data_7HDL
# 
_entry.id   7HDL 
# 
_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   7HDL         pdb_00007hdl 10.2210/pdb7hdl/pdb 
WWPDB D_1001407339 ?            ?                   
# 
_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                        7HDL 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                              18178.766 2   
'3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'trifluoroacetic acid'                                                                  114.023   1   ? ? ? ? 
3 non-polymer syn '2-[(2R)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]-2,3-dihydro-1H-inden-2-ol' 320.388   1   ? ? ? ? 
4 water       nat water                                                                                   18.015    427 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                                                  TFA   
3 '2-[(2R)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]-2,3-dihydro-1H-inden-2-ol' A1A8J 
4 water                                                                                   HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A8J non-polymer         . '2-[(2R)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]-2,3-dihydro-1H-inden-2-ol' ? 
'C19 H20 N4 O'   320.388 
ALA   'L-peptide linking' y ALANINE                                                                                 ? 'C3 H7 N O2' 
89.093  
ARG   'L-peptide linking' y ARGININE                                                                                ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                              ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                         ? 'C4 H7 N O4' 
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                ? 
'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                               ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                         ? 'C5 H9 N O4' 
147.129 
GLY   'peptide linking'   y GLYCINE                                                                                 ? 'C2 H5 N O2' 
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                               ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                   ? 'H2 O' 
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                              ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                 ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                  ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                              ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                           ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                 ? 'C5 H9 N O2' 
115.130 
SER   'L-peptide linking' y SERINE                                                                                  ? 'C3 H7 N O3' 
105.093 
TFA   non-polymer         . 'trifluoroacetic acid'                                                                  ? 'C2 H F3 O2' 
114.023 
THR   'L-peptide linking' y THREONINE                                                                               ? 'C4 H9 N O3' 
119.119 
TYR   'L-peptide linking' y TYROSINE                                                                                ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                  ? 
'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TFA   1   201 201  TFA   TFA A . 
D 3 A1A8J 1   202 201  A1A8J LA1 A . 
E 4 HOH   1   301 292  HOH   HOH A . 
E 4 HOH   2   302 625  HOH   HOH A . 
E 4 HOH   3   303 229  HOH   HOH A . 
E 4 HOH   4   304 151  HOH   HOH A . 
E 4 HOH   5   305 196  HOH   HOH A . 
E 4 HOH   6   306 209  HOH   HOH A . 
E 4 HOH   7   307 964  HOH   HOH A . 
E 4 HOH   8   308 109  HOH   HOH A . 
E 4 HOH   9   309 5    HOH   HOH A . 
E 4 HOH   10  310 17   HOH   HOH A . 
E 4 HOH   11  311 1283 HOH   HOH A . 
E 4 HOH   12  312 93   HOH   HOH A . 
E 4 HOH   13  313 76   HOH   HOH A . 
E 4 HOH   14  314 247  HOH   HOH A . 
E 4 HOH   15  315 1295 HOH   HOH A . 
E 4 HOH   16  316 1290 HOH   HOH A . 
E 4 HOH   17  317 1284 HOH   HOH A . 
E 4 HOH   18  318 155  HOH   HOH A . 
E 4 HOH   19  319 136  HOH   HOH A . 
E 4 HOH   20  320 7    HOH   HOH A . 
E 4 HOH   21  321 1301 HOH   HOH A . 
E 4 HOH   22  322 124  HOH   HOH A . 
E 4 HOH   23  323 661  HOH   HOH A . 
E 4 HOH   24  324 337  HOH   HOH A . 
E 4 HOH   25  325 225  HOH   HOH A . 
E 4 HOH   26  326 86   HOH   HOH A . 
E 4 HOH   27  327 11   HOH   HOH A . 
E 4 HOH   28  328 18   HOH   HOH A . 
E 4 HOH   29  329 409  HOH   HOH A . 
E 4 HOH   30  330 15   HOH   HOH A . 
E 4 HOH   31  331 405  HOH   HOH A . 
E 4 HOH   32  332 630  HOH   HOH A . 
E 4 HOH   33  333 393  HOH   HOH A . 
E 4 HOH   34  334 140  HOH   HOH A . 
E 4 HOH   35  335 236  HOH   HOH A . 
E 4 HOH   36  336 165  HOH   HOH A . 
E 4 HOH   37  337 21   HOH   HOH A . 
E 4 HOH   38  338 469  HOH   HOH A . 
E 4 HOH   39  339 164  HOH   HOH A . 
E 4 HOH   40  340 1310 HOH   HOH A . 
E 4 HOH   41  341 57   HOH   HOH A . 
E 4 HOH   42  342 241  HOH   HOH A . 
E 4 HOH   43  343 92   HOH   HOH A . 
E 4 HOH   44  344 1    HOH   HOH A . 
E 4 HOH   45  345 42   HOH   HOH A . 
E 4 HOH   46  346 33   HOH   HOH A . 
E 4 HOH   47  347 320  HOH   HOH A . 
E 4 HOH   48  348 39   HOH   HOH A . 
E 4 HOH   49  349 169  HOH   HOH A . 
E 4 HOH   50  350 939  HOH   HOH A . 
E 4 HOH   51  351 18   HOH   HOH A . 
E 4 HOH   52  352 153  HOH   HOH A . 
E 4 HOH   53  353 26   HOH   HOH A . 
E 4 HOH   54  354 81   HOH   HOH A . 
E 4 HOH   55  355 1300 HOH   HOH A . 
E 4 HOH   56  356 162  HOH   HOH A . 
E 4 HOH   57  357 354  HOH   HOH A . 
E 4 HOH   58  358 56   HOH   HOH A . 
E 4 HOH   59  359 138  HOH   HOH A . 
E 4 HOH   60  360 139  HOH   HOH A . 
E 4 HOH   61  361 105  HOH   HOH A . 
E 4 HOH   62  362 159  HOH   HOH A . 
E 4 HOH   63  363 102  HOH   HOH A . 
E 4 HOH   64  364 66   HOH   HOH A . 
E 4 HOH   65  365 2    HOH   HOH A . 
E 4 HOH   66  366 36   HOH   HOH A . 
E 4 HOH   67  367 662  HOH   HOH A . 
E 4 HOH   68  368 19   HOH   HOH A . 
E 4 HOH   69  369 461  HOH   HOH A . 
E 4 HOH   70  370 366  HOH   HOH A . 
E 4 HOH   71  371 192  HOH   HOH A . 
E 4 HOH   72  372 134  HOH   HOH A . 
E 4 HOH   73  373 5    HOH   HOH A . 
E 4 HOH   74  374 396  HOH   HOH A . 
E 4 HOH   75  375 17   HOH   HOH A . 
E 4 HOH   76  376 45   HOH   HOH A . 
E 4 HOH   77  377 12   HOH   HOH A . 
E 4 HOH   78  378 62   HOH   HOH A . 
E 4 HOH   79  379 148  HOH   HOH A . 
E 4 HOH   80  380 46   HOH   HOH A . 
E 4 HOH   81  381 49   HOH   HOH A . 
E 4 HOH   82  382 218  HOH   HOH A . 
E 4 HOH   83  383 85   HOH   HOH A . 
E 4 HOH   84  384 3    HOH   HOH A . 
E 4 HOH   85  385 1308 HOH   HOH A . 
E 4 HOH   86  386 186  HOH   HOH A . 
E 4 HOH   87  387 35   HOH   HOH A . 
E 4 HOH   88  388 34   HOH   HOH A . 
E 4 HOH   89  389 13   HOH   HOH A . 
E 4 HOH   90  390 333  HOH   HOH A . 
E 4 HOH   91  391 58   HOH   HOH A . 
E 4 HOH   92  392 140  HOH   HOH A . 
E 4 HOH   93  393 116  HOH   HOH A . 
E 4 HOH   94  394 27   HOH   HOH A . 
E 4 HOH   95  395 303  HOH   HOH A . 
E 4 HOH   96  396 115  HOH   HOH A . 
E 4 HOH   97  397 493  HOH   HOH A . 
E 4 HOH   98  398 83   HOH   HOH A . 
E 4 HOH   99  399 1315 HOH   HOH A . 
E 4 HOH   100 400 199  HOH   HOH A . 
E 4 HOH   101 401 24   HOH   HOH A . 
E 4 HOH   102 402 132  HOH   HOH A . 
E 4 HOH   103 403 6    HOH   HOH A . 
E 4 HOH   104 404 25   HOH   HOH A . 
E 4 HOH   105 405 154  HOH   HOH A . 
E 4 HOH   106 406 296  HOH   HOH A . 
E 4 HOH   107 407 1275 HOH   HOH A . 
E 4 HOH   108 408 68   HOH   HOH A . 
E 4 HOH   109 409 1068 HOH   HOH A . 
E 4 HOH   110 410 67   HOH   HOH A . 
E 4 HOH   111 411 121  HOH   HOH A . 
E 4 HOH   112 412 278  HOH   HOH A . 
E 4 HOH   113 413 281  HOH   HOH A . 
E 4 HOH   114 414 123  HOH   HOH A . 
E 4 HOH   115 415 78   HOH   HOH A . 
E 4 HOH   116 416 351  HOH   HOH A . 
E 4 HOH   117 417 4    HOH   HOH A . 
E 4 HOH   118 418 125  HOH   HOH A . 
E 4 HOH   119 419 122  HOH   HOH A . 
E 4 HOH   120 420 1222 HOH   HOH A . 
E 4 HOH   121 421 15   HOH   HOH A . 
E 4 HOH   122 422 51   HOH   HOH A . 
E 4 HOH   123 423 74   HOH   HOH A . 
E 4 HOH   124 424 8    HOH   HOH A . 
E 4 HOH   125 425 53   HOH   HOH A . 
E 4 HOH   126 426 397  HOH   HOH A . 
E 4 HOH   127 427 1296 HOH   HOH A . 
E 4 HOH   128 428 156  HOH   HOH A . 
E 4 HOH   129 429 195  HOH   HOH A . 
E 4 HOH   130 430 1289 HOH   HOH A . 
E 4 HOH   131 431 95   HOH   HOH A . 
E 4 HOH   132 432 12   HOH   HOH A . 
E 4 HOH   133 433 70   HOH   HOH A . 
E 4 HOH   134 434 16   HOH   HOH A . 
E 4 HOH   135 435 381  HOH   HOH A . 
E 4 HOH   136 436 6    HOH   HOH A . 
E 4 HOH   137 437 1313 HOH   HOH A . 
E 4 HOH   138 438 7    HOH   HOH A . 
E 4 HOH   139 439 582  HOH   HOH A . 
E 4 HOH   140 440 3    HOH   HOH A . 
E 4 HOH   141 441 952  HOH   HOH A . 
E 4 HOH   142 442 1279 HOH   HOH A . 
E 4 HOH   143 443 1189 HOH   HOH A . 
E 4 HOH   144 444 1134 HOH   HOH A . 
E 4 HOH   145 445 14   HOH   HOH A . 
E 4 HOH   146 446 71   HOH   HOH A . 
E 4 HOH   147 447 10   HOH   HOH A . 
E 4 HOH   148 448 1238 HOH   HOH A . 
E 4 HOH   149 449 1309 HOH   HOH A . 
E 4 HOH   150 450 80   HOH   HOH A . 
E 4 HOH   151 451 73   HOH   HOH A . 
E 4 HOH   152 452 40   HOH   HOH A . 
E 4 HOH   153 453 212  HOH   HOH A . 
E 4 HOH   154 454 104  HOH   HOH A . 
E 4 HOH   155 455 94   HOH   HOH A . 
E 4 HOH   156 456 79   HOH   HOH A . 
E 4 HOH   157 457 576  HOH   HOH A . 
E 4 HOH   158 458 1286 HOH   HOH A . 
E 4 HOH   159 459 1094 HOH   HOH A . 
E 4 HOH   160 460 944  HOH   HOH A . 
E 4 HOH   161 461 9    HOH   HOH A . 
E 4 HOH   162 462 97   HOH   HOH A . 
E 4 HOH   163 463 16   HOH   HOH A . 
E 4 HOH   164 464 188  HOH   HOH A . 
E 4 HOH   165 465 96   HOH   HOH A . 
E 4 HOH   166 466 330  HOH   HOH A . 
E 4 HOH   167 467 726  HOH   HOH A . 
E 4 HOH   168 468 1119 HOH   HOH A . 
E 4 HOH   169 469 509  HOH   HOH A . 
E 4 HOH   170 470 107  HOH   HOH A . 
E 4 HOH   171 471 408  HOH   HOH A . 
E 4 HOH   172 472 163  HOH   HOH A . 
E 4 HOH   173 473 4    HOH   HOH A . 
E 4 HOH   174 474 756  HOH   HOH A . 
E 4 HOH   175 475 556  HOH   HOH A . 
E 4 HOH   176 476 280  HOH   HOH A . 
E 4 HOH   177 477 319  HOH   HOH A . 
E 4 HOH   178 478 801  HOH   HOH A . 
E 4 HOH   179 479 1276 HOH   HOH A . 
E 4 HOH   180 480 361  HOH   HOH A . 
E 4 HOH   181 481 63   HOH   HOH A . 
E 4 HOH   182 482 126  HOH   HOH A . 
E 4 HOH   183 483 1307 HOH   HOH A . 
E 4 HOH   184 484 521  HOH   HOH A . 
E 4 HOH   185 485 224  HOH   HOH A . 
E 4 HOH   186 486 267  HOH   HOH A . 
E 4 HOH   187 487 250  HOH   HOH A . 
E 4 HOH   188 488 342  HOH   HOH A . 
E 4 HOH   189 489 370  HOH   HOH A . 
E 4 HOH   190 490 202  HOH   HOH A . 
E 4 HOH   191 491 1287 HOH   HOH A . 
E 4 HOH   192 492 1306 HOH   HOH A . 
E 4 HOH   193 493 326  HOH   HOH A . 
E 4 HOH   194 494 674  HOH   HOH A . 
E 4 HOH   195 495 1314 HOH   HOH A . 
E 4 HOH   196 496 695  HOH   HOH A . 
E 4 HOH   197 497 919  HOH   HOH A . 
E 4 HOH   198 498 315  HOH   HOH A . 
E 4 HOH   199 499 135  HOH   HOH A . 
E 4 HOH   200 500 309  HOH   HOH A . 
E 4 HOH   201 501 331  HOH   HOH A . 
E 4 HOH   202 502 318  HOH   HOH A . 
E 4 HOH   203 503 1299 HOH   HOH A . 
E 4 HOH   204 504 805  HOH   HOH A . 
E 4 HOH   205 505 711  HOH   HOH A . 
E 4 HOH   206 506 941  HOH   HOH A . 
E 4 HOH   207 507 263  HOH   HOH A . 
E 4 HOH   208 508 208  HOH   HOH A . 
E 4 HOH   209 509 152  HOH   HOH A . 
E 4 HOH   210 510 180  HOH   HOH A . 
E 4 HOH   211 511 350  HOH   HOH A . 
E 4 HOH   212 512 8    HOH   HOH A . 
E 4 HOH   213 513 1071 HOH   HOH A . 
E 4 HOH   214 514 363  HOH   HOH A . 
E 4 HOH   215 515 371  HOH   HOH A . 
E 4 HOH   216 516 313  HOH   HOH A . 
E 4 HOH   217 517 356  HOH   HOH A . 
E 4 HOH   218 518 185  HOH   HOH A . 
E 4 HOH   219 519 2    HOH   HOH A . 
E 4 HOH   220 520 429  HOH   HOH A . 
E 4 HOH   221 521 772  HOH   HOH A . 
E 4 HOH   222 522 70   HOH   HOH A . 
E 4 HOH   223 523 376  HOH   HOH A . 
E 4 HOH   224 524 1074 HOH   HOH A . 
E 4 HOH   225 525 346  HOH   HOH A . 
E 4 HOH   226 526 1292 HOH   HOH A . 
E 4 HOH   227 527 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 531  HOH   HOH B . 
F 4 HOH   3   203 758  HOH   HOH B . 
F 4 HOH   4   204 654  HOH   HOH B . 
F 4 HOH   5   205 549  HOH   HOH B . 
F 4 HOH   6   206 358  HOH   HOH B . 
F 4 HOH   7   207 1249 HOH   HOH B . 
F 4 HOH   8   208 240  HOH   HOH B . 
F 4 HOH   9   209 900  HOH   HOH B . 
F 4 HOH   10  210 1278 HOH   HOH B . 
F 4 HOH   11  211 50   HOH   HOH B . 
F 4 HOH   12  212 232  HOH   HOH B . 
F 4 HOH   13  213 120  HOH   HOH B . 
F 4 HOH   14  214 353  HOH   HOH B . 
F 4 HOH   15  215 364  HOH   HOH B . 
F 4 HOH   16  216 343  HOH   HOH B . 
F 4 HOH   17  217 452  HOH   HOH B . 
F 4 HOH   18  218 332  HOH   HOH B . 
F 4 HOH   19  219 743  HOH   HOH B . 
F 4 HOH   20  220 264  HOH   HOH B . 
F 4 HOH   21  221 1140 HOH   HOH B . 
F 4 HOH   22  222 444  HOH   HOH B . 
F 4 HOH   23  223 131  HOH   HOH B . 
F 4 HOH   24  224 75   HOH   HOH B . 
F 4 HOH   25  225 398  HOH   HOH B . 
F 4 HOH   26  226 723  HOH   HOH B . 
F 4 HOH   27  227 325  HOH   HOH B . 
F 4 HOH   28  228 276  HOH   HOH B . 
F 4 HOH   29  229 69   HOH   HOH B . 
F 4 HOH   30  230 282  HOH   HOH B . 
F 4 HOH   31  231 205  HOH   HOH B . 
F 4 HOH   32  232 54   HOH   HOH B . 
F 4 HOH   33  233 166  HOH   HOH B . 
F 4 HOH   34  234 110  HOH   HOH B . 
F 4 HOH   35  235 127  HOH   HOH B . 
F 4 HOH   36  236 60   HOH   HOH B . 
F 4 HOH   37  237 144  HOH   HOH B . 
F 4 HOH   38  238 272  HOH   HOH B . 
F 4 HOH   39  239 300  HOH   HOH B . 
F 4 HOH   40  240 1    HOH   HOH B . 
F 4 HOH   41  241 30   HOH   HOH B . 
F 4 HOH   42  242 252  HOH   HOH B . 
F 4 HOH   43  243 231  HOH   HOH B . 
F 4 HOH   44  244 143  HOH   HOH B . 
F 4 HOH   45  245 14   HOH   HOH B . 
F 4 HOH   46  246 9    HOH   HOH B . 
F 4 HOH   47  247 129  HOH   HOH B . 
F 4 HOH   48  248 133  HOH   HOH B . 
F 4 HOH   49  249 82   HOH   HOH B . 
F 4 HOH   50  250 72   HOH   HOH B . 
F 4 HOH   51  251 391  HOH   HOH B . 
F 4 HOH   52  252 181  HOH   HOH B . 
F 4 HOH   53  253 347  HOH   HOH B . 
F 4 HOH   54  254 52   HOH   HOH B . 
F 4 HOH   55  255 103  HOH   HOH B . 
F 4 HOH   56  256 41   HOH   HOH B . 
F 4 HOH   57  257 47   HOH   HOH B . 
F 4 HOH   58  258 59   HOH   HOH B . 
F 4 HOH   59  259 128  HOH   HOH B . 
F 4 HOH   60  260 31   HOH   HOH B . 
F 4 HOH   61  261 387  HOH   HOH B . 
F 4 HOH   62  262 150  HOH   HOH B . 
F 4 HOH   63  263 341  HOH   HOH B . 
F 4 HOH   64  264 172  HOH   HOH B . 
F 4 HOH   65  265 10   HOH   HOH B . 
F 4 HOH   66  266 271  HOH   HOH B . 
F 4 HOH   67  267 216  HOH   HOH B . 
F 4 HOH   68  268 221  HOH   HOH B . 
F 4 HOH   69  269 242  HOH   HOH B . 
F 4 HOH   70  270 302  HOH   HOH B . 
F 4 HOH   71  271 77   HOH   HOH B . 
F 4 HOH   72  272 11   HOH   HOH B . 
F 4 HOH   73  273 147  HOH   HOH B . 
F 4 HOH   74  274 1277 HOH   HOH B . 
F 4 HOH   75  275 61   HOH   HOH B . 
F 4 HOH   76  276 20   HOH   HOH B . 
F 4 HOH   77  277 84   HOH   HOH B . 
F 4 HOH   78  278 117  HOH   HOH B . 
F 4 HOH   79  279 43   HOH   HOH B . 
F 4 HOH   80  280 243  HOH   HOH B . 
F 4 HOH   81  281 287  HOH   HOH B . 
F 4 HOH   82  282 1312 HOH   HOH B . 
F 4 HOH   83  283 89   HOH   HOH B . 
F 4 HOH   84  284 1305 HOH   HOH B . 
F 4 HOH   85  285 220  HOH   HOH B . 
F 4 HOH   86  286 114  HOH   HOH B . 
F 4 HOH   87  287 175  HOH   HOH B . 
F 4 HOH   88  288 13   HOH   HOH B . 
F 4 HOH   89  289 22   HOH   HOH B . 
F 4 HOH   90  290 88   HOH   HOH B . 
F 4 HOH   91  291 106  HOH   HOH B . 
F 4 HOH   92  292 235  HOH   HOH B . 
F 4 HOH   93  293 99   HOH   HOH B . 
F 4 HOH   94  294 311  HOH   HOH B . 
F 4 HOH   95  295 635  HOH   HOH B . 
F 4 HOH   96  296 1066 HOH   HOH B . 
F 4 HOH   97  297 299  HOH   HOH B . 
F 4 HOH   98  298 112  HOH   HOH B . 
F 4 HOH   99  299 137  HOH   HOH B . 
F 4 HOH   100 300 142  HOH   HOH B . 
F 4 HOH   101 301 316  HOH   HOH B . 
F 4 HOH   102 302 160  HOH   HOH B . 
F 4 HOH   103 303 101  HOH   HOH B . 
F 4 HOH   104 304 416  HOH   HOH B . 
F 4 HOH   105 305 1106 HOH   HOH B . 
F 4 HOH   106 306 38   HOH   HOH B . 
F 4 HOH   107 307 32   HOH   HOH B . 
F 4 HOH   108 308 215  HOH   HOH B . 
F 4 HOH   109 309 170  HOH   HOH B . 
F 4 HOH   110 310 297  HOH   HOH B . 
F 4 HOH   111 311 37   HOH   HOH B . 
F 4 HOH   112 312 1291 HOH   HOH B . 
F 4 HOH   113 313 91   HOH   HOH B . 
F 4 HOH   114 314 118  HOH   HOH B . 
F 4 HOH   115 315 28   HOH   HOH B . 
F 4 HOH   116 316 177  HOH   HOH B . 
F 4 HOH   117 317 48   HOH   HOH B . 
F 4 HOH   118 318 23   HOH   HOH B . 
F 4 HOH   119 319 100  HOH   HOH B . 
F 4 HOH   120 320 197  HOH   HOH B . 
F 4 HOH   121 321 1126 HOH   HOH B . 
F 4 HOH   122 322 1294 HOH   HOH B . 
F 4 HOH   123 323 29   HOH   HOH B . 
F 4 HOH   124 324 1274 HOH   HOH B . 
F 4 HOH   125 325 182  HOH   HOH B . 
F 4 HOH   126 326 44   HOH   HOH B . 
F 4 HOH   127 327 704  HOH   HOH B . 
F 4 HOH   128 328 161  HOH   HOH B . 
F 4 HOH   129 329 98   HOH   HOH B . 
F 4 HOH   130 330 1285 HOH   HOH B . 
F 4 HOH   131 331 717  HOH   HOH B . 
F 4 HOH   132 332 334  HOH   HOH B . 
F 4 HOH   133 333 207  HOH   HOH B . 
F 4 HOH   134 334 234  HOH   HOH B . 
F 4 HOH   135 335 141  HOH   HOH B . 
F 4 HOH   136 336 55   HOH   HOH B . 
F 4 HOH   137 337 65   HOH   HOH B . 
F 4 HOH   138 338 445  HOH   HOH B . 
F 4 HOH   139 339 339  HOH   HOH B . 
F 4 HOH   140 340 619  HOH   HOH B . 
F 4 HOH   141 341 1293 HOH   HOH B . 
F 4 HOH   142 342 362  HOH   HOH B . 
F 4 HOH   143 343 178  HOH   HOH B . 
F 4 HOH   144 344 960  HOH   HOH B . 
F 4 HOH   145 345 90   HOH   HOH B . 
F 4 HOH   146 346 1304 HOH   HOH B . 
F 4 HOH   147 347 463  HOH   HOH B . 
F 4 HOH   148 348 1046 HOH   HOH B . 
F 4 HOH   149 349 87   HOH   HOH B . 
F 4 HOH   150 350 623  HOH   HOH B . 
F 4 HOH   151 351 191  HOH   HOH B . 
F 4 HOH   152 352 335  HOH   HOH B . 
F 4 HOH   153 353 304  HOH   HOH B . 
F 4 HOH   154 354 541  HOH   HOH B . 
F 4 HOH   155 355 203  HOH   HOH B . 
F 4 HOH   156 356 1280 HOH   HOH B . 
F 4 HOH   157 357 290  HOH   HOH B . 
F 4 HOH   158 358 1077 HOH   HOH B . 
F 4 HOH   159 359 389  HOH   HOH B . 
F 4 HOH   160 360 479  HOH   HOH B . 
F 4 HOH   161 361 718  HOH   HOH B . 
F 4 HOH   162 362 1072 HOH   HOH B . 
F 4 HOH   163 363 283  HOH   HOH B . 
F 4 HOH   164 364 615  HOH   HOH B . 
F 4 HOH   165 365 291  HOH   HOH B . 
F 4 HOH   166 366 1316 HOH   HOH B . 
F 4 HOH   167 367 898  HOH   HOH B . 
F 4 HOH   168 368 1303 HOH   HOH B . 
F 4 HOH   169 369 340  HOH   HOH B . 
F 4 HOH   170 370 373  HOH   HOH B . 
F 4 HOH   171 371 667  HOH   HOH B . 
F 4 HOH   172 372 310  HOH   HOH B . 
F 4 HOH   173 373 190  HOH   HOH B . 
F 4 HOH   174 374 431  HOH   HOH B . 
F 4 HOH   175 375 149  HOH   HOH B . 
F 4 HOH   176 376 183  HOH   HOH B . 
F 4 HOH   177 377 1163 HOH   HOH B . 
F 4 HOH   178 378 1173 HOH   HOH B . 
F 4 HOH   179 379 1000 HOH   HOH B . 
F 4 HOH   180 380 418  HOH   HOH B . 
F 4 HOH   181 381 1311 HOH   HOH B . 
F 4 HOH   182 382 176  HOH   HOH B . 
F 4 HOH   183 383 424  HOH   HOH B . 
F 4 HOH   184 384 470  HOH   HOH B . 
F 4 HOH   185 385 981  HOH   HOH B . 
F 4 HOH   186 386 265  HOH   HOH B . 
F 4 HOH   187 387 248  HOH   HOH B . 
F 4 HOH   188 388 1298 HOH   HOH B . 
F 4 HOH   189 389 491  HOH   HOH B . 
F 4 HOH   190 390 184  HOH   HOH B . 
F 4 HOH   191 391 360  HOH   HOH B . 
F 4 HOH   192 392 355  HOH   HOH B . 
F 4 HOH   193 393 410  HOH   HOH B . 
F 4 HOH   194 394 274  HOH   HOH B . 
F 4 HOH   195 395 566  HOH   HOH B . 
F 4 HOH   196 396 157  HOH   HOH B . 
F 4 HOH   197 397 314  HOH   HOH B . 
F 4 HOH   198 398 792  HOH   HOH B . 
F 4 HOH   199 399 321  HOH   HOH B . 
F 4 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HDL 
_cell.length_a           88.791 
_cell.length_b           88.791 
_cell.length_c           39.626 
_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                         7HDL 
_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          7HDL 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.85 
_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                     7HDL 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.400 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   166031 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.700 
_reflns.pdbx_Rmerge_I_obs            0.048 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.400 
_reflns.B_iso_Wilson_estimate        12.420 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.052 
_reflns.pdbx_Rpim_I_all              0.020 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1056814 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 34299 7733 ? 1.733 ? ? ? 4.400 ? 0.600  ? ? ? ? ? ? 93.900 1.965 0.906 0.476 
1 2 5.480 44.400 ? 7500  1099 ? 0.027 ? ? ? 6.800 ? 50.600 ? ? ? ? ? ? 99.900 0.030 0.011 0.999 
# 
_refine.entry_id                                 7HDL 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.4000 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.5400 
_refine.ls_number_reflns_obs                     165851 
_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                          0.1536 
_refine.ls_R_factor_R_work                       0.1528 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1688 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7991 
_refine.ls_number_reflns_R_work                  157860 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.3268 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1200 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                66.930 
_refine.B_iso_min                                9.130 
_refine.pdbx_overall_phase_error                 21.6100 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        44.4000 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.number_atoms_solvent             427 
_refine_hist.number_atoms_total               3020 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           14.52 
_refine_hist.pdbx_B_iso_mean_solvent          31.58 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 91.0000  4781 . 0.4821 0.4318 . 248 0.0000 5029 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 97.0000  5154 . 0.4026 0.4168 . 241 0.0000 5395 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5250 . 0.3581 0.3646 . 238 0.0000 5488 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5207 . 0.3179 0.3189 . 284 0.0000 5491 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5211 . 0.2937 0.3093 . 308 0.0000 5519 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5254 . 0.2724 0.3126 . 260 0.0000 5514 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5281 . 0.2441 0.2805 . 268 0.0000 5549 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5255 . 0.2201 0.2332 . 257 0.0000 5512 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5244 . 0.2072 0.2108 . 280 0.0000 5524 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5299 . 0.1895 0.1992 . 233 0.0000 5532 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5273 . 0.1722 0.1911 . 260 0.0000 5533 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5272 . 0.1595 0.1945 . 266 0.0000 5538 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5204 . 0.1471 0.1804 . 286 0.0000 5490 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5305 . 0.1403 0.1798 . 245 0.0000 5550 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5229 . 0.1392 0.1620 . 265 0.0000 5494 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5302 . 0.1357 0.1598 . 275 0.0000 5577 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5261 . 0.1351 0.1540 . 279 0.0000 5540 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5231 . 0.1330 0.1579 . 280 0.0000 5511 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5298 . 0.1355 0.1584 . 254 0.0000 5552 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5277 . 0.1311 0.1689 . 262 0.0000 5539 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5310 . 0.1280 0.1362 . 257 0.0000 5567 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5261 . 0.1221 0.1348 . 275 0.0000 5536 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5277 . 0.1229 0.1392 . 262 0.0000 5539 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5344 . 0.1283 0.1529 . 267 0.0000 5611 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5302 . 0.1346 0.1469 . 256 0.0000 5558 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5284 . 0.1351 0.1435 . 283 0.0000 5567 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5316 . 0.1403 0.1462 . 280 0.0000 5596 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5326 . 0.1404 0.1476 . 293 0.0000 5619 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5354 . 0.1510 0.1650 . 259 0.0000 5613 . 'X-RAY DIFFRACTION' 
3.1100 44.4000 30 100.0000 5498 . 0.1529 0.1764 . 270 0.0000 5768 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDL 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003731' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDL 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HDL A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDL 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 7HDL SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDL MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDL SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDL MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? PHE A 168 ? ASP A 157 PHE A 168 1 ? 12 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HDL 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   HD1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HIS 
_pdbx_validate_close_contact.auth_seq_id_1    91 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    302 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.59 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.60 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.84  -132.62 
2 1 SER A 128 ? B 62.72  70.00   
3 1 PHE A 156 ? B -98.95 39.13   
4 1 HIS B 86  ? ? 57.44  -128.60 
# 
_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 525 ? 5.92 . 
2 1 O ? A HOH 526 ? 5.98 . 
3 1 O ? A HOH 527 ? 7.60 . 
4 1 O ? B HOH 400 ? 6.26 . 
# 
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 
A1A8J N2   N Y N 1   
A1A8J C3   C N N 2   
A1A8J C6   C Y N 3   
A1A8J C9   C Y N 4   
A1A8J C12  C N N 5   
A1A8J C14  C Y N 6   
A1A8J C17  C Y N 7   
A1A8J C19  C N N 8   
A1A8J C1   C N N 9   
A1A8J C10  C Y N 10  
A1A8J C11  C Y N 11  
A1A8J C13  C Y N 12  
A1A8J C15  C Y N 13  
A1A8J C16  C Y N 14  
A1A8J C18  C Y N 15  
A1A8J C2   C N R 16  
A1A8J C4   C N N 17  
A1A8J C5   C N N 18  
A1A8J C7   C Y N 19  
A1A8J C8   C Y N 20  
A1A8J N1   N N N 21  
A1A8J N3   N Y N 22  
A1A8J N4   N Y N 23  
A1A8J O1   O N N 24  
A1A8J H3   H N N 25  
A1A8J H4   H N N 26  
A1A8J H13  H N N 27  
A1A8J H14  H N N 28  
A1A8J H15  H N N 29  
A1A8J H18  H N N 30  
A1A8J H20  H N N 31  
A1A8J H19  H N N 32  
A1A8J H10  H N N 33  
A1A8J H11  H N N 34  
A1A8J H16  H N N 35  
A1A8J H17  H N N 36  
A1A8J H1   H N N 37  
A1A8J H5   H N N 38  
A1A8J H6   H N N 39  
A1A8J H8   H N N 40  
A1A8J H7   H N N 41  
A1A8J H9   H N N 42  
A1A8J H12  H N N 43  
A1A8J H2   H N N 44  
ALA   N    N N N 45  
ALA   CA   C N S 46  
ALA   C    C N N 47  
ALA   O    O N N 48  
ALA   CB   C N N 49  
ALA   OXT  O N N 50  
ALA   H    H N N 51  
ALA   H2   H N N 52  
ALA   HA   H N N 53  
ALA   HB1  H N N 54  
ALA   HB2  H N N 55  
ALA   HB3  H N N 56  
ALA   HXT  H N N 57  
ARG   N    N N N 58  
ARG   CA   C N S 59  
ARG   C    C N N 60  
ARG   O    O N N 61  
ARG   CB   C N N 62  
ARG   CG   C N N 63  
ARG   CD   C N N 64  
ARG   NE   N N N 65  
ARG   CZ   C N N 66  
ARG   NH1  N N N 67  
ARG   NH2  N N N 68  
ARG   OXT  O N N 69  
ARG   H    H N N 70  
ARG   H2   H N N 71  
ARG   HA   H N N 72  
ARG   HB2  H N N 73  
ARG   HB3  H N N 74  
ARG   HG2  H N N 75  
ARG   HG3  H N N 76  
ARG   HD2  H N N 77  
ARG   HD3  H N N 78  
ARG   HE   H N N 79  
ARG   HH11 H N N 80  
ARG   HH12 H N N 81  
ARG   HH21 H N N 82  
ARG   HH22 H N N 83  
ARG   HXT  H N N 84  
ASN   N    N N N 85  
ASN   CA   C N S 86  
ASN   C    C N N 87  
ASN   O    O N N 88  
ASN   CB   C N N 89  
ASN   CG   C N N 90  
ASN   OD1  O N N 91  
ASN   ND2  N N N 92  
ASN   OXT  O N N 93  
ASN   H    H N N 94  
ASN   H2   H N N 95  
ASN   HA   H N N 96  
ASN   HB2  H N N 97  
ASN   HB3  H N N 98  
ASN   HD21 H N N 99  
ASN   HD22 H N N 100 
ASN   HXT  H N N 101 
ASP   N    N N N 102 
ASP   CA   C N S 103 
ASP   C    C N N 104 
ASP   O    O N N 105 
ASP   CB   C N N 106 
ASP   CG   C N N 107 
ASP   OD1  O N N 108 
ASP   OD2  O N N 109 
ASP   OXT  O N N 110 
ASP   H    H N N 111 
ASP   H2   H N N 112 
ASP   HA   H N N 113 
ASP   HB2  H N N 114 
ASP   HB3  H N N 115 
ASP   HD2  H N N 116 
ASP   HXT  H N N 117 
CYS   N    N N N 118 
CYS   CA   C N R 119 
CYS   C    C N N 120 
CYS   O    O N N 121 
CYS   CB   C N N 122 
CYS   SG   S N N 123 
CYS   OXT  O N N 124 
CYS   H    H N N 125 
CYS   H2   H N N 126 
CYS   HA   H N N 127 
CYS   HB2  H N N 128 
CYS   HB3  H N N 129 
CYS   HG   H N N 130 
CYS   HXT  H N N 131 
GLN   N    N N N 132 
GLN   CA   C N S 133 
GLN   C    C N N 134 
GLN   O    O N N 135 
GLN   CB   C N N 136 
GLN   CG   C N N 137 
GLN   CD   C N N 138 
GLN   OE1  O N N 139 
GLN   NE2  N N N 140 
GLN   OXT  O N N 141 
GLN   H    H N N 142 
GLN   H2   H N N 143 
GLN   HA   H N N 144 
GLN   HB2  H N N 145 
GLN   HB3  H N N 146 
GLN   HG2  H N N 147 
GLN   HG3  H N N 148 
GLN   HE21 H N N 149 
GLN   HE22 H N N 150 
GLN   HXT  H N N 151 
GLU   N    N N N 152 
GLU   CA   C N S 153 
GLU   C    C N N 154 
GLU   O    O N N 155 
GLU   CB   C N N 156 
GLU   CG   C N N 157 
GLU   CD   C N N 158 
GLU   OE1  O N N 159 
GLU   OE2  O N N 160 
GLU   OXT  O N N 161 
GLU   H    H N N 162 
GLU   H2   H N N 163 
GLU   HA   H N N 164 
GLU   HB2  H N N 165 
GLU   HB3  H N N 166 
GLU   HG2  H N N 167 
GLU   HG3  H N N 168 
GLU   HE2  H N N 169 
GLU   HXT  H N N 170 
GLY   N    N N N 171 
GLY   CA   C N N 172 
GLY   C    C N N 173 
GLY   O    O N N 174 
GLY   OXT  O N N 175 
GLY   H    H N N 176 
GLY   H2   H N N 177 
GLY   HA2  H N N 178 
GLY   HA3  H N N 179 
GLY   HXT  H N N 180 
HIS   N    N N N 181 
HIS   CA   C N S 182 
HIS   C    C N N 183 
HIS   O    O N N 184 
HIS   CB   C N N 185 
HIS   CG   C Y N 186 
HIS   ND1  N Y N 187 
HIS   CD2  C Y N 188 
HIS   CE1  C Y N 189 
HIS   NE2  N Y N 190 
HIS   OXT  O N N 191 
HIS   H    H N N 192 
HIS   H2   H N N 193 
HIS   HA   H N N 194 
HIS   HB2  H N N 195 
HIS   HB3  H N N 196 
HIS   HD1  H N N 197 
HIS   HD2  H N N 198 
HIS   HE1  H N N 199 
HIS   HE2  H N N 200 
HIS   HXT  H N N 201 
HOH   O    O N N 202 
HOH   H1   H N N 203 
HOH   H2   H N N 204 
ILE   N    N N N 205 
ILE   CA   C N S 206 
ILE   C    C N N 207 
ILE   O    O N N 208 
ILE   CB   C N S 209 
ILE   CG1  C N N 210 
ILE   CG2  C N N 211 
ILE   CD1  C N N 212 
ILE   OXT  O N N 213 
ILE   H    H N N 214 
ILE   H2   H N N 215 
ILE   HA   H N N 216 
ILE   HB   H N N 217 
ILE   HG12 H N N 218 
ILE   HG13 H N N 219 
ILE   HG21 H N N 220 
ILE   HG22 H N N 221 
ILE   HG23 H N N 222 
ILE   HD11 H N N 223 
ILE   HD12 H N N 224 
ILE   HD13 H N N 225 
ILE   HXT  H N N 226 
LEU   N    N N N 227 
LEU   CA   C N S 228 
LEU   C    C N N 229 
LEU   O    O N N 230 
LEU   CB   C N N 231 
LEU   CG   C N N 232 
LEU   CD1  C N N 233 
LEU   CD2  C N N 234 
LEU   OXT  O N N 235 
LEU   H    H N N 236 
LEU   H2   H N N 237 
LEU   HA   H N N 238 
LEU   HB2  H N N 239 
LEU   HB3  H N N 240 
LEU   HG   H N N 241 
LEU   HD11 H N N 242 
LEU   HD12 H N N 243 
LEU   HD13 H N N 244 
LEU   HD21 H N N 245 
LEU   HD22 H N N 246 
LEU   HD23 H N N 247 
LEU   HXT  H N N 248 
LYS   N    N N N 249 
LYS   CA   C N S 250 
LYS   C    C N N 251 
LYS   O    O N N 252 
LYS   CB   C N N 253 
LYS   CG   C N N 254 
LYS   CD   C N N 255 
LYS   CE   C N N 256 
LYS   NZ   N N N 257 
LYS   OXT  O N N 258 
LYS   H    H N N 259 
LYS   H2   H N N 260 
LYS   HA   H N N 261 
LYS   HB2  H N N 262 
LYS   HB3  H N N 263 
LYS   HG2  H N N 264 
LYS   HG3  H N N 265 
LYS   HD2  H N N 266 
LYS   HD3  H N N 267 
LYS   HE2  H N N 268 
LYS   HE3  H N N 269 
LYS   HZ1  H N N 270 
LYS   HZ2  H N N 271 
LYS   HZ3  H N N 272 
LYS   HXT  H N N 273 
MET   N    N N N 274 
MET   CA   C N S 275 
MET   C    C N N 276 
MET   O    O N N 277 
MET   CB   C N N 278 
MET   CG   C N N 279 
MET   SD   S N N 280 
MET   CE   C N N 281 
MET   OXT  O N N 282 
MET   H    H N N 283 
MET   H2   H N N 284 
MET   HA   H N N 285 
MET   HB2  H N N 286 
MET   HB3  H N N 287 
MET   HG2  H N N 288 
MET   HG3  H N N 289 
MET   HE1  H N N 290 
MET   HE2  H N N 291 
MET   HE3  H N N 292 
MET   HXT  H N N 293 
PHE   N    N N N 294 
PHE   CA   C N S 295 
PHE   C    C N N 296 
PHE   O    O N N 297 
PHE   CB   C N N 298 
PHE   CG   C Y N 299 
PHE   CD1  C Y N 300 
PHE   CD2  C Y N 301 
PHE   CE1  C Y N 302 
PHE   CE2  C Y N 303 
PHE   CZ   C Y N 304 
PHE   OXT  O N N 305 
PHE   H    H N N 306 
PHE   H2   H N N 307 
PHE   HA   H N N 308 
PHE   HB2  H N N 309 
PHE   HB3  H N N 310 
PHE   HD1  H N N 311 
PHE   HD2  H N N 312 
PHE   HE1  H N N 313 
PHE   HE2  H N N 314 
PHE   HZ   H N N 315 
PHE   HXT  H N N 316 
PRO   N    N N N 317 
PRO   CA   C N S 318 
PRO   C    C N N 319 
PRO   O    O N N 320 
PRO   CB   C N N 321 
PRO   CG   C N N 322 
PRO   CD   C N N 323 
PRO   OXT  O N N 324 
PRO   H    H N N 325 
PRO   HA   H N N 326 
PRO   HB2  H N N 327 
PRO   HB3  H N N 328 
PRO   HG2  H N N 329 
PRO   HG3  H N N 330 
PRO   HD2  H N N 331 
PRO   HD3  H N N 332 
PRO   HXT  H N N 333 
SER   N    N N N 334 
SER   CA   C N S 335 
SER   C    C N N 336 
SER   O    O N N 337 
SER   CB   C N N 338 
SER   OG   O N N 339 
SER   OXT  O N N 340 
SER   H    H N N 341 
SER   H2   H N N 342 
SER   HA   H N N 343 
SER   HB2  H N N 344 
SER   HB3  H N N 345 
SER   HG   H N N 346 
SER   HXT  H N N 347 
TFA   C1   C N N 348 
TFA   C2   C N N 349 
TFA   O    O N N 350 
TFA   F1   F N N 351 
TFA   F2   F N N 352 
TFA   F3   F N N 353 
TFA   OXT  O N N 354 
TFA   HXT  H N N 355 
THR   N    N N N 356 
THR   CA   C N S 357 
THR   C    C N N 358 
THR   O    O N N 359 
THR   CB   C N R 360 
THR   OG1  O N N 361 
THR   CG2  C N N 362 
THR   OXT  O N N 363 
THR   H    H N N 364 
THR   H2   H N N 365 
THR   HA   H N N 366 
THR   HB   H N N 367 
THR   HG1  H N N 368 
THR   HG21 H N N 369 
THR   HG22 H N N 370 
THR   HG23 H N N 371 
THR   HXT  H N N 372 
TYR   N    N N N 373 
TYR   CA   C N S 374 
TYR   C    C N N 375 
TYR   O    O N N 376 
TYR   CB   C N N 377 
TYR   CG   C Y N 378 
TYR   CD1  C Y N 379 
TYR   CD2  C Y N 380 
TYR   CE1  C Y N 381 
TYR   CE2  C Y N 382 
TYR   CZ   C Y N 383 
TYR   OH   O N N 384 
TYR   OXT  O N N 385 
TYR   H    H N N 386 
TYR   H2   H N N 387 
TYR   HA   H N N 388 
TYR   HB2  H N N 389 
TYR   HB3  H N N 390 
TYR   HD1  H N N 391 
TYR   HD2  H N N 392 
TYR   HE1  H N N 393 
TYR   HE2  H N N 394 
TYR   HH   H N N 395 
TYR   HXT  H N N 396 
VAL   N    N N N 397 
VAL   CA   C N S 398 
VAL   C    C N N 399 
VAL   O    O N N 400 
VAL   CB   C N N 401 
VAL   CG1  C N N 402 
VAL   CG2  C N N 403 
VAL   OXT  O N N 404 
VAL   H    H N N 405 
VAL   H2   H N N 406 
VAL   HA   H N N 407 
VAL   HB   H N N 408 
VAL   HG11 H N N 409 
VAL   HG12 H N N 410 
VAL   HG13 H N N 411 
VAL   HG21 H N N 412 
VAL   HG22 H N N 413 
VAL   HG23 H N N 414 
VAL   HXT  H N N 415 
# 
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 
A1A8J C15 C16  doub Y N 1   
A1A8J C15 C14  sing Y N 2   
A1A8J C16 C17  sing Y N 3   
A1A8J C14 C13  doub Y N 4   
A1A8J C17 C18  doub Y N 5   
A1A8J C13 C18  sing Y N 6   
A1A8J C13 C12  sing N N 7   
A1A8J C18 C19  sing N N 8   
A1A8J C4  C3   sing N N 9   
A1A8J C4  C5   sing N N 10  
A1A8J C3  C2   sing N N 11  
A1A8J C12 C1   sing N N 12  
A1A8J C19 C1   sing N N 13  
A1A8J C5  N1   sing N N 14  
A1A8J C2  C1   sing N N 15  
A1A8J C2  N1   sing N N 16  
A1A8J C1  O1   sing N N 17  
A1A8J N1  C6   sing N N 18  
A1A8J C6  N2   doub Y N 19  
A1A8J C6  C9   sing Y N 20  
A1A8J C10 C9   sing Y N 21  
A1A8J C10 C11  doub Y N 22  
A1A8J N2  C7   sing Y N 23  
A1A8J C9  C8   doub Y N 24  
A1A8J C11 N4   sing Y N 25  
A1A8J C7  N3   doub Y N 26  
A1A8J C8  N4   sing Y N 27  
A1A8J C8  N3   sing Y N 28  
A1A8J C3  H3   sing N N 29  
A1A8J C3  H4   sing N N 30  
A1A8J C12 H13  sing N N 31  
A1A8J C12 H14  sing N N 32  
A1A8J C14 H15  sing N N 33  
A1A8J C17 H18  sing N N 34  
A1A8J C19 H20  sing N N 35  
A1A8J C19 H19  sing N N 36  
A1A8J C10 H10  sing N N 37  
A1A8J C11 H11  sing N N 38  
A1A8J C15 H16  sing N N 39  
A1A8J C16 H17  sing N N 40  
A1A8J C2  H1   sing N N 41  
A1A8J C4  H5   sing N N 42  
A1A8J C4  H6   sing N N 43  
A1A8J C5  H8   sing N N 44  
A1A8J C5  H7   sing N N 45  
A1A8J C7  H9   sing N N 46  
A1A8J N4  H12  sing N N 47  
A1A8J O1  H2   sing N N 48  
ALA   N   CA   sing N N 49  
ALA   N   H    sing N N 50  
ALA   N   H2   sing N N 51  
ALA   CA  C    sing N N 52  
ALA   CA  CB   sing N N 53  
ALA   CA  HA   sing N N 54  
ALA   C   O    doub N N 55  
ALA   C   OXT  sing N N 56  
ALA   CB  HB1  sing N N 57  
ALA   CB  HB2  sing N N 58  
ALA   CB  HB3  sing N N 59  
ALA   OXT HXT  sing N N 60  
ARG   N   CA   sing N N 61  
ARG   N   H    sing N N 62  
ARG   N   H2   sing N N 63  
ARG   CA  C    sing N N 64  
ARG   CA  CB   sing N N 65  
ARG   CA  HA   sing N N 66  
ARG   C   O    doub N N 67  
ARG   C   OXT  sing N N 68  
ARG   CB  CG   sing N N 69  
ARG   CB  HB2  sing N N 70  
ARG   CB  HB3  sing N N 71  
ARG   CG  CD   sing N N 72  
ARG   CG  HG2  sing N N 73  
ARG   CG  HG3  sing N N 74  
ARG   CD  NE   sing N N 75  
ARG   CD  HD2  sing N N 76  
ARG   CD  HD3  sing N N 77  
ARG   NE  CZ   sing N N 78  
ARG   NE  HE   sing N N 79  
ARG   CZ  NH1  sing N N 80  
ARG   CZ  NH2  doub N N 81  
ARG   NH1 HH11 sing N N 82  
ARG   NH1 HH12 sing N N 83  
ARG   NH2 HH21 sing N N 84  
ARG   NH2 HH22 sing N N 85  
ARG   OXT HXT  sing N N 86  
ASN   N   CA   sing N N 87  
ASN   N   H    sing N N 88  
ASN   N   H2   sing N N 89  
ASN   CA  C    sing N N 90  
ASN   CA  CB   sing N N 91  
ASN   CA  HA   sing N N 92  
ASN   C   O    doub N N 93  
ASN   C   OXT  sing N N 94  
ASN   CB  CG   sing N N 95  
ASN   CB  HB2  sing N N 96  
ASN   CB  HB3  sing N N 97  
ASN   CG  OD1  doub N N 98  
ASN   CG  ND2  sing N N 99  
ASN   ND2 HD21 sing N N 100 
ASN   ND2 HD22 sing N N 101 
ASN   OXT HXT  sing N N 102 
ASP   N   CA   sing N N 103 
ASP   N   H    sing N N 104 
ASP   N   H2   sing N N 105 
ASP   CA  C    sing N N 106 
ASP   CA  CB   sing N N 107 
ASP   CA  HA   sing N N 108 
ASP   C   O    doub N N 109 
ASP   C   OXT  sing N N 110 
ASP   CB  CG   sing N N 111 
ASP   CB  HB2  sing N N 112 
ASP   CB  HB3  sing N N 113 
ASP   CG  OD1  doub N N 114 
ASP   CG  OD2  sing N N 115 
ASP   OD2 HD2  sing N N 116 
ASP   OXT HXT  sing N N 117 
CYS   N   CA   sing N N 118 
CYS   N   H    sing N N 119 
CYS   N   H2   sing N N 120 
CYS   CA  C    sing N N 121 
CYS   CA  CB   sing N N 122 
CYS   CA  HA   sing N N 123 
CYS   C   O    doub N N 124 
CYS   C   OXT  sing N N 125 
CYS   CB  SG   sing N N 126 
CYS   CB  HB2  sing N N 127 
CYS   CB  HB3  sing N N 128 
CYS   SG  HG   sing N N 129 
CYS   OXT HXT  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
HIS   N   CA   sing N N 177 
HIS   N   H    sing N N 178 
HIS   N   H2   sing N N 179 
HIS   CA  C    sing N N 180 
HIS   CA  CB   sing N N 181 
HIS   CA  HA   sing N N 182 
HIS   C   O    doub N N 183 
HIS   C   OXT  sing N N 184 
HIS   CB  CG   sing N N 185 
HIS   CB  HB2  sing N N 186 
HIS   CB  HB3  sing N N 187 
HIS   CG  ND1  sing Y N 188 
HIS   CG  CD2  doub Y N 189 
HIS   ND1 CE1  doub Y N 190 
HIS   ND1 HD1  sing N N 191 
HIS   CD2 NE2  sing Y N 192 
HIS   CD2 HD2  sing N N 193 
HIS   CE1 NE2  sing Y N 194 
HIS   CE1 HE1  sing N N 195 
HIS   NE2 HE2  sing N N 196 
HIS   OXT HXT  sing N N 197 
HOH   O   H1   sing N N 198 
HOH   O   H2   sing N N 199 
ILE   N   CA   sing N N 200 
ILE   N   H    sing N N 201 
ILE   N   H2   sing N N 202 
ILE   CA  C    sing N N 203 
ILE   CA  CB   sing N N 204 
ILE   CA  HA   sing N N 205 
ILE   C   O    doub N N 206 
ILE   C   OXT  sing N N 207 
ILE   CB  CG1  sing N N 208 
ILE   CB  CG2  sing N N 209 
ILE   CB  HB   sing N N 210 
ILE   CG1 CD1  sing N N 211 
ILE   CG1 HG12 sing N N 212 
ILE   CG1 HG13 sing N N 213 
ILE   CG2 HG21 sing N N 214 
ILE   CG2 HG22 sing N N 215 
ILE   CG2 HG23 sing N N 216 
ILE   CD1 HD11 sing N N 217 
ILE   CD1 HD12 sing N N 218 
ILE   CD1 HD13 sing N N 219 
ILE   OXT HXT  sing N N 220 
LEU   N   CA   sing N N 221 
LEU   N   H    sing N N 222 
LEU   N   H2   sing N N 223 
LEU   CA  C    sing N N 224 
LEU   CA  CB   sing N N 225 
LEU   CA  HA   sing N N 226 
LEU   C   O    doub N N 227 
LEU   C   OXT  sing N N 228 
LEU   CB  CG   sing N N 229 
LEU   CB  HB2  sing N N 230 
LEU   CB  HB3  sing N N 231 
LEU   CG  CD1  sing N N 232 
LEU   CG  CD2  sing N N 233 
LEU   CG  HG   sing N N 234 
LEU   CD1 HD11 sing N N 235 
LEU   CD1 HD12 sing N N 236 
LEU   CD1 HD13 sing N N 237 
LEU   CD2 HD21 sing N N 238 
LEU   CD2 HD22 sing N N 239 
LEU   CD2 HD23 sing N N 240 
LEU   OXT HXT  sing N N 241 
LYS   N   CA   sing N N 242 
LYS   N   H    sing N N 243 
LYS   N   H2   sing N N 244 
LYS   CA  C    sing N N 245 
LYS   CA  CB   sing N N 246 
LYS   CA  HA   sing N N 247 
LYS   C   O    doub N N 248 
LYS   C   OXT  sing N N 249 
LYS   CB  CG   sing N N 250 
LYS   CB  HB2  sing N N 251 
LYS   CB  HB3  sing N N 252 
LYS   CG  CD   sing N N 253 
LYS   CG  HG2  sing N N 254 
LYS   CG  HG3  sing N N 255 
LYS   CD  CE   sing N N 256 
LYS   CD  HD2  sing N N 257 
LYS   CD  HD3  sing N N 258 
LYS   CE  NZ   sing N N 259 
LYS   CE  HE2  sing N N 260 
LYS   CE  HE3  sing N N 261 
LYS   NZ  HZ1  sing N N 262 
LYS   NZ  HZ2  sing N N 263 
LYS   NZ  HZ3  sing N N 264 
LYS   OXT HXT  sing N N 265 
MET   N   CA   sing N N 266 
MET   N   H    sing N N 267 
MET   N   H2   sing N N 268 
MET   CA  C    sing N N 269 
MET   CA  CB   sing N N 270 
MET   CA  HA   sing N N 271 
MET   C   O    doub N N 272 
MET   C   OXT  sing N N 273 
MET   CB  CG   sing N N 274 
MET   CB  HB2  sing N N 275 
MET   CB  HB3  sing N N 276 
MET   CG  SD   sing N N 277 
MET   CG  HG2  sing N N 278 
MET   CG  HG3  sing N N 279 
MET   SD  CE   sing N N 280 
MET   CE  HE1  sing N N 281 
MET   CE  HE2  sing N N 282 
MET   CE  HE3  sing N N 283 
MET   OXT HXT  sing N N 284 
PHE   N   CA   sing N N 285 
PHE   N   H    sing N N 286 
PHE   N   H2   sing N N 287 
PHE   CA  C    sing N N 288 
PHE   CA  CB   sing N N 289 
PHE   CA  HA   sing N N 290 
PHE   C   O    doub N N 291 
PHE   C   OXT  sing N N 292 
PHE   CB  CG   sing N N 293 
PHE   CB  HB2  sing N N 294 
PHE   CB  HB3  sing N N 295 
PHE   CG  CD1  doub Y N 296 
PHE   CG  CD2  sing Y N 297 
PHE   CD1 CE1  sing Y N 298 
PHE   CD1 HD1  sing N N 299 
PHE   CD2 CE2  doub Y N 300 
PHE   CD2 HD2  sing N N 301 
PHE   CE1 CZ   doub Y N 302 
PHE   CE1 HE1  sing N N 303 
PHE   CE2 CZ   sing Y N 304 
PHE   CE2 HE2  sing N N 305 
PHE   CZ  HZ   sing N N 306 
PHE   OXT HXT  sing N N 307 
PRO   N   CA   sing N N 308 
PRO   N   CD   sing N N 309 
PRO   N   H    sing N N 310 
PRO   CA  C    sing N N 311 
PRO   CA  CB   sing N N 312 
PRO   CA  HA   sing N N 313 
PRO   C   O    doub N N 314 
PRO   C   OXT  sing N N 315 
PRO   CB  CG   sing N N 316 
PRO   CB  HB2  sing N N 317 
PRO   CB  HB3  sing N N 318 
PRO   CG  CD   sing N N 319 
PRO   CG  HG2  sing N N 320 
PRO   CG  HG3  sing N N 321 
PRO   CD  HD2  sing N N 322 
PRO   CD  HD3  sing N N 323 
PRO   OXT HXT  sing N N 324 
SER   N   CA   sing N N 325 
SER   N   H    sing N N 326 
SER   N   H2   sing N N 327 
SER   CA  C    sing N N 328 
SER   CA  CB   sing N N 329 
SER   CA  HA   sing N N 330 
SER   C   O    doub N N 331 
SER   C   OXT  sing N N 332 
SER   CB  OG   sing N N 333 
SER   CB  HB2  sing N N 334 
SER   CB  HB3  sing N N 335 
SER   OG  HG   sing N N 336 
SER   OXT HXT  sing N N 337 
TFA   C1  C2   sing N N 338 
TFA   C1  O    doub N N 339 
TFA   C1  OXT  sing N N 340 
TFA   C2  F1   sing N N 341 
TFA   C2  F2   sing N N 342 
TFA   C2  F3   sing N N 343 
TFA   OXT HXT  sing N N 344 
THR   N   CA   sing N N 345 
THR   N   H    sing N N 346 
THR   N   H2   sing N N 347 
THR   CA  C    sing N N 348 
THR   CA  CB   sing N N 349 
THR   CA  HA   sing N N 350 
THR   C   O    doub N N 351 
THR   C   OXT  sing N N 352 
THR   CB  OG1  sing N N 353 
THR   CB  CG2  sing N N 354 
THR   CB  HB   sing N N 355 
THR   OG1 HG1  sing N N 356 
THR   CG2 HG21 sing N N 357 
THR   CG2 HG22 sing N N 358 
THR   CG2 HG23 sing N N 359 
THR   OXT HXT  sing N N 360 
TYR   N   CA   sing N N 361 
TYR   N   H    sing N N 362 
TYR   N   H2   sing N N 363 
TYR   CA  C    sing N N 364 
TYR   CA  CB   sing N N 365 
TYR   CA  HA   sing N N 366 
TYR   C   O    doub N N 367 
TYR   C   OXT  sing N N 368 
TYR   CB  CG   sing N N 369 
TYR   CB  HB2  sing N N 370 
TYR   CB  HB3  sing N N 371 
TYR   CG  CD1  doub Y N 372 
TYR   CG  CD2  sing Y N 373 
TYR   CD1 CE1  sing Y N 374 
TYR   CD1 HD1  sing N N 375 
TYR   CD2 CE2  doub Y N 376 
TYR   CD2 HD2  sing N N 377 
TYR   CE1 CZ   doub Y N 378 
TYR   CE1 HE1  sing N N 379 
TYR   CE2 CZ   sing Y N 380 
TYR   CE2 HE2  sing N N 381 
TYR   CZ  OH   sing N N 382 
TYR   OH  HH   sing N N 383 
TYR   OXT HXT  sing N N 384 
VAL   N   CA   sing N N 385 
VAL   N   H    sing N N 386 
VAL   N   H2   sing N N 387 
VAL   CA  C    sing N N 388 
VAL   CA  CB   sing N N 389 
VAL   CA  HA   sing N N 390 
VAL   C   O    doub N N 391 
VAL   C   OXT  sing N N 392 
VAL   CB  CG1  sing N N 393 
VAL   CB  CG2  sing N N 394 
VAL   CB  HB   sing N N 395 
VAL   CG1 HG11 sing N N 396 
VAL   CG1 HG12 sing N N 397 
VAL   CG1 HG13 sing N N 398 
VAL   CG2 HG21 sing N N 399 
VAL   CG2 HG22 sing N N 400 
VAL   CG2 HG23 sing N N 401 
VAL   OXT HXT  sing N N 402 
# 
_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                    7HDL 
_atom_sites.fract_transf_matrix[1][1]   0.011262 
_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]   0.011262 
_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]   0.025236 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
F 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.654 -16.139 22.260  0.60 55.10 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.573 -16.108 22.396  0.40 54.82 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.669 -15.079 22.435  0.60 54.78 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.601 -15.031 22.535  0.40 54.53 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.301 -13.721 22.145  0.60 53.45 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.254 -13.690 22.223  0.40 53.33 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.436 -13.458 22.543  0.60 53.74 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.363 -13.410 22.678  0.40 53.65 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.041 -15.125 23.843  0.60 55.47 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 17.964 -15.029 23.939  0.40 55.12 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.002 -14.024 24.006  0.60 55.75 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 16.915 -13.931 24.049  0.40 55.39 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.416 -16.489 24.099  0.60 55.75 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.354 -16.388 24.246  0.40 55.37 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.954 -15.209 21.796  0.60 65.77 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.889 -15.166 21.894  0.40 65.46 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.734 -14.985 24.507  0.60 66.59 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.651 -14.853 24.600  0.40 66.18 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.508 -14.176 24.827  0.60 66.93 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.422 -14.049 24.876  0.40 66.49 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.452 -13.166 24.046  0.60 66.93 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.357 -13.068 24.050  0.40 66.49 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.397 -14.047 23.248  0.60 66.93 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.311 -13.995 23.293  0.40 66.49 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.963 -16.473 24.957  0.60 66.93 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.879 -16.337 25.090  0.40 66.47 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.780 -16.681 23.392  0.60 66.93 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.740 -16.626 23.534  0.40 66.47 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.115 -17.161 24.107  0.60 66.93 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.063 -17.047 24.305  0.40 66.47 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.562 -12.866 21.438  1.00 51.44 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.016 -11.520 21.112  1.00 47.43 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 17.868 -10.543 21.349  1.00 44.27 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.761 -10.934 21.733  1.00 44.23 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.576 -11.431 19.685  1.00 46.44 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.572 -11.842 18.631  1.00 45.52 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.431 -11.380 18.628  1.00 45.10 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 18.994 -12.718 17.725  1.00 45.17 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.779 -13.050 21.132  0.60 61.75 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.807 -13.071 21.078  0.40 61.75 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.735 -11.285 21.713  1.00 56.94 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 19.839 -10.513 19.507  1.00 55.76 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.346 -12.015 19.612  1.00 55.76 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.464 -12.985 17.103  1.00 54.23 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.800 -13.019 17.760  1.00 54.23 ?  4   ASN   A HD22 1 
ATOM   46   N N    . SER   A 1 5   ? 18.135 -9.258  21.114  1.00 40.95 ?  5   SER   A N    1 
ATOM   47   C CA   . SER   A 1 5   ? 17.219 -8.185  21.482  1.00 37.78 ?  5   SER   A CA   1 
ATOM   48   C C    . SER   A 1 5   ? 16.361 -7.691  20.320  1.00 33.37 ?  5   SER   A C    1 
ATOM   49   O O    . SER   A 1 5   ? 15.675 -6.674  20.462  1.00 33.78 ?  5   SER   A O    1 
ATOM   50   C CB   . SER   A 1 5   ? 17.989 -7.018  22.107  1.00 38.88 ?  5   SER   A CB   1 
ATOM   51   O OG   . SER   A 1 5   ? 18.863 -6.419  21.167  1.00 39.63 ?  5   SER   A OG   1 
ATOM   52   H H    . SER   A 1 5   ? 18.855 -8.983  20.730  1.00 49.16 ?  5   SER   A H    1 
ATOM   53   H HA   . SER   A 1 5   ? 16.616 -8.520  22.160  1.00 45.37 ?  5   SER   A HA   1 
ATOM   54   H HB2  . SER   A 1 5   ? 17.356 -6.350  22.418  1.00 46.69 ?  5   SER   A HB2  1 
ATOM   55   H HB3  . SER   A 1 5   ? 18.513 -7.346  22.858  1.00 46.69 ?  5   SER   A HB3  1 
ATOM   56   H HG   . SER   A 1 5   ? 19.277 -5.778  21.526  1.00 47.59 ?  5   SER   A HG   1 
ATOM   57   N N    . PHE   A 1 6   ? 16.376 -8.378  19.181  1.00 28.51 ?  6   PHE   A N    1 
ATOM   58   C CA   . PHE   A 1 6   ? 15.477 -8.019  18.089  1.00 24.38 ?  6   PHE   A CA   1 
ATOM   59   C C    . PHE   A 1 6   ? 14.047 -8.387  18.472  1.00 23.92 ?  6   PHE   A C    1 
ATOM   60   O O    . PHE   A 1 6   ? 13.791 -9.495  18.948  1.00 25.29 ?  6   PHE   A O    1 
ATOM   61   C CB   . PHE   A 1 6   ? 15.894 -8.746  16.815  1.00 21.84 ?  6   PHE   A CB   1 
ATOM   62   C CG   . PHE   A 1 6   ? 17.187 -8.238  16.225  1.00 20.51 ?  6   PHE   A CG   1 
ATOM   63   C CD1  . PHE   A 1 6   ? 17.215 -7.061  15.496  1.00 19.73 ?  6   PHE   A CD1  1 
ATOM   64   C CD2  . PHE   A 1 6   ? 18.367 -8.940  16.394  1.00 20.99 ?  6   PHE   A CD2  1 
ATOM   65   C CE1  . PHE   A 1 6   ? 18.392 -6.588  14.948  1.00 19.89 ?  6   PHE   A CE1  1 
ATOM   66   C CE2  . PHE   A 1 6   ? 19.547 -8.475  15.847  1.00 20.80 ?  6   PHE   A CE2  1 
ATOM   67   C CZ   . PHE   A 1 6   ? 19.559 -7.293  15.123  1.00 20.39 ?  6   PHE   A CZ   1 
ATOM   68   H H    . PHE   A 1 6   ? 16.885 -9.054  19.020  1.00 34.24 ?  6   PHE   A H    1 
ATOM   69   H HA   . PHE   A 1 6   ? 15.519 -7.068  17.935  1.00 29.28 ?  6   PHE   A HA   1 
ATOM   70   H HB2  . PHE   A 1 6   ? 16.006 -9.692  17.017  1.00 26.24 ?  6   PHE   A HB2  1 
ATOM   71   H HB3  . PHE   A 1 6   ? 15.196 -8.638  16.151  1.00 26.24 ?  6   PHE   A HB3  1 
ATOM   72   H HD1  . PHE   A 1 6   ? 16.424 -6.587  15.376  1.00 23.71 ?  6   PHE   A HD1  1 
ATOM   73   H HD2  . PHE   A 1 6   ? 18.364 -9.736  16.883  1.00 25.22 ?  6   PHE   A HD2  1 
ATOM   74   H HE1  . PHE   A 1 6   ? 18.391 -5.797  14.460  1.00 23.90 ?  6   PHE   A HE1  1 
ATOM   75   H HE2  . PHE   A 1 6   ? 20.336 -8.953  15.970  1.00 24.99 ?  6   PHE   A HE2  1 
ATOM   76   H HZ   . PHE   A 1 6   ? 20.350 -6.978  14.756  1.00 24.50 ?  6   PHE   A HZ   1 
ATOM   77   N N    A SER   A 1 7   ? 13.111 -7.465  18.236  0.60 22.82 ?  7   SER   A N    1 
ATOM   78   N N    B SER   A 1 7   ? 13.117 -7.449  18.289  0.40 23.49 ?  7   SER   A N    1 
ATOM   79   C CA   A SER   A 1 7   ? 11.735 -7.603  18.698  0.60 22.50 ?  7   SER   A CA   1 
ATOM   80   C CA   B SER   A 1 7   ? 11.763 -7.586  18.809  0.40 23.50 ?  7   SER   A CA   1 
ATOM   81   C C    A SER   A 1 7   ? 10.757 -7.410  17.545  0.60 20.28 ?  7   SER   A C    1 
ATOM   82   C C    B SER   A 1 7   ? 10.739 -7.304  17.719  0.40 22.07 ?  7   SER   A C    1 
ATOM   83   O O    A SER   A 1 7   ? 10.969 -6.561  16.674  0.60 20.13 ?  7   SER   A O    1 
ATOM   84   O O    B SER   A 1 7   ? 10.898 -6.368  16.930  0.40 21.95 ?  7   SER   A O    1 
ATOM   85   C CB   A SER   A 1 7   ? 11.438 -6.563  19.791  0.60 24.58 ?  7   SER   A CB   1 
ATOM   86   C CB   B SER   A 1 7   ? 11.535 -6.621  19.983  0.40 25.00 ?  7   SER   A CB   1 
ATOM   87   O OG   A SER   A 1 7   ? 10.101 -6.653  20.244  0.60 26.34 ?  7   SER   A OG   1 
ATOM   88   O OG   B SER   A 1 7   ? 10.228 -6.753  20.510  0.40 26.23 ?  7   SER   A OG   1 
ATOM   89   H H    A SER   A 1 7   ? 13.255 -6.738  17.801  0.60 27.41 ?  7   SER   A H    1 
ATOM   90   H H    B SER   A 1 7   ? 13.251 -6.717  17.859  0.40 28.22 ?  7   SER   A H    1 
ATOM   91   H HA   A SER   A 1 7   ? 11.603 -8.487  19.073  0.60 27.03 ?  7   SER   A HA   1 
ATOM   92   H HA   B SER   A 1 7   ? 11.625 -8.489  19.129  0.40 28.22 ?  7   SER   A HA   1 
ATOM   93   H HB2  A SER   A 1 7   ? 12.040 -6.713  20.539  0.60 29.52 ?  7   SER   A HB2  1 
ATOM   94   H HB2  B SER   A 1 7   ? 12.174 -6.823  20.685  0.40 30.03 ?  7   SER   A HB2  1 
ATOM   95   H HB3  A SER   A 1 7   ? 11.582 -5.676  19.427  0.60 29.52 ?  7   SER   A HB3  1 
ATOM   96   H HB3  B SER   A 1 7   ? 11.663 -5.710  19.673  0.40 30.03 ?  7   SER   A HB3  1 
ATOM   97   H HG   A SER   A 1 7   ? 9.963  -6.082  20.848  0.60 31.64 ?  7   SER   A HG   1 
ATOM   98   H HG   B SER   A 1 7   ? 10.117 -6.214  21.146  0.40 31.50 ?  7   SER   A HG   1 
ATOM   99   N N    A GLY   A 1 8   ? 9.681  -8.199  17.552  0.60 18.92 ?  8   GLY   A N    1 
ATOM   100  N N    B GLY   A 1 8   ? 9.683  -8.117  17.687  0.40 21.01 ?  8   GLY   A N    1 
ATOM   101  C CA   A GLY   A 1 8   ? 8.589  -7.991  16.621  0.60 18.03 ?  8   GLY   A CA   1 
ATOM   102  C CA   B GLY   A 1 8   ? 8.585  -7.890  16.769  0.40 20.04 ?  8   GLY   A CA   1 
ATOM   103  C C    A GLY   A 1 8   ? 8.818  -8.481  15.212  0.60 16.75 ?  8   GLY   A C    1 
ATOM   104  C C    B GLY   A 1 8   ? 8.816  -8.368  15.357  0.40 18.85 ?  8   GLY   A C    1 
ATOM   105  O O    A GLY   A 1 8   ? 8.076  -8.087  14.304  0.60 17.10 ?  8   GLY   A O    1 
ATOM   106  O O    B GLY   A 1 8   ? 8.092  -7.947  14.449  0.40 19.23 ?  8   GLY   A O    1 
ATOM   107  H H    A GLY   A 1 8   ? 9.563  -8.859  18.097  0.60 22.73 ?  8   GLY   A H    1 
ATOM   108  H H    B GLY   A 1 8   ? 9.585  -8.809  18.190  0.40 25.24 ?  8   GLY   A H    1 
ATOM   109  H HA2  A GLY   A 1 8   ? 7.800  -8.440  16.966  0.60 21.66 ?  8   GLY   A HA2  1 
ATOM   110  H HA2  B GLY   A 1 8   ? 7.794  -8.336  17.109  0.40 24.08 ?  8   GLY   A HA2  1 
ATOM   111  H HA3  A GLY   A 1 8   ? 8.395  -7.043  16.581  0.60 21.66 ?  8   GLY   A HA3  1 
ATOM   112  H HA3  B GLY   A 1 8   ? 8.400  -6.941  16.729  0.40 24.08 ?  8   GLY   A HA3  1 
ATOM   113  N N    A TYR   A 1 9   ? 9.813  -9.339  14.994  0.60 15.67 ?  9   TYR   A N    1 
ATOM   114  N N    B TYR   A 1 9   ? 9.800  -9.235  15.141  0.40 17.82 ?  9   TYR   A N    1 
ATOM   115  C CA   A TYR   A 1 9   ? 10.073 -9.866  13.664  0.60 14.32 ?  9   TYR   A CA   1 
ATOM   116  C CA   B TYR   A 1 9   ? 10.097 -9.753  13.815  0.40 16.57 ?  9   TYR   A CA   1 
ATOM   117  C C    A TYR   A 1 9   ? 9.178  -11.061 13.366  0.60 13.44 ?  9   TYR   A C    1 
ATOM   118  C C    B TYR   A 1 9   ? 9.344  -11.054 13.561  0.40 16.28 ?  9   TYR   A C    1 
ATOM   119  O O    A TYR   A 1 9   ? 8.891  -11.886 14.239  0.60 15.06 ?  9   TYR   A O    1 
ATOM   120  O O    B TYR   A 1 9   ? 9.151  -11.873 14.464  0.40 16.91 ?  9   TYR   A O    1 
ATOM   121  C CB   A TYR   A 1 9   ? 11.539 -10.289 13.524  0.60 14.64 ?  9   TYR   A CB   1 
ATOM   122  C CB   B TYR   A 1 9   ? 11.601 -10.006 13.665  0.40 16.00 ?  9   TYR   A CB   1 
ATOM   123  C CG   A TYR   A 1 9   ? 12.475 -9.118  13.361  0.60 14.57 ?  9   TYR   A CG   1 
ATOM   124  C CG   B TYR   A 1 9   ? 12.431 -8.753  13.469  0.40 15.35 ?  9   TYR   A CG   1 
ATOM   125  C CD1  A TYR   A 1 9   ? 12.839 -8.347  14.453  0.60 14.80 ?  9   TYR   A CD1  1 
ATOM   126  C CD1  B TYR   A 1 9   ? 12.649 -7.870  14.518  0.40 15.38 ?  9   TYR   A CD1  1 
ATOM   127  C CD2  A TYR   A 1 9   ? 12.967 -8.769  12.113  0.60 14.66 ?  9   TYR   A CD2  1 
ATOM   128  C CD2  B TYR   A 1 9   ? 12.995 -8.459  12.236  0.40 14.73 ?  9   TYR   A CD2  1 
ATOM   129  C CE1  A TYR   A 1 9   ? 13.673 -7.259  14.312  0.60 15.20 ?  9   TYR   A CE1  1 
ATOM   130  C CE1  B TYR   A 1 9   ? 13.401 -6.729  14.342  0.40 14.94 ?  9   TYR   A CE1  1 
ATOM   131  C CE2  A TYR   A 1 9   ? 13.804 -7.684  11.959  0.60 14.95 ?  9   TYR   A CE2  1 
ATOM   132  C CE2  B TYR   A 1 9   ? 13.749 -7.321  12.049  0.40 14.47 ?  9   TYR   A CE2  1 
ATOM   133  C CZ   A TYR   A 1 9   ? 14.151 -6.927  13.062  0.60 15.31 ?  9   TYR   A CZ   1 
ATOM   134  C CZ   B TYR   A 1 9   ? 13.948 -6.462  13.104  0.40 14.40 ?  9   TYR   A CZ   1 
ATOM   135  O OH   A TYR   A 1 9   ? 14.989 -5.849  12.910  0.60 16.72 ?  9   TYR   A OH   1 
ATOM   136  O OH   B TYR   A 1 9   ? 14.697 -5.324  12.913  0.40 14.79 ?  9   TYR   A OH   1 
ATOM   137  H H    A TYR   A 1 9   ? 10.342 -9.640  15.604  0.60 18.83 ?  9   TYR   A H    1 
ATOM   138  H H    B TYR   A 1 9   ? 10.315 -9.547  15.756  0.40 21.41 ?  9   TYR   A H    1 
ATOM   139  H HA   A TYR   A 1 9   ? 9.893  -9.175  13.006  0.60 17.21 ?  9   TYR   A HA   1 
ATOM   140  H HA   B TYR   A 1 9   ? 9.832  -9.106  13.145  0.40 19.91 ?  9   TYR   A HA   1 
ATOM   141  H HB2  A TYR   A 1 9   ? 11.804 -10.784 14.317  0.60 17.60 ?  9   TYR   A HB2  1 
ATOM   142  H HB2  B TYR   A 1 9   ? 11.925 -10.456 14.463  0.40 19.23 ?  9   TYR   A HB2  1 
ATOM   143  H HB3  A TYR   A 1 9   ? 11.618 -10.855 12.740  0.60 17.60 ?  9   TYR   A HB3  1 
ATOM   144  H HB3  B TYR   A 1 9   ? 11.741 -10.574 12.892  0.40 19.23 ?  9   TYR   A HB3  1 
ATOM   145  H HD1  A TYR   A 1 9   ? 12.504 -8.567  15.297  0.60 17.79 ?  9   TYR   A HD1  1 
ATOM   146  H HD1  B TYR   A 1 9   ? 12.279 -8.051  15.352  0.40 18.48 ?  9   TYR   A HD1  1 
ATOM   147  H HD2  A TYR   A 1 9   ? 12.728 -9.279  11.367  0.60 17.62 ?  9   TYR   A HD2  1 
ATOM   148  H HD2  B TYR   A 1 9   ? 12.860 -9.039  11.522  0.40 17.70 ?  9   TYR   A HD2  1 
ATOM   149  H HE1  A TYR   A 1 9   ? 13.909 -6.757  15.054  0.60 18.26 ?  9   TYR   A HE1  1 
ATOM   150  H HE1  B TYR   A 1 9   ? 13.541 -6.143  15.050  0.40 17.95 ?  9   TYR   A HE1  1 
ATOM   151  H HE2  A TYR   A 1 9   ? 14.136 -7.468  11.117  0.60 17.97 ?  9   TYR   A HE2  1 
ATOM   152  H HE2  B TYR   A 1 9   ? 14.123 -7.133  11.214  0.40 17.39 ?  9   TYR   A HE2  1 
ATOM   153  H HH   A TYR   A 1 9   ? 15.125 -5.499  13.659  0.60 20.09 ?  9   TYR   A HH   1 
ATOM   154  H HH   B TYR   A 1 9   ? 14.891 -4.975  13.653  0.40 17.78 ?  9   TYR   A HH   1 
ATOM   155  N N    A LEU   A 1 10  ? 8.742  -11.143 12.118  0.60 13.18 ?  10  LEU   A N    1 
ATOM   156  N N    B LEU   A 1 10  ? 8.933  -11.239 12.311  0.40 16.02 ?  10  LEU   A N    1 
ATOM   157  C CA   A LEU   A 1 10  ? 8.137  -12.357 11.601  0.60 13.22 ?  10  LEU   A CA   1 
ATOM   158  C CA   B LEU   A 1 10  ? 8.357  -12.494 11.856  0.40 16.22 ?  10  LEU   A CA   1 
ATOM   159  C C    A LEU   A 1 10  ? 9.257  -13.303 11.172  0.60 13.34 ?  10  LEU   A C    1 
ATOM   160  C C    B LEU   A 1 10  ? 9.467  -13.411 11.368  0.40 14.96 ?  10  LEU   A C    1 
ATOM   161  O O    A LEU   A 1 10  ? 10.194 -12.891 10.477  0.60 12.84 ?  10  LEU   A O    1 
ATOM   162  O O    B LEU   A 1 10  ? 10.463 -12.958 10.800  0.40 14.31 ?  10  LEU   A O    1 
ATOM   163  C CB   A LEU   A 1 10  ? 7.245  -11.992 10.415  0.60 13.87 ?  10  LEU   A CB   1 
ATOM   164  C CB   B LEU   A 1 10  ? 7.385  -12.243 10.700  0.40 18.00 ?  10  LEU   A CB   1 
ATOM   165  C CG   A LEU   A 1 10  ? 6.609  -13.178 9.703   0.60 15.20 ?  10  LEU   A CG   1 
ATOM   166  C CG   B LEU   A 1 10  ? 5.976  -11.770 11.048  0.40 19.70 ?  10  LEU   A CG   1 
ATOM   167  C CD1  A LEU   A 1 10  ? 5.564  -13.824 10.587  0.60 16.68 ?  10  LEU   A CD1  1 
ATOM   168  C CD1  B LEU   A 1 10  ? 5.075  -11.940 9.837   0.40 20.21 ?  10  LEU   A CD1  1 
ATOM   169  C CD2  A LEU   A 1 10  ? 6.016  -12.745 8.374   0.60 16.58 ?  10  LEU   A CD2  1 
ATOM   170  C CD2  B LEU   A 1 10  ? 5.428  -12.537 12.238  0.40 20.47 ?  10  LEU   A CD2  1 
ATOM   171  H H    A LEU   A 1 10  ? 8.776  -10.493 11.547  0.60 15.84 ?  10  LEU   A H    1 
ATOM   172  H H    B LEU   A 1 10  ? 8.984  -10.645 11.688  0.40 19.25 ?  10  LEU   A H    1 
ATOM   173  H HA   A LEU   A 1 10  ? 7.585  -12.776 12.290  0.60 15.89 ?  10  LEU   A HA   1 
ATOM   174  H HA   B LEU   A 1 10  ? 7.891  -12.933 12.586  0.40 19.49 ?  10  LEU   A HA   1 
ATOM   175  H HB2  A LEU   A 1 10  ? 6.518  -11.416 10.723  0.60 16.68 ?  10  LEU   A HB2  1 
ATOM   176  H HB2  B LEU   A 1 10  ? 7.774  -11.564 10.121  0.40 21.63 ?  10  LEU   A HB2  1 
ATOM   177  H HB3  A LEU   A 1 10  ? 7.776  -11.511 9.762   0.60 16.68 ?  10  LEU   A HB3  1 
ATOM   178  H HB3  B LEU   A 1 10  ? 7.288  -13.067 10.197  0.40 21.63 ?  10  LEU   A HB3  1 
ATOM   179  H HG   A LEU   A 1 10  ? 7.290  -13.840 9.519   0.60 18.26 ?  10  LEU   A HG   1 
ATOM   180  H HG   B LEU   A 1 10  ? 6.001  -10.825 11.278  0.40 23.67 ?  10  LEU   A HG   1 
ATOM   181  H HD11 A LEU   A 1 10  ? 5.135  -14.544 10.097  0.60 20.04 ?  10  LEU   A HD11 1 
ATOM   182  H HD11 B LEU   A 1 10  ? 4.183  -11.639 10.063  0.40 24.28 ?  10  LEU   A HD11 1 
ATOM   183  H HD12 A LEU   A 1 10  ? 5.992  -14.178 11.383  0.60 20.04 ?  10  LEU   A HD12 1 
ATOM   184  H HD12 B LEU   A 1 10  ? 5.430  -11.412 9.104   0.40 24.28 ?  10  LEU   A HD12 1 
ATOM   185  H HD13 A LEU   A 1 10  ? 4.902  -13.158 10.837  0.60 20.04 ?  10  LEU   A HD13 1 
ATOM   186  H HD13 B LEU   A 1 10  ? 5.057  -12.878 9.590   0.40 24.28 ?  10  LEU   A HD13 1 
ATOM   187  H HD21 A LEU   A 1 10  ? 5.618  -13.519 7.946   0.60 19.92 ?  10  LEU   A HD21 1 
ATOM   188  H HD21 B LEU   A 1 10  ? 4.469  -12.428 12.271  0.40 24.59 ?  10  LEU   A HD21 1 
ATOM   189  H HD22 A LEU   A 1 10  ? 5.342  -12.070 8.536   0.60 19.92 ?  10  LEU   A HD22 1 
ATOM   190  H HD22 B LEU   A 1 10  ? 5.655  -13.476 12.134  0.40 24.59 ?  10  LEU   A HD22 1 
ATOM   191  H HD23 A LEU   A 1 10  ? 6.725  -12.386 7.820   0.60 19.92 ?  10  LEU   A HD23 1 
ATOM   192  H HD23 B LEU   A 1 10  ? 5.832  -12.190 13.050  0.40 24.59 ?  10  LEU   A HD23 1 
ATOM   193  N N    A LYS   A 1 11  ? 9.171  -14.560 11.600  0.60 13.85 ?  11  LYS   A N    1 
ATOM   194  N N    B LYS   A 1 11  ? 9.294  -14.708 11.599  0.40 14.95 ?  11  LYS   A N    1 
ATOM   195  C CA   A LYS   A 1 11  ? 10.196 -15.557 11.316  0.60 14.27 ?  11  LYS   A CA   1 
ATOM   196  C CA   B LYS   A 1 11  ? 10.220 -15.707 11.091  0.40 15.37 ?  11  LYS   A CA   1 
ATOM   197  C C    A LYS   A 1 11  ? 9.892  -16.208 9.973   0.60 14.35 ?  11  LYS   A C    1 
ATOM   198  C C    B LYS   A 1 11  ? 9.757  -16.124 9.699   0.40 14.65 ?  11  LYS   A C    1 
ATOM   199  O O    A LYS   A 1 11  ? 8.861  -16.872 9.824   0.60 15.14 ?  11  LYS   A O    1 
ATOM   200  O O    B LYS   A 1 11  ? 8.590  -16.478 9.510   0.40 14.44 ?  11  LYS   A O    1 
ATOM   201  C CB   A LYS   A 1 11  ? 10.247 -16.606 12.431  0.60 13.39 ?  11  LYS   A CB   1 
ATOM   202  C CB   B LYS   A 1 11  ? 10.247 -16.914 12.034  0.40 16.14 ?  11  LYS   A CB   1 
ATOM   203  C CG   A LYS   A 1 11  ? 11.198 -17.775 12.176  0.60 12.82 ?  11  LYS   A CG   1 
ATOM   204  C CG   B LYS   A 1 11  ? 11.614 -17.544 12.244  0.40 17.35 ?  11  LYS   A CG   1 
ATOM   205  C CD   A LYS   A 1 11  ? 11.302 -18.645 13.428  0.60 13.34 ?  11  LYS   A CD   1 
ATOM   206  C CD   B LYS   A 1 11  ? 11.493 -18.871 12.981  0.40 18.81 ?  11  LYS   A CD   1 
ATOM   207  C CE   A LYS   A 1 11  ? 12.277 -19.814 13.253  0.60 13.28 ?  11  LYS   A CE   1 
ATOM   208  C CE   B LYS   A 1 11  ? 12.735 -19.194 13.793  0.40 19.86 ?  11  LYS   A CE   1 
ATOM   209  N NZ   A LYS   A 1 11  ? 13.652 -19.355 12.950  0.60 14.22 ?  11  LYS   A NZ   1 
ATOM   210  N NZ   B LYS   A 1 11  ? 13.952 -19.318 12.962  0.40 20.17 ?  11  LYS   A NZ   1 
ATOM   211  H H    A LYS   A 1 11  ? 8.499  -14.860 12.048  0.60 16.65 ?  11  LYS   A H    1 
ATOM   212  H H    B LYS   A 1 11  ? 8.638  -15.039 12.052  0.40 17.96 ?  11  LYS   A H    1 
ATOM   213  H HA   A LYS   A 1 11  ? 11.053 -15.106 11.254  0.60 17.15 ?  11  LYS   A HA   1 
ATOM   214  H HA   B LYS   A 1 11  ? 11.113 -15.331 11.030  0.40 18.47 ?  11  LYS   A HA   1 
ATOM   215  H HB2  A LYS   A 1 11  ? 10.535 -16.152 13.244  0.60 16.10 ?  11  LYS   A HB2  1 
ATOM   216  H HB2  B LYS   A 1 11  ? 9.925  -16.632 12.905  0.40 19.40 ?  11  LYS   A HB2  1 
ATOM   217  H HB3  A LYS   A 1 11  ? 9.356  -16.953 12.553  0.60 16.10 ?  11  LYS   A HB3  1 
ATOM   218  H HB3  B LYS   A 1 11  ? 9.669  -17.599 11.676  0.40 19.40 ?  11  LYS   A HB3  1 
ATOM   219  H HG2  A LYS   A 1 11  ? 10.853 -18.315 11.448  0.60 15.41 ?  11  LYS   A HG2  1 
ATOM   220  H HG2  B LYS   A 1 11  ? 12.033 -17.701 11.387  0.40 20.85 ?  11  LYS   A HG2  1 
ATOM   221  H HG3  A LYS   A 1 11  ? 12.080 -17.435 11.959  0.60 15.41 ?  11  LYS   A HG3  1 
ATOM   222  H HG3  B LYS   A 1 11  ? 12.165 -16.954 12.779  0.40 20.85 ?  11  LYS   A HG3  1 
ATOM   223  H HD2  A LYS   A 1 11  ? 11.608 -18.100 14.167  0.60 16.03 ?  11  LYS   A HD2  1 
ATOM   224  H HD2  B LYS   A 1 11  ? 10.741 -18.829 13.590  0.40 22.60 ?  11  LYS   A HD2  1 
ATOM   225  H HD3  A LYS   A 1 11  ? 10.422 -19.010 13.629  0.60 16.03 ?  11  LYS   A HD3  1 
ATOM   226  H HD3  B LYS   A 1 11  ? 11.365 -19.583 12.336  0.40 22.60 ?  11  LYS   A HD3  1 
ATOM   227  H HE2  A LYS   A 1 11  ? 12.304 -20.330 14.075  0.60 15.96 ?  11  LYS   A HE2  1 
ATOM   228  H HE2  B LYS   A 1 11  ? 12.885 -18.477 14.429  0.40 23.86 ?  11  LYS   A HE2  1 
ATOM   229  H HE3  A LYS   A 1 11  ? 11.974 -20.375 12.520  0.60 15.96 ?  11  LYS   A HE3  1 
ATOM   230  H HE3  B LYS   A 1 11  ? 12.604 -20.033 14.263  0.40 23.86 ?  11  LYS   A HE3  1 
ATOM   231  H HZ1  A LYS   A 1 11  ? 14.190 -20.055 12.853  0.60 17.09 ?  11  LYS   A HZ1  1 
ATOM   232  H HZ1  B LYS   A 1 11  ? 14.491 -19.941 13.300  0.40 24.24 ?  11  LYS   A HZ1  1 
ATOM   233  H HZ2  A LYS   A 1 11  ? 13.651 -18.884 12.193  0.60 17.09 ?  11  LYS   A HZ2  1 
ATOM   234  H HZ2  B LYS   A 1 11  ? 13.724 -19.548 12.134  0.40 24.24 ?  11  LYS   A HZ2  1 
ATOM   235  H HZ3  A LYS   A 1 11  ? 13.952 -18.843 13.610  0.60 17.09 ?  11  LYS   A HZ3  1 
ATOM   236  H HZ3  B LYS   A 1 11  ? 14.383 -18.541 12.937  0.40 24.24 ?  11  LYS   A HZ3  1 
ATOM   237  N N    A LEU   A 1 12  ? 10.785 -16.030 8.998   0.60 13.53 ?  12  LEU   A N    1 
ATOM   238  N N    B LEU   A 1 12  ? 10.653 -16.033 8.718   0.40 14.35 ?  12  LEU   A N    1 
ATOM   239  C CA   A LEU   A 1 12  ? 10.544 -16.611 7.681   0.60 14.02 ?  12  LEU   A CA   1 
ATOM   240  C CA   B LEU   A 1 12  ? 10.394 -16.575 7.388   0.40 14.58 ?  12  LEU   A CA   1 
ATOM   241  C C    A LEU   A 1 12  ? 11.099 -18.024 7.556   0.60 13.87 ?  12  LEU   A C    1 
ATOM   242  C C    B LEU   A 1 12  ? 11.019 -17.946 7.189   0.40 14.67 ?  12  LEU   A C    1 
ATOM   243  O O    A LEU   A 1 12  ? 10.429 -18.906 7.009   0.60 14.34 ?  12  LEU   A O    1 
ATOM   244  O O    B LEU   A 1 12  ? 10.416 -18.816 6.553   0.40 14.40 ?  12  LEU   A O    1 
ATOM   245  C CB   A LEU   A 1 12  ? 11.127 -15.722 6.577   0.60 14.61 ?  12  LEU   A CB   1 
ATOM   246  C CB   B LEU   A 1 12  ? 10.934 -15.634 6.308   0.40 14.57 ?  12  LEU   A CB   1 
ATOM   247  C CG   A LEU   A 1 12  ? 10.418 -14.397 6.295   0.60 15.87 ?  12  LEU   A CG   1 
ATOM   248  C CG   B LEU   A 1 12  ? 10.380 -14.211 6.318   0.40 15.37 ?  12  LEU   A CG   1 
ATOM   249  C CD1  A LEU   A 1 12  ? 11.156 -13.654 5.194   0.60 16.33 ?  12  LEU   A CD1  1 
ATOM   250  C CD1  B LEU   A 1 12  ? 11.065 -13.371 5.254   0.40 15.87 ?  12  LEU   A CD1  1 
ATOM   251  C CD2  A LEU   A 1 12  ? 8.962  -14.632 5.911   0.60 16.10 ?  12  LEU   A CD2  1 
ATOM   252  C CD2  B LEU   A 1 12  ? 8.869  -14.210 6.123   0.40 15.43 ?  12  LEU   A CD2  1 
ATOM   253  H H    A LEU   A 1 12  ? 11.529 -15.588 9.068   0.60 16.26 ?  12  LEU   A H    1 
ATOM   254  H H    B LEU   A 1 12  ? 11.414 -15.641 8.795   0.40 17.25 ?  12  LEU   A H    1 
ATOM   255  H HA   A LEU   A 1 12  ? 9.593  -16.669 7.540   0.60 16.86 ?  12  LEU   A HA   1 
ATOM   256  H HA   B LEU   A 1 12  ? 9.432  -16.658 7.265   0.40 17.53 ?  12  LEU   A HA   1 
ATOM   257  H HB2  A LEU   A 1 12  ? 12.043 -15.507 6.810   0.60 17.56 ?  12  LEU   A HB2  1 
ATOM   258  H HB2  B LEU   A 1 12  ? 11.895 -15.578 6.415   0.40 17.51 ?  12  LEU   A HB2  1 
ATOM   259  H HB3  A LEU   A 1 12  ? 11.119 -16.227 5.748   0.60 17.56 ?  12  LEU   A HB3  1 
ATOM   260  H HB3  B LEU   A 1 12  ? 10.728 -16.025 5.444   0.40 17.51 ?  12  LEU   A HB3  1 
ATOM   261  H HG   A LEU   A 1 12  ? 10.437 -13.848 7.093   0.60 19.08 ?  12  LEU   A HG   1 
ATOM   262  H HG   B LEU   A 1 12  ? 10.571 -13.814 7.178   0.40 18.47 ?  12  LEU   A HG   1 
ATOM   263  H HD11 A LEU   A 1 12  ? 10.705 -12.813 5.020   0.60 19.63 ?  12  LEU   A HD11 1 
ATOM   264  H HD11 B LEU   A 1 12  ? 10.700 -12.473 5.280   0.40 19.08 ?  12  LEU   A HD11 1 
ATOM   265  H HD12 A LEU   A 1 12  ? 12.068 -13.484 5.483   0.60 19.63 ?  12  LEU   A HD12 1 
ATOM   266  H HD12 B LEU   A 1 12  ? 12.019 -13.345 5.437   0.40 19.08 ?  12  LEU   A HD12 1 
ATOM   267  H HD13 A LEU   A 1 12  ? 11.161 -14.199 4.391   0.60 19.63 ?  12  LEU   A HD13 1 
ATOM   268  H HD13 B LEU   A 1 12  ? 10.907 -13.769 4.384   0.40 19.08 ?  12  LEU   A HD13 1 
ATOM   269  H HD21 A LEU   A 1 12  ? 8.595  -13.814 5.542   0.60 19.35 ?  12  LEU   A HD21 1 
ATOM   270  H HD21 B LEU   A 1 12  ? 8.568  -13.292 6.028   0.40 18.54 ?  12  LEU   A HD21 1 
ATOM   271  H HD22 A LEU   A 1 12  ? 8.922  -15.340 5.249   0.60 19.35 ?  12  LEU   A HD22 1 
ATOM   272  H HD22 B LEU   A 1 12  ? 8.652  -14.713 5.322   0.40 18.54 ?  12  LEU   A HD22 1 
ATOM   273  H HD23 A LEU   A 1 12  ? 8.465  -14.893 6.701   0.60 19.35 ?  12  LEU   A HD23 1 
ATOM   274  H HD23 B LEU   A 1 12  ? 8.449  -14.618 6.895   0.40 18.54 ?  12  LEU   A HD23 1 
ATOM   275  N N    A THR   A 1 13  ? 12.314 -18.253 8.048   0.60 13.11 ?  13  THR   A N    1 
ATOM   276  N N    B THR   A 1 13  ? 12.230 -18.141 7.705   0.40 14.88 ?  13  THR   A N    1 
ATOM   277  C CA   A THR   A 1 13  ? 13.003 -19.529 7.908   0.60 13.73 ?  13  THR   A CA   1 
ATOM   278  C CA   B THR   A 1 13  ? 12.902 -19.431 7.709   0.40 15.49 ?  13  THR   A CA   1 
ATOM   279  C C    A THR   A 1 13  ? 13.777 -19.787 9.191   0.60 13.64 ?  13  THR   A C    1 
ATOM   280  C C    B THR   A 1 13  ? 13.634 -19.566 9.041   0.40 15.72 ?  13  THR   A C    1 
ATOM   281  O O    A THR   A 1 13  ? 13.676 -19.037 10.169  0.60 13.16 ?  13  THR   A O    1 
ATOM   282  O O    B THR   A 1 13  ? 13.509 -18.721 9.931   0.40 15.55 ?  13  THR   A O    1 
ATOM   283  C CB   A THR   A 1 13  ? 13.984 -19.513 6.731   0.60 14.59 ?  13  THR   A CB   1 
ATOM   284  C CB   B THR   A 1 13  ? 13.881 -19.560 6.534   0.40 15.96 ?  13  THR   A CB   1 
ATOM   285  O OG1  A THR   A 1 13  ? 15.030 -18.587 7.027   0.60 14.59 ?  13  THR   A OG1  1 
ATOM   286  O OG1  B THR   A 1 13  ? 14.936 -18.606 6.684   0.40 16.08 ?  13  THR   A OG1  1 
ATOM   287  C CG2  A THR   A 1 13  ? 13.308 -19.125 5.420   0.60 15.37 ?  13  THR   A CG2  1 
ATOM   288  C CG2  B THR   A 1 13  ? 13.189 -19.336 5.203   0.40 16.53 ?  13  THR   A CG2  1 
ATOM   289  H H    A THR   A 1 13  ? 12.780 -17.665 8.473   0.60 15.76 ?  13  THR   A H    1 
ATOM   290  H H    B THR   A 1 13  ? 12.695 -17.516 8.067   0.40 17.88 ?  13  THR   A H    1 
ATOM   291  H HA   A THR   A 1 13  ? 12.370 -20.245 7.771   0.60 16.50 ?  13  THR   A HA   1 
ATOM   292  H HA   B THR   A 1 13  ? 12.240 -20.140 7.639   0.40 18.61 ?  13  THR   A HA   1 
ATOM   293  H HB   A THR   A 1 13  ? 14.375 -20.392 6.610   0.60 17.54 ?  13  THR   A HB   1 
ATOM   294  H HB   B THR   A 1 13  ? 14.258 -20.452 6.535   0.40 19.18 ?  13  THR   A HB   1 
ATOM   295  H HG1  A THR   A 1 13  ? 15.770 -18.984 7.103   0.60 17.54 ?  13  THR   A HG1  1 
ATOM   296  H HG1  B THR   A 1 13  ? 15.479 -18.672 6.046   0.40 19.32 ?  13  THR   A HG1  1 
ATOM   297  H HG21 A THR   A 1 13  ? 13.932 -19.215 4.678   0.60 18.47 ?  13  THR   A HG21 1 
ATOM   298  H HG21 B THR   A 1 13  ? 13.809 -19.521 4.479   0.40 19.87 ?  13  THR   A HG21 1 
ATOM   299  H HG22 A THR   A 1 13  ? 12.549 -19.709 5.258   0.60 18.47 ?  13  THR   A HG22 1 
ATOM   300  H HG22 B THR   A 1 13  ? 12.426 -19.926 5.125   0.40 19.87 ?  13  THR   A HG22 1 
ATOM   301  H HG23 A THR   A 1 13  ? 12.999 -18.209 5.459   0.60 18.47 ?  13  THR   A HG23 1 
ATOM   302  H HG23 B THR   A 1 13  ? 12.890 -18.417 5.135   0.40 19.87 ?  13  THR   A HG23 1 
ATOM   303  N N    A ASP   A 1 14  ? 14.599 -20.837 9.161   0.60 14.27 ?  14  ASP   A N    1 
ATOM   304  N N    B ASP   A 1 14  ? 14.436 -20.625 9.157   0.40 16.25 ?  14  ASP   A N    1 
ATOM   305  C CA   A ASP   A 1 14  ? 15.466 -21.122 10.293  0.60 14.80 ?  14  ASP   A CA   1 
ATOM   306  C CA   B ASP   A 1 14  ? 15.195 -20.870 10.378  0.40 16.56 ?  14  ASP   A CA   1 
ATOM   307  C C    A ASP   A 1 14  ? 16.303 -19.912 10.691  0.60 14.51 ?  14  ASP   A C    1 
ATOM   308  C C    B ASP   A 1 14  ? 16.053 -19.674 10.774  0.40 15.26 ?  14  ASP   A C    1 
ATOM   309  O O    A ASP   A 1 14  ? 16.578 -19.706 11.878  0.60 15.39 ?  14  ASP   A O    1 
ATOM   310  O O    B ASP   A 1 14  ? 16.252 -19.429 11.970  0.40 15.40 ?  14  ASP   A O    1 
ATOM   311  C CB   A ASP   A 1 14  ? 16.389 -22.292 9.964   0.60 17.05 ?  14  ASP   A CB   1 
ATOM   312  C CB   B ASP   A 1 14  ? 16.077 -22.103 10.188  0.40 18.71 ?  14  ASP   A CB   1 
ATOM   313  C CG   A ASP   A 1 14  ? 17.329 -22.604 11.094  0.60 20.28 ?  14  ASP   A CG   1 
ATOM   314  C CG   B ASP   A 1 14  ? 16.896 -22.425 11.417  0.40 21.05 ?  14  ASP   A CG   1 
ATOM   315  O OD1  A ASP   A 1 14  ? 16.846 -23.037 12.164  0.60 21.05 ?  14  ASP   A OD1  1 
ATOM   316  O OD1  B ASP   A 1 14  ? 16.306 -22.700 12.485  0.40 21.86 ?  14  ASP   A OD1  1 
ATOM   317  O OD2  A ASP   A 1 14  ? 18.545 -22.394 10.913  0.60 22.85 -1 14  ASP   A OD2  1 
ATOM   318  O OD2  B ASP   A 1 14  ? 18.135 -22.412 11.312  0.40 22.24 -1 14  ASP   A OD2  1 
ATOM   319  H H    A ASP   A 1 14  ? 14.690 -21.384 8.493   0.60 17.16 ?  14  ASP   A H    1 
ATOM   320  H H    B ASP   A 1 14  ? 14.567 -21.202 8.541   0.40 19.53 ?  14  ASP   A H    1 
ATOM   321  H HA   A ASP   A 1 14  ? 14.923 -21.378 11.049  0.60 17.79 ?  14  ASP   A HA   1 
ATOM   322  H HA   B ASP   A 1 14  ? 14.584 -21.059 11.108  0.40 19.90 ?  14  ASP   A HA   1 
ATOM   323  H HB2  A ASP   A 1 14  ? 15.850 -23.089 9.783   0.60 20.49 ?  14  ASP   A HB2  1 
ATOM   324  H HB2  B ASP   A 1 14  ? 15.513 -22.867 9.981   0.40 22.48 ?  14  ASP   A HB2  1 
ATOM   325  H HB3  A ASP   A 1 14  ? 16.928 -22.082 9.188   0.60 20.49 ?  14  ASP   A HB3  1 
ATOM   326  H HB3  B ASP   A 1 14  ? 16.694 -21.943 9.456   0.40 22.48 ?  14  ASP   A HB3  1 
ATOM   327  N N    A ASN   A 1 15  ? 16.735 -19.109 9.711   0.60 14.08 ?  15  ASN   A N    1 
ATOM   328  N N    B ASN   A 1 15  ? 16.557 -18.909 9.798   0.40 14.39 ?  15  ASN   A N    1 
ATOM   329  C CA   A ASN   A 1 15  ? 17.727 -18.072 9.962   0.60 14.51 ?  15  ASN   A CA   1 
ATOM   330  C CA   B ASN   A 1 15  ? 17.537 -17.864 10.073  0.40 14.33 ?  15  ASN   A CA   1 
ATOM   331  C C    A ASN   A 1 15  ? 17.361 -16.684 9.442   0.60 14.67 ?  15  ASN   A C    1 
ATOM   332  C C    B ASN   A 1 15  ? 17.149 -16.466 9.599   0.40 14.12 ?  15  ASN   A C    1 
ATOM   333  O O    A ASN   A 1 15  ? 18.157 -15.757 9.622   0.60 15.33 ?  15  ASN   A O    1 
ATOM   334  O O    B ASN   A 1 15  ? 17.844 -15.509 9.958   0.40 14.87 ?  15  ASN   A O    1 
ATOM   335  C CB   A ASN   A 1 15  ? 19.090 -18.485 9.375   0.60 14.41 ?  15  ASN   A CB   1 
ATOM   336  C CB   B ASN   A 1 15  ? 18.911 -18.236 9.485   0.40 14.36 ?  15  ASN   A CB   1 
ATOM   337  C CG   A ASN   A 1 15  ? 19.067 -18.562 7.867   0.60 14.89 ?  15  ASN   A CG   1 
ATOM   338  C CG   B ASN   A 1 15  ? 18.900 -18.325 7.973   0.40 14.84 ?  15  ASN   A CG   1 
ATOM   339  O OD1  A ASN   A 1 15  ? 18.351 -19.381 7.288   0.60 16.12 ?  15  ASN   A OD1  1 
ATOM   340  O OD1  B ASN   A 1 15  ? 18.210 -19.169 7.398   0.40 15.61 ?  15  ASN   A OD1  1 
ATOM   341  N ND2  A ASN   A 1 15  ? 19.854 -17.712 7.218   0.60 14.76 ?  15  ASN   A ND2  1 
ATOM   342  N ND2  B ASN   A 1 15  ? 19.673 -17.455 7.318   0.40 14.68 ?  15  ASN   A ND2  1 
ATOM   343  H H    A ASN   A 1 15  ? 16.473 -19.156 8.894   0.60 16.92 ?  15  ASN   A H    1 
ATOM   344  H H    B ASN   A 1 15  ? 16.341 -18.981 8.971   0.40 17.30 ?  15  ASN   A H    1 
ATOM   345  H HA   A ASN   A 1 15  ? 17.856 -17.999 10.918  0.60 17.45 ?  15  ASN   A HA   1 
ATOM   346  H HA   B ASN   A 1 15  ? 17.654 -17.809 11.031  0.40 17.22 ?  15  ASN   A HA   1 
ATOM   347  H HB2  A ASN   A 1 15  ? 19.765 -17.830 9.635   0.60 17.32 ?  15  ASN   A HB2  1 
ATOM   348  H HB2  B ASN   A 1 15  ? 19.559 -17.559 9.741   0.40 17.26 ?  15  ASN   A HB2  1 
ATOM   349  H HB3  A ASN   A 1 15  ? 19.344 -19.361 9.717   0.60 17.32 ?  15  ASN   A HB3  1 
ATOM   350  H HB3  B ASN   A 1 15  ? 19.182 -19.100 9.831   0.40 17.26 ?  15  ASN   A HB3  1 
ATOM   351  H HD21 A ASN   A 1 15  ? 19.879 -17.718 6.357   0.60 17.74 ?  15  ASN   A HD21 1 
ATOM   352  H HD21 B ASN   A 1 15  ? 19.710 -17.464 6.456   0.40 17.65 ?  15  ASN   A HD21 1 
ATOM   353  H HD22 A ASN   A 1 15  ? 20.349 -17.154 7.653   0.60 17.74 ?  15  ASN   A HD22 1 
ATOM   354  H HD22 B ASN   A 1 15  ? 20.145 -16.878 7.754   0.40 17.65 ?  15  ASN   A HD22 1 
ATOM   355  N N    A VAL   A 1 16  ? 16.207 -16.507 8.801   0.60 14.36 ?  16  VAL   A N    1 
ATOM   356  N N    B VAL   A 1 16  ? 16.068 -16.309 8.835   0.40 13.76 ?  16  VAL   A N    1 
ATOM   357  C CA   A VAL   A 1 16  ? 15.811 -15.220 8.235   0.60 14.26 ?  16  VAL   A CA   1 
ATOM   358  C CA   B VAL   A 1 16  ? 15.685 -15.027 8.246   0.40 13.97 ?  16  VAL   A CA   1 
ATOM   359  C C    A VAL   A 1 16  ? 14.530 -14.729 8.902   0.60 13.66 ?  16  VAL   A C    1 
ATOM   360  C C    B VAL   A 1 16  ? 14.430 -14.510 8.943   0.40 13.83 ?  16  VAL   A C    1 
ATOM   361  O O    A VAL   A 1 16  ? 13.546 -15.474 9.022   0.60 13.24 ?  16  VAL   A O    1 
ATOM   362  O O    B VAL   A 1 16  ? 13.404 -15.203 8.997   0.40 13.64 ?  16  VAL   A O    1 
ATOM   363  C CB   A VAL   A 1 16  ? 15.643 -15.281 6.707   0.60 14.62 ?  16  VAL   A CB   1 
ATOM   364  C CB   B VAL   A 1 16  ? 15.483 -15.143 6.723   0.40 14.42 ?  16  VAL   A CB   1 
ATOM   365  C CG1  A VAL   A 1 16  ? 15.190 -13.925 6.171   0.60 15.47 ?  16  VAL   A CG1  1 
ATOM   366  C CG1  B VAL   A 1 16  ? 15.135 -13.783 6.116   0.40 14.96 ?  16  VAL   A CG1  1 
ATOM   367  C CG2  A VAL   A 1 16  ? 16.937 -15.723 6.037   0.60 15.30 ?  16  VAL   A CG2  1 
ATOM   368  C CG2  B VAL   A 1 16  ? 16.730 -15.729 6.057   0.40 14.94 ?  16  VAL   A CG2  1 
ATOM   369  H H    A VAL   A 1 16  ? 15.640 -17.144 8.673   0.60 17.26 ?  16  VAL   A H    1 
ATOM   370  H H    B VAL   A 1 16  ? 15.522 -16.943 8.644   0.40 16.54 ?  16  VAL   A H    1 
ATOM   371  H HA   A VAL   A 1 16  ? 16.520 -14.583 8.425   0.60 17.14 ?  16  VAL   A HA   1 
ATOM   372  H HA   B VAL   A 1 16  ? 16.390 -14.383 8.397   0.40 16.79 ?  16  VAL   A HA   1 
ATOM   373  H HB   A VAL   A 1 16  ? 14.961 -15.935 6.495   0.60 17.57 ?  16  VAL   A HB   1 
ATOM   374  H HB   B VAL   A 1 16  ? 14.746 -15.744 6.545   0.40 17.33 ?  16  VAL   A HB   1 
ATOM   375  H HG11 A VAL   A 1 16  ? 15.288 -13.922 5.207   0.60 18.59 ?  16  VAL   A HG11 1 
ATOM   376  H HG11 B VAL   A 1 16  ? 15.170 -13.852 5.147   0.40 17.98 ?  16  VAL   A HG11 1 
ATOM   377  H HG12 A VAL   A 1 16  ? 14.260 -13.786 6.409   0.60 18.59 ?  16  VAL   A HG12 1 
ATOM   378  H HG12 B VAL   A 1 16  ? 14.240 -13.533 6.394   0.40 17.98 ?  16  VAL   A HG12 1 
ATOM   379  H HG13 A VAL   A 1 16  ? 15.742 -13.230 6.562   0.60 18.59 ?  16  VAL   A HG13 1 
ATOM   380  H HG13 B VAL   A 1 16  ? 15.776 -13.125 6.423   0.40 17.98 ?  16  VAL   A HG13 1 
ATOM   381  H HG21 A VAL   A 1 16  ? 16.819 -15.689 5.076   0.60 18.38 ?  16  VAL   A HG21 1 
ATOM   382  H HG21 B VAL   A 1 16  ? 16.610 -15.725 5.094   0.40 17.96 ?  16  VAL   A HG21 1 
ATOM   383  H HG22 A VAL   A 1 16  ? 17.652 -15.127 6.305   0.60 18.38 ?  16  VAL   A HG22 1 
ATOM   384  H HG22 B VAL   A 1 16  ? 17.501 -15.191 6.295   0.40 17.96 ?  16  VAL   A HG22 1 
ATOM   385  H HG23 A VAL   A 1 16  ? 17.142 -16.631 6.314   0.60 18.38 ?  16  VAL   A HG23 1 
ATOM   386  H HG23 B VAL   A 1 16  ? 16.856 -16.641 6.368   0.40 17.96 ?  16  VAL   A HG23 1 
ATOM   387  N N    A TYR   A 1 17  ? 14.550 -13.455 9.294   0.60 13.31 ?  17  TYR   A N    1 
ATOM   388  N N    B TYR   A 1 17  ? 14.520 -13.280 9.462   0.40 13.60 ?  17  TYR   A N    1 
ATOM   389  C CA   A TYR   A 1 17  ? 13.459 -12.768 9.964   0.60 13.07 ?  17  TYR   A CA   1 
ATOM   390  C CA   B TYR   A 1 17  ? 13.465 -12.611 10.211  0.40 13.33 ?  17  TYR   A CA   1 
