58 15.07 ?  41  VAL   A HG21 1 
ATOM   1143 H HG22 A VAL   A 1 41  ? 30.701 1.848   -7.497  0.42 14.90 ?  41  VAL   A HG22 1 
ATOM   1144 H HG22 B VAL   A 1 41  ? 30.704 2.034   -7.611  0.58 15.07 ?  41  VAL   A HG22 1 
ATOM   1145 H HG23 A VAL   A 1 41  ? 32.162 2.419   -7.246  0.42 14.90 ?  41  VAL   A HG23 1 
ATOM   1146 H HG23 B VAL   A 1 41  ? 32.240 2.362   -7.370  0.58 15.07 ?  41  VAL   A HG23 1 
ATOM   1147 N N    A TYR   A 1 42  ? 31.791 3.407   -4.627  0.42 10.25 ?  42  TYR   A N    1 
ATOM   1148 N N    B TYR   A 1 42  ? 31.520 3.443   -4.700  0.58 10.10 ?  42  TYR   A N    1 
ATOM   1149 C CA   A TYR   A 1 42  ? 32.517 4.587   -4.175  0.42 10.24 ?  42  TYR   A CA   1 
ATOM   1150 C CA   B TYR   A 1 42  ? 32.271 4.631   -4.293  0.58 9.94  ?  42  TYR   A CA   1 
ATOM   1151 C C    A TYR   A 1 42  ? 32.189 4.951   -2.737  0.42 9.93  ?  42  TYR   A C    1 
ATOM   1152 C C    B TYR   A 1 42  ? 32.047 5.016   -2.837  0.58 9.87  ?  42  TYR   A C    1 
ATOM   1153 O O    A TYR   A 1 42  ? 32.789 5.886   -2.196  0.42 10.18 ?  42  TYR   A O    1 
ATOM   1154 O O    B TYR   A 1 42  ? 32.594 6.029   -2.384  0.58 10.37 ?  42  TYR   A O    1 
ATOM   1155 C CB   A TYR   A 1 42  ? 32.221 5.781   -5.101  0.42 10.86 ?  42  TYR   A CB   1 
ATOM   1156 C CB   B TYR   A 1 42  ? 31.908 5.820   -5.195  0.58 10.85 ?  42  TYR   A CB   1 
ATOM   1157 C CG   A TYR   A 1 42  ? 32.409 5.449   -6.568  0.42 10.92 ?  42  TYR   A CG   1 
ATOM   1158 C CG   B TYR   A 1 42  ? 32.043 5.516   -6.669  0.58 11.05 ?  42  TYR   A CG   1 
ATOM   1159 C CD1  A TYR   A 1 42  ? 33.679 5.242   -7.091  0.42 11.34 ?  42  TYR   A CD1  1 
ATOM   1160 C CD1  B TYR   A 1 42  ? 33.288 5.314   -7.249  0.58 11.23 ?  42  TYR   A CD1  1 
ATOM   1161 C CD2  A TYR   A 1 42  ? 31.321 5.323   -7.426  0.42 11.55 ?  42  TYR   A CD2  1 
ATOM   1162 C CD2  B TYR   A 1 42  ? 30.923 5.432   -7.484  0.58 12.87 ?  42  TYR   A CD2  1 
ATOM   1163 C CE1  A TYR   A 1 42  ? 33.865 4.920   -8.422  0.42 11.45 ?  42  TYR   A CE1  1 
ATOM   1164 C CE1  B TYR   A 1 42  ? 33.411 5.027   -8.598  0.58 11.94 ?  42  TYR   A CE1  1 
ATOM   1165 C CE2  A TYR   A 1 42  ? 31.501 5.012   -8.767  0.42 11.84 ?  42  TYR   A CE2  1 
ATOM   1166 C CE2  B TYR   A 1 42  ? 31.036 5.159   -8.835  0.58 13.74 ?  42  TYR   A CE2  1 
ATOM   1167 C CZ   A TYR   A 1 42  ? 32.778 4.808   -9.255  0.42 11.79 ?  42  TYR   A CZ   1 
ATOM   1168 C CZ   B TYR   A 1 42  ? 32.281 4.954   -9.388  0.58 13.18 ?  42  TYR   A CZ   1 
ATOM   1169 O OH   A TYR   A 1 42  ? 32.968 4.492   -10.580 0.42 12.66 ?  42  TYR   A OH   1 
ATOM   1170 O OH   B TYR   A 1 42  ? 32.402 4.677   -10.731 0.58 14.21 ?  42  TYR   A OH   1 
ATOM   1171 H H    A TYR   A 1 42  ? 31.028 3.588   -4.963  0.42 12.30 ?  42  TYR   A H    1 
ATOM   1172 H H    B TYR   A 1 42  ? 30.718 3.621   -4.966  0.58 12.12 ?  42  TYR   A H    1 
ATOM   1173 H HA   A TYR   A 1 42  ? 33.473 4.409   -4.223  0.42 12.28 ?  42  TYR   A HA   1 
ATOM   1174 H HA   B TYR   A 1 42  ? 33.212 4.453   -4.407  0.58 11.93 ?  42  TYR   A HA   1 
ATOM   1175 H HB2  A TYR   A 1 42  ? 31.302 6.060   -4.970  0.42 13.03 ?  42  TYR   A HB2  1 
ATOM   1176 H HB2  B TYR   A 1 42  ? 30.986 6.075   -5.026  0.58 13.02 ?  42  TYR   A HB2  1 
ATOM   1177 H HB3  A TYR   A 1 42  ? 32.822 6.512   -4.878  0.42 13.03 ?  42  TYR   A HB3  1 
ATOM   1178 H HB3  B TYR   A 1 42  ? 32.498 6.561   -4.988  0.58 13.02 ?  42  TYR   A HB3  1 
ATOM   1179 H HD1  A TYR   A 1 42  ? 34.419 5.313   -6.533  0.42 13.60 ?  42  TYR   A HD1  1 
ATOM   1180 H HD1  B TYR   A 1 42  ? 34.052 5.356   -6.718  0.58 13.48 ?  42  TYR   A HD1  1 
ATOM   1181 H HD2  A TYR   A 1 42  ? 30.460 5.462   -7.098  0.42 13.87 ?  42  TYR   A HD2  1 
ATOM   1182 H HD2  B TYR   A 1 42  ? 30.080 5.575   -7.115  0.58 15.44 ?  42  TYR   A HD2  1 
ATOM   1183 H HE1  A TYR   A 1 42  ? 34.721 4.784   -8.759  0.42 13.74 ?  42  TYR   A HE1  1 
ATOM   1184 H HE1  B TYR   A 1 42  ? 34.253 4.888   -8.970  0.58 14.32 ?  42  TYR   A HE1  1 
ATOM   1185 H HE2  A TYR   A 1 42  ? 30.761 4.932   -9.334  0.42 14.20 ?  42  TYR   A HE2  1 
ATOM   1186 H HE2  B TYR   A 1 42  ? 30.273 5.109   -9.366  0.58 16.49 ?  42  TYR   A HE2  1 
ATOM   1187 H HH   A TYR   A 1 42  ? 33.756 4.243   -10.710 0.42 15.20 ?  42  TYR   A HH   1 
ATOM   1188 H HH   B TYR   A 1 42  ? 31.644 4.662   -11.088 0.58 17.05 ?  42  TYR   A HH   1 
ATOM   1189 N N    . LEU   A 1 43  ? 31.252 4.242   -2.107  1.00 9.89  ?  43  LEU   A N    1 
ATOM   1190 C CA   . LEU   A 1 43  ? 30.807 4.583   -0.759  1.00 9.66  ?  43  LEU   A CA   1 
ATOM   1191 C C    . LEU   A 1 43  ? 30.322 6.028   -0.668  1.00 10.07 ?  43  LEU   A C    1 
ATOM   1192 O O    . LEU   A 1 43  ? 30.585 6.732   0.307   1.00 11.14 ?  43  LEU   A O    1 
ATOM   1193 C CB   . LEU   A 1 43  ? 31.848 4.267   0.314   1.00 10.30 ?  43  LEU   A CB   1 
ATOM   1194 C CG   . LEU   A 1 43  ? 32.342 2.820   0.398   1.00 10.71 ?  43  LEU   A CG   1 
ATOM   1195 C CD1  . LEU   A 1 43  ? 33.387 2.725   1.490   1.00 12.00 ?  43  LEU   A CD1  1 
ATOM   1196 C CD2  . LEU   A 1 43  ? 31.212 1.829   0.635   1.00 10.77 ?  43  LEU   A CD2  1 
ATOM   1197 H H    A LEU   A 1 43  ? 30.853 3.551   -2.441  0.42 11.87 ?  43  LEU   A H    1 
ATOM   1198 H H    B LEU   A 1 43  ? 30.949 3.477   -2.376  0.58 11.87 ?  43  LEU   A H    1 
ATOM   1199 H HA   . LEU   A 1 43  ? 30.035 4.019   -0.557  1.00 11.59 ?  43  LEU   A HA   1 
ATOM   1200 H HB2  . LEU   A 1 43  ? 32.620 4.826   0.161   1.00 12.36 ?  43  LEU   A HB2  1 
ATOM   1201 H HB3  . LEU   A 1 43  ? 31.461 4.481   1.182   1.00 12.36 ?  43  LEU   A HB3  1 
ATOM   1202 H HG   . LEU   A 1 43  ? 32.772 2.582   -0.440  1.00 12.85 ?  43  LEU   A HG   1 
ATOM   1203 H HD11 . LEU   A 1 43  ? 33.704 1.810   1.544   1.00 14.40 ?  43  LEU   A HD11 1 
ATOM   1204 H HD12 . LEU   A 1 43  ? 34.120 3.319   1.272   1.00 14.40 ?  43  LEU   A HD12 1 
ATOM   1205 H HD13 . LEU   A 1 43  ? 32.983 2.987   2.331   1.00 14.40 ?  43  LEU   A HD13 1 
ATOM   1206 H HD21 . LEU   A 1 43  ? 31.588 0.943   0.762   1.00 12.92 ?  43  LEU   A HD21 1 
ATOM   1207 H HD22 . LEU   A 1 43  ? 30.719 2.097   1.423   1.00 12.92 ?  43  LEU   A HD22 1 
ATOM   1208 H HD23 . LEU   A 1 43  ? 30.628 1.830   -0.140  1.00 12.92 ?  43  LEU   A HD23 1 
ATOM   1209 N N    A LYS   A 1 44  ? 29.614 6.477   -1.702  0.42 10.27 ?  44  LYS   A N    1 
ATOM   1210 N N    B LYS   A 1 44  ? 29.600 6.467   -1.698  0.58 9.96  ?  44  LYS   A N    1 
ATOM   1211 C CA   A LYS   A 1 44  ? 28.986 7.798   -1.701  0.42 10.90 ?  44  LYS   A CA   1 
ATOM   1212 C CA   B LYS   A 1 44  ? 28.952 7.777   -1.706  0.58 10.50 ?  44  LYS   A CA   1 
ATOM   1213 C C    A LYS   A 1 44  ? 27.559 7.619   -1.204  0.42 10.23 ?  44  LYS   A C    1 
ATOM   1214 C C    B LYS   A 1 44  ? 27.524 7.580   -1.222  0.58 10.29 ?  44  LYS   A C    1 
ATOM   1215 O O    A LYS   A 1 44  ? 26.693 7.123   -1.928  0.42 11.28 ?  44  LYS   A O    1 
ATOM   1216 O O    B LYS   A 1 44  ? 26.677 7.047   -1.945  0.58 11.30 ?  44  LYS   A O    1 
ATOM   1217 C CB   A LYS   A 1 44  ? 29.035 8.415   -3.093  0.42 13.05 ?  44  LYS   A CB   1 
ATOM   1218 C CB   B LYS   A 1 44  ? 29.005 8.387   -3.101  0.58 12.58 ?  44  LYS   A CB   1 
ATOM   1219 C CG   A LYS   A 1 44  ? 30.426 8.831   -3.541  0.42 16.57 ?  44  LYS   A CG   1 
ATOM   1220 C CG   B LYS   A 1 44  ? 30.374 8.901   -3.503  0.58 16.76 ?  44  LYS   A CG   1 
ATOM   1221 C CD   A LYS   A 1 44  ? 31.091 9.759   -2.533  0.42 20.69 ?  44  LYS   A CD   1 
ATOM   1222 C CD   B LYS   A 1 44  ? 31.008 9.736   -2.401  0.58 21.72 ?  44  LYS   A CD   1 
ATOM   1223 C CE   A LYS   A 1 44  ? 32.429 10.254  -3.040  0.42 23.21 ?  44  LYS   A CE   1 
ATOM   1224 C CE   B LYS   A 1 44  ? 32.274 10.411  -2.876  0.58 24.19 ?  44  LYS   A CE   1 
ATOM   1225 N NZ   A LYS   A 1 44  ? 33.212 10.920  -1.966  0.42 24.46 ?  44  LYS   A NZ   1 
ATOM   1226 N NZ   B LYS   A 1 44  ? 33.113 10.852  -1.731  0.58 25.51 ?  44  LYS   A NZ   1 
ATOM   1227 H H    A LYS   A 1 44  ? 29.483 6.027   -2.426  0.42 12.33 ?  44  LYS   A H    1 
ATOM   1228 H H    B LYS   A 1 44  ? 29.470 6.014   -2.417  0.58 11.96 ?  44  LYS   A H    1 
ATOM   1229 H HA   A LYS   A 1 44  ? 29.449 8.373   -1.072  0.42 13.08 ?  44  LYS   A HA   1 
ATOM   1230 H HA   B LYS   A 1 44  ? 29.394 8.360   -1.068  0.58 12.60 ?  44  LYS   A HA   1 
ATOM   1231 H HB2  A LYS   A 1 44  ? 28.699 7.770   -3.732  0.42 15.66 ?  44  LYS   A HB2  1 
ATOM   1232 H HB2  B LYS   A 1 44  ? 28.741 7.716   -3.747  0.58 15.10 ?  44  LYS   A HB2  1 
ATOM   1233 H HB3  A LYS   A 1 44  ? 28.475 9.207   -3.099  0.42 15.66 ?  44  LYS   A HB3  1 
ATOM   1234 H HB3  B LYS   A 1 44  ? 28.390 9.138   -3.135  0.58 15.10 ?  44  LYS   A HB3  1 
ATOM   1235 H HG2  A LYS   A 1 44  ? 30.981 8.041   -3.639  0.42 19.89 ?  44  LYS   A HG2  1 
ATOM   1236 H HG2  B LYS   A 1 44  ? 30.956 8.146   -3.688  0.58 20.12 ?  44  LYS   A HG2  1 
ATOM   1237 H HG3  A LYS   A 1 44  ? 30.362 9.302   -4.388  0.42 19.89 ?  44  LYS   A HG3  1 
ATOM   1238 H HG3  B LYS   A 1 44  ? 30.288 9.458   -4.294  0.58 20.12 ?  44  LYS   A HG3  1 
ATOM   1239 H HD2  A LYS   A 1 44  ? 30.512 10.521  -2.372  0.42 24.83 ?  44  LYS   A HD2  1 
ATOM   1240 H HD2  B LYS   A 1 44  ? 30.377 10.413  -2.110  0.58 26.07 ?  44  LYS   A HD2  1 
ATOM   1241 H HD3  A LYS   A 1 44  ? 31.248 9.274   -1.706  0.42 24.83 ?  44  LYS   A HD3  1 
ATOM   1242 H HD3  B LYS   A 1 44  ? 31.247 9.156   -1.659  0.58 26.07 ?  44  LYS   A HD3  1 
ATOM   1243 H HE2  A LYS   A 1 44  ? 32.943 9.499   -3.367  0.42 27.85 ?  44  LYS   A HE2  1 
ATOM   1244 H HE2  B LYS   A 1 44  ? 32.791 9.782   -3.407  0.58 29.03 ?  44  LYS   A HE2  1 
ATOM   1245 H HE3  A LYS   A 1 44  ? 32.281 10.893  -3.752  0.42 27.85 ?  44  LYS   A HE3  1 
ATOM   1246 H HE3  B LYS   A 1 44  ? 32.043 11.187  -3.405  0.58 29.03 ?  44  LYS   A HE3  1 
ATOM   1247 H HZ1  A LYS   A 1 44  ? 33.991 11.201  -2.288  0.42 29.36 ?  44  LYS   A HZ1  1 
ATOM   1248 H HZ1  B LYS   A 1 44  ? 33.852 11.247  -2.031  0.58 30.61 ?  44  LYS   A HZ1  1 
ATOM   1249 H HZ2  A LYS   A 1 44  ? 32.760 11.621  -1.650  0.42 29.36 ?  44  LYS   A HZ2  1 
ATOM   1250 H HZ2  B LYS   A 1 44  ? 32.659 11.432  -1.229  0.58 30.61 ?  44  LYS   A HZ2  1 
ATOM   1251 H HZ3  A LYS   A 1 44  ? 33.362 10.351  -1.299  0.42 29.36 ?  44  LYS   A HZ3  1 
ATOM   1252 H HZ3  B LYS   A 1 44  ? 33.340 10.153  -1.231  0.58 30.61 ?  44  LYS   A HZ3  1 
ATOM   1253 N N    A HIS   A 1 45  ? 27.318 8.015   0.045   0.42 9.42  ?  45  HIS   A N    1 
ATOM   1254 N N    B HIS   A 1 45  ? 27.266 7.985   0.020   0.58 10.21 ?  45  HIS   A N    1 
ATOM   1255 C CA   A HIS   A 1 45  ? 26.085 7.658   0.749   0.42 9.12  ?  45  HIS   A CA   1 
ATOM   1256 C CA   B HIS   A 1 45  ? 26.007 7.678   0.698   0.58 10.26 ?  45  HIS   A CA   1 
ATOM   1257 C C    A HIS   A 1 45  ? 25.042 8.771   0.608   0.42 9.69  ?  45  HIS   A C    1 
ATOM   1258 C C    B HIS   A 1 45  ? 25.020 8.818   0.473   0.58 10.74 ?  45  HIS   A C    1 
ATOM   1259 O O    A HIS   A 1 45  ? 24.657 9.442   1.566   0.42 10.28 ?  45  HIS   A O    1 
ATOM   1260 O O    B HIS   A 1 45  ? 24.899 9.739   1.283   0.58 12.25 ?  45  HIS   A O    1 
ATOM   1261 C CB   A HIS   A 1 45  ? 26.396 7.343   2.202   0.42 9.27  ?  45  HIS   A CB   1 
ATOM   1262 C CB   B HIS   A 1 45  ? 26.268 7.466   2.177   0.58 10.40 ?  45  HIS   A CB   1 
ATOM   1263 C CG   A HIS   A 1 45  ? 27.505 6.354   2.379   0.42 8.79  ?  45  HIS   A CG   1 
ATOM   1264 C CG   B HIS   A 1 45  ? 27.392 6.523   2.459   0.58 9.62  ?  45  HIS   A CG   1 
ATOM   1265 N ND1  A HIS   A 1 45  ? 27.470 5.082   1.843   0.42 8.88  ?  45  HIS   A ND1  1 
ATOM   1266 N ND1  B HIS   A 1 45  ? 27.425 5.230   1.977   0.58 10.39 ?  45  HIS   A ND1  1 
ATOM   1267 C CD2  A HIS   A 1 45  ? 28.687 6.458   3.032   0.42 9.49  ?  45  HIS   A CD2  1 
ATOM   1268 C CD2  B HIS   A 1 45  ? 28.532 6.694   3.171   0.58 9.01  ?  45  HIS   A CD2  1 
ATOM   1269 C CE1  A HIS   A 1 45  ? 28.581 4.445   2.168   0.42 9.90  ?  45  HIS   A CE1  1 
ATOM   1270 C CE1  B HIS   A 1 45  ? 28.536 4.645   2.393   0.58 9.08  ?  45  HIS   A CE1  1 
ATOM   1271 N NE2  A HIS   A 1 45  ? 29.337 5.257   2.887   0.42 10.16 ?  45  HIS   A NE2  1 
ATOM   1272 N NE2  B HIS   A 1 45  ? 29.224 5.510   3.117   0.58 8.66  ?  45  HIS   A NE2  1 
ATOM   1273 H H    A HIS   A 1 45  ? 27.857 8.502   0.512   0.42 11.31 ?  45  HIS   A H    1 
ATOM   1274 H H    B HIS   A 1 45  ? 27.812 8.449   0.500   0.58 12.25 ?  45  HIS   A H    1 
ATOM   1275 H HA   A HIS   A 1 45  ? 25.716 6.864   0.345   0.42 10.95 ?  45  HIS   A HA   1 
ATOM   1276 H HA   B HIS   A 1 45  ? 25.631 6.860   0.327   0.58 12.31 ?  45  HIS   A HA   1 
ATOM   1277 H HB2  A HIS   A 1 45  ? 26.650 8.159   2.658   0.42 11.12 ?  45  HIS   A HB2  1 
ATOM   1278 H HB2  B HIS   A 1 45  ? 26.484 8.315   2.584   0.58 12.48 ?  45  HIS   A HB2  1 
ATOM   1279 H HB3  A HIS   A 1 45  ? 25.601 6.969   2.617   0.42 11.12 ?  45  HIS   A HB3  1 
ATOM   1280 H HB3  B HIS   A 1 45  ? 25.465 7.098   2.586   0.58 12.48 ?  45  HIS   A HB3  1 
ATOM   1281 H HD2  A HIS   A 1 45  ? 29.003 7.201   3.493   0.42 11.38 ?  45  HIS   A HD2  1 
ATOM   1282 H HD2  B HIS   A 1 45  ? 28.798 7.465   3.616   0.58 10.82 ?  45  HIS   A HD2  1 
ATOM   1283 H HE1  A HIS   A 1 45  ? 28.800 3.569   1.936   0.42 11.88 ?  45  HIS   A HE1  1 
ATOM   1284 H HE1  B HIS   A 1 45  ? 28.789 3.766   2.212   0.58 10.89 ?  45  HIS   A HE1  1 
ATOM   1285 H HE2  A HIS   A 1 45  ? 30.115 5.063   3.215   0.42 12.19 ?  45  HIS   A HE2  1 
ATOM   1286 H HE2  B HIS   A 1 45  ? 29.987 5.353   3.493   0.58 10.39 ?  45  HIS   A HE2  1 
ATOM   1287 N N    A GLY   A 1 46  ? 24.561 8.933   -0.622  0.42 10.59 ?  46  GLY   A N    1 
ATOM   1288 N N    B GLY   A 1 46  ? 24.289 8.751   -0.630  0.58 11.01 ?  46  GLY   A N    1 
ATOM   1289 C CA   A GLY   A 1 46  ? 23.746 10.088  -0.966  0.42 11.55 ?  46  GLY   A CA   1 
ATOM   1290 C CA   B GLY   A 1 46  ? 23.451 9.870   -1.011  0.58 11.56 ?  46  GLY   A CA   1 
ATOM   1291 C C    A GLY   A 1 46  ? 22.245 9.934   -0.789  0.42 11.22 ?  46  GLY   A C    1 
ATOM   1292 C C    B GLY   A 1 46  ? 22.003 9.776   -0.572  0.58 11.07 ?  46  GLY   A C    1 
ATOM   1293 O O    A GLY   A 1 46  ? 21.543 10.928  -0.574  0.42 11.45 ?  46  GLY   A O    1 
ATOM   1294 O O    B GLY   A 1 46  ? 21.430 10.753  -0.074  0.58 12.43 ?  46  GLY   A O    1 
ATOM   1295 H H    A GLY   A 1 46  ? 24.698 8.391   -1.275  0.42 12.70 ?  46  GLY   A H    1 
ATOM   1296 H H    B GLY   A 1 46  ? 24.260 8.074   -1.161  0.58 13.21 ?  46  GLY   A H    1 
ATOM   1297 H HA2  A GLY   A 1 46  ? 24.038 10.844  -0.429  0.42 13.86 ?  46  GLY   A HA2  1 
ATOM   1298 H HA2  B GLY   A 1 46  ? 23.822 10.683  -0.630  0.58 13.87 ?  46  GLY   A HA2  1 
ATOM   1299 H HA3  A GLY   A 1 46  ? 23.905 10.313  -1.897  0.42 13.86 ?  46  GLY   A HA3  1 
ATOM   1300 H HA3  B GLY   A 1 46  ? 23.470 9.956   -1.973  0.58 13.87 ?  46  GLY   A HA3  1 
ATOM   1301 N N    A GLY   A 1 47  ? 21.735 8.711   -0.897  0.42 10.89 ?  47  GLY   A N    1 
ATOM   1302 N N    B GLY   A 1 47  ? 21.398 8.606   -0.754  0.58 11.16 ?  47  GLY   A N    1 
ATOM   1303 C CA   A GLY   A 1 47  ? 20.302 8.489   -0.851  0.42 10.69 ?  47  GLY   A CA   1 
ATOM   1304 C CA   B GLY   A 1 47  ? 19.979 8.440   -0.519  0.58 10.96 ?  47  GLY   A CA   1 
ATOM   1305 C C    A GLY   A 1 47  ? 19.997 7.058   -0.466  0.42 10.41 ?  47  GLY   A C    1 
ATOM   1306 C C    B GLY   A 1 47  ? 19.655 7.009   -0.152  0.58 9.89  ?  47  GLY   A C    1 
ATOM   1307 O O    A GLY   A 1 47  ? 20.896 6.255   -0.217  0.42 10.75 ?  47  GLY   A O    1 
ATOM   1308 O O    B GLY   A 1 47  ? 20.544 6.170   -0.011  0.58 9.98  ?  47  GLY   A O    1 
ATOM   1309 H H    A GLY   A 1 47  ? 22.202 8.000   -0.991  0.42 13.07 ?  47  GLY   A H    1 
ATOM   1310 H H    B GLY   A 1 47  ? 21.802 7.887   -1.002  0.58 13.40 ?  47  GLY   A H    1 
ATOM   1311 H HA2  A GLY   A 1 47  ? 19.892 9.086   -0.204  0.42 12.83 ?  47  GLY   A HA2  1 
ATOM   1312 H HA2  B GLY   A 1 47  ? 19.697 9.021   0.202   0.58 13.16 ?  47  GLY   A HA2  1 
ATOM   1313 H HA3  A GLY   A 1 47  ? 19.920 8.667   -1.725  0.42 12.83 ?  47  GLY   A HA3  1 
ATOM   1314 H HA3  B GLY   A 1 47  ? 19.489 8.670   -1.320  0.58 13.16 ?  47  GLY   A HA3  1 
ATOM   1315 N N    A GLY   A 1 48  ? 18.706 6.743   -0.423  0.42 9.88  ?  48  GLY   A N    1 
ATOM   1316 N N    B GLY   A 1 48  ? 18.362 6.739   0.009   0.58 10.12 ?  48  GLY   A N    1 
ATOM   1317 C CA   A GLY   A 1 48  ? 18.287 5.410   -0.035  0.42 10.00 ?  48  GLY   A CA   1 
ATOM   1318 C CA   B GLY   A 1 48  ? 17.951 5.412   0.425   0.58 9.57  ?  48  GLY   A CA   1 
ATOM   1319 C C    A GLY   A 1 48  ? 18.717 5.083   1.382   0.42 9.64  ?  48  GLY   A C    1 
ATOM   1320 C C    B GLY   A 1 48  ? 18.554 5.037   1.765   0.58 9.59  ?  48  GLY   A C    1 
ATOM   1321 O O    A GLY   A 1 48  ? 18.891 5.967   2.226   0.42 9.99  ?  48  GLY   A O    1 
ATOM   1322 O O    B GLY   A 1 48  ? 18.728 5.870   2.661   0.58 10.10 ?  48  GLY   A O    1 
ATOM   1323 H H    A GLY   A 1 48  ? 18.066 7.280   -0.612  0.42 11.86 ?  48  GLY   A H    1 
ATOM   1324 H H    B GLY   A 1 48  ? 17.715 7.302   -0.108  0.58 12.14 ?  48  GLY   A H    1 
ATOM   1325 H HA2  A GLY   A 1 48  ? 17.325 5.342   -0.086  0.42 12.00 ?  48  GLY   A HA2  1 
ATOM   1326 H HA2  B GLY   A 1 48  ? 16.982 5.369   0.498   0.58 11.49 ?  48  GLY   A HA2  1 
ATOM   1327 H HA3  A GLY   A 1 48  ? 18.682 4.756   -0.632  0.42 12.00 ?  48  GLY   A HA3  1 
ATOM   1328 H HA3  B GLY   A 1 48  ? 18.239 4.759   -0.232  0.58 11.49 ?  48  GLY   A HA3  1 
ATOM   1329 N N    A VAL   A 1 49  ? 18.906 3.787   1.646   0.42 10.34 ?  49  VAL   A N    1 
ATOM   1330 N N    B VAL   A 1 49  ? 18.867 3.748   1.906   0.58 9.84  ?  49  VAL   A N    1 
ATOM   1331 C CA   A VAL   A 1 49  ? 19.378 3.363   2.964   0.42 10.48 ?  49  VAL   A CA   1 
ATOM   1332 C CA   B VAL   A 1 49  ? 19.495 3.245   3.125   0.58 9.43  ?  49  VAL   A CA   1 
ATOM   1333 C C    A VAL   A 1 49  ? 20.697 4.047   3.307   0.42 9.73  ?  49  VAL   A C    1 
ATOM   1334 C C    B VAL   A 1 49  ? 20.767 4.024   3.440   0.58 9.27  ?  49  VAL   A C    1 
ATOM   1335 O O    A VAL   A 1 49  ? 20.909 4.481   4.443   0.42 10.00 ?  49  VAL   A O    1 
ATOM   1336 O O    B VAL   A 1 49  ? 21.005 4.421   4.584   0.58 9.40  ?  49  VAL   A O    1 
ATOM   1337 C CB   A VAL   A 1 49  ? 19.504 1.828   3.025   0.42 11.48 ?  49  VAL   A CB   1 
ATOM   1338 C CB   B VAL   A 1 49  ? 19.795 1.743   2.978   0.58 10.08 ?  49  VAL   A CB   1 
ATOM   1339 C CG1  A VAL   A 1 49  ? 20.289 1.399   4.264   0.42 11.59 ?  49  VAL   A CG1  1 
ATOM   1340 C CG1  B VAL   A 1 49  ? 20.656 1.257   4.132   0.58 9.82  ?  49  VAL   A CG1  1 
ATOM   1341 C CG2  A VAL   A 1 49  ? 18.128 1.176   3.015   0.42 12.88 ?  49  VAL   A CG2  1 
ATOM   1342 C CG2  B VAL   A 1 49  ? 18.502 0.936   2.881   0.58 11.28 ?  49  VAL   A CG2  1 
ATOM   1343 H H    A VAL   A 1 49  ? 18.773 3.143   1.092   0.42 12.41 ?  49  VAL   A H    1 
ATOM   1344 H H    B VAL   A 1 49  ? 18.720 3.147   1.314   0.58 11.81 ?  49  VAL   A H    1 
ATOM   1345 H HA   A VAL   A 1 49  ? 18.725 3.623   3.632   0.42 12.58 ?  49  VAL   A HA   1 
ATOM   1346 H HA   B VAL   A 1 49  ? 18.885 3.356   3.871   0.58 11.31 ?  49  VAL   A HA   1 
ATOM   1347 H HB   A VAL   A 1 49  ? 19.991 1.515   2.245   0.42 13.78 ?  49  VAL   A HB   1 
ATOM   1348 H HB   B VAL   A 1 49  ? 20.294 1.601   2.158   0.58 12.10 ?  49  VAL   A HB   1 
ATOM   1349 H HG11 A VAL   A 1 49  ? 20.115 0.461   4.441   0.42 13.91 ?  49  VAL   A HG11 1 
ATOM   1350 H HG11 B VAL   A 1 49  ? 20.585 0.293   4.190   0.58 11.78 ?  49  VAL   A HG11 1 
ATOM   1351 H HG12 A VAL   A 1 49  ? 21.237 1.533   4.106   0.42 13.91 ?  49  VAL   A HG12 1 
ATOM   1352 H HG12 B VAL   A 1 49  ? 21.577 1.512   3.968   0.58 11.78 ?  49  VAL   A HG12 1 
ATOM   1353 H HG13 A VAL   A 1 49  ? 20.000 1.934   5.022   0.42 13.91 ?  49  VAL   A HG13 1 
ATOM   1354 H HG13 B VAL   A 1 49  ? 20.337 1.664   4.952   0.58 11.78 ?  49  VAL   A HG13 1 
ATOM   1355 H HG21 A VAL   A 1 49  ? 18.235 0.212   3.044   0.42 15.46 ?  49  VAL   A HG21 1 
ATOM   1356 H HG21 B VAL   A 1 49  ? 18.719 -0.004  2.790   0.58 13.53 ?  49  VAL   A HG21 1 
ATOM   1357 H HG22 A VAL   A 1 49  ? 17.633 1.479   3.791   0.42 15.46 ?  49  VAL   A HG22 1 
ATOM   1358 H HG22 B VAL   A 1 49  ? 17.980 1.080   3.687   0.58 13.53 ?  49  VAL   A HG22 1 
ATOM   1359 H HG23 A VAL   A 1 49  ? 17.668 1.434   2.203   0.42 15.46 ?  49  VAL   A HG23 1 
ATOM   1360 H HG23 B VAL   A 1 49  ? 17.999 1.237   2.106   0.58 13.53 ?  49  VAL   A HG23 1 
ATOM   1361 N N    A ALA   A 1 50  ? 21.614 4.120   2.341   0.42 9.44  ?  50  ALA   A N    1 
ATOM   1362 N N    B ALA   A 1 50  ? 21.638 4.181   2.443   0.58 9.31  ?  50  ALA   A N    1 
ATOM   1363 C CA   A ALA   A 1 50  ? 22.937 4.678   2.609   0.42 9.31  ?  50  ALA   A CA   1 
ATOM   1364 C CA   B ALA   A 1 50  ? 22.955 4.756   2.699   0.58 9.25  ?  50  ALA   A CA   1 
ATOM   1365 C C    A ALA   A 1 50  ? 22.847 6.139   3.024   0.42 9.02  ?  50  ALA   A C    1 
ATOM   1366 C C    B ALA   A 1 50  ? 22.845 6.206   3.143   0.58 9.20  ?  50  ALA   A C    1 
ATOM   1367 O O    A ALA   A 1 50  ? 23.498 6.563   3.986   0.42 9.26  ?  50  ALA   A O    1 
ATOM   1368 O O    B ALA   A 1 50  ? 23.465 6.613   4.133   0.58 9.61  ?  50  ALA   A O    1 
ATOM   1369 C CB   A ALA   A 1 50  ? 23.814 4.535   1.369   0.42 9.80  ?  50  ALA   A CB   1 
ATOM   1370 C CB   B ALA   A 1 50  ? 23.811 4.653   1.441   0.58 9.54  ?  50  ALA   A CB   1 
ATOM   1371 H H    A ALA   A 1 50  ? 21.492 3.859   1.536   0.42 11.32 ?  50  ALA   A H    1 
ATOM   1372 H H    B ALA   A 1 50  ? 21.487 3.976   1.622   0.58 11.18 ?  50  ALA   A H    1 
ATOM   1373 H HA   A ALA   A 1 50  ? 23.348 4.191   3.338   0.42 11.18 ?  50  ALA   A HA   1 
ATOM   1374 H HA   B ALA   A 1 50  ? 23.387 4.260   3.409   0.58 11.10 ?  50  ALA   A HA   1 
ATOM   1375 H HB1  A ALA   A 1 50  ? 24.686 4.914   1.559   0.42 11.76 ?  50  ALA   A HB1  1 
ATOM   1376 H HB1  B ALA   A 1 50  ? 24.683 5.037   1.622   0.58 11.45 ?  50  ALA   A HB1  1 
ATOM   1377 H HB2  A ALA   A 1 50  ? 23.896 3.597   1.150   0.42 11.76 ?  50  ALA   A HB2  1 
ATOM   1378 H HB2  B ALA   A 1 50  ? 23.902 3.719   1.199   0.58 11.45 ?  50  ALA   A HB2  1 
ATOM   1379 H HB3  A ALA   A 1 50  ? 23.398 5.015   0.635   0.42 11.76 ?  50  ALA   A HB3  1 
ATOM   1380 H HB3  B ALA   A 1 50  ? 23.377 5.141   0.723   0.58 11.45 ?  50  ALA   A HB3  1 
ATOM   1381 N N    A GLY   A 1 51  ? 22.062 6.931   2.295   0.42 9.27  ?  51  GLY   A N    1 
ATOM   1382 N N    B GLY   A 1 51  ? 22.063 7.003   2.416   0.58 9.66  ?  51  GLY   A N    1 
ATOM   1383 C CA   A GLY   A 1 51  ? 21.888 8.322   2.679   0.42 10.26 ?  51  GLY   A CA   1 
ATOM   1384 C CA   B GLY   A 1 51  ? 21.917 8.399   2.783   0.58 9.97  ?  51  GLY   A CA   1 
ATOM   1385 C C    A GLY   A 1 51  ? 21.271 8.460   4.056   0.42 10.43 ?  51  GLY   A C    1 
ATOM   1386 C C    B GLY   A 1 51  ? 21.300 8.563   4.157   0.58 9.84  ?  51  GLY   A C    1 
ATOM   1387 O O    A GLY   A 1 51  ? 21.654 9.341   4.831   0.42 11.13 ?  51  GLY   A O    1 
ATOM   1388 O O    B GLY   A 1 51  ? 21.693 9.449   4.924   0.58 10.44 ?  51  GLY   A O    1 
ATOM   1389 H H    A GLY   A 1 51  ? 21.635 6.696   1.589   0.42 11.12 ?  51  GLY   A H    1 
ATOM   1390 H H    B GLY   A 1 51  ? 21.617 6.764   1.718   0.58 11.60 ?  51  GLY   A H    1 
ATOM   1391 H HA2  A GLY   A 1 51  ? 22.744 8.773   2.687   0.42 12.32 ?  51  GLY   A HA2  1 
ATOM   1392 H HA2  B GLY   A 1 51  ? 22.784 8.833   2.780   0.58 11.96 ?  51  GLY   A HA2  1 
ATOM   1393 H HA3  A GLY   A 1 51  ? 21.310 8.770   2.038   0.42 12.32 ?  51  GLY   A HA3  1 
ATOM   1394 H HA3  B GLY   A 1 51  ? 21.347 8.851   2.134   0.58 11.96 ?  51  GLY   A HA3  1 
ATOM   1395 N N    A ALA   A 1 52  ? 20.324 7.575   4.386   0.42 10.51 ?  52  ALA   A N    1 
ATOM   1396 N N    B ALA   A 1 52  ? 20.327 7.704   4.491   0.58 9.44  ?  52  ALA   A N    1 
ATOM   1397 C CA   A ALA   A 1 52  ? 19.666 7.626   5.687   0.42 10.62 ?  52  ALA   A CA   1 
ATOM   1398 C CA   B ALA   A 1 52  ? 19.670 7.795   5.790   0.58 10.29 ?  52  ALA   A CA   1 
ATOM   1399 C C    A ALA   A 1 52  ? 20.624 7.253   6.811   0.42 10.75 ?  52  ALA   A C    1 
ATOM   1400 C C    B ALA   A 1 52  ? 20.581 7.332   6.922   0.58 9.75  ?  52  ALA   A C    1 
ATOM   1401 O O    A ALA   A 1 52  ? 20.704 7.948   7.829   0.42 11.19 ?  52  ALA   A O    1 
ATOM   1402 O O    B ALA   A 1 52  ? 20.624 7.958   7.987   0.58 10.80 ?  52  ALA   A O    1 
ATOM   1403 C CB   A ALA   A 1 52  ? 18.448 6.700   5.684   0.42 11.15 ?  52  ALA   A CB   1 
ATOM   1404 C CB   B ALA   A 1 52  ? 18.357 7.012   5.770   0.58 11.22 ?  52  ALA   A CB   1 
ATOM   1405 H H    A ALA   A 1 52  ? 20.059 6.936   3.880   0.42 12.62 ?  52  ALA   A H    1 
ATOM   1406 H H    B ALA   A 1 52  ? 20.038 7.071   3.980   0.58 11.32 ?  52  ALA   A H    1 
ATOM   1407 H HA   A ALA   A 1 52  ? 19.355 8.528   5.852   0.42 12.75 ?  52  ALA   A HA   1 
ATOM   1408 H HA   B ALA   A 1 52  ? 19.451 8.723   5.951   0.58 12.35 ?  52  ALA   A HA   1 
ATOM   1409 H HB1  A ALA   A 1 52  ? 18.012 6.746   6.552   0.42 13.38 ?  52  ALA   A HB1  1 
ATOM   1410 H HB1  B ALA   A 1 52  ? 17.928 7.098   6.637   0.58 13.46 ?  52  ALA   A HB1  1 
ATOM   1411 H HB2  A ALA   A 1 52  ? 17.833 6.992   4.993   0.42 13.38 ?  52  ALA   A HB2  1 
ATOM   1412 H HB2  B ALA   A 1 52  ? 17.781 7.375   5.080   0.58 13.46 ?  52  ALA   A HB2  1 
ATOM   1413 H HB3  A ALA   A 1 52  ? 18.738 5.792   5.509   0.42 13.38 ?  52  ALA   A HB3  1 
ATOM   1414 H HB3  B ALA   A 1 52  ? 18.546 6.078   5.586   0.58 13.46 ?  52  ALA   A HB3  1 
ATOM   1415 N N    A LEU   A 1 53  ? 21.361 6.152   6.651   0.42 10.56 ?  53  LEU   A N    1 
ATOM   1416 N N    B LEU   A 1 53  ? 21.320 6.238   6.723   0.58 9.20  ?  53  LEU   A N    1 
ATOM   1417 C CA   A LEU   A 1 53  ? 22.299 5.748   7.696   0.42 10.80 ?  53  LEU   A CA   1 
ATOM   1418 C CA   B LEU   A 1 53  ? 22.306 5.839   7.727   0.58 9.58  ?  53  LEU   A CA   1 
ATOM   1419 C C    A LEU   A 1 53  ? 23.361 6.815   7.907   0.42 10.38 ?  53  LEU   A C    1 
ATOM   1420 C C    B LEU   A 1 53  ? 23.334 6.942   7.919   0.58 8.57  ?  53  LEU   A C    1 
ATOM   1421 O O    A LEU   A 1 53  ? 23.758 7.094   9.043   0.42 10.48 ?  53  LEU   A O    1 
ATOM   1422 O O    B LEU   A 1 53  ? 23.608 7.366   9.046   0.58 9.38  ?  53  LEU   A O    1 
ATOM   1423 C CB   A LEU   A 1 53  ? 22.957 4.413   7.338   0.42 10.51 ?  53  LEU   A CB   1 
ATOM   1424 C CB   B LEU   A 1 53  ? 23.015 4.538   7.326   0.58 9.67  ?  53  LEU   A CB   1 
ATOM   1425 C CG   A LEU   A 1 53  ? 22.037 3.189   7.370   0.42 10.71 ?  53  LEU   A CG   1 
ATOM   1426 C CG   B LEU   A 1 53  ? 22.276 3.197   7.438   0.58 10.37 ?  53  LEU   A CG   1 
ATOM   1427 C CD1  A LEU   A 1 53  ? 22.761 1.977   6.817   0.42 11.13 ?  53  LEU   A CD1  1 
ATOM   1428 C CD1  B LEU   A 1 53  ? 23.088 2.109   6.751   0.58 10.80 ?  53  LEU   A CD1  1 
ATOM   1429 C CD2  A LEU   A 1 53  ? 21.538 2.919   8.782   0.42 10.78 ?  53  LEU   A CD2  1 
ATOM   1430 C CD2  B LEU   A 1 53  ? 22.000 2.820   8.883   0.58 11.14 ?  53  LEU   A CD2  1 
ATOM   1431 H H    A LEU   A 1 53  ? 21.341 5.636   5.965   0.42 12.67 ?  53  LEU   A H    1 
ATOM   1432 H H    B LEU   A 1 53  ? 21.265 5.717   6.038   0.58 11.05 ?  53  LEU   A H    1 
ATOM   1433 H HA   A LEU   A 1 53  ? 21.821 5.635   8.529   0.42 12.96 ?  53  LEU   A HA   1 
ATOM   1434 H HA   B LEU   A 1 53  ? 21.857 5.693   8.572   0.58 11.50 ?  53  LEU   A HA   1 
ATOM   1435 H HB2  A LEU   A 1 53  ? 23.318 4.479   6.436   0.42 12.61 ?  53  LEU   A HB2  1 
ATOM   1436 H HB2  B LEU   A 1 53  ? 23.283 4.627   6.397   0.58 11.61 ?  53  LEU   A HB2  1 
ATOM   1437 H HB3  A LEU   A 1 53  ? 23.681 4.247   7.960   0.42 12.61 ?  53  LEU   A HB3  1 
ATOM   1438 H HB3  B LEU   A 1 53  ? 23.810 4.461   7.873   0.58 11.61 ?  53  LEU   A HB3  1 
ATOM   1439 H HG   A LEU   A 1 53  ? 21.266 3.360   6.804   0.42 12.85 ?  53  LEU   A HG   1 
ATOM   1440 H HG   B LEU   A 1 53  ? 21.427 3.267   6.977   0.58 12.44 ?  53  LEU   A HG   1 
ATOM   1441 H HD11 A LEU   A 1 53  ? 22.164 1.214   6.846   0.42 13.36 ?  53  LEU   A HD11 1 
ATOM   1442 H HD11 B LEU   A 1 53  ? 22.616 1.265   6.835   0.58 12.96 ?  53  LEU   A HD11 1 
ATOM   1443 H HD12 A LEU   A 1 53  ? 23.025 2.157   5.901   0.42 13.36 ?  53  LEU   A HD12 1 
ATOM   1444 H HD12 B LEU   A 1 53  ? 23.193 2.337   5.814   0.58 12.96 ?  53  LEU   A HD12 1 
ATOM   1445 H HD13 A LEU   A 1 53  ? 23.546 1.806   7.361   0.42 13.36 ?  53  LEU   A HD13 1 
ATOM   1446 H HD13 B LEU   A 1 53  ? 23.956 2.046   7.177   0.58 12.96 ?  53  LEU   A HD13 1 
ATOM   1447 H HD21 A LEU   A 1 53  ? 21.026 2.098   8.783   0.42 12.94 ?  53  LEU   A HD21 1 
ATOM   1448 H HD21 B LEU   A 1 53  ? 21.539 1.968   8.906   0.58 13.37 ?  53  LEU   A HD21 1 
ATOM   1449 H HD22 A LEU   A 1 53  ? 22.303 2.834   9.372   0.42 12.94 ?  53  LEU   A HD22 1 
ATOM   1450 H HD22 B LEU   A 1 53  ? 22.841 2.757   9.361   0.58 13.37 ?  53  LEU   A HD22 1 
ATOM   1451 H HD23 A LEU   A 1 53  ? 20.980 3.658   9.069   0.42 12.94 ?  53  LEU   A HD23 1 
ATOM   1452 H HD23 B LEU   A 1 53  ? 21.443 3.508   9.285   0.58 13.37 ?  53  LEU   A HD23 1 
ATOM   1453 N N    A ASN   A 1 54  ? 23.834 7.422   6.822   0.42 10.42 ?  54  ASN   A N    1 
ATOM   1454 N N    B ASN   A 1 54  ? 23.913 7.422   6.820   0.58 8.79  ?  54  ASN   A N    1 
ATOM   1455 C CA   A ASN   A 1 54  ? 24.906 8.398   6.959   0.42 10.30 ?  54  ASN   A CA   1 
ATOM   1456 C CA   B ASN   A 1 54  ? 24.943 8.442   6.948   0.58 9.01  ?  54  ASN   A CA   1 
ATOM   1457 C C    A ASN   A 1 54  ? 24.420 9.668   7.656   0.42 10.34 ?  54  ASN   A C    1 
ATOM   1458 C C    B ASN   A 1 54  ? 24.413 9.668   7.684   0.58 9.75  ?  54  ASN   A C    1 
ATOM   1459 O O    A ASN   A 1 54  ? 25.138 10.243  8.482   0.42 10.60 ?  54  ASN   A O    1 
ATOM   1460 O O    B ASN   A 1 54  ? 25.083 10.205  8.574   0.58 10.25 ?  54  ASN   A O    1 
ATOM   1461 C CB   A ASN   A 1 54  ? 25.507 8.706   5.594   0.42 10.35 ?  54  ASN   A CB   1 
ATOM   1462 C CB   B ASN   A 1 54  ? 25.496 8.840   5.588   0.58 9.10  ?  54  ASN   A CB   1 
ATOM   1463 C CG   A ASN   A 1 54  ? 26.570 9.766   5.673   0.42 10.92 ?  54  ASN   A CG   1 
ATOM   1464 C CG   B ASN   A 1 54  ? 26.480 9.975   5.709   0.58 9.15  ?  54  ASN   A CG   1 
ATOM   1465 O OD1  A ASN   A 1 54  ? 27.566 9.603   6.381   0.42 10.99 ?  54  ASN   A OD1  1 
ATOM   1466 O OD1  B ASN   A 1 54  ? 27.495 9.841   6.402   0.58 9.13  ?  54  ASN   A OD1  1 
ATOM   1467 N ND2  A ASN   A 1 54  ? 26.368 10.865  4.963   0.42 11.07 ?  54  ASN   A ND2  1 
ATOM   1468 N ND2  B ASN   A 1 54  ? 26.180 11.108  5.083   0.58 9.55  ?  54  ASN   A ND2  1 
ATOM   1469 H H    A ASN   A 1 54  ? 23.560 7.284   6.016   0.42 12.50 ?  54  ASN   A H    1 
ATOM   1470 H H    B ASN   A 1 54  ? 23.728 7.183   6.014   0.58 10.54 ?  54  ASN   A H    1 
ATOM   1471 H HA   A ASN   A 1 54  ? 25.601 8.010   7.507   0.42 12.36 ?  54  ASN   A HA   1 
ATOM   1472 H HA   B ASN   A 1 54  ? 25.670 8.083   7.470   0.58 10.81 ?  54  ASN   A HA   1 
ATOM   1473 H HB2  A ASN   A 1 54  ? 25.909 7.897   5.237   0.42 12.42 ?  54  ASN   A HB2  1 
ATOM   1474 H HB2  B ASN   A 1 54  ? 25.956 8.080   5.198   0.58 10.93 ?  54  ASN   A HB2  1 
ATOM   1475 H HB3  A ASN   A 1 54  ? 24.809 9.022   5.002   0.42 12.42 ?  54  ASN   A HB3  1 
ATOM   1476 H HB3  B ASN   A 1 54  ? 24.769 9.125   5.014   0.58 10.93 ?  54  ASN   A HB3  1 
ATOM   1477 H HD21 A ASN   A 1 54  ? 26.948 11.499  4.979   0.42 13.28 ?  54  ASN   A HD21 1 
ATOM   1478 H HD21 B ASN   A 1 54  ? 26.711 11.784  5.136   0.58 11.46 ?  54  ASN   A HD21 1 
ATOM   1479 H HD22 A ASN   A 1 54  ? 25.659 10.940  4.485   0.42 13.28 ?  54  ASN   A HD22 1 
ATOM   1480 H HD22 B ASN   A 1 54  ? 25.461 11.163  4.616   0.58 11.46 ?  54  ASN   A HD22 1 
ATOM   1481 N N    . LYS   A 1 55  ? 23.204 10.123  7.334   1.00 10.05 ?  55  LYS   A N    1 
ATOM   1482 C CA   . LYS   A 1 55  ? 22.630 11.285  8.007   1.00 11.16 ?  55  LYS   A CA   1 
ATOM   1483 C C    . LYS   A 1 55  ? 22.530 11.046  9.508   1.00 11.03 ?  55  LYS   A C    1 
ATOM   1484 O O    . LYS   A 1 55  ? 22.808 11.942  10.314  1.00 11.59 ?  55  LYS   A O    1 
ATOM   1485 C CB   . LYS   A 1 55  ? 21.261 11.603  7.396   1.00 12.16 ?  55  LYS   A CB   1 
ATOM   1486 C CG   . LYS   A 1 55  ? 20.517 12.765  8.035   1.00 14.38 ?  55  LYS   A CG   1 
ATOM   1487 C CD   . LYS   A 1 55  ? 19.190 13.011  7.311   1.00 16.29 ?  55  LYS   A CD   1 
ATOM   1488 C CE   . LYS   A 1 55  ? 18.330 14.071  7.991   1.00 18.29 ?  55  LYS   A CE   1 
ATOM   1489 N NZ   . LYS   A 1 55  ? 16.986 14.184  7.344   1.00 20.26 ?  55  LYS   A NZ   1 
ATOM   1490 H H    A LYS   A 1 55  ? 22.694 9.774   6.732   0.42 12.06 ?  55  LYS   A H    1 
ATOM   1491 H H    B LYS   A 1 55  ? 22.696 9.767   6.735   0.58 12.06 ?  55  LYS   A H    1 
ATOM   1492 H HA   . LYS   A 1 55  ? 23.210 12.047  7.862   1.00 13.39 ?  55  LYS   A HA   1 
ATOM   1493 H HB2  . LYS   A 1 55  ? 21.388 11.817  6.459   1.00 14.60 ?  55  LYS   A HB2  1 
ATOM   1494 H HB3  . LYS   A 1 55  ? 20.700 10.816  7.477   1.00 14.60 ?  55  LYS   A HB3  1 
ATOM   1495 H HG2  . LYS   A 1 55  ? 20.326 12.556  8.964   1.00 17.26 ?  55  LYS   A HG2  1 
ATOM   1496 H HG3  . LYS   A 1 55  ? 21.059 13.568  7.974   1.00 17.26 ?  55  LYS   A HG3  1 
ATOM   1497 H HD2  . LYS   A 1 55  ? 19.379 13.309  6.405   1.00 19.55 ?  55  LYS   A HD2  1 
ATOM   1498 H HD3  . LYS   A 1 55  ? 18.688 12.181  7.285   1.00 19.55 ?  55  LYS   A HD3  1 
ATOM   1499 H HE2  . LYS   A 1 55  ? 18.202 13.828  8.920   1.00 21.95 ?  55  LYS   A HE2  1 
ATOM   1500 H HE3  . LYS   A 1 55  ? 18.773 14.931  7.926   1.00 21.95 ?  55  LYS   A HE3  1 
ATOM   1501 H HZ1  . LYS   A 1 55  ? 16.420 14.602  7.890   1.00 24.32 ?  55  LYS   A HZ1  1 
ATOM   1502 H HZ2  . LYS   A 1 55  ? 17.048 14.647  6.586   1.00 24.32 ?  55  LYS   A HZ2  1 
ATOM   1503 H HZ3  . LYS   A 1 55  ? 16.663 13.374  7.163   1.00 24.32 ?  55  LYS   A HZ3  1 
ATOM   1504 N N    . ALA   A 1 56  ? 22.138 9.832   9.904   1.00 11.27 ?  56  ALA   A N    1 
ATOM   1505 C CA   . ALA   A 1 56  ? 22.010 9.506   11.318  1.00 11.85 ?  56  ALA   A CA   1 
ATOM   1506 C C    . ALA   A 1 56  ? 23.351 9.538   12.047  1.00 11.93 ?  56  ALA   A C    1 
ATOM   1507 O O    . ALA   A 1 56  ? 23.365 9.728   13.267  1.00 13.12 ?  56  ALA   A O    1 
ATOM   1508 C CB   . ALA   A 1 56  ? 21.311 8.153   11.495  1.00 12.92 ?  56  ALA   A CB   1 
ATOM   1509 H H    . ALA   A 1 56  ? 21.938 9.192   9.373   1.00 13.53 ?  56  ALA   A H    1 
ATOM   1510 H HA   . ALA   A 1 56  ? 21.459 10.172  11.739  1.00 14.22 ?  56  ALA   A HA   1 
ATOM   1511 H HB1  . ALA   A 1 56  ? 21.250 7.952   12.445  1.00 15.50 ?  56  ALA   A HB1  1 
ATOM   1512 H HB2  . ALA   A 1 56  ? 20.422 8.211   11.114  1.00 15.50 ?  56  ALA   A HB2  1 
ATOM   1513 H HB3  . ALA   A 1 56  ? 21.823 7.465   11.045  1.00 15.50 ?  56  ALA   A HB3  1 
ATOM   1514 N N    . THR   A 1 57  ? 24.470 9.352   11.335  1.00 10.60 ?  57  THR   A N    1 
ATOM   1515 C CA   . THR   A 1 57  ? 25.812 9.476   11.913  1.00 10.97 ?  57  THR   A CA   1 
ATOM   1516 C C    . THR   A 1 57  ? 26.361 10.896  11.841  1.00 11.14 ?  57  THR   A C    1 
ATOM   1517 O O    . THR   A 1 57  ? 27.547 11.108  12.130  1.00 12.06 ?  57  THR   A O    1 
ATOM   1518 C CB   . THR   A 1 57  ? 26.827 8.532   11.237  1.00 10.84 ?  57  THR   A CB   1 
ATOM   1519 O OG1  . THR   A 1 57  ? 27.204 9.025   9.940   1.00 10.44 ?  57  THR   A OG1  1 
ATOM   1520 C CG2  . THR   A 1 57  ? 26.295 7.112   11.131  1.00 11.27 ?  57  THR   A CG2  1 
ATOM   1521 H H    . THR   A 1 57  ? 24.483 9.118   10.498  1.00 12.72 ?  57  THR   A H    1 
ATOM   1522 H HA   . THR   A 1 57  ? 25.770 9.219   12.849  1.00 13.16 ?  57  THR   A HA   1 
ATOM   1523 H HB   . THR   A 1 57  ? 27.630 8.491   11.795  1.00 13.01 ?  57  THR   A HB   1 
ATOM   1524 H HG1  . THR   A 1 57  ? 26.522 9.089   9.458   1.00 12.53 ?  57  THR   A HG1  1 
ATOM   1525 H HG21 . THR   A 1 57  ? 26.972 6.528   10.745  1.00 13.52 ?  57  THR   A HG21 1 
ATOM   1526 H HG22 . THR   A 1 57  ? 26.055 6.775   12.006  1.00 13.52 ?  57  THR   A HG22 1 
ATOM   1527 H HG23 . THR   A 1 57  ? 25.512 7.095   10.561  1.00 13.52 ?  57  THR   A HG23 1 
ATOM   1528 N N    . ASN   A 1 58  ? 25.548 11.865  11.425  1.00 11.70 ?  58  ASN   A N    1 
ATOM   1529 C CA   . ASN   A 1 58  ? 26.007 13.246  11.325  1.00 12.79 ?  58  ASN   A CA   1 
ATOM   1530 C C    . ASN   A 1 58  ? 27.155 13.374  10.322  1.00 11.74 ?  58  ASN   A C    1 
ATOM   1531 O O    . ASN   A 1 58  ? 28.049 14.209  10.487  1.00 12.56 ?  58  ASN   A O    1 
ATOM   1532 C CB   . ASN   A 1 58  ? 26.381 13.781  12.720  1.00 15.17 ?  58  ASN   A CB   1 
ATOM   1533 C CG   . ASN   A 1 58  ? 26.773 15.236  12.724  1.00 19.79 ?  58  ASN   A CG   1 
ATOM   1534 O OD1  . ASN   A 1 58  ? 26.128 16.059  12.087  1.00 21.82 ?  58  ASN   A OD1  1 
ATOM   1535 N ND2  . ASN   A 1 58  ? 27.835 15.568  13.469  1.00 21.23 ?  58  ASN   A ND2  1 
ATOM   1536 H H    . ASN   A 1 58  ? 24.727 11.740  11.185  1.00 14.03 ?  58  ASN   A H    1 
ATOM   1537 H HA   . ASN   A 1 58  ? 25.273 13.781  10.998  1.00 15.34 ?  58  ASN   A HA   1 
ATOM   1538 H HB2  . ASN   A 1 58  ? 25.611 13.675  13.314  1.00 18.21 ?  58  ASN   A HB2  1 
ATOM   1539 H HB3  . ASN   A 1 58  ? 27.127 13.277  13.071  1.00 18.21 ?  58  ASN   A HB3  1 
ATOM   1540 H HD21 . ASN   A 1 58  ? 28.094 16.389  13.510  1.00 25.47 ?  58  ASN   A HD21 1 
ATOM   1541 H HD22 . ASN   A 1 58  ? 28.255 14.962  13.906  1.00 25.47 ?  58  ASN   A HD22 1 
ATOM   1542 N N    . ASN   A 1 59  ? 27.138 12.555  9.268   1.00 10.72 ?  59  ASN   A N    1 
ATOM   1543 C CA   . ASN   A 1 59  ? 28.119 12.529  8.178   1.00 10.26 ?  59  ASN   A CA   1 
ATOM   1544 C C    . ASN   A 1 59  ? 29.436 11.850  8.567   1.00 10.26 ?  59  ASN   A C    1 
ATOM   1545 O O    . ASN   A 1 59  ? 30.350 11.808  7.741   1.00 10.58 ?  59  ASN   A O    1 
ATOM   1546 C CB   . ASN   A 1 59  ? 28.414 13.918  7.575   1.00 10.80 ?  59  ASN   A CB   1 
ATOM   1547 C CG   . ASN   A 1 59  ? 28.785 13.850  6.104   1.00 10.85 ?  59  ASN   A CG   1 
ATOM   1548 O OD1  . ASN   A 1 59  ? 28.083 13.231  5.303   1.00 11.27 ?  59  ASN   A OD1  1 
ATOM   1549 N ND2  . ASN   A 1 59  ? 29.874 14.511  5.730   1.00 12.02 ?  59  ASN   A ND2  1 
ATOM   1550 H H    . ASN   A 1 59  ? 26.520 11.960  9.154   1.00 12.86 ?  59  ASN   A H    1 
ATOM   1551 H HA   . ASN   A 1 59  ? 27.737 12.002  7.462   1.00 12.31 ?  59  ASN   A HA   1 
ATOM   1552 H HB2  . ASN   A 1 59  ? 27.630 14.480  7.653   1.00 12.96 ?  59  ASN   A HB2  1 
ATOM   1553 H HB3  . ASN   A 1 59  ? 29.162 14.320  8.044   1.00 12.96 ?  59  ASN   A HB3  1 
ATOM   1554 H HD21 . ASN   A 1 59  ? 30.119 14.506  4.905   1.00 14.43 ?  59  ASN   A HD21 1 
ATOM   1555 H HD22 . ASN   A 1 59  ? 30.341 14.942  6.312   1.00 14.43 ?  59  ASN   A HD22 1 
ATOM   1556 N N    . ALA   A 1 60  ? 29.558 11.302  9.775   1.00 10.32 ?  60  ALA   A N    1 
ATOM   1557 C CA   . ALA   A 1 60  ? 30.798 10.623  10.136  1.00 10.28 ?  60  ALA   A CA   1 
ATOM   1558 C C    . ALA   A 1 60  ? 31.026 9.386   9.279   1.00 10.46 ?  60  ALA   A C    1 
ATOM   1559 O O    . ALA   A 1 60  ? 32.170 9.063   8.949   1.00 11.06 ?  60  ALA   A O    1 
ATOM   1560 C CB   . ALA   A 1 60  ? 30.795 10.257  11.620  1.00 11.58 ?  60  ALA   A CB   1 
ATOM   1561 H H    . ALA   A 1 60  ? 28.953 11.301  10.387  1.00 12.38 ?  60  ALA   A H    1 
ATOM   1562 H HA   . ALA   A 1 60  ? 31.539 11.229  9.980   1.00 12.34 ?  60  ALA   A HA   1 
ATOM   1563 H HB1  . ALA   A 1 60  ? 31.627 9.813   11.839  1.00 13.90 ?  60  ALA   A HB1  1 
ATOM   1564 H HB2  . ALA   A 1 60  ? 30.707 11.072  12.144  1.00 13.90 ?  60  ALA   A HB2  1 
ATOM   1565 H HB3  . ALA   A 1 60  ? 30.045 9.670   11.799  1.00 13.90 ?  60  ALA   A HB3  1 
ATOM   1566 N N    . MET   A 1 61  ? 29.955 8.688   8.899   1.00 9.77  ?  61  MET   A N    1 
ATOM   1567 C CA   . MET   A 1 61  ? 30.097 7.552   7.996   1.00 9.72  ?  61  MET   A CA   1 
ATOM   1568 C C    . MET   A 1 61  ? 30.723 7.971   6.665   1.00 9.85  ?  61  MET   A C    1 
ATOM   1569 O O    . MET   A 1 61  ? 31.617 7.292   6.148   1.00 10.13 ?  61  MET   A O    1 
ATOM   1570 C CB   . MET   A 1 61  ? 28.736 6.877   7.794   1.00 10.00 ?  61  MET   A CB   1 
ATOM   1571 C CG   . MET   A 1 61  ? 28.737 5.718   6.807   1.00 10.58 ?  61  MET   A CG   1 
ATOM   1572 S SD   . MET   A 1 61  ? 27.118 4.960   6.602   1.00 11.27 ?  61  MET   A SD   1 
ATOM   1573 C CE   . MET   A 1 61  ? 26.998 4.091   8.163   1.00 12.97 ?  61  MET   A CE   1 
ATOM   1574 H H    . MET   A 1 61  ? 29.146 8.852   9.141   1.00 11.73 ?  61  MET   A H    1 
ATOM   1575 H HA   . MET   A 1 61  ? 30.683 6.900   8.415   1.00 11.66 ?  61  MET   A HA   1 
ATOM   1576 H HB2  . MET   A 1 61  ? 28.433 6.539   8.649   1.00 12.00 ?  61  MET   A HB2  1 
ATOM   1577 H HB3  . MET   A 1 61  ? 28.109 7.541   7.466   1.00 12.00 ?  61  MET   A HB3  1 
ATOM   1578 H HG2  . MET   A 1 61  ? 29.018 6.034   5.938   1.00 12.70 ?  61  MET   A HG2  1 
ATOM   1579 H HG3  . MET   A 1 61  ? 29.342 5.031   7.126   1.00 12.70 ?  61  MET   A HG3  1 
ATOM   1580 H HE1  . MET   A 1 61  ? 26.163 3.595   8.183   1.00 15.56 ?  61  MET   A HE1  1 
ATOM   1581 H HE2  . MET   A 1 61  ? 27.746 3.485   8.247   1.00 15.56 ?  61  MET   A HE2  1 
ATOM   1582 H HE3  . MET   A 1 61  ? 27.010 4.737   8.891   1.00 15.56 ?  61  MET   A HE3  1 
ATOM   1583 N N    . GLN   A 1 62  ? 30.286 9.099   6.103   1.00 9.73  ?  62  GLN   A N    1 
ATOM   1584 C CA   . GLN   A 1 62  ? 30.857 9.565   4.843   1.00 10.24 ?  62  GLN   A CA   1 
ATOM   1585 C C    . GLN   A 1 62  ? 32.325 9.945   4.994   1.00 10.18 ?  62  GLN   A C    1 
ATOM   1586 O O    . GLN   A 1 62  ? 33.136 9.633   4.119   1.00 10.55 ?  62  GLN   A O    1 
ATOM   1587 C CB   . GLN   A 1 62  ? 30.065 10.747  4.295   1.00 10.35 ?  62  GLN   A CB   1 
ATOM   1588 C CG   . GLN   A 1 62  ? 30.448 11.106  2.869   1.00 10.53 ?  62  GLN   A CG   1 
ATOM   1589 C CD   . GLN   A 1 62  ? 30.110 9.972   1.924   1.00 10.52 ?  62  GLN   A CD   1 
ATOM   1590 O OE1  . GLN   A 1 62  ? 28.931 9.672   1.707   1.00 11.00 ?  62  GLN   A OE1  1 
ATOM   1591 N NE2  . GLN   A 1 62  ? 31.128 9.287   1.412   1.00 10.88 ?  62  GLN   A NE2  1 
ATOM   1592 H H    . GLN   A 1 62  ? 29.665 9.598   6.428   1.00 11.67 ?  62  GLN   A H    1 
ATOM   1593 H HA   . GLN   A 1 62  ? 30.805 8.841   4.200   1.00 12.29 ?  62  GLN   A HA   1 
ATOM   1594 H HB2  . GLN   A 1 62  ? 29.123 10.532  4.312   1.00 12.42 ?  62  GLN   A HB2  1 
ATOM   1595 H HB3  . GLN   A 1 62  ? 30.239 11.525  4.853   1.00 12.42 ?  62  GLN   A HB3  1 
ATOM   1596 H HG2  . GLN   A 1 62  ? 29.942 11.885  2.591   1.00 12.64 ?  62  GLN   A HG2  1 
ATOM   1597 H HG3  . GLN   A 1 62  ? 31.397 11.278  2.818   1.00 12.64 ?  62  GLN   A HG3  1 
ATOM   1598 H HE21 . GLN   A 1 62  ? 31.938 9.514   1.600   1.00 13.05 ?  62  GLN   A HE21 1 
ATOM   1599 H HE22 . GLN   A 1 62  ? 30.984 8.626   0.881   1.00 13.05 ?  62  GLN   A HE22 1 
ATOM   1600 N N    . VAL   A 1 63  ? 32.681 10.630  6.084   1.00 10.66 ?  63  VAL   A N    1 
ATOM   1601 C CA   . VAL   A 1 63  ? 34.074 11.023  6.296   1.00 11.32 ?  63  VAL   A CA   1 
ATOM   1602 C C    . VAL   A 1 63  ? 34.969 9.788   6.367   1.00 10.50 ?  63  VAL   A C    1 
ATOM   1603 O O    . VAL   A 1 63  ? 36.018 9.712   5.715   1.00 11.04 ?  63  VAL   A O    1 
ATOM   1604 C CB   . VAL   A 1 63  ? 34.181 11.901  7.557   1.00 13.13 ?  63  VAL   A CB   1 
ATOM   1605 C CG1  . VAL   A 1 63  ? 35.628 12.162  7.914   1.00 15.33 ?  63  VAL   A CG1  1 
ATOM   1606 C CG2  . VAL   A 1 63  ? 33.450 13.231  7.340   1.00 13.54 ?  63  VAL   A CG2  1 
ATOM   1607 H H    . VAL   A 1 63  ? 32.136 10.878  6.705   1.00 12.79 ?  63  VAL   A H    1 
ATOM   1608 H HA   . VAL   A 1 63  ? 34.364 11.559  5.544   1.00 13.58 ?  63  VAL   A HA   1 
ATOM   1609 H HB   . VAL   A 1 63  ? 33.763 11.448  8.305   1.00 15.76 ?  63  VAL   A HB   1 
ATOM   1610 H HG11 . VAL   A 1 63  ? 35.667 12.896  8.548   1.00 18.40 ?  63  VAL   A HG11 1 
ATOM   1611 H HG12 . VAL   A 1 63  ? 36.006 11.364  8.308   1.00 18.40 ?  63  VAL   A HG12 1 
ATOM   1612 H HG13 . VAL   A 1 63  ? 36.111 12.400  7.107   1.00 18.40 ?  63  VAL   A HG13 1 
ATOM   1613 H HG21 . VAL   A 1 63  ? 33.536 13.774  8.142   1.00 16.25 ?  63  VAL   A HG21 1 
ATOM   1614 H HG22 . VAL   A 1 63  ? 33.853 13.693  6.587   1.00 16.25 ?  63  VAL   A HG22 1 
ATOM   1615 H HG23 . VAL   A 1 63  ? 32.516 13.053  7.160   1.00 16.25 ?  63  VAL   A HG23 1 
ATOM   1616 N N    . GLU   A 1 64  ? 34.544 8.785   7.139   1.00 10.66 ?  64  GLU   A N    1 
ATOM   1617 C CA   . GLU   A 1 64  ? 35.304 7.546   7.237   1.00 10.55 ?  64  GLU   A CA   1 
ATOM   1618 C C    . GLU   A 1 64  ? 35.389 6.853   5.885   1.00 10.42 ?  64  GLU   A C    1 
ATOM   1619 O O    . GLU   A 1 64  ? 36.439 6.311   5.508   1.00 11.04 ?  64  GLU   A O    1 
ATOM   1620 C CB   . GLU   A 1 64  ? 34.615 6.640   8.260   1.00 11.23 ?  64  GLU   A CB   1 
ATOM   1621 C CG   . GLU   A 1 64  ? 35.256 5.278   8.401   1.00 12.12 ?  64  GLU   A CG   1 
ATOM   1622 C CD   . GLU   A 1 64  ? 34.385 4.286   9.141   1.00 12.85 ?  64  GLU   A CD   1 
ATOM   1623 O OE1  . GLU   A 1 64  ? 33.149 4.378   9.015   1.00 13.26 ?  64  GLU   A OE1  1 
ATOM   1624 O OE2  . GLU   A 1 64  ? 34.943 3.394   9.822   1.00 12.78 -1 64  GLU   A OE2  1 
ATOM   1625 H H    . GLU   A 1 64  ? 33.809 8.795   7.594   1.00 12.79 ?  64  GLU   A H    1 
ATOM   1626 H HA   . GLU   A 1 64  ? 36.199 7.748   7.550   1.00 12.66 ?  64  GLU   A HA   1 
ATOM   1627 H HB2  . GLU   A 1 64  ? 34.648 7.074   9.133   1.00 13.48 ?  64  GLU   A HB2  1 
ATOM   1628 H HB3  . GLU   A 1 64  ? 33.693 6.515   7.994   1.00 13.48 ?  64  GLU   A HB3  1 
ATOM   1629 H HG2  . GLU   A 1 64  ? 35.439 4.911   7.519   1.00 14.54 ?  64  GLU   A HG2  1 
ATOM   1630 H HG3  . GLU   A 1 64  ? 36.086 5.372   8.892   1.00 14.54 ?  64  GLU   A HG3  1 
ATOM   1631 N N    . SER   A 1 65  ? 34.271 6.844   5.152   1.00 10.27 ?  65  SER   A N    1 
ATOM   1632 C CA   . SER   A 1 65  ? 34.222 6.179   3.855   1.00 10.29 ?  65  SER   A CA   1 
ATOM   1633 C C    . SER   A 1 65  ? 35.148 6.841   2.844   1.00 10.19 ?  65  SER   A C    1 
ATOM   1634 O O    . SER   A 1 65  ? 35.787 6.158   2.039   1.00 10.97 ?  65  SER   A O    1 
ATOM   1635 C CB   . SER   A 1 65  ? 32.788 6.181   3.317   1.00 10.35 ?  65  SER   A CB   1 
ATOM   1636 O OG   . SER   A 1 65  ? 31.928 5.372   4.105   1.00 10.64 ?  65  SER   A OG   1 
ATOM   1637 H H    . SER   A 1 65  ? 33.535 7.224   5.385   1.00 12.33 ?  65  SER   A H    1 
ATOM   1638 H HA   . SER   A 1 65  ? 34.506 5.262   3.961   1.00 12.35 ?  65  SER   A HA   1 
ATOM   1639 H HB2  . SER   A 1 65  ? 32.452 7.090   3.323   1.00 12.42 ?  65  SER   A HB2  1 
ATOM   1640 H HB3  . SER   A 1 65  ? 32.798 5.838   2.411   1.00 12.42 ?  65  SER   A HB3  1 
ATOM   1641 H HG   . SER   A 1 65  ? 31.916 5.655   4.900   1.00 12.77 ?  65  SER   A HG   1 
ATOM   1642 N N    . ASP   A 1 66  ? 35.223 8.171   2.852   1.00 10.30 ?  66  ASP   A N    1 
ATOM   1643 C CA   . ASP   A 1 66  ? 36.090 8.857   1.899   1.00 11.10 ?  66  ASP   A CA   1 
ATOM   1644 C C    . ASP   A 1 66  ? 37.552 8.508   2.152   1.00 11.15 ?  66  ASP   A C    1 
ATOM   1645 O O    . ASP   A 1 66  ? 38.334 8.336   1.209   1.00 12.21 ?  66  ASP   A O    1 
ATOM   1646 C CB   . ASP   A 1 66  ? 35.882 10.366  1.982   1.00 12.71 ?  66  ASP   A CB   1 
ATOM   1647 C CG   . ASP   A 1 66  ? 34.550 10.834  1.376   1.00 14.50 ?  66  ASP   A CG   1 
ATOM   1648 O OD1  . ASP   A 1 66  ? 33.843 10.029  0.731   1.00 14.95 ?  66  ASP   A OD1  1 
ATOM   1649 O OD2  . ASP   A 1 66  ? 34.251 12.041  1.518   1.00 17.57 -1 66  ASP   A OD2  1 
ATOM   1650 H H    . ASP   A 1 66  ? 34.782 8.697   3.379   1.00 12.36 ?  66  ASP   A H    1 
ATOM   1651 H HA   . ASP   A 1 66  ? 35.860 8.570   0.998   1.00 13.32 ?  66  ASP   A HA   1 
ATOM   1652 H HB2  . ASP   A 1 66  ? 35.892 10.637  2.909   1.00 15.25 ?  66  ASP   A HB2  1 
ATOM   1653 H HB3  . ASP   A 1 66  ? 36.601 10.809  1.498   1.00 15.25 ?  66  ASP   A HB3  1 
ATOM   1654 N N    . ASP   A 1 67  ? 37.939 8.399   3.421   1.00 11.30 ?  67  ASP   A N    1 
ATOM   1655 C CA   . ASP   A 1 67  ? 39.291 7.951   3.737   1.00 12.55 ?  67  ASP   A CA   1 
ATOM   1656 C C    . ASP   A 1 67  ? 39.521 6.515   3.271   1.00 12.01 ?  67  ASP   A C    1 
ATOM   1657 O O    . ASP   A 1 67  ? 40.590 6.191   2.740   1.00 12.93 ?  67  ASP   A O    1 
ATOM   1658 C CB   . ASP   A 1 67  ? 39.556 8.101   5.236   1.00 13.56 ?  67  ASP   A CB   1 
ATOM   1659 C CG   . ASP   A 1 67  ? 40.853 7.445   5.666   1.00 15.04 ?  67  ASP   A CG   1 
ATOM   1660 O OD1  . ASP   A 1 67  ? 41.922 8.081   5.534   1.00 18.09 ?  67  ASP   A OD1  1 
ATOM   1661 O OD2  . ASP   A 1 67  ? 40.804 6.285   6.122   1.00 14.61 -1 67  ASP   A OD2  1 
ATOM   1662 H H    . ASP   A 1 67  ? 37.448 8.576   4.102   1.00 13.56 ?  67  ASP   A H    1 
ATOM   1663 H HA   . ASP   A 1 67  ? 39.926 8.521   3.269   1.00 15.06 ?  67  ASP   A HA   1 
ATOM   1664 H HB2  . ASP   A 1 67  ? 39.612 9.044   5.453   1.00 16.27 ?  67  ASP   A HB2  1 
ATOM   1665 H HB3  . ASP   A 1 67  ? 38.827 7.689   5.726   1.00 16.27 ?  67  ASP   A HB3  1 
ATOM   1666 N N    . TYR   A 1 68  ? 38.529 5.636   3.457   1.00 12.01 ?  68  TYR   A N    1 
ATOM   1667 C CA   . TYR   A 1 68  ? 38.659 4.255   2.992   1.00 11.78 ?  68  TYR   A CA   1 
ATOM   1668 C C    . TYR   A 1 68  ? 38.908 4.206   1.486   1.00 12.03 ?  68  TYR   A C    1 
ATOM   1669 O O    . TYR   A 1 68  ? 39.796 3.479   1.017   1.00 12.63 ?  68  TYR   A O    1 
ATOM   1670 C CB   . TYR   A 1 68  ? 37.410 3.430   3.365   1.00 12.39 ?  68  TYR   A CB   1 
ATOM   1671 C CG   . TYR   A 1 68  ? 37.435 2.043   2.730   1.00 13.60 ?  68  TYR   A CG   1 
ATOM   1672 C CD1  . TYR   A 1 68  ? 36.986 1.853   1.429   1.00 14.49 ?  68  TYR   A CD1  1 
ATOM   1673 C CD2  . TYR   A 1 68  ? 37.970 0.957   3.397   1.00 15.04 ?  68  TYR   A CD2  1 
ATOM   1674 C CE1  . TYR   A 1 68  ? 37.059 0.635   0.809   1.00 16.07 ?  68  TYR   A CE1  1 
ATOM   1675 C CE2  . TYR   A 1 68  ? 38.039 -0.297  2.777   1.00 15.61 ?  68  TYR   A CE2  1 
ATOM   1676 C CZ   . TYR   A 1 68  ? 37.584 -0.430  1.486   1.00 16.43 ?  68  TYR   A CZ   1 
ATOM   1677 O OH   . TYR   A 1 68  ? 37.664 -1.641  0.850   1.00 17.93 ?  68  TYR   A OH   1 
ATOM   1678 H H    . TYR   A 1 68  ? 37.780 5.818   3.845   1.00 14.41 ?  68  TYR   A H    1 
ATOM   1679 H HA   . TYR   A 1 68  ? 39.418 3.851   3.434   1.00 14.13 ?  68  TYR   A HA   1 
ATOM   1680 H HB2  . TYR   A 1 68  ? 37.373 3.319   4.328   1.00 14.87 ?  68  TYR   A HB2  1 
ATOM   1681 H HB3  . TYR   A 1 68  ? 36.614 3.893   3.053   1.00 14.87 ?  68  TYR   A HB3  1 
ATOM   1682 H HD1  . TYR   A 1 68  ? 36.639 2.582   0.959   1.00 17.39 ?  68  TYR   A HD1  1 
ATOM   1683 H HD2  . TYR   A 1 68  ? 38.297 1.058   4.256   1.00 18.05 ?  68  TYR   A HD2  1 
ATOM   1684 H HE1  . TYR   A 1 68  ? 36.746 0.536   -0.065  1.00 19.28 ?  68  TYR   A HE1  1 
ATOM   1685 H HE2  . TYR   A 1 68  ? 38.406 -1.028  3.216   1.00 18.73 ?  68  TYR   A HE2  1 
ATOM   1686 H HH   . TYR   A 1 68  ? 37.999 -2.217  1.365   1.00 21.52 ?  68  TYR   A HH   1 
ATOM   1687 N N    . ILE   A 1 69  ? 38.123 4.963   0.711   1.00 11.46 ?  69  ILE   A N    1 
ATOM   1688 C CA   . ILE   A 1 69  ? 38.259 4.946   -0.744  1.00 11.59 ?  69  ILE   A CA   1 
ATOM   1689 C C    . ILE   A 1 69  ? 39.590 5.557   -1.173  1.00 11.47 ?  69  ILE   A C    1 
ATOM   1690 O O    . ILE   A 1 69  ? 40.236 5.072   -2.109  1.00 11.73 ?  69  ILE   A O    1 
ATOM   1691 C CB   . ILE   A 1 69  ? 37.058 5.654   -1.407  1.00 12.37 ?  69  ILE   A CB   1 
ATOM   1692 C CG1  . ILE   A 1 69  ? 35.747 4.912   -1.130  1.00 12.98 ?  69  ILE   A CG1  1 
ATOM   1693 C CG2  . ILE   A 1 69  ? 37.307 5.831   -2.910  1.00 14.11 ?  69  ILE   A CG2  1 
ATOM   1694 C CD1  . ILE   A 1 69  ? 35.593 3.620   -1.896  1.00 13.92 ?  69  ILE   A CD1  1 
ATOM   1695 H H    . ILE   A 1 69  ? 37.504 5.485   1.003   1.00 13.75 ?  69  ILE   A H    1 
ATOM   1696 H HA   . ILE   A 1 69  ? 38.254 4.024   -1.041  1.00 13.91 ?  69  ILE   A HA   1 
ATOM   1697 H HB   . ILE   A 1 69  ? 36.984 6.536   -1.018  1.00 14.85 ?  69  ILE   A HB   1 
ATOM   1698 H HG12 . ILE   A 1 69  ? 35.709 4.702   -0.182  1.00 15.58 ?  69  ILE   A HG12 1 
ATOM   1699 H HG13 . ILE   A 1 69  ? 35.011 5.493   -1.365  1.00 15.58 ?  69  ILE   A HG13 1 
ATOM   1700 H HG21 . ILE   A 1 69  ? 36.462 6.022   -3.348  1.00 16.94 ?  69  ILE   A HG21 1 
ATOM   1701 H HG22 . ILE   A 1 69  ? 37.919 6.574   -3.045  1.00 16.94 ?  69  ILE   A HG22 1 
ATOM   1702 H HG23 . ILE   A 1 69  ? 37.688 5.017   -3.269  1.00 16.94 ?  69  ILE   A HG23 1 
ATOM   1703 H HD11 . ILE   A 1 69  ? 34.801 3.166   -1.580  1.00 16.71 ?  69  ILE   A HD11 1 
ATOM   1704 H HD12 . ILE   A 1 69  ? 35.505 3.825   -2.841  1.00 16.71 ?  69  ILE   A HD12 1 
ATOM   1705 H HD13 . ILE   A 1 69  ? 36.376 3.068   -1.748  1.00 16.71 ?  69  ILE   A HD13 1 
ATOM   1706 N N    . ALA   A 1 70  ? 40.008 6.637   -0.513  1.00 12.01 ?  70  ALA   A N    1 
ATOM   1707 C CA   . ALA   A 1 70  ? 41.281 7.258   -0.862  1.00 12.86 ?  70  ALA   A CA   1 
ATOM   1708 C C    . ALA   A 1 70  ? 42.439 6.283   -0.690  1.00 13.10 ?  70  ALA   A C    1 
ATOM   1709 O O    . ALA   A 1 70  ? 43.416 6.338   -1.442  1.00 15.48 ?  70  ALA   A O    1 
ATOM   1710 C CB   . ALA   A 1 70  ? 41.505 8.514   -0.016  1.00 13.80 ?  70  ALA   A CB   1 
ATOM   1711 H H    . ALA   A 1 70  ? 39.577 7.024   0.117   1.00 14.41 ?  70  ALA   A H    1 
ATOM   1712 H HA   . ALA   A 1 70  ? 41.255 7.531   -1.794  1.00 15.43 ?  70  ALA   A HA   1 
ATOM   1713 H HB1  . ALA   A 1 70  ? 42.359 8.908   -0.258  1.00 16.56 ?  70  ALA   A HB1  1 
ATOM   1714 H HB2  . ALA   A 1 70  ? 40.789 9.143   -0.185  1.00 16.56 ?  70  ALA   A HB2  1 
ATOM   1715 H HB3  . ALA   A 1 70  ? 41.513 8.263   0.922   1.00 16.56 ?  70  ALA   A HB3  1 
ATOM   1716 N N    . THR   A 1 71  ? 42.333 5.367   0.268   1.00 12.55 ?  71  THR   A N    1 
ATOM   1717 C CA   . THR   A 1 71  ? 43.386 4.394   0.523   1.00 14.46 ?  71  THR   A CA   1 
ATOM   1718 C C    . THR   A 1 71  ? 43.267 3.163   -0.361  1.00 14.55 ?  71  THR   A C    1 
ATOM   1719 O O    . THR   A 1 71  ? 44.281 2.653   -0.855  1.00 17.08 ?  71  THR   A O    1 
ATOM   1720 C CB   . THR   A 1 71  ? 43.323 3.953   1.986   1.00 16.68 ?  71  THR   A CB   1 
ATOM   1721 O OG1  . THR   A 1 71  ? 43.547 5.086   2.831   1.00 18.30 ?  71  THR   A OG1  1 
ATOM   1722 C CG2  . THR   A 1 71  ? 44.348 2.862   2.282   1.00 18.56 ?  71  THR   A CG2  1 
ATOM   1723 H H    . THR   A 1 71  ? 41.644 5.275   0.776   1.00 15.06 ?  71  THR   A H    1 
ATOM   1724 H HA   . THR   A 1 71  ? 44.245 4.797   0.351   1.00 17.35 ?  71  THR   A HA   1 
ATOM   1725 H HB   . THR   A 1 71  ? 42.441 3.589   2.166   1.00 20.01 ?  71  THR   A HB   1 
ATOM   1726 H HG1  . THR   A 1 71  ? 42.958 5.664   2.684   1.00 21.96 ?  71  THR   A HG1  1 
ATOM   1727 H HG21 . THR   A 1 71  ? 44.471 2.783   3.241   1.00 22.27 ?  71  THR   A HG21 1 
ATOM   1728 H HG22 . THR   A 1 71  ? 44.047 2.009   1.933   1.00 22.27 ?  71  THR   A HG22 1 
ATOM   1729 H HG23 . THR   A 1 71  ? 45.200 3.088   1.875   1.00 22.27 ?  71  THR   A HG23 1 
ATOM   1730 N N    . ASN   A 1 72  ? 42.042 2.659   -0.554  1.00 12.79 ?  72  ASN   A N    1 
ATOM   1731 C CA   . ASN   A 1 72  ? 41.825 1.329   -1.119  1.00 13.48 ?  72  ASN   A CA   1 
ATOM   1732 C C    . ASN   A 1 72  ? 41.207 1.317   -2.506  1.00 13.79 ?  72  ASN   A C    1 
ATOM   1733 O O    . ASN   A 1 72  ? 41.217 0.262   -3.157  1.00 14.87 ?  72  ASN   A O    1 
ATOM   1734 C CB   . ASN   A 1 72  ? 40.944 0.501   -0.175  1.00 14.31 ?  72  ASN   A CB   1 
ATOM   1735 C CG   . ASN   A 1 72  ? 41.565 0.354   1.188   1.00 15.60 ?  72  ASN   A CG   1 
ATOM   1736 O OD1  . ASN   A 1 72  ? 41.119 0.960   2.163   1.00 17.73 ?  72  ASN   A OD1  1 
ATOM   1737 N ND2  . ASN   A 1 72  ? 42.621 -0.427  1.260   1.00 16.06 ?  72  ASN   A ND2  1 
ATOM   1738 H H    . ASN   A 1 72  ? 41.306 3.067   -0.357  1.00 15.35 ?  72  ASN   A H    1 
ATOM   1739 H HA   . ASN   A 1 72  ? 42.679 0.880   -1.185  1.00 16.18 ?  72  ASN   A HA   1 
ATOM   1740 H HB2  . ASN   A 1 72  ? 40.084 0.934   -0.071  1.00 17.17 ?  72  ASN   A HB2  1 
ATOM   1741 H HB3  . ASN   A 1 72  ? 40.825 -0.391  -0.547  1.00 17.17 ?  72  ASN   A HB3  1 
ATOM   1742 H HD21 . ASN   A 1 72  ? 43.021 -0.544  2.014   1.00 19.27 ?  72  ASN   A HD21 1 
ATOM   1743 H HD22 . ASN   A 1 72  ? 42.912 -0.827  0.556   1.00 19.27 ?  72  ASN   A HD22 1 
ATOM   1744 N N    . GLY   A 1 73  ? 40.655 2.428   -2.968  1.00 13.02 ?  73  GLY   A N    1 
ATOM   1745 C CA   . GLY   A 1 73  ? 39.920 2.445   -4.208  1.00 12.85 ?  73  GLY   A CA   1 
ATOM   1746 C C    . GLY   A 1 73  ? 38.530 1.861   -4.043  1.00 12.25 ?  73  GLY   A C    1 
ATOM   1747 O O    . GLY   A 1 73  ? 38.140 1.414   -2.957  1.00 12.52 ?  73  GLY   A O    1 
ATOM   1748 H H    . GLY   A 1 73  ? 40.701 3.203   -2.579  1.00 15.63 ?  73  GLY   A H    1 
ATOM   1749 H HA2  . GLY   A 1 73  ? 39.840 3.363   -4.523  1.00 15.42 ?  73  GLY   A HA2  1 
ATOM   1750 H HA3  . GLY   A 1 73  ? 40.400 1.933   -4.876  1.00 15.42 ?  73  GLY   A HA3  1 
ATOM   1751 N N    . PRO   A 1 74  ? 37.755 1.863   -5.126  1.00 12.93 ?  74  PRO   A N    1 
ATOM   1752 C CA   . PRO   A 1 74  ? 36.354 1.433   -5.039  1.00 12.80 ?  74  PRO   A CA   1 
ATOM   1753 C C    . PRO   A 1 74  ? 36.203 -0.049  -4.721  1.00 11.78 ?  74  PRO   A C    1 
ATOM   1754 O O    . PRO   A 1 74  ? 37.078 -0.877  -5.006  1.00 13.16 ?  74  PRO   A O    1 
ATOM   1755 C CB   . PRO   A 1 74  ? 35.807 1.740   -6.438  1.00 14.88 ?  74  PRO   A CB   1 
ATOM   1756 C CG   . PRO   A 1 74  ? 36.750 2.739   -7.030  1.00 17.35 ?  74  PRO   A CG   1 
ATOM   1757 C CD   . PRO   A 1 74  ? 38.089 2.397   -6.457  1.00 14.42 ?  74  PRO   A CD   1 
ATOM   1758 H HA   . PRO   A 1 74  ? 35.878 1.961   -4.375  1.00 15.37 ?  74  PRO   A HA   1 
ATOM   1759 H HB2  . PRO   A 1 74  ? 35.787 0.929   -6.963  1.00 17.86 ?  74  PRO   A HB2  1 
ATOM   1760 H HB3  . PRO   A 1 74  ? 34.914 2.120   -6.358  1.00 17.86 ?  74  PRO   A HB3  1 
ATOM   1761 H HG2  . PRO   A 1 74  ? 36.759 2.651   -7.995  1.00 20.82 ?  74  PRO   A HG2  1 
ATOM   1762 H HG3  . PRO   A 1 74  ? 36.488 3.636   -6.769  1.00 20.82 ?  74  PRO   A HG3  1 
ATOM   1763 H HD2  . PRO   A 1 74  ? 38.530 1.717   -6.994  1.00 17.30 ?  74  PRO   A HD2  1 
ATOM   1764 H HD3  . PRO   A 1 74  ? 38.639 3.197   -6.384  1.00 17.30 ?  74  PRO   A HD3  1 
ATOM   1765 N N    . LEU   A 1 75  ? 35.063 -0.377  -4.121  1.00 11.33 ?  75  LEU   A N    1 
ATOM   1766 C CA   . LEU   A 1 75  ? 34.679 -1.769  -3.964  1.00 10.83 ?  75  LEU   A CA   1 
ATOM   1767 C C    . LEU   A 1 75  ? 34.313 -2.369  -5.320  1.00 11.32 ?  75  LEU   A C    1 
ATOM   1768 O O    . LEU   A 1 75  ? 34.132 -1.665  -6.316  1.00 12.65 ?  75  LEU   A O    1 
ATOM   1769 C CB   . LEU   A 1 75  ? 33.484 -1.900  -3.023  1.00 10.86 ?  75  LEU   A CB   1 
ATOM   1770 C CG   . LEU   A 1 75  ? 33.682 -1.464  -1.574  1.00 12.83 ?  75  LEU   A CG   1 
ATOM   1771 C CD1  . LEU   A 1 75  ? 32.387 -1.657  -0.794  1.00 14.49 ?  75  LEU   A CD1  1 
ATOM   1772 C CD2  . LEU   A 1 75  ? 34.812 -2.181  -0.894  1.00 16.81 ?  75  LEU   A CD2  1 
ATOM   1773 H H    . LEU   A 1 75  ? 34.493 0.191   -3.805  1.00 13.60 ?  75  LEU   A H    1 
ATOM   1774 H HA   . LEU   A 1 75  ? 35.428 -2.263  -3.598  1.00 13.00 ?  75  LEU   A HA   1 
ATOM   1775 H HB2  . LEU   A 1 75  ? 32.757 -1.374  -3.385  1.00 13.03 ?  75  LEU   A HB2  1 
ATOM   1776 H HB3  . LEU   A 1 75  ? 33.225 -2.836  -3.006  1.00 13.03 ?  75  LEU   A HB3  1 
ATOM   1777 H HG   . LEU   A 1 75  ? 33.897 -0.515  -1.565  1.00 15.40 ?  75  LEU   A HG   1 
ATOM   1778 H HD11 . LEU   A 1 75  ? 32.529 -1.368  0.121   1.00 17.39 ?  75  LEU   A HD11 1 
ATOM   1779 H HD12 . LEU   A 1 75  ? 31.695 -1.116  -1.208  1.00 17.39 ?  75  LEU   A HD12 1 
ATOM   1780 H HD13 . LEU   A 1 75  ? 32.144 -2.590  -0.818  1.00 17.39 ?  75  LEU   A HD13 1 
ATOM   1781 H HD21 . LEU   A 1 75  ? 34.853 -1.898  0.033   1.00 20.17 ?  75  LEU   A HD21 1 
ATOM   1782 H HD22 . LEU   A 1 75  ? 34.654 -3.136  -0.943  1.00 20.17 ?  75  LEU   A HD22 1 
ATOM   1783 H HD23 . LEU   A 1 75  ? 35.646 -1.960  -1.342  1.00 20.17 ?  75  LEU   A HD23 1 
ATOM   1784 N N    . LYS   A 1 76  ? 34.198 -3.695  -5.342  1.00 11.70 ?  76  LYS   A N    1 
ATOM   1785 C CA   . LYS   A 1 76  ? 33.613 -4.415  -6.466  1.00 12.00 ?  76  LYS   A CA   1 
ATOM   1786 C C    . LYS   A 1 76  ? 32.098 -4.502  -6.297  1.00 10.96 ?  76  LYS   A C    1 
ATOM   1787 O O    . LYS   A 1 76  ? 31.592 -4.584  -5.179  1.00 11.20 ?  76  LYS   A O    1 
ATOM   1788 C CB   . LYS   A 1 76  ? 34.153 -5.855  -6.497  1.00 13.55 ?  76  LYS   A CB   1 
ATOM   1789 C CG   . LYS   A 1 76  ? 35.664 -5.974  -6.687  1.00 15.11 ?  76  LYS   A CG   1 
ATOM   1790 C CD   . LYS   A 1 76  ? 36.172 -7.384  -6.464  1.00 16.51 ?  76  LYS   A CD   1 
ATOM   1791 C CE   . LYS   A 1 76  ? 37.669 -7.462  -6.706  1.00 19.16 ?  76  LYS   A CE   1 
ATOM   1792 N NZ   . LYS   A 1 76  ? 38.211 -8.812  -6.475  1.00 20.17 ?  76  LYS   A NZ   1 
ATOM   1793 H H    . LYS   A 1 76  ? 34.456 -4.208  -4.700  1.00 14.04 ?  76  LYS   A H    1 
ATOM   1794 H HA   . LYS   A 1 76  ? 33.824 -3.970  -7.302  1.00 14.41 ?  76  LYS   A HA   1 
ATOM   1795 H HB2  . LYS   A 1 76  ? 33.929 -6.285  -5.661  1.00 16.26 ?  76  LYS   A HB2  1 
ATOM   1796 H HB3  . LYS   A 1 76  ? 33.729 -6.324  -7.233  1.00 16.26 ?  76  LYS   A HB3  1 
ATOM   1797 H HG2  . LYS   A 1 76  ? 35.893 -5.711  -7.594  1.00 18.14 ?  76  LYS   A HG2  1 
ATOM   1798 H HG3  . LYS   A 1 76  ? 36.112 -5.389  -6.053  1.00 18.14 ?  76  LYS   A HG3  1 
ATOM   1799 H HD2  . LYS   A 1 76  ? 35.994 -7.648  -5.548  1.00 19.81 ?  76  LYS   A HD2  1 
ATOM   1800 H HD3  . LYS   A 1 76  ? 35.728 -7.987  -7.082  1.00 19.81 ?  76  LYS   A HD3  1 
ATOM   1801 H HE2  . LYS   A 1 76  ? 37.852 -7.217  -7.626  1.00 23.00 ?  76  LYS   A HE2  1 
ATOM   1802 H HE3  . LYS   A 1 76  ? 38.118 -6.852  -6.102  1.00 23.00 ?  76  LYS   A HE3  1 
ATOM   1803 H HZ1  . LYS   A 1 76  ? 39.089 -8.826  -6.628  1.00 24.21 ?  76  LYS   A HZ1  1 
ATOM   1804 H HZ2  . LYS   A 1 76  ? 38.062 -9.070  -5.635  1.00 24.21 ?  76  LYS   A HZ2  1 
ATOM   1805 H HZ3  . LYS   A 1 76  ? 37.820 -9.403  -7.024  1.00 24.21 ?  76  LYS   A HZ3  1 
ATOM   1806 N N    A VAL   A 1 77  ? 31.378 -4.522  -7.419  0.42 11.83 ?  77  VAL   A N    1 
ATOM   1807 N N    B VAL   A 1 77  ? 31.377 -4.480  -7.420  0.58 11.87 ?  77  VAL   A N    1 
ATOM   1808 C CA   A VAL   A 1 77  ? 29.959 -4.860  -7.362  0.42 12.10 ?  77  VAL   A CA   1 
ATOM   1809 C CA   B VAL   A 1 77  ? 29.975 -4.873  -7.374  0.58 12.12 ?  77  VAL   A CA   1 
ATOM   1810 C C    A VAL   A 1 77  ? 29.836 -6.315  -6.926  0.42 11.54 ?  77  VAL   A C    1 
ATOM   1811 C C    B VAL   A 1 77  ? 29.916 -6.307  -6.866  0.58 11.71 ?  77  VAL   A C    1 
ATOM   1812 O O    A VAL   A 1 77  ? 30.422 -7.214  -7.541  0.42 11.79 ?  77  VAL   A O    1 
ATOM   1813 O O    B VAL   A 1 77  ? 30.637 -7.186  -7.358  0.58 11.86 ?  77  VAL   A O    1 
ATOM   1814 C CB   A VAL   A 1 77  ? 29.264 -4.608  -8.706  0.42 13.30 ?  77  VAL   A CB   1 
ATOM   1815 C CB   B VAL   A 1 77  ? 29.326 -4.724  -8.758  0.58 13.38 ?  77  VAL   A CB   1 
ATOM   1816 C CG1  A VAL   A 1 77  ? 27.796 -5.015  -8.629  0.42 14.10 ?  77  VAL   A CG1  1 
ATOM   1817 C CG1  B VAL   A 1 77  ? 27.847 -5.066  -8.694  0.58 14.35 ?  77  VAL   A CG1  1 
ATOM   1818 C CG2  A VAL   A 1 77  ? 29.389 -3.145  -9.089  0.42 14.17 ?  77  VAL   A CG2  1 
ATOM   1819 C CG2  B VAL   A 1 77  ? 29.528 -3.311  -9.282  0.58 14.56 ?  77  VAL   A CG2  1 
ATOM   1820 H H    A VAL   A 1 77  ? 31.677 -4.351  -8.208  0.42 14.20 ?  77  VAL   A H    1 
ATOM   1821 H H    B VAL   A 1 77  ? 31.674 -4.253  -8.193  0.58 14.25 ?  77  VAL   A H    1 
ATOM   1822 H HA   A VAL   A 1 77  ? 29.530 -4.313  -6.690  0.42 14.52 ?  77  VAL   A HA   1 
ATOM   1823 H HA   B VAL   A 1 77  ? 29.502 -4.303  -6.748  0.58 14.54 ?  77  VAL   A HA   1 
ATOM   1824 H HB   A VAL   A 1 77  ? 29.694 -5.138  -9.396  0.42 15.96 ?  77  VAL   A HB   1 
ATOM   1825 H HB   B VAL   A 1 77  ? 29.756 -5.335  -9.376  0.58 16.06 ?  77  VAL   A HB   1 
ATOM   1826 H HG11 A VAL   A 1 77  ? 27.338 -4.684  -9.417  0.42 16.92 ?  77  VAL   A HG11 1 
ATOM   1827 H HG11 B VAL   A 1 77  ? 27.442 -4.856  -9.549  0.58 17.23 ?  77  VAL   A HG11 1 
ATOM   1828 H HG12 A VAL   A 1 77  ? 27.736 -5.981  -8.593  0.42 16.92 ?  77  VAL   A HG12 1 
ATOM   1829 H HG12 B VAL   A 1 77  ? 27.751 -6.010  -8.502  0.58 17.23 ?  77  VAL   A HG12 1 
ATOM   1830 H HG13 A VAL   A 1 77  ? 27.405 -4.626  -7.831  0.42 16.92 ?  77  VAL   A HG13 1 
ATOM   1831 H HG13 B VAL   A 1 77  ? 27.434 -4.537  -7.993  0.58 17.23 ?  77  VAL   A HG13 1 
ATOM   1832 H HG21 A VAL   A 1 77  ? 28.903 -2.991  -9.912  0.42 17.00 ?  77  VAL   A HG21 1 
ATOM   1833 H HG21 B VAL   A 1 77  ? 28.982 -3.184  -10.072 0.58 17.48 ?  77  VAL   A HG21 1 
ATOM   1834 H HG22 A VAL   A 1 77  ? 29.019 -2.601  -8.376  0.42 17.00 ?  77  VAL   A HG22 1 
ATOM   1835 H HG22 B VAL   A 1 77  ? 29.265 -2.677  -8.593  0.58 17.48 ?  77  VAL   A HG22 1 
ATOM   1836 H HG23 A VAL   A 1 77  ? 30.328 -2.930  -9.214  0.42 17.00 ?  77  VAL   A HG23 1 
ATOM   1837 H HG23 B VAL   A 1 77  ? 30.465 -3.181  -9.504  0.58 17.48 ?  77  VAL   A HG23 1 
ATOM   1838 N N    . GLY   A 1 78  ? 29.081 -6.547  -5.853  1.00 11.05 ?  78  GLY   A N    1 
ATOM   1839 C CA   . GLY   A 1 78  ? 29.029 -7.829  -5.182  1.00 11.39 ?  78  GLY   A CA   1 
ATOM   1840 C C    . GLY   A 1 78  ? 29.941 -7.919  -3.975  1.00 10.78 ?  78  GLY   A C    1 
ATOM   1841 O O    . GLY   A 1 78  ? 29.881 -8.918  -3.244  1.00 11.34 ?  78  GLY   A O    1 
ATOM   1842 H H    A GLY   A 1 78  ? 28.572 -5.950  -5.492  0.42 13.26 ?  78  GLY   A H    1 
ATOM   1843 H H    B GLY   A 1 78  ? 28.521 -5.967  -5.542  0.58 13.26 ?  78  GLY   A H    1 
ATOM   1844 H HA2  . GLY   A 1 78  ? 28.118 -7.997  -4.893  1.00 13.67 ?  78  GLY   A HA2  1 
ATOM   1845 H HA3  . GLY   A 1 78  ? 29.278 -8.526  -5.811  1.00 13.67 ?  78  GLY   A HA3  1 
ATOM   1846 N N    . GLY   A 1 79  ? 30.799 -6.916  -3.758  1.00 10.95 ?  79  GLY   A N    1 
ATOM   1847 C CA   . GLY   A 1 79  ? 31.751 -6.924  -2.670  1.00 11.40 ?  79  GLY   A CA   1 
ATOM   1848 C C    . GLY   A 1 79  ? 31.291 -6.125  -1.464  1.00 10.23 ?  79  GLY   A C    1 
ATOM   1849 O O    . GLY   A 1 79  ? 30.166 -5.630  -1.392  1.00 10.73 ?  79  GLY   A O    1 
ATOM   1850 H H    . GLY   A 1 79  ? 30.849 -6.209  -4.250  1.00 13.14 ?  79  GLY   A H    1 
ATOM   1851 H HA2  . GLY   A 1 79  ? 31.909 -7.846  -2.395  1.00 13.68 ?  79  GLY   A HA2  1 
ATOM   1852 H HA3  . GLY   A 1 79  ? 32.596 -6.560  -2.983  1.00 13.68 ?  79  GLY   A HA3  1 
ATOM   1853 N N    . SER   A 1 80  ? 32.189 -6.022  -0.487  1.00 10.90 ?  80  SER   A N    1 
ATOM   1854 C CA   . SER   A 1 80  ? 31.853 -5.394  0.779   1.00 10.13 ?  80  SER   A CA   1 
ATOM   1855 C C    . SER   A 1 80  ? 33.117 -4.935  1.489   1.00 10.35 ?  80  SER   A C    1 
ATOM   1856 O O    . SER   A 1 80  ? 34.237 -5.373  1.178   1.00 11.96 ?  80  SER   A O    1 
ATOM   1857 C CB   . SER   A 1 80  ? 31.090 -6.360  1.697   1.00 11.52 ?  80  SER   A CB   1 
ATOM   1858 O OG   . SER   A 1 80  ? 31.926 -7.405  2.162   1.00 13.53 ?  80  SER   A OG   1 
ATOM   1859 H H    . SER   A 1 80  ? 33.005 -6.298  -0.542  1.00 13.08 ?  80  SER   A H    1 
ATOM   1860 H HA   . SER   A 1 80  ? 31.297 -4.624  0.601   1.00 12.16 ?  80  SER   A HA   1 
ATOM   1861 H HB2  . SER   A 1 80  ? 30.757 -5.866  2.461   1.00 13.82 ?  80  SER   A HB2  1 
ATOM   1862 H HB3  . SER   A 1 80  ? 30.349 -6.743  1.202   1.00 13.82 ?  80  SER   A HB3  1 
ATOM   1863 H HG   . SER   A 1 80  ? 32.219 -7.848  1.505   1.00 16.24 ?  80  SER   A HG   1 
ATOM   1864 N N    . CYS   A 1 81  ? 32.918 -4.072  2.479   1.00 10.06 ?  81  CYS   A N    1 
ATOM   1865 C CA   . CYS   A 1 81  ? 33.959 -3.787  3.450   1.00 10.38 ?  81  CYS   A CA   1 
ATOM   1866 C C    . CYS   A 1 81  ? 33.313 -3.555  4.806   1.00 10.26 ?  81  CYS   A C    1 
ATOM   1867 O O    . CYS   A 1 81  ? 32.148 -3.153  4.891   1.00 11.03 ?  81  CYS   A O    1 
ATOM   1868 C CB   . CYS   A 1 81  ? 34.831 -2.601  3.031   1.00 10.91 ?  81  CYS   A CB   1 
ATOM   1869 S SG   . CYS   A 1 81  ? 33.938 -1.027  3.044   1.00 11.20 ?  81  CYS   A SG   1 
ATOM   1870 H H    . CYS   A 1 81  ? 32.186 -3.633  2.606   1.00 12.07 ?  81  CYS   A H    1 
ATOM   1871 H HA   . CYS   A 1 81  ? 34.535 -4.559  3.524   1.00 12.45 ?  81  CYS   A HA   1 
ATOM   1872 H HB2  . CYS   A 1 81  ? 35.582 -2.530  3.644   1.00 13.10 ?  81  CYS   A HB2  1 
ATOM   1873 H HB3  . CYS   A 1 81  ? 35.160 -2.754  2.129   1.00 13.10 ?  81  CYS   A HB3  1 
ATOM   1874 H HG   . CYS   A 1 81  ? 34.683 -0.146  2.711   1.00 13.44 ?  81  CYS   A HG   1 
ATOM   1875 N N    . VAL   A 1 82  ? 34.075 -3.817  5.866   1.00 10.39 ?  82  VAL   A N    1 
ATOM   1876 C CA   . VAL   A 1 82  ? 33.650 -3.570  7.236   1.00 10.80 ?  82  VAL   A CA   1 
ATOM   1877 C C    . VAL   A 1 82  ? 34.247 -2.255  7.706   1.00 10.94 ?  82  VAL   A C    1 
ATOM   1878 O O    . VAL   A 1 82  ? 35.470 -2.081  7.701   1.00 11.91 ?  82  VAL   A O    1 
ATOM   1879 C CB   . VAL   A 1 82  ? 34.073 -4.709  8.175   1.00 12.58 ?  82  VAL   A CB   1 
ATOM   1880 C CG1  . VAL   A 1 82  ? 33.624 -4.421  9.598   1.00 14.38 ?  82  VAL   A CG1  1 
ATOM   1881 C CG2  . VAL   A 1 82  ? 33.524 -6.047  7.690   1.00 13.74 ?  82  VAL   A CG2  1 
ATOM   1882 H H    . VAL   A 1 82  ? 34.867 -4.167  5.811   1.00 12.47 ?  82  VAL   A H    1 
ATOM   1883 H HA   . VAL   A 1 82  ? 32.683 -3.492  7.260   1.00 12.96 ?  82  VAL   A HA   1 
ATOM   1884 H HB   . VAL   A 1 82  ? 35.037 -4.768  8.177   1.00 15.10 ?  82  VAL   A HB   1 
ATOM   1885 H HG11 . VAL   A 1 82  ? 33.717 -5.229  10.127  1.00 17.26 ?  82  VAL   A HG11 1 
ATOM   1886 H HG12 . VAL   A 1 82  ? 34.176 -3.718  9.972   1.00 17.26 ?  82  VAL   A HG12 1 
ATOM   1887 H HG13 . VAL   A 1 82  ? 32.693 -4.142  9.588   1.00 17.26 ?  82  VAL   A HG13 1 
ATOM   1888 H HG21 . VAL   A 1 82  ? 33.763 -6.735  8.329   1.00 16.49 ?  82  VAL   A HG21 1 
ATOM   1889 H HG22 . VAL   A 1 82  ? 32.558 -5.984  7.617   1.00 16.49 ?  82  VAL   A HG22 1 
ATOM   1890 H HG23 . VAL   A 1 82  ? 33.908 -6.250  6.824   1.00 16.49 ?  82  VAL   A HG23 1 
ATOM   1891 N N    . LEU   A 1 83  ? 33.389 -1.334  8.123   1.00 10.61 ?  83  LEU   A N    1 
ATOM   1892 C CA   . LEU   A 1 83  ? 33.802 -0.065  8.701   1.00 10.57 ?  83  LEU   A CA   1 
ATOM   1893 C C    . LEU   A 1 83  ? 33.079 0.113   10.030  1.00 10.78 ?  83  LEU   A C    1 
ATOM   1894 O O    . LEU   A 1 83  ? 32.356 -0.776  10.489  1.00 11.38 ?  83  LEU   A O    1 
ATOM   1895 C CB   . LEU   A 1 83  ? 33.551 1.092   7.724   1.00 11.04 ?  83  LEU   A CB   1 
ATOM   1896 C CG   . LEU   A 1 83  ? 34.455 1.087   6.488   1.00 12.20 ?  83  LEU   A CG   1 
ATOM   1897 C CD1  . LEU   A 1 83  ? 34.024 2.131   5.481   1.00 12.93 ?  83  LEU   A CD1  1 
ATOM   1898 C CD2  . LEU   A 1 83  ? 35.929 1.306   6.878   1.00 12.82 ?  83  LEU   A CD2  1 
ATOM   1899 H H    . LEU   A 1 83  ? 32.538 -1.424  8.078   1.00 12.73 ?  83  LEU   A H    1 
ATOM   1900 H HA   . LEU   A 1 83  ? 34.755 -0.088  8.884   1.00 12.68 ?  83  LEU   A HA   1 
ATOM   1901 H HB2  . LEU   A 1 83  ? 32.632 1.048   7.413   1.00 13.25 ?  83  LEU   A HB2  1 
ATOM   1902 H HB3  . LEU   A 1 83  ? 33.693 1.935   8.186   1.00 13.25 ?  83  LEU   A HB3  1 
ATOM   1903 H HG   . LEU   A 1 83  ? 34.393 0.220   6.062   1.00 14.64 ?  83  LEU   A HG   1 
ATOM   1904 H HD11 . LEU   A 1 83  ? 34.616 2.092   4.713   1.00 15.51 ?  83  LEU   A HD11 1 
ATOM   1905 H HD12 . LEU   A 1 83  ? 33.113 1.943   5.206   1.00 15.51 ?  83  LEU   A HD12 1 
ATOM   1906 H HD13 . LEU   A 1 83  ? 34.072 3.007   5.893   1.00 15.51 ?  83  LEU   A HD13 1 
ATOM   1907 H HD21 . LEU   A 1 83  ? 36.454 1.464   6.074   1.00 15.39 ?  83  LEU   A HD21 1 
ATOM   1908 H HD22 . LEU   A 1 83  ? 35.994 2.080   7.465   1.00 15.39 ?  83  LEU   A HD22 1 
ATOM   1909 H HD23 . LEU   A 1 83  ? 36.264 0.520   7.337   1.00 15.39 ?  83  LEU   A HD23 1 
ATOM   1910 N N    . SER   A 1 84  ? 33.277 1.266   10.660  1.00 11.52 ?  84  SER   A N    1 
ATOM   1911 C CA   . SER   A 1 84  ? 32.624 1.519   11.932  1.00 11.38 ?  84  SER   A CA   1 
ATOM   1912 C C    . SER   A 1 84  ? 31.110 1.628   11.770  1.00 11.32 ?  84  SER   A C    1 
ATOM   1913 O O    . SER   A 1 84  ? 30.601 2.082   10.746  1.00 11.63 ?  84  SER   A O    1 
ATOM   1914 C CB   . SER   A 1 84  ? 33.135 2.836   12.509  1.00 12.70 ?  84  SER   A CB   1 
ATOM   1915 O OG   . SER   A 1 84  ? 32.503 3.131   13.735  1.00 13.85 ?  84  SER   A OG   1 
ATOM   1916 H H    . SER   A 1 84  ? 33.765 1.915   10.368  1.00 13.83 ?  84  SER   A H    1 
ATOM   1917 H HA   . SER   A 1 84  ? 32.831 0.795   12.552  1.00 13.66 ?  84  SER   A HA   1 
ATOM   1918 H HB2  . SER   A 1 84  ? 34.092 2.766   12.650  1.00 15.25 ?  84  SER   A HB2  1 
ATOM   1919 H HB3  . SER   A 1 84  ? 32.943 3.544   11.877  1.00 15.25 ?  84  SER   A HB3  1 
ATOM   1920 H HG   . SER   A 1 84  ? 32.799 3.857   14.038  1.00 16.62 ?  84  SER   A HG   1 
ATOM   1921 N N    A GLY   A 1 85  ? 30.395 1.221   12.813  0.42 12.25 ?  85  GLY   A N    1 
ATOM   1922 N N    B GLY   A 1 85  ? 30.392 1.220   12.810  0.58 12.50 ?  85  GLY   A N    1 
ATOM   1923 C CA   A GLY   A 1 85  ? 28.973 1.464   12.902  0.42 12.68 ?  85  GLY   A CA   1 
ATOM   1924 C CA   B GLY   A 1 85  ? 28.970 1.469   12.894  0.58 12.91 ?  85  GLY   A CA   1 
ATOM   1925 C C    A GLY   A 1 85  ? 28.609 2.785   13.539  0.42 12.82 ?  85  GLY   A C    1 
ATOM   1926 C C    B GLY   A 1 85  ? 28.608 2.782   13.549  0.58 12.92 ?  85  GLY   A C    1 
ATOM   1927 O O    A GLY   A 1 85  ? 27.423 3.117   13.628  0.42 13.25 ?  85  GLY   A O    1 
ATOM   1928 O O    B GLY   A 1 85  ? 27.422 3.104   13.666  0.58 13.34 ?  85  GLY   A O    1 
ATOM   1929 H H    A GLY   A 1 85  ? 30.719 0.797   13.490  0.42 14.71 ?  85  GLY   A H    1 
ATOM   1930 H H    B GLY   A 1 85  ? 30.710 0.792   13.487  0.58 15.00 ?  85  GLY   A H    1 
ATOM   1931 H HA2  A GLY   A 1 85  ? 28.594 1.448   12.009  0.42 15.22 ?  85  GLY   A HA2  1 
ATOM   1932 H HA2  B GLY   A 1 85  ? 28.595 1.463   11.998  0.58 15.49 ?  85  GLY   A HA2  1 
ATOM   1933 H HA3  A GLY   A 1 85  ? 28.560 0.755   13.416  0.42 15.22 ?  85  GLY   A HA3  1 
ATOM   1934 H HA3  B GLY   A 1 85  ? 28.550 0.758   13.399  0.58 15.49 ?  85  GLY   A HA3  1 
ATOM   1935 N N    . HIS   A 1 86  ? 29.598 3.552   13.988  1.00 12.65 ?  86  HIS   A N    1 
ATOM   1936 C CA   . HIS   A 1 86  ? 29.380 4.887   14.555  1.00 12.74 ?  86  HIS   A CA   1 
ATOM   1937 C C    . HIS   A 1 86  ? 28.395 4.770   15.710  1.00 13.04 ?  86  HIS   A C    1 
ATOM   1938 O O    . HIS   A 1 86  ? 28.582 3.897   16.572  1.00 14.76 ?  86  HIS   A O    1 
ATOM   1939 C CB   . HIS   A 1 86  ? 29.005 5.862   13.446  1.00 12.72 ?  86  HIS   A CB   1 
ATOM   1940 C CG   . HIS   A 1 86  ? 30.066 5.964   12.409  1.00 12.51 ?  86  HIS   A CG   1 
ATOM   1941 N ND1  . HIS   A 1 86  ? 31.161 6.789   12.553  1.00 13.99 ?  86  HIS   A ND1  1 
ATOM   1942 C CD2  . HIS   A 1 86  ? 30.259 5.270   11.264  1.00 12.44 ?  86  HIS   A CD2  1 
ATOM   1943 C CE1  . HIS   A 1 86  ? 31.967 6.621   11.520  1.00 14.08 ?  86  HIS   A CE1  1 
ATOM   1944 N NE2  . HIS   A 1 86  ? 31.444 5.706   10.724  1.00 13.30 ?  86  HIS   A NE2  1 
ATOM   1945 H H    A HIS   A 1 86  ? 30.420 3.319   13.980  0.42 15.18 ?  86  HIS   A H    1 
ATOM   1946 H H    B HIS   A 1 86  ? 30.420 3.319   13.979  0.58 15.18 ?  86  HIS   A H    1 
ATOM   1947 H HA   . HIS   A 1 86  ? 30.220 5.199   14.921  1.00 15.28 ?  86  HIS   A HA   1 
ATOM   1948 H HB2  . HIS   A 1 86  ? 28.188 5.563   13.013  1.00 15.26 ?  86  HIS   A HB2  1 
ATOM   1949 H HB3  . HIS   A 1 86  ? 28.874 6.749   13.821  1.00 15.26 ?  86  HIS   A HB3  1 
ATOM   1950 H HD2  . HIS   A 1 86  ? 29.697 4.619   10.898  1.00 14.93 ?  86  HIS   A HD2  1 
ATOM   1951 H HE1  . HIS   A 1 86  ? 32.764 7.078   11.365  1.00 16.89 ?  86  HIS   A HE1  1 
ATOM   1952 H HE2  . HIS   A 1 86  ? 31.790 5.434   9.975   1.00 15.97 ?  86  HIS   A HE2  1 
ATOM   1953 N N    . ASN   A 1 87  ? 27.383 5.621   15.779  1.00 14.07 ?  87  ASN   A N    1 
ATOM   1954 C CA   . ASN   A 1 87  ? 26.395 5.612   16.842  1.00 14.96 ?  87  ASN   A CA   1 
ATOM   1955 C C    . ASN   A 1 87  ? 25.264 4.627   16.598  1.00 16.39 ?  87  ASN   A C    1 
ATOM   1956 O O    . ASN   A 1 87  ? 24.336 4.576   17.406  1.00 18.96 ?  87  ASN   A O    1 
ATOM   1957 C CB   . ASN   A 1 87  ? 25.803 7.019   16.994  1.00 15.87 ?  87  ASN   A CB   1 
ATOM   1958 C CG   . ASN   A 1 87  ? 25.285 7.585   15.673  1.00 16.73 ?  87  ASN   A CG   1 
ATOM   1959 O OD1  . ASN   A 1 87  ? 25.933 7.471   14.638  1.00 17.34 ?  87  ASN   A OD1  1 
ATOM   1960 N ND2  . ASN   A 1 87  ? 24.111 8.191   15.708  1.00 18.23 ?  87  ASN   A ND2  1 
ATOM   1961 H H    . ASN   A 1 87  ? 27.239 6.231   15.199  1.00 16.89 ?  87  ASN   A H    1 
ATOM   1962 H HA   . ASN   A 1 87  ? 26.820 5.369   17.683  1.00 17.95 ?  87  ASN   A HA   1 
ATOM   1963 H HB2  . ASN   A 1 87  ? 25.060 6.986   17.622  1.00 19.05 ?  87  ASN   A HB2  1 
ATOM   1964 H HB3  . ASN   A 1 87  ? 26.491 7.615   17.332  1.00 19.05 ?  87  ASN   A HB3  1 
ATOM   1965 H HD21 . ASN   A 1 87  ? 23.783 8.520   14.987  1.00 21.87 ?  87  ASN   A HD21 1 
ATOM   1966 H HD22 . ASN   A 1 87  ? 23.681 8.255   16.449  1.00 21.87 ?  87  ASN   A HD22 1 
ATOM   1967 N N    A LEU   A 1 88  ? 25.323 3.848   15.518  0.42 15.02 ?  88  LEU   A N    1 
ATOM   1968 N N    B LEU   A 1 88  ? 25.324 3.834   15.528  0.58 15.01 ?  88  LEU   A N    1 
ATOM   1969 C CA   A LEU   A 1 88  ? 24.225 2.975   15.118  0.42 14.64 ?  88  LEU   A CA   1 
ATOM   1970 C CA   B LEU   A 1 88  ? 24.213 2.976   15.133  0.58 14.80 ?  88  LEU   A CA   1 
ATOM   1971 C C    A LEU   A 1 88  ? 24.446 1.510   15.473  0.42 14.32 ?  88  LEU   A C    1 
ATOM   1972 C C    B LEU   A 1 88  ? 24.442 1.491   15.379  0.58 14.41 ?  88  LEU   A C    1 
ATOM   1973 O O    A LEU   A 1 88  ? 23.476 0.803   15.763  0.42 15.16 ?  88  LEU   A O    1 
ATOM   1974 O O    B LEU   A 1 88  ? 23.464 0.743   15.471  0.58 15.31 ?  88  LEU   A O    1 
ATOM   1975 C CB   A LEU   A 1 88  ? 24.002 3.085   13.605  0.42 14.62 ?  88  LEU   A CB   1 
ATOM   1976 C CB   B LEU   A 1 88  ? 23.906 3.179   13.644  0.58 15.28 ?  88  LEU   A CB   1 
ATOM   1977 C CG   A LEU   A 1 88  ? 23.731 4.487   13.056  0.42 15.40 ?  88  LEU   A CG   1 
ATOM   1978 C CG   B LEU   A 1 88  ? 23.587 4.621   13.238  0.58 15.94 ?  88  LEU   A CG   1 
ATOM   1979 C CD1  A LEU   A 1 88  ? 23.649 4.446   11.540  0.42 15.47 ?  88  LEU   A CD1  1 
ATOM   1980 C CD1  B LEU   A 1 88  ? 23.405 4.739   11.730  0.58 16.01 ?  88  LEU   A CD1  1 
ATOM   1981 C CD2  A LEU   A 1 88  ? 22.452 5.068   13.649  0.42 17.14 ?  88  LEU   A CD2  1 
ATOM   1982 C CD2  B LEU   A 1 88  ? 22.349 5.130   13.966  0.58 17.20 ?  88  LEU   A CD2  1 
ATOM   1983 H H    A LEU   A 1 88  ? 26.009 3.805   14.997  0.42 18.02 ?  88  LEU   A H    1 
ATOM   1984 H H    B LEU   A 1 88  ? 26.013 3.773   15.017  0.58 18.01 ?  88  LEU   A H    1 
ATOM   1985 H HA   A LEU   A 1 88  ? 23.415 3.266   15.558  0.42 17.56 ?  88  LEU   A HA   1 
ATOM   1986 H HA   B LEU   A 1 88  ? 23.428 3.241   15.634  0.58 17.76 ?  88  LEU   A HA   1 
ATOM   1987 H HB2  A LEU   A 1 88  ? 24.788 2.753   13.150  0.42 17.54 ?  88  LEU   A HB2  1 
ATOM   1988 H HB2  B LEU   A 1 88  ? 24.672 2.892   13.129  0.58 18.33 ?  88  LEU   A HB2  1 
ATOM   1989 H HB3  A LEU   A 1 88  ? 23.236 2.539   13.369  0.42 17.54 ?  88  LEU   A HB3  1 
ATOM   1990 H HB3  B LEU   A 1 88  ? 23.135 2.635   13.416  0.58 18.33 ?  88  LEU   A HB3  1 
ATOM   1991 H HG   A LEU   A 1 88  ? 24.465 5.073   13.298  0.42 18.48 ?  88  LEU   A HG   1 
ATOM   1992 H HG   B LEU   A 1 88  ? 24.331 5.189   13.488  0.58 19.13 ?  88  LEU   A HG   1 
ATOM   1993 H HD11 A LEU   A 1 88  ? 23.514 5.346   11.204  0.42 18.57 ?  88  LEU   A HD11 1 
ATOM   1994 H HD11 B LEU   A 1 88  ? 23.227 5.668   11.504  0.58 19.21 ?  88  LEU   A HD11 1 
ATOM   1995 H HD12 A LEU   A 1 88  ? 24.476 4.081   11.189  0.42 18.57 ?  88  LEU   A HD12 1 
ATOM   1996 H HD12 B LEU   A 1 88  ? 24.216 4.443   11.288  0.58 19.21 ?  88  LEU   A HD12 1 
ATOM   1997 H HD13 A LEU   A 1 88  ? 22.902 3.882   11.281  0.42 18.57 ?  88  LEU   A HD13 1 
ATOM   1998 H HD13 B LEU   A 1 88  ? 22.657 4.186   11.456  0.58 19.21 ?  88  LEU   A HD13 1 
ATOM   1999 H HD21 A LEU   A 1 88  ? 22.266 5.922   13.227  0.42 20.57 ?  88  LEU   A HD21 1 
ATOM   2000 H HD21 B LEU   A 1 88  ? 22.100 5.991   13.595  0.58 20.64 ?  88  LEU   A HD21 1 
ATOM   2001 H HD22 A LEU   A 1 88  ? 21.722 4.452   13.488  0.42 20.57 ?  88  LEU   A HD22 1 
ATOM   2002 H HD22 B LEU   A 1 88  ? 21.629 4.494   13.841  0.58 20.64 ?  88  LEU   A HD22 1 
ATOM   2003 H HD23 A LEU   A 1 88  ? 22.577 5.193   14.604  0.42 20.57 ?  88  LEU   A HD23 1 
ATOM   2004 H HD23 B LEU   A 1 88  ? 22.555 5.221   14.908  0.58 20.64 ?  88  LEU   A HD23 1 
ATOM   2005 N N    . ALA   A 1 89  ? 25.692 1.051   15.468  1.00 13.89 ?  89  ALA   A N    1 
ATOM   2006 C CA   . ALA   A 1 89  ? 26.027 -0.363  15.585  1.00 13.54 ?  89  ALA   A CA   1 
ATOM   2007 C C    . ALA   A 1 89  ? 27.514 -0.420  15.884  1.00 14.02 ?  89  ALA   A C    1 
ATOM   2008 O O    . ALA   A 1 89  ? 28.218 0.582   15.759  1.00 14.93 ?  89  ALA   A O    1 
ATOM   2009 C CB   . ALA   A 1 89  ? 25.767 -1.079  14.259  1.00 13.60 ?  89  ALA   A CB   1 
ATOM   2010 H H    A ALA   A 1 89  ? 26.383 1.560   15.405  0.42 16.67 ?  89  ALA   A H    1 
ATOM   2011 H H    B ALA   A 1 89  ? 26.381 1.566   15.440  0.58 16.67 ?  89  ALA   A H    1 
ATOM   2012 H HA   . ALA   A 1 89  ? 25.523 -0.781  16.299  1.00 16.25 ?  89  ALA   A HA   1 
ATOM   2013 H HB1  . ALA   A 1 89  ? 26.021 -2.010  14.348  1.00 16.32 ?  89  ALA   A HB1  1 
ATOM   2014 H HB2  . ALA   A 1 89  ? 24.824 -1.012  14.042  1.00 16.32 ?  89  ALA   A HB2  1 
ATOM   2015 H HB3  . ALA   A 1 89  ? 26.297 -0.658  13.563  1.00 16.32 ?  89  ALA   A HB3  1 
ATOM   2016 N N    A LYS   A 1 90  ? 28.004 -1.611  16.228  0.42 15.20 ?  90  LYS   A N    1 
ATOM   2017 N N    B LYS   A 1 90  ? 27.991 -1.588  16.305  0.58 13.90 ?  90  LYS   A N    1 
ATOM   2018 C CA   A LYS   A 1 90  ? 29.448 -1.770  16.381  0.42 16.10 ?  90  LYS   A CA   1 
ATOM   2019 C CA   B LYS   A 1 90  ? 29.435 -1.735  16.447  0.58 14.08 ?  90  LYS   A CA   1 
ATOM   2020 C C    A LYS   A 1 90  ? 30.160 -1.630  15.039  0.42 15.53 ?  90  LYS   A C    1 
ATOM   2021 C C    B LYS   A 1 90  ? 30.123 -1.532  15.103  0.58 12.80 ?  90  LYS   A C    1 
ATOM   2022 O O    A LYS   A 1 90  ? 31.124 -0.860  14.912  0.42 16.75 ?  90  LYS   A O    1 
ATOM   2023 O O    B LYS   A 1 90  ? 31.046 -0.710  14.973  0.58 13.98 ?  90  LYS   A O    1 
ATOM   2024 C CB   A LYS   A 1 90  ? 29.777 -3.111  17.038  0.42 18.22 ?  90  LYS   A CB   1 
ATOM   2025 C CB   B LYS   A 1 90  ? 29.780 -3.100  17.042  0.58 16.10 ?  90  LYS   A CB   1 
ATOM   2026 C CG   A LYS   A 1 90  ? 31.260 -3.285  17.344  0.42 21.45 ?  90  LYS   A CG   1 
ATOM   2027 C CG   B LYS   A 1 90  ? 31.255 -3.250  17.379  0.58 20.70 ?  90  LYS   A CG   1 
ATOM   2028 C CD   A LYS   A 1 90  ? 31.505 -4.500  18.226  0.42 24.04 ?  90  LYS   A CD   1 
ATOM   2029 C CD   B LYS   A 1 90  ? 31.512 -4.508  18.190  0.58 24.07 ?  90  LYS   A CD   1 
ATOM   2030 C CE   A LYS   A 1 90  ? 32.929 -4.528  18.769  0.42 26.09 ?  90  LYS   A CE   1 
ATOM   2031 C CE   B LYS   A 1 90  ? 32.888 -4.481  18.840  0.58 26.61 ?  90  LYS   A CE   1 
ATOM   2032 N NZ   A LYS   A 1 90  ? 33.933 -4.951  17.754  0.42 27.53 ?  90  LYS   A NZ   1 
ATOM   2033 N NZ   B LYS   A 1 90  ? 33.990 -4.552  17.845  0.58 28.31 ?  90  LYS   A NZ   1 
ATOM   2034 H H    A LYS   A 1 90  ? 27.537 -2.314  16.378  0.42 18.24 ?  90  LYS   A H    1 
ATOM   2035 H H    B LYS   A 1 90  ? 27.520 -2.277  16.509  0.58 16.68 ?  90  LYS   A H    1 
ATOM   2036 H HA   A LYS   A 1 90  ? 29.779 -1.070  16.960  0.42 19.32 ?  90  LYS   A HA   1 
ATOM   2037 H HA   B LYS   A 1 90  ? 29.764 -1.056  17.053  0.58 16.90 ?  90  LYS   A HA   1 
ATOM   2038 H HB2  A LYS   A 1 90  ? 29.290 -3.176  17.876  0.42 21.87 ?  90  LYS   A HB2  1 
ATOM   2039 H HB2  B LYS   A 1 90  ? 29.270 -3.225  17.861  0.58 19.33 ?  90  LYS   A HB2  1 
ATOM   2040 H HB3  A LYS   A 1 90  ? 29.508 -3.829  16.444  0.42 21.87 ?  90  LYS   A HB3  1 
ATOM   2041 H HB3  B LYS   A 1 90  ? 29.546 -3.793  16.404  0.58 19.33 ?  90  LYS   A HB3  1 
ATOM   2042 H HG2  A LYS   A 1 90  ? 31.747 -3.408  16.514  0.42 25.74 ?  90  LYS   A HG2  1 
ATOM   2043 H HG2  B LYS   A 1 90  ? 31.769 -3.307  16.559  0.58 24.84 ?  90  LYS   A HG2  1 
ATOM   2044 H HG3  A LYS   A 1 90  ? 31.585 -2.499  17.811  0.42 25.74 ?  90  LYS   A HG3  1 
ATOM   2045 H HG3  B LYS   A 1 90  ? 31.543 -2.487  17.905  0.58 24.84 ?  90  LYS   A HG3  1 
ATOM   2046 H HD2  A LYS   A 1 90  ? 30.893 -4.477  18.979  0.42 28.85 ?  90  LYS   A HD2  1 
ATOM   2047 H HD2  B LYS   A 1 90  ? 30.845 -4.580  18.893  0.58 28.89 ?  90  LYS   A HD2  1 
ATOM   2048 H HD3  A LYS   A 1 90  ? 31.363 -5.307  17.705  0.42 28.85 ?  90  LYS   A HD3  1 
ATOM   2049 H HD3  B LYS   A 1 90  ? 31.467 -5.283  17.606  0.58 28.89 ?  90  LYS   A HD3  1 
ATOM   2050 H HE2  A LYS   A 1 90  ? 33.169 -3.638  19.073  0.42 31.31 ?  90  LYS   A HE2  1 
ATOM   2051 H HE2  B LYS   A 1 90  ? 32.986 -3.654  19.339  0.58 31.93 ?  90  LYS   A HE2  1 
ATOM   2052 H HE3  A LYS   A 1 90  ? 32.973 -5.153  19.510  0.42 31.31 ?  90  LYS   A HE3  1 
ATOM   2053 H HE3  B LYS   A 1 90  ? 32.972 -5.241  19.438  0.58 31.93 ?  90  LYS   A HE3  1 
ATOM   2054 H HZ1  A LYS   A 1 90  ? 34.740 -5.002  18.127  0.42 33.04 ?  90  LYS   A HZ1  1 
ATOM   2055 H HZ1  B LYS   A 1 90  ? 34.777 -4.534  18.260  0.58 33.97 ?  90  LYS   A HZ1  1 
ATOM   2056 H HZ2  A LYS   A 1 90  ? 33.716 -5.749  17.425  0.42 33.04 ?  90  LYS   A HZ2  1 
ATOM   2057 H HZ2  B LYS   A 1 90  ? 33.928 -5.308  17.377  0.58 33.97 ?  90  LYS   A HZ2  1 
ATOM   2058 H HZ3  A LYS   A 1 90  ? 33.960 -4.361  17.089  0.42 33.04 ?  90  LYS   A HZ3  1 
ATOM   2059 H HZ3  B LYS   A 1 90  ? 33.941 -3.862  17.287  0.58 33.97 ?  90  LYS   A HZ3  1 
ATOM   2060 N N    A HIS   A 1 91  ? 29.692 -2.357  14.026  0.42 14.34 ?  91  HIS   A N    1 
ATOM   2061 N N    B HIS   A 1 91  ? 29.644 -2.239  14.079  0.58 11.09 ?  91  HIS   A N    1 
ATOM   2062 C CA   A HIS   A 1 91  ? 30.280 -2.343  12.697  0.42 13.72 ?  91  HIS   A CA   1 
ATOM   2063 C CA   B HIS   A 1 91  ? 30.226 -2.227  12.753  0.58 10.60 ?  91  HIS   A CA   1 
ATOM   2064 C C    A HIS   A 1 91  ? 29.194 -2.098  11.666  0.42 11.87 ?  91  HIS   A C    1 
ATOM   2065 C C    B HIS   A 1 91  ? 29.145 -1.958  11.725  0.58 10.43 ?  91  HIS   A C    1 
ATOM   2066 O O    A HIS   A 1 91  ? 28.051 -2.533  11.831  0.42 11.43 ?  91  HIS   A O    1 
ATOM   2067 O O    B HIS   A 1 91  ? 27.966 -2.258  11.940  0.58 10.93 ?  91  HIS   A O    1 
ATOM   2068 C CB   A HIS   A 1 91  ? 30.909 -3.695  12.346  0.42 15.89 ?  91  HIS   A CB   1 
ATOM   2069 C CB   B HIS   A 1 91  ? 30.828 -3.588  12.404  0.58 13.05 ?  91  HIS   A CB   1 
ATOM   2070 C CG   A HIS   A 1 91  ? 31.897 -4.188  13.354  0.42 19.07 ?  91  HIS   A CG   1 
ATOM   2071 C CG   B HIS   A 1 91  ? 31.822 -4.081  13.402  0.58 17.43 ?  91  HIS   A CG   1 
ATOM   2072 N ND1  A HIS   A 1 91  ? 33.173 -3.679  13.456  0.42 20.51 ?  91  HIS   A ND1  1 
ATOM   2073 N ND1  B HIS   A 1 91  ? 33.100 -3.575  13.488  0.58 19.68 ?  91  HIS   A ND1  1 
ATOM   2074 C CD2  A HIS   A 1 91  ? 31.804 -5.161  14.290  0.42 20.37 ?  91  HIS   A CD2  1 
ATOM   2075 C CD2  B HIS   A 1 91  ? 31.732 -5.041  14.352  0.58 19.59 ?  91  HIS   A CD2  1 
ATOM   2076 C CE1  A HIS   A 1 91  ? 33.820 -4.309  14.421  0.42 21.27 ?  91  HIS   A CE1  1 
ATOM   2077 C CE1  B HIS   A 1 91  ? 33.755 -4.200  14.451  0.58 21.00 ?  91  HIS   A CE1  1 
ATOM   2078 N NE2  A HIS   A 1 91  ? 33.012 -5.214  14.943  0.42 21.38 ?  91  HIS   A NE2  1 
ATOM   2079 N NE2  B HIS   A 1 91  ? 32.946 -5.095  14.991  0.58 21.27 ?  91  HIS   A NE2  1 
ATOM   2080 H H    A HIS   A 1 91  ? 29.008 -2.883  14.087  0.42 17.21 ?  91  HIS   A H    1 
ATOM   2081 H H    B HIS   A 1 91  ? 28.947 -2.758  14.143  0.58 13.30 ?  91  HIS   A H    1 
ATOM   2082 H HA   A HIS   A 1 91  ? 30.949 -1.649  12.624  0.42 16.47 ?  91  HIS   A HA   1 
ATOM   2083 H HA   B HIS   A 1 91  ? 30.903 -1.544  12.694  0.58 12.72 ?  91  HIS   A HA   1 
ATOM   2084 H HB2  A HIS   A 1 91  ? 30.206 -4.358  12.271  0.42 19.07 ?  91  HIS   A HB2  1 
ATOM   2085 H HB2  B HIS   A 1 91  ? 30.116 -4.243  12.345  0.58 15.66 ?  91  HIS   A HB2  1 
ATOM   2086 H HB3  A HIS   A 1 91  ? 31.371 -3.610  11.495  0.42 19.07 ?  91  HIS   A HB3  1 
ATOM   2087 H HB3  B HIS   A 1 91  ? 31.278 -3.514  11.546  0.58 15.66 ?  91  HIS   A HB3  1 
ATOM   2088 H HD1  A HIS   A 1 91  ? 33.496 -3.045  12.969  0.42 24.61 ?  91  HIS   A HD1  1 
ATOM   2089 H HD1  B HIS   A 1 91  ? 33.423 -2.949  12.989  0.58 23.62 ?  91  HIS   A HD1  1 
ATOM   2090 H HD2  A HIS   A 1 91  ? 31.060 -5.688  14.463  0.42 24.44 ?  91  HIS   A HD2  1 
ATOM   2091 H HD2  B HIS   A 1 91  ? 30.988 -5.563  14.538  0.58 23.51 ?  91  HIS   A HD2  1 
ATOM   2092 H HE1  A HIS   A 1 91  ? 34.696 -4.141  14.685  0.42 25.53 ?  91  HIS   A HE1  1 
ATOM   2093 H HE1  B HIS   A 1 91  ? 34.636 -4.036  14.703  0.58 25.21 ?  91  HIS   A HE1  1 
ATOM   2094 N N    . CYS   A 1 92  ? 29.565 -1.418  10.587  1.00 10.80 ?  92  CYS   A N    1 
ATOM   2095 C CA   . CYS   A 1 92  ? 28.737 -1.341  9.395   1.00 10.54 ?  92  CYS   A CA   1 
ATOM   2096 C C    . CYS   A 1 92  ? 29.394 -2.165  8.299   1.00 10.09 ?  92  CYS   A C    1 
ATOM   2097 O O    . CYS   A 1 92  ? 30.552 -1.920  7.941   1.00 11.10 ?  92  CYS   A O    1 
ATOM   2098 C CB   . CYS   A 1 92  ? 28.516 0.097   8.932   1.00 10.90 ?  92  CYS   A CB   1 
ATOM   2099 S SG   . CYS   A 1 92  ? 27.519 0.185   7.415   1.00 10.70 ?  92  CYS   A SG   1 
ATOM   2100 H H    A CYS   A 1 92  ? 30.301 -0.976  10.530  0.42 12.96 ?  92  CYS   A H    1 
ATOM   2101 H H    B CYS   A 1 92  ? 30.354 -1.093  10.478  0.58 12.96 ?  92  CYS   A H    1 
ATOM   2102 H HA   . CYS   A 1 92  ? 27.872 -1.727  9.580   1.00 12.65 ?  92  CYS   A HA   1 
ATOM   2103 H HB2  . CYS   A 1 92  ? 28.045 0.590   9.625   1.00 13.08 ?  92  CYS   A HB2  1 
ATOM   2104 H HB3  . CYS   A 1 92  ? 29.370 0.515   8.749   1.00 13.08 ?  92  CYS   A HB3  1 
ATOM   2105 H HG   . CYS   A 1 92  ? 27.370 1.337   7.117   1.00 12.83 ?  92  CYS   A HG   1 
ATOM   2106 N N    . LEU   A 1 93  ? 28.665 -3.153  7.794   1.00 10.26 ?  93  LEU   A N    1 
ATOM   2107 C CA   . LEU   A 1 93  ? 29.080 -3.916  6.624   1.00 9.77  ?  93  LEU   A CA   1 
ATOM   2108 C C    . LEU   A 1 93  ? 28.487 -3.235  5.393   1.00 9.45  ?  93  LEU   A C    1 
ATOM   2109 O O    . LEU   A 1 93  ? 27.275 -3.302  5.160   1.00 9.39  ?  93  LEU   A O    1 
ATOM   2110 C CB   . LEU   A 1 93  ? 28.612 -5.366  6.745   1.00 10.03 ?  93  LEU   A CB   1 
ATOM   2111 C CG   . LEU   A 1 93  ? 28.998 -6.265  5.573   1.00 10.47 ?  93  LEU   A CG   1 
ATOM   2112 C CD1  . LEU   A 1 93  ? 30.491 -6.525  5.549   1.00 11.58 ?  93  LEU   A CD1  1 
ATOM   2113 C CD2  . LEU   A 1 93  ? 28.240 -7.598  5.609   1.00 11.48 ?  93  LEU   A CD2  1 
ATOM   2114 H H    . LEU   A 1 93  ? 27.909 -3.401  8.122   1.00 12.31 ?  93  LEU   A H    1 
ATOM   2115 H HA   . LEU   A 1 93  ? 30.045 -3.898  6.556   1.00 11.72 ?  93  LEU   A HA   1 
ATOM   2116 H HB2  . LEU   A 1 93  ? 29.005 -5.746  7.551   1.00 12.04 ?  93  LEU   A HB2  1 
ATOM   2117 H HB3  . LEU   A 1 93  ? 27.649 -5.376  6.819   1.00 12.04 ?  93  LEU   A HB3  1 
ATOM   2118 H HG   . LEU   A 1 93  ? 28.768 -5.821  4.748   1.00 12.57 ?  93  LEU   A HG   1 
ATOM   2119 H HD11 . LEU   A 1 93  ? 30.696 -7.132  4.824   1.00 13.90 ?  93  LEU   A HD11 1 
ATOM   2120 H HD12 . LEU   A 1 93  ? 30.957 -5.683  5.420   1.00 13.90 ?  93  LEU   A HD12 1 
ATOM   2121 H HD13 . LEU   A 1 93  ? 30.758 -6.921  6.397   1.00 13.90 ?  93  LEU   A HD13 1 
ATOM   2122 H HD21 . LEU   A 1 93  ? 28.515 -8.139  4.851   1.00 13.77 ?  93  LEU   A HD21 1 
ATOM   2123 H HD22 . LEU   A 1 93  ? 28.451 -8.062  6.437   1.00 13.77 ?  93  LEU   A HD22 1 
ATOM   2124 H HD23 . LEU   A 1 93  ? 27.289 -7.421  5.563   1.00 13.77 ?  93  LEU   A HD23 1 
ATOM   2125 N N    . HIS   A 1 94  ? 29.335 -2.540  4.630   1.00 9.23  ?  94  HIS   A N    1 
ATOM   2126 C CA   . HIS   A 1 94  ? 28.909 -1.880  3.400   1.00 9.40  ?  94  HIS   A CA   1 
ATOM   2127 C C    . HIS   A 1 94  ? 28.943 -2.912  2.289   1.00 9.46  ?  94  HIS   A C    1 
ATOM   2128 O O    . HIS   A 1 94  ? 30.020 -3.438  1.972   1.00 10.79 ?  94  HIS   A O    1 
ATOM   2129 C CB   . HIS   A 1 94  ? 29.852 -0.721  3.068   1.00 9.65  ?  94  HIS   A CB   1 
ATOM   2130 C CG   . HIS   A 1 94  ? 29.837 0.365   4.086   1.00 9.48  ?  94  HIS   A CG   1 
ATOM   2131 N ND1  . HIS   A 1 94  ? 28.963 1.432   4.026   1.00 9.41  ?  94  HIS   A ND1  1 
ATOM   2132 C CD2  . HIS   A 1 94  ? 30.568 0.530   5.211   1.00 10.27 ?  94  HIS   A CD2  1 
ATOM   2133 C CE1  . HIS   A 1 94  ? 29.179 2.214   5.068   1.00 9.71  ?  94  HIS   A CE1  1 
ATOM   2134 N NE2  . HIS   A 1 94  ? 30.147 1.689   5.801   1.00 10.01 ?  94  HIS   A NE2  1 
ATOM   2135 H H    . HIS   A 1 94  ? 30.170 -2.434  4.807   1.00 11.08 ?  94  HIS   A H    1 
ATOM   2136 H HA   . HIS   A 1 94  ? 28.004 -1.540  3.496   1.00 11.28 ?  94  HIS   A HA   1 
ATOM   2137 H HB2  . HIS   A 1 94  ? 30.754 -1.056  3.004   1.00 11.58 ?  94  HIS   A HB2  1 
ATOM   2138 H HB3  . HIS   A 1 94  ? 29.579 -0.329  2.221   1.00 11.58 ?  94  HIS   A HB3  1 
ATOM   2139 H HD2  . HIS   A 1 94  ? 31.245 -0.025  5.522   1.00 12.33 ?  94  HIS   A HD2  1 
ATOM   2140 H HE1  . HIS   A 1 94  ? 28.718 3.003   5.252   1.00 11.65 ?  94  HIS   A HE1  1 
ATOM   2141 H HE2  . HIS   A 1 94  ? 30.460 2.034   6.527   1.00 12.01 ?  94  HIS   A HE2  1 
ATOM   2142 N N    . VAL   A 1 95  ? 27.777 -3.231  1.725   1.00 9.18  ?  95  VAL   A N    1 
ATOM   2143 C CA   . VAL   A 1 95  ? 27.642 -4.268  0.709   1.00 9.29  ?  95  VAL   A CA   1 
ATOM   2144 C C    . VAL   A 1 95  ? 27.108 -3.645  -0.567  1.00 9.08  ?  95  VAL   A C    1 
ATOM   2145 O O    . VAL   A 1 95  ? 26.100 -2.925  -0.533  1.00 10.15 ?  95  VAL   A O    1 
ATOM   2146 C CB   . VAL   A 1 95  ? 26.711 -5.406  1.164   1.00 9.65  ?  95  VAL   A CB   1 
ATOM   2147 C CG1  . VAL   A 1 95  ? 26.600 -6.454  0.061   1.00 10.70 ?  95  VAL   A CG1  1 
ATOM   2148 C CG2  . VAL   A 1 95  ? 27.201 -6.005  2.462   1.00 9.92  ?  95  VAL   A CG2  1 
ATOM   2149 H H    . VAL   A 1 95  ? 27.028 -2.850  1.920   1.00 11.02 ?  95  VAL   A H    1 
ATOM   2150 H HA   . VAL   A 1 95  ? 28.514 -4.650  0.520   1.00 11.15 ?  95  VAL   A HA   1 
ATOM   2151 H HB   . VAL   A 1 95  ? 25.826 -5.050  1.317   1.00 11.57 ?  95  VAL   A HB   1 
ATOM   2152 H HG11 . VAL   A 1 95  ? 26.219 -7.268  0.428   1.00 12.84 ?  95  VAL   A HG11 1 
ATOM   2153 H HG12 . VAL   A 1 95  ? 26.026 -6.117  -0.648  1.00 12.84 ?  95  VAL   A HG12 1 
ATOM   2154 H HG13 . VAL   A 1 95  ? 27.485 -6.641  -0.295  1.00 12.84 ?  95  VAL   A HG13 1 
ATOM   2155 H HG21 . VAL   A 1 95  ? 26.641 -6.767  2.687   1.00 11.90 ?  95  VAL   A HG21 1 
ATOM   2156 H HG22 . VAL   A 1 95  ? 28.120 -6.296  2.348   1.00 11.90 ?  95  VAL   A HG22 1 
ATOM   2157 H HG23 . VAL   A 1 95  ? 27.145 -5.335  3.156   1.00 11.90 ?  95  VAL   A HG23 1 
ATOM   2158 N N    . VAL   A 1 96  ? 27.745 -3.957  -1.696  1.00 9.15  ?  96  VAL   A N    1 
ATOM   2159 C CA   . VAL   A 1 96  ? 27.345 -3.425  -2.993  1.00 10.01 ?  96  VAL   A CA   1 
ATOM   2160 C C    . VAL   A 1 96  ? 26.558 -4.482  -3.763  1.00 10.60 ?  96  VAL   A C    1 
ATOM   2161 O O    . VAL   A 1 96  ? 27.129 -5.427  -4.308  1.00 11.44 ?  96  VAL   A O    1 
ATOM   2162 C CB   . VAL   A 1 96  ? 28.547 -2.937  -3.805  1.00 10.53 ?  96  VAL   A CB   1 
ATOM   2163 C CG1  . VAL   A 1 96  ? 28.063 -2.338  -5.097  1.00 10.85 ?  96  VAL   A CG1  1 
ATOM   2164 C CG2  . VAL   A 1 96  ? 29.371 -1.938  -3.013  1.00 11.28 ?  96  VAL   A CG2  1 
ATOM   2165 H H    . VAL   A 1 96  ? 28.435 -4.476  -1.731  1.00 10.98 ?  96  VAL   A H    1 
ATOM   2166 H HA   . VAL   A 1 96  ? 26.762 -2.666  -2.847  1.00 12.02 ?  96  VAL   A HA   1 
ATOM   2167 H HB   . VAL   A 1 96  ? 29.115 -3.688  -4.017  1.00 12.64 ?  96  VAL   A HB   1 
ATOM   2168 H HG11 . VAL   A 1 96  ? 28.793 -1.842  -5.506  1.00 13.02 ?  96  VAL   A HG11 1 
ATOM   2169 H HG12 . VAL   A 1 96  ? 27.776 -3.047  -5.690  1.00 13.02 ?  96  VAL   A HG12 1 
ATOM   2170 H HG13 . VAL   A 1 96  ? 27.324 -1.736  -4.913  1.00 13.02 ?  96  VAL   A HG13 1 
ATOM   2171 H HG21 . VAL   A 1 96  ? 30.076 -1.590  -3.577  1.00 13.54 ?  96  VAL   A HG21 1 
ATOM   2172 H HG22 . VAL   A 1 96  ? 28.792 -1.211  -2.722  1.00 13.54 ?  96  VAL   A HG22 1 
ATOM   2173 H HG23 . VAL   A 1 96  ? 29.750 -2.383  -2.240  1.00 13.54 ?  96  VAL   A HG23 1 
ATOM   2174 N N    A GLY   A 1 97  ? 25.239 -4.334  -3.763  0.42 10.63 ?  97  GLY   A N    1 
ATOM   2175 N N    B GLY   A 1 97  ? 25.244 -4.316  -3.860  0.58 10.38 ?  97  GLY   A N    1 
ATOM   2176 C CA   A GLY   A 1 97  ? 24.392 -5.082  -4.651  0.42 11.23 ?  97  GLY   A CA   1 
ATOM   2177 C CA   B GLY   A 1 97  ? 24.469 -5.105  -4.789  0.58 11.20 ?  97  GLY   A CA   1 
ATOM   2178 C C    A GLY   A 1 97  ? 24.334 -4.393  -5.999  0.42 11.34 ?  97  GLY   A C    1 
ATOM   2179 C C    B GLY   A 1 97  ? 24.582 -4.550  -6.199  0.58 10.99 ?  97  GLY   A C    1 
ATOM   2180 O O    A GLY   A 1 97  ? 24.548 -3.181  -6.109  0.42 11.46 ?  97  GLY   A O    1 
ATOM   2181 O O    B GLY   A 1 97  ? 24.960 -3.391  -6.399  0.58 11.99 ?  97  GLY   A O    1 
ATOM   2182 H H    A GLY   A 1 97  ? 24.809 -3.792  -3.246  0.42 12.76 ?  97  GLY   A H    1 
ATOM   2183 H H    B GLY   A 1 97  ? 24.778 -3.757  -3.394  0.58 12.45 ?  97  GLY   A H    1 
ATOM   2184 H HA2  A GLY   A 1 97  ? 24.750 -5.971  -4.768  0.42 13.47 ?  97  GLY   A HA2  1 
ATOM   2185 H HA2  B GLY   A 1 97  ? 24.791 -6.021  -4.780  0.58 13.44 ?  97  GLY   A HA2  1 
ATOM   2186 H HA3  A GLY   A 1 97  ? 23.494 -5.147  -4.282  0.42 13.47 ?  97  GLY   A HA3  1 
ATOM   2187 H HA3  B GLY   A 1 97  ? 23.534 -5.104  -4.527  0.58 13.44 ?  97  GLY   A HA3  1 
ATOM   2188 N N    A PRO   A 1 98  ? 24.045 -5.150  -7.053  0.42 11.28 ?  98  PRO   A N    1 
ATOM   2189 N N    B PRO   A 1 98  ? 24.254 -5.358  -7.206  0.58 11.75 ?  98  PRO   A N    1 
ATOM   2190 C CA   A PRO   A 1 98  ? 23.940 -4.543  -8.383  0.42 11.77 ?  98  PRO   A CA   1 
ATOM   2191 C CA   B PRO   A 1 98  ? 24.267 -4.857  -8.587  0.58 12.90 ?  98  PRO   A CA   1 
ATOM   2192 C C    A PRO   A 1 98  ? 22.823 -3.515  -8.428  0.42 12.09 ?  98  PRO   A C    1 
ATOM   2193 C C    B PRO   A 1 98  ? 23.184 -3.816  -8.818  0.58 13.13 ?  98  PRO   A C    1 
ATOM   2194 O O    A PRO   A 1 98  ? 21.755 -3.700  -7.840  0.42 12.13 ?  98  PRO   A O    1 
ATOM   2195 O O    B PRO   A 1 98  ? 22.071 -3.913  -8.293  0.58 13.58 ?  98  PRO   A O    1 
ATOM   2196 C CB   A PRO   A 1 98  ? 23.644 -5.740  -9.294  0.42 11.55 ?  98  PRO   A CB   1 
ATOM   2197 C CB   B PRO   A 1 98  ? 24.003 -6.116  -9.422  0.58 13.31 ?  98  PRO   A CB   1 
ATOM   2198 C CG   A PRO   A 1 98  ? 23.010 -6.758  -8.387  0.42 11.53 ?  98  PRO   A CG   1 
ATOM   2199 C CG   B PRO   A 1 98  ? 23.271 -7.033  -8.492  0.58 13.59 ?  98  PRO   A CG   1 
ATOM   2200 C CD   A PRO   A 1 98  ? 23.728 -6.588  -7.071  0.42 11.30 ?  98  PRO   A CD   1 
ATOM   2201 C CD   B PRO   A 1 98  ? 23.898 -6.786  -7.143  0.58 12.78 ?  98  PRO   A CD   1 
ATOM   2202 H HA   A PRO   A 1 98  ? 24.776 -4.132  -8.638  0.42 14.12 ?  98  PRO   A HA   1 
ATOM   2203 H HA   B PRO   A 1 98  ? 25.138 -4.491  -8.811  0.58 15.48 ?  98  PRO   A HA   1 
ATOM   2204 H HB2  A PRO   A 1 98  ? 23.031 -5.479  -9.996  0.42 13.86 ?  98  PRO   A HB2  1 
ATOM   2205 H HB2  B PRO   A 1 98  ? 23.454 -5.891  -10.188 0.58 15.97 ?  98  PRO   A HB2  1 
ATOM   2206 H HB3  A PRO   A 1 98  ? 24.473 -6.082  -9.665  0.42 13.86 ?  98  PRO   A HB3  1 
ATOM   2207 H HB3  B PRO   A 1 98  ? 24.845 -6.510  -9.702  0.58 15.97 ?  98  PRO   A HB3  1 
ATOM   2208 H HG2  A PRO   A 1 98  ? 22.064 -6.570  -8.290  0.42 13.83 ?  98  PRO   A HG2  1 
ATOM   2209 H HG2  B PRO   A 1 98  ? 22.328 -6.805  -8.480  0.58 16.31 ?  98  PRO   A HG2  1 
ATOM   2210 H HG3  A PRO   A 1 98  ? 23.152 -7.650  -8.741  0.42 13.83 ?  98  PRO   A HG3  1 
ATOM   2211 H HG3  B PRO   A 1 98  ? 23.400 -7.955  -8.768  0.58 16.31 ?  98  PRO   A HG3  1 
ATOM   2212 H HD2  A PRO   A 1 98  ? 23.143 -6.823  -6.330  0.42 13.56 ?  98  PRO   A HD2  1 
ATOM   2213 H HD2  B PRO   A 1 98  ? 23.254 -6.947  -6.433  0.58 15.33 ?  98  PRO   A HD2  1 
ATOM   2214 H HD3  A PRO   A 1 98  ? 24.548 -7.107  -7.054  0.42 13.56 ?  98  PRO   A HD3  1 
ATOM   2215 H HD3  B PRO   A 1 98  ? 24.694 -7.333  -7.030  0.58 15.33 ?  98  PRO   A HD3  1 
ATOM   2216 N N    A ASN   A 1 99  ? 23.093 -2.413  -9.116  0.42 12.61 ?  99  ASN   A N    1 
ATOM   2217 N N    B ASN   A 1 99  ? 23.523 -2.813  -9.621  0.58 14.29 ?  99  ASN   A N    1 
ATOM   2218 C CA   A ASN   A 1 99  ? 22.105 -1.371  -9.355  0.42 13.33 ?  99  ASN   A CA   1 
ATOM   2219 C CA   B ASN   A 1 99  ? 22.580 -1.784  -10.053 0.58 16.41 ?  99  ASN   A CA   1 
ATOM   2220 C C    A ASN   A 1 99  ? 21.553 -1.565  -10.762 0.42 14.69 ?  99  ASN   A C    1 
ATOM   2221 C C    B ASN   A 1 99  ? 22.085 -2.182  -11.438 0.58 16.79 ?  99  ASN   A C    1 
ATOM   2222 O O    A ASN   A 1 99  ? 22.245 -1.297  -11.751 0.42 15.67 ?  99  ASN   A O    1 
ATOM   2223 O O    B ASN   A 1 99  ? 22.764 -1.954  -12.442 0.58 16.33 ?  99  ASN   A O    1 
ATOM   2224 C CB   A ASN   A 1 99  ? 22.735 0.010   -9.200  0.42 13.77 ?  99  ASN   A CB   1 
ATOM   2225 C CB   B ASN   A 1 99  ? 23.259 -0.421  -10.091 0.58 18.44 ?  99  ASN   A CB   1 
ATOM   2226 C CG   A ASN   A 1 99  ? 21.699 1.124   -9.148  0.42 15.37 ?  99  ASN   A CG   1 
ATOM   2227 C CG   B ASN   A 1 99  ? 22.297 0.704   -10.432 0.58 19.94 ?  99  ASN   A CG   1 
ATOM   2228 O OD1  A ASN   A 1 99  ? 20.680 1.074   -9.838  0.42 16.29 ?  99  ASN   A OD1  1 
ATOM   2229 O OD1  B ASN   A 1 99  ? 21.222 0.477   -10.981 0.58 19.98 ?  99  ASN   A OD1  1 
ATOM   2230 N ND2  A ASN   A 1 99  ? 21.959 2.135   -8.325  0.42 16.27 ?  99  ASN   A ND2  1 
ATOM   2231 N ND2  B ASN   A 1 99  ? 22.682 1.928   -10.105 0.58 21.64 ?  99  ASN   A ND2  1 
ATOM   2232 H H    A ASN   A 1 99  ? 23.865 -2.238  -9.446  0.42 15.14 ?  99  ASN   A H    1 
ATOM   2233 H H    B ASN   A 1 99  ? 24.320 -2.704  -9.928  0.58 17.15 ?  99  ASN   A H    1 
ATOM   2234 H HA   A ASN   A 1 99  ? 21.375 -1.456  -8.721  0.42 16.00 ?  99  ASN   A HA   1 
ATOM   2235 H HA   B ASN   A 1 99  ? 21.825 -1.753  -9.450  0.58 19.70 ?  99  ASN   A HA   1 
ATOM   2236 H HB2  A ASN   A 1 99  ? 23.247 0.033   -8.379  0.42 16.52 ?  99  ASN   A HB2  1 
ATOM   2237 H HB2  B ASN   A 1 99  ? 23.646 -0.238  -9.223  0.58 22.13 ?  99  ASN   A HB2  1 
ATOM   2238 H HB3  A ASN   A 1 99  ? 23.316 0.177   -9.960  0.42 16.52 ?  99  ASN   A HB3  1 
ATOM   2239 H HB3  B ASN   A 1 99  ? 23.951 -0.449  -10.766 0.58 22.13 ?  99  ASN   A HB3  1 
ATOM   2240 H HD21 A ASN   A 1 99  ? 21.407 2.788   -8.257  0.42 19.53 ?  99  ASN   A HD21 1 
ATOM   2241 H HD21 B ASN   A 1 99  ? 22.167 2.595   -10.277 0.58 25.97 ?  99  ASN   A HD21 1 
ATOM   2242 H HD22 A ASN   A 1 99  ? 22.685 2.134   -7.860  0.42 19.53 ?  99  ASN   A HD22 1 
ATOM   2243 H HD22 B ASN   A 1 99  ? 23.439 2.052   -9.727  0.58 25.97 ?  99  ASN   A HD22 1 
ATOM   2244 N N    A VAL   A 1 100 ? 20.307 -2.042  -10.845 0.42 16.04 ?  100 VAL   A N    1 
ATOM   2245 N N    B VAL   A 1 100 ? 20.895 -2.781  -11.492 0.58 19.31 ?  100 VAL   A N    1 
ATOM   2246 C CA   A VAL   A 1 100 ? 19.671 -2.273  -12.140 0.42 18.29 ?  100 VAL   A CA   1 
ATOM   2247 C CA   B VAL   A 1 100 ? 20.354 -3.229  -12.773 0.58 22.31 ?  100 VAL   A CA   1 
ATOM   2248 C C    A VAL   A 1 100 ? 19.585 -0.982  -12.941 0.42 19.84 ?  100 VAL   A C    1 
ATOM   2249 C C    B VAL   A 1 100 ? 20.080 -2.050  -13.698 0.58 23.94 ?  100 VAL   A C    1 
ATOM   2250 O O    A VAL   A 1 100 ? 19.655 -1.003  -14.176 0.42 21.38 ?  100 VAL   A O    1 
ATOM   2251 O O    B VAL   A 1 100 ? 20.101 -2.198  -14.926 0.58 23.94 ?  100 VAL   A O    1 
ATOM   2252 C CB   A VAL   A 1 100 ? 18.290 -2.937  -11.945 0.42 19.36 ?  100 VAL   A CB   1 
ATOM   2253 C CB   B VAL   A 1 100 ? 19.112 -4.111  -12.548 0.58 23.89 ?  100 VAL   A CB   1 
ATOM   2254 C CG1  A VAL   A 1 100 ? 17.586 -3.136  -13.280 0.42 19.95 ?  100 VAL   A CG1  1 
ATOM   2255 C CG1  B VAL   A 1 100 ? 18.393 -4.383  -13.862 0.58 24.20 ?  100 VAL   A CG1  1 
ATOM   2256 C CG2  A VAL   A 1 100 ? 18.443 -4.268  -11.222 0.42 19.28 ?  100 VAL   A CG2  1 
ATOM   2257 C CG2  B VAL   A 1 100 ? 19.520 -5.414  -11.887 0.58 24.66 ?  100 VAL   A CG2  1 
ATOM   2258 H H    A VAL   A 1 100 ? 19.811 -2.238  -10.169 0.42 19.25 ?  100 VAL   A H    1 
ATOM   2259 H H    B VAL   A 1 100 ? 20.392 -2.945  -10.815 0.58 23.17 ?  100 VAL   A H    1 
ATOM   2260 H HA   A VAL   A 1 100 ? 20.216 -2.892  -12.646 0.42 21.95 ?  100 VAL   A HA   1 
ATOM   2261 H HA   B VAL   A 1 100 ? 21.019 -3.786  -13.206 0.58 26.77 ?  100 VAL   A HA   1 
ATOM   2262 H HB   A VAL   A 1 100 ? 17.735 -2.362  -11.397 0.42 23.23 ?  100 VAL   A HB   1 
ATOM   2263 H HB   B VAL   A 1 100 ? 18.497 -3.651  -11.959 0.58 28.67 ?  100 VAL   A HB   1 
ATOM   2264 H HG11 A VAL   A 1 100 ? 16.814 -3.711  -13.147 0.42 23.94 ?  100 VAL   A HG11 1 
ATOM   2265 H HG11 B VAL   A 1 100 ? 17.708 -5.053  -13.708 0.58 29.04 ?  100 VAL   A HG11 1 
ATOM   2266 H HG12 A VAL   A 1 100 ? 17.299 -2.275  -13.620 0.42 23.94 ?  100 VAL   A HG12 1 
ATOM   2267 H HG12 B VAL   A 1 100 ? 17.982 -3.564  -14.179 0.58 29.04 ?  100 VAL   A HG12 1 
ATOM   2268 H HG13 A VAL   A 1 100 ? 18.201 -3.553  -13.903 0.42 23.94 ?  100 VAL   A HG13 1 
ATOM   2269 H HG13 B VAL   A 1 100 ? 19.033 -4.710  -14.513 0.58 29.04 ?  100 VAL   A HG13 1 
ATOM   2270 H HG21 A VAL   A 1 100 ? 17.578 -4.704  -11.176 0.42 23.13 ?  100 VAL   A HG21 1 
ATOM   2271 H HG21 B VAL   A 1 100 ? 18.731 -5.966  -11.765 0.58 29.60 ?  100 VAL   A HG21 1 
ATOM   2272 H HG22 A VAL   A 1 100 ? 19.068 -4.824  -11.714 0.42 23.13 ?  100 VAL   A HG22 1 
ATOM   2273 H HG22 B VAL   A 1 100 ? 20.158 -5.872  -12.458 0.58 29.60 ?  100 VAL   A HG22 1 
ATOM   2274 H HG23 A VAL   A 1 100 ? 18.779 -4.105  -10.327 0.42 23.13 ?  100 VAL   A HG23 1 
ATOM   2275 H HG23 B VAL   A 1 100 ? 19.925 -5.219  -11.028 0.58 29.60 ?  100 VAL   A HG23 1 
ATOM   2276 N N    A ASN   A 1 101 ? 19.436 0.159   -12.263 0.42 20.27 ?  101 ASN   A N    1 
ATOM   2277 N N    B ASN   A 1 101 ? 19.815 -0.868  -13.138 0.58 25.04 ?  101 ASN   A N    1 
ATOM   2278 C CA   A ASN   A 1 101 ? 19.360 1.444   -12.951 0.42 21.44 ?  101 ASN   A CA   1 
ATOM   2279 C CA   B ASN   A 1 101 ? 19.676 0.326   -13.964 0.58 26.36 ?  101 ASN   A CA   1 
ATOM   2280 C C    A ASN   A 1 101 ? 20.704 1.897   -13.509 0.42 22.70 ?  101 ASN   A C    1 
ATOM   2281 C C    B ASN   A 1 101 ? 21.016 0.843   -14.477 0.58 26.96 ?  101 ASN   A C    1 
ATOM   2282 O O    A ASN   A 1 101 ? 20.758 2.930   -14.189 0.42 23.80 ?  101 ASN   A O    1 
ATOM   2283 O O    B ASN   A 1 101 ? 21.026 1.767   -15.297 0.58 27.23 ?  101 ASN   A O    1 
ATOM   2284 C CB   A ASN   A 1 101 ? 18.776 2.503   -12.015 0.42 21.02 ?  101 ASN   A CB   1 
ATOM   2285 C CB   B ASN   A 1 101 ? 18.923 1.418   -13.199 0.58 27.28 ?  101 ASN   A CB   1 
ATOM   2286 C CG   A ASN   A 1 101 ? 17.421 2.103   -11.463 0.42 21.31 ?  101 ASN   A CG   1 
ATOM   2287 C CG   B ASN   A 1 101 ? 17.548 0.964   -12.738 0.58 27.81 ?  101 ASN   A CG   1 
ATOM   2288 O OD1  A ASN   A 1 101 ? 16.560 1.603   -12.193 0.42 22.14 ?  101 ASN   A OD1  1 
ATOM   2289 O OD1  B ASN   A 1 101 ? 16.905 0.132   -13.379 0.58 28.04 ?  101 ASN   A OD1  1 
ATOM   2290 N ND2  A ASN   A 1 101 ? 17.224 2.313   -10.168 0.42 21.06 ?  101 ASN   A ND2  1 
ATOM   2291 N ND2  B ASN   A 1 101 ? 17.092 1.508   -11.620 0.58 27.85 ?  101 ASN   A ND2  1 
ATOM   2292 H H    A ASN   A 1 101 ? 19.372 0.211   -11.406 0.42 24.32 ?  101 ASN   A H    1 
ATOM   2293 H H    B ASN   A 1 101 ? 19.697 -0.738  -12.297 0.58 30.05 ?  101 ASN   A H    1 
ATOM   2294 H HA   A ASN   A 1 101 ? 18.751 1.352   -13.698 0.42 25.73 ?  101 ASN   A HA   1 
ATOM   2295 H HA   B ASN   A 1 101 ? 19.146 0.103   -14.741 0.58 31.63 ?  101 ASN   A HA   1 
ATOM   2296 H HB2  A ASN   A 1 101 ? 19.377 2.636   -11.267 0.42 25.23 ?  101 ASN   A HB2  1 
ATOM   2297 H HB2  B ASN   A 1 101 ? 19.433 1.669   -12.415 0.58 32.73 ?  101 ASN   A HB2  1 
ATOM   2298 H HB3  A ASN   A 1 101 ? 18.665 3.332   -12.506 0.42 25.23 ?  101 ASN   A HB3  1 
ATOM   2299 H HB3  B ASN   A 1 101 ? 18.803 2.187   -13.780 0.58 32.73 ?  101 ASN   A HB3  1 
ATOM   2300 H HD21 A ASN   A 1 101 ? 16.472 2.103   -9.807  0.42 25.27 ?  101 ASN   A HD21 1 
ATOM   2301 H HD21 B ASN   A 1 101 ? 16.318 1.283   -11.321 0.58 33.42 ?  101 ASN   A HD21 1 
ATOM   2302 H HD22 A ASN   A 1 101 ? 17.845 2.667   -9.690  0.42 25.27 ?  101 ASN   A HD22 1 
ATOM   2303 H HD22 B ASN   A 1 101 ? 17.565 2.090   -11.203 0.58 33.42 ?  101 ASN   A HD22 1 
ATOM   2304 N N    A LYS   A 1 102 ? 21.782 1.162   -13.234 0.42 23.98 ?  102 LYS   A N    1 
ATOM   2305 N N    B LYS   A 1 102 ? 22.133 0.278   -14.012 0.58 27.37 ?  102 LYS   A N    1 
ATOM   2306 C CA   A LYS   A 1 102 ? 23.061 1.361   -13.898 0.42 25.02 ?  102 LYS   A CA   1 
ATOM   2307 C CA   B LYS   A 1 102 ? 23.455 0.510   -14.584 0.58 27.30 ?  102 LYS   A CA   1 
ATOM   2308 C C    A LYS   A 1 102 ? 23.366 0.263   -14.905 0.42 24.92 ?  102 LYS   A C    1 
ATOM   2309 C C    B LYS   A 1 102 ? 23.862 -0.588  -15.565 0.58 24.66 ?  102 LYS   A C    1 
ATOM   2310 O O    A LYS   A 1 102 ? 24.440 0.283   -15.516 0.42 25.29 ?  102 LYS   A O    1 
ATOM   2311 O O    B LYS   A 1 102 ? 25.000 -0.587  -16.045 0.58 25.63 ?  102 LYS   A O    1 
ATOM   2312 C CB   A LYS   A 1 102 ? 24.195 1.432   -12.870 0.42 26.21 ?  102 LYS   A CB   1 
ATOM   2313 C CB   B LYS   A 1 102 ? 24.515 0.579   -13.477 0.58 29.68 ?  102 LYS   A CB   1 
ATOM   2314 C CG   A LYS   A 1 102 ? 24.059 2.548   -11.851 0.42 27.22 ?  102 LYS   A CG   1 
ATOM   2315 C CG   B LYS   A 1 102 ? 24.610 1.888   -12.703 0.58 31.93 ?  102 LYS   A CG   1 
ATOM   2316 C CD   A LYS   A 1 102 ? 25.212 2.509   -10.859 0.42 28.06 ?  102 LYS   A CD   1 
ATOM   2317 C CD   B LYS   A 1 102 ? 25.650 1.762   -11.582 0.58 33.81 ?  102 LYS   A CD   1 
ATOM   2318 C CE   A LYS   A 1 102 ? 25.108 3.616   -9.825  0.42 28.65 ?  102 LYS   A CE   1 
ATOM   2319 C CE   B LYS   A 1 102 ? 25.626 2.951   -10.633 0.58 35.02 ?  102 LYS   A CE   1 
ATOM   2320 N NZ   A LYS   A 1 102 ? 26.192 3.515   -8.806  0.42 29.00 ?  102 LYS   A NZ   1 
ATOM   2321 N NZ   B LYS   A 1 102 ? 25.842 2.534   -9.213  0.58 35.86 ?  102 LYS   A NZ   1 
ATOM   2322 H H    A LYS   A 1 102 ? 21.794 0.526   -12.654 0.42 28.78 ?  102 LYS   A H    1 
ATOM   2323 H H    B LYS   A 1 102 ? 22.146 -0.256  -13.337 0.58 32.85 ?  102 LYS   A H    1 
ATOM   2324 H HA   A LYS   A 1 102 ? 23.039 2.202   -14.376 0.42 30.03 ?  102 LYS   A HA   1 
ATOM   2325 H HA   B LYS   A 1 102 ? 23.452 1.366   -15.048 0.58 32.76 ?  102 LYS   A HA   1 
ATOM   2326 H HB2  A LYS   A 1 102 ? 24.227 0.593   -12.384 0.42 31.45 ?  102 LYS   A HB2  1 
ATOM   2327 H HB2  B LYS   A 1 102 ? 24.332 -0.124  -12.836 0.58 35.62 ?  102 LYS   A HB2  1 
ATOM   2328 H HB3  A LYS   A 1 102 ? 25.032 1.567   -13.342 0.42 31.45 ?  102 LYS   A HB3  1 
ATOM   2329 H HB3  B LYS   A 1 102 ? 25.384 0.426   -13.877 0.58 35.62 ?  102 LYS   A HB3  1 
ATOM   2330 H HG2  A LYS   A 1 102 ? 24.073 3.405   -12.306 0.42 32.67 ?  102 LYS   A HG2  1 
ATOM   2331 H HG2  B LYS   A 1 102 ? 24.895 2.598   -13.299 0.58 38.32 ?  102 LYS   A HG2  1 
ATOM   2332 H HG3  A LYS   A 1 102 ? 23.228 2.439   -11.361 0.42 32.67 ?  102 LYS   A HG3  1 
ATOM   2333 H HG3  B LYS   A 1 102 ? 23.751 2.102   -12.311 0.58 38.32 ?  102 LYS   A HG3  1 
ATOM   2334 H HD2  A LYS   A 1 102 ? 25.203 1.657   -10.394 0.42 33.68 ?  102 LYS   A HD2  1 
ATOM   2335 H HD2  B LYS   A 1 102 ? 25.479 0.960   -11.065 0.58 40.57 ?  102 LYS   A HD2  1 
ATOM   2336 H HD3  A LYS   A 1 102 ? 26.048 2.618   -11.339 0.42 33.68 ?  102 LYS   A HD3  1 
ATOM   2337 H HD3  B LYS   A 1 102 ? 26.535 1.713   -11.978 0.58 40.57 ?  102 LYS   A HD3  1 
ATOM   2338 H HE2  A LYS   A 1 102 ? 25.187 4.476   -10.269 0.42 34.38 ?  102 LYS   A HE2  1 
ATOM   2339 H HE2  B LYS   A 1 102 ? 26.336 3.566   -10.876 0.58 42.03 ?  102 LYS   A HE2  1 
ATOM   2340 H HE3  A LYS   A 1 102 ? 24.254 3.551   -9.370  0.42 34.38 ?  102 LYS   A HE3  1 
ATOM   2341 H HE3  B LYS   A 1 102 ? 24.766 3.393   -10.693 0.58 42.03 ?  102 LYS   A HE3  1 
ATOM   2342 H HZ1  A LYS   A 1 102 ? 26.113 4.172   -8.211  0.42 34.80 ?  102 LYS   A HZ1  1 
ATOM   2343 H HZ1  B LYS   A 1 102 ? 25.776 3.240   -8.675  0.58 43.03 ?  102 LYS   A HZ1  1 
ATOM   2344 H HZ2  A LYS   A 1 102 ? 26.138 2.734   -8.383  0.42 34.80 ?  102 LYS   A HZ2  1 
ATOM   2345 H HZ2  B LYS   A 1 102 ? 25.229 1.933   -8.975  0.58 43.03 ?  102 LYS   A HZ2  1 
ATOM   2346 H HZ3  A LYS   A 1 102 ? 26.987 3.576   -9.201  0.42 34.80 ?  102 LYS   A HZ3  1 