ATOM   391  C C    A TYR   A 1 17  ? 13.190 -11.457 9.229   0.60 12.85 ?  17  TYR   A C    1 
ATOM   392  C C    B TYR   A 1 17  ? 13.193 -11.258 9.565   0.40 12.66 ?  17  TYR   A C    1 
ATOM   393  O O    A TYR   A 1 17  ? 14.087 -10.910 8.581   0.60 12.79 ?  17  TYR   A O    1 
ATOM   394  O O    B TYR   A 1 17  ? 14.101 -10.655 8.992   0.40 12.50 ?  17  TYR   A O    1 
ATOM   395  C CB   A TYR   A 1 17  ? 13.849 -12.494 11.427  0.60 13.52 ?  17  TYR   A CB   1 
ATOM   396  C CB   B TYR   A 1 17  ? 13.913 -12.392 11.662  0.40 14.80 ?  17  TYR   A CB   1 
ATOM   397  C CG   A TYR   A 1 17  ? 14.024 -13.753 12.262  0.60 14.04 ?  17  TYR   A CG   1 
ATOM   398  C CG   B TYR   A 1 17  ? 14.284 -13.657 12.410  0.40 16.20 ?  17  TYR   A CG   1 
ATOM   399  C CD1  A TYR   A 1 17  ? 15.194 -14.511 12.195  0.60 14.55 ?  17  TYR   A CD1  1 
ATOM   400  C CD1  B TYR   A 1 17  ? 15.530 -14.257 12.240  0.40 17.11 ?  17  TYR   A CD1  1 
ATOM   401  C CD2  A TYR   A 1 17  ? 13.015 -14.191 13.114  0.60 13.96 ?  17  TYR   A CD2  1 
ATOM   402  C CD2  B TYR   A 1 17  ? 13.396 -14.242 13.303  0.40 17.04 ?  17  TYR   A CD2  1 
ATOM   403  C CE1  A TYR   A 1 17  ? 15.352 -15.671 12.947  0.60 14.24 ?  17  TYR   A CE1  1 
ATOM   404  C CE1  B TYR   A 1 17  ? 15.870 -15.407 12.928  0.40 18.07 ?  17  TYR   A CE1  1 
ATOM   405  C CE2  A TYR   A 1 17  ? 13.166 -15.358 13.876  0.60 14.01 ?  17  TYR   A CE2  1 
ATOM   406  C CE2  B TYR   A 1 17  ? 13.733 -15.389 13.999  0.40 17.73 ?  17  TYR   A CE2  1 
ATOM   407  C CZ   A TYR   A 1 17  ? 14.343 -16.090 13.790  0.60 14.13 ?  17  TYR   A CZ   1 
ATOM   408  C CZ   B TYR   A 1 17  ? 14.966 -15.968 13.802  0.40 18.47 ?  17  TYR   A CZ   1 
ATOM   409  O OH   A TYR   A 1 17  ? 14.518 -17.247 14.529  0.60 14.72 ?  17  TYR   A OH   1 
ATOM   410  O OH   B TYR   A 1 17  ? 15.303 -17.110 14.490  0.40 19.49 ?  17  TYR   A OH   1 
ATOM   411  H H    A TYR   A 1 17  ? 15.237 -12.952 9.169   0.60 16.00 ?  17  TYR   A H    1 
ATOM   412  H H    B TYR   A 1 17  ? 15.225 -12.787 9.381   0.40 16.35 ?  17  TYR   A H    1 
ATOM   413  H HA   A TYR   A 1 17  ? 12.666 -13.336 9.944   0.60 15.72 ?  17  TYR   A HA   1 
ATOM   414  H HA   B TYR   A 1 17  ? 12.656 -13.134 10.194  0.40 16.02 ?  17  TYR   A HA   1 
ATOM   415  H HB2  A TYR   A 1 17  ? 14.683 -12.009 11.444  0.60 16.25 ?  17  TYR   A HB2  1 
ATOM   416  H HB2  B TYR   A 1 17  ? 14.689 -11.814 11.659  0.40 17.79 ?  17  TYR   A HB2  1 
ATOM   417  H HB3  A TYR   A 1 17  ? 13.147 -11.966 11.834  0.60 16.25 ?  17  TYR   A HB3  1 
ATOM   418  H HB3  B TYR   A 1 17  ? 13.190 -11.969 12.147  0.40 17.79 ?  17  TYR   A HB3  1 
ATOM   419  H HD1  A TYR   A 1 17  ? 15.880 -14.239 11.631  0.60 17.49 ?  17  TYR   A HD1  1 
ATOM   420  H HD1  B TYR   A 1 17  ? 16.141 -13.885 11.649  0.40 20.56 ?  17  TYR   A HD1  1 
ATOM   421  H HD2  A TYR   A 1 17  ? 12.222 -13.709 13.180  0.60 16.78 ?  17  TYR   A HD2  1 
ATOM   422  H HD2  B TYR   A 1 17  ? 12.560 -13.859 13.434  0.40 20.48 ?  17  TYR   A HD2  1 
ATOM   423  H HE1  A TYR   A 1 17  ? 16.142 -16.161 12.891  0.60 17.11 ?  17  TYR   A HE1  1 
ATOM   424  H HE1  B TYR   A 1 17  ? 16.705 -15.801 12.804  0.40 21.72 ?  17  TYR   A HE1  1 
ATOM   425  H HE2  A TYR   A 1 17  ? 12.481 -15.636 14.446  0.60 16.84 ?  17  TYR   A HE2  1 
ATOM   426  H HE2  B TYR   A 1 17  ? 13.126 -15.777 14.590  0.40 21.31 ?  17  TYR   A HE2  1 
ATOM   427  H HH   A TYR   A 1 17  ? 13.810 -17.435 14.939  0.60 17.69 ?  17  TYR   A HH   1 
ATOM   428  H HH   B TYR   A 1 17  ? 14.624 -17.448 14.847  0.40 23.41 ?  17  TYR   A HH   1 
ATOM   429  N N    A ILE   A 1 18  ? 11.963 -10.937 9.334   0.60 13.13 ?  18  ILE   A N    1 
ATOM   430  N N    B ILE   A 1 18  ? 11.956 -10.755 9.670   0.40 12.03 ?  18  ILE   A N    1 
ATOM   431  C CA   A ILE   A 1 18  ? 11.574 -9.754  8.564   0.60 12.79 ?  18  ILE   A CA   1 
ATOM   432  C CA   B ILE   A 1 18  ? 11.562 -9.557  8.929   0.40 11.89 ?  18  ILE   A CA   1 
ATOM   433  C C    A ILE   A 1 18  ? 10.591 -8.908  9.365   0.60 13.52 ?  18  ILE   A C    1 
ATOM   434  C C    B ILE   A 1 18  ? 10.622 -8.676  9.746   0.40 11.81 ?  18  ILE   A C    1 
ATOM   435  O O    A ILE   A 1 18  ? 9.758  -9.432  10.108  0.60 13.55 ?  18  ILE   A O    1 
ATOM   436  O O    B ILE   A 1 18  ? 9.809  -9.162  10.541  0.40 11.87 ?  18  ILE   A O    1 
ATOM   437  C CB   A ILE   A 1 18  ? 11.022 -10.160 7.177   0.60 12.60 ?  18  ILE   A CB   1 
ATOM   438  C CB   B ILE   A 1 18  ? 10.948 -9.926  7.560   0.40 12.17 ?  18  ILE   A CB   1 
ATOM   439  C CG1  A ILE   A 1 18  ? 10.966 -8.953  6.246   0.60 13.08 ?  18  ILE   A CG1  1 
ATOM   440  C CG1  B ILE   A 1 18  ? 10.873 -8.701  6.644   0.40 13.10 ?  18  ILE   A CG1  1 
ATOM   441  C CG2  A ILE   A 1 18  ? 9.666  -10.860 7.307   0.60 12.58 ?  18  ILE   A CG2  1 
ATOM   442  C CG2  B ILE   A 1 18  ? 9.579  -10.576 7.737   0.40 12.67 ?  18  ILE   A CG2  1 
ATOM   443  C CD1  A ILE   A 1 18  ? 10.769 -9.332  4.808   0.60 14.25 ?  18  ILE   A CD1  1 
ATOM   444  C CD1  B ILE   A 1 18  ? 10.563 -9.054  5.207   0.40 14.28 ?  18  ILE   A CD1  1 
ATOM   445  H H    A ILE   A 1 18  ? 11.354 -11.261 9.849   0.60 15.79 ?  18  ILE   A H    1 
ATOM   446  H H    B ILE   A 1 18  ? 11.331 -11.088 10.156  0.40 14.47 ?  18  ILE   A H    1 
ATOM   447  H HA   A ILE   A 1 18  ? 12.376 -9.228  8.419   0.60 15.38 ?  18  ILE   A HA   1 
ATOM   448  H HA   B ILE   A 1 18  ? 12.365 -9.033  8.753   0.40 14.30 ?  18  ILE   A HA   1 
ATOM   449  H HB   A ILE   A 1 18  ? 11.642 -10.802 6.790   0.60 15.15 ?  18  ILE   A HB   1 
ATOM   450  H HB   B ILE   A 1 18  ? 11.535 -10.569 7.140   0.40 14.63 ?  18  ILE   A HB   1 
ATOM   451  H HG12 A ILE   A 1 18  ? 10.233 -8.384  6.518   0.60 15.73 ?  18  ILE   A HG12 1 
ATOM   452  H HG12 B ILE   A 1 18  ? 10.179 -8.105  6.959   0.40 15.75 ?  18  ILE   A HG12 1 
ATOM   453  H HG13 A ILE   A 1 18  ? 11.806 -8.468  6.316   0.60 15.73 ?  18  ILE   A HG13 1 
ATOM   454  H HG13 B ILE   A 1 18  ? 11.731 -8.242  6.653   0.40 15.75 ?  18  ILE   A HG13 1 
ATOM   455  H HG21 A ILE   A 1 18  ? 9.421  -11.237 6.446   0.60 15.13 ?  18  ILE   A HG21 1 
ATOM   456  H HG21 B ILE   A 1 18  ? 9.305  -10.964 6.890   0.40 15.23 ?  18  ILE   A HG21 1 
ATOM   457  H HG22 A ILE   A 1 18  ? 9.732  -11.567 7.968   0.60 15.13 ?  18  ILE   A HG22 1 
ATOM   458  H HG22 B ILE   A 1 18  ? 9.645  -11.266 8.412   0.40 15.23 ?  18  ILE   A HG22 1 
ATOM   459  H HG23 A ILE   A 1 18  ? 8.999  -10.211 7.583   0.60 15.13 ?  18  ILE   A HG23 1 
ATOM   460  H HG23 B ILE   A 1 18  ? 8.939  -9.900  8.012   0.40 15.23 ?  18  ILE   A HG23 1 
ATOM   461  H HD11 A ILE   A 1 18  ? 10.788 -8.524  4.268   0.60 17.13 ?  18  ILE   A HD11 1 
ATOM   462  H HD11 B ILE   A 1 18  ? 10.581 -8.247  4.667   0.40 17.16 ?  18  ILE   A HD11 1 
ATOM   463  H HD12 A ILE   A 1 18  ? 11.476 -9.931  4.536   0.60 17.13 ?  18  ILE   A HD12 1 
ATOM   464  H HD12 B ILE   A 1 18  ? 11.228 -9.682  4.882   0.40 17.16 ?  18  ILE   A HD12 1 
ATOM   465  H HD13 A ILE   A 1 18  ? 9.906  -9.767  4.715   0.60 17.13 ?  18  ILE   A HD13 1 
ATOM   466  H HD13 B ILE   A 1 18  ? 9.681  -9.458  5.164   0.40 17.16 ?  18  ILE   A HD13 1 
ATOM   467  N N    A LYS   A 1 19  ? 10.678 -7.587  9.189   0.60 14.12 ?  19  LYS   A N    1 
ATOM   468  N N    B LYS   A 1 19  ? 10.725 -7.362  9.518   0.40 11.77 ?  19  LYS   A N    1 
ATOM   469  C CA   A LYS   A 1 19  ? 9.867  -6.640  9.947   0.60 14.86 ?  19  LYS   A CA   1 
ATOM   470  C CA   B LYS   A 1 19  ? 9.915  -6.382  10.229  0.40 12.65 ?  19  LYS   A CA   1 
ATOM   471  C C    A LYS   A 1 19  ? 9.688  -5.361  9.135   0.60 14.81 ?  19  LYS   A C    1 
ATOM   472  C C    B LYS   A 1 19  ? 9.716  -5.148  9.357   0.40 12.97 ?  19  LYS   A C    1 
ATOM   473  O O    A LYS   A 1 19  ? 10.565 -4.982  8.355   0.60 14.77 ?  19  LYS   A O    1 
ATOM   474  O O    B LYS   A 1 19  ? 10.634 -4.733  8.648   0.40 13.33 ?  19  LYS   A O    1 
ATOM   475  C CB   A LYS   A 1 19  ? 10.555 -6.329  11.288  0.60 15.95 ?  19  LYS   A CB   1 
ATOM   476  C CB   B LYS   A 1 19  ? 10.602 -5.972  11.535  0.40 13.62 ?  19  LYS   A CB   1 
ATOM   477  C CG   A LYS   A 1 19  ? 9.863  -5.324  12.210  0.60 17.00 ?  19  LYS   A CG   1 
ATOM   478  C CG   B LYS   A 1 19  ? 9.766  -5.100  12.441  0.40 15.31 ?  19  LYS   A CG   1 
ATOM   479  C CD   A LYS   A 1 19  ? 10.730 -5.100  13.454  0.60 17.67 ?  19  LYS   A CD   1 
ATOM   480  C CD   B LYS   A 1 19  ? 10.551 -4.743  13.684  0.40 16.71 ?  19  LYS   A CD   1 
ATOM   481  C CE   A LYS   A 1 19  ? 10.139 -4.110  14.448  0.60 18.13 ?  19  LYS   A CE   1 
ATOM   482  C CE   B LYS   A 1 19  ? 9.758  -3.844  14.608  0.40 17.54 ?  19  LYS   A CE   1 
ATOM   483  N NZ   A LYS   A 1 19  ? 11.033 -3.940  15.639  0.60 18.09 ?  19  LYS   A NZ   1 
ATOM   484  N NZ   B LYS   A 1 19  ? 10.576 -3.424  15.774  0.40 17.92 ?  19  LYS   A NZ   1 
ATOM   485  H H    A LYS   A 1 19  ? 11.217 -7.220  8.630   0.60 16.97 ?  19  LYS   A H    1 
ATOM   486  H H    B LYS   A 1 19  ? 11.275 -7.002  8.944   0.40 14.16 ?  19  LYS   A H    1 
ATOM   487  H HA   A LYS   A 1 19  ? 9.000  -7.033  10.128  0.60 17.86 ?  19  LYS   A HA   1 
ATOM   488  H HA   B LYS   A 1 19  ? 9.052  -6.761  10.431  0.40 15.20 ?  19  LYS   A HA   1 
ATOM   489  H HB2  A LYS   A 1 19  ? 10.637 -7.160  11.787  0.60 19.17 ?  19  LYS   A HB2  1 
ATOM   490  H HB2  B LYS   A 1 19  ? 10.824 -6.776  12.031  0.40 16.37 ?  19  LYS   A HB2  1 
ATOM   491  H HB3  A LYS   A 1 19  ? 11.439 -5.983  11.101  0.60 19.17 ?  19  LYS   A HB3  1 
ATOM   492  H HB3  B LYS   A 1 19  ? 11.413 -5.485  11.324  0.40 16.37 ?  19  LYS   A HB3  1 
ATOM   493  H HG2  A LYS   A 1 19  ? 9.755  -4.475  11.754  0.60 20.43 ?  19  LYS   A HG2  1 
ATOM   494  H HG2  B LYS   A 1 19  ? 9.532  -4.282  11.977  0.40 18.40 ?  19  LYS   A HG2  1 
ATOM   495  H HG3  A LYS   A 1 19  ? 9.001  -5.671  12.494  0.60 20.43 ?  19  LYS   A HG3  1 
ATOM   496  H HG3  B LYS   A 1 19  ? 8.967  -5.583  12.706  0.40 18.40 ?  19  LYS   A HG3  1 
ATOM   497  H HD2  A LYS   A 1 19  ? 10.842 -5.945  13.916  0.60 21.24 ?  19  LYS   A HD2  1 
ATOM   498  H HD2  B LYS   A 1 19  ? 10.772 -5.558  14.164  0.40 20.08 ?  19  LYS   A HD2  1 
ATOM   499  H HD3  A LYS   A 1 19  ? 11.593 -4.758  13.179  0.60 21.24 ?  19  LYS   A HD3  1 
ATOM   500  H HD3  B LYS   A 1 19  ? 11.362 -4.279  13.424  0.40 20.08 ?  19  LYS   A HD3  1 
ATOM   501  H HE2  A LYS   A 1 19  ? 10.035 -3.242  14.024  0.60 21.78 ?  19  LYS   A HE2  1 
ATOM   502  H HE2  B LYS   A 1 19  ? 9.485  -3.051  14.122  0.40 21.08 ?  19  LYS   A HE2  1 
ATOM   503  H HE3  A LYS   A 1 19  ? 9.279  -4.433  14.762  0.60 21.78 ?  19  LYS   A HE3  1 
ATOM   504  H HE3  B LYS   A 1 19  ? 8.982  -4.326  14.933  0.40 21.08 ?  19  LYS   A HE3  1 
ATOM   505  H HZ1  A LYS   A 1 19  ? 10.729 -3.284  16.160  0.60 21.74 ?  19  LYS   A HZ1  1 
ATOM   506  H HZ1  B LYS   A 1 19  ? 10.096 -2.897  16.305  0.40 21.53 ?  19  LYS   A HZ1  1 
ATOM   507  H HZ2  A LYS   A 1 19  ? 11.057 -4.694  16.111  0.60 21.74 ?  19  LYS   A HZ2  1 
ATOM   508  H HZ2  B LYS   A 1 19  ? 10.838 -4.140  16.234  0.40 21.53 ?  19  LYS   A HZ2  1 
ATOM   509  H HZ3  A LYS   A 1 19  ? 11.857 -3.738  15.374  0.60 21.74 ?  19  LYS   A HZ3  1 
ATOM   510  H HZ3  B LYS   A 1 19  ? 11.295 -2.980  15.496  0.40 21.53 ?  19  LYS   A HZ3  1 
ATOM   511  N N    A ASN   A 1 20  ? 8.538  -4.703  9.314   0.60 15.66 ?  20  ASN   A N    1 
ATOM   512  N N    B ASN   A 1 20  ? 8.517  -4.569  9.415   0.40 13.60 ?  20  ASN   A N    1 
ATOM   513  C CA   A ASN   A 1 20  ? 8.330  -3.360  8.773   0.60 16.57 ?  20  ASN   A CA   1 
ATOM   514  C CA   B ASN   A 1 20  ? 8.229  -3.288  8.767   0.40 14.39 ?  20  ASN   A CA   1 
ATOM   515  C C    A ASN   A 1 20  ? 8.987  -2.369  9.726   0.60 16.60 ?  20  ASN   A C    1 
ATOM   516  C C    B ASN   A 1 20  ? 8.778  -2.183  9.663   0.40 15.31 ?  20  ASN   A C    1 
ATOM   517  O O    A ASN   A 1 20  ? 8.508  -2.161  10.847  0.60 16.83 ?  20  ASN   A O    1 
ATOM   518  O O    B ASN   A 1 20  ? 8.113  -1.749  10.608  0.40 15.76 ?  20  ASN   A O    1 
ATOM   519  C CB   A ASN   A 1 20  ? 6.837  -3.079  8.609   0.60 17.59 ?  20  ASN   A CB   1 
ATOM   520  C CB   B ASN   A 1 20  ? 6.722  -3.137  8.569   0.40 14.61 ?  20  ASN   A CB   1 
ATOM   521  C CG   A ASN   A 1 20  ? 6.536  -1.625  8.256   0.60 19.05 ?  20  ASN   A CG   1 
ATOM   522  C CG   B ASN   A 1 20  ? 6.326  -1.828  7.886   0.40 15.09 ?  20  ASN   A CG   1 
ATOM   523  O OD1  A ASN   A 1 20  ? 5.589  -1.041  8.783   0.60 20.69 ?  20  ASN   A OD1  1 
ATOM   524  O OD1  B ASN   A 1 20  ? 5.175  -1.389  7.991   0.40 14.84 ?  20  ASN   A OD1  1 
ATOM   525  N ND2  A ASN   A 1 20  ? 7.331  -1.041  7.363   0.60 19.20 ?  20  ASN   A ND2  1 
ATOM   526  N ND2  B ASN   A 1 20  ? 7.265  -1.206  7.184   0.40 15.88 ?  20  ASN   A ND2  1 
ATOM   527  H H    A ASN   A 1 20  ? 7.864  -5.020  9.746   0.60 18.82 ?  20  ASN   A H    1 
ATOM   528  H H    B ASN   A 1 20  ? 7.848  -4.914  9.818   0.40 16.35 ?  20  ASN   A H    1 
ATOM   529  H HA   A ASN   A 1 20  ? 8.754  -3.294  7.905   0.60 19.91 ?  20  ASN   A HA   1 
ATOM   530  H HA   B ASN   A 1 20  ? 8.672  -3.254  7.903   0.40 17.29 ?  20  ASN   A HA   1 
ATOM   531  H HB2  A ASN   A 1 20  ? 6.485  -3.642  7.898   0.60 21.13 ?  20  ASN   A HB2  1 
ATOM   532  H HB2  B ASN   A 1 20  ? 6.397  -3.866  8.028   0.40 17.56 ?  20  ASN   A HB2  1 
ATOM   533  H HB3  A ASN   A 1 20  ? 6.383  -3.284  9.442   0.60 21.13 ?  20  ASN   A HB3  1 
ATOM   534  H HB3  B ASN   A 1 20  ? 6.294  -3.165  9.439   0.40 17.56 ?  20  ASN   A HB3  1 
ATOM   535  H HD21 A ASN   A 1 20  ? 7.193  -0.226  7.129   0.60 23.07 ?  20  ASN   A HD21 1 
ATOM   536  H HD21 B ASN   A 1 20  ? 7.081  -0.469  6.794   0.40 19.09 ?  20  ASN   A HD21 1 
ATOM   537  H HD22 A ASN   A 1 20  ? 7.987  -1.481  7.016   0.60 23.07 ?  20  ASN   A HD22 1 
ATOM   538  H HD22 B ASN   A 1 20  ? 8.058  -1.538  7.119   0.40 19.09 ?  20  ASN   A HD22 1 
ATOM   539  N N    A ALA   A 1 21  ? 10.103 -1.778  9.305   0.60 16.80 ?  21  ALA   A N    1 
ATOM   540  N N    B ALA   A 1 21  ? 9.996  -1.722  9.378   0.40 16.19 ?  21  ALA   A N    1 
ATOM   541  C CA   A ALA   A 1 21  ? 10.818 -0.895  10.211  0.60 16.66 ?  21  ALA   A CA   1 
ATOM   542  C CA   B ALA   A 1 21  ? 10.640 -0.738  10.239  0.40 16.62 ?  21  ALA   A CA   1 
ATOM   543  C C    A ALA   A 1 21  ? 11.777 -0.013  9.432   0.60 15.92 ?  21  ALA   A C    1 
ATOM   544  C C    B ALA   A 1 21  ? 11.732 -0.008  9.470   0.40 15.93 ?  21  ALA   A C    1 
ATOM   545  O O    A ALA   A 1 21  ? 12.278 -0.399  8.372   0.60 16.43 ?  21  ALA   A O    1 
ATOM   546  O O    B ALA   A 1 21  ? 12.115 -0.398  8.365   0.40 15.97 ?  21  ALA   A O    1 
ATOM   547  C CB   A ALA   A 1 21  ? 11.578 -1.699  11.268  0.60 17.27 ?  21  ALA   A CB   1 
ATOM   548  C CB   B ALA   A 1 21  ? 11.218 -1.392  11.496  0.40 17.35 ?  21  ALA   A CB   1 
ATOM   549  H H    A ALA   A 1 21  ? 10.453 -1.872  8.525   0.60 20.19 ?  21  ALA   A H    1 
ATOM   550  H H    B ALA   A 1 21  ? 10.461 -1.961  8.694   0.40 19.45 ?  21  ALA   A H    1 
ATOM   551  H HA   A ALA   A 1 21  ? 10.174 -0.324  10.666  0.60 20.02 ?  21  ALA   A HA   1 
ATOM   552  H HA   B ALA   A 1 21  ? 9.980  -0.086  10.516  0.40 19.97 ?  21  ALA   A HA   1 
ATOM   553  H HB1  A ALA   A 1 21  ? 11.990 -1.082  11.885  0.60 20.75 ?  21  ALA   A HB1  1 
ATOM   554  H HB1  B ALA   A 1 21  ? 11.636 -0.708  12.042  0.40 20.84 ?  21  ALA   A HB1  1 
ATOM   555  H HB2  A ALA   A 1 21  ? 10.945 -2.268  11.742  0.60 20.75 ?  21  ALA   A HB2  1 
ATOM   556  H HB2  B ALA   A 1 21  ? 10.499 -1.816  11.990  0.40 20.84 ?  21  ALA   A HB2  1 
ATOM   557  H HB3  A ALA   A 1 21  ? 12.245 -2.242  10.828  0.60 20.75 ?  21  ALA   A HB3  1 
ATOM   558  H HB3  B ALA   A 1 21  ? 11.876 -2.055  11.234  0.40 20.84 ?  21  ALA   A HB3  1 
ATOM   559  N N    A ASP   A 1 22  ? 11.998 1.185   9.972   0.60 15.43 ?  22  ASP   A N    1 
ATOM   560  N N    B ASP   A 1 22  ? 12.223 1.069   10.086  0.40 15.69 ?  22  ASP   A N    1 
ATOM   561  C CA   A ASP   A 1 22  ? 13.058 2.076   9.521   0.60 15.07 ?  22  ASP   A CA   1 
ATOM   562  C CA   B ASP   A 1 22  ? 13.362 1.829   9.593   0.40 15.71 ?  22  ASP   A CA   1 
ATOM   563  C C    A ASP   A 1 22  ? 14.373 1.581   10.109  0.60 14.56 ?  22  ASP   A C    1 
ATOM   564  C C    B ASP   A 1 22  ? 14.629 1.230   10.194  0.40 14.50 ?  22  ASP   A C    1 
ATOM   565  O O    A ASP   A 1 22  ? 14.549 1.581   11.332  0.60 15.28 ?  22  ASP   A O    1 
ATOM   566  O O    B ASP   A 1 22  ? 14.741 1.102   11.418  0.40 14.60 ?  22  ASP   A O    1 
ATOM   567  C CB   A ASP   A 1 22  ? 12.739 3.491   10.000  0.60 16.35 ?  22  ASP   A CB   1 
ATOM   568  C CB   B ASP   A 1 22  ? 13.225 3.289   10.031  0.40 17.05 ?  22  ASP   A CB   1 
ATOM   569  C CG   A ASP   A 1 22  ? 13.803 4.507   9.615   0.60 17.56 ?  22  ASP   A CG   1 
ATOM   570  C CG   B ASP   A 1 22  ? 14.227 4.209   9.355   0.40 18.35 ?  22  ASP   A CG   1 
ATOM   571  O OD1  A ASP   A 1 22  ? 14.895 4.130   9.145   0.60 17.92 ?  22  ASP   A OD1  1 
ATOM   572  O OD1  B ASP   A 1 22  ? 15.320 3.734   8.980   0.40 18.65 ?  22  ASP   A OD1  1 
ATOM   573  O OD2  A ASP   A 1 22  ? 13.538 5.713   9.789   0.60 19.00 -1 22  ASP   A OD2  1 
ATOM   574  O OD2  B ASP   A 1 22  ? 13.928 5.414   9.205   0.40 19.48 -1 22  ASP   A OD2  1 
ATOM   575  H H    A ASP   A 1 22  ? 11.517 1.511   10.616  0.60 18.55 ?  22  ASP   A H    1 
ATOM   576  H H    B ASP   A 1 22  ? 11.897 1.383   10.818  0.40 18.86 ?  22  ASP   A H    1 
ATOM   577  H HA   A ASP   A 1 22  ? 13.106 2.066   8.553   0.60 18.11 ?  22  ASP   A HA   1 
ATOM   578  H HA   B ASP   A 1 22  ? 13.406 1.781   8.623   0.40 18.88 ?  22  ASP   A HA   1 
ATOM   579  H HB2  A ASP   A 1 22  ? 11.889 3.773   9.616   0.60 19.64 ?  22  ASP   A HB2  1 
ATOM   580  H HB2  B ASP   A 1 22  ? 12.333 3.599   9.823   0.40 20.49 ?  22  ASP   A HB2  1 
ATOM   581  H HB3  A ASP   A 1 22  ? 12.672 3.489   10.968  0.60 19.64 ?  22  ASP   A HB3  1 
ATOM   582  H HB3  B ASP   A 1 22  ? 13.386 3.345   10.985  0.40 20.49 ?  22  ASP   A HB3  1 
ATOM   583  N N    A ILE   A 1 23  ? 15.290 1.157   9.237   0.60 14.19 ?  23  ILE   A N    1 
ATOM   584  N N    B ILE   A 1 23  ? 15.579 0.860   9.331   0.40 14.00 ?  23  ILE   A N    1 
ATOM   585  C CA   A ILE   A 1 23  ? 16.540 0.553   9.691   0.60 13.73 ?  23  ILE   A CA   1 
ATOM   586  C CA   B ILE   A 1 23  ? 16.810 0.229   9.797   0.40 13.84 ?  23  ILE   A CA   1 
ATOM   587  C C    A ILE   A 1 23  ? 17.327 1.509   10.575  0.60 13.92 ?  23  ILE   A C    1 
ATOM   588  C C    B ILE   A 1 23  ? 17.565 1.143   10.752  0.40 14.08 ?  23  ILE   A C    1 
ATOM   589  O O    A ILE   A 1 23  ? 18.047 1.073   11.482  0.60 14.57 ?  23  ILE   A O    1 
ATOM   590  O O    B ILE   A 1 23  ? 18.240 0.670   11.675  0.40 13.61 ?  23  ILE   A O    1 
ATOM   591  C CB   A ILE   A 1 23  ? 17.360 0.047   8.483   0.60 13.31 ?  23  ILE   A CB   1 
ATOM   592  C CB   B ILE   A 1 23  ? 17.679 -0.231  8.604   0.40 13.32 ?  23  ILE   A CB   1 
ATOM   593  C CG1  A ILE   A 1 23  ? 18.475 -0.896  8.939   0.60 13.27 ?  23  ILE   A CG1  1 
ATOM   594  C CG1  B ILE   A 1 23  ? 18.734 -1.232  9.083   0.40 13.53 ?  23  ILE   A CG1  1 
ATOM   595  C CG2  A ILE   A 1 23  ? 17.912 1.218   7.666   0.60 13.55 ?  23  ILE   A CG2  1 
ATOM   596  C CG2  B ILE   A 1 23  ? 18.339 0.958   7.903   0.40 13.15 ?  23  ILE   A CG2  1 
ATOM   597  C CD1  A ILE   A 1 23  ? 19.171 -1.600  7.798   0.60 13.11 ?  23  ILE   A CD1  1 
ATOM   598  C CD1  B ILE   A 1 23  ? 19.595 -1.790  7.985   0.40 13.68 ?  23  ILE   A CD1  1 
ATOM   599  H H    A ILE   A 1 23  ? 15.203 1.206   8.388   0.60 17.05 ?  23  ILE   A H    1 
ATOM   600  H H    B ILE   A 1 23  ? 15.533 0.960   8.488   0.40 16.83 ?  23  ILE   A H    1 
ATOM   601  H HA   A ILE   A 1 23  ? 16.319 -0.219  10.235  0.60 16.51 ?  23  ILE   A HA   1 
ATOM   602  H HA   B ILE   A 1 23  ? 16.568 -0.568  10.288  0.40 16.64 ?  23  ILE   A HA   1 
ATOM   603  H HB   A ILE   A 1 23  ? 16.758 -0.457  7.914   0.60 15.99 ?  23  ILE   A HB   1 
ATOM   604  H HB   B ILE   A 1 23  ? 17.106 -0.683  7.962   0.40 16.01 ?  23  ILE   A HB   1 
ATOM   605  H HG12 A ILE   A 1 23  ? 19.139 -0.385  9.426   0.60 15.95 ?  23  ILE   A HG12 1 
ATOM   606  H HG12 B ILE   A 1 23  ? 19.315 -0.792  9.720   0.40 16.26 ?  23  ILE   A HG12 1 
ATOM   607  H HG13 A ILE   A 1 23  ? 18.093 -1.576  9.520   0.60 15.95 ?  23  ILE   A HG13 1 
ATOM   608  H HG13 B ILE   A 1 23  ? 18.283 -1.979  9.510   0.40 16.26 ?  23  ILE   A HG13 1 
ATOM   609  H HG21 A ILE   A 1 23  ? 18.257 0.877   6.826   0.60 16.29 ?  23  ILE   A HG21 1 
ATOM   610  H HG21 B ILE   A 1 23  ? 18.691 0.662   7.045   0.40 15.81 ?  23  ILE   A HG21 1 
ATOM   611  H HG22 A ILE   A 1 23  ? 17.192 1.848   7.495   0.60 16.29 ?  23  ILE   A HG22 1 
ATOM   612  H HG22 B ILE   A 1 23  ? 17.674 1.648   7.763   0.40 15.81 ?  23  ILE   A HG22 1 
ATOM   613  H HG23 A ILE   A 1 23  ? 18.618 1.650   8.166   0.60 16.29 ?  23  ILE   A HG23 1 
ATOM   614  H HG23 B ILE   A 1 23  ? 19.058 1.293   8.457   0.40 15.81 ?  23  ILE   A HG23 1 
ATOM   615  H HD11 A ILE   A 1 23  ? 19.808 -2.233  8.162   0.60 15.76 ?  23  ILE   A HD11 1 
ATOM   616  H HD11 B ILE   A 1 23  ? 20.147 -2.499  8.348   0.40 16.44 ?  23  ILE   A HD11 1 
ATOM   617  H HD12 A ILE   A 1 23  ? 18.507 -2.067  7.266   0.60 15.76 ?  23  ILE   A HD12 1 
ATOM   618  H HD12 B ILE   A 1 23  ? 19.021 -2.140  7.287   0.40 16.44 ?  23  ILE   A HD12 1 
ATOM   619  H HD13 A ILE   A 1 23  ? 19.628 -0.941  7.254   0.60 15.76 ?  23  ILE   A HD13 1 
ATOM   620  H HD13 B ILE   A 1 23  ? 20.154 -1.081  7.632   0.40 16.44 ?  23  ILE   A HD13 1 
ATOM   621  N N    A VAL   A 1 24  ? 17.196 2.817   10.346  0.60 14.13 ?  24  VAL   A N    1 
ATOM   622  N N    B VAL   A 1 24  ? 17.455 2.460   10.562  0.40 15.25 ?  24  VAL   A N    1 
ATOM   623  C CA   A VAL   A 1 24  ? 17.867 3.791   11.204  0.60 15.01 ?  24  VAL   A CA   1 
ATOM   624  C CA   B VAL   A 1 24  ? 18.117 3.403   11.460  0.40 16.08 ?  24  VAL   A CA   1 
ATOM   625  C C    A VAL   A 1 24  ? 17.329 3.703   12.625  0.60 15.64 ?  24  VAL   A C    1 
ATOM   626  C C    B VAL   A 1 24  ? 17.534 3.296   12.864  0.40 16.62 ?  24  VAL   A C    1 
ATOM   627  O O    A VAL   A 1 24  ? 18.091 3.625   13.597  0.60 16.63 ?  24  VAL   A O    1 
ATOM   628  O O    B VAL   A 1 24  ? 18.265 3.305   13.864  0.40 16.81 ?  24  VAL   A O    1 
ATOM   629  C CB   A VAL   A 1 24  ? 17.718 5.211   10.628  0.60 15.69 ?  24  VAL   A CB   1 
ATOM   630  C CB   B VAL   A 1 24  ? 18.009 4.833   10.897  0.40 16.71 ?  24  VAL   A CB   1 
ATOM   631  C CG1  A VAL   A 1 24  ? 18.226 6.256   11.621  0.60 16.25 ?  24  VAL   A CG1  1 
ATOM   632  C CG1  B VAL   A 1 24  ? 18.615 5.832   11.864  0.40 17.25 ?  24  VAL   A CG1  1 
ATOM   633  C CG2  A VAL   A 1 24  ? 18.441 5.326   9.296   0.60 16.45 ?  24  VAL   A CG2  1 
ATOM   634  C CG2  B VAL   A 1 24  ? 18.682 4.913   9.534   0.40 17.43 ?  24  VAL   A CG2  1 
ATOM   635  H H    A VAL   A 1 24  ? 16.731 3.162   9.711   0.60 16.98 ?  24  VAL   A H    1 
ATOM   636  H H    B VAL   A 1 24  ? 17.006 2.825   9.928   0.40 18.33 ?  24  VAL   A H    1 
ATOM   637  H HA   A VAL   A 1 24  ? 18.812 3.587   11.237  0.60 18.05 ?  24  VAL   A HA   1 
ATOM   638  H HA   B VAL   A 1 24  ? 19.060 3.178   11.509  0.40 19.32 ?  24  VAL   A HA   1 
ATOM   639  H HB   A VAL   A 1 24  ? 16.776 5.390   10.467  0.60 18.86 ?  24  VAL   A HB   1 
ATOM   640  H HB   B VAL   A 1 24  ? 17.072 5.056   10.778  0.40 20.08 ?  24  VAL   A HB   1 
ATOM   641  H HG11 A VAL   A 1 24  ? 18.375 7.090   11.150  0.60 19.52 ?  24  VAL   A HG11 1 
ATOM   642  H HG11 B VAL   A 1 24  ? 18.943 6.594   11.362  0.40 20.73 ?  24  VAL   A HG11 1 
ATOM   643  H HG12 A VAL   A 1 24  ? 17.564 6.381   12.317  0.60 19.52 ?  24  VAL   A HG12 1 
ATOM   644  H HG12 B VAL   A 1 24  ? 17.923 6.115   12.478  0.40 20.73 ?  24  VAL   A HG12 1 
ATOM   645  H HG13 A VAL   A 1 24  ? 19.060 5.941   12.005  0.60 19.52 ?  24  VAL   A HG13 1 
ATOM   646  H HG13 B VAL   A 1 24  ? 19.345 5.410   12.343  0.40 20.73 ?  24  VAL   A HG13 1 
ATOM   647  H HG21 A VAL   A 1 24  ? 18.272 6.201   8.916   0.60 19.77 ?  24  VAL   A HG21 1 
ATOM   648  H HG21 B VAL   A 1 24  ? 18.617 5.823   9.203   0.40 20.94 ?  24  VAL   A HG21 1 
ATOM   649  H HG22 A VAL   A 1 24  ? 19.393 5.208   9.444   0.60 19.77 ?  24  VAL   A HG22 1 
ATOM   650  H HG22 B VAL   A 1 24  ? 19.614 4.662   9.627   0.40 20.94 ?  24  VAL   A HG22 1 
ATOM   651  H HG23 A VAL   A 1 24  ? 18.113 4.636   8.696   0.60 19.77 ?  24  VAL   A HG23 1 
ATOM   652  H HG23 B VAL   A 1 24  ? 18.236 4.307   8.921   0.40 20.94 ?  24  VAL   A HG23 1 
ATOM   653  N N    A GLU   A 1 25  ? 16.002 3.718   12.767  0.60 16.42 ?  25  GLU   A N    1 
ATOM   654  N N    B GLU   A 1 25  ? 16.208 3.180   12.958  0.40 17.10 ?  25  GLU   A N    1 
ATOM   655  C CA   A GLU   A 1 25  ? 15.412 3.669   14.101  0.60 17.56 ?  25  GLU   A CA   1 
ATOM   656  C CA   B GLU   A 1 25  ? 15.561 3.050   14.259  0.40 18.02 ?  25  GLU   A CA   1 
ATOM   657  C C    A GLU   A 1 25  ? 15.641 2.314   14.758  0.60 16.50 ?  25  GLU   A C    1 
ATOM   658  C C    B GLU   A 1 25  ? 15.850 1.692   14.889  0.40 17.24 ?  25  GLU   A C    1 
ATOM   659  O O    A GLU   A 1 25  ? 15.857 2.238   15.973  0.60 17.38 ?  25  GLU   A O    1 
ATOM   660  O O    B GLU   A 1 25  ? 16.093 1.604   16.099  0.40 17.43 ?  25  GLU   A O    1 
ATOM   661  C CB   A GLU   A 1 25  ? 13.925 4.028   14.038  0.60 20.07 ?  25  GLU   A CB   1 
ATOM   662  C CB   B GLU   A 1 25  ? 14.058 3.290   14.114  0.40 19.24 ?  25  GLU   A CB   1 
ATOM   663  C CG   A GLU   A 1 25  ? 13.681 5.496   13.695  0.60 22.78 ?  25  GLU   A CG   1 
ATOM   664  C CG   B GLU   A 1 25  ? 13.716 4.682   13.598  0.40 21.26 ?  25  GLU   A CG   1 
ATOM   665  C CD   A GLU   A 1 25  ? 14.536 6.450   14.515  0.60 25.15 ?  25  GLU   A CD   1 
ATOM   666  C CD   B GLU   A 1 25  ? 14.199 5.782   14.525  0.40 23.06 ?  25  GLU   A CD   1 
ATOM   667  O OE1  A GLU   A 1 25  ? 14.619 6.275   15.750  0.60 25.73 ?  25  GLU   A OE1  1 
ATOM   668  O OE1  B GLU   A 1 25  ? 14.184 5.571   15.758  0.40 23.64 ?  25  GLU   A OE1  1 
ATOM   669  O OE2  A GLU   A 1 25  ? 15.144 7.365   13.918  0.60 26.38 -1 25  GLU   A OE2  1 
ATOM   670  O OE2  B GLU   A 1 25  ? 14.598 6.854   14.021  0.40 24.09 -1 25  GLU   A OE2  1 
ATOM   671  H H    A GLU   A 1 25  ? 15.432 3.769   12.120  0.60 19.73 ?  25  GLU   A H    1 
ATOM   672  H H    B GLU   A 1 25  ? 15.672 3.176   12.288  0.40 20.55 ?  25  GLU   A H    1 
ATOM   673  H HA   A GLU   A 1 25  ? 15.856 4.324   14.657  0.60 21.10 ?  25  GLU   A HA   1 
ATOM   674  H HA   B GLU   A 1 25  ? 15.916 3.727   14.851  0.40 21.65 ?  25  GLU   A HA   1 
ATOM   675  H HB2  A GLU   A 1 25  ? 13.492 3.492   13.352  0.60 24.11 ?  25  GLU   A HB2  1 
ATOM   676  H HB2  B GLU   A 1 25  ? 13.694 2.644   13.489  0.40 23.11 ?  25  GLU   A HB2  1 
ATOM   677  H HB3  A GLU   A 1 25  ? 13.515 3.854   14.900  0.60 24.11 ?  25  GLU   A HB3  1 
ATOM   678  H HB3  B GLU   A 1 25  ? 13.639 3.183   14.981  0.40 23.11 ?  25  GLU   A HB3  1 
ATOM   679  H HG2  A GLU   A 1 25  ? 13.894 5.643   12.763  0.60 27.37 ?  25  GLU   A HG2  1 
ATOM   680  H HG2  B GLU   A 1 25  ? 14.135 4.812   12.733  0.40 25.54 ?  25  GLU   A HG2  1 
ATOM   681  H HG3  A GLU   A 1 25  ? 12.749 5.711   13.864  0.60 27.37 ?  25  GLU   A HG3  1 
ATOM   682  H HG3  B GLU   A 1 25  ? 12.752 4.759   13.514  0.40 25.54 ?  25  GLU   A HG3  1 
ATOM   683  N N    A GLU   A 1 26  ? 15.619 1.235   13.972  0.60 16.04 ?  26  GLU   A N    1 
ATOM   684  N N    B GLU   A 1 26  ? 15.844 0.622   14.088  0.40 16.96 ?  26  GLU   A N    1 
ATOM   685  C CA   A GLU   A 1 26  ? 15.926 -0.082  14.523  0.60 15.95 ?  26  GLU   A CA   1 
ATOM   686  C CA   B GLU   A 1 26  ? 16.238 -0.683  14.613  0.40 17.01 ?  26  GLU   A CA   1 
ATOM   687  C C    A GLU   A 1 26  ? 17.356 -0.132  15.039  0.60 15.41 ?  26  GLU   A C    1 
ATOM   688  C C    B GLU   A 1 26  ? 17.664 -0.645  15.146  0.40 16.73 ?  26  GLU   A C    1 
ATOM   689  O O    A GLU   A 1 26  ? 17.619 -0.643  16.132  0.60 15.55 ?  26  GLU   A O    1 
ATOM   690  O O    B GLU   A 1 26  ? 17.954 -1.209  16.207  0.40 16.97 ?  26  GLU   A O    1 
ATOM   691  C CB   A GLU   A 1 26  ? 15.734 -1.150  13.450  0.60 17.18 ?  26  GLU   A CB   1 
ATOM   692  C CB   B GLU   A 1 26  ? 16.089 -1.763  13.539  0.40 17.82 ?  26  GLU   A CB   1 
ATOM   693  C CG   A GLU   A 1 26  ? 14.309 -1.581  13.246  0.60 20.18 ?  26  GLU   A CG   1 
ATOM   694  C CG   B GLU   A 1 26  ? 14.658 -2.136  13.227  0.40 18.43 ?  26  GLU   A CG   1 
ATOM   695  C CD   A GLU   A 1 26  ? 13.758 -2.357  14.417  0.60 22.25 ?  26  GLU   A CD   1 
ATOM   696  C CD   B GLU   A 1 26  ? 13.967 -2.787  14.398  0.40 18.71 ?  26  GLU   A CD   1 
ATOM   697  O OE1  A GLU   A 1 26  ? 14.386 -3.353  14.827  0.60 22.76 ?  26  GLU   A OE1  1 
ATOM   698  O OE1  B GLU   A 1 26  ? 14.362 -3.909  14.806  0.40 18.68 ?  26  GLU   A OE1  1 
ATOM   699  O OE2  A GLU   A 1 26  ? 12.701 -1.944  14.936  0.60 23.74 -1 26  GLU   A OE2  1 
ATOM   700  O OE2  B GLU   A 1 26  ? 13.030 -2.157  14.908  0.40 18.85 -1 26  GLU   A OE2  1 
ATOM   701  H H    A GLU   A 1 26  ? 15.416 1.244   13.135  0.60 19.27 ?  26  GLU   A H    1 
ATOM   702  H H    B GLU   A 1 26  ? 15.618 0.622   13.258  0.40 20.38 ?  26  GLU   A H    1 
ATOM   703  H HA   A GLU   A 1 26  ? 15.321 -0.270  15.258  0.60 19.16 ?  26  GLU   A HA   1 
ATOM   704  H HA   B GLU   A 1 26  ? 15.658 -0.915  15.351  0.40 20.44 ?  26  GLU   A HA   1 
ATOM   705  H HB2  A GLU   A 1 26  ? 16.055 -0.800  12.604  0.60 20.65 ?  26  GLU   A HB2  1 
ATOM   706  H HB2  B GLU   A 1 26  ? 16.492 -1.451  12.717  0.40 21.42 ?  26  GLU   A HB2  1 
ATOM   707  H HB3  A GLU   A 1 26  ? 16.251 -1.930  13.699  0.60 20.65 ?  26  GLU   A HB3  1 
ATOM   708  H HB3  B GLU   A 1 26  ? 16.538 -2.571  13.840  0.40 21.42 ?  26  GLU   A HB3  1 
ATOM   709  H HG2  A GLU   A 1 26  ? 13.749 -0.802  13.178  0.60 24.25 ?  26  GLU   A HG2  1 
ATOM   710  H HG2  B GLU   A 1 26  ? 14.166 -1.333  12.974  0.40 22.14 ?  26  GLU   A HG2  1 
ATOM   711  H HG3  A GLU   A 1 26  ? 14.254 -2.112  12.432  0.60 24.25 ?  26  GLU   A HG3  1 
ATOM   712  H HG3  B GLU   A 1 26  ? 14.634 -2.778  12.507  0.40 22.14 ?  26  GLU   A HG3  1 
ATOM   713  N N    A ALA   A 1 27  ? 18.300 0.389   14.250  0.60 15.15 ?  27  ALA   A N    1 
ATOM   714  N N    B ALA   A 1 27  ? 18.570 0.025   14.432  0.40 16.80 ?  27  ALA   A N    1 
ATOM   715  C CA   A ALA   A 1 27  ? 19.701 0.357   14.652  0.60 16.10 ?  27  ALA   A CA   1 
ATOM   716  C CA   B ALA   A 1 27  ? 19.945 0.111   14.911  0.40 17.30 ?  27  ALA   A CA   1 
ATOM   717  C C    A ALA   A 1 27  ? 19.907 1.087   15.971  0.60 17.69 ?  27  ALA   A C    1 
ATOM   718  C C    B ALA   A 1 27  ? 20.044 1.007   16.141  0.40 18.52 ?  27  ALA   A C    1 
ATOM   719  O O    A ALA   A 1 27  ? 20.607 0.593   16.863  0.60 18.19 ?  27  ALA   A O    1 
ATOM   720  O O    B ALA   A 1 27  ? 20.710 0.653   17.122  0.40 18.10 ?  27  ALA   A O    1 
ATOM   721  C CB   A ALA   A 1 27  ? 20.570 0.974   13.555  0.60 15.73 ?  27  ALA   A CB   1 
ATOM   722  C CB   B ALA   A 1 27  ? 20.870 0.593   13.791  0.40 16.97 ?  27  ALA   A CB   1 
ATOM   723  H H    A ALA   A 1 27  ? 18.146 0.769   13.491  0.60 18.21 ?  27  ALA   A H    1 
ATOM   724  H H    B ALA   A 1 27  ? 18.418 0.422   13.682  0.40 20.18 ?  27  ALA   A H    1 
ATOM   725  H HA   A ALA   A 1 27  ? 19.968 -0.564  14.769  0.60 19.35 ?  27  ALA   A HA   1 
ATOM   726  H HA   B ALA   A 1 27  ? 20.239 -0.775  15.168  0.40 20.78 ?  27  ALA   A HA   1 
ATOM   727  H HB1  A ALA   A 1 27  ? 21.495 0.944   13.835  0.60 18.90 ?  27  ALA   A HB1  1 
ATOM   728  H HB1  B ALA   A 1 27  ? 21.781 0.632   14.126  0.40 20.40 ?  27  ALA   A HB1  1 
ATOM   729  H HB2  A ALA   A 1 27  ? 20.450 0.469   12.736  0.60 18.90 ?  27  ALA   A HB2  1 
ATOM   730  H HB2  B ALA   A 1 27  ? 20.822 -0.034  13.049  0.40 20.40 ?  27  ALA   A HB2  1 
ATOM   731  H HB3  A ALA   A 1 27  ? 20.294 1.896   13.416  0.60 18.90 ?  27  ALA   A HB3  1 
ATOM   732  H HB3  B ALA   A 1 27  ? 20.588 1.471   13.498  0.40 20.40 ?  27  ALA   A HB3  1 
ATOM   733  N N    A LYS   A 1 28  ? 19.290 2.260   16.122  0.60 19.63 ?  28  LYS   A N    1 
ATOM   734  N N    B LYS   A 1 28  ? 19.369 2.161   16.122  0.40 20.39 ?  28  LYS   A N    1 
ATOM   735  C CA   A LYS   A 1 28  ? 19.479 3.031   17.344  0.60 22.73 ?  28  LYS   A CA   1 
ATOM   736  C CA   B LYS   A 1 28  ? 19.401 3.050   17.280  0.40 22.86 ?  28  LYS   A CA   1 
ATOM   737  C C    A LYS   A 1 28  ? 18.906 2.316   18.559  0.60 23.95 ?  28  LYS   A C    1 
ATOM   738  C C    B LYS   A 1 28  ? 18.883 2.348   18.529  0.40 23.91 ?  28  LYS   A C    1 
ATOM   739  O O    A LYS   A 1 28  ? 19.422 2.481   19.670  0.60 25.16 ?  28  LYS   A O    1 
ATOM   740  O O    B LYS   A 1 28  ? 19.406 2.554   19.630  0.40 24.82 ?  28  LYS   A O    1 
ATOM   741  C CB   A LYS   A 1 28  ? 18.885 4.431   17.184  0.60 24.79 ?  28  LYS   A CB   1 
ATOM   742  C CB   B LYS   A 1 28  ? 18.598 4.322   17.001  0.40 24.40 ?  28  LYS   A CB   1 
ATOM   743  C CG   A LYS   A 1 28  ? 19.653 5.284   16.188  0.60 26.71 ?  28  LYS   A CG   1 
ATOM   744  C CG   B LYS   A 1 28  ? 19.406 5.418   16.327  0.40 25.88 ?  28  LYS   A CG   1 
ATOM   745  C CD   A LYS   A 1 28  ? 19.239 6.743   16.225  0.60 28.89 ?  28  LYS   A CD   1 
ATOM   746  C CD   B LYS   A 1 28  ? 18.729 6.780   16.437  0.40 27.64 ?  28  LYS   A CD   1 
ATOM   747  C CE   A LYS   A 1 28  ? 17.916 6.965   15.525  0.60 30.49 ?  28  LYS   A CE   1 
ATOM   748  C CE   B LYS   A 1 28  ? 17.855 7.069   15.232  0.40 29.07 ?  28  LYS   A CE   1 
ATOM   749  N NZ   A LYS   A 1 28  ? 17.587 8.415   15.437  0.60 31.46 ?  28  LYS   A NZ   1 
ATOM   750  N NZ   B LYS   A 1 28  ? 17.624 8.530   15.055  0.40 29.90 ?  28  LYS   A NZ   1 
ATOM   751  H H    A LYS   A 1 28  ? 18.763 2.619   15.548  0.60 23.58 ?  28  LYS   A H    1 
ATOM   752  H H    B LYS   A 1 28  ? 18.890 2.441   15.465  0.40 24.49 ?  28  LYS   A H    1 
ATOM   753  H HA   A LYS   A 1 28  ? 20.427 3.135   17.498  0.60 27.31 ?  28  LYS   A HA   1 
ATOM   754  H HA   B LYS   A 1 28  ? 20.316 3.309   17.452  0.40 27.46 ?  28  LYS   A HA   1 
ATOM   755  H HB2  A LYS   A 1 28  ? 17.971 4.354   16.870  0.60 29.78 ?  28  LYS   A HB2  1 
ATOM   756  H HB2  B LYS   A 1 28  ? 17.854 4.106   16.418  0.40 29.31 ?  28  LYS   A HB2  1 
ATOM   757  H HB3  A LYS   A 1 28  ? 18.904 4.883   18.042  0.60 29.78 ?  28  LYS   A HB3  1 
ATOM   758  H HB3  B LYS   A 1 28  ? 18.266 4.675   17.841  0.40 29.31 ?  28  LYS   A HB3  1 
ATOM   759  H HG2  A LYS   A 1 28  ? 20.600 5.234   16.394  0.60 32.08 ?  28  LYS   A HG2  1 
ATOM   760  H HG2  B LYS   A 1 28  ? 20.274 5.483   16.752  0.40 31.09 ?  28  LYS   A HG2  1 
ATOM   761  H HG3  A LYS   A 1 28  ? 19.490 4.947   15.293  0.60 32.08 ?  28  LYS   A HG3  1 
ATOM   762  H HG3  B LYS   A 1 28  ? 19.511 5.205   15.386  0.40 31.09 ?  28  LYS   A HG3  1 
ATOM   763  H HD2  A LYS   A 1 28  ? 19.145 7.026   17.148  0.60 34.69 ?  28  LYS   A HD2  1 
ATOM   764  H HD2  B LYS   A 1 28  ? 18.168 6.799   17.230  0.40 33.19 ?  28  LYS   A HD2  1 
ATOM   765  H HD3  A LYS   A 1 28  ? 19.913 7.278   15.777  0.60 34.69 ?  28  LYS   A HD3  1 
ATOM   766  H HD3  B LYS   A 1 28  ? 19.407 7.471   16.491  0.40 33.19 ?  28  LYS   A HD3  1 
ATOM   767  H HE2  A LYS   A 1 28  ? 17.966 6.609   14.623  0.60 36.62 ?  28  LYS   A HE2  1 
ATOM   768  H HE2  B LYS   A 1 28  ? 18.298 6.739   14.438  0.40 34.91 ?  28  LYS   A HE2  1 
ATOM   769  H HE3  A LYS   A 1 28  ? 17.211 6.522   16.022  0.60 36.62 ?  28  LYS   A HE3  1 
ATOM   770  H HE3  B LYS   A 1 28  ? 16.994 6.634   15.344  0.40 34.91 ?  28  LYS   A HE3  1 
ATOM   771  H HZ1  A LYS   A 1 28  ? 16.808 8.527   15.023  0.60 37.78 ?  28  LYS   A HZ1  1 
ATOM   772  H HZ1  B LYS   A 1 28  ? 17.111 8.674   14.342  0.40 35.91 ?  28  LYS   A HZ1  1 
ATOM   773  H HZ2  A LYS   A 1 28  ? 17.534 8.765   16.254  0.60 37.78 ?  28  LYS   A HZ2  1 
ATOM   774  H HZ2  B LYS   A 1 28  ? 17.222 8.865   15.774  0.40 35.91 ?  28  LYS   A HZ2  1 
ATOM   775  H HZ3  A LYS   A 1 28  ? 18.221 8.844   14.981  0.60 37.78 ?  28  LYS   A HZ3  1 
ATOM   776  H HZ3  B LYS   A 1 28  ? 18.402 8.948   14.938  0.40 35.91 ?  28  LYS   A HZ3  1 
ATOM   777  N N    . LYS   A 1 29  ? 17.859 1.508   18.374  1.00 24.43 ?  29  LYS   A N    1 
ATOM   778  C CA   . LYS   A 1 29  ? 17.268 0.803   19.508  1.00 26.77 ?  29  LYS   A CA   1 
ATOM   779  C C    . LYS   A 1 29  ? 18.094 -0.417  19.903  1.00 26.22 ?  29  LYS   A C    1 
ATOM   780  O O    . LYS   A 1 29  ? 18.370 -0.634  21.089  1.00 27.44 ?  29  LYS   A O    1 
ATOM   781  C CB   . LYS   A 1 29  ? 15.838 0.379   19.160  1.00 30.37 ?  29  LYS   A CB   1 
ATOM   782  C CG   . LYS   A 1 29  ? 15.082 -0.283  20.303  1.00 33.73 ?  29  LYS   A CG   1 
ATOM   783  C CD   . LYS   A 1 29  ? 14.720 0.723   21.382  1.00 36.69 ?  29  LYS   A CD   1 
ATOM   784  C CE   . LYS   A 1 29  ? 13.875 0.088   22.475  1.00 38.76 ?  29  LYS   A CE   1 
ATOM   785  N NZ   . LYS   A 1 29  ? 13.464 1.084   23.502  1.00 39.96 ?  29  LYS   A NZ   1 
ATOM   786  H H    A LYS   A 1 29  ? 17.476 1.358   17.619  0.60 29.35 ?  29  LYS   A H    1 
ATOM   787  H H    B LYS   A 1 29  ? 17.487 1.327   17.620  0.40 29.35 ?  29  LYS   A H    1 
ATOM   788  H HA   . LYS   A 1 29  ? 17.226 1.400   20.270  1.00 32.15 ?  29  LYS   A HA   1 
ATOM   789  H HB2  . LYS   A 1 29  ? 15.334 1.165   18.895  1.00 36.47 ?  29  LYS   A HB2  1 
ATOM   790  H HB3  . LYS   A 1 29  ? 15.868 -0.253  18.425  1.00 36.47 ?  29  LYS   A HB3  1 
ATOM   791  H HG2  . LYS   A 1 29  ? 14.260 -0.670  19.961  1.00 40.50 ?  29  LYS   A HG2  1 
ATOM   792  H HG3  . LYS   A 1 29  ? 15.633 -0.975  20.703  1.00 40.50 ?  29  LYS   A HG3  1 
ATOM   793  H HD2  . LYS   A 1 29  ? 15.532 1.066   21.786  1.00 44.06 ?  29  LYS   A HD2  1 
ATOM   794  H HD3  . LYS   A 1 29  ? 14.210 1.447   20.985  1.00 44.06 ?  29  LYS   A HD3  1 
ATOM   795  H HE2  . LYS   A 1 29  ? 13.074 -0.291  22.081  1.00 46.54 ?  29  LYS   A HE2  1 
ATOM   796  H HE3  . LYS   A 1 29  ? 14.391 -0.606  22.915  1.00 46.54 ?  29  LYS   A HE3  1 
ATOM   797  H HZ1  . LYS   A 1 29  ? 12.971 0.688   24.129  1.00 47.98 ?  29  LYS   A HZ1  1 
ATOM   798  H HZ2  . LYS   A 1 29  ? 14.183 1.443   23.883  1.00 47.98 ?  29  LYS   A HZ2  1 
ATOM   799  H HZ3  . LYS   A 1 29  ? 12.983 1.730   23.123  1.00 47.98 ?  29  LYS   A HZ3  1 
ATOM   800  N N    . VAL   A 1 30  ? 18.477 -1.235  18.927  1.00 25.08 ?  30  VAL   A N    1 
ATOM   801  C CA   . VAL   A 1 30  ? 19.119 -2.510  19.222  1.00 24.40 ?  30  VAL   A CA   1 
ATOM   802  C C    . VAL   A 1 30  ? 20.627 -2.370  19.397  1.00 23.70 ?  30  VAL   A C    1 
ATOM   803  O O    . VAL   A 1 30  ? 21.232 -3.122  20.167  1.00 24.12 ?  30  VAL   A O    1 
ATOM   804  C CB   . VAL   A 1 30  ? 18.788 -3.519  18.106  1.00 25.10 ?  30  VAL   A CB   1 
ATOM   805  C CG1  . VAL   A 1 30  ? 19.558 -4.819  18.299  1.00 25.92 ?  30  VAL   A CG1  1 
ATOM   806  C CG2  . VAL   A 1 30  ? 17.292 -3.783  18.053  1.00 25.45 ?  30  VAL   A CG2  1 
ATOM   807  H H    . VAL   A 1 30  ? 18.371 -1.079  18.086  1.00 30.13 ?  30  VAL   A H    1 
ATOM   808  H HA   . VAL   A 1 30  ? 18.748 -2.859  20.049  1.00 29.31 ?  30  VAL   A HA   1 
ATOM   809  H HB   . VAL   A 1 30  ? 19.052 -3.146  17.254  1.00 30.14 ?  30  VAL   A HB   1 
ATOM   810  H HG11 . VAL   A 1 30  ? 19.148 -5.511  17.754  1.00 31.14 ?  30  VAL   A HG11 1 
ATOM   811  H HG12 . VAL   A 1 30  ? 20.477 -4.686  18.027  1.00 31.14 ?  30  VAL   A HG12 1 
ATOM   812  H HG13 . VAL   A 1 30  ? 19.519 -5.073  19.234  1.00 31.14 ?  30  VAL   A HG13 1 
ATOM   813  H HG21 . VAL   A 1 30  ? 17.110 -4.450  17.370  1.00 30.56 ?  30  VAL   A HG21 1 
ATOM   814  H HG22 . VAL   A 1 30  ? 16.997 -4.114  18.919  1.00 30.56 ?  30  VAL   A HG22 1 
ATOM   815  H HG23 . VAL   A 1 30  ? 16.831 -2.959  17.841  1.00 30.56 ?  30  VAL   A HG23 1 
ATOM   816  N N    A LYS   A 1 31  ? 21.244 -1.416  18.709  0.60 23.14 ?  31  LYS   A N    1 
ATOM   817  N N    B LYS   A 1 31  ? 21.245 -1.416  18.710  0.40 23.52 ?  31  LYS   A N    1 
ATOM   818  C CA   A LYS   A 1 31  ? 22.696 -1.292  18.648  0.60 23.92 ?  31  LYS   A CA   1 
ATOM   819  C CA   B LYS   A 1 31  ? 22.696 -1.294  18.650  0.40 24.16 ?  31  LYS   A CA   1 
ATOM   820  C C    A LYS   A 1 31  ? 23.324 -2.644  18.297  0.60 21.39 ?  31  LYS   A C    1 
ATOM   821  C C    B LYS   A 1 31  ? 23.325 -2.645  18.298  0.40 21.80 ?  31  LYS   A C    1 
ATOM   822  O O    A LYS   A 1 31  ? 24.101 -3.199  19.081  0.60 22.07 ?  31  LYS   A O    1 
ATOM   823  O O    B LYS   A 1 31  ? 24.102 -3.200  19.080  0.40 22.36 ?  31  LYS   A O    1 
ATOM   824  C CB   A LYS   A 1 31  ? 23.274 -0.737  19.941  0.60 28.18 ?  31  LYS   A CB   1 
ATOM   825  C CB   B LYS   A 1 31  ? 23.274 -0.744  19.947  0.40 27.72 ?  31  LYS   A CB   1 
ATOM   826  C CG   A LYS   A 1 31  ? 22.581 0.526   20.439  0.60 32.48 ?  31  LYS   A CG   1 
ATOM   827  C CG   B LYS   A 1 31  ? 22.542 0.478   20.489  0.40 31.15 ?  31  LYS   A CG   1 
ATOM   828  C CD   A LYS   A 1 31  ? 23.581 1.613   20.809  0.60 35.88 ?  31  LYS   A CD   1 
ATOM   829  C CD   B LYS   A 1 31  ? 23.505 1.606   20.830  0.40 33.82 ?  31  LYS   A CD   1 
ATOM   830  C CE   A LYS   A 1 31  ? 22.956 2.663   21.718  0.60 38.23 ?  31  LYS   A CE   1 
ATOM   831  C CE   B LYS   A 1 31  ? 22.884 2.606   21.791  0.40 35.69 ?  31  LYS   A CE   1 
ATOM   832  N NZ   A LYS   A 1 31  ? 21.748 3.296   21.122  0.60 39.47 ?  31  LYS   A NZ   1 
ATOM   833  N NZ   B LYS   A 1 31  ? 21.539 3.085   21.363  0.40 36.63 ?  31  LYS   A NZ   1 
ATOM   834  H H    A LYS   A 1 31  ? 20.829 -0.813  18.259  0.60 27.79 ?  31  LYS   A H    1 
ATOM   835  H H    B LYS   A 1 31  ? 20.832 -0.811  18.260  0.40 28.26 ?  31  LYS   A H    1 
ATOM   836  H HA   A LYS   A 1 31  ? 22.913 -0.668  17.943  0.60 28.73 ?  31  LYS   A HA   1 
ATOM   837  H HA   B LYS   A 1 31  ? 22.919 -0.669  17.950  0.40 29.02 ?  31  LYS   A HA   1 
ATOM   838  H HB2  A LYS   A 1 31  ? 23.199 -1.409  20.633  0.60 33.84 ?  31  LYS   A HB2  1 
ATOM   839  H HB2  B LYS   A 1 31  ? 23.235 -1.435  20.619  0.40 33.29 ?  31  LYS   A HB2  1 
ATOM   840  H HB3  A LYS   A 1 31  ? 24.209 -0.520  19.793  0.60 33.84 ?  31  LYS   A HB3  1 
ATOM   841  H HB3  B LYS   A 1 31  ? 24.199 -0.491  19.791  0.40 33.29 ?  31  LYS   A HB3  1 
ATOM   842  H HG2  A LYS   A 1 31  ? 22.004 0.872   19.740  0.60 39.00 ?  31  LYS   A HG2  1 
ATOM   843  H HG2  B LYS   A 1 31  ? 21.922 0.804   19.818  0.40 37.41 ?  31  LYS   A HG2  1 
ATOM   844  H HG3  A LYS   A 1 31  ? 22.060 0.314   21.229  0.60 39.00 ?  31  LYS   A HG3  1 
ATOM   845  H HG3  B LYS   A 1 31  ? 22.064 0.232   21.296  0.40 37.41 ?  31  LYS   A HG3  1 
ATOM   846  H HD2  A LYS   A 1 31  ? 24.331 1.215   21.277  0.60 43.08 ?  31  LYS   A HD2  1 
ATOM   847  H HD2  B LYS   A 1 31  ? 24.298 1.236   21.249  0.40 40.61 ?  31  LYS   A HD2  1 
ATOM   848  H HD3  A LYS   A 1 31  ? 23.887 2.055   20.000  0.60 43.08 ?  31  LYS   A HD3  1 
ATOM   849  H HD3  B LYS   A 1 31  ? 23.743 2.081   20.019  0.40 40.61 ?  31  LYS   A HD3  1 
ATOM   850  H HE2  A LYS   A 1 31  ? 22.694 2.242   22.552  0.60 45.90 ?  31  LYS   A HE2  1 
ATOM   851  H HE2  B LYS   A 1 31  ? 22.808 2.203   22.664  0.40 42.85 ?  31  LYS   A HE2  1 
ATOM   852  H HE3  A LYS   A 1 31  ? 23.607 3.362   21.889  0.60 45.90 ?  31  LYS   A HE3  1 
ATOM   853  H HE3  B LYS   A 1 31  ? 23.460 3.376   21.853  0.40 42.85 ?  31  LYS   A HE3  1 
ATOM   854  H HZ1  A LYS   A 1 31  ? 21.420 3.909   21.678  0.60 47.40 ?  31  LYS   A HZ1  1 
ATOM   855  H HZ1  B LYS   A 1 31  ? 21.229 3.685   21.944  0.40 43.98 ?  31  LYS   A HZ1  1 
ATOM   856  H HZ2  A LYS   A 1 31  ? 21.958 3.687   20.351  0.60 47.40 ?  31  LYS   A HZ2  1 
ATOM   857  H HZ2  B LYS   A 1 31  ? 21.600 3.465   20.561  0.40 43.98 ?  31  LYS   A HZ2  1 
ATOM   858  H HZ3  A LYS   A 1 31  ? 21.123 2.679   20.972  0.60 47.40 ?  31  LYS   A HZ3  1 
ATOM   859  H HZ3  B LYS   A 1 31  ? 20.968 2.405   21.320  0.40 43.98 ?  31  LYS   A HZ3  1 
ATOM   860  N N    . PRO   A 1 32  ? 23.005 -3.194  17.130  1.00 19.46 ?  32  PRO   A N    1 
ATOM   861  C CA   . PRO   A 1 32  ? 23.483 -4.533  16.789  1.00 19.19 ?  32  PRO   A CA   1 
ATOM   862  C C    . PRO   A 1 32  ? 24.979 -4.538  16.550  1.00 19.05 ?  32  PRO   A C    1 
ATOM   863  O O    . PRO   A 1 32  ? 25.610 -3.501  16.333  1.00 19.10 ?  32  PRO   A O    1 
ATOM   864  C CB   . PRO   A 1 32  ? 22.731 -4.840  15.491  1.00 19.07 ?  32  PRO   A CB   1 
ATOM   865  C CG   . PRO   A 1 32  ? 22.557 -3.495  14.858  1.00 18.10 ?  32  PRO   A CG   1 
ATOM   866  C CD   . PRO   A 1 32  ? 22.298 -2.560  16.007  1.00 17.90 ?  32  PRO   A CD   1 
ATOM   867  H HA   . PRO   A 1 32  ? 23.248 -5.170  17.478  1.00 23.06 ?  32  PRO   A HA   1 
ATOM   868  H HB2  . PRO   A 1 32  ? 23.263 -5.432  14.932  1.00 22.92 ?  32  PRO   A HB2  1 
ATOM   869  H HB3  . PRO   A 1 32  ? 21.870 -5.249  15.698  1.00 22.92 ?  32  PRO   A HB3  1 
ATOM   870  H HG2  . PRO   A 1 32  ? 23.365 -3.264  14.381  1.00 21.74 ?  32  PRO   A HG2  1 
ATOM   871  H HG3  . PRO   A 1 32  ? 21.796 -3.529  14.251  1.00 21.74 ?  32  PRO   A HG3  1 
ATOM   872  H HD2  . PRO   A 1 32  ? 22.677 -1.689  15.800  1.00 21.51 ?  32  PRO   A HD2  1 
ATOM   873  H HD3  . PRO   A 1 32  ? 21.351 -2.507  16.182  1.00 21.51 ?  32  PRO   A HD3  1 
ATOM   874  N N    . THR   A 1 33  ? 25.541 -5.746  16.573  1.00 19.22 ?  33  THR   A N    1 
ATOM   875  C CA   . THR   A 1 33  ? 26.950 -5.905  16.245  1.00 19.06 ?  33  THR   A CA   1 
ATOM   876  C C    . THR   A 1 33  ? 27.236 -5.437  14.825  1.00 17.19 ?  33  THR   A C    1 
ATOM   877  O O    . THR   A 1 33  ? 28.266 -4.795  14.571  1.00 17.52 ?  33  THR   A O    1 
ATOM   878  C CB   . THR   A 1 33  ? 27.357 -7.367  16.426  1.00 20.78 ?  33  THR   A CB   1 
ATOM   879  O OG1  . THR   A 1 33  ? 27.066 -7.782  17.765  1.00 22.37 ?  33  THR   A OG1  1 
ATOM   880  C CG2  . THR   A 1 33  ? 28.840 -7.548  16.156  1.00 21.25 ?  33  THR   A CG2  1 
ATOM   881  H H    . THR   A 1 33  ? 25.130 -6.478  16.761  1.00 23.09 ?  33  THR   A H    1 
ATOM   882  H HA   . THR   A 1 33  ? 27.482 -5.369  16.851  1.00 22.91 ?  33  THR   A HA   1 
ATOM   883  H HB   . THR   A 1 33  ? 26.861 -7.923  15.800  1.00 24.97 ?  33  THR   A HB   1 
ATOM   884  H HG1  . THR   A 1 33  ? 27.493 -7.308  18.313  1.00 26.87 ?  33  THR   A HG1  1 
ATOM   885  H HG21 . THR   A 1 33  ? 29.120 -8.432  16.442  1.00 25.53 ?  33  THR   A HG21 1 
ATOM   886  H HG22 . THR   A 1 33  ? 29.021 -7.453  15.208  1.00 25.53 ?  33  THR   A HG22 1 
ATOM   887  H HG23 . THR   A 1 33  ? 29.346 -6.883  16.646  1.00 25.53 ?  33  THR   A HG23 1 
ATOM   888  N N    . VAL   A 1 34  ? 26.335 -5.742  13.889  1.00 15.71 ?  34  VAL   A N    1 
ATOM   889  C CA   . VAL   A 1 34  ? 26.519 -5.415  12.479  1.00 13.87 ?  34  VAL   A CA   1 
ATOM   890  C C    . VAL   A 1 34  ? 25.215 -4.858  11.918  1.00 13.54 ?  34  VAL   A C    1 
ATOM   891  O O    . VAL   A 1 34  ? 24.176 -5.530  11.963  1.00 14.59 ?  34  VAL   A O    1 
ATOM   892  C CB   . VAL   A 1 34  ? 26.958 -6.632  11.643  1.00 14.79 ?  34  VAL   A CB   1 
ATOM   893  C CG1  . VAL   A 1 34  ? 27.146 -6.239  10.185  1.00 15.54 ?  34  VAL   A CG1  1 
ATOM   894  C CG2  . VAL   A 1 34  ? 28.232 -7.263  12.206  1.00 16.22 ?  34  VAL   A CG2  1 
ATOM   895  H H    . VAL   A 1 34  ? 25.592 -6.144  14.051  1.00 18.88 ?  34  VAL   A H    1 
ATOM   896  H HA   . VAL   A 1 34  ? 27.200 -4.726  12.392  1.00 16.67 ?  34  VAL   A HA   1 
ATOM   897  H HB   . VAL   A 1 34  ? 26.254 -7.299  11.679  1.00 17.77 ?  34  VAL   A HB   1 
ATOM   898  H HG11 . VAL   A 1 34  ? 27.619 -6.954  9.729   1.00 18.68 ?  34  VAL   A HG11 1 
ATOM   899  H HG12 . VAL   A 1 34  ? 26.280 -6.103  9.776   1.00 18.68 ?  34  VAL   A HG12 1 
ATOM   900  H HG13 . VAL   A 1 34  ? 27.668 -5.422  10.145  1.00 18.68 ?  34  VAL   A HG13 1 
ATOM   901  H HG21 . VAL   A 1 34  ? 28.498 -7.999  11.631  1.00 19.49 ?  34  VAL   A HG21 1 
ATOM   902  H HG22 . VAL   A 1 34  ? 28.929 -6.595  12.238  1.00 19.49 ?  34  VAL   A HG22 1 
ATOM   903  H HG23 . VAL   A 1 34  ? 28.047 -7.597  13.100  1.00 19.49 ?  34  VAL   A HG23 1 
ATOM   904  N N    . VAL   A 1 35  ? 25.271 -3.642  11.380  1.00 12.90 ?  35  VAL   A N    1 
ATOM   905  C CA   . VAL   A 1 35  ? 24.239 -3.126  10.491  1.00 12.39 ?  35  VAL   A CA   1 
ATOM   906  C C    . VAL   A 1 35  ? 24.786 -3.126  9.069   1.00 11.77 ?  35  VAL   A C    1 
ATOM   907  O O    . VAL   A 1 35  ? 25.932 -2.720  8.834   1.00 12.29 ?  35  VAL   A O    1 
ATOM   908  C CB   . VAL   A 1 35  ? 23.715 -1.735  10.908  1.00 13.42 ?  35  VAL   A CB   1 
ATOM   909  C CG1  . VAL   A 1 35  ? 24.791 -0.653  10.785  1.00 14.19 ?  35  VAL   A CG1  1 
ATOM   910  C CG2  . VAL   A 1 35  ? 22.472 -1.374  10.093  1.00 13.68 ?  35  VAL   A CG2  1 
ATOM   911  H H    . VAL   A 1 35  ? 25.902 -3.080  11.519  1.00 15.51 ?  35  VAL   A H    1 
ATOM   912  H HA   . VAL   A 1 35  ? 23.477 -3.737  10.509  1.00 14.90 ?  35  VAL   A HA   1 
ATOM   913  H HB   . VAL   A 1 35  ? 23.440 -1.774  11.836  1.00 16.13 ?  35  VAL   A HB   1 
ATOM   914  H HG11 . VAL   A 1 35  ? 24.451 0.176   11.160  1.00 17.06 ?  35  VAL   A HG11 1 
ATOM   915  H HG12 . VAL   A 1 35  ? 25.578 -0.938  11.272  1.00 17.06 ?  35  VAL   A HG12 1 
ATOM   916  H HG13 . VAL   A 1 35  ? 25.009 -0.525  9.848   1.00 17.06 ?  35  VAL   A HG13 1 
ATOM   917  H HG21 . VAL   A 1 35  ? 22.123 -0.527  10.408  1.00 16.44 ?  35  VAL   A HG21 1 
ATOM   918  H HG22 . VAL   A 1 35  ? 22.720 -1.301  9.156   1.00 16.44 ?  35  VAL   A HG22 1 
ATOM   919  H HG23 . VAL   A 1 35  ? 21.807 -2.070  10.205  1.00 16.44 ?  35  VAL   A HG23 1 
ATOM   920  N N    . VAL   A 1 36  ? 23.966 -3.581  8.121   1.00 11.09 ?  36  VAL   A N    1 
ATOM   921  C CA   . VAL   A 1 36  ? 24.330 -3.600  6.714   1.00 10.88 ?  36  VAL   A CA   1 
ATOM   922  C C    . VAL   A 1 36  ? 23.869 -2.312  6.047   1.00 11.37 ?  36  VAL   A C    1 
ATOM   923  O O    . VAL   A 1 36  ? 22.711 -1.898  6.193   1.00 11.78 ?  36  VAL   A O    1 
ATOM   924  C CB   . VAL   A 1 36  ? 23.720 -4.817  6.004   1.00 10.76 ?  36  VAL   A CB   1 
ATOM   925  C CG1  . VAL   A 1 36  ? 23.971 -4.746  4.525   1.00 11.50 ?  36  VAL   A CG1  1 
ATOM   926  C CG2  . VAL   A 1 36  ? 24.264 -6.112  6.588   1.00 11.90 ?  36  VAL   A CG2  1 
ATOM   927  H H    . VAL   A 1 36  ? 23.173 -3.890  8.275   1.00 13.34 ?  36  VAL   A H    1 
ATOM   928  H HA   . VAL   A 1 36  ? 25.297 -3.660  6.633   1.00 13.09 ?  36  VAL   A HA   1 
ATOM   929  H HB   . VAL   A 1 36  ? 22.757 -4.806  6.142   1.00 12.95 ?  36  VAL   A HB   1 
ATOM   930  H HG11 . VAL   A 1 36  ? 23.837 -5.627  4.139   1.00 13.83 ?  36  VAL   A HG11 1 
ATOM   931  H HG12 . VAL   A 1 36  ? 23.355 -4.115  4.120   1.00 13.83 ?  36  VAL   A HG12 1 
ATOM   932  H HG13 . VAL   A 1 36  ? 24.887 -4.459  4.373   1.00 13.83 ?  36  VAL   A HG13 1 
ATOM   933  H HG21 . VAL   A 1 36  ? 23.869 -6.866  6.121   1.00 14.31 ?  36  VAL   A HG21 1 
ATOM   934  H HG22 . VAL   A 1 36  ? 25.228 -6.129  6.485   1.00 14.31 ?  36  VAL   A HG22 1 
ATOM   935  H HG23 . VAL   A 1 36  ? 24.035 -6.159  7.533   1.00 14.31 ?  36  VAL   A HG23 1 
ATOM   936  N N    . ASN   A 1 37  ? 24.785 -1.685  5.309   1.00 10.67 ?  37  ASN   A N    1 
ATOM   937  C CA   . ASN   A 1 37  ? 24.460 -0.566  4.440   1.00 10.63 ?  37  ASN   A CA   1 
ATOM   938  C C    . ASN   A 1 37  ? 24.325 -1.044  3.002   1.00 10.49 ?  37  ASN   A C    1 
ATOM   939  O O    . ASN   A 1 37  ? 25.114 -1.871  2.530   1.00 10.88 ?  37  ASN   A O    1 
ATOM   940  C CB   . ASN   A 1 37  ? 25.540 0.515   4.508   1.00 11.19 ?  37  ASN   A CB   1 
ATOM   941  C CG   . ASN   A 1 37  ? 25.207 1.709   3.652   1.00 11.38 ?  37  ASN   A CG   1 
ATOM   942  O OD1  . ASN   A 1 37  ? 24.033 2.044   3.467   1.00 11.51 ?  37  ASN   A OD1  1 
ATOM   943  N ND2  . ASN   A 1 37  ? 26.236 2.364   3.124   1.00 11.87 ?  37  ASN   A ND2  1 
ATOM   944  H H    . ASN   A 1 37  ? 25.623 -1.884  5.311   1.00 12.83 ?  37  ASN   A H    1 
ATOM   945  H HA   . ASN   A 1 37  ? 23.622 -0.167  4.718   1.00 12.79 ?  37  ASN   A HA   1 
ATOM   946  H HB2  . ASN   A 1 37  ? 25.633 0.820   5.426   1.00 13.46 ?  37  ASN   A HB2  1 
ATOM   947  H HB3  . ASN   A 1 37  ? 26.384 0.145   4.197   1.00 13.46 ?  37  ASN   A HB3  1 
ATOM   948  H HD21 . ASN   A 1 37  ? 26.095 3.056   2.626   1.00 14.28 ?  37  ASN   A HD21 1 
ATOM   949  H HD22 . ASN   A 1 37  ? 27.038 2.111   3.271   1.00 14.28 ?  37  ASN   A HD22 1 
ATOM   950  N N    . ALA   A 1 38  ? 23.303 -0.531  2.317   1.00 10.67 ?  38  ALA   A N    1 
ATOM   951  C CA   . ALA   A 1 38  ? 23.126 -0.712  0.880   1.00 10.86 ?  38  ALA   A CA   1 
ATOM   952  C C    . ALA   A 1 38  ? 23.999 0.309   0.147   1.00 11.49 ?  38  ALA   A C    1 
ATOM   953  O O    . ALA   A 1 38  ? 23.553 1.389   -0.261  1.00 11.46 ?  38  ALA   A O    1 
ATOM   954  C CB   . ALA   A 1 38  ? 21.655 -0.560  0.511   1.00 12.74 ?  38  ALA   A CB   1 
ATOM   955  H H    . ALA   A 1 38  ? 22.692 -0.050  2.681   1.00 12.83 ?  38  ALA   A H    1 
ATOM   956  H HA   . ALA   A 1 38  ? 23.417 -1.604  0.629   1.00 13.06 ?  38  ALA   A HA   1 
ATOM   957  H HB1  . ALA   A 1 38  ? 21.561 -0.632  -0.449  1.00 15.32 ?  38  ALA   A HB1  1 
ATOM   958  H HB2  . ALA   A 1 38  ? 21.143 -1.262  0.949   1.00 15.32 ?  38  ALA   A HB2  1 
ATOM   959  H HB3  . ALA   A 1 38  ? 21.343 0.309   0.809   1.00 15.32 ?  38  ALA   A HB3  1 
ATOM   960  N N    . ALA   A 1 39  ? 25.275 -0.041  -0.011  1.00 11.31 ?  39  ALA   A N    1 
ATOM   961  C CA   . ALA   A 1 39  ? 26.297 0.870   -0.495  1.00 11.56 ?  39  ALA   A CA   1 
ATOM   962  C C    . ALA   A 1 39  ? 26.418 0.818   -2.013  1.00 11.11 ?  39  ALA   A C    1 
ATOM   963  O O    . ALA   A 1 39  ? 25.948 -0.111  -2.677  1.00 11.59 ?  39  ALA   A O    1 
ATOM   964  C CB   . ALA   A 1 39  ? 27.635 0.513   0.158   1.00 12.23 ?  39  ALA   A CB   1 
ATOM   965  H H    . ALA   A 1 39  ? 25.574 -0.830  0.173   1.00 13.59 ?  39  ALA   A H    1 
ATOM   966  H HA   . ALA   A 1 39  ? 26.058 1.775   -0.230  1.00 13.90 ?  39  ALA   A HA   1 
ATOM   967  H HB1  . ALA   A 1 39  ? 28.312 1.125   -0.164  1.00 14.70 ?  39  ALA   A HB1  1 
ATOM   968  H HB2  . ALA   A 1 39  ? 27.549 0.595   1.125   1.00 14.70 ?  39  ALA   A HB2  1 
ATOM   969  H HB3  . ALA   A 1 39  ? 27.867 -0.397  -0.075  1.00 14.70 ?  39  ALA   A HB3  1 
ATOM   970  N N    . ASN   A 1 40  ? 27.103 1.824   -2.561  1.00 11.76 ?  40  ASN   A N    1 
ATOM   971  C CA   . ASN   A 1 40  ? 27.634 1.781   -3.918  1.00 11.88 ?  40  ASN   A CA   1 
ATOM   972  C C    . ASN   A 1 40  ? 29.160 1.661   -3.860  1.00 11.49 ?  40  ASN   A C    1 
ATOM   973  O O    . ASN   A 1 40  ? 29.762 1.751   -2.787  1.00 11.52 ?  40  ASN   A O    1 
ATOM   974  C CB   . ASN   A 1 40  ? 27.159 2.978   -4.759  1.00 12.60 ?  40  ASN   A CB   1 
ATOM   975  C CG   . ASN   A 1 40  ? 27.535 4.312   -4.157  1.00 13.86 ?  40  ASN   A CG   1 
ATOM   976  O OD1  . ASN   A 1 40  ? 28.709 4.569   -3.876  1.00 14.25 ?  40  ASN   A OD1  1 
ATOM   977  N ND2  . ASN   A 1 40  ? 26.532 5.176   -3.960  1.00 14.80 ?  40  ASN   A ND2  1 
ATOM   978  H H    . ASN   A 1 40  ? 27.292 2.549   -2.145  1.00 14.14 ?  40  ASN   A H    1 
ATOM   979  H HA   . ASN   A 1 40  ? 27.306 0.977   -4.349  1.00 14.28 ?  40  ASN   A HA   1 
ATOM   980  H HB2  . ASN   A 1 40  ? 27.566 2.922   -5.640  1.00 15.15 ?  40  ASN   A HB2  1 
ATOM   981  H HB3  . ASN   A 1 40  ? 26.196 2.941   -4.837  1.00 15.15 ?  40  ASN   A HB3  1 
ATOM   982  H HD21 . ASN   A 1 40  ? 26.691 5.953   -3.623  1.00 17.79 ?  40  ASN   A HD21 1 
ATOM   983  H HD22 . ASN   A 1 40  ? 25.727 4.955   -4.165  1.00 17.79 ?  40  ASN   A HD22 1 
ATOM   984  N N    . VAL   A 1 41  ? 29.776 1.410   -5.019  1.00 12.21 ?  41  VAL   A N    1 
ATOM   985  C CA   . VAL   A 1 41  ? 31.206 1.096   -5.049  1.00 12.77 ?  41  VAL   A CA   1 
ATOM   986  C C    . VAL   A 1 41  ? 32.067 2.243   -4.560  1.00 12.82 ?  41  VAL   A C    1 
ATOM   987  O O    . VAL   A 1 41  ? 33.204 2.017   -4.135  1.00 12.98 ?  41  VAL   A O    1 
ATOM   988  C CB   . VAL   A 1 41  ? 31.692 0.622   -6.440  1.00 13.36 ?  41  VAL   A CB   1 
ATOM   989  C CG1  . VAL   A 1 41  ? 31.002 -0.673  -6.844  1.00 14.34 ?  41  VAL   A CG1  1 
ATOM   990  C CG2  . VAL   A 1 41  ? 31.523 1.703   -7.498  1.00 14.35 ?  41  VAL   A CG2  1 
ATOM   991  H H    . VAL   A 1 41  ? 29.392 1.409   -5.790  1.00 14.68 ?  41  VAL   A H    1 
ATOM   992  H HA   . VAL   A 1 41  ? 31.358 0.352   -4.442  1.00 15.35 ?  41  VAL   A HA   1 
ATOM   993  H HB   . VAL   A 1 41  ? 32.639 0.428   -6.382  1.00 16.06 ?  41  VAL   A HB   1 
ATOM   994  H HG11 . VAL   A 1 41  ? 31.337 -0.954  -7.712  1.00 17.24 ?  41  VAL   A HG11 1 
ATOM   995  H HG12 . VAL   A 1 41  ? 31.197 -1.354  -6.180  1.00 17.24 ?  41  VAL   A HG12 1 
ATOM   996  H HG13 . VAL   A 1 41  ? 30.046 -0.522  -6.893  1.00 17.24 ?  41  VAL   A HG13 1 
ATOM   997  H HG21 . VAL   A 1 41  ? 31.751 1.337   -8.368  1.00 17.25 ?  41  VAL   A HG21 1 
ATOM   998  H HG22 . VAL   A 1 41  ? 30.604 2.008   -7.499  1.00 17.25 ?  41  VAL   A HG22 1 
ATOM   999  H HG23 . VAL   A 1 41  ? 32.117 2.444   -7.290  1.00 17.25 ?  41  VAL   A HG23 1 
ATOM   1000 N N    . TYR   A 1 42  ? 31.562 3.478   -4.632  1.00 12.36 ?  42  TYR   A N    1 
ATOM   1001 C CA   . TYR   A 1 42  ? 32.301 4.663   -4.215  1.00 12.30 ?  42  TYR   A CA   1 
ATOM   1002 C C    . TYR   A 1 42  ? 32.045 5.039   -2.765  1.00 12.38 ?  42  TYR   A C    1 
ATOM   1003 O O    . TYR   A 1 42  ? 32.612 6.031   -2.283  1.00 12.63 ?  42  TYR   A O    1 
ATOM   1004 C CB   . TYR   A 1 42  ? 31.962 5.849   -5.138  1.00 12.55 ?  42  TYR   A CB   1 
ATOM   1005 C CG   . TYR   A 1 42  ? 32.160 5.538   -6.604  1.00 13.44 ?  42  TYR   A CG   1 
ATOM   1006 C CD1  . TYR   A 1 42  ? 33.424 5.321   -7.125  1.00 14.54 ?  42  TYR   A CD1  1 
ATOM   1007 C CD2  . TYR   A 1 42  ? 31.074 5.419   -7.464  1.00 15.40 ?  42  TYR   A CD2  1 
ATOM   1008 C CE1  . TYR   A 1 42  ? 33.605 5.013   -8.466  1.00 15.25 ?  42  TYR   A CE1  1 
ATOM   1009 C CE2  . TYR   A 1 42  ? 31.250 5.120   -8.803  1.00 16.17 ?  42  TYR   A CE2  1 
ATOM   1010 C CZ   . TYR   A 1 42  ? 32.519 4.920   -9.300  1.00 16.32 ?  42  TYR   A CZ   1 
ATOM   1011 O OH   . TYR   A 1 42  ? 32.691 4.615   -10.629 1.00 18.20 ?  42  TYR   A OH   1 
ATOM   1012 H H    . TYR   A 1 42  ? 30.771 3.651   -4.929  1.00 14.86 ?  42  TYR   A H    1 
ATOM   1013 H HA   . TYR   A 1 42  ? 33.245 4.491   -4.311  1.00 14.79 ?  42  TYR   A HA   1 
ATOM   1014 H HB2  . TYR   A 1 42  ? 31.027 6.099   -5.008  1.00 15.09 ?  42  TYR   A HB2  1 
ATOM   1015 H HB3  . TYR   A 1 42  ? 32.531 6.603   -4.912  1.00 15.09 ?  42  TYR   A HB3  1 
ATOM   1016 H HD1  . TYR   A 1 42  ? 34.167 5.382   -6.566  1.00 17.48 ?  42  TYR   A HD1  1 
ATOM   1017 H HD2  . TYR   A 1 42  ? 30.215 5.567   -7.135  1.00 18.51 ?  42  TYR   A HD2  1 
ATOM   1018 H HE1  . TYR   A 1 42  ? 34.464 4.875   -8.800  1.00 18.33 ?  42  TYR   A HE1  1 
ATOM   1019 H HE2  . TYR   A 1 42  ? 30.514 5.060   -9.371  1.00 19.43 ?  42  TYR   A HE2  1 
ATOM   1020 H HH   . TYR   A 1 42  ? 33.511 4.507   -10.795 1.00 21.87 ?  42  TYR   A HH   1 
ATOM   1021 N N    . LEU   A 1 43  ? 31.182 4.286   -2.077  1.00 12.25 ?  43  LEU   A N    1 
ATOM   1022 C CA   . LEU   A 1 43  ? 30.746 4.617   -0.723  1.00 11.71 ?  43  LEU   A CA   1 
ATOM   1023 C C    . LEU   A 1 43  ? 30.267 6.067   -0.627  1.00 11.99 ?  43  LEU   A C    1 
ATOM   1024 O O    . LEU   A 1 43  ? 30.539 6.772   0.348   1.00 12.81 ?  43  LEU   A O    1 
ATOM   1025 C CB   . LEU   A 1 43  ? 31.802 4.307   0.335   1.00 12.20 ?  43  LEU   A CB   1 
ATOM   1026 C CG   . LEU   A 1 43  ? 32.300 2.855   0.412   1.00 12.31 ?  43  LEU   A CG   1 
ATOM   1027 C CD1  . LEU   A 1 43  ? 33.339 2.748   1.517   1.00 13.31 ?  43  LEU   A CD1  1 
ATOM   1028 C CD2  . LEU   A 1 43  ? 31.159 1.871   0.638   1.00 13.10 ?  43  LEU   A CD2  1 
ATOM   1029 H H    . LEU   A 1 43  ? 30.834 3.547   -2.371  1.00 14.73 ?  43  LEU   A H    1 
ATOM   1030 H HA   . LEU   A 1 43  ? 29.977 4.059   -0.513  1.00 14.08 ?  43  LEU   A HA   1 
ATOM   1031 H HB2  . LEU   A 1 43  ? 32.572 4.872   0.168   1.00 14.67 ?  43  LEU   A HB2  1 
ATOM   1032 H HB3  . LEU   A 1 43  ? 31.429 4.528   1.206   1.00 14.67 ?  43  LEU   A HB3  1 
ATOM   1033 H HG   . LEU   A 1 43  ? 32.736 2.628   -0.423  1.00 14.80 ?  43  LEU   A HG   1 
ATOM   1034 H HD11 . LEU   A 1 43  ? 33.656 1.833   1.567   1.00 16.00 ?  43  LEU   A HD11 1 
ATOM   1035 H HD12 . LEU   A 1 43  ? 34.079 3.345   1.317   1.00 16.00 ?  43  LEU   A HD12 1 
ATOM   1036 H HD13 . LEU   A 1 43  ? 32.931 3.002   2.361   1.00 16.00 ?  43  LEU   A HD13 1 
ATOM   1037 H HD21 . LEU   A 1 43  ? 31.531 0.987   0.777   1.00 15.74 ?  43  LEU   A HD21 1 
ATOM   1038 H HD22 . LEU   A 1 43  ? 30.657 2.148   1.418   1.00 15.74 ?  43  LEU   A HD22 1 
ATOM   1039 H HD23 . LEU   A 1 43  ? 30.588 1.873   -0.145  1.00 15.74 ?  43  LEU   A HD23 1 
ATOM   1040 N N    . LYS   A 1 44  ? 29.531 6.509   -1.650  1.00 12.15 ?  44  LYS   A N    1 
ATOM   1041 C CA   . LYS   A 1 44  ? 28.890 7.822   -1.648  1.00 12.68 ?  44  LYS   A CA   1 
ATOM   1042 C C    . LYS   A 1 44  ? 27.471 7.621   -1.139  1.00 11.87 ?  44  LYS   A C    1 
ATOM   1043 O O    . LYS   A 1 44  ? 26.605 7.102   -1.851  1.00 12.93 ?  44  LYS   A O    1 
ATOM   1044 C CB   . LYS   A 1 44  ? 28.914 8.437   -3.040  1.00 14.51 ?  44  LYS   A CB   1 
ATOM   1045 C CG   . LYS   A 1 44  ? 30.288 8.912   -3.478  1.00 17.72 ?  44  LYS   A CG   1 
ATOM   1046 C CD   . LYS   A 1 44  ? 30.959 9.788   -2.422  1.00 22.71 ?  44  LYS   A CD   1 
ATOM   1047 C CE   . LYS   A 1 44  ? 32.270 10.357  -2.925  1.00 25.80 ?  44  LYS   A CE   1 
ATOM   1048 N NZ   . LYS   A 1 44  ? 33.144 10.814  -1.811  1.00 26.77 ?  44  LYS   A NZ   1 
ATOM   1049 H H    . LYS   A 1 44  ? 29.386 6.055   -2.368  1.00 14.61 ?  44  LYS   A H    1 
ATOM   1050 H HA   . LYS   A 1 44  ? 29.339 8.403   -1.019  1.00 15.24 ?  44  LYS   A HA   1 
ATOM   1051 H HB2  . LYS   A 1 44  ? 28.614 7.776   -3.684  1.00 17.44 ?  44  LYS   A HB2  1 
ATOM   1052 H HB3  . LYS   A 1 44  ? 28.320 9.204   -3.056  1.00 17.44 ?  44  LYS   A HB3  1 
ATOM   1053 H HG2  . LYS   A 1 44  ? 30.855 8.144   -3.640  1.00 21.29 ?  44  LYS   A HG2  1 
ATOM   1054 H HG3  . LYS   A 1 44  ? 30.199 9.440   -4.289  1.00 21.29 ?  44  LYS   A HG3  1 
ATOM   1055 H HD2  . LYS   A 1 44  ? 30.365 10.518  -2.186  1.00 27.28 ?  44  LYS   A HD2  1 
ATOM   1056 H HD3  . LYS   A 1 44  ? 31.155 9.247   -1.637  1.00 27.28 ?  44  LYS   A HD3  1 
ATOM   1057 H HE2  . LYS   A 1 44  ? 32.744 9.669   -3.418  1.00 30.99 ?  44  LYS   A HE2  1 
ATOM   1058 H HE3  . LYS   A 1 44  ? 32.085 11.114  -3.498  1.00 30.99 ?  44  LYS   A HE3  1 
ATOM   1059 H HZ1  . LYS   A 1 44  ? 33.902 11.142  -2.137  1.00 32.15 ?  44  LYS   A HZ1  1 
ATOM   1060 H HZ2  . LYS   A 1 44  ? 32.730 11.449  -1.343  1.00 32.15 ?  44  LYS   A HZ2  1 
ATOM   1061 H HZ3  . LYS   A 1 44  ? 33.330 10.132  -1.270  1.00 32.15 ?  44  LYS   A HZ3  1 
ATOM   1062 N N    A HIS   A 1 45  ? 27.231 8.022   0.106   0.60 11.35 ?  45  HIS   A N    1 
ATOM   1063 N N    B HIS   A 1 45  ? 27.232 8.012   0.110   0.40 11.68 ?  45  HIS   A N    1 
ATOM   1064 C CA   A HIS   A 1 45  ? 26.004 7.657   0.815   0.60 11.37 ?  45  HIS   A CA   1 
ATOM   1065 C CA   B HIS   A 1 45  ? 25.975 7.711   0.796   0.40 11.89 ?  45  HIS   A CA   1 
ATOM   1066 C C    A HIS   A 1 45  ? 24.950 8.761   0.675   0.60 11.90 ?  45  HIS   A C    1 
ATOM   1067 C C    B HIS   A 1 45  ? 24.982 8.837   0.523   0.40 12.63 ?  45  HIS   A C    1 
ATOM   1068 O O    A HIS   A 1 45  ? 24.605 9.471   1.623   0.60 12.12 ?  45  HIS   A O    1 
ATOM   1069 O O    B HIS   A 1 45  ? 24.869 9.796   1.288   0.40 13.42 ?  45  HIS   A O    1 
ATOM   1070 C CB   A HIS   A 1 45  ? 26.321 7.373   2.273   0.60 11.14 ?  45  HIS   A CB   1 
ATOM   1071 C CB   B HIS   A 1 45  ? 26.233 7.529   2.284   0.40 11.50 ?  45  HIS   A CB   1 
ATOM   1072 C CG   A HIS   A 1 45  ? 27.440 6.399   2.463   0.60 10.48 ?  45  HIS   A CG   1 
ATOM   1073 C CG   B HIS   A 1 45  ? 27.357 6.585   2.587   0.40 11.28 ?  45  HIS   A CG   1 
ATOM   1074 N ND1  A HIS   A 1 45  ? 27.422 5.122   1.941   0.60 10.39 ?  45  HIS   A ND1  1 
ATOM   1075 N ND1  B HIS   A 1 45  ? 27.371 5.278   2.150   0.40 11.80 ?  45  HIS   A ND1  1 
ATOM   1076 C CD2  A HIS   A 1 45  ? 28.624 6.529   3.108   0.60 10.92 ?  45  HIS   A CD2  1 
ATOM   1077 C CD2  B HIS   A 1 45  ? 28.512 6.766   3.272   0.40 10.76 ?  45  HIS   A CD2  1 
ATOM   1078 C CE1  A HIS   A 1 45  ? 28.543 4.505   2.271   0.60 10.62 ?  45  HIS   A CE1  1 
ATOM   1079 C CE1  B HIS   A 1 45  ? 28.484 4.694   2.556   0.40 11.00 ?  45  HIS   A CE1  1 
ATOM   1080 N NE2  A HIS   A 1 45  ? 29.291 5.336   2.976   0.60 11.15 ?  45  HIS   A NE2  1 
ATOM   1081 N NE2  B HIS   A 1 45  ? 29.195 5.575   3.238   0.40 10.89 ?  45  HIS   A NE2  1 
ATOM   1082 H H    A HIS   A 1 45  ? 27.767 8.512   0.567   0.60 13.65 ?  45  HIS   A H    1 
ATOM   1083 H H    B HIS   A 1 45  ? 27.786 8.461   0.590   0.40 14.05 ?  45  HIS   A H    1 
ATOM   1084 H HA   A HIS   A 1 45  ? 25.641 6.848   0.424   0.60 13.67 ?  45  HIS   A HA   1 
ATOM   1085 H HA   B HIS   A 1 45  ? 25.604 6.886   0.447   0.40 14.30 ?  45  HIS   A HA   1 
ATOM   1086 H HB2  A HIS   A 1 45  ? 26.568 8.199   2.711   0.60 13.39 ?  45  HIS   A HB2  1 
ATOM   1087 H HB2  B HIS   A 1 45  ? 26.453 8.389   2.673   0.40 13.82 ?  45  HIS   A HB2  1 
ATOM   1088 H HB3  A HIS   A 1 45  ? 25.530 6.998   2.699   0.60 13.39 ?  45  HIS   A HB3  1 
ATOM   1089 H HB3  B HIS   A 1 45  ? 25.428 7.176   2.701   0.40 13.82 ?  45  HIS   A HB3  1 
ATOM   1090 H HD2  A HIS   A 1 45  ? 28.931 7.284   3.557   0.60 13.14 ?  45  HIS   A HD2  1 
ATOM   1091 H HD2  B HIS   A 1 45  ? 28.792 7.552   3.686   0.40 12.94 ?  45  HIS   A HD2  1 
ATOM   1092 H HE1  A HIS   A 1 45  ? 28.767 3.626   2.057   0.60 12.77 ?  45  HIS   A HE1  1 
ATOM   1093 H HE1  B HIS   A 1 45  ? 28.722 3.812   2.392   0.40 13.23 ?  45  HIS   A HE1  1 
ATOM   1094 H HE2  A HIS   A 1 45  ? 30.068 5.157   3.305   0.60 13.41 ?  45  HIS   A HE2  1 
ATOM   1095 H HE2  B HIS   A 1 45  ? 29.956 5.425   3.603   0.40 13.09 ?  45  HIS   A HE2  1 
ATOM   1096 N N    A GLY   A 1 46  ? 24.425 8.888   -0.540  0.60 12.39 ?  46  GLY   A N    1 
ATOM   1097 N N    B GLY   A 1 46  ? 24.245 8.716   -0.578  0.40 12.63 ?  46  GLY   A N    1 
ATOM   1098 C CA   A GLY   A 1 46  ? 23.595 10.035  -0.867  0.60 12.70 ?  46  GLY   A CA   1 
ATOM   1099 C CA   B GLY   A 1 46  ? 23.404 9.804   -1.043  0.40 13.02 ?  46  GLY   A CA   1 
ATOM   1100 C C    A GLY   A 1 46  ? 22.108 9.882   -0.605  0.60 13.33 ?  46  GLY   A C    1 
ATOM   1101 C C    B GLY   A 1 46  ? 21.944 9.723   -0.639  0.40 13.45 ?  46  GLY   A C    1 
ATOM   1102 O O    A GLY   A 1 46  ? 21.439 10.858  -0.243  0.60 14.99 ?  46  GLY   A O    1 
ATOM   1103 O O    B GLY   A 1 46  ? 21.332 10.749  -0.312  0.40 14.67 ?  46  GLY   A O    1 
ATOM   1104 H H    A GLY   A 1 46  ? 24.534 8.332   -1.188  0.60 14.89 ?  46  GLY   A H    1 
ATOM   1105 H H    B GLY   A 1 46  ? 24.219 8.010   -1.068  0.40 15.18 ?  46  GLY   A H    1 
ATOM   1106 H HA2  A GLY   A 1 46  ? 23.907 10.803  -0.358  0.60 15.26 ?  46  GLY   A HA2  1 
ATOM   1107 H HA2  B GLY   A 1 46  ? 23.754 10.641  -0.704  0.40 15.65 ?  46  GLY   A HA2  1 
ATOM   1108 H HA3  A GLY   A 1 46  ? 23.704 10.245  -1.808  0.60 15.26 ?  46  GLY   A HA3  1 
ATOM   1109 H HA3  B GLY   A 1 46  ? 23.449 9.835   -2.013  0.40 15.65 ?  46  GLY   A HA3  1 
ATOM   1110 N N    A GLY   A 1 47  ? 21.572 8.683   -0.810  0.60 13.03 ?  47  GLY   A N    1 
ATOM   1111 N N    B GLY   A 1 47  ? 21.365 8.528   -0.668  0.40 12.91 ?  47  GLY   A N    1 
ATOM   1112 C CA   A GLY   A 1 47  ? 20.138 8.474   -0.735  0.60 12.83 ?  47  GLY   A CA   1 
ATOM   1113 C CA   B GLY   A 1 47  ? 19.953 8.378   -0.392  0.40 12.34 ?  47  GLY   A CA   1 
ATOM   1114 C C    A GLY   A 1 47  ? 19.823 7.031   -0.410  0.60 11.91 ?  47  GLY   A C    1 
ATOM   1115 C C    B GLY   A 1 47  ? 19.628 6.978   0.082   0.40 10.94 ?  47  GLY   A C    1 
ATOM   1116 O O    A GLY   A 1 47  ? 20.716 6.202   -0.229  0.60 11.93 ?  47  GLY   A O    1 
ATOM   1117 O O    B GLY   A 1 47  ? 20.517 6.150   0.292   0.40 10.28 ?  47  GLY   A O    1 
ATOM   1118 H H    A GLY   A 1 47  ? 22.021 7.975   -0.984  0.60 15.67 ?  47  GLY   A H    1 
ATOM   1119 H H    B GLY   A 1 47  ? 21.771 7.786   -0.842  0.40 15.52 ?  47  GLY   A H    1 
ATOM   1120 H HA2  A GLY   A 1 47  ? 19.755 9.049   -0.051  0.60 15.43 ?  47  GLY   A HA2  1 
ATOM   1121 H HA2  B GLY   A 1 47  ? 19.685 8.997   0.300   0.40 14.84 ?  47  GLY   A HA2  1 
ATOM   1122 H HA3  A GLY   A 1 47  ? 19.734 8.686   -1.587  0.60 15.43 ?  47  GLY   A HA3  1 
ATOM   1123 H HA3  B GLY   A 1 47  ? 19.438 8.570   -1.197  0.40 14.84 ?  47  GLY   A HA3  1 
ATOM   1124 N N    A GLY   A 1 48  ? 18.531 6.726   -0.350  0.60 11.56 ?  48  GLY   A N    1 
ATOM   1125 N N    B GLY   A 1 48  ? 18.330 6.725   0.250   0.40 10.46 ?  48  GLY   A N    1 
ATOM   1126 C CA   A GLY   A 1 48  ? 18.121 5.398   0.046   0.60 11.03 ?  48  GLY   A CA   1 
ATOM   1127 C CA   B GLY   A 1 48  ? 17.888 5.419   0.706   0.40 9.90  ?  48  GLY   A CA   1 
ATOM   1128 C C    A GLY   A 1 48  ? 18.577 5.085   1.455   0.60 10.42 ?  48  GLY   A C    1 
ATOM   1129 C C    B GLY   A 1 48  ? 18.510 5.063   2.042   0.40 10.30 ?  48  GLY   A C    1 
ATOM   1130 O O    A GLY   A 1 48  ? 18.726 5.969   2.308   0.60 10.80 ?  48  GLY   A O    1 
ATOM   1131 O O    B GLY   A 1 48  ? 18.696 5.912   2.925   0.40 10.66 ?  48  GLY   A O    1 
ATOM   1132 H H    A GLY   A 1 48  ? 17.890 7.262   -0.522  0.60 13.90 ?  48  GLY   A H    1 
ATOM   1133 H H    B GLY   A 1 48  ? 17.686 7.289   0.104   0.40 12.58 ?  48  GLY   A H    1 
ATOM   1134 H HA2  A GLY   A 1 48  ? 17.159 5.321   0.006   0.60 13.27 ?  48  GLY   A HA2  1 
ATOM   1135 H HA2  B GLY   A 1 48  ? 16.914 5.410   0.791   0.40 11.91 ?  48  GLY   A HA2  1 
ATOM   1136 H HA3  A GLY   A 1 48  ? 18.516 4.740   -0.548  0.60 13.27 ?  48  GLY   A HA3  1 
ATOM   1137 H HA3  B GLY   A 1 48  ? 18.136 4.740   0.054   0.40 11.91 ?  48  GLY   A HA3  1 
ATOM   1138 N N    A VAL   A 1 49  ? 18.817 3.794   1.701   0.60 11.04 ?  49  VAL   A N    1 
ATOM   1139 N N    B VAL   A 1 49  ? 18.836 3.779   2.191   0.40 10.17 ?  49  VAL   A N    1 
ATOM   1140 C CA   A VAL   A 1 49  ? 19.318 3.362   3.003   0.60 11.52 ?  49  VAL   A CA   1 
ATOM   1141 C CA   B VAL   A 1 49  ? 19.457 3.291   3.419   0.40 10.63 ?  49  VAL   A CA   1 
ATOM   1142 C C    A VAL   A 1 49  ? 20.627 4.064   3.339   0.60 10.63 ?  49  VAL   A C    1 
ATOM   1143 C C    B VAL   A 1 49  ? 20.741 4.057   3.717   0.40 10.82 ?  49  VAL   A C    1 
ATOM   1144 O O    A VAL   A 1 49  ? 20.838 4.480   4.480   0.60 10.73 ?  49  VAL   A O    1 
ATOM   1145 O O    B VAL   A 1 49  ? 20.973 4.490   4.852   0.40 11.20 ?  49  VAL   A O    1 
ATOM   1146 C CB   A VAL   A 1 49  ? 19.489 1.831   3.032   0.60 12.68 ?  49  VAL   A CB   1 
ATOM   1147 C CB   B VAL   A 1 49  ? 19.719 1.779   3.309   0.40 11.22 ?  49  VAL   A CB   1 
ATOM   1148 C CG1  A VAL   A 1 49  ? 20.243 1.397   4.288   0.60 13.00 ?  49  VAL   A CG1  1 
ATOM   1149 C CG1  B VAL   A 1 49  ? 20.626 1.315   4.435   0.40 11.31 ?  49  VAL   A CG1  1 
ATOM   1150 C CG2  A VAL   A 1 49  ? 18.137 1.146   2.965   0.60 14.03 ?  49  VAL   A CG2  1 
ATOM   1151 C CG2  B VAL   A 1 49  ? 18.409 1.007   3.311   0.40 12.28 ?  49  VAL   A CG2  1 
ATOM   1152 H H    A VAL   A 1 49  ? 18.701 3.155   1.142   0.60 13.27 ?  49  VAL   A H    1 
ATOM   1153 H H    B VAL   A 1 49  ? 18.700 3.172   1.594   0.40 12.24 ?  49  VAL   A H    1 
ATOM   1154 H HA   A VAL   A 1 49  ? 18.673 3.595   3.689   0.60 13.85 ?  49  VAL   A HA   1 
ATOM   1155 H HA   B VAL   A 1 49  ? 18.851 3.435   4.157   0.40 12.78 ?  49  VAL   A HA   1 
ATOM   1156 H HB   A VAL   A 1 49  ? 20.011 1.550   2.265   0.60 15.25 ?  49  VAL   A HB   1 
ATOM   1157 H HB   B VAL   A 1 49  ? 20.168 1.595   2.467   0.40 13.49 ?  49  VAL   A HB   1 
ATOM   1158 H HG11 A VAL   A 1 49  ? 20.095 0.449   4.436   0.60 15.62 ?  49  VAL   A HG11 1 
ATOM   1159 H HG11 B VAL   A 1 49  ? 20.534 0.357   4.538   0.40 13.61 ?  49  VAL   A HG11 1 
ATOM   1160 H HG12 A VAL   A 1 49  ? 21.191 1.567   4.170   0.60 15.62 ?  49  VAL   A HG12 1 
ATOM   1161 H HG12 B VAL   A 1 49  ? 21.545 1.536   4.213   0.40 13.61 ?  49  VAL   A HG12 1 
ATOM   1162 H HG13 A VAL   A 1 49  ? 19.909 1.902   5.048   0.60 15.62 ?  49  VAL   A HG13 1 
ATOM   1163 H HG13 B VAL   A 1 49  ? 20.363 1.762   5.253   0.40 13.61 ?  49  VAL   A HG13 1 
ATOM   1164 H HG21 A VAL   A 1 49  ? 18.268 0.183   2.985   0.60 16.86 ?  49  VAL   A HG21 1 
ATOM   1165 H HG21 B VAL   A 1 49  ? 18.600 0.060   3.219   0.40 14.77 ?  49  VAL   A HG21 1 
ATOM   1166 H HG22 A VAL   A 1 49  ? 17.606 1.420   3.729   0.60 16.86 ?  49  VAL   A HG22 1 
ATOM   1167 H HG22 B VAL   A 1 49  ? 17.946 1.172   4.146   0.40 14.77 ?  49  VAL   A HG22 1 
ATOM   1168 H HG23 A VAL   A 1 49  ? 17.696 1.403   2.143   0.60 16.86 ?  49  VAL   A HG23 1 
ATOM   1169 H HG23 B VAL   A 1 49  ? 17.864 1.306   2.564   0.40 14.77 ?  49  VAL   A HG23 1 
ATOM   1170 N N    A ALA   A 1 50  ? 21.544 4.149   2.372   0.60 10.11 ?  50  ALA   A N    1 
ATOM   1171 N N    B ALA   A 1 50  ? 21.611 4.192   2.712   0.40 10.50 ?  50  ALA   A N    1 
ATOM   1172 C CA   A ALA   A 1 50  ? 22.867 4.708   2.639   0.60 10.48 ?  50  ALA   A CA   1 
ATOM   1173 C CA   B ALA   A 1 50  ? 22.918 4.802   2.943   0.40 10.16 ?  50  ALA   A CA   1 
ATOM   1174 C C    A ALA   A 1 50  ? 22.780 6.165   3.068   0.60 10.62 ?  50  ALA   A C    1 
ATOM   1175 C C    B ALA   A 1 50  ? 22.775 6.257   3.367   0.40 10.10 ?  50  ALA   A C    1 
ATOM   1176 O O    A ALA   A 1 50  ? 23.424 6.576   4.035   0.60 10.98 ?  50  ALA   A O    1 
ATOM   1177 O O    B ALA   A 1 50  ? 23.418 6.701   4.325   0.40 10.22 ?  50  ALA   A O    1 
ATOM   1178 C CB   A ALA   A 1 50  ? 23.744 4.582   1.397   0.60 11.03 ?  50  ALA   A CB   1 
ATOM   1179 C CB   B ALA   A 1 50  ? 23.790 4.678   1.692   0.40 10.29 ?  50  ALA   A CB   1 
ATOM   1180 H H    A ALA   A 1 50  ? 21.426 3.889   1.570   0.60 12.16 ?  50  ALA   A H    1 
ATOM   1181 H H    B ALA   A 1 50  ? 21.468 3.948   1.892   0.40 12.63 ?  50  ALA   A H    1 
ATOM   1182 H HA   A ALA   A 1 50  ? 23.285 4.217   3.366   0.60 12.60 ?  50  ALA   A HA   1 
ATOM   1183 H HA   B ALA   A 1 50  ? 23.360 4.334   3.659   0.40 12.22 ?  50  ALA   A HA   1 
ATOM   1184 H HB1  A ALA   A 1 50  ? 24.615 4.965   1.591   0.60 13.27 ?  50  ALA   A HB1  1 
ATOM   1185 H HB1  B ALA   A 1 50  ? 24.654 5.089   1.863   0.40 12.37 ?  50  ALA   A HB1  1 
ATOM   1186 H HB2  A ALA   A 1 50  ? 23.829 3.650   1.170   0.60 13.27 ?  50  ALA   A HB2  1 
ATOM   1187 H HB2  B ALA   A 1 50  ? 23.911 3.738   1.480   0.40 12.37 ?  50  ALA   A HB2  1 
ATOM   1188 H HB3  A ALA   A 1 50  ? 23.324 5.072   0.672   0.60 13.27 ?  50  ALA   A HB3  1 
ATOM   1189 H HB3  B ALA   A 1 50  ? 23.355 5.129   0.949   0.40 12.37 ?  50  ALA   A HB3  1 
ATOM   1190 N N    A GLY   A 1 51  ? 21.997 6.969   2.351   0.60 10.76 ?  51  GLY   A N    1 
ATOM   1191 N N    B GLY   A 1 51  ? 21.925 7.015   2.667   0.40 10.25 ?  51  GLY   A N    1 
ATOM   1192 C CA   A GLY   A 1 51  ? 21.869 8.365   2.727   0.60 11.08 ?  51  GLY   A CA   1 
ATOM   1193 C CA   B GLY   A 1 51  ? 21.689 8.394   3.062   0.40 10.53 ?  51  GLY   A CA   1 
ATOM   1194 C C    A GLY   A 1 51  ? 21.253 8.534   4.099   0.60 10.61 ?  51  GLY   A C    1 
ATOM   1195 C C    B GLY   A 1 51  ? 21.150 8.495   4.477   0.40 11.27 ?  51  GLY   A C    1 
ATOM   1196 O O    A GLY   A 1 51  ? 21.619 9.444   4.845   0.60 10.97 ?  51  GLY   A O    1 
ATOM   1197 O O    B GLY   A 1 51  ? 21.583 9.344   5.260   0.40 11.79 ?  51  GLY   A O    1 
ATOM   1198 H H    A GLY   A 1 51  ? 21.543 6.737   1.667   0.60 12.94 ?  51  GLY   A H    1 
ATOM   1199 H H    B GLY   A 1 51  ? 21.481 6.753   1.968   0.40 12.32 ?  51  GLY   A H    1 
ATOM   1200 H HA2  A GLY   A 1 51  ? 22.742 8.782   2.746   0.60 13.33 ?  51  GLY   A HA2  1 
ATOM   1201 H HA2  B GLY   A 1 51  ? 22.522 8.889   3.000   0.40 12.66 ?  51  GLY   A HA2  1 
ATOM   1202 H HA3  A GLY   A 1 51  ? 21.313 8.832   2.086   0.60 13.33 ?  51  GLY   A HA3  1 
ATOM   1203 H HA3  B GLY   A 1 51  ? 21.053 8.799   2.440   0.40 12.66 ?  51  GLY   A HA3  1 
ATOM   1204 N N    A ALA   A 1 52  ? 20.296 7.666   4.443   0.60 11.02 ?  52  ALA   A N    1 
ATOM   1205 N N    B ALA   A 1 52  ? 20.206 7.617   4.826   0.40 11.18 ?  52  ALA   A N    1 
ATOM   1206 C CA   A ALA   A 1 52  ? 19.642 7.739   5.745   0.60 11.38 ?  52  ALA   A CA   1 
ATOM   1207 C CA   B ALA   A 1 52  ? 19.612 7.660   6.158   0.40 11.52 ?  52  ALA   A CA   1 
ATOM   1208 C C    A ALA   A 1 52  ? 20.589 7.338   6.875   0.60 11.51 ?  52  ALA   A C    1 
ATOM   1209 C C    B ALA   A 1 52  ? 20.607 7.234   7.233   0.40 11.06 ?  52  ALA   A C    1 
ATOM   1210 O O    A ALA   A 1 52  ? 20.657 8.015   7.906   0.60 12.11 ?  52  ALA   A O    1 
ATOM   1211 O O    B ALA   A 1 52  ? 20.696 7.872   8.291   0.40 11.62 ?  52  ALA   A O    1 
ATOM   1212 C CB   A ALA   A 1 52  ? 18.383 6.864   5.747   0.60 12.38 ?  52  ALA   A CB   1 
ATOM   1213 C CB   B ALA   A 1 52  ? 18.350 6.798   6.196   0.40 12.86 ?  52  ALA   A CB   1 
ATOM   1214 H H    A ALA   A 1 52  ? 20.019 7.023   3.947   0.60 13.25 ?  52  ALA   A H    1 
ATOM   1215 H H    B ALA   A 1 52  ? 19.910 6.987   4.308   0.40 13.45 ?  52  ALA   A H    1 
ATOM   1216 H HA   A ALA   A 1 52  ? 19.356 8.650   5.904   0.60 13.69 ?  52  ALA   A HA   1 
ATOM   1217 H HA   B ALA   A 1 52  ? 19.354 8.573   6.335   0.40 13.86 ?  52  ALA   A HA   1 
ATOM   1218 H HB1  A ALA   A 1 52  ? 17.951 6.922   6.619   0.60 14.89 ?  52  ALA   A HB1  1 
ATOM   1219 H HB1  B ALA   A 1 52  ? 17.972 6.844   7.085   0.40 15.46 ?  52  ALA   A HB1  1 
ATOM   1220 H HB2  A ALA   A 1 52  ? 17.771 7.181   5.061   0.60 14.89 ?  52  ALA   A HB2  1 
ATOM   1221 H HB2  B ALA   A 1 52  ? 17.713 7.142   5.546   0.40 15.46 ?  52  ALA   A HB2  1 
ATOM   1222 H HB3  A ALA   A 1 52  ? 18.629 5.943   5.567   0.60 14.89 ?  52  ALA   A HB3  1 
ATOM   1223 H HB3  B ALA   A 1 52  ? 18.582 5.883   5.977   0.40 15.46 ?  52  ALA   A HB3  1 
ATOM   1224 N N    A LEU   A 1 53  ? 21.314 6.226   6.713   0.60 11.37 ?  53  LEU   A N    1 
ATOM   1225 N N    B LEU   A 1 53  ? 21.356 6.152   6.993   0.40 10.90 ?  53  LEU   A N    1 
ATOM   1226 C CA   A LEU   A 1 53  ? 22.252 5.808   7.752   0.60 11.83 ?  53  LEU   A CA   1 
ATOM   1227 C CA   B LEU   A 1 53  ? 22.407 5.773   7.933   0.40 10.87 ?  53  LEU   A CA   1 
ATOM   1228 C C    A LEU   A 1 53  ? 23.325 6.863   7.963   0.60 11.76 ?  53  LEU   A C    1 
ATOM   1229 C C    B LEU   A 1 53  ? 23.410 6.909   8.094   0.40 11.20 ?  53  LEU   A C    1 
ATOM   1230 O O    A LEU   A 1 53  ? 23.691 7.168   9.100   0.60 12.73 ?  53  LEU   A O    1 
ATOM   1231 O O    B LEU   A 1 53  ? 23.700 7.345   9.214   0.40 11.69 ?  53  LEU   A O    1 
ATOM   1232 C CB   A LEU   A 1 53  ? 22.906 4.470   7.388   0.60 12.17 ?  53  LEU   A CB   1 
ATOM   1233 C CB   B LEU   A 1 53  ? 23.113 4.491   7.471   0.40 10.27 ?  53  LEU   A CB   1 
ATOM   1234 C CG   A LEU   A 1 53  ? 22.022 3.222   7.459   0.60 12.06 ?  53  LEU   A CG   1 
ATOM   1235 C CG   B LEU   A 1 53  ? 22.386 3.146   7.579   0.40 10.67 ?  53  LEU   A CG   1 
ATOM   1236 C CD1  A LEU   A 1 53  ? 22.759 2.023   6.880   0.60 11.99 ?  53  LEU   A CD1  1 
ATOM   1237 C CD1  B LEU   A 1 53  ? 23.237 2.074   6.914   0.40 10.61 ?  53  LEU   A CD1  1 
ATOM   1238 C CD2  A LEU   A 1 53  ? 21.587 2.941   8.884   0.60 12.78 ?  53  LEU   A CD2  1 
ATOM   1239 C CD2  B LEU   A 1 53  ? 22.096 2.762   9.022   0.40 11.16 ?  53  LEU   A CD2  1 
ATOM   1240 H H    A LEU   A 1 53  ? 21.274 5.712   6.035   0.60 13.67 ?  53  LEU   A H    1 
ATOM   1241 H H    B LEU   A 1 53  ? 21.273 5.630   6.304   0.40 13.11 ?  53  LEU   A H    1 
ATOM   1242 H HA   A LEU   A 1 53  ? 21.775 5.693   8.592   0.60 14.22 ?  53  LEU   A HA   1 
ATOM   1243 H HA   B LEU   A 1 53  ? 22.003 5.598   8.792   0.40 13.07 ?  53  LEU   A HA   1 
ATOM   1244 H HB2  A LEU   A 1 53  ? 23.237 4.540   6.478   0.60 14.64 ?  53  LEU   A HB2  1 
ATOM   1245 H HB2  B LEU   A 1 53  ? 23.345 4.602   6.535   0.40 12.36 ?  53  LEU   A HB2  1 
ATOM   1246 H HB3  A LEU   A 1 53  ? 23.654 4.328   7.989   0.60 14.64 ?  53  LEU   A HB3  1 
ATOM   1247 H HB3  B LEU   A 1 53  ? 23.927 4.405   7.986   0.40 12.36 ?  53  LEU   A HB3  1 
ATOM   1248 H HG   A LEU   A 1 53  ? 21.227 3.371   6.924   0.60 14.50 ?  53  LEU   A HG   1 
ATOM   1249 H HG   B LEU   A 1 53  ? 21.545 3.194   7.100   0.40 12.83 ?  53  LEU   A HG   1 
ATOM   1250 H HD11 A LEU   A 1 53  ? 22.181 1.245   6.935   0.60 14.42 ?  53  LEU   A HD11 1 
ATOM   1251 H HD11 B LEU   A 1 53  ? 22.784 1.218   6.987   0.40 12.76 ?  53  LEU   A HD11 1 
ATOM   1252 H HD12 A LEU   A 1 53  ? 22.983 2.205   5.955   0.60 14.42 ?  53  LEU   A HD12 1 
ATOM   1253 H HD12 B LEU   A 1 53  ? 23.361 2.302   5.979   0.40 12.76 ?  53  LEU   A HD12 1 
ATOM   1254 H HD13 A LEU   A 1 53  ? 23.567 1.872   7.394   0.60 14.42 ?  53  LEU   A HD13 1 
ATOM   1255 H HD13 B LEU   A 1 53  ? 24.098 2.030   7.360   0.40 12.76 ?  53  LEU   A HD13 1 
ATOM   1256 H HD21 A LEU   A 1 53  ? 21.089 2.109   8.903   0.60 15.36 ?  53  LEU   A HD21 1 
ATOM   1257 H HD21 B LEU   A 1 53  ? 21.641 1.904   9.037   0.40 13.42 ?  53  LEU   A HD21 1 
ATOM   1258 H HD22 A LEU   A 1 53  ? 22.376 2.866   9.445   0.60 15.36 ?  53  LEU   A HD22 1 
ATOM   1259 H HD22 B LEU   A 1 53  ? 22.931 2.701   9.510   0.40 13.42 ?  53  LEU   A HD22 1 
ATOM   1260 H HD23 A LEU   A 1 53  ? 21.028 3.668   9.197   0.60 15.36 ?  53  LEU   A HD23 1 
ATOM   1261 H HD23 B LEU   A 1 53  ? 21.528 3.441   9.420   0.40 13.42 ?  53  LEU   A HD23 1 
ATOM   1262 N N    A ASN   A 1 54  ? 23.847 7.427   6.879   0.60 10.96 ?  54  ASN   A N    1 
ATOM   1263 N N    B ASN   A 1 54  ? 23.932 7.418   6.978   0.40 11.32 ?  54  ASN   A N    1 
ATOM   1264 C CA   A ASN   A 1 54  ? 24.907 8.414   7.031   0.60 11.63 ?  54  ASN   A CA   1 
ATOM   1265 C CA   B ASN   A 1 54  ? 24.954 8.454   7.070   0.40 11.65 ?  54  ASN   A CA   1 
ATOM   1266 C C    A ASN   A 1 54  ? 24.405 9.653   7.769   0.60 12.06 ?  54  ASN   A C    1 
ATOM   1267 C C    B ASN   A 1 54  ? 24.421 9.700   7.767   0.40 11.88 ?  54  ASN   A C    1 
ATOM   1268 O O    A ASN   A 1 54  ? 25.099 10.189  8.643   0.60 12.70 ?  54  ASN   A O    1 
ATOM   1269 O O    B ASN   A 1 54  ? 25.111 10.293  8.606   0.40 12.17 ?  54  ASN   A O    1 
ATOM   1270 C CB   A ASN   A 1 54  ? 25.467 8.787   5.668   0.60 11.74 ?  54  ASN   A CB   1 
ATOM   1271 C CB   B ASN   A 1 54  ? 25.495 8.805   5.691   0.40 11.88 ?  54  ASN   A CB   1 
ATOM   1272 C CG   A ASN   A 1 54  ? 26.508 9.866   5.775   0.60 11.75 ?  54  ASN   A CG   1 
ATOM   1273 C CG   B ASN   A 1 54  ? 26.485 9.945   5.750   0.40 11.93 ?  54  ASN   A CG   1 
ATOM   1274 O OD1  A ASN   A 1 54  ? 27.479 9.727   6.529   0.60 11.14 ?  54  ASN   A OD1  1 
ATOM   1275 O OD1  B ASN   A 1 54  ? 27.563 9.803   6.328   0.40 12.19 ?  54  ASN   A OD1  1 
ATOM   1276 N ND2  A ASN   A 1 54  ? 26.298 10.971  5.074   0.60 12.51 ?  54  ASN   A ND2  1 
ATOM   1277 N ND2  B ASN   A 1 54  ? 26.123 11.088  5.183   0.40 12.06 ?  54  ASN   A ND2  1 
ATOM   1278 H H    A ASN   A 1 54  ? 23.604 7.261   6.074   0.60 13.18 ?  54  ASN   A H    1 
ATOM   1279 H H    B ASN   A 1 54  ? 23.711 7.189   6.177   0.40 13.61 ?  54  ASN   A H    1 
ATOM   1280 H HA   A ASN   A 1 54  ? 25.619 8.026   7.555   0.60 13.98 ?  54  ASN   A HA   1 
ATOM   1281 H HA   B ASN   A 1 54  ? 25.686 8.114   7.601   0.40 14.00 ?  54  ASN   A HA   1 
ATOM   1282 H HB2  A ASN   A 1 54  ? 25.885 7.998   5.274   0.60 14.11 ?  54  ASN   A HB2  1 
ATOM   1283 H HB2  B ASN   A 1 54  ? 25.947 8.028   5.323   0.40 14.29 ?  54  ASN   A HB2  1 
ATOM   1284 H HB3  A ASN   A 1 54  ? 24.752 9.103   5.099   0.60 14.11 ?  54  ASN   A HB3  1 
ATOM   1285 H HB3  B ASN   A 1 54  ? 24.762 9.069   5.117   0.40 14.29 ?  54  ASN   A HB3  1 
ATOM   1286 H HD21 A ASN   A 1 54  ? 26.867 11.611  5.109   0.60 15.05 ?  54  ASN   A HD21 1 
ATOM   1287 H HD21 B ASN   A 1 54  ? 26.657 11.762  5.203   0.40 14.50 ?  54  ASN   A HD21 1 
ATOM   1288 H HD22 A ASN   A 1 54  ? 25.600 11.037  4.577   0.60 15.05 ?  54  ASN   A HD22 1 
ATOM   1289 H HD22 B ASN   A 1 54  ? 25.364 11.149  4.788   0.40 14.50 ?  54  ASN   A HD22 1 
ATOM   1290 N N    . LYS   A 1 55  ? 23.196 10.118  7.434   1.00 11.93 ?  55  LYS   A N    1 
ATOM   1291 C CA   . LYS   A 1 55  ? 22.616 11.277  8.102   1.00 12.86 ?  55  LYS   A CA   1 
ATOM   1292 C C    . LYS   A 1 55  ? 22.538 11.042  9.604   1.00 12.78 ?  55  LYS   A C    1 
ATOM   1293 O O    . LYS   A 1 55  ? 22.816 11.948  10.402  1.00 13.43 ?  55  LYS   A O    1 
ATOM   1294 C CB   . LYS   A 1 55  ? 21.237 11.564  7.499   1.00 14.06 ?  55  LYS   A CB   1 
ATOM   1295 C CG   . LYS   A 1 55  ? 20.485 12.727  8.117   1.00 15.82 ?  55  LYS   A CG   1 
ATOM   1296 C CD   . LYS   A 1 55  ? 19.155 12.949  7.393   1.00 17.15 ?  55  LYS   A CD   1 
ATOM   1297 C CE   . LYS   A 1 55  ? 18.326 14.061  8.021   1.00 18.73 ?  55  LYS   A CE   1 
ATOM   1298 N NZ   . LYS   A 1 55  ? 16.996 14.215  7.360   1.00 19.78 ?  55  LYS   A NZ   1 
ATOM   1299 H H    A LYS   A 1 55  ? 22.687 9.769   6.833   0.60 14.35 ?  55  LYS   A H    1 
ATOM   1300 H H    B LYS   A 1 55  ? 22.684 9.746   6.849   0.40 14.35 ?  55  LYS   A H    1 
ATOM   1301 H HA   . LYS   A 1 55  ? 23.177 12.052  7.945   1.00 15.46 ?  55  LYS   A HA   1 
ATOM   1302 H HB2  . LYS   A 1 55  ? 21.345 11.761  6.556   1.00 16.90 ?  55  LYS   A HB2  1 
ATOM   1303 H HB3  . LYS   A 1 55  ? 20.682 10.774  7.604   1.00 16.90 ?  55  LYS   A HB3  1 
ATOM   1304 H HG2  . LYS   A 1 55  ? 20.294 12.532  9.049   1.00 19.02 ?  55  LYS   A HG2  1 
ATOM   1305 H HG3  . LYS   A 1 55  ? 21.014 13.533  8.039   1.00 19.02 ?  55  LYS   A HG3  1 
ATOM   1306 H HD2  . LYS   A 1 55  ? 19.342 13.199  6.478   1.00 20.61 ?  55  LYS   A HD2  1 
ATOM   1307 H HD3  . LYS   A 1 55  ? 18.634 12.128  7.416   1.00 20.61 ?  55  LYS   A HD3  1 
ATOM   1308 H HE2  . LYS   A 1 55  ? 18.175 13.858  8.957   1.00 22.51 ?  55  LYS   A HE2  1 
ATOM   1309 H HE3  . LYS   A 1 55  ? 18.804 14.901  7.933   1.00 22.51 ?  55  LYS   A HE3  1 
ATOM   1310 H HZ1  . LYS   A 1 55  ? 16.377 14.432  7.965   1.00 23.77 ?  55  LYS   A HZ1  1 
ATOM   1311 H HZ2  . LYS   A 1 55  ? 17.029 14.861  6.746   1.00 23.77 ?  55  LYS   A HZ2  1 
ATOM   1312 H HZ3  . LYS   A 1 55  ? 16.755 13.454  6.967   1.00 23.77 ?  55  LYS   A HZ3  1 
ATOM   1313 N N    . ALA   A 1 56  ? 22.151 9.830   10.010  1.00 13.21 ?  56  ALA   A N    1 
ATOM   1314 C CA   . ALA   A 1 56  ? 22.034 9.502   11.426  1.00 13.67 ?  56  ALA   A CA   1 
ATOM   1315 C C    . ALA   A 1 56  ? 23.377 9.528   12.148  1.00 13.75 ?  56  ALA   A C    1 
ATOM   1316 O O    . ALA   A 1 56  ? 23.403 9.695   13.369  1.00 15.23 ?  56  ALA   A O    1 
ATOM   1317 C CB   . ALA   A 1 56  ? 21.353 8.137   11.597  1.00 15.14 ?  56  ALA   A CB   1 
ATOM   1318 H H    . ALA   A 1 56  ? 21.943 9.188   9.478   1.00 15.88 ?  56  ALA   A H    1 
ATOM   1319 H HA   . ALA   A 1 56  ? 21.470 10.156  11.853  1.00 16.43 ?  56  ALA   A HA   1 
ATOM   1320 H HB1  . ALA   A 1 56  ? 21.280 7.932   12.544  1.00 18.20 ?  56  ALA   A HB1  1 
ATOM   1321 H HB2  . ALA   A 1 56  ? 20.472 8.172   11.197  1.00 18.20 ?  56  ALA   A HB2  1 
ATOM   1322 H HB3  . ALA   A 1 56  ? 21.888 7.452   11.157  1.00 18.20 ?  56  ALA   A HB3  1 
ATOM   1323 N N    . THR   A 1 57  ? 24.487 9.344   11.426  1.00 13.01 ?  57  THR   A N    1 
ATOM   1324 C CA   . THR   A 1 57  ? 25.832 9.474   11.994  1.00 13.20 ?  57  THR   A CA   1 
ATOM   1325 C C    . THR   A 1 57  ? 26.385 10.894  11.908  1.00 13.74 ?  57  THR   A C    1 
ATOM   1326 O O    . THR   A 1 57  ? 27.573 11.103  12.184  1.00 14.29 ?  57  THR   A O    1 
ATOM   1327 C CB   . THR   A 1 57  ? 26.842 8.523   11.324  1.00 13.06 ?  57  THR   A CB   1 
ATOM   1328 O OG1  . THR   A 1 57  ? 27.208 9.007   10.021  1.00 12.55 ?  57  THR   A OG1  1 
ATOM   1329 C CG2  . THR   A 1 57  ? 26.307 7.100   11.234  1.00 12.74 ?  57  THR   A CG2  1 
ATOM   1330 H H    . THR   A 1 57  ? 24.487 9.108   10.595  1.00 15.64 ?  57  THR   A H    1 
ATOM   1331 H HA   . THR   A 1 57  ? 25.792 9.221   12.933  1.00 15.86 ?  57  THR   A HA   1 
ATOM   1332 H HB   . THR   A 1 57  ? 27.644 8.485   11.872  1.00 15.70 ?  57  THR   A HB   1 
ATOM   1333 H HG1  . THR   A 1 57  ? 26.522 9.056   9.534   1.00 15.08 ?  57  THR   A HG1  1 
ATOM   1334 H HG21 . THR   A 1 57  ? 26.991 6.501   10.894  1.00 15.31 ?  57  THR   A HG21 1 
ATOM   1335 H HG22 . THR   A 1 57  ? 26.030 6.789   12.113  1.00 15.31 ?  57  THR   A HG22 1 
ATOM   1336 H HG23 . THR   A 1 57  ? 25.541 7.066   10.639  1.00 15.31 ?  57  THR   A HG23 1 
ATOM   1337 N N    . ASN   A 1 58  ? 25.564 11.864  11.515  1.00 14.13 ?  58  ASN   A N    1 
ATOM   1338 C CA   . ASN   A 1 58  ? 26.023 13.245  11.410  1.00 15.12 ?  58  ASN   A CA   1 
ATOM   1339 C C    . ASN   A 1 58  ? 27.171 13.373  10.403  1.00 13.93 ?  58  ASN   A C    1 
ATOM   1340 O O    . ASN   A 1 58  ? 28.067 14.205  10.559  1.00 14.53 ?  58  ASN   A O    1 
ATOM   1341 C CB   . ASN   A 1 58  ? 26.388 13.794  12.803  1.00 17.98 ?  58  ASN   A CB   1 
ATOM   1342 C CG   . ASN   A 1 58  ? 26.799 15.252  12.787  1.00 21.85 ?  58  ASN   A CG   1 
ATOM   1343 O OD1  . ASN   A 1 58  ? 26.164 16.074  12.136  1.00 23.59 ?  58  ASN   A OD1  1 
ATOM   1344 N ND2  . ASN   A 1 58  ? 27.869 15.582  13.518  1.00 23.05 ?  58  ASN   A ND2  1 
ATOM   1345 H H    . ASN   A 1 58  ? 24.740 11.743  11.295  1.00 16.98 ?  58  ASN   A H    1 
ATOM   1346 H HA   . ASN   A 1 58  ? 25.289 13.775  11.078  1.00 18.17 ?  58  ASN   A HA   1 
ATOM   1347 H HB2  . ASN   A 1 58  ? 25.610 13.709  13.389  1.00 21.61 ?  58  ASN   A HB2  1 
ATOM   1348 H HB3  . ASN   A 1 58  ? 27.124 13.286  13.170  1.00 21.61 ?  58  ASN   A HB3  1 
ATOM   1349 H HD21 . ASN   A 1 58  ? 28.137 16.403  13.543  1.00 27.69 ?  58  ASN   A HD21 1 
ATOM   1350 H HD22 . ASN   A 1 58  ? 28.282 14.981  13.965  1.00 27.69 ?  58  ASN   A HD22 1 
ATOM   1351 N N    . ASN   A 1 59  ? 27.144 12.558  9.347   1.00 12.92 ?  59  ASN   A N    1 
ATOM   1352 C CA   . ASN   A 1 59  ? 28.118 12.536  8.241   1.00 12.44 ?  59  ASN   A CA   1 
ATOM   1353 C C    . ASN   A 1 59  ? 29.436 11.846  8.617   1.00 12.50 ?  59  ASN   A C    1 
ATOM   1354 O O    . ASN   A 1 59  ? 30.354 11.798  7.789   1.00 12.28 ?  59  ASN   A O    1 
ATOM   1355 C CB   . ASN   A 1 59  ? 28.408 13.923  7.638   1.00 12.44 ?  59  ASN   A CB   1 
ATOM   1356 C CG   . ASN   A 1 59  ? 28.768 13.856  6.171   1.00 12.74 ?  59  ASN   A CG   1 
ATOM   1357 O OD1  . ASN   A 1 59  ? 28.059 13.240  5.375   1.00 13.33 ?  59  ASN   A OD1  1 
ATOM   1358 N ND2  . ASN   A 1 59  ? 29.863 14.513  5.796   1.00 13.49 ?  59  ASN   A ND2  1 
ATOM   1359 H H    . ASN   A 1 59  ? 26.528 11.967  9.240   1.00 15.53 ?  59  ASN   A H    1 
ATOM   1360 H HA   . ASN   A 1 59  ? 27.729 12.012  7.533   1.00 14.95 ?  59  ASN   A HA   1 
ATOM   1361 H HB2  . ASN   A 1 59  ? 27.615 14.483  7.722   1.00 14.96 ?  59  ASN   A HB2  1 
ATOM   1362 H HB3  . ASN   A 1 59  ? 29.150 14.333  8.106   1.00 14.96 ?  59  ASN   A HB3  1 
ATOM   1363 H HD21 . ASN   A 1 59  ? 30.110 14.508  4.971   1.00 16.21 ?  59  ASN   A HD21 1 
ATOM   1364 H HD22 . ASN   A 1 59  ? 30.329 14.944  6.378   1.00 16.21 ?  59  ASN   A HD22 1 
ATOM   1365 N N    . ALA   A 1 60  ? 29.567 11.302  9.824   1.00 12.19 ?  60  ALA   A N    1 
ATOM   1366 C CA   . ALA   A 1 60  ? 30.806 10.618  10.177  1.00 12.36 ?  60  ALA   A CA   1 
ATOM   1367 C C    . ALA   A 1 60  ? 31.030 9.380   9.319   1.00 12.53 ?  60  ALA   A C    1 
ATOM   1368 O O    . ALA   A 1 60  ? 32.175 9.056   8.989   1.00 12.94 ?  60  ALA   A O    1 
ATOM   1369 C CB   . ALA   A 1 60  ? 30.811 10.269  11.660  1.00 12.99 ?  60  ALA   A CB   1 
ATOM   1370 H H    . ALA   A 1 60  ? 28.973 11.318  10.443  1.00 14.66 ?  60  ALA   A H    1 
ATOM   1371 H HA   . ALA   A 1 60  ? 31.551 11.223  10.013  1.00 14.86 ?  60  ALA   A HA   1 
ATOM   1372 H HB1  . ALA   A 1 60  ? 31.641 9.816   11.875  1.00 15.62 ?  60  ALA   A HB1  1 
ATOM   1373 H HB2  . ALA   A 1 60  ? 30.740 11.089  12.176  1.00 15.62 ?  60  ALA   A HB2  1 
ATOM   1374 H HB3  . ALA   A 1 60  ? 30.057 9.692   11.850  1.00 15.62 ?  60  ALA   A HB3  1 
ATOM   1375 N N    . MET   A 1 61  ? 29.953 8.688   8.933   1.00 11.94 ?  61  MET   A N    1 
ATOM   1376 C CA   . MET   A 1 61  ? 30.088 7.550   8.028   1.00 12.00 ?  61  MET   A CA   1 
ATOM   1377 C C    . MET   A 1 61  ? 30.721 7.977   6.704   1.00 11.86 ?  61  MET   A C    1 
ATOM   1378 O O    . MET   A 1 61  ? 31.609 7.292   6.180   1.00 12.03 ?  61  MET   A O    1 
ATOM   1379 C CB   . MET   A 1 61  ? 28.722 6.890   7.812   1.00 11.91 ?  61  MET   A CB   1 
ATOM   1380 C CG   . MET   A 1 61  ? 28.722 5.726   6.835   1.00 12.50 ?  61  MET   A CG   1 
ATOM   1381 S SD   . MET   A 1 61  ? 27.109 4.962   6.662   1.00 13.44 ?  61  MET   A SD   1 
ATOM   1382 C CE   . MET   A 1 61  ? 27.013 4.078   8.221   1.00 15.23 ?  61  MET   A CE   1 
ATOM   1383 H H    . MET   A 1 61  ? 29.146 8.861   9.174   1.00 14.36 ?  61  MET   A H    1 
ATOM   1384 H HA   . MET   A 1 61  ? 30.665 6.894   8.444   1.00 14.43 ?  61  MET   A HA   1 
ATOM   1385 H HB2  . MET   A 1 61  ? 28.405 6.559   8.662   1.00 14.32 ?  61  MET   A HB2  1 
ATOM   1386 H HB3  . MET   A 1 61  ? 28.108 7.558   7.470   1.00 14.32 ?  61  MET   A HB3  1 
ATOM   1387 H HG2  . MET   A 1 61  ? 28.986 6.042   5.956   1.00 15.03 ?  61  MET   A HG2  1 
ATOM   1388 H HG3  . MET   A 1 61  ? 29.340 5.049   7.144   1.00 15.03 ?  61  MET   A HG3  1 
ATOM   1389 H HE1  . MET   A 1 61  ? 26.182 3.578   8.253   1.00 18.30 ?  61  MET   A HE1  1 
ATOM   1390 H HE2  . MET   A 1 61  ? 27.766 3.469   8.285   1.00 18.30 ?  61  MET   A HE2  1 
ATOM   1391 H HE3  . MET   A 1 61  ? 27.043 4.715   8.954   1.00 18.30 ?  61  MET   A HE3  1 
ATOM   1392 N N    . GLN   A 1 62  ? 30.271 9.106   6.145   1.00 11.94 ?  62  GLN   A N    1 
ATOM   1393 C CA   . GLN   A 1 62  ? 30.829 9.584   4.883   1.00 12.15 ?  62  GLN   A CA   1 
ATOM   1394 C C    . GLN   A 1 62  ? 32.298 9.964   5.022   1.00 11.79 ?  62  GLN   A C    1 
ATOM   1395 O O    . GLN   A 1 62  ? 33.107 9.643   4.144   1.00 12.10 ?  62  GLN   A O    1 
ATOM   1396 C CB   . GLN   A 1 62  ? 30.025 10.769  4.352   1.00 12.55 ?  62  GLN   A CB   1 
ATOM   1397 C CG   . GLN   A 1 62  ? 30.388 11.127  2.915   1.00 12.50 ?  62  GLN   A CG   1 
ATOM   1398 C CD   . GLN   A 1 62  ? 30.059 9.998   1.973   1.00 12.62 ?  62  GLN   A CD   1 
ATOM   1399 O OE1  . GLN   A 1 62  ? 28.878 9.695   1.759   1.00 13.04 ?  62  GLN   A OE1  1 
ATOM   1400 N NE2  . GLN   A 1 62  ? 31.076 9.329   1.447   1.00 13.33 ?  62  GLN   A NE2  1 
ATOM   1401 H H    . GLN   A 1 62  ? 29.649 9.597   6.468   1.00 14.35 ?  62  GLN   A H    1 
ATOM   1402 H HA   . GLN   A 1 62  ? 30.776 8.865   4.230   1.00 14.60 ?  62  GLN   A HA   1 
ATOM   1403 H HB2  . GLN   A 1 62  ? 29.083 10.551  4.382   1.00 15.09 ?  62  GLN   A HB2  1 
ATOM   1404 H HB3  . GLN   A 1 62  ? 30.208 11.545  4.905   1.00 15.09 ?  62  GLN   A HB3  1 
ATOM   1405 H HG2  . GLN   A 1 62  ? 29.870 11.898  2.637   1.00 15.03 ?  62  GLN   A HG2  1 
ATOM   1406 H HG3  . GLN   A 1 62  ? 31.334 11.310  2.850   1.00 15.03 ?  62  GLN   A HG3  1 
ATOM   1407 H HE21 . GLN   A 1 62  ? 31.884 9.564   1.627   1.00 16.02 ?  62  GLN   A HE21 1 
ATOM   1408 H HE22 . GLN   A 1 62  ? 30.931 8.672   0.910   1.00 16.02 ?  62  GLN   A HE22 1 
ATOM   1409 N N    . VAL   A 1 63  ? 32.666 10.643  6.115   1.00 12.73 ?  63  VAL   A N    1 
ATOM   1410 C CA   . VAL   A 1 63  ? 34.060 11.036  6.328   1.00 13.58 ?  63  VAL   A CA   1 
ATOM   1411 C C    . VAL   A 1 63  ? 34.959 9.800   6.388   1.00 12.62 ?  63  VAL   A C    1 
ATOM   1412 O O    . VAL   A 1 63  ? 36.008 9.730   5.730   1.00 13.29 ?  63  VAL   A O    1 
ATOM   1413 C CB   . VAL   A 1 63  ? 34.174 11.909  7.593   1.00 15.06 ?  63  VAL   A CB   1 
ATOM   1414 C CG1  . VAL   A 1 63  ? 35.627 12.153  7.947   1.00 16.56 ?  63  VAL   A CG1  1 
ATOM   1415 C CG2  . VAL   A 1 63  ? 33.450 13.238  7.397   1.00 15.22 ?  63  VAL   A CG2  1 
ATOM   1416 H H    . VAL   A 1 63  ? 32.126 10.884  6.742   1.00 15.31 ?  63  VAL   A H    1 
ATOM   1417 H HA   . VAL   A 1 63  ? 34.347 11.570  5.575   1.00 16.33 ?  63  VAL   A HA   1 
ATOM   1418 H HB   . VAL   A 1 63  ? 33.759 11.443  8.338   1.00 18.10 ?  63  VAL   A HB   1 
ATOM   1419 H HG11 . VAL   A 1 63  ? 35.676 12.888  8.573   1.00 19.91 ?  63  VAL   A HG11 1 
ATOM   1420 H HG12 . VAL   A 1 63  ? 35.995 11.350  8.347   1.00 19.91 ?  63  VAL   A HG12 1 
ATOM   1421 H HG13 . VAL   A 1 63  ? 36.111 12.373  7.136   1.00 19.91 ?  63  VAL   A HG13 1 
ATOM   1422 H HG21 . VAL   A 1 63  ? 33.537 13.766  8.209   1.00 18.29 ?  63  VAL   A HG21 1 
ATOM   1423 H HG22 . VAL   A 1 63  ? 33.847 13.708  6.651   1.00 18.29 ?  63  VAL   A HG22 1 
ATOM   1424 H HG23 . VAL   A 1 63  ? 32.511 13.063  7.220   1.00 18.29 ?  63  VAL   A HG23 1 
ATOM   1425 N N    . GLU   A 1 64  ? 34.538 8.791   7.154   1.00 12.80 ?  64  GLU   A N    1 
ATOM   1426 C CA   . GLU   A 1 64  ? 35.297 7.550   7.247   1.00 12.69 ?  64  GLU   A CA   1 
ATOM   1427 C C    . GLU   A 1 64  ? 35.382 6.865   5.889   1.00 12.33 ?  64  GLU   A C    1 
ATOM   1428 O O    . GLU   A 1 64  ? 36.432 6.320   5.511   1.00 12.77 ?  64  GLU   A O    1 
ATOM   1429 C CB   . GLU   A 1 64  ? 34.602 6.634   8.254   1.00 13.12 ?  64  GLU   A CB   1 
ATOM   1430 C CG   . GLU   A 1 64  ? 35.258 5.285   8.422   1.00 13.82 ?  64  GLU   A CG   1 
ATOM   1431 C CD   . GLU   A 1 64  ? 34.377 4.290   9.149   1.00 14.50 ?  64  GLU   A CD   1 
ATOM   1432 O OE1  . GLU   A 1 64  ? 33.138 4.383   9.016   1.00 15.09 ?  64  GLU   A OE1  1 
ATOM   1433 O OE2  . GLU   A 1 64  ? 34.930 3.402   9.836   1.00 14.59 -1 64  GLU   A OE2  1 
ATOM   1434 H H    . GLU   A 1 64  ? 33.814 8.797   7.622   1.00 15.38 ?  64  GLU   A H    1 
ATOM   1435 H HA   . GLU   A 1 64  ? 36.197 7.744   7.566   1.00 15.26 ?  64  GLU   A HA   1 
ATOM   1436 H HB2  . GLU   A 1 64  ? 34.600 7.077   9.123   1.00 15.77 ?  64  GLU   A HB2  1 
ATOM   1437 H HB3  . GLU   A 1 64  ? 33.689 6.497   7.961   1.00 15.77 ?  64  GLU   A HB3  1 
ATOM   1438 H HG2  . GLU   A 1 64  ? 35.455 4.912   7.549   1.00 16.62 ?  64  GLU   A HG2  1 
ATOM   1439 H HG3  . GLU   A 1 64  ? 36.075 5.397   8.928   1.00 16.62 ?  64  GLU   A HG3  1 
ATOM   1440 N N    . SER   A 1 65  ? 34.262 6.858   5.161   1.00 12.23 ?  65  SER   A N    1 
ATOM   1441 C CA   . SER   A 1 65  ? 34.202 6.197   3.862   1.00 12.12 ?  65  SER   A CA   1 
ATOM   1442 C C    . SER   A 1 65  ? 35.124 6.863   2.849   1.00 12.22 ?  65  SER   A C    1 
ATOM   1443 O O    . SER   A 1 65  ? 35.767 6.181   2.044   1.00 13.06 ?  65  SER   A O    1 
ATOM   1444 C CB   . SER   A 1 65  ? 32.765 6.206   3.339   1.00 12.00 ?  65  SER   A CB   1 
ATOM   1445 O OG   . SER   A 1 65  ? 31.911 5.390   4.130   1.00 12.46 ?  65  SER   A OG   1 
ATOM   1446 H H    . SER   A 1 65  ? 33.524 7.230   5.399   1.00 14.71 ?  65  SER   A H    1 
ATOM   1447 H HA   . SER   A 1 65  ? 34.485 5.276   3.960   1.00 14.57 ?  65  SER   A HA   1 
ATOM   1448 H HB2  . SER   A 1 65  ? 32.428 7.109   3.352   1.00 14.42 ?  65  SER   A HB2  1 
ATOM   1449 H HB3  . SER   A 1 65  ? 32.763 5.863   2.429   1.00 14.42 ?  65  SER   A HB3  1 
ATOM   1450 H HG   . SER   A 1 65  ? 31.904 5.664   4.927   1.00 14.98 ?  65  SER   A HG   1 
ATOM   1451 N N    . ASP   A 1 66  ? 35.201 8.197   2.866   1.00 12.43 ?  66  ASP   A N    1 
ATOM   1452 C CA   . ASP   A 1 66  ? 36.066 8.891   1.917   1.00 13.43 ?  66  ASP   A CA   1 
ATOM   1453 C C    . ASP   A 1 66  ? 37.528 8.534   2.151   1.00 13.41 ?  66  ASP   A C    1 
ATOM   1454 O O    . ASP   A 1 66  ? 38.297 8.368   1.197   1.00 14.37 ?  66  ASP   A O    1 
ATOM   1455 C CB   . ASP   A 1 66  ? 35.854 10.401  2.020   1.00 14.57 ?  66  ASP   A CB   1 
ATOM   1456 C CG   . ASP   A 1 66  ? 34.518 10.867  1.430   1.00 16.04 ?  66  ASP   A CG   1 
ATOM   1457 O OD1  . ASP   A 1 66  ? 33.786 10.072  0.794   1.00 16.52 ?  66  ASP   A OD1  1 
ATOM   1458 O OD2  . ASP   A 1 66  ? 34.224 12.070  1.584   1.00 18.59 -1 66  ASP   A OD2  1 
ATOM   1459 H H    . ASP   A 1 66  ? 34.765 8.711   3.402   1.00 14.95 ?  66  ASP   A H    1 
ATOM   1460 H HA   . ASP   A 1 66  ? 35.830 8.619   1.019   1.00 16.15 ?  66  ASP   A HA   1 
ATOM   1461 H HB2  . ASP   A 1 66  ? 35.875 10.662  2.953   1.00 17.52 ?  66  ASP   A HB2  1 
ATOM   1462 H HB3  . ASP   A 1 66  ? 36.569 10.852  1.537   1.00 17.52 ?  66  ASP   A HB3  1 
ATOM   1463 N N    . ASP   A 1 67  ? 37.928 8.408   3.413   1.00 13.41 ?  67  ASP   A N    1 
ATOM   1464 C CA   . ASP   A 1 67  ? 39.284 7.962   3.706   1.00 14.11 ?  67  ASP   A CA   1 
ATOM   1465 C C    . ASP   A 1 67  ? 39.501 6.525   3.241   1.00 13.86 ?  67  ASP   A C    1 
ATOM   1466 O O    . ASP   A 1 67  ? 40.564 6.197   2.698   1.00 14.43 ?  67  ASP   A O    1 
ATOM   1467 C CB   . ASP   A 1 67  ? 39.563 8.099   5.200   1.00 15.29 ?  67  ASP   A CB   1 
ATOM   1468 C CG   . ASP   A 1 67  ? 40.857 7.431   5.613   1.00 16.31 ?  67  ASP   A CG   1 
ATOM   1469 O OD1  . ASP   A 1 67  ? 41.936 8.052   5.465   1.00 18.79 ?  67  ASP   A OD1  1 
ATOM   1470 O OD2  . ASP   A 1 67  ? 40.798 6.269   6.079   1.00 16.47 -1 67  ASP   A OD2  1 
ATOM   1471 H H    . ASP   A 1 67  ? 37.452 8.580   4.103   1.00 16.12 ?  67  ASP   A H    1 
ATOM   1472 H HA   . ASP   A 1 67  ? 39.916 8.525   3.228   1.00 16.96 ?  67  ASP   A HA   1 
ATOM   1473 H HB2  . ASP   A 1 67  ? 39.631 9.036   5.422   1.00 18.37 ?  67  ASP   A HB2  1 
ATOM   1474 H HB3  . ASP   A 1 67  ? 38.842 7.683   5.693   1.00 18.37 ?  67  ASP   A HB3  1 
ATOM   1475 N N    . TYR   A 1 68  ? 38.506 5.648   3.439   1.00 13.53 ?  68  TYR   A N    1 
ATOM   1476 C CA   . TYR   A 1 68  ? 38.626 4.266   2.971   1.00 13.81 ?  68  TYR   A CA   1 
ATOM   1477 C C    . TYR   A 1 68  ? 38.866 4.217   1.462   1.00 13.29 ?  68  TYR   A C    1 
ATOM   1478 O O    . TYR   A 1 68  ? 39.739 3.479   0.986   1.00 13.73 ?  68  TYR   A O    1 
ATOM   1479 C CB   . TYR   A 1 68  ? 37.373 3.449   3.348   1.00 14.17 ?  68  TYR   A CB   1 
ATOM   1480 C CG   . TYR   A 1 68  ? 37.397 2.061   2.716   1.00 15.51 ?  68  TYR   A CG   1 
ATOM   1481 C CD1  . TYR   A 1 68  ? 36.934 1.865   1.420   1.00 16.43 ?  68  TYR   A CD1  1 
ATOM   1482 C CD2  . TYR   A 1 68  ? 37.944 0.976   3.384   1.00 16.88 ?  68  TYR   A CD2  1 
ATOM   1483 C CE1  . TYR   A 1 68  ? 36.998 0.641   0.807   1.00 17.45 ?  68  TYR   A CE1  1 
ATOM   1484 C CE2  . TYR   A 1 68  ? 38.008 -0.286  2.772   1.00 17.17 ?  68  TYR   A CE2  1 
ATOM   1485 C CZ   . TYR   A 1 68  ? 37.542 -0.425  1.485   1.00 17.60 ?  68  TYR   A CZ   1 
ATOM   1486 O OH   . TYR   A 1 68  ? 37.618 -1.640  0.861   1.00 18.97 ?  68  TYR   A OH   1 
ATOM   1487 H H    . TYR   A 1 68  ? 37.761 5.831   3.833   1.00 16.26 ?  68  TYR   A H    1 
ATOM   1488 H HA   . TYR   A 1 68  ? 39.384 3.855   3.408   1.00 16.60 ?  68  TYR   A HA   1 
ATOM   1489 H HB2  . TYR   A 1 68  ? 37.336 3.341   4.311   1.00 17.03 ?  68  TYR   A HB2  1 
ATOM   1490 H HB3  . TYR   A 1 68  ? 36.578 3.913   3.034   1.00 17.03 ?  68  TYR   A HB3  1 
ATOM   1491 H HD1  . TYR   A 1 68  ? 36.576 2.587   0.950   1.00 19.75 ?  68  TYR   A HD1  1 
ATOM   1492 H HD2  . TYR   A 1 68  ? 38.278 1.085   4.242   1.00 20.29 ?  68  TYR   A HD2  1 
ATOM   1493 H HE1  . TYR   A 1 68  ? 36.674 0.532   -0.060  1.00 20.96 ?  68  TYR   A HE1  1 
ATOM   1494 H HE2  . TYR   A 1 68  ? 38.378 -1.013  3.214   1.00 20.64 ?  68  TYR   A HE2  1 
ATOM   1495 H HH   . TYR   A 1 68  ? 37.954 -2.214  1.380   1.00 22.79 ?  68  TYR   A HH   1 
ATOM   1496 N N    . ILE   A 1 69  ? 38.078 4.974   0.690   1.00 12.55 ?  69  ILE   A N    1 
ATOM   1497 C CA   . ILE   A 1 69  ? 38.211 4.958   -0.764  1.00 12.73 ?  69  ILE   A CA   1 
ATOM   1498 C C    . ILE   A 1 69  ? 39.542 5.571   -1.195  1.00 13.05 ?  69  ILE   A C    1 
ATOM   1499 O O    . ILE   A 1 69  ? 40.188 5.089   -2.131  1.00 13.21 ?  69  ILE   A O    1 
ATOM   1500 C CB   . ILE   A 1 69  ? 37.007 5.660   -1.422  1.00 13.94 ?  69  ILE   A CB   1 
ATOM   1501 C CG1  . ILE   A 1 69  ? 35.704 4.913   -1.130  1.00 14.67 ?  69  ILE   A CG1  1 
ATOM   1502 C CG2  . ILE   A 1 69  ? 37.216 5.828   -2.925  1.00 15.35 ?  69  ILE   A CG2  1 
ATOM   1503 C CD1  . ILE   A 1 69  ? 35.540 3.629   -1.910  1.00 14.92 ?  69  ILE   A CD1  1 
ATOM   1504 H H    . ILE   A 1 69  ? 37.472 5.504   0.988   1.00 15.09 ?  69  ILE   A H    1 
ATOM   1505 H HA   . ILE   A 1 69  ? 38.207 4.034   -1.058  1.00 15.31 ?  69  ILE   A HA   1 
ATOM   1506 H HB   . ILE   A 1 69  ? 36.926 6.540   -1.035  1.00 16.75 ?  69  ILE   A HB   1 
ATOM   1507 H HG12 . ILE   A 1 69  ? 35.676 4.685   -0.185  1.00 17.63 ?  69  ILE   A HG12 1 
ATOM   1508 H HG13 . ILE   A 1 69  ? 34.955 5.487   -1.348  1.00 17.63 ?  69  ILE   A HG13 1 
ATOM   1509 H HG21 . ILE   A 1 69  ? 36.363 6.040   -3.343  1.00 18.45 ?  69  ILE   A HG21 1 
ATOM   1510 H HG22 . ILE   A 1 69  ? 37.840 6.558   -3.077  1.00 18.45 ?  69  ILE   A HG22 1 
ATOM   1511 H HG23 . ILE   A 1 69  ? 37.569 5.007   -3.296  1.00 18.45 ?  69  ILE   A HG23 1 
ATOM   1512 H HD11 . ILE   A 1 69  ? 34.775 3.145   -1.561  1.00 17.93 ?  69  ILE   A HD11 1 
ATOM   1513 H HD12 . ILE   A 1 69  ? 35.393 3.844   -2.845  1.00 17.93 ?  69  ILE   A HD12 1 
ATOM   1514 H HD13 . ILE   A 1 69  ? 36.341 3.093   -1.814  1.00 17.93 ?  69  ILE   A HD13 1 
ATOM   1515 N N    . ALA   A 1 70  ? 39.965 6.652   -0.540  1.00 13.36 ?  70  ALA   A N    1 
ATOM   1516 C CA   . ALA   A 1 70  ? 41.244 7.257   -0.897  1.00 14.39 ?  70  ALA   A CA   1 
ATOM   1517 C C    . ALA   A 1 70  ? 42.393 6.272   -0.727  1.00 14.72 ?  70  ALA   A C    1 
ATOM   1518 O O    . ALA   A 1 70  ? 43.362 6.312   -1.489  1.00 16.46 ?  70  ALA   A O    1 
ATOM   1519 C CB   . ALA   A 1 70  ? 41.484 8.513   -0.059  1.00 14.98 ?  70  ALA   A CB   1 
ATOM   1520 H H    . ALA   A 1 70  ? 39.540 7.043   0.093   1.00 16.07 ?  70  ALA   A H    1 
ATOM   1521 H HA   . ALA   A 1 70  ? 41.215 7.528   -1.831  1.00 17.30 ?  70  ALA   A HA   1 
ATOM   1522 H HB1  . ALA   A 1 70  ? 42.344 8.901   -0.310  1.00 18.00 ?  70  ALA   A HB1  1 
ATOM   1523 H HB2  . ALA   A 1 70  ? 40.777 9.151   -0.224  1.00 18.00 ?  70  ALA   A HB2  1 
ATOM   1524 H HB3  . ALA   A 1 70  ? 41.502 8.269   0.880   1.00 18.00 ?  70  ALA   A HB3  1 
ATOM   1525 N N    . THR   A 1 71  ? 42.296 5.375   0.253   1.00 14.32 ?  71  THR   A N    1 
ATOM   1526 C CA   . THR   A 1 71  ? 43.350 4.398   0.504   1.00 15.53 ?  71  THR   A CA   1 
ATOM   1527 C C    . THR   A 1 71  ? 43.231 3.176   -0.396  1.00 15.91 ?  71  THR   A C    1 
ATOM   1528 O O    . THR   A 1 71  ? 44.243 2.657   -0.888  1.00 17.38 ?  71  THR   A O    1 
ATOM   1529 C CB   . THR   A 1 71  ? 43.273 3.949   1.960   1.00 17.32 ?  71  THR   A CB   1 
ATOM   1530 O OG1  . THR   A 1 71  ? 43.522 5.075   2.809   1.00 18.58 ?  71  THR   A OG1  1 
ATOM   1531 C CG2  . THR   A 1 71  ? 44.279 2.846   2.246   1.00 18.68 ?  71  THR   A CG2  1 
ATOM   1532 H H    . THR   A 1 71  ? 41.623 5.311   0.781   1.00 17.22 ?  71  THR   A H    1 
ATOM   1533 H HA   . THR   A 1 71  ? 44.213 4.807   0.350   1.00 18.66 ?  71  THR   A HA   1 
ATOM   1534 H HB   . THR   A 1 71  ? 42.382 3.592   2.131   1.00 20.81 ?  71  THR   A HB   1 
ATOM   1535 H HG1  . THR   A 1 71  ? 42.927 5.654   2.679   1.00 22.32 ?  71  THR   A HG1  1 
ATOM   1536 H HG21 . THR   A 1 71  ? 44.415 2.767   3.203   1.00 22.44 ?  71  THR   A HG21 1 
ATOM   1537 H HG22 . THR   A 1 71  ? 43.959 1.996   1.904   1.00 22.44 ?  71  THR   A HG22 1 
ATOM   1538 H HG23 . THR   A 1 71  ? 45.129 3.056   1.826   1.00 22.44 ?  71  THR   A HG23 1 
ATOM   1539 N N    . ASN   A 1 72  ? 42.005 2.676   -0.588  1.00 15.21 ?  72  ASN   A N    1 
ATOM   1540 C CA   . ASN   A 1 72  ? 41.779 1.348   -1.143  1.00 15.29 ?  72  ASN   A CA   1 
ATOM   1541 C C    . ASN   A 1 72  ? 41.157 1.330   -2.528  1.00 15.19 ?  72  ASN   A C    1 
ATOM   1542 O O    . ASN   A 1 72  ? 41.164 0.270   -3.170  1.00 16.23 ?  72  ASN   A O    1 
ATOM   1543 C CB   . ASN   A 1 72  ? 40.893 0.530   -0.195  1.00 15.55 ?  72  ASN   A CB   1 
ATOM   1544 C CG   . ASN   A 1 72  ? 41.513 0.379   1.168   1.00 16.39 ?  72  ASN   A CG   1 
ATOM   1545 O OD1  . ASN   A 1 72  ? 41.065 0.981   2.142   1.00 18.46 ?  72  ASN   A OD1  1 
ATOM   1546 N ND2  . ASN   A 1 72  ? 42.569 -0.409  1.242   1.00 16.76 ?  72  ASN   A ND2  1 
ATOM   1547 H H    . ASN   A 1 72  ? 41.278 3.103   -0.412  1.00 18.28 ?  72  ASN   A H    1 
ATOM   1548 H HA   . ASN   A 1 72  ? 42.632 0.896   -1.209  1.00 18.37 ?  72  ASN   A HA   1 
ATOM   1549 H HB2  . ASN   A 1 72  ? 40.041 0.976   -0.090  1.00 18.68 ?  72  ASN   A HB2  1 
ATOM   1550 H HB3  . ASN   A 1 72  ? 40.766 -0.357  -0.566  1.00 18.68 ?  72  ASN   A HB3  1 
ATOM   1551 H HD21 . ASN   A 1 72  ? 42.969 -0.527  1.995   1.00 20.14 ?  72  ASN   A HD21 1 
ATOM   1552 H HD22 . ASN   A 1 72  ? 42.864 -0.805  0.536   1.00 20.14 ?  72  ASN   A HD22 1 
ATOM   1553 N N    . GLY   A 1 73  ? 40.605 2.443   -2.999  1.00 14.73 ?  73  GLY   A N    1 
ATOM   1554 C CA   . GLY   A 1 73  ? 39.864 2.440   -4.236  1.00 14.56 ?  73  GLY   A CA   1 
ATOM   1555 C C    . GLY   A 1 73  ? 38.469 1.869   -4.062  1.00 13.73 ?  73  GLY   A C    1 
ATOM   1556 O O    . GLY   A 1 73  ? 38.081 1.415   -2.978  1.00 14.35 ?  73  GLY   A O    1 
ATOM   1557 H H    . GLY   A 1 73  ? 40.643 3.215   -2.617  1.00 17.71 ?  73  GLY   A H    1 
ATOM   1558 H HA2  . GLY   A 1 73  ? 39.789 3.351   -4.568  1.00 17.50 ?  73  GLY   A HA2  1 
ATOM   1559 H HA3  . GLY   A 1 73  ? 40.335 1.911   -4.897  1.00 17.50 ?  73  GLY   A HA3  1 
ATOM   1560 N N    . PRO   A 1 74  ? 37.693 1.887   -5.144  1.00 14.22 ?  74  PRO   A N    1 
ATOM   1561 C CA   . PRO   A 1 74  ? 36.296 1.455   -5.063  1.00 14.46 ?  74  PRO   A CA   1 
ATOM   1562 C C    . PRO   A 1 74  ? 36.149 -0.024  -4.736  1.00 13.65 ?  74  PRO   A C    1 
ATOM   1563 O O    . PRO   A 1 74  ? 37.017 -0.852  -5.023  1.00 14.69 ?  74  PRO   A O    1 
ATOM   1564 C CB   . PRO   A 1 74  ? 35.752 1.749   -6.469  1.00 16.07 ?  74  PRO   A CB   1 
ATOM   1565 C CG   . PRO   A 1 74  ? 36.714 2.709   -7.083  1.00 18.25 ?  74  PRO   A CG   1 
ATOM   1566 C CD   . PRO   A 1 74  ? 38.043 2.365   -6.491  1.00 16.13 ?  74  PRO   A CD   1 
ATOM   1567 H HA   . PRO   A 1 74  ? 35.807 1.984   -4.409  1.00 17.38 ?  74  PRO   A HA   1 
ATOM   1568 H HB2  . PRO   A 1 74  ? 35.716 0.923   -6.981  1.00 19.31 ?  74  PRO   A HB2  1 
ATOM   1569 H HB3  . PRO   A 1 74  ? 34.868 2.144   -6.402  1.00 19.31 ?  74  PRO   A HB3  1 
ATOM   1570 H HG2  . PRO   A 1 74  ? 36.727 2.588   -8.045  1.00 21.93 ?  74  PRO   A HG2  1 
ATOM   1571 H HG3  . PRO   A 1 74  ? 36.461 3.614   -6.852  1.00 21.93 ?  74  PRO   A HG3  1 
ATOM   1572 H HD2  . PRO   A 1 74  ? 38.473 1.657   -7.000  1.00 19.38 ?  74  PRO   A HD2  1 
ATOM   1573 H HD3  . PRO   A 1 74  ? 38.604 3.157   -6.446  1.00 19.38 ?  74  PRO   A HD3  1 
ATOM   1574 N N    . LEU   A 1 75  ? 35.001 -0.347  -4.145  1.00 12.80 ?  75  LEU   A N    1 
ATOM   1575 C CA   . LEU   A 1 75  ? 34.599 -1.735  -3.989  1.00 12.49 ?  75  LEU   A CA   1 
ATOM   1576 C C    . LEU   A 1 75  ? 34.212 -2.316  -5.347  1.00 12.95 ?  75  LEU   A C    1 
ATOM   1577 O O    . LEU   A 1 75  ? 34.073 -1.605  -6.345  1.00 14.29 ?  75  LEU   A O    1 
ATOM   1578 C CB   . LEU   A 1 75  ? 33.408 -1.847  -3.036  1.00 12.85 ?  75  LEU   A CB   1 
ATOM   1579 C CG   . LEU   A 1 75  ? 33.616 -1.438  -1.583  1.00 14.38 ?  75  LEU   A CG   1 
ATOM   1580 C CD1  . LEU   A 1 75  ? 32.329 -1.613  -0.788  1.00 16.17 ?  75  LEU   A CD1  1 
ATOM   1581 C CD2  . LEU   A 1 75  ? 34.749 -2.174  -0.925  1.00 17.22 ?  75  LEU   A CD2  1 
ATOM   1582 H H    . LEU   A 1 75  ? 34.445 0.222   -3.827  1.00 15.39 ?  75  LEU   A H    1 
ATOM   1583 H HA   . LEU   A 1 75  ? 35.340 -2.249  -3.635  1.00 15.02 ?  75  LEU   A HA   1 
ATOM   1584 H HB2  . LEU   A 1 75  ? 32.692 -1.301  -3.389  1.00 15.45 ?  75  LEU   A HB2  1 
ATOM   1585 H HB3  . LEU   A 1 75  ? 33.125 -2.778  -3.031  1.00 15.45 ?  75  LEU   A HB3  1 
ATOM   1586 H HG   . LEU   A 1 75  ? 33.851 -0.492  -1.564  1.00 17.29 ?  75  LEU   A HG   1 
ATOM   1587 H HD11 . LEU   A 1 75  ? 32.487 -1.339  0.130   1.00 19.44 ?  75  LEU   A HD11 1 
ATOM   1588 H HD12 . LEU   A 1 75  ? 31.642 -1.054  -1.185  1.00 19.44 ?  75  LEU   A HD12 1 
ATOM   1589 H HD13 . LEU   A 1 75  ? 32.066 -2.541  -0.820  1.00 19.44 ?  75  LEU   A HD13 1 
ATOM   1590 H HD21 . LEU   A 1 75  ? 34.805 -1.907  0.007   1.00 20.70 ?  75  LEU   A HD21 1 
ATOM   1591 H HD22 . LEU   A 1 75  ? 34.584 -3.128  -0.986  1.00 20.70 ?  75  LEU   A HD22 1 
ATOM   1592 H HD23 . LEU   A 1 75  ? 35.583 -1.956  -1.377  1.00 20.70 ?  75  LEU   A HD23 1 
ATOM   1593 N N    . LYS   A 1 76  ? 34.051 -3.641  -5.369  1.00 13.34 ?  76  LYS   A N    1 
ATOM   1594 C CA   . LYS   A 1 76  ? 33.451 -4.354  -6.490  1.00 14.10 ?  76  LYS   A CA   1 
ATOM   1595 C C    . LYS   A 1 76  ? 31.937 -4.430  -6.300  1.00 12.65 ?  76  LYS   A C    1 
ATOM   1596 O O    . LYS   A 1 76  ? 31.450 -4.542  -5.176  1.00 12.75 ?  76  LYS   A O    1 
ATOM   1597 C CB   . LYS   A 1 76  ? 33.989 -5.794  -6.552  1.00 15.77 ?  76  LYS   A CB   1 
ATOM   1598 C CG   . LYS   A 1 76  ? 35.500 -5.907  -6.720  1.00 17.17 ?  76  LYS   A CG   1 
ATOM   1599 C CD   . LYS   A 1 76  ? 36.000 -7.325  -6.556  1.00 18.51 ?  76  LYS   A CD   1 
ATOM   1600 C CE   . LYS   A 1 76  ? 37.506 -7.390  -6.715  1.00 20.77 ?  76  LYS   A CE   1 
ATOM   1601 N NZ   . LYS   A 1 76  ? 38.043 -8.748  -6.509  1.00 21.33 ?  76  LYS   A NZ   1 
ATOM   1602 H H    . LYS   A 1 76  ? 34.289 -4.162  -4.725  1.00 16.04 ?  76  LYS   A H    1 
ATOM   1603 H HA   . LYS   A 1 76  ? 33.654 -3.898  -7.326  1.00 16.95 ?  76  LYS   A HA   1 
ATOM   1604 H HB2  . LYS   A 1 76  ? 33.751 -6.244  -5.730  1.00 18.95 ?  76  LYS   A HB2  1 
ATOM   1605 H HB3  . LYS   A 1 76  ? 33.577 -6.242  -7.306  1.00 18.95 ?  76  LYS   A HB3  1 
ATOM   1606 H HG2  . LYS   A 1 76  ? 35.744 -5.599  -7.608  1.00 20.63 ?  76  LYS   A HG2  1 
ATOM   1607 H HG3  . LYS   A 1 76  ? 35.936 -5.355  -6.049  1.00 20.63 ?  76  LYS   A HG3  1 
ATOM   1608 H HD2  . LYS   A 1 76  ? 35.766 -7.651  -5.672  1.00 22.23 ?  76  LYS   A HD2  1 
ATOM   1609 H HD3  . LYS   A 1 76  ? 35.594 -7.890  -7.238  1.00 22.23 ?  76  LYS   A HD3  1 
ATOM   1610 H HE2  . LYS   A 1 76  ? 37.741 -7.104  -7.610  1.00 24.96 ?  76  LYS   A HE2  1 
ATOM   1611 H HE3  . LYS   A 1 76  ? 37.914 -6.803  -6.059  1.00 24.96 ?  76  LYS   A HE3  1 
ATOM   1612 H HZ1  . LYS   A 1 76  ? 38.926 -8.750  -6.609  1.00 25.63 ?  76  LYS   A HZ1  1 
ATOM   1613 H HZ2  . LYS   A 1 76  ? 37.845 -9.039  -5.689  1.00 25.63 ?  76  LYS   A HZ2  1 
ATOM   1614 H HZ3  . LYS   A 1 76  ? 37.686 -9.313  -7.103  1.00 25.63 ?  76  LYS   A HZ3  1 
ATOM   1615 N N    . VAL   A 1 77  ? 31.195 -4.400  -7.411  1.00 13.14 ?  77  VAL   A N    1 
ATOM   1616 C CA   . VAL   A 1 77  ? 29.788 -4.784  -7.337  1.00 13.31 ?  77  VAL   A CA   1 
ATOM   1617 C C    . VAL   A 1 77  ? 29.716 -6.235  -6.892  1.00 13.22 ?  77  VAL   A C    1 
ATOM   1618 O O    . VAL   A 1 77  ? 30.371 -7.110  -7.471  1.00 13.11 ?  77  VAL   A O    1 
ATOM   1619 C CB   . VAL   A 1 77  ? 29.077 -4.566  -8.681  1.00 14.31 ?  77  VAL   A CB   1 
ATOM   1620 C CG1  . VAL   A 1 77  ? 27.616 -4.990  -8.581  1.00 15.35 ?  77  VAL   A CG1  1 
ATOM   1621 C CG2  . VAL   A 1 77  ? 29.168 -3.109  -9.103  1.00 15.90 ?  77  VAL   A CG2  1 
ATOM   1622 H H    . VAL   A 1 77  ? 31.480 -4.169  -8.191  1.00 15.79 ?  77  VAL   A H    1 
ATOM   1623 H HA   . VAL   A 1 77  ? 29.350 -4.242  -6.669  1.00 16.00 ?  77  VAL   A HA   1 
ATOM   1624 H HB   . VAL   A 1 77  ? 29.506 -5.102  -9.365  1.00 17.20 ?  77  VAL   A HB   1 
ATOM   1625 H HG11 . VAL   A 1 77  ? 27.152 -4.708  -9.383  1.00 18.45 ?  77  VAL   A HG11 1 
ATOM   1626 H HG12 . VAL   A 1 77  ? 27.572 -5.954  -8.493  1.00 18.45 ?  77  VAL   A HG12 1 
ATOM   1627 H HG13 . VAL   A 1 77  ? 27.220 -4.566  -7.803  1.00 18.45 ?  77  VAL   A HG13 1 
ATOM   1628 H HG21 . VAL   A 1 77  ? 28.669 -2.985  -9.926  1.00 19.11 ?  77  VAL   A HG21 1 
ATOM   1629 H HG22 . VAL   A 1 77  ? 28.791 -2.552  -8.402  1.00 19.11 ?  77  VAL   A HG22 1 
ATOM   1630 H HG23 . VAL   A 1 77  ? 30.099 -2.873  -9.244  1.00 19.11 ?  77  VAL   A HG23 1 
ATOM   1631 N N    . GLY   A 1 78  ? 28.927 -6.499  -5.850  1.00 12.57 ?  78  GLY   A N    1 
ATOM   1632 C CA   . GLY   A 1 78  ? 28.908 -7.788  -5.196  1.00 12.73 ?  78  GLY   A CA   1 
ATOM   1633 C C    . GLY   A 1 78  ? 29.818 -7.886  -3.991  1.00 12.32 ?  78  GLY   A C    1 
ATOM   1634 O O    . GLY   A 1 78  ? 29.750 -8.891  -3.267  1.00 12.86 ?  78  GLY   A O    1 
ATOM   1635 H H    . GLY   A 1 78  ? 28.378 -5.926  -5.510  1.00 15.12 ?  78  GLY   A H    1 
ATOM   1636 H HA2  . GLY   A 1 78  ? 28.002 -7.982  -4.910  1.00 15.31 ?  78  GLY   A HA2  1 
ATOM   1637 H HA3  . GLY   A 1 78  ? 29.172 -8.469  -5.836  1.00 15.31 ?  78  GLY   A HA3  1 
ATOM   1638 N N    . GLY   A 1 79  ? 30.667 -6.879  -3.757  1.00 12.07 ?  79  GLY   A N    1 
ATOM   1639 C CA   . GLY   A 1 79  ? 31.624 -6.904  -2.676  1.00 12.47 ?  79  GLY   A CA   1 
ATOM   1640 C C    . GLY   A 1 79  ? 31.179 -6.105  -1.464  1.00 11.78 ?  79  GLY   A C    1 
ATOM   1641 O O    . GLY   A 1 79  ? 30.061 -5.595  -1.389  1.00 12.81 ?  79  GLY   A O    1 
ATOM   1642 H H    . GLY   A 1 79  ? 30.706 -6.163  -4.238  1.00 14.51 ?  79  GLY   A H    1 
ATOM   1643 H HA2  . GLY   A 1 79  ? 31.768 -7.827  -2.404  1.00 15.00 ?  79  GLY   A HA2  1 
ATOM   1644 H HA3  . GLY   A 1 79  ? 32.468 -6.548  -2.992  1.00 15.00 ?  79  GLY   A HA3  1 
ATOM   1645 N N    . SER   A 1 80  ? 32.087 -6.001  -0.496  1.00 12.61 ?  80  SER   A N    1 
ATOM   1646 C CA   . SER   A 1 80  ? 31.771 -5.367  0.774   1.00 12.17 ?  80  SER   A CA   1 
ATOM   1647 C C    . SER   A 1 80  ? 33.043 -4.920  1.471   1.00 12.16 ?  80  SER   A C    1 
ATOM   1648 O O    . SER   A 1 80  ? 34.153 -5.353  1.138   1.00 13.71 ?  80  SER   A O    1 
ATOM   1649 C CB   . SER   A 1 80  ? 31.003 -6.328  1.691   1.00 13.53 ?  80  SER   A CB   1 
ATOM   1650 O OG   . SER   A 1 80  ? 31.834 -7.384  2.166   1.00 14.82 ?  80  SER   A OG   1 
ATOM   1651 H H    . SER   A 1 80  ? 32.899 -6.279  -0.561  1.00 15.16 ?  80  SER   A H    1 
ATOM   1652 H HA   . SER   A 1 80  ? 31.219 -4.588  0.596   1.00 14.63 ?  80  SER   A HA   1 
ATOM   1653 H HB2  . SER   A 1 80  ? 30.664 -5.824  2.447   1.00 16.27 ?  80  SER   A HB2  1 
ATOM   1654 H HB3  . SER   A 1 80  ? 30.262 -6.708  1.192   1.00 16.27 ?  80  SER   A HB3  1 
ATOM   1655 H HG   . SER   A 1 80  ? 32.133 -7.819  1.513   1.00 17.81 ?  80  SER   A HG   1 
ATOM   1656 N N    . CYS   A 1 81  ? 32.859 -4.076  2.483   1.00 11.94 ?  81  CYS   A N    1 
ATOM   1657 C CA   . CYS   A 1 81  ? 33.915 -3.789  3.440   1.00 12.11 ?  81  CYS   A CA   1 
ATOM   1658 C C    . CYS   A 1 81  ? 33.274 -3.558  4.801   1.00 11.97 ?  81  CYS   A C    1 
ATOM   1659 O O    . CYS   A 1 81  ? 32.107 -3.166  4.896   1.00 12.89 ?  81  CYS   A O    1 
ATOM   1660 C CB   . CYS   A 1 81  ? 34.777 -2.590  3.017   1.00 12.91 ?  81  CYS   A CB   1 
ATOM   1661 S SG   . CYS   A 1 81  ? 33.888 -1.022  3.048   1.00 13.15 ?  81  CYS   A SG   1 
ATOM   1662 H H    . CYS   A 1 81  ? 32.122 -3.658  2.643   1.00 14.35 ?  81  CYS   A H    1 
ATOM   1663 H HA   . CYS   A 1 81  ? 34.498 -4.562  3.510   1.00 14.56 ?  81  CYS   A HA   1 
ATOM   1664 H HB2  . CYS   A 1 81  ? 35.536 -2.522  3.625   1.00 15.52 ?  81  CYS   A HB2  1 
ATOM   1665 H HB3  . CYS   A 1 81  ? 35.100 -2.739  2.113   1.00 15.52 ?  81  CYS   A HB3  1 
ATOM   1666 H HG   . CYS   A 1 81  ? 34.631 -0.145  2.711   1.00 15.81 ?  81  CYS   A HG   1 
ATOM   1667 N N    . VAL   A 1 82  ? 34.044 -3.819  5.853   1.00 12.14 ?  82  VAL   A N    1 
ATOM   1668 C CA   . VAL   A 1 82  ? 33.623 -3.577  7.226   1.00 12.72 ?  82  VAL   A CA   1 
ATOM   1669 C C    . VAL   A 1 82  ? 34.223 -2.263  7.697   1.00 13.01 ?  82  VAL   A C    1 
ATOM   1670 O O    . VAL   A 1 82  ? 35.449 -2.093  7.688   1.00 13.86 ?  82  VAL   A O    1 
ATOM   1671 C CB   . VAL   A 1 82  ? 34.049 -4.718  8.158   1.00 13.86 ?  82  VAL   A CB   1 
ATOM   1672 C CG1  . VAL   A 1 82  ? 33.609 -4.422  9.579   1.00 15.55 ?  82  VAL   A CG1  1 
ATOM   1673 C CG2  . VAL   A 1 82  ? 33.491 -6.045  7.676   1.00 15.22 ?  82  VAL   A CG2  1 
ATOM   1674 H H    . VAL   A 1 82  ? 34.839 -4.160  5.792   1.00 14.60 ?  82  VAL   A H    1 
ATOM   1675 H HA   . VAL   A 1 82  ? 32.656 -3.500  7.251   1.00 15.30 ?  82  VAL   A HA   1 
ATOM   1676 H HB   . VAL   A 1 82  ? 35.015 -4.778  8.152   1.00 16.67 ?  82  VAL   A HB   1 
ATOM   1677 H HG11 . VAL   A 1 82  ? 33.690 -5.231  10.106  1.00 18.68 ?  82  VAL   A HG11 1 
ATOM   1678 H HG12 . VAL   A 1 82  ? 34.174 -3.727  9.951   1.00 18.68 ?  82  VAL   A HG12 1 
ATOM   1679 H HG13 . VAL   A 1 82  ? 32.684 -4.127  9.569   1.00 18.68 ?  82  VAL   A HG13 1 
ATOM   1680 H HG21 . VAL   A 1 82  ? 33.734 -6.735  8.313   1.00 18.29 ?  82  VAL   A HG21 1 
ATOM   1681 H HG22 . VAL   A 1 82  ? 32.525 -5.977  7.613   1.00 18.29 ?  82  VAL   A HG22 1 
ATOM   1682 H HG23 . VAL   A 1 82  ? 33.867 -6.249  6.806   1.00 18.29 ?  82  VAL   A HG23 1 
ATOM   1683 N N    . LEU   A 1 83  ? 33.363 -1.339  8.116   1.00 12.29 ?  83  LEU   A N    1 
ATOM   1684 C CA   . LEU   A 1 83  ? 33.783 -0.074  8.694   1.00 12.49 ?  83  LEU   A CA   1 
ATOM   1685 C C    . LEU   A 1 83  ? 33.067 0.103   10.028  1.00 12.66 ?  83  LEU   A C    1 
ATOM   1686 O O    . LEU   A 1 83  ? 32.347 -0.787  10.497  1.00 13.36 ?  83  LEU   A O    1 
ATOM   1687 C CB   . LEU   A 1 83  ? 33.530 1.084   7.718   1.00 12.81 ?  83  LEU   A CB   1 
ATOM   1688 C CG   . LEU   A 1 83  ? 34.435 1.086   6.482   1.00 13.53 ?  83  LEU   A CG   1 
ATOM   1689 C CD1  . LEU   A 1 83  ? 33.993 2.127   5.470   1.00 13.65 ?  83  LEU   A CD1  1 
ATOM   1690 C CD2  . LEU   A 1 83  ? 35.903 1.323   6.868   1.00 14.11 ?  83  LEU   A CD2  1 
ATOM   1691 H H    . LEU   A 1 83  ? 32.509 -1.430  8.071   1.00 14.77 ?  83  LEU   A H    1 
ATOM   1692 H HA   . LEU   A 1 83  ? 34.735 -0.109  8.870   1.00 15.02 ?  83  LEU   A HA   1 
ATOM   1693 H HB2  . LEU   A 1 83  ? 32.616 1.040   7.403   1.00 15.40 ?  83  LEU   A HB2  1 
ATOM   1694 H HB3  . LEU   A 1 83  ? 33.676 1.923   8.183   1.00 15.40 ?  83  LEU   A HB3  1 
ATOM   1695 H HG   . LEU   A 1 83  ? 34.388 0.218   6.054   1.00 16.27 ?  83  LEU   A HG   1 
ATOM   1696 H HD11 . LEU   A 1 83  ? 34.591 2.092   4.702   1.00 16.40 ?  83  LEU   A HD11 1 
ATOM   1697 H HD12 . LEU   A 1 83  ? 33.089 1.927   5.194   1.00 16.40 ?  83  LEU   A HD12 1 
ATOM   1698 H HD13 . LEU   A 1 83  ? 34.036 3.003   5.880   1.00 16.40 ?  83  LEU   A HD13 1 
ATOM   1699 H HD21 . LEU   A 1 83  ? 36.428 1.473   6.061   1.00 16.96 ?  83  LEU   A HD21 1 
ATOM   1700 H HD22 . LEU   A 1 83  ? 35.961 2.105   7.441   1.00 16.96 ?  83  LEU   A HD22 1 
ATOM   1701 H HD23 . LEU   A 1 83  ? 36.243 0.545   7.337   1.00 16.96 ?  83  LEU   A HD23 1 
ATOM   1702 N N    . SER   A 1 84  ? 33.278 1.257   10.657  1.00 13.24 ?  84  SER   A N    1 
ATOM   1703 C CA   . SER   A 1 84  ? 32.644 1.513   11.941  1.00 13.69 ?  84  SER   A CA   1 
ATOM   1704 C C    . SER   A 1 84  ? 31.125 1.609   11.799  1.00 13.24 ?  84  SER   A C    1 
ATOM   1705 O O    . SER   A 1 84  ? 30.601 2.077   10.788  1.00 13.37 ?  84  SER   A O    1 
ATOM   1706 C CB   . SER   A 1 84  ? 33.157 2.828   12.521  1.00 14.58 ?  84  SER   A CB   1 
ATOM   1707 O OG   . SER   A 1 84  ? 32.527 3.107   13.755  1.00 15.58 ?  84  SER   A OG   1 
ATOM   1708 H H    . SER   A 1 84  ? 33.782 1.894   10.363  1.00 15.91 ?  84  SER   A H    1 
ATOM   1709 H HA   . SER   A 1 84  ? 32.865 0.795   12.555  1.00 16.45 ?  84  SER   A HA   1 
ATOM   1710 H HB2  . SER   A 1 84  ? 34.116 2.762   12.661  1.00 17.52 ?  84  SER   A HB2  1 
ATOM   1711 H HB3  . SER   A 1 84  ? 32.966 3.545   11.894  1.00 17.52 ?  84  SER   A HB3  1 
ATOM   1712 H HG   . SER   A 1 84  ? 32.812 3.835   14.064  1.00 18.73 ?  84  SER   A HG   1 
ATOM   1713 N N    . GLY   A 1 85  ? 30.419 1.193   12.852  1.00 14.06 ?  85  GLY   A N    1 
ATOM   1714 C CA   . GLY   A 1 85  ? 28.996 1.432   12.957  1.00 14.59 ?  85  GLY   A CA   1 
ATOM   1715 C C    . GLY   A 1 85  ? 28.643 2.746   13.616  1.00 14.53 ?  85  GLY   A C    1 
ATOM   1716 O O    . GLY   A 1 85  ? 27.454 3.069   13.744  1.00 15.21 ?  85  GLY   A O    1 
ATOM   1717 H H    . GLY   A 1 85  ? 30.753 0.765   13.521  1.00 16.90 ?  85  GLY   A H    1 
ATOM   1718 H HA2  . GLY   A 1 85  ? 28.611 1.420   12.066  1.00 17.54 ?  85  GLY   A HA2  1 
ATOM   1719 H HA3  . GLY   A 1 85  ? 28.593 0.720   13.470  1.00 17.54 ?  85  GLY   A HA3  1 
ATOM   1720 N N    . HIS   A 1 86  ? 29.643 3.508   14.052  1.00 14.07 ?  86  HIS   A N    1 
ATOM   1721 C CA   . HIS   A 1 86  ? 29.436 4.846   14.622  1.00 14.45 ?  86  HIS   A CA   1 
ATOM   1722 C C    . HIS   A 1 86  ? 28.459 4.724   15.785  1.00 15.18 ?  86  HIS   A C    1 
ATOM   1723 O O    . HIS   A 1 86  ? 28.640 3.838   16.636  1.00 16.18 ?  86  HIS   A O    1 
ATOM   1724 C CB   . HIS   A 1 86  ? 29.053 5.830   13.526  1.00 14.57 ?  86  HIS   A CB   1 
ATOM   1725 C CG   . HIS   A 1 86  ? 30.097 5.934   12.472  1.00 14.36 ?  86  HIS   A CG   1 
ATOM   1726 N ND1  . HIS   A 1 86  ? 31.191 6.764   12.593  1.00 15.55 ?  86  HIS   A ND1  1 
ATOM   1727 C CD2  . HIS   A 1 86  ? 30.259 5.254   11.315  1.00 14.29 ?  86  HIS   A CD2  1 
ATOM   1728 C CE1  . HIS   A 1 86  ? 31.969 6.605   11.537  1.00 15.05 ?  86  HIS   A CE1  1 
ATOM   1729 N NE2  . HIS   A 1 86  ? 31.435 5.683   10.756  1.00 14.58 ?  86  HIS   A NE2  1 
ATOM   1730 H H    . HIS   A 1 86  ? 30.466 3.272   14.039  1.00 16.91 ?  86  HIS   A H    1 
ATOM   1731 H HA   . HIS   A 1 86  ? 30.277 5.152   14.991  1.00 17.37 ?  86  HIS   A HA   1 
ATOM   1732 H HB2  . HIS   A 1 86  ? 28.226 5.540   13.106  1.00 17.52 ?  86  HIS   A HB2  1 
ATOM   1733 H HB3  . HIS   A 1 86  ? 28.929 6.715   13.914  1.00 17.52 ?  86  HIS   A HB3  1 
ATOM   1734 H HD2  . HIS   A 1 86  ? 29.689 4.600   10.971  1.00 17.18 ?  86  HIS   A HD2  1 
ATOM   1735 H HE1  . HIS   A 1 86  ? 32.762 7.061   11.365  1.00 18.08 ?  86  HIS   A HE1  1 
ATOM   1736 H HE2  . HIS   A 1 86  ? 31.756 5.416   9.998   1.00 17.52 ?  86  HIS   A HE2  1 
ATOM   1737 N N    . ASN   A 1 87  ? 27.445 5.572   15.864  1.00 16.26 ?  87  ASN   A N    1 
ATOM   1738 C CA   . ASN   A 1 87  ? 26.480 5.570   16.947  1.00 17.29 ?  87  ASN   A CA   1 
ATOM   1739 C C    . ASN   A 1 87  ? 25.344 4.583   16.727  1.00 18.21 ?  87  ASN   A C    1 
ATOM   1740 O O    . ASN   A 1 87  ? 24.444 4.514   17.566  1.00 20.33 ?  87  ASN   A O    1 
ATOM   1741 C CB   . ASN   A 1 87  ? 25.899 6.981   17.103  1.00 17.73 ?  87  ASN   A CB   1 
ATOM   1742 C CG   . ASN   A 1 87  ? 25.381 7.553   15.787  1.00 18.52 ?  87  ASN   A CG   1 
ATOM   1743 O OD1  . ASN   A 1 87  ? 26.031 7.452   14.749  1.00 18.87 ?  87  ASN   A OD1  1 
ATOM   1744 N ND2  . ASN   A 1 87  ? 24.207 8.161   15.831  1.00 19.81 ?  87  ASN   A ND2  1 
ATOM   1745 H H    . ASN   A 1 87  ? 27.289 6.178   15.280  1.00 19.54 ?  87  ASN   A H    1 
ATOM   1746 H HA   . ASN   A 1 87  ? 26.918 5.327   17.779  1.00 20.77 ?  87  ASN   A HA   1 
ATOM   1747 H HB2  . ASN   A 1 87  ? 25.159 6.951   17.734  1.00 21.31 ?  87  ASN   A HB2  1 
ATOM   1748 H HB3  . ASN   A 1 87  ? 26.593 7.570   17.437  1.00 21.31 ?  87  ASN   A HB3  1 
ATOM   1749 H HD21 . ASN   A 1 87  ? 23.874 8.493   15.113  1.00 23.80 ?  87  ASN   A HD21 1 
ATOM   1750 H HD22 . ASN   A 1 87  ? 23.781 8.221   16.575  1.00 23.80 ?  87  ASN   A HD22 1 
ATOM   1751 N N    A LEU   A 1 88  ? 25.381 3.805   15.647  0.60 17.04 ?  88  LEU   A N    1 
ATOM   1752 N N    B LEU   A 1 88  ? 25.367 3.811   15.642  0.40 17.37 ?  88  LEU   A N    1 
ATOM   1753 C CA   A LEU   A 1 88  ? 24.264 2.952   15.252  0.60 16.71 ?  88  LEU   A CA   1 
ATOM   1754 C CA   B LEU   A 1 88  ? 24.248 2.951   15.273  0.40 17.15 ?  88  LEU   A CA   1 
ATOM   1755 C C    A LEU   A 1 88  ? 24.483 1.476   15.554  0.60 16.77 ?  88  LEU   A C    1 
ATOM   1756 C C    B LEU   A 1 88  ? 24.481 1.472   15.544  0.40 16.92 ?  88  LEU   A C    1 
ATOM   1757 O O    A LEU   A 1 88  ? 23.511 0.752   15.790  0.60 17.69 ?  88  LEU   A O    1 
ATOM   1758 O O    B LEU   A 1 88  ? 23.514 0.740   15.762  0.40 17.54 ?  88  LEU   A O    1 
ATOM   1759 C CB   A LEU   A 1 88  ? 24.015 3.096   13.748  0.60 17.09 ?  88  LEU   A CB   1 
ATOM   1760 C CB   B LEU   A 1 88  ? 23.919 3.131   13.787  0.40 17.59 ?  88  LEU   A CB   1 
ATOM   1761 C CG   A LEU   A 1 88  ? 23.708 4.496   13.212  0.60 18.25 ?  88  LEU   A CG   1 
ATOM   1762 C CG   B LEU   A 1 88  ? 23.624 4.570   13.357  0.40 18.24 ?  88  LEU   A CG   1 
ATOM   1763 C CD1  A LEU   A 1 88  ? 23.561 4.456   11.700  0.60 18.74 ?  88  LEU   A CD1  1 
ATOM   1764 C CD1  B LEU   A 1 88  ? 23.452 4.653   11.850  0.40 18.37 ?  88  LEU   A CD1  1 
ATOM   1765 C CD2  A LEU   A 1 88  ? 22.452 5.061   13.859  0.60 19.50 ?  88  LEU   A CD2  1 
ATOM   1766 C CD2  B LEU   A 1 88  ? 22.390 5.107   14.071  0.40 18.94 ?  88  LEU   A CD2  1 
ATOM   1767 H H    A LEU   A 1 88  ? 26.062 3.741   15.129  0.60 20.48 ?  88  LEU   A H    1 
ATOM   1768 H H    B LEU   A 1 88  ? 26.033 3.765   15.102  0.40 20.88 ?  88  LEU   A H    1 
ATOM   1769 H HA   A LEU   A 1 88  ? 23.465 3.239   15.717  0.60 20.08 ?  88  LEU   A HA   1 
ATOM   1770 H HA   B LEU   A 1 88  ? 23.467 3.223   15.778  0.40 20.60 ?  88  LEU   A HA   1 
ATOM   1771 H HB2  A LEU   A 1 88  ? 24.804 2.785   13.282  0.60 20.54 ?  88  LEU   A HB2  1 
ATOM   1772 H HB2  B LEU   A 1 88  ? 24.671 2.820   13.261  0.40 21.14 ?  88  LEU   A HB2  1 
ATOM   1773 H HB3  A LEU   A 1 88  ? 23.261 2.535   13.515  0.60 20.54 ?  88  LEU   A HB3  1 
ATOM   1774 H HB3  B LEU   A 1 88  ? 23.134 2.600   13.576  0.40 21.14 ?  88  LEU   A HB3  1 
ATOM   1775 H HG   A LEU   A 1 88  ? 24.445 5.089   13.423  0.60 21.92 ?  88  LEU   A HG   1 
ATOM   1776 H HG   B LEU   A 1 88  ? 24.376 5.132   13.598  0.40 21.91 ?  88  LEU   A HG   1 
ATOM   1777 H HD11 A LEU   A 1 88  ? 23.385 5.353   11.373  0.60 22.51 ?  88  LEU   A HD11 1 
ATOM   1778 H HD11 B LEU   A 1 88  ? 23.271 5.573   11.601  0.40 22.08 ?  88  LEU   A HD11 1 
ATOM   1779 H HD12 A LEU   A 1 88  ? 24.383 4.118   11.311  0.60 22.51 ?  88  LEU   A HD12 1 
ATOM   1780 H HD12 B LEU   A 1 88  ? 24.268 4.350   11.421  0.40 22.08 ?  88  LEU   A HD12 1 
ATOM   1781 H HD13 A LEU   A 1 88  ? 22.821 3.871   11.470  0.60 22.51 ?  88  LEU   A HD13 1 
ATOM   1782 H HD13 B LEU   A 1 88  ? 22.710 4.087   11.584  0.40 22.08 ?  88  LEU   A HD13 1 
ATOM   1783 H HD21 A LEU   A 1 88  ? 22.240 5.913   13.445  0.60 23.43 ?  88  LEU   A HD21 1 
ATOM   1784 H HD21 B LEU   A 1 88  ? 22.163 5.973   13.698  0.40 22.75 ?  88  LEU   A HD21 1 
ATOM   1785 H HD22 A LEU   A 1 88  ? 21.722 4.437   13.726  0.60 23.43 ?  88  LEU   A HD22 1 
ATOM   1786 H HD22 B LEU   A 1 88  ? 21.656 4.487   13.940  0.40 22.75 ?  88  LEU   A HD22 1 
ATOM   1787 H HD23 A LEU   A 1 88  ? 22.615 5.184   14.806  0.60 23.43 ?  88  LEU   A HD23 1 
ATOM   1788 H HD23 B LEU   A 1 88  ? 22.587 5.194   15.016  0.40 22.75 ?  88  LEU   A HD23 1 
ATOM   1789 N N    . ALA   A 1 89  ? 25.730 1.020   15.532  1.00 16.29 ?  89  ALA   A N    1 
ATOM   1790 C CA   . ALA   A 1 89  ? 26.065 -0.390  15.662  1.00 15.95 ?  89  ALA   A CA   1 
ATOM   1791 C C    . ALA   A 1 89  ? 27.554 -0.452  15.954  1.00 16.61 ?  89  ALA   A C    1 
ATOM   1792 O O    . ALA   A 1 89  ? 28.265 0.544   15.817  1.00 17.15 ?  89  ALA   A O    1 
ATOM   1793 C CB   . ALA   A 1 89  ? 25.775 -1.123  14.355  1.00 15.67 ?  89  ALA   A CB   1 
ATOM   1794 H H    A ALA   A 1 89  ? 26.417 1.526   15.432  0.60 19.58 ?  89  ALA   A H    1 
ATOM   1795 H H    B ALA   A 1 89  ? 26.417 1.528   15.437  0.40 19.58 ?  89  ALA   A H    1 
ATOM   1796 H HA   . ALA   A 1 89  ? 25.562 -0.794  16.389  1.00 19.17 ?  89  ALA   A HA   1 
ATOM   1797 H HB1  . ALA   A 1 89  ? 26.033 -2.055  14.454  1.00 18.83 ?  89  ALA   A HB1  1 
ATOM   1798 H HB2  . ALA   A 1 89  ? 24.826 -1.065  14.158  1.00 18.83 ?  89  ALA   A HB2  1 
ATOM   1799 H HB3  . ALA   A 1 89  ? 26.288 -0.714  13.642  1.00 18.83 ?  89  ALA   A HB3  1 
ATOM   1800 N N    . LYS   A 1 90  ? 28.037 -1.631  16.340  1.00 17.36 ?  90  LYS   A N    1 
ATOM   1801 C CA   . LYS   A 1 90  ? 29.481 -1.786  16.476  1.00 17.67 ?  90  LYS   A CA   1 
ATOM   1802 C C    . LYS   A 1 90  ? 30.167 -1.602  15.126  1.00 16.02 ?  90  LYS   A C    1 
ATOM   1803 O O    . LYS   A 1 90  ? 31.107 -0.801  14.991  1.00 17.61 ?  90  LYS   A O    1 
ATOM   1804 C CB   . LYS   A 1 90  ? 29.820 -3.147  17.084  1.00 21.01 ?  90  LYS   A CB   1 
ATOM   1805 C CG   . LYS   A 1 90  ? 31.304 -3.318  17.383  1.00 25.64 ?  90  LYS   A CG   1 
ATOM   1806 C CD   . LYS   A 1 90  ? 31.557 -4.559  18.226  1.00 29.84 ?  90  LYS   A CD   1 
ATOM   1807 C CE   . LYS   A 1 90  ? 32.972 -4.590  18.786  1.00 32.93 ?  90  LYS   A CE   1 
ATOM   1808 N NZ   . LYS   A 1 90  ? 33.968 -5.099  17.804  1.00 35.76 ?  90  LYS   A NZ   1 
ATOM   1809 H H    . LYS   A 1 90  ? 27.567 -2.323  16.522  1.00 20.85 ?  90  LYS   A H    1 
ATOM   1810 H HA   . LYS   A 1 90  ? 29.817 -1.100  17.071  1.00 21.23 ?  90  LYS   A HA   1 
ATOM   1811 H HB2  . LYS   A 1 90  ? 29.332 -3.248  17.919  1.00 25.25 ?  90  LYS   A HB2  1 
ATOM   1812 H HB3  . LYS   A 1 90  ? 29.556 -3.846  16.464  1.00 25.25 ?  90  LYS   A HB3  1 
ATOM   1813 H HG2  . LYS   A 1 90  ? 31.791 -3.411  16.549  1.00 30.80 ?  90  LYS   A HG2  1 
ATOM   1814 H HG3  . LYS   A 1 90  ? 31.622 -2.545  17.875  1.00 30.80 ?  90  LYS   A HG3  1 
ATOM   1815 H HD2  . LYS   A 1 90  ? 30.936 -4.572  18.972  1.00 35.84 ?  90  LYS   A HD2  1 
ATOM   1816 H HD3  . LYS   A 1 90  ? 31.432 -5.350  17.676  1.00 35.84 ?  90  LYS   A HD3  1 
ATOM   1817 H HE2  . LYS   A 1 90  ? 33.232 -3.690  19.038  1.00 39.55 ?  90  LYS   A HE2  1 
ATOM   1818 H HE3  . LYS   A 1 90  ? 32.992 -5.171  19.563  1.00 39.55 ?  90  LYS   A HE3  1 
ATOM   1819 H HZ1  . LYS   A 1 90  ? 34.774 -5.138  18.181  1.00 42.94 ?  90  LYS   A HZ1  1 
ATOM   1820 H HZ2  . LYS   A 1 90  ? 33.737 -5.915  17.533  1.00 42.94 ?  90  LYS   A HZ2  1 
ATOM   1821 H HZ3  . LYS   A 1 90  ? 34.004 -4.559  17.099  1.00 42.94 ?  90  LYS   A HZ3  1 
ATOM   1822 N N    . HIS   A 1 91  ? 29.687 -2.317  14.109  1.00 14.12 ?  91  HIS   A N    1 
ATOM   1823 C CA   . HIS   A 1 91  ? 30.256 -2.303  12.777  1.00 13.47 ?  91  HIS   A CA   1 
ATOM   1824 C C    . HIS   A 1 91  ? 29.168 -2.025  11.757  1.00 12.54 ?  91  HIS   A C    1 
ATOM   1825 O O    . HIS   A 1 91  ? 27.999 -2.371  11.959  1.00 13.58 ?  91  HIS   A O    1 
ATOM   1826 C CB   . HIS   A 1 91  ? 30.853 -3.666  12.400  1.00 16.53 ?  91  HIS   A CB   1 
ATOM   1827 C CG   . HIS   A 1 91  ? 31.884 -4.167  13.359  1.00 20.79 ?  91  HIS   A CG   1 
ATOM   1828 N ND1  . HIS   A 1 91  ? 33.165 -3.662  13.406  1.00 22.80 ?  91  HIS   A ND1  1 
ATOM   1829 C CD2  . HIS   A 1 91  ? 31.828 -5.140  14.299  1.00 22.61 ?  91  HIS   A CD2  1 
ATOM   1830 C CE1  . HIS   A 1 91  ? 33.853 -4.298  14.338  1.00 23.91 ?  91  HIS   A CE1  1 
ATOM   1831 N NE2  . HIS   A 1 91  ? 33.065 -5.201  14.894  1.00 24.03 ?  91  HIS   A NE2  1 
ATOM   1832 H H    . HIS   A 1 91  ? 29.010 -2.857  14.180  1.00 16.97 ?  91  HIS   A H    1 
ATOM   1833 H HA   . HIS   A 1 91  ? 30.943 -1.626  12.708  1.00 16.19 ?  91  HIS   A HA   1 
ATOM   1834 H HB2  . HIS   A 1 91  ? 30.141 -4.325  12.367  1.00 19.86 ?  91  HIS   A HB2  1 
ATOM   1835 H HB3  . HIS   A 1 91  ? 31.273 -3.596  11.528  1.00 19.86 ?  91  HIS   A HB3  1 
ATOM   1836 H HD1  . HIS   A 1 91  ? 33.470 -3.031  12.905  1.00 27.39 ?  91  HIS   A HD1  1 
ATOM   1837 H HD2  . HIS   A 1 91  ? 31.095 -5.667  14.507  1.00 27.16 ?  91  HIS   A HD2  1 
ATOM   1838 H HE1  . HIS   A 1 91  ? 34.745 -4.134  14.562  1.00 28.72 ?  91  HIS   A HE1  1 
ATOM   1839 N N    . CYS   A 1 92  ? 29.569 -1.434  10.639  1.00 12.36 ?  92  CYS   A N    1 
ATOM   1840 C CA   . CYS   A 1 92  ? 28.730 -1.355  9.450   1.00 12.30 ?  92  CYS   A CA   1 
ATOM   1841 C C    . CYS   A 1 92  ? 29.378 -2.178  8.344   1.00 12.20 ?  92  CYS   A C    1 
ATOM   1842 O O    . CYS   A 1 92  ? 30.536 -1.929  7.974   1.00 12.45 ?  92  CYS   A O    1 
ATOM   1843 C CB   . CYS   A 1 92  ? 28.525 0.090   8.985   1.00 12.99 ?  92  CYS   A CB   1 
ATOM   1844 S SG   . CYS   A 1 92  ? 27.497 0.196   7.476   1.00 12.59 ?  92  CYS   A SG   1 
ATOM   1845 H H    . CYS   A 1 92  ? 30.334 -1.050  10.547  1.00 14.86 ?  92  CYS   A H    1 
ATOM   1846 H HA   . CYS   A 1 92  ? 27.859 -1.733  9.648   1.00 14.79 ?  92  CYS   A HA   1 
ATOM   1847 H HB2  . CYS   A 1 92  ? 28.077 0.594   9.685   1.00 15.61 ?  92  CYS   A HB2  1 
ATOM   1848 H HB3  . CYS   A 1 92  ? 29.386 0.489   8.789   1.00 15.61 ?  92  CYS   A HB3  1 
ATOM   1849 H HG   . CYS   A 1 92  ? 27.365 1.347   7.177   1.00 15.13 ?  92  CYS   A HG   1 
ATOM   1850 N N    . LEU   A 1 93  ? 28.640 -3.163  7.835   1.00 12.16 ?  93  LEU   A N    1 
ATOM   1851 C CA   . LEU   A 1 93  ? 29.042 -3.918  6.653   1.00 11.52 ?  93  LEU   A CA   1 
ATOM   1852 C C    . LEU   A 1 93  ? 28.447 -3.229  5.431   1.00 11.26 ?  93  LEU   A C    1 
ATOM   1853 O O    . LEU   A 1 93  ? 27.232 -3.279  5.216   1.00 11.28 ?  93  LEU   A O    1 
ATOM   1854 C CB   . LEU   A 1 93  ? 28.547 -5.360  6.755   1.00 12.11 ?  93  LEU   A CB   1 
ATOM   1855 C CG   . LEU   A 1 93  ? 28.938 -6.269  5.590   1.00 12.50 ?  93  LEU   A CG   1 
ATOM   1856 C CD1  . LEU   A 1 93  ? 30.445 -6.536  5.579   1.00 13.47 ?  93  LEU   A CD1  1 
ATOM   1857 C CD2  . LEU   A 1 93  ? 28.165 -7.590  5.631   1.00 12.88 ?  93  LEU   A CD2  1 
ATOM   1858 H H    . LEU   A 1 93  ? 27.884 -3.411  8.169   1.00 14.62 ?  93  LEU   A H    1 
ATOM   1859 H HA   . LEU   A 1 93  ? 30.005 -3.914  6.580   1.00 13.85 ?  93  LEU   A HA   1 
ATOM   1860 H HB2  . LEU   A 1 93  ? 28.909 -5.747  7.568   1.00 14.56 ?  93  LEU   A HB2  1 
ATOM   1861 H HB3  . LEU   A 1 93  ? 27.579 -5.349  6.806   1.00 14.56 ?  93  LEU   A HB3  1 
ATOM   1862 H HG   . LEU   A 1 93  ? 28.719 -5.830  4.759   1.00 15.03 ?  93  LEU   A HG   1 
ATOM   1863 H HD11 . LEU   A 1 93  ? 30.659 -7.153  4.862   1.00 16.19 ?  93  LEU   A HD11 1 
ATOM   1864 H HD12 . LEU   A 1 93  ? 30.918 -5.699  5.447   1.00 16.19 ?  93  LEU   A HD12 1 
ATOM   1865 H HD13 . LEU   A 1 93  ? 30.708 -6.927  6.434   1.00 16.19 ?  93  LEU   A HD13 1 
ATOM   1866 H HD21 . LEU   A 1 93  ? 28.445 -8.138  4.879   1.00 15.49 ?  93  LEU   A HD21 1 
ATOM   1867 H HD22 . LEU   A 1 93  ? 28.361 -8.044  6.463   1.00 15.49 ?  93  LEU   A HD22 1 
ATOM   1868 H HD23 . LEU   A 1 93  ? 27.219 -7.397  5.567   1.00 15.49 ?  93  LEU   A HD23 1 
ATOM   1869 N N    . HIS   A 1 94  ? 29.294 -2.537  4.664   1.00 10.76 ?  94  HIS   A N    1 
ATOM   1870 C CA   . HIS   A 1 94  ? 28.866 -1.865  3.438   1.00 11.03 ?  94  HIS   A CA   1 
ATOM   1871 C C    . HIS   A 1 94  ? 28.880 -2.897  2.324   1.00 10.97 ?  94  HIS   A C    1 
ATOM   1872 O O    . HIS   A 1 94  ? 29.943 -3.419  1.986   1.00 12.18 ?  94  HIS   A O    1 
ATOM   1873 C CB   . HIS   A 1 94  ? 29.817 -0.715  3.104   1.00 10.93 ?  94  HIS   A CB   1 
ATOM   1874 C CG   . HIS   A 1 94  ? 29.808 0.377   4.121   1.00 11.09 ?  94  HIS   A CG   1 
ATOM   1875 N ND1  . HIS   A 1 94  ? 28.929 1.442   4.073   1.00 11.24 ?  94  HIS   A ND1  1 
ATOM   1876 C CD2  . HIS   A 1 94  ? 30.548 0.541   5.240   1.00 11.75 ?  94  HIS   A CD2  1 
ATOM   1877 C CE1  . HIS   A 1 94  ? 29.147 2.220   5.118   1.00 11.68 ?  94  HIS   A CE1  1 
ATOM   1878 N NE2  . HIS   A 1 94  ? 30.124 1.698   5.839   1.00 11.37 ?  94  HIS   A NE2  1 
ATOM   1879 H H    . HIS   A 1 94  ? 30.133 -2.439  4.834   1.00 12.94 ?  94  HIS   A H    1 
ATOM   1880 H HA   . HIS   A 1 94  ? 27.963 -1.517  3.543   1.00 13.26 ?  94  HIS   A HA   1 
ATOM   1881 H HB2  . HIS   A 1 94  ? 30.715 -1.063  3.046   1.00 13.15 ?  94  HIS   A HB2  1 
ATOM   1882 H HB3  . HIS   A 1 94  ? 29.550 -0.329  2.253   1.00 13.15 ?  94  HIS   A HB3  1 
ATOM   1883 H HD2  . HIS   A 1 94  ? 31.229 -0.013  5.540   1.00 14.13 ?  94  HIS   A HD2  1 
ATOM   1884 H HE1  . HIS   A 1 94  ? 28.682 3.002   5.308   1.00 14.04 ?  94  HIS   A HE1  1 
ATOM   1885 H HE2  . HIS   A 1 94  ? 30.442 2.039   6.559   1.00 13.68 ?  94  HIS   A HE2  1 
ATOM   1886 N N    . VAL   A 1 95  ? 27.707 -3.221  1.777   1.00 10.16 ?  95  VAL   A N    1 
ATOM   1887 C CA   . VAL   A 1 95  ? 27.561 -4.258  0.759   1.00 10.59 ?  95  VAL   A CA   1 
ATOM   1888 C C    . VAL   A 1 95  ? 27.011 -3.625  -0.507  1.00 10.56 ?  95  VAL   A C    1 
ATOM   1889 O O    . VAL   A 1 95  ? 26.013 -2.895  -0.453  1.00 10.88 ?  95  VAL   A O    1 
ATOM   1890 C CB   . VAL   A 1 95  ? 26.630 -5.392  1.218   1.00 11.25 ?  95  VAL   A CB   1 
ATOM   1891 C CG1  . VAL   A 1 95  ? 26.525 -6.441  0.123   1.00 11.95 ?  95  VAL   A CG1  1 
ATOM   1892 C CG2  . VAL   A 1 95  ? 27.118 -5.996  2.514   1.00 11.81 ?  95  VAL   A CG2  1 
ATOM   1893 H H    . VAL   A 1 95  ? 26.961 -2.855  1.994   1.00 12.22 ?  95  VAL   A H    1 
ATOM   1894 H HA   . VAL   A 1 95  ? 28.428 -4.640  0.555   1.00 12.73 ?  95  VAL   A HA   1 
ATOM   1895 H HB   . VAL   A 1 95  ? 25.743 -5.034  1.364   1.00 13.53 ?  95  VAL   A HB   1 
ATOM   1896 H HG11 . VAL   A 1 95  ? 26.136 -7.249  0.493   1.00 14.37 ?  95  VAL   A HG11 1 
ATOM   1897 H HG12 . VAL   A 1 95  ? 25.961 -6.105  -0.594  1.00 14.37 ?  95  VAL   A HG12 1 
ATOM   1898 H HG13 . VAL   A 1 95  ? 27.413 -6.634  -0.221  1.00 14.37 ?  95  VAL   A HG13 1 
ATOM   1899 H HG21 . VAL   A 1 95  ? 26.550 -6.752  2.741   1.00 14.21 ?  95  VAL   A HG21 1 
ATOM   1900 H HG22 . VAL   A 1 95  ? 28.032 -6.287  2.405   1.00 14.21 ?  95  VAL   A HG22 1 
ATOM   1901 H HG23 . VAL   A 1 95  ? 27.060 -5.322  3.210   1.00 14.21 ?  95  VAL   A HG23 1 
ATOM   1902 N N    . VAL   A 1 96  ? 27.638 -3.916  -1.643  1.00 10.61 ?  96  VAL   A N    1 
ATOM   1903 C CA   . VAL   A 1 96  ? 27.231 -3.365  -2.927  1.00 10.92 ?  96  VAL   A CA   1 
ATOM   1904 C C    . VAL   A 1 96  ? 26.428 -4.412  -3.692  1.00 11.68 ?  96  VAL   A C    1 
ATOM   1905 O O    . VAL   A 1 96  ? 26.990 -5.362  -4.246  1.00 12.30 ?  96  VAL   A O    1 
ATOM   1906 C CB   . VAL   A 1 96  ? 28.428 -2.890  -3.748  1.00 11.52 ?  96  VAL   A CB   1 
ATOM   1907 C CG1  . VAL   A 1 96  ? 27.929 -2.250  -5.019  1.00 12.16 ?  96  VAL   A CG1  1 
ATOM   1908 C CG2  . VAL   A 1 96  ? 29.294 -1.928  -2.948  1.00 12.45 ?  96  VAL   A CG2  1 
ATOM   1909 H H    . VAL   A 1 96  ? 28.323 -4.446  -1.691  1.00 12.76 ?  96  VAL   A H    1 
ATOM   1910 H HA   . VAL   A 1 96  ? 26.658 -2.604  -2.768  1.00 13.13 ?  96  VAL   A HA   1 
ATOM   1911 H HB   . VAL   A 1 96  ? 28.972 -3.650  -3.991  1.00 13.86 ?  96  VAL   A HB   1 
ATOM   1912 H HG11 . VAL   A 1 96  ? 28.664 -1.763  -5.434  1.00 14.62 ?  96  VAL   A HG11 1 
ATOM   1913 H HG12 . VAL   A 1 96  ? 27.608 -2.933  -5.620  1.00 14.62 ?  96  VAL   A HG12 1 
ATOM   1914 H HG13 . VAL   A 1 96  ? 27.213 -1.628  -4.803  1.00 14.62 ?  96  VAL   A HG13 1 
ATOM   1915 H HG21 . VAL   A 1 96  ? 29.997 -1.581  -3.517  1.00 14.97 ?  96  VAL   A HG21 1 
ATOM   1916 H HG22 . VAL   A 1 96  ? 28.741 -1.197  -2.622  1.00 14.97 ?  96  VAL   A HG22 1 
ATOM   1917 H HG23 . VAL   A 1 96  ? 29.683 -2.403  -2.194  1.00 14.97 ?  96  VAL   A HG23 1 
ATOM   1918 N N    A GLY   A 1 97  ? 25.107 -4.258  -3.697  0.60 11.41 ?  97  GLY   A N    1 
ATOM   1919 N N    B GLY   A 1 97  ? 25.114 -4.222  -3.774  0.40 11.62 ?  97  GLY   A N    1 
ATOM   1920 C CA   A GLY   A 1 97  ? 24.274 -4.995  -4.610  0.60 12.34 ?  97  GLY   A CA   1 
ATOM   1921 C CA   B GLY   A 1 97  ? 24.305 -5.007  -4.672  0.40 12.26 ?  97  GLY   A CA   1 
ATOM   1922 C C    A GLY   A 1 97  ? 24.244 -4.296  -5.953  0.60 12.05 ?  97  GLY   A C    1 
ATOM   1923 C C    B GLY   A 1 97  ? 24.373 -4.468  -6.087  0.40 12.38 ?  97  GLY   A C    1 
ATOM   1924 O O    A GLY   A 1 97  ? 24.482 -3.089  -6.043  0.60 12.70 ?  97  GLY   A O    1 
ATOM   1925 O O    B GLY   A 1 97  ? 24.755 -3.315  -6.316  0.40 12.62 ?  97  GLY   A O    1 
ATOM   1926 H H    A GLY   A 1 97  ? 24.677 -3.717  -3.179  0.60 13.72 ?  97  GLY   A H    1 
ATOM   1927 H H    B GLY   A 1 97  ? 24.673 -3.638  -3.315  0.40 13.97 ?  97  GLY   A H    1 
ATOM   1928 H HA2  A GLY   A 1 97  ? 24.630 -5.882  -4.725  0.60 14.84 ?  97  GLY   A HA2  1 
ATOM   1929 H HA2  B GLY   A 1 97  ? 24.624 -5.920  -4.670  0.40 14.74 ?  97  GLY   A HA2  1 
ATOM   1930 H HA3  A GLY   A 1 97  ? 23.371 -5.047  -4.262  0.60 14.84 ?  97  GLY   A HA3  1 
ATOM   1931 H HA3  B GLY   A 1 97  ? 23.382 -4.995  -4.375  0.40 14.74 ?  97  GLY   A HA3  1 
ATOM   1932 N N    A PRO   A 1 98  ? 23.962 -5.038  -7.024  0.60 11.49 ?  98  PRO   A N    1 
ATOM   1933 N N    B PRO   A 1 98  ? 24.013 -5.292  -7.070  0.40 12.79 ?  98  PRO   A N    1 
ATOM   1934 C CA   A PRO   A 1 98  ? 23.856 -4.403  -8.341  0.60 11.59 ?  98  PRO   A CA   1 
ATOM   1935 C CA   B PRO   A 1 98  ? 24.009 -4.820  -8.459  0.40 13.72 ?  98  PRO   A CA   1 
ATOM   1936 C C    A PRO   A 1 98  ? 22.731 -3.382  -8.375  0.60 11.50 ?  98  PRO   A C    1 
ATOM   1937 C C    B PRO   A 1 98  ? 22.922 -3.784  -8.706  0.40 14.76 ?  98  PRO   A C    1 
ATOM   1938 O O    A PRO   A 1 98  ? 21.660 -3.586  -7.797  0.60 11.72 ?  98  PRO   A O    1 
ATOM   1939 O O    B PRO   A 1 98  ? 21.797 -3.898  -8.214  0.40 14.90 ?  98  PRO   A O    1 
ATOM   1940 C CB   A PRO   A 1 98  ? 23.574 -5.582  -9.281  0.60 11.95 ?  98  PRO   A CB   1 
ATOM   1941 C CB   B PRO   A 1 98  ? 23.752 -6.096  -9.269  0.40 13.76 ?  98  PRO   A CB   1 
ATOM   1942 C CG   A PRO   A 1 98  ? 22.957 -6.624  -8.400  0.60 12.13 ?  98  PRO   A CG   1 
ATOM   1943 C CG   B PRO   A 1 98  ? 23.058 -7.012  -8.312  0.40 13.86 ?  98  PRO   A CG   1 
ATOM   1944 C CD   A PRO   A 1 98  ? 23.672 -6.479  -7.082  0.60 11.84 ?  98  PRO   A CD   1 
ATOM   1945 C CD   B PRO   A 1 98  ? 23.668 -6.720  -6.971  0.40 13.17 ?  98  PRO   A CD   1 
ATOM   1946 H HA   A PRO   A 1 98  ? 24.689 -3.976  -8.581  0.60 13.93 ?  98  PRO   A HA   1 
ATOM   1947 H HA   B PRO   A 1 98  ? 24.873 -4.447  -8.701  0.40 16.49 ?  98  PRO   A HA   1 
ATOM   1948 H HB2  A PRO   A 1 98  ? 22.955 -5.310  -9.974  0.60 14.37 ?  98  PRO   A HB2  1 
ATOM   1949 H HB2  B PRO   A 1 98  ? 23.182 -5.894  -10.029 0.40 16.55 ?  98  PRO   A HB2  1 
ATOM   1950 H HB3  A PRO   A 1 98  ? 24.406 -5.900  -9.658  0.60 14.37 ?  98  PRO   A HB3  1 
ATOM   1951 H HB3  B PRO   A 1 98  ? 24.594 -6.475  -9.562  0.40 16.55 ?  98  PRO   A HB3  1 
ATOM   1952 H HG2  A PRO   A 1 98  ? 22.008 -6.450  -8.294  0.60 14.58 ?  98  PRO   A HG2  1 
ATOM   1953 H HG2  B PRO   A 1 98  ? 22.110 -6.810  -8.302  0.40 16.66 ?  98  PRO   A HG2  1 
ATOM   1954 H HG3  A PRO   A 1 98  ? 23.109 -7.505  -8.772  0.60 14.58 ?  98  PRO   A HG3  1 
ATOM   1955 H HG3  B PRO   A 1 98  ? 23.212 -7.935  -8.569  0.40 16.66 ?  98  PRO   A HG3  1 
ATOM   1956 H HD2  A PRO   A 1 98  ? 23.095 -6.745  -6.345  0.60 14.24 ?  98  PRO   A HD2  1 
ATOM   1957 H HD2  B PRO   A 1 98  ? 23.020 -6.861  -6.263  0.40 15.84 ?  98  PRO   A HD2  1 
ATOM   1958 H HD3  A PRO   A 1 98  ? 24.503 -6.977  -7.081  0.60 14.24 ?  98  PRO   A HD3  1 
ATOM   1959 H HD3  B PRO   A 1 98  ? 24.468 -7.251  -6.835  0.40 15.84 ?  98  PRO   A HD3  1 
ATOM   1960 N N    A ASN   A 1 99  ? 22.994 -2.269  -9.057  0.60 12.05 ?  99  ASN   A N    1 
ATOM   1961 N N    B ASN   A 1 99  ? 23.273 -2.766  -9.489  0.40 15.94 ?  99  ASN   A N    1 
ATOM   1962 C CA   A ASN   A 1 99  ? 22.008 -1.219  -9.283  0.60 12.82 ?  99  ASN   A CA   1 
ATOM   1963 C CA   B ASN   A 1 99  ? 22.329 -1.738  -9.919  0.40 17.69 ?  99  ASN   A CA   1 
ATOM   1964 C C    A ASN   A 1 99  ? 21.473 -1.380  -10.701 0.60 13.42 ?  99  ASN   A C    1 
ATOM   1965 C C    B ASN   A 1 99  ? 21.798 -2.178  -11.276 0.40 19.14 ?  99  ASN   A C    1 
ATOM   1966 O O    A ASN   A 1 99  ? 22.163 -1.057  -11.673 0.60 14.74 ?  99  ASN   A O    1 
ATOM   1967 O O    B ASN   A 1 99  ? 22.388 -1.896  -12.320 0.40 18.38 ?  99  ASN   A O    1 
ATOM   1968 C CB   A ASN   A 1 99  ? 22.641 0.158   -9.095  0.60 13.01 ?  99  ASN   A CB   1 
ATOM   1969 C CB   B ASN   A 1 99  ? 23.028 -0.387  -10.000 0.40 18.35 ?  99  ASN   A CB   1 
ATOM   1970 C CG   A ASN   A 1 99  ? 21.614 1.283   -9.099  0.60 13.82 ?  99  ASN   A CG   1 
ATOM   1971 C CG   B ASN   A 1 99  ? 22.075 0.753   -10.295 0.40 18.85 ?  99  ASN   A CG   1 
ATOM   1972 O OD1  A ASN   A 1 99  ? 20.623 1.232   -9.828  0.60 14.24 ?  99  ASN   A OD1  1 
ATOM   1973 O OD1  B ASN   A 1 99  ? 20.945 0.539   -10.729 0.40 18.70 ?  99  ASN   A OD1  1 
ATOM   1974 N ND2  A ASN   A 1 99  ? 21.853 2.303   -8.283  0.60 14.83 ?  99  ASN   A ND2  1 
ATOM   1975 N ND2  B ASN   A 1 99  ? 22.534 1.976   -10.069 0.40 19.78 ?  99  ASN   A ND2  1 
ATOM   1976 H H    A ASN   A 1 99  ? 23.764 -2.087  -9.391  0.60 14.48 ?  99  ASN   A H    1 
ATOM   1977 H H    B ASN   A 1 99  ? 24.067 -2.649  -9.792  0.40 19.15 ?  99  ASN   A H    1 
ATOM   1978 H HA   A ASN   A 1 99  ? 21.274 -1.310  -8.651  0.60 15.41 ?  99  ASN   A HA   1 
ATOM   1979 H HA   B ASN   A 1 99  ? 21.588 -1.680  -9.294  0.40 21.26 ?  99  ASN   A HA   1 
ATOM   1980 H HB2  A ASN   A 1 99  ? 23.110 0.181   -8.247  0.60 15.64 ?  99  ASN   A HB2  1 
ATOM   1981 H HB2  B ASN   A 1 99  ? 23.460 -0.208  -9.152  0.40 22.04 ?  99  ASN   A HB2  1 
ATOM   1982 H HB3  A ASN   A 1 99  ? 23.262 0.320   -9.823  0.60 15.64 ?  99  ASN   A HB3  1 
ATOM   1983 H HB3  B ASN   A 1 99  ? 23.690 -0.420  -10.710 0.40 22.04 ?  99  ASN   A HB3  1 
ATOM   1984 H HD21 A ASN   A 1 99  ? 21.304 2.964   -8.247  0.60 17.83 ?  99  ASN   A HD21 1 
ATOM   1985 H HD21 B ASN   A 1 99  ? 22.035 2.657   -10.226 0.40 23.76 ?  99  ASN   A HD21 1 
ATOM   1986 H HD22 A ASN   A 1 99  ? 22.559 2.304   -7.791  0.60 17.83 ?  99  ASN   A HD22 1 
ATOM   1987 H HD22 B ASN   A 1 99  ? 23.334 2.086   -9.775  0.40 23.76 ?  99  ASN   A HD22 1 
ATOM   1988 N N    A VAL   A 1 100 ? 20.241 -1.892  -10.805 0.60 14.71 ?  100 VAL   A N    1 
ATOM   1989 N N    B VAL   A 1 100 ? 20.672 -2.898  -11.262 0.40 22.02 ?  100 VAL   A N    1 
ATOM   1990 C CA   A VAL   A 1 100 ? 19.601 -2.108  -12.101 0.60 17.45 ?  100 VAL   A CA   1 
ATOM   1991 C CA   B VAL   A 1 100 ? 20.131 -3.445  -12.501 0.40 24.62 ?  100 VAL   A CA   1 
ATOM   1992 C C    A VAL   A 1 100 ? 19.488 -0.806  -12.882 0.60 17.66 ?  100 VAL   A C    1 
ATOM   1993 C C    B VAL   A 1 100 ? 19.618 -2.344  -13.417 0.40 26.32 ?  100 VAL   A C    1 
ATOM   1994 O O    A VAL   A 1 100 ? 19.547 -0.807  -14.117 0.60 19.05 ?  100 VAL   A O    1 
ATOM   1995 O O    B VAL   A 1 100 ? 19.559 -2.534  -14.638 0.40 26.73 ?  100 VAL   A O    1 
ATOM   1996 C CB   A VAL   A 1 100 ? 18.229 -2.790  -11.901 0.60 19.42 ?  100 VAL   A CB   1 
ATOM   1997 C CB   B VAL   A 1 100 ? 19.057 -4.515  -12.213 0.40 25.25 ?  100 VAL   A CB   1 
ATOM   1998 C CG1  A VAL   A 1 100 ? 17.514 -2.987  -13.234 0.60 20.24 ?  100 VAL   A CG1  1 
ATOM   1999 C CG1  B VAL   A 1 100 ? 17.727 -3.867  -11.863 0.40 25.49 ?  100 VAL   A CG1  1 
ATOM   2000 C CG2  A VAL   A 1 100 ? 18.404 -4.121  -11.183 0.60 20.04 ?  100 VAL   A CG2  1 
ATOM   2001 C CG2  B VAL   A 1 100 ? 18.909 -5.460  -13.404 0.40 25.50 ?  100 VAL   A CG2  1 
ATOM   2002 H H    A VAL   A 1 100 ? 19.753 -2.129  -10.130 0.60 17.68 ?  100 VAL   A H    1 
ATOM   2003 H H    B VAL   A 1 100 ? 20.209 -3.078  -10.559 0.40 26.45 ?  100 VAL   A H    1 
ATOM   2004 H HA   A VAL   A 1 100 ? 20.150 -2.714  -12.617 0.60 20.97 ?  100 VAL   A HA   1 
ATOM   2005 H HA   B VAL   A 1 100 ? 20.849 -3.891  -12.971 0.40 29.58 ?  100 VAL   A HA   1 
ATOM   2006 H HB   A VAL   A 1 100 ? 17.670 -2.225  -11.347 0.60 23.34 ?  100 VAL   A HB   1 
ATOM   2007 H HB   B VAL   A 1 100 ? 19.339 -5.048  -11.452 0.40 30.33 ?  100 VAL   A HB   1 
ATOM   2008 H HG11 A VAL   A 1 100 ? 16.744 -3.563  -13.097 0.60 24.32 ?  100 VAL   A HG11 1 
ATOM   2009 H HG11 B VAL   A 1 100 ? 17.119 -4.554  -11.547 0.40 30.62 ?  100 VAL   A HG11 1 
ATOM   2010 H HG12 A VAL   A 1 100 ? 17.223 -2.125  -13.570 0.60 24.32 ?  100 VAL   A HG12 1 
ATOM   2011 H HG12 B VAL   A 1 100 ? 17.874 -3.209  -11.168 0.40 30.62 ?  100 VAL   A HG12 1 
ATOM   2012 H HG13 A VAL   A 1 100 ? 18.126 -3.401  -13.863 0.60 24.32 ?  100 VAL   A HG13 1 
ATOM   2013 H HG13 B VAL   A 1 100 ? 17.358 -3.446  -12.653 0.40 30.62 ?  100 VAL   A HG13 1 
ATOM   2014 H HG21 A VAL   A 1 100 ? 17.550 -4.584  -11.161 0.60 24.07 ?  100 VAL   A HG21 1 
ATOM   2015 H HG21 B VAL   A 1 100 ? 18.227 -6.121  -13.203 0.40 30.63 ?  100 VAL   A HG21 1 
ATOM   2016 H HG22 A VAL   A 1 100 ? 19.056 -4.655  -11.662 0.60 24.07 ?  100 VAL   A HG22 1 
ATOM   2017 H HG22 B VAL   A 1 100 ? 18.651 -4.947  -14.185 0.40 30.63 ?  100 VAL   A HG22 1 
ATOM   2018 H HG23 A VAL   A 1 100 ? 18.712 -3.955  -10.279 0.60 24.07 ?  100 VAL   A HG23 1 
ATOM   2019 H HG23 B VAL   A 1 100 ? 19.758 -5.903  -13.565 0.40 30.63 ?  100 VAL   A HG23 1 
ATOM   2020 N N    A ASN   A 1 101 ? 19.306 0.318   -12.192 0.60 18.10 ?  101 ASN   A N    1 
ATOM   2021 N N    B ASN   A 1 101 ? 19.252 -1.187  -12.864 0.40 27.09 ?  101 ASN   A N    1 
ATOM   2022 C CA   A ASN   A 1 101 ? 19.237 1.605   -12.875 0.60 19.30 ?  101 ASN   A CA   1 
ATOM   2023 C CA   B ASN   A 1 101 ? 18.834 -0.078  -13.711 0.40 27.64 ?  101 ASN   A CA   1 
ATOM   2024 C C    A ASN   A 1 101 ? 20.587 2.056   -13.422 0.60 20.98 ?  101 ASN   A C    1 
ATOM   2025 C C    B ASN   A 1 101 ? 19.987 0.465   -14.538 0.40 27.70 ?  101 ASN   A C    1 
ATOM   2026 O O    A ASN   A 1 101 ? 20.644 3.106   -14.074 0.60 22.40 ?  101 ASN   A O    1 
ATOM   2027 O O    B ASN   A 1 101 ? 19.750 1.072   -15.588 0.40 28.32 ?  101 ASN   A O    1 
ATOM   2028 C CB   A ASN   A 1 101 ? 18.626 2.648   -11.940 0.60 18.96 ?  101 ASN   A CB   1 
ATOM   2029 C CB   B ASN   A 1 101 ? 18.225 1.042   -12.869 0.40 27.87 ?  101 ASN   A CB   1 
ATOM   2030 C CG   A ASN   A 1 101 ? 17.238 2.245   -11.460 0.60 18.52 ?  101 ASN   A CG   1 
ATOM   2031 C CG   B ASN   A 1 101 ? 16.814 0.731   -12.417 0.40 28.05 ?  101 ASN   A CG   1 
ATOM   2032 O OD1  A ASN   A 1 101 ? 16.405 1.796   -12.249 0.60 18.81 ?  101 ASN   A OD1  1 
ATOM   2033 O OD1  B ASN   A 1 101 ? 16.173 -0.186  -12.930 0.40 28.04 ?  101 ASN   A OD1  1 
ATOM   2034 N ND2  A ASN   A 1 101 ? 16.995 2.373   -10.164 0.60 18.69 ?  101 ASN   A ND2  1 
ATOM   2035 N ND2  B ASN   A 1 101 ? 16.318 1.501   -11.459 0.40 27.99 ?  101 ASN   A ND2  1 
ATOM   2036 H H    A ASN   A 1 101 ? 19.209 0.363   -11.343 0.60 21.75 ?  101 ASN   A H    1 
ATOM   2037 H H    B ASN   A 1 101 ? 19.252 -1.023  -12.021 0.40 32.54 ?  101 ASN   A H    1 
ATOM   2038 H HA   A ASN   A 1 101 ? 18.642 1.514   -13.634 0.60 23.19 ?  101 ASN   A HA   1 
ATOM   2039 H HA   B ASN   A 1 101 ? 18.151 -0.397  -14.321 0.40 33.20 ?  101 ASN   A HA   1 
ATOM   2040 H HB2  A ASN   A 1 101 ? 19.200 2.758   -11.167 0.60 22.78 ?  101 ASN   A HB2  1 
ATOM   2041 H HB2  B ASN   A 1 101 ? 18.773 1.175   -12.080 0.40 33.48 ?  101 ASN   A HB2  1 
ATOM   2042 H HB3  A ASN   A 1 101 ? 18.554 3.496   -12.420 0.60 22.78 ?  101 ASN   A HB3  1 
ATOM   2043 H HB3  B ASN   A 1 101 ? 18.200 1.854   -13.398 0.40 33.48 ?  101 ASN   A HB3  1 
ATOM   2044 H HD21 A ASN   A 1 101 ? 16.222 2.158   -9.856  0.60 22.45 ?  101 ASN   A HD21 1 
ATOM   2045 H HD21 B ASN   A 1 101 ? 15.520 1.365   -11.169 0.40 33.61 ?  101 ASN   A HD21 1 
ATOM   2046 H HD22 A ASN   A 1 101 ? 17.600 2.683   -9.642  0.60 22.45 ?  101 ASN   A HD22 1 
ATOM   2047 H HD22 B ASN   A 1 101 ? 16.795 2.134   -11.127 0.40 33.61 ?  101 ASN   A HD22 1 
ATOM   2048 N N    A LYS   A 1 102 ? 21.656 1.287   -13.183 0.60 22.16 ?  102 LYS   A N    1 
ATOM   2049 N N    B LYS   A 1 102 ? 21.226 0.260   -14.088 0.40 26.99 ?  102 LYS   A N    1 
ATOM   2050 C CA   A LYS   A 1 102 ? 22.953 1.491   -13.817 0.60 23.16 ?  102 LYS   A CA   1 
ATOM   2051 C CA   B LYS   A 1 102 ? 22.410 0.624   -14.849 0.40 26.32 ?  102 LYS   A CA   1 
ATOM   2052 C C    A LYS   A 1 102 ? 23.280 0.433   -14.861 0.60 23.84 ?  102 LYS   A C    1 
ATOM   2053 C C    B LYS   A 1 102 ? 23.051 -0.578  -15.542 0.40 25.17 ?  102 LYS   A C    1 
ATOM   2054 O O    A LYS   A 1 102 ? 24.358 0.495   -15.457 0.60 24.14 ?  102 LYS   A O    1 
ATOM   2055 O O    B LYS   A 1 102 ? 24.236 -0.529  -15.886 0.40 25.06 ?  102 LYS   A O    1 
ATOM   2056 C CB   A LYS   A 1 102 ? 24.076 1.502   -12.770 0.60 23.96 ?  102 LYS   A CB   1 
ATOM   2057 C CB   B LYS   A 1 102 ? 23.436 1.328   -13.961 0.40 27.21 ?  102 LYS   A CB   1 
ATOM   2058 C CG   A LYS   A 1 102 ? 24.002 2.630   -11.764 0.60 24.70 ?  102 LYS   A CG   1 
ATOM   2059 C CG   B LYS   A 1 102 ? 22.948 2.634   -13.355 0.40 28.10 ?  102 LYS   A CG   1 
ATOM   2060 C CD   A LYS   A 1 102 ? 25.150 2.538   -10.767 0.60 25.51 ?  102 LYS   A CD   1 
ATOM   2061 C CD   B LYS   A 1 102 ? 24.047 3.695   -13.342 0.40 28.92 ?  102 LYS   A CD   1 
ATOM   2062 C CE   A LYS   A 1 102 ? 25.098 3.663   -9.747  0.60 26.20 ?  102 LYS   A CE   1 
ATOM   2063 C CE   B LYS   A 1 102 ? 24.314 4.230   -11.943 0.40 29.70 ?  102 LYS   A CE   1 
ATOM   2064 N NZ   A LYS   A 1 102 ? 26.166 3.520   -8.715  0.60 26.59 ?  102 LYS   A NZ   1 
ATOM   2065 N NZ   B LYS   A 1 102 ? 25.101 3.278   -11.109 0.40 30.04 ?  102 LYS   A NZ   1 
ATOM   2066 H H    A LYS   A 1 102 ? 21.654 0.617   -12.642 0.60 26.62 ?  102 LYS   A H    1 
ATOM   2067 H H    B LYS   A 1 102 ? 21.406 -0.089  -13.330 0.40 32.41 ?  102 LYS   A H    1 
ATOM   2068 H HA   A LYS   A 1 102 ? 22.959 2.340   -14.270 0.60 27.82 ?  102 LYS   A HA   1 
ATOM   2069 H HA   B LYS   A 1 102 ? 22.113 1.261   -15.511 0.40 31.61 ?  102 LYS   A HA   1 
ATOM   2070 H HB2  A LYS   A 1 102 ? 24.049 0.666   -12.276 0.60 28.78 ?  102 LYS   A HB2  1 
ATOM   2071 H HB2  B LYS   A 1 102 ? 23.672 0.735   -13.233 0.40 32.68 ?  102 LYS   A HB2  1 
ATOM   2072 H HB3  A LYS   A 1 102 ? 24.930 1.574   -13.229 0.60 28.78 ?  102 LYS   A HB3  1 
ATOM   2073 H HB3  B LYS   A 1 102 ? 24.223 1.518   -14.497 0.40 32.68 ?  102 LYS   A HB3  1 
ATOM   2074 H HG2  A LYS   A 1 102 ? 24.063 3.478   -12.229 0.60 29.67 ?  102 LYS   A HG2  1 
ATOM   2075 H HG2  B LYS   A 1 102 ? 22.205 2.973   -13.878 0.40 33.75 ?  102 LYS   A HG2  1 
ATOM   2076 H HG3  A LYS   A 1 102 ? 23.165 2.569   -11.277 0.60 29.67 ?  102 LYS   A HG3  1 
ATOM   2077 H HG3  B LYS   A 1 102 ? 22.665 2.476   -12.441 0.40 33.75 ?  102 LYS   A HG3  1 
ATOM   2078 H HD2  A LYS   A 1 102 ? 25.095 1.694   -10.293 0.60 30.63 ?  102 LYS   A HD2  1 
ATOM   2079 H HD2  B LYS   A 1 102 ? 24.875 3.315   -13.677 0.40 34.74 ?  102 LYS   A HD2  1 
ATOM   2080 H HD3  A LYS   A 1 102 ? 25.992 2.599   -11.246 0.60 30.63 ?  102 LYS   A HD3  1 
ATOM   2081 H HD3  B LYS   A 1 102 ? 23.772 4.436   -13.903 0.40 34.74 ?  102 LYS   A HD3  1 
ATOM   2082 H HE2  A LYS   A 1 102 ? 25.225 4.511   -10.202 0.60 31.47 ?  102 LYS   A HE2  1 
ATOM   2083 H HE2  B LYS   A 1 102 ? 24.818 5.056   -12.012 0.40 35.67 ?  102 LYS   A HE2  1 
ATOM   2084 H HE3  A LYS   A 1 102 ? 24.237 3.648   -9.301  0.60 31.47 ?  102 LYS   A HE3  1 
ATOM   2085 H HE3  B LYS   A 1 102 ? 23.468 4.393   -11.497 0.40 35.67 ?  102 LYS   A HE3  1 
ATOM   2086 H HZ1  A LYS   A 1 102 ? 26.114 4.188   -8.131  0.60 31.94 ?  102 LYS   A HZ1  1 
ATOM   2087 H HZ1  B LYS   A 1 102 ? 25.146 3.573   -10.270 0.40 36.08 ?  102 LYS   A HZ1  1 
ATOM   2088 H HZ2  A LYS   A 1 102 ? 26.067 2.748   -8.283  0.60 31.94 ?  102 LYS   A HZ2  1 
ATOM   2089 H HZ2  B LYS   A 1 102 ? 24.715 2.477   -11.115 0.40 36.08 ?  102 LYS   A HZ2  1 
ATOM   2090 H HZ3  A LYS   A 1 102 ? 26.966 3.533   -9.103  0.60 31.94 ?  102 LYS   A HZ3  1 
ATOM   2091 H HZ3  B LYS   A 1 102 ? 25.927 3.201   -11.433 0.40 36.08 ?  102 LYS   A HZ3  1 
ATOM   2092 N N    A GLY   A 1 103 ? 22.394 -0.533  -15.096 0.60 24.74 ?  103 GLY   A N    1 
ATOM   2093 N N    B GLY   A 1 103 ? 22.303 -1.664  -15.720 0.40 24.27 ?  103 GLY   A N    1 
ATOM   2094 C CA   A GLY   A 1 103 ? 22.683 -1.607  -16.026 0.60 25.63 ?  103 GLY   A CA   1 
ATOM   2095 C CA   B GLY   A 1 103 ? 22.777 -2.793  -16.495 0.40 23.64 ?  103 GLY   A CA   1 
ATOM   2096 C C    A GLY   A 1 103 ? 23.545 -2.711  -15.463 0.60 26.34 ?  103 GLY   A C    1 
ATOM   2097 C C    B GLY   A 1 103 ? 23.654 -3.775  -15.755 0.40 22.66 ?  103 GLY   A C    1 
ATOM   2098 O O    A GLY   A 1 103 ? 24.135 -3.472  -16.234 0.60 27.41 ?  103 GLY   A O    1 
ATOM   2099 O O    B GLY   A 1 103 ? 24.223 -4.670  -16.391 0.40 22.78 ?  103 GLY   A O    1 
ATOM   2100 H H    A GLY   A 1 103 ? 21.625 -0.596  -14.726 0.60 29.72 ?  103 GLY   A H    1 
ATOM   2101 H H    B GLY   A 1 103 ? 21.518 -1.765  -15.389 0.40 29.15 ?  103 GLY   A H    1 
ATOM   2102 H HA2  A GLY   A 1 103 ? 21.846 -1.993  -16.346 0.60 30.78 ?  103 GLY   A HA2  1 
ATOM   2103 H HA2  B GLY   A 1 103 ? 22.015 -3.284  -16.834 0.40 28.40 ?  103 GLY   A HA2  1 
ATOM   2104 H HA3  A GLY   A 1 103 ? 23.157 -1.254  -16.791 0.60 30.78 ?  103 GLY   A HA3  1 
ATOM   2105 H HA3  B GLY   A 1 103 ? 23.278 -2.458  -17.256 0.40 28.40 ?  103 GLY   A HA3  1 
ATOM   2106 N N    A GLU   A 1 104 ? 23.642 -2.819  -14.142 0.60 25.45 ?  104 GLU   A N    1 
ATOM   2107 N N    B GLU   A 1 104 ? 23.779 -3.650  -14.438 0.40 21.86 ?  104 GLU   A N    1 
ATOM   2108 C CA   A GLU   A 1 104 ? 24.484 -3.826  -13.517 0.60 24.76 ?  104 GLU   A CA   1 
ATOM   2109 C CA   B GLU   A 1 104 ? 24.651 -4.539  -13.685 0.40 20.97 ?  104 GLU   A CA   1 
ATOM   2110 C C    A GLU   A 1 104 ? 23.758 -5.167  -13.426 0.60 25.17 ?  104 GLU   A C    1 
ATOM   2111 C C    B GLU   A 1 104 ? 23.973 -5.893  -13.484 0.40 20.83 ?  104 GLU   A C    1 
ATOM   2112 O O    A GLU   A 1 104 ? 22.532 -5.233  -13.283 0.60 25.47 ?  104 GLU   A O    1 
ATOM   2113 O O    B GLU   A 1 104 ? 22.782 -5.973  -13.166 0.40 20.79 ?  104 GLU   A O    1 
ATOM   2114 C CB   A GLU   A 1 104 ? 24.953 -3.335  -12.142 0.60 23.35 ?  104 GLU   A CB   1 
ATOM   2115 C CB   B GLU   A 1 104 ? 25.043 -3.891  -12.355 0.40 20.44 ?  104 GLU   A CB   1 
ATOM   2116 C CG   A GLU   A 1 104 ? 25.865 -2.104  -12.265 0.60 22.35 ?  104 GLU   A CG   1 
ATOM   2117 C CG   B GLU   A 1 104 ? 25.799 -2.571  -12.550 0.40 20.45 ?  104 GLU   A CG   1 
ATOM   2118 C CD   A GLU   A 1 104 ? 26.164 -1.382  -10.957 0.60 21.30 ?  104 GLU   A CD   1 
ATOM   2119 C CD   B GLU   A 1 104 ? 26.336 -1.959  -11.272 0.40 20.31 ?  104 GLU   A CD   1 
ATOM   2120 O OE1  A GLU   A 1 104 ? 25.580 -1.729  -9.911  0.60 19.91 ?  104 GLU   A OE1  1 
ATOM   2121 O OE1  B GLU   A 1 104 ? 25.830 -2.284  -10.179 0.40 20.11 ?  104 GLU   A OE1  1 
ATOM   2122 O OE2  A GLU   A 1 104 ? 26.988 -0.439  -10.992 0.60 21.71 -1 104 GLU   A OE2  1 
ATOM   2123 O OE2  B GLU   A 1 104 ? 27.269 -1.129  -11.373 0.40 20.56 -1 104 GLU   A OE2  1 
ATOM   2124 H H    A GLU   A 1 104 ? 23.233 -2.315  -13.585 0.60 30.57 ?  104 GLU   A H    1 
ATOM   2125 H H    B GLU   A 1 104 ? 23.363 -3.064  -13.962 0.40 26.26 ?  104 GLU   A H    1 
ATOM   2126 H HA   A GLU   A 1 104 ? 25.266 -3.963  -14.068 0.60 29.74 ?  104 GLU   A HA   1 
ATOM   2127 H HA   B GLU   A 1 104 ? 25.465 -4.681  -14.194 0.40 25.19 ?  104 GLU   A HA   1 
ATOM   2128 H HB2  A GLU   A 1 104 ? 24.178 -3.095  -11.612 0.60 28.04 ?  104 GLU   A HB2  1 
ATOM   2129 H HB2  B GLU   A 1 104 ? 24.243 -3.701  -11.844 0.40 24.55 ?  104 GLU   A HB2  1 
ATOM   2130 H HB3  A GLU   A 1 104 ? 25.450 -4.047  -11.707 0.60 28.04 ?  104 GLU   A HB3  1 
ATOM   2131 H HB3  B GLU   A 1 104 ? 25.621 -4.494  -11.866 0.40 24.55 ?  104 GLU   A HB3  1 
ATOM   2132 H HG2  A GLU   A 1 104 ? 26.706 -2.388  -12.652 0.60 26.85 ?  104 GLU   A HG2  1 
ATOM   2133 H HG2  B GLU   A 1 104 ? 26.549 -2.723  -13.145 0.40 24.57 ?  104 GLU   A HG2  1 
ATOM   2134 H HG3  A GLU   A 1 104 ? 25.434 -1.463  -12.848 0.60 26.85 ?  104 GLU   A HG3  1 
ATOM   2135 H HG3  B GLU   A 1 104 ? 25.197 -1.918  -12.937 0.40 24.57 ?  104 GLU   A HG3  1 
ATOM   2136 N N    A ASP   A 1 105 ? 24.541 -6.241  -13.529 0.60 25.91 ?  105 ASP   A N    1 
ATOM   2137 N N    B ASP   A 1 105 ? 24.744 -6.958  -13.703 0.40 21.51 ?  105 ASP   A N    1 
ATOM   2138 C CA   A ASP   A 1 105 ? 24.008 -7.594  -13.641 0.60 26.85 ?  105 ASP   A CA   1 
ATOM   2139 C CA   B ASP   A 1 105 ? 24.227 -8.322  -13.726 0.40 22.33 ?  105 ASP   A CA   1 
ATOM   2140 C C    A ASP   A 1 105 ? 23.299 -7.997  -12.353 0.60 25.46 ?  105 ASP   A C    1 
ATOM   2141 C C    B ASP   A 1 105 ? 23.514 -8.660  -12.424 0.40 21.72 ?  105 ASP   A C    1 
ATOM   2142 O O    A ASP   A 1 105 ? 23.914 -8.024  -11.284 0.60 24.69 ?  105 ASP   A O    1 
ATOM   2143 O O    B ASP   A 1 105 ? 24.113 -8.619  -11.345 0.40 20.15 ?  105 ASP   A O    1 
ATOM   2144 C CB   A ASP   A 1 105 ? 25.162 -8.554  -13.926 0.60 29.06 ?  105 ASP   A CB   1 