ATOM   2347 H HZ3  B LYS   A 1 102 ? 26.650 2.174   -9.120  0.58 43.03 ?  102 LYS   A HZ3  1 
ATOM   2348 N N    A GLY   A 1 103 ? 22.457 -0.694  -15.089 0.42 24.97 ?  103 GLY   A N    1 
ATOM   2349 N N    B GLY   A 1 103 ? 22.973 -1.534  -15.858 0.58 21.70 ?  103 GLY   A N    1 
ATOM   2350 C CA   A GLY   A 1 103 ? 22.689 -1.798  -15.998 0.42 25.06 ?  103 GLY   A CA   1 
ATOM   2351 C CA   B GLY   A 1 103 ? 23.335 -2.674  -16.683 0.58 21.03 ?  103 GLY   A CA   1 
ATOM   2352 C C    A GLY   A 1 103 ? 23.542 -2.910  -15.436 0.42 25.28 ?  103 GLY   A C    1 
ATOM   2353 C C    B GLY   A 1 103 ? 24.089 -3.775  -15.959 0.58 20.70 ?  103 GLY   A C    1 
ATOM   2354 O O    A GLY   A 1 103 ? 24.108 -3.689  -16.208 0.42 26.22 ?  103 GLY   A O    1 
ATOM   2355 O O    B GLY   A 1 103 ? 24.609 -4.690  -16.611 0.58 21.60 ?  103 GLY   A O    1 
ATOM   2356 H H    A GLY   A 1 103 ? 21.696 -0.727  -14.692 0.42 29.97 ?  103 GLY   A H    1 
ATOM   2357 H H    B GLY   A 1 103 ? 22.151 -1.521  -15.598 0.58 26.04 ?  103 GLY   A H    1 
ATOM   2358 H HA2  A GLY   A 1 103 ? 21.834 -2.171  -16.273 0.42 30.07 ?  103 GLY   A HA2  1 
ATOM   2359 H HA2  B GLY   A 1 103 ? 22.519 -3.050  -17.050 0.58 25.23 ?  103 GLY   A HA2  1 
ATOM   2360 H HA3  A GLY   A 1 103 ? 23.137 -1.465  -16.788 0.42 30.07 ?  103 GLY   A HA3  1 
ATOM   2361 H HA3  B GLY   A 1 103 ? 23.866 -2.342  -17.435 0.58 25.23 ?  103 GLY   A HA3  1 
ATOM   2362 N N    A GLU   A 1 104 ? 23.656 -3.011  -14.115 0.42 24.72 ?  104 GLU   A N    1 
ATOM   2363 N N    B GLU   A 1 104 ? 24.155 -3.730  -14.635 0.58 18.98 ?  104 GLU   A N    1 
ATOM   2364 C CA   A GLU   A 1 104 ? 24.542 -3.991  -13.505 0.42 24.29 ?  104 GLU   A CA   1 
ATOM   2365 C CA   B GLU   A 1 104 ? 24.957 -4.684  -13.885 0.58 17.74 ?  104 GLU   A CA   1 
ATOM   2366 C C    A GLU   A 1 104 ? 23.870 -5.356  -13.391 0.42 24.71 ?  104 GLU   A C    1 
ATOM   2367 C C    B GLU   A 1 104 ? 24.203 -5.995  -13.676 0.58 17.56 ?  104 GLU   A C    1 
ATOM   2368 O O    A GLU   A 1 104 ? 22.658 -5.468  -13.186 0.42 24.65 ?  104 GLU   A O    1 
ATOM   2369 O O    B GLU   A 1 104 ? 22.977 -6.022  -13.534 0.58 18.60 ?  104 GLU   A O    1 
ATOM   2370 C CB   A GLU   A 1 104 ? 25.025 -3.489  -12.142 0.42 23.27 ?  104 GLU   A CB   1 
ATOM   2371 C CB   B GLU   A 1 104 ? 25.389 -4.067  -12.554 0.58 17.32 ?  104 GLU   A CB   1 
ATOM   2372 C CG   A GLU   A 1 104 ? 25.942 -2.273  -12.280 0.42 22.68 ?  104 GLU   A CG   1 
ATOM   2373 C CG   B GLU   A 1 104 ? 26.268 -2.831  -12.758 0.58 17.07 ?  104 GLU   A CG   1 
ATOM   2374 C CD   A GLU   A 1 104 ? 26.254 -1.565  -10.969 0.42 21.67 ?  104 GLU   A CD   1 
ATOM   2375 C CD   B GLU   A 1 104 ? 26.671 -2.106  -11.478 0.58 16.97 ?  104 GLU   A CD   1 
ATOM   2376 O OE1  A GLU   A 1 104 ? 25.653 -1.908  -9.929  0.42 20.53 ?  104 GLU   A OE1  1 
ATOM   2377 O OE1  B GLU   A 1 104 ? 26.144 -2.417  -10.394 0.58 16.75 ?  104 GLU   A OE1  1 
ATOM   2378 O OE2  A GLU   A 1 104 ? 27.097 -0.640  -10.989 0.42 21.87 -1 104 GLU   A OE2  1 
ATOM   2379 O OE2  B GLU   A 1 104 ? 27.524 -1.194  -11.570 0.58 17.73 -1 104 GLU   A OE2  1 
ATOM   2380 H H    A GLU   A 1 104 ? 23.237 -2.517  -13.553 0.42 29.66 ?  104 GLU   A H    1 
ATOM   2381 H H    B GLU   A 1 104 ? 23.738 -3.150  -14.160 0.58 22.77 ?  104 GLU   A H    1 
ATOM   2382 H HA   A GLU   A 1 104 ? 25.319 -4.097  -14.071 0.42 29.15 ?  104 GLU   A HA   1 
ATOM   2383 H HA   B GLU   A 1 104 ? 25.757 -4.875  -14.405 0.58 21.29 ?  104 GLU   A HA   1 
ATOM   2384 H HB2  A GLU   A 1 104 ? 24.259 -3.234  -11.606 0.42 27.92 ?  104 GLU   A HB2  1 
ATOM   2385 H HB2  B GLU   A 1 104 ? 24.599 -3.805  -12.063 0.58 20.79 ?  104 GLU   A HB2  1 
ATOM   2386 H HB3  A GLU   A 1 104 ? 25.521 -4.198  -11.701 0.42 27.92 ?  104 GLU   A HB3  1 
ATOM   2387 H HB3  B GLU   A 1 104 ? 25.895 -4.728  -12.063 0.58 20.79 ?  104 GLU   A HB3  1 
ATOM   2388 H HG2  A GLU   A 1 104 ? 26.777 -2.563  -12.683 0.42 27.22 ?  104 GLU   A HG2  1 
ATOM   2389 H HG2  B GLU   A 1 104 ? 27.072 -3.103  -13.228 0.58 20.48 ?  104 GLU   A HG2  1 
ATOM   2390 H HG3  A GLU   A 1 104 ? 25.509 -1.626  -12.858 0.42 27.22 ?  104 GLU   A HG3  1 
ATOM   2391 H HG3  B GLU   A 1 104 ? 25.777 -2.190  -13.295 0.58 20.48 ?  104 GLU   A HG3  1 
ATOM   2392 N N    A ASP   A 1 105 ? 24.686 -6.400  -13.528 0.42 25.21 ?  105 ASP   A N    1 
ATOM   2393 N N    B ASP   A 1 105 ? 24.960 -7.090  -13.670 0.58 17.84 ?  105 ASP   A N    1 
ATOM   2394 C CA   A ASP   A 1 105 ? 24.196 -7.770  -13.620 0.42 25.88 ?  105 ASP   A CA   1 
ATOM   2395 C CA   B ASP   A 1 105 ? 24.396 -8.436  -13.717 0.58 18.44 ?  105 ASP   A CA   1 
ATOM   2396 C C    A ASP   A 1 105 ? 23.510 -8.182  -12.323 0.42 25.11 ?  105 ASP   A C    1 
ATOM   2397 C C    B ASP   A 1 105 ? 23.690 -8.773  -12.406 0.58 16.66 ?  105 ASP   A C    1 
ATOM   2398 O O    A ASP   A 1 105 ? 24.130 -8.187  -11.255 0.42 24.74 ?  105 ASP   A O    1 
ATOM   2399 O O    B ASP   A 1 105 ? 24.306 -8.767  -11.338 0.58 14.53 ?  105 ASP   A O    1 
ATOM   2400 C CB   A ASP   A 1 105 ? 25.382 -8.690  -13.910 0.42 27.23 ?  105 ASP   A CB   1 
ATOM   2401 C CB   B ASP   A 1 105 ? 25.531 -9.422  -13.987 0.58 21.09 ?  105 ASP   A CB   1 
ATOM   2402 C CG   A ASP   A 1 105 ? 24.961 -10.104 -14.231 0.42 28.36 ?  105 ASP   A CG   1 
ATOM   2403 C CG   B ASP   A 1 105 ? 25.086 -10.865 -13.958 0.58 23.37 ?  105 ASP   A CG   1 
ATOM   2404 O OD1  A ASP   A 1 105 ? 23.742 -10.360 -14.311 0.42 28.60 ?  105 ASP   A OD1  1 
ATOM   2405 O OD1  B ASP   A 1 105 ? 23.870 -11.125 -14.046 0.58 23.42 ?  105 ASP   A OD1  1 
ATOM   2406 O OD2  A ASP   A 1 105 ? 25.857 -10.958 -14.411 0.42 28.97 -1 105 ASP   A OD2  1 
ATOM   2407 O OD2  B ASP   A 1 105 ? 25.970 -11.744 -13.847 0.58 25.75 -1 105 ASP   A OD2  1 
ATOM   2408 H H    A ASP   A 1 105 ? 25.542 -6.340  -13.570 0.42 30.25 ?  105 ASP   A H    1 
ATOM   2409 H H    B ASP   A 1 105 ? 25.816 -7.069  -13.645 0.58 21.40 ?  105 ASP   A H    1 
ATOM   2410 H HA   A ASP   A 1 105 ? 23.559 -7.850  -14.348 0.42 31.06 ?  105 ASP   A HA   1 
ATOM   2411 H HA   B ASP   A 1 105 ? 23.749 -8.494  -14.441 0.58 22.12 ?  105 ASP   A HA   1 
ATOM   2412 H HB2  A ASP   A 1 105 ? 25.867 -8.353  -14.681 0.42 32.68 ?  105 ASP   A HB2  1 
ATOM   2413 H HB2  B ASP   A 1 105 ? 25.904 -9.238  -14.863 0.58 25.31 ?  105 ASP   A HB2  1 
ATOM   2414 H HB3  A ASP   A 1 105 ? 25.967 -8.713  -13.136 0.42 32.68 ?  105 ASP   A HB3  1 
ATOM   2415 H HB3  B ASP   A 1 105 ? 26.206 -9.314  -13.305 0.58 25.31 ?  105 ASP   A HB3  1 
ATOM   2416 N N    A ILE   A 1 106 ? 22.225 -8.540  -12.421 0.42 24.61 ?  106 ILE   A N    1 
ATOM   2417 N N    B ILE   A 1 106 ? 22.395 -9.084  -12.488 0.58 17.47 ?  106 ILE   A N    1 
ATOM   2418 C CA   A ILE   A 1 106 ? 21.467 -8.954  -11.246 0.42 24.16 ?  106 ILE   A CA   1 
ATOM   2419 C CA   B ILE   A 1 106 ? 21.634 -9.411  -11.289 0.58 17.78 ?  106 ILE   A CA   1 
ATOM   2420 C C    A ILE   A 1 106 ? 22.002 -10.253 -10.658 0.42 23.34 ?  106 ILE   A C    1 
ATOM   2421 C C    B ILE   A 1 106 ? 22.172 -10.652 -10.600 0.58 16.87 ?  106 ILE   A C    1 
ATOM   2422 O O    A ILE   A 1 106 ? 21.778 -10.529 -9.475  0.42 22.56 ?  106 ILE   A O    1 
ATOM   2423 O O    B ILE   A 1 106 ? 21.961 -10.824 -9.395  0.58 16.56 ?  106 ILE   A O    1 
ATOM   2424 C CB   A ILE   A 1 106 ? 19.961 -9.048  -11.572 0.42 24.96 ?  106 ILE   A CB   1 
ATOM   2425 C CB   B ILE   A 1 106 ? 20.128 -9.537  -11.611 0.58 20.36 ?  106 ILE   A CB   1 
ATOM   2426 C CG1  A ILE   A 1 106 ? 19.123 -9.082  -10.291 0.42 25.50 ?  106 ILE   A CG1  1 
ATOM   2427 C CG1  B ILE   A 1 106 ? 19.293 -9.496  -10.329 0.58 22.07 ?  106 ILE   A CG1  1 
ATOM   2428 C CG2  A ILE   A 1 106 ? 19.666 -10.288 -12.393 0.42 25.16 ?  106 ILE   A CG2  1 
ATOM   2429 C CG2  B ILE   A 1 106 ? 19.846 -10.826 -12.350 0.58 20.94 ?  106 ILE   A CG2  1 
ATOM   2430 C CD1  A ILE   A 1 106 ? 19.258 -7.844  -9.436  0.42 25.98 ?  106 ILE   A CD1  1 
ATOM   2431 C CD1  B ILE   A 1 106 ? 19.505 -8.252  -9.497  0.58 23.15 ?  106 ILE   A CD1  1 
ATOM   2432 H H    A ILE   A 1 106 ? 21.777 -8.546  -13.150 0.42 29.53 ?  106 ILE   A H    1 
ATOM   2433 H H    B ILE   A 1 106 ? 21.945 -9.114  -13.213 0.58 20.97 ?  106 ILE   A H    1 
ATOM   2434 H HA   A ILE   A 1 106 ? 21.579 -8.277  -10.567 0.42 29.00 ?  106 ILE   A HA   1 
ATOM   2435 H HA   B ILE   A 1 106 ? 21.750 -8.688  -10.660 0.58 21.33 ?  106 ILE   A HA   1 
ATOM   2436 H HB   A ILE   A 1 106 ? 19.704 -8.269  -12.088 0.42 29.96 ?  106 ILE   A HB   1 
ATOM   2437 H HB   B ILE   A 1 106 ? 19.873 -8.790  -12.172 0.58 24.43 ?  106 ILE   A HB   1 
ATOM   2438 H HG12 A ILE   A 1 106 ? 18.186 -9.172  -10.532 0.42 30.60 ?  106 ILE   A HG12 1 
ATOM   2439 H HG12 B ILE   A 1 106 ? 18.354 -9.532  -10.568 0.58 26.48 ?  106 ILE   A HG12 1 
ATOM   2440 H HG13 A ILE   A 1 106 ? 19.396 -9.844  -9.757  0.42 30.60 ?  106 ILE   A HG13 1 
ATOM   2441 H HG13 B ILE   A 1 106 ? 19.522 -10.261 -9.780  0.58 26.48 ?  106 ILE   A HG13 1 
ATOM   2442 H HG21 A ILE   A 1 106 ? 18.789 -10.196 -12.798 0.42 30.19 ?  106 ILE   A HG21 1 
ATOM   2443 H HG21 B ILE   A 1 106 ? 18.967 -10.766 -12.751 0.58 25.12 ?  106 ILE   A HG21 1 
ATOM   2444 H HG22 A ILE   A 1 106 ? 20.343 -10.376 -13.079 0.42 30.19 ?  106 ILE   A HG22 1 
ATOM   2445 H HG22 B ILE   A 1 106 ? 20.520 -10.944 -13.033 0.58 25.12 ?  106 ILE   A HG22 1 
ATOM   2446 H HG23 A ILE   A 1 106 ? 19.680 -11.064 -11.810 0.42 30.19 ?  106 ILE   A HG23 1 
ATOM   2447 H HG23 B ILE   A 1 106 ? 19.876 -11.562 -11.719 0.58 25.12 ?  106 ILE   A HG23 1 
ATOM   2448 H HD11 A ILE   A 1 106 ? 18.519 -7.813  -8.811  0.42 31.17 ?  106 ILE   A HD11 1 
ATOM   2449 H HD11 B ILE   A 1 106 ? 18.751 -8.139  -8.901  0.58 27.78 ?  106 ILE   A HD11 1 
ATOM   2450 H HD12 A ILE   A 1 106 ? 20.098 -7.886  -8.952  0.42 31.17 ?  106 ILE   A HD12 1 
ATOM   2451 H HD12 B ILE   A 1 106 ? 20.322 -8.352  -8.980  0.58 27.78 ?  106 ILE   A HD12 1 
ATOM   2452 H HD13 A ILE   A 1 106 ? 19.241 -7.063  -10.010 0.42 31.17 ?  106 ILE   A HD13 1 
ATOM   2453 H HD13 B ILE   A 1 106 ? 19.580 -7.486  -10.087 0.58 27.78 ?  106 ILE   A HD13 1 
ATOM   2454 N N    A GLN   A 1 107 ? 22.717 -11.055 -11.453 0.42 23.69 ?  107 GLN   A N    1 
ATOM   2455 N N    B GLN   A 1 107 ? 22.885 -11.520 -11.329 0.58 17.01 ?  107 GLN   A N    1 
ATOM   2456 C CA   A GLN   A 1 107 ? 23.312 -12.283 -10.938 0.42 24.64 ?  107 GLN   A CA   1 
ATOM   2457 C CA   B GLN   A 1 107 ? 23.521 -12.668 -10.692 0.58 19.51 ?  107 GLN   A CA   1 
ATOM   2458 C C    A GLN   A 1 107 ? 24.301 -12.008 -9.812  0.42 22.38 ?  107 GLN   A C    1 
ATOM   2459 C C    B GLN   A 1 107 ? 24.486 -12.235 -9.594  0.58 17.05 ?  107 GLN   A C    1 
ATOM   2460 O O    A GLN   A 1 107 ? 24.528 -12.884 -8.971  0.42 23.62 ?  107 GLN   A O    1 
ATOM   2461 O O    B GLN   A 1 107 ? 24.733 -13.000 -8.652  0.58 17.51 ?  107 GLN   A O    1 
ATOM   2462 C CB   A GLN   A 1 107 ? 24.006 -13.046 -12.073 0.42 27.91 ?  107 GLN   A CB   1 
ATOM   2463 C CB   B GLN   A 1 107 ? 24.226 -13.536 -11.747 0.58 24.28 ?  107 GLN   A CB   1 
ATOM   2464 C CG   A GLN   A 1 107 ? 23.116 -13.310 -13.281 0.42 31.29 ?  107 GLN   A CG   1 
ATOM   2465 C CG   B GLN   A 1 107 ? 23.327 -13.951 -12.915 0.58 28.96 ?  107 GLN   A CG   1 
ATOM   2466 C CD   A GLN   A 1 107 ? 21.862 -14.085 -12.928 0.42 34.05 ?  107 GLN   A CD   1 
ATOM   2467 C CD   B GLN   A 1 107 ? 22.080 -14.690 -12.466 0.58 32.54 ?  107 GLN   A CD   1 
ATOM   2468 O OE1  A GLN   A 1 107 ? 21.926 -15.138 -12.294 0.42 35.29 ?  107 GLN   A OE1  1 
ATOM   2469 O OE1  B GLN   A 1 107 ? 22.139 -15.562 -11.595 0.58 34.29 ?  107 GLN   A OE1  1 
ATOM   2470 N NE2  A GLN   A 1 107 ? 20.711 -13.562 -13.333 0.42 34.94 ?  107 GLN   A NE2  1 
ATOM   2471 N NE2  B GLN   A 1 107 ? 20.941 -14.343 -13.060 0.58 34.13 ?  107 GLN   A NE2  1 
ATOM   2472 H H    A GLN   A 1 107 ? 22.871 -10.907 -12.284 0.42 28.43 ?  107 GLN   A H    1 
ATOM   2473 H H    B GLN   A 1 107 ? 23.018 -11.465 -12.180 0.58 20.42 ?  107 GLN   A H    1 
ATOM   2474 H HA   A GLN   A 1 107 ? 22.612 -12.853 -10.585 0.42 29.57 ?  107 GLN   A HA   1 
ATOM   2475 H HA   B GLN   A 1 107 ? 22.842 -13.220 -10.285 0.58 23.41 ?  107 GLN   A HA   1 
ATOM   2476 H HB2  A GLN   A 1 107 ? 24.769 -12.531 -12.378 0.42 33.49 ?  107 GLN   A HB2  1 
ATOM   2477 H HB2  B GLN   A 1 107 ? 24.975 -13.046 -12.119 0.58 29.13 ?  107 GLN   A HB2  1 
ATOM   2478 H HB3  A GLN   A 1 107 ? 24.306 -13.906 -11.738 0.42 33.49 ?  107 GLN   A HB3  1 
ATOM   2479 H HB3  B GLN   A 1 107 ? 24.546 -14.353 -11.330 0.58 29.13 ?  107 GLN   A HB3  1 
ATOM   2480 H HG2  A GLN   A 1 107 ? 22.845 -12.465 -13.669 0.42 37.54 ?  107 GLN   A HG2  1 
ATOM   2481 H HG2  B GLN   A 1 107 ? 23.043 -13.160 -13.399 0.58 34.75 ?  107 GLN   A HG2  1 
ATOM   2482 H HG3  A GLN   A 1 107 ? 23.615 -13.828 -13.934 0.42 37.54 ?  107 GLN   A HG3  1 
ATOM   2483 H HG3  B GLN   A 1 107 ? 23.823 -14.537 -13.509 0.58 34.75 ?  107 GLN   A HG3  1 
ATOM   2484 H HE21 A GLN   A 1 107 ? 20.704 -12.824 -13.773 0.42 41.93 ?  107 GLN   A HE21 1 
ATOM   2485 H HE21 B GLN   A 1 107 ? 20.938 -13.728 -13.664 0.58 40.95 ?  107 GLN   A HE21 1 
ATOM   2486 H HE22 A GLN   A 1 107 ? 19.972 -13.965 -13.157 0.42 41.93 ?  107 GLN   A HE22 1 
ATOM   2487 H HE22 B GLN   A 1 107 ? 20.204 -14.730 -12.841 0.58 40.95 ?  107 GLN   A HE22 1 
ATOM   2488 N N    A LEU   A 1 108 ? 24.880 -10.805 -9.768  0.42 18.95 ?  108 LEU   A N    1 
ATOM   2489 N N    B LEU   A 1 108 ? 25.006 -11.008 -9.671  0.58 15.28 ?  108 LEU   A N    1 
ATOM   2490 C CA   A LEU   A 1 108 ? 25.819 -10.445 -8.712  0.42 16.39 ?  108 LEU   A CA   1 
ATOM   2491 C CA   B LEU   A 1 108 ? 25.883 -10.502 -8.626  0.58 14.38 ?  108 LEU   A CA   1 
ATOM   2492 C C    A LEU   A 1 108 ? 25.143 -10.270 -7.357  0.42 14.21 ?  108 LEU   A C    1 
ATOM   2493 C C    B LEU   A 1 108 ? 25.146 -10.253 -7.317  0.58 12.83 ?  108 LEU   A C    1 
ATOM   2494 O O    A LEU   A 1 108 ? 25.843 -10.125 -6.349  0.42 14.54 ?  108 LEU   A O    1 
ATOM   2495 O O    B LEU   A 1 108 ? 25.804 -10.037 -6.293  0.58 13.17 ?  108 LEU   A O    1 
ATOM   2496 C CB   A LEU   A 1 108 ? 26.573 -9.169  -9.101  0.42 16.20 ?  108 LEU   A CB   1 
ATOM   2497 C CB   B LEU   A 1 108 ? 26.599 -9.231  -9.096  0.58 14.69 ?  108 LEU   A CB   1 
ATOM   2498 C CG   A LEU   A 1 108 ? 27.532 -9.332  -10.283 0.42 17.18 ?  108 LEU   A CG   1 
ATOM   2499 C CG   B LEU   A 1 108 ? 27.661 -9.474  -10.173 0.58 16.42 ?  108 LEU   A CG   1 
ATOM   2500 C CD1  A LEU   A 1 108 ? 27.949 -7.979  -10.841 0.42 17.61 ?  108 LEU   A CD1  1 
ATOM   2501 C CD1  B LEU   A 1 108 ? 28.139 -8.168  -10.785 0.58 17.12 ?  108 LEU   A CD1  1 
ATOM   2502 C CD2  A LEU   A 1 108 ? 28.757 -10.133 -9.870  0.42 18.28 ?  108 LEU   A CD2  1 
ATOM   2503 C CD2  B LEU   A 1 108 ? 28.839 -10.244 -9.594  0.58 18.04 ?  108 LEU   A CD2  1 
ATOM   2504 H H    A LEU   A 1 108 ? 24.742 -10.185 -10.343 0.42 22.74 ?  108 LEU   A H    1 
ATOM   2505 H H    B LEU   A 1 108 ? 24.859 -10.461 -10.314 0.58 18.34 ?  108 LEU   A H    1 
ATOM   2506 H HA   A LEU   A 1 108 ? 26.469 -11.158 -8.623  0.42 19.67 ?  108 LEU   A HA   1 
ATOM   2507 H HA   B LEU   A 1 108 ? 26.560 -11.173 -8.451  0.58 17.26 ?  108 LEU   A HA   1 
ATOM   2508 H HB2  A LEU   A 1 108 ? 25.925 -8.488  -9.342  0.42 19.44 ?  108 LEU   A HB2  1 
ATOM   2509 H HB2  B LEU   A 1 108 ? 25.940 -8.622  -9.463  0.58 17.63 ?  108 LEU   A HB2  1 
ATOM   2510 H HB3  A LEU   A 1 108 ? 27.092 -8.873  -8.340  0.42 19.44 ?  108 LEU   A HB3  1 
ATOM   2511 H HB3  B LEU   A 1 108 ? 27.037 -8.826  -8.335  0.58 17.63 ?  108 LEU   A HB3  1 
ATOM   2512 H HG   A LEU   A 1 108 ? 27.083 -9.819  -10.991 0.42 20.62 ?  108 LEU   A HG   1 
ATOM   2513 H HG   B LEU   A 1 108 ? 27.274 -10.010 -10.883 0.58 19.70 ?  108 LEU   A HG   1 
ATOM   2514 H HD11 A LEU   A 1 108 ? 28.507 -8.119  -11.624 0.42 21.13 ?  108 LEU   A HD11 1 
ATOM   2515 H HD11 B LEU   A 1 108 ? 28.803 -8.362  -11.467 0.58 20.54 ?  108 LEU   A HD11 1 
ATOM   2516 H HD12 A LEU   A 1 108 ? 27.156 -7.479  -11.086 0.42 21.13 ?  108 LEU   A HD12 1 
ATOM   2517 H HD12 B LEU   A 1 108 ? 27.383 -7.708  -11.182 0.58 20.54 ?  108 LEU   A HD12 1 
ATOM   2518 H HD13 A LEU   A 1 108 ? 28.449 -7.498  -10.163 0.42 21.13 ?  108 LEU   A HD13 1 
ATOM   2519 H HD13 B LEU   A 1 108 ? 28.533 -7.618  -10.090 0.58 20.54 ?  108 LEU   A HD13 1 
ATOM   2520 H HD21 A LEU   A 1 108 ? 29.388 -10.148 -10.605 0.42 21.93 ?  108 LEU   A HD21 1 
ATOM   2521 H HD21 B LEU   A 1 108 ? 29.570 -10.225 -10.230 0.58 21.64 ?  108 LEU   A HD21 1 
ATOM   2522 H HD22 A LEU   A 1 108 ? 29.162 -9.712  -9.095  0.42 21.93 ?  108 LEU   A HD22 1 
ATOM   2523 H HD22 B LEU   A 1 108 ? 29.111 -9.823  -8.764  0.58 21.64 ?  108 LEU   A HD22 1 
ATOM   2524 H HD23 A LEU   A 1 108 ? 28.484 -11.037 -9.649  0.42 21.93 ?  108 LEU   A HD23 1 
ATOM   2525 H HD23 B LEU   A 1 108 ? 28.567 -11.159 -9.427  0.58 21.64 ?  108 LEU   A HD23 1 
ATOM   2526 N N    . LEU   A 1 109 ? 23.809 -10.301 -7.308  1.00 13.00 ?  109 LEU   A N    1 
ATOM   2527 C CA   . LEU   A 1 109 ? 23.102 -10.159 -6.042  1.00 12.20 ?  109 LEU   A CA   1 
ATOM   2528 C C    . LEU   A 1 109 ? 23.423 -11.315 -5.100  1.00 11.27 ?  109 LEU   A C    1 
ATOM   2529 O O    . LEU   A 1 109 ? 23.538 -11.123 -3.886  1.00 11.83 ?  109 LEU   A O    1 
ATOM   2530 C CB   . LEU   A 1 109 ? 21.597 -10.059 -6.300  1.00 12.96 ?  109 LEU   A CB   1 
ATOM   2531 C CG   . LEU   A 1 109 ? 20.697 -9.780  -5.094  1.00 13.84 ?  109 LEU   A CG   1 
ATOM   2532 C CD1  . LEU   A 1 109 ? 21.132 -8.514  -4.376  1.00 13.60 ?  109 LEU   A CD1  1 
ATOM   2533 C CD2  . LEU   A 1 109 ? 19.234 -9.666  -5.531  1.00 15.05 ?  109 LEU   A CD2  1 
ATOM   2534 H H    A LEU   A 1 109 ? 23.294 -10.410 -7.989  0.42 15.60 ?  109 LEU   A H    1 
ATOM   2535 H H    B LEU   A 1 109 ? 23.306 -10.414 -7.997  0.58 15.60 ?  109 LEU   A H    1 
ATOM   2536 H HA   . LEU   A 1 109 ? 23.391 -9.338  -5.616  1.00 14.63 ?  109 LEU   A HA   1 
ATOM   2537 H HB2  . LEU   A 1 109 ? 21.450 -9.342  -6.935  1.00 15.55 ?  109 LEU   A HB2  1 
ATOM   2538 H HB3  . LEU   A 1 109 ? 21.301 -10.895 -6.684  1.00 15.55 ?  109 LEU   A HB3  1 
ATOM   2539 H HG   . LEU   A 1 109 ? 20.765 -10.513 -4.467  1.00 16.60 ?  109 LEU   A HG   1 
ATOM   2540 H HD11 . LEU   A 1 109 ? 20.460 -8.271  -3.720  1.00 16.32 ?  109 LEU   A HD11 1 
ATOM   2541 H HD12 . LEU   A 1 109 ? 21.982 -8.669  -3.939  1.00 16.32 ?  109 LEU   A HD12 1 
ATOM   2542 H HD13 . LEU   A 1 109 ? 21.224 -7.794  -5.028  1.00 16.32 ?  109 LEU   A HD13 1 
ATOM   2543 H HD21 . LEU   A 1 109 ? 18.706 -9.322  -4.790  1.00 18.07 ?  109 LEU   A HD21 1 
ATOM   2544 H HD22 . LEU   A 1 109 ? 19.170 -9.061  -6.286  1.00 18.07 ?  109 LEU   A HD22 1 
ATOM   2545 H HD23 . LEU   A 1 109 ? 18.908 -10.545 -5.784  1.00 18.07 ?  109 LEU   A HD23 1 
ATOM   2546 N N    . LYS   A 1 110 ? 23.578 -12.529 -5.636  1.00 11.43 ?  110 LYS   A N    1 
ATOM   2547 C CA   . LYS   A 1 110 ? 23.942 -13.644 -4.771  1.00 11.60 ?  110 LYS   A CA   1 
ATOM   2548 C C    . LYS   A 1 110 ? 25.321 -13.417 -4.160  1.00 11.01 ?  110 LYS   A C    1 
ATOM   2549 O O    . LYS   A 1 110 ? 25.516 -13.620 -2.957  1.00 11.26 ?  110 LYS   A O    1 
ATOM   2550 C CB   . LYS   A 1 110 ? 23.866 -14.967 -5.534  1.00 13.16 ?  110 LYS   A CB   1 
ATOM   2551 C CG   . LYS   A 1 110 ? 24.054 -16.180 -4.626  1.00 13.02 ?  110 LYS   A CG   1 
ATOM   2552 C CD   . LYS   A 1 110 ? 23.793 -17.498 -5.340  1.00 13.07 ?  110 LYS   A CD   1 
ATOM   2553 C CE   . LYS   A 1 110 ? 23.913 -18.692 -4.404  1.00 14.37 ?  110 LYS   A CE   1 
ATOM   2554 N NZ   . LYS   A 1 110 ? 22.743 -18.817 -3.499  1.00 14.65 ?  110 LYS   A NZ   1 
ATOM   2555 H H    . LYS   A 1 110 ? 23.479 -12.726 -6.466  1.00 13.72 ?  110 LYS   A H    1 
ATOM   2556 H HA   . LYS   A 1 110 ? 23.300 -13.691 -4.043  1.00 13.92 ?  110 LYS   A HA   1 
ATOM   2557 H HB2  . LYS   A 1 110 ? 22.998 -15.041 -5.958  1.00 15.79 ?  110 LYS   A HB2  1 
ATOM   2558 H HB3  . LYS   A 1 110 ? 24.568 -14.985 -6.203  1.00 15.79 ?  110 LYS   A HB3  1 
ATOM   2559 H HG2  . LYS   A 1 110 ? 24.964 -16.189 -4.293  1.00 15.63 ?  110 LYS   A HG2  1 
ATOM   2560 H HG3  . LYS   A 1 110 ? 23.431 -16.112 -3.882  1.00 15.63 ?  110 LYS   A HG3  1 
ATOM   2561 H HD2  . LYS   A 1 110 ? 22.896 -17.491 -5.702  1.00 15.69 ?  110 LYS   A HD2  1 
ATOM   2562 H HD3  . LYS   A 1 110 ? 24.444 -17.604 -6.050  1.00 15.69 ?  110 LYS   A HD3  1 
ATOM   2563 H HE2  . LYS   A 1 110 ? 23.979 -19.503 -4.930  1.00 17.25 ?  110 LYS   A HE2  1 
ATOM   2564 H HE3  . LYS   A 1 110 ? 24.711 -18.587 -3.855  1.00 17.25 ?  110 LYS   A HE3  1 
ATOM   2565 H HZ1  . LYS   A 1 110 ? 22.841 -19.521 -2.965  1.00 17.59 ?  110 LYS   A HZ1  1 
ATOM   2566 H HZ2  . LYS   A 1 110 ? 22.664 -18.083 -2.998  1.00 17.59 ?  110 LYS   A HZ2  1 
ATOM   2567 H HZ3  . LYS   A 1 110 ? 21.998 -18.917 -3.977  1.00 17.59 ?  110 LYS   A HZ3  1 
ATOM   2568 N N    . SER   A 1 111 ? 26.284 -12.974 -4.971  1.00 11.34 ?  111 SER   A N    1 
ATOM   2569 C CA   . SER   A 1 111 ? 27.608 -12.665 -4.441  1.00 11.46 ?  111 SER   A CA   1 
ATOM   2570 C C    . SER   A 1 111 ? 27.529 -11.618 -3.337  1.00 10.94 ?  111 SER   A C    1 
ATOM   2571 O O    . SER   A 1 111 ? 28.220 -11.721 -2.318  1.00 11.36 ?  111 SER   A O    1 
ATOM   2572 C CB   . SER   A 1 111 ? 28.512 -12.173 -5.567  1.00 12.86 ?  111 SER   A CB   1 
ATOM   2573 O OG   . SER   A 1 111 ? 28.574 -13.137 -6.606  1.00 14.82 ?  111 SER   A OG   1 
ATOM   2574 H H    . SER   A 1 111 ? 26.187 -12.848 -5.816  1.00 13.61 ?  111 SER   A H    1 
ATOM   2575 H HA   . SER   A 1 111 ? 27.994 -13.475 -4.073  1.00 13.76 ?  111 SER   A HA   1 
ATOM   2576 H HB2  . SER   A 1 111 ? 28.150 -11.354 -5.933  1.00 15.43 ?  111 SER   A HB2  1 
ATOM   2577 H HB3  . SER   A 1 111 ? 29.401 -12.022 -5.214  1.00 15.43 ?  111 SER   A HB3  1 
ATOM   2578 H HG   . SER   A 1 111 ? 29.091 -12.867 -7.219  1.00 17.78 ?  111 SER   A HG   1 
ATOM   2579 N N    . ALA   A 1 112 ? 26.691 -10.599 -3.526  1.00 10.70 ?  112 ALA   A N    1 
ATOM   2580 C CA   . ALA   A 1 112 ? 26.527 -9.568  -2.505  1.00 10.39 ?  112 ALA   A CA   1 
ATOM   2581 C C    . ALA   A 1 112 ? 26.041 -10.168 -1.186  1.00 10.17 ?  112 ALA   A C    1 
ATOM   2582 O O    . ALA   A 1 112 ? 26.589 -9.878  -0.117  1.00 10.66 ?  112 ALA   A O    1 
ATOM   2583 C CB   . ALA   A 1 112 ? 25.563 -8.489  -3.004  1.00 11.44 ?  112 ALA   A CB   1 
ATOM   2584 H H    . ALA   A 1 112 ? 26.215 -10.478 -4.231  1.00 12.84 ?  112 ALA   A H    1 
ATOM   2585 H HA   . ALA   A 1 112 ? 27.384 -9.145  -2.341  1.00 12.47 ?  112 ALA   A HA   1 
ATOM   2586 H HB1  . ALA   A 1 112 ? 25.472 -7.802  -2.317  1.00 13.72 ?  112 ALA   A HB1  1 
ATOM   2587 H HB2  . ALA   A 1 112 ? 25.916 -8.094  -3.814  1.00 13.72 ?  112 ALA   A HB2  1 
ATOM   2588 H HB3  . ALA   A 1 112 ? 24.697 -8.889  -3.179  1.00 13.72 ?  112 ALA   A HB3  1 
ATOM   2589 N N    A TYR   A 1 113 ? 25.001 -11.004 -1.245  0.42 10.65 ?  113 TYR   A N    1 
ATOM   2590 N N    B TYR   A 1 113 ? 24.995 -10.998 -1.238  0.58 10.56 ?  113 TYR   A N    1 
ATOM   2591 C CA   A TYR   A 1 113 ? 24.474 -11.609 -0.027  0.42 10.40 ?  113 TYR   A CA   1 
ATOM   2592 C CA   B TYR   A 1 113 ? 24.484 -11.597 -0.009  0.58 9.98  ?  113 TYR   A CA   1 
ATOM   2593 C C    A TYR   A 1 113 ? 25.468 -12.574 0.619   0.42 10.41 ?  113 TYR   A C    1 
ATOM   2594 C C    B TYR   A 1 113 ? 25.487 -12.558 0.628   0.58 10.06 ?  113 TYR   A C    1 
ATOM   2595 O O    A TYR   A 1 113 ? 25.415 -12.782 1.836   0.42 10.88 ?  113 TYR   A O    1 
ATOM   2596 O O    B TYR   A 1 113 ? 25.459 -12.750 1.848   0.58 10.48 ?  113 TYR   A O    1 
ATOM   2597 C CB   A TYR   A 1 113 ? 23.147 -12.318 -0.321  0.42 10.86 ?  113 TYR   A CB   1 
ATOM   2598 C CB   B TYR   A 1 113 ? 23.152 -12.309 -0.268  0.58 10.50 ?  113 TYR   A CB   1 
ATOM   2599 C CG   A TYR   A 1 113 ? 21.926 -11.419 -0.238  0.42 11.15 ?  113 TYR   A CG   1 
ATOM   2600 C CG   B TYR   A 1 113 ? 21.956 -11.382 -0.277  0.58 10.41 ?  113 TYR   A CG   1 
ATOM   2601 C CD1  A TYR   A 1 113 ? 21.568 -10.810 0.958   0.42 11.83 ?  113 TYR   A CD1  1 
ATOM   2602 C CD1  B TYR   A 1 113 ? 21.589 -10.673 0.861   0.58 10.83 ?  113 TYR   A CD1  1 
ATOM   2603 C CD2  A TYR   A 1 113 ? 21.120 -11.199 -1.349  0.42 11.46 ?  113 TYR   A CD2  1 
ATOM   2604 C CD2  B TYR   A 1 113 ? 21.186 -11.223 -1.420  0.58 11.14 ?  113 TYR   A CD2  1 
ATOM   2605 C CE1  A TYR   A 1 113 ? 20.447 -10.005 1.045   0.42 12.21 ?  113 TYR   A CE1  1 
ATOM   2606 C CE1  B TYR   A 1 113 ? 20.485 -9.841  0.859   0.58 11.41 ?  113 TYR   A CE1  1 
ATOM   2607 C CE2  A TYR   A 1 113 ? 19.985 -10.392 -1.269  0.42 11.80 ?  113 TYR   A CE2  1 
ATOM   2608 C CE2  B TYR   A 1 113 ? 20.069 -10.394 -1.430  0.58 11.94 ?  113 TYR   A CE2  1 
ATOM   2609 C CZ   A TYR   A 1 113 ? 19.665 -9.794  -0.069  0.42 11.80 ?  113 TYR   A CZ   1 
ATOM   2610 C CZ   B TYR   A 1 113 ? 19.733 -9.700  -0.289  0.58 12.28 ?  113 TYR   A CZ   1 
ATOM   2611 O OH   A TYR   A 1 113 ? 18.546 -8.992  0.032   0.42 11.29 ?  113 TYR   A OH   1 
ATOM   2612 O OH   B TYR   A 1 113 ? 18.634 -8.868  -0.293  0.58 13.49 ?  113 TYR   A OH   1 
ATOM   2613 H H    A TYR   A 1 113 ? 24.596 -11.231 -1.967  0.42 12.78 ?  113 TYR   A H    1 
ATOM   2614 H H    B TYR   A 1 113 ? 24.582 -11.228 -1.955  0.58 12.68 ?  113 TYR   A H    1 
ATOM   2615 H HA   A TYR   A 1 113 ? 24.296 -10.905 0.612   0.42 12.47 ?  113 TYR   A HA   1 
ATOM   2616 H HA   B TYR   A 1 113 ? 24.322 -10.891 0.631   0.58 11.98 ?  113 TYR   A HA   1 
ATOM   2617 H HB2  A TYR   A 1 113 ? 23.183 -12.683 -1.220  0.42 13.03 ?  113 TYR   A HB2  1 
ATOM   2618 H HB2  B TYR   A 1 113 ? 23.193 -12.746 -1.134  0.58 12.60 ?  113 TYR   A HB2  1 
ATOM   2619 H HB3  A TYR   A 1 113 ? 23.030 -13.035 0.319   0.42 13.03 ?  113 TYR   A HB3  1 
ATOM   2620 H HB3  B TYR   A 1 113 ? 23.009 -12.971 0.426   0.58 12.60 ?  113 TYR   A HB3  1 
ATOM   2621 H HD1  A TYR   A 1 113 ? 22.095 -10.950 1.712   0.42 14.20 ?  113 TYR   A HD1  1 
ATOM   2622 H HD1  B TYR   A 1 113 ? 22.095 -10.773 1.639   0.58 13.00 ?  113 TYR   A HD1  1 
ATOM   2623 H HD2  A TYR   A 1 113 ? 21.336 -11.604 -2.159  0.42 13.75 ?  113 TYR   A HD2  1 
ATOM   2624 H HD2  B TYR   A 1 113 ? 21.409 -11.695 -2.189  0.58 13.36 ?  113 TYR   A HD2  1 
ATOM   2625 H HE1  A TYR   A 1 113 ? 20.225 -9.605  1.854   0.42 14.66 ?  113 TYR   A HE1  1 
ATOM   2626 H HE1  B TYR   A 1 113 ? 20.257 -9.376  1.632   0.58 13.69 ?  113 TYR   A HE1  1 
ATOM   2627 H HE2  A TYR   A 1 113 ? 19.453 -10.252 -2.021  0.42 14.16 ?  113 TYR   A HE2  1 
ATOM   2628 H HE2  B TYR   A 1 113 ? 19.563 -10.295 -2.203  0.58 14.32 ?  113 TYR   A HE2  1 
ATOM   2629 H HH   A TYR   A 1 113 ? 18.093 -9.040  -0.677  0.42 13.55 ?  113 TYR   A HH   1 
ATOM   2630 H HH   B TYR   A 1 113 ? 18.264 -8.885  -1.051  0.58 16.19 ?  113 TYR   A HH   1 
ATOM   2631 N N    . GLU   A 1 114 ? 26.374 -13.177 -0.162  1.00 10.40 ?  114 GLU   A N    1 
ATOM   2632 C CA   . GLU   A 1 114 ? 27.369 -14.073 0.432   1.00 10.86 ?  114 GLU   A CA   1 
ATOM   2633 C C    . GLU   A 1 114 ? 28.214 -13.366 1.486   1.00 10.35 ?  114 GLU   A C    1 
ATOM   2634 O O    . GLU   A 1 114 ? 28.691 -14.000 2.433   1.00 10.69 ?  114 GLU   A O    1 
ATOM   2635 C CB   . GLU   A 1 114 ? 28.245 -14.715 -0.648  1.00 10.99 ?  114 GLU   A CB   1 
ATOM   2636 C CG   . GLU   A 1 114 ? 27.487 -15.763 -1.444  1.00 11.71 ?  114 GLU   A CG   1 
ATOM   2637 C CD   . GLU   A 1 114 ? 28.222 -16.307 -2.668  1.00 12.04 ?  114 GLU   A CD   1 
ATOM   2638 O OE1  . GLU   A 1 114 ? 29.183 -15.673 -3.166  1.00 12.04 ?  114 GLU   A OE1  1 
ATOM   2639 O OE2  . GLU   A 1 114 ? 27.805 -17.385 -3.157  1.00 13.44 -1 114 GLU   A OE2  1 
ATOM   2640 H H    A GLU   A 1 114 ? 26.425 -13.089 -1.020  0.42 12.48 ?  114 GLU   A H    1 
ATOM   2641 H H    B GLU   A 1 114 ? 26.416 -13.095 -1.021  0.58 12.48 ?  114 GLU   A H    1 
ATOM   2642 H HA   . GLU   A 1 114 ? 26.898 -14.788 0.878   1.00 13.04 ?  114 GLU   A HA   1 
ATOM   2643 H HB2  . GLU   A 1 114 ? 28.551 -14.035 -1.267  1.00 13.18 ?  114 GLU   A HB2  1 
ATOM   2644 H HB3  . GLU   A 1 114 ? 29.000 -15.154 -0.230  1.00 13.18 ?  114 GLU   A HB3  1 
ATOM   2645 H HG2  . GLU   A 1 114 ? 27.302 -16.516 -0.868  1.00 14.05 ?  114 GLU   A HG2  1 
ATOM   2646 H HG3  . GLU   A 1 114 ? 26.652 -15.373 -1.751  1.00 14.05 ?  114 GLU   A HG3  1 
ATOM   2647 N N    . ASN   A 1 115 ? 28.406 -12.050 1.352   1.00 10.08 ?  115 ASN   A N    1 
ATOM   2648 C CA   . ASN   A 1 115 ? 29.178 -11.323 2.357   1.00 10.59 ?  115 ASN   A CA   1 
ATOM   2649 C C    . ASN   A 1 115 ? 28.558 -11.446 3.745   1.00 10.24 ?  115 ASN   A C    1 
ATOM   2650 O O    . ASN   A 1 115 ? 29.265 -11.365 4.754   1.00 10.74 ?  115 ASN   A O    1 
ATOM   2651 C CB   . ASN   A 1 115 ? 29.294 -9.852  1.966   1.00 11.08 ?  115 ASN   A CB   1 
ATOM   2652 C CG   . ASN   A 1 115 ? 30.094 -9.655  0.705   1.00 11.46 ?  115 ASN   A CG   1 
ATOM   2653 O OD1  . ASN   A 1 115 ? 31.306 -9.814  0.714   1.00 14.77 ?  115 ASN   A OD1  1 
ATOM   2654 N ND2  . ASN   A 1 115 ? 29.430 -9.327  -0.387  1.00 10.87 ?  115 ASN   A ND2  1 
ATOM   2655 H H    . ASN   A 1 115 ? 28.103 -11.562 0.708   1.00 12.10 ?  115 ASN   A H    1 
ATOM   2656 H HA   . ASN   A 1 115 ? 30.071 -11.695 2.395   1.00 12.71 ?  115 ASN   A HA   1 
ATOM   2657 H HB2  . ASN   A 1 115 ? 28.403 -9.489  1.829   1.00 13.29 ?  115 ASN   A HB2  1 
ATOM   2658 H HB3  . ASN   A 1 115 ? 29.735 -9.369  2.688   1.00 13.29 ?  115 ASN   A HB3  1 
ATOM   2659 H HD21 . ASN   A 1 115 ? 29.856 -9.202  -1.124  1.00 13.05 ?  115 ASN   A HD21 1 
ATOM   2660 H HD22 . ASN   A 1 115 ? 28.577 -9.237  -0.362  1.00 13.05 ?  115 ASN   A HD22 1 
ATOM   2661 N N    . PHE   A 1 116 ? 27.230 -11.608 3.824   1.00 10.31 ?  116 PHE   A N    1 
ATOM   2662 C CA   . PHE   A 1 116 ? 26.575 -11.699 5.126   1.00 10.25 ?  116 PHE   A CA   1 
ATOM   2663 C C    . PHE   A 1 116 ? 27.045 -12.929 5.904   1.00 10.81 ?  116 PHE   A C    1 
ATOM   2664 O O    . PHE   A 1 116 ? 26.980 -12.942 7.135   1.00 11.21 ?  116 PHE   A O    1 
ATOM   2665 C CB   . PHE   A 1 116 ? 25.047 -11.826 4.983   1.00 10.38 ?  116 PHE   A CB   1 
ATOM   2666 C CG   . PHE   A 1 116 ? 24.297 -10.588 4.485   1.00 10.18 ?  116 PHE   A CG   1 
ATOM   2667 C CD1  . PHE   A 1 116 ? 24.864 -9.588  3.711   1.00 10.88 ?  116 PHE   A CD1  1 
ATOM   2668 C CD2  . PHE   A 1 116 ? 22.944 -10.472 4.804   1.00 11.41 ?  116 PHE   A CD2  1 
ATOM   2669 C CE1  . PHE   A 1 116 ? 24.092 -8.519  3.264   1.00 11.16 ?  116 PHE   A CE1  1 
ATOM   2670 C CE2  . PHE   A 1 116 ? 22.170 -9.410  4.370   1.00 11.54 ?  116 PHE   A CE2  1 
ATOM   2671 C CZ   . PHE   A 1 116 ? 22.737 -8.428  3.600   1.00 10.92 ?  116 PHE   A CZ   1 
ATOM   2672 H H    . PHE   A 1 116 ? 26.698 -11.661 3.148   1.00 12.37 ?  116 PHE   A H    1 
ATOM   2673 H HA   . PHE   A 1 116 ? 26.774 -10.908 5.648   1.00 12.30 ?  116 PHE   A HA   1 
ATOM   2674 H HB2  . PHE   A 1 116 ? 24.864 -12.551 4.362   1.00 12.46 ?  116 PHE   A HB2  1 
ATOM   2675 H HB3  . PHE   A 1 116 ? 24.686 -12.063 5.856   1.00 12.46 ?  116 PHE   A HB3  1 
ATOM   2676 H HD1  . PHE   A 1 116 ? 25.760 -9.654  3.481   1.00 13.06 ?  116 PHE   A HD1  1 
ATOM   2677 H HD2  . PHE   A 1 116 ? 22.541 -11.147 5.317   1.00 13.69 ?  116 PHE   A HD2  1 
ATOM   2678 H HE1  . PHE   A 1 116 ? 24.492 -7.852  2.754   1.00 13.39 ?  116 PHE   A HE1  1 
ATOM   2679 H HE2  . PHE   A 1 116 ? 21.268 -9.363  4.603   1.00 13.85 ?  116 PHE   A HE2  1 
ATOM   2680 H HZ   . PHE   A 1 116 ? 22.231 -7.701  3.316   1.00 13.10 ?  116 PHE   A HZ   1 
ATOM   2681 N N    . ASN   A 1 117 ? 27.490 -13.977 5.209   1.00 10.53 ?  117 ASN   A N    1 
ATOM   2682 C CA   . ASN   A 1 117 ? 27.859 -15.215 5.888   1.00 11.15 ?  117 ASN   A CA   1 
ATOM   2683 C C    . ASN   A 1 117 ? 29.123 -15.092 6.719   1.00 11.45 ?  117 ASN   A C    1 
ATOM   2684 O O    . ASN   A 1 117 ? 29.413 -15.995 7.509   1.00 12.37 ?  117 ASN   A O    1 
ATOM   2685 C CB   . ASN   A 1 117 ? 27.989 -16.336 4.868   1.00 11.13 ?  117 ASN   A CB   1 
ATOM   2686 C CG   . ASN   A 1 117 ? 26.640 -16.736 4.324   1.00 11.38 ?  117 ASN   A CG   1 
ATOM   2687 O OD1  . ASN   A 1 117 ? 25.664 -16.771 5.064   1.00 12.26 ?  117 ASN   A OD1  1 
ATOM   2688 N ND2  . ASN   A 1 117 ? 26.563 -17.000 3.039   1.00 11.30 ?  117 ASN   A ND2  1 
ATOM   2689 H H    . ASN   A 1 117 ? 27.571 -13.999 4.352   1.00 12.64 ?  117 ASN   A H    1 
ATOM   2690 H HA   . ASN   A 1 117 ? 27.136 -15.455 6.491   1.00 13.38 ?  117 ASN   A HA   1 
ATOM   2691 H HB2  . ASN   A 1 117 ? 28.540 -16.030 4.127   1.00 13.36 ?  117 ASN   A HB2  1 
ATOM   2692 H HB3  . ASN   A 1 117 ? 28.390 -17.106 5.291   1.00 13.36 ?  117 ASN   A HB3  1 
ATOM   2693 H HD21 . ASN   A 1 117 ? 25.812 -17.220 2.700   1.00 13.56 ?  117 ASN   A HD21 1 
ATOM   2694 H HD22 . ASN   A 1 117 ? 27.269 -16.945 2.554   1.00 13.56 ?  117 ASN   A HD22 1 
ATOM   2695 N N    . GLN   A 1 118 ? 29.848 -13.986 6.594   1.00 11.29 ?  118 GLN   A N    1 
ATOM   2696 C CA   . GLN   A 1 118 ? 31.018 -13.743 7.425   1.00 12.04 ?  118 GLN   A CA   1 
ATOM   2697 C C    . GLN   A 1 118 ? 30.669 -13.169 8.790   1.00 12.30 ?  118 GLN   A C    1 
ATOM   2698 O O    . GLN   A 1 118 ? 31.583 -12.882 9.572   1.00 13.47 ?  118 GLN   A O    1 
ATOM   2699 C CB   . GLN   A 1 118 ? 32.014 -12.843 6.691   1.00 12.04 ?  118 GLN   A CB   1 
ATOM   2700 C CG   . GLN   A 1 118 ? 32.493 -13.430 5.367   1.00 12.29 ?  118 GLN   A CG   1 
ATOM   2701 C CD   . GLN   A 1 118 ? 33.327 -14.683 5.545   1.00 12.82 ?  118 GLN   A CD   1 
ATOM   2702 O OE1  . GLN   A 1 118 ? 34.188 -14.752 6.430   1.00 13.80 ?  118 GLN   A OE1  1 
ATOM   2703 N NE2  . GLN   A 1 118 ? 33.082 -15.686 4.700   1.00 12.87 ?  118 GLN   A NE2  1 
ATOM   2704 H H    . GLN   A 1 118 ? 29.672 -13.345 6.040   1.00 13.54 ?  118 GLN   A H    1 
ATOM   2705 H HA   . GLN   A 1 118 ? 31.452 -14.597 7.577   1.00 14.45 ?  118 GLN   A HA   1 
ATOM   2706 H HB2  . GLN   A 1 118 ? 31.593 -11.993 6.505   1.00 14.45 ?  118 GLN   A HB2  1 
ATOM   2707 H HB3  . GLN   A 1 118 ? 32.791 -12.713 7.258   1.00 14.45 ?  118 GLN   A HB3  1 
ATOM   2708 H HG2  . GLN   A 1 118 ? 31.727 -13.657 4.819   1.00 14.75 ?  118 GLN   A HG2  1 
ATOM   2709 H HG3  . GLN   A 1 118 ? 33.044 -12.774 4.910   1.00 14.75 ?  118 GLN   A HG3  1 
ATOM   2710 H HE21 . GLN   A 1 118 ? 32.468 -15.599 4.097   1.00 15.45 ?  118 GLN   A HE21 1 
ATOM   2711 H HE22 . GLN   A 1 118 ? 33.518 -16.422 4.760   1.00 15.45 ?  118 GLN   A HE22 1 
ATOM   2712 N N    . HIS   A 1 119 ? 29.379 -13.005 9.092   1.00 11.83 ?  119 HIS   A N    1 
ATOM   2713 C CA   . HIS   A 1 119 ? 28.922 -12.400 10.337  1.00 12.08 ?  119 HIS   A CA   1 
ATOM   2714 C C    . HIS   A 1 119 ? 27.787 -13.227 10.912  1.00 12.65 ?  119 HIS   A C    1 
ATOM   2715 O O    . HIS   A 1 119 ? 26.843 -13.572 10.197  1.00 13.04 ?  119 HIS   A O    1 
ATOM   2716 C CB   . HIS   A 1 119 ? 28.459 -10.974 10.063  1.00 12.45 ?  119 HIS   A CB   1 
ATOM   2717 C CG   . HIS   A 1 119 ? 29.535 -10.163 9.440   1.00 14.01 ?  119 HIS   A CG   1 
ATOM   2718 N ND1  . HIS   A 1 119 ? 30.507 -9.544  10.191  1.00 16.34 ?  119 HIS   A ND1  1 
ATOM   2719 C CD2  . HIS   A 1 119 ? 29.874 -9.982  8.144   1.00 15.02 ?  119 HIS   A CD2  1 
ATOM   2720 C CE1  . HIS   A 1 119 ? 31.373 -8.966  9.378   1.00 16.85 ?  119 HIS   A CE1  1 
ATOM   2721 N NE2  . HIS   A 1 119 ? 31.021 -9.229  8.132   1.00 16.45 ?  119 HIS   A NE2  1 
ATOM   2722 H H    . HIS   A 1 119 ? 28.727 -13.266 8.583   1.00 14.20 ?  119 HIS   A H    1 
ATOM   2723 H HA   . HIS   A 1 119 ? 29.644 -12.382 10.977  1.00 14.50 ?  119 HIS   A HA   1 
ATOM   2724 H HB2  . HIS   A 1 119 ? 27.698 -10.994 9.459   1.00 14.94 ?  119 HIS   A HB2  1 
ATOM   2725 H HB3  . HIS   A 1 119 ? 28.208 -10.556 10.902  1.00 14.94 ?  119 HIS   A HB3  1 
ATOM   2726 H HD2  . HIS   A 1 119 ? 29.419 -10.308 7.399   1.00 18.03 ?  119 HIS   A HD2  1 
ATOM   2727 H HE1  . HIS   A 1 119 ? 32.108 -8.458  9.636   1.00 20.22 ?  119 HIS   A HE1  1 
ATOM   2728 H HE2  . HIS   A 1 119 ? 31.426 -8.943  7.426   1.00 19.74 ?  119 HIS   A HE2  1 
ATOM   2729 N N    . GLU   A 1 120 ? 27.876 -13.528 12.208  1.00 13.03 ?  120 GLU   A N    1 
ATOM   2730 C CA   . GLU   A 1 120 ? 26.924 -14.453 12.823  1.00 15.20 ?  120 GLU   A CA   1 
ATOM   2731 C C    . GLU   A 1 120 ? 25.506 -13.893 12.862  1.00 14.13 ?  120 GLU   A C    1 
ATOM   2732 O O    . GLU   A 1 120 ? 24.532 -14.654 12.750  1.00 14.58 ?  120 GLU   A O    1 
ATOM   2733 C CB   . GLU   A 1 120 ? 27.384 -14.811 14.238  1.00 19.38 ?  120 GLU   A CB   1 
ATOM   2734 C CG   . GLU   A 1 120 ? 28.587 -15.733 14.286  1.00 25.44 ?  120 GLU   A CG   1 
ATOM   2735 C CD   . GLU   A 1 120 ? 28.663 -16.511 15.579  1.00 30.30 ?  120 GLU   A CD   1 
ATOM   2736 O OE1  . GLU   A 1 120 ? 28.305 -15.942 16.633  1.00 33.01 ?  120 GLU   A OE1  1 
ATOM   2737 O OE2  . GLU   A 1 120 ? 29.071 -17.692 15.540  1.00 34.69 -1 120 GLU   A OE2  1 
ATOM   2738 H H    . GLU   A 1 120 ? 28.479 -13.225 12.747  1.00 15.63 ?  120 GLU   A H    1 
ATOM   2739 H HA   . GLU   A 1 120 ? 26.907 -15.274 12.314  1.00 18.24 ?  120 GLU   A HA   1 
ATOM   2740 H HB2  . GLU   A 1 120 ? 27.622 -14.004 14.717  1.00 23.26 ?  120 GLU   A HB2  1 
ATOM   2741 H HB3  . GLU   A 1 120 ? 26.657 -15.263 14.706  1.00 23.26 ?  120 GLU   A HB3  1 
ATOM   2742 H HG2  . GLU   A 1 120 ? 28.540 -16.363 13.552  1.00 30.52 ?  120 GLU   A HG2  1 
ATOM   2743 H HG3  . GLU   A 1 120 ? 29.398 -15.208 14.231  1.00 30.52 ?  120 GLU   A HG3  1 
ATOM   2744 N N    . VAL   A 1 121 ? 25.367 -12.581 13.062  1.00 13.41 ?  121 VAL   A N    1 
ATOM   2745 C CA   . VAL   A 1 121 ? 24.068 -11.923 13.176  1.00 13.54 ?  121 VAL   A CA   1 
ATOM   2746 C C    . VAL   A 1 121 ? 24.173 -10.548 12.532  1.00 12.24 ?  121 VAL   A C    1 
ATOM   2747 O O    . VAL   A 1 121 ? 25.130 -9.808  12.784  1.00 12.89 ?  121 VAL   A O    1 
ATOM   2748 C CB   . VAL   A 1 121 ? 23.627 -11.767 14.651  1.00 16.46 ?  121 VAL   A CB   1 
ATOM   2749 C CG1  . VAL   A 1 121 ? 22.220 -11.189 14.727  1.00 17.24 ?  121 VAL   A CG1  1 
ATOM   2750 C CG2  . VAL   A 1 121 ? 23.690 -13.080 15.411  1.00 19.24 ?  121 VAL   A CG2  1 
ATOM   2751 H H    . VAL   A 1 121 ? 26.030 -12.040 13.145  1.00 16.10 ?  121 VAL   A H    1 
ATOM   2752 H HA   . VAL   A 1 121 ? 23.400 -12.446 12.710  1.00 16.25 ?  121 VAL   A HA   1 
ATOM   2753 H HB   . VAL   A 1 121 ? 24.220 -11.143 15.095  1.00 19.75 ?  121 VAL   A HB   1 
ATOM   2754 H HG11 . VAL   A 1 121 ? 21.908 -11.225 15.647  1.00 20.68 ?  121 VAL   A HG11 1 
ATOM   2755 H HG12 . VAL   A 1 121 ? 22.234 -10.269 14.423  1.00 20.68 ?  121 VAL   A HG12 1 
ATOM   2756 H HG13 . VAL   A 1 121 ? 21.630 -11.715 14.162  1.00 20.68 ?  121 VAL   A HG13 1 
ATOM   2757 H HG21 . VAL   A 1 121 ? 23.333 -12.945 16.309  1.00 23.09 ?  121 VAL   A HG21 1 
ATOM   2758 H HG22 . VAL   A 1 121 ? 23.155 -13.742 14.946  1.00 23.09 ?  121 VAL   A HG22 1 
ATOM   2759 H HG23 . VAL   A 1 121 ? 24.610 -13.372 15.466  1.00 23.09 ?  121 VAL   A HG23 1 
ATOM   2760 N N    . LEU   A 1 122 ? 23.169 -10.185 11.732  1.00 11.45 ?  122 LEU   A N    1 
ATOM   2761 C CA   . LEU   A 1 122 ? 23.161 -8.891  11.058  1.00 11.42 ?  122 LEU   A CA   1 
ATOM   2762 C C    . LEU   A 1 122 ? 21.756 -8.310  11.023  1.00 11.20 ?  122 LEU   A C    1 
ATOM   2763 O O    . LEU   A 1 122 ? 20.771 -9.037  10.881  1.00 12.47 ?  122 LEU   A O    1 
ATOM   2764 C CB   . LEU   A 1 122 ? 23.596 -8.985  9.593   1.00 13.02 ?  122 LEU   A CB   1 
ATOM   2765 C CG   . LEU   A 1 122 ? 24.808 -9.829  9.247   1.00 12.98 ?  122 LEU   A CG   1 
ATOM   2766 C CD1  . LEU   A 1 122 ? 24.408 -11.288 9.040   1.00 13.75 ?  122 LEU   A CD1  1 
ATOM   2767 C CD2  . LEU   A 1 122 ? 25.478 -9.258  8.009   1.00 12.74 ?  122 LEU   A CD2  1 
ATOM   2768 H H    . LEU   A 1 122 ? 22.473 -10.671 11.567  1.00 13.74 ?  122 LEU   A H    1 
ATOM   2769 H HA   . LEU   A 1 122 ? 23.749 -8.274  11.522  1.00 13.71 ?  122 LEU   A HA   1 
ATOM   2770 H HB2  . LEU   A 1 122 ? 22.858 -9.346  9.085   1.00 15.63 ?  122 LEU   A HB2  1 
ATOM   2771 H HB3  . LEU   A 1 122 ? 23.789 -8.088  9.283   1.00 15.63 ?  122 LEU   A HB3  1 
ATOM   2772 H HG   . LEU   A 1 122 ? 25.454 -9.794  9.973   1.00 15.57 ?  122 LEU   A HG   1 
ATOM   2773 H HD11 . LEU   A 1 122 ? 25.182 -11.798 8.751   1.00 16.50 ?  122 LEU   A HD11 1 
ATOM   2774 H HD12 . LEU   A 1 122 ? 24.074 -11.648 9.877   1.00 16.50 ?  122 LEU   A HD12 1 
ATOM   2775 H HD13 . LEU   A 1 122 ? 23.714 -11.334 8.362   1.00 16.50 ?  122 LEU   A HD13 1 
ATOM   2776 H HD21 . LEU   A 1 122 ? 26.225 -9.830  7.754   1.00 15.29 ?  122 LEU   A HD21 1 
ATOM   2777 H HD22 . LEU   A 1 122 ? 24.833 -9.222  7.287   1.00 15.29 ?  122 LEU   A HD22 1 
ATOM   2778 H HD23 . LEU   A 1 122 ? 25.806 -8.365  8.206   1.00 15.29 ?  122 LEU   A HD23 1 
ATOM   2779 N N    . LEU   A 1 123 ? 21.688 -6.978  11.113  1.00 10.69 ?  123 LEU   A N    1 
ATOM   2780 C CA   . LEU   A 1 123 ? 20.513 -6.191  10.740  1.00 10.88 ?  123 LEU   A CA   1 
ATOM   2781 C C    . LEU   A 1 123 ? 20.748 -5.663  9.332   1.00 10.40 ?  123 LEU   A C    1 
ATOM   2782 O O    . LEU   A 1 123 ? 21.799 -5.070  9.077   1.00 10.85 ?  123 LEU   A O    1 
ATOM   2783 C CB   . LEU   A 1 123 ? 20.368 -5.013  11.705  1.00 11.76 ?  123 LEU   A CB   1 
ATOM   2784 C CG   . LEU   A 1 123 ? 19.324 -3.955  11.346  1.00 12.47 ?  123 LEU   A CG   1 
ATOM   2785 C CD1  . LEU   A 1 123 ? 17.902 -4.530  11.322  1.00 12.97 ?  123 LEU   A CD1  1 
ATOM   2786 C CD2  . LEU   A 1 123 ? 19.435 -2.791  12.326  1.00 13.13 ?  123 LEU   A CD2  1 
ATOM   2787 H H    . LEU   A 1 123 ? 22.345 -6.490  11.398  1.00 12.83 ?  123 LEU   A H    1 
ATOM   2788 H HA   . LEU   A 1 123 ? 19.716 -6.742  10.770  1.00 13.05 ?  123 LEU   A HA   1 
ATOM   2789 H HB2  . LEU   A 1 123 ? 20.124 -5.358  12.581  1.00 14.11 ?  123 LEU   A HB2  1 
ATOM   2790 H HB3  . LEU   A 1 123 ? 21.221 -4.559  11.768  1.00 14.11 ?  123 LEU   A HB3  1 
ATOM   2791 H HG   . LEU   A 1 123 ? 19.514 -3.601  10.460  1.00 14.96 ?  123 LEU   A HG   1 
ATOM   2792 H HD11 . LEU   A 1 123 ? 17.276 -3.824  11.104  1.00 15.57 ?  123 LEU   A HD11 1 
ATOM   2793 H HD12 . LEU   A 1 123 ? 17.861 -5.231  10.652  1.00 15.57 ?  123 LEU   A HD12 1 
ATOM   2794 H HD13 . LEU   A 1 123 ? 17.700 -4.897  12.197  1.00 15.57 ?  123 LEU   A HD13 1 
ATOM   2795 H HD21 . LEU   A 1 123 ? 18.772 -2.122  12.103  1.00 15.76 ?  123 LEU   A HD21 1 
ATOM   2796 H HD22 . LEU   A 1 123 ? 19.276 -3.127  13.225  1.00 15.76 ?  123 LEU   A HD22 1 
ATOM   2797 H HD23 . LEU   A 1 123 ? 20.325 -2.415  12.268  1.00 15.76 ?  123 LEU   A HD23 1 
ATOM   2798 N N    . ALA   A 1 124 ? 19.799 -5.872  8.419   1.00 10.16 ?  124 ALA   A N    1 
ATOM   2799 C CA   . ALA   A 1 124 ? 20.081 -5.606  7.017   1.00 10.20 ?  124 ALA   A CA   1 
ATOM   2800 C C    . ALA   A 1 124 ? 18.842 -5.135  6.268   1.00 10.29 ?  124 ALA   A C    1 
ATOM   2801 O O    . ALA   A 1 124 ? 17.708 -5.470  6.644   1.00 11.17 ?  124 ALA   A O    1 
ATOM   2802 C CB   . ALA   A 1 124 ? 20.631 -6.850  6.316   1.00 10.58 ?  124 ALA   A CB   1 
ATOM   2803 H H    . ALA   A 1 124 ? 19.001 -6.161  8.588   1.00 12.20 ?  124 ALA   A H    1 
ATOM   2804 H HA   . ALA   A 1 124 ? 20.763 -4.918  6.985   1.00 12.24 ?  124 ALA   A HA   1 
ATOM   2805 H HB1  . ALA   A 1 124 ? 20.813 -6.637  5.390   1.00 12.70 ?  124 ALA   A HB1  1 
ATOM   2806 H HB2  . ALA   A 1 124 ? 21.455 -7.125  6.759   1.00 12.70 ?  124 ALA   A HB2  1 
ATOM   2807 H HB3  . ALA   A 1 124 ? 19.977 -7.561  6.375   1.00 12.70 ?  124 ALA   A HB3  1 
ATOM   2808 N N    A PRO   A 1 125 ? 19.030 -4.366  5.205   0.42 10.46 ?  125 PRO   A N    1 
ATOM   2809 N N    B PRO   A 1 125 ? 19.035 -4.417  5.154   0.58 9.63  ?  125 PRO   A N    1 
ATOM   2810 C CA   A PRO   A 1 125 ? 17.968 -4.119  4.234   0.42 11.03 ?  125 PRO   A CA   1 
ATOM   2811 C CA   B PRO   A 1 125 ? 17.946 -4.107  4.230   0.58 10.24 ?  125 PRO   A CA   1 
ATOM   2812 C C    A PRO   A 1 125 ? 18.016 -5.177  3.137   0.42 11.31 ?  125 PRO   A C    1 
ATOM   2813 C C    B PRO   A 1 125 ? 17.921 -5.127  3.106   0.58 10.42 ?  125 PRO   A C    1 
ATOM   2814 O O    A PRO   A 1 125 ? 18.958 -5.969  3.041   0.42 11.25 ?  125 PRO   A O    1 
ATOM   2815 O O    B PRO   A 1 125 ? 18.863 -5.918  2.975   0.58 11.10 ?  125 PRO   A O    1 
ATOM   2816 C CB   A PRO   A 1 125 ? 18.390 -2.764  3.654   0.42 11.31 ?  125 PRO   A CB   1 
ATOM   2817 C CB   B PRO   A 1 125 ? 18.399 -2.755  3.668   0.58 10.41 ?  125 PRO   A CB   1 
ATOM   2818 C CG   A PRO   A 1 125 ? 19.891 -2.857  3.630   0.42 11.43 ?  125 PRO   A CG   1 
ATOM   2819 C CG   B PRO   A 1 125 ? 19.907 -2.972  3.496   0.58 10.07 ?  125 PRO   A CG   1 
ATOM   2820 C CD   A PRO   A 1 125 ? 20.254 -3.604  4.889   0.42 10.85 ?  125 PRO   A CD   1 
ATOM   2821 C CD   B PRO   A 1 125 ? 20.319 -3.868  4.664   0.58 9.18  ?  125 PRO   A CD   1 
ATOM   2822 H HA   A PRO   A 1 125 ? 17.089 -4.074  4.647   0.42 13.24 ?  125 PRO   A HA   1 
ATOM   2823 H HA   B PRO   A 1 125 ? 17.085 -4.037  4.679   0.58 12.29 ?  125 PRO   A HA   1 
ATOM   2824 H HB2  A PRO   A 1 125 ? 18.030 -2.657  2.759   0.42 13.57 ?  125 PRO   A HB2  1 
ATOM   2825 H HB2  B PRO   A 1 125 ? 17.961 -2.580  2.817   0.58 12.49 ?  125 PRO   A HB2  1 
ATOM   2826 H HB3  A PRO   A 1 125 ? 18.093 -2.046  4.237   0.42 13.57 ?  125 PRO   A HB3  1 
ATOM   2827 H HB3  B PRO   A 1 125 ? 18.212 -2.045  4.307   0.58 12.49 ?  125 PRO   A HB3  1 
ATOM   2828 H HG2  A PRO   A 1 125 ? 20.177 -3.351  2.844   0.42 13.71 ?  125 PRO   A HG2  1 
ATOM   2829 H HG2  B PRO   A 1 125 ? 20.080 -3.409  2.643   0.58 12.09 ?  125 PRO   A HG2  1 
ATOM   2830 H HG3  A PRO   A 1 125 ? 20.276 -1.966  3.634   0.42 13.71 ?  125 PRO   A HG3  1 
ATOM   2831 H HG3  B PRO   A 1 125 ? 20.368 -2.116  3.534   0.58 12.09 ?  125 PRO   A HG3  1 
ATOM   2832 H HD2  A PRO   A 1 125 ? 20.998 -4.204  4.727   0.42 13.02 ?  125 PRO   A HD2  1 
ATOM   2833 H HD2  B PRO   A 1 125 ? 20.904 -4.578  4.350   0.58 11.01 ?  125 PRO   A HD2  1 
ATOM   2834 H HD3  A PRO   A 1 125 ? 20.452 -2.979  5.608   0.42 13.02 ?  125 PRO   A HD3  1 
ATOM   2835 H HD3  B PRO   A 1 125 ? 20.747 -3.338  5.354   0.58 11.01 ?  125 PRO   A HD3  1 
ATOM   2836 N N    A LEU   A 1 126 ? 16.986 -5.164  2.295   0.42 11.85 ?  126 LEU   A N    1 
ATOM   2837 N N    B LEU   A 1 126 ? 16.890 -5.100  2.263   0.58 11.03 ?  126 LEU   A N    1 
ATOM   2838 C CA   A LEU   A 1 126 ? 16.985 -5.985  1.091   0.42 12.33 ?  126 LEU   A CA   1 
ATOM   2839 C CA   B LEU   A 1 126 ? 16.961 -5.829  1.007   0.58 11.23 ?  126 LEU   A CA   1 
ATOM   2840 C C    A LEU   A 1 126 ? 17.911 -5.360  0.057   0.42 12.73 ?  126 LEU   A C    1 
ATOM   2841 C C    B LEU   A 1 126 ? 17.910 -5.119  0.051   0.58 11.03 ?  126 LEU   A C    1 
ATOM   2842 O O    A LEU   A 1 126 ? 17.647 -4.266  -0.455  0.42 13.13 ?  126 LEU   A O    1 
ATOM   2843 O O    B LEU   A 1 126 ? 17.847 -3.897  -0.115  0.58 12.62 ?  126 LEU   A O    1 
ATOM   2844 C CB   A LEU   A 1 126 ? 15.571 -6.138  0.546   0.42 12.44 ?  126 LEU   A CB   1 
ATOM   2845 C CB   B LEU   A 1 126 ? 15.580 -5.953  0.373   0.58 13.02 ?  126 LEU   A CB   1 
ATOM   2846 C CG   A LEU   A 1 126 ? 14.693 -7.062  1.385   0.42 12.59 ?  126 LEU   A CG   1 
ATOM   2847 C CG   B LEU   A 1 126 ? 14.624 -6.965  0.998   0.58 14.33 ?  126 LEU   A CG   1 
ATOM   2848 C CD1  A LEU   A 1 126 ? 13.252 -6.946  0.947   0.42 12.51 ?  126 LEU   A CD1  1 
ATOM   2849 C CD1  B LEU   A 1 126 ? 13.273 -6.862  0.322   0.58 14.71 ?  126 LEU   A CD1  1 
ATOM   2850 C CD2  A LEU   A 1 126 ? 15.177 -8.501  1.263   0.42 12.76 ?  126 LEU   A CD2  1 
ATOM   2851 C CD2  B LEU   A 1 126 ? 15.161 -8.390  0.891   0.58 15.12 ?  126 LEU   A CD2  1 
ATOM   2852 H H    A LEU   A 1 126 ? 16.274 -4.686  2.394   0.42 14.22 ?  126 LEU   A H    1 
ATOM   2853 H H    B LEU   A 1 126 ? 16.163 -4.650  2.379   0.58 13.24 ?  126 LEU   A H    1 
ATOM   2854 H HA   A LEU   A 1 126 ? 17.329 -6.864  1.304   0.42 14.80 ?  126 LEU   A HA   1 
ATOM   2855 H HA   B LEU   A 1 126 ? 17.306 -6.712  1.170   0.58 13.48 ?  126 LEU   A HA   1 
ATOM   2856 H HB2  A LEU   A 1 126 ? 15.148 -5.264  0.521   0.42 14.93 ?  126 LEU   A HB2  1 
ATOM   2857 H HB2  B LEU   A 1 126 ? 15.145 -5.086  0.417   0.58 15.63 ?  126 LEU   A HB2  1 
ATOM   2858 H HB3  A LEU   A 1 126 ? 15.617 -6.504  -0.353  0.42 14.93 ?  126 LEU   A HB3  1 
ATOM   2859 H HB3  B LEU   A 1 126 ? 15.693 -6.205  -0.556  0.58 15.63 ?  126 LEU   A HB3  1 
ATOM   2860 H HG   A LEU   A 1 126 ? 14.748 -6.799  2.317   0.42 15.11 ?  126 LEU   A HG   1 
ATOM   2861 H HG   B LEU   A 1 126 ? 14.505 -6.755  1.937   0.58 17.20 ?  126 LEU   A HG   1 
ATOM   2862 H HD11 A LEU   A 1 126 ? 12.708 -7.538  1.490   0.42 15.01 ?  126 LEU   A HD11 1 
ATOM   2863 H HD11 B LEU   A 1 126 ? 12.669 -7.508  0.722   0.58 17.65 ?  126 LEU   A HD11 1 
ATOM   2864 H HD12 A LEU   A 1 126 ? 12.959 -6.028  1.064   0.42 15.01 ?  126 LEU   A HD12 1 
ATOM   2865 H HD12 B LEU   A 1 126 ? 12.925 -5.964  0.443   0.58 17.65 ?  126 LEU   A HD12 1 
ATOM   2866 H HD13 A LEU   A 1 126 ? 13.184 -7.198  0.013   0.42 15.01 ?  126 LEU   A HD13 1 
ATOM   2867 H HD13 B LEU   A 1 126 ? 13.378 -7.050  -0.625  0.58 17.65 ?  126 LEU   A HD13 1 
ATOM   2868 H HD21 A LEU   A 1 126 ? 14.506 -9.094  1.630   0.42 15.31 ?  126 LEU   A HD21 1 
ATOM   2869 H HD21 B LEU   A 1 126 ? 14.471 -9.012  1.169   0.58 18.15 ?  126 LEU   A HD21 1 
ATOM   2870 H HD22 A LEU   A 1 126 ? 15.323 -8.706  0.325   0.42 15.31 ?  126 LEU   A HD22 1 
ATOM   2871 H HD22 B LEU   A 1 126 ? 15.411 -8.565  -0.031  0.58 18.15 ?  126 LEU   A HD22 1 
ATOM   2872 H HD23 A LEU   A 1 126 ? 16.009 -8.598  1.753   0.42 15.31 ?  126 LEU   A HD23 1 
ATOM   2873 H HD23 B LEU   A 1 126 ? 15.938 -8.480  1.465   0.58 18.15 ?  126 LEU   A HD23 1 
ATOM   2874 N N    A LEU   A 1 127 ? 18.992 -6.068  -0.256  0.42 13.41 ?  127 LEU   A N    1 
ATOM   2875 N N    B LEU   A 1 127 ? 18.793 -5.889  -0.578  0.58 10.80 ?  127 LEU   A N    1 
ATOM   2876 C CA   A LEU   A 1 127 ? 19.967 -5.578  -1.212  0.42 13.55 ?  127 LEU   A CA   1 
ATOM   2877 C CA   B LEU   A 1 127 ? 19.795 -5.337  -1.472  0.58 11.66 ?  127 LEU   A CA   1 
ATOM   2878 C C    A LEU   A 1 127 ? 19.327 -5.404  -2.580  0.42 12.84 ?  127 LEU   A C    1 
ATOM   2879 C C    B LEU   A 1 127 ? 19.282 -5.290  -2.905  0.58 12.46 ?  127 LEU   A C    1 
ATOM   2880 O O    A LEU   A 1 127 ? 18.441 -6.164  -2.987  0.42 13.25 ?  127 LEU   A O    1 
ATOM   2881 O O    B LEU   A 1 127 ? 18.518 -6.153  -3.357  0.58 12.49 ?  127 LEU   A O    1 
ATOM   2882 C CB   A LEU   A 1 127 ? 21.134 -6.557  -1.322  0.42 13.62 ?  127 LEU   A CB   1 
ATOM   2883 C CB   B LEU   A 1 127 ? 21.094 -6.148  -1.416  0.58 12.35 ?  127 LEU   A CB   1 
ATOM   2884 C CG   A LEU   A 1 127 ? 21.928 -6.813  -0.042  0.42 13.65 ?  127 LEU   A CG   1 
ATOM   2885 C CG   B LEU   A 1 127 ? 21.840 -6.166  -0.078  0.58 13.19 ?  127 LEU   A CG   1 
ATOM   2886 C CD1  A LEU   A 1 127 ? 23.013 -7.833  -0.313  0.42 13.78 ?  127 LEU   A CD1  1 
ATOM   2887 C CD1  B LEU   A 1 127 ? 23.036 -7.105  -0.142  0.58 13.98 ?  127 LEU   A CD1  1 
ATOM   2888 C CD2  A LEU   A 1 127 ? 22.531 -5.525  0.485   0.42 14.20 ?  127 LEU   A CD2  1 
ATOM   2889 C CD2  B LEU   A 1 127 ? 22.288 -4.761  0.313   0.58 14.39 ?  127 LEU   A CD2  1 
ATOM   2890 H H    A LEU   A 1 127 ? 19.178 -6.842  0.068   0.42 16.09 ?  127 LEU   A H    1 
ATOM   2891 H H    B LEU   A 1 127 ? 18.826 -6.748  -0.498  0.58 12.97 ?  127 LEU   A H    1 
ATOM   2892 H HA   A LEU   A 1 127 ? 20.306 -4.720  -0.923  0.42 16.26 ?  127 LEU   A HA   1 
ATOM   2893 H HA   B LEU   A 1 127 ? 19.995 -4.433  -1.193  0.58 13.99 ?  127 LEU   A HA   1 
ATOM   2894 H HB2  A LEU   A 1 127 ? 20.785 -7.412  -1.621  0.42 16.35 ?  127 LEU   A HB2  1 
ATOM   2895 H HB2  B LEU   A 1 127 ? 20.888 -7.068  -1.639  0.58 14.82 ?  127 LEU   A HB2  1 
ATOM   2896 H HB3  A LEU   A 1 127 ? 21.756 -6.216  -1.982  0.42 16.35 ?  127 LEU   A HB3  1 
ATOM   2897 H HB3  B LEU   A 1 127 ? 21.702 -5.785  -2.077  0.58 14.82 ?  127 LEU   A HB3  1 
ATOM   2898 H HG   A LEU   A 1 127 ? 21.335 -7.176  0.637   0.42 16.38 ?  127 LEU   A HG   1 
ATOM   2899 H HG   B LEU   A 1 127 ? 21.243 -6.490  0.615   0.58 15.83 ?  127 LEU   A HG   1 
ATOM   2900 H HD11 A LEU   A 1 127 ? 23.494 -8.009  0.511   0.42 16.54 ?  127 LEU   A HD11 1 
ATOM   2901 H HD11 B LEU   A 1 127 ? 23.492 -7.099  0.716   0.58 16.78 ?  127 LEU   A HD11 1 
ATOM   2902 H HD12 A LEU   A 1 127 ? 22.605 -8.651  -0.639  0.42 16.54 ?  127 LEU   A HD12 1 
ATOM   2903 H HD12 B LEU   A 1 127 ? 22.724 -8.001  -0.342  0.58 16.78 ?  127 LEU   A HD12 1 
ATOM   2904 H HD13 A LEU   A 1 127 ? 23.619 -7.477  -0.981  0.42 16.54 ?  127 LEU   A HD13 1 
ATOM   2905 H HD13 B LEU   A 1 127 ? 23.641 -6.802  -0.837  0.58 16.78 ?  127 LEU   A HD13 1 
ATOM   2906 H HD21 A LEU   A 1 127 ? 23.122 -5.733  1.224   0.42 17.03 ?  127 LEU   A HD21 1 
ATOM   2907 H HD21 B LEU   A 1 127 ? 22.847 -4.816  1.105   0.58 17.27 ?  127 LEU   A HD21 1 
ATOM   2908 H HD22 A LEU   A 1 127 ? 23.031 -5.099  -0.230  0.42 17.03 ?  127 LEU   A HD22 1 
ATOM   2909 H HD22 B LEU   A 1 127 ? 22.793 -4.375  -0.420  0.58 17.27 ?  127 LEU   A HD22 1 
ATOM   2910 H HD23 A LEU   A 1 127 ? 21.817 -4.942  0.783   0.42 17.03 ?  127 LEU   A HD23 1 
ATOM   2911 H HD23 B LEU   A 1 127 ? 21.506 -4.219  0.499   0.58 17.27 ?  127 LEU   A HD23 1 
ATOM   2912 N N    A SER   A 1 128 ? 19.795 -4.381  -3.289  0.42 12.90 ?  128 SER   A N    1 
ATOM   2913 N N    B SER   A 1 128 ? 19.715 -4.248  -3.610  0.58 14.14 ?  128 SER   A N    1 
ATOM   2914 C CA   A SER   A 1 128 ? 19.383 -4.018  -4.636  0.42 12.72 ?  128 SER   A CA   1 
ATOM   2915 C CA   B SER   A 1 128 ? 19.470 -3.984  -5.019  0.58 15.68 ?  128 SER   A CA   1 
ATOM   2916 C C    A SER   A 1 128 ? 17.937 -3.544  -4.719  0.42 12.24 ?  128 SER   A C    1 
ATOM   2917 C C    B SER   A 1 128 ? 18.036 -3.571  -5.325  0.58 17.37 ?  128 SER   A C    1 
ATOM   2918 O O    A SER   A 1 128 ? 17.477 -3.227  -5.820  0.42 12.82 ?  128 SER   A O    1 
ATOM   2919 O O    B SER   A 1 128 ? 17.740 -3.276  -6.486  0.58 17.52 ?  128 SER   A O    1 
ATOM   2920 C CB   A SER   A 1 128 ? 19.669 -5.111  -5.676  0.42 12.69 ?  128 SER   A CB   1 
ATOM   2921 C CB   B SER   A 1 128 ? 19.930 -5.130  -5.934  0.58 14.39 ?  128 SER   A CB   1 
ATOM   2922 O OG   A SER   A 1 128 ? 21.062 -5.388  -5.730  0.42 13.35 ?  128 SER   A OG   1 
ATOM   2923 O OG   B SER   A 1 128 ? 21.346 -5.241  -5.902  0.58 12.69 ?  128 SER   A OG   1 
ATOM   2924 H H    A SER   A 1 128 ? 20.395 -3.840  -2.985  0.42 15.48 ?  128 SER   A H    1 
ATOM   2925 H H    B SER   A 1 128 ? 20.193 -3.628  -3.254  0.58 16.97 ?  128 SER   A H    1 
ATOM   2926 H HA   A SER   A 1 128 ? 19.915 -3.261  -4.897  0.42 15.27 ?  128 SER   A HA   1 
ATOM   2927 H HA   B SER   A 1 128 ? 20.008 -3.221  -5.256  0.58 18.82 ?  128 SER   A HA   1 
ATOM   2928 H HB2  A SER   A 1 128 ? 19.193 -5.918  -5.436  0.42 15.23 ?  128 SER   A HB2  1 
ATOM   2929 H HB2  B SER   A 1 128 ? 19.531 -5.958  -5.632  0.58 17.27 ?  128 SER   A HB2  1 
ATOM   2930 H HB3  A SER   A 1 128 ? 19.378 -4.800  -6.551  0.42 15.23 ?  128 SER   A HB3  1 
ATOM   2931 H HB3  B SER   A 1 128 ? 19.652 -4.935  -6.844  0.58 17.27 ?  128 SER   A HB3  1 
ATOM   2932 H HG   A SER   A 1 128 ? 21.485 -4.697  -5.939  0.42 16.02 ?  128 SER   A HG   1 
ATOM   2933 H HG   B SER   A 1 128 ? 21.690 -4.512  -6.138  0.58 15.22 ?  128 SER   A HG   1 
ATOM   2934 N N    A ALA   A 1 129 ? 17.213 -3.465  -3.600  0.42 12.43 ?  129 ALA   A N    1 
ATOM   2935 N N    B ALA   A 1 129 ? 17.152 -3.490  -4.327  0.58 19.11 ?  129 ALA   A N    1 
ATOM   2936 C CA   A ALA   A 1 129 ? 15.844 -2.970  -3.605  0.42 12.98 ?  129 ALA   A CA   1 
ATOM   2937 C CA   B ALA   A 1 129 ? 15.725 -3.284  -4.552  0.58 21.31 ?  129 ALA   A CA   1 
ATOM   2938 C C    A ALA   A 1 129 ? 15.841 -1.441  -3.585  0.42 13.07 ?  129 ALA   A C    1 
ATOM   2939 C C    B ALA   A 1 129 ? 15.292 -1.820  -4.479  0.58 22.46 ?  129 ALA   A C    1 
ATOM   2940 O O    A ALA   A 1 129 ? 16.885 -0.785  -3.657  0.42 13.34 ?  129 ALA   A O    1 
ATOM   2941 O O    B ALA   A 1 129 ? 14.087 -1.547  -4.429  0.58 23.08 ?  129 ALA   A O    1 
ATOM   2942 C CB   A ALA   A 1 129 ? 15.059 -3.560  -2.433  0.42 14.59 ?  129 ALA   A CB   1 
ATOM   2943 C CB   B ALA   A 1 129 ? 14.908 -4.122  -3.564  0.58 21.95 ?  129 ALA   A CB   1 
ATOM   2944 H H    A ALA   A 1 129 ? 17.500 -3.688  -2.817  0.42 14.92 ?  129 ALA   A H    1 
ATOM   2945 H H    B ALA   A 1 129 ? 17.359 -3.541  -3.494  0.58 22.93 ?  129 ALA   A H    1 
ATOM   2946 H HA   A ALA   A 1 129 ? 15.414 -3.244  -4.421  0.42 15.58 ?  129 ALA   A HA   1 
ATOM   2947 H HA   B ALA   A 1 129 ? 15.515 -3.602  -5.440  0.58 25.57 ?  129 ALA   A HA   1 
ATOM   2948 H HB1  A ALA   A 1 129 ? 14.149 -3.225  -2.462  0.42 17.51 ?  129 ALA   A HB1  1 
ATOM   2949 H HB1  B ALA   A 1 129 ? 13.962 -3.974  -3.732  0.58 26.34 ?  129 ALA   A HB1  1 
ATOM   2950 H HB2  A ALA   A 1 129 ? 15.059 -4.527  -2.512  0.42 17.51 ?  129 ALA   A HB2  1 
ATOM   2951 H HB2  B ALA   A 1 129 ? 15.124 -5.057  -3.696  0.58 26.34 ?  129 ALA   A HB2  1 
ATOM   2952 H HB3  A ALA   A 1 129 ? 15.482 -3.297  -1.600  0.42 17.51 ?  129 ALA   A HB3  1 
ATOM   2953 H HB3  B ALA   A 1 129 ? 15.129 -3.852  -2.661  0.58 26.34 ?  129 ALA   A HB3  1 
ATOM   2954 N N    A GLY   A 1 130 ? 14.649 -0.865  -3.505  0.42 13.65 ?  130 GLY   A N    1 
ATOM   2955 N N    B GLY   A 1 130 ? 16.235 -0.880  -4.482  0.58 22.83 ?  130 GLY   A N    1 
ATOM   2956 C CA   A GLY   A 1 130 ? 14.542 0.583   -3.462  0.42 14.36 ?  130 GLY   A CA   1 
ATOM   2957 C CA   B GLY   A 1 130 ? 15.906 0.534   -4.512  0.58 23.19 ?  130 GLY   A CA   1 
ATOM   2958 C C    A GLY   A 1 130 ? 15.157 1.207   -4.698  0.42 14.33 ?  130 GLY   A C    1 
ATOM   2959 C C    B GLY   A 1 130 ? 16.182 1.156   -5.865  0.58 23.50 ?  130 GLY   A C    1 
ATOM   2960 O O    A GLY   A 1 130 ? 14.906 0.776   -5.830  0.42 14.31 ?  130 GLY   A O    1 
ATOM   2961 O O    B GLY   A 1 130 ? 15.690 0.662   -6.885  0.58 23.05 ?  130 GLY   A O    1 
ATOM   2962 H H    A GLY   A 1 130 ? 13.900 -1.283  -3.485  0.42 16.38 ?  130 GLY   A H    1 
ATOM   2963 H H    B GLY   A 1 130 ? 17.077 -1.039  -4.469  0.58 27.40 ?  130 GLY   A H    1 
ATOM   2964 H HA2  A GLY   A 1 130 ? 13.607 0.840   -3.408  0.42 17.23 ?  130 GLY   A HA2  1 
ATOM   2965 H HA2  B GLY   A 1 130 ? 14.968 0.661   -4.299  0.58 27.83 ?  130 GLY   A HA2  1 
ATOM   2966 H HA3  A GLY   A 1 130 ? 15.003 0.924   -2.681  0.42 17.23 ?  130 GLY   A HA3  1 
ATOM   2967 H HA3  B GLY   A 1 130 ? 16.437 1.003   -3.854  0.58 27.83 ?  130 GLY   A HA3  1 
ATOM   2968 N N    A ILE   A 1 131 ? 16.002 2.219   -4.480  0.42 14.69 ?  131 ILE   A N    1 
ATOM   2969 N N    B ILE   A 1 131 ? 16.975 2.234   -5.894  0.58 24.26 ?  131 ILE   A N    1 
ATOM   2970 C CA   A ILE   A 1 131 ? 16.573 2.987   -5.584  0.42 14.77 ?  131 ILE   A CA   1 
ATOM   2971 C CA   B ILE   A 1 131 ? 17.351 2.851   -7.163  0.58 24.95 ?  131 ILE   A CA   1 
ATOM   2972 C C    A ILE   A 1 131 ? 17.565 2.195   -6.418  0.42 15.03 ?  131 ILE   A C    1 
ATOM   2973 C C    B ILE   A 1 131 ? 18.153 1.893   -8.031  0.58 24.05 ?  131 ILE   A C    1 
ATOM   2974 O O    A ILE   A 1 131 ? 17.975 2.674   -7.481  0.42 15.00 ?  131 ILE   A O    1 
ATOM   2975 O O    B ILE   A 1 131 ? 18.282 2.114   -9.239  0.58 24.17 ?  131 ILE   A O    1 
ATOM   2976 C CB   A ILE   A 1 131 ? 17.180 4.331   -5.118  0.42 15.48 ?  131 ILE   A CB   1 
ATOM   2977 C CB   B ILE   A 1 131 ? 18.103 4.185   -6.950  0.58 26.50 ?  131 ILE   A CB   1 
ATOM   2978 C CG1  A ILE   A 1 131 ? 18.458 4.118   -4.301  0.42 16.83 ?  131 ILE   A CG1  1 
ATOM   2979 C CG1  B ILE   A 1 131 ? 19.470 3.944   -6.306  0.58 27.28 ?  131 ILE   A CG1  1 
ATOM   2980 C CG2  A ILE   A 1 131 ? 16.158 5.119   -4.311  0.42 15.83 ?  131 ILE   A CG2  1 
ATOM   2981 C CG2  B ILE   A 1 131 ? 17.265 5.139   -6.108  0.58 27.23 ?  131 ILE   A CG2  1 
ATOM   2982 C CD1  A ILE   A 1 131 ? 19.115 5.415   -3.847  0.42 18.01 ?  131 ILE   A CD1  1 
ATOM   2983 C CD1  B ILE   A 1 131 ? 20.343 5.175   -6.262  0.58 27.97 ?  131 ILE   A CD1  1 
ATOM   2984 H H    A ILE   A 1 131 ? 16.255 2.478   -3.703  0.42 17.62 ?  131 ILE   A H    1 
ATOM   2985 H H    B ILE   A 1 131 ? 17.309 2.618   -5.201  0.58 29.11 ?  131 ILE   A H    1 
ATOM   2986 H HA   A ILE   A 1 131 ? 15.854 3.208   -6.186  0.42 17.72 ?  131 ILE   A HA   1 
ATOM   2987 H HA   B ILE   A 1 131 ? 16.544 3.062   -7.651  0.58 29.94 ?  131 ILE   A HA   1 
ATOM   2988 H HB   A ILE   A 1 131 ? 17.407 4.851   -5.906  0.42 18.58 ?  131 ILE   A HB   1 
ATOM   2989 H HB   B ILE   A 1 131 ? 18.243 4.599   -7.817  0.58 31.80 ?  131 ILE   A HB   1 
ATOM   2990 H HG12 A ILE   A 1 131 ? 18.241 3.604   -3.511  0.42 20.19 ?  131 ILE   A HG12 1 
ATOM   2991 H HG12 B ILE   A 1 131 ? 19.336 3.641   -5.396  0.58 32.74 ?  131 ILE   A HG12 1 
ATOM   2992 H HG13 A ILE   A 1 131 ? 19.105 3.642   -4.842  0.42 20.19 ?  131 ILE   A HG13 1 
ATOM   2993 H HG13 B ILE   A 1 131 ? 19.949 3.270   -6.812  0.58 32.74 ?  131 ILE   A HG13 1 
ATOM   2994 H HG21 A ILE   A 1 131 ? 16.478 6.026   -4.189  0.42 19.00 ?  131 ILE   A HG21 1 
ATOM   2995 H HG21 B ILE   A 1 131 ? 17.693 6.010   -6.095  0.58 32.68 ?  131 ILE   A HG21 1 
ATOM   2996 H HG22 A ILE   A 1 131 ? 15.317 5.129   -4.794  0.42 19.00 ?  131 ILE   A HG22 1 
ATOM   2997 H HG22 B ILE   A 1 131 ? 16.381 5.212   -6.502  0.58 32.68 ?  131 ILE   A HG22 1 
ATOM   2998 H HG23 A ILE   A 1 131 ? 16.038 4.690   -3.449  0.42 19.00 ?  131 ILE   A HG23 1 
ATOM   2999 H HG23 B ILE   A 1 131 ? 17.198 4.789   -5.207  0.58 32.68 ?  131 ILE   A HG23 1 
ATOM   3000 H HD11 A ILE   A 1 131 ? 19.985 5.214   -3.470  0.42 21.61 ?  131 ILE   A HD11 1 
ATOM   3001 H HD11 B ILE   A 1 131 ? 21.232 4.920   -5.970  0.58 33.57 ?  131 ILE   A HD11 1 
ATOM   3002 H HD12 A ILE   A 1 131 ? 19.216 6.005   -4.613  0.42 21.61 ?  131 ILE   A HD12 1 
ATOM   3003 H HD12 B ILE   A 1 131 ? 20.386 5.564   -7.150  0.58 33.57 ?  131 ILE   A HD12 1 
ATOM   3004 H HD13 A ILE   A 1 131 ? 18.555 5.840   -3.178  0.42 21.61 ?  131 ILE   A HD13 1 
ATOM   3005 H HD13 B ILE   A 1 131 ? 19.959 5.812   -5.641  0.58 33.57 ?  131 ILE   A HD13 1 
ATOM   3006 N N    A PHE   A 1 132 ? 17.954 0.993   -5.979  0.42 14.25 ?  132 PHE   A N    1 
ATOM   3007 N N    B PHE   A 1 132 ? 18.708 0.832   -7.443  0.58 23.19 ?  132 PHE   A N    1 
ATOM   3008 C CA   A PHE   A 1 132 ? 18.824 0.141   -6.782  0.42 14.65 ?  132 PHE   A CA   1 
ATOM   3009 C CA   B PHE   A 1 132 ? 19.392 -0.183  -8.234  0.58 23.27 ?  132 PHE   A CA   1 
ATOM   3010 C C    A PHE   A 1 132 ? 18.073 -0.613  -7.880  0.42 14.88 ?  132 PHE   A C    1 
ATOM   3011 C C    B PHE   A 1 132 ? 18.431 -1.032  -9.056  0.58 24.28 ?  132 PHE   A C    1 
ATOM   3012 O O    A PHE   A 1 132 ? 18.716 -1.200  -8.757  0.42 14.92 ?  132 PHE   A O    1 
ATOM   3013 O O    B PHE   A 1 132 ? 18.890 -1.861  -9.848  0.58 23.41 ?  132 PHE   A O    1 
ATOM   3014 C CB   A PHE   A 1 132 ? 19.610 -0.830  -5.888  0.42 13.96 ?  132 PHE   A CB   1 
ATOM   3015 C CB   B PHE   A 1 132 ? 20.262 -1.064  -7.329  0.58 23.17 ?  132 PHE   A CB   1 
ATOM   3016 C CG   A PHE   A 1 132 ? 20.818 -0.214  -5.212  0.42 13.45 ?  132 PHE   A CG   1 
ATOM   3017 C CG   B PHE   A 1 132 ? 21.559 -0.415  -6.904  0.58 23.37 ?  132 PHE   A CG   1 
ATOM   3018 C CD1  A PHE   A 1 132 ? 20.677 0.815   -4.290  0.42 13.57 ?  132 PHE   A CD1  1 
ATOM   3019 C CD1  B PHE   A 1 132 ? 21.847 0.901   -7.244  0.58 23.95 ?  132 PHE   A CD1  1 
ATOM   3020 C CD2  A PHE   A 1 132 ? 22.092 -0.696  -5.472  0.42 13.39 ?  132 PHE   A CD2  1 
ATOM   3021 C CD2  B PHE   A 1 132 ? 22.491 -1.128  -6.170  0.58 23.28 ?  132 PHE   A CD2  1 
ATOM   3022 C CE1  A PHE   A 1 132 ? 21.790 1.373   -3.668  0.42 13.60 ?  132 PHE   A CE1  1 
ATOM   3023 C CE1  B PHE   A 1 132 ? 23.035 1.490   -6.857  0.58 23.96 ?  132 PHE   A CE1  1 
ATOM   3024 C CE2  A PHE   A 1 132 ? 23.204 -0.151  -4.848  0.42 13.09 ?  132 PHE   A CE2  1 
ATOM   3025 C CE2  B PHE   A 1 132 ? 23.680 -0.544  -5.779  0.58 23.48 ?  132 PHE   A CE2  1 
ATOM   3026 C CZ   A PHE   A 1 132 ? 23.050 0.882   -3.944  0.42 13.08 ?  132 PHE   A CZ   1 
ATOM   3027 C CZ   B PHE   A 1 132 ? 23.953 0.766   -6.122  0.58 23.62 ?  132 PHE   A CZ   1 
ATOM   3028 H H    A PHE   A 1 132 ? 17.726 0.651   -5.221  0.42 17.10 ?  132 PHE   A H    1 
ATOM   3029 H H    B PHE   A 1 132 ? 18.698 0.682   -6.597  0.58 27.82 ?  132 PHE   A H    1 
ATOM   3030 H HA   A PHE   A 1 132 ? 19.475 0.705   -7.219  0.42 17.58 ?  132 PHE   A HA   1 
ATOM   3031 H HA   B PHE   A 1 132 ? 19.973 0.262   -8.869  0.58 27.92 ?  132 PHE   A HA   1 
ATOM   3032 H HB2  A PHE   A 1 132 ? 19.025 -1.156  -5.188  0.42 16.75 ?  132 PHE   A HB2  1 
ATOM   3033 H HB2  B PHE   A 1 132 ? 19.765 -1.269  -6.524  0.58 27.81 ?  132 PHE   A HB2  1 
ATOM   3034 H HB3  A PHE   A 1 132 ? 19.925 -1.571  -6.429  0.42 16.75 ?  132 PHE   A HB3  1 
ATOM   3035 H HB3  B PHE   A 1 132 ? 20.476 -1.886  -7.797  0.58 27.81 ?  132 PHE   A HB3  1 
ATOM   3036 H HD1  A PHE   A 1 132 ? 19.831 1.149   -4.099  0.42 16.29 ?  132 PHE   A HD1  1 
ATOM   3037 H HD1  B PHE   A 1 132 ? 21.232 1.394   -7.739  0.58 28.74 ?  132 PHE   A HD1  1 
ATOM   3038 H HD2  A PHE   A 1 132 ? 22.204 -1.390  -6.080  0.42 16.07 ?  132 PHE   A HD2  1 
ATOM   3039 H HD2  B PHE   A 1 132 ? 22.312 -2.010  -5.935  0.58 27.94 ?  132 PHE   A HD2  1 
ATOM   3040 H HE1  A PHE   A 1 132 ? 21.681 2.067   -3.056  0.42 16.33 ?  132 PHE   A HE1  1 
ATOM   3041 H HE1  B PHE   A 1 132 ? 23.213 2.373   -7.091  0.58 28.76 ?  132 PHE   A HE1  1 
ATOM   3042 H HE2  A PHE   A 1 132 ? 24.051 -0.478  -5.042  0.42 15.71 ?  132 PHE   A HE2  1 
ATOM   3043 H HE2  B PHE   A 1 132 ? 24.296 -1.032  -5.284  0.58 28.17 ?  132 PHE   A HE2  1 
ATOM   3044 H HZ   A PHE   A 1 132 ? 23.793 1.254   -3.528  0.42 15.69 ?  132 PHE   A HZ   1 
ATOM   3045 H HZ   B PHE   A 1 132 ? 24.753 1.160   -5.859  0.58 28.34 ?  132 PHE   A HZ   1 
ATOM   3046 N N    A GLY   A 1 133 ? 16.741 -0.622  -7.860  0.42 15.46 ?  133 GLY   A N    1 
ATOM   3047 N N    B GLY   A 1 133 ? 17.124 -0.833  -8.902  0.58 25.85 ?  133 GLY   A N    1 
ATOM   3048 C CA   A GLY   A 1 133 ? 15.964 -1.009  -9.025  0.42 16.00 ?  133 GLY   A CA   1 
ATOM   3049 C CA   B GLY   A 1 133 ? 16.144 -1.493  -9.742  0.58 27.68 ?  133 GLY   A CA   1 
ATOM   3050 C C    A GLY   A 1 133 ? 15.638 -2.483  -9.196  0.42 15.42 ?  133 GLY   A C    1 
ATOM   3051 C C    B GLY   A 1 133 ? 15.543 -2.738  -9.118  0.58 29.39 ?  133 GLY   A C    1 
ATOM   3052 O O    A GLY   A 1 133 ? 14.946 -2.831  -10.166 0.42 16.41 ?  133 GLY   A O    1 
ATOM   3053 O O    B GLY   A 1 133 ? 14.518 -2.674  -8.433  0.58 30.77 ?  133 GLY   A O    1 
ATOM   3054 H H    A GLY   A 1 133 ? 16.263 -0.400  -7.176  0.42 18.55 ?  133 GLY   A H    1 
ATOM   3055 H H    B GLY   A 1 133 ? 16.785 -0.307  -8.313  0.58 31.02 ?  133 GLY   A H    1 
ATOM   3056 H HA2  A GLY   A 1 133 ? 15.121 -0.533  -9.000  0.42 19.20 ?  133 GLY   A HA2  1 
ATOM   3057 H HA2  B GLY   A 1 133 ? 15.433 -0.864  -9.944  0.58 33.21 ?  133 GLY   A HA2  1 
ATOM   3058 H HA3  A GLY   A 1 133 ? 16.443 -0.724  -9.816  0.42 19.20 ?  133 GLY   A HA3  1 
ATOM   3059 H HA3  B GLY   A 1 133 ? 16.569 -1.743  -10.583 0.58 33.21 ?  133 GLY   A HA3  1 
ATOM   3060 N N    A ALA   A 1 134 ? 16.101 -3.363  -8.308  0.42 14.14 ?  134 ALA   A N    1 
ATOM   3061 N N    B ALA   A 1 134 ? 16.193 -3.874  -9.376  0.58 29.00 ?  134 ALA   A N    1 
ATOM   3062 C CA   A ALA   A 1 134 ? 15.749 -4.769  -8.429  0.42 14.72 ?  134 ALA   A CA   1 
ATOM   3063 C CA   B ALA   A 1 134 ? 15.835 -5.225  -8.941  0.58 28.19 ?  134 ALA   A CA   1 
ATOM   3064 C C    A ALA   A 1 134 ? 14.389 -5.044  -7.787  0.42 14.88 ?  134 ALA   A C    1 
ATOM   3065 C C    B ALA   A 1 134 ? 14.540 -5.377  -8.145  0.58 26.96 ?  134 ALA   A C    1 
ATOM   3066 O O    A ALA   A 1 134 ? 13.827 -4.214  -7.066  0.42 15.77 ?  134 ALA   A O    1 
ATOM   3067 O O    B ALA   A 1 134 ? 14.310 -4.680  -7.151  0.58 27.54 ?  134 ALA   A O    1 
ATOM   3068 C CB   A ALA   A 1 134 ? 16.821 -5.656  -7.800  0.42 14.65 ?  134 ALA   A CB   1 
ATOM   3069 C CB   B ALA   A 1 134 ? 17.014 -5.862  -8.197  0.58 28.42 ?  134 ALA   A CB   1 
ATOM   3070 H H    A ALA   A 1 134 ? 16.609 -3.169  -7.634  0.42 16.96 ?  134 ALA   A H    1 
ATOM   3071 H H    B ALA   A 1 134 ? 16.893 -3.883  -9.859  0.58 34.80 ?  134 ALA   A H    1 
ATOM   3072 H HA   A ALA   A 1 134 ? 15.688 -4.994  -9.366  0.42 17.67 ?  134 ALA   A HA   1 
ATOM   3073 H HA   B ALA   A 1 134 ? 15.708 -5.751  -9.739  0.58 33.82 ?  134 ALA   A HA   1 
ATOM   3074 H HB1  A ALA   A 1 134 ? 16.560 -6.583  -7.908  0.42 17.58 ?  134 ALA   A HB1  1 
ATOM   3075 H HB1  B ALA   A 1 134 ? 16.798 -6.784  -7.992  0.58 34.10 ?  134 ALA   A HB1  1 
ATOM   3076 H HB2  A ALA   A 1 134 ? 17.664 -5.494  -8.250  0.42 17.58 ?  134 ALA   A HB2  1 
ATOM   3077 H HB2  B ALA   A 1 134 ? 17.798 -5.829  -8.774  0.58 34.10 ?  134 ALA   A HB2  1 
ATOM   3078 H HB3  A ALA   A 1 134 ? 16.900 -5.440  -6.859  0.42 17.58 ?  134 ALA   A HB3  1 
ATOM   3079 H HB3  B ALA   A 1 134 ? 17.186 -5.370  -7.383  0.58 34.10 ?  134 ALA   A HB3  1 
ATOM   3080 N N    A ASP   A 1 135 ? 13.866 -6.238  -8.064  0.42 15.03 ?  135 ASP   A N    1 
ATOM   3081 N N    B ASP   A 1 135 ? 13.704 -6.315  -8.583  0.58 25.12 ?  135 ASP   A N    1 
ATOM   3082 C CA   A ASP   A 1 135 ? 12.596 -6.695  -7.506  0.42 15.54 ?  135 ASP   A CA   1 
ATOM   3083 C CA   B ASP   A 1 135 ? 12.455 -6.619  -7.900  0.58 23.80 ?  135 ASP   A CA   1 
ATOM   3084 C C    A ASP   A 1 135 ? 12.802 -7.124  -6.057  0.42 14.44 ?  135 ASP   A C    1 
ATOM   3085 C C    B ASP   A 1 135 ? 12.734 -7.113  -6.481  0.58 21.16 ?  135 ASP   A C    1 
ATOM   3086 O O    A ASP   A 1 135 ? 13.579 -8.053  -5.805  0.42 12.84 ?  135 ASP   A O    1 
ATOM   3087 O O    B ASP   A 1 135 ? 13.551 -8.028  -6.296  0.58 19.92 ?  135 ASP   A O    1 
ATOM   3088 C CB   A ASP   A 1 135 ? 12.108 -7.887  -8.324  0.42 17.66 ?  135 ASP   A CB   1 
ATOM   3089 C CB   B ASP   A 1 135 ? 11.716 -7.700  -8.689  0.58 25.64 ?  135 ASP   A CB   1 
ATOM   3090 C CG   A ASP   A 1 135 ? 10.825 -8.508  -7.785  0.42 19.99 ?  135 ASP   A CG   1 
ATOM   3091 C CG   B ASP   A 1 135 ? 10.302 -7.941  -8.185  0.58 27.31 ?  135 ASP   A CG   1 
ATOM   3092 O OD1  A ASP   A 1 135 ? 10.191 -7.932  -6.876  0.42 20.30 ?  135 ASP   A OD1  1 
ATOM   3093 O OD1  B ASP   A 1 135 ? 9.945  -7.428  -7.103  0.58 28.38 ?  135 ASP   A OD1  1 
ATOM   3094 O OD2  A ASP   A 1 135 ? 10.470 -9.602  -8.271  0.42 22.30 -1 135 ASP   A OD2  1 
ATOM   3095 O OD2  B ASP   A 1 135 ? 9.545  -8.651  -8.877  0.58 27.82 -1 135 ASP   A OD2  1 
ATOM   3096 H H    A ASP   A 1 135 ? 14.244 -6.817  -8.574  0.42 18.04 ?  135 ASP   A H    1 
ATOM   3097 H H    B ASP   A 1 135 ? 13.831 -6.788  -9.290  0.58 30.14 ?  135 ASP   A H    1 
ATOM   3098 H HA   A ASP   A 1 135 ? 11.942 -5.984  -7.552  0.42 18.65 ?  135 ASP   A HA   1 
ATOM   3099 H HA   B ASP   A 1 135 ? 11.903 -5.825  -7.878  0.58 28.56 ?  135 ASP   A HA   1 
ATOM   3100 H HB2  A ASP   A 1 135 ? 11.979 -7.599  -9.242  0.42 21.19 ?  135 ASP   A HB2  1 
ATOM   3101 H HB2  B ASP   A 1 135 ? 11.685 -7.438  -9.625  0.58 30.77 ?  135 ASP   A HB2  1 
ATOM   3102 H HB3  A ASP   A 1 135 ? 12.774 -8.588  -8.288  0.42 21.19 ?  135 ASP   A HB3  1 
ATOM   3103 H HB3  B ASP   A 1 135 ? 12.190 -8.540  -8.600  0.58 30.77 ?  135 ASP   A HB3  1 
ATOM   3104 N N    A PRO   A 1 136 ? 12.146 -6.483  -5.082  0.42 15.24 ?  136 PRO   A N    1 
ATOM   3105 N N    B PRO   A 1 136 ? 12.087 -6.541  -5.462  0.58 20.34 ?  136 PRO   A N    1 
ATOM   3106 C CA   A PRO   A 1 136 ? 12.386 -6.864  -3.679  0.42 14.85 ?  136 PRO   A CA   1 
ATOM   3107 C CA   B PRO   A 1 136 ? 12.341 -6.993  -4.081  0.58 19.37 ?  136 PRO   A CA   1 
ATOM   3108 C C    A PRO   A 1 136 ? 11.935 -8.278  -3.340  0.42 13.33 ?  136 PRO   A C    1 
ATOM   3109 C C    B PRO   A 1 136 ? 11.972 -8.442  -3.809  0.58 18.19 ?  136 PRO   A C    1 
ATOM   3110 O O    A PRO   A 1 136 ? 12.534 -8.905  -2.459  0.42 12.05 ?  136 PRO   A O    1 
ATOM   3111 O O    B PRO   A 1 136 ? 12.599 -9.067  -2.945  0.58 17.23 ?  136 PRO   A O    1 
ATOM   3112 C CB   A PRO   A 1 136 ? 11.631 -5.790  -2.878  0.42 15.84 ?  136 PRO   A CB   1 
ATOM   3113 C CB   B PRO   A 1 136 ? 11.510 -6.018  -3.230  0.58 20.43 ?  136 PRO   A CB   1 
ATOM   3114 C CG   A PRO   A 1 136 ? 10.602 -5.270  -3.818  0.42 17.04 ?  136 PRO   A CG   1 
ATOM   3115 C CG   B PRO   A 1 136 ? 10.567 -5.354  -4.194  0.58 21.55 ?  136 PRO   A CG   1 
ATOM   3116 C CD   A PRO   A 1 136 ? 11.194 -5.363  -5.195  0.42 16.25 ?  136 PRO   A CD   1 
ATOM   3117 C CD   B PRO   A 1 136 ? 11.272 -5.316  -5.497  0.58 21.25 ?  136 PRO   A CD   1 
ATOM   3118 H HA   A PRO   A 1 136 ? 13.332 -6.786  -3.471  0.42 17.82 ?  136 PRO   A HA   1 
ATOM   3119 H HA   B PRO   A 1 136 ? 13.280 -6.874  -3.863  0.58 23.24 ?  136 PRO   A HA   1 
ATOM   3120 H HB2  A PRO   A 1 136 ? 11.215 -6.185  -2.096  0.42 19.01 ?  136 PRO   A HB2  1 
ATOM   3121 H HB2  B PRO   A 1 136 ? 11.021 -6.514  -2.553  0.58 24.52 ?  136 PRO   A HB2  1 
ATOM   3122 H HB3  A PRO   A 1 136 ? 12.244 -5.078  -2.615  0.42 19.01 ?  136 PRO   A HB3  1 
ATOM   3123 H HB3  B PRO   A 1 136 ? 12.099 -5.367  -2.816  0.58 24.52 ?  136 PRO   A HB3  1 
ATOM   3124 H HG2  A PRO   A 1 136 ? 9.806  -5.818  -3.756  0.42 20.45 ?  136 PRO   A HG2  1 
ATOM   3125 H HG2  B PRO   A 1 136 ? 9.755  -5.877  -4.267  0.58 25.87 ?  136 PRO   A HG2  1 
ATOM   3126 H HG3  A PRO   A 1 136 ? 10.399 -4.347  -3.601  0.42 20.45 ?  136 PRO   A HG3  1 
ATOM   3127 H HG3  B PRO   A 1 136 ? 10.373 -4.456  -3.891  0.58 25.87 ?  136 PRO   A HG3  1 
ATOM   3128 H HD2  A PRO   A 1 136 ? 10.505 -5.576  -5.845  0.42 19.51 ?  136 PRO   A HD2  1 
ATOM   3129 H HD2  B PRO   A 1 136 ? 10.635 -5.349  -6.226  0.58 25.50 ?  136 PRO   A HD2  1 
ATOM   3130 H HD3  A PRO   A 1 136 ? 11.659 -4.544  -5.423  0.42 19.51 ?  136 PRO   A HD3  1 
ATOM   3131 H HD3  B PRO   A 1 136 ? 11.843 -4.532  -5.558  0.58 25.50 ?  136 PRO   A HD3  1 
ATOM   3132 N N    A ILE   A 1 137 ? 10.906 -8.801  -4.011  0.42 14.20 ?  137 ILE   A N    1 
ATOM   3133 N N    B ILE   A 1 137 ? 10.966 -8.992  -4.492  0.58 18.30 ?  137 ILE   A N    1 
ATOM   3134 C CA   A ILE   A 1 137 ? 10.546 -10.204 -3.820  0.42 15.11 ?  137 ILE   A CA   1 
ATOM   3135 C CA   B ILE   A 1 137 ? 10.622 -10.398 -4.292  0.58 19.09 ?  137 ILE   A CA   1 
ATOM   3136 C C    A ILE   A 1 137 ? 11.716 -11.101 -4.212  0.42 14.18 ?  137 ILE   A C    1 
ATOM   3137 C C    B ILE   A 1 137 ? 11.807 -11.288 -4.648  0.58 17.67 ?  137 ILE   A C    1 
ATOM   3138 O O    A ILE   A 1 137 ? 12.047 -12.070 -3.514  0.42 14.09 ?  137 ILE   A O    1 
ATOM   3139 O O    B ILE   A 1 137 ? 12.140 -12.234 -3.921  0.58 16.65 ?  137 ILE   A O    1 
ATOM   3140 C CB   A ILE   A 1 137 ? 9.272  -10.537 -4.619  0.42 16.98 ?  137 ILE   A CB   1 
ATOM   3141 C CB   B ILE   A 1 137 ? 9.364  -10.759 -5.102  0.58 21.57 ?  137 ILE   A CB   1 
ATOM   3142 C CG1  A ILE   A 1 137 ? 8.074  -9.741  -4.082  0.42 18.15 ?  137 ILE   A CG1  1 
ATOM   3143 C CG1  B ILE   A 1 137 ? 8.275  -9.698  -4.891  0.58 23.01 ?  137 ILE   A CG1  1 
ATOM   3144 C CG2  A ILE   A 1 137 ? 8.994  -12.035 -4.578  0.42 18.08 ?  137 ILE   A CG2  1 
ATOM   3145 C CG2  B ILE   A 1 137 ? 8.857  -12.132 -4.692  0.58 22.59 ?  137 ILE   A CG2  1 
ATOM   3146 C CD1  A ILE   A 1 137 ? 6.796  -9.952  -4.866  0.42 19.28 ?  137 ILE   A CD1  1 
ATOM   3147 C CD1  B ILE   A 1 137 ? 6.980  -9.981  -5.612  0.58 24.19 ?  137 ILE   A CD1  1 
ATOM   3148 H H    A ILE   A 1 137 ? 10.424 -8.369  -4.577  0.42 17.04 ?  137 ILE   A H    1 
ATOM   3149 H H    B ILE   A 1 137 ? 10.479 -8.574  -5.063  0.58 21.97 ?  137 ILE   A H    1 
ATOM   3150 H HA   A ILE   A 1 137 ? 10.354 -10.348 -2.883  0.42 18.14 ?  137 ILE   A HA   1 
ATOM   3151 H HA   B ILE   A 1 137 ? 10.416 -10.544 -3.355  0.58 22.91 ?  137 ILE   A HA   1 
ATOM   3152 H HB   A ILE   A 1 137 ? 9.411  -10.274 -5.540  0.42 20.38 ?  137 ILE   A HB   1 
ATOM   3153 H HB   B ILE   A 1 137 ? 9.593  -10.784 -6.043  0.58 25.88 ?  137 ILE   A HB   1 
ATOM   3154 H HG12 A ILE   A 1 137 ? 7.905  -10.004 -3.164  0.42 21.78 ?  137 ILE   A HG12 1 
ATOM   3155 H HG12 B ILE   A 1 137 ? 8.086  -9.633  -3.942  0.58 27.62 ?  137 ILE   A HG12 1 
ATOM   3156 H HG13 A ILE   A 1 137 ? 8.285  -8.791  -4.115  0.42 21.78 ?  137 ILE   A HG13 1 
ATOM   3157 H HG13 B ILE   A 1 137 ? 8.595  -8.841  -5.219  0.58 27.62 ?  137 ILE   A HG13 1 
ATOM   3158 H HG21 A ILE   A 1 137 ? 8.209  -12.230 -5.112  0.42 21.69 ?  137 ILE   A HG21 1 
ATOM   3159 H HG21 B ILE   A 1 137 ? 8.118  -12.383 -5.268  0.58 27.11 ?  137 ILE   A HG21 1 
ATOM   3160 H HG22 A ILE   A 1 137 ? 9.748  -12.512 -4.943  0.42 21.69 ?  137 ILE   A HG22 1 
ATOM   3161 H HG22 B ILE   A 1 137 ? 9.576  -12.774 -4.780  0.58 27.11 ?  137 ILE   A HG22 1 
ATOM   3162 H HG23 A ILE   A 1 137 ? 8.841  -12.298 -3.658  0.42 21.69 ?  137 ILE   A HG23 1 
ATOM   3163 H HG23 B ILE   A 1 137 ? 8.558  -12.092 -3.770  0.58 27.11 ?  137 ILE   A HG23 1 
ATOM   3164 H HD11 A ILE   A 1 137 ? 6.072  -9.563  -4.362  0.42 23.13 ?  137 ILE   A HD11 1 
ATOM   3165 H HD11 B ILE   A 1 137 ? 6.530  -9.141  -5.791  0.58 29.03 ?  137 ILE   A HD11 1 
ATOM   3166 H HD12 A ILE   A 1 137 ? 6.877  -9.520  -5.732  0.42 23.13 ?  137 ILE   A HD12 1 
ATOM   3167 H HD12 B ILE   A 1 137 ? 7.179  -10.433 -6.445  0.58 29.03 ?  137 ILE   A HD12 1 
ATOM   3168 H HD13 A ILE   A 1 137 ? 6.630  -10.900 -4.983  0.42 23.13 ?  137 ILE   A HD13 1 
ATOM   3169 H HD13 B ILE   A 1 137 ? 6.427  -10.546 -5.052  0.58 29.03 ?  137 ILE   A HD13 1 
ATOM   3170 N N    A HIS   A 1 138 ? 12.352 -10.794 -5.342  0.42 14.23 ?  138 HIS   A N    1 
ATOM   3171 N N    B HIS   A 1 138 ? 12.465 -10.996 -5.769  0.58 17.68 ?  138 HIS   A N    1 
ATOM   3172 C CA   A HIS   A 1 138 ? 13.518 -11.558 -5.771  0.42 13.84 ?  138 HIS   A CA   1 
ATOM   3173 C CA   B HIS   A 1 138 ? 13.657 -11.750 -6.137  0.58 17.07 ?  138 HIS   A CA   1 
ATOM   3174 C C    A HIS   A 1 138 ? 14.681 -11.384 -4.801  0.42 13.24 ?  138 HIS   A C    1 
ATOM   3175 C C    B HIS   A 1 138 ? 14.760 -11.587 -5.097  0.58 16.05 ?  138 HIS   A C    1 
ATOM   3176 O O    A HIS   A 1 138 ? 15.329 -12.364 -4.413  0.42 12.93 ?  138 HIS   A O    1 
ATOM   3177 O O    B HIS   A 1 138 ? 15.466 -12.550 -4.776  0.58 16.16 ?  138 HIS   A O    1 
ATOM   3178 C CB   A HIS   A 1 138 ? 13.916 -11.143 -7.187  0.42 14.64 ?  138 HIS   A CB   1 
ATOM   3179 C CB   B HIS   A 1 138 ? 14.147 -11.319 -7.519  0.58 18.05 ?  138 HIS   A CB   1 
ATOM   3180 C CG   A HIS   A 1 138 ? 15.181 -11.780 -7.668  0.42 15.69 ?  138 HIS   A CG   1 
ATOM   3181 C CG   B HIS   A 1 138 ? 15.436 -11.964 -7.927  0.58 18.47 ?  138 HIS   A CG   1 
ATOM   3182 N ND1  A HIS   A 1 138 ? 15.280 -13.128 -7.944  0.42 16.61 ?  138 HIS   A ND1  1 
ATOM   3183 N ND1  B HIS   A 1 138 ? 15.548 -13.317 -8.168  0.58 19.12 ?  138 HIS   A ND1  1 
ATOM   3184 C CD2  A HIS   A 1 138 ? 16.404 -11.254 -7.913  0.42 16.25 ?  138 HIS   A CD2  1 
ATOM   3185 C CD2  B HIS   A 1 138 ? 16.670 -11.443 -8.124  0.58 19.07 ?  138 HIS   A CD2  1 
ATOM   3186 C CE1  A HIS   A 1 138 ? 16.509 -13.402 -8.343  0.42 16.89 ?  138 HIS   A CE1  1 
ATOM   3187 C CE1  B HIS   A 1 138 ? 16.793 -13.599 -8.504  0.58 19.37 ?  138 HIS   A CE1  1 
ATOM   3188 N NE2  A HIS   A 1 138 ? 17.212 -12.284 -8.331  0.42 16.69 ?  138 HIS   A NE2  1 
ATOM   3189 N NE2  B HIS   A 1 138 ? 17.495 -12.481 -8.483  0.58 19.29 ?  138 HIS   A NE2  1 
ATOM   3190 H H    A HIS   A 1 138 ? 12.128 -10.153 -5.872  0.42 17.08 ?  138 HIS   A H    1 
ATOM   3191 H H    B HIS   A 1 138 ? 12.247 -10.370 -6.320  0.58 21.22 ?  138 HIS   A H    1 
ATOM   3192 H HA   A HIS   A 1 138 ? 13.284 -12.495 -5.789  0.42 16.61 ?  138 HIS   A HA   1 
ATOM   3193 H HA   B HIS   A 1 138 ? 13.430 -12.689 -6.184  0.58 20.49 ?  138 HIS   A HA   1 
ATOM   3194 H HB2  A HIS   A 1 138 ? 13.205 -11.396 -7.797  0.42 17.57 ?  138 HIS   A HB2  1 
ATOM   3195 H HB2  B HIS   A 1 138 ? 13.473 -11.555 -8.177  0.58 21.66 ?  138 HIS   A HB2  1 
ATOM   3196 H HB3  A HIS   A 1 138 ? 14.041 -10.182 -7.209  0.42 17.57 ?  138 HIS   A HB3  1 
ATOM   3197 H HB3  B HIS   A 1 138 ? 14.282 -10.358 -7.520  0.58 21.66 ?  138 HIS   A HB3  1 
ATOM   3198 H HD1  A HIS   A 1 138 ? 14.640 -13.699 -7.870  0.42 19.93 ?  138 HIS   A HD1  1 
ATOM   3199 H HD2  A HIS   A 1 138 ? 16.650 -10.364 -7.818  0.42 19.50 ?  138 HIS   A HD2  1 
ATOM   3200 H HD2  B HIS   A 1 138 ? 16.911 -10.551 -8.035  0.58 22.89 ?  138 HIS   A HD2  1 
ATOM   3201 H HE1  A HIS   A 1 138 ? 16.825 -14.242 -8.590  0.42 20.27 ?  138 HIS   A HE1  1 
ATOM   3202 H HE1  B HIS   A 1 138 ? 17.116 -14.444 -8.718  0.58 23.25 ?  138 HIS   A HE1  1 
ATOM   3203 H HE2  B HIS   A 1 138 ? 18.329 -12.414 -8.667  0.58 23.15 ?  138 HIS   A HE2  1 
ATOM   3204 N N    A SER   A 1 139 ? 14.967 -10.142 -4.400  0.42 12.96 ?  139 SER   A N    1 
ATOM   3205 N N    B SER   A 1 139 ? 14.923 -10.379 -4.553  0.58 14.53 ?  139 SER   A N    1 
ATOM   3206 C CA   A SER   A 1 139 ? 16.030 -9.908  -3.430  0.42 12.99 ?  139 SER   A CA   1 
ATOM   3207 C CA   B SER   A 1 139 ? 15.999 -10.143 -3.595  0.58 13.49 ?  139 SER   A CA   1 
ATOM   3208 C C    A SER   A 1 139 ? 15.818 -10.739 -2.173  0.42 12.80 ?  139 SER   A C    1 
ATOM   3209 C C    B SER   A 1 139 ? 15.785 -10.932 -2.306  0.58 12.95 ?  139 SER   A C    1 
ATOM   3210 O O    A SER   A 1 139 ? 16.783 -11.229 -1.573  0.42 12.70 ?  139 SER   A O    1 
ATOM   3211 O O    B SER   A 1 139 ? 16.724 -11.544 -1.784  0.58 12.60 ?  139 SER   A O    1 
ATOM   3212 C CB   A SER   A 1 139 ? 16.116 -8.418  -3.090  0.42 13.14 ?  139 SER   A CB   1 
ATOM   3213 C CB   B SER   A 1 139 ? 16.141 -8.647  -3.309  0.58 13.00 ?  139 SER   A CB   1 
ATOM   3214 O OG   A SER   A 1 139 ? 17.101 -8.201  -2.095  0.42 13.43 ?  139 SER   A OG   1 
ATOM   3215 O OG   B SER   A 1 139 ? 17.257 -8.419  -2.468  0.58 12.03 ?  139 SER   A OG   1 
ATOM   3216 H H    A SER   A 1 139 ? 14.567 -9.430  -4.663  0.42 15.56 ?  139 SER   A H    1 
ATOM   3217 H H    B SER   A 1 139 ? 14.436 -9.692  -4.719  0.58 17.43 ?  139 SER   A H    1 
ATOM   3218 H HA   A SER   A 1 139 ? 16.880 -10.171 -3.807  0.42 15.59 ?  139 SER   A HA   1 
ATOM   3219 H HA   B SER   A 1 139 ? 16.837 -10.440 -3.986  0.58 16.19 ?  139 SER   A HA   1 
ATOM   3220 H HB2  A SER   A 1 139 ? 16.354 -7.921  -3.892  0.42 15.77 ?  139 SER   A HB2  1 
ATOM   3221 H HB2  B SER   A 1 139 ? 16.284 -8.172  -4.142  0.58 15.60 ?  139 SER   A HB2  1 
ATOM   3222 H HB3  A SER   A 1 139 ? 15.261 -8.109  -2.754  0.42 15.77 ?  139 SER   A HB3  1 
ATOM   3223 H HB3  B SER   A 1 139 ? 15.342 -8.326  -2.868  0.58 15.60 ?  139 SER   A HB3  1 
ATOM   3224 H HG   A SER   A 1 139 ? 17.874 -8.298  -2.414  0.42 16.12 ?  139 SER   A HG   1 
ATOM   3225 H HG   B SER   A 1 139 ? 17.343 -7.600  -2.300  0.58 14.44 ?  139 SER   A HG   1 
ATOM   3226 N N    . LEU   A 1 140 ? 14.561 -10.919 -1.766  1.00 13.30 ?  140 LEU   A N    1 
ATOM   3227 C CA   . LEU   A 1 140 ? 14.284 -11.726 -0.582  1.00 13.30 ?  140 LEU   A CA   1 
ATOM   3228 C C    . LEU   A 1 140 ? 14.567 -13.203 -0.845  1.00 13.35 ?  140 LEU   A C    1 
ATOM   3229 O O    . LEU   A 1 140 ? 15.128 -13.899 0.012   1.00 13.83 ?  140 LEU   A O    1 
ATOM   3230 C CB   . LEU   A 1 140 ? 12.835 -11.527 -0.139  1.00 13.62 ?  140 LEU   A CB   1 
ATOM   3231 C CG   . LEU   A 1 140 ? 12.392 -12.356 1.069   1.00 14.14 ?  140 LEU   A CG   1 
ATOM   3232 C CD1  . LEU   A 1 140 ? 13.260 -12.097 2.296   1.00 14.59 ?  140 LEU   A CD1  1 
ATOM   3233 C CD2  . LEU   A 1 140 ? 10.917 -12.094 1.377   1.00 15.54 ?  140 LEU   A CD2  1 
ATOM   3234 H H    A LEU   A 1 140 ? 13.868 -10.591 -2.150  0.42 15.96 ?  140 LEU   A H    1 
ATOM   3235 H H    B LEU   A 1 140 ? 13.898 -10.452 -2.050  0.58 15.96 ?  140 LEU   A H    1 
ATOM   3236 H HA   . LEU   A 1 140 ? 14.857 -11.435 0.146   1.00 15.96 ?  140 LEU   A HA   1 
ATOM   3237 H HB2  . LEU   A 1 140 ? 12.706 -10.597 0.092   1.00 16.35 ?  140 LEU   A HB2  1 
ATOM   3238 H HB3  . LEU   A 1 140 ? 12.253 -11.765 -0.876  1.00 16.35 ?  140 LEU   A HB3  1 
ATOM   3239 H HG   . LEU   A 1 140 ? 12.473 -13.299 0.850   1.00 16.97 ?  140 LEU   A HG   1 
ATOM   3240 H HD11 . LEU   A 1 140 ? 12.884 -12.577 3.055   1.00 17.51 ?  140 LEU   A HD11 1 
ATOM   3241 H HD12 . LEU   A 1 140 ? 14.158 -12.416 2.120   1.00 17.51 ?  140 LEU   A HD12 1 
ATOM   3242 H HD13 . LEU   A 1 140 ? 13.270 -11.147 2.480   1.00 17.51 ?  140 LEU   A HD13 1 
ATOM   3243 H HD21 . LEU   A 1 140 ? 10.651 -12.632 2.144   1.00 18.65 ?  140 LEU   A HD21 1 
ATOM   3244 H HD22 . LEU   A 1 140 ? 10.794 -11.156 1.575   1.00 18.65 ?  140 LEU   A HD22 1 
ATOM   3245 H HD23 . LEU   A 1 140 ? 10.382 -12.345 0.605   1.00 18.65 ?  140 LEU   A HD23 1 
ATOM   3246 N N    A ARG   A 1 141 ? 14.176 -13.696 -2.023  0.42 14.12 ?  141 ARG   A N    1 
ATOM   3247 N N    B ARG   A 1 141 ? 14.174 -13.703 -2.020  0.58 13.90 ?  141 ARG   A N    1 
ATOM   3248 C CA   A ARG   A 1 141 ? 14.428 -15.089 -2.384  0.42 15.23 ?  141 ARG   A CA   1 
ATOM   3249 C CA   B ARG   A 1 141 ? 14.432 -15.099 -2.364  0.58 14.85 ?  141 ARG   A CA   1 
ATOM   3250 C C    A ARG   A 1 141 ? 15.923 -15.389 -2.376  0.42 14.14 ?  141 ARG   A C    1 
ATOM   3251 C C    B ARG   A 1 141 ? 15.929 -15.391 -2.371  0.58 13.87 ?  141 ARG   A C    1 
ATOM   3252 O O    A ARG   A 1 141 ? 16.365 -16.398 -1.816  0.42 14.18 ?  141 ARG   A O    1 
ATOM   3253 O O    B ARG   A 1 141 ? 16.380 -16.398 -1.814  0.58 13.94 ?  141 ARG   A O    1 
ATOM   3254 C CB   A ARG   A 1 141 ? 13.833 -15.359 -3.768  0.42 17.43 ?  141 ARG   A CB   1 
ATOM   3255 C CB   B ARG   A 1 141 ? 13.813 -15.402 -3.731  0.58 16.96 ?  141 ARG   A CB   1 
ATOM   3256 C CG   A ARG   A 1 141 ? 13.799 -16.816 -4.187  0.42 20.37 ?  141 ARG   A CG   1 
ATOM   3257 C CG   B ARG   A 1 141 ? 13.914 -16.850 -4.177  0.58 20.41 ?  141 ARG   A CG   1 
ATOM   3258 C CD   A ARG   A 1 141 ? 12.746 -17.572 -3.413  0.42 22.68 ?  141 ARG   A CD   1 
ATOM   3259 C CD   B ARG   A 1 141 ? 12.892 -17.703 -3.467  0.58 23.07 ?  141 ARG   A CD   1 
ATOM   3260 N NE   A ARG   A 1 141 ? 13.331 -18.385 -2.357  0.42 24.08 ?  141 ARG   A NE   1 
ATOM   3261 N NE   B ARG   A 1 141 ? 13.492 -18.520 -2.422  0.58 24.67 ?  141 ARG   A NE   1 
ATOM   3262 C CZ   A ARG   A 1 141 ? 12.636 -18.950 -1.379  0.42 24.95 ?  141 ARG   A CZ   1 
ATOM   3263 C CZ   B ARG   A 1 141 ? 12.804 -19.122 -1.462  0.58 25.42 ?  141 ARG   A CZ   1 
ATOM   3264 N NH1  A ARG   A 1 141 ? 11.332 -18.758 -1.258  0.42 25.37 ?  141 ARG   A NH1  1 
ATOM   3265 N NH1  B ARG   A 1 141 ? 11.496 -18.961 -1.342  0.58 25.93 ?  141 ARG   A NH1  1 
ATOM   3266 N NH2  A ARG   A 1 141 ? 13.265 -19.720 -0.497  0.42 25.32 ?  141 ARG   A NH2  1 
ATOM   3267 N NH2  B ARG   A 1 141 ? 13.445 -19.901 -0.595  0.58 25.70 ?  141 ARG   A NH2  1 
ATOM   3268 H H    A ARG   A 1 141 ? 13.764 -13.244 -2.626  0.42 16.95 ?  141 ARG   A H    1 
ATOM   3269 H H    B ARG   A 1 141 ? 13.760 -13.256 -2.625  0.58 16.68 ?  141 ARG   A H    1 
ATOM   3270 H HA   A ARG   A 1 141 ? 13.996 -15.673 -1.743  0.42 18.27 ?  141 ARG   A HA   1 
ATOM   3271 H HA   B ARG   A 1 141 ? 14.013 -15.673 -1.707  0.58 17.82 ?  141 ARG   A HA   1 
ATOM   3272 H HB2  A ARG   A 1 141 ? 12.922 -15.026 -3.783  0.42 20.92 ?  141 ARG   A HB2  1 
ATOM   3273 H HB2  B ARG   A 1 141 ? 12.873 -15.162 -3.706  0.58 20.35 ?  141 ARG   A HB2  1 
ATOM   3274 H HB3  A ARG   A 1 141 ? 14.361 -14.881 -4.426  0.42 20.92 ?  141 ARG   A HB3  1 
ATOM   3275 H HB3  B ARG   A 1 141 ? 14.264 -14.862 -4.398  0.58 20.35 ?  141 ARG   A HB3  1 
ATOM   3276 H HG2  A ARG   A 1 141 ? 13.587 -16.875 -5.132  0.42 24.44 ?  141 ARG   A HG2  1 
ATOM   3277 H HG2  B ARG   A 1 141 ? 13.747 -16.906 -5.132  0.58 24.50 ?  141 ARG   A HG2  1 
ATOM   3278 H HG3  A ARG   A 1 141 ? 14.662 -17.225 -4.011  0.42 24.44 ?  141 ARG   A HG3  1 
ATOM   3279 H HG3  B ARG   A 1 141 ? 14.797 -17.198 -3.972  0.58 24.50 ?  141 ARG   A HG3  1 
ATOM   3280 H HD2  A ARG   A 1 141 ? 12.135 -16.942 -3.001  0.42 27.22 ?  141 ARG   A HD2  1 
ATOM   3281 H HD2  B ARG   A 1 141 ? 12.227 -17.130 -3.050  0.58 27.69 ?  141 ARG   A HD2  1 
ATOM   3282 H HD3  A ARG   A 1 141 ? 12.263 -18.156 -4.020  0.42 27.22 ?  141 ARG   A HD3  1 
ATOM   3283 H HD3  B ARG   A 1 141 ? 12.463 -18.290 -4.111  0.58 27.69 ?  141 ARG   A HD3  1 
ATOM   3284 H HE   A ARG   A 1 141 ? 14.169 -18.568 -2.409  0.42 28.90 ?  141 ARG   A HE   1 
ATOM   3285 H HE   B ARG   A 1 141 ? 14.330 -18.696 -2.485  0.58 29.60 ?  141 ARG   A HE   1 
ATOM   3286 H HH11 A ARG   A 1 141 ? 10.912 -18.266 -1.824  0.42 30.45 ?  141 ARG   A HH11 1 
ATOM   3287 H HH11 B ARG   A 1 141 ? 11.066 -18.465 -1.898  0.58 31.11 ?  141 ARG   A HH11 1 
ATOM   3288 H HH12 A ARG   A 1 141 ? 10.901 -19.132 -0.613  0.42 30.45 ?  141 ARG   A HH12 1 
ATOM   3289 H HH12 B ARG   A 1 141 ? 11.070 -19.358 -0.708  0.58 31.11 ?  141 ARG   A HH12 1 
ATOM   3290 H HH21 A ARG   A 1 141 ? 14.112 -19.852 -0.569  0.42 30.38 ?  141 ARG   A HH21 1 
ATOM   3291 H HH21 B ARG   A 1 141 ? 14.295 -20.012 -0.665  0.58 30.84 ?  141 ARG   A HH21 1 
ATOM   3292 H HH22 A ARG   A 1 141 ? 12.826 -20.087 0.144   0.42 30.38 ?  141 ARG   A HH22 1 
ATOM   3293 H HH22 B ARG   A 1 141 ? 13.011 -20.291 0.037   0.58 30.84 ?  141 ARG   A HH22 1 
ATOM   3294 N N    . VAL   A 1 142 ? 16.719 -14.520 -3.001  1.00 13.34 ?  142 VAL   A N    1 
ATOM   3295 C CA   . VAL   A 1 142 ? 18.164 -14.723 -3.022  1.00 13.18 ?  142 VAL   A CA   1 
ATOM   3296 C C    . VAL   A 1 142 ? 18.728 -14.677 -1.610  1.00 12.74 ?  142 VAL   A C    1 
ATOM   3297 O O    . VAL   A 1 142 ? 19.582 -15.491 -1.244  1.00 13.08 ?  142 VAL   A O    1 
ATOM   3298 C CB   . VAL   A 1 142 ? 18.854 -13.702 -3.947  1.00 13.73 ?  142 VAL   A CB   1 
ATOM   3299 C CG1  . VAL   A 1 142 ? 20.368 -13.901 -3.913  1.00 13.32 ?  142 VAL   A CG1  1 
ATOM   3300 C CG2  . VAL   A 1 142 ? 18.350 -13.840 -5.368  1.00 15.69 ?  142 VAL   A CG2  1 
ATOM   3301 H H    A VAL   A 1 142 ? 16.451 -13.814 -3.416  0.42 16.01 ?  142 VAL   A H    1 
ATOM   3302 H H    B VAL   A 1 142 ? 16.449 -13.815 -3.417  0.58 16.01 ?  142 VAL   A H    1 
ATOM   3303 H HA   . VAL   A 1 142 ? 18.349 -15.600 -3.378  1.00 15.81 ?  142 VAL   A HA   1 
ATOM   3304 H HB   . VAL   A 1 142 ? 18.663 -12.798 -3.637  1.00 16.48 ?  142 VAL   A HB   1 
ATOM   3305 H HG11 . VAL   A 1 142 ? 20.767 -13.405 -4.646  1.00 15.99 ?  142 VAL   A HG11 1 
ATOM   3306 H HG12 . VAL   A 1 142 ? 20.716 -13.571 -3.068  1.00 15.99 ?  142 VAL   A HG12 1 
ATOM   3307 H HG13 . VAL   A 1 142 ? 20.563 -14.845 -4.007  1.00 15.99 ?  142 VAL   A HG13 1 
ATOM   3308 H HG21 . VAL   A 1 142 ? 18.719 -13.117 -5.901  1.00 18.83 ?  142 VAL   A HG21 1 
ATOM   3309 H HG22 . VAL   A 1 142 ? 18.643 -14.692 -5.718  1.00 18.83 ?  142 VAL   A HG22 1 
ATOM   3310 H HG23 . VAL   A 1 142 ? 17.386 -13.790 -5.366  1.00 18.83 ?  142 VAL   A HG23 1 
ATOM   3311 N N    . CYS   A 1 143 ? 18.256 -13.738 -0.789  1.00 12.32 ?  143 CYS   A N    1 
ATOM   3312 C CA   . CYS   A 1 143 ? 18.715 -13.675 0.595   1.00 12.74 ?  143 CYS   A CA   1 
ATOM   3313 C C    . CYS   A 1 143 ? 18.474 -15.003 1.306   1.00 12.34 ?  143 CYS   A C    1 
ATOM   3314 O O    . CYS   A 1 143 ? 19.387 -15.581 1.907   1.00 12.45 ?  143 CYS   A O    1 
ATOM   3315 C CB   . CYS   A 1 143 ? 17.993 -12.543 1.322   1.00 13.24 ?  143 CYS   A CB   1 
ATOM   3316 S SG   . CYS   A 1 143 ? 18.477 -12.334 3.037   1.00 13.64 ?  143 CYS   A SG   1 
ATOM   3317 H H    . CYS   A 1 143 ? 17.672 -13.144 -1.001  1.00 14.79 ?  143 CYS   A H    1 
ATOM   3318 H HA   . CYS   A 1 143 ? 19.666 -13.493 0.610   1.00 15.29 ?  143 CYS   A HA   1 
ATOM   3319 H HB2  . CYS   A 1 143 ? 18.166 -11.712 0.861   1.00 15.89 ?  143 CYS   A HB2  1 
ATOM   3320 H HB3  . CYS   A 1 143 ? 17.042 -12.727 1.308   1.00 15.89 ?  143 CYS   A HB3  1 
ATOM   3321 H HG   . CYS   A 1 143 ? 19.644 -12.098 3.091   1.00 16.36 ?  143 CYS   A HG   1 
ATOM   3322 N N    . VAL   A 1 144 ? 17.240 -15.503 1.242   1.00 13.03 ?  144 VAL   A N    1 
ATOM   3323 C CA   . VAL   A 1 144 ? 16.879 -16.736 1.937   1.00 14.31 ?  144 VAL   A CA   1 
ATOM   3324 C C    . VAL   A 1 144 ? 17.713 -17.910 1.446   1.00 13.83 ?  144 VAL   A C    1 
ATOM   3325 O O    . VAL   A 1 144 ? 18.094 -18.787 2.231   1.00 14.58 ?  144 VAL   A O    1 
ATOM   3326 C CB   . VAL   A 1 144 ? 15.368 -16.983 1.765   1.00 16.10 ?  144 VAL   A CB   1 
ATOM   3327 C CG1  . VAL   A 1 144 ? 15.001 -18.422 2.082   1.00 17.68 ?  144 VAL   A CG1  1 
ATOM   3328 C CG2  . VAL   A 1 144 ? 14.587 -15.997 2.630   1.00 16.77 ?  144 VAL   A CG2  1 
ATOM   3329 H H    . VAL   A 1 144 ? 16.592 -15.141 0.799   1.00 15.64 ?  144 VAL   A H    1 
ATOM   3330 H HA   . VAL   A 1 144 ? 17.048 -16.619 2.879   1.00 17.17 ?  144 VAL   A HA   1 
ATOM   3331 H HB   . VAL   A 1 144 ? 15.122 -16.811 0.839   1.00 19.32 ?  144 VAL   A HB   1 
ATOM   3332 H HG11 . VAL   A 1 144 ? 14.042 -18.475 2.226   1.00 21.22 ?  144 VAL   A HG11 1 
ATOM   3333 H HG12 . VAL   A 1 144 ? 15.252 -18.984 1.334   1.00 21.22 ?  144 VAL   A HG12 1 
ATOM   3334 H HG13 . VAL   A 1 144 ? 15.470 -18.695 2.883   1.00 21.22 ?  144 VAL   A HG13 1 
ATOM   3335 H HG21 . VAL   A 1 144 ? 13.634 -16.169 2.537   1.00 20.12 ?  144 VAL   A HG21 1 
ATOM   3336 H HG22 . VAL   A 1 144 ? 14.849 -16.105 3.557   1.00 20.12 ?  144 VAL   A HG22 1 
ATOM   3337 H HG23 . VAL   A 1 144 ? 14.781 -15.088 2.339   1.00 20.12 ?  144 VAL   A HG23 1 
ATOM   3338 N N    . ASP   A 1 145 ? 17.991 -17.959 0.147   1.00 14.36 ?  145 ASP   A N    1 
ATOM   3339 C CA   . ASP   A 1 145 ? 18.720 -19.070 -0.453  1.00 14.88 ?  145 ASP   A CA   1 
ATOM   3340 C C    . ASP   A 1 145 ? 20.237 -18.911 -0.389  1.00 14.53 ?  145 ASP   A C    1 
ATOM   3341 O O    . ASP   A 1 145 ? 20.951 -19.811 -0.839  1.00 16.66 ?  145 ASP   A O    1 
ATOM   3342 C CB   . ASP   A 1 145 ? 18.299 -19.234 -1.917  1.00 16.91 ?  145 ASP   A CB   1 
ATOM   3343 C CG   . ASP   A 1 145 ? 16.857 -19.676 -2.070  1.00 19.63 ?  145 ASP   A CG   1 
ATOM   3344 O OD1  . ASP   A 1 145 ? 16.262 -20.180 -1.091  1.00 20.37 ?  145 ASP   A OD1  1 
ATOM   3345 O OD2  . ASP   A 1 145 ? 16.320 -19.520 -3.186  1.00 21.00 -1 145 ASP   A OD2  1 
ATOM   3346 H H    . ASP   A 1 145 ? 17.759 -17.353 -0.419  1.00 17.23 ?  145 ASP   A H    1 
ATOM   3347 H HA   . ASP   A 1 145 ? 18.485 -19.887 0.015   1.00 17.86 ?  145 ASP   A HA   1 
ATOM   3348 H HB2  . ASP   A 1 145 ? 18.406 -18.385 -2.372  1.00 20.29 ?  145 ASP   A HB2  1 
ATOM   3349 H HB3  . ASP   A 1 145 ? 18.860 -19.907 -2.332  1.00 20.29 ?  145 ASP   A HB3  1 
ATOM   3350 N N    . THR   A 1 146 ? 20.747 -17.805 0.144   1.00 12.55 ?  146 THR   A N    1 
ATOM   3351 C CA   . THR   A 1 146 ? 22.185 -17.543 0.171   1.00 12.27 ?  146 THR   A CA   1 
ATOM   3352 C C    . THR   A 1 146 ? 22.736 -17.358 1.573   1.00 11.99 ?  146 THR   A C    1 
ATOM   3353 O O    . THR   A 1 146 ? 23.810 -17.895 1.893   1.00 12.88 ?  146 THR   A O    1 
ATOM   3354 C CB   . THR   A 1 146 ? 22.506 -16.292 -0.670  1.00 12.25 ?  146 THR   A CB   1 
ATOM   3355 O OG1  . THR   A 1 146 ? 22.005 -16.475 -1.996  1.00 12.79 ?  146 THR   A OG1  1 
ATOM   3356 C CG2  . THR   A 1 146 ? 24.002 -16.033 -0.730  1.00 13.02 ?  146 THR   A CG2  1 
ATOM   3357 H H    . THR   A 1 146 ? 20.272 -17.175 0.499   1.00 15.06 ?  146 THR   A H    1 
ATOM   3358 H HA   . THR   A 1 146 ? 22.649 -18.284 -0.229  1.00 14.72 ?  146 THR   A HA   1 
ATOM   3359 H HB   . THR   A 1 146 ? 22.079 -15.512 -0.277  1.00 14.69 ?  146 THR   A HB   1 
ATOM   3360 H HG1  . THR   A 1 146 ? 21.175 -16.578 -1.976  1.00 15.35 ?  146 THR   A HG1  1 
ATOM   3361 H HG21 . THR   A 1 146 ? 24.195 -15.377 -1.418  1.00 15.62 ?  146 THR   A HG21 1 
ATOM   3362 H HG22 . THR   A 1 146 ? 24.313 -15.689 0.124   1.00 15.62 ?  146 THR   A HG22 1 
ATOM   3363 H HG23 . THR   A 1 146 ? 24.469 -16.853 -0.932  1.00 15.62 ?  146 THR   A HG23 1 
ATOM   3364 N N    . VAL   A 1 147 ? 22.046 -16.593 2.409   1.00 11.84 ?  147 VAL   A N    1 
ATOM   3365 C CA   . VAL   A 1 147 ? 22.527 -16.283 3.745   1.00 12.21 ?  147 VAL   A CA   1 
ATOM   3366 C C    . VAL   A 1 147 ? 22.194 -17.448 4.663   1.00 12.45 ?  147 VAL   A C    1 
ATOM   3367 O O    . VAL   A 1 147 ? 21.049 -17.922 4.701   1.00 12.97 ?  147 VAL   A O    1 
ATOM   3368 C CB   . VAL   A 1 147 ? 21.893 -14.977 4.248   1.00 12.35 ?  147 VAL   A CB   1 
ATOM   3369 C CG1  . VAL   A 1 147 ? 22.406 -14.640 5.626   1.00 13.19 ?  147 VAL   A CG1  1 
ATOM   3370 C CG2  . VAL   A 1 147 ? 22.159 -13.835 3.256   1.00 12.43 ?  147 VAL   A CG2  1 
ATOM   3371 H H    . VAL   A 1 147 ? 21.286 -16.239 2.226   1.00 14.21 ?  147 VAL   A H    1 
ATOM   3372 H HA   . VAL   A 1 147 ? 23.490 -16.169 3.727   1.00 14.65 ?  147 VAL   A HA   1 
ATOM   3373 H HB   . VAL   A 1 147 ? 20.934 -15.101 4.313   1.00 14.82 ?  147 VAL   A HB   1 
ATOM   3374 H HG11 . VAL   A 1 147 ? 22.134 -13.737 5.850   1.00 15.83 ?  147 VAL   A HG11 1 
ATOM   3375 H HG12 . VAL   A 1 147 ? 22.029 -15.265 6.267   1.00 15.83 ?  147 VAL   A HG12 1 
ATOM   3376 H HG13 . VAL   A 1 147 ? 23.373 -14.705 5.628   1.00 15.83 ?  147 VAL   A HG13 1 
ATOM   3377 H HG21 . VAL   A 1 147 ? 21.827 -13.005 3.638   1.00 14.92 ?  147 VAL   A HG21 1 
ATOM   3378 H HG22 . VAL   A 1 147 ? 23.108 -13.771 3.094   1.00 14.92 ?  147 VAL   A HG22 1 
ATOM   3379 H HG23 . VAL   A 1 147 ? 21.688 -14.024 2.427   1.00 14.92 ?  147 VAL   A HG23 1 
ATOM   3380 N N    . ARG   A 1 148 ? 23.205 -17.911 5.397   1.00 12.61 ?  148 ARG   A N    1 
ATOM   3381 C CA   . ARG   A 1 148 ? 23.074 -18.984 6.367   1.00 13.03 ?  148 ARG   A CA   1 
ATOM   3382 C C    . ARG   A 1 148 ? 23.189 -18.505 7.803   1.00 12.90 ?  148 ARG   A C    1 
ATOM   3383 O O    . ARG   A 1 148 ? 22.787 -19.227 8.721   1.00 14.03 ?  148 ARG   A O    1 
ATOM   3384 C CB   . ARG   A 1 148 ? 24.125 -20.072 6.101   1.00 13.95 ?  148 ARG   A CB   1 
ATOM   3385 C CG   . ARG   A 1 148 ? 23.967 -20.717 4.736   1.00 14.87 ?  148 ARG   A CG   1 
ATOM   3386 C CD   . ARG   A 1 148 ? 25.064 -21.751 4.454   1.00 15.87 ?  148 ARG   A CD   1 
ATOM   3387 N NE   . ARG   A 1 148 ? 26.403 -21.174 4.466   1.00 15.97 ?  148 ARG   A NE   1 
ATOM   3388 C CZ   . ARG   A 1 148 ? 26.915 -20.453 3.475   1.00 14.98 ?  148 ARG   A CZ   1 
ATOM   3389 N NH1  . ARG   A 1 148 ? 26.235 -20.234 2.360   1.00 15.45 ?  148 ARG   A NH1  1 
ATOM   3390 N NH2  . ARG   A 1 148 ? 28.130 -19.921 3.615   1.00 15.62 ?  148 ARG   A NH2  1 
ATOM   3391 H H    . ARG   A 1 148 ? 24.012 -17.599 5.344   1.00 15.14 ?  148 ARG   A H    1 
ATOM   3392 H HA   . ARG   A 1 148 ? 22.206 -19.385 6.272   1.00 15.63 ?  148 ARG   A HA   1 
ATOM   3393 H HB2  . ARG   A 1 148 ? 25.012 -19.685 6.147   1.00 16.74 ?  148 ARG   A HB2  1 
ATOM   3394 H HB3  . ARG   A 1 148 ? 24.034 -20.772 6.770   1.00 16.74 ?  148 ARG   A HB3  1 
ATOM   3395 H HG2  . ARG   A 1 148 ? 23.108 -21.164 4.697   1.00 17.84 ?  148 ARG   A HG2  1 
ATOM   3396 H HG3  . ARG   A 1 148 ? 24.016 -20.026 4.057   1.00 17.84 ?  148 ARG   A HG3  1 
ATOM   3397 H HD2  . ARG   A 1 148 ? 25.030 -22.440 5.134   1.00 19.05 ?  148 ARG   A HD2  1 
ATOM   3398 H HD3  . ARG   A 1 148 ? 24.910 -22.141 3.579   1.00 19.05 ?  148 ARG   A HD3  1 
ATOM   3399 H HE   . ARG   A 1 148 ? 26.895 -21.311 5.155   1.00 19.17 ?  148 ARG   A HE   1 
ATOM   3400 H HH11 . ARG   A 1 148 ? 25.446 -20.558 2.261   1.00 18.54 ?  148 ARG   A HH11 1 
ATOM   3401 H HH12 . ARG   A 1 148 ? 26.583 -19.755 1.732   1.00 18.54 ?  148 ARG   A HH12 1 
ATOM   3402 H HH21 . ARG   A 1 148 ? 28.579 -20.059 4.333   1.00 18.74 ?  148 ARG   A HH21 1 
ATOM   3403 H HH22 . ARG   A 1 148 ? 28.471 -19.452 2.978   1.00 18.74 ?  148 ARG   A HH22 1 
ATOM   3404 N N    . THR   A 1 149 ? 23.745 -17.319 8.012   1.00 12.82 ?  149 THR   A N    1 
ATOM   3405 C CA   . THR   A 1 149 ? 23.820 -16.718 9.328   1.00 12.93 ?  149 THR   A CA   1 
ATOM   3406 C C    . THR   A 1 149 ? 22.486 -16.032 9.623   1.00 12.51 ?  149 THR   A C    1 
ATOM   3407 O O    . THR   A 1 149 ? 21.553 -16.037 8.804   1.00 13.44 ?  149 THR   A O    1 
ATOM   3408 C CB   . THR   A 1 149 ? 25.016 -15.771 9.376   1.00 13.60 ?  149 THR   A CB   1 
ATOM   3409 O OG1  . THR   A 1 149 ? 24.880 -14.849 8.295   1.00 13.62 ?  149 THR   A OG1  1 
ATOM   3410 C CG2  . THR   A 1 149 ? 26.338 -16.553 9.261   1.00 13.80 ?  149 THR   A CG2  1 
ATOM   3411 H H    . THR   A 1 149 ? 24.103 -16.829 7.393   1.00 15.38 ?  149 THR   A H    1 
ATOM   3412 H HA   . THR   A 1 149 ? 23.956 -17.419 9.987   1.00 15.52 ?  149 THR   A HA   1 
ATOM   3413 H HB   . THR   A 1 149 ? 25.006 -15.295 10.218  1.00 16.32 ?  149 THR   A HB   1 
ATOM   3414 H HG1  . THR   A 1 149 ? 25.527 -14.314 8.290   1.00 16.35 ?  149 THR   A HG1  1 
ATOM   3415 H HG21 . THR   A 1 149 ? 27.090 -15.943 9.306   1.00 16.56 ?  149 THR   A HG21 1 
ATOM   3416 H HG22 . THR   A 1 149 ? 26.414 -17.199 9.985   1.00 16.56 ?  149 THR   A HG22 1 
ATOM   3417 H HG23 . THR   A 1 149 ? 26.374 -17.033 8.415   1.00 16.56 ?  149 THR   A HG23 1 
ATOM   3418 N N    . ASN   A 1 150 ? 22.354 -15.491 10.828  1.00 13.12 ?  150 ASN   A N    1 
ATOM   3419 C CA   . ASN   A 1 150 ? 21.067 -14.980 11.292  1.00 13.13 ?  150 ASN   A CA   1 
ATOM   3420 C C    . ASN   A 1 150 ? 20.887 -13.543 10.828  1.00 12.74 ?  150 ASN   A C    1 
ATOM   3421 O O    . ASN   A 1 150 ? 21.635 -12.651 11.242  1.00 14.40 ?  150 ASN   A O    1 
ATOM   3422 C CB   . ASN   A 1 150 ? 20.979 -15.083 12.808  1.00 15.52 ?  150 ASN   A CB   1 
ATOM   3423 C CG   . ASN   A 1 150 ? 20.910 -16.516 13.274  1.00 19.44 ?  150 ASN   A CG   1 
ATOM   3424 O OD1  . ASN   A 1 150 ? 20.300 -17.356 12.613  1.00 20.95 ?  150 ASN   A OD1  1 
ATOM   3425 N ND2  . ASN   A 1 150 ? 21.557 -16.815 14.396  1.00 21.89 ?  150 ASN   A ND2  1 
ATOM   3426 H H    . ASN   A 1 150 ? 22.991 -15.408 11.399  1.00 15.75 ?  150 ASN   A H    1 
ATOM   3427 H HA   . ASN   A 1 150 ? 20.351 -15.520 10.913  1.00 15.75 ?  150 ASN   A HA   1 
ATOM   3428 H HB2  . ASN   A 1 150 ? 21.764 -14.676 13.204  1.00 18.63 ?  150 ASN   A HB2  1 
ATOM   3429 H HB3  . ASN   A 1 150 ? 20.176 -14.630 13.115  1.00 18.63 ?  150 ASN   A HB3  1 
ATOM   3430 H HD21 . ASN   A 1 150 ? 21.552 -17.621 14.704  1.00 26.27 ?  150 ASN   A HD21 1 
ATOM   3431 H HD22 . ASN   A 1 150 ? 21.980 -16.200 14.828  1.00 26.27 ?  150 ASN   A HD22 1 
ATOM   3432 N N    . VAL   A 1 151 ? 19.901 -13.320 9.966   1.00 12.27 ?  151 VAL   A N    1 
ATOM   3433 C CA   . VAL   A 1 151 ? 19.694 -12.018 9.357   1.00 12.11 ?  151 VAL   A CA   1 
ATOM   3434 C C    . VAL   A 1 151 ? 18.302 -11.509 9.705   1.00 12.31 ?  151 VAL   A C    1 
ATOM   3435 O O    . VAL   A 1 151 ? 17.297 -12.221 9.545   1.00 13.60 ?  151 VAL   A O    1 
ATOM   3436 C CB   . VAL   A 1 151 ? 19.982 -12.035 7.842   1.00 13.37 ?  151 VAL   A CB   1 
ATOM   3437 C CG1  . VAL   A 1 151 ? 19.151 -13.071 7.114   1.00 14.83 ?  151 VAL   A CG1  1 
ATOM   3438 C CG2  . VAL   A 1 151 ? 19.805 -10.641 7.245   1.00 13.75 ?  151 VAL   A CG2  1 
ATOM   3439 H H    . VAL   A 1 151 ? 19.335 -13.922 9.716   1.00 14.73 ?  151 VAL   A H    1 
ATOM   3440 H HA   . VAL   A 1 151 ? 20.330 -11.401 9.751   1.00 14.53 ?  151 VAL   A HA   1 
ATOM   3441 H HB   . VAL   A 1 151 ? 20.914 -12.282 7.715   1.00 16.04 ?  151 VAL   A HB   1 
ATOM   3442 H HG11 . VAL   A 1 151 ? 19.354 -13.036 6.166   1.00 17.80 ?  151 VAL   A HG11 1 
ATOM   3443 H HG12 . VAL   A 1 151 ? 19.369 -13.956 7.462   1.00 17.80 ?  151 VAL   A HG12 1 
ATOM   3444 H HG13 . VAL   A 1 151 ? 18.211 -12.887 7.260   1.00 17.80 ?  151 VAL   A HG13 1 
ATOM   3445 H HG21 . VAL   A 1 151 ? 20.117 -10.650 6.325   1.00 16.50 ?  151 VAL   A HG21 1 
ATOM   3446 H HG22 . VAL   A 1 151 ? 18.865 -10.402 7.270   1.00 16.50 ?  151 VAL   A HG22 1 
ATOM   3447 H HG23 . VAL   A 1 151 ? 20.324 -10.007 7.762   1.00 16.50 ?  151 VAL   A HG23 1 
ATOM   3448 N N    . TYR   A 1 152 ? 18.270 -10.267 10.185  1.00 12.31 ?  152 TYR   A N    1 
ATOM   3449 C CA   . TYR   A 1 152 ? 17.064 -9.542  10.557  1.00 11.85 ?  152 TYR   A CA   1 
ATOM   3450 C C    . TYR   A 1 152 ? 16.862 -8.449  9.518   1.00 11.01 ?  152 TYR   A C    1 
ATOM   3451 O O    . TYR   A 1 152 ? 17.636 -7.488  9.463   1.00 11.42 ?  152 TYR   A O    1 
ATOM   3452 C CB   . TYR   A 1 152 ? 17.229 -8.978  11.966  1.00 13.28 ?  152 TYR   A CB   1 
ATOM   3453 C CG   . TYR   A 1 152 ? 17.185 -10.082 12.985  1.00 13.80 ?  152 TYR   A CG   1 
ATOM   3454 C CD1  . TYR   A 1 152 ? 18.309 -10.846 13.260  1.00 15.35 ?  152 TYR   A CD1  1 
ATOM   3455 C CD2  . TYR   A 1 152 ? 16.004 -10.405 13.628  1.00 14.28 ?  152 TYR   A CD2  1 
ATOM   3456 C CE1  . TYR   A 1 152 ? 18.268 -11.882 14.168  1.00 16.97 ?  152 TYR   A CE1  1 
ATOM   3457 C CE2  . TYR   A 1 152 ? 15.950 -11.444 14.542  1.00 16.04 ?  152 TYR   A CE2  1 
ATOM   3458 C CZ   . TYR   A 1 152 ? 17.085 -12.179 14.806  1.00 17.12 ?  152 TYR   A CZ   1 
ATOM   3459 O OH   . TYR   A 1 152 ? 17.044 -13.214 15.710  1.00 20.27 ?  152 TYR   A OH   1 
ATOM   3460 H H    . TYR   A 1 152 ? 18.985 -9.797  10.313  1.00 14.77 ?  152 TYR   A H    1 
ATOM   3461 H HA   . TYR   A 1 152 ? 16.303 -10.141 10.546  1.00 14.22 ?  152 TYR   A HA   1 
ATOM   3462 H HB2  . TYR   A 1 152 ? 18.090 -8.535  12.035  1.00 15.94 ?  152 TYR   A HB2  1 
ATOM   3463 H HB3  . TYR   A 1 152 ? 16.514 -8.354  12.152  1.00 15.94 ?  152 TYR   A HB3  1 
ATOM   3464 H HD1  . TYR   A 1 152 ? 19.108 -10.643 12.826  1.00 18.42 ?  152 TYR   A HD1  1 
ATOM   3465 H HD2  . TYR   A 1 152 ? 15.231 -9.911  13.448  1.00 17.14 ?  152 TYR   A HD2  1 
ATOM   3466 H HE1  . TYR   A 1 152 ? 19.035 -12.376 14.348  1.00 20.36 ?  152 TYR   A HE1  1 
ATOM   3467 H HE2  . TYR   A 1 152 ? 15.152 -11.647 14.975  1.00 19.25 ?  152 TYR   A HE2  1 
ATOM   3468 H HH   . TYR   A 1 152 ? 16.270 -13.287 16.032  1.00 24.32 ?  152 TYR   A HH   1 
ATOM   3469 N N    . LEU   A 1 153 ? 15.862 -8.625  8.663   1.00 11.50 ?  153 LEU   A N    1 
ATOM   3470 C CA   . LEU   A 1 153 ? 15.602 -7.729  7.547   1.00 11.68 ?  153 LEU   A CA   1 
ATOM   3471 C C    . LEU   A 1 153 ? 14.589 -6.665  7.942   1.00 12.14 ?  153 LEU   A C    1 
ATOM   3472 O O    . LEU   A 1 153 ? 13.481 -6.981  8.395   1.00 13.44 ?  153 LEU   A O    1 
ATOM   3473 C CB   . LEU   A 1 153 ? 15.050 -8.514  6.357   1.00 12.40 ?  153 LEU   A CB   1 
ATOM   3474 C CG   . LEU   A 1 153 ? 16.007 -9.516  5.711   1.00 12.41 ?  153 LEU   A CG   1 
ATOM   3475 C CD1  . LEU   A 1 153 ? 15.224 -10.392 4.750   1.00 12.62 ?  153 LEU   A CD1  1 
ATOM   3476 C CD2  . LEU   A 1 153 ? 17.132 -8.802  4.991   1.00 13.07 ?  153 LEU   A CD2  1 
ATOM   3477 H H    . LEU   A 1 153 ? 15.294 -9.280  8.711   1.00 13.80 ?  153 LEU   A H    1 
ATOM   3478 H HA   . LEU   A 1 153 ? 16.424 -7.295  7.285   1.00 14.02 ?  153 LEU   A HA   1 
ATOM   3479 H HB2  . LEU   A 1 153 ? 14.266 -8.999  6.654   1.00 14.88 ?  153 LEU   A HB2  1 
ATOM   3480 H HB3  . LEU   A 1 153 ? 14.792 -7.874  5.672   1.00 14.88 ?  153 LEU   A HB3  1 
ATOM   3481 H HG   . LEU   A 1 153 ? 16.389 -10.083 6.403   1.00 14.89 ?  153 LEU   A HG   1 
ATOM   3482 H HD11 . LEU   A 1 153 ? 15.830 -11.019 4.334   1.00 15.14 ?  153 LEU   A HD11 1 
ATOM   3483 H HD12 . LEU   A 1 153 ? 14.536 -10.864 5.242   1.00 15.14 ?  153 LEU   A HD12 1 
ATOM   3484 H HD13 . LEU   A 1 153 ? 14.816 -9.824  4.075   1.00 15.14 ?  153 LEU   A HD13 1 
ATOM   3485 H HD21 . LEU   A 1 153 ? 17.685 -9.463  4.548   1.00 15.68 ?  153 LEU   A HD21 1 
ATOM   3486 H HD22 . LEU   A 1 153 ? 16.750 -8.195  4.341   1.00 15.68 ?  153 LEU   A HD22 1 
ATOM   3487 H HD23 . LEU   A 1 153 ? 17.657 -8.309  5.640   1.00 15.68 ?  153 LEU   A HD23 1 
ATOM   3488 N N    . ALA   A 1 154 ? 14.974 -5.408  7.751   1.00 12.42 ?  154 ALA   A N    1 
ATOM   3489 C CA   . ALA   A 1 154 ? 14.102 -4.263  7.962   1.00 13.02 ?  154 ALA   A CA   1 
ATOM   3490 C C    . ALA   A 1 154 ? 13.609 -3.777  6.607   1.00 12.91 ?  154 ALA   A C    1 
ATOM   3491 O O    . ALA   A 1 154 ? 14.413 -3.364  5.762   1.00 13.46 ?  154 ALA   A O    1 
ATOM   3492 C CB   . ALA   A 1 154 ? 14.864 -3.146  8.670   1.00 13.31 ?  154 ALA   A CB   1 
ATOM   3493 H H    . ALA   A 1 154 ? 15.761 -5.188  7.478   1.00 14.90 ?  154 ALA   A H    1 
ATOM   3494 H HA   . ALA   A 1 154 ? 13.340 -4.517  8.502   1.00 15.62 ?  154 ALA   A HA   1 
ATOM   3495 H HB1  . ALA   A 1 154 ? 14.269 -2.388  8.800   1.00 15.97 ?  154 ALA   A HB1  1 
ATOM   3496 H HB2  . ALA   A 1 154 ? 15.180 -3.469  9.525   1.00 15.97 ?  154 ALA   A HB2  1 
ATOM   3497 H HB3  . ALA   A 1 154 ? 15.618 -2.876  8.118   1.00 15.97 ?  154 ALA   A HB3  1 
ATOM   3498 N N    A VAL   A 1 155 ? 12.295 -3.825  6.423   0.42 13.33 ?  155 VAL   A N    1 
ATOM   3499 N N    B VAL   A 1 155 ? 12.291 -3.842  6.391   0.58 13.52 ?  155 VAL   A N    1 
ATOM   3500 C CA   A VAL   A 1 155 ? 11.623 -3.313  5.241   0.42 13.44 ?  155 VAL   A CA   1 
ATOM   3501 C CA   B VAL   A 1 155 ? 11.653 -3.507  5.116   0.58 13.68 ?  155 VAL   A CA   1 
ATOM   3502 C C    A VAL   A 1 155 ? 10.969 -1.997  5.632   0.42 13.37 ?  155 VAL   A C    1 
ATOM   3503 C C    B VAL   A 1 155 ? 10.899 -2.195  5.299   0.58 13.50 ?  155 VAL   A C    1 
ATOM   3504 O O    A VAL   A 1 155 ? 10.066 -1.973  6.476   0.42 13.89 ?  155 VAL   A O    1 
ATOM   3505 O O    B VAL   A 1 155 ? 9.919  -2.140  6.050   0.58 14.08 ?  155 VAL   A O    1 
ATOM   3506 C CB   A VAL   A 1 155 ? 10.588 -4.325  4.724   0.42 13.82 ?  155 VAL   A CB   1 
ATOM   3507 C CB   B VAL   A 1 155 ? 10.703 -4.624  4.641   0.58 14.06 ?  155 VAL   A CB   1 
ATOM   3508 C CG1  A VAL   A 1 155 ? 9.837  -3.768  3.528   0.42 14.20 ?  155 VAL   A CG1  1 
ATOM   3509 C CG1  B VAL   A 1 155 ? 9.927  -4.186  3.396   0.58 14.26 ?  155 VAL   A CG1  1 
ATOM   3510 C CG2  A VAL   A 1 155 ? 11.280 -5.633  4.367   0.42 13.99 ?  155 VAL   A CG2  1 
ATOM   3511 C CG2  B VAL   A 1 155 ? 11.474 -5.908  4.353   0.58 15.28 ?  155 VAL   A CG2  1 
ATOM   3512 H H    A VAL   A 1 155 ? 11.753 -4.172  6.996   0.42 16.00 ?  155 VAL   A H    1 
ATOM   3513 H H    B VAL   A 1 155 ? 11.722 -4.086  6.991   0.58 16.22 ?  155 VAL   A H    1 
ATOM   3514 H HA   A VAL   A 1 155 ? 12.270 -3.141  4.545   0.42 16.13 ?  155 VAL   A HA   1 
ATOM   3515 H HA   B VAL   A 1 155 ? 12.326 -3.388  4.432   0.58 16.41 ?  155 VAL   A HA   1 
ATOM   3516 H HB   A VAL   A 1 155 ? 9.942  -4.505  5.431   0.42 16.58 ?  155 VAL   A HB   1 
ATOM   3517 H HB   B VAL   A 1 155 ? 10.057 -4.822  5.339   0.58 16.87 ?  155 VAL   A HB   1 
ATOM   3518 H HG11 A VAL   A 1 155 ? 9.305  -4.477  3.137   0.42 17.04 ?  155 VAL   A HG11 1 
ATOM   3519 H HG11 B VAL   A 1 155 ? 9.567  -4.971  2.949   0.58 17.11 ?  155 VAL   A HG11 1 
ATOM   3520 H HG12 A VAL   A 1 155 ? 9.261  -3.045  3.821   0.42 17.04 ?  155 VAL   A HG12 1 
ATOM   3521 H HG12 B VAL   A 1 155 ? 9.200  -3.602  3.664   0.58 17.11 ?  155 VAL   A HG12 1 
ATOM   3522 H HG13 A VAL   A 1 155 ? 10.480 -3.440  2.881   0.42 17.04 ?  155 VAL   A HG13 1 
ATOM   3523 H HG13 B VAL   A 1 155 ? 10.527 -3.716  2.798   0.58 17.11 ?  155 VAL   A HG13 1 
ATOM   3524 H HG21 A VAL   A 1 155 ? 10.637 -6.230  3.958   0.42 16.78 ?  155 VAL   A HG21 1 
ATOM   3525 H HG21 B VAL   A 1 155 ? 10.869 -6.568  3.976   0.58 18.33 ?  155 VAL   A HG21 1 
ATOM   3526 H HG22 A VAL   A 1 155 ? 12.002 -5.447  3.743   0.42 16.78 ?  155 VAL   A HG22 1 
ATOM   3527 H HG22 B VAL   A 1 155 ? 12.184 -5.715  3.721   0.58 18.33 ?  155 VAL   A HG22 1 
ATOM   3528 H HG23 A VAL   A 1 155 ? 11.641 -6.036  5.174   0.42 16.78 ?  155 VAL   A HG23 1 
ATOM   3529 H HG23 B VAL   A 1 155 ? 11.851 -6.243  5.182   0.58 18.33 ?  155 VAL   A HG23 1 
ATOM   3530 N N    A PHE   A 1 156 ? 11.443 -0.898  5.039   0.42 12.71 ?  156 PHE   A N    1 
ATOM   3531 N N    B PHE   A 1 156 ? 11.332 -1.151  4.577   0.58 13.21 ?  156 PHE   A N    1 
ATOM   3532 C CA   A PHE   A 1 156 ? 10.946 0.424   5.418   0.42 14.11 ?  156 PHE   A CA   1 
ATOM   3533 C CA   B PHE   A 1 156 ? 10.836 0.211   4.804   0.58 13.09 ?  156 PHE   A CA   1 
ATOM   3534 C C    A PHE   A 1 156 ? 9.473  0.603   5.061   0.42 13.30 ?  156 PHE   A C    1 
ATOM   3535 C C    B PHE   A 1 156 ? 9.377  0.384   4.375   0.58 13.73 ?  156 PHE   A C    1 
ATOM   3536 O O    A PHE   A 1 156 ? 8.707  1.181   5.842   0.42 13.36 ?  156 PHE   A O    1 
ATOM   3537 O O    B PHE   A 1 156 ? 8.586  1.010   5.095   0.58 14.98 ?  156 PHE   A O    1 
ATOM   3538 C CB   A PHE   A 1 156 ? 11.796 1.514   4.759   0.42 15.85 ?  156 PHE   A CB   1 
ATOM   3539 C CB   B PHE   A 1 156 ? 11.762 1.192   4.070   0.58 12.31 ?  156 PHE   A CB   1 
ATOM   3540 C CG   A PHE   A 1 156 ? 11.308 2.910   5.039   0.42 18.05 ?  156 PHE   A CG   1 
ATOM   3541 C CG   B PHE   A 1 156 ? 11.458 2.669   4.292   0.58 12.23 ?  156 PHE   A CG   1 
ATOM   3542 C CD1  A PHE   A 1 156 ? 11.294 3.399   6.335   0.42 19.28 ?  156 PHE   A CD1  1 
ATOM   3543 C CD1  B PHE   A 1 156 ? 11.973 3.354   5.392   0.58 13.41 ?  156 PHE   A CD1  1 
ATOM   3544 C CD2  A PHE   A 1 156 ? 10.865 3.732   4.013   0.42 19.18 ?  156 PHE   A CD2  1 
ATOM   3545 C CD2  B PHE   A 1 156 ? 10.730 3.385   3.351   0.58 13.62 ?  156 PHE   A CD2  1 
ATOM   3546 C CE1  A PHE   A 1 156 ? 10.843 4.678   6.606   0.42 20.21 ?  156 PHE   A CE1  1 
ATOM   3547 C CE1  B PHE   A 1 156 ? 11.720 4.718   5.567   0.58 14.56 ?  156 PHE   A CE1  1 
ATOM   3548 C CE2  A PHE   A 1 156 ? 10.414 5.016   4.279   0.42 20.10 ?  156 PHE   A CE2  1 
ATOM   3549 C CE2  B PHE   A 1 156 ? 10.481 4.740   3.519   0.58 14.48 ?  156 PHE   A CE2  1 
ATOM   3550 C CZ   A PHE   A 1 156 ? 10.405 5.488   5.577   0.42 20.51 ?  156 PHE   A CZ   1 