ATOM   2145 C CB   B ASP   A 1 105 ? 25.400 -9.276  -13.952 0.40 23.90 ?  105 ASP   A CB   1 
ATOM   2146 C CG   A ASP   A 1 105 ? 24.683 -9.940  -14.289 0.60 30.99 ?  105 ASP   A CG   1 
ATOM   2147 C CG   B ASP   A 1 105 ? 25.013 -10.734 -13.821 0.40 25.21 ?  105 ASP   A CG   1 
ATOM   2148 O OD1  A ASP   A 1 105 ? 23.451 -10.134 -14.372 0.60 31.52 ?  105 ASP   A OD1  1 
ATOM   2149 O OD1  B ASP   A 1 105 ? 23.812 -11.052 -13.953 0.40 25.59 ?  105 ASP   A OD1  1 
ATOM   2150 O OD2  A ASP   A 1 105 ? 25.534 -10.829 -14.505 0.60 31.87 -1 105 ASP   A OD2  1 
ATOM   2151 O OD2  B ASP   A 1 105 ? 25.920 -11.563 -13.587 0.40 25.94 -1 105 ASP   A OD2  1 
ATOM   2152 H H    A ASP   A 1 105 ? 25.403 -6.218  -13.546 0.60 31.12 ?  105 ASP   A H    1 
ATOM   2153 H H    B ASP   A 1 105 ? 25.583 -6.910  -13.854 0.40 25.84 ?  105 ASP   A H    1 
ATOM   2154 H HA   A ASP   A 1 105 ? 23.380 -7.654  -14.378 0.60 32.25 ?  105 ASP   A HA   1 
ATOM   2155 H HA   B ASP   A 1 105 ? 23.594 -8.422  -14.452 0.40 26.83 ?  105 ASP   A HA   1 
ATOM   2156 H HB2  A ASP   A 1 105 ? 25.678 -8.231  -14.683 0.60 34.90 ?  105 ASP   A HB2  1 
ATOM   2157 H HB2  B ASP   A 1 105 ? 25.738 -9.144  -14.850 0.40 28.71 ?  105 ASP   A HB2  1 
ATOM   2158 H HB3  A ASP   A 1 105 ? 25.741 -8.607  -13.141 0.60 34.90 ?  105 ASP   A HB3  1 
ATOM   2159 H HB3  B ASP   A 1 105 ? 26.093 -9.079  -13.303 0.40 28.71 ?  105 ASP   A HB3  1 
ATOM   2160 N N    A ILE   A 1 106 ? 22.011 -8.343  -12.458 0.60 25.22 ?  106 ILE   A N    1 
ATOM   2161 N N    B ILE   A 1 106 ? 22.230 -9.009  -12.527 0.40 22.80 ?  106 ILE   A N    1 
ATOM   2162 C CA   A ILE   A 1 106 ? 21.252 -8.783  -11.292 0.60 24.46 ?  106 ILE   A CA   1 
ATOM   2163 C CA   B ILE   A 1 106 ? 21.457 -9.299  -11.330 0.40 23.92 ?  106 ILE   A CA   1 
ATOM   2164 C C    A ILE   A 1 106 ? 21.797 -10.085 -10.728 0.60 23.19 ?  106 ILE   A C    1 
ATOM   2165 C C    B ILE   A 1 106 ? 21.916 -10.580 -10.648 0.40 23.73 ?  106 ILE   A C    1 
ATOM   2166 O O    A ILE   A 1 106 ? 21.608 -10.368 -9.542  0.60 22.46 ?  106 ILE   A O    1 
ATOM   2167 O O    B ILE   A 1 106 ? 21.640 -10.776 -9.459  0.40 23.95 ?  106 ILE   A O    1 
ATOM   2168 C CB   A ILE   A 1 106 ? 19.746 -8.905  -11.616 0.60 25.44 ?  106 ILE   A CB   1 
ATOM   2169 C CB   B ILE   A 1 106 ? 19.941 -9.284  -11.626 0.40 25.41 ?  106 ILE   A CB   1 
ATOM   2170 C CG1  A ILE   A 1 106 ? 18.928 -9.070  -10.333 0.60 25.92 ?  106 ILE   A CG1  1 
ATOM   2171 C CG1  B ILE   A 1 106 ? 19.153 -8.934  -10.361 0.40 26.49 ?  106 ILE   A CG1  1 
ATOM   2172 C CG2  A ILE   A 1 106 ? 19.490 -10.090 -12.531 0.60 25.70 ?  106 ILE   A CG2  1 
ATOM   2173 C CG2  B ILE   A 1 106 ? 19.483 -10.626 -12.181 0.40 25.57 ?  106 ILE   A CG2  1 
ATOM   2174 C CD1  A ILE   A 1 106 ? 19.031 -7.898  -9.384  0.60 26.20 ?  106 ILE   A CD1  1 
ATOM   2175 C CD1  B ILE   A 1 106 ? 19.674 -7.703  -9.651  0.40 27.04 ?  106 ILE   A CD1  1 
ATOM   2176 H H    A ILE   A 1 106 ? 21.564 -8.335  -13.191 0.60 30.29 ?  106 ILE   A H    1 
ATOM   2177 H H    B ILE   A 1 106 ? 21.788 -9.059  -13.260 0.40 27.39 ?  106 ILE   A H    1 
ATOM   2178 H HA   A ILE   A 1 106 ? 21.355 -8.115  -10.604 0.60 29.39 ?  106 ILE   A HA   1 
ATOM   2179 H HA   B ILE   A 1 106 ? 21.663 -8.587  -10.718 0.40 28.73 ?  106 ILE   A HA   1 
ATOM   2180 H HB   A ILE   A 1 106 ? 19.461 -8.098  -12.068 0.60 30.56 ?  106 ILE   A HB   1 
ATOM   2181 H HB   B ILE   A 1 106 ? 19.760 -8.603  -12.293 0.40 30.52 ?  106 ILE   A HB   1 
ATOM   2182 H HG12 A ILE   A 1 106 ? 17.995 -9.174  -10.573 0.60 31.13 ?  106 ILE   A HG12 1 
ATOM   2183 H HG12 B ILE   A 1 106 ? 18.226 -8.768  -10.601 0.40 31.81 ?  106 ILE   A HG12 1 
ATOM   2184 H HG13 A ILE   A 1 106 ? 19.233 -9.863  -9.863  0.60 31.13 ?  106 ILE   A HG13 1 
ATOM   2185 H HG13 B ILE   A 1 106 ? 19.203 -9.678  -9.742  0.40 31.81 ?  106 ILE   A HG13 1 
ATOM   2186 H HG21 A ILE   A 1 106 ? 18.597 -10.014 -12.899 0.60 30.87 ?  106 ILE   A HG21 1 
ATOM   2187 H HG21 B ILE   A 1 106 ? 18.610 -10.517 -12.593 0.40 30.71 ?  106 ILE   A HG21 1 
ATOM   2188 H HG22 A ILE   A 1 106 ? 20.146 -10.085 -13.244 0.60 30.87 ?  106 ILE   A HG22 1 
ATOM   2189 H HG22 B ILE   A 1 106 ? 20.125 -10.925 -12.842 0.40 30.71 ?  106 ILE   A HG22 1 
ATOM   2190 H HG23 A ILE   A 1 106 ? 19.567 -10.910 -12.016 0.60 30.87 ?  106 ILE   A HG23 1 
ATOM   2191 H HG23 B ILE   A 1 106 ? 19.428 -11.268 -11.457 0.40 30.71 ?  106 ILE   A HG23 1 
ATOM   2192 H HD11 A ILE   A 1 106 ? 18.314 -7.956  -8.736  0.60 31.47 ?  106 ILE   A HD11 1 
ATOM   2193 H HD11 B ILE   A 1 106 ? 19.056 -7.464  -8.962  0.40 32.48 ?  106 ILE   A HD11 1 
ATOM   2194 H HD12 A ILE   A 1 106 ? 19.890 -7.932  -8.931  0.60 31.47 ?  106 ILE   A HD12 1 
ATOM   2195 H HD12 B ILE   A 1 106 ? 20.524 -7.908  -9.237  0.40 32.48 ?  106 ILE   A HD12 1 
ATOM   2196 H HD13 A ILE   A 1 106 ? 18.955 -7.075  -9.892  0.60 31.47 ?  106 ILE   A HD13 1 
ATOM   2197 H HD13 B ILE   A 1 106 ? 19.776 -6.979  -10.294 0.40 32.48 ?  106 ILE   A HD13 1 
ATOM   2198 N N    A GLN   A 1 107 ? 22.487 -10.885 -11.550 0.60 23.60 ?  107 GLN   A N    1 
ATOM   2199 N N    B GLN   A 1 107 ? 22.629 -11.454 -11.363 0.40 23.72 ?  107 GLN   A N    1 
ATOM   2200 C CA   A GLN   A 1 107 ? 23.102 -12.113 -11.061 0.60 25.04 ?  107 GLN   A CA   1 
ATOM   2201 C CA   B GLN   A 1 107 ? 23.221 -12.620 -10.721 0.40 24.64 ?  107 GLN   A CA   1 
ATOM   2202 C C    A GLN   A 1 107 ? 24.091 -11.851 -9.938  0.60 22.53 ?  107 GLN   A C    1 
ATOM   2203 C C    B GLN   A 1 107 ? 24.207 -12.224 -9.634  0.40 22.42 ?  107 GLN   A C    1 
ATOM   2204 O O    A GLN   A 1 107 ? 24.353 -12.755 -9.138  0.60 23.68 ?  107 GLN   A O    1 
ATOM   2205 O O    B GLN   A 1 107 ? 24.427 -12.995 -8.693  0.40 22.67 ?  107 GLN   A O    1 
ATOM   2206 C CB   A GLN   A 1 107 ? 23.810 -12.853 -12.204 0.60 28.90 ?  107 GLN   A CB   1 
ATOM   2207 C CB   B GLN   A 1 107 ? 23.907 -13.500 -11.769 0.40 27.69 ?  107 GLN   A CB   1 
ATOM   2208 C CG   A GLN   A 1 107 ? 22.911 -13.193 -13.382 0.60 32.68 ?  107 GLN   A CG   1 
ATOM   2209 C CG   B GLN   A 1 107 ? 23.079 -14.701 -12.207 0.40 30.56 ?  107 GLN   A CG   1 
ATOM   2210 C CD   A GLN   A 1 107 ? 21.733 -14.059 -12.989 0.60 35.77 ?  107 GLN   A CD   1 
ATOM   2211 C CD   B GLN   A 1 107 ? 21.586 -14.415 -12.245 0.40 32.87 ?  107 GLN   A CD   1 
ATOM   2212 O OE1  A GLN   A 1 107 ? 21.900 -15.124 -12.394 0.60 36.87 ?  107 GLN   A OE1  1 
ATOM   2213 O OE1  B GLN   A 1 107 ? 20.816 -14.978 -11.466 0.40 33.75 ?  107 GLN   A OE1  1 
ATOM   2214 N NE2  A GLN   A 1 107 ? 20.529 -13.601 -13.314 0.60 37.10 ?  107 GLN   A NE2  1 
ATOM   2215 N NE2  B GLN   A 1 107 ? 21.173 -13.532 -13.144 0.40 33.66 ?  107 GLN   A NE2  1 
ATOM   2216 H H    A GLN   A 1 107 ? 22.622 -10.736 -12.380 0.60 28.35 ?  107 GLN   A H    1 
ATOM   2217 H H    B GLN   A 1 107 ? 22.787 -11.384 -12.205 0.40 28.49 ?  107 GLN   A H    1 
ATOM   2218 H HA   A GLN   A 1 107 ? 22.420 -12.698 -10.707 0.60 30.08 ?  107 GLN   A HA   1 
ATOM   2219 H HA   B GLN   A 1 107 ? 22.520 -13.134 -10.298 0.40 29.60 ?  107 GLN   A HA   1 
ATOM   2220 H HB2  A GLN   A 1 107 ? 24.533 -12.301 -12.538 0.60 34.71 ?  107 GLN   A HB2  1 
ATOM   2221 H HB2  B GLN   A 1 107 ? 24.094 -12.967 -12.558 0.40 33.25 ?  107 GLN   A HB2  1 
ATOM   2222 H HB3  A GLN   A 1 107 ? 24.171 -13.690 -11.863 0.60 34.71 ?  107 GLN   A HB3  1 
ATOM   2223 H HB3  B GLN   A 1 107 ? 24.740 -13.833 -11.398 0.40 33.25 ?  107 GLN   A HB3  1 
ATOM   2224 H HG2  A GLN   A 1 107 ? 22.566 -12.372 -13.763 0.60 39.24 ?  107 GLN   A HG2  1 
ATOM   2225 H HG2  B GLN   A 1 107 ? 23.354 -14.960 -13.099 0.40 36.71 ?  107 GLN   A HG2  1 
ATOM   2226 H HG3  A GLN   A 1 107 ? 23.429 -13.675 -14.047 0.60 39.24 ?  107 GLN   A HG3  1 
ATOM   2227 H HG3  B GLN   A 1 107 ? 23.234 -15.428 -11.585 0.40 36.71 ?  107 GLN   A HG3  1 
ATOM   2228 H HE21 A GLN   A 1 107 ? 20.453 -12.852 -13.729 0.60 44.55 ?  107 GLN   A HE21 1 
ATOM   2229 H HE21 B GLN   A 1 107 ? 21.738 -13.161 -13.674 0.40 40.42 ?  107 GLN   A HE21 1 
ATOM   2230 H HE22 A GLN   A 1 107 ? 19.828 -14.055 -13.112 0.60 44.55 ?  107 GLN   A HE22 1 
ATOM   2231 H HE22 B GLN   A 1 107 ? 20.337 -13.337 -13.197 0.40 40.42 ?  107 GLN   A HE22 1 
ATOM   2232 N N    A LEU   A 1 108 ? 24.637 -10.635 -9.850  0.60 18.38 ?  108 LEU   A N    1 
ATOM   2233 N N    B LEU   A 1 108 ? 24.791 -11.029 -9.732  0.40 19.89 ?  108 LEU   A N    1 
ATOM   2234 C CA   A LEU   A 1 108 ? 25.590 -10.310 -8.794  0.60 16.38 ?  108 LEU   A CA   1 
ATOM   2235 C CA   B LEU   A 1 108 ? 25.669 -10.529 -8.685  0.40 17.65 ?  108 LEU   A CA   1 
ATOM   2236 C C    A LEU   A 1 108 ? 24.931 -10.204 -7.427  0.60 14.74 ?  108 LEU   A C    1 
ATOM   2237 C C    B LEU   A 1 108 ? 24.940 -10.272 -7.374  0.40 15.57 ?  108 LEU   A C    1 
ATOM   2238 O O    A LEU   A 1 108 ? 25.637 -10.067 -6.424  0.60 14.69 ?  108 LEU   A O    1 
ATOM   2239 O O    B LEU   A 1 108 ? 25.603 -10.070 -6.352  0.40 15.44 ?  108 LEU   A O    1 
ATOM   2240 C CB   A LEU   A 1 108 ? 26.337 -9.016  -9.137  0.60 16.39 ?  108 LEU   A CB   1 
ATOM   2241 C CB   B LEU   A 1 108 ? 26.395 -9.262  -9.151  0.40 17.67 ?  108 LEU   A CB   1 
ATOM   2242 C CG   A LEU   A 1 108 ? 27.337 -9.175  -10.285 0.60 18.13 ?  108 LEU   A CG   1 
ATOM   2243 C CG   B LEU   A 1 108 ? 27.429 -9.475  -10.261 0.40 18.58 ?  108 LEU   A CG   1 
ATOM   2244 C CD1  A LEU   A 1 108 ? 27.781 -7.822  -10.822 0.60 18.44 ?  108 LEU   A CD1  1 
ATOM   2245 C CD1  B LEU   A 1 108 ? 27.978 -8.143  -10.753 0.40 18.75 ?  108 LEU   A CD1  1 
ATOM   2246 C CD2  A LEU   A 1 108 ? 28.547 -9.992  -9.845  0.60 19.52 ?  108 LEU   A CD2  1 
ATOM   2247 C CD2  B LEU   A 1 108 ? 28.562 -10.375 -9.784  0.40 19.28 ?  108 LEU   A CD2  1 
ATOM   2248 H H    A LEU   A 1 108 ? 24.467 -9.986  -10.384 0.60 22.09 ?  108 LEU   A H    1 
ATOM   2249 H H    B LEU   A 1 108 ? 24.698 -10.501 -10.399 0.40 23.90 ?  108 LEU   A H    1 
ATOM   2250 H HA   A LEU   A 1 108 ? 26.245 -11.018 -8.739  0.60 19.68 ?  108 LEU   A HA   1 
ATOM   2251 H HA   B LEU   A 1 108 ? 26.339 -11.201 -8.503  0.40 21.21 ?  108 LEU   A HA   1 
ATOM   2252 H HB2  A LEU   A 1 108 ? 25.692 -8.339  -9.400  0.60 19.69 ?  108 LEU   A HB2  1 
ATOM   2253 H HB2  B LEU   A 1 108 ? 25.738 -8.631  -9.483  0.40 21.23 ?  108 LEU   A HB2  1 
ATOM   2254 H HB3  A LEU   A 1 108 ? 26.826 -8.716  -8.355  0.60 19.69 ?  108 LEU   A HB3  1 
ATOM   2255 H HB3  B LEU   A 1 108 ? 26.860 -8.877  -8.392  0.40 21.23 ?  108 LEU   A HB3  1 
ATOM   2256 H HG   A LEU   A 1 108 ? 26.909 -9.654  -11.011 0.60 21.78 ?  108 LEU   A HG   1 
ATOM   2257 H HG   B LEU   A 1 108 ? 26.999 -9.913  -11.012 0.40 22.33 ?  108 LEU   A HG   1 
ATOM   2258 H HD11 A LEU   A 1 108 ? 28.340 -7.960  -11.605 0.60 22.15 ?  108 LEU   A HD11 1 
ATOM   2259 H HD11 B LEU   A 1 108 ? 28.625 -8.308  -11.458 0.40 22.53 ?  108 LEU   A HD11 1 
ATOM   2260 H HD12 A LEU   A 1 108 ? 26.998 -7.305  -11.062 0.60 22.15 ?  108 LEU   A HD12 1 
ATOM   2261 H HD12 B LEU   A 1 108 ? 27.246 -7.606  -11.096 0.40 22.53 ?  108 LEU   A HD12 1 
ATOM   2262 H HD13 A LEU   A 1 108 ? 28.287 -7.360  -10.135 0.60 22.15 ?  108 LEU   A HD13 1 
ATOM   2263 H HD13 B LEU   A 1 108 ? 28.406 -7.684  -10.013 0.40 22.53 ?  108 LEU   A HD13 1 
ATOM   2264 H HD21 A LEU   A 1 108 ? 29.221 -9.961  -10.540 0.60 23.45 ?  108 LEU   A HD21 1 
ATOM   2265 H HD21 B LEU   A 1 108 ? 29.285 -10.339 -10.428 0.40 23.16 ?  108 LEU   A HD21 1 
ATOM   2266 H HD22 A LEU   A 1 108 ? 28.899 -9.616  -9.023  0.60 23.45 ?  108 LEU   A HD22 1 
ATOM   2267 H HD22 B LEU   A 1 108 ? 28.871 -10.057 -8.920  0.40 23.16 ?  108 LEU   A HD22 1 
ATOM   2268 H HD23 A LEU   A 1 108 ? 28.270 -10.911 -9.694  0.60 23.45 ?  108 LEU   A HD23 1 
ATOM   2269 H HD23 B LEU   A 1 108 ? 28.232 -11.282 -9.703  0.40 23.16 ?  108 LEU   A HD23 1 
ATOM   2270 N N    . LEU   A 1 109 ? 23.603 -10.286 -7.357  1.00 14.27 ?  109 LEU   A N    1 
ATOM   2271 C CA   . LEU   A 1 109 ? 22.915 -10.147 -6.082  1.00 13.41 ?  109 LEU   A CA   1 
ATOM   2272 C C    . LEU   A 1 109 ? 23.258 -11.296 -5.138  1.00 12.77 ?  109 LEU   A C    1 
ATOM   2273 O O    . LEU   A 1 109 ? 23.406 -11.090 -3.931  1.00 13.13 ?  109 LEU   A O    1 
ATOM   2274 C CB   . LEU   A 1 109 ? 21.410 -10.047 -6.322  1.00 14.12 ?  109 LEU   A CB   1 
ATOM   2275 C CG   . LEU   A 1 109 ? 20.520 -9.768  -5.111  1.00 14.35 ?  109 LEU   A CG   1 
ATOM   2276 C CD1  . LEU   A 1 109 ? 20.968 -8.491  -4.416  1.00 14.35 ?  109 LEU   A CD1  1 
ATOM   2277 C CD2  . LEU   A 1 109 ? 19.055 -9.662  -5.528  1.00 15.39 ?  109 LEU   A CD2  1 
ATOM   2278 H H    A LEU   A 1 109 ? 23.080 -10.418 -8.028  0.60 17.15 ?  109 LEU   A H    1 
ATOM   2279 H H    B LEU   A 1 109 ? 23.090 -10.371 -8.043  0.40 17.15 ?  109 LEU   A H    1 
ATOM   2280 H HA   . LEU   A 1 109 ? 23.201 -9.321  -5.661  1.00 16.12 ?  109 LEU   A HA   1 
ATOM   2281 H HB2  . LEU   A 1 109 ? 21.250 -9.331  -6.956  1.00 16.98 ?  109 LEU   A HB2  1 
ATOM   2282 H HB3  . LEU   A 1 109 ? 21.107 -10.884 -6.703  1.00 16.98 ?  109 LEU   A HB3  1 
ATOM   2283 H HG   . LEU   A 1 109 ? 20.594 -10.497 -4.479  1.00 17.25 ?  109 LEU   A HG   1 
ATOM   2284 H HD11 . LEU   A 1 109 ? 20.303 -8.236  -3.755  1.00 17.25 ?  109 LEU   A HD11 1 
ATOM   2285 H HD12 . LEU   A 1 109 ? 21.820 -8.647  -3.985  1.00 17.25 ?  109 LEU   A HD12 1 
ATOM   2286 H HD13 . LEU   A 1 109 ? 21.055 -7.783  -5.079  1.00 17.25 ?  109 LEU   A HD13 1 
ATOM   2287 H HD21 . LEU   A 1 109 ? 18.525 -9.357  -4.771  1.00 18.50 ?  109 LEU   A HD21 1 
ATOM   2288 H HD22 . LEU   A 1 109 ? 18.971 -9.032  -6.260  1.00 18.50 ?  109 LEU   A HD22 1 
ATOM   2289 H HD23 . LEU   A 1 109 ? 18.738 -10.538 -5.813  1.00 18.50 ?  109 LEU   A HD23 1 
ATOM   2290 N N    . LYS   A 1 110 ? 23.396 -12.516 -5.663  1.00 12.91 ?  110 LYS   A N    1 
ATOM   2291 C CA   . LYS   A 1 110 ? 23.774 -13.632 -4.797  1.00 13.17 ?  110 LYS   A CA   1 
ATOM   2292 C C    . LYS   A 1 110 ? 25.160 -13.411 -4.195  1.00 12.77 ?  110 LYS   A C    1 
ATOM   2293 O O    . LYS   A 1 110 ? 25.355 -13.592 -2.992  1.00 12.53 ?  110 LYS   A O    1 
ATOM   2294 C CB   . LYS   A 1 110 ? 23.687 -14.964 -5.549  1.00 14.15 ?  110 LYS   A CB   1 
ATOM   2295 C CG   . LYS   A 1 110 ? 23.896 -16.174 -4.640  1.00 14.27 ?  110 LYS   A CG   1 
ATOM   2296 C CD   . LYS   A 1 110 ? 23.655 -17.498 -5.352  1.00 14.52 ?  110 LYS   A CD   1 
ATOM   2297 C CE   . LYS   A 1 110 ? 23.763 -18.672 -4.393  1.00 15.32 ?  110 LYS   A CE   1 
ATOM   2298 N NZ   . LYS   A 1 110 ? 22.590 -18.772 -3.477  1.00 15.72 ?  110 LYS   A NZ   1 
ATOM   2299 H H    . LYS   A 1 110 ? 23.279 -12.718 -6.489  1.00 15.52 ?  110 LYS   A H    1 
ATOM   2300 H HA   . LYS   A 1 110 ? 23.137 -13.676 -4.062  1.00 15.83 ?  110 LYS   A HA   1 
ATOM   2301 H HB2  . LYS   A 1 110 ? 22.805 -15.045 -5.952  1.00 17.01 ?  110 LYS   A HB2  1 
ATOM   2302 H HB3  . LYS   A 1 110 ? 24.367 -14.986 -6.236  1.00 17.01 ?  110 LYS   A HB3  1 
ATOM   2303 H HG2  . LYS   A 1 110 ? 24.808 -16.175 -4.312  1.00 17.15 ?  110 LYS   A HG2  1 
ATOM   2304 H HG3  . LYS   A 1 110 ? 23.276 -16.125 -3.894  1.00 17.15 ?  110 LYS   A HG3  1 
ATOM   2305 H HD2  . LYS   A 1 110 ? 22.766 -17.503 -5.736  1.00 17.45 ?  110 LYS   A HD2  1 
ATOM   2306 H HD3  . LYS   A 1 110 ? 24.324 -17.614 -6.047  1.00 17.45 ?  110 LYS   A HD3  1 
ATOM   2307 H HE2  . LYS   A 1 110 ? 23.819 -19.498 -4.899  1.00 18.42 ?  110 LYS   A HE2  1 
ATOM   2308 H HE3  . LYS   A 1 110 ? 24.560 -18.566 -3.845  1.00 18.42 ?  110 LYS   A HE3  1 
ATOM   2309 H HZ1  . LYS   A 1 110 ? 22.680 -19.463 -2.929  1.00 18.89 ?  110 LYS   A HZ1  1 
ATOM   2310 H HZ2  . LYS   A 1 110 ? 22.517 -18.025 -2.992  1.00 18.89 ?  110 LYS   A HZ2  1 
ATOM   2311 H HZ3  . LYS   A 1 110 ? 21.841 -18.874 -3.952  1.00 18.89 ?  110 LYS   A HZ3  1 
ATOM   2312 N N    . SER   A 1 111 ? 26.122 -12.974 -5.013  1.00 12.45 ?  111 SER   A N    1 
ATOM   2313 C CA   . SER   A 1 111 ? 27.453 -12.667 -4.497  1.00 12.60 ?  111 SER   A CA   1 
ATOM   2314 C C    . SER   A 1 111 ? 27.387 -11.611 -3.400  1.00 12.72 ?  111 SER   A C    1 
ATOM   2315 O O    . SER   A 1 111 ? 28.084 -11.709 -2.385  1.00 13.23 ?  111 SER   A O    1 
ATOM   2316 C CB   . SER   A 1 111 ? 28.348 -12.181 -5.637  1.00 14.28 ?  111 SER   A CB   1 
ATOM   2317 O OG   . SER   A 1 111 ? 28.468 -13.180 -6.640  1.00 16.02 ?  111 SER   A OG   1 
ATOM   2318 H H    . SER   A 1 111 ? 26.020 -12.850 -5.856  1.00 14.97 ?  111 SER   A H    1 
ATOM   2319 H HA   . SER   A 1 111 ? 27.842 -13.473 -4.124  1.00 15.14 ?  111 SER   A HA   1 
ATOM   2320 H HB2  . SER   A 1 111 ? 27.952 -11.392 -6.035  1.00 17.16 ?  111 SER   A HB2  1 
ATOM   2321 H HB3  . SER   A 1 111 ? 29.224 -11.973 -5.281  1.00 17.16 ?  111 SER   A HB3  1 
ATOM   2322 H HG   . SER   A 1 111 ? 28.979 -12.903 -7.257  1.00 19.25 ?  111 SER   A HG   1 
ATOM   2323 N N    . ALA   A 1 112 ? 26.538 -10.595 -3.581  1.00 12.75 ?  112 ALA   A N    1 
ATOM   2324 C CA   . ALA   A 1 112 ? 26.399 -9.551  -2.567  1.00 12.45 ?  112 ALA   A CA   1 
ATOM   2325 C C    . ALA   A 1 112 ? 25.913 -10.140 -1.244  1.00 12.64 ?  112 ALA   A C    1 
ATOM   2326 O O    . ALA   A 1 112 ? 26.464 -9.849  -0.176  1.00 12.64 ?  112 ALA   A O    1 
ATOM   2327 C CB   . ALA   A 1 112 ? 25.443 -8.466  -3.062  1.00 13.09 ?  112 ALA   A CB   1 
ATOM   2328 H H    . ALA   A 1 112 ? 26.039 -10.485 -4.271  1.00 15.33 ?  112 ALA   A H    1 
ATOM   2329 H HA   . ALA   A 1 112 ? 27.263 -9.137  -2.407  1.00 14.97 ?  112 ALA   A HA   1 
ATOM   2330 H HB1  . ALA   A 1 112 ? 25.370 -7.771  -2.382  1.00 15.74 ?  112 ALA   A HB1  1 
ATOM   2331 H HB2  . ALA   A 1 112 ? 25.796 -8.081  -3.880  1.00 15.74 ?  112 ALA   A HB2  1 
ATOM   2332 H HB3  . ALA   A 1 112 ? 24.573 -8.856  -3.226  1.00 15.74 ?  112 ALA   A HB3  1 
ATOM   2333 N N    . TYR   A 1 113 ? 24.876 -10.984 -1.294  1.00 12.54 ?  113 TYR   A N    1 
ATOM   2334 C CA   . TYR   A 1 113 ? 24.364 -11.581 -0.060  1.00 12.27 ?  113 TYR   A CA   1 
ATOM   2335 C C    . TYR   A 1 113 ? 25.366 -12.537 0.593   1.00 12.15 ?  113 TYR   A C    1 
ATOM   2336 O O    . TYR   A 1 113 ? 25.322 -12.719 1.815   1.00 12.75 ?  113 TYR   A O    1 
ATOM   2337 C CB   . TYR   A 1 113 ? 23.044 -12.310 -0.322  1.00 12.74 ?  113 TYR   A CB   1 
ATOM   2338 C CG   . TYR   A 1 113 ? 21.831 -11.411 -0.257  1.00 12.75 ?  113 TYR   A CG   1 
ATOM   2339 C CD1  . TYR   A 1 113 ? 21.474 -10.784 0.931   1.00 13.08 ?  113 TYR   A CD1  1 
ATOM   2340 C CD2  . TYR   A 1 113 ? 21.027 -11.210 -1.371  1.00 12.80 ?  113 TYR   A CD2  1 
ATOM   2341 C CE1  . TYR   A 1 113 ? 20.351 -9.979  1.011   1.00 13.65 ?  113 TYR   A CE1  1 
ATOM   2342 C CE2  . TYR   A 1 113 ? 19.880 -10.403 -1.301  1.00 12.90 ?  113 TYR   A CE2  1 
ATOM   2343 C CZ   . TYR   A 1 113 ? 19.556 -9.790  -0.105  1.00 13.18 ?  113 TYR   A CZ   1 
ATOM   2344 O OH   . TYR   A 1 113 ? 18.430 -8.995  -0.006  1.00 14.28 ?  113 TYR   A OH   1 
ATOM   2345 H H    . TYR   A 1 113 ? 24.465 -11.223 -2.012  1.00 15.07 ?  113 TYR   A H    1 
ATOM   2346 H HA   . TYR   A 1 113 ? 24.190 -10.874 0.574   1.00 14.75 ?  113 TYR   A HA   1 
ATOM   2347 H HB2  . TYR   A 1 113 ? 23.072 -12.701 -1.208  1.00 15.32 ?  113 TYR   A HB2  1 
ATOM   2348 H HB3  . TYR   A 1 113 ? 22.934 -13.006 0.343   1.00 15.32 ?  113 TYR   A HB3  1 
ATOM   2349 H HD1  . TYR   A 1 113 ? 21.999 -10.914 1.688   1.00 15.73 ?  113 TYR   A HD1  1 
ATOM   2350 H HD2  . TYR   A 1 113 ? 21.242 -11.630 -2.172  1.00 15.39 ?  113 TYR   A HD2  1 
ATOM   2351 H HE1  . TYR   A 1 113 ? 20.132 -9.572  1.814   1.00 16.41 ?  113 TYR   A HE1  1 
ATOM   2352 H HE2  . TYR   A 1 113 ? 19.349 -10.274 -2.053  1.00 15.51 ?  113 TYR   A HE2  1 
ATOM   2353 H HH   . TYR   A 1 113 ? 18.049 -8.964  -0.758  1.00 17.16 ?  113 TYR   A HH   1 
ATOM   2354 N N    . GLU   A 1 114 ? 26.266 -13.157 -0.186  1.00 12.12 ?  114 GLU   A N    1 
ATOM   2355 C CA   . GLU   A 1 114 ? 27.258 -14.053 0.412   1.00 12.66 ?  114 GLU   A CA   1 
ATOM   2356 C C    . GLU   A 1 114 ? 28.110 -13.340 1.456   1.00 12.74 ?  114 GLU   A C    1 
ATOM   2357 O O    . GLU   A 1 114 ? 28.586 -13.973 2.407   1.00 12.93 ?  114 GLU   A O    1 
ATOM   2358 C CB   . GLU   A 1 114 ? 28.127 -14.704 -0.674  1.00 12.85 ?  114 GLU   A CB   1 
ATOM   2359 C CG   . GLU   A 1 114 ? 27.365 -15.765 -1.453  1.00 13.29 ?  114 GLU   A CG   1 
ATOM   2360 C CD   . GLU   A 1 114 ? 28.072 -16.290 -2.695  1.00 13.51 ?  114 GLU   A CD   1 
ATOM   2361 O OE1  . GLU   A 1 114 ? 29.040 -15.666 -3.175  1.00 13.87 ?  114 GLU   A OE1  1 
ATOM   2362 O OE2  . GLU   A 1 114 ? 27.619 -17.346 -3.201  1.00 14.56 -1 114 GLU   A OE2  1 
ATOM   2363 H H    . GLU   A 1 114 ? 26.324 -13.068 -1.046  1.00 14.57 ?  114 GLU   A H    1 
ATOM   2364 H HA   . GLU   A 1 114 ? 26.784 -14.764 0.863   1.00 15.22 ?  114 GLU   A HA   1 
ATOM   2365 H HB2  . GLU   A 1 114 ? 28.418 -14.028 -1.304  1.00 15.45 ?  114 GLU   A HB2  1 
ATOM   2366 H HB3  . GLU   A 1 114 ? 28.890 -15.131 -0.260  1.00 15.45 ?  114 GLU   A HB3  1 
ATOM   2367 H HG2  . GLU   A 1 114 ? 27.208 -16.525 -0.868  1.00 15.98 ?  114 GLU   A HG2  1 
ATOM   2368 H HG3  . GLU   A 1 114 ? 26.517 -15.395 -1.738  1.00 15.98 ?  114 GLU   A HG3  1 
ATOM   2369 N N    . ASN   A 1 115 ? 28.292 -12.022 1.321   1.00 12.31 ?  115 ASN   A N    1 
ATOM   2370 C CA   . ASN   A 1 115 ? 29.056 -11.290 2.327   1.00 12.75 ?  115 ASN   A CA   1 
ATOM   2371 C C    . ASN   A 1 115 ? 28.437 -11.416 3.714   1.00 12.60 ?  115 ASN   A C    1 
ATOM   2372 O O    . ASN   A 1 115 ? 29.148 -11.351 4.725   1.00 12.83 ?  115 ASN   A O    1 
ATOM   2373 C CB   . ASN   A 1 115 ? 29.162 -9.815  1.942   1.00 12.74 ?  115 ASN   A CB   1 
ATOM   2374 C CG   . ASN   A 1 115 ? 29.965 -9.602  0.681   1.00 13.61 ?  115 ASN   A CG   1 
ATOM   2375 O OD1  . ASN   A 1 115 ? 31.185 -9.713  0.699   1.00 16.60 ?  115 ASN   A OD1  1 
ATOM   2376 N ND2  . ASN   A 1 115 ? 29.295 -9.299  -0.415  1.00 13.14 ?  115 ASN   A ND2  1 
ATOM   2377 H H    . ASN   A 1 115 ? 27.988 -11.536 0.676   1.00 14.80 ?  115 ASN   A H    1 
ATOM   2378 H HA   . ASN   A 1 115 ? 29.950 -11.656 2.369   1.00 15.33 ?  115 ASN   A HA   1 
ATOM   2379 H HB2  . ASN   A 1 115 ? 28.266 -9.463  1.805   1.00 15.32 ?  115 ASN   A HB2  1 
ATOM   2380 H HB3  . ASN   A 1 115 ? 29.595 -9.335  2.667   1.00 15.32 ?  115 ASN   A HB3  1 
ATOM   2381 H HD21 . ASN   A 1 115 ? 29.715 -9.161  -1.151  1.00 15.80 ?  115 ASN   A HD21 1 
ATOM   2382 H HD22 . ASN   A 1 115 ? 28.435 -9.241  -0.394  1.00 15.80 ?  115 ASN   A HD22 1 
ATOM   2383 N N    . PHE   A 1 116 ? 27.111 -11.579 3.789   1.00 12.85 ?  116 PHE   A N    1 
ATOM   2384 C CA   . PHE   A 1 116 ? 26.457 -11.678 5.092   1.00 12.59 ?  116 PHE   A CA   1 
ATOM   2385 C C    . PHE   A 1 116 ? 26.928 -12.911 5.867   1.00 12.43 ?  116 PHE   A C    1 
ATOM   2386 O O    . PHE   A 1 116 ? 26.860 -12.929 7.098   1.00 12.93 ?  116 PHE   A O    1 
ATOM   2387 C CB   . PHE   A 1 116 ? 24.929 -11.807 4.946   1.00 12.50 ?  116 PHE   A CB   1 
ATOM   2388 C CG   . PHE   A 1 116 ? 24.176 -10.555 4.489   1.00 12.22 ?  116 PHE   A CG   1 
ATOM   2389 C CD1  . PHE   A 1 116 ? 24.746 -9.537  3.743   1.00 12.32 ?  116 PHE   A CD1  1 
ATOM   2390 C CD2  . PHE   A 1 116 ? 22.820 -10.447 4.811   1.00 12.83 ?  116 PHE   A CD2  1 
ATOM   2391 C CE1  . PHE   A 1 116 ? 23.985 -8.457  3.334   1.00 12.54 ?  116 PHE   A CE1  1 
ATOM   2392 C CE2  . PHE   A 1 116 ? 22.062 -9.372  4.409   1.00 12.85 ?  116 PHE   A CE2  1 
ATOM   2393 C CZ   . PHE   A 1 116 ? 22.634 -8.378  3.671   1.00 12.56 ?  116 PHE   A CZ   1 
ATOM   2394 H H    . PHE   A 1 116 ? 26.574 -11.617 3.115   1.00 15.45 ?  116 PHE   A H    1 
ATOM   2395 H HA   . PHE   A 1 116 ? 26.644 -10.886 5.619   1.00 15.14 ?  116 PHE   A HA   1 
ATOM   2396 H HB2  . PHE   A 1 116 ? 24.743 -12.507 4.298   1.00 15.03 ?  116 PHE   A HB2  1 
ATOM   2397 H HB3  . PHE   A 1 116 ? 24.561 -12.068 5.807   1.00 15.03 ?  116 PHE   A HB3  1 
ATOM   2398 H HD1  . PHE   A 1 116 ? 25.640 -9.594  3.509   1.00 14.81 ?  116 PHE   A HD1  1 
ATOM   2399 H HD2  . PHE   A 1 116 ? 22.415 -11.134 5.304   1.00 15.42 ?  116 PHE   A HD2  1 
ATOM   2400 H HE1  . PHE   A 1 116 ? 24.380 -7.773  2.841   1.00 15.08 ?  116 PHE   A HE1  1 
ATOM   2401 H HE2  . PHE   A 1 116 ? 21.159 -9.323  4.640   1.00 15.45 ?  116 PHE   A HE2  1 
ATOM   2402 H HZ   . PHE   A 1 116 ? 22.132 -7.638  3.410   1.00 15.11 ?  116 PHE   A HZ   1 
ATOM   2403 N N    . ASN   A 1 117 ? 27.371 -13.963 5.166   1.00 12.68 ?  117 ASN   A N    1 
ATOM   2404 C CA   . ASN   A 1 117 ? 27.736 -15.206 5.837   1.00 13.33 ?  117 ASN   A CA   1 
ATOM   2405 C C    . ASN   A 1 117 ? 29.002 -15.094 6.668   1.00 13.86 ?  117 ASN   A C    1 
ATOM   2406 O O    . ASN   A 1 117 ? 29.299 -16.021 7.432   1.00 14.82 ?  117 ASN   A O    1 
ATOM   2407 C CB   . ASN   A 1 117 ? 27.851 -16.331 4.815   1.00 13.57 ?  117 ASN   A CB   1 
ATOM   2408 C CG   . ASN   A 1 117 ? 26.498 -16.717 4.279   1.00 13.13 ?  117 ASN   A CG   1 
ATOM   2409 O OD1  . ASN   A 1 117 ? 25.520 -16.737 5.029   1.00 14.08 ?  117 ASN   A OD1  1 
ATOM   2410 N ND2  . ASN   A 1 117 ? 26.412 -16.981 2.991   1.00 12.91 ?  117 ASN   A ND2  1 
ATOM   2411 H H    . ASN   A 1 117 ? 27.445 -13.980 4.305   1.00 15.24 ?  117 ASN   A H    1 
ATOM   2412 H HA   . ASN   A 1 117 ? 27.011 -15.442 6.439   1.00 16.02 ?  117 ASN   A HA   1 
ATOM   2413 H HB2  . ASN   A 1 117 ? 28.397 -16.033 4.070   1.00 16.31 ?  117 ASN   A HB2  1 
ATOM   2414 H HB3  . ASN   A 1 117 ? 28.244 -17.106 5.236   1.00 16.31 ?  117 ASN   A HB3  1 
ATOM   2415 H HD21 . ASN   A 1 117 ? 25.657 -17.201 2.650   1.00 15.53 ?  117 ASN   A HD21 1 
ATOM   2416 H HD22 . ASN   A 1 117 ? 27.118 -16.952 2.500   1.00 15.53 ?  117 ASN   A HD22 1 
ATOM   2417 N N    . GLN   A 1 118 ? 29.734 -13.988 6.557   1.00 13.79 ?  118 GLN   A N    1 
ATOM   2418 C CA   . GLN   A 1 118 ? 30.916 -13.752 7.375   1.00 14.07 ?  118 GLN   A CA   1 
ATOM   2419 C C    . GLN   A 1 118 ? 30.576 -13.179 8.746   1.00 14.43 ?  118 GLN   A C    1 
ATOM   2420 O O    . GLN   A 1 118 ? 31.494 -12.890 9.526   1.00 15.97 ?  118 GLN   A O    1 
ATOM   2421 C CB   . GLN   A 1 118 ? 31.903 -12.851 6.630   1.00 14.24 ?  118 GLN   A CB   1 
ATOM   2422 C CG   . GLN   A 1 118 ? 32.372 -13.438 5.313   1.00 14.25 ?  118 GLN   A CG   1 
ATOM   2423 C CD   . GLN   A 1 118 ? 33.210 -14.694 5.496   1.00 14.62 ?  118 GLN   A CD   1 
ATOM   2424 O OE1  . GLN   A 1 118 ? 34.077 -14.755 6.378   1.00 15.98 ?  118 GLN   A OE1  1 
ATOM   2425 N NE2  . GLN   A 1 118 ? 32.960 -15.703 4.658   1.00 14.57 ?  118 GLN   A NE2  1 
ATOM   2426 H H    . GLN   A 1 118 ? 29.556 -13.345 6.006   1.00 16.58 ?  118 GLN   A H    1 
ATOM   2427 H HA   . GLN   A 1 118 ? 31.349 -14.609 7.521   1.00 16.91 ?  118 GLN   A HA   1 
ATOM   2428 H HB2  . GLN   A 1 118 ? 31.471 -12.005 6.446   1.00 17.12 ?  118 GLN   A HB2  1 
ATOM   2429 H HB3  . GLN   A 1 118 ? 32.679 -12.716 7.193   1.00 17.12 ?  118 GLN   A HB3  1 
ATOM   2430 H HG2  . GLN   A 1 118 ? 31.601 -13.664 4.768   1.00 17.13 ?  118 GLN   A HG2  1 
ATOM   2431 H HG3  . GLN   A 1 118 ? 32.920 -12.782 4.853   1.00 17.13 ?  118 GLN   A HG3  1 
ATOM   2432 H HE21 . GLN   A 1 118 ? 32.340 -15.622 4.058   1.00 17.51 ?  118 GLN   A HE21 1 
ATOM   2433 H HE22 . GLN   A 1 118 ? 33.397 -16.437 4.719   1.00 17.51 ?  118 GLN   A HE22 1 
ATOM   2434 N N    . HIS   A 1 119 ? 29.287 -13.029 9.061   1.00 14.09 ?  119 HIS   A N    1 
ATOM   2435 C CA   . HIS   A 1 119 ? 28.845 -12.424 10.311  1.00 14.22 ?  119 HIS   A CA   1 
ATOM   2436 C C    . HIS   A 1 119 ? 27.707 -13.245 10.890  1.00 14.55 ?  119 HIS   A C    1 
ATOM   2437 O O    . HIS   A 1 119 ? 26.752 -13.569 10.180  1.00 14.99 ?  119 HIS   A O    1 
ATOM   2438 C CB   . HIS   A 1 119 ? 28.393 -10.987 10.051  1.00 14.74 ?  119 HIS   A CB   1 
ATOM   2439 C CG   . HIS   A 1 119 ? 29.469 -10.178 9.419   1.00 15.85 ?  119 HIS   A CG   1 
ATOM   2440 N ND1  . HIS   A 1 119 ? 30.453 -9.562  10.157  1.00 18.02 ?  119 HIS   A ND1  1 
ATOM   2441 C CD2  . HIS   A 1 119 ? 29.788 -9.990  8.119   1.00 16.46 ?  119 HIS   A CD2  1 
ATOM   2442 C CE1  . HIS   A 1 119 ? 31.304 -8.979  9.333   1.00 17.82 ?  119 HIS   A CE1  1 
ATOM   2443 N NE2  . HIS   A 1 119 ? 30.930 -9.229  8.092   1.00 18.03 ?  119 HIS   A NE2  1 
ATOM   2444 H H    . HIS   A 1 119 ? 28.634 -13.291 8.559   1.00 16.94 ?  119 HIS   A H    1 
ATOM   2445 H HA   . HIS   A 1 119 ? 29.576 -12.418 10.947  1.00 17.10 ?  119 HIS   A HA   1 
ATOM   2446 H HB2  . HIS   A 1 119 ? 27.628 -11.002 9.457   1.00 17.72 ?  119 HIS   A HB2  1 
ATOM   2447 H HB3  . HIS   A 1 119 ? 28.159 -10.576 10.895  1.00 17.72 ?  119 HIS   A HB3  1 
ATOM   2448 H HD2  . HIS   A 1 119 ? 29.316 -10.308 7.378   1.00 19.78 ?  119 HIS   A HD2  1 
ATOM   2449 H HE1  . HIS   A 1 119 ? 32.045 -8.477  9.581   1.00 21.41 ?  119 HIS   A HE1  1 
ATOM   2450 H HE2  . HIS   A 1 119 ? 31.324 -8.944  7.379   1.00 21.66 ?  119 HIS   A HE2  1 
ATOM   2451 N N    . GLU   A 1 120 ? 27.798 -13.556 12.182  1.00 15.33 ?  120 GLU   A N    1 
ATOM   2452 C CA   . GLU   A 1 120 ? 26.841 -14.485 12.782  1.00 17.77 ?  120 GLU   A CA   1 
ATOM   2453 C C    . GLU   A 1 120 ? 25.424 -13.918 12.840  1.00 16.55 ?  120 GLU   A C    1 
ATOM   2454 O O    . GLU   A 1 120 ? 24.448 -14.674 12.725  1.00 16.93 ?  120 GLU   A O    1 
ATOM   2455 C CB   . GLU   A 1 120 ? 27.311 -14.887 14.183  1.00 22.91 ?  120 GLU   A CB   1 
ATOM   2456 C CG   . GLU   A 1 120 ? 28.517 -15.812 14.191  1.00 29.48 ?  120 GLU   A CG   1 
ATOM   2457 C CD   . GLU   A 1 120 ? 28.706 -16.509 15.522  1.00 36.25 ?  120 GLU   A CD   1 
ATOM   2458 O OE1  . GLU   A 1 120 ? 28.225 -15.979 16.546  1.00 37.97 ?  120 GLU   A OE1  1 
ATOM   2459 O OE2  . GLU   A 1 120 ? 29.335 -17.588 15.543  1.00 41.07 -1 120 GLU   A OE2  1 
ATOM   2460 H H    . GLU   A 1 120 ? 28.406 -13.260 12.721  1.00 18.43 ?  120 GLU   A H    1 
ATOM   2461 H HA   . GLU   A 1 120 ? 26.819 -15.291 12.250  1.00 21.35 ?  120 GLU   A HA   1 
ATOM   2462 H HB2  . GLU   A 1 120 ? 27.555 -14.094 14.685  1.00 27.52 ?  120 GLU   A HB2  1 
ATOM   2463 H HB3  . GLU   A 1 120 ? 26.589 -15.353 14.640  1.00 27.52 ?  120 GLU   A HB3  1 
ATOM   2464 H HG2  . GLU   A 1 120 ? 28.407 -16.485 13.501  1.00 35.40 ?  120 GLU   A HG2  1 
ATOM   2465 H HG3  . GLU   A 1 120 ? 29.319 -15.295 14.031  1.00 35.40 ?  120 GLU   A HG3  1 
ATOM   2466 N N    . VAL   A 1 121 ? 25.292 -12.610 13.065  1.00 15.90 ?  121 VAL   A N    1 
ATOM   2467 C CA   . VAL   A 1 121 ? 23.998 -11.940 13.181  1.00 15.64 ?  121 VAL   A CA   1 
ATOM   2468 C C    . VAL   A 1 121 ? 24.116 -10.561 12.543  1.00 14.44 ?  121 VAL   A C    1 
ATOM   2469 O O    . VAL   A 1 121 ? 25.100 -9.847  12.774  1.00 15.39 ?  121 VAL   A O    1 
ATOM   2470 C CB   . VAL   A 1 121 ? 23.561 -11.787 14.655  1.00 17.97 ?  121 VAL   A CB   1 
ATOM   2471 C CG1  . VAL   A 1 121 ? 22.169 -11.171 14.742  1.00 18.65 ?  121 VAL   A CG1  1 
ATOM   2472 C CG2  . VAL   A 1 121 ? 23.593 -13.114 15.391  1.00 19.60 ?  121 VAL   A CG2  1 
ATOM   2473 H H    . VAL   A 1 121 ? 25.959 -12.074 13.160  1.00 19.11 ?  121 VAL   A H    1 
ATOM   2474 H HA   . VAL   A 1 121 ? 23.325 -12.455 12.711  1.00 18.79 ?  121 VAL   A HA   1 
ATOM   2475 H HB   . VAL   A 1 121 ? 24.175 -11.189 15.105  1.00 21.60 ?  121 VAL   A HB   1 
ATOM   2476 H HG11 . VAL   A 1 121 ? 21.859 -11.219 15.662  1.00 22.41 ?  121 VAL   A HG11 1 
ATOM   2477 H HG12 . VAL   A 1 121 ? 22.211 -10.246 14.458  1.00 22.41 ?  121 VAL   A HG12 1 
ATOM   2478 H HG13 . VAL   A 1 121 ? 21.565 -11.669 14.168  1.00 22.41 ?  121 VAL   A HG13 1 
ATOM   2479 H HG21 . VAL   A 1 121 ? 23.239 -12.990 16.292  1.00 23.55 ?  121 VAL   A HG21 1 
ATOM   2480 H HG22 . VAL   A 1 121 ? 23.041 -13.758 14.915  1.00 23.55 ?  121 VAL   A HG22 1 
ATOM   2481 H HG23 . VAL   A 1 121 ? 24.505 -13.434 15.441  1.00 23.55 ?  121 VAL   A HG23 1 
ATOM   2482 N N    . LEU   A 1 122 ? 23.102 -10.169 11.764  1.00 13.52 ?  122 LEU   A N    1 
ATOM   2483 C CA   . LEU   A 1 122 ? 23.105 -8.870  11.101  1.00 13.68 ?  122 LEU   A CA   1 
ATOM   2484 C C    . LEU   A 1 122 ? 21.708 -8.271  11.059  1.00 13.71 ?  122 LEU   A C    1 
ATOM   2485 O O    . LEU   A 1 122 ? 20.713 -8.985  10.928  1.00 14.45 ?  122 LEU   A O    1 
ATOM   2486 C CB   . LEU   A 1 122 ? 23.542 -8.965  9.635   1.00 14.78 ?  122 LEU   A CB   1 
ATOM   2487 C CG   . LEU   A 1 122 ? 24.739 -9.829  9.266   1.00 15.07 ?  122 LEU   A CG   1 
ATOM   2488 C CD1  . LEU   A 1 122 ? 24.319 -11.271 9.032   1.00 15.59 ?  122 LEU   A CD1  1 
ATOM   2489 C CD2  . LEU   A 1 122 ? 25.427 -9.259  8.040   1.00 14.42 ?  122 LEU   A CD2  1 
ATOM   2490 H H    . LEU   A 1 122 ? 22.400 -10.644 11.597  1.00 16.25 ?  122 LEU   A H    1 
ATOM   2491 H HA   . LEU   A 1 122 ? 23.701 -8.261  11.567  1.00 16.44 ?  122 LEU   A HA   1 
ATOM   2492 H HB2  . LEU   A 1 122 ? 22.795 -9.304  9.125   1.00 17.77 ?  122 LEU   A HB2  1 
ATOM   2493 H HB3  . LEU   A 1 122 ? 23.752 -8.068  9.331   1.00 17.77 ?  122 LEU   A HB3  1 
ATOM   2494 H HG   . LEU   A 1 122 ? 25.383 -9.821  9.994   1.00 18.11 ?  122 LEU   A HG   1 
ATOM   2495 H HD11 . LEU   A 1 122 ? 25.090 -11.788 8.750   1.00 18.73 ?  122 LEU   A HD11 1 
ATOM   2496 H HD12 . LEU   A 1 122 ? 23.963 -11.635 9.858   1.00 18.73 ?  122 LEU   A HD12 1 
ATOM   2497 H HD13 . LEU   A 1 122 ? 23.637 -11.293 8.341   1.00 18.73 ?  122 LEU   A HD13 1 
ATOM   2498 H HD21 . LEU   A 1 122 ? 26.166 -9.839  7.783   1.00 17.33 ?  122 LEU   A HD21 1 
ATOM   2499 H HD22 . LEU   A 1 122 ? 24.790 -9.199  7.312   1.00 17.33 ?  122 LEU   A HD22 1 
ATOM   2500 H HD23 . LEU   A 1 122 ? 25.771 -8.372  8.249   1.00 17.33 ?  122 LEU   A HD23 1 
ATOM   2501 N N    A LEU   A 1 123 ? 21.657 -6.944  11.134  0.60 13.36 ?  123 LEU   A N    1 
ATOM   2502 N N    B LEU   A 1 123 ? 21.656 -6.946  11.188  0.40 13.04 ?  123 LEU   A N    1 
ATOM   2503 C CA   A LEU   A 1 123 ? 20.493 -6.157  10.741  0.60 12.65 ?  123 LEU   A CA   1 
ATOM   2504 C CA   B LEU   A 1 123 ? 20.471 -6.146  10.902  0.40 12.37 ?  123 LEU   A CA   1 
ATOM   2505 C C    A LEU   A 1 123 ? 20.742 -5.650  9.327   0.60 12.01 ?  123 LEU   A C    1 
ATOM   2506 C C    B LEU   A 1 123 ? 20.677 -5.536  9.523   0.40 11.30 ?  123 LEU   A C    1 
ATOM   2507 O O    A LEU   A 1 123 ? 21.827 -5.132  9.045   0.60 12.03 ?  123 LEU   A O    1 
ATOM   2508 O O    B LEU   A 1 123 ? 21.656 -4.812  9.315   0.40 11.34 ?  123 LEU   A O    1 
ATOM   2509 C CB   A LEU   A 1 123 ? 20.338 -4.969  11.688  0.60 12.90 ?  123 LEU   A CB   1 
ATOM   2510 C CB   B LEU   A 1 123 ? 20.330 -5.040  11.948  0.40 13.25 ?  123 LEU   A CB   1 
ATOM   2511 C CG   A LEU   A 1 123 ? 19.262 -3.938  11.345  0.60 13.39 ?  123 LEU   A CG   1 
ATOM   2512 C CG   B LEU   A 1 123 ? 19.357 -3.908  11.602  0.40 13.62 ?  123 LEU   A CG   1 
ATOM   2513 C CD1  A LEU   A 1 123 ? 17.888 -4.577  11.358  0.60 13.97 ?  123 LEU   A CD1  1 
ATOM   2514 C CD1  B LEU   A 1 123 ? 17.916 -4.401  11.578  0.40 14.10 ?  123 LEU   A CD1  1 
ATOM   2515 C CD2  A LEU   A 1 123 ? 19.330 -2.769  12.321  0.60 13.65 ?  123 LEU   A CD2  1 
ATOM   2516 C CD2  B LEU   A 1 123 ? 19.527 -2.754  12.574  0.40 13.95 ?  123 LEU   A CD2  1 
ATOM   2517 H H    A LEU   A 1 123 ? 22.316 -6.461  11.413  0.60 16.06 ?  123 LEU   A H    1 
ATOM   2518 H H    B LEU   A 1 123 ? 22.327 -6.466  11.438  0.40 15.67 ?  123 LEU   A H    1 
ATOM   2519 H HA   A LEU   A 1 123 ? 19.693 -6.710  10.760  0.60 15.21 ?  123 LEU   A HA   1 
ATOM   2520 H HA   B LEU   A 1 123 ? 19.677 -6.692  10.895  0.40 14.87 ?  123 LEU   A HA   1 
ATOM   2521 H HB2  A LEU   A 1 123 ? 20.124 -5.315  12.570  0.60 15.51 ?  123 LEU   A HB2  1 
ATOM   2522 H HB2  B LEU   A 1 123 ? 20.022 -5.445  12.775  0.40 15.93 ?  123 LEU   A HB2  1 
ATOM   2523 H HB3  A LEU   A 1 123 ? 21.182 -4.502  11.722  0.60 15.51 ?  123 LEU   A HB3  1 
ATOM   2524 H HB3  B LEU   A 1 123 ? 21.202 -4.639  12.094  0.40 15.93 ?  123 LEU   A HB3  1 
ATOM   2525 H HG   A LEU   A 1 123 ? 19.426 -3.588  10.454  0.60 16.09 ?  123 LEU   A HG   1 
ATOM   2526 H HG   B LEU   A 1 123 ? 19.564 -3.566  10.719  0.40 16.37 ?  123 LEU   A HG   1 
ATOM   2527 H HD11 A LEU   A 1 123 ? 17.219 -3.889  11.225  0.60 16.80 ?  123 LEU   A HD11 1 
ATOM   2528 H HD11 B LEU   A 1 123 ? 17.332 -3.657  11.360  0.40 16.94 ?  123 LEU   A HD11 1 
ATOM   2529 H HD12 A LEU   A 1 123 ? 17.839 -5.231  10.645  0.60 16.80 ?  123 LEU   A HD12 1 
ATOM   2530 H HD12 B LEU   A 1 123 ? 17.829 -5.097  10.905  0.40 16.94 ?  123 LEU   A HD12 1 
ATOM   2531 H HD13 A LEU   A 1 123 ? 17.752 -5.010  12.216  0.60 16.80 ?  123 LEU   A HD13 1 
ATOM   2532 H HD13 B LEU   A 1 123 ? 17.688 -4.756  12.451  0.40 16.94 ?  123 LEU   A HD13 1 
ATOM   2533 H HD21 A LEU   A 1 123 ? 18.646 -2.123  12.092  0.60 16.41 ?  123 LEU   A HD21 1 
ATOM   2534 H HD21 B LEU   A 1 123 ? 18.902 -2.054  12.337  0.40 16.77 ?  123 LEU   A HD21 1 
ATOM   2535 H HD22 A LEU   A 1 123 ? 19.181 -3.103  13.222  0.60 16.41 ?  123 LEU   A HD22 1 
ATOM   2536 H HD22 B LEU   A 1 123 ? 19.350 -3.073  13.471  0.40 16.77 ?  123 LEU   A HD22 1 
ATOM   2537 H HD23 A LEU   A 1 123 ? 20.208 -2.358  12.265  0.60 16.41 ?  123 LEU   A HD23 1 
ATOM   2538 H HD23 B LEU   A 1 123 ? 20.437 -2.425  12.510  0.40 16.77 ?  123 LEU   A HD23 1 
ATOM   2539 N N    A ALA   A 1 124 ? 19.754 -5.778  8.441   0.60 11.91 ?  124 ALA   A N    1 
ATOM   2540 N N    B ALA   A 1 124 ? 19.780 -5.819  8.584   0.40 10.95 ?  124 ALA   A N    1 
ATOM   2541 C CA   A ALA   A 1 124 ? 20.047 -5.559  7.031   0.60 12.16 ?  124 ALA   A CA   1 
ATOM   2542 C CA   B ALA   A 1 124 ? 20.024 -5.459  7.196   0.40 10.45 ?  124 ALA   A CA   1 
ATOM   2543 C C    A ALA   A 1 124 ? 18.815 -5.135  6.242   0.60 11.51 ?  124 ALA   A C    1 
ATOM   2544 C C    B ALA   A 1 124 ? 18.764 -4.968  6.504   0.40 10.43 ?  124 ALA   A C    1 
ATOM   2545 O O    A ALA   A 1 124 ? 17.687 -5.505  6.589   0.60 11.72 ?  124 ALA   A O    1 
ATOM   2546 O O    B ALA   A 1 124 ? 17.644 -5.269  6.937   0.40 10.70 ?  124 ALA   A O    1 
ATOM   2547 C CB   A ALA   A 1 124 ? 20.640 -6.830  6.406   0.60 12.83 ?  124 ALA   A CB   1 
ATOM   2548 C CB   B ALA   A 1 124 ? 20.569 -6.653  6.400   0.40 10.36 ?  124 ALA   A CB   1 
ATOM   2549 H H    A ALA   A 1 124 ? 18.943 -5.975  8.629   0.60 14.33 ?  124 ALA   A H    1 
ATOM   2550 H H    B ALA   A 1 124 ? 19.033 -6.220  8.720   0.40 13.17 ?  124 ALA   A H    1 
ATOM   2551 H HA   A ALA   A 1 124 ? 20.725 -4.867  6.972   0.60 14.62 ?  124 ALA   A HA   1 
ATOM   2552 H HA   B ALA   A 1 124 ? 20.687 -4.755  7.164   0.40 12.56 ?  124 ALA   A HA   1 
ATOM   2553 H HB1  A ALA   A 1 124 ? 20.834 -6.667  5.472   0.60 15.42 ?  124 ALA   A HB1  1 
ATOM   2554 H HB1  B ALA   A 1 124 ? 20.719 -6.379  5.480   0.40 12.46 ?  124 ALA   A HB1  1 
ATOM   2555 H HB2  A ALA   A 1 124 ? 21.461 -7.071  6.874   0.60 15.42 ?  124 ALA   A HB2  1 
ATOM   2556 H HB2  B ALA   A 1 124 ? 21.404 -6.944  6.798   0.40 12.46 ?  124 ALA   A HB2  1 
ATOM   2557 H HB3  A ALA   A 1 124 ? 19.997 -7.554  6.491   0.60 15.42 ?  124 ALA   A HB3  1 
ATOM   2558 H HB3  B ALA   A 1 124 ? 19.920 -7.374  6.426   0.40 12.46 ?  124 ALA   A HB3  1 
ATOM   2559 N N    A PRO   A 1 125 ? 19.008 -4.392  5.160   0.60 11.02 ?  125 PRO   A N    1 
ATOM   2560 N N    B PRO   A 1 125 ? 18.919 -4.216  5.416   0.40 10.85 ?  125 PRO   A N    1 
ATOM   2561 C CA   A PRO   A 1 125 ? 17.941 -4.137  4.197   0.60 10.99 ?  125 PRO   A CA   1 
ATOM   2562 C CA   B PRO   A 1 125 ? 17.831 -4.020  4.460   0.40 11.47 ?  125 PRO   A CA   1 
ATOM   2563 C C    A PRO   A 1 125 ? 17.994 -5.188  3.093   0.60 11.01 ?  125 PRO   A C    1 
ATOM   2564 C C    B PRO   A 1 125 ? 17.933 -5.084  3.369   0.40 11.36 ?  125 PRO   A C    1 
ATOM   2565 O O    A PRO   A 1 125 ? 18.977 -5.914  2.936   0.60 11.49 ?  125 PRO   A O    1 
ATOM   2566 O O    B PRO   A 1 125 ? 18.915 -5.824  3.285   0.40 11.53 ?  125 PRO   A O    1 
ATOM   2567 C CB   A PRO   A 1 125 ? 18.371 -2.786  3.623   0.60 10.78 ?  125 PRO   A CB   1 
ATOM   2568 C CB   B PRO   A 1 125 ? 18.159 -2.631  3.892   0.40 12.07 ?  125 PRO   A CB   1 
ATOM   2569 C CG   A PRO   A 1 125 ? 19.881 -2.931  3.546   0.60 10.28 ?  125 PRO   A CG   1 
ATOM   2570 C CG   B PRO   A 1 125 ? 19.665 -2.638  3.829   0.40 12.23 ?  125 PRO   A CG   1 
ATOM   2571 C CD   A PRO   A 1 125 ? 20.275 -3.764  4.747   0.60 10.25 ?  125 PRO   A CD   1 
ATOM   2572 C CD   B PRO   A 1 125 ? 20.133 -3.472  5.010   0.40 11.53 ?  125 PRO   A CD   1 
ATOM   2573 H HA   A PRO   A 1 125 ? 17.060 -4.105  4.621   0.60 13.22 ?  125 PRO   A HA   1 
ATOM   2574 H HA   B PRO   A 1 125 ? 16.970 -4.024  4.886   0.40 13.80 ?  125 PRO   A HA   1 
ATOM   2575 H HB2  A PRO   A 1 125 ? 17.972 -2.671  2.747   0.60 12.96 ?  125 PRO   A HB2  1 
ATOM   2576 H HB2  B PRO   A 1 125 ? 17.769 -2.521  3.008   0.40 14.52 ?  125 PRO   A HB2  1 
ATOM   2577 H HB3  A PRO   A 1 125 ? 18.104 -2.082  4.230   0.60 12.96 ?  125 PRO   A HB3  1 
ATOM   2578 H HB3  B PRO   A 1 125 ? 17.838 -1.936  4.497   0.40 14.52 ?  125 PRO   A HB3  1 
ATOM   2579 H HG2  A PRO   A 1 125 ? 20.125 -3.384  2.723   0.60 12.36 ?  125 PRO   A HG2  1 
ATOM   2580 H HG2  B PRO   A 1 125 ? 19.950 -3.040  2.992   0.40 14.71 ?  125 PRO   A HG2  1 
ATOM   2581 H HG3  A PRO   A 1 125 ? 20.290 -2.055  3.590   0.60 12.36 ?  125 PRO   A HG3  1 
ATOM   2582 H HG3  B PRO   A 1 125 ? 20.000 -1.728  3.894   0.40 14.71 ?  125 PRO   A HG3  1 
ATOM   2583 H HD2  A PRO   A 1 125 ? 20.925 -4.443  4.502   0.60 12.33 ?  125 PRO   A HD2  1 
ATOM   2584 H HD2  B PRO   A 1 125 ? 20.843 -4.074  4.723   0.40 13.86 ?  125 PRO   A HD2  1 
ATOM   2585 H HD3  A PRO   A 1 125 ? 20.609 -3.198  5.462   0.60 12.33 ?  125 PRO   A HD3  1 
ATOM   2586 H HD3  B PRO   A 1 125 ? 20.441 -2.889  5.723   0.40 13.86 ?  125 PRO   A HD3  1 
ATOM   2587 N N    A LEU   A 1 126 ? 16.927 -5.233  2.306   0.60 11.43 ?  126 LEU   A N    1 
ATOM   2588 N N    B LEU   A 1 126 ? 16.892 -5.158  2.536   0.40 11.91 ?  126 LEU   A N    1 
ATOM   2589 C CA   A LEU   A 1 126 ? 16.932 -6.031  1.089   0.60 11.55 ?  126 LEU   A CA   1 
ATOM   2590 C CA   B LEU   A 1 126 ? 17.010 -5.906  1.290   0.40 12.54 ?  126 LEU   A CA   1 
ATOM   2591 C C    A LEU   A 1 126 ? 17.868 -5.406  0.062   0.60 11.47 ?  126 LEU   A C    1 
ATOM   2592 C C    B LEU   A 1 126 ? 17.907 -5.138  0.322   0.40 13.08 ?  126 LEU   A C    1 
ATOM   2593 O O    A LEU   A 1 126 ? 17.632 -4.293  -0.427  0.60 11.71 ?  126 LEU   A O    1 
ATOM   2594 O O    B LEU   A 1 126 ? 17.929 -3.907  0.314   0.40 14.43 ?  126 LEU   A O    1 
ATOM   2595 C CB   A LEU   A 1 126 ? 15.518 -6.144  0.535   0.60 12.54 ?  126 LEU   A CB   1 
ATOM   2596 C CB   B LEU   A 1 126 ? 15.633 -6.124  0.653   0.40 13.35 ?  126 LEU   A CB   1 
ATOM   2597 C CG   A LEU   A 1 126 ? 14.600 -7.000  1.409   0.60 13.40 ?  126 LEU   A CG   1 
ATOM   2598 C CG   B LEU   A 1 126 ? 14.682 -7.152  1.284   0.40 14.06 ?  126 LEU   A CG   1 
ATOM   2599 C CD1  A LEU   A 1 126 ? 13.153 -6.841  0.990   0.60 14.17 ?  126 LEU   A CD1  1 
ATOM   2600 C CD1  B LEU   A 1 126 ? 13.299 -7.085  0.634   0.40 14.46 ?  126 LEU   A CD1  1 
ATOM   2601 C CD2  A LEU   A 1 126 ? 15.007 -8.471  1.342   0.60 13.75 ?  126 LEU   A CD2  1 
ATOM   2602 C CD2  B LEU   A 1 126 ? 15.241 -8.572  1.188   0.40 14.38 ?  126 LEU   A CD2  1 
ATOM   2603 H H    A LEU   A 1 126 ? 16.194 -4.812  2.452   0.60 13.75 ?  126 LEU   A H    1 
ATOM   2604 H H    B LEU   A 1 126 ? 16.114 -4.798  2.652   0.40 14.32 ?  126 LEU   A H    1 
ATOM   2605 H HA   A LEU   A 1 126 ? 17.252 -6.924  1.288   0.60 13.89 ?  126 LEU   A HA   1 
ATOM   2606 H HA   B LEU   A 1 126 ? 17.409 -6.770  1.461   0.40 15.07 ?  126 LEU   A HA   1 
ATOM   2607 H HB2  A LEU   A 1 126 ? 15.127 -5.259  0.473   0.60 15.07 ?  126 LEU   A HB2  1 
ATOM   2608 H HB2  B LEU   A 1 126 ? 15.163 -5.276  0.657   0.40 16.05 ?  126 LEU   A HB2  1 
ATOM   2609 H HB3  A LEU   A 1 126 ? 15.551 -6.553  -0.345  0.60 15.07 ?  126 LEU   A HB3  1 
ATOM   2610 H HB3  B LEU   A 1 126 ? 15.766 -6.404  -0.267  0.40 16.05 ?  126 LEU   A HB3  1 
ATOM   2611 H HG   A LEU   A 1 126 ? 14.672 -6.710  2.332   0.60 16.11 ?  126 LEU   A HG   1 
ATOM   2612 H HG   B LEU   A 1 126 ? 14.568 -6.942  2.223   0.40 16.90 ?  126 LEU   A HG   1 
ATOM   2613 H HD11 A LEU   A 1 126 ? 12.592 -7.392  1.562   0.60 17.03 ?  126 LEU   A HD11 1 
ATOM   2614 H HD11 B LEU   A 1 126 ? 12.714 -7.736  1.057   0.40 17.38 ?  126 LEU   A HD11 1 
ATOM   2615 H HD12 A LEU   A 1 126 ? 12.898 -5.910  1.078   0.60 17.03 ?  126 LEU   A HD12 1 
ATOM   2616 H HD12 B LEU   A 1 126 ? 12.935 -6.192  0.752   0.40 17.38 ?  126 LEU   A HD12 1 
ATOM   2617 H HD13 A LEU   A 1 126 ? 13.057 -7.125  0.067   0.60 17.03 ?  126 LEU   A HD13 1 
ATOM   2618 H HD13 B LEU   A 1 126 ? 13.382 -7.284  -0.312  0.40 17.38 ?  126 LEU   A HD13 1 
ATOM   2619 H HD21 A LEU   A 1 126 ? 14.321 -9.012  1.760   0.60 16.53 ?  126 LEU   A HD21 1 
ATOM   2620 H HD21 B LEU   A 1 126 ? 14.589 -9.195  1.550   0.40 17.28 ?  126 LEU   A HD21 1 
ATOM   2621 H HD22 A LEU   A 1 126 ? 15.109 -8.727  0.411   0.60 16.53 ?  126 LEU   A HD22 1 
ATOM   2622 H HD22 B LEU   A 1 126 ? 15.414 -8.781  0.257   0.40 17.28 ?  126 LEU   A HD22 1 
ATOM   2623 H HD23 A LEU   A 1 126 ? 15.850 -8.586  1.809   0.60 16.53 ?  126 LEU   A HD23 1 
ATOM   2624 H HD23 B LEU   A 1 126 ? 16.063 -8.620  1.698   0.40 17.28 ?  126 LEU   A HD23 1 
ATOM   2625 N N    A LEU   A 1 127 ? 18.930 -6.132  -0.268  0.60 11.27 ?  127 LEU   A N    1 
ATOM   2626 N N    B LEU   A 1 127 ? 18.674 -5.869  -0.484  0.40 13.20 ?  127 LEU   A N    1 
ATOM   2627 C CA   A LEU   A 1 127 ? 19.922 -5.625  -1.202  0.60 10.55 ?  127 LEU   A CA   1 
ATOM   2628 C CA   B LEU   A 1 127 ? 19.616 -5.252  -1.410  0.40 14.82 ?  127 LEU   A CA   1 
ATOM   2629 C C    A LEU   A 1 127 ? 19.317 -5.452  -2.586  0.60 9.95  ?  127 LEU   A C    1 
ATOM   2630 C C    B LEU   A 1 127 ? 19.020 -5.122  -2.812  0.40 16.10 ?  127 LEU   A C    1 
ATOM   2631 O O    A LEU   A 1 127 ? 18.499 -6.264  -3.039  0.60 10.28 ?  127 LEU   A O    1 
ATOM   2632 O O    B LEU   A 1 127 ? 18.107 -5.859  -3.197  0.40 16.22 ?  127 LEU   A O    1 
ATOM   2633 C CB   A LEU   A 1 127 ? 21.111 -6.583  -1.281  0.60 11.13 ?  127 LEU   A CB   1 
ATOM   2634 C CB   B LEU   A 1 127 ? 20.937 -6.033  -1.461  0.40 15.31 ?  127 LEU   A CB   1 
ATOM   2635 C CG   A LEU   A 1 127 ? 21.898 -6.817  0.006   0.60 11.89 ?  127 LEU   A CG   1 
ATOM   2636 C CG   B LEU   A 1 127 ? 21.724 -6.113  -0.142  0.40 15.55 ?  127 LEU   A CG   1 
ATOM   2637 C CD1  A LEU   A 1 127 ? 23.004 -7.817  -0.244  0.60 12.16 ?  127 LEU   A CD1  1 
ATOM   2638 C CD1  B LEU   A 1 127 ? 22.957 -7.014  -0.263  0.40 16.02 ?  127 LEU   A CD1  1 
ATOM   2639 C CD2  A LEU   A 1 127 ? 22.491 -5.530  0.519   0.60 13.01 ?  127 LEU   A CD2  1 
ATOM   2640 C CD2  B LEU   A 1 127 ? 22.121 -4.720  0.341   0.40 15.45 ?  127 LEU   A CD2  1 
ATOM   2641 H H    A LEU   A 1 127 ? 19.103 -6.917  0.047   0.60 13.55 ?  127 LEU   A H    1 
ATOM   2642 H H    B LEU   A 1 127 ? 18.685 -6.733  -0.496  0.40 15.87 ?  127 LEU   A H    1 
ATOM   2643 H HA   A LEU   A 1 127 ? 20.244 -4.765  -0.895  0.60 12.68 ?  127 LEU   A HA   1 
ATOM   2644 H HA   B LEU   A 1 127 ? 19.817 -4.358  -1.092  0.40 17.82 ?  127 LEU   A HA   1 
ATOM   2645 H HB2  A LEU   A 1 127 ? 20.787 -7.446  -1.581  0.60 13.39 ?  127 LEU   A HB2  1 
ATOM   2646 H HB2  B LEU   A 1 127 ? 20.748 -6.940  -1.739  0.40 18.40 ?  127 LEU   A HB2  1 
ATOM   2647 H HB3  A LEU   A 1 127 ? 21.737 -6.232  -1.937  0.60 13.39 ?  127 LEU   A HB3  1 
ATOM   2648 H HB3  B LEU   A 1 127 ? 21.516 -5.608  -2.115  0.40 18.40 ?  127 LEU   A HB3  1 
ATOM   2649 H HG   A LEU   A 1 127 ? 21.307 -7.179  0.686   0.60 14.29 ?  127 LEU   A HG   1 
ATOM   2650 H HG   B LEU   A 1 127 ? 21.152 -6.502  0.533   0.40 18.69 ?  127 LEU   A HG   1 
ATOM   2651 H HD11 A LEU   A 1 127 ? 23.477 -7.982  0.588   0.60 14.62 ?  127 LEU   A HD11 1 
ATOM   2652 H HD11 B LEU   A 1 127 ? 23.420 -7.036  0.592   0.40 19.26 ?  127 LEU   A HD11 1 
ATOM   2653 H HD12 A LEU   A 1 127 ? 22.618 -8.643  -0.574  0.60 14.62 ?  127 LEU   A HD12 1 
ATOM   2654 H HD12 B LEU   A 1 127 ? 22.673 -7.910  -0.505  0.40 19.26 ?  127 LEU   A HD12 1 
ATOM   2655 H HD13 A LEU   A 1 127 ? 23.616 -7.452  -0.903  0.60 14.62 ?  127 LEU   A HD13 1 
ATOM   2656 H HD13 B LEU   A 1 127 ? 23.548 -6.659  -0.946  0.40 19.26 ?  127 LEU   A HD13 1 
ATOM   2657 H HD21 A LEU   A 1 127 ? 23.072 -5.729  1.270   0.60 15.65 ?  127 LEU   A HD21 1 
ATOM   2658 H HD21 B LEU   A 1 127 ? 22.722 -4.807  1.097   0.40 18.57 ?  127 LEU   A HD21 1 
ATOM   2659 H HD22 A LEU   A 1 127 ? 23.006 -5.118  -0.195  0.60 15.65 ?  127 LEU   A HD22 1 
ATOM   2660 H HD22 B LEU   A 1 127 ? 22.564 -4.249  -0.382  0.40 18.57 ?  127 LEU   A HD22 1 
ATOM   2661 H HD23 A LEU   A 1 127 ? 21.776 -4.941  0.796   0.60 15.65 ?  127 LEU   A HD23 1 
ATOM   2662 H HD23 B LEU   A 1 127 ? 21.321 -4.241  0.607   0.40 18.57 ?  127 LEU   A HD23 1 
ATOM   2663 N N    A SER   A 1 128 ? 19.743 -4.390  -3.261  0.60 10.48 ?  128 SER   A N    1 
ATOM   2664 N N    B SER   A 1 128 ? 19.536 -4.143  -3.559  0.40 17.17 ?  128 SER   A N    1 
ATOM   2665 C CA   A SER   A 1 128 ? 19.349 -4.013  -4.611  0.60 10.34 ?  128 SER   A CA   1 
ATOM   2666 C CA   B SER   A 1 128 ? 19.173 -3.887  -4.956  0.40 18.53 ?  128 SER   A CA   1 
ATOM   2667 C C    A SER   A 1 128 ? 17.895 -3.555  -4.728  0.60 10.54 ?  128 SER   A C    1 
ATOM   2668 C C    B SER   A 1 128 ? 17.691 -3.513  -5.088  0.40 20.52 ?  128 SER   A C    1 
ATOM   2669 O O    A SER   A 1 128 ? 17.462 -3.255  -5.834  0.60 11.12 ?  128 SER   A O    1 
ATOM   2670 O O    B SER   A 1 128 ? 16.873 -4.255  -5.636  0.40 21.42 ?  128 SER   A O    1 
ATOM   2671 C CB   A SER   A 1 128 ? 19.682 -5.085  -5.661  0.60 11.36 ?  128 SER   A CB   1 
ATOM   2672 C CB   B SER   A 1 128 ? 19.547 -5.073  -5.857  0.40 18.11 ?  128 SER   A CB   1 
ATOM   2673 O OG   A SER   A 1 128 ? 21.083 -5.291  -5.729  0.60 12.23 ?  128 SER   A OG   1 
ATOM   2674 O OG   B SER   A 1 128 ? 20.946 -5.306  -5.860  0.40 17.79 ?  128 SER   A OG   1 
ATOM   2675 H H    A SER   A 1 128 ? 20.324 -3.844  -2.930  0.60 12.60 ?  128 SER   A H    1 
ATOM   2676 H H    B SER   A 1 128 ? 20.121 -3.592  -3.260  0.40 20.63 ?  128 SER   A H    1 
ATOM   2677 H HA   A SER   A 1 128 ? 19.885 -3.247  -4.844  0.60 12.43 ?  128 SER   A HA   1 
ATOM   2678 H HA   B SER   A 1 128 ? 19.691 -3.128  -5.257  0.40 22.27 ?  128 SER   A HA   1 
ATOM   2679 H HB2  A SER   A 1 128 ? 19.255 -5.917  -5.425  0.60 13.66 ?  128 SER   A HB2  1 
ATOM   2680 H HB2  B SER   A 1 128 ? 19.097 -5.868  -5.536  0.40 21.76 ?  128 SER   A HB2  1 
ATOM   2681 H HB3  A SER   A 1 128 ? 19.379 -4.781  -6.531  0.60 13.66 ?  128 SER   A HB3  1 
ATOM   2682 H HB3  B SER   A 1 128 ? 19.268 -4.874  -6.763  0.40 21.76 ?  128 SER   A HB3  1 
ATOM   2683 H HG   A SER   A 1 128 ? 21.479 -4.568  -5.916  0.60 14.70 ?  128 SER   A HG   1 
ATOM   2684 H HG   B SER   A 1 128 ? 21.351 -4.621  -6.130  0.40 21.37 ?  128 SER   A HG   1 
ATOM   2685 N N    A ALA   A 1 129 ? 17.148 -3.491  -3.628  0.60 10.71 ?  129 ALA   A N    1 
ATOM   2686 N N    B ALA   A 1 129 ? 17.365 -2.314  -4.594  0.40 22.01 ?  129 ALA   A N    1 
ATOM   2687 C CA   A ALA   A 1 129 ? 15.776 -3.010  -3.643  0.60 11.91 ?  129 ALA   A CA   1 
ATOM   2688 C CA   B ALA   A 1 129 ? 15.977 -1.868  -4.655  0.40 23.24 ?  129 ALA   A CA   1 
ATOM   2689 C C    A ALA   A 1 129 ? 15.763 -1.484  -3.574  0.60 11.90 ?  129 ALA   A C    1 
ATOM   2690 C C    B ALA   A 1 129 ? 15.531 -1.503  -6.068  0.40 23.90 ?  129 ALA   A C    1 
ATOM   2691 O O    A ALA   A 1 129 ? 16.802 -0.822  -3.610  0.60 12.56 ?  129 ALA   A O    1 
ATOM   2692 O O    B ALA   A 1 129 ? 14.323 -1.441  -6.321  0.40 24.11 ?  129 ALA   A O    1 
ATOM   2693 C CB   A ALA   A 1 129 ? 14.978 -3.642  -2.501  0.60 12.72 ?  129 ALA   A CB   1 
ATOM   2694 C CB   B ALA   A 1 129 ? 15.716 -0.710  -3.693  0.40 23.60 ?  129 ALA   A CB   1 
ATOM   2695 H H    A ALA   A 1 129 ? 17.425 -3.722  -2.839  0.60 12.88 ?  129 ALA   A H    1 
ATOM   2696 H H    B ALA   A 1 129 ? 17.908 -1.760  -4.220  0.40 26.44 ?  129 ALA   A H    1 
ATOM   2697 H HA   A ALA   A 1 129 ? 15.363 -3.271  -4.474  0.60 14.32 ?  129 ALA   A HA   1 
ATOM   2698 H HA   B ALA   A 1 129 ? 15.434 -2.601  -4.355  0.40 27.92 ?  129 ALA   A HA   1 
ATOM   2699 H HB1  A ALA   A 1 129 ? 14.064 -3.318  -2.536  0.60 15.30 ?  129 ALA   A HB1  1 
ATOM   2700 H HB1  B ALA   A 1 129 ? 14.779 -0.455  -3.756  0.40 28.35 ?  129 ALA   A HB1  1 
ATOM   2701 H HB2  A ALA   A 1 129 ? 14.990 -4.606  -2.601  0.60 15.30 ?  129 ALA   A HB2  1 
ATOM   2702 H HB2  B ALA   A 1 129 ? 15.914 -1.005  -2.790  0.40 28.35 ?  129 ALA   A HB2  1 
ATOM   2703 H HB3  A ALA   A 1 129 ? 15.382 -3.394  -1.652  0.60 15.30 ?  129 ALA   A HB3  1 
ATOM   2704 H HB3  B ALA   A 1 129 ? 16.280 0.036   -3.934  0.40 28.35 ?  129 ALA   A HB3  1 
ATOM   2705 N N    A GLY   A 1 130 ? 14.565 -0.916  -3.487  0.60 12.28 ?  130 GLY   A N    1 
ATOM   2706 N N    B GLY   A 1 130 ? 16.464 -1.255  -6.990  0.40 24.34 ?  130 GLY   A N    1 
ATOM   2707 C CA   A GLY   A 1 130 ? 14.445 0.531   -3.431  0.60 12.88 ?  130 GLY   A CA   1 
ATOM   2708 C CA   B GLY   A 1 130 ? 16.094 -0.940  -8.361  0.40 24.80 ?  130 GLY   A CA   1 
ATOM   2709 C C    A GLY   A 1 130 ? 15.052 1.170   -4.662  0.60 12.46 ?  130 GLY   A C    1 
ATOM   2710 C C    B GLY   A 1 130 ? 15.403 -2.073  -9.084  0.40 25.39 ?  130 GLY   A C    1 
ATOM   2711 O O    A GLY   A 1 130 ? 14.805 0.743   -5.793  0.60 12.65 ?  130 GLY   A O    1 
ATOM   2712 O O    B GLY   A 1 130 ? 14.814 -1.846  -10.147 0.40 25.29 ?  130 GLY   A O    1 
ATOM   2713 H H    A GLY   A 1 130 ? 13.816 -1.343  -3.461  0.60 14.77 ?  130 GLY   A H    1 
ATOM   2714 H H    B GLY   A 1 130 ? 17.309 -1.276  -6.852  0.40 29.23 ?  130 GLY   A H    1 
ATOM   2715 H HA2  A GLY   A 1 130 ? 13.505 0.779   -3.383  0.60 15.48 ?  130 GLY   A HA2  1 
ATOM   2716 H HA2  B GLY   A 1 130 ? 15.499 -0.176  -8.364  0.40 29.79 ?  130 GLY   A HA2  1 
ATOM   2717 H HA3  A GLY   A 1 130 ? 14.898 0.871   -2.650  0.60 15.48 ?  130 GLY   A HA3  1 
ATOM   2718 H HA3  B GLY   A 1 130 ? 16.888 -0.714  -8.868  0.40 29.79 ?  130 GLY   A HA3  1 
ATOM   2719 N N    A ILE   A 1 131 ? 15.848 2.223   -4.445  0.60 13.14 ?  131 ILE   A N    1 
ATOM   2720 N N    B ILE   A 1 131 ? 15.466 -3.287  -8.534  0.40 26.28 ?  131 ILE   A N    1 
ATOM   2721 C CA   A ILE   A 1 131 ? 16.406 2.987   -5.559  0.60 12.93 ?  131 ILE   A CA   1 
ATOM   2722 C CA   B ILE   A 1 131 ? 14.810 -4.438  -9.144  0.40 27.27 ?  131 ILE   A CA   1 
ATOM   2723 C C    A ILE   A 1 131 ? 17.444 2.221   -6.369  0.60 12.24 ?  131 ILE   A C    1 
ATOM   2724 C C    B ILE   A 1 131 ? 13.346 -4.553  -8.765  0.40 27.74 ?  131 ILE   A C    1 
ATOM   2725 O O    A ILE   A 1 131 ? 17.863 2.710   -7.424  0.60 12.87 ?  131 ILE   A O    1 
ATOM   2726 O O    B ILE   A 1 131 ? 12.618 -5.346  -9.378  0.40 28.02 ?  131 ILE   A O    1 
ATOM   2727 C CB   A ILE   A 1 131 ? 16.941 4.369   -5.121  0.60 14.50 ?  131 ILE   A CB   1 
ATOM   2728 C CB   B ILE   A 1 131 ? 15.541 -5.719  -8.707  0.40 27.70 ?  131 ILE   A CB   1 
ATOM   2729 C CG1  A ILE   A 1 131 ? 18.182 4.231   -4.230  0.60 16.09 ?  131 ILE   A CG1  1 
ATOM   2730 C CG1  B ILE   A 1 131 ? 15.074 -6.165  -7.317  0.40 28.04 ?  131 ILE   A CG1  1 
ATOM   2731 C CG2  A ILE   A 1 131 ? 15.846 5.161   -4.416  0.60 15.03 ?  131 ILE   A CG2  1 
ATOM   2732 C CG2  B ILE   A 1 131 ? 17.037 -5.495  -8.708  0.40 27.69 ?  131 ILE   A CG2  1 
ATOM   2733 C CD1  A ILE   A 1 131 ? 18.808 5.565   -3.839  0.60 17.17 ?  131 ILE   A CD1  1 
ATOM   2734 C CD1  B ILE   A 1 131 ? 15.942 -7.234  -6.690  0.40 28.36 ?  131 ILE   A CD1  1 
ATOM   2735 H H    A ILE   A 1 131 ? 16.066 2.512   -3.669  0.60 15.80 ?  131 ILE   A H    1 
ATOM   2736 H H    B ILE   A 1 131 ? 15.888 -3.468  -7.810  0.40 31.56 ?  131 ILE   A H    1 
ATOM   2737 H HA   A ILE   A 1 131 ? 15.685 3.164   -6.172  0.60 15.54 ?  131 ILE   A HA   1 
ATOM   2738 H HA   B ILE   A 1 131 ? 14.874 -4.374  -10.105 0.40 32.76 ?  131 ILE   A HA   1 
ATOM   2739 H HB   A ILE   A 1 131 ? 17.197 4.857   -5.919  0.60 17.42 ?  131 ILE   A HB   1 
ATOM   2740 H HB   B ILE   A 1 131 ? 15.337 -6.412  -9.345  0.40 33.27 ?  131 ILE   A HB   1 
ATOM   2741 H HG12 A ILE   A 1 131 ? 17.932 3.770   -3.416  0.60 19.34 ?  131 ILE   A HG12 1 
ATOM   2742 H HG12 B ILE   A 1 131 ? 15.067 -5.396  -6.727  0.40 33.67 ?  131 ILE   A HG12 1 
ATOM   2743 H HG13 A ILE   A 1 131 ? 18.857 3.720   -4.705  0.60 19.34 ?  131 ILE   A HG13 1 
ATOM   2744 H HG13 B ILE   A 1 131 ? 14.181 -6.537  -7.386  0.40 33.67 ?  131 ILE   A HG13 1 
ATOM   2745 H HG21 A ILE   A 1 131 ? 16.143 6.074   -4.295  0.60 18.07 ?  131 ILE   A HG21 1 
ATOM   2746 H HG21 B ILE   A 1 131 ? 17.460 -6.337  -8.904  0.40 33.26 ?  131 ILE   A HG21 1 
ATOM   2747 H HG22 A ILE   A 1 131 ? 15.045 5.142   -4.962  0.60 18.07 ?  131 ILE   A HG22 1 
ATOM   2748 H HG22 B ILE   A 1 131 ? 17.267 -4.844  -9.388  0.40 33.26 ?  131 ILE   A HG22 1 
ATOM   2749 H HG23 A ILE   A 1 131 ? 15.667 4.750   -3.555  0.60 18.07 ?  131 ILE   A HG23 1 
ATOM   2750 H HG23 B ILE   A 1 131 ? 17.317 -5.173  -7.837  0.40 33.26 ?  131 ILE   A HG23 1 
ATOM   2751 H HD11 A ILE   A 1 131 ? 19.647 5.395   -3.381  0.60 20.63 ?  131 ILE   A HD11 1 
ATOM   2752 H HD11 B ILE   A 1 131 ? 15.429 -7.691  -6.005  0.40 34.06 ?  131 ILE   A HD11 1 
ATOM   2753 H HD12 A ILE   A 1 131 ? 18.970 6.084   -4.643  0.60 20.63 ?  131 ILE   A HD12 1 
ATOM   2754 H HD12 B ILE   A 1 131 ? 16.210 -7.864  -7.377  0.40 34.06 ?  131 ILE   A HD12 1 
ATOM   2755 H HD13 A ILE   A 1 131 ? 18.201 6.040   -3.253  0.60 20.63 ?  131 ILE   A HD13 1 
ATOM   2756 H HD13 B ILE   A 1 131 ? 16.725 -6.818  -6.298  0.40 34.06 ?  131 ILE   A HD13 1 
ATOM   2757 N N    A PHE   A 1 132 ? 17.863 1.028   -5.926  0.60 11.63 ?  132 PHE   A N    1 
ATOM   2758 N N    B PHE   A 1 132 ? 12.888 -3.780  -7.780  0.40 27.66 ?  132 PHE   A N    1 
ATOM   2759 C CA   A PHE   A 1 132 ? 18.734 0.192   -6.747  0.60 12.04 ?  132 PHE   A CA   1 
ATOM   2760 C CA   B PHE   A 1 132 ? 11.568 -4.011  -7.209  0.40 27.46 ?  132 PHE   A CA   1 
ATOM   2761 C C    A PHE   A 1 132 ? 17.976 -0.559  -7.843  0.60 12.42 ?  132 PHE   A C    1 
ATOM   2762 C C    B PHE   A 1 132 ? 10.436 -3.577  -8.129  0.40 28.20 ?  132 PHE   A C    1 
ATOM   2763 O O    A PHE   A 1 132 ? 18.609 -1.157  -8.716  0.60 13.26 ?  132 PHE   A O    1 
ATOM   2764 O O    B PHE   A 1 132 ? 9.288  -3.964  -7.889  0.40 28.09 ?  132 PHE   A O    1 
ATOM   2765 C CB   A PHE   A 1 132 ? 19.541 -0.788  -5.879  0.60 11.29 ?  132 PHE   A CB   1 
ATOM   2766 C CB   B PHE   A 1 132 ? 11.459 -3.335  -5.843  0.40 26.56 ?  132 PHE   A CB   1 
ATOM   2767 C CG   A PHE   A 1 132 ? 20.767 -0.185  -5.213  0.60 11.12 ?  132 PHE   A CG   1 
ATOM   2768 C CG   B PHE   A 1 132 ? 12.141 -4.096  -4.741  0.40 25.86 ?  132 PHE   A CG   1 
ATOM   2769 C CD1  A PHE   A 1 132 ? 20.654 0.861   -4.313  0.60 12.23 ?  132 PHE   A CD1  1 
ATOM   2770 C CD1  B PHE   A 1 132 ? 13.520 -4.180  -4.690  0.40 25.80 ?  132 PHE   A CD1  1 
ATOM   2771 C CD2  A PHE   A 1 132 ? 22.026 -0.711  -5.458  0.60 11.49 ?  132 PHE   A CD2  1 
ATOM   2772 C CD2  B PHE   A 1 132 ? 11.401 -4.731  -3.761  0.40 25.49 ?  132 PHE   A CD2  1 
ATOM   2773 C CE1  A PHE   A 1 132 ? 21.776 1.393   -3.689  0.60 12.57 ?  132 PHE   A CE1  1 
ATOM   2774 C CE1  B PHE   A 1 132 ? 14.153 -4.879  -3.675  0.40 25.85 ?  132 PHE   A CE1  1 
ATOM   2775 C CE2  A PHE   A 1 132 ? 23.154 -0.183  -4.834  0.60 11.77 ?  132 PHE   A CE2  1 
ATOM   2776 C CE2  B PHE   A 1 132 ? 12.025 -5.433  -2.746  0.40 25.58 ?  132 PHE   A CE2  1 
ATOM   2777 C CZ   A PHE   A 1 132 ? 23.022 0.872   -3.947  0.60 12.11 ?  132 PHE   A CZ   1 
ATOM   2778 C CZ   B PHE   A 1 132 ? 13.404 -5.506  -2.703  0.40 25.79 ?  132 PHE   A CZ   1 
ATOM   2779 H H    A PHE   A 1 132 ? 17.658 0.681   -5.163  0.60 13.99 ?  132 PHE   A H    1 
ATOM   2780 H H    B PHE   A 1 132 ? 13.314 -3.112  -7.442  0.40 33.22 ?  132 PHE   A H    1 
ATOM   2781 H HA   A PHE   A 1 132 ? 19.377 0.764   -7.187  0.60 14.48 ?  132 PHE   A HA   1 
ATOM   2782 H HA   B PHE   A 1 132 ? 11.472 -4.961  -7.063  0.40 32.98 ?  132 PHE   A HA   1 
ATOM   2783 H HB2  A PHE   A 1 132 ? 18.969 -1.125  -5.172  0.60 13.58 ?  132 PHE   A HB2  1 
ATOM   2784 H HB2  B PHE   A 1 132 ? 11.866 -2.456  -5.892  0.40 31.90 ?  132 PHE   A HB2  1 
ATOM   2785 H HB3  A PHE   A 1 132 ? 19.845 -1.528  -6.432  0.60 13.58 ?  132 PHE   A HB3  1 
ATOM   2786 H HB3  B PHE   A 1 132 ? 10.522 -3.254  -5.607  0.40 31.90 ?  132 PHE   A HB3  1 
ATOM   2787 H HD1  A PHE   A 1 132 ? 19.819 1.219   -4.126  0.60 14.71 ?  132 PHE   A HD1  1 
ATOM   2788 H HD1  B PHE   A 1 132 ? 14.033 -3.755  -5.343  0.40 30.99 ?  132 PHE   A HD1  1 
ATOM   2789 H HD2  A PHE   A 1 132 ? 22.127 -1.423  -6.052  0.60 13.81 ?  132 PHE   A HD2  1 
ATOM   2790 H HD2  B PHE   A 1 132 ? 10.474 -4.684  -3.787  0.40 30.62 ?  132 PHE   A HD2  1 
ATOM   2791 H HE1  A PHE   A 1 132 ? 21.684 2.102   -3.092  0.60 15.12 ?  132 PHE   A HE1  1 
ATOM   2792 H HE1  B PHE   A 1 132 ? 15.083 -4.923  -3.650  0.40 31.05 ?  132 PHE   A HE1  1 
ATOM   2793 H HE2  A PHE   A 1 132 ? 23.996 -0.538  -5.015  0.60 14.15 ?  132 PHE   A HE2  1 
ATOM   2794 H HE2  B PHE   A 1 132 ? 11.517 -5.854  -2.093  0.40 30.72 ?  132 PHE   A HE2  1 
ATOM   2795 H HZ   A PHE   A 1 132 ? 23.773 1.230   -3.533  0.60 14.56 ?  132 PHE   A HZ   1 
ATOM   2796 H HZ   B PHE   A 1 132 ? 13.825 -5.976  -2.020  0.40 30.98 ?  132 PHE   A HZ   1 
ATOM   2797 N N    A GLY   A 1 133 ? 16.646 -0.551  -7.823  0.60 11.98 ?  133 GLY   A N    1 
ATOM   2798 N N    B GLY   A 1 133 ? 10.725 -2.794  -9.168  0.40 29.30 ?  133 GLY   A N    1 
ATOM   2799 C CA   A GLY   A 1 133 ? 15.858 -0.916  -8.982  0.60 12.61 ?  133 GLY   A CA   1 
ATOM   2800 C CA   B GLY   A 1 133 ? 9.709  -2.527  -10.172 0.40 30.38 ?  133 GLY   A CA   1 
ATOM   2801 C C    A GLY   A 1 133 ? 15.488 -2.373  -9.150  0.60 12.85 ?  133 GLY   A C    1 
ATOM   2802 C C    B GLY   A 1 133 ? 9.383  -3.761  -10.992 0.40 31.37 ?  133 GLY   A C    1 
ATOM   2803 O O    A GLY   A 1 133 ? 14.796 -2.691  -10.123 0.60 14.57 ?  133 GLY   A O    1 
ATOM   2804 O O    B GLY   A 1 133 ? 8.213  -4.085  -11.214 0.40 31.82 ?  133 GLY   A O    1 
ATOM   2805 H H    A GLY   A 1 133 ? 16.175 -0.321  -7.144  0.60 14.40 ?  133 GLY   A H    1 
ATOM   2806 H H    B GLY   A 1 133 ? 11.483 -2.412  -9.304  0.40 35.18 ?  133 GLY   A H    1 
ATOM   2807 H HA2  A GLY   A 1 133 ? 15.022 -0.429  -8.958  0.60 15.16 ?  133 GLY   A HA2  1 
ATOM   2808 H HA2  B GLY   A 1 133 ? 8.897  -2.218  -9.739  0.40 36.49 ?  133 GLY   A HA2  1 
ATOM   2809 H HA3  A GLY   A 1 133 ? 16.332 -0.649  -9.784  0.60 15.16 ?  133 GLY   A HA3  1 
ATOM   2810 H HA3  B GLY   A 1 133 ? 10.022 -1.832  -10.773 0.40 36.49 ?  133 GLY   A HA3  1 
ATOM   2811 N N    A ALA   A 1 134 ? 15.909 -3.268  -8.257  0.60 12.47 ?  134 ALA   A N    1 
ATOM   2812 N N    B ALA   A 1 134 ? 10.418 -4.473  -11.447 0.40 31.69 ?  134 ALA   A N    1 
ATOM   2813 C CA   A ALA   A 1 134 ? 15.557 -4.673  -8.406  0.60 12.97 ?  134 ALA   A CA   1 
ATOM   2814 C CA   B ALA   A 1 134 ? 10.199 -5.676  -12.244 0.40 31.66 ?  134 ALA   A CA   1 
ATOM   2815 C C    A ALA   A 1 134 ? 14.197 -4.964  -7.780  0.60 13.12 ?  134 ALA   A C    1 
ATOM   2816 C C    B ALA   A 1 134 ? 9.695  -6.832  -11.387 0.40 31.37 ?  134 ALA   A C    1 
ATOM   2817 O O    A ALA   A 1 134 ? 13.670 -4.185  -6.984  0.60 14.18 ?  134 ALA   A O    1 
ATOM   2818 O O    B ALA   A 1 134 ? 8.845  -7.614  -11.827 0.40 31.50 ?  134 ALA   A O    1 
ATOM   2819 C CB   A ALA   A 1 134 ? 16.611 -5.587  -7.779  0.60 13.49 ?  134 ALA   A CB   1 
ATOM   2820 C CB   B ALA   A 1 134 ? 11.493 -6.072  -12.954 0.40 31.84 ?  134 ALA   A CB   1 
ATOM   2821 H H    A ALA   A 1 134 ? 16.402 -3.087  -7.563  0.60 14.99 ?  134 ALA   A H    1 
ATOM   2822 H H    B ALA   A 1 134 ? 11.244 -4.275  -11.314 0.40 38.06 ?  134 ALA   A H    1 
ATOM   2823 H HA   A ALA   A 1 134 ? 15.506 -4.885  -9.349  0.60 15.59 ?  134 ALA   A HA   1 
ATOM   2824 H HA   B ALA   A 1 134 ? 9.532  -5.487  -12.921 0.40 38.02 ?  134 ALA   A HA   1 
ATOM   2825 H HB1  A ALA   A 1 134 ? 16.348 -6.510  -7.914  0.60 16.21 ?  134 ALA   A HB1  1 
ATOM   2826 H HB1  B ALA   A 1 134 ? 11.332 -6.874  -13.477 0.40 38.24 ?  134 ALA   A HB1  1 
ATOM   2827 H HB2  A ALA   A 1 134 ? 17.467 -5.422  -8.209  0.60 16.21 ?  134 ALA   A HB2  1 
ATOM   2828 H HB2  B ALA   A 1 134 ? 11.769 -5.348  -13.536 0.40 38.24 ?  134 ALA   A HB2  1 
ATOM   2829 H HB3  A ALA   A 1 134 ? 16.676 -5.395  -6.831  0.60 16.21 ?  134 ALA   A HB3  1 
ATOM   2830 H HB3  B ALA   A 1 134 ? 12.179 -6.244  -12.289 0.40 38.24 ?  134 ALA   A HB3  1 
ATOM   2831 N N    A ASP   A 1 135 ? 13.642 -6.119  -8.142  0.60 13.19 ?  135 ASP   A N    1 
ATOM   2832 N N    B ASP   A 1 135 ? 10.212 -6.961  -10.168 0.40 30.84 ?  135 ASP   A N    1 
ATOM   2833 C CA   A ASP   A 1 135 ? 12.376 -6.588  -7.579  0.60 14.17 ?  135 ASP   A CA   1 
ATOM   2834 C CA   B ASP   A 1 135 ? 9.848  -8.058  -9.282  0.40 30.32 ?  135 ASP   A CA   1 
ATOM   2835 C C    A ASP   A 1 135 ? 12.601 -7.030  -6.138  0.60 13.47 ?  135 ASP   A C    1 
ATOM   2836 C C    B ASP   A 1 135 ? 10.143 -7.660  -7.840  0.40 29.49 ?  135 ASP   A C    1 
ATOM   2837 O O    A ASP   A 1 135 ? 13.383 -7.952  -5.905  0.60 13.05 ?  135 ASP   A O    1 
ATOM   2838 O O    B ASP   A 1 135 ? 11.310 -7.647  -7.427  0.40 29.46 ?  135 ASP   A O    1 
ATOM   2839 C CB   A ASP   A 1 135 ? 11.885 -7.767  -8.419  0.60 16.86 ?  135 ASP   A CB   1 
ATOM   2840 C CB   B ASP   A 1 135 ? 10.631 -9.317  -9.654  0.40 30.67 ?  135 ASP   A CB   1 
ATOM   2841 C CG   A ASP   A 1 135 ? 10.589 -8.388  -7.896  0.60 19.28 ?  135 ASP   A CG   1 
ATOM   2842 C CG   B ASP   A 1 135 ? 10.181 -10.537 -8.872  0.40 30.93 ?  135 ASP   A CG   1 
ATOM   2843 O OD1  A ASP   A 1 135 ? 10.024 -7.895  -6.898  0.60 19.57 ?  135 ASP   A OD1  1 
ATOM   2844 O OD1  B ASP   A 1 135 ? 9.268  -10.402 -8.030  0.40 30.92 ?  135 ASP   A OD1  1 
ATOM   2845 O OD2  A ASP   A 1 135 ? 10.134 -9.382  -8.504  0.60 22.02 -1 135 ASP   A OD2  1 
ATOM   2846 O OD2  B ASP   A 1 135 ? 10.738 -11.632 -9.100  0.40 31.07 -1 135 ASP   A OD2  1 
ATOM   2847 H H    A ASP   A 1 135 ? 13.982 -6.655  -8.724  0.60 15.85 ?  135 ASP   A H    1 
ATOM   2848 H H    B ASP   A 1 135 ? 10.782 -6.419  -9.828  0.40 37.03 ?  135 ASP   A H    1 
ATOM   2849 H HA   A ASP   A 1 135 ? 11.716 -5.880  -7.615  0.60 17.04 ?  135 ASP   A HA   1 
ATOM   2850 H HA   B ASP   A 1 135 ? 8.905  -8.258  -9.380  0.40 36.41 ?  135 ASP   A HA   1 
ATOM   2851 H HB2  A ASP   A 1 135 ? 11.725 -7.463  -9.325  0.60 20.26 ?  135 ASP   A HB2  1 
ATOM   2852 H HB2  B ASP   A 1 135 ? 10.506 -9.495  -10.600 0.40 36.83 ?  135 ASP   A HB2  1 
ATOM   2853 H HB3  A ASP   A 1 135 ? 12.564 -8.459  -8.417  0.60 20.26 ?  135 ASP   A HB3  1 
ATOM   2854 H HB3  B ASP   A 1 135 ? 11.571 -9.170  -9.467  0.40 36.83 ?  135 ASP   A HB3  1 
ATOM   2855 N N    A PRO   A 1 136 ? 11.963 -6.407  -5.148  0.60 13.12 ?  136 PRO   A N    1 
ATOM   2856 N N    B PRO   A 1 136 ? 9.123  -7.331  -7.045  0.40 28.57 ?  136 PRO   A N    1 
ATOM   2857 C CA   A PRO   A 1 136 ? 12.211 -6.809  -3.752  0.60 13.24 ?  136 PRO   A CA   1 
ATOM   2858 C CA   B PRO   A 1 136 ? 9.350  -6.911  -5.657  0.40 27.74 ?  136 PRO   A CA   1 
ATOM   2859 C C    A PRO   A 1 136 ? 11.808 -8.236  -3.430  0.60 12.55 ?  136 PRO   A C    1 
ATOM   2860 C C    B PRO   A 1 136 ? 9.634  -8.049  -4.689  0.40 26.73 ?  136 PRO   A C    1 
ATOM   2861 O O    A PRO   A 1 136 ? 12.419 -8.842  -2.548  0.60 11.33 ?  136 PRO   A O    1 
ATOM   2862 O O    B PRO   A 1 136 ? 9.601  -7.828  -3.476  0.40 26.93 ?  136 PRO   A O    1 
ATOM   2863 C CB   A PRO   A 1 136 ? 11.411 -5.783  -2.938  0.60 14.38 ?  136 PRO   A CB   1 
ATOM   2864 C CB   B PRO   A 1 136 ? 8.017  -6.236  -5.302  0.40 28.01 ?  136 PRO   A CB   1 
ATOM   2865 C CG   A PRO   A 1 136 ? 10.395 -5.248  -3.891  0.60 15.46 ?  136 PRO   A CG   1 
ATOM   2866 C CG   B PRO   A 1 136 ? 7.012  -6.988  -6.101  0.40 28.21 ?  136 PRO   A CG   1 
ATOM   2867 C CD   A PRO   A 1 136 ? 11.036 -5.270  -5.239  0.60 14.29 ?  136 PRO   A CD   1 
ATOM   2868 C CD   B PRO   A 1 136 ? 7.693  -7.322  -7.399  0.40 28.39 ?  136 PRO   A CD   1 
ATOM   2869 H HA   A PRO   A 1 136 ? 13.155 -6.701  -3.541  0.60 15.91 ?  136 PRO   A HA   1 
ATOM   2870 H HA   B PRO   A 1 136 ? 10.068 -6.259  -5.613  0.40 33.32 ?  136 PRO   A HA   1 
ATOM   2871 H HB2  A PRO   A 1 136 ? 10.979 -6.224  -2.189  0.60 17.28 ?  136 PRO   A HB2  1 
ATOM   2872 H HB2  B PRO   A 1 136 ? 7.843  -6.322  -4.352  0.40 33.65 ?  136 PRO   A HB2  1 
ATOM   2873 H HB3  A PRO   A 1 136 ? 12.000 -5.078  -2.629  0.60 17.28 ?  136 PRO   A HB3  1 
ATOM   2874 H HB3  B PRO   A 1 136 ? 8.042  -5.305  -5.568  0.40 33.65 ?  136 PRO   A HB3  1 
ATOM   2875 H HG2  A PRO   A 1 136 ? 9.611  -5.814  -3.880  0.60 18.58 ?  136 PRO   A HG2  1 
ATOM   2876 H HG2  B PRO   A 1 136 ? 6.764  -7.800  -5.630  0.40 33.88 ?  136 PRO   A HG2  1 
ATOM   2877 H HG3  A PRO   A 1 136 ? 10.167 -4.340  -3.643  0.60 18.58 ?  136 PRO   A HG3  1 
ATOM   2878 H HG3  B PRO   A 1 136 ? 6.236  -6.431  -6.258  0.40 33.88 ?  136 PRO   A HG3  1 
ATOM   2879 H HD2  A PRO   A 1 136 ? 10.369 -5.435  -5.927  0.60 17.18 ?  136 PRO   A HD2  1 
ATOM   2880 H HD2  B PRO   A 1 136 ? 7.418  -8.200  -7.713  0.40 34.09 ?  136 PRO   A HD2  1 
ATOM   2881 H HD3  A PRO   A 1 136 ? 11.522 -4.447  -5.406  0.60 17.18 ?  136 PRO   A HD3  1 
ATOM   2882 H HD3  B PRO   A 1 136 ? 7.519  -6.638  -8.065  0.40 34.09 ?  136 PRO   A HD3  1 
ATOM   2883 N N    A ILE   A 1 137 ? 10.783 -8.779  -4.090  0.60 12.52 ?  137 ILE   A N    1 
ATOM   2884 N N    B ILE   A 1 137 ? 9.915  -9.244  -5.200  0.40 25.39 ?  137 ILE   A N    1 
ATOM   2885 C CA   A ILE   A 1 137 ? 10.408 -10.172 -3.868  0.60 13.09 ?  137 ILE   A CA   1 
ATOM   2886 C CA   B ILE   A 1 137 ? 10.056 -10.443 -4.382  0.40 23.73 ?  137 ILE   A CA   1 
ATOM   2887 C C    A ILE   A 1 137 ? 11.557 -11.086 -4.269  0.60 12.47 ?  137 ILE   A C    1 
ATOM   2888 C C    B ILE   A 1 137 ? 11.417 -11.104 -4.548  0.40 21.40 ?  137 ILE   A C    1 
ATOM   2889 O O    A ILE   A 1 137 ? 11.895 -12.041 -3.559  0.60 12.86 ?  137 ILE   A O    1 
ATOM   2890 O O    B ILE   A 1 137 ? 11.785 -11.956 -3.724  0.40 21.46 ?  137 ILE   A O    1 
ATOM   2891 C CB   A ILE   A 1 137 ? 9.110  -10.500 -4.633  0.60 14.50 ?  137 ILE   A CB   1 
ATOM   2892 C CB   B ILE   A 1 137 ? 8.922  -11.445 -4.700  0.40 24.47 ?  137 ILE   A CB   1 
ATOM   2893 C CG1  A ILE   A 1 137 ? 7.948  -9.633  -4.129  0.60 16.30 ?  137 ILE   A CG1  1 
ATOM   2894 C CG1  B ILE   A 1 137 ? 7.563  -10.766 -4.510  0.40 24.78 ?  137 ILE   A CG1  1 
ATOM   2895 C CG2  A ILE   A 1 137 ? 8.783  -11.991 -4.522  0.60 14.75 ?  137 ILE   A CG2  1 
ATOM   2896 C CG2  B ILE   A 1 137 ? 8.972  -12.663 -3.822  0.40 24.70 ?  137 ILE   A CG2  1 
ATOM   2897 C CD1  A ILE   A 1 137 ? 6.664  -9.799  -4.918  0.60 17.73 ?  137 ILE   A CD1  1 
ATOM   2898 C CD1  B ILE   A 1 137 ? 6.746  -10.657 -5.775  0.40 25.02 ?  137 ILE   A CD1  1 
ATOM   2899 H H    A ILE   A 1 137 ? 10.293 -8.361  -4.661  0.60 15.06 ?  137 ILE   A H    1 
ATOM   2900 H H    B ILE   A 1 137 ? 10.032 -9.389  -6.036  0.40 30.50 ?  137 ILE   A H    1 
ATOM   2901 H HA   A ILE   A 1 137 ? 10.247 -10.308 -2.925  0.60 15.73 ?  137 ILE   A HA   1 
ATOM   2902 H HA   B ILE   A 1 137 ? 9.968  -10.191 -3.449  0.40 28.51 ?  137 ILE   A HA   1 
ATOM   2903 H HB   A ILE   A 1 137 ? 9.251  -10.296 -5.565  0.60 17.42 ?  137 ILE   A HB   1 
ATOM   2904 H HB   B ILE   A 1 137 ? 9.008  -11.725 -5.622  0.40 29.39 ?  137 ILE   A HB   1 
ATOM   2905 H HG12 A ILE   A 1 137 ? 7.765  -9.859  -3.204  0.60 19.58 ?  137 ILE   A HG12 1 
ATOM   2906 H HG12 B ILE   A 1 137 ? 7.047  -11.281 -3.873  0.40 29.77 ?  137 ILE   A HG12 1 
ATOM   2907 H HG13 A ILE   A 1 137 ? 8.212  -8.698  -4.188  0.60 19.58 ?  137 ILE   A HG13 1 
ATOM   2908 H HG13 B ILE   A 1 137 ? 7.702  -9.870  -4.166  0.40 29.77 ?  137 ILE   A HG13 1 
ATOM   2909 H HG21 A ILE   A 1 137 ? 7.891  -12.160 -4.871  0.60 17.72 ?  137 ILE   A HG21 1 
ATOM   2910 H HG21 B ILE   A 1 137 ? 8.327  -13.306 -4.155  0.40 29.67 ?  137 ILE   A HG21 1 
ATOM   2911 H HG22 A ILE   A 1 137 ? 9.428  -12.498 -5.037  0.60 17.72 ?  137 ILE   A HG22 1 
ATOM   2912 H HG22 B ILE   A 1 137 ? 9.856  -13.055 -3.830  0.40 29.67 ?  137 ILE   A HG22 1 
ATOM   2913 H HG23 A ILE   A 1 137 ? 8.820  -12.257 -3.590  0.60 17.72 ?  137 ILE   A HG23 1 
ATOM   2914 H HG23 B ILE   A 1 137 ? 8.726  -12.385 -2.932  0.40 29.67 ?  137 ILE   A HG23 1 
ATOM   2915 H HD11 A ILE   A 1 137 ? 5.950  -10.043 -4.309  0.60 21.30 ?  137 ILE   A HD11 1 
ATOM   2916 H HD11 B ILE   A 1 137 ? 5.913  -10.204 -5.571  0.40 30.06 ?  137 ILE   A HD11 1 
ATOM   2917 H HD12 A ILE   A 1 137 ? 6.463  -8.960  -5.354  0.60 21.30 ?  137 ILE   A HD12 1 
ATOM   2918 H HD12 B ILE   A 1 137 ? 7.247  -10.151 -6.432  0.40 30.06 ?  137 ILE   A HD12 1 
ATOM   2919 H HD13 A ILE   A 1 137 ? 6.783  -10.492 -5.586  0.60 21.30 ?  137 ILE   A HD13 1 
ATOM   2920 H HD13 B ILE   A 1 137 ? 6.565  -11.549 -6.110  0.40 30.06 ?  137 ILE   A HD13 1 
ATOM   2921 N N    A HIS   A 1 138 ? 12.190 -10.790 -5.408  0.60 13.31 ?  138 HIS   A N    1 
ATOM   2922 N N    B HIS   A 1 138 ? 12.190 -10.702 -5.553  0.40 19.32 ?  138 HIS   A N    1 
ATOM   2923 C CA   A HIS   A 1 138 ? 13.363 -11.549 -5.823  0.60 13.98 ?  138 HIS   A CA   1 
ATOM   2924 C CA   B HIS   A 1 138 ? 13.387 -11.434 -5.949  0.40 17.13 ?  138 HIS   A CA   1 
ATOM   2925 C C    A HIS   A 1 138 ? 14.520 -11.359 -4.850  0.60 14.16 ?  138 HIS   A C    1 
ATOM   2926 C C    B HIS   A 1 138 ? 14.494 -11.333 -4.900  0.40 15.70 ?  138 HIS   A C    1 
ATOM   2927 O O    A HIS   A 1 138 ? 15.209 -12.325 -4.499  0.60 14.33 ?  138 HIS   A O    1 
ATOM   2928 O O    B HIS   A 1 138 ? 15.117 -12.340 -4.541  0.40 15.82 ?  138 HIS   A O    1 
ATOM   2929 C CB   A HIS   A 1 138 ? 13.768 -11.159 -7.243  0.60 15.19 ?  138 HIS   A CB   1 
ATOM   2930 C CB   B HIS   A 1 138 ? 13.837 -10.887 -7.302  0.40 16.90 ?  138 HIS   A CB   1 
ATOM   2931 C CG   A HIS   A 1 138 ? 15.040 -11.802 -7.696  0.60 16.22 ?  138 HIS   A CG   1 
ATOM   2932 C CG   B HIS   A 1 138 ? 15.122 -11.463 -7.796  0.40 16.91 ?  138 HIS   A CG   1 
ATOM   2933 N ND1  A HIS   A 1 138 ? 15.149 -13.158 -7.921  0.60 17.08 ?  138 HIS   A ND1  1 
ATOM   2934 N ND1  B HIS   A 1 138 ? 15.258 -12.787 -8.152  0.40 17.24 ?  138 HIS   A ND1  1 
ATOM   2935 C CD2  A HIS   A 1 138 ? 16.263 -11.279 -7.946  0.60 16.57 ?  138 HIS   A CD2  1 
ATOM   2936 C CD2  B HIS   A 1 138 ? 16.330 -10.891 -8.001  0.40 16.69 ?  138 HIS   A CD2  1 
ATOM   2937 C CE1  A HIS   A 1 138 ? 16.382 -13.441 -8.301  0.60 17.50 ?  138 HIS   A CE1  1 
ATOM   2938 C CE1  B HIS   A 1 138 ? 16.498 -13.006 -8.550  0.40 16.97 ?  138 HIS   A CE1  1 
ATOM   2939 N NE2  A HIS   A 1 138 ? 17.078 -12.319 -8.322  0.60 17.18 ?  138 HIS   A NE2  1 
ATOM   2940 N NE2  B HIS   A 1 138 ? 17.169 -11.871 -8.469  0.40 16.85 ?  138 HIS   A NE2  1 
ATOM   2941 H H    A HIS   A 1 138 ? 11.958 -10.164 -5.956  0.60 16.00 ?  138 HIS   A H    1 
ATOM   2942 H H    B HIS   A 1 138 ? 12.036 -10.008 -6.034  0.40 23.21 ?  138 HIS   A H    1 
ATOM   2943 H HA   A HIS   A 1 138 ? 13.137 -12.489 -5.834  0.60 16.80 ?  138 HIS   A HA   1 
ATOM   2944 H HA   B HIS   A 1 138 ? 13.165 -12.370 -6.060  0.40 20.58 ?  138 HIS   A HA   1 
ATOM   2945 H HB2  A HIS   A 1 138 ? 13.067 -11.430 -7.860  0.60 18.25 ?  138 HIS   A HB2  1 
ATOM   2946 H HB2  B HIS   A 1 138 ? 13.150 -11.086 -7.960  0.40 20.31 ?  138 HIS   A HB2  1 
ATOM   2947 H HB3  A HIS   A 1 138 ? 13.892 -10.199 -7.290  0.60 18.25 ?  138 HIS   A HB3  1 
ATOM   2948 H HB3  B HIS   A 1 138 ? 13.951 -9.927  -7.230  0.40 20.31 ?  138 HIS   A HB3  1 
ATOM   2949 H HD1  A HIS   A 1 138 ? 14.515 -13.732 -7.837  0.60 20.52 ?  138 HIS   A HD1  1 
ATOM   2950 H HD2  A HIS   A 1 138 ? 16.506 -10.385 -7.878  0.60 19.92 ?  138 HIS   A HD2  1 
ATOM   2951 H HD2  B HIS   A 1 138 ? 16.548 -10.000 -7.850  0.40 20.05 ?  138 HIS   A HD2  1 
ATOM   2952 H HE1  A HIS   A 1 138 ? 16.709 -14.287 -8.514  0.60 21.03 ?  138 HIS   A HE1  1 
ATOM   2953 H HE1  B HIS   A 1 138 ? 16.837 -13.821 -8.839  0.40 20.39 ?  138 HIS   A HE1  1 
ATOM   2954 H HE2  B HIS   A 1 138 ? 17.994 -11.765 -8.674  0.40 20.25 ?  138 HIS   A HE2  1 
ATOM   2955 N N    . SER   A 1 139 ? 14.755 -10.124 -4.398  1.00 14.32 ?  139 SER   A N    1 
ATOM   2956 C CA   . SER   A 1 139 ? 15.834 -9.920  -3.438  1.00 14.30 ?  139 SER   A CA   1 
ATOM   2957 C C    . SER   A 1 139 ? 15.629 -10.749 -2.177  1.00 14.00 ?  139 SER   A C    1 
ATOM   2958 O O    . SER   A 1 139 ? 16.585 -11.333 -1.651  1.00 13.94 ?  139 SER   A O    1 
ATOM   2959 C CB   . SER   A 1 139 ? 15.978 -8.440  -3.093  1.00 14.30 ?  139 SER   A CB   1 
ATOM   2960 O OG   . SER   A 1 139 ? 17.064 -8.257  -2.201  1.00 14.62 ?  139 SER   A OG   1 
ATOM   2961 H H    A SER   A 1 139 ? 14.321 -9.414  -4.619  0.60 17.21 ?  139 SER   A H    1 
ATOM   2962 H H    B SER   A 1 139 ? 14.321 -9.408  -4.597  0.40 17.21 ?  139 SER   A H    1 
ATOM   2963 H HA   . SER   A 1 139 ? 16.669 -10.203 -3.839  1.00 17.19 ?  139 SER   A HA   1 
ATOM   2964 H HB2  . SER   A 1 139 ? 16.154 -7.932  -3.900  1.00 17.19 ?  139 SER   A HB2  1 
ATOM   2965 H HB3  . SER   A 1 139 ? 15.158 -8.123  -2.674  1.00 17.19 ?  139 SER   A HB3  1 
ATOM   2966 H HG   . SER   A 1 139 ? 17.138 -7.436  -1.994  1.00 17.57 ?  139 SER   A HG   1 
ATOM   2967 N N    . LEU   A 1 140 ? 14.393 -10.816 -1.678  1.00 13.63 ?  140 LEU   A N    1 
ATOM   2968 C CA   . LEU   A 1 140 ? 14.125 -11.623 -0.490  1.00 13.62 ?  140 LEU   A CA   1 
ATOM   2969 C C    . LEU   A 1 140 ? 14.380 -13.102 -0.761  1.00 13.74 ?  140 LEU   A C    1 
ATOM   2970 O O    . LEU   A 1 140 ? 14.932 -13.814 0.088   1.00 14.31 ?  140 LEU   A O    1 
ATOM   2971 C CB   . LEU   A 1 140 ? 12.692 -11.392 -0.012  1.00 13.91 ?  140 LEU   A CB   1 
ATOM   2972 C CG   . LEU   A 1 140 ? 12.234 -12.227 1.190   1.00 14.11 ?  140 LEU   A CG   1 
ATOM   2973 C CD1  . LEU   A 1 140 ? 13.158 -12.067 2.388   1.00 14.61 ?  140 LEU   A CD1  1 
ATOM   2974 C CD2  . LEU   A 1 140 ? 10.793 -11.877 1.566   1.00 15.16 ?  140 LEU   A CD2  1 
ATOM   2975 H H    . LEU   A 1 140 ? 13.704 -10.414 -2.002  1.00 16.38 ?  140 LEU   A H    1 
ATOM   2976 H HA   . LEU   A 1 140 ? 14.723 -11.343 0.219   1.00 16.37 ?  140 LEU   A HA   1 
ATOM   2977 H HB2  . LEU   A 1 140 ? 12.599 -10.462 0.238   1.00 16.72 ?  140 LEU   A HB2  1 
ATOM   2978 H HB3  . LEU   A 1 140 ? 12.090 -11.594 -0.743  1.00 16.72 ?  140 LEU   A HB3  1 
ATOM   2979 H HG   . LEU   A 1 140 ? 12.237 -13.164 0.938   1.00 16.96 ?  140 LEU   A HG   1 
ATOM   2980 H HD11 . LEU   A 1 140 ? 12.786 -12.557 3.143   1.00 17.56 ?  140 LEU   A HD11 1 
ATOM   2981 H HD12 . LEU   A 1 140 ? 14.029 -12.440 2.162   1.00 17.56 ?  140 LEU   A HD12 1 
ATOM   2982 H HD13 . LEU   A 1 140 ? 13.242 -11.133 2.606   1.00 17.56 ?  140 LEU   A HD13 1 
ATOM   2983 H HD21 . LEU   A 1 140 ? 10.429 -12.587 2.120   1.00 18.22 ?  140 LEU   A HD21 1 
ATOM   2984 H HD22 . LEU   A 1 140 ? 10.792 -11.042 2.062   1.00 18.22 ?  140 LEU   A HD22 1 
ATOM   2985 H HD23 . LEU   A 1 140 ? 10.267 -11.784 0.760   1.00 18.22 ?  140 LEU   A HD23 1 
ATOM   2986 N N    . ARG   A 1 141 ? 13.992 -13.579 -1.944  1.00 14.30 ?  141 ARG   A N    1 
ATOM   2987 C CA   . ARG   A 1 141 ? 14.231 -14.974 -2.303  1.00 15.09 ?  141 ARG   A CA   1 
ATOM   2988 C C    . ARG   A 1 141 ? 15.727 -15.282 -2.331  1.00 14.66 ?  141 ARG   A C    1 
ATOM   2989 O O    . ARG   A 1 141 ? 16.180 -16.294 -1.782  1.00 14.75 ?  141 ARG   A O    1 
ATOM   2990 C CB   . ARG   A 1 141 ? 13.592 -15.245 -3.668  1.00 16.74 ?  141 ARG   A CB   1 
ATOM   2991 C CG   . ARG   A 1 141 ? 13.618 -16.684 -4.129  1.00 19.67 ?  141 ARG   A CG   1 
ATOM   2992 C CD   . ARG   A 1 141 ? 12.597 -17.486 -3.385  1.00 22.11 ?  141 ARG   A CD   1 
ATOM   2993 N NE   . ARG   A 1 141 ? 13.210 -18.275 -2.329  1.00 23.15 ?  141 ARG   A NE   1 
ATOM   2994 C CZ   . ARG   A 1 141 ? 12.528 -18.853 -1.348  1.00 23.91 ?  141 ARG   A CZ   1 
ATOM   2995 N NH1  . ARG   A 1 141 ? 11.234 -18.627 -1.177  1.00 23.63 ?  141 ARG   A NH1  1 
ATOM   2996 N NH2  . ARG   A 1 141 ? 13.161 -19.672 -0.511  1.00 24.96 ?  141 ARG   A NH2  1 
ATOM   2997 H H    . ARG   A 1 141 ? 13.595 -13.118 -2.551  1.00 17.19 ?  141 ARG   A H    1 
ATOM   2998 H HA   . ARG   A 1 141 ? 13.815 -15.553 -1.651  1.00 18.14 ?  141 ARG   A HA   1 
ATOM   2999 H HB2  . ARG   A 1 141 ? 12.664 -14.957 -3.638  1.00 20.12 ?  141 ARG   A HB2  1 
ATOM   3000 H HB3  . ARG   A 1 141 ? 14.063 -14.721 -4.336  1.00 20.12 ?  141 ARG   A HB3  1 
ATOM   3001 H HG2  . ARG   A 1 141 ? 13.409 -16.729 -5.078  1.00 23.63 ?  141 ARG   A HG2  1 
ATOM   3002 H HG3  . ARG   A 1 141 ? 14.492 -17.070 -3.960  1.00 23.63 ?  141 ARG   A HG3  1 
ATOM   3003 H HD2  . ARG   A 1 141 ? 11.952 -16.891 -2.967  1.00 26.56 ?  141 ARG   A HD2  1 
ATOM   3004 H HD3  . ARG   A 1 141 ? 12.137 -18.083 -4.003  1.00 26.56 ?  141 ARG   A HD3  1 
ATOM   3005 H HE   . ARG   A 1 141 ? 14.032 -18.503 -2.427  1.00 27.81 ?  141 ARG   A HE   1 
ATOM   3006 H HH11 . ARG   A 1 141 ? 10.807 -18.115 -1.720  1.00 28.39 ?  141 ARG   A HH11 1 
ATOM   3007 H HH12 . ARG   A 1 141 ? 10.811 -19.008 -0.530  1.00 28.39 ?  141 ARG   A HH12 1 
ATOM   3008 H HH21 . ARG   A 1 141 ? 14.000 -19.827 -0.613  1.00 29.98 ?  141 ARG   A HH21 1 
ATOM   3009 H HH22 . ARG   A 1 141 ? 12.733 -20.040 0.140   1.00 29.98 ?  141 ARG   A HH22 1 
ATOM   3010 N N    . VAL   A 1 142 ? 16.517 -14.414 -2.968  1.00 14.01 ?  142 VAL   A N    1 
ATOM   3011 C CA   . VAL   A 1 142 ? 17.962 -14.630 -3.001  1.00 13.94 ?  142 VAL   A CA   1 
ATOM   3012 C C    . VAL   A 1 142 ? 18.533 -14.606 -1.590  1.00 13.23 ?  142 VAL   A C    1 
ATOM   3013 O O    . VAL   A 1 142 ? 19.398 -15.419 -1.244  1.00 14.08 ?  142 VAL   A O    1 
ATOM   3014 C CB   . VAL   A 1 142 ? 18.662 -13.617 -3.927  1.00 14.42 ?  142 VAL   A CB   1 
ATOM   3015 C CG1  . VAL   A 1 142 ? 20.171 -13.840 -3.903  1.00 14.49 ?  142 VAL   A CG1  1 
ATOM   3016 C CG2  . VAL   A 1 142 ? 18.152 -13.751 -5.346  1.00 15.59 ?  142 VAL   A CG2  1 
ATOM   3017 H H    . VAL   A 1 142 ? 16.249 -13.700 -3.382  1.00 16.84 ?  142 VAL   A H    1 
ATOM   3018 H HA   . VAL   A 1 142 ? 18.130 -15.506 -3.370  1.00 16.76 ?  142 VAL   A HA   1 
ATOM   3019 H HB   . VAL   A 1 142 ? 18.489 -12.709 -3.624  1.00 17.33 ?  142 VAL   A HB   1 
ATOM   3020 H HG11 . VAL   A 1 142 ? 20.581 -13.351 -4.636  1.00 17.41 ?  142 VAL   A HG11 1 
ATOM   3021 H HG12 . VAL   A 1 142 ? 20.532 -13.522 -3.059  1.00 17.41 ?  142 VAL   A HG12 1 
ATOM   3022 H HG13 . VAL   A 1 142 ? 20.353 -14.789 -4.003  1.00 17.41 ?  142 VAL   A HG13 1 
ATOM   3023 H HG21 . VAL   A 1 142 ? 18.630 -13.126 -5.916  1.00 18.74 ?  142 VAL   A HG21 1 
ATOM   3024 H HG22 . VAL   A 1 142 ? 18.314 -14.660 -5.648  1.00 18.74 ?  142 VAL   A HG22 1 
ATOM   3025 H HG23 . VAL   A 1 142 ? 17.207 -13.558 -5.358  1.00 18.74 ?  142 VAL   A HG23 1 
ATOM   3026 N N    . CYS   A 1 143 ? 18.072 -13.667 -0.758  1.00 13.18 ?  143 CYS   A N    1 
ATOM   3027 C CA   . CYS   A 1 143 ? 18.528 -13.616 0.627   1.00 13.44 ?  143 CYS   A CA   1 
ATOM   3028 C C    . CYS   A 1 143 ? 18.304 -14.954 1.324   1.00 13.86 ?  143 CYS   A C    1 
ATOM   3029 O O    . CYS   A 1 143 ? 19.226 -15.537 1.903   1.00 14.04 ?  143 CYS   A O    1 
ATOM   3030 C CB   . CYS   A 1 143 ? 17.812 -12.490 1.368   1.00 13.97 ?  143 CYS   A CB   1 
ATOM   3031 S SG   . CYS   A 1 143 ? 18.302 -12.315 3.089   1.00 14.44 ?  143 CYS   A SG   1 
ATOM   3032 H H    . CYS   A 1 143 ? 17.505 -13.062 -0.970  1.00 15.84 ?  143 CYS   A H    1 
ATOM   3033 H HA   . CYS   A 1 143 ? 19.479 -13.435 0.641   1.00 16.16 ?  143 CYS   A HA   1 
ATOM   3034 H HB2  . CYS   A 1 143 ? 18.000 -11.652 0.916   1.00 16.80 ?  143 CYS   A HB2  1 
ATOM   3035 H HB3  . CYS   A 1 143 ? 16.860 -12.661 1.347   1.00 16.80 ?  143 CYS   A HB3  1 
ATOM   3036 H HG   . CYS   A 1 143 ? 17.718 -11.378 3.550   1.00 17.36 ?  143 CYS   A HG   1 
ATOM   3037 N N    . VAL   A 1 144 ? 17.074 -15.460 1.270   1.00 14.22 ?  144 VAL   A N    1 
ATOM   3038 C CA   . VAL   A 1 144 ? 16.738 -16.694 1.971   1.00 15.71 ?  144 VAL   A CA   1 
ATOM   3039 C C    . VAL   A 1 144 ? 17.558 -17.862 1.442   1.00 15.45 ?  144 VAL   A C    1 
ATOM   3040 O O    . VAL   A 1 144 ? 17.936 -18.769 2.200   1.00 16.16 ?  144 VAL   A O    1 
ATOM   3041 C CB   . VAL   A 1 144 ? 15.220 -16.940 1.862   1.00 18.24 ?  144 VAL   A CB   1 
ATOM   3042 C CG1  . VAL   A 1 144 ? 14.865 -18.377 2.190   1.00 20.40 ?  144 VAL   A CG1  1 
ATOM   3043 C CG2  . VAL   A 1 144 ? 14.471 -15.950 2.760   1.00 17.81 ?  144 VAL   A CG2  1 
ATOM   3044 H H    . VAL   A 1 144 ? 16.415 -15.106 0.835   1.00 17.09 ?  144 VAL   A H    1 
ATOM   3045 H HA   . VAL   A 1 144 ? 16.946 -16.588 2.905   1.00 18.88 ?  144 VAL   A HA   1 
ATOM   3046 H HB   . VAL   A 1 144 ? 14.938 -16.767 0.946   1.00 21.91 ?  144 VAL   A HB   1 
ATOM   3047 H HG11 . VAL   A 1 144 ? 13.915 -18.431 2.383   1.00 24.51 ?  144 VAL   A HG11 1 
ATOM   3048 H HG12 . VAL   A 1 144 ? 15.077 -18.939 1.428   1.00 24.51 ?  144 VAL   A HG12 1 
ATOM   3049 H HG13 . VAL   A 1 144 ? 15.375 -18.658 2.964   1.00 24.51 ?  144 VAL   A HG13 1 
ATOM   3050 H HG21 . VAL   A 1 144 ? 13.516 -16.114 2.692   1.00 21.40 ?  144 VAL   A HG21 1 
ATOM   3051 H HG22 . VAL   A 1 144 ? 14.760 -16.074 3.678   1.00 21.40 ?  144 VAL   A HG22 1 
ATOM   3052 H HG23 . VAL   A 1 144 ? 14.669 -15.043 2.473   1.00 21.40 ?  144 VAL   A HG23 1 
ATOM   3053 N N    . ASP   A 1 145 ? 17.815 -17.886 0.137   1.00 15.66 ?  145 ASP   A N    1 
ATOM   3054 C CA   . ASP   A 1 145 ? 18.531 -18.993 -0.490  1.00 16.41 ?  145 ASP   A CA   1 
ATOM   3055 C C    . ASP   A 1 145 ? 20.050 -18.849 -0.435  1.00 15.83 ?  145 ASP   A C    1 
ATOM   3056 O O    . ASP   A 1 145 ? 20.756 -19.741 -0.918  1.00 17.19 ?  145 ASP   A O    1 
ATOM   3057 C CB   . ASP   A 1 145 ? 18.095 -19.137 -1.950  1.00 18.18 ?  145 ASP   A CB   1 
ATOM   3058 C CG   . ASP   A 1 145 ? 16.647 -19.575 -2.085  1.00 20.29 ?  145 ASP   A CG   1 
ATOM   3059 O OD1  . ASP   A 1 145 ? 16.083 -20.123 -1.112  1.00 20.81 ?  145 ASP   A OD1  1 
ATOM   3060 O OD2  . ASP   A 1 145 ? 16.067 -19.370 -3.168  1.00 21.64 -1 145 ASP   A OD2  1 
ATOM   3061 H H    . ASP   A 1 145 ? 17.565 -17.277 -0.420  1.00 18.82 ?  145 ASP   A H    1 
ATOM   3062 H HA   . ASP   A 1 145 ? 18.292 -19.817 -0.033  1.00 19.73 ?  145 ASP   A HA   1 
ATOM   3063 H HB2  . ASP   A 1 145 ? 18.201 -18.285 -2.399  1.00 21.85 ?  145 ASP   A HB2  1 
ATOM   3064 H HB3  . ASP   A 1 145 ? 18.639 -19.813 -2.380  1.00 21.85 ?  145 ASP   A HB3  1 
ATOM   3065 N N    . THR   A 1 146 ? 20.572 -17.758 0.123   1.00 14.29 ?  146 THR   A N    1 
ATOM   3066 C CA   . THR   A 1 146 ? 22.013 -17.512 0.135   1.00 13.85 ?  146 THR   A CA   1 
ATOM   3067 C C    . THR   A 1 146 ? 22.568 -17.331 1.537   1.00 13.73 ?  146 THR   A C    1 
ATOM   3068 O O    . THR   A 1 146 ? 23.642 -17.867 1.851   1.00 14.76 ?  146 THR   A O    1 
ATOM   3069 C CB   . THR   A 1 146 ? 22.338 -16.260 -0.700  1.00 13.93 ?  146 THR   A CB   1 
ATOM   3070 O OG1  . THR   A 1 146 ? 21.823 -16.420 -2.021  1.00 14.24 ?  146 THR   A OG1  1 
ATOM   3071 C CG2  . THR   A 1 146 ? 23.843 -16.029 -0.786  1.00 14.20 ?  146 THR   A CG2  1 
ATOM   3072 H H    . THR   A 1 146 ? 20.112 -17.136 0.495   1.00 17.18 ?  146 THR   A H    1 
ATOM   3073 H HA   . THR   A 1 146 ? 22.471 -18.263 -0.267  1.00 16.64 ?  146 THR   A HA   1 
ATOM   3074 H HB   . THR   A 1 146 ? 21.940 -15.477 -0.289  1.00 16.74 ?  146 THR   A HB   1 
ATOM   3075 H HG1  . THR   A 1 146 ? 20.988 -16.501 -1.993  1.00 17.12 ?  146 THR   A HG1  1 
ATOM   3076 H HG21 . THR   A 1 146 ? 24.039 -15.363 -1.461  1.00 17.07 ?  146 THR   A HG21 1 
ATOM   3077 H HG22 . THR   A 1 146 ? 24.182 -15.720 0.069   1.00 17.07 ?  146 THR   A HG22 1 
ATOM   3078 H HG23 . THR   A 1 146 ? 24.290 -16.858 -1.022  1.00 17.07 ?  146 THR   A HG23 1 
ATOM   3079 N N    . VAL   A 1 147 ? 21.895 -16.542 2.366   1.00 13.64 ?  147 VAL   A N    1 
ATOM   3080 C CA   . VAL   A 1 147 ? 22.372 -16.245 3.708   1.00 13.86 ?  147 VAL   A CA   1 
ATOM   3081 C C    . VAL   A 1 147 ? 22.052 -17.416 4.623   1.00 14.24 ?  147 VAL   A C    1 
ATOM   3082 O O    . VAL   A 1 147 ? 20.909 -17.889 4.677   1.00 15.17 ?  147 VAL   A O    1 
ATOM   3083 C CB   . VAL   A 1 147 ? 21.744 -14.941 4.225   1.00 14.11 ?  147 VAL   A CB   1 
ATOM   3084 C CG1  . VAL   A 1 147 ? 22.263 -14.629 5.613   1.00 15.06 ?  147 VAL   A CG1  1 
ATOM   3085 C CG2  . VAL   A 1 147 ? 22.003 -13.790 3.259   1.00 14.46 ?  147 VAL   A CG2  1 
ATOM   3086 H H    . VAL   A 1 147 ? 21.145 -16.167 2.175   1.00 16.40 ?  147 VAL   A H    1 
ATOM   3087 H HA   . VAL   A 1 147 ? 23.334 -16.131 3.688   1.00 16.66 ?  147 VAL   A HA   1 
ATOM   3088 H HB   . VAL   A 1 147 ? 20.785 -15.066 4.292   1.00 16.97 ?  147 VAL   A HB   1 
ATOM   3089 H HG11 . VAL   A 1 147 ? 22.008 -13.728 5.848   1.00 18.10 ?  147 VAL   A HG11 1 
ATOM   3090 H HG12 . VAL   A 1 147 ? 21.864 -15.258 6.246   1.00 18.10 ?  147 VAL   A HG12 1 
ATOM   3091 H HG13 . VAL   A 1 147 ? 23.224 -14.723 5.620   1.00 18.10 ?  147 VAL   A HG13 1 
ATOM   3092 H HG21 . VAL   A 1 147 ? 21.668 -12.971 3.654   1.00 17.39 ?  147 VAL   A HG21 1 
ATOM   3093 H HG22 . VAL   A 1 147 ? 22.955 -13.721 3.103   1.00 17.39 ?  147 VAL   A HG22 1 
ATOM   3094 H HG23 . VAL   A 1 147 ? 21.540 -13.972 2.427   1.00 17.39 ?  147 VAL   A HG23 1 
ATOM   3095 N N    . ARG   A 1 148 ? 23.071 -17.890 5.338   1.00 14.43 ?  148 ARG   A N    1 
ATOM   3096 C CA   . ARG   A 1 148 ? 22.934 -18.966 6.306   1.00 14.63 ?  148 ARG   A CA   1 
ATOM   3097 C C    . ARG   A 1 148 ? 23.059 -18.494 7.743   1.00 15.07 ?  148 ARG   A C    1 
ATOM   3098 O O    . ARG   A 1 148 ? 22.645 -19.221 8.657   1.00 16.46 ?  148 ARG   A O    1 
ATOM   3099 C CB   . ARG   A 1 148 ? 23.970 -20.069 6.035   1.00 15.36 ?  148 ARG   A CB   1 
ATOM   3100 C CG   . ARG   A 1 148 ? 23.824 -20.708 4.662   1.00 16.44 ?  148 ARG   A CG   1 
ATOM   3101 C CD   . ARG   A 1 148 ? 24.909 -21.748 4.386   1.00 16.98 ?  148 ARG   A CD   1 
ATOM   3102 N NE   . ARG   A 1 148 ? 26.248 -21.170 4.408   1.00 17.13 ?  148 ARG   A NE   1 
ATOM   3103 C CZ   . ARG   A 1 148 ? 26.760 -20.435 3.430   1.00 16.40 ?  148 ARG   A CZ   1 
ATOM   3104 N NH1  . ARG   A 1 148 ? 26.085 -20.199 2.317   1.00 17.18 ?  148 ARG   A NH1  1 
ATOM   3105 N NH2  . ARG   A 1 148 ? 27.976 -19.906 3.579   1.00 16.95 ?  148 ARG   A NH2  1 
ATOM   3106 H H    . ARG   A 1 148 ? 23.876 -17.591 5.271   1.00 17.35 ?  148 ARG   A H    1 
ATOM   3107 H HA   . ARG   A 1 148 ? 22.058 -19.360 6.208   1.00 17.59 ?  148 ARG   A HA   1 
ATOM   3108 H HB2  . ARG   A 1 148 ? 24.860 -19.696 6.095   1.00 18.46 ?  148 ARG   A HB2  1 
ATOM   3109 H HB3  . ARG   A 1 148 ? 23.860 -20.774 6.696   1.00 18.46 ?  148 ARG   A HB3  1 
ATOM   3110 H HG2  . ARG   A 1 148 ? 22.960 -21.143 4.606   1.00 19.76 ?  148 ARG   A HG2  1 
ATOM   3111 H HG3  . ARG   A 1 148 ? 23.890 -20.011 3.987   1.00 19.76 ?  148 ARG   A HG3  1 
ATOM   3112 H HD2  . ARG   A 1 148 ? 24.867 -22.435 5.065   1.00 20.40 ?  148 ARG   A HD2  1 
ATOM   3113 H HD3  . ARG   A 1 148 ? 24.761 -22.132 3.508   1.00 20.40 ?  148 ARG   A HD3  1 
ATOM   3114 H HE   . ARG   A 1 148 ? 26.732 -21.302 5.104   1.00 20.58 ?  148 ARG   A HE   1 
ATOM   3115 H HH11 . ARG   A 1 148 ? 25.296 -20.521 2.212   1.00 20.64 ?  148 ARG   A HH11 1 
ATOM   3116 H HH12 . ARG   A 1 148 ? 26.433 -19.711 1.697   1.00 20.64 ?  148 ARG   A HH12 1 
ATOM   3117 H HH21 . ARG   A 1 148 ? 28.420 -20.044 4.303   1.00 20.37 ?  148 ARG   A HH21 1 
ATOM   3118 H HH22 . ARG   A 1 148 ? 28.319 -19.421 2.954   1.00 20.37 ?  148 ARG   A HH22 1 
ATOM   3119 N N    . THR   A 1 149 ? 23.619 -17.306 7.958   1.00 15.31 ?  149 THR   A N    1 
ATOM   3120 C CA   . THR   A 1 149 ? 23.699 -16.712 9.277   1.00 15.35 ?  149 THR   A CA   1 
ATOM   3121 C C    . THR   A 1 149 ? 22.383 -15.999 9.590   1.00 14.63 ?  149 THR   A C    1 
ATOM   3122 O O    . THR   A 1 149 ? 21.444 -15.983 8.783   1.00 15.11 ?  149 THR   A O    1 
ATOM   3123 C CB   . THR   A 1 149 ? 24.905 -15.781 9.335   1.00 15.50 ?  149 THR   A CB   1 
ATOM   3124 O OG1  . THR   A 1 149 ? 24.785 -14.836 8.268   1.00 15.70 ?  149 THR   A OG1  1 
ATOM   3125 C CG2  . THR   A 1 149 ? 26.206 -16.576 9.192   1.00 15.82 ?  149 THR   A CG2  1 
ATOM   3126 H H    . THR   A 1 149 ? 23.974 -16.815 7.339   1.00 18.40 ?  149 THR   A H    1 
ATOM   3127 H HA   . THR   A 1 149 ? 23.826 -17.418 9.931   1.00 18.45 ?  149 THR   A HA   1 
ATOM   3128 H HB   . THR   A 1 149 ? 24.908 -15.318 10.188  1.00 18.63 ?  149 THR   A HB   1 
ATOM   3129 H HG1  . THR   A 1 149 ? 25.437 -14.306 8.281   1.00 18.86 ?  149 THR   A HG1  1 
ATOM   3130 H HG21 . THR   A 1 149 ? 26.968 -15.980 9.257   1.00 19.01 ?  149 THR   A HG21 1 
ATOM   3131 H HG22 . THR   A 1 149 ? 26.271 -17.246 9.893   1.00 19.01 ?  149 THR   A HG22 1 
ATOM   3132 H HG23 . THR   A 1 149 ? 26.231 -17.025 8.330   1.00 19.01 ?  149 THR   A HG23 1 
ATOM   3133 N N    . ASN   A 1 150 ? 22.267 -15.470 10.800  1.00 14.81 ?  150 ASN   A N    1 
ATOM   3134 C CA   . ASN   A 1 150 ? 20.986 -14.951 11.287  1.00 15.37 ?  150 ASN   A CA   1 
ATOM   3135 C C    . ASN   A 1 150 ? 20.812 -13.509 10.832  1.00 14.72 ?  150 ASN   A C    1 
ATOM   3136 O O    . ASN   A 1 150 ? 21.559 -12.619 11.256  1.00 16.27 ?  150 ASN   A O    1 
ATOM   3137 C CB   . ASN   A 1 150 ? 20.926 -15.064 12.806  1.00 17.62 ?  150 ASN   A CB   1 
ATOM   3138 C CG   . ASN   A 1 150 ? 20.830 -16.497 13.269  1.00 21.67 ?  150 ASN   A CG   1 
ATOM   3139 O OD1  . ASN   A 1 150 ? 20.229 -17.331 12.595  1.00 23.19 ?  150 ASN   A OD1  1 
ATOM   3140 N ND2  . ASN   A 1 150 ? 21.435 -16.798 14.413  1.00 23.63 ?  150 ASN   A ND2  1 
ATOM   3141 H H    . ASN   A 1 150 ? 22.909 -15.407 11.366  1.00 17.80 ?  150 ASN   A H    1 
ATOM   3142 H HA   . ASN   A 1 150 ? 20.262 -15.485 10.916  1.00 18.47 ?  150 ASN   A HA   1 
ATOM   3143 H HB2  . ASN   A 1 150 ? 21.728 -14.680 13.188  1.00 21.17 ?  150 ASN   A HB2  1 
ATOM   3144 H HB3  . ASN   A 1 150 ? 20.141 -14.596 13.129  1.00 21.17 ?  150 ASN   A HB3  1 
ATOM   3145 H HD21 . ASN   A 1 150 ? 21.411 -17.605 14.722  1.00 28.38 ?  150 ASN   A HD21 1 
ATOM   3146 H HD22 . ASN   A 1 150 ? 21.847 -16.187 14.858  1.00 28.38 ?  150 ASN   A HD22 1 
ATOM   3147 N N    . VAL   A 1 151 ? 19.823 -13.272 9.977   1.00 13.98 ?  151 VAL   A N    1 
ATOM   3148 C CA   . VAL   A 1 151 ? 19.611 -11.961 9.380   1.00 13.91 ?  151 VAL   A CA   1 
ATOM   3149 C C    . VAL   A 1 151 ? 18.223 -11.445 9.740   1.00 13.92 ?  151 VAL   A C    1 
ATOM   3150 O O    . VAL   A 1 151 ? 17.215 -12.153 9.587   1.00 15.15 ?  151 VAL   A O    1 
ATOM   3151 C CB   . VAL   A 1 151 ? 19.895 -11.953 7.864   1.00 14.64 ?  151 VAL   A CB   1 
ATOM   3152 C CG1  . VAL   A 1 151 ? 19.073 -12.977 7.123   1.00 15.54 ?  151 VAL   A CG1  1 
ATOM   3153 C CG2  . VAL   A 1 151 ? 19.701 -10.544 7.285   1.00 15.24 ?  151 VAL   A CG2  1 
ATOM   3154 H H    . VAL   A 1 151 ? 19.249 -13.866 9.726   1.00 16.80 ?  151 VAL   A H    1 
ATOM   3155 H HA   . VAL   A 1 151 ? 20.251 -11.352 9.780   1.00 16.72 ?  151 VAL   A HA   1 
ATOM   3156 H HB   . VAL   A 1 151 ? 20.829 -12.182 7.729   1.00 17.60 ?  151 VAL   A HB   1 
ATOM   3157 H HG11 . VAL   A 1 151 ? 19.272 -12.922 6.174   1.00 18.67 ?  151 VAL   A HG11 1 
ATOM   3158 H HG12 . VAL   A 1 151 ? 19.308 -13.866 7.451   1.00 18.67 ?  151 VAL   A HG12 1 
ATOM   3159 H HG13 . VAL   A 1 151 ? 18.135 -12.810 7.277   1.00 18.67 ?  151 VAL   A HG13 1 
ATOM   3160 H HG21 . VAL   A 1 151 ? 20.016 -10.534 6.366   1.00 18.32 ?  151 VAL   A HG21 1 
ATOM   3161 H HG22 . VAL   A 1 151 ? 18.756 -10.320 7.308   1.00 18.32 ?  151 VAL   A HG22 1 
ATOM   3162 H HG23 . VAL   A 1 151 ? 20.205 -9.910  7.814   1.00 18.32 ?  151 VAL   A HG23 1 
ATOM   3163 N N    . TYR   A 1 152 ? 18.202 -10.202 10.232  1.00 13.86 ?  152 TYR   A N    1 
ATOM   3164 C CA   . TYR   A 1 152 ? 17.004 -9.472  10.616  1.00 13.59 ?  152 TYR   A CA   1 
ATOM   3165 C C    . TYR   A 1 152 ? 16.809 -8.367  9.589   1.00 12.94 ?  152 TYR   A C    1 
ATOM   3166 O O    . TYR   A 1 152 ? 17.582 -7.403  9.550   1.00 13.48 ?  152 TYR   A O    1 
ATOM   3167 C CB   . TYR   A 1 152 ? 17.173 -8.936  12.036  1.00 14.70 ?  152 TYR   A CB   1 
ATOM   3168 C CG   . TYR   A 1 152 ? 17.140 -10.067 13.026  1.00 14.99 ?  152 TYR   A CG   1 
ATOM   3169 C CD1  . TYR   A 1 152 ? 18.275 -10.822 13.299  1.00 16.57 ?  152 TYR   A CD1  1 
ATOM   3170 C CD2  . TYR   A 1 152 ? 15.953 -10.425 13.656  1.00 15.46 ?  152 TYR   A CD2  1 
ATOM   3171 C CE1  . TYR   A 1 152 ? 18.238 -11.886 14.182  1.00 17.85 ?  152 TYR   A CE1  1 
ATOM   3172 C CE2  . TYR   A 1 152 ? 15.905 -11.493 14.543  1.00 17.02 ?  152 TYR   A CE2  1 
ATOM   3173 C CZ   . TYR   A 1 152 ? 17.051 -12.218 14.805  1.00 17.94 ?  152 TYR   A CZ   1 
ATOM   3174 O OH   . TYR   A 1 152 ? 17.010 -13.286 15.685  1.00 20.16 ?  152 TYR   A OH   1 
ATOM   3175 H H    . TYR   A 1 152 ? 18.921 -9.733  10.342  1.00 16.67 ?  152 TYR   A H    1 
ATOM   3176 H HA   . TYR   A 1 152 ? 16.240 -10.067 10.589  1.00 16.33 ?  152 TYR   A HA   1 
ATOM   3177 H HB2  . TYR   A 1 152 ? 18.027 -8.492  12.114  1.00 17.66 ?  152 TYR   A HB2  1 
ATOM   3178 H HB3  . TYR   A 1 152 ? 16.448 -8.330  12.241  1.00 17.66 ?  152 TYR   A HB3  1 
ATOM   3179 H HD1  . TYR   A 1 152 ? 19.076 -10.609 12.878  1.00 19.91 ?  152 TYR   A HD1  1 
ATOM   3180 H HD2  . TYR   A 1 152 ? 15.175 -9.945  13.481  1.00 18.58 ?  152 TYR   A HD2  1 
ATOM   3181 H HE1  . TYR   A 1 152 ? 19.009 -12.376 14.359  1.00 21.45 ?  152 TYR   A HE1  1 
ATOM   3182 H HE2  . TYR   A 1 152 ? 15.105 -11.715 14.965  1.00 20.45 ?  152 TYR   A HE2  1 
ATOM   3183 H HH   . TYR   A 1 152 ? 16.232 -13.368 15.997  1.00 24.22 ?  152 TYR   A HH   1 
ATOM   3184 N N    A LEU   A 1 153 ? 15.823 -8.568  8.711   0.60 12.73 ?  153 LEU   A N    1 
ATOM   3185 N N    B LEU   A 1 153 ? 15.751 -8.470  8.797   0.40 12.63 ?  153 LEU   A N    1 
ATOM   3186 C CA   A LEU   A 1 153 ? 15.574 -7.702  7.561   0.60 12.63 ?  153 LEU   A CA   1 
ATOM   3187 C CA   B LEU   A 1 153 ? 15.488 -7.509  7.736   0.40 11.92 ?  153 LEU   A CA   1 
ATOM   3188 C C    A LEU   A 1 153 ? 14.564 -6.616  7.910   0.60 12.48 ?  153 LEU   A C    1 
ATOM   3189 C C    B LEU   A 1 153 ? 14.523 -6.432  8.214   0.40 12.28 ?  153 LEU   A C    1 
ATOM   3190 O O    A LEU   A 1 153 ? 13.427 -6.913  8.295   0.60 13.10 ?  153 LEU   A O    1 
ATOM   3191 O O    B LEU   A 1 153 ? 13.470 -6.738  8.788   0.40 11.88 ?  153 LEU   A O    1 
ATOM   3192 C CB   A LEU   A 1 153 ? 15.029 -8.519  6.389   0.60 12.84 ?  153 LEU   A CB   1 
ATOM   3193 C CB   B LEU   A 1 153 ? 14.914 -8.208  6.506   0.40 11.26 ?  153 LEU   A CB   1 
ATOM   3194 C CG   A LEU   A 1 153 ? 15.974 -9.539  5.758   0.60 13.08 ?  153 LEU   A CG   1 
ATOM   3195 C CG   B LEU   A 1 153 ? 15.831 -9.233  5.841   0.40 11.10 ?  153 LEU   A CG   1 
ATOM   3196 C CD1  A LEU   A 1 153 ? 15.210 -10.438 4.796   0.60 13.43 ?  153 LEU   A CD1  1 
ATOM   3197 C CD1  B LEU   A 1 153 ? 15.022 -10.112 4.907   0.40 11.51 ?  153 LEU   A CD1  1 
ATOM   3198 C CD2  A LEU   A 1 153 ? 17.112 -8.836  5.039   0.60 13.24 ?  153 LEU   A CD2  1 
ATOM   3199 C CD2  B LEU   A 1 153 ? 16.950 -8.540  5.085   0.40 11.77 ?  153 LEU   A CD2  1 
ATOM   3200 H H    A LEU   A 1 153 ? 15.268 -9.232  8.763   0.60 15.31 ?  153 LEU   A H    1 
ATOM   3201 H H    B LEU   A 1 153 ? 15.152 -9.089  8.861   0.40 15.18 ?  153 LEU   A H    1 
ATOM   3202 H HA   A LEU   A 1 153 ? 16.402 -7.291  7.290   0.60 15.18 ?  153 LEU   A HA   1 
ATOM   3203 H HA   B LEU   A 1 153 ? 16.317 -7.083  7.484   0.40 14.33 ?  153 LEU   A HA   1 
ATOM   3204 H HB2  A LEU   A 1 153 ? 14.245 -9.008  6.693   0.60 15.44 ?  153 LEU   A HB2  1 
ATOM   3205 H HB2  B LEU   A 1 153 ? 14.104 -8.669  6.768   0.40 13.54 ?  153 LEU   A HB2  1 
ATOM   3206 H HB3  A LEU   A 1 153 ? 14.767 -7.904  5.686   0.60 15.44 ?  153 LEU   A HB3  1 
ATOM   3207 H HB3  B LEU   A 1 153 ? 14.706 -7.533  5.843   0.40 13.54 ?  153 LEU   A HB3  1 
ATOM   3208 H HG   A LEU   A 1 153 ? 16.355 -10.099 6.457   0.60 15.72 ?  153 LEU   A HG   1 
ATOM   3209 H HG   B LEU   A 1 153 ? 16.231 -9.799  6.524   0.40 13.35 ?  153 LEU   A HG   1 
ATOM   3210 H HD11 A LEU   A 1 153 ? 15.764 -11.199 4.566   0.60 16.14 ?  153 LEU   A HD11 1 
ATOM   3211 H HD11 B LEU   A 1 153 ? 15.615 -10.751 4.482   0.40 13.84 ?  153 LEU   A HD11 1 
ATOM   3212 H HD12 A LEU   A 1 153 ? 14.396 -10.740 5.226   0.60 16.14 ?  153 LEU   A HD12 1 
ATOM   3213 H HD12 B LEU   A 1 153 ? 14.345 -10.579 5.420   0.40 13.84 ?  153 LEU   A HD12 1 
ATOM   3214 H HD13 A LEU   A 1 153 ? 14.994 -9.930  3.998   0.60 16.14 ?  153 LEU   A HD13 1 
ATOM   3215 H HD13 B LEU   A 1 153 ? 14.601 -9.553  4.235   0.40 13.84 ?  153 LEU   A HD13 1 
ATOM   3216 H HD21 A LEU   A 1 153 ? 17.720 -9.502  4.689   0.60 15.92 ?  153 LEU   A HD21 1 
ATOM   3217 H HD21 B LEU   A 1 153 ? 17.501 -9.212  4.655   0.40 14.16 ?  153 LEU   A HD21 1 
ATOM   3218 H HD22 A LEU   A 1 153 ? 16.741 -8.308  4.316   0.60 15.92 ?  153 LEU   A HD22 1 
ATOM   3219 H HD22 B LEU   A 1 153 ? 16.559 -7.954  4.419   0.40 14.16 ?  153 LEU   A HD22 1 
ATOM   3220 H HD23 A LEU   A 1 153 ? 17.573 -8.263  5.668   0.60 15.92 ?  153 LEU   A HD23 1 
ATOM   3221 H HD23 B LEU   A 1 153 ? 17.480 -8.024  5.711   0.40 14.16 ?  153 LEU   A HD23 1 
ATOM   3222 N N    A ALA   A 1 154 ? 14.963 -5.363  7.728   0.60 12.34 ?  154 ALA   A N    1 
ATOM   3223 N N    B ALA   A 1 154 ? 14.885 -5.172  7.962   0.40 12.42 ?  154 ALA   A N    1 
ATOM   3224 C CA   A ALA   A 1 154 ? 14.095 -4.214  7.951   0.60 12.73 ?  154 ALA   A CA   1 
ATOM   3225 C CA   B ALA   A 1 154 ? 14.039 -4.016  8.236   0.40 12.95 ?  154 ALA   A CA   1 
ATOM   3226 C C    A ALA   A 1 154 ? 13.591 -3.706  6.606   0.60 12.41 ?  154 ALA   A C    1 
ATOM   3227 C C    B ALA   A 1 154 ? 13.570 -3.465  6.895   0.40 13.23 ?  154 ALA   A C    1 
ATOM   3228 O O    A ALA   A 1 154 ? 14.386 -3.317  5.743   0.60 12.07 ?  154 ALA   A O    1 
ATOM   3229 O O    B ALA   A 1 154 ? 14.382 -2.981  6.100   0.40 13.11 ?  154 ALA   A O    1 
ATOM   3230 C CB   A ALA   A 1 154 ? 14.857 -3.108  8.678   0.60 13.68 ?  154 ALA   A CB   1 
ATOM   3231 C CB   B ALA   A 1 154 ? 14.814 -2.957  9.020   0.40 13.50 ?  154 ALA   A CB   1 
ATOM   3232 H H    A ALA   A 1 154 ? 15.757 -5.156  7.474   0.60 14.83 ?  154 ALA   A H    1 
ATOM   3233 H H    B ALA   A 1 154 ? 15.647 -4.952  7.616   0.40 14.94 ?  154 ALA   A H    1 
ATOM   3234 H HA   A ALA   A 1 154 ? 13.336 -4.485  8.496   0.60 15.31 ?  154 ALA   A HA   1 
ATOM   3235 H HA   B ALA   A 1 154 ? 13.264 -4.284  8.751   0.40 15.57 ?  154 ALA   A HA   1 
ATOM   3236 H HB1  A ALA   A 1 154 ? 14.257 -2.360  8.813   0.60 16.45 ?  154 ALA   A HB1  1 
ATOM   3237 H HB1  B ALA   A 1 154 ? 14.233 -2.199  9.192   0.40 16.23 ?  154 ALA   A HB1  1 
ATOM   3238 H HB2  A ALA   A 1 154 ? 15.165 -3.447  9.534   0.60 16.45 ?  154 ALA   A HB2  1 
ATOM   3239 H HB2  B ALA   A 1 154 ? 15.112 -3.343  9.859   0.40 16.23 ?  154 ALA   A HB2  1 
ATOM   3240 H HB3  A ALA   A 1 154 ? 15.611 -2.841  8.135   0.60 16.45 ?  154 ALA   A HB3  1 
ATOM   3241 H HB3  B ALA   A 1 154 ? 15.581 -2.673  8.496   0.40 16.23 ?  154 ALA   A HB3  1 
ATOM   3242 N N    A VAL   A 1 155 ? 12.271 -3.709  6.436   0.40 11.62 ?  155 VAL   A N    1 
ATOM   3243 N N    B VAL   A 1 155 ? 12.266 -3.545  6.641   0.40 13.31 ?  155 VAL   A N    1 
ATOM   3244 C CA   A VAL   A 1 155 ? 11.611 -3.226  5.229   0.40 13.02 ?  155 VAL   A CA   1 
ATOM   3245 C CA   B VAL   A 1 155 ? 11.662 -3.080  5.396   0.40 14.60 ?  155 VAL   A CA   1 
ATOM   3246 C CA   T VAL   A 1 155 ? 11.600 -3.256  5.285   0.20 14.02 ?  155 VAL   A CA   1 
ATOM   3247 C C    A VAL   A 1 155 ? 10.909 -1.922  5.585   0.40 14.23 ?  155 VAL   A C    1 
ATOM   3248 C C    B VAL   A 1 155 ? 10.913 -1.788  5.694   0.40 15.72 ?  155 VAL   A C    1 
ATOM   3249 C C    T VAL   A 1 155 ? 10.979 -1.891  5.593   0.20 13.92 ?  155 VAL   A C    1 
ATOM   3250 O O    A VAL   A 1 155 ? 9.963  -1.919  6.382   0.40 14.71 ?  155 VAL   A O    1 
ATOM   3251 O O    B VAL   A 1 155 ? 9.944  -1.790  6.464   0.40 16.28 ?  155 VAL   A O    1 
ATOM   3252 O O    T VAL   A 1 155 ? 10.132 -1.767  6.477   0.20 14.03 ?  155 VAL   A O    1 
ATOM   3253 C CB   A VAL   A 1 155 ? 10.622 -4.264  4.684   0.40 13.31 ?  155 VAL   A CB   1 
ATOM   3254 C CB   B VAL   A 1 155 ? 10.727 -4.141  4.794   0.40 14.91 ?  155 VAL   A CB   1 
ATOM   3255 C CB   T VAL   A 1 155 ? 10.577 -4.264  4.720   0.20 14.11 ?  155 VAL   A CB   1 
ATOM   3256 C CG1  A VAL   A 1 155 ? 9.942  -3.743  3.429   0.40 13.69 ?  155 VAL   A CG1  1 
ATOM   3257 C CG1  B VAL   A 1 155 ? 10.050 -3.602  3.542   0.40 15.14 ?  155 VAL   A CG1  1 
ATOM   3258 C CG1  T VAL   A 1 155 ? 9.893  -3.696  3.489   0.20 14.32 ?  155 VAL   A CG1  1 
ATOM   3259 C CG2  A VAL   A 1 155 ? 11.339 -5.584  4.412   0.40 14.12 ?  155 VAL   A CG2  1 
ATOM   3260 C CG2  B VAL   A 1 155 ? 11.508 -5.414  4.479   0.40 15.62 ?  155 VAL   A CG2  1 
ATOM   3261 C CG2  T VAL   A 1 155 ? 11.261 -5.590  4.391   0.20 14.40 ?  155 VAL   A CG2  1 
ATOM   3262 H H    A VAL   A 1 155 ? 11.722 -4.014  7.027   0.40 13.97 ?  155 VAL   A H    1 
ATOM   3263 H H    B VAL   A 1 155 ? 11.693 -3.872  7.192   0.40 16.00 ?  155 VAL   A H    1 
ATOM   3264 H HA   A VAL   A 1 155 ? 12.280 -3.044  4.552   0.40 15.65 ?  155 VAL   A HA   1 
ATOM   3265 H HA   B VAL   A 1 155 ? 12.360 -2.888  4.748   0.40 17.55 ?  155 VAL   A HA   1 
ATOM   3266 H HB   A VAL   A 1 155 ? 9.938  -4.428  5.355   0.40 16.00 ?  155 VAL   A HB   1 
ATOM   3267 H HB   B VAL   A 1 155 ? 10.039 -4.362  5.441   0.40 17.93 ?  155 VAL   A HB   1 
ATOM   3268 H HB   T VAL   A 1 155 ? 9.899  -4.438  5.391   0.20 16.97 ?  155 VAL   A HB   1 
ATOM   3269 H HG11 A VAL   A 1 155 ? 9.428  -4.461  3.031   0.40 16.45 ?  155 VAL   A HG11 1 
ATOM   3270 H HG11 B VAL   A 1 155 ? 9.636  -4.340  3.065   0.40 18.20 ?  155 VAL   A HG11 1 
ATOM   3271 H HG11 T VAL   A 1 155 ? 9.395  -4.403  3.050   0.20 17.21 ?  155 VAL   A HG11 1 
ATOM   3272 H HG12 A VAL   A 1 155 ? 9.352  -3.010  3.669   0.40 16.45 ?  155 VAL   A HG12 1 
ATOM   3273 H HG12 B VAL   A 1 155 ? 9.370  -2.957  3.799   0.40 18.20 ?  155 VAL   A HG12 1 
ATOM   3274 H HG12 T VAL   A 1 155 ? 9.291  -2.986  3.761   0.20 17.21 ?  155 VAL   A HG12 1 
ATOM   3275 H HG13 A VAL   A 1 155 ? 10.619 -3.434  2.809   0.40 16.45 ?  155 VAL   A HG13 1 
ATOM   3276 H HG13 B VAL   A 1 155 ? 10.715 -3.178  2.978   0.40 18.20 ?  155 VAL   A HG13 1 
ATOM   3277 H HG13 T VAL   A 1 155 ? 10.569 -3.347  2.887   0.20 17.21 ?  155 VAL   A HG13 1 
ATOM   3278 H HG21 A VAL   A 1 155 ? 10.721 -6.196  3.987   0.40 16.97 ?  155 VAL   A HG21 1 
ATOM   3279 H HG21 B VAL   A 1 155 ? 10.915 -6.048  4.045   0.40 18.77 ?  155 VAL   A HG21 1 
ATOM   3280 H HG21 T VAL   A 1 155 ? 10.601 -6.209  4.041   0.20 17.30 ?  155 VAL   A HG21 1 
ATOM   3281 H HG22 A VAL   A 1 155 ? 12.095 -5.415  3.825   0.40 16.97 ?  155 VAL   A HG22 1 
ATOM   3282 H HG22 B VAL   A 1 155 ? 12.245 -5.194  3.887   0.40 18.77 ?  155 VAL   A HG22 1 
ATOM   3283 H HG22 T VAL   A 1 155 ? 11.951 -5.433  3.725   0.20 17.30 ?  155 VAL   A HG22 1 
ATOM   3284 H HG23 A VAL   A 1 155 ? 11.652 -5.956  5.252   0.40 16.97 ?  155 VAL   A HG23 1 
ATOM   3285 H HG23 B VAL   A 1 155 ? 11.848 -5.791  5.305   0.40 18.77 ?  155 VAL   A HG23 1 
ATOM   3286 H HG23 T VAL   A 1 155 ? 11.659 -5.951  5.199   0.20 17.30 ?  155 VAL   A HG23 1 
ATOM   3287 N N    A PHE   A 1 156 ? 11.358 -0.813  4.986   0.40 15.39 ?  156 PHE   A N    1 
ATOM   3288 N N    B PHE   A 1 156 ? 11.358 -0.687  5.087   0.40 16.56 ?  156 PHE   A N    1 
ATOM   3289 N N    T PHE   A 1 156 ? 11.421 -0.869  4.855   0.20 13.90 ?  156 PHE   A N    1 
ATOM   3290 C CA   A PHE   A 1 156 ? 10.868 0.505   5.389   0.40 16.68 ?  156 PHE   A CA   1 
ATOM   3291 C CA   B PHE   A 1 156 ? 10.816 0.645   5.360   0.40 17.71 ?  156 PHE   A CA   1 
ATOM   3292 C CA   T PHE   A 1 156 ? 11.012 0.504   5.149   0.20 13.77 ?  156 PHE   A CA   1 
ATOM   3293 C C    A PHE   A 1 156 ? 9.409  0.706   5.002   0.40 16.68 ?  156 PHE   A C    1 
ATOM   3294 C C    B PHE   A 1 156 ? 9.799  1.091   4.319   0.40 18.42 ?  156 PHE   A C    1 
ATOM   3295 C C    T PHE   A 1 156 ? 9.562  0.756   4.760   0.20 14.46 ?  156 PHE   A C    1 
ATOM   3296 O O    A PHE   A 1 156 ? 8.626  1.270   5.777   0.40 17.08 ?  156 PHE   A O    1 
ATOM   3297 O O    B PHE   A 1 156 ? 9.773  2.259   3.921   0.40 19.11 ?  156 PHE   A O    1 
ATOM   3298 O O    T PHE   A 1 156 ? 8.828  1.440   5.485   0.20 14.74 ?  156 PHE   A O    1 
ATOM   3299 C CB   A PHE   A 1 156 ? 11.742 1.599   4.771   0.40 17.65 ?  156 PHE   A CB   1 
ATOM   3300 C CB   B PHE   A 1 156 ? 11.948 1.662   5.489   0.40 18.48 ?  156 PHE   A CB   1 
ATOM   3301 C CB   T PHE   A 1 156 ? 11.931 1.474   4.406   0.20 12.68 ?  156 PHE   A CB   1 
ATOM   3302 C CG   A PHE   A 1 156 ? 11.258 2.991   5.069   0.40 18.84 ?  156 PHE   A CG   1 
ATOM   3303 C CG   B PHE   A 1 156 ? 11.540 2.957   6.138   0.40 19.65 ?  156 PHE   A CG   1 
ATOM   3304 C CG   T PHE   A 1 156 ? 11.571 2.925   4.593   0.20 12.40 ?  156 PHE   A CG   1 
ATOM   3305 C CD1  A PHE   A 1 156 ? 11.233 3.455   6.373   0.40 19.29 ?  156 PHE   A CD1  1 
ATOM   3306 C CD1  B PHE   A 1 156 ? 10.671 2.971   7.217   0.40 20.26 ?  156 PHE   A CD1  1 
ATOM   3307 C CD1  T PHE   A 1 156 ? 11.917 3.592   5.758   0.20 12.42 ?  156 PHE   A CD1  1 
ATOM   3308 C CD2  A PHE   A 1 156 ? 10.821 3.829   4.054   0.40 19.53 ?  156 PHE   A CD2  1 
ATOM   3309 C CD2  B PHE   A 1 156 ? 12.053 4.159   5.685   0.40 19.83 ?  156 PHE   A CD2  1 
ATOM   3310 C CD2  T PHE   A 1 156 ? 10.899 3.623   3.601   0.20 12.86 ?  156 PHE   A CD2  1 
ATOM   3311 C CE1  A PHE   A 1 156 ? 10.786 4.725   6.662   0.40 19.80 ?  156 PHE   A CE1  1 
ATOM   3312 C CE1  B PHE   A 1 156 ? 10.304 4.161   7.816   0.40 20.64 ?  156 PHE   A CE1  1 
ATOM   3313 C CE1  T PHE   A 1 156 ? 11.593 4.924   5.934   0.20 13.08 ?  156 PHE   A CE1  1 
ATOM   3314 C CE2  A PHE   A 1 156 ? 10.370 5.106   4.336   0.40 20.01 ?  156 PHE   A CE2  1 
ATOM   3315 C CE2  B PHE   A 1 156 ? 11.694 5.352   6.279   0.40 20.20 ?  156 PHE   A CE2  1 
ATOM   3316 C CE2  T PHE   A 1 156 ? 10.573 4.955   3.771   0.20 13.25 ?  156 PHE   A CE2  1 
ATOM   3317 C CZ   A PHE   A 1 156 ? 10.357 5.556   5.643   0.40 20.01 ?  156 PHE   A CZ   1 
ATOM   3318 C CZ   B PHE   A 1 156 ? 10.820 5.354   7.349   0.40 20.47 ?  156 PHE   A CZ   1 
ATOM   3319 C CZ   T PHE   A 1 156 ? 10.922 5.607   4.940   0.20 13.40 ?  156 PHE   A CZ   1 
ATOM   3320 H H    A PHE   A 1 156 ? 11.944 -0.806  4.353   0.40 18.49 ?  156 PHE   A H    1 
ATOM   3321 H H    B PHE   A 1 156 ? 11.998 -0.686  4.510   0.40 19.90 ?  156 PHE   A H    1 
ATOM   3322 H H    T PHE   A 1 156 ? 11.965 -0.949  4.194   0.20 16.70 ?  156 PHE   A H    1 
ATOM   3323 H HA   A PHE   A 1 156 ? 10.939 0.583   6.353   0.40 20.04 ?  156 PHE   A HA   1 
ATOM   3324 H HA   B PHE   A 1 156 ? 10.361 0.600   6.207   0.40 21.28 ?  156 PHE   A HA   1 
ATOM   3325 H HA   T PHE   A 1 156 ? 11.107 0.659   6.102   0.20 16.55 ?  156 PHE   A HA   1 
ATOM   3326 H HB2  A PHE   A 1 156 ? 12.648 1.518   5.119   0.40 21.21 ?  156 PHE   A HB2  1 
ATOM   3327 H HB2  B PHE   A 1 156 ? 12.651 1.279   6.032   0.40 22.20 ?  156 PHE   A HB2  1 
ATOM   3328 H HB2  T PHE   A 1 156 ? 12.838 1.347   4.726   0.20 15.24 ?  156 PHE   A HB2  1 
ATOM   3329 H HB3  A PHE   A 1 156 ? 11.753 1.487   3.807   0.40 21.21 ?  156 PHE   A HB3  1 
ATOM   3330 H HB3  B PHE   A 1 156 ? 12.294 1.872   4.603   0.40 22.20 ?  156 PHE   A HB3  1 
ATOM   3331 H HB3  T PHE   A 1 156 ? 11.887 1.275   3.459   0.20 15.24 ?  156 PHE   A HB3  1 
ATOM   3332 H HD1  A PHE   A 1 156 ? 11.524 2.901   7.063   0.40 23.18 ?  156 PHE   A HD1  1 
ATOM   3333 H HD1  B PHE   A 1 156 ? 10.321 2.167   7.534   0.40 24.34 ?  156 PHE   A HD1  1 
ATOM   3334 H HD1  T PHE   A 1 156 ? 12.366 3.132   6.434   0.20 14.94 ?  156 PHE   A HD1  1 
ATOM   3335 H HD2  A PHE   A 1 156 ? 10.833 3.527   3.174   0.40 23.47 ?  156 PHE   A HD2  1 
ATOM   3336 H HD2  B PHE   A 1 156 ? 12.643 4.163   4.966   0.40 23.82 ?  156 PHE   A HD2  1 
ATOM   3337 H HD2  T PHE   A 1 156 ? 10.662 3.184   2.816   0.20 15.46 ?  156 PHE   A HD2  1 
ATOM   3338 H HE1  A PHE   A 1 156 ? 10.777 5.026   7.543   0.40 23.79 ?  156 PHE   A HE1  1 
ATOM   3339 H HE1  B PHE   A 1 156 ? 9.715  4.155   8.536   0.40 24.79 ?  156 PHE   A HE1  1 
ATOM   3340 H HE1  T PHE   A 1 156 ? 11.826 5.356   6.724   0.20 15.72 ?  156 PHE   A HE1  1 
ATOM   3341 H HE2  A PHE   A 1 156 ? 10.083 5.660   3.648   0.40 24.04 ?  156 PHE   A HE2  1 
ATOM   3342 H HE2  B PHE   A 1 156 ? 12.043 6.152   5.961   0.40 24.27 ?  156 PHE   A HE2  1 
ATOM   3343 H HE2  T PHE   A 1 156 ? 10.120 5.410   3.103   0.20 15.93 ?  156 PHE   A HE2  1 
ATOM   3344 H HZ   A PHE   A 1 156 ? 10.055 6.413   5.838   0.40 24.04 ?  156 PHE   A HZ   1 
ATOM   3345 H HZ   B PHE   A 1 156 ? 10.575 6.155   7.750   0.40 24.59 ?  156 PHE   A HZ   1 
ATOM   3346 H HZ   T PHE   A 1 156 ? 10.701 6.500   5.060   0.20 16.11 ?  156 PHE   A HZ   1 
ATOM   3347 N N    A ASP   A 1 157 ? 9.034  0.269   3.806   0.40 17.32 ?  157 ASP   A N    1 
ATOM   3348 N N    B ASP   A 1 157 ? 8.953  0.177   3.854   0.40 18.00 ?  157 ASP   A N    1 
ATOM   3349 N N    T ASP   A 1 157 ? 9.140  0.236   3.614   0.20 14.99 ?  157 ASP   A N    1 
ATOM   3350 C CA   A ASP   A 1 157 ? 7.708  0.538   3.269   0.40 18.52 ?  157 ASP   A CA   1 
ATOM   3351 C CA   B ASP   A 1 157 ? 7.813  0.533   3.016   0.40 17.81 ?  157 ASP   A CA   1 
ATOM   3352 C CA   T ASP   A 1 157 ? 7.820  0.510   3.067   0.20 15.76 ?  157 ASP   A CA   1 
ATOM   3353 C C    A ASP   A 1 157 ? 6.723  -0.489  3.818   0.40 18.50 ?  157 ASP   A C    1 
ATOM   3354 C C    B ASP   A 1 157 ? 6.682  -0.414  3.382   0.40 17.75 ?  157 ASP   A C    1 
ATOM   3355 C C    T ASP   A 1 157 ? 6.816  -0.473  3.659   0.20 16.65 ?  157 ASP   A C    1 
ATOM   3356 O O    A ASP   A 1 157 ? 6.892  -1.694  3.597   0.40 17.89 ?  157 ASP   A O    1 
ATOM   3357 O O    B ASP   A 1 157 ? 6.783  -1.624  3.152   0.40 17.47 ?  157 ASP   A O    1 
ATOM   3358 O O    T ASP   A 1 157 ? 6.980  -1.691  3.521   0.20 16.30 ?  157 ASP   A O    1 
ATOM   3359 C CB   A ASP   A 1 157 ? 7.776  0.460   1.747   0.40 19.80 ?  157 ASP   A CB   1 
ATOM   3360 C CB   B ASP   A 1 157 ? 8.159  0.445   1.530   0.40 17.72 ?  157 ASP   A CB   1 
ATOM   3361 C CB   T ASP   A 1 157 ? 7.873  0.366   1.549   0.20 15.56 ?  157 ASP   A CB   1 
ATOM   3362 C CG   A ASP   A 1 157 ? 6.503  0.926   1.084   0.40 21.23 ?  157 ASP   A CG   1 
ATOM   3363 C CG   B ASP   A 1 157 ? 7.018  0.883   0.639   0.40 17.65 ?  157 ASP   A CG   1 
ATOM   3364 C CG   T ASP   A 1 157 ? 6.695  1.020   0.865   0.20 15.24 ?  157 ASP   A CG   1 
ATOM   3365 O OD1  A ASP   A 1 157 ? 6.176  2.125   1.192   0.40 22.10 ?  157 ASP   A OD1  1 
ATOM   3366 O OD1  B ASP   A 1 157 ? 5.934  0.270   0.733   0.40 18.16 ?  157 ASP   A OD1  1 
ATOM   3367 O OD1  T ASP   A 1 157 ? 5.586  0.448   0.931   0.20 15.77 ?  157 ASP   A OD1  1 
ATOM   3368 O OD2  A ASP   A 1 157 ? 5.820  0.087   0.457   0.40 21.57 -1 157 ASP   A OD2  1 
ATOM   3369 O OD2  B ASP   A 1 157 ? 7.196  1.838   -0.149  0.40 17.82 -1 157 ASP   A OD2  1 
ATOM   3370 O OD2  T ASP   A 1 157 ? 6.869  2.114   0.285   0.20 14.65 -1 157 ASP   A OD2  1 
ATOM   3371 H H    A ASP   A 1 157 ? 9.541  -0.196  3.281   0.40 20.81 ?  157 ASP   A H    1 
ATOM   3372 H H    B ASP   A 1 157 ? 9.025  -0.674  4.004   0.40 21.63 ?  157 ASP   A H    1 
ATOM   3373 H H    T ASP   A 1 157 ? 9.614  -0.286  3.122   0.20 18.02 ?  157 ASP   A H    1 
ATOM   3374 H HA   A ASP   A 1 157 ? 7.425  1.428   3.530   0.40 22.25 ?  157 ASP   A HA   1 
ATOM   3375 H HA   B ASP   A 1 157 ? 7.533  1.438   3.217   0.40 21.41 ?  157 ASP   A HA   1 
ATOM   3376 H HA   T ASP   A 1 157 ? 7.549  1.416   3.288   0.20 18.94 ?  157 ASP   A HA   1 
ATOM   3377 H HB2  A ASP   A 1 157 ? 8.537  0.986   1.439   0.40 23.79 ?  157 ASP   A HB2  1 
ATOM   3378 H HB2  B ASP   A 1 157 ? 8.924  1.009   1.351   0.40 21.29 ?  157 ASP   A HB2  1 
ATOM   3379 H HB2  T ASP   A 1 157 ? 8.696  0.764   1.223   0.20 18.70 ?  157 ASP   A HB2  1 
ATOM   3380 H HB3  A ASP   A 1 157 ? 7.889  -0.461  1.482   0.40 23.79 ?  157 ASP   A HB3  1 
ATOM   3381 H HB3  B ASP   A 1 157 ? 8.362  -0.473  1.302   0.40 21.29 ?  157 ASP   A HB3  1 
ATOM   3382 H HB3  T ASP   A 1 157 ? 7.861  -0.579  1.324   0.20 18.70 ?  157 ASP   A HB3  1 
ATOM   3383 N N    A LYS   A 1 158 ? 5.696  -0.019  4.535   0.40 19.17 ?  158 LYS   A N    1 
ATOM   3384 N N    B LYS   A 1 158 ? 5.611  0.139   3.958   0.40 18.35 ?  158 LYS   A N    1 
ATOM   3385 N N    T LYS   A 1 158 ? 5.777  0.052   4.314   0.20 17.83 ?  158 LYS   A N    1 
ATOM   3386 C CA   A LYS   A 1 158 ? 4.725  -0.949  5.106   0.40 19.83 ?  158 LYS   A CA   1 
ATOM   3387 C CA   B LYS   A 1 158 ? 4.560  -0.691  4.535   0.40 18.95 ?  158 LYS   A CA   1 
ATOM   3388 C CA   T LYS   A 1 158 ? 4.790  -0.825  4.938   0.20 18.84 ?  158 LYS   A CA   1 
ATOM   3389 C C    A LYS   A 1 158 ? 3.975  -1.697  4.016   0.40 19.22 ?  158 LYS   A C    1 
ATOM   3390 C C    B LYS   A 1 158 ? 3.895  -1.553  3.470   0.40 18.90 ?  158 LYS   A C    1 
ATOM   3391 C C    T LYS   A 1 158 ? 4.029  -1.633  3.895   0.20 18.86 ?  158 LYS   A C    1 
ATOM   3392 O O    A LYS   A 1 158 ? 3.760  -2.910  4.124   0.40 19.02 ?  158 LYS   A O    1 
ATOM   3393 O O    B LYS   A 1 158 ? 3.725  -2.764  3.651   0.40 18.59 ?  158 LYS   A O    1 
ATOM   3394 O O    T LYS   A 1 158 ? 3.805  -2.835  4.079   0.20 18.76 ?  158 LYS   A O    1 
ATOM   3395 C CB   A LYS   A 1 158 ? 3.749  -0.219  6.031   0.40 20.84 ?  158 LYS   A CB   1 
ATOM   3396 C CB   B LYS   A 1 158 ? 3.529  0.187   5.247   0.40 19.73 ?  158 LYS   A CB   1 
ATOM   3397 C CB   T LYS   A 1 158 ? 3.823  -0.019  5.807   0.20 19.83 ?  158 LYS   A CB   1 
ATOM   3398 C CG   A LYS   A 1 158 ? 2.507  -1.036  6.419   0.40 22.14 ?  158 LYS   A CG   1 
ATOM   3399 C CG   B LYS   A 1 158 ? 2.380  -0.599  5.858   0.40 20.67 ?  158 LYS   A CG   1 
ATOM   3400 C CG   T LYS   A 1 158 ? 2.597  -0.805  6.278   0.20 20.90 ?  158 LYS   A CG   1 
ATOM   3401 C CD   A LYS   A 1 158 ? 2.846  -2.317  7.190   0.40 23.04 ?  158 LYS   A CD   1 
ATOM   3402 C CD   B LYS   A 1 158 ? 1.407  0.303   6.593   0.40 21.67 ?  158 LYS   A CD   1 
ATOM   3403 C CD   T LYS   A 1 158 ? 2.978  -2.024  7.114   0.20 21.84 ?  158 LYS   A CD   1 
ATOM   3404 C CE   A LYS   A 1 158 ? 1.575  -3.002  7.697   0.40 23.41 ?  158 LYS   A CE   1 
ATOM   3405 C CE   B LYS   A 1 158 ? 0.233  -0.489  7.147   0.40 22.27 ?  158 LYS   A CE   1 
ATOM   3406 C CE   T LYS   A 1 158 ? 1.743  -2.825  7.517   0.20 22.48 ?  158 LYS   A CE   1 
ATOM   3407 N NZ   A LYS   A 1 158 ? 1.823  -4.352  8.287   0.40 23.58 ?  158 LYS   A NZ   1 
ATOM   3408 N NZ   B LYS   A 1 158 ? -0.494 -1.240  6.086   0.40 22.49 ?  158 LYS   A NZ   1 
ATOM   3409 N NZ   T LYS   A 1 158 ? 2.081  -4.039  8.315   0.20 22.85 ?  158 LYS   A NZ   1 
ATOM   3410 H H    A LYS   A 1 158 ? 5.548  0.812   4.697   0.40 23.03 ?  158 LYS   A H    1 
ATOM   3411 H H    B LYS   A 1 158 ? 5.472  0.985   4.019   0.40 22.05 ?  158 LYS   A H    1 
ATOM   3412 H H    T LYS   A 1 158 ? 5.624  0.893   4.407   0.20 21.43 ?  158 LYS   A H    1 
ATOM   3413 H HA   A LYS   A 1 158 ? 5.201  -1.603  5.635   0.40 23.82 ?  158 LYS   A HA   1 
ATOM   3414 H HA   B LYS   A 1 158 ? 4.948  -1.281  5.198   0.40 22.77 ?  158 LYS   A HA   1 
ATOM   3415 H HA   T LYS   A 1 158 ? 5.251  -1.450  5.515   0.20 22.64 ?  158 LYS   A HA   1 
ATOM   3416 H HB2  A LYS   A 1 158 ? 4.215  0.011   6.850   0.40 25.04 ?  158 LYS   A HB2  1 
ATOM   3417 H HB2  B LYS   A 1 158 ? 3.970  0.674   5.964   0.40 23.71 ?  158 LYS   A HB2  1 
ATOM   3418 H HB2  T LYS   A 1 158 ? 4.296  0.287   6.598   0.20 23.83 ?  158 LYS   A HB2  1 
ATOM   3419 H HB3  A LYS   A 1 158 ? 3.445  0.588   5.589   0.40 25.04 ?  158 LYS   A HB3  1 
ATOM   3420 H HB3  B LYS   A 1 158 ? 3.153  0.815   4.609   0.40 23.71 ?  158 LYS   A HB3  1 
ATOM   3421 H HB3  T LYS   A 1 158 ? 3.506  0.744   5.300   0.20 23.83 ?  158 LYS   A HB3  1 
ATOM   3422 H HG2  A LYS   A 1 158 ? 1.946  -0.492  6.989   0.40 26.59 ?  158 LYS   A HG2  1 
ATOM   3423 H HG2  B LYS   A 1 158 ? 1.894  -1.054  5.154   0.40 24.84 ?  158 LYS   A HG2  1 
ATOM   3424 H HG2  T LYS   A 1 158 ? 2.049  -0.229  6.830   0.20 25.11 ?  158 LYS   A HG2  1 
ATOM   3425 H HG3  A LYS   A 1 158 ? 2.013  -1.285  5.620   0.40 26.59 ?  158 LYS   A HG3  1 
ATOM   3426 H HG3  B LYS   A 1 158 ? 2.736  -1.243  6.491   0.40 24.84 ?  158 LYS   A HG3  1 
ATOM   3427 H HG3  T LYS   A 1 158 ? 2.084  -1.109  5.512   0.20 25.11 ?  158 LYS   A HG3  1 
ATOM   3428 H HD2  A LYS   A 1 158 ? 3.314  -2.934  6.605   0.40 27.67 ?  158 LYS   A HD2  1 
ATOM   3429 H HD2  B LYS   A 1 158 ? 1.865  0.731   7.335   0.40 26.04 ?  158 LYS   A HD2  1 
ATOM   3430 H HD2  T LYS   A 1 158 ? 3.559  -2.605  6.598   0.20 26.23 ?  158 LYS   A HD2  1 
ATOM   3431 H HD3  A LYS   A 1 158 ? 3.400  -2.093  7.955   0.40 27.67 ?  158 LYS   A HD3  1 
ATOM   3432 H HD3  B LYS   A 1 158 ? 1.065  0.972   5.980   0.40 26.04 ?  158 LYS   A HD3  1 
ATOM   3433 H HD3  T LYS   A 1 158 ? 3.428  -1.731  7.923   0.20 26.23 ?  158 LYS   A HD3  1 
ATOM   3434 H HE2  A LYS   A 1 158 ? 1.172  -2.447  8.382   0.40 28.12 ?  158 LYS   A HE2  1 
ATOM   3435 H HE2  B LYS   A 1 158 ? 0.562  -1.130  7.794   0.40 26.75 ?  158 LYS   A HE2  1 
ATOM   3436 H HE2  T LYS   A 1 158 ? 1.162  -2.265  8.056   0.20 27.01 ?  158 LYS   A HE2  1 
ATOM   3437 H HE3  A LYS   A 1 158 ? 0.961  -3.110  6.955   0.40 28.12 ?  158 LYS   A HE3  1 
ATOM   3438 H HE3  B LYS   A 1 158 ? -0.392 0.122   7.568   0.40 26.75 ?  158 LYS   A HE3  1 
ATOM   3439 H HE3  T LYS   A 1 158 ? 1.276  -3.113  6.717   0.20 27.01 ?  158 LYS   A HE3  1 
ATOM   3440 H HZ1  A LYS   A 1 158 ? 1.056  -4.707  8.566   0.40 28.33 ?  158 LYS   A HZ1  1 
ATOM   3441 H HZ1  B LYS   A 1 158 ? -1.219 -1.625  6.430   0.40 27.01 ?  158 LYS   A HZ1  1 
ATOM   3442 H HZ1  T LYS   A 1 158 ? 1.338  -4.479  8.531   0.20 27.45 ?  158 LYS   A HZ1  1 
ATOM   3443 H HZ2  A LYS   A 1 158 ? 2.185  -4.889  7.676   0.40 28.33 ?  158 LYS   A HZ2  1 
ATOM   3444 H HZ2  B LYS   A 1 158 ? -0.743 -0.684  5.437   0.40 27.01 ?  158 LYS   A HZ2  1 
ATOM   3445 H HZ2  T LYS   A 1 158 ? 2.608  -4.578  7.840   0.20 27.45 ?  158 LYS   A HZ2  1 
ATOM   3446 H HZ3  A LYS   A 1 158 ? 2.379  -4.284  8.979   0.40 28.33 ?  158 LYS   A HZ3  1 
ATOM   3447 H HZ3  B LYS   A 1 158 ? 0.033  -1.868  5.742   0.40 27.01 ?  158 LYS   A HZ3  1 
ATOM   3448 H HZ3  T LYS   A 1 158 ? 2.505  -3.805  9.061   0.20 27.45 ?  158 LYS   A HZ3  1 
ATOM   3449 N N    A ASN   A 1 159 ? 3.558  -0.995  2.961   0.40 18.91 ?  159 ASN   A N    1 
ATOM   3450 N N    B ASN   A 1 159 ? 3.499  -0.943  2.350   0.40 19.71 ?  159 ASN   A N    1 
ATOM   3451 N N    T ASN   A 1 159 ? 3.613  -0.997  2.806   0.20 19.07 ?  159 ASN   A N    1 
ATOM   3452 C CA   A ASN   A 1 159 ? 2.870  -1.678  1.872   0.40 18.43 ?  159 ASN   A CA   1 
ATOM   3453 C CA   B ASN   A 1 159 ? 2.855  -1.715  1.293   0.40 20.98 ?  159 ASN   A CA   1 
ATOM   3454 C CA   T ASN   A 1 159 ? 2.869  -1.697  1.765   0.20 19.12 ?  159 ASN   A CA   1 
ATOM   3455 C C    A ASN   A 1 159 ? 3.758  -2.755  1.257   0.40 17.48 ?  159 ASN   A C    1 
ATOM   3456 C C    B ASN   A 1 159 ? 3.770  -2.827  0.802   0.40 20.02 ?  159 ASN   A C    1 
ATOM   3457 C C    T ASN   A 1 159 ? 3.707  -2.799  1.126   0.20 18.93 ?  159 ASN   A C    1 
ATOM   3458 O O    A ASN   A 1 159 ? 3.296  -3.870  0.984   0.40 16.93 ?  159 ASN   A O    1 
ATOM   3459 O O    B ASN   A 1 159 ? 3.316  -3.944  0.527   0.40 19.89 ?  159 ASN   A O    1 
ATOM   3460 O O    T ASN   A 1 159 ? 3.183  -3.852  0.769   0.20 18.90 ?  159 ASN   A O    1 
ATOM   3461 C CB   A ASN   A 1 159 ? 2.371  -0.666  0.834   0.40 19.29 ?  159 ASN   A CB   1 
ATOM   3462 C CB   B ASN   A 1 159 ? 2.450  -0.795  0.140   0.40 23.05 ?  159 ASN   A CB   1 
ATOM   3463 C CB   T ASN   A 1 159 ? 2.360  -0.717  0.703   0.20 19.50 ?  159 ASN   A CB   1 
ATOM   3464 C CG   A ASN   A 1 159 ? 1.102  0.053   1.282   0.40 20.59 ?  159 ASN   A CG   1 
ATOM   3465 C CG   B ASN   A 1 159 ? 1.445  0.265   0.560   0.40 24.85 ?  159 ASN   A CG   1 
ATOM   3466 C CG   T ASN   A 1 159 ? 1.141  0.062   1.168   0.20 20.05 ?  159 ASN   A CG   1 
ATOM   3467 O OD1  A ASN   A 1 159 ? 0.285  -0.511  2.010   0.40 21.63 ?  159 ASN   A OD1  1 
ATOM   3468 O OD1  B ASN   A 1 159 ? 1.571  1.438   0.199   0.40 25.75 ?  159 ASN   A OD1  1 
ATOM   3469 O OD1  T ASN   A 1 159 ? 0.340  -0.434  1.960   0.20 20.54 ?  159 ASN   A OD1  1 
ATOM   3470 N ND2  A ASN   A 1 159 ? 0.933  1.298   0.844   0.40 20.65 ?  159 ASN   A ND2  1 
ATOM   3471 N ND2  B ASN   A 1 159 ? 0.438  -0.144  1.321   0.40 25.29 ?  159 ASN   A ND2  1 
ATOM   3472 N ND2  T ASN   A 1 159 ? 0.995  1.285   0.676   0.20 20.01 ?  159 ASN   A ND2  1 
ATOM   3473 H H    A ASN   A 1 159 ? 3.664  -0.147  2.850   0.40 22.72 ?  159 ASN   A H    1 
ATOM   3474 H H    B ASN   A 1 159 ? 3.596  -0.106  2.183   0.40 23.68 ?  159 ASN   A H    1 
ATOM   3475 H H    T ASN   A 1 159 ? 3.741  -0.162  2.649   0.20 22.91 ?  159 ASN   A H    1 
ATOM   3476 H HA   A ASN   A 1 159 ? 2.091  -2.123  2.231   0.40 22.15 ?  159 ASN   A HA   1 
ATOM   3477 H HA   B ASN   A 1 159 ? 2.052  -2.128  1.645   0.40 25.21 ?  159 ASN   A HA   1 
ATOM   3478 H HA   T ASN   A 1 159 ? 2.099  -2.121  2.166   0.20 22.97 ?  159 ASN   A HA   1 
ATOM   3479 H HB2  A ASN   A 1 159 ? 3.051  0.009   0.685   0.40 23.18 ?  159 ASN   A HB2  1 
ATOM   3480 H HB2  B ASN   A 1 159 ? 3.236  -0.341  -0.197  0.40 27.69 ?  159 ASN   A HB2  1 
ATOM   3481 H HB2  T ASN   A 1 159 ? 3.061  -0.081  0.494   0.20 23.42 ?  159 ASN   A HB2  1 
ATOM   3482 H HB3  A ASN   A 1 159 ? 2.174  -1.127  0.002   0.40 23.18 ?  159 ASN   A HB3  1 
ATOM   3483 H HB3  B ASN   A 1 159 ? 2.045  -1.327  -0.563  0.40 27.69 ?  159 ASN   A HB3  1 
ATOM   3484 H HB3  T ASN   A 1 159 ? 2.116  -1.215  -0.096  0.20 23.42 ?  159 ASN   A HB3  1 
ATOM   3485 H HD21 A ASN   A 1 159 ? 0.229  1.740   1.068   0.40 24.81 ?  159 ASN   A HD21 1 
ATOM   3486 H HD21 B ASN   A 1 159 ? -0.157 0.418   1.583   0.40 30.38 ?  159 ASN   A HD21 1 
ATOM   3487 H HD21 T ASN   A 1 159 ? 0.319  1.762   0.908   0.20 24.04 ?  159 ASN   A HD21 1 
ATOM   3488 H HD22 A ASN   A 1 159 ? 1.526  1.660   0.340   0.40 24.81 ?  159 ASN   A HD22 1 
ATOM   3489 H HD22 B ASN   A 1 159 ? 0.378  -0.970  1.554   0.40 30.38 ?  159 ASN   A HD22 1 
ATOM   3490 H HD22 T ASN   A 1 159 ? 1.576  1.598   0.126   0.20 24.04 ?  159 ASN   A HD22 1 
ATOM   3491 N N    A LEU   A 1 160 ? 5.046  -2.467  1.076   0.40 16.93 ?  160 LEU   A N    1 
ATOM   3492 N N    B LEU   A 1 160 ? 5.068  -2.549  0.707   0.40 18.94 ?  160 LEU   A N    1 
ATOM   3493 N N    T LEU   A 1 160 ? 5.007  -2.567  0.993   0.20 18.72 ?  160 LEU   A N    1 
ATOM   3494 C CA   A LEU   A 1 160 ? 5.930  -3.485  0.515   0.40 16.61 ?  160 LEU   A CA   1 
ATOM   3495 C CA   B LEU   A 1 160 ? 6.005  -3.579  0.275   0.40 18.14 ?  160 LEU   A CA   1 
ATOM   3496 C CA   T LEU   A 1 160 ? 5.894  -3.580  0.436   0.20 18.52 ?  160 LEU   A CA   1 
ATOM   3497 C C    A LEU   A 1 160 ? 6.096  -4.661  1.469   0.40 16.10 ?  160 LEU   A C    1 
ATOM   3498 C C    B LEU   A 1 160 ? 6.125  -4.682  1.322   0.40 17.15 ?  160 LEU   A C    1 
ATOM   3499 O O    A LEU   A 1 160 ? 6.118  -5.821  1.040   0.40 16.04 ?  160 LEU   A O    1 
ATOM   3500 O O    B LEU   A 1 160 ? 6.061  -5.873  0.994   0.40 16.98 ?  160 LEU   A O    1 
ATOM   3501 C CB   A LEU   A 1 160 ? 7.285  -2.877  0.166   0.40 16.93 ?  160 LEU   A CB   1 
ATOM   3502 C CB   B LEU   A 1 160 ? 7.364  -2.951  -0.019  0.40 18.41 ?  160 LEU   A CB   1 
ATOM   3503 C CB   T LEU   A 1 160 ? 7.266  -2.984  0.124   0.20 18.45 ?  160 LEU   A CB   1 
ATOM   3504 C CG   A LEU   A 1 160 ? 8.310  -3.890  -0.340  0.40 17.45 ?  160 LEU   A CG   1 
ATOM   3505 C CG   B LEU   A 1 160 ? 8.484  -3.963  -0.261  0.40 19.05 ?  160 LEU   A CG   1 
ATOM   3506 C CG   T LEU   A 1 160 ? 8.320  -3.992  -0.331  0.20 18.51 ?  160 LEU   A CG   1 
ATOM   3507 C CD1  A LEU   A 1 160 ? 7.774  -4.650  -1.540  0.40 17.96 ?  160 LEU   A CD1  1 
ATOM   3508 C CD1  B LEU   A 1 160 ? 8.233  -4.741  -1.539  0.40 19.39 ?  160 LEU   A CD1  1 
ATOM   3509 C CD1  T LEU   A 1 160 ? 7.849  -4.745  -1.561  0.20 18.71 ?  160 LEU   A CD1  1 
ATOM   3510 C CD2  A LEU   A 1 160 ? 9.604  -3.184  -0.691  0.40 17.16 ?  160 LEU   A CD2  1 
ATOM   3511 C CD2  B LEU   A 1 160 ? 9.824  -3.264  -0.304  0.40 19.00 ?  160 LEU   A CD2  1 
ATOM   3512 C CD2  T LEU   A 1 160 ? 9.636  -3.288  -0.604  0.20 18.35 ?  160 LEU   A CD2  1 
ATOM   3513 H H    A LEU   A 1 160 ? 5.424  -1.716  1.275   0.40 20.34 ?  160 LEU   A H    1 
ATOM   3514 H H    B LEU   A 1 160 ? 5.424  -1.787  0.896   0.40 22.76 ?  160 LEU   A H    1 
ATOM   3515 H H    T LEU   A 1 160 ? 5.401  -1.835  1.219   0.20 22.49 ?  160 LEU   A H    1 
ATOM   3516 H HA   A LEU   A 1 160 ? 5.535  -3.812  -0.303  0.40 19.96 ?  160 LEU   A HA   1 
ATOM   3517 H HA   B LEU   A 1 160 ? 5.676  -3.971  -0.548  0.40 21.80 ?  160 LEU   A HA   1 
ATOM   3518 H HB2  A LEU   A 1 160 ? 7.167  -2.201  -0.525  0.40 20.34 ?  160 LEU   A HB2  1 
ATOM   3519 H HB2  B LEU   A 1 160 ? 7.290  -2.392  -0.815  0.40 22.13 ?  160 LEU   A HB2  1 
ATOM   3520 H HB2  T LEU   A 1 160 ? 7.168  -2.315  -0.576  0.20 22.17 ?  160 LEU   A HB2  1 
ATOM   3521 H HB3  A LEU   A 1 160 ? 7.657  -2.471  0.962   0.40 20.34 ?  160 LEU   A HB3  1 
ATOM   3522 H HB3  B LEU   A 1 160 ? 7.621  -2.403  0.738   0.40 22.13 ?  160 LEU   A HB3  1 
ATOM   3523 H HB3  T LEU   A 1 160 ? 7.608  -2.570  0.929   0.20 22.17 ?  160 LEU   A HB3  1 
ATOM   3524 H HG   A LEU   A 1 160 ? 8.506  -4.529  0.364   0.40 20.97 ?  160 LEU   A HG   1 
ATOM   3525 H HG   B LEU   A 1 160 ? 8.513  -4.594  0.473   0.40 22.88 ?  160 LEU   A HG   1 
ATOM   3526 H HG   T LEU   A 1 160 ? 8.469  -4.636  0.380   0.20 22.24 ?  160 LEU   A HG   1 
ATOM   3527 H HD11 A LEU   A 1 160 ? 8.491  -5.183  -1.918  0.40 21.59 ?  160 LEU   A HD11 1 
ATOM   3528 H HD11 B LEU   A 1 160 ? 8.982  -5.334  -1.697  0.40 23.30 ?  160 LEU   A HD11 1 
ATOM   3529 H HD11 T LEU   A 1 160 ? 8.578  -5.293  -1.891  0.20 22.49 ?  160 LEU   A HD11 1 
ATOM   3530 H HD12 A LEU   A 1 160 ? 7.051  -5.228  -1.251  0.40 21.59 ?  160 LEU   A HD12 1 
ATOM   3531 H HD12 B LEU   A 1 160 ? 7.416  -5.256  -1.442  0.40 23.30 ?  160 LEU   A HD12 1 
ATOM   3532 H HD12 T LEU   A 1 160 ? 7.096  -5.305  -1.319  0.20 22.49 ?  160 LEU   A HD12 1 
ATOM   3533 H HD13 A LEU   A 1 160 ? 7.452  -4.015  -2.197  0.40 21.59 ?  160 LEU   A HD13 1 
ATOM   3534 H HD13 B LEU   A 1 160 ? 8.143  -4.116  -2.276  0.40 23.30 ?  160 LEU   A HD13 1 
ATOM   3535 H HD13 T LEU   A 1 160 ? 7.584  -4.104  -2.239  0.20 22.49 ?  160 LEU   A HD13 1 
ATOM   3536 H HD21 A LEU   A 1 160 ? 10.248 -3.839  -1.006  0.40 20.63 ?  160 LEU   A HD21 1 
ATOM   3537 H HD21 B LEU   A 1 160 ? 10.517 -3.925  -0.457  0.40 22.83 ?  160 LEU   A HD21 1 
ATOM   3538 H HD21 T LEU   A 1 160 ? 10.292 -3.944  -0.888  0.20 22.05 ?  160 LEU   A HD21 1 
ATOM   3539 H HD22 A LEU   A 1 160 ? 9.430  -2.531  -1.387  0.40 20.63 ?  160 LEU   A HD22 1 
ATOM   3540 H HD22 B LEU   A 1 160 ? 9.820  -2.616  -1.025  0.40 22.83 ?  160 LEU   A HD22 1 
ATOM   3541 H HD22 T LEU   A 1 160 ? 9.501  -2.630  -1.304  0.20 22.05 ?  160 LEU   A HD22 1 
ATOM   3542 H HD23 A LEU   A 1 160 ? 9.948  -2.739  0.100   0.40 20.63 ?  160 LEU   A HD23 1 
ATOM   3543 H HD23 B LEU   A 1 160 ? 9.975  -2.816  0.543   0.40 22.83 ?  160 LEU   A HD23 1 
ATOM   3544 H HD23 T LEU   A 1 160 ? 9.935  -2.851  0.209   0.20 22.05 ?  160 LEU   A HD23 1 
ATOM   3545 N N    A TYR   A 1 161 ? 6.217  -4.382  2.766   0.60 16.25 ?  161 TYR   A N    1 
ATOM   3546 N N    B TYR   A 1 161 ? 6.315  -4.306  2.589   0.40 16.41 ?  161 TYR   A N    1 
ATOM   3547 C CA   A TYR   A 1 161 ? 6.354  -5.451  3.747   0.60 16.27 ?  161 TYR   A CA   1 
ATOM   3548 C CA   B TYR   A 1 161 ? 6.384  -5.308  3.648   0.40 15.99 ?  161 TYR   A CA   1 
ATOM   3549 C C    A TYR   A 1 161 ? 5.203  -6.449  3.646   0.60 16.87 ?  161 TYR   A C    1 
ATOM   3550 C C    B TYR   A 1 161 ? 5.156  -6.207  3.621   0.40 16.13 ?  161 TYR   A C    1 
ATOM   3551 O O    A TYR   A 1 161 ? 5.420  -7.666  3.610   0.60 17.12 ?  161 TYR   A O    1 
ATOM   3552 O O    B TYR   A 1 161 ? 5.264  -7.436  3.702   0.40 15.87 ?  161 TYR   A O    1 
ATOM   3553 C CB   A TYR   A 1 161 ? 6.433  -4.855  5.150   0.60 16.31 ?  161 TYR   A CB   1 
ATOM   3554 C CB   B TYR   A 1 161 ? 6.514  -4.638  5.018   0.40 15.82 ?  161 TYR   A CB   1 
ATOM   3555 C CG   A TYR   A 1 161 ? 6.350  -5.901  6.221   0.60 15.74 ?  161 TYR   A CG   1 
ATOM   3556 C CG   B TYR   A 1 161 ? 6.401  -5.621  6.170   0.40 15.19 ?  161 TYR   A CG   1 
ATOM   3557 C CD1  A TYR   A 1 161 ? 7.469  -6.627  6.589   0.60 15.82 ?  161 TYR   A CD1  1 
ATOM   3558 C CD1  B TYR   A 1 161 ? 7.512  -6.320  6.626   0.40 15.24 ?  161 TYR   A CD1  1 
ATOM   3559 C CD2  A TYR   A 1 161 ? 5.146  -6.178  6.853   0.60 15.41 ?  161 TYR   A CD2  1 
ATOM   3560 C CD2  B TYR   A 1 161 ? 5.182  -5.848  6.802   0.40 14.91 ?  161 TYR   A CD2  1 
ATOM   3561 C CE1  A TYR   A 1 161 ? 7.398  -7.594  7.555   0.60 15.55 ?  161 TYR   A CE1  1 
ATOM   3562 C CE1  B TYR   A 1 161 ? 7.414  -7.222  7.673   0.40 15.19 ?  161 TYR   A CE1  1 
ATOM   3563 C CE2  A TYR   A 1 161 ? 5.066  -7.148  7.823   0.60 15.22 ?  161 TYR   A CE2  1 
ATOM   3564 C CE2  B TYR   A 1 161 ? 5.076  -6.749  7.851   0.40 14.98 ?  161 TYR   A CE2  1 
ATOM   3565 C CZ   A TYR   A 1 161 ? 6.196  -7.854  8.171   0.60 15.21 ?  161 TYR   A CZ   1 
ATOM   3566 C CZ   B TYR   A 1 161 ? 6.192  -7.430  8.282   0.40 15.24 ?  161 TYR   A CZ   1 
ATOM   3567 O OH   A TYR   A 1 161 ? 6.141  -8.825  9.139   0.60 15.53 ?  161 TYR   A OH   1 
ATOM   3568 O OH   B TYR   A 1 161 ? 6.086  -8.324  9.322   0.40 16.05 ?  161 TYR   A OH   1 
ATOM   3569 H H    A TYR   A 1 161 ? 6.216  -3.593  3.100   0.60 19.52 ?  161 TYR   A H    1 
ATOM   3570 H H    B TYR   A 1 161 ? 6.396  -3.491  2.851   0.40 19.72 ?  161 TYR   A H    1 
ATOM   3571 H HA   A TYR   A 1 161 ? 7.177  -5.933  3.580   0.60 19.55 ?  161 TYR   A HA   1 
ATOM   3572 H HA   B TYR   A 1 161 ? 7.169  -5.859  3.509   0.40 19.21 ?  161 TYR   A HA   1 
ATOM   3573 H HB2  A TYR   A 1 161 ? 7.279  -4.391  5.248   0.60 19.60 ?  161 TYR   A HB2  1 
ATOM   3574 H HB2  B TYR   A 1 161 ? 7.380  -4.202  5.077   0.40 19.01 ?  161 TYR   A HB2  1 
ATOM   3575 H HB3  A TYR   A 1 161 ? 5.697  -4.236  5.274   0.60 19.60 ?  161 TYR   A HB3  1 
ATOM   3576 H HB3  B TYR   A 1 161 ? 5.808  -3.977  5.114   0.40 19.01 ?  161 TYR   A HB3  1 
ATOM   3577 H HD1  A TYR   A 1 161 ? 8.281  -6.455  6.169   0.60 19.02 ?  161 TYR   A HD1  1 
ATOM   3578 H HD1  B TYR   A 1 161 ? 8.335  -6.182  6.218   0.40 18.32 ?  161 TYR   A HD1  1 
ATOM   3579 H HD2  A TYR   A 1 161 ? 4.381  -5.704  6.616   0.60 18.52 ?  161 TYR   A HD2  1 
ATOM   3580 H HD2  B TYR   A 1 161 ? 4.424  -5.389  6.518   0.40 17.92 ?  161 TYR   A HD2  1 
ATOM   3581 H HE1  A TYR   A 1 161 ? 8.158  -8.076  7.790   0.60 18.69 ?  161 TYR   A HE1  1 
ATOM   3582 H HE1  B TYR   A 1 161 ? 8.167  -7.683  7.969   0.40 18.26 ?  161 TYR   A HE1  1 
ATOM   3583 H HE2  A TYR   A 1 161 ? 4.250  -7.327  8.241   0.60 18.29 ?  161 TYR   A HE2  1 
ATOM   3584 H HE2  B TYR   A 1 161 ? 4.253  -6.888  8.267   0.40 18.01 ?  161 TYR   A HE2  1 
ATOM   3585 H HH   A TYR   A 1 161 ? 5.354  -8.893  9.433   0.60 18.66 ?  161 TYR   A HH   1 
ATOM   3586 H HH   B TYR   A 1 161 ? 6.830  -8.669  9.493   0.40 19.28 ?  161 TYR   A HH   1 
ATOM   3587 N N    A ASP   A 1 162 ? 3.965  -5.954  3.614   0.60 17.49 ?  162 ASP   A N    1 
ATOM   3588 N N    B ASP   A 1 162 ? 3.971  -5.602  3.515   0.40 16.76 ?  162 ASP   A N    1 
ATOM   3589 C CA   A ASP   A 1 162 ? 2.817  -6.855  3.531   0.60 18.15 ?  162 ASP   A CA   1 
ATOM   3590 C CA   B ASP   A 1 162 ? 2.744  -6.391  3.497   0.40 17.43 ?  162 ASP   A CA   1 
ATOM   3591 C C    A ASP   A 1 162 ? 2.853  -7.663  2.243   0.60 17.94 ?  162 ASP   A C    1 
ATOM   3592 C C    B ASP   A 1 162 ? 2.769  -7.433  2.384   0.40 18.18 ?  162 ASP   A C    1 
ATOM   3593 O O    A ASP   A 1 162 ? 2.511  -8.852  2.234   0.60 18.41 ?  162 ASP   A O    1 
ATOM   3594 O O    B ASP   A 1 162 ? 2.355  -8.581  2.590   0.40 18.44 ?  162 ASP   A O    1 
ATOM   3595 C CB   A ASP   A 1 162 ? 1.509  -6.064  3.603   0.60 19.43 ?  162 ASP   A CB   1 
ATOM   3596 C CB   B ASP   A 1 162 ? 1.525  -5.475  3.368   0.40 17.41 ?  162 ASP   A CB   1 
ATOM   3597 C CG   A ASP   A 1 162 ? 1.246  -5.469  4.974   0.60 20.98 ?  162 ASP   A CG   1 
ATOM   3598 C CG   B ASP   A 1 162 ? 1.224  -4.720  4.650   0.40 17.24 ?  162 ASP   A CG   1 
ATOM   3599 O OD1  A ASP   A 1 162 ? 1.855  -5.925  5.963   0.60 21.54 ?  162 ASP   A OD1  1 
ATOM   3600 O OD1  B ASP   A 1 162 ? 1.716  -5.134  5.720   0.40 17.26 ?  162 ASP   A OD1  1 
ATOM   3601 O OD2  A ASP   A 1 162 ? 0.393  -4.559  5.066   0.60 21.72 -1 162 ASP   A OD2  1 
ATOM   3602 O OD2  B ASP   A 1 162 ? 0.483  -3.717  4.590   0.40 17.87 -1 162 ASP   A OD2  1 
ATOM   3603 H H    A ASP   A 1 162 ? 3.764  -5.123  3.632   0.60 21.01 ?  162 ASP   A H    1 
ATOM   3604 H H    B ASP   A 1 162 ? 3.855  -4.747  3.465   0.40 20.14 ?  162 ASP   A H    1 
ATOM   3605 H HA   A ASP   A 1 162 ? 2.836  -7.477  4.274   0.60 21.81 ?  162 ASP   A HA   1 
ATOM   3606 H HA   B ASP   A 1 162 ? 2.670  -6.863  4.336   0.40 20.95 ?  162 ASP   A HA   1 
ATOM   3607 H HB2  A ASP   A 1 162 ? 1.544  -5.338  2.964   0.60 23.35 ?  162 ASP   A HB2  1 
ATOM   3608 H HB2  B ASP   A 1 162 ? 1.685  -4.824  2.666   0.40 20.92 ?  162 ASP   A HB2  1 
ATOM   3609 H HB3  A ASP   A 1 162 ? 0.768  -6.658  3.391   0.60 23.35 ?  162 ASP   A HB3  1 
ATOM   3610 H HB3  B ASP   A 1 162 ? 0.746  -6.009  3.158   0.40 20.92 ?  162 ASP   A HB3  1 
ATOM   3611 N N    A LYS   A 1 163 ? 3.242  -7.030  1.137   0.60 18.38 ?  163 LYS   A N    1 
ATOM   3612 N N    B LYS   A 1 163 ? 3.249  -7.057  1.197   0.40 19.32 ?  163 LYS   A N    1 
ATOM   3613 C CA   A LYS   A 1 163 ? 3.351  -7.761  -0.119  0.60 18.82 ?  163 LYS   A CA   1 
ATOM   3614 C CA   B LYS   A 1 163 ? 3.324  -8.024  0.105   0.40 20.39 ?  163 LYS   A CA   1 
ATOM   3615 C C    A LYS   A 1 163 ? 4.434  -8.829  -0.038  0.60 17.60 ?  163 LYS   A C    1 
ATOM   3616 C C    B LYS   A 1 163 ? 4.382  -9.093  0.373   0.40 19.78 ?  163 LYS   A C    1 
ATOM   3617 O O    A LYS   A 1 163 ? 4.274  -9.926  -0.583  0.60 17.26 ?  163 LYS   A O    1 
ATOM   3618 O O    B LYS   A 1 163 ? 4.191  -10.262 0.020   0.40 19.44 ?  163 LYS   A O    1 
ATOM   3619 C CB   A LYS   A 1 163 ? 3.628  -6.804  -1.278  0.60 21.38 ?  163 LYS   A CB   1 
ATOM   3620 C CB   B LYS   A 1 163 ? 3.578  -7.303  -1.222  0.40 22.58 ?  163 LYS   A CB   1 
ATOM   3621 C CG   A LYS   A 1 163 ? 3.656  -7.514  -2.621  0.60 23.89 ?  163 LYS   A CG   1 
ATOM   3622 C CG   B LYS   A 1 163 ? 3.798  -8.227  -2.416  0.40 24.84 ?  163 LYS   A CG   1 
ATOM   3623 C CD   A LYS   A 1 163 ? 4.127  -6.621  -3.747  0.60 26.23 ?  163 LYS   A CD   1 
ATOM   3624 C CD   B LYS   A 1 163 ? 4.142  -7.437  -3.670  0.40 26.81 ?  163 LYS   A CD   1 
ATOM   3625 C CE   A LYS   A 1 163 ? 4.047  -7.356  -5.076  0.60 28.01 ?  163 LYS   A CE   1 
ATOM   3626 C CE   B LYS   A 1 163 ? 2.910  -6.805  -4.300  0.40 28.34 ?  163 LYS   A CE   1 
ATOM   3627 N NZ   A LYS   A 1 163 ? 4.685  -6.595  -6.183  0.60 29.10 ?  163 LYS   A NZ   1 
ATOM   3628 N NZ   B LYS   A 1 163 ? 2.093  -7.804  -5.045  0.40 29.23 ?  163 LYS   A NZ   1 
ATOM   3629 H H    A LYS   A 1 163 ? 3.426  -6.191  1.089   0.60 22.08 ?  163 LYS   A H    1 
ATOM   3630 H H    B LYS   A 1 163 ? 3.514  -6.257  0.995   0.40 23.21 ?  163 LYS   A H    1 
ATOM   3631 H HA   A LYS   A 1 163 ? 2.504  -8.201  -0.298  0.60 22.61 ?  163 LYS   A HA   1 
ATOM   3632 H HA   B LYS   A 1 163 ? 2.470  -8.470  0.033   0.40 24.50 ?  163 LYS   A HA   1 
ATOM   3633 H HB2  A LYS   A 1 163 ? 2.923  -6.129  -1.312  0.60 25.69 ?  163 LYS   A HB2  1 
ATOM   3634 H HB2  B LYS   A 1 163 ? 2.807  -6.745  -1.425  0.40 27.13 ?  163 LYS   A HB2  1 
ATOM   3635 H HB3  A LYS   A 1 163 ? 4.485  -6.376  -1.143  0.60 25.69 ?  163 LYS   A HB3  1 
ATOM   3636 H HB3  B LYS   A 1 163 ? 4.365  -6.747  -1.134  0.40 27.13 ?  163 LYS   A HB3  1 
ATOM   3637 H HG2  A LYS   A 1 163 ? 4.261  -8.270  -2.571  0.60 28.70 ?  163 LYS   A HG2  1 
ATOM   3638 H HG2  B LYS   A 1 163 ? 4.535  -8.828  -2.232  0.40 29.84 ?  163 LYS   A HG2  1 
ATOM   3639 H HG3  A LYS   A 1 163 ? 2.760  -7.821  -2.835  0.60 28.70 ?  163 LYS   A HG3  1 
ATOM   3640 H HG3  B LYS   A 1 163 ? 2.986  -8.730  -2.587  0.40 29.84 ?  163 LYS   A HG3  1 
ATOM   3641 H HD2  A LYS   A 1 163 ? 3.562  -5.836  -3.795  0.60 31.51 ?  163 LYS   A HD2  1 
ATOM   3642 H HD2  B LYS   A 1 163 ? 4.764  -6.728  -3.440  0.40 32.20 ?  163 LYS   A HD2  1 
ATOM   3643 H HD3  A LYS   A 1 163 ? 5.051  -6.366  -3.591  0.60 31.51 ?  163 LYS   A HD3  1 
ATOM   3644 H HD3  B LYS   A 1 163 ? 4.543  -8.034  -4.322  0.40 32.20 ?  163 LYS   A HD3  1 
ATOM   3645 H HE2  A LYS   A 1 163 ? 4.493  -8.214  -4.995  0.60 33.64 ?  163 LYS   A HE2  1 
ATOM   3646 H HE2  B LYS   A 1 163 ? 2.355  -6.419  -3.604  0.40 34.04 ?  163 LYS   A HE2  1 
ATOM   3647 H HE3  A LYS   A 1 163 ? 3.116  -7.492  -5.305  0.60 33.64 ?  163 LYS   A HE3  1 
ATOM   3648 H HE3  B LYS   A 1 163 ? 3.189  -6.116  -4.924  0.40 34.04 ?  163 LYS   A HE3  1 
ATOM   3649 H HZ1  A LYS   A 1 163 ? 4.620  -7.053  -6.944  0.60 34.94 ?  163 LYS   A HZ1  1 
ATOM   3650 H HZ1  B LYS   A 1 163 ? 1.380  -7.408  -5.403  0.40 35.11 ?  163 LYS   A HZ1  1 
ATOM   3651 H HZ2  A LYS   A 1 163 ? 4.278  -5.810  -6.283  0.60 34.94 ?  163 LYS   A HZ2  1 
ATOM   3652 H HZ2  B LYS   A 1 163 ? 2.578  -8.168  -5.697  0.40 35.11 ?  163 LYS   A HZ2  1 
ATOM   3653 H HZ3  A LYS   A 1 163 ? 5.544  -6.455  -6.001  0.60 34.94 ?  163 LYS   A HZ3  1 
ATOM   3654 H HZ3  B LYS   A 1 163 ? 1.821  -8.447  -4.494  0.40 35.11 ?  163 LYS   A HZ3  1 
ATOM   3655 N N    A LEU   A 1 164 ? 5.553  -8.520  0.622   0.60 15.75 ?  164 LEU   A N    1 
ATOM   3656 N N    B LEU   A 1 164 ? 5.501  -8.718  0.999   0.40 19.32 ?  164 LEU   A N    1 
ATOM   3657 C CA   A LEU   A 1 164 ? 6.623  -9.504  0.761   0.60 15.43 ?  164 LEU   A CA   1 
ATOM   3658 C CA   B LEU   A 1 164 ? 6.581  -9.678  1.216   0.40 19.18 ?  164 LEU   A CA   1 
ATOM   3659 C C    A LEU   A 1 164 ? 6.184  -10.684 1.621   0.60 15.18 ?  164 LEU   A C    1 
ATOM   3660 C C    B LEU   A 1 164 ? 6.157  -10.791 2.166   0.40 19.56 ?  164 LEU   A C    1 
ATOM   3661 O O    A LEU   A 1 164 ? 6.467  -11.840 1.285   0.60 15.06 ?  164 LEU   A O    1 
ATOM   3662 O O    B LEU   A 1 164 ? 6.460  -11.965 1.927   0.40 19.37 ?  164 LEU   A O    1 
ATOM   3663 C CB   A LEU   A 1 164 ? 7.858  -8.846  1.371   0.60 15.61 ?  164 LEU   A CB   1 
ATOM   3664 C CB   B LEU   A 1 164 ? 7.821  -8.964  1.754   0.40 18.74 ?  164 LEU   A CB   1 
ATOM   3665 C CG   A LEU   A 1 164 ? 8.647  -7.877  0.489   0.60 15.53 ?  164 LEU   A CG   1 
ATOM   3666 C CG   B LEU   A 1 164 ? 8.573  -8.071  0.768   0.40 18.97 ?  164 LEU   A CG   1 
ATOM   3667 C CD1  A LEU   A 1 164 ? 9.553  -7.007  1.350   0.60 15.21 ?  164 LEU   A CD1  1 
ATOM   3668 C CD1  B LEU   A 1 164 ? 9.716  -7.367  1.475   0.40 19.24 ?  164 LEU   A CD1  1 
ATOM   3669 C CD2  A LEU   A 1 164 ? 9.467  -8.637  -0.543  0.60 15.45 ?  164 LEU   A CD2  1 
ATOM   3670 C CD2  B LEU   A 1 164 ? 9.092  -8.889  -0.405  0.40 18.94 ?  164 LEU   A CD2  1 
ATOM   3671 H H    A LEU   A 1 164 ? 5.713  -7.751  0.989   0.60 18.93 ?  164 LEU   A H    1 
ATOM   3672 H H    B LEU   A 1 164 ? 5.655  -7.931  1.307   0.40 23.21 ?  164 LEU   A H    1 
ATOM   3673 H HA   A LEU   A 1 164 ? 6.858  -9.834  -0.119  0.60 18.55 ?  164 LEU   A HA   1 
ATOM   3674 H HA   B LEU   A 1 164 ? 6.815  -10.088 0.369   0.40 23.05 ?  164 LEU   A HA   1 
ATOM   3675 H HB2  A LEU   A 1 164 ? 7.578  -8.352  2.156   0.60 18.76 ?  164 LEU   A HB2  1 
ATOM   3676 H HB2  B LEU   A 1 164 ? 7.554  -8.402  2.496   0.40 22.51 ?  164 LEU   A HB2  1 
ATOM   3677 H HB3  A LEU   A 1 164 ? 8.468  -9.549  1.634   0.60 18.76 ?  164 LEU   A HB3  1 
ATOM   3678 H HB3  B LEU   A 1 164 ? 8.451  -9.632  2.065   0.40 22.51 ?  164 LEU   A HB3  1 
ATOM   3679 H HG   A LEU   A 1 164 ? 8.030  -7.294  0.020   0.60 18.66 ?  164 LEU   A HG   1 
ATOM   3680 H HG   B LEU   A 1 164 ? 7.972  -7.393  0.422   0.40 22.80 ?  164 LEU   A HG   1 
ATOM   3681 H HD11 A LEU   A 1 164 ? 10.048 -6.400  0.778   0.60 18.28 ?  164 LEU   A HD11 1 
ATOM   3682 H HD11 B LEU   A 1 164 ? 10.184 -6.803  0.840   0.40 23.12 ?  164 LEU   A HD11 1 
ATOM   3683 H HD12 A LEU   A 1 164 ? 9.006  -6.499  1.974   0.60 18.28 ?  164 LEU   A HD12 1 
ATOM   3684 H HD12 B LEU   A 1 164 ? 9.356  -6.828  2.197   0.40 23.12 ?  164 LEU   A HD12 1 
ATOM   3685 H HD13 A LEU   A 1 164 ? 10.167 -7.576  1.840   0.60 18.28 ?  164 LEU   A HD13 1 
ATOM   3686 H HD13 B LEU   A 1 164 ? 10.323 -8.035  1.834   0.40 23.12 ?  164 LEU   A HD13 1 
ATOM   3687 H HD21 A LEU   A 1 164 ? 9.965  -8.001  -1.080  0.60 18.57 ?  164 LEU   A HD21 1 
ATOM   3688 H HD21 B LEU   A 1 164 ? 9.723  -8.353  -0.910  0.40 22.75 ?  164 LEU   A HD21 1 
ATOM   3689 H HD22 A LEU   A 1 164 ? 10.077 -9.234  -0.084  0.60 18.57 ?  164 LEU   A HD22 1 
ATOM   3690 H HD22 B LEU   A 1 164 ? 9.531  -9.684  -0.063  0.40 22.75 ?  164 LEU   A HD22 1 
ATOM   3691 H HD23 A LEU   A 1 164 ? 8.865  -9.146  -1.107  0.60 18.57 ?  164 LEU   A HD23 1 
ATOM   3692 H HD23 B LEU   A 1 164 ? 8.345  -9.141  -0.969  0.40 22.75 ?  164 LEU   A HD23 1 
ATOM   3693 N N    A VAL   A 1 165 ? 5.509  -10.411 2.741   0.60 14.66 ?  165 VAL   A N    1 
ATOM   3694 N N    B VAL   A 1 165 ? 5.465  -10.444 3.253   0.40 19.93 ?  165 VAL   A N    1 
ATOM   3695 C CA   A VAL   A 1 165 ? 5.042  -11.484 3.616   0.60 14.99 ?  165 VAL   A CA   1 
ATOM   3696 C CA   B VAL   A 1 165 ? 5.054  -11.464 4.214   0.40 21.19 ?  165 VAL   A CA   1 
ATOM   3697 C C    A VAL   A 1 165 ? 4.019  -12.345 2.897   0.60 15.69 ?  165 VAL   A C    1 
ATOM   3698 C C    B VAL   A 1 165 ? 3.944  -12.334 3.638   0.40 22.04 ?  165 VAL   A C    1 
ATOM   3699 O O    A VAL   A 1 165 ? 4.118  -13.578 2.880   0.60 15.42 ?  165 VAL   A O    1 
ATOM   3700 O O    B VAL   A 1 165 ? 3.911  -13.549 3.867   0.40 22.93 ?  165 VAL   A O    1 
ATOM   3701 C CB   A VAL   A 1 165 ? 4.461  -10.898 4.915   0.60 15.35 ?  165 VAL   A CB   1 
ATOM   3702 C CB   B VAL   A 1 165 ? 4.675  -10.834 5.569   0.40 21.84 ?  165 VAL   A CB   1 
ATOM   3703 C CG1  A VAL   A 1 165 ? 3.731  -11.976 5.714   0.60 15.46 ?  165 VAL   A CG1  1 
ATOM   3704 C CG1  B VAL   A 1 165 ? 5.911  -10.257 6.245   0.40 22.09 ?  165 VAL   A CG1  1 
ATOM   3705 C CG2  A VAL   A 1 165 ? 5.561  -10.248 5.738   0.60 16.00 ?  165 VAL   A CG2  1 
ATOM   3706 C CG2  B VAL   A 1 165 ? 3.608  -9.761  5.398   0.40 22.20 ?  165 VAL   A CG2  1 
ATOM   3707 H H    A VAL   A 1 165 ? 5.319  -9.617  3.010   0.60 17.62 ?  165 VAL   A H    1 
ATOM   3708 H H    B VAL   A 1 165 ? 5.230  -9.641  3.447   0.40 23.94 ?  165 VAL   A H    1 
ATOM   3709 H HA   A VAL   A 1 165 ? 5.794  -12.047 3.848   0.60 18.02 ?  165 VAL   A HA   1 
ATOM   3710 H HA   B VAL   A 1 165 ? 5.809  -12.045 4.377   0.40 25.46 ?  165 VAL   A HA   1 
ATOM   3711 H HB   A VAL   A 1 165 ? 3.819  -10.209 4.685   0.60 18.44 ?  165 VAL   A HB   1 
ATOM   3712 H HB   B VAL   A 1 165 ? 4.316  -11.522 6.150   0.40 26.24 ?  165 VAL   A HB   1 
ATOM   3713 H HG11 A VAL   A 1 165 ? 3.631  -11.671 6.627   0.60 18.58 ?  165 VAL   A HG11 1 
ATOM   3714 H HG11 B VAL   A 1 165 ? 5.667  -9.933  7.126   0.40 26.54 ?  165 VAL   A HG11 1 
ATOM   3715 H HG12 A VAL   A 1 165 ? 2.859  -12.126 5.316   0.60 18.58 ?  165 VAL   A HG12 1 
ATOM   3716 H HG12 B VAL   A 1 165 ? 6.581  -10.954 6.323   0.40 26.54 ?  165 VAL   A HG12 1 
ATOM   3717 H HG13 A VAL   A 1 165 ? 4.254  -12.791 5.691   0.60 18.58 ?  165 VAL   A HG13 1 
ATOM   3718 H HG13 B VAL   A 1 165 ? 6.253  -9.527  5.706   0.40 26.54 ?  165 VAL   A HG13 1 
ATOM   3719 H HG21 A VAL   A 1 165 ? 5.177  -9.906  6.560   0.60 19.23 ?  165 VAL   A HG21 1 
ATOM   3720 H HG21 B VAL   A 1 165 ? 3.292  -9.491  6.274   0.40 26.66 ?  165 VAL   A HG21 1 
ATOM   3721 H HG22 A VAL   A 1 165 ? 6.239  -10.911 5.940   0.60 19.23 ?  165 VAL   A HG22 1 
ATOM   3722 H HG22 B VAL   A 1 165 ? 3.994  -8.998  4.941   0.40 26.66 ?  165 VAL   A HG22 1 
ATOM   3723 H HG23 A VAL   A 1 165 ? 5.953  -9.520  5.228   0.60 19.23 ?  165 VAL   A HG23 1 
ATOM   3724 H HG23 B VAL   A 1 165 ? 2.876  -10.124 4.880   0.40 26.66 ?  165 VAL   A HG23 1 
ATOM   3725 N N    A SER   A 1 166 ? 3.012  -11.702 2.301   0.60 15.71 ?  166 SER   A N    1 
ATOM   3726 N N    B SER   A 1 166 ? 3.036  -11.741 2.860   0.40 22.04 ?  166 SER   A N    1 
ATOM   3727 C CA   A SER   A 1 166 ? 1.901  -12.441 1.709   0.60 16.96 ?  166 SER   A CA   1 
ATOM   3728 C CA   B SER   A 1 166 ? 1.928  -12.487 2.275   0.40 22.50 ?  166 SER   A CA   1 
ATOM   3729 C C    A SER   A 1 166 ? 2.351  -13.289 0.535   0.60 17.42 ?  166 SER   A C    1 
ATOM   3730 C C    B SER   A 1 166 ? 2.321  -13.231 1.007   0.40 23.54 ?  166 SER   A C    1 
ATOM   3731 O O    A SER   A 1 166 ? 1.721  -14.312 0.236   0.60 19.52 ?  166 SER   A O    1 
ATOM   3732 O O    B SER   A 1 166 ? 1.440  -13.670 0.255   0.40 23.51 ?  166 SER   A O    1 
ATOM   3733 C CB   A SER   A 1 166 ? 0.803  -11.477 1.250   0.60 18.23 ?  166 SER   A CB   1 
ATOM   3734 C CB   B SER   A 1 166 ? 0.745  -11.559 1.993   0.40 22.10 ?  166 SER   A CB   1 
ATOM   3735 O OG   A SER   A 1 166 ? 0.145  -10.865 2.349   0.60 19.86 ?  166 SER   A OG   1 
ATOM   3736 O OG   B SER   A 1 166 ? 1.022  -10.708 0.895   0.40 21.97 ?  166 SER   A OG   1 
ATOM   3737 H H    A SER   A 1 166 ? 2.938  -10.848 2.233   0.60 18.88 ?  166 SER   A H    1 
ATOM   3738 H H    B SER   A 1 166 ? 3.046  -10.904 2.651   0.40 26.48 ?  166 SER   A H    1 
ATOM   3739 H HA   A SER   A 1 166 ? 1.518  -13.037 2.368   0.60 20.38 ?  166 SER   A HA   1 
ATOM   3740 H HA   B SER   A 1 166 ? 1.632  -13.146 2.918   0.40 27.03 ?  166 SER   A HA   1 
ATOM   3741 H HB2  A SER   A 1 166 ? 1.201  -10.790 0.691   0.60 21.90 ?  166 SER   A HB2  1 
ATOM   3742 H HB2  B SER   A 1 166 ? -0.035 -12.098 1.786   0.40 26.55 ?  166 SER   A HB2  1 
ATOM   3743 H HB3  A SER   A 1 166 ? 0.142  -11.971 0.735   0.60 21.90 ?  166 SER   A HB3  1 
ATOM   3744 H HB3  B SER   A 1 166 ? 0.569  -11.023 2.783   0.40 26.55 ?  166 SER   A HB3  1 
ATOM   3745 H HG   A SER   A 1 166 ? -0.441 -10.333 2.072   0.60 23.86 ?  166 SER   A HG   1 
ATOM   3746 H HG   B SER   A 1 166 ? 1.691  -10.230 1.067   0.40 26.40 ?  166 SER   A HG   1 
ATOM   3747 N N    A SER   A 1 167 ? 3.422  -12.883 -0.148  0.60 16.40 ?  167 SER   A N    1 
ATOM   3748 N N    B SER   A 1 167 ? 3.624  -13.377 0.762   0.40 25.02 ?  167 SER   A N    1 
ATOM   3749 C CA   A SER   A 1 167 ? 3.903  -13.592 -1.323  0.60 16.68 ?  167 SER   A CA   1 
ATOM   3750 C CA   B SER   A 1 167 ? 4.135  -14.094 -0.393  0.40 26.43 ?  167 SER   A CA   1 
ATOM   3751 C C    A SER   A 1 167 ? 5.050  -14.548 -1.016  0.60 17.05 ?  167 SER   A C    1 
ATOM   3752 C C    B SER   A 1 167 ? 5.079  -15.229 -0.033  0.40 27.31 ?  167 SER   A C    1 
ATOM   3753 O O    A SER   A 1 167 ? 5.536  -15.220 -1.930  0.60 17.94 ?  167 SER   A O    1 
ATOM   3754 O O    B SER   A 1 167 ? 5.262  -16.134 -0.855  0.40 27.43 ?  167 SER   A O    1 
ATOM   3755 C CB   A SER   A 1 167 ? 4.332  -12.594 -2.413  0.60 17.57 ?  167 SER   A CB   1 
ATOM   3756 C CB   B SER   A 1 167 ? 4.880  -13.133 -1.332  0.40 27.33 ?  167 SER   A CB   1 
ATOM   3757 O OG   A SER   A 1 167 ? 5.379  -11.755 -1.956  0.60 18.02 ?  167 SER   A OG   1 
ATOM   3758 O OG   B SER   A 1 167 ? 5.626  -13.844 -2.302  0.40 28.11 ?  167 SER   A OG   1 
ATOM   3759 H H    A SER   A 1 167 ? 3.880  -12.172 0.041   0.60 19.71 ?  167 SER   A H    1 
ATOM   3760 H H    B SER   A 1 167 ? 4.244  -13.067 1.269   0.40 30.06 ?  167 SER   A H    1 
ATOM   3761 H HA   A SER   A 1 167 ? 3.176  -14.109 -1.691  0.60 20.04 ?  167 SER   A HA   1 
ATOM   3762 H HA   B SER   A 1 167 ? 3.391  -14.474 -0.883  0.40 31.75 ?  167 SER   A HA   1 
ATOM   3763 H HB2  A SER   A 1 167 ? 4.646  -13.085 -3.192  0.60 21.11 ?  167 SER   A HB2  1 
ATOM   3764 H HB2  B SER   A 1 167 ? 4.233  -12.579 -1.790  0.40 32.82 ?  167 SER   A HB2  1 
ATOM   3765 H HB3  A SER   A 1 167 ? 3.565  -12.046 -2.669  0.60 21.11 ?  167 SER   A HB3  1 
ATOM   3766 H HB3  B SER   A 1 167 ? 5.478  -12.579 -0.804  0.40 32.82 ?  167 SER   A HB3  1 
ATOM   3767 H HG   A SER   A 1 167 ? 5.106  -11.299 -1.301  0.60 21.65 ?  167 SER   A HG   1 
ATOM   3768 H HG   B SER   A 1 167 ? 6.042  -13.307 -2.795  0.40 33.76 ?  167 SER   A HG   1 
ATOM   3769 N N    A PHE   A 1 168 ? 5.495  -14.633 0.235   0.60 16.99 ?  168 PHE   A N    1 
ATOM   3770 N N    B PHE   A 1 168 ? 5.675  -15.213 1.161   0.40 28.39 ?  168 PHE   A N    1 
ATOM   3771 C CA   A PHE   A 1 168 ? 6.669  -15.445 0.538   0.60 17.05 ?  168 PHE   A CA   1 
ATOM   3772 C CA   B PHE   A 1 168 ? 6.669  -16.201 1.555   0.40 29.72 ?  168 PHE   A CA   1 
ATOM   3773 C C    A PHE   A 1 168 ? 6.352  -16.927 0.405   0.60 18.46 ?  168 PHE   A C    1 
ATOM   3774 C C    B PHE   A 1 168 ? 6.185  -17.179 2.614   0.40 30.43 ?  168 PHE   A C    1 
ATOM   3775 O O    A PHE   A 1 168 ? 5.345  -17.407 0.933   0.60 20.10 ?  168 PHE   A O    1 
ATOM   3776 O O    B PHE   A 1 168 ? 6.869  -18.180 2.859   0.40 30.69 ?  168 PHE   A O    1 
ATOM   3777 C CB   A PHE   A 1 168 ? 7.178  -15.175 1.950   0.60 16.46 ?  168 PHE   A CB   1 
ATOM   3778 C CB   B PHE   A 1 168 ? 7.941  -15.506 2.064   0.40 30.25 ?  168 PHE   A CB   1 
ATOM   3779 C CG   A PHE   A 1 168 ? 8.444  -15.930 2.272   0.60 16.01 ?  168 PHE   A CG   1 
ATOM   3780 C CG   B PHE   A 1 168 ? 8.941  -15.210 0.987   0.40 30.66 ?  168 PHE   A CG   1 
ATOM   3781 C CD1  A PHE   A 1 168 ? 9.635  -15.575 1.671   0.60 16.29 ?  168 PHE   A CD1  1 
ATOM   3782 C CD1  B PHE   A 1 168 ? 8.735  -14.172 0.100   0.40 30.75 ?  168 PHE   A CD1  1 
ATOM   3783 C CD2  A PHE   A 1 168 ? 8.442  -17.011 3.142   0.60 15.35 ?  168 PHE   A CD2  1 
ATOM   3784 C CD2  B PHE   A 1 168 ? 10.093 -15.969 0.865   0.40 30.82 ?  168 PHE   A CD2  1 
ATOM   3785 C CE1  A PHE   A 1 168 ? 10.801 -16.267 1.942   0.60 15.81 ?  168 PHE   A CE1  1 
ATOM   3786 C CE1  B PHE   A 1 168 ? 9.655  -13.899 -0.889  0.40 30.78 ?  168 PHE   A CE1  1 
ATOM   3787 C CE2  A PHE   A 1 168 ? 9.614  -17.707 3.420   0.60 15.79 ?  168 PHE   A CE2  1 
ATOM   3788 C CE2  B PHE   A 1 168 ? 11.017 -15.696 -0.125  0.40 30.90 ?  168 PHE   A CE2  1 
ATOM   3789 C CZ   A PHE   A 1 168 ? 10.791 -17.329 2.817   0.60 15.75 ?  168 PHE   A CZ   1 
ATOM   3790 C CZ   B PHE   A 1 168 ? 10.796 -14.660 -1.003  0.40 30.87 ?  168 PHE   A CZ   1 
ATOM   3791 H H    A PHE   A 1 168 ? 5.146  -14.227 0.909   0.60 20.42 ?  168 PHE   A H    1 
ATOM   3792 H H    B PHE   A 1 168 ? 5.515  -14.625 1.769   0.40 34.10 ?  168 PHE   A H    1 
ATOM   3793 H HA   A PHE   A 1 168 ? 7.375  -15.226 -0.091  0.60 20.49 ?  168 PHE   A HA   1 
ATOM   3794 H HA   B PHE   A 1 168 ? 6.913  -16.724 0.781   0.40 35.69 ?  168 PHE   A HA   1 
ATOM   3795 H HB2  A PHE   A 1 168 ? 7.363  -14.229 2.042   0.60 19.79 ?  168 PHE   A HB2  1 
ATOM   3796 H HB2  B PHE   A 1 168 ? 7.697  -14.663 2.478   0.40 36.33 ?  168 PHE   A HB2  1 
ATOM   3797 H HB3  A PHE   A 1 168 ? 6.498  -15.446 2.585   0.60 19.79 ?  168 PHE   A HB3  1 
ATOM   3798 H HB3  B PHE   A 1 168 ? 8.374  -16.078 2.717   0.40 36.33 ?  168 PHE   A HB3  1 
ATOM   3799 H HD1  A PHE   A 1 168 ? 9.659  -14.858 1.077   0.60 19.57 ?  168 PHE   A HD1  1 
ATOM   3800 H HD1  B PHE   A 1 168 ? 7.965  -13.653 0.167   0.40 36.92 ?  168 PHE   A HD1  1 
ATOM   3801 H HD2  A PHE   A 1 168 ? 7.646  -17.269 3.551   0.60 18.45 ?  168 PHE   A HD2  1 
ATOM   3802 H HD2  B PHE   A 1 168 ? 10.245 -16.669 1.456   0.40 37.02 ?  168 PHE   A HD2  1 
ATOM   3803 H HE1  A PHE   A 1 168 ? 11.603 -16.013 1.536   0.60 19.01 ?  168 PHE   A HE1  1 
ATOM   3804 H HE1  B PHE   A 1 168 ? 9.504  -13.201 -1.475  0.40 36.96 ?  168 PHE   A HE1  1 
ATOM   3805 H HE2  A PHE   A 1 168 ? 9.598  -18.426 4.010   0.60 18.98 ?  168 PHE   A HE2  1 
ATOM   3806 H HE2  B PHE   A 1 168 ? 11.786 -16.212 -0.199  0.40 37.11 ?  168 PHE   A HE2  1 
ATOM   3807 H HZ   A PHE   A 1 168 ? 11.578 -17.793 2.999   0.60 18.93 ?  168 PHE   A HZ   1 
ATOM   3808 H HZ   B PHE   A 1 168 ? 11.415 -14.472 -1.672  0.40 37.07 ?  168 PHE   A HZ   1 
ATOM   3809 N N    A LEU   A 1 169 ? 7.232  -17.659 -0.271  0.60 19.98 ?  169 LEU   A N    1 
ATOM   3810 N N    B LEU   A 1 169 ? 5.037  -16.935 3.239   0.40 30.81 ?  169 LEU   A N    1 
ATOM   3811 C CA   A LEU   A 1 169 ? 7.035  -19.093 -0.434  0.60 22.77 ?  169 LEU   A CA   1 
ATOM   3812 C CA   B LEU   A 1 169 ? 4.575  -17.812 4.307   0.40 31.14 ?  169 LEU   A CA   1 
ATOM   3813 C C    A LEU   A 1 169 ? 7.884  -19.866 0.566   0.60 23.21 ?  169 LEU   A C    1 
ATOM   3814 C C    B LEU   A 1 169 ? 3.539  -18.806 3.788   0.40 32.03 ?  169 LEU   A C    1 
ATOM   3815 O O    A LEU   A 1 169 ? 7.340  -20.400 1.535   0.60 23.65 ?  169 LEU   A O    1 
ATOM   3816 O O    B LEU   A 1 169 ? 3.764  -20.016 3.815   0.40 32.30 ?  169 LEU   A O    1 
ATOM   3817 C CB   A LEU   A 1 169 ? 7.342  -19.531 -1.871  0.60 24.91 ?  169 LEU   A CB   1 
ATOM   3818 C CB   B LEU   A 1 169 ? 4.015  -16.996 5.478   0.40 30.54 ?  169 LEU   A CB   1 
ATOM   3819 C CG   A LEU   A 1 169 ? 7.039  -20.997 -2.202  0.60 26.55 ?  169 LEU   A CG   1 
ATOM   3820 C CG   B LEU   A 1 169 ? 5.090  -16.291 6.312   0.40 29.92 ?  169 LEU   A CG   1 
ATOM   3821 C CD1  A LEU   A 1 169 ? 5.622  -21.372 -1.788  0.60 27.20 ?  169 LEU   A CD1  1 
ATOM   3822 C CD1  B LEU   A 1 169 ? 4.492  -15.633 7.539   0.40 29.78 ?  169 LEU   A CD1  1 
ATOM   3823 C CD2  A LEU   A 1 169 ? 7.245  -21.276 -3.685  0.60 27.07 ?  169 LEU   A CD2  1 
ATOM   3824 C CD2  B LEU   A 1 169 ? 6.182  -17.270 6.715   0.40 29.59 ?  169 LEU   A CD2  1 
ATOM   3825 O OXT  A LEU   A 1 169 ? 9.108  -19.965 0.442   0.60 23.51 -1 169 LEU   A OXT  1 
ATOM   3826 O OXT  B LEU   A 1 169 ? 2.466  -18.428 3.317   0.40 32.39 -1 169 LEU   A OXT  1 
ATOM   3827 H H    A LEU   A 1 169 ? 7.943  -17.350 -0.641  0.60 24.01 ?  169 LEU   A H    1 
ATOM   3828 H H    B LEU   A 1 169 ? 4.503  -16.284 3.058   0.40 37.00 ?  169 LEU   A H    1 
ATOM   3829 H HA   A LEU   A 1 169 ? 6.111  -19.305 -0.248  0.60 27.35 ?  169 LEU   A HA   1 
ATOM   3830 H HA   B LEU   A 1 169 ? 5.337  -18.310 4.637   0.40 37.40 ?  169 LEU   A HA   1 
ATOM   3831 H HB2  A LEU   A 1 169 ? 6.812  -18.987 -2.476  0.60 29.92 ?  169 LEU   A HB2  1 
ATOM   3832 H HB2  B LEU   A 1 169 ? 3.418  -16.313 5.131   0.40 36.67 ?  169 LEU   A HB2  1 
ATOM   3833 H HB3  A LEU   A 1 169 ? 8.282  -19.387 -2.046  0.60 29.92 ?  169 LEU   A HB3  1 
ATOM   3834 H HB3  B LEU   A 1 169 ? 3.523  -17.586 6.073   0.40 36.67 ?  169 LEU   A HB3  1 
ATOM   3835 H HG   A LEU   A 1 169 ? 7.650  -21.565 -1.708  0.60 31.89 ?  169 LEU   A HG   1 
ATOM   3836 H HG   B LEU   A 1 169 ? 5.497  -15.595 5.773   0.40 35.93 ?  169 LEU   A HG   1 
ATOM   3837 H HD11 A LEU   A 1 169 ? 5.392  -22.227 -2.184  0.60 32.66 ?  169 LEU   A HD11 1 
ATOM   3838 H HD11 B LEU   A 1 169 ? 5.155  -15.051 7.942   0.40 35.77 ?  169 LEU   A HD11 1 
ATOM   3839 H HD12 A LEU   A 1 169 ? 5.581  -21.435 -0.821  0.60 32.66 ?  169 LEU   A HD12 1 
ATOM   3840 H HD12 B LEU   A 1 169 ? 3.715  -15.116 7.274   0.40 35.77 ?  169 LEU   A HD12 1 
ATOM   3841 H HD13 A LEU   A 1 169 ? 5.010  -20.688 -2.103  0.60 32.66 ?  169 LEU   A HD13 1 
ATOM   3842 H HD13 B LEU   A 1 169 ? 4.231  -16.325 8.168   0.40 35.77 ?  169 LEU   A HD13 1 
ATOM   3843 H HD21 A LEU   A 1 169 ? 7.054  -22.212 -3.862  0.60 32.51 ?  169 LEU   A HD21 1 
ATOM   3844 H HD21 B LEU   A 1 169 ? 6.629  -16.936 7.504   0.40 35.54 ?  169 LEU   A HD21 1 
ATOM   3845 H HD22 A LEU   A 1 169 ? 6.643  -20.714 -4.199  0.60 32.51 ?  169 LEU   A HD22 1 
ATOM   3846 H HD22 B LEU   A 1 169 ? 5.775  -18.132 6.901   0.40 35.54 ?  169 LEU   A HD22 1 
ATOM   3847 H HD23 A LEU   A 1 169 ? 8.164  -21.077 -3.919  0.60 32.51 ?  169 LEU   A HD23 1 
ATOM   3848 H HD23 B LEU   A 1 169 ? 6.813  -17.355 5.983   0.40 35.54 ?  169 LEU   A HD23 1 
ATOM   3849 N N    A SER   B 1 1   ? 50.769 -9.237  -23.737 0.60 28.84 ?  1   SER   B N    1 
ATOM   3850 N N    B SER   B 1 1   ? 50.672 -9.197  -23.780 0.40 26.90 ?  1   SER   B N    1 
ATOM   3851 C CA   A SER   B 1 1   ? 51.281 -10.301 -22.853 0.60 28.63 ?  1   SER   B CA   1 
ATOM   3852 C CA   B SER   B 1 1   ? 51.174 -10.228 -22.848 0.40 26.62 ?  1   SER   B CA   1 
ATOM   3853 C C    A SER   B 1 1   ? 50.207 -11.343 -22.590 0.60 27.54 ?  1   SER   B C    1 
ATOM   3854 C C    B SER   B 1 1   ? 50.098 -11.272 -22.580 0.40 25.65 ?  1   SER   B C    1 
ATOM   3855 O O    A SER   B 1 1   ? 49.011 -11.119 -22.819 0.60 27.45 ?  1   SER   B O    1 
ATOM   3856 O O    B SER   B 1 1   ? 48.926 -11.098 -22.934 0.40 25.17 ?  1   SER   B O    1 
ATOM   3857 C CB   A SER   B 1 1   ? 51.764 -9.718  -21.529 0.60 29.51 ?  1   SER   B CB   1 
ATOM   3858 C CB   B SER   B 1 1   ? 51.613 -9.596  -21.531 0.40 27.37 ?  1   SER   B CB   1 
ATOM   3859 O OG   A SER   B 1 1   ? 50.668 -9.376  -20.703 0.60 30.95 ?  1   SER   B OG   1 
ATOM   3860 O OG   B SER   B 1 1   ? 50.506 -9.436  -20.663 0.40 28.42 ?  1   SER   B OG   1 
ATOM   3861 H H1   A SER   B 1 1   ? 50.617 -9.580  -24.541 0.60 34.63 ?  1   SER   B H1   1 
ATOM   3862 H H1   B SER   B 1 1   ? 51.365 -8.761  -24.127 0.40 32.31 ?  1   SER   B H1   1 
ATOM   3863 H H2   A SER   B 1 1   ? 50.018 -8.916  -23.395 0.60 34.63 ?  1   SER   B H2   1 
ATOM   3864 H H2   B SER   B 1 1   ? 50.211 -9.592  -24.426 0.40 32.31 ?  1   SER   B H2   1 
ATOM   3865 H H3   A SER   B 1 1   ? 51.379 -8.594  -23.793 0.60 34.63 ?  1   SER   B H3   1 
ATOM   3866 H H3   B SER   B 1 1   ? 50.153 -8.634  -23.334 0.40 32.31 ?  1   SER   B H3   1 
ATOM   3867 H HA   A SER   B 1 1   ? 52.030 -10.728 -23.291 0.60 34.38 ?  1   SER   B HA   1 
ATOM   3868 H HA   B SER   B 1 1   ? 51.939 -10.660 -23.253 0.40 31.97 ?  1   SER   B HA   1 
ATOM   3869 H HB2  A SER   B 1 1   ? 52.309 -10.382 -21.079 0.60 35.44 ?  1   SER   B HB2  1 
ATOM   3870 H HB2  B SER   B 1 1   ? 52.271 -10.174 -21.116 0.40 32.87 ?  1   SER   B HB2  1 
ATOM   3871 H HB3  A SER   B 1 1   ? 52.287 -8.921  -21.704 0.60 35.44 ?  1   SER   B HB3  1 
ATOM   3872 H HB3  B SER   B 1 1   ? 52.001 -8.725  -21.710 0.40 32.87 ?  1   SER   B HB3  1 
ATOM   3873 H HG   A SER   B 1 1   ? 50.905 -8.795  -20.145 0.60 37.16 ?  1   SER   B HG   1 
ATOM   3874 H HG   B SER   B 1 1   ? 50.644 -8.787  -20.148 0.40 34.13 ?  1   SER   B HG   1 
ATOM   3875 N N    A MET   B 1 2   ? 50.654 -12.485 -22.087 0.60 26.82 ?  2   MET   B N    1 
ATOM   3876 N N    B MET   B 1 2   ? 50.512 -12.355 -21.933 0.40 25.42 ?  2   MET   B N    1 
ATOM   3877 C CA   A MET   B 1 2   ? 49.819 -13.662 -21.910 0.60 26.59 ?  2   MET   B CA   1 
ATOM   3878 C CA   B MET   B 1 2   ? 49.697 -13.555 -21.778 0.40 25.53 ?  2   MET   B CA   1 
ATOM   3879 C C    A MET   B 1 2   ? 49.590 -13.862 -20.420 0.60 23.87 ?  2   MET   B C    1 
ATOM   3880 C C    B MET   B 1 2   ? 49.459 -13.803 -20.294 0.40 23.89 ?  2   MET   B C    1 
ATOM   3881 O O    A MET   B 1 2   ? 50.542 -14.095 -19.669 0.60 23.64 ?  2   MET   B O    1 
ATOM   3882 O O    B MET   B 1 2   ? 50.359 -14.260 -19.582 0.40 24.26 ?  2   MET   B O    1 
ATOM   3883 C CB   A MET   B 1 2   ? 50.518 -14.873 -22.519 0.60 30.09 ?  2   MET   B CB   1 
ATOM   3884 C CB   B MET   B 1 2   ? 50.422 -14.726 -22.416 0.40 27.91 ?  2   MET   B CB   1 
ATOM   3885 C CG   A MET   B 1 2   ? 49.662 -16.120 -22.629 0.60 33.30 ?  2   MET   B CG   1 
ATOM   3886 C CG   B MET   B 1 2   ? 49.548 -15.914 -22.776 0.40 30.02 ?  2   MET   B CG   1 
ATOM   3887 S SD   A MET   B 1 2   ? 50.493 -17.397 -23.590 0.60 36.29 ?  2   MET   B SD   1 
ATOM   3888 S SD   B MET   B 1 2   ? 50.453 -17.081 -23.803 0.40 31.94 ?  2   MET   B SD   1 
ATOM   3889 C CE   A MET   B 1 2   ? 51.008 -16.424 -25.003 0.60 36.38 ?  2   MET   B CE   1 
ATOM   3890 C CE   B MET   B 1 2   ? 51.430 -15.956 -24.785 0.40 31.91 ?  2   MET   B CE   1 
ATOM   3891 H H    A MET   B 1 2   ? 51.467 -12.609 -21.827 0.60 32.21 ?  2   MET   B H    1 
ATOM   3892 H H    B MET   B 1 2   ? 51.294 -12.426 -21.579 0.40 30.54 ?  2   MET   B H    1 
ATOM   3893 H HA   A MET   B 1 2   ? 48.972 -13.545 -22.362 0.60 31.94 ?  2   MET   B HA   1 
ATOM   3894 H HA   B MET   B 1 2   ? 48.853 -13.440 -22.243 0.40 30.66 ?  2   MET   B HA   1 
ATOM   3895 H HB2  A MET   B 1 2   ? 50.804 -14.610 -23.406 0.60 36.14 ?  2   MET   B HB2  1 
ATOM   3896 H HB2  B MET   B 1 2   ? 50.818 -14.359 -23.215 0.40 33.52 ?  2   MET   B HB2  1 
ATOM   3897 H HB3  A MET   B 1 2   ? 51.292 -15.105 -21.986 0.60 36.14 ?  2   MET   B HB3  1 