ATOM   3551 C CZ   B PHE   A 1 156 ? 10.978 5.406   4.630   0.58 14.68 ?  156 PHE   A CZ   1 
ATOM   3552 H H    A PHE   A 1 156 ? 12.044 -0.889  4.424   0.42 15.25 ?  156 PHE   A H    1 
ATOM   3553 H H    B PHE   A 1 156 ? 11.916 -1.216  3.948   0.58 15.85 ?  156 PHE   A H    1 
ATOM   3554 H HA   A PHE   A 1 156 ? 11.034 0.535   6.376   0.42 16.94 ?  156 PHE   A HA   1 
ATOM   3555 H HA   B PHE   A 1 156 ? 10.887 0.396   5.747   0.58 15.71 ?  156 PHE   A HA   1 
ATOM   3556 H HB2  A PHE   A 1 156 ? 12.709 1.449   5.090   0.42 19.02 ?  156 PHE   A HB2  1 
ATOM   3557 H HB2  B PHE   A 1 156 ? 12.666 1.030   4.372   0.58 14.77 ?  156 PHE   A HB2  1 
ATOM   3558 H HB3  A PHE   A 1 156 ? 11.788 1.387   3.798   0.42 19.02 ?  156 PHE   A HB3  1 
ATOM   3559 H HB3  B PHE   A 1 156 ? 11.702 1.018   3.116   0.58 14.77 ?  156 PHE   A HB3  1 
ATOM   3560 H HD1  A PHE   A 1 156 ? 11.590 2.857   7.032   0.42 23.14 ?  156 PHE   A HD1  1 
ATOM   3561 H HD1  B PHE   A 1 156 ? 12.472 2.888   6.027   0.58 16.09 ?  156 PHE   A HD1  1 
ATOM   3562 H HD2  A PHE   A 1 156 ? 10.873 3.418   3.138   0.42 23.02 ?  156 PHE   A HD2  1 
ATOM   3563 H HD2  B PHE   A 1 156 ? 10.392 2.945   2.605   0.58 16.34 ?  156 PHE   A HD2  1 
ATOM   3564 H HE1  A PHE   A 1 156 ? 10.840 4.990   7.484   0.42 24.26 ?  156 PHE   A HE1  1 
ATOM   3565 H HE1  B PHE   A 1 156 ? 12.054 5.155   6.315   0.58 17.48 ?  156 PHE   A HE1  1 
ATOM   3566 H HE2  A PHE   A 1 156 ? 10.120 5.558   3.584   0.42 24.11 ?  156 PHE   A HE2  1 
ATOM   3567 H HE2  B PHE   A 1 156 ? 9.976  5.202   2.891   0.58 17.38 ?  156 PHE   A HE2  1 
ATOM   3568 H HZ   A PHE   A 1 156 ? 10.103 6.348   5.761   0.42 24.61 ?  156 PHE   A HZ   1 
ATOM   3569 H HZ   B PHE   A 1 156 ? 10.805 6.311   4.749   0.58 17.61 ?  156 PHE   A HZ   1 
ATOM   3570 N N    A ASP   A 1 157 ? 9.059  0.122   3.893   0.42 13.04 ?  157 ASP   A N    1 
ATOM   3571 N N    B ASP   A 1 157 ? 8.992  -0.162  3.222   0.58 14.58 ?  157 ASP   A N    1 
ATOM   3572 C CA   A ASP   A 1 157 ? 7.730  0.394   3.357   0.42 13.93 ?  157 ASP   A CA   1 
ATOM   3573 C CA   B ASP   A 1 157 ? 7.669  0.090   2.652   0.58 15.44 ?  157 ASP   A CA   1 
ATOM   3574 C C    A ASP   A 1 157 ? 6.736  -0.642  3.879   0.42 14.18 ?  157 ASP   A C    1 
ATOM   3575 C C    B ASP   A 1 157 ? 6.657  -0.950  3.129   0.58 14.86 ?  157 ASP   A C    1 
ATOM   3576 O O    A ASP   A 1 157 ? 6.919  -1.845  3.665   0.42 14.45 ?  157 ASP   A O    1 
ATOM   3577 O O    B ASP   A 1 157 ? 6.860  -2.151  2.941   0.58 14.20 ?  157 ASP   A O    1 
ATOM   3578 C CB   A ASP   A 1 157 ? 7.794  0.338   1.833   0.42 14.91 ?  157 ASP   A CB   1 
ATOM   3579 C CB   B ASP   A 1 157 ? 7.739  0.065   1.125   0.58 16.71 ?  157 ASP   A CB   1 
ATOM   3580 C CG   A ASP   A 1 157 ? 6.537  0.866   1.184   0.42 16.74 ?  157 ASP   A CG   1 
ATOM   3581 C CG   B ASP   A 1 157 ? 6.436  0.490   0.475   0.58 17.93 ?  157 ASP   A CG   1 
ATOM   3582 O OD1  A ASP   A 1 157 ? 6.382  2.102   1.124   0.42 19.07 ?  157 ASP   A OD1  1 
ATOM   3583 O OD1  B ASP   A 1 157 ? 6.100  1.688   0.551   0.58 19.91 ?  157 ASP   A OD1  1 
ATOM   3584 O OD2  A ASP   A 1 157 ? 5.698  0.051   0.744   0.42 16.54 -1 157 ASP   A OD2  1 
ATOM   3585 O OD2  B ASP   A 1 157 ? 5.743  -0.366  -0.111  0.58 18.39 -1 157 ASP   A OD2  1 
ATOM   3586 H H    A ASP   A 1 157 ? 9.540  -0.375  3.381   0.42 15.65 ?  157 ASP   A H    1 
ATOM   3587 H H    B ASP   A 1 157 ? 9.475  -0.697  2.749   0.58 17.49 ?  157 ASP   A H    1 
ATOM   3588 H HA   A ASP   A 1 157 ? 7.436  1.284   3.622   0.42 16.72 ?  157 ASP   A HA   1 
ATOM   3589 H HA   B ASP   A 1 157 ? 7.360  0.962   2.930   0.58 18.53 ?  157 ASP   A HA   1 
ATOM   3590 H HB2  A ASP   A 1 157 ? 8.545  0.872   1.526   0.42 17.90 ?  157 ASP   A HB2  1 
ATOM   3591 H HB2  B ASP   A 1 157 ? 8.440  0.665   0.835   0.58 20.05 ?  157 ASP   A HB2  1 
ATOM   3592 H HB3  A ASP   A 1 157 ? 7.920  -0.585  1.557   0.42 17.90 ?  157 ASP   A HB3  1 
ATOM   3593 H HB3  B ASP   A 1 157 ? 7.929  -0.839  0.829   0.58 20.05 ?  157 ASP   A HB3  1 
ATOM   3594 N N    A LYS   A 1 158 ? 5.668  -0.173  4.536   0.42 14.72 ?  158 LYS   A N    1 
ATOM   3595 N N    B LYS   A 1 158 ? 5.547  -0.481  3.710   0.58 15.30 ?  158 LYS   A N    1 
ATOM   3596 C CA   A LYS   A 1 158 ? 4.692  -1.094  5.116   0.42 15.63 ?  158 LYS   A CA   1 
ATOM   3597 C CA   B LYS   A 1 158 ? 4.570  -1.391  4.309   0.58 16.29 ?  158 LYS   A CA   1 
ATOM   3598 C C    A LYS   A 1 158 ? 3.959  -1.883  4.037   0.42 15.80 ?  158 LYS   A C    1 
ATOM   3599 C C    B LYS   A 1 158 ? 3.896  -2.272  3.260   0.58 15.29 ?  158 LYS   A C    1 
ATOM   3600 O O    A LYS   A 1 158 ? 3.762  -3.097  4.175   0.42 15.86 ?  158 LYS   A O    1 
ATOM   3601 O O    B LYS   A 1 158 ? 3.742  -3.484  3.459   0.58 15.35 ?  158 LYS   A O    1 
ATOM   3602 C CB   A LYS   A 1 158 ? 3.702  -0.327  5.997   0.42 16.36 ?  158 LYS   A CB   1 
ATOM   3603 C CB   B LYS   A 1 158 ? 3.520  -0.595  5.093   0.58 19.22 ?  158 LYS   A CB   1 
ATOM   3604 C CG   A LYS   A 1 158 ? 2.469  -1.127  6.423   0.42 17.75 ?  158 LYS   A CG   1 
ATOM   3605 C CG   B LYS   A 1 158 ? 2.326  -1.429  5.560   0.58 22.38 ?  158 LYS   A CG   1 
ATOM   3606 C CD   A LYS   A 1 158 ? 2.818  -2.396  7.200   0.42 18.81 ?  158 LYS   A CD   1 
ATOM   3607 C CD   B LYS   A 1 158 ? 2.763  -2.638  6.388   0.58 25.23 ?  158 LYS   A CD   1 
ATOM   3608 C CE   A LYS   A 1 158 ? 1.546  -3.121  7.637   0.42 18.63 ?  158 LYS   A CE   1 
ATOM   3609 C CE   B LYS   A 1 158 ? 2.714  -2.360  7.880   0.58 27.22 ?  158 LYS   A CE   1 
ATOM   3610 N NZ   A LYS   A 1 158 ? 1.793  -4.467  8.224   0.42 18.27 ?  158 LYS   A NZ   1 
ATOM   3611 N NZ   B LYS   A 1 158 ? 1.347  -2.498  8.440   0.58 28.53 ?  158 LYS   A NZ   1 
ATOM   3612 H H    A LYS   A 1 158 ? 5.487  0.664   4.652   0.42 17.66 ?  158 LYS   A H    1 
ATOM   3613 H H    B LYS   A 1 158 ? 5.338  0.349   3.775   0.58 18.37 ?  158 LYS   A H    1 
ATOM   3614 H HA   A LYS   A 1 158 ? 5.158  -1.723  5.681   0.42 18.76 ?  158 LYS   A HA   1 
ATOM   3615 H HA   B LYS   A 1 158 ? 5.034  -1.969  4.933   0.58 19.55 ?  158 LYS   A HA   1 
ATOM   3616 H HB2  A LYS   A 1 158 ? 4.158  -0.045  6.806   0.42 19.63 ?  158 LYS   A HB2  1 
ATOM   3617 H HB2  B LYS   A 1 158 ? 3.937  -0.216  5.884   0.58 23.06 ?  158 LYS   A HB2  1 
ATOM   3618 H HB3  A LYS   A 1 158 ? 3.388  0.453   5.513   0.42 19.63 ?  158 LYS   A HB3  1 
ATOM   3619 H HB3  B LYS   A 1 158 ? 3.179  0.118   4.530   0.58 23.06 ?  158 LYS   A HB3  1 
ATOM   3620 H HG2  A LYS   A 1 158 ? 1.922  -0.570  7.000   0.42 21.30 ?  158 LYS   A HG2  1 
ATOM   3621 H HG2  B LYS   A 1 158 ? 1.750  -0.877  6.117   0.58 26.86 ?  158 LYS   A HG2  1 
ATOM   3622 H HG3  A LYS   A 1 158 ? 1.959  -1.381  5.638   0.42 21.30 ?  158 LYS   A HG3  1 
ATOM   3623 H HG3  B LYS   A 1 158 ? 1.825  -1.748  4.790   0.58 26.86 ?  158 LYS   A HG3  1 
ATOM   3624 H HD2  A LYS   A 1 158 ? 3.331  -2.993  6.635   0.42 22.58 ?  158 LYS   A HD2  1 
ATOM   3625 H HD2  B LYS   A 1 158 ? 2.163  -3.370  6.202   0.58 30.27 ?  158 LYS   A HD2  1 
ATOM   3626 H HD3  A LYS   A 1 158 ? 3.325  -2.160  7.993   0.42 22.58 ?  158 LYS   A HD3  1 
ATOM   3627 H HD3  B LYS   A 1 158 ? 3.670  -2.894  6.168   0.58 30.27 ?  158 LYS   A HD3  1 
ATOM   3628 H HE2  A LYS   A 1 158 ? 1.087  -2.587  8.304   0.42 22.35 ?  158 LYS   A HE2  1 
ATOM   3629 H HE2  B LYS   A 1 158 ? 3.291  -2.989  8.336   0.58 32.66 ?  158 LYS   A HE2  1 
ATOM   3630 H HE3  A LYS   A 1 158 ? 0.973  -3.240  6.866   0.42 22.35 ?  158 LYS   A HE3  1 
ATOM   3631 H HE3  B LYS   A 1 158 ? 3.012  -1.452  8.043   0.58 32.66 ?  158 LYS   A HE3  1 
ATOM   3632 H HZ1  A LYS   A 1 158 ? 1.019  -4.845  8.462   0.42 21.92 ?  158 LYS   A HZ1  1 
ATOM   3633 H HZ1  B LYS   A 1 158 ? 1.361  -2.330  9.314   0.58 34.24 ?  158 LYS   A HZ1  1 
ATOM   3634 H HZ2  A LYS   A 1 158 ? 2.195  -4.993  7.629   0.42 21.92 ?  158 LYS   A HZ2  1 
ATOM   3635 H HZ2  B LYS   A 1 158 ? 0.796  -1.924  8.043   0.58 34.24 ?  158 LYS   A HZ2  1 
ATOM   3636 H HZ3  A LYS   A 1 158 ? 2.310  -4.400  8.945   0.42 21.92 ?  158 LYS   A HZ3  1 
ATOM   3637 H HZ3  B LYS   A 1 158 ? 1.048  -3.326  8.309   0.58 34.24 ?  158 LYS   A HZ3  1 
ATOM   3638 N N    A ASN   A 1 159 ? 3.535  -1.214  2.962   0.42 16.57 ?  159 ASN   A N    1 
ATOM   3639 N N    B ASN   A 1 159 ? 3.459  -1.681  2.149   0.58 15.81 ?  159 ASN   A N    1 
ATOM   3640 C CA   A ASN   A 1 159 ? 2.857  -1.924  1.882   0.42 17.54 ?  159 ASN   A CA   1 
ATOM   3641 C CA   B ASN   A 1 159 ? 2.812  -2.471  1.106   0.58 17.14 ?  159 ASN   A CA   1 
ATOM   3642 C C    A ASN   A 1 159 ? 3.745  -3.017  1.305   0.42 16.82 ?  159 ASN   A C    1 
ATOM   3643 C C    B ASN   A 1 159 ? 3.757  -3.550  0.590   0.58 16.07 ?  159 ASN   A C    1 
ATOM   3644 O O    A ASN   A 1 159 ? 3.290  -4.143  1.076   0.42 16.52 ?  159 ASN   A O    1 
ATOM   3645 O O    B ASN   A 1 159 ? 3.347  -4.692  0.349   0.58 16.71 ?  159 ASN   A O    1 
ATOM   3646 C CB   A ASN   A 1 159 ? 2.427  -0.940  0.793   0.42 19.28 ?  159 ASN   A CB   1 
ATOM   3647 C CB   B ASN   A 1 159 ? 2.363  -1.542  -0.023  0.58 20.27 ?  159 ASN   A CB   1 
ATOM   3648 C CG   A ASN   A 1 159 ? 1.192  -0.151  1.178   0.42 21.26 ?  159 ASN   A CG   1 
ATOM   3649 C CG   B ASN   A 1 159 ? 1.442  -2.219  -1.011  0.58 23.56 ?  159 ASN   A CG   1 
ATOM   3650 O OD1  A ASN   A 1 159 ? 0.331  -0.653  1.895   0.42 22.08 ?  159 ASN   A OD1  1 
ATOM   3651 O OD1  B ASN   A 1 159 ? 0.522  -2.941  -0.629  0.58 24.80 ?  159 ASN   A OD1  1 
ATOM   3652 N ND2  A ASN   A 1 159 ? 1.096  1.088   0.701   0.42 22.02 ?  159 ASN   A ND2  1 
ATOM   3653 N ND2  B ASN   A 1 159 ? 1.678  -1.980  -2.295  0.58 25.73 ?  159 ASN   A ND2  1 
ATOM   3654 H H    A ASN   A 1 159 ? 3.625  -0.369  2.838   0.42 19.89 ?  159 ASN   A H    1 
ATOM   3655 H H    B ASN   A 1 159 ? 3.520  -0.844  1.981   0.58 18.98 ?  159 ASN   A H    1 
ATOM   3656 H HA   A ASN   A 1 159 ? 2.058  -2.347  2.233   0.42 21.05 ?  159 ASN   A HA   1 
ATOM   3657 H HA   B ASN   A 1 159 ? 2.022  -2.905  1.470   0.58 20.57 ?  159 ASN   A HA   1 
ATOM   3658 H HB2  A ASN   A 1 159 ? 3.143  -0.308  0.631   0.42 23.13 ?  159 ASN   A HB2  1 
ATOM   3659 H HB2  B ASN   A 1 159 ? 1.889  -0.783  0.360   0.58 24.32 ?  159 ASN   A HB2  1 
ATOM   3660 H HB3  A ASN   A 1 159 ? 2.224  -1.430  -0.020  0.42 23.13 ?  159 ASN   A HB3  1 
ATOM   3661 H HB3  B ASN   A 1 159 ? 3.143  -1.231  -0.507  0.58 24.32 ?  159 ASN   A HB3  1 
ATOM   3662 H HD21 A ASN   A 1 159 ? 0.412  1.575   0.893   0.42 26.42 ?  159 ASN   A HD21 1 
ATOM   3663 H HD21 B ASN   A 1 159 ? 1.178  -2.335  -2.898  0.58 30.88 ?  159 ASN   A HD21 1 
ATOM   3664 H HD22 A ASN   A 1 159 ? 1.720  1.406   0.204   0.42 26.42 ?  159 ASN   A HD22 1 
ATOM   3665 H HD22 B ASN   A 1 159 ? 2.328  -1.466  -2.522  0.58 30.88 ?  159 ASN   A HD22 1 
ATOM   3666 N N    A LEU   A 1 160 ? 5.021  -2.706  1.074   0.42 16.24 ?  160 LEU   A N    1 
ATOM   3667 N N    B LEU   A 1 160 ? 5.038  -3.212  0.441   0.58 15.84 ?  160 LEU   A N    1 
ATOM   3668 C CA   A LEU   A 1 160 ? 5.940  -3.710  0.552   0.42 16.28 ?  160 LEU   A CA   1 
ATOM   3669 C CA   B LEU   A 1 160 ? 6.016  -4.205  0.009   0.58 15.64 ?  160 LEU   A CA   1 
ATOM   3670 C C    A LEU   A 1 160 ? 6.135  -4.843  1.546   0.42 15.92 ?  160 LEU   A C    1 
ATOM   3671 C C    B LEU   A 1 160 ? 6.163  -5.317  1.041   0.58 15.72 ?  160 LEU   A C    1 
ATOM   3672 O O    A LEU   A 1 160 ? 6.172  -6.019  1.161   0.42 16.23 ?  160 LEU   A O    1 
ATOM   3673 O O    B LEU   A 1 160 ? 6.163  -6.503  0.693   0.58 15.98 ?  160 LEU   A O    1 
ATOM   3674 C CB   A LEU   A 1 160 ? 7.280  -3.063  0.218   0.42 16.83 ?  160 LEU   A CB   1 
ATOM   3675 C CB   B LEU   A 1 160 ? 7.370  -3.545  -0.246  0.58 15.99 ?  160 LEU   A CB   1 
ATOM   3676 C CG   A LEU   A 1 160 ? 8.345  -4.048  -0.252  0.42 17.30 ?  160 LEU   A CG   1 
ATOM   3677 C CG   B LEU   A 1 160 ? 8.470  -4.561  -0.560  0.58 16.67 ?  160 LEU   A CG   1 
ATOM   3678 C CD1  A LEU   A 1 160 ? 7.886  -4.756  -1.512  0.42 17.50 ?  160 LEU   A CD1  1 
ATOM   3679 C CD1  B LEU   A 1 160 ? 8.086  -5.361  -1.792  0.58 17.58 ?  160 LEU   A CD1  1 
ATOM   3680 C CD2  A LEU   A 1 160 ? 9.651  -3.326  -0.485  0.42 17.26 ?  160 LEU   A CD2  1 
ATOM   3681 C CD2  B LEU   A 1 160 ? 9.809  -3.878  -0.738  0.58 17.15 ?  160 LEU   A CD2  1 
ATOM   3682 H H    A LEU   A 1 160 ? 5.374  -1.937  1.213   0.42 19.49 ?  160 LEU   A H    1 
ATOM   3683 H H    B LEU   A 1 160 ? 5.358  -2.431  0.586   0.58 19.00 ?  160 LEU   A H    1 
ATOM   3684 H HA   A LEU   A 1 160 ? 5.573  -4.084  -0.261  0.42 19.54 ?  160 LEU   A HA   1 
ATOM   3685 H HA   B LEU   A 1 160 ? 5.712  -4.600  -0.824  0.58 18.76 ?  160 LEU   A HA   1 
ATOM   3686 H HB2  A LEU   A 1 160 ? 7.146  -2.408  -0.487  0.42 20.19 ?  160 LEU   A HB2  1 
ATOM   3687 H HB2  B LEU   A 1 160 ? 7.292  -2.938  -1.002  0.58 19.18 ?  160 LEU   A HB2  1 
ATOM   3688 H HB3  A LEU   A 1 160 ? 7.619  -2.626  1.013   0.42 20.19 ?  160 LEU   A HB3  1 
ATOM   3689 H HB3  B LEU   A 1 160 ? 7.634  -3.051  0.547   0.58 19.18 ?  160 LEU   A HB3  1 
ATOM   3690 H HG   A LEU   A 1 160 ? 8.494  -4.717  0.436   0.42 20.76 ?  160 LEU   A HG   1 
ATOM   3691 H HG   B LEU   A 1 160 ? 8.558  -5.181  0.181   0.58 20.01 ?  160 LEU   A HG   1 
ATOM   3692 H HD11 A LEU   A 1 160 ? 8.625  -5.269  -1.868  0.42 21.00 ?  160 LEU   A HD11 1 
ATOM   3693 H HD11 B LEU   A 1 160 ? 8.854  -5.861  -2.092  0.58 21.10 ?  160 LEU   A HD11 1 
ATOM   3694 H HD12 A LEU   A 1 160 ? 7.148  -5.347  -1.294  0.42 21.00 ?  160 LEU   A HD12 1 
ATOM   3695 H HD12 B LEU   A 1 160 ? 7.362  -5.969  -1.565  0.58 21.10 ?  160 LEU   A HD12 1 
ATOM   3696 H HD13 A LEU   A 1 160 ? 7.600  -4.092  -2.159  0.42 21.00 ?  160 LEU   A HD13 1 
ATOM   3697 H HD13 B LEU   A 1 160 ? 7.793  -4.747  -2.486  0.58 21.10 ?  160 LEU   A HD13 1 
ATOM   3698 H HD21 A LEU   A 1 160 ? 10.316 -3.968  -0.779  0.42 20.71 ?  160 LEU   A HD21 1 
ATOM   3699 H HD21 B LEU   A 1 160 ? 10.482 -4.550  -0.931  0.58 20.59 ?  160 LEU   A HD21 1 
ATOM   3700 H HD22 A LEU   A 1 160 ? 9.520  -2.649  -1.165  0.42 20.71 ?  160 LEU   A HD22 1 
ATOM   3701 H HD22 B LEU   A 1 160 ? 9.749  -3.248  -1.471  0.58 20.59 ?  160 LEU   A HD22 1 
ATOM   3702 H HD23 A LEU   A 1 160 ? 9.935  -2.912  0.346   0.42 20.71 ?  160 LEU   A HD23 1 
ATOM   3703 H HD23 B LEU   A 1 160 ? 10.036 -3.411  0.083   0.58 20.59 ?  160 LEU   A HD23 1 
ATOM   3704 N N    A TYR   A 1 161 ? 6.267  -4.511  2.830   0.42 15.69 ?  161 TYR   A N    1 
ATOM   3705 N N    B TYR   A 1 161 ? 6.318  -4.952  2.318   0.58 15.79 ?  161 TYR   A N    1 
ATOM   3706 C CA   A TYR   A 1 161 ? 6.404  -5.546  3.844   0.42 15.84 ?  161 TYR   A CA   1 
ATOM   3707 C CA   B TYR   A 1 161 ? 6.425  -5.949  3.383   0.58 16.15 ?  161 TYR   A CA   1 
ATOM   3708 C C    A TYR   A 1 161 ? 5.259  -6.543  3.764   0.42 16.88 ?  161 TYR   A C    1 
ATOM   3709 C C    B TYR   A 1 161 ? 5.248  -6.909  3.347   0.58 16.60 ?  161 TYR   A C    1 
ATOM   3710 O O    A TYR   A 1 161 ? 5.479  -7.758  3.841   0.42 16.71 ?  161 TYR   A O    1 
ATOM   3711 O O    B TYR   A 1 161 ? 5.430  -8.131  3.297   0.58 15.89 ?  161 TYR   A O    1 
ATOM   3712 C CB   A TYR   A 1 161 ? 6.485  -4.927  5.241   0.42 15.87 ?  161 TYR   A CB   1 
ATOM   3713 C CB   B TYR   A 1 161 ? 6.506  -5.249  4.744   0.58 16.74 ?  161 TYR   A CB   1 
ATOM   3714 C CG   A TYR   A 1 161 ? 6.416  -5.988  6.305   0.42 15.90 ?  161 TYR   A CG   1 
ATOM   3715 C CG   B TYR   A 1 161 ? 6.345  -6.142  5.974   0.58 17.79 ?  161 TYR   A CG   1 
ATOM   3716 C CD1  A TYR   A 1 161 ? 7.555  -6.678  6.689   0.42 16.06 ?  161 TYR   A CD1  1 
ATOM   3717 C CD1  B TYR   A 1 161 ? 7.427  -6.840  6.506   0.58 18.39 ?  161 TYR   A CD1  1 
ATOM   3718 C CD2  A TYR   A 1 161 ? 5.203  -6.338  6.892   0.42 16.41 ?  161 TYR   A CD2  1 
ATOM   3719 C CD2  B TYR   A 1 161 ? 5.114  -6.254  6.630   0.58 18.69 ?  161 TYR   A CD2  1 
ATOM   3720 C CE1  A TYR   A 1 161 ? 7.498  -7.667  7.638   0.42 16.68 ?  161 TYR   A CE1  1 
ATOM   3721 C CE1  B TYR   A 1 161 ? 7.284  -7.643  7.634   0.58 18.81 ?  161 TYR   A CE1  1 
ATOM   3722 C CE2  A TYR   A 1 161 ? 5.136  -7.327  7.845   0.42 16.94 ?  161 TYR   A CE2  1 
ATOM   3723 C CE2  B TYR   A 1 161 ? 4.963  -7.052  7.764   0.58 18.91 ?  161 TYR   A CE2  1 
ATOM   3724 C CZ   A TYR   A 1 161 ? 6.290  -7.987  8.215   0.42 17.02 ?  161 TYR   A CZ   1 
ATOM   3725 C CZ   B TYR   A 1 161 ? 6.051  -7.741  8.259   0.58 19.22 ?  161 TYR   A CZ   1 
ATOM   3726 O OH   A TYR   A 1 161 ? 6.233  -8.975  9.165   0.42 17.27 ?  161 TYR   A OH   1 
ATOM   3727 O OH   B TYR   A 1 161 ? 5.908  -8.538  9.380   0.58 20.01 ?  161 TYR   A OH   1 
ATOM   3728 H H    A TYR   A 1 161 ? 6.271  -3.713  3.137   0.42 18.83 ?  161 TYR   A H    1 
ATOM   3729 H H    B TYR   A 1 161 ? 6.357  -4.146  2.588   0.58 18.95 ?  161 TYR   A H    1 
ATOM   3730 H HA   A TYR   A 1 161 ? 7.220  -6.041  3.693   0.42 19.01 ?  161 TYR   A HA   1 
ATOM   3731 H HA   B TYR   A 1 161 ? 7.233  -6.472  3.257   0.58 19.38 ?  161 TYR   A HA   1 
ATOM   3732 H HB2  A TYR   A 1 161 ? 7.330  -4.455  5.335   0.42 19.05 ?  161 TYR   A HB2  1 
ATOM   3733 H HB2  B TYR   A 1 161 ? 7.373  -4.825  4.812   0.58 20.08 ?  161 TYR   A HB2  1 
ATOM   3734 H HB3  A TYR   A 1 161 ? 5.744  -4.314  5.371   0.42 19.05 ?  161 TYR   A HB3  1 
ATOM   3735 H HB3  B TYR   A 1 161 ? 5.810  -4.580  4.784   0.58 20.08 ?  161 TYR   A HB3  1 
ATOM   3736 H HD1  A TYR   A 1 161 ? 8.372  -6.460  6.302   0.42 19.27 ?  161 TYR   A HD1  1 
ATOM   3737 H HD1  B TYR   A 1 161 ? 8.256  -6.784  6.094   0.58 22.07 ?  161 TYR   A HD1  1 
ATOM   3738 H HD2  A TYR   A 1 161 ? 4.426  -5.888  6.642   0.42 19.69 ?  161 TYR   A HD2  1 
ATOM   3739 H HD2  B TYR   A 1 161 ? 4.378  -5.793  6.304   0.58 22.43 ?  161 TYR   A HD2  1 
ATOM   3740 H HE1  A TYR   A 1 161 ? 8.272  -8.118  7.890   0.42 20.02 ?  161 TYR   A HE1  1 
ATOM   3741 H HE1  B TYR   A 1 161 ? 8.017  -8.110  7.977   0.58 22.57 ?  161 TYR   A HE1  1 
ATOM   3742 H HE2  A TYR   A 1 161 ? 4.320  -7.550  8.234   0.42 20.32 ?  161 TYR   A HE2  1 
ATOM   3743 H HE2  B TYR   A 1 161 ? 4.134  -7.121  8.191   0.58 22.69 ?  161 TYR   A HE2  1 
ATOM   3744 H HH   A TYR   A 1 161 ? 5.436  -9.076  9.425   0.42 20.72 ?  161 TYR   A HH   1 
ATOM   3745 H HH   B TYR   A 1 161 ? 5.124  -8.485  9.691   0.58 24.01 ?  161 TYR   A HH   1 
ATOM   3746 N N    A ASP   A 1 162 ? 4.026  -6.049  3.598   0.42 17.88 ?  162 ASP   A N    1 
ATOM   3747 N N    B ASP   A 1 162 ? 4.023  -6.363  3.370   0.58 18.04 ?  162 ASP   A N    1 
ATOM   3748 C CA   A ASP   A 1 162 ? 2.873  -6.944  3.525   0.42 18.62 ?  162 ASP   A CA   1 
ATOM   3749 C CA   B ASP   A 1 162 ? 2.821  -7.192  3.326   0.58 19.35 ?  162 ASP   A CA   1 
ATOM   3750 C C    A ASP   A 1 162 ? 2.913  -7.794  2.260   0.42 19.04 ?  162 ASP   A C    1 
ATOM   3751 C C    B ASP   A 1 162 ? 2.861  -8.138  2.135   0.58 19.57 ?  162 ASP   A C    1 
ATOM   3752 O O    A ASP   A 1 162 ? 2.528  -8.969  2.282   0.42 19.67 ?  162 ASP   A O    1 
ATOM   3753 O O    B ASP   A 1 162 ? 2.516  -9.320  2.253   0.58 20.07 ?  162 ASP   A O    1 
ATOM   3754 C CB   A ASP   A 1 162 ? 1.569  -6.144  3.597   0.42 19.19 ?  162 ASP   A CB   1 
ATOM   3755 C CB   B ASP   A 1 162 ? 1.568  -6.307  3.247   0.58 21.20 ?  162 ASP   A CB   1 
ATOM   3756 C CG   A ASP   A 1 162 ? 1.271  -5.617  4.987   0.42 19.73 ?  162 ASP   A CG   1 
ATOM   3757 C CG   B ASP   A 1 162 ? 1.338  -5.480  4.497   0.58 22.96 ?  162 ASP   A CG   1 
ATOM   3758 O OD1  A ASP   A 1 162 ? 1.992  -5.973  5.942   0.42 20.98 ?  162 ASP   A OD1  1 
ATOM   3759 O OD1  B ASP   A 1 162 ? 1.885  -5.817  5.562   0.58 24.05 ?  162 ASP   A OD1  1 
ATOM   3760 O OD2  A ASP   A 1 162 ? 0.292  -4.848  5.117   0.42 19.55 -1 162 ASP   A OD2  1 
ATOM   3761 O OD2  B ASP   A 1 162 ? 0.571  -4.494  4.411   0.58 23.74 -1 162 ASP   A OD2  1 
ATOM   3762 H H    A ASP   A 1 162 ? 3.831  -5.211  3.523   0.42 21.46 ?  162 ASP   A H    1 
ATOM   3763 H H    B ASP   A 1 162 ? 3.866  -5.525  3.417   0.58 21.64 ?  162 ASP   A H    1 
ATOM   3764 H HA   A ASP   A 1 162 ? 2.889  -7.542  4.288   0.42 22.34 ?  162 ASP   A HA   1 
ATOM   3765 H HA   B ASP   A 1 162 ? 2.757  -7.726  4.135   0.58 23.22 ?  162 ASP   A HA   1 
ATOM   3766 H HB2  A ASP   A 1 162 ? 1.622  -5.387  2.995   0.42 23.03 ?  162 ASP   A HB2  1 
ATOM   3767 H HB2  B ASP   A 1 162 ? 1.656  -5.690  2.509   0.58 25.44 ?  162 ASP   A HB2  1 
ATOM   3768 H HB3  A ASP   A 1 162 ? 0.827  -6.717  3.351   0.42 23.03 ?  162 ASP   A HB3  1 
ATOM   3769 H HB3  B ASP   A 1 162 ? 0.783  -6.862  3.131   0.58 25.44 ?  162 ASP   A HB3  1 
ATOM   3770 N N    A LYS   A 1 163 ? 3.376  -7.222  1.145   0.42 19.75 ?  163 LYS   A N    1 
ATOM   3771 N N    B LYS   A 1 163 ? 3.293  -7.638  0.981   0.58 19.95 ?  163 LYS   A N    1 
ATOM   3772 C CA   A LYS   A 1 163 ? 3.458  -7.992  -0.093  0.42 20.34 ?  163 LYS   A CA   1 
ATOM   3773 C CA   B LYS   A 1 163 ? 3.389  -8.482  -0.202  0.58 20.82 ?  163 LYS   A CA   1 
ATOM   3774 C C    A LYS   A 1 163 ? 4.538  -9.066  -0.012  0.42 19.32 ?  163 LYS   A C    1 
ATOM   3775 C C    B LYS   A 1 163 ? 4.453  -9.561  -0.027  0.58 19.32 ?  163 LYS   A C    1 
ATOM   3776 O O    A LYS   A 1 163 ? 4.385  -10.151 -0.585  0.42 19.21 ?  163 LYS   A O    1 
ATOM   3777 O O    B LYS   A 1 163 ? 4.228  -10.724 -0.379  0.58 19.61 ?  163 LYS   A O    1 
ATOM   3778 C CB   A LYS   A 1 163 ? 3.716  -7.060  -1.277  0.42 22.29 ?  163 LYS   A CB   1 
ATOM   3779 C CB   B LYS   A 1 163 ? 3.683  -7.612  -1.422  0.58 23.54 ?  163 LYS   A CB   1 
ATOM   3780 C CG   A LYS   A 1 163 ? 3.728  -7.766  -2.627  0.42 24.26 ?  163 LYS   A CG   1 
ATOM   3781 C CG   B LYS   A 1 163 ? 3.977  -8.398  -2.681  0.58 26.84 ?  163 LYS   A CG   1 
ATOM   3782 C CD   A LYS   A 1 163 ? 4.164  -6.838  -3.746  0.42 26.22 ?  163 LYS   A CD   1 
ATOM   3783 C CD   B LYS   A 1 163 ? 4.781  -7.581  -3.668  0.58 29.67 ?  163 LYS   A CD   1 
ATOM   3784 C CE   A LYS   A 1 163 ? 4.107  -7.536  -5.098  0.42 27.62 ?  163 LYS   A CE   1 
ATOM   3785 C CE   B LYS   A 1 163 ? 3.888  -6.783  -4.596  0.58 31.20 ?  163 LYS   A CE   1 
ATOM   3786 N NZ   A LYS   A 1 163 ? 4.790  -6.755  -6.164  0.42 28.70 ?  163 LYS   A NZ   1 
ATOM   3787 N NZ   B LYS   A 1 163 ? 4.673  -6.222  -5.729  0.58 32.32 ?  163 LYS   A NZ   1 
ATOM   3788 H H    A LYS   A 1 163 ? 3.635  -6.405  1.083   0.42 23.69 ?  163 LYS   A H    1 
ATOM   3789 H H    B LYS   A 1 163 ? 3.535  -6.827  0.862   0.58 23.94 ?  163 LYS   A H    1 
ATOM   3790 H HA   A LYS   A 1 163 ? 2.609  -8.435  -0.241  0.42 24.41 ?  163 LYS   A HA   1 
ATOM   3791 H HA   B LYS   A 1 163 ? 2.538  -8.924  -0.349  0.58 24.98 ?  163 LYS   A HA   1 
ATOM   3792 H HB2  A LYS   A 1 163 ? 3.017  -6.386  -1.302  0.42 26.75 ?  163 LYS   A HB2  1 
ATOM   3793 H HB2  B LYS   A 1 163 ? 2.905  -7.051  -1.598  0.58 28.25 ?  163 LYS   A HB2  1 
ATOM   3794 H HB3  A LYS   A 1 163 ? 4.578  -6.634  -1.158  0.42 26.75 ?  163 LYS   A HB3  1 
ATOM   3795 H HB3  B LYS   A 1 163 ? 4.448  -7.052  -1.225  0.58 28.25 ?  163 LYS   A HB3  1 
ATOM   3796 H HG2  A LYS   A 1 163 ? 4.348  -8.512  -2.597  0.42 29.11 ?  163 LYS   A HG2  1 
ATOM   3797 H HG2  B LYS   A 1 163 ? 4.487  -9.195  -2.473  0.58 32.21 ?  163 LYS   A HG2  1 
ATOM   3798 H HG3  A LYS   A 1 163 ? 2.833  -8.084  -2.828  0.42 29.11 ?  163 LYS   A HG3  1 
ATOM   3799 H HG3  B LYS   A 1 163 ? 3.136  -8.645  -3.096  0.58 32.21 ?  163 LYS   A HG3  1 
ATOM   3800 H HD2  A LYS   A 1 163 ? 3.571  -6.070  -3.776  0.42 31.46 ?  163 LYS   A HD2  1 
ATOM   3801 H HD2  B LYS   A 1 163 ? 5.352  -6.961  -3.185  0.58 35.61 ?  163 LYS   A HD2  1 
ATOM   3802 H HD3  A LYS   A 1 163 ? 5.077  -6.551  -3.588  0.42 31.46 ?  163 LYS   A HD3  1 
ATOM   3803 H HD3  B LYS   A 1 163 ? 5.319  -8.181  -4.201  0.58 35.61 ?  163 LYS   A HD3  1 
ATOM   3804 H HE2  A LYS   A 1 163 ? 4.530  -8.405  -5.035  0.42 33.15 ?  163 LYS   A HE2  1 
ATOM   3805 H HE2  B LYS   A 1 163 ? 3.200  -7.364  -4.957  0.58 37.44 ?  163 LYS   A HE2  1 
ATOM   3806 H HE3  A LYS   A 1 163 ? 3.180  -7.643  -5.356  0.42 33.15 ?  163 LYS   A HE3  1 
ATOM   3807 H HE3  B LYS   A 1 163 ? 3.487  -6.049  -4.105  0.58 37.44 ?  163 LYS   A HE3  1 
ATOM   3808 H HZ1  A LYS   A 1 163 ? 4.742  -7.189  -6.939  0.42 34.45 ?  163 LYS   A HZ1  1 
ATOM   3809 H HZ1  B LYS   A 1 163 ? 5.312  -5.686  -5.419  0.58 38.78 ?  163 LYS   A HZ1  1 
ATOM   3810 H HZ2  A LYS   A 1 163 ? 4.401  -5.959  -6.253  0.42 34.45 ?  163 LYS   A HZ2  1 
ATOM   3811 H HZ2  B LYS   A 1 163 ? 5.051  -6.883  -6.192  0.58 38.78 ?  163 LYS   A HZ2  1 
ATOM   3812 H HZ3  A LYS   A 1 163 ? 5.647  -6.635  -5.953  0.42 34.45 ?  163 LYS   A HZ3  1 
ATOM   3813 H HZ3  B LYS   A 1 163 ? 4.140  -5.759  -6.267  0.58 38.78 ?  163 LYS   A HZ3  1 
ATOM   3814 N N    A LEU   A 1 164 ? 5.642  -8.780  0.683   0.42 17.90 ?  164 LEU   A N    1 
ATOM   3815 N N    B LEU   A 1 164 ? 5.626  -9.193  0.496   0.58 17.95 ?  164 LEU   A N    1 
ATOM   3816 C CA   A LEU   A 1 164 ? 6.734  -9.745  0.791   0.42 17.08 ?  164 LEU   A CA   1 
ATOM   3817 C CA   B LEU   A 1 164 ? 6.682  -10.182 0.702   0.58 17.70 ?  164 LEU   A CA   1 
ATOM   3818 C C    A LEU   A 1 164 ? 6.310  -10.966 1.595   0.42 17.37 ?  164 LEU   A C    1 
ATOM   3819 C C    B LEU   A 1 164 ? 6.231  -11.272 1.672   0.58 18.24 ?  164 LEU   A C    1 
ATOM   3820 O O    A LEU   A 1 164 ? 6.587  -12.106 1.205   0.42 17.24 ?  164 LEU   A O    1 
ATOM   3821 O O    B LEU   A 1 164 ? 6.496  -12.460 1.448   0.58 18.89 ?  164 LEU   A O    1 
ATOM   3822 C CB   A LEU   A 1 164 ? 7.944  -9.083  1.448   0.42 16.24 ?  164 LEU   A CB   1 
ATOM   3823 C CB   B LEU   A 1 164 ? 7.956  -9.495  1.202   0.58 17.13 ?  164 LEU   A CB   1 
ATOM   3824 C CG   A LEU   A 1 164 ? 8.711  -8.071  0.598   0.42 16.15 ?  164 LEU   A CG   1 
ATOM   3825 C CG   B LEU   A 1 164 ? 8.645  -8.494  0.267   0.58 17.21 ?  164 LEU   A CG   1 
ATOM   3826 C CD1  A LEU   A 1 164 ? 9.642  -7.243  1.466   0.42 15.70 ?  164 LEU   A CD1  1 
ATOM   3827 C CD1  B LEU   A 1 164 ? 9.750  -7.751  1.009   0.58 16.45 ?  164 LEU   A CD1  1 
ATOM   3828 C CD2  A LEU   A 1 164 ? 9.494  -8.783  -0.493  0.42 16.00 ?  164 LEU   A CD2  1 
ATOM   3829 C CD2  B LEU   A 1 164 ? 9.201  -9.203  -0.955  0.58 18.02 ?  164 LEU   A CD2  1 
ATOM   3830 H H    A LEU   A 1 164 ? 5.783  -8.040  1.098   0.42 21.48 ?  164 LEU   A H    1 
ATOM   3831 H H    B LEU   A 1 164 ? 5.831  -8.398  0.741   0.58 21.54 ?  164 LEU   A H    1 
ATOM   3832 H HA   A LEU   A 1 164 ? 6.987  -10.045 -0.093  0.42 20.50 ?  164 LEU   A HA   1 
ATOM   3833 H HA   B LEU   A 1 164 ? 6.887  -10.611 -0.144  0.58 21.24 ?  164 LEU   A HA   1 
ATOM   3834 H HB2  A LEU   A 1 164 ? 7.638  -8.622  2.245   0.42 19.48 ?  164 LEU   A HB2  1 
ATOM   3835 H HB2  B LEU   A 1 164 ? 7.739  -9.019  2.016   0.58 20.55 ?  164 LEU   A HB2  1 
ATOM   3836 H HB3  A LEU   A 1 164 ? 8.568  -9.780  1.703   0.42 19.48 ?  164 LEU   A HB3  1 
ATOM   3837 H HB3  B LEU   A 1 164 ? 8.610  -10.185 1.403   0.58 20.55 ?  164 LEU   A HB3  1 
ATOM   3838 H HG   A LEU   A 1 164 ? 8.078  -7.469  0.177   0.42 19.38 ?  164 LEU   A HG   1 
ATOM   3839 H HG   B LEU   A 1 164 ? 7.997  -7.841  -0.033  0.58 20.65 ?  164 LEU   A HG   1 
ATOM   3840 H HD11 A LEU   A 1 164 ? 10.118 -6.613  0.904   0.42 18.84 ?  164 LEU   A HD11 1 
ATOM   3841 H HD11 B LEU   A 1 164 ? 10.174 -7.124  0.403   0.58 19.75 ?  164 LEU   A HD11 1 
ATOM   3842 H HD12 A LEU   A 1 164 ? 9.117  -6.765  2.128   0.42 18.84 ?  164 LEU   A HD12 1 
ATOM   3843 H HD12 B LEU   A 1 164 ? 9.363  -7.274  1.761   0.58 19.75 ?  164 LEU   A HD12 1 
ATOM   3844 H HD13 A LEU   A 1 164 ? 10.271 -7.835  1.908   0.42 18.84 ?  164 LEU   A HD13 1 
ATOM   3845 H HD13 B LEU   A 1 164 ? 10.405 -8.394  1.329   0.58 19.75 ?  164 LEU   A HD13 1 
ATOM   3846 H HD21 A LEU   A 1 164 ? 10.014 -8.129  -0.984  0.42 19.21 ?  164 LEU   A HD21 1 
ATOM   3847 H HD21 B LEU   A 1 164 ? 9.681  -8.560  -1.501  0.58 21.62 ?  164 LEU   A HD21 1 
ATOM   3848 H HD22 A LEU   A 1 164 ? 10.082 -9.437  -0.084  0.42 19.21 ?  164 LEU   A HD22 1 
ATOM   3849 H HD22 B LEU   A 1 164 ? 9.802  -9.906  -0.666  0.58 21.62 ?  164 LEU   A HD22 1 
ATOM   3850 H HD23 A LEU   A 1 164 ? 8.871  -9.226  -1.091  0.42 19.21 ?  164 LEU   A HD23 1 
ATOM   3851 H HD23 B LEU   A 1 164 ? 8.465  -9.581  -1.460  0.58 21.62 ?  164 LEU   A HD23 1 
ATOM   3852 N N    A VAL   A 1 165 ? 5.657  -10.738 2.736   0.42 17.87 ?  165 VAL   A N    1 
ATOM   3853 N N    B VAL   A 1 165 ? 5.551  -10.885 2.757   0.58 18.81 ?  165 VAL   A N    1 
ATOM   3854 C CA   A VAL   A 1 165 ? 5.227  -11.832 3.600   0.42 18.08 ?  165 VAL   A CA   1 
ATOM   3855 C CA   B VAL   A 1 165 ? 5.083  -11.851 3.753   0.58 19.20 ?  165 VAL   A CA   1 
ATOM   3856 C C    A VAL   A 1 165 ? 4.168  -12.677 2.903   0.42 17.86 ?  165 VAL   A C    1 
ATOM   3857 C C    B VAL   A 1 165 ? 4.050  -12.800 3.151   0.58 18.99 ?  165 VAL   A C    1 
ATOM   3858 O O    A VAL   A 1 165 ? 4.290  -13.902 2.803   0.42 18.10 ?  165 VAL   A O    1 
ATOM   3859 O O    B VAL   A 1 165 ? 3.979  -13.982 3.518   0.58 18.78 ?  165 VAL   A O    1 
ATOM   3860 C CB   A VAL   A 1 165 ? 4.717  -11.265 4.939   0.42 19.51 ?  165 VAL   A CB   1 
ATOM   3861 C CB   B VAL   A 1 165 ? 4.520  -11.110 4.985   0.58 20.53 ?  165 VAL   A CB   1 
ATOM   3862 C CG1  A VAL   A 1 165 ? 3.993  -12.338 5.740   0.42 19.94 ?  165 VAL   A CG1  1 
ATOM   3863 C CG1  B VAL   A 1 165 ? 3.764  -12.072 5.899   0.58 20.95 ?  165 VAL   A CG1  1 
ATOM   3864 C CG2  A VAL   A 1 165 ? 5.868  -10.650 5.732   0.42 19.73 ?  165 VAL   A CG2  1 
ATOM   3865 C CG2  B VAL   A 1 165 ? 5.638  -10.416 5.748   0.58 20.71 ?  165 VAL   A CG2  1 
ATOM   3866 H H    A VAL   A 1 165 ? 5.449  -9.959  3.031   0.42 21.45 ?  165 VAL   A H    1 
ATOM   3867 H H    B VAL   A 1 165 ? 5.360  -10.066 2.942   0.58 22.57 ?  165 VAL   A H    1 
ATOM   3868 H HA   A VAL   A 1 165 ? 5.984  -12.405 3.791   0.42 21.70 ?  165 VAL   A HA   1 
ATOM   3869 H HA   B VAL   A 1 165 ? 5.838  -12.379 4.051   0.58 23.04 ?  165 VAL   A HA   1 
ATOM   3870 H HB   A VAL   A 1 165 ? 4.081  -10.556 4.755   0.42 23.42 ?  165 VAL   A HB   1 
ATOM   3871 H HB   B VAL   A 1 165 ? 3.896  -10.430 4.687   0.58 24.64 ?  165 VAL   A HB   1 
ATOM   3872 H HG11 A VAL   A 1 165 ? 3.936  -12.053 6.664   0.42 23.93 ?  165 VAL   A HG11 1 
ATOM   3873 H HG11 B VAL   A 1 165 ? 3.652  -11.655 6.768   0.58 25.14 ?  165 VAL   A HG11 1 
ATOM   3874 H HG12 A VAL   A 1 165 ? 3.100  -12.453 5.375   0.42 23.93 ?  165 VAL   A HG12 1 
ATOM   3875 H HG12 B VAL   A 1 165 ? 2.894  -12.261 5.512   0.58 25.14 ?  165 VAL   A HG12 1 
ATOM   3876 H HG13 A VAL   A 1 165 ? 4.490  -13.165 5.677   0.42 23.93 ?  165 VAL   A HG13 1 
ATOM   3877 H HG13 B VAL   A 1 165 ? 4.275  -12.890 5.989   0.58 25.14 ?  165 VAL   A HG13 1 
ATOM   3878 H HG21 A VAL   A 1 165 ? 5.528  -10.305 6.573   0.42 23.68 ?  165 VAL   A HG21 1 
ATOM   3879 H HG21 B VAL   A 1 165 ? 5.259  -9.956  6.515   0.58 24.85 ?  165 VAL   A HG21 1 
ATOM   3880 H HG22 A VAL   A 1 165 ? 6.538  -11.330 5.899   0.42 23.68 ?  165 VAL   A HG22 1 
ATOM   3881 H HG22 B VAL   A 1 165 ? 6.280  -11.079 6.044   0.58 24.85 ?  165 VAL   A HG22 1 
ATOM   3882 H HG23 A VAL   A 1 165 ? 6.257  -9.925  5.214   0.42 23.68 ?  165 VAL   A HG23 1 
ATOM   3883 H HG23 B VAL   A 1 165 ? 6.070  -9.775  5.161   0.58 24.85 ?  165 VAL   A HG23 1 
ATOM   3884 N N    A SER   A 1 166 ? 3.120  -12.028 2.395   0.42 17.77 ?  166 SER   A N    1 
ATOM   3885 N N    B SER   A 1 166 ? 3.217  -12.295 2.243   0.58 20.25 ?  166 SER   A N    1 
ATOM   3886 C CA   A SER   A 1 166 ? 2.008  -12.765 1.806   0.42 17.81 ?  166 SER   A CA   1 
ATOM   3887 C CA   B SER   A 1 166 ? 2.125  -13.071 1.667   0.58 21.98 ?  166 SER   A CA   1 
ATOM   3888 C C    A SER   A 1 166 ? 2.456  -13.634 0.639   0.42 17.86 ?  166 SER   A C    1 
ATOM   3889 C C    B SER   A 1 166 ? 2.530  -13.830 0.409   0.58 24.31 ?  166 SER   A C    1 
ATOM   3890 O O    A SER   A 1 166 ? 1.884  -14.710 0.413   0.42 19.02 ?  166 SER   A O    1 
ATOM   3891 O O    B SER   A 1 166 ? 1.659  -14.380 -0.276  0.58 24.55 ?  166 SER   A O    1 
ATOM   3892 C CB   A SER   A 1 166 ? 0.913  -11.787 1.373   0.42 18.29 ?  166 SER   A CB   1 
ATOM   3893 C CB   B SER   A 1 166 ? 0.932  -12.161 1.358   0.58 21.97 ?  166 SER   A CB   1 
ATOM   3894 O OG   A SER   A 1 166 ? 0.451  -11.036 2.485   0.42 19.41 ?  166 SER   A OG   1 
ATOM   3895 O OG   B SER   A 1 166 ? 1.241  -11.232 0.333   0.58 22.46 ?  166 SER   A OG   1 
ATOM   3896 H H    A SER   A 1 166 ? 3.028  -11.173 2.381   0.42 21.32 ?  166 SER   A H    1 
ATOM   3897 H H    B SER   A 1 166 ? 3.258  -11.489 1.948   0.58 24.30 ?  166 SER   A H    1 
ATOM   3898 H HA   A SER   A 1 166 ? 1.625  -13.350 2.469   0.42 21.37 ?  166 SER   A HA   1 
ATOM   3899 H HA   B SER   A 1 166 ? 1.833  -13.718 2.324   0.58 26.37 ?  166 SER   A HA   1 
ATOM   3900 H HB2  A SER   A 1 166 ? 1.268  -11.176 0.707   0.42 21.94 ?  166 SER   A HB2  1 
ATOM   3901 H HB2  B SER   A 1 166 ? 0.185  -12.709 1.068   0.58 26.37 ?  166 SER   A HB2  1 
ATOM   3902 H HB3  A SER   A 1 166 ? 0.164  -12.282 1.002   0.42 21.94 ?  166 SER   A HB3  1 
ATOM   3903 H HB3  B SER   A 1 166 ? 0.689  -11.676 2.163   0.58 26.37 ?  166 SER   A HB3  1 
ATOM   3904 H HG   A SER   A 1 166 ? 1.084  -10.587 2.811   0.42 23.29 ?  166 SER   A HG   1 
ATOM   3905 H HG   B SER   A 1 166 ? 1.884  -10.746 0.570   0.58 26.95 ?  166 SER   A HG   1 
ATOM   3906 N N    A SER   A 1 167 ? 3.482  -13.200 -0.096  0.42 17.69 ?  167 SER   A N    1 
ATOM   3907 N N    B SER   A 1 167 ? 3.821  -13.878 0.094   0.58 26.66 ?  167 SER   A N    1 
ATOM   3908 C CA   A SER   A 1 167 ? 3.952  -13.921 -1.271  0.42 18.35 ?  167 SER   A CA   1 
ATOM   3909 C CA   B SER   A 1 167 ? 4.317  -14.532 -1.106  0.58 29.58 ?  167 SER   A CA   1 
ATOM   3910 C C    A SER   A 1 167 ? 5.134  -14.839 -0.984  0.42 18.46 ?  167 SER   A C    1 
ATOM   3911 C C    B SER   A 1 167 ? 5.057  -15.812 -0.743  0.58 32.23 ?  167 SER   A C    1 
ATOM   3912 O O    A SER   A 1 167 ? 5.616  -15.502 -1.908  0.42 19.06 ?  167 SER   A O    1 
ATOM   3913 O O    B SER   A 1 167 ? 5.838  -15.842 0.214   0.58 32.50 ?  167 SER   A O    1 
ATOM   3914 C CB   A SER   A 1 167 ? 4.331  -12.938 -2.385  0.42 18.98 ?  167 SER   A CB   1 
ATOM   3915 C CB   B SER   A 1 167 ? 5.274  -13.617 -1.867  0.58 30.19 ?  167 SER   A CB   1 
ATOM   3916 O OG   A SER   A 1 167 ? 5.461  -12.172 -2.010  0.42 18.75 ?  167 SER   A OG   1 
ATOM   3917 O OG   B SER   A 1 167 ? 4.684  -12.362 -2.149  0.58 30.72 ?  167 SER   A OG   1 
ATOM   3918 H H    A SER   A 1 167 ? 3.925  -12.472 0.066   0.42 21.23 ?  167 SER   A H    1 
ATOM   3919 H H    B SER   A 1 167 ? 4.441  -13.523 0.574   0.58 31.99 ?  167 SER   A H    1 
ATOM   3920 H HA   A SER   A 1 167 ? 3.231  -14.465 -1.609  0.42 22.02 ?  167 SER   A HA   1 
ATOM   3921 H HA   B SER   A 1 167 ? 3.574  -14.757 -1.684  0.58 35.50 ?  167 SER   A HA   1 
ATOM   3922 H HB2  A SER   A 1 167 ? 4.545  -13.435 -3.193  0.42 22.78 ?  167 SER   A HB2  1 
ATOM   3923 H HB2  B SER   A 1 167 ? 6.054  -13.482 -1.315  0.58 36.23 ?  167 SER   A HB2  1 
ATOM   3924 H HB3  A SER   A 1 167 ? 3.584  -12.340 -2.559  0.42 22.78 ?  167 SER   A HB3  1 
ATOM   3925 H HB3  B SER   A 1 167 ? 5.526  -14.047 -2.699  0.58 36.23 ?  167 SER   A HB3  1 
ATOM   3926 H HG   A SER   A 1 167 ? 5.289  -11.716 -1.327  0.42 22.50 ?  167 SER   A HG   1 
ATOM   3927 H HG   B SER   A 1 167 ? 4.434  -11.999 -1.434  0.58 36.87 ?  167 SER   A HG   1 
ATOM   3928 N N    A PHE   A 1 168 ? 5.621  -14.895 0.254   0.42 18.21 ?  168 PHE   A N    1 
ATOM   3929 N N    B PHE   A 1 168 ? 4.811  -16.862 -1.526  0.58 34.70 ?  168 PHE   A N    1 
ATOM   3930 C CA   A PHE   A 1 168 ? 6.814  -15.687 0.530   0.42 18.63 ?  168 PHE   A CA   1 
ATOM   3931 C CA   B PHE   A 1 168 ? 5.477  -18.152 -1.376  0.58 37.45 ?  168 PHE   A CA   1 
ATOM   3932 C C    A PHE   A 1 168 ? 6.499  -17.173 0.450   0.42 21.70 ?  168 PHE   A C    1 
ATOM   3933 C C    B PHE   A 1 168 ? 6.662  -18.262 -2.329  0.58 40.03 ?  168 PHE   A C    1 
ATOM   3934 O O    A PHE   A 1 168 ? 5.544  -17.657 1.067   0.42 23.20 ?  168 PHE   A O    1 
ATOM   3935 O O    B PHE   A 1 168 ? 7.802  -18.467 -1.899  0.58 39.97 ?  168 PHE   A O    1 
ATOM   3936 C CB   A PHE   A 1 168 ? 7.407  -15.356 1.898   0.42 17.20 ?  168 PHE   A CB   1 
ATOM   3937 C CB   B PHE   A 1 168 ? 4.456  -19.263 -1.664  0.58 37.75 ?  168 PHE   A CB   1 
ATOM   3938 C CG   A PHE   A 1 168 ? 8.672  -16.123 2.195   0.42 16.24 ?  168 PHE   A CG   1 
ATOM   3939 C CG   B PHE   A 1 168 ? 4.892  -20.634 -1.230  0.58 38.02 ?  168 PHE   A CG   1 
ATOM   3940 C CD1  A PHE   A 1 168 ? 9.835  -15.844 1.502   0.42 16.47 ?  168 PHE   A CD1  1 
ATOM   3941 C CD1  B PHE   A 1 168 ? 4.776  -21.024 0.093   0.58 38.12 ?  168 PHE   A CD1  1 
ATOM   3942 C CD2  A PHE   A 1 168 ? 8.693  -17.137 3.144   0.42 14.32 ?  168 PHE   A CD2  1 
ATOM   3943 C CD2  B PHE   A 1 168 ? 5.391  -21.543 -2.150  0.58 38.13 ?  168 PHE   A CD2  1 
ATOM   3944 C CE1  A PHE   A 1 168 ? 10.992 -16.547 1.755   0.42 16.04 ?  168 PHE   A CE1  1 
ATOM   3945 C CE1  B PHE   A 1 168 ? 5.164  -22.289 0.495   0.58 38.18 ?  168 PHE   A CE1  1 
ATOM   3946 C CE2  A PHE   A 1 168 ? 9.858  -17.839 3.405   0.42 14.37 ?  168 PHE   A CE2  1 
ATOM   3947 C CE2  B PHE   A 1 168 ? 5.781  -22.810 -1.754  0.58 38.19 ?  168 PHE   A CE2  1 
ATOM   3948 C CZ   A PHE   A 1 168 ? 11.006 -17.543 2.708   0.42 15.39 ?  168 PHE   A CZ   1 
ATOM   3949 C CZ   B PHE   A 1 168 ? 5.667  -23.182 -0.429  0.58 38.22 ?  168 PHE   A CZ   1 
ATOM   3950 H H    A PHE   A 1 168 ? 5.285  -14.490 0.935   0.42 21.86 ?  168 PHE   A H    1 
ATOM   3951 H H    B PHE   A 1 168 ? 4.247  -16.846 -2.174  0.58 41.64 ?  168 PHE   A H    1 
ATOM   3952 H HA   A PHE   A 1 168 ? 7.483  -15.485 -0.141  0.42 22.36 ?  168 PHE   A HA   1 
ATOM   3953 H HA   B PHE   A 1 168 ? 5.796  -18.253 -0.463  0.58 44.94 ?  168 PHE   A HA   1 
ATOM   3954 H HB2  A PHE   A 1 168 ? 7.615  -14.409 1.930   0.42 20.64 ?  168 PHE   A HB2  1 
ATOM   3955 H HB2  B PHE   A 1 168 ? 3.631  -19.058 -1.199  0.58 45.30 ?  168 PHE   A HB2  1 
ATOM   3956 H HB3  A PHE   A 1 168 ? 6.755  -15.573 2.584   0.42 20.64 ?  168 PHE   A HB3  1 
ATOM   3957 H HB3  B PHE   A 1 168 ? 4.294  -19.296 -2.620  0.58 45.30 ?  168 PHE   A HB3  1 
ATOM   3958 H HD1  A PHE   A 1 168 ? 9.839  -15.171 0.859   0.42 19.77 ?  168 PHE   A HD1  1 
ATOM   3959 H HD1  B PHE   A 1 168 ? 4.437  -20.427 0.720   0.58 45.75 ?  168 PHE   A HD1  1 
ATOM   3960 H HD2  A PHE   A 1 168 ? 7.917  -17.339 3.618   0.42 17.19 ?  168 PHE   A HD2  1 
ATOM   3961 H HD2  B PHE   A 1 168 ? 5.470  -21.296 -3.043  0.58 45.76 ?  168 PHE   A HD2  1 
ATOM   3962 H HE1  A PHE   A 1 168 ? 11.772 -16.343 1.287   0.42 19.25 ?  168 PHE   A HE1  1 
ATOM   3963 H HE1  B PHE   A 1 168 ? 5.084  -22.538 1.388   0.58 45.81 ?  168 PHE   A HE1  1 
ATOM   3964 H HE2  A PHE   A 1 168 ? 9.863  -18.514 4.045   0.42 17.25 ?  168 PHE   A HE2  1 
ATOM   3965 H HE2  B PHE   A 1 168 ? 6.118  -23.411 -2.379  0.58 45.83 ?  168 PHE   A HE2  1 
ATOM   3966 H HZ   A PHE   A 1 168 ? 11.789 -18.015 2.879   0.42 18.46 ?  168 PHE   A HZ   1 
ATOM   3967 H HZ   B PHE   A 1 168 ? 5.926  -24.034 -0.161  0.58 45.87 ?  168 PHE   A HZ   1 
ATOM   3968 N N    A LEU   A 1 169 ? 7.316  -17.896 -0.308  0.42 23.40 ?  169 LEU   A N    1 
ATOM   3969 N N    B LEU   A 1 169 ? 6.403  -18.121 -3.625  0.58 42.64 ?  169 LEU   A N    1 
ATOM   3970 C CA   A LEU   A 1 169 ? 7.149  -19.330 -0.461  0.42 25.51 ?  169 LEU   A CA   1 
ATOM   3971 C CA   B LEU   A 1 169 ? 7.436  -18.116 -4.655  0.58 45.24 ?  169 LEU   A CA   1 
ATOM   3972 C C    A LEU   A 1 169 ? 8.046  -20.060 0.528   0.42 26.15 ?  169 LEU   A C    1 
ATOM   3973 C C    B LEU   A 1 169 ? 7.970  -16.703 -4.868  0.58 46.34 ?  169 LEU   A C    1 
ATOM   3974 O O    A LEU   A 1 169 ? 7.587  -20.552 1.560   0.42 26.23 ?  169 LEU   A O    1 
ATOM   3975 O O    B LEU   A 1 169 ? 7.397  -15.917 -5.623  0.58 46.88 ?  169 LEU   A O    1 
ATOM   3976 C CB   A LEU   A 1 169 ? 7.492  -19.748 -1.893  0.42 26.94 ?  169 LEU   A CB   1 
ATOM   3977 C CB   B LEU   A 1 169 ? 6.843  -18.658 -5.960  0.58 46.58 ?  169 LEU   A CB   1 
ATOM   3978 C CG   A LEU   A 1 169 ? 7.156  -21.187 -2.287  0.42 28.41 ?  169 LEU   A CG   1 
ATOM   3979 C CG   B LEU   A 1 169 ? 7.550  -18.487 -7.307  0.58 47.64 ?  169 LEU   A CG   1 
ATOM   3980 C CD1  A LEU   A 1 169 ? 5.723  -21.520 -1.913  0.42 29.02 ?  169 LEU   A CD1  1 
ATOM   3981 C CD1  B LEU   A 1 169 ? 7.888  -19.839 -7.920  0.58 48.09 ?  169 LEU   A CD1  1 
ATOM   3982 C CD2  A LEU   A 1 169 ? 7.377  -21.385 -3.778  0.42 28.68 ?  169 LEU   A CD2  1 
ATOM   3983 C CD2  B LEU   A 1 169 ? 6.663  -17.686 -8.251  0.58 48.17 ?  169 LEU   A CD2  1 
ATOM   3984 O OXT  A LEU   A 1 169 ? 9.254  -20.163 0.322   0.42 26.45 -1 169 LEU   A OXT  1 
ATOM   3985 O OXT  B LEU   A 1 169 ? 8.988  -16.314 -4.295  0.58 46.77 -1 169 LEU   A OXT  1 
ATOM   3986 H H    A LEU   A 1 169 ? 7.979  -17.571 -0.750  0.42 28.07 ?  169 LEU   A H    1 
ATOM   3987 H H    B LEU   A 1 169 ? 5.610  -18.037 -3.939  0.58 51.17 ?  169 LEU   A H    1 
ATOM   3988 H HA   A LEU   A 1 169 ? 6.227  -19.563 -0.275  0.42 30.62 ?  169 LEU   A HA   1 
ATOM   3989 H HA   B LEU   A 1 169 ? 8.168  -18.686 -4.378  0.58 54.29 ?  169 LEU   A HA   1 
ATOM   3990 H HB2  A LEU   A 1 169 ? 7.014  -19.166 -2.502  0.42 32.32 ?  169 LEU   A HB2  1 
ATOM   3991 H HB2  B LEU   A 1 169 ? 6.727  -19.608 -5.839  0.58 55.90 ?  169 LEU   A HB2  1 
ATOM   3992 H HB3  A LEU   A 1 169 ? 8.446  -19.633 -2.021  0.42 32.32 ?  169 LEU   A HB3  1 
ATOM   3993 H HB3  B LEU   A 1 169 ? 5.974  -18.247 -6.065  0.58 55.90 ?  169 LEU   A HB3  1 
ATOM   3994 H HG   A LEU   A 1 169 ? 7.744  -21.795 -1.811  0.42 34.10 ?  169 LEU   A HG   1 
ATOM   3995 H HG   B LEU   A 1 169 ? 8.378  -18.001 -7.185  0.58 57.17 ?  169 LEU   A HG   1 
ATOM   3996 H HD11 A LEU   A 1 169 ? 5.460  -22.333 -2.368  0.42 34.83 ?  169 LEU   A HD11 1 
ATOM   3997 H HD11 B LEU   A 1 169 ? 8.337  -19.699 -8.769  0.58 57.71 ?  169 LEU   A HD11 1 
ATOM   3998 H HD12 A LEU   A 1 169 ? 5.669  -21.645 -0.952  0.42 34.83 ?  169 LEU   A HD12 1 
ATOM   3999 H HD12 B LEU   A 1 169 ? 8.470  -20.323 -7.314  0.58 57.71 ?  169 LEU   A HD12 1 
ATOM   4000 H HD13 A LEU   A 1 169 ? 5.149  -20.786 -2.185  0.42 34.83 ?  169 LEU   A HD13 1 
ATOM   4001 H HD13 B LEU   A 1 169 ? 7.067  -20.338 -8.059  0.58 57.71 ?  169 LEU   A HD13 1 
ATOM   4002 H HD21 A LEU   A 1 169 ? 7.167  -22.303 -4.009  0.42 34.41 ?  169 LEU   A HD21 1 
ATOM   4003 H HD21 B LEU   A 1 169 ? 7.119  -17.575 -9.099  0.58 57.80 ?  169 LEU   A HD21 1 
ATOM   4004 H HD22 A LEU   A 1 169 ? 6.796  -20.780 -4.266  0.42 34.41 ?  169 LEU   A HD22 1 
ATOM   4005 H HD22 B LEU   A 1 169 ? 5.828  -18.165 -8.385  0.58 57.80 ?  169 LEU   A HD22 1 
ATOM   4006 H HD23 A LEU   A 1 169 ? 8.305  -21.195 -3.988  0.42 34.41 ?  169 LEU   A HD23 1 
ATOM   4007 H HD23 B LEU   A 1 169 ? 6.485  -16.819 -7.854  0.58 57.80 ?  169 LEU   A HD23 1 
ATOM   4008 N N    A SER   B 1 1   ? 50.881 -9.259  -23.719 0.42 28.55 ?  1   SER   B N    1 
ATOM   4009 N N    B SER   B 1 1   ? 50.831 -9.285  -23.741 0.58 27.04 ?  1   SER   B N    1 
ATOM   4010 C CA   A SER   B 1 1   ? 51.407 -10.338 -22.856 0.42 28.26 ?  1   SER   B CA   1 
ATOM   4011 C CA   B SER   B 1 1   ? 51.323 -10.277 -22.764 0.58 26.47 ?  1   SER   B CA   1 
ATOM   4012 C C    A SER   B 1 1   ? 50.337 -11.390 -22.595 0.42 27.40 ?  1   SER   B C    1 
ATOM   4013 C C    B SER   B 1 1   ? 50.280 -11.356 -22.526 0.58 24.96 ?  1   SER   B C    1 
ATOM   4014 O O    A SER   B 1 1   ? 49.154 -11.189 -22.891 0.42 27.24 ?  1   SER   B O    1 
ATOM   4015 O O    B SER   B 1 1   ? 49.081 -11.171 -22.782 0.58 24.98 ?  1   SER   B O    1 
ATOM   4016 C CB   A SER   B 1 1   ? 51.916 -9.770  -21.534 0.42 28.96 ?  1   SER   B CB   1 
ATOM   4017 C CB   B SER   B 1 1   ? 51.678 -9.607  -21.441 0.58 27.54 ?  1   SER   B CB   1 
ATOM   4018 O OG   A SER   B 1 1   ? 50.840 -9.445  -20.676 0.42 30.25 ?  1   SER   B OG   1 
ATOM   4019 O OG   B SER   B 1 1   ? 50.531 -9.476  -20.621 0.58 29.21 ?  1   SER   B OG   1 
ATOM   4020 H H1   A SER   B 1 1   ? 50.774 -9.574  -24.542 0.42 34.26 ?  1   SER   B H1   1 
ATOM   4021 H H1   B SER   B 1 1   ? 50.738 -9.680  -24.530 0.58 32.44 ?  1   SER   B H1   1 
ATOM   4022 H H2   A SER   B 1 1   ? 50.103 -8.983  -23.396 0.42 34.26 ?  1   SER   B H2   1 
ATOM   4023 H H2   B SER   B 1 1   ? 50.051 -8.970  -23.465 0.58 32.44 ?  1   SER   B H2   1 
ATOM   4024 H H3   A SER   B 1 1   ? 51.462 -8.588  -23.726 0.42 34.26 ?  1   SER   B H3   1 
ATOM   4025 H H3   B SER   B 1 1   ? 51.422 -8.626  -23.799 0.58 32.44 ?  1   SER   B H3   1 
ATOM   4026 H HA   A SER   B 1 1   ? 52.146 -10.758 -23.314 0.42 33.91 ?  1   SER   B HA   1 
ATOM   4027 H HA   B SER   B 1 1   ? 52.117 -10.693 -23.123 0.58 31.76 ?  1   SER   B HA   1 
ATOM   4028 H HB2  A SER   B 1 1   ? 52.473 -10.436 -21.108 0.42 34.75 ?  1   SER   B HB2  1 
ATOM   4029 H HB2  B SER   B 1 1   ? 52.338 -10.152 -20.986 0.58 33.05 ?  1   SER   B HB2  1 
ATOM   4030 H HB3  A SER   B 1 1   ? 52.431 -8.967  -21.712 0.42 34.75 ?  1   SER   B HB3  1 
ATOM   4031 H HB3  B SER   B 1 1   ? 52.041 -8.725  -21.621 0.58 33.05 ?  1   SER   B HB3  1 
ATOM   4032 H HG   A SER   B 1 1   ? 51.128 -9.031  -20.005 0.42 36.30 ?  1   SER   B HG   1 
ATOM   4033 H HG   B SER   B 1 1   ? 50.697 -8.946  -19.988 0.58 35.05 ?  1   SER   B HG   1 
ATOM   4034 N N    A MET   B 1 2   ? 50.767 -12.512 -22.029 0.42 27.07 ?  2   MET   B N    1 
ATOM   4035 N N    B MET   B 1 2   ? 50.755 -12.490 -22.029 0.58 24.03 ?  2   MET   B N    1 
ATOM   4036 C CA   A MET   B 1 2   ? 49.932 -13.695 -21.859 0.42 26.79 ?  2   MET   B CA   1 
ATOM   4037 C CA   B MET   B 1 2   ? 49.940 -13.680 -21.834 0.58 24.01 ?  2   MET   B CA   1 
ATOM   4038 C C    A MET   B 1 2   ? 49.680 -13.912 -20.371 0.42 24.53 ?  2   MET   B C    1 
ATOM   4039 C C    B MET   B 1 2   ? 49.690 -13.843 -20.346 0.58 23.17 ?  2   MET   B C    1 
ATOM   4040 O O    A MET   B 1 2   ? 50.603 -14.246 -19.622 0.42 24.90 ?  2   MET   B O    1 
ATOM   4041 O O    B MET   B 1 2   ? 50.628 -14.049 -19.571 0.58 23.54 ?  2   MET   B O    1 
ATOM   4042 C CB   A MET   B 1 2   ? 50.634 -14.900 -22.475 0.42 29.73 ?  2   MET   B CB   1 
ATOM   4043 C CB   B MET   B 1 2   ? 50.682 -14.879 -22.392 0.58 26.77 ?  2   MET   B CB   1 
ATOM   4044 C CG   A MET   B 1 2   ? 49.768 -16.140 -22.605 0.42 32.51 ?  2   MET   B CG   1 
ATOM   4045 C CG   B MET   B 1 2   ? 49.806 -16.059 -22.801 0.58 28.78 ?  2   MET   B CG   1 
ATOM   4046 S SD   A MET   B 1 2   ? 50.602 -17.441 -23.535 0.42 34.87 ?  2   MET   B SD   1 
ATOM   4047 S SD   B MET   B 1 2   ? 50.692 -17.135 -23.938 0.58 30.85 ?  2   MET   B SD   1 
ATOM   4048 C CE   A MET   B 1 2   ? 51.184 -16.485 -24.935 0.42 34.83 ?  2   MET   B CE   1 
ATOM   4049 C CE   B MET   B 1 2   ? 51.730 -15.944 -24.745 0.58 31.23 ?  2   MET   B CE   1 
ATOM   4050 H H    A MET   B 1 2   ? 51.569 -12.617 -21.735 0.42 32.48 ?  2   MET   B H    1 
ATOM   4051 H H    B MET   B 1 2   ? 51.579 -12.609 -21.796 0.58 28.83 ?  2   MET   B H    1 
ATOM   4052 H HA   A MET   B 1 2   ? 49.089 -13.569 -22.320 0.42 32.15 ?  2   MET   B HA   1 
ATOM   4053 H HA   B MET   B 1 2   ? 49.106 -13.603 -22.319 0.58 28.81 ?  2   MET   B HA   1 
ATOM   4054 H HB2  A MET   B 1 2   ? 50.934 -14.635 -23.356 0.42 35.68 ?  2   MET   B HB2  1 
ATOM   4055 H HB2  B MET   B 1 2   ? 51.134 -14.500 -23.150 0.58 32.13 ?  2   MET   B HB2  1 
ATOM   4056 H HB3  A MET   B 1 2   ? 51.398 -15.140 -21.929 0.42 35.68 ?  2   MET   B HB3  1 
ATOM   4057 H HB3  B MET   B 1 2   ? 51.331 -15.223 -21.763 0.58 32.13 ?  2   MET   B HB3  1 
ATOM   4058 H HG2  A MET   B 1 2   ? 49.566 -16.480 -21.718 0.42 39.01 ?  2   MET   B HG2  1 
ATOM   4059 H HG2  B MET   B 1 2   ? 49.560 -16.577 -22.008 0.58 34.53 ?  2   MET   B HG2  1 
ATOM   4060 H HG3  A MET   B 1 2   ? 48.950 -15.914 -23.074 0.42 39.01 ?  2   MET   B HG3  1 
ATOM   4061 H HG3  B MET   B 1 2   ? 49.010 -15.749 -23.253 0.58 34.53 ?  2   MET   B HG3  1 
ATOM   4062 H HE1  A MET   B 1 2   ? 51.361 -17.082 -25.669 0.42 41.79 ?  2   MET   B HE1  1 
ATOM   4063 H HE1  B MET   B 1 2   ? 52.087 -16.371 -25.498 0.58 37.48 ?  2   MET   B HE1  1 
ATOM   4064 H HE2  A MET   B 1 2   ? 50.495 -15.843 -25.183 0.42 41.79 ?  2   MET   B HE2  1 
ATOM   4065 H HE2  B MET   B 1 2   ? 51.186 -15.182 -25.019 0.58 37.48 ?  2   MET   B HE2  1 
ATOM   4066 H HE3  A MET   B 1 2   ? 51.997 -16.009 -24.688 0.42 41.79 ?  2   MET   B HE3  1 
ATOM   4067 H HE3  B MET   B 1 2   ? 52.453 -15.662 -24.147 0.58 37.48 ?  2   MET   B HE3  1 
ATOM   4068 N N    . VAL   B 1 3   ? 48.431 -13.723 -19.948 1.00 21.76 ?  3   VAL   B N    1 
ATOM   4069 C CA   . VAL   B 1 3   ? 48.020 -13.960 -18.574 1.00 20.85 ?  3   VAL   B CA   1 
ATOM   4070 C C    . VAL   B 1 3   ? 46.787 -14.852 -18.597 1.00 19.10 ?  3   VAL   B C    1 
ATOM   4071 O O    . VAL   B 1 3   ? 46.062 -14.927 -19.591 1.00 19.56 ?  3   VAL   B O    1 
ATOM   4072 C CB   . VAL   B 1 3   ? 47.742 -12.651 -17.800 1.00 22.85 ?  3   VAL   B CB   1 
ATOM   4073 C CG1  . VAL   B 1 3   ? 49.019 -11.806 -17.679 1.00 23.66 ?  3   VAL   B CG1  1 
ATOM   4074 C CG2  . VAL   B 1 3   ? 46.624 -11.863 -18.466 1.00 23.42 ?  3   VAL   B CG2  1 
ATOM   4075 H H    A VAL   B 1 3   ? 47.792 -13.461 -20.461 0.42 26.12 ?  3   VAL   B H    1 
ATOM   4076 H H    B VAL   B 1 3   ? 47.789 -13.484 -20.469 0.58 26.12 ?  3   VAL   B H    1 
ATOM   4077 H HA   . VAL   B 1 3   ? 48.727 -14.436 -18.109 1.00 25.01 ?  3   VAL   B HA   1 
ATOM   4078 H HB   . VAL   B 1 3   ? 47.457 -12.878 -16.903 1.00 27.42 ?  3   VAL   B HB   1 
ATOM   4079 H HG11 . VAL   B 1 3   ? 48.815 -10.996 -17.184 1.00 28.39 ?  3   VAL   B HG11 1 
ATOM   4080 H HG12 . VAL   B 1 3   ? 49.695 -12.318 -17.207 1.00 28.39 ?  3   VAL   B HG12 1 
ATOM   4081 H HG13 . VAL   B 1 3   ? 49.335 -11.580 -18.567 1.00 28.39 ?  3   VAL   B HG13 1 
ATOM   4082 H HG21 . VAL   B 1 3   ? 46.558 -10.992 -18.048 1.00 28.10 ?  3   VAL   B HG21 1 
ATOM   4083 H HG22 . VAL   B 1 3   ? 46.821 -11.765 -19.410 1.00 28.10 ?  3   VAL   B HG22 1 
ATOM   4084 H HG23 . VAL   B 1 3   ? 45.787 -12.346 -18.353 1.00 28.10 ?  3   VAL   B HG23 1 
ATOM   4085 N N    . ASN   B 1 4   ? 46.564 -15.544 -17.484 1.00 16.84 ?  4   ASN   B N    1 
ATOM   4086 C CA   . ASN   B 1 4   ? 45.419 -16.444 -17.362 1.00 15.45 ?  4   ASN   B CA   1 
ATOM   4087 C C    . ASN   B 1 4   ? 45.359 -17.415 -18.539 1.00 15.83 ?  4   ASN   B C    1 
ATOM   4088 O O    . ASN   B 1 4   ? 44.301 -17.666 -19.110 1.00 16.86 ?  4   ASN   B O    1 
ATOM   4089 C CB   . ASN   B 1 4   ? 44.113 -15.661 -17.211 1.00 14.96 ?  4   ASN   B CB   1 
ATOM   4090 C CG   . ASN   B 1 4   ? 44.063 -14.863 -15.915 1.00 14.38 ?  4   ASN   B CG   1 
ATOM   4091 O OD1  . ASN   B 1 4   ? 44.357 -15.382 -14.839 1.00 13.98 ?  4   ASN   B OD1  1 
ATOM   4092 N ND2  . ASN   B 1 4   ? 43.699 -13.590 -16.019 1.00 15.26 ?  4   ASN   B ND2  1 
ATOM   4093 H H    . ASN   B 1 4   ? 47.068 -15.518 -16.789 1.00 20.21 ?  4   ASN   B H    1 
ATOM   4094 H HA   . ASN   B 1 4   ? 45.536 -16.971 -16.557 1.00 18.54 ?  4   ASN   B HA   1 
ATOM   4095 H HB2  . ASN   B 1 4   ? 44.028 -15.038 -17.951 1.00 17.95 ?  4   ASN   B HB2  1 
ATOM   4096 H HB3  . ASN   B 1 4   ? 43.369 -16.282 -17.212 1.00 17.95 ?  4   ASN   B HB3  1 
ATOM   4097 H HD21 . ASN   B 1 4   ? 43.653 -13.094 -15.315 1.00 18.31 ?  4   ASN   B HD21 1 
ATOM   4098 H HD22 . ASN   B 1 4   ? 43.500 -13.255 -16.788 1.00 18.31 ?  4   ASN   B HD22 1 
ATOM   4099 N N    . SER   B 1 5   ? 46.515 -17.964 -18.910 1.00 16.36 ?  5   SER   B N    1 
ATOM   4100 C CA   . SER   B 1 5   ? 46.610 -18.881 -20.045 1.00 18.64 ?  5   SER   B CA   1 
ATOM   4101 C C    . SER   B 1 5   ? 46.582 -20.309 -19.513 1.00 20.79 ?  5   SER   B C    1 
ATOM   4102 O O    . SER   B 1 5   ? 47.594 -20.997 -19.430 1.00 22.98 ?  5   SER   B O    1 
ATOM   4103 C CB   . SER   B 1 5   ? 47.876 -18.604 -20.857 1.00 20.83 ?  5   SER   B CB   1 
ATOM   4104 O OG   . SER   B 1 5   ? 49.046 -18.789 -20.076 1.00 24.59 ?  5   SER   B OG   1 
ATOM   4105 H H    . SER   B 1 5   ? 47.265 -17.834 -18.510 1.00 19.63 ?  5   SER   B H    1 
ATOM   4106 H HA   . SER   B 1 5   ? 45.843 -18.760 -20.626 1.00 22.36 ?  5   SER   B HA   1 
ATOM   4107 H HB2  . SER   B 1 5   ? 47.899 -19.214 -21.618 1.00 25.00 ?  5   SER   B HB2  1 
ATOM   4108 H HB3  . SER   B 1 5   ? 47.838 -17.690 -21.175 1.00 25.00 ?  5   SER   B HB3  1 
ATOM   4109 H HG   . SER   B 1 5   ? 49.088 -19.586 -19.817 1.00 29.51 ?  5   SER   B HG   1 
ATOM   4110 N N    . PHE   B 1 6   ? 45.386 -20.724 -19.106 1.00 21.54 ?  6   PHE   B N    1 
ATOM   4111 C CA   . PHE   B 1 6   ? 45.179 -22.064 -18.582 1.00 20.78 ?  6   PHE   B CA   1 
ATOM   4112 C C    . PHE   B 1 6   ? 45.085 -23.039 -19.745 1.00 24.08 ?  6   PHE   B C    1 
ATOM   4113 O O    . PHE   B 1 6   ? 44.399 -22.765 -20.734 1.00 26.24 ?  6   PHE   B O    1 
ATOM   4114 C CB   . PHE   B 1 6   ? 43.894 -22.110 -17.755 1.00 19.31 ?  6   PHE   B CB   1 
ATOM   4115 C CG   . PHE   B 1 6   ? 43.930 -21.251 -16.521 1.00 17.44 ?  6   PHE   B CG   1 
ATOM   4116 C CD1  . PHE   B 1 6   ? 44.434 -21.744 -15.333 1.00 15.91 ?  6   PHE   B CD1  1 
ATOM   4117 C CD2  . PHE   B 1 6   ? 43.461 -19.946 -16.555 1.00 16.90 ?  6   PHE   B CD2  1 
ATOM   4118 C CE1  . PHE   B 1 6   ? 44.462 -20.957 -14.194 1.00 15.52 ?  6   PHE   B CE1  1 
ATOM   4119 C CE2  . PHE   B 1 6   ? 43.490 -19.151 -15.425 1.00 17.20 ?  6   PHE   B CE2  1 
ATOM   4120 C CZ   . PHE   B 1 6   ? 43.996 -19.649 -14.246 1.00 16.27 ?  6   PHE   B CZ   1 
ATOM   4121 H H    . PHE   B 1 6   ? 44.666 -20.254 -19.137 1.00 25.85 ?  6   PHE   B H    1 
ATOM   4122 H HA   . PHE   B 1 6   ? 45.922 -22.324 -18.018 1.00 24.93 ?  6   PHE   B HA   1 
ATOM   4123 H HB2  . PHE   B 1 6   ? 43.154 -21.804 -18.304 1.00 23.18 ?  6   PHE   B HB2  1 
ATOM   4124 H HB3  . PHE   B 1 6   ? 43.731 -23.025 -17.470 1.00 23.18 ?  6   PHE   B HB3  1 
ATOM   4125 H HD1  . PHE   B 1 6   ? 44.757 -22.616 -15.295 1.00 19.09 ?  6   PHE   B HD1  1 
ATOM   4126 H HD2  . PHE   B 1 6   ? 43.116 -19.606 -17.347 1.00 20.28 ?  6   PHE   B HD2  1 
ATOM   4127 H HE1  . PHE   B 1 6   ? 44.812 -21.293 -13.399 1.00 18.62 ?  6   PHE   B HE1  1 
ATOM   4128 H HE2  . PHE   B 1 6   ? 43.167 -18.278 -15.461 1.00 20.63 ?  6   PHE   B HE2  1 
ATOM   4129 H HZ   . PHE   B 1 6   ? 44.016 -19.119 -13.481 1.00 19.52 ?  6   PHE   B HZ   1 
ATOM   4130 N N    . SER   B 1 7   ? 45.793 -24.162 -19.636 1.00 24.75 ?  7   SER   B N    1 
ATOM   4131 C CA   . SER   B 1 7   ? 45.847 -25.145 -20.708 1.00 28.06 ?  7   SER   B CA   1 
ATOM   4132 C C    . SER   B 1 7   ? 45.776 -26.549 -20.131 1.00 27.62 ?  7   SER   B C    1 
ATOM   4133 O O    . SER   B 1 7   ? 46.383 -26.840 -19.097 1.00 28.81 ?  7   SER   B O    1 
ATOM   4134 C CB   . SER   B 1 7   ? 47.134 -24.989 -21.531 1.00 30.20 ?  7   SER   B CB   1 
ATOM   4135 O OG   . SER   B 1 7   ? 47.109 -25.825 -22.676 1.00 33.05 ?  7   SER   B OG   1 
ATOM   4136 H H    . SER   B 1 7   ? 46.268 -24.373 -18.945 1.00 29.70 ?  7   SER   B H    1 
ATOM   4137 H HA   . SER   B 1 7   ? 45.093 -25.023 -21.298 1.00 33.67 ?  7   SER   B HA   1 
ATOM   4138 H HB2  . SER   B 1 7   ? 47.217 -24.064 -21.816 1.00 36.23 ?  7   SER   B HB2  1 
ATOM   4139 H HB3  . SER   B 1 7   ? 47.896 -25.233 -20.982 1.00 36.23 ?  7   SER   B HB3  1 
ATOM   4140 H HG   . SER   B 1 7   ? 47.816 -25.726 -23.120 1.00 39.66 ?  7   SER   B HG   1 
ATOM   4141 N N    . GLY   B 1 8   ? 45.029 -27.417 -20.809 1.00 27.49 ?  8   GLY   B N    1 
ATOM   4142 C CA   . GLY   B 1 8   ? 44.984 -28.812 -20.438 1.00 26.98 ?  8   GLY   B CA   1 
ATOM   4143 C C    . GLY   B 1 8   ? 44.065 -29.138 -19.290 1.00 25.38 ?  8   GLY   B C    1 
ATOM   4144 O O    . GLY   B 1 8   ? 44.222 -30.200 -18.672 1.00 27.11 ?  8   GLY   B O    1 
ATOM   4145 H H    . GLY   B 1 8   ? 44.546 -27.211 -21.485 1.00 32.99 ?  8   GLY   B H    1 
ATOM   4146 H HA2  . GLY   B 1 8   ? 44.689 -29.329 -21.201 1.00 32.38 ?  8   GLY   B HA2  1 
ATOM   4147 H HA3  . GLY   B 1 8   ? 45.871 -29.106 -20.194 1.00 32.38 ?  8   GLY   B HA3  1 
ATOM   4148 N N    . TYR   B 1 9   ? 43.086 -28.286 -18.998 1.00 22.75 ?  9   TYR   B N    1 
ATOM   4149 C CA   . TYR   B 1 9   ? 42.149 -28.564 -17.924 1.00 20.94 ?  9   TYR   B CA   1 
ATOM   4150 C C    . TYR   B 1 9   ? 40.962 -29.360 -18.428 1.00 20.53 ?  9   TYR   B C    1 
ATOM   4151 O O    . TYR   B 1 9   ? 40.531 -29.226 -19.578 1.00 22.28 ?  9   TYR   B O    1 
ATOM   4152 C CB   . TYR   B 1 9   ? 41.642 -27.282 -17.263 1.00 20.28 ?  9   TYR   B CB   1 
ATOM   4153 C CG   . TYR   B 1 9   ? 42.676 -26.660 -16.362 1.00 19.73 ?  9   TYR   B CG   1 
ATOM   4154 C CD1  . TYR   B 1 9   ? 43.747 -25.963 -16.895 1.00 20.10 ?  9   TYR   B CD1  1 
ATOM   4155 C CD2  . TYR   B 1 9   ? 42.602 -26.792 -14.981 1.00 18.87 ?  9   TYR   B CD2  1 
ATOM   4156 C CE1  . TYR   B 1 9   ? 44.714 -25.408 -16.084 1.00 19.83 ?  9   TYR   B CE1  1 
ATOM   4157 C CE2  . TYR   B 1 9   ? 43.568 -26.236 -14.158 1.00 19.04 ?  9   TYR   B CE2  1 
ATOM   4158 C CZ   . TYR   B 1 9   ? 44.623 -25.542 -14.719 1.00 19.50 ?  9   TYR   B CZ   1 
ATOM   4159 O OH   . TYR   B 1 9   ? 45.592 -24.991 -13.917 1.00 20.49 ?  9   TYR   B OH   1 
ATOM   4160 H H    . TYR   B 1 9   ? 42.923 -27.554 -19.421 1.00 27.30 ?  9   TYR   B H    1 
ATOM   4161 H HA   . TYR   B 1 9   ? 42.585 -29.092 -17.243 1.00 25.13 ?  9   TYR   B HA   1 
ATOM   4162 H HB2  . TYR   B 1 9   ? 41.398 -26.632 -17.944 1.00 24.34 ?  9   TYR   B HB2  1 
ATOM   4163 H HB3  . TYR   B 1 9   ? 40.872 -27.502 -16.721 1.00 24.34 ?  9   TYR   B HB3  1 
ATOM   4164 H HD1  . TYR   B 1 9   ? 43.811 -25.869 -17.819 1.00 24.12 ?  9   TYR   B HD1  1 
ATOM   4165 H HD2  . TYR   B 1 9   ? 41.886 -27.265 -14.604 1.00 22.65 ?  9   TYR   B HD2  1 
ATOM   4166 H HE1  . TYR   B 1 9   ? 45.417 -24.940 -16.460 1.00 23.79 ?  9   TYR   B HE1  1 
ATOM   4167 H HE2  . TYR   B 1 9   ? 43.497 -26.335 -13.233 1.00 22.85 ?  9   TYR   B HE2  1 
ATOM   4168 H HH   . TYR   B 1 9   ? 46.156 -24.597 -14.394 1.00 24.59 ?  9   TYR   B HH   1 
ATOM   4169 N N    . LEU   B 1 10  ? 40.449 -30.208 -17.547 1.00 18.70 ?  10  LEU   B N    1 
ATOM   4170 C CA   . LEU   B 1 10  ? 39.242 -30.971 -17.799 1.00 18.15 ?  10  LEU   B CA   1 
ATOM   4171 C C    . LEU   B 1 10  ? 38.063 -30.198 -17.228 1.00 18.24 ?  10  LEU   B C    1 
ATOM   4172 O O    . LEU   B 1 10  ? 38.096 -29.774 -16.070 1.00 17.94 ?  10  LEU   B O    1 
ATOM   4173 C CB   . LEU   B 1 10  ? 39.348 -32.334 -17.115 1.00 19.12 ?  10  LEU   B CB   1 
ATOM   4174 C CG   . LEU   B 1 10  ? 38.214 -33.304 -17.432 1.00 21.06 ?  10  LEU   B CG   1 
ATOM   4175 C CD1  . LEU   B 1 10  ? 38.385 -33.862 -18.837 1.00 21.91 ?  10  LEU   B CD1  1 
ATOM   4176 C CD2  . LEU   B 1 10  ? 38.130 -34.422 -16.405 1.00 22.15 ?  10  LEU   B CD2  1 
ATOM   4177 H H    . LEU   B 1 10  ? 40.780 -30.357 -16.763 1.00 22.44 ?  10  LEU   B H    1 
ATOM   4178 H HA   . LEU   B 1 10  ? 39.109 -31.099 -18.749 1.00 21.77 ?  10  LEU   B HA   1 
ATOM   4179 H HB2  . LEU   B 1 10  ? 40.178 -32.752 -17.392 1.00 22.95 ?  10  LEU   B HB2  1 
ATOM   4180 H HB3  . LEU   B 1 10  ? 39.358 -32.200 -16.153 1.00 22.95 ?  10  LEU   B HB3  1 
ATOM   4181 H HG   . LEU   B 1 10  ? 37.373 -32.822 -17.408 1.00 25.27 ?  10  LEU   B HG   1 
ATOM   4182 H HD11 . LEU   B 1 10  ? 37.677 -34.502 -19.009 1.00 26.29 ?  10  LEU   B HD11 1 
ATOM   4183 H HD12 . LEU   B 1 10  ? 38.332 -33.132 -19.473 1.00 26.29 ?  10  LEU   B HD12 1 
ATOM   4184 H HD13 . LEU   B 1 10  ? 39.248 -34.297 -18.900 1.00 26.29 ?  10  LEU   B HD13 1 
ATOM   4185 H HD21 . LEU   B 1 10  ? 37.400 -35.012 -16.646 1.00 26.58 ?  10  LEU   B HD21 1 
ATOM   4186 H HD22 . LEU   B 1 10  ? 38.966 -34.907 -16.400 1.00 26.58 ?  10  LEU   B HD22 1 
ATOM   4187 H HD23 . LEU   B 1 10  ? 37.965 -34.030 -15.532 1.00 26.58 ?  10  LEU   B HD23 1 
ATOM   4188 N N    . LYS   B 1 11  ? 37.032 -30.015 -18.044 1.00 19.31 ?  11  LYS   B N    1 
ATOM   4189 C CA   . LYS   B 1 11  ? 35.833 -29.305 -17.624 1.00 21.43 ?  11  LYS   B CA   1 
ATOM   4190 C C    . LYS   B 1 11  ? 34.976 -30.232 -16.768 1.00 20.57 ?  11  LYS   B C    1 
ATOM   4191 O O    . LYS   B 1 11  ? 34.604 -31.325 -17.209 1.00 22.28 ?  11  LYS   B O    1 
ATOM   4192 C CB   . LYS   B 1 11  ? 35.068 -28.861 -18.870 1.00 25.77 ?  11  LYS   B CB   1 
ATOM   4193 C CG   . LYS   B 1 11  ? 33.926 -27.892 -18.631 1.00 29.82 ?  11  LYS   B CG   1 
ATOM   4194 C CD   . LYS   B 1 11  ? 33.221 -27.574 -19.947 1.00 32.79 ?  11  LYS   B CD   1 
ATOM   4195 C CE   . LYS   B 1 11  ? 32.236 -26.427 -19.803 1.00 34.81 ?  11  LYS   B CE   1 
ATOM   4196 N NZ   . LYS   B 1 11  ? 32.924 -25.120 -19.609 1.00 36.19 ?  11  LYS   B NZ   1 
ATOM   4197 H H    . LYS   B 1 11  ? 36.995 -30.300 -18.860 1.00 23.17 ?  11  LYS   B H    1 
ATOM   4198 H HA   . LYS   B 1 11  ? 36.074 -28.522 -17.105 1.00 25.71 ?  11  LYS   B HA   1 
ATOM   4199 H HB2  . LYS   B 1 11  ? 35.691 -28.424 -19.475 1.00 30.92 ?  11  LYS   B HB2  1 
ATOM   4200 H HB3  . LYS   B 1 11  ? 34.695 -29.644 -19.302 1.00 30.92 ?  11  LYS   B HB3  1 
ATOM   4201 H HG2  . LYS   B 1 11  ? 33.283 -28.293 -18.028 1.00 35.78 ?  11  LYS   B HG2  1 
ATOM   4202 H HG3  . LYS   B 1 11  ? 34.273 -27.066 -18.262 1.00 35.78 ?  11  LYS   B HG3  1 
ATOM   4203 H HD2  . LYS   B 1 11  ? 33.884 -27.324 -20.610 1.00 39.35 ?  11  LYS   B HD2  1 
ATOM   4204 H HD3  . LYS   B 1 11  ? 32.732 -28.358 -20.243 1.00 39.35 ?  11  LYS   B HD3  1 
ATOM   4205 H HE2  . LYS   B 1 11  ? 31.695 -26.366 -20.606 1.00 41.77 ?  11  LYS   B HE2  1 
ATOM   4206 H HE3  . LYS   B 1 11  ? 31.671 -26.595 -19.033 1.00 41.77 ?  11  LYS   B HE3  1 
ATOM   4207 H HZ1  . LYS   B 1 11  ? 32.323 -24.467 -19.535 1.00 43.43 ?  11  LYS   B HZ1  1 
ATOM   4208 H HZ2  . LYS   B 1 11  ? 33.420 -25.144 -18.871 1.00 43.43 ?  11  LYS   B HZ2  1 
ATOM   4209 H HZ3  . LYS   B 1 11  ? 33.451 -24.949 -20.307 1.00 43.43 ?  11  LYS   B HZ3  1 
ATOM   4210 N N    . LEU   B 1 12  ? 34.662 -29.805 -15.544 1.00 18.79 ?  12  LEU   B N    1 
ATOM   4211 C CA   . LEU   B 1 12  ? 33.698 -30.513 -14.707 1.00 18.16 ?  12  LEU   B CA   1 
ATOM   4212 C C    . LEU   B 1 12  ? 32.311 -29.901 -14.802 1.00 17.89 ?  12  LEU   B C    1 
ATOM   4213 O O    . LEU   B 1 12  ? 31.325 -30.612 -14.987 1.00 18.67 ?  12  LEU   B O    1 
ATOM   4214 C CB   . LEU   B 1 12  ? 34.153 -30.542 -13.242 1.00 17.87 ?  12  LEU   B CB   1 
ATOM   4215 C CG   . LEU   B 1 12  ? 35.498 -31.215 -12.970 1.00 17.74 ?  12  LEU   B CG   1 
ATOM   4216 C CD1  . LEU   B 1 12  ? 35.862 -31.136 -11.499 1.00 17.92 ?  12  LEU   B CD1  1 
ATOM   4217 C CD2  . LEU   B 1 12  ? 35.493 -32.667 -13.431 1.00 18.02 ?  12  LEU   B CD2  1 
ATOM   4218 H H    . LEU   B 1 12  ? 34.988 -29.099 -15.176 1.00 22.55 ?  12  LEU   B H    1 
ATOM   4219 H HA   . LEU   B 1 12  ? 33.624 -31.427 -15.016 1.00 21.80 ?  12  LEU   B HA   1 
ATOM   4220 H HB2  . LEU   B 1 12  ? 34.209 -29.635 -12.920 1.00 21.45 ?  12  LEU   B HB2  1 
ATOM   4221 H HB3  . LEU   B 1 12  ? 33.480 -31.027 -12.728 1.00 21.45 ?  12  LEU   B HB3  1 
ATOM   4222 H HG   . LEU   B 1 12  ? 36.183 -30.750 -13.473 1.00 21.28 ?  12  LEU   B HG   1 
ATOM   4223 H HD11 . LEU   B 1 12  ? 36.723 -31.568 -11.363 1.00 21.50 ?  12  LEU   B HD11 1 
ATOM   4224 H HD12 . LEU   B 1 12  ? 35.916 -30.206 -11.234 1.00 21.50 ?  12  LEU   B HD12 1 
ATOM   4225 H HD13 . LEU   B 1 12  ? 35.182 -31.591 -10.977 1.00 21.50 ?  12  LEU   B HD13 1 
ATOM   4226 H HD21 . LEU   B 1 12  ? 36.315 -33.094 -13.145 1.00 21.62 ?  12  LEU   B HD21 1 
ATOM   4227 H HD22 . LEU   B 1 12  ? 34.731 -33.123 -13.035 1.00 21.62 ?  12  LEU   B HD22 1 
ATOM   4228 H HD23 . LEU   B 1 12  ? 35.424 -32.696 -14.398 1.00 21.62 ?  12  LEU   B HD23 1 
ATOM   4229 N N    . THR   B 1 13  ? 32.225 -28.584 -14.679 1.00 17.69 ?  13  THR   B N    1 
ATOM   4230 C CA   . THR   B 1 13  ? 31.007 -27.828 -14.901 1.00 17.56 ?  13  THR   B CA   1 
ATOM   4231 C C    . THR   B 1 13  ? 31.359 -26.642 -15.792 1.00 19.83 ?  13  THR   B C    1 
ATOM   4232 O O    . THR   B 1 13  ? 32.511 -26.462 -16.202 1.00 20.92 ?  13  THR   B O    1 
ATOM   4233 C CB   . THR   B 1 13  ? 30.402 -27.337 -13.581 1.00 17.32 ?  13  THR   B CB   1 
ATOM   4234 O OG1  . THR   B 1 13  ? 31.242 -26.311 -13.042 1.00 16.84 ?  13  THR   B OG1  1 
ATOM   4235 C CG2  . THR   B 1 13  ? 30.283 -28.475 -12.580 1.00 17.96 ?  13  THR   B CG2  1 
ATOM   4236 H H    . THR   B 1 13  ? 32.888 -28.087 -14.458 1.00 21.23 ?  13  THR   B H    1 
ATOM   4237 H HA   . THR   B 1 13  ? 30.349 -28.381 -15.353 1.00 21.07 ?  13  THR   B HA   1 
ATOM   4238 H HB   . THR   B 1 13  ? 29.512 -26.975 -13.746 1.00 20.78 ?  13  THR   B HB   1 
ATOM   4239 H HG1  . THR   B 1 13  ? 30.931 -25.548 -13.244 1.00 20.21 ?  13  THR   B HG1  1 
ATOM   4240 H HG21 . THR   B 1 13  ? 29.778 -28.186 -11.804 1.00 21.56 ?  13  THR   B HG21 1 
ATOM   4241 H HG22 . THR   B 1 13  ? 29.828 -29.229 -12.988 1.00 21.56 ?  13  THR   B HG22 1 
ATOM   4242 H HG23 . THR   B 1 13  ? 31.166 -28.759 -12.295 1.00 21.56 ?  13  THR   B HG23 1 
ATOM   4243 N N    A ASP   B 1 14  ? 30.357 -25.807 -16.067 0.42 20.83 ?  14  ASP   B N    1 
ATOM   4244 N N    B ASP   B 1 14  ? 30.359 -25.812 -16.086 0.58 20.80 ?  14  ASP   B N    1 
ATOM   4245 C CA   A ASP   B 1 14  ? 30.581 -24.658 -16.936 0.42 22.09 ?  14  ASP   B CA   1 
ATOM   4246 C CA   B ASP   B 1 14  ? 30.597 -24.662 -16.952 0.58 22.27 ?  14  ASP   B CA   1 
ATOM   4247 C C    A ASP   B 1 14  ? 31.672 -23.741 -16.397 0.42 20.31 ?  14  ASP   B C    1 
ATOM   4248 C C    B ASP   B 1 14  ? 31.637 -23.702 -16.391 0.58 20.42 ?  14  ASP   B C    1 
ATOM   4249 O O    A ASP   B 1 14  ? 32.338 -23.055 -17.180 0.42 21.48 ?  14  ASP   B O    1 
ATOM   4250 O O    B ASP   B 1 14  ? 32.210 -22.925 -17.160 0.58 22.00 ?  14  ASP   B O    1 
ATOM   4251 C CB   A ASP   B 1 14  ? 29.278 -23.882 -17.138 0.42 24.98 ?  14  ASP   B CB   1 
ATOM   4252 C CB   B ASP   B 1 14  ? 29.297 -23.904 -17.218 0.58 25.49 ?  14  ASP   B CB   1 
ATOM   4253 C CG   A ASP   B 1 14  ? 28.286 -24.614 -18.021 0.42 27.84 ?  14  ASP   B CG   1 
ATOM   4254 C CG   B ASP   B 1 14  ? 28.428 -24.588 -18.255 0.58 28.81 ?  14  ASP   B CG   1 
ATOM   4255 O OD1  A ASP   B 1 14  ? 28.629 -25.680 -18.579 0.42 28.31 ?  14  ASP   B OD1  1 
ATOM   4256 O OD1  B ASP   B 1 14  ? 28.979 -25.310 -19.114 0.58 29.83 ?  14  ASP   B OD1  1 
ATOM   4257 O OD2  A ASP   B 1 14  ? 27.149 -24.116 -18.151 0.42 29.59 -1 14  ASP   B OD2  1 
ATOM   4258 O OD2  B ASP   B 1 14  ? 27.194 -24.407 -18.212 0.58 30.64 -1 14  ASP   B OD2  1 
ATOM   4259 H H    A ASP   B 1 14  ? 29.559 -25.872 -15.759 0.42 25.00 ?  14  ASP   B H    1 
ATOM   4260 H H    B ASP   B 1 14  ? 29.554 -25.885 -15.798 0.58 24.95 ?  14  ASP   B H    1 
ATOM   4261 H HA   A ASP   B 1 14  ? 30.880 -24.965 -17.800 0.42 26.50 ?  14  ASP   B HA   1 
ATOM   4262 H HA   B ASP   B 1 14  ? 30.932 -24.976 -17.803 0.58 26.72 ?  14  ASP   B HA   1 
ATOM   4263 H HB2  A ASP   B 1 14  ? 28.844 -23.755 -16.284 0.42 29.98 ?  14  ASP   B HB2  1 
ATOM   4264 H HB2  B ASP   B 1 14  ? 28.792 -23.844 -16.393 0.58 30.59 ?  14  ASP   B HB2  1 
ATOM   4265 H HB3  A ASP   B 1 14  ? 29.475 -23.024 -17.547 0.42 29.98 ?  14  ASP   B HB3  1 
ATOM   4266 H HB3  B ASP   B 1 14  ? 29.512 -23.012 -17.540 0.58 30.59 ?  14  ASP   B HB3  1 
ATOM   4267 N N    . ASN   B 1 15  ? 31.885 -23.722 -15.077 1.00 18.24 ?  15  ASN   B N    1 
ATOM   4268 C CA   . ASN   B 1 15  ? 32.847 -22.803 -14.470 1.00 16.12 ?  15  ASN   B CA   1 
ATOM   4269 C C    . ASN   B 1 15  ? 33.939 -23.461 -13.636 1.00 14.50 ?  15  ASN   B C    1 
ATOM   4270 O O    . ASN   B 1 15  ? 34.800 -22.746 -13.119 1.00 14.52 ?  15  ASN   B O    1 
ATOM   4271 C CB   . ASN   B 1 15  ? 32.135 -21.750 -13.605 1.00 16.17 ?  15  ASN   B CB   1 
ATOM   4272 C CG   . ASN   B 1 15  ? 31.513 -22.350 -12.363 1.00 15.90 ?  15  ASN   B CG   1 
ATOM   4273 O OD1  . ASN   B 1 15  ? 30.568 -23.147 -12.447 1.00 17.47 ?  15  ASN   B OD1  1 
ATOM   4274 N ND2  . ASN   B 1 15  ? 32.042 -21.997 -11.204 1.00 14.74 ?  15  ASN   B ND2  1 
ATOM   4275 H H    A ASN   B 1 15  ? 31.480 -24.231 -14.511 0.42 21.89 ?  15  ASN   B H    1 
ATOM   4276 H H    B ASN   B 1 15  ? 31.490 -24.241 -14.513 0.58 21.89 ?  15  ASN   B H    1 
ATOM   4277 H HA   . ASN   B 1 15  ? 33.293 -22.317 -15.173 1.00 19.34 ?  15  ASN   B HA   1 
ATOM   4278 H HB2  . ASN   B 1 15  ? 32.780 -21.073 -13.325 1.00 19.40 ?  15  ASN   B HB2  1 
ATOM   4279 H HB3  . ASN   B 1 15  ? 31.428 -21.325 -14.123 1.00 19.40 ?  15  ASN   B HB3  1 
ATOM   4280 H HD21 . ASN   B 1 15  ? 31.724 -22.314 -10.468 1.00 17.69 ?  15  ASN   B HD21 1 
ATOM   4281 H HD22 . ASN   B 1 15  ? 32.709 -21.448 -11.174 1.00 17.69 ?  15  ASN   B HD22 1 
ATOM   4282 N N    . VAL   B 1 16  ? 33.937 -24.781 -13.480 1.00 14.32 ?  16  VAL   B N    1 
ATOM   4283 C CA   . VAL   B 1 16  ? 34.931 -25.473 -12.667 1.00 13.99 ?  16  VAL   B CA   1 
ATOM   4284 C C    . VAL   B 1 16  ? 35.722 -26.413 -13.561 1.00 13.99 ?  16  VAL   B C    1 
ATOM   4285 O O    . VAL   B 1 16  ? 35.142 -27.293 -14.218 1.00 14.96 ?  16  VAL   B O    1 
ATOM   4286 C CB   . VAL   B 1 16  ? 34.299 -26.233 -11.492 1.00 14.04 ?  16  VAL   B CB   1 
ATOM   4287 C CG1  . VAL   B 1 16  ? 35.374 -26.977 -10.699 1.00 14.45 ?  16  VAL   B CG1  1 
ATOM   4288 C CG2  . VAL   B 1 16  ? 33.509 -25.285 -10.596 1.00 14.91 ?  16  VAL   B CG2  1 
ATOM   4289 H H    . VAL   B 1 16  ? 33.348 -25.304 -13.834 1.00 17.18 ?  16  VAL   B H    1 
ATOM   4290 H HA   . VAL   B 1 16  ? 35.546 -24.822 -12.302 1.00 16.78 ?  16  VAL   B HA   1 
ATOM   4291 H HB   . VAL   B 1 16  ? 33.679 -26.895 -11.841 1.00 16.85 ?  16  VAL   B HB   1 
ATOM   4292 H HG11 . VAL   B 1 16  ? 34.994 -27.268 -9.855  1.00 17.34 ?  16  VAL   B HG11 1 
ATOM   4293 H HG12 . VAL   B 1 16  ? 35.673 -27.742 -11.210 1.00 17.34 ?  16  VAL   B HG12 1 
ATOM   4294 H HG13 . VAL   B 1 16  ? 36.114 -26.371 -10.535 1.00 17.34 ?  16  VAL   B HG13 1 
ATOM   4295 H HG21 . VAL   B 1 16  ? 33.161 -25.782 -9.839  1.00 17.89 ?  16  VAL   B HG21 1 
ATOM   4296 H HG22 . VAL   B 1 16  ? 34.097 -24.580 -10.287 1.00 17.89 ?  16  VAL   B HG22 1 
ATOM   4297 H HG23 . VAL   B 1 16  ? 32.776 -24.905 -11.106 1.00 17.89 ?  16  VAL   B HG23 1 
ATOM   4298 N N    . TYR   B 1 17  ? 37.043 -26.244 -13.548 1.00 14.16 ?  17  TYR   B N    1 
ATOM   4299 C CA   . TYR   B 1 17  ? 37.986 -26.996 -14.360 1.00 14.78 ?  17  TYR   B CA   1 
ATOM   4300 C C    . TYR   B 1 17  ? 39.039 -27.610 -13.445 1.00 13.87 ?  17  TYR   B C    1 
ATOM   4301 O O    . TYR   B 1 17  ? 39.312 -27.090 -12.362 1.00 13.74 ?  17  TYR   B O    1 
ATOM   4302 C CB   . TYR   B 1 17  ? 38.695 -26.076 -15.370 1.00 17.79 ?  17  TYR   B CB   1 
ATOM   4303 C CG   . TYR   B 1 17  ? 37.763 -25.312 -16.278 1.00 21.34 ?  17  TYR   B CG   1 
ATOM   4304 C CD1  . TYR   B 1 17  ? 37.198 -24.110 -15.878 1.00 23.05 ?  17  TYR   B CD1  1 
ATOM   4305 C CD2  . TYR   B 1 17  ? 37.447 -25.797 -17.540 1.00 23.50 ?  17  TYR   B CD2  1 
ATOM   4306 C CE1  . TYR   B 1 17  ? 36.340 -23.407 -16.711 1.00 24.83 ?  17  TYR   B CE1  1 
ATOM   4307 C CE2  . TYR   B 1 17  ? 36.596 -25.104 -18.381 1.00 24.95 ?  17  TYR   B CE2  1 
ATOM   4308 C CZ   . TYR   B 1 17  ? 36.044 -23.909 -17.961 1.00 25.73 ?  17  TYR   B CZ   1 
ATOM   4309 O OH   . TYR   B 1 17  ? 35.195 -23.220 -18.797 1.00 27.45 ?  17  TYR   B OH   1 
ATOM   4310 H H    . TYR   B 1 17  ? 37.437 -25.659 -13.046 1.00 17.00 ?  17  TYR   B H    1 
ATOM   4311 H HA   . TYR   B 1 17  ? 37.521 -27.699 -14.840 1.00 17.74 ?  17  TYR   B HA   1 
ATOM   4312 H HB2  . TYR   B 1 17  ? 39.240 -25.436 -14.889 1.00 21.35 ?  17  TYR   B HB2  1 
ATOM   4313 H HB3  . TYR   B 1 17  ? 39.254 -26.626 -15.936 1.00 21.35 ?  17  TYR   B HB3  1 
ATOM   4314 H HD1  . TYR   B 1 17  ? 37.398 -23.768 -15.038 1.00 27.66 ?  17  TYR   B HD1  1 
ATOM   4315 H HD2  . TYR   B 1 17  ? 37.812 -26.600 -17.830 1.00 28.20 ?  17  TYR   B HD2  1 
ATOM   4316 H HE1  . TYR   B 1 17  ? 35.968 -22.600 -16.432 1.00 29.80 ?  17  TYR   B HE1  1 
ATOM   4317 H HE2  . TYR   B 1 17  ? 36.387 -25.442 -19.225 1.00 29.94 ?  17  TYR   B HE2  1 
ATOM   4318 H HH   . TYR   B 1 17  ? 35.098 -23.637 -19.520 1.00 32.94 ?  17  TYR   B HH   1 
ATOM   4319 N N    . ILE   B 1 18  ? 39.651 -28.712 -13.884 1.00 14.24 ?  18  ILE   B N    1 
ATOM   4320 C CA   . ILE   B 1 18  ? 40.573 -29.448 -13.023 1.00 14.23 ?  18  ILE   B CA   1 
ATOM   4321 C C    . ILE   B 1 18  ? 41.734 -30.006 -13.838 1.00 14.69 ?  18  ILE   B C    1 
ATOM   4322 O O    . ILE   B 1 18  ? 41.579 -30.407 -14.996 1.00 16.02 ?  18  ILE   B O    1 
ATOM   4323 C CB   . ILE   B 1 18  ? 39.816 -30.554 -12.233 1.00 14.85 ?  18  ILE   B CB   1 
ATOM   4324 C CG1  . ILE   B 1 18  ? 40.671 -31.098 -11.086 1.00 14.90 ?  18  ILE   B CG1  1 
ATOM   4325 C CG2  . ILE   B 1 18  ? 39.320 -31.675 -13.167 1.00 15.26 ?  18  ILE   B CG2  1 
ATOM   4326 C CD1  . ILE   B 1 18  ? 39.874 -31.911 -10.074 1.00 16.07 ?  18  ILE   B CD1  1 
ATOM   4327 H H    . ILE   B 1 18  ? 39.555 -29.042 -14.668 1.00 17.09 ?  18  ILE   B H    1 
ATOM   4328 H HA   . ILE   B 1 18  ? 40.928 -28.840 -12.358 1.00 17.07 ?  18  ILE   B HA   1 
ATOM   4329 H HB   . ILE   B 1 18  ? 39.027 -30.151 -11.837 1.00 17.82 ?  18  ILE   B HB   1 
ATOM   4330 H HG12 . ILE   B 1 18  ? 41.358 -31.670 -11.449 1.00 17.88 ?  18  ILE   B HG12 1 
ATOM   4331 H HG13 . ILE   B 1 18  ? 41.067 -30.351 -10.614 1.00 17.88 ?  18  ILE   B HG13 1 
ATOM   4332 H HG21 . ILE   B 1 18  ? 38.731 -32.267 -12.669 1.00 18.31 ?  18  ILE   B HG21 1 
ATOM   4333 H HG22 . ILE   B 1 18  ? 38.830 -31.275 -13.905 1.00 18.31 ?  18  ILE   B HG22 1 
ATOM   4334 H HG23 . ILE   B 1 18  ? 40.079 -32.170 -13.503 1.00 18.31 ?  18  ILE   B HG23 1 
ATOM   4335 H HD11 . ILE   B 1 18  ? 40.465 -32.191 -9.359  1.00 19.29 ?  18  ILE   B HD11 1 
ATOM   4336 H HD12 . ILE   B 1 18  ? 39.158 -31.361 -9.716  1.00 19.29 ?  18  ILE   B HD12 1 
ATOM   4337 H HD13 . ILE   B 1 18  ? 39.500 -32.690 -10.518 1.00 19.29 ?  18  ILE   B HD13 1 
ATOM   4338 N N    . LYS   B 1 19  ? 42.911 -30.040 -13.214 1.00 15.01 ?  19  LYS   B N    1 
ATOM   4339 C CA   . LYS   B 1 19  ? 44.116 -30.519 -13.871 1.00 15.90 ?  19  LYS   B CA   1 
ATOM   4340 C C    . LYS   B 1 19  ? 45.014 -31.205 -12.852 1.00 15.73 ?  19  LYS   B C    1 
ATOM   4341 O O    . LYS   B 1 19  ? 45.108 -30.770 -11.702 1.00 15.28 ?  19  LYS   B O    1 
ATOM   4342 C CB   . LYS   B 1 19  ? 44.877 -29.353 -14.514 1.00 17.17 ?  19  LYS   B CB   1 
ATOM   4343 C CG   . LYS   B 1 19  ? 46.068 -29.779 -15.348 1.00 19.17 ?  19  LYS   B CG   1 
ATOM   4344 C CD   . LYS   B 1 19  ? 46.800 -28.563 -15.897 1.00 21.33 ?  19  LYS   B CD   1 
ATOM   4345 C CE   . LYS   B 1 19  ? 47.972 -28.954 -16.778 1.00 23.48 ?  19  LYS   B CE   1 
ATOM   4346 N NZ   . LYS   B 1 19  ? 48.711 -27.762 -17.271 1.00 24.83 ?  19  LYS   B NZ   1 
ATOM   4347 H H    . LYS   B 1 19  ? 43.023 -29.790 -12.396 1.00 18.01 ?  19  LYS   B H    1 
ATOM   4348 H HA   . LYS   B 1 19  ? 43.869 -31.157 -14.561 1.00 19.08 ?  19  LYS   B HA   1 
ATOM   4349 H HB2  . LYS   B 1 19  ? 44.264 -28.870 -15.092 1.00 20.60 ?  19  LYS   B HB2  1 
ATOM   4350 H HB3  . LYS   B 1 19  ? 45.189 -28.764 -13.806 1.00 20.60 ?  19  LYS   B HB3  1 
ATOM   4351 H HG2  . LYS   B 1 19  ? 46.678 -30.289 -14.794 1.00 23.00 ?  19  LYS   B HG2  1 
ATOM   4352 H HG3  . LYS   B 1 19  ? 45.753 -30.319 -16.091 1.00 23.00 ?  19  LYS   B HG3  1 
ATOM   4353 H HD2  . LYS   B 1 19  ? 46.183 -28.033 -16.427 1.00 25.60 ?  19  LYS   B HD2  1 
ATOM   4354 H HD3  . LYS   B 1 19  ? 47.139 -28.036 -15.155 1.00 25.60 ?  19  LYS   B HD3  1 
ATOM   4355 H HE2  . LYS   B 1 19  ? 48.584 -29.505 -16.265 1.00 28.18 ?  19  LYS   B HE2  1 
ATOM   4356 H HE3  . LYS   B 1 19  ? 47.640 -29.448 -17.545 1.00 28.18 ?  19  LYS   B HE3  1 
ATOM   4357 H HZ1  . LYS   B 1 19  ? 49.352 -28.013 -17.836 1.00 29.79 ?  19  LYS   B HZ1  1 
ATOM   4358 H HZ2  . LYS   B 1 19  ? 48.154 -27.211 -17.695 1.00 29.79 ?  19  LYS   B HZ2  1 
ATOM   4359 H HZ3  . LYS   B 1 19  ? 49.081 -27.328 -16.589 1.00 29.79 ?  19  LYS   B HZ3  1 
ATOM   4360 N N    . ASN   B 1 20  ? 45.700 -32.260 -13.287 1.00 17.34 ?  20  ASN   B N    1 
ATOM   4361 C CA   . ASN   B 1 20  ? 46.721 -32.896 -12.460 1.00 18.22 ?  20  ASN   B CA   1 
ATOM   4362 C C    . ASN   B 1 20  ? 48.010 -32.099 -12.636 1.00 18.48 ?  20  ASN   B C    1 
ATOM   4363 O O    . ASN   B 1 20  ? 48.655 -32.180 -13.689 1.00 20.43 ?  20  ASN   B O    1 
ATOM   4364 C CB   . ASN   B 1 20  ? 46.875 -34.358 -12.882 1.00 19.98 ?  20  ASN   B CB   1 
ATOM   4365 C CG   . ASN   B 1 20  ? 48.044 -35.069 -12.206 1.00 21.26 ?  20  ASN   B CG   1 
ATOM   4366 O OD1  . ASN   B 1 20  ? 48.703 -35.914 -12.825 1.00 24.15 ?  20  ASN   B OD1  1 
ATOM   4367 N ND2  . ASN   B 1 20  ? 48.295 -34.757 -10.939 1.00 20.89 ?  20  ASN   B ND2  1 
ATOM   4368 H H    . ASN   B 1 20  ? 45.590 -32.616 -14.060 1.00 20.81 ?  20  ASN   B H    1 
ATOM   4369 H HA   . ASN   B 1 20  ? 46.440 -32.869 -11.530 1.00 21.87 ?  20  ASN   B HA   1 
ATOM   4370 H HB2  . ASN   B 1 20  ? 46.057 -34.839 -12.656 1.00 23.98 ?  20  ASN   B HB2  1 
ATOM   4371 H HB3  . ASN   B 1 20  ? 47.014 -34.391 -13.840 1.00 23.98 ?  20  ASN   B HB3  1 
ATOM   4372 H HD21 . ASN   B 1 20  ? 48.942 -35.135 -10.523 1.00 25.06 ?  20  ASN   B HD21 1 
ATOM   4373 H HD22 . ASN   B 1 20  ? 47.809 -34.169 -10.530 1.00 25.06 ?  20  ASN   B HD22 1 
ATOM   4374 N N    . ALA   B 1 21  ? 48.375 -31.306 -11.627 1.00 17.97 ?  21  ALA   B N    1 
ATOM   4375 C CA   . ALA   B 1 21  ? 49.494 -30.392 -11.788 1.00 18.94 ?  21  ALA   B CA   1 
ATOM   4376 C C    . ALA   B 1 21  ? 49.952 -29.869 -10.435 1.00 17.62 ?  21  ALA   B C    1 
ATOM   4377 O O    . ALA   B 1 21  ? 49.209 -29.883 -9.450  1.00 17.02 ?  21  ALA   B O    1 
ATOM   4378 C CB   . ALA   B 1 21  ? 49.118 -29.237 -12.715 1.00 20.71 ?  21  ALA   B CB   1 
ATOM   4379 H H    . ALA   B 1 21  ? 47.983 -31.281 -10.851 1.00 21.57 ?  21  ALA   B H    1 
ATOM   4380 H HA   . ALA   B 1 21  ? 50.227 -30.881 -12.181 1.00 22.72 ?  21  ALA   B HA   1 
ATOM   4381 H HB1  . ALA   B 1 21  ? 49.906 -28.699 -12.858 1.00 24.85 ?  21  ALA   B HB1  1 
ATOM   4382 H HB2  . ALA   B 1 21  ? 48.810 -29.610 -13.557 1.00 24.85 ?  21  ALA   B HB2  1 
ATOM   4383 H HB3  . ALA   B 1 21  ? 48.415 -28.719 -12.303 1.00 24.85 ?  21  ALA   B HB3  1 
ATOM   4384 N N    . ASP   B 1 22  ? 51.206 -29.419 -10.419 1.00 16.88 ?  22  ASP   B N    1 
ATOM   4385 C CA   . ASP   B 1 22  ? 51.826 -28.720 -9.297  1.00 16.09 ?  22  ASP   B CA   1 
ATOM   4386 C C    . ASP   B 1 22  ? 51.423 -27.248 -9.381  1.00 14.39 ?  22  ASP   B C    1 
ATOM   4387 O O    . ASP   B 1 22  ? 51.737 -26.576 -10.368 1.00 14.92 ?  22  ASP   B O    1 
ATOM   4388 C CB   . ASP   B 1 22  ? 53.342 -28.901 -9.457  1.00 17.20 ?  22  ASP   B CB   1 
ATOM   4389 C CG   . ASP   B 1 22  ? 54.174 -28.142 -8.435  1.00 18.81 ?  22  ASP   B CG   1 
ATOM   4390 O OD1  . ASP   B 1 22  ? 53.817 -27.020 -8.044  1.00 18.92 ?  22  ASP   B OD1  1 
ATOM   4391 O OD2  . ASP   B 1 22  ? 55.244 -28.662 -8.048  1.00 21.38 -1 22  ASP   B OD2  1 
ATOM   4392 H H    . ASP   B 1 22  ? 51.739 -29.507 -11.089 1.00 20.26 ?  22  ASP   B H    1 
ATOM   4393 H HA   . ASP   B 1 22  ? 51.531 -29.101 -8.452  1.00 19.31 ?  22  ASP   B HA   1 
ATOM   4394 H HB2  . ASP   B 1 22  ? 53.555 -29.839 -9.375  1.00 20.64 ?  22  ASP   B HB2  1 
ATOM   4395 H HB3  . ASP   B 1 22  ? 53.598 -28.577 -10.335 1.00 20.64 ?  22  ASP   B HB3  1 
ATOM   4396 N N    . ILE   B 1 23  ? 50.714 -26.752 -8.359  1.00 13.73 ?  23  ILE   B N    1 
ATOM   4397 C CA   . ILE   B 1 23  ? 50.126 -25.409 -8.429  1.00 12.64 ?  23  ILE   B CA   1 
ATOM   4398 C C    . ILE   B 1 23  ? 51.188 -24.327 -8.578  1.00 12.51 ?  23  ILE   B C    1 
ATOM   4399 O O    . ILE   B 1 23  ? 50.930 -23.290 -9.196  1.00 12.05 ?  23  ILE   B O    1 
ATOM   4400 C CB   . ILE   B 1 23  ? 49.199 -25.145 -7.224  1.00 13.12 ?  23  ILE   B CB   1 
ATOM   4401 C CG1  . ILE   B 1 23  ? 48.367 -23.878 -7.440  1.00 13.66 ?  23  ILE   B CG1  1 
ATOM   4402 C CG2  . ILE   B 1 23  ? 49.985 -25.102 -5.925  1.00 14.55 ?  23  ILE   B CG2  1 
ATOM   4403 C CD1  . ILE   B 1 23  ? 47.252 -23.694 -6.420  1.00 14.76 ?  23  ILE   B CD1  1 
ATOM   4404 H H    . ILE   B 1 23  ? 50.556 -27.170 -7.624  1.00 16.48 ?  23  ILE   B H    1 
ATOM   4405 H HA   . ILE   B 1 23  ? 49.569 -25.367 -9.220  1.00 15.17 ?  23  ILE   B HA   1 
ATOM   4406 H HB   . ILE   B 1 23  ? 48.578 -25.889 -7.167  1.00 15.74 ?  23  ILE   B HB   1 
ATOM   4407 H HG12 . ILE   B 1 23  ? 48.956 -23.106 -7.385  1.00 16.39 ?  23  ILE   B HG12 1 
ATOM   4408 H HG13 . ILE   B 1 23  ? 47.963 -23.915 -8.324  1.00 16.39 ?  23  ILE   B HG13 1 
ATOM   4409 H HG21 . ILE   B 1 23  ? 49.366 -25.088 -5.181  1.00 17.46 ?  23  ILE   B HG21 1 
ATOM   4410 H HG22 . ILE   B 1 23  ? 50.547 -25.894 -5.872  1.00 17.46 ?  23  ILE   B HG22 1 
ATOM   4411 H HG23 . ILE   B 1 23  ? 50.537 -24.306 -5.915  1.00 17.46 ?  23  ILE   B HG23 1 
ATOM   4412 H HD11 . ILE   B 1 23  ? 46.739 -22.907 -6.656  1.00 17.72 ?  23  ILE   B HD11 1 
ATOM   4413 H HD12 . ILE   B 1 23  ? 46.685 -24.479 -6.434  1.00 17.72 ?  23  ILE   B HD12 1 
ATOM   4414 H HD13 . ILE   B 1 23  ? 47.648 -23.583 -5.542  1.00 17.72 ?  23  ILE   B HD13 1 
ATOM   4415 N N    . VAL   B 1 24  ? 52.385 -24.533 -8.019  1.00 12.33 ?  24  VAL   B N    1 
ATOM   4416 C CA   . VAL   B 1 24  ? 53.462 -23.555 -8.188  1.00 13.33 ?  24  VAL   B CA   1 
ATOM   4417 C C    . VAL   B 1 24  ? 53.917 -23.511 -9.641  1.00 13.89 ?  24  VAL   B C    1 
ATOM   4418 O O    . VAL   B 1 24  ? 54.052 -22.436 -10.240 1.00 14.30 ?  24  VAL   B O    1 
ATOM   4419 C CB   . VAL   B 1 24  ? 54.638 -23.871 -7.241  1.00 14.10 ?  24  VAL   B CB   1 
ATOM   4420 C CG1  . VAL   B 1 24  ? 55.854 -22.995 -7.573  1.00 15.03 ?  24  VAL   B CG1  1 
ATOM   4421 C CG2  . VAL   B 1 24  ? 54.214 -23.673 -5.807  1.00 15.16 ?  24  VAL   B CG2  1 
ATOM   4422 H H    . VAL   B 1 24  ? 52.597 -25.220 -7.551  1.00 14.80 ?  24  VAL   B H    1 
ATOM   4423 H HA   . VAL   B 1 24  ? 53.127 -22.676 -7.953  1.00 15.99 ?  24  VAL   B HA   1 
ATOM   4424 H HB   . VAL   B 1 24  ? 54.895 -24.801 -7.349  1.00 16.92 ?  24  VAL   B HB   1 
ATOM   4425 H HG11 . VAL   B 1 24  ? 56.454 -22.992 -6.810  1.00 18.04 ?  24  VAL   B HG11 1 
ATOM   4426 H HG12 . VAL   B 1 24  ? 56.306 -23.366 -8.345  1.00 18.04 ?  24  VAL   B HG12 1 
ATOM   4427 H HG13 . VAL   B 1 24  ? 55.551 -22.095 -7.759  1.00 18.04 ?  24  VAL   B HG13 1 
ATOM   4428 H HG21 . VAL   B 1 24  ? 54.938 -23.942 -5.221  1.00 18.20 ?  24  VAL   B HG21 1 
ATOM   4429 H HG22 . VAL   B 1 24  ? 54.006 -22.736 -5.667  1.00 18.20 ?  24  VAL   B HG22 1 
ATOM   4430 H HG23 . VAL   B 1 24  ? 53.427 -24.216 -5.631  1.00 18.20 ?  24  VAL   B HG23 1 
ATOM   4431 N N    . GLU   B 1 25  ? 54.186 -24.685 -10.221 1.00 15.05 ?  25  GLU   B N    1 
ATOM   4432 C CA   . GLU   B 1 25  ? 54.574 -24.732 -11.625 1.00 16.49 ?  25  GLU   B CA   1 
ATOM   4433 C C    . GLU   B 1 25  ? 53.466 -24.189 -12.512 1.00 15.09 ?  25  GLU   B C    1 
ATOM   4434 O O    . GLU   B 1 25  ? 53.734 -23.479 -13.491 1.00 15.84 ?  25  GLU   B O    1 
ATOM   4435 C CB   . GLU   B 1 25  ? 54.963 -26.156 -12.015 1.00 20.37 ?  25  GLU   B CB   1 
ATOM   4436 C CG   . GLU   B 1 25  ? 56.266 -26.613 -11.371 1.00 25.60 ?  25  GLU   B CG   1 
ATOM   4437 C CD   . GLU   B 1 25  ? 57.389 -25.591 -11.493 1.00 30.16 ?  25  GLU   B CD   1 
ATOM   4438 O OE1  . GLU   B 1 25  ? 57.771 -25.253 -12.635 1.00 31.96 ?  25  GLU   B OE1  1 
ATOM   4439 O OE2  . GLU   B 1 25  ? 57.882 -25.113 -10.445 1.00 31.83 -1 25  GLU   B OE2  1 
ATOM   4440 H H    . GLU   B 1 25  ? 54.157 -25.448 -9.826  1.00 18.06 ?  25  GLU   B H    1 
ATOM   4441 H HA   . GLU   B 1 25  ? 55.338 -24.151 -11.754 1.00 19.79 ?  25  GLU   B HA   1 
ATOM   4442 H HB2  . GLU   B 1 25  ? 54.261 -26.766 -11.729 1.00 24.44 ?  25  GLU   B HB2  1 
ATOM   4443 H HB3  . GLU   B 1 25  ? 55.067 -26.203 -12.978 1.00 24.44 ?  25  GLU   B HB3  1 
ATOM   4444 H HG2  . GLU   B 1 25  ? 56.119 -26.762 -10.430 1.00 30.72 ?  25  GLU   B HG2  1 
ATOM   4445 H HG3  . GLU   B 1 25  ? 56.563 -27.425 -11.806 1.00 30.72 ?  25  GLU   B HG3  1 
ATOM   4446 N N    A GLU   B 1 26  ? 52.211 -24.501 -12.180 0.42 14.06 ?  26  GLU   B N    1 
ATOM   4447 N N    B GLU   B 1 26  ? 52.210 -24.502 -12.180 0.58 14.30 ?  26  GLU   B N    1 
ATOM   4448 C CA   A GLU   B 1 26  ? 51.088 -23.968 -12.946 0.42 14.53 ?  26  GLU   B CA   1 
ATOM   4449 C CA   B GLU   B 1 26  ? 51.081 -23.975 -12.943 0.58 15.57 ?  26  GLU   B CA   1 
ATOM   4450 C C    A GLU   B 1 26  ? 51.048 -22.450 -12.872 0.42 13.78 ?  26  GLU   B C    1 
ATOM   4451 C C    B GLU   B 1 26  ? 51.032 -22.455 -12.869 0.58 14.09 ?  26  GLU   B C    1 
ATOM   4452 O O    A GLU   B 1 26  ? 50.871 -21.772 -13.890 0.42 14.88 ?  26  GLU   B O    1 
ATOM   4453 O O    B GLU   B 1 26  ? 50.819 -21.780 -13.882 0.58 15.39 ?  26  GLU   B O    1 
ATOM   4454 C CB   A GLU   B 1 26  ? 49.774 -24.550 -12.428 0.42 15.46 ?  26  GLU   B CB   1 
ATOM   4455 C CB   B GLU   B 1 26  ? 49.765 -24.556 -12.420 0.58 17.92 ?  26  GLU   B CB   1 
ATOM   4456 C CG   A GLU   B 1 26  ? 49.461 -25.929 -12.957 0.42 17.29 ?  26  GLU   B CG   1 
ATOM   4457 C CG   B GLU   B 1 26  ? 49.241 -25.765 -13.181 0.58 21.11 ?  26  GLU   B CG   1 
ATOM   4458 C CD   A GLU   B 1 26  ? 49.279 -25.958 -14.465 0.42 17.56 ?  26  GLU   B CD   1 
ATOM   4459 C CD   B GLU   B 1 26  ? 48.916 -25.460 -14.641 0.58 22.16 ?  26  GLU   B CD   1 
ATOM   4460 O OE1  A GLU   B 1 26  ? 48.445 -25.187 -14.990 0.42 16.62 ?  26  GLU   B OE1  1 
ATOM   4461 O OE1  B GLU   B 1 26  ? 47.892 -24.800 -14.927 0.58 23.06 ?  26  GLU   B OE1  1 
ATOM   4462 O OE2  A GLU   B 1 26  ? 49.975 -26.754 -15.123 0.42 18.28 -1 26  GLU   B OE2  1 
ATOM   4463 O OE2  B GLU   B 1 26  ? 49.687 -25.896 -15.509 0.58 21.81 -1 26  GLU   B OE2  1 
ATOM   4464 H H    A GLU   B 1 26  ? 51.986 -25.011 -11.522 0.42 16.87 ?  26  GLU   B H    1 
ATOM   4465 H H    B GLU   B 1 26  ? 51.987 -25.015 -11.522 0.58 17.16 ?  26  GLU   B H    1 
ATOM   4466 H HA   A GLU   B 1 26  ? 51.191 -24.221 -13.874 0.42 17.44 ?  26  GLU   B HA   1 
ATOM   4467 H HA   B GLU   B 1 26  ? 51.183 -24.231 -13.871 0.58 18.68 ?  26  GLU   B HA   1 
ATOM   4468 H HB2  A GLU   B 1 26  ? 49.819 -24.605 -11.458 0.42 18.55 ?  26  GLU   B HB2  1 
ATOM   4469 H HB2  B GLU   B 1 26  ? 49.889 -24.818 -11.495 0.58 21.50 ?  26  GLU   B HB2  1 
ATOM   4470 H HB3  A GLU   B 1 26  ? 49.049 -23.956 -12.684 0.42 18.55 ?  26  GLU   B HB3  1 
ATOM   4471 H HB3  B GLU   B 1 26  ? 49.086 -23.863 -12.471 0.58 21.50 ?  26  GLU   B HB3  1 
ATOM   4472 H HG2  A GLU   B 1 26  ? 50.198 -26.508 -12.739 0.42 20.74 ?  26  GLU   B HG2  1 
ATOM   4473 H HG2  B GLU   B 1 26  ? 49.912 -26.465 -13.143 0.58 25.33 ?  26  GLU   B HG2  1 
ATOM   4474 H HG3  A GLU   B 1 26  ? 48.645 -26.236 -12.539 0.42 20.74 ?  26  GLU   B HG3  1 
ATOM   4475 H HG3  B GLU   B 1 26  ? 48.423 -26.066 -12.759 0.58 25.33 ?  26  GLU   B HG3  1 
ATOM   4476 N N    . ALA   B 1 27  ? 51.198 -21.896 -11.668 1.00 13.00 ?  27  ALA   B N    1 
ATOM   4477 C CA   . ALA   B 1 27  ? 51.158 -20.447 -11.524 1.00 13.09 ?  27  ALA   B CA   1 
ATOM   4478 C C    . ALA   B 1 27  ? 52.221 -19.788 -12.394 1.00 14.16 ?  27  ALA   B C    1 
ATOM   4479 O O    . ALA   B 1 27  ? 51.949 -18.796 -13.081 1.00 14.91 ?  27  ALA   B O    1 
ATOM   4480 C CB   . ALA   B 1 27  ? 51.334 -20.056 -10.057 1.00 12.83 ?  27  ALA   B CB   1 
ATOM   4481 H H    A ALA   B 1 27  ? 51.321 -22.328 -10.936 0.42 15.60 ?  27  ALA   B H    1 
ATOM   4482 H H    B ALA   B 1 27  ? 51.326 -22.327 -10.936 0.58 15.60 ?  27  ALA   B H    1 
ATOM   4483 H HA   . ALA   B 1 27  ? 50.296 -20.121 -11.817 1.00 15.71 ?  27  ALA   B HA   1 
ATOM   4484 H HB1  . ALA   B 1 27  ? 51.301 -19.089 -9.979  1.00 15.40 ?  27  ALA   B HB1  1 
ATOM   4485 H HB2  . ALA   B 1 27  ? 50.615 -20.452 -9.538  1.00 15.40 ?  27  ALA   B HB2  1 
ATOM   4486 H HB3  . ALA   B 1 27  ? 52.189 -20.384 -9.739  1.00 15.40 ?  27  ALA   B HB3  1 
ATOM   4487 N N    . LYS   B 1 28  ? 53.437 -20.342 -12.399 1.00 15.65 ?  28  LYS   B N    1 
ATOM   4488 C CA   . LYS   B 1 28  ? 54.510 -19.729 -13.176 1.00 17.87 ?  28  LYS   B CA   1 
ATOM   4489 C C    . LYS   B 1 28  ? 54.249 -19.822 -14.675 1.00 18.35 ?  28  LYS   B C    1 
ATOM   4490 O O    . LYS   B 1 28  ? 54.654 -18.928 -15.428 1.00 19.39 ?  28  LYS   B O    1 
ATOM   4491 C CB   . LYS   B 1 28  ? 55.868 -20.328 -12.781 1.00 21.44 ?  28  LYS   B CB   1 
ATOM   4492 C CG   . LYS   B 1 28  ? 56.260 -19.997 -11.342 1.00 24.74 ?  28  LYS   B CG   1 
ATOM   4493 C CD   . LYS   B 1 28  ? 57.697 -20.383 -11.005 1.00 28.64 ?  28  LYS   B CD   1 
ATOM   4494 C CE   . LYS   B 1 28  ? 57.827 -21.849 -10.674 1.00 31.39 ?  28  LYS   B CE   1 
ATOM   4495 N NZ   . LYS   B 1 28  ? 59.189 -22.161 -10.153 1.00 35.75 ?  28  LYS   B NZ   1 
ATOM   4496 H H    . LYS   B 1 28  ? 53.662 -21.055 -11.970 1.00 18.77 ?  28  LYS   B H    1 
ATOM   4497 H HA   . LYS   B 1 28  ? 54.547 -18.788 -12.955 1.00 21.44 ?  28  LYS   B HA   1 
ATOM   4498 H HB2  . LYS   B 1 28  ? 55.832 -21.292 -12.864 1.00 25.73 ?  28  LYS   B HB2  1 
ATOM   4499 H HB3  . LYS   B 1 28  ? 56.559 -19.970 -13.365 1.00 25.73 ?  28  LYS   B HB3  1 
ATOM   4500 H HG2  . LYS   B 1 28  ? 56.167 -19.039 -11.205 1.00 29.69 ?  28  LYS   B HG2  1 
ATOM   4501 H HG3  . LYS   B 1 28  ? 55.672 -20.475 -10.739 1.00 29.69 ?  28  LYS   B HG3  1 
ATOM   4502 H HD2  . LYS   B 1 28  ? 58.264 -20.191 -11.769 1.00 34.37 ?  28  LYS   B HD2  1 
ATOM   4503 H HD3  . LYS   B 1 28  ? 57.990 -19.869 -10.236 1.00 34.37 ?  28  LYS   B HD3  1 
ATOM   4504 H HE2  . LYS   B 1 28  ? 57.177 -22.083 -9.992  1.00 37.67 ?  28  LYS   B HE2  1 
ATOM   4505 H HE3  . LYS   B 1 28  ? 57.678 -22.375 -11.476 1.00 37.67 ?  28  LYS   B HE3  1 
ATOM   4506 H HZ1  . LYS   B 1 28  ? 59.251 -23.027 -9.962  1.00 42.90 ?  28  LYS   B HZ1  1 
ATOM   4507 H HZ2  . LYS   B 1 28  ? 59.802 -21.954 -10.764 1.00 42.90 ?  28  LYS   B HZ2  1 
ATOM   4508 H HZ3  . LYS   B 1 28  ? 59.347 -21.689 -9.414  1.00 42.90 ?  28  LYS   B HZ3  1 
ATOM   4509 N N    . LYS   B 1 29  ? 53.551 -20.868 -15.124 1.00 19.49 ?  29  LYS   B N    1 
ATOM   4510 C CA   . LYS   B 1 29  ? 53.263 -21.028 -16.548 1.00 22.21 ?  29  LYS   B CA   1 
ATOM   4511 C C    . LYS   B 1 29  ? 52.021 -20.251 -16.981 1.00 21.17 ?  29  LYS   B C    1 
ATOM   4512 O O    . LYS   B 1 29  ? 52.017 -19.639 -18.056 1.00 22.72 ?  29  LYS   B O    1 
ATOM   4513 C CB   . LYS   B 1 29  ? 53.094 -22.511 -16.882 1.00 26.82 ?  29  LYS   B CB   1 
ATOM   4514 C CG   . LYS   B 1 29  ? 52.944 -22.799 -18.370 1.00 30.97 ?  29  LYS   B CG   1 
ATOM   4515 C CD   . LYS   B 1 29  ? 53.129 -24.280 -18.676 1.00 34.42 ?  29  LYS   B CD   1 
ATOM   4516 C CE   . LYS   B 1 29  ? 51.981 -25.119 -18.141 1.00 35.76 ?  29  LYS   B CE   1 
ATOM   4517 N NZ   . LYS   B 1 29  ? 52.168 -26.566 -18.451 1.00 37.37 ?  29  LYS   B NZ   1 
ATOM   4518 H H    . LYS   B 1 29  ? 53.242 -21.497 -14.624 1.00 23.39 ?  29  LYS   B H    1 
ATOM   4519 H HA   . LYS   B 1 29  ? 54.012 -20.692 -17.057 1.00 26.66 ?  29  LYS   B HA   1 
ATOM   4520 H HB2  . LYS   B 1 29  ? 53.875 -22.992 -16.568 1.00 32.18 ?  29  LYS   B HB2  1 
ATOM   4521 H HB3  . LYS   B 1 29  ? 52.301 -22.846 -16.437 1.00 32.18 ?  29  LYS   B HB3  1 
ATOM   4522 H HG2  . LYS   B 1 29  ? 52.055 -22.537 -18.659 1.00 37.17 ?  29  LYS   B HG2  1 
ATOM   4523 H HG3  . LYS   B 1 29  ? 53.616 -22.300 -18.862 1.00 37.17 ?  29  LYS   B HG3  1 
ATOM   4524 H HD2  . LYS   B 1 29  ? 53.172 -24.407 -19.637 1.00 41.31 ?  29  LYS   B HD2  1 
ATOM   4525 H HD3  . LYS   B 1 29  ? 53.949 -24.593 -18.262 1.00 41.31 ?  29  LYS   B HD3  1 
ATOM   4526 H HE2  . LYS   B 1 29  ? 51.933 -25.019 -17.177 1.00 42.91 ?  29  LYS   B HE2  1 
ATOM   4527 H HE3  . LYS   B 1 29  ? 51.152 -24.825 -18.551 1.00 42.91 ?  29  LYS   B HE3  1 
ATOM   4528 H HZ1  . LYS   B 1 29  ? 51.485 -27.038 -18.129 1.00 44.85 ?  29  LYS   B HZ1  1 
ATOM   4529 H HZ2  . LYS   B 1 29  ? 52.211 -26.686 -19.332 1.00 44.85 ?  29  LYS   B HZ2  1 
ATOM   4530 H HZ3  . LYS   B 1 29  ? 52.922 -26.862 -18.082 1.00 44.85 ?  29  LYS   B HZ3  1 
ATOM   4531 N N    . VAL   B 1 30  ? 50.959 -20.286 -16.171 1.00 19.19 ?  30  VAL   B N    1 
ATOM   4532 C CA   . VAL   B 1 30  ? 49.667 -19.701 -16.540 1.00 19.37 ?  30  VAL   B CA   1 
ATOM   4533 C C    . VAL   B 1 30  ? 49.670 -18.185 -16.399 1.00 17.97 ?  30  VAL   B C    1 
ATOM   4534 O O    . VAL   B 1 30  ? 48.933 -17.481 -17.107 1.00 19.02 ?  30  VAL   B O    1 
ATOM   4535 C CB   . VAL   B 1 30  ? 48.570 -20.313 -15.646 1.00 21.09 ?  30  VAL   B CB   1 
ATOM   4536 C CG1  . VAL   B 1 30  ? 47.287 -19.488 -15.698 1.00 22.01 ?  30  VAL   B CG1  1 
ATOM   4537 C CG2  . VAL   B 1 30  ? 48.310 -21.765 -16.026 1.00 22.24 ?  30  VAL   B CG2  1 
ATOM   4538 H H    . VAL   B 1 30  ? 50.957 -20.668 -15.392 1.00 23.02 ?  30  VAL   B H    1 
ATOM   4539 H HA   . VAL   B 1 30  ? 49.468 -19.938 -17.458 1.00 23.24 ?  30  VAL   B HA   1 
ATOM   4540 H HB   . VAL   B 1 30  ? 48.877 -20.321 -14.729 1.00 25.31 ?  30  VAL   B HB   1 
ATOM   4541 H HG11 . VAL   B 1 30  ? 46.543 -20.054 -15.435 1.00 26.42 ?  30  VAL   B HG11 1 
ATOM   4542 H HG12 . VAL   B 1 30  ? 47.363 -18.746 -15.081 1.00 26.42 ?  30  VAL   B HG12 1 
ATOM   4543 H HG13 . VAL   B 1 30  ? 47.145 -19.171 -16.599 1.00 26.42 ?  30  VAL   B HG13 1 
ATOM   4544 H HG21 . VAL   B 1 30  ? 47.622 -22.129 -15.442 1.00 26.69 ?  30  VAL   B HG21 1 
ATOM   4545 H HG22 . VAL   B 1 30  ? 48.007 -21.802 -16.948 1.00 26.69 ?  30  VAL   B HG22 1 
ATOM   4546 H HG23 . VAL   B 1 30  ? 49.128 -22.272 -15.925 1.00 26.69 ?  30  VAL   B HG23 1 
ATOM   4547 N N    . LYS   B 1 31  ? 50.444 -17.677 -15.455 1.00 17.97 ?  31  LYS   B N    1 
ATOM   4548 C CA   . LYS   B 1 31  ? 50.481 -16.267 -15.105 1.00 18.87 ?  31  LYS   B CA   1 
ATOM   4549 C C    . LYS   B 1 31  ? 49.084 -15.783 -14.720 1.00 16.60 ?  31  LYS   B C    1 
ATOM   4550 O O    . LYS   B 1 31  ? 48.549 -14.863 -15.350 1.00 16.79 ?  31  LYS   B O    1 
ATOM   4551 C CB   . LYS   B 1 31  ? 51.116 -15.467 -16.248 1.00 22.69 ?  31  LYS   B CB   1 
ATOM   4552 C CG   . LYS   B 1 31  ? 52.547 -15.911 -16.560 1.00 26.37 ?  31  LYS   B CG   1 
ATOM   4553 C CD   . LYS   B 1 31  ? 53.144 -15.122 -17.711 1.00 29.62 ?  31  LYS   B CD   1 
ATOM   4554 C CE   . LYS   B 1 31  ? 54.633 -15.373 -17.845 1.00 33.19 ?  31  LYS   B CE   1 
ATOM   4555 N NZ   . LYS   B 1 31  ? 55.350 -15.000 -16.595 1.00 35.41 ?  31  LYS   B NZ   1 
ATOM   4556 H H    . LYS   B 1 31  ? 50.977 -18.165 -14.994 1.00 21.57 ?  31  LYS   B H    1 
ATOM   4557 H HA   . LYS   B 1 31  ? 51.044 -16.183 -14.332 1.00 22.65 ?  31  LYS   B HA   1 
ATOM   4558 H HB2  . LYS   B 1 31  ? 50.592 -15.579 -17.055 1.00 27.23 ?  31  LYS   B HB2  1 
ATOM   4559 H HB3  . LYS   B 1 31  ? 51.146 -14.536 -15.992 1.00 27.23 ?  31  LYS   B HB3  1 
ATOM   4560 H HG2  . LYS   B 1 31  ? 53.095 -15.776 -15.772 1.00 31.65 ?  31  LYS   B HG2  1 
ATOM   4561 H HG3  . LYS   B 1 31  ? 52.543 -16.851 -16.806 1.00 31.65 ?  31  LYS   B HG3  1 
ATOM   4562 H HD2  . LYS   B 1 31  ? 52.714 -15.391 -18.537 1.00 35.55 ?  31  LYS   B HD2  1 
ATOM   4563 H HD3  . LYS   B 1 31  ? 53.009 -14.177 -17.551 1.00 35.55 ?  31  LYS   B HD3  1 
ATOM   4564 H HE2  . LYS   B 1 31  ? 54.790 -16.316 -18.017 1.00 39.82 ?  31  LYS   B HE2  1 
ATOM   4565 H HE3  . LYS   B 1 31  ? 54.987 -14.836 -18.572 1.00 39.82 ?  31  LYS   B HE3  1 
ATOM   4566 H HZ1  . LYS   B 1 31  ? 56.228 -15.007 -16.733 1.00 42.49 ?  31  LYS   B HZ1  1 
ATOM   4567 H HZ2  . LYS   B 1 31  ? 55.104 -14.184 -16.338 1.00 42.49 ?  31  LYS   B HZ2  1 
ATOM   4568 H HZ3  . LYS   B 1 31  ? 55.154 -15.578 -15.947 1.00 42.49 ?  31  LYS   B HZ3  1 
ATOM   4569 N N    . PRO   B 1 32  ? 48.478 -16.355 -13.677 1.00 14.27 ?  32  PRO   B N    1 
ATOM   4570 C CA   . PRO   B 1 32  ? 47.106 -15.986 -13.320 1.00 13.28 ?  32  PRO   B CA   1 
ATOM   4571 C C    . PRO   B 1 32  ? 47.040 -14.645 -12.613 1.00 13.34 ?  32  PRO   B C    1 
ATOM   4572 O O    . PRO   B 1 32  ? 47.971 -14.233 -11.914 1.00 14.76 ?  32  PRO   B O    1 
ATOM   4573 C CB   . PRO   B 1 32  ? 46.700 -17.098 -12.346 1.00 13.69 ?  32  PRO   B CB   1 
ATOM   4574 C CG   . PRO   B 1 32  ? 47.999 -17.440 -11.663 1.00 14.30 ?  32  PRO   B CG   1 
ATOM   4575 C CD   . PRO   B 1 32  ? 49.049 -17.333 -12.731 1.00 14.69 ?  32  PRO   B CD   1 
ATOM   4576 H HA   . PRO   B 1 32  ? 46.524 -15.991 -14.104 1.00 15.94 ?  32  PRO   B HA   1 
ATOM   4577 H HB2  . PRO   B 1 32  ? 46.047 -16.762 -11.712 1.00 16.43 ?  32  PRO   B HB2  1 
ATOM   4578 H HB3  . PRO   B 1 32  ? 46.350 -17.860 -12.837 1.00 16.43 ?  32  PRO   B HB3  1 
ATOM   4579 H HG2  . PRO   B 1 32  ? 48.171 -16.806 -10.949 1.00 17.16 ?  32  PRO   B HG2  1 
ATOM   4580 H HG3  . PRO   B 1 32  ? 47.960 -18.345 -11.317 1.00 17.16 ?  32  PRO   B HG3  1 
ATOM   4581 H HD2  . PRO   B 1 32  ? 49.873 -16.990 -12.364 1.00 17.63 ?  32  PRO   B HD2  1 
ATOM   4582 H HD3  . PRO   B 1 32  ? 49.170 -18.183 -13.172 1.00 17.63 ?  32  PRO   B HD3  1 
ATOM   4583 N N    . THR   B 1 33  ? 45.890 -13.983 -12.770 1.00 12.79 ?  33  THR   B N    1 
ATOM   4584 C CA   . THR   B 1 33  ? 45.614 -12.803 -11.960 1.00 13.00 ?  33  THR   B CA   1 
ATOM   4585 C C    . THR   B 1 33  ? 45.572 -13.156 -10.479 1.00 12.95 ?  33  THR   B C    1 
ATOM   4586 O O    . THR   B 1 33  ? 46.048 -12.377 -9.637  1.00 13.89 ?  33  THR   B O    1 
ATOM   4587 C CB   . THR   B 1 33  ? 44.293 -12.169 -12.401 1.00 13.98 ?  33  THR   B CB   1 
ATOM   4588 O OG1  . THR   B 1 33  ? 44.330 -11.924 -13.806 1.00 14.07 ?  33  THR   B OG1  1 
ATOM   4589 C CG2  . THR   B 1 33  ? 44.046 -10.869 -11.664 1.00 15.59 ?  33  THR   B CG2  1 
ATOM   4590 H H    . THR   B 1 33  ? 45.264 -14.197 -13.326 1.00 15.35 ?  33  THR   B H    1 
ATOM   4591 H HA   . THR   B 1 33  ? 46.315 -12.156 -12.096 1.00 15.60 ?  33  THR   B HA   1 
ATOM   4592 H HB   . THR   B 1 33  ? 43.560 -12.782 -12.205 1.00 16.78 ?  33  THR   B HB   1 
ATOM   4593 H HG1  . THR   B 1 33  ? 43.612 -11.550 -14.054 1.00 16.88 ?  33  THR   B HG1  1 
ATOM   4594 H HG21 . THR   B 1 33  ? 43.284 -10.413 -12.044 1.00 18.71 ?  33  THR   B HG21 1 
ATOM   4595 H HG22 . THR   B 1 33  ? 43.872 -11.048 -10.725 1.00 18.71 ?  33  THR   B HG22 1 
ATOM   4596 H HG23 . THR   B 1 33  ? 44.828 -10.299 -11.735 1.00 18.71 ?  33  THR   B HG23 1 
ATOM   4597 N N    . VAL   B 1 34  ? 45.000 -14.320 -10.139 1.00 11.85 ?  34  VAL   B N    1 
ATOM   4598 C CA   . VAL   B 1 34  ? 44.804 -14.721 -8.750  1.00 11.55 ?  34  VAL   B CA   1 
ATOM   4599 C C    . VAL   B 1 34  ? 45.227 -16.171 -8.578  1.00 10.61 ?  34  VAL   B C    1 
ATOM   4600 O O    . VAL   B 1 34  ? 44.708 -17.056 -9.268  1.00 11.00 ?  34  VAL   B O    1 
ATOM   4601 C CB   . VAL   B 1 34  ? 43.336 -14.563 -8.301  1.00 13.06 ?  34  VAL   B CB   1 
ATOM   4602 C CG1  . VAL   B 1 34  ? 43.175 -15.022 -6.857  1.00 12.86 ?  34  VAL   B CG1  1 
ATOM   4603 C CG2  . VAL   B 1 34  ? 42.855 -13.131 -8.482  1.00 14.22 ?  34  VAL   B CG2  1 
ATOM   4604 H H    . VAL   B 1 34  ? 44.722 -14.910 -10.711 1.00 14.22 ?  34  VAL   B H    1 
ATOM   4605 H HA   . VAL   B 1 34  ? 45.364 -14.175 -8.177  1.00 13.86 ?  34  VAL   B HA   1 
ATOM   4606 H HB   . VAL   B 1 34  ? 42.782 -15.129 -8.860  1.00 15.67 ?  34  VAL   B HB   1 
ATOM   4607 H HG11 . VAL   B 1 34  ? 42.330 -14.689 -6.513  1.00 15.44 ?  34  VAL   B HG11 1 
ATOM   4608 H HG12 . VAL   B 1 34  ? 43.181 -15.992 -6.827  1.00 15.44 ?  34  VAL   B HG12 1 
ATOM   4609 H HG13 . VAL   B 1 34  ? 43.906 -14.668 -6.326  1.00 15.44 ?  34  VAL   B HG13 1 
ATOM   4610 H HG21 . VAL   B 1 34  ? 41.937 -13.065 -8.174  1.00 17.06 ?  34  VAL   B HG21 1 
ATOM   4611 H HG22 . VAL   B 1 34  ? 43.421 -12.536 -7.969  1.00 17.06 ?  34  VAL   B HG22 1 
ATOM   4612 H HG23 . VAL   B 1 34  ? 42.900 -12.896 -9.426  1.00 17.06 ?  34  VAL   B HG23 1 
ATOM   4613 N N    . VAL   B 1 35  ? 46.128 -16.419 -7.630  1.00 10.07 ?  35  VAL   B N    1 
ATOM   4614 C CA   . VAL   B 1 35  ? 46.360 -17.760 -7.111  1.00 9.85  ?  35  VAL   B CA   1 
ATOM   4615 C C    . VAL   B 1 35  ? 45.816 -17.812 -5.692  1.00 9.66  ?  35  VAL   B C    1 
ATOM   4616 O O    . VAL   B 1 35  ? 46.036 -16.890 -4.898  1.00 9.97  ?  35  VAL   B O    1 
ATOM   4617 C CB   . VAL   B 1 35  ? 47.839 -18.207 -7.198  1.00 10.59 ?  35  VAL   B CB   1 
ATOM   4618 C CG1  . VAL   B 1 35  ? 48.758 -17.369 -6.302  1.00 11.67 ?  35  VAL   B CG1  1 
ATOM   4619 C CG2  . VAL   B 1 35  ? 47.959 -19.698 -6.868  1.00 11.24 ?  35  VAL   B CG2  1 
ATOM   4620 H H    . VAL   B 1 35  ? 46.630 -15.814 -7.272  1.00 12.08 ?  35  VAL   B H    1 
ATOM   4621 H HA   . VAL   B 1 35  ? 45.843 -18.384 -7.638  1.00 11.82 ?  35  VAL   B HA   1 
ATOM   4622 H HB   . VAL   B 1 35  ? 48.140 -18.094 -8.116  1.00 12.71 ?  35  VAL   B HB   1 
ATOM   4623 H HG11 . VAL   B 1 35  ? 49.677 -17.630 -6.473  1.00 14.00 ?  35  VAL   B HG11 1 
ATOM   4624 H HG12 . VAL   B 1 35  ? 48.628 -16.437 -6.510  1.00 14.00 ?  35  VAL   B HG12 1 
ATOM   4625 H HG13 . VAL   B 1 35  ? 48.531 -17.545 -5.376  1.00 14.00 ?  35  VAL   B HG13 1 
ATOM   4626 H HG21 . VAL   B 1 35  ? 48.875 -19.984 -6.982  1.00 13.49 ?  35  VAL   B HG21 1 
ATOM   4627 H HG22 . VAL   B 1 35  ? 47.680 -19.844 -5.945  1.00 13.49 ?  35  VAL   B HG22 1 
ATOM   4628 H HG23 . VAL   B 1 35  ? 47.377 -20.208 -7.461  1.00 13.49 ?  35  VAL   B HG23 1 
ATOM   4629 N N    . VAL   B 1 36  ? 45.094 -18.888 -5.376  1.00 9.68  ?  36  VAL   B N    1 
ATOM   4630 C CA   . VAL   B 1 36  ? 44.544 -19.085 -4.042  1.00 9.28  ?  36  VAL   B CA   1 
ATOM   4631 C C    . VAL   B 1 36  ? 45.550 -19.844 -3.186  1.00 9.18  ?  36  VAL   B C    1 
ATOM   4632 O O    . VAL   B 1 36  ? 46.093 -20.878 -3.606  1.00 10.00 ?  36  VAL   B O    1 
ATOM   4633 C CB   . VAL   B 1 36  ? 43.209 -19.847 -4.110  1.00 9.66  ?  36  VAL   B CB   1 
ATOM   4634 C CG1  . VAL   B 1 36  ? 42.708 -20.213 -2.722  1.00 10.52 ?  36  VAL   B CG1  1 
ATOM   4635 C CG2  . VAL   B 1 36  ? 42.182 -19.027 -4.865  1.00 10.41 ?  36  VAL   B CG2  1 
ATOM   4636 H H    . VAL   B 1 36  ? 44.910 -19.526 -5.925  1.00 11.61 ?  36  VAL   B H    1 
ATOM   4637 H HA   . VAL   B 1 36  ? 44.383 -18.225 -3.629  1.00 11.14 ?  36  VAL   B HA   1 
ATOM   4638 H HB   . VAL   B 1 36  ? 43.342 -20.670 -4.603  1.00 11.59 ?  36  VAL   B HB   1 
ATOM   4639 H HG11 . VAL   B 1 36  ? 41.767 -20.448 -2.775  1.00 12.62 ?  36  VAL   B HG11 1 
ATOM   4640 H HG12 . VAL   B 1 36  ? 43.217 -20.965 -2.386  1.00 12.62 ?  36  VAL   B HG12 1 
ATOM   4641 H HG13 . VAL   B 1 36  ? 42.818 -19.447 -2.133  1.00 12.62 ?  36  VAL   B HG13 1 
ATOM   4642 H HG21 . VAL   B 1 36  ? 41.339 -19.512 -4.881  1.00 12.49 ?  36  VAL   B HG21 1 
ATOM   4643 H HG22 . VAL   B 1 36  ? 42.065 -18.175 -4.424  1.00 12.49 ?  36  VAL   B HG22 1 
ATOM   4644 H HG23 . VAL   B 1 36  ? 42.494 -18.889 -5.777  1.00 12.49 ?  36  VAL   B HG23 1 
ATOM   4645 N N    . ASN   B 1 37  ? 45.766 -19.355 -1.972  1.00 9.08  ?  37  ASN   B N    1 
ATOM   4646 C CA   . ASN   B 1 37  ? 46.519 -20.079 -0.967  1.00 9.53  ?  37  ASN   B CA   1 
ATOM   4647 C C    . ASN   B 1 37  ? 45.572 -20.745 0.020   1.00 9.69  ?  37  ASN   B C    1 
ATOM   4648 O O    . ASN   B 1 37  ? 44.562 -20.160 0.426   1.00 10.30 ?  37  ASN   B O    1 
ATOM   4649 C CB   . ASN   B 1 37  ? 47.446 -19.135 -0.209  1.00 9.36  ?  37  ASN   B CB   1 
ATOM   4650 C CG   . ASN   B 1 37  ? 48.290 -19.847 0.811   1.00 10.03 ?  37  ASN   B CG   1 
ATOM   4651 O OD1  . ASN   B 1 37  ? 48.627 -21.022 0.641   1.00 10.59 ?  37  ASN   B OD1  1 
ATOM   4652 N ND2  . ASN   B 1 37  ? 48.636 -19.143 1.886   1.00 10.06 ?  37  ASN   B ND2  1 
ATOM   4653 H H    . ASN   B 1 37  ? 45.481 -18.594 -1.699  1.00 10.89 ?  37  ASN   B H    1 
ATOM   4654 H HA   . ASN   B 1 37  ? 47.057 -20.774 -1.381  1.00 11.44 ?  37  ASN   B HA   1 
ATOM   4655 H HB2  . ASN   B 1 37  ? 48.041 -18.708 -0.835  1.00 11.24 ?  37  ASN   B HB2  1 
ATOM   4656 H HB3  . ASN   B 1 37  ? 46.912 -18.473 0.259   1.00 11.24 ?  37  ASN   B HB3  1 
ATOM   4657 H HD21 . ASN   B 1 37  ? 49.124 -19.507 2.498   1.00 12.08 ?  37  ASN   B HD21 1 
ATOM   4658 H HD22 . ASN   B 1 37  ? 48.382 -18.333 1.975   1.00 12.08 ?  37  ASN   B HD22 1 
ATOM   4659 N N    . ALA   B 1 38  ? 45.913 -21.979 0.400   1.00 9.96  ?  38  ALA   B N    1 
ATOM   4660 C CA   . ALA   B 1 38  ? 45.257 -22.709 1.483   1.00 10.24 ?  38  ALA   B CA   1 
ATOM   4661 C C    . ALA   B 1 38  ? 45.850 -22.223 2.804   1.00 10.26 ?  38  ALA   B C    1 
ATOM   4662 O O    . ALA   B 1 38  ? 46.749 -22.841 3.393   1.00 11.23 ?  38  ALA   B O    1 
ATOM   4663 C CB   . ALA   B 1 38  ? 45.470 -24.206 1.307   1.00 11.59 ?  38  ALA   B CB   1 
ATOM   4664 H H    . ALA   B 1 38  ? 46.556 -22.422 0.043   1.00 11.96 ?  38  ALA   B H    1 
ATOM   4665 H HA   . ALA   B 1 38  ? 44.302 -22.522 1.477   1.00 12.29 ?  38  ALA   B HA   1 
ATOM   4666 H HB1  . ALA   B 1 38  ? 45.022 -24.675 2.035   1.00 13.91 ?  38  ALA   B HB1  1 
ATOM   4667 H HB2  . ALA   B 1 38  ? 45.086 -24.480 0.460   1.00 13.91 ?  38  ALA   B HB2  1 
ATOM   4668 H HB3  . ALA   B 1 38  ? 46.415 -24.396 1.326   1.00 13.91 ?  38  ALA   B HB3  1 
ATOM   4669 N N    . ALA   B 1 39  ? 45.335 -21.081 3.265   1.00 10.16 ?  39  ALA   B N    1 
ATOM   4670 C CA   . ALA   B 1 39  ? 45.887 -20.346 4.392   1.00 10.70 ?  39  ALA   B CA   1 
ATOM   4671 C C    . ALA   B 1 39  ? 45.273 -20.792 5.715   1.00 10.51 ?  39  ALA   B C    1 
ATOM   4672 O O    . ALA   B 1 39  ? 44.236 -21.455 5.765   1.00 11.35 ?  39  ALA   B O    1 
ATOM   4673 C CB   . ALA   B 1 39  ? 45.636 -18.848 4.199   1.00 10.94 ?  39  ALA   B CB   1 
ATOM   4674 H H    . ALA   B 1 39  ? 44.633 -20.705 2.926   1.00 12.19 ?  39  ALA   B H    1 
ATOM   4675 H HA   . ALA   B 1 39  ? 46.840 -20.495 4.433   1.00 12.85 ?  39  ALA   B HA   1 
ATOM   4676 H HB1  . ALA   B 1 39  ? 46.012 -18.365 4.955   1.00 13.13 ?  39  ALA   B HB1  1 
ATOM   4677 H HB2  . ALA   B 1 39  ? 46.066 -18.557 3.379   1.00 13.13 ?  39  ALA   B HB2  1 
ATOM   4678 H HB3  . ALA   B 1 39  ? 44.681 -18.686 4.148   1.00 13.13 ?  39  ALA   B HB3  1 
ATOM   4679 N N    . ASN   B 1 40  ? 45.916 -20.372 6.802   1.00 11.30 ?  40  ASN   B N    1 
ATOM   4680 C CA   . ASN   B 1 40  ? 45.348 -20.409 8.139   1.00 12.26 ?  40  ASN   B CA   1 
ATOM   4681 C C    . ASN   B 1 40  ? 45.171 -18.978 8.655   1.00 11.64 ?  40  ASN   B C    1 
ATOM   4682 O O    . ASN   B 1 40  ? 45.587 -18.001 8.018   1.00 11.45 ?  40  ASN   B O    1 
ATOM   4683 C CB   . ASN   B 1 40  ? 46.193 -21.281 9.082   1.00 13.14 ?  40  ASN   B CB   1 
ATOM   4684 C CG   . ASN   B 1 40  ? 47.648 -20.873 9.115   1.00 14.17 ?  40  ASN   B CG   1 
ATOM   4685 O OD1  . ASN   B 1 40  ? 47.971 -19.689 9.195   1.00 16.27 ?  40  ASN   B OD1  1 
ATOM   4686 N ND2  . ASN   B 1 40  ? 48.541 -21.855 9.061   1.00 14.51 ?  40  ASN   B ND2  1 
ATOM   4687 H H    . ASN   B 1 40  ? 46.713 -20.049 6.781   1.00 13.56 ?  40  ASN   B H    1 
ATOM   4688 H HA   . ASN   B 1 40  ? 44.462 -20.802 8.088   1.00 14.71 ?  40  ASN   B HA   1 
ATOM   4689 H HB2  . ASN   B 1 40  ? 45.834 -21.200 9.981   1.00 15.77 ?  40  ASN   B HB2  1 
ATOM   4690 H HB3  . ASN   B 1 40  ? 46.136 -22.199 8.784   1.00 15.77 ?  40  ASN   B HB3  1 
ATOM   4691 H HD21 . ASN   B 1 40  ? 49.379 -21.679 9.082   1.00 17.41 ?  40  ASN   B HD21 1 
ATOM   4692 H HD22 . ASN   B 1 40  ? 48.273 -22.674 9.007   1.00 17.41 ?  40  ASN   B HD22 1 
ATOM   4693 N N    . VAL   B 1 41  ? 44.518 -18.850 9.811   1.00 11.77 ?  41  VAL   B N    1 
ATOM   4694 C CA   . VAL   B 1 41  ? 44.060 -17.525 10.249  1.00 12.43 ?  41  VAL   B CA   1 
ATOM   4695 C C    . VAL   B 1 41  ? 45.214 -16.574 10.542  1.00 12.14 ?  41  VAL   B C    1 
ATOM   4696 O O    . VAL   B 1 41  ? 45.040 -15.351 10.458  1.00 12.69 ?  41  VAL   B O    1 
ATOM   4697 C CB   . VAL   B 1 41  ? 43.089 -17.591 11.445  1.00 14.16 ?  41  VAL   B CB   1 
ATOM   4698 C CG1  . VAL   B 1 41  ? 41.771 -18.259 11.053  1.00 14.84 ?  41  VAL   B CG1  1 
ATOM   4699 C CG2  . VAL   B 1 41  ? 43.734 -18.264 12.646  1.00 15.20 ?  41  VAL   B CG2  1 
ATOM   4700 H H    . VAL   B 1 41  ? 44.319 -19.489 10.342  1.00 14.13 ?  41  VAL   B H    1 
ATOM   4701 H HA   . VAL   B 1 41  ? 43.558 -17.127 9.519   1.00 14.92 ?  41  VAL   B HA   1 
ATOM   4702 H HB   . VAL   B 1 41  ? 42.868 -16.683 11.715  1.00 17.00 ?  41  VAL   B HB   1 
ATOM   4703 H HG11 . VAL   B 1 41  ? 41.171 -18.256 11.819  1.00 17.81 ?  41  VAL   B HG11 1 
ATOM   4704 H HG12 . VAL   B 1 41  ? 41.370 -17.762 10.321  1.00 17.81 ?  41  VAL   B HG12 1 
ATOM   4705 H HG13 . VAL   B 1 41  ? 41.949 -19.170 10.777  1.00 17.81 ?  41  VAL   B HG13 1 
ATOM   4706 H HG21 . VAL   B 1 41  ? 43.092 -18.302 13.372  1.00 18.24 ?  41  VAL   B HG21 1 
ATOM   4707 H HG22 . VAL   B 1 41  ? 44.002 -19.163 12.396  1.00 18.24 ?  41  VAL   B HG22 1 
ATOM   4708 H HG23 . VAL   B 1 41  ? 44.509 -17.750 12.915  1.00 18.24 ?  41  VAL   B HG23 1 
ATOM   4709 N N    . TYR   B 1 42  ? 46.382 -17.095 10.914  1.00 12.89 ?  42  TYR   B N    1 
ATOM   4710 C CA   . TYR   B 1 42  ? 47.533 -16.248 11.190  1.00 13.07 ?  42  TYR   B CA   1 
ATOM   4711 C C    . TYR   B 1 42  ? 48.495 -16.167 10.010  1.00 12.46 ?  42  TYR   B C    1 
ATOM   4712 O O    . TYR   B 1 42  ? 49.582 -15.593 10.148  1.00 13.77 ?  42  TYR   B O    1 
ATOM   4713 C CB   . TYR   B 1 42  ? 48.223 -16.656 12.496  1.00 15.39 ?  42  TYR   B CB   1 
ATOM   4714 C CG   . TYR   B 1 42  ? 47.623 -15.964 13.716  1.00 15.59 ?  42  TYR   B CG   1 
ATOM   4715 C CD1  . TYR   B 1 42  ? 47.841 -14.608 13.936  1.00 14.69 ?  42  TYR   B CD1  1 
ATOM   4716 C CD2  . TYR   B 1 42  ? 46.849 -16.654 14.640  1.00 17.03 ?  42  TYR   B CD2  1 
ATOM   4717 C CE1  . TYR   B 1 42  ? 47.304 -13.961 15.024  1.00 15.24 ?  42  TYR   B CE1  1 
ATOM   4718 C CE2  . TYR   B 1 42  ? 46.309 -16.009 15.745  1.00 16.86 ?  42  TYR   B CE2  1 
ATOM   4719 C CZ   . TYR   B 1 42  ? 46.544 -14.657 15.934  1.00 17.10 ?  42  TYR   B CZ   1 
ATOM   4720 O OH   . TYR   B 1 42  ? 46.022 -13.994 17.028  1.00 20.53 ?  42  TYR   B OH   1 
ATOM   4721 H H    . TYR   B 1 42  ? 46.529 -17.939 11.009  1.00 15.47 ?  42  TYR   B H    1 
ATOM   4722 H HA   . TYR   B 1 42  ? 47.204 -15.349 11.326  1.00 15.68 ?  42  TYR   B HA   1 
ATOM   4723 H HB2  . TYR   B 1 42  ? 48.133 -17.613 12.616  1.00 18.47 ?  42  TYR   B HB2  1 
ATOM   4724 H HB3  . TYR   B 1 42  ? 49.162 -16.415 12.442  1.00 18.47 ?  42  TYR   B HB3  1 
ATOM   4725 H HD1  . TYR   B 1 42  ? 48.358 -14.127 13.324  1.00 17.63 ?  42  TYR   B HD1  1 
ATOM   4726 H HD2  . TYR   B 1 42  ? 46.687 -17.564 14.511  1.00 20.44 ?  42  TYR   B HD2  1 
ATOM   4727 H HE1  . TYR   B 1 42  ? 47.467 -13.053 15.152  1.00 18.29 ?  42  TYR   B HE1  1 
ATOM   4728 H HE2  . TYR   B 1 42  ? 45.789 -16.483 16.355  1.00 20.24 ?  42  TYR   B HE2  1 
ATOM   4729 H HH   . TYR   B 1 42  ? 46.246 -13.187 17.001  1.00 24.64 ?  42  TYR   B HH   1 
ATOM   4730 N N    . LEU   B 1 43  ? 48.099 -16.687 8.851   1.00 11.42 ?  43  LEU   B N    1 
ATOM   4731 C CA   . LEU   B 1 43  ? 48.911 -16.626 7.639   1.00 11.19 ?  43  LEU   B CA   1 
ATOM   4732 C C    . LEU   B 1 43  ? 50.325 -17.135 7.897   1.00 11.33 ?  43  LEU   B C    1 
ATOM   4733 O O    . LEU   B 1 43  ? 51.306 -16.547 7.444   1.00 12.26 ?  43  LEU   B O    1 
ATOM   4734 C CB   . LEU   B 1 43  ? 48.925 -15.224 7.026   1.00 11.41 ?  43  LEU   B CB   1 
ATOM   4735 C CG   . LEU   B 1 43  ? 47.569 -14.613 6.667   1.00 11.81 ?  43  LEU   B CG   1 
ATOM   4736 C CD1  . LEU   B 1 43  ? 47.779 -13.214 6.107   1.00 13.58 ?  43  LEU   B CD1  1 
ATOM   4737 C CD2  . LEU   B 1 43  ? 46.800 -15.481 5.686   1.00 11.59 ?  43  LEU   B CD2  1 
ATOM   4738 H H    . LEU   B 1 43  ? 47.355 -17.105 8.740   1.00 13.71 ?  43  LEU   B H    1 
ATOM   4739 H HA   . LEU   B 1 43  ? 48.512 -17.223 6.980   1.00 13.43 ?  43  LEU   B HA   1 
ATOM   4740 H HB2  . LEU   B 1 43  ? 49.352 -14.627 7.654   1.00 13.69 ?  43  LEU   B HB2  1 
ATOM   4741 H HB3  . LEU   B 1 43  ? 49.448 -15.262 6.208   1.00 13.69 ?  43  LEU   B HB3  1 
ATOM   4742 H HG   . LEU   B 1 43  ? 47.039 -14.544 7.471   1.00 14.17 ?  43  LEU   B HG   1 
ATOM   4743 H HD11 . LEU   B 1 43  ? 46.913 -12.832 5.882   1.00 16.29 ?  43  LEU   B HD11 1 
ATOM   4744 H HD12 . LEU   B 1 43  ? 48.211 -12.667 6.783   1.00 16.29 ?  43  LEU   B HD12 1 
ATOM   4745 H HD13 . LEU   B 1 43  ? 48.334 -13.263 5.315   1.00 16.29 ?  43  LEU   B HD13 1 
ATOM   4746 H HD21 . LEU   B 1 43  ? 45.989 -15.019 5.422   1.00 13.90 ?  43  LEU   B HD21 1 
ATOM   4747 H HD22 . LEU   B 1 43  ? 47.353 -15.649 4.904   1.00 13.90 ?  43  LEU   B HD22 1 
ATOM   4748 H HD23 . LEU   B 1 43  ? 46.574 -16.325 6.112   1.00 13.90 ?  43  LEU   B HD23 1 
ATOM   4749 N N    . LYS   B 1 44  ? 50.426 -18.253 8.616   1.00 11.48 ?  44  LYS   B N    1 
ATOM   4750 C CA   . LYS   B 1 44  ? 51.691 -18.936 8.855   1.00 12.06 ?  44  LYS   B CA   1 
ATOM   4751 C C    . LYS   B 1 44  ? 51.808 -20.056 7.834   1.00 11.72 ?  44  LYS   B C    1 
ATOM   4752 O O    . LYS   B 1 44  ? 51.108 -21.072 7.926   1.00 13.45 ?  44  LYS   B O    1 
ATOM   4753 C CB   . LYS   B 1 44  ? 51.742 -19.453 10.290  1.00 14.02 ?  44  LYS   B CB   1 
ATOM   4754 C CG   . LYS   B 1 44  ? 51.941 -18.333 11.308  1.00 17.31 ?  44  LYS   B CG   1 