ATOM   3898 H HB3  B MET   B 1 2   ? 51.119 -15.055 -21.827 0.40 33.52 ?  2   MET   B HB3  1 
ATOM   3899 H HG2  A MET   B 1 2   ? 49.491 -16.469 -21.739 0.60 39.99 ?  2   MET   B HG2  1 
ATOM   3900 H HG2  B MET   B 1 2   ? 49.268 -16.371 -21.963 0.40 36.05 ?  2   MET   B HG2  1 
ATOM   3901 H HG3  A MET   B 1 2   ? 48.827 -15.905 -23.073 0.60 39.99 ?  2   MET   B HG3  1 
ATOM   3902 H HG3  B MET   B 1 2   ? 48.774 -15.621 -23.276 0.40 36.05 ?  2   MET   B HG3  1 
ATOM   3903 H HE1  A MET   B 1 2   ? 51.160 -17.013 -25.747 0.60 43.68 ?  2   MET   B HE1  1 
ATOM   3904 H HE1  B MET   B 1 2   ? 51.775 -16.440 -25.528 0.40 38.32 ?  2   MET   B HE1  1 
ATOM   3905 H HE2  A MET   B 1 2   ? 50.302 -15.788 -25.216 0.60 43.68 ?  2   MET   B HE2  1 
ATOM   3906 H HE2  B MET   B 1 2   ? 50.858 -15.231 -25.093 0.40 38.32 ?  2   MET   B HE2  1 
ATOM   3907 H HE3  A MET   B 1 2   ? 51.825 -15.941 -24.783 0.60 43.68 ?  2   MET   B HE3  1 
ATOM   3908 H HE3  B MET   B 1 2   ? 52.161 -15.604 -24.243 0.40 38.32 ?  2   MET   B HE3  1 
ATOM   3909 N N    A VAL   B 1 3   ? 48.335 -13.732 -19.994 0.60 21.66 ?  3   VAL   B N    1 
ATOM   3910 N N    B VAL   B 1 3   ? 48.251 -13.501 -19.832 0.40 22.00 ?  3   VAL   B N    1 
ATOM   3911 C CA   A VAL   B 1 3   ? 47.933 -13.970 -18.615 0.60 20.44 ?  3   VAL   B CA   1 
ATOM   3912 C CA   B VAL   B 1 3   ? 47.842 -13.797 -18.466 0.40 20.68 ?  3   VAL   B CA   1 
ATOM   3913 C C    A VAL   B 1 3   ? 46.695 -14.857 -18.628 0.60 18.99 ?  3   VAL   B C    1 
ATOM   3914 C C    B VAL   B 1 3   ? 46.586 -14.655 -18.504 0.40 19.25 ?  3   VAL   B C    1 
ATOM   3915 O O    A VAL   B 1 3   ? 45.983 -14.958 -19.629 0.60 19.02 ?  3   VAL   B O    1 
ATOM   3916 O O    B VAL   B 1 3   ? 45.756 -14.540 -19.411 0.40 19.13 ?  3   VAL   B O    1 
ATOM   3917 C CB   A VAL   B 1 3   ? 47.663 -12.657 -17.842 0.60 21.60 ?  3   VAL   B CB   1 
ATOM   3918 C CB   B VAL   B 1 3   ? 47.611 -12.525 -17.620 0.40 21.05 ?  3   VAL   B CB   1 
ATOM   3919 C CG1  A VAL   B 1 3   ? 48.935 -11.808 -17.752 0.60 22.07 ?  3   VAL   B CG1  1 
ATOM   3920 C CG1  B VAL   B 1 3   ? 48.898 -11.716 -17.500 0.40 21.21 ?  3   VAL   B CG1  1 
ATOM   3921 C CG2  A VAL   B 1 3   ? 46.537 -11.871 -18.497 0.60 22.26 ?  3   VAL   B CG2  1 
ATOM   3922 C CG2  B VAL   B 1 3   ? 46.492 -11.684 -18.212 0.40 21.19 ?  3   VAL   B CG2  1 
ATOM   3923 H H    A VAL   B 1 3   ? 47.683 -13.495 -20.502 0.60 26.02 ?  3   VAL   B H    1 
ATOM   3924 H H    B VAL   B 1 3   ? 47.646 -13.113 -20.307 0.40 26.42 ?  3   VAL   B H    1 
ATOM   3925 H HA   A VAL   B 1 3   ? 48.641 -14.446 -18.154 0.60 24.56 ?  3   VAL   B HA   1 
ATOM   3926 H HA   B VAL   B 1 3   ? 48.544 -14.312 -18.043 0.40 24.85 ?  3   VAL   B HA   1 
ATOM   3927 H HB   A VAL   B 1 3   ? 47.391 -12.874 -16.936 0.60 25.95 ?  3   VAL   B HB   1 
ATOM   3928 H HB   B VAL   B 1 3   ? 47.344 -12.793 -16.728 0.40 25.29 ?  3   VAL   B HB   1 
ATOM   3929 H HG11 A VAL   B 1 3   ? 48.739 -10.998 -17.254 0.60 26.51 ?  3   VAL   B HG11 1 
ATOM   3930 H HG11 B VAL   B 1 3   ? 48.727 -10.934 -16.953 0.40 25.48 ?  3   VAL   B HG11 1 
ATOM   3931 H HG12 A VAL   B 1 3   ? 49.623 -12.317 -17.296 0.60 26.51 ?  3   VAL   B HG12 1 
ATOM   3932 H HG12 B VAL   B 1 3   ? 49.580 -12.267 -17.088 0.40 25.48 ?  3   VAL   B HG12 1 
ATOM   3933 H HG13 A VAL   B 1 3   ? 49.228 -11.582 -18.648 0.60 26.51 ?  3   VAL   B HG13 1 
ATOM   3934 H HG13 B VAL   B 1 3   ? 49.182 -11.444 -18.387 0.40 25.48 ?  3   VAL   B HG13 1 
ATOM   3935 H HG21 A VAL   B 1 3   ? 46.484 -10.995 -18.086 0.60 26.74 ?  3   VAL   B HG21 1 
ATOM   3936 H HG21 B VAL   B 1 3   ? 46.454 -10.838 -17.743 0.40 25.45 ?  3   VAL   B HG21 1 
ATOM   3937 H HG22 A VAL   B 1 3   ? 46.723 -11.784 -19.444 0.60 26.74 ?  3   VAL   B HG22 1 
ATOM   3938 H HG22 B VAL   B 1 3   ? 46.673 -11.535 -19.153 0.40 25.45 ?  3   VAL   B HG22 1 
ATOM   3939 H HG23 A VAL   B 1 3   ? 45.703 -12.349 -18.366 0.60 26.74 ?  3   VAL   B HG23 1 
ATOM   3940 H HG23 B VAL   B 1 3   ? 45.651 -12.158 -18.108 0.40 25.45 ?  3   VAL   B HG23 1 
ATOM   3941 N N    . ASN   B 1 4   ? 46.448 -15.515 -17.496 1.00 18.08 ?  4   ASN   B N    1 
ATOM   3942 C CA   . ASN   B 1 4   ? 45.303 -16.419 -17.375 1.00 17.51 ?  4   ASN   B CA   1 
ATOM   3943 C C    . ASN   B 1 4   ? 45.240 -17.394 -18.549 1.00 18.17 ?  4   ASN   B C    1 
ATOM   3944 O O    . ASN   B 1 4   ? 44.176 -17.655 -19.107 1.00 18.74 ?  4   ASN   B O    1 
ATOM   3945 C CB   . ASN   B 1 4   ? 43.983 -15.655 -17.219 1.00 17.14 ?  4   ASN   B CB   1 
ATOM   3946 C CG   . ASN   B 1 4   ? 43.933 -14.846 -15.939 1.00 16.39 ?  4   ASN   B CG   1 
ATOM   3947 O OD1  . ASN   B 1 4   ? 44.220 -15.354 -14.859 1.00 15.87 ?  4   ASN   B OD1  1 
ATOM   3948 N ND2  . ASN   B 1 4   ? 43.591 -13.569 -16.059 1.00 17.36 ?  4   ASN   B ND2  1 
ATOM   3949 H H    A ASN   B 1 4   ? 46.934 -15.461 -16.792 0.60 21.73 ?  4   ASN   B H    1 
ATOM   3950 H H    B ASN   B 1 4   ? 47.016 -15.588 -16.858 0.40 21.73 ?  4   ASN   B H    1 
ATOM   3951 H HA   . ASN   B 1 4   ? 45.426 -16.942 -16.571 1.00 21.03 ?  4   ASN   B HA   1 
ATOM   3952 H HB2  . ASN   B 1 4   ? 43.876 -15.043 -17.964 1.00 20.59 ?  4   ASN   B HB2  1 
ATOM   3953 H HB3  . ASN   B 1 4   ? 43.252 -16.289 -17.200 1.00 20.59 ?  4   ASN   B HB3  1 
ATOM   3954 H HD21 . ASN   B 1 4   ? 43.554 -13.063 -15.359 1.00 20.86 ?  4   ASN   B HD21 1 
ATOM   3955 H HD22 . ASN   B 1 4   ? 43.405 -13.238 -16.830 1.00 20.86 ?  4   ASN   B HD22 1 
ATOM   3956 N N    . SER   B 1 5   ? 46.398 -17.934 -18.935 1.00 19.54 ?  5   SER   B N    1 
ATOM   3957 C CA   . SER   B 1 5   ? 46.484 -18.859 -20.063 1.00 21.93 ?  5   SER   B CA   1 
ATOM   3958 C C    . SER   B 1 5   ? 46.490 -20.277 -19.505 1.00 23.14 ?  5   SER   B C    1 
ATOM   3959 O O    . SER   B 1 5   ? 47.526 -20.929 -19.391 1.00 24.36 ?  5   SER   B O    1 
ATOM   3960 C CB   . SER   B 1 5   ? 47.721 -18.567 -20.908 1.00 23.79 ?  5   SER   B CB   1 
ATOM   3961 O OG   . SER   B 1 5   ? 48.910 -18.725 -20.153 1.00 26.36 ?  5   SER   B OG   1 
ATOM   3962 H H    . SER   B 1 5   ? 47.154 -17.779 -18.555 1.00 23.47 ?  5   SER   B H    1 
ATOM   3963 H HA   . SER   B 1 5   ? 45.700 -18.759 -20.623 1.00 26.35 ?  5   SER   B HA   1 
ATOM   3964 H HB2  . SER   B 1 5   ? 47.737 -19.180 -21.662 1.00 28.57 ?  5   SER   B HB2  1 
ATOM   3965 H HB3  . SER   B 1 5   ? 47.662 -17.654 -21.229 1.00 28.57 ?  5   SER   B HB3  1 
ATOM   3966 H HG   . SER   B 1 5   ? 48.976 -19.520 -19.891 1.00 31.66 ?  5   SER   B HG   1 
ATOM   3967 N N    . PHE   B 1 6   ? 45.299 -20.750 -19.143 1.00 23.55 ?  6   PHE   B N    1 
ATOM   3968 C CA   . PHE   B 1 6   ? 45.135 -22.089 -18.594 1.00 22.95 ?  6   PHE   B CA   1 
ATOM   3969 C C    . PHE   B 1 6   ? 45.079 -23.094 -19.735 1.00 26.41 ?  6   PHE   B C    1 
ATOM   3970 O O    . PHE   B 1 6   ? 44.383 -22.873 -20.729 1.00 28.21 ?  6   PHE   B O    1 
ATOM   3971 C CB   . PHE   B 1 6   ? 43.851 -22.161 -17.769 1.00 20.33 ?  6   PHE   B CB   1 
ATOM   3972 C CG   . PHE   B 1 6   ? 43.858 -21.282 -16.551 1.00 18.38 ?  6   PHE   B CG   1 
ATOM   3973 C CD1  . PHE   B 1 6   ? 44.355 -21.751 -15.351 1.00 17.40 ?  6   PHE   B CD1  1 
ATOM   3974 C CD2  . PHE   B 1 6   ? 43.373 -19.984 -16.609 1.00 17.48 ?  6   PHE   B CD2  1 
ATOM   3975 C CE1  . PHE   B 1 6   ? 44.356 -20.947 -14.221 1.00 16.91 ?  6   PHE   B CE1  1 
ATOM   3976 C CE2  . PHE   B 1 6   ? 43.379 -19.172 -15.488 1.00 18.03 ?  6   PHE   B CE2  1 
ATOM   3977 C CZ   . PHE   B 1 6   ? 43.874 -19.647 -14.297 1.00 17.27 ?  6   PHE   B CZ   1 
ATOM   3978 H H    . PHE   B 1 6   ? 44.565 -20.313 -19.214 1.00 28.29 ?  6   PHE   B H    1 
ATOM   3979 H HA   . PHE   B 1 6   ? 45.885 -22.311 -18.023 1.00 27.57 ?  6   PHE   B HA   1 
ATOM   3980 H HB2  . PHE   B 1 6   ? 43.103 -21.889 -18.325 1.00 24.43 ?  6   PHE   B HB2  1 
ATOM   3981 H HB3  . PHE   B 1 6   ? 43.717 -23.077 -17.471 1.00 24.43 ?  6   PHE   B HB3  1 
ATOM   3982 H HD1  . PHE   B 1 6   ? 44.687 -22.618 -15.295 1.00 20.91 ?  6   PHE   B HD1  1 
ATOM   3983 H HD2  . PHE   B 1 6   ? 43.032 -19.660 -17.409 1.00 21.00 ?  6   PHE   B HD2  1 
ATOM   3984 H HE1  . PHE   B 1 6   ? 44.701 -21.267 -13.417 1.00 20.32 ?  6   PHE   B HE1  1 
ATOM   3985 H HE2  . PHE   B 1 6   ? 43.043 -18.307 -15.540 1.00 21.66 ?  6   PHE   B HE2  1 
ATOM   3986 H HZ   . PHE   B 1 6   ? 43.877 -19.107 -13.540 1.00 20.75 ?  6   PHE   B HZ   1 
ATOM   3987 N N    A SER   B 1 7   ? 45.811 -24.198 -19.594 0.60 26.70 ?  7   SER   B N    1 
ATOM   3988 N N    B SER   B 1 7   ? 45.823 -24.191 -19.593 0.40 27.11 ?  7   SER   B N    1 
ATOM   3989 C CA   A SER   B 1 7   ? 45.884 -25.205 -20.642 0.60 28.14 ?  7   SER   B CA   1 
ATOM   3990 C CA   B SER   B 1 7   ? 45.934 -25.198 -20.637 0.40 28.40 ?  7   SER   B CA   1 
ATOM   3991 C C    A SER   B 1 7   ? 45.832 -26.599 -20.034 0.60 27.42 ?  7   SER   B C    1 
ATOM   3992 C C    B SER   B 1 7   ? 45.883 -26.586 -20.018 0.40 27.91 ?  7   SER   B C    1 
ATOM   3993 O O    A SER   B 1 7   ? 46.413 -26.849 -18.974 0.60 27.79 ?  7   SER   B O    1 
ATOM   3994 O O    B SER   B 1 7   ? 46.470 -26.827 -18.960 0.40 28.20 ?  7   SER   B O    1 
ATOM   3995 C CB   A SER   B 1 7   ? 47.166 -25.041 -21.470 0.60 30.16 ?  7   SER   B CB   1 
ATOM   3996 C CB   B SER   B 1 7   ? 47.247 -25.032 -21.414 0.40 30.03 ?  7   SER   B CB   1 
ATOM   3997 O OG   A SER   B 1 7   ? 47.126 -25.846 -22.636 0.60 31.81 ?  7   SER   B OG   1 
ATOM   3998 O OG   B SER   B 1 7   ? 47.316 -25.937 -22.502 0.40 31.22 ?  7   SER   B OG   1 
ATOM   3999 H H    A SER   B 1 7   ? 46.282 -24.382 -18.897 0.60 32.06 ?  7   SER   B H    1 
ATOM   4000 H H    B SER   B 1 7   ? 46.284 -24.371 -18.889 0.40 32.56 ?  7   SER   B H    1 
ATOM   4001 H HA   A SER   B 1 7   ? 45.126 -25.108 -21.236 0.60 33.79 ?  7   SER   B HA   1 
ATOM   4002 H HA   B SER   B 1 7   ? 45.195 -25.112 -21.258 0.40 34.11 ?  7   SER   B HA   1 
ATOM   4003 H HB2  A SER   B 1 7   ? 47.253 -24.111 -21.734 0.60 36.22 ?  7   SER   B HB2  1 
ATOM   4004 H HB2  B SER   B 1 7   ? 47.299 -24.123 -21.751 0.40 36.06 ?  7   SER   B HB2  1 
ATOM   4005 H HB3  A SER   B 1 7   ? 47.927 -25.303 -20.929 0.60 36.22 ?  7   SER   B HB3  1 
ATOM   4006 H HB3  B SER   B 1 7   ? 47.991 -25.205 -20.817 0.40 36.06 ?  7   SER   B HB3  1 
ATOM   4007 H HG   A SER   B 1 7   ? 47.835 -25.748 -23.077 0.60 38.20 ?  7   SER   B HG   1 
ATOM   4008 H HG   B SER   B 1 7   ? 48.036 -25.828 -22.921 0.40 37.49 ?  7   SER   B HG   1 
ATOM   4009 N N    A GLY   B 1 8   ? 45.131 -27.504 -20.714 0.60 26.98 ?  8   GLY   B N    1 
ATOM   4010 N N    B GLY   B 1 8   ? 45.177 -27.496 -20.687 0.40 27.39 ?  8   GLY   B N    1 
ATOM   4011 C CA   A GLY   B 1 8   ? 45.095 -28.892 -20.306 0.60 26.35 ?  8   GLY   B CA   1 
ATOM   4012 C CA   B GLY   B 1 8   ? 45.133 -28.878 -20.259 0.40 26.63 ?  8   GLY   B CA   1 
ATOM   4013 C C    A GLY   B 1 8   ? 44.125 -29.213 -19.197 0.60 25.40 ?  8   GLY   B C    1 
ATOM   4014 C C    B GLY   B 1 8   ? 44.170 -29.175 -19.137 0.40 25.65 ?  8   GLY   B C    1 
ATOM   4015 O O    A GLY   B 1 8   ? 44.249 -30.273 -18.573 0.60 26.07 ?  8   GLY   B O    1 
ATOM   4016 O O    B GLY   B 1 8   ? 44.347 -30.181 -18.440 0.40 26.18 ?  8   GLY   B O    1 
ATOM   4017 H H    A GLY   B 1 8   ? 44.668 -27.330 -21.416 0.60 32.41 ?  8   GLY   B H    1 
ATOM   4018 H H    B GLY   B 1 8   ? 44.717 -27.332 -21.393 0.40 32.89 ?  8   GLY   B H    1 
ATOM   4019 H HA2  A GLY   B 1 8   ? 44.862 -29.437 -21.074 0.60 31.65 ?  8   GLY   B HA2  1 
ATOM   4020 H HA2  B GLY   B 1 8   ? 44.891 -29.433 -21.017 0.40 31.98 ?  8   GLY   B HA2  1 
ATOM   4021 H HA3  A GLY   B 1 8   ? 45.976 -29.156 -20.006 0.60 31.65 ?  8   GLY   B HA3  1 
ATOM   4022 H HA3  B GLY   B 1 8   ? 46.013 -29.145 -19.959 0.40 31.98 ?  8   GLY   B HA3  1 
ATOM   4023 N N    . TYR   B 1 9   ? 43.148 -28.347 -18.940 1.00 24.56 ?  9   TYR   B N    1 
ATOM   4024 C CA   . TYR   B 1 9   ? 42.172 -28.590 -17.890 1.00 22.23 ?  9   TYR   B CA   1 
ATOM   4025 C C    . TYR   B 1 9   ? 40.988 -29.382 -18.415 1.00 22.13 ?  9   TYR   B C    1 
ATOM   4026 O O    . TYR   B 1 9   ? 40.585 -29.251 -19.574 1.00 23.56 ?  9   TYR   B O    1 
ATOM   4027 C CB   . TYR   B 1 9   ? 41.667 -27.291 -17.270 1.00 21.18 ?  9   TYR   B CB   1 
ATOM   4028 C CG   . TYR   B 1 9   ? 42.683 -26.671 -16.346 1.00 20.29 ?  9   TYR   B CG   1 
ATOM   4029 C CD1  . TYR   B 1 9   ? 43.795 -26.015 -16.857 1.00 20.60 ?  9   TYR   B CD1  1 
ATOM   4030 C CD2  . TYR   B 1 9   ? 42.549 -26.755 -14.970 1.00 19.53 ?  9   TYR   B CD2  1 
ATOM   4031 C CE1  . TYR   B 1 9   ? 44.745 -25.454 -16.025 1.00 20.75 ?  9   TYR   B CE1  1 
ATOM   4032 C CE2  . TYR   B 1 9   ? 43.495 -26.195 -14.124 1.00 19.75 ?  9   TYR   B CE2  1 
ATOM   4033 C CZ   . TYR   B 1 9   ? 44.592 -25.541 -14.662 1.00 20.40 ?  9   TYR   B CZ   1 
ATOM   4034 O OH   . TYR   B 1 9   ? 45.544 -24.987 -13.842 1.00 21.00 ?  9   TYR   B OH   1 
ATOM   4035 H H    A TYR   B 1 9   ? 43.016 -27.617 -19.374 0.60 29.50 ?  9   TYR   B H    1 
ATOM   4036 H H    B TYR   B 1 9   ? 42.987 -27.644 -19.410 0.40 29.50 ?  9   TYR   B H    1 
ATOM   4037 H HA   . TYR   B 1 9   ? 42.578 -29.112 -17.188 1.00 26.71 ?  9   TYR   B HA   1 
ATOM   4038 H HB2  . TYR   B 1 9   ? 41.463 -26.651 -17.972 1.00 25.44 ?  9   TYR   B HB2  1 
ATOM   4039 H HB3  . TYR   B 1 9   ? 40.874 -27.483 -16.751 1.00 25.44 ?  9   TYR   B HB3  1 
ATOM   4040 H HD1  . TYR   B 1 9   ? 43.902 -25.955 -17.780 1.00 24.75 ?  9   TYR   B HD1  1 
ATOM   4041 H HD2  . TYR   B 1 9   ? 41.810 -27.195 -14.608 1.00 23.46 ?  9   TYR   B HD2  1 
ATOM   4042 H HE1  . TYR   B 1 9   ? 45.479 -25.022 -16.385 1.00 24.93 ?  9   TYR   B HE1  1 
ATOM   4043 H HE2  . TYR   B 1 9   ? 43.388 -26.260 -13.201 1.00 23.73 ?  9   TYR   B HE2  1 
ATOM   4044 H HH   . TYR   B 1 9   ? 46.145 -24.632 -14.304 1.00 25.23 ?  9   TYR   B HH   1 
ATOM   4045 N N    . LEU   B 1 10  ? 40.440 -30.215 -17.539 1.00 20.42 ?  10  LEU   B N    1 
ATOM   4046 C CA   . LEU   B 1 10  ? 39.239 -30.981 -17.816 1.00 20.25 ?  10  LEU   B CA   1 
ATOM   4047 C C    . LEU   B 1 10  ? 38.048 -30.217 -17.258 1.00 19.61 ?  10  LEU   B C    1 
ATOM   4048 O O    . LEU   B 1 10  ? 38.059 -29.803 -16.096 1.00 19.34 ?  10  LEU   B O    1 
ATOM   4049 C CB   . LEU   B 1 10  ? 39.343 -32.353 -17.149 1.00 21.06 ?  10  LEU   B CB   1 
ATOM   4050 C CG   . LEU   B 1 10  ? 38.203 -33.316 -17.450 1.00 22.46 ?  10  LEU   B CG   1 
ATOM   4051 C CD1  . LEU   B 1 10  ? 38.299 -33.814 -18.883 1.00 23.63 ?  10  LEU   B CD1  1 
ATOM   4052 C CD2  . LEU   B 1 10  ? 38.213 -34.471 -16.465 1.00 23.26 ?  10  LEU   B CD2  1 
ATOM   4053 H H    . LEU   B 1 10  ? 40.750 -30.354 -16.741 1.00 24.53 ?  10  LEU   B H    1 
ATOM   4054 H HA   . LEU   B 1 10  ? 39.122 -31.098 -18.770 1.00 24.33 ?  10  LEU   B HA   1 
ATOM   4055 H HB2  . LEU   B 1 10  ? 40.166 -32.774 -17.445 1.00 25.30 ?  10  LEU   B HB2  1 
ATOM   4056 H HB3  . LEU   B 1 10  ? 39.373 -32.228 -16.187 1.00 25.30 ?  10  LEU   B HB3  1 
ATOM   4057 H HG   . LEU   B 1 10  ? 37.359 -32.849 -17.352 1.00 26.98 ?  10  LEU   B HG   1 
ATOM   4058 H HD11 . LEU   B 1 10  ? 37.596 -34.464 -19.036 1.00 28.38 ?  10  LEU   B HD11 1 
ATOM   4059 H HD12 . LEU   B 1 10  ? 38.191 -33.062 -19.486 1.00 28.38 ?  10  LEU   B HD12 1 
ATOM   4060 H HD13 . LEU   B 1 10  ? 39.166 -34.225 -19.016 1.00 28.38 ?  10  LEU   B HD13 1 
ATOM   4061 H HD21 . LEU   B 1 10  ? 37.486 -35.071 -16.682 1.00 27.94 ?  10  LEU   B HD21 1 
ATOM   4062 H HD22 . LEU   B 1 10  ? 39.062 -34.931 -16.534 1.00 27.94 ?  10  LEU   B HD22 1 
ATOM   4063 H HD23 . LEU   B 1 10  ? 38.098 -34.115 -15.570 1.00 27.94 ?  10  LEU   B HD23 1 
ATOM   4064 N N    . LYS   B 1 11  ? 37.023 -30.043 -18.083 1.00 20.96 ?  11  LYS   B N    1 
ATOM   4065 C CA   . LYS   B 1 11  ? 35.826 -29.327 -17.671 1.00 23.01 ?  11  LYS   B CA   1 
ATOM   4066 C C    . LYS   B 1 11  ? 34.953 -30.250 -16.827 1.00 21.92 ?  11  LYS   B C    1 
ATOM   4067 O O    . LYS   B 1 11  ? 34.591 -31.347 -17.272 1.00 23.56 ?  11  LYS   B O    1 
ATOM   4068 C CB   . LYS   B 1 11  ? 35.072 -28.866 -18.918 1.00 27.12 ?  11  LYS   B CB   1 
ATOM   4069 C CG   . LYS   B 1 11  ? 33.915 -27.919 -18.664 1.00 30.76 ?  11  LYS   B CG   1 
ATOM   4070 C CD   . LYS   B 1 11  ? 33.169 -27.629 -19.961 1.00 33.46 ?  11  LYS   B CD   1 
ATOM   4071 C CE   . LYS   B 1 11  ? 32.186 -26.481 -19.804 1.00 35.40 ?  11  LYS   B CE   1 
ATOM   4072 N NZ   . LYS   B 1 11  ? 32.878 -25.172 -19.660 1.00 36.53 ?  11  LYS   B NZ   1 
ATOM   4073 H H    . LYS   B 1 11  ? 36.990 -30.339 -18.892 1.00 25.18 ?  11  LYS   B H    1 
ATOM   4074 H HA   . LYS   B 1 11  ? 36.069 -28.551 -17.145 1.00 27.63 ?  11  LYS   B HA   1 
ATOM   4075 H HB2  . LYS   B 1 11  ? 35.698 -28.408 -19.503 1.00 32.58 ?  11  LYS   B HB2  1 
ATOM   4076 H HB3  . LYS   B 1 11  ? 34.717 -29.645 -19.372 1.00 32.58 ?  11  LYS   B HB3  1 
ATOM   4077 H HG2  . LYS   B 1 11  ? 33.294 -28.326 -18.040 1.00 36.94 ?  11  LYS   B HG2  1 
ATOM   4078 H HG3  . LYS   B 1 11  ? 34.252 -27.082 -18.311 1.00 36.94 ?  11  LYS   B HG3  1 
ATOM   4079 H HD2  . LYS   B 1 11  ? 33.810 -27.389 -20.649 1.00 40.17 ?  11  LYS   B HD2  1 
ATOM   4080 H HD3  . LYS   B 1 11  ? 32.674 -28.420 -20.227 1.00 40.17 ?  11  LYS   B HD3  1 
ATOM   4081 H HE2  . LYS   B 1 11  ? 31.618 -26.439 -20.589 1.00 42.51 ?  11  LYS   B HE2  1 
ATOM   4082 H HE3  . LYS   B 1 11  ? 31.650 -26.633 -19.011 1.00 42.51 ?  11  LYS   B HE3  1 
ATOM   4083 H HZ1  . LYS   B 1 11  ? 32.279 -24.519 -19.580 1.00 43.87 ?  11  LYS   B HZ1  1 
ATOM   4084 H HZ2  . LYS   B 1 11  ? 33.397 -25.180 -18.938 1.00 43.87 ?  11  LYS   B HZ2  1 
ATOM   4085 H HZ3  . LYS   B 1 11  ? 33.382 -25.015 -20.377 1.00 43.87 ?  11  LYS   B HZ3  1 
ATOM   4086 N N    . LEU   B 1 12  ? 34.612 -29.812 -15.613 1.00 20.34 ?  12  LEU   B N    1 
ATOM   4087 C CA   . LEU   B 1 12  ? 33.654 -30.517 -14.766 1.00 19.53 ?  12  LEU   B CA   1 
ATOM   4088 C C    . LEU   B 1 12  ? 32.262 -29.912 -14.856 1.00 19.55 ?  12  LEU   B C    1 
ATOM   4089 O O    . LEU   B 1 12  ? 31.278 -30.635 -15.027 1.00 19.79 ?  12  LEU   B O    1 
ATOM   4090 C CB   . LEU   B 1 12  ? 34.110 -30.535 -13.301 1.00 18.75 ?  12  LEU   B CB   1 
ATOM   4091 C CG   . LEU   B 1 12  ? 35.451 -31.211 -13.009 1.00 18.70 ?  12  LEU   B CG   1 
ATOM   4092 C CD1  . LEU   B 1 12  ? 35.781 -31.169 -11.530 1.00 19.12 ?  12  LEU   B CD1  1 
ATOM   4093 C CD2  . LEU   B 1 12  ? 35.462 -32.654 -13.509 1.00 19.25 ?  12  LEU   B CD2  1 
ATOM   4094 H H    . LEU   B 1 12  ? 34.921 -29.092 -15.254 1.00 24.44 ?  12  LEU   B H    1 
ATOM   4095 H HA   . LEU   B 1 12  ? 33.581 -31.432 -15.071 1.00 23.46 ?  12  LEU   B HA   1 
ATOM   4096 H HB2  . LEU   B 1 12  ? 34.173 -29.622 -12.993 1.00 22.53 ?  12  LEU   B HB2  1 
ATOM   4097 H HB3  . LEU   B 1 12  ? 33.431 -31.002 -12.784 1.00 22.53 ?  12  LEU   B HB3  1 
ATOM   4098 H HG   . LEU   B 1 12  ? 36.145 -30.735 -13.482 1.00 22.46 ?  12  LEU   B HG   1 
ATOM   4099 H HD11 . LEU   B 1 12  ? 36.638 -31.605 -11.385 1.00 22.97 ?  12  LEU   B HD11 1 
ATOM   4100 H HD12 . LEU   B 1 12  ? 35.828 -30.245 -11.243 1.00 22.97 ?  12  LEU   B HD12 1 
ATOM   4101 H HD13 . LEU   B 1 12  ? 35.089 -31.636 -11.034 1.00 22.97 ?  12  LEU   B HD13 1 
ATOM   4102 H HD21 . LEU   B 1 12  ? 36.275 -33.086 -13.207 1.00 23.13 ?  12  LEU   B HD21 1 
ATOM   4103 H HD22 . LEU   B 1 12  ? 34.688 -33.120 -13.151 1.00 23.13 ?  12  LEU   B HD22 1 
ATOM   4104 H HD23 . LEU   B 1 12  ? 35.426 -32.654 -14.478 1.00 23.13 ?  12  LEU   B HD23 1 
ATOM   4105 N N    . THR   B 1 13  ? 32.165 -28.596 -14.723 1.00 19.30 ?  13  THR   B N    1 
ATOM   4106 C CA   . THR   B 1 13  ? 30.939 -27.846 -14.941 1.00 19.14 ?  13  THR   B CA   1 
ATOM   4107 C C    . THR   B 1 13  ? 31.276 -26.652 -15.828 1.00 21.09 ?  13  THR   B C    1 
ATOM   4108 O O    . THR   B 1 13  ? 32.425 -26.457 -16.242 1.00 21.92 ?  13  THR   B O    1 
ATOM   4109 C CB   . THR   B 1 13  ? 30.334 -27.364 -13.617 1.00 18.57 ?  13  THR   B CB   1 
ATOM   4110 O OG1  . THR   B 1 13  ? 31.170 -26.339 -13.071 1.00 18.42 ?  13  THR   B OG1  1 
ATOM   4111 C CG2  . THR   B 1 13  ? 30.218 -28.512 -12.620 1.00 19.23 ?  13  THR   B CG2  1 
ATOM   4112 H H    . THR   B 1 13  ? 32.822 -28.091 -14.491 1.00 23.19 ?  13  THR   B H    1 
ATOM   4113 H HA   . THR   B 1 13  ? 30.287 -28.400 -15.391 1.00 23.00 ?  13  THR   B HA   1 
ATOM   4114 H HB   . THR   B 1 13  ? 29.442 -27.003 -13.775 1.00 22.31 ?  13  THR   B HB   1 
ATOM   4115 H HG1  . THR   B 1 13  ? 30.853 -25.573 -13.259 1.00 22.13 ?  13  THR   B HG1  1 
ATOM   4116 H HG21 . THR   B 1 13  ? 29.708 -28.231 -11.845 1.00 23.11 ?  13  THR   B HG21 1 
ATOM   4117 H HG22 . THR   B 1 13  ? 29.773 -29.265 -13.036 1.00 23.11 ?  13  THR   B HG22 1 
ATOM   4118 H HG23 . THR   B 1 13  ? 31.103 -28.788 -12.332 1.00 23.11 ?  13  THR   B HG23 1 
ATOM   4119 N N    A ASP   B 1 14  ? 30.261 -25.833 -16.103 0.60 21.89 ?  14  ASP   B N    1 
ATOM   4120 N N    B ASP   B 1 14  ? 30.266 -25.822 -16.101 0.40 21.79 ?  14  ASP   B N    1 
ATOM   4121 C CA   A ASP   B 1 14  ? 30.472 -24.668 -16.954 0.60 23.37 ?  14  ASP   B CA   1 
ATOM   4122 C CA   B ASP   B 1 14  ? 30.476 -24.665 -16.966 0.40 22.85 ?  14  ASP   B CA   1 
ATOM   4123 C C    A ASP   B 1 14  ? 31.580 -23.768 -16.421 0.60 21.64 ?  14  ASP   B C    1 
ATOM   4124 C C    B ASP   B 1 14  ? 31.483 -23.675 -16.400 0.40 21.28 ?  14  ASP   B C    1 
ATOM   4125 O O    A ASP   B 1 14  ? 32.263 -23.100 -17.207 0.60 22.82 ?  14  ASP   B O    1 
ATOM   4126 O O    B ASP   B 1 14  ? 31.968 -22.816 -17.145 0.40 21.92 ?  14  ASP   B O    1 
ATOM   4127 C CB   A ASP   B 1 14  ? 29.167 -23.885 -17.109 0.60 26.73 ?  14  ASP   B CB   1 
ATOM   4128 C CB   B ASP   B 1 14  ? 29.156 -23.937 -17.224 0.40 25.53 ?  14  ASP   B CB   1 
ATOM   4129 C CG   A ASP   B 1 14  ? 28.188 -24.557 -18.048 0.60 29.84 ?  14  ASP   B CG   1 
ATOM   4130 C CG   B ASP   B 1 14  ? 28.292 -24.648 -18.246 0.40 27.89 ?  14  ASP   B CG   1 
ATOM   4131 O OD1  A ASP   B 1 14  ? 28.560 -25.549 -18.717 0.60 31.01 ?  14  ASP   B OD1  1 
ATOM   4132 O OD1  B ASP   B 1 14  ? 28.859 -25.282 -19.162 0.40 28.85 ?  14  ASP   B OD1  1 
ATOM   4133 O OD2  A ASP   B 1 14  ? 27.032 -24.093 -18.110 0.60 31.07 -1 14  ASP   B OD2  1 
ATOM   4134 O OD2  B ASP   B 1 14  ? 27.050 -24.581 -18.136 0.40 28.70 -1 14  ASP   B OD2  1 
ATOM   4135 H H    A ASP   B 1 14  ? 29.463 -25.915 -15.799 0.60 26.29 ?  14  ASP   B H    1 
ATOM   4136 H H    B ASP   B 1 14  ? 29.467 -25.901 -15.798 0.40 26.18 ?  14  ASP   B H    1 
ATOM   4137 H HA   A ASP   B 1 14  ? 30.746 -24.961 -17.830 0.60 28.08 ?  14  ASP   B HA   1 
ATOM   4138 H HA   B ASP   B 1 14  ? 30.814 -24.973 -17.819 0.40 27.44 ?  14  ASP   B HA   1 
ATOM   4139 H HB2  A ASP   B 1 14  ? 28.732 -23.809 -16.246 0.60 32.10 ?  14  ASP   B HB2  1 
ATOM   4140 H HB2  B ASP   B 1 14  ? 28.662 -23.875 -16.391 0.40 30.66 ?  14  ASP   B HB2  1 
ATOM   4141 H HB3  A ASP   B 1 14  ? 29.360 -23.002 -17.463 0.60 32.10 ?  14  ASP   B HB3  1 
ATOM   4142 H HB3  B ASP   B 1 14  ? 29.350 -23.043 -17.558 0.40 30.66 ?  14  ASP   B HB3  1 
ATOM   4143 N N    . ASN   B 1 15  ? 31.788 -23.746 -15.102 1.00 19.56 ?  15  ASN   B N    1 
ATOM   4144 C CA   . ASN   B 1 15  ? 32.748 -22.826 -14.498 1.00 17.18 ?  15  ASN   B CA   1 
ATOM   4145 C C    . ASN   B 1 15  ? 33.840 -23.479 -13.660 1.00 16.12 ?  15  ASN   B C    1 
ATOM   4146 O O    . ASN   B 1 15  ? 34.685 -22.750 -13.133 1.00 15.84 ?  15  ASN   B O    1 
ATOM   4147 C CB   . ASN   B 1 15  ? 32.035 -21.768 -13.640 1.00 17.08 ?  15  ASN   B CB   1 
ATOM   4148 C CG   . ASN   B 1 15  ? 31.408 -22.361 -12.402 1.00 16.90 ?  15  ASN   B CG   1 
ATOM   4149 O OD1  . ASN   B 1 15  ? 30.478 -23.164 -12.496 1.00 18.26 ?  15  ASN   B OD1  1 
ATOM   4150 N ND2  . ASN   B 1 15  ? 31.917 -22.002 -11.236 1.00 15.70 ?  15  ASN   B ND2  1 
ATOM   4151 H H    A ASN   B 1 15  ? 31.390 -24.258 -14.538 0.60 23.50 ?  15  ASN   B H    1 
ATOM   4152 H H    B ASN   B 1 15  ? 31.430 -24.295 -14.547 0.40 23.50 ?  15  ASN   B H    1 
ATOM   4153 H HA   . ASN   B 1 15  ? 33.201 -22.345 -15.198 1.00 20.64 ?  15  ASN   B HA   1 
ATOM   4154 H HB2  . ASN   B 1 15  ? 32.682 -21.093 -13.360 1.00 20.52 ?  15  ASN   B HB2  1 
ATOM   4155 H HB3  . ASN   B 1 15  ? 31.335 -21.346 -14.165 1.00 20.52 ?  15  ASN   B HB3  1 
ATOM   4156 H HD21 . ASN   B 1 15  ? 31.587 -22.308 -10.500 1.00 18.87 ?  15  ASN   B HD21 1 
ATOM   4157 H HD22 . ASN   B 1 15  ? 32.579 -21.445 -11.200 1.00 18.87 ?  15  ASN   B HD22 1 
ATOM   4158 N N    . VAL   B 1 16  ? 33.857 -24.799 -13.510 1.00 15.82 ?  16  VAL   B N    1 
ATOM   4159 C CA   . VAL   B 1 16  ? 34.859 -25.487 -12.704 1.00 15.78 ?  16  VAL   B CA   1 
ATOM   4160 C C    . VAL   B 1 16  ? 35.648 -26.429 -13.600 1.00 15.88 ?  16  VAL   B C    1 
ATOM   4161 O O    . VAL   B 1 16  ? 35.068 -27.310 -14.253 1.00 17.06 ?  16  VAL   B O    1 
ATOM   4162 C CB   . VAL   B 1 16  ? 34.231 -26.245 -11.520 1.00 15.69 ?  16  VAL   B CB   1 
ATOM   4163 C CG1  . VAL   B 1 16  ? 35.310 -26.977 -10.721 1.00 15.49 ?  16  VAL   B CG1  1 
ATOM   4164 C CG2  . VAL   B 1 16  ? 33.444 -25.286 -10.631 1.00 16.06 ?  16  VAL   B CG2  1 
ATOM   4165 H H    . VAL   B 1 16  ? 33.281 -25.332 -13.874 1.00 19.01 ?  16  VAL   B H    1 
ATOM   4166 H HA   . VAL   B 1 16  ? 35.474 -24.833 -12.340 1.00 18.96 ?  16  VAL   B HA   1 
ATOM   4167 H HB   . VAL   B 1 16  ? 33.614 -26.912 -11.861 1.00 18.86 ?  16  VAL   B HB   1 
ATOM   4168 H HG11 . VAL   B 1 16  ? 34.929 -27.276 -9.879  1.00 18.62 ?  16  VAL   B HG11 1 
ATOM   4169 H HG12 . VAL   B 1 16  ? 35.625 -27.737 -11.230 1.00 18.62 ?  16  VAL   B HG12 1 
ATOM   4170 H HG13 . VAL   B 1 16  ? 36.043 -26.363 -10.548 1.00 18.62 ?  16  VAL   B HG13 1 
ATOM   4171 H HG21 . VAL   B 1 16  ? 33.110 -25.775 -9.862  1.00 19.30 ?  16  VAL   B HG21 1 
ATOM   4172 H HG22 . VAL   B 1 16  ? 34.030 -24.573 -10.343 1.00 19.30 ?  16  VAL   B HG22 1 
ATOM   4173 H HG23 . VAL   B 1 16  ? 32.703 -24.925 -11.141 1.00 19.30 ?  16  VAL   B HG23 1 
ATOM   4174 N N    . TYR   B 1 17  ? 36.972 -26.262 -13.581 1.00 16.00 ?  17  TYR   B N    1 
ATOM   4175 C CA   . TYR   B 1 17  ? 37.921 -27.014 -14.387 1.00 16.62 ?  17  TYR   B CA   1 
ATOM   4176 C C    . TYR   B 1 17  ? 38.974 -27.616 -13.465 1.00 15.72 ?  17  TYR   B C    1 
ATOM   4177 O O    . TYR   B 1 17  ? 39.238 -27.087 -12.385 1.00 15.84 ?  17  TYR   B O    1 
ATOM   4178 C CB   . TYR   B 1 17  ? 38.623 -26.086 -15.390 1.00 19.04 ?  17  TYR   B CB   1 
ATOM   4179 C CG   . TYR   B 1 17  ? 37.690 -25.320 -16.299 1.00 22.39 ?  17  TYR   B CG   1 
ATOM   4180 C CD1  . TYR   B 1 17  ? 37.088 -24.137 -15.884 1.00 23.77 ?  17  TYR   B CD1  1 
ATOM   4181 C CD2  . TYR   B 1 17  ? 37.415 -25.779 -17.579 1.00 24.50 ?  17  TYR   B CD2  1 
ATOM   4182 C CE1  . TYR   B 1 17  ? 36.234 -23.436 -16.720 1.00 25.57 ?  17  TYR   B CE1  1 
ATOM   4183 C CE2  . TYR   B 1 17  ? 36.568 -25.086 -18.421 1.00 25.89 ?  17  TYR   B CE2  1 
ATOM   4184 C CZ   . TYR   B 1 17  ? 35.978 -23.917 -17.986 1.00 26.56 ?  17  TYR   B CZ   1 
ATOM   4185 O OH   . TYR   B 1 17  ? 35.134 -23.226 -18.824 1.00 27.84 ?  17  TYR   B OH   1 
ATOM   4186 H H    . TYR   B 1 17  ? 37.364 -25.679 -13.079 1.00 19.22 ?  17  TYR   B H    1 
ATOM   4187 H HA   . TYR   B 1 17  ? 37.463 -27.724 -14.870 1.00 19.98 ?  17  TYR   B HA   1 
ATOM   4188 H HB2  . TYR   B 1 17  ? 39.156 -25.442 -14.900 1.00 22.87 ?  17  TYR   B HB2  1 
ATOM   4189 H HB3  . TYR   B 1 17  ? 39.193 -26.623 -15.955 1.00 22.87 ?  17  TYR   B HB3  1 
ATOM   4190 H HD1  . TYR   B 1 17  ? 37.256 -23.810 -15.030 1.00 28.55 ?  17  TYR   B HD1  1 
ATOM   4191 H HD2  . TYR   B 1 17  ? 37.807 -26.565 -17.878 1.00 29.43 ?  17  TYR   B HD2  1 
ATOM   4192 H HE1  . TYR   B 1 17  ? 35.834 -22.646 -16.430 1.00 30.71 ?  17  TYR   B HE1  1 
ATOM   4193 H HE2  . TYR   B 1 17  ? 36.389 -25.406 -19.277 1.00 31.10 ?  17  TYR   B HE2  1 
ATOM   4194 H HH   . TYR   B 1 17  ? 35.063 -23.624 -19.561 1.00 33.44 ?  17  TYR   B HH   1 
ATOM   4195 N N    . ILE   B 1 18  ? 39.594 -28.721 -13.890 1.00 15.70 ?  18  ILE   B N    1 
ATOM   4196 C CA   . ILE   B 1 18  ? 40.520 -29.441 -13.022 1.00 15.59 ?  18  ILE   B CA   1 
ATOM   4197 C C    . ILE   B 1 18  ? 41.684 -29.998 -13.833 1.00 15.79 ?  18  ILE   B C    1 
ATOM   4198 O O    . ILE   B 1 18  ? 41.531 -30.388 -14.993 1.00 17.57 ?  18  ILE   B O    1 
ATOM   4199 C CB   . ILE   B 1 18  ? 39.767 -30.540 -12.229 1.00 16.01 ?  18  ILE   B CB   1 
ATOM   4200 C CG1  . ILE   B 1 18  ? 40.616 -31.072 -11.074 1.00 15.96 ?  18  ILE   B CG1  1 
ATOM   4201 C CG2  . ILE   B 1 18  ? 39.296 -31.672 -13.152 1.00 16.67 ?  18  ILE   B CG2  1 
ATOM   4202 C CD1  . ILE   B 1 18  ? 39.805 -31.887 -10.071 1.00 17.38 ?  18  ILE   B CD1  1 
ATOM   4203 H H    . ILE   B 1 18  ? 39.495 -29.070 -14.666 1.00 18.87 ?  18  ILE   B H    1 
ATOM   4204 H HA   . ILE   B 1 18  ? 40.882 -28.821 -12.369 1.00 18.73 ?  18  ILE   B HA   1 
ATOM   4205 H HB   . ILE   B 1 18  ? 38.975 -30.139 -11.840 1.00 19.24 ?  18  ILE   B HB   1 
ATOM   4206 H HG12 . ILE   B 1 18  ? 41.313 -31.642 -11.427 1.00 19.19 ?  18  ILE   B HG12 1 
ATOM   4207 H HG13 . ILE   B 1 18  ? 41.005 -30.321 -10.599 1.00 19.19 ?  18  ILE   B HG13 1 
ATOM   4208 H HG21 . ILE   B 1 18  ? 38.692 -32.252 -12.657 1.00 20.03 ?  18  ILE   B HG21 1 
ATOM   4209 H HG22 . ILE   B 1 18  ? 38.832 -31.284 -13.908 1.00 20.03 ?  18  ILE   B HG22 1 
ATOM   4210 H HG23 . ILE   B 1 18  ? 40.065 -32.176 -13.454 1.00 20.03 ?  18  ILE   B HG23 1 
ATOM   4211 H HD11 . ILE   B 1 18  ? 40.385 -32.150 -9.338  1.00 20.88 ?  18  ILE   B HD11 1 
ATOM   4212 H HD12 . ILE   B 1 18  ? 39.076 -31.342 -9.736  1.00 20.88 ?  18  ILE   B HD12 1 
ATOM   4213 H HD13 . ILE   B 1 18  ? 39.455 -32.675 -10.514 1.00 20.88 ?  18  ILE   B HD13 1 
ATOM   4214 N N    . LYS   B 1 19  ? 42.859 -30.039 -13.200 1.00 16.10 ?  19  LYS   B N    1 
ATOM   4215 C CA   . LYS   B 1 19  ? 44.076 -30.508 -13.848 1.00 16.77 ?  19  LYS   B CA   1 
ATOM   4216 C C    . LYS   B 1 19  ? 44.971 -31.186 -12.821 1.00 16.73 ?  19  LYS   B C    1 
ATOM   4217 O O    . LYS   B 1 19  ? 45.042 -30.757 -11.669 1.00 16.25 ?  19  LYS   B O    1 
ATOM   4218 C CB   . LYS   B 1 19  ? 44.845 -29.342 -14.482 1.00 18.34 ?  19  LYS   B CB   1 
ATOM   4219 C CG   . LYS   B 1 19  ? 46.083 -29.750 -15.272 1.00 19.81 ?  19  LYS   B CG   1 
ATOM   4220 C CD   . LYS   B 1 19  ? 46.806 -28.517 -15.806 1.00 21.61 ?  19  LYS   B CD   1 
ATOM   4221 C CE   . LYS   B 1 19  ? 47.954 -28.885 -16.728 1.00 23.35 ?  19  LYS   B CE   1 
ATOM   4222 N NZ   . LYS   B 1 19  ? 48.681 -27.683 -17.222 1.00 24.20 ?  19  LYS   B NZ   1 
ATOM   4223 H H    . LYS   B 1 19  ? 42.964 -29.803 -12.374 1.00 19.34 ?  19  LYS   B H    1 
ATOM   4224 H HA   . LYS   B 1 19  ? 43.844 -31.149 -14.535 1.00 20.16 ?  19  LYS   B HA   1 
ATOM   4225 H HB2  . LYS   B 1 19  ? 44.245 -28.878 -15.088 1.00 22.03 ?  19  LYS   B HB2  1 
ATOM   4226 H HB3  . LYS   B 1 19  ? 45.123 -28.737 -13.774 1.00 22.03 ?  19  LYS   B HB3  1 
ATOM   4227 H HG2  . LYS   B 1 19  ? 46.688 -30.237 -14.692 1.00 23.80 ?  19  LYS   B HG2  1 
ATOM   4228 H HG3  . LYS   B 1 19  ? 45.813 -30.301 -16.023 1.00 23.80 ?  19  LYS   B HG3  1 
ATOM   4229 H HD2  . LYS   B 1 19  ? 46.176 -27.970 -16.303 1.00 25.96 ?  19  LYS   B HD2  1 
ATOM   4230 H HD3  . LYS   B 1 19  ? 47.165 -28.012 -15.058 1.00 25.96 ?  19  LYS   B HD3  1 
ATOM   4231 H HE2  . LYS   B 1 19  ? 48.582 -29.444 -16.244 1.00 28.05 ?  19  LYS   B HE2  1 
ATOM   4232 H HE3  . LYS   B 1 19  ? 47.602 -29.366 -17.494 1.00 28.05 ?  19  LYS   B HE3  1 
ATOM   4233 H HZ1  . LYS   B 1 19  ? 49.303 -27.925 -17.811 1.00 29.07 ?  19  LYS   B HZ1  1 
ATOM   4234 H HZ2  . LYS   B 1 19  ? 48.112 -27.124 -17.618 1.00 29.07 ?  19  LYS   B HZ2  1 
ATOM   4235 H HZ3  . LYS   B 1 19  ? 49.073 -27.264 -16.543 1.00 29.07 ?  19  LYS   B HZ3  1 
ATOM   4236 N N    . ASN   B 1 20  ? 45.659 -32.240 -13.250 1.00 17.91 ?  20  ASN   B N    1 
ATOM   4237 C CA   . ASN   B 1 20  ? 46.680 -32.879 -12.426 1.00 18.95 ?  20  ASN   B CA   1 
ATOM   4238 C C    . ASN   B 1 20  ? 47.955 -32.065 -12.612 1.00 19.64 ?  20  ASN   B C    1 
ATOM   4239 O O    . ASN   B 1 20  ? 48.609 -32.148 -13.657 1.00 21.61 ?  20  ASN   B O    1 
ATOM   4240 C CB   . ASN   B 1 20  ? 46.846 -34.335 -12.858 1.00 20.40 ?  20  ASN   B CB   1 
ATOM   4241 C CG   . ASN   B 1 20  ? 47.988 -35.049 -12.154 1.00 21.84 ?  20  ASN   B CG   1 
ATOM   4242 O OD1  . ASN   B 1 20  ? 48.644 -35.915 -12.747 1.00 24.29 ?  20  ASN   B OD1  1 
ATOM   4243 N ND2  . ASN   B 1 20  ? 48.215 -34.722 -10.889 1.00 21.31 ?  20  ASN   B ND2  1 
ATOM   4244 H H    . ASN   B 1 20  ? 45.555 -32.599 -14.022 1.00 21.52 ?  20  ASN   B H    1 
ATOM   4245 H HA   . ASN   B 1 20  ? 46.402 -32.852 -11.495 1.00 22.76 ?  20  ASN   B HA   1 
ATOM   4246 H HB2  . ASN   B 1 20  ? 46.024 -34.814 -12.658 1.00 24.51 ?  20  ASN   B HB2  1 
ATOM   4247 H HB3  . ASN   B 1 20  ? 47.017 -34.357 -13.809 1.00 24.51 ?  20  ASN   B HB3  1 
ATOM   4248 H HD21 . ASN   B 1 20  ? 48.849 -35.098 -10.453 1.00 25.60 ?  20  ASN   B HD21 1 
ATOM   4249 H HD22 . ASN   B 1 20  ? 47.729 -34.120 -10.499 1.00 25.60 ?  20  ASN   B HD22 1 
ATOM   4250 N N    . ALA   B 1 21  ? 48.296 -31.242 -11.614 1.00 19.09 ?  21  ALA   B N    1 
ATOM   4251 C CA   . ALA   B 1 21  ? 49.419 -30.331 -11.769 1.00 19.50 ?  21  ALA   B CA   1 
ATOM   4252 C C    . ALA   B 1 21  ? 49.881 -29.824 -10.414 1.00 18.45 ?  21  ALA   B C    1 
ATOM   4253 O O    . ALA   B 1 21  ? 49.144 -29.849 -9.424  1.00 18.54 ?  21  ALA   B O    1 
ATOM   4254 C CB   . ALA   B 1 21  ? 49.055 -29.151 -12.669 1.00 20.68 ?  21  ALA   B CB   1 
ATOM   4255 H H    . ALA   B 1 21  ? 47.893 -31.196 -10.846 1.00 22.93 ?  21  ALA   B H    1 
ATOM   4256 H HA   . ALA   B 1 21  ? 50.154 -30.814 -12.175 1.00 23.42 ?  21  ALA   B HA   1 
ATOM   4257 H HB1  . ALA   B 1 21  ? 49.847 -28.615 -12.804 1.00 24.84 ?  21  ALA   B HB1  1 
ATOM   4258 H HB2  . ALA   B 1 21  ? 48.735 -29.498 -13.514 1.00 24.84 ?  21  ALA   B HB2  1 
ATOM   4259 H HB3  . ALA   B 1 21  ? 48.361 -28.630 -12.237 1.00 24.84 ?  21  ALA   B HB3  1 
ATOM   4260 N N    . ASP   B 1 22  ? 51.137 -29.371 -10.404 1.00 18.00 ?  22  ASP   B N    1 
ATOM   4261 C CA   . ASP   B 1 22  ? 51.752 -28.665 -9.287  1.00 17.40 ?  22  ASP   B CA   1 
ATOM   4262 C C    . ASP   B 1 22  ? 51.333 -27.199 -9.377  1.00 16.27 ?  22  ASP   B C    1 
ATOM   4263 O O    . ASP   B 1 22  ? 51.634 -26.528 -10.368 1.00 16.55 ?  22  ASP   B O    1 
ATOM   4264 C CB   . ASP   B 1 22  ? 53.271 -28.832 -9.441  1.00 18.80 ?  22  ASP   B CB   1 
ATOM   4265 C CG   . ASP   B 1 22  ? 54.093 -28.083 -8.394  1.00 20.09 ?  22  ASP   B CG   1 
ATOM   4266 O OD1  . ASP   B 1 22  ? 53.716 -26.975 -7.975  1.00 20.04 ?  22  ASP   B OD1  1 
ATOM   4267 O OD2  . ASP   B 1 22  ? 55.169 -28.593 -8.014  1.00 22.33 -1 22  ASP   B OD2  1 
ATOM   4268 H H    . ASP   B 1 22  ? 51.676 -29.464 -11.075 1.00 21.63 ?  22  ASP   B H    1 
ATOM   4269 H HA   . ASP   B 1 22  ? 51.468 -29.041 -8.441  1.00 20.91 ?  22  ASP   B HA   1 
ATOM   4270 H HB2  . ASP   B 1 22  ? 53.497 -29.769 -9.375  1.00 22.59 ?  22  ASP   B HB2  1 
ATOM   4271 H HB3  . ASP   B 1 22  ? 53.539 -28.486 -10.309 1.00 22.59 ?  22  ASP   B HB3  1 
ATOM   4272 N N    . ILE   B 1 23  ? 50.619 -26.704 -8.359  1.00 15.45 ?  23  ILE   B N    1 
ATOM   4273 C CA   . ILE   B 1 23  ? 50.025 -25.365 -8.432  1.00 14.66 ?  23  ILE   B CA   1 
ATOM   4274 C C    . ILE   B 1 23  ? 51.081 -24.276 -8.573  1.00 14.43 ?  23  ILE   B C    1 
ATOM   4275 O O    . ILE   B 1 23  ? 50.814 -23.233 -9.178  1.00 14.14 ?  23  ILE   B O    1 
ATOM   4276 C CB   . ILE   B 1 23  ? 49.090 -25.113 -7.232  1.00 15.15 ?  23  ILE   B CB   1 
ATOM   4277 C CG1  . ILE   B 1 23  ? 48.268 -23.842 -7.442  1.00 15.84 ?  23  ILE   B CG1  1 
ATOM   4278 C CG2  . ILE   B 1 23  ? 49.866 -25.084 -5.932  1.00 16.63 ?  23  ILE   B CG2  1 
ATOM   4279 C CD1  . ILE   B 1 23  ? 47.158 -23.655 -6.429  1.00 16.30 ?  23  ILE   B CD1  1 
ATOM   4280 H H    . ILE   B 1 23  ? 50.471 -27.123 -7.626  1.00 18.57 ?  23  ILE   B H    1 
ATOM   4281 H HA   . ILE   B 1 23  ? 49.478 -25.328 -9.229  1.00 17.62 ?  23  ILE   B HA   1 
ATOM   4282 H HB   . ILE   B 1 23  ? 48.469 -25.860 -7.189  1.00 18.21 ?  23  ILE   B HB   1 
ATOM   4283 H HG12 . ILE   B 1 23  ? 48.863 -23.074 -7.380  1.00 19.04 ?  23  ILE   B HG12 1 
ATOM   4284 H HG13 . ILE   B 1 23  ? 47.867 -23.869 -8.327  1.00 19.04 ?  23  ILE   B HG13 1 
ATOM   4285 H HG21 . ILE   B 1 23  ? 49.242 -25.075 -5.192  1.00 19.99 ?  23  ILE   B HG21 1 
ATOM   4286 H HG22 . ILE   B 1 23  ? 50.428 -25.876 -5.880  1.00 19.99 ?  23  ILE   B HG22 1 
ATOM   4287 H HG23 . ILE   B 1 23  ? 50.420 -24.289 -5.912  1.00 19.99 ?  23  ILE   B HG23 1 
ATOM   4288 H HD11 . ILE   B 1 23  ? 46.647 -22.867 -6.669  1.00 19.58 ?  23  ILE   B HD11 1 
ATOM   4289 H HD12 . ILE   B 1 23  ? 46.589 -24.439 -6.445  1.00 19.58 ?  23  ILE   B HD12 1 
ATOM   4290 H HD13 . ILE   B 1 23  ? 47.552 -23.544 -5.552  1.00 19.58 ?  23  ILE   B HD13 1 
ATOM   4291 N N    . VAL   B 1 24  ? 52.279 -24.480 -8.016  1.00 14.78 ?  24  VAL   B N    1 
ATOM   4292 C CA   . VAL   B 1 24  ? 53.357 -23.503 -8.186  1.00 15.29 ?  24  VAL   B CA   1 
ATOM   4293 C C    . VAL   B 1 24  ? 53.807 -23.462 -9.640  1.00 15.73 ?  24  VAL   B C    1 
ATOM   4294 O O    . VAL   B 1 24  ? 53.950 -22.387 -10.240 1.00 16.00 ?  24  VAL   B O    1 
ATOM   4295 C CB   . VAL   B 1 24  ? 54.533 -23.822 -7.241  1.00 16.12 ?  24  VAL   B CB   1 
ATOM   4296 C CG1  . VAL   B 1 24  ? 55.742 -22.951 -7.576  1.00 16.99 ?  24  VAL   B CG1  1 
ATOM   4297 C CG2  . VAL   B 1 24  ? 54.120 -23.623 -5.796  1.00 16.97 ?  24  VAL   B CG2  1 
ATOM   4298 H H    . VAL   B 1 24  ? 52.491 -25.165 -7.541  1.00 17.77 ?  24  VAL   B H    1 
ATOM   4299 H HA   . VAL   B 1 24  ? 53.025 -22.625 -7.951  1.00 18.38 ?  24  VAL   B HA   1 
ATOM   4300 H HB   . VAL   B 1 24  ? 54.794 -24.752 -7.353  1.00 19.38 ?  24  VAL   B HB   1 
ATOM   4301 H HG11 . VAL   B 1 24  ? 56.334 -22.929 -6.809  1.00 20.42 ?  24  VAL   B HG11 1 
ATOM   4302 H HG12 . VAL   B 1 24  ? 56.202 -23.332 -8.338  1.00 20.42 ?  24  VAL   B HG12 1 
ATOM   4303 H HG13 . VAL   B 1 24  ? 55.434 -22.055 -7.781  1.00 20.42 ?  24  VAL   B HG13 1 
ATOM   4304 H HG21 . VAL   B 1 24  ? 54.850 -23.887 -5.216  1.00 20.39 ?  24  VAL   B HG21 1 
ATOM   4305 H HG22 . VAL   B 1 24  ? 53.907 -22.687 -5.657  1.00 20.39 ?  24  VAL   B HG22 1 
ATOM   4306 H HG23 . VAL   B 1 24  ? 53.338 -24.170 -5.613  1.00 20.39 ?  24  VAL   B HG23 1 
ATOM   4307 N N    . GLU   B 1 25  ? 54.068 -24.636 -10.222 1.00 16.79 ?  25  GLU   B N    1 
ATOM   4308 C CA   . GLU   B 1 25  ? 54.457 -24.677 -11.625 1.00 18.19 ?  25  GLU   B CA   1 
ATOM   4309 C C    . GLU   B 1 25  ? 53.348 -24.137 -12.513 1.00 16.50 ?  25  GLU   B C    1 
ATOM   4310 O O    . GLU   B 1 25  ? 53.613 -23.413 -13.482 1.00 17.48 ?  25  GLU   B O    1 
ATOM   4311 C CB   . GLU   B 1 25  ? 54.848 -26.098 -12.022 1.00 22.26 ?  25  GLU   B CB   1 
ATOM   4312 C CG   . GLU   B 1 25  ? 56.143 -26.553 -11.369 1.00 27.46 ?  25  GLU   B CG   1 
ATOM   4313 C CD   . GLU   B 1 25  ? 57.255 -25.514 -11.453 1.00 32.35 ?  25  GLU   B CD   1 
ATOM   4314 O OE1  . GLU   B 1 25  ? 57.628 -25.126 -12.580 1.00 34.25 ?  25  GLU   B OE1  1 
ATOM   4315 O OE2  . GLU   B 1 25  ? 57.744 -25.069 -10.388 1.00 33.82 -1 25  GLU   B OE2  1 
ATOM   4316 H H    . GLU   B 1 25  ? 54.027 -25.403 -9.832  1.00 20.17 ?  25  GLU   B H    1 
ATOM   4317 H HA   . GLU   B 1 25  ? 55.215 -24.091 -11.753 1.00 21.86 ?  25  GLU   B HA   1 
ATOM   4318 H HB2  . GLU   B 1 25  ? 54.143 -26.708 -11.746 1.00 26.74 ?  25  GLU   B HB2  1 
ATOM   4319 H HB3  . GLU   B 1 25  ? 54.961 -26.137 -12.984 1.00 26.74 ?  25  GLU   B HB3  1 
ATOM   4320 H HG2  . GLU   B 1 25  ? 55.982 -26.718 -10.433 1.00 32.98 ?  25  GLU   B HG2  1 
ATOM   4321 H HG3  . GLU   B 1 25  ? 56.449 -27.358 -11.812 1.00 32.98 ?  25  GLU   B HG3  1 
ATOM   4322 N N    . GLU   B 1 26  ? 52.095 -24.454 -12.181 1.00 15.55 ?  26  GLU   B N    1 
ATOM   4323 C CA   . GLU   B 1 26  ? 50.965 -23.922 -12.936 1.00 16.37 ?  26  GLU   B CA   1 
ATOM   4324 C C    . GLU   B 1 26  ? 50.926 -22.404 -12.865 1.00 15.57 ?  26  GLU   B C    1 
ATOM   4325 O O    . GLU   B 1 26  ? 50.733 -21.731 -13.881 1.00 16.60 ?  26  GLU   B O    1 
ATOM   4326 C CB   . GLU   B 1 26  ? 49.654 -24.503 -12.402 1.00 18.19 ?  26  GLU   B CB   1 
ATOM   4327 C CG   . GLU   B 1 26  ? 49.212 -25.787 -13.071 1.00 21.40 ?  26  GLU   B CG   1 
ATOM   4328 C CD   . GLU   B 1 26  ? 48.973 -25.642 -14.575 1.00 23.31 ?  26  GLU   B CD   1 
ATOM   4329 O OE1  . GLU   B 1 26  ? 48.003 -24.975 -15.000 1.00 23.79 ?  26  GLU   B OE1  1 
ATOM   4330 O OE2  . GLU   B 1 26  ? 49.758 -26.224 -15.335 1.00 25.29 -1 26  GLU   B OE2  1 
ATOM   4331 H H    . GLU   B 1 26  ? 51.874 -24.976 -11.529 1.00 18.69 ?  26  GLU   B H    1 
ATOM   4332 H HA   . GLU   B 1 26  ? 51.055 -24.177 -13.864 1.00 19.67 ?  26  GLU   B HA   1 
ATOM   4333 H HB2  . GLU   B 1 26  ? 49.756 -24.685 -11.451 1.00 21.85 ?  26  GLU   B HB2  1 
ATOM   4334 H HB3  . GLU   B 1 26  ? 48.948 -23.847 -12.527 1.00 21.85 ?  26  GLU   B HB3  1 
ATOM   4335 H HG2  . GLU   B 1 26  ? 49.904 -26.447 -12.942 1.00 25.71 ?  26  GLU   B HG2  1 
ATOM   4336 H HG3  . GLU   B 1 26  ? 48.384 -26.082 -12.658 1.00 25.71 ?  26  GLU   B HG3  1 
ATOM   4337 N N    . ALA   B 1 27  ? 51.084 -21.849 -11.664 1.00 14.87 ?  27  ALA   B N    1 
ATOM   4338 C CA   . ALA   B 1 27  ? 51.043 -20.397 -11.525 1.00 14.96 ?  27  ALA   B CA   1 
ATOM   4339 C C    . ALA   B 1 27  ? 52.118 -19.735 -12.378 1.00 16.16 ?  27  ALA   B C    1 
ATOM   4340 O O    . ALA   B 1 27  ? 51.859 -18.728 -13.054 1.00 16.77 ?  27  ALA   B O    1 
ATOM   4341 C CB   . ALA   B 1 27  ? 51.186 -20.009 -10.053 1.00 14.77 ?  27  ALA   B CB   1 
ATOM   4342 H H    . ALA   B 1 27  ? 51.210 -22.281 -10.927 1.00 17.87 ?  27  ALA   B H    1 
ATOM   4343 H HA   . ALA   B 1 27  ? 50.181 -20.077 -11.830 1.00 17.98 ?  27  ALA   B HA   1 
ATOM   4344 H HB1  . ALA   B 1 27  ? 51.146 -19.042 -9.976  1.00 17.76 ?  27  ALA   B HB1  1 
ATOM   4345 H HB2  . ALA   B 1 27  ? 50.452 -20.406 -9.549  1.00 17.76 ?  27  ALA   B HB2  1 
ATOM   4346 H HB3  . ALA   B 1 27  ? 52.031 -20.336 -9.717  1.00 17.76 ?  27  ALA   B HB3  1 
ATOM   4347 N N    . LYS   B 1 28  ? 53.329 -20.296 -12.380 1.00 17.43 ?  28  LYS   B N    1 
ATOM   4348 C CA   . LYS   B 1 28  ? 54.403 -19.685 -13.153 1.00 19.39 ?  28  LYS   B CA   1 
ATOM   4349 C C    . LYS   B 1 28  ? 54.145 -19.772 -14.653 1.00 20.18 ?  28  LYS   B C    1 
ATOM   4350 O O    . LYS   B 1 28  ? 54.550 -18.875 -15.402 1.00 20.96 ?  28  LYS   B O    1 
ATOM   4351 C CB   . LYS   B 1 28  ? 55.755 -20.292 -12.761 1.00 22.23 ?  28  LYS   B CB   1 
ATOM   4352 C CG   . LYS   B 1 28  ? 56.165 -19.944 -11.330 1.00 25.29 ?  28  LYS   B CG   1 
ATOM   4353 C CD   . LYS   B 1 28  ? 57.597 -20.348 -11.003 1.00 29.12 ?  28  LYS   B CD   1 
ATOM   4354 C CE   . LYS   B 1 28  ? 57.693 -21.800 -10.602 1.00 33.09 ?  28  LYS   B CE   1 
ATOM   4355 N NZ   . LYS   B 1 28  ? 59.055 -22.133 -10.100 1.00 36.19 ?  28  LYS   B NZ   1 
ATOM   4356 H H    . LYS   B 1 28  ? 53.546 -21.010 -11.957 1.00 20.95 ?  28  LYS   B H    1 
ATOM   4357 H HA   . LYS   B 1 28  ? 54.442 -18.742 -12.930 1.00 23.30 ?  28  LYS   B HA   1 
ATOM   4358 H HB2  . LYS   B 1 28  ? 55.701 -21.257 -12.828 1.00 26.70 ?  28  LYS   B HB2  1 
ATOM   4359 H HB3  . LYS   B 1 28  ? 56.441 -19.954 -13.359 1.00 26.70 ?  28  LYS   B HB3  1 
ATOM   4360 H HG2  . LYS   B 1 28  ? 56.087 -18.982 -11.209 1.00 30.37 ?  28  LYS   B HG2  1 
ATOM   4361 H HG3  . LYS   B 1 28  ? 55.573 -20.401 -10.715 1.00 30.37 ?  28  LYS   B HG3  1 
ATOM   4362 H HD2  . LYS   B 1 28  ? 58.152 -20.208 -11.786 1.00 34.98 ?  28  LYS   B HD2  1 
ATOM   4363 H HD3  . LYS   B 1 28  ? 57.917 -19.804 -10.265 1.00 34.98 ?  28  LYS   B HD3  1 
ATOM   4364 H HE2  . LYS   B 1 28  ? 57.054 -21.979 -9.894  1.00 39.74 ?  28  LYS   B HE2  1 
ATOM   4365 H HE3  . LYS   B 1 28  ? 57.505 -22.359 -11.372 1.00 39.74 ?  28  LYS   B HE3  1 
ATOM   4366 H HZ1  . LYS   B 1 28  ? 59.093 -22.991 -9.869  1.00 43.46 ?  28  LYS   B HZ1  1 
ATOM   4367 H HZ2  . LYS   B 1 28  ? 59.659 -21.976 -10.735 1.00 43.46 ?  28  LYS   B HZ2  1 
ATOM   4368 H HZ3  . LYS   B 1 28  ? 59.247 -21.632 -9.389  1.00 43.46 ?  28  LYS   B HZ3  1 
ATOM   4369 N N    . LYS   B 1 29  ? 53.435 -20.809 -15.102 1.00 21.44 ?  29  LYS   B N    1 
ATOM   4370 C CA   . LYS   B 1 29  ? 53.141 -20.954 -16.526 1.00 24.49 ?  29  LYS   B CA   1 
ATOM   4371 C C    . LYS   B 1 29  ? 51.904 -20.164 -16.944 1.00 23.43 ?  29  LYS   B C    1 
ATOM   4372 O O    . LYS   B 1 29  ? 51.911 -19.515 -17.995 1.00 24.45 ?  29  LYS   B O    1 
ATOM   4373 C CB   . LYS   B 1 29  ? 52.963 -22.434 -16.873 1.00 29.47 ?  29  LYS   B CB   1 
ATOM   4374 C CG   . LYS   B 1 29  ? 52.868 -22.706 -18.366 1.00 34.17 ?  29  LYS   B CG   1 
ATOM   4375 C CD   . LYS   B 1 29  ? 53.139 -24.171 -18.690 1.00 37.76 ?  29  LYS   B CD   1 
ATOM   4376 C CE   . LYS   B 1 29  ? 52.025 -25.077 -18.193 1.00 40.00 ?  29  LYS   B CE   1 
ATOM   4377 N NZ   . LYS   B 1 29  ? 52.300 -26.511 -18.501 1.00 41.90 ?  29  LYS   B NZ   1 
ATOM   4378 H H    . LYS   B 1 29  ? 53.116 -21.434 -14.605 1.00 25.75 ?  29  LYS   B H    1 
ATOM   4379 H HA   . LYS   B 1 29  ? 53.889 -20.616 -17.034 1.00 29.41 ?  29  LYS   B HA   1 
ATOM   4380 H HB2  . LYS   B 1 29  ? 53.724 -22.926 -16.529 1.00 35.40 ?  29  LYS   B HB2  1 
ATOM   4381 H HB3  . LYS   B 1 29  ? 52.148 -22.758 -16.460 1.00 35.40 ?  29  LYS   B HB3  1 
ATOM   4382 H HG2  . LYS   B 1 29  ? 51.975 -22.487 -18.674 1.00 41.03 ?  29  LYS   B HG2  1 
ATOM   4383 H HG3  . LYS   B 1 29  ? 53.525 -22.166 -18.832 1.00 41.03 ?  29  LYS   B HG3  1 
ATOM   4384 H HD2  . LYS   B 1 29  ? 53.209 -24.277 -19.652 1.00 45.34 ?  29  LYS   B HD2  1 
ATOM   4385 H HD3  . LYS   B 1 29  ? 53.966 -24.445 -18.263 1.00 45.34 ?  29  LYS   B HD3  1 
ATOM   4386 H HE2  . LYS   B 1 29  ? 51.942 -24.985 -17.231 1.00 48.03 ?  29  LYS   B HE2  1 
ATOM   4387 H HE3  . LYS   B 1 29  ? 51.194 -24.828 -18.626 1.00 48.03 ?  29  LYS   B HE3  1 
ATOM   4388 H HZ1  . LYS   B 1 29  ? 51.634 -27.020 -18.200 1.00 50.30 ?  29  LYS   B HZ1  1 
ATOM   4389 H HZ2  . LYS   B 1 29  ? 52.376 -26.624 -19.381 1.00 50.30 ?  29  LYS   B HZ2  1 
ATOM   4390 H HZ3  . LYS   B 1 29  ? 53.058 -26.766 -18.110 1.00 50.30 ?  29  LYS   B HZ3  1 
ATOM   4391 N N    . VAL   B 1 30  ? 50.835 -20.222 -16.144 1.00 21.44 ?  30  VAL   B N    1 
ATOM   4392 C CA   . VAL   B 1 30  ? 49.549 -19.616 -16.504 1.00 20.90 ?  30  VAL   B CA   1 
ATOM   4393 C C    . VAL   B 1 30  ? 49.566 -18.103 -16.336 1.00 20.00 ?  30  VAL   B C    1 
ATOM   4394 O O    . VAL   B 1 30  ? 48.855 -17.383 -17.052 1.00 21.49 ?  30  VAL   B O    1 
ATOM   4395 C CB   . VAL   B 1 30  ? 48.442 -20.226 -15.620 1.00 21.12 ?  30  VAL   B CB   1 
ATOM   4396 C CG1  . VAL   B 1 30  ? 47.164 -19.396 -15.689 1.00 21.61 ?  30  VAL   B CG1  1 
ATOM   4397 C CG2  . VAL   B 1 30  ? 48.175 -21.673 -16.011 1.00 21.77 ?  30  VAL   B CG2  1 
ATOM   4398 H H    . VAL   B 1 30  ? 50.820 -20.631 -15.381 1.00 25.76 ?  30  VAL   B H    1 
ATOM   4399 H HA   . VAL   B 1 30  ? 49.343 -19.835 -17.427 1.00 25.11 ?  30  VAL   B HA   1 
ATOM   4400 H HB   . VAL   B 1 30  ? 48.742 -20.231 -14.697 1.00 25.37 ?  30  VAL   B HB   1 
ATOM   4401 H HG11 . VAL   B 1 30  ? 46.414 -19.967 -15.455 1.00 25.96 ?  30  VAL   B HG11 1 
ATOM   4402 H HG12 . VAL   B 1 30  ? 47.226 -18.665 -15.058 1.00 25.96 ?  30  VAL   B HG12 1 
ATOM   4403 H HG13 . VAL   B 1 30  ? 47.048 -19.065 -16.588 1.00 25.96 ?  30  VAL   B HG13 1 
ATOM   4404 H HG21 . VAL   B 1 30  ? 47.478 -22.037 -15.434 1.00 26.15 ?  30  VAL   B HG21 1 
ATOM   4405 H HG22 . VAL   B 1 30  ? 47.878 -21.702 -16.935 1.00 26.15 ?  30  VAL   B HG22 1 
ATOM   4406 H HG23 . VAL   B 1 30  ? 48.987 -22.188 -15.906 1.00 26.15 ?  30  VAL   B HG23 1 
ATOM   4407 N N    A LYS   B 1 31  ? 50.340 -17.604 -15.382 0.60 19.41 ?  31  LYS   B N    1 
ATOM   4408 N N    B LYS   B 1 31  ? 50.342 -17.610 -15.382 0.40 19.68 ?  31  LYS   B N    1 
ATOM   4409 C CA   A LYS   B 1 31  ? 50.381 -16.193 -15.017 0.60 19.65 ?  31  LYS   B CA   1 
ATOM   4410 C CA   B LYS   B 1 31  ? 50.379 -16.202 -15.016 0.40 19.89 ?  31  LYS   B CA   1 
ATOM   4411 C C    A LYS   B 1 31  ? 48.985 -15.701 -14.641 0.60 17.94 ?  31  LYS   B C    1 
ATOM   4412 C C    B LYS   B 1 31  ? 48.973 -15.728 -14.661 0.40 17.94 ?  31  LYS   B C    1 
ATOM   4413 O O    A LYS   B 1 31  ? 48.465 -14.762 -15.258 0.60 18.70 ?  31  LYS   B O    1 
ATOM   4414 O O    B LYS   B 1 31  ? 48.428 -14.835 -15.322 0.40 18.32 ?  31  LYS   B O    1 
ATOM   4415 C CB   A LYS   B 1 31  ? 51.008 -15.364 -16.141 0.60 22.49 ?  31  LYS   B CB   1 
ATOM   4416 C CB   B LYS   B 1 31  ? 51.013 -15.380 -16.140 0.40 22.38 ?  31  LYS   B CB   1 
ATOM   4417 C CG   A LYS   B 1 31  ? 52.451 -15.752 -16.461 0.60 25.24 ?  31  LYS   B CG   1 
ATOM   4418 C CG   B LYS   B 1 31  ? 52.385 -15.908 -16.550 0.40 24.58 ?  31  LYS   B CG   1 
ATOM   4419 C CD   A LYS   B 1 31  ? 53.001 -14.933 -17.619 0.60 27.80 ?  31  LYS   B CD   1 
ATOM   4420 C CD   B LYS   B 1 31  ? 52.968 -15.147 -17.724 0.40 26.53 ?  31  LYS   B CD   1 
ATOM   4421 C CE   A LYS   B 1 31  ? 54.462 -15.246 -17.868 0.60 29.48 ?  31  LYS   B CE   1 
ATOM   4422 C CE   B LYS   B 1 31  ? 54.428 -15.503 -17.926 0.40 27.92 ?  31  LYS   B CE   1 
ATOM   4423 N NZ   A LYS   B 1 31  ? 55.289 -14.912 -16.678 0.60 30.68 ?  31  LYS   B NZ   1 
ATOM   4424 N NZ   B LYS   B 1 31  ? 55.227 -15.209 -16.705 0.40 28.78 ?  31  LYS   B NZ   1 
ATOM   4425 H H    A LYS   B 1 31  ? 50.865 -18.095 -14.914 0.60 23.32 ?  31  LYS   B H    1 
ATOM   4426 H H    B LYS   B 1 31  ? 50.876 -18.096 -14.917 0.40 23.65 ?  31  LYS   B H    1 
ATOM   4427 H HA   A LYS   B 1 31  ? 50.936 -16.110 -14.234 0.60 23.60 ?  31  LYS   B HA   1 
ATOM   4428 H HA   B LYS   B 1 31  ? 50.932 -16.110 -14.234 0.40 23.89 ?  31  LYS   B HA   1 
ATOM   4429 H HB2  A LYS   B 1 31  ? 50.484 -15.479 -16.948 0.60 27.02 ?  31  LYS   B HB2  1 
ATOM   4430 H HB2  B LYS   B 1 31  ? 50.440 -15.400 -16.918 0.40 26.88 ?  31  LYS   B HB2  1 
ATOM   4431 H HB3  A LYS   B 1 31  ? 51.003 -14.435 -15.872 0.60 27.02 ?  31  LYS   B HB3  1 
ATOM   4432 H HB3  B LYS   B 1 31  ? 51.127 -14.467 -15.831 0.40 26.88 ?  31  LYS   B HB3  1 
ATOM   4433 H HG2  A LYS   B 1 31  ? 53.003 -15.592 -15.679 0.60 30.32 ?  31  LYS   B HG2  1 
ATOM   4434 H HG2  B LYS   B 1 31  ? 52.990 -15.823 -15.797 0.40 29.53 ?  31  LYS   B HG2  1 
ATOM   4435 H HG3  A LYS   B 1 31  ? 52.484 -16.691 -16.706 0.60 30.32 ?  31  LYS   B HG3  1 
ATOM   4436 H HG3  B LYS   B 1 31  ? 52.305 -16.839 -16.809 0.40 29.53 ?  31  LYS   B HG3  1 
ATOM   4437 H HD2  A LYS   B 1 31  ? 52.499 -15.143 -18.423 0.60 33.39 ?  31  LYS   B HD2  1 
ATOM   4438 H HD2  B LYS   B 1 31  ? 52.481 -15.381 -18.530 0.40 31.86 ?  31  LYS   B HD2  1 
ATOM   4439 H HD3  A LYS   B 1 31  ? 52.919 -13.990 -17.409 0.60 33.39 ?  31  LYS   B HD3  1 
ATOM   4440 H HD3  B LYS   B 1 31  ? 52.904 -14.196 -17.553 0.40 31.86 ?  31  LYS   B HD3  1 
ATOM   4441 H HE2  A LYS   B 1 31  ? 54.562 -16.194 -18.054 0.60 35.40 ?  31  LYS   B HE2  1 
ATOM   4442 H HE2  B LYS   B 1 31  ? 54.506 -16.452 -18.119 0.40 33.53 ?  31  LYS   B HE2  1 
ATOM   4443 H HE3  A LYS   B 1 31  ? 54.780 -14.721 -18.619 0.60 35.40 ?  31  LYS   B HE3  1 
ATOM   4444 H HE3  B LYS   B 1 31  ? 54.788 -14.980 -18.659 0.40 33.53 ?  31  LYS   B HE3  1 
ATOM   4445 H HZ1  A LYS   B 1 31  ? 56.151 -15.015 -16.868 0.60 36.85 ?  31  LYS   B HZ1  1 
ATOM   4446 H HZ1  B LYS   B 1 31  ? 56.096 -15.250 -16.891 0.40 34.56 ?  31  LYS   B HZ1  1 
ATOM   4447 H HZ2  A LYS   B 1 31  ? 55.144 -14.068 -16.436 0.60 36.85 ?  31  LYS   B HZ2  1 
ATOM   4448 H HZ2  B LYS   B 1 31  ? 55.035 -14.392 -16.406 0.40 34.56 ?  31  LYS   B HZ2  1 
ATOM   4449 H HZ3  A LYS   B 1 31  ? 55.076 -15.447 -15.999 0.60 36.85 ?  31  LYS   B HZ3  1 
ATOM   4450 H HZ3  B LYS   B 1 31  ? 55.040 -15.800 -16.066 0.40 34.56 ?  31  LYS   B HZ3  1 
ATOM   4451 N N    . PRO   B 1 32  ? 48.356 -16.302 -13.626 1.00 15.91 ?  32  PRO   B N    1 
ATOM   4452 C CA   . PRO   B 1 32  ? 46.977 -15.938 -13.290 1.00 15.08 ?  32  PRO   B CA   1 
ATOM   4453 C C    . PRO   B 1 32  ? 46.885 -14.596 -12.581 1.00 14.93 ?  32  PRO   B C    1 
ATOM   4454 O O    . PRO   B 1 32  ? 47.805 -14.167 -11.879 1.00 16.35 ?  32  PRO   B O    1 
ATOM   4455 C CB   . PRO   B 1 32  ? 46.560 -17.061 -12.332 1.00 15.09 ?  32  PRO   B CB   1 
ATOM   4456 C CG   . PRO   B 1 32  ? 47.840 -17.401 -11.626 1.00 15.46 ?  32  PRO   B CG   1 
ATOM   4457 C CD   . PRO   B 1 32  ? 48.908 -17.288 -12.677 1.00 15.57 ?  32  PRO   B CD   1 
ATOM   4458 H HA   . PRO   B 1 32  ? 46.412 -15.940 -14.078 1.00 18.13 ?  32  PRO   B HA   1 
ATOM   4459 H HB2  . PRO   B 1 32  ? 45.887 -16.739 -11.710 1.00 18.14 ?  32  PRO   B HB2  1 
ATOM   4460 H HB3  . PRO   B 1 32  ? 46.226 -17.822 -12.838 1.00 18.14 ?  32  PRO   B HB3  1 
ATOM   4461 H HG2  . PRO   B 1 32  ? 47.993 -16.765 -10.905 1.00 18.58 ?  32  PRO   B HG2  1 
ATOM   4462 H HG3  . PRO   B 1 32  ? 47.793 -18.305 -11.276 1.00 18.58 ?  32  PRO   B HG3  1 
ATOM   4463 H HD2  . PRO   B 1 32  ? 49.725 -16.957 -12.277 1.00 18.71 ?  32  PRO   B HD2  1 
ATOM   4464 H HD3  . PRO   B 1 32  ? 49.033 -18.140 -13.108 1.00 18.71 ?  32  PRO   B HD3  1 
ATOM   4465 N N    . THR   B 1 33  ? 45.735 -13.944 -12.755 1.00 14.61 ?  33  THR   B N    1 
ATOM   4466 C CA   . THR   B 1 33  ? 45.438 -12.763 -11.955 1.00 14.28 ?  33  THR   B CA   1 
ATOM   4467 C C    . THR   B 1 33  ? 45.387 -13.107 -10.473 1.00 14.30 ?  33  THR   B C    1 
ATOM   4468 O O    . THR   B 1 33  ? 45.861 -12.328 -9.630  1.00 15.17 ?  33  THR   B O    1 
ATOM   4469 C CB   . THR   B 1 33  ? 44.121 -12.134 -12.420 1.00 15.19 ?  33  THR   B CB   1 
ATOM   4470 O OG1  . THR   B 1 33  ? 44.182 -11.877 -13.825 1.00 15.32 ?  33  THR   B OG1  1 
ATOM   4471 C CG2  . THR   B 1 33  ? 43.830 -10.835 -11.665 1.00 16.24 ?  33  THR   B CG2  1 
ATOM   4472 H H    . THR   B 1 33  ? 45.121 -14.161 -13.316 1.00 17.56 ?  33  THR   B H    1 
ATOM   4473 H HA   . THR   B 1 33  ? 46.135 -12.106 -12.078 1.00 17.17 ?  33  THR   B HA   1 
ATOM   4474 H HB   . THR   B 1 33  ? 43.389 -12.751 -12.241 1.00 18.25 ?  33  THR   B HB   1 
ATOM   4475 H HG1  . THR   B 1 33  ? 43.463 -11.514 -14.084 1.00 18.42 ?  33  THR   B HG1  1 
ATOM   4476 H HG21 . THR   B 1 33  ? 43.074 -10.380 -12.064 1.00 19.52 ?  33  THR   B HG21 1 
ATOM   4477 H HG22 . THR   B 1 33  ? 43.626 -11.028 -10.735 1.00 19.52 ?  33  THR   B HG22 1 
ATOM   4478 H HG23 . THR   B 1 33  ? 44.605 -10.253 -11.702 1.00 19.52 ?  33  THR   B HG23 1 
ATOM   4479 N N    . VAL   B 1 34  ? 44.832 -14.278 -10.135 1.00 13.53 ?  34  VAL   B N    1 
ATOM   4480 C CA   . VAL   B 1 34  ? 44.638 -14.678 -8.745  1.00 13.25 ?  34  VAL   B CA   1 
ATOM   4481 C C    . VAL   B 1 34  ? 45.072 -16.128 -8.584  1.00 12.37 ?  34  VAL   B C    1 
ATOM   4482 O O    . VAL   B 1 34  ? 44.544 -17.020 -9.263  1.00 12.93 ?  34  VAL   B O    1 
ATOM   4483 C CB   . VAL   B 1 34  ? 43.170 -14.538 -8.298  1.00 14.34 ?  34  VAL   B CB   1 
ATOM   4484 C CG1  . VAL   B 1 34  ? 43.014 -14.989 -6.855  1.00 14.64 ?  34  VAL   B CG1  1 
ATOM   4485 C CG2  . VAL   B 1 34  ? 42.669 -13.112 -8.488  1.00 15.22 ?  34  VAL   B CG2  1 
ATOM   4486 H H    . VAL   B 1 34  ? 44.561 -14.870 -10.700 1.00 16.27 ?  34  VAL   B H    1 
ATOM   4487 H HA   . VAL   B 1 34  ? 45.194 -14.127 -8.165  1.00 15.93 ?  34  VAL   B HA   1 
ATOM   4488 H HB   . VAL   B 1 34  ? 42.625 -15.121 -8.848  1.00 17.23 ?  34  VAL   B HB   1 
ATOM   4489 H HG11 . VAL   B 1 34  ? 42.156 -14.677 -6.518  1.00 17.60 ?  34  VAL   B HG11 1 
ATOM   4490 H HG12 . VAL   B 1 34  ? 43.046 -15.959 -6.812  1.00 17.60 ?  34  VAL   B HG12 1 
ATOM   4491 H HG13 . VAL   B 1 34  ? 43.730 -14.610 -6.321  1.00 17.60 ?  34  VAL   B HG13 1 
ATOM   4492 H HG21 . VAL   B 1 34  ? 41.753 -13.056 -8.170  1.00 18.29 ?  34  VAL   B HG21 1 
ATOM   4493 H HG22 . VAL   B 1 34  ? 43.232 -12.508 -7.979  1.00 18.29 ?  34  VAL   B HG22 1 
ATOM   4494 H HG23 . VAL   B 1 34  ? 42.706 -12.886 -9.430  1.00 18.29 ?  34  VAL   B HG23 1 
ATOM   4495 N N    . VAL   B 1 35  ? 45.984 -16.377 -7.648  1.00 11.73 ?  35  VAL   B N    1 
ATOM   4496 C CA   . VAL   B 1 35  ? 46.220 -17.719 -7.125  1.00 11.66 ?  35  VAL   B CA   1 
ATOM   4497 C C    . VAL   B 1 35  ? 45.684 -17.767 -5.704  1.00 11.03 ?  35  VAL   B C    1 
ATOM   4498 O O    . VAL   B 1 35  ? 45.902 -16.837 -4.917  1.00 11.58 ?  35  VAL   B O    1 
ATOM   4499 C CB   . VAL   B 1 35  ? 47.705 -18.142 -7.198  1.00 12.51 ?  35  VAL   B CB   1 
ATOM   4500 C CG1  . VAL   B 1 35  ? 48.607 -17.289 -6.294  1.00 13.36 ?  35  VAL   B CG1  1 
ATOM   4501 C CG2  . VAL   B 1 35  ? 47.840 -19.631 -6.847  1.00 13.24 ?  35  VAL   B CG2  1 
ATOM   4502 H H    . VAL   B 1 35  ? 46.490 -15.774 -7.292  1.00 14.10 ?  35  VAL   B H    1 
ATOM   4503 H HA   . VAL   B 1 35  ? 45.709 -18.353 -7.648  1.00 14.02 ?  35  VAL   B HA   1 
ATOM   4504 H HB   . VAL   B 1 35  ? 48.011 -18.035 -8.113  1.00 15.04 ?  35  VAL   B HB   1 
ATOM   4505 H HG11 . VAL   B 1 35  ? 49.531 -17.525 -6.469  1.00 16.06 ?  35  VAL   B HG11 1 
ATOM   4506 H HG12 . VAL   B 1 35  ? 48.453 -16.359 -6.494  1.00 16.06 ?  35  VAL   B HG12 1 
ATOM   4507 H HG13 . VAL   B 1 35  ? 48.386 -17.478 -5.369  1.00 16.06 ?  35  VAL   B HG13 1 
ATOM   4508 H HG21 . VAL   B 1 35  ? 48.759 -19.906 -6.967  1.00 15.91 ?  35  VAL   B HG21 1 
ATOM   4509 H HG22 . VAL   B 1 35  ? 47.573 -19.765 -5.921  1.00 15.91 ?  35  VAL   B HG22 1 
ATOM   4510 H HG23 . VAL   B 1 35  ? 47.260 -20.152 -7.430  1.00 15.91 ?  35  VAL   B HG23 1 
ATOM   4511 N N    . VAL   B 1 36  ? 44.957 -18.844 -5.385  1.00 11.51 ?  36  VAL   B N    1 
ATOM   4512 C CA   . VAL   B 1 36  ? 44.414 -19.043 -4.053  1.00 11.28 ?  36  VAL   B CA   1 
ATOM   4513 C C    . VAL   B 1 36  ? 45.418 -19.806 -3.195  1.00 11.18 ?  36  VAL   B C    1 
ATOM   4514 O O    . VAL   B 1 36  ? 45.962 -20.839 -3.615  1.00 11.99 ?  36  VAL   B O    1 
ATOM   4515 C CB   . VAL   B 1 36  ? 43.076 -19.801 -4.131  1.00 11.71 ?  36  VAL   B CB   1 
ATOM   4516 C CG1  . VAL   B 1 36  ? 42.570 -20.146 -2.743  1.00 12.40 ?  36  VAL   B CG1  1 
ATOM   4517 C CG2  . VAL   B 1 36  ? 42.053 -18.965 -4.883  1.00 12.25 ?  36  VAL   B CG2  1 
ATOM   4518 H H    . VAL   B 1 36  ? 44.780 -19.484 -5.930  1.00 13.84 ?  36  VAL   B H    1 
ATOM   4519 H HA   . VAL   B 1 36  ? 44.248 -18.185 -3.638  1.00 13.56 ?  36  VAL   B HA   1 
ATOM   4520 H HB   . VAL   B 1 36  ? 43.205 -20.631 -4.620  1.00 14.08 ?  36  VAL   B HB   1 
ATOM   4521 H HG11 . VAL   B 1 36  ? 41.627 -20.372 -2.802  1.00 14.91 ?  36  VAL   B HG11 1 
ATOM   4522 H HG12 . VAL   B 1 36  ? 43.070 -20.897 -2.398  1.00 14.91 ?  36  VAL   B HG12 1 
ATOM   4523 H HG13 . VAL   B 1 36  ? 42.684 -19.371 -2.169  1.00 14.91 ?  36  VAL   B HG13 1 
ATOM   4524 H HG21 . VAL   B 1 36  ? 41.210 -19.440 -4.903  1.00 14.73 ?  36  VAL   B HG21 1 
ATOM   4525 H HG22 . VAL   B 1 36  ? 41.947 -18.116 -4.426  1.00 14.73 ?  36  VAL   B HG22 1 
ATOM   4526 H HG23 . VAL   B 1 36  ? 42.372 -18.816 -5.787  1.00 14.73 ?  36  VAL   B HG23 1 
ATOM   4527 N N    . ASN   B 1 37  ? 45.630 -19.314 -1.976  1.00 11.36 ?  37  ASN   B N    1 
ATOM   4528 C CA   . ASN   B 1 37  ? 46.391 -20.028 -0.964  1.00 11.58 ?  37  ASN   B CA   1 
ATOM   4529 C C    . ASN   B 1 37  ? 45.447 -20.699 0.023   1.00 11.63 ?  37  ASN   B C    1 
ATOM   4530 O O    . ASN   B 1 37  ? 44.434 -20.120 0.427   1.00 11.88 ?  37  ASN   B O    1 
ATOM   4531 C CB   . ASN   B 1 37  ? 47.318 -19.081 -0.208  1.00 11.47 ?  37  ASN   B CB   1 
ATOM   4532 C CG   . ASN   B 1 37  ? 48.173 -19.795 0.805   1.00 12.20 ?  37  ASN   B CG   1 
ATOM   4533 O OD1  . ASN   B 1 37  ? 48.509 -20.974 0.633   1.00 12.83 ?  37  ASN   B OD1  1 
ATOM   4534 N ND2  . ASN   B 1 37  ? 48.523 -19.092 1.875   1.00 12.16 ?  37  ASN   B ND2  1 
ATOM   4535 H H    . ASN   B 1 37  ? 45.336 -18.549 -1.708  1.00 13.66 ?  37  ASN   B H    1 
ATOM   4536 H HA   . ASN   B 1 37  ? 46.930 -20.714 -1.385  1.00 13.92 ?  37  ASN   B HA   1 
ATOM   4537 H HB2  . ASN   B 1 37  ? 47.910 -18.645 -0.844  1.00 13.79 ?  37  ASN   B HB2  1 
ATOM   4538 H HB3  . ASN   B 1 37  ? 46.790 -18.418 0.260   1.00 13.79 ?  37  ASN   B HB3  1 
ATOM   4539 H HD21 . ASN   B 1 37  ? 49.028 -19.446 2.475   1.00 14.63 ?  37  ASN   B HD21 1 
ATOM   4540 H HD22 . ASN   B 1 37  ? 48.285 -18.273 1.953   1.00 14.63 ?  37  ASN   B HD22 1 
ATOM   4541 N N    . ALA   B 1 38  ? 45.798 -21.930 0.403   1.00 12.03 ?  38  ALA   B N    1 
ATOM   4542 C CA   . ALA   B 1 38  ? 45.135 -22.673 1.478   1.00 12.49 ?  38  ALA   B CA   1 
ATOM   4543 C C    . ALA   B 1 38  ? 45.720 -22.182 2.799   1.00 12.41 ?  38  ALA   B C    1 
ATOM   4544 O O    . ALA   B 1 38  ? 46.619 -22.788 3.392   1.00 13.00 ?  38  ALA   B O    1 
ATOM   4545 C CB   . ALA   B 1 38  ? 45.358 -24.168 1.300   1.00 13.31 ?  38  ALA   B CB   1 
ATOM   4546 H H    . ALA   B 1 38  ? 46.448 -22.370 0.050   1.00 14.46 ?  38  ALA   B H    1 
ATOM   4547 H HA   . ALA   B 1 38  ? 44.182 -22.489 1.469   1.00 15.01 ?  38  ALA   B HA   1 
ATOM   4548 H HB1  . ALA   B 1 38  ? 44.905 -24.642 2.023   1.00 16.01 ?  38  ALA   B HB1  1 
ATOM   4549 H HB2  . ALA   B 1 38  ? 44.985 -24.442 0.449   1.00 16.01 ?  38  ALA   B HB2  1 
ATOM   4550 H HB3  . ALA   B 1 38  ? 46.305 -24.355 1.329   1.00 16.01 ?  38  ALA   B HB3  1 
ATOM   4551 N N    . ALA   B 1 39  ? 45.201 -21.041 3.252   1.00 12.27 ?  39  ALA   B N    1 
ATOM   4552 C CA   . ALA   B 1 39  ? 45.751 -20.304 4.377   1.00 12.60 ?  39  ALA   B CA   1 
ATOM   4553 C C    . ALA   B 1 39  ? 45.135 -20.736 5.706   1.00 12.53 ?  39  ALA   B C    1 
ATOM   4554 O O    . ALA   B 1 39  ? 44.107 -21.411 5.761   1.00 13.63 ?  39  ALA   B O    1 
ATOM   4555 C CB   . ALA   B 1 39  ? 45.520 -18.805 4.173   1.00 12.97 ?  39  ALA   B CB   1 
ATOM   4556 H H    . ALA   B 1 39  ? 44.506 -20.666 2.911   1.00 14.76 ?  39  ALA   B H    1 
ATOM   4557 H HA   . ALA   B 1 39  ? 46.705 -20.459 4.425   1.00 15.14 ?  39  ALA   B HA   1 
ATOM   4558 H HB1  . ALA   B 1 39  ? 45.892 -18.320 4.928   1.00 15.59 ?  39  ALA   B HB1  1 
ATOM   4559 H HB2  . ALA   B 1 39  ? 45.962 -18.525 3.355   1.00 15.59 ?  39  ALA   B HB2  1 
ATOM   4560 H HB3  . ALA   B 1 39  ? 44.568 -18.634 4.109   1.00 15.59 ?  39  ALA   B HB3  1 
ATOM   4561 N N    . ASN   B 1 40  ? 45.775 -20.307 6.793   1.00 13.04 ?  40  ASN   B N    1 
ATOM   4562 C CA   . ASN   B 1 40  ? 45.213 -20.353 8.132   1.00 13.76 ?  40  ASN   B CA   1 
ATOM   4563 C C    . ASN   B 1 40  ? 45.038 -18.924 8.652   1.00 13.85 ?  40  ASN   B C    1 
ATOM   4564 O O    . ASN   B 1 40  ? 45.456 -17.948 8.020   1.00 13.74 ?  40  ASN   B O    1 
ATOM   4565 C CB   . ASN   B 1 40  ? 46.060 -21.226 9.073   1.00 14.59 ?  40  ASN   B CB   1 
ATOM   4566 C CG   . ASN   B 1 40  ? 47.517 -20.829 9.090   1.00 15.92 ?  40  ASN   B CG   1 
ATOM   4567 O OD1  . ASN   B 1 40  ? 47.842 -19.650 9.143   1.00 17.88 ?  40  ASN   B OD1  1 
ATOM   4568 N ND2  . ASN   B 1 40  ? 48.405 -21.811 9.056   1.00 16.04 ?  40  ASN   B ND2  1 
ATOM   4569 H H    . ASN   B 1 40  ? 46.569 -19.977 6.771   1.00 15.68 ?  40  ASN   B H    1 
ATOM   4570 H HA   . ASN   B 1 40  ? 44.330 -20.751 8.082   1.00 16.54 ?  40  ASN   B HA   1 
ATOM   4571 H HB2  . ASN   B 1 40  ? 45.712 -21.142 9.974   1.00 17.53 ?  40  ASN   B HB2  1 
ATOM   4572 H HB3  . ASN   B 1 40  ? 46.003 -22.147 8.778   1.00 17.53 ?  40  ASN   B HB3  1 
ATOM   4573 H HD21 . ASN   B 1 40  ? 49.247 -21.635 9.067   1.00 19.28 ?  40  ASN   B HD21 1 
ATOM   4574 H HD22 . ASN   B 1 40  ? 48.137 -22.629 9.024   1.00 19.28 ?  40  ASN   B HD22 1 
ATOM   4575 N N    . VAL   B 1 41  ? 44.398 -18.797 9.818   1.00 14.26 ?  41  VAL   B N    1 
ATOM   4576 C CA   . VAL   B 1 41  ? 43.938 -17.479 10.263  1.00 14.98 ?  41  VAL   B CA   1 
ATOM   4577 C C    . VAL   B 1 41  ? 45.088 -16.524 10.556  1.00 14.87 ?  41  VAL   B C    1 
ATOM   4578 O O    . VAL   B 1 41  ? 44.909 -15.305 10.459  1.00 15.32 ?  41  VAL   B O    1 
ATOM   4579 C CB   . VAL   B 1 41  ? 42.950 -17.556 11.446  1.00 16.36 ?  41  VAL   B CB   1 
ATOM   4580 C CG1  . VAL   B 1 41  ? 41.648 -18.231 11.026  1.00 16.51 ?  41  VAL   B CG1  1 
ATOM   4581 C CG2  . VAL   B 1 41  ? 43.576 -18.248 12.646  1.00 17.71 ?  41  VAL   B CG2  1 
ATOM   4582 H H    . VAL   B 1 41  ? 44.223 -19.441 10.353  1.00 17.14 ?  41  VAL   B H    1 
ATOM   4583 H HA   . VAL   B 1 41  ? 43.443 -17.084 9.532   1.00 18.00 ?  41  VAL   B HA   1 
ATOM   4584 H HB   . VAL   B 1 41  ? 42.725 -16.654 11.721  1.00 19.67 ?  41  VAL   B HB   1 
ATOM   4585 H HG11 . VAL   B 1 41  ? 41.034 -18.231 11.777  1.00 19.84 ?  41  VAL   B HG11 1 
ATOM   4586 H HG12 . VAL   B 1 41  ? 41.264 -17.740 10.283  1.00 19.84 ?  41  VAL   B HG12 1 
ATOM   4587 H HG13 . VAL   B 1 41  ? 41.840 -19.144 10.756  1.00 19.84 ?  41  VAL   B HG13 1 
ATOM   4588 H HG21 . VAL   B 1 41  ? 42.932 -18.271 13.373  1.00 21.28 ?  41  VAL   B HG21 1 
ATOM   4589 H HG22 . VAL   B 1 41  ? 43.822 -19.154 12.399  1.00 21.28 ?  41  VAL   B HG22 1 
ATOM   4590 H HG23 . VAL   B 1 41  ? 44.364 -17.755 12.921  1.00 21.28 ?  41  VAL   B HG23 1 
ATOM   4591 N N    . TYR   B 1 42  ? 46.260 -17.034 10.937  1.00 15.11 ?  42  TYR   B N    1 
ATOM   4592 C CA   . TYR   B 1 42  ? 47.410 -16.180 11.199  1.00 15.59 ?  42  TYR   B CA   1 
ATOM   4593 C C    . TYR   B 1 42  ? 48.377 -16.120 10.021  1.00 14.82 ?  42  TYR   B C    1 
ATOM   4594 O O    . TYR   B 1 42  ? 49.469 -15.555 10.150  1.00 15.81 ?  42  TYR   B O    1 
ATOM   4595 C CB   . TYR   B 1 42  ? 48.103 -16.581 12.507  1.00 17.60 ?  42  TYR   B CB   1 
ATOM   4596 C CG   . TYR   B 1 42  ? 47.471 -15.929 13.732  1.00 17.97 ?  42  TYR   B CG   1 
ATOM   4597 C CD1  . TYR   B 1 42  ? 47.684 -14.583 14.010  1.00 17.38 ?  42  TYR   B CD1  1 
ATOM   4598 C CD2  . TYR   B 1 42  ? 46.665 -16.653 14.598  1.00 19.47 ?  42  TYR   B CD2  1 
ATOM   4599 C CE1  . TYR   B 1 42  ? 47.109 -13.977 15.114  1.00 18.38 ?  42  TYR   B CE1  1 
ATOM   4600 C CE2  . TYR   B 1 42  ? 46.094 -16.061 15.707  1.00 19.81 ?  42  TYR   B CE2  1 
ATOM   4601 C CZ   . TYR   B 1 42  ? 46.312 -14.720 15.960  1.00 20.32 ?  42  TYR   B CZ   1 
ATOM   4602 O OH   . TYR   B 1 42  ? 45.739 -14.127 17.065  1.00 23.10 ?  42  TYR   B OH   1 
ATOM   4603 H H    . TYR   B 1 42  ? 46.410 -17.879 11.036  1.00 18.16 ?  42  TYR   B H    1 
ATOM   4604 H HA   . TYR   B 1 42  ? 47.078 -15.281 11.328  1.00 18.74 ?  42  TYR   B HA   1 
ATOM   4605 H HB2  . TYR   B 1 42  ? 48.044 -17.542 12.616  1.00 21.15 ?  42  TYR   B HB2  1 
ATOM   4606 H HB3  . TYR   B 1 42  ? 49.030 -16.305 12.466  1.00 21.15 ?  42  TYR   B HB3  1 
ATOM   4607 H HD1  . TYR   B 1 42  ? 48.219 -14.079 13.435  1.00 20.88 ?  42  TYR   B HD1  1 
ATOM   4608 H HD2  . TYR   B 1 42  ? 46.508 -17.555 14.427  1.00 23.39 ?  42  TYR   B HD2  1 
ATOM   4609 H HE1  . TYR   B 1 42  ? 47.263 -13.076 15.284  1.00 22.09 ?  42  TYR   B HE1  1 
ATOM   4610 H HE2  . TYR   B 1 42  ? 45.552 -16.559 16.274  1.00 23.80 ?  42  TYR   B HE2  1 
ATOM   4611 H HH   . TYR   B 1 42  ? 45.958 -13.319 17.098  1.00 27.75 ?  42  TYR   B HH   1 
ATOM   4612 N N    . LEU   B 1 43  ? 47.976 -16.637 8.864   1.00 13.78 ?  43  LEU   B N    1 
ATOM   4613 C CA   . LEU   B 1 43  ? 48.786 -16.580 7.651   1.00 13.20 ?  43  LEU   B CA   1 
ATOM   4614 C C    . LEU   B 1 43  ? 50.198 -17.091 7.912   1.00 13.47 ?  43  LEU   B C    1 
ATOM   4615 O O    . LEU   B 1 43  ? 51.183 -16.505 7.464   1.00 14.22 ?  43  LEU   B O    1 
ATOM   4616 C CB   . LEU   B 1 43  ? 48.804 -15.179 7.033   1.00 13.35 ?  43  LEU   B CB   1 
ATOM   4617 C CG   . LEU   B 1 43  ? 47.448 -14.563 6.664   1.00 13.63 ?  43  LEU   B CG   1 
ATOM   4618 C CD1  . LEU   B 1 43  ? 47.665 -13.175 6.055   1.00 14.91 ?  43  LEU   B CD1  1 
ATOM   4619 C CD2  . LEU   B 1 43  ? 46.660 -15.456 5.714   1.00 13.84 ?  43  LEU   B CD2  1 
ATOM   4620 H H    . LEU   B 1 43  ? 47.226 -17.046 8.753   1.00 16.57 ?  43  LEU   B H    1 
ATOM   4621 H HA   . LEU   B 1 43  ? 48.384 -17.174 6.995   1.00 15.87 ?  43  LEU   B HA   1 
ATOM   4622 H HB2  . LEU   B 1 43  ? 49.232 -14.577 7.660   1.00 16.05 ?  43  LEU   B HB2  1 
ATOM   4623 H HB3  . LEU   B 1 43  ? 49.328 -15.218 6.218   1.00 16.05 ?  43  LEU   B HB3  1 
ATOM   4624 H HG   . LEU   B 1 43  ? 46.924 -14.448 7.472   1.00 16.38 ?  43  LEU   B HG   1 
ATOM   4625 H HD11 . LEU   B 1 43  ? 46.803 -12.790 5.827   1.00 17.92 ?  43  LEU   B HD11 1 
ATOM   4626 H HD12 . LEU   B 1 43  ? 48.115 -12.611 6.706   1.00 17.92 ?  43  LEU   B HD12 1 
ATOM   4627 H HD13 . LEU   B 1 43  ? 48.211 -13.260 5.259   1.00 17.92 ?  43  LEU   B HD13 1 
ATOM   4628 H HD21 . LEU   B 1 43  ? 45.853 -14.990 5.437   1.00 16.63 ?  43  LEU   B HD21 1 
ATOM   4629 H HD22 . LEU   B 1 43  ? 47.206 -15.658 4.940   1.00 16.63 ?  43  LEU   B HD22 1 
ATOM   4630 H HD23 . LEU   B 1 43  ? 46.422 -16.276 6.176   1.00 16.63 ?  43  LEU   B HD23 1 
ATOM   4631 N N    . LYS   B 1 44  ? 50.293 -18.207 8.633   1.00 13.77 ?  44  LYS   B N    1 
ATOM   4632 C CA   . LYS   B 1 44  ? 51.556 -18.892 8.873   1.00 14.27 ?  44  LYS   B CA   1 
ATOM   4633 C C    . LYS   B 1 44  ? 51.669 -20.010 7.848   1.00 13.89 ?  44  LYS   B C    1 
ATOM   4634 O O    . LYS   B 1 44  ? 50.972 -21.025 7.941   1.00 15.15 ?  44  LYS   B O    1 
ATOM   4635 C CB   . LYS   B 1 44  ? 51.615 -19.411 10.309  1.00 16.05 ?  44  LYS   B CB   1 
ATOM   4636 C CG   . LYS   B 1 44  ? 51.805 -18.307 11.340  1.00 18.79 ?  44  LYS   B CG   1 
ATOM   4637 C CD   . LYS   B 1 44  ? 53.013 -17.443 10.970  1.00 21.84 ?  44  LYS   B CD   1 
ATOM   4638 C CE   . LYS   B 1 44  ? 53.374 -16.453 12.044  1.00 24.48 ?  44  LYS   B CE   1 
ATOM   4639 N NZ   . LYS   B 1 44  ? 54.612 -15.698 11.726  1.00 25.67 ?  44  LYS   B NZ   1 
ATOM   4640 H H    . LYS   B 1 44  ? 49.619 -18.593 8.998   1.00 16.56 ?  44  LYS   B H    1 
ATOM   4641 H HA   . LYS   B 1 44  ? 52.292 -18.282 8.712   1.00 17.15 ?  44  LYS   B HA   1 
ATOM   4642 H HB2  . LYS   B 1 44  ? 50.775 -19.866 10.510  1.00 19.29 ?  44  LYS   B HB2  1 
ATOM   4643 H HB3  . LYS   B 1 44  ? 52.350 -20.034 10.391  1.00 19.29 ?  44  LYS   B HB3  1 
ATOM   4644 H HG2  . LYS   B 1 44  ? 51.017 -17.747 11.366  1.00 22.58 ?  44  LYS   B HG2  1 
ATOM   4645 H HG3  . LYS   B 1 44  ? 51.968 -18.708 12.212  1.00 22.58 ?  44  LYS   B HG3  1 
ATOM   4646 H HD2  . LYS   B 1 44  ? 53.775 -18.028 10.802  1.00 26.23 ?  44  LYS   B HD2  1 
ATOM   4647 H HD3  . LYS   B 1 44  ? 52.803 -16.938 10.169  1.00 26.23 ?  44  LYS   B HD3  1 
ATOM   4648 H HE2  . LYS   B 1 44  ? 52.647 -15.820 12.136  1.00 29.41 ?  44  LYS   B HE2  1 
ATOM   4649 H HE3  . LYS   B 1 44  ? 53.519 -16.931 12.870  1.00 29.41 ?  44  LYS   B HE3  1 
ATOM   4650 H HZ1  . LYS   B 1 44  ? 54.784 -15.113 12.375  1.00 30.83 ?  44  LYS   B HZ1  1 
ATOM   4651 H HZ2  . LYS   B 1 44  ? 55.300 -16.254 11.647  1.00 30.83 ?  44  LYS   B HZ2  1 
ATOM   4652 H HZ3  . LYS   B 1 44  ? 54.512 -15.252 10.959  1.00 30.83 ?  44  LYS   B HZ3  1 
ATOM   4653 N N    . HIS   B 1 45  ? 52.523 -19.801 6.847   1.00 13.83 ?  45  HIS   B N    1 
ATOM   4654 C CA   . HIS   B 1 45  ? 52.547 -20.639 5.648   1.00 13.90 ?  45  HIS   B CA   1 
ATOM   4655 C C    . HIS   B 1 45  ? 53.565 -21.764 5.820   1.00 16.02 ?  45  HIS   B C    1 
ATOM   4656 O O    . HIS   B 1 45  ? 54.627 -21.794 5.204   1.00 18.16 ?  45  HIS   B O    1 
ATOM   4657 C CB   . HIS   B 1 45  ? 52.858 -19.790 4.426   1.00 13.78 ?  45  HIS   B CB   1 
ATOM   4658 C CG   . HIS   B 1 45  ? 51.993 -18.582 4.308   1.00 13.78 ?  45  HIS   B CG   1 
ATOM   4659 N ND1  . HIS   B 1 45  ? 50.616 -18.653 4.266   1.00 13.78 ?  45  HIS   B ND1  1 
ATOM   4660 C CD2  . HIS   B 1 45  ? 52.315 -17.270 4.233   1.00 14.14 ?  45  HIS   B CD2  1 
ATOM   4661 C CE1  . HIS   B 1 45  ? 50.133 -17.427 4.162   1.00 13.45 ?  45  HIS   B CE1  1 
ATOM   4662 N NE2  . HIS   B 1 45  ? 51.140 -16.570 4.140   1.00 13.74 ?  45  HIS   B NE2  1 
ATOM   4663 H H    . HIS   B 1 45  ? 53.096 -19.158 6.829   1.00 16.62 ?  45  HIS   B H    1 
ATOM   4664 H HA   . HIS   B 1 45  ? 51.667 -21.036 5.522   1.00 16.71 ?  45  HIS   B HA   1 
ATOM   4665 H HB2  . HIS   B 1 45  ? 53.778 -19.496 4.475   1.00 16.56 ?  45  HIS   B HB2  1 
ATOM   4666 H HB3  . HIS   B 1 45  ? 52.726 -20.332 3.629   1.00 16.56 ?  45  HIS   B HB3  1 
ATOM   4667 H HD2  . HIS   B 1 45  ? 53.174 -16.910 4.246   1.00 17.00 ?  45  HIS   B HD2  1 
ATOM   4668 H HE1  . HIS   B 1 45  ? 49.233 -17.203 4.105   1.00 16.17 ?  45  HIS   B HE1  1 
ATOM   4669 H HE2  . HIS   B 1 45  ? 51.070 -15.715 4.082   1.00 16.52 ?  45  HIS   B HE2  1 
ATOM   4670 N N    A GLY   B 1 46  ? 53.192 -22.724 6.662   0.60 16.87 ?  46  GLY   B N    1 
ATOM   4671 N N    B GLY   B 1 46  ? 53.205 -22.711 6.679   0.40 16.79 ?  46  GLY   B N    1 
ATOM   4672 C CA   A GLY   B 1 46  ? 54.110 -23.771 7.069   0.60 18.29 ?  46  GLY   B CA   1 
ATOM   4673 C CA   B GLY   B 1 46  ? 54.123 -23.772 7.036   0.40 17.88 ?  46  GLY   B CA   1 
ATOM   4674 C C    A GLY   B 1 46  ? 54.178 -25.001 6.184   0.60 19.42 ?  46  GLY   B C    1 
ATOM   4675 C C    B GLY   B 1 46  ? 54.170 -24.922 6.048   0.40 18.78 ?  46  GLY   B C    1 
ATOM   4676 O O    A GLY   B 1 46  ? 55.270 -25.463 5.840   0.60 21.94 ?  46  GLY   B O    1 
ATOM   4677 O O    B GLY   B 1 46  ? 55.220 -25.220 5.469   0.40 20.03 ?  46  GLY   B O    1 
ATOM   4678 H H    A GLY   B 1 46  ? 52.411 -22.776 7.026   0.60 20.28 ?  46  GLY   B H    1 
ATOM   4679 H H    B GLY   B 1 46  ? 52.436 -22.750 7.071   0.40 20.18 ?  46  GLY   B H    1 
ATOM   4680 H HA2  A GLY   B 1 46  ? 55.002 -23.395 7.125   0.60 21.98 ?  46  GLY   B HA2  1 
ATOM   4681 H HA2  B GLY   B 1 46  ? 55.015 -23.400 7.112   0.40 21.49 ?  46  GLY   B HA2  1 
ATOM   4682 H HA3  A GLY   B 1 46  ? 53.860 -24.075 7.954   0.60 21.98 ?  46  GLY   B HA3  1 
ATOM   4683 H HA3  B GLY   B 1 46  ? 53.871 -24.121 7.907   0.40 21.49 ?  46  GLY   B HA3  1 
ATOM   4684 N N    . GLY   B 1 47  ? 53.026 -25.568 5.830   1.00 18.88 ?  47  GLY   B N    1 
ATOM   4685 C CA   . GLY   B 1 47  ? 52.981 -26.842 5.138   1.00 17.15 ?  47  GLY   B CA   1 
ATOM   4686 C C    . GLY   B 1 47  ? 52.050 -26.831 3.940   1.00 15.21 ?  47  GLY   B C    1 
ATOM   4687 O O    . GLY   B 1 47  ? 51.398 -25.828 3.644   1.00 15.08 ?  47  GLY   B O    1 
ATOM   4688 H H    A GLY   B 1 47  ? 52.253 -25.241 6.008   0.60 22.68 ?  47  GLY   B H    1 
ATOM   4689 H H    B GLY   B 1 47  ? 52.256 -25.283 6.081   0.40 22.68 ?  47  GLY   B H    1 
ATOM   4690 H HA2  . GLY   B 1 47  ? 53.869 -27.081 4.831   1.00 20.61 ?  47  GLY   B HA2  1 
ATOM   4691 H HA3  . GLY   B 1 47  ? 52.678 -27.528 5.754   1.00 20.61 ?  47  GLY   B HA3  1 
ATOM   4692 N N    . GLY   B 1 48  ? 52.006 -27.978 3.260   1.00 14.66 ?  48  GLY   B N    1 
ATOM   4693 C CA   . GLY   B 1 48  ? 51.088 -28.136 2.147   1.00 14.38 ?  48  GLY   B CA   1 
ATOM   4694 C C    . GLY   B 1 48  ? 51.225 -27.028 1.128   1.00 13.78 ?  48  GLY   B C    1 
ATOM   4695 O O    . GLY   B 1 48  ? 52.327 -26.558 0.828   1.00 14.36 ?  48  GLY   B O    1 
ATOM   4696 H H    . GLY   B 1 48  ? 52.500 -28.659 3.418   1.00 17.62 ?  48  GLY   B H    1 
ATOM   4697 H HA2  . GLY   B 1 48  ? 51.258 -28.987 1.706   1.00 17.28 ?  48  GLY   B HA2  1 
ATOM   4698 H HA3  . GLY   B 1 48  ? 50.175 -28.140 2.475   1.00 17.28 ?  48  GLY   B HA3  1 
ATOM   4699 N N    . VAL   B 1 49  ? 50.080 -26.599 0.592   1.00 13.66 ?  49  VAL   B N    1 
ATOM   4700 C CA   . VAL   B 1 49  ? 50.061 -25.581 -0.457  1.00 13.77 ?  49  VAL   B CA   1 
ATOM   4701 C C    . VAL   B 1 49  ? 50.718 -24.289 0.022   1.00 12.95 ?  49  VAL   B C    1 
ATOM   4702 O O    . VAL   B 1 49  ? 51.503 -23.669 -0.704  1.00 13.37 ?  49  VAL   B O    1 
ATOM   4703 C CB   . VAL   B 1 49  ? 48.616 -25.331 -0.933  1.00 14.75 ?  49  VAL   B CB   1 
ATOM   4704 C CG1  . VAL   B 1 49  ? 48.539 -24.088 -1.815  1.00 15.05 ?  49  VAL   B CG1  1 
ATOM   4705 C CG2  . VAL   B 1 49  ? 48.068 -26.548 -1.676  1.00 16.22 ?  49  VAL   B CG2  1 
ATOM   4706 H H    . VAL   B 1 49  ? 49.295 -26.875 0.825   1.00 16.43 ?  49  VAL   B H    1 
ATOM   4707 H HA   . VAL   B 1 49  ? 50.564 -25.905 -1.217  1.00 16.56 ?  49  VAL   B HA   1 
ATOM   4708 H HB   . VAL   B 1 49  ? 48.051 -25.179 -0.162  1.00 17.73 ?  49  VAL   B HB   1 
ATOM   4709 H HG11 . VAL   B 1 49  ? 47.709 -24.109 -2.318  1.00 18.09 ?  49  VAL   B HG11 1 
ATOM   4710 H HG12 . VAL   B 1 49  ? 48.561 -23.297 -1.252  1.00 18.09 ?  49  VAL   B HG12 1 
ATOM   4711 H HG13 . VAL   B 1 49  ? 49.292 -24.085 -2.425  1.00 18.09 ?  49  VAL   B HG13 1 
ATOM   4712 H HG21 . VAL   B 1 49  ? 47.157 -26.364 -1.958  1.00 19.49 ?  49  VAL   B HG21 1 
ATOM   4713 H HG22 . VAL   B 1 49  ? 48.624 -26.722 -2.453  1.00 19.49 ?  49  VAL   B HG22 1 
ATOM   4714 H HG23 . VAL   B 1 49  ? 48.081 -27.313 -1.081  1.00 19.49 ?  49  VAL   B HG23 1 
ATOM   4715 N N    . ALA   B 1 50  ? 50.371 -23.837 1.226   1.00 12.72 ?  50  ALA   B N    1 
ATOM   4716 C CA   . ALA   B 1 50  ? 50.890 -22.556 1.697   1.00 12.66 ?  50  ALA   B CA   1 
ATOM   4717 C C    . ALA   B 1 50  ? 52.409 -22.586 1.811   1.00 13.06 ?  50  ALA   B C    1 
ATOM   4718 O O    . ALA   B 1 50  ? 53.093 -21.622 1.441   1.00 12.73 ?  50  ALA   B O    1 
ATOM   4719 C CB   . ALA   B 1 50  ? 50.261 -22.203 3.041   1.00 12.98 ?  50  ALA   B CB   1 
ATOM   4720 H H    . ALA   B 1 50  ? 49.844 -24.237 1.774   1.00 15.29 ?  50  ALA   B H    1 
ATOM   4721 H HA   . ALA   B 1 50  ? 50.658 -21.863 1.064   1.00 15.22 ?  50  ALA   B HA   1 
ATOM   4722 H HB1  . ALA   B 1 50  ? 50.617 -21.349 3.341   1.00 15.60 ?  50  ALA   B HB1  1 
ATOM   4723 H HB2  . ALA   B 1 50  ? 49.299 -22.136 2.930   1.00 15.60 ?  50  ALA   B HB2  1 
ATOM   4724 H HB3  . ALA   B 1 50  ? 50.475 -22.894 3.684   1.00 15.60 ?  50  ALA   B HB3  1 
ATOM   4725 N N    . GLY   B 1 51  ? 52.961 -23.682 2.327   1.00 13.25 ?  51  GLY   B N    1 
ATOM   4726 C CA   . GLY   B 1 51  ? 54.406 -23.781 2.403   1.00 14.18 ?  51  GLY   B CA   1 
ATOM   4727 C C    . GLY   B 1 51  ? 55.056 -23.735 1.037   1.00 13.87 ?  51  GLY   B C    1 
ATOM   4728 O O    . GLY   B 1 51  ? 56.098 -23.098 0.857   1.00 14.76 ?  51  GLY   B O    1 
ATOM   4729 H H    . GLY   B 1 51  ? 52.534 -24.364 2.627   1.00 15.93 ?  51  GLY   B H    1 
ATOM   4730 H HA2  . GLY   B 1 51  ? 54.759 -23.048 2.928   1.00 17.04 ?  51  GLY   B HA2  1 
ATOM   4731 H HA3  . GLY   B 1 51  ? 54.655 -24.616 2.832   1.00 17.04 ?  51  GLY   B HA3  1 
ATOM   4732 N N    . ALA   B 1 52  ? 54.451 -24.405 0.055   1.00 13.20 ?  52  ALA   B N    1 
ATOM   4733 C CA   . ALA   B 1 52  ? 55.007 -24.420 -1.290  1.00 13.60 ?  52  ALA   B CA   1 
ATOM   4734 C C    . ALA   B 1 52  ? 54.928 -23.044 -1.941  1.00 13.06 ?  52  ALA   B C    1 
ATOM   4735 O O    . ALA   B 1 52  ? 55.897 -22.593 -2.568  1.00 13.64 ?  52  ALA   B O    1 
ATOM   4736 C CB   . ALA   B 1 52  ? 54.293 -25.462 -2.145  1.00 14.26 ?  52  ALA   B CB   1 
ATOM   4737 H H    . ALA   B 1 52  ? 53.714 -24.845 0.139   1.00 15.86 ?  52  ALA   B H    1 
ATOM   4738 H HA   . ALA   B 1 52  ? 55.939 -24.669 -1.239  1.00 16.34 ?  52  ALA   B HA   1 
ATOM   4739 H HB1  . ALA   B 1 52  ? 54.677 -25.462 -3.037  1.00 17.14 ?  52  ALA   B HB1  1 
ATOM   4740 H HB2  . ALA   B 1 52  ? 54.413 -26.339 -1.738  1.00 17.14 ?  52  ALA   B HB2  1 
ATOM   4741 H HB3  . ALA   B 1 52  ? 53.349 -25.249 -2.192  1.00 17.14 ?  52  ALA   B HB3  1 
ATOM   4742 N N    . LEU   B 1 53  ? 53.785 -22.365 -1.824  1.00 12.57 ?  53  LEU   B N    1 
ATOM   4743 C CA   . LEU   B 1 53  ? 53.674 -21.025 -2.396  1.00 12.49 ?  53  LEU   B CA   1 
ATOM   4744 C C    . LEU   B 1 53  ? 54.684 -20.082 -1.753  1.00 12.27 ?  53  LEU   B C    1 
ATOM   4745 O O    . LEU   B 1 53  ? 55.389 -19.338 -2.447  1.00 13.24 ?  53  LEU   B O    1 
ATOM   4746 C CB   . LEU   B 1 53  ? 52.250 -20.482 -2.233  1.00 13.36 ?  53  LEU   B CB   1 
ATOM   4747 C CG   . LEU   B 1 53  ? 51.115 -21.203 -2.969  1.00 13.86 ?  53  LEU   B CG   1 
ATOM   4748 C CD1  . LEU   B 1 53  ? 49.770 -20.605 -2.617  1.00 15.01 ?  53  LEU   B CD1  1 
ATOM   4749 C CD2  . LEU   B 1 53  ? 51.324 -21.189 -4.477  1.00 15.44 ?  53  LEU   B CD2  1 
ATOM   4750 H H    . LEU   B 1 53  ? 53.081 -22.646 -1.427  1.00 15.11 ?  53  LEU   B H    1 
ATOM   4751 H HA   . LEU   B 1 53  ? 53.875 -21.069 -3.347  1.00 15.02 ?  53  LEU   B HA   1 
ATOM   4752 H HB2  . LEU   B 1 53  ? 52.034 -20.504 -1.289  1.00 16.06 ?  53  LEU   B HB2  1 
ATOM   4753 H HB3  . LEU   B 1 53  ? 52.247 -19.562 -2.538  1.00 16.06 ?  53  LEU   B HB3  1 
ATOM   4754 H HG   . LEU   B 1 53  ? 51.102 -22.130 -2.688  1.00 16.66 ?  53  LEU   B HG   1 
ATOM   4755 H HD11 . LEU   B 1 53  ? 49.074 -21.089 -3.100  1.00 18.04 ?  53  LEU   B HD11 1 
ATOM   4756 H HD12 . LEU   B 1 53  ? 49.624 -20.697 -1.662  1.00 18.04 ?  53  LEU   B HD12 1 
ATOM   4757 H HD13 . LEU   B 1 53  ? 49.758 -19.673 -2.870  1.00 18.04 ?  53  LEU   B HD13 1 
ATOM   4758 H HD21 . LEU   B 1 53  ? 50.633 -21.727 -4.897  1.00 18.56 ?  53  LEU   B HD21 1 
ATOM   4759 H HD22 . LEU   B 1 53  ? 51.267 -20.276 -4.797  1.00 18.56 ?  53  LEU   B HD22 1 
ATOM   4760 H HD23 . LEU   B 1 53  ? 52.196 -21.561 -4.683  1.00 18.56 ?  53  LEU   B HD23 1 
ATOM   4761 N N    . ASN   B 1 54  ? 54.771 -20.098 -0.424  1.00 12.09 ?  54  ASN   B N    1 
ATOM   4762 C CA   . ASN   B 1 54  ? 55.692 -19.191 0.247   1.00 12.95 ?  54  ASN   B CA   1 
ATOM   4763 C C    . ASN   B 1 54  ? 57.134 -19.476 -0.152  1.00 13.77 ?  54  ASN   B C    1 
ATOM   4764 O O    . ASN   B 1 54  ? 57.914 -18.543 -0.395  1.00 14.09 ?  54  ASN   B O    1 
ATOM   4765 C CB   . ASN   B 1 54  ? 55.533 -19.273 1.757   1.00 13.78 ?  54  ASN   B CB   1 
ATOM   4766 C CG   . ASN   B 1 54  ? 56.508 -18.360 2.472   1.00 14.11 ?  54  ASN   B CG   1 
ATOM   4767 O OD1  . ASN   B 1 54  ? 56.539 -17.151 2.217   1.00 14.64 ?  54  ASN   B OD1  1 
ATOM   4768 N ND2  . ASN   B 1 54  ? 57.334 -18.932 3.342   1.00 15.87 ?  54  ASN   B ND2  1 
ATOM   4769 H H    . ASN   B 1 54  ? 54.323 -20.617 0.094   1.00 14.54 ?  54  ASN   B H    1 
ATOM   4770 H HA   . ASN   B 1 54  ? 55.485 -18.285 -0.024  1.00 15.57 ?  54  ASN   B HA   1 
ATOM   4771 H HB2  . ASN   B 1 54  ? 54.633 -19.005 2.000   1.00 16.56 ?  54  ASN   B HB2  1 
ATOM   4772 H HB3  . ASN   B 1 54  ? 55.701 -20.183 2.049   1.00 16.56 ?  54  ASN   B HB3  1 
ATOM   4773 H HD21 . ASN   B 1 54  ? 57.903 -18.454 3.774   1.00 19.07 ?  54  ASN   B HD21 1 
ATOM   4774 H HD22 . ASN   B 1 54  ? 57.285 -19.779 3.491   1.00 19.07 ?  54  ASN   B HD22 1 
ATOM   4775 N N    . LYS   B 1 55  ? 57.520 -20.756 -0.207  1.00 14.35 ?  55  LYS   B N    1 
ATOM   4776 C CA   . LYS   B 1 55  ? 58.878 -21.097 -0.619  1.00 15.25 ?  55  LYS   B CA   1 
ATOM   4777 C C    . LYS   B 1 55  ? 59.173 -20.566 -2.017  1.00 15.03 ?  55  LYS   B C    1 
ATOM   4778 O O    . LYS   B 1 55  ? 60.272 -20.061 -2.278  1.00 15.65 ?  55  LYS   B O    1 
ATOM   4779 C CB   . LYS   B 1 55  ? 59.074 -22.612 -0.554  1.00 17.26 ?  55  LYS   B CB   1 
ATOM   4780 C CG   . LYS   B 1 55  ? 60.449 -23.079 -0.979  1.00 20.81 ?  55  LYS   B CG   1 
ATOM   4781 C CD   . LYS   B 1 55  ? 60.606 -24.577 -0.808  1.00 24.03 ?  55  LYS   B CD   1 
ATOM   4782 C CE   . LYS   B 1 55  ? 60.645 -24.984 0.664   1.00 27.09 ?  55  LYS   B CE   1 
ATOM   4783 N NZ   . LYS   B 1 55  ? 61.051 -26.401 0.837   1.00 28.77 ?  55  LYS   B NZ   1 
ATOM   4784 H H    . LYS   B 1 55  ? 57.015 -21.428 -0.017  1.00 17.25 ?  55  LYS   B H    1 
ATOM   4785 H HA   . LYS   B 1 55  ? 59.502 -20.686 -0.003  1.00 18.33 ?  55  LYS   B HA   1 
ATOM   4786 H HB2  . LYS   B 1 55  ? 58.931 -22.900 0.364   1.00 20.74 ?  55  LYS   B HB2  1 
ATOM   4787 H HB3  . LYS   B 1 55  ? 58.425 -23.037 -1.133  1.00 20.74 ?  55  LYS   B HB3  1 
ATOM   4788 H HG2  . LYS   B 1 55  ? 60.585 -22.867 -1.915  1.00 25.00 ?  55  LYS   B HG2  1 
ATOM   4789 H HG3  . LYS   B 1 55  ? 61.120 -22.639 -0.433  1.00 25.00 ?  55  LYS   B HG3  1 
ATOM   4790 H HD2  . LYS   B 1 55  ? 59.856 -25.030 -1.225  1.00 28.86 ?  55  LYS   B HD2  1 
ATOM   4791 H HD3  . LYS   B 1 55  ? 61.439 -24.863 -1.218  1.00 28.86 ?  55  LYS   B HD3  1 
ATOM   4792 H HE2  . LYS   B 1 55  ? 61.282 -24.418 1.131   1.00 32.54 ?  55  LYS   B HE2  1 
ATOM   4793 H HE3  . LYS   B 1 55  ? 59.758 -24.868 1.046   1.00 32.54 ?  55  LYS   B HE3  1 
ATOM   4794 H HZ1  . LYS   B 1 55  ? 61.027 -26.617 1.700   1.00 34.55 ?  55  LYS   B HZ1  1 
ATOM   4795 H HZ2  . LYS   B 1 55  ? 60.493 -26.930 0.390   1.00 34.55 ?  55  LYS   B HZ2  1 
ATOM   4796 H HZ3  . LYS   B 1 55  ? 61.875 -26.518 0.529   1.00 34.55 ?  55  LYS   B HZ3  1 
ATOM   4797 N N    . ALA   B 1 56  ? 58.198 -20.651 -2.927  1.00 14.52 ?  56  ALA   B N    1 
ATOM   4798 C CA   . ALA   B 1 56  ? 58.422 -20.156 -4.280  1.00 15.40 ?  56  ALA   B CA   1 
ATOM   4799 C C    . ALA   B 1 56  ? 58.701 -18.659 -4.285  1.00 15.17 ?  56  ALA   B C    1 
ATOM   4800 O O    . ALA   B 1 56  ? 59.428 -18.166 -5.160  1.00 16.03 ?  56  ALA   B O    1 
ATOM   4801 C CB   . ALA   B 1 56  ? 57.224 -20.492 -5.169  1.00 16.03 ?  56  ALA   B CB   1 
ATOM   4802 H H    . ALA   B 1 56  ? 57.412 -20.976 -2.787  1.00 17.45 ?  56  ALA   B H    1 
ATOM   4803 H HA   . ALA   B 1 56  ? 59.199 -20.598 -4.647  1.00 18.51 ?  56  ALA   B HA   1 
ATOM   4804 H HB1  . ALA   B 1 56  ? 57.396 -20.158 -6.065  1.00 19.26 ?  56  ALA   B HB1  1 
ATOM   4805 H HB2  . ALA   B 1 56  ? 57.111 -21.454 -5.191  1.00 19.26 ?  56  ALA   B HB2  1 
ATOM   4806 H HB3  . ALA   B 1 56  ? 56.431 -20.071 -4.806  1.00 19.26 ?  56  ALA   B HB3  1 
ATOM   4807 N N    . THR   B 1 57  ? 58.133 -17.920 -3.330  1.00 14.85 ?  57  THR   B N    1 
ATOM   4808 C CA   . THR   B 1 57  ? 58.373 -16.484 -3.222  1.00 15.06 ?  57  THR   B CA   1 
ATOM   4809 C C    . THR   B 1 57  ? 59.624 -16.153 -2.415  1.00 15.73 ?  57  THR   B C    1 
ATOM   4810 O O    . THR   B 1 57  ? 59.862 -14.973 -2.117  1.00 16.40 ?  57  THR   B O    1 
ATOM   4811 C CB   . THR   B 1 57  ? 57.173 -15.748 -2.594  1.00 14.30 ?  57  THR   B CB   1 
ATOM   4812 O OG1  . THR   B 1 57  ? 57.148 -15.958 -1.176  1.00 14.79 ?  57  THR   B OG1  1 
ATOM   4813 C CG2  . THR   B 1 57  ? 55.856 -16.171 -3.226  1.00 14.55 ?  57  THR   B CG2  1 
ATOM   4814 H H    . THR   B 1 57  ? 57.583 -18.227 -2.738  1.00 17.85 ?  57  THR   B H    1 
ATOM   4815 H HA   . THR   B 1 57  ? 58.494 -16.129 -4.118  1.00 18.10 ?  57  THR   B HA   1 
ATOM   4816 H HB   . THR   B 1 57  ? 57.282 -14.797 -2.764  1.00 17.19 ?  57  THR   B HB   1 
ATOM   4817 H HG1  . THR   B 1 57  ? 57.079 -16.779 -1.013  1.00 17.78 ?  57  THR   B HG1  1 
ATOM   4818 H HG21 . THR   B 1 57  ? 55.135 -15.616 -2.896  1.00 17.49 ?  57  THR   B HG21 1 
ATOM   4819 H HG22 . THR   B 1 57  ? 55.904 -16.090 -4.191  1.00 17.49 ?  57  THR   B HG22 1 
ATOM   4820 H HG23 . THR   B 1 57  ? 55.664 -17.098 -3.002  1.00 17.49 ?  57  THR   B HG23 1 
ATOM   4821 N N    . ASN   B 1 58  ? 60.419 -17.156 -2.051  1.00 16.58 ?  58  ASN   B N    1 
ATOM   4822 C CA   . ASN   B 1 58  ? 61.615 -16.944 -1.240  1.00 19.08 ?  58  ASN   B CA   1 
ATOM   4823 C C    . ASN   B 1 58  ? 61.281 -16.232 0.073   1.00 17.30 ?  58  ASN   B C    1 
ATOM   4824 O O    . ASN   B 1 58  ? 62.022 -15.359 0.536   1.00 18.10 ?  58  ASN   B O    1 
ATOM   4825 C CB   . ASN   B 1 58  ? 62.709 -16.203 -2.016  1.00 24.79 ?  58  ASN   B CB   1 
ATOM   4826 C CG   . ASN   B 1 58  ? 64.075 -16.347 -1.374  1.00 32.84 ?  58  ASN   B CG   1 
ATOM   4827 O OD1  . ASN   B 1 58  ? 64.391 -17.382 -0.787  1.00 35.17 ?  58  ASN   B OD1  1 
ATOM   4828 N ND2  . ASN   B 1 58  ? 64.892 -15.306 -1.477  1.00 38.01 ?  58  ASN   B ND2  1 
ATOM   4829 H H    . ASN   B 1 58  ? 60.285 -17.983 -2.259  1.00 19.93 ?  58  ASN   B H    1 
ATOM   4830 H HA   . ASN   B 1 58  ? 61.975 -17.818 -1.013  1.00 22.93 ?  58  ASN   B HA   1 
ATOM   4831 H HB2  . ASN   B 1 58  ? 62.761 -16.564 -2.918  1.00 29.78 ?  58  ASN   B HB2  1 
ATOM   4832 H HB3  . ASN   B 1 58  ? 62.493 -15.260 -2.048  1.00 29.78 ?  58  ASN   B HB3  1 
ATOM   4833 H HD21 . ASN   B 1 58  ? 65.678 -15.341 -1.129  1.00 45.64 ?  58  ASN   B HD21 1 
ATOM   4834 H HD22 . ASN   B 1 58  ? 64.635 -14.599 -1.892  1.00 45.64 ?  58  ASN   B HD22 1 
ATOM   4835 N N    . ASN   B 1 59  ? 60.157 -16.612 0.681   1.00 16.53 ?  59  ASN   B N    1 
ATOM   4836 C CA   . ASN   B 1 59  ? 59.682 -16.130 1.980   1.00 15.97 ?  59  ASN   B CA   1 
ATOM   4837 C C    . ASN   B 1 59  ? 59.085 -14.725 1.918   1.00 15.58 ?  59  ASN   B C    1 
ATOM   4838 O O    . ASN   B 1 59  ? 58.654 -14.217 2.961   1.00 15.71 ?  59  ASN   B O    1 
ATOM   4839 C CB   . ASN   B 1 59  ? 60.751 -16.180 3.086   1.00 16.90 ?  59  ASN   B CB   1 
ATOM   4840 C CG   . ASN   B 1 59  ? 60.157 -16.355 4.468   1.00 17.89 ?  59  ASN   B CG   1 
ATOM   4841 O OD1  . ASN   B 1 59  ? 59.335 -17.245 4.693   1.00 18.33 ?  59  ASN   B OD1  1 
ATOM   4842 N ND2  . ASN   B 1 59  ? 60.574 -15.509 5.408   1.00 18.76 ?  59  ASN   B ND2  1 
ATOM   4843 H H    . ASN   B 1 59  ? 59.617 -17.193 0.340   1.00 19.87 ?  59  ASN   B H    1 
ATOM   4844 H HA   . ASN   B 1 59  ? 58.972 -16.725 2.266   1.00 19.19 ?  59  ASN   B HA   1 
ATOM   4845 H HB2  . ASN   B 1 59  ? 61.347 -16.930 2.927   1.00 20.31 ?  59  ASN   B HB2  1 
ATOM   4846 H HB3  . ASN   B 1 59  ? 61.251 -15.352 3.089   1.00 20.31 ?  59  ASN   B HB3  1 
ATOM   4847 H HD21 . ASN   B 1 59  ? 60.264 -15.569 6.212   1.00 22.54 ?  59  ASN   B HD21 1 
ATOM   4848 H HD22 . ASN   B 1 59  ? 61.144 -14.901 5.213   1.00 22.54 ?  59  ASN   B HD22 1 
ATOM   4849 N N    . ALA   B 1 60  ? 59.025 -14.087 0.746   1.00 15.18 ?  60  ALA   B N    1 
ATOM   4850 C CA   . ALA   B 1 60  ? 58.432 -12.753 0.674   1.00 15.03 ?  60  ALA   B CA   1 
ATOM   4851 C C    . ALA   B 1 60  ? 56.960 -12.772 1.066   1.00 14.31 ?  60  ALA   B C    1 
ATOM   4852 O O    . ALA   B 1 60  ? 56.464 -11.817 1.679   1.00 14.66 ?  60  ALA   B O    1 
ATOM   4853 C CB   . ALA   B 1 60  ? 58.608 -12.163 -0.728  1.00 16.13 ?  60  ALA   B CB   1 
ATOM   4854 H H    . ALA   B 1 60  ? 59.305 -14.402 -0.001  1.00 18.24 ?  60  ALA   B H    1 
ATOM   4855 H HA   . ALA   B 1 60  ? 58.894 -12.175 1.296   1.00 18.07 ?  60  ALA   B HA   1 
ATOM   4856 H HB1  . ALA   B 1 60  ? 58.213 -11.281 -0.752  1.00 19.38 ?  60  ALA   B HB1  1 
ATOM   4857 H HB2  . ALA   B 1 60  ? 59.559 -12.106 -0.928  1.00 19.38 ?  60  ALA   B HB2  1 
ATOM   4858 H HB3  . ALA   B 1 60  ? 58.173 -12.743 -1.373  1.00 19.38 ?  60  ALA   B HB3  1 
ATOM   4859 N N    . MET   B 1 61  ? 56.248 -13.848 0.728   1.00 13.93 ?  61  MET   B N    1 
ATOM   4860 C CA   . MET   B 1 61  ? 54.855 -13.971 1.130   1.00 13.47 ?  61  MET   B CA   1 
ATOM   4861 C C    . MET   B 1 61  ? 54.720 -13.969 2.651   1.00 13.76 ?  61  MET   B C    1 
ATOM   4862 O O    . MET   B 1 61  ? 53.818 -13.320 3.199   1.00 13.51 ?  61  MET   B O    1 
ATOM   4863 C CB   . MET   B 1 61  ? 54.275 -15.245 0.513   1.00 13.75 ?  61  MET   B CB   1 
ATOM   4864 C CG   . MET   B 1 61  ? 52.829 -15.531 0.913   1.00 13.52 ?  61  MET   B CG   1 
ATOM   4865 S SD   . MET   B 1 61  ? 52.181 -17.033 0.150   1.00 13.72 ?  61  MET   B SD   1 
ATOM   4866 C CE   . MET   B 1 61  ? 51.908 -16.462 -1.523  1.00 15.41 ?  61  MET   B CE   1 
ATOM   4867 H H    . MET   B 1 61  ? 56.551 -14.515 0.271   1.00 16.75 ?  61  MET   B H    1 
ATOM   4868 H HA   . MET   B 1 61  ? 54.357 -13.223 0.771   1.00 16.19 ?  61  MET   B HA   1 
ATOM   4869 H HB2  . MET   B 1 61  ? 54.299 -15.166 -0.456  1.00 16.53 ?  61  MET   B HB2  1 
ATOM   4870 H HB3  . MET   B 1 61  ? 54.812 -16.004 0.789   1.00 16.53 ?  61  MET   B HB3  1 
ATOM   4871 H HG2  . MET   B 1 61  ? 52.780 -15.650 1.876   1.00 16.26 ?  61  MET   B HG2  1 
ATOM   4872 H HG3  . MET   B 1 61  ? 52.269 -14.788 0.643   1.00 16.26 ?  61  MET   B HG3  1 
ATOM   4873 H HE1  . MET   B 1 61  ? 51.533 -17.191 -2.046  1.00 18.52 ?  61  MET   B HE1  1 
ATOM   4874 H HE2  . MET   B 1 61  ? 51.283 -15.717 -1.507  1.00 18.52 ?  61  MET   B HE2  1 
ATOM   4875 H HE3  . MET   B 1 61  ? 52.750 -16.179 -1.905  1.00 18.52 ?  61  MET   B HE3  1 
ATOM   4876 N N    . GLN   B 1 62  ? 55.596 -14.694 3.355   1.00 13.70 ?  62  GLN   B N    1 
ATOM   4877 C CA   . GLN   B 1 62  ? 55.491 -14.750 4.809   1.00 14.04 ?  62  GLN   B CA   1 
ATOM   4878 C C    . GLN   B 1 62  ? 55.779 -13.397 5.443   1.00 14.49 ?  62  GLN   B C    1 
ATOM   4879 O O    . GLN   B 1 62  ? 55.095 -12.990 6.388   1.00 14.72 ?  62  GLN   B O    1 
ATOM   4880 C CB   . GLN   B 1 62  ? 56.433 -15.815 5.375   1.00 14.33 ?  62  GLN   B CB   1 
ATOM   4881 C CG   . GLN   B 1 62  ? 56.211 -16.069 6.848   1.00 14.54 ?  62  GLN   B CG   1 
ATOM   4882 C CD   . GLN   B 1 62  ? 54.834 -16.657 7.106   1.00 14.67 ?  62  GLN   B CD   1 
ATOM   4883 O OE1  . GLN   B 1 62  ? 54.570 -17.808 6.759   1.00 14.72 ?  62  GLN   B OE1  1 
ATOM   4884 N NE2  . GLN   B 1 62  ? 53.932 -15.856 7.674   1.00 14.94 ?  62  GLN   B NE2  1 
ATOM   4885 H H    . GLN   B 1 62  ? 56.239 -15.160 3.016   1.00 16.47 ?  62  GLN   B H    1 
ATOM   4886 H HA   . GLN   B 1 62  ? 54.580 -15.004 5.042   1.00 16.88 ?  62  GLN   B HA   1 
ATOM   4887 H HB2  . GLN   B 1 62  ? 56.289 -16.653 4.905   1.00 17.23 ?  62  GLN   B HB2  1 
ATOM   4888 H HB3  . GLN   B 1 62  ? 57.349 -15.521 5.256   1.00 17.23 ?  62  GLN   B HB3  1 
ATOM   4889 H HG2  . GLN   B 1 62  ? 56.876 -16.699 7.168   1.00 17.48 ?  62  GLN   B HG2  1 
ATOM   4890 H HG3  . GLN   B 1 62  ? 56.286 -15.232 7.336   1.00 17.48 ?  62  GLN   B HG3  1 
ATOM   4891 H HE21 . GLN   B 1 62  ? 54.147 -15.050 7.891   1.00 17.96 ?  62  GLN   B HE21 1 
ATOM   4892 H HE22 . GLN   B 1 62  ? 53.140 -16.146 7.836   1.00 17.96 ?  62  GLN   B HE22 1 
ATOM   4893 N N    . VAL   B 1 63  ? 56.795 -12.690 4.950   1.00 14.97 ?  63  VAL   B N    1 
ATOM   4894 C CA   . VAL   B 1 63  ? 57.102 -11.369 5.495   1.00 15.82 ?  63  VAL   B CA   1 
ATOM   4895 C C    . VAL   B 1 63  ? 55.912 -10.433 5.309   1.00 15.06 ?  63  VAL   B C    1 
ATOM   4896 O O    . VAL   B 1 63  ? 55.504 -9.719  6.236   1.00 15.57 ?  63  VAL   B O    1 
ATOM   4897 C CB   . VAL   B 1 63  ? 58.397 -10.819 4.867   1.00 16.92 ?  63  VAL   B CB   1 
ATOM   4898 C CG1  . VAL   B 1 63  ? 58.628 -9.383  5.294   1.00 17.28 ?  63  VAL   B CG1  1 
ATOM   4899 C CG2  . VAL   B 1 63  ? 59.586 -11.689 5.269   1.00 17.67 ?  63  VAL   B CG2  1 
ATOM   4900 H H    . VAL   B 1 63  ? 57.306 -12.946 4.305   1.00 18.00 ?  63  VAL   B H    1 
ATOM   4901 H HA   . VAL   B 1 63  ? 57.260 -11.463 6.445   1.00 19.02 ?  63  VAL   B HA   1 
ATOM   4902 H HB   . VAL   B 1 63  ? 58.325 -10.847 3.899   1.00 20.33 ?  63  VAL   B HB   1 
ATOM   4903 H HG11 . VAL   B 1 63  ? 59.549 -9.143  5.098   1.00 20.77 ?  63  VAL   B HG11 1 
ATOM   4904 H HG12 . VAL   B 1 63  ? 58.026 -8.808  4.804   1.00 20.77 ?  63  VAL   B HG12 1 
ATOM   4905 H HG13 . VAL   B 1 63  ? 58.466 -9.310  6.247   1.00 20.77 ?  63  VAL   B HG13 1 
ATOM   4906 H HG21 . VAL   B 1 63  ? 60.395 -11.323 4.877   1.00 21.23 ?  63  VAL   B HG21 1 
ATOM   4907 H HG22 . VAL   B 1 63  ? 59.662 -11.690 6.238   1.00 21.23 ?  63  VAL   B HG22 1 
ATOM   4908 H HG23 . VAL   B 1 63  ? 59.444 -12.594 4.950   1.00 21.23 ?  63  VAL   B HG23 1 
ATOM   4909 N N    . GLU   B 1 64  ? 55.340 -10.425 4.104   1.00 14.63 ?  64  GLU   B N    1 
ATOM   4910 C CA   . GLU   B 1 64  ? 54.179 -9.583  3.829   1.00 14.26 ?  64  GLU   B CA   1 
ATOM   4911 C C    . GLU   B 1 64  ? 52.996 -9.978  4.706   1.00 13.80 ?  64  GLU   B C    1 
ATOM   4912 O O    . GLU   B 1 64  ? 52.252 -9.113  5.197   1.00 14.27 ?  64  GLU   B O    1 
ATOM   4913 C CB   . GLU   B 1 64  ? 53.816 -9.734  2.351   1.00 14.57 ?  64  GLU   B CB   1 
ATOM   4914 C CG   . GLU   B 1 64  ? 52.564 -8.985  1.913   1.00 14.87 ?  64  GLU   B CG   1 
ATOM   4915 C CD   . GLU   B 1 64  ? 52.013 -9.490  0.592   1.00 15.57 ?  64  GLU   B CD   1 
ATOM   4916 O OE1  . GLU   B 1 64  ? 52.184 -10.699 0.286   1.00 16.32 ?  64  GLU   B OE1  1 
ATOM   4917 O OE2  . GLU   B 1 64  ? 51.382 -8.683  -0.132  1.00 16.21 -1 64  GLU   B OE2  1 
ATOM   4918 H H    . GLU   B 1 64  ? 55.610 -10.895 3.430   1.00 17.58 ?  64  GLU   B H    1 
ATOM   4919 H HA   . GLU   B 1 64  ? 54.401 -8.656  4.001   1.00 17.14 ?  64  GLU   B HA   1 
ATOM   4920 H HB2  . GLU   B 1 64  ? 54.553 -9.399  1.813   1.00 17.51 ?  64  GLU   B HB2  1 
ATOM   4921 H HB3  . GLU   B 1 64  ? 53.676 -10.671 2.161   1.00 17.51 ?  64  GLU   B HB3  1 
ATOM   4922 H HG2  . GLU   B 1 64  ? 51.868 -9.086  2.581   1.00 17.87 ?  64  GLU   B HG2  1 
ATOM   4923 H HG3  . GLU   B 1 64  ? 52.781 -8.043  1.806   1.00 17.87 ?  64  GLU   B HG3  1 
ATOM   4924 N N    . SER   B 1 65  ? 52.810 -11.285 4.905   1.00 13.29 ?  65  SER   B N    1 
ATOM   4925 C CA   . SER   B 1 65  ? 51.699 -11.785 5.704   1.00 13.85 ?  65  SER   B CA   1 
ATOM   4926 C C    . SER   B 1 65  ? 51.835 -11.391 7.168   1.00 13.92 ?  65  SER   B C    1 
ATOM   4927 O O    . SER   B 1 65  ? 50.842 -11.013 7.804   1.00 14.08 ?  65  SER   B O    1 
ATOM   4928 C CB   . SER   B 1 65  ? 51.618 -13.305 5.572   1.00 13.93 ?  65  SER   B CB   1 
ATOM   4929 O OG   . SER   B 1 65  ? 51.271 -13.704 4.252   1.00 13.82 ?  65  SER   B OG   1 
ATOM   4930 H H    . SER   B 1 65  ? 53.323 -11.906 4.589   1.00 15.98 ?  65  SER   B H    1 
ATOM   4931 H HA   . SER   B 1 65  ? 50.872 -11.409 5.363   1.00 16.65 ?  65  SER   B HA   1 
ATOM   4932 H HB2  . SER   B 1 65  ? 52.475 -13.691 5.794   1.00 16.75 ?  65  SER   B HB2  1 
ATOM   4933 H HB3  . SER   B 1 65  ? 50.938 -13.636 6.187   1.00 16.75 ?  65  SER   B HB3  1 
ATOM   4934 H HG   . SER   B 1 65  ? 51.838 -13.414 3.704   1.00 16.62 ?  65  SER   B HG   1 
ATOM   4935 N N    . ASP   B 1 66  ? 53.043 -11.494 7.731   1.00 14.33 ?  66  ASP   B N    1 
ATOM   4936 C CA   . ASP   B 1 66  ? 53.231 -11.110 9.125   1.00 14.64 ?  66  ASP   B CA   1 
ATOM   4937 C C    . ASP   B 1 66  ? 52.922 -9.631  9.329   1.00 14.73 ?  66  ASP   B C    1 
ATOM   4938 O O    . ASP   B 1 66  ? 52.339 -9.244  10.349  1.00 15.09 ?  66  ASP   B O    1 
ATOM   4939 C CB   . ASP   B 1 66  ? 54.658 -11.431 9.583   1.00 15.78 ?  66  ASP   B CB   1 
ATOM   4940 C CG   . ASP   B 1 66  ? 54.911 -12.928 9.741   1.00 17.57 ?  66  ASP   B CG   1 
ATOM   4941 O OD1  . ASP   B 1 66  ? 53.952 -13.731 9.679   1.00 18.55 ?  66  ASP   B OD1  1 
ATOM   4942 O OD2  . ASP   B 1 66  ? 56.088 -13.310 9.935   1.00 19.82 -1 66  ASP   B OD2  1 
ATOM   4943 H H    . ASP   B 1 66  ? 53.747 -11.791 7.337   1.00 17.23 ?  66  ASP   B H    1 
ATOM   4944 H HA   . ASP   B 1 66  ? 52.623 -11.616 9.682   1.00 17.59 ?  66  ASP   B HA   1 
ATOM   4945 H HB2  . ASP   B 1 66  ? 55.287 -11.095 8.924   1.00 18.96 ?  66  ASP   B HB2  1 
ATOM   4946 H HB3  . ASP   B 1 66  ? 54.821 -11.006 10.441  1.00 18.96 ?  66  ASP   B HB3  1 
ATOM   4947 N N    . ASP   B 1 67  ? 53.306 -8.786  8.368   1.00 14.69 ?  67  ASP   B N    1 
ATOM   4948 C CA   . ASP   B 1 67  ? 52.964 -7.371  8.454   1.00 15.34 ?  67  ASP   B CA   1 
ATOM   4949 C C    . ASP   B 1 67  ? 51.453 -7.159  8.368   1.00 15.22 ?  67  ASP   B C    1 
ATOM   4950 O O    . ASP   B 1 67  ? 50.891 -6.351  9.116   1.00 15.71 ?  67  ASP   B O    1 
ATOM   4951 C CB   . ASP   B 1 67  ? 53.685 -6.598  7.356   1.00 16.66 ?  67  ASP   B CB   1 
ATOM   4952 C CG   . ASP   B 1 67  ? 53.268 -5.153  7.311   1.00 18.35 ?  67  ASP   B CG   1 
ATOM   4953 O OD1  . ASP   B 1 67  ? 53.761 -4.351  8.142   1.00 19.31 ?  67  ASP   B OD1  1 
ATOM   4954 O OD2  . ASP   B 1 67  ? 52.421 -4.836  6.457   1.00 19.42 -1 67  ASP   B OD2  1 
ATOM   4955 H H    . ASP   B 1 67  ? 53.761 -9.006  7.673   1.00 17.65 ?  67  ASP   B H    1 
ATOM   4956 H HA   . ASP   B 1 67  ? 53.269 -7.024  9.307   1.00 18.44 ?  67  ASP   B HA   1 
ATOM   4957 H HB2  . ASP   B 1 67  ? 54.644 -6.631  7.517   1.00 20.02 ?  67  ASP   B HB2  1 
ATOM   4958 H HB3  . ASP   B 1 67  ? 53.485 -7.004  6.495   1.00 20.02 ?  67  ASP   B HB3  1 
ATOM   4959 N N    . TYR   B 1 68  ? 50.772 -7.885  7.474   1.00 15.11 ?  68  TYR   B N    1 
ATOM   4960 C CA   . TYR   B 1 68  ? 49.315 -7.792  7.399   1.00 15.94 ?  68  TYR   B CA   1 
ATOM   4961 C C    . TYR   B 1 68  ? 48.675 -8.136  8.740   1.00 15.47 ?  68  TYR   B C    1 
ATOM   4962 O O    . TYR   B 1 68  ? 47.746 -7.453  9.190   1.00 16.36 ?  68  TYR   B O    1 
ATOM   4963 C CB   . TYR   B 1 68  ? 48.778 -8.714  6.297   1.00 16.78 ?  68  TYR   B CB   1 
ATOM   4964 C CG   . TYR   B 1 68  ? 47.272 -8.863  6.344   1.00 18.07 ?  68  TYR   B CG   1 
ATOM   4965 C CD1  . TYR   B 1 68  ? 46.676 -9.822  7.156   1.00 18.92 ?  68  TYR   B CD1  1 
ATOM   4966 C CD2  . TYR   B 1 68  ? 46.447 -8.027  5.610   1.00 18.82 ?  68  TYR   B CD2  1 
ATOM   4967 C CE1  . TYR   B 1 68  ? 45.307 -9.949  7.230   1.00 20.12 ?  68  TYR   B CE1  1 
ATOM   4968 C CE2  . TYR   B 1 68  ? 45.063 -8.156  5.671   1.00 19.61 ?  68  TYR   B CE2  1 
ATOM   4969 C CZ   . TYR   B 1 68  ? 44.513 -9.113  6.487   1.00 20.11 ?  68  TYR   B CZ   1 
ATOM   4970 O OH   . TYR   B 1 68  ? 43.145 -9.234  6.565   1.00 21.75 ?  68  TYR   B OH   1 
ATOM   4971 H H    . TYR   B 1 68  ? 51.128 -8.439  6.918   1.00 18.16 ?  68  TYR   B H    1 
ATOM   4972 H HA   . TYR   B 1 68  ? 49.073 -6.883  7.178   1.00 19.15 ?  68  TYR   B HA   1 
ATOM   4973 H HB2  . TYR   B 1 68  ? 49.013 -8.342  5.433   1.00 20.16 ?  68  TYR   B HB2  1 
ATOM   4974 H HB3  . TYR   B 1 68  ? 49.170 -9.595  6.398   1.00 20.16 ?  68  TYR   B HB3  1 
ATOM   4975 H HD1  . TYR   B 1 68  ? 47.213 -10.393 7.661   1.00 22.74 ?  68  TYR   B HD1  1 
ATOM   4976 H HD2  . TYR   B 1 68  ? 46.822 -7.374  5.068   1.00 22.61 ?  68  TYR   B HD2  1 
ATOM   4977 H HE1  . TYR   B 1 68  ? 44.921 -10.608 7.767   1.00 24.17 ?  68  TYR   B HE1  1 
ATOM   4978 H HE2  . TYR   B 1 68  ? 44.513 -7.591  5.175   1.00 23.56 ?  68  TYR   B HE2  1 
ATOM   4979 H HH   . TYR   B 1 68  ? 42.764 -8.684  6.052   1.00 26.13 ?  68  TYR   B HH   1 
ATOM   4980 N N    . ILE   B 1 69  ? 49.142 -9.215  9.380   1.00 15.30 ?  69  ILE   B N    1 
ATOM   4981 C CA   . ILE   B 1 69  ? 48.579 -9.639  10.661  1.00 15.98 ?  69  ILE   B CA   1 
ATOM   4982 C C    . ILE   B 1 69  ? 48.835 -8.601  11.746  1.00 15.79 ?  69  ILE   B C    1 
ATOM   4983 O O    . ILE   B 1 69  ? 47.961 -8.320  12.575  1.00 16.08 ?  69  ILE   B O    1 
ATOM   4984 C CB   . ILE   B 1 69  ? 49.140 -11.020 11.052  1.00 16.82 ?  69  ILE   B CB   1 
ATOM   4985 C CG1  . ILE   B 1 69  ? 48.616 -12.109 10.109  1.00 17.26 ?  69  ILE   B CG1  1 
ATOM   4986 C CG2  . ILE   B 1 69  ? 48.819 -11.340 12.505  1.00 17.97 ?  69  ILE   B CG2  1 
ATOM   4987 C CD1  . ILE   B 1 69  ? 47.141 -12.424 10.272  1.00 17.73 ?  69  ILE   B CD1  1 
ATOM   4988 H H    . ILE   B 1 69  ? 49.774 -9.720  9.091   1.00 18.38 ?  69  ILE   B H    1 
ATOM   4989 H HA   . ILE   B 1 69  ? 47.621 -9.730  10.564  1.00 19.20 ?  69  ILE   B HA   1 
ATOM   4990 H HB   . ILE   B 1 69  ? 50.105 -10.991 10.961  1.00 20.21 ?  69  ILE   B HB   1 
ATOM   4991 H HG12 . ILE   B 1 69  ? 48.755 -11.821 9.193   1.00 20.74 ?  69  ILE   B HG12 1 
ATOM   4992 H HG13 . ILE   B 1 69  ? 49.111 -12.928 10.271  1.00 20.74 ?  69  ILE   B HG13 1 
ATOM   4993 H HG21 . ILE   B 1 69  ? 48.936 -12.293 12.650  1.00 21.59 ?  69  ILE   B HG21 1 
ATOM   4994 H HG22 . ILE   B 1 69  ? 49.422 -10.845 13.081  1.00 21.59 ?  69  ILE   B HG22 1 
ATOM   4995 H HG23 . ILE   B 1 69  ? 47.900 -11.090 12.688  1.00 21.59 ?  69  ILE   B HG23 1 
ATOM   4996 H HD11 . ILE   B 1 69  ? 46.897 -13.101 9.624   1.00 21.31 ?  69  ILE   B HD11 1 
ATOM   4997 H HD12 . ILE   B 1 69  ? 46.986 -12.754 11.170  1.00 21.31 ?  69  ILE   B HD12 1 
ATOM   4998 H HD13 . ILE   B 1 69  ? 46.627 -11.618 10.118  1.00 21.31 ?  69  ILE   B HD13 1 
ATOM   4999 N N    . ALA   B 1 70  ? 50.039 -8.030  11.781  1.00 15.51 ?  70  ALA   B N    1 
ATOM   5000 C CA   . ALA   B 1 70  ? 50.323 -7.000  12.776  1.00 15.07 ?  70  ALA   B CA   1 
ATOM   5001 C C    . ALA   B 1 70  ? 49.336 -5.844  12.665  1.00 15.38 ?  70  ALA   B C    1 
ATOM   5002 O O    . ALA   B 1 70  ? 48.886 -5.303  13.679  1.00 15.76 ?  70  ALA   B O    1 
ATOM   5003 C CB   . ALA   B 1 70  ? 51.758 -6.504  12.620  1.00 15.39 ?  70  ALA   B CB   1 
ATOM   5004 H H    . ALA   B 1 70  ? 50.690 -8.222  11.257  1.00 18.64 ?  70  ALA   B H    1 
ATOM   5005 H HA   . ALA   B 1 70  ? 50.238 -7.386  13.662  1.00 18.11 ?  70  ALA   B HA   1 
ATOM   5006 H HB1  . ALA   B 1 70  ? 51.941 -5.839  13.304  1.00 18.50 ?  70  ALA   B HB1  1 
ATOM   5007 H HB2  . ALA   B 1 70  ? 52.369 -7.254  12.724  1.00 18.50 ?  70  ALA   B HB2  1 
ATOM   5008 H HB3  . ALA   B 1 70  ? 51.868 -6.112  11.740  1.00 18.50 ?  70  ALA   B HB3  1 
ATOM   5009 N N    . THR   B 1 71  ? 48.972 -5.471  11.438  1.00 15.97 ?  71  THR   B N    1 
ATOM   5010 C CA   . THR   B 1 71  ? 48.090 -4.330  11.220  1.00 16.95 ?  71  THR   B CA   1 
ATOM   5011 C C    . THR   B 1 71  ? 46.619 -4.685  11.418  1.00 17.68 ?  71  THR   B C    1 
ATOM   5012 O O    . THR   B 1 71  ? 45.845 -3.864  11.930  1.00 18.74 ?  71  THR   B O    1 
ATOM   5013 C CB   . THR   B 1 71  ? 48.322 -3.766  9.812   1.00 18.42 ?  71  THR   B CB   1 
ATOM   5014 O OG1  . THR   B 1 71  ? 49.654 -3.247  9.718   1.00 20.16 ?  71  THR   B OG1  1 
ATOM   5015 C CG2  . THR   B 1 71  ? 47.328 -2.663  9.485   1.00 19.22 ?  71  THR   B CG2  1 
ATOM   5016 H H    . THR   B 1 71  ? 49.229 -5.861  10.718  1.00 19.20 ?  71  THR   B H    1 
ATOM   5017 H HA   . THR   B 1 71  ? 48.314 -3.634  11.856  1.00 20.36 ?  71  THR   B HA   1 
ATOM   5018 H HB   . THR   B 1 71  ? 48.223 -4.473  9.158   1.00 22.13 ?  71  THR   B HB   1 
ATOM   5019 H HG1  . THR   B 1 71  ? 49.796 -2.923  8.952   1.00 24.22 ?  71  THR   B HG1  1 
ATOM   5020 H HG21 . THR   B 1 71  ? 47.643 -2.151  8.721   1.00 23.10 ?  71  THR   B HG21 1 
ATOM   5021 H HG22 . THR   B 1 71  ? 46.466 -3.045  9.274   1.00 23.10 ?  71  THR   B HG22 1 
ATOM   5022 H HG23 . THR   B 1 71  ? 47.238 -2.064  10.244  1.00 23.10 ?  71  THR   B HG23 1 
ATOM   5023 N N    . ASN   B 1 72  ? 46.214 -5.895  11.021  1.00 17.29 ?  72  ASN   B N    1 
ATOM   5024 C CA   . ASN   B 1 72  ? 44.809 -6.238  10.896  1.00 17.55 ?  72  ASN   B CA   1 
ATOM   5025 C C    . ASN   B 1 72  ? 44.332 -7.332  11.839  1.00 18.10 ?  72  ASN   B C    1 
ATOM   5026 O O    . ASN   B 1 72  ? 43.115 -7.481  12.007  1.00 19.29 ?  72  ASN   B O    1 
ATOM   5027 C CB   . ASN   B 1 72  ? 44.497 -6.660  9.451   1.00 18.26 ?  72  ASN   B CB   1 
ATOM   5028 C CG   . ASN   B 1 72  ? 44.783 -5.556  8.455   1.00 19.28 ?  72  ASN   B CG   1 
ATOM   5029 O OD1  . ASN   B 1 72  ? 45.791 -5.577  7.741   1.00 20.42 ?  72  ASN   B OD1  1 
ATOM   5030 N ND2  . ASN   B 1 72  ? 43.911 -4.570  8.418   1.00 20.52 ?  72  ASN   B ND2  1 
ATOM   5031 H H    . ASN   B 1 72  ? 46.750 -6.544  10.818  1.00 20.78 ?  72  ASN   B H    1 
ATOM   5032 H HA   . ASN   B 1 72  ? 44.284 -5.449  11.084  1.00 21.09 ?  72  ASN   B HA   1 
ATOM   5033 H HB2  . ASN   B 1 72  ? 45.048 -7.427  9.217   1.00 21.94 ?  72  ASN   B HB2  1 
ATOM   5034 H HB3  . ASN   B 1 72  ? 43.559 -6.893  9.383   1.00 21.94 ?  72  ASN   B HB3  1 
ATOM   5035 H HD21 . ASN   B 1 72  ? 44.024 -3.916  7.872   1.00 24.65 ?  72  ASN   B HD21 1 
ATOM   5036 H HD22 . ASN   B 1 72  ? 43.219 -4.585  8.931   1.00 24.65 ?  72  ASN   B HD22 1 
ATOM   5037 N N    . GLY   B 1 73  ? 45.233 -8.092  12.454  1.00 17.93 ?  73  GLY   B N    1 
ATOM   5038 C CA   . GLY   B 1 73  ? 44.835 -9.225  13.253  1.00 17.13 ?  73  GLY   B CA   1 
ATOM   5039 C C    . GLY   B 1 73  ? 44.464 -10.410 12.387  1.00 16.07 ?  73  GLY   B C    1 
ATOM   5040 O O    . GLY   B 1 73  ? 44.454 -10.327 11.157  1.00 15.79 ?  73  GLY   B O    1 
ATOM   5041 H H    . GLY   B 1 73  ? 46.085 -7.963  12.426  1.00 21.54 ?  73  GLY   B H    1 
ATOM   5042 H HA2  . GLY   B 1 73  ? 45.563 -9.484  13.840  1.00 20.58 ?  73  GLY   B HA2  1 
ATOM   5043 H HA3  . GLY   B 1 73  ? 44.068 -8.987  13.799  1.00 20.58 ?  73  GLY   B HA3  1 
ATOM   5044 N N    . PRO   B 1 74  ? 44.142 -11.533 13.023  1.00 16.25 ?  74  PRO   B N    1 
ATOM   5045 C CA   . PRO   B 1 74  ? 43.893 -12.767 12.276  1.00 15.77 ?  74  PRO   B CA   1 
ATOM   5046 C C    . PRO   B 1 74  ? 42.594 -12.714 11.486  1.00 15.47 ?  74  PRO   B C    1 
ATOM   5047 O O    . PRO   B 1 74  ? 41.651 -11.981 11.807  1.00 16.13 ?  74  PRO   B O    1 
ATOM   5048 C CB   . PRO   B 1 74  ? 43.820 -13.832 13.377  1.00 16.94 ?  74  PRO   B CB   1 
ATOM   5049 C CG   . PRO   B 1 74  ? 43.383 -13.085 14.591  1.00 18.21 ?  74  PRO   B CG   1 
ATOM   5050 C CD   . PRO   B 1 74  ? 44.028 -11.734 14.477  1.00 17.70 ?  74  PRO   B CD   1 
ATOM   5051 H HA   . PRO   B 1 74  ? 44.637 -12.960 11.680  1.00 18.96 ?  74  PRO   B HA   1 
ATOM   5052 H HB2  . PRO   B 1 74  ? 43.170 -14.509 13.133  1.00 20.35 ?  74  PRO   B HB2  1 
ATOM   5053 H HB3  . PRO   B 1 74  ? 44.697 -14.227 13.510  1.00 20.35 ?  74  PRO   B HB3  1 
ATOM   5054 H HG2  . PRO   B 1 74  ? 42.416 -13.005 14.592  1.00 21.88 ?  74  PRO   B HG2  1 
ATOM   5055 H HG3  . PRO   B 1 74  ? 43.691 -13.547 15.385  1.00 21.88 ?  74  PRO   B HG3  1 
ATOM   5056 H HD2  . PRO   B 1 74  ? 43.456 -11.054 14.874  1.00 21.26 ?  74  PRO   B HD2  1 
ATOM   5057 H HD3  . PRO   B 1 74  ? 44.906 -11.741 14.887  1.00 21.26 ?  74  PRO   B HD3  1 
ATOM   5058 N N    . LEU   B 1 75  ? 42.561 -13.533 10.438  1.00 14.55 ?  75  LEU   B N    1 
ATOM   5059 C CA   . LEU   B 1 75  ? 41.348 -13.748 9.670   1.00 14.12 ?  75  LEU   B CA   1 
ATOM   5060 C C    . LEU   B 1 75  ? 40.373 -14.606 10.472  1.00 14.36 ?  75  LEU   B C    1 
ATOM   5061 O O    . LEU   B 1 75  ? 40.708 -15.158 11.519  1.00 15.55 ?  75  LEU   B O    1 
ATOM   5062 C CB   . LEU   B 1 75  ? 41.671 -14.470 8.362   1.00 14.14 ?  75  LEU   B CB   1 
ATOM   5063 C CG   . LEU   B 1 75  ? 42.517 -13.726 7.327   1.00 15.99 ?  75  LEU   B CG   1 
ATOM   5064 C CD1  . LEU   B 1 75  ? 42.697 -14.556 6.063   1.00 16.90 ?  75  LEU   B CD1  1 
ATOM   5065 C CD2  . LEU   B 1 75  ? 41.921 -12.387 6.993   1.00 18.96 ?  75  LEU   B CD2  1 
ATOM   5066 H H    . LEU   B 1 75  ? 43.235 -13.990 10.149  1.00 17.49 ?  75  LEU   B H    1 
ATOM   5067 H HA   . LEU   B 1 75  ? 40.926 -12.901 9.470   1.00 16.97 ?  75  LEU   B HA   1 
ATOM   5068 H HB2  . LEU   B 1 75  ? 42.146 -15.290 8.580   1.00 17.00 ?  75  LEU   B HB2  1 
ATOM   5069 H HB3  . LEU   B 1 75  ? 40.833 -14.700 7.929   1.00 17.00 ?  75  LEU   B HB3  1 
ATOM   5070 H HG   . LEU   B 1 75  ? 43.398 -13.573 7.702   1.00 19.22 ?  75  LEU   B HG   1 
ATOM   5071 H HD11 . LEU   B 1 75  ? 43.244 -14.058 5.432   1.00 20.31 ?  75  LEU   B HD11 1 
ATOM   5072 H HD12 . LEU   B 1 75  ? 43.138 -15.391 6.289   1.00 20.31 ?  75  LEU   B HD12 1 
ATOM   5073 H HD13 . LEU   B 1 75  ? 41.828 -14.736 5.673   1.00 20.31 ?  75  LEU   B HD13 1 
ATOM   5074 H HD21 . LEU   B 1 75  ? 42.410 -11.999 6.252   1.00 22.78 ?  75  LEU   B HD21 1 
ATOM   5075 H HD22 . LEU   B 1 75  ? 40.991 -12.510 6.751   1.00 22.78 ?  75  LEU   B HD22 1 
ATOM   5076 H HD23 . LEU   B 1 75  ? 41.987 -11.810 7.772   1.00 22.78 ?  75  LEU   B HD23 1 
ATOM   5077 N N    . LYS   B 1 76  ? 39.144 -14.705 9.963   1.00 15.61 ?  76  LYS   B N    1 
ATOM   5078 C CA   . LYS   B 1 76  ? 38.161 -15.667 10.444  1.00 17.16 ?  76  LYS   B CA   1 
ATOM   5079 C C    . LYS   B 1 76  ? 38.244 -16.937 9.601   1.00 15.68 ?  76  LYS   B C    1 
ATOM   5080 O O    . LYS   B 1 76  ? 38.513 -16.880 8.403   1.00 15.33 ?  76  LYS   B O    1 
ATOM   5081 C CB   . LYS   B 1 76  ? 36.741 -15.098 10.282  1.00 19.28 ?  76  LYS   B CB   1 
ATOM   5082 C CG   . LYS   B 1 76  ? 36.470 -13.713 10.889  1.00 21.07 ?  76  LYS   B CG   1 
ATOM   5083 C CD   . LYS   B 1 76  ? 35.062 -13.195 10.526  1.00 22.35 ?  76  LYS   B CD   1 
ATOM   5084 C CE   . LYS   B 1 76  ? 34.787 -11.817 11.112  1.00 24.30 ?  76  LYS   B CE   1 
ATOM   5085 N NZ   . LYS   B 1 76  ? 33.492 -11.235 10.649  1.00 25.14 ?  76  LYS   B NZ   1 
ATOM   5086 H H    . LYS   B 1 76  ? 38.854 -14.219 9.317   1.00 18.77 ?  76  LYS   B H    1 
ATOM   5087 H HA   . LYS   B 1 76  ? 38.321 -15.890 11.373  1.00 20.62 ?  76  LYS   B HA   1 
ATOM   5088 H HB2  . LYS   B 1 76  ? 36.550 -15.039 9.333   1.00 23.17 ?  76  LYS   B HB2  1 
ATOM   5089 H HB3  . LYS   B 1 76  ? 36.121 -15.720 10.694  1.00 23.17 ?  76  LYS   B HB3  1 
ATOM   5090 H HG2  . LYS   B 1 76  ? 36.536 -13.772 11.855  1.00 25.31 ?  76  LYS   B HG2  1 
ATOM   5091 H HG3  . LYS   B 1 76  ? 37.126 -13.083 10.548  1.00 25.31 ?  76  LYS   B HG3  1 
ATOM   5092 H HD2  . LYS   B 1 76  ? 34.988 -13.135 9.560   1.00 26.84 ?  76  LYS   B HD2  1 
ATOM   5093 H HD3  . LYS   B 1 76  ? 34.400 -13.812 10.874  1.00 26.84 ?  76  LYS   B HD3  1 
ATOM   5094 H HE2  . LYS   B 1 76  ? 34.756 -11.889 12.078  1.00 29.19 ?  76  LYS   B HE2  1 
ATOM   5095 H HE3  . LYS   B 1 76  ? 35.499 -11.215 10.846  1.00 29.19 ?  76  LYS   B HE3  1 
ATOM   5096 H HZ1  . LYS   B 1 76  ? 33.371 -10.431 11.016  1.00 30.19 ?  76  LYS   B HZ1  1 
ATOM   5097 H HZ2  . LYS   B 1 76  ? 33.493 -11.148 9.763   1.00 30.19 ?  76  LYS   B HZ2  1 
ATOM   5098 H HZ3  . LYS   B 1 76  ? 32.815 -11.763 10.887  1.00 30.19 ?  76  LYS   B HZ3  1 
ATOM   5099 N N    . VAL   B 1 77  ? 37.991 -18.093 10.227  1.00 16.57 ?  77  VAL   B N    1 
ATOM   5100 C CA   . VAL   B 1 77  ? 37.784 -19.304 9.441   1.00 16.55 ?  77  VAL   B CA   1 
ATOM   5101 C C    . VAL   B 1 77  ? 36.593 -19.066 8.527   1.00 15.40 ?  77  VAL   B C    1 
ATOM   5102 O O    . VAL   B 1 77  ? 35.529 -18.620 8.976   1.00 15.50 ?  77  VAL   B O    1 
ATOM   5103 C CB   . VAL   B 1 77  ? 37.577 -20.527 10.347  1.00 17.66 ?  77  VAL   B CB   1 
ATOM   5104 C CG1  . VAL   B 1 77  ? 37.302 -21.765 9.499   1.00 18.06 ?  77  VAL   B CG1  1 
ATOM   5105 C CG2  . VAL   B 1 77  ? 38.798 -20.746 11.236  1.00 19.28 ?  77  VAL   B CG2  1 
ATOM   5106 H H    . VAL   B 1 77  ? 37.931 -18.198 11.075  1.00 19.92 ?  77  VAL   B H    1 
ATOM   5107 H HA   . VAL   B 1 77  ? 38.555 -19.465 8.883   1.00 19.89 ?  77  VAL   B HA   1 
ATOM   5108 H HB   . VAL   B 1 77  ? 36.806 -20.376 10.918  1.00 21.22 ?  77  VAL   B HB   1 
ATOM   5109 H HG11 . VAL   B 1 77  ? 37.352 -22.550 10.067  1.00 21.70 ?  77  VAL   B HG11 1 
ATOM   5110 H HG12 . VAL   B 1 77  ? 36.412 -21.696 9.114   1.00 21.70 ?  77  VAL   B HG12 1 
ATOM   5111 H HG13 . VAL   B 1 77  ? 37.965 -21.819 8.797   1.00 21.70 ?  77  VAL   B HG13 1 
ATOM   5112 H HG21 . VAL   B 1 77  ? 38.661 -21.550 11.759  1.00 23.16 ?  77  VAL   B HG21 1 
ATOM   5113 H HG22 . VAL   B 1 77  ? 39.578 -20.841 10.672  1.00 23.16 ?  77  VAL   B HG22 1 
ATOM   5114 H HG23 . VAL   B 1 77  ? 38.897 -19.980 11.820  1.00 23.16 ?  77  VAL   B HG23 1 
ATOM   5115 N N    . GLY   B 1 78  ? 36.767 -19.346 7.239   1.00 14.39 ?  78  GLY   B N    1 
ATOM   5116 C CA   . GLY   B 1 78  ? 35.786 -19.029 6.228   1.00 13.89 ?  78  GLY   B CA   1 
ATOM   5117 C C    . GLY   B 1 78  ? 36.026 -17.714 5.524   1.00 13.80 ?  78  GLY   B C    1 
ATOM   5118 O O    . GLY   B 1 78  ? 35.349 -17.438 4.527   1.00 14.64 ?  78  GLY   B O    1 
ATOM   5119 H H    . GLY   B 1 78  ? 37.469 -19.730 6.920   1.00 17.29 ?  78  GLY   B H    1 
ATOM   5120 H HA2  . GLY   B 1 78  ? 35.779 -19.725 5.556   1.00 16.70 ?  78  GLY   B HA2  1 
ATOM   5121 H HA3  . GLY   B 1 78  ? 34.907 -18.990 6.635   1.00 16.70 ?  78  GLY   B HA3  1 
ATOM   5122 N N    . GLY   B 1 79  ? 36.975 -16.906 6.010   1.00 13.80 ?  79  GLY   B N    1 
ATOM   5123 C CA   . GLY   B 1 79  ? 37.284 -15.618 5.426   1.00 13.87 ?  79  GLY   B CA   1 
ATOM   5124 C C    . GLY   B 1 79  ? 38.524 -15.646 4.539   1.00 13.48 ?  79  GLY   B C    1 
ATOM   5125 O O    . GLY   B 1 79  ? 39.140 -16.681 4.295   1.00 13.74 ?  79  GLY   B O    1 
ATOM   5126 H H    . GLY   B 1 79  ? 37.466 -17.094 6.690   1.00 16.59 ?  79  GLY   B H    1 
ATOM   5127 H HA2  . GLY   B 1 79  ? 36.534 -15.316 4.890   1.00 16.67 ?  79  GLY   B HA2  1 
ATOM   5128 H HA3  . GLY   B 1 79  ? 37.436 -14.971 6.131   1.00 16.67 ?  79  GLY   B HA3  1 
ATOM   5129 N N    . SER   B 1 80  ? 38.889 -14.457 4.058   1.00 13.47 ?  80  SER   B N    1 
ATOM   5130 C CA   . SER   B 1 80  ? 40.005 -14.327 3.129   1.00 13.06 ?  80  SER   B CA   1 
ATOM   5131 C C    . SER   B 1 80  ? 40.590 -12.921 3.187   1.00 13.01 ?  80  SER   B C    1 
ATOM   5132 O O    . SER   B 1 80  ? 39.970 -11.983 3.698   1.00 14.27 ?  80  SER   B O    1 
ATOM   5133 C CB   . SER   B 1 80  ? 39.565 -14.609 1.690   1.00 13.37 ?  80  SER   B CB   1 
ATOM   5134 O OG   . SER   B 1 80  ? 38.719 -13.584 1.200   1.00 14.37 ?  80  SER   B OG   1 
ATOM   5135 H H    . SER   B 1 80  ? 38.513 -13.714 4.258   1.00 16.19 ?  80  SER   B H    1 
ATOM   5136 H HA   . SER   B 1 80  ? 40.696 -14.961 3.376   1.00 15.70 ?  80  SER   B HA   1 
ATOM   5137 H HB2  . SER   B 1 80  ? 40.350 -14.658 1.122   1.00 16.07 ?  80  SER   B HB2  1 
ATOM   5138 H HB3  . SER   B 1 80  ? 39.087 -15.452 1.666   1.00 16.07 ?  80  SER   B HB3  1 
ATOM   5139 H HG   . SER   B 1 80  ? 38.027 -13.529 1.686   1.00 17.28 ?  80  SER   B HG   1 
ATOM   5140 N N    . CYS   B 1 81  ? 41.777 -12.778 2.599   1.00 12.73 ?  81  CYS   B N    1 
ATOM   5141 C CA   . CYS   B 1 81  ? 42.327 -11.466 2.286   1.00 12.66 ?  81  CYS   B CA   1 
ATOM   5142 C C    . CYS   B 1 81  ? 43.096 -11.546 0.976   1.00 12.44 ?  81  CYS   B C    1 
ATOM   5143 O O    . CYS   B 1 81  ? 43.596 -12.611 0.597   1.00 13.22 ?  81  CYS   B O    1 
ATOM   5144 C CB   . CYS   B 1 81  ? 43.218 -10.911 3.406   1.00 13.60 ?  81  CYS   B CB   1 
ATOM   5145 S SG   . CYS   B 1 81  ? 44.733 -11.851 3.661   1.00 14.10 ?  81  CYS   B SG   1 
ATOM   5146 H H    . CYS   B 1 81  ? 42.291 -13.435 2.371   1.00 15.30 ?  81  CYS   B H    1 
ATOM   5147 H HA   . CYS   B 1 81  ? 41.591 -10.847 2.160   1.00 15.22 ?  81  CYS   B HA   1 
ATOM   5148 H HB2  . CYS   B 1 81  ? 43.474 -10.002 3.184   1.00 16.35 ?  81  CYS   B HB2  1 
ATOM   5149 H HB3  . CYS   B 1 81  ? 42.717 -10.914 4.239   1.00 16.35 ?  81  CYS   B HB3  1 
ATOM   5150 H HG   . CYS   B 1 81  ? 45.361 -11.352 4.560   1.00 16.95 ?  81  CYS   B HG   1 
ATOM   5151 N N    . VAL   B 1 82  ? 43.202 -10.402 0.300   1.00 12.39 ?  82  VAL   B N    1 
ATOM   5152 C CA   . VAL   B 1 82  ? 43.963 -10.285 -0.940  1.00 12.66 ?  82  VAL   B CA   1 
ATOM   5153 C C    . VAL   B 1 82  ? 45.306 -9.646  -0.621  1.00 13.08 ?  82  VAL   B C    1 
ATOM   5154 O O    . VAL   B 1 82  ? 45.358 -8.529  -0.088  1.00 13.81 ?  82  VAL   B O    1 
ATOM   5155 C CB   . VAL   B 1 82  ? 43.216 -9.444  -1.986  1.00 13.79 ?  82  VAL   B CB   1 
ATOM   5156 C CG1  . VAL   B 1 82  ? 44.056 -9.303  -3.255  1.00 15.22 ?  82  VAL   B CG1  1 
ATOM   5157 C CG2  . VAL   B 1 82  ? 41.851 -10.037 -2.289  1.00 14.91 ?  82  VAL   B CG2  1 
ATOM   5158 H H    . VAL   B 1 82  ? 42.826 -9.668  0.542   1.00 14.90 ?  82  VAL   B H    1 
ATOM   5159 H HA   . VAL   B 1 82  ? 44.119 -11.171 -1.309  1.00 15.22 ?  82  VAL   B HA   1 
ATOM   5160 H HB   . VAL   B 1 82  ? 43.073 -8.560  -1.627  1.00 16.57 ?  82  VAL   B HB   1 
ATOM   5161 H HG11 . VAL   B 1 82  ? 43.489 -8.975  -3.971  1.00 18.29 ?  82  VAL   B HG11 1 
ATOM   5162 H HG12 . VAL   B 1 82  ? 44.775 -8.674  -3.089  1.00 18.29 ?  82  VAL   B HG12 1 
ATOM   5163 H HG13 . VAL   B 1 82  ? 44.418 -10.170 -3.493  1.00 18.29 ?  82  VAL   B HG13 1 
ATOM   5164 H HG21 . VAL   B 1 82  ? 41.422 -9.510  -2.981  1.00 17.92 ?  82  VAL   B HG21 1 
ATOM   5165 H HG22 . VAL   B 1 82  ? 41.960 -10.953 -2.593  1.00 17.92 ?  82  VAL   B HG22 1 
ATOM   5166 H HG23 . VAL   B 1 82  ? 41.311 -10.022 -1.482  1.00 17.92 ?  82  VAL   B HG23 1 
ATOM   5167 N N    . LEU   B 1 83  ? 46.388 -10.333 -0.981  1.00 12.64 ?  83  LEU   B N    1 
ATOM   5168 C CA   . LEU   B 1 83  ? 47.746 -9.817  -0.855  1.00 12.87 ?  83  LEU   B CA   1 
ATOM   5169 C C    . LEU   B 1 83  ? 48.447 -9.963  -2.206  1.00 12.73 ?  83  LEU   B C    1 
ATOM   5170 O O    . LEU   B 1 83  ? 47.846 -10.384 -3.198  1.00 12.24 ?  83  LEU   B O    1 
ATOM   5171 C CB   . LEU   B 1 83  ? 48.491 -10.503 0.299   1.00 13.40 ?  83  LEU   B CB   1 
ATOM   5172 C CG   . LEU   B 1 83  ? 47.982 -10.130 1.697   1.00 14.35 ?  83  LEU   B CG   1 
ATOM   5173 C CD1  . LEU   B 1 83  ? 48.595 -11.009 2.773   1.00 14.69 ?  83  LEU   B CD1  1 
ATOM   5174 C CD2  . LEU   B 1 83  ? 48.208 -8.646  2.017   1.00 15.29 ?  83  LEU   B CD2  1 
ATOM   5175 H H    . LEU   B 1 83  ? 46.348 -11.130 -1.312  1.00 15.19 ?  83  LEU   B H    1 
ATOM   5176 H HA   . LEU   B 1 83  ? 47.694 -8.876  -0.657  1.00 15.47 ?  83  LEU   B HA   1 
ATOM   5177 H HB2  . LEU   B 1 83  ? 48.401 -11.464 0.202   1.00 16.10 ?  83  LEU   B HB2  1 
ATOM   5178 H HB3  . LEU   B 1 83  ? 49.426 -10.256 0.248   1.00 16.10 ?  83  LEU   B HB3  1 
ATOM   5179 H HG   . LEU   B 1 83  ? 47.024 -10.275 1.714   1.00 17.25 ?  83  LEU   B HG   1 
ATOM   5180 H HD11 . LEU   B 1 83  ? 48.243 -10.746 3.637   1.00 17.66 ?  83  LEU   B HD11 1 
ATOM   5181 H HD12 . LEU   B 1 83  ? 48.355 -11.937 2.591   1.00 17.66 ?  83  LEU   B HD12 1 
ATOM   5182 H HD13 . LEU   B 1 83  ? 49.556 -10.911 2.757   1.00 17.66 ?  83  LEU   B HD13 1 
ATOM   5183 H HD21 . LEU   B 1 83  ? 48.003 -8.489  2.952   1.00 18.38 ?  83  LEU   B HD21 1 
ATOM   5184 H HD22 . LEU   B 1 83  ? 49.134 -8.420  1.838   1.00 18.38 ?  83  LEU   B HD22 1 
ATOM   5185 H HD23 . LEU   B 1 83  ? 47.624 -8.106  1.457   1.00 18.38 ?  83  LEU   B HD23 1 
ATOM   5186 N N    . SER   B 1 84  ? 49.722 -9.593  -2.256  1.00 13.53 ?  84  SER   B N    1 
ATOM   5187 C CA   . SER   B 1 84  ? 50.463 -9.710  -3.501  1.00 13.83 ?  84  SER   B CA   1 
ATOM   5188 C C    . SER   B 1 84  ? 50.615 -11.172 -3.916  1.00 12.85 ?  84  SER   B C    1 
ATOM   5189 O O    . SER   B 1 84  ? 50.725 -12.076 -3.084  1.00 12.69 ?  84  SER   B O    1 
ATOM   5190 C CB   . SER   B 1 84  ? 51.855 -9.101  -3.346  1.00 15.71 ?  84  SER   B CB   1 
ATOM   5191 O OG   . SER   B 1 84  ? 52.602 -9.323  -4.523  1.00 17.57 ?  84  SER   B OG   1 
ATOM   5192 H H    . SER   B 1 84  ? 50.165 -9.261  -1.598  1.00 16.26 ?  84  SER   B H    1 
ATOM   5193 H HA   . SER   B 1 84  ? 49.997 -9.237  -4.208  1.00 16.62 ?  84  SER   B HA   1 
ATOM   5194 H HB2  . SER   B 1 84  ? 51.770 -8.144  -3.181  1.00 18.88 ?  84  SER   B HB2  1 
ATOM   5195 H HB3  . SER   B 1 84  ? 52.312 -9.524  -2.604  1.00 18.88 ?  84  SER   B HB3  1 
ATOM   5196 H HG   . SER   B 1 84  ? 53.367 -8.965  -4.451  1.00 21.11 ?  84  SER   B HG   1 
ATOM   5197 N N    . GLY   B 1 85  ? 50.670 -11.389 -5.223  1.00 13.80 ?  85  GLY   B N    1 
ATOM   5198 C CA   . GLY   B 1 85  ? 51.016 -12.675 -5.781  1.00 14.27 ?  85  GLY   B CA   1 
ATOM   5199 C C    . GLY   B 1 85  ? 52.491 -12.877 -6.069  1.00 13.92 ?  85  GLY   B C    1 
ATOM   5200 O O    . GLY   B 1 85  ? 52.871 -13.959 -6.521  1.00 14.20 ?  85  GLY   B O    1 
ATOM   5201 H H    . GLY   B 1 85  ? 50.521 -10.792 -5.816  1.00 16.59 ?  85  GLY   B H    1 
ATOM   5202 H HA2  . GLY   B 1 85  ? 50.737 -13.374 -5.167  1.00 17.15 ?  85  GLY   B HA2  1 
ATOM   5203 H HA3  . GLY   B 1 85  ? 50.537 -12.800 -6.612  1.00 17.15 ?  85  GLY   B HA3  1 
ATOM   5204 N N    . HIS   B 1 86  ? 53.346 -11.882 -5.841  1.00 13.87 ?  86  HIS   B N    1 
ATOM   5205 C CA   . HIS   B 1 86  ? 54.812 -12.055 -5.918  1.00 13.60 ?  86  HIS   B CA   1 
ATOM   5206 C C    . HIS   B 1 86  ? 55.188 -12.568 -7.307  1.00 14.09 ?  86  HIS   B C    1 
ATOM   5207 O O    . HIS   B 1 86  ? 54.794 -11.955 -8.313  1.00 14.91 ?  86  HIS   B O    1 
ATOM   5208 C CB   . HIS   B 1 86  ? 55.289 -12.899 -4.739  1.00 14.03 ?  86  HIS   B CB   1 
ATOM   5209 C CG   . HIS   B 1 86  ? 54.981 -12.288 -3.414  1.00 14.19 ?  86  HIS   B CG   1 
ATOM   5210 N ND1  . HIS   B 1 86  ? 55.818 -11.382 -2.796  1.00 15.74 ?  86  HIS   B ND1  1 
ATOM   5211 C CD2  . HIS   B 1 86  ? 53.904 -12.425 -2.602  1.00 14.55 ?  86  HIS   B CD2  1 
ATOM   5212 C CE1  . HIS   B 1 86  ? 55.269 -10.994 -1.658  1.00 15.40 ?  86  HIS   B CE1  1 
ATOM   5213 N NE2  . HIS   B 1 86  ? 54.105 -11.606 -1.520  1.00 14.90 ?  86  HIS   B NE2  1 
ATOM   5214 H H    . HIS   B 1 86  ? 53.108 -11.082 -5.646  1.00 16.67 ?  86  HIS   B H    1 
ATOM   5215 H HA   . HIS   B 1 86  ? 55.223 -11.186 -5.818  1.00 16.35 ?  86  HIS   B HA   1 
ATOM   5216 H HB2  . HIS   B 1 86  ? 54.860 -13.769 -4.776  1.00 16.86 ?  86  HIS   B HB2  1 
ATOM   5217 H HB3  . HIS   B 1 86  ? 56.253 -13.005 -4.795  1.00 16.86 ?  86  HIS   B HB3  1 
ATOM   5218 H HD2  . HIS   B 1 86  ? 53.154 -12.960 -2.756  1.00 17.49 ?  86  HIS   B HD2  1 
ATOM   5219 H HE1  . HIS   B 1 86  ? 55.644 -10.400 -1.051  1.00 18.51 ?  86  HIS   B HE1  1 
ATOM   5220 H HE2  . HIS   B 1 86  ? 53.569 -11.519 -0.849  1.00 17.90 ?  86  HIS   B HE2  1 
ATOM   5221 N N    . ASN   B 1 87  ? 55.963 -13.648 -7.414  1.00 14.47 ?  87  ASN   B N    1 
ATOM   5222 C CA   . ASN   B 1 87  ? 56.355 -14.223 -8.691  1.00 15.22 ?  87  ASN   B CA   1 
ATOM   5223 C C    . ASN   B 1 87  ? 55.362 -15.259 -9.196  1.00 15.04 ?  87  ASN   B C    1 
ATOM   5224 O O    . ASN   B 1 87  ? 55.667 -15.968 -10.161 1.00 16.59 ?  87  ASN   B O    1 
ATOM   5225 C CB   . ASN   B 1 87  ? 57.746 -14.859 -8.580  1.00 16.93 ?  87  ASN   B CB   1 
ATOM   5226 C CG   . ASN   B 1 87  ? 57.801 -15.966 -7.537  1.00 17.64 ?  87  ASN   B CG   1 
ATOM   5227 O OD1  . ASN   B 1 87  ? 57.166 -15.880 -6.483  1.00 17.20 ?  87  ASN   B OD1  1 
ATOM   5228 N ND2  . ASN   B 1 87  ? 58.550 -17.032 -7.841  1.00 19.81 ?  87  ASN   B ND2  1 
ATOM   5229 H H    . ASN   B 1 87  ? 56.289 -14.076 -6.735  1.00 17.39 ?  87  ASN   B H    1 
ATOM   5230 H HA   . ASN   B 1 87  ? 56.402 -13.514 -9.348  1.00 18.30 ?  87  ASN   B HA   1 
ATOM   5231 H HB2  . ASN   B 1 87  ? 57.985 -15.240 -9.440  1.00 20.35 ?  87  ASN   B HB2  1 
ATOM   5232 H HB3  . ASN   B 1 87  ? 58.385 -14.177 -8.328  1.00 20.35 ?  87  ASN   B HB3  1 
ATOM   5233 H HD21 . ASN   B 1 87  ? 58.617 -17.685 -7.287  1.00 23.80 ?  87  ASN   B HD21 1 
ATOM   5234 H HD22 . ASN   B 1 87  ? 58.977 -17.059 -8.590  1.00 23.80 ?  87  ASN   B HD22 1 
ATOM   5235 N N    . LEU   B 1 88  ? 54.185 -15.362 -8.573  1.00 13.77 ?  88  LEU   B N    1 
ATOM   5236 C CA   . LEU   B 1 88  ? 53.208 -16.396 -8.903  1.00 13.91 ?  88  LEU   B CA   1 
ATOM   5237 C C    . LEU   B 1 88  ? 51.976 -15.886 -9.629  1.00 13.80 ?  88  LEU   B C    1 
ATOM   5238 O O    . LEU   B 1 88  ? 51.371 -16.642 -10.397 1.00 15.44 ?  88  LEU   B O    1 
ATOM   5239 C CB   . LEU   B 1 88  ? 52.737 -17.092 -7.623  1.00 15.07 ?  88  LEU   B CB   1 
ATOM   5240 C CG   . LEU   B 1 88  ? 53.853 -17.730 -6.807  1.00 17.26 ?  88  LEU   B CG   1 
ATOM   5241 C CD1  . LEU   B 1 88  ? 53.332 -18.153 -5.443  1.00 18.58 ?  88  LEU   B CD1  1 
ATOM   5242 C CD2  . LEU   B 1 88  ? 54.433 -18.912 -7.562  1.00 20.23 ?  88  LEU   B CD2  1 
ATOM   5243 H H    . LEU   B 1 88  ? 53.928 -14.833 -7.933  1.00 16.55 ?  88  LEU   B H    1 
ATOM   5244 H HA   . LEU   B 1 88  ? 53.629 -17.053 -9.461  1.00 16.72 ?  88  LEU   B HA   1 
ATOM   5245 H HB2  . LEU   B 1 88  ? 52.287 -16.449 -7.052  1.00 18.11 ?  88  LEU   B HB2  1 
ATOM   5246 H HB3  . LEU   B 1 88  ? 52.112 -17.800 -7.866  1.00 18.11 ?  88  LEU   B HB3  1 
ATOM   5247 H HG   . LEU   B 1 88  ? 54.557 -17.082 -6.669  1.00 20.74 ?  88  LEU   B HG   1 
ATOM   5248 H HD11 . LEU   B 1 88  ? 54.000 -18.701 -5.003  1.00 22.33 ?  88  LEU   B HD11 1 
ATOM   5249 H HD12 . LEU   B 1 88  ? 53.149 -17.362 -4.913  1.00 22.33 ?  88  LEU   B HD12 1 
ATOM   5250 H HD13 . LEU   B 1 88  ? 52.515 -18.665 -5.564  1.00 22.33 ?  88  LEU   B HD13 1 
ATOM   5251 H HD21 . LEU   B 1 88  ? 55.067 -19.370 -6.988  1.00 24.31 ?  88  LEU   B HD21 1 
ATOM   5252 H HD22 . LEU   B 1 88  ? 53.714 -19.512 -7.809  1.00 24.31 ?  88  LEU   B HD22 1 
ATOM   5253 H HD23 . LEU   B 1 88  ? 54.882 -18.585 -8.357  1.00 24.31 ?  88  LEU   B HD23 1 
ATOM   5254 N N    . ALA   B 1 89  ? 51.574 -14.647 -9.377  1.00 13.31 ?  89  ALA   B N    1 
ATOM   5255 C CA   . ALA   B 1 89  ? 50.276 -14.162 -9.819  1.00 12.74 ?  89  ALA   B CA   1 
ATOM   5256 C C    . ALA   B 1 89  ? 50.243 -12.670 -9.546  1.00 13.33 ?  89  ALA   B C    1 
ATOM   5257 O O    . ALA   B 1 89  ? 51.086 -12.140 -8.821  1.00 14.04 ?  89  ALA   B O    1 
ATOM   5258 C CB   . ALA   B 1 89  ? 49.146 -14.841 -9.052  1.00 13.02 ?  89  ALA   B CB   1 
ATOM   5259 H H    . ALA   B 1 89  ? 52.035 -14.055 -8.948  1.00 16.00 ?  89  ALA   B H    1 
ATOM   5260 H HA   . ALA   B 1 89  ? 50.160 -14.316 -10.771 1.00 15.32 ?  89  ALA   B HA   1 
ATOM   5261 H HB1  . ALA   B 1 89  ? 48.297 -14.507 -9.381  1.00 15.65 ?  89  ALA   B HB1  1 
ATOM   5262 H HB2  . ALA   B 1 89  ? 49.205 -15.798 -9.199  1.00 15.65 ?  89  ALA   B HB2  1 
ATOM   5263 H HB3  . ALA   B 1 89  ? 49.243 -14.640 -8.112  1.00 15.65 ?  89  ALA   B HB3  1 
ATOM   5264 N N    . LYS   B 1 90  ? 49.246 -11.986 -10.105 1.00 13.98 ?  90  LYS   B N    1 
ATOM   5265 C CA   . LYS   B 1 90  ? 49.061 -10.595 -9.708  1.00 14.21 ?  90  LYS   B CA   1 
ATOM   5266 C C    . LYS   B 1 90  ? 48.747 -10.515 -8.218  1.00 13.76 ?  90  LYS   B C    1 
ATOM   5267 O O    . LYS   B 1 90  ? 49.386 -9.754  -7.472  1.00 15.03 ?  90  LYS   B O    1 
ATOM   5268 C CB   . LYS   B 1 90  ? 47.981 -9.935  -10.566 1.00 15.80 ?  90  LYS   B CB   1 
ATOM   5269 C CG   . LYS   B 1 90  ? 47.699 -8.490  -10.211 1.00 16.39 ?  90  LYS   B CG   1 
ATOM   5270 C CD   . LYS   B 1 90  ? 48.913 -7.603  -10.290 1.00 18.96 ?  90  LYS   B CD   1 
ATOM   5271 C CE   . LYS   B 1 90  ? 48.480 -6.179  -10.040 1.00 20.68 ?  90  LYS   B CE   1 
ATOM   5272 N NZ   . LYS   B 1 90  ? 49.633 -5.260  -9.937  1.00 20.57 ?  90  LYS   B NZ   1 
ATOM   5273 H H    . LYS   B 1 90  ? 48.686 -12.294 -10.683 1.00 16.80 ?  90  LYS   B H    1 
ATOM   5274 H HA   . LYS   B 1 90  ? 49.888 -10.121 -9.861  1.00 17.09 ?  90  LYS   B HA   1 
ATOM   5275 H HB2  . LYS   B 1 90  ? 48.267 -9.959  -11.498 1.00 18.99 ?  90  LYS   B HB2  1 
ATOM   5276 H HB3  . LYS   B 1 90  ? 47.154 -10.430 -10.471 1.00 18.99 ?  90  LYS   B HB3  1 
ATOM   5277 H HG2  . LYS   B 1 90  ? 47.038 -8.137  -10.828 1.00 19.70 ?  90  LYS   B HG2  1 
ATOM   5278 H HG3  . LYS   B 1 90  ? 47.358 -8.447  -9.305  1.00 19.70 ?  90  LYS   B HG3  1 
ATOM   5279 H HD2  . LYS   B 1 90  ? 49.555 -7.858  -9.608  1.00 22.78 ?  90  LYS   B HD2  1 
ATOM   5280 H HD3  . LYS   B 1 90  ? 49.310 -7.660  -11.174 1.00 22.78 ?  90  LYS   B HD3  1 
ATOM   5281 H HE2  . LYS   B 1 90  ? 47.923 -5.874  -10.776 1.00 24.84 ?  90  LYS   B HE2  1 
ATOM   5282 H HE3  . LYS   B 1 90  ? 47.987 -6.129  -9.207  1.00 24.84 ?  90  LYS   B HE3  1 
ATOM   5283 H HZ1  . LYS   B 1 90  ? 49.354 -4.424  -9.792  1.00 24.71 ?  90  LYS   B HZ1  1 
ATOM   5284 H HZ2  . LYS   B 1 90  ? 50.164 -5.504  -9.265  1.00 24.71 ?  90  LYS   B HZ2  1 
ATOM   5285 H HZ3  . LYS   B 1 90  ? 50.106 -5.272  -10.694 1.00 24.71 ?  90  LYS   B HZ3  1 
ATOM   5286 N N    . HIS   B 1 91  ? 47.791 -11.333 -7.764  1.00 12.50 ?  91  HIS   B N    1 
ATOM   5287 C CA   . HIS   B 1 91  ? 47.323 -11.345 -6.392  1.00 12.67 ?  91  HIS   B CA   1 
ATOM   5288 C C    . HIS   B 1 91  ? 47.315 -12.767 -5.866  1.00 11.93 ?  91  HIS   B C    1 
ATOM   5289 O O    . HIS   B 1 91  ? 47.087 -13.725 -6.616  1.00 12.27 ?  91  HIS   B O    1 
ATOM   5290 C CB   . HIS   B 1 91  ? 45.867 -10.864 -6.287  1.00 14.62 ?  91  HIS   B CB   1 
ATOM   5291 C CG   . HIS   B 1 91  ? 45.659 -9.457  -6.730  1.00 17.49 ?  91  HIS   B CG   1 
ATOM   5292 N ND1  . HIS   B 1 91  ? 46.256 -8.382  -6.107  1.00 19.58 ?  91  HIS   B ND1  1 
ATOM   5293 C CD2  . HIS   B 1 91  ? 44.886 -8.942  -7.712  1.00 19.62 ?  91  HIS   B CD2  1 
ATOM   5294 C CE1  . HIS   B 1 91  ? 45.882 -7.264  -6.707  1.00 20.68 ?  91  HIS   B CE1  1 
ATOM   5295 N NE2  . HIS   B 1 91  ? 45.044 -7.577  -7.680  1.00 20.83 ?  91  HIS   B NE2  1 
ATOM   5296 H H    . HIS   B 1 91  ? 47.385 -11.913 -8.258  1.00 15.03 ?  91  HIS   B H    1 
ATOM   5297 H HA   . HIS   B 1 91  ? 47.893 -10.779 -5.834  1.00 15.23 ?  91  HIS   B HA   1 
ATOM   5298 H HB2  . HIS   B 1 91  ? 45.313 -11.432 -6.842  1.00 17.57 ?  91  HIS   B HB2  1 
ATOM   5299 H HB3  . HIS   B 1 91  ? 45.583 -10.931 -5.361  1.00 17.57 ?  91  HIS   B HB3  1 
ATOM   5300 H HD1  . HIS   B 1 91  ? 46.801 -8.430  -5.439  1.00 23.52 ?  91  HIS   B HD1  1 
ATOM   5301 H HD2  . HIS   B 1 91  ? 44.358 -9.417  -8.307  1.00 23.58 ?  91  HIS   B HD2  1 
ATOM   5302 H HE1  . HIS   B 1 91  ? 46.156 -6.403  -6.471  1.00 24.84 ?  91  HIS   B HE1  1 
ATOM   5303 N N    . CYS   B 1 92  ? 47.504 -12.891 -4.561  1.00 11.67 ?  92  CYS   B N    1 
ATOM   5304 C CA   . CYS   B 1 92  ? 47.205 -14.130 -3.855  1.00 11.68 ?  92  CYS   B CA   1 
ATOM   5305 C C    . CYS   B 1 92  ? 45.988 -13.897 -2.973  1.00 11.29 ?  92  CYS   B C    1 
ATOM   5306 O O    . CYS   B 1 92  ? 45.987 -12.995 -2.126  1.00 12.07 ?  92  CYS   B O    1 
ATOM   5307 C CB   . CYS   B 1 92  ? 48.381 -14.591 -3.000  1.00 12.19 ?  92  CYS   B CB   1 
ATOM   5308 S SG   . CYS   B 1 92  ? 48.026 -16.121 -2.084  1.00 12.64 ?  92  CYS   B SG   1 
ATOM   5309 H H    . CYS   B 1 92  ? 47.822 -12.269 -4.054  1.00 14.03 ?  92  CYS   B H    1 
ATOM   5310 H HA   . CYS   B 1 92  ? 47.001 -14.823 -4.504  1.00 14.05 ?  92  CYS   B HA   1 
ATOM   5311 H HB2  . CYS   B 1 92  ? 49.142 -14.753 -3.573  1.00 14.66 ?  92  CYS   B HB2  1 
ATOM   5312 H HB3  . CYS   B 1 92  ? 48.584 -13.899 -2.355  1.00 14.66 ?  92  CYS   B HB3  1 
ATOM   5313 H HG   . CYS   B 1 92  ? 49.001 -16.429 -1.454  1.00 15.19 ?  92  CYS   B HG   1 
ATOM   5314 N N    . LEU   B 1 93  ? 44.951 -14.704 -3.182  1.00 11.37 ?  93  LEU   B N    1 
ATOM   5315 C CA   . LEU   B 1 93  ? 43.775 -14.704 -2.323  1.00 11.54 ?  93  LEU   B CA   1 
ATOM   5316 C C    . LEU   B 1 93  ? 43.997 -15.764 -1.251  1.00 10.99 ?  93  LEU   B C    1 
ATOM   5317 O O    . LEU   B 1 93  ? 43.946 -16.969 -1.537  1.00 11.81 ?  93  LEU   B O    1 
ATOM   5318 C CB   . LEU   B 1 93  ? 42.514 -15.012 -3.125  1.00 12.06 ?  93  LEU   B CB   1 
ATOM   5319 C CG   . LEU   B 1 93  ? 41.215 -15.013 -2.319  1.00 12.39 ?  93  LEU   B CG   1 
ATOM   5320 C CD1  . LEU   B 1 93  ? 40.863 -13.616 -1.844  1.00 12.98 ?  93  LEU   B CD1  1 
ATOM   5321 C CD2  . LEU   B 1 93  ? 40.077 -15.618 -3.133  1.00 12.98 ?  93  LEU   B CD2  1 
ATOM   5322 H H    . LEU   B 1 93  ? 44.911 -15.280 -3.829  1.00 13.68 ?  93  LEU   B H    1 
ATOM   5323 H HA   . LEU   B 1 93  ? 43.682 -13.838 -1.900  1.00 13.88 ?  93  LEU   B HA   1 
ATOM   5324 H HB2  . LEU   B 1 93  ? 42.423 -14.341 -3.821  1.00 14.50 ?  93  LEU   B HB2  1 
ATOM   5325 H HB3  . LEU   B 1 93  ? 42.610 -15.886 -3.527  1.00 14.50 ?  93  LEU   B HB3  1 
ATOM   5326 H HG   . LEU   B 1 93  ? 41.337 -15.567 -1.535  1.00 14.89 ?  93  LEU   B HG   1 
ATOM   5327 H HD11 . LEU   B 1 93  ? 40.007 -13.642 -1.392  1.00 15.60 ?  93  LEU   B HD11 1 
ATOM   5328 H HD12 . LEU   B 1 93  ? 41.552 -13.305 -1.236  1.00 15.60 ?  93  LEU   B HD12 1 
ATOM   5329 H HD13 . LEU   B 1 93  ? 40.812 -13.024 -2.614  1.00 15.60 ?  93  LEU   B HD13 1 
ATOM   5330 H HD21 . LEU   B 1 93  ? 39.267 -15.609 -2.601  1.00 15.61 ?  93  LEU   B HD21 1 
ATOM   5331 H HD22 . LEU   B 1 93  ? 39.951 -15.099 -3.941  1.00 15.61 ?  93  LEU   B HD22 1 
ATOM   5332 H HD23 . LEU   B 1 93  ? 40.307 -16.536 -3.364  1.00 15.61 ?  93  LEU   B HD23 1 
ATOM   5333 N N    . HIS   B 1 94  ? 44.271 -15.332 -0.028  1.00 11.44 ?  94  HIS   B N    1 
ATOM   5334 C CA   . HIS   B 1 94  ? 44.493 -16.237 1.094   1.00 11.55 ?  94  HIS   B CA   1 
ATOM   5335 C C    . HIS   B 1 94  ? 43.131 -16.590 1.677   1.00 12.15 ?  94  HIS   B C    1 
ATOM   5336 O O    . HIS   B 1 94  ? 42.461 -15.717 2.233   1.00 13.21 ?  94  HIS   B O    1 
ATOM   5337 C CB   . HIS   B 1 94  ? 45.362 -15.552 2.149   1.00 11.74 ?  94  HIS   B CB   1 
ATOM   5338 C CG   . HIS   B 1 94  ? 46.745 -15.252 1.685   1.00 11.80 ?  94  HIS   B CG   1 
ATOM   5339 N ND1  . HIS   B 1 94  ? 47.767 -16.173 1.770   1.00 12.13 ?  94  HIS   B ND1  1 
ATOM   5340 C CD2  . HIS   B 1 94  ? 47.260 -14.144 1.099   1.00 12.18 ?  94  HIS   B CD2  1 
ATOM   5341 C CE1  . HIS   B 1 94  ? 48.861 -15.622 1.273   1.00 12.09 ?  94  HIS   B CE1  1 
ATOM   5342 N NE2  . HIS   B 1 94  ? 48.583 -14.397 0.856   1.00 12.56 ?  94  HIS   B NE2  1 
ATOM   5343 H H    . HIS   B 1 94  ? 44.344 -14.496 0.179   1.00 13.75 ?  94  HIS   B H    1 
ATOM   5344 H HA   . HIS   B 1 94  ? 44.928 -17.046 0.786   1.00 13.89 ?  94  HIS   B HA   1 
ATOM   5345 H HB2  . HIS   B 1 94  ? 44.939 -14.717 2.397   1.00 14.11 ?  94  HIS   B HB2  1 
ATOM   5346 H HB3  . HIS   B 1 94  ? 45.423 -16.136 2.916   1.00 14.11 ?  94  HIS   B HB3  1 
ATOM   5347 H HD2  . HIS   B 1 94  ? 46.808 -13.356 0.901   1.00 14.64 ?  94  HIS   B HD2  1 
ATOM   5348 H HE1  . HIS   B 1 94  ? 49.689 -16.040 1.219   1.00 14.53 ?  94  HIS   B HE1  1 
ATOM   5349 H HE2  . HIS   B 1 94  ? 49.146 -13.856 0.495   1.00 15.10 ?  94  HIS   B HE2  1 
ATOM   5350 N N    . VAL   B 1 95  ? 42.700 -17.846 1.528   1.00 11.63 ?  95  VAL   B N    1 
ATOM   5351 C CA   . VAL   B 1 95  ? 41.372 -18.280 1.963   1.00 12.00 ?  95  VAL   B CA   1 
ATOM   5352 C C    . VAL   B 1 95  ? 41.536 -19.316 3.062   1.00 12.41 ?  95  VAL   B C    1 
ATOM   5353 O O    . VAL   B 1 95  ? 42.312 -20.270 2.910   1.00 12.70 ?  95  VAL   B O    1 
ATOM   5354 C CB   . VAL   B 1 95  ? 40.552 -18.886 0.808   1.00 12.08 ?  95  VAL   B CB   1 
ATOM   5355 C CG1  . VAL   B 1 95  ? 39.179 -19.340 1.302   1.00 13.39 ?  95  VAL   B CG1  1 
ATOM   5356 C CG2  . VAL   B 1 95  ? 40.418 -17.904 -0.336  1.00 12.25 ?  95  VAL   B CG2  1 
ATOM   5357 H H    . VAL   B 1 95  ? 43.162 -18.476 1.167   1.00 13.98 ?  95  VAL   B H    1 
ATOM   5358 H HA   . VAL   B 1 95  ? 40.879 -17.525 2.321   1.00 14.43 ?  95  VAL   B HA   1 
ATOM   5359 H HB   . VAL   B 1 95  ? 41.012 -19.665 0.470   1.00 14.53 ?  95  VAL   B HB   1 
ATOM   5360 H HG11 . VAL   B 1 95  ? 38.608 -19.521 0.534   1.00 16.09 ?  95  VAL   B HG11 1 
ATOM   5361 H HG12 . VAL   B 1 95  ? 39.278 -20.147 1.830   1.00 16.09 ?  95  VAL   B HG12 1 
ATOM   5362 H HG13 . VAL   B 1 95  ? 38.783 -18.637 1.841   1.00 16.09 ?  95  VAL   B HG13 1 
ATOM   5363 H HG21 . VAL   B 1 95  ? 39.844 -18.291 -1.018  1.00 14.73 ?  95  VAL   B HG21 1 
ATOM   5364 H HG22 . VAL   B 1 95  ? 40.018 -17.083 -0.000  1.00 14.73 ?  95  VAL   B HG22 1 
ATOM   5365 H HG23 . VAL   B 1 95  ? 41.293 -17.724 -0.699  1.00 14.73 ?  95  VAL   B HG23 1 
ATOM   5366 N N    . VAL   B 1 96  ? 40.793 -19.148 4.153   1.00 12.43 ?  96  VAL   B N    1 
ATOM   5367 C CA   . VAL   B 1 96  ? 40.876 -20.052 5.299   1.00 12.84 ?  96  VAL   B CA   1 
ATOM   5368 C C    . VAL   B 1 96  ? 39.688 -21.012 5.258   1.00 13.65 ?  96  VAL   B C    1 
ATOM   5369 O O    . VAL   B 1 96  ? 38.565 -20.652 5.628   1.00 14.39 ?  96  VAL   B O    1 
ATOM   5370 C CB   . VAL   B 1 96  ? 40.934 -19.297 6.630   1.00 13.76 ?  96  VAL   B CB   1 
ATOM   5371 C CG1  . VAL   B 1 96  ? 41.110 -20.285 7.780   1.00 14.36 ?  96  VAL   B CG1  1 
ATOM   5372 C CG2  . VAL   B 1 96  ? 42.051 -18.269 6.627   1.00 14.18 ?  96  VAL   B CG2  1 
ATOM   5373 H H    . VAL   B 1 96  ? 40.221 -18.513 4.256   1.00 14.94 ?  96  VAL   B H    1 
ATOM   5374 H HA   . VAL   B 1 96  ? 41.686 -20.582 5.226   1.00 15.44 ?  96  VAL   B HA   1 
ATOM   5375 H HB   . VAL   B 1 96  ? 40.095 -18.827 6.765   1.00 16.54 ?  96  VAL   B HB   1 
ATOM   5376 H HG11 . VAL   B 1 96  ? 41.305 -19.790 8.592   1.00 17.26 ?  96  VAL   B HG11 1 
ATOM   5377 H HG12 . VAL   B 1 96  ? 40.294 -20.794 7.891   1.00 17.26 ?  96  VAL   B HG12 1 
ATOM   5378 H HG13 . VAL   B 1 96  ? 41.849 -20.879 7.572   1.00 17.26 ?  96  VAL   B HG13 1 
ATOM   5379 H HG21 . VAL   B 1 96  ? 42.101 -17.853 7.505   1.00 17.04 ?  96  VAL   B HG21 1 
ATOM   5380 H HG22 . VAL   B 1 96  ? 42.888 -18.709 6.422   1.00 17.04 ?  96  VAL   B HG22 1 
ATOM   5381 H HG23 . VAL   B 1 96  ? 41.858 -17.592 5.956   1.00 17.04 ?  96  VAL   B HG23 1 
ATOM   5382 N N    . GLY   B 1 97  ? 39.930 -22.249 4.831   1.00 13.31 ?  97  GLY   B N    1 
ATOM   5383 C CA   . GLY   B 1 97  ? 38.953 -23.302 4.977   1.00 14.14 ?  97  GLY   B CA   1 
ATOM   5384 C C    . GLY   B 1 97  ? 39.065 -23.914 6.356   1.00 15.20 ?  97  GLY   B C    1 
ATOM   5385 O O    . GLY   B 1 97  ? 40.101 -23.788 7.023   1.00 15.18 ?  97  GLY   B O    1 
ATOM   5386 H H    . GLY   B 1 97  ? 40.666 -22.493 4.450   1.00 16.00 ?  97  GLY   B H    1 
ATOM   5387 H HA2  . GLY   B 1 97  ? 38.062 -22.930 4.855   1.00 17.00 ?  97  GLY   B HA2  1 
ATOM   5388 H HA3  . GLY   B 1 97  ? 39.102 -23.982 4.302   1.00 17.00 ?  97  GLY   B HA3  1 
ATOM   5389 N N    . PRO   B 1 98  ? 38.013 -24.592 6.815   1.00 15.73 ?  98  PRO   B N    1 
ATOM   5390 C CA   . PRO   B 1 98  ? 38.099 -25.282 8.106   1.00 16.38 ?  98  PRO   B CA   1 
ATOM   5391 C C    . PRO   B 1 98  ? 39.129 -26.403 8.071   1.00 16.15 ?  98  PRO   B C    1 
ATOM   5392 O O    . PRO   B 1 98  ? 39.246 -27.138 7.089   1.00 16.38 ?  98  PRO   B O    1 
ATOM   5393 C CB   . PRO   B 1 98  ? 36.680 -25.825 8.307   1.00 16.29 ?  98  PRO   B CB   1 
ATOM   5394 C CG   . PRO   B 1 98  ? 36.143 -25.981 6.938   1.00 16.10 ?  98  PRO   B CG   1 
ATOM   5395 C CD   . PRO   B 1 98  ? 36.699 -24.800 6.179   1.00 15.65 ?  98  PRO   B CD   1 
ATOM   5396 H HA   . PRO   B 1 98  ? 38.321 -24.655 8.810   1.00 19.69 ?  98  PRO   B HA   1 
ATOM   5397 H HB2  . PRO   B 1 98  ? 36.724 -26.683 8.763   1.00 19.58 ?  98  PRO   B HB2  1 
ATOM   5398 H HB3  . PRO   B 1 98  ? 36.158 -25.190 8.815   1.00 19.58 ?  98  PRO   B HB3  1 
ATOM   5399 H HG2  . PRO   B 1 98  ? 36.459 -26.817 6.552   1.00 19.35 ?  98  PRO   B HG2  1 
ATOM   5400 H HG3  . PRO   B 1 98  ? 35.177 -25.955 6.958   1.00 19.35 ?  98  PRO   B HG3  1 
ATOM   5401 H HD2  . PRO   B 1 98  ? 36.801 -25.018 5.237   1.00 18.81 ?  98  PRO   B HD2  1 
ATOM   5402 H HD3  . PRO   B 1 98  ? 36.138 -24.021 6.306   1.00 18.81 ?  98  PRO   B HD3  1 
ATOM   5403 N N    . ASN   B 1 99  ? 39.891 -26.517 9.155   1.00 17.22 ?  99  ASN   B N    1 
ATOM   5404 C CA   . ASN   B 1 99  ? 40.873 -27.588 9.325   1.00 18.26 ?  99  ASN   B CA   1 
ATOM   5405 C C    . ASN   B 1 99  ? 40.246 -28.662 10.209  1.00 20.93 ?  99  ASN   B C    1 
ATOM   5406 O O    . ASN   B 1 99  ? 40.186 -28.516 11.432  1.00 21.70 ?  99  ASN   B O    1 
ATOM   5407 C CB   . ASN   B 1 99  ? 42.144 -27.030 9.950   1.00 18.42 ?  99  ASN   B CB   1 
ATOM   5408 C CG   . ASN   B 1 99  ? 43.280 -28.035 9.958   1.00 19.16 ?  99  ASN   B CG   1 
ATOM   5409 O OD1  . ASN   B 1 99  ? 43.061 -29.232 10.123  1.00 19.98 ?  99  ASN   B OD1  1 
ATOM   5410 N ND2  . ASN   B 1 99  ? 44.498 -27.553 9.771   1.00 19.41 ?  99  ASN   B ND2  1 
ATOM   5411 H H    . ASN   B 1 99  ? 39.852 -25.974 9.821   1.00 20.70 ?  99  ASN   B H    1 
ATOM   5412 H HA   . ASN   B 1 99  ? 41.085 -27.979 8.465   1.00 21.94 ?  99  ASN   B HA   1 
ATOM   5413 H HB2  . ASN   B 1 99  ? 42.426 -26.253 9.448   1.00 22.13 ?  99  ASN   B HB2  1 
ATOM   5414 H HB3  . ASN   B 1 99  ? 41.954 -26.780 10.871  1.00 22.13 ?  99  ASN   B HB3  1 
ATOM   5415 H HD21 . ASN   B 1 99  ? 45.172 -28.081 9.765   1.00 23.31 ?  99  ASN   B HD21 1 
ATOM   5416 H HD22 . ASN   B 1 99  ? 44.609 -26.706 9.660   1.00 23.31 ?  99  ASN   B HD22 1 
ATOM   5417 N N    A VAL   B 1 100 ? 39.763 -29.738 9.582   0.60 22.47 ?  100 VAL   B N    1 
ATOM   5418 N N    B VAL   B 1 100 ? 39.779 -29.743 9.579   0.40 22.55 ?  100 VAL   B N    1 
ATOM   5419 C CA   A VAL   B 1 100 ? 39.147 -30.826 10.340  0.60 25.25 ?  100 VAL   B CA   1 
ATOM   5420 C CA   B VAL   B 1 100 ? 39.154 -30.837 10.319  0.40 24.98 ?  100 VAL   B CA   1 
ATOM   5421 C C    A VAL   B 1 100 ? 40.155 -31.481 11.276  0.60 26.11 ?  100 VAL   B C    1 
ATOM   5422 C C    B VAL   B 1 100 ? 40.151 -31.500 11.259  0.40 25.89 ?  100 VAL   B C    1 
ATOM   5423 O O    A VAL   B 1 100 ? 39.788 -31.963 12.354  0.60 26.74 ?  100 VAL   B O    1 
ATOM   5424 O O    B VAL   B 1 100 ? 39.773 -32.003 12.324  0.40 26.25 ?  100 VAL   B O    1 
ATOM   5425 C CB   A VAL   B 1 100 ? 38.493 -31.843 9.382   0.60 27.29 ?  100 VAL   B CB   1 
ATOM   5426 C CB   B VAL   B 1 100 ? 38.521 -31.844 9.337   0.40 26.55 ?  100 VAL   B CB   1 
ATOM   5427 C CG1  A VAL   B 1 100 ? 38.010 -33.067 10.146  0.60 28.18 ?  100 VAL   B CG1  1 
ATOM   5428 C CG1  B VAL   B 1 100 ? 38.010 -33.072 10.077  0.40 27.19 ?  100 VAL   B CG1  1 
ATOM   5429 C CG2  A VAL   B 1 100 ? 37.339 -31.194 8.632   0.60 27.78 ?  100 VAL   B CG2  1 
ATOM   5430 C CG2  B VAL   B 1 100 ? 37.395 -31.182 8.558   0.40 26.96 ?  100 VAL   B CG2  1 
ATOM   5431 H H    A VAL   B 1 100 ? 39.763 -29.847 8.728   0.60 26.99 ?  100 VAL   B H    1 
ATOM   5432 H H    B VAL   B 1 100 ? 39.807 -29.859 8.728   0.40 27.09 ?  100 VAL   B H    1 
ATOM   5433 H HA   A VAL   B 1 100 ? 38.437 -30.455 10.888  0.60 30.33 ?  100 VAL   B HA   1 
ATOM   5434 H HA   B VAL   B 1 100 ? 38.438 -30.473 10.860  0.40 30.01 ?  100 VAL   B HA   1 
ATOM   5435 H HB   A VAL   B 1 100 ? 39.150 -32.136 8.734   0.60 32.78 ?  100 VAL   B HB   1 
ATOM   5436 H HB   B VAL   B 1 100 ? 39.193 -32.137 8.702   0.40 31.89 ?  100 VAL   B HB   1 
ATOM   5437 H HG11 A VAL   B 1 100 ? 37.416 -33.579 9.574   0.60 33.84 ?  100 VAL   B HG11 1 
ATOM   5438 H HG11 B VAL   B 1 100 ? 37.433 -33.579 9.482   0.40 32.65 ?  100 VAL   B HG11 1 
ATOM   5439 H HG12 A VAL   B 1 100 ? 38.773 -33.610 10.397  0.60 33.84 ?  100 VAL   B HG12 1 
ATOM   5440 H HG12 B VAL   B 1 100 ? 38.764 -33.619 10.347  0.40 32.65 ?  100 VAL   B HG12 1 
ATOM   5441 H HG13 A VAL   B 1 100 ? 37.532 -32.778 10.939  0.60 33.84 ?  100 VAL   B HG13 1 
ATOM   5442 H HG13 B VAL   B 1 100 ? 37.508 -32.786 10.856  0.40 32.65 ?  100 VAL   B HG13 1 
ATOM   5443 H HG21 A VAL   B 1 100 ? 36.929 -31.855 8.051   0.60 33.37 ?  100 VAL   B HG21 1 
ATOM   5444 H HG21 B VAL   B 1 100 ? 36.989 -31.837 7.970   0.40 32.38 ?  100 VAL   B HG21 1 
ATOM   5445 H HG22 A VAL   B 1 100 ? 36.687 -30.871 9.275   0.60 33.37 ?  100 VAL   B HG22 1 
ATOM   5446 H HG22 B VAL   B 1 100 ? 36.735 -30.846 9.185   0.40 32.38 ?  100 VAL   B HG22 1 
ATOM   5447 H HG23 A VAL   B 1 100 ? 37.680 -30.456 8.106   0.60 33.37 ?  100 VAL   B HG23 1 
ATOM   5448 H HG23 B VAL   B 1 100 ? 37.760 -30.450 8.038   0.40 32.38 ?  100 VAL   B HG23 1 
ATOM   5449 N N    . ASN   B 1 101 ? 41.433 -31.521 10.885  1.00 26.53 ?  101 ASN   B N    1 
ATOM   5450 C CA   . ASN   B 1 101 ? 42.462 -32.072 11.765  1.00 28.46 ?  101 ASN   B CA   1 
ATOM   5451 C C    . ASN   B 1 101 ? 42.661 -31.235 13.024  1.00 30.87 ?  101 ASN   B C    1 
ATOM   5452 O O    . ASN   B 1 101 ? 43.270 -31.720 13.985  1.00 31.81 ?  101 ASN   B O    1 
ATOM   5453 C CB   . ASN   B 1 101 ? 43.789 -32.219 11.016  1.00 28.23 ?  101 ASN   B CB   1 
ATOM   5454 C CG   . ASN   B 1 101 ? 43.778 -33.372 10.034  1.00 28.07 ?  101 ASN   B CG   1 
ATOM   5455 O OD1  . ASN   B 1 101 ? 43.111 -34.374 10.257  1.00 28.84 ?  101 ASN   B OD1  1 
ATOM   5456 N ND2  . ASN   B 1 101 ? 44.513 -33.232 8.939   1.00 27.92 ?  101 ASN   B ND2  1 
ATOM   5457 H H    A ASN   B 1 101 ? 41.722 -31.252 10.121  0.60 31.86 ?  101 ASN   B H    1 
ATOM   5458 H H    B ASN   B 1 101 ? 41.727 -31.234 10.129  0.40 31.86 ?  101 ASN   B H    1 
ATOM   5459 H HA   . ASN   B 1 101 ? 42.184 -32.954 12.047  1.00 34.18 ?  101 ASN   B HA   1 
ATOM   5460 H HB2  . ASN   B 1 101 ? 43.971 -31.409 10.519  1.00 33.91 ?  101 ASN   B HB2  1 
ATOM   5461 H HB3  . ASN   B 1 101 ? 44.498 -32.380 11.661  1.00 33.91 ?  101 ASN   B HB3  1 
ATOM   5462 H HD21 . ASN   B 1 101 ? 44.539 -33.863 8.355   1.00 33.54 ?  101 ASN   B HD21 1 
ATOM   5463 H HD22 . ASN   B 1 101 ? 44.961 -32.511 8.814   1.00 33.54 ?  101 ASN   B HD22 1 
ATOM   5464 N N    . LYS   B 1 102 ? 42.177 -29.992 13.032  1.00 33.02 ?  102 LYS   B N    1 
ATOM   5465 C CA   . LYS   B 1 102 ? 42.147 -29.155 14.224  1.00 35.92 ?  102 LYS   B CA   1 
ATOM   5466 C C    . LYS   B 1 102 ? 40.766 -29.110 14.864  1.00 35.47 ?  102 LYS   B C    1 
ATOM   5467 O O    . LYS   B 1 102 ? 40.542 -28.308 15.776  1.00 36.02 ?  102 LYS   B O    1 
ATOM   5468 C CB   . LYS   B 1 102 ? 42.576 -27.727 13.886  1.00 39.26 ?  102 LYS   B CB   1 
ATOM   5469 C CG   . LYS   B 1 102 ? 44.020 -27.559 13.455  1.00 42.58 ?  102 LYS   B CG   1 
ATOM   5470 C CD   . LYS   B 1 102 ? 44.232 -26.142 12.945  1.00 45.21 ?  102 LYS   B CD   1 
ATOM   5471 C CE   . LYS   B 1 102 ? 45.697 -25.802 12.757  1.00 47.23 ?  102 LYS   B CE   1 
ATOM   5472 N NZ   . LYS   B 1 102 ? 45.856 -24.394 12.289  1.00 48.42 ?  102 LYS   B NZ   1 
ATOM   5473 H H    . LYS   B 1 102 ? 41.851 -29.602 12.339  1.00 39.65 ?  102 LYS   B H    1 
ATOM   5474 H HA   . LYS   B 1 102 ? 42.774 -29.508 14.875  1.00 43.14 ?  102 LYS   B HA   1 
ATOM   5475 H HB2  . LYS   B 1 102 ? 42.018 -27.401 13.164  1.00 47.14 ?  102 LYS   B HB2  1 
ATOM   5476 H HB3  . LYS   B 1 102 ? 42.444 -27.172 14.672  1.00 47.14 ?  102 LYS   B HB3  1 
ATOM   5477 H HG2  . LYS   B 1 102 ? 44.608 -27.707 14.213  1.00 51.12 ?  102 LYS   B HG2  1 
ATOM   5478 H HG3  . LYS   B 1 102 ? 44.222 -28.181 12.738  1.00 51.12 ?  102 LYS   B HG3  1 
ATOM   5479 H HD2  . LYS   B 1 102 ? 43.788 -26.045 12.088  1.00 54.28 ?  102 LYS   B HD2  1 
ATOM   5480 H HD3  . LYS   B 1 102 ? 43.857 -25.516 13.585  1.00 54.28 ?  102 LYS   B HD3  1 
ATOM   5481 H HE2  . LYS   B 1 102 ? 46.162 -25.898 13.603  1.00 56.70 ?  102 LYS   B HE2  1 
ATOM   5482 H HE3  . LYS   B 1 102 ? 46.082 -26.392 12.090  1.00 56.70 ?  102 LYS   B HE3  1 
ATOM   5483 H HZ1  . LYS   B 1 102 ? 46.718 -24.204 12.182  1.00 58.14 ?  102 LYS   B HZ1  1 
ATOM   5484 H HZ2  . LYS   B 1 102 ? 45.436 -24.283 11.512  1.00 58.14 ?  102 LYS   B HZ2  1 
ATOM   5485 H HZ3  . LYS   B 1 102 ? 45.508 -23.834 12.887  1.00 58.14 ?  102 LYS   B HZ3  1 
ATOM   5486 N N    . GLY   B 1 103 ? 39.829 -29.929 14.393  1.00 34.38 ?  103 GLY   B N    1 
ATOM   5487 C CA   . GLY   B 1 103 ? 38.498 -29.966 14.963  1.00 33.66 ?  103 GLY   B CA   1 
ATOM   5488 C C    . GLY   B 1 103 ? 37.564 -28.874 14.497  1.00 32.54 ?  103 GLY   B C    1 
ATOM   5489 O O    . GLY   B 1 103 ? 36.485 -28.718 15.080  1.00 32.97 ?  103 GLY   B O    1 
ATOM   5490 H H    . GLY   B 1 103 ? 39.944 -30.473 13.739  1.00 41.29 ?  103 GLY   B H    1 
ATOM   5491 H HA2  . GLY   B 1 103 ? 38.088 -30.817 14.747  1.00 40.42 ?  103 GLY   B HA2  1 
ATOM   5492 H HA3  . GLY   B 1 103 ? 38.568 -29.904 15.929  1.00 40.42 ?  103 GLY   B HA3  1 
ATOM   5493 N N    . GLU   B 1 104 ? 37.932 -28.117 13.467  1.00 30.59 ?  104 GLU   B N    1 
ATOM   5494 C CA   . GLU   B 1 104 ? 37.084 -27.034 12.996  1.00 28.68 ?  104 GLU   B CA   1 
ATOM   5495 C C    . GLU   B 1 104 ? 35.899 -27.582 12.200  1.00 28.88 ?  104 GLU   B C    1 
ATOM   5496 O O    . GLU   B 1 104 ? 35.949 -28.677 11.632  1.00 29.16 ?  104 GLU   B O    1 
ATOM   5497 C CB   . GLU   B 1 104 ? 37.908 -26.028 12.191  1.00 27.17 ?  104 GLU   B CB   1 
ATOM   5498 C CG   . GLU   B 1 104 ? 39.011 -25.396 13.038  1.00 25.88 ?  104 GLU   B CG   1 
ATOM   5499 C CD   . GLU   B 1 104 ? 39.960 -24.507 12.261  1.00 24.73 ?  104 GLU   B CD   1 
ATOM   5500 O OE1  . GLU   B 1 104 ? 39.961 -24.539 11.013  1.00 23.31 ?  104 GLU   B OE1  1 
ATOM   5501 O OE2  . GLU   B 1 104 ? 40.721 -23.771 12.923  1.00 25.16 -1 104 GLU   B OE2  1 
ATOM   5502 H H    . GLU   B 1 104 ? 38.672 -28.204 13.033  1.00 36.74 ?  104 GLU   B H    1 
ATOM   5503 H HA   . GLU   B 1 104 ? 36.730 -26.564 13.766  1.00 34.45 ?  104 GLU   B HA   1 
ATOM   5504 H HB2  . GLU   B 1 104 ? 38.325 -26.478 11.441  1.00 32.64 ?  104 GLU   B HB2  1 
ATOM   5505 H HB3  . GLU   B 1 104 ? 37.328 -25.316 11.876  1.00 32.64 ?  104 GLU   B HB3  1 
ATOM   5506 H HG2  . GLU   B 1 104 ? 38.606 -24.856 13.736  1.00 31.08 ?  104 GLU   B HG2  1 
ATOM   5507 H HG3  . GLU   B 1 104 ? 39.545 -26.100 13.442  1.00 31.08 ?  104 GLU   B HG3  1 
ATOM   5508 N N    A ASP   B 1 105 ? 34.826 -26.794 12.171  0.60 29.13 ?  105 ASP   B N    1 
ATOM   5509 N N    B ASP   B 1 105 ? 34.820 -26.803 12.166  0.40 28.96 ?  105 ASP   B N    1 
ATOM   5510 C CA   A ASP   B 1 105 ? 33.546 -27.241 11.633  0.60 29.53 ?  105 ASP   B CA   1 
ATOM   5511 C CA   B ASP   B 1 105 ? 33.553 -27.275 11.619  0.40 29.00 ?  105 ASP   B CA   1 
ATOM   5512 C C    A ASP   B 1 105 ? 33.601 -27.287 10.110  0.60 27.40 ?  105 ASP   B C    1 
ATOM   5513 C C    B ASP   B 1 105 ? 33.617 -27.306 10.096  0.40 27.78 ?  105 ASP   B C    1 
ATOM   5514 O O    A ASP   B 1 105 ? 33.764 -26.254 9.453   0.60 26.59 ?  105 ASP   B O    1 
ATOM   5515 O O    B ASP   B 1 105 ? 33.822 -26.270 9.453   0.40 27.36 ?  105 ASP   B O    1 
ATOM   5516 C CB   A ASP   B 1 105 ? 32.444 -26.288 12.095  0.60 32.17 ?  105 ASP   B CB   1 
ATOM   5517 C CB   B ASP   B 1 105 ? 32.410 -26.377 12.091  0.40 30.22 ?  105 ASP   B CB   1 
ATOM   5518 C CG   A ASP   B 1 105 ? 31.062 -26.737 11.662  0.60 34.40 ?  105 ASP   B CG   1 
ATOM   5519 C CG   B ASP   B 1 105 ? 31.044 -26.968 11.792  0.40 31.09 ?  105 ASP   B CG   1 
ATOM   5520 O OD1  A ASP   B 1 105 ? 30.937 -27.850 11.107  0.60 34.82 ?  105 ASP   B OD1  1 
ATOM   5521 O OD1  B ASP   B 1 105 ? 30.971 -27.950 11.023  0.40 31.40 ?  105 ASP   B OD1  1 
ATOM   5522 O OD2  A ASP   B 1 105 ? 30.096 -25.972 11.873  0.60 35.67 -1 105 ASP   B OD2  1 
ATOM   5523 O OD2  B ASP   B 1 105 ? 30.041 -26.461 12.338  0.40 31.16 -1 105 ASP   B OD2  1 
ATOM   5524 H H    A ASP   B 1 105 ? 34.816 -25.987 12.458  0.60 34.98 ?  105 ASP   B H    1 
ATOM   5525 H H    B ASP   B 1 105 ? 34.800 -25.993 12.450  0.40 34.78 ?  105 ASP   B H    1 
ATOM   5526 H HA   A ASP   B 1 105 ? 33.341 -28.130 11.965  0.60 35.47 ?  105 ASP   B HA   1 
ATOM   5527 H HA   B ASP   B 1 105 ? 33.379 -28.175 11.934  0.40 34.83 ?  105 ASP   B HA   1 
ATOM   5528 H HB2  A ASP   B 1 105 ? 32.464 -26.224 13.066  0.60 38.63 ?  105 ASP   B HB2  1 
ATOM   5529 H HB2  B ASP   B 1 105 ? 32.476 -26.258 13.052  0.40 36.30 ?  105 ASP   B HB2  1 
ATOM   5530 H HB3  A ASP   B 1 105 ? 32.595 -25.413 11.705  0.60 38.63 ?  105 ASP   B HB3  1 
ATOM   5531 H HB3  B ASP   B 1 105 ? 32.479 -25.516 11.646  0.40 36.30 ?  105 ASP   B HB3  1 
ATOM   5532 N N    A ILE   B 1 106 ? 33.444 -28.490 9.550   0.60 26.77 ?  106 ILE   B N    1 
ATOM   5533 N N    B ILE   B 1 106 ? 33.430 -28.498 9.522   0.40 27.29 ?  106 ILE   B N    1 
ATOM   5534 C CA   A ILE   B 1 106 ? 33.436 -28.670 8.103   0.60 25.67 ?  106 ILE   B CA   1 
ATOM   5535 C CA   B ILE   B 1 106 ? 33.429 -28.661 8.072   0.40 26.65 ?  106 ILE   B CA   1 
ATOM   5536 C C    A ILE   B 1 106 ? 32.339 -27.849 7.435   0.60 24.35 ?  106 ILE   B C    1 
ATOM   5537 C C    B ILE   B 1 106 ? 32.331 -27.839 7.409   0.40 25.73 ?  106 ILE   B C    1 
ATOM   5538 O O    A ILE   B 1 106 ? 32.433 -27.546 6.241   0.60 23.11 ?  106 ILE   B O    1 
ATOM   5539 O O    B ILE   B 1 106 ? 32.417 -27.544 6.212   0.40 25.08 ?  106 ILE   B O    1 
ATOM   5540 C CB   A ILE   B 1 106 ? 33.319 -30.175 7.772   0.60 26.45 ?  106 ILE   B CB   1 
ATOM   5541 C CB   B ILE   B 1 106 ? 33.319 -30.162 7.717   0.40 27.13 ?  106 ILE   B CB   1 
ATOM   5542 C CG1  A ILE   B 1 106 ? 33.561 -30.432 6.285   0.60 27.01 ?  106 ILE   B CG1  1 
ATOM   5543 C CG1  B ILE   B 1 106 ? 33.618 -30.399 6.236   0.40 27.45 ?  106 ILE   B CG1  1 
ATOM   5544 C CG2  A ILE   B 1 106 ? 31.953 -30.709 8.184   0.60 27.04 ?  106 ILE   B CG2  1 
ATOM   5545 C CG2  B ILE   B 1 106 ? 31.935 -30.694 8.064   0.40 27.51 ?  106 ILE   B CG2  1 
ATOM   5546 C CD1  A ILE   B 1 106 ? 34.926 -29.995 5.811   0.60 27.23 ?  106 ILE   B CD1  1 
ATOM   5547 C CD1  B ILE   B 1 106 ? 34.995 -29.944 5.813   0.40 27.58 ?  106 ILE   B CD1  1 
ATOM   5548 H H    A ILE   B 1 106 ? 33.346 -29.217 9.994   0.60 32.15 ?  106 ILE   B H    1 
ATOM   5549 H H    B ILE   B 1 106 ? 33.309 -29.228 9.955   0.40 32.77 ?  106 ILE   B H    1 
ATOM   5550 H HA   A ILE   B 1 106 ? 34.283 -28.355 7.758   0.60 30.84 ?  106 ILE   B HA   1 
ATOM   5551 H HA   B ILE   B 1 106 ? 34.275 -28.337 7.735   0.40 32.01 ?  106 ILE   B HA   1 
ATOM   5552 H HB   A ILE   B 1 106 ? 33.994 -30.652 8.278   0.60 31.77 ?  106 ILE   B HB   1 
ATOM   5553 H HB   B ILE   B 1 106 ? 33.971 -30.649 8.242   0.40 32.58 ?  106 ILE   B HB   1 
ATOM   5554 H HG12 A ILE   B 1 106 ? 33.484 -31.385 6.116   0.60 32.44 ?  106 ILE   B HG12 1 
ATOM   5555 H HG12 B ILE   B 1 106 ? 33.555 -31.352 6.054   0.40 32.97 ?  106 ILE   B HG12 1 
ATOM   5556 H HG13 A ILE   B 1 106 ? 32.899 -29.952 5.767   0.60 32.44 ?  106 ILE   B HG13 1 
ATOM   5557 H HG13 B ILE   B 1 106 ? 32.968 -29.920 5.701   0.40 32.97 ?  106 ILE   B HG13 1 
ATOM   5558 H HG21 A ILE   B 1 106 ? 31.958 -31.677 8.110   0.60 32.47 ?  106 ILE   B HG21 1 
ATOM   5559 H HG21 B ILE   B 1 106 ? 31.948 -31.663 8.011   0.40 33.04 ?  106 ILE   B HG21 1 
ATOM   5560 H HG22 A ILE   B 1 106 ? 31.777 -30.450 9.103   0.60 32.47 ?  106 ILE   B HG22 1 
ATOM   5561 H HG22 B ILE   B 1 106 ? 31.707 -30.416 8.965   0.40 33.04 ?  106 ILE   B HG22 1 
ATOM   5562 H HG23 A ILE   B 1 106 ? 31.275 -30.337 7.600   0.60 32.47 ?  106 ILE   B HG23 1 
ATOM   5563 H HG23 B ILE   B 1 106 ? 31.289 -30.339 7.434   0.40 33.04 ?  106 ILE   B HG23 1 
ATOM   5564 H HD11 A ILE   B 1 106 ? 35.107 -30.402 4.951   0.60 32.70 ?  106 ILE   B HD11 1 
ATOM   5565 H HD11 B ILE   B 1 106 ? 35.216 -30.357 4.965   0.40 33.13 ?  106 ILE   B HD11 1 
ATOM   5566 H HD12 A ILE   B 1 106 ? 34.939 -29.028 5.727   0.60 32.70 ?  106 ILE   B HD12 1 
ATOM   5567 H HD12 B ILE   B 1 106 ? 34.993 -28.978 5.719   0.40 33.13 ?  106 ILE   B HD12 1 
ATOM   5568 H HD13 A ILE   B 1 106 ? 35.592 -30.280 6.458   0.60 32.70 ?  106 ILE   B HD13 1 
ATOM   5569 H HD13 B ILE   B 1 106 ? 35.637 -30.211 6.489   0.40 33.13 ?  106 ILE   B HD13 1 
ATOM   5570 N N    A GLN   B 1 107 ? 31.300 -27.467 8.179   0.60 24.99 ?  107 GLN   B N    1 
ATOM   5571 N N    B GLN   B 1 107 ? 31.294 -27.459 8.158   0.40 25.92 ?  107 GLN   B N    1 
ATOM   5572 C CA   A GLN   B 1 107 ? 30.218 -26.679 7.598   0.60 25.78 ?  107 GLN   B CA   1 
ATOM   5573 C CA   B GLN   B 1 107 ? 30.208 -26.669 7.589   0.40 26.23 ?  107 GLN   B CA   1 
ATOM   5574 C C    A GLN   B 1 107 ? 30.703 -25.336 7.067   0.60 23.87 ?  107 GLN   B C    1 
ATOM   5575 C C    B GLN   B 1 107 ? 30.678 -25.306 7.098   0.40 24.09 ?  107 GLN   B C    1 
ATOM   5576 O O    A GLN   B 1 107 ? 30.073 -24.778 6.164   0.60 24.06 ?  107 GLN   B O    1 
ATOM   5577 O O    B GLN   B 1 107 ? 30.008 -24.699 6.257   0.40 24.18 ?  107 GLN   B O    1 
ATOM   5578 C CB   A GLN   B 1 107 ? 29.111 -26.471 8.637   0.60 29.26 ?  107 GLN   B CB   1 
ATOM   5579 C CB   B GLN   B 1 107 ? 29.091 -26.507 8.626   0.40 29.07 ?  107 GLN   B CB   1 
ATOM   5580 C CG   A GLN   B 1 107 ? 27.785 -25.970 8.070   0.60 32.76 ?  107 GLN   B CG   1 
ATOM   5581 C CG   B GLN   B 1 107 ? 27.762 -26.014 8.064   0.40 31.88 ?  107 GLN   B CG   1 
ATOM   5582 C CD   A GLN   B 1 107 ? 27.724 -24.458 7.946   0.60 35.47 ?  107 GLN   B CD   1 
ATOM   5583 C CD   B GLN   B 1 107 ? 27.650 -24.500 8.048   0.40 34.06 ?  107 GLN   B CD   1 
ATOM   5584 O OE1  A GLN   B 1 107 ? 28.565 -23.742 8.493   0.60 36.53 ?  107 GLN   B OE1  1 
ATOM   5585 O OE1  B GLN   B 1 107 ? 28.470 -23.798 8.641   0.40 34.84 ?  107 GLN   B OE1  1 
ATOM   5586 N NE2  A GLN   B 1 107 ? 26.720 -23.964 7.226   0.60 36.47 ?  107 GLN   B NE2  1 
ATOM   5587 N NE2  B GLN   B 1 107 ? 26.628 -23.990 7.369   0.40 34.89 ?  107 GLN   B NE2  1 
ATOM   5588 H H    A GLN   B 1 107 ? 31.204 -27.637 9.014   0.60 30.01 ?  107 GLN   B H    1 
ATOM   5589 H H    B GLN   B 1 107 ? 31.197 -27.645 8.990   0.40 31.13 ?  107 GLN   B H    1 
ATOM   5590 H HA   A GLN   B 1 107 ? 29.836 -27.173 6.855   0.60 30.97 ?  107 GLN   B HA   1 
ATOM   5591 H HA   B GLN   B 1 107 ? 29.837 -27.148 6.832   0.40 31.51 ?  107 GLN   B HA   1 
ATOM   5592 H HB2  A GLN   B 1 107 ? 28.937 -27.316 9.075   0.60 35.14 ?  107 GLN   B HB2  1 
ATOM   5593 H HB2  B GLN   B 1 107 ? 28.929 -27.366 9.039   0.40 34.91 ?  107 GLN   B HB2  1 
ATOM   5594 H HB3  A GLN   B 1 107 ? 29.416 -25.822 9.291   0.60 35.14 ?  107 GLN   B HB3  1 
ATOM   5595 H HB3  B GLN   B 1 107 ? 29.381 -25.872 9.300   0.40 34.91 ?  107 GLN   B HB3  1 
ATOM   5596 H HG2  A GLN   B 1 107 ? 27.655 -26.344 7.186   0.60 39.34 ?  107 GLN   B HG2  1 
ATOM   5597 H HG2  B GLN   B 1 107 ? 27.665 -26.329 7.152   0.40 38.28 ?  107 GLN   B HG2  1 
ATOM   5598 H HG3  A GLN   B 1 107 ? 27.063 -26.253 8.657   0.60 39.34 ?  107 GLN   B HG3  1 
ATOM   5599 H HG3  B GLN   B 1 107 ? 27.038 -26.364 8.612   0.40 38.28 ?  107 GLN   B HG3  1 
ATOM   5600 H HE21 A GLN   B 1 107 ? 26.151 -24.495 6.858   0.60 43.79 ?  107 GLN   B HE21 1 
ATOM   5601 H HE21 B GLN   B 1 107 ? 26.074 -24.512 6.966   0.40 41.90 ?  107 GLN   B HE21 1 
ATOM   5602 H HE22 A GLN   B 1 107 ? 26.636 -23.113 7.128   0.60 43.79 ?  107 GLN   B HE22 1 
ATOM   5603 H HE22 B GLN   B 1 107 ? 26.518 -23.138 7.332   0.40 41.90 ?  107 GLN   B HE22 1 
ATOM   5604 N N    . LEU   B 1 108 ? 31.815 -24.814 7.592   1.00 22.04 ?  108 LEU   B N    1 
ATOM   5605 C CA   . LEU   B 1 108 ? 32.353 -23.521 7.173   1.00 19.58 ?  108 LEU   B CA   1 
ATOM   5606 C C    . LEU   B 1 108 ? 33.003 -23.554 5.797   1.00 17.54 ?  108 LEU   B C    1 
ATOM   5607 O O    . LEU   B 1 108 ? 33.437 -22.501 5.306   1.00 16.90 ?  108 LEU   B O    1 
ATOM   5608 C CB   . LEU   B 1 108 ? 33.358 -23.023 8.211   1.00 20.23 ?  108 LEU   B CB   1 
ATOM   5609 C CG   . LEU   B 1 108 ? 32.746 -22.534 9.523   1.00 21.99 ?  108 LEU   B CG   1 
ATOM   5610 C CD1  . LEU   B 1 108 ? 33.789 -22.473 10.623  1.00 22.52 ?  108 LEU   B CD1  1 
ATOM   5611 C CD2  . LEU   B 1 108 ? 32.106 -21.165 9.328   1.00 23.13 ?  108 LEU   B CD2  1 
ATOM   5612 H H    A LEU   B 1 108 ? 32.270 -25.196 8.209   0.60 26.48 ?  108 LEU   B H    1 
ATOM   5613 H H    B LEU   B 1 108 ? 32.287 -25.213 8.185   0.40 26.48 ?  108 LEU   B H    1 
ATOM   5614 H HA   . LEU   B 1 108 ? 31.625 -22.884 7.135   1.00 23.53 ?  108 LEU   B HA   1 
ATOM   5615 H HB2  . LEU   B 1 108 ? 33.963 -23.746 8.428   1.00 24.30 ?  108 LEU   B HB2  1 
ATOM   5616 H HB3  . LEU   B 1 108 ? 33.852 -22.283 7.829   1.00 24.30 ?  108 LEU   B HB3  1 
ATOM   5617 H HG   . LEU   B 1 108 ? 32.048 -23.150 9.803   1.00 26.41 ?  108 LEU   B HG   1 
ATOM   5618 H HD11 . LEU   B 1 108 ? 33.365 -22.187 11.448  1.00 27.05 ?  108 LEU   B HD11 1 
ATOM   5619 H HD12 . LEU   B 1 108 ? 34.176 -23.354 10.738  1.00 27.05 ?  108 LEU   B HD12 1 
ATOM   5620 H HD13 . LEU   B 1 108 ? 34.478 -21.838 10.370  1.00 27.05 ?  108 LEU   B HD13 1 
ATOM   5621 H HD21 . LEU   B 1 108 ? 31.767 -20.849 10.181  1.00 27.79 ?  108 LEU   B HD21 1 
ATOM   5622 H HD22 . LEU   B 1 108 ? 32.775 -20.550 8.990   1.00 27.79 ?  108 LEU   B HD22 1 
ATOM   5623 H HD23 . LEU   B 1 108 ? 31.377 -21.244 8.692   1.00 27.79 ?  108 LEU   B HD23 1 
ATOM   5624 N N    . LEU   B 1 109 ? 33.076 -24.727 5.169   1.00 16.51 ?  109 LEU   B N    1 
ATOM   5625 C CA   . LEU   B 1 109 ? 33.709 -24.837 3.862   1.00 15.49 ?  109 LEU   B CA   1 
ATOM   5626 C C    . LEU   B 1 109 ? 32.946 -24.050 2.801   1.00 14.80 ?  109 LEU   B C    1 
ATOM   5627 O O    . LEU   B 1 109 ? 33.561 -23.458 1.906   1.00 14.43 ?  109 LEU   B O    1 
ATOM   5628 C CB   . LEU   B 1 109 ? 33.830 -26.312 3.482   1.00 15.92 ?  109 LEU   B CB   1 
ATOM   5629 C CG   . LEU   B 1 109 ? 34.617 -26.654 2.220   1.00 15.73 ?  109 LEU   B CG   1 
ATOM   5630 C CD1  . LEU   B 1 109 ? 35.990 -26.001 2.226   1.00 15.60 ?  109 LEU   B CD1  1 
ATOM   5631 C CD2  . LEU   B 1 109 ? 34.760 -28.168 2.102   1.00 16.73 ?  109 LEU   B CD2  1 
ATOM   5632 H H    . LEU   B 1 109 ? 32.774 -25.468 5.476   1.00 19.84 ?  109 LEU   B H    1 
ATOM   5633 H HA   . LEU   B 1 109 ? 34.604 -24.468 3.915   1.00 18.62 ?  109 LEU   B HA   1 
ATOM   5634 H HB2  . LEU   B 1 109 ? 34.263 -26.778 4.213   1.00 19.13 ?  109 LEU   B HB2  1 
ATOM   5635 H HB3  . LEU   B 1 109 ? 32.937 -26.669 3.360   1.00 19.13 ?  109 LEU   B HB3  1 
ATOM   5636 H HG   . LEU   B 1 109 ? 34.132 -26.345 1.436   1.00 18.91 ?  109 LEU   B HG   1 
ATOM   5637 H HD11 . LEU   B 1 109 ? 36.517 -26.361 1.495   1.00 18.74 ?  109 LEU   B HD11 1 
ATOM   5638 H HD12 . LEU   B 1 109 ? 35.879 -25.045 2.112   1.00 18.74 ?  109 LEU   B HD12 1 
ATOM   5639 H HD13 . LEU   B 1 109 ? 36.423 -26.190 3.071   1.00 18.74 ?  109 LEU   B HD13 1 
ATOM   5640 H HD21 . LEU   B 1 109 ? 35.335 -28.377 1.346   1.00 20.11 ?  109 LEU   B HD21 1 
ATOM   5641 H HD22 . LEU   B 1 109 ? 35.155 -28.513 2.918   1.00 20.11 ?  109 LEU   B HD22 1 
ATOM   5642 H HD23 . LEU   B 1 109 ? 33.884 -28.562 1.966   1.00 20.11 ?  109 LEU   B HD23 1 
ATOM   5643 N N    . LYS   B 1 110 ? 31.613 -24.013 2.881   1.00 14.74 ?  110 LYS   B N    1 
ATOM   5644 C CA   . LYS   B 1 110 ? 30.860 -23.250 1.888   1.00 14.85 ?  110 LYS   B CA   1 
ATOM   5645 C C    . LYS   B 1 110 ? 31.197 -21.762 1.973   1.00 14.50 ?  110 LYS   B C    1 
ATOM   5646 O O    . LYS   B 1 110 ? 31.452 -21.115 0.951   1.00 14.28 ?  110 LYS   B O    1 
ATOM   5647 C CB   . LYS   B 1 110 ? 29.355 -23.495 2.041   1.00 15.54 ?  110 LYS   B CB   1 
ATOM   5648 C CG   . LYS   B 1 110 ? 28.543 -22.872 0.915   1.00 15.51 ?  110 LYS   B CG   1 
ATOM   5649 C CD   . LYS   B 1 110 ? 27.080 -23.306 0.940   1.00 15.90 ?  110 LYS   B CD   1 
ATOM   5650 C CE   . LYS   B 1 110 ? 26.324 -22.770 -0.275  1.00 16.70 ?  110 LYS   B CE   1 