ATOM   4755 C CD   . LYS   B 1 44  ? 53.195 -17.533 10.939  1.00 21.44 ?  44  LYS   B CD   1 
ATOM   4756 C CE   . LYS   B 1 44  ? 53.613 -16.540 11.985  1.00 24.51 ?  44  LYS   B CE   1 
ATOM   4757 N NZ   . LYS   B 1 44  ? 54.846 -15.807 11.602  1.00 25.89 ?  44  LYS   B NZ   1 
ATOM   4758 H H    . LYS   B 1 44  ? 49.754 -18.639 8.987   1.00 13.77 ?  44  LYS   B H    1 
ATOM   4759 H HA   . LYS   B 1 44  ? 52.424 -18.329 8.689   1.00 14.47 ?  44  LYS   B HA   1 
ATOM   4760 H HB2  . LYS   B 1 44  ? 50.899 -19.901 10.494  1.00 16.82 ?  44  LYS   B HB2  1 
ATOM   4761 H HB3  . LYS   B 1 44  ? 52.474 -20.081 10.377  1.00 16.82 ?  44  LYS   B HB3  1 
ATOM   4762 H HG2  . LYS   B 1 44  ? 51.177 -17.742 11.298  1.00 20.77 ?  44  LYS   B HG2  1 
ATOM   4763 H HG3  . LYS   B 1 44  ? 52.069 -18.719 12.192  1.00 20.77 ?  44  LYS   B HG3  1 
ATOM   4764 H HD2  . LYS   B 1 44  ? 53.927 -18.159 10.781  1.00 25.72 ?  44  LYS   B HD2  1 
ATOM   4765 H HD3  . LYS   B 1 44  ? 53.016 -17.030 10.130  1.00 25.72 ?  44  LYS   B HD3  1 
ATOM   4766 H HE2  . LYS   B 1 44  ? 52.903 -15.892 12.089  1.00 29.42 ?  44  LYS   B HE2  1 
ATOM   4767 H HE3  . LYS   B 1 44  ? 53.784 -17.010 12.813  1.00 29.42 ?  44  LYS   B HE3  1 
ATOM   4768 H HZ1  . LYS   B 1 44  ? 55.061 -15.225 12.241  1.00 31.07 ?  44  LYS   B HZ1  1 
ATOM   4769 H HZ2  . LYS   B 1 44  ? 55.520 -16.376 11.489  1.00 31.07 ?  44  LYS   B HZ2  1 
ATOM   4770 H HZ3  . LYS   B 1 44  ? 54.713 -15.361 10.841  1.00 31.07 ?  44  LYS   B HZ3  1 
ATOM   4771 N N    . HIS   B 1 45  ? 52.661 -19.848 6.833   1.00 11.57 ?  45  HIS   B N    1 
ATOM   4772 C CA   . HIS   B 1 45  ? 52.672 -20.683 5.634   1.00 11.70 ?  45  HIS   B CA   1 
ATOM   4773 C C    . HIS   B 1 45  ? 53.684 -21.813 5.794   1.00 13.78 ?  45  HIS   B C    1 
ATOM   4774 O O    . HIS   B 1 45  ? 54.750 -21.838 5.183   1.00 16.70 ?  45  HIS   B O    1 
ATOM   4775 C CB   . HIS   B 1 45  ? 52.990 -19.834 4.415   1.00 11.60 ?  45  HIS   B CB   1 
ATOM   4776 C CG   . HIS   B 1 45  ? 52.128 -18.624 4.307   1.00 11.38 ?  45  HIS   B CG   1 
ATOM   4777 N ND1  . HIS   B 1 45  ? 50.749 -18.692 4.282   1.00 11.65 ?  45  HIS   B ND1  1 
ATOM   4778 C CD2  . HIS   B 1 45  ? 52.453 -17.314 4.217   1.00 12.42 ?  45  HIS   B CD2  1 
ATOM   4779 C CE1  . HIS   B 1 45  ? 50.269 -17.466 4.179   1.00 11.52 ?  45  HIS   B CE1  1 
ATOM   4780 N NE2  . HIS   B 1 45  ? 51.278 -16.613 4.136   1.00 12.28 ?  45  HIS   B NE2  1 
ATOM   4781 H H    . HIS   B 1 45  ? 53.232 -19.203 6.811   1.00 13.89 ?  45  HIS   B H    1 
ATOM   4782 H HA   . HIS   B 1 45  ? 51.789 -21.074 5.504   1.00 14.05 ?  45  HIS   B HA   1 
ATOM   4783 H HB2  . HIS   B 1 45  ? 53.911 -19.544 4.459   1.00 13.93 ?  45  HIS   B HB2  1 
ATOM   4784 H HB3  . HIS   B 1 45  ? 52.853 -20.371 3.610   1.00 13.93 ?  45  HIS   B HB3  1 
ATOM   4785 H HD2  . HIS   B 1 45  ? 53.313 -16.953 4.213   1.00 14.90 ?  45  HIS   B HD2  1 
ATOM   4786 H HE1  . HIS   B 1 45  ? 49.368 -17.241 4.134   1.00 13.83 ?  45  HIS   B HE1  1 
ATOM   4787 H HE2  . HIS   B 1 45  ? 51.207 -15.756 4.077   1.00 14.73 ?  45  HIS   B HE2  1 
ATOM   4788 N N    A GLY   B 1 46  ? 53.311 -22.779 6.628   0.42 15.15 ?  46  GLY   B N    1 
ATOM   4789 N N    B GLY   B 1 46  ? 53.322 -22.766 6.642   0.58 14.96 ?  46  GLY   B N    1 
ATOM   4790 C CA   A GLY   B 1 46  ? 54.237 -23.821 7.027   0.42 16.93 ?  46  GLY   B CA   1 
ATOM   4791 C CA   B GLY   B 1 46  ? 54.247 -23.822 6.997   0.58 16.80 ?  46  GLY   B CA   1 
ATOM   4792 C C    A GLY   B 1 46  ? 54.295 -25.059 6.152   0.42 18.36 ?  46  GLY   B C    1 
ATOM   4793 C C    B GLY   B 1 46  ? 54.288 -24.991 6.031   0.58 18.37 ?  46  GLY   B C    1 
ATOM   4794 O O    A GLY   B 1 46  ? 55.386 -25.522 5.803   0.42 20.52 ?  46  GLY   B O    1 
ATOM   4795 O O    B GLY   B 1 46  ? 55.342 -25.314 5.474   0.58 20.81 ?  46  GLY   B O    1 
ATOM   4796 H H    A GLY   B 1 46  ? 52.528 -22.837 6.985   0.42 18.18 ?  46  GLY   B H    1 
ATOM   4797 H H    B GLY   B 1 46  ? 52.551 -22.810 7.029   0.58 17.96 ?  46  GLY   B H    1 
ATOM   4798 H HA2  A GLY   B 1 46  ? 55.128 -23.441 7.065   0.42 20.32 ?  46  GLY   B HA2  1 
ATOM   4799 H HA2  B GLY   B 1 46  ? 55.140 -23.447 7.056   0.58 20.16 ?  46  GLY   B HA2  1 
ATOM   4800 H HA3  A GLY   B 1 46  ? 54.001 -24.116 7.918   0.42 20.32 ?  46  GLY   B HA3  1 
ATOM   4801 H HA3  B GLY   B 1 46  ? 54.008 -24.160 7.875   0.58 20.16 ?  46  GLY   B HA3  1 
ATOM   4802 N N    . GLY   B 1 47  ? 53.142 -25.631 5.810   1.00 18.09 ?  47  GLY   B N    1 
ATOM   4803 C CA   . GLY   B 1 47  ? 53.095 -26.906 5.120   1.00 15.75 ?  47  GLY   B CA   1 
ATOM   4804 C C    . GLY   B 1 47  ? 52.170 -26.882 3.919   1.00 13.92 ?  47  GLY   B C    1 
ATOM   4805 O O    . GLY   B 1 47  ? 51.516 -25.881 3.632   1.00 13.92 ?  47  GLY   B O    1 
ATOM   4806 H H    A GLY   B 1 47  ? 52.368 -25.303 5.989   0.42 21.71 ?  47  GLY   B H    1 
ATOM   4807 H H    B GLY   B 1 47  ? 52.371 -25.338 6.055   0.58 21.71 ?  47  GLY   B H    1 
ATOM   4808 H HA2  . GLY   B 1 47  ? 53.981 -27.149 4.811   1.00 18.90 ?  47  GLY   B HA2  1 
ATOM   4809 H HA3  . GLY   B 1 47  ? 52.789 -27.592 5.736   1.00 18.90 ?  47  GLY   B HA3  1 
ATOM   4810 N N    . GLY   B 1 48  ? 52.115 -28.026 3.239   1.00 13.23 ?  48  GLY   B N    1 
ATOM   4811 C CA   . GLY   B 1 48  ? 51.194 -28.177 2.130   1.00 12.92 ?  48  GLY   B CA   1 
ATOM   4812 C C    . GLY   B 1 48  ? 51.333 -27.072 1.109   1.00 11.96 ?  48  GLY   B C    1 
ATOM   4813 O O    . GLY   B 1 48  ? 52.437 -26.612 0.798   1.00 12.59 ?  48  GLY   B O    1 
ATOM   4814 H H    . GLY   B 1 48  ? 52.599 -28.716 3.399   1.00 15.87 ?  48  GLY   B H    1 
ATOM   4815 H HA2  . GLY   B 1 48  ? 51.356 -29.030 1.688   1.00 15.50 ?  48  GLY   B HA2  1 
ATOM   4816 H HA3  . GLY   B 1 48  ? 50.281 -28.175 2.457   1.00 15.50 ?  48  GLY   B HA3  1 
ATOM   4817 N N    . VAL   B 1 49  ? 50.188 -26.638 0.578   1.00 12.10 ?  49  VAL   B N    1 
ATOM   4818 C CA   . VAL   B 1 49  ? 50.173 -25.613 -0.463  1.00 11.88 ?  49  VAL   B CA   1 
ATOM   4819 C C    . VAL   B 1 49  ? 50.836 -24.326 0.023   1.00 11.02 ?  49  VAL   B C    1 
ATOM   4820 O O    . VAL   B 1 49  ? 51.622 -23.703 -0.700  1.00 11.64 ?  49  VAL   B O    1 
ATOM   4821 C CB   . VAL   B 1 49  ? 48.729 -25.359 -0.938  1.00 13.33 ?  49  VAL   B CB   1 
ATOM   4822 C CG1  . VAL   B 1 49  ? 48.650 -24.098 -1.796  1.00 13.55 ?  49  VAL   B CG1  1 
ATOM   4823 C CG2  . VAL   B 1 49  ? 48.197 -26.565 -1.693  1.00 15.22 ?  49  VAL   B CG2  1 
ATOM   4824 H H    . VAL   B 1 49  ? 49.406 -26.914 0.805   1.00 14.53 ?  49  VAL   B H    1 
ATOM   4825 H HA   . VAL   B 1 49  ? 50.675 -25.935 -1.228  1.00 14.26 ?  49  VAL   B HA   1 
ATOM   4826 H HB   . VAL   B 1 49  ? 48.163 -25.223 -0.165  1.00 15.99 ?  49  VAL   B HB   1 
ATOM   4827 H HG11 . VAL   B 1 49  ? 47.817 -24.110 -2.299  1.00 16.26 ?  49  VAL   B HG11 1 
ATOM   4828 H HG12 . VAL   B 1 49  ? 48.669 -23.317 -1.219  1.00 16.26 ?  49  VAL   B HG12 1 
ATOM   4829 H HG13 . VAL   B 1 49  ? 49.400 -24.080 -2.408  1.00 16.26 ?  49  VAL   B HG13 1 
ATOM   4830 H HG21 . VAL   B 1 49  ? 47.287 -26.386 -1.984  1.00 18.26 ?  49  VAL   B HG21 1 
ATOM   4831 H HG22 . VAL   B 1 49  ? 48.761 -26.731 -2.467  1.00 18.26 ?  49  VAL   B HG22 1 
ATOM   4832 H HG23 . VAL   B 1 49  ? 48.209 -27.337 -1.106  1.00 18.26 ?  49  VAL   B HG23 1 
ATOM   4833 N N    . ALA   B 1 50  ? 50.495 -23.883 1.231   1.00 10.74 ?  50  ALA   B N    1 
ATOM   4834 C CA   . ALA   B 1 50  ? 51.011 -22.602 1.704   1.00 10.61 ?  50  ALA   B CA   1 
ATOM   4835 C C    . ALA   B 1 50  ? 52.529 -22.634 1.817   1.00 10.78 ?  50  ALA   B C    1 
ATOM   4836 O O    . ALA   B 1 50  ? 53.215 -21.673 1.442   1.00 10.94 ?  50  ALA   B O    1 
ATOM   4837 C CB   . ALA   B 1 50  ? 50.378 -22.252 3.046   1.00 11.05 ?  50  ALA   B CB   1 
ATOM   4838 H H    . ALA   B 1 50  ? 49.978 -24.292 1.782   1.00 12.89 ?  50  ALA   B H    1 
ATOM   4839 H HA   . ALA   B 1 50  ? 50.778 -21.908 1.073   1.00 12.73 ?  50  ALA   B HA   1 
ATOM   4840 H HB1  . ALA   B 1 50  ? 50.727 -21.398 3.352   1.00 13.26 ?  50  ALA   B HB1  1 
ATOM   4841 H HB2  . ALA   B 1 50  ? 49.414 -22.190 2.935   1.00 13.26 ?  50  ALA   B HB2  1 
ATOM   4842 H HB3  . ALA   B 1 50  ? 50.589 -22.944 3.692   1.00 13.26 ?  50  ALA   B HB3  1 
ATOM   4843 N N    . GLY   B 1 51  ? 53.077 -23.727 2.337   1.00 11.62 ?  51  GLY   B N    1 
ATOM   4844 C CA   . GLY   B 1 51  ? 54.523 -23.839 2.404   1.00 12.23 ?  51  GLY   B CA   1 
ATOM   4845 C C    . GLY   B 1 51  ? 55.171 -23.789 1.035   1.00 12.61 ?  51  GLY   B C    1 
ATOM   4846 O O    . GLY   B 1 51  ? 56.219 -23.162 0.856   1.00 13.19 ?  51  GLY   B O    1 
ATOM   4847 H H    . GLY   B 1 51  ? 52.648 -24.406 2.648   1.00 13.95 ?  51  GLY   B H    1 
ATOM   4848 H HA2  . GLY   B 1 51  ? 54.883 -23.114 2.938   1.00 14.67 ?  51  GLY   B HA2  1 
ATOM   4849 H HA3  . GLY   B 1 51  ? 54.768 -24.680 2.827   1.00 14.67 ?  51  GLY   B HA3  1 
ATOM   4850 N N    . ALA   B 1 52  ? 54.565 -24.452 0.051   1.00 11.69 ?  52  ALA   B N    1 
ATOM   4851 C CA   . ALA   B 1 52  ? 55.137 -24.465 -1.288  1.00 12.10 ?  52  ALA   B CA   1 
ATOM   4852 C C    . ALA   B 1 52  ? 55.060 -23.088 -1.940  1.00 11.20 ?  52  ALA   B C    1 
ATOM   4853 O O    . ALA   B 1 52  ? 56.029 -22.637 -2.569  1.00 12.32 ?  52  ALA   B O    1 
ATOM   4854 C CB   . ALA   B 1 52  ? 54.422 -25.507 -2.142  1.00 12.66 ?  52  ALA   B CB   1 
ATOM   4855 H H    . ALA   B 1 52  ? 53.824 -24.886 0.132   1.00 14.03 ?  52  ALA   B H    1 
ATOM   4856 H HA   . ALA   B 1 52  ? 56.072 -24.716 -1.225  1.00 14.52 ?  52  ALA   B HA   1 
ATOM   4857 H HB1  . ALA   B 1 52  ? 54.819 -25.509 -3.030  1.00 15.19 ?  52  ALA   B HB1  1 
ATOM   4858 H HB2  . ALA   B 1 52  ? 54.533 -26.380 -1.732  1.00 15.19 ?  52  ALA   B HB2  1 
ATOM   4859 H HB3  . ALA   B 1 52  ? 53.484 -25.281 -2.198  1.00 15.19 ?  52  ALA   B HB3  1 
ATOM   4860 N N    . LEU   B 1 53  ? 53.910 -22.413 -1.820  1.00 11.10 ?  53  LEU   B N    1 
ATOM   4861 C CA   . LEU   B 1 53  ? 53.796 -21.074 -2.391  1.00 11.31 ?  53  LEU   B CA   1 
ATOM   4862 C C    . LEU   B 1 53  ? 54.802 -20.128 -1.746  1.00 11.53 ?  53  LEU   B C    1 
ATOM   4863 O O    . LEU   B 1 53  ? 55.509 -19.381 -2.436  1.00 12.21 ?  53  LEU   B O    1 
ATOM   4864 C CB   . LEU   B 1 53  ? 52.369 -20.532 -2.232  1.00 11.51 ?  53  LEU   B CB   1 
ATOM   4865 C CG   . LEU   B 1 53  ? 51.237 -21.260 -2.966  1.00 11.79 ?  53  LEU   B CG   1 
ATOM   4866 C CD1  . LEU   B 1 53  ? 49.886 -20.668 -2.605  1.00 13.65 ?  53  LEU   B CD1  1 
ATOM   4867 C CD2  . LEU   B 1 53  ? 51.438 -21.250 -4.488  1.00 13.63 ?  53  LEU   B CD2  1 
ATOM   4868 H H    . LEU   B 1 53  ? 53.204 -22.704 -1.422  1.00 13.32 ?  53  LEU   B H    1 
ATOM   4869 H HA   . LEU   B 1 53  ? 53.998 -21.124 -3.342  1.00 13.57 ?  53  LEU   B HA   1 
ATOM   4870 H HB2  . LEU   B 1 53  ? 52.149 -20.556 -1.291  1.00 13.81 ?  53  LEU   B HB2  1 
ATOM   4871 H HB3  . LEU   B 1 53  ? 52.363 -19.620 -2.545  1.00 13.81 ?  53  LEU   B HB3  1 
ATOM   4872 H HG   . LEU   B 1 53  ? 51.229 -22.190 -2.687  1.00 14.15 ?  53  LEU   B HG   1 
ATOM   4873 H HD11 . LEU   B 1 53  ? 49.190 -21.153 -3.084  1.00 16.38 ?  53  LEU   B HD11 1 
ATOM   4874 H HD12 . LEU   B 1 53  ? 49.749 -20.763 -1.649  1.00 16.38 ?  53  LEU   B HD12 1 
ATOM   4875 H HD13 . LEU   B 1 53  ? 49.871 -19.736 -2.854  1.00 16.38 ?  53  LEU   B HD13 1 
ATOM   4876 H HD21 . LEU   B 1 53  ? 50.757 -21.806 -4.904  1.00 16.35 ?  53  LEU   B HD21 1 
ATOM   4877 H HD22 . LEU   B 1 53  ? 51.356 -20.339 -4.813  1.00 16.35 ?  53  LEU   B HD22 1 
ATOM   4878 H HD23 . LEU   B 1 53  ? 52.317 -21.600 -4.699  1.00 16.35 ?  53  LEU   B HD23 1 
ATOM   4879 N N    . ASN   B 1 54  ? 54.896 -20.155 -0.419  1.00 10.83 ?  54  ASN   B N    1 
ATOM   4880 C CA   . ASN   B 1 54  ? 55.815 -19.245 0.249   1.00 11.58 ?  54  ASN   B CA   1 
ATOM   4881 C C    . ASN   B 1 54  ? 57.262 -19.534 -0.139  1.00 11.95 ?  54  ASN   B C    1 
ATOM   4882 O O    . ASN   B 1 54  ? 58.045 -18.602 -0.377  1.00 12.30 ?  54  ASN   B O    1 
ATOM   4883 C CB   . ASN   B 1 54  ? 55.647 -19.307 1.759   1.00 12.35 ?  54  ASN   B CB   1 
ATOM   4884 C CG   . ASN   B 1 54  ? 56.631 -18.400 2.463   1.00 12.31 ?  54  ASN   B CG   1 
ATOM   4885 O OD1  . ASN   B 1 54  ? 56.649 -17.191 2.218   1.00 12.69 ?  54  ASN   B OD1  1 
ATOM   4886 N ND2  . ASN   B 1 54  ? 57.477 -18.969 3.317   1.00 14.51 ?  54  ASN   B ND2  1 
ATOM   4887 H H    . ASN   B 1 54  ? 54.445 -20.670 0.101   1.00 12.99 ?  54  ASN   B H    1 
ATOM   4888 H HA   . ASN   B 1 54  ? 55.608 -18.337 -0.035  1.00 13.89 ?  54  ASN   B HA   1 
ATOM   4889 H HB2  . ASN   B 1 54  ? 54.751 -19.017 1.994   1.00 14.82 ?  54  ASN   B HB2  1 
ATOM   4890 H HB3  . ASN   B 1 54  ? 55.800 -20.212 2.061   1.00 14.82 ?  54  ASN   B HB3  1 
ATOM   4891 H HD21 . ASN   B 1 54  ? 58.063 -18.492 3.729   1.00 17.41 ?  54  ASN   B HD21 1 
ATOM   4892 H HD22 . ASN   B 1 54  ? 57.446 -19.819 3.454   1.00 17.41 ?  54  ASN   B HD22 1 
ATOM   4893 N N    . LYS   B 1 55  ? 57.638 -20.814 -0.208  1.00 12.61 ?  55  LYS   B N    1 
ATOM   4894 C CA   . LYS   B 1 55  ? 58.991 -21.163 -0.625  1.00 13.94 ?  55  LYS   B CA   1 
ATOM   4895 C C    . LYS   B 1 55  ? 59.295 -20.613 -2.014  1.00 13.55 ?  55  LYS   B C    1 
ATOM   4896 O O    . LYS   B 1 55  ? 60.400 -20.110 -2.262  1.00 14.21 ?  55  LYS   B O    1 
ATOM   4897 C CB   . LYS   B 1 55  ? 59.173 -22.682 -0.575  1.00 15.86 ?  55  LYS   B CB   1 
ATOM   4898 C CG   . LYS   B 1 55  ? 60.550 -23.159 -1.005  1.00 20.23 ?  55  LYS   B CG   1 
ATOM   4899 C CD   . LYS   B 1 55  ? 60.713 -24.664 -0.808  1.00 23.91 ?  55  LYS   B CD   1 
ATOM   4900 C CE   . LYS   B 1 55  ? 60.794 -25.039 0.674   1.00 27.16 ?  55  LYS   B CE   1 
ATOM   4901 N NZ   . LYS   B 1 55  ? 61.202 -26.450 0.884   1.00 29.28 ?  55  LYS   B NZ   1 
ATOM   4902 H H    . LYS   B 1 55  ? 57.133 -21.480 -0.017  1.00 15.13 ?  55  LYS   B H    1 
ATOM   4903 H HA   . LYS   B 1 55  ? 59.620 -20.769 -0.008  1.00 16.73 ?  55  LYS   B HA   1 
ATOM   4904 H HB2  . LYS   B 1 55  ? 59.025 -22.979 0.339   1.00 19.03 ?  55  LYS   B HB2  1 
ATOM   4905 H HB3  . LYS   B 1 55  ? 58.518 -23.097 -1.160  1.00 19.03 ?  55  LYS   B HB3  1 
ATOM   4906 H HG2  . LYS   B 1 55  ? 60.676 -22.961 -1.947  1.00 24.28 ?  55  LYS   B HG2  1 
ATOM   4907 H HG3  . LYS   B 1 55  ? 61.224 -22.706 -0.475  1.00 24.28 ?  55  LYS   B HG3  1 
ATOM   4908 H HD2  . LYS   B 1 55  ? 59.950 -25.124 -1.194  1.00 28.69 ?  55  LYS   B HD2  1 
ATOM   4909 H HD3  . LYS   B 1 55  ? 61.532 -24.958 -1.237  1.00 28.69 ?  55  LYS   B HD3  1 
ATOM   4910 H HE2  . LYS   B 1 55  ? 61.446 -24.462 1.107   1.00 32.60 ?  55  LYS   B HE2  1 
ATOM   4911 H HE3  . LYS   B 1 55  ? 59.920 -24.908 1.079   1.00 32.60 ?  55  LYS   B HE3  1 
ATOM   4912 H HZ1  . LYS   B 1 55  ? 61.209 -26.635 1.755   1.00 35.14 ?  55  LYS   B HZ1  1 
ATOM   4913 H HZ2  . LYS   B 1 55  ? 60.627 -26.993 0.477   1.00 35.14 ?  55  LYS   B HZ2  1 
ATOM   4914 H HZ3  . LYS   B 1 55  ? 62.014 -26.583 0.552   1.00 35.14 ?  55  LYS   B HZ3  1 
ATOM   4915 N N    . ALA   B 1 56  ? 58.329 -20.698 -2.934  1.00 13.11 ?  56  ALA   B N    1 
ATOM   4916 C CA   . ALA   B 1 56  ? 58.553 -20.201 -4.287  1.00 13.58 ?  56  ALA   B CA   1 
ATOM   4917 C C    . ALA   B 1 56  ? 58.830 -18.704 -4.291  1.00 13.12 ?  56  ALA   B C    1 
ATOM   4918 O O    . ALA   B 1 56  ? 59.557 -18.211 -5.165  1.00 14.20 ?  56  ALA   B O    1 
ATOM   4919 C CB   . ALA   B 1 56  ? 57.350 -20.529 -5.176  1.00 14.76 ?  56  ALA   B CB   1 
ATOM   4920 H H    . ALA   B 1 56  ? 57.542 -21.024 -2.801  1.00 15.73 ?  56  ALA   B H    1 
ATOM   4921 H HA   . ALA   B 1 56  ? 59.327 -20.640 -4.660  1.00 16.30 ?  56  ALA   B HA   1 
ATOM   4922 H HB1  . ALA   B 1 56  ? 57.519 -20.193 -6.073  1.00 17.71 ?  56  ALA   B HB1  1 
ATOM   4923 H HB2  . ALA   B 1 56  ? 57.232 -21.490 -5.202  1.00 17.71 ?  56  ALA   B HB2  1 
ATOM   4924 H HB3  . ALA   B 1 56  ? 56.558 -20.106 -4.812  1.00 17.71 ?  56  ALA   B HB3  1 
ATOM   4925 N N    . THR   B 1 57  ? 58.256 -17.965 -3.337  1.00 13.07 ?  57  THR   B N    1 
ATOM   4926 C CA   . THR   B 1 57  ? 58.500 -16.532 -3.218  1.00 13.29 ?  57  THR   B CA   1 
ATOM   4927 C C    . THR   B 1 57  ? 59.748 -16.211 -2.409  1.00 14.04 ?  57  THR   B C    1 
ATOM   4928 O O    . THR   B 1 57  ? 59.982 -15.038 -2.104  1.00 14.24 ?  57  THR   B O    1 
ATOM   4929 C CB   . THR   B 1 57  ? 57.298 -15.803 -2.585  1.00 11.97 ?  57  THR   B CB   1 
ATOM   4930 O OG1  . THR   B 1 57  ? 57.283 -16.001 -1.163  1.00 12.73 ?  57  THR   B OG1  1 
ATOM   4931 C CG2  . THR   B 1 57  ? 55.980 -16.245 -3.212  1.00 12.47 ?  57  THR   B CG2  1 
ATOM   4932 H H    . THR   B 1 57  ? 57.709 -18.273 -2.745  1.00 15.68 ?  57  THR   B H    1 
ATOM   4933 H HA   . THR   B 1 57  ? 58.621 -16.165 -4.107  1.00 15.94 ?  57  THR   B HA   1 
ATOM   4934 H HB   . THR   B 1 57  ? 57.391 -14.851 -2.760  1.00 14.37 ?  57  THR   B HB   1 
ATOM   4935 H HG1  . THR   B 1 57  ? 57.214 -16.819 -0.986  1.00 15.28 ?  57  THR   B HG1  1 
ATOM   4936 H HG21 . THR   B 1 57  ? 55.261 -15.657 -2.936  1.00 14.96 ?  57  THR   B HG21 1 
ATOM   4937 H HG22 . THR   B 1 57  ? 56.046 -16.228 -4.180  1.00 14.96 ?  57  THR   B HG22 1 
ATOM   4938 H HG23 . THR   B 1 57  ? 55.766 -17.150 -2.932  1.00 14.96 ?  57  THR   B HG23 1 
ATOM   4939 N N    . ASN   B 1 58  ? 60.540 -17.212 -2.048  1.00 14.93 ?  58  ASN   B N    1 
ATOM   4940 C CA   . ASN   B 1 58  ? 61.737 -16.994 -1.240  1.00 16.80 ?  58  ASN   B CA   1 
ATOM   4941 C C    . ASN   B 1 58  ? 61.403 -16.282 0.070   1.00 15.00 ?  58  ASN   B C    1 
ATOM   4942 O O    . ASN   B 1 58  ? 62.148 -15.415 0.537   1.00 16.08 ?  58  ASN   B O    1 
ATOM   4943 C CB   . ASN   B 1 58  ? 62.824 -16.246 -2.019  1.00 20.92 ?  58  ASN   B CB   1 
ATOM   4944 C CG   . ASN   B 1 58  ? 64.194 -16.373 -1.375  1.00 28.47 ?  58  ASN   B CG   1 
ATOM   4945 O OD1  . ASN   B 1 58  ? 64.504 -17.387 -0.749  1.00 32.13 ?  58  ASN   B OD1  1 
ATOM   4946 N ND2  . ASN   B 1 58  ? 65.018 -15.341 -1.521  1.00 34.29 ?  58  ASN   B ND2  1 
ATOM   4947 H H    . ASN   B 1 58  ? 60.403 -18.035 -2.256  1.00 17.92 ?  58  ASN   B H    1 
ATOM   4948 H HA   . ASN   B 1 58  ? 62.102 -17.862 -1.016  1.00 20.16 ?  58  ASN   B HA   1 
ATOM   4949 H HB2  . ASN   B 1 58  ? 62.880 -16.609 -2.919  1.00 25.10 ?  58  ASN   B HB2  1 
ATOM   4950 H HB3  . ASN   B 1 58  ? 62.600 -15.304 -2.057  1.00 25.10 ?  58  ASN   B HB3  1 
ATOM   4951 H HD21 . ASN   B 1 58  ? 65.806 -15.366 -1.175  1.00 41.14 ?  58  ASN   B HD21 1 
ATOM   4952 H HD22 . ASN   B 1 58  ? 64.765 -14.648 -1.963  1.00 41.14 ?  58  ASN   B HD22 1 
ATOM   4953 N N    . ASN   B 1 59  ? 60.277 -16.660 0.672   1.00 13.71 ?  59  ASN   B N    1 
ATOM   4954 C CA   . ASN   B 1 59  ? 59.800 -16.183 1.967   1.00 13.79 ?  59  ASN   B CA   1 
ATOM   4955 C C    . ASN   B 1 59  ? 59.209 -14.775 1.907   1.00 13.28 ?  59  ASN   B C    1 
ATOM   4956 O O    . ASN   B 1 59  ? 58.775 -14.266 2.946   1.00 13.59 ?  59  ASN   B O    1 
ATOM   4957 C CB   . ASN   B 1 59  ? 60.874 -16.243 3.069   1.00 15.14 ?  59  ASN   B CB   1 
ATOM   4958 C CG   . ASN   B 1 59  ? 60.287 -16.402 4.450   1.00 16.39 ?  59  ASN   B CG   1 
ATOM   4959 O OD1  . ASN   B 1 59  ? 59.446 -17.274 4.683   1.00 16.40 ?  59  ASN   B OD1  1 
ATOM   4960 N ND2  . ASN   B 1 59  ? 60.732 -15.567 5.382   1.00 17.33 ?  59  ASN   B ND2  1 
ATOM   4961 H H    . ASN   B 1 59  ? 59.735 -17.237 0.326   1.00 16.46 ?  59  ASN   B H    1 
ATOM   4962 H HA   . ASN   B 1 59  ? 59.091 -16.779 2.255   1.00 16.55 ?  59  ASN   B HA   1 
ATOM   4963 H HB2  . ASN   B 1 59  ? 61.459 -17.002 2.913   1.00 18.17 ?  59  ASN   B HB2  1 
ATOM   4964 H HB3  . ASN   B 1 59  ? 61.387 -15.422 3.066   1.00 18.17 ?  59  ASN   B HB3  1 
ATOM   4965 H HD21 . ASN   B 1 59  ? 60.430 -15.615 6.189   1.00 20.79 ?  59  ASN   B HD21 1 
ATOM   4966 H HD22 . ASN   B 1 59  ? 61.316 -14.969 5.181   1.00 20.79 ?  59  ASN   B HD22 1 
ATOM   4967 N N    . ALA   B 1 60  ? 59.153 -14.134 0.737   1.00 13.14 ?  60  ALA   B N    1 
ATOM   4968 C CA   . ALA   B 1 60  ? 58.556 -12.803 0.660   1.00 13.22 ?  60  ALA   B CA   1 
ATOM   4969 C C    . ALA   B 1 60  ? 57.088 -12.826 1.061   1.00 12.43 ?  60  ALA   B C    1 
ATOM   4970 O O    . ALA   B 1 60  ? 56.587 -11.869 1.665   1.00 13.05 ?  60  ALA   B O    1 
ATOM   4971 C CB   . ALA   B 1 60  ? 58.721 -12.229 -0.747  1.00 14.62 ?  60  ALA   B CB   1 
ATOM   4972 H H    . ALA   B 1 60  ? 59.443 -14.449 -0.005  1.00 15.77 ?  60  ALA   B H    1 
ATOM   4973 H HA   . ALA   B 1 60  ? 59.022 -12.220 1.279   1.00 15.86 ?  60  ALA   B HA   1 
ATOM   4974 H HB1  . ALA   B 1 60  ? 58.322 -11.350 -0.774  1.00 17.55 ?  60  ALA   B HB1  1 
ATOM   4975 H HB2  . ALA   B 1 60  ? 59.667 -12.176 -0.954  1.00 17.55 ?  60  ALA   B HB2  1 
ATOM   4976 H HB3  . ALA   B 1 60  ? 58.278 -12.818 -1.378  1.00 17.55 ?  60  ALA   B HB3  1 
ATOM   4977 N N    . MET   B 1 61  ? 56.378 -13.902 0.717   1.00 11.64 ?  61  MET   B N    1 
ATOM   4978 C CA   . MET   B 1 61  ? 54.983 -14.022 1.113   1.00 11.30 ?  61  MET   B CA   1 
ATOM   4979 C C    . MET   B 1 61  ? 54.840 -14.020 2.634   1.00 11.33 ?  61  MET   B C    1 
ATOM   4980 O O    . MET   B 1 61  ? 53.936 -13.371 3.178   1.00 11.46 ?  61  MET   B O    1 
ATOM   4981 C CB   . MET   B 1 61  ? 54.401 -15.295 0.492   1.00 11.56 ?  61  MET   B CB   1 
ATOM   4982 C CG   . MET   B 1 61  ? 52.954 -15.574 0.880   1.00 11.13 ?  61  MET   B CG   1 
ATOM   4983 S SD   . MET   B 1 61  ? 52.310 -17.081 0.141   1.00 12.03 ?  61  MET   B SD   1 
ATOM   4984 C CE   . MET   B 1 61  ? 52.048 -16.522 -1.536  1.00 13.36 ?  61  MET   B CE   1 
ATOM   4985 H H    . MET   B 1 61  ? 56.680 -14.567 0.252   1.00 13.96 ?  61  MET   B H    1 
ATOM   4986 H HA   . MET   B 1 61  ? 54.490 -13.272 0.747   1.00 13.57 ?  61  MET   B HA   1 
ATOM   4987 H HB2  . MET   B 1 61  ? 54.435 -15.218 -0.476  1.00 13.87 ?  61  MET   B HB2  1 
ATOM   4988 H HB3  . MET   B 1 61  ? 54.934 -16.055 0.776   1.00 13.87 ?  61  MET   B HB3  1 
ATOM   4989 H HG2  . MET   B 1 61  ? 52.899 -15.671 1.842   1.00 13.36 ?  61  MET   B HG2  1 
ATOM   4990 H HG3  . MET   B 1 61  ? 52.404 -14.835 0.585   1.00 13.36 ?  61  MET   B HG3  1 
ATOM   4991 H HE1  . MET   B 1 61  ? 51.677 -17.252 -2.056  1.00 16.03 ?  61  MET   B HE1  1 
ATOM   4992 H HE2  . MET   B 1 61  ? 51.432 -15.774 -1.527  1.00 16.03 ?  61  MET   B HE2  1 
ATOM   4993 H HE3  . MET   B 1 61  ? 52.899 -16.246 -1.914  1.00 16.03 ?  61  MET   B HE3  1 
ATOM   4994 N N    . GLN   B 1 62  ? 55.716 -14.738 3.340   1.00 11.56 ?  62  GLN   B N    1 
ATOM   4995 C CA   . GLN   B 1 62  ? 55.608 -14.790 4.795   1.00 12.07 ?  62  GLN   B CA   1 
ATOM   4996 C C    . GLN   B 1 62  ? 55.890 -13.430 5.420   1.00 12.09 ?  62  GLN   B C    1 
ATOM   4997 O O    . GLN   B 1 62  ? 55.214 -13.026 6.372   1.00 12.52 ?  62  GLN   B O    1 
ATOM   4998 C CB   . GLN   B 1 62  ? 56.564 -15.838 5.366   1.00 12.48 ?  62  GLN   B CB   1 
ATOM   4999 C CG   . GLN   B 1 62  ? 56.336 -16.118 6.844   1.00 12.73 ?  62  GLN   B CG   1 
ATOM   5000 C CD   . GLN   B 1 62  ? 54.960 -16.698 7.081   1.00 12.28 ?  62  GLN   B CD   1 
ATOM   5001 O OE1  . GLN   B 1 62  ? 54.698 -17.849 6.733   1.00 12.86 ?  62  GLN   B OE1  1 
ATOM   5002 N NE2  . GLN   B 1 62  ? 54.050 -15.889 7.619   1.00 12.42 ?  62  GLN   B NE2  1 
ATOM   5003 H H    . GLN   B 1 62  ? 56.364 -15.201 3.004   1.00 13.87 ?  62  GLN   B H    1 
ATOM   5004 H HA   . GLN   B 1 62  ? 54.703 -15.045 5.029   1.00 14.48 ?  62  GLN   B HA   1 
ATOM   5005 H HB2  . GLN   B 1 62  ? 56.447 -16.670 4.881   1.00 14.98 ?  62  GLN   B HB2  1 
ATOM   5006 H HB3  . GLN   B 1 62  ? 57.476 -15.521 5.262   1.00 14.98 ?  62  GLN   B HB3  1 
ATOM   5007 H HG2  . GLN   B 1 62  ? 56.993 -16.764 7.149   1.00 15.27 ?  62  GLN   B HG2  1 
ATOM   5008 H HG3  . GLN   B 1 62  ? 56.410 -15.296 7.344   1.00 15.27 ?  62  GLN   B HG3  1 
ATOM   5009 H HE21 . GLN   B 1 62  ? 54.263 -15.085 7.829   1.00 14.90 ?  62  GLN   B HE21 1 
ATOM   5010 H HE22 . GLN   B 1 62  ? 53.251 -16.175 7.756   1.00 14.90 ?  62  GLN   B HE22 1 
ATOM   5011 N N    . VAL   B 1 63  ? 56.903 -12.719 4.922   1.00 12.49 ?  63  VAL   B N    1 
ATOM   5012 C CA   . VAL   B 1 63  ? 57.209 -11.401 5.476   1.00 13.48 ?  63  VAL   B CA   1 
ATOM   5013 C C    . VAL   B 1 63  ? 56.019 -10.466 5.290   1.00 12.68 ?  63  VAL   B C    1 
ATOM   5014 O O    . VAL   B 1 63  ? 55.611 -9.749  6.214   1.00 13.33 ?  63  VAL   B O    1 
ATOM   5015 C CB   . VAL   B 1 63  ? 58.498 -10.841 4.847   1.00 15.23 ?  63  VAL   B CB   1 
ATOM   5016 C CG1  . VAL   B 1 63  ? 58.735 -9.398  5.299   1.00 15.60 ?  63  VAL   B CG1  1 
ATOM   5017 C CG2  . VAL   B 1 63  ? 59.690 -11.714 5.219   1.00 15.89 ?  63  VAL   B CG2  1 
ATOM   5018 H H    . VAL   B 1 63  ? 57.413 -12.969 4.272   1.00 14.99 ?  63  VAL   B H    1 
ATOM   5019 H HA   . VAL   B 1 63  ? 57.369 -11.496 6.424   1.00 16.18 ?  63  VAL   B HA   1 
ATOM   5020 H HB   . VAL   B 1 63  ? 58.419 -10.846 3.880   1.00 18.28 ?  63  VAL   B HB   1 
ATOM   5021 H HG11 . VAL   B 1 63  ? 59.651 -9.150  5.098   1.00 18.73 ?  63  VAL   B HG11 1 
ATOM   5022 H HG12 . VAL   B 1 63  ? 58.123 -8.815  4.825   1.00 18.73 ?  63  VAL   B HG12 1 
ATOM   5023 H HG13 . VAL   B 1 63  ? 58.579 -9.340  6.255   1.00 18.73 ?  63  VAL   B HG13 1 
ATOM   5024 H HG21 . VAL   B 1 63  ? 60.498 -11.336 4.834   1.00 19.07 ?  63  VAL   B HG21 1 
ATOM   5025 H HG22 . VAL   B 1 63  ? 59.773 -11.741 6.188   1.00 19.07 ?  63  VAL   B HG22 1 
ATOM   5026 H HG23 . VAL   B 1 63  ? 59.550 -12.610 4.878   1.00 19.07 ?  63  VAL   B HG23 1 
ATOM   5027 N N    . GLU   B 1 64  ? 55.456 -10.453 4.085   1.00 12.40 ?  64  GLU   B N    1 
ATOM   5028 C CA   . GLU   B 1 64  ? 54.289 -9.622  3.804   1.00 11.92 ?  64  GLU   B CA   1 
ATOM   5029 C C    . GLU   B 1 64  ? 53.106 -10.020 4.678   1.00 11.56 ?  64  GLU   B C    1 
ATOM   5030 O O    . GLU   B 1 64  ? 52.356 -9.159  5.169   1.00 12.17 ?  64  GLU   B O    1 
ATOM   5031 C CB   . GLU   B 1 64  ? 53.929 -9.772  2.326   1.00 12.06 ?  64  GLU   B CB   1 
ATOM   5032 C CG   . GLU   B 1 64  ? 52.670 -9.036  1.893   1.00 12.52 ?  64  GLU   B CG   1 
ATOM   5033 C CD   . GLU   B 1 64  ? 52.142 -9.532  0.561   1.00 13.33 ?  64  GLU   B CD   1 
ATOM   5034 O OE1  . GLU   B 1 64  ? 52.320 -10.742 0.249   1.00 13.80 ?  64  GLU   B OE1  1 
ATOM   5035 O OE2  . GLU   B 1 64  ? 51.526 -8.721  -0.171  1.00 14.26 -1 64  GLU   B OE2  1 
ATOM   5036 H H    . GLU   B 1 64  ? 55.729 -10.921 3.411   1.00 14.88 ?  64  GLU   B H    1 
ATOM   5037 H HA   . GLU   B 1 64  ? 54.504 -8.693  3.977   1.00 14.30 ?  64  GLU   B HA   1 
ATOM   5038 H HB2  . GLU   B 1 64  ? 54.664 -9.425  1.790   1.00 14.48 ?  64  GLU   B HB2  1 
ATOM   5039 H HB3  . GLU   B 1 64  ? 53.804 -10.712 2.132   1.00 14.48 ?  64  GLU   B HB3  1 
ATOM   5040 H HG2  . GLU   B 1 64  ? 51.968 -9.166  2.555   1.00 15.02 ?  64  GLU   B HG2  1 
ATOM   5041 H HG3  . GLU   B 1 64  ? 52.866 -8.090  1.809   1.00 15.02 ?  64  GLU   B HG3  1 
ATOM   5042 N N    . SER   B 1 65  ? 52.925 -11.327 4.875   1.00 11.36 ?  65  SER   B N    1 
ATOM   5043 C CA   . SER   B 1 65  ? 51.813 -11.829 5.674   1.00 11.89 ?  65  SER   B CA   1 
ATOM   5044 C C    . SER   B 1 65  ? 51.940 -11.430 7.138   1.00 11.53 ?  65  SER   B C    1 
ATOM   5045 O O    . SER   B 1 65  ? 50.941 -11.051 7.768   1.00 11.94 ?  65  SER   B O    1 
ATOM   5046 C CB   . SER   B 1 65  ? 51.732 -13.351 5.553   1.00 12.10 ?  65  SER   B CB   1 
ATOM   5047 O OG   . SER   B 1 65  ? 51.380 -13.759 4.242   1.00 11.44 ?  65  SER   B OG   1 
ATOM   5048 H H    . SER   B 1 65  ? 53.437 -11.950 4.558   1.00 13.63 ?  65  SER   B H    1 
ATOM   5049 H HA   . SER   B 1 65  ? 50.986 -11.459 5.329   1.00 14.27 ?  65  SER   B HA   1 
ATOM   5050 H HB2  . SER   B 1 65  ? 52.589 -13.735 5.779   1.00 14.52 ?  65  SER   B HB2  1 
ATOM   5051 H HB3  . SER   B 1 65  ? 51.051 -13.677 6.168   1.00 14.52 ?  65  SER   B HB3  1 
ATOM   5052 H HG   . SER   B 1 65  ? 51.956 -13.477 3.688   1.00 13.73 ?  65  SER   B HG   1 
ATOM   5053 N N    . ASP   B 1 66  ? 53.145 -11.535 7.710   1.00 12.08 ?  66  ASP   B N    1 
ATOM   5054 C CA   . ASP   B 1 66  ? 53.332 -11.137 9.102   1.00 12.42 ?  66  ASP   B CA   1 
ATOM   5055 C C    . ASP   B 1 66  ? 53.017 -9.658  9.293   1.00 12.34 ?  66  ASP   B C    1 
ATOM   5056 O O    . ASP   B 1 66  ? 52.454 -9.258  10.319  1.00 13.04 ?  66  ASP   B O    1 
ATOM   5057 C CB   . ASP   B 1 66  ? 54.766 -11.441 9.549   1.00 14.22 ?  66  ASP   B CB   1 
ATOM   5058 C CG   . ASP   B 1 66  ? 55.037 -12.936 9.707   1.00 15.65 ?  66  ASP   B CG   1 
ATOM   5059 O OD1  . ASP   B 1 66  ? 54.080 -13.742 9.648   1.00 16.37 ?  66  ASP   B OD1  1 
ATOM   5060 O OD2  . ASP   B 1 66  ? 56.219 -13.302 9.909   1.00 18.67 -1 66  ASP   B OD2  1 
ATOM   5061 H H    . ASP   B 1 66  ? 53.844 -11.844 7.326   1.00 14.50 ?  66  ASP   B H    1 
ATOM   5062 H HA   . ASP   B 1 66  ? 52.729 -11.643 9.670   1.00 14.90 ?  66  ASP   B HA   1 
ATOM   5063 H HB2  . ASP   B 1 66  ? 55.382 -11.095 8.887   1.00 17.07 ?  66  ASP   B HB2  1 
ATOM   5064 H HB3  . ASP   B 1 66  ? 54.926 -11.010 10.407  1.00 17.07 ?  66  ASP   B HB3  1 
ATOM   5065 N N    . ASP   B 1 67  ? 53.394 -8.821  8.325   1.00 12.12 ?  67  ASP   B N    1 
ATOM   5066 C CA   . ASP   B 1 67  ? 53.048 -7.409  8.403   1.00 13.18 ?  67  ASP   B CA   1 
ATOM   5067 C C    . ASP   B 1 67  ? 51.537 -7.202  8.327   1.00 13.06 ?  67  ASP   B C    1 
ATOM   5068 O O    . ASP   B 1 67  ? 50.975 -6.391  9.076   1.00 13.89 ?  67  ASP   B O    1 
ATOM   5069 C CB   . ASP   B 1 67  ? 53.762 -6.648  7.290   1.00 14.50 ?  67  ASP   B CB   1 
ATOM   5070 C CG   . ASP   B 1 67  ? 53.338 -5.206  7.232   1.00 15.89 ?  67  ASP   B CG   1 
ATOM   5071 O OD1  . ASP   B 1 67  ? 53.855 -4.391  8.030   1.00 17.03 ?  67  ASP   B OD1  1 
ATOM   5072 O OD2  . ASP   B 1 67  ? 52.455 -4.902  6.416   1.00 17.15 -1 67  ASP   B OD2  1 
ATOM   5073 H H    . ASP   B 1 67  ? 53.857 -9.047  7.633   1.00 14.55 ?  67  ASP   B H    1 
ATOM   5074 H HA   . ASP   B 1 67  ? 53.360 -7.054  9.250   1.00 15.82 ?  67  ASP   B HA   1 
ATOM   5075 H HB2  . ASP   B 1 67  ? 54.722 -6.683  7.441   1.00 17.40 ?  67  ASP   B HB2  1 
ATOM   5076 H HB3  . ASP   B 1 67  ? 53.552 -7.065  6.435   1.00 17.40 ?  67  ASP   B HB3  1 
ATOM   5077 N N    . TYR   B 1 68  ? 50.860 -7.926  7.428   1.00 12.53 ?  68  TYR   B N    1 
ATOM   5078 C CA   . TYR   B 1 68  ? 49.404 -7.847  7.354   1.00 13.24 ?  68  TYR   B CA   1 
ATOM   5079 C C    . TYR   B 1 68  ? 48.767 -8.193  8.696   1.00 13.18 ?  68  TYR   B C    1 
ATOM   5080 O O    . TYR   B 1 68  ? 47.834 -7.510  9.145   1.00 13.76 ?  68  TYR   B O    1 
ATOM   5081 C CB   . TYR   B 1 68  ? 48.874 -8.783  6.260   1.00 14.45 ?  68  TYR   B CB   1 
ATOM   5082 C CG   . TYR   B 1 68  ? 47.367 -8.925  6.313   1.00 15.46 ?  68  TYR   B CG   1 
ATOM   5083 C CD1  . TYR   B 1 68  ? 46.777 -9.874  7.141   1.00 15.95 ?  68  TYR   B CD1  1 
ATOM   5084 C CD2  . TYR   B 1 68  ? 46.540 -8.091  5.583   1.00 16.33 ?  68  TYR   B CD2  1 
ATOM   5085 C CE1  . TYR   B 1 68  ? 45.413 -9.997  7.236   1.00 17.16 ?  68  TYR   B CE1  1 
ATOM   5086 C CE2  . TYR   B 1 68  ? 45.153 -8.220  5.661   1.00 16.85 ?  68  TYR   B CE2  1 
ATOM   5087 C CZ   . TYR   B 1 68  ? 44.611 -9.174  6.496   1.00 17.14 ?  68  TYR   B CZ   1 
ATOM   5088 O OH   . TYR   B 1 68  ? 43.243 -9.297  6.601   1.00 18.38 ?  68  TYR   B OH   1 
ATOM   5089 H H    . TYR   B 1 68  ? 51.221 -8.467  6.854   1.00 15.04 ?  68  TYR   B H    1 
ATOM   5090 H HA   . TYR   B 1 68  ? 49.153 -6.943  7.126   1.00 15.89 ?  68  TYR   B HA   1 
ATOM   5091 H HB2  . TYR   B 1 68  ? 49.108 -8.423  5.393   1.00 17.34 ?  68  TYR   B HB2  1 
ATOM   5092 H HB3  . TYR   B 1 68  ? 49.264 -9.663  6.376   1.00 17.34 ?  68  TYR   B HB3  1 
ATOM   5093 H HD1  . TYR   B 1 68  ? 47.320 -10.439 7.646   1.00 19.14 ?  68  TYR   B HD1  1 
ATOM   5094 H HD2  . TYR   B 1 68  ? 46.911 -7.442  5.033   1.00 19.60 ?  68  TYR   B HD2  1 
ATOM   5095 H HE1  . TYR   B 1 68  ? 45.036 -10.650 7.783   1.00 20.59 ?  68  TYR   B HE1  1 
ATOM   5096 H HE2  . TYR   B 1 68  ? 44.593 -7.657  5.172   1.00 20.22 ?  68  TYR   B HE2  1 
ATOM   5097 H HH   . TYR   B 1 68  ? 42.857 -8.750  6.091   1.00 22.05 ?  68  TYR   B HH   1 
ATOM   5098 N N    . ILE   B 1 69  ? 49.257 -9.256  9.346   1.00 12.68 ?  69  ILE   B N    1 
ATOM   5099 C CA   . ILE   B 1 69  ? 48.701 -9.680  10.630  1.00 13.07 ?  69  ILE   B CA   1 
ATOM   5100 C C    . ILE   B 1 69  ? 48.946 -8.622  11.701  1.00 12.71 ?  69  ILE   B C    1 
ATOM   5101 O O    . ILE   B 1 69  ? 48.075 -8.343  12.533  1.00 13.23 ?  69  ILE   B O    1 
ATOM   5102 C CB   . ILE   B 1 69  ? 49.282 -11.051 11.035  1.00 13.73 ?  69  ILE   B CB   1 
ATOM   5103 C CG1  . ILE   B 1 69  ? 48.758 -12.176 10.129  1.00 14.50 ?  69  ILE   B CG1  1 
ATOM   5104 C CG2  . ILE   B 1 69  ? 48.989 -11.366 12.499  1.00 14.81 ?  69  ILE   B CG2  1 
ATOM   5105 C CD1  . ILE   B 1 69  ? 47.270 -12.467 10.285  1.00 14.87 ?  69  ILE   B CD1  1 
ATOM   5106 H H    . ILE   B 1 69  ? 49.912 -9.745  9.066   1.00 15.22 ?  69  ILE   B H    1 
ATOM   5107 H HA   . ILE   B 1 69  ? 47.748 -9.784  10.532  1.00 15.68 ?  69  ILE   B HA   1 
ATOM   5108 H HB   . ILE   B 1 69  ? 50.248 -11.015 10.930  1.00 16.48 ?  69  ILE   B HB   1 
ATOM   5109 H HG12 . ILE   B 1 69  ? 48.915 -11.926 9.205   1.00 17.40 ?  69  ILE   B HG12 1 
ATOM   5110 H HG13 . ILE   B 1 69  ? 49.243 -12.992 10.332  1.00 17.40 ?  69  ILE   B HG13 1 
ATOM   5111 H HG21 . ILE   B 1 69  ? 49.134 -12.316 12.652  1.00 17.78 ?  69  ILE   B HG21 1 
ATOM   5112 H HG22 . ILE   B 1 69  ? 49.582 -10.851 13.065  1.00 17.78 ?  69  ILE   B HG22 1 
ATOM   5113 H HG23 . ILE   B 1 69  ? 48.064 -11.144 12.691  1.00 17.78 ?  69  ILE   B HG23 1 
ATOM   5114 H HD11 . ILE   B 1 69  ? 47.032 -13.193 9.689   1.00 17.85 ?  69  ILE   B HD11 1 
ATOM   5115 H HD12 . ILE   B 1 69  ? 47.091 -12.724 11.203  1.00 17.85 ?  69  ILE   B HD12 1 
ATOM   5116 H HD13 . ILE   B 1 69  ? 46.765 -11.673 10.057  1.00 17.85 ?  69  ILE   B HD13 1 
ATOM   5117 N N    . ALA   B 1 70  ? 50.138 -8.034  11.721  1.00 12.79 ?  70  ALA   B N    1 
ATOM   5118 C CA   . ALA   B 1 70  ? 50.414 -6.995  12.709  1.00 12.79 ?  70  ALA   B CA   1 
ATOM   5119 C C    . ALA   B 1 70  ? 49.412 -5.857  12.592  1.00 13.32 ?  70  ALA   B C    1 
ATOM   5120 O O    . ALA   B 1 70  ? 48.954 -5.318  13.602  1.00 13.79 ?  70  ALA   B O    1 
ATOM   5121 C CB   . ALA   B 1 70  ? 51.837 -6.469  12.536  1.00 13.57 ?  70  ALA   B CB   1 
ATOM   5122 H H    . ALA   B 1 70  ? 50.786 -8.213  11.195  1.00 15.34 ?  70  ALA   B H    1 
ATOM   5123 H HA   . ALA   B 1 70  ? 50.343 -7.371  13.603  1.00 15.35 ?  70  ALA   B HA   1 
ATOM   5124 H HB1  . ALA   B 1 70  ? 52.025 -5.819  13.233  1.00 16.28 ?  70  ALA   B HB1  1 
ATOM   5125 H HB2  . ALA   B 1 70  ? 52.461 -7.210  12.603  1.00 16.28 ?  70  ALA   B HB2  1 
ATOM   5126 H HB3  . ALA   B 1 70  ? 51.918 -6.050  11.664  1.00 16.28 ?  70  ALA   B HB3  1 
ATOM   5127 N N    . THR   B 1 71  ? 49.059 -5.482  11.367  1.00 13.68 ?  71  THR   B N    1 
ATOM   5128 C CA   . THR   B 1 71  ? 48.156 -4.356  11.151  1.00 14.79 ?  71  THR   B CA   1 
ATOM   5129 C C    . THR   B 1 71  ? 46.688 -4.726  11.363  1.00 15.14 ?  71  THR   B C    1 
ATOM   5130 O O    . THR   B 1 71  ? 45.911 -3.912  11.879  1.00 16.62 ?  71  THR   B O    1 
ATOM   5131 C CB   . THR   B 1 71  ? 48.372 -3.798  9.741   1.00 16.57 ?  71  THR   B CB   1 
ATOM   5132 O OG1  . THR   B 1 71  ? 49.700 -3.268  9.636   1.00 18.49 ?  71  THR   B OG1  1 
ATOM   5133 C CG2  . THR   B 1 71  ? 47.352 -2.717  9.418   1.00 17.66 ?  71  THR   B CG2  1 
ATOM   5134 H H    . THR   B 1 71  ? 49.328 -5.869  10.648  1.00 16.42 ?  71  THR   B H    1 
ATOM   5135 H HA   . THR   B 1 71  ? 48.378 -3.659  11.780  1.00 17.75 ?  71  THR   B HA   1 
ATOM   5136 H HB   . THR   B 1 71  ? 48.277 -4.509  9.090   1.00 19.88 ?  71  THR   B HB   1 
ATOM   5137 H HG1  . THR   B 1 71  ? 49.816 -2.929  8.870   1.00 22.19 ?  71  THR   B HG1  1 
ATOM   5138 H HG21 . THR   B 1 71  ? 47.653 -2.198  8.653   1.00 21.20 ?  71  THR   B HG21 1 
ATOM   5139 H HG22 . THR   B 1 71  ? 46.496 -3.117  9.208   1.00 21.20 ?  71  THR   B HG22 1 
ATOM   5140 H HG23 . THR   B 1 71  ? 47.249 -2.120  10.176  1.00 21.20 ?  71  THR   B HG23 1 
ATOM   5141 N N    . ASN   B 1 72  ? 46.291 -5.942  10.984  1.00 14.54 ?  72  ASN   B N    1 
ATOM   5142 C CA   . ASN   B 1 72  ? 44.886 -6.299  10.862  1.00 15.28 ?  72  ASN   B CA   1 
ATOM   5143 C C    . ASN   B 1 72  ? 44.419 -7.386  11.817  1.00 16.04 ?  72  ASN   B C    1 
ATOM   5144 O O    . ASN   B 1 72  ? 43.204 -7.543  11.986  1.00 17.13 ?  72  ASN   B O    1 
ATOM   5145 C CB   . ASN   B 1 72  ? 44.577 -6.740  9.423   1.00 16.68 ?  72  ASN   B CB   1 
ATOM   5146 C CG   . ASN   B 1 72  ? 44.849 -5.644  8.418   1.00 17.83 ?  72  ASN   B CG   1 
ATOM   5147 O OD1  . ASN   B 1 72  ? 45.870 -5.650  7.722   1.00 19.04 ?  72  ASN   B OD1  1 
ATOM   5148 N ND2  . ASN   B 1 72  ? 43.959 -4.674  8.362   1.00 19.49 ?  72  ASN   B ND2  1 
ATOM   5149 H H    . ASN   B 1 72  ? 46.831 -6.594  10.794  1.00 17.45 ?  72  ASN   B H    1 
ATOM   5150 H HA   . ASN   B 1 72  ? 44.357 -5.510  11.045  1.00 18.34 ?  72  ASN   B HA   1 
ATOM   5151 H HB2  . ASN   B 1 72  ? 45.134 -7.500  9.196   1.00 20.02 ?  72  ASN   B HB2  1 
ATOM   5152 H HB3  . ASN   B 1 72  ? 43.641 -6.978  9.359   1.00 20.02 ?  72  ASN   B HB3  1 
ATOM   5153 H HD21 . ASN   B 1 72  ? 44.061 -4.024  7.806   1.00 23.39 ?  72  ASN   B HD21 1 
ATOM   5154 H HD22 . ASN   B 1 72  ? 43.257 -4.703  8.860   1.00 23.39 ?  72  ASN   B HD22 1 
ATOM   5155 N N    . GLY   B 1 73  ? 45.326 -8.136  12.437  1.00 15.71 ?  73  GLY   B N    1 
ATOM   5156 C CA   . GLY   B 1 73  ? 44.932 -9.276  13.224  1.00 14.72 ?  73  GLY   B CA   1 
ATOM   5157 C C    . GLY   B 1 73  ? 44.583 -10.464 12.355  1.00 13.41 ?  73  GLY   B C    1 
ATOM   5158 O O    . GLY   B 1 73  ? 44.568 -10.383 11.126  1.00 13.47 ?  73  GLY   B O    1 
ATOM   5159 H H    . GLY   B 1 73  ? 46.176 -7.999  12.413  1.00 18.85 ?  73  GLY   B H    1 
ATOM   5160 H HA2  . GLY   B 1 73  ? 45.656 -9.527  13.818  1.00 17.66 ?  73  GLY   B HA2  1 
ATOM   5161 H HA3  . GLY   B 1 73  ? 44.158 -9.044  13.764  1.00 17.66 ?  73  GLY   B HA3  1 
ATOM   5162 N N    . PRO   B 1 74  ? 44.278 -11.591 12.998  1.00 13.61 ?  74  PRO   B N    1 
ATOM   5163 C CA   . PRO   B 1 74  ? 44.016 -12.828 12.260  1.00 13.00 ?  74  PRO   B CA   1 
ATOM   5164 C C    . PRO   B 1 74  ? 42.715 -12.775 11.472  1.00 12.43 ?  74  PRO   B C    1 
ATOM   5165 O O    . PRO   B 1 74  ? 41.780 -12.037 11.799  1.00 13.90 ?  74  PRO   B O    1 
ATOM   5166 C CB   . PRO   B 1 74  ? 43.941 -13.883 13.371  1.00 13.90 ?  74  PRO   B CB   1 
ATOM   5167 C CG   . PRO   B 1 74  ? 43.477 -13.116 14.572  1.00 15.88 ?  74  PRO   B CG   1 
ATOM   5168 C CD   . PRO   B 1 74  ? 44.135 -11.772 14.451  1.00 15.12 ?  74  PRO   B CD   1 
ATOM   5169 H HA   . PRO   B 1 74  ? 44.756 -13.029 11.661  1.00 15.60 ?  74  PRO   B HA   1 
ATOM   5170 H HB2  . PRO   B 1 74  ? 43.300 -14.569 13.127  1.00 16.68 ?  74  PRO   B HB2  1 
ATOM   5171 H HB3  . PRO   B 1 74  ? 44.819 -14.264 13.521  1.00 16.68 ?  74  PRO   B HB3  1 
ATOM   5172 H HG2  . PRO   B 1 74  ? 42.508 -13.025 14.548  1.00 19.05 ?  74  PRO   B HG2  1 
ATOM   5173 H HG3  . PRO   B 1 74  ? 43.759 -13.566 15.380  1.00 19.05 ?  74  PRO   B HG3  1 
ATOM   5174 H HD2  . PRO   B 1 74  ? 43.563 -11.082 14.831  1.00 18.14 ?  74  PRO   B HD2  1 
ATOM   5175 H HD3  . PRO   B 1 74  ? 45.005 -11.784 14.877  1.00 18.14 ?  74  PRO   B HD3  1 
ATOM   5176 N N    . LEU   B 1 75  ? 42.675 -13.579 10.417  1.00 11.94 ?  75  LEU   B N    1 
ATOM   5177 C CA   . LEU   B 1 75  ? 41.463 -13.787 9.648   1.00 12.18 ?  75  LEU   B CA   1 
ATOM   5178 C C    . LEU   B 1 75  ? 40.473 -14.631 10.447  1.00 12.83 ?  75  LEU   B C    1 
ATOM   5179 O O    . LEU   B 1 75  ? 40.808 -15.225 11.472  1.00 13.63 ?  75  LEU   B O    1 
ATOM   5180 C CB   . LEU   B 1 75  ? 41.787 -14.511 8.342   1.00 11.85 ?  75  LEU   B CB   1 
ATOM   5181 C CG   . LEU   B 1 75  ? 42.611 -13.754 7.297   1.00 13.63 ?  75  LEU   B CG   1 
ATOM   5182 C CD1  . LEU   B 1 75  ? 42.843 -14.601 6.055   1.00 15.30 ?  75  LEU   B CD1  1 
ATOM   5183 C CD2  . LEU   B 1 75  ? 41.972 -12.448 6.923   1.00 17.53 ?  75  LEU   B CD2  1 
ATOM   5184 H H    . LEU   B 1 75  ? 43.354 -14.026 10.123  1.00 14.33 ?  75  LEU   B H    1 
ATOM   5185 H HA   . LEU   B 1 75  ? 41.056 -12.932 9.437   1.00 14.61 ?  75  LEU   B HA   1 
ATOM   5186 H HB2  . LEU   B 1 75  ? 42.285 -15.320 8.558   1.00 14.22 ?  75  LEU   B HB2  1 
ATOM   5187 H HB3  . LEU   B 1 75  ? 40.952 -14.762 7.916   1.00 14.22 ?  75  LEU   B HB3  1 
ATOM   5188 H HG   . LEU   B 1 75  ? 43.480 -13.553 7.675   1.00 16.35 ?  75  LEU   B HG   1 
ATOM   5189 H HD11 . LEU   B 1 75  ? 43.375 -14.093 5.415   1.00 18.36 ?  75  LEU   B HD11 1 
ATOM   5190 H HD12 . LEU   B 1 75  ? 43.323 -15.409 6.304   1.00 18.36 ?  75  LEU   B HD12 1 
ATOM   5191 H HD13 . LEU   B 1 75  ? 41.990 -14.834 5.659   1.00 18.36 ?  75  LEU   B HD13 1 
ATOM   5192 H HD21 . LEU   B 1 75  ? 42.464 -12.054 6.187   1.00 21.03 ?  75  LEU   B HD21 1 
ATOM   5193 H HD22 . LEU   B 1 75  ? 41.053 -12.609 6.660   1.00 21.03 ?  75  LEU   B HD22 1 
ATOM   5194 H HD23 . LEU   B 1 75  ? 41.997 -11.854 7.691   1.00 21.03 ?  75  LEU   B HD23 1 
ATOM   5195 N N    . LYS   B 1 76  ? 39.239 -14.693 9.949   1.00 14.03 ?  76  LYS   B N    1 
ATOM   5196 C CA   . LYS   B 1 76  ? 38.253 -15.653 10.423  1.00 15.39 ?  76  LYS   B CA   1 
ATOM   5197 C C    . LYS   B 1 76  ? 38.361 -16.939 9.608   1.00 14.03 ?  76  LYS   B C    1 
ATOM   5198 O O    . LYS   B 1 76  ? 38.653 -16.905 8.415   1.00 13.54 ?  76  LYS   B O    1 
ATOM   5199 C CB   . LYS   B 1 76  ? 36.835 -15.092 10.227  1.00 17.59 ?  76  LYS   B CB   1 
ATOM   5200 C CG   . LYS   B 1 76  ? 36.566 -13.697 10.820  1.00 19.20 ?  76  LYS   B CG   1 
ATOM   5201 C CD   . LYS   B 1 76  ? 35.151 -13.187 10.481  1.00 20.30 ?  76  LYS   B CD   1 
ATOM   5202 C CE   . LYS   B 1 76  ? 34.897 -11.802 11.059  1.00 21.93 ?  76  LYS   B CE   1 
ATOM   5203 N NZ   . LYS   B 1 76  ? 33.589 -11.223 10.643  1.00 22.36 ?  76  LYS   B NZ   1 
ATOM   5204 H H    . LYS   B 1 76  ? 38.950 -14.182 9.318   1.00 16.84 ?  76  LYS   B H    1 
ATOM   5205 H HA   . LYS   B 1 76  ? 38.400 -15.856 11.360  1.00 18.47 ?  76  LYS   B HA   1 
ATOM   5206 H HB2  . LYS   B 1 76  ? 36.660 -15.039 9.275   1.00 21.11 ?  76  LYS   B HB2  1 
ATOM   5207 H HB3  . LYS   B 1 76  ? 36.209 -15.705 10.638  1.00 21.11 ?  76  LYS   B HB3  1 
ATOM   5208 H HG2  . LYS   B 1 76  ? 36.652 -13.739 11.786  1.00 23.04 ?  76  LYS   B HG2  1 
ATOM   5209 H HG3  . LYS   B 1 76  ? 37.211 -13.066 10.457  1.00 23.04 ?  76  LYS   B HG3  1 
ATOM   5210 H HD2  . LYS   B 1 76  ? 35.052 -13.138 9.516   1.00 24.36 ?  76  LYS   B HD2  1 
ATOM   5211 H HD3  . LYS   B 1 76  ? 34.495 -13.798 10.853  1.00 24.36 ?  76  LYS   B HD3  1 
ATOM   5212 H HE2  . LYS   B 1 76  ? 34.903 -11.861 12.026  1.00 26.31 ?  76  LYS   B HE2  1 
ATOM   5213 H HE3  . LYS   B 1 76  ? 35.598 -11.204 10.758  1.00 26.31 ?  76  LYS   B HE3  1 
ATOM   5214 H HZ1  . LYS   B 1 76  ? 33.485 -10.414 11.004  1.00 26.83 ?  76  LYS   B HZ1  1 
ATOM   5215 H HZ2  . LYS   B 1 76  ? 33.556 -11.147 9.756   1.00 26.83 ?  76  LYS   B HZ2  1 
ATOM   5216 H HZ3  . LYS   B 1 76  ? 32.922 -11.746 10.913  1.00 26.83 ?  76  LYS   B HZ3  1 
ATOM   5217 N N    . VAL   B 1 77  ? 38.105 -18.082 10.252  1.00 14.78 ?  77  VAL   B N    1 
ATOM   5218 C CA   . VAL   B 1 77  ? 37.907 -19.305 9.478   1.00 15.22 ?  77  VAL   B CA   1 
ATOM   5219 C C    . VAL   B 1 77  ? 36.718 -19.084 8.555   1.00 13.55 ?  77  VAL   B C    1 
ATOM   5220 O O    . VAL   B 1 77  ? 35.652 -18.640 8.995   1.00 13.34 ?  77  VAL   B O    1 
ATOM   5221 C CB   . VAL   B 1 77  ? 37.702 -20.518 10.397  1.00 17.13 ?  77  VAL   B CB   1 
ATOM   5222 C CG1  . VAL   B 1 77  ? 37.436 -21.765 9.554   1.00 17.66 ?  77  VAL   B CG1  1 
ATOM   5223 C CG2  . VAL   B 1 77  ? 38.917 -20.723 11.304  1.00 18.38 ?  77  VAL   B CG2  1 
ATOM   5224 H H    . VAL   B 1 77  ? 38.046 -18.172 11.100  1.00 17.73 ?  77  VAL   B H    1 
ATOM   5225 H HA   . VAL   B 1 77  ? 38.687 -19.465 8.926   1.00 18.27 ?  77  VAL   B HA   1 
ATOM   5226 H HB   . VAL   B 1 77  ? 36.925 -20.362 10.957  1.00 20.55 ?  77  VAL   B HB   1 
ATOM   5227 H HG11 . VAL   B 1 77  ? 37.484 -22.545 10.128  1.00 21.19 ?  77  VAL   B HG11 1 
ATOM   5228 H HG12 . VAL   B 1 77  ? 36.552 -21.701 9.158   1.00 21.19 ?  77  VAL   B HG12 1 
ATOM   5229 H HG13 . VAL   B 1 77  ? 38.108 -21.824 8.858   1.00 21.19 ?  77  VAL   B HG13 1 
ATOM   5230 H HG21 . VAL   B 1 77  ? 38.775 -21.518 11.839  1.00 22.06 ?  77  VAL   B HG21 1 
ATOM   5231 H HG22 . VAL   B 1 77  ? 39.706 -20.827 10.752  1.00 22.06 ?  77  VAL   B HG22 1 
ATOM   5232 H HG23 . VAL   B 1 77  ? 39.012 -19.948 11.879  1.00 22.06 ?  77  VAL   B HG23 1 
ATOM   5233 N N    . GLY   B 1 78  ? 36.898 -19.373 7.267   1.00 13.02 ?  78  GLY   B N    1 
ATOM   5234 C CA   . GLY   B 1 78  ? 35.919 -19.049 6.253   1.00 12.82 ?  78  GLY   B CA   1 
ATOM   5235 C C    . GLY   B 1 78  ? 36.158 -17.732 5.549   1.00 12.35 ?  78  GLY   B C    1 
ATOM   5236 O O    . GLY   B 1 78  ? 35.478 -17.452 4.558   1.00 12.35 ?  78  GLY   B O    1 
ATOM   5237 H H    . GLY   B 1 78  ? 37.596 -19.770 6.950   1.00 15.62 ?  78  GLY   B H    1 
ATOM   5238 H HA2  . GLY   B 1 78  ? 35.911 -19.745 5.581   1.00 15.39 ?  78  GLY   B HA2  1 
ATOM   5239 H HA3  . GLY   B 1 78  ? 35.039 -19.014 6.662   1.00 15.39 ?  78  GLY   B HA3  1 
ATOM   5240 N N    . GLY   B 1 79  ? 37.116 -16.929 6.019   1.00 12.20 ?  79  GLY   B N    1 
ATOM   5241 C CA   . GLY   B 1 79  ? 37.413 -15.640 5.432   1.00 11.96 ?  79  GLY   B CA   1 
ATOM   5242 C C    . GLY   B 1 79  ? 38.655 -15.664 4.552   1.00 11.55 ?  79  GLY   B C    1 
ATOM   5243 O O    . GLY   B 1 79  ? 39.272 -16.702 4.310   1.00 11.97 ?  79  GLY   B O    1 
ATOM   5244 H H    . GLY   B 1 79  ? 37.614 -17.116 6.692   1.00 14.64 ?  79  GLY   B H    1 
ATOM   5245 H HA2  . GLY   B 1 79  ? 36.662 -15.349 4.886   1.00 14.35 ?  79  GLY   B HA2  1 
ATOM   5246 H HA3  . GLY   B 1 79  ? 37.551 -14.987 6.131   1.00 14.35 ?  79  GLY   B HA3  1 
ATOM   5247 N N    . SER   B 1 80  ? 39.021 -14.473 4.070   1.00 11.13 ?  80  SER   B N    1 
ATOM   5248 C CA   . SER   B 1 80  ? 40.138 -14.349 3.143   1.00 10.75 ?  80  SER   B CA   1 
ATOM   5249 C C    . SER   B 1 80  ? 40.723 -12.946 3.191   1.00 10.80 ?  80  SER   B C    1 
ATOM   5250 O O    . SER   B 1 80  ? 40.114 -12.008 3.709   1.00 11.95 ?  80  SER   B O    1 
ATOM   5251 C CB   . SER   B 1 80  ? 39.711 -14.652 1.704   1.00 11.20 ?  80  SER   B CB   1 
ATOM   5252 O OG   . SER   B 1 80  ? 38.867 -13.637 1.187   1.00 12.18 ?  80  SER   B OG   1 
ATOM   5253 H H    . SER   B 1 80  ? 38.644 -13.729 4.272   1.00 13.35 ?  80  SER   B H    1 
ATOM   5254 H HA   . SER   B 1 80  ? 40.825 -14.978 3.399   1.00 12.89 ?  80  SER   B HA   1 
ATOM   5255 H HB2  . SER   B 1 80  ? 40.503 -14.706 1.143   1.00 13.44 ?  80  SER   B HB2  1 
ATOM   5256 H HB3  . SER   B 1 80  ? 39.237 -15.497 1.684   1.00 13.44 ?  80  SER   B HB3  1 
ATOM   5257 H HG   . SER   B 1 80  ? 38.162 -13.579 1.650   1.00 14.62 ?  80  SER   B HG   1 
ATOM   5258 N N    . CYS   B 1 81  ? 41.909 -12.806 2.602   1.00 10.56 ?  81  CYS   B N    1 
ATOM   5259 C CA   . CYS   B 1 81  ? 42.459 -11.496 2.292   1.00 10.87 ?  81  CYS   B CA   1 
ATOM   5260 C C    . CYS   B 1 81  ? 43.229 -11.589 0.983   1.00 10.21 ?  81  CYS   B C    1 
ATOM   5261 O O    . CYS   B 1 81  ? 43.725 -12.655 0.609   1.00 11.21 ?  81  CYS   B O    1 
ATOM   5262 C CB   . CYS   B 1 81  ? 43.345 -10.960 3.419   1.00 11.63 ?  81  CYS   B CB   1 
ATOM   5263 S SG   . CYS   B 1 81  ? 44.874 -11.890 3.647   1.00 12.14 ?  81  CYS   B SG   1 
ATOM   5264 H H    . CYS   B 1 81  ? 42.417 -13.463 2.359   1.00 12.68 ?  81  CYS   B H    1 
ATOM   5265 H HA   . CYS   B 1 81  ? 41.729 -10.869 2.165   1.00 13.05 ?  81  CYS   B HA   1 
ATOM   5266 H HB2  . CYS   B 1 81  ? 43.585 -10.042 3.222   1.00 13.96 ?  81  CYS   B HB2  1 
ATOM   5267 H HB3  . CYS   B 1 81  ? 42.845 -10.995 4.253   1.00 13.96 ?  81  CYS   B HB3  1 
ATOM   5268 H HG   . CYS   B 1 81  ? 45.494 -11.409 4.549   1.00 14.57 ?  81  CYS   B HG   1 
ATOM   5269 N N    . VAL   B 1 82  ? 43.337 -10.448 0.306   1.00 10.75 ?  82  VAL   B N    1 
ATOM   5270 C CA   . VAL   B 1 82  ? 44.099 -10.323 -0.932  1.00 10.70 ?  82  VAL   B CA   1 
ATOM   5271 C C    . VAL   B 1 82  ? 45.442 -9.683  -0.618  1.00 10.75 ?  82  VAL   B C    1 
ATOM   5272 O O    . VAL   B 1 82  ? 45.498 -8.565  -0.091  1.00 11.93 ?  82  VAL   B O    1 
ATOM   5273 C CB   . VAL   B 1 82  ? 43.348 -9.488  -1.981  1.00 12.15 ?  82  VAL   B CB   1 
ATOM   5274 C CG1  . VAL   B 1 82  ? 44.186 -9.347  -3.246  1.00 13.40 ?  82  VAL   B CG1  1 
ATOM   5275 C CG2  . VAL   B 1 82  ? 41.989 -10.087 -2.296  1.00 12.85 ?  82  VAL   B CG2  1 
ATOM   5276 H H    . VAL   B 1 82  ? 42.964 -9.707  0.545   1.00 12.90 ?  82  VAL   B H    1 
ATOM   5277 H HA   . VAL   B 1 82  ? 44.257 -11.205 -1.305  1.00 12.84 ?  82  VAL   B HA   1 
ATOM   5278 H HB   . VAL   B 1 82  ? 43.204 -8.601  -1.630  1.00 14.58 ?  82  VAL   B HB   1 
ATOM   5279 H HG11 . VAL   B 1 82  ? 43.624 -9.024  -3.967  1.00 16.08 ?  82  VAL   B HG11 1 
ATOM   5280 H HG12 . VAL   B 1 82  ? 44.904 -8.709  -3.082  1.00 16.08 ?  82  VAL   B HG12 1 
ATOM   5281 H HG13 . VAL   B 1 82  ? 44.561 -10.209 -3.480  1.00 16.08 ?  82  VAL   B HG13 1 
ATOM   5282 H HG21 . VAL   B 1 82  ? 41.559 -9.556  -2.986  1.00 15.42 ?  82  VAL   B HG21 1 
ATOM   5283 H HG22 . VAL   B 1 82  ? 42.107 -10.999 -2.610  1.00 15.42 ?  82  VAL   B HG22 1 
ATOM   5284 H HG23 . VAL   B 1 82  ? 41.449 -10.082 -1.491  1.00 15.42 ?  82  VAL   B HG23 1 
ATOM   5285 N N    . LEU   B 1 83  ? 46.521 -10.375 -0.986  1.00 10.49 ?  83  LEU   B N    1 
ATOM   5286 C CA   . LEU   B 1 83  ? 47.879 -9.866  -0.869  1.00 10.41 ?  83  LEU   B CA   1 
ATOM   5287 C C    . LEU   B 1 83  ? 48.576 -10.017 -2.221  1.00 10.27 ?  83  LEU   B C    1 
ATOM   5288 O O    . LEU   B 1 83  ? 47.973 -10.439 -3.208  1.00 10.31 ?  83  LEU   B O    1 
ATOM   5289 C CB   . LEU   B 1 83  ? 48.627 -10.537 0.290   1.00 11.06 ?  83  LEU   B CB   1 
ATOM   5290 C CG   . LEU   B 1 83  ? 48.117 -10.174 1.688   1.00 12.19 ?  83  LEU   B CG   1 
ATOM   5291 C CD1  . LEU   B 1 83  ? 48.760 -11.043 2.756   1.00 12.96 ?  83  LEU   B CD1  1 
ATOM   5292 C CD2  . LEU   B 1 83  ? 48.329 -8.697  2.001   1.00 13.71 ?  83  LEU   B CD2  1 
ATOM   5293 H H    . LEU   B 1 83  ? 46.483 -11.167 -1.326  1.00 12.59 ?  83  LEU   B H    1 
ATOM   5294 H HA   . LEU   B 1 83  ? 47.832 -8.919  -0.675  1.00 12.49 ?  83  LEU   B HA   1 
ATOM   5295 H HB2  . LEU   B 1 83  ? 48.549 -11.501 0.187   1.00 13.27 ?  83  LEU   B HB2  1 
ATOM   5296 H HB3  . LEU   B 1 83  ? 49.560 -10.283 0.238   1.00 13.27 ?  83  LEU   B HB3  1 
ATOM   5297 H HG   . LEU   B 1 83  ? 47.166 -10.344 1.716   1.00 14.62 ?  83  LEU   B HG   1 
ATOM   5298 H HD11 . LEU   B 1 83  ? 48.408 -10.790 3.626   1.00 15.56 ?  83  LEU   B HD11 1 
ATOM   5299 H HD12 . LEU   B 1 83  ? 48.546 -11.977 2.578   1.00 15.56 ?  83  LEU   B HD12 1 
ATOM   5300 H HD13 . LEU   B 1 83  ? 49.720 -10.919 2.739   1.00 15.56 ?  83  LEU   B HD13 1 
ATOM   5301 H HD21 . LEU   B 1 83  ? 48.130 -8.539  2.938   1.00 16.45 ?  83  LEU   B HD21 1 
ATOM   5302 H HD22 . LEU   B 1 83  ? 49.250 -8.458  1.814   1.00 16.45 ?  83  LEU   B HD22 1 
ATOM   5303 H HD23 . LEU   B 1 83  ? 47.733 -8.167  1.446   1.00 16.45 ?  83  LEU   B HD23 1 
ATOM   5304 N N    . SER   B 1 84  ? 49.853 -9.652  -2.277  1.00 11.47 ?  84  SER   B N    1 
ATOM   5305 C CA   . SER   B 1 84  ? 50.583 -9.775  -3.529  1.00 11.70 ?  84  SER   B CA   1 
ATOM   5306 C C    . SER   B 1 84  ? 50.752 -11.240 -3.923  1.00 10.42 ?  84  SER   B C    1 
ATOM   5307 O O    . SER   B 1 84  ? 50.860 -12.127 -3.080  1.00 10.88 ?  84  SER   B O    1 
ATOM   5308 C CB   . SER   B 1 84  ? 51.967 -9.147  -3.391  1.00 13.62 ?  84  SER   B CB   1 
ATOM   5309 O OG   . SER   B 1 84  ? 52.722 -9.384  -4.564  1.00 15.38 ?  84  SER   B OG   1 
ATOM   5310 H H    . SER   B 1 84  ? 50.299 -9.318  -1.622  1.00 13.76 ?  84  SER   B H    1 
ATOM   5311 H HA   . SER   B 1 84  ? 50.101 -9.317  -4.236  1.00 14.04 ?  84  SER   B HA   1 
ATOM   5312 H HB2  . SER   B 1 84  ? 51.870 -8.188  -3.265  1.00 16.34 ?  84  SER   B HB2  1 
ATOM   5313 H HB3  . SER   B 1 84  ? 52.419 -9.537  -2.626  1.00 16.34 ?  84  SER   B HB3  1 
ATOM   5314 H HG   . SER   B 1 84  ? 53.490 -9.043  -4.483  1.00 18.45 ?  84  SER   B HG   1 
ATOM   5315 N N    . GLY   B 1 85  ? 50.812 -11.478 -5.226  1.00 11.57 ?  85  GLY   B N    1 
ATOM   5316 C CA   . GLY   B 1 85  ? 51.162 -12.774 -5.749  1.00 12.32 ?  85  GLY   B CA   1 
ATOM   5317 C C    . GLY   B 1 85  ? 52.630 -12.959 -6.056  1.00 11.67 ?  85  GLY   B C    1 
ATOM   5318 O O    . GLY   B 1 85  ? 53.013 -14.039 -6.509  1.00 12.31 ?  85  GLY   B O    1 
ATOM   5319 H H    . GLY   B 1 85  ? 50.658 -10.898 -5.836  1.00 13.88 ?  85  GLY   B H    1 
ATOM   5320 H HA2  . GLY   B 1 85  ? 50.905 -13.461 -5.106  1.00 14.79 ?  85  GLY   B HA2  1 
ATOM   5321 H HA3  . GLY   B 1 85  ? 50.667 -12.939 -6.565  1.00 14.79 ?  85  GLY   B HA3  1 
ATOM   5322 N N    . HIS   B 1 86  ? 53.476 -11.953 -5.840  1.00 11.80 ?  86  HIS   B N    1 
ATOM   5323 C CA   . HIS   B 1 86  ? 54.942 -12.112 -5.928  1.00 11.70 ?  86  HIS   B CA   1 
ATOM   5324 C C    . HIS   B 1 86  ? 55.317 -12.626 -7.317  1.00 12.10 ?  86  HIS   B C    1 
ATOM   5325 O O    . HIS   B 1 86  ? 54.922 -12.017 -8.322  1.00 12.88 ?  86  HIS   B O    1 
ATOM   5326 C CB   . HIS   B 1 86  ? 55.444 -12.948 -4.753  1.00 12.46 ?  86  HIS   B CB   1 
ATOM   5327 C CG   . HIS   B 1 86  ? 55.122 -12.344 -3.429  1.00 12.67 ?  86  HIS   B CG   1 
ATOM   5328 N ND1  . HIS   B 1 86  ? 55.938 -11.419 -2.815  1.00 14.17 ?  86  HIS   B ND1  1 
ATOM   5329 C CD2  . HIS   B 1 86  ? 54.050 -12.502 -2.616  1.00 12.59 ?  86  HIS   B CD2  1 
ATOM   5330 C CE1  . HIS   B 1 86  ? 55.379 -11.034 -1.680  1.00 14.14 ?  86  HIS   B CE1  1 
ATOM   5331 N NE2  . HIS   B 1 86  ? 54.229 -11.670 -1.540  1.00 13.19 ?  86  HIS   B NE2  1 
ATOM   5332 H H    . HIS   B 1 86  ? 53.226 -11.157 -5.639  1.00 14.16 ?  86  HIS   B H    1 
ATOM   5333 H HA   . HIS   B 1 86  ? 55.342 -11.238 -5.838  1.00 14.04 ?  86  HIS   B HA   1 
ATOM   5334 H HB2  . HIS   B 1 86  ? 55.038 -13.829 -4.789  1.00 14.95 ?  86  HIS   B HB2  1 
ATOM   5335 H HB3  . HIS   B 1 86  ? 56.412 -13.031 -4.813  1.00 14.95 ?  86  HIS   B HB3  1 
ATOM   5336 H HD2  . HIS   B 1 86  ? 53.317 -13.058 -2.773  1.00 15.11 ?  86  HIS   B HD2  1 
ATOM   5337 H HE1  . HIS   B 1 86  ? 55.740 -10.435 -1.070  1.00 16.97 ?  86  HIS   B HE1  1 
ATOM   5338 H HE2  . HIS   B 1 86  ? 53.691 -11.603 -0.871  1.00 15.83 ?  86  HIS   B HE2  1 
ATOM   5339 N N    . ASN   B 1 87  ? 56.090 -13.708 -7.423  1.00 12.61 ?  87  ASN   B N    1 
ATOM   5340 C CA   . ASN   B 1 87  ? 56.482 -14.289 -8.697  1.00 13.55 ?  87  ASN   B CA   1 
ATOM   5341 C C    . ASN   B 1 87  ? 55.494 -15.326 -9.202  1.00 12.85 ?  87  ASN   B C    1 
ATOM   5342 O O    . ASN   B 1 87  ? 55.798 -16.021 -10.176 1.00 14.80 ?  87  ASN   B O    1 
ATOM   5343 C CB   . ASN   B 1 87  ? 57.872 -14.926 -8.581  1.00 15.56 ?  87  ASN   B CB   1 
ATOM   5344 C CG   . ASN   B 1 87  ? 57.934 -16.016 -7.516  1.00 16.70 ?  87  ASN   B CG   1 
ATOM   5345 O OD1  . ASN   B 1 87  ? 57.286 -15.923 -6.472  1.00 15.28 ?  87  ASN   B OD1  1 
ATOM   5346 N ND2  . ASN   B 1 87  ? 58.706 -17.073 -7.790  1.00 18.77 ?  87  ASN   B ND2  1 
ATOM   5347 H H    . ASN   B 1 87  ? 56.397 -14.138 -6.749  1.00 15.13 ?  87  ASN   B H    1 
ATOM   5348 H HA   . ASN   B 1 87  ? 56.531 -13.587 -9.359  1.00 16.26 ?  87  ASN   B HA   1 
ATOM   5349 H HB2  . ASN   B 1 87  ? 58.110 -15.326 -9.435  1.00 18.67 ?  87  ASN   B HB2  1 
ATOM   5350 H HB3  . ASN   B 1 87  ? 58.512 -14.239 -8.348  1.00 18.67 ?  87  ASN   B HB3  1 
ATOM   5351 H HD21 . ASN   B 1 87  ? 58.786 -17.710 -7.220  1.00 22.52 ?  87  ASN   B HD21 1 
ATOM   5352 H HD22 . ASN   B 1 87  ? 59.148 -17.106 -8.532  1.00 22.52 ?  87  ASN   B HD22 1 
ATOM   5353 N N    . LEU   B 1 88  ? 54.321 -15.438 -8.578  1.00 11.92 ?  88  LEU   B N    1 
ATOM   5354 C CA   . LEU   B 1 88  ? 53.345 -16.470 -8.909  1.00 12.22 ?  88  LEU   B CA   1 
ATOM   5355 C C    . LEU   B 1 88  ? 52.113 -15.949 -9.627  1.00 12.03 ?  88  LEU   B C    1 
ATOM   5356 O O    . LEU   B 1 88  ? 51.517 -16.688 -10.418 1.00 13.93 ?  88  LEU   B O    1 
ATOM   5357 C CB   . LEU   B 1 88  ? 52.875 -17.156 -7.624  1.00 13.57 ?  88  LEU   B CB   1 
ATOM   5358 C CG   . LEU   B 1 88  ? 54.005 -17.806 -6.835  1.00 15.86 ?  88  LEU   B CG   1 
ATOM   5359 C CD1  . LEU   B 1 88  ? 53.523 -18.226 -5.460  1.00 17.48 ?  88  LEU   B CD1  1 
ATOM   5360 C CD2  . LEU   B 1 88  ? 54.550 -18.986 -7.612  1.00 19.44 ?  88  LEU   B CD2  1 
ATOM   5361 H H    . LEU   B 1 88  ? 54.062 -14.920 -7.937  1.00 14.31 ?  88  LEU   B H    1 
ATOM   5362 H HA   . LEU   B 1 88  ? 53.758 -17.135 -9.474  1.00 14.67 ?  88  LEU   B HA   1 
ATOM   5363 H HB2  . LEU   B 1 88  ? 52.448 -16.501 -7.048  1.00 16.28 ?  88  LEU   B HB2  1 
ATOM   5364 H HB3  . LEU   B 1 88  ? 52.232 -17.852 -7.853  1.00 16.28 ?  88  LEU   B HB3  1 
ATOM   5365 H HG   . LEU   B 1 88  ? 54.718 -17.162 -6.723  1.00 19.04 ?  88  LEU   B HG   1 
ATOM   5366 H HD11 . LEU   B 1 88  ? 54.244 -18.683 -5.002  1.00 20.98 ?  88  LEU   B HD11 1 
ATOM   5367 H HD12 . LEU   B 1 88  ? 53.260 -17.436 -4.963  1.00 20.98 ?  88  LEU   B HD12 1 
ATOM   5368 H HD13 . LEU   B 1 88  ? 52.764 -18.821 -5.562  1.00 20.98 ?  88  LEU   B HD13 1 
ATOM   5369 H HD21 . LEU   B 1 88  ? 55.161 -19.479 -7.044  1.00 23.32 ?  88  LEU   B HD21 1 
ATOM   5370 H HD22 . LEU   B 1 88  ? 53.812 -19.559 -7.878  1.00 23.32 ?  88  LEU   B HD22 1 
ATOM   5371 H HD23 . LEU   B 1 88  ? 55.016 -18.663 -8.399  1.00 23.32 ?  88  LEU   B HD23 1 
ATOM   5372 N N    . ALA   B 1 89  ? 51.705 -14.714 -9.352  1.00 11.83 ?  89  ALA   B N    1 
ATOM   5373 C CA   . ALA   B 1 89  ? 50.411 -14.215 -9.793  1.00 11.15 ?  89  ALA   B CA   1 
ATOM   5374 C C    . ALA   B 1 89  ? 50.396 -12.725 -9.511  1.00 11.22 ?  89  ALA   B C    1 
ATOM   5375 O O    . ALA   B 1 89  ? 51.232 -12.217 -8.766  1.00 12.12 ?  89  ALA   B O    1 
ATOM   5376 C CB   . ALA   B 1 89  ? 49.278 -14.888 -9.023  1.00 11.18 ?  89  ALA   B CB   1 
ATOM   5377 H H    . ALA   B 1 89  ? 52.157 -14.141 -8.899  1.00 14.20 ?  89  ALA   B H    1 
ATOM   5378 H HA   . ALA   B 1 89  ? 50.294 -14.374 -10.753 1.00 13.38 ?  89  ALA   B HA   1 
ATOM   5379 H HB1  . ALA   B 1 89  ? 48.430 -14.547 -9.352  1.00 13.42 ?  89  ALA   B HB1  1 
ATOM   5380 H HB2  . ALA   B 1 89  ? 49.324 -15.847 -9.166  1.00 13.42 ?  89  ALA   B HB2  1 
ATOM   5381 H HB3  . ALA   B 1 89  ? 49.379 -14.684 -8.085  1.00 13.42 ?  89  ALA   B HB3  1 
ATOM   5382 N N    . LYS   B 1 90  ? 49.424 -12.024 -10.087 1.00 12.04 ?  90  LYS   B N    1 
ATOM   5383 C CA   . LYS   B 1 90  ? 49.241 -10.637 -9.680  1.00 12.21 ?  90  LYS   B CA   1 
ATOM   5384 C C    . LYS   B 1 90  ? 48.909 -10.561 -8.195  1.00 12.04 ?  90  LYS   B C    1 
ATOM   5385 O O    . LYS   B 1 90  ? 49.554 -9.820  -7.441  1.00 12.80 ?  90  LYS   B O    1 
ATOM   5386 C CB   . LYS   B 1 90  ? 48.168 -9.969  -10.537 1.00 13.83 ?  90  LYS   B CB   1 
ATOM   5387 C CG   . LYS   B 1 90  ? 47.859 -8.537  -10.134 1.00 14.59 ?  90  LYS   B CG   1 
ATOM   5388 C CD   . LYS   B 1 90  ? 49.064 -7.627  -10.209 1.00 17.07 ?  90  LYS   B CD   1 
ATOM   5389 C CE   . LYS   B 1 90  ? 48.600 -6.211  -9.969  1.00 20.03 ?  90  LYS   B CE   1 
ATOM   5390 N NZ   . LYS   B 1 90  ? 49.732 -5.264  -9.835  1.00 19.81 ?  90  LYS   B NZ   1 
ATOM   5391 H H    . LYS   B 1 90  ? 48.878 -12.318 -10.683 1.00 14.45 ?  90  LYS   B H    1 
ATOM   5392 H HA   . LYS   B 1 90  ? 50.072 -10.163 -9.820  1.00 14.65 ?  90  LYS   B HA   1 
ATOM   5393 H HB2  . LYS   B 1 90  ? 48.469 -9.957  -11.461 1.00 16.60 ?  90  LYS   B HB2  1 
ATOM   5394 H HB3  . LYS   B 1 90  ? 47.347 -10.482 -10.470 1.00 16.60 ?  90  LYS   B HB3  1 
ATOM   5395 H HG2  . LYS   B 1 90  ? 47.181 -8.183  -10.732 1.00 17.50 ?  90  LYS   B HG2  1 
ATOM   5396 H HG3  . LYS   B 1 90  ? 47.525 -8.525  -9.222  1.00 17.50 ?  90  LYS   B HG3  1 
ATOM   5397 H HD2  . LYS   B 1 90  ? 49.704 -7.867  -9.518  1.00 20.49 ?  90  LYS   B HD2  1 
ATOM   5398 H HD3  . LYS   B 1 90  ? 49.468 -7.682  -11.088 1.00 20.49 ?  90  LYS   B HD3  1 
ATOM   5399 H HE2  . LYS   B 1 90  ? 48.055 -5.921  -10.719 1.00 24.04 ?  90  LYS   B HE2  1 
ATOM   5400 H HE3  . LYS   B 1 90  ? 48.083 -6.175  -9.149  1.00 24.04 ?  90  LYS   B HE3  1 
ATOM   5401 H HZ1  . LYS   B 1 90  ? 49.430 -4.438  -9.697  1.00 23.77 ?  90  LYS   B HZ1  1 
ATOM   5402 H HZ2  . LYS   B 1 90  ? 50.249 -5.499  -9.150  1.00 23.77 ?  90  LYS   B HZ2  1 
ATOM   5403 H HZ3  . LYS   B 1 90  ? 50.224 -5.268  -10.580 1.00 23.77 ?  90  LYS   B HZ3  1 
ATOM   5404 N N    . HIS   B 1 91  ? 47.942 -11.369 -7.750  1.00 10.46 ?  91  HIS   B N    1 
ATOM   5405 C CA   . HIS   B 1 91  ? 47.476 -11.391 -6.376  1.00 10.90 ?  91  HIS   B CA   1 
ATOM   5406 C C    . HIS   B 1 91  ? 47.465 -12.819 -5.854  1.00 10.26 ?  91  HIS   B C    1 
ATOM   5407 O O    . HIS   B 1 91  ? 47.225 -13.770 -6.612  1.00 10.65 ?  91  HIS   B O    1 
ATOM   5408 C CB   . HIS   B 1 91  ? 46.026 -10.910 -6.258  1.00 12.77 ?  91  HIS   B CB   1 
ATOM   5409 C CG   . HIS   B 1 91  ? 45.816 -9.499  -6.685  1.00 16.04 ?  91  HIS   B CG   1 
ATOM   5410 N ND1  . HIS   B 1 91  ? 46.414 -8.427  -6.057  1.00 18.61 ?  91  HIS   B ND1  1 
ATOM   5411 C CD2  . HIS   B 1 91  ? 45.036 -8.979  -7.659  1.00 18.29 ?  91  HIS   B CD2  1 
ATOM   5412 C CE1  . HIS   B 1 91  ? 46.030 -7.307  -6.644  1.00 19.87 ?  91  HIS   B CE1  1 
ATOM   5413 N NE2  . HIS   B 1 91  ? 45.188 -7.614  -7.614  1.00 19.79 ?  91  HIS   B NE2  1 
ATOM   5414 H H    . HIS   B 1 91  ? 47.522 -11.932 -8.251  1.00 12.55 ?  91  HIS   B H    1 
ATOM   5415 H HA   . HIS   B 1 91  ? 48.046 -10.839 -5.811  1.00 13.08 ?  91  HIS   B HA   1 
ATOM   5416 H HB2  . HIS   B 1 91  ? 45.465 -11.474 -6.812  1.00 15.32 ?  91  HIS   B HB2  1 
ATOM   5417 H HB3  . HIS   B 1 91  ? 45.746 -10.984 -5.330  1.00 15.32 ?  91  HIS   B HB3  1 
ATOM   5418 H HD1  . HIS   B 1 91  ? 46.958 -8.478  -5.393  1.00 22.33 ?  91  HIS   B HD1  1 
ATOM   5419 H HD2  . HIS   B 1 91  ? 44.503 -9.453  -8.256  1.00 21.94 ?  91  HIS   B HD2  1 
ATOM   5420 H HE1  . HIS   B 1 91  ? 46.296 -6.446  -6.405  1.00 23.84 ?  91  HIS   B HE1  1 
ATOM   5421 N N    . CYS   B 1 92  ? 47.655 -12.954 -4.549  1.00 9.69  ?  92  CYS   B N    1 
ATOM   5422 C CA   . CYS   B 1 92  ? 47.353 -14.188 -3.833  1.00 9.90  ?  92  CYS   B CA   1 
ATOM   5423 C C    . CYS   B 1 92  ? 46.128 -13.945 -2.958  1.00 9.72  ?  92  CYS   B C    1 
ATOM   5424 O O    . CYS   B 1 92  ? 46.125 -13.036 -2.119  1.00 10.62 ?  92  CYS   B O    1 
ATOM   5425 C CB   . CYS   B 1 92  ? 48.534 -14.654 -2.987  1.00 10.42 ?  92  CYS   B CB   1 
ATOM   5426 S SG   . CYS   B 1 92  ? 48.158 -16.175 -2.079  1.00 10.62 ?  92  CYS   B SG   1 
ATOM   5427 H H    . CYS   B 1 92  ? 47.979 -12.331 -4.044  1.00 11.63 ?  92  CYS   B H    1 
ATOM   5428 H HA   . CYS   B 1 92  ? 47.148 -14.881 -4.480  1.00 11.88 ?  92  CYS   B HA   1 
ATOM   5429 H HB2  . CYS   B 1 92  ? 49.292 -14.825 -3.566  1.00 12.50 ?  92  CYS   B HB2  1 
ATOM   5430 H HB3  . CYS   B 1 92  ? 48.752 -13.964 -2.344  1.00 12.50 ?  92  CYS   B HB3  1 
ATOM   5431 H HG   . CYS   B 1 92  ? 49.132 -16.499 -1.456  1.00 12.75 ?  92  CYS   B HG   1 
ATOM   5432 N N    . LEU   B 1 93  ? 45.088 -14.751 -3.169  1.00 9.58  ?  93  LEU   B N    1 
ATOM   5433 C CA   . LEU   B 1 93  ? 43.908 -14.766 -2.312  1.00 9.77  ?  93  LEU   B CA   1 
ATOM   5434 C C    . LEU   B 1 93  ? 44.125 -15.824 -1.240  1.00 8.99  ?  93  LEU   B C    1 
ATOM   5435 O O    . LEU   B 1 93  ? 44.082 -17.026 -1.528  1.00 9.72  ?  93  LEU   B O    1 
ATOM   5436 C CB   . LEU   B 1 93  ? 42.644 -15.055 -3.118  1.00 9.62  ?  93  LEU   B CB   1 
ATOM   5437 C CG   . LEU   B 1 93  ? 41.341 -15.062 -2.310  1.00 10.89 ?  93  LEU   B CG   1 
ATOM   5438 C CD1  . LEU   B 1 93  ? 40.977 -13.668 -1.810  1.00 11.24 ?  93  LEU   B CD1  1 
ATOM   5439 C CD2  . LEU   B 1 93  ? 40.208 -15.645 -3.130  1.00 11.27 ?  93  LEU   B CD2  1 
ATOM   5440 H H    . LEU   B 1 93  ? 45.045 -15.325 -3.822  1.00 11.49 ?  93  LEU   B H    1 
ATOM   5441 H HA   . LEU   B 1 93  ? 43.814 -13.899 -1.889  1.00 11.72 ?  93  LEU   B HA   1 
ATOM   5442 H HB2  . LEU   B 1 93  ? 42.554 -14.371 -3.803  1.00 11.55 ?  93  LEU   B HB2  1 
ATOM   5443 H HB3  . LEU   B 1 93  ? 42.734 -15.921 -3.533  1.00 11.55 ?  93  LEU   B HB3  1 
ATOM   5444 H HG   . LEU   B 1 93  ? 41.461 -15.627 -1.533  1.00 13.07 ?  93  LEU   B HG   1 
ATOM   5445 H HD11 . LEU   B 1 93  ? 40.129 -13.713 -1.346  1.00 13.48 ?  93  LEU   B HD11 1 
ATOM   5446 H HD12 . LEU   B 1 93  ? 41.671 -13.354 -1.215  1.00 13.48 ?  93  LEU   B HD12 1 
ATOM   5447 H HD13 . LEU   B 1 93  ? 40.902 -13.072 -2.576  1.00 13.48 ?  93  LEU   B HD13 1 
ATOM   5448 H HD21 . LEU   B 1 93  ? 39.394 -15.624 -2.603  1.00 13.52 ?  93  LEU   B HD21 1 
ATOM   5449 H HD22 . LEU   B 1 93  ? 40.095 -15.115 -3.936  1.00 13.52 ?  93  LEU   B HD22 1 
ATOM   5450 H HD23 . LEU   B 1 93  ? 40.427 -16.560 -3.365  1.00 13.52 ?  93  LEU   B HD23 1 
ATOM   5451 N N    . HIS   B 1 94  ? 44.397 -15.380 -0.018  1.00 9.21  ?  94  HIS   B N    1 
ATOM   5452 C CA   . HIS   B 1 94  ? 44.618 -16.279 1.105   1.00 9.29  ?  94  HIS   B CA   1 
ATOM   5453 C C    . HIS   B 1 94  ? 43.255 -16.624 1.689   1.00 9.83  ?  94  HIS   B C    1 
ATOM   5454 O O    . HIS   B 1 94  ? 42.591 -15.747 2.243   1.00 10.83 ?  94  HIS   B O    1 
ATOM   5455 C CB   . HIS   B 1 94  ? 45.488 -15.601 2.159   1.00 10.09 ?  94  HIS   B CB   1 
ATOM   5456 C CG   . HIS   B 1 94  ? 46.872 -15.303 1.688   1.00 9.76  ?  94  HIS   B CG   1 
ATOM   5457 N ND1  . HIS   B 1 94  ? 47.899 -16.216 1.777   1.00 9.75  ?  94  HIS   B ND1  1 
ATOM   5458 C CD2  . HIS   B 1 94  ? 47.383 -14.199 1.089   1.00 10.16 ?  94  HIS   B CD2  1 
ATOM   5459 C CE1  . HIS   B 1 94  ? 48.990 -15.677 1.266   1.00 10.09 ?  94  HIS   B CE1  1 
ATOM   5460 N NE2  . HIS   B 1 94  ? 48.706 -14.456 0.841   1.00 10.18 ?  94  HIS   B NE2  1 
ATOM   5461 H H    . HIS   B 1 94  ? 44.466 -14.537 0.188   1.00 11.05 ?  94  HIS   B H    1 
ATOM   5462 H HA   . HIS   B 1 94  ? 45.052 -17.088 0.797   1.00 11.15 ?  94  HIS   B HA   1 
ATOM   5463 H HB2  . HIS   B 1 94  ? 45.072 -14.761 2.410   1.00 12.10 ?  94  HIS   B HB2  1 
ATOM   5464 H HB3  . HIS   B 1 94  ? 45.554 -16.183 2.926   1.00 12.10 ?  94  HIS   B HB3  1 
ATOM   5465 H HD2  . HIS   B 1 94  ? 46.930 -13.416 0.886   1.00 12.19 ?  94  HIS   B HD2  1 
ATOM   5466 H HE1  . HIS   B 1 94  ? 49.818 -16.101 1.213   1.00 12.11 ?  94  HIS   B HE1  1 
ATOM   5467 H HE2  . HIS   B 1 94  ? 49.265 -13.923 0.474   1.00 12.22 ?  94  HIS   B HE2  1 
ATOM   5468 N N    . VAL   B 1 95  ? 42.820 -17.879 1.541   1.00 9.62  ?  95  VAL   B N    1 
ATOM   5469 C CA   . VAL   B 1 95  ? 41.492 -18.315 1.976   1.00 9.94  ?  95  VAL   B CA   1 
ATOM   5470 C C    . VAL   B 1 95  ? 41.656 -19.347 3.075   1.00 10.07 ?  95  VAL   B C    1 
ATOM   5471 O O    . VAL   B 1 95  ? 42.427 -20.301 2.923   1.00 10.72 ?  95  VAL   B O    1 
ATOM   5472 C CB   . VAL   B 1 95  ? 40.671 -18.921 0.823   1.00 10.05 ?  95  VAL   B CB   1 
ATOM   5473 C CG1  . VAL   B 1 95  ? 39.300 -19.365 1.312   1.00 11.37 ?  95  VAL   B CG1  1 
ATOM   5474 C CG2  . VAL   B 1 95  ? 40.545 -17.944 -0.318  1.00 10.19 ?  95  VAL   B CG2  1 
ATOM   5475 H H    . VAL   B 1 95  ? 43.283 -18.509 1.177   1.00 11.55 ?  95  VAL   B H    1 
ATOM   5476 H HA   . VAL   B 1 95  ? 41.003 -17.558 2.333   1.00 11.93 ?  95  VAL   B HA   1 
ATOM   5477 H HB   . VAL   B 1 95  ? 41.131 -19.702 0.486   1.00 12.06 ?  95  VAL   B HB   1 
ATOM   5478 H HG11 . VAL   B 1 95  ? 38.729 -19.547 0.545   1.00 13.64 ?  95  VAL   B HG11 1 
ATOM   5479 H HG12 . VAL   B 1 95  ? 39.393 -20.170 1.845   1.00 13.64 ?  95  VAL   B HG12 1 
ATOM   5480 H HG13 . VAL   B 1 95  ? 38.905 -18.658 1.848   1.00 13.64 ?  95  VAL   B HG13 1 
ATOM   5481 H HG21 . VAL   B 1 95  ? 39.971 -18.332 -0.998  1.00 12.23 ?  95  VAL   B HG21 1 
ATOM   5482 H HG22 . VAL   B 1 95  ? 40.158 -17.122 0.015   1.00 12.23 ?  95  VAL   B HG22 1 
ATOM   5483 H HG23 . VAL   B 1 95  ? 41.425 -17.778 -0.683  1.00 12.23 ?  95  VAL   B HG23 1 
ATOM   5484 N N    . VAL   B 1 96  ? 40.923 -19.169 4.165   1.00 10.45 ?  96  VAL   B N    1 
ATOM   5485 C CA   . VAL   B 1 96  ? 41.005 -20.076 5.306   1.00 11.09 ?  96  VAL   B CA   1 
ATOM   5486 C C    . VAL   B 1 96  ? 39.819 -21.037 5.260   1.00 11.92 ?  96  VAL   B C    1 
ATOM   5487 O O    . VAL   B 1 96  ? 38.698 -20.690 5.644   1.00 12.33 ?  96  VAL   B O    1 
ATOM   5488 C CB   . VAL   B 1 96  ? 41.061 -19.323 6.638   1.00 11.75 ?  96  VAL   B CB   1 
ATOM   5489 C CG1  . VAL   B 1 96  ? 41.233 -20.312 7.784   1.00 12.61 ?  96  VAL   B CG1  1 
ATOM   5490 C CG2  . VAL   B 1 96  ? 42.180 -18.292 6.632   1.00 12.54 ?  96  VAL   B CG2  1 
ATOM   5491 H H    . VAL   B 1 96  ? 40.360 -18.525 4.271   1.00 12.53 ?  96  VAL   B H    1 
ATOM   5492 H HA   . VAL   B 1 96  ? 41.816 -20.600 5.233   1.00 13.31 ?  96  VAL   B HA   1 
ATOM   5493 H HB   . VAL   B 1 96  ? 40.220 -18.855 6.773   1.00 14.10 ?  96  VAL   B HB   1 
ATOM   5494 H HG11 . VAL   B 1 96  ? 41.428 -19.821 8.601   1.00 15.13 ?  96  VAL   B HG11 1 
ATOM   5495 H HG12 . VAL   B 1 96  ? 40.414 -20.821 7.899   1.00 15.13 ?  96  VAL   B HG12 1 
ATOM   5496 H HG13 . VAL   B 1 96  ? 41.968 -20.911 7.582   1.00 15.13 ?  96  VAL   B HG13 1 
ATOM   5497 H HG21 . VAL   B 1 96  ? 42.238 -17.882 7.511   1.00 15.04 ?  96  VAL   B HG21 1 
ATOM   5498 H HG22 . VAL   B 1 96  ? 43.014 -18.729 6.414   1.00 15.04 ?  96  VAL   B HG22 1 
ATOM   5499 H HG23 . VAL   B 1 96  ? 41.978 -17.611 5.967   1.00 15.04 ?  96  VAL   B HG23 1 
ATOM   5500 N N    . GLY   B 1 97  ? 40.056 -22.268 4.818   1.00 11.51 ?  97  GLY   B N    1 
ATOM   5501 C CA   . GLY   B 1 97  ? 39.086 -23.329 4.984   1.00 12.35 ?  97  GLY   B CA   1 
ATOM   5502 C C    . GLY   B 1 97  ? 39.217 -23.935 6.364   1.00 13.61 ?  97  GLY   B C    1 
ATOM   5503 O O    . GLY   B 1 97  ? 40.260 -23.813 7.022   1.00 14.20 ?  97  GLY   B O    1 
ATOM   5504 H H    . GLY   B 1 97  ? 40.779 -22.507 4.406   1.00 13.81 ?  97  GLY   B H    1 
ATOM   5505 H HA2  . GLY   B 1 97  ? 38.191 -22.965 4.861   1.00 14.82 ?  97  GLY   B HA2  1 
ATOM   5506 H HA3  . GLY   B 1 97  ? 39.233 -24.017 4.312   1.00 14.82 ?  97  GLY   B HA3  1 
ATOM   5507 N N    . PRO   B 1 98  ? 38.162 -24.599 6.839   1.00 14.66 ?  98  PRO   B N    1 
ATOM   5508 C CA   . PRO   B 1 98  ? 38.257 -25.294 8.126   1.00 16.10 ?  98  PRO   B CA   1 
ATOM   5509 C C    . PRO   B 1 98  ? 39.281 -26.417 8.078   1.00 15.93 ?  98  PRO   B C    1 
ATOM   5510 O O    . PRO   B 1 98  ? 39.375 -27.162 7.103   1.00 16.31 ?  98  PRO   B O    1 
ATOM   5511 C CB   . PRO   B 1 98  ? 36.837 -25.834 8.339   1.00 16.61 ?  98  PRO   B CB   1 
ATOM   5512 C CG   . PRO   B 1 98  ? 36.261 -25.960 6.975   1.00 16.21 ?  98  PRO   B CG   1 
ATOM   5513 C CD   . PRO   B 1 98  ? 36.845 -24.802 6.200   1.00 15.14 ?  98  PRO   B CD   1 
ATOM   5514 H HA   . PRO   B 1 98  ? 38.480 -24.666 8.828   1.00 19.31 ?  98  PRO   B HA   1 
ATOM   5515 H HB2  . PRO   B 1 98  ? 36.883 -26.699 8.774   1.00 19.93 ?  98  PRO   B HB2  1 
ATOM   5516 H HB3  . PRO   B 1 98  ? 36.324 -25.207 8.867   1.00 19.93 ?  98  PRO   B HB3  1 
ATOM   5517 H HG2  . PRO   B 1 98  ? 36.532 -26.812 6.586   1.00 19.45 ?  98  PRO   B HG2  1 
ATOM   5518 H HG3  . PRO   B 1 98  ? 35.295 -25.900 7.022   1.00 19.45 ?  98  PRO   B HG3  1 
ATOM   5519 H HD2  . PRO   B 1 98  ? 36.948 -25.044 5.260   1.00 18.16 ?  98  PRO   B HD2  1 
ATOM   5520 H HD3  . PRO   B 1 98  ? 36.290 -24.014 6.300   1.00 18.16 ?  98  PRO   B HD3  1 
ATOM   5521 N N    . ASN   B 1 99  ? 40.050 -26.535 9.153   1.00 17.01 ?  99  ASN   B N    1 
ATOM   5522 C CA   . ASN   B 1 99  ? 41.020 -27.616 9.321   1.00 18.35 ?  99  ASN   B CA   1 
ATOM   5523 C C    . ASN   B 1 99  ? 40.395 -28.690 10.212  1.00 21.05 ?  99  ASN   B C    1 
ATOM   5524 O O    . ASN   B 1 99  ? 40.329 -28.536 11.435  1.00 21.78 ?  99  ASN   B O    1 
ATOM   5525 C CB   . ASN   B 1 99  ? 42.305 -27.063 9.924   1.00 18.65 ?  99  ASN   B CB   1 
ATOM   5526 C CG   . ASN   B 1 99  ? 43.435 -28.075 9.928   1.00 19.14 ?  99  ASN   B CG   1 
ATOM   5527 O OD1  . ASN   B 1 99  ? 43.215 -29.267 10.113  1.00 20.26 ?  99  ASN   B OD1  1 
ATOM   5528 N ND2  . ASN   B 1 99  ? 44.652 -27.603 9.719   1.00 19.47 ?  99  ASN   B ND2  1 
ATOM   5529 H H    . ASN   B 1 99  ? 40.027 -25.985 9.814   1.00 20.41 ?  99  ASN   B H    1 
ATOM   5530 H HA   . ASN   B 1 99  ? 41.218 -28.011 8.458   1.00 22.03 ?  99  ASN   B HA   1 
ATOM   5531 H HB2  . ASN   B 1 99  ? 42.583 -26.296 9.412   1.00 22.38 ?  99  ASN   B HB2  1 
ATOM   5532 H HB3  . ASN   B 1 99  ? 42.126 -26.809 10.845  1.00 22.38 ?  99  ASN   B HB3  1 
ATOM   5533 H HD21 . ASN   B 1 99  ? 45.322 -28.137 9.710   1.00 23.37 ?  99  ASN   B HD21 1 
ATOM   5534 H HD22 . ASN   B 1 99  ? 44.763 -26.760 9.603   1.00 23.37 ?  99  ASN   B HD22 1 
ATOM   5535 N N    A VAL   B 1 100 ? 39.920 -29.774 9.591   0.42 23.09 ?  100 VAL   B N    1 
ATOM   5536 N N    B VAL   B 1 100 ? 39.936 -29.779 9.587   0.58 23.04 ?  100 VAL   B N    1 
ATOM   5537 C CA   A VAL   B 1 100 ? 39.311 -30.859 10.358  0.42 25.66 ?  100 VAL   B CA   1 
ATOM   5538 C CA   B VAL   B 1 100 ? 39.313 -30.869 10.335  0.58 25.77 ?  100 VAL   B CA   1 
ATOM   5539 C C    A VAL   B 1 100 ? 40.331 -31.514 11.282  0.42 26.28 ?  100 VAL   B C    1 
ATOM   5540 C C    B VAL   B 1 100 ? 40.322 -31.552 11.253  0.58 26.21 ?  100 VAL   B C    1 
ATOM   5541 O O    A VAL   B 1 100 ? 39.981 -31.979 12.374  0.42 27.19 ?  100 VAL   B O    1 
ATOM   5542 O O    B VAL   B 1 100 ? 39.952 -32.084 12.307  0.58 27.04 ?  100 VAL   B O    1 
ATOM   5543 C CB   A VAL   B 1 100 ? 38.639 -31.877 9.413   0.42 27.54 ?  100 VAL   B CB   1 
ATOM   5544 C CB   B VAL   B 1 100 ? 38.642 -31.861 9.365   0.58 28.03 ?  100 VAL   B CB   1 
ATOM   5545 C CG1  A VAL   B 1 100 ? 38.153 -33.093 10.188  0.42 27.99 ?  100 VAL   B CG1  1 
ATOM   5546 C CG1  B VAL   B 1 100 ? 38.193 -33.116 10.099  0.58 28.59 ?  100 VAL   B CG1  1 
ATOM   5547 C CG2  A VAL   B 1 100 ? 37.480 -31.223 8.671   0.42 28.10 ?  100 VAL   B CG2  1 
ATOM   5548 C CG2  B VAL   B 1 100 ? 37.461 -31.198 8.672   0.58 28.64 ?  100 VAL   B CG2  1 
ATOM   5549 H H    A VAL   B 1 100 ? 39.930 -29.897 8.736   0.42 27.71 ?  100 VAL   B H    1 
ATOM   5550 H H    B VAL   B 1 100 ? 39.968 -29.904 8.733   0.58 27.65 ?  100 VAL   B H    1 
ATOM   5551 H HA   A VAL   B 1 100 ? 38.610 -30.481 10.913  0.42 30.79 ?  100 VAL   B HA   1 
ATOM   5552 H HA   B VAL   B 1 100 ? 38.611 -30.495 10.890  0.58 30.92 ?  100 VAL   B HA   1 
ATOM   5553 H HB   A VAL   B 1 100 ? 39.286 -32.180 8.757   0.42 33.05 ?  100 VAL   B HB   1 
ATOM   5554 H HB   B VAL   B 1 100 ? 39.281 -32.126 8.685   0.58 33.63 ?  100 VAL   B HB   1 
ATOM   5555 H HG11 A VAL   B 1 100 ? 37.550 -33.604 9.625   0.42 33.59 ?  100 VAL   B HG11 1 
ATOM   5556 H HG11 B VAL   B 1 100 ? 37.581 -33.611 9.529   0.58 34.31 ?  100 VAL   B HG11 1 
ATOM   5557 H HG12 A VAL   B 1 100 ? 38.915 -33.640 10.435  0.42 33.59 ?  100 VAL   B HG12 1 
ATOM   5558 H HG12 B VAL   B 1 100 ? 38.968 -33.663 10.301  0.58 34.31 ?  100 VAL   B HG12 1 
ATOM   5559 H HG13 A VAL   B 1 100 ? 37.686 -32.793 10.984  0.42 33.59 ?  100 VAL   B HG13 1 
ATOM   5560 H HG13 B VAL   B 1 100 ? 37.743 -32.859 10.918  0.58 34.31 ?  100 VAL   B HG13 1 
ATOM   5561 H HG21 A VAL   B 1 100 ? 37.059 -31.883 8.097   0.42 33.72 ?  100 VAL   B HG21 1 
ATOM   5562 H HG21 B VAL   B 1 100 ? 37.044 -31.839 8.075   0.58 34.37 ?  100 VAL   B HG21 1 
ATOM   5563 H HG22 A VAL   B 1 100 ? 36.837 -30.893 9.320   0.42 33.72 ?  100 VAL   B HG22 1 
ATOM   5564 H HG22 B VAL   B 1 100 ? 36.823 -30.911 9.345   0.58 34.37 ?  100 VAL   B HG22 1 
ATOM   5565 H HG23 A VAL   B 1 100 ? 37.820 -30.489 8.138   0.42 33.72 ?  100 VAL   B HG23 1 
ATOM   5566 H HG23 B VAL   B 1 100 ? 37.779 -30.434 8.169   0.58 34.37 ?  100 VAL   B HG23 1 
ATOM   5567 N N    . ASN   B 1 101 ? 41.599 -31.573 10.868  1.00 26.16 ?  101 ASN   B N    1 
ATOM   5568 C CA   . ASN   B 1 101 ? 42.641 -32.114 11.738  1.00 27.61 ?  101 ASN   B CA   1 
ATOM   5569 C C    . ASN   B 1 101 ? 42.857 -31.273 12.990  1.00 29.57 ?  101 ASN   B C    1 
ATOM   5570 O O    . ASN   B 1 101 ? 43.506 -31.749 13.932  1.00 31.17 ?  101 ASN   B O    1 
ATOM   5571 C CB   . ASN   B 1 101 ? 43.955 -32.269 10.969  1.00 27.45 ?  101 ASN   B CB   1 
ATOM   5572 C CG   . ASN   B 1 101 ? 43.924 -33.433 9.995   1.00 27.11 ?  101 ASN   B CG   1 
ATOM   5573 O OD1  . ASN   B 1 101 ? 43.210 -34.410 10.207  1.00 28.14 ?  101 ASN   B OD1  1 
ATOM   5574 N ND2  . ASN   B 1 101 ? 44.691 -33.327 8.917   1.00 26.58 ?  101 ASN   B ND2  1 
ATOM   5575 H H    A ASN   B 1 101 ? 41.872 -31.322 10.093  0.42 31.39 ?  101 ASN   B H    1 
ATOM   5576 H H    B ASN   B 1 101 ? 41.879 -31.299 10.103  0.58 31.39 ?  101 ASN   B H    1 
ATOM   5577 H HA   . ASN   B 1 101 ? 42.367 -32.992 12.031  1.00 33.14 ?  101 ASN   B HA   1 
ATOM   5578 H HB2  . ASN   B 1 101 ? 44.130 -31.460 10.463  1.00 32.94 ?  101 ASN   B HB2  1 
ATOM   5579 H HB3  . ASN   B 1 101 ? 44.673 -32.428 11.600  1.00 32.94 ?  101 ASN   B HB3  1 
ATOM   5580 H HD21 . ASN   B 1 101 ? 44.707 -33.962 8.337   1.00 31.90 ?  101 ASN   B HD21 1 
ATOM   5581 H HD22 . ASN   B 1 101 ? 45.177 -32.627 8.803   1.00 31.90 ?  101 ASN   B HD22 1 
ATOM   5582 N N    . LYS   B 1 102 ? 42.340 -30.043 13.018  1.00 31.96 ?  102 LYS   B N    1 
ATOM   5583 C CA   . LYS   B 1 102 ? 42.304 -29.217 14.217  1.00 34.87 ?  102 LYS   B CA   1 
ATOM   5584 C C    . LYS   B 1 102 ? 40.914 -29.164 14.838  1.00 34.53 ?  102 LYS   B C    1 
ATOM   5585 O O    . LYS   B 1 102 ? 40.676 -28.345 15.730  1.00 34.99 ?  102 LYS   B O    1 
ATOM   5586 C CB   . LYS   B 1 102 ? 42.762 -27.793 13.899  1.00 38.07 ?  102 LYS   B CB   1 
ATOM   5587 C CG   . LYS   B 1 102 ? 44.223 -27.649 13.515  1.00 41.45 ?  102 LYS   B CG   1 
ATOM   5588 C CD   . LYS   B 1 102 ? 44.484 -26.233 13.023  1.00 44.03 ?  102 LYS   B CD   1 
ATOM   5589 C CE   . LYS   B 1 102 ? 45.965 -25.925 12.903  1.00 46.21 ?  102 LYS   B CE   1 
ATOM   5590 N NZ   . LYS   B 1 102 ? 46.182 -24.522 12.437  1.00 47.37 ?  102 LYS   B NZ   1 
ATOM   5591 H H    . LYS   B 1 102 ? 41.990 -29.654 12.333  1.00 38.35 ?  102 LYS   B H    1 
ATOM   5592 H HA   . LYS   B 1 102 ? 42.914 -29.586 14.873  1.00 41.85 ?  102 LYS   B HA   1 
ATOM   5593 H HB2  . LYS   B 1 102 ? 42.232 -27.456 13.160  1.00 45.68 ?  102 LYS   B HB2  1 
ATOM   5594 H HB3  . LYS   B 1 102 ? 42.613 -27.239 14.683  1.00 45.68 ?  102 LYS   B HB3  1 
ATOM   5595 H HG2  . LYS   B 1 102 ? 44.783 -27.816 14.290  1.00 49.74 ?  102 LYS   B HG2  1 
ATOM   5596 H HG3  . LYS   B 1 102 ? 44.436 -28.270 12.800  1.00 49.74 ?  102 LYS   B HG3  1 
ATOM   5597 H HD2  . LYS   B 1 102 ? 44.081 -26.123 12.147  1.00 52.84 ?  102 LYS   B HD2  1 
ATOM   5598 H HD3  . LYS   B 1 102 ? 44.094 -25.603 13.650  1.00 52.84 ?  102 LYS   B HD3  1 
ATOM   5599 H HE2  . LYS   B 1 102 ? 46.387 -26.028 13.771  1.00 55.45 ?  102 LYS   B HE2  1 
ATOM   5600 H HE3  . LYS   B 1 102 ? 46.368 -26.527 12.258  1.00 55.45 ?  102 LYS   B HE3  1 
ATOM   5601 H HZ1  . LYS   B 1 102 ? 47.053 -24.354 12.371  1.00 56.84 ?  102 LYS   B HZ1  1 
ATOM   5602 H HZ2  . LYS   B 1 102 ? 45.803 -24.405 11.640  1.00 56.84 ?  102 LYS   B HZ2  1 
ATOM   5603 H HZ3  . LYS   B 1 102 ? 45.820 -23.950 13.016  1.00 56.84 ?  102 LYS   B HZ3  1 
ATOM   5604 N N    . GLY   B 1 103 ? 39.987 -29.997 14.371  1.00 33.58 ?  103 GLY   B N    1 
ATOM   5605 C CA   . GLY   B 1 103 ? 38.656 -30.052 14.939  1.00 33.49 ?  103 GLY   B CA   1 
ATOM   5606 C C    . GLY   B 1 103 ? 37.712 -28.956 14.499  1.00 32.71 ?  103 GLY   B C    1 
ATOM   5607 O O    . GLY   B 1 103 ? 36.640 -28.811 15.098  1.00 33.11 ?  103 GLY   B O    1 
ATOM   5608 H H    . GLY   B 1 103 ? 40.109 -30.540 13.718  1.00 40.29 ?  103 GLY   B H    1 
ATOM   5609 H HA2  . GLY   B 1 103 ? 38.253 -30.904 14.707  1.00 40.19 ?  103 GLY   B HA2  1 
ATOM   5610 H HA3  . GLY   B 1 103 ? 38.725 -30.008 15.905  1.00 40.19 ?  103 GLY   B HA3  1 
ATOM   5611 N N    A GLU   B 1 104 ? 38.081 -28.169 13.492  0.42 32.07 ?  104 GLU   B N    1 
ATOM   5612 N N    B GLU   B 1 104 ? 38.055 -28.197 13.462  0.58 31.28 ?  104 GLU   B N    1 
ATOM   5613 C CA   A GLU   B 1 104 ? 37.241 -27.067 13.053  0.42 31.51 ?  104 GLU   B CA   1 
ATOM   5614 C CA   B GLU   B 1 104 ? 37.192 -27.119 13.006  0.58 30.06 ?  104 GLU   B CA   1 
ATOM   5615 C C    A GLU   B 1 104 ? 36.047 -27.585 12.252  0.42 31.63 ?  104 GLU   B C    1 
ATOM   5616 C C    B GLU   B 1 104 ? 36.020 -27.667 12.191  0.58 29.97 ?  104 GLU   B C    1 
ATOM   5617 O O    A GLU   B 1 104 ? 36.078 -28.671 11.665  0.42 31.90 ?  104 GLU   B O    1 
ATOM   5618 O O    B GLU   B 1 104 ? 36.079 -28.758 11.617  0.58 30.44 ?  104 GLU   B O    1 
ATOM   5619 C CB   A GLU   B 1 104 ? 38.065 -26.068 12.238  0.42 30.99 ?  104 GLU   B CB   1 
ATOM   5620 C CB   B GLU   B 1 104 ? 38.003 -26.099 12.205  0.58 29.29 ?  104 GLU   B CB   1 
ATOM   5621 C CG   A GLU   B 1 104 ? 39.180 -25.418 13.053  0.42 30.46 ?  104 GLU   B CG   1 
ATOM   5622 C CG   B GLU   B 1 104 ? 39.107 -25.465 13.040  0.58 28.53 ?  104 GLU   B CG   1 
ATOM   5623 C CD   A GLU   B 1 104 ? 40.082 -24.520 12.232  0.42 29.67 ?  104 GLU   B CD   1 
ATOM   5624 C CD   B GLU   B 1 104 ? 40.044 -24.575 12.249  0.58 27.41 ?  104 GLU   B CD   1 
ATOM   5625 O OE1  A GLU   B 1 104 ? 40.045 -24.599 10.986  0.42 28.46 ?  104 GLU   B OE1  1 
ATOM   5626 O OE1  B GLU   B 1 104 ? 40.032 -24.629 11.002  0.58 25.50 ?  104 GLU   B OE1  1 
ATOM   5627 O OE2  A GLU   B 1 104 ? 40.838 -23.733 12.840  0.42 29.93 -1 104 GLU   B OE2  1 
ATOM   5628 O OE2  B GLU   B 1 104 ? 40.806 -23.820 12.887  0.58 27.63 -1 104 GLU   B OE2  1 
ATOM   5629 H H    A GLU   B 1 104 ? 38.818 -28.248 13.054  0.42 38.49 ?  104 GLU   B H    1 
ATOM   5630 H H    B GLU   B 1 104 ? 38.784 -28.281 13.013  0.58 37.54 ?  104 GLU   B H    1 
ATOM   5631 H HA   A GLU   B 1 104 ? 36.901 -26.601 13.833  0.42 37.81 ?  104 GLU   B HA   1 
ATOM   5632 H HA   B GLU   B 1 104 ? 36.828 -26.664 13.780  0.58 36.07 ?  104 GLU   B HA   1 
ATOM   5633 H HB2  A GLU   B 1 104 ? 38.472 -26.528 11.489  0.42 37.19 ?  104 GLU   B HB2  1 
ATOM   5634 H HB2  B GLU   B 1 104 ? 38.412 -26.543 11.447  0.58 35.15 ?  104 GLU   B HB2  1 
ATOM   5635 H HB3  A GLU   B 1 104 ? 37.481 -25.363 11.917  0.42 37.19 ?  104 GLU   B HB3  1 
ATOM   5636 H HB3  B GLU   B 1 104 ? 37.410 -25.393 11.899  0.58 35.15 ?  104 GLU   B HB3  1 
ATOM   5637 H HG2  A GLU   B 1 104 ? 38.785 -24.883 13.760  0.42 36.56 ?  104 GLU   B HG2  1 
ATOM   5638 H HG2  B GLU   B 1 104 ? 38.701 -24.927 13.738  0.58 34.24 ?  104 GLU   B HG2  1 
ATOM   5639 H HG3  A GLU   B 1 104 ? 39.737 -26.111 13.437  0.42 36.56 ?  104 GLU   B HG3  1 
ATOM   5640 H HG3  B GLU   B 1 104 ? 39.644 -26.167 13.437  0.58 34.24 ?  104 GLU   B HG3  1 
ATOM   5641 N N    A ASP   B 1 105 ? 34.982 -26.786 12.239  0.42 31.66 ?  105 ASP   B N    1 
ATOM   5642 N N    B ASP   B 1 105 ? 34.940 -26.887 12.152  0.58 29.61 ?  105 ASP   B N    1 
ATOM   5643 C CA   A ASP   B 1 105 ? 33.706 -27.225 11.686  0.42 32.03 ?  105 ASP   B CA   1 
ATOM   5644 C CA   B ASP   B 1 105 ? 33.671 -27.350 11.601  0.58 29.97 ?  105 ASP   B CA   1 
ATOM   5645 C C    A ASP   B 1 105 ? 33.778 -27.279 10.164  0.42 30.47 ?  105 ASP   B C    1 
ATOM   5646 C C    B ASP   B 1 105 ? 33.730 -27.359 10.078  0.58 28.30 ?  105 ASP   B C    1 
ATOM   5647 O O    A ASP   B 1 105 ? 33.997 -26.257 9.506   0.42 30.20 ?  105 ASP   B O    1 
ATOM   5648 O O    B ASP   B 1 105 ? 33.889 -26.307 9.450   0.58 27.71 ?  105 ASP   B O    1 
ATOM   5649 C CB   A ASP   B 1 105 ? 32.598 -26.274 12.133  0.42 34.04 ?  105 ASP   B CB   1 
ATOM   5650 C CB   B ASP   B 1 105 ? 32.534 -26.452 12.087  0.58 32.63 ?  105 ASP   B CB   1 
ATOM   5651 C CG   A ASP   B 1 105 ? 31.220 -26.746 11.717  0.42 35.75 ?  105 ASP   B CG   1 
ATOM   5652 C CG   B ASP   B 1 105 ? 31.163 -27.005 11.740  0.58 34.67 ?  105 ASP   B CG   1 
ATOM   5653 O OD1  A ASP   B 1 105 ? 31.110 -27.857 11.157  0.42 36.00 ?  105 ASP   B OD1  1 
ATOM   5654 O OD1  B ASP   B 1 105 ? 31.089 -27.995 10.983  0.58 35.09 ?  105 ASP   B OD1  1 
ATOM   5655 O OD2  A ASP   B 1 105 ? 30.243 -26.002 11.949  0.42 36.77 -1 105 ASP   B OD2  1 
ATOM   5656 O OD2  B ASP   B 1 105 ? 30.154 -26.455 12.234  0.58 35.45 -1 105 ASP   B OD2  1 
ATOM   5657 H H    A ASP   B 1 105 ? 34.974 -25.983 12.545  0.42 37.99 ?  105 ASP   B H    1 
ATOM   5658 H H    B ASP   B 1 105 ? 34.917 -26.077 12.438  0.58 35.53 ?  105 ASP   B H    1 
ATOM   5659 H HA   A ASP   B 1 105 ? 33.500 -28.114 12.013  0.42 38.44 ?  105 ASP   B HA   1 
ATOM   5660 H HA   B ASP   B 1 105 ? 33.494 -28.254 11.904  0.58 35.96 ?  105 ASP   B HA   1 
ATOM   5661 H HB2  A ASP   B 1 105 ? 32.618 -26.199 13.101  0.42 40.85 ?  105 ASP   B HB2  1 
ATOM   5662 H HB2  B ASP   B 1 105 ? 32.586 -26.369 13.051  0.58 39.15 ?  105 ASP   B HB2  1 
ATOM   5663 H HB3  A ASP   B 1 105 ? 32.742 -25.405 11.729  0.42 40.85 ?  105 ASP   B HB3  1 
ATOM   5664 H HB3  B ASP   B 1 105 ? 32.624 -25.576 11.674  0.58 39.15 ?  105 ASP   B HB3  1 
ATOM   5665 N N    A ILE   B 1 106 ? 33.576 -28.477 9.607   0.42 29.72 ?  106 ILE   B N    1 
ATOM   5666 N N    B ILE   B 1 106 ? 33.568 -28.548 9.490   0.58 27.90 ?  106 ILE   B N    1 
ATOM   5667 C CA   A ILE   B 1 106 ? 33.583 -28.665 8.161   0.42 28.53 ?  106 ILE   B CA   1 
ATOM   5668 C CA   B ILE   B 1 106 ? 33.566 -28.701 8.040   0.58 26.95 ?  106 ILE   B CA   1 
ATOM   5669 C C    A ILE   B 1 106 ? 32.497 -27.843 7.475   0.42 27.26 ?  106 ILE   B C    1 
ATOM   5670 C C    B ILE   B 1 106 ? 32.471 -27.868 7.388   0.58 25.37 ?  106 ILE   B C    1 
ATOM   5671 O O    A ILE   B 1 106 ? 32.611 -27.543 6.282   0.42 26.98 ?  106 ILE   B O    1 
ATOM   5672 O O    B ILE   B 1 106 ? 32.548 -27.570 6.192   0.58 24.62 ?  106 ILE   B O    1 
ATOM   5673 C CB   A ILE   B 1 106 ? 33.464 -30.172 7.833   0.42 28.60 ?  106 ILE   B CB   1 
ATOM   5674 C CB   B ILE   B 1 106 ? 33.450 -30.202 7.679   0.58 27.54 ?  106 ILE   B CB   1 
ATOM   5675 C CG1  A ILE   B 1 106 ? 33.696 -30.429 6.342   0.42 28.71 ?  106 ILE   B CG1  1 
ATOM   5676 C CG1  B ILE   B 1 106 ? 33.736 -30.436 6.194   0.58 28.15 ?  106 ILE   B CG1  1 
ATOM   5677 C CG2  A ILE   B 1 106 ? 32.101 -30.704 8.257   0.42 28.96 ?  106 ILE   B CG2  1 
ATOM   5678 C CG2  B ILE   B 1 106 ? 32.072 -30.741 8.051   0.58 28.12 ?  106 ILE   B CG2  1 
ATOM   5679 C CD1  A ILE   B 1 106 ? 35.052 -29.974 5.851   0.42 28.61 ?  106 ILE   B CD1  1 
ATOM   5680 C CD1  B ILE   B 1 106 ? 35.099 -29.951 5.758   0.58 28.30 ?  106 ILE   B CD1  1 
ATOM   5681 H H    A ILE   B 1 106 ? 33.441 -29.198 10.052  0.42 35.66 ?  106 ILE   B H    1 
ATOM   5682 H H    B ILE   B 1 106 ? 33.453 -29.281 9.916   0.58 33.48 ?  106 ILE   B H    1 
ATOM   5683 H HA   A ILE   B 1 106 ? 34.433 -28.356 7.822   0.42 34.24 ?  106 ILE   B HA   1 
ATOM   5684 H HA   B ILE   B 1 106 ? 34.412 -28.382 7.702   0.58 32.35 ?  106 ILE   B HA   1 
ATOM   5685 H HB   A ILE   B 1 106 ? 34.145 -30.649 8.333   0.42 34.33 ?  106 ILE   B HB   1 
ATOM   5686 H HB   B ILE   B 1 106 ? 34.109 -30.690 8.193   0.58 33.04 ?  106 ILE   B HB   1 
ATOM   5687 H HG12 A ILE   B 1 106 ? 33.630 -31.384 6.175   0.42 34.46 ?  106 ILE   B HG12 1 
ATOM   5688 H HG12 B ILE   B 1 106 ? 33.692 -31.390 6.013   0.58 33.78 ?  106 ILE   B HG12 1 
ATOM   5689 H HG13 A ILE   B 1 106 ? 33.021 -29.961 5.829   0.42 34.46 ?  106 ILE   B HG13 1 
ATOM   5690 H HG13 B ILE   B 1 106 ? 33.071 -29.971 5.666   0.58 33.78 ?  106 ILE   B HG13 1 
ATOM   5691 H HG21 A ILE   B 1 106 ? 32.101 -31.670 8.174   0.42 34.75 ?  106 ILE   B HG21 1 
ATOM   5692 H HG21 B ILE   B 1 106 ? 32.081 -31.709 7.974   0.58 33.74 ?  106 ILE   B HG21 1 
ATOM   5693 H HG22 A ILE   B 1 106 ? 31.937 -30.452 9.179   0.42 34.75 ?  106 ILE   B HG22 1 
ATOM   5694 H HG22 B ILE   B 1 106 ? 31.870 -30.485 8.964   0.58 33.74 ?  106 ILE   B HG22 1 
ATOM   5695 H HG23 A ILE   B 1 106 ? 31.419 -30.323 7.683   0.42 34.75 ?  106 ILE   B HG23 1 
ATOM   5696 H HG23 B ILE   B 1 106 ? 31.410 -30.369 7.448   0.58 33.74 ?  106 ILE   B HG23 1 
ATOM   5697 H HD11 A ILE   B 1 106 ? 35.227 -30.377 4.988   0.42 34.33 ?  106 ILE   B HD11 1 
ATOM   5698 H HD11 B ILE   B 1 106 ? 35.326 -30.366 4.913   0.58 33.95 ?  106 ILE   B HD11 1 
ATOM   5699 H HD12 A ILE   B 1 106 ? 35.050 -29.007 5.769   0.42 34.33 ?  106 ILE   B HD12 1 
ATOM   5700 H HD12 B ILE   B 1 106 ? 35.073 -28.986 5.656   0.58 33.95 ?  106 ILE   B HD12 1 
ATOM   5701 H HD13 A ILE   B 1 106 ? 35.728 -30.252 6.489   0.42 34.33 ?  106 ILE   B HD13 1 
ATOM   5702 H HD13 B ILE   B 1 106 ? 35.752 -30.196 6.432   0.58 33.95 ?  106 ILE   B HD13 1 
ATOM   5703 N N    A GLN   B 1 107 ? 31.439 -27.473 8.201   0.42 27.05 ?  107 GLN   B N    1 
ATOM   5704 N N    B GLN   B 1 107 ? 31.450 -27.472 8.151   0.58 25.83 ?  107 GLN   B N    1 
ATOM   5705 C CA   A GLN   B 1 107 ? 30.369 -26.671 7.617   0.42 26.72 ?  107 GLN   B CA   1 
ATOM   5706 C CA   B GLN   B 1 107 ? 30.367 -26.671 7.593   0.58 25.88 ?  107 GLN   B CA   1 
ATOM   5707 C C    A GLN   B 1 107 ? 30.861 -25.323 7.102   0.42 24.44 ?  107 GLN   B C    1 
ATOM   5708 C C    B GLN   B 1 107 ? 30.842 -25.304 7.119   0.58 23.90 ?  107 GLN   B C    1 
ATOM   5709 O O    A GLN   B 1 107 ? 30.228 -24.749 6.210   0.42 24.82 ?  107 GLN   B O    1 
ATOM   5710 O O    B GLN   B 1 107 ? 30.181 -24.696 6.272   0.58 24.62 ?  107 GLN   B O    1 
ATOM   5711 C CB   A GLN   B 1 107 ? 29.252 -26.469 8.645   0.42 29.24 ?  107 GLN   B CB   1 
ATOM   5712 C CB   B GLN   B 1 107 ? 29.247 -26.519 8.624   0.58 28.95 ?  107 GLN   B CB   1 
ATOM   5713 C CG   A GLN   B 1 107 ? 27.930 -25.974 8.064   0.42 31.75 ?  107 GLN   B CG   1 
ATOM   5714 C CG   B GLN   B 1 107 ? 27.897 -26.113 8.042   0.58 32.22 ?  107 GLN   B CG   1 
ATOM   5715 C CD   A GLN   B 1 107 ? 27.861 -24.462 7.941   0.42 33.55 ?  107 GLN   B CD   1 
ATOM   5716 C CD   B GLN   B 1 107 ? 27.741 -24.610 7.897   0.58 34.48 ?  107 GLN   B CD   1 
ATOM   5717 O OE1  A GLN   B 1 107 ? 28.689 -23.742 8.501   0.42 34.08 ?  107 GLN   B OE1  1 
ATOM   5718 O OE1  B GLN   B 1 107 ? 28.515 -23.834 8.460   0.58 35.16 ?  107 GLN   B OE1  1 
ATOM   5719 N NE2  A GLN   B 1 107 ? 26.864 -23.973 7.208   0.42 34.32 ?  107 GLN   B NE2  1 
ATOM   5720 N NE2  B GLN   B 1 107 ? 26.730 -24.191 7.141   0.58 35.44 ?  107 GLN   B NE2  1 
ATOM   5721 H H    A GLN   B 1 107 ? 31.315 -27.680 9.023   0.42 32.46 ?  107 GLN   B H    1 
ATOM   5722 H H    B GLN   B 1 107 ? 31.368 -27.647 8.984   0.58 31.00 ?  107 GLN   B H    1 
ATOM   5723 H HA   A GLN   B 1 107 ? 29.994 -27.151 6.865   0.42 32.07 ?  107 GLN   B HA   1 
ATOM   5724 H HA   B GLN   B 1 107 ? 30.002 -27.138 6.826   0.58 31.05 ?  107 GLN   B HA   1 
ATOM   5725 H HB2  A GLN   B 1 107 ? 29.081 -27.317 9.078   0.42 35.08 ?  107 GLN   B HB2  1 
ATOM   5726 H HB2  B GLN   B 1 107 ? 29.127 -27.368 9.071   0.58 34.74 ?  107 GLN   B HB2  1 
ATOM   5727 H HB3  A GLN   B 1 107 ? 29.548 -25.820 9.301   0.42 35.08 ?  107 GLN   B HB3  1 
ATOM   5728 H HB3  B GLN   B 1 107 ? 29.509 -25.843 9.267   0.58 34.74 ?  107 GLN   B HB3  1 
ATOM   5729 H HG2  A GLN   B 1 107 ? 27.810 -26.350 7.179   0.42 38.10 ?  107 GLN   B HG2  1 
ATOM   5730 H HG2  B GLN   B 1 107 ? 27.798 -26.507 7.162   0.58 38.66 ?  107 GLN   B HG2  1 
ATOM   5731 H HG3  A GLN   B 1 107 ? 27.205 -26.262 8.645   0.42 38.10 ?  107 GLN   B HG3  1 
ATOM   5732 H HG3  B GLN   B 1 107 ? 27.194 -26.434 8.630   0.58 38.66 ?  107 GLN   B HG3  1 
ATOM   5733 H HE21 A GLN   B 1 107 ? 26.304 -24.506 6.830   0.42 41.18 ?  107 GLN   B HE21 1 
ATOM   5734 H HE21 B GLN   B 1 107 ? 26.210 -24.762 6.761   0.58 42.53 ?  107 GLN   B HE21 1 
ATOM   5735 H HE22 A GLN   B 1 107 ? 26.778 -23.122 7.111   0.42 41.18 ?  107 GLN   B HE22 1 
ATOM   5736 H HE22 B GLN   B 1 107 ? 26.595 -23.349 7.030   0.58 42.53 ?  107 GLN   B HE22 1 
ATOM   5737 N N    . LEU   B 1 108 ? 31.977 -24.812 7.629   1.00 21.98 ?  108 LEU   B N    1 
ATOM   5738 C CA   . LEU   B 1 108 ? 32.517 -23.516 7.208   1.00 19.37 ?  108 LEU   B CA   1 
ATOM   5739 C C    . LEU   B 1 108 ? 33.159 -23.551 5.830   1.00 16.66 ?  108 LEU   B C    1 
ATOM   5740 O O    . LEU   B 1 108 ? 33.589 -22.499 5.332   1.00 15.53 ?  108 LEU   B O    1 
ATOM   5741 C CB   . LEU   B 1 108 ? 33.524 -23.012 8.242   1.00 19.72 ?  108 LEU   B CB   1 
ATOM   5742 C CG   . LEU   B 1 108 ? 32.906 -22.452 9.524   1.00 21.43 ?  108 LEU   B CG   1 
ATOM   5743 C CD1  . LEU   B 1 108 ? 33.904 -22.467 10.663  1.00 22.10 ?  108 LEU   B CD1  1 
ATOM   5744 C CD2  . LEU   B 1 108 ? 32.408 -21.039 9.278   1.00 21.92 ?  108 LEU   B CD2  1 
ATOM   5745 H H    A LEU   B 1 108 ? 32.434 -25.193 8.244   0.42 26.38 ?  108 LEU   B H    1 
ATOM   5746 H H    B LEU   B 1 108 ? 32.442 -25.204 8.231   0.58 26.38 ?  108 LEU   B H    1 
ATOM   5747 H HA   . LEU   B 1 108 ? 31.788 -22.879 7.174   1.00 23.25 ?  108 LEU   B HA   1 
ATOM   5748 H HB2  . LEU   B 1 108 ? 34.101 -23.745 8.499   1.00 23.66 ?  108 LEU   B HB2  1 
ATOM   5749 H HB3  . LEU   B 1 108 ? 34.050 -22.304 7.842   1.00 23.66 ?  108 LEU   B HB3  1 
ATOM   5750 H HG   . LEU   B 1 108 ? 32.144 -22.996 9.780   1.00 25.71 ?  108 LEU   B HG   1 
ATOM   5751 H HD11 . LEU   B 1 108 ? 33.473 -22.135 11.468  1.00 26.52 ?  108 LEU   B HD11 1 
ATOM   5752 H HD12 . LEU   B 1 108 ? 34.209 -23.376 10.804  1.00 26.52 ?  108 LEU   B HD12 1 
ATOM   5753 H HD13 . LEU   B 1 108 ? 34.655 -21.897 10.434  1.00 26.52 ?  108 LEU   B HD13 1 
ATOM   5754 H HD21 . LEU   B 1 108 ? 32.024 -20.691 10.098  1.00 26.31 ?  108 LEU   B HD21 1 
ATOM   5755 H HD22 . LEU   B 1 108 ? 33.156 -20.485 9.003   1.00 26.31 ?  108 LEU   B HD22 1 
ATOM   5756 H HD23 . LEU   B 1 108 ? 31.735 -21.057 8.580   1.00 26.31 ?  108 LEU   B HD23 1 
ATOM   5757 N N    . LEU   B 1 109 ? 33.226 -24.724 5.207   1.00 15.18 ?  109 LEU   B N    1 
ATOM   5758 C CA   . LEU   B 1 109 ? 33.854 -24.843 3.901   1.00 14.21 ?  109 LEU   B CA   1 
ATOM   5759 C C    . LEU   B 1 109 ? 33.086 -24.063 2.839   1.00 13.61 ?  109 LEU   B C    1 
ATOM   5760 O O    . LEU   B 1 109 ? 33.695 -23.485 1.933   1.00 13.44 ?  109 LEU   B O    1 
ATOM   5761 C CB   . LEU   B 1 109 ? 33.971 -26.323 3.534   1.00 14.07 ?  109 LEU   B CB   1 
ATOM   5762 C CG   . LEU   B 1 109 ? 34.744 -26.663 2.264   1.00 13.99 ?  109 LEU   B CG   1 
ATOM   5763 C CD1  . LEU   B 1 109 ? 36.128 -26.016 2.265   1.00 14.13 ?  109 LEU   B CD1  1 
ATOM   5764 C CD2  . LEU   B 1 109 ? 34.854 -28.189 2.118   1.00 14.70 ?  109 LEU   B CD2  1 
ATOM   5765 H H    . LEU   B 1 109 ? 32.921 -25.463 5.516   1.00 18.22 ?  109 LEU   B H    1 
ATOM   5766 H HA   . LEU   B 1 109 ? 34.752 -24.471 3.946   1.00 17.05 ?  109 LEU   B HA   1 
ATOM   5767 H HB2  . LEU   B 1 109 ? 34.412 -26.782 4.264   1.00 16.88 ?  109 LEU   B HB2  1 
ATOM   5768 H HB3  . LEU   B 1 109 ? 33.077 -26.678 3.423   1.00 16.88 ?  109 LEU   B HB3  1 
ATOM   5769 H HG   . LEU   B 1 109 ? 34.259 -26.333 1.494   1.00 16.79 ?  109 LEU   B HG   1 
ATOM   5770 H HD11 . LEU   B 1 109 ? 36.650 -26.384 1.531   1.00 16.96 ?  109 LEU   B HD11 1 
ATOM   5771 H HD12 . LEU   B 1 109 ? 36.028 -25.062 2.153   1.00 16.96 ?  109 LEU   B HD12 1 
ATOM   5772 H HD13 . LEU   B 1 109 ? 36.567 -26.213 3.108   1.00 16.96 ?  109 LEU   B HD13 1 
ATOM   5773 H HD21 . LEU   B 1 109 ? 35.432 -28.394 1.360   1.00 17.64 ?  109 LEU   B HD21 1 
ATOM   5774 H HD22 . LEU   B 1 109 ? 35.234 -28.561 2.928   1.00 17.64 ?  109 LEU   B HD22 1 
ATOM   5775 H HD23 . LEU   B 1 109 ? 33.971 -28.560 1.965   1.00 17.64 ?  109 LEU   B HD23 1 
ATOM   5776 N N    . LYS   B 1 110 ? 31.756 -24.023 2.930   1.00 12.99 ?  110 LYS   B N    1 
ATOM   5777 C CA   . LYS   B 1 110 ? 30.999 -23.263 1.943   1.00 13.09 ?  110 LYS   B CA   1 
ATOM   5778 C C    . LYS   B 1 110 ? 31.338 -21.777 2.022   1.00 12.36 ?  110 LYS   B C    1 
ATOM   5779 O O    . LYS   B 1 110 ? 31.597 -21.139 0.997   1.00 12.35 ?  110 LYS   B O    1 
ATOM   5780 C CB   . LYS   B 1 110 ? 29.496 -23.508 2.099   1.00 13.85 ?  110 LYS   B CB   1 
ATOM   5781 C CG   . LYS   B 1 110 ? 28.690 -22.890 0.954   1.00 13.81 ?  110 LYS   B CG   1 
ATOM   5782 C CD   . LYS   B 1 110 ? 27.214 -23.315 0.974   1.00 14.45 ?  110 LYS   B CD   1 
ATOM   5783 C CE   . LYS   B 1 110 ? 26.459 -22.792 -0.254  1.00 15.43 ?  110 LYS   B CE   1 
ATOM   5784 N NZ   . LYS   B 1 110 ? 26.808 -23.526 -1.505  1.00 15.25 ?  110 LYS   B NZ   1 
ATOM   5785 H H    . LYS   B 1 110 ? 31.286 -24.416 3.536   1.00 15.58 ?  110 LYS   B H    1 
ATOM   5786 H HA   . LYS   B 1 110 ? 31.251 -23.569 1.063   1.00 15.70 ?  110 LYS   B HA   1 
ATOM   5787 H HB2  . LYS   B 1 110 ? 29.329 -24.463 2.110   1.00 16.62 ?  110 LYS   B HB2  1 
ATOM   5788 H HB3  . LYS   B 1 110 ? 29.191 -23.108 2.931   1.00 16.62 ?  110 LYS   B HB3  1 
ATOM   5789 H HG2  . LYS   B 1 110 ? 28.721 -21.927 1.023   1.00 16.57 ?  110 LYS   B HG2  1 
ATOM   5790 H HG3  . LYS   B 1 110 ? 29.068 -23.181 0.110   1.00 16.57 ?  110 LYS   B HG3  1 
ATOM   5791 H HD2  . LYS   B 1 110 ? 27.153 -24.286 0.978   1.00 17.34 ?  110 LYS   B HD2  1 
ATOM   5792 H HD3  . LYS   B 1 110 ? 26.783 -22.955 1.770   1.00 17.34 ?  110 LYS   B HD3  1 
ATOM   5793 H HE2  . LYS   B 1 110 ? 25.506 -22.889 -0.110  1.00 18.52 ?  110 LYS   B HE2  1 
ATOM   5794 H HE3  . LYS   B 1 110 ? 26.683 -21.858 -0.386  1.00 18.52 ?  110 LYS   B HE3  1 
ATOM   5795 H HZ1  . LYS   B 1 110 ? 26.356 -23.194 -2.193  1.00 18.30 ?  110 LYS   B HZ1  1 
ATOM   5796 H HZ2  . LYS   B 1 110 ? 27.682 -23.452 -1.669  1.00 18.30 ?  110 LYS   B HZ2  1 
ATOM   5797 H HZ3  . LYS   B 1 110 ? 26.609 -24.391 -1.417  1.00 18.30 ?  110 LYS   B HZ3  1 
ATOM   5798 N N    . SER   B 1 111 ? 31.356 -21.219 3.237   1.00 13.06 ?  111 SER   B N    1 
ATOM   5799 C CA   . SER   B 1 111 ? 31.757 -19.824 3.408   1.00 12.89 ?  111 SER   B CA   1 
ATOM   5800 C C    . SER   B 1 111 ? 33.138 -19.571 2.811   1.00 12.40 ?  111 SER   B C    1 
ATOM   5801 O O    . SER   B 1 111 ? 33.365 -18.543 2.156   1.00 12.65 ?  111 SER   B O    1 
ATOM   5802 C CB   . SER   B 1 111 ? 31.765 -19.463 4.890   1.00 14.43 ?  111 SER   B CB   1 
ATOM   5803 O OG   . SER   B 1 111 ? 30.458 -19.450 5.419   1.00 15.72 ?  111 SER   B OG   1 
ATOM   5804 H H    . SER   B 1 111 ? 31.154 -21.627 3.970   1.00 15.67 ?  111 SER   B H    1 
ATOM   5805 H HA   . SER   B 1 111 ? 31.123 -19.252 2.957   1.00 15.46 ?  111 SER   B HA   1 
ATOM   5806 H HB2  . SER   B 1 111 ? 32.286 -20.123 5.376   1.00 17.32 ?  111 SER   B HB2  1 
ATOM   5807 H HB3  . SER   B 1 111 ? 32.160 -18.585 5.001   1.00 17.32 ?  111 SER   B HB3  1 
ATOM   5808 H HG   . SER   B 1 111 ? 30.478 -19.241 6.242   1.00 18.86 ?  111 SER   B HG   1 
ATOM   5809 N N    . ALA   B 1 112 ? 34.076 -20.501 3.026   1.00 12.34 ?  112 ALA   B N    1 
ATOM   5810 C CA   . ALA   B 1 112 ? 35.423 -20.339 2.487   1.00 11.95 ?  112 ALA   B CA   1 
ATOM   5811 C C    . ALA   B 1 112 ? 35.392 -20.247 0.964   1.00 11.60 ?  112 ALA   B C    1 
ATOM   5812 O O    . ALA   B 1 112 ? 36.012 -19.356 0.372   1.00 11.62 ?  112 ALA   B O    1 
ATOM   5813 C CB   . ALA   B 1 112 ? 36.320 -21.480 2.973   1.00 12.81 ?  112 ALA   B CB   1 
ATOM   5814 H H    . ALA   B 1 112 ? 33.958 -21.226 3.478   1.00 14.81 ?  112 ALA   B H    1 
ATOM   5815 H HA   . ALA   B 1 112 ? 35.794 -19.510 2.822   1.00 14.34 ?  112 ALA   B HA   1 
ATOM   5816 H HB1  . ALA   B 1 112 ? 37.214 -21.354 2.612   1.00 15.37 ?  112 ALA   B HB1  1 
ATOM   5817 H HB2  . ALA   B 1 112 ? 36.357 -21.459 3.945   1.00 15.37 ?  112 ALA   B HB2  1 
ATOM   5818 H HB3  . ALA   B 1 112 ? 35.957 -22.323 2.673   1.00 15.37 ?  112 ALA   B HB3  1 
ATOM   5819 N N    . TYR   B 1 113 ? 34.644 -21.145 0.310   1.00 11.38 ?  113 TYR   B N    1 
ATOM   5820 C CA   . TYR   B 1 113 ? 34.575 -21.102 -1.145  1.00 10.92 ?  113 TYR   B CA   1 
ATOM   5821 C C    . TYR   B 1 113 ? 33.866 -19.855 -1.664  1.00 10.58 ?  113 TYR   B C    1 
ATOM   5822 O O    . TYR   B 1 113 ? 34.137 -19.422 -2.790  1.00 10.89 ?  113 TYR   B O    1 
ATOM   5823 C CB   . TYR   B 1 113 ? 33.908 -22.366 -1.686  1.00 11.49 ?  113 TYR   B CB   1 
ATOM   5824 C CG   . TYR   B 1 113 ? 34.870 -23.515 -1.934  1.00 11.72 ?  113 TYR   B CG   1 
ATOM   5825 C CD1  . TYR   B 1 113 ? 35.862 -23.416 -2.891  1.00 12.18 ?  113 TYR   B CD1  1 
ATOM   5826 C CD2  . TYR   B 1 113 ? 34.760 -24.702 -1.235  1.00 12.08 ?  113 TYR   B CD2  1 
ATOM   5827 C CE1  . TYR   B 1 113 ? 36.747 -24.442 -3.126  1.00 12.04 ?  113 TYR   B CE1  1 
ATOM   5828 C CE2  . TYR   B 1 113 ? 35.639 -25.755 -1.468  1.00 12.30 ?  113 TYR   B CE2  1 
ATOM   5829 C CZ   . TYR   B 1 113 ? 36.622 -25.623 -2.422  1.00 12.65 ?  113 TYR   B CZ   1 
ATOM   5830 O OH   . TYR   B 1 113 ? 37.505 -26.639 -2.694  1.00 13.55 ?  113 TYR   B OH   1 
ATOM   5831 H H    . TYR   B 1 113 ? 34.156 -21.753 0.685   1.00 13.65 ?  113 TYR   B H    1 
ATOM   5832 H HA   . TYR   B 1 113 ? 35.476 -21.082 -1.481  1.00 13.11 ?  113 TYR   B HA   1 
ATOM   5833 H HB2  . TYR   B 1 113 ? 33.244 -22.676 -1.045  1.00 13.79 ?  113 TYR   B HB2  1 
ATOM   5834 H HB3  . TYR   B 1 113 ? 33.471 -22.157 -2.527  1.00 13.79 ?  113 TYR   B HB3  1 
ATOM   5835 H HD1  . TYR   B 1 113 ? 35.952 -22.616 -3.371  1.00 14.61 ?  113 TYR   B HD1  1 
ATOM   5836 H HD2  . TYR   B 1 113 ? 34.089 -24.797 -0.598  1.00 14.49 ?  113 TYR   B HD2  1 
ATOM   5837 H HE1  . TYR   B 1 113 ? 37.406 -24.344 -3.776  1.00 14.45 ?  113 TYR   B HE1  1 
ATOM   5838 H HE2  . TYR   B 1 113 ? 35.551 -26.553 -0.998  1.00 14.76 ?  113 TYR   B HE2  1 
ATOM   5839 H HH   . TYR   B 1 113 ? 37.330 -27.307 -2.222  1.00 16.27 ?  113 TYR   B HH   1 
ATOM   5840 N N    . GLU   B 1 114 ? 32.951 -19.274 -0.881  1.00 11.12 ?  114 GLU   B N    1 
ATOM   5841 C CA   . GLU   B 1 114 ? 32.269 -18.063 -1.337  1.00 11.16 ?  114 GLU   B CA   1 
ATOM   5842 C C    . GLU   B 1 114 ? 33.255 -16.938 -1.638  1.00 10.94 ?  114 GLU   B C    1 
ATOM   5843 O O    . GLU   B 1 114 ? 32.982 -16.080 -2.482  1.00 11.18 ?  114 GLU   B O    1 
ATOM   5844 C CB   . GLU   B 1 114 ? 31.205 -17.628 -0.325  1.00 11.66 ?  114 GLU   B CB   1 
ATOM   5845 C CG   . GLU   B 1 114 ? 29.979 -18.540 -0.396  1.00 11.69 ?  114 GLU   B CG   1 
ATOM   5846 C CD   . GLU   B 1 114 ? 28.954 -18.341 0.712   1.00 12.06 ?  114 GLU   B CD   1 
ATOM   5847 O OE1  . GLU   B 1 114 ? 29.250 -17.724 1.756   1.00 12.00 ?  114 GLU   B OE1  1 
ATOM   5848 O OE2  . GLU   B 1 114 ? 27.829 -18.874 0.551   1.00 12.79 -1 114 GLU   B OE2  1 
ATOM   5849 H H    . GLU   B 1 114 ? 32.703 -19.564 -0.107  1.00 13.34 ?  114 GLU   B H    1 
ATOM   5850 H HA   . GLU   B 1 114 ? 31.807 -18.267 -2.160  1.00 13.39 ?  114 GLU   B HA   1 
ATOM   5851 H HB2  . GLU   B 1 114 ? 31.570 -17.677 0.575   1.00 13.99 ?  114 GLU   B HB2  1 
ATOM   5852 H HB3  . GLU   B 1 114 ? 30.921 -16.722 -0.523  1.00 13.99 ?  114 GLU   B HB3  1 
ATOM   5853 H HG2  . GLU   B 1 114 ? 29.528 -18.381 -1.236  1.00 14.03 ?  114 GLU   B HG2  1 
ATOM   5854 H HG3  . GLU   B 1 114 ? 30.281 -19.460 -0.354  1.00 14.03 ?  114 GLU   B HG3  1 
ATOM   5855 N N    . ASN   B 1 115 ? 34.427 -16.941 -0.997  1.00 10.97 ?  115 ASN   B N    1 
ATOM   5856 C CA   . ASN   B 1 115 ? 35.418 -15.909 -1.293  1.00 10.67 ?  115 ASN   B CA   1 
ATOM   5857 C C    . ASN   B 1 115 ? 35.836 -15.937 -2.755  1.00 10.61 ?  115 ASN   B C    1 
ATOM   5858 O O    . ASN   B 1 115 ? 36.209 -14.897 -3.320  1.00 11.10 ?  115 ASN   B O    1 
ATOM   5859 C CB   . ASN   B 1 115 ? 36.657 -16.085 -0.406  1.00 11.47 ?  115 ASN   B CB   1 
ATOM   5860 C CG   . ASN   B 1 115 ? 36.383 -15.805 1.047   1.00 11.71 ?  115 ASN   B CG   1 
ATOM   5861 O OD1  . ASN   B 1 115 ? 36.381 -14.656 1.476   1.00 13.83 ?  115 ASN   B OD1  1 
ATOM   5862 N ND2  . ASN   B 1 115 ? 36.201 -16.862 1.833   1.00 11.87 ?  115 ASN   B ND2  1 
ATOM   5863 H H    . ASN   B 1 115 ? 34.666 -17.513 -0.396  1.00 13.17 ?  115 ASN   B H    1 
ATOM   5864 H HA   . ASN   B 1 115 ? 35.035 -15.040 -1.110  1.00 12.80 ?  115 ASN   B HA   1 
ATOM   5865 H HB2  . ASN   B 1 115 ? 36.975 -16.996 -0.484  1.00 13.76 ?  115 ASN   B HB2  1 
ATOM   5866 H HB3  . ASN   B 1 115 ? 37.343 -15.466 -0.703  1.00 13.76 ?  115 ASN   B HB3  1 
ATOM   5867 H HD21 . ASN   B 1 115 ? 36.053 -16.751 2.675   1.00 14.25 ?  115 ASN   B HD21 1 
ATOM   5868 H HD22 . ASN   B 1 115 ? 36.224 -17.654 1.503   1.00 14.25 ?  115 ASN   B HD22 1 
ATOM   5869 N N    . PHE   B 1 116 ? 35.805 -17.118 -3.382  1.00 10.32 ?  116 PHE   B N    1 
ATOM   5870 C CA   . PHE   B 1 116 ? 36.233 -17.222 -4.770  1.00 10.47 ?  116 PHE   B CA   1 
ATOM   5871 C C    . PHE   B 1 116 ? 35.336 -16.394 -5.689  1.00 10.19 ?  116 PHE   B C    1 
ATOM   5872 O O    . PHE   B 1 116 ? 35.772 -15.963 -6.761  1.00 11.11 ?  116 PHE   B O    1 
ATOM   5873 C CB   . PHE   B 1 116 ? 36.183 -18.674 -5.277  1.00 10.25 ?  116 PHE   B CB   1 
ATOM   5874 C CG   . PHE   B 1 116 ? 37.260 -19.626 -4.739  1.00 10.35 ?  116 PHE   B CG   1 
ATOM   5875 C CD1  . PHE   B 1 116 ? 37.907 -19.439 -3.533  1.00 11.07 ?  116 PHE   B CD1  1 
ATOM   5876 C CD2  . PHE   B 1 116 ? 37.561 -20.765 -5.474  1.00 10.65 ?  116 PHE   B CD2  1 
ATOM   5877 C CE1  . PHE   B 1 116 ? 38.838 -20.376 -3.085  1.00 11.33 ?  116 PHE   B CE1  1 
ATOM   5878 C CE2  . PHE   B 1 116 ? 38.488 -21.693 -5.033  1.00 10.92 ?  116 PHE   B CE2  1 
ATOM   5879 C CZ   . PHE   B 1 116 ? 39.118 -21.501 -3.843  1.00 10.78 ?  116 PHE   B CZ   1 
ATOM   5880 H H    . PHE   B 1 116 ? 35.536 -17.865 -3.030  1.00 12.39 ?  116 PHE   B H    1 
ATOM   5881 H HA   . PHE   B 1 116 ? 37.138 -16.905 -4.854  1.00 12.56 ?  116 PHE   B HA   1 
ATOM   5882 H HB2  . PHE   B 1 116 ? 35.313 -19.050 -5.040  1.00 12.30 ?  116 PHE   B HB2  1 
ATOM   5883 H HB3  . PHE   B 1 116 ? 36.263 -18.662 -6.244  1.00 12.30 ?  116 PHE   B HB3  1 
ATOM   5884 H HD1  . PHE   B 1 116 ? 37.705 -18.693 -3.011  1.00 13.29 ?  116 PHE   B HD1  1 
ATOM   5885 H HD2  . PHE   B 1 116 ? 37.119 -20.912 -6.282  1.00 12.78 ?  116 PHE   B HD2  1 
ATOM   5886 H HE1  . PHE   B 1 116 ? 39.279 -20.243 -2.275  1.00 13.60 ?  116 PHE   B HE1  1 
ATOM   5887 H HE2  . PHE   B 1 116 ? 38.677 -22.439 -5.549  1.00 13.10 ?  116 PHE   B HE2  1 
ATOM   5888 H HZ   . PHE   B 1 116 ? 39.757 -22.111 -3.550  1.00 12.93 ?  116 PHE   B HZ   1 
ATOM   5889 N N    . ASN   B 1 117 ? 34.067 -16.191 -5.309  1.00 10.59 ?  117 ASN   B N    1 
ATOM   5890 C CA   . ASN   B 1 117 ? 33.120 -15.484 -6.173  1.00 11.40 ?  117 ASN   B CA   1 
ATOM   5891 C C    . ASN   B 1 117 ? 33.433 -14.003 -6.323  1.00 11.62 ?  117 ASN   B C    1 
ATOM   5892 O O    . ASN   B 1 117 ? 32.841 -13.354 -7.189  1.00 12.74 ?  117 ASN   B O    1 
ATOM   5893 C CB   . ASN   B 1 117 ? 31.694 -15.702 -5.677  1.00 11.50 ?  117 ASN   B CB   1 
ATOM   5894 C CG   . ASN   B 1 117 ? 31.240 -17.111 -5.924  1.00 11.79 ?  117 ASN   B CG   1 
ATOM   5895 O OD1  . ASN   B 1 117 ? 31.589 -17.703 -6.949  1.00 12.49 ?  117 ASN   B OD1  1 
ATOM   5896 N ND2  . ASN   B 1 117 ? 30.498 -17.680 -4.983  1.00 11.80 ?  117 ASN   B ND2  1 
ATOM   5897 H H    . ASN   B 1 117 ? 33.736 -16.453 -4.557  1.00 12.71 ?  117 ASN   B H    1 
ATOM   5898 H HA   . ASN   B 1 117 ? 33.173 -15.876 -7.053  1.00 13.68 ?  117 ASN   B HA   1 
ATOM   5899 H HB2  . ASN   B 1 117 ? 31.653 -15.530 -4.717  1.00 13.80 ?  117 ASN   B HB2  1 
ATOM   5900 H HB3  . ASN   B 1 117 ? 31.094 -15.095 -6.143  1.00 13.80 ?  117 ASN   B HB3  1 
ATOM   5901 H HD21 . ASN   B 1 117 ? 30.222 -18.489 -5.082  1.00 14.16 ?  117 ASN   B HD21 1 
ATOM   5902 H HD22 . ASN   B 1 117 ? 30.283 -17.241 -4.272  1.00 14.16 ?  117 ASN   B HD22 1 
ATOM   5903 N N    . GLN   B 1 118 ? 34.373 -13.477 -5.548  1.00 11.10 ?  118 GLN   B N    1 
ATOM   5904 C CA   . GLN   B 1 118 ? 34.802 -12.092 -5.688  1.00 11.76 ?  118 GLN   B CA   1 
ATOM   5905 C C    . GLN   B 1 118 ? 35.869 -11.906 -6.758  1.00 11.95 ?  118 GLN   B C    1 
ATOM   5906 O O    . GLN   B 1 118 ? 36.359 -10.783 -6.927  1.00 13.76 ?  118 GLN   B O    1 
ATOM   5907 C CB   . GLN   B 1 118 ? 35.279 -11.563 -4.333  1.00 12.10 ?  118 GLN   B CB   1 
ATOM   5908 C CG   . GLN   B 1 118 ? 34.196 -11.604 -3.268  1.00 12.45 ?  118 GLN   B CG   1 
ATOM   5909 C CD   . GLN   B 1 118 ? 33.033 -10.682 -3.598  1.00 12.30 ?  118 GLN   B CD   1 
ATOM   5910 O OE1  . GLN   B 1 118 ? 33.233 -9.542  -4.037  1.00 13.76 ?  118 GLN   B OE1  1 
ATOM   5911 N NE2  . GLN   B 1 118 ? 31.814 -11.164 -3.392  1.00 12.73 ?  118 GLN   B NE2  1 
ATOM   5912 H H    . GLN   B 1 118 ? 34.798 -13.908 -4.934  1.00 13.33 ?  118 GLN   B H    1 
ATOM   5913 H HA   . GLN   B 1 118 ? 34.036 -11.563 -5.954  1.00 14.11 ?  118 GLN   B HA   1 
ATOM   5914 H HB2  . GLN   B 1 118 ? 36.023 -12.097 -4.023  1.00 14.52 ?  118 GLN   B HB2  1 
ATOM   5915 H HB3  . GLN   B 1 118 ? 35.552 -10.636 -4.431  1.00 14.52 ?  118 GLN   B HB3  1 
ATOM   5916 H HG2  . GLN   B 1 118 ? 33.856 -12.516 -3.197  1.00 14.94 ?  118 GLN   B HG2  1 
ATOM   5917 H HG3  . GLN   B 1 118 ? 34.574 -11.331 -2.416  1.00 14.94 ?  118 GLN   B HG3  1 
ATOM   5918 H HE21 . GLN   B 1 118 ? 31.710 -11.963 -3.082  1.00 15.27 ?  118 GLN   B HE21 1 
ATOM   5919 H HE22 . GLN   B 1 118 ? 31.130 -10.680 -3.568  1.00 15.27 ?  118 GLN   B HE22 1 
ATOM   5920 N N    . HIS   B 1 119 ? 36.226 -12.965 -7.487  1.00 11.09 ?  119 HIS   B N    1 
ATOM   5921 C CA   . HIS   B 1 119 ? 37.272 -12.920 -8.497  1.00 11.45 ?  119 HIS   B CA   1 
ATOM   5922 C C    . HIS   B 1 119 ? 36.784 -13.651 -9.733  1.00 11.53 ?  119 HIS   B C    1 
ATOM   5923 O O    . HIS   B 1 119 ? 36.269 -14.764 -9.628  1.00 12.41 ?  119 HIS   B O    1 
ATOM   5924 C CB   . HIS   B 1 119 ? 38.539 -13.562 -7.943  1.00 12.24 ?  119 HIS   B CB   1 
ATOM   5925 C CG   . HIS   B 1 119 ? 39.018 -12.872 -6.716  1.00 13.92 ?  119 HIS   B CG   1 
ATOM   5926 N ND1  . HIS   B 1 119 ? 39.821 -11.753 -6.764  1.00 15.17 ?  119 HIS   B ND1  1 
ATOM   5927 C CD2  . HIS   B 1 119 ? 38.723 -13.075 -5.413  1.00 14.93 ?  119 HIS   B CD2  1 
ATOM   5928 C CE1  . HIS   B 1 119 ? 40.032 -11.321 -5.535  1.00 16.02 ?  119 HIS   B CE1  1 
ATOM   5929 N NE2  . HIS   B 1 119 ? 39.373 -12.102 -4.698  1.00 16.15 ?  119 HIS   B NE2  1 
ATOM   5930 H H    . HIS   B 1 119 ? 35.854 -13.742 -7.416  1.00 13.30 ?  119 HIS   B H    1 
ATOM   5931 H HA   . HIS   B 1 119 ? 37.460 -11.995 -8.730  1.00 13.75 ?  119 HIS   B HA   1 
ATOM   5932 H HB2  . HIS   B 1 119 ? 38.356 -14.486 -7.722  1.00 14.69 ?  119 HIS   B HB2  1 
ATOM   5933 H HB3  . HIS   B 1 119 ? 39.238 -13.507 -8.614  1.00 14.69 ?  119 HIS   B HB3  1 
ATOM   5934 H HD2  . HIS   B 1 119 ? 38.190 -13.751 -5.064  1.00 17.91 ?  119 HIS   B HD2  1 
ATOM   5935 H HE1  . HIS   B 1 119 ? 40.568 -10.598 -5.294  1.00 19.22 ?  119 HIS   B HE1  1 
ATOM   5936 H HE2  . HIS   B 1 119 ? 39.377 -12.028 -3.838  1.00 19.38 ?  119 HIS   B HE2  1 
ATOM   5937 N N    . GLU   B 1 120 ? 36.942 -13.035 -10.905 1.00 12.67 ?  120 GLU   B N    1 
ATOM   5938 C CA   . GLU   B 1 120 ? 36.346 -13.614 -12.102 1.00 13.80 ?  120 GLU   B CA   1 
ATOM   5939 C C    . GLU   B 1 120 ? 37.016 -14.917 -12.521 1.00 12.77 ?  120 GLU   B C    1 
ATOM   5940 O O    . GLU   B 1 120 ? 36.349 -15.784 -13.099 1.00 12.89 ?  120 GLU   B O    1 
ATOM   5941 C CB   . GLU   B 1 120 ? 36.353 -12.600 -13.241 1.00 17.96 ?  120 GLU   B CB   1 
ATOM   5942 C CG   . GLU   B 1 120 ? 35.367 -11.466 -13.024 1.00 23.35 ?  120 GLU   B CG   1 
ATOM   5943 C CD   . GLU   B 1 120 ? 35.177 -10.600 -14.251 1.00 28.56 ?  120 GLU   B CD   1 
ATOM   5944 O OE1  . GLU   B 1 120 ? 36.188 -10.276 -14.912 1.00 31.07 ?  120 GLU   B OE1  1 
ATOM   5945 O OE2  . GLU   B 1 120 ? 34.017 -10.243 -14.551 1.00 31.64 -1 120 GLU   B OE2  1 
ATOM   5946 H H    . GLU   B 1 120 ? 37.378 -12.298 -11.029 1.00 15.21 ?  120 GLU   B H    1 
ATOM   5947 H HA   . GLU   B 1 120 ? 35.423 -13.821 -11.906 1.00 16.56 ?  120 GLU   B HA   1 
ATOM   5948 H HB2  . GLU   B 1 120 ? 37.235 -12.212 -13.325 1.00 21.55 ?  120 GLU   B HB2  1 
ATOM   5949 H HB3  . GLU   B 1 120 ? 36.107 -13.050 -14.067 1.00 21.55 ?  120 GLU   B HB3  1 
ATOM   5950 H HG2  . GLU   B 1 120 ? 34.499 -11.835 -12.795 1.00 28.02 ?  120 GLU   B HG2  1 
ATOM   5951 H HG3  . GLU   B 1 120 ? 35.685 -10.898 -12.307 1.00 28.02 ?  120 GLU   B HG3  1 
ATOM   5952 N N    . VAL   B 1 121 ? 38.316 -15.067 -12.259 1.00 12.10 ?  121 VAL   B N    1 
ATOM   5953 C CA   . VAL   B 1 121 ? 39.061 -16.276 -12.609 1.00 11.77 ?  121 VAL   B CA   1 
ATOM   5954 C C    . VAL   B 1 121 ? 40.179 -16.482 -11.594 1.00 11.78 ?  121 VAL   B C    1 
ATOM   5955 O O    . VAL   B 1 121 ? 40.859 -15.528 -11.205 1.00 12.20 ?  121 VAL   B O    1 
ATOM   5956 C CB   . VAL   B 1 121 ? 39.569 -16.224 -14.070 1.00 14.16 ?  121 VAL   B CB   1 
ATOM   5957 C CG1  . VAL   B 1 121 ? 40.421 -14.981 -14.322 1.00 15.47 ?  121 VAL   B CG1  1 
ATOM   5958 C CG2  . VAL   B 1 121 ? 40.316 -17.504 -14.433 1.00 15.65 ?  121 VAL   B CG2  1 
ATOM   5959 H H    . VAL   B 1 121 ? 38.803 -14.466 -11.874 1.00 14.52 ?  121 VAL   B H    1 
ATOM   5960 H HA   . VAL   B 1 121 ? 38.453 -17.027 -12.541 1.00 14.12 ?  121 VAL   B HA   1 
ATOM   5961 H HB   . VAL   B 1 121 ? 38.796 -16.168 -14.657 1.00 17.00 ?  121 VAL   B HB   1 
ATOM   5962 H HG11 . VAL   B 1 121 ? 40.737 -14.995 -15.240 1.00 18.57 ?  121 VAL   B HG11 1 
ATOM   5963 H HG12 . VAL   B 1 121 ? 39.880 -14.188 -14.174 1.00 18.57 ?  121 VAL   B HG12 1 
ATOM   5964 H HG13 . VAL   B 1 121 ? 41.176 -14.984 -13.714 1.00 18.57 ?  121 VAL   B HG13 1 
ATOM   5965 H HG21 . VAL   B 1 121 ? 40.518 -17.491 -15.383 1.00 18.78 ?  121 VAL   B HG21 1 
ATOM   5966 H HG22 . VAL   B 1 121 ? 41.139 -17.547 -13.922 1.00 18.78 ?  121 VAL   B HG22 1 
ATOM   5967 H HG23 . VAL   B 1 121 ? 39.756 -18.268 -14.227 1.00 18.78 ?  121 VAL   B HG23 1 
ATOM   5968 N N    . LEU   B 1 122 ? 40.368 -17.736 -11.170 1.00 11.31 ?  122 LEU   B N    1 
ATOM   5969 C CA   . LEU   B 1 122 ? 41.338 -18.097 -10.143 1.00 10.76 ?  122 LEU   B CA   1 
ATOM   5970 C C    . LEU   B 1 122 ? 41.992 -19.430 -10.470 1.00 10.76 ?  122 LEU   B C    1 
ATOM   5971 O O    . LEU   B 1 122 ? 41.335 -20.350 -10.975 1.00 12.27 ?  122 LEU   B O    1 
ATOM   5972 C CB   . LEU   B 1 122 ? 40.674 -18.331 -8.773  1.00 12.69 ?  122 LEU   B CB   1 
ATOM   5973 C CG   . LEU   B 1 122 ? 39.645 -17.308 -8.290  1.00 12.96 ?  122 LEU   B CG   1 
ATOM   5974 C CD1  . LEU   B 1 122 ? 38.251 -17.688 -8.750  1.00 13.03 ?  122 LEU   B CD1  1 
ATOM   5975 C CD2  . LEU   B 1 122 ? 39.694 -17.174 -6.776  1.00 12.05 ?  122 LEU   B CD2  1 
ATOM   5976 H H    . LEU   B 1 122 ? 39.943 -18.415 -11.481 1.00 13.58 ?  122 LEU   B H    1 
ATOM   5977 H HA   . LEU   B 1 122 ? 42.021 -17.406 -10.054 1.00 12.91 ?  122 LEU   B HA   1 
ATOM   5978 H HB2  . LEU   B 1 122 ? 40.223 -19.186 -8.804  1.00 15.22 ?  122 LEU   B HB2  1 
ATOM   5979 H HB3  . LEU   B 1 122 ? 41.370 -18.359 -8.100  1.00 15.22 ?  122 LEU   B HB3  1 
ATOM   5980 H HG   . LEU   B 1 122 ? 39.854 -16.442 -8.673  1.00 15.55 ?  122 LEU   B HG   1 
ATOM   5981 H HD11 . LEU   B 1 122 ? 37.617 -17.030 -8.426  1.00 15.64 ?  122 LEU   B HD11 1 
ATOM   5982 H HD12 . LEU   B 1 122 ? 38.232 -17.711 -9.722  1.00 15.64 ?  122 LEU   B HD12 1 
ATOM   5983 H HD13 . LEU   B 1 122 ? 38.027 -18.564 -8.398  1.00 15.64 ?  122 LEU   B HD13 1 
ATOM   5984 H HD21 . LEU   B 1 122 ? 39.014 -16.542 -6.488  1.00 14.46 ?  122 LEU   B HD21 1 
ATOM   5985 H HD22 . LEU   B 1 122 ? 39.531 -18.040 -6.373  1.00 14.46 ?  122 LEU   B HD22 1 
ATOM   5986 H HD23 . LEU   B 1 122 ? 40.573 -16.849 -6.516  1.00 14.46 ?  122 LEU   B HD23 1 
ATOM   5987 N N    . LEU   B 1 123 ? 43.278 -19.539 -10.111 1.00 10.18 ?  123 LEU   B N    1 
ATOM   5988 C CA   . LEU   B 1 123 ? 43.987 -20.811 -9.990  1.00 10.56 ?  123 LEU   B CA   1 
ATOM   5989 C C    . LEU   B 1 123 ? 43.954 -21.201 -8.519  1.00 10.10 ?  123 LEU   B C    1 
ATOM   5990 O O    . LEU   B 1 123 ? 44.308 -20.375 -7.669  1.00 10.69 ?  123 LEU   B O    1 
ATOM   5991 C CB   . LEU   B 1 123 ? 45.437 -20.629 -10.446 1.00 11.27 ?  123 LEU   B CB   1 
ATOM   5992 C CG   . LEU   B 1 123 ? 46.371 -21.815 -10.203 1.00 11.53 ?  123 LEU   B CG   1 
ATOM   5993 C CD1  . LEU   B 1 123 ? 45.937 -23.074 -10.966 1.00 12.21 ?  123 LEU   B CD1  1 
ATOM   5994 C CD2  . LEU   B 1 123 ? 47.788 -21.426 -10.571 1.00 12.69 ?  123 LEU   B CD2  1 
ATOM   5995 H H    . LEU   B 1 123 ? 43.774 -18.861 -9.901  1.00 12.22 ?  123 LEU   B H    1 
ATOM   5996 H HA   . LEU   B 1 123 ? 43.551 -21.493 -10.519 1.00 12.68 ?  123 LEU   B HA   1 
ATOM   5997 H HB2  . LEU   B 1 123 ? 45.430 -20.451 -11.399 1.00 13.52 ?  123 LEU   B HB2  1 
ATOM   5998 H HB3  . LEU   B 1 123 ? 45.808 -19.863 -9.978  1.00 13.52 ?  123 LEU   B HB3  1 
ATOM   5999 H HG   . LEU   B 1 123 ? 46.363 -22.029 -9.255  1.00 13.84 ?  123 LEU   B HG   1 
ATOM   6000 H HD11 . LEU   B 1 123 ? 46.572 -23.784 -10.782 1.00 14.66 ?  123 LEU   B HD11 1 
ATOM   6001 H HD12 . LEU   B 1 123 ? 45.052 -23.338 -10.662 1.00 14.66 ?  123 LEU   B HD12 1 
ATOM   6002 H HD13 . LEU   B 1 123 ? 45.919 -22.878 -11.912 1.00 14.66 ?  123 LEU   B HD13 1 
ATOM   6003 H HD21 . LEU   B 1 123 ? 48.372 -22.182 -10.416 1.00 15.23 ?  123 LEU   B HD21 1 
ATOM   6004 H HD22 . LEU   B 1 123 ? 47.810 -21.174 -11.508 1.00 15.23 ?  123 LEU   B HD22 1 
ATOM   6005 H HD23 . LEU   B 1 123 ? 48.061 -20.675 -10.020 1.00 15.23 ?  123 LEU   B HD23 1 
ATOM   6006 N N    . ALA   B 1 124 ? 43.512 -22.427 -8.204  1.00 9.76  ?  124 ALA   B N    1 
ATOM   6007 C CA   . ALA   B 1 124 ? 43.253 -22.739 -6.804  1.00 10.32 ?  124 ALA   B CA   1 
ATOM   6008 C C    . ALA   B 1 124 ? 43.528 -24.197 -6.477  1.00 10.06 ?  124 ALA   B C    1 
ATOM   6009 O O    . ALA   B 1 124 ? 43.397 -25.075 -7.341  1.00 10.59 ?  124 ALA   B O    1 
ATOM   6010 C CB   . ALA   B 1 124 ? 41.802 -22.422 -6.432  1.00 10.96 ?  124 ALA   B CB   1 
ATOM   6011 H H    . ALA   B 1 124 ? 43.348 -23.068 -8.766  1.00 11.71 ?  124 ALA   B H    1 
ATOM   6012 H HA   . ALA   B 1 124 ? 43.836 -22.194 -6.262  1.00 12.39 ?  124 ALA   B HA   1 
ATOM   6013 H HB1  . ALA   B 1 124 ? 41.657 -22.640 -5.502  1.00 13.15 ?  124 ALA   B HB1  1 
ATOM   6014 H HB2  . ALA   B 1 124 ? 41.643 -21.478 -6.585  1.00 13.15 ?  124 ALA   B HB2  1 
ATOM   6015 H HB3  . ALA   B 1 124 ? 41.210 -22.951 -6.994  1.00 13.15 ?  124 ALA   B HB3  1 
ATOM   6016 N N    . PRO   B 1 125 ? 43.828 -24.490 -5.214  1.00 10.40 ?  125 PRO   B N    1 
ATOM   6017 C CA   . PRO   B 1 125 ? 43.766 -25.856 -4.692  1.00 10.81 ?  125 PRO   B CA   1 
ATOM   6018 C C    . PRO   B 1 125 ? 42.363 -26.124 -4.148  1.00 11.19 ?  125 PRO   B C    1 
ATOM   6019 O O    . PRO   B 1 125 ? 41.566 -25.208 -3.947  1.00 11.44 ?  125 PRO   B O    1 
ATOM   6020 C CB   . PRO   B 1 125 ? 44.750 -25.779 -3.521  1.00 11.81 ?  125 PRO   B CB   1 
ATOM   6021 C CG   . PRO   B 1 125 ? 44.495 -24.390 -2.950  1.00 11.75 ?  125 PRO   B CG   1 
ATOM   6022 C CD   . PRO   B 1 125 ? 44.152 -23.524 -4.148  1.00 10.90 ?  125 PRO   B CD   1 
ATOM   6023 H HA   . PRO   B 1 125 ? 44.039 -26.524 -5.343  1.00 12.97 ?  125 PRO   B HA   1 
ATOM   6024 H HB2  . PRO   B 1 125 ? 44.543 -26.469 -2.866  1.00 14.17 ?  125 PRO   B HB2  1 
ATOM   6025 H HB3  . PRO   B 1 125 ? 45.660 -25.865 -3.840  1.00 14.17 ?  125 PRO   B HB3  1 
ATOM   6026 H HG2  . PRO   B 1 125 ? 43.749 -24.422 -2.327  1.00 14.10 ?  125 PRO   B HG2  1 
ATOM   6027 H HG3  . PRO   B 1 125 ? 45.295 -24.068 -2.503  1.00 14.10 ?  125 PRO   B HG3  1 
ATOM   6028 H HD2  . PRO   B 1 125 ? 43.390 -22.966 -3.956  1.00 13.08 ?  125 PRO   B HD2  1 
ATOM   6029 H HD3  . PRO   B 1 125 ? 44.929 -22.989 -4.401  1.00 13.08 ?  125 PRO   B HD3  1 
ATOM   6030 N N    . LEU   B 1 126 ? 42.091 -27.398 -3.856  1.00 12.06 ?  126 LEU   B N    1 
ATOM   6031 C CA   . LEU   B 1 126 ? 40.871 -27.757 -3.135  1.00 12.33 ?  126 LEU   B CA   1 
ATOM   6032 C C    . LEU   B 1 126 ? 40.989 -27.350 -1.674  1.00 12.46 ?  126 LEU   B C    1 
ATOM   6033 O O    . LEU   B 1 126 ? 41.882 -27.807 -0.956  1.00 14.54 ?  126 LEU   B O    1 
ATOM   6034 C CB   . LEU   B 1 126 ? 40.604 -29.251 -3.237  1.00 14.17 ?  126 LEU   B CB   1 
ATOM   6035 C CG   . LEU   B 1 126 ? 40.100 -29.752 -4.588  1.00 14.90 ?  126 LEU   B CG   1 
ATOM   6036 C CD1  . LEU   B 1 126 ? 40.122 -31.262 -4.630  1.00 16.76 ?  126 LEU   B CD1  1 
ATOM   6037 C CD2  . LEU   B 1 126 ? 38.693 -29.241 -4.871  1.00 15.03 ?  126 LEU   B CD2  1 
ATOM   6038 H H    . LEU   B 1 126 ? 42.597 -28.068 -4.056  1.00 14.47 ?  126 LEU   B H    1 
ATOM   6039 H HA   . LEU   B 1 126 ? 40.123 -27.279 -3.525  1.00 14.80 ?  126 LEU   B HA   1 
ATOM   6040 H HB2  . LEU   B 1 126 ? 41.427 -29.720 -3.040  1.00 17.01 ?  126 LEU   B HB2  1 
ATOM   6041 H HB3  . LEU   B 1 126 ? 39.932 -29.481 -2.576  1.00 17.01 ?  126 LEU   B HB3  1 
ATOM   6042 H HG   . LEU   B 1 126 ? 40.691 -29.416 -5.286  1.00 17.88 ?  126 LEU   B HG   1 
ATOM   6043 H HD11 . LEU   B 1 126 ? 39.800 -31.556 -5.495  1.00 20.11 ?  126 LEU   B HD11 1 
ATOM   6044 H HD12 . LEU   B 1 126 ? 41.030 -31.569 -4.489  1.00 20.11 ?  126 LEU   B HD12 1 
ATOM   6045 H HD13 . LEU   B 1 126 ? 39.544 -31.601 -3.928  1.00 20.11 ?  126 LEU   B HD13 1 
ATOM   6046 H HD21 . LEU   B 1 126 ? 38.366 -29.660 -5.682  1.00 18.04 ?  126 LEU   B HD21 1 
ATOM   6047 H HD22 . LEU   B 1 126 ? 38.120 -29.468 -4.124  1.00 18.04 ?  126 LEU   B HD22 1 
ATOM   6048 H HD23 . LEU   B 1 126 ? 38.720 -28.276 -4.986  1.00 18.04 ?  126 LEU   B HD23 1 
ATOM   6049 N N    . LEU   B 1 127 ? 40.056 -26.529 -1.217  1.00 12.50 ?  127 LEU   B N    1 
ATOM   6050 C CA   . LEU   B 1 127 ? 40.113 -26.033 0.146   1.00 13.07 ?  127 LEU   B CA   1 
ATOM   6051 C C    . LEU   B 1 127 ? 39.833 -27.149 1.144   1.00 12.82 ?  127 LEU   B C    1 
ATOM   6052 O O    . LEU   B 1 127 ? 39.010 -28.042 0.923   1.00 13.33 ?  127 LEU   B O    1 
ATOM   6053 C CB   . LEU   B 1 127 ? 39.101 -24.907 0.354   1.00 13.74 ?  127 LEU   B CB   1 
ATOM   6054 C CG   . LEU   B 1 127 ? 39.293 -23.640 -0.484  1.00 13.85 ?  127 LEU   B CG   1 
ATOM   6055 C CD1  . LEU   B 1 127 ? 38.169 -22.675 -0.155  1.00 14.34 ?  127 LEU   B CD1  1 
ATOM   6056 C CD2  . LEU   B 1 127 ? 40.669 -23.002 -0.267  1.00 14.60 ?  127 LEU   B CD2  1 
ATOM   6057 H H    . LEU   B 1 127 ? 39.381 -26.231 -1.677  1.00 15.00 ?  127 LEU   B H    1 
ATOM   6058 H HA   . LEU   B 1 127 ? 41.001 -25.676 0.318   1.00 15.68 ?  127 LEU   B HA   1 
ATOM   6059 H HB2  . LEU   B 1 127 ? 38.218 -25.253 0.151   1.00 16.49 ?  127 LEU   B HB2  1 
ATOM   6060 H HB3  . LEU   B 1 127 ? 39.132 -24.641 1.288   1.00 16.49 ?  127 LEU   B HB3  1 
ATOM   6061 H HG   . LEU   B 1 127 ? 39.215 -23.868 -1.420  1.00 16.62 ?  127 LEU   B HG   1 
ATOM   6062 H HD11 . LEU   B 1 127 ? 38.285 -21.861 -0.676  1.00 17.21 ?  127 LEU   B HD11 1 
ATOM   6063 H HD12 . LEU   B 1 127 ? 37.320 -23.086 -0.372  1.00 17.21 ?  127 LEU   B HD12 1 
ATOM   6064 H HD13 . LEU   B 1 127 ? 38.200 -22.460 0.793   1.00 17.21 ?  127 LEU   B HD13 1 
ATOM   6065 H HD21 . LEU   B 1 127 ? 40.708 -22.158 -0.747  1.00 17.52 ?  127 LEU   B HD21 1 
ATOM   6066 H HD22 . LEU   B 1 127 ? 40.804 -22.847 0.682   1.00 17.52 ?  127 LEU   B HD22 1 
ATOM   6067 H HD23 . LEU   B 1 127 ? 41.352 -23.603 -0.603  1.00 17.52 ?  127 LEU   B HD23 1 
ATOM   6068 N N    . SER   B 1 128 ? 40.513 -27.062 2.276   1.00 12.99 ?  128 SER   B N    1 
ATOM   6069 C CA   . SER   B 1 128 ? 40.399 -27.975 3.400   1.00 13.40 ?  128 SER   B CA   1 
ATOM   6070 C C    . SER   B 1 128 ? 40.885 -29.389 3.085   1.00 14.77 ?  128 SER   B C    1 
ATOM   6071 O O    . SER   B 1 128 ? 40.787 -30.258 3.947   1.00 16.41 ?  128 SER   B O    1 
ATOM   6072 C CB   . SER   B 1 128 ? 38.998 -27.972 4.037   1.00 13.53 ?  128 SER   B CB   1 
ATOM   6073 O OG   . SER   B 1 128 ? 38.706 -26.681 4.577   1.00 14.00 ?  128 SER   B OG   1 
ATOM   6074 H H    . SER   B 1 128 ? 41.075 -26.433 2.427   1.00 15.59 ?  128 SER   B H    1 
ATOM   6075 H HA   . SER   B 1 128 ? 40.993 -27.638 4.081   1.00 16.08 ?  128 SER   B HA   1 
ATOM   6076 H HB2  . SER   B 1 128 ? 38.335 -28.202 3.370   1.00 16.24 ?  128 SER   B HB2  1 
ATOM   6077 H HB3  . SER   B 1 128 ? 38.980 -28.633 4.760   1.00 16.24 ?  128 SER   B HB3  1 
ATOM   6078 H HG   . SER   B 1 128 ? 39.281 -26.483 5.159   1.00 16.80 ?  128 SER   B HG   1 
ATOM   6079 N N    . ALA   B 1 129 ? 41.463 -29.625 1.901   1.00 15.83 ?  129 ALA   B N    1 
ATOM   6080 C CA   . ALA   B 1 129 ? 42.013 -30.921 1.532   1.00 16.80 ?  129 ALA   B CA   1 
ATOM   6081 C C    . ALA   B 1 129 ? 43.403 -31.107 2.130   1.00 15.76 ?  129 ALA   B C    1 
ATOM   6082 O O    . ALA   B 1 129 ? 43.965 -30.213 2.775   1.00 15.28 ?  129 ALA   B O    1 
ATOM   6083 C CB   . ALA   B 1 129 ? 42.077 -31.058 0.012   1.00 18.49 ?  129 ALA   B CB   1 
ATOM   6084 H H    . ALA   B 1 129 ? 41.546 -29.034 1.275   1.00 19.00 ?  129 ALA   B H    1 
ATOM   6085 H HA   . ALA   B 1 129 ? 41.440 -31.619 1.875   1.00 20.16 ?  129 ALA   B HA   1 
ATOM   6086 H HB1  . ALA   B 1 129 ? 42.438 -31.932 -0.213  1.00 22.18 ?  129 ALA   B HB1  1 
ATOM   6087 H HB2  . ALA   B 1 129 ? 41.185 -30.965 -0.353  1.00 22.18 ?  129 ALA   B HB2  1 
ATOM   6088 H HB3  . ALA   B 1 129 ? 42.655 -30.363 -0.346  1.00 22.18 ?  129 ALA   B HB3  1 
ATOM   6089 N N    . GLY   B 1 130 ? 43.964 -32.291 1.899   1.00 15.77 ?  130 GLY   B N    1 
ATOM   6090 C CA   . GLY   B 1 130 ? 45.352 -32.530 2.251   1.00 16.63 ?  130 GLY   B CA   1 
ATOM   6091 C C    . GLY   B 1 130 ? 45.565 -32.421 3.743   1.00 16.55 ?  130 GLY   B C    1 
ATOM   6092 O O    . GLY   B 1 130 ? 44.865 -33.058 4.543   1.00 17.30 ?  130 GLY   B O    1 
ATOM   6093 H H    . GLY   B 1 130 ? 43.567 -32.963 1.535   1.00 18.92 ?  130 GLY   B H    1 
ATOM   6094 H HA2  . GLY   B 1 130 ? 45.617 -33.420 1.958   1.00 19.96 ?  130 GLY   B HA2  1 
ATOM   6095 H HA3  . GLY   B 1 130 ? 45.923 -31.882 1.808   1.00 19.96 ?  130 GLY   B HA3  1 
ATOM   6096 N N    . ILE   B 1 131 ? 46.547 -31.599 4.130   1.00 16.99 ?  131 ILE   B N    1 
ATOM   6097 C CA   . ILE   B 1 131 ? 46.914 -31.470 5.531   1.00 18.05 ?  131 ILE   B CA   1 
ATOM   6098 C C    . ILE   B 1 131 ? 45.801 -30.873 6.374   1.00 17.37 ?  131 ILE   B C    1 
ATOM   6099 O O    . ILE   B 1 131 ? 45.879 -30.928 7.601   1.00 18.41 ?  131 ILE   B O    1 
ATOM   6100 C CB   . ILE   B 1 131 ? 48.235 -30.685 5.729   1.00 19.82 ?  131 ILE   B CB   1 
ATOM   6101 C CG1  . ILE   B 1 131 ? 48.062 -29.204 5.363   1.00 20.60 ?  131 ILE   B CG1  1 
ATOM   6102 C CG2  . ILE   B 1 131 ? 49.361 -31.318 4.916   1.00 20.88 ?  131 ILE   B CG2  1 
ATOM   6103 C CD1  . ILE   B 1 131 ? 49.285 -28.347 5.666   1.00 21.78 ?  131 ILE   B CD1  1 
ATOM   6104 H H    . ILE   B 1 131 ? 47.011 -31.108 3.594   1.00 20.39 ?  131 ILE   B H    1 
ATOM   6105 H HA   . ILE   B 1 131 ? 47.069 -32.359 5.877   1.00 21.66 ?  131 ILE   B HA   1 
ATOM   6106 H HB   . ILE   B 1 131 ? 48.472 -30.734 6.670   1.00 23.78 ?  131 ILE   B HB   1 
ATOM   6107 H HG12 . ILE   B 1 131 ? 47.878 -29.139 4.413   1.00 24.72 ?  131 ILE   B HG12 1 
ATOM   6108 H HG13 . ILE   B 1 131 ? 47.317 -28.833 5.865   1.00 24.72 ?  131 ILE   B HG13 1 
ATOM   6109 H HG21 . ILE   B 1 131 ? 50.201 -30.909 5.171   1.00 25.06 ?  131 ILE   B HG21 1 
ATOM   6110 H HG22 . ILE   B 1 131 ? 49.382 -32.267 5.099   1.00 25.06 ?  131 ILE   B HG22 1 
ATOM   6111 H HG23 . ILE   B 1 131 ? 49.188 -31.164 3.973   1.00 25.06 ?  131 ILE   B HG23 1 
ATOM   6112 H HD11 . ILE   B 1 131 ? 49.061 -27.416 5.509   1.00 26.14 ?  131 ILE   B HD11 1 
ATOM   6113 H HD12 . ILE   B 1 131 ? 49.535 -28.475 6.594   1.00 26.14 ?  131 ILE   B HD12 1 
ATOM   6114 H HD13 . ILE   B 1 131 ? 50.010 -28.617 5.084   1.00 26.14 ?  131 ILE   B HD13 1 
ATOM   6115 N N    . PHE   B 1 132 ? 44.767 -30.304 5.747   1.00 16.34 ?  132 PHE   B N    1 
ATOM   6116 C CA   . PHE   B 1 132 ? 43.619 -29.779 6.477   1.00 16.79 ?  132 PHE   B CA   1 
ATOM   6117 C C    . PHE   B 1 132 ? 42.584 -30.853 6.807   1.00 18.19 ?  132 PHE   B C    1 
ATOM   6118 O O    . PHE   B 1 132 ? 41.669 -30.582 7.595   1.00 19.66 ?  132 PHE   B O    1 
ATOM   6119 C CB   . PHE   B 1 132 ? 42.951 -28.647 5.684   1.00 15.59 ?  132 PHE   B CB   1 
ATOM   6120 C CG   . PHE   B 1 132 ? 43.646 -27.304 5.793   1.00 15.02 ?  132 PHE   B CG   1 
ATOM   6121 C CD1  . PHE   B 1 132 ? 44.946 -27.121 5.338   1.00 16.28 ?  132 PHE   B CD1  1 
ATOM   6122 C CD2  . PHE   B 1 132 ? 42.957 -26.208 6.292   1.00 14.12 ?  132 PHE   B CD2  1 
ATOM   6123 C CE1  . PHE   B 1 132 ? 45.560 -25.882 5.434   1.00 16.66 ?  132 PHE   B CE1  1 
ATOM   6124 C CE2  . PHE   B 1 132 ? 43.556 -24.963 6.370   1.00 14.86 ?  132 PHE   B CE2  1 
ATOM   6125 C CZ   . PHE   B 1 132 ? 44.859 -24.800 5.945   1.00 16.11 ?  132 PHE   B CZ   1 
ATOM   6126 H H    . PHE   B 1 132 ? 44.704 -30.219 4.896   1.00 19.61 ?  132 PHE   B H    1 
ATOM   6127 H HA   . PHE   B 1 132 ? 43.930 -29.410 7.315   1.00 20.14 ?  132 PHE   B HA   1 
ATOM   6128 H HB2  . PHE   B 1 132 ? 42.941 -28.895 4.747   1.00 18.71 ?  132 PHE   B HB2  1 
ATOM   6129 H HB3  . PHE   B 1 132 ? 42.042 -28.540 6.005   1.00 18.71 ?  132 PHE   B HB3  1 
ATOM   6130 H HD1  . PHE   B 1 132 ? 45.417 -27.854 5.003   1.00 19.53 ?  132 PHE   B HD1  1 
ATOM   6131 H HD2  . PHE   B 1 132 ? 42.078 -26.316 6.585   1.00 16.94 ?  132 PHE   B HD2  1 
ATOM   6132 H HE1  . PHE   B 1 132 ? 46.433 -25.776 5.143   1.00 19.99 ?  132 PHE   B HE1  1 
ATOM   6133 H HE2  . PHE   B 1 132 ? 43.083 -24.243 6.727   1.00 17.83 ?  132 PHE   B HE2  1 
ATOM   6134 H HZ   . PHE   B 1 132 ? 45.262 -23.965 6.010   1.00 19.33 ?  132 PHE   B HZ   1 
ATOM   6135 N N    . GLY   B 1 133 ? 42.680 -32.049 6.211   1.00 17.80 ?  133 GLY   B N    1 
ATOM   6136 C CA   . GLY   B 1 133 ? 41.968 -33.214 6.702   1.00 18.53 ?  133 GLY   B CA   1 
ATOM   6137 C C    . GLY   B 1 133 ? 40.570 -33.471 6.169   1.00 19.08 ?  133 GLY   B C    1 
ATOM   6138 O O    . GLY   B 1 133 ? 39.981 -34.495 6.534   1.00 21.30 ?  133 GLY   B O    1 
ATOM   6139 H H    . GLY   B 1 133 ? 43.162 -32.205 5.513   1.00 21.36 ?  133 GLY   B H    1 
ATOM   6140 H HA2  . GLY   B 1 133 ? 42.498 -34.002 6.506   1.00 22.24 ?  133 GLY   B HA2  1 
ATOM   6141 H HA3  . GLY   B 1 133 ? 41.894 -33.143 7.665   1.00 22.24 ?  133 GLY   B HA3  1 
ATOM   6142 N N    . ALA   B 1 134 ? 40.009 -32.599 5.337   1.00 17.82 ?  134 ALA   B N    1 
ATOM   6143 C CA   . ALA   B 1 134 ? 38.685 -32.877 4.800   1.00 18.12 ?  134 ALA   B CA   1 
ATOM   6144 C C    . ALA   B 1 134 ? 38.772 -33.869 3.645   1.00 17.67 ?  134 ALA   B C    1 
ATOM   6145 O O    . ALA   B 1 134 ? 39.827 -34.059 3.029   1.00 18.74 ?  134 ALA   B O    1 
ATOM   6146 C CB   . ALA   B 1 134 ? 38.012 -31.593 4.317   1.00 18.36 ?  134 ALA   B CB   1 
ATOM   6147 H H    . ALA   B 1 134 ? 40.358 -31.852 5.083   1.00 21.38 ?  134 ALA   B H    1 
ATOM   6148 H HA   . ALA   B 1 134 ? 38.130 -33.262 5.497   1.00 21.74 ?  134 ALA   B HA   1 
ATOM   6149 H HB1  . ALA   B 1 134 ? 37.125 -31.808 3.984   1.00 22.04 ?  134 ALA   B HB1  1 
ATOM   6150 H HB2  . ALA   B 1 134 ? 37.945 -30.972 5.058   1.00 22.04 ?  134 ALA   B HB2  1 
ATOM   6151 H HB3  . ALA   B 1 134 ? 38.545 -31.205 3.606   1.00 22.04 ?  134 ALA   B HB3  1 
ATOM   6152 N N    . ASP   B 1 135 ? 37.641 -34.501 3.356   1.00 18.08 ?  135 ASP   B N    1 
ATOM   6153 C CA   . ASP   B 1 135 ? 37.547 -35.396 2.212   1.00 19.02 ?  135 ASP   B CA   1 
ATOM   6154 C C    . ASP   B 1 135 ? 37.642 -34.557 0.944   1.00 17.59 ?  135 ASP   B C    1 
ATOM   6155 O O    . ASP   B 1 135 ? 36.780 -33.695 0.716   1.00 18.07 ?  135 ASP   B O    1 
ATOM   6156 C CB   . ASP   B 1 135 ? 36.210 -36.133 2.266   1.00 20.67 ?  135 ASP   B CB   1 
ATOM   6157 C CG   . ASP   B 1 135 ? 36.041 -37.144 1.149   1.00 22.63 ?  135 ASP   B CG   1 
ATOM   6158 O OD1  . ASP   B 1 135 ? 36.889 -37.193 0.236   1.00 22.43 ?  135 ASP   B OD1  1 
ATOM   6159 O OD2  . ASP   B 1 135 ? 35.048 -37.905 1.197   1.00 25.90 -1 135 ASP   B OD2  1 
ATOM   6160 H H    . ASP   B 1 135 ? 36.911 -34.426 3.805   1.00 21.69 ?  135 ASP   B H    1 
ATOM   6161 H HA   . ASP   B 1 135 ? 38.268 -36.046 2.244   1.00 22.82 ?  135 ASP   B HA   1 
ATOM   6162 H HB2  . ASP   B 1 135 ? 36.148 -36.605 3.110   1.00 24.81 ?  135 ASP   B HB2  1 
ATOM   6163 H HB3  . ASP   B 1 135 ? 35.495 -35.491 2.185   1.00 24.81 ?  135 ASP   B HB3  1 
ATOM   6164 N N    . PRO   B 1 136 ? 38.656 -34.758 0.100   1.00 17.65 ?  136 PRO   B N    1 
ATOM   6165 C CA   . PRO   B 1 136 ? 38.742 -33.949 -1.125  1.00 17.10 ?  136 PRO   B CA   1 
ATOM   6166 C C    . PRO   B 1 136 ? 37.540 -34.103 -2.036  1.00 16.41 ?  136 PRO   B C    1 
ATOM   6167 O O    . PRO   B 1 136 ? 37.215 -33.153 -2.757  1.00 15.13 ?  136 PRO   B O    1 
ATOM   6168 C CB   . PRO   B 1 136 ? 40.047 -34.431 -1.780  1.00 18.12 ?  136 PRO   B CB   1 
ATOM   6169 C CG   . PRO   B 1 136 ? 40.265 -35.818 -1.216  1.00 19.35 ?  136 PRO   B CG   1 
ATOM   6170 C CD   . PRO   B 1 136 ? 39.744 -35.749 0.189   1.00 19.01 ?  136 PRO   B CD   1 
ATOM   6171 H HA   . PRO   B 1 136 ? 38.829 -33.014 -0.901  1.00 20.51 ?  136 PRO   B HA   1 
ATOM   6172 H HB2  . PRO   B 1 136 ? 39.947 -34.458 -2.746  1.00 21.75 ?  136 PRO   B HB2  1 
ATOM   6173 H HB3  . PRO   B 1 136 ? 40.772 -33.833 -1.529  1.00 21.75 ?  136 PRO   B HB3  1 
ATOM   6174 H HG2  . PRO   B 1 136 ? 39.765 -36.465 -1.736  1.00 23.23 ?  136 PRO   B HG2  1 
ATOM   6175 H HG3  . PRO   B 1 136 ? 41.212 -36.028 -1.219  1.00 23.23 ?  136 PRO   B HG3  1 
ATOM   6176 H HD2  . PRO   B 1 136 ? 39.398 -36.612 0.463   1.00 22.81 ?  136 PRO   B HD2  1 
ATOM   6177 H HD3  . PRO   B 1 136 ? 40.431 -35.429 0.796   1.00 22.81 ?  136 PRO   B HD3  1 
ATOM   6178 N N    . ILE   B 1 137 ? 36.873 -35.265 -2.026  1.00 16.52 ?  137 ILE   B N    1 
ATOM   6179 C CA   . ILE   B 1 137 ? 35.650 -35.439 -2.809  1.00 16.80 ?  137 ILE   B CA   1 
ATOM   6180 C C    . ILE   B 1 137 ? 34.574 -34.469 -2.335  1.00 16.25 ?  137 ILE   B C    1 
ATOM   6181 O O    . ILE   B 1 137 ? 33.857 -33.859 -3.140  1.00 15.91 ?  137 ILE   B O    1 
ATOM   6182 C CB   . ILE   B 1 137 ? 35.177 -36.907 -2.738  1.00 18.85 ?  137 ILE   B CB   1 
ATOM   6183 C CG1  . ILE   B 1 137 ? 36.186 -37.812 -3.444  1.00 21.08 ?  137 ILE   B CG1  1 
ATOM   6184 C CG2  . ILE   B 1 137 ? 33.792 -37.063 -3.356  1.00 19.78 ?  137 ILE   B CG2  1 
ATOM   6185 C CD1  . ILE   B 1 137 ? 35.892 -39.294 -3.293  1.00 23.48 ?  137 ILE   B CD1  1 
ATOM   6186 H H    . ILE   B 1 137 ? 37.102 -35.960 -1.578  1.00 19.83 ?  137 ILE   B H    1 
ATOM   6187 H HA   . ILE   B 1 137 ? 35.837 -35.238 -3.740  1.00 20.17 ?  137 ILE   B HA   1 
ATOM   6188 H HB   . ILE   B 1 137 ? 35.124 -37.168 -1.809  1.00 22.62 ?  137 ILE   B HB   1 
ATOM   6189 H HG12 . ILE   B 1 137 ? 36.184 -37.611 -4.392  1.00 25.29 ?  137 ILE   B HG12 1 
ATOM   6190 H HG13 . ILE   B 1 137 ? 37.066 -37.651 -3.073  1.00 25.29 ?  137 ILE   B HG13 1 
ATOM   6191 H HG21 . ILE   B 1 137 ? 33.553 -38.004 -3.375  1.00 23.73 ?  137 ILE   B HG21 1 
ATOM   6192 H HG22 . ILE   B 1 137 ? 33.145 -36.582 -2.821  1.00 23.73 ?  137 ILE   B HG22 1 
ATOM   6193 H HG23 . ILE   B 1 137 ? 33.808 -36.711 -4.259  1.00 23.73 ?  137 ILE   B HG23 1 
ATOM   6194 H HD11 . ILE   B 1 137 ? 36.586 -39.791 -3.752  1.00 28.17 ?  137 ILE   B HD11 1 
ATOM   6195 H HD12 . ILE   B 1 137 ? 35.889 -39.527 -2.349  1.00 28.17 ?  137 ILE   B HD12 1 
ATOM   6196 H HD13 . ILE   B 1 137 ? 35.032 -39.502 -3.689  1.00 28.17 ?  137 ILE   B HD13 1 
ATOM   6197 N N    . HIS   B 1 138 ? 34.442 -34.314 -1.021  1.00 16.31 ?  138 HIS   B N    1 
ATOM   6198 C CA   . HIS   B 1 138 ? 33.500 -33.334 -0.492  1.00 16.78 ?  138 HIS   B CA   1 
ATOM   6199 C C    . HIS   B 1 138 ? 33.931 -31.910 -0.820  1.00 15.82 ?  138 HIS   B C    1 
ATOM   6200 O O    . HIS   B 1 138 ? 33.092 -31.057 -1.125  1.00 16.37 ?  138 HIS   B O    1 
ATOM   6201 C CB   . HIS   B 1 138 ? 33.380 -33.505 1.014   1.00 18.40 ?  138 HIS   B CB   1 
ATOM   6202 C CG   . HIS   B 1 138 ? 32.450 -32.523 1.645   1.00 19.81 ?  138 HIS   B CG   1 
ATOM   6203 N ND1  . HIS   B 1 138 ? 31.111 -32.456 1.323   1.00 21.50 ?  138 HIS   B ND1  1 
ATOM   6204 C CD2  . HIS   B 1 138 ? 32.670 -31.545 2.553   1.00 20.43 ?  138 HIS   B CD2  1 
ATOM   6205 C CE1  . HIS   B 1 138 ? 30.542 -31.489 2.020   1.00 21.66 ?  138 HIS   B CE1  1 
ATOM   6206 N NE2  . HIS   B 1 138 ? 31.465 -30.924 2.778   1.00 20.76 ?  138 HIS   B NE2  1 
ATOM   6207 H H    . HIS   B 1 138 ? 34.875 -34.760 -0.427  1.00 19.57 ?  138 HIS   B H    1 
ATOM   6208 H HA   . HIS   B 1 138 ? 32.626 -33.491 -0.886  1.00 20.14 ?  138 HIS   B HA   1 
ATOM   6209 H HB2  . HIS   B 1 138 ? 33.043 -34.396 1.205   1.00 22.08 ?  138 HIS   B HB2  1 
ATOM   6210 H HB3  . HIS   B 1 138 ? 34.252 -33.388 1.416   1.00 22.08 ?  138 HIS   B HB3  1 
ATOM   6211 H HD1  . HIS   B 1 138 ? 30.707 -32.972 0.761   1.00 25.80 ?  138 HIS   B HD1  1 
ATOM   6212 H HD2  . HIS   B 1 138 ? 33.473 -31.342 2.965   1.00 24.52 ?  138 HIS   B HD2  1 
ATOM   6213 H HE1  . HIS   B 1 138 ? 29.637 -31.259 1.988   1.00 25.99 ?  138 HIS   B HE1  1 
ATOM   6214 N N    . SER   B 1 139 ? 35.228 -31.627 -0.751  1.00 14.98 ?  139 SER   B N    1 
ATOM   6215 C CA   . SER   B 1 139 ? 35.674 -30.281 -1.070  1.00 14.50 ?  139 SER   B CA   1 
ATOM   6216 C C    . SER   B 1 139 ? 35.337 -29.925 -2.507  1.00 13.25 ?  139 SER   B C    1 
ATOM   6217 O O    . SER   B 1 139 ? 34.901 -28.803 -2.785  1.00 13.69 ?  139 SER   B O    1 
ATOM   6218 C CB   . SER   B 1 139 ? 37.168 -30.132 -0.809  1.00 14.47 ?  139 SER   B CB   1 
ATOM   6219 O OG   . SER   B 1 139 ? 37.580 -28.794 -1.068  1.00 14.60 ?  139 SER   B OG   1 
ATOM   6220 H H    . SER   B 1 139 ? 35.848 -32.177 -0.537  1.00 17.97 ?  139 SER   B H    1 
ATOM   6221 H HA   . SER   B 1 139 ? 35.204 -29.652 -0.501  1.00 17.40 ?  139 SER   B HA   1 
ATOM   6222 H HB2  . SER   B 1 139 ? 37.346 -30.354 0.120   1.00 17.36 ?  139 SER   B HB2  1 
ATOM   6223 H HB3  . SER   B 1 139 ? 37.655 -30.728 -1.395  1.00 17.36 ?  139 SER   B HB3  1 
ATOM   6224 H HG   . SER   B 1 139 ? 38.403 -28.712 -0.904  1.00 17.52 ?  139 SER   B HG   1 
ATOM   6225 N N    . LEU   B 1 140 ? 35.518 -30.871 -3.431  1.00 12.89 ?  140 LEU   B N    1 
ATOM   6226 C CA   . LEU   B 1 140 ? 35.157 -30.623 -4.821  1.00 13.37 ?  140 LEU   B CA   1 
ATOM   6227 C C    . LEU   B 1 140 ? 33.656 -30.389 -4.954  1.00 14.03 ?  140 LEU   B C    1 
ATOM   6228 O O    . LEU   B 1 140 ? 33.221 -29.499 -5.691  1.00 13.75 ?  140 LEU   B O    1 
ATOM   6229 C CB   . LEU   B 1 140 ? 35.630 -31.788 -5.694  1.00 14.30 ?  140 LEU   B CB   1 
ATOM   6230 C CG   . LEU   B 1 140 ? 35.265 -31.687 -7.166  1.00 14.52 ?  140 LEU   B CG   1 
ATOM   6231 C CD1  . LEU   B 1 140 ? 35.848 -30.412 -7.771  1.00 15.28 ?  140 LEU   B CD1  1 
ATOM   6232 C CD2  . LEU   B 1 140 ? 35.731 -32.924 -7.911  1.00 15.25 ?  140 LEU   B CD2  1 
ATOM   6233 H H    . LEU   B 1 140 ? 35.849 -31.647 -3.283  1.00 15.47 ?  140 LEU   B H    1 
ATOM   6234 H HA   . LEU   B 1 140 ? 35.620 -29.824 -5.129  1.00 16.05 ?  140 LEU   B HA   1 
ATOM   6235 H HB2  . LEU   B 1 140 ? 36.599 -31.851 -5.641  1.00 17.16 ?  140 LEU   B HB2  1 
ATOM   6236 H HB3  . LEU   B 1 140 ? 35.236 -32.608 -5.360  1.00 17.16 ?  140 LEU   B HB3  1 
ATOM   6237 H HG   . LEU   B 1 140 ? 34.304 -31.634 -7.249  1.00 17.42 ?  140 LEU   B HG   1 
ATOM   6238 H HD11 . LEU   B 1 140 ? 35.734 -30.440 -8.733  1.00 18.34 ?  140 LEU   B HD11 1 
ATOM   6239 H HD12 . LEU   B 1 140 ? 35.379 -29.644 -7.405  1.00 18.34 ?  140 LEU   B HD12 1 
ATOM   6240 H HD13 . LEU   B 1 140 ? 36.792 -30.359 -7.551  1.00 18.34 ?  140 LEU   B HD13 1 
ATOM   6241 H HD21 . LEU   B 1 140 ? 35.486 -32.835 -8.846  1.00 18.30 ?  140 LEU   B HD21 1 
ATOM   6242 H HD22 . LEU   B 1 140 ? 36.689 -33.004 -7.822  1.00 18.30 ?  140 LEU   B HD22 1 
ATOM   6243 H HD23 . LEU   B 1 140 ? 35.291 -33.698 -7.526  1.00 18.30 ?  140 LEU   B HD23 1 
ATOM   6244 N N    . ARG   B 1 141 ? 32.849 -31.180 -4.237  1.00 14.11 ?  141 ARG   B N    1 
ATOM   6245 C CA   . ARG   B 1 141 ? 31.399 -31.002 -4.223  1.00 14.83 ?  141 ARG   B CA   1 
ATOM   6246 C C    . ARG   B 1 141 ? 31.021 -29.589 -3.797  1.00 14.37 ?  141 ARG   B C    1 
ATOM   6247 O O    . ARG   B 1 141 ? 30.221 -28.908 -4.460  1.00 14.44 ?  141 ARG   B O    1 
ATOM   6248 C CB   . ARG   B 1 141 ? 30.812 -32.026 -3.245  1.00 16.31 ?  141 ARG   B CB   1 
ATOM   6249 C CG   . ARG   B 1 141 ? 29.349 -31.904 -2.928  1.00 18.33 ?  141 ARG   B CG   1 
ATOM   6250 C CD   . ARG   B 1 141 ? 28.559 -32.548 -3.994  1.00 20.25 ?  141 ARG   B CD   1 
ATOM   6251 N NE   . ARG   B 1 141 ? 28.299 -31.645 -5.102  1.00 20.27 ?  141 ARG   B NE   1 
ATOM   6252 C CZ   . ARG   B 1 141 ? 28.271 -32.009 -6.376  1.00 19.69 ?  141 ARG   B CZ   1 
ATOM   6253 N NH1  . ARG   B 1 141 ? 28.696 -33.200 -6.767  1.00 19.24 ?  141 ARG   B NH1  1 
ATOM   6254 N NH2  . ARG   B 1 141 ? 27.803 -31.155 -7.281  1.00 20.50 ?  141 ARG   B NH2  1 
ATOM   6255 H H    . ARG   B 1 141 ? 33.133 -31.822 -3.742  1.00 16.94 ?  141 ARG   B H    1 
ATOM   6256 H HA   . ARG   B 1 141 ? 31.045 -31.162 -5.105  1.00 17.80 ?  141 ARG   B HA   1 
ATOM   6257 H HB2  . ARG   B 1 141 ? 30.966 -32.911 -3.612  1.00 19.58 ?  141 ARG   B HB2  1 
ATOM   6258 H HB3  . ARG   B 1 141 ? 31.291 -31.949 -2.407  1.00 19.58 ?  141 ARG   B HB3  1 
ATOM   6259 H HG2  . ARG   B 1 141 ? 29.165 -32.344 -2.088  1.00 22.00 ?  141 ARG   B HG2  1 
ATOM   6260 H HG3  . ARG   B 1 141 ? 29.092 -30.963 -2.875  1.00 22.00 ?  141 ARG   B HG3  1 
ATOM   6261 H HD2  . ARG   B 1 141 ? 29.045 -33.323 -4.327  1.00 24.30 ?  141 ARG   B HD2  1 
ATOM   6262 H HD3  . ARG   B 1 141 ? 27.712 -32.833 -3.627  1.00 24.30 ?  141 ARG   B HD3  1 
ATOM   6263 H HE   . ARG   B 1 141 ? 28.138 -30.820 -4.916  1.00 24.32 ?  141 ARG   B HE   1 
ATOM   6264 H HH11 . ARG   B 1 141 ? 28.984 -33.771 -6.194  1.00 23.09 ?  141 ARG   B HH11 1 
ATOM   6265 H HH12 . ARG   B 1 141 ? 28.671 -33.410 -7.599  1.00 23.09 ?  141 ARG   B HH12 1 
ATOM   6266 H HH21 . ARG   B 1 141 ? 27.534 -30.373 -7.041  1.00 24.60 ?  141 ARG   B HH21 1 
ATOM   6267 H HH22 . ARG   B 1 141 ? 27.799 -31.370 -8.116  1.00 24.60 ?  141 ARG   B HH22 1 
ATOM   6268 N N    . VAL   B 1 142 ? 31.564 -29.142 -2.667  1.00 14.31 ?  142 VAL   B N    1 
ATOM   6269 C CA   . VAL   B 1 142 ? 31.234 -27.804 -2.186  1.00 13.78 ?  142 VAL   B CA   1 
ATOM   6270 C C    . VAL   B 1 142 ? 31.716 -26.748 -3.174  1.00 13.76 ?  142 VAL   B C    1 
ATOM   6271 O O    . VAL   B 1 142 ? 31.024 -25.756 -3.430  1.00 13.59 ?  142 VAL   B O    1 
ATOM   6272 C CB   . VAL   B 1 142 ? 31.789 -27.582 -0.767  1.00 14.44 ?  142 VAL   B CB   1 
ATOM   6273 C CG1  . VAL   B 1 142 ? 31.496 -26.161 -0.278  1.00 14.51 ?  142 VAL   B CG1  1 
ATOM   6274 C CG2  . VAL   B 1 142 ? 31.220 -28.620 0.189   1.00 15.34 ?  142 VAL   B CG2  1 
ATOM   6275 H H    . VAL   B 1 142 ? 32.112 -29.581 -2.167  1.00 17.17 ?  142 VAL   B H    1 
ATOM   6276 H HA   . VAL   B 1 142 ? 30.273 -27.727 -2.127  1.00 16.54 ?  142 VAL   B HA   1 
ATOM   6277 H HB   . VAL   B 1 142 ? 32.753 -27.696 -0.782  1.00 17.32 ?  142 VAL   B HB   1 
ATOM   6278 H HG11 . VAL   B 1 142 ? 31.704 -26.106 0.669   1.00 17.41 ?  142 VAL   B HG11 1 
ATOM   6279 H HG12 . VAL   B 1 142 ? 32.053 -25.537 -0.772  1.00 17.41 ?  142 VAL   B HG12 1 
ATOM   6280 H HG13 . VAL   B 1 142 ? 30.562 -25.964 -0.426  1.00 17.41 ?  142 VAL   B HG13 1 
ATOM   6281 H HG21 . VAL   B 1 142 ? 31.533 -28.429 1.086   1.00 18.41 ?  142 VAL   B HG21 1 
ATOM   6282 H HG22 . VAL   B 1 142 ? 30.252 -28.577 0.158   1.00 18.41 ?  142 VAL   B HG22 1 
ATOM   6283 H HG23 . VAL   B 1 142 ? 31.521 -29.500 -0.086  1.00 18.41 ?  142 VAL   B HG23 1 
ATOM   6284 N N    . CYS   B 1 143 ? 32.901 -26.951 -3.753  1.00 13.35 ?  143 CYS   B N    1 
ATOM   6285 C CA   . CYS   B 1 143 ? 33.400 -26.019 -4.759  1.00 13.17 ?  143 CYS   B CA   1 
ATOM   6286 C C    . CYS   B 1 143 ? 32.398 -25.873 -5.901  1.00 13.15 ?  143 CYS   B C    1 
ATOM   6287 O O    . CYS   B 1 143 ? 31.999 -24.761 -6.262  1.00 13.15 ?  143 CYS   B O    1 
ATOM   6288 C CB   . CYS   B 1 143 ? 34.754 -26.511 -5.285  1.00 13.17 ?  143 CYS   B CB   1 
ATOM   6289 S SG   . CYS   B 1 143 ? 35.512 -25.411 -6.518  1.00 13.62 ?  143 CYS   B SG   1 
ATOM   6290 H H    . CYS   B 1 143 ? 33.432 -27.604 -3.575  1.00 16.02 ?  143 CYS   B H    1 
ATOM   6291 H HA   . CYS   B 1 143 ? 33.536 -25.145 -4.355  1.00 15.80 ?  143 CYS   B HA   1 
ATOM   6292 H HB2  . CYS   B 1 143 ? 35.378 -26.587 -4.541  1.00 15.81 ?  143 CYS   B HB2  1 
ATOM   6293 H HB3  . CYS   B 1 143 ? 34.636 -27.377 -5.695  1.00 15.81 ?  143 CYS   B HB3  1 
ATOM   6294 H HG   . CYS   B 1 143 ? 36.580 -25.855 -6.844  1.00 16.34 ?  143 CYS   B HG   1 
ATOM   6295 N N    . VAL   B 1 144 ? 31.984 -26.996 -6.486  1.00 13.60 ?  144 VAL   B N    1 
ATOM   6296 C CA   . VAL   B 1 144 ? 31.081 -26.943 -7.630  1.00 14.83 ?  144 VAL   B CA   1 
ATOM   6297 C C    . VAL   B 1 144 ? 29.745 -26.317 -7.256  1.00 14.54 ?  144 VAL   B C    1 
ATOM   6298 O O    . VAL   B 1 144 ? 29.131 -25.609 -8.064  1.00 15.78 ?  144 VAL   B O    1 
ATOM   6299 C CB   . VAL   B 1 144 ? 30.912 -28.360 -8.185  1.00 17.46 ?  144 VAL   B CB   1 
ATOM   6300 C CG1  . VAL   B 1 144 ? 29.637 -28.483 -9.011  1.00 20.04 ?  144 VAL   B CG1  1 
ATOM   6301 C CG2  . VAL   B 1 144 ? 32.151 -28.771 -8.970  1.00 17.35 ?  144 VAL   B CG2  1 
ATOM   6302 H H    . VAL   B 1 144 ? 32.219 -27.787 -6.253  1.00 16.32 ?  144 VAL   B H    1 
ATOM   6303 H HA   . VAL   B 1 144 ? 31.470 -26.391 -8.325  1.00 17.80 ?  144 VAL   B HA   1 
ATOM   6304 H HB   . VAL   B 1 144 ? 30.832 -28.971 -7.435  1.00 20.96 ?  144 VAL   B HB   1 
ATOM   6305 H HG11 . VAL   B 1 144 ? 29.703 -29.281 -9.564  1.00 24.04 ?  144 VAL   B HG11 1 
ATOM   6306 H HG12 . VAL   B 1 144 ? 28.877 -28.568 -8.413  1.00 24.04 ?  144 VAL   B HG12 1 
ATOM   6307 H HG13 . VAL   B 1 144 ? 29.542 -27.703 -9.571  1.00 24.04 ?  144 VAL   B HG13 1 
ATOM   6308 H HG21 . VAL   B 1 144 ? 32.025 -29.674 -9.305  1.00 20.82 ?  144 VAL   B HG21 1 
ATOM   6309 H HG22 . VAL   B 1 144 ? 32.269 -28.158 -9.714  1.00 20.82 ?  144 VAL   B HG22 1 
ATOM   6310 H HG23 . VAL   B 1 144 ? 32.922 -28.737 -8.386  1.00 20.82 ?  144 VAL   B HG23 1 
ATOM   6311 N N    . ASP   B 1 145 ? 29.277 -26.561 -6.038  1.00 14.46 ?  145 ASP   B N    1 
ATOM   6312 C CA   . ASP   B 1 145 ? 27.972 -26.084 -5.606  1.00 15.66 ?  145 ASP   B CA   1 
ATOM   6313 C C    . ASP   B 1 145 ? 28.006 -24.662 -5.065  1.00 14.95 ?  145 ASP   B C    1 
ATOM   6314 O O    . ASP   B 1 145 ? 26.951 -24.127 -4.719  1.00 17.26 ?  145 ASP   B O    1 
ATOM   6315 C CB   . ASP   B 1 145 ? 27.396 -27.002 -4.521  1.00 17.00 ?  145 ASP   B CB   1 
ATOM   6316 C CG   . ASP   B 1 145 ? 27.025 -28.374 -5.034  1.00 19.11 ?  145 ASP   B CG   1 
ATOM   6317 O OD1  . ASP   B 1 145 ? 26.906 -28.571 -6.264  1.00 19.09 ?  145 ASP   B OD1  1 
ATOM   6318 O OD2  . ASP   B 1 145 ? 26.835 -29.261 -4.179  1.00 20.93 -1 145 ASP   B OD2  1 
ATOM   6319 H H    . ASP   B 1 145 ? 29.704 -26.992 -5.432  1.00 17.35 ?  145 ASP   B H    1 
ATOM   6320 H HA   . ASP   B 1 145 ? 27.367 -26.084 -6.361  1.00 18.79 ?  145 ASP   B HA   1 
ATOM   6321 H HB2  . ASP   B 1 145 ? 28.055 -27.123 -3.827  1.00 20.40 ?  145 ASP   B HB2  1 
ATOM   6322 H HB3  . ASP   B 1 145 ? 26.594 -26.593 -4.157  1.00 20.40 ?  145 ASP   B HB3  1 
ATOM   6323 N N    . THR   B 1 146 ? 29.179 -24.046 -4.970  1.00 13.06 ?  146 THR   B N    1 
ATOM   6324 C CA   . THR   B 1 146 ? 29.325 -22.722 -4.369  1.00 13.02 ?  146 THR   B CA   1 
ATOM   6325 C C    . THR   B 1 146 ? 29.962 -21.700 -5.294  1.00 12.76 ?  146 THR   B C    1 
ATOM   6326 O O    . THR   B 1 146 ? 29.507 -20.541 -5.354  1.00 12.90 ?  146 THR   B O    1 
ATOM   6327 C CB   . THR   B 1 146 ? 30.149 -22.827 -3.081  1.00 13.41 ?  146 THR   B CB   1 
ATOM   6328 O OG1  . THR   B 1 146 ? 29.572 -23.817 -2.218  1.00 13.43 ?  146 THR   B OG1  1 
ATOM   6329 C CG2  . THR   B 1 146 ? 30.222 -21.478 -2.370  1.00 13.52 ?  146 THR   B CG2  1 
ATOM   6330 H H    . THR   B 1 146 ? 29.928 -24.368 -5.259  1.00 15.68 ?  146 THR   B H    1 
ATOM   6331 H HA   . THR   B 1 146 ? 28.451 -22.386 -4.129  1.00 15.62 ?  146 THR   B HA   1 
ATOM   6332 H HB   . THR   B 1 146 ? 31.060 -23.084 -3.305  1.00 16.09 ?  146 THR   B HB   1 
ATOM   6333 H HG1  . THR   B 1 146 ? 29.611 -24.574 -2.589  1.00 16.11 ?  146 THR   B HG1  1 
ATOM   6334 H HG21 . THR   B 1 146 ? 30.567 -21.594 -1.470  1.00 16.23 ?  146 THR   B HG21 1 
ATOM   6335 H HG22 . THR   B 1 146 ? 30.813 -20.875 -2.853  1.00 16.23 ?  146 THR   B HG22 1 
ATOM   6336 H HG23 . THR   B 1 146 ? 29.340 -21.081 -2.320  1.00 16.23 ?  146 THR   B HG23 1 
ATOM   6337 N N    . VAL   B 1 147 ? 31.025 -22.081 -5.987  1.00 12.52 ?  147 VAL   B N    1 
ATOM   6338 C CA   . VAL   B 1 147 ? 31.748 -21.141 -6.831  1.00 12.00 ?  147 VAL   B CA   1 
ATOM   6339 C C    . VAL   B 1 147 ? 31.013 -21.008 -8.150  1.00 12.62 ?  147 VAL   B C    1 
ATOM   6340 O O    . VAL   B 1 147 ? 30.638 -22.012 -8.775  1.00 13.44 ?  147 VAL   B O    1 
ATOM   6341 C CB   . VAL   B 1 147 ? 33.201 -21.596 -7.036  1.00 11.92 ?  147 VAL   B CB   1 
ATOM   6342 C CG1  . VAL   B 1 147 ? 33.960 -20.576 -7.874  1.00 12.29 ?  147 VAL   B CG1  1 
ATOM   6343 C CG2  . VAL   B 1 147 ? 33.881 -21.808 -5.691  1.00 12.18 ?  147 VAL   B CG2  1 
ATOM   6344 H H    . VAL   B 1 147 ? 31.351 -22.878 -5.991  1.00 15.02 ?  147 VAL   B H    1 
ATOM   6345 H HA   . VAL   B 1 147 ? 31.765 -20.269 -6.399  1.00 14.41 ?  147 VAL   B HA   1 
ATOM   6346 H HB   . VAL   B 1 147 ? 33.205 -22.437 -7.515  1.00 14.31 ?  147 VAL   B HB   1 
ATOM   6347 H HG11 . VAL   B 1 147 ? 34.904 -20.796 -7.862  1.00 14.75 ?  147 VAL   B HG11 1 
ATOM   6348 H HG12 . VAL   B 1 147 ? 33.628 -20.601 -8.786  1.00 14.75 ?  147 VAL   B HG12 1 
ATOM   6349 H HG13 . VAL   B 1 147 ? 33.823 -19.691 -7.497  1.00 14.75 ?  147 VAL   B HG13 1 
ATOM   6350 H HG21 . VAL   B 1 147 ? 34.823 -21.997 -5.839  1.00 14.62 ?  147 VAL   B HG21 1 
ATOM   6351 H HG22 . VAL   B 1 147 ? 33.786 -21.005 -5.157  1.00 14.62 ?  147 VAL   B HG22 1 
ATOM   6352 H HG23 . VAL   B 1 147 ? 33.463 -22.558 -5.240  1.00 14.62 ?  147 VAL   B HG23 1 
ATOM   6353 N N    . ARG   B 1 148 ? 30.804 -19.756 -8.572  1.00 12.45 ?  148 ARG   B N    1 
ATOM   6354 C CA   . ARG   B 1 148 ? 30.185 -19.442 -9.848  1.00 12.78 ?  148 ARG   B CA   1 
ATOM   6355 C C    . ARG   B 1 148 ? 31.143 -18.773 -10.822 1.00 12.80 ?  148 ARG   B C    1 
ATOM   6356 O O    . ARG   B 1 148 ? 30.852 -18.751 -12.022 1.00 14.31 ?  148 ARG   B O    1 
ATOM   6357 C CB   . ARG   B 1 148 ? 28.946 -18.556 -9.634  1.00 13.46 ?  148 ARG   B CB   1 
ATOM   6358 C CG   . ARG   B 1 148 ? 27.878 -19.261 -8.807  1.00 13.79 ?  148 ARG   B CG   1 
ATOM   6359 C CD   . ARG   B 1 148 ? 26.665 -18.380 -8.505  1.00 15.16 ?  148 ARG   B CD   1 
ATOM   6360 N NE   . ARG   B 1 148 ? 27.045 -17.168 -7.786  1.00 15.14 ?  148 ARG   B NE   1 
ATOM   6361 C CZ   . ARG   B 1 148 ? 27.359 -17.126 -6.497  1.00 14.29 ?  148 ARG   B CZ   1 
ATOM   6362 N NH1  . ARG   B 1 148 ? 27.305 -18.210 -5.734  1.00 14.48 ?  148 ARG   B NH1  1 
ATOM   6363 N NH2  . ARG   B 1 148 ? 27.746 -15.971 -5.964  1.00 14.26 ?  148 ARG   B NH2  1 
ATOM   6364 H H    . ARG   B 1 148 ? 31.017 -19.053 -8.116  1.00 14.94 ?  148 ARG   B H    1 
ATOM   6365 H HA   . ARG   B 1 148 ? 29.883 -20.266 -10.254 1.00 15.34 ?  148 ARG   B HA   1 
ATOM   6366 H HB2  . ARG   B 1 148 ? 29.206 -17.748 -9.164  1.00 16.15 ?  148 ARG   B HB2  1 
ATOM   6367 H HB3  . ARG   B 1 148 ? 28.560 -18.333 -10.495 1.00 16.15 ?  148 ARG   B HB3  1 
ATOM   6368 H HG2  . ARG   B 1 148 ? 27.568 -20.042 -9.296  1.00 16.55 ?  148 ARG   B HG2  1 
ATOM   6369 H HG3  . ARG   B 1 148 ? 28.266 -19.538 -7.961  1.00 16.55 ?  148 ARG   B HG3  1 
ATOM   6370 H HD2  . ARG   B 1 148 ? 26.246 -18.120 -9.338  1.00 18.19 ?  148 ARG   B HD2  1 
ATOM   6371 H HD3  . ARG   B 1 148 ? 26.039 -18.878 -7.955  1.00 18.19 ?  148 ARG   B HD3  1 
ATOM   6372 H HE   . ARG   B 1 148 ? 27.068 -16.432 -8.227  1.00 18.17 ?  148 ARG   B HE   1 
ATOM   6373 H HH11 . ARG   B 1 148 ? 27.058 -18.964 -6.065  1.00 17.37 ?  148 ARG   B HH11 1 
ATOM   6374 H HH12 . ARG   B 1 148 ? 27.511 -18.159 -4.898  1.00 17.37 ?  148 ARG   B HH12 1 
ATOM   6375 H HH21 . ARG   B 1 148 ? 27.783 -15.264 -6.452  1.00 17.12 ?  148 ARG   B HH21 1 
ATOM   6376 H HH22 . ARG   B 1 148 ? 27.949 -15.927 -5.130  1.00 17.12 ?  148 ARG   B HH22 1 
ATOM   6377 N N    . THR   B 1 149 ? 32.256 -18.226 -10.336 1.00 12.61 ?  149 THR   B N    1 
ATOM   6378 C CA   . THR   B 1 149 ? 33.293 -17.670 -11.189 1.00 12.67 ?  149 THR   B CA   1 
ATOM   6379 C C    . THR   B 1 149 ? 34.171 -18.810 -11.709 1.00 12.44 ?  149 THR   B C    1 
ATOM   6380 O O    . THR   B 1 149 ? 33.971 -19.983 -11.381 1.00 13.00 ?  149 THR   B O    1 
ATOM   6381 C CB   . THR   B 1 149 ? 34.062 -16.615 -10.402 1.00 12.93 ?  149 THR   B CB   1 
ATOM   6382 O OG1  . THR   B 1 149 ? 34.518 -17.210 -9.187  1.00 12.84 ?  149 THR   B OG1  1 
ATOM   6383 C CG2  . THR   B 1 149 ? 33.166 -15.418 -10.090 1.00 13.56 ?  149 THR   B CG2  1 
ATOM   6384 H H    . THR   B 1 149 ? 32.423 -18.157 -9.495  1.00 15.14 ?  149 THR   B H    1 
ATOM   6385 H HA   . THR   B 1 149 ? 32.875 -17.233 -11.950 1.00 15.20 ?  149 THR   B HA   1 
ATOM   6386 H HB   . THR   B 1 149 ? 34.815 -16.312 -10.921 1.00 15.52 ?  149 THR   B HB   1 
ATOM   6387 H HG1  . THR   B 1 149 ? 34.944 -16.641 -8.729  1.00 15.41 ?  149 THR   B HG1  1 
ATOM   6388 H HG21 . THR   B 1 149 ? 33.670 -14.743 -9.607  1.00 16.27 ?  149 THR   B HG21 1 
ATOM   6389 H HG22 . THR   B 1 149 ? 32.827 -15.029 -10.911 1.00 16.27 ?  149 THR   B HG22 1 
ATOM   6390 H HG23 . THR   B 1 149 ? 32.412 -15.695 -9.540  1.00 16.27 ?  149 THR   B HG23 1 
ATOM   6391 N N    . ASN   B 1 150 ? 35.135 -18.485 -12.557 1.00 12.48 ?  150 ASN   B N    1 
ATOM   6392 C CA   . ASN   B 1 150 ? 35.906 -19.506 -13.253 1.00 12.81 ?  150 ASN   B CA   1 
ATOM   6393 C C    . ASN   B 1 150 ? 37.066 -19.957 -12.378 1.00 12.46 ?  150 ASN   B C    1 
ATOM   6394 O O    . ASN   B 1 150 ? 38.001 -19.195 -12.132 1.00 12.95 ?  150 ASN   B O    1 
ATOM   6395 C CB   . ASN   B 1 150 ? 36.380 -18.973 -14.595 1.00 14.82 ?  150 ASN   B CB   1 
ATOM   6396 C CG   . ASN   B 1 150 ? 35.236 -18.759 -15.548 1.00 17.89 ?  150 ASN   B CG   1 
ATOM   6397 O OD1  . ASN   B 1 150 ? 34.332 -19.585 -15.623 1.00 18.95 ?  150 ASN   B OD1  1 
ATOM   6398 N ND2  . ASN   B 1 150 ? 35.239 -17.638 -16.249 1.00 20.41 ?  150 ASN   B ND2  1 
ATOM   6399 H H    . ASN   B 1 150 ? 35.360 -17.676 -12.745 1.00 14.98 ?  150 ASN   B H    1 
ATOM   6400 H HA   . ASN   B 1 150 ? 35.328 -20.275 -13.416 1.00 15.38 ?  150 ASN   B HA   1 
ATOM   6401 H HB2  . ASN   B 1 150 ? 36.820 -18.120 -14.455 1.00 17.78 ?  150 ASN   B HB2  1 
ATOM   6402 H HB3  . ASN   B 1 150 ? 36.990 -19.610 -14.988 1.00 17.78 ?  150 ASN   B HB3  1 
ATOM   6403 H HD21 . ASN   B 1 150 ? 34.604 -17.473 -16.809 1.00 24.49 ?  150 ASN   B HD21 1 
ATOM   6404 H HD22 . ASN   B 1 150 ? 35.884 -17.075 -16.159 1.00 24.49 ?  150 ASN   B HD22 1 
ATOM   6405 N N    . VAL   B 1 151 ? 37.013 -21.198 -11.908 1.00 12.01 ?  151 VAL   B N    1 
ATOM   6406 C CA   . VAL   B 1 151 ? 38.029 -21.735 -11.017 1.00 11.94 ?  151 VAL   B CA   1 
ATOM   6407 C C    . VAL   B 1 151 ? 38.726 -22.910 -11.691 1.00 11.80 ?  151 VAL   B C    1 
ATOM   6408 O O    . VAL   B 1 151 ? 38.077 -23.843 -12.193 1.00 13.39 ?  151 VAL   B O    1 
ATOM   6409 C CB   . VAL   B 1 151 ? 37.474 -22.070 -9.618  1.00 13.50 ?  151 VAL   B CB   1 
ATOM   6410 C CG1  . VAL   B 1 151 ? 36.310 -23.054 -9.679  1.00 14.83 ?  151 VAL   B CG1  1 
ATOM   6411 C CG2  . VAL   B 1 151 ? 38.592 -22.576 -8.715  1.00 13.66 ?  151 VAL   B CG2  1 
ATOM   6412 H H    . VAL   B 1 151 ? 36.384 -21.762 -12.094 1.00 14.41 ?  151 VAL   B H    1 
ATOM   6413 H HA   . VAL   B 1 151 ? 38.701 -21.045 -10.888 1.00 14.33 ?  151 VAL   B HA   1 
ATOM   6414 H HB   . VAL   B 1 151 ? 37.143 -21.248 -9.219  1.00 16.20 ?  151 VAL   B HB   1 
ATOM   6415 H HG11 . VAL   B 1 151 ? 36.004 -23.237 -8.775  1.00 17.79 ?  151 VAL   B HG11 1 
ATOM   6416 H HG12 . VAL   B 1 151 ? 35.590 -22.658 -10.195 1.00 17.79 ?  151 VAL   B HG12 1 
ATOM   6417 H HG13 . VAL   B 1 151 ? 36.609 -23.873 -10.099 1.00 17.79 ?  151 VAL   B HG13 1 
ATOM   6418 H HG21 . VAL   B 1 151 ? 38.256 -22.645 -7.804  1.00 16.39 ?  151 VAL   B HG21 1 
ATOM   6419 H HG22 . VAL   B 1 151 ? 38.882 -23.449 -9.022  1.00 16.39 ?  151 VAL   B HG22 1 
ATOM   6420 H HG23 . VAL   B 1 151 ? 39.335 -21.952 -8.741  1.00 16.39 ?  151 VAL   B HG23 1 
ATOM   6421 N N    . TYR   B 1 152 ? 40.057 -22.828 -11.712 1.00 11.63 ?  152 TYR   B N    1 
ATOM   6422 C CA   . TYR   B 1 152 ? 40.959 -23.812 -12.291 1.00 11.94 ?  152 TYR   B CA   1 
ATOM   6423 C C    . TYR   B 1 152 ? 41.681 -24.490 -11.132 1.00 10.92 ?  152 TYR   B C    1 
ATOM   6424 O O    . TYR   B 1 152 ? 42.534 -23.874 -10.481 1.00 11.70 ?  152 TYR   B O    1 
ATOM   6425 C CB   . TYR   B 1 152 ? 41.934 -23.122 -13.251 1.00 12.42 ?  152 TYR   B CB   1 
ATOM   6426 C CG   . TYR   B 1 152 ? 41.255 -22.660 -14.512 1.00 13.14 ?  152 TYR   B CG   1 
ATOM   6427 C CD1  . TYR   B 1 152 ? 40.612 -21.430 -14.573 1.00 13.56 ?  152 TYR   B CD1  1 
ATOM   6428 C CD2  . TYR   B 1 152 ? 41.234 -23.463 -15.638 1.00 14.72 ?  152 TYR   B CD2  1 
ATOM   6429 C CE1  . TYR   B 1 152 ? 39.968 -21.014 -15.723 1.00 15.14 ?  152 TYR   B CE1  1 
ATOM   6430 C CE2  . TYR   B 1 152 ? 40.589 -23.063 -16.792 1.00 15.32 ?  152 TYR   B CE2  1 
ATOM   6431 C CZ   . TYR   B 1 152 ? 39.964 -21.830 -16.833 1.00 15.50 ?  152 TYR   B CZ   1 
ATOM   6432 O OH   . TYR   B 1 152 ? 39.327 -21.427 -17.979 1.00 18.49 ?  152 TYR   B OH   1 
ATOM   6433 H H    . TYR   B 1 152 ? 40.488 -22.160 -11.371 1.00 13.95 ?  152 TYR   B H    1 
ATOM   6434 H HA   . TYR   B 1 152 ? 40.446 -24.478 -12.781 1.00 14.33 ?  152 TYR   B HA   1 
ATOM   6435 H HB2  . TYR   B 1 152 ? 42.314 -22.348 -12.808 1.00 14.90 ?  152 TYR   B HB2  1 
ATOM   6436 H HB3  . TYR   B 1 152 ? 42.635 -23.746 -13.492 1.00 14.90 ?  152 TYR   B HB3  1 
ATOM   6437 H HD1  . TYR   B 1 152 ? 40.612 -20.878 -13.824 1.00 16.27 ?  152 TYR   B HD1  1 
ATOM   6438 H HD2  . TYR   B 1 152 ? 41.649 -24.300 -15.613 1.00 17.66 ?  152 TYR   B HD2  1 
ATOM   6439 H HE1  . TYR   B 1 152 ? 39.543 -20.186 -15.752 1.00 18.16 ?  152 TYR   B HE1  1 
ATOM   6440 H HE2  . TYR   B 1 152 ? 40.587 -23.619 -17.539 1.00 18.38 ?  152 TYR   B HE2  1 
ATOM   6441 H HH   . TYR   B 1 152 ? 39.400 -22.020 -18.569 1.00 22.19 ?  152 TYR   B HH   1 
ATOM   6442 N N    . LEU   B 1 153 ? 41.304 -25.743 -10.859 1.00 11.41 ?  153 LEU   B N    1 
ATOM   6443 C CA   . LEU   B 1 153 ? 41.814 -26.490 -9.721  1.00 11.42 ?  153 LEU   B CA   1 
ATOM   6444 C C    . LEU   B 1 153 ? 43.043 -27.295 -10.116 1.00 11.85 ?  153 LEU   B C    1 
ATOM   6445 O O    . LEU   B 1 153 ? 43.022 -28.019 -11.116 1.00 12.80 ?  153 LEU   B O    1 
ATOM   6446 C CB   . LEU   B 1 153 ? 40.737 -27.441 -9.201  1.00 11.55 ?  153 LEU   B CB   1 
ATOM   6447 C CG   . LEU   B 1 153 ? 39.484 -26.793 -8.619  1.00 12.51 ?  153 LEU   B CG   1 
ATOM   6448 C CD1  . LEU   B 1 153 ? 38.404 -27.843 -8.462  1.00 13.41 ?  153 LEU   B CD1  1 
ATOM   6449 C CD2  . LEU   B 1 153 ? 39.804 -26.131 -7.286  1.00 13.33 ?  153 LEU   B CD2  1 
ATOM   6450 H H    . LEU   B 1 153 ? 40.742 -26.194 -11.339 1.00 13.69 ?  153 LEU   B H    1 
ATOM   6451 H HA   . LEU   B 1 153 ? 42.049 -25.875 -9.014  1.00 13.71 ?  153 LEU   B HA   1 
ATOM   6452 H HB2  . LEU   B 1 153 ? 40.453 -28.011 -9.933  1.00 13.86 ?  153 LEU   B HB2  1 
ATOM   6453 H HB3  . LEU   B 1 153 ? 41.128 -27.991 -8.501  1.00 13.86 ?  153 LEU   B HB3  1 
ATOM   6454 H HG   . LEU   B 1 153 ? 39.162 -26.107 -9.227  1.00 15.02 ?  153 LEU   B HG   1 
ATOM   6455 H HD11 . LEU   B 1 153 ? 37.604 -27.418 -8.111  1.00 16.09 ?  153 LEU   B HD11 1 
ATOM   6456 H HD12 . LEU   B 1 153 ? 38.220 -28.234 -9.326  1.00 16.09 ?  153 LEU   B HD12 1 
ATOM   6457 H HD13 . LEU   B 1 153 ? 38.716 -28.521 -7.845  1.00 16.09 ?  153 LEU   B HD13 1 
ATOM   6458 H HD21 . LEU   B 1 153 ? 38.990 -25.768 -6.908  1.00 16.00 ?  153 LEU   B HD21 1 
ATOM   6459 H HD22 . LEU   B 1 153 ? 40.176 -26.802 -6.685  1.00 16.00 ?  153 LEU   B HD22 1 
ATOM   6460 H HD23 . LEU   B 1 153 ? 40.452 -25.425 -7.428  1.00 16.00 ?  153 LEU   B HD23 1 
ATOM   6461 N N    . ALA   B 1 154 ? 44.097 -27.189 -9.309  1.00 11.88 ?  154 ALA   B N    1 
ATOM   6462 C CA   . ALA   B 1 154 ? 45.326 -27.950 -9.495  1.00 12.58 ?  154 ALA   B CA   1 
ATOM   6463 C C    . ALA   B 1 154 ? 45.401 -29.027 -8.418  1.00 13.38 ?  154 ALA   B C    1 
ATOM   6464 O O    . ALA   B 1 154 ? 45.345 -28.724 -7.218  1.00 14.84 ?  154 ALA   B O    1 
ATOM   6465 C CB   . ALA   B 1 154 ? 46.552 -27.044 -9.440  1.00 13.98 ?  154 ALA   B CB   1 
ATOM   6466 H H    . ALA   B 1 154 ? 44.114 -26.663 -8.621  1.00 14.26 ?  154 ALA   B H    1 
ATOM   6467 H HA   . ALA   B 1 154 ? 45.302 -28.380 -10.362 1.00 15.09 ?  154 ALA   B HA   1 
ATOM   6468 H HB1  . ALA   B 1 154 ? 47.347 -27.583 -9.570  1.00 16.78 ?  154 ALA   B HB1  1 
ATOM   6469 H HB2  . ALA   B 1 154 ? 46.487 -26.376 -10.142 1.00 16.78 ?  154 ALA   B HB2  1 
ATOM   6470 H HB3  . ALA   B 1 154 ? 46.587 -26.607 -8.574  1.00 16.78 ?  154 ALA   B HB3  1 
ATOM   6471 N N    . VAL   B 1 155 ? 45.505 -30.280 -8.846  1.00 12.87 ?  155 VAL   B N    1 
ATOM   6472 C CA   . VAL   B 1 155 ? 45.605 -31.422 -7.946  1.00 13.54 ?  155 VAL   B CA   1 
ATOM   6473 C C    . VAL   B 1 155 ? 46.940 -32.102 -8.226  1.00 13.55 ?  155 VAL   B C    1 
ATOM   6474 O O    . VAL   B 1 155 ? 47.166 -32.603 -9.334  1.00 15.13 ?  155 VAL   B O    1 
ATOM   6475 C CB   . VAL   B 1 155 ? 44.447 -32.417 -8.140  1.00 15.03 ?  155 VAL   B CB   1 
ATOM   6476 C CG1  . VAL   B 1 155 ? 44.625 -33.613 -7.211  1.00 15.31 ?  155 VAL   B CG1  1 
ATOM   6477 C CG2  . VAL   B 1 155 ? 43.099 -31.725 -7.919  1.00 15.90 ?  155 VAL   B CG2  1 
ATOM   6478 H H    . VAL   B 1 155 ? 45.531 -30.500 -9.679  1.00 15.45 ?  155 VAL   B H    1 
ATOM   6479 H HA   . VAL   B 1 155 ? 45.598 -31.117 -7.027  1.00 16.24 ?  155 VAL   B HA   1 
ATOM   6480 H HB   . VAL   B 1 155 ? 44.466 -32.745 -9.053  1.00 18.03 ?  155 VAL   B HB   1 
ATOM   6481 H HG11 . VAL   B 1 155 ? 43.796 -34.115 -7.179  1.00 18.38 ?  155 VAL   B HG11 1 
ATOM   6482 H HG12 . VAL   B 1 155 ? 45.339 -34.178 -7.548  1.00 18.38 ?  155 VAL   B HG12 1 
ATOM   6483 H HG13 . VAL   B 1 155 ? 44.849 -33.292 -6.322  1.00 18.38 ?  155 VAL   B HG13 1 
ATOM   6484 H HG21 . VAL   B 1 155 ? 42.388 -32.382 -8.005  1.00 19.08 ?  155 VAL   B HG21 1 
ATOM   6485 H HG22 . VAL   B 1 155 ? 43.084 -31.338 -7.030  1.00 19.08 ?  155 VAL   B HG22 1 
ATOM   6486 H HG23 . VAL   B 1 155 ? 42.985 -31.029 -8.585  1.00 19.08 ?  155 VAL   B HG23 1 
ATOM   6487 N N    . PHE   B 1 156 ? 47.813 -32.139 -7.218  1.00 13.91 ?  156 PHE   B N    1 
ATOM   6488 C CA   . PHE   B 1 156 ? 49.188 -32.600 -7.425  1.00 14.70 ?  156 PHE   B CA   1 
ATOM   6489 C C    . PHE   B 1 156 ? 49.279 -34.100 -7.706  1.00 16.33 ?  156 PHE   B C    1 
ATOM   6490 O O    . PHE   B 1 156 ? 49.994 -34.528 -8.621  1.00 18.06 ?  156 PHE   B O    1 
ATOM   6491 C CB   . PHE   B 1 156 ? 50.022 -32.238 -6.201  1.00 14.57 ?  156 PHE   B CB   1 
ATOM   6492 C CG   . PHE   B 1 156 ? 51.454 -32.704 -6.272  1.00 14.90 ?  156 PHE   B CG   1 
ATOM   6493 C CD1  . PHE   B 1 156 ? 52.321 -32.174 -7.208  1.00 16.62 ?  156 PHE   B CD1  1 
ATOM   6494 C CD2  . PHE   B 1 156 ? 51.930 -33.656 -5.389  1.00 15.72 ?  156 PHE   B CD2  1 
ATOM   6495 C CE1  . PHE   B 1 156 ? 53.650 -32.594 -7.268  1.00 17.64 ?  156 PHE   B CE1  1 
ATOM   6496 C CE2  . PHE   B 1 156 ? 53.250 -34.076 -5.443  1.00 17.34 ?  156 PHE   B CE2  1 
ATOM   6497 C CZ   . PHE   B 1 156 ? 54.102 -33.546 -6.385  1.00 17.68 ?  156 PHE   B CZ   1 
ATOM   6498 H H    . PHE   B 1 156 ? 47.631 -31.909 -6.407  1.00 16.70 ?  156 PHE   B H    1 
ATOM   6499 H HA   . PHE   B 1 156 ? 49.558 -32.132 -8.183  1.00 17.63 ?  156 PHE   B HA   1 
ATOM   6500 H HB2  . PHE   B 1 156 ? 50.033 -31.274 -6.104  1.00 17.49 ?  156 PHE   B HB2  1 
ATOM   6501 H HB3  . PHE   B 1 156 ? 49.624 -32.643 -5.414  1.00 17.49 ?  156 PHE   B HB3  1 
ATOM   6502 H HD1  . PHE   B 1 156 ? 52.018 -31.525 -7.807  1.00 19.95 ?  156 PHE   B HD1  1 
ATOM   6503 H HD2  . PHE   B 1 156 ? 51.357 -34.023 -4.754  1.00 18.87 ?  156 PHE   B HD2  1 
ATOM   6504 H HE1  . PHE   B 1 156 ? 54.229 -32.231 -7.905  1.00 21.17 ?  156 PHE   B HE1  1 
ATOM   6505 H HE2  . PHE   B 1 156 ? 53.555 -34.726 -4.850  1.00 20.81 ?  156 PHE   B HE2  1 
ATOM   6506 H HZ   . PHE   B 1 156 ? 54.988 -33.830 -6.425  1.00 21.22 ?  156 PHE   B HZ   1 
ATOM   6507 N N    . ASP   B 1 157 ? 48.618 -34.916 -6.898  1.00 16.83 ?  157 ASP   B N    1 
ATOM   6508 C CA   . ASP   B 1 157 ? 48.761 -36.366 -6.998  1.00 17.62 ?  157 ASP   B CA   1 
ATOM   6509 C C    . ASP   B 1 157 ? 47.843 -36.914 -8.084  1.00 18.19 ?  157 ASP   B C    1 
ATOM   6510 O O    . ASP   B 1 157 ? 46.619 -36.801 -7.974  1.00 17.27 ?  157 ASP   B O    1 
ATOM   6511 C CB   . ASP   B 1 157 ? 48.396 -36.981 -5.654  1.00 19.28 ?  157 ASP   B CB   1 
ATOM   6512 C CG   . ASP   B 1 157 ? 48.548 -38.493 -5.633  1.00 21.69 ?  157 ASP   B CG   1 
ATOM   6513 O OD1  . ASP   B 1 157 ? 48.911 -39.101 -6.669  1.00 22.59 ?  157 ASP   B OD1  1 
ATOM   6514 O OD2  . ASP   B 1 157 ? 48.309 -39.077 -4.558  1.00 24.13 -1 157 ASP   B OD2  1 
ATOM   6515 H H    . ASP   B 1 157 ? 48.081 -34.662 -6.284  1.00 20.19 ?  157 ASP   B H    1 
ATOM   6516 H HA   . ASP   B 1 157 ? 49.680 -36.598 -7.218  1.00 21.14 ?  157 ASP   B HA   1 
ATOM   6517 H HB2  . ASP   B 1 157 ? 48.973 -36.599 -4.975  1.00 23.14 ?  157 ASP   B HB2  1 
ATOM   6518 H HB3  . ASP   B 1 157 ? 47.470 -36.765 -5.458  1.00 23.14 ?  157 ASP   B HB3  1 
ATOM   6519 N N    . LYS   B 1 158 ? 48.431 -37.543 -9.110  1.00 19.07 ?  158 LYS   B N    1 
ATOM   6520 C CA   . LYS   B 1 158 ? 47.645 -38.154 -10.187 1.00 20.70 ?  158 LYS   B CA   1 
ATOM   6521 C C    . LYS   B 1 158 ? 46.579 -39.113 -9.652  1.00 20.83 ?  158 LYS   B C    1 
ATOM   6522 O O    . LYS   B 1 158 ? 45.474 -39.198 -10.200 1.00 20.83 ?  158 LYS   B O    1 
ATOM   6523 C CB   . LYS   B 1 158 ? 48.589 -38.875 -11.161 1.00 22.26 ?  158 LYS   B CB   1 
ATOM   6524 C CG   . LYS   B 1 158 ? 47.901 -39.763 -12.190 1.00 24.56 ?  158 LYS   B CG   1 
ATOM   6525 C CD   . LYS   B 1 158 ? 47.044 -38.961 -13.147 1.00 26.64 ?  158 LYS   B CD   1 
ATOM   6526 C CE   . LYS   B 1 158 ? 46.430 -39.863 -14.205 1.00 28.38 ?  158 LYS   B CE   1 
ATOM   6527 N NZ   . LYS   B 1 158 ? 45.374 -39.166 -14.989 1.00 28.41 ?  158 LYS   B NZ   1 
ATOM   6528 H H    . LYS   B 1 158 ? 49.286 -37.637 -9.204  1.00 22.88 ?  158 LYS   B H    1 
ATOM   6529 H HA   . LYS   B 1 158 ? 47.202 -37.449 -10.689 1.00 24.84 ?  158 LYS   B HA   1 
ATOM   6530 H HB2  . LYS   B 1 158 ? 49.106 -38.212 -11.655 1.00 26.72 ?  158 LYS   B HB2  1 
ATOM   6531 H HB3  . LYS   B 1 158 ? 49.197 -39.436 -10.653 1.00 26.72 ?  158 LYS   B HB3  1 
ATOM   6532 H HG2  . LYS   B 1 158 ? 48.579 -40.221 -12.713 1.00 29.48 ?  158 LYS   B HG2  1 
ATOM   6533 H HG3  . LYS   B 1 158 ? 47.340 -40.416 -11.743 1.00 29.48 ?  158 LYS   B HG3  1 
ATOM   6534 H HD2  . LYS   B 1 158 ? 46.325 -38.532 -12.657 1.00 31.97 ?  158 LYS   B HD2  1 
ATOM   6535 H HD3  . LYS   B 1 158 ? 47.592 -38.297 -13.594 1.00 31.97 ?  158 LYS   B HD3  1 
ATOM   6536 H HE2  . LYS   B 1 158 ? 47.122 -40.151 -14.820 1.00 34.05 ?  158 LYS   B HE2  1 
ATOM   6537 H HE3  . LYS   B 1 158 ? 46.027 -40.633 -13.774 1.00 34.05 ?  158 LYS   B HE3  1 
ATOM   6538 H HZ1  . LYS   B 1 158 ? 45.033 -39.716 -15.599 1.00 34.09 ?  158 LYS   B HZ1  1 
ATOM   6539 H HZ2  . LYS   B 1 158 ? 44.722 -38.894 -14.447 1.00 34.09 ?  158 LYS   B HZ2  1 
ATOM   6540 H HZ3  . LYS   B 1 158 ? 45.721 -38.457 -15.401 1.00 34.09 ?  158 LYS   B HZ3  1 
ATOM   6541 N N    . ASN   B 1 159 ? 46.898 -39.871 -8.602  1.00 20.77 ?  159 ASN   B N    1 
ATOM   6542 C CA   . ASN   B 1 159 ? 45.937 -40.846 -8.093  1.00 21.31 ?  159 ASN   B CA   1 
ATOM   6543 C C    . ASN   B 1 159 ? 44.745 -40.164 -7.419  1.00 19.91 ?  159 ASN   B C    1 
ATOM   6544 O O    . ASN   B 1 159 ? 43.606 -40.636 -7.531  1.00 20.01 ?  159 ASN   B O    1 
ATOM   6545 C CB   . ASN   B 1 159 ? 46.636 -41.814 -7.148  1.00 23.13 ?  159 ASN   B CB   1 
ATOM   6546 C CG   . ASN   B 1 159 ? 47.660 -42.665 -7.858  1.00 26.52 ?  159 ASN   B CG   1 
ATOM   6547 O OD1  . ASN   B 1 159 ? 47.398 -43.187 -8.951  1.00 26.94 ?  159 ASN   B OD1  1 
ATOM   6548 N ND2  . ASN   B 1 159 ? 48.832 -42.822 -7.244  1.00 25.61 ?  159 ASN   B ND2  1 
ATOM   6549 H H    . ASN   B 1 159 ? 47.642 -39.824 -8.183  1.00 24.93 ?  159 ASN   B H    1 
ATOM   6550 H HA   . ASN   B 1 159 ? 45.600 -41.353 -8.849  1.00 25.58 ?  159 ASN   B HA   1 
ATOM   6551 H HB2  . ASN   B 1 159 ? 47.088 -41.310 -6.457  1.00 27.76 ?  159 ASN   B HB2  1 
ATOM   6552 H HB3  . ASN   B 1 159 ? 45.974 -42.402 -6.763  1.00 27.76 ?  159 ASN   B HB3  1 
ATOM   6553 H HD21 . ASN   B 1 159 ? 49.457 -43.297 -7.606  1.00 30.73 ?  159 ASN   B HD21 1 
ATOM   6554 H HD22 . ASN   B 1 159 ? 48.974 -42.453 -6.478  1.00 30.73 ?  159 ASN   B HD22 1 
ATOM   6555 N N    . LEU   B 1 160 ? 44.972 -39.047 -6.722  1.00 18.90 ?  160 LEU   B N    1 
ATOM   6556 C CA   . LEU   B 1 160 ? 43.845 -38.299 -6.175  1.00 17.97 ?  160 LEU   B CA   1 
ATOM   6557 C C    . LEU   B 1 160 ? 43.050 -37.625 -7.284  1.00 16.99 ?  160 LEU   B C    1 
ATOM   6558 O O    . LEU   B 1 160 ? 41.810 -37.611 -7.250  1.00 16.40 ?  160 LEU   B O    1 
ATOM   6559 C CB   . LEU   B 1 160 ? 44.326 -37.268 -5.157  1.00 17.52 ?  160 LEU   B CB   1 
ATOM   6560 C CG   . LEU   B 1 160 ? 43.208 -36.354 -4.645  1.00 16.94 ?  160 LEU   B CG   1 
ATOM   6561 C CD1  . LEU   B 1 160 ? 42.085 -37.167 -4.015  1.00 18.07 ?  160 LEU   B CD1  1 
ATOM   6562 C CD2  . LEU   B 1 160 ? 43.765 -35.335 -3.660  1.00 17.10 ?  160 LEU   B CD2  1 
ATOM   6563 H H    . LEU   B 1 160 ? 45.750 -38.713 -6.564  1.00 22.68 ?  160 LEU   B H    1 
ATOM   6564 H HA   . LEU   B 1 160 ? 43.257 -38.922 -5.727  1.00 21.57 ?  160 LEU   B HA   1 
ATOM   6565 H HB2  . LEU   B 1 160 ? 44.706 -37.741 -4.397  1.00 21.02 ?  160 LEU   B HB2  1 
ATOM   6566 H HB3  . LEU   B 1 160 ? 45.010 -36.716 -5.572  1.00 21.02 ?  160 LEU   B HB3  1 
ATOM   6567 H HG   . LEU   B 1 160 ? 42.838 -35.864 -5.396  1.00 20.32 ?  160 LEU   B HG   1 
ATOM   6568 H HD11 . LEU   B 1 160 ? 41.467 -36.559 -3.586  1.00 21.68 ?  160 LEU   B HD11 1 
ATOM   6569 H HD12 . LEU   B 1 160 ? 41.628 -37.672 -4.706  1.00 21.68 ?  160 LEU   B HD12 1 
ATOM   6570 H HD13 . LEU   B 1 160 ? 42.465 -37.773 -3.359  1.00 21.68 ?  160 LEU   B HD13 1 
ATOM   6571 H HD21 . LEU   B 1 160 ? 43.046 -34.752 -3.377  1.00 20.52 ?  160 LEU   B HD21 1 
ATOM   6572 H HD22 . LEU   B 1 160 ? 44.137 -35.803 -2.899  1.00 20.52 ?  160 LEU   B HD22 1 
ATOM   6573 H HD23 . LEU   B 1 160 ? 44.458 -34.816 -4.102  1.00 20.52 ?  160 LEU   B HD23 1 
ATOM   6574 N N    . TYR   B 1 161 ? 43.747 -37.067 -8.278  1.00 17.35 ?  161 TYR   B N    1 
ATOM   6575 C CA   . TYR   B 1 161 ? 43.076 -36.499 -9.443  1.00 17.58 ?  161 TYR   B CA   1 
ATOM   6576 C C    . TYR   B 1 161 ? 42.127 -37.518 -10.059 1.00 17.12 ?  161 TYR   B C    1 
ATOM   6577 O O    . TYR   B 1 161 ? 40.956 -37.221 -10.317 1.00 16.95 ?  161 TYR   B O    1 
ATOM   6578 C CB   . TYR   B 1 161 ? 44.121 -36.030 -10.468 1.00 18.05 ?  161 TYR   B CB   1 
ATOM   6579 C CG   . TYR   B 1 161 ? 43.538 -35.559 -11.785 1.00 18.72 ?  161 TYR   B CG   1 
ATOM   6580 C CD1  . TYR   B 1 161 ? 43.153 -34.234 -11.958 1.00 18.64 ?  161 TYR   B CD1  1 
ATOM   6581 C CD2  . TYR   B 1 161 ? 43.362 -36.437 -12.852 1.00 19.26 ?  161 TYR   B CD2  1 
ATOM   6582 C CE1  . TYR   B 1 161 ? 42.617 -33.798 -13.146 1.00 20.11 ?  161 TYR   B CE1  1 
ATOM   6583 C CE2  . TYR   B 1 161 ? 42.825 -36.010 -14.046 1.00 20.54 ?  161 TYR   B CE2  1 
ATOM   6584 C CZ   . TYR   B 1 161 ? 42.459 -34.689 -14.189 1.00 20.50 ?  161 TYR   B CZ   1 
ATOM   6585 O OH   . TYR   B 1 161 ? 41.918 -34.261 -15.375 1.00 22.48 ?  161 TYR   B OH   1 
ATOM   6586 H H    . TYR   B 1 161 ? 44.605 -37.004 -8.303  1.00 20.82 ?  161 TYR   B H    1 
ATOM   6587 H HA   . TYR   B 1 161 ? 42.557 -35.728 -9.173  1.00 21.10 ?  161 TYR   B HA   1 
ATOM   6588 H HB2  . TYR   B 1 161 ? 44.619 -35.288 -10.092 1.00 21.66 ?  161 TYR   B HB2  1 
ATOM   6589 H HB3  . TYR   B 1 161 ? 44.722 -36.763 -10.666 1.00 21.66 ?  161 TYR   B HB3  1 
ATOM   6590 H HD1  . TYR   B 1 161 ? 43.263 -33.628 -11.262 1.00 22.37 ?  161 TYR   B HD1  1 
ATOM   6591 H HD2  . TYR   B 1 161 ? 43.605 -37.329 -12.764 1.00 23.11 ?  161 TYR   B HD2  1 
ATOM   6592 H HE1  . TYR   B 1 161 ? 42.368 -32.903 -13.246 1.00 24.13 ?  161 TYR   B HE1  1 
ATOM   6593 H HE2  . TYR   B 1 161 ? 42.709 -36.606 -14.753 1.00 24.64 ?  161 TYR   B HE2  1 
ATOM   6594 H HH   . TYR   B 1 161 ? 41.872 -34.899 -15.921 1.00 26.97 ?  161 TYR   B HH   1 
ATOM   6595 N N    . ASP   B 1 162 ? 42.615 -38.742 -10.273 1.00 17.46 ?  162 ASP   B N    1 
ATOM   6596 C CA   . ASP   B 1 162 ? 41.782 -39.774 -10.883 1.00 18.08 ?  162 ASP   B CA   1 
ATOM   6597 C C    . ASP   B 1 162 ? 40.575 -40.098 -10.009 1.00 17.79 ?  162 ASP   B C    1 
ATOM   6598 O O    . ASP   B 1 162 ? 39.467 -40.302 -10.518 1.00 18.04 ?  162 ASP   B O    1 
ATOM   6599 C CB   . ASP   B 1 162 ? 42.607 -41.039 -11.135 1.00 19.74 ?  162 ASP   B CB   1 
ATOM   6600 C CG   . ASP   B 1 162 ? 43.617 -40.878 -12.255 1.00 20.92 ?  162 ASP   B CG   1 
ATOM   6601 O OD1  . ASP   B 1 162 ? 43.485 -39.942 -13.069 1.00 20.77 ?  162 ASP   B OD1  1 
ATOM   6602 O OD2  . ASP   B 1 162 ? 44.530 -41.730 -12.336 1.00 22.81 -1 162 ASP   B OD2  1 
ATOM   6603 H H    . ASP   B 1 162 ? 43.414 -38.997 -10.077 1.00 20.95 ?  162 ASP   B H    1 
ATOM   6604 H HA   . ASP   B 1 162 ? 41.456 -39.457 -11.738 1.00 21.70 ?  162 ASP   B HA   1 
ATOM   6605 H HB2  . ASP   B 1 162 ? 43.102 -41.267 -10.336 1.00 23.69 ?  162 ASP   B HB2  1 
ATOM   6606 H HB3  . ASP   B 1 162 ? 42.013 -41.766 -11.380 1.00 23.69 ?  162 ASP   B HB3  1 
ATOM   6607 N N    . LYS   B 1 163 ? 40.774 -40.176 -8.692  1.00 17.01 ?  163 LYS   B N    1 
ATOM   6608 C CA   . LYS   B 1 163 ? 39.658 -40.450 -7.794  1.00 17.85 ?  163 LYS   B CA   1 
ATOM   6609 C C    . LYS   B 1 163 ? 38.616 -39.339 -7.854  1.00 16.46 ?  163 LYS   B C    1 
ATOM   6610 O O    . LYS   B 1 163 ? 37.406 -39.605 -7.851  1.00 17.05 ?  163 LYS   B O    1 
ATOM   6611 C CB   . LYS   B 1 163 ? 40.163 -40.622 -6.364  1.00 20.19 ?  163 LYS   B CB   1 
ATOM   6612 C CG   . LYS   B 1 163 ? 39.093 -41.127 -5.423  1.00 24.62 ?  163 LYS   B CG   1 
ATOM   6613 C CD   . LYS   B 1 163 ? 39.588 -41.283 -3.999  1.00 28.91 ?  163 LYS   B CD   1 
ATOM   6614 C CE   . LYS   B 1 163 ? 38.502 -41.900 -3.127  1.00 33.30 ?  163 LYS   B CE   1 
ATOM   6615 N NZ   . LYS   B 1 163 ? 38.683 -41.591 -1.683  1.00 35.59 ?  163 LYS   B NZ   1 
ATOM   6616 H H    . LYS   B 1 163 ? 41.537 -40.083 -8.307  1.00 20.41 ?  163 LYS   B H    1 
ATOM   6617 H HA   . LYS   B 1 163 ? 39.233 -41.278 -8.063  1.00 21.43 ?  163 LYS   B HA   1 
ATOM   6618 H HB2  . LYS   B 1 163 ? 40.895 -41.263 -6.362  1.00 24.23 ?  163 LYS   B HB2  1 
ATOM   6619 H HB3  . LYS   B 1 163 ? 40.476 -39.766 -6.035  1.00 24.23 ?  163 LYS   B HB3  1 
ATOM   6620 H HG2  . LYS   B 1 163 ? 38.355 -40.500 -5.416  1.00 29.54 ?  163 LYS   B HG2  1 
ATOM   6621 H HG3  . LYS   B 1 163 ? 38.787 -41.997 -5.731  1.00 29.54 ?  163 LYS   B HG3  1 
ATOM   6622 H HD2  . LYS   B 1 163 ? 40.362 -41.870 -3.986  1.00 34.69 ?  163 LYS   B HD2  1 
ATOM   6623 H HD3  . LYS   B 1 163 ? 39.817 -40.413 -3.638  1.00 34.69 ?  163 LYS   B HD3  1 
ATOM   6624 H HE2  . LYS   B 1 163 ? 37.636 -41.565 -3.407  1.00 39.96 ?  163 LYS   B HE2  1 
ATOM   6625 H HE3  . LYS   B 1 163 ? 38.527 -42.863 -3.231  1.00 39.96 ?  163 LYS   B HE3  1 
ATOM   6626 H HZ1  . LYS   B 1 163 ? 38.030 -41.965 -1.208  1.00 42.71 ?  163 LYS   B HZ1  1 
ATOM   6627 H HZ2  . LYS   B 1 163 ? 39.465 -41.909 -1.402  1.00 42.71 ?  163 LYS   B HZ2  1 
ATOM   6628 H HZ3  . LYS   B 1 163 ? 38.665 -40.710 -1.556  1.00 42.71 ?  163 LYS   B HZ3  1 
ATOM   6629 N N    . LEU   B 1 164 ? 39.074 -38.087 -7.916  1.00 14.91 ?  164 LEU   B N    1 
ATOM   6630 C CA   . LEU   B 1 164 ? 38.171 -36.942 -7.977  1.00 14.61 ?  164 LEU   B CA   1 
ATOM   6631 C C    . LEU   B 1 164 ? 37.387 -36.930 -9.283  1.00 15.24 ?  164 LEU   B C    1 
ATOM   6632 O O    . LEU   B 1 164 ? 36.164 -36.729 -9.285  1.00 16.62 ?  164 LEU   B O    1 
ATOM   6633 C CB   . LEU   B 1 164 ? 38.978 -35.651 -7.822  1.00 14.34 ?  164 LEU   B CB   1 
ATOM   6634 C CG   . LEU   B 1 164 ? 39.518 -35.372 -6.422  1.00 15.51 ?  164 LEU   B CG   1 
ATOM   6635 C CD1  . LEU   B 1 164 ? 40.607 -34.315 -6.488  1.00 15.19 ?  164 LEU   B CD1  1 
ATOM   6636 C CD2  . LEU   B 1 164 ? 38.409 -34.910 -5.496  1.00 17.37 ?  164 LEU   B CD2  1 
ATOM   6637 H H    . LEU   B 1 164 ? 39.914 -37.871 -7.928  1.00 17.89 ?  164 LEU   B H    1 
ATOM   6638 H HA   . LEU   B 1 164 ? 37.541 -36.997 -7.249  1.00 17.53 ?  164 LEU   B HA   1 
ATOM   6639 H HB2  . LEU   B 1 164 ? 39.740 -35.688 -8.422  1.00 17.21 ?  164 LEU   B HB2  1 
ATOM   6640 H HB3  . LEU   B 1 164 ? 38.413 -34.903 -8.065  1.00 17.21 ?  164 LEU   B HB3  1 
ATOM   6641 H HG   . LEU   B 1 164 ? 39.907 -36.182 -6.057  1.00 18.61 ?  164 LEU   B HG   1 
ATOM   6642 H HD11 . LEU   B 1 164 ? 40.938 -34.139 -5.591  1.00 18.22 ?  164 LEU   B HD11 1 
ATOM   6643 H HD12 . LEU   B 1 164 ? 41.337 -34.641 -7.044  1.00 18.22 ?  164 LEU   B HD12 1 
ATOM   6644 H HD13 . LEU   B 1 164 ? 40.243 -33.502 -6.870  1.00 18.22 ?  164 LEU   B HD13 1 
ATOM   6645 H HD21 . LEU   B 1 164 ? 38.787 -34.692 -4.630  1.00 20.85 ?  164 LEU   B HD21 1 
ATOM   6646 H HD22 . LEU   B 1 164 ? 37.986 -34.124 -5.878  1.00 20.85 ?  164 LEU   B HD22 1 
ATOM   6647 H HD23 . LEU   B 1 164 ? 37.760 -35.624 -5.404  1.00 20.85 ?  164 LEU   B HD23 1 
ATOM   6648 N N    . VAL   B 1 165 ? 38.078 -37.114 -10.409 1.00 16.46 ?  165 VAL   B N    1 
ATOM   6649 C CA   . VAL   B 1 165 ? 37.422 -37.055 -11.711 1.00 18.20 ?  165 VAL   B CA   1 
ATOM   6650 C C    . VAL   B 1 165 ? 36.505 -38.258 -11.899 1.00 20.07 ?  165 VAL   B C    1 
ATOM   6651 O O    . VAL   B 1 165 ? 35.342 -38.120 -12.298 1.00 21.07 ?  165 VAL   B O    1 
ATOM   6652 C CB   . VAL   B 1 165 ? 38.467 -36.961 -12.839 1.00 19.31 ?  165 VAL   B CB   1 
ATOM   6653 C CG1  . VAL   B 1 165 ? 37.799 -37.057 -14.191 1.00 20.72 ?  165 VAL   B CG1  1 
ATOM   6654 C CG2  . VAL   B 1 165 ? 39.267 -35.671 -12.726 1.00 19.28 ?  165 VAL   B CG2  1 
ATOM   6655 H H    . VAL   B 1 165 ? 38.926 -37.277 -10.446 1.00 19.76 ?  165 VAL   B H    1 
ATOM   6656 H HA   . VAL   B 1 165 ? 36.879 -36.253 -11.752 1.00 21.84 ?  165 VAL   B HA   1 
ATOM   6657 H HB   . VAL   B 1 165 ? 39.092 -37.699 -12.757 1.00 23.17 ?  165 VAL   B HB   1 
ATOM   6658 H HG11 . VAL   B 1 165 ? 38.411 -36.739 -14.870 1.00 24.87 ?  165 VAL   B HG11 1 
ATOM   6659 H HG12 . VAL   B 1 165 ? 37.572 -37.986 -14.362 1.00 24.87 ?  165 VAL   B HG12 1 
ATOM   6660 H HG13 . VAL   B 1 165 ? 36.997 -36.515 -14.184 1.00 24.87 ?  165 VAL   B HG13 1 
ATOM   6661 H HG21 . VAL   B 1 165 ? 39.904 -35.623 -13.459 1.00 23.14 ?  165 VAL   B HG21 1 
ATOM   6662 H HG22 . VAL   B 1 165 ? 38.659 -34.914 -12.773 1.00 23.14 ?  165 VAL   B HG22 1 
ATOM   6663 H HG23 . VAL   B 1 165 ? 39.742 -35.658 -11.880 1.00 23.14 ?  165 VAL   B HG23 1 
ATOM   6664 N N    . SER   B 1 166 ? 37.021 -39.459 -11.615 1.00 20.87 ?  166 SER   B N    1 
ATOM   6665 C CA   . SER   B 1 166 ? 36.265 -40.675 -11.890 1.00 21.74 ?  166 SER   B CA   1 
ATOM   6666 C C    . SER   B 1 166 ? 34.993 -40.745 -11.059 1.00 21.66 ?  166 SER   B C    1 
ATOM   6667 O O    . SER   B 1 166 ? 34.025 -41.375 -11.482 1.00 23.30 ?  166 SER   B O    1 
ATOM   6668 C CB   . SER   B 1 166 ? 37.126 -41.929 -11.675 1.00 22.97 ?  166 SER   B CB   1 
ATOM   6669 O OG   . SER   B 1 166 ? 37.455 -42.125 -10.310 1.00 23.48 ?  166 SER   B OG   1 
ATOM   6670 H H    . SER   B 1 166 ? 37.805 -39.588 -11.275 1.00 25.05 ?  166 SER   B H    1 
ATOM   6671 H HA   . SER   B 1 166 ? 36.008 -40.664 -12.827 1.00 26.09 ?  166 SER   B HA   1 
ATOM   6672 H HB2  . SER   B 1 166 ? 36.634 -42.700 -11.990 1.00 27.57 ?  166 SER   B HB2  1 
ATOM   6673 H HB3  . SER   B 1 166 ? 37.949 -41.833 -12.183 1.00 27.57 ?  166 SER   B HB3  1 
ATOM   6674 H HG   . SER   B 1 166 ? 37.883 -41.456 -10.024 1.00 28.18 ?  166 SER   B HG   1 
ATOM   6675 N N    . SER   B 1 167 ? 34.964 -40.116 -9.886  1.00 19.89 ?  167 SER   B N    1 
ATOM   6676 C CA   . SER   B 1 167 ? 33.802 -40.171 -9.007  1.00 19.85 ?  167 SER   B CA   1 
ATOM   6677 C C    . SER   B 1 167 ? 32.894 -38.944 -9.094  1.00 19.78 ?  167 SER   B C    1 
ATOM   6678 O O    . SER   B 1 167 ? 31.817 -38.949 -8.488  1.00 20.36 ?  167 SER   B O    1 
ATOM   6679 C CB   . SER   B 1 167 ? 34.242 -40.368 -7.549  1.00 20.03 ?  167 SER   B CB   1 
ATOM   6680 O OG   . SER   B 1 167 ? 34.934 -39.215 -7.076  1.00 20.34 ?  167 SER   B OG   1 
ATOM   6681 H H    . SER   B 1 167 ? 35.619 -39.664 -9.574  1.00 23.86 ?  167 SER   B H    1 
ATOM   6682 H HA   . SER   B 1 167 ? 33.270 -40.944 -9.256  1.00 23.83 ?  167 SER   B HA   1 
ATOM   6683 H HB2  . SER   B 1 167 ? 33.452 -40.520 -7.004  1.00 24.03 ?  167 SER   B HB2  1 
ATOM   6684 H HB3  . SER   B 1 167 ? 34.820 -41.155 -7.502  1.00 24.03 ?  167 SER   B HB3  1 
ATOM   6685 H HG   . SER   B 1 167 ? 35.630 -39.109 -7.529  1.00 24.41 ?  167 SER   B HG   1 
ATOM   6686 N N    . PHE   B 1 168 ? 33.281 -37.901 -9.830  1.00 19.63 ?  168 PHE   B N    1 
ATOM   6687 C CA   . PHE   B 1 168 ? 32.440 -36.704 -9.893  1.00 18.91 ?  168 PHE   B CA   1 
ATOM   6688 C C    . PHE   B 1 168 ? 31.133 -36.972 -10.635 1.00 15.79 ?  168 PHE   B C    1 
ATOM   6689 O O    . PHE   B 1 168 ? 30.085 -36.388 -10.296 1.00 16.26 ?  168 PHE   B O    1 
ATOM   6690 C CB   . PHE   B 1 168 ? 33.205 -35.551 -10.546 1.00 19.49 ?  168 PHE   B CB   1 
ATOM   6691 C CG   . PHE   B 1 168 ? 32.385 -34.308 -10.701 1.00 19.60 ?  168 PHE   B CG   1 
ATOM   6692 C CD1  . PHE   B 1 168 ? 32.013 -33.572 -9.585  1.00 21.05 ?  168 PHE   B CD1  1 
ATOM   6693 C CD2  . PHE   B 1 168 ? 31.956 -33.890 -11.946 1.00 18.90 ?  168 PHE   B CD2  1 
ATOM   6694 C CE1  . PHE   B 1 168 ? 31.239 -32.439 -9.706  1.00 20.83 ?  168 PHE   B CE1  1 
ATOM   6695 C CE2  . PHE   B 1 168 ? 31.192 -32.734 -12.079 1.00 19.54 ?  168 PHE   B CE2  1 
ATOM   6696 C CZ   . PHE   B 1 168 ? 30.826 -32.010 -10.952 1.00 20.01 ?  168 PHE   B CZ   1 
ATOM   6697 H H    . PHE   B 1 168 ? 34.012 -37.858 -10.284 1.00 23.55 ?  168 PHE   B H    1 
ATOM   6698 H HA   . PHE   B 1 168 ? 32.213 -36.440 -8.993  1.00 22.69 ?  168 PHE   B HA   1 
ATOM   6699 H HB2  . PHE   B 1 168 ? 33.972 -35.331 -9.993  1.00 23.38 ?  168 PHE   B HB2  1 
ATOM   6700 H HB3  . PHE   B 1 168 ? 33.500 -35.822 -11.428 1.00 23.38 ?  168 PHE   B HB3  1 
ATOM   6701 H HD1  . PHE   B 1 168 ? 32.282 -33.856 -8.743  1.00 25.27 ?  168 PHE   B HD1  1 
ATOM   6702 H HD2  . PHE   B 1 168 ? 32.199 -34.366 -12.702 1.00 22.68 ?  168 PHE   B HD2  1 
ATOM   6703 H HE1  . PHE   B 1 168 ? 31.000 -31.957 -8.948  1.00 25.00 ?  168 PHE   B HE1  1 
ATOM   6704 H HE2  . PHE   B 1 168 ? 30.908 -32.454 -12.921 1.00 23.45 ?  168 PHE   B HE2  1 
ATOM   6705 H HZ   . PHE   B 1 168 ? 30.304 -31.243 -11.035 1.00 24.01 ?  168 PHE   B HZ   1 
ATOM   6706 N N    . LEU   B 1 169 ? 31.183 -37.836 -11.647 1.00 16.29 ?  169 LEU   B N    1 
ATOM   6707 C CA   . LEU   B 1 169 ? 30.011 -38.175 -12.450 1.00 18.94 ?  169 LEU   B CA   1 
ATOM   6708 C C    . LEU   B 1 169 ? 30.010 -39.620 -12.924 1.00 22.50 ?  169 LEU   B C    1 
ATOM   6709 O O    . LEU   B 1 169 ? 29.094 -40.059 -13.623 1.00 25.13 ?  169 LEU   B O    1 
ATOM   6710 C CB   . LEU   B 1 169 ? 29.931 -37.259 -13.668 1.00 21.08 ?  169 LEU   B CB   1 
ATOM   6711 C CG   . LEU   B 1 169 ? 28.706 -36.352 -13.760 1.00 24.62 ?  169 LEU   B CG   1 
ATOM   6712 C CD1  . LEU   B 1 169 ? 28.662 -35.691 -15.120 1.00 25.66 ?  169 LEU   B CD1  1 
ATOM   6713 C CD2  . LEU   B 1 169 ? 27.425 -37.121 -13.494 1.00 25.04 ?  169 LEU   B CD2  1 
ATOM   6714 O OXT  . LEU   B 1 169 ? 30.926 -40.378 -12.636 1.00 23.53 -1 169 LEU   B OXT  1 
ATOM   6715 H H    . LEU   B 1 169 ? 31.904 -38.237 -11.906 1.00 19.55 ?  169 LEU   B H    1 
ATOM   6716 H HA   . LEU   B 1 169 ? 29.227 -38.036 -11.907 1.00 22.72 ?  169 LEU   B HA   1 
ATOM   6717 H HB2  . LEU   B 1 169 ? 30.713 -36.683 -13.676 1.00 25.29 ?  169 LEU   B HB2  1 
ATOM   6718 H HB3  . LEU   B 1 169 ? 29.934 -37.811 -14.466 1.00 25.29 ?  169 LEU   B HB3  1 
ATOM   6719 H HG   . LEU   B 1 169 ? 28.779 -35.651 -13.092 1.00 29.55 ?  169 LEU   B HG   1 
ATOM   6720 H HD11 . LEU   B 1 169 ? 27.896 -35.098 -15.157 1.00 30.79 ?  169 LEU   B HD11 1 
ATOM   6721 H HD12 . LEU   B 1 169 ? 29.480 -35.187 -15.250 1.00 30.79 ?  169 LEU   B HD12 1 
ATOM   6722 H HD13 . LEU   B 1 169 ? 28.583 -36.379 -15.799 1.00 30.79 ?  169 LEU   B HD13 1 
ATOM   6723 H HD21 . LEU   B 1 169 ? 26.685 -36.663 -13.917 1.00 30.05 ?  169 LEU   B HD21 1 
ATOM   6724 H HD22 . LEU   B 1 169 ? 27.517 -38.016 -13.862 1.00 30.05 ?  169 LEU   B HD22 1 
ATOM   6725 H HD23 . LEU   B 1 169 ? 27.283 -37.172 -12.537 1.00 30.05 ?  169 LEU   B HD23 1 
HETATM 6726 N N2   B A1A7W C 2 .   ? 15.591 3.260   5.765   0.58 10.42 ?  201 A1A7W A N2   1 
HETATM 6727 C C3   B A1A7W C 2 .   ? 14.062 0.374   -0.385  0.58 12.18 ?  201 A1A7W A C3   1 
HETATM 6728 C C6   B A1A7W C 2 .   ? 14.383 2.130   0.892   0.58 11.33 ?  201 A1A7W A C6   1 
HETATM 6729 C C9   B A1A7W C 2 .   ? 15.520 3.601   3.557   0.58 10.68 ?  201 A1A7W A C9   1 
HETATM 6730 C C12  B A1A7W C 2 .   ? 15.041 -0.204  5.023   0.58 12.34 ?  201 A1A7W A C12  1 
HETATM 6731 C C1   B A1A7W C 2 .   ? 15.986 -1.006  0.662   0.58 12.16 ?  201 A1A7W A C1   1 
HETATM 6732 C C10  B A1A7W C 2 .   ? 15.685 4.214   4.773   0.58 10.61 ?  201 A1A7W A C10  1 
HETATM 6733 C C11  B A1A7W C 2 .   ? 15.366 2.019   5.204   0.58 10.85 ?  201 A1A7W A C11  1 
HETATM 6734 C C13  B A1A7W C 2 .   ? 13.189 1.469   0.214   0.58 11.78 ?  201 A1A7W A C13  1 
HETATM 6735 C C2   B A1A7W C 2 .   ? 14.714 -0.185  0.898   0.58 11.18 ?  201 A1A7W A C2   1 
HETATM 6736 C C4   B A1A7W C 2 .   ? 15.083 1.201   -1.197  0.58 12.27 ?  201 A1A7W A C4   1 
HETATM 6737 C C5   B A1A7W C 2 .   ? 15.284 2.441   -0.313  0.58 11.62 ?  201 A1A7W A C5   1 
HETATM 6738 C C7   B A1A7W C 2 .   ? 15.070 1.018   3.045   0.58 11.08 ?  201 A1A7W A C7   1 
HETATM 6739 C C8   B A1A7W C 2 .   ? 15.304 2.198   3.806   0.58 11.00 ?  201 A1A7W A C8   1 
HETATM 6740 N N1   B A1A7W C 2 .   ? 14.997 1.037   1.647   0.58 11.20 ?  201 A1A7W A N1   1 
HETATM 6741 N N3   B A1A7W C 2 .   ? 15.235 0.829   5.845   0.58 11.92 ?  201 A1A7W A N3   1 
HETATM 6742 N N4   B A1A7W C 2 .   ? 14.968 -0.179  3.689   0.58 11.81 ?  201 A1A7W A N4   1 
HETATM 6743 O O1   B A1A7W C 2 .   ? 15.683 -2.112  -0.154  0.58 13.19 ?  201 A1A7W A O1   1 
HETATM 6744 H H13  B A1A7W C 2 .   ? 15.689 3.459   6.751   0.58 12.50 ?  201 A1A7W A H13  1 
HETATM 6745 H H2   B A1A7W C 2 .   ? 13.526 -0.376  -0.966  0.58 14.62 ?  201 A1A7W A H2   1 
HETATM 6746 H H3   B A1A7W C 2 .   ? 14.122 3.006   1.481   0.58 13.59 ?  201 A1A7W A H3   1 
HETATM 6747 H H11  B A1A7W C 2 .   ? 15.516 4.069   2.590   0.58 12.81 ?  201 A1A7W A H11  1 
HETATM 6748 H H14  B A1A7W C 2 .   ? 14.916 -1.164  5.506   0.58 14.80 ?  201 A1A7W A H14  1 
HETATM 6749 H H5   B A1A7W C 2 .   ? 16.798 -0.411  0.235   0.58 14.59 ?  201 A1A7W A H5   1 
HETATM 6750 H H6   B A1A7W C 2 .   ? 16.358 -1.396  1.608   0.58 14.59 ?  201 A1A7W A H6   1 
HETATM 6751 H H12  B A1A7W C 2 .   ? 15.847 5.249   5.012   0.58 12.74 ?  201 A1A7W A H12  1 
HETATM 6752 H H15  B A1A7W C 2 .   ? 12.436 1.104   0.916   0.58 14.13 ?  201 A1A7W A H15  1 
HETATM 6753 H H16  B A1A7W C 2 .   ? 12.704 2.098   -0.534  0.58 14.13 ?  201 A1A7W A H16  1 
HETATM 6754 H H1   B A1A7W C 2 .   ? 13.971 -0.792  1.429   0.58 13.42 ?  201 A1A7W A H1   1 
HETATM 6755 H H8   B A1A7W C 2 .   ? 14.655 1.480   -2.155  0.58 14.72 ?  201 A1A7W A H8   1 
HETATM 6756 H H7   B A1A7W C 2 .   ? 16.010 0.670   -1.409  0.58 14.72 ?  201 A1A7W A H7   1 
HETATM 6757 H H9   B A1A7W C 2 .   ? 14.990 3.366   -0.819  0.58 13.95 ?  201 A1A7W A H9   1 
HETATM 6758 H H10  B A1A7W C 2 .   ? 16.326 2.540   -0.011  0.58 13.95 ?  201 A1A7W A H10  1 
HETATM 6759 H H4   B A1A7W C 2 .   ? 16.423 -2.284  -0.713  0.58 15.83 ?  201 A1A7W A H4   1 
HETATM 6760 O O    A HOH   D 3 .   ? 14.848 -4.558  20.369  0.42 33.11 ?  301 HOH   A O    1 
HETATM 6761 O O    . HOH   D 3 .   ? 3.729  -9.496  9.709   1.00 40.58 ?  302 HOH   A O    1 
HETATM 6762 O O    . HOH   D 3 .   ? 25.989 -1.009  -7.695  1.00 25.79 ?  303 HOH   A O    1 
HETATM 6763 O O    . HOH   D 3 .   ? 29.054 0.314   -9.888  1.00 21.64 ?  304 HOH   A O    1 
HETATM 6764 O O    . HOH   D 3 .   ? 34.464 -1.811  12.475  1.00 36.59 ?  305 HOH   A O    1 
HETATM 6765 O O    . HOH   D 3 .   ? 15.148 -12.202 18.563  1.00 45.81 ?  306 HOH   A O    1 
HETATM 6766 O O    . HOH   D 3 .   ? 17.162 -18.001 14.937  1.00 30.16 ?  307 HOH   A O    1 
HETATM 6767 O O    . HOH   D 3 .   ? 11.992 0.358   14.537  1.00 34.27 ?  308 HOH   A O    1 
HETATM 6768 O O    . HOH   D 3 .   ? 10.936 1.720   12.195  1.00 23.25 ?  309 HOH   A O    1 
HETATM 6769 O O    . HOH   D 3 .   ? 14.214 -4.498  -11.921 1.00 47.53 ?  310 HOH   A O    1 
HETATM 6770 O O    . HOH   D 3 .   ? 4.618  3.854   0.559   1.00 27.27 ?  311 HOH   A O    1 
HETATM 6771 O O    . HOH   D 3 .   ? 28.124 -6.206  19.562  1.00 42.32 ?  312 HOH   A O    1 
HETATM 6772 O O    . HOH   D 3 .   ? 11.847 -10.860 -10.032 1.00 59.18 ?  313 HOH   A O    1 
HETATM 6773 O O    . HOH   D 3 .   ? 14.978 4.012   17.400  1.00 40.10 ?  314 HOH   A O    1 
HETATM 6774 O O    . HOH   D 3 .   ? 7.622  -6.398  -6.631  1.00 42.99 ?  315 HOH   A O    1 
HETATM 6775 O O    . HOH   D 3 .   ? 9.326  -10.081 19.349  1.00 43.75 ?  316 HOH   A O    1 
HETATM 6776 O O    . HOH   D 3 .   ? 30.362 -13.327 -8.490  1.00 21.17 ?  317 HOH   A O    1 
HETATM 6777 O O    . HOH   D 3 .   ? 42.393 10.598  5.054   1.00 20.09 ?  318 HOH   A O    1 
HETATM 6778 O O    . HOH   D 3 .   ? 14.716 -13.845 16.698  1.00 28.25 ?  319 HOH   A O    1 
HETATM 6779 O O    . HOH   D 3 .   ? 22.675 -12.017 21.892  1.00 55.94 ?  320 HOH   A O    1 
HETATM 6780 O O    . HOH   D 3 .   ? 15.263 -21.537 14.173  1.00 18.85 ?  321 HOH   A O    1 
HETATM 6781 O O    . HOH   D 3 .   ? 20.112 -12.676 -8.759  1.00 27.66 ?  322 HOH   A O    1 
HETATM 6782 O O    . HOH   D 3 .   ? 26.895 11.465  1.586   1.00 16.67 ?  323 HOH   A O    1 
HETATM 6783 O O    . HOH   D 3 .   ? 19.520 -11.022 24.079  1.00 78.29 ?  324 HOH   A O    1 
HETATM 6784 O O    . HOH   D 3 .   ? 36.285 -5.098  -0.504  1.00 31.91 ?  325 HOH   A O    1 
HETATM 6785 O O    . HOH   D 3 .   ? 30.905 6.209   -12.317 1.00 26.20 ?  326 HOH   A O    1 
HETATM 6786 O O    . HOH   D 3 .   ? 37.529 2.855   10.183  1.00 27.44 ?  327 HOH   A O    1 
HETATM 6787 O O    . HOH   D 3 .   ? 31.065 -18.075 7.772   1.00 18.89 ?  328 HOH   A O    1 
HETATM 6788 O O    . HOH   D 3 .   ? 8.053  -12.702 -0.950  1.00 29.16 ?  329 HOH   A O    1 
HETATM 6789 O O    . HOH   D 3 .   ? 18.754 -19.327 13.564  1.00 31.20 ?  330 HOH   A O    1 
HETATM 6790 O O    . HOH   D 3 .   ? 14.533 -21.213 -4.249  1.00 32.98 ?  331 HOH   A O    1 
HETATM 6791 O O    A HOH   D 3 .   ? 0.806  -4.617  0.184   0.42 24.21 ?  332 HOH   A O    1 
HETATM 6792 O O    A HOH   D 3 .   ? 17.568 -1.718  0.386   0.42 18.53 ?  333 HOH   A O    1 
HETATM 6793 O O    . HOH   D 3 .   ? 22.254 -19.305 11.353  1.00 33.94 ?  334 HOH   A O    1 
HETATM 6794 O O    . HOH   D 3 .   ? 38.264 10.287  7.073   1.00 41.69 ?  335 HOH   A O    1 
HETATM 6795 O O    B HOH   D 3 .   ? 15.290 6.834   7.070   0.58 17.49 ?  336 HOH   A O    1 
HETATM 6796 O O    . HOH   D 3 .   ? 27.441 13.809  2.752   1.00 26.07 ?  337 HOH   A O    1 
HETATM 6797 O O    . HOH   D 3 .   ? 44.309 7.188   6.409   1.00 26.31 ?  338 HOH   A O    1 
HETATM 6798 O O    . HOH   D 3 .   ? 38.563 5.008   6.940   1.00 15.10 ?  339 HOH   A O    1 
HETATM 6799 O O    . HOH   D 3 .   ? 22.747 12.508  1.525   1.00 14.48 ?  340 HOH   A O    1 
HETATM 6800 O O    . HOH   D 3 .   ? 10.091 -21.347 5.686   1.00 21.81 ?  341 HOH   A O    1 
HETATM 6801 O O    . HOH   D 3 .   ? 8.186  -21.465 4.047   1.00 47.73 ?  342 HOH   A O    1 
HETATM 6802 O O    B HOH   D 3 .   ? 14.928 -2.851  3.144   0.58 12.14 ?  343 HOH   A O    1 
HETATM 6803 O O    A HOH   D 3 .   ? 28.304 -0.233  -13.392 0.42 23.22 ?  344 HOH   A O    1 
HETATM 6804 O O    . HOH   D 3 .   ? 19.088 -21.958 6.879   1.00 36.00 ?  345 HOH   A O    1 
HETATM 6805 O O    . HOH   D 3 .   ? 21.254 10.260  14.905  1.00 37.64 ?  346 HOH   A O    1 
HETATM 6806 O O    . HOH   D 3 .   ? 32.177 -9.304  -6.605  1.00 23.33 ?  347 HOH   A O    1 
HETATM 6807 O O    . HOH   D 3 .   ? 31.714 8.260   14.779  1.00 23.95 ?  348 HOH   A O    1 
HETATM 6808 O O    . HOH   D 3 .   ? 43.345 7.797   2.627   1.00 28.68 ?  349 HOH   A O    1 
HETATM 6809 O O    B HOH   D 3 .   ? 11.196 6.416   8.878   0.58 21.95 ?  350 HOH   A O    1 
HETATM 6810 O O    . HOH   D 3 .   ? 34.070 -1.103  -8.983  1.00 25.82 ?  351 HOH   A O    1 
HETATM 6811 O O    A HOH   D 3 .   ? 14.343 0.583   6.736   0.42 24.27 ?  352 HOH   A O    1 
HETATM 6812 O O    . HOH   D 3 .   ? 39.799 -1.033  -5.207  1.00 19.85 ?  353 HOH   A O    1 
HETATM 6813 O O    . HOH   D 3 .   ? 13.637 -15.296 -7.673  1.00 32.09 ?  354 HOH   A O    1 
HETATM 6814 O O    . HOH   D 3 .   ? 22.182 5.418   18.865  1.00 49.12 ?  355 HOH   A O    1 
HETATM 6815 O O    . HOH   D 3 .   ? 42.538 4.301   5.389   1.00 33.30 ?  356 HOH   A O    1 
HETATM 6816 O O    . HOH   D 3 .   ? 5.322  2.513   4.927   1.00 35.65 ?  357 HOH   A O    1 
HETATM 6817 O O    . HOH   D 3 .   ? 35.869 -12.622 6.808   1.00 15.61 ?  358 HOH   A O    1 
HETATM 6818 O O    . HOH   D 3 .   ? 18.555 9.514   8.886   1.00 21.70 ?  359 HOH   A O    1 
HETATM 6819 O O    . HOH   D 3 .   ? 31.186 -13.936 -2.468  1.00 13.32 ?  360 HOH   A O    1 
HETATM 6820 O O    . HOH   D 3 .   ? 20.757 -19.738 -5.157  1.00 28.39 ?  361 HOH   A O    1 
HETATM 6821 O O    . HOH   D 3 .   ? 17.282 -17.810 -5.109  1.00 31.92 ?  362 HOH   A O    1 
HETATM 6822 O O    A HOH   D 3 .   ? 14.706 -3.653  3.044   0.42 17.46 ?  363 HOH   A O    1 
HETATM 6823 O O    . HOH   D 3 .   ? 29.793 -2.036  -12.877 1.00 53.10 ?  364 HOH   A O    1 
HETATM 6824 O O    A HOH   D 3 .   ? 7.014  -8.140  11.801  0.42 16.06 ?  365 HOH   A O    1 
HETATM 6825 O O    . HOH   D 3 .   ? 27.481 -10.492 14.047  1.00 16.69 ?  366 HOH   A O    1 
HETATM 6826 O O    B HOH   D 3 .   ? 13.284 -3.207  -0.960  0.58 18.33 ?  367 HOH   A O    1 
HETATM 6827 O O    . HOH   D 3 .   ? 30.815 3.117   8.196   1.00 11.61 ?  368 HOH   A O    1 
HETATM 6828 O O    A HOH   D 3 .   ? 21.320 -2.407  -2.104  0.42 15.63 ?  369 HOH   A O    1 
HETATM 6829 O O    B HOH   D 3 .   ? 10.949 -1.119  1.524   0.58 14.90 ?  370 HOH   A O    1 
HETATM 6830 O O    . HOH   D 3 .   ? 21.892 -21.837 8.496   1.00 28.46 ?  371 HOH   A O    1 
HETATM 6831 O O    A HOH   D 3 .   ? 24.659 2.018   -7.048  0.42 19.49 ?  372 HOH   A O    1 
HETATM 6832 O O    . HOH   D 3 .   ? 24.098 -2.138  -2.285  1.00 12.30 ?  373 HOH   A O    1 
HETATM 6833 O O    . HOH   D 3 .   ? -0.848 -8.631  2.000   1.00 43.33 ?  374 HOH   A O    1 
HETATM 6834 O O    . HOH   D 3 .   ? 44.001 8.531   -3.041  1.00 29.17 ?  375 HOH   A O    1 
HETATM 6835 O O    . HOH   D 3 .   ? 8.821  -11.890 17.197  1.00 35.67 ?  376 HOH   A O    1 
HETATM 6836 O O    . HOH   D 3 .   ? 37.231 -2.895  9.691   1.00 48.39 ?  377 HOH   A O    1 
HETATM 6837 O O    . HOH   D 3 .   ? 37.248 12.069  4.898   1.00 25.85 ?  378 HOH   A O    1 
HETATM 6838 O O    . HOH   D 3 .   ? 14.514 -24.655 11.576  1.00 44.09 ?  379 HOH   A O    1 
HETATM 6839 O O    . HOH   D 3 .   ? 33.703 -7.126  4.289   1.00 15.87 ?  380 HOH   A O    1 
HETATM 6840 O O    B HOH   D 3 .   ? 21.230 2.782   -0.019  0.58 12.02 ?  381 HOH   A O    1 
HETATM 6841 O O    . HOH   D 3 .   ? 24.368 3.653   -1.829  1.00 19.11 ?  382 HOH   A O    1 
HETATM 6842 O O    B HOH   D 3 .   ? 21.278 -2.019  -3.006  0.58 15.42 ?  383 HOH   A O    1 
HETATM 6843 O O    A HOH   D 3 .   ? -0.407 -3.090  3.035   0.42 28.49 ?  384 HOH   A O    1 
HETATM 6844 O O    . HOH   D 3 .   ? 32.098 -7.327  -9.769  1.00 21.78 ?  385 HOH   A O    1 
HETATM 6845 O O    B HOH   D 3 .   ? 9.208  2.080   7.596   0.58 27.23 ?  386 HOH   A O    1 
HETATM 6846 O O    . HOH   D 3 .   ? 10.460 -22.155 -1.218  1.00 62.01 ?  387 HOH   A O    1 
HETATM 6847 O O    . HOH   D 3 .   ? 14.385 -0.397  -12.292 1.00 47.48 ?  388 HOH   A O    1 
HETATM 6848 O O    . HOH   D 3 .   ? 24.235 -7.686  14.374  1.00 15.59 ?  389 HOH   A O    1 
HETATM 6849 O O    . HOH   D 3 .   ? 26.918 -3.123  19.484  1.00 39.26 ?  390 HOH   A O    1 
HETATM 6850 O O    A HOH   D 3 .   ? 13.385 -1.457  -6.583  0.42 19.19 ?  391 HOH   A O    1 
HETATM 6851 O O    . HOH   D 3 .   ? 17.123 -19.267 4.851   1.00 15.32 ?  392 HOH   A O    1 
HETATM 6852 O O    . HOH   D 3 .   ? 26.977 4.152   -0.777  1.00 12.25 ?  393 HOH   A O    1 
HETATM 6853 O O    . HOH   D 3 .   ? 15.409 11.886  7.827   1.00 41.79 ?  394 HOH   A O    1 
HETATM 6854 O O    . HOH   D 3 .   ? 16.694 -22.082 0.962   1.00 34.14 ?  395 HOH   A O    1 
HETATM 6855 O O    . HOH   D 3 .   ? 6.416  -5.504  11.054  1.00 21.04 ?  396 HOH   A O    1 
HETATM 6856 O O    . HOH   D 3 .   ? 23.501 11.419  3.986   1.00 12.18 ?  397 HOH   A O    1 
HETATM 6857 O O    . HOH   D 3 .   ? 30.632 1.939   16.676  1.00 20.06 ?  398 HOH   A O    1 
HETATM 6858 O O    . HOH   D 3 .   ? 20.656 -19.981 2.789   1.00 19.38 ?  399 HOH   A O    1 
HETATM 6859 O O    . HOH   D 3 .   ? 24.792 -17.484 12.683  1.00 23.89 ?  400 HOH   A O    1 
HETATM 6860 O O    . HOH   D 3 .   ? 13.806 -4.699  17.223  1.00 26.61 ?  401 HOH   A O    1 
HETATM 6861 O O    . HOH   D 3 .   ? 27.972 0.826   -7.337  1.00 14.94 ?  402 HOH   A O    1 
HETATM 6862 O O    A HOH   D 3 .   ? 21.420 3.149   -0.414  0.42 9.10  ?  403 HOH   A O    1 
HETATM 6863 O O    . HOH   D 3 .   ? 14.177 -23.039 7.422   1.00 19.95 ?  404 HOH   A O    1 
HETATM 6864 O O    . HOH   D 3 .   ? 27.234 2.404   18.597  1.00 30.63 ?  405 HOH   A O    1 
HETATM 6865 O O    . HOH   D 3 .   ? 38.134 -1.305  -1.947  1.00 18.33 ?  406 HOH   A O    1 
HETATM 6866 O O    . HOH   D 3 .   ? 32.817 -9.224  5.910   1.00 20.02 ?  407 HOH   A O    1 
HETATM 6867 O O    A HOH   D 3 .   ? 18.655 -2.507  -16.392 0.42 28.59 ?  408 HOH   A O    1 
HETATM 6868 O O    . HOH   D 3 .   ? 18.833 -0.788  -1.559  1.00 24.82 ?  409 HOH   A O    1 
HETATM 6869 O O    . HOH   D 3 .   ? 37.618 -2.025  5.804   1.00 26.99 ?  410 HOH   A O    1 
HETATM 6870 O O    . HOH   D 3 .   ? 10.484 -13.836 -1.872  1.00 21.49 ?  411 HOH   A O    1 
HETATM 6871 O O    A HOH   D 3 .   ? 20.175 4.519   -7.615  0.42 23.58 ?  412 HOH   A O    1 
HETATM 6872 O O    . HOH   D 3 .   ? 11.786 -10.608 16.928  1.00 27.42 ?  413 HOH   A O    1 
HETATM 6873 O O    A HOH   D 3 .   ? 15.869 -0.939  5.211   0.42 26.06 ?  414 HOH   A O    1 
HETATM 6874 O O    . HOH   D 3 .   ? 16.281 16.675  8.612   1.00 39.73 ?  415 HOH   A O    1 
HETATM 6875 O O    . HOH   D 3 .   ? 15.287 -8.328  -9.909  1.00 32.35 ?  416 HOH   A O    1 
HETATM 6876 O O    B HOH   D 3 .   ? 7.872  3.783   1.455   0.58 24.96 ?  417 HOH   A O    1 
HETATM 6877 O O    . HOH   D 3 .   ? 21.937 -13.921 -8.216  1.00 52.26 ?  418 HOH   A O    1 
HETATM 6878 O O    . HOH   D 3 .   ? 15.765 2.311   24.566  1.00 63.80 ?  419 HOH   A O    1 
HETATM 6879 O O    . HOH   D 3 .   ? 27.740 -6.419  -14.145 1.00 38.56 ?  420 HOH   A O    1 
HETATM 6880 O O    . HOH   D 3 .   ? -1.358 -4.921  7.500   1.00 41.49 ?  421 HOH   A O    1 
HETATM 6881 O O    . HOH   D 3 .   ? 30.099 -10.022 13.024  1.00 22.85 ?  422 HOH   A O    1 
HETATM 6882 O O    . HOH   D 3 .   ? 41.046 -8.258  -6.755  1.00 36.46 ?  423 HOH   A O    1 
HETATM 6883 O O    . HOH   D 3 .   ? 30.366 -12.823 13.527  1.00 19.62 ?  424 HOH   A O    1 
HETATM 6884 O O    . HOH   D 3 .   ? 16.024 6.929   2.765   1.00 17.37 ?  425 HOH   A O    1 
HETATM 6885 O O    . HOH   D 3 .   ? 24.037 -20.267 -1.332  1.00 17.10 ?  426 HOH   A O    1 
HETATM 6886 O O    . HOH   D 3 .   ? 28.718 -10.513 -14.030 1.00 46.27 ?  427 HOH   A O    1 
HETATM 6887 O O    . HOH   D 3 .   ? 35.199 -5.253  -3.083  1.00 18.31 ?  428 HOH   A O    1 
HETATM 6888 O O    . HOH   D 3 .   ? 24.008 3.964   -4.872  1.00 31.14 ?  429 HOH   A O    1 
HETATM 6889 O O    . HOH   D 3 .   ? 16.293 -14.152 20.227  1.00 54.34 ?  430 HOH   A O    1 
HETATM 6890 O O    . HOH   D 3 .   ? 24.068 -15.796 -9.247  1.00 38.95 ?  431 HOH   A O    1 
HETATM 6891 O O    . HOH   D 3 .   ? 32.634 -10.613 3.215   1.00 30.89 ?  432 HOH   A O    1 
HETATM 6892 O O    A HOH   D 3 .   ? 11.138 -0.381  1.870   0.42 20.51 ?  433 HOH   A O    1 
HETATM 6893 O O    . HOH   D 3 .   ? 41.666 1.545   5.003   1.00 36.83 ?  434 HOH   A O    1 
HETATM 6894 O O    . HOH   D 3 .   ? 32.912 -4.552  -9.941  1.00 27.70 ?  435 HOH   A O    1 
HETATM 6895 O O    . HOH   D 3 .   ? 36.743 -4.998  5.378   1.00 23.73 ?  436 HOH   A O    1 
HETATM 6896 O O    . HOH   D 3 .   ? 6.644  -3.441  12.833  1.00 32.88 ?  437 HOH   A O    1 
HETATM 6897 O O    . HOH   D 3 .   ? 11.068 -15.200 -6.089  1.00 40.67 ?  438 HOH   A O    1 
HETATM 6898 O O    . HOH   D 3 .   ? 45.092 -0.654  2.886   1.00 40.20 ?  439 HOH   A O    1 
HETATM 6899 O O    B HOH   D 3 .   ? 7.418  3.525   4.017   0.58 21.93 ?  440 HOH   A O    1 
HETATM 6900 O O    B HOH   D 3 .   ? 19.189 -0.368  -4.172  0.58 14.64 ?  441 HOH   A O    1 
HETATM 6901 O O    A HOH   D 3 .   ? 18.936 2.026   -0.815  0.42 9.63  ?  442 HOH   A O    1 
HETATM 6902 O O    . HOH   D 3 .   ? 23.470 -20.931 1.305   1.00 19.41 ?  443 HOH   A O    1 
HETATM 6903 O O    . HOH   D 3 .   ? 20.545 -17.614 24.800  1.00 59.23 ?  444 HOH   A O    1 
HETATM 6904 O O    . HOH   D 3 .   ? 23.535 -7.978  17.050  1.00 22.99 ?  445 HOH   A O    1 
HETATM 6905 O O    . HOH   D 3 .   ? 22.591 8.170   18.356  1.00 46.07 ?  446 HOH   A O    1 
HETATM 6906 O O    A HOH   D 3 .   ? 18.516 4.802   -15.099 0.42 40.23 ?  447 HOH   A O    1 
HETATM 6907 O O    . HOH   D 3 .   ? 37.857 -8.853  -3.428  1.00 23.16 ?  448 HOH   A O    1 
HETATM 6908 O O    . HOH   D 3 .   ? 18.434 -15.920 16.107  1.00 40.79 ?  449 HOH   A O    1 
HETATM 6909 O O    . HOH   D 3 .   ? 34.256 -8.288  -0.416  1.00 30.59 ?  450 HOH   A O    1 
HETATM 6910 O O    . HOH   D 3 .   ? 31.385 -12.806 0.012   1.00 20.26 ?  451 HOH   A O    1 
HETATM 6911 O O    A HOH   D 3 .   ? 16.331 2.938   -1.509  0.42 19.03 ?  452 HOH   A O    1 
HETATM 6912 O O    . HOH   D 3 .   ? 23.301 7.127   -3.061  1.00 39.12 ?  453 HOH   A O    1 
HETATM 6913 O O    . HOH   D 3 .   ? 30.578 14.786  2.694   1.00 19.03 ?  454 HOH   A O    1 
HETATM 6914 O O    A HOH   D 3 .   ? 9.461  -16.336 -2.011  0.42 36.67 ?  455 HOH   A O    1 
HETATM 6915 O O    A HOH   D 3 .   ? 14.098 -0.336  3.400   0.42 39.84 ?  456 HOH   A O    1 
HETATM 6916 O O    B HOH   D 3 .   ? 18.714 1.670   -0.515  0.58 13.46 ?  457 HOH   A O    1 
HETATM 6917 O O    B HOH   D 3 .   ? 17.797 3.426   -3.029  0.58 31.02 ?  458 HOH   A O    1 
HETATM 6918 O O    . HOH   D 3 .   ? 21.506 -9.089  21.277  1.00 62.80 ?  459 HOH   A O    1 
HETATM 6919 O O    . HOH   D 3 .   ? 21.626 -14.828 17.856  1.00 55.64 ?  460 HOH   A O    1 
HETATM 6920 O O    . HOH   D 3 .   ? 29.827 -15.942 10.741  1.00 29.71 ?  461 HOH   A O    1 
HETATM 6921 O O    . HOH   D 3 .   ? 25.434 8.364   -4.675  1.00 35.49 ?  462 HOH   A O    1 
HETATM 6922 O O    . HOH   D 3 .   ? 32.460 -15.899 10.822  1.00 30.05 ?  463 HOH   A O    1 
HETATM 6923 O O    . HOH   D 3 .   ? 24.883 5.696   20.602  1.00 54.82 ?  464 HOH   A O    1 
HETATM 6924 O O    . HOH   D 3 .   ? 20.006 -17.420 -5.034  1.00 32.22 ?  465 HOH   A O    1 
HETATM 6925 O O    . HOH   D 3 .   ? 27.968 7.073   -6.778  1.00 46.51 ?  466 HOH   A O    1 
HETATM 6926 O O    . HOH   D 3 .   ? 23.269 -22.304 -3.370  1.00 35.73 ?  467 HOH   A O    1 
HETATM 6927 O O    . HOH   D 3 .   ? 24.711 14.693  7.644   1.00 35.48 ?  468 HOH   A O    1 
HETATM 6928 O O    . HOH   D 3 .   ? 18.831 10.964  11.106  1.00 31.28 ?  469 HOH   A O    1 
HETATM 6929 O O    . HOH   D 3 .   ? 12.074 -13.313 16.272  1.00 53.67 ?  470 HOH   A O    1 
HETATM 6930 O O    B HOH   D 3 .   ? 12.569 -3.367  1.602   0.58 16.23 ?  471 HOH   A O    1 
HETATM 6931 O O    . HOH   D 3 .   ? 26.987 11.760  -1.362  1.00 37.36 ?  472 HOH   A O    1 
HETATM 6932 O O    . HOH   D 3 .   ? 23.446 13.731  5.471   1.00 19.19 ?  473 HOH   A O    1 
HETATM 6933 O O    . HOH   D 3 .   ? 15.981 -21.607 3.735   1.00 25.35 ?  474 HOH   A O    1 
HETATM 6934 O O    . HOH   D 3 .   ? 12.325 1.624   17.180  1.00 43.23 ?  475 HOH   A O    1 
HETATM 6935 O O    . HOH   D 3 .   ? 39.838 -7.050  -3.447  1.00 39.32 ?  476 HOH   A O    1 
HETATM 6936 O O    . HOH   D 3 .   ? 27.567 -11.430 16.455  1.00 38.80 ?  477 HOH   A O    1 
HETATM 6937 O O    . HOH   D 3 .   ? 25.848 10.948  -3.704  1.00 29.70 ?  478 HOH   A O    1 
HETATM 6938 O O    . HOH   D 3 .   ? 28.760 -4.818  -12.345 1.00 43.70 ?  479 HOH   A O    1 
HETATM 6939 O O    . HOH   D 3 .   ? 18.377 -16.278 -8.878  1.00 51.27 ?  480 HOH   A O    1 
HETATM 6940 O O    A HOH   D 3 .   ? 22.041 5.248   -5.905  0.42 27.96 ?  481 HOH   A O    1 
HETATM 6941 O O    . HOH   D 3 .   ? 16.170 -6.853  -11.975 1.00 54.36 ?  482 HOH   A O    1 
HETATM 6942 O O    . HOH   D 3 .   ? 23.198 12.028  -4.094  1.00 22.51 ?  483 HOH   A O    1 
HETATM 6943 O O    . HOH   D 3 .   ? 28.835 9.023   17.514  1.00 41.92 ?  484 HOH   A O    1 
HETATM 6944 O O    . HOH   D 3 .   ? 15.905 -17.238 -7.056  1.00 38.02 ?  485 HOH   A O    1 
HETATM 6945 O O    . HOH   D 3 .   ? 35.193 7.526   12.168  1.00 46.32 ?  486 HOH   A O    1 
HETATM 6946 O O    . HOH   D 3 .   ? 41.082 -3.949  -0.352  1.00 35.93 ?  487 HOH   A O    1 
HETATM 6947 O O    . HOH   D 3 .   ? 16.891 -20.479 16.172  1.00 35.21 ?  488 HOH   A O    1 
HETATM 6948 O O    . HOH   D 3 .   ? 30.795 0.750   19.130  1.00 41.45 ?  489 HOH   A O    1 
HETATM 6949 O O    . HOH   D 3 .   ? 17.422 -18.781 19.802  1.00 49.26 ?  490 HOH   A O    1 
HETATM 6950 O O    . HOH   D 3 .   ? 20.717 -15.902 -7.571  1.00 31.83 ?  491 HOH   A O    1 
HETATM 6951 O O    . HOH   D 3 .   ? 44.529 10.479  -1.597  1.00 34.62 ?  492 HOH   A O    1 
HETATM 6952 O O    . HOH   D 3 .   ? 14.129 -10.337 -10.996 1.00 40.87 ?  493 HOH   A O    1 
HETATM 6953 O O    . HOH   D 3 .   ? 28.905 -8.046  -15.267 1.00 55.80 ?  494 HOH   A O    1 
HETATM 6954 O O    . HOH   D 3 .   ? 39.226 2.436   7.264   1.00 32.93 ?  495 HOH   A O    1 
HETATM 6955 O O    . HOH   D 3 .   ? 31.701 -0.624  -10.577 1.00 25.18 ?  496 HOH   A O    1 
HETATM 6956 O O    . HOH   D 3 .   ? 23.259 -12.830 19.288  1.00 55.58 ?  497 HOH   A O    1 
HETATM 6957 O O    . HOH   D 3 .   ? 41.732 9.426   -3.987  1.00 30.08 ?  498 HOH   A O    1 
HETATM 6958 O O    . HOH   D 3 .   ? 13.826 -25.166 8.953   1.00 38.91 ?  499 HOH   A O    1 
HETATM 6959 O O    . HOH   D 3 .   ? 18.582 -23.202 1.911   1.00 47.83 ?  500 HOH   A O    1 
HETATM 6960 O O    . HOH   D 3 .   ? 40.627 -0.266  -7.801  1.00 33.15 ?  501 HOH   A O    1 
HETATM 6961 O O    . HOH   D 3 .   ? 20.180 -22.305 4.202   1.00 31.93 ?  502 HOH   A O    1 
HETATM 6962 O O    . HOH   D 3 .   ? 16.319 -23.415 5.881   1.00 31.45 ?  503 HOH   A O    1 
HETATM 6963 O O    . HOH   D 3 .   ? 30.807 5.802   -14.794 1.00 36.75 ?  504 HOH   A O    1 
HETATM 6964 O O    B HOH   D 3 .   ? 14.620 7.995   4.998   0.58 21.01 ?  505 HOH   A O    1 
HETATM 6965 O O    B HOH   D 3 .   ? 10.368 -0.318  -1.121  0.58 22.52 ?  506 HOH   A O    1 
HETATM 6966 O O    . HOH   D 3 .   ? 23.370 -23.817 1.653   1.00 33.11 ?  507 HOH   A O    1 
HETATM 6967 O O    . HOH   D 3 .   ? 30.816 -5.875  -11.985 1.00 51.35 ?  508 HOH   A O    1 
HETATM 6968 O O    . HOH   D 3 .   ? 37.452 -6.622  7.492   1.00 24.75 ?  509 HOH   A O    1 
HETATM 6969 O O    B HOH   D 3 .   ? 8.975  4.986   7.911   0.58 26.30 ?  510 HOH   A O    1 
HETATM 6970 O O    . HOH   D 3 .   ? 39.570 -0.023  6.572   1.00 31.24 ?  511 HOH   A O    1 
HETATM 6971 O O    . HOH   D 3 .   ? 8.127  -2.946  -5.721  1.00 61.07 ?  512 HOH   A O    1 
HETATM 6972 O O    . HOH   D 3 .   ? 29.018 14.494  0.776   1.00 57.91 ?  513 HOH   A O    1 
HETATM 6973 O O    . HOH   D 3 .   ? 37.958 14.019  6.626   1.00 27.60 ?  514 HOH   A O    1 
HETATM 6974 O O    B HOH   D 3 .   ? 7.466  5.687   5.488   0.58 29.71 ?  515 HOH   A O    1 
HETATM 6975 O O    . HOH   D 3 .   ? 22.154 -24.028 4.478   1.00 28.88 ?  516 HOH   A O    1 
HETATM 6976 O O    . HOH   D 3 .   ? 36.558 -6.431  10.221  1.00 46.69 ?  517 HOH   A O    1 
HETATM 6977 O O    . HOH   D 3 .   ? 17.226 -7.337  -14.158 1.00 54.08 ?  518 HOH   A O    1 
HETATM 6978 O O    A HOH   D 3 .   ? 14.919 8.656   4.807   0.42 24.70 ?  519 HOH   A O    1 
HETATM 6979 O O    . HOH   D 3 .   ? 24.096 9.051   -7.198  1.00 48.44 ?  520 HOH   A O    1 
HETATM 6980 O O    . HOH   D 3 .   ? 15.823 -12.296 27.318  1.00 48.07 ?  521 HOH   A O    1 
HETATM 6981 O O    . HOH   D 3 .   ? 16.358 -21.124 18.737  1.00 43.58 ?  522 HOH   A O    1 
HETATM 6982 O O    B HOH   D 3 .   ? 7.993  7.077   2.263   0.58 25.96 ?  523 HOH   A O    1 
HETATM 6983 O O    . HOH   D 3 .   ? 14.760 -22.729 19.853  1.00 38.75 ?  524 HOH   A O    1 
HETATM 6984 O O    . HOH   E 3 .   ? 29.934 -22.421 5.518   1.00 20.90 ?  201 HOH   B O    1 
HETATM 6985 O O    . HOH   E 3 .   ? 41.737 -36.047 -17.143 1.00 33.64 ?  202 HOH   B O    1 
HETATM 6986 O O    . HOH   E 3 .   ? 27.752 -29.166 -1.813  1.00 33.87 ?  203 HOH   B O    1 
HETATM 6987 O O    . HOH   E 3 .   ? 59.270 -18.735 6.787   1.00 36.87 ?  204 HOH   B O    1 
HETATM 6988 O O    . HOH   E 3 .   ? 38.048 -39.452 -0.160  1.00 40.67 ?  205 HOH   B O    1 
HETATM 6989 O O    . HOH   E 3 .   ? 49.487 -22.748 -19.704 1.00 48.84 ?  206 HOH   B O    1 
HETATM 6990 O O    . HOH   E 3 .   ? 54.578 -9.478  -8.747  1.00 19.29 ?  207 HOH   B O    1 
HETATM 6991 O O    . HOH   E 3 .   ? 30.053 -26.286 4.098   1.00 27.11 ?  208 HOH   B O    1 
HETATM 6992 O O    . HOH   E 3 .   ? 57.814 -24.540 5.082   1.00 41.88 ?  209 HOH   B O    1 
HETATM 6993 O O    . HOH   E 3 .   ? 47.507 -7.437  -3.889  1.00 42.72 ?  210 HOH   B O    1 
HETATM 6994 O O    . HOH   E 3 .   ? 53.101 -13.543 -20.314 1.00 32.81 ?  211 HOH   B O    1 
HETATM 6995 O O    . HOH   E 3 .   ? 48.158 -6.978  15.483  1.00 27.28 ?  212 HOH   B O    1 
HETATM 6996 O O    . HOH   E 3 .   ? 50.297 -3.388  7.074   1.00 32.24 ?  213 HOH   B O    1 
HETATM 6997 O O    . HOH   E 3 .   ? 27.923 -41.902 -15.096 1.00 37.51 ?  214 HOH   B O    1 
HETATM 6998 O O    . HOH   E 3 .   ? 58.340 -12.894 8.383   1.00 29.91 ?  215 HOH   B O    1 
HETATM 6999 O O    . HOH   E 3 .   ? 41.482 -7.748  5.376   1.00 37.83 ?  216 HOH   B O    1 
HETATM 7000 O O    . HOH   E 3 .   ? 30.258 -41.046 -8.049  1.00 17.50 ?  217 HOH   B O    1 
HETATM 7001 O O    . HOH   E 3 .   ? 44.588 -7.204  1.999   1.00 36.85 ?  218 HOH   B O    1 
HETATM 7002 O O    . HOH   E 3 .   ? 31.008 -28.729 4.363   1.00 29.90 ?  219 HOH   B O    1 
HETATM 7003 O O    . HOH   E 3 .   ? 34.616 -36.420 -7.146  1.00 18.71 ?  220 HOH   B O    1 
HETATM 7004 O O    . HOH   E 3 .   ? 26.596 -19.330 -1.773  1.00 14.16 ?  221 HOH   B O    1 
HETATM 7005 O O    . HOH   E 3 .   ? 44.989 -43.595 -10.476 1.00 28.42 ?  222 HOH   B O    1 
HETATM 7006 O O    . HOH   E 3 .   ? 56.774 -30.844 -7.796  1.00 28.54 ?  223 HOH   B O    1 
HETATM 7007 O O    . HOH   E 3 .   ? 56.508 -19.790 7.154   1.00 30.67 ?  224 HOH   B O    1 
HETATM 7008 O O    . HOH   E 3 .   ? 57.484 -16.332 -12.253 1.00 17.64 ?  225 HOH   B O    1 
HETATM 7009 O O    . HOH   E 3 .   ? 29.725 -34.037 -0.368  1.00 33.82 ?  226 HOH   B O    1 
HETATM 7010 O O    . HOH   E 3 .   ? 51.010 -39.978 -8.129  1.00 33.60 ?  227 HOH   B O    1 
HETATM 7011 O O    . HOH   E 3 .   ? 46.458 -1.579  13.133  1.00 27.17 ?  228 HOH   B O    1 
HETATM 7012 O O    . HOH   E 3 .   ? 41.537 -39.224 -14.810 1.00 23.81 ?  229 HOH   B O    1 
HETATM 7013 O O    . HOH   E 3 .   ? 50.812 -6.127  0.161   1.00 26.82 ?  230 HOH   B O    1 
HETATM 7014 O O    . HOH   E 3 .   ? 35.042 -24.635 13.890  1.00 32.32 ?  231 HOH   B O    1 
HETATM 7015 O O    . HOH   E 3 .   ? 55.562 -16.599 -14.341 1.00 32.91 ?  232 HOH   B O    1 
HETATM 7016 O O    . HOH   E 3 .   ? 45.212 -34.932 6.775   1.00 40.32 ?  233 HOH   B O    1 
HETATM 7017 O O    . HOH   E 3 .   ? 41.506 -9.627  13.046  1.00 22.32 ?  234 HOH   B O    1 
HETATM 7018 O O    . HOH   E 3 .   ? 35.215 -8.032  -2.923  1.00 18.27 ?  235 HOH   B O    1 
HETATM 7019 O O    . HOH   E 3 .   ? 28.556 -19.680 -13.172 1.00 25.70 ?  236 HOH   B O    1 
HETATM 7020 O O    . HOH   E 3 .   ? 44.597 -27.777 -0.656  1.00 22.20 ?  237 HOH   B O    1 
HETATM 7021 O O    . HOH   E 3 .   ? 57.275 -26.889 -7.594  1.00 42.07 ?  238 HOH   B O    1 
HETATM 7022 O O    . HOH   E 3 .   ? 37.223 -19.682 -18.069 1.00 44.55 ?  239 HOH   B O    1 
HETATM 7023 O O    . HOH   E 3 .   ? 36.038 -43.437 -8.370  1.00 43.51 ?  240 HOH   B O    1 
HETATM 7024 O O    . HOH   E 3 .   ? 51.747 -6.527  4.323   1.00 20.29 ?  241 HOH   B O    1 
HETATM 7025 O O    . HOH   E 3 .   ? 25.405 -25.864 -1.204  1.00 33.06 ?  242 HOH   B O    1 
HETATM 7026 O O    . HOH   E 3 .   ? 38.594 -11.085 -2.268  1.00 19.10 ?  243 HOH   B O    1 
HETATM 7027 O O    . HOH   E 3 .   ? 32.818 -43.840 -11.302 1.00 21.69 ?  244 HOH   B O    1 
HETATM 7028 O O    . HOH   E 3 .   ? 39.429 -10.794 6.085   1.00 22.89 ?  245 HOH   B O    1 
HETATM 7029 O O    . HOH   E 3 .   ? 50.870 -13.020 -0.470  1.00 11.56 ?  246 HOH   B O    1 
HETATM 7030 O O    . HOH   E 3 .   ? 57.748 -24.425 -3.782  1.00 21.48 ?  247 HOH   B O    1 
HETATM 7031 O O    . HOH   E 3 .   ? 42.746 -22.874 3.873   1.00 11.53 ?  248 HOH   B O    1 
HETATM 7032 O O    . HOH   E 3 .   ? 42.675 -25.385 2.668   1.00 15.22 ?  249 HOH   B O    1 
HETATM 7033 O O    . HOH   E 3 .   ? 39.639 -11.142 0.280   1.00 16.14 ?  250 HOH   B O    1 
HETATM 7034 O O    . HOH   E 3 .   ? 34.388 -18.465 11.448  1.00 25.43 ?  251 HOH   B O    1 
HETATM 7035 O O    . HOH   E 3 .   ? 41.965 -23.514 9.318   1.00 18.47 ?  252 HOH   B O    1 
HETATM 7036 O O    . HOH   E 3 .   ? 40.663 -16.074 14.100  1.00 23.98 ?  253 HOH   B O    1 
HETATM 7037 O O    . HOH   E 3 .   ? 43.124 -43.294 -8.156  1.00 28.38 ?  254 HOH   B O    1 
HETATM 7038 O O    . HOH   E 3 .   ? 40.482 -12.800 -11.529 1.00 14.83 ?  255 HOH   B O    1 
HETATM 7039 O O    . HOH   E 3 .   ? 48.099 -22.776 5.816   1.00 17.34 ?  256 HOH   B O    1 
HETATM 7040 O O    . HOH   E 3 .   ? 48.708 -36.545 -15.529 1.00 45.09 ?  257 HOH   B O    1 
HETATM 7041 O O    . HOH   E 3 .   ? 33.650 -16.927 8.088   1.00 19.29 ?  258 HOH   B O    1 
HETATM 7042 O O    . HOH   E 3 .   ? 49.854 -0.532  10.144  1.00 28.04 ?  259 HOH   B O    1 
HETATM 7043 O O    . HOH   E 3 .   ? 41.221 -5.635  11.534  1.00 48.66 ?  260 HOH   B O    1 
HETATM 7044 O O    . HOH   E 3 .   ? 29.804 -25.236 -10.763 1.00 17.07 ?  261 HOH   B O    1 
HETATM 7045 O O    . HOH   E 3 .   ? 51.627 -13.811 10.979  1.00 25.63 ?  262 HOH   B O    1 
HETATM 7046 O O    . HOH   E 3 .   ? 30.957 -15.713 2.675   1.00 13.26 ?  263 HOH   B O    1 
HETATM 7047 O O    . HOH   E 3 .   ? 30.624 -42.278 -10.609 1.00 30.82 ?  264 HOH   B O    1 
HETATM 7048 O O    . HOH   E 3 .   ? 58.305 -10.639 -4.087  1.00 20.46 ?  265 HOH   B O    1 
HETATM 7049 O O    . HOH   E 3 .   ? 28.547 -30.900 -14.795 1.00 30.05 ?  266 HOH   B O    1 
HETATM 7050 O O    . HOH   E 3 .   ? 56.260 -23.655 -14.685 1.00 30.31 ?  267 HOH   B O    1 
HETATM 7051 O O    . HOH   E 3 .   ? 43.217 -32.415 -17.037 1.00 24.83 ?  268 HOH   B O    1 
HETATM 7052 O O    . HOH   E 3 .   ? 49.399 -28.758 -6.877  1.00 15.71 ?  269 HOH   B O    1 
HETATM 7053 O O    . HOH   E 3 .   ? 34.586 -12.807 2.609   1.00 21.37 ?  270 HOH   B O    1 
HETATM 7054 O O    . HOH   E 3 .   ? 57.047 -8.611  8.355   1.00 19.22 ?  271 HOH   B O    1 
HETATM 7055 O O    . HOH   E 3 .   ? 27.214 -31.839 -9.951  1.00 19.60 ?  272 HOH   B O    1 
HETATM 7056 O O    . HOH   E 3 .   ? 57.617 -9.258  1.393   1.00 19.39 ?  273 HOH   B O    1 
HETATM 7057 O O    . HOH   E 3 .   ? 50.019 -24.743 5.740   1.00 32.69 ?  274 HOH   B O    1 
HETATM 7058 O O    . HOH   E 3 .   ? 43.489 -15.844 -12.188 1.00 14.13 ?  275 HOH   B O    1 
HETATM 7059 O O    . HOH   E 3 .   ? 42.468 -9.942  9.283   1.00 19.81 ?  276 HOH   B O    1 
HETATM 7060 O O    . HOH   E 3 .   ? 46.683 -31.298 -4.765  1.00 18.90 ?  277 HOH   B O    1 
HETATM 7061 O O    . HOH   E 3 .   ? 47.043 -29.532 9.775   1.00 32.99 ?  278 HOH   B O    1 
HETATM 7062 O O    . HOH   E 3 .   ? 48.499 -25.059 3.099   1.00 13.02 ?  279 HOH   B O    1 
HETATM 7063 O O    . HOH   E 3 .   ? 31.882 -17.898 -14.530 1.00 29.74 ?  280 HOH   B O    1 
HETATM 7064 O O    . HOH   E 3 .   ? 51.740 -5.919  -7.933  1.00 42.01 ?  281 HOH   B O    1 
HETATM 7065 O O    . HOH   E 3 .   ? 39.006 -11.856 12.400  1.00 35.71 ?  282 HOH   B O    1 
HETATM 7066 O O    . HOH   E 3 .   ? 42.483 -34.736 3.805   1.00 26.60 ?  283 HOH   B O    1 
HETATM 7067 O O    . HOH   E 3 .   ? 42.948 -20.312 -20.700 1.00 43.20 ?  284 HOH   B O    1 
HETATM 7068 O O    . HOH   E 3 .   ? 28.053 -22.886 -7.951  1.00 17.86 ?  285 HOH   B O    1 
HETATM 7069 O O    . HOH   E 3 .   ? 48.069 -24.612 -17.770 1.00 32.33 ?  286 HOH   B O    1 
HETATM 7070 O O    . HOH   E 3 .   ? 36.939 -12.787 -1.541  1.00 26.47 ?  287 HOH   B O    1 
HETATM 7071 O O    . HOH   E 3 .   ? 35.024 -33.396 -19.132 1.00 29.17 ?  288 HOH   B O    1 
HETATM 7072 O O    . HOH   E 3 .   ? 28.297 -34.364 -9.346  1.00 16.91 ?  289 HOH   B O    1 
HETATM 7073 O O    . HOH   E 3 .   ? 52.668 -10.394 12.933  1.00 22.05 ?  290 HOH   B O    1 
HETATM 7074 O O    . HOH   E 3 .   ? 33.649 -15.368 -13.951 1.00 21.61 ?  291 HOH   B O    1 
HETATM 7075 O O    . HOH   E 3 .   ? 47.143 -34.034 -4.600  1.00 17.57 ?  292 HOH   B O    1 
HETATM 7076 O O    . HOH   E 3 .   ? 48.816 -20.040 5.937   1.00 13.47 ?  293 HOH   B O    1 
HETATM 7077 O O    . HOH   E 3 .   ? 27.657 -26.694 -15.549 1.00 34.37 ?  294 HOH   B O    1 
HETATM 7078 O O    . HOH   E 3 .   ? 51.286 -37.647 -9.559  1.00 27.02 ?  295 HOH   B O    1 
HETATM 7079 O O    . HOH   E 3 .   ? 42.493 -9.969  -14.888 1.00 34.14 ?  296 HOH   B O    1 
HETATM 7080 O O    . HOH   E 3 .   ? 37.578 -17.965 13.109  1.00 31.62 ?  297 HOH   B O    1 
HETATM 7081 O O    . HOH   E 3 .   ? 52.627 -35.763 -8.646  1.00 30.38 ?  298 HOH   B O    1 
HETATM 7082 O O    . HOH   E 3 .   ? 45.362 -33.436 -15.929 1.00 24.74 ?  299 HOH   B O    1 
HETATM 7083 O O    . HOH   E 3 .   ? 45.954 -40.450 -3.531  1.00 31.14 ?  300 HOH   B O    1 
HETATM 7084 O O    . HOH   E 3 .   ? 26.058 -21.471 -3.448  1.00 16.95 ?  301 HOH   B O    1 
HETATM 7085 O O    . HOH   E 3 .   ? 57.186 -12.078 12.387  1.00 39.27 ?  302 HOH   B O    1 
HETATM 7086 O O    . HOH   E 3 .   ? 44.737 -27.480 2.049   1.00 15.85 ?  303 HOH   B O    1 
HETATM 7087 O O    . HOH   E 3 .   ? 38.483 -9.430  -13.295 1.00 29.94 ?  304 HOH   B O    1 
HETATM 7088 O O    . HOH   E 3 .   ? 59.893 -15.323 8.184   1.00 31.54 ?  305 HOH   B O    1 
HETATM 7089 O O    . HOH   E 3 .   ? 42.899 -12.238 -18.499 1.00 29.40 ?  306 HOH   B O    1 
HETATM 7090 O O    . HOH   E 3 .   ? 35.157 -33.592 4.630   1.00 29.93 ?  307 HOH   B O    1 
HETATM 7091 O O    . HOH   E 3 .   ? 40.386 -10.889 -9.516  1.00 17.23 ?  308 HOH   B O    1 
HETATM 7092 O O    . HOH   E 3 .   ? 44.102 -29.404 -4.636  1.00 23.63 ?  309 HOH   B O    1 
HETATM 7093 O O    . HOH   E 3 .   ? 53.226 -16.080 -12.745 1.00 27.12 ?  310 HOH   B O    1 
HETATM 7094 O O    . HOH   E 3 .   ? 37.376 -35.683 7.256   1.00 32.94 ?  311 HOH   B O    1 
HETATM 7095 O O    . HOH   E 3 .   ? 37.988 -10.276 -10.757 1.00 17.91 ?  312 HOH   B O    1 
HETATM 7096 O O    . HOH   E 3 .   ? 62.809 -13.580 4.693   1.00 28.46 ?  313 HOH   B O    1 
HETATM 7097 O O    . HOH   E 3 .   ? 52.600 -29.333 -13.032 1.00 24.30 ?  314 HOH   B O    1 
HETATM 7098 O O    . HOH   E 3 .   ? 43.643 -15.414 18.079  1.00 30.85 ?  315 HOH   B O    1 
HETATM 7099 O O    . HOH   E 3 .   ? 53.557 -30.248 4.570   1.00 18.69 ?  316 HOH   B O    1 
HETATM 7100 O O    . HOH   E 3 .   ? 32.873 -34.631 -5.832  1.00 17.55 ?  317 HOH   B O    1 
HETATM 7101 O O    . HOH   E 3 .   ? 38.436 -12.646 7.949   1.00 17.53 ?  318 HOH   B O    1 
HETATM 7102 O O    . HOH   E 3 .   ? 41.865 -8.091  1.363   1.00 23.38 ?  319 HOH   B O    1 
HETATM 7103 O O    . HOH   E 3 .   ? 48.748 -12.113 -14.235 1.00 28.07 ?  320 HOH   B O    1 
HETATM 7104 O O    . HOH   E 3 .   ? 51.420 -33.049 -10.778 1.00 42.62 ?  321 HOH   B O    1 
HETATM 7105 O O    . HOH   E 3 .   ? 53.740 -12.588 -22.212 1.00 35.26 ?  322 HOH   B O    1 
HETATM 7106 O O    . HOH   E 3 .   ? 43.307 -21.424 10.701  1.00 16.12 ?  323 HOH   B O    1 
HETATM 7107 O O    . HOH   E 3 .   ? 37.190 -30.667 -20.953 1.00 33.44 ?  324 HOH   B O    1 
HETATM 7108 O O    . HOH   E 3 .   ? 44.204 -1.760  7.705   1.00 47.11 ?  325 HOH   B O    1 
HETATM 7109 O O    . HOH   E 3 .   ? 26.454 -21.052 -6.195  1.00 16.70 ?  326 HOH   B O    1 
HETATM 7110 O O    . HOH   E 3 .   ? 36.836 -12.422 4.256   1.00 17.34 ?  327 HOH   B O    1 
HETATM 7111 O O    . HOH   E 3 .   ? 57.611 -21.976 3.355   1.00 32.58 ?  328 HOH   B O    1 
HETATM 7112 O O    . HOH   E 3 .   ? 44.736 -24.594 9.584   1.00 21.97 ?  329 HOH   B O    1 
HETATM 7113 O O    . HOH   E 3 .   ? 27.818 -14.792 -9.472  1.00 36.07 ?  330 HOH   B O    1 
HETATM 7114 O O    . HOH   E 3 .   ? 48.187 -32.732 -16.623 1.00 44.89 ?  331 HOH   B O    1 
HETATM 7115 O O    . HOH   E 3 .   ? 47.325 -24.501 8.206   1.00 27.53 ?  332 HOH   B O    1 
HETATM 7116 O O    . HOH   E 3 .   ? 33.751 -31.139 11.060  1.00 38.45 ?  333 HOH   B O    1 
HETATM 7117 O O    . HOH   E 3 .   ? 41.337 -24.513 15.794  1.00 48.67 ?  334 HOH   B O    1 
HETATM 7118 O O    . HOH   E 3 .   ? 63.089 -20.178 -0.836  1.00 39.24 ?  335 HOH   B O    1 
HETATM 7119 O O    . HOH   E 3 .   ? 60.036 -17.320 -10.519 1.00 35.72 ?  336 HOH   B O    1 
HETATM 7120 O O    . HOH   E 3 .   ? 43.198 -34.668 0.114   1.00 22.86 ?  337 HOH   B O    1 
HETATM 7121 O O    . HOH   E 3 .   ? 45.808 -36.310 -16.118 1.00 36.51 ?  338 HOH   B O    1 
HETATM 7122 O O    . HOH   E 3 .   ? 42.939 -43.547 -14.287 1.00 45.05 ?  339 HOH   B O    1 
HETATM 7123 O O    . HOH   E 3 .   ? 37.137 -15.197 -16.551 1.00 40.04 ?  340 HOH   B O    1 
HETATM 7124 O O    . HOH   E 3 .   ? 47.563 -27.459 2.035   1.00 15.05 ?  341 HOH   B O    1 
HETATM 7125 O O    . HOH   E 3 .   ? 28.912 -42.913 -12.350 1.00 34.69 ?  342 HOH   B O    1 
HETATM 7126 O O    . HOH   E 3 .   ? 39.616 -23.545 -20.305 1.00 38.10 ?  343 HOH   B O    1 
HETATM 7127 O O    . HOH   E 3 .   ? 46.959 -19.939 12.199  1.00 29.86 ?  344 HOH   B O    1 
HETATM 7128 O O    . HOH   E 3 .   ? 37.115 -45.267 -9.689  1.00 37.52 ?  345 HOH   B O    1 
HETATM 7129 O O    . HOH   E 3 .   ? 34.563 -10.306 7.671   1.00 23.17 ?  346 HOH   B O    1 
HETATM 7130 O O    . HOH   E 3 .   ? 33.122 -14.680 1.104   1.00 19.02 ?  347 HOH   B O    1 
HETATM 7131 O O    . HOH   E 3 .   ? 39.813 -44.271 -11.154 1.00 42.29 ?  348 HOH   B O    1 
HETATM 7132 O O    . HOH   E 3 .   ? 38.718 -22.477 15.070  1.00 47.27 ?  349 HOH   B O    1 
HETATM 7133 O O    . HOH   E 3 .   ? 38.586 -12.195 -16.208 1.00 42.50 ?  350 HOH   B O    1 
HETATM 7134 O O    . HOH   E 3 .   ? 40.450 -43.521 -9.069  1.00 27.85 ?  351 HOH   B O    1 
HETATM 7135 O O    . HOH   E 3 .   ? 44.258 -37.440 -17.682 1.00 36.04 ?  352 HOH   B O    1 
HETATM 7136 O O    . HOH   E 3 .   ? 62.666 -20.015 -4.799  1.00 53.13 ?  353 HOH   B O    1 
HETATM 7137 O O    . HOH   E 3 .   ? 27.826 -26.637 -0.541  1.00 30.40 ?  354 HOH   B O    1 
HETATM 7138 O O    . HOH   E 3 .   ? 23.359 -23.671 6.829   1.00 31.87 ?  355 HOH   B O    1 
HETATM 7139 O O    . HOH   E 3 .   ? 33.948 -9.279  -8.895  1.00 28.75 ?  356 HOH   B O    1 
HETATM 7140 O O    . HOH   E 3 .   ? 55.830 -8.259  10.808  1.00 23.36 ?  357 HOH   B O    1 
HETATM 7141 O O    . HOH   E 3 .   ? 36.295 -8.526  -9.740  1.00 34.08 ?  358 HOH   B O    1 
HETATM 7142 O O    . HOH   E 3 .   ? 56.699 -7.260  2.913   1.00 28.03 ?  359 HOH   B O    1 
HETATM 7143 O O    . HOH   E 3 .   ? 34.180 -7.728  11.438  1.00 43.28 ?  360 HOH   B O    1 
HETATM 7144 O O    . HOH   E 3 .   ? 56.984 -21.593 -16.445 1.00 42.10 ?  361 HOH   B O    1 
HETATM 7145 O O    . HOH   E 3 .   ? 61.617 -19.910 1.790   1.00 38.12 ?  362 HOH   B O    1 
HETATM 7146 O O    . HOH   E 3 .   ? 27.262 -26.012 -11.333 1.00 34.30 ?  363 HOH   B O    1 
HETATM 7147 O O    . HOH   E 3 .   ? 40.300 -8.815  9.868   1.00 36.99 ?  364 HOH   B O    1 
HETATM 7148 O O    . HOH   E 3 .   ? 43.275 -12.757 -21.290 1.00 42.16 ?  365 HOH   B O    1 
HETATM 7149 O O    . HOH   E 3 .   ? 40.377 -11.350 -13.956 1.00 30.72 ?  366 HOH   B O    1 
HETATM 7150 O O    . HOH   E 3 .   ? 32.674 -23.568 14.066  1.00 41.33 ?  367 HOH   B O    1 
HETATM 7151 O O    . HOH   E 3 .   ? 59.035 -10.459 9.216   1.00 42.91 ?  368 HOH   B O    1 
HETATM 7152 O O    . HOH   E 3 .   ? 36.248 -8.643  8.954   1.00 33.12 ?  369 HOH   B O    1 
HETATM 7153 O O    . HOH   E 3 .   ? 48.461 -26.444 8.849   1.00 42.03 ?  370 HOH   B O    1 
HETATM 7154 O O    . HOH   E 3 .   ? 54.402 -5.803  2.857   1.00 35.83 ?  371 HOH   B O    1 
HETATM 7155 O O    . HOH   E 3 .   ? 39.992 -6.964  7.777   1.00 41.20 ?  372 HOH   B O    1 
HETATM 7156 O O    . HOH   E 3 .   ? 41.985 -10.060 -17.501 1.00 52.93 ?  373 HOH   B O    1 
HETATM 7157 O O    . HOH   E 3 .   ? 56.148 -7.831  -0.618  1.00 33.71 ?  374 HOH   B O    1 
HETATM 7158 O O    . HOH   E 3 .   ? 52.112 -12.965 13.309  1.00 26.74 ?  375 HOH   B O    1 
HETATM 7159 O O    . HOH   E 3 .   ? 41.987 -6.740  -4.938  1.00 46.18 ?  376 HOH   B O    1 
HETATM 7160 O O    . HOH   E 3 .   ? 63.029 -12.280 6.912   1.00 40.89 ?  377 HOH   B O    1 
HETATM 7161 O O    . HOH   E 3 .   ? 38.173 -10.502 9.981   1.00 27.86 ?  378 HOH   B O    1 
HETATM 7162 O O    . HOH   E 3 .   ? 36.615 -22.819 13.307  1.00 28.78 ?  379 HOH   B O    1 
HETATM 7163 O O    . HOH   E 3 .   ? 42.813 -17.172 -23.174 1.00 43.11 ?  380 HOH   B O    1 
HETATM 7164 O O    . HOH   E 3 .   ? 40.257 -7.643  3.141   1.00 38.96 ?  381 HOH   B O    1 
HETATM 7165 O O    . HOH   E 3 .   ? 39.715 -14.107 15.613  1.00 46.75 ?  382 HOH   B O    1 
HETATM 7166 O O    . HOH   E 3 .   ? 44.112 -5.616  -3.501  1.00 42.25 ?  383 HOH   B O    1 
HETATM 7167 O O    . HOH   E 3 .   ? 60.528 -22.265 2.862   1.00 41.90 ?  384 HOH   B O    1 
HETATM 7168 O O    . HOH   E 3 .   ? 52.990 -29.897 7.214   1.00 23.66 ?  385 HOH   B O    1 
HETATM 7169 O O    . HOH   E 3 .   ? 46.851 -5.459  2.847   1.00 37.08 ?  386 HOH   B O    1 
HETATM 7170 O O    . HOH   E 3 .   ? 35.394 -20.307 13.294  1.00 34.93 ?  387 HOH   B O    1 
HETATM 7171 O O    . HOH   E 3 .   ? 41.070 -9.788  15.831  1.00 47.29 ?  388 HOH   B O    1 
HETATM 7172 O O    . HOH   E 3 .   ? 25.947 -18.939 -11.938 1.00 44.27 ?  389 HOH   B O    1 
HETATM 7173 O O    . HOH   E 3 .   ? 35.431 -33.694 7.371   1.00 43.99 ?  390 HOH   B O    1 
HETATM 7174 O O    . HOH   E 3 .   ? 24.047 -20.940 -7.721  1.00 28.51 ?  391 HOH   B O    1 
HETATM 7175 O O    . HOH   E 3 .   ? 40.885 -6.577  -0.832  1.00 24.71 ?  392 HOH   B O    1 
HETATM 7176 O O    . HOH   E 3 .   ? 44.209 -31.846 -3.798  1.00 34.80 ?  393 HOH   B O    1 
HETATM 7177 O O    . HOH   E 3 .   ? 28.076 -27.053 2.342   1.00 33.02 ?  394 HOH   B O    1 
HETATM 7178 O O    . HOH   E 3 .   ? 26.721 -28.002 -13.456 1.00 35.91 ?  395 HOH   B O    1 
HETATM 7179 O O    . HOH   E 3 .   ? 50.715 -30.902 8.694   1.00 28.54 ?  396 HOH   B O    1 
HETATM 7180 O O    . HOH   E 3 .   ? 34.453 -33.472 9.664   1.00 37.74 ?  397 HOH   B O    1 
HETATM 7181 O O    . HOH   E 3 .   ? 24.713 -20.657 -10.534 1.00 40.87 ?  398 HOH   B O    1 
HETATM 7182 O O    . HOH   E 3 .   ? 26.903 -30.672 -12.583 1.00 28.33 ?  399 HOH   B O    1 
HETATM 7183 O O    . HOH   E 3 .   ? 57.712 -6.563  -2.390  1.00 35.02 ?  400 HOH   B O    1 
HETATM 7184 O O    . HOH   E 3 .   ? 45.729 -20.085 15.314  1.00 45.56 ?  401 HOH   B O    1 
HETATM 7185 O O    . HOH   E 3 .   ? 40.978 -11.785 -22.289 1.00 41.56 ?  402 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.7015 0.7040 0.8145 -0.0002 -0.0122 0.0509  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.7190 0.7056 0.8232 -0.0010 -0.0160 0.0681  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6980 0.7004 0.8057 -0.0004 -0.0122 0.0512  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.7148 0.7015 0.8125 -0.0013 -0.0163 0.0682  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.6801 0.6843 0.7682 -0.0042 -0.0127 0.0526  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6958 0.6830 0.7680 -0.0058 -0.0170 0.0694  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.6824 0.6860 0.7764 -0.0034 -0.0137 0.0545  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6992 0.6853 0.7777 -0.0052 -0.0194 0.0716  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.7091 0.7103 0.8272 0.0022  -0.0106 0.0513  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.7260 0.7126 0.8373 0.0018  -0.0141 0.0683  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.7121 0.7126 0.8366 0.0024  -0.0099 0.0520  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.7293 0.7156 0.8467 0.0018  -0.0131 0.0696  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.7135 0.7143 0.8370 0.0040  -0.0103 0.0519  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.7302 0.7169 0.8475 0.0041  -0.0133 0.0693  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.6566 0.6638 0.7092 -0.0093 -0.0108 0.0522  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.6697 0.6588 0.7002 -0.0118 -0.0136 0.0692  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.6287 0.6389 0.6431 -0.0156 -0.0088 0.0505  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.6402 0.6303 0.6248 -0.0194 -0.0114 0.0662  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.5867 0.6025 0.6040 -0.0246 0.0026  0.0392  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.5973 0.5918 0.5808 -0.0319 0.0097  0.0528  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.5889 0.6028 0.6104 -0.0234 0.0012  0.0396  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.6009 0.5930 0.5861 -0.0316 0.0072  0.0531  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.6390 0.6462 0.6137 -0.0140 -0.0174 0.0592  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.6507 0.6361 0.5887 -0.0168 -0.0290 0.0769  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.6460 0.6492 0.5874 -0.0137 -0.0232 0.0657  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.6592 0.6373 0.5560 -0.0159 -0.0408 0.0856  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.6490 0.6485 0.5746 -0.0127 -0.0253 0.0686  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.6640 0.6355 0.5416 -0.0145 -0.0443 0.0900  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.6475 0.6514 0.5766 -0.0147 -0.0250 0.0693  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.6602 0.6385 0.5442 -0.0165 -0.0440 0.0903  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.5401 0.5640 0.5524 -0.0352 0.0137  0.0283  5   SER   A N   
60   N N   B SER   A 5   ? 0.5480 0.5499 0.5266 -0.0453 0.0313  0.0394  5   SER   A N   
61   C CA  A SER   A 5   ? 0.4928 0.5244 0.4993 -0.0430 0.0257  0.0199  5   SER   A CA  
62   C CA  B SER   A 5   ? 0.4975 0.5080 0.4751 -0.0580 0.0532  0.0286  5   SER   A CA  
63   C C   A SER   A 5   ? 0.4405 0.4800 0.4325 -0.0471 0.0395  0.0148  5   SER   A C   
64   C C   B SER   A 5   ? 0.4409 0.4579 0.3981 -0.0669 0.0797  0.0212  5   SER   A C   
65   O O   A SER   A 5   ? 0.4438 0.4822 0.4331 -0.0454 0.0399  0.0086  5   SER   A O   
66   O O   B SER   A 5   ? 0.4476 0.4612 0.3939 -0.0655 0.0812  0.0094  5   SER   A O   
67   C CB  A SER   A 5   ? 0.4974 0.5287 0.5055 -0.0447 0.0264  0.0173  5   SER   A CB  
68   C CB  B SER   A 5   ? 0.5031 0.5153 0.4888 -0.0596 0.0529  0.0268  5   SER   A CB  
69   O OG  A SER   A 5   ? 0.5004 0.5311 0.5106 -0.0446 0.0281  0.0152  5   SER   A OG  
70   O OG  B SER   A 5   ? 0.5066 0.5201 0.5016 -0.0601 0.0539  0.0238  5   SER   A OG  
81   N N   A PHE   A 6   ? 0.3834 0.4318 0.3677 -0.0520 0.0531  0.0171  6   PHE   A N   
82   N N   B PHE   A 6   ? 0.3759 0.4028 0.3266 -0.0771 0.1047  0.0239  6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.3269 0.3826 0.3042 -0.0561 0.0619  0.0221  6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.3131 0.3453 0.2722 -0.0867 0.1172  0.0349  6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.3023 0.3687 0.2863 -0.0620 0.0762  0.0205  6   PHE   A C   
86   C C   B PHE   A 6   ? 0.3015 0.3355 0.2842 -0.0873 0.1313  0.0352  6   PHE   A C   
87   O O   A PHE   A 6   ? 0.3034 0.3712 0.2937 -0.0688 0.0791  0.0205  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.3104 0.3419 0.3127 -0.0856 0.1296  0.0492  6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.2991 0.3505 0.2639 -0.0487 0.0540  0.0249  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.2727 0.3021 0.2291 -0.0862 0.0902  0.0389  6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.2729 0.3239 0.2305 -0.0424 0.0469  0.0310  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.2382 0.2746 0.2004 -0.0746 0.0652  0.0364  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.2607 0.3109 0.2168 -0.0347 0.0399  0.0304  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.2222 0.2612 0.1925 -0.0629 0.0544  0.0334  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.2656 0.3143 0.2283 -0.0391 0.0476  0.0341  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.2356 0.2693 0.2236 -0.0696 0.0505  0.0325  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.2546 0.3033 0.2121 -0.0342 0.0410  0.0320  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.2152 0.2522 0.1927 -0.0663 0.0497  0.0308  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.2601 0.3093 0.2322 -0.0369 0.0457  0.0313  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.2300 0.2665 0.2372 -0.0679 0.0405  0.0217  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.2564 0.3049 0.2198 -0.0350 0.0431  0.0277  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.2221 0.2585 0.2173 -0.0683 0.0437  0.0173  6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.2778 0.3519 0.2698 -0.0597 0.0808  0.0201  7   SER   A N   
122  N N   B SER   A 7   ? 0.2820 0.3188 0.2788 -0.0854 0.1354  0.0213  7   SER   A N   
123  C CA  A SER   A 7   ? 0.2630 0.3413 0.2679 -0.0509 0.0754  0.0064  7   SER   A CA  
124  C CA  B SER   A 7   ? 0.2771 0.3175 0.3076 -0.0778 0.1154  -0.0079 7   SER   A CA  
125  C C   A SER   A 7   ? 0.2420 0.3104 0.2551 -0.0472 0.0840  0.0092  7   SER   A C   
126  C C   B SER   A 7   ? 0.2538 0.2879 0.2874 -0.0837 0.1176  -0.0065 7   SER   A C   
127  O O   A SER   A 7   ? 0.2476 0.3075 0.2572 -0.0476 0.0845  0.0124  7   SER   A O   
128  O O   B SER   A 7   ? 0.2568 0.2768 0.2889 -0.0926 0.1174  -0.0004 7   SER   A O   
129  C CB  A SER   A 7   ? 0.2720 0.3604 0.2719 -0.0431 0.0654  0.0008  7   SER   A CB  
130  C CB  B SER   A 7   ? 0.2964 0.3461 0.3482 -0.0657 0.1023  -0.0195 7   SER   A CB  
131  O OG  A SER   A 7   ? 0.2818 0.3745 0.2822 -0.0377 0.0523  -0.0023 7   SER   A OG  
132  O OG  B SER   A 7   ? 0.3143 0.3688 0.3910 -0.0583 0.0898  -0.0246 7   SER   A OG  
143  N N   A GLY   A 8   ? 0.2202 0.2852 0.2556 -0.0415 0.0861  0.0050  8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2342 0.2726 0.2921 -0.0787 0.1123  -0.0089 8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.1977 0.2599 0.2487 -0.0309 0.0897  0.0130  8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.2223 0.2541 0.2955 -0.0647 0.0959  0.0004  8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.1752 0.2366 0.2436 -0.0172 0.0780  0.0151  8   GLY   A C   
148  C C   B GLY   A 8   ? 0.2028 0.2324 0.2869 -0.0466 0.0808  0.0129  8   GLY   A C   
149  O O   A GLY   A 8   ? 0.1723 0.2343 0.2635 -0.0056 0.0801  -0.0054 8   GLY   A O   
150  O O   B GLY   A 8   ? 0.2004 0.2242 0.3011 -0.0377 0.0748  -0.0031 8   GLY   A O   
157  N N   A TYR   A 9   ? 0.1597 0.2163 0.2139 -0.0098 0.0674  0.0294  9   TYR   A N   
158  N N   B TYR   A 9   ? 0.1901 0.2180 0.2600 -0.0264 0.0669  0.0315  9   TYR   A N   
159  C CA  A TYR   A 9   ? 0.1421 0.2004 0.1979 -0.0117 0.0591  0.0424  9   TYR   A CA  
160  C CA  B TYR   A 9   ? 0.1713 0.2048 0.2344 -0.0175 0.0542  0.0500  9   TYR   A CA  
161  C C   A TYR   A 9   ? 0.1367 0.1867 0.2082 -0.0093 0.0546  0.0567  9   TYR   A C   
162  C C   B TYR   A 9   ? 0.1716 0.1915 0.2402 -0.0098 0.0520  0.0666  9   TYR   A C   
163  O O   A TYR   A 9   ? 0.1533 0.1994 0.2267 -0.0060 0.0431  0.0517  9   TYR   A O   
164  O O   B TYR   A 9   ? 0.1884 0.2056 0.2650 -0.0162 0.0551  0.0737  9   TYR   A O   
165  C CB  A TYR   A 9   ? 0.1382 0.2021 0.1836 -0.0083 0.0443  0.0283  9   TYR   A CB  
166  C CB  B TYR   A 9   ? 0.1565 0.2091 0.2229 -0.0056 0.0376  0.0393  9   TYR   A CB  
167  C CG  A TYR   A 9   ? 0.1417 0.2060 0.1895 -0.0034 0.0498  0.0145  9   TYR   A CG  
168  C CG  B TYR   A 9   ? 0.1489 0.2121 0.2148 -0.0051 0.0496  0.0411  9   TYR   A CG  
169  C CD1 A TYR   A 9   ? 0.1498 0.2102 0.2044 -0.0084 0.0450  0.0086  9   TYR   A CD1 
170  C CD1 B TYR   A 9   ? 0.1553 0.2187 0.2307 -0.0145 0.0477  0.0414  9   TYR   A CD1 
171  C CD2 A TYR   A 9   ? 0.1415 0.1986 0.1831 0.0003  0.0469  0.0154  9   TYR   A CD2 
172  C CD2 B TYR   A 9   ? 0.1441 0.2025 0.1980 0.0050  0.0446  0.0462  9   TYR   A CD2 
173  C CE1 A TYR   A 9   ? 0.1509 0.2114 0.2073 -0.0062 0.0464  0.0041  9   TYR   A CE1 
174  C CE1 B TYR   A 9   ? 0.1554 0.2141 0.2300 -0.0145 0.0432  0.0379  9   TYR   A CE1 
175  C CE2 A TYR   A 9   ? 0.1426 0.2025 0.1951 -0.0002 0.0452  0.0116  9   TYR   A CE2 
176  C CE2 B TYR   A 9   ? 0.1422 0.2042 0.2038 0.0046  0.0426  0.0455  9   TYR   A CE2 
177  C CZ  A TYR   A 9   ? 0.1484 0.2130 0.2129 -0.0123 0.0502  0.0056  9   TYR   A CZ  
178  C CZ  B TYR   A 9   ? 0.1429 0.2083 0.2229 -0.0102 0.0453  0.0457  9   TYR   A CZ  
179  O OH  A TYR   A 9   ? 0.1631 0.2205 0.2395 -0.0191 0.0508  0.0011  9   TYR   A OH  
180  O OH  B TYR   A 9   ? 0.1383 0.2151 0.2289 -0.0175 0.0341  0.0482  9   TYR   A OH  
199  N N   A LEU   A 10  ? 0.1308 0.1738 0.2115 -0.0176 0.0509  0.0539  10  LEU   A N   
200  N N   B LEU   A 10  ? 0.1596 0.1785 0.2428 -0.0086 0.0320  0.0543  10  LEU   A N   
201  C CA  A LEU   A 10  ? 0.1394 0.1717 0.2120 -0.0241 0.0495  0.0594  10  LEU   A CA  
202  C CA  B LEU   A 10  ? 0.1658 0.1778 0.2455 -0.0126 0.0188  0.0497  10  LEU   A CA  
203  C C   A LEU   A 10  ? 0.1394 0.1532 0.1935 -0.0289 0.0396  0.0525  10  LEU   A C   
204  C C   B LEU   A 10  ? 0.1597 0.1648 0.2488 -0.0174 0.0106  0.0575  10  LEU   A C   
205  O O   A LEU   A 10  ? 0.1339 0.1402 0.1531 -0.0362 0.0397  0.0346  10  LEU   A O   
206  O O   B LEU   A 10  ? 0.1540 0.1636 0.2178 -0.0126 -0.0015 0.0585  10  LEU   A O   
207  C CB  A LEU   A 10  ? 0.1457 0.1854 0.2587 -0.0164 0.0494  0.0665  10  LEU   A CB  
208  C CB  B LEU   A 10  ? 0.1720 0.1854 0.2579 -0.0126 0.0143  0.0526  10  LEU   A CB  
209  C CG  A LEU   A 10  ? 0.1690 0.1952 0.3001 -0.0096 0.0342  0.0572  10  LEU   A CG  
210  C CG  B LEU   A 10  ? 0.1964 0.1961 0.2884 -0.0128 -0.0012 0.0407  10  LEU   A CG  
211  C CD1 A LEU   A 10  ? 0.1780 0.2049 0.3194 -0.0141 0.0383  0.0428  10  LEU   A CD1 
212  C CD1 B LEU   A 10  ? 0.2047 0.2184 0.3197 -0.0310 0.0020  0.0231  10  LEU   A CD1 
213  C CD2 A LEU   A 10  ? 0.1772 0.2009 0.3121 -0.0001 0.0351  0.0408  10  LEU   A CD2 
214  C CD2 B LEU   A 10  ? 0.2145 0.2047 0.2987 -0.0077 -0.0219 0.0430  10  LEU   A CD2 
237  N N   A LYS   A 11  ? 0.1474 0.1530 0.2066 -0.0221 0.0281  0.0608  11  LYS   A N   
238  N N   B LYS   A 11  ? 0.1604 0.1601 0.2685 -0.0254 0.0142  0.0635  11  LYS   A N   
239  C CA  A LYS   A 11  ? 0.1470 0.1522 0.2206 -0.0195 0.0149  0.0544  11  LYS   A CA  
240  C CA  B LYS   A 11  ? 0.1570 0.1499 0.2681 -0.0360 0.0135  0.0682  11  LYS   A CA  
241  C C   A LYS   A 11  ? 0.1364 0.1555 0.2386 -0.0164 0.0097  0.0479  11  LYS   A C   
242  C C   B LYS   A 11  ? 0.1359 0.1431 0.2581 -0.0387 0.0191  0.0627  11  LYS   A C   
243  O O   A LYS   A 11  ? 0.1334 0.1551 0.2698 -0.0217 0.0108  0.0550  11  LYS   A O   
244  O O   B LYS   A 11  ? 0.1217 0.1476 0.2729 -0.0324 0.0215  0.0560  11  LYS   A O   
245  C CB  A LYS   A 11  ? 0.1575 0.1506 0.2064 -0.0138 0.0113  0.0389  11  LYS   A CB  
246  C CB  B LYS   A 11  ? 0.1748 0.1475 0.2636 -0.0368 0.0174  0.0573  11  LYS   A CB  
247  C CG  A LYS   A 11  ? 0.1657 0.1516 0.1819 -0.0122 0.0041  0.0310  11  LYS   A CG  
248  C CG  B LYS   A 11  ? 0.1917 0.1512 0.2468 -0.0398 0.0190  0.0528  11  LYS   A CG  
249  C CD  A LYS   A 11  ? 0.1714 0.1433 0.1694 -0.0177 0.0009  0.0308  11  LYS   A CD  
250  C CD  B LYS   A 11  ? 0.2130 0.1575 0.2347 -0.0320 0.0187  0.0457  11  LYS   A CD  
251  C CE  A LYS   A 11  ? 0.1783 0.1444 0.1600 -0.0086 0.0098  0.0424  11  LYS   A CE  
252  C CE  B LYS   A 11  ? 0.2189 0.1543 0.2258 -0.0322 0.0201  0.0425  11  LYS   A CE  
253  N NZ  A LYS   A 11  ? 0.1779 0.1487 0.1559 0.0043  0.0073  0.0611  11  LYS   A NZ  
254  N NZ  B LYS   A 11  ? 0.2198 0.1516 0.2337 -0.0257 0.0025  0.0281  11  LYS   A NZ  
281  N N   A LEU   A 12  ? 0.1393 0.1580 0.2190 -0.0163 -0.0015 0.0456  12  LEU   A N   
282  N N   B LEU   A 12  ? 0.1350 0.1570 0.2435 -0.0354 -0.0010 0.0549  12  LEU   A N   
283  C CA  A LEU   A 12  ? 0.1446 0.1706 0.2035 -0.0199 -0.0134 0.0545  12  LEU   A CA  
284  C CA  B LEU   A 12  ? 0.1423 0.1807 0.2377 -0.0347 -0.0154 0.0662  12  LEU   A CA  
285  C C   A LEU   A 12  ? 0.1370 0.1711 0.2043 -0.0282 -0.0078 0.0440  12  LEU   A C   
286  C C   B LEU   A 12  ? 0.1380 0.1783 0.2310 -0.0365 -0.0079 0.0725  12  LEU   A C   
287  O O   A LEU   A 12  ? 0.1393 0.1821 0.2079 -0.0282 -0.0081 0.0253  12  LEU   A O   
288  O O   B LEU   A 12  ? 0.1355 0.1858 0.2115 -0.0312 -0.0029 0.0785  12  LEU   A O   
289  C CB  A LEU   A 12  ? 0.1606 0.1681 0.2071 -0.0119 -0.0132 0.0671  12  LEU   A CB  
290  C CB  B LEU   A 12  ? 0.1557 0.1906 0.2577 -0.0333 -0.0181 0.0647  12  LEU   A CB  
291  C CG  A LEU   A 12  ? 0.1713 0.1655 0.2337 0.0007  -0.0069 0.0751  12  LEU   A CG  
292  C CG  B LEU   A 12  ? 0.1614 0.1956 0.2993 -0.0244 -0.0080 0.0718  12  LEU   A CG  
293  C CD1 A LEU   A 12  ? 0.1823 0.1616 0.2473 0.0110  -0.0089 0.0832  12  LEU   A CD1 
294  C CD1 B LEU   A 12  ? 0.1705 0.1984 0.3122 -0.0192 0.0091  0.0803  12  LEU   A CD1 
295  C CD2 A LEU   A 12  ? 0.1723 0.1632 0.2362 0.0134  -0.0022 0.0703  12  LEU   A CD2 
296  C CD2 B LEU   A 12  ? 0.1613 0.1990 0.3122 -0.0103 -0.0134 0.0548  12  LEU   A CD2 
319  N N   A THR   A 13  ? 0.1297 0.1601 0.2008 -0.0242 -0.0064 0.0342  13  THR   A N   
320  N N   B THR   A 13  ? 0.1347 0.1664 0.2335 -0.0344 -0.0037 0.0505  13  THR   A N   
321  C CA  A THR   A 13  ? 0.1321 0.1607 0.2071 -0.0225 -0.0017 0.0344  13  THR   A CA  
322  C CA  B THR   A 13  ? 0.1463 0.1667 0.2448 -0.0324 0.0090  0.0481  13  THR   A CA  
323  C C   A THR   A 13  ? 0.1293 0.1541 0.2107 -0.0239 -0.0069 0.0413  13  THR   A C   
324  C C   B THR   A 13  ? 0.1461 0.1614 0.2467 -0.0359 0.0097  0.0485  13  THR   A C   
325  O O   A THR   A 13  ? 0.1385 0.1526 0.2174 -0.0159 -0.0087 0.0413  13  THR   A O   
326  O O   B THR   A 13  ? 0.1534 0.1600 0.2426 -0.0256 0.0074  0.0530  13  THR   A O   
327  C CB  A THR   A 13  ? 0.1342 0.1728 0.2104 -0.0207 -0.0049 0.0393  13  THR   A CB  
328  C CB  B THR   A 13  ? 0.1525 0.1744 0.2504 -0.0290 0.0002  0.0567  13  THR   A CB  
329  O OG1 A THR   A 13  ? 0.1308 0.1696 0.2210 -0.0271 -0.0016 0.0393  13  THR   A OG1 
330  O OG1 B THR   A 13  ? 0.1511 0.1623 0.2680 -0.0335 -0.0046 0.0530  13  THR   A OG1 
331  C CG2 A THR   A 13  ? 0.1375 0.1895 0.2135 -0.0177 0.0041  0.0318  13  THR   A CG2 
332  C CG2 B THR   A 13  ? 0.1598 0.1968 0.2535 -0.0233 0.0132  0.0457  13  THR   A CG2 
347  N N   A ASP   A 14  ? 0.1376 0.1485 0.2168 -0.0218 -0.0042 0.0539  14  ASP   A N   
348  N N   B ASP   A 14  ? 0.1616 0.1566 0.2598 -0.0364 0.0121  0.0538  14  ASP   A N   
349  C CA  A ASP   A 14  ? 0.1389 0.1500 0.2201 -0.0188 -0.0044 0.0592  14  ASP   A CA  
350  C CA  B ASP   A 14  ? 0.1703 0.1621 0.2690 -0.0262 0.0085  0.0519  14  ASP   A CA  
351  C C   A ASP   A 14  ? 0.1343 0.1531 0.2047 -0.0130 -0.0051 0.0584  14  ASP   A C   
352  C C   B ASP   A 14  ? 0.1533 0.1567 0.2369 -0.0232 0.0003  0.0608  14  ASP   A C   
353  O O   A ASP   A 14  ? 0.1357 0.1609 0.2038 -0.0102 -0.0118 0.0560  14  ASP   A O   
354  O O   B ASP   A 14  ? 0.1602 0.1616 0.2602 -0.0234 -0.0066 0.0660  14  ASP   A O   
355  C CB  A ASP   A 14  ? 0.1644 0.1571 0.2586 -0.0205 -0.0073 0.0684  14  ASP   A CB  
356  C CB  B ASP   A 14  ? 0.2134 0.1851 0.3302 -0.0121 0.0065  0.0492  14  ASP   A CB  
357  C CG  A ASP   A 14  ? 0.1766 0.1749 0.3097 -0.0261 0.0038  0.0426  14  ASP   A CG  
358  C CG  B ASP   A 14  ? 0.2464 0.2242 0.4093 0.0047  0.0030  0.0157  14  ASP   A CG  
359  O OD1 A ASP   A 14  ? 0.1820 0.1700 0.3135 -0.0280 -0.0052 0.0526  14  ASP   A OD1 
360  O OD1 B ASP   A 14  ? 0.2566 0.2434 0.4377 0.0156  -0.0091 -0.0021 14  ASP   A OD1 
361  O OD2 A ASP   A 14  ? 0.1869 0.1808 0.3338 -0.0347 0.0060  0.0233  14  ASP   A OD2 
362  O OD2 B ASP   A 14  ? 0.2733 0.2311 0.4343 0.0099  -0.0033 0.0116  14  ASP   A OD2 
371  N N   . ASN   A 15  ? 0.1360 0.1512 0.2075 -0.0206 0.0073  0.0546  15  ASN   A N   
372  C CA  . ASN   A 15  ? 0.1330 0.1490 0.2165 -0.0135 -0.0034 0.0439  15  ASN   A CA  
373  C C   . ASN   A 15  ? 0.1230 0.1448 0.2398 -0.0234 -0.0002 0.0454  15  ASN   A C   
374  O O   . ASN   A 15  ? 0.1390 0.1461 0.2756 -0.0193 -0.0158 0.0467  15  ASN   A O   
375  C CB  . ASN   A 15  ? 0.1450 0.1498 0.2099 -0.0115 -0.0031 0.0446  15  ASN   A CB  
376  C CG  . ASN   A 15  ? 0.1334 0.1577 0.2240 -0.0088 -0.0005 0.0273  15  ASN   A CG  
377  O OD1 . ASN   A 15  ? 0.1548 0.1718 0.2483 -0.0245 -0.0009 0.0344  15  ASN   A OD1 
378  N ND2 . ASN   A 15  ? 0.1477 0.1621 0.2189 -0.0237 0.0170  0.0326  15  ASN   A ND2 
386  N N   A VAL   A 16  ? 0.1228 0.1451 0.2313 -0.0203 0.0010  0.0472  16  VAL   A N   
387  N N   B VAL   A 16  ? 0.1261 0.1479 0.2449 -0.0156 0.0020  0.0451  16  VAL   A N   
388  C CA  A VAL   A 16  ? 0.1266 0.1447 0.2173 -0.0223 0.0056  0.0593  16  VAL   A CA  
389  C CA  B VAL   A 16  ? 0.1337 0.1508 0.2368 -0.0144 0.0077  0.0569  16  VAL   A CA  
390  C C   A VAL   A 16  ? 0.1176 0.1377 0.2123 -0.0219 0.0060  0.0549  16  VAL   A C   
391  C C   B VAL   A 16  ? 0.1260 0.1505 0.2351 -0.0165 0.0083  0.0491  16  VAL   A C   
392  O O   A VAL   A 16  ? 0.1151 0.1395 0.2143 -0.0238 0.0097  0.0469  16  VAL   A O   
393  O O   B VAL   A 16  ? 0.1274 0.1544 0.2347 -0.0118 0.0173  0.0368  16  VAL   A O   
394  C CB  A VAL   A 16  ? 0.1429 0.1527 0.2169 -0.0099 0.0126  0.0579  16  VAL   A CB  
395  C CB  B VAL   A 16  ? 0.1516 0.1559 0.2387 0.0059  0.0190  0.0567  16  VAL   A CB  
396  C CG1 A VAL   A 16  ? 0.1561 0.1612 0.2113 -0.0055 0.0223  0.0643  16  VAL   A CG1 
397  C CG1 B VAL   A 16  ? 0.1652 0.1642 0.2351 0.0155  0.0335  0.0593  16  VAL   A CG1 
398  C CG2 A VAL   A 16  ? 0.1483 0.1635 0.2305 -0.0048 0.0259  0.0502  16  VAL   A CG2 
399  C CG2 B VAL   A 16  ? 0.1587 0.1676 0.2570 0.0092  0.0353  0.0518  16  VAL   A CG2 
418  N N   A TYR   A 17  ? 0.1167 0.1268 0.2044 -0.0161 0.0148  0.0565  17  TYR   A N   
419  N N   B TYR   A 17  ? 0.1228 0.1430 0.2287 -0.0166 0.0107  0.0485  17  TYR   A N   
420  C CA  A TYR   A 17  ? 0.1318 0.1346 0.1959 -0.0093 0.0218  0.0547  17  TYR   A CA  
421  C CA  B TYR   A 17  ? 0.1341 0.1471 0.2102 -0.0195 0.0147  0.0490  17  TYR   A CA  
422  C C   A TYR   A 17  ? 0.1306 0.1229 0.1988 -0.0059 0.0161  0.0584  17  TYR   A C   
423  C C   B TYR   A 17  ? 0.1297 0.1469 0.2166 -0.0179 0.0143  0.0441  17  TYR   A C   
424  O O   A TYR   A 17  ? 0.1273 0.1168 0.2014 -0.0102 0.0179  0.0559  17  TYR   A O   
425  O O   B TYR   A 17  ? 0.1295 0.1514 0.2104 -0.0213 0.0116  0.0316  17  TYR   A O   
426  C CB  A TYR   A 17  ? 0.1490 0.1492 0.1982 -0.0073 0.0132  0.0535  17  TYR   A CB  
427  C CB  B TYR   A 17  ? 0.1550 0.1472 0.2055 -0.0222 -0.0103 0.0525  17  TYR   A CB  
428  C CG  A TYR   A 17  ? 0.1681 0.1668 0.2124 -0.0035 0.0159  0.0462  17  TYR   A CG  
429  C CG  B TYR   A 17  ? 0.1853 0.1535 0.2226 -0.0330 -0.0176 0.0443  17  TYR   A CG  
430  C CD1 A TYR   A 17  ? 0.1776 0.1729 0.2203 0.0103  0.0135  0.0490  17  TYR   A CD1 
431  C CD1 B TYR   A 17  ? 0.2000 0.1591 0.2322 -0.0257 -0.0234 0.0447  17  TYR   A CD1 
432  C CD2 A TYR   A 17  ? 0.1788 0.1800 0.2186 -0.0121 0.0210  0.0455  17  TYR   A CD2 
433  C CD2 B TYR   A 17  ? 0.2008 0.1562 0.2202 -0.0523 -0.0152 0.0504  17  TYR   A CD2 
434  C CE1 A TYR   A 17  ? 0.1890 0.1824 0.2217 0.0110  0.0133  0.0473  17  TYR   A CE1 
435  C CE1 B TYR   A 17  ? 0.2123 0.1613 0.2358 -0.0318 -0.0292 0.0436  17  TYR   A CE1 
436  C CE2 A TYR   A 17  ? 0.1918 0.1901 0.2221 -0.0086 0.0143  0.0430  17  TYR   A CE2 
437  C CE2 B TYR   A 17  ? 0.2166 0.1656 0.2237 -0.0474 -0.0305 0.0413  17  TYR   A CE2 
438  C CZ  A TYR   A 17  ? 0.1985 0.1901 0.2248 0.0003  0.0060  0.0490  17  TYR   A CZ  
439  C CZ  B TYR   A 17  ? 0.2228 0.1602 0.2257 -0.0446 -0.0372 0.0515  17  TYR   A CZ  
440  O OH  A TYR   A 17  ? 0.2096 0.1970 0.2371 0.0054  0.0039  0.0491  17  TYR   A OH  
441  O OH  B TYR   A 17  ? 0.2403 0.1543 0.2284 -0.0515 -0.0337 0.0541  17  TYR   A OH  
460  N N   A ILE   A 18  ? 0.1315 0.1341 0.1869 -0.0056 0.0098  0.0621  18  ILE   A N   
461  N N   B ILE   A 18  ? 0.1248 0.1537 0.2205 -0.0263 0.0160  0.0531  18  ILE   A N   
462  C CA  A ILE   A 18  ? 0.1354 0.1398 0.1877 0.0021  0.0071  0.0459  18  ILE   A CA  
463  C CA  B ILE   A 18  ? 0.1274 0.1629 0.2298 -0.0221 0.0198  0.0587  18  ILE   A CA  
464  C C   A ILE   A 18  ? 0.1389 0.1504 0.1924 0.0051  0.0042  0.0452  18  ILE   A C   
465  C C   B ILE   A 18  ? 0.1373 0.1674 0.2509 -0.0254 0.0318  0.0649  18  ILE   A C   
466  O O   A ILE   A 18  ? 0.1437 0.1652 0.2075 0.0023  0.0192  0.0533  18  ILE   A O   
467  O O   B ILE   A 18  ? 0.1385 0.1844 0.2687 -0.0349 0.0499  0.0702  18  ILE   A O   
468  C CB  A ILE   A 18  ? 0.1456 0.1501 0.1959 0.0000  0.0061  0.0475  18  ILE   A CB  
469  C CB  B ILE   A 18  ? 0.1467 0.1685 0.2293 -0.0128 0.0128  0.0777  18  ILE   A CB  
470  C CG1 A ILE   A 18  ? 0.1634 0.1669 0.2161 -0.0055 0.0075  0.0427  18  ILE   A CG1 
471  C CG1 B ILE   A 18  ? 0.1631 0.1734 0.2308 -0.0058 0.0038  0.0834  18  ILE   A CG1 
472  C CG2 A ILE   A 18  ? 0.1518 0.1559 0.2018 -0.0005 -0.0046 0.0445  18  ILE   A CG2 
473  C CG2 B ILE   A 18  ? 0.1542 0.1797 0.2381 -0.0222 0.0092  0.0758  18  ILE   A CG2 
474  C CD1 A ILE   A 18  ? 0.1864 0.1849 0.2430 -0.0048 0.0026  0.0356  18  ILE   A CD1 
475  C CD1 B ILE   A 18  ? 0.1958 0.1799 0.2528 0.0020  0.0026  0.0873  18  ILE   A CD1 
498  N N   A LYS   A 19  ? 0.1379 0.1485 0.1883 0.0116  0.0136  0.0322  19  LYS   A N   
499  N N   B LYS   A 19  ? 0.1372 0.1633 0.2401 -0.0196 0.0458  0.0656  19  LYS   A N   
500  C CA  A LYS   A 19  ? 0.1441 0.1507 0.1915 0.0094  0.0281  0.0307  19  LYS   A CA  
501  C CA  B LYS   A 19  ? 0.1420 0.1668 0.2359 -0.0046 0.0326  0.0576  19  LYS   A CA  
502  C C   A LYS   A 19  ? 0.1408 0.1412 0.1845 0.0081  0.0365  0.0240  19  LYS   A C   
503  C C   B LYS   A 19  ? 0.1262 0.1603 0.2317 -0.0045 0.0306  0.0502  19  LYS   A C   
504  O O   A LYS   A 19  ? 0.1416 0.1463 0.1943 0.0068  0.0374  0.0291  19  LYS   A O   
505  O O   B LYS   A 19  ? 0.1208 0.1546 0.2273 -0.0033 0.0198  0.0551  19  LYS   A O   
506  C CB  A LYS   A 19  ? 0.1474 0.1657 0.1952 0.0005  0.0369  0.0299  19  LYS   A CB  
507  C CB  B LYS   A 19  ? 0.1521 0.1815 0.2260 0.0056  0.0359  0.0543  19  LYS   A CB  
508  C CG  A LYS   A 19  ? 0.1599 0.1802 0.1938 -0.0042 0.0313  0.0375  19  LYS   A CG  
509  C CG  B LYS   A 19  ? 0.1667 0.2064 0.2414 0.0070  0.0336  0.0310  19  LYS   A CG  
510  C CD  A LYS   A 19  ? 0.1741 0.1909 0.2011 -0.0042 0.0281  0.0452  19  LYS   A CD  
511  C CD  B LYS   A 19  ? 0.1787 0.2279 0.2588 0.0106  0.0328  0.0138  19  LYS   A CD  
512  C CE  A LYS   A 19  ? 0.1808 0.1957 0.2042 -0.0090 0.0154  0.0452  19  LYS   A CE  
513  C CE  B LYS   A 19  ? 0.1868 0.2390 0.2586 0.0084  0.0331  0.0082  19  LYS   A CE  
514  N NZ  A LYS   A 19  ? 0.1821 0.1975 0.2096 -0.0196 0.0194  0.0481  19  LYS   A NZ  
515  N NZ  B LYS   A 19  ? 0.1920 0.2443 0.2583 0.0132  0.0319  -0.0008 19  LYS   A NZ  
542  N N   A ASN   A 20  ? 0.1531 0.1419 0.1933 0.0031  0.0358  0.0204  20  ASN   A N   
543  N N   B ASN   A 20  ? 0.1263 0.1634 0.2496 -0.0165 0.0191  0.0542  20  ASN   A N   
544  C CA  A ASN   A 20  ? 0.1538 0.1488 0.1742 0.0108  0.0270  0.0126  20  ASN   A CA  
545  C CA  B ASN   A 20  ? 0.1256 0.1824 0.2563 0.0038  0.0295  0.0448  20  ASN   A CA  
546  C C   A ASN   A 20  ? 0.1638 0.1549 0.1738 0.0094  0.0338  0.0132  20  ASN   A C   
547  C C   B ASN   A 20  ? 0.1450 0.1946 0.2386 0.0008  0.0522  0.0426  20  ASN   A C   
548  O O   A ASN   A 20  ? 0.1718 0.1637 0.1491 0.0045  0.0340  0.0241  20  ASN   A O   
549  O O   B ASN   A 20  ? 0.1624 0.2222 0.2490 -0.0014 0.0422  0.0506  20  ASN   A O   
550  C CB  A ASN   A 20  ? 0.1518 0.1517 0.1843 0.0121  0.0191  0.0205  20  ASN   A CB  
551  C CB  B ASN   A 20  ? 0.1245 0.1942 0.2706 0.0047  0.0261  0.0478  20  ASN   A CB  
552  C CG  A ASN   A 20  ? 0.1612 0.1612 0.2068 0.0187  0.0239  0.0197  20  ASN   A CG  
553  C CG  B ASN   A 20  ? 0.1278 0.2055 0.2973 0.0204  0.0262  0.0546  20  ASN   A CG  
554  O OD1 A ASN   A 20  ? 0.1877 0.1816 0.2452 0.0222  0.0229  0.0106  20  ASN   A OD1 
555  O OD1 B ASN   A 20  ? 0.1568 0.2135 0.3175 0.0348  0.0422  0.0363  20  ASN   A OD1 
556  N ND2 A ASN   A 20  ? 0.1601 0.1573 0.2131 0.0221  0.0160  0.0327  20  ASN   A ND2 
557  N ND2 B ASN   A 20  ? 0.1365 0.2030 0.2922 0.0175  0.0113  0.0657  20  ASN   A ND2 
570  N N   A ALA   A 21  ? 0.1717 0.1500 0.1844 0.0070  0.0302  0.0063  21  ALA   A N   
571  N N   B ALA   A 21  ? 0.1517 0.1760 0.2310 -0.0062 0.0630  0.0258  21  ALA   A N   
572  C CA  A ALA   A 21  ? 0.1859 0.1482 0.1873 -0.0034 0.0243  0.0151  21  ALA   A CA  
573  C CA  B ALA   A 21  ? 0.1664 0.1695 0.2212 -0.0060 0.0445  0.0348  21  ALA   A CA  
574  C C   A ALA   A 21  ? 0.2005 0.1631 0.1781 -0.0070 0.0309  0.0006  21  ALA   A C   
575  C C   B ALA   A 21  ? 0.1490 0.1607 0.1874 -0.0043 0.0365  0.0225  21  ALA   A C   
576  O O   A ALA   A 21  ? 0.2039 0.1767 0.1891 -0.0079 0.0324  -0.0171 21  ALA   A O   
577  O O   B ALA   A 21  ? 0.1447 0.1570 0.1768 -0.0126 0.0317  0.0088  21  ALA   A O   
578  C CB  A ALA   A 21  ? 0.1822 0.1548 0.2094 -0.0182 0.0126  0.0292  21  ALA   A CB  
579  C CB  B ALA   A 21  ? 0.1908 0.1862 0.2455 -0.0120 0.0270  0.0355  21  ALA   A CB  
590  N N   A ASP   A 22  ? 0.2091 0.1597 0.1833 -0.0093 0.0320  0.0040  22  ASP   A N   
591  N N   B ASP   A 22  ? 0.1472 0.1537 0.1841 0.0021  0.0408  0.0286  22  ASP   A N   
592  C CA  A ASP   A 22  ? 0.2154 0.1639 0.1845 -0.0095 0.0237  0.0199  22  ASP   A CA  
593  C CA  B ASP   A 22  ? 0.1446 0.1558 0.1687 0.0040  0.0311  0.0316  22  ASP   A CA  
594  C C   A ASP   A 22  ? 0.2041 0.1758 0.1691 -0.0139 0.0290  0.0177  22  ASP   A C   
595  C C   B ASP   A 22  ? 0.1460 0.1546 0.1476 -0.0055 0.0373  0.0290  22  ASP   A C   
596  O O   A ASP   A 22  ? 0.2027 0.1877 0.1659 -0.0201 0.0341  0.0110  22  ASP   A O   
597  O O   B ASP   A 22  ? 0.1517 0.1688 0.1482 -0.0166 0.0308  0.0188  22  ASP   A O   
598  C CB  A ASP   A 22  ? 0.2411 0.1704 0.2191 -0.0088 0.0154  0.0179  22  ASP   A CB  
599  C CB  B ASP   A 22  ? 0.1620 0.1553 0.1939 0.0065  0.0329  0.0246  22  ASP   A CB  
600  C CG  A ASP   A 22  ? 0.2558 0.1792 0.2410 -0.0149 0.0046  0.0256  22  ASP   A CG  
601  C CG  B ASP   A 22  ? 0.1716 0.1490 0.2112 0.0165  0.0361  0.0219  22  ASP   A CG  
602  O OD1 A ASP   A 22  ? 0.2511 0.1737 0.2421 -0.0303 -0.0090 0.0381  22  ASP   A OD1 
603  O OD1 B ASP   A 22  ? 0.1709 0.1428 0.1892 0.0103  0.0401  0.0183  22  ASP   A OD1 
604  O OD2 A ASP   A 22  ? 0.2727 0.1949 0.2593 -0.0110 0.0041  0.0155  22  ASP   A OD2 
605  O OD2 B ASP   A 22  ? 0.1963 0.1629 0.2733 0.0104  0.0364  0.0303  22  ASP   A OD2 
614  N N   A ILE   A 23  ? 0.1995 0.1721 0.1440 -0.0149 0.0277  0.0170  23  ILE   A N   
615  N N   B ILE   A 23  ? 0.1454 0.1495 0.1608 -0.0112 0.0294  0.0267  23  ILE   A N   
616  C CA  A ILE   A 23  ? 0.1921 0.1624 0.1498 -0.0098 0.0281  0.0187  23  ILE   A CA  
617  C CA  B ILE   A 23  ? 0.1400 0.1563 0.1510 -0.0120 0.0209  0.0277  23  ILE   A CA  
618  C C   A ILE   A 23  ? 0.1802 0.1673 0.1482 -0.0067 0.0296  0.0242  23  ILE   A C   
619  C C   B ILE   A 23  ? 0.1387 0.1622 0.1536 -0.0146 0.0215  0.0245  23  ILE   A C   
620  O O   A ILE   A 23  ? 0.1770 0.1696 0.1583 -0.0023 0.0277  0.0177  23  ILE   A O   
621  O O   B ILE   A 23  ? 0.1423 0.1610 0.1611 -0.0131 0.0140  0.0158  23  ILE   A O   
622  C CB  A ILE   A 23  ? 0.1961 0.1603 0.1339 -0.0076 0.0358  0.0209  23  ILE   A CB  
623  C CB  B ILE   A 23  ? 0.1443 0.1451 0.1535 0.0006  0.0209  0.0257  23  ILE   A CB  
624  C CG1 A ILE   A 23  ? 0.2017 0.1538 0.1392 -0.0131 0.0427  0.0132  23  ILE   A CG1 
625  C CG1 B ILE   A 23  ? 0.1511 0.1386 0.1595 -0.0051 0.0106  0.0093  23  ILE   A CG1 
626  C CG2 A ILE   A 23  ? 0.1979 0.1648 0.1375 0.0023  0.0360  0.0310  23  ILE   A CG2 
627  C CG2 B ILE   A 23  ? 0.1383 0.1371 0.1747 0.0140  0.0321  0.0255  23  ILE   A CG2 
628  C CD1 A ILE   A 23  ? 0.2050 0.1516 0.1472 -0.0114 0.0341  -0.0001 23  ILE   A CD1 
629  C CD1 B ILE   A 23  ? 0.1488 0.1436 0.1513 0.0031  -0.0135 -0.0085 23  ILE   A CD1 
652  N N   A VAL   A 24  ? 0.1771 0.1684 0.1674 -0.0112 0.0197  0.0160  24  VAL   A N   
653  N N   B VAL   A 24  ? 0.1444 0.1685 0.1611 -0.0152 0.0236  0.0139  24  VAL   A N   
654  C CA  A VAL   A 24  ? 0.1840 0.1772 0.1894 -0.0149 0.0117  0.0036  24  VAL   A CA  
655  C CA  B VAL   A 24  ? 0.1615 0.1748 0.1861 -0.0177 0.0200  0.0141  24  VAL   A CA  
656  C C   A VAL   A 24  ? 0.1918 0.1963 0.1970 -0.0175 -0.0012 0.0044  24  VAL   A C   
657  C C   B VAL   A 24  ? 0.1649 0.1876 0.1933 -0.0137 0.0169  0.0049  24  VAL   A C   
658  O O   A VAL   A 24  ? 0.1912 0.1985 0.1920 -0.0162 0.0008  0.0113  24  VAL   A O   
659  O O   B VAL   A 24  ? 0.1779 0.1958 0.2247 -0.0115 0.0260  0.0126  24  VAL   A O   
660  C CB  A VAL   A 24  ? 0.1839 0.1763 0.2014 -0.0186 0.0291  0.0078  24  VAL   A CB  
661  C CB  B VAL   A 24  ? 0.1694 0.1760 0.2074 -0.0277 0.0203  0.0221  24  VAL   A CB  
662  C CG1 A VAL   A 24  ? 0.1833 0.1858 0.1946 -0.0045 0.0499  -0.0056 24  VAL   A CG1 
663  C CG1 B VAL   A 24  ? 0.1913 0.1846 0.2299 -0.0208 0.0036  0.0125  24  VAL   A CG1 
664  C CG2 A VAL   A 24  ? 0.1945 0.1745 0.2054 -0.0282 0.0343  0.0138  24  VAL   A CG2 
665  C CG2 B VAL   A 24  ? 0.1755 0.1783 0.2033 -0.0416 0.0248  0.0225  24  VAL   A CG2 
684  N N   A GLU   A 25  ? 0.2033 0.2190 0.1976 -0.0219 -0.0021 -0.0099 25  GLU   A N   
685  N N   B GLU   A 25  ? 0.1616 0.2088 0.1894 -0.0073 0.0387  -0.0061 25  GLU   A N   
686  C CA  A GLU   A 25  ? 0.2198 0.2400 0.2130 -0.0177 -0.0011 -0.0139 25  GLU   A CA  
687  C CA  B GLU   A 25  ? 0.1683 0.2270 0.1876 -0.0068 0.0418  0.0031  25  GLU   A CA  
688  C C   A GLU   A 25  ? 0.2115 0.2412 0.1836 -0.0225 0.0139  -0.0133 25  GLU   A C   
689  C C   B GLU   A 25  ? 0.1611 0.2372 0.1633 -0.0088 0.0473  0.0136  25  GLU   A C   
690  O O   A GLU   A 25  ? 0.2152 0.2511 0.1906 -0.0187 0.0195  -0.0151 25  GLU   A O   
691  O O   B GLU   A 25  ? 0.1767 0.2480 0.1809 -0.0049 0.0521  0.0116  25  GLU   A O   
692  C CB  A GLU   A 25  ? 0.2422 0.2585 0.2608 -0.0161 -0.0100 -0.0167 25  GLU   A CB  
693  C CB  B GLU   A 25  ? 0.1894 0.2380 0.2213 -0.0027 0.0480  -0.0028 25  GLU   A CB  
694  C CG  A GLU   A 25  ? 0.2648 0.2761 0.3101 -0.0201 -0.0232 -0.0162 25  GLU   A CG  
695  C CG  B GLU   A 25  ? 0.2285 0.2544 0.2910 -0.0069 0.0404  -0.0134 25  GLU   A CG  
696  C CD  A GLU   A 25  ? 0.2828 0.2915 0.3461 -0.0214 -0.0358 -0.0157 25  GLU   A CD  
697  C CD  B GLU   A 25  ? 0.2684 0.2736 0.3564 -0.0114 0.0274  -0.0242 25  GLU   A CD  
698  O OE1 A GLU   A 25  ? 0.2886 0.2951 0.3515 -0.0206 -0.0494 -0.0233 25  GLU   A OE1 
699  O OE1 B GLU   A 25  ? 0.2855 0.2808 0.3948 -0.0123 0.0240  -0.0262 25  GLU   A OE1 
700  O OE2 A GLU   A 25  ? 0.2912 0.3027 0.3743 -0.0215 -0.0386 -0.0219 25  GLU   A OE2 
701  O OE2 B GLU   A 25  ? 0.2798 0.2819 0.3802 -0.0128 0.0191  -0.0319 25  GLU   A OE2 
714  N N   A GLU   A 26  ? 0.2031 0.2304 0.1704 -0.0396 0.0251  -0.0171 26  GLU   A N   
715  N N   B GLU   A 26  ? 0.1542 0.2353 0.1639 -0.0174 0.0563  0.0005  26  GLU   A N   
716  C CA  A GLU   A 26  ? 0.2128 0.2210 0.1657 -0.0538 0.0366  -0.0097 26  GLU   A CA  
717  C CA  B GLU   A 26  ? 0.1648 0.2304 0.1647 -0.0276 0.0591  0.0142  26  GLU   A CA  
718  C C   A GLU   A 26  ? 0.2119 0.2157 0.1465 -0.0558 0.0358  -0.0081 26  GLU   A C   
719  C C   B GLU   A 26  ? 0.1639 0.2144 0.1428 -0.0162 0.0370  0.0168  26  GLU   A C   
720  O O   A GLU   A 26  ? 0.2183 0.2138 0.1283 -0.0576 0.0330  -0.0180 26  GLU   A O   
721  O O   B GLU   A 26  ? 0.1823 0.2158 0.1414 -0.0206 0.0395  0.0177  26  GLU   A O   
722  C CB  A GLU   A 26  ? 0.2302 0.2159 0.1916 -0.0600 0.0474  -0.0037 26  GLU   A CB  
723  C CB  B GLU   A 26  ? 0.1858 0.2400 0.2102 -0.0426 0.0391  0.0152  26  GLU   A CB  
724  C CG  A GLU   A 26  ? 0.2441 0.2244 0.2509 -0.0587 0.0571  -0.0085 26  GLU   A CG  
725  C CG  B GLU   A 26  ? 0.2010 0.2542 0.2470 -0.0433 0.0394  0.0058  26  GLU   A CG  
726  C CD  A GLU   A 26  ? 0.2501 0.2304 0.2889 -0.0645 0.0731  -0.0108 26  GLU   A CD  
727  C CD  B GLU   A 26  ? 0.2090 0.2701 0.2702 -0.0479 0.0511  0.0035  26  GLU   A CD  
728  O OE1 A GLU   A 26  ? 0.2457 0.2363 0.2984 -0.0583 0.1000  -0.0390 26  GLU   A OE1 
729  O OE1 B GLU   A 26  ? 0.2169 0.2909 0.2667 -0.0347 0.0809  -0.0079 26  GLU   A OE1 
730  O OE2 A GLU   A 26  ? 0.2557 0.2369 0.2841 -0.0651 0.0723  0.0027  26  GLU   A OE2 
731  O OE2 B GLU   A 26  ? 0.2137 0.2685 0.2399 -0.0543 0.0569  0.0051  26  GLU   A OE2 
744  N N   A ALA   A 27  ? 0.2024 0.2170 0.1486 -0.0564 0.0445  0.0051  27  ALA   A N   
745  N N   B ALA   A 27  ? 0.1455 0.2012 0.1395 -0.0038 0.0304  0.0305  27  ALA   A N   
746  C CA  A ALA   A 27  ? 0.2045 0.2263 0.1581 -0.0549 0.0425  0.0117  27  ALA   A CA  
747  C CA  B ALA   A 27  ? 0.1460 0.2020 0.1470 0.0055  0.0135  0.0350  27  ALA   A CA  
748  C C   A ALA   A 27  ? 0.2198 0.2441 0.1810 -0.0597 0.0440  0.0006  27  ALA   A C   
749  C C   B ALA   A 27  ? 0.1599 0.2086 0.1496 0.0066  0.0108  0.0146  27  ALA   A C   
750  O O   A ALA   A 27  ? 0.2263 0.2452 0.1796 -0.0606 0.0361  -0.0060 27  ALA   A O   
751  O O   B ALA   A 27  ? 0.1617 0.2116 0.1664 0.0093  0.0144  0.0042  27  ALA   A O   
752  C CB  A ALA   A 27  ? 0.1924 0.2155 0.1572 -0.0580 0.0376  0.0250  27  ALA   A CB  
753  C CB  B ALA   A 27  ? 0.1344 0.2010 0.1529 -0.0048 0.0045  0.0407  27  ALA   A CB  
764  N N   A LYS   A 28  ? 0.2398 0.2685 0.2173 -0.0496 0.0417  -0.0126 28  LYS   A N   
765  N N   B LYS   A 28  ? 0.1940 0.2224 0.1637 0.0242  0.0044  -0.0073 28  LYS   A N   
766  C CA  A LYS   A 28  ? 0.2714 0.2961 0.2584 -0.0364 0.0400  -0.0194 28  LYS   A CA  
767  C CA  B LYS   A 28  ? 0.2337 0.2548 0.1795 0.0445  -0.0018 -0.0248 28  LYS   A CA  
768  C C   A LYS   A 28  ? 0.2827 0.3183 0.2655 -0.0326 0.0440  -0.0192 28  LYS   A C   
769  C C   B LYS   A 28  ? 0.2565 0.2840 0.1800 0.0419  0.0032  -0.0128 28  LYS   A C   
770  O O   A LYS   A 28  ? 0.2844 0.3252 0.2906 -0.0290 0.0299  -0.0198 28  LYS   A O   
771  O O   B LYS   A 28  ? 0.2741 0.3016 0.2081 0.0351  -0.0166 -0.0032 28  LYS   A O   
772  C CB  A LYS   A 28  ? 0.2910 0.3061 0.3075 -0.0245 0.0378  -0.0203 28  LYS   A CB  
773  C CB  B LYS   A 28  ? 0.2585 0.2679 0.2286 0.0596  -0.0105 -0.0421 28  LYS   A CB  
774  C CG  A LYS   A 28  ? 0.3091 0.3185 0.3554 -0.0139 0.0335  -0.0181 28  LYS   A CG  
775  C CG  B LYS   A 28  ? 0.2831 0.2877 0.2923 0.0672  -0.0083 -0.0426 28  LYS   A CG  
776  C CD  A LYS   A 28  ? 0.3219 0.3325 0.3990 -0.0047 0.0265  -0.0164 28  LYS   A CD  
777  C CD  B LYS   A 28  ? 0.3066 0.3159 0.3736 0.0672  -0.0147 -0.0432 28  LYS   A CD  
778  C CE  A LYS   A 28  ? 0.3285 0.3399 0.4336 0.0000  0.0175  -0.0149 28  LYS   A CE  
779  C CE  B LYS   A 28  ? 0.3256 0.3353 0.4273 0.0626  -0.0199 -0.0496 28  LYS   A CE  
780  N NZ  A LYS   A 28  ? 0.3339 0.3419 0.4486 0.0029  0.0152  -0.0133 28  LYS   A NZ  
781  N NZ  B LYS   A 28  ? 0.3353 0.3430 0.4516 0.0623  -0.0274 -0.0503 28  LYS   A NZ  
808  N N   A LYS   A 29  ? 0.2904 0.3336 0.2577 -0.0345 0.0613  -0.0065 29  LYS   A N   
809  N N   B LYS   A 29  ? 0.2550 0.2961 0.1593 0.0441  0.0532  0.0044  29  LYS   A N   
810  C CA  A LYS   A 29  ? 0.3034 0.3509 0.2657 -0.0325 0.0691  0.0016  29  LYS   A CA  
811  C CA  B LYS   A 29  ? 0.2674 0.3212 0.1680 0.0383  0.0771  0.0275  29  LYS   A CA  
812  C C   A LYS   A 29  ? 0.2944 0.3423 0.2337 -0.0363 0.0615  0.0067  29  LYS   A C   
813  C C   B LYS   A 29  ? 0.2635 0.3146 0.1385 0.0268  0.0663  0.0342  29  LYS   A C   
814  O O   A LYS   A 29  ? 0.3003 0.3496 0.2426 -0.0288 0.0595  -0.0041 29  LYS   A O   
815  O O   B LYS   A 29  ? 0.2773 0.3291 0.1615 0.0305  0.0528  0.0245  29  LYS   A O   
816  C CB  A LYS   A 29  ? 0.3194 0.3730 0.3185 -0.0264 0.0827  0.0048  29  LYS   A CB  
817  C CB  B LYS   A 29  ? 0.2847 0.3495 0.2136 0.0417  0.1179  0.0368  29  LYS   A CB  
818  C CG  A LYS   A 29  ? 0.3350 0.3909 0.3749 -0.0211 0.0880  0.0047  29  LYS   A CG  
819  C CG  B LYS   A 29  ? 0.3115 0.3762 0.3020 0.0430  0.1322  0.0337  29  LYS   A CG  
820  C CD  A LYS   A 29  ? 0.3492 0.4055 0.4248 -0.0175 0.0884  0.0031  29  LYS   A CD  
821  C CD  B LYS   A 29  ? 0.3342 0.3969 0.3809 0.0433  0.1346  0.0287  29  LYS   A CD  
822  C CE  A LYS   A 29  ? 0.3593 0.4154 0.4630 -0.0154 0.0896  0.0048  29  LYS   A CE  
823  C CE  B LYS   A 29  ? 0.3489 0.4108 0.4420 0.0423  0.1373  0.0259  29  LYS   A CE  
824  N NZ  A LYS   A 29  ? 0.3650 0.4214 0.4815 -0.0141 0.0870  0.0051  29  LYS   A NZ  
825  N NZ  B LYS   A 29  ? 0.3567 0.4186 0.4741 0.0418  0.1322  0.0253  29  LYS   A NZ  
852  N N   A VAL   A 30  ? 0.2779 0.3237 0.2096 -0.0461 0.0511  0.0155  30  VAL   A N   
853  N N   B VAL   A 30  ? 0.2433 0.2909 0.1447 0.0126  0.0663  0.0397  30  VAL   A N   
854  C CA  A VAL   A 30  ? 0.2706 0.3058 0.1898 -0.0532 0.0338  0.0212  30  VAL   A CA  
855  C CA  B VAL   A 30  ? 0.2312 0.2700 0.1510 -0.0054 0.0469  0.0468  30  VAL   A CA  
856  C C   A VAL   A 30  ? 0.2634 0.2891 0.1613 -0.0465 0.0200  0.0255  30  VAL   A C   
857  C C   B VAL   A 30  ? 0.2276 0.2607 0.1446 -0.0043 0.0341  0.0404  30  VAL   A C   
858  O O   A VAL   A 30  ? 0.2685 0.2915 0.1729 -0.0407 0.0140  0.0287  30  VAL   A O   
859  O O   B VAL   A 30  ? 0.2374 0.2639 0.1637 -0.0120 0.0227  0.0504  30  VAL   A O   
860  C CB  A VAL   A 30  ? 0.2728 0.3072 0.2107 -0.0597 0.0234  0.0139  30  VAL   A CB  
861  C CB  B VAL   A 30  ? 0.2288 0.2610 0.1826 -0.0148 0.0238  0.0491  30  VAL   A CB  
862  C CG1 A VAL   A 30  ? 0.2759 0.3078 0.2248 -0.0598 0.0140  0.0044  30  VAL   A CG1 
863  C CG1 B VAL   A 30  ? 0.2390 0.2574 0.2124 -0.0145 0.0061  0.0355  30  VAL   A CG1 
864  C CG2 A VAL   A 30  ? 0.2743 0.3089 0.2334 -0.0640 0.0203  0.0175  30  VAL   A CG2 
865  C CG2 B VAL   A 30  ? 0.2241 0.2615 0.2132 -0.0229 0.0160  0.0659  30  VAL   A CG2 
884  N N   A LYS   A 31  ? 0.2472 0.2686 0.1445 -0.0453 0.0186  0.0197  31  LYS   A N   
885  N N   B LYS   A 31  ? 0.2215 0.2464 0.1394 0.0020  0.0350  0.0251  31  LYS   A N   
886  C CA  A LYS   A 31  ? 0.2486 0.2617 0.1519 -0.0360 0.0022  0.0224  31  LYS   A CA  
887  C CA  B LYS   A 31  ? 0.2303 0.2471 0.1572 0.0042  0.0104  0.0091  31  LYS   A CA  
888  C C   A LYS   A 31  ? 0.2383 0.2389 0.1136 -0.0335 -0.0102 0.0475  31  LYS   A C   
889  C C   B LYS   A 31  ? 0.2179 0.2318 0.1350 0.0080  0.0099  0.0240  31  LYS   A C   
890  O O   A LYS   A 31  ? 0.2452 0.2439 0.1163 -0.0297 -0.0203 0.0576  31  LYS   A O   
891  O O   B LYS   A 31  ? 0.2297 0.2390 0.1555 0.0187  0.0018  0.0070  31  LYS   A O   
892  C CB  A LYS   A 31  ? 0.2720 0.2827 0.2413 -0.0285 -0.0067 0.0033  31  LYS   A CB  
893  C CB  B LYS   A 31  ? 0.2595 0.2696 0.2333 0.0032  -0.0121 -0.0209 31  LYS   A CB  
894  C CG  A LYS   A 31  ? 0.2974 0.3044 0.3410 -0.0174 -0.0144 -0.0062 31  LYS   A CG  
895  C CG  B LYS   A 31  ? 0.2959 0.3037 0.3422 0.0056  -0.0260 -0.0361 31  LYS   A CG  
896  C CD  A LYS   A 31  ? 0.3220 0.3208 0.4188 -0.0110 -0.0196 -0.0137 31  LYS   A CD  
897  C CD  B LYS   A 31  ? 0.3203 0.3312 0.4366 0.0087  -0.0368 -0.0528 31  LYS   A CD  
898  C CE  A LYS   A 31  ? 0.3362 0.3294 0.4756 -0.0073 -0.0255 -0.0197 31  LYS   A CE  
899  C CE  B LYS   A 31  ? 0.3358 0.3444 0.5050 0.0057  -0.0478 -0.0612 31  LYS   A CE  
900  N NZ  A LYS   A 31  ? 0.3418 0.3326 0.5012 -0.0026 -0.0300 -0.0227 31  LYS   A NZ  
901  N NZ  B LYS   A 31  ? 0.3498 0.3570 0.5391 0.0058  -0.0490 -0.0668 31  LYS   A NZ  
928  N N   A PRO   A 32  ? 0.2197 0.2208 0.1016 -0.0340 -0.0072 0.0484  32  PRO   A N   
929  N N   B PRO   A 32  ? 0.1938 0.2180 0.1199 0.0034  0.0191  0.0306  32  PRO   A N   
930  C CA  A PRO   A 32  ? 0.2151 0.2116 0.1284 -0.0331 -0.0092 0.0540  32  PRO   A CA  
931  C CA  B PRO   A 32  ? 0.1958 0.2118 0.1367 0.0049  0.0068  0.0450  32  PRO   A CA  
932  C C   A PRO   A 32  ? 0.2084 0.2041 0.1312 -0.0274 -0.0020 0.0432  32  PRO   A C   
933  C C   B PRO   A 32  ? 0.2003 0.2078 0.1296 0.0083  0.0039  0.0468  32  PRO   A C   
934  O O   A PRO   A 32  ? 0.2038 0.1962 0.1276 -0.0328 0.0013  0.0302  32  PRO   A O   
935  O O   B PRO   A 32  ? 0.2005 0.2048 0.1494 0.0045  0.0015  0.0393  32  PRO   A O   
936  C CB  A PRO   A 32  ? 0.2139 0.2189 0.1458 -0.0350 -0.0070 0.0416  32  PRO   A CB  
937  C CB  B PRO   A 32  ? 0.1879 0.2169 0.1530 0.0014  0.0086  0.0311  32  PRO   A CB  
938  C CG  A PRO   A 32  ? 0.2138 0.2241 0.1234 -0.0319 -0.0143 0.0371  32  PRO   A CG  
939  C CG  B PRO   A 32  ? 0.1887 0.2249 0.1361 0.0001  -0.0033 0.0244  32  PRO   A CG  
940  C CD  A PRO   A 32  ? 0.2123 0.2187 0.0908 -0.0338 -0.0106 0.0421  32  PRO   A CD  
941  C CD  B PRO   A 32  ? 0.1858 0.2207 0.1122 -0.0012 0.0108  0.0201  32  PRO   A CD  
956  N N   A THR   A 33  ? 0.2111 0.2071 0.1437 -0.0189 -0.0055 0.0431  33  THR   A N   
957  N N   B THR   A 33  ? 0.2031 0.2104 0.1261 0.0083  -0.0050 0.0582  33  THR   A N   
958  C CA  A THR   A 33  ? 0.2091 0.2112 0.1567 -0.0075 -0.0203 0.0401  33  THR   A CA  
959  C CA  B THR   A 33  ? 0.2037 0.2103 0.1310 0.0156  -0.0241 0.0536  33  THR   A CA  
960  C C   A THR   A 33  ? 0.1858 0.1996 0.1537 -0.0088 -0.0209 0.0349  33  THR   A C   
961  C C   B THR   A 33  ? 0.1772 0.1890 0.1323 0.0016  -0.0191 0.0315  33  THR   A C   
962  O O   A THR   A 33  ? 0.1808 0.1977 0.1558 -0.0088 -0.0304 0.0367  33  THR   A O   
963  O O   B THR   A 33  ? 0.1695 0.1763 0.1320 -0.0025 -0.0117 0.0225  33  THR   A O   
964  C CB  A THR   A 33  ? 0.2257 0.2282 0.1822 0.0044  -0.0214 0.0448  33  THR   A CB  
965  C CB  B THR   A 33  ? 0.2301 0.2294 0.1431 0.0284  -0.0234 0.0739  33  THR   A CB  
966  O OG1 A THR   A 33  ? 0.2422 0.2418 0.2113 0.0082  -0.0122 0.0457  33  THR   A OG1 
967  O OG1 B THR   A 33  ? 0.2553 0.2508 0.1769 0.0306  -0.0307 0.0888  33  THR   A OG1 
968  C CG2 A THR   A 33  ? 0.2276 0.2308 0.1912 0.0117  -0.0298 0.0380  33  THR   A CG2 
969  C CG2 B THR   A 33  ? 0.2300 0.2306 0.1767 0.0332  -0.0219 0.0593  33  THR   A CG2 
984  N N   . VAL   A 34  ? 0.1692 0.1826 0.1222 -0.0154 -0.0091 0.0307  34  VAL   A N   
985  C CA  . VAL   A 34  ? 0.1593 0.1719 0.1208 -0.0115 -0.0030 0.0324  34  VAL   A CA  
986  C C   . VAL   A 34  ? 0.1518 0.1645 0.1057 -0.0138 -0.0005 0.0291  34  VAL   A C   
987  O O   . VAL   A 34  ? 0.1505 0.1641 0.1399 -0.0212 -0.0009 0.0270  34  VAL   A O   
988  C CB  . VAL   A 34  ? 0.1619 0.1674 0.1359 -0.0176 0.0019  0.0183  34  VAL   A CB  
989  C CG1 . VAL   A 34  ? 0.1763 0.1711 0.1224 -0.0099 0.0075  -0.0013 34  VAL   A CG1 
990  C CG2 . VAL   A 34  ? 0.1791 0.1779 0.1636 -0.0144 -0.0032 0.0209  34  VAL   A CG2 
1001 N N   . VAL   A 35  ? 0.1430 0.1538 0.1075 -0.0212 -0.0041 0.0253  35  VAL   A N   
1002 C CA  . VAL   A 35  ? 0.1332 0.1477 0.1099 -0.0185 0.0028  0.0170  35  VAL   A CA  
1003 C C   . VAL   A 35  ? 0.1285 0.1360 0.1133 -0.0107 0.0034  0.0168  35  VAL   A C   
1004 O O   . VAL   A 35  ? 0.1285 0.1488 0.1261 -0.0190 0.0109  0.0126  35  VAL   A O   
1005 C CB  . VAL   A 35  ? 0.1411 0.1591 0.1300 -0.0090 0.0118  0.0086  35  VAL   A CB  
1006 C CG1 . VAL   A 35  ? 0.1489 0.1590 0.1425 0.0006  0.0122  0.0041  35  VAL   A CG1 
1007 C CG2 . VAL   A 35  ? 0.1411 0.1603 0.1584 -0.0085 0.0195  0.0019  35  VAL   A CG2 
1017 N N   . VAL   A 36  ? 0.1203 0.1344 0.0977 -0.0100 0.0041  0.0213  36  VAL   A N   
1018 C CA  . VAL   A 36  ? 0.1079 0.1267 0.1134 -0.0071 0.0025  0.0070  36  VAL   A CA  
1019 C C   . VAL   A 36  ? 0.1119 0.1319 0.1117 -0.0085 0.0121  0.0156  36  VAL   A C   
1020 O O   . VAL   A 36  ? 0.1191 0.1316 0.1257 -0.0055 0.0105  0.0158  36  VAL   A O   
1021 C CB  . VAL   A 36  ? 0.1174 0.1234 0.1137 -0.0037 0.0037  0.0142  36  VAL   A CB  
1022 C CG1 . VAL   A 36  ? 0.1143 0.1314 0.1380 -0.0058 0.0040  0.0017  36  VAL   A CG1 
1023 C CG2 . VAL   A 36  ? 0.1270 0.1322 0.1330 -0.0084 -0.0023 0.0224  36  VAL   A CG2 
1033 N N   . ASN   A 37  ? 0.1131 0.1251 0.1041 0.0017  0.0082  0.0146  37  ASN   A N   
1034 C CA  . ASN   A 37  ? 0.1165 0.1249 0.0980 -0.0045 0.0035  0.0305  37  ASN   A CA  
1035 C C   . ASN   A 37  ? 0.1215 0.1204 0.1027 -0.0067 0.0090  0.0349  37  ASN   A C   
1036 O O   . ASN   A 37  ? 0.1209 0.1329 0.1053 0.0037  0.0068  0.0206  37  ASN   A O   
1037 C CB  . ASN   A 37  ? 0.1148 0.1252 0.1254 0.0018  0.0102  0.0235  37  ASN   A CB  
1038 C CG  . ASN   A 37  ? 0.1217 0.1215 0.1362 -0.0020 0.0123  0.0206  37  ASN   A CG  
1039 O OD1 . ASN   A 37  ? 0.1200 0.1220 0.1543 -0.0014 0.0062  0.0218  37  ASN   A OD1 
1040 N ND2 . ASN   A 37  ? 0.1293 0.1143 0.1482 -0.0045 -0.0030 0.0286  37  ASN   A ND2 
1047 N N   A ALA   A 38  ? 0.1176 0.1230 0.1182 -0.0039 -0.0001 0.0222  38  ALA   A N   
1048 N N   B ALA   A 38  ? 0.1188 0.1257 0.1184 -0.0005 0.0034  0.0294  38  ALA   A N   
1049 C CA  A ALA   A 38  ? 0.1229 0.1235 0.1156 -0.0051 -0.0123 0.0124  38  ALA   A CA  
1050 C CA  B ALA   A 38  ? 0.1291 0.1320 0.1223 -0.0086 -0.0014 0.0317  38  ALA   A CA  
1051 C C   A ALA   A 38  ? 0.1143 0.1243 0.1304 0.0062  -0.0180 0.0016  38  ALA   A C   
1052 C C   B ALA   A 38  ? 0.1225 0.1379 0.1198 -0.0038 -0.0068 0.0262  38  ALA   A C   
1053 O O   A ALA   A 38  ? 0.1042 0.1104 0.1339 0.0075  -0.0167 -0.0063 38  ALA   A O   
1054 O O   B ALA   A 38  ? 0.1256 0.1310 0.1450 -0.0065 -0.0077 0.0343  38  ALA   A O   
1055 C CB  A ALA   A 38  ? 0.1183 0.1275 0.1186 -0.0125 -0.0220 0.0224  38  ALA   A CB  
1056 C CB  B ALA   A 38  ? 0.1297 0.1356 0.1373 -0.0072 -0.0083 0.0257  38  ALA   A CB  
1067 N N   A ALA   A 39  ? 0.1191 0.1245 0.1445 0.0090  -0.0131 0.0059  39  ALA   A N   
1068 N N   B ALA   A 39  ? 0.1256 0.1413 0.1282 -0.0014 0.0087  0.0403  39  ALA   A N   
1069 C CA  A ALA   A 39  ? 0.1197 0.1238 0.1417 0.0067  -0.0071 0.0125  39  ALA   A CA  
1070 C CA  B ALA   A 39  ? 0.1190 0.1458 0.1177 -0.0015 0.0122  0.0267  39  ALA   A CA  
1071 C C   A ALA   A 39  ? 0.1224 0.1295 0.1272 -0.0042 -0.0179 0.0119  39  ALA   A C   
1072 C C   B ALA   A 39  ? 0.1210 0.1334 0.1148 -0.0042 0.0041  0.0120  39  ALA   A C   
1073 O O   A ALA   A 39  ? 0.1414 0.1329 0.1441 -0.0097 -0.0067 0.0112  39  ALA   A O   
1074 O O   B ALA   A 39  ? 0.1427 0.1296 0.1231 -0.0059 0.0084  -0.0009 39  ALA   A O   
1075 C CB  A ALA   A 39  ? 0.1211 0.1203 0.1478 0.0006  -0.0146 0.0050  39  ALA   A CB  
1076 C CB  B ALA   A 39  ? 0.1340 0.1619 0.1331 -0.0037 0.0083  0.0213  39  ALA   A CB  
1087 N N   A ASN   A 40  ? 0.1187 0.1336 0.1260 -0.0087 -0.0067 0.0113  40  ASN   A N   
1088 N N   B ASN   A 40  ? 0.1165 0.1257 0.1110 -0.0011 0.0111  0.0113  40  ASN   A N   
1089 C CA  A ASN   A 40  ? 0.1287 0.1379 0.1294 -0.0075 -0.0064 0.0024  40  ASN   A CA  
1090 C CA  B ASN   A 40  ? 0.1212 0.1206 0.1119 -0.0004 0.0017  0.0181  40  ASN   A CA  
1091 C C   A ASN   A 40  ? 0.1263 0.1266 0.1264 0.0047  -0.0075 0.0094  40  ASN   A C   
1092 C C   B ASN   A 40  ? 0.1228 0.1140 0.0978 -0.0029 0.0155  0.0233  40  ASN   A C   
1093 O O   A ASN   A 40  ? 0.1274 0.1319 0.1264 0.0101  0.0029  0.0062  40  ASN   A O   
1094 O O   B ASN   A 40  ? 0.1132 0.1144 0.1101 -0.0087 0.0082  0.0228  40  ASN   A O   
1095 C CB  A ASN   A 40  ? 0.1378 0.1470 0.1509 -0.0020 -0.0087 -0.0020 40  ASN   A CB  
1096 C CB  B ASN   A 40  ? 0.1350 0.1223 0.1247 0.0054  -0.0129 0.0143  40  ASN   A CB  
1097 C CG  A ASN   A 40  ? 0.1500 0.1495 0.1836 -0.0053 -0.0103 -0.0020 40  ASN   A CG  
1098 C CG  B ASN   A 40  ? 0.1501 0.1129 0.1213 -0.0016 -0.0118 0.0176  40  ASN   A CG  
1099 O OD1 A ASN   A 40  ? 0.1507 0.1450 0.1776 -0.0036 -0.0153 0.0014  40  ASN   A OD1 
1100 O OD1 B ASN   A 40  ? 0.1571 0.1111 0.1526 -0.0062 0.0037  0.0198  40  ASN   A OD1 
1101 N ND2 A ASN   A 40  ? 0.1564 0.1602 0.2128 0.0033  -0.0232 -0.0065 40  ASN   A ND2 
1102 N ND2 B ASN   A 40  ? 0.1595 0.1238 0.1596 0.0093  -0.0230 -0.0029 40  ASN   A ND2 
1115 N N   A VAL   A 41  ? 0.1316 0.1281 0.1303 -0.0009 -0.0042 0.0071  41  VAL   A N   
1116 N N   B VAL   A 41  ? 0.1293 0.1261 0.1036 0.0020  0.0147  0.0199  41  VAL   A N   
1117 C CA  A VAL   A 41  ? 0.1408 0.1265 0.1488 0.0016  0.0045  0.0026  41  VAL   A CA  
1118 C CA  B VAL   A 41  ? 0.1368 0.1315 0.1108 -0.0025 0.0267  0.0228  41  VAL   A CA  
1119 C C   A VAL   A 41  ? 0.1342 0.1222 0.1482 0.0059  -0.0101 0.0088  41  VAL   A C   
1120 C C   B VAL   A 41  ? 0.1342 0.1302 0.1198 -0.0036 0.0223  0.0145  41  VAL   A C   
1121 O O   A VAL   A 41  ? 0.1445 0.1153 0.1684 0.0098  -0.0264 0.0120  41  VAL   A O   
1122 O O   B VAL   A 41  ? 0.1478 0.1287 0.1107 -0.0078 0.0291  0.0118  41  VAL   A O   
1123 C CB  A VAL   A 41  ? 0.1536 0.1295 0.1471 -0.0050 0.0025  -0.0131 41  VAL   A CB  
1124 C CB  B VAL   A 41  ? 0.1704 0.1441 0.1307 -0.0075 0.0467  0.0252  41  VAL   A CB  
1125 C CG1 A VAL   A 41  ? 0.1478 0.1230 0.1454 0.0039  -0.0112 -0.0136 41  VAL   A CG1 
1126 C CG1 B VAL   A 41  ? 0.1891 0.1502 0.1618 -0.0076 0.0540  0.0186  41  VAL   A CG1 
1127 C CG2 A VAL   A 41  ? 0.1717 0.1420 0.1583 -0.0112 0.0079  -0.0210 41  VAL   A CG2 
1128 C CG2 B VAL   A 41  ? 0.1941 0.1541 0.1288 -0.0114 0.0582  0.0254  41  VAL   A CG2 
1147 N N   A TYR   A 42  ? 0.1154 0.1224 0.1518 0.0022  0.0055  0.0136  42  TYR   A N   
1148 N N   B TYR   A 42  ? 0.1224 0.1268 0.1346 -0.0030 0.0283  0.0217  42  TYR   A N   
1149 C CA  A TYR   A 42  ? 0.1201 0.1203 0.1486 -0.0060 0.0018  0.0219  42  TYR   A CA  
1150 C CA  B TYR   A 42  ? 0.1243 0.1228 0.1307 -0.0007 0.0335  0.0289  42  TYR   A CA  
1151 C C   A TYR   A 42  ? 0.1245 0.1129 0.1400 -0.0020 0.0041  0.0148  42  TYR   A C   
1152 C C   B TYR   A 42  ? 0.1294 0.1239 0.1216 -0.0063 0.0356  0.0329  42  TYR   A C   
1153 O O   A TYR   A 42  ? 0.1276 0.1031 0.1559 -0.0070 0.0004  0.0034  42  TYR   A O   
1154 O O   B TYR   A 42  ? 0.1274 0.1251 0.1416 -0.0147 0.0266  0.0180  42  TYR   A O   
1155 C CB  A TYR   A 42  ? 0.1260 0.1391 0.1475 -0.0060 0.0099  0.0334  42  TYR   A CB  
1156 C CB  B TYR   A 42  ? 0.1396 0.1341 0.1384 0.0038  0.0266  0.0423  42  TYR   A CB  
1157 C CG  A TYR   A 42  ? 0.1297 0.1476 0.1378 -0.0063 0.0127  0.0361  42  TYR   A CG  
1158 C CG  B TYR   A 42  ? 0.1432 0.1424 0.1343 0.0153  0.0115  0.0389  42  TYR   A CG  
1159 C CD1 A TYR   A 42  ? 0.1336 0.1538 0.1433 -0.0159 0.0164  0.0353  42  TYR   A CD1 
1160 C CD1 B TYR   A 42  ? 0.1465 0.1453 0.1351 0.0077  0.0198  0.0362  42  TYR   A CD1 
1161 C CD2 A TYR   A 42  ? 0.1319 0.1573 0.1499 -0.0011 0.0032  0.0270  42  TYR   A CD2 
1162 C CD2 B TYR   A 42  ? 0.1512 0.1663 0.1715 0.0217  0.0077  0.0263  42  TYR   A CD2 
1163 C CE1 A TYR   A 42  ? 0.1371 0.1586 0.1392 -0.0161 0.0095  0.0230  42  TYR   A CE1 
1164 C CE1 B TYR   A 42  ? 0.1516 0.1576 0.1443 0.0046  0.0212  0.0281  42  TYR   A CE1 
1165 C CE2 A TYR   A 42  ? 0.1339 0.1605 0.1553 -0.0105 0.0125  0.0266  42  TYR   A CE2 
1166 C CE2 B TYR   A 42  ? 0.1602 0.1758 0.1860 0.0204  0.0055  0.0345  42  TYR   A CE2 
1167 C CZ  A TYR   A 42  ? 0.1405 0.1663 0.1411 -0.0106 0.0157  0.0270  42  TYR   A CZ  
1168 C CZ  B TYR   A 42  ? 0.1634 0.1755 0.1621 0.0067  0.0145  0.0238  42  TYR   A CZ  
1169 O OH  A TYR   A 42  ? 0.1496 0.1751 0.1564 -0.0029 0.0114  0.0233  42  TYR   A OH  
1170 O OH  B TYR   A 42  ? 0.1678 0.1936 0.1785 -0.0002 0.0156  0.0216  42  TYR   A OH  
1189 N N   . LEU   A 43  ? 0.1299 0.1229 0.1230 -0.0099 0.0155  0.0057  43  LEU   A N   
1190 C CA  . LEU   A 43  ? 0.1197 0.1246 0.1227 -0.0129 0.0032  0.0142  43  LEU   A CA  
1191 C C   . LEU   A 43  ? 0.1264 0.1212 0.1350 -0.0076 0.0045  0.0097  43  LEU   A C   
1192 O O   . LEU   A 43  ? 0.1437 0.1262 0.1535 0.0008  -0.0090 0.0035  43  LEU   A O   
1193 C CB  . LEU   A 43  ? 0.1273 0.1219 0.1420 -0.0102 0.0048  0.0157  43  LEU   A CB  
1194 C CG  . LEU   A 43  ? 0.1327 0.1195 0.1548 0.0004  0.0020  0.0094  43  LEU   A CG  
1195 C CD1 . LEU   A 43  ? 0.1392 0.1313 0.1855 -0.0037 0.0011  0.0177  43  LEU   A CD1 
1196 C CD2 . LEU   A 43  ? 0.1432 0.1232 0.1426 -0.0081 0.0038  0.0229  43  LEU   A CD2 
1209 N N   A LYS   A 44  ? 0.1350 0.1232 0.1321 -0.0044 0.0095  0.0142  44  LYS   A N   
1210 N N   B LYS   A 44  ? 0.1336 0.1217 0.1233 0.0003  0.0044  0.0138  44  LYS   A N   
1211 C CA  A LYS   A 44  ? 0.1455 0.1279 0.1407 -0.0054 0.0179  0.0227  44  LYS   A CA  
1212 C CA  B LYS   A 44  ? 0.1452 0.1282 0.1255 0.0049  0.0091  0.0166  44  LYS   A CA  
1213 C C   A LYS   A 44  ? 0.1320 0.1196 0.1370 0.0000  0.0102  0.0105  44  LYS   A C   
1214 C C   B LYS   A 44  ? 0.1372 0.1252 0.1287 0.0053  -0.0037 0.0102  44  LYS   A C   
1215 O O   A LYS   A 44  ? 0.1395 0.1327 0.1566 0.0012  0.0024  0.0014  44  LYS   A O   
1216 O O   B LYS   A 44  ? 0.1455 0.1378 0.1459 0.0002  -0.0138 -0.0071 44  LYS   A O   
1217 C CB  A LYS   A 44  ? 0.1737 0.1422 0.1800 -0.0121 0.0278  0.0315  44  LYS   A CB  
1218 C CB  B LYS   A 44  ? 0.1738 0.1378 0.1665 0.0088  0.0224  0.0122  44  LYS   A CB  
1219 C CG  A LYS   A 44  ? 0.2059 0.1777 0.2461 -0.0213 0.0444  0.0367  44  LYS   A CG  
1220 C CG  B LYS   A 44  ? 0.2080 0.1824 0.2466 0.0038  0.0405  0.0101  44  LYS   A CG  
1221 C CD  A LYS   A 44  ? 0.2424 0.2256 0.3182 -0.0266 0.0364  0.0311  44  LYS   A CD  
1222 C CD  B LYS   A 44  ? 0.2486 0.2428 0.3340 -0.0094 0.0265  0.0109  44  LYS   A CD  
1223 C CE  A LYS   A 44  ? 0.2638 0.2550 0.3630 -0.0271 0.0330  0.0240  44  LYS   A CE  
1224 C CE  B LYS   A 44  ? 0.2681 0.2706 0.3804 -0.0180 0.0188  0.0111  44  LYS   A CE  
1225 N NZ  A LYS   A 44  ? 0.2729 0.2738 0.3828 -0.0282 0.0382  0.0241  44  LYS   A NZ  
1226 N NZ  B LYS   A 44  ? 0.2775 0.2905 0.4013 -0.0248 0.0234  0.0191  44  LYS   A NZ  
1253 N N   A HIS   A 45  ? 0.1189 0.1080 0.1310 -0.0045 0.0142  0.0084  45  HIS   A N   
1254 N N   B HIS   A 45  ? 0.1323 0.1212 0.1343 -0.0039 -0.0039 0.0186  45  HIS   A N   
1255 C CA  A HIS   A 45  ? 0.1177 0.1062 0.1228 0.0038  0.0143  0.0046  45  HIS   A CA  
1256 C CA  B HIS   A 45  ? 0.1309 0.1252 0.1336 0.0014  -0.0065 0.0179  45  HIS   A CA  
1257 C C   A HIS   A 45  ? 0.1199 0.1130 0.1352 0.0044  0.0083  0.0068  45  HIS   A C   
1258 C C   B HIS   A 45  ? 0.1336 0.1350 0.1396 0.0036  -0.0128 0.0152  45  HIS   A C   
1259 O O   A HIS   A 45  ? 0.1250 0.1114 0.1544 -0.0076 0.0126  0.0038  45  HIS   A O   
1260 O O   B HIS   A 45  ? 0.1516 0.1464 0.1675 0.0123  -0.0079 0.0044  45  HIS   A O   
1261 C CB  A HIS   A 45  ? 0.1207 0.1099 0.1217 0.0007  0.0159  0.0025  45  HIS   A CB  
1262 C CB  B HIS   A 45  ? 0.1321 0.1299 0.1330 -0.0010 -0.0025 0.0161  45  HIS   A CB  
1263 C CG  A HIS   A 45  ? 0.1222 0.1013 0.1106 -0.0000 0.0064  0.0065  45  HIS   A CG  
1264 C CG  B HIS   A 45  ? 0.1255 0.1234 0.1166 -0.0045 0.0139  0.0208  45  HIS   A CG  
1265 N ND1 A HIS   A 45  ? 0.1210 0.1026 0.1137 -0.0018 0.0040  -0.0014 45  HIS   A ND1 
1266 N ND1 B HIS   A 45  ? 0.1225 0.1275 0.1449 0.0019  -0.0039 0.0217  45  HIS   A ND1 
1267 C CD2 A HIS   A 45  ? 0.1248 0.1158 0.1197 0.0025  -0.0051 0.0095  45  HIS   A CD2 
1268 C CD2 B HIS   A 45  ? 0.1177 0.1175 0.1073 -0.0033 0.0078  0.0053  45  HIS   A CD2 
1269 C CE1 A HIS   A 45  ? 0.1275 0.1211 0.1274 -0.0029 0.0032  0.0140  45  HIS   A CE1 
1270 C CE1 B HIS   A 45  ? 0.1155 0.1204 0.1090 -0.0024 -0.0070 0.0058  45  HIS   A CE1 
1271 N NE2 A HIS   A 45  ? 0.1306 0.1204 0.1351 0.0078  0.0033  0.0174  45  HIS   A NE2 
1272 N NE2 B HIS   A 45  ? 0.1116 0.1113 0.1060 -0.0028 0.0012  -0.0007 45  HIS   A NE2 
1287 N N   A GLY   A 46  ? 0.1227 0.1206 0.1589 0.0119  -0.0179 0.0160  46  GLY   A N   
1288 N N   B GLY   A 46  ? 0.1264 0.1322 0.1597 -0.0092 -0.0236 0.0257  46  GLY   A N   
1289 C CA  A GLY   A 46  ? 0.1260 0.1286 0.1843 0.0135  -0.0157 0.0175  46  GLY   A CA  
1290 C CA  B GLY   A 46  ? 0.1297 0.1388 0.1706 -0.0052 -0.0227 0.0356  46  GLY   A CA  
1291 C C   A GLY   A 46  ? 0.1302 0.1236 0.1725 0.0155  -0.0142 0.0331  46  GLY   A C   
1292 C C   B GLY   A 46  ? 0.1316 0.1334 0.1556 0.0022  0.0015  0.0321  46  GLY   A C   
1293 O O   A GLY   A 46  ? 0.1421 0.1232 0.1697 0.0131  -0.0264 0.0506  46  GLY   A O   
1294 O O   B GLY   A 46  ? 0.1526 0.1517 0.1679 0.0021  -0.0093 0.0163  46  GLY   A O   
1301 N N   A GLY   A 47  ? 0.1206 0.1306 0.1627 0.0140  -0.0107 0.0293  47  GLY   A N   
1302 N N   B GLY   A 47  ? 0.1351 0.1348 0.1543 -0.0015 0.0127  0.0154  47  GLY   A N   
1303 C CA  A GLY   A 47  ? 0.1193 0.1390 0.1478 0.0216  -0.0215 0.0248  47  GLY   A CA  
1304 C CA  B GLY   A 47  ? 0.1287 0.1387 0.1493 0.0003  -0.0013 0.0124  47  GLY   A CA  
1305 C C   A GLY   A 47  ? 0.1177 0.1369 0.1411 0.0156  -0.0164 0.0247  47  GLY   A C   
1306 C C   B GLY   A 47  ? 0.1197 0.1243 0.1317 0.0059  0.0037  -0.0007 47  GLY   A C   
1307 O O   A GLY   A 47  ? 0.1142 0.1338 0.1606 0.0123  -0.0214 0.0296  47  GLY   A O   
1308 O O   B GLY   A 47  ? 0.1166 0.1185 0.1440 0.0076  -0.0032 0.0095  47  GLY   A O   
1315 N N   A GLY   A 48  ? 0.1133 0.1322 0.1300 0.0181  -0.0085 0.0210  48  GLY   A N   
1316 N N   B GLY   A 48  ? 0.1187 0.1242 0.1414 0.0051  0.0089  -0.0001 48  GLY   A N   
1317 C CA  A GLY   A 48  ? 0.1040 0.1321 0.1439 0.0137  0.0008  0.0081  48  GLY   A CA  
1318 C CA  B GLY   A 48  ? 0.1146 0.1203 0.1289 0.0042  -0.0032 -0.0100 48  GLY   A CA  
1319 C C   A GLY   A 48  ? 0.1084 0.1261 0.1318 -0.0002 0.0091  0.0148  48  GLY   A C   
1320 C C   B GLY   A 48  ? 0.1202 0.1211 0.1231 0.0023  0.0077  0.0068  48  GLY   A C   
1321 O O   A GLY   A 48  ? 0.1220 0.1287 0.1288 -0.0070 -0.0013 0.0141  48  GLY   A O   
1322 O O   B GLY   A 48  ? 0.1373 0.1291 0.1175 0.0039  0.0082  -0.0037 48  GLY   A O   
1329 N N   A VAL   A 49  ? 0.1161 0.1245 0.1522 -0.0021 -0.0041 0.0169  49  VAL   A N   
1330 N N   B VAL   A 49  ? 0.1184 0.1170 0.1387 -0.0037 -0.0096 0.0017  49  VAL   A N   
1331 C CA  A VAL   A 49  ? 0.1253 0.1249 0.1481 -0.0069 -0.0037 0.0314  49  VAL   A CA  
1332 C CA  B VAL   A 49  ? 0.1187 0.1152 0.1243 -0.0089 -0.0016 0.0143  49  VAL   A CA  
1333 C C   A VAL   A 49  ? 0.1270 0.1238 0.1187 -0.0006 -0.0070 0.0422  49  VAL   A C   
1334 C C   B VAL   A 49  ? 0.1281 0.1116 0.1126 -0.0060 0.0030  -0.0110 49  VAL   A C   
1335 O O   A VAL   A 49  ? 0.1282 0.1340 0.1178 -0.0018 -0.0100 0.0341  49  VAL   A O   
1336 O O   B VAL   A 49  ? 0.1258 0.1163 0.1152 -0.0070 0.0110  -0.0116 49  VAL   A O   
1337 C CB  A VAL   A 49  ? 0.1376 0.1279 0.1707 -0.0087 -0.0079 0.0114  49  VAL   A CB  
1338 C CB  B VAL   A 49  ? 0.1140 0.1175 0.1515 -0.0033 -0.0081 0.0155  49  VAL   A CB  
1339 C CG1 A VAL   A 49  ? 0.1402 0.1269 0.1732 -0.0003 0.0008  0.0091  49  VAL   A CG1 
1340 C CG1 B VAL   A 49  ? 0.1075 0.1170 0.1484 -0.0021 -0.0096 0.0178  49  VAL   A CG1 
1341 C CG2 A VAL   A 49  ? 0.1457 0.1348 0.2089 -0.0246 -0.0074 0.0005  49  VAL   A CG2 
1342 C CG2 B VAL   A 49  ? 0.1161 0.1231 0.1893 -0.0023 -0.0052 0.0169  49  VAL   A CG2 
1361 N N   A ALA   A 50  ? 0.1228 0.1235 0.1122 -0.0008 -0.0161 0.0400  50  ALA   A N   
1362 N N   B ALA   A 50  ? 0.1245 0.1132 0.1162 -0.0061 -0.0035 -0.0211 50  ALA   A N   
1363 C CA  A ALA   A 50  ? 0.1238 0.1209 0.1092 -0.0092 -0.0209 0.0558  50  ALA   A CA  
1364 C CA  B ALA   A 50  ? 0.1220 0.1149 0.1145 -0.0161 0.0054  -0.0162 50  ALA   A CA  
1365 C C   A ALA   A 50  ? 0.1145 0.1213 0.1069 -0.0039 -0.0199 0.0447  50  ALA   A C   
1366 C C   B ALA   A 50  ? 0.1172 0.1135 0.1190 -0.0105 0.0075  -0.0171 50  ALA   A C   
1367 O O   A ALA   A 50  ? 0.1122 0.1233 0.1163 0.0013  -0.0233 0.0523  50  ALA   A O   
1368 O O   B ALA   A 50  ? 0.1198 0.1179 0.1273 -0.0105 0.0110  -0.0290 50  ALA   A O   
1369 C CB  A ALA   A 50  ? 0.1245 0.1228 0.1251 -0.0025 -0.0297 0.0484  50  ALA   A CB  
1370 C CB  B ALA   A 50  ? 0.1219 0.1147 0.1260 -0.0102 0.0172  -0.0338 50  ALA   A CB  
1381 N N   A GLY   A 51  ? 0.1166 0.1140 0.1216 0.0039  -0.0259 0.0344  51  GLY   A N   
1382 N N   B GLY   A 51  ? 0.1207 0.1102 0.1362 0.0024  -0.0092 -0.0098 51  GLY   A N   
1383 C CA  A GLY   A 51  ? 0.1214 0.1149 0.1538 0.0030  -0.0160 0.0341  51  GLY   A CA  
1384 C CA  B GLY   A 51  ? 0.1303 0.1076 0.1409 0.0003  -0.0188 -0.0091 51  GLY   A CA  
1385 C C   A GLY   A 51  ? 0.1091 0.1255 0.1616 0.0018  -0.0044 0.0272  51  GLY   A C   
1386 C C   B GLY   A 51  ? 0.1226 0.1170 0.1344 0.0076  -0.0101 -0.0189 51  GLY   A C   
1387 O O   A GLY   A 51  ? 0.1221 0.1352 0.1655 -0.0024 -0.0118 0.0365  51  GLY   A O   
1388 O O   B GLY   A 51  ? 0.1294 0.1261 0.1414 -0.0020 -0.0065 -0.0308 51  GLY   A O   
1395 N N   A ALA   A 52  ? 0.1083 0.1325 0.1587 -0.0085 0.0063  0.0220  52  ALA   A N   
1396 N N   B ALA   A 52  ? 0.1279 0.1218 0.1087 0.0043  -0.0176 -0.0174 52  ALA   A N   
1397 C CA  A ALA   A 52  ? 0.1133 0.1367 0.1536 -0.0095 0.0088  0.0120  52  ALA   A CA  
1398 C CA  B ALA   A 52  ? 0.1312 0.1277 0.1323 0.0010  -0.0067 -0.0202 52  ALA   A CA  
1399 C C   A ALA   A 52  ? 0.1235 0.1425 0.1425 0.0036  0.0149  0.0153  52  ALA   A C   
1400 C C   B ALA   A 52  ? 0.1305 0.1292 0.1107 -0.0053 0.0053  -0.0192 52  ALA   A C   
1401 O O   A ALA   A 52  ? 0.1279 0.1429 0.1543 0.0147  0.0172  0.0180  52  ALA   A O   
1402 O O   B ALA   A 52  ? 0.1364 0.1392 0.1350 -0.0125 0.0037  -0.0253 52  ALA   A O   
1403 C CB  A ALA   A 52  ? 0.1133 0.1543 0.1560 -0.0140 0.0055  0.0045  52  ALA   A CB  
1404 C CB  B ALA   A 52  ? 0.1401 0.1461 0.1400 0.0080  -0.0144 -0.0195 52  ALA   A CB  
1415 N N   A LEU   A 53  ? 0.1236 0.1388 0.1389 0.0027  0.0125  0.0201  53  LEU   A N   
1416 N N   B LEU   A 53  ? 0.1202 0.1148 0.1148 -0.0147 -0.0023 -0.0067 53  LEU   A N   
1417 C CA  A LEU   A 53  ? 0.1336 0.1378 0.1389 -0.0009 0.0108  0.0197  53  LEU   A CA  
1418 C CA  B LEU   A 53  ? 0.1296 0.1237 0.1109 -0.0088 -0.0033 -0.0032 53  LEU   A CA  
1419 C C   A LEU   A 53  ? 0.1294 0.1361 0.1291 0.0054  0.0060  0.0024  53  LEU   A C   
1420 C C   B LEU   A 53  ? 0.1159 0.1263 0.0836 0.0073  -0.0075 0.0032  53  LEU   A C   
1421 O O   A LEU   A 53  ? 0.1371 0.1296 0.1317 0.0046  0.0174  -0.0032 53  LEU   A O   
1422 O O   B LEU   A 53  ? 0.1289 0.1302 0.0974 0.0007  -0.0042 0.0108  53  LEU   A O   
1423 C CB  A LEU   A 53  ? 0.1314 0.1392 0.1286 -0.0042 0.0104  0.0339  53  LEU   A CB  
1424 C CB  B LEU   A 53  ? 0.1267 0.1310 0.1099 -0.0067 -0.0020 -0.0028 53  LEU   A CB  
1425 C CG  A LEU   A 53  ? 0.1332 0.1392 0.1345 -0.0139 -0.0050 0.0388  53  LEU   A CG  
1426 C CG  B LEU   A 53  ? 0.1322 0.1325 0.1292 -0.0096 -0.0076 0.0011  53  LEU   A CG  
1427 C CD1 A LEU   A 53  ? 0.1295 0.1425 0.1510 -0.0098 -0.0118 0.0391  53  LEU   A CD1 
1428 C CD1 B LEU   A 53  ? 0.1386 0.1365 0.1352 -0.0063 0.0027  -0.0113 53  LEU   A CD1 
1429 C CD2 A LEU   A 53  ? 0.1336 0.1529 0.1231 -0.0179 -0.0192 0.0384  53  LEU   A CD2 
1430 C CD2 B LEU   A 53  ? 0.1375 0.1435 0.1421 -0.0128 -0.0088 0.0090  53  LEU   A CD2 
1453 N N   A ASN   A 54  ? 0.1282 0.1334 0.1343 -0.0073 -0.0050 0.0055  54  ASN   A N   
1454 N N   B ASN   A 54  ? 0.1160 0.1301 0.0878 -0.0016 -0.0030 0.0064  54  ASN   A N   
1455 C CA  A ASN   A 54  ? 0.1227 0.1281 0.1404 -0.0122 -0.0046 0.0021  54  ASN   A CA  
1456 C CA  B ASN   A 54  ? 0.1105 0.1301 0.1016 -0.0011 -0.0011 0.0018  54  ASN   A CA  
1457 C C   A ASN   A 54  ? 0.1263 0.1323 0.1342 -0.0119 -0.0041 -0.0012 54  ASN   A C   
1458 C C   B ASN   A 54  ? 0.1224 0.1359 0.1121 -0.0052 -0.0048 -0.0013 54  ASN   A C   
1459 O O   A ASN   A 54  ? 0.1237 0.1366 0.1426 -0.0161 -0.0041 -0.0071 54  ASN   A O   
1460 O O   B ASN   A 54  ? 0.1207 0.1450 0.1238 -0.0019 -0.0123 -0.0136 54  ASN   A O   
1461 C CB  A ASN   A 54  ? 0.1182 0.1245 0.1506 -0.0179 -0.0122 0.0054  54  ASN   A CB  
1462 C CB  B ASN   A 54  ? 0.1069 0.1281 0.1110 0.0040  -0.0186 0.0067  54  ASN   A CB  
1463 C CG  A ASN   A 54  ? 0.1263 0.1345 0.1541 -0.0122 -0.0121 0.0052  54  ASN   A CG  
1464 C CG  B ASN   A 54  ? 0.1178 0.1277 0.1022 0.0057  -0.0183 -0.0101 54  ASN   A CG  
1465 O OD1 A ASN   A 54  ? 0.1227 0.1304 0.1644 -0.0110 -0.0022 0.0216  54  ASN   A OD1 
1466 O OD1 B ASN   A 54  ? 0.1171 0.1208 0.1090 0.0031  -0.0165 -0.0244 54  ASN   A OD1 
1467 N ND2 A ASN   A 54  ? 0.1214 0.1397 0.1594 -0.0027 -0.0142 0.0136  54  ASN   A ND2 
1468 N ND2 B ASN   A 54  ? 0.1143 0.1244 0.1241 0.0029  -0.0113 0.0108  54  ASN   A ND2 
1481 N N   . LYS   A 55  ? 0.1259 0.1329 0.1228 -0.0006 -0.0043 -0.0005 55  LYS   A N   
1482 C CA  . LYS   A 55  ? 0.1382 0.1444 0.1413 0.0094  -0.0045 -0.0105 55  LYS   A CA  
1483 C C   . LYS   A 55  ? 0.1280 0.1443 0.1469 -0.0034 -0.0005 -0.0113 55  LYS   A C   
1484 O O   . LYS   A 55  ? 0.1377 0.1532 0.1496 0.0024  -0.0045 -0.0247 55  LYS   A O   
1485 C CB  . LYS   A 55  ? 0.1450 0.1557 0.1614 0.0194  -0.0095 -0.0187 55  LYS   A CB  
1486 C CG  . LYS   A 55  ? 0.1722 0.1917 0.1826 0.0402  -0.0241 -0.0311 55  LYS   A CG  
1487 C CD  . LYS   A 55  ? 0.1941 0.2143 0.2107 0.0562  -0.0232 -0.0235 55  LYS   A CD  
1488 C CE  . LYS   A 55  ? 0.2118 0.2445 0.2385 0.0670  -0.0226 -0.0242 55  LYS   A CE  
1489 N NZ  . LYS   A 55  ? 0.2291 0.2754 0.2654 0.0656  -0.0221 -0.0257 55  LYS   A NZ  
1504 N N   . ALA   A 56  ? 0.1389 0.1496 0.1397 -0.0077 0.0046  -0.0099 56  ALA   A N   
1505 C CA  . ALA   A 56  ? 0.1472 0.1703 0.1328 -0.0062 0.0090  -0.0096 56  ALA   A CA  
1506 C C   . ALA   A 56  ? 0.1568 0.1815 0.1147 -0.0058 0.0124  -0.0226 56  ALA   A C   
1507 O O   . ALA   A 56  ? 0.1632 0.2138 0.1217 0.0034  0.0066  -0.0130 56  ALA   A O   
1508 C CB  . ALA   A 56  ? 0.1470 0.1892 0.1547 -0.0154 0.0108  0.0029  56  ALA   A CB  
1514 N N   . THR   A 57  ? 0.1343 0.1649 0.1035 -0.0038 0.0094  -0.0137 57  THR   A N   
1515 C CA  . THR   A 57  ? 0.1372 0.1640 0.1155 -0.0076 -0.0011 -0.0099 57  THR   A CA  
1516 C C   . THR   A 57  ? 0.1411 0.1640 0.1181 -0.0065 -0.0032 -0.0232 57  THR   A C   
1517 O O   . THR   A 57  ? 0.1481 0.1697 0.1407 -0.0164 -0.0156 -0.0252 57  THR   A O   
1518 C CB  . THR   A 57  ? 0.1410 0.1599 0.1110 -0.0039 -0.0023 -0.0130 57  THR   A CB  
1519 O OG1 . THR   A 57  ? 0.1284 0.1572 0.1110 -0.0073 0.0017  -0.0092 57  THR   A OG1 
1520 C CG2 . THR   A 57  ? 0.1442 0.1585 0.1253 -0.0045 0.0065  0.0051  57  THR   A CG2 
1528 N N   . ASN   A 58  ? 0.1453 0.1565 0.1426 -0.0032 0.0034  -0.0274 58  ASN   A N   
1529 C CA  . ASN   A 58  ? 0.1679 0.1492 0.1687 -0.0087 0.0155  -0.0362 58  ASN   A CA  
1530 C C   . ASN   A 58  ? 0.1496 0.1395 0.1570 -0.0023 -0.0027 -0.0245 58  ASN   A C   
1531 O O   . ASN   A 58  ? 0.1491 0.1481 0.1799 -0.0144 -0.0133 -0.0304 58  ASN   A O   
1532 C CB  . ASN   A 58  ? 0.2154 0.1631 0.1980 -0.0212 0.0453  -0.0450 58  ASN   A CB  
1533 C CG  . ASN   A 58  ? 0.2717 0.1968 0.2835 -0.0177 0.0470  -0.0321 58  ASN   A CG  
1534 O OD1 . ASN   A 58  ? 0.3012 0.1907 0.3370 0.0210  0.0753  -0.0162 58  ASN   A OD1 
1535 N ND2 . ASN   A 58  ? 0.2844 0.2091 0.3129 -0.0222 0.0315  -0.0299 58  ASN   A ND2 
1542 N N   . ASN   A 59  ? 0.1319 0.1330 0.1423 -0.0074 -0.0068 -0.0105 59  ASN   A N   
1543 C CA  . ASN   A 59  ? 0.1356 0.1247 0.1296 -0.0009 -0.0132 -0.0085 59  ASN   A CA  
1544 C C   . ASN   A 59  ? 0.1363 0.1325 0.1211 -0.0074 -0.0078 -0.0015 59  ASN   A C   
1545 O O   . ASN   A 59  ? 0.1348 0.1394 0.1278 -0.0080 0.0034  0.0062  59  ASN   A O   
1546 C CB  . ASN   A 59  ? 0.1446 0.1233 0.1423 0.0042  -0.0253 -0.0193 59  ASN   A CB  
1547 C CG  . ASN   A 59  ? 0.1407 0.1307 0.1410 0.0000  -0.0293 -0.0054 59  ASN   A CG  
1548 O OD1 . ASN   A 59  ? 0.1519 0.1418 0.1344 -0.0124 -0.0209 0.0025  59  ASN   A OD1 
1549 N ND2 . ASN   A 59  ? 0.1520 0.1358 0.1691 -0.0210 -0.0248 0.0040  59  ASN   A ND2 
1556 N N   . ALA   A 60  ? 0.1245 0.1325 0.1351 0.0003  -0.0033 -0.0001 60  ALA   A N   
1557 C CA  . ALA   A 60  ? 0.1257 0.1369 0.1281 -0.0015 -0.0112 0.0002  60  ALA   A CA  
1558 C C   . ALA   A 60  ? 0.1246 0.1376 0.1352 -0.0073 -0.0059 0.0025  60  ALA   A C   
1559 O O   . ALA   A 60  ? 0.1203 0.1361 0.1640 -0.0064 -0.0102 -0.0071 60  ALA   A O   
1560 C CB  . ALA   A 60  ? 0.1396 0.1471 0.1535 0.0008  -0.0211 -0.0183 60  ALA   A CB  
1566 N N   . MET   A 61  ? 0.1221 0.1263 0.1228 -0.0059 0.0027  -0.0027 61  MET   A N   
1567 C CA  . MET   A 61  ? 0.1191 0.1257 0.1243 -0.0042 -0.0053 0.0049  61  MET   A CA  
1568 C C   . MET   A 61  ? 0.1163 0.1204 0.1376 -0.0094 -0.0039 -0.0006 61  MET   A C   
1569 O O   . MET   A 61  ? 0.1157 0.1244 0.1448 -0.0046 0.0048  0.0015  61  MET   A O   
1570 C CB  . MET   A 61  ? 0.1310 0.1269 0.1221 -0.0040 -0.0008 0.0064  61  MET   A CB  
1571 C CG  . MET   A 61  ? 0.1316 0.1354 0.1350 -0.0012 -0.0026 0.0034  61  MET   A CG  
1572 S SD  . MET   A 61  ? 0.1300 0.1350 0.1630 -0.0109 -0.0027 -0.0138 61  MET   A SD  
1573 C CE  . MET   A 61  ? 0.1461 0.1436 0.2031 -0.0116 0.0105  -0.0265 61  MET   A CE  
1583 N N   . GLN   A 62  ? 0.1160 0.1216 0.1319 -0.0054 -0.0006 0.0022  62  GLN   A N   
1584 C CA  . GLN   A 62  ? 0.1291 0.1200 0.1400 -0.0050 0.0048  0.0126  62  GLN   A CA  
1585 C C   . GLN   A 62  ? 0.1260 0.1159 0.1450 -0.0017 0.0033  0.0025  62  GLN   A C   
1586 O O   . GLN   A 62  ? 0.1345 0.1301 0.1361 -0.0047 0.0088  0.0059  62  GLN   A O   
1587 C CB  . GLN   A 62  ? 0.1255 0.1245 0.1433 -0.0066 0.0024  0.0030  62  GLN   A CB  
1588 C CG  . GLN   A 62  ? 0.1293 0.1214 0.1496 -0.0093 0.0026  0.0110  62  GLN   A CG  
1589 C CD  . GLN   A 62  ? 0.1360 0.1204 0.1432 -0.0097 0.0047  0.0124  62  GLN   A CD  
1590 O OE1 . GLN   A 62  ? 0.1394 0.1357 0.1428 -0.0010 -0.0046 -0.0008 62  GLN   A OE1 
1591 N NE2 . GLN   A 62  ? 0.1420 0.1241 0.1471 -0.0005 0.0026  -0.0011 62  GLN   A NE2 
1600 N N   . VAL   A 63  ? 0.1211 0.1233 0.1606 -0.0099 0.0060  -0.0136 63  VAL   A N   
1601 C CA  . VAL   A 63  ? 0.1244 0.1399 0.1657 -0.0174 -0.0010 -0.0117 63  VAL   A CA  
1602 C C   . VAL   A 63  ? 0.1147 0.1366 0.1476 -0.0157 -0.0003 -0.0088 63  VAL   A C   
1603 O O   . VAL   A 63  ? 0.1189 0.1391 0.1615 -0.0156 0.0008  -0.0109 63  VAL   A O   
1604 C CB  . VAL   A 63  ? 0.1360 0.1560 0.2070 -0.0129 -0.0083 -0.0371 63  VAL   A CB  
1605 C CG1 . VAL   A 63  ? 0.1493 0.1700 0.2631 -0.0099 -0.0164 -0.0638 63  VAL   A CG1 
1606 C CG2 . VAL   A 63  ? 0.1413 0.1429 0.2303 -0.0049 0.0068  -0.0425 63  VAL   A CG2 
1616 N N   . GLU   A 64  ? 0.1166 0.1428 0.1456 -0.0054 -0.0024 -0.0049 64  GLU   A N   
1617 C CA  . GLU   A 64  ? 0.1229 0.1396 0.1383 -0.0076 -0.0095 0.0052  64  GLU   A CA  
1618 C C   . GLU   A 64  ? 0.1212 0.1275 0.1473 -0.0077 0.0004  0.0119  64  GLU   A C   
1619 O O   . GLU   A 64  ? 0.1331 0.1384 0.1480 0.0003  -0.0018 0.0002  64  GLU   A O   
1620 C CB  . GLU   A 64  ? 0.1334 0.1474 0.1460 -0.0079 -0.0028 0.0049  64  GLU   A CB  
1621 C CG  . GLU   A 64  ? 0.1338 0.1552 0.1715 -0.0117 0.0005  0.0064  64  GLU   A CG  
1622 C CD  . GLU   A 64  ? 0.1415 0.1610 0.1858 -0.0154 0.0025  0.0009  64  GLU   A CD  
1623 O OE1 . GLU   A 64  ? 0.1464 0.1665 0.1909 -0.0239 0.0143  0.0017  64  GLU   A OE1 
1624 O OE2 . GLU   A 64  ? 0.1595 0.1602 0.1659 -0.0175 0.0013  0.0084  64  GLU   A OE2 
1631 N N   . SER   A 65  ? 0.1192 0.1302 0.1410 -0.0025 -0.0067 0.0076  65  SER   A N   
1632 C CA  . SER   A 65  ? 0.1239 0.1292 0.1379 -0.0012 -0.0039 0.0015  65  SER   A CA  
1633 C C   . SER   A 65  ? 0.1223 0.1270 0.1377 -0.0007 0.0007  0.0018  65  SER   A C   
1634 O O   . SER   A 65  ? 0.1247 0.1340 0.1581 -0.0030 0.0136  -0.0020 65  SER   A O   
1635 C CB  . SER   A 65  ? 0.1200 0.1272 0.1459 -0.0130 0.0027  0.0055  65  SER   A CB  
1636 O OG  . SER   A 65  ? 0.1272 0.1349 0.1423 -0.0097 0.0014  0.0150  65  SER   A OG  
1642 N N   . ASP   A 66  ? 0.1285 0.1300 0.1328 -0.0036 0.0113  0.0101  66  ASP   A N   
1643 C CA  . ASP   A 66  ? 0.1338 0.1336 0.1543 -0.0044 0.0041  0.0200  66  ASP   A CA  
1644 C C   . ASP   A 66  ? 0.1233 0.1378 0.1626 -0.0099 0.0003  0.0243  66  ASP   A C   
1645 O O   . ASP   A 66  ? 0.1342 0.1450 0.1846 -0.0019 0.0160  0.0286  66  ASP   A O   
1646 C CB  . ASP   A 66  ? 0.1450 0.1486 0.1893 0.0062  0.0010  0.0385  66  ASP   A CB  
1647 C CG  . ASP   A 66  ? 0.1635 0.1628 0.2246 0.0028  0.0066  0.0517  66  ASP   A CG  
1648 O OD1 . ASP   A 66  ? 0.1664 0.1994 0.2022 -0.0137 -0.0023 0.0519  66  ASP   A OD1 
1649 O OD2 . ASP   A 66  ? 0.1805 0.1751 0.3121 0.0189  -0.0039 0.0365  66  ASP   A OD2 
1654 N N   . ASP   A 67  ? 0.1099 0.1420 0.1776 -0.0043 0.0052  0.0195  67  ASP   A N   
1655 C CA  . ASP   A 67  ? 0.1227 0.1577 0.1964 -0.0056 0.0060  0.0315  67  ASP   A CA  
1656 C C   . ASP   A 67  ? 0.1242 0.1577 0.1745 -0.0001 0.0134  0.0324  67  ASP   A C   
1657 O O   . ASP   A 67  ? 0.1222 0.1661 0.2027 -0.0032 0.0223  0.0301  67  ASP   A O   
1658 C CB  . ASP   A 67  ? 0.1354 0.1638 0.2160 -0.0009 -0.0196 0.0419  67  ASP   A CB  
1659 C CG  . ASP   A 67  ? 0.1350 0.1818 0.2545 -0.0087 -0.0275 0.0543  67  ASP   A CG  
1660 O OD1 . ASP   A 67  ? 0.1367 0.2048 0.3458 -0.0137 -0.0381 0.0641  67  ASP   A OD1 
1661 O OD2 . ASP   A 67  ? 0.1347 0.1791 0.2412 0.0037  -0.0182 0.0430  67  ASP   A OD2 
1666 N N   . TYR   A 68  ? 0.1313 0.1425 0.1824 0.0064  0.0267  0.0351  68  TYR   A N   
1667 C CA  . TYR   A 68  ? 0.1391 0.1387 0.1696 0.0051  0.0254  0.0297  68  TYR   A CA  
1668 C C   . TYR   A 68  ? 0.1335 0.1391 0.1846 0.0007  0.0254  0.0233  68  TYR   A C   
1669 O O   . TYR   A 68  ? 0.1417 0.1471 0.1911 0.0065  0.0326  0.0260  68  TYR   A O   
1670 C CB  . TYR   A 68  ? 0.1488 0.1322 0.1899 0.0032  0.0445  0.0240  68  TYR   A CB  
1671 C CG  . TYR   A 68  ? 0.1531 0.1536 0.2101 0.0072  0.0695  0.0323  68  TYR   A CG  
1672 C CD1 . TYR   A 68  ? 0.1555 0.1554 0.2397 -0.0162 0.0574  -0.0058 68  TYR   A CD1 
1673 C CD2 . TYR   A 68  ? 0.1716 0.1630 0.2367 0.0140  0.0633  0.0523  68  TYR   A CD2 
1674 C CE1 . TYR   A 68  ? 0.1671 0.1691 0.2743 -0.0122 0.0489  -0.0054 68  TYR   A CE1 
1675 C CE2 . TYR   A 68  ? 0.1699 0.1608 0.2623 0.0062  0.0687  0.0344  68  TYR   A CE2 
1676 C CZ  . TYR   A 68  ? 0.1735 0.1663 0.2843 -0.0098 0.0593  0.0025  68  TYR   A CZ  
1677 O OH  . TYR   A 68  ? 0.2005 0.1691 0.3118 -0.0078 0.0356  -0.0380 68  TYR   A OH  
1687 N N   . ILE   A 69  ? 0.1291 0.1348 0.1715 0.0004  0.0258  0.0201  69  ILE   A N   
1688 C CA  . ILE   A 69  ? 0.1342 0.1400 0.1661 0.0014  0.0187  0.0092  69  ILE   A CA  
1689 C C   . ILE   A 69  ? 0.1408 0.1423 0.1527 0.0053  0.0173  0.0126  69  ILE   A C   
1690 O O   . ILE   A 69  ? 0.1421 0.1493 0.1544 0.0022  0.0248  0.0162  69  ILE   A O   
1691 C CB  . ILE   A 69  ? 0.1432 0.1589 0.1681 0.0035  0.0118  -0.0124 69  ILE   A CB  
1692 C CG1 . ILE   A 69  ? 0.1400 0.1745 0.1787 0.0072  0.0170  -0.0215 69  ILE   A CG1 
1693 C CG2 . ILE   A 69  ? 0.1628 0.1819 0.1915 0.0106  0.0041  -0.0184 69  ILE   A CG2 
1694 C CD1 . ILE   A 69  ? 0.1440 0.1813 0.2038 -0.0055 0.0193  -0.0310 69  ILE   A CD1 
1706 N N   . ALA   A 70  ? 0.1356 0.1432 0.1775 -0.0099 0.0128  0.0190  70  ALA   A N   
1707 C CA  . ALA   A 70  ? 0.1414 0.1584 0.1887 -0.0175 0.0267  0.0325  70  ALA   A CA  
1708 C C   . ALA   A 70  ? 0.1436 0.1753 0.1788 -0.0125 0.0290  0.0242  70  ALA   A C   
1709 O O   . ALA   A 70  ? 0.1656 0.2096 0.2130 0.0108  0.0528  0.0369  70  ALA   A O   
1710 C CB  . ALA   A 70  ? 0.1427 0.1610 0.2205 -0.0141 0.0234  0.0263  70  ALA   A CB  
1716 N N   . THR   A 71  ? 0.1395 0.1669 0.1704 -0.0054 0.0044  0.0316  71  THR   A N   
1717 C CA  . THR   A 71  ? 0.1529 0.1831 0.2134 0.0122  0.0182  0.0442  71  THR   A CA  
1718 C C   . THR   A 71  ? 0.1371 0.1761 0.2397 0.0201  0.0336  0.0374  71  THR   A C   
1719 O O   . THR   A 71  ? 0.1447 0.2031 0.3012 0.0108  0.0501  0.0018  71  THR   A O   
1720 C CB  . THR   A 71  ? 0.1897 0.2036 0.2404 0.0237  -0.0210 0.0431  71  THR   A CB  
1721 O OG1 . THR   A 71  ? 0.2182 0.2246 0.2526 0.0142  -0.0423 0.0240  71  THR   A OG1 
1722 C CG2 . THR   A 71  ? 0.2037 0.2211 0.2802 0.0339  -0.0295 0.0486  71  THR   A CG2 
1730 N N   . ASN   A 72  ? 0.1352 0.1570 0.1937 0.0169  0.0291  0.0326  72  ASN   A N   
1731 C CA  . ASN   A 72  ? 0.1444 0.1558 0.2121 0.0217  0.0406  0.0334  72  ASN   A CA  
1732 C C   . ASN   A 72  ? 0.1563 0.1574 0.2102 0.0140  0.0440  0.0293  72  ASN   A C   
1733 O O   . ASN   A 72  ? 0.1746 0.1618 0.2286 0.0154  0.0432  0.0054  72  ASN   A O   
1734 C CB  . ASN   A 72  ? 0.1624 0.1699 0.2114 0.0279  0.0419  0.0391  72  ASN   A CB  
1735 C CG  . ASN   A 72  ? 0.1871 0.1834 0.2224 0.0329  0.0412  0.0347  72  ASN   A CG  
1736 O OD1 . ASN   A 72  ? 0.2088 0.2180 0.2469 0.0332  0.0541  0.0399  72  ASN   A OD1 
1737 N ND2 . ASN   A 72  ? 0.2006 0.1765 0.2332 0.0564  0.0210  0.0229  72  ASN   A ND2 
1744 N N   . GLY   A 73  ? 0.1564 0.1492 0.1892 0.0053  0.0420  0.0138  73  GLY   A N   
1745 C CA  . GLY   A 73  ? 0.1636 0.1536 0.1712 -0.0026 0.0455  0.0173  73  GLY   A CA  
1746 C C   . GLY   A 73  ? 0.1615 0.1451 0.1591 0.0023  0.0494  0.0291  73  GLY   A C   
1747 O O   . GLY   A 73  ? 0.1602 0.1489 0.1666 0.0098  0.0328  0.0295  73  GLY   A O   
1751 N N   . PRO   A 74  ? 0.1695 0.1458 0.1762 -0.0024 0.0473  0.0185  74  PRO   A N   
1752 C CA  . PRO   A 74  ? 0.1620 0.1382 0.1864 0.0018  0.0413  0.0234  74  PRO   A CA  
1753 C C   . PRO   A 74  ? 0.1622 0.1200 0.1656 -0.0003 0.0283  0.0147  74  PRO   A C   
1754 O O   . PRO   A 74  ? 0.1723 0.1287 0.1990 0.0034  0.0315  -0.0011 74  PRO   A O   
1755 C CB  . PRO   A 74  ? 0.1809 0.1753 0.2092 0.0054  0.0444  0.0381  74  PRO   A CB  
1756 C CG  . PRO   A 74  ? 0.2085 0.2077 0.2429 -0.0113 0.0400  0.0180  74  PRO   A CG  
1757 C CD  . PRO   A 74  ? 0.1800 0.1770 0.1907 -0.0180 0.0323  0.0077  74  PRO   A CD  
1765 N N   . LEU   A 75  ? 0.1645 0.1192 0.1469 0.0002  0.0268  0.0082  75  LEU   A N   
1766 C CA  . LEU   A 75  ? 0.1690 0.1218 0.1208 0.0029  0.0104  0.0160  75  LEU   A CA  
1767 C C   . LEU   A 75  ? 0.1780 0.1336 0.1188 0.0047  0.0202  0.0150  75  LEU   A C   
1768 O O   . LEU   A 75  ? 0.2075 0.1394 0.1337 0.0083  0.0063  0.0108  75  LEU   A O   
1769 C CB  . LEU   A 75  ? 0.1704 0.1271 0.1153 -0.0058 0.0138  0.0173  75  LEU   A CB  
1770 C CG  . LEU   A 75  ? 0.1845 0.1637 0.1394 -0.0304 0.0156  0.0161  75  LEU   A CG  
1771 C CD1 . LEU   A 75  ? 0.1896 0.2091 0.1519 -0.0318 0.0125  0.0083  75  LEU   A CD1 
1772 C CD2 . LEU   A 75  ? 0.2165 0.1942 0.2280 -0.0116 0.0195  0.0273  75  LEU   A CD2 
1784 N N   . LYS   A 76  ? 0.1747 0.1312 0.1387 0.0005  0.0120  0.0065  76  LYS   A N   
1785 C CA  . LYS   A 76  ? 0.1710 0.1443 0.1409 -0.0018 0.0076  0.0026  76  LYS   A CA  
1786 C C   . LYS   A 76  ? 0.1690 0.1353 0.1120 0.0016  0.0009  0.0087  76  LYS   A C   
1787 O O   . LYS   A 76  ? 0.1755 0.1292 0.1210 0.0023  0.0088  0.0097  76  LYS   A O   
1788 C CB  . LYS   A 76  ? 0.1746 0.1608 0.1796 0.0043  0.0091  -0.0245 76  LYS   A CB  
1789 C CG  . LYS   A 76  ? 0.1777 0.1556 0.2409 0.0100  -0.0098 -0.0279 76  LYS   A CG  
1790 C CD  . LYS   A 76  ? 0.1901 0.1646 0.2725 0.0161  -0.0180 -0.0234 76  LYS   A CD  
1791 C CE  . LYS   A 76  ? 0.2003 0.1891 0.3388 0.0014  -0.0167 -0.0275 76  LYS   A CE  
1792 N NZ  . LYS   A 76  ? 0.1979 0.1825 0.3861 -0.0090 -0.0165 -0.0462 76  LYS   A NZ  
1806 N N   A VAL   A 77  ? 0.1800 0.1437 0.1259 -0.0024 0.0124  0.0145  77  VAL   A N   
1807 N N   B VAL   A 77  ? 0.1804 0.1407 0.1301 -0.0049 0.0166  0.0219  77  VAL   A N   
1808 C CA  A VAL   A 77  ? 0.1848 0.1448 0.1302 0.0031  0.0053  0.0127  77  VAL   A CA  
1809 C CA  B VAL   A 77  ? 0.1825 0.1393 0.1387 -0.0025 -0.0012 0.0142  77  VAL   A CA  
1810 C C   A VAL   A 77  ? 0.1799 0.1400 0.1184 0.0089  0.0034  0.0085  77  VAL   A C   
1811 C C   B VAL   A 77  ? 0.1791 0.1325 0.1335 0.0050  0.0013  0.0032  77  VAL   A C   
1812 O O   A VAL   A 77  ? 0.1831 0.1503 0.1146 0.0104  0.0116  0.0089  77  VAL   A O   
1813 O O   B VAL   A 77  ? 0.1784 0.1370 0.1352 0.0040  0.0086  -0.0052 77  VAL   A O   
1814 C CB  A VAL   A 77  ? 0.2032 0.1561 0.1460 0.0019  -0.0017 0.0174  77  VAL   A CB  
1815 C CB  B VAL   A 77  ? 0.2010 0.1498 0.1577 -0.0095 -0.0221 0.0235  77  VAL   A CB  
1816 C CG1 A VAL   A 77  ? 0.2081 0.1579 0.1697 0.0041  -0.0071 0.0124  77  VAL   A CG1 
1817 C CG1 B VAL   A 77  ? 0.2112 0.1556 0.1786 -0.0050 -0.0338 0.0202  77  VAL   A CG1 
1818 C CG2 A VAL   A 77  ? 0.2154 0.1670 0.1560 0.0053  0.0016  0.0202  77  VAL   A CG2 
1819 C CG2 B VAL   A 77  ? 0.2083 0.1627 0.1824 -0.0021 -0.0165 0.0282  77  VAL   A CG2 
1838 N N   . GLY   A 78  ? 0.1691 0.1330 0.1176 0.0056  0.0111  0.0072  78  GLY   A N   
1839 C CA  . GLY   A 78  ? 0.1667 0.1381 0.1279 -0.0001 0.0249  0.0124  78  GLY   A CA  
1840 C C   . GLY   A 78  ? 0.1531 0.1334 0.1231 0.0035  0.0177  0.0225  78  GLY   A C   
1841 O O   . GLY   A 78  ? 0.1475 0.1353 0.1481 0.0049  0.0121  0.0267  78  GLY   A O   
1846 N N   . GLY   A 79  ? 0.1526 0.1317 0.1316 -0.0068 0.0090  0.0163  79  GLY   A N   
1847 C CA  . GLY   A 79  ? 0.1454 0.1325 0.1553 0.0007  0.0103  0.0129  79  GLY   A CA  
1848 C C   . GLY   A 79  ? 0.1286 0.1254 0.1346 0.0046  0.0152  0.0061  79  GLY   A C   
1849 O O   . GLY   A 79  ? 0.1422 0.1344 0.1311 0.0162  0.0080  0.0083  79  GLY   A O   
1853 N N   . SER   A 80  ? 0.1224 0.1404 0.1513 0.0031  0.0088  -0.0032 80  SER   A N   
1854 C CA  . SER   A 80  ? 0.1211 0.1279 0.1361 -0.0038 0.0024  0.0000  80  SER   A CA  
1855 C C   . SER   A 80  ? 0.1251 0.1365 0.1317 -0.0006 0.0058  0.0112  80  SER   A C   
1856 O O   . SER   A 80  ? 0.1291 0.1503 0.1751 0.0058  0.0147  0.0026  80  SER   A O   
1857 C CB  . SER   A 80  ? 0.1351 0.1305 0.1720 -0.0036 0.0096  0.0074  80  SER   A CB  
1858 O OG  . SER   A 80  ? 0.1606 0.1300 0.2236 0.0095  0.0035  0.0327  80  SER   A OG  
1864 N N   . CYS   A 81  ? 0.1122 0.1335 0.1366 0.0001  -0.0002 0.0134  81  CYS   A N   
1865 C CA  . CYS   A 81  ? 0.1180 0.1402 0.1360 -0.0061 -0.0005 0.0197  81  CYS   A CA  
1866 C C   . CYS   A 81  ? 0.1118 0.1416 0.1367 -0.0127 0.0036  0.0284  81  CYS   A C   
1867 O O   . CYS   A 81  ? 0.1125 0.1754 0.1311 -0.0021 0.0022  0.0309  81  CYS   A O   
1868 C CB  . CYS   A 81  ? 0.1268 0.1482 0.1396 -0.0100 0.0027  0.0178  81  CYS   A CB  
1869 S SG  . CYS   A 81  ? 0.1401 0.1317 0.1538 -0.0110 0.0014  0.0138  81  CYS   A SG  
1875 N N   . VAL   A 82  ? 0.1171 0.1434 0.1344 0.0024  -0.0076 0.0163  82  VAL   A N   
1876 C CA  . VAL   A 82  ? 0.1326 0.1471 0.1306 0.0053  -0.0048 0.0220  82  VAL   A CA  
1877 C C   . VAL   A 82  ? 0.1296 0.1469 0.1390 -0.0005 -0.0055 0.0293  82  VAL   A C   
1878 O O   . VAL   A 82  ? 0.1289 0.1502 0.1735 -0.0020 -0.0027 -0.0017 82  VAL   A O   
1879 C CB  . VAL   A 82  ? 0.1621 0.1607 0.1552 0.0057  0.0094  0.0277  82  VAL   A CB  
1880 C CG1 . VAL   A 82  ? 0.1806 0.1782 0.1877 0.0057  0.0124  0.0299  82  VAL   A CG1 
1881 C CG2 . VAL   A 82  ? 0.1710 0.1651 0.1860 -0.0020 0.0035  0.0277  82  VAL   A CG2 
1891 N N   . LEU   A 83  ? 0.1215 0.1444 0.1372 -0.0033 -0.0083 0.0133  83  LEU   A N   
1892 C CA  . LEU   A 83  ? 0.1222 0.1472 0.1320 -0.0100 -0.0094 0.0144  83  LEU   A CA  
1893 C C   . LEU   A 83  ? 0.1326 0.1499 0.1272 -0.0075 -0.0060 0.0201  83  LEU   A C   
1894 O O   . LEU   A 83  ? 0.1431 0.1513 0.1379 -0.0091 -0.0030 0.0281  83  LEU   A O   
1895 C CB  . LEU   A 83  ? 0.1313 0.1490 0.1391 -0.0137 -0.0111 0.0262  83  LEU   A CB  
1896 C CG  . LEU   A 83  ? 0.1533 0.1590 0.1513 -0.0160 -0.0033 0.0193  83  LEU   A CG  
1897 C CD1 . LEU   A 83  ? 0.1621 0.1604 0.1687 -0.0249 0.0028  0.0284  83  LEU   A CD1 
1898 C CD2 . LEU   A 83  ? 0.1542 0.1644 0.1685 -0.0076 0.0179  0.0129  83  LEU   A CD2 
1910 N N   . SER   A 84  ? 0.1438 0.1541 0.1399 -0.0093 -0.0092 0.0134  84  SER   A N   
1911 C CA  . SER   A 84  ? 0.1527 0.1592 0.1207 -0.0083 -0.0051 0.0116  84  SER   A CA  
1912 C C   . SER   A 84  ? 0.1570 0.1592 0.1138 -0.0188 0.0091  0.0107  84  SER   A C   
1913 O O   . SER   A 84  ? 0.1514 0.1747 0.1159 -0.0120 -0.0057 0.0134  84  SER   A O   
1914 C CB  . SER   A 84  ? 0.1598 0.1778 0.1450 -0.0079 -0.0107 -0.0001 84  SER   A CB  
1915 O OG  . SER   A 84  ? 0.1719 0.1979 0.1564 -0.0094 -0.0182 -0.0106 84  SER   A OG  
1921 N N   A GLY   A 85  ? 0.1644 0.1710 0.1303 -0.0186 0.0111  0.0088  85  GLY   A N   
1922 N N   B GLY   A 85  ? 0.1659 0.1739 0.1351 -0.0193 0.0130  0.0073  85  GLY   A N   
1923 C CA  A GLY   A 85  ? 0.1650 0.1792 0.1377 -0.0208 0.0113  -0.0054 85  GLY   A CA  
1924 C CA  B GLY   A 85  ? 0.1644 0.1827 0.1434 -0.0235 0.0144  -0.0104 85  GLY   A CA  
1925 C C   A GLY   A 85  ? 0.1697 0.1834 0.1342 -0.0141 -0.0007 -0.0007 85  GLY   A C   
1926 C C   B GLY   A 85  ? 0.1686 0.1862 0.1362 -0.0170 -0.0011 -0.0047 85  GLY   A C   
1927 O O   A GLY   A 85  ? 0.1744 0.1873 0.1418 -0.0128 0.0028  -0.0063 85  GLY   A O   
1928 O O   B GLY   A 85  ? 0.1731 0.1909 0.1427 -0.0179 0.0034  -0.0171 85  GLY   A O   
1935 N N   . HIS   A 86  ? 0.1725 0.1809 0.1274 -0.0069 -0.0033 0.0054  86  HIS   A N   
1936 C CA  . HIS   A 86  ? 0.1886 0.1781 0.1172 -0.0095 -0.0033 0.0110  86  HIS   A CA  
1937 C C   . HIS   A 86  ? 0.2107 0.1813 0.1036 -0.0118 -0.0100 0.0063  86  HIS   A C   
1938 O O   . HIS   A 86  ? 0.2281 0.2069 0.1257 -0.0034 0.0071  0.0112  86  HIS   A O   
1939 C CB  . HIS   A 86  ? 0.1839 0.1723 0.1271 -0.0064 -0.0028 0.0153  86  HIS   A CB  
1940 C CG  . HIS   A 86  ? 0.1773 0.1729 0.1250 -0.0051 0.0004  0.0178  86  HIS   A CG  
1941 N ND1 . HIS   A 86  ? 0.1881 0.1753 0.1682 -0.0115 -0.0007 0.0152  86  HIS   A ND1 
1942 C CD2 . HIS   A 86  ? 0.1790 0.1650 0.1289 0.0077  0.0062  0.0110  86  HIS   A CD2 
1943 C CE1 . HIS   A 86  ? 0.1869 0.1758 0.1722 -0.0017 0.0174  0.0198  86  HIS   A CE1 
1944 N NE2 . HIS   A 86  ? 0.1812 0.1674 0.1569 0.0156  0.0169  0.0254  86  HIS   A NE2 
1953 N N   . ASN   A 87  ? 0.2193 0.1939 0.1215 -0.0002 0.0069  0.0092  87  ASN   A N   
1954 C CA  . ASN   A 87  ? 0.2341 0.2084 0.1257 0.0038  0.0299  -0.0033 87  ASN   A CA  
1955 C C   . ASN   A 87  ? 0.2360 0.2299 0.1570 -0.0108 0.0490  0.0031  87  ASN   A C   
1956 O O   . ASN   A 87  ? 0.2676 0.2575 0.1952 -0.0321 0.0881  -0.0119 87  ASN   A O   
1957 C CB  . ASN   A 87  ? 0.2525 0.2102 0.1405 0.0191  0.0261  -0.0068 87  ASN   A CB  
1958 C CG  . ASN   A 87  ? 0.2685 0.2244 0.1427 0.0236  0.0386  0.0074  87  ASN   A CG  
1959 O OD1 . ASN   A 87  ? 0.2888 0.2263 0.1437 0.0394  0.0449  0.0108  87  ASN   A OD1 
1960 N ND2 . ASN   A 87  ? 0.2709 0.2474 0.1744 0.0208  0.0360  0.0036  87  ASN   A ND2 
1967 N N   A LEU   A 88  ? 0.2134 0.2179 0.1392 -0.0115 0.0257  0.0125  88  LEU   A N   
1968 N N   B LEU   A 88  ? 0.2119 0.2218 0.1365 -0.0087 0.0317  0.0030  88  LEU   A N   
1969 C CA  A LEU   A 88  ? 0.1928 0.2144 0.1489 -0.0158 0.0207  0.0288  88  LEU   A CA  
1970 C CA  B LEU   A 88  ? 0.1892 0.2218 0.1514 -0.0119 0.0384  0.0176  88  LEU   A CA  
1971 C C   A LEU   A 88  ? 0.1843 0.2181 0.1416 -0.0197 0.0241  0.0280  88  LEU   A C   
1972 C C   B LEU   A 88  ? 0.1798 0.2227 0.1450 -0.0134 0.0361  0.0359  88  LEU   A C   
1973 O O   A LEU   A 88  ? 0.1885 0.2225 0.1651 -0.0199 0.0252  0.0354  88  LEU   A O   
1974 O O   B LEU   A 88  ? 0.1821 0.2261 0.1736 -0.0015 0.0400  0.0634  88  LEU   A O   
1975 C CB  A LEU   A 88  ? 0.1887 0.2118 0.1548 -0.0196 -0.0103 0.0498  88  LEU   A CB  
1976 C CB  B LEU   A 88  ? 0.1869 0.2261 0.1675 -0.0168 0.0151  0.0155  88  LEU   A CB  
1977 C CG  A LEU   A 88  ? 0.2003 0.2144 0.1704 -0.0172 -0.0250 0.0630  88  LEU   A CG  
1978 C CG  B LEU   A 88  ? 0.1961 0.2308 0.1790 -0.0090 0.0095  0.0092  88  LEU   A CG  
1979 C CD1 A LEU   A 88  ? 0.2084 0.2132 0.1663 -0.0162 -0.0319 0.0585  88  LEU   A CD1 
1980 C CD1 B LEU   A 88  ? 0.2002 0.2284 0.1798 -0.0059 0.0078  -0.0082 88  LEU   A CD1 
1981 C CD2 A LEU   A 88  ? 0.2140 0.2251 0.2123 -0.0136 -0.0125 0.0576  88  LEU   A CD2 
1982 C CD2 B LEU   A 88  ? 0.2087 0.2413 0.2034 -0.0021 0.0253  0.0047  88  LEU   A CD2 
2005 N N   . ALA   A 89  ? 0.1807 0.2144 0.1327 -0.0145 0.0167  0.0131  89  ALA   A N   
2006 C CA  . ALA   A 89  ? 0.1830 0.2109 0.1205 -0.0068 0.0072  0.0187  89  ALA   A CA  
2007 C C   . ALA   A 89  ? 0.1870 0.2131 0.1327 -0.0024 -0.0053 0.0190  89  ALA   A C   
2008 O O   . ALA   A 89  ? 0.1787 0.2099 0.1785 -0.0171 -0.0046 -0.0146 89  ALA   A O   
2009 C CB  . ALA   A 89  ? 0.1808 0.2085 0.1273 -0.0146 0.0185  0.0062  89  ALA   A CB  
2016 N N   A LYS   A 90  ? 0.1964 0.2244 0.1566 -0.0070 -0.0136 0.0191  90  LYS   A N   
2017 N N   B LYS   A 90  ? 0.1879 0.2170 0.1231 -0.0098 -0.0136 0.0292  90  LYS   A N   
2018 C CA  A LYS   A 90  ? 0.2045 0.2357 0.1716 -0.0067 -0.0216 0.0197  90  LYS   A CA  
2019 C CA  B LYS   A 90  ? 0.1898 0.2223 0.1230 -0.0074 -0.0344 0.0333  90  LYS   A CA  
2020 C C   A LYS   A 90  ? 0.1901 0.2260 0.1741 -0.0132 -0.0219 0.0049  90  LYS   A C   
2021 C C   B LYS   A 90  ? 0.1663 0.2013 0.1187 -0.0148 -0.0338 0.0154  90  LYS   A C   
2022 O O   A LYS   A 90  ? 0.1934 0.2442 0.1988 -0.0186 -0.0231 -0.0020 90  LYS   A O   
2023 O O   B LYS   A 90  ? 0.1757 0.2128 0.1425 -0.0207 -0.0313 0.0082  90  LYS   A O   
2024 C CB  A LYS   A 90  ? 0.2236 0.2616 0.2071 -0.0043 -0.0232 0.0313  90  LYS   A CB  
2025 C CB  B LYS   A 90  ? 0.2119 0.2557 0.1442 -0.0027 -0.0434 0.0442  90  LYS   A CB  
2026 C CG  A LYS   A 90  ? 0.2482 0.2857 0.2811 0.0006  -0.0227 0.0381  90  LYS   A CG  
2027 C CG  B LYS   A 90  ? 0.2450 0.2855 0.2560 0.0071  -0.0421 0.0465  90  LYS   A CG  
2028 C CD  A LYS   A 90  ? 0.2695 0.3036 0.3403 0.0016  -0.0182 0.0437  90  LYS   A CD  
2029 C CD  B LYS   A 90  ? 0.2725 0.3069 0.3353 0.0099  -0.0360 0.0491  90  LYS   A CD  
2030 C CE  A LYS   A 90  ? 0.2852 0.3158 0.3902 0.0014  -0.0157 0.0432  90  LYS   A CE  
2031 C CE  B LYS   A 90  ? 0.2910 0.3199 0.4001 0.0091  -0.0335 0.0433  90  LYS   A CE  
2032 N NZ  A LYS   A 90  ? 0.2986 0.3243 0.4232 -0.0009 -0.0096 0.0372  90  LYS   A NZ  
2033 N NZ  B LYS   A 90  ? 0.3065 0.3289 0.4402 0.0048  -0.0255 0.0299  90  LYS   A NZ  
2060 N N   A HIS   A 91  ? 0.1851 0.2060 0.1538 -0.0108 -0.0179 0.0061  91  HIS   A N   
2061 N N   B HIS   A 91  ? 0.1592 0.1767 0.0853 -0.0081 -0.0211 0.0239  91  HIS   A N   
2062 C CA  A HIS   A 91  ? 0.1767 0.1903 0.1543 -0.0102 -0.0154 0.0092  91  HIS   A CA  
2063 C CA  B HIS   A 91  ? 0.1480 0.1635 0.0913 -0.0004 -0.0175 0.0139  91  HIS   A CA  
2064 C C   A HIS   A 91  ? 0.1524 0.1659 0.1327 -0.0109 -0.0062 0.0157  91  HIS   A C   
2065 C C   B HIS   A 91  ? 0.1404 0.1541 0.1018 -0.0036 -0.0058 0.0132  91  HIS   A C   
2066 O O   A HIS   A 91  ? 0.1479 0.1608 0.1257 -0.0107 -0.0001 0.0129  91  HIS   A O   
2067 O O   B HIS   A 91  ? 0.1388 0.1570 0.1196 -0.0072 -0.0015 0.0148  91  HIS   A O   
2068 C CB  A HIS   A 91  ? 0.2003 0.2154 0.1882 0.0003  -0.0304 0.0106  91  HIS   A CB  
2069 C CB  B HIS   A 91  ? 0.1593 0.1939 0.1425 0.0191  -0.0379 0.0200  91  HIS   A CB  
2070 C CG  A HIS   A 91  ? 0.2321 0.2511 0.2413 0.0064  -0.0500 0.0071  91  HIS   A CG  
2071 C CG  B HIS   A 91  ? 0.2009 0.2432 0.2181 0.0295  -0.0670 0.0103  91  HIS   A CG  
2072 N ND1 A HIS   A 91  ? 0.2420 0.2722 0.2649 0.0112  -0.0584 -0.0055 91  HIS   A ND1 
2073 N ND1 B HIS   A 91  ? 0.2135 0.2742 0.2602 0.0314  -0.0712 -0.0154 91  HIS   A ND1 
2074 C CD2 A HIS   A 91  ? 0.2501 0.2662 0.2576 0.0099  -0.0614 0.0159  91  HIS   A CD2 
2075 C CD2 B HIS   A 91  ? 0.2337 0.2663 0.2443 0.0303  -0.0765 0.0231  91  HIS   A CD2 
2076 C CE1 A HIS   A 91  ? 0.2514 0.2792 0.2776 0.0147  -0.0642 0.0031  91  HIS   A CE1 
2077 C CE1 B HIS   A 91  ? 0.2327 0.2863 0.2790 0.0327  -0.0736 -0.0024 91  HIS   A CE1 
2078 N NE2 A HIS   A 91  ? 0.2588 0.2779 0.2757 0.0166  -0.0704 0.0069  91  HIS   A NE2 
2079 N NE2 B HIS   A 91  ? 0.2462 0.2851 0.2768 0.0339  -0.0799 0.0043  91  HIS   A NE2 
2094 N N   . CYS   A 92  ? 0.1354 0.1557 0.1193 -0.0155 -0.0070 0.0177  92  CYS   A N   
2095 C CA  . CYS   A 92  ? 0.1317 0.1445 0.1242 -0.0179 0.0004  0.0145  92  CYS   A CA  
2096 C C   . CYS   A 92  ? 0.1252 0.1382 0.1200 -0.0181 0.0031  0.0117  92  CYS   A C   
2097 O O   . CYS   A 92  ? 0.1308 0.1545 0.1365 -0.0170 -0.0006 0.0095  92  CYS   A O   
2098 C CB  . CYS   A 92  ? 0.1399 0.1451 0.1293 -0.0078 -0.0010 0.0094  92  CYS   A CB  
2099 S SG  . CYS   A 92  ? 0.1366 0.1359 0.1339 -0.0104 -0.0026 0.0131  92  CYS   A SG  
2106 N N   . LEU   A 93  ? 0.1228 0.1316 0.1353 -0.0080 0.0118  0.0102  93  LEU   A N   
2107 C CA  . LEU   A 93  ? 0.1159 0.1262 0.1290 -0.0074 -0.0016 0.0199  93  LEU   A CA  
2108 C C   . LEU   A 93  ? 0.1130 0.1203 0.1259 0.0037  0.0064  0.0149  93  LEU   A C   
2109 O O   . LEU   A 93  ? 0.1133 0.1268 0.1166 0.0008  0.0030  0.0119  93  LEU   A O   
2110 C CB  . LEU   A 93  ? 0.1228 0.1224 0.1359 0.0017  0.0014  0.0144  93  LEU   A CB  
2111 C CG  . LEU   A 93  ? 0.1290 0.1269 0.1420 -0.0059 0.0003  0.0321  93  LEU   A CG  
2112 C CD1 . LEU   A 93  ? 0.1370 0.1433 0.1596 -0.0002 0.0150  0.0197  93  LEU   A CD1 
2113 C CD2 . LEU   A 93  ? 0.1462 0.1235 0.1664 -0.0089 0.0048  0.0163  93  LEU   A CD2 
2125 N N   . HIS   A 94  ? 0.1120 0.1199 0.1188 -0.0020 0.0089  0.0218  94  HIS   A N   
2126 C CA  . HIS   A 94  ? 0.1152 0.1214 0.1206 -0.0032 -0.0014 0.0143  94  HIS   A CA  
2127 C C   . HIS   A 94  ? 0.1130 0.1156 0.1308 -0.0082 0.0003  0.0045  94  HIS   A C   
2128 O O   . HIS   A 94  ? 0.1178 0.1390 0.1534 -0.0013 0.0069  -0.0090 94  HIS   A O   
2129 C CB  . HIS   A 94  ? 0.1193 0.1229 0.1244 -0.0045 -0.0001 0.0124  94  HIS   A CB  
2130 C CG  . HIS   A 94  ? 0.1205 0.1196 0.1201 -0.0058 -0.0025 0.0126  94  HIS   A CG  
2131 N ND1 . HIS   A 94  ? 0.1181 0.1157 0.1236 -0.0036 -0.0019 0.0175  94  HIS   A ND1 
2132 C CD2 . HIS   A 94  ? 0.1255 0.1304 0.1344 -0.0032 -0.0038 0.0046  94  HIS   A CD2 
2133 C CE1 . HIS   A 94  ? 0.1244 0.1194 0.1251 -0.0050 -0.0087 0.0090  94  HIS   A CE1 
2134 N NE2 . HIS   A 94  ? 0.1325 0.1248 0.1230 -0.0097 -0.0048 0.0079  94  HIS   A NE2 
2142 N N   . VAL   A 95  ? 0.1151 0.1162 0.1175 -0.0036 0.0050  0.0034  95  VAL   A N   
2143 C CA  . VAL   A 95  ? 0.1194 0.1221 0.1116 -0.0027 0.0162  0.0110  95  VAL   A CA  
2144 C C   . VAL   A 95  ? 0.1198 0.1156 0.1095 -0.0089 -0.0069 0.0123  95  VAL   A C   
2145 O O   . VAL   A 95  ? 0.1304 0.1300 0.1252 0.0136  -0.0040 0.0060  95  VAL   A O   
2146 C CB  . VAL   A 95  ? 0.1200 0.1217 0.1248 -0.0064 0.0073  0.0089  95  VAL   A CB  
2147 C CG1 . VAL   A 95  ? 0.1393 0.1201 0.1470 -0.0149 0.0001  0.0035  95  VAL   A CG1 
2148 C CG2 . VAL   A 95  ? 0.1260 0.1181 0.1327 -0.0087 0.0124  0.0233  95  VAL   A CG2 
2158 N N   . VAL   A 96  ? 0.1306 0.1180 0.0990 -0.0025 0.0032  0.0176  96  VAL   A N   
2159 C CA  . VAL   A 96  ? 0.1449 0.1214 0.1142 -0.0056 0.0065  0.0174  96  VAL   A CA  
2160 C C   . VAL   A 96  ? 0.1398 0.1366 0.1265 -0.0077 0.0016  0.0164  96  VAL   A C   
2161 O O   . VAL   A 96  ? 0.1485 0.1387 0.1475 -0.0064 0.0102  -0.0044 96  VAL   A O   
2162 C CB  . VAL   A 96  ? 0.1483 0.1283 0.1237 -0.0041 0.0136  0.0105  96  VAL   A CB  
2163 C CG1 . VAL   A 96  ? 0.1595 0.1260 0.1268 -0.0046 0.0190  0.0179  96  VAL   A CG1 
2164 C CG2 . VAL   A 96  ? 0.1432 0.1388 0.1468 -0.0130 0.0123  0.0099  96  VAL   A CG2 
2174 N N   A GLY   A 97  ? 0.1407 0.1319 0.1314 -0.0095 0.0030  0.0277  97  GLY   A N   
2175 N N   B GLY   A 97  ? 0.1384 0.1348 0.1212 -0.0163 -0.0040 0.0157  97  GLY   A N   
2176 C CA  A GLY   A 97  ? 0.1504 0.1410 0.1352 -0.0035 -0.0008 0.0361  97  GLY   A CA  
2177 C CA  B GLY   A 97  ? 0.1470 0.1471 0.1314 -0.0140 -0.0139 0.0166  97  GLY   A CA  
2178 C C   A GLY   A 97  ? 0.1548 0.1490 0.1272 0.0016  0.0009  0.0350  97  GLY   A C   
2179 C C   B GLY   A 97  ? 0.1487 0.1543 0.1147 -0.0106 -0.0111 0.0184  97  GLY   A C   
2180 O O   A GLY   A 97  ? 0.1528 0.1548 0.1276 0.0038  0.0125  0.0256  97  GLY   A O   
2181 O O   B GLY   A 97  ? 0.1507 0.1599 0.1447 -0.0163 -0.0103 0.0376  97  GLY   A O   
2188 N N   A PRO   A 98  ? 0.1665 0.1423 0.1199 0.0034  -0.0075 0.0372  98  PRO   A N   
2189 N N   B PRO   A 98  ? 0.1677 0.1607 0.1181 0.0001  -0.0058 0.0151  98  PRO   A N   
2190 C CA  A PRO   A 98  ? 0.1669 0.1553 0.1249 0.0034  -0.0114 0.0223  98  PRO   A CA  
2191 C CA  B PRO   A 98  ? 0.1822 0.1666 0.1413 0.0055  -0.0118 0.0102  98  PRO   A CA  
2192 C C   A PRO   A 98  ? 0.1675 0.1697 0.1220 -0.0061 0.0057  0.0312  98  PRO   A C   
2193 C C   B PRO   A 98  ? 0.2043 0.1637 0.1311 0.0063  -0.0059 0.0215  98  PRO   A C   
2194 O O   A PRO   A 98  ? 0.1614 0.1642 0.1353 -0.0063 0.0083  0.0276  98  PRO   A O   
2195 O O   B PRO   A 98  ? 0.2027 0.1625 0.1507 0.0104  -0.0026 0.0334  98  PRO   A O   
2196 C CB  A PRO   A 98  ? 0.1719 0.1578 0.1092 0.0170  -0.0123 0.0023  98  PRO   A CB  
2197 C CB  B PRO   A 98  ? 0.1876 0.1693 0.1487 0.0139  -0.0139 0.0106  98  PRO   A CB  
2198 C CG  A PRO   A 98  ? 0.1763 0.1451 0.1167 0.0200  -0.0105 0.0009  98  PRO   A CG  
2199 C CG  B PRO   A 98  ? 0.1932 0.1679 0.1553 0.0046  -0.0141 0.0073  98  PRO   A CG  
2200 C CD  A PRO   A 98  ? 0.1734 0.1400 0.1159 0.0084  -0.0105 0.0248  98  PRO   A CD  
2201 C CD  B PRO   A 98  ? 0.1748 0.1632 0.1474 0.0033  -0.0136 0.0138  98  PRO   A CD  
2216 N N   A ASN   A 99  ? 0.1753 0.1885 0.1154 -0.0013 0.0121  0.0404  99  ASN   A N   
2217 N N   B ASN   A 99  ? 0.2302 0.1690 0.1437 0.0062  -0.0231 0.0407  99  ASN   A N   
2218 C CA  A ASN   A 99  ? 0.1901 0.2047 0.1118 0.0075  0.0062  0.0521  99  ASN   A CA  
2219 C CA  B ASN   A 99  ? 0.2596 0.1850 0.1791 0.0098  -0.0284 0.0463  99  ASN   A CA  
2220 C C   A ASN   A 99  ? 0.2129 0.2354 0.1100 0.0067  0.0016  0.0553  99  ASN   A C   
2221 C C   B ASN   A 99  ? 0.2675 0.2147 0.1558 0.0102  -0.0310 0.0469  99  ASN   A C   
2222 O O   A ASN   A 99  ? 0.2211 0.2532 0.1210 0.0133  0.0124  0.0329  99  ASN   A O   
2223 O O   B ASN   A 99  ? 0.2622 0.2161 0.1423 0.0180  -0.0239 0.0514  99  ASN   A O   
2224 C CB  A ASN   A 99  ? 0.1901 0.2016 0.1314 0.0189  -0.0057 0.0488  99  ASN   A CB  
2225 C CB  B ASN   A 99  ? 0.2839 0.1787 0.2382 0.0105  -0.0320 0.0554  99  ASN   A CB  
2226 C CG  A ASN   A 99  ? 0.1951 0.2099 0.1791 0.0290  -0.0113 0.0391  99  ASN   A CG  
2227 C CG  B ASN   A 99  ? 0.3075 0.1776 0.2727 0.0081  -0.0367 0.0560  99  ASN   A CG  
2228 O OD1 A ASN   A 99  ? 0.2036 0.2196 0.1957 0.0340  -0.0109 0.0255  99  ASN   A OD1 
2229 O OD1 B ASN   A 99  ? 0.3108 0.1868 0.2617 0.0166  -0.0465 0.0618  99  ASN   A OD1 
2230 N ND2 A ASN   A 99  ? 0.1997 0.2060 0.2126 0.0358  -0.0062 0.0507  99  ASN   A ND2 
2231 N ND2 B ASN   A 99  ? 0.3220 0.1802 0.3199 0.0042  -0.0463 0.0365  99  ASN   A ND2 
2244 N N   A VAL   A 100 ? 0.2288 0.2505 0.1302 -0.0008 -0.0201 0.0507  100 VAL   A N   
2245 N N   B VAL   A 100 ? 0.2887 0.2587 0.1862 0.0043  -0.0324 0.0321  100 VAL   A N   
2246 C CA  A VAL   A 100 ? 0.2509 0.2704 0.1739 -0.0043 -0.0221 0.0494  100 VAL   A CA  
2247 C CA  B VAL   A 100 ? 0.3168 0.2946 0.2362 0.0063  -0.0370 0.0161  100 VAL   A CA  
2248 C C   A VAL   A 100 ? 0.2699 0.2881 0.1958 -0.0067 -0.0392 0.0603  100 VAL   A C   
2249 C C   B VAL   A 100 ? 0.3369 0.3216 0.2510 0.0168  -0.0435 0.0182  100 VAL   A C   
2250 O O   A VAL   A 100 ? 0.2821 0.2930 0.2372 -0.0116 -0.0201 0.0632  100 VAL   A O   
2251 O O   B VAL   A 100 ? 0.3381 0.3281 0.2435 0.0137  -0.0453 0.0150  100 VAL   A O   
2252 C CB  A VAL   A 100 ? 0.2567 0.2729 0.2060 -0.0050 -0.0111 0.0383  100 VAL   A CB  
2253 C CB  B VAL   A 100 ? 0.3254 0.2999 0.2825 0.0005  -0.0365 0.0130  100 VAL   A CB  
2254 C CG1 A VAL   A 100 ? 0.2589 0.2797 0.2194 -0.0092 -0.0023 0.0306  100 VAL   A CG1 
2255 C CG1 B VAL   A 100 ? 0.3274 0.3042 0.2881 -0.0008 -0.0466 0.0164  100 VAL   A CG1 
2256 C CG2 A VAL   A 100 ? 0.2595 0.2701 0.2028 -0.0024 0.0002  0.0435  100 VAL   A CG2 
2257 C CG2 B VAL   A 100 ? 0.3313 0.3017 0.3042 -0.0000 -0.0307 0.0096  100 VAL   A CG2 
2276 N N   A ASN   A 101 ? 0.2780 0.2987 0.1934 -0.0065 -0.0608 0.0738  101 ASN   A N   
2277 N N   B ASN   A 101 ? 0.3525 0.3368 0.2621 0.0341  -0.0461 0.0252  101 ASN   A N   
2278 C CA  A ASN   A 101 ? 0.2907 0.3070 0.2169 -0.0067 -0.0651 0.0792  101 ASN   A CA  
2279 C CA  B ASN   A 101 ? 0.3720 0.3486 0.2808 0.0470  -0.0322 0.0400  101 ASN   A CA  
2280 C C   A ASN   A 101 ? 0.3090 0.3178 0.2357 -0.0031 -0.0415 0.0884  101 ASN   A C   
2281 C C   B ASN   A 101 ? 0.3862 0.3512 0.2868 0.0436  -0.0199 0.0534  101 ASN   A C   
2282 O O   A ASN   A 101 ? 0.3210 0.3163 0.2668 -0.0012 -0.0334 0.0910  101 ASN   A O   
2283 O O   B ASN   A 101 ? 0.3934 0.3520 0.2892 0.0433  -0.0223 0.0646  101 ASN   A O   
2284 C CB  A ASN   A 101 ? 0.2873 0.3001 0.2114 -0.0118 -0.0811 0.0759  101 ASN   A CB  
2285 C CB  B ASN   A 101 ? 0.3790 0.3566 0.3007 0.0549  -0.0247 0.0377  101 ASN   A CB  
2286 C CG  A ASN   A 101 ? 0.2878 0.2978 0.2242 -0.0211 -0.0838 0.0493  101 ASN   A CG  
2287 C CG  B ASN   A 101 ? 0.3824 0.3573 0.3171 0.0632  -0.0246 0.0373  101 ASN   A CG  
2288 O OD1 A ASN   A 101 ? 0.2952 0.3078 0.2383 -0.0244 -0.0758 0.0269  101 ASN   A OD1 
2289 O OD1 B ASN   A 101 ? 0.3810 0.3580 0.3263 0.0640  -0.0295 0.0412  101 ASN   A OD1 
2290 N ND2 A ASN   A 101 ? 0.2837 0.2888 0.2276 -0.0247 -0.0948 0.0437  101 ASN   A ND2 
2291 N ND2 B ASN   A 101 ? 0.3865 0.3600 0.3117 0.0683  -0.0250 0.0410  101 ASN   A ND2 
2304 N N   A LYS   A 102 ? 0.3147 0.3339 0.2624 -0.0051 -0.0279 0.0700  102 LYS   A N   
2305 N N   B LYS   A 102 ? 0.3882 0.3534 0.2986 0.0435  -0.0100 0.0453  102 LYS   A N   
2306 C CA  A LYS   A 102 ? 0.3248 0.3490 0.2770 -0.0063 -0.0254 0.0528  102 LYS   A CA  
2307 C CA  B LYS   A 102 ? 0.3903 0.3576 0.2892 0.0405  -0.0021 0.0502  102 LYS   A CA  
2308 C C   A LYS   A 102 ? 0.3293 0.3584 0.2593 0.0001  -0.0173 0.0450  102 LYS   A C   
2309 C C   B LYS   A 102 ? 0.3768 0.3440 0.2163 0.0478  -0.0044 0.0695  102 LYS   A C   
2310 O O   A LYS   A 102 ? 0.3334 0.3644 0.2629 0.0053  -0.0207 0.0406  102 LYS   A O   
2311 O O   B LYS   A 102 ? 0.3815 0.3439 0.2486 0.0507  0.0031  0.0673  102 LYS   A O   
2312 C CB  A LYS   A 102 ? 0.3299 0.3551 0.3110 -0.0109 -0.0281 0.0329  102 LYS   A CB  
2313 C CB  B LYS   A 102 ? 0.4060 0.3760 0.3458 0.0320  -0.0041 0.0270  102 LYS   A CB  
2314 C CG  A LYS   A 102 ? 0.3330 0.3582 0.3431 -0.0121 -0.0310 0.0123  102 LYS   A CG  
2315 C CG  B LYS   A 102 ? 0.4198 0.3923 0.4010 0.0245  -0.0085 0.0154  102 LYS   A CG  
2316 C CD  A LYS   A 102 ? 0.3370 0.3621 0.3672 -0.0121 -0.0372 -0.0072 102 LYS   A CD  
2317 C CD  B LYS   A 102 ? 0.4298 0.4057 0.4492 0.0198  -0.0126 0.0093  102 LYS   A CD  
2318 C CE  A LYS   A 102 ? 0.3387 0.3648 0.3851 -0.0117 -0.0419 -0.0185 102 LYS   A CE  
2319 C CE  B LYS   A 102 ? 0.4355 0.4133 0.4819 0.0154  -0.0166 0.0089  102 LYS   A CE  
2320 N NZ  A LYS   A 102 ? 0.3396 0.3675 0.3949 -0.0135 -0.0426 -0.0292 102 LYS   A NZ  
2321 N NZ  B LYS   A 102 ? 0.4385 0.4164 0.5074 0.0141  -0.0195 0.0060  102 LYS   A NZ  
2348 N N   A GLY   A 103 ? 0.3290 0.3622 0.2575 0.0024  -0.0109 0.0313  103 GLY   A N   
2349 N N   B GLY   A 103 ? 0.3571 0.3334 0.1341 0.0561  -0.0129 0.0621  103 GLY   A N   
2350 C CA  A GLY   A 103 ? 0.3306 0.3644 0.2570 0.0051  -0.0011 0.0220  103 GLY   A CA  
2351 C CA  B GLY   A 103 ? 0.3396 0.3240 0.1353 0.0592  -0.0172 0.0519  103 GLY   A CA  
2352 C C   A GLY   A 103 ? 0.3309 0.3672 0.2624 0.0045  0.0102  0.0140  103 GLY   A C   
2353 C C   B GLY   A 103 ? 0.3232 0.3116 0.1517 0.0555  -0.0236 0.0423  103 GLY   A C   
2354 O O   A GLY   A 103 ? 0.3374 0.3730 0.2857 0.0087  0.0147  0.0004  103 GLY   A O   
2355 O O   B GLY   A 103 ? 0.3342 0.3144 0.1722 0.0555  -0.0078 0.0358  103 GLY   A O   
2362 N N   A GLU   A 104 ? 0.3235 0.3646 0.2510 -0.0040 0.0209  0.0126  104 GLU   A N   
2363 N N   B GLU   A 104 ? 0.2910 0.2890 0.1411 0.0469  -0.0458 0.0536  104 GLU   A N   
2364 C CA  A GLU   A 104 ? 0.3163 0.3619 0.2448 -0.0144 0.0256  0.0117  104 GLU   A CA  
2365 C CA  B GLU   A 104 ? 0.2654 0.2704 0.1384 0.0294  -0.0397 0.0370  104 GLU   A CA  
2366 C C   A GLU   A 104 ? 0.3216 0.3684 0.2490 -0.0191 0.0242  -0.0010 104 GLU   A C   
2367 C C   B GLU   A 104 ? 0.2572 0.2624 0.1476 0.0240  -0.0321 0.0222  104 GLU   A C   
2368 O O   A GLU   A 104 ? 0.3210 0.3675 0.2479 -0.0223 0.0300  -0.0058 104 GLU   A O   
2369 O O   B GLU   A 104 ? 0.2469 0.2585 0.2012 0.0146  -0.0349 0.0116  104 GLU   A O   
2370 C CB  A GLU   A 104 ? 0.3018 0.3537 0.2286 -0.0201 0.0377  0.0242  104 GLU   A CB  
2371 C CB  B GLU   A 104 ? 0.2546 0.2553 0.1482 0.0136  -0.0329 0.0481  104 GLU   A CB  
2372 C CG  A GLU   A 104 ? 0.2882 0.3453 0.2284 -0.0252 0.0446  0.0319  104 GLU   A CG  
2373 C CG  B GLU   A 104 ? 0.2472 0.2475 0.1538 -0.0070 -0.0203 0.0581  104 GLU   A CG  
2374 C CD  A GLU   A 104 ? 0.2732 0.3363 0.2139 -0.0301 0.0499  0.0404  104 GLU   A CD  
2375 C CD  B GLU   A 104 ? 0.2447 0.2438 0.1561 -0.0238 -0.0268 0.0562  104 GLU   A CD  
2376 O OE1 A GLU   A 104 ? 0.2650 0.3295 0.1854 -0.0334 0.0555  0.0521  104 GLU   A OE1 
2377 O OE1 B GLU   A 104 ? 0.2437 0.2427 0.1501 -0.0285 -0.0360 0.0556  104 GLU   A OE1 
2378 O OE2 A GLU   A 104 ? 0.2726 0.3354 0.2230 -0.0294 0.0524  0.0380  104 GLU   A OE2 
2379 O OE2 B GLU   A 104 ? 0.2510 0.2457 0.1769 -0.0336 -0.0181 0.0610  104 GLU   A OE2 
2392 N N   A ASP   A 105 ? 0.3271 0.3747 0.2560 -0.0177 0.0191  -0.0105 105 ASP   A N   
2393 N N   B ASP   A 105 ? 0.2669 0.2587 0.1522 0.0202  -0.0271 0.0176  105 ASP   A N   
2394 C CA  A ASP   A 105 ? 0.3300 0.3801 0.2731 -0.0171 0.0153  -0.0230 105 ASP   A CA  
2395 C CA  B ASP   A 105 ? 0.2746 0.2492 0.1767 0.0243  -0.0182 -0.0012 105 ASP   A CA  
2396 C C   A ASP   A 105 ? 0.3163 0.3752 0.2626 -0.0216 0.0022  -0.0366 105 ASP   A C   
2397 C C   B ASP   A 105 ? 0.2605 0.2194 0.1531 0.0165  -0.0214 -0.0139 105 ASP   A C   
2398 O O   A ASP   A 105 ? 0.3139 0.3779 0.2481 -0.0212 0.0029  -0.0419 105 ASP   A O   
2399 O O   B ASP   A 105 ? 0.2446 0.1942 0.1132 0.0260  -0.0222 -0.0119 105 ASP   A O   
2400 C CB  A ASP   A 105 ? 0.3451 0.3887 0.3009 -0.0122 0.0238  -0.0195 105 ASP   A CB  
2401 C CB  B ASP   A 105 ? 0.2977 0.2664 0.2373 0.0340  -0.0054 -0.0222 105 ASP   A CB  
2402 C CG  A ASP   A 105 ? 0.3568 0.3942 0.3266 -0.0097 0.0270  -0.0181 105 ASP   A CG  
2403 C CG  B ASP   A 105 ? 0.3173 0.2831 0.2876 0.0458  0.0031  -0.0476 105 ASP   A CG  
2404 O OD1 A ASP   A 105 ? 0.3615 0.3951 0.3299 -0.0134 0.0199  -0.0255 105 ASP   A OD1 
2405 O OD1 B ASP   A 105 ? 0.3270 0.2829 0.2799 0.0379  -0.0021 -0.0663 105 ASP   A OD1 
2406 O OD2 A ASP   A 105 ? 0.3624 0.3977 0.3407 -0.0057 0.0348  -0.0065 105 ASP   A OD2 
2407 O OD2 B ASP   A 105 ? 0.3277 0.2988 0.3519 0.0532  0.0042  -0.0439 105 ASP   A OD2 
2416 N N   A ILE   A 106 ? 0.3032 0.3640 0.2678 -0.0282 -0.0197 -0.0445 106 ILE   A N   
2417 N N   B ILE   A 106 ? 0.2579 0.2273 0.1787 0.0062  -0.0366 -0.0130 106 ILE   A N   
2418 C CA  A ILE   A 106 ? 0.2877 0.3521 0.2784 -0.0357 -0.0388 -0.0513 106 ILE   A CA  
2419 C CA  B ILE   A 106 ? 0.2485 0.2285 0.1985 -0.0075 -0.0509 -0.0190 106 ILE   A CA  
2420 C C   A ILE   A 106 ? 0.2749 0.3331 0.2790 -0.0513 -0.0447 -0.0730 106 ILE   A C   
2421 C C   B ILE   A 106 ? 0.2372 0.2118 0.1921 -0.0169 -0.0493 -0.0103 106 ILE   A C   
2422 O O   A ILE   A 106 ? 0.2637 0.3257 0.2677 -0.0628 -0.0462 -0.0847 106 ILE   A O   
2423 O O   B ILE   A 106 ? 0.2222 0.2133 0.1939 -0.0207 -0.0361 -0.0021 106 ILE   A O   
2424 C CB  A ILE   A 106 ? 0.2879 0.3588 0.3018 -0.0274 -0.0481 -0.0282 106 ILE   A CB  
2425 C CB  B ILE   A 106 ? 0.2612 0.2585 0.2538 -0.0051 -0.0580 -0.0162 106 ILE   A CB  
2426 C CG1 A ILE   A 106 ? 0.2847 0.3632 0.3212 -0.0213 -0.0500 -0.0131 106 ILE   A CG1 
2427 C CG1 B ILE   A 106 ? 0.2726 0.2801 0.2859 0.0015  -0.0460 0.0006  106 ILE   A CG1 
2428 C CG2 A ILE   A 106 ? 0.2903 0.3584 0.3073 -0.0258 -0.0489 -0.0256 106 ILE   A CG2 
2429 C CG2 B ILE   A 106 ? 0.2622 0.2647 0.2685 -0.0054 -0.0626 -0.0217 106 ILE   A CG2 
2430 C CD1 A ILE   A 106 ? 0.2863 0.3658 0.3349 -0.0163 -0.0439 -0.0071 106 ILE   A CD1 
2431 C CD1 B ILE   A 106 ? 0.2834 0.2897 0.3063 0.0069  -0.0285 -0.0006 106 ILE   A CD1 
2454 N N   A GLN   A 107 ? 0.2812 0.3224 0.2967 -0.0477 -0.0325 -0.0848 107 GLN   A N   
2455 N N   B GLN   A 107 ? 0.2538 0.1944 0.1983 -0.0113 -0.0371 -0.0121 107 GLN   A N   
2456 C CA  A GLN   A 107 ? 0.2871 0.3106 0.3386 -0.0358 -0.0148 -0.0820 107 GLN   A CA  
2457 C CA  B GLN   A 107 ? 0.2758 0.1956 0.2697 -0.0025 -0.0233 -0.0093 107 GLN   A CA  
2458 C C   A GLN   A 107 ? 0.2610 0.2779 0.3115 -0.0314 -0.0002 -0.0672 107 GLN   A C   
2459 C C   B GLN   A 107 ? 0.2493 0.1612 0.2372 0.0084  -0.0126 0.0105  107 GLN   A C   
2460 O O   A GLN   A 107 ? 0.2672 0.2805 0.3496 -0.0261 0.0140  -0.0618 107 GLN   A O   
2461 O O   B GLN   A 107 ? 0.2575 0.1584 0.2495 0.0117  -0.0155 0.0115  107 GLN   A O   
2462 C CB  A GLN   A 107 ? 0.3182 0.3325 0.4096 -0.0322 -0.0176 -0.0829 107 GLN   A CB  
2463 C CB  B GLN   A 107 ? 0.3241 0.2418 0.3565 -0.0094 -0.0321 -0.0237 107 GLN   A CB  
2464 C CG  A GLN   A 107 ? 0.3465 0.3551 0.4871 -0.0278 -0.0188 -0.0736 107 GLN   A CG  
2465 C CG  B GLN   A 107 ? 0.3650 0.2857 0.4497 -0.0116 -0.0386 -0.0136 107 GLN   A CG  
2466 C CD  A GLN   A 107 ? 0.3694 0.3730 0.5514 -0.0253 -0.0182 -0.0642 107 GLN   A CD  
2467 C CD  B GLN   A 107 ? 0.3907 0.3213 0.5242 -0.0124 -0.0371 -0.0038 107 GLN   A CD  
2468 O OE1 A GLN   A 107 ? 0.3816 0.3820 0.5771 -0.0206 -0.0166 -0.0599 107 GLN   A OE1 
2469 O OE1 B GLN   A 107 ? 0.4149 0.3336 0.5542 -0.0109 -0.0329 0.0001  107 GLN   A OE1 
2470 N NE2 A GLN   A 107 ? 0.3782 0.3783 0.5712 -0.0284 -0.0182 -0.0660 107 GLN   A NE2 
2471 N NE2 B GLN   A 107 ? 0.4141 0.3333 0.5493 -0.0140 -0.0427 -0.0018 107 GLN   A NE2 
2488 N N   A LEU   A 108 ? 0.2303 0.2421 0.2477 -0.0300 0.0047  -0.0629 108 LEU   A N   
2489 N N   B LEU   A 108 ? 0.2270 0.1535 0.2002 -0.0007 0.0091  -0.0049 108 LEU   A N   
2490 C CA  A LEU   A 108 ? 0.2046 0.2111 0.2071 -0.0210 0.0040  -0.0287 108 LEU   A CA  
2491 C CA  B LEU   A 108 ? 0.2053 0.1536 0.1874 0.0010  0.0093  0.0085  108 LEU   A CA  
2492 C C   A LEU   A 108 ? 0.1810 0.1742 0.1848 -0.0079 -0.0041 -0.0084 108 LEU   A C   
2493 C C   B LEU   A 108 ? 0.1790 0.1398 0.1688 0.0019  0.0030  0.0156  108 LEU   A C   
2494 O O   A LEU   A 108 ? 0.1800 0.1756 0.1967 -0.0099 -0.0021 -0.0072 108 LEU   A O   
2495 O O   B LEU   A 108 ? 0.1784 0.1418 0.1801 -0.0028 0.0263  0.0210  108 LEU   A O   
2496 C CB  A LEU   A 108 ? 0.2071 0.2199 0.1884 -0.0279 0.0104  -0.0224 108 LEU   A CB  
2497 C CB  B LEU   A 108 ? 0.2114 0.1705 0.1762 -0.0042 0.0089  0.0054  108 LEU   A CB  
2498 C CG  A LEU   A 108 ? 0.2163 0.2355 0.2010 -0.0235 0.0250  -0.0133 108 LEU   A CG  
2499 C CG  B LEU   A 108 ? 0.2239 0.1913 0.2087 0.0066  0.0152  0.0105  108 LEU   A CG  
2500 C CD1 A LEU   A 108 ? 0.2207 0.2395 0.2088 -0.0237 0.0398  -0.0094 108 LEU   A CD1 
2501 C CD1 B LEU   A 108 ? 0.2323 0.1963 0.2219 0.0056  0.0321  0.0154  108 LEU   A CD1 
2502 C CD2 A LEU   A 108 ? 0.2176 0.2495 0.2274 -0.0218 0.0340  -0.0085 108 LEU   A CD2 
2503 C CD2 B LEU   A 108 ? 0.2259 0.2136 0.2458 0.0113  0.0203  0.0115  108 LEU   A CD2 
2526 N N   . LEU   A 109 ? 0.1675 0.1484 0.1781 0.0058  -0.0029 0.0106  109 LEU   A N   
2527 C CA  . LEU   A 109 ? 0.1601 0.1431 0.1601 0.0032  -0.0106 0.0108  109 LEU   A CA  
2528 C C   . LEU   A 109 ? 0.1460 0.1364 0.1456 0.0001  -0.0026 0.0050  109 LEU   A C   
2529 O O   . LEU   A 109 ? 0.1515 0.1318 0.1663 -0.0060 -0.0039 0.0014  109 LEU   A O   
2530 C CB  . LEU   A 109 ? 0.1674 0.1506 0.1744 0.0083  -0.0190 0.0207  109 LEU   A CB  
2531 C CG  . LEU   A 109 ? 0.1623 0.1630 0.2005 0.0008  -0.0132 0.0269  109 LEU   A CG  
2532 C CD1 . LEU   A 109 ? 0.1639 0.1490 0.2038 -0.0074 -0.0042 0.0093  109 LEU   A CD1 
2533 C CD2 . LEU   A 109 ? 0.1649 0.1744 0.2327 -0.0043 -0.0220 0.0292  109 LEU   A CD2 
2546 N N   . LYS   A 110 ? 0.1516 0.1372 0.1456 0.0052  -0.0129 0.0032  110 LYS   A N   
2547 C CA  . LYS   A 110 ? 0.1444 0.1294 0.1669 -0.0038 -0.0116 0.0030  110 LYS   A CA  
2548 C C   . LYS   A 110 ? 0.1456 0.1173 0.1553 -0.0111 -0.0020 -0.0025 110 LYS   A C   
2549 O O   . LYS   A 110 ? 0.1416 0.1219 0.1643 -0.0075 0.0021  -0.0031 110 LYS   A O   
2550 C CB  . LYS   A 110 ? 0.1633 0.1375 0.1991 -0.0019 -0.0164 -0.0037 110 LYS   A CB  
2551 C CG  . LYS   A 110 ? 0.1509 0.1344 0.2095 0.0006  -0.0095 -0.0020 110 LYS   A CG  
2552 C CD  . LYS   A 110 ? 0.1511 0.1404 0.2051 -0.0095 0.0042  -0.0135 110 LYS   A CD  
2553 C CE  . LYS   A 110 ? 0.1628 0.1431 0.2402 -0.0094 0.0161  -0.0073 110 LYS   A CE  
2554 N NZ  . LYS   A 110 ? 0.1641 0.1426 0.2500 -0.0149 0.0161  0.0058  110 LYS   A NZ  
2568 N N   . SER   A 111 ? 0.1519 0.1254 0.1534 -0.0048 -0.0018 0.0068  111 SER   A N   
2569 C CA  . SER   A 111 ? 0.1399 0.1386 0.1571 -0.0037 -0.0032 -0.0045 111 SER   A CA  
2570 C C   . SER   A 111 ? 0.1355 0.1245 0.1557 -0.0033 -0.0057 0.0089  111 SER   A C   
2571 O O   . SER   A 111 ? 0.1470 0.1165 0.1683 -0.0031 0.0041  0.0088  111 SER   A O   
2572 C CB  . SER   A 111 ? 0.1609 0.1603 0.1674 -0.0067 0.0124  -0.0100 111 SER   A CB  
2573 O OG  . SER   A 111 ? 0.2090 0.1831 0.1709 0.0034  0.0184  -0.0191 111 SER   A OG  
2579 N N   . ALA   A 112 ? 0.1375 0.1172 0.1519 -0.0025 -0.0002 0.0008  112 ALA   A N   
2580 C CA  . ALA   A 112 ? 0.1340 0.1109 0.1499 -0.0049 0.0044  0.0021  112 ALA   A CA  
2581 C C   . ALA   A 112 ? 0.1243 0.1087 0.1534 0.0041  -0.0015 0.0071  112 ALA   A C   
2582 O O   . ALA   A 112 ? 0.1283 0.1171 0.1595 -0.0121 0.0056  0.0097  112 ALA   A O   
2583 C CB  . ALA   A 112 ? 0.1470 0.1183 0.1692 -0.0040 0.0042  0.0133  112 ALA   A CB  
2589 N N   A TYR   A 113 ? 0.1214 0.1191 0.1642 -0.0031 0.0006  0.0112  113 TYR   A N   
2590 N N   B TYR   A 113 ? 0.1198 0.1169 0.1648 -0.0096 0.0045  0.0145  113 TYR   A N   
2591 C CA  A TYR   A 113 ? 0.1209 0.1166 0.1574 0.0005  0.0051  0.0095  113 TYR   A CA  
2592 C CA  B TYR   A 113 ? 0.1190 0.1061 0.1542 -0.0076 0.0111  0.0134  113 TYR   A CA  
2593 C C   A TYR   A 113 ? 0.1260 0.1146 0.1551 -0.0035 0.0010  0.0117  113 TYR   A C   
2594 C C   B TYR   A 113 ? 0.1242 0.1083 0.1498 -0.0082 0.0027  0.0132  113 TYR   A C   
2595 O O   A TYR   A 113 ? 0.1326 0.1159 0.1650 0.0000  0.0033  0.0117  113 TYR   A O   
2596 O O   B TYR   A 113 ? 0.1308 0.1094 0.1579 -0.0017 0.0065  0.0064  113 TYR   A O   
2597 C CB  A TYR   A 113 ? 0.1228 0.1326 0.1571 0.0067  -0.0023 0.0103  113 TYR   A CB  
2598 C CB  B TYR   A 113 ? 0.1246 0.1163 0.1579 -0.0078 0.0014  0.0193  113 TYR   A CB  
2599 C CG  A TYR   A 113 ? 0.1239 0.1413 0.1584 0.0050  0.0044  0.0091  113 TYR   A CG  
2600 C CG  B TYR   A 113 ? 0.1259 0.1089 0.1607 -0.0175 0.0042  0.0224  113 TYR   A CG  
2601 C CD1 A TYR   A 113 ? 0.1246 0.1546 0.1704 0.0093  0.0070  0.0028  113 TYR   A CD1 
2602 C CD1 B TYR   A 113 ? 0.1311 0.1098 0.1708 -0.0054 0.0003  0.0161  113 TYR   A CD1 
2603 C CD2 A TYR   A 113 ? 0.1295 0.1480 0.1580 0.0044  0.0035  0.0050  113 TYR   A CD2 
2604 C CD2 B TYR   A 113 ? 0.1333 0.1212 0.1687 -0.0195 -0.0008 0.0163  113 TYR   A CD2 
2605 C CE1 A TYR   A 113 ? 0.1267 0.1608 0.1766 0.0099  0.0095  0.0037  113 TYR   A CE1 
2606 C CE1 B TYR   A 113 ? 0.1432 0.1183 0.1720 0.0039  -0.0076 0.0197  113 TYR   A CE1 
2607 C CE2 A TYR   A 113 ? 0.1238 0.1582 0.1662 0.0067  0.0058  0.0126  113 TYR   A CE2 
2608 C CE2 B TYR   A 113 ? 0.1396 0.1344 0.1795 -0.0069 -0.0093 0.0209  113 TYR   A CE2 
2609 C CZ  A TYR   A 113 ? 0.1210 0.1620 0.1655 0.0110  0.0119  0.0158  113 TYR   A CZ  
2610 C CZ  B TYR   A 113 ? 0.1417 0.1314 0.1935 0.0079  -0.0124 0.0205  113 TYR   A CZ  
2611 O OH  A TYR   A 113 ? 0.1114 0.1635 0.1542 0.0116  0.0134  0.0232  113 TYR   A OH  
2612 O OH  B TYR   A 113 ? 0.1480 0.1409 0.2238 0.0176  -0.0231 0.0107  113 TYR   A OH  
2631 N N   . GLU   A 114 ? 0.1273 0.1105 0.1573 0.0001  0.0089  0.0120  114 GLU   A N   
2632 C CA  . GLU   A 114 ? 0.1293 0.1112 0.1722 0.0052  0.0031  0.0125  114 GLU   A CA  
2633 C C   . GLU   A 114 ? 0.1181 0.1110 0.1641 0.0044  0.0104  0.0195  114 GLU   A C   
2634 O O   . GLU   A 114 ? 0.1338 0.1175 0.1549 0.0055  0.0021  0.0117  114 GLU   A O   
2635 C CB  . GLU   A 114 ? 0.1237 0.1205 0.1732 -0.0003 0.0004  0.0121  114 GLU   A CB  
2636 C CG  . GLU   A 114 ? 0.1348 0.1235 0.1865 0.0009  0.0094  0.0041  114 GLU   A CG  
2637 C CD  . GLU   A 114 ? 0.1434 0.1249 0.1892 -0.0067 0.0013  0.0008  114 GLU   A CD  
2638 O OE1 . GLU   A 114 ? 0.1453 0.1157 0.1964 -0.0067 0.0078  -0.0048 114 GLU   A OE1 
2639 O OE2 . GLU   A 114 ? 0.1686 0.1319 0.2103 -0.0074 0.0092  -0.0152 114 GLU   A OE2 
2647 N N   . ASN   A 115 ? 0.1190 0.1165 0.1476 -0.0033 0.0082  0.0065  115 ASN   A N   
2648 C CA  . ASN   A 115 ? 0.1269 0.1199 0.1554 -0.0057 0.0155  0.0146  115 ASN   A CA  
2649 C C   . ASN   A 115 ? 0.1288 0.1166 0.1436 -0.0099 0.0041  0.0097  115 ASN   A C   
2650 O O   . ASN   A 115 ? 0.1344 0.1319 0.1417 -0.0093 0.0071  0.0156  115 ASN   A O   
2651 C CB  . ASN   A 115 ? 0.1420 0.1299 0.1490 -0.0107 0.0155  0.0050  115 ASN   A CB  
2652 C CG  . ASN   A 115 ? 0.1330 0.1482 0.1542 -0.0161 0.0177  0.0129  115 ASN   A CG  
2653 O OD1 . ASN   A 115 ? 0.1400 0.2555 0.1656 -0.0165 0.0225  0.0302  115 ASN   A OD1 
2654 N ND2 . ASN   A 115 ? 0.1326 0.1240 0.1566 -0.0061 0.0241  0.0120  115 ASN   A ND2 
2661 N N   . PHE   A 116 ? 0.1170 0.1263 0.1484 0.0024  0.0099  0.0170  116 PHE   A N   
2662 C CA  . PHE   A 116 ? 0.1202 0.1283 0.1411 0.0001  0.0159  0.0155  116 PHE   A CA  
2663 C C   . PHE   A 116 ? 0.1200 0.1335 0.1570 -0.0050 0.0150  0.0187  116 PHE   A C   
2664 O O   . PHE   A 116 ? 0.1339 0.1334 0.1585 0.0057  0.0209  0.0322  116 PHE   A O   
2665 C CB  . PHE   A 116 ? 0.1278 0.1212 0.1456 -0.0017 0.0180  0.0101  116 PHE   A CB  
2666 C CG  . PHE   A 116 ? 0.1207 0.1243 0.1418 -0.0035 0.0107  0.0152  116 PHE   A CG  
2667 C CD1 . PHE   A 116 ? 0.1257 0.1241 0.1636 -0.0071 0.0063  0.0213  116 PHE   A CD1 
2668 C CD2 . PHE   A 116 ? 0.1252 0.1347 0.1736 -0.0021 0.0115  0.0201  116 PHE   A CD2 
2669 C CE1 . PHE   A 116 ? 0.1254 0.1231 0.1755 -0.0181 0.0035  0.0190  116 PHE   A CE1 
2670 C CE2 . PHE   A 116 ? 0.1185 0.1260 0.1940 -0.0013 0.0097  0.0171  116 PHE   A CE2 
2671 C CZ  . PHE   A 116 ? 0.1275 0.1156 0.1718 -0.0029 0.0041  0.0138  116 PHE   A CZ  
2681 N N   . ASN   A 117 ? 0.1199 0.1232 0.1571 -0.0014 0.0139  0.0232  117 ASN   A N   
2682 C CA  . ASN   A 117 ? 0.1246 0.1284 0.1706 0.0033  0.0211  0.0279  117 ASN   A CA  
2683 C C   . ASN   A 117 ? 0.1234 0.1347 0.1767 0.0037  0.0160  0.0271  117 ASN   A C   
2684 O O   . ASN   A 117 ? 0.1397 0.1469 0.1832 0.0010  0.0071  0.0405  117 ASN   A O   
2685 C CB  . ASN   A 117 ? 0.1272 0.1299 0.1660 -0.0021 0.0171  0.0331  117 ASN   A CB  
2686 C CG  . ASN   A 117 ? 0.1316 0.1219 0.1788 -0.0029 0.0230  0.0337  117 ASN   A CG  
2687 O OD1 . ASN   A 117 ? 0.1340 0.1407 0.1911 -0.0147 0.0214  0.0131  117 ASN   A OD1 
2688 N ND2 . ASN   A 117 ? 0.1227 0.1251 0.1814 -0.0016 0.0117  0.0234  117 ASN   A ND2 
2695 N N   . GLN   A 118 ? 0.1189 0.1353 0.1746 -0.0023 0.0003  0.0298  118 GLN   A N   
2696 C CA  . GLN   A 118 ? 0.1298 0.1435 0.1843 -0.0029 -0.0007 0.0224  118 GLN   A CA  
2697 C C   . GLN   A 118 ? 0.1311 0.1543 0.1818 -0.0014 0.0017  0.0301  118 GLN   A C   
2698 O O   . GLN   A 118 ? 0.1353 0.1835 0.1928 0.0028  -0.0048 0.0113  118 GLN   A O   
2699 C CB  . GLN   A 118 ? 0.1259 0.1373 0.1942 0.0047  0.0171  0.0222  118 GLN   A CB  
2700 C CG  . GLN   A 118 ? 0.1265 0.1331 0.2076 -0.0013 0.0162  0.0284  118 GLN   A CG  
2701 C CD  . GLN   A 118 ? 0.1299 0.1535 0.2038 -0.0001 0.0127  0.0213  118 GLN   A CD  
2702 O OE1 . GLN   A 118 ? 0.1374 0.1670 0.2200 0.0127  -0.0048 0.0108  118 GLN   A OE1 
2703 N NE2 . GLN   A 118 ? 0.1384 0.1575 0.1932 0.0095  0.0066  0.0253  118 GLN   A NE2 
2712 N N   . HIS   A 119 ? 0.1358 0.1419 0.1719 0.0016  0.0045  0.0255  119 HIS   A N   
2713 C CA  . HIS   A 119 ? 0.1415 0.1500 0.1675 -0.0035 0.0089  0.0329  119 HIS   A CA  
2714 C C   . HIS   A 119 ? 0.1512 0.1612 0.1682 -0.0014 0.0191  0.0387  119 HIS   A C   
2715 O O   . HIS   A 119 ? 0.1545 0.1636 0.1774 -0.0199 -0.0011 0.0349  119 HIS   A O   
2716 C CB  . HIS   A 119 ? 0.1441 0.1521 0.1767 -0.0027 0.0263  0.0344  119 HIS   A CB  
2717 C CG  . HIS   A 119 ? 0.1492 0.1571 0.2262 0.0052  0.0158  0.0424  119 HIS   A CG  
2718 N ND1 . HIS   A 119 ? 0.1588 0.1704 0.2915 -0.0090 0.0129  0.0264  119 HIS   A ND1 
2719 C CD2 . HIS   A 119 ? 0.1545 0.1634 0.2530 0.0176  0.0265  0.0588  119 HIS   A CD2 
2720 C CE1 . HIS   A 119 ? 0.1583 0.1743 0.3078 -0.0095 0.0327  0.0487  119 HIS   A CE1 
2721 N NE2 . HIS   A 119 ? 0.1632 0.1704 0.2914 0.0014  0.0434  0.0717  119 HIS   A NE2 
2729 N N   . GLU   A 120 ? 0.1538 0.1827 0.1585 0.0045  0.0069  0.0583  120 GLU   A N   
2730 C CA  . GLU   A 120 ? 0.1676 0.2148 0.1949 0.0164  0.0053  0.0890  120 GLU   A CA  
2731 C C   . GLU   A 120 ? 0.1543 0.1952 0.1873 0.0011  0.0132  0.0896  120 GLU   A C   
2732 O O   . GLU   A 120 ? 0.1531 0.1961 0.2050 -0.0040 0.0100  0.0842  120 GLU   A O   
2733 C CB  . GLU   A 120 ? 0.2096 0.2692 0.2576 0.0270  0.0013  0.1377  120 GLU   A CB  
2734 C CG  . GLU   A 120 ? 0.2731 0.3174 0.3761 0.0391  -0.0101 0.1335  120 GLU   A CG  
2735 C CD  . GLU   A 120 ? 0.3231 0.3533 0.4751 0.0485  -0.0105 0.1332  120 GLU   A CD  
2736 O OE1 . GLU   A 120 ? 0.3749 0.3844 0.4947 0.0455  -0.0085 0.1311  120 GLU   A OE1 
2737 O OE2 . GLU   A 120 ? 0.3973 0.3973 0.5234 0.0454  -0.0121 0.1317  120 GLU   A OE2 
2744 N N   . VAL   A 121 ? 0.1524 0.1916 0.1657 0.0051  0.0150  0.0693  121 VAL   A N   
2745 C CA  . VAL   A 121 ? 0.1647 0.2024 0.1474 0.0041  0.0210  0.0636  121 VAL   A CA  
2746 C C   . VAL   A 121 ? 0.1492 0.1821 0.1338 -0.0111 0.0081  0.0587  121 VAL   A C   
2747 O O   . VAL   A 121 ? 0.1480 0.1812 0.1606 -0.0200 0.0015  0.0379  121 VAL   A O   
2748 C CB  . VAL   A 121 ? 0.2015 0.2412 0.1826 0.0081  0.0354  0.0705  121 VAL   A CB  
2749 C CG1 . VAL   A 121 ? 0.2025 0.2575 0.1950 0.0181  0.0392  0.0786  121 VAL   A CG1 
2750 C CG2 . VAL   A 121 ? 0.2294 0.2586 0.2429 -0.0034 0.0284  0.0525  121 VAL   A CG2 
2760 N N   . LEU   A 122 ? 0.1420 0.1570 0.1360 -0.0099 0.0098  0.0451  122 LEU   A N   
2761 C CA  . LEU   A 122 ? 0.1443 0.1477 0.1421 -0.0142 0.0312  0.0450  122 LEU   A CA  
2762 C C   . LEU   A 122 ? 0.1377 0.1501 0.1376 -0.0101 0.0101  0.0395  122 LEU   A C   
2763 O O   . LEU   A 122 ? 0.1375 0.1548 0.1817 -0.0263 0.0059  0.0399  122 LEU   A O   
2764 C CB  . LEU   A 122 ? 0.1642 0.1451 0.1854 -0.0036 0.0220  0.0565  122 LEU   A CB  
2765 C CG  . LEU   A 122 ? 0.1699 0.1534 0.1698 -0.0033 0.0311  0.0320  122 LEU   A CG  
2766 C CD1 . LEU   A 122 ? 0.1881 0.1561 0.1781 -0.0075 0.0284  0.0367  122 LEU   A CD1 
2767 C CD2 . LEU   A 122 ? 0.1639 0.1528 0.1673 0.0035  0.0363  0.0189  122 LEU   A CD2 
2779 N N   . LEU   A 123 ? 0.1344 0.1426 0.1291 -0.0147 0.0049  0.0329  123 LEU   A N   
2780 C CA  . LEU   A 123 ? 0.1363 0.1455 0.1315 -0.0135 0.0146  0.0301  123 LEU   A CA  
2781 C C   . LEU   A 123 ? 0.1320 0.1378 0.1253 -0.0067 0.0104  0.0359  123 LEU   A C   
2782 O O   . LEU   A 123 ? 0.1231 0.1505 0.1386 -0.0206 0.0103  0.0325  123 LEU   A O   
2783 C CB  . LEU   A 123 ? 0.1473 0.1545 0.1452 -0.0128 0.0218  0.0269  123 LEU   A CB  
2784 C CG  . LEU   A 123 ? 0.1510 0.1678 0.1549 -0.0077 0.0183  0.0171  123 LEU   A CG  
2785 C CD1 . LEU   A 123 ? 0.1514 0.1700 0.1714 -0.0072 0.0145  0.0100  123 LEU   A CD1 
2786 C CD2 . LEU   A 123 ? 0.1590 0.1714 0.1686 -0.0025 0.0133  0.0155  123 LEU   A CD2 
2798 N N   . ALA   A 124 ? 0.1303 0.1358 0.1201 -0.0077 0.0028  0.0276  124 ALA   A N   
2799 C CA  . ALA   A 124 ? 0.1201 0.1348 0.1326 -0.0047 -0.0024 0.0260  124 ALA   A CA  
2800 C C   . ALA   A 124 ? 0.1242 0.1298 0.1371 -0.0105 0.0113  0.0328  124 ALA   A C   
2801 O O   . ALA   A 124 ? 0.1266 0.1399 0.1579 -0.0126 0.0143  0.0369  124 ALA   A O   
2802 C CB  . ALA   A 124 ? 0.1182 0.1357 0.1483 -0.0026 0.0063  0.0294  124 ALA   A CB  
2808 N N   A PRO   A 125 ? 0.1276 0.1321 0.1376 -0.0018 -0.0038 0.0307  125 PRO   A N   
2809 N N   B PRO   A 125 ? 0.1165 0.1183 0.1310 -0.0101 0.0069  0.0313  125 PRO   A N   
2810 C CA  A PRO   A 125 ? 0.1346 0.1386 0.1458 0.0015  -0.0174 0.0252  125 PRO   A CA  
2811 C CA  B PRO   A 125 ? 0.1247 0.1270 0.1375 -0.0105 0.0023  0.0247  125 PRO   A CA  
2812 C C   A PRO   A 125 ? 0.1259 0.1426 0.1612 0.0089  -0.0174 0.0200  125 PRO   A C   
2813 C C   B PRO   A 125 ? 0.1180 0.1305 0.1475 -0.0107 0.0179  0.0234  125 PRO   A C   
2814 O O   A PRO   A 125 ? 0.1230 0.1356 0.1691 0.0072  -0.0221 0.0160  125 PRO   A O   
2815 O O   B PRO   A 125 ? 0.1276 0.1241 0.1700 -0.0144 0.0065  0.0168  125 PRO   A O   
2816 C CB  A PRO   A 125 ? 0.1454 0.1394 0.1449 -0.0057 -0.0120 0.0267  125 PRO   A CB  
2817 C CB  B PRO   A 125 ? 0.1325 0.1261 0.1368 -0.0163 0.0121  0.0297  125 PRO   A CB  
2818 C CG  A PRO   A 125 ? 0.1435 0.1392 0.1515 -0.0075 -0.0133 0.0220  125 PRO   A CG  
2819 C CG  B PRO   A 125 ? 0.1231 0.1235 0.1361 -0.0172 0.0165  0.0256  125 PRO   A CG  
2820 C CD  A PRO   A 125 ? 0.1345 0.1374 0.1405 -0.0058 -0.0012 0.0218  125 PRO   A CD  
2821 C CD  B PRO   A 125 ? 0.1152 0.1137 0.1198 -0.0178 0.0208  0.0216  125 PRO   A CD  
2836 N N   A LEU   A 126 ? 0.1303 0.1565 0.1634 0.0115  -0.0281 0.0184  126 LEU   A N   
2837 N N   B LEU   A 126 ? 0.1216 0.1424 0.1552 -0.0130 0.0062  0.0235  126 LEU   A N   
2838 C CA  A LEU   A 126 ? 0.1323 0.1632 0.1730 0.0049  -0.0235 0.0175  126 LEU   A CA  
2839 C CA  B LEU   A 126 ? 0.1257 0.1354 0.1656 -0.0153 0.0014  0.0292  126 LEU   A CA  
2840 C C   A LEU   A 126 ? 0.1367 0.1642 0.1828 -0.0025 -0.0172 0.0100  126 LEU   A C   
2841 C C   B LEU   A 126 ? 0.1298 0.1291 0.1603 -0.0001 -0.0010 0.0100  126 LEU   A C   
2842 O O   A LEU   A 126 ? 0.1387 0.1599 0.2001 -0.0071 -0.0011 0.0038  126 LEU   A O   
2843 O O   B LEU   A 126 ? 0.1488 0.1292 0.2014 0.0000  0.0214  0.0122  126 LEU   A O   
2844 C CB  A LEU   A 126 ? 0.1376 0.1669 0.1682 -0.0033 -0.0263 0.0177  126 LEU   A CB  
2845 C CB  B LEU   A 126 ? 0.1439 0.1598 0.1911 -0.0242 -0.0079 0.0344  126 LEU   A CB  
2846 C CG  A LEU   A 126 ? 0.1326 0.1760 0.1698 -0.0110 -0.0075 0.0163  126 LEU   A CG  
2847 C CG  B LEU   A 126 ? 0.1482 0.1748 0.2216 -0.0205 -0.0092 0.0427  126 LEU   A CG  
2848 C CD1 A LEU   A 126 ? 0.1299 0.1772 0.1682 -0.0128 -0.0006 0.0096  126 LEU   A CD1 
2849 C CD1 B LEU   A 126 ? 0.1466 0.1819 0.2305 -0.0109 -0.0161 0.0396  126 LEU   A CD1 
2850 C CD2 A LEU   A 126 ? 0.1420 0.1773 0.1656 -0.0163 -0.0146 0.0288  126 LEU   A CD2 
2851 C CD2 B LEU   A 126 ? 0.1571 0.1801 0.2373 -0.0301 -0.0100 0.0425  126 LEU   A CD2 
2874 N N   A LEU   A 127 ? 0.1476 0.1751 0.1869 -0.0032 -0.0099 0.0042  127 LEU   A N   
2875 N N   B LEU   A 127 ? 0.1298 0.1325 0.1481 0.0053  0.0015  0.0046  127 LEU   A N   
2876 C CA  A LEU   A 127 ? 0.1577 0.1715 0.1858 -0.0065 -0.0021 0.0043  127 LEU   A CA  
2877 C CA  B LEU   A 127 ? 0.1336 0.1438 0.1657 0.0045  0.0033  0.0166  127 LEU   A CA  
2878 C C   A LEU   A 127 ? 0.1598 0.1616 0.1664 -0.0135 0.0132  0.0123  127 LEU   A C   
2879 C C   B LEU   A 127 ? 0.1366 0.1628 0.1741 -0.0007 -0.0042 0.0234  127 LEU   A C   
2880 O O   A LEU   A 127 ? 0.1700 0.1758 0.1575 -0.0204 0.0251  0.0109  127 LEU   A O   
2881 O O   B LEU   A 127 ? 0.1446 0.1746 0.1555 -0.0178 -0.0082 0.0195  127 LEU   A O   
2882 C CB  A LEU   A 127 ? 0.1609 0.1724 0.1843 0.0035  -0.0019 -0.0033 127 LEU   A CB  
2883 C CB  B LEU   A 127 ? 0.1377 0.1539 0.1777 -0.0000 0.0144  0.0053  127 LEU   A CB  
2884 C CG  A LEU   A 127 ? 0.1636 0.1696 0.1854 0.0061  -0.0049 0.0049  127 LEU   A CG  
2885 C CG  B LEU   A 127 ? 0.1415 0.1749 0.1850 0.0003  0.0094  0.0179  127 LEU   A CG  
2886 C CD1 A LEU   A 127 ? 0.1680 0.1658 0.1899 0.0034  -0.0081 0.0044  127 LEU   A CD1 
2887 C CD1 B LEU   A 127 ? 0.1362 0.1845 0.2105 0.0030  0.0147  0.0284  127 LEU   A CD1 
2888 C CD2 A LEU   A 127 ? 0.1640 0.1675 0.2078 0.0067  -0.0065 0.0156  127 LEU   A CD2 
2889 C CD2 B LEU   A 127 ? 0.1592 0.1889 0.1986 0.0029  -0.0096 0.0062  127 LEU   A CD2 
2912 N N   A SER   A 128 ? 0.1617 0.1544 0.1741 -0.0133 0.0103  0.0199  128 SER   A N   
2913 N N   B SER   A 128 ? 0.1503 0.1792 0.2078 0.0087  -0.0020 0.0320  128 SER   A N   
2914 C CA  A SER   A 128 ? 0.1673 0.1662 0.1498 -0.0160 0.0023  0.0256  128 SER   A CA  
2915 C CA  B SER   A 128 ? 0.1743 0.2139 0.2076 0.0115  -0.0108 0.0349  128 SER   A CA  
2916 C C   A SER   A 128 ? 0.1688 0.1595 0.1369 -0.0107 -0.0164 0.0181  128 SER   A C   
2917 C C   B SER   A 128 ? 0.2054 0.2333 0.2214 0.0162  -0.0340 0.0463  128 SER   A C   
2918 O O   A SER   A 128 ? 0.1835 0.1605 0.1430 -0.0071 -0.0115 0.0157  128 SER   A O   
2919 O O   B SER   A 128 ? 0.2178 0.2343 0.2134 0.0076  -0.0369 0.0429  128 SER   A O   
2920 C CB  A SER   A 128 ? 0.1709 0.1785 0.1328 -0.0331 0.0046  0.0343  128 SER   A CB  
2921 C CB  B SER   A 128 ? 0.1608 0.2150 0.1711 -0.0080 -0.0261 0.0446  128 SER   A CB  
2922 O OG  A SER   A 128 ? 0.1735 0.1820 0.1518 -0.0239 0.0088  0.0161  128 SER   A OG  
2923 O OG  B SER   A 128 ? 0.1425 0.2001 0.1394 -0.0147 -0.0216 0.0366  128 SER   A OG  
2934 N N   A ALA   A 129 ? 0.1583 0.1663 0.1478 -0.0055 -0.0183 0.0234  129 ALA   A N   
2935 N N   B ALA   A 129 ? 0.2245 0.2605 0.2411 0.0283  -0.0449 0.0581  129 ALA   A N   
2936 C CA  A ALA   A 129 ? 0.1538 0.1740 0.1654 -0.0026 -0.0202 0.0274  129 ALA   A CA  
2937 C CA  B ALA   A 129 ? 0.2534 0.2821 0.2743 0.0181  -0.0413 0.0505  129 ALA   A CA  
2938 C C   A ALA   A 129 ? 0.1509 0.1825 0.1632 0.0034  -0.0215 -0.0015 129 ALA   A C   
2939 C C   B ALA   A 129 ? 0.2806 0.2948 0.2778 0.0082  -0.0236 0.0432  129 ALA   A C   
2940 O O   A ALA   A 129 ? 0.1498 0.1918 0.1652 -0.0074 -0.0075 0.0005  129 ALA   A O   
2941 O O   B ALA   A 129 ? 0.2876 0.3011 0.2882 -0.0129 -0.0132 0.0320  129 ALA   A O   
2942 C CB  A ALA   A 129 ? 0.1594 0.1903 0.2047 0.0023  -0.0144 0.0405  129 ALA   A CB  
2943 C CB  B ALA   A 129 ? 0.2563 0.2913 0.2866 0.0071  -0.0356 0.0541  129 ALA   A CB  
2954 N N   A GLY   A 130 ? 0.1639 0.1786 0.1762 0.0086  -0.0262 -0.0267 130 GLY   A N   
2955 N N   B GLY   A 130 ? 0.2994 0.2993 0.2688 0.0140  -0.0268 0.0393  130 GLY   A N   
2956 C CA  A GLY   A 130 ? 0.1795 0.1791 0.1870 0.0121  -0.0256 -0.0167 130 GLY   A CA  
2957 C CA  B GLY   A 130 ? 0.3124 0.3021 0.2666 0.0209  -0.0338 0.0381  130 GLY   A CA  
2958 C C   A GLY   A 130 ? 0.1876 0.1751 0.1817 0.0108  -0.0279 -0.0052 130 GLY   A C   
2959 C C   B GLY   A 130 ? 0.3244 0.3082 0.2605 0.0170  -0.0383 0.0272  130 GLY   A C   
2960 O O   A GLY   A 130 ? 0.1924 0.1713 0.1801 0.0071  -0.0161 0.0066  130 GLY   A O   
2961 O O   B GLY   A 130 ? 0.3307 0.3110 0.2342 0.0159  -0.0350 0.0235  130 GLY   A O   
2968 N N   A ILE   A 131 ? 0.2014 0.1715 0.1851 0.0045  -0.0295 0.0115  131 ILE   A N   
2969 N N   B ILE   A 131 ? 0.3281 0.3052 0.2884 0.0181  -0.0325 0.0231  131 ILE   A N   
2970 C CA  A ILE   A 131 ? 0.2082 0.1747 0.1783 -0.0063 -0.0549 0.0136  131 ILE   A CA  
2971 C CA  B ILE   A 131 ? 0.3340 0.2999 0.3140 0.0152  -0.0327 0.0206  131 ILE   A CA  
2972 C C   A ILE   A 131 ? 0.2039 0.1741 0.1930 -0.0175 -0.0544 0.0205  131 ILE   A C   
2973 C C   B ILE   A 131 ? 0.3263 0.2860 0.3013 0.0219  -0.0416 0.0255  131 ILE   A C   
2974 O O   A ILE   A 131 ? 0.2063 0.1778 0.1859 -0.0247 -0.0715 0.0223  131 ILE   A O   
2975 O O   B ILE   A 131 ? 0.3326 0.2835 0.3022 0.0250  -0.0282 0.0225  131 ILE   A O   
2976 C CB  A ILE   A 131 ? 0.2181 0.1824 0.1877 -0.0013 -0.0531 0.0157  131 ILE   A CB  
2977 C CB  B ILE   A 131 ? 0.3487 0.3115 0.3468 0.0047  -0.0274 0.0103  131 ILE   A CB  
2978 C CG1 A ILE   A 131 ? 0.2163 0.2034 0.2196 -0.0093 -0.0525 0.0015  131 ILE   A CG1 
2979 C CG1 B ILE   A 131 ? 0.3558 0.3148 0.3660 -0.0022 -0.0216 0.0066  131 ILE   A CG1 
2980 C CG2 A ILE   A 131 ? 0.2265 0.1791 0.1959 0.0082  -0.0386 0.0215  131 ILE   A CG2 
2981 C CG2 B ILE   A 131 ? 0.3578 0.3160 0.3607 0.0022  -0.0266 0.0052  131 ILE   A CG2 
2982 C CD1 A ILE   A 131 ? 0.2144 0.2105 0.2594 -0.0109 -0.0509 0.0010  131 ILE   A CD1 
2983 C CD1 B ILE   A 131 ? 0.3600 0.3198 0.3831 -0.0061 -0.0185 0.0086  131 ILE   A CD1 
3006 N N   A PHE   A 132 ? 0.1926 0.1624 0.1865 -0.0177 -0.0402 0.0374  132 PHE   A N   
3007 N N   B PHE   A 132 ? 0.3131 0.2777 0.2901 0.0208  -0.0661 0.0301  132 PHE   A N   
3008 C CA  A PHE   A 132 ? 0.1915 0.1785 0.1866 -0.0247 -0.0314 0.0173  132 PHE   A CA  
3009 C CA  B PHE   A 132 ? 0.3031 0.2766 0.3044 0.0093  -0.0745 0.0177  132 PHE   A CA  
3010 C C   A PHE   A 132 ? 0.1856 0.1889 0.1910 -0.0218 -0.0329 0.0294  132 PHE   A C   
3011 C C   B PHE   A 132 ? 0.3128 0.2942 0.3157 0.0017  -0.0607 0.0179  132 PHE   A C   
3012 O O   A PHE   A 132 ? 0.1868 0.1930 0.1872 -0.0133 -0.0212 0.0206  132 PHE   A O   
3013 O O   B PHE   A 132 ? 0.3134 0.2893 0.2868 0.0034  -0.0632 0.0079  132 PHE   A O   
3014 C CB  A PHE   A 132 ? 0.1935 0.1752 0.1616 -0.0213 -0.0406 0.0184  132 PHE   A CB  
3015 C CB  B PHE   A 132 ? 0.2884 0.2649 0.3271 0.0129  -0.0918 0.0051  132 PHE   A CB  
3016 C CG  A PHE   A 132 ? 0.1898 0.1717 0.1495 -0.0156 -0.0423 0.0149  132 PHE   A CG  
3017 C CG  B PHE   A 132 ? 0.2806 0.2553 0.3519 0.0120  -0.0936 0.0007  132 PHE   A CG  
3018 C CD1 A PHE   A 132 ? 0.1838 0.1728 0.1591 -0.0067 -0.0440 0.0070  132 PHE   A CD1 
3019 C CD1 B PHE   A 132 ? 0.2845 0.2545 0.3710 0.0092  -0.0835 -0.0048 132 PHE   A CD1 
3020 C CD2 A PHE   A 132 ? 0.1877 0.1684 0.1526 -0.0153 -0.0333 0.0158  132 PHE   A CD2 
3021 C CD2 B PHE   A 132 ? 0.2761 0.2510 0.3575 0.0089  -0.0973 0.0005  132 PHE   A CD2 
3022 C CE1 A PHE   A 132 ? 0.1796 0.1802 0.1571 -0.0121 -0.0463 0.0123  132 PHE   A CE1 
3023 C CE1 B PHE   A 132 ? 0.2825 0.2509 0.3771 0.0075  -0.0800 -0.0073 132 PHE   A CE1 
3024 C CE2 A PHE   A 132 ? 0.1820 0.1720 0.1436 -0.0045 -0.0368 0.0079  132 PHE   A CE2 
3025 C CE2 B PHE   A 132 ? 0.2757 0.2503 0.3661 0.0010  -0.0980 -0.0064 132 PHE   A CE2 
3026 C CZ  A PHE   A 132 ? 0.1796 0.1709 0.1463 -0.0163 -0.0348 0.0082  132 PHE   A CZ  
3027 C CZ  B PHE   A 132 ? 0.2757 0.2493 0.3723 0.0002  -0.0932 -0.0104 132 PHE   A CZ  
3046 N N   A GLY   A 133 ? 0.1805 0.2028 0.2041 -0.0241 -0.0546 0.0530  133 GLY   A N   
3047 N N   B GLY   A 133 ? 0.3179 0.3097 0.3545 -0.0097 -0.0458 0.0225  133 GLY   A N   
3048 C CA  A GLY   A 133 ? 0.1765 0.2197 0.2117 -0.0246 -0.0581 0.0430  133 GLY   A CA  
3049 C CA  B GLY   A 133 ? 0.3256 0.3268 0.3992 -0.0176 -0.0421 0.0259  133 GLY   A CA  
3050 C C   A GLY   A 133 ? 0.1746 0.2259 0.1853 -0.0271 -0.0675 0.0385  133 GLY   A C   
3051 C C   B GLY   A 133 ? 0.3317 0.3428 0.4422 -0.0237 -0.0329 0.0273  133 GLY   A C   
3052 O O   A GLY   A 133 ? 0.1860 0.2438 0.1937 -0.0247 -0.0556 0.0264  133 GLY   A O   
3053 O O   B GLY   A 133 ? 0.3428 0.3563 0.4701 -0.0208 -0.0223 0.0257  133 GLY   A O   
3060 N N   A ALA   A 134 ? 0.1716 0.2092 0.1563 -0.0225 -0.0668 0.0408  134 ALA   A N   
3061 N N   B ALA   A 134 ? 0.3260 0.3397 0.4363 -0.0273 -0.0385 0.0327  134 ALA   A N   
3062 C CA  A ALA   A 134 ? 0.1744 0.2028 0.1822 -0.0178 -0.0461 0.0216  134 ALA   A CA  
3063 C CA  B ALA   A 134 ? 0.3205 0.3310 0.4194 -0.0272 -0.0450 0.0300  134 ALA   A CA  
3064 C C   A ALA   A 134 ? 0.1736 0.2031 0.1886 -0.0228 -0.0471 0.0233  134 ALA   A C   
3065 C C   B ALA   A 134 ? 0.3113 0.3249 0.3882 -0.0254 -0.0578 0.0360  134 ALA   A C   
3066 O O   A ALA   A 134 ? 0.1767 0.1903 0.2323 -0.0187 -0.0326 0.0401  134 ALA   A O   
3067 O O   B ALA   A 134 ? 0.3131 0.3308 0.4026 -0.0248 -0.0566 0.0389  134 ALA   A O   
3068 C CB  A ALA   A 134 ? 0.1792 0.1956 0.1817 -0.0150 -0.0325 0.0106  134 ALA   A CB  
3069 C CB  B ALA   A 134 ? 0.3244 0.3293 0.4260 -0.0277 -0.0392 0.0221  134 ALA   A CB  
3080 N N   A ASP   A 135 ? 0.1763 0.2059 0.1889 -0.0270 -0.0484 0.0220  135 ASP   A N   
3081 N N   B ASP   A 135 ? 0.2988 0.3102 0.3453 -0.0230 -0.0705 0.0452  135 ASP   A N   
3082 C CA  A ASP   A 135 ? 0.1729 0.2138 0.2037 -0.0303 -0.0621 0.0319  135 ASP   A CA  
3083 C CA  B ASP   A 135 ? 0.2856 0.2996 0.3191 -0.0152 -0.0699 0.0523  135 ASP   A CA  
3084 C C   A ASP   A 135 ? 0.1570 0.1949 0.1968 -0.0143 -0.0523 0.0469  135 ASP   A C   
3085 C C   B ASP   A 135 ? 0.2568 0.2743 0.2728 -0.0043 -0.0717 0.0627  135 ASP   A C   
3086 O O   A ASP   A 135 ? 0.1430 0.1781 0.1666 -0.0225 -0.0601 0.0438  135 ASP   A O   
3087 O O   B ASP   A 135 ? 0.2480 0.2580 0.2510 -0.0168 -0.0702 0.0555  135 ASP   A O   
3088 C CB  A ASP   A 135 ? 0.1889 0.2372 0.2448 -0.0461 -0.0735 0.0259  135 ASP   A CB  
3089 C CB  B ASP   A 135 ? 0.3014 0.3130 0.3598 -0.0201 -0.0637 0.0370  135 ASP   A CB  
3090 C CG  A ASP   A 135 ? 0.2071 0.2555 0.2968 -0.0550 -0.0632 0.0264  135 ASP   A CG  
3091 C CG  B ASP   A 135 ? 0.3154 0.3234 0.3989 -0.0199 -0.0572 0.0227  135 ASP   A CG  
3092 O OD1 A ASP   A 135 ? 0.2032 0.2567 0.3113 -0.0553 -0.0724 0.0537  135 ASP   A OD1 
3093 O OD1 B ASP   A 135 ? 0.3230 0.3283 0.4268 -0.0244 -0.0551 0.0181  135 ASP   A OD1 
3094 O OD2 A ASP   A 135 ? 0.2388 0.2721 0.3363 -0.0480 -0.0288 0.0244  135 ASP   A OD2 
3095 O OD2 B ASP   A 135 ? 0.3187 0.3262 0.4122 -0.0171 -0.0571 0.0240  135 ASP   A OD2 
3104 N N   A PRO   A 136 ? 0.1558 0.1952 0.2279 0.0093  -0.0290 0.0495  136 PRO   A N   
3105 N N   B PRO   A 136 ? 0.2407 0.2675 0.2645 0.0180  -0.0521 0.0765  136 PRO   A N   
3106 C CA  A PRO   A 136 ? 0.1449 0.1871 0.2322 0.0097  -0.0189 0.0340  136 PRO   A CA  
3107 C CA  B PRO   A 136 ? 0.2258 0.2541 0.2560 0.0215  -0.0383 0.0601  136 PRO   A CA  
3108 C C   A PRO   A 136 ? 0.1226 0.1786 0.2053 -0.0030 -0.0144 0.0281  136 PRO   A C   
3109 C C   B PRO   A 136 ? 0.2009 0.2417 0.2485 0.0157  -0.0360 0.0419  136 PRO   A C   
3110 O O   A PRO   A 136 ? 0.1074 0.1587 0.1917 -0.0097 0.0044  0.0317  136 PRO   A O   
3111 O O   B PRO   A 136 ? 0.1930 0.2377 0.2239 0.0172  -0.0293 0.0427  136 PRO   A O   
3112 C CB  A PRO   A 136 ? 0.1637 0.1893 0.2491 0.0168  -0.0103 0.0301  136 PRO   A CB  
3113 C CB  B PRO   A 136 ? 0.2400 0.2567 0.2795 0.0268  -0.0254 0.0608  136 PRO   A CB  
3114 C CG  A PRO   A 136 ? 0.1765 0.2014 0.2696 0.0204  -0.0072 0.0331  136 PRO   A CG  
3115 C CG  B PRO   A 136 ? 0.2505 0.2696 0.2989 0.0283  -0.0226 0.0581  136 PRO   A CG  
3116 C CD  A PRO   A 136 ? 0.1711 0.2004 0.2460 0.0202  -0.0048 0.0557  136 PRO   A CD  
3117 C CD  B PRO   A 136 ? 0.2480 0.2704 0.2891 0.0263  -0.0293 0.0770  136 PRO   A CD  
3132 N N   A ILE   A 137 ? 0.1308 0.1988 0.2099 -0.0038 -0.0250 0.0252  137 ILE   A N   
3133 N N   B ILE   A 137 ? 0.1972 0.2441 0.2541 0.0096  -0.0436 0.0366  137 ILE   A N   
3134 C CA  A ILE   A 137 ? 0.1395 0.2198 0.2149 -0.0138 -0.0306 0.0258  137 ILE   A CA  
3135 C CA  B ILE   A 137 ? 0.1985 0.2545 0.2723 0.0022  -0.0473 0.0256  137 ILE   A CA  
3136 C C   A ILE   A 137 ? 0.1398 0.2105 0.1886 -0.0245 -0.0329 0.0358  137 ILE   A C   
3137 C C   B ILE   A 137 ? 0.1847 0.2386 0.2481 -0.0054 -0.0465 0.0135  137 ILE   A C   
3138 O O   A ILE   A 137 ? 0.1465 0.2060 0.1829 -0.0385 -0.0247 0.0428  137 ILE   A O   
3139 O O   B ILE   A 137 ? 0.1823 0.2220 0.2284 -0.0207 -0.0146 -0.0105 137 ILE   A O   
3140 C CB  A ILE   A 137 ? 0.1489 0.2459 0.2504 -0.0168 -0.0523 0.0221  137 ILE   A CB  
3141 C CB  B ILE   A 137 ? 0.2180 0.2820 0.3195 0.0032  -0.0579 0.0244  137 ILE   A CB  
3142 C CG1 A ILE   A 137 ? 0.1591 0.2641 0.2665 -0.0137 -0.0433 0.0292  137 ILE   A CG1 
3143 C CG1 B ILE   A 137 ? 0.2396 0.3016 0.3332 0.0076  -0.0585 0.0231  137 ILE   A CG1 
3144 C CG2 A ILE   A 137 ? 0.1588 0.2535 0.2746 -0.0186 -0.0596 0.0168  137 ILE   A CG2 
3145 C CG2 B ILE   A 137 ? 0.2296 0.2890 0.3399 -0.0001 -0.0583 0.0139  137 ILE   A CG2 
3146 C CD1 A ILE   A 137 ? 0.1749 0.2732 0.2843 -0.0115 -0.0293 0.0241  137 ILE   A CD1 
3147 C CD1 B ILE   A 137 ? 0.2568 0.3120 0.3505 0.0055  -0.0502 0.0175  137 ILE   A CD1 
3170 N N   A HIS   A 138 ? 0.1449 0.2075 0.1883 -0.0196 -0.0178 0.0264  138 HIS   A N   
3171 N N   B HIS   A 138 ? 0.1868 0.2413 0.2438 0.0035  -0.0496 0.0124  138 HIS   A N   
3172 C CA  A HIS   A 138 ? 0.1482 0.1950 0.1829 -0.0161 -0.0080 0.0188  138 HIS   A CA  
3173 C CA  B HIS   A 138 ? 0.1834 0.2345 0.2307 0.0027  -0.0411 0.0182  138 HIS   A CA  
3174 C C   A HIS   A 138 ? 0.1468 0.1713 0.1848 -0.0134 -0.0112 0.0218  138 HIS   A C   
3175 C C   B HIS   A 138 ? 0.1714 0.2135 0.2250 0.0042  -0.0371 0.0295  138 HIS   A C   
3176 O O   A HIS   A 138 ? 0.1474 0.1655 0.1783 -0.0140 -0.0137 0.0059  138 HIS   A O   
3177 O O   B HIS   A 138 ? 0.1706 0.2134 0.2299 0.0071  -0.0338 0.0270  138 HIS   A O   
3178 C CB  A HIS   A 138 ? 0.1622 0.2081 0.1860 -0.0093 -0.0076 0.0057  138 HIS   A CB  
3179 C CB  B HIS   A 138 ? 0.2008 0.2447 0.2403 -0.0019 -0.0480 0.0125  138 HIS   A CB  
3180 C CG  A HIS   A 138 ? 0.1775 0.2186 0.2000 -0.0052 -0.0138 -0.0019 138 HIS   A CG  
3181 C CG  B HIS   A 138 ? 0.2105 0.2458 0.2453 -0.0093 -0.0427 -0.0009 138 HIS   A CG  
3182 N ND1 A HIS   A 138 ? 0.1881 0.2278 0.2152 -0.0038 -0.0139 -0.0150 138 HIS   A ND1 
3183 N ND1 B HIS   A 138 ? 0.2152 0.2510 0.2602 -0.0112 -0.0406 -0.0177 138 HIS   A ND1 
3184 C CD2 A HIS   A 138 ? 0.1816 0.2265 0.2094 0.0023  -0.0138 0.0001  138 HIS   A CD2 
3185 C CD2 B HIS   A 138 ? 0.2160 0.2523 0.2564 -0.0096 -0.0494 -0.0008 138 HIS   A CD2 
3186 C CE1 A HIS   A 138 ? 0.1885 0.2282 0.2251 0.0041  -0.0111 -0.0116 138 HIS   A CE1 
3187 C CE1 B HIS   A 138 ? 0.2177 0.2543 0.2642 -0.0101 -0.0438 -0.0060 138 HIS   A CE1 
3188 N NE2 A HIS   A 138 ? 0.1861 0.2311 0.2170 0.0059  -0.0062 -0.0031 138 HIS   A NE2 
3189 N NE2 B HIS   A 138 ? 0.2163 0.2559 0.2608 -0.0069 -0.0490 -0.0004 138 HIS   A NE2 
3204 N N   A SER   A 139 ? 0.1436 0.1542 0.1948 -0.0105 -0.0095 0.0291  139 SER   A N   
3205 N N   B SER   A 139 ? 0.1550 0.1905 0.2064 0.0037  -0.0271 0.0355  139 SER   A N   
3206 C CA  A SER   A 139 ? 0.1421 0.1482 0.2034 -0.0053 -0.0083 0.0244  139 SER   A CA  
3207 C CA  B SER   A 139 ? 0.1415 0.1745 0.1967 -0.0078 -0.0098 0.0378  139 SER   A CA  
3208 C C   A SER   A 139 ? 0.1320 0.1477 0.2065 -0.0033 -0.0127 0.0170  139 SER   A C   
3209 C C   B SER   A 139 ? 0.1308 0.1536 0.2076 -0.0175 -0.0019 0.0279  139 SER   A C   
3210 O O   A SER   A 139 ? 0.1282 0.1431 0.2114 0.0017  -0.0333 0.0077  139 SER   A O   
3211 O O   B SER   A 139 ? 0.1285 0.1415 0.2087 -0.0222 -0.0102 0.0163  139 SER   A O   
3212 C CB  A SER   A 139 ? 0.1512 0.1449 0.2032 -0.0010 -0.0022 0.0265  139 SER   A CB  
3213 C CB  B SER   A 139 ? 0.1370 0.1713 0.1857 -0.0025 0.0046  0.0350  139 SER   A CB  
3214 O OG  A SER   A 139 ? 0.1571 0.1451 0.2081 0.0014  -0.0065 0.0234  139 SER   A OG  
3215 O OG  B SER   A 139 ? 0.1289 0.1629 0.1654 -0.0001 -0.0051 0.0209  139 SER   A OG  
3226 N N   . LEU   A 140 ? 0.1325 0.1635 0.2093 -0.0072 -0.0084 0.0363  140 LEU   A N   
3227 C CA  . LEU   A 140 ? 0.1258 0.1610 0.2184 -0.0087 -0.0169 0.0382  140 LEU   A CA  
3228 C C   . LEU   A 140 ? 0.1254 0.1657 0.2161 -0.0175 -0.0065 0.0369  140 LEU   A C   
3229 O O   . LEU   A 140 ? 0.1318 0.1661 0.2278 -0.0117 -0.0128 0.0392  140 LEU   A O   
3230 C CB  . LEU   A 140 ? 0.1243 0.1688 0.2245 -0.0087 -0.0125 0.0353  140 LEU   A CB  
3231 C CG  . LEU   A 140 ? 0.1258 0.1785 0.2330 -0.0185 -0.0060 0.0478  140 LEU   A CG  
3232 C CD1 . LEU   A 140 ? 0.1303 0.1748 0.2493 -0.0114 -0.0077 0.0353  140 LEU   A CD1 
3233 C CD2 . LEU   A 140 ? 0.1362 0.1962 0.2581 -0.0126 -0.0046 0.0520  140 LEU   A CD2 
3246 N N   A ARG   A 141 ? 0.1433 0.1720 0.2213 -0.0122 -0.0170 0.0251  141 ARG   A N   
3247 N N   B ARG   A 141 ? 0.1380 0.1719 0.2182 -0.0137 -0.0241 0.0234  141 ARG   A N   
3248 C CA  A ARG   A 141 ? 0.1585 0.1811 0.2389 -0.0162 -0.0256 0.0093  141 ARG   A CA  
3249 C CA  B ARG   A 141 ? 0.1464 0.1815 0.2362 -0.0235 -0.0392 0.0039  141 ARG   A CA  
3250 C C   A ARG   A 141 ? 0.1491 0.1683 0.2198 -0.0136 -0.0195 0.0095  141 ARG   A C   
3251 C C   B ARG   A 141 ? 0.1418 0.1667 0.2183 -0.0180 -0.0234 0.0071  141 ARG   A C   
3252 O O   A ARG   A 141 ? 0.1511 0.1633 0.2246 -0.0142 -0.0068 0.0042  141 ARG   A O   
3253 O O   B ARG   A 141 ? 0.1435 0.1583 0.2278 -0.0212 -0.0003 0.0023  141 ARG   A O   
3254 C CB  A ARG   A 141 ? 0.1861 0.2045 0.2718 -0.0188 -0.0262 -0.0092 141 ARG   A CB  
3255 C CB  B ARG   A 141 ? 0.1672 0.2092 0.2678 -0.0319 -0.0430 -0.0198 141 ARG   A CB  
3256 C CG  A ARG   A 141 ? 0.2200 0.2340 0.3197 -0.0203 -0.0220 -0.0097 141 ARG   A CG  
3257 C CG  B ARG   A 141 ? 0.2035 0.2489 0.3232 -0.0337 -0.0343 -0.0248 141 ARG   A CG  
3258 C CD  A ARG   A 141 ? 0.2483 0.2611 0.3524 -0.0240 -0.0255 -0.0016 141 ARG   A CD  
3259 C CD  B ARG   A 141 ? 0.2316 0.2869 0.3581 -0.0398 -0.0268 -0.0134 141 ARG   A CD  
3260 N NE  A ARG   A 141 ? 0.2601 0.2796 0.3753 -0.0246 -0.0328 0.0043  141 ARG   A NE  
3261 N NE  B ARG   A 141 ? 0.2401 0.3188 0.3783 -0.0430 -0.0248 -0.0072 141 ARG   A NE  
3262 C CZ  A ARG   A 141 ? 0.2685 0.2916 0.3879 -0.0313 -0.0373 0.0074  141 ARG   A CZ  
3263 C CZ  B ARG   A 141 ? 0.2449 0.3369 0.3842 -0.0518 -0.0242 0.0000  141 ARG   A CZ  
3264 N NH1 A ARG   A 141 ? 0.2704 0.2992 0.3946 -0.0336 -0.0365 0.0029  141 ARG   A NH1 
3265 N NH1 B ARG   A 141 ? 0.2449 0.3448 0.3955 -0.0514 -0.0200 -0.0040 141 ARG   A NH1 
3266 N NH2 A ARG   A 141 ? 0.2730 0.2937 0.3953 -0.0302 -0.0439 0.0096  141 ARG   A NH2 
3267 N NH2 B ARG   A 141 ? 0.2484 0.3455 0.3825 -0.0525 -0.0281 -0.0000 141 ARG   A NH2 
3294 N N   . VAL   A 142 ? 0.1398 0.1621 0.2049 -0.0117 -0.0155 0.0104  142 VAL   A N   
3295 C CA  . VAL   A 142 ? 0.1354 0.1633 0.2020 -0.0126 0.0067  0.0095  142 VAL   A CA  
3296 C C   . VAL   A 142 ? 0.1342 0.1556 0.1942 -0.0151 0.0006  0.0195  142 VAL   A C   
3297 O O   . VAL   A 142 ? 0.1368 0.1542 0.2061 -0.0030 0.0026  0.0166  142 VAL   A O   
3298 C CB  . VAL   A 142 ? 0.1513 0.1758 0.1946 -0.0081 0.0024  0.0228  142 VAL   A CB  
3299 C CG1 . VAL   A 142 ? 0.1526 0.1632 0.1905 -0.0118 0.0083  0.0153  142 VAL   A CG1 
3300 C CG2 . VAL   A 142 ? 0.1694 0.1991 0.2278 -0.0048 -0.0002 0.0277  142 VAL   A CG2 
3311 N N   . CYS   A 143 ? 0.1286 0.1484 0.1913 -0.0154 -0.0033 0.0187  143 CYS   A N   
3312 C CA  . CYS   A 143 ? 0.1378 0.1454 0.2010 -0.0063 -0.0025 0.0107  143 CYS   A CA  
3313 C C   . CYS   A 143 ? 0.1369 0.1286 0.2034 -0.0033 -0.0005 0.0269  143 CYS   A C   
3314 O O   . CYS   A 143 ? 0.1344 0.1317 0.2067 -0.0033 -0.0021 0.0225  143 CYS   A O   
3315 C CB  . CYS   A 143 ? 0.1446 0.1417 0.2167 -0.0025 0.0089  0.0216  143 CYS   A CB  
3316 S SG  . CYS   A 143 ? 0.1602 0.1546 0.2034 0.0092  0.0042  0.0113  143 CYS   A SG  
3322 N N   . VAL   A 144 ? 0.1343 0.1396 0.2212 -0.0074 0.0088  0.0222  144 VAL   A N   
3323 C CA  . VAL   A 144 ? 0.1385 0.1518 0.2535 -0.0108 0.0241  0.0335  144 VAL   A CA  
3324 C C   . VAL   A 144 ? 0.1363 0.1468 0.2424 -0.0174 -0.0121 0.0283  144 VAL   A C   
3325 O O   . VAL   A 144 ? 0.1492 0.1561 0.2486 -0.0030 -0.0045 0.0347  144 VAL   A O   
3326 C CB  . VAL   A 144 ? 0.1550 0.1762 0.2805 -0.0008 0.0222  0.0344  144 VAL   A CB  
3327 C CG1 . VAL   A 144 ? 0.1595 0.1983 0.3141 -0.0148 0.0075  0.0384  144 VAL   A CG1 
3328 C CG2 . VAL   A 144 ? 0.1570 0.1866 0.2936 -0.0056 0.0137  0.0382  144 VAL   A CG2 
3338 N N   . ASP   A 145 ? 0.1443 0.1443 0.2569 -0.0149 -0.0011 0.0119  145 ASP   A N   
3339 C CA  . ASP   A 145 ? 0.1512 0.1529 0.2613 -0.0147 -0.0043 0.0031  145 ASP   A CA  
3340 C C   . ASP   A 145 ? 0.1546 0.1411 0.2563 -0.0135 0.0050  -0.0062 145 ASP   A C   
3341 O O   . ASP   A 145 ? 0.1690 0.1543 0.3097 -0.0135 -0.0021 -0.0392 145 ASP   A O   
3342 C CB  . ASP   A 145 ? 0.1730 0.1827 0.2867 -0.0231 -0.0228 0.0039  145 ASP   A CB  
3343 C CG  . ASP   A 145 ? 0.1923 0.2198 0.3335 -0.0391 -0.0256 0.0086  145 ASP   A CG  
3344 O OD1 . ASP   A 145 ? 0.1891 0.2325 0.3524 -0.0600 -0.0136 0.0137  145 ASP   A OD1 
3345 O OD2 . ASP   A 145 ? 0.2106 0.2354 0.3518 -0.0448 -0.0403 0.0018  145 ASP   A OD2 
3350 N N   . THR   A 146 ? 0.1449 0.1309 0.2009 -0.0110 0.0007  0.0028  146 THR   A N   
3351 C CA  . THR   A 146 ? 0.1333 0.1397 0.1931 -0.0042 0.0002  0.0134  146 THR   A CA  
3352 C C   . THR   A 146 ? 0.1290 0.1329 0.1935 -0.0069 0.0025  0.0161  146 THR   A C   
3353 O O   . THR   A 146 ? 0.1363 0.1475 0.2055 -0.0024 -0.0017 0.0147  146 THR   A O   
3354 C CB  . THR   A 146 ? 0.1373 0.1410 0.1870 0.0031  0.0081  0.0156  146 THR   A CB  
3355 O OG1 . THR   A 146 ? 0.1378 0.1543 0.1939 -0.0020 0.0023  0.0039  146 THR   A OG1 
3356 C CG2 . THR   A 146 ? 0.1391 0.1408 0.2146 -0.0069 0.0093  0.0178  146 THR   A CG2 
3364 N N   . VAL   A 147 ? 0.1237 0.1361 0.1901 0.0028  0.0142  0.0170  147 VAL   A N   
3365 C CA  . VAL   A 147 ? 0.1246 0.1427 0.1965 -0.0055 0.0274  0.0181  147 VAL   A CA  
3366 C C   . VAL   A 147 ? 0.1349 0.1385 0.1997 -0.0065 0.0219  0.0326  147 VAL   A C   
3367 O O   . VAL   A 147 ? 0.1373 0.1345 0.2209 -0.0132 0.0196  0.0324  147 VAL   A O   
3368 C CB  . VAL   A 147 ? 0.1392 0.1400 0.1900 -0.0044 0.0221  0.0205  147 VAL   A CB  
3369 C CG1 . VAL   A 147 ? 0.1670 0.1449 0.1894 -0.0043 0.0169  0.0330  147 VAL   A CG1 
3370 C CG2 . VAL   A 147 ? 0.1364 0.1395 0.1964 -0.0093 0.0129  0.0270  147 VAL   A CG2 
3380 N N   . ARG   A 148 ? 0.1367 0.1376 0.2048 -0.0080 0.0182  0.0436  148 ARG   A N   
3381 C CA  . ARG   A 148 ? 0.1442 0.1395 0.2113 -0.0097 0.0206  0.0487  148 ARG   A CA  
3382 C C   . ARG   A 148 ? 0.1531 0.1397 0.1974 -0.0110 0.0200  0.0601  148 ARG   A C   
3383 O O   . ARG   A 148 ? 0.1743 0.1482 0.2108 -0.0103 0.0332  0.0518  148 ARG   A O   
3384 C CB  . ARG   A 148 ? 0.1526 0.1397 0.2376 -0.0057 0.0279  0.0413  148 ARG   A CB  
3385 C CG  . ARG   A 148 ? 0.1591 0.1431 0.2627 -0.0088 0.0442  0.0276  148 ARG   A CG  
3386 C CD  . ARG   A 148 ? 0.1750 0.1398 0.2881 -0.0001 0.0497  0.0472  148 ARG   A CD  
3387 N NE  . ARG   A 148 ? 0.1690 0.1433 0.2946 0.0122  0.0501  0.0572  148 ARG   A NE  
3388 C CZ  . ARG   A 148 ? 0.1650 0.1411 0.2632 0.0115  0.0596  0.0548  148 ARG   A CZ  
3389 N NH1 . ARG   A 148 ? 0.1708 0.1456 0.2705 -0.0033 0.0482  0.0298  148 ARG   A NH1 
3390 N NH2 . ARG   A 148 ? 0.1535 0.1622 0.2777 0.0220  0.0658  0.0566  148 ARG   A NH2 
3404 N N   . THR   A 149 ? 0.1497 0.1428 0.1946 -0.0139 0.0133  0.0542  149 THR   A N   
3405 C CA  . THR   A 149 ? 0.1442 0.1547 0.1926 -0.0114 0.0134  0.0495  149 THR   A CA  
3406 C C   . THR   A 149 ? 0.1364 0.1525 0.1864 -0.0101 0.0157  0.0530  149 THR   A C   
3407 O O   . THR   A 149 ? 0.1383 0.1601 0.2124 -0.0158 0.0113  0.0503  149 THR   A O   
3408 C CB  . THR   A 149 ? 0.1456 0.1700 0.2012 -0.0117 0.0148  0.0391  149 THR   A CB  
3409 O OG1 . THR   A 149 ? 0.1481 0.1491 0.2203 -0.0204 0.0106  0.0431  149 THR   A OG1 
3410 C CG2 . THR   A 149 ? 0.1325 0.1793 0.2125 -0.0035 0.0143  0.0325  149 THR   A CG2 
3418 N N   . ASN   A 150 ? 0.1398 0.1570 0.2017 -0.0080 0.0102  0.0638  150 ASN   A N   
3419 C CA  . ASN   A 150 ? 0.1487 0.1633 0.1868 -0.0059 0.0129  0.0496  150 ASN   A CA  
3420 C C   . ASN   A 150 ? 0.1241 0.1571 0.2029 -0.0089 0.0119  0.0453  150 ASN   A C   
3421 O O   . ASN   A 150 ? 0.1459 0.1602 0.2409 -0.0118 -0.0125 0.0520  150 ASN   A O   
3422 C CB  . ASN   A 150 ? 0.1959 0.1908 0.2030 -0.0104 0.0227  0.0681  150 ASN   A CB  
3423 C CG  . ASN   A 150 ? 0.2533 0.2188 0.2664 -0.0087 0.0106  0.0719  150 ASN   A CG  
3424 O OD1 . ASN   A 150 ? 0.2724 0.2328 0.2908 -0.0247 0.0168  0.0850  150 ASN   A OD1 
3425 N ND2 . ASN   A 150 ? 0.2946 0.2380 0.2991 0.0015  0.0035  0.0723  150 ASN   A ND2 
3432 N N   . VAL   A 151 ? 0.1265 0.1403 0.1996 -0.0173 0.0037  0.0430  151 VAL   A N   
3433 C CA  . VAL   A 151 ? 0.1368 0.1365 0.1867 -0.0123 0.0212  0.0418  151 VAL   A CA  
3434 C C   . VAL   A 151 ? 0.1316 0.1434 0.1926 -0.0156 0.0220  0.0491  151 VAL   A C   
3435 O O   . VAL   A 151 ? 0.1389 0.1487 0.2290 -0.0136 0.0255  0.0415  151 VAL   A O   
3436 C CB  . VAL   A 151 ? 0.1578 0.1590 0.1911 0.0005  0.0219  0.0369  151 VAL   A CB  
3437 C CG1 . VAL   A 151 ? 0.1594 0.1889 0.2152 -0.0085 0.0075  0.0178  151 VAL   A CG1 
3438 C CG2 . VAL   A 151 ? 0.1720 0.1565 0.1941 -0.0042 0.0240  0.0225  151 VAL   A CG2 
3448 N N   . TYR   A 152 ? 0.1286 0.1425 0.1965 -0.0127 0.0117  0.0416  152 TYR   A N   
3449 C CA  . TYR   A 152 ? 0.1231 0.1522 0.1748 -0.0162 0.0077  0.0347  152 TYR   A CA  
3450 C C   . TYR   A 152 ? 0.1167 0.1446 0.1569 -0.0169 0.0138  0.0396  152 TYR   A C   
3451 O O   . TYR   A 152 ? 0.1340 0.1403 0.1596 -0.0216 0.0144  0.0310  152 TYR   A O   
3452 C CB  . TYR   A 152 ? 0.1465 0.1579 0.2002 -0.0201 0.0199  0.0432  152 TYR   A CB  
3453 C CG  . TYR   A 152 ? 0.1613 0.1753 0.1879 -0.0156 0.0297  0.0513  152 TYR   A CG  
3454 C CD1 . TYR   A 152 ? 0.1774 0.2003 0.2055 -0.0004 0.0347  0.0606  152 TYR   A CD1 
3455 C CD2 . TYR   A 152 ? 0.1630 0.1970 0.1826 -0.0233 0.0290  0.0505  152 TYR   A CD2 
3456 C CE1 . TYR   A 152 ? 0.2066 0.2206 0.2174 0.0042  0.0261  0.0753  152 TYR   A CE1 
3457 C CE2 . TYR   A 152 ? 0.1945 0.2171 0.1979 -0.0255 0.0291  0.0562  152 TYR   A CE2 
3458 C CZ  . TYR   A 152 ? 0.2252 0.2173 0.2082 -0.0133 0.0217  0.0901  152 TYR   A CZ  
3459 O OH  . TYR   A 152 ? 0.2654 0.2503 0.2545 -0.0061 0.0198  0.1168  152 TYR   A OH  
3469 N N   . LEU   A 153 ? 0.1228 0.1389 0.1752 -0.0175 0.0111  0.0432  153 LEU   A N   
3470 C CA  . LEU   A 153 ? 0.1193 0.1407 0.1838 -0.0112 0.0179  0.0420  153 LEU   A CA  
3471 C C   . LEU   A 153 ? 0.1238 0.1442 0.1931 -0.0061 0.0322  0.0522  153 LEU   A C   
3472 O O   . LEU   A 153 ? 0.1355 0.1458 0.2295 -0.0057 0.0430  0.0429  153 LEU   A O   
3473 C CB  . LEU   A 153 ? 0.1229 0.1421 0.2061 -0.0108 0.0174  0.0466  153 LEU   A CB  
3474 C CG  . LEU   A 153 ? 0.1311 0.1419 0.1984 -0.0110 0.0135  0.0351  153 LEU   A CG  
3475 C CD1 . LEU   A 153 ? 0.1424 0.1487 0.1884 -0.0106 -0.0000 0.0304  153 LEU   A CD1 
3476 C CD2 . LEU   A 153 ? 0.1334 0.1538 0.2095 -0.0188 0.0255  0.0213  153 LEU   A CD2 
3488 N N   . ALA   A 154 ? 0.1310 0.1353 0.2055 -0.0007 0.0315  0.0533  154 ALA   A N   
3489 C CA  . ALA   A 154 ? 0.1422 0.1359 0.2165 0.0017  0.0290  0.0496  154 ALA   A CA  
3490 C C   . ALA   A 154 ? 0.1372 0.1339 0.2193 0.0023  0.0335  0.0554  154 ALA   A C   
3491 O O   . ALA   A 154 ? 0.1393 0.1501 0.2220 -0.0026 0.0305  0.0585  154 ALA   A O   
3492 C CB  . ALA   A 154 ? 0.1510 0.1435 0.2112 0.0035  0.0286  0.0360  154 ALA   A CB  
3498 N N   A VAL   A 155 ? 0.1441 0.1449 0.2176 0.0078  0.0277  0.0530  155 VAL   A N   
3499 N N   B VAL   A 155 ? 0.1386 0.1417 0.2333 0.0036  0.0387  0.0556  155 VAL   A N   
3500 C CA  A VAL   A 155 ? 0.1511 0.1508 0.2088 0.0084  0.0085  0.0461  155 VAL   A CA  
3501 C CA  B VAL   A 155 ? 0.1419 0.1414 0.2363 -0.0027 0.0314  0.0587  155 VAL   A CA  
3502 C C   A VAL   A 155 ? 0.1590 0.1558 0.1931 0.0156  0.0011  0.0350  155 VAL   A C   
3503 C C   B VAL   A 155 ? 0.1434 0.1458 0.2237 -0.0004 0.0286  0.0502  155 VAL   A C   
3504 O O   A VAL   A 155 ? 0.1602 0.1667 0.2009 0.0252  -0.0025 0.0243  155 VAL   A O   
3505 O O   B VAL   A 155 ? 0.1449 0.1456 0.2446 0.0006  0.0367  0.0598  155 VAL   A O   
3506 C CB  A VAL   A 155 ? 0.1530 0.1512 0.2209 0.0141  -0.0093 0.0406  155 VAL   A CB  
3507 C CB  B VAL   A 155 ? 0.1457 0.1317 0.2566 0.0030  0.0180  0.0498  155 VAL   A CB  
3508 C CG1 A VAL   A 155 ? 0.1665 0.1497 0.2235 0.0120  -0.0246 0.0322  155 VAL   A CG1 
3509 C CG1 B VAL   A 155 ? 0.1526 0.1208 0.2685 0.0047  -0.0012 0.0411  155 VAL   A CG1 
3510 C CG2 A VAL   A 155 ? 0.1506 0.1566 0.2242 0.0210  -0.0231 0.0463  155 VAL   A CG2 
3511 C CG2 B VAL   A 155 ? 0.1589 0.1450 0.2766 0.0101  0.0030  0.0453  155 VAL   A CG2 
3530 N N   A PHE   A 156 ? 0.1628 0.1478 0.1723 0.0172  0.0022  0.0462  156 PHE   A N   
3531 N N   B PHE   A 156 ? 0.1432 0.1454 0.2133 0.0011  0.0305  0.0408  156 PHE   A N   
3532 C CA  A PHE   A 156 ? 0.1863 0.1579 0.1921 0.0238  -0.0067 0.0276  156 PHE   A CA  
3533 C CA  B PHE   A 156 ? 0.1454 0.1493 0.2027 0.0010  0.0174  0.0439  156 PHE   A CA  
3534 C C   A PHE   A 156 ? 0.1758 0.1521 0.1775 0.0273  0.0022  0.0233  156 PHE   A C   
3535 C C   B PHE   A 156 ? 0.1494 0.1574 0.2150 0.0031  0.0203  0.0539  156 PHE   A C   
3536 O O   A PHE   A 156 ? 0.1800 0.1594 0.1684 0.0300  0.0183  0.0174  156 PHE   A O   
3537 O O   B PHE   A 156 ? 0.1608 0.1764 0.2319 -0.0003 0.0162  0.0400  156 PHE   A O   
3538 C CB  A PHE   A 156 ? 0.2171 0.1734 0.2118 0.0264  -0.0174 0.0272  156 PHE   A CB  
3539 C CB  B PHE   A 156 ? 0.1520 0.1377 0.1780 -0.0091 0.0114  0.0433  156 PHE   A CB  
3540 C CG  A PHE   A 156 ? 0.2476 0.1911 0.2470 0.0370  -0.0370 0.0250  156 PHE   A CG  
3541 C CG  B PHE   A 156 ? 0.1598 0.1302 0.1747 -0.0091 -0.0030 0.0479  156 PHE   A CG  
3542 C CD1 A PHE   A 156 ? 0.2650 0.2007 0.2669 0.0456  -0.0333 0.0209  156 PHE   A CD1 
3543 C CD1 B PHE   A 156 ? 0.1684 0.1435 0.1977 -0.0028 0.0024  0.0519  156 PHE   A CD1 
3544 C CD2 A PHE   A 156 ? 0.2664 0.2027 0.2598 0.0401  -0.0468 0.0224  156 PHE   A CD2 
3545 C CD2 B PHE   A 156 ? 0.1849 0.1391 0.1934 -0.0151 -0.0070 0.0432  156 PHE   A CD2 
3546 C CE1 A PHE   A 156 ? 0.2760 0.2057 0.2863 0.0489  -0.0273 0.0136  156 PHE   A CE1 
3547 C CE1 B PHE   A 156 ? 0.1797 0.1516 0.2220 -0.0048 0.0080  0.0456  156 PHE   A CE1 
3548 C CE2 A PHE   A 156 ? 0.2794 0.2091 0.2751 0.0433  -0.0464 0.0148  156 PHE   A CE2 
3549 C CE2 B PHE   A 156 ? 0.1959 0.1408 0.2136 -0.0167 -0.0104 0.0455  156 PHE   A CE2 
3550 C CZ  A PHE   A 156 ? 0.2816 0.2106 0.2871 0.0475  -0.0306 0.0081  156 PHE   A CZ  
3551 C CZ  B PHE   A 156 ? 0.1884 0.1386 0.2306 -0.0184 0.0098  0.0446  156 PHE   A CZ  
3570 N N   A ASP   A 157 ? 0.1706 0.1519 0.1731 0.0260  -0.0050 0.0301  157 ASP   A N   
3571 N N   B ASP   A 157 ? 0.1609 0.1620 0.2309 -0.0069 0.0001  0.0636  157 ASP   A N   
3572 C CA  A ASP   A 157 ? 0.1728 0.1608 0.1957 0.0197  -0.0180 0.0288  157 ASP   A CA  
3573 C CA  B ASP   A 157 ? 0.1696 0.1688 0.2483 -0.0127 -0.0181 0.0497  157 ASP   A CA  
3574 C C   A ASP   A 157 ? 0.1705 0.1654 0.2031 0.0268  -0.0088 0.0376  157 ASP   A C   
3575 C C   B ASP   A 157 ? 0.1563 0.1626 0.2458 -0.0088 -0.0116 0.0555  157 ASP   A C   
3576 O O   A ASP   A 157 ? 0.1721 0.1661 0.2109 0.0273  0.0003  0.0383  157 ASP   A O   
3577 O O   B ASP   A 157 ? 0.1564 0.1560 0.2271 -0.0123 -0.0056 0.0543  157 ASP   A O   
3578 C CB  A ASP   A 157 ? 0.1839 0.1633 0.2194 0.0176  -0.0400 0.0317  157 ASP   A CB  
3579 C CB  B ASP   A 157 ? 0.1924 0.1720 0.2704 -0.0129 -0.0286 0.0484  157 ASP   A CB  
3580 C CG  A ASP   A 157 ? 0.2038 0.1725 0.2596 0.0182  -0.0589 0.0264  157 ASP   A CG  
3581 C CG  B ASP   A 157 ? 0.2180 0.1698 0.2936 -0.0138 -0.0544 0.0387  157 ASP   A CG  
3582 O OD1 A ASP   A 157 ? 0.2305 0.1908 0.3033 0.0096  -0.0844 0.0091  157 ASP   A OD1 
3583 O OD1 B ASP   A 157 ? 0.2497 0.1761 0.3306 -0.0052 -0.0915 0.0307  157 ASP   A OD1 
3584 O OD2 A ASP   A 157 ? 0.1992 0.1619 0.2675 0.0156  -0.0547 0.0273  157 ASP   A OD2 
3585 O OD2 B ASP   A 157 ? 0.2171 0.1747 0.3068 -0.0173 -0.0480 0.0346  157 ASP   A OD2 
3594 N N   A LYS   A 158 ? 0.1700 0.1743 0.2148 0.0300  0.0007  0.0399  158 LYS   A N   
3595 N N   B LYS   A 158 ? 0.1479 0.1684 0.2651 -0.0041 0.0003  0.0437  158 LYS   A N   
3596 C CA  A LYS   A 158 ? 0.1700 0.1921 0.2318 0.0368  0.0046  0.0322  158 LYS   A CA  
3597 C CA  B LYS   A 158 ? 0.1562 0.1910 0.2716 -0.0016 0.0110  0.0288  158 LYS   A CA  
3598 C C   A LYS   A 158 ? 0.1656 0.2033 0.2314 0.0396  0.0015  0.0280  158 LYS   A C   
3599 C C   B LYS   A 158 ? 0.1407 0.1757 0.2646 -0.0003 0.0000  0.0359  158 LYS   A C   
3600 O O   A LYS   A 158 ? 0.1611 0.2081 0.2333 0.0392  0.0076  0.0091  158 LYS   A O   
3601 O O   B LYS   A 158 ? 0.1377 0.1716 0.2739 -0.0135 0.0082  0.0436  158 LYS   A O   
3602 C CB  A LYS   A 158 ? 0.1800 0.1979 0.2435 0.0373  0.0176  0.0278  158 LYS   A CB  
3603 C CB  B LYS   A 158 ? 0.1829 0.2393 0.3080 -0.0001 0.0195  0.0219  158 LYS   A CB  
3604 C CG  A LYS   A 158 ? 0.1974 0.2120 0.2649 0.0294  0.0331  0.0280  158 LYS   A CG  
3605 C CG  B LYS   A 158 ? 0.2142 0.2906 0.3457 0.0015  0.0272  0.0120  158 LYS   A CG  
3606 C CD  A LYS   A 158 ? 0.2119 0.2256 0.2773 0.0243  0.0568  0.0402  158 LYS   A CD  
3607 C CD  B LYS   A 158 ? 0.2448 0.3251 0.3886 0.0014  0.0344  0.0005  158 LYS   A CD  
3608 C CE  A LYS   A 158 ? 0.2023 0.2236 0.2819 0.0199  0.0840  0.0608  158 LYS   A CE  
3609 C CE  B LYS   A 158 ? 0.2653 0.3455 0.4233 -0.0003 0.0384  -0.0035 158 LYS   A CE  
3610 N NZ  A LYS   A 158 ? 0.1905 0.2190 0.2847 0.0110  0.1021  0.0701  158 LYS   A NZ  
3611 N NZ  B LYS   A 158 ? 0.2732 0.3674 0.4435 0.0009  0.0414  -0.0061 158 LYS   A NZ  
3638 N N   A ASN   A 159 ? 0.1683 0.2098 0.2516 0.0407  -0.0134 0.0358  159 ASN   A N   
3639 N N   B ASN   A 159 ? 0.1461 0.1822 0.2725 0.0034  -0.0180 0.0340  159 ASN   A N   
3640 C CA  A ASN   A 159 ? 0.1775 0.2216 0.2673 0.0361  -0.0241 0.0263  159 ASN   A CA  
3641 C CA  B ASN   A 159 ? 0.1633 0.1967 0.2912 0.0016  -0.0267 0.0424  159 ASN   A CA  
3642 C C   A ASN   A 159 ? 0.1664 0.2161 0.2564 0.0266  -0.0137 0.0096  159 ASN   A C   
3643 C C   B ASN   A 159 ? 0.1467 0.1787 0.2851 -0.0060 -0.0220 0.0428  159 ASN   A C   
3644 O O   A ASN   A 159 ? 0.1606 0.2189 0.2482 0.0265  -0.0214 -0.0119 159 ASN   A O   
3645 O O   B ASN   A 159 ? 0.1393 0.1909 0.3048 -0.0121 -0.0264 0.0253  159 ASN   A O   
3646 C CB  A ASN   A 159 ? 0.1944 0.2373 0.3007 0.0430  -0.0397 0.0352  159 ASN   A CB  
3647 C CB  B ASN   A 159 ? 0.2061 0.2319 0.3321 0.0110  -0.0177 0.0528  159 ASN   A CB  
3648 C CG  A ASN   A 159 ? 0.2161 0.2501 0.3415 0.0388  -0.0347 0.0435  159 ASN   A CG  
3649 C CG  B ASN   A 159 ? 0.2576 0.2721 0.3655 0.0001  -0.0045 0.0496  159 ASN   A CG  
3650 O OD1 A ASN   A 159 ? 0.2234 0.2577 0.3577 0.0340  -0.0238 0.0529  159 ASN   A OD1 
3651 O OD1 B ASN   A 159 ? 0.2631 0.2918 0.3876 -0.0031 -0.0128 0.0417  159 ASN   A OD1 
3652 N ND2 A ASN   A 159 ? 0.2255 0.2558 0.3552 0.0310  -0.0369 0.0370  159 ASN   A ND2 
3653 N ND2 B ASN   A 159 ? 0.2832 0.2975 0.3970 -0.0118 0.0067  0.0456  159 ASN   A ND2 
3666 N N   A LEU   A 160 ? 0.1591 0.2033 0.2548 0.0231  -0.0127 0.0156  160 LEU   A N   
3667 N N   B LEU   A 160 ? 0.1442 0.1650 0.2925 -0.0033 -0.0248 0.0490  160 LEU   A N   
3668 C CA  A LEU   A 160 ? 0.1606 0.1969 0.2611 0.0132  0.0029  0.0203  160 LEU   A CA  
3669 C CA  B LEU   A 160 ? 0.1487 0.1572 0.2882 -0.0086 -0.0157 0.0542  160 LEU   A CA  
3670 C C   A LEU   A 160 ? 0.1480 0.1922 0.2649 0.0095  0.0062  0.0227  160 LEU   A C   
3671 C C   B LEU   A 160 ? 0.1491 0.1571 0.2911 -0.0067 -0.0131 0.0467  160 LEU   A C   
3672 O O   A LEU   A 160 ? 0.1484 0.1904 0.2779 0.0116  -0.0069 0.0132  160 LEU   A O   
3673 O O   B LEU   A 160 ? 0.1535 0.1462 0.3073 -0.0149 -0.0122 0.0343  160 LEU   A O   
3674 C CB  A LEU   A 160 ? 0.1735 0.1973 0.2686 0.0034  0.0120  0.0101  160 LEU   A CB  
3675 C CB  B LEU   A 160 ? 0.1614 0.1571 0.2889 -0.0213 -0.0159 0.0633  160 LEU   A CB  
3676 C CG  A LEU   A 160 ? 0.1788 0.1972 0.2813 -0.0015 0.0203  0.0076  160 LEU   A CG  
3677 C CG  B LEU   A 160 ? 0.1708 0.1718 0.2908 -0.0294 -0.0278 0.0541  160 LEU   A CG  
3678 C CD1 A LEU   A 160 ? 0.1819 0.1957 0.2873 -0.0033 0.0235  -0.0036 160 LEU   A CD1 
3679 C CD1 B LEU   A 160 ? 0.1778 0.1837 0.3064 -0.0276 -0.0286 0.0591  160 LEU   A CD1 
3680 C CD2 A LEU   A 160 ? 0.1756 0.1991 0.2810 0.0009  0.0339  0.0039  160 LEU   A CD2 
3681 C CD2 B LEU   A 160 ? 0.1741 0.1759 0.3018 -0.0373 -0.0254 0.0437  160 LEU   A CD2 
3704 N N   A TYR   A 161 ? 0.1419 0.1924 0.2620 0.0069  0.0166  0.0321  161 TYR   A N   
3705 N N   B TYR   A 161 ? 0.1463 0.1607 0.2930 -0.0051 -0.0080 0.0539  161 TYR   A N   
3706 C CA  A TYR   A 161 ? 0.1403 0.1910 0.2706 0.0046  0.0216  0.0477  161 TYR   A CA  
3707 C CA  B TYR   A 161 ? 0.1510 0.1649 0.2979 -0.0029 0.0004  0.0719  161 TYR   A CA  
3708 C C   A TYR   A 161 ? 0.1362 0.2078 0.2973 0.0089  0.0240  0.0546  161 TYR   A C   
3709 C C   B TYR   A 161 ? 0.1413 0.1702 0.3190 -0.0013 -0.0090 0.0664  161 TYR   A C   
3710 O O   A TYR   A 161 ? 0.1288 0.2140 0.2919 0.0103  0.0257  0.0469  161 TYR   A O   
3711 O O   B TYR   A 161 ? 0.1373 0.1651 0.3013 -0.0043 -0.0096 0.0627  161 TYR   A O   
3712 C CB  A TYR   A 161 ? 0.1488 0.1770 0.2773 0.0016  0.0215  0.0534  161 TYR   A CB  
3713 C CB  B TYR   A 161 ? 0.1573 0.1761 0.3025 0.0090  0.0184  0.0774  161 TYR   A CB  
3714 C CG  A TYR   A 161 ? 0.1530 0.1691 0.2820 -0.0065 -0.0013 0.0609  161 TYR   A CG  
3715 C CG  B TYR   A 161 ? 0.1681 0.1871 0.3210 0.0121  0.0081  0.0759  161 TYR   A CG  
3716 C CD1 A TYR   A 161 ? 0.1482 0.1670 0.2949 -0.0122 -0.0237 0.0515  161 TYR   A CD1 
3717 C CD1 B TYR   A 161 ? 0.1658 0.1928 0.3401 0.0167  -0.0041 0.0692  161 TYR   A CD1 
3718 C CD2 A TYR   A 161 ? 0.1613 0.1752 0.2870 -0.0049 -0.0077 0.0802  161 TYR   A CD2 
3719 C CD2 B TYR   A 161 ? 0.1739 0.2007 0.3355 0.0125  0.0098  0.0848  161 TYR   A CD2 
3720 C CE1 A TYR   A 161 ? 0.1577 0.1703 0.3058 -0.0126 -0.0344 0.0632  161 TYR   A CE1 
3721 C CE1 B TYR   A 161 ? 0.1707 0.1956 0.3483 0.0215  -0.0195 0.0790  161 TYR   A CE1 
3722 C CE2 A TYR   A 161 ? 0.1667 0.1745 0.3023 -0.0048 -0.0233 0.0882  161 TYR   A CE2 
3723 C CE2 B TYR   A 161 ? 0.1736 0.1996 0.3454 0.0156  -0.0039 0.0950  161 TYR   A CE2 
3724 C CZ  A TYR   A 161 ? 0.1688 0.1693 0.3085 -0.0055 -0.0397 0.0848  161 TYR   A CZ  
3725 C CZ  B TYR   A 161 ? 0.1795 0.1970 0.3537 0.0201  -0.0107 0.0886  161 TYR   A CZ  
3726 O OH  A TYR   A 161 ? 0.1780 0.1586 0.3195 0.0023  -0.0591 0.0975  161 TYR   A OH  
3727 O OH  B TYR   A 161 ? 0.1912 0.1940 0.3751 0.0207  -0.0043 0.0870  161 TYR   A OH  
3746 N N   A ASP   A 162 ? 0.1349 0.2202 0.3244 0.0129  0.0233  0.0724  162 ASP   A N   
3747 N N   B ASP   A 162 ? 0.1319 0.1829 0.3705 -0.0110 -0.0111 0.0733  162 ASP   A N   
3748 C CA  A ASP   A 162 ? 0.1375 0.2387 0.3313 0.0117  0.0270  0.0815  162 ASP   A CA  
3749 C CA  B ASP   A 162 ? 0.1340 0.2066 0.3948 -0.0204 -0.0130 0.0867  162 ASP   A CA  
3750 C C   A ASP   A 162 ? 0.1433 0.2519 0.3282 0.0093  0.0232  0.0810  162 ASP   A C   
3751 C C   B ASP   A 162 ? 0.1391 0.2089 0.3954 -0.0271 -0.0201 0.0946  162 ASP   A C   
3752 O O   A ASP   A 162 ? 0.1481 0.2530 0.3462 0.0114  0.0275  0.0712  162 ASP   A O   
3753 O O   B ASP   A 162 ? 0.1455 0.1985 0.4186 -0.0370 -0.0203 0.0898  162 ASP   A O   
3754 C CB  A ASP   A 162 ? 0.1403 0.2462 0.3427 0.0208  0.0275  0.0835  162 ASP   A CB  
3755 C CB  B ASP   A 162 ? 0.1492 0.2312 0.4251 -0.0093 -0.0151 0.0870  162 ASP   A CB  
3756 C CG  A ASP   A 162 ? 0.1450 0.2565 0.3484 0.0242  0.0342  0.0878  162 ASP   A CG  
3757 C CG  B ASP   A 162 ? 0.1708 0.2540 0.4475 -0.0042 -0.0096 0.0785  162 ASP   A CG  
3758 O OD1 A ASP   A 162 ? 0.1614 0.2679 0.3680 0.0266  0.0417  0.0674  162 ASP   A OD1 
3759 O OD1 B ASP   A 162 ? 0.1844 0.2648 0.4647 0.0048  -0.0076 0.0718  162 ASP   A OD1 
3760 O OD2 A ASP   A 162 ? 0.1454 0.2519 0.3456 0.0263  0.0475  0.0972  162 ASP   A OD2 
3761 O OD2 B ASP   A 162 ? 0.1911 0.2583 0.4526 -0.0043 0.0014  0.0782  162 ASP   A OD2 
3770 N N   A LYS   A 163 ? 0.1569 0.2674 0.3259 0.0021  0.0087  0.0728  163 LYS   A N   
3771 N N   B LYS   A 163 ? 0.1491 0.2218 0.3871 -0.0304 -0.0551 0.0988  163 LYS   A N   
3772 C CA  A LYS   A 163 ? 0.1733 0.2788 0.3208 -0.0034 0.0019  0.0640  163 LYS   A CA  
3773 C CA  B LYS   A 163 ? 0.1781 0.2306 0.3823 -0.0306 -0.0582 0.0977  163 LYS   A CA  
3774 C C   A LYS   A 163 ? 0.1678 0.2699 0.2963 -0.0136 0.0018  0.0631  163 LYS   A C   
3775 C C   B LYS   A 163 ? 0.1730 0.2109 0.3502 -0.0395 -0.0478 0.0782  163 LYS   A C   
3776 O O   A LYS   A 163 ? 0.1642 0.2728 0.2929 -0.0231 -0.0085 0.0654  163 LYS   A O   
3777 O O   B LYS   A 163 ? 0.1832 0.2098 0.3522 -0.0474 -0.0417 0.0826  163 LYS   A O   
3778 C CB  A LYS   A 163 ? 0.2010 0.2965 0.3495 0.0068  -0.0051 0.0553  163 LYS   A CB  
3779 C CB  B LYS   A 163 ? 0.2121 0.2626 0.4198 -0.0275 -0.0651 0.0905  163 LYS   A CB  
3780 C CG  A LYS   A 163 ? 0.2294 0.3113 0.3811 0.0128  -0.0058 0.0538  163 LYS   A CG  
3781 C CG  B LYS   A 163 ? 0.2520 0.2989 0.4688 -0.0242 -0.0552 0.0884  163 LYS   A CG  
3782 C CD  A LYS   A 163 ? 0.2570 0.3249 0.4142 0.0192  -0.0086 0.0485  163 LYS   A CD  
3783 C CD  B LYS   A 163 ? 0.2870 0.3264 0.5139 -0.0244 -0.0536 0.0865  163 LYS   A CD  
3784 C CE  A LYS   A 163 ? 0.2663 0.3353 0.4479 0.0182  -0.0078 0.0408  163 LYS   A CE  
3785 C CE  B LYS   A 163 ? 0.2907 0.3443 0.5504 -0.0281 -0.0485 0.0848  163 LYS   A CE  
3786 N NZ  A LYS   A 163 ? 0.2792 0.3438 0.4676 0.0140  -0.0075 0.0352  163 LYS   A NZ  
3787 N NZ  B LYS   A 163 ? 0.3052 0.3529 0.5698 -0.0313 -0.0462 0.0824  163 LYS   A NZ  
3814 N N   A LEU   A 164 ? 0.1545 0.2518 0.2738 -0.0179 -0.0007 0.0558  164 LEU   A N   
3815 N N   B LEU   A 164 ? 0.1623 0.1983 0.3212 -0.0306 -0.0502 0.0591  164 LEU   A N   
3816 C CA  A LEU   A 164 ? 0.1483 0.2382 0.2626 -0.0241 0.0047  0.0528  164 LEU   A CA  
3817 C CA  B LEU   A 164 ? 0.1708 0.1967 0.3049 -0.0161 -0.0319 0.0702  164 LEU   A CA  
3818 C C   A LEU   A 164 ? 0.1516 0.2452 0.2632 -0.0233 0.0137  0.0617  164 LEU   A C   
3819 C C   B LEU   A 164 ? 0.1850 0.2007 0.3075 -0.0048 -0.0291 0.0766  164 LEU   A C   
3820 O O   A LEU   A 164 ? 0.1497 0.2468 0.2585 -0.0310 0.0293  0.0478  164 LEU   A O   
3821 O O   B LEU   A 164 ? 0.2024 0.2068 0.3084 0.0125  -0.0214 0.0616  164 LEU   A O   
3822 C CB  A LEU   A 164 ? 0.1432 0.2250 0.2487 -0.0199 0.0052  0.0442  164 LEU   A CB  
3823 C CB  B LEU   A 164 ? 0.1694 0.1967 0.2847 -0.0196 -0.0089 0.0662  164 LEU   A CB  
3824 C CG  A LEU   A 164 ? 0.1485 0.2209 0.2442 -0.0160 -0.0075 0.0289  164 LEU   A CG  
3825 C CG  B LEU   A 164 ? 0.1732 0.2105 0.2703 -0.0181 0.0017  0.0468  164 LEU   A CG  
3826 C CD1 A LEU   A 164 ? 0.1450 0.2221 0.2295 -0.0025 -0.0100 0.0191  164 LEU   A CD1 
3827 C CD1 B LEU   A 164 ? 0.1591 0.2115 0.2546 -0.0140 -0.0068 0.0431  164 LEU   A CD1 
3828 C CD2 A LEU   A 164 ? 0.1524 0.2190 0.2367 -0.0234 -0.0175 0.0253  164 LEU   A CD2 
3829 C CD2 B LEU   A 164 ? 0.1876 0.2227 0.2743 -0.0141 0.0104  0.0429  164 LEU   A CD2 
3852 N N   A VAL   A 165 ? 0.1543 0.2538 0.2710 -0.0182 0.0187  0.0729  165 VAL   A N   
3853 N N   B VAL   A 165 ? 0.1839 0.2131 0.3176 -0.0121 -0.0191 0.0843  165 VAL   A N   
3854 C CA  A VAL   A 165 ? 0.1626 0.2569 0.2675 -0.0183 0.0251  0.0804  165 VAL   A CA  
3855 C CA  B VAL   A 165 ? 0.1933 0.2255 0.3108 -0.0241 0.0023  0.0776  165 VAL   A CA  
3856 C C   A VAL   A 165 ? 0.1526 0.2602 0.2658 -0.0178 0.0342  0.0755  165 VAL   A C   
3857 C C   B VAL   A 165 ? 0.1864 0.2267 0.3086 -0.0370 -0.0096 0.0795  165 VAL   A C   
3858 O O   A VAL   A 165 ? 0.1527 0.2665 0.2686 -0.0182 0.0507  0.0814  165 VAL   A O   
3859 O O   B VAL   A 165 ? 0.1851 0.2247 0.3039 -0.0314 -0.0219 0.0664  165 VAL   A O   
3860 C CB  A VAL   A 165 ? 0.1925 0.2607 0.2882 -0.0174 0.0133  0.0805  165 VAL   A CB  
3861 C CB  B VAL   A 165 ? 0.2170 0.2406 0.3225 -0.0246 0.0205  0.0573  165 VAL   A CB  
3862 C CG1 A VAL   A 165 ? 0.1924 0.2623 0.3030 -0.0180 0.0155  0.0740  165 VAL   A CG1 
3863 C CG1 B VAL   A 165 ? 0.2239 0.2456 0.3266 -0.0270 0.0302  0.0477  165 VAL   A CG1 
3864 C CG2 A VAL   A 165 ? 0.2025 0.2582 0.2889 -0.0109 0.0081  0.0886  165 VAL   A CG2 
3865 C CG2 B VAL   A 165 ? 0.2169 0.2441 0.3258 -0.0094 0.0210  0.0514  165 VAL   A CG2 
3884 N N   A SER   A 166 ? 0.1470 0.2581 0.2700 -0.0162 0.0273  0.0708  166 SER   A N   
3885 N N   B SER   A 166 ? 0.1954 0.2446 0.3294 -0.0464 -0.0206 0.0809  166 SER   A N   
3886 C CA  A SER   A 166 ? 0.1461 0.2592 0.2712 -0.0277 0.0296  0.0573  166 SER   A CA  
3887 C CA  B SER   A 166 ? 0.2098 0.2753 0.3500 -0.0537 -0.0278 0.0678  166 SER   A CA  
3888 C C   A SER   A 166 ? 0.1394 0.2654 0.2738 -0.0348 0.0103  0.0459  166 SER   A C   
3889 C C   B SER   A 166 ? 0.2481 0.3182 0.3574 -0.0548 -0.0205 0.0515  166 SER   A C   
3890 O O   A SER   A 166 ? 0.1546 0.2704 0.2977 -0.0338 0.0051  0.0328  166 SER   A O   
3891 O O   B SER   A 166 ? 0.2513 0.3283 0.3531 -0.0472 -0.0386 0.0477  166 SER   A O   
3892 C CB  A SER   A 166 ? 0.1559 0.2611 0.2778 -0.0236 0.0415  0.0475  166 SER   A CB  
3893 C CB  B SER   A 166 ? 0.1979 0.2693 0.3676 -0.0516 -0.0380 0.0692  166 SER   A CB  
3894 O OG  A SER   A 166 ? 0.1755 0.2656 0.2965 -0.0184 0.0440  0.0389  166 SER   A OG  
3895 O OG  B SER   A 166 ? 0.1958 0.2720 0.3856 -0.0433 -0.0452 0.0731  166 SER   A OG  
3906 N N   A SER   A 167 ? 0.1461 0.2696 0.2565 -0.0237 -0.0089 0.0442  167 SER   A N   
3907 N N   B SER   A 167 ? 0.2918 0.3514 0.3698 -0.0532 0.0091  0.0339  167 SER   A N   
3908 C CA  A SER   A 167 ? 0.1718 0.2719 0.2537 -0.0125 -0.0261 0.0339  167 SER   A CA  
3909 C CA  B SER   A 167 ? 0.3453 0.3887 0.3900 -0.0478 0.0177  0.0176  167 SER   A CA  
3910 C C   A SER   A 167 ? 0.1850 0.2670 0.2495 -0.0007 -0.0193 0.0295  167 SER   A C   
3911 C C   B SER   A 167 ? 0.3925 0.4217 0.4103 -0.0359 0.0233  0.0112  167 SER   A C   
3912 O O   A SER   A 167 ? 0.1893 0.2625 0.2725 0.0055  -0.0348 0.0286  167 SER   A O   
3913 O O   B SER   A 167 ? 0.4016 0.4259 0.4074 -0.0390 0.0259  0.0024  167 SER   A O   
3914 C CB  A SER   A 167 ? 0.1826 0.2745 0.2641 -0.0102 -0.0263 0.0413  167 SER   A CB  
3915 C CB  B SER   A 167 ? 0.3530 0.3959 0.3983 -0.0473 0.0232  0.0127  167 SER   A CB  
3916 O OG  A SER   A 167 ? 0.1782 0.2749 0.2593 -0.0111 -0.0226 0.0555  167 SER   A OG  
3917 O OG  B SER   A 167 ? 0.3592 0.3999 0.4083 -0.0487 0.0255  0.0153  167 SER   A OG  
3928 N N   A PHE   A 168 ? 0.1955 0.2632 0.2333 0.0050  -0.0148 0.0387  168 PHE   A N   
3929 N N   B PHE   A 168 ? 0.4347 0.4493 0.4346 -0.0231 0.0270  0.0098  168 PHE   A N   
3930 C CA  A PHE   A 168 ? 0.2089 0.2627 0.2363 -0.0025 -0.0257 0.0430  168 PHE   A CA  
3931 C CA  B PHE   A 168 ? 0.4772 0.4753 0.4706 -0.0126 0.0276  0.0044  168 PHE   A CA  
3932 C C   A PHE   A 168 ? 0.2379 0.2847 0.3018 -0.0148 -0.0181 0.0369  168 PHE   A C   
3933 C C   B PHE   A 168 ? 0.5089 0.5018 0.5102 -0.0036 0.0189  0.0065  168 PHE   A C   
3934 O O   A PHE   A 168 ? 0.2524 0.2902 0.3387 -0.0126 -0.0163 0.0446  168 PHE   A O   
3935 O O   B PHE   A 168 ? 0.5093 0.5080 0.5013 -0.0007 0.0211  0.0056  168 PHE   A O   
3936 C CB  A PHE   A 168 ? 0.2012 0.2461 0.2062 0.0008  -0.0460 0.0513  168 PHE   A CB  
3937 C CB  B PHE   A 168 ? 0.4865 0.4753 0.4726 -0.0103 0.0354  -0.0051 168 PHE   A CB  
3938 C CG  A PHE   A 168 ? 0.1947 0.2348 0.1876 -0.0064 -0.0448 0.0441  168 PHE   A CG  
3939 C CG  B PHE   A 168 ? 0.4933 0.4761 0.4752 -0.0072 0.0466  -0.0054 168 PHE   A CG  
3940 C CD1 A PHE   A 168 ? 0.1982 0.2380 0.1897 -0.0121 -0.0510 0.0514  168 PHE   A CD1 
3941 C CD1 B PHE   A 168 ? 0.4966 0.4770 0.4749 -0.0063 0.0537  -0.0027 168 PHE   A CD1 
3942 C CD2 A PHE   A 168 ? 0.1788 0.2205 0.1449 -0.0057 -0.0212 0.0384  168 PHE   A CD2 
3943 C CD2 B PHE   A 168 ? 0.4956 0.4753 0.4779 -0.0077 0.0508  -0.0045 168 PHE   A CD2 
3944 C CE1 A PHE   A 168 ? 0.1874 0.2389 0.1832 -0.0190 -0.0492 0.0416  168 PHE   A CE1 
3945 C CE1 B PHE   A 168 ? 0.4982 0.4763 0.4759 -0.0066 0.0563  -0.0047 168 PHE   A CE1 
3946 C CE2 A PHE   A 168 ? 0.1770 0.2163 0.1527 -0.0125 -0.0163 0.0403  168 PHE   A CE2 
3947 C CE2 B PHE   A 168 ? 0.4968 0.4743 0.4800 -0.0086 0.0536  -0.0071 168 PHE   A CE2 
3948 C CZ  A PHE   A 168 ? 0.1822 0.2298 0.1725 -0.0162 -0.0319 0.0320  168 PHE   A CZ  
3949 C CZ  B PHE   A 168 ? 0.4982 0.4753 0.4788 -0.0082 0.0559  -0.0067 168 PHE   A CZ  
3968 N N   A LEU   A 169 ? 0.2587 0.2989 0.3313 -0.0245 -0.0173 0.0211  169 LEU   A N   
3969 N N   B LEU   A 169 ? 0.5393 0.5203 0.5607 0.0008  0.0105  0.0089  169 LEU   A N   
3970 C CA  A LEU   A 169 ? 0.2879 0.3148 0.3667 -0.0263 -0.0188 0.0148  169 LEU   A CA  
3971 C CA  B LEU   A 169 ? 0.5678 0.5395 0.6118 0.0037  0.0001  0.0148  169 LEU   A CA  
3972 C C   A LEU   A 169 ? 0.2993 0.3198 0.3744 -0.0311 -0.0209 0.0263  169 LEU   A C   
3973 C C   B LEU   A 169 ? 0.5789 0.5481 0.6335 0.0047  -0.0166 0.0172  169 LEU   A C   
3974 O O   A LEU   A 169 ? 0.3002 0.3217 0.3747 -0.0361 -0.0155 0.0304  169 LEU   A O   
3975 O O   B LEU   A 169 ? 0.5854 0.5513 0.6446 0.0038  -0.0227 0.0186  169 LEU   A O   
3976 C CB  A LEU   A 169 ? 0.3037 0.3216 0.3981 -0.0255 -0.0188 -0.0040 169 LEU   A CB  
3977 C CB  B LEU   A 169 ? 0.5816 0.5500 0.6382 0.0052  0.0087  0.0181  169 LEU   A CB  
3978 C CG  A LEU   A 169 ? 0.3199 0.3312 0.4285 -0.0258 -0.0142 -0.0194 169 LEU   A CG  
3979 C CG  B LEU   A 169 ? 0.5913 0.5617 0.6572 0.0068  0.0129  0.0190  169 LEU   A CG  
3980 C CD1 A LEU   A 169 ? 0.3259 0.3373 0.4395 -0.0249 -0.0110 -0.0210 169 LEU   A CD1 
3981 C CD1 B LEU   A 169 ? 0.5911 0.5676 0.6686 0.0078  0.0125  0.0174  169 LEU   A CD1 
3982 C CD2 A LEU   A 169 ? 0.3244 0.3319 0.4333 -0.0252 -0.0110 -0.0233 169 LEU   A CD2 
3983 C CD2 B LEU   A 169 ? 0.5976 0.5645 0.6681 0.0063  0.0138  0.0201  169 LEU   A CD2 
3984 O OXT A LEU   A 169 ? 0.3042 0.3215 0.3791 -0.0305 -0.0216 0.0319  169 LEU   A OXT 
3985 O OXT B LEU   A 169 ? 0.5807 0.5519 0.6444 0.0067  -0.0203 0.0179  169 LEU   A OXT 
4008 N N   A SER   B 1   ? 0.3625 0.3618 0.3604 -0.0940 -0.0883 0.0410  1   SER   B N   
4009 N N   B SER   B 1   ? 0.3347 0.3362 0.3564 -0.1361 -0.0709 0.0396  1   SER   B N   
4010 C CA  A SER   B 1   ? 0.3560 0.3636 0.3541 -0.0954 -0.0964 0.0402  1   SER   B CA  
4011 C CA  B SER   B 1   ? 0.3224 0.3395 0.3437 -0.1391 -0.0844 0.0379  1   SER   B CA  
4012 C C   A SER   B 1   ? 0.3389 0.3614 0.3408 -0.0945 -0.0979 0.0515  1   SER   B C   
4013 C C   B SER   B 1   ? 0.2952 0.3384 0.3149 -0.1365 -0.0974 0.0524  1   SER   B C   
4014 O O   A SER   B 1   ? 0.3424 0.3596 0.3330 -0.0922 -0.0935 0.0487  1   SER   B O   
4015 O O   B SER   B 1   ? 0.3024 0.3406 0.3062 -0.1279 -0.0831 0.0449  1   SER   B O   
4016 C CB  A SER   B 1   ? 0.3641 0.3659 0.3704 -0.0959 -0.0907 0.0264  1   SER   B CB  
4017 C CB  B SER   B 1   ? 0.3347 0.3412 0.3706 -0.1416 -0.0675 0.0161  1   SER   B CB  
4018 O OG  A SER   B 1   ? 0.3740 0.3738 0.4016 -0.0927 -0.0727 0.0180  1   SER   B OG  
4019 O OG  B SER   B 1   ? 0.3484 0.3512 0.4100 -0.1389 -0.0495 -0.0006 1   SER   B OG  
4034 N N   A MET   B 2   ? 0.3219 0.3596 0.3469 -0.0934 -0.0903 0.0779  2   MET   B N   
4035 N N   B MET   B 2   ? 0.2725 0.3340 0.3064 -0.1343 -0.0976 0.0998  2   MET   B N   
4036 C CA  A MET   B 2   ? 0.3065 0.3584 0.3532 -0.0826 -0.0846 0.1001  2   MET   B CA  
4037 C CA  B MET   B 2   ? 0.2647 0.3401 0.3074 -0.1028 -0.1032 0.1293  2   MET   B CA  
4038 C C   A MET   B 2   ? 0.2713 0.3366 0.3243 -0.0798 -0.0926 0.1322  2   MET   B C   
4039 C C   B MET   B 2   ? 0.2498 0.3287 0.3019 -0.0863 -0.1061 0.1491  2   MET   B C   
4040 O O   A MET   B 2   ? 0.2706 0.3450 0.3305 -0.0689 -0.0997 0.1275  2   MET   B O   
4041 O O   B MET   B 2   ? 0.2471 0.3388 0.3085 -0.0721 -0.1225 0.1430  2   MET   B O   
4042 C CB  A MET   B 2   ? 0.3290 0.3822 0.4183 -0.0680 -0.0653 0.0791  2   MET   B CB  
4043 C CB  B MET   B 2   ? 0.2838 0.3699 0.3635 -0.0720 -0.0923 0.1141  2   MET   B CB  
4044 C CG  A MET   B 2   ? 0.3470 0.3990 0.4892 -0.0545 -0.0450 0.0659  2   MET   B CG  
4045 C CG  B MET   B 2   ? 0.3008 0.3922 0.4004 -0.0417 -0.0862 0.1179  2   MET   B CG  
4046 S SD  A MET   B 2   ? 0.3633 0.4116 0.5499 -0.0435 -0.0260 0.0539  2   MET   B SD  
4047 S SD  B MET   B 2   ? 0.3205 0.4130 0.4387 -0.0162 -0.0784 0.1224  2   MET   B SD  
4048 C CE  A MET   B 2   ? 0.3600 0.4083 0.5549 -0.0472 -0.0181 0.0546  2   MET   B CE  
4049 C CE  B MET   B 2   ? 0.3230 0.4145 0.4493 -0.0179 -0.0660 0.1136  2   MET   B CE  
4068 N N   . VAL   B 3   ? 0.2356 0.3060 0.2853 -0.0929 -0.0934 0.1622  3   VAL   B N   
4069 C CA  . VAL   B 3   ? 0.2232 0.2737 0.2952 -0.0863 -0.0852 0.1421  3   VAL   B CA  
4070 C C   . VAL   B 3   ? 0.2041 0.2653 0.2561 -0.0797 -0.0794 0.1216  3   VAL   B C   
4071 O O   . VAL   B 3   ? 0.1980 0.2875 0.2578 -0.0779 -0.0782 0.1380  3   VAL   B O   
4072 C CB  . VAL   B 3   ? 0.2358 0.2641 0.3682 -0.0860 -0.0789 0.1157  3   VAL   B CB  
4073 C CG1 . VAL   B 3   ? 0.2463 0.2525 0.4000 -0.0842 -0.0737 0.1084  3   VAL   B CG1 
4074 C CG2 . VAL   B 3   ? 0.2385 0.2682 0.3831 -0.0866 -0.0568 0.1220  3   VAL   B CG2 
4085 N N   . ASN   B 4   ? 0.1986 0.2343 0.2071 -0.0740 -0.0687 0.0975  4   ASN   B N   
4086 C CA  . ASN   B 4   ? 0.2022 0.2248 0.1601 -0.0635 -0.0588 0.0609  4   ASN   B CA  
4087 C C   . ASN   B 4   ? 0.1995 0.2363 0.1658 -0.0642 -0.0470 0.0479  4   ASN   B C   
4088 O O   . ASN   B 4   ? 0.2028 0.2433 0.1946 -0.0600 -0.0484 0.0242  4   ASN   B O   
4089 C CB  . ASN   B 4   ? 0.2049 0.2090 0.1545 -0.0633 -0.0660 0.0514  4   ASN   B CB  
4090 C CG  . ASN   B 4   ? 0.2047 0.1940 0.1478 -0.0617 -0.0540 0.0382  4   ASN   B CG  
4091 O OD1 . ASN   B 4   ? 0.2007 0.1836 0.1469 -0.0550 -0.0516 0.0351  4   ASN   B OD1 
4092 N ND2 . ASN   B 4   ? 0.2190 0.1935 0.1673 -0.0392 -0.0468 0.0397  4   ASN   B ND2 
4099 N N   . SER   B 5   ? 0.2089 0.2552 0.1575 -0.0645 -0.0274 0.0387  5   SER   B N   
4100 C CA  . SER   B 5   ? 0.2363 0.2901 0.1817 -0.0638 -0.0066 0.0295  5   SER   B CA  
4101 C C   . SER   B 5   ? 0.2616 0.2906 0.2375 -0.0797 0.0156  0.0302  5   SER   B C   
4102 O O   . SER   B 5   ? 0.2754 0.2736 0.3243 -0.0695 0.0482  0.0232  5   SER   B O   
4103 C CB  . SER   B 5   ? 0.2524 0.3172 0.2221 -0.0547 -0.0015 0.0415  5   SER   B CB  
4104 O OG  . SER   B 5   ? 0.2908 0.3536 0.2900 -0.0367 0.0004  0.0479  5   SER   B OG  
4110 N N   . PHE   B 6   ? 0.2824 0.3153 0.2210 -0.0909 0.0350  0.0446  6   PHE   B N   
4111 C CA  . PHE   B 6   ? 0.2965 0.3229 0.1700 -0.1110 0.0347  0.0199  6   PHE   B CA  
4112 C C   . PHE   B 6   ? 0.3441 0.3524 0.2182 -0.1120 0.0603  -0.0112 6   PHE   B C   
4113 O O   . PHE   B 6   ? 0.3555 0.3874 0.2542 -0.0996 0.0391  -0.0251 6   PHE   B O   
4114 C CB  . PHE   B 6   ? 0.2715 0.3054 0.1569 -0.1057 0.0097  0.0240  6   PHE   B CB  
4115 C CG  . PHE   B 6   ? 0.2334 0.2739 0.1552 -0.0988 -0.0090 0.0302  6   PHE   B CG  
4116 C CD1 . PHE   B 6   ? 0.2300 0.2433 0.1313 -0.0896 -0.0194 0.0283  6   PHE   B CD1 
4117 C CD2 . PHE   B 6   ? 0.2008 0.2663 0.1750 -0.0790 -0.0088 0.0562  6   PHE   B CD2 
4118 C CE1 . PHE   B 6   ? 0.2171 0.2219 0.1506 -0.0699 -0.0208 0.0255  6   PHE   B CE1 
4119 C CE2 . PHE   B 6   ? 0.1985 0.2517 0.2031 -0.0587 -0.0015 0.0518  6   PHE   B CE2 
4120 C CZ  . PHE   B 6   ? 0.2026 0.2284 0.1870 -0.0555 -0.0097 0.0385  6   PHE   B CZ  
4130 N N   . SER   B 7   ? 0.3807 0.3377 0.2220 -0.1355 0.0950  -0.0402 7   SER   B N   
4131 C CA  . SER   B 7   ? 0.4189 0.3543 0.2929 -0.1350 0.1165  -0.0568 7   SER   B CA  
4132 C C   . SER   B 7   ? 0.4164 0.3421 0.2908 -0.1398 0.1372  -0.0812 7   SER   B C   
4133 O O   . SER   B 7   ? 0.4323 0.3377 0.3245 -0.1477 0.1447  -0.0789 7   SER   B O   
4134 C CB  . SER   B 7   ? 0.4455 0.3595 0.3423 -0.1298 0.1349  -0.0553 7   SER   B CB  
4135 O OG  . SER   B 7   ? 0.4668 0.3807 0.4083 -0.1242 0.1279  -0.0450 7   SER   B OG  
4141 N N   . GLY   B 8   ? 0.4079 0.3305 0.3059 -0.1200 0.1374  -0.0909 8   GLY   B N   
4142 C CA  . GLY   B 8   ? 0.3895 0.3129 0.3227 -0.1085 0.1432  -0.0878 8   GLY   B CA  
4143 C C   . GLY   B 8   ? 0.3667 0.2818 0.3157 -0.1028 0.1554  -0.0760 8   GLY   B C   
4144 O O   . GLY   B 8   ? 0.3840 0.2886 0.3575 -0.0871 0.1557  -0.0827 8   GLY   B O   
4148 N N   . TYR   B 9   ? 0.3427 0.2540 0.2676 -0.0943 0.1303  -0.0925 9   TYR   B N   
4149 C CA  . TYR   B 9   ? 0.3226 0.2305 0.2424 -0.0741 0.0955  -0.0803 9   TYR   B CA  
4150 C C   . TYR   B 9   ? 0.3185 0.2278 0.2339 -0.0698 0.0563  -0.0685 9   TYR   B C   
4151 O O   . TYR   B 9   ? 0.3275 0.2390 0.2800 -0.0781 0.0590  -0.0448 9   TYR   B O   
4152 C CB  . TYR   B 9   ? 0.3134 0.2032 0.2539 -0.0731 0.0854  -0.0670 9   TYR   B CB  
4153 C CG  . TYR   B 9   ? 0.3064 0.1932 0.2500 -0.0809 0.0780  -0.0569 9   TYR   B CG  
4154 C CD1 . TYR   B 9   ? 0.3102 0.1978 0.2557 -0.0924 0.0818  -0.0576 9   TYR   B CD1 
4155 C CD2 . TYR   B 9   ? 0.2937 0.1852 0.2383 -0.0779 0.0646  -0.0635 9   TYR   B CD2 
4156 C CE1 . TYR   B 9   ? 0.3015 0.2095 0.2424 -0.0908 0.0942  -0.0768 9   TYR   B CE1 
4157 C CE2 . TYR   B 9   ? 0.2923 0.1872 0.2440 -0.0725 0.0773  -0.0548 9   TYR   B CE2 
4158 C CZ  . TYR   B 9   ? 0.2936 0.2024 0.2451 -0.0877 0.0789  -0.0777 9   TYR   B CZ  
4159 O OH  . TYR   B 9   ? 0.2868 0.2202 0.2717 -0.1015 0.0719  -0.0916 9   TYR   B OH  
4169 N N   . LEU   B 10  ? 0.2999 0.2054 0.2052 -0.0765 0.0362  -0.0628 10  LEU   B N   
4170 C CA  . LEU   B 10  ? 0.2981 0.2005 0.1909 -0.0904 0.0024  -0.0531 10  LEU   B CA  
4171 C C   . LEU   B 10  ? 0.2842 0.2041 0.2046 -0.0813 -0.0184 -0.0458 10  LEU   B C   
4172 O O   . LEU   B 10  ? 0.2706 0.2064 0.2047 -0.0667 -0.0122 -0.0361 10  LEU   B O   
4173 C CB  . LEU   B 10  ? 0.3164 0.2039 0.2063 -0.1001 -0.0083 -0.0242 10  LEU   B CB  
4174 C CG  . LEU   B 10  ? 0.3347 0.2168 0.2487 -0.0924 -0.0455 -0.0070 10  LEU   B CG  
4175 C CD1 . LEU   B 10  ? 0.3457 0.2216 0.2652 -0.0818 -0.0524 -0.0104 10  LEU   B CD1 
4176 C CD2 . LEU   B 10  ? 0.3438 0.2340 0.2637 -0.0887 -0.0326 0.0270  10  LEU   B CD2 
4188 N N   . LYS   B 11  ? 0.2985 0.2341 0.2012 -0.0742 -0.0323 -0.0366 11  LYS   B N   
4189 C CA  . LYS   B 11  ? 0.3160 0.2617 0.2365 -0.0652 -0.0424 -0.0331 11  LYS   B CA  
4190 C C   . LYS   B 11  ? 0.2927 0.2375 0.2512 -0.0808 -0.0506 -0.0461 11  LYS   B C   
4191 O O   . LYS   B 11  ? 0.3111 0.2589 0.2764 -0.0953 -0.0532 -0.0671 11  LYS   B O   
4192 C CB  . LYS   B 11  ? 0.3563 0.3131 0.3097 -0.0418 -0.0434 -0.0284 11  LYS   B CB  
4193 C CG  . LYS   B 11  ? 0.3887 0.3452 0.3989 -0.0273 -0.0509 -0.0303 11  LYS   B CG  
4194 C CD  . LYS   B 11  ? 0.4118 0.3660 0.4682 -0.0174 -0.0520 -0.0401 11  LYS   B CD  
4195 C CE  . LYS   B 11  ? 0.4205 0.3802 0.5220 -0.0130 -0.0476 -0.0432 11  LYS   B CE  
4196 N NZ  . LYS   B 11  ? 0.4325 0.3896 0.5530 -0.0094 -0.0431 -0.0377 11  LYS   B NZ  
4210 N N   . LEU   B 12  ? 0.2553 0.2116 0.2470 -0.0721 -0.0523 -0.0367 12  LEU   B N   
4211 C CA  . LEU   B 12  ? 0.2380 0.1847 0.2674 -0.0658 -0.0387 -0.0330 12  LEU   B CA  
4212 C C   . LEU   B 12  ? 0.2278 0.1868 0.2652 -0.0667 -0.0506 -0.0340 12  LEU   B C   
4213 O O   . LEU   B 12  ? 0.2240 0.1945 0.2907 -0.0678 -0.0711 -0.0277 12  LEU   B O   
4214 C CB  . LEU   B 12  ? 0.2392 0.1614 0.2786 -0.0523 -0.0275 -0.0383 12  LEU   B CB  
4215 C CG  . LEU   B 12  ? 0.2409 0.1615 0.2715 -0.0455 -0.0104 -0.0290 12  LEU   B CG  
4216 C CD1 . LEU   B 12  ? 0.2475 0.1621 0.2713 -0.0292 -0.0169 -0.0018 12  LEU   B CD1 
4217 C CD2 . LEU   B 12  ? 0.2466 0.1729 0.2651 -0.0513 -0.0065 -0.0303 12  LEU   B CD2 
4229 N N   . THR   B 13  ? 0.2160 0.1876 0.2686 -0.0651 -0.0502 -0.0386 13  THR   B N   
4230 C CA  . THR   B 13  ? 0.2156 0.1947 0.2569 -0.0584 -0.0633 -0.0256 13  THR   B CA  
4231 C C   . THR   B 13  ? 0.2631 0.2179 0.2723 -0.0749 -0.0823 -0.0202 13  THR   B C   
4232 O O   . THR   B 13  ? 0.2838 0.2202 0.2910 -0.0738 -0.0515 -0.0227 13  THR   B O   
4233 C CB  . THR   B 13  ? 0.1884 0.2000 0.2694 -0.0477 -0.0641 -0.0193 13  THR   B CB  
4234 O OG1 . THR   B 13  ? 0.1815 0.1907 0.2676 -0.0427 -0.0433 -0.0146 13  THR   B OG1 
4235 C CG2 . THR   B 13  ? 0.1954 0.2038 0.2833 -0.0423 -0.0384 -0.0032 13  THR   B CG2 
4243 N N   A ASP   B 14  ? 0.2756 0.2327 0.2833 -0.0822 -0.0994 -0.0080 14  ASP   B N   
4244 N N   B ASP   B 14  ? 0.2795 0.2370 0.2735 -0.0788 -0.1063 -0.0025 14  ASP   B N   
4245 C CA  A ASP   B 14  ? 0.2836 0.2429 0.3127 -0.0863 -0.1099 0.0062  14  ASP   B CA  
4246 C CA  B ASP   B 14  ? 0.2917 0.2508 0.3035 -0.0795 -0.1163 0.0193  14  ASP   B CA  
4247 C C   A ASP   B 14  ? 0.2723 0.2290 0.2706 -0.0862 -0.1045 0.0186  14  ASP   B C   
4248 C C   B ASP   B 14  ? 0.2777 0.2342 0.2638 -0.0842 -0.1096 0.0263  14  ASP   B C   
4249 O O   A ASP   B 14  ? 0.2953 0.2438 0.2771 -0.0856 -0.0933 0.0292  14  ASP   B O   
4250 O O   B ASP   B 14  ? 0.3060 0.2537 0.2760 -0.0827 -0.0975 0.0439  14  ASP   B O   
4251 C CB  A ASP   B 14  ? 0.3001 0.2713 0.3779 -0.0858 -0.1157 0.0024  14  ASP   B CB  
4252 C CB  B ASP   B 14  ? 0.3156 0.2861 0.3668 -0.0718 -0.1161 0.0243  14  ASP   B CB  
4253 C CG  A ASP   B 14  ? 0.3181 0.2958 0.4439 -0.0805 -0.1118 -0.0082 14  ASP   B CG  
4254 C CG  B ASP   B 14  ? 0.3417 0.3185 0.4347 -0.0605 -0.1059 0.0172  14  ASP   B CG  
4255 O OD1 A ASP   B 14  ? 0.3235 0.2956 0.4567 -0.0894 -0.1134 -0.0201 14  ASP   B OD1 
4256 O OD1 B ASP   B 14  ? 0.3523 0.3313 0.4500 -0.0610 -0.0988 0.0111  14  ASP   B OD1 
4257 O OD2 A ASP   B 14  ? 0.3274 0.3144 0.4823 -0.0748 -0.1077 -0.0067 14  ASP   B OD2 
4258 O OD2 B ASP   B 14  ? 0.3530 0.3346 0.4766 -0.0590 -0.1041 0.0169  14  ASP   B OD2 
4267 N N   . ASN   B 15  ? 0.2435 0.2079 0.2416 -0.0726 -0.1036 0.0253  15  ASN   B N   
4268 C CA  . ASN   B 15  ? 0.2016 0.1789 0.2320 -0.0478 -0.0732 0.0112  15  ASN   B CA  
4269 C C   . ASN   B 15  ? 0.1811 0.1613 0.2087 -0.0298 -0.0532 0.0081  15  ASN   B C   
4270 O O   . ASN   B 15  ? 0.1738 0.1494 0.2286 -0.0342 -0.0555 -0.0090 15  ASN   B O   
4271 C CB  . ASN   B 15  ? 0.1895 0.1679 0.2568 -0.0212 -0.0619 0.0091  15  ASN   B CB  
4272 C CG  . ASN   B 15  ? 0.1743 0.1655 0.2644 -0.0290 -0.0385 0.0126  15  ASN   B CG  
4273 O OD1 . ASN   B 15  ? 0.1777 0.2032 0.2829 -0.0511 -0.0389 0.0119  15  ASN   B OD1 
4274 N ND2 . ASN   B 15  ? 0.1684 0.1502 0.2414 -0.0153 -0.0001 -0.0041 15  ASN   B ND2 
4282 N N   . VAL   B 16  ? 0.1783 0.1539 0.2118 -0.0404 -0.0624 -0.0007 16  VAL   B N   
4283 C CA  . VAL   B 16  ? 0.1823 0.1520 0.1971 -0.0345 -0.0405 -0.0185 16  VAL   B CA  
4284 C C   . VAL   B 16  ? 0.1808 0.1678 0.1828 -0.0455 -0.0446 -0.0133 16  VAL   B C   
4285 O O   . VAL   B 16  ? 0.1824 0.1781 0.2081 -0.0397 -0.0370 -0.0258 16  VAL   B O   
4286 C CB  . VAL   B 16  ? 0.1787 0.1531 0.2018 -0.0181 -0.0256 -0.0146 16  VAL   B CB  
4287 C CG1 . VAL   B 16  ? 0.1910 0.1522 0.2057 -0.0047 -0.0180 -0.0230 16  VAL   B CG1 
4288 C CG2 . VAL   B 16  ? 0.1872 0.1517 0.2276 -0.0155 -0.0217 -0.0215 16  VAL   B CG2 
4298 N N   . TYR   B 17  ? 0.1895 0.1709 0.1777 -0.0427 -0.0345 -0.0105 17  TYR   B N   
4299 C CA  . TYR   B 17  ? 0.1977 0.1912 0.1727 -0.0502 -0.0353 0.0014  17  TYR   B CA  
4300 C C   . TYR   B 17  ? 0.1874 0.1640 0.1756 -0.0563 -0.0245 -0.0183 17  TYR   B C   
4301 O O   . TYR   B 17  ? 0.1833 0.1696 0.1693 -0.0439 -0.0279 -0.0323 17  TYR   B O   
4302 C CB  . TYR   B 17  ? 0.2376 0.2401 0.1983 -0.0395 -0.0370 0.0345  17  TYR   B CB  
4303 C CG  . TYR   B 17  ? 0.2689 0.2940 0.2480 -0.0307 -0.0472 0.0421  17  TYR   B CG  
4304 C CD1 . TYR   B 17  ? 0.2862 0.3106 0.2790 -0.0299 -0.0553 0.0590  17  TYR   B CD1 
4305 C CD2 . TYR   B 17  ? 0.2914 0.3274 0.2742 -0.0150 -0.0632 0.0441  17  TYR   B CD2 
4306 C CE1 . TYR   B 17  ? 0.3055 0.3333 0.3048 -0.0186 -0.0706 0.0604  17  TYR   B CE1 
4307 C CE2 . TYR   B 17  ? 0.3072 0.3457 0.2951 0.0016  -0.0825 0.0577  17  TYR   B CE2 
4308 C CZ  . TYR   B 17  ? 0.3211 0.3421 0.3145 -0.0019 -0.0844 0.0602  17  TYR   B CZ  
4309 O OH  . TYR   B 17  ? 0.3398 0.3632 0.3400 0.0081  -0.0860 0.0524  17  TYR   B OH  
4319 N N   . ILE   B 18  ? 0.2043 0.1665 0.1705 -0.0428 -0.0099 -0.0233 18  ILE   B N   
4320 C CA  . ILE   B 18  ? 0.2082 0.1560 0.1764 -0.0468 0.0097  -0.0264 18  ILE   B CA  
4321 C C   . ILE   B 18  ? 0.2194 0.1598 0.1790 -0.0561 0.0086  -0.0386 18  ILE   B C   
4322 O O   . ILE   B 18  ? 0.2363 0.1775 0.1947 -0.0540 0.0167  -0.0446 18  ILE   B O   
4323 C CB  . ILE   B 18  ? 0.2059 0.1636 0.1946 -0.0456 0.0012  -0.0291 18  ILE   B CB  
4324 C CG1 . ILE   B 18  ? 0.2043 0.1657 0.1962 -0.0469 0.0036  -0.0180 18  ILE   B CG1 
4325 C CG2 . ILE   B 18  ? 0.2105 0.1697 0.1995 -0.0469 -0.0120 -0.0325 18  ILE   B CG2 
4326 C CD1 . ILE   B 18  ? 0.2041 0.1944 0.2122 -0.0417 -0.0150 0.0216  18  ILE   B CD1 
4338 N N   . LYS   B 19  ? 0.2186 0.1595 0.1921 -0.0388 0.0415  -0.0488 19  LYS   B N   
4339 C CA  . LYS   B 19  ? 0.2183 0.1720 0.2137 -0.0436 0.0307  -0.0555 19  LYS   B CA  
4340 C C   . LYS   B 19  ? 0.2039 0.1598 0.2338 -0.0327 0.0420  -0.0646 19  LYS   B C   
4341 O O   . LYS   B 19  ? 0.2021 0.1629 0.2154 -0.0263 0.0380  -0.0550 19  LYS   B O   
4342 C CB  . LYS   B 19  ? 0.2375 0.1918 0.2229 -0.0486 0.0393  -0.0501 19  LYS   B CB  
4343 C CG  . LYS   B 19  ? 0.2667 0.2127 0.2488 -0.0562 0.0495  -0.0543 19  LYS   B CG  
4344 C CD  . LYS   B 19  ? 0.3006 0.2447 0.2653 -0.0595 0.0676  -0.0571 19  LYS   B CD  
4345 C CE  . LYS   B 19  ? 0.3318 0.2716 0.2889 -0.0657 0.0606  -0.0550 19  LYS   B CE  
4346 N NZ  . LYS   B 19  ? 0.3635 0.2851 0.2946 -0.0712 0.0633  -0.0456 19  LYS   B NZ  
4360 N N   . ASN   B 20  ? 0.2020 0.1811 0.2758 -0.0319 0.0527  -0.0783 20  ASN   B N   
4361 C CA  . ASN   B 20  ? 0.2026 0.1927 0.2970 -0.0269 0.0609  -0.0909 20  ASN   B CA  
4362 C C   . ASN   B 20  ? 0.2011 0.2168 0.2843 -0.0305 0.0698  -0.1018 20  ASN   B C   
4363 O O   . ASN   B 20  ? 0.2185 0.2505 0.3072 -0.0428 0.0753  -0.0935 20  ASN   B O   
4364 C CB  . ASN   B 20  ? 0.2358 0.1980 0.3254 -0.0070 0.0457  -0.0893 20  ASN   B CB  
4365 C CG  . ASN   B 20  ? 0.2694 0.1951 0.3434 0.0245  0.0418  -0.1091 20  ASN   B CG  
4366 O OD1 . ASN   B 20  ? 0.3101 0.2289 0.3787 0.0414  0.0441  -0.1117 20  ASN   B OD1 
4367 N ND2 . ASN   B 20  ? 0.2590 0.1893 0.3453 0.0282  0.0233  -0.0953 20  ASN   B ND2 
4374 N N   . ALA   B 21  ? 0.1989 0.2073 0.2768 -0.0382 0.0626  -0.0896 21  ALA   B N   
4375 C CA  . ALA   B 21  ? 0.2039 0.2100 0.3056 -0.0452 0.0561  -0.0678 21  ALA   B CA  
4376 C C   . ALA   B 21  ? 0.2030 0.1840 0.2824 -0.0335 0.0619  -0.0520 21  ALA   B C   
4377 O O   . ALA   B 21  ? 0.2122 0.1744 0.2599 -0.0375 0.0584  -0.0496 21  ALA   B O   
4378 C CB  . ALA   B 21  ? 0.2226 0.2413 0.3231 -0.0639 0.0540  -0.0501 21  ALA   B CB  
4384 N N   . ASP   B 22  ? 0.2013 0.1672 0.2730 -0.0322 0.0492  -0.0503 22  ASP   B N   
4385 C CA  . ASP   B 22  ? 0.1961 0.1583 0.2568 -0.0138 0.0350  -0.0381 22  ASP   B CA  
4386 C C   . ASP   B 22  ? 0.1873 0.1499 0.2097 -0.0198 0.0258  -0.0222 22  ASP   B C   
4387 O O   . ASP   B 22  ? 0.1906 0.1614 0.2149 -0.0116 0.0205  -0.0108 22  ASP   B O   
4388 C CB  . ASP   B 22  ? 0.2007 0.1665 0.2862 -0.0068 0.0414  -0.0243 22  ASP   B CB  
4389 C CG  . ASP   B 22  ? 0.2000 0.1822 0.3324 0.0011  0.0144  -0.0194 22  ASP   B CG  
4390 O OD1 . ASP   B 22  ? 0.2090 0.1753 0.3345 0.0049  -0.0099 -0.0132 22  ASP   B OD1 
4391 O OD2 . ASP   B 22  ? 0.2115 0.2082 0.3927 0.0093  -0.0109 -0.0236 22  ASP   B OD2 
4396 N N   . ILE   B 23  ? 0.1855 0.1520 0.1842 -0.0096 0.0083  0.0094  23  ILE   B N   
4397 C CA  . ILE   B 23  ? 0.1713 0.1451 0.1639 -0.0165 0.0011  0.0042  23  ILE   B CA  
4398 C C   . ILE   B 23  ? 0.1641 0.1556 0.1554 -0.0097 -0.0103 0.0084  23  ILE   B C   
4399 O O   . ILE   B 23  ? 0.1541 0.1574 0.1462 -0.0144 -0.0089 0.0043  23  ILE   B O   
4400 C CB  . ILE   B 23  ? 0.1688 0.1427 0.1870 -0.0235 -0.0017 0.0151  23  ILE   B CB  
4401 C CG1 . ILE   B 23  ? 0.1687 0.1554 0.1950 -0.0120 0.0077  0.0211  23  ILE   B CG1 
4402 C CG2 . ILE   B 23  ? 0.1777 0.1662 0.2089 -0.0158 0.0021  0.0071  23  ILE   B CG2 
4403 C CD1 . ILE   B 23  ? 0.1758 0.1754 0.2097 -0.0100 0.0120  0.0272  23  ILE   B CD1 
4415 N N   . VAL   B 24  ? 0.1633 0.1505 0.1548 -0.0167 -0.0061 0.0069  24  VAL   B N   
4416 C CA  . VAL   B 24  ? 0.1649 0.1543 0.1871 -0.0112 -0.0176 -0.0071 24  VAL   B CA  
4417 C C   . VAL   B 24  ? 0.1641 0.1586 0.2050 -0.0121 -0.0026 0.0036  24  VAL   B C   
4418 O O   . VAL   B 24  ? 0.1612 0.1723 0.2098 -0.0208 0.0009  0.0086  24  VAL   B O   
4419 C CB  . VAL   B 24  ? 0.1704 0.1725 0.1929 -0.0034 -0.0219 -0.0071 24  VAL   B CB  
4420 C CG1 . VAL   B 24  ? 0.1748 0.1666 0.2296 -0.0101 -0.0309 -0.0063 24  VAL   B CG1 
4421 C CG2 . VAL   B 24  ? 0.1808 0.1993 0.1960 0.0051  -0.0140 -0.0116 24  VAL   B CG2 
4431 N N   . GLU   B 25  ? 0.1894 0.1701 0.2124 -0.0108 0.0123  -0.0032 25  GLU   B N   
4432 C CA  . GLU   B 25  ? 0.2037 0.2002 0.2225 -0.0105 0.0225  -0.0108 25  GLU   B CA  
4433 C C   . GLU   B 25  ? 0.1979 0.1912 0.1843 -0.0227 0.0191  -0.0042 25  GLU   B C   
4434 O O   . GLU   B 25  ? 0.1936 0.2045 0.2038 -0.0209 0.0252  0.0036  25  GLU   B O   
4435 C CB  . GLU   B 25  ? 0.2327 0.2516 0.2895 0.0075  0.0310  -0.0107 25  GLU   B CB  
4436 C CG  . GLU   B 25  ? 0.2673 0.3075 0.3979 0.0107  0.0215  -0.0204 25  GLU   B CG  
4437 C CD  . GLU   B 25  ? 0.3189 0.3481 0.4789 0.0038  0.0145  -0.0240 25  GLU   B CD  
4438 O OE1 . GLU   B 25  ? 0.3216 0.3792 0.5137 0.0051  0.0256  -0.0211 25  GLU   B OE1 
4439 O OE2 . GLU   B 25  ? 0.3147 0.3823 0.5123 0.0031  0.0067  -0.0282 25  GLU   B OE2 
4446 N N   A GLU   B 26  ? 0.1964 0.1789 0.1588 -0.0364 0.0147  -0.0068 26  GLU   B N   
4447 N N   B GLU   B 26  ? 0.1899 0.1791 0.1744 -0.0345 0.0180  -0.0019 26  GLU   B N   
4448 C CA  A GLU   B 26  ? 0.2005 0.1830 0.1686 -0.0442 0.0052  -0.0006 26  GLU   B CA  
4449 C CA  B GLU   B 26  ? 0.1900 0.1926 0.2090 -0.0428 0.0101  0.0135  26  GLU   B CA  
4450 C C   A GLU   B 26  ? 0.1853 0.1789 0.1596 -0.0349 0.0125  0.0090  26  GLU   B C   
4451 C C   B GLU   B 26  ? 0.1792 0.1848 0.1712 -0.0355 0.0222  0.0205  26  GLU   B C   
4452 O O   A GLU   B 26  ? 0.1985 0.1967 0.1702 -0.0303 0.0086  0.0070  26  GLU   B O   
4453 O O   B GLU   B 26  ? 0.1969 0.2099 0.1779 -0.0302 0.0224  0.0203  26  GLU   B O   
4454 C CB  A GLU   B 26  ? 0.2254 0.1919 0.1702 -0.0485 0.0099  0.0086  26  GLU   B CB  
4455 C CB  B GLU   B 26  ? 0.2112 0.2181 0.2516 -0.0437 0.0167  0.0297  26  GLU   B CB  
4456 C CG  A GLU   B 26  ? 0.2555 0.2020 0.1994 -0.0459 0.0165  0.0053  26  GLU   B CG  
4457 C CG  B GLU   B 26  ? 0.2376 0.2479 0.3167 -0.0362 0.0236  0.0264  26  GLU   B CG  
4458 C CD  A GLU   B 26  ? 0.2723 0.1974 0.1975 -0.0541 0.0317  -0.0099 26  GLU   B CD  
4459 C CD  B GLU   B 26  ? 0.2426 0.2485 0.3508 -0.0394 0.0291  0.0312  26  GLU   B CD  
4460 O OE1 A GLU   B 26  ? 0.2830 0.1801 0.1684 -0.0502 0.0604  -0.0355 26  GLU   B OE1 
4461 O OE1 B GLU   B 26  ? 0.2462 0.2528 0.3770 -0.0475 0.0645  0.0299  26  GLU   B OE1 
4462 O OE2 A GLU   B 26  ? 0.2775 0.2126 0.2045 -0.0558 0.0315  0.0200  26  GLU   B OE2 
4463 O OE2 B GLU   B 26  ? 0.2406 0.2436 0.3443 -0.0311 0.0233  0.0156  26  GLU   B OE2 
4476 N N   . ALA   B 27  ? 0.1661 0.1682 0.1598 -0.0319 0.0152  0.0140  27  ALA   B N   
4477 C CA  . ALA   B 27  ? 0.1625 0.1634 0.1714 -0.0179 -0.0033 0.0290  27  ALA   B CA  
4478 C C   . ALA   B 27  ? 0.1680 0.1793 0.1909 -0.0165 0.0097  0.0416  27  ALA   B C   
4479 O O   . ALA   B 27  ? 0.1715 0.1876 0.2073 -0.0110 0.0118  0.0521  27  ALA   B O   
4480 C CB  . ALA   B 27  ? 0.1707 0.1523 0.1646 -0.0187 0.0016  0.0215  27  ALA   B CB  
4487 N N   . LYS   B 28  ? 0.1604 0.1965 0.2376 -0.0219 0.0137  0.0611  28  LYS   B N   
4488 C CA  . LYS   B 28  ? 0.1758 0.2332 0.2699 -0.0198 0.0501  0.0905  28  LYS   B CA  
4489 C C   . LYS   B 28  ? 0.2021 0.2482 0.2469 -0.0031 0.0577  0.0836  28  LYS   B C   
4490 O O   . LYS   B 28  ? 0.2259 0.2578 0.2531 -0.0055 0.0623  0.0783  28  LYS   B O   
4491 C CB  . LYS   B 28  ? 0.1957 0.2750 0.3440 -0.0129 0.0659  0.1103  28  LYS   B CB  
4492 C CG  . LYS   B 28  ? 0.2229 0.3212 0.3958 -0.0079 0.0697  0.1321  28  LYS   B CG  
4493 C CD  . LYS   B 28  ? 0.2554 0.3648 0.4681 -0.0021 0.0866  0.1358  28  LYS   B CD  
4494 C CE  . LYS   B 28  ? 0.2865 0.3950 0.5113 0.0152  0.0867  0.1384  28  LYS   B CE  
4495 N NZ  . LYS   B 28  ? 0.3584 0.4554 0.5446 0.0320  0.0898  0.1468  28  LYS   B NZ  
4509 N N   . LYS   B 29  ? 0.2218 0.2730 0.2458 0.0093  0.0554  0.0546  29  LYS   B N   
4510 C CA  . LYS   B 29  ? 0.2696 0.3068 0.2676 0.0064  0.0518  0.0515  29  LYS   B CA  
4511 C C   . LYS   B 29  ? 0.2622 0.3120 0.2300 -0.0008 0.0432  0.0718  29  LYS   B C   
4512 O O   . LYS   B 29  ? 0.2835 0.3399 0.2397 0.0083  0.0528  0.0761  29  LYS   B O   
4513 C CB  . LYS   B 29  ? 0.3237 0.3401 0.3551 0.0120  0.0495  0.0338  29  LYS   B CB  
4514 C CG  . LYS   B 29  ? 0.3676 0.3724 0.4368 0.0110  0.0560  0.0296  29  LYS   B CG  
4515 C CD  . LYS   B 29  ? 0.3990 0.3955 0.5133 0.0097  0.0643  0.0148  29  LYS   B CD  
4516 C CE  . LYS   B 29  ? 0.4053 0.4022 0.5512 0.0071  0.0776  0.0073  29  LYS   B CE  
4517 N NZ  . LYS   B 29  ? 0.4367 0.4108 0.5726 0.0074  0.0873  0.0048  29  LYS   B NZ  
4531 N N   . VAL   B 30  ? 0.2244 0.2934 0.2112 -0.0181 0.0316  0.0807  30  VAL   B N   
4532 C CA  . VAL   B 30  ? 0.2108 0.2835 0.2416 -0.0261 -0.0087 0.0836  30  VAL   B CA  
4533 C C   . VAL   B 30  ? 0.1845 0.2763 0.2220 -0.0193 -0.0141 0.1015  30  VAL   B C   
4534 O O   . VAL   B 30  ? 0.1960 0.2923 0.2345 -0.0098 -0.0038 0.1092  30  VAL   B O   
4535 C CB  . VAL   B 30  ? 0.2236 0.2778 0.3000 -0.0448 -0.0307 0.0792  30  VAL   B CB  
4536 C CG1 . VAL   B 30  ? 0.2333 0.2967 0.3065 -0.0381 -0.0249 0.0670  30  VAL   B CG1 
4537 C CG2 . VAL   B 30  ? 0.2446 0.2670 0.3334 -0.0588 -0.0359 0.0526  30  VAL   B CG2 
4547 N N   . LYS   B 31  ? 0.1768 0.2366 0.2695 -0.0331 -0.0072 0.1112  31  LYS   B N   
4548 C CA  . LYS   B 31  ? 0.1724 0.2314 0.3133 -0.0402 -0.0151 0.1137  31  LYS   B CA  
4549 C C   . LYS   B 31  ? 0.1697 0.1960 0.2651 -0.0431 -0.0303 0.0875  31  LYS   B C   
4550 O O   . LYS   B 31  ? 0.1611 0.2071 0.2697 -0.0341 -0.0188 0.0971  31  LYS   B O   
4551 C CB  . LYS   B 31  ? 0.1921 0.2837 0.3864 -0.0372 0.0147  0.1189  31  LYS   B CB  
4552 C CG  . LYS   B 31  ? 0.2289 0.3311 0.4420 -0.0483 0.0319  0.1290  31  LYS   B CG  
4553 C CD  . LYS   B 31  ? 0.2494 0.3725 0.5037 -0.0458 0.0323  0.1248  31  LYS   B CD  
4554 C CE  . LYS   B 31  ? 0.3137 0.3946 0.5526 -0.0426 0.0253  0.1144  31  LYS   B CE  
4555 N NZ  . LYS   B 31  ? 0.3318 0.4427 0.5709 -0.0307 0.0166  0.0972  31  LYS   B NZ  
4569 N N   . PRO   B 32  ? 0.1775 0.1623 0.2023 -0.0408 -0.0461 0.0564  32  PRO   B N   
4570 C CA  . PRO   B 32  ? 0.1879 0.1623 0.1543 -0.0430 -0.0469 0.0394  32  PRO   B CA  
4571 C C   . PRO   B 32  ? 0.1973 0.1498 0.1598 -0.0459 -0.0593 0.0473  32  PRO   B C   
4572 O O   . PRO   B 32  ? 0.2076 0.1532 0.2002 -0.0443 -0.0757 0.0397  32  PRO   B O   
4573 C CB  . PRO   B 32  ? 0.2120 0.1587 0.1496 -0.0468 -0.0382 0.0190  32  PRO   B CB  
4574 C CG  . PRO   B 32  ? 0.2268 0.1510 0.1654 -0.0392 -0.0568 0.0227  32  PRO   B CG  
4575 C CD  . PRO   B 32  ? 0.2085 0.1514 0.1984 -0.0364 -0.0660 0.0322  32  PRO   B CD  
4583 N N   . THR   B 33  ? 0.2026 0.1425 0.1411 -0.0454 -0.0499 0.0267  33  THR   B N   
4584 C CA  . THR   B 33  ? 0.2163 0.1469 0.1307 -0.0455 -0.0511 0.0345  33  THR   B CA  
4585 C C   . THR   B 33  ? 0.2128 0.1411 0.1380 -0.0464 -0.0516 0.0214  33  THR   B C   
4586 O O   . THR   B 33  ? 0.2365 0.1447 0.1464 -0.0529 -0.0565 0.0196  33  THR   B O   
4587 C CB  . THR   B 33  ? 0.2308 0.1548 0.1457 -0.0283 -0.0640 0.0368  33  THR   B CB  
4588 O OG1 . THR   B 33  ? 0.2084 0.1626 0.1636 -0.0354 -0.0589 0.0419  33  THR   B OG1 
4589 C CG2 . THR   B 33  ? 0.2589 0.1476 0.1860 -0.0157 -0.0661 0.0380  33  THR   B CG2 
4597 N N   . VAL   B 34  ? 0.1873 0.1392 0.1238 -0.0443 -0.0456 0.0200  34  VAL   B N   
4598 C CA  . VAL   B 34  ? 0.1732 0.1384 0.1273 -0.0357 -0.0433 0.0108  34  VAL   B CA  
4599 C C   . VAL   B 34  ? 0.1628 0.1346 0.1055 -0.0331 -0.0241 0.0025  34  VAL   B C   
4600 O O   . VAL   B 34  ? 0.1792 0.1379 0.1008 -0.0299 -0.0332 0.0032  34  VAL   B O   
4601 C CB  . VAL   B 34  ? 0.1815 0.1462 0.1685 -0.0119 -0.0359 0.0091  34  VAL   B CB  
4602 C CG1 . VAL   B 34  ? 0.1766 0.1562 0.1560 -0.0107 -0.0171 0.0022  34  VAL   B CG1 
4603 C CG2 . VAL   B 34  ? 0.1956 0.1464 0.1982 -0.0149 -0.0369 0.0088  34  VAL   B CG2 
4613 N N   . VAL   B 35  ? 0.1541 0.1264 0.1020 -0.0359 -0.0170 0.0101  35  VAL   B N   
4614 C CA  . VAL   B 35  ? 0.1516 0.1203 0.1025 -0.0280 -0.0091 0.0091  35  VAL   B CA  
4615 C C   . VAL   B 35  ? 0.1380 0.1185 0.1105 -0.0190 -0.0163 0.0042  35  VAL   B C   
4616 O O   . VAL   B 35  ? 0.1442 0.1250 0.1097 -0.0213 -0.0024 -0.0033 35  VAL   B O   
4617 C CB  . VAL   B 35  ? 0.1437 0.1456 0.1132 -0.0201 0.0025  0.0029  35  VAL   B CB  
4618 C CG1 . VAL   B 35  ? 0.1441 0.1599 0.1393 -0.0276 0.0050  -0.0060 35  VAL   B CG1 
4619 C CG2 . VAL   B 35  ? 0.1437 0.1369 0.1464 -0.0090 -0.0021 0.0005  35  VAL   B CG2 
4629 N N   . VAL   B 36  ? 0.1364 0.1217 0.1095 -0.0202 -0.0156 0.0194  36  VAL   B N   
4630 C CA  . VAL   B 36  ? 0.1328 0.1166 0.1032 -0.0169 -0.0093 0.0102  36  VAL   B CA  
4631 C C   . VAL   B 36  ? 0.1318 0.1224 0.0947 -0.0089 0.0010  0.0092  36  VAL   B C   
4632 O O   . VAL   B 36  ? 0.1370 0.1256 0.1174 -0.0112 -0.0029 -0.0077 36  VAL   B O   
4633 C CB  . VAL   B 36  ? 0.1341 0.1229 0.1099 -0.0164 -0.0039 0.0111  36  VAL   B CB  
4634 C CG1 . VAL   B 36  ? 0.1267 0.1321 0.1408 -0.0197 -0.0078 0.0063  36  VAL   B CG1 
4635 C CG2 . VAL   B 36  ? 0.1483 0.1309 0.1162 -0.0199 -0.0133 0.0069  36  VAL   B CG2 
4645 N N   . ASN   B 37  ? 0.1352 0.1228 0.0868 -0.0033 -0.0047 0.0108  37  ASN   B N   
4646 C CA  . ASN   B 37  ? 0.1345 0.1242 0.1034 0.0013  -0.0094 0.0045  37  ASN   B CA  
4647 C C   . ASN   B 37  ? 0.1385 0.1330 0.0966 0.0088  -0.0018 0.0040  37  ASN   B C   
4648 O O   . ASN   B 37  ? 0.1451 0.1380 0.1084 -0.0004 0.0047  0.0043  37  ASN   B O   
4649 C CB  . ASN   B 37  ? 0.1268 0.1222 0.1068 -0.0037 -0.0101 0.0023  37  ASN   B CB  
4650 C CG  . ASN   B 37  ? 0.1344 0.1252 0.1215 0.0007  -0.0125 0.0062  37  ASN   B CG  
4651 O OD1 . ASN   B 37  ? 0.1409 0.1313 0.1300 0.0116  -0.0147 0.0005  37  ASN   B OD1 
4652 N ND2 . ASN   B 37  ? 0.1366 0.1252 0.1206 0.0057  -0.0192 0.0066  37  ASN   B ND2 
4659 N N   . ALA   B 38  ? 0.1407 0.1305 0.1074 0.0087  0.0013  0.0101  38  ALA   B N   
4660 C CA  . ALA   B 38  ? 0.1514 0.1299 0.1079 0.0010  0.0059  0.0070  38  ALA   B CA  
4661 C C   . ALA   B 38  ? 0.1419 0.1281 0.1199 0.0012  0.0108  0.0064  38  ALA   B C   
4662 O O   . ALA   B 38  ? 0.1601 0.1353 0.1311 0.0123  -0.0020 0.0112  38  ALA   B O   
4663 C CB  . ALA   B 38  ? 0.1719 0.1433 0.1252 -0.0102 0.0150  0.0060  38  ALA   B CB  
4669 N N   . ALA   B 39  ? 0.1463 0.1305 0.1092 0.0099  0.0041  0.0082  39  ALA   B N   
4670 C CA  . ALA   B 39  ? 0.1547 0.1384 0.1136 0.0118  -0.0013 -0.0017 39  ALA   B CA  
4671 C C   . ALA   B 39  ? 0.1587 0.1423 0.0983 0.0102  -0.0015 -0.0038 39  ALA   B C   
4672 O O   . ALA   B 39  ? 0.1590 0.1478 0.1246 0.0033  -0.0000 0.0036  39  ALA   B O   
4673 C CB  . ALA   B 39  ? 0.1524 0.1379 0.1254 0.0018  0.0026  0.0033  39  ALA   B CB  
4679 N N   . ASN   B 40  ? 0.1569 0.1662 0.1062 0.0019  0.0030  -0.0107 40  ASN   B N   
4680 C CA  . ASN   B 40  ? 0.1726 0.1706 0.1226 0.0042  0.0016  -0.0019 40  ASN   B CA  
4681 C C   . ASN   B 40  ? 0.1725 0.1698 0.1001 0.0094  0.0030  0.0027  40  ASN   B C   
4682 O O   . ASN   B 40  ? 0.1706 0.1565 0.1080 0.0133  -0.0050 -0.0009 40  ASN   B O   
4683 C CB  . ASN   B 40  ? 0.1835 0.1674 0.1483 0.0147  -0.0152 0.0160  40  ASN   B CB  
4684 C CG  . ASN   B 40  ? 0.1913 0.1696 0.1775 0.0103  -0.0273 0.0232  40  ASN   B CG  
4685 O OD1 . ASN   B 40  ? 0.1899 0.1649 0.2634 0.0033  -0.0361 0.0293  40  ASN   B OD1 
4686 N ND2 . ASN   B 40  ? 0.1960 0.1748 0.1804 0.0073  -0.0177 0.0235  40  ASN   B ND2 
4693 N N   . VAL   B 41  ? 0.1741 0.1649 0.1083 0.0192  0.0024  -0.0026 41  VAL   B N   
4694 C CA  . VAL   B 41  ? 0.1846 0.1755 0.1123 0.0161  0.0020  -0.0061 41  VAL   B CA  
4695 C C   . VAL   B 41  ? 0.1830 0.1753 0.1030 0.0251  -0.0051 -0.0102 41  VAL   B C   
4696 O O   . VAL   B 41  ? 0.1821 0.1747 0.1252 0.0240  -0.0134 -0.0163 41  VAL   B O   
4697 C CB  . VAL   B 41  ? 0.2049 0.1857 0.1474 0.0060  0.0171  -0.0156 41  VAL   B CB  
4698 C CG1 . VAL   B 41  ? 0.2084 0.1913 0.1641 -0.0014 0.0252  -0.0232 41  VAL   B CG1 
4699 C CG2 . VAL   B 41  ? 0.2178 0.2000 0.1596 -0.0059 0.0218  -0.0150 41  VAL   B CG2 
4709 N N   . TYR   B 42  ? 0.1927 0.1688 0.1283 0.0218  -0.0205 -0.0049 42  TYR   B N   
4710 C CA  . TYR   B 42  ? 0.2004 0.1779 0.1183 0.0276  -0.0360 -0.0161 42  TYR   B CA  
4711 C C   . TYR   B 42  ? 0.1854 0.1676 0.1205 0.0264  -0.0277 -0.0231 42  TYR   B C   
4712 O O   . TYR   B 42  ? 0.1852 0.1769 0.1609 0.0197  -0.0394 -0.0190 42  TYR   B O   
4713 C CB  . TYR   B 42  ? 0.2246 0.2156 0.1445 0.0188  -0.0451 -0.0041 42  TYR   B CB  
4714 C CG  . TYR   B 42  ? 0.2247 0.2317 0.1361 0.0066  -0.0373 0.0181  42  TYR   B CG  
4715 C CD1 . TYR   B 42  ? 0.2149 0.2267 0.1166 -0.0002 -0.0229 0.0019  42  TYR   B CD1 
4716 C CD2 . TYR   B 42  ? 0.2322 0.2434 0.1715 0.0124  -0.0236 0.0215  42  TYR   B CD2 
4717 C CE1 . TYR   B 42  ? 0.2251 0.2396 0.1145 0.0029  -0.0208 0.0006  42  TYR   B CE1 
4718 C CE2 . TYR   B 42  ? 0.2383 0.2506 0.1517 0.0119  0.0136  0.0352  42  TYR   B CE2 
4719 C CZ  . TYR   B 42  ? 0.2522 0.2579 0.1395 0.0259  0.0089  0.0156  42  TYR   B CZ  
4720 O OH  . TYR   B 42  ? 0.2937 0.2827 0.2037 0.0398  0.0140  0.0228  42  TYR   B OH  
4730 N N   . LEU   B 43  ? 0.1671 0.1544 0.1126 0.0112  -0.0133 -0.0182 43  LEU   B N   
4731 C CA  . LEU   B 43  ? 0.1634 0.1496 0.1123 0.0060  -0.0171 -0.0042 43  LEU   B CA  
4732 C C   . LEU   B 43  ? 0.1713 0.1457 0.1136 0.0045  -0.0215 0.0025  43  LEU   B C   
4733 O O   . LEU   B 43  ? 0.1669 0.1566 0.1423 0.0077  -0.0163 0.0043  43  LEU   B O   
4734 C CB  . LEU   B 43  ? 0.1541 0.1396 0.1397 0.0072  -0.0168 -0.0107 43  LEU   B CB  
4735 C CG  . LEU   B 43  ? 0.1614 0.1397 0.1474 0.0105  -0.0248 -0.0037 43  LEU   B CG  
4736 C CD1 . LEU   B 43  ? 0.1733 0.1497 0.1928 0.0025  -0.0457 -0.0115 43  LEU   B CD1 
4737 C CD2 . LEU   B 43  ? 0.1638 0.1423 0.1341 0.0066  -0.0213 -0.0069 43  LEU   B CD2 
4749 N N   . LYS   B 44  ? 0.1664 0.1441 0.1256 0.0090  -0.0119 -0.0024 44  LYS   B N   
4750 C CA  . LYS   B 44  ? 0.1748 0.1649 0.1186 0.0157  -0.0127 0.0010  44  LYS   B CA  
4751 C C   . LYS   B 44  ? 0.1689 0.1589 0.1175 0.0203  -0.0170 -0.0045 44  LYS   B C   
4752 O O   . LYS   B 44  ? 0.1935 0.1594 0.1580 0.0095  -0.0012 0.0017  44  LYS   B O   
4753 C CB  . LYS   B 44  ? 0.2069 0.1882 0.1375 0.0250  -0.0321 -0.0032 44  LYS   B CB  
4754 C CG  . LYS   B 44  ? 0.2495 0.2267 0.1814 0.0135  -0.0559 0.0100  44  LYS   B CG  
4755 C CD  . LYS   B 44  ? 0.2956 0.2500 0.2688 -0.0123 -0.0664 0.0062  44  LYS   B CD  
4756 C CE  . LYS   B 44  ? 0.3291 0.2813 0.3210 -0.0240 -0.0631 0.0182  44  LYS   B CE  
4757 N NZ  . LYS   B 44  ? 0.3483 0.2898 0.3456 -0.0214 -0.0743 0.0280  44  LYS   B NZ  
4771 N N   . HIS   B 45  ? 0.1677 0.1624 0.1095 0.0200  -0.0138 0.0035  45  HIS   B N   
4772 C CA  . HIS   B 45  ? 0.1671 0.1623 0.1154 0.0150  -0.0151 -0.0082 45  HIS   B CA  
4773 C C   . HIS   B 45  ? 0.1885 0.1739 0.1612 0.0282  -0.0240 -0.0097 45  HIS   B C   
4774 O O   . HIS   B 45  ? 0.1985 0.2080 0.2280 0.0510  0.0028  -0.0036 45  HIS   B O   
4775 C CB  . HIS   B 45  ? 0.1614 0.1646 0.1149 0.0070  -0.0107 -0.0029 45  HIS   B CB  
4776 C CG  . HIS   B 45  ? 0.1589 0.1603 0.1133 -0.0003 -0.0125 0.0009  45  HIS   B CG  
4777 N ND1 . HIS   B 45  ? 0.1617 0.1506 0.1303 0.0102  -0.0213 -0.0088 45  HIS   B ND1 
4778 C CD2 . HIS   B 45  ? 0.1673 0.1559 0.1487 -0.0044 -0.0132 0.0057  45  HIS   B CD2 
4779 C CE1 . HIS   B 45  ? 0.1679 0.1437 0.1262 0.0043  -0.0306 -0.0069 45  HIS   B CE1 
4780 N NE2 . HIS   B 45  ? 0.1742 0.1537 0.1386 0.0051  -0.0260 -0.0075 45  HIS   B NE2 
4788 N N   A GLY   B 46  ? 0.2060 0.1716 0.1980 0.0320  -0.0355 0.0011  46  GLY   B N   
4789 N N   B GLY   B 46  ? 0.2088 0.1696 0.1902 0.0353  -0.0398 0.0109  46  GLY   B N   
4790 C CA  A GLY   B 46  ? 0.2181 0.1813 0.2440 0.0290  -0.0455 -0.0014 46  GLY   B CA  
4791 C CA  B GLY   B 46  ? 0.2232 0.1823 0.2328 0.0326  -0.0549 0.0127  46  GLY   B CA  
4792 C C   A GLY   B 46  ? 0.2192 0.1929 0.2854 0.0307  -0.0458 -0.0033 46  GLY   B C   
4793 C C   B GLY   B 46  ? 0.2250 0.1990 0.2742 0.0363  -0.0526 0.0147  46  GLY   B C   
4794 O O   A GLY   B 46  ? 0.2227 0.2016 0.3552 0.0359  -0.0281 -0.0249 46  GLY   B O   
4795 O O   B GLY   B 46  ? 0.2355 0.2202 0.3348 0.0416  -0.0262 0.0104  46  GLY   B O   
4802 N N   . GLY   B 47  ? 0.2206 0.2026 0.2643 0.0115  -0.0368 -0.0036 47  GLY   B N   
4803 C CA  . GLY   B 47  ? 0.2049 0.1787 0.2150 0.0059  -0.0223 -0.0131 47  GLY   B CA  
4804 C C   . GLY   B 47  ? 0.1864 0.1630 0.1795 0.0009  -0.0005 -0.0034 47  GLY   B C   
4805 O O   . GLY   B 47  ? 0.1910 0.1563 0.1816 0.0060  -0.0042 0.0087  47  GLY   B O   
4810 N N   . GLY   B 48  ? 0.1710 0.1495 0.1822 0.0008  -0.0081 0.0143  48  GLY   B N   
4811 C CA  . GLY   B 48  ? 0.1616 0.1506 0.1786 -0.0049 -0.0004 0.0059  48  GLY   B CA  
4812 C C   . GLY   B 48  ? 0.1557 0.1446 0.1542 -0.0019 0.0053  -0.0002 48  GLY   B C   
4813 O O   . GLY   B 48  ? 0.1510 0.1416 0.1858 0.0040  -0.0079 0.0009  48  GLY   B O   
4817 N N   . VAL   B 49  ? 0.1554 0.1529 0.1517 0.0084  -0.0002 0.0050  49  VAL   B N   
4818 C CA  . VAL   B 49  ? 0.1519 0.1664 0.1332 0.0144  -0.0120 -0.0122 49  VAL   B CA  
4819 C C   . VAL   B 49  ? 0.1477 0.1549 0.1159 0.0146  -0.0057 -0.0022 49  VAL   B C   
4820 O O   . VAL   B 49  ? 0.1531 0.1551 0.1339 0.0109  -0.0008 0.0022  49  VAL   B O   
4821 C CB  . VAL   B 49  ? 0.1581 0.1787 0.1696 0.0032  -0.0303 -0.0139 49  VAL   B CB  
4822 C CG1 . VAL   B 49  ? 0.1552 0.1889 0.1708 0.0123  -0.0374 -0.0030 49  VAL   B CG1 
4823 C CG2 . VAL   B 49  ? 0.1789 0.2012 0.1982 -0.0069 -0.0382 -0.0171 49  VAL   B CG2 
4833 N N   . ALA   B 50  ? 0.1430 0.1440 0.1210 0.0006  -0.0092 0.0046  50  ALA   B N   
4834 C CA  . ALA   B 50  ? 0.1401 0.1329 0.1301 0.0071  -0.0013 0.0069  50  ALA   B CA  
4835 C C   . ALA   B 50  ? 0.1382 0.1473 0.1241 0.0094  0.0011  0.0045  50  ALA   B C   
4836 O O   . ALA   B 50  ? 0.1458 0.1512 0.1188 0.0090  -0.0009 -0.0022 50  ALA   B O   
4837 C CB  . ALA   B 50  ? 0.1514 0.1316 0.1369 0.0009  -0.0083 0.0099  50  ALA   B CB  
4843 N N   . GLY   B 51  ? 0.1420 0.1557 0.1440 0.0206  -0.0177 0.0082  51  GLY   B N   
4844 C CA  . GLY   B 51  ? 0.1483 0.1598 0.1564 0.0184  -0.0206 0.0125  51  GLY   B CA  
4845 C C   . GLY   B 51  ? 0.1456 0.1548 0.1789 0.0221  -0.0207 0.0033  51  GLY   B C   
4846 O O   . GLY   B 51  ? 0.1448 0.1720 0.1843 0.0092  -0.0155 -0.0123 51  GLY   B O   
4850 N N   . ALA   B 52  ? 0.1414 0.1477 0.1552 0.0206  -0.0067 0.0011  52  ALA   B N   
4851 C CA  . ALA   B 52  ? 0.1462 0.1535 0.1601 0.0190  0.0033  -0.0194 52  ALA   B CA  
4852 C C   . ALA   B 52  ? 0.1425 0.1453 0.1379 0.0114  0.0036  -0.0120 52  ALA   B C   
4853 O O   . ALA   B 52  ? 0.1454 0.1606 0.1620 0.0126  -0.0006 -0.0027 52  ALA   B O   
4854 C CB  . ALA   B 52  ? 0.1601 0.1580 0.1628 0.0127  0.0042  -0.0183 52  ALA   B CB  
4860 N N   . LEU   B 53  ? 0.1376 0.1499 0.1342 0.0189  -0.0042 -0.0040 53  LEU   B N   
4861 C CA  . LEU   B 53  ? 0.1411 0.1590 0.1296 0.0164  -0.0048 -0.0079 53  LEU   B CA  
4862 C C   . LEU   B 53  ? 0.1439 0.1525 0.1416 0.0149  0.0009  0.0013  53  LEU   B C   
4863 O O   . LEU   B 53  ? 0.1443 0.1573 0.1623 0.0029  0.0101  0.0055  53  LEU   B O   
4864 C CB  . LEU   B 53  ? 0.1361 0.1589 0.1423 0.0160  -0.0055 0.0079  53  LEU   B CB  
4865 C CG  . LEU   B 53  ? 0.1360 0.1688 0.1431 0.0031  -0.0067 0.0220  53  LEU   B CG  
4866 C CD1 . LEU   B 53  ? 0.1469 0.1927 0.1791 0.0130  -0.0015 0.0048  53  LEU   B CD1 
4867 C CD2 . LEU   B 53  ? 0.1524 0.1981 0.1673 -0.0008 -0.0188 -0.0058 53  LEU   B CD2 
4879 N N   . ASN   B 54  ? 0.1426 0.1392 0.1296 0.0050  -0.0084 0.0021  54  ASN   B N   
4880 C CA  . ASN   B 54  ? 0.1436 0.1603 0.1359 0.0103  -0.0095 0.0001  54  ASN   B CA  
4881 C C   . ASN   B 54  ? 0.1372 0.1590 0.1578 0.0041  -0.0032 -0.0029 54  ASN   B C   
4882 O O   . ASN   B 54  ? 0.1397 0.1625 0.1650 0.0002  0.0066  -0.0132 54  ASN   B O   
4883 C CB  . ASN   B 54  ? 0.1521 0.1744 0.1427 0.0157  0.0034  -0.0061 54  ASN   B CB  
4884 C CG  . ASN   B 54  ? 0.1481 0.1725 0.1471 0.0138  -0.0091 -0.0142 54  ASN   B CG  
4885 O OD1 . ASN   B 54  ? 0.1477 0.1718 0.1628 0.0084  -0.0133 -0.0199 54  ASN   B OD1 
4886 N ND2 . ASN   B 54  ? 0.1633 0.1915 0.1966 0.0017  -0.0286 0.0121  54  ASN   B ND2 
4893 N N   . LYS   B 55  ? 0.1393 0.1587 0.1811 0.0127  0.0041  -0.0053 55  LYS   B N   
4894 C CA  . LYS   B 55  ? 0.1492 0.1715 0.2090 0.0173  0.0056  -0.0099 55  LYS   B CA  
4895 C C   . LYS   B 55  ? 0.1427 0.1717 0.2005 0.0111  0.0084  -0.0067 55  LYS   B C   
4896 O O   . LYS   B 55  ? 0.1399 0.1868 0.2134 0.0094  0.0071  -0.0192 55  LYS   B O   
4897 C CB  . LYS   B 55  ? 0.1632 0.1801 0.2593 0.0349  0.0227  -0.0092 55  LYS   B CB  
4898 C CG  . LYS   B 55  ? 0.2103 0.2128 0.3455 0.0342  0.0316  -0.0003 55  LYS   B CG  
4899 C CD  . LYS   B 55  ? 0.2479 0.2431 0.4176 0.0442  0.0484  0.0134  55  LYS   B CD  
4900 C CE  . LYS   B 55  ? 0.2790 0.2667 0.4864 0.0422  0.0662  0.0189  55  LYS   B CE  
4901 N NZ  . LYS   B 55  ? 0.2964 0.2890 0.5271 0.0364  0.0539  0.0311  55  LYS   B NZ  
4915 N N   . ALA   B 56  ? 0.1426 0.1775 0.1781 0.0119  0.0051  -0.0139 56  ALA   B N   
4916 C CA  . ALA   B 56  ? 0.1553 0.1882 0.1724 0.0031  0.0024  -0.0067 56  ALA   B CA  
4917 C C   . ALA   B 56  ? 0.1552 0.1878 0.1553 0.0036  0.0154  -0.0060 56  ALA   B C   
4918 O O   . ALA   B 56  ? 0.1660 0.1978 0.1756 0.0044  0.0372  -0.0041 56  ALA   B O   
4919 C CB  . ALA   B 56  ? 0.1768 0.2045 0.1794 -0.0149 -0.0031 -0.0128 56  ALA   B CB  
4925 N N   . THR   B 57  ? 0.1520 0.1762 0.1684 0.0017  0.0245  -0.0118 57  THR   B N   
4926 C CA  . THR   B 57  ? 0.1599 0.1704 0.1744 -0.0045 0.0232  -0.0105 57  THR   B CA  
4927 C C   . THR   B 57  ? 0.1601 0.1857 0.1878 -0.0006 0.0264  -0.0128 57  THR   B C   
4928 O O   . THR   B 57  ? 0.1636 0.1904 0.1871 -0.0136 0.0172  -0.0112 57  THR   B O   
4929 C CB  . THR   B 57  ? 0.1642 0.1565 0.1342 -0.0059 0.0189  0.0149  57  THR   B CB  
4930 O OG1 . THR   B 57  ? 0.1575 0.1573 0.1690 -0.0102 0.0140  0.0035  57  THR   B OG1 
4931 C CG2 . THR   B 57  ? 0.1503 0.1667 0.1567 0.0006  0.0307  0.0069  57  THR   B CG2 
4939 N N   . ASN   B 58  ? 0.1453 0.2061 0.2159 -0.0118 0.0194  -0.0310 58  ASN   B N   
4940 C CA  . ASN   B 58  ? 0.1513 0.2339 0.2531 -0.0197 0.0360  -0.0316 58  ASN   B CA  
4941 C C   . ASN   B 58  ? 0.1405 0.2233 0.2061 -0.0079 0.0045  -0.0171 58  ASN   B C   
4942 O O   . ASN   B 58  ? 0.1518 0.2374 0.2219 -0.0051 -0.0012 -0.0235 58  ASN   B O   
4943 C CB  . ASN   B 58  ? 0.1831 0.2700 0.3417 -0.0373 0.0703  -0.0278 58  ASN   B CB  
4944 C CG  . ASN   B 58  ? 0.2862 0.3154 0.4802 -0.0384 0.0722  -0.0015 58  ASN   B CG  
4945 O OD1 . ASN   B 58  ? 0.3369 0.3450 0.5391 -0.0247 0.0583  0.0031  58  ASN   B OD1 
4946 N ND2 . ASN   B 58  ? 0.3866 0.3866 0.5296 -0.0450 0.0831  0.0069  58  ASN   B ND2 
4953 N N   . ASN   B 59  ? 0.1412 0.2077 0.1722 -0.0068 0.0061  -0.0116 59  ASN   B N   
4954 C CA  . ASN   B 59  ? 0.1451 0.2056 0.1734 -0.0078 -0.0110 -0.0034 59  ASN   B CA  
4955 C C   . ASN   B 59  ? 0.1422 0.1940 0.1684 -0.0099 -0.0128 -0.0154 59  ASN   B C   
4956 O O   . ASN   B 59  ? 0.1482 0.1958 0.1722 -0.0094 -0.0117 -0.0103 59  ASN   B O   
4957 C CB  . ASN   B 59  ? 0.1536 0.2288 0.1930 -0.0005 -0.0215 -0.0072 59  ASN   B CB  
4958 C CG  . ASN   B 59  ? 0.1669 0.2434 0.2124 0.0050  -0.0364 -0.0028 59  ASN   B CG  
4959 O OD1 . ASN   B 59  ? 0.1685 0.2437 0.2109 0.0124  -0.0279 0.0168  59  ASN   B OD1 
4960 N ND2 . ASN   B 59  ? 0.1791 0.2513 0.2279 -0.0033 -0.0357 -0.0031 59  ASN   B ND2 
4967 N N   . ALA   B 60  ? 0.1445 0.1844 0.1704 -0.0081 0.0010  -0.0131 60  ALA   B N   
4968 C CA  . ALA   B 60  ? 0.1542 0.1751 0.1729 -0.0197 0.0021  -0.0069 60  ALA   B CA  
4969 C C   . ALA   B 60  ? 0.1536 0.1674 0.1511 -0.0076 -0.0023 -0.0092 60  ALA   B C   
4970 O O   . ALA   B 60  ? 0.1591 0.1600 0.1767 -0.0174 -0.0004 -0.0030 60  ALA   B O   
4971 C CB  . ALA   B 60  ? 0.1717 0.1744 0.2095 -0.0202 0.0145  -0.0027 60  ALA   B CB  
4977 N N   . MET   B 61  ? 0.1388 0.1562 0.1472 -0.0070 -0.0025 -0.0000 61  MET   B N   
4978 C CA  . MET   B 61  ? 0.1385 0.1498 0.1412 -0.0040 -0.0092 0.0027  61  MET   B CA  
4979 C C   . MET   B 61  ? 0.1424 0.1493 0.1387 -0.0092 -0.0078 0.0055  61  MET   B C   
4980 O O   . MET   B 61  ? 0.1473 0.1483 0.1396 -0.0006 -0.0070 -0.0140 61  MET   B O   
4981 C CB  . MET   B 61  ? 0.1416 0.1451 0.1524 -0.0009 -0.0049 -0.0026 61  MET   B CB  
4982 C CG  . MET   B 61  ? 0.1358 0.1476 0.1397 -0.0018 -0.0071 0.0042  61  MET   B CG  
4983 S SD  . MET   B 61  ? 0.1419 0.1511 0.1640 -0.0024 -0.0052 -0.0137 61  MET   B SD  
4984 C CE  . MET   B 61  ? 0.1462 0.1712 0.1903 -0.0019 -0.0070 -0.0244 61  MET   B CE  
4994 N N   . GLN   B 62  ? 0.1513 0.1569 0.1309 -0.0028 -0.0239 0.0067  62  GLN   B N   
4995 C CA  . GLN   B 62  ? 0.1547 0.1586 0.1452 0.0029  -0.0216 -0.0046 62  GLN   B CA  
4996 C C   . GLN   B 62  ? 0.1523 0.1633 0.1437 -0.0022 -0.0250 -0.0116 62  GLN   B C   
4997 O O   . GLN   B 62  ? 0.1665 0.1639 0.1454 0.0046  -0.0237 -0.0161 62  GLN   B O   
4998 C CB  . GLN   B 62  ? 0.1605 0.1619 0.1519 0.0097  -0.0144 0.0079  62  GLN   B CB  
4999 C CG  . GLN   B 62  ? 0.1652 0.1651 0.1533 0.0061  -0.0287 -0.0027 62  GLN   B CG  
5000 C CD  . GLN   B 62  ? 0.1616 0.1606 0.1443 0.0107  -0.0321 0.0012  62  GLN   B CD  
5001 O OE1 . GLN   B 62  ? 0.1627 0.1618 0.1642 0.0077  -0.0296 -0.0135 62  GLN   B OE1 
5002 N NE2 . GLN   B 62  ? 0.1650 0.1685 0.1383 0.0113  -0.0275 -0.0056 62  GLN   B NE2 
5011 N N   . VAL   B 63  ? 0.1423 0.1673 0.1649 -0.0062 -0.0253 -0.0177 63  VAL   B N   
5012 C CA  . VAL   B 63  ? 0.1556 0.1705 0.1861 -0.0124 -0.0265 -0.0143 63  VAL   B CA  
5013 C C   . VAL   B 63  ? 0.1565 0.1550 0.1703 -0.0126 -0.0305 -0.0266 63  VAL   B C   
5014 O O   . VAL   B 63  ? 0.1698 0.1537 0.1828 -0.0119 -0.0451 -0.0163 63  VAL   B O   
5015 C CB  . VAL   B 63  ? 0.1629 0.1866 0.2292 -0.0149 -0.0311 -0.0169 63  VAL   B CB  
5016 C CG1 . VAL   B 63  ? 0.1679 0.1894 0.2356 -0.0157 -0.0156 -0.0213 63  VAL   B CG1 
5017 C CG2 . VAL   B 63  ? 0.1621 0.2095 0.2321 -0.0111 -0.0364 -0.0088 63  VAL   B CG2 
5027 N N   . GLU   B 64  ? 0.1583 0.1533 0.1597 -0.0075 -0.0291 -0.0171 64  GLU   B N   
5028 C CA  . GLU   B 64  ? 0.1555 0.1443 0.1530 -0.0112 -0.0280 -0.0044 64  GLU   B CA  
5029 C C   . GLU   B 64  ? 0.1551 0.1457 0.1386 -0.0032 -0.0266 -0.0183 64  GLU   B C   
5030 O O   . GLU   B 64  ? 0.1684 0.1535 0.1403 -0.0063 -0.0217 -0.0199 64  GLU   B O   
5031 C CB  . GLU   B 64  ? 0.1501 0.1572 0.1512 -0.0156 -0.0219 0.0019  64  GLU   B CB  
5032 C CG  . GLU   B 64  ? 0.1660 0.1540 0.1556 -0.0212 -0.0232 -0.0116 64  GLU   B CG  
5033 C CD  . GLU   B 64  ? 0.1676 0.1693 0.1696 -0.0264 -0.0317 -0.0132 64  GLU   B CD  
5034 O OE1 . GLU   B 64  ? 0.1647 0.1821 0.1775 -0.0285 -0.0210 -0.0357 64  GLU   B OE1 
5035 O OE2 . GLU   B 64  ? 0.1836 0.1839 0.1742 -0.0291 -0.0310 -0.0100 64  GLU   B OE2 
5042 N N   . SER   B 65  ? 0.1610 0.1429 0.1278 -0.0050 -0.0110 -0.0176 65  SER   B N   
5043 C CA  . SER   B 65  ? 0.1618 0.1440 0.1462 0.0047  -0.0153 -0.0147 65  SER   B CA  
5044 C C   . SER   B 65  ? 0.1592 0.1485 0.1305 0.0118  -0.0182 -0.0154 65  SER   B C   
5045 O O   . SER   B 65  ? 0.1642 0.1564 0.1330 0.0057  -0.0128 -0.0196 65  SER   B O   
5046 C CB  . SER   B 65  ? 0.1626 0.1473 0.1499 -0.0002 -0.0154 -0.0085 65  SER   B CB  
5047 O OG  . SER   B 65  ? 0.1606 0.1463 0.1277 -0.0023 -0.0110 -0.0171 65  SER   B OG  
5053 N N   . ASP   B 66  ? 0.1709 0.1583 0.1299 0.0058  -0.0361 -0.0188 66  ASP   B N   
5054 C CA  . ASP   B 66  ? 0.1806 0.1624 0.1288 0.0098  -0.0412 -0.0092 66  ASP   B CA  
5055 C C   . ASP   B 66  ? 0.1795 0.1632 0.1263 0.0006  -0.0267 -0.0178 66  ASP   B C   
5056 O O   . ASP   B 66  ? 0.1839 0.1680 0.1436 0.0071  -0.0300 -0.0251 66  ASP   B O   
5057 C CB  . ASP   B 66  ? 0.1937 0.1746 0.1721 0.0170  -0.0533 -0.0267 66  ASP   B CB  
5058 C CG  . ASP   B 66  ? 0.2162 0.1857 0.1926 0.0241  -0.0621 -0.0120 66  ASP   B CG  
5059 O OD1 . ASP   B 66  ? 0.2459 0.1818 0.1941 0.0209  -0.0553 -0.0023 66  ASP   B OD1 
5060 O OD2 . ASP   B 66  ? 0.2322 0.2065 0.2707 0.0473  -0.0491 -0.0070 66  ASP   B OD2 
5065 N N   . ASP   B 67  ? 0.1767 0.1554 0.1284 -0.0015 -0.0293 -0.0202 67  ASP   B N   
5066 C CA  . ASP   B 67  ? 0.1924 0.1549 0.1534 -0.0110 -0.0275 -0.0097 67  ASP   B CA  
5067 C C   . ASP   B 67  ? 0.1882 0.1603 0.1476 0.0008  -0.0238 -0.0208 67  ASP   B C   
5068 O O   . ASP   B 67  ? 0.1965 0.1717 0.1594 0.0008  -0.0149 -0.0318 67  ASP   B O   
5069 C CB  . ASP   B 67  ? 0.2052 0.1626 0.1831 -0.0182 -0.0459 -0.0253 67  ASP   B CB  
5070 C CG  . ASP   B 67  ? 0.2424 0.1732 0.1882 -0.0057 -0.0720 -0.0261 67  ASP   B CG  
5071 O OD1 . ASP   B 67  ? 0.2685 0.1809 0.1978 0.0006  -0.0598 -0.0192 67  ASP   B OD1 
5072 O OD2 . ASP   B 67  ? 0.2613 0.1748 0.2154 0.0113  -0.0687 -0.0147 67  ASP   B OD2 
5077 N N   . TYR   B 68  ? 0.1762 0.1622 0.1376 0.0089  -0.0343 -0.0250 68  TYR   B N   
5078 C CA  . TYR   B 68  ? 0.1693 0.1773 0.1566 0.0129  -0.0447 -0.0318 68  TYR   B CA  
5079 C C   . TYR   B 68  ? 0.1676 0.1670 0.1663 0.0138  -0.0333 -0.0399 68  TYR   B C   
5080 O O   . TYR   B 68  ? 0.1741 0.1727 0.1760 0.0122  -0.0329 -0.0502 68  TYR   B O   
5081 C CB  . TYR   B 68  ? 0.1768 0.1999 0.1724 0.0119  -0.0558 -0.0489 68  TYR   B CB  
5082 C CG  . TYR   B 68  ? 0.1874 0.2164 0.1835 0.0184  -0.0434 -0.0649 68  TYR   B CG  
5083 C CD1 . TYR   B 68  ? 0.1867 0.2224 0.1970 0.0016  -0.0293 -0.0759 68  TYR   B CD1 
5084 C CD2 . TYR   B 68  ? 0.1976 0.2274 0.1957 0.0214  -0.0585 -0.0591 68  TYR   B CD2 
5085 C CE1 . TYR   B 68  ? 0.1964 0.2371 0.2185 0.0099  -0.0180 -0.0775 68  TYR   B CE1 
5086 C CE2 . TYR   B 68  ? 0.1934 0.2324 0.2145 0.0203  -0.0462 -0.0731 68  TYR   B CE2 
5087 C CZ  . TYR   B 68  ? 0.1871 0.2372 0.2270 0.0183  -0.0310 -0.0681 68  TYR   B CZ  
5088 O OH  . TYR   B 68  ? 0.1796 0.2534 0.2654 0.0191  -0.0197 -0.0322 68  TYR   B OH  
5098 N N   . ILE   B 69  ? 0.1663 0.1512 0.1643 0.0069  -0.0359 -0.0336 69  ILE   B N   
5099 C CA  . ILE   B 69  ? 0.1692 0.1624 0.1649 -0.0023 -0.0131 -0.0350 69  ILE   B CA  
5100 C C   . ILE   B 69  ? 0.1700 0.1584 0.1545 0.0106  -0.0271 -0.0258 69  ILE   B C   
5101 O O   . ILE   B 69  ? 0.1821 0.1702 0.1504 0.0075  -0.0228 -0.0324 69  ILE   B O   
5102 C CB  . ILE   B 69  ? 0.1739 0.1654 0.1824 0.0001  0.0032  -0.0294 69  ILE   B CB  
5103 C CG1 . ILE   B 69  ? 0.1784 0.1757 0.1966 -0.0089 0.0094  -0.0373 69  ILE   B CG1 
5104 C CG2 . ILE   B 69  ? 0.1893 0.1751 0.1984 0.0007  0.0011  -0.0204 69  ILE   B CG2 
5105 C CD1 . ILE   B 69  ? 0.1789 0.1813 0.2049 -0.0132 0.0027  -0.0509 69  ILE   B CD1 
5117 N N   . ALA   B 70  ? 0.1692 0.1621 0.1545 0.0152  -0.0322 -0.0260 70  ALA   B N   
5118 C CA  . ALA   B 70  ? 0.1730 0.1703 0.1425 0.0093  -0.0375 -0.0317 70  ALA   B CA  
5119 C C   . ALA   B 70  ? 0.1815 0.1683 0.1561 0.0050  -0.0429 -0.0441 70  ALA   B C   
5120 O O   . ALA   B 70  ? 0.1926 0.1653 0.1660 0.0028  -0.0380 -0.0401 70  ALA   B O   
5121 C CB  . ALA   B 70  ? 0.1742 0.1838 0.1575 0.0071  -0.0403 -0.0376 70  ALA   B CB  
5127 N N   . THR   B 71  ? 0.1837 0.1661 0.1700 0.0056  -0.0584 -0.0365 71  THR   B N   
5128 C CA  . THR   B 71  ? 0.1994 0.1653 0.1974 0.0114  -0.0660 -0.0344 71  THR   B CA  
5129 C C   . THR   B 71  ? 0.1922 0.1622 0.2211 0.0285  -0.0555 -0.0530 71  THR   B C   
5130 O O   . THR   B 71  ? 0.2045 0.1763 0.2506 0.0351  -0.0445 -0.0609 71  THR   B O   
5131 C CB  . THR   B 71  ? 0.2284 0.1847 0.2164 0.0067  -0.0706 -0.0174 71  THR   B CB  
5132 O OG1 . THR   B 71  ? 0.2412 0.2148 0.2466 -0.0161 -0.0698 -0.0003 71  THR   B OG1 
5133 C CG2 . THR   B 71  ? 0.2499 0.1842 0.2371 0.0138  -0.0564 -0.0064 71  THR   B CG2 
5141 N N   . ASN   B 72  ? 0.1750 0.1681 0.2094 0.0166  -0.0620 -0.0647 72  ASN   B N   
5142 C CA  . ASN   B 72  ? 0.1767 0.1921 0.2118 0.0159  -0.0537 -0.0754 72  ASN   B CA  
5143 C C   . ASN   B 72  ? 0.1774 0.2042 0.2280 0.0068  -0.0262 -0.0768 72  ASN   B C   
5144 O O   . ASN   B 72  ? 0.1826 0.2131 0.2550 0.0090  -0.0104 -0.0745 72  ASN   B O   
5145 C CB  . ASN   B 72  ? 0.1841 0.2071 0.2427 0.0139  -0.0656 -0.0659 72  ASN   B CB  
5146 C CG  . ASN   B 72  ? 0.2043 0.2219 0.2515 0.0284  -0.0692 -0.0318 72  ASN   B CG  
5147 O OD1 . ASN   B 72  ? 0.2255 0.2375 0.2602 0.0165  -0.0477 -0.0424 72  ASN   B OD1 
5148 N ND2 . ASN   B 72  ? 0.2205 0.2263 0.2938 0.0448  -0.0609 0.0128  72  ASN   B ND2 
5155 N N   . GLY   B 73  ? 0.1800 0.2018 0.2152 0.0025  -0.0259 -0.0805 73  GLY   B N   
5156 C CA  . GLY   B 73  ? 0.1748 0.2142 0.1703 -0.0030 -0.0170 -0.0719 73  GLY   B CA  
5157 C C   . GLY   B 73  ? 0.1751 0.2073 0.1273 0.0084  -0.0224 -0.0472 73  GLY   B C   
5158 O O   . GLY   B 73  ? 0.1711 0.1913 0.1492 0.0118  -0.0207 -0.0357 73  GLY   B O   
5162 N N   . PRO   B 74  ? 0.1818 0.2181 0.1171 0.0032  -0.0120 -0.0418 74  PRO   B N   
5163 C CA  . PRO   B 74  ? 0.1754 0.2151 0.1036 0.0075  -0.0169 -0.0233 74  PRO   B CA  
5164 C C   . PRO   B 74  ? 0.1618 0.1927 0.1176 0.0089  -0.0082 -0.0237 74  PRO   B C   
5165 O O   . PRO   B 74  ? 0.1657 0.1914 0.1708 0.0103  -0.0054 -0.0326 74  PRO   B O   
5166 C CB  . PRO   B 74  ? 0.1841 0.2306 0.1133 0.0069  -0.0145 -0.0177 74  PRO   B CB  
5167 C CG  . PRO   B 74  ? 0.2110 0.2464 0.1458 0.0048  -0.0174 -0.0103 74  PRO   B CG  
5168 C CD  . PRO   B 74  ? 0.2058 0.2361 0.1326 0.0041  -0.0119 -0.0323 74  PRO   B CD  
5176 N N   . LEU   B 75  ? 0.1581 0.1828 0.1129 0.0103  -0.0125 -0.0172 75  LEU   B N   
5177 C CA  . LEU   B 75  ? 0.1618 0.1818 0.1190 0.0038  -0.0137 -0.0073 75  LEU   B CA  
5178 C C   . LEU   B 75  ? 0.1667 0.1949 0.1259 0.0113  -0.0138 -0.0061 75  LEU   B C   
5179 O O   . LEU   B 75  ? 0.1829 0.2072 0.1280 -0.0034 -0.0111 0.0038  75  LEU   B O   
5180 C CB  . LEU   B 75  ? 0.1628 0.1815 0.1060 -0.0031 -0.0161 0.0056  75  LEU   B CB  
5181 C CG  . LEU   B 75  ? 0.1913 0.1911 0.1354 -0.0241 -0.0044 -0.0031 75  LEU   B CG  
5182 C CD1 . LEU   B 75  ? 0.2233 0.2091 0.1490 -0.0361 0.0213  -0.0124 75  LEU   B CD1 
5183 C CD2 . LEU   B 75  ? 0.2350 0.2141 0.2169 -0.0112 0.0052  0.0041  75  LEU   B CD2 
5195 N N   . LYS   B 76  ? 0.1653 0.2130 0.1550 0.0052  -0.0013 0.0140  76  LYS   B N   
5196 C CA  . LYS   B 76  ? 0.1792 0.2244 0.1812 -0.0036 0.0131  0.0042  76  LYS   B CA  
5197 C C   . LYS   B 76  ? 0.1711 0.2102 0.1518 -0.0002 0.0181  0.0276  76  LYS   B C   
5198 O O   . LYS   B 76  ? 0.1795 0.1867 0.1481 -0.0014 0.0140  0.0222  76  LYS   B O   
5199 C CB  . LYS   B 76  ? 0.1927 0.2334 0.2424 -0.0060 0.0399  -0.0347 76  LYS   B CB  
5200 C CG  . LYS   B 76  ? 0.1981 0.2518 0.2797 0.0019  0.0366  -0.0452 76  LYS   B CG  
5201 C CD  . LYS   B 76  ? 0.2003 0.2558 0.3153 0.0062  0.0291  -0.0624 76  LYS   B CD  
5202 C CE  . LYS   B 76  ? 0.2079 0.2677 0.3576 0.0055  0.0133  -0.0743 76  LYS   B CE  
5203 N NZ  . LYS   B 76  ? 0.2048 0.2719 0.3730 -0.0020 -0.0121 -0.0973 76  LYS   B NZ  
5217 N N   . VAL   B 77  ? 0.1847 0.2212 0.1555 0.0038  0.0197  0.0329  77  VAL   B N   
5218 C CA  . VAL   B 77  ? 0.1869 0.2163 0.1751 0.0116  0.0281  0.0635  77  VAL   B CA  
5219 C C   . VAL   B 77  ? 0.1705 0.1874 0.1570 0.0163  0.0477  0.0412  77  VAL   B C   
5220 O O   . VAL   B 77  ? 0.1741 0.1837 0.1492 0.0265  0.0462  0.0329  77  VAL   B O   
5221 C CB  . VAL   B 77  ? 0.1960 0.2272 0.2275 0.0149  0.0362  0.0881  77  VAL   B CB  
5222 C CG1 . VAL   B 77  ? 0.1899 0.2202 0.2609 0.0116  0.0355  0.1027  77  VAL   B CG1 
5223 C CG2 . VAL   B 77  ? 0.2167 0.2445 0.2372 0.0104  0.0224  0.0933  77  VAL   B CG2 
5233 N N   . GLY   B 78  ? 0.1669 0.1726 0.1551 0.0132  0.0337  0.0303  78  GLY   B N   
5234 C CA  . GLY   B 78  ? 0.1706 0.1658 0.1508 0.0167  0.0284  0.0276  78  GLY   B CA  
5235 C C   . GLY   B 78  ? 0.1603 0.1607 0.1482 0.0134  0.0308  0.0315  78  GLY   B C   
5236 O O   . GLY   B 78  ? 0.1606 0.1504 0.1582 0.0139  0.0219  0.0247  78  GLY   B O   
5240 N N   . GLY   B 79  ? 0.1487 0.1668 0.1479 0.0109  0.0244  0.0144  79  GLY   B N   
5241 C CA  . GLY   B 79  ? 0.1531 0.1571 0.1440 0.0155  0.0166  0.0207  79  GLY   B CA  
5242 C C   . GLY   B 79  ? 0.1479 0.1494 0.1415 0.0212  0.0159  0.0148  79  GLY   B C   
5243 O O   . GLY   B 79  ? 0.1488 0.1474 0.1586 0.0159  0.0166  0.0226  79  GLY   B O   
5247 N N   . SER   B 80  ? 0.1482 0.1351 0.1394 0.0169  0.0195  0.0102  80  SER   B N   
5248 C CA  . SER   B 80  ? 0.1382 0.1378 0.1324 0.0063  -0.0034 0.0088  80  SER   B CA  
5249 C C   . SER   B 80  ? 0.1360 0.1356 0.1387 0.0101  -0.0052 -0.0042 80  SER   B C   
5250 O O   . SER   B 80  ? 0.1539 0.1353 0.1650 0.0153  -0.0001 -0.0067 80  SER   B O   
5251 C CB  . SER   B 80  ? 0.1417 0.1436 0.1401 0.0008  0.0005  0.0147  80  SER   B CB  
5252 O OG  . SER   B 80  ? 0.1495 0.1603 0.1532 -0.0037 -0.0130 0.0108  80  SER   B OG  
5258 N N   . CYS   B 81  ? 0.1340 0.1271 0.1403 0.0037  -0.0103 0.0001  81  CYS   B N   
5259 C CA  . CYS   B 81  ? 0.1475 0.1251 0.1406 0.0091  -0.0142 0.0027  81  CYS   B CA  
5260 C C   . CYS   B 81  ? 0.1418 0.1261 0.1200 0.0044  -0.0143 -0.0043 81  CYS   B C   
5261 O O   . CYS   B 81  ? 0.1631 0.1233 0.1395 0.0102  -0.0048 0.0010  81  CYS   B O   
5262 C CB  . CYS   B 81  ? 0.1523 0.1448 0.1450 -0.0038 -0.0164 0.0002  81  CYS   B CB  
5263 S SG  . CYS   B 81  ? 0.1608 0.1551 0.1454 -0.0004 -0.0245 -0.0068 81  CYS   B SG  
5269 N N   . VAL   B 82  ? 0.1462 0.1273 0.1351 0.0015  -0.0147 -0.0028 82  VAL   B N   
5270 C CA  . VAL   B 82  ? 0.1498 0.1311 0.1258 -0.0042 -0.0049 0.0037  82  VAL   B CA  
5271 C C   . VAL   B 82  ? 0.1532 0.1245 0.1308 -0.0043 -0.0136 0.0019  82  VAL   B C   
5272 O O   . VAL   B 82  ? 0.1682 0.1237 0.1612 -0.0007 -0.0156 -0.0214 82  VAL   B O   
5273 C CB  . VAL   B 82  ? 0.1562 0.1490 0.1565 -0.0062 -0.0172 0.0156  82  VAL   B CB  
5274 C CG1 . VAL   B 82  ? 0.1737 0.1640 0.1715 -0.0009 -0.0176 0.0322  82  VAL   B CG1 
5275 C CG2 . VAL   B 82  ? 0.1581 0.1555 0.1744 -0.0057 -0.0305 0.0167  82  VAL   B CG2 
5285 N N   . LEU   B 83  ? 0.1417 0.1237 0.1333 -0.0118 -0.0169 -0.0040 83  LEU   B N   
5286 C CA  . LEU   B 83  ? 0.1504 0.1273 0.1177 -0.0132 -0.0249 -0.0060 83  LEU   B CA  
5287 C C   . LEU   B 83  ? 0.1546 0.1221 0.1135 -0.0170 -0.0255 0.0025  83  LEU   B C   
5288 O O   . LEU   B 83  ? 0.1502 0.1401 0.1014 -0.0232 -0.0147 0.0036  83  LEU   B O   
5289 C CB  . LEU   B 83  ? 0.1534 0.1409 0.1260 -0.0113 -0.0239 -0.0113 83  LEU   B CB  
5290 C CG  . LEU   B 83  ? 0.1674 0.1600 0.1356 -0.0057 -0.0195 -0.0120 83  LEU   B CG  
5291 C CD1 . LEU   B 83  ? 0.1764 0.1656 0.1505 -0.0077 -0.0314 -0.0033 83  LEU   B CD1 
5292 C CD2 . LEU   B 83  ? 0.1875 0.1652 0.1682 -0.0017 -0.0288 -0.0183 83  LEU   B CD2 
5304 N N   . SER   B 84  ? 0.1526 0.1379 0.1453 -0.0196 -0.0201 0.0040  84  SER   B N   
5305 C CA  . SER   B 84  ? 0.1509 0.1542 0.1396 -0.0267 -0.0124 0.0152  84  SER   B CA  
5306 C C   . SER   B 84  ? 0.1429 0.1673 0.0858 -0.0185 -0.0128 0.0167  84  SER   B C   
5307 O O   . SER   B 84  ? 0.1577 0.1589 0.0969 -0.0243 -0.0082 0.0071  84  SER   B O   
5308 C CB  . SER   B 84  ? 0.1663 0.1653 0.1858 -0.0266 0.0121  0.0120  84  SER   B CB  
5309 O OG  . SER   B 84  ? 0.1644 0.1804 0.2396 -0.0390 -0.0008 0.0184  84  SER   B OG  
5315 N N   . GLY   B 85  ? 0.1463 0.1871 0.1062 -0.0240 -0.0143 0.0179  85  GLY   B N   
5316 C CA  . GLY   B 85  ? 0.1465 0.1954 0.1263 -0.0318 0.0037  -0.0173 85  GLY   B CA  
5317 C C   . GLY   B 85  ? 0.1487 0.1818 0.1129 -0.0396 -0.0043 -0.0025 85  GLY   B C   
5318 O O   . GLY   B 85  ? 0.1609 0.1844 0.1225 -0.0566 0.0153  -0.0128 85  GLY   B O   
5322 N N   . HIS   B 86  ? 0.1446 0.1699 0.1339 -0.0362 -0.0121 0.0115  86  HIS   B N   
5323 C CA  . HIS   B 86  ? 0.1572 0.1674 0.1201 -0.0333 -0.0243 0.0128  86  HIS   B CA  
5324 C C   . HIS   B 86  ? 0.1494 0.1770 0.1333 -0.0387 -0.0066 0.0305  86  HIS   B C   
5325 O O   . HIS   B 86  ? 0.1610 0.1934 0.1351 -0.0351 0.0049  0.0271  86  HIS   B O   
5326 C CB  . HIS   B 86  ? 0.1639 0.1725 0.1369 -0.0196 -0.0177 0.0085  86  HIS   B CB  
5327 C CG  . HIS   B 86  ? 0.1622 0.1730 0.1462 -0.0147 -0.0234 0.0090  86  HIS   B CG  
5328 N ND1 . HIS   B 86  ? 0.1625 0.1934 0.1826 -0.0129 -0.0184 -0.0138 86  HIS   B ND1 
5329 C CD2 . HIS   B 86  ? 0.1607 0.1756 0.1422 -0.0082 -0.0121 0.0010  86  HIS   B CD2 
5330 C CE1 . HIS   B 86  ? 0.1745 0.1947 0.1683 -0.0075 0.0042  -0.0263 86  HIS   B CE1 
5331 N NE2 . HIS   B 86  ? 0.1731 0.1867 0.1413 -0.0022 -0.0070 -0.0011 86  HIS   B NE2 
5339 N N   . ASN   B 87  ? 0.1512 0.1758 0.1519 -0.0291 0.0090  0.0169  87  ASN   B N   
5340 C CA  . ASN   B 87  ? 0.1620 0.1980 0.1549 -0.0338 0.0329  0.0161  87  ASN   B CA  
5341 C C   . ASN   B 87  ? 0.1743 0.1861 0.1279 -0.0332 0.0357  0.0075  87  ASN   B C   
5342 O O   . ASN   B 87  ? 0.2084 0.1916 0.1622 -0.0277 0.0590  -0.0012 87  ASN   B O   
5343 C CB  . ASN   B 87  ? 0.1645 0.2332 0.1934 -0.0263 0.0429  0.0190  87  ASN   B CB  
5344 C CG  . ASN   B 87  ? 0.1722 0.2560 0.2061 0.0060  0.0508  0.0274  87  ASN   B CG  
5345 O OD1 . ASN   B 87  ? 0.1676 0.2330 0.1800 0.0145  0.0563  0.0373  87  ASN   B OD1 
5346 N ND2 . ASN   B 87  ? 0.2045 0.2708 0.2378 0.0179  0.0583  0.0267  87  ASN   B ND2 
5353 N N   . LEU   B 88  ? 0.1581 0.1809 0.1140 -0.0324 0.0179  0.0026  88  LEU   B N   
5354 C CA  . LEU   B 88  ? 0.1765 0.1701 0.1179 -0.0366 0.0038  0.0033  88  LEU   B CA  
5355 C C   . LEU   B 88  ? 0.1816 0.1526 0.1229 -0.0375 -0.0009 -0.0041 88  LEU   B C   
5356 O O   . LEU   B 88  ? 0.2038 0.1643 0.1612 -0.0205 -0.0276 -0.0103 88  LEU   B O   
5357 C CB  . LEU   B 88  ? 0.1947 0.1783 0.1424 -0.0502 -0.0109 0.0116  88  LEU   B CB  
5358 C CG  . LEU   B 88  ? 0.2345 0.2091 0.1592 -0.0408 -0.0295 0.0381  88  LEU   B CG  
5359 C CD1 . LEU   B 88  ? 0.2351 0.2433 0.1858 -0.0548 -0.0295 0.0556  88  LEU   B CD1 
5360 C CD2 . LEU   B 88  ? 0.2773 0.2365 0.2246 0.0010  -0.0468 0.0086  88  LEU   B CD2 
5372 N N   . ALA   B 89  ? 0.1676 0.1539 0.1280 -0.0443 0.0161  0.0022  89  ALA   B N   
5373 C CA  . ALA   B 89  ? 0.1657 0.1551 0.1029 -0.0376 -0.0008 0.0111  89  ALA   B CA  
5374 C C   . ALA   B 89  ? 0.1768 0.1492 0.1003 -0.0403 0.0164  0.0061  89  ALA   B C   
5375 O O   . ALA   B 89  ? 0.1519 0.1667 0.1419 -0.0449 0.0073  -0.0251 89  ALA   B O   
5376 C CB  . ALA   B 89  ? 0.1504 0.1532 0.1212 -0.0383 0.0085  0.0131  89  ALA   B CB  
5382 N N   . LYS   B 90  ? 0.2101 0.1397 0.1077 -0.0492 -0.0059 0.0105  90  LYS   B N   
5383 C CA  . LYS   B 90  ? 0.2164 0.1391 0.1084 -0.0482 -0.0146 0.0145  90  LYS   B CA  
5384 C C   . LYS   B 90  ? 0.1948 0.1390 0.1236 -0.0433 -0.0156 -0.0014 90  LYS   B C   
5385 O O   . LYS   B 90  ? 0.1952 0.1515 0.1398 -0.0535 -0.0154 0.0039  90  LYS   B O   
5386 C CB  . LYS   B 90  ? 0.2295 0.1419 0.1542 -0.0381 -0.0001 0.0222  90  LYS   B CB  
5387 C CG  . LYS   B 90  ? 0.2274 0.1605 0.1663 -0.0242 0.0219  0.0120  90  LYS   B CG  
5388 C CD  . LYS   B 90  ? 0.2479 0.1865 0.2144 -0.0133 0.0380  -0.0090 90  LYS   B CD  
5389 C CE  . LYS   B 90  ? 0.2748 0.2086 0.2777 -0.0175 0.0366  -0.0265 90  LYS   B CE  
5390 N NZ  . LYS   B 90  ? 0.2747 0.2112 0.2668 -0.0368 0.0530  -0.0257 90  LYS   B NZ  
5404 N N   . HIS   B 91  ? 0.1701 0.1273 0.1001 -0.0349 -0.0105 0.0080  91  HIS   B N   
5405 C CA  . HIS   B 91  ? 0.1613 0.1261 0.1266 -0.0262 -0.0203 0.0087  91  HIS   B CA  
5406 C C   . HIS   B 91  ? 0.1527 0.1319 0.1054 -0.0211 -0.0051 0.0025  91  HIS   B C   
5407 O O   . HIS   B 91  ? 0.1626 0.1392 0.1030 -0.0273 -0.0150 0.0007  91  HIS   B O   
5408 C CB  . HIS   B 91  ? 0.1823 0.1319 0.1711 -0.0113 -0.0199 0.0174  91  HIS   B CB  
5409 C CG  . HIS   B 91  ? 0.2209 0.1537 0.2350 -0.0024 0.0169  0.0297  91  HIS   B CG  
5410 N ND1 . HIS   B 91  ? 0.2531 0.1594 0.2945 -0.0004 0.0251  0.0034  91  HIS   B ND1 
5411 C CD2 . HIS   B 91  ? 0.2314 0.1763 0.2871 0.0151  0.0020  0.0694  91  HIS   B CD2 
5412 C CE1 . HIS   B 91  ? 0.2577 0.1738 0.3233 0.0158  0.0308  0.0156  91  HIS   B CE1 
5413 N NE2 . HIS   B 91  ? 0.2505 0.1882 0.3134 0.0215  0.0208  0.0675  91  HIS   B NE2 
5421 N N   . CYS   B 92  ? 0.1490 0.1290 0.0900 -0.0247 -0.0069 -0.0011 92  CYS   B N   
5422 C CA  . CYS   B 92  ? 0.1538 0.1254 0.0970 -0.0206 -0.0058 0.0022  92  CYS   B CA  
5423 C C   . CYS   B 92  ? 0.1421 0.1315 0.0957 -0.0156 -0.0021 -0.0013 92  CYS   B C   
5424 O O   . CYS   B 92  ? 0.1489 0.1363 0.1184 -0.0140 -0.0051 -0.0001 92  CYS   B O   
5425 C CB  . CYS   B 92  ? 0.1497 0.1321 0.1139 -0.0121 -0.0123 -0.0012 92  CYS   B CB  
5426 S SG  . CYS   B 92  ? 0.1391 0.1356 0.1290 -0.0111 -0.0111 0.0058  92  CYS   B SG  
5432 N N   . LEU   B 93  ? 0.1363 0.1293 0.0983 -0.0141 -0.0016 -0.0088 93  LEU   B N   
5433 C CA  . LEU   B 93  ? 0.1397 0.1254 0.1061 0.0001  -0.0134 -0.0031 93  LEU   B CA  
5434 C C   . LEU   B 93  ? 0.1331 0.1184 0.0899 0.0061  -0.0042 0.0168  93  LEU   B C   
5435 O O   . LEU   B 93  ? 0.1388 0.1186 0.1121 -0.0016 -0.0078 0.0012  93  LEU   B O   
5436 C CB  . LEU   B 93  ? 0.1403 0.1152 0.1100 -0.0015 -0.0057 0.0027  93  LEU   B CB  
5437 C CG  . LEU   B 93  ? 0.1302 0.1410 0.1427 -0.0035 -0.0071 0.0050  93  LEU   B CG  
5438 C CD1 . LEU   B 93  ? 0.1361 0.1516 0.1392 0.0059  -0.0039 -0.0037 93  LEU   B CD1 
5439 C CD2 . LEU   B 93  ? 0.1336 0.1467 0.1478 0.0008  -0.0114 -0.0024 93  LEU   B CD2 
5451 N N   . HIS   B 94  ? 0.1391 0.1172 0.0936 0.0022  -0.0068 0.0089  94  HIS   B N   
5452 C CA  . HIS   B 94  ? 0.1374 0.1178 0.0978 -0.0018 -0.0036 -0.0013 94  HIS   B CA  
5453 C C   . HIS   B 94  ? 0.1288 0.1224 0.1224 -0.0031 -0.0027 0.0100  94  HIS   B C   
5454 O O   . HIS   B 94  ? 0.1273 0.1266 0.1576 0.0004  0.0117  -0.0081 94  HIS   B O   
5455 C CB  . HIS   B 94  ? 0.1291 0.1368 0.1174 0.0057  -0.0066 0.0052  94  HIS   B CB  
5456 C CG  . HIS   B 94  ? 0.1334 0.1236 0.1140 0.0019  -0.0186 -0.0033 94  HIS   B CG  
5457 N ND1 . HIS   B 94  ? 0.1368 0.1266 0.1073 -0.0034 -0.0183 -0.0038 94  HIS   B ND1 
5458 C CD2 . HIS   B 94  ? 0.1298 0.1310 0.1253 0.0009  -0.0158 0.0062  94  HIS   B CD2 
5459 C CE1 . HIS   B 94  ? 0.1407 0.1341 0.1087 -0.0063 -0.0136 0.0030  94  HIS   B CE1 
5460 N NE2 . HIS   B 94  ? 0.1297 0.1397 0.1174 -0.0098 -0.0105 0.0011  94  HIS   B NE2 
5468 N N   . VAL   B 95  ? 0.1229 0.1221 0.1206 0.0003  0.0016  0.0056  95  VAL   B N   
5469 C CA  . VAL   B 95  ? 0.1286 0.1367 0.1126 0.0013  0.0040  0.0133  95  VAL   B CA  
5470 C C   . VAL   B 95  ? 0.1395 0.1315 0.1116 0.0029  0.0101  0.0115  95  VAL   B C   
5471 O O   . VAL   B 95  ? 0.1412 0.1268 0.1393 0.0149  0.0083  0.0184  95  VAL   B O   
5472 C CB  . VAL   B 95  ? 0.1363 0.1343 0.1112 -0.0015 -0.0056 0.0065  95  VAL   B CB  
5473 C CG1 . VAL   B 95  ? 0.1400 0.1475 0.1445 -0.0054 -0.0013 0.0129  95  VAL   B CG1 
5474 C CG2 . VAL   B 95  ? 0.1459 0.1274 0.1140 0.0018  -0.0097 0.0088  95  VAL   B CG2 
5484 N N   . VAL   B 96  ? 0.1465 0.1367 0.1136 0.0109  0.0059  0.0186  96  VAL   B N   
5485 C CA  . VAL   B 96  ? 0.1592 0.1480 0.1141 0.0080  0.0090  0.0216  96  VAL   B CA  
5486 C C   . VAL   B 96  ? 0.1610 0.1528 0.1393 0.0090  0.0252  0.0231  96  VAL   B C   
5487 O O   . VAL   B 96  ? 0.1559 0.1565 0.1562 -0.0003 0.0306  0.0040  96  VAL   B O   
5488 C CB  . VAL   B 96  ? 0.1678 0.1650 0.1137 0.0129  0.0064  0.0105  96  VAL   B CB  
5489 C CG1 . VAL   B 96  ? 0.1650 0.1782 0.1358 0.0182  0.0099  0.0109  96  VAL   B CG1 
5490 C CG2 . VAL   B 96  ? 0.1710 0.1663 0.1391 0.0065  0.0068  -0.0012 96  VAL   B CG2 
5500 N N   . GLY   B 97  ? 0.1599 0.1547 0.1227 0.0112  0.0096  0.0211  97  GLY   B N   
5501 C CA  . GLY   B 97  ? 0.1795 0.1531 0.1366 0.0094  0.0125  0.0244  97  GLY   B CA  
5502 C C   . GLY   B 97  ? 0.2025 0.1611 0.1535 0.0113  0.0182  0.0215  97  GLY   B C   
5503 O O   . GLY   B 97  ? 0.2222 0.1683 0.1489 0.0080  0.0048  0.0128  97  GLY   B O   
5507 N N   . PRO   B 98  ? 0.2236 0.1724 0.1611 0.0149  0.0422  0.0381  98  PRO   B N   
5508 C CA  . PRO   B 98  ? 0.2442 0.1902 0.1772 0.0341  0.0584  0.0397  98  PRO   B CA  
5509 C C   . PRO   B 98  ? 0.2628 0.1884 0.1539 0.0535  0.0583  0.0594  98  PRO   B C   
5510 O O   . PRO   B 98  ? 0.2512 0.1891 0.1793 0.0442  0.0688  0.0534  98  PRO   B O   
5511 C CB  . PRO   B 98  ? 0.2314 0.1959 0.2038 0.0273  0.0734  0.0551  98  PRO   B CB  
5512 C CG  . PRO   B 98  ? 0.2195 0.1867 0.2097 0.0246  0.0555  0.0633  98  PRO   B CG  
5513 C CD  . PRO   B 98  ? 0.2077 0.1747 0.1927 0.0151  0.0502  0.0492  98  PRO   B CD  
5521 N N   . ASN   B 99  ? 0.2800 0.2096 0.1568 0.0747  0.0609  0.0488  99  ASN   B N   
5522 C CA  . ASN   B 99  ? 0.3035 0.2239 0.1700 0.0889  0.0572  0.0672  99  ASN   B CA  
5523 C C   . ASN   B 99  ? 0.3290 0.2591 0.2118 0.0911  0.0809  0.1030  99  ASN   B C   
5524 O O   . ASN   B 99  ? 0.3410 0.2672 0.2194 0.0871  0.0828  0.1021  99  ASN   B O   
5525 C CB  . ASN   B 99  ? 0.3098 0.2143 0.1847 0.0891  0.0475  0.0601  99  ASN   B CB  
5526 C CG  . ASN   B 99  ? 0.3185 0.2198 0.1888 0.0759  0.0385  0.0502  99  ASN   B CG  
5527 O OD1 . ASN   B 99  ? 0.3279 0.2189 0.2230 0.0747  0.0446  0.0587  99  ASN   B OD1 
5528 N ND2 . ASN   B 99  ? 0.3178 0.2247 0.1974 0.0695  0.0029  0.0323  99  ASN   B ND2 
5535 N N   A VAL   B 100 ? 0.3454 0.2728 0.2593 0.0805  0.0837  0.1182  100 VAL   B N   
5536 N N   B VAL   B 100 ? 0.3429 0.2714 0.2613 0.0786  0.0913  0.1249  100 VAL   B N   
5537 C CA  A VAL   B 100 ? 0.3657 0.2922 0.3169 0.0665  0.0757  0.1247  100 VAL   B CA  
5538 C CA  B VAL   B 100 ? 0.3631 0.2911 0.3250 0.0639  0.0851  0.1333  100 VAL   B CA  
5539 C C   A VAL   B 100 ? 0.3820 0.3009 0.3157 0.0651  0.0743  0.1430  100 VAL   B C   
5540 C C   B VAL   B 100 ? 0.3807 0.2990 0.3163 0.0637  0.0824  0.1495  100 VAL   B C   
5541 O O   A VAL   B 100 ? 0.3873 0.3130 0.3328 0.0610  0.0850  0.1352  100 VAL   B O   
5542 O O   B VAL   B 100 ? 0.3865 0.3107 0.3300 0.0605  0.0965  0.1386  100 VAL   B O   
5543 C CB  A VAL   B 100 ? 0.3727 0.3031 0.3705 0.0470  0.0664  0.1208  100 VAL   B CB  
5544 C CB  B VAL   B 100 ? 0.3705 0.3030 0.3913 0.0411  0.0769  0.1345  100 VAL   B CB  
5545 C CG1 A VAL   B 100 ? 0.3750 0.3076 0.3809 0.0412  0.0610  0.1231  100 VAL   B CG1 
5546 C CG1 B VAL   B 100 ? 0.3741 0.3087 0.4033 0.0351  0.0717  0.1381  100 VAL   B CG1 
5547 C CG2 A VAL   B 100 ? 0.3757 0.3059 0.3860 0.0403  0.0643  0.1200  100 VAL   B CG2 
5548 C CG2 B VAL   B 100 ? 0.3726 0.3054 0.4102 0.0329  0.0760  0.1356  100 VAL   B CG2 
5567 N N   . ASN   B 101 ? 0.3933 0.3004 0.3002 0.0716  0.0647  0.1538  101 ASN   B N   
5568 C CA  . ASN   B 101 ? 0.4250 0.3079 0.3162 0.0761  0.0379  0.1641  101 ASN   B CA  
5569 C C   . ASN   B 101 ? 0.4661 0.3409 0.3166 0.0735  0.0146  0.1769  101 ASN   B C   
5570 O O   . ASN   B 101 ? 0.4723 0.3570 0.3550 0.0779  0.0234  0.1336  101 ASN   B O   
5571 C CB  . ASN   B 101 ? 0.4201 0.2946 0.3284 0.0708  0.0495  0.1366  101 ASN   B CB  
5572 C CG  . ASN   B 101 ? 0.4130 0.2860 0.3311 0.0682  0.0522  0.1245  101 ASN   B CG  
5573 O OD1 . ASN   B 101 ? 0.4173 0.2908 0.3612 0.0617  0.0619  0.1123  101 ASN   B OD1 
5574 N ND2 . ASN   B 101 ? 0.4067 0.2833 0.3200 0.0676  0.0478  0.1114  101 ASN   B ND2 
5582 N N   . LYS   B 102 ? 0.4995 0.3750 0.3399 0.0573  0.0104  0.1695  102 LYS   B N   
5583 C CA  . LYS   B 102 ? 0.5299 0.4197 0.3753 0.0337  0.0045  0.1393  102 LYS   B CA  
5584 C C   . LYS   B 102 ? 0.5276 0.4273 0.3569 0.0351  0.0096  0.1373  102 LYS   B C   
5585 O O   . LYS   B 102 ? 0.5365 0.4318 0.3611 0.0351  -0.0089 0.1353  102 LYS   B O   
5586 C CB  . LYS   B 102 ? 0.5576 0.4543 0.4345 0.0117  0.0120  0.0969  102 LYS   B CB  
5587 C CG  . LYS   B 102 ? 0.5809 0.4844 0.5095 -0.0026 0.0130  0.0535  102 LYS   B CG  
5588 C CD  . LYS   B 102 ? 0.5999 0.5087 0.5643 -0.0120 0.0176  0.0198  102 LYS   B CD  
5589 C CE  . LYS   B 102 ? 0.6120 0.5253 0.6184 -0.0190 0.0231  -0.0030 102 LYS   B CE  
5590 N NZ  . LYS   B 102 ? 0.6189 0.5353 0.6455 -0.0223 0.0242  -0.0187 102 LYS   B NZ  
5604 N N   . GLY   B 103 ? 0.5130 0.4269 0.3359 0.0347  0.0377  0.1287  103 GLY   B N   
5605 C CA  . GLY   B 103 ? 0.4954 0.4240 0.3531 0.0370  0.0656  0.1096  103 GLY   B CA  
5606 C C   . GLY   B 103 ? 0.4733 0.4175 0.3522 0.0375  0.0885  0.0866  103 GLY   B C   
5607 O O   . GLY   B 103 ? 0.4770 0.4260 0.3550 0.0300  0.0926  0.0893  103 GLY   B O   
5611 N N   A GLU   B 104 ? 0.4619 0.4122 0.3445 0.0417  0.0901  0.0688  104 GLU   B N   
5612 N N   B GLU   B 104 ? 0.4556 0.4050 0.3281 0.0421  0.1047  0.0739  104 GLU   B N   
5613 C CA  A GLU   B 104 ? 0.4500 0.4062 0.3411 0.0485  0.0868  0.0487  104 GLU   B CA  
5614 C CA  B GLU   B 104 ? 0.4383 0.3928 0.3110 0.0505  0.1098  0.0592  104 GLU   B CA  
5615 C C   A GLU   B 104 ? 0.4448 0.4028 0.3542 0.0350  0.1080  0.0461  104 GLU   B C   
5616 C C   B GLU   B 104 ? 0.4324 0.3887 0.3178 0.0313  0.1435  0.0655  104 GLU   B C   
5617 O O   A GLU   B 104 ? 0.4434 0.4041 0.3644 0.0324  0.1086  0.0461  104 GLU   B O   
5618 O O   B GLU   B 104 ? 0.4300 0.3900 0.3365 0.0279  0.1446  0.0630  104 GLU   B O   
5619 C CB  A GLU   B 104 ? 0.4455 0.4015 0.3304 0.0669  0.0582  0.0238  104 GLU   B CB  
5620 C CB  B GLU   B 104 ? 0.4310 0.3824 0.2995 0.0765  0.0724  0.0259  104 GLU   B CB  
5621 C CG  A GLU   B 104 ? 0.4386 0.3954 0.3236 0.0807  0.0228  -0.0039 104 GLU   B CG  
5622 C CG  B GLU   B 104 ? 0.4218 0.3713 0.2911 0.0978  0.0268  -0.0114 104 GLU   B CG  
5623 C CD  A GLU   B 104 ? 0.4298 0.3878 0.3096 0.0885  -0.0014 -0.0222 104 GLU   B CD  
5624 C CD  B GLU   B 104 ? 0.4113 0.3593 0.2710 0.1109  -0.0042 -0.0333 104 GLU   B CD  
5625 O OE1 A GLU   B 104 ? 0.4178 0.3764 0.2872 0.0908  0.0013  -0.0311 104 GLU   B OE1 
5626 O OE1 B GLU   B 104 ? 0.3946 0.3413 0.2330 0.1181  0.0048  -0.0492 104 GLU   B OE1 
5627 O OE2 A GLU   B 104 ? 0.4328 0.3926 0.3116 0.0909  -0.0191 -0.0339 104 GLU   B OE2 
5628 O OE2 B GLU   B 104 ? 0.4156 0.3664 0.2677 0.1122  -0.0284 -0.0450 104 GLU   B OE2 
5641 N N   A ASP   B 105 ? 0.4399 0.3993 0.3636 0.0248  0.1268  0.0432  105 ASP   B N   
5642 N N   B ASP   B 105 ? 0.4264 0.3846 0.3139 0.0168  0.1729  0.0724  105 ASP   B N   
5643 C CA  A ASP   B 105 ? 0.4378 0.3966 0.3826 0.0168  0.1445  0.0289  105 ASP   B CA  
5644 C CA  B ASP   B 105 ? 0.4243 0.3817 0.3328 0.0060  0.2016  0.0572  105 ASP   B CA  
5645 C C   A ASP   B 105 ? 0.4224 0.3778 0.3576 0.0109  0.1500  0.0225  105 ASP   B C   
5646 C C   B ASP   B 105 ? 0.4062 0.3578 0.3114 -0.0007 0.2033  0.0489  105 ASP   B C   
5647 O O   A ASP   B 105 ? 0.4187 0.3751 0.3538 0.0168  0.1566  0.0233  105 ASP   B O   
5648 O O   B ASP   B 105 ? 0.3918 0.3504 0.3107 0.0056  0.2009  0.0492  105 ASP   B O   
5649 C CB  A ASP   B 105 ? 0.4478 0.4096 0.4361 0.0193  0.1554  0.0167  105 ASP   B CB  
5650 C CB  B ASP   B 105 ? 0.4368 0.3989 0.4040 0.0099  0.2101  0.0391  105 ASP   B CB  
5651 C CG  A ASP   B 105 ? 0.4542 0.4189 0.4852 0.0208  0.1610  0.0094  105 ASP   B CG  
5652 C CG  B ASP   B 105 ? 0.4421 0.4100 0.4651 0.0092  0.2178  0.0330  105 ASP   B CG  
5653 O OD1 A ASP   B 105 ? 0.4527 0.4187 0.4966 0.0197  0.1671  0.0115  105 ASP   B OD1 
5654 O OD1 B ASP   B 105 ? 0.4418 0.4101 0.4815 0.0055  0.2226  0.0385  105 ASP   B OD1 
5655 O OD2 A ASP   B 105 ? 0.4590 0.4257 0.5122 0.0244  0.1544  0.0032  105 ASP   B OD2 
5656 O OD2 B ASP   B 105 ? 0.4408 0.4183 0.4879 0.0103  0.2203  0.0281  105 ASP   B OD2 
5665 N N   A ILE   B 106 ? 0.4088 0.3582 0.3622 0.0027  0.1400  0.0193  106 ILE   B N   
5666 N N   B ILE   B 106 ? 0.3956 0.3361 0.3283 -0.0096 0.1871  0.0438  106 ILE   B N   
5667 C CA  A ILE   B 106 ? 0.3890 0.3374 0.3577 -0.0047 0.1399  0.0118  106 ILE   B CA  
5668 C CA  B ILE   B 106 ? 0.3765 0.3132 0.3344 -0.0186 0.1851  0.0302  106 ILE   B CA  
5669 C C   A ILE   B 106 ? 0.3611 0.3254 0.3494 -0.0026 0.1400  0.0063  106 ILE   B C   
5670 C C   B ILE   B 106 ? 0.3424 0.3014 0.3201 -0.0181 0.1904  0.0212  106 ILE   B C   
5671 O O   A ILE   B 106 ? 0.3580 0.3136 0.3536 -0.0034 0.1392  0.0065  106 ILE   B O   
5672 O O   B ILE   B 106 ? 0.3353 0.2824 0.3175 -0.0252 0.1879  0.0294  106 ILE   B O   
5673 C CB  A ILE   B 106 ? 0.3959 0.3314 0.3595 -0.0140 0.1374  0.0115  106 ILE   B CB  
5674 C CB  B ILE   B 106 ? 0.3912 0.3078 0.3473 -0.0273 0.1773  0.0272  106 ILE   B CB  
5675 C CG1 A ILE   B 106 ? 0.4006 0.3286 0.3618 -0.0168 0.1327  0.0126  106 ILE   B CG1 
5676 C CG1 B ILE   B 106 ? 0.4013 0.3083 0.3598 -0.0256 0.1639  0.0245  106 ILE   B CG1 
5677 C CG2 A ILE   B 106 ? 0.3965 0.3332 0.3707 -0.0157 0.1382  0.0113  106 ILE   B CG2 
5678 C CG2 B ILE   B 106 ? 0.3933 0.3115 0.3635 -0.0297 0.1794  0.0268  106 ILE   B CG2 
5679 C CD1 A ILE   B 106 ? 0.4029 0.3277 0.3565 -0.0166 0.1307  0.0140  106 ILE   B CD1 
5680 C CD1 B ILE   B 106 ? 0.4063 0.3097 0.3591 -0.0220 0.1590  0.0253  106 ILE   B CD1 
5703 N N   A GLN   B 107 ? 0.3396 0.3293 0.3589 -0.0046 0.1331  0.0069  107 GLN   B N   
5704 N N   B GLN   B 107 ? 0.3218 0.3138 0.3459 -0.0178 0.1742  0.0155  107 GLN   B N   
5705 C CA  A GLN   B 107 ? 0.3188 0.3309 0.3657 -0.0055 0.1242  0.0111  107 GLN   B CA  
5706 C CA  B GLN   B 107 ? 0.3016 0.3240 0.3576 -0.0202 0.1635  0.0207  107 GLN   B CA  
5707 C C   A GLN   B 107 ? 0.2898 0.3031 0.3358 0.0072  0.1174  0.0078  107 GLN   B C   
5708 C C   B GLN   B 107 ? 0.2782 0.2988 0.3310 -0.0018 0.1405  0.0137  107 GLN   B C   
5709 O O   A GLN   B 107 ? 0.2845 0.3030 0.3557 0.0164  0.0956  -0.0024 107 GLN   B O   
5710 O O   B GLN   B 107 ? 0.2693 0.3008 0.3652 0.0123  0.1121  -0.0037 107 GLN   B O   
5711 C CB  A GLN   B 107 ? 0.3361 0.3618 0.4130 -0.0125 0.1070  0.0132  107 GLN   B CB  
5712 C CB  B GLN   B 107 ? 0.3246 0.3630 0.4124 -0.0269 0.1415  0.0219  107 GLN   B CB  
5713 C CG  A GLN   B 107 ? 0.3556 0.3857 0.4649 -0.0127 0.0813  0.0104  107 GLN   B CG  
5714 C CG  B GLN   B 107 ? 0.3533 0.3944 0.4764 -0.0229 0.1011  0.0147  107 GLN   B CG  
5715 C CD  A GLN   B 107 ? 0.3687 0.4010 0.5052 -0.0144 0.0628  0.0117  107 GLN   B CD  
5716 C CD  B GLN   B 107 ? 0.3721 0.4140 0.5239 -0.0221 0.0720  0.0124  107 GLN   B CD  
5717 O OE1 A GLN   B 107 ? 0.3704 0.4059 0.5187 -0.0126 0.0620  0.0093  107 GLN   B OE1 
5718 O OE1 B GLN   B 107 ? 0.3749 0.4204 0.5406 -0.0202 0.0698  0.0102  107 GLN   B OE1 
5719 N NE2 A GLN   B 107 ? 0.3777 0.4060 0.5201 -0.0147 0.0534  0.0157  107 GLN   B NE2 
5720 N NE2 B GLN   B 107 ? 0.3842 0.4218 0.5407 -0.0212 0.0577  0.0141  107 GLN   B NE2 
5737 N N   . LEU   B 108 ? 0.2636 0.2781 0.2935 0.0208  0.1221  0.0118  108 LEU   B N   
5738 C CA  . LEU   B 108 ? 0.2417 0.2523 0.2420 0.0305  0.0858  0.0250  108 LEU   B CA  
5739 C C   . LEU   B 108 ? 0.2062 0.2033 0.2237 0.0315  0.0508  0.0272  108 LEU   B C   
5740 O O   . LEU   B 108 ? 0.1963 0.1885 0.2052 0.0306  0.0395  0.0190  108 LEU   B O   
5741 C CB  . LEU   B 108 ? 0.2583 0.2806 0.2104 0.0314  0.0951  0.0365  108 LEU   B CB  
5742 C CG  . LEU   B 108 ? 0.2704 0.3162 0.2276 0.0367  0.0798  0.0213  108 LEU   B CG  
5743 C CD1 . LEU   B 108 ? 0.2873 0.3365 0.2159 0.0304  0.0721  0.0178  108 LEU   B CD1 
5744 C CD2 . LEU   B 108 ? 0.2740 0.3229 0.2360 0.0477  0.0622  -0.0053 108 LEU   B CD2 
5757 N N   . LEU   B 109 ? 0.1853 0.1762 0.2154 0.0185  0.0512  0.0271  109 LEU   B N   
5758 C CA  . LEU   B 109 ? 0.1635 0.1541 0.2221 0.0128  0.0490  0.0262  109 LEU   B CA  
5759 C C   . LEU   B 109 ? 0.1554 0.1342 0.2273 0.0083  0.0451  0.0232  109 LEU   B C   
5760 O O   . LEU   B 109 ? 0.1514 0.1328 0.2264 0.0094  0.0474  0.0350  109 LEU   B O   
5761 C CB  . LEU   B 109 ? 0.1682 0.1382 0.2281 0.0066  0.0408  0.0446  109 LEU   B CB  
5762 C CG  . LEU   B 109 ? 0.1672 0.1341 0.2303 0.0009  0.0265  0.0275  109 LEU   B CG  
5763 C CD1 . LEU   B 109 ? 0.1666 0.1467 0.2236 0.0065  0.0305  0.0260  109 LEU   B CD1 
5764 C CD2 . LEU   B 109 ? 0.1757 0.1421 0.2406 0.0007  0.0200  0.0276  109 LEU   B CD2 
5776 N N   . LYS   B 110 ? 0.1509 0.1301 0.2124 -0.0044 0.0398  0.0201  110 LYS   B N   
5777 C CA  . LYS   B 110 ? 0.1477 0.1289 0.2207 -0.0018 0.0364  0.0181  110 LYS   B CA  
5778 C C   . LYS   B 110 ? 0.1386 0.1274 0.2036 0.0015  0.0436  0.0133  110 LYS   B C   
5779 O O   . LYS   B 110 ? 0.1389 0.1356 0.1946 -0.0073 0.0235  0.0046  110 LYS   B O   
5780 C CB  . LYS   B 110 ? 0.1549 0.1358 0.2355 -0.0044 0.0329  0.0066  110 LYS   B CB  
5781 C CG  . LYS   B 110 ? 0.1506 0.1347 0.2395 -0.0106 0.0211  0.0224  110 LYS   B CG  
5782 C CD  . LYS   B 110 ? 0.1525 0.1362 0.2604 -0.0046 0.0236  0.0184  110 LYS   B CD  
5783 C CE  . LYS   B 110 ? 0.1523 0.1522 0.2819 0.0029  0.0200  0.0076  110 LYS   B CE  
5784 N NZ  . LYS   B 110 ? 0.1447 0.1572 0.2775 0.0047  0.0110  0.0018  110 LYS   B NZ  
5798 N N   . SER   B 111 ? 0.1468 0.1273 0.2221 0.0022  0.0311  0.0136  111 SER   B N   
5799 C CA  . SER   B 111 ? 0.1496 0.1354 0.2045 0.0083  0.0431  0.0125  111 SER   B CA  
5800 C C   . SER   B 111 ? 0.1489 0.1246 0.1978 -0.0004 0.0226  0.0088  111 SER   B C   
5801 O O   . SER   B 111 ? 0.1476 0.1341 0.1990 -0.0038 0.0261  0.0082  111 SER   B O   
5802 C CB  . SER   B 111 ? 0.1675 0.1650 0.2158 0.0108  0.0587  0.0218  111 SER   B CB  
5803 O OG  . SER   B 111 ? 0.1911 0.1892 0.2170 0.0154  0.0597  0.0288  111 SER   B OG  
5809 N N   . ALA   B 112 ? 0.1437 0.1302 0.1950 0.0057  0.0287  0.0180  112 ALA   B N   
5810 C CA  . ALA   B 112 ? 0.1389 0.1402 0.1751 0.0056  0.0201  0.0063  112 ALA   B CA  
5811 C C   . ALA   B 112 ? 0.1252 0.1373 0.1782 0.0024  0.0192  0.0089  112 ALA   B C   
5812 O O   . ALA   B 112 ? 0.1345 0.1351 0.1718 -0.0009 0.0145  -0.0014 112 ALA   B O   
5813 C CB  . ALA   B 112 ? 0.1500 0.1409 0.1958 0.0097  0.0087  0.0224  112 ALA   B CB  
5819 N N   . TYR   B 113 ? 0.1304 0.1239 0.1780 0.0020  0.0125  0.0180  113 TYR   B N   
5820 C CA  . TYR   B 113 ? 0.1247 0.1199 0.1705 0.0012  0.0229  0.0052  113 TYR   B CA  
5821 C C   . TYR   B 113 ? 0.1283 0.1090 0.1649 -0.0062 0.0205  0.0087  113 TYR   B C   
5822 O O   . TYR   B 113 ? 0.1356 0.1181 0.1603 -0.0054 0.0084  -0.0039 113 TYR   B O   
5823 C CB  . TYR   B 113 ? 0.1353 0.1128 0.1885 0.0006  0.0226  0.0109  113 TYR   B CB  
5824 C CG  . TYR   B 113 ? 0.1377 0.1193 0.1883 -0.0004 0.0136  0.0163  113 TYR   B CG  
5825 C CD1 . TYR   B 113 ? 0.1392 0.1210 0.2025 -0.0030 0.0208  0.0217  113 TYR   B CD1 
5826 C CD2 . TYR   B 113 ? 0.1458 0.1237 0.1894 -0.0025 0.0121  0.0182  113 TYR   B CD2 
5827 C CE1 . TYR   B 113 ? 0.1405 0.1265 0.1903 -0.0026 0.0196  0.0162  113 TYR   B CE1 
5828 C CE2 . TYR   B 113 ? 0.1472 0.1150 0.2051 0.0037  0.0130  0.0232  113 TYR   B CE2 
5829 C CZ  . TYR   B 113 ? 0.1429 0.1229 0.2150 0.0090  0.0173  0.0059  113 TYR   B CZ  
5830 O OH  . TYR   B 113 ? 0.1463 0.1197 0.2490 0.0121  0.0203  0.0047  113 TYR   B OH  
5840 N N   . GLU   B 114 ? 0.1236 0.1158 0.1831 -0.0021 0.0169  0.0113  114 GLU   B N   
5841 C CA  . GLU   B 114 ? 0.1256 0.1214 0.1769 0.0014  0.0084  0.0062  114 GLU   B CA  
5842 C C   . GLU   B 114 ? 0.1240 0.1232 0.1684 -0.0003 0.0112  0.0052  114 GLU   B C   
5843 O O   . GLU   B 114 ? 0.1220 0.1239 0.1790 0.0037  0.0005  0.0165  114 GLU   B O   
5844 C CB  . GLU   B 114 ? 0.1303 0.1224 0.1902 -0.0018 0.0178  0.0002  114 GLU   B CB  
5845 C CG  . GLU   B 114 ? 0.1340 0.1222 0.1881 -0.0024 0.0116  0.0018  114 GLU   B CG  
5846 C CD  . GLU   B 114 ? 0.1303 0.1263 0.2018 -0.0070 0.0100  0.0041  114 GLU   B CD  
5847 O OE1 . GLU   B 114 ? 0.1244 0.1389 0.1928 -0.0048 0.0166  0.0095  114 GLU   B OE1 
5848 O OE2 . GLU   B 114 ? 0.1320 0.1423 0.2115 -0.0177 0.0159  -0.0035 114 GLU   B OE2 
5855 N N   . ASN   B 115 ? 0.1278 0.1236 0.1655 -0.0082 0.0047  0.0027  115 ASN   B N   
5856 C CA  . ASN   B 115 ? 0.1283 0.1278 0.1492 -0.0098 0.0032  0.0053  115 ASN   B CA  
5857 C C   . ASN   B 115 ? 0.1225 0.1237 0.1571 -0.0096 -0.0011 0.0007  115 ASN   B C   
5858 O O   . ASN   B 115 ? 0.1341 0.1235 0.1642 -0.0110 0.0041  0.0048  115 ASN   B O   
5859 C CB  . ASN   B 115 ? 0.1402 0.1349 0.1607 -0.0131 0.0014  0.0022  115 ASN   B CB  
5860 C CG  . ASN   B 115 ? 0.1441 0.1475 0.1532 0.0044  0.0052  0.0016  115 ASN   B CG  
5861 O OD1 . ASN   B 115 ? 0.1813 0.1546 0.1895 -0.0015 0.0107  -0.0121 115 ASN   B OD1 
5862 N ND2 . ASN   B 115 ? 0.1428 0.1553 0.1530 -0.0048 0.0038  0.0156  115 ASN   B ND2 
5869 N N   . PHE   B 116 ? 0.1302 0.1182 0.1437 -0.0045 -0.0015 -0.0028 116 PHE   B N   
5870 C CA  . PHE   B 116 ? 0.1315 0.1195 0.1468 -0.0056 -0.0049 0.0038  116 PHE   B CA  
5871 C C   . PHE   B 116 ? 0.1294 0.1112 0.1465 -0.0115 -0.0009 0.0033  116 PHE   B C   
5872 O O   . PHE   B 116 ? 0.1303 0.1228 0.1690 -0.0057 -0.0052 0.0047  116 PHE   B O   
5873 C CB  . PHE   B 116 ? 0.1301 0.1129 0.1465 -0.0021 -0.0074 0.0026  116 PHE   B CB  
5874 C CG  . PHE   B 116 ? 0.1158 0.1189 0.1587 -0.0116 -0.0010 0.0017  116 PHE   B CG  
5875 C CD1 . PHE   B 116 ? 0.1278 0.1203 0.1726 -0.0033 -0.0030 -0.0002 116 PHE   B CD1 
5876 C CD2 . PHE   B 116 ? 0.1259 0.1300 0.1488 -0.0123 -0.0039 -0.0042 116 PHE   B CD2 
5877 C CE1 . PHE   B 116 ? 0.1349 0.1282 0.1676 -0.0016 -0.0140 0.0005  116 PHE   B CE1 
5878 C CE2 . PHE   B 116 ? 0.1277 0.1265 0.1608 -0.0016 -0.0033 0.0050  116 PHE   B CE2 
5879 C CZ  . PHE   B 116 ? 0.1223 0.1326 0.1545 0.0006  -0.0093 0.0111  116 PHE   B CZ  
5889 N N   . ASN   B 117 ? 0.1363 0.1109 0.1553 -0.0083 -0.0141 0.0062  117 ASN   B N   
5890 C CA  . ASN   B 117 ? 0.1462 0.1228 0.1640 0.0023  -0.0184 0.0024  117 ASN   B CA  
5891 C C   . ASN   B 117 ? 0.1399 0.1207 0.1807 0.0010  -0.0223 0.0122  117 ASN   B C   
5892 O O   . ASN   B 117 ? 0.1532 0.1221 0.2087 -0.0039 -0.0425 0.0152  117 ASN   B O   
5893 C CB  . ASN   B 117 ? 0.1425 0.1268 0.1675 -0.0037 -0.0134 0.0025  117 ASN   B CB  
5894 C CG  . ASN   B 117 ? 0.1393 0.1248 0.1838 0.0033  -0.0134 -0.0021 117 ASN   B CG  
5895 O OD1 . ASN   B 117 ? 0.1555 0.1298 0.1891 -0.0116 -0.0075 -0.0111 117 ASN   B OD1 
5896 N ND2 . ASN   B 117 ? 0.1426 0.1278 0.1779 -0.0027 -0.0048 0.0004  117 ASN   B ND2 
5903 N N   . GLN   B 118 ? 0.1407 0.1089 0.1723 -0.0044 -0.0221 0.0054  118 GLN   B N   
5904 C CA  . GLN   B 118 ? 0.1503 0.1165 0.1800 0.0010  -0.0166 0.0018  118 GLN   B CA  
5905 C C   . GLN   B 118 ? 0.1486 0.1215 0.1839 -0.0033 -0.0100 -0.0016 118 GLN   B C   
5906 O O   . GLN   B 118 ? 0.1626 0.1244 0.2357 -0.0106 -0.0052 0.0095  118 GLN   B O   
5907 C CB  . GLN   B 118 ? 0.1530 0.1283 0.1786 0.0057  -0.0173 -0.0063 118 GLN   B CB  
5908 C CG  . GLN   B 118 ? 0.1622 0.1249 0.1860 0.0050  -0.0162 -0.0093 118 GLN   B CG  
5909 C CD  . GLN   B 118 ? 0.1711 0.1172 0.1790 0.0047  -0.0147 -0.0030 118 GLN   B CD  
5910 O OE1 . GLN   B 118 ? 0.1739 0.1238 0.2251 0.0079  0.0052  0.0083  118 GLN   B OE1 
5911 N NE2 . GLN   B 118 ? 0.1810 0.1129 0.1898 0.0062  -0.0246 0.0027  118 GLN   B NE2 
5920 N N   . HIS   B 119 ? 0.1539 0.1348 0.1325 -0.0066 -0.0106 0.0101  119 HIS   B N   
5921 C CA  . HIS   B 119 ? 0.1661 0.1411 0.1280 -0.0025 -0.0223 0.0093  119 HIS   B CA  
5922 C C   . HIS   B 119 ? 0.1645 0.1337 0.1400 -0.0049 -0.0321 0.0184  119 HIS   B C   
5923 O O   . HIS   B 119 ? 0.1687 0.1370 0.1659 -0.0274 -0.0169 0.0135  119 HIS   B O   
5924 C CB  . HIS   B 119 ? 0.1651 0.1494 0.1505 0.0059  -0.0232 0.0038  119 HIS   B CB  
5925 C CG  . HIS   B 119 ? 0.1663 0.1745 0.1883 0.0062  -0.0578 -0.0182 119 HIS   B CG  
5926 N ND1 . HIS   B 119 ? 0.1706 0.1891 0.2166 -0.0000 -0.0507 -0.0433 119 HIS   B ND1 
5927 C CD2 . HIS   B 119 ? 0.1863 0.1874 0.1934 0.0426  -0.0588 -0.0267 119 HIS   B CD2 
5928 C CE1 . HIS   B 119 ? 0.1897 0.1981 0.2207 0.0189  -0.0657 -0.0491 119 HIS   B CE1 
5929 N NE2 . HIS   B 119 ? 0.2048 0.2103 0.1986 0.0350  -0.0614 -0.0370 119 HIS   B NE2 
5937 N N   . GLU   B 120 ? 0.1820 0.1402 0.1593 -0.0125 -0.0387 0.0190  120 GLU   B N   
5938 C CA  . GLU   B 120 ? 0.2111 0.1494 0.1640 -0.0031 -0.0531 0.0346  120 GLU   B CA  
5939 C C   . GLU   B 120 ? 0.1902 0.1459 0.1491 -0.0172 -0.0331 0.0214  120 GLU   B C   
5940 O O   . GLU   B 120 ? 0.1765 0.1623 0.1509 -0.0171 -0.0367 0.0088  120 GLU   B O   
5941 C CB  . GLU   B 120 ? 0.2678 0.1816 0.2331 0.0141  -0.0830 0.0406  120 GLU   B CB  
5942 C CG  . GLU   B 120 ? 0.3178 0.2354 0.3339 0.0206  -0.0923 0.0567  120 GLU   B CG  
5943 C CD  . GLU   B 120 ? 0.3548 0.2984 0.4318 0.0163  -0.0893 0.0659  120 GLU   B CD  
5944 O OE1 . GLU   B 120 ? 0.3881 0.3210 0.4712 0.0097  -0.0757 0.0789  120 GLU   B OE1 
5945 O OE2 . GLU   B 120 ? 0.3776 0.3286 0.4960 0.0145  -0.0860 0.0536  120 GLU   B OE2 
5952 N N   . VAL   B 121 ? 0.1799 0.1387 0.1412 -0.0270 -0.0252 0.0213  121 VAL   B N   
5953 C CA  . VAL   B 121 ? 0.1691 0.1485 0.1295 -0.0186 -0.0250 0.0154  121 VAL   B CA  
5954 C C   . VAL   B 121 ? 0.1621 0.1516 0.1338 -0.0291 -0.0233 0.0191  121 VAL   B C   
5955 O O   . VAL   B 121 ? 0.1661 0.1476 0.1497 -0.0377 -0.0228 0.0173  121 VAL   B O   
5956 C CB  . VAL   B 121 ? 0.1878 0.1920 0.1583 -0.0047 -0.0265 0.0213  121 VAL   B CB  
5957 C CG1 . VAL   B 121 ? 0.1885 0.1997 0.1997 -0.0153 -0.0018 0.0151  121 VAL   B CG1 
5958 C CG2 . VAL   B 121 ? 0.2164 0.2154 0.1629 0.0010  -0.0187 0.0114  121 VAL   B CG2 
5968 N N   . LEU   B 122 ? 0.1523 0.1372 0.1403 -0.0179 -0.0239 0.0166  122 LEU   B N   
5969 C CA  . LEU   B 122 ? 0.1458 0.1484 0.1146 -0.0211 -0.0253 0.0145  122 LEU   B CA  
5970 C C   . LEU   B 122 ? 0.1438 0.1360 0.1290 -0.0236 -0.0219 0.0147  122 LEU   B C   
5971 O O   . LEU   B 122 ? 0.1536 0.1441 0.1683 -0.0328 -0.0342 0.0001  122 LEU   B O   
5972 C CB  . LEU   B 122 ? 0.1638 0.1663 0.1520 -0.0032 -0.0233 0.0278  122 LEU   B CB  
5973 C CG  . LEU   B 122 ? 0.1532 0.1757 0.1635 -0.0140 -0.0077 0.0175  122 LEU   B CG  
5974 C CD1 . LEU   B 122 ? 0.1567 0.1882 0.1503 -0.0213 -0.0207 0.0106  122 LEU   B CD1 
5975 C CD2 . LEU   B 122 ? 0.1527 0.1836 0.1215 -0.0119 -0.0125 0.0096  122 LEU   B CD2 
5987 N N   . LEU   B 123 ? 0.1494 0.1242 0.1132 -0.0316 -0.0187 0.0115  123 LEU   B N   
5988 C CA  . LEU   B 123 ? 0.1500 0.1261 0.1253 -0.0286 -0.0232 0.0102  123 LEU   B CA  
5989 C C   . LEU   B 123 ? 0.1415 0.1228 0.1193 -0.0235 -0.0157 0.0037  123 LEU   B C   
5990 O O   . LEU   B 123 ? 0.1558 0.1312 0.1190 -0.0334 -0.0142 -0.0000 123 LEU   B O   
5991 C CB  . LEU   B 123 ? 0.1539 0.1377 0.1366 -0.0236 -0.0134 0.0065  123 LEU   B CB  
5992 C CG  . LEU   B 123 ? 0.1479 0.1389 0.1514 -0.0228 -0.0033 0.0067  123 LEU   B CG  
5993 C CD1 . LEU   B 123 ? 0.1591 0.1437 0.1613 -0.0188 -0.0017 -0.0180 123 LEU   B CD1 
5994 C CD2 . LEU   B 123 ? 0.1664 0.1419 0.1739 -0.0200 0.0015  0.0079  123 LEU   B CD2 
6006 N N   . ALA   B 124 ? 0.1390 0.1171 0.1147 -0.0184 -0.0051 -0.0017 124 ALA   B N   
6007 C CA  . ALA   B 124 ? 0.1284 0.1214 0.1425 -0.0178 -0.0084 -0.0066 124 ALA   B CA  
6008 C C   . ALA   B 124 ? 0.1268 0.1184 0.1371 -0.0179 -0.0097 0.0008  124 ALA   B C   
6009 O O   . ALA   B 124 ? 0.1406 0.1218 0.1399 -0.0190 -0.0132 -0.0019 124 ALA   B O   
6010 C CB  . ALA   B 124 ? 0.1338 0.1304 0.1523 -0.0052 0.0074  0.0020  124 ALA   B CB  
6016 N N   . PRO   B 125 ? 0.1413 0.1279 0.1259 -0.0170 -0.0131 0.0099  125 PRO   B N   
6017 C CA  . PRO   B 125 ? 0.1521 0.1238 0.1347 -0.0198 -0.0096 0.0128  125 PRO   B CA  
6018 C C   . PRO   B 125 ? 0.1473 0.1198 0.1581 -0.0149 -0.0018 0.0098  125 PRO   B C   
6019 O O   . PRO   B 125 ? 0.1469 0.1208 0.1670 -0.0042 0.0046  0.0135  125 PRO   B O   
6020 C CB  . PRO   B 125 ? 0.1579 0.1457 0.1451 -0.0197 -0.0180 0.0296  125 PRO   B CB  
6021 C CG  . PRO   B 125 ? 0.1583 0.1508 0.1375 -0.0266 -0.0218 0.0172  125 PRO   B CG  
6022 C CD  . PRO   B 125 ? 0.1535 0.1381 0.1224 -0.0288 -0.0105 0.0095  125 PRO   B CD  
6030 N N   . LEU   B 126 ? 0.1481 0.1153 0.1947 -0.0149 0.0129  0.0189  126 LEU   B N   
6031 C CA  . LEU   B 126 ? 0.1601 0.1164 0.1922 -0.0078 0.0305  0.0216  126 LEU   B CA  
6032 C C   . LEU   B 126 ? 0.1536 0.1328 0.1870 0.0039  0.0236  0.0231  126 LEU   B C   
6033 O O   . LEU   B 126 ? 0.1700 0.1642 0.2183 0.0231  -0.0042 -0.0095 126 LEU   B O   
6034 C CB  . LEU   B 126 ? 0.1842 0.1322 0.2221 -0.0153 0.0428  0.0121  126 LEU   B CB  
6035 C CG  . LEU   B 126 ? 0.1937 0.1426 0.2298 -0.0253 0.0353  -0.0056 126 LEU   B CG  
6036 C CD1 . LEU   B 126 ? 0.2044 0.1437 0.2886 -0.0203 0.0289  -0.0039 126 LEU   B CD1 
6037 C CD2 . LEU   B 126 ? 0.1917 0.1583 0.2213 -0.0345 0.0263  -0.0213 126 LEU   B CD2 
6049 N N   . LEU   B 127 ? 0.1551 0.1239 0.1959 0.0034  0.0358  0.0082  127 LEU   B N   
6050 C CA  . LEU   B 127 ? 0.1573 0.1384 0.2009 -0.0039 0.0337  0.0192  127 LEU   B CA  
6051 C C   . LEU   B 127 ? 0.1425 0.1297 0.2148 -0.0009 0.0356  0.0227  127 LEU   B C   
6052 O O   . LEU   B 127 ? 0.1505 0.1373 0.2186 -0.0134 0.0210  0.0231  127 LEU   B O   
6053 C CB  . LEU   B 127 ? 0.1679 0.1379 0.2162 0.0012  0.0227  0.0211  127 LEU   B CB  
6054 C CG  . LEU   B 127 ? 0.1784 0.1300 0.2177 0.0030  0.0352  0.0210  127 LEU   B CG  
6055 C CD1 . LEU   B 127 ? 0.1856 0.1282 0.2310 0.0145  0.0322  0.0233  127 LEU   B CD1 
6056 C CD2 . LEU   B 127 ? 0.1856 0.1411 0.2280 -0.0111 0.0429  0.0231  127 LEU   B CD2 
6068 N N   . SER   B 128 ? 0.1517 0.1286 0.2132 0.0010  0.0125  0.0206  128 SER   B N   
6069 C CA  . SER   B 128 ? 0.1615 0.1419 0.2058 0.0090  -0.0042 0.0306  128 SER   B CA  
6070 C C   . SER   B 128 ? 0.1784 0.1445 0.2383 0.0065  -0.0203 0.0238  128 SER   B C   
6071 O O   . SER   B 128 ? 0.2021 0.1480 0.2733 0.0106  -0.0240 0.0430  128 SER   B O   
6072 C CB  . SER   B 128 ? 0.1668 0.1461 0.2013 0.0050  0.0058  0.0371  128 SER   B CB  
6073 O OG  . SER   B 128 ? 0.1764 0.1596 0.1959 0.0133  0.0170  0.0346  128 SER   B OG  
6079 N N   . ALA   B 129 ? 0.1889 0.1561 0.2566 0.0305  -0.0030 0.0096  129 ALA   B N   
6080 C CA  . ALA   B 129 ? 0.2004 0.1682 0.2698 0.0358  -0.0016 -0.0041 129 ALA   B CA  
6081 C C   . ALA   B 129 ? 0.1877 0.1562 0.2548 0.0272  0.0102  0.0008  129 ALA   B C   
6082 O O   . ALA   B 129 ? 0.1784 0.1524 0.2497 0.0220  0.0015  0.0087  129 ALA   B O   
6083 C CB  . ALA   B 129 ? 0.2226 0.1880 0.2917 0.0389  0.0095  -0.0180 129 ALA   B CB  
6089 N N   . GLY   B 130 ? 0.1899 0.1540 0.2551 0.0308  0.0089  0.0007  130 GLY   B N   
6090 C CA  . GLY   B 130 ? 0.1970 0.1576 0.2775 0.0226  0.0312  0.0005  130 GLY   B CA  
6091 C C   . GLY   B 130 ? 0.1998 0.1562 0.2727 0.0155  0.0217  0.0180  130 GLY   B C   
6092 O O   . GLY   B 130 ? 0.2060 0.1678 0.2836 0.0189  0.0128  0.0254  130 GLY   B O   
6096 N N   . ILE   B 131 ? 0.1944 0.1740 0.2771 0.0333  0.0276  0.0164  131 ILE   B N   
6097 C CA  . ILE   B 131 ? 0.2188 0.1895 0.2776 0.0257  0.0162  0.0267  131 ILE   B CA  
6098 C C   . ILE   B 131 ? 0.2307 0.1835 0.2457 0.0250  0.0162  0.0320  131 ILE   B C   
6099 O O   . ILE   B 131 ? 0.2518 0.2020 0.2458 0.0254  -0.0006 0.0325  131 ILE   B O   
6100 C CB  . ILE   B 131 ? 0.2243 0.2150 0.3138 0.0201  0.0035  0.0284  131 ILE   B CB  
6101 C CG1 . ILE   B 131 ? 0.2354 0.2266 0.3207 -0.0086 -0.0007 0.0373  131 ILE   B CG1 
6102 C CG2 . ILE   B 131 ? 0.2240 0.2315 0.3378 0.0330  0.0027  0.0149  131 ILE   B CG2 
6103 C CD1 . ILE   B 131 ? 0.2465 0.2437 0.3374 -0.0248 -0.0128 0.0429  131 ILE   B CD1 
6115 N N   . PHE   B 132 ? 0.2201 0.1629 0.2378 0.0229  0.0440  0.0307  132 PHE   B N   
6116 C CA  . PHE   B 132 ? 0.2226 0.1769 0.2384 0.0125  0.0659  0.0268  132 PHE   B CA  
6117 C C   . PHE   B 132 ? 0.2327 0.1948 0.2636 0.0182  0.0752  0.0259  132 PHE   B C   
6118 O O   . PHE   B 132 ? 0.2498 0.2162 0.2811 0.0076  0.0803  0.0397  132 PHE   B O   
6119 C CB  . PHE   B 132 ? 0.2090 0.1659 0.2176 0.0123  0.0640  0.0289  132 PHE   B CB  
6120 C CG  . PHE   B 132 ? 0.1964 0.1675 0.2067 0.0160  0.0445  0.0295  132 PHE   B CG  
6121 C CD1 . PHE   B 132 ? 0.2029 0.1672 0.2484 0.0159  0.0273  0.0215  132 PHE   B CD1 
6122 C CD2 . PHE   B 132 ? 0.1896 0.1741 0.1728 0.0241  0.0316  0.0356  132 PHE   B CD2 
6123 C CE1 . PHE   B 132 ? 0.2044 0.1701 0.2586 0.0060  0.0079  0.0270  132 PHE   B CE1 
6124 C CE2 . PHE   B 132 ? 0.1950 0.1805 0.1890 0.0186  0.0185  0.0280  132 PHE   B CE2 
6125 C CZ  . PHE   B 132 ? 0.2005 0.1747 0.2368 0.0123  -0.0094 0.0360  132 PHE   B CZ  
6135 N N   . GLY   B 133 ? 0.2345 0.1835 0.2584 0.0129  0.0602  0.0456  133 GLY   B N   
6136 C CA  . GLY   B 133 ? 0.2385 0.1913 0.2742 -0.0109 0.0609  0.0606  133 GLY   B CA  
6137 C C   . GLY   B 133 ? 0.2452 0.1970 0.2829 -0.0304 0.0586  0.0695  133 GLY   B C   
6138 O O   . GLY   B 133 ? 0.2645 0.2189 0.3260 -0.0496 0.0418  0.0706  133 GLY   B O   
6142 N N   . ALA   B 134 ? 0.2336 0.1848 0.2587 -0.0259 0.0589  0.0410  134 ALA   B N   
6143 C CA  . ALA   B 134 ? 0.2231 0.1798 0.2855 -0.0192 0.0548  0.0244  134 ALA   B CA  
6144 C C   . ALA   B 134 ? 0.2268 0.1665 0.2780 -0.0095 0.0428  0.0371  134 ALA   B C   
6145 O O   . ALA   B 134 ? 0.2265 0.1930 0.2925 0.0019  0.0306  0.0296  134 ALA   B O   
6146 C CB  . ALA   B 134 ? 0.2161 0.1871 0.2946 -0.0139 0.0432  0.0163  134 ALA   B CB  
6152 N N   . ASP   B 135 ? 0.2477 0.1666 0.2726 -0.0042 0.0309  0.0446  135 ASP   B N   
6153 C CA  . ASP   B 135 ? 0.2630 0.1574 0.3022 -0.0018 0.0242  0.0462  135 ASP   B CA  
6154 C C   . ASP   B 135 ? 0.2408 0.1523 0.2753 0.0030  0.0155  0.0438  135 ASP   B C   
6155 O O   . ASP   B 135 ? 0.2301 0.1497 0.3067 -0.0044 0.0171  0.0476  135 ASP   B O   
6156 C CB  . ASP   B 135 ? 0.2954 0.1682 0.3220 -0.0185 0.0235  0.0622  135 ASP   B CB  
6157 C CG  . ASP   B 135 ? 0.3209 0.1747 0.3641 -0.0423 0.0215  0.0509  135 ASP   B CG  
6158 O OD1 . ASP   B 135 ? 0.3245 0.1590 0.3688 -0.0270 0.0064  0.0452  135 ASP   B OD1 
6159 O OD2 . ASP   B 135 ? 0.3454 0.2142 0.4243 -0.0585 0.0303  0.0308  135 ASP   B OD2 
6164 N N   . PRO   B 136 ? 0.2271 0.1569 0.2864 0.0163  -0.0070 0.0298  136 PRO   B N   
6165 C CA  . PRO   B 136 ? 0.2039 0.1485 0.2972 0.0206  -0.0003 0.0110  136 PRO   B CA  
6166 C C   . PRO   B 136 ? 0.1923 0.1320 0.2991 0.0177  0.0089  0.0071  136 PRO   B C   
6167 O O   . PRO   B 136 ? 0.1653 0.1308 0.2789 0.0069  0.0045  0.0098  136 PRO   B O   
6168 C CB  . PRO   B 136 ? 0.2077 0.1717 0.3092 0.0323  -0.0051 0.0023  136 PRO   B CB  
6169 C CG  . PRO   B 136 ? 0.2284 0.1788 0.3282 0.0313  0.0058  0.0014  136 PRO   B CG  
6170 C CD  . PRO   B 136 ? 0.2359 0.1719 0.3145 0.0361  0.0027  0.0225  136 PRO   B CD  
6178 N N   . ILE   B 137 ? 0.2015 0.1232 0.3031 0.0152  0.0087  0.0128  137 ILE   B N   
6179 C CA  . ILE   B 137 ? 0.2011 0.1216 0.3158 0.0056  0.0097  0.0029  137 ILE   B CA  
6180 C C   . ILE   B 137 ? 0.1889 0.1247 0.3039 -0.0071 0.0262  0.0156  137 ILE   B C   
6181 O O   . ILE   B 137 ? 0.1881 0.1276 0.2888 -0.0021 0.0252  0.0125  137 ILE   B O   
6182 C CB  . ILE   B 137 ? 0.2342 0.1224 0.3595 0.0020  0.0075  0.0020  137 ILE   B CB  
6183 C CG1 . ILE   B 137 ? 0.2504 0.1437 0.4067 0.0091  0.0088  -0.0202 137 ILE   B CG1 
6184 C CG2 . ILE   B 137 ? 0.2454 0.1249 0.3812 -0.0240 0.0052  0.0176  137 ILE   B CG2 
6185 C CD1 . ILE   B 137 ? 0.2670 0.1860 0.4389 0.0194  -0.0052 -0.0100 137 ILE   B CD1 
6197 N N   . HIS   B 138 ? 0.1970 0.1283 0.2943 -0.0028 0.0386  0.0227  138 HIS   B N   
6198 C CA  . HIS   B 138 ? 0.2087 0.1375 0.2915 -0.0001 0.0457  0.0263  138 HIS   B CA  
6199 C C   . HIS   B 138 ? 0.1894 0.1336 0.2780 -0.0082 0.0397  0.0392  138 HIS   B C   
6200 O O   . HIS   B 138 ? 0.1834 0.1493 0.2894 0.0028  0.0378  0.0418  138 HIS   B O   
6201 C CB  . HIS   B 138 ? 0.2403 0.1515 0.3074 -0.0121 0.0671  0.0340  138 HIS   B CB  
6202 C CG  . HIS   B 138 ? 0.2613 0.1725 0.3191 -0.0115 0.0922  0.0493  138 HIS   B CG  
6203 N ND1 . HIS   B 138 ? 0.2703 0.1910 0.3556 -0.0073 0.1040  0.0400  138 HIS   B ND1 
6204 C CD2 . HIS   B 138 ? 0.2781 0.1854 0.3127 -0.0190 0.0927  0.0403  138 HIS   B CD2 
6205 C CE1 . HIS   B 138 ? 0.2776 0.1945 0.3507 -0.0062 0.1015  0.0351  138 HIS   B CE1 
6206 N NE2 . HIS   B 138 ? 0.2830 0.1792 0.3266 -0.0061 0.1039  0.0310  138 HIS   B NE2 
6214 N N   . SER   B 139 ? 0.1869 0.1133 0.2687 0.0009  0.0363  0.0229  139 SER   B N   
6215 C CA  . SER   B 139 ? 0.1782 0.1189 0.2538 -0.0004 0.0270  0.0109  139 SER   B CA  
6216 C C   . SER   B 139 ? 0.1486 0.1213 0.2334 -0.0026 0.0220  0.0117  139 SER   B C   
6217 O O   . SER   B 139 ? 0.1491 0.1260 0.2448 -0.0033 0.0078  0.0104  139 SER   B O   
6218 C CB  . SER   B 139 ? 0.1785 0.1281 0.2431 -0.0019 0.0139  0.0086  139 SER   B CB  
6219 O OG  . SER   B 139 ? 0.1764 0.1294 0.2489 -0.0050 -0.0023 0.0262  139 SER   B OG  
6225 N N   . LEU   B 140 ? 0.1520 0.1131 0.2249 -0.0001 0.0295  0.0008  140 LEU   B N   
6226 C CA  . LEU   B 140 ? 0.1522 0.1164 0.2395 -0.0044 0.0248  0.0095  140 LEU   B CA  
6227 C C   . LEU   B 140 ? 0.1472 0.1179 0.2680 -0.0073 0.0191  -0.0037 140 LEU   B C   
6228 O O   . LEU   B 140 ? 0.1477 0.1186 0.2561 -0.0057 0.0103  0.0073  140 LEU   B O   
6229 C CB  . LEU   B 140 ? 0.1534 0.1190 0.2709 -0.0120 0.0343  0.0098  140 LEU   B CB  
6230 C CG  . LEU   B 140 ? 0.1574 0.1206 0.2737 -0.0075 0.0163  0.0086  140 LEU   B CG  
6231 C CD1 . LEU   B 140 ? 0.1713 0.1263 0.2830 -0.0104 0.0222  0.0014  140 LEU   B CD1 
6232 C CD2 . LEU   B 140 ? 0.1763 0.1320 0.2711 -0.0120 0.0108  -0.0051 140 LEU   B CD2 
6244 N N   . ARG   B 141 ? 0.1477 0.1223 0.2662 -0.0140 0.0224  -0.0046 141 ARG   B N   
6245 C CA  . ARG   B 141 ? 0.1456 0.1212 0.2967 -0.0196 0.0340  0.0022  141 ARG   B CA  
6246 C C   . ARG   B 141 ? 0.1430 0.1137 0.2891 -0.0145 0.0229  0.0053  141 ARG   B C   
6247 O O   . ARG   B 141 ? 0.1501 0.1293 0.2691 -0.0111 0.0046  -0.0103 141 ARG   B O   
6248 C CB  . ARG   B 141 ? 0.1563 0.1384 0.3252 -0.0225 0.0377  0.0121  141 ARG   B CB  
6249 C CG  . ARG   B 141 ? 0.1952 0.1595 0.3418 -0.0274 0.0315  -0.0004 141 ARG   B CG  
6250 C CD  . ARG   B 141 ? 0.2432 0.1863 0.3399 -0.0303 0.0058  -0.0037 141 ARG   B CD  
6251 N NE  . ARG   B 141 ? 0.2604 0.1850 0.3247 -0.0523 0.0097  -0.0005 141 ARG   B NE  
6252 C CZ  . ARG   B 141 ? 0.2666 0.1766 0.3048 -0.0460 0.0176  -0.0187 141 ARG   B CZ  
6253 N NH1 . ARG   B 141 ? 0.2820 0.1601 0.2889 -0.0272 0.0170  -0.0263 141 ARG   B NH1 
6254 N NH2 . ARG   B 141 ? 0.2687 0.1984 0.3119 -0.0300 -0.0010 -0.0112 141 ARG   B NH2 
6268 N N   . VAL   B 142 ? 0.1506 0.1197 0.2733 -0.0094 0.0211  -0.0050 142 VAL   B N   
6269 C CA  . VAL   B 142 ? 0.1356 0.1244 0.2637 -0.0017 0.0264  -0.0010 142 VAL   B CA  
6270 C C   . VAL   B 142 ? 0.1358 0.1240 0.2628 -0.0008 0.0108  -0.0017 142 VAL   B C   
6271 O O   . VAL   B 142 ? 0.1456 0.1187 0.2521 0.0044  0.0205  0.0019  142 VAL   B O   
6272 C CB  . VAL   B 142 ? 0.1477 0.1346 0.2663 0.0027  0.0298  0.0069  142 VAL   B CB  
6273 C CG1 . VAL   B 142 ? 0.1441 0.1331 0.2741 0.0073  0.0287  0.0016  142 VAL   B CG1 
6274 C CG2 . VAL   B 142 ? 0.1797 0.1347 0.2684 0.0052  0.0288  0.0246  142 VAL   B CG2 
6284 N N   . CYS   B 143 ? 0.1338 0.1305 0.2431 -0.0026 0.0103  0.0117  143 CYS   B N   
6285 C CA  . CYS   B 143 ? 0.1327 0.1219 0.2457 -0.0064 0.0101  0.0013  143 CYS   B CA  
6286 C C   . CYS   B 143 ? 0.1363 0.1237 0.2397 -0.0105 0.0079  -0.0091 143 CYS   B C   
6287 O O   . CYS   B 143 ? 0.1366 0.1218 0.2413 -0.0032 -0.0020 -0.0108 143 CYS   B O   
6288 C CB  . CYS   B 143 ? 0.1355 0.1311 0.2340 -0.0107 -0.0001 0.0113  143 CYS   B CB  
6289 S SG  . CYS   B 143 ? 0.1438 0.1431 0.2306 -0.0049 0.0099  0.0055  143 CYS   B SG  
6295 N N   . VAL   B 144 ? 0.1377 0.1272 0.2520 -0.0082 -0.0005 -0.0239 144 VAL   B N   
6296 C CA  . VAL   B 144 ? 0.1461 0.1410 0.2765 -0.0185 0.0041  -0.0261 144 VAL   B CA  
6297 C C   . VAL   B 144 ? 0.1321 0.1356 0.2847 -0.0091 0.0016  -0.0052 144 VAL   B C   
6298 O O   . VAL   B 144 ? 0.1501 0.1589 0.2905 0.0001  -0.0040 0.0149  144 VAL   B O   
6299 C CB  . VAL   B 144 ? 0.1700 0.1581 0.3355 -0.0154 -0.0018 -0.0510 144 VAL   B CB  
6300 C CG1 . VAL   B 144 ? 0.1927 0.2055 0.3631 -0.0057 -0.0141 -0.0551 144 VAL   B CG1 
6301 C CG2 . VAL   B 144 ? 0.1856 0.1494 0.3240 -0.0036 -0.0170 -0.0636 144 VAL   B CG2 
6311 N N   . ASP   B 145 ? 0.1365 0.1257 0.2871 -0.0090 0.0032  -0.0235 145 ASP   B N   
6312 C CA  . ASP   B 145 ? 0.1462 0.1326 0.3163 -0.0046 0.0103  -0.0069 145 ASP   B CA  
6313 C C   . ASP   B 145 ? 0.1411 0.1331 0.2939 -0.0080 0.0033  -0.0047 145 ASP   B C   
6314 O O   . ASP   B 145 ? 0.1370 0.1535 0.3652 -0.0108 0.0190  -0.0299 145 ASP   B O   
6315 C CB  . ASP   B 145 ? 0.1543 0.1434 0.3481 -0.0085 0.0197  0.0084  145 ASP   B CB  
6316 C CG  . ASP   B 145 ? 0.1743 0.1494 0.4023 -0.0217 0.0234  -0.0017 145 ASP   B CG  
6317 O OD1 . ASP   B 145 ? 0.1749 0.1406 0.4100 -0.0276 -0.0056 -0.0148 145 ASP   B OD1 
6318 O OD2 . ASP   B 145 ? 0.1984 0.1609 0.4360 -0.0325 0.0472  -0.0000 145 ASP   B OD2 
6323 N N   . THR   B 146 ? 0.1301 0.1246 0.2416 -0.0083 0.0041  0.0000  146 THR   B N   
6324 C CA  . THR   B 146 ? 0.1394 0.1322 0.2229 -0.0013 0.0092  0.0024  146 THR   B CA  
6325 C C   . THR   B 146 ? 0.1350 0.1342 0.2158 -0.0028 0.0030  0.0028  146 THR   B C   
6326 O O   . THR   B 146 ? 0.1369 0.1288 0.2244 -0.0047 -0.0040 0.0037  146 THR   B O   
6327 C CB  . THR   B 146 ? 0.1396 0.1308 0.2389 0.0025  0.0252  0.0025  146 THR   B CB  
6328 O OG1 . THR   B 146 ? 0.1472 0.1285 0.2345 -0.0026 0.0258  0.0188  146 THR   B OG1 
6329 C CG2 . THR   B 146 ? 0.1474 0.1337 0.2328 0.0019  0.0165  -0.0061 146 THR   B CG2 
6337 N N   . VAL   B 147 ? 0.1416 0.1288 0.2052 -0.0006 0.0124  -0.0018 147 VAL   B N   
6338 C CA  . VAL   B 147 ? 0.1379 0.1214 0.1968 -0.0106 0.0037  0.0066  147 VAL   B CA  
6339 C C   . VAL   B 147 ? 0.1448 0.1315 0.2031 -0.0182 -0.0102 -0.0082 147 VAL   B C   
6340 O O   . VAL   B 147 ? 0.1497 0.1395 0.2215 -0.0164 -0.0280 -0.0125 147 VAL   B O   
6341 C CB  . VAL   B 147 ? 0.1398 0.1302 0.1830 -0.0056 -0.0029 0.0055  147 VAL   B CB  
6342 C CG1 . VAL   B 147 ? 0.1414 0.1509 0.1748 -0.0142 -0.0073 0.0080  147 VAL   B CG1 
6343 C CG2 . VAL   B 147 ? 0.1406 0.1295 0.1929 -0.0075 0.0045  0.0016  147 VAL   B CG2 
6353 N N   . ARG   B 148 ? 0.1396 0.1284 0.2052 -0.0078 -0.0137 -0.0088 148 ARG   B N   
6354 C CA  . ARG   B 148 ? 0.1473 0.1320 0.2062 -0.0043 -0.0269 -0.0109 148 ARG   B CA  
6355 C C   . ARG   B 148 ? 0.1471 0.1424 0.1970 -0.0083 -0.0391 -0.0056 148 ARG   B C   
6356 O O   . ARG   B 148 ? 0.1720 0.1678 0.2039 -0.0286 -0.0471 -0.0002 148 ARG   B O   
6357 C CB  . ARG   B 148 ? 0.1554 0.1438 0.2122 0.0004  -0.0310 -0.0137 148 ARG   B CB  
6358 C CG  . ARG   B 148 ? 0.1489 0.1626 0.2123 -0.0034 -0.0214 -0.0445 148 ARG   B CG  
6359 C CD  . ARG   B 148 ? 0.1591 0.1840 0.2329 0.0121  -0.0145 -0.0448 148 ARG   B CD  
6360 N NE  . ARG   B 148 ? 0.1720 0.1803 0.2230 0.0258  -0.0301 -0.0353 148 ARG   B NE  
6361 C CZ  . ARG   B 148 ? 0.1604 0.1671 0.2156 0.0173  -0.0230 -0.0325 148 ARG   B CZ  
6362 N NH1 . ARG   B 148 ? 0.1561 0.1679 0.2261 0.0007  -0.0049 -0.0185 148 ARG   B NH1 
6363 N NH2 . ARG   B 148 ? 0.1732 0.1495 0.2192 0.0205  -0.0204 -0.0203 148 ARG   B NH2 
6377 N N   . THR   B 149 ? 0.1499 0.1352 0.1942 -0.0148 -0.0374 0.0072  149 THR   B N   
6378 C CA  . THR   B 149 ? 0.1557 0.1440 0.1815 -0.0168 -0.0399 0.0025  149 THR   B CA  
6379 C C   . THR   B 149 ? 0.1516 0.1393 0.1817 -0.0173 -0.0337 -0.0013 149 THR   B C   
6380 O O   . THR   B 149 ? 0.1598 0.1389 0.1952 -0.0242 -0.0105 0.0027  149 THR   B O   
6381 C CB  . THR   B 149 ? 0.1573 0.1461 0.1878 -0.0144 -0.0326 0.0067  149 THR   B CB  
6382 O OG1 . THR   B 149 ? 0.1592 0.1416 0.1870 -0.0217 -0.0326 0.0055  149 THR   B OG1 
6383 C CG2 . THR   B 149 ? 0.1668 0.1517 0.1966 -0.0094 -0.0202 0.0050  149 THR   B CG2 
6391 N N   . ASN   B 150 ? 0.1664 0.1368 0.1709 -0.0197 -0.0395 0.0114  150 ASN   B N   
6392 C CA  . ASN   B 150 ? 0.1776 0.1574 0.1519 -0.0242 -0.0367 0.0008  150 ASN   B CA  
6393 C C   . ASN   B 150 ? 0.1678 0.1531 0.1527 -0.0223 -0.0340 -0.0006 150 ASN   B C   
6394 O O   . ASN   B 150 ? 0.1705 0.1491 0.1726 -0.0305 -0.0398 -0.0011 150 ASN   B O   
6395 C CB  . ASN   B 150 ? 0.2043 0.1925 0.1661 -0.0254 -0.0448 0.0108  150 ASN   B CB  
6396 C CG  . ASN   B 150 ? 0.2306 0.2343 0.2149 -0.0334 -0.0506 0.0314  150 ASN   B CG  
6397 O OD1 . ASN   B 150 ? 0.2377 0.2573 0.2251 -0.0410 -0.0691 0.0351  150 ASN   B OD1 
6398 N ND2 . ASN   B 150 ? 0.2509 0.2582 0.2662 -0.0189 -0.0640 0.0740  150 ASN   B ND2 
6405 N N   . VAL   B 151 ? 0.1569 0.1487 0.1508 -0.0282 -0.0336 0.0034  151 VAL   B N   
6406 C CA  . VAL   B 151 ? 0.1658 0.1455 0.1425 -0.0245 -0.0247 -0.0029 151 VAL   B CA  
6407 C C   . VAL   B 151 ? 0.1613 0.1393 0.1480 -0.0350 -0.0234 -0.0061 151 VAL   B C   
6408 O O   . VAL   B 151 ? 0.1726 0.1524 0.1837 -0.0281 -0.0221 -0.0167 151 VAL   B O   
6409 C CB  . VAL   B 151 ? 0.1846 0.1573 0.1711 -0.0112 -0.0168 -0.0102 151 VAL   B CB  
6410 C CG1 . VAL   B 151 ? 0.2007 0.1617 0.2009 -0.0149 -0.0023 -0.0102 151 VAL   B CG1 
6411 C CG2 . VAL   B 151 ? 0.1963 0.1729 0.1497 0.0038  -0.0132 0.0100  151 VAL   B CG2 
6421 N N   . TYR   B 152 ? 0.1523 0.1273 0.1622 -0.0318 -0.0242 -0.0072 152 TYR   B N   
6422 C CA  . TYR   B 152 ? 0.1495 0.1565 0.1476 -0.0309 -0.0195 -0.0103 152 TYR   B CA  
6423 C C   . TYR   B 152 ? 0.1505 0.1330 0.1315 -0.0225 -0.0177 -0.0068 152 TYR   B C   
6424 O O   . TYR   B 152 ? 0.1591 0.1416 0.1440 -0.0296 -0.0157 0.0012  152 TYR   B O   
6425 C CB  . TYR   B 152 ? 0.1631 0.1671 0.1416 -0.0398 -0.0095 0.0086  152 TYR   B CB  
6426 C CG  . TYR   B 152 ? 0.1822 0.1719 0.1451 -0.0501 -0.0109 0.0024  152 TYR   B CG  
6427 C CD1 . TYR   B 152 ? 0.1967 0.1790 0.1394 -0.0407 -0.0221 0.0128  152 TYR   B CD1 
6428 C CD2 . TYR   B 152 ? 0.2044 0.1947 0.1601 -0.0475 -0.0172 -0.0117 152 TYR   B CD2 
6429 C CE1 . TYR   B 152 ? 0.2160 0.1989 0.1602 -0.0354 -0.0268 0.0244  152 TYR   B CE1 
6430 C CE2 . TYR   B 152 ? 0.2153 0.2064 0.1602 -0.0501 -0.0223 -0.0117 152 TYR   B CE2 
6431 C CZ  . TYR   B 152 ? 0.2212 0.2230 0.1447 -0.0452 -0.0410 0.0197  152 TYR   B CZ  
6432 O OH  . TYR   B 152 ? 0.2479 0.2649 0.1898 -0.0335 -0.0475 0.0285  152 TYR   B OH  
6442 N N   . LEU   B 153 ? 0.1555 0.1240 0.1540 -0.0268 -0.0173 -0.0086 153 LEU   B N   
6443 C CA  . LEU   B 153 ? 0.1634 0.1206 0.1500 -0.0198 -0.0078 -0.0081 153 LEU   B CA  
6444 C C   . LEU   B 153 ? 0.1644 0.1281 0.1579 -0.0291 -0.0120 -0.0217 153 LEU   B C   
6445 O O   . LEU   B 153 ? 0.1647 0.1464 0.1752 -0.0193 -0.0076 -0.0348 153 LEU   B O   
6446 C CB  . LEU   B 153 ? 0.1549 0.1244 0.1596 -0.0305 -0.0038 -0.0013 153 LEU   B CB  
6447 C CG  . LEU   B 153 ? 0.1506 0.1365 0.1884 -0.0265 0.0002  -0.0036 153 LEU   B CG  
6448 C CD1 . LEU   B 153 ? 0.1569 0.1522 0.2002 -0.0249 0.0034  0.0072  153 LEU   B CD1 
6449 C CD2 . LEU   B 153 ? 0.1580 0.1529 0.1956 -0.0286 0.0122  0.0045  153 LEU   B CD2 
6461 N N   . ALA   B 154 ? 0.1562 0.1280 0.1672 -0.0097 -0.0127 -0.0193 154 ALA   B N   
6462 C CA  . ALA   B 154 ? 0.1643 0.1356 0.1780 -0.0012 -0.0117 -0.0296 154 ALA   B CA  
6463 C C   . ALA   B 154 ? 0.1799 0.1404 0.1882 0.0081  -0.0204 -0.0378 154 ALA   B C   
6464 O O   . ALA   B 154 ? 0.2144 0.1408 0.2088 0.0125  -0.0115 -0.0110 154 ALA   B O   
6465 C CB  . ALA   B 154 ? 0.1598 0.1534 0.2181 -0.0044 -0.0048 -0.0382 154 ALA   B CB  
6471 N N   . VAL   B 155 ? 0.1477 0.1352 0.2063 -0.0036 0.0042  -0.0231 155 VAL   B N   
6472 C CA  . VAL   B 155 ? 0.1398 0.1386 0.2359 -0.0007 -0.0004 -0.0095 155 VAL   B CA  
6473 C C   . VAL   B 155 ? 0.1432 0.1414 0.2302 -0.0059 -0.0041 -0.0320 155 VAL   B C   
6474 O O   . VAL   B 155 ? 0.1581 0.1577 0.2590 -0.0000 -0.0024 -0.0522 155 VAL   B O   
6475 C CB  . VAL   B 155 ? 0.1445 0.1586 0.2678 -0.0058 -0.0170 0.0027  155 VAL   B CB  
6476 C CG1 . VAL   B 155 ? 0.1542 0.1566 0.2711 -0.0057 -0.0236 0.0101  155 VAL   B CG1 
6477 C CG2 . VAL   B 155 ? 0.1453 0.1669 0.2919 -0.0095 -0.0219 0.0353  155 VAL   B CG2 
6487 N N   . PHE   B 156 ? 0.1371 0.1505 0.2411 -0.0023 -0.0041 -0.0296 156 PHE   B N   
6488 C CA  . PHE   B 156 ? 0.1360 0.1501 0.2723 0.0069  0.0007  -0.0308 156 PHE   B CA  
6489 C C   . PHE   B 156 ? 0.1367 0.1572 0.3266 0.0070  -0.0061 -0.0454 156 PHE   B C   
6490 O O   . PHE   B 156 ? 0.1645 0.1730 0.3485 0.0154  0.0061  -0.0526 156 PHE   B O   
6491 C CB  . PHE   B 156 ? 0.1394 0.1453 0.2690 0.0013  -0.0135 -0.0170 156 PHE   B CB  
6492 C CG  . PHE   B 156 ? 0.1461 0.1580 0.2620 0.0002  -0.0231 -0.0013 156 PHE   B CG  
6493 C CD1 . PHE   B 156 ? 0.1496 0.1806 0.3013 0.0064  0.0075  0.0390  156 PHE   B CD1 
6494 C CD2 . PHE   B 156 ? 0.1575 0.1722 0.2676 0.0122  -0.0226 0.0050  156 PHE   B CD2 
6495 C CE1 . PHE   B 156 ? 0.1530 0.2003 0.3168 0.0074  0.0028  0.0412  156 PHE   B CE1 
6496 C CE2 . PHE   B 156 ? 0.1641 0.1948 0.3000 0.0120  -0.0188 0.0063  156 PHE   B CE2 
6497 C CZ  . PHE   B 156 ? 0.1486 0.2030 0.3202 0.0117  -0.0117 0.0167  156 PHE   B CZ  
6507 N N   . ASP   B 157 ? 0.1439 0.1480 0.3475 0.0155  -0.0176 -0.0246 157 ASP   B N   
6508 C CA  . ASP   B 157 ? 0.1605 0.1465 0.3625 0.0084  -0.0151 -0.0375 157 ASP   B CA  
6509 C C   . ASP   B 157 ? 0.1569 0.1542 0.3801 0.0126  -0.0123 -0.0644 157 ASP   B C   
6510 O O   . ASP   B 157 ? 0.1392 0.1542 0.3629 0.0097  -0.0198 -0.0441 157 ASP   B O   
6511 C CB  . ASP   B 157 ? 0.1895 0.1692 0.3739 0.0060  -0.0330 -0.0182 157 ASP   B CB  
6512 C CG  . ASP   B 157 ? 0.2323 0.1851 0.4066 -0.0001 -0.0196 -0.0196 157 ASP   B CG  
6513 O OD1 . ASP   B 157 ? 0.2452 0.1841 0.4290 0.0158  -0.0141 -0.0183 157 ASP   B OD1 
6514 O OD2 . ASP   B 157 ? 0.2772 0.2051 0.4344 -0.0083 -0.0035 -0.0133 157 ASP   B OD2 
6519 N N   . LYS   B 158 ? 0.1569 0.1782 0.3895 0.0094  -0.0056 -0.0884 158 LYS   B N   
6520 C CA  . LYS   B 158 ? 0.1847 0.2019 0.4000 -0.0022 0.0000  -0.1031 158 LYS   B CA  
6521 C C   . LYS   B 158 ? 0.1810 0.1859 0.4246 0.0033  -0.0102 -0.0922 158 LYS   B C   
6522 O O   . LYS   B 158 ? 0.1798 0.1835 0.4281 0.0025  -0.0067 -0.1032 158 LYS   B O   
6523 C CB  . LYS   B 158 ? 0.2091 0.2460 0.3907 0.0002  0.0062  -0.1273 158 LYS   B CB  
6524 C CG  . LYS   B 158 ? 0.2438 0.2898 0.3996 0.0016  0.0120  -0.1269 158 LYS   B CG  
6525 C CD  . LYS   B 158 ? 0.2719 0.3284 0.4121 -0.0012 0.0235  -0.1110 158 LYS   B CD  
6526 C CE  . LYS   B 158 ? 0.2971 0.3579 0.4232 -0.0008 0.0282  -0.1013 158 LYS   B CE  
6527 N NZ  . LYS   B 158 ? 0.2987 0.3718 0.4089 -0.0052 0.0410  -0.1000 158 LYS   B NZ  
6541 N N   . ASN   B 159 ? 0.1816 0.1672 0.4405 0.0061  -0.0116 -0.0753 159 ASN   B N   
6542 C CA  . ASN   B 159 ? 0.1941 0.1529 0.4629 0.0219  -0.0313 -0.0513 159 ASN   B CA  
6543 C C   . ASN   B 159 ? 0.1737 0.1423 0.4407 0.0177  -0.0529 -0.0358 159 ASN   B C   
6544 O O   . ASN   B 159 ? 0.1683 0.1349 0.4570 -0.0019 -0.0666 -0.0274 159 ASN   B O   
6545 C CB  . ASN   B 159 ? 0.2279 0.1662 0.4849 0.0315  -0.0416 -0.0561 159 ASN   B CB  
6546 C CG  . ASN   B 159 ? 0.2588 0.2030 0.5456 0.0398  -0.0603 -0.0602 159 ASN   B CG  
6547 O OD1 . ASN   B 159 ? 0.2808 0.2135 0.5293 0.0477  -0.0583 -0.0696 159 ASN   B OD1 
6548 N ND2 . ASN   B 159 ? 0.2580 0.1983 0.5166 0.0315  -0.0659 -0.0494 159 ASN   B ND2 
6555 N N   . LEU   B 160 ? 0.1677 0.1456 0.4049 0.0138  -0.0413 -0.0283 160 LEU   B N   
6556 C CA  . LEU   B 160 ? 0.1618 0.1457 0.3754 0.0089  -0.0400 -0.0186 160 LEU   B CA  
6557 C C   . LEU   B 160 ? 0.1567 0.1377 0.3511 0.0042  -0.0228 -0.0276 160 LEU   B C   
6558 O O   . LEU   B 160 ? 0.1389 0.1418 0.3426 -0.0017 -0.0256 -0.0201 160 LEU   B O   
6559 C CB  . LEU   B 160 ? 0.1576 0.1610 0.3470 0.0084  -0.0474 -0.0129 160 LEU   B CB  
6560 C CG  . LEU   B 160 ? 0.1546 0.1725 0.3163 0.0084  -0.0393 -0.0046 160 LEU   B CG  
6561 C CD1 . LEU   B 160 ? 0.1735 0.1972 0.3158 -0.0034 -0.0217 -0.0061 160 LEU   B CD1 
6562 C CD2 . LEU   B 160 ? 0.1608 0.1705 0.3183 0.0214  -0.0363 -0.0098 160 LEU   B CD2 
6574 N N   . TYR   B 161 ? 0.1591 0.1395 0.3607 -0.0095 0.0026  -0.0442 161 TYR   B N   
6575 C CA  . TYR   B 161 ? 0.1642 0.1517 0.3520 -0.0250 0.0259  -0.0556 161 TYR   B CA  
6576 C C   . TYR   B 161 ? 0.1685 0.1510 0.3310 -0.0143 0.0283  -0.0468 161 TYR   B C   
6577 O O   . TYR   B 161 ? 0.1693 0.1519 0.3226 -0.0189 0.0142  -0.0383 161 TYR   B O   
6578 C CB  . TYR   B 161 ? 0.1761 0.1589 0.3509 -0.0355 0.0396  -0.0693 161 TYR   B CB  
6579 C CG  . TYR   B 161 ? 0.2015 0.1702 0.3395 -0.0375 0.0429  -0.0729 161 TYR   B CG  
6580 C CD1 . TYR   B 161 ? 0.2060 0.1680 0.3342 -0.0514 0.0477  -0.0714 161 TYR   B CD1 
6581 C CD2 . TYR   B 161 ? 0.2266 0.1741 0.3309 -0.0279 0.0378  -0.0724 161 TYR   B CD2 
6582 C CE1 . TYR   B 161 ? 0.2350 0.1873 0.3416 -0.0491 0.0465  -0.0701 161 TYR   B CE1 
6583 C CE2 . TYR   B 161 ? 0.2499 0.1888 0.3416 -0.0341 0.0476  -0.0602 161 TYR   B CE2 
6584 C CZ  . TYR   B 161 ? 0.2539 0.1923 0.3328 -0.0553 0.0441  -0.0549 161 TYR   B CZ  
6585 O OH  . TYR   B 161 ? 0.2823 0.2134 0.3584 -0.0637 0.0457  -0.0523 161 TYR   B OH  
6595 N N   . ASP   B 162 ? 0.1719 0.1559 0.3356 -0.0110 0.0127  -0.0654 162 ASP   B N   
6596 C CA  . ASP   B 162 ? 0.1790 0.1604 0.3476 -0.0063 0.0021  -0.0581 162 ASP   B CA  
6597 C C   . ASP   B 162 ? 0.1743 0.1435 0.3582 -0.0143 0.0019  -0.0441 162 ASP   B C   
6598 O O   . ASP   B 162 ? 0.1723 0.1481 0.3652 -0.0150 -0.0182 -0.0318 162 ASP   B O   
6599 C CB  . ASP   B 162 ? 0.1971 0.1793 0.3736 0.0017  -0.0138 -0.0775 162 ASP   B CB  
6600 C CG  . ASP   B 162 ? 0.2042 0.2021 0.3885 0.0097  -0.0145 -0.0852 162 ASP   B CG  
6601 O OD1 . ASP   B 162 ? 0.2043 0.2226 0.3622 0.0032  0.0106  -0.0921 162 ASP   B OD1 
6602 O OD2 . ASP   B 162 ? 0.2137 0.2253 0.4275 0.0256  -0.0023 -0.0809 162 ASP   B OD2 
6607 N N   . LYS   B 163 ? 0.1731 0.1275 0.3457 -0.0143 -0.0078 -0.0254 163 LYS   B N   
6608 C CA  . LYS   B 163 ? 0.1828 0.1493 0.3463 -0.0138 -0.0025 -0.0023 163 LYS   B CA  
6609 C C   . LYS   B 163 ? 0.1518 0.1421 0.3316 -0.0192 -0.0073 0.0006  163 LYS   B C   
6610 O O   . LYS   B 163 ? 0.1558 0.1450 0.3472 -0.0176 -0.0165 0.0131  163 LYS   B O   
6611 C CB  . LYS   B 163 ? 0.2229 0.1769 0.3675 0.0039  -0.0118 0.0165  163 LYS   B CB  
6612 C CG  . LYS   B 163 ? 0.2866 0.2298 0.4191 0.0108  0.0027  0.0090  163 LYS   B CG  
6613 C CD  . LYS   B 163 ? 0.3406 0.2855 0.4722 0.0052  0.0158  0.0022  163 LYS   B CD  
6614 C CE  . LYS   B 163 ? 0.4013 0.3570 0.5068 -0.0048 0.0281  0.0097  163 LYS   B CE  
6615 N NZ  . LYS   B 163 ? 0.4467 0.3765 0.5291 -0.0156 0.0303  0.0118  163 LYS   B NZ  
6629 N N   . LEU   B 164 ? 0.1422 0.1354 0.2889 -0.0152 -0.0060 0.0015  164 LEU   B N   
6630 C CA  . LEU   B 164 ? 0.1428 0.1339 0.2783 -0.0129 -0.0179 0.0003  164 LEU   B CA  
6631 C C   . LEU   B 164 ? 0.1497 0.1355 0.2937 -0.0143 -0.0216 -0.0046 164 LEU   B C   
6632 O O   . LEU   B 164 ? 0.1585 0.1559 0.3172 -0.0186 -0.0290 0.0074  164 LEU   B O   
6633 C CB  . LEU   B 164 ? 0.1357 0.1315 0.2779 -0.0107 -0.0146 -0.0062 164 LEU   B CB  
6634 C CG  . LEU   B 164 ? 0.1510 0.1552 0.2831 -0.0115 -0.0039 0.0023  164 LEU   B CG  
6635 C CD1 . LEU   B 164 ? 0.1659 0.1494 0.2618 -0.0157 -0.0118 -0.0067 164 LEU   B CD1 
6636 C CD2 . LEU   B 164 ? 0.1702 0.1872 0.3027 -0.0116 0.0075  -0.0012 164 LEU   B CD2 
6648 N N   . VAL   B 165 ? 0.1779 0.1441 0.3036 -0.0240 -0.0336 -0.0067 165 VAL   B N   
6649 C CA  . VAL   B 165 ? 0.2196 0.1583 0.3136 -0.0418 -0.0629 -0.0070 165 VAL   B CA  
6650 C C   . VAL   B 165 ? 0.2521 0.1764 0.3339 -0.0517 -0.0862 -0.0040 165 VAL   B C   
6651 O O   . VAL   B 165 ? 0.2745 0.1922 0.3337 -0.0512 -0.0989 0.0051  165 VAL   B O   
6652 C CB  . VAL   B 165 ? 0.2425 0.1723 0.3188 -0.0186 -0.0311 -0.0140 165 VAL   B CB  
6653 C CG1 . VAL   B 165 ? 0.2666 0.1824 0.3382 -0.0142 -0.0096 -0.0117 165 VAL   B CG1 
6654 C CG2 . VAL   B 165 ? 0.2412 0.1718 0.3197 -0.0140 -0.0097 -0.0173 165 VAL   B CG2 
6664 N N   . SER   B 166 ? 0.2606 0.1653 0.3672 -0.0461 -0.0943 -0.0196 166 SER   B N   
6665 C CA  . SER   B 166 ? 0.2539 0.1616 0.4104 -0.0420 -0.0698 -0.0269 166 SER   B CA  
6666 C C   . SER   B 166 ? 0.2402 0.1625 0.4204 -0.0448 -0.0622 -0.0069 166 SER   B C   
6667 O O   . SER   B 166 ? 0.2423 0.1970 0.4461 -0.0618 -0.0764 -0.0323 166 SER   B O   
6668 C CB  . SER   B 166 ? 0.2491 0.1702 0.4536 -0.0313 -0.0596 -0.0489 166 SER   B CB  
6669 O OG  . SER   B 166 ? 0.2377 0.1722 0.4823 -0.0216 -0.0667 -0.0294 166 SER   B OG  
6675 N N   . SER   B 167 ? 0.2172 0.1613 0.3770 -0.0402 -0.0809 0.0315  167 SER   B N   
6676 C CA  . SER   B 167 ? 0.2090 0.1719 0.3735 -0.0319 -0.0519 0.0420  167 SER   B CA  
6677 C C   . SER   B 167 ? 0.1997 0.1918 0.3600 -0.0460 -0.0419 0.0661  167 SER   B C   
6678 O O   . SER   B 167 ? 0.1994 0.2058 0.3685 -0.0509 -0.0451 0.0566  167 SER   B O   
6679 C CB  . SER   B 167 ? 0.1897 0.1748 0.3964 -0.0285 -0.0228 0.0418  167 SER   B CB  
6680 O OG  . SER   B 167 ? 0.1859 0.1894 0.3977 -0.0224 0.0025  0.0369  167 SER   B OG  
6686 N N   . PHE   B 168 ? 0.1950 0.1920 0.3588 -0.0473 -0.0309 0.0733  168 PHE   B N   
6687 C CA  . PHE   B 168 ? 0.2052 0.1849 0.3283 -0.0468 -0.0340 0.0419  168 PHE   B CA  
6688 C C   . PHE   B 168 ? 0.1792 0.1683 0.2524 -0.0257 -0.0230 0.0174  168 PHE   B C   
6689 O O   . PHE   B 168 ? 0.2070 0.1629 0.2479 0.0008  -0.0119 -0.0006 168 PHE   B O   
6690 C CB  . PHE   B 168 ? 0.2216 0.1863 0.3325 -0.0591 -0.0415 0.0572  168 PHE   B CB  
6691 C CG  . PHE   B 168 ? 0.2490 0.1707 0.3250 -0.0536 -0.0351 0.0267  168 PHE   B CG  
6692 C CD1 . PHE   B 168 ? 0.2787 0.1788 0.3426 -0.0500 -0.0409 0.0106  168 PHE   B CD1 
6693 C CD2 . PHE   B 168 ? 0.2365 0.1610 0.3206 -0.0460 -0.0362 0.0281  168 PHE   B CD2 
6694 C CE1 . PHE   B 168 ? 0.2824 0.1788 0.3304 -0.0421 -0.0297 0.0211  168 PHE   B CE1 
6695 C CE2 . PHE   B 168 ? 0.2580 0.1637 0.3208 -0.0300 -0.0369 0.0213  168 PHE   B CE2 
6696 C CZ  . PHE   B 168 ? 0.2684 0.1620 0.3299 -0.0246 -0.0376 0.0331  168 PHE   B CZ  
6706 N N   . LEU   B 169 ? 0.1945 0.1733 0.2513 -0.0012 -0.0047 0.0110  169 LEU   B N   
6707 C CA  . LEU   B 169 ? 0.2279 0.2000 0.2917 -0.0054 0.0063  -0.0231 169 LEU   B CA  
6708 C C   . LEU   B 169 ? 0.2620 0.2293 0.3634 0.0094  0.0047  -0.0478 169 LEU   B C   
6709 O O   . LEU   B 169 ? 0.2838 0.2450 0.4260 0.0051  -0.0025 -0.0627 169 LEU   B O   
6710 C CB  . LEU   B 169 ? 0.2527 0.2446 0.3035 -0.0121 0.0059  0.0029  169 LEU   B CB  
6711 C CG  . LEU   B 169 ? 0.2912 0.2914 0.3530 -0.0098 0.0096  0.0112  169 LEU   B CG  
6712 C CD1 . LEU   B 169 ? 0.3056 0.3110 0.3583 -0.0128 0.0002  0.0219  169 LEU   B CD1 
6713 C CD2 . LEU   B 169 ? 0.2941 0.3015 0.3557 0.0009  0.0282  -0.0003 169 LEU   B CD2 
6714 O OXT . LEU   B 169 ? 0.2817 0.2496 0.3625 0.0391  0.0184  -0.0493 169 LEU   B OXT 
6726 N N2  B A1A7W C .   ? 0.1304 0.1297 0.1358 0.0068  -0.0115 0.0288  201 A1A7W A N2  
6727 C C3  B A1A7W C .   ? 0.1503 0.1404 0.1722 -0.0082 -0.0101 0.0144  201 A1A7W A C3  
6728 C C6  B A1A7W C .   ? 0.1474 0.1285 0.1545 0.0003  -0.0199 0.0263  201 A1A7W A C6  
6729 C C9  B A1A7W C .   ? 0.1331 0.1293 0.1432 0.0009  -0.0038 0.0320  201 A1A7W A C9  
6730 C C12 B A1A7W C .   ? 0.1363 0.1360 0.1964 0.0095  -0.0202 0.0448  201 A1A7W A C12 
6731 C C1  B A1A7W C .   ? 0.1538 0.1287 0.1796 0.0054  -0.0185 0.0021  201 A1A7W A C1  
6732 C C10 B A1A7W C .   ? 0.1257 0.1333 0.1443 -0.0040 -0.0032 0.0353  201 A1A7W A C10 
6733 C C11 B A1A7W C .   ? 0.1303 0.1244 0.1574 0.0058  -0.0005 0.0194  201 A1A7W A C11 
6734 C C13 B A1A7W C .   ? 0.1515 0.1412 0.1548 -0.0021 -0.0174 0.0277  201 A1A7W A C13 
6735 C C2  B A1A7W C .   ? 0.1485 0.1292 0.1472 -0.0067 -0.0218 0.0052  201 A1A7W A C2  
6736 C C4  B A1A7W C .   ? 0.1518 0.1499 0.1643 -0.0045 -0.0023 0.0198  201 A1A7W A C4  
6737 C C5  B A1A7W C .   ? 0.1514 0.1416 0.1487 0.0009  -0.0138 0.0141  201 A1A7W A C5  
6738 C C7  B A1A7W C .   ? 0.1290 0.1143 0.1778 0.0079  -0.0250 0.0263  201 A1A7W A C7  
6739 C C8  B A1A7W C .   ? 0.1275 0.1197 0.1705 0.0028  -0.0099 0.0241  201 A1A7W A C8  
6740 N N1  B A1A7W C .   ? 0.1400 0.1172 0.1684 0.0057  -0.0238 0.0257  201 A1A7W A N1  
6741 N N3  B A1A7W C .   ? 0.1326 0.1295 0.1907 0.0068  0.0147  0.0464  201 A1A7W A N3  
6742 N N4  B A1A7W C .   ? 0.1300 0.1247 0.1942 0.0052  -0.0359 0.0281  201 A1A7W A N4  
6743 O O1  B A1A7W C .   ? 0.1550 0.1409 0.2054 0.0045  -0.0329 -0.0006 201 A1A7W A O1  
6760 O O   A HOH   D .   ? 0.3325 0.5698 0.3556 -0.0252 -0.0245 0.1037  301 HOH   A O   
6761 O O   . HOH   D .   ? 0.4664 0.5087 0.5666 0.0064  0.1995  0.2463  302 HOH   A O   
6762 O O   . HOH   D .   ? 0.3277 0.3608 0.2913 -0.1618 -0.1062 0.1618  303 HOH   A O   
6763 O O   . HOH   D .   ? 0.2998 0.3250 0.1974 -0.0183 0.0464  0.0572  304 HOH   A O   
6764 O O   . HOH   D .   ? 0.6024 0.4852 0.3027 0.2033  -0.1041 0.0537  305 HOH   A O   
6765 O O   . HOH   D .   ? 0.6078 0.4540 0.6786 -0.0190 0.2213  0.2316  306 HOH   A O   
6766 O O   . HOH   D .   ? 0.3225 0.2944 0.5289 -0.0407 -0.1298 0.1768  307 HOH   A O   
6767 O O   . HOH   D .   ? 0.4498 0.3472 0.5052 -0.0038 0.1646  0.0058  308 HOH   A O   
6768 O O   . HOH   D .   ? 0.2293 0.2867 0.3673 -0.0014 0.1079  -0.0010 309 HOH   A O   
6769 O O   . HOH   D .   ? 0.5296 0.6102 0.6660 0.0072  0.0038  -0.0429 310 HOH   A O   
6770 O O   . HOH   D .   ? 0.2942 0.2314 0.5105 -0.0158 -0.0904 0.0244  311 HOH   A O   
6771 O O   . HOH   D .   ? 0.6033 0.6336 0.3712 -0.1225 -0.0592 0.0996  312 HOH   A O   
6772 O O   . HOH   D .   ? 0.7371 0.8505 0.6611 -0.1198 -0.1465 -0.0949 313 HOH   A O   
6773 O O   . HOH   D .   ? 0.4764 0.6260 0.4213 0.2489  0.0943  -0.0918 314 HOH   A O   
6774 O O   . HOH   D .   ? 0.3640 0.5543 0.7152 -0.0591 -0.1483 0.1951  315 HOH   A O   
6775 O O   . HOH   D .   ? 0.6336 0.4448 0.5838 -0.1020 0.1898  0.2084  316 HOH   A O   
6776 O O   . HOH   D .   ? 0.1994 0.3239 0.2810 0.0384  -0.0278 -0.0630 317 HOH   A O   
6777 O O   . HOH   D .   ? 0.2107 0.2048 0.3479 -0.0507 0.0106  -0.0075 318 HOH   A O   
6778 O O   . HOH   D .   ? 0.3295 0.3468 0.3970 -0.1008 0.0148  0.1163  319 HOH   A O   
6779 O O   . HOH   D .   ? 0.6429 0.7068 0.7759 -0.1538 -0.1229 0.1501  320 HOH   A O   
6780 O O   . HOH   D .   ? 0.1988 0.2216 0.2960 -0.0179 -0.0056 0.0801  321 HOH   A O   
6781 O O   . HOH   D .   ? 0.2317 0.3310 0.4882 -0.0249 0.0404  -0.0769 322 HOH   A O   
6782 O O   . HOH   D .   ? 0.2316 0.1753 0.2264 0.0348  -0.0581 -0.0127 323 HOH   A O   
6783 O O   . HOH   D .   ? 1.1213 1.0116 0.8419 -0.0319 -0.0913 0.1411  324 HOH   A O   
6784 O O   . HOH   D .   ? 0.3425 0.4306 0.4395 -0.0299 0.1802  0.0650  325 HOH   A O   
6785 O O   . HOH   D .   ? 0.4121 0.3146 0.2689 -0.1186 -0.0138 0.0438  326 HOH   A O   
6786 O O   . HOH   D .   ? 0.2230 0.4038 0.4156 -0.0258 -0.0849 0.1624  327 HOH   A O   
6787 O O   . HOH   D .   ? 0.2322 0.2103 0.2754 0.0448  0.0542  0.0416  328 HOH   A O   
6788 O O   . HOH   D .   ? 0.2046 0.5476 0.3558 0.0027  0.0389  0.0982  329 HOH   A O   
6789 O O   . HOH   D .   ? 0.3575 0.4016 0.4265 -0.1599 -0.1129 0.2151  330 HOH   A O   
6790 O O   . HOH   D .   ? 0.3571 0.3978 0.4981 -0.0755 -0.0979 -0.0790 331 HOH   A O   
6791 O O   A HOH   D .   ? 0.2229 0.3429 0.3539 -0.0100 -0.0323 0.0788  332 HOH   A O   
6792 O O   A HOH   D .   ? 0.2746 0.2049 0.2244 0.0082  -0.0122 -0.0283 333 HOH   A O   
6793 O O   . HOH   D .   ? 0.5929 0.3960 0.3005 0.1054  0.0903  0.1317  334 HOH   A O   
6794 O O   . HOH   D .   ? 0.6401 0.5757 0.3681 0.1030  -0.0559 0.0171  335 HOH   A O   
6795 O O   B HOH   D .   ? 0.2071 0.2147 0.2428 -0.0264 0.0035  0.0641  336 HOH   A O   
6796 O O   . HOH   D .   ? 0.4344 0.2117 0.3443 0.0283  -0.1334 0.0441  337 HOH   A O   
6797 O O   . HOH   D .   ? 0.2461 0.4033 0.3504 0.0848  -0.0711 -0.0186 338 HOH   A O   
6798 O O   . HOH   D .   ? 0.1502 0.2280 0.1956 -0.0020 -0.0131 0.0595  339 HOH   A O   
6799 O O   . HOH   D .   ? 0.1738 0.1693 0.2072 0.0119  -0.0226 0.0205  340 HOH   A O   
6800 O O   . HOH   D .   ? 0.3064 0.2527 0.2697 -0.0445 0.0050  -0.0353 341 HOH   A O   
6801 O O   . HOH   D .   ? 0.5958 0.4970 0.7208 -0.0800 -0.1486 0.0255  342 HOH   A O   
6802 O O   B HOH   D .   ? 0.1421 0.1262 0.1928 0.0069  -0.0071 0.0498  343 HOH   A O   
6803 O O   A HOH   D .   ? 0.2971 0.3850 0.2002 -0.1453 -0.0117 0.0597  344 HOH   A O   
6804 O O   . HOH   D .   ? 0.5051 0.2084 0.6545 0.0915  -0.0573 -0.0415 345 HOH   A O   
6805 O O   . HOH   D .   ? 0.4164 0.7053 0.3085 0.1682  0.1163  -0.0516 346 HOH   A O   
6806 O O   . HOH   D .   ? 0.4307 0.2177 0.2380 0.1293  0.0501  0.0302  347 HOH   A O   
6807 O O   . HOH   D .   ? 0.3218 0.3349 0.2535 -0.0759 -0.0305 -0.0739 348 HOH   A O   
6808 O O   . HOH   D .   ? 0.2303 0.5606 0.2988 -0.0580 -0.0206 0.0786  349 HOH   A O   
6809 O O   B HOH   D .   ? 0.2127 0.2409 0.3802 0.0124  0.0202  0.0168  350 HOH   A O   
6810 O O   . HOH   D .   ? 0.3280 0.4479 0.2050 -0.0386 0.0660  0.0334  351 HOH   A O   
6811 O O   A HOH   D .   ? 0.2199 0.4091 0.2931 0.0827  -0.0714 -0.0429 352 HOH   A O   
6812 O O   . HOH   D .   ? 0.2045 0.1949 0.3546 0.0234  0.0797  -0.0063 353 HOH   A O   
6813 O O   . HOH   D .   ? 0.4405 0.3248 0.4540 -0.1229 -0.0537 -0.0147 354 HOH   A O   
6814 O O   . HOH   D .   ? 0.7031 0.6926 0.4705 -0.0994 0.2327  -0.1348 355 HOH   A O   
6815 O O   . HOH   D .   ? 0.3538 0.5238 0.3875 0.1809  0.0764  0.0834  356 HOH   A O   
6816 O O   . HOH   D .   ? 0.3231 0.2728 0.7588 0.0740  0.1765  0.0407  357 HOH   A O   
6817 O O   . HOH   D .   ? 0.1409 0.1978 0.2544 0.0091  -0.0016 0.0014  358 HOH   A O   
6818 O O   . HOH   D .   ? 0.1987 0.2371 0.3885 0.0151  0.0905  -0.0548 359 HOH   A O   
6819 O O   . HOH   D .   ? 0.1694 0.1359 0.2009 -0.0050 0.0241  -0.0090 360 HOH   A O   
6820 O O   . HOH   D .   ? 0.3020 0.3838 0.3930 -0.1190 -0.0740 -0.0211 361 HOH   A O   
6821 O O   . HOH   D .   ? 0.3029 0.4652 0.4447 -0.0904 0.0330  -0.0346 362 HOH   A O   
6822 O O   A HOH   D .   ? 0.1754 0.2508 0.2373 0.0892  0.0541  0.0978  363 HOH   A O   
6823 O O   . HOH   D .   ? 0.6436 0.7905 0.5835 -0.1104 0.2044  0.1354  364 HOH   A O   
6824 O O   A HOH   D .   ? 0.1946 0.1715 0.2440 -0.0410 0.0222  0.0853  365 HOH   A O   
6825 O O   . HOH   D .   ? 0.1804 0.2246 0.2291 -0.0119 -0.0398 0.0448  366 HOH   A O   
6826 O O   B HOH   D .   ? 0.2039 0.1542 0.3383 -0.0433 -0.1045 0.0415  367 HOH   A O   
6827 O O   . HOH   D .   ? 0.1405 0.1502 0.1502 -0.0064 -0.0086 -0.0010 368 HOH   A O   
6828 O O   A HOH   D .   ? 0.1602 0.1516 0.2820 0.0333  -0.0764 -0.0354 369 HOH   A O   
6829 O O   B HOH   D .   ? 0.1430 0.1576 0.2653 -0.0013 -0.0022 0.0309  370 HOH   A O   
6830 O O   . HOH   D .   ? 0.4235 0.2154 0.4423 -0.1223 0.0883  0.0159  371 HOH   A O   
6831 O O   A HOH   D .   ? 0.2379 0.1739 0.3287 0.0360  -0.0908 -0.0082 372 HOH   A O   
6832 O O   . HOH   D .   ? 0.1442 0.1378 0.1853 0.0034  0.0064  0.0065  373 HOH   A O   
6833 O O   . HOH   D .   ? 0.6164 0.4610 0.5689 -0.0083 -0.0664 -0.0482 374 HOH   A O   
6834 O O   . HOH   D .   ? 0.2727 0.5085 0.3273 0.0664  0.0866  0.2110  375 HOH   A O   
6835 O O   . HOH   D .   ? 0.4875 0.4778 0.3899 -0.1222 -0.0748 0.1703  376 HOH   A O   
6836 O O   . HOH   D .   ? 0.3668 0.8487 0.6231 -0.0818 -0.1709 0.0057  377 HOH   A O   
6837 O O   . HOH   D .   ? 0.3616 0.2218 0.3987 -0.1044 0.1323  -0.0462 378 HOH   A O   
6838 O O   . HOH   D .   ? 0.4004 0.5381 0.7368 0.1142  0.1683  -0.1701 379 HOH   A O   
6839 O O   . HOH   D .   ? 0.1859 0.1988 0.2181 -0.0230 0.0095  0.0327  380 HOH   A O   
6840 O O   B HOH   D .   ? 0.1695 0.1342 0.1530 -0.0102 -0.0223 0.0334  381 HOH   A O   
6841 O O   . HOH   D .   ? 0.2281 0.2365 0.2614 -0.0177 0.0258  0.0236  382 HOH   A O   
6842 O O   B HOH   D .   ? 0.1856 0.1931 0.2074 -0.0011 0.0054  0.0301  383 HOH   A O   
6843 O O   A HOH   D .   ? 0.2329 0.4366 0.4129 0.0803  -0.0218 0.1081  384 HOH   A O   
6844 O O   . HOH   D .   ? 0.3283 0.2775 0.2217 0.0166  0.0741  0.0016  385 HOH   A O   
6845 O O   B HOH   D .   ? 0.3296 0.3204 0.3847 0.0822  -0.0055 0.0498  386 HOH   A O   
6846 O O   . HOH   D .   ? 0.8812 0.8540 0.6207 -0.1383 0.0839  -0.0140 387 HOH   A O   
6847 O O   . HOH   D .   ? 0.6168 0.8094 0.3777 -0.1291 0.0242  -0.0991 388 HOH   A O   
6848 O O   . HOH   D .   ? 0.2282 0.1923 0.1718 -0.0432 0.0254  0.0303  389 HOH   A O   
6849 O O   . HOH   D .   ? 0.5724 0.5055 0.4137 -0.0264 -0.2018 0.0164  390 HOH   A O   
6850 O O   A HOH   D .   ? 0.2214 0.1554 0.3523 0.0059  -0.0761 0.0249  391 HOH   A O   
6851 O O   . HOH   D .   ? 0.1738 0.1688 0.2396 -0.0111 0.0126  0.0341  392 HOH   A O   
6852 O O   . HOH   D .   ? 0.1679 0.1388 0.1586 -0.0228 0.0116  0.0098  393 HOH   A O   
6853 O O   . HOH   D .   ? 0.3804 0.5430 0.6644 0.0528  -0.1018 0.0769  394 HOH   A O   
6854 O O   . HOH   D .   ? 0.4499 0.2397 0.6076 -0.0843 0.0108  -0.0111 395 HOH   A O   
6855 O O   . HOH   D .   ? 0.1690 0.2542 0.3762 -0.0009 0.0776  0.1191  396 HOH   A O   
6856 O O   . HOH   D .   ? 0.1388 0.1435 0.1803 -0.0013 -0.0218 0.0084  397 HOH   A O   
6857 O O   . HOH   D .   ? 0.2796 0.2313 0.2515 -0.0566 -0.0757 0.0356  398 HOH   A O   
6858 O O   . HOH   D .   ? 0.2003 0.1784 0.3575 0.0070  -0.0328 0.0238  399 HOH   A O   
6859 O O   . HOH   D .   ? 0.2957 0.2586 0.3534 -0.0167 -0.0390 0.0992  400 HOH   A O   
6860 O O   . HOH   D .   ? 0.2842 0.3293 0.3977 -0.1000 0.1002  0.0075  401 HOH   A O   
6861 O O   . HOH   D .   ? 0.2070 0.1681 0.1926 -0.0006 0.0030  0.0245  402 HOH   A O   
6862 O O   A HOH   D .   ? 0.1262 0.1216 0.0978 0.0068  0.0083  0.0126  403 HOH   A O   
6863 O O   . HOH   D .   ? 0.2722 0.1976 0.2883 0.0068  0.0148  0.0445  404 HOH   A O   
6864 O O   . HOH   D .   ? 0.4546 0.5004 0.2089 0.0325  0.0487  0.0201  405 HOH   A O   
6865 O O   . HOH   D .   ? 0.2422 0.2026 0.2515 -0.0457 -0.0096 0.0517  406 HOH   A O   
6866 O O   . HOH   D .   ? 0.1889 0.1927 0.3792 0.0464  0.1110  0.1056  407 HOH   A O   
6867 O O   A HOH   D .   ? 0.4793 0.3192 0.2877 -0.1241 0.0023  0.0685  408 HOH   A O   
6868 O O   . HOH   D .   ? 0.2287 0.3177 0.3967 0.0315  -0.1109 -0.0947 409 HOH   A O   
6869 O O   . HOH   D .   ? 0.2394 0.3988 0.3874 -0.0324 0.1043  -0.0835 410 HOH   A O   
6870 O O   . HOH   D .   ? 0.2083 0.2509 0.3572 -0.0028 -0.0323 0.0365  411 HOH   A O   
6871 O O   A HOH   D .   ? 0.2960 0.3171 0.2828 0.0359  -0.0070 -0.0429 412 HOH   A O   
6872 O O   . HOH   D .   ? 0.4302 0.3305 0.2812 -0.0456 0.0400  0.0549  413 HOH   A O   
6873 O O   A HOH   D .   ? 0.2825 0.3073 0.4002 -0.1192 -0.0563 0.0307  414 HOH   A O   
6874 O O   . HOH   D .   ? 0.5202 0.5328 0.4566 0.1280  -0.1023 -0.1699 415 HOH   A O   
6875 O O   . HOH   D .   ? 0.4922 0.3827 0.3542 -0.0102 -0.1407 -0.0294 416 HOH   A O   
6876 O O   B HOH   D .   ? 0.3517 0.1639 0.4329 -0.0222 -0.1108 0.0575  417 HOH   A O   
6877 O O   . HOH   D .   ? 0.7041 0.6404 0.6413 0.3328  0.2171  0.1674  418 HOH   A O   
6878 O O   . HOH   D .   ? 0.7720 0.8552 0.7971 0.1539  -0.0233 0.1828  419 HOH   A O   
6879 O O   . HOH   D .   ? 0.3425 0.6812 0.4412 -0.0351 -0.0349 0.1362  420 HOH   A O   
6880 O O   . HOH   D .   ? 0.4291 0.5798 0.5677 0.0210  0.1276  0.2145  421 HOH   A O   
6881 O O   . HOH   D .   ? 0.1705 0.2545 0.4432 0.0007  -0.0047 0.0385  422 HOH   A O   
6882 O O   . HOH   D .   ? 0.2326 0.3849 0.7678 -0.0253 0.0492  -0.0405 423 HOH   A O   
6883 O O   . HOH   D .   ? 0.2032 0.2574 0.2848 -0.0034 -0.0540 0.0638  424 HOH   A O   
6884 O O   . HOH   D .   ? 0.1767 0.1991 0.2842 0.0173  -0.0262 0.0295  425 HOH   A O   
6885 O O   . HOH   D .   ? 0.1553 0.1729 0.3215 0.0027  0.0094  0.0119  426 HOH   A O   
6886 O O   . HOH   D .   ? 0.5243 0.8071 0.4265 0.2226  -0.0751 -0.0239 427 HOH   A O   
6887 O O   . HOH   D .   ? 0.3593 0.1342 0.2021 -0.0090 -0.0726 0.0233  428 HOH   A O   
6888 O O   . HOH   D .   ? 0.2201 0.3838 0.5792 0.0344  -0.0985 -0.1891 429 HOH   A O   
6889 O O   . HOH   D .   ? 0.6003 0.7653 0.6991 0.0349  -0.1205 0.0698  430 HOH   A O   
6890 O O   . HOH   D .   ? 0.5634 0.3022 0.6143 0.1329  -0.0613 -0.0411 431 HOH   A O   
6891 O O   . HOH   D .   ? 0.4085 0.2343 0.5310 -0.0879 -0.2338 0.1063  432 HOH   A O   
6892 O O   A HOH   D .   ? 0.2545 0.2160 0.3090 0.0512  0.0435  0.0483  433 HOH   A O   
6893 O O   . HOH   D .   ? 0.4290 0.6634 0.3069 -0.1111 -0.0204 0.1280  434 HOH   A O   
6894 O O   . HOH   D .   ? 0.3010 0.5831 0.1682 -0.0274 0.0569  0.0086  435 HOH   A O   
6895 O O   . HOH   D .   ? 0.2275 0.4040 0.2701 0.1404  -0.0114 0.0148  436 HOH   A O   
6896 O O   . HOH   D .   ? 0.3078 0.3525 0.5888 0.0003  0.1274  -0.0302 437 HOH   A O   
6897 O O   . HOH   D .   ? 0.5192 0.6100 0.4161 0.1000  -0.1030 -0.1087 438 HOH   A O   
6898 O O   . HOH   D .   ? 0.6638 0.3773 0.4864 0.1596  -0.1177 0.1092  439 HOH   A O   
6899 O O   B HOH   D .   ? 0.2799 0.2087 0.3445 -0.0761 -0.0583 0.0520  440 HOH   A O   
6900 O O   B HOH   D .   ? 0.1840 0.1769 0.1955 0.0243  -0.0273 0.0162  441 HOH   A O   
6901 O O   A HOH   D .   ? 0.1433 0.1026 0.1198 -0.0017 0.0227  0.0225  442 HOH   A O   
6902 O O   . HOH   D .   ? 0.2461 0.1674 0.3241 0.0126  0.0158  0.0111  443 HOH   A O   
6903 O O   . HOH   D .   ? 0.8180 0.6476 0.7847 0.0274  0.0189  -0.0704 444 HOH   A O   
6904 O O   . HOH   D .   ? 0.4139 0.2712 0.1884 -0.0843 0.0448  0.0502  445 HOH   A O   
6905 O O   . HOH   D .   ? 0.6589 0.6779 0.4137 0.0960  0.2805  -0.0327 446 HOH   A O   
6906 O O   A HOH   D .   ? 0.6036 0.5312 0.3938 0.1901  -0.1171 0.0922  447 HOH   A O   
6907 O O   . HOH   D .   ? 0.1814 0.2236 0.4752 -0.0243 -0.0880 0.0676  448 HOH   A O   
6908 O O   . HOH   D .   ? 0.4286 0.6042 0.5172 -0.0609 -0.0875 -0.1450 449 HOH   A O   
6909 O O   . HOH   D .   ? 0.4635 0.3975 0.3012 0.2521  -0.0682 -0.0465 450 HOH   A O   
6910 O O   . HOH   D .   ? 0.2201 0.2892 0.2607 -0.0045 -0.0098 -0.0568 451 HOH   A O   
6911 O O   A HOH   D .   ? 0.3702 0.1651 0.1879 -0.0304 -0.0471 -0.0154 452 HOH   A O   
6912 O O   . HOH   D .   ? 0.3225 0.4327 0.7313 0.0121  0.0514  -0.2944 453 HOH   A O   
6913 O O   . HOH   D .   ? 0.2234 0.2217 0.2780 0.0065  0.0175  0.0496  454 HOH   A O   
6914 O O   A HOH   D .   ? 0.4694 0.4309 0.4931 -0.1057 0.0917  -0.0028 455 HOH   A O   
6915 O O   A HOH   D .   ? 0.6633 0.4636 0.3868 0.0685  0.0505  0.1216  456 HOH   A O   
6916 O O   B HOH   D .   ? 0.1395 0.1837 0.1884 -0.0440 -0.0140 0.0129  457 HOH   A O   
6917 O O   B HOH   D .   ? 0.4188 0.3796 0.3803 0.0184  0.0319  -0.1982 458 HOH   A O   
6918 O O   . HOH   D .   ? 0.8725 0.7615 0.7522 -0.1363 0.0751  -0.1304 459 HOH   A O   
6919 O O   . HOH   D .   ? 0.6362 0.7090 0.7688 -0.0625 -0.1126 0.1384  460 HOH   A O   
6920 O O   . HOH   D .   ? 0.3162 0.3922 0.4204 0.0793  0.0623  0.0611  461 HOH   A O   
6921 O O   . HOH   D .   ? 0.4515 0.4273 0.4695 0.2283  -0.0953 0.0323  462 HOH   A O   
6922 O O   . HOH   D .   ? 0.4321 0.3261 0.3835 0.0403  0.0878  0.0396  463 HOH   A O   
6923 O O   . HOH   D .   ? 0.7943 0.7947 0.4938 0.0004  -0.1259 -0.0455 464 HOH   A O   
6924 O O   . HOH   D .   ? 0.3320 0.3112 0.5808 -0.0417 -0.0528 -0.1587 465 HOH   A O   
6925 O O   . HOH   D .   ? 0.4471 0.6971 0.6231 -0.0148 0.0520  0.1606  466 HOH   A O   
6926 O O   . HOH   D .   ? 0.3016 0.5563 0.4999 -0.1082 0.0846  -0.0876 467 HOH   A O   
6927 O O   . HOH   D .   ? 0.3569 0.4929 0.4982 0.0301  -0.1687 0.1062  468 HOH   A O   
6928 O O   . HOH   D .   ? 0.2678 0.4420 0.4787 0.0578  -0.0029 -0.2007 469 HOH   A O   
6929 O O   . HOH   D .   ? 0.6904 0.7227 0.6261 0.1942  0.2346  0.2586  470 HOH   A O   
6930 O O   B HOH   D .   ? 0.1512 0.1600 0.3053 -0.0231 -0.0273 0.0568  471 HOH   A O   
6931 O O   . HOH   D .   ? 0.4665 0.5075 0.4455 -0.1259 0.0445  0.0254  472 HOH   A O   
6932 O O   . HOH   D .   ? 0.2765 0.1847 0.2679 0.0429  -0.1000 -0.0498 473 HOH   A O   
6933 O O   . HOH   D .   ? 0.3087 0.2698 0.3848 -0.0976 0.0430  -0.0350 474 HOH   A O   
6934 O O   . HOH   D .   ? 0.5828 0.5052 0.5545 -0.0767 0.1561  0.0014  475 HOH   A O   
6935 O O   . HOH   D .   ? 0.5353 0.2817 0.6768 0.1262  0.0871  0.1597  476 HOH   A O   
6936 O O   . HOH   D .   ? 0.3877 0.6702 0.4162 -0.0557 -0.1237 0.2164  477 HOH   A O   
6937 O O   . HOH   D .   ? 0.3691 0.3418 0.4176 0.0064  0.1164  0.0627  478 HOH   A O   
6938 O O   . HOH   D .   ? 0.7436 0.4400 0.4770 0.0020  0.0338  0.0741  479 HOH   A O   
6939 O O   . HOH   D .   ? 0.6622 0.7212 0.5645 0.1978  0.0124  -0.0284 480 HOH   A O   
6940 O O   A HOH   D .   ? 0.2894 0.2800 0.4931 -0.0046 -0.1206 -0.0776 481 HOH   A O   
6941 O O   . HOH   D .   ? 0.7031 0.6155 0.7467 -0.1279 -0.1129 -0.1122 482 HOH   A O   
6942 O O   . HOH   D .   ? 0.2736 0.3138 0.2678 0.0461  0.0119  0.0005  483 HOH   A O   
6943 O O   . HOH   D .   ? 0.4196 0.4325 0.7407 -0.2012 -0.0119 -0.0287 484 HOH   A O   
6944 O O   . HOH   D .   ? 0.5698 0.5108 0.3641 -0.0222 -0.0539 0.0453  485 HOH   A O   
6945 O O   . HOH   D .   ? 0.5958 0.6034 0.5607 -0.1820 -0.1433 0.0127  486 HOH   A O   
6946 O O   . HOH   D .   ? 0.5030 0.3455 0.5166 0.0581  -0.0293 -0.1125 487 HOH   A O   
6947 O O   . HOH   D .   ? 0.6416 0.3141 0.3820 -0.0117 -0.0372 0.0802  488 HOH   A O   
6948 O O   . HOH   D .   ? 0.8622 0.3890 0.3235 -0.0495 -0.1544 0.0122  489 HOH   A O   
6949 O O   . HOH   D .   ? 0.5336 0.5676 0.7705 -0.1418 0.0374  -0.0630 490 HOH   A O   
6950 O O   . HOH   D .   ? 0.3363 0.5130 0.3600 0.0075  -0.0497 -0.0313 491 HOH   A O   
6951 O O   . HOH   D .   ? 0.3229 0.4580 0.5346 0.0212  0.1732  0.1116  492 HOH   A O   
6952 O O   . HOH   D .   ? 0.5983 0.5369 0.4176 -0.0858 -0.0164 -0.0649 493 HOH   A O   
6953 O O   . HOH   D .   ? 0.6614 0.6672 0.7913 -0.0206 0.2182  -0.1369 494 HOH   A O   
6954 O O   . HOH   D .   ? 0.2751 0.2499 0.7261 0.0070  -0.1395 0.0114  495 HOH   A O   
6955 O O   . HOH   D .   ? 0.3902 0.3262 0.2402 -0.0793 0.0991  -0.0313 496 HOH   A O   
6956 O O   . HOH   D .   ? 0.8010 0.7524 0.5584 -0.0847 0.1743  0.1174  497 HOH   A O   
6957 O O   . HOH   D .   ? 0.2422 0.5027 0.3981 0.0996  0.0813  0.2584  498 HOH   A O   
6958 O O   . HOH   D .   ? 0.5428 0.4965 0.4393 -0.0107 0.0891  0.1384  499 HOH   A O   
6959 O O   . HOH   D .   ? 0.5589 0.6119 0.6467 0.1217  -0.1227 0.0260  500 HOH   A O   
6960 O O   . HOH   D .   ? 0.4595 0.3255 0.4747 -0.0205 0.2447  0.0522  501 HOH   A O   
6961 O O   . HOH   D .   ? 0.3179 0.2285 0.6669 0.0167  0.0911  0.0994  502 HOH   A O   
6962 O O   . HOH   D .   ? 0.2991 0.2636 0.6323 0.0024  0.0775  -0.0161 503 HOH   A O   
6963 O O   . HOH   D .   ? 0.6968 0.2580 0.4414 -0.0851 0.1038  0.0386  504 HOH   A O   
6964 O O   B HOH   D .   ? 0.2234 0.3270 0.2479 0.0012  0.0181  0.0453  505 HOH   A O   
6965 O O   B HOH   D .   ? 0.2956 0.2070 0.3529 -0.0219 -0.0107 -0.0245 506 HOH   A O   
6966 O O   . HOH   D .   ? 0.4992 0.2481 0.5105 -0.1641 -0.0025 0.0311  507 HOH   A O   
6967 O O   . HOH   D .   ? 0.4330 0.9816 0.5363 -0.1442 -0.0582 0.1958  508 HOH   A O   
6968 O O   . HOH   D .   ? 0.2503 0.3381 0.3522 0.0344  -0.0656 0.0630  509 HOH   A O   
6969 O O   B HOH   D .   ? 0.2756 0.4343 0.2893 -0.0514 -0.0043 0.0270  510 HOH   A O   
6970 O O   . HOH   D .   ? 0.2848 0.4474 0.4550 -0.0071 -0.0955 -0.0052 511 HOH   A O   
6971 O O   . HOH   D .   ? 0.7442 0.8816 0.6945 0.2618  -0.1468 0.0446  512 HOH   A O   
6972 O O   . HOH   D .   ? 0.7390 0.8501 0.6114 0.1841  0.0736  0.2561  513 HOH   A O   
6973 O O   . HOH   D .   ? 0.4449 0.2359 0.3677 -0.0230 -0.1442 0.0088  514 HOH   A O   
6974 O O   B HOH   D .   ? 0.4866 0.2763 0.3660 -0.1219 0.1324  0.0249  515 HOH   A O   
6975 O O   . HOH   D .   ? 0.3111 0.2335 0.5527 0.0209  0.0470  0.0673  516 HOH   A O   
6976 O O   . HOH   D .   ? 0.5617 0.7118 0.5003 0.3593  -0.0351 0.0640  517 HOH   A O   
6977 O O   . HOH   D .   ? 0.7051 0.8638 0.4858 -0.1086 -0.1240 -0.1153 518 HOH   A O   
6978 O O   A HOH   D .   ? 0.2941 0.4673 0.1772 0.0805  0.0054  0.1158  519 HOH   A O   
6979 O O   . HOH   D .   ? 0.4597 0.8172 0.5638 0.1995  0.0256  -0.0952 520 HOH   A O   
6980 O O   . HOH   D .   ? 0.5465 0.7417 0.5383 -0.0472 -0.0230 0.1107  521 HOH   A O   
6981 O O   . HOH   D .   ? 0.5740 0.5515 0.5302 0.1371  0.0922  0.1611  522 HOH   A O   
6982 O O   B HOH   D .   ? 0.2990 0.2729 0.4145 -0.0138 0.0050  0.1278  523 HOH   A O   
6983 O O   . HOH   D .   ? 0.3317 0.5392 0.6013 -0.0601 -0.0648 0.3285  524 HOH   A O   
6984 O O   . HOH   E .   ? 0.2505 0.2294 0.3144 0.0188  0.0996  0.0393  201 HOH   B O   
6985 O O   . HOH   E .   ? 0.4983 0.3437 0.4362 -0.0474 0.0154  -0.1713 202 HOH   B O   
6986 O O   . HOH   E .   ? 0.3235 0.2870 0.6764 -0.0045 0.0058  0.0454  203 HOH   B O   
6987 O O   . HOH   E .   ? 0.3291 0.7287 0.3432 0.0310  -0.0067 0.2252  204 HOH   B O   
6988 O O   . HOH   E .   ? 0.7091 0.3827 0.4533 -0.0264 0.0454  -0.0349 205 HOH   B O   
6989 O O   . HOH   E .   ? 0.6624 0.6365 0.5566 0.2015  0.1109  0.0725  206 HOH   B O   
6990 O O   . HOH   E .   ? 0.2633 0.2026 0.2672 0.0189  0.0318  0.0010  207 HOH   B O   
6991 O O   . HOH   E .   ? 0.3206 0.2168 0.4927 0.0420  0.1911  0.1105  208 HOH   B O   
6992 O O   . HOH   E .   ? 0.3587 0.5863 0.6465 0.2196  0.0521  -0.0932 209 HOH   B O   
6993 O O   . HOH   E .   ? 0.5849 0.3774 0.6607 0.0727  -0.0894 0.2477  210 HOH   B O   
6994 O O   . HOH   E .   ? 0.3197 0.4101 0.5168 -0.1131 0.0535  -0.1523 211 HOH   B O   
6995 O O   . HOH   E .   ? 0.3362 0.4516 0.2488 -0.0433 -0.0032 -0.0991 212 HOH   B O   
6996 O O   . HOH   E .   ? 0.4083 0.4684 0.3482 0.1949  -0.0480 -0.0039 213 HOH   B O   
6997 O O   . HOH   E .   ? 0.2963 0.5616 0.5675 -0.0139 0.1672  -0.1956 214 HOH   B O   
6998 O O   . HOH   E .   ? 0.3052 0.4846 0.3465 -0.0346 -0.0993 0.0893  215 HOH   B O   
6999 O O   . HOH   E .   ? 0.4735 0.5951 0.3688 0.2739  -0.1218 -0.0219 216 HOH   B O   
7000 O O   . HOH   E .   ? 0.1574 0.2122 0.2953 -0.0293 -0.0094 0.0166  217 HOH   B O   
7001 O O   . HOH   E .   ? 0.5497 0.4454 0.4052 0.0409  0.0818  -0.1895 218 HOH   B O   
7002 O O   . HOH   E .   ? 0.3439 0.2336 0.5586 -0.0141 0.2192  0.0275  219 HOH   B O   
7003 O O   . HOH   E .   ? 0.1682 0.2054 0.3373 -0.0177 0.0152  -0.0148 220 HOH   B O   
7004 O O   . HOH   E .   ? 0.1541 0.1516 0.2322 -0.0199 0.0166  -0.0076 221 HOH   B O   
7005 O O   . HOH   E .   ? 0.3503 0.2616 0.4680 0.0690  -0.0410 -0.0603 222 HOH   B O   
7006 O O   . HOH   E .   ? 0.3082 0.3105 0.4657 0.0350  -0.0770 -0.0512 223 HOH   B O   
7007 O O   . HOH   E .   ? 0.3064 0.2469 0.6123 0.0765  -0.0798 0.0604  224 HOH   B O   
7008 O O   . HOH   E .   ? 0.2487 0.1696 0.2520 -0.0223 0.0928  -0.0058 225 HOH   B O   
7009 O O   . HOH   E .   ? 0.4055 0.3740 0.5054 -0.1456 0.0180  0.0572  226 HOH   B O   
7010 O O   . HOH   E .   ? 0.2762 0.4618 0.5387 0.1438  -0.0526 -0.1177 227 HOH   B O   
7011 O O   . HOH   E .   ? 0.3585 0.2500 0.4238 0.0436  -0.0731 -0.1249 228 HOH   B O   
7012 O O   . HOH   E .   ? 0.2343 0.2378 0.4327 -0.0373 -0.0100 -0.0665 229 HOH   B O   
7013 O O   . HOH   E .   ? 0.5058 0.2149 0.2984 0.0117  -0.0818 0.0037  230 HOH   B O   
7014 O O   . HOH   E .   ? 0.5751 0.3771 0.2759 -0.0506 0.0263  -0.0219 231 HOH   B O   
7015 O O   . HOH   E .   ? 0.5724 0.3088 0.3692 -0.1758 0.0045  0.0235  232 HOH   B O   
7016 O O   . HOH   E .   ? 0.6024 0.5523 0.3773 0.0871  0.1095  0.0088  233 HOH   B O   
7017 O O   . HOH   E .   ? 0.2394 0.2953 0.3134 0.0363  0.0307  -0.0845 234 HOH   B O   
7018 O O   . HOH   E .   ? 0.2372 0.1325 0.3244 0.0068  -0.0794 -0.0106 235 HOH   B O   
7019 O O   . HOH   E .   ? 0.2446 0.3812 0.3509 -0.0457 -0.0832 -0.0751 236 HOH   B O   
7020 O O   . HOH   E .   ? 0.2087 0.3793 0.2554 -0.0365 -0.0036 0.0863  237 HOH   B O   
7021 O O   . HOH   E .   ? 0.4661 0.4752 0.6572 0.0768  -0.1604 -0.1342 238 HOH   B O   
7022 O O   . HOH   E .   ? 0.5878 0.7004 0.4044 0.3386  0.0472  0.0755  239 HOH   B O   
7023 O O   . HOH   E .   ? 0.3370 0.5465 0.7696 0.0681  0.1664  0.0470  240 HOH   B O   
7024 O O   . HOH   E .   ? 0.3909 0.1886 0.1914 0.0323  -0.0921 -0.0127 241 HOH   B O   
7025 O O   . HOH   E .   ? 0.5087 0.3353 0.4120 -0.2363 0.0285  0.0029  242 HOH   B O   
7026 O O   . HOH   E .   ? 0.2537 0.2281 0.2441 0.0845  -0.0922 -0.0626 243 HOH   B O   
7027 O O   . HOH   E .   ? 0.2378 0.2478 0.3385 -0.0631 0.0008  -0.0190 244 HOH   B O   
7028 O O   . HOH   E .   ? 0.2822 0.3493 0.2383 -0.0617 0.0126  -0.0422 245 HOH   B O   
7029 O O   . HOH   E .   ? 0.1584 0.1440 0.1370 -0.0064 -0.0068 -0.0033 246 HOH   B O   
7030 O O   . HOH   E .   ? 0.2943 0.2210 0.3007 0.0861  0.0788  -0.0063 247 HOH   B O   
7031 O O   . HOH   E .   ? 0.1514 0.1339 0.1526 0.0001  -0.0039 0.0061  248 HOH   B O   
7032 O O   . HOH   E .   ? 0.1555 0.1575 0.2654 -0.0100 0.0199  -0.0091 249 HOH   B O   
7033 O O   . HOH   E .   ? 0.2180 0.1901 0.2050 -0.0223 -0.0439 0.0179  250 HOH   B O   
7034 O O   . HOH   E .   ? 0.3836 0.3553 0.2272 0.0111  0.0952  -0.0063 251 HOH   B O   
7035 O O   . HOH   E .   ? 0.2853 0.2192 0.1974 0.0297  -0.0157 -0.0154 252 HOH   B O   
7036 O O   . HOH   E .   ? 0.3904 0.3293 0.1915 0.0360  0.0487  0.0193  253 HOH   B O   
7037 O O   . HOH   E .   ? 0.2977 0.1806 0.6001 -0.0010 -0.1083 -0.0544 254 HOH   B O   
7038 O O   . HOH   E .   ? 0.2130 0.1566 0.1939 -0.0286 -0.0343 0.0242  255 HOH   B O   
7039 O O   . HOH   E .   ? 0.2268 0.2352 0.1968 0.0206  -0.0043 0.0004  256 HOH   B O   
7040 O O   . HOH   E .   ? 0.6427 0.5319 0.5386 0.1338  0.0527  -0.0686 257 HOH   B O   
7041 O O   . HOH   E .   ? 0.1815 0.2886 0.2630 0.0433  0.0564  0.0949  258 HOH   B O   
7042 O O   . HOH   E .   ? 0.3949 0.2895 0.3812 -0.0234 -0.0817 -0.0305 259 HOH   B O   
7043 O O   . HOH   E .   ? 0.3244 0.7707 0.7537 -0.0208 -0.0800 -0.0963 260 HOH   B O   
7044 O O   . HOH   E .   ? 0.1580 0.1714 0.3190 -0.0240 -0.0087 0.0109  261 HOH   B O   
7045 O O   . HOH   E .   ? 0.2734 0.3566 0.3439 -0.0709 -0.0356 -0.0348 262 HOH   B O   
7046 O O   . HOH   E .   ? 0.1423 0.1689 0.1925 -0.0079 0.0015  0.0165  263 HOH   B O   
7047 O O   . HOH   E .   ? 0.4379 0.4058 0.3275 0.0825  -0.0081 -0.1282 264 HOH   B O   
7048 O O   . HOH   E .   ? 0.2397 0.3253 0.2123 -0.0669 0.0364  0.0497  265 HOH   B O   
7049 O O   . HOH   E .   ? 0.2251 0.4873 0.4292 -0.0627 -0.0205 -0.1385 266 HOH   B O   
7050 O O   . HOH   E .   ? 0.3001 0.3786 0.4728 -0.0283 0.1875  -0.0383 267 HOH   B O   
7051 O O   . HOH   E .   ? 0.3375 0.2757 0.3302 -0.0484 0.0466  -0.0500 268 HOH   B O   
7052 O O   . HOH   E .   ? 0.2068 0.1634 0.2266 -0.0339 -0.0096 0.0212  269 HOH   B O   
7053 O O   . HOH   E .   ? 0.2262 0.2604 0.3253 -0.0137 0.0293  -0.0560 270 HOH   B O   
7054 O O   . HOH   E .   ? 0.2318 0.2644 0.2339 -0.0370 -0.0709 -0.0368 271 HOH   B O   
7055 O O   . HOH   E .   ? 0.2043 0.2035 0.3368 0.0061  -0.0491 -0.0386 272 HOH   B O   
7056 O O   . HOH   E .   ? 0.2507 0.2020 0.2840 -0.0485 0.0203  -0.0107 273 HOH   B O   
7057 O O   . HOH   E .   ? 0.5439 0.3719 0.3264 0.2506  0.1185  0.0871  274 HOH   B O   
7058 O O   . HOH   E .   ? 0.1925 0.1841 0.1602 -0.0496 -0.0451 0.0151  275 HOH   B O   
7059 O O   . HOH   E .   ? 0.2406 0.2604 0.2518 -0.0453 -0.0724 0.0213  276 HOH   B O   
7060 O O   . HOH   E .   ? 0.2228 0.2329 0.2624 0.0251  -0.0231 -0.0111 277 HOH   B O   
7061 O O   . HOH   E .   ? 0.3739 0.4092 0.4704 0.1349  -0.0804 -0.1420 278 HOH   B O   
7062 O O   . HOH   E .   ? 0.1760 0.1518 0.1669 0.0028  0.0152  0.0008  279 HOH   B O   
7063 O O   . HOH   E .   ? 0.3390 0.4798 0.3111 -0.0737 -0.0897 0.0884  280 HOH   B O   
7064 O O   . HOH   E .   ? 0.5489 0.5547 0.4924 0.2268  -0.0635 0.0415  281 HOH   B O   
7065 O O   . HOH   E .   ? 0.2924 0.4413 0.6232 0.0422  -0.0455 -0.1374 282 HOH   B O   
7066 O O   . HOH   E .   ? 0.2984 0.2133 0.4990 0.0281  0.0318  0.0559  283 HOH   B O   
7067 O O   . HOH   E .   ? 0.6039 0.7695 0.2679 -0.0503 -0.1686 0.0079  284 HOH   B O   
7068 O O   . HOH   E .   ? 0.1736 0.1533 0.3519 -0.0239 0.0046  -0.0023 285 HOH   B O   
7069 O O   . HOH   E .   ? 0.5376 0.3574 0.3333 -0.1236 0.0901  -0.1021 286 HOH   B O   
7070 O O   . HOH   E .   ? 0.3734 0.2282 0.4042 -0.0884 -0.2090 0.0876  287 HOH   B O   
7071 O O   . HOH   E .   ? 0.4333 0.2805 0.3944 -0.0038 -0.0307 -0.0926 288 HOH   B O   
7072 O O   . HOH   E .   ? 0.1837 0.1581 0.3006 -0.0054 -0.0164 -0.0064 289 HOH   B O   
7073 O O   . HOH   E .   ? 0.3574 0.2708 0.2095 0.0384  -0.0716 0.0077  290 HOH   B O   
7074 O O   . HOH   E .   ? 0.2577 0.2750 0.2883 -0.0047 -0.0846 0.0351  291 HOH   B O   
7075 O O   . HOH   E .   ? 0.1811 0.1996 0.2870 0.0188  0.0068  0.0086  292 HOH   B O   
7076 O O   . HOH   E .   ? 0.1642 0.1940 0.1536 -0.0033 -0.0180 0.0044  293 HOH   B O   
7077 O O   . HOH   E .   ? 0.2908 0.4742 0.5409 -0.1092 -0.1486 0.0791  294 HOH   B O   
7078 O O   . HOH   E .   ? 0.1891 0.3532 0.4842 0.0420  -0.0152 -0.1558 295 HOH   B O   
7079 O O   . HOH   E .   ? 0.3844 0.5689 0.3439 0.2117  -0.0469 -0.0358 296 HOH   B O   
7080 O O   . HOH   E .   ? 0.4567 0.5123 0.2325 0.0084  0.0853  0.0937  297 HOH   B O   
7081 O O   . HOH   E .   ? 0.2280 0.3198 0.6064 0.0649  -0.0502 -0.1544 298 HOH   B O   
7082 O O   . HOH   E .   ? 0.3142 0.3029 0.3230 -0.0201 0.0162  -0.1526 299 HOH   B O   
7083 O O   . HOH   E .   ? 0.3108 0.2850 0.5873 -0.0251 -0.0594 0.1316  300 HOH   B O   
7084 O O   . HOH   E .   ? 0.1653 0.1512 0.3275 0.0078  -0.0087 -0.0006 301 HOH   B O   
7085 O O   . HOH   E .   ? 0.4570 0.5687 0.4664 0.0248  -0.1860 0.0653  302 HOH   B O   
7086 O O   . HOH   E .   ? 0.1845 0.1666 0.2510 0.0160  0.0100  0.0328  303 HOH   B O   
7087 O O   . HOH   E .   ? 0.5087 0.3062 0.3228 0.0488  0.0469  0.0896  304 HOH   B O   
7088 O O   . HOH   E .   ? 0.3045 0.6787 0.2150 0.1343  -0.0497 -0.0672 305 HOH   B O   
7089 O O   . HOH   E .   ? 0.4514 0.4312 0.2346 0.1669  -0.0468 0.0662  306 HOH   B O   
7090 O O   . HOH   E .   ? 0.3045 0.3609 0.4719 -0.1073 0.1455  -0.0492 307 HOH   B O   
7091 O O   . HOH   E .   ? 0.2259 0.1664 0.2625 -0.0347 -0.0209 -0.0024 308 HOH   B O   
7092 O O   . HOH   E .   ? 0.3431 0.1827 0.3721 0.0597  0.1439  0.0576  309 HOH   B O   
7093 O O   . HOH   E .   ? 0.5076 0.2876 0.2354 -0.1808 0.0966  -0.0283 310 HOH   B O   
7094 O O   . HOH   E .   ? 0.4597 0.3611 0.4307 -0.0569 0.0658  0.1123  311 HOH   B O   
7095 O O   . HOH   E .   ? 0.2659 0.1565 0.2581 -0.0234 -0.0183 0.0324  312 HOH   B O   
7096 O O   . HOH   E .   ? 0.2263 0.3219 0.5330 -0.0338 -0.0558 -0.0196 313 HOH   B O   
7097 O O   . HOH   E .   ? 0.2787 0.3046 0.3400 -0.0290 0.1204  -0.0930 314 HOH   B O   
7098 O O   . HOH   E .   ? 0.5073 0.4501 0.2148 0.1209  -0.1001 -0.0353 315 HOH   B O   
7099 O O   . HOH   E .   ? 0.2018 0.1568 0.3515 0.0228  -0.0898 0.0137  316 HOH   B O   
7100 O O   . HOH   E .   ? 0.1650 0.1868 0.3149 -0.0192 -0.0028 0.0084  317 HOH   B O   
7101 O O   . HOH   E .   ? 0.1815 0.2664 0.2180 -0.0145 -0.0191 0.0598  318 HOH   B O   
7102 O O   . HOH   E .   ? 0.4061 0.2076 0.2745 0.1320  0.0959  0.0316  319 HOH   B O   
7103 O O   . HOH   E .   ? 0.2363 0.2599 0.5703 -0.0593 0.0010  0.1518  320 HOH   B O   
7104 O O   . HOH   E .   ? 0.3905 0.3741 0.8546 -0.0044 -0.0896 0.2160  321 HOH   B O   
7105 O O   . HOH   E .   ? 0.2243 0.5817 0.5338 -0.0998 -0.0033 -0.0066 322 HOH   B O   
7106 O O   . HOH   E .   ? 0.2197 0.2050 0.1879 -0.0092 0.0125  0.0186  323 HOH   B O   
7107 O O   . HOH   E .   ? 0.5470 0.4482 0.2755 0.0292  -0.0472 -0.0947 324 HOH   B O   
7108 O O   . HOH   E .   ? 0.5804 0.5546 0.6549 0.1511  -0.1316 0.2186  325 HOH   B O   
7109 O O   . HOH   E .   ? 0.1622 0.1690 0.3035 -0.0178 -0.0142 -0.0202 326 HOH   B O   
7110 O O   . HOH   E .   ? 0.1878 0.1874 0.2839 0.0306  0.0558  0.0131  327 HOH   B O   
7111 O O   . HOH   E .   ? 0.3107 0.3447 0.5824 -0.0604 -0.1934 0.1911  328 HOH   B O   
7112 O O   . HOH   E .   ? 0.3455 0.2406 0.2486 0.0452  -0.0211 0.0233  329 HOH   B O   
7113 O O   . HOH   E .   ? 0.7731 0.2039 0.3936 -0.0196 -0.0727 0.0146  330 HOH   B O   
7114 O O   . HOH   E .   ? 0.6163 0.5307 0.5584 0.1892  0.1598  0.0094  331 HOH   B O   
7115 O O   . HOH   E .   ? 0.2988 0.2021 0.5450 0.0207  -0.0083 0.0509  332 HOH   B O   
7116 O O   . HOH   E .   ? 0.6430 0.3867 0.4311 0.0971  0.1820  0.1907  333 HOH   B O   
7117 O O   . HOH   E .   ? 0.6176 0.6668 0.5650 -0.1287 -0.0772 0.1875  334 HOH   B O   
7118 O O   . HOH   E .   ? 0.4759 0.4093 0.6057 0.0793  -0.0278 -0.0014 335 HOH   B O   
7119 O O   . HOH   E .   ? 0.4818 0.3277 0.5476 0.1419  0.2476  0.1911  336 HOH   B O   
7120 O O   . HOH   E .   ? 0.2029 0.3142 0.3514 0.0422  -0.0159 -0.0867 337 HOH   B O   
7121 O O   . HOH   E .   ? 0.5252 0.3986 0.4636 -0.0018 0.0967  -0.1740 338 HOH   B O   
7122 O O   . HOH   E .   ? 0.5911 0.5016 0.6189 -0.0918 -0.1241 -0.1337 339 HOH   B O   
7123 O O   . HOH   E .   ? 0.4072 0.7252 0.3891 -0.0501 -0.0980 0.1384  340 HOH   B O   
7124 O O   . HOH   E .   ? 0.1810 0.1599 0.2307 0.0123  -0.0199 0.0165  341 HOH   B O   
7125 O O   . HOH   E .   ? 0.3286 0.4272 0.5622 -0.0016 0.1282  -0.0363 342 HOH   B O   
7126 O O   . HOH   E .   ? 0.5030 0.5814 0.3631 0.0348  -0.1024 -0.0154 343 HOH   B O   
7127 O O   . HOH   E .   ? 0.4987 0.3351 0.3007 0.0872  -0.1051 -0.0606 344 HOH   B O   
7128 O O   . HOH   E .   ? 0.4265 0.5744 0.4247 -0.0993 -0.1084 -0.0473 345 HOH   B O   
7129 O O   . HOH   E .   ? 0.2782 0.1889 0.4133 0.0437  -0.1125 -0.0621 346 HOH   B O   
7130 O O   . HOH   E .   ? 0.2150 0.2173 0.2905 -0.0201 0.0727  -0.0237 347 HOH   B O   
7131 O O   . HOH   E .   ? 0.4030 0.6227 0.5810 0.0145  -0.1117 0.1068  348 HOH   B O   
7132 O O   . HOH   E .   ? 0.5999 0.5341 0.6620 -0.1532 0.1049  0.1101  349 HOH   B O   
7133 O O   . HOH   E .   ? 0.7211 0.5832 0.3107 -0.0044 -0.0074 0.1157  350 HOH   B O   
7134 O O   . HOH   E .   ? 0.2872 0.2332 0.5378 -0.0319 -0.0971 -0.0586 351 HOH   B O   
7135 O O   . HOH   E .   ? 0.3625 0.4973 0.5094 -0.1799 0.0757  -0.0608 352 HOH   B O   
7136 O O   . HOH   E .   ? 0.4773 0.7203 0.8212 0.0970  0.0945  0.0563  353 HOH   B O   
7137 O O   . HOH   E .   ? 0.2557 0.3463 0.5531 0.0161  0.0467  -0.0025 354 HOH   B O   
7138 O O   . HOH   E .   ? 0.5011 0.2522 0.4575 -0.0605 0.1250  0.0196  355 HOH   B O   
7139 O O   . HOH   E .   ? 0.2260 0.5517 0.3144 0.1383  -0.0639 -0.1337 356 HOH   B O   
7140 O O   . HOH   E .   ? 0.3567 0.2244 0.3066 -0.0505 0.0206  -0.0898 357 HOH   B O   
7141 O O   . HOH   E .   ? 0.5057 0.3492 0.4399 -0.0248 0.1184  -0.1041 358 HOH   B O   
7142 O O   . HOH   E .   ? 0.3513 0.2799 0.4339 -0.0659 -0.0173 -0.0574 359 HOH   B O   
7143 O O   . HOH   E .   ? 0.5244 0.5559 0.5640 0.2256  -0.1481 0.1536  360 HOH   B O   
7144 O O   . HOH   E .   ? 0.6277 0.4061 0.5658 0.0865  0.1960  0.1214  361 HOH   B O   
7145 O O   . HOH   E .   ? 0.5778 0.3487 0.5219 0.0396  -0.1841 -0.0761 362 HOH   B O   
7146 O O   . HOH   E .   ? 0.2172 0.4042 0.6819 -0.0740 -0.0562 -0.0889 363 HOH   B O   
7147 O O   . HOH   E .   ? 0.3846 0.6699 0.3509 0.2252  -0.0237 -0.0119 364 HOH   B O   
7148 O O   . HOH   E .   ? 0.6059 0.4950 0.5012 0.0030  0.0027  0.0218  365 HOH   B O   
7149 O O   . HOH   E .   ? 0.6312 0.2481 0.2877 -0.0108 -0.0033 0.0568  366 HOH   B O   
7150 O O   . HOH   E .   ? 0.6882 0.4777 0.4043 0.1438  0.0086  0.0490  367 HOH   B O   
7151 O O   . HOH   E .   ? 0.6172 0.6616 0.3516 0.2113  -0.1356 0.1065  368 HOH   B O   
7152 O O   . HOH   E .   ? 0.2983 0.3766 0.5836 0.0526  -0.1519 -0.0407 369 HOH   B O   
7153 O O   . HOH   E .   ? 0.5429 0.5647 0.4892 0.0248  -0.0729 -0.1259 370 HOH   B O   
7154 O O   . HOH   E .   ? 0.4953 0.3209 0.5452 -0.1242 -0.0710 0.0199  371 HOH   B O   
7155 O O   . HOH   E .   ? 0.4112 0.5607 0.5936 0.2557  0.1181  0.1473  372 HOH   B O   
7156 O O   . HOH   E .   ? 0.8193 0.6879 0.5038 0.2934  -0.1531 -0.0291 373 HOH   B O   
7157 O O   . HOH   E .   ? 0.5932 0.4053 0.2823 -0.1105 -0.1032 -0.0487 374 HOH   B O   
7158 O O   . HOH   E .   ? 0.3772 0.3379 0.3008 0.0866  -0.0521 -0.0539 375 HOH   B O   
7159 O O   . HOH   E .   ? 0.4322 0.6678 0.6546 0.0909  0.0289  0.2658  376 HOH   B O   
7160 O O   . HOH   E .   ? 0.4311 0.5941 0.5283 -0.0688 -0.0564 0.0283  377 HOH   B O   
7161 O O   . HOH   E .   ? 0.2579 0.3903 0.4102 0.0484  -0.0481 -0.0690 378 HOH   B O   
7162 O O   . HOH   E .   ? 0.3043 0.5583 0.2310 0.0254  0.0232  -0.0003 379 HOH   B O   
7163 O O   . HOH   E .   ? 0.4597 0.7790 0.3993 -0.1643 0.0070  -0.1569 380 HOH   B O   
7164 O O   . HOH   E .   ? 0.3325 0.5668 0.5809 0.0811  -0.0903 0.0643  381 HOH   B O   
7165 O O   . HOH   E .   ? 0.5706 0.5977 0.6078 -0.0099 0.2434  0.1296  382 HOH   B O   
7166 O O   . HOH   E .   ? 0.6324 0.3356 0.6372 -0.1177 -0.1429 0.0245  383 HOH   B O   
7167 O O   . HOH   E .   ? 0.3407 0.8339 0.4175 0.1388  0.0587  0.1827  384 HOH   B O   
7168 O O   . HOH   E .   ? 0.2998 0.2689 0.3303 0.0078  0.0355  0.0203  385 HOH   B O   
7169 O O   . HOH   E .   ? 0.6078 0.3852 0.4159 0.0472  0.0334  -0.0952 386 HOH   B O   
7170 O O   . HOH   E .   ? 0.5854 0.4241 0.3175 -0.0070 0.0906  0.0087  387 HOH   B O   
7171 O O   . HOH   E .   ? 0.7395 0.5496 0.5076 0.2572  0.0530  -0.0079 388 HOH   B O   
7172 O O   . HOH   E .   ? 0.4948 0.6703 0.5171 0.0820  -0.1103 -0.0484 389 HOH   B O   
7173 O O   . HOH   E .   ? 0.6840 0.4403 0.5473 -0.0742 0.0462  0.0779  390 HOH   B O   
7174 O O   . HOH   E .   ? 0.2322 0.4383 0.4129 -0.0505 -0.0947 -0.0397 391 HOH   B O   
7175 O O   . HOH   E .   ? 0.3792 0.2396 0.3201 0.0807  -0.0407 0.0026  392 HOH   B O   
7176 O O   . HOH   E .   ? 0.4544 0.4695 0.3983 0.0040  0.0081  0.0424  393 HOH   B O   
7177 O O   . HOH   E .   ? 0.4499 0.2279 0.5770 -0.0478 0.0528  0.1217  394 HOH   B O   
7178 O O   . HOH   E .   ? 0.2469 0.3799 0.7377 -0.0919 -0.0957 0.0334  395 HOH   B O   
7179 O O   . HOH   E .   ? 0.3239 0.3827 0.3776 0.0488  0.0128  -0.0887 396 HOH   B O   
7180 O O   . HOH   E .   ? 0.5179 0.4650 0.4509 0.0969  0.1425  0.1138  397 HOH   B O   
7181 O O   . HOH   E .   ? 0.4019 0.7048 0.4461 0.0648  -0.0262 -0.1366 398 HOH   B O   
7182 O O   . HOH   E .   ? 0.2247 0.2748 0.5770 -0.0483 -0.0893 0.0171  399 HOH   B O   
7183 O O   . HOH   E .   ? 0.5695 0.4265 0.3344 -0.2459 -0.0631 0.0900  400 HOH   B O   
7184 O O   . HOH   E .   ? 0.5108 0.6466 0.5736 -0.0481 -0.1357 0.3416  401 HOH   B O   
7185 O O   . HOH   E .   ? 0.6822 0.5205 0.3764 0.0947  -0.0317 -0.0024 402 HOH   B O   
# 