ATOM   5651 N NZ   . LYS   B 1 110 ? 26.649 -23.496 -1.532  1.00 16.89 ?  110 LYS   B NZ   1 
ATOM   5652 H H    . LYS   B 1 110 ? 31.139 -24.413 3.472   1.00 17.72 ?  110 LYS   B H    1 
ATOM   5653 H HA   . LYS   B 1 110 ? 31.114 -23.556 1.002   1.00 17.85 ?  110 LYS   B HA   1 
ATOM   5654 H HB2  . LYS   B 1 110 ? 29.189 -24.455 2.033   1.00 18.68 ?  110 LYS   B HB2  1 
ATOM   5655 H HB3  . LYS   B 1 110 ? 29.054 -23.116 2.879   1.00 18.68 ?  110 LYS   B HB3  1 
ATOM   5656 H HG2  . LYS   B 1 110 ? 28.566 -21.905 1.005   1.00 18.64 ?  110 LYS   B HG2  1 
ATOM   5657 H HG3  . LYS   B 1 110 ? 28.919 -23.135 0.063   1.00 18.64 ?  110 LYS   B HG3  1 
ATOM   5658 H HD2  . LYS   B 1 110 ? 27.035 -24.278 0.924   1.00 19.11 ?  110 LYS   B HD2  1 
ATOM   5659 H HD3  . LYS   B 1 110 ? 26.655 -22.966 1.744   1.00 19.11 ?  110 LYS   B HD3  1 
ATOM   5660 H HE2  . LYS   B 1 110 ? 25.373 -22.854 -0.116  1.00 20.07 ?  110 LYS   B HE2  1 
ATOM   5661 H HE3  . LYS   B 1 110 ? 26.559 -21.835 -0.399  1.00 20.07 ?  110 LYS   B HE3  1 
ATOM   5662 H HZ1  . LYS   B 1 110 ? 26.194 -23.151 -2.211  1.00 20.30 ?  110 LYS   B HZ1  1 
ATOM   5663 H HZ2  . LYS   B 1 110 ? 27.523 -23.428 -1.705  1.00 20.30 ?  110 LYS   B HZ2  1 
ATOM   5664 H HZ3  . LYS   B 1 110 ? 26.442 -24.358 -1.447  1.00 20.30 ?  110 LYS   B HZ3  1 
ATOM   5665 N N    . SER   B 1 111 ? 31.222 -21.212 3.192   1.00 14.87 ?  111 SER   B N    1 
ATOM   5666 C CA   . SER   B 1 111 ? 31.610 -19.814 3.371   1.00 14.58 ?  111 SER   B CA   1 
ATOM   5667 C C    . SER   B 1 111 ? 32.991 -19.553 2.784   1.00 14.07 ?  111 SER   B C    1 
ATOM   5668 O O    . SER   B 1 111 ? 33.209 -18.526 2.122   1.00 14.39 ?  111 SER   B O    1 
ATOM   5669 C CB   . SER   B 1 111 ? 31.598 -19.451 4.855   1.00 15.76 ?  111 SER   B CB   1 
ATOM   5670 O OG   . SER   B 1 111 ? 30.287 -19.448 5.384   1.00 17.52 ?  111 SER   B OG   1 
ATOM   5671 H H    . SER   B 1 111 ? 31.027 -21.630 3.918   1.00 17.87 ?  111 SER   B H    1 
ATOM   5672 H HA   . SER   B 1 111 ? 30.976 -19.249 2.912   1.00 17.52 ?  111 SER   B HA   1 
ATOM   5673 H HB2  . SER   B 1 111 ? 32.122 -20.108 5.343   1.00 18.94 ?  111 SER   B HB2  1 
ATOM   5674 H HB3  . SER   B 1 111 ? 31.981 -18.573 4.967   1.00 18.94 ?  111 SER   B HB3  1 
ATOM   5675 H HG   . SER   B 1 111 ? 30.303 -19.244 6.204   1.00 21.05 ?  111 SER   B HG   1 
ATOM   5676 N N    . ALA   B 1 112 ? 33.931 -20.473 3.009   1.00 14.05 ?  112 ALA   B N    1 
ATOM   5677 C CA   . ALA   B 1 112 ? 35.276 -20.305 2.471   1.00 13.62 ?  112 ALA   B CA   1 
ATOM   5678 C C    . ALA   B 1 112 ? 35.248 -20.220 0.948   1.00 13.12 ?  112 ALA   B C    1 
ATOM   5679 O O    . ALA   B 1 112 ? 35.874 -19.335 0.350   1.00 13.17 ?  112 ALA   B O    1 
ATOM   5680 C CB   . ALA   B 1 112 ? 36.173 -21.451 2.951   1.00 14.45 ?  112 ALA   B CB   1 
ATOM   5681 H H    . ALA   B 1 112 ? 33.817 -21.195 3.470   1.00 16.89 ?  112 ALA   B H    1 
ATOM   5682 H HA   . ALA   B 1 112 ? 35.648 -19.477 2.811   1.00 16.37 ?  112 ALA   B HA   1 
ATOM   5683 H HB1  . ALA   B 1 112 ? 37.068 -21.322 2.590   1.00 17.37 ?  112 ALA   B HB1  1 
ATOM   5684 H HB2  . ALA   B 1 112 ? 36.209 -21.442 3.921   1.00 17.37 ?  112 ALA   B HB2  1 
ATOM   5685 H HB3  . ALA   B 1 112 ? 35.810 -22.292 2.640   1.00 17.37 ?  112 ALA   B HB3  1 
ATOM   5686 N N    . TYR   B 1 113 ? 34.520 -21.130 0.297   1.00 13.16 ?  113 TYR   B N    1 
ATOM   5687 C CA   . TYR   B 1 113 ? 34.444 -21.081 -1.158  1.00 12.87 ?  113 TYR   B CA   1 
ATOM   5688 C C    . TYR   B 1 113 ? 33.736 -19.829 -1.674  1.00 13.05 ?  113 TYR   B C    1 
ATOM   5689 O O    . TYR   B 1 113 ? 33.998 -19.403 -2.802  1.00 12.78 ?  113 TYR   B O    1 
ATOM   5690 C CB   . TYR   B 1 113 ? 33.769 -22.342 -1.699  1.00 12.92 ?  113 TYR   B CB   1 
ATOM   5691 C CG   . TYR   B 1 113 ? 34.729 -23.493 -1.951  1.00 13.42 ?  113 TYR   B CG   1 
ATOM   5692 C CD1  . TYR   B 1 113 ? 35.733 -23.389 -2.906  1.00 13.85 ?  113 TYR   B CD1  1 
ATOM   5693 C CD2  . TYR   B 1 113 ? 34.618 -24.684 -1.249  1.00 13.70 ?  113 TYR   B CD2  1 
ATOM   5694 C CE1  . TYR   B 1 113 ? 36.610 -24.423 -3.148  1.00 14.15 ?  113 TYR   B CE1  1 
ATOM   5695 C CE2  . TYR   B 1 113 ? 35.490 -25.737 -1.485  1.00 14.05 ?  113 TYR   B CE2  1 
ATOM   5696 C CZ   . TYR   B 1 113 ? 36.483 -25.606 -2.439  1.00 14.38 ?  113 TYR   B CZ   1 
ATOM   5697 O OH   . TYR   B 1 113 ? 37.366 -26.625 -2.708  1.00 15.12 ?  113 TYR   B OH   1 
ATOM   5698 H H    . TYR   B 1 113 ? 34.066 -21.765 0.671   1.00 15.82 ?  113 TYR   B H    1 
ATOM   5699 H HA   . TYR   B 1 113 ? 35.345 -21.067 -1.497  1.00 15.48 ?  113 TYR   B HA   1 
ATOM   5700 H HB2  . TYR   B 1 113 ? 33.104 -22.649 -1.056  1.00 15.53 ?  113 TYR   B HB2  1 
ATOM   5701 H HB3  . TYR   B 1 113 ? 33.334 -22.129 -2.538  1.00 15.53 ?  113 TYR   B HB3  1 
ATOM   5702 H HD1  . TYR   B 1 113 ? 35.820 -22.593 -3.384  1.00 16.64 ?  113 TYR   B HD1  1 
ATOM   5703 H HD2  . TYR   B 1 113 ? 33.947 -24.776 -0.611  1.00 16.47 ?  113 TYR   B HD2  1 
ATOM   5704 H HE1  . TYR   B 1 113 ? 37.273 -24.327 -3.792  1.00 17.01 ?  113 TYR   B HE1  1 
ATOM   5705 H HE2  . TYR   B 1 113 ? 35.400 -26.531 -1.010  1.00 16.89 ?  113 TYR   B HE2  1 
ATOM   5706 H HH   . TYR   B 1 113 ? 37.185 -27.293 -2.228  1.00 18.18 ?  113 TYR   B HH   1 
ATOM   5707 N N    . GLU   B 1 114 ? 32.814 -19.255 -0.896  1.00 13.01 ?  114 GLU   B N    1 
ATOM   5708 C CA   . GLU   B 1 114 ? 32.132 -18.048 -1.357  1.00 12.93 ?  114 GLU   B CA   1 
ATOM   5709 C C    . GLU   B 1 114 ? 33.116 -16.927 -1.667  1.00 12.85 ?  114 GLU   B C    1 
ATOM   5710 O O    . GLU   B 1 114 ? 32.832 -16.065 -2.507  1.00 13.17 ?  114 GLU   B O    1 
ATOM   5711 C CB   . GLU   B 1 114 ? 31.072 -17.607 -0.343  1.00 13.75 ?  114 GLU   B CB   1 
ATOM   5712 C CG   . GLU   B 1 114 ? 29.847 -18.522 -0.419  1.00 13.78 ?  114 GLU   B CG   1 
ATOM   5713 C CD   . GLU   B 1 114 ? 28.825 -18.334 0.683   1.00 13.55 ?  114 GLU   B CD   1 
ATOM   5714 O OE1  . GLU   B 1 114 ? 29.115 -17.712 1.723   1.00 14.15 ?  114 GLU   B OE1  1 
ATOM   5715 O OE2  . GLU   B 1 114 ? 27.699 -18.866 0.516   1.00 14.50 -1 114 GLU   B OE2  1 
ATOM   5716 H H    . GLU   B 1 114 ? 32.568 -19.538 -0.118  1.00 15.64 ?  114 GLU   B H    1 
ATOM   5717 H HA   . GLU   B 1 114 ? 31.675 -18.253 -2.181  1.00 15.55 ?  114 GLU   B HA   1 
ATOM   5718 H HB2  . GLU   B 1 114 ? 31.439 -17.660 0.555   1.00 16.53 ?  114 GLU   B HB2  1 
ATOM   5719 H HB3  . GLU   B 1 114 ? 30.792 -16.701 -0.541  1.00 16.53 ?  114 GLU   B HB3  1 
ATOM   5720 H HG2  . GLU   B 1 114 ? 29.403 -18.362 -1.264  1.00 16.56 ?  114 GLU   B HG2  1 
ATOM   5721 H HG3  . GLU   B 1 114 ? 30.151 -19.440 -0.376  1.00 16.56 ?  114 GLU   B HG3  1 
ATOM   5722 N N    . ASN   B 1 115 ? 34.283 -16.918 -1.020  1.00 12.51 ?  115 ASN   B N    1 
ATOM   5723 C CA   . ASN   B 1 115 ? 35.276 -15.887 -1.324  1.00 12.35 ?  115 ASN   B CA   1 
ATOM   5724 C C    . ASN   B 1 115 ? 35.681 -15.907 -2.790  1.00 12.08 ?  115 ASN   B C    1 
ATOM   5725 O O    . ASN   B 1 115 ? 36.070 -14.868 -3.345  1.00 12.65 ?  115 ASN   B O    1 
ATOM   5726 C CB   . ASN   B 1 115 ? 36.518 -16.060 -0.440  1.00 12.91 ?  115 ASN   B CB   1 
ATOM   5727 C CG   . ASN   B 1 115 ? 36.245 -15.795 1.021   1.00 13.23 ?  115 ASN   B CG   1 
ATOM   5728 O OD1  . ASN   B 1 115 ? 36.259 -14.648 1.464   1.00 15.54 ?  115 ASN   B OD1  1 
ATOM   5729 N ND2  . ASN   B 1 115 ? 36.070 -16.856 1.796   1.00 13.67 ?  115 ASN   B ND2  1 
ATOM   5730 H H    . ASN   B 1 115 ? 34.521 -17.473 -0.402  1.00 15.04 ?  115 ASN   B H    1 
ATOM   5731 H HA   . ASN   B 1 115 ? 34.903 -15.015 -1.132  1.00 14.85 ?  115 ASN   B HA   1 
ATOM   5732 H HB2  . ASN   B 1 115 ? 36.846 -16.970 -0.527  1.00 15.52 ?  115 ASN   B HB2  1 
ATOM   5733 H HB3  . ASN   B 1 115 ? 37.205 -15.436 -0.732  1.00 15.52 ?  115 ASN   B HB3  1 
ATOM   5734 H HD21 . ASN   B 1 115 ? 35.924 -16.755 2.636   1.00 16.43 ?  115 ASN   B HD21 1 
ATOM   5735 H HD22 . ASN   B 1 115 ? 36.086 -17.647 1.455   1.00 16.43 ?  115 ASN   B HD22 1 
ATOM   5736 N N    . PHE   B 1 116 ? 35.660 -17.089 -3.421  1.00 11.74 ?  116 PHE   B N    1 
ATOM   5737 C CA   . PHE   B 1 116 ? 36.090 -17.186 -4.809  1.00 12.50 ?  116 PHE   B CA   1 
ATOM   5738 C C    . PHE   B 1 116 ? 35.191 -16.362 -5.722  1.00 12.34 ?  116 PHE   B C    1 
ATOM   5739 O O    . PHE   B 1 116 ? 35.628 -15.938 -6.798  1.00 12.66 ?  116 PHE   B O    1 
ATOM   5740 C CB   . PHE   B 1 116 ? 36.061 -18.635 -5.329  1.00 12.19 ?  116 PHE   B CB   1 
ATOM   5741 C CG   . PHE   B 1 116 ? 37.124 -19.589 -4.770  1.00 12.23 ?  116 PHE   B CG   1 
ATOM   5742 C CD1  . PHE   B 1 116 ? 37.761 -19.407 -3.554  1.00 13.03 ?  116 PHE   B CD1  1 
ATOM   5743 C CD2  . PHE   B 1 116 ? 37.435 -20.727 -5.501  1.00 12.46 ?  116 PHE   B CD2  1 
ATOM   5744 C CE1  . PHE   B 1 116 ? 38.701 -20.337 -3.093  1.00 12.82 ?  116 PHE   B CE1  1 
ATOM   5745 C CE2  . PHE   B 1 116 ? 38.368 -21.661 -5.046  1.00 12.70 ?  116 PHE   B CE2  1 
ATOM   5746 C CZ   . PHE   B 1 116 ? 38.988 -21.475 -3.841  1.00 12.70 ?  116 PHE   B CZ   1 
ATOM   5747 H H    . PHE   B 1 116 ? 35.400 -17.836 -3.071  1.00 14.11 ?  116 PHE   B H    1 
ATOM   5748 H HA   . PHE   B 1 116 ? 36.997 -16.856 -4.889  1.00 15.03 ?  116 PHE   B HA   1 
ATOM   5749 H HB2  . PHE   B 1 116 ? 35.189 -19.016 -5.120  1.00 14.65 ?  116 PHE   B HB2  1 
ATOM   5750 H HB3  . PHE   B 1 116 ? 36.171 -18.614 -6.294  1.00 14.65 ?  116 PHE   B HB3  1 
ATOM   5751 H HD1  . PHE   B 1 116 ? 37.561 -18.655 -3.039  1.00 15.66 ?  116 PHE   B HD1  1 
ATOM   5752 H HD2  . PHE   B 1 116 ? 37.009 -20.878 -6.315  1.00 14.98 ?  116 PHE   B HD2  1 
ATOM   5753 H HE1  . PHE   B 1 116 ? 39.123 -20.198 -2.275  1.00 15.41 ?  116 PHE   B HE1  1 
ATOM   5754 H HE2  . PHE   B 1 116 ? 38.561 -22.412 -5.557  1.00 15.26 ?  116 PHE   B HE2  1 
ATOM   5755 H HZ   . PHE   B 1 116 ? 39.623 -22.083 -3.540  1.00 15.27 ?  116 PHE   B HZ   1 
ATOM   5756 N N    . ASN   B 1 117 ? 33.919 -16.167 -5.341  1.00 12.42 ?  117 ASN   B N    1 
ATOM   5757 C CA   . ASN   B 1 117 ? 32.974 -15.467 -6.209  1.00 12.87 ?  117 ASN   B CA   1 
ATOM   5758 C C    . ASN   B 1 117 ? 33.287 -13.986 -6.363  1.00 13.30 ?  117 ASN   B C    1 
ATOM   5759 O O    . ASN   B 1 117 ? 32.691 -13.332 -7.222  1.00 14.24 ?  117 ASN   B O    1 
ATOM   5760 C CB   . ASN   B 1 117 ? 31.551 -15.687 -5.714  1.00 13.09 ?  117 ASN   B CB   1 
ATOM   5761 C CG   . ASN   B 1 117 ? 31.094 -17.091 -5.965  1.00 13.28 ?  117 ASN   B CG   1 
ATOM   5762 O OD1  . ASN   B 1 117 ? 31.448 -17.686 -6.986  1.00 14.21 ?  117 ASN   B OD1  1 
ATOM   5763 N ND2  . ASN   B 1 117 ? 30.358 -17.658 -5.021  1.00 13.45 ?  117 ASN   B ND2  1 
ATOM   5764 H H    . ASN   B 1 117 ? 33.593 -16.428 -4.590  1.00 14.93 ?  117 ASN   B H    1 
ATOM   5765 H HA   . ASN   B 1 117 ? 33.035 -15.869 -7.090  1.00 15.48 ?  117 ASN   B HA   1 
ATOM   5766 H HB2  . ASN   B 1 117 ? 31.518 -15.521 -4.757  1.00 15.73 ?  117 ASN   B HB2  1 
ATOM   5767 H HB3  . ASN   B 1 117 ? 30.958 -15.078 -6.179  1.00 15.73 ?  117 ASN   B HB3  1 
ATOM   5768 H HD21 . ASN   B 1 117 ? 30.071 -18.463 -5.123  1.00 16.17 ?  117 ASN   B HD21 1 
ATOM   5769 H HD22 . ASN   B 1 117 ? 30.141 -17.213 -4.316  1.00 16.17 ?  117 ASN   B HD22 1 
ATOM   5770 N N    . GLN   B 1 118 ? 34.224 -13.456 -5.589  1.00 13.03 ?  118 GLN   B N    1 
ATOM   5771 C CA   . GLN   B 1 118 ? 34.650 -12.068 -5.732  1.00 13.74 ?  118 GLN   B CA   1 
ATOM   5772 C C    . GLN   B 1 118 ? 35.721 -11.881 -6.806  1.00 13.69 ?  118 GLN   B C    1 
ATOM   5773 O O    . GLN   B 1 118 ? 36.192 -10.756 -6.992  1.00 15.25 ?  118 GLN   B O    1 
ATOM   5774 C CB   . GLN   B 1 118 ? 35.129 -11.531 -4.378  1.00 14.17 ?  118 GLN   B CB   1 
ATOM   5775 C CG   . GLN   B 1 118 ? 34.053 -11.563 -3.303  1.00 14.19 ?  118 GLN   B CG   1 
ATOM   5776 C CD   . GLN   B 1 118 ? 32.882 -10.655 -3.631  1.00 14.40 ?  118 GLN   B CD   1 
ATOM   5777 O OE1  . GLN   B 1 118 ? 33.071 -9.511  -4.060  1.00 14.79 ?  118 GLN   B OE1  1 
ATOM   5778 N NE2  . GLN   B 1 118 ? 31.664 -11.152 -3.429  1.00 14.79 ?  118 GLN   B NE2  1 
ATOM   5779 H H    . GLN   B 1 118 ? 34.645 -13.884 -4.970  1.00 15.67 ?  118 GLN   B H    1 
ATOM   5780 H HA   . GLN   B 1 118 ? 33.883 -11.541 -6.002  1.00 16.52 ?  118 GLN   B HA   1 
ATOM   5781 H HB2  . GLN   B 1 118 ? 35.874 -12.060 -4.070  1.00 17.03 ?  118 GLN   B HB2  1 
ATOM   5782 H HB3  . GLN   B 1 118 ? 35.406 -10.602 -4.489  1.00 17.03 ?  118 GLN   B HB3  1 
ATOM   5783 H HG2  . GLN   B 1 118 ? 33.716 -12.466 -3.217  1.00 17.06 ?  118 GLN   B HG2  1 
ATOM   5784 H HG3  . GLN   B 1 118 ? 34.433 -11.265 -2.462  1.00 17.06 ?  118 GLN   B HG3  1 
ATOM   5785 H HE21 . GLN   B 1 118 ? 31.575 -11.952 -3.125  1.00 17.78 ?  118 GLN   B HE21 1 
ATOM   5786 H HE22 . GLN   B 1 118 ? 30.976 -10.673 -3.598  1.00 17.78 ?  118 GLN   B HE22 1 
ATOM   5787 N N    . HIS   B 1 119 ? 36.083 -12.942 -7.532  1.00 12.68 ?  119 HIS   B N    1 
ATOM   5788 C CA   . HIS   B 1 119 ? 37.125 -12.896 -8.549  1.00 13.13 ?  119 HIS   B CA   1 
ATOM   5789 C C    . HIS   B 1 119 ? 36.639 -13.637 -9.781  1.00 13.40 ?  119 HIS   B C    1 
ATOM   5790 O O    . HIS   B 1 119 ? 36.127 -14.753 -9.670  1.00 14.10 ?  119 HIS   B O    1 
ATOM   5791 C CB   . HIS   B 1 119 ? 38.407 -13.522 -7.994  1.00 13.82 ?  119 HIS   B CB   1 
ATOM   5792 C CG   . HIS   B 1 119 ? 38.885 -12.815 -6.769  1.00 15.06 ?  119 HIS   B CG   1 
ATOM   5793 N ND1  . HIS   B 1 119 ? 39.682 -11.691 -6.827  1.00 16.57 ?  119 HIS   B ND1  1 
ATOM   5794 C CD2  . HIS   B 1 119 ? 38.595 -13.006 -5.462  1.00 16.32 ?  119 HIS   B CD2  1 
ATOM   5795 C CE1  . HIS   B 1 119 ? 39.893 -11.247 -5.603  1.00 17.50 ?  119 HIS   B CE1  1 
ATOM   5796 N NE2  . HIS   B 1 119 ? 39.239 -12.020 -4.757  1.00 17.58 ?  119 HIS   B NE2  1 
ATOM   5797 H H    . HIS   B 1 119 ? 35.727 -13.723 -7.450  1.00 15.25 ?  119 HIS   B H    1 
ATOM   5798 H HA   . HIS   B 1 119 ? 37.307 -11.968 -8.787  1.00 15.78 ?  119 HIS   B HA   1 
ATOM   5799 H HB2  . HIS   B 1 119 ? 38.239 -14.445 -7.768  1.00 16.61 ?  119 HIS   B HB2  1 
ATOM   5800 H HB3  . HIS   B 1 119 ? 39.106 -13.462 -8.668  1.00 16.61 ?  119 HIS   B HB3  1 
ATOM   5801 H HD2  . HIS   B 1 119 ? 38.063 -13.681 -5.107  1.00 19.62 ?  119 HIS   B HD2  1 
ATOM   5802 H HE1  . HIS   B 1 119 ? 40.427 -10.520 -5.370  1.00 21.03 ?  119 HIS   B HE1  1 
ATOM   5803 H HE2  . HIS   B 1 119 ? 39.244 -11.940 -3.897  1.00 21.12 ?  119 HIS   B HE2  1 
ATOM   5804 N N    . GLU   B 1 120 ? 36.797 -13.028 -10.955 1.00 13.89 ?  120 GLU   B N    1 
ATOM   5805 C CA   . GLU   B 1 120 ? 36.206 -13.612 -12.154 1.00 15.53 ?  120 GLU   B CA   1 
ATOM   5806 C C    . GLU   B 1 120 ? 36.885 -14.914 -12.563 1.00 14.54 ?  120 GLU   B C    1 
ATOM   5807 O O    . GLU   B 1 120 ? 36.220 -15.797 -13.118 1.00 14.37 ?  120 GLU   B O    1 
ATOM   5808 C CB   . GLU   B 1 120 ? 36.203 -12.600 -13.300 1.00 19.81 ?  120 GLU   B CB   1 
ATOM   5809 C CG   . GLU   B 1 120 ? 35.268 -11.425 -13.051 1.00 25.28 ?  120 GLU   B CG   1 
ATOM   5810 C CD   . GLU   B 1 120 ? 35.087 -10.537 -14.266 1.00 30.53 ?  120 GLU   B CD   1 
ATOM   5811 O OE1  . GLU   B 1 120 ? 36.064 -10.353 -15.023 1.00 32.40 ?  120 GLU   B OE1  1 
ATOM   5812 O OE2  . GLU   B 1 120 ? 33.964 -10.019 -14.459 1.00 33.13 -1 120 GLU   B OE2  1 
ATOM   5813 H H    . GLU   B 1 120 ? 37.224 -12.288 -11.082 1.00 16.70 ?  120 GLU   B H    1 
ATOM   5814 H HA   . GLU   B 1 120 ? 35.281 -13.825 -11.958 1.00 18.67 ?  120 GLU   B HA   1 
ATOM   5815 H HB2  . GLU   B 1 120 ? 37.097 -12.251 -13.415 1.00 23.81 ?  120 GLU   B HB2  1 
ATOM   5816 H HB3  . GLU   B 1 120 ? 35.911 -13.047 -14.111 1.00 23.81 ?  120 GLU   B HB3  1 
ATOM   5817 H HG2  . GLU   B 1 120 ? 34.393 -11.765 -12.802 1.00 30.36 ?  120 GLU   B HG2  1 
ATOM   5818 H HG3  . GLU   B 1 120 ? 35.629 -10.882 -12.335 1.00 30.36 ?  120 GLU   B HG3  1 
ATOM   5819 N N    . VAL   B 1 121 ? 38.188 -15.055 -12.308 1.00 13.84 ?  121 VAL   B N    1 
ATOM   5820 C CA   . VAL   B 1 121 ? 38.932 -16.269 -12.648 1.00 13.95 ?  121 VAL   B CA   1 
ATOM   5821 C C    . VAL   B 1 121 ? 40.042 -16.470 -11.623 1.00 13.28 ?  121 VAL   B C    1 
ATOM   5822 O O    . VAL   B 1 121 ? 40.713 -15.508 -11.227 1.00 13.73 ?  121 VAL   B O    1 
ATOM   5823 C CB   . VAL   B 1 121 ? 39.462 -16.223 -14.101 1.00 15.49 ?  121 VAL   B CB   1 
ATOM   5824 C CG1  . VAL   B 1 121 ? 40.342 -15.000 -14.329 1.00 17.07 ?  121 VAL   B CG1  1 
ATOM   5825 C CG2  . VAL   B 1 121 ? 40.204 -17.510 -14.448 1.00 17.09 ?  121 VAL   B CG2  1 
ATOM   5826 H H    . VAL   B 1 121 ? 38.674 -14.445 -11.941 1.00 16.64 ?  121 VAL   B H    1 
ATOM   5827 H HA   . VAL   B 1 121 ? 38.324 -17.020 -12.585 1.00 16.77 ?  121 VAL   B HA   1 
ATOM   5828 H HB   . VAL   B 1 121 ? 38.703 -16.153 -14.707 1.00 18.62 ?  121 VAL   B HB   1 
ATOM   5829 H HG11 . VAL   B 1 121 ? 40.653 -14.999 -15.248 1.00 20.51 ?  121 VAL   B HG11 1 
ATOM   5830 H HG12 . VAL   B 1 121 ? 39.822 -14.198 -14.158 1.00 20.51 ?  121 VAL   B HG12 1 
ATOM   5831 H HG13 . VAL   B 1 121 ? 41.099 -15.037 -13.724 1.00 20.51 ?  121 VAL   B HG13 1 
ATOM   5832 H HG21 . VAL   B 1 121 ? 40.413 -17.509 -15.397 1.00 20.53 ?  121 VAL   B HG21 1 
ATOM   5833 H HG22 . VAL   B 1 121 ? 41.024 -17.553 -13.932 1.00 20.53 ?  121 VAL   B HG22 1 
ATOM   5834 H HG23 . VAL   B 1 121 ? 39.639 -18.269 -14.238 1.00 20.53 ?  121 VAL   B HG23 1 
ATOM   5835 N N    . LEU   B 1 122 ? 40.227 -17.725 -11.188 1.00 12.48 ?  122 LEU   B N    1 
ATOM   5836 C CA   . LEU   B 1 122 ? 41.210 -18.072 -10.163 1.00 12.82 ?  122 LEU   B CA   1 
ATOM   5837 C C    . LEU   B 1 122 ? 41.865 -19.402 -10.484 1.00 12.50 ?  122 LEU   B C    1 
ATOM   5838 O O    . LEU   B 1 122 ? 41.210 -20.324 -10.987 1.00 13.26 ?  122 LEU   B O    1 
ATOM   5839 C CB   . LEU   B 1 122 ? 40.558 -18.295 -8.787  1.00 14.21 ?  122 LEU   B CB   1 
ATOM   5840 C CG   . LEU   B 1 122 ? 39.526 -17.269 -8.302  1.00 14.12 ?  122 LEU   B CG   1 
ATOM   5841 C CD1  . LEU   B 1 122 ? 38.122 -17.602 -8.784  1.00 15.09 ?  122 LEU   B CD1  1 
ATOM   5842 C CD2  . LEU   B 1 122 ? 39.560 -17.143 -6.788  1.00 13.48 ?  122 LEU   B CD2  1 
ATOM   5843 H H    . LEU   B 1 122 ? 39.786 -18.401 -11.482 1.00 15.00 ?  122 LEU   B H    1 
ATOM   5844 H HA   . LEU   B 1 122 ? 41.889 -17.382 -10.094 1.00 15.41 ?  122 LEU   B HA   1 
ATOM   5845 H HB2  . LEU   B 1 122 ? 40.113 -19.151 -8.803  1.00 17.08 ?  122 LEU   B HB2  1 
ATOM   5846 H HB3  . LEU   B 1 122 ? 41.267 -18.313 -8.125  1.00 17.08 ?  122 LEU   B HB3  1 
ATOM   5847 H HG   . LEU   B 1 122 ? 39.765 -16.402 -8.663  1.00 16.97 ?  122 LEU   B HG   1 
ATOM   5848 H HD11 . LEU   B 1 122 ? 37.504 -16.959 -8.404  1.00 18.13 ?  122 LEU   B HD11 1 
ATOM   5849 H HD12 . LEU   B 1 122 ? 38.106 -17.544 -9.752  1.00 18.13 ?  122 LEU   B HD12 1 
ATOM   5850 H HD13 . LEU   B 1 122 ? 37.896 -18.495 -8.497  1.00 18.13 ?  122 LEU   B HD13 1 
ATOM   5851 H HD21 . LEU   B 1 122 ? 38.888 -16.503 -6.504  1.00 16.21 ?  122 LEU   B HD21 1 
ATOM   5852 H HD22 . LEU   B 1 122 ? 39.380 -18.010 -6.389  1.00 16.21 ?  122 LEU   B HD22 1 
ATOM   5853 H HD23 . LEU   B 1 122 ? 40.442 -16.834 -6.510  1.00 16.21 ?  122 LEU   B HD23 1 
ATOM   5854 N N    . LEU   B 1 123 ? 43.147 -19.506 -10.124 1.00 12.01 ?  123 LEU   B N    1 
ATOM   5855 C CA   . LEU   B 1 123 ? 43.859 -20.775 -9.996  1.00 12.38 ?  123 LEU   B CA   1 
ATOM   5856 C C    . LEU   B 1 123 ? 43.837 -21.161 -8.522  1.00 12.01 ?  123 LEU   B C    1 
ATOM   5857 O O    . LEU   B 1 123 ? 44.195 -20.333 -7.675  1.00 12.36 ?  123 LEU   B O    1 
ATOM   5858 C CB   . LEU   B 1 123 ? 45.309 -20.591 -10.448 1.00 13.00 ?  123 LEU   B CB   1 
ATOM   5859 C CG   . LEU   B 1 123 ? 46.256 -21.777 -10.211 1.00 13.19 ?  123 LEU   B CG   1 
ATOM   5860 C CD1  . LEU   B 1 123 ? 45.829 -23.019 -11.003 1.00 14.15 ?  123 LEU   B CD1  1 
ATOM   5861 C CD2  . LEU   B 1 123 ? 47.675 -21.372 -10.573 1.00 13.80 ?  123 LEU   B CD2  1 
ATOM   5862 H H    . LEU   B 1 123 ? 43.642 -18.830 -9.944  1.00 14.44 ?  123 LEU   B H    1 
ATOM   5863 H HA   . LEU   B 1 123 ? 43.434 -21.472 -10.526 1.00 14.89 ?  123 LEU   B HA   1 
ATOM   5864 H HB2  . LEU   B 1 123 ? 45.309 -20.413 -11.403 1.00 15.63 ?  123 LEU   B HB2  1 
ATOM   5865 H HB3  . LEU   B 1 123 ? 45.680 -19.830 -9.979  1.00 15.63 ?  123 LEU   B HB3  1 
ATOM   5866 H HG   . LEU   B 1 123 ? 46.247 -22.008 -9.269  1.00 15.85 ?  123 LEU   B HG   1 
ATOM   5867 H HD11 . LEU   B 1 123 ? 46.466 -23.727 -10.839 1.00 17.01 ?  123 LEU   B HD11 1 
ATOM   5868 H HD12 . LEU   B 1 123 ? 44.945 -23.286 -10.710 1.00 17.01 ?  123 LEU   B HD12 1 
ATOM   5869 H HD13 . LEU   B 1 123 ? 45.813 -22.794 -11.947 1.00 17.01 ?  123 LEU   B HD13 1 
ATOM   5870 H HD21 . LEU   B 1 123 ? 48.265 -22.124 -10.419 1.00 16.59 ?  123 LEU   B HD21 1 
ATOM   5871 H HD22 . LEU   B 1 123 ? 47.699 -21.112 -11.506 1.00 16.59 ?  123 LEU   B HD22 1 
ATOM   5872 H HD23 . LEU   B 1 123 ? 47.938 -20.623 -10.013 1.00 16.59 ?  123 LEU   B HD23 1 
ATOM   5873 N N    . ALA   B 1 124 ? 43.407 -22.392 -8.208  1.00 12.08 ?  124 ALA   B N    1 
ATOM   5874 C CA   . ALA   B 1 124 ? 43.138 -22.699 -6.811  1.00 12.27 ?  124 ALA   B CA   1 
ATOM   5875 C C    . ALA   B 1 124 ? 43.415 -24.159 -6.478  1.00 11.58 ?  124 ALA   B C    1 
ATOM   5876 O O    . ALA   B 1 124 ? 43.280 -25.044 -7.336  1.00 12.28 ?  124 ALA   B O    1 
ATOM   5877 C CB   . ALA   B 1 124 ? 41.679 -22.393 -6.473  1.00 12.57 ?  124 ALA   B CB   1 
ATOM   5878 H H    . ALA   B 1 124 ? 43.237 -23.032 -8.769  1.00 14.53 ?  124 ALA   B H    1 
ATOM   5879 H HA   . ALA   B 1 124 ? 43.707 -22.139 -6.265  1.00 14.75 ?  124 ALA   B HA   1 
ATOM   5880 H HB1  . ALA   B 1 124 ? 41.514 -22.599 -5.544  1.00 15.11 ?  124 ALA   B HB1  1 
ATOM   5881 H HB2  . ALA   B 1 124 ? 41.506 -21.451 -6.643  1.00 15.11 ?  124 ALA   B HB2  1 
ATOM   5882 H HB3  . ALA   B 1 124 ? 41.101 -22.935 -7.041  1.00 15.11 ?  124 ALA   B HB3  1 
ATOM   5883 N N    . PRO   B 1 125 ? 43.703 -24.446 -5.212  1.00 11.90 ?  125 PRO   B N    1 
ATOM   5884 C CA   . PRO   B 1 125 ? 43.641 -25.811 -4.690  1.00 12.75 ?  125 PRO   B CA   1 
ATOM   5885 C C    . PRO   B 1 125 ? 42.242 -26.084 -4.141  1.00 12.99 ?  125 PRO   B C    1 
ATOM   5886 O O    . PRO   B 1 125 ? 41.449 -25.164 -3.927  1.00 13.36 ?  125 PRO   B O    1 
ATOM   5887 C CB   . PRO   B 1 125 ? 44.628 -25.736 -3.521  1.00 13.93 ?  125 PRO   B CB   1 
ATOM   5888 C CG   . PRO   B 1 125 ? 44.388 -24.350 -2.952  1.00 13.73 ?  125 PRO   B CG   1 
ATOM   5889 C CD   . PRO   B 1 125 ? 44.041 -23.476 -4.152  1.00 12.78 ?  125 PRO   B CD   1 
ATOM   5890 H HA   . PRO   B 1 125 ? 43.912 -26.479 -5.334  1.00 15.33 ?  125 PRO   B HA   1 
ATOM   5891 H HB2  . PRO   B 1 125 ? 44.423 -26.415 -2.857  1.00 16.74 ?  125 PRO   B HB2  1 
ATOM   5892 H HB3  . PRO   B 1 125 ? 45.537 -25.821 -3.839  1.00 16.74 ?  125 PRO   B HB3  1 
ATOM   5893 H HG2  . PRO   B 1 125 ? 43.648 -24.375 -2.322  1.00 16.51 ?  125 PRO   B HG2  1 
ATOM   5894 H HG3  . PRO   B 1 125 ? 45.194 -24.029 -2.512  1.00 16.51 ?  125 PRO   B HG3  1 
ATOM   5895 H HD2  . PRO   B 1 125 ? 43.281 -22.908 -3.953  1.00 15.36 ?  125 PRO   B HD2  1 
ATOM   5896 H HD3  . PRO   B 1 125 ? 44.815 -22.947 -4.418  1.00 15.36 ?  125 PRO   B HD3  1 
ATOM   5897 N N    . LEU   B 1 126 ? 41.971 -27.365 -3.859  1.00 13.31 ?  126 LEU   B N    1 
ATOM   5898 C CA   . LEU   B 1 126 ? 40.749 -27.726 -3.142  1.00 14.04 ?  126 LEU   B CA   1 
ATOM   5899 C C    . LEU   B 1 126 ? 40.864 -27.324 -1.679  1.00 13.99 ?  126 LEU   B C    1 
ATOM   5900 O O    . LEU   B 1 126 ? 41.751 -27.792 -0.962  1.00 15.97 ?  126 LEU   B O    1 
ATOM   5901 C CB   . LEU   B 1 126 ? 40.487 -29.224 -3.252  1.00 15.26 ?  126 LEU   B CB   1 
ATOM   5902 C CG   . LEU   B 1 126 ? 39.969 -29.717 -4.604  1.00 16.40 ?  126 LEU   B CG   1 
ATOM   5903 C CD1  . LEU   B 1 126 ? 40.027 -31.233 -4.680  1.00 18.25 ?  126 LEU   B CD1  1 
ATOM   5904 C CD2  . LEU   B 1 126 ? 38.544 -29.238 -4.852  1.00 16.92 ?  126 LEU   B CD2  1 
ATOM   5905 H H    . LEU   B 1 126 ? 42.478 -28.033 -4.054  1.00 16.00 ?  126 LEU   B H    1 
ATOM   5906 H HA   . LEU   B 1 126 ? 40.001 -27.251 -3.527  1.00 16.87 ?  126 LEU   B HA   1 
ATOM   5907 H HB2  . LEU   B 1 126 ? 41.313 -29.694 -3.070  1.00 18.34 ?  126 LEU   B HB2  1 
ATOM   5908 H HB3  . LEU   B 1 126 ? 39.823 -29.467 -2.586  1.00 18.34 ?  126 LEU   B HB3  1 
ATOM   5909 H HG   . LEU   B 1 126 ? 40.535 -29.356 -5.308  1.00 19.71 ?  126 LEU   B HG   1 
ATOM   5910 H HD11 . LEU   B 1 126 ? 39.695 -31.515 -5.546  1.00 21.93 ?  126 LEU   B HD11 1 
ATOM   5911 H HD12 . LEU   B 1 126 ? 40.946 -31.518 -4.567  1.00 21.93 ?  126 LEU   B HD12 1 
ATOM   5912 H HD13 . LEU   B 1 126 ? 39.475 -31.601 -3.974  1.00 21.93 ?  126 LEU   B HD13 1 
ATOM   5913 H HD21 . LEU   B 1 126 ? 38.216 -29.637 -5.673  1.00 20.34 ?  126 LEU   B HD21 1 
ATOM   5914 H HD22 . LEU   B 1 126 ? 37.987 -29.509 -4.106  1.00 20.34 ?  126 LEU   B HD22 1 
ATOM   5915 H HD23 . LEU   B 1 126 ? 38.542 -28.270 -4.931  1.00 20.34 ?  126 LEU   B HD23 1 
ATOM   5916 N N    . LEU   B 1 127 ? 39.938 -26.489 -1.223  1.00 13.63 ?  127 LEU   B N    1 
ATOM   5917 C CA   . LEU   B 1 127 ? 39.986 -25.993 0.142   1.00 14.24 ?  127 LEU   B CA   1 
ATOM   5918 C C    . LEU   B 1 127 ? 39.717 -27.114 1.136   1.00 14.52 ?  127 LEU   B C    1 
ATOM   5919 O O    . LEU   B 1 127 ? 38.900 -28.013 0.904   1.00 15.10 ?  127 LEU   B O    1 
ATOM   5920 C CB   . LEU   B 1 127 ? 38.960 -24.874 0.345   1.00 14.90 ?  127 LEU   B CB   1 
ATOM   5921 C CG   . LEU   B 1 127 ? 39.139 -23.610 -0.497  1.00 15.43 ?  127 LEU   B CG   1 
ATOM   5922 C CD1  . LEU   B 1 127 ? 38.025 -22.629 -0.184  1.00 15.53 ?  127 LEU   B CD1  1 
ATOM   5923 C CD2  . LEU   B 1 127 ? 40.508 -22.968 -0.263  1.00 15.98 ?  127 LEU   B CD2  1 
ATOM   5924 H H    . LEU   B 1 127 ? 39.278 -26.183 -1.687  1.00 16.38 ?  127 LEU   B H    1 
ATOM   5925 H HA   . LEU   B 1 127 ? 40.867 -25.627 0.322   1.00 17.12 ?  127 LEU   B HA   1 
ATOM   5926 H HB2  . LEU   B 1 127 ? 38.077 -25.231 0.144   1.00 17.91 ?  127 LEU   B HB2  1 
ATOM   5927 H HB3  . LEU   B 1 127 ? 38.983 -24.603 1.278   1.00 17.91 ?  127 LEU   B HB3  1 
ATOM   5928 H HG   . LEU   B 1 127 ? 39.065 -23.843 -1.432  1.00 18.54 ?  127 LEU   B HG   1 
ATOM   5929 H HD11 . LEU   B 1 127 ? 38.152 -21.825 -0.718  1.00 18.66 ?  127 LEU   B HD11 1 
ATOM   5930 H HD12 . LEU   B 1 127 ? 37.169 -23.031 -0.396  1.00 18.66 ?  127 LEU   B HD12 1 
ATOM   5931 H HD13 . LEU   B 1 127 ? 38.056 -22.398 0.760   1.00 18.66 ?  127 LEU   B HD13 1 
ATOM   5932 H HD21 . LEU   B 1 127 ? 40.541 -22.116 -0.727  1.00 19.20 ?  127 LEU   B HD21 1 
ATOM   5933 H HD22 . LEU   B 1 127 ? 40.634 -22.827 0.691   1.00 19.20 ?  127 LEU   B HD22 1 
ATOM   5934 H HD23 . LEU   B 1 127 ? 41.194 -23.559 -0.603  1.00 19.20 ?  127 LEU   B HD23 1 
ATOM   5935 N N    . SER   B 1 128 ? 40.397 -27.029 2.268   1.00 14.39 ?  128 SER   B N    1 
ATOM   5936 C CA   . SER   B 1 128 ? 40.284 -27.945 3.391   1.00 15.02 ?  128 SER   B CA   1 
ATOM   5937 C C    . SER   B 1 128 ? 40.780 -29.351 3.072   1.00 15.85 ?  128 SER   B C    1 
ATOM   5938 O O    . SER   B 1 128 ? 40.675 -30.231 3.922   1.00 17.27 ?  128 SER   B O    1 
ATOM   5939 C CB   . SER   B 1 128 ? 38.882 -27.950 4.013   1.00 15.39 ?  128 SER   B CB   1 
ATOM   5940 O OG   . SER   B 1 128 ? 38.566 -26.665 4.541   1.00 15.94 ?  128 SER   B OG   1 
ATOM   5941 H H    . SER   B 1 128 ? 40.967 -26.403 2.418   1.00 17.29 ?  128 SER   B H    1 
ATOM   5942 H HA   . SER   B 1 128 ? 40.869 -27.612 4.076   1.00 18.06 ?  128 SER   B HA   1 
ATOM   5943 H HB2  . SER   B 1 128 ? 38.227 -28.195 3.337   1.00 18.50 ?  128 SER   B HB2  1 
ATOM   5944 H HB3  . SER   B 1 128 ? 38.860 -28.609 4.736   1.00 18.50 ?  128 SER   B HB3  1 
ATOM   5945 H HG   . SER   B 1 128 ? 39.135 -26.461 5.122   1.00 19.16 ?  128 SER   B HG   1 
ATOM   5946 N N    . ALA   B 1 129 ? 41.366 -29.570 1.893   1.00 17.02 ?  129 ALA   B N    1 
ATOM   5947 C CA   . ALA   B 1 129 ? 41.916 -30.868 1.531   1.00 17.73 ?  129 ALA   B CA   1 
ATOM   5948 C C    . ALA   B 1 129 ? 43.304 -31.048 2.132   1.00 16.91 ?  129 ALA   B C    1 
ATOM   5949 O O    . ALA   B 1 129 ? 43.860 -30.149 2.776   1.00 16.70 ?  129 ALA   B O    1 
ATOM   5950 C CB   . ALA   B 1 129 ? 41.984 -31.008 0.012   1.00 19.86 ?  129 ALA   B CB   1 
ATOM   5951 H H    . ALA   B 1 129 ? 41.461 -28.971 1.279   1.00 20.46 ?  129 ALA   B H    1 
ATOM   5952 H HA   . ALA   B 1 129 ? 41.344 -31.565 1.878   1.00 21.31 ?  129 ALA   B HA   1 
ATOM   5953 H HB1  . ALA   B 1 129 ? 42.341 -31.883 -0.208  1.00 23.86 ?  129 ALA   B HB1  1 
ATOM   5954 H HB2  . ALA   B 1 129 ? 41.091 -30.913 -0.352  1.00 23.86 ?  129 ALA   B HB2  1 
ATOM   5955 H HB3  . ALA   B 1 129 ? 42.563 -30.315 -0.345  1.00 23.86 ?  129 ALA   B HB3  1 
ATOM   5956 N N    . GLY   B 1 130 ? 43.873 -32.232 1.898   1.00 17.02 ?  130 GLY   B N    1 
ATOM   5957 C CA   . GLY   B 1 130 ? 45.258 -32.472 2.261   1.00 17.55 ?  130 GLY   B CA   1 
ATOM   5958 C C    . GLY   B 1 130 ? 45.456 -32.372 3.754   1.00 17.60 ?  130 GLY   B C    1 
ATOM   5959 O O    . GLY   B 1 130 ? 44.746 -33.008 4.547   1.00 18.34 ?  130 GLY   B O    1 
ATOM   5960 H H    . GLY   B 1 130 ? 43.482 -32.899 1.522   1.00 20.46 ?  130 GLY   B H    1 
ATOM   5961 H HA2  . GLY   B 1 130 ? 45.521 -33.362 1.971   1.00 21.09 ?  130 GLY   B HA2  1 
ATOM   5962 H HA3  . GLY   B 1 130 ? 45.831 -31.824 1.824   1.00 21.09 ?  130 GLY   B HA3  1 
ATOM   5963 N N    . ILE   B 1 131 ? 46.428 -31.545 4.148   1.00 18.12 ?  131 ILE   B N    1 
ATOM   5964 C CA   . ILE   B 1 131 ? 46.773 -31.408 5.553   1.00 18.79 ?  131 ILE   B CA   1 
ATOM   5965 C C    . ILE   B 1 131 ? 45.650 -30.808 6.381   1.00 17.96 ?  131 ILE   B C    1 
ATOM   5966 O O    . ILE   B 1 131 ? 45.708 -30.873 7.610   1.00 19.51 ?  131 ILE   B O    1 
ATOM   5967 C CB   . ILE   B 1 131 ? 48.096 -30.629 5.758   1.00 20.50 ?  131 ILE   B CB   1 
ATOM   5968 C CG1  . ILE   B 1 131 ? 47.935 -29.148 5.380   1.00 21.35 ?  131 ILE   B CG1  1 
ATOM   5969 C CG2  . ILE   B 1 131 ? 49.226 -31.274 4.961   1.00 21.47 ?  131 ILE   B CG2  1 
ATOM   5970 C CD1  . ILE   B 1 131 ? 49.153 -28.297 5.704   1.00 22.28 ?  131 ILE   B CD1  1 
ATOM   5971 H H    . ILE   B 1 131 ? 46.898 -31.054 3.615   1.00 21.78 ?  131 ILE   B H    1 
ATOM   5972 H HA   . ILE   B 1 131 ? 46.916 -32.293 5.905   1.00 22.58 ?  131 ILE   B HA   1 
ATOM   5973 H HB   . ILE   B 1 131 ? 48.319 -30.672 6.703   1.00 24.63 ?  131 ILE   B HB   1 
ATOM   5974 H HG12 . ILE   B 1 131 ? 47.773 -29.088 4.427   1.00 25.65 ?  131 ILE   B HG12 1 
ATOM   5975 H HG13 . ILE   B 1 131 ? 47.181 -28.771 5.864   1.00 25.65 ?  131 ILE   B HG13 1 
ATOM   5976 H HG21 . ILE   B 1 131 ? 50.062 -30.868 5.226   1.00 25.79 ?  131 ILE   B HG21 1 
ATOM   5977 H HG22 . ILE   B 1 131 ? 49.234 -32.221 5.148   1.00 25.79 ?  131 ILE   B HG22 1 
ATOM   5978 H HG23 . ILE   B 1 131 ? 49.061 -31.120 4.017   1.00 25.79 ?  131 ILE   B HG23 1 
ATOM   5979 H HD11 . ILE   B 1 131 ? 48.937 -27.367 5.537   1.00 26.76 ?  131 ILE   B HD11 1 
ATOM   5980 H HD12 . ILE   B 1 131 ? 49.382 -28.421 6.639   1.00 26.76 ?  131 ILE   B HD12 1 
ATOM   5981 H HD13 . ILE   B 1 131 ? 49.889 -28.576 5.141   1.00 26.76 ?  131 ILE   B HD13 1 
ATOM   5982 N N    . PHE   B 1 132 ? 44.630 -30.219 5.744   1.00 16.51 ?  132 PHE   B N    1 
ATOM   5983 C CA   . PHE   B 1 132 ? 43.468 -29.715 6.470   1.00 16.80 ?  132 PHE   B CA   1 
ATOM   5984 C C    . PHE   B 1 132 ? 42.444 -30.805 6.796   1.00 18.13 ?  132 PHE   B C    1 
ATOM   5985 O O    . PHE   B 1 132 ? 41.527 -30.554 7.587   1.00 19.59 ?  132 PHE   B O    1 
ATOM   5986 C CB   . PHE   B 1 132 ? 42.792 -28.585 5.684   1.00 16.22 ?  132 PHE   B CB   1 
ATOM   5987 C CG   . PHE   B 1 132 ? 43.495 -27.243 5.790   1.00 16.38 ?  132 PHE   B CG   1 
ATOM   5988 C CD1  . PHE   B 1 132 ? 44.787 -27.064 5.320   1.00 17.22 ?  132 PHE   B CD1  1 
ATOM   5989 C CD2  . PHE   B 1 132 ? 42.825 -26.142 6.311   1.00 16.08 ?  132 PHE   B CD2  1 
ATOM   5990 C CE1  . PHE   B 1 132 ? 45.405 -25.822 5.407   1.00 17.85 ?  132 PHE   B CE1  1 
ATOM   5991 C CE2  . PHE   B 1 132 ? 43.435 -24.899 6.395   1.00 16.57 ?  132 PHE   B CE2  1 
ATOM   5992 C CZ   . PHE   B 1 132 ? 44.721 -24.742 5.943   1.00 17.34 ?  132 PHE   B CZ   1 
ATOM   5993 H H    . PHE   B 1 132 ? 44.584 -30.101 4.891   1.00 19.84 ?  132 PHE   B H    1 
ATOM   5994 H HA   . PHE   B 1 132 ? 43.771 -29.338 7.308   1.00 20.18 ?  132 PHE   B HA   1 
ATOM   5995 H HB2  . PHE   B 1 132 ? 42.772 -28.825 4.748   1.00 19.49 ?  132 PHE   B HB2  1 
ATOM   5996 H HB3  . PHE   B 1 132 ? 41.886 -28.466 6.015   1.00 19.49 ?  132 PHE   B HB3  1 
ATOM   5997 H HD1  . PHE   B 1 132 ? 45.251 -27.787 4.961   1.00 20.69 ?  132 PHE   B HD1  1 
ATOM   5998 H HD2  . PHE   B 1 132 ? 41.955 -26.244 6.620   1.00 19.33 ?  132 PHE   B HD2  1 
ATOM   5999 H HE1  . PHE   B 1 132 ? 46.276 -25.715 5.102   1.00 21.45 ?  132 PHE   B HE1  1 
ATOM   6000 H HE2  . PHE   B 1 132 ? 42.976 -24.176 6.760   1.00 19.91 ?  132 PHE   B HE2  1 
ATOM   6001 H HZ   . PHE   B 1 132 ? 45.137 -23.908 6.003   1.00 20.83 ?  132 PHE   B HZ   1 
ATOM   6002 N N    . GLY   B 1 133 ? 42.556 -32.000 6.204   1.00 17.91 ?  133 GLY   B N    1 
ATOM   6003 C CA   . GLY   B 1 133 ? 41.841 -33.168 6.692   1.00 18.84 ?  133 GLY   B CA   1 
ATOM   6004 C C    . GLY   B 1 133 ? 40.442 -33.425 6.157   1.00 19.25 ?  133 GLY   B C    1 
ATOM   6005 O O    . GLY   B 1 133 ? 39.845 -34.438 6.533   1.00 20.95 ?  133 GLY   B O    1 
ATOM   6006 H H    . GLY   B 1 133 ? 43.056 -32.151 5.518   1.00 21.52 ?  133 GLY   B H    1 
ATOM   6007 H HA2  . GLY   B 1 133 ? 42.377 -33.951 6.494   1.00 22.64 ?  133 GLY   B HA2  1 
ATOM   6008 H HA3  . GLY   B 1 133 ? 41.775 -33.096 7.657   1.00 22.64 ?  133 GLY   B HA3  1 
ATOM   6009 N N    . ALA   B 1 134 ? 39.890 -32.563 5.311   1.00 18.30 ?  134 ALA   B N    1 
ATOM   6010 C CA   . ALA   B 1 134 ? 38.562 -32.840 4.780   1.00 18.51 ?  134 ALA   B CA   1 
ATOM   6011 C C    . ALA   B 1 134 ? 38.643 -33.845 3.635   1.00 18.30 ?  134 ALA   B C    1 
ATOM   6012 O O    . ALA   B 1 134 ? 39.693 -34.041 3.015   1.00 19.37 ?  134 ALA   B O    1 
ATOM   6013 C CB   . ALA   B 1 134 ? 37.896 -31.557 4.287   1.00 19.01 ?  134 ALA   B CB   1 
ATOM   6014 H H    . ALA   B 1 134 ? 40.251 -31.826 5.041   1.00 21.99 ?  134 ALA   B H    1 
ATOM   6015 H HA   . ALA   B 1 134 ? 38.012 -33.213 5.489   1.00 22.24 ?  134 ALA   B HA   1 
ATOM   6016 H HB1  . ALA   B 1 134 ? 37.007 -31.771 3.964   1.00 22.85 ?  134 ALA   B HB1  1 
ATOM   6017 H HB2  . ALA   B 1 134 ? 37.838 -30.925 5.021   1.00 22.85 ?  134 ALA   B HB2  1 
ATOM   6018 H HB3  . ALA   B 1 134 ? 38.428 -31.182 3.568   1.00 22.85 ?  134 ALA   B HB3  1 
ATOM   6019 N N    . ASP   B 1 135 ? 37.508 -34.477 3.354   1.00 18.34 ?  135 ASP   B N    1 
ATOM   6020 C CA   . ASP   B 1 135 ? 37.408 -35.371 2.210   1.00 19.19 ?  135 ASP   B CA   1 
ATOM   6021 C C    . ASP   B 1 135 ? 37.512 -34.536 0.940   1.00 17.86 ?  135 ASP   B C    1 
ATOM   6022 O O    . ASP   B 1 135 ? 36.654 -33.668 0.709   1.00 17.95 ?  135 ASP   B O    1 
ATOM   6023 C CB   . ASP   B 1 135 ? 36.067 -36.098 2.260   1.00 21.24 ?  135 ASP   B CB   1 
ATOM   6024 C CG   . ASP   B 1 135 ? 35.883 -37.089 1.126   1.00 22.82 ?  135 ASP   B CG   1 
ATOM   6025 O OD1  . ASP   B 1 135 ? 36.745 -37.155 0.225   1.00 22.61 ?  135 ASP   B OD1  1 
ATOM   6026 O OD2  . ASP   B 1 135 ? 34.874 -37.833 1.153   1.00 25.67 -1 135 ASP   B OD2  1 
ATOM   6027 H H    . ASP   B 1 135 ? 36.784 -34.402 3.815   1.00 22.04 ?  135 ASP   B H    1 
ATOM   6028 H HA   . ASP   B 1 135 ? 38.127 -36.024 2.247   1.00 23.05 ?  135 ASP   B HA   1 
ATOM   6029 H HB2  . ASP   B 1 135 ? 36.009 -36.592 3.089   1.00 25.52 ?  135 ASP   B HB2  1 
ATOM   6030 H HB3  . ASP   B 1 135 ? 35.358 -35.444 2.204   1.00 25.52 ?  135 ASP   B HB3  1 
ATOM   6031 N N    . PRO   B 1 136 ? 38.531 -34.738 0.103   1.00 18.33 ?  136 PRO   B N    1 
ATOM   6032 C CA   . PRO   B 1 136 ? 38.627 -33.923 -1.118  1.00 17.58 ?  136 PRO   B CA   1 
ATOM   6033 C C    . PRO   B 1 136 ? 37.436 -34.084 -2.040  1.00 16.91 ?  136 PRO   B C    1 
ATOM   6034 O O    . PRO   B 1 136 ? 37.114 -33.141 -2.769  1.00 16.72 ?  136 PRO   B O    1 
ATOM   6035 C CB   . PRO   B 1 136 ? 39.936 -34.400 -1.762  1.00 18.51 ?  136 PRO   B CB   1 
ATOM   6036 C CG   . PRO   B 1 136 ? 40.140 -35.785 -1.208  1.00 19.81 ?  136 PRO   B CG   1 
ATOM   6037 C CD   . PRO   B 1 136 ? 39.625 -35.719 0.198   1.00 19.23 ?  136 PRO   B CD   1 
ATOM   6038 H HA   . PRO   B 1 136 ? 38.714 -32.986 -0.887  1.00 21.13 ?  136 PRO   B HA   1 
ATOM   6039 H HB2  . PRO   B 1 136 ? 39.837 -34.429 -2.727  1.00 22.24 ?  136 PRO   B HB2  1 
ATOM   6040 H HB3  . PRO   B 1 136 ? 40.660 -33.814 -1.504  1.00 22.24 ?  136 PRO   B HB3  1 
ATOM   6041 H HG2  . PRO   B 1 136 ? 39.632 -36.431 -1.725  1.00 23.80 ?  136 PRO   B HG2  1 
ATOM   6042 H HG3  . PRO   B 1 136 ? 41.085 -36.008 -1.213  1.00 23.80 ?  136 PRO   B HG3  1 
ATOM   6043 H HD2  . PRO   B 1 136 ? 39.284 -36.582 0.480   1.00 23.10 ?  136 PRO   B HD2  1 
ATOM   6044 H HD3  . PRO   B 1 136 ? 40.312 -35.393 0.804   1.00 23.10 ?  136 PRO   B HD3  1 
ATOM   6045 N N    . ILE   B 1 137 ? 36.773 -35.246 -2.032  1.00 17.48 ?  137 ILE   B N    1 
ATOM   6046 C CA   . ILE   B 1 137 ? 35.558 -35.419 -2.825  1.00 17.66 ?  137 ILE   B CA   1 
ATOM   6047 C C    . ILE   B 1 137 ? 34.479 -34.449 -2.358  1.00 17.04 ?  137 ILE   B C    1 
ATOM   6048 O O    . ILE   B 1 137 ? 33.765 -33.842 -3.169  1.00 16.81 ?  137 ILE   B O    1 
ATOM   6049 C CB   . ILE   B 1 137 ? 35.090 -36.887 -2.762  1.00 19.42 ?  137 ILE   B CB   1 
ATOM   6050 C CG1  . ILE   B 1 137 ? 36.116 -37.796 -3.446  1.00 21.71 ?  137 ILE   B CG1  1 
ATOM   6051 C CG2  . ILE   B 1 137 ? 33.699 -37.032 -3.383  1.00 19.96 ?  137 ILE   B CG2  1 
ATOM   6052 C CD1  . ILE   B 1 137 ? 35.783 -39.267 -3.377  1.00 24.06 ?  137 ILE   B CD1  1 
ATOM   6053 H H    . ILE   B 1 137 ? 37.004 -35.940 -1.583  1.00 21.00 ?  137 ILE   B H    1 
ATOM   6054 H HA   . ILE   B 1 137 ? 35.755 -35.213 -3.752  1.00 21.22 ?  137 ILE   B HA   1 
ATOM   6055 H HB   . ILE   B 1 137 ? 35.027 -37.144 -1.834  1.00 23.34 ?  137 ILE   B HB   1 
ATOM   6056 H HG12 . ILE   B 1 137 ? 36.179 -37.552 -4.382  1.00 26.08 ?  137 ILE   B HG12 1 
ATOM   6057 H HG13 . ILE   B 1 137 ? 36.976 -37.670 -3.015  1.00 26.08 ?  137 ILE   B HG13 1 
ATOM   6058 H HG21 . ILE   B 1 137 ? 33.441 -37.968 -3.387  1.00 23.98 ?  137 ILE   B HG21 1 
ATOM   6059 H HG22 . ILE   B 1 137 ? 33.056 -36.532 -2.859  1.00 23.98 ?  137 ILE   B HG22 1 
ATOM   6060 H HG23 . ILE   B 1 137 ? 33.720 -36.695 -4.292  1.00 23.98 ?  137 ILE   B HG23 1 
ATOM   6061 H HD11 . ILE   B 1 137 ? 36.450 -39.748 -3.885  1.00 28.90 ?  137 ILE   B HD11 1 
ATOM   6062 H HD12 . ILE   B 1 137 ? 35.795 -39.556 -2.450  1.00 28.90 ?  137 ILE   B HD12 1 
ATOM   6063 H HD13 . ILE   B 1 137 ? 34.909 -39.426 -3.764  1.00 28.90 ?  137 ILE   B HD13 1 
ATOM   6064 N N    . HIS   B 1 138 ? 34.345 -34.288 -1.044  1.00 17.17 ?  138 HIS   B N    1 
ATOM   6065 C CA   . HIS   B 1 138 ? 33.398 -33.317 -0.513  1.00 17.53 ?  138 HIS   B CA   1 
ATOM   6066 C C    . HIS   B 1 138 ? 33.819 -31.891 -0.843  1.00 16.88 ?  138 HIS   B C    1 
ATOM   6067 O O    . HIS   B 1 138 ? 32.972 -31.047 -1.158  1.00 17.52 ?  138 HIS   B O    1 
ATOM   6068 C CB   . HIS   B 1 138 ? 33.280 -33.487 0.994   1.00 18.76 ?  138 HIS   B CB   1 
ATOM   6069 C CG   . HIS   B 1 138 ? 32.356 -32.499 1.628   1.00 19.65 ?  138 HIS   B CG   1 
ATOM   6070 N ND1  . HIS   B 1 138 ? 31.015 -32.432 1.318   1.00 21.02 ?  138 HIS   B ND1  1 
ATOM   6071 C CD2  . HIS   B 1 138 ? 32.586 -31.515 2.529   1.00 20.21 ?  138 HIS   B CD2  1 
ATOM   6072 C CE1  . HIS   B 1 138 ? 30.455 -31.460 2.015   1.00 20.91 ?  138 HIS   B CE1  1 
ATOM   6073 N NE2  . HIS   B 1 138 ? 31.384 -30.896 2.765   1.00 20.44 ?  138 HIS   B NE2  1 
ATOM   6074 H H    . HIS   B 1 138 ? 34.786 -34.723 -0.450  1.00 20.63 ?  138 HIS   B H    1 
ATOM   6075 H HA   . HIS   B 1 138 ? 32.524 -33.476 -0.906  1.00 21.07 ?  138 HIS   B HA   1 
ATOM   6076 H HB2  . HIS   B 1 138 ? 32.936 -34.373 1.188   1.00 22.55 ?  138 HIS   B HB2  1 
ATOM   6077 H HB3  . HIS   B 1 138 ? 34.153 -33.373 1.396   1.00 22.55 ?  138 HIS   B HB3  1 
ATOM   6078 H HD1  . HIS   B 1 138 ? 30.606 -32.946 0.764   1.00 25.25 ?  138 HIS   B HD1  1 
ATOM   6079 H HD2  . HIS   B 1 138 ? 33.394 -31.310 2.934   1.00 24.28 ?  138 HIS   B HD2  1 
ATOM   6080 H HE1  . HIS   B 1 138 ? 29.552 -31.224 1.991   1.00 25.12 ?  138 HIS   B HE1  1 
ATOM   6081 N N    . SER   B 1 139 ? 35.115 -31.592 -0.763  1.00 16.45 ?  139 SER   B N    1 
ATOM   6082 C CA   . SER   B 1 139 ? 35.559 -30.245 -1.092  1.00 15.87 ?  139 SER   B CA   1 
ATOM   6083 C C    . SER   B 1 139 ? 35.223 -29.905 -2.535  1.00 15.26 ?  139 SER   B C    1 
ATOM   6084 O O    . SER   B 1 139 ? 34.781 -28.787 -2.824  1.00 15.19 ?  139 SER   B O    1 
ATOM   6085 C CB   . SER   B 1 139 ? 37.054 -30.109 -0.826  1.00 16.49 ?  139 SER   B CB   1 
ATOM   6086 O OG   . SER   B 1 139 ? 37.457 -28.778 -1.079  1.00 16.68 ?  139 SER   B OG   1 
ATOM   6087 H H    . SER   B 1 139 ? 35.734 -32.137 -0.527  1.00 19.77 ?  139 SER   B H    1 
ATOM   6088 H HA   . SER   B 1 139 ? 35.093 -29.616 -0.525  1.00 19.08 ?  139 SER   B HA   1 
ATOM   6089 H HB2  . SER   B 1 139 ? 37.237 -30.332 0.102   1.00 19.82 ?  139 SER   B HB2  1 
ATOM   6090 H HB3  . SER   B 1 139 ? 37.545 -30.698 -1.416  1.00 19.82 ?  139 SER   B HB3  1 
ATOM   6091 H HG   . SER   B 1 139 ? 38.279 -28.687 -0.919  1.00 20.04 ?  139 SER   B HG   1 
ATOM   6092 N N    . LEU   B 1 140 ? 35.409 -30.856 -3.454  1.00 14.50 ?  140 LEU   B N    1 
ATOM   6093 C CA   . LEU   B 1 140 ? 35.049 -30.615 -4.845  1.00 14.86 ?  140 LEU   B CA   1 
ATOM   6094 C C    . LEU   B 1 140 ? 33.551 -30.381 -4.985  1.00 15.06 ?  140 LEU   B C    1 
ATOM   6095 O O    . LEU   B 1 140 ? 33.124 -29.491 -5.727  1.00 14.99 ?  140 LEU   B O    1 
ATOM   6096 C CB   . LEU   B 1 140 ? 35.510 -31.783 -5.720  1.00 14.70 ?  140 LEU   B CB   1 
ATOM   6097 C CG   . LEU   B 1 140 ? 35.167 -31.678 -7.203  1.00 15.05 ?  140 LEU   B CG   1 
ATOM   6098 C CD1  . LEU   B 1 140 ? 35.721 -30.398 -7.809  1.00 15.72 ?  140 LEU   B CD1  1 
ATOM   6099 C CD2  . LEU   B 1 140 ? 35.664 -32.904 -7.944  1.00 15.98 ?  140 LEU   B CD2  1 
ATOM   6100 H H    . LEU   B 1 140 ? 35.731 -31.641 -3.299  1.00 17.43 ?  140 LEU   B H    1 
ATOM   6101 H HA   . LEU   B 1 140 ? 35.510 -29.818 -5.150  1.00 17.87 ?  140 LEU   B HA   1 
ATOM   6102 H HB2  . LEU   B 1 140 ? 36.472 -31.862 -5.650  1.00 17.67 ?  140 LEU   B HB2  1 
ATOM   6103 H HB3  . LEU   B 1 140 ? 35.093 -32.596 -5.389  1.00 17.67 ?  140 LEU   B HB3  1 
ATOM   6104 H HG   . LEU   B 1 140 ? 34.203 -31.644 -7.297  1.00 18.08 ?  140 LEU   B HG   1 
ATOM   6105 H HD11 . LEU   B 1 140 ? 35.588 -30.425 -8.770  1.00 18.89 ?  140 LEU   B HD11 1 
ATOM   6106 H HD12 . LEU   B 1 140 ? 35.246 -29.638 -7.433  1.00 18.89 ?  140 LEU   B HD12 1 
ATOM   6107 H HD13 . LEU   B 1 140 ? 36.664 -30.335 -7.606  1.00 18.89 ?  140 LEU   B HD13 1 
ATOM   6108 H HD21 . LEU   B 1 140 ? 35.432 -32.811 -8.883  1.00 19.21 ?  140 LEU   B HD21 1 
ATOM   6109 H HD22 . LEU   B 1 140 ? 36.620 -32.968 -7.839  1.00 19.21 ?  140 LEU   B HD22 1 
ATOM   6110 H HD23 . LEU   B 1 140 ? 35.227 -33.685 -7.572  1.00 19.21 ?  140 LEU   B HD23 1 
ATOM   6111 N N    . ARG   B 1 141 ? 32.744 -31.173 -4.276  1.00 14.83 ?  141 ARG   B N    1 
ATOM   6112 C CA   . ARG   B 1 141 ? 31.295 -30.990 -4.255  1.00 15.98 ?  141 ARG   B CA   1 
ATOM   6113 C C    . ARG   B 1 141 ? 30.918 -29.578 -3.825  1.00 15.95 ?  141 ARG   B C    1 
ATOM   6114 O O    . ARG   B 1 141 ? 30.119 -28.900 -4.487  1.00 16.07 ?  141 ARG   B O    1 
ATOM   6115 C CB   . ARG   B 1 141 ? 30.703 -32.019 -3.284  1.00 17.06 ?  141 ARG   B CB   1 
ATOM   6116 C CG   . ARG   B 1 141 ? 29.235 -31.904 -2.974  1.00 18.95 ?  141 ARG   B CG   1 
ATOM   6117 C CD   . ARG   B 1 141 ? 28.446 -32.542 -4.044  1.00 20.61 ?  141 ARG   B CD   1 
ATOM   6118 N NE   . ARG   B 1 141 ? 28.192 -31.634 -5.151  1.00 21.15 ?  141 ARG   B NE   1 
ATOM   6119 C CZ   . ARG   B 1 141 ? 28.179 -31.994 -6.426  1.00 20.84 ?  141 ARG   B CZ   1 
ATOM   6120 N NH1  . ARG   B 1 141 ? 28.587 -33.194 -6.811  1.00 20.53 ?  141 ARG   B NH1  1 
ATOM   6121 N NH2  . ARG   B 1 141 ? 27.733 -31.135 -7.338  1.00 21.38 ?  141 ARG   B NH2  1 
ATOM   6122 H H    . ARG   B 1 141 ? 33.017 -31.823 -3.785  1.00 17.83 ?  141 ARG   B H    1 
ATOM   6123 H HA   . ARG   B 1 141 ? 30.931 -31.146 -5.135  1.00 19.20 ?  141 ARG   B HA   1 
ATOM   6124 H HB2  . ARG   B 1 141 ? 30.855 -32.905 -3.653  1.00 20.51 ?  141 ARG   B HB2  1 
ATOM   6125 H HB3  . ARG   B 1 141 ? 31.172 -31.948 -2.441  1.00 20.51 ?  141 ARG   B HB3  1 
ATOM   6126 H HG2  . ARG   B 1 141 ? 29.047 -32.354 -2.137  1.00 22.77 ?  141 ARG   B HG2  1 
ATOM   6127 H HG3  . ARG   B 1 141 ? 28.975 -30.966 -2.912  1.00 22.77 ?  141 ARG   B HG3  1 
ATOM   6128 H HD2  . ARG   B 1 141 ? 28.926 -33.319 -4.375  1.00 24.76 ?  141 ARG   B HD2  1 
ATOM   6129 H HD3  . ARG   B 1 141 ? 27.594 -32.820 -3.680  1.00 24.76 ?  141 ARG   B HD3  1 
ATOM   6130 H HE   . ARG   B 1 141 ? 28.054 -30.805 -4.965  1.00 25.41 ?  141 ARG   B HE   1 
ATOM   6131 H HH11 . ARG   B 1 141 ? 28.865 -33.768 -6.235  1.00 24.66 ?  141 ARG   B HH11 1 
ATOM   6132 H HH12 . ARG   B 1 141 ? 28.575 -33.401 -7.644  1.00 24.66 ?  141 ARG   B HH12 1 
ATOM   6133 H HH21 . ARG   B 1 141 ? 27.475 -30.348 -7.101  1.00 25.69 ?  141 ARG   B HH21 1 
ATOM   6134 H HH22 . ARG   B 1 141 ? 27.740 -31.348 -8.172  1.00 25.69 ?  141 ARG   B HH22 1 
ATOM   6135 N N    . VAL   B 1 142 ? 31.466 -29.128 -2.696  1.00 15.73 ?  142 VAL   B N    1 
ATOM   6136 C CA   . VAL   B 1 142 ? 31.129 -27.793 -2.214  1.00 15.16 ?  142 VAL   B CA   1 
ATOM   6137 C C    . VAL   B 1 142 ? 31.602 -26.737 -3.204  1.00 14.98 ?  142 VAL   B C    1 
ATOM   6138 O O    . VAL   B 1 142 ? 30.899 -25.749 -3.465  1.00 15.61 ?  142 VAL   B O    1 
ATOM   6139 C CB   . VAL   B 1 142 ? 31.669 -27.561 -0.790  1.00 15.62 ?  142 VAL   B CB   1 
ATOM   6140 C CG1  . VAL   B 1 142 ? 31.361 -26.137 -0.323  1.00 15.74 ?  142 VAL   B CG1  1 
ATOM   6141 C CG2  . VAL   B 1 142 ? 31.069 -28.578 0.171   1.00 16.37 ?  142 VAL   B CG2  1 
ATOM   6142 H H    . VAL   B 1 142 ? 32.025 -29.562 -2.202  1.00 18.91 ?  142 VAL   B H    1 
ATOM   6143 H HA   . VAL   B 1 142 ? 30.169 -27.723 -2.162  1.00 18.22 ?  142 VAL   B HA   1 
ATOM   6144 H HB   . VAL   B 1 142 ? 32.634 -27.680 -0.787  1.00 18.77 ?  142 VAL   B HB   1 
ATOM   6145 H HG11 . VAL   B 1 142 ? 31.550 -26.070 0.626   1.00 18.91 ?  142 VAL   B HG11 1 
ATOM   6146 H HG12 . VAL   B 1 142 ? 31.921 -25.515 -0.814  1.00 18.91 ?  142 VAL   B HG12 1 
ATOM   6147 H HG13 . VAL   B 1 142 ? 30.426 -25.948 -0.489  1.00 18.91 ?  142 VAL   B HG13 1 
ATOM   6148 H HG21 . VAL   B 1 142 ? 31.384 -28.392 1.069   1.00 19.68 ?  142 VAL   B HG21 1 
ATOM   6149 H HG22 . VAL   B 1 142 ? 30.102 -28.510 0.138   1.00 19.68 ?  142 VAL   B HG22 1 
ATOM   6150 H HG23 . VAL   B 1 142 ? 31.345 -29.470 -0.097  1.00 19.68 ?  142 VAL   B HG23 1 
ATOM   6151 N N    . CYS   B 1 143 ? 32.783 -26.941 -3.791  1.00 14.74 ?  143 CYS   B N    1 
ATOM   6152 C CA   . CYS   B 1 143 ? 33.283 -26.004 -4.795  1.00 14.59 ?  143 CYS   B CA   1 
ATOM   6153 C C    . CYS   B 1 143 ? 32.287 -25.858 -5.942  1.00 14.66 ?  143 CYS   B C    1 
ATOM   6154 O O    . CYS   B 1 143 ? 31.878 -24.746 -6.301  1.00 14.84 ?  143 CYS   B O    1 
ATOM   6155 C CB   . CYS   B 1 143 ? 34.647 -26.488 -5.308  1.00 15.09 ?  143 CYS   B CB   1 
ATOM   6156 S SG   . CYS   B 1 143 ? 35.399 -25.392 -6.535  1.00 14.87 ?  143 CYS   B SG   1 
ATOM   6157 H H    . CYS   B 1 143 ? 33.315 -27.595 -3.622  1.00 17.71 ?  143 CYS   B H    1 
ATOM   6158 H HA   . CYS   B 1 143 ? 33.414 -25.130 -4.390  1.00 17.53 ?  143 CYS   B HA   1 
ATOM   6159 H HB2  . CYS   B 1 143 ? 35.269 -26.557 -4.560  1.00 18.14 ?  143 CYS   B HB2  1 
ATOM   6160 H HB3  . CYS   B 1 143 ? 34.542 -27.359 -5.714  1.00 18.14 ?  143 CYS   B HB3  1 
ATOM   6161 H HG   . CYS   B 1 143 ? 36.477 -25.825 -6.849  1.00 17.87 ?  143 CYS   B HG   1 
ATOM   6162 N N    . VAL   B 1 144 ? 31.878 -26.983 -6.526  1.00 15.25 ?  144 VAL   B N    1 
ATOM   6163 C CA   . VAL   B 1 144 ? 30.978 -26.934 -7.672  1.00 16.18 ?  144 VAL   B CA   1 
ATOM   6164 C C    . VAL   B 1 144 ? 29.638 -26.310 -7.295  1.00 16.25 ?  144 VAL   B C    1 
ATOM   6165 O O    . VAL   B 1 144 ? 29.028 -25.592 -8.097  1.00 17.25 ?  144 VAL   B O    1 
ATOM   6166 C CB   . VAL   B 1 144 ? 30.818 -28.346 -8.252  1.00 18.02 ?  144 VAL   B CB   1 
ATOM   6167 C CG1  . VAL   B 1 144 ? 29.542 -28.469 -9.081  1.00 20.10 ?  144 VAL   B CG1  1 
ATOM   6168 C CG2  . VAL   B 1 144 ? 32.057 -28.737 -9.055  1.00 18.14 ?  144 VAL   B CG2  1 
ATOM   6169 H H    . VAL   B 1 144 ? 32.107 -27.779 -6.284  1.00 18.33 ?  144 VAL   B H    1 
ATOM   6170 H HA   . VAL   B 1 144 ? 31.370 -26.376 -8.357  1.00 19.44 ?  144 VAL   B HA   1 
ATOM   6171 H HB   . VAL   B 1 144 ? 30.745 -28.974 -7.514  1.00 21.65 ?  144 VAL   B HB   1 
ATOM   6172 H HG11 . VAL   B 1 144 ? 29.615 -29.257 -9.648  1.00 24.15 ?  144 VAL   B HG11 1 
ATOM   6173 H HG12 . VAL   B 1 144 ? 28.784 -28.568 -8.484  1.00 24.15 ?  144 VAL   B HG12 1 
ATOM   6174 H HG13 . VAL   B 1 144 ? 29.441 -27.680 -9.630  1.00 24.15 ?  144 VAL   B HG13 1 
ATOM   6175 H HG21 . VAL   B 1 144 ? 31.938 -29.631 -9.403  1.00 21.79 ?  144 VAL   B HG21 1 
ATOM   6176 H HG22 . VAL   B 1 144 ? 32.163 -28.106 -9.788  1.00 21.79 ?  144 VAL   B HG22 1 
ATOM   6177 H HG23 . VAL   B 1 144 ? 32.831 -28.701 -8.475  1.00 21.79 ?  144 VAL   B HG23 1 
ATOM   6178 N N    . ASP   B 1 145 ? 29.167 -26.558 -6.076  1.00 16.11 ?  145 ASP   B N    1 
ATOM   6179 C CA   . ASP   B 1 145 ? 27.857 -26.082 -5.653  1.00 16.74 ?  145 ASP   B CA   1 
ATOM   6180 C C    . ASP   B 1 145 ? 27.883 -24.656 -5.119  1.00 16.49 ?  145 ASP   B C    1 
ATOM   6181 O O    . ASP   B 1 145 ? 26.822 -24.109 -4.795  1.00 18.13 ?  145 ASP   B O    1 
ATOM   6182 C CB   . ASP   B 1 145 ? 27.270 -26.999 -4.573  1.00 18.35 ?  145 ASP   B CB   1 
ATOM   6183 C CG   . ASP   B 1 145 ? 26.907 -28.376 -5.088  1.00 19.68 ?  145 ASP   B CG   1 
ATOM   6184 O OD1  . ASP   B 1 145 ? 26.821 -28.576 -6.317  1.00 20.13 ?  145 ASP   B OD1  1 
ATOM   6185 O OD2  . ASP   B 1 145 ? 26.702 -29.256 -4.235  1.00 21.77 -1 145 ASP   B OD2  1 
ATOM   6186 H H    . ASP   B 1 145 ? 29.595 -26.991 -5.468  1.00 19.36 ?  145 ASP   B H    1 
ATOM   6187 H HA   . ASP   B 1 145 ? 27.264 -26.087 -6.417  1.00 20.12 ?  145 ASP   B HA   1 
ATOM   6188 H HB2  . ASP   B 1 145 ? 27.914 -27.113 -3.868  1.00 22.05 ?  145 ASP   B HB2  1 
ATOM   6189 H HB3  . ASP   B 1 145 ? 26.458 -26.589 -4.226  1.00 22.05 ?  145 ASP   B HB3  1 
ATOM   6190 N N    . THR   B 1 146 ? 29.057 -24.040 -5.013  1.00 14.79 ?  146 THR   B N    1 
ATOM   6191 C CA   . THR   B 1 146 ? 29.192 -22.718 -4.409  1.00 14.41 ?  146 THR   B CA   1 
ATOM   6192 C C    . THR   B 1 146 ? 29.825 -21.690 -5.329  1.00 14.63 ?  146 THR   B C    1 
ATOM   6193 O O    . THR   B 1 146 ? 29.368 -20.529 -5.380  1.00 14.88 ?  146 THR   B O    1 
ATOM   6194 C CB   . THR   B 1 146 ? 30.017 -22.817 -3.115  1.00 14.79 ?  146 THR   B CB   1 
ATOM   6195 O OG1  . THR   B 1 146 ? 29.437 -23.795 -2.246  1.00 15.10 ?  146 THR   B OG1  1 
ATOM   6196 C CG2  . THR   B 1 146 ? 30.080 -21.472 -2.411  1.00 14.84 ?  146 THR   B CG2  1 
ATOM   6197 H H    . THR   B 1 146 ? 29.812 -24.365 -5.283  1.00 17.77 ?  146 THR   B H    1 
ATOM   6198 H HA   . THR   B 1 146 ? 28.316 -22.386 -4.171  1.00 17.32 ?  146 THR   B HA   1 
ATOM   6199 H HB   . THR   B 1 146 ? 30.924 -23.081 -3.329  1.00 17.78 ?  146 THR   B HB   1 
ATOM   6200 H HG1  . THR   B 1 146 ? 29.449 -24.556 -2.618  1.00 18.15 ?  146 THR   B HG1  1 
ATOM   6201 H HG21 . THR   B 1 146 ? 30.406 -21.582 -1.505  1.00 17.84 ?  146 THR   B HG21 1 
ATOM   6202 H HG22 . THR   B 1 146 ? 30.680 -20.872 -2.888  1.00 17.84 ?  146 THR   B HG22 1 
ATOM   6203 H HG23 . THR   B 1 146 ? 29.197 -21.070 -2.380  1.00 17.84 ?  146 THR   B HG23 1 
ATOM   6204 N N    . VAL   B 1 147 ? 30.894 -22.067 -6.026  1.00 14.13 ?  147 VAL   B N    1 
ATOM   6205 C CA   . VAL   B 1 147 ? 31.620 -21.126 -6.867  1.00 13.99 ?  147 VAL   B CA   1 
ATOM   6206 C C    . VAL   B 1 147 ? 30.886 -20.996 -8.189  1.00 14.00 ?  147 VAL   B C    1 
ATOM   6207 O O    . VAL   B 1 147 ? 30.511 -22.000 -8.809  1.00 14.97 ?  147 VAL   B O    1 
ATOM   6208 C CB   . VAL   B 1 147 ? 33.071 -21.586 -7.071  1.00 14.05 ?  147 VAL   B CB   1 
ATOM   6209 C CG1  . VAL   B 1 147 ? 33.837 -20.567 -7.906  1.00 14.03 ?  147 VAL   B CG1  1 
ATOM   6210 C CG2  . VAL   B 1 147 ? 33.746 -21.793 -5.725  1.00 14.22 ?  147 VAL   B CG2  1 
ATOM   6211 H H    . VAL   B 1 147 ? 31.218 -22.867 -6.033  1.00 16.99 ?  147 VAL   B H    1 
ATOM   6212 H HA   . VAL   B 1 147 ? 31.638 -20.257 -6.438  1.00 16.82 ?  147 VAL   B HA   1 
ATOM   6213 H HB   . VAL   B 1 147 ? 33.077 -22.434 -7.548  1.00 16.89 ?  147 VAL   B HB   1 
ATOM   6214 H HG11 . VAL   B 1 147 ? 34.781 -20.792 -7.896  1.00 16.86 ?  147 VAL   B HG11 1 
ATOM   6215 H HG12 . VAL   B 1 147 ? 33.504 -20.581 -8.817  1.00 16.86 ?  147 VAL   B HG12 1 
ATOM   6216 H HG13 . VAL   B 1 147 ? 33.707 -19.684 -7.520  1.00 16.86 ?  147 VAL   B HG13 1 
ATOM   6217 H HG21 . VAL   B 1 147 ? 34.688 -21.980 -5.868  1.00 17.09 ?  147 VAL   B HG21 1 
ATOM   6218 H HG22 . VAL   B 1 147 ? 33.647 -20.985 -5.197  1.00 17.09 ?  147 VAL   B HG22 1 
ATOM   6219 H HG23 . VAL   B 1 147 ? 33.327 -22.539 -5.270  1.00 17.09 ?  147 VAL   B HG23 1 
ATOM   6220 N N    . ARG   B 1 148 ? 30.679 -19.749 -8.617  1.00 13.81 ?  148 ARG   B N    1 
ATOM   6221 C CA   . ARG   B 1 148 ? 30.053 -19.439 -9.893  1.00 14.30 ?  148 ARG   B CA   1 
ATOM   6222 C C    . ARG   B 1 148 ? 31.012 -18.769 -10.864 1.00 13.95 ?  148 ARG   B C    1 
ATOM   6223 O O    . ARG   B 1 148 ? 30.735 -18.752 -12.065 1.00 15.71 ?  148 ARG   B O    1 
ATOM   6224 C CB   . ARG   B 1 148 ? 28.820 -18.545 -9.681  1.00 14.40 ?  148 ARG   B CB   1 
ATOM   6225 C CG   . ARG   B 1 148 ? 27.739 -19.243 -8.868  1.00 15.08 ?  148 ARG   B CG   1 
ATOM   6226 C CD   . ARG   B 1 148 ? 26.539 -18.346 -8.575  1.00 16.17 ?  148 ARG   B CD   1 
ATOM   6227 N NE   . ARG   B 1 148 ? 26.930 -17.150 -7.840  1.00 16.40 ?  148 ARG   B NE   1 
ATOM   6228 C CZ   . ARG   B 1 148 ? 27.216 -17.114 -6.545  1.00 15.16 ?  148 ARG   B CZ   1 
ATOM   6229 N NH1  . ARG   B 1 148 ? 27.141 -18.194 -5.785  1.00 15.24 ?  148 ARG   B NH1  1 
ATOM   6230 N NH2  . ARG   B 1 148 ? 27.618 -15.970 -6.003  1.00 15.10 ?  148 ARG   B NH2  1 
ATOM   6231 H H    . ARG   B 1 148 ? 30.910 -19.042 -8.172  1.00 16.61 ?  148 ARG   B H    1 
ATOM   6232 H HA   . ARG   B 1 148 ? 29.756 -20.264 -10.299 1.00 17.19 ?  148 ARG   B HA   1 
ATOM   6233 H HB2  . ARG   B 1 148 ? 29.087 -17.744 -9.203  1.00 17.30 ?  148 ARG   B HB2  1 
ATOM   6234 H HB3  . ARG   B 1 148 ? 28.448 -18.311 -10.545 1.00 17.30 ?  148 ARG   B HB3  1 
ATOM   6235 H HG2  . ARG   B 1 148 ? 27.423 -20.016 -9.367  1.00 18.13 ?  148 ARG   B HG2  1 
ATOM   6236 H HG3  . ARG   B 1 148 ? 28.117 -19.531 -8.022  1.00 18.13 ?  148 ARG   B HG3  1 
ATOM   6237 H HD2  . ARG   B 1 148 ? 26.139 -18.067 -9.412  1.00 19.44 ?  148 ARG   B HD2  1 
ATOM   6238 H HD3  . ARG   B 1 148 ? 25.898 -18.836 -8.040  1.00 19.44 ?  148 ARG   B HD3  1 
ATOM   6239 H HE   . ARG   B 1 148 ? 26.990 -16.413 -8.277  1.00 19.71 ?  148 ARG   B HE   1 
ATOM   6240 H HH11 . ARG   B 1 148 ? 26.882 -18.945 -6.119  1.00 18.31 ?  148 ARG   B HH11 1 
ATOM   6241 H HH12 . ARG   B 1 148 ? 27.327 -18.147 -4.944  1.00 18.31 ?  148 ARG   B HH12 1 
ATOM   6242 H HH21 . ARG   B 1 148 ? 27.678 -15.262 -6.484  1.00 18.15 ?  148 ARG   B HH21 1 
ATOM   6243 H HH22 . ARG   B 1 148 ? 27.806 -15.933 -5.161  1.00 18.15 ?  148 ARG   B HH22 1 
ATOM   6244 N N    . THR   B 1 149 ? 32.119 -18.217 -10.375 1.00 14.13 ?  149 THR   B N    1 
ATOM   6245 C CA   . THR   B 1 149 ? 33.159 -17.660 -11.222 1.00 14.25 ?  149 THR   B CA   1 
ATOM   6246 C C    . THR   B 1 149 ? 34.043 -18.803 -11.729 1.00 14.10 ?  149 THR   B C    1 
ATOM   6247 O O    . THR   B 1 149 ? 33.850 -19.970 -11.382 1.00 14.12 ?  149 THR   B O    1 
ATOM   6248 C CB   . THR   B 1 149 ? 33.932 -16.604 -10.438 1.00 14.55 ?  149 THR   B CB   1 
ATOM   6249 O OG1  . THR   B 1 149 ? 34.393 -17.204 -9.225  1.00 14.54 ?  149 THR   B OG1  1 
ATOM   6250 C CG2  . THR   B 1 149 ? 33.039 -15.391 -10.137 1.00 15.31 ?  149 THR   B CG2  1 
ATOM   6251 H H    . THR   B 1 149 ? 32.283 -18.143 -9.537  1.00 16.99 ?  149 THR   B H    1 
ATOM   6252 H HA   . THR   B 1 149 ? 32.753 -17.225 -11.990 1.00 17.13 ?  149 THR   B HA   1 
ATOM   6253 H HB   . THR   B 1 149 ? 34.692 -16.311 -10.960 1.00 17.49 ?  149 THR   B HB   1 
ATOM   6254 H HG1  . THR   B 1 149 ? 34.821 -16.639 -8.769  1.00 17.48 ?  149 THR   B HG1  1 
ATOM   6255 H HG21 . THR   B 1 149 ? 33.542 -14.722 -9.647  1.00 18.40 ?  149 THR   B HG21 1 
ATOM   6256 H HG22 . THR   B 1 149 ? 32.718 -15.000 -10.965 1.00 18.40 ?  149 THR   B HG22 1 
ATOM   6257 H HG23 . THR   B 1 149 ? 32.275 -15.662 -9.601  1.00 18.40 ?  149 THR   B HG23 1 
ATOM   6258 N N    . ASN   B 1 150 ? 35.012 -18.488 -12.577 1.00 13.93 ?  150 ASN   B N    1 
ATOM   6259 C CA   . ASN   B 1 150 ? 35.779 -19.520 -13.270 1.00 14.29 ?  150 ASN   B CA   1 
ATOM   6260 C C    . ASN   B 1 150 ? 36.945 -19.962 -12.395 1.00 14.01 ?  150 ASN   B C    1 
ATOM   6261 O O    . ASN   B 1 150 ? 37.876 -19.189 -12.143 1.00 14.78 ?  150 ASN   B O    1 
ATOM   6262 C CB   . ASN   B 1 150 ? 36.254 -18.997 -14.620 1.00 15.92 ?  150 ASN   B CB   1 
ATOM   6263 C CG   . ASN   B 1 150 ? 35.109 -18.772 -15.569 1.00 18.54 ?  150 ASN   B CG   1 
ATOM   6264 O OD1  . ASN   B 1 150 ? 34.219 -19.607 -15.671 1.00 19.72 ?  150 ASN   B OD1  1 
ATOM   6265 N ND2  . ASN   B 1 150 ? 35.098 -17.630 -16.239 1.00 20.05 ?  150 ASN   B ND2  1 
ATOM   6266 H H    . ASN   B 1 150 ? 35.254 -17.684 -12.770 1.00 16.74 ?  150 ASN   B H    1 
ATOM   6267 H HA   . ASN   B 1 150 ? 35.205 -20.291 -13.432 1.00 17.18 ?  150 ASN   B HA   1 
ATOM   6268 H HB2  . ASN   B 1 150 ? 36.708 -18.151 -14.492 1.00 19.13 ?  150 ASN   B HB2  1 
ATOM   6269 H HB3  . ASN   B 1 150 ? 36.854 -19.644 -15.023 1.00 19.13 ?  150 ASN   B HB3  1 
ATOM   6270 H HD21 . ASN   B 1 150 ? 34.462 -17.456 -16.793 1.00 24.09 ?  150 ASN   B HD21 1 
ATOM   6271 H HD22 . ASN   B 1 150 ? 35.737 -17.062 -16.131 1.00 24.09 ?  150 ASN   B HD22 1 
ATOM   6272 N N    . VAL   B 1 151 ? 36.905 -21.210 -11.937 1.00 13.63 ?  151 VAL   B N    1 
ATOM   6273 C CA   . VAL   B 1 151 ? 37.923 -21.734 -11.041 1.00 13.93 ?  151 VAL   B CA   1 
ATOM   6274 C C    . VAL   B 1 151 ? 38.630 -22.906 -11.710 1.00 13.53 ?  151 VAL   B C    1 
ATOM   6275 O O    . VAL   B 1 151 ? 37.987 -23.850 -12.202 1.00 14.63 ?  151 VAL   B O    1 
ATOM   6276 C CB   . VAL   B 1 151 ? 37.358 -22.066 -9.644  1.00 15.25 ?  151 VAL   B CB   1 
ATOM   6277 C CG1  . VAL   B 1 151 ? 36.210 -23.071 -9.717  1.00 16.31 ?  151 VAL   B CG1  1 
ATOM   6278 C CG2  . VAL   B 1 151 ? 38.471 -22.529 -8.710  1.00 15.38 ?  151 VAL   B CG2  1 
ATOM   6279 H H    . VAL   B 1 151 ? 36.283 -21.778 -12.135 1.00 16.38 ?  151 VAL   B H    1 
ATOM   6280 H HA   . VAL   B 1 151 ? 38.586 -21.038 -10.911 1.00 16.74 ?  151 VAL   B HA   1 
ATOM   6281 H HB   . VAL   B 1 151 ? 36.992 -21.248 -9.266  1.00 18.33 ?  151 VAL   B HB   1 
ATOM   6282 H HG11 . VAL   B 1 151 ? 35.884 -23.249 -8.818  1.00 19.60 ?  151 VAL   B HG11 1 
ATOM   6283 H HG12 . VAL   B 1 151 ? 35.492 -22.701 -10.256 1.00 19.60 ?  151 VAL   B HG12 1 
ATOM   6284 H HG13 . VAL   B 1 151 ? 36.531 -23.895 -10.117 1.00 19.60 ?  151 VAL   B HG13 1 
ATOM   6285 H HG21 . VAL   B 1 151 ? 38.109 -22.617 -7.813  1.00 18.48 ?  151 VAL   B HG21 1 
ATOM   6286 H HG22 . VAL   B 1 151 ? 38.806 -23.383 -9.017  1.00 18.48 ?  151 VAL   B HG22 1 
ATOM   6287 H HG23 . VAL   B 1 151 ? 39.181 -21.868 -8.714  1.00 18.48 ?  151 VAL   B HG23 1 
ATOM   6288 N N    . TYR   B 1 152 ? 39.961 -22.818 -11.732 1.00 13.32 ?  152 TYR   B N    1 
ATOM   6289 C CA   . TYR   B 1 152 ? 40.865 -23.805 -12.304 1.00 13.56 ?  152 TYR   B CA   1 
ATOM   6290 C C    . TYR   B 1 152 ? 41.580 -24.471 -11.135 1.00 12.79 ?  152 TYR   B C    1 
ATOM   6291 O O    . TYR   B 1 152 ? 42.427 -23.850 -10.486 1.00 13.33 ?  152 TYR   B O    1 
ATOM   6292 C CB   . TYR   B 1 152 ? 41.838 -23.106 -13.256 1.00 14.00 ?  152 TYR   B CB   1 
ATOM   6293 C CG   . TYR   B 1 152 ? 41.152 -22.636 -14.520 1.00 14.85 ?  152 TYR   B CG   1 
ATOM   6294 C CD1  . TYR   B 1 152 ? 40.482 -21.418 -14.576 1.00 15.23 ?  152 TYR   B CD1  1 
ATOM   6295 C CD2  . TYR   B 1 152 ? 41.152 -23.434 -15.653 1.00 15.49 ?  152 TYR   B CD2  1 
ATOM   6296 C CE1  . TYR   B 1 152 ? 39.838 -21.012 -15.729 1.00 16.57 ?  152 TYR   B CE1  1 
ATOM   6297 C CE2  . TYR   B 1 152 ? 40.512 -23.041 -16.806 1.00 16.52 ?  152 TYR   B CE2  1 
ATOM   6298 C CZ   . TYR   B 1 152 ? 39.858 -21.827 -16.845 1.00 16.76 ?  152 TYR   B CZ   1 
ATOM   6299 O OH   . TYR   B 1 152 ? 39.229 -21.450 -18.005 1.00 19.36 ?  152 TYR   B OH   1 
ATOM   6300 H H    . TYR   B 1 152 ? 40.389 -22.152 -11.387 1.00 16.01 ?  152 TYR   B H    1 
ATOM   6301 H HA   . TYR   B 1 152 ? 40.357 -24.476 -12.792 1.00 16.30 ?  152 TYR   B HA   1 
ATOM   6302 H HB2  . TYR   B 1 152 ? 42.212 -22.333 -12.805 1.00 16.83 ?  152 TYR   B HB2  1 
ATOM   6303 H HB3  . TYR   B 1 152 ? 42.541 -23.724 -13.500 1.00 16.83 ?  152 TYR   B HB3  1 
ATOM   6304 H HD1  . TYR   B 1 152 ? 40.460 -20.868 -13.822 1.00 18.31 ?  152 TYR   B HD1  1 
ATOM   6305 H HD2  . TYR   B 1 152 ? 41.589 -24.256 -15.630 1.00 18.62 ?  152 TYR   B HD2  1 
ATOM   6306 H HE1  . TYR   B 1 152 ? 39.398 -20.192 -15.758 1.00 19.91 ?  152 TYR   B HE1  1 
ATOM   6307 H HE2  . TYR   B 1 152 ? 40.532 -23.583 -17.559 1.00 19.85 ?  152 TYR   B HE2  1 
ATOM   6308 H HH   . TYR   B 1 152 ? 38.875 -20.691 -17.904 1.00 23.26 ?  152 TYR   B HH   1 
ATOM   6309 N N    . LEU   B 1 153 ? 41.214 -25.724 -10.859 1.00 12.78 ?  153 LEU   B N    1 
ATOM   6310 C CA   . LEU   B 1 153 ? 41.724 -26.470 -9.719  1.00 12.97 ?  153 LEU   B CA   1 
ATOM   6311 C C    . LEU   B 1 153 ? 42.955 -27.274 -10.115 1.00 13.47 ?  153 LEU   B C    1 
ATOM   6312 O O    . LEU   B 1 153 ? 42.938 -28.003 -11.111 1.00 14.42 ?  153 LEU   B O    1 
ATOM   6313 C CB   . LEU   B 1 153 ? 40.645 -27.424 -9.195  1.00 13.09 ?  153 LEU   B CB   1 
ATOM   6314 C CG   . LEU   B 1 153 ? 39.386 -26.769 -8.631  1.00 14.47 ?  153 LEU   B CG   1 
ATOM   6315 C CD1  . LEU   B 1 153 ? 38.285 -27.813 -8.465  1.00 15.21 ?  153 LEU   B CD1  1 
ATOM   6316 C CD2  . LEU   B 1 153 ? 39.683 -26.092 -7.302  1.00 15.23 ?  153 LEU   B CD2  1 
ATOM   6317 H H    . LEU   B 1 153 ? 40.645 -26.173 -11.331 1.00 15.37 ?  153 LEU   B H    1 
ATOM   6318 H HA   . LEU   B 1 153 ? 41.957 -25.853 -9.010  1.00 15.59 ?  153 LEU   B HA   1 
ATOM   6319 H HB2  . LEU   B 1 153 ? 40.366 -28.005 -9.918  1.00 15.74 ?  153 LEU   B HB2  1 
ATOM   6320 H HB3  . LEU   B 1 153 ? 41.030 -27.962 -8.481  1.00 15.74 ?  153 LEU   B HB3  1 
ATOM   6321 H HG   . LEU   B 1 153 ? 39.068 -26.091 -9.249  1.00 17.39 ?  153 LEU   B HG   1 
ATOM   6322 H HD11 . LEU   B 1 153 ? 37.479 -27.372 -8.148  1.00 18.28 ?  153 LEU   B HD11 1 
ATOM   6323 H HD12 . LEU   B 1 153 ? 38.119 -28.229 -9.321  1.00 18.28 ?  153 LEU   B HD12 1 
ATOM   6324 H HD13 . LEU   B 1 153 ? 38.576 -28.473 -7.819  1.00 18.28 ?  153 LEU   B HD13 1 
ATOM   6325 H HD21 . LEU   B 1 153 ? 38.867 -25.714 -6.940  1.00 18.31 ?  153 LEU   B HD21 1 
ATOM   6326 H HD22 . LEU   B 1 153 ? 40.048 -26.745 -6.685  1.00 18.31 ?  153 LEU   B HD22 1 
ATOM   6327 H HD23 . LEU   B 1 153 ? 40.335 -25.381 -7.447  1.00 18.31 ?  153 LEU   B HD23 1 
ATOM   6328 N N    . ALA   B 1 154 ? 44.008 -27.160 -9.311  1.00 13.41 ?  154 ALA   B N    1 
ATOM   6329 C CA   . ALA   B 1 154 ? 45.237 -27.925 -9.488  1.00 14.55 ?  154 ALA   B CA   1 
ATOM   6330 C C    . ALA   B 1 154 ? 45.300 -28.996 -8.409  1.00 15.04 ?  154 ALA   B C    1 
ATOM   6331 O O    . ALA   B 1 154 ? 45.229 -28.689 -7.213  1.00 16.31 ?  154 ALA   B O    1 
ATOM   6332 C CB   . ALA   B 1 154 ? 46.460 -27.014 -9.424  1.00 15.45 ?  154 ALA   B CB   1 
ATOM   6333 H H    . ALA   B 1 154 ? 44.030 -26.628 -8.633  1.00 16.12 ?  154 ALA   B H    1 
ATOM   6334 H HA   . ALA   B 1 154 ? 45.224 -28.357 -10.355 1.00 17.49 ?  154 ALA   B HA   1 
ATOM   6335 H HB1  . ALA   B 1 154 ? 47.261 -27.547 -9.545  1.00 18.57 ?  154 ALA   B HB1  1 
ATOM   6336 H HB2  . ALA   B 1 154 ? 46.399 -26.346 -10.129 1.00 18.57 ?  154 ALA   B HB2  1 
ATOM   6337 H HB3  . ALA   B 1 154 ? 46.485 -26.573 -8.558  1.00 18.57 ?  154 ALA   B HB3  1 
ATOM   6338 N N    . VAL   B 1 155 ? 45.416 -30.248 -8.836  1.00 14.29 ?  155 VAL   B N    1 
ATOM   6339 C CA   . VAL   B 1 155 ? 45.522 -31.395 -7.941  1.00 14.94 ?  155 VAL   B CA   1 
ATOM   6340 C C    . VAL   B 1 155 ? 46.858 -32.070 -8.218  1.00 14.81 ?  155 VAL   B C    1 
ATOM   6341 O O    . VAL   B 1 155 ? 47.090 -32.568 -9.327  1.00 16.67 ?  155 VAL   B O    1 
ATOM   6342 C CB   . VAL   B 1 155 ? 44.363 -32.383 -8.138  1.00 16.19 ?  155 VAL   B CB   1 
ATOM   6343 C CG1  . VAL   B 1 155 ? 44.552 -33.582 -7.228  1.00 16.49 ?  155 VAL   B CG1  1 
ATOM   6344 C CG2  . VAL   B 1 155 ? 43.032 -31.687 -7.873  1.00 17.10 ?  155 VAL   B CG2  1 
ATOM   6345 H H    . VAL   B 1 155 ? 45.446 -30.466 -9.672  1.00 17.18 ?  155 VAL   B H    1 
ATOM   6346 H HA   . VAL   B 1 155 ? 45.514 -31.090 -7.023  1.00 17.96 ?  155 VAL   B HA   1 
ATOM   6347 H HB   . VAL   B 1 155 ? 44.360 -32.691 -9.058  1.00 19.45 ?  155 VAL   B HB   1 
ATOM   6348 H HG11 . VAL   B 1 155 ? 43.719 -34.075 -7.179  1.00 19.81 ?  155 VAL   B HG11 1 
ATOM   6349 H HG12 . VAL   B 1 155 ? 45.250 -34.151 -7.592  1.00 19.81 ?  155 VAL   B HG12 1 
ATOM   6350 H HG13 . VAL   B 1 155 ? 44.804 -33.273 -6.344  1.00 19.81 ?  155 VAL   B HG13 1 
ATOM   6351 H HG21 . VAL   B 1 155 ? 42.319 -32.338 -7.959  1.00 20.55 ?  155 VAL   B HG21 1 
ATOM   6352 H HG22 . VAL   B 1 155 ? 43.044 -31.324 -6.974  1.00 20.55 ?  155 VAL   B HG22 1 
ATOM   6353 H HG23 . VAL   B 1 155 ? 42.913 -30.975 -8.519  1.00 20.55 ?  155 VAL   B HG23 1 
ATOM   6354 N N    . PHE   B 1 156 ? 47.725 -32.107 -7.204  1.00 15.08 ?  156 PHE   B N    1 
ATOM   6355 C CA   . PHE   B 1 156 ? 49.100 -32.569 -7.404  1.00 16.12 ?  156 PHE   B CA   1 
ATOM   6356 C C    . PHE   B 1 156 ? 49.190 -34.072 -7.676  1.00 17.29 ?  156 PHE   B C    1 
ATOM   6357 O O    . PHE   B 1 156 ? 49.909 -34.510 -8.585  1.00 19.12 ?  156 PHE   B O    1 
ATOM   6358 C CB   . PHE   B 1 156 ? 49.936 -32.196 -6.181  1.00 16.60 ?  156 PHE   B CB   1 
ATOM   6359 C CG   . PHE   B 1 156 ? 51.363 -32.659 -6.246  1.00 17.21 ?  156 PHE   B CG   1 
ATOM   6360 C CD1  . PHE   B 1 156 ? 52.242 -32.122 -7.170  1.00 18.39 ?  156 PHE   B CD1  1 
ATOM   6361 C CD2  . PHE   B 1 156 ? 51.834 -33.607 -5.360  1.00 17.80 ?  156 PHE   B CD2  1 
ATOM   6362 C CE1  . PHE   B 1 156 ? 53.567 -32.530 -7.219  1.00 19.26 ?  156 PHE   B CE1  1 
ATOM   6363 C CE2  . PHE   B 1 156 ? 53.155 -34.024 -5.407  1.00 19.18 ?  156 PHE   B CE2  1 
ATOM   6364 C CZ   . PHE   B 1 156 ? 54.014 -33.483 -6.339  1.00 19.27 ?  156 PHE   B CZ   1 
ATOM   6365 H H    . PHE   B 1 156 ? 47.538 -31.877 -6.397  1.00 18.12 ?  156 PHE   B H    1 
ATOM   6366 H HA   . PHE   B 1 156 ? 49.469 -32.107 -8.168  1.00 19.37 ?  156 PHE   B HA   1 
ATOM   6367 H HB2  . PHE   B 1 156 ? 49.943 -31.231 -6.095  1.00 19.95 ?  156 PHE   B HB2  1 
ATOM   6368 H HB3  . PHE   B 1 156 ? 49.535 -32.595 -5.394  1.00 19.95 ?  156 PHE   B HB3  1 
ATOM   6369 H HD1  . PHE   B 1 156 ? 51.943 -31.472 -7.770  1.00 22.10 ?  156 PHE   B HD1  1 
ATOM   6370 H HD2  . PHE   B 1 156 ? 51.254 -33.977 -4.734  1.00 21.38 ?  156 PHE   B HD2  1 
ATOM   6371 H HE1  . PHE   B 1 156 ? 54.147 -32.165 -7.851  1.00 23.14 ?  156 PHE   B HE1  1 
ATOM   6372 H HE2  . PHE   B 1 156 ? 53.458 -34.674 -4.811  1.00 23.05 ?  156 PHE   B HE2  1 
ATOM   6373 H HZ   . PHE   B 1 156 ? 54.902 -33.767 -6.371  1.00 23.15 ?  156 PHE   B HZ   1 
ATOM   6374 N N    . ASP   B 1 157 ? 48.532 -34.885 -6.860  1.00 17.36 ?  157 ASP   B N    1 
ATOM   6375 C CA   . ASP   B 1 157 ? 48.676 -36.335 -6.950  1.00 18.70 ?  157 ASP   B CA   1 
ATOM   6376 C C    . ASP   B 1 157 ? 47.765 -36.884 -8.041  1.00 18.96 ?  157 ASP   B C    1 
ATOM   6377 O O    . ASP   B 1 157 ? 46.538 -36.767 -7.946  1.00 18.67 ?  157 ASP   B O    1 
ATOM   6378 C CB   . ASP   B 1 157 ? 48.305 -36.944 -5.604  1.00 19.83 ?  157 ASP   B CB   1 
ATOM   6379 C CG   . ASP   B 1 157 ? 48.454 -38.455 -5.581  1.00 21.82 ?  157 ASP   B CG   1 
ATOM   6380 O OD1  . ASP   B 1 157 ? 48.785 -39.065 -6.626  1.00 22.44 ?  157 ASP   B OD1  1 
ATOM   6381 O OD2  . ASP   B 1 157 ? 48.252 -39.028 -4.494  1.00 23.79 -1 157 ASP   B OD2  1 
ATOM   6382 H H    . ASP   B 1 157 ? 48.004 -34.621 -6.238  1.00 20.86 ?  157 ASP   B H    1 
ATOM   6383 H HA   . ASP   B 1 157 ? 49.594 -36.568 -7.157  1.00 22.47 ?  157 ASP   B HA   1 
ATOM   6384 H HB2  . ASP   B 1 157 ? 48.874 -36.567 -4.920  1.00 23.82 ?  157 ASP   B HB2  1 
ATOM   6385 H HB3  . ASP   B 1 157 ? 47.374 -36.736 -5.411  1.00 23.82 ?  157 ASP   B HB3  1 
ATOM   6386 N N    . LYS   B 1 158 ? 48.362 -37.512 -9.062  1.00 20.07 ?  158 LYS   B N    1 
ATOM   6387 C CA   . LYS   B 1 158 ? 47.589 -38.134 -10.141 1.00 21.26 ?  158 LYS   B CA   1 
ATOM   6388 C C    . LYS   B 1 158 ? 46.524 -39.094 -9.609  1.00 20.88 ?  158 LYS   B C    1 
ATOM   6389 O O    . LYS   B 1 158 ? 45.418 -39.181 -10.162 1.00 21.03 ?  158 LYS   B O    1 
ATOM   6390 C CB   . LYS   B 1 158 ? 48.542 -38.870 -11.095 1.00 23.25 ?  158 LYS   B CB   1 
ATOM   6391 C CG   . LYS   B 1 158 ? 47.864 -39.770 -12.120 1.00 25.41 ?  158 LYS   B CG   1 
ATOM   6392 C CD   . LYS   B 1 158 ? 47.014 -38.986 -13.101 1.00 27.41 ?  158 LYS   B CD   1 
ATOM   6393 C CE   . LYS   B 1 158 ? 46.424 -39.901 -14.162 1.00 29.04 ?  158 LYS   B CE   1 
ATOM   6394 N NZ   . LYS   B 1 158 ? 45.378 -39.220 -14.977 1.00 29.23 ?  158 LYS   B NZ   1 
ATOM   6395 H H    . LYS   B 1 158 ? 49.218 -37.596 -9.151  1.00 24.11 ?  158 LYS   B H    1 
ATOM   6396 H HA   . LYS   B 1 158 ? 47.145 -37.440 -10.651 1.00 25.55 ?  158 LYS   B HA   1 
ATOM   6397 H HB2  . LYS   B 1 158 ? 49.061 -38.209 -11.588 1.00 27.93 ?  158 LYS   B HB2  1 
ATOM   6398 H HB3  . LYS   B 1 158 ? 49.144 -39.422 -10.571 1.00 27.93 ?  158 LYS   B HB3  1 
ATOM   6399 H HG2  . LYS   B 1 158 ? 48.549 -40.235 -12.627 1.00 30.52 ?  158 LYS   B HG2  1 
ATOM   6400 H HG3  . LYS   B 1 158 ? 47.299 -40.419 -11.671 1.00 30.52 ?  158 LYS   B HG3  1 
ATOM   6401 H HD2  . LYS   B 1 158 ? 46.286 -38.557 -12.626 1.00 32.92 ?  158 LYS   B HD2  1 
ATOM   6402 H HD3  . LYS   B 1 158 ? 47.566 -38.322 -13.545 1.00 32.92 ?  158 LYS   B HD3  1 
ATOM   6403 H HE2  . LYS   B 1 158 ? 47.128 -40.192 -14.760 1.00 34.88 ?  158 LYS   B HE2  1 
ATOM   6404 H HE3  . LYS   B 1 158 ? 46.016 -40.668 -13.730 1.00 34.88 ?  158 LYS   B HE3  1 
ATOM   6405 H HZ1  . LYS   B 1 158 ? 45.053 -39.781 -15.586 1.00 35.10 ?  158 LYS   B HZ1  1 
ATOM   6406 H HZ2  . LYS   B 1 158 ? 44.714 -38.945 -14.452 1.00 35.10 ?  158 LYS   B HZ2  1 
ATOM   6407 H HZ3  . LYS   B 1 158 ? 45.729 -38.514 -15.392 1.00 35.10 ?  158 LYS   B HZ3  1 
ATOM   6408 N N    . ASN   B 1 159 ? 46.841 -39.844 -8.553  1.00 21.29 ?  159 ASN   B N    1 
ATOM   6409 C CA   . ASN   B 1 159 ? 45.883 -40.821 -8.042  1.00 21.82 ?  159 ASN   B CA   1 
ATOM   6410 C C    . ASN   B 1 159 ? 44.685 -40.143 -7.376  1.00 20.79 ?  159 ASN   B C    1 
ATOM   6411 O O    . ASN   B 1 159 ? 43.549 -40.631 -7.482  1.00 21.26 ?  159 ASN   B O    1 
ATOM   6412 C CB   . ASN   B 1 159 ? 46.592 -41.783 -7.096  1.00 23.72 ?  159 ASN   B CB   1 
ATOM   6413 C CG   . ASN   B 1 159 ? 47.623 -42.627 -7.806  1.00 25.57 ?  159 ASN   B CG   1 
ATOM   6414 O OD1  . ASN   B 1 159 ? 47.384 -43.111 -8.921  1.00 26.30 ?  159 ASN   B OD1  1 
ATOM   6415 N ND2  . ASN   B 1 159 ? 48.780 -42.812 -7.170  1.00 26.20 ?  159 ASN   B ND2  1 
ATOM   6416 H H    . ASN   B 1 159 ? 47.589 -39.805 -8.135  1.00 25.58 ?  159 ASN   B H    1 
ATOM   6417 H HA   . ASN   B 1 159 ? 45.553 -41.339 -8.794  1.00 26.21 ?  159 ASN   B HA   1 
ATOM   6418 H HB2  . ASN   B 1 159 ? 47.043 -41.280 -6.404  1.00 28.49 ?  159 ASN   B HB2  1 
ATOM   6419 H HB3  . ASN   B 1 159 ? 45.943 -42.385 -6.713  1.00 28.49 ?  159 ASN   B HB3  1 
ATOM   6420 H HD21 . ASN   B 1 159 ? 49.411 -43.283 -7.529  1.00 31.46 ?  159 ASN   B HD21 1 
ATOM   6421 H HD22 . ASN   B 1 159 ? 48.905 -42.474 -6.386  1.00 31.46 ?  159 ASN   B HD22 1 
ATOM   6422 N N    . LEU   B 1 160 ? 44.903 -39.014 -6.694  1.00 19.68 ?  160 LEU   B N    1 
ATOM   6423 C CA   . LEU   B 1 160 ? 43.769 -38.270 -6.160  1.00 18.74 ?  160 LEU   B CA   1 
ATOM   6424 C C    . LEU   B 1 160 ? 42.985 -37.611 -7.282  1.00 18.20 ?  160 LEU   B C    1 
ATOM   6425 O O    . LEU   B 1 160 ? 41.748 -37.601 -7.263  1.00 18.08 ?  160 LEU   B O    1 
ATOM   6426 C CB   . LEU   B 1 160 ? 44.239 -37.225 -5.149  1.00 18.32 ?  160 LEU   B CB   1 
ATOM   6427 C CG   . LEU   B 1 160 ? 43.110 -36.331 -4.616  1.00 18.25 ?  160 LEU   B CG   1 
ATOM   6428 C CD1  . LEU   B 1 160 ? 41.992 -37.167 -4.007  1.00 19.13 ?  160 LEU   B CD1  1 
ATOM   6429 C CD2  . LEU   B 1 160 ? 43.650 -35.333 -3.607  1.00 18.45 ?  160 LEU   B CD2  1 
ATOM   6430 H H    . LEU   B 1 160 ? 45.679 -38.670 -6.541  1.00 23.65 ?  160 LEU   B H    1 
ATOM   6431 H HA   . LEU   B 1 160 ? 43.183 -38.892 -5.709  1.00 22.52 ?  160 LEU   B HA   1 
ATOM   6432 H HB2  . LEU   B 1 160 ? 44.646 -37.684 -4.395  1.00 22.01 ?  160 LEU   B HB2  1 
ATOM   6433 H HB3  . LEU   B 1 160 ? 44.901 -36.653 -5.575  1.00 22.01 ?  160 LEU   B HB3  1 
ATOM   6434 H HG   . LEU   B 1 160 ? 42.738 -35.832 -5.355  1.00 21.93 ?  160 LEU   B HG   1 
ATOM   6435 H HD11 . LEU   B 1 160 ? 41.374 -36.578 -3.554  1.00 22.99 ?  160 LEU   B HD11 1 
ATOM   6436 H HD12 . LEU   B 1 160 ? 41.532 -37.652 -4.712  1.00 22.99 ?  160 LEU   B HD12 1 
ATOM   6437 H HD13 . LEU   B 1 160 ? 42.375 -37.797 -3.372  1.00 22.99 ?  160 LEU   B HD13 1 
ATOM   6438 H HD21 . LEU   B 1 160 ? 42.922 -34.770 -3.310  1.00 22.17 ?  160 LEU   B HD21 1 
ATOM   6439 H HD22 . LEU   B 1 160 ? 44.027 -35.817 -2.855  1.00 22.17 ?  160 LEU   B HD22 1 
ATOM   6440 H HD23 . LEU   B 1 160 ? 44.337 -34.797 -4.033  1.00 22.17 ?  160 LEU   B HD23 1 
ATOM   6441 N N    . TYR   B 1 161 ? 43.689 -37.040 -8.263  1.00 18.46 ?  161 TYR   B N    1 
ATOM   6442 C CA   . TYR   B 1 161 ? 43.022 -36.474 -9.430  1.00 18.16 ?  161 TYR   B CA   1 
ATOM   6443 C C    . TYR   B 1 161 ? 42.076 -37.495 -10.054 1.00 18.28 ?  161 TYR   B C    1 
ATOM   6444 O O    . TYR   B 1 161 ? 40.903 -37.201 -10.308 1.00 18.20 ?  161 TYR   B O    1 
ATOM   6445 C CB   . TYR   B 1 161 ? 44.072 -35.999 -10.443 1.00 18.63 ?  161 TYR   B CB   1 
ATOM   6446 C CG   . TYR   B 1 161 ? 43.504 -35.533 -11.761 1.00 19.06 ?  161 TYR   B CG   1 
ATOM   6447 C CD1  . TYR   B 1 161 ? 43.104 -34.213 -11.933 1.00 19.08 ?  161 TYR   B CD1  1 
ATOM   6448 C CD2  . TYR   B 1 161 ? 43.347 -36.414 -12.828 1.00 19.90 ?  161 TYR   B CD2  1 
ATOM   6449 C CE1  . TYR   B 1 161 ? 42.581 -33.784 -13.126 1.00 19.99 ?  161 TYR   B CE1  1 
ATOM   6450 C CE2  . TYR   B 1 161 ? 42.817 -35.991 -14.027 1.00 20.71 ?  161 TYR   B CE2  1 
ATOM   6451 C CZ   . TYR   B 1 161 ? 42.436 -34.673 -14.170 1.00 20.59 ?  161 TYR   B CZ   1 
ATOM   6452 O OH   . TYR   B 1 161 ? 41.902 -34.238 -15.358 1.00 22.65 ?  161 TYR   B OH   1 
ATOM   6453 H H    . TYR   B 1 161 ? 44.546 -36.987 -8.286  1.00 22.18 ?  161 TYR   B H    1 
ATOM   6454 H HA   . TYR   B 1 161 ? 42.497 -35.711 -9.156  1.00 21.82 ?  161 TYR   B HA   1 
ATOM   6455 H HB2  . TYR   B 1 161 ? 44.558 -35.255 -10.055 1.00 22.38 ?  161 TYR   B HB2  1 
ATOM   6456 H HB3  . TYR   B 1 161 ? 44.680 -36.728 -10.630 1.00 22.38 ?  161 TYR   B HB3  1 
ATOM   6457 H HD1  . TYR   B 1 161 ? 43.200 -33.606 -11.234 1.00 22.93 ?  161 TYR   B HD1  1 
ATOM   6458 H HD2  . TYR   B 1 161 ? 43.601 -37.303 -12.734 1.00 23.91 ?  161 TYR   B HD2  1 
ATOM   6459 H HE1  . TYR   B 1 161 ? 42.326 -32.891 -13.226 1.00 24.01 ?  161 TYR   B HE1  1 
ATOM   6460 H HE2  . TYR   B 1 161 ? 42.722 -36.584 -14.738 1.00 24.88 ?  161 TYR   B HE2  1 
ATOM   6461 H HH   . TYR   B 1 161 ? 41.881 -34.866 -15.913 1.00 27.20 ?  161 TYR   B HH   1 
ATOM   6462 N N    . ASP   B 1 162 ? 42.569 -38.715 -10.282 1.00 18.27 ?  162 ASP   B N    1 
ATOM   6463 C CA   . ASP   B 1 162 ? 41.743 -39.756 -10.889 1.00 18.87 ?  162 ASP   B CA   1 
ATOM   6464 C C    . ASP   B 1 162 ? 40.530 -40.086 -10.026 1.00 18.16 ?  162 ASP   B C    1 
ATOM   6465 O O    . ASP   B 1 162 ? 39.426 -40.299 -10.548 1.00 18.99 ?  162 ASP   B O    1 
ATOM   6466 C CB   . ASP   B 1 162 ? 42.573 -41.022 -11.124 1.00 20.46 ?  162 ASP   B CB   1 
ATOM   6467 C CG   . ASP   B 1 162 ? 43.583 -40.867 -12.241 1.00 22.03 ?  162 ASP   B CG   1 
ATOM   6468 O OD1  . ASP   B 1 162 ? 43.464 -39.930 -13.053 1.00 22.62 ?  162 ASP   B OD1  1 
ATOM   6469 O OD2  . ASP   B 1 162 ? 44.494 -41.716 -12.324 1.00 23.47 -1 162 ASP   B OD2  1 
ATOM   6470 H H    . ASP   B 1 162 ? 43.370 -38.958 -10.100 1.00 21.96 ?  162 ASP   B H    1 
ATOM   6471 H HA   . ASP   B 1 162 ? 41.424 -39.449 -11.750 1.00 22.68 ?  162 ASP   B HA   1 
ATOM   6472 H HB2  . ASP   B 1 162 ? 43.065 -41.238 -10.316 1.00 24.59 ?  162 ASP   B HB2  1 
ATOM   6473 H HB3  . ASP   B 1 162 ? 41.984 -41.753 -11.361 1.00 24.59 ?  162 ASP   B HB3  1 
ATOM   6474 N N    A LYS   B 1 163 ? 40.713 -40.153 -8.706  0.60 17.44 ?  163 LYS   B N    1 
ATOM   6475 N N    B LYS   B 1 163 ? 40.712 -40.144 -8.706  0.40 17.91 ?  163 LYS   B N    1 
ATOM   6476 C CA   A LYS   B 1 163 ? 39.583 -40.432 -7.827  0.60 18.12 ?  163 LYS   B CA   1 
ATOM   6477 C CA   B LYS   B 1 163 ? 39.586 -40.430 -7.822  0.40 18.48 ?  163 LYS   B CA   1 
ATOM   6478 C C    A LYS   B 1 163 ? 38.545 -39.318 -7.897  0.60 17.08 ?  163 LYS   B C    1 
ATOM   6479 C C    B LYS   B 1 163 ? 38.547 -39.316 -7.870  0.40 17.26 ?  163 LYS   B C    1 
ATOM   6480 O O    A LYS   B 1 163 ? 37.335 -39.585 -7.913  0.60 17.55 ?  163 LYS   B O    1 
ATOM   6481 O O    B LYS   B 1 163 ? 37.339 -39.583 -7.840  0.40 17.49 ?  163 LYS   B O    1 
ATOM   6482 C CB   A LYS   B 1 163 ? 40.058 -40.617 -6.388  0.60 20.64 ?  163 LYS   B CB   1 
ATOM   6483 C CB   B LYS   B 1 163 ? 40.081 -40.625 -6.391  0.40 20.82 ?  163 LYS   B CB   1 
ATOM   6484 C CG   A LYS   B 1 163 ? 38.978 -41.173 -5.478  0.60 24.54 ?  163 LYS   B CG   1 
ATOM   6485 C CG   B LYS   B 1 163 ? 39.004 -41.118 -5.446  0.40 23.99 ?  163 LYS   B CG   1 
ATOM   6486 C CD   A LYS   B 1 163 ? 39.371 -41.134 -4.013  0.60 27.51 ?  163 LYS   B CD   1 
ATOM   6487 C CD   B LYS   B 1 163 ? 39.517 -41.295 -4.030  0.40 26.52 ?  163 LYS   B CD   1 
ATOM   6488 C CE   A LYS   B 1 163 ? 38.312 -41.820 -3.163  0.60 29.47 ?  163 LYS   B CE   1 
ATOM   6489 C CE   B LYS   B 1 163 ? 38.454 -41.949 -3.162  0.40 28.16 ?  163 LYS   B CE   1 
ATOM   6490 N NZ   A LYS   B 1 163 ? 38.426 -41.485 -1.718  0.60 31.24 ?  163 LYS   B NZ   1 
ATOM   6491 N NZ   B LYS   B 1 163 ? 38.686 -41.726 -1.709  0.40 29.13 ?  163 LYS   B NZ   1 
ATOM   6492 H H    A LYS   B 1 163 ? 41.470 -40.048 -8.307  0.60 20.96 ?  163 LYS   B H    1 
ATOM   6493 H H    B LYS   B 1 163 ? 41.465 -40.027 -8.306  0.40 21.53 ?  163 LYS   B H    1 
ATOM   6494 H HA   A LYS   B 1 163 ? 39.160 -41.255 -8.113  0.60 21.77 ?  163 LYS   B HA   1 
ATOM   6495 H HA   B LYS   B 1 163 ? 39.160 -41.252 -8.110  0.40 22.20 ?  163 LYS   B HA   1 
ATOM   6496 H HB2  A LYS   B 1 163 ? 40.804 -41.239 -6.380  0.60 24.79 ?  163 LYS   B HB2  1 
ATOM   6497 H HB2  B LYS   B 1 163 ? 40.798 -41.278 -6.392  0.40 25.02 ?  163 LYS   B HB2  1 
ATOM   6498 H HB3  A LYS   B 1 163 ? 40.336 -39.761 -6.034  0.60 24.79 ?  163 LYS   B HB3  1 
ATOM   6499 H HB3  B LYS   B 1 163 ? 40.406 -39.776 -6.053  0.40 25.02 ?  163 LYS   B HB3  1 
ATOM   6500 H HG2  A LYS   B 1 163 ? 38.168 -40.651 -5.584  0.60 29.48 ?  163 LYS   B HG2  1 
ATOM   6501 H HG2  B LYS   B 1 163 ? 38.278 -40.475 -5.423  0.40 28.82 ?  163 LYS   B HG2  1 
ATOM   6502 H HG3  A LYS   B 1 163 ? 38.807 -42.100 -5.717  0.60 29.48 ?  163 LYS   B HG3  1 
ATOM   6503 H HG3  B LYS   B 1 163 ? 38.677 -41.978 -5.757  0.40 28.82 ?  163 LYS   B HG3  1 
ATOM   6504 H HD2  A LYS   B 1 163 ? 40.213 -41.603 -3.890  0.60 33.03 ?  163 LYS   B HD2  1 
ATOM   6505 H HD2  B LYS   B 1 163 ? 40.302 -41.866 -4.039  0.40 31.86 ?  163 LYS   B HD2  1 
ATOM   6506 H HD3  A LYS   B 1 163 ? 39.450 -40.212 -3.724  0.60 33.03 ?  163 LYS   B HD3  1 
ATOM   6507 H HD3  B LYS   B 1 163 ? 39.733 -40.428 -3.653  0.40 31.86 ?  163 LYS   B HD3  1 
ATOM   6508 H HE2  A LYS   B 1 163 ? 37.431 -41.556 -3.471  0.60 35.39 ?  163 LYS   B HE2  1 
ATOM   6509 H HE2  B LYS   B 1 163 ? 37.587 -41.580 -3.391  0.40 33.82 ?  163 LYS   B HE2  1 
ATOM   6510 H HE3  A LYS   B 1 163 ? 38.413 -42.779 -3.254  0.60 35.39 ?  163 LYS   B HE3  1 
ATOM   6511 H HE3  B LYS   B 1 163 ? 38.460 -42.905 -3.324  0.40 33.82 ?  163 LYS   B HE3  1 
ATOM   6512 H HZ1  A LYS   B 1 163 ? 37.789 -41.903 -1.258  0.60 37.51 ?  163 LYS   B HZ1  1 
ATOM   6513 H HZ1  B LYS   B 1 163 ? 38.044 -42.121 -1.236  0.40 34.98 ?  163 LYS   B HZ1  1 
ATOM   6514 H HZ2  A LYS   B 1 163 ? 39.221 -41.740 -1.411  0.60 37.51 ?  163 LYS   B HZ2  1 
ATOM   6515 H HZ2  B LYS   B 1 163 ? 39.472 -42.065 -1.472  0.40 34.98 ?  163 LYS   B HZ2  1 
ATOM   6516 H HZ3  A LYS   B 1 163 ? 38.339 -40.607 -1.602  0.60 37.51 ?  163 LYS   B HZ3  1 
ATOM   6517 H HZ3  B LYS   B 1 163 ? 38.680 -40.853 -1.532  0.40 34.98 ?  163 LYS   B HZ3  1 
ATOM   6518 N N    . LEU   B 1 164 ? 39.002 -38.062 -7.932  1.00 16.41 ?  164 LEU   B N    1 
ATOM   6519 C CA   . LEU   B 1 164 ? 38.090 -36.924 -7.997  1.00 16.08 ?  164 LEU   B CA   1 
ATOM   6520 C C    . LEU   B 1 164 ? 37.317 -36.911 -9.311  1.00 16.50 ?  164 LEU   B C    1 
ATOM   6521 O O    . LEU   B 1 164 ? 36.093 -36.714 -9.321  1.00 17.62 ?  164 LEU   B O    1 
ATOM   6522 C CB   . LEU   B 1 164 ? 38.892 -35.632 -7.830  1.00 15.31 ?  164 LEU   B CB   1 
ATOM   6523 C CG   . LEU   B 1 164 ? 39.408 -35.335 -6.424  1.00 16.07 ?  164 LEU   B CG   1 
ATOM   6524 C CD1  . LEU   B 1 164 ? 40.497 -34.277 -6.476  1.00 15.99 ?  164 LEU   B CD1  1 
ATOM   6525 C CD2  . LEU   B 1 164 ? 38.278 -34.891 -5.509  1.00 17.72 ?  164 LEU   B CD2  1 
ATOM   6526 H H    A LEU   B 1 164 ? 39.841 -37.845 -7.916  0.60 19.72 ?  164 LEU   B H    1 
ATOM   6527 H H    B LEU   B 1 164 ? 39.842 -37.846 -7.934  0.40 19.72 ?  164 LEU   B H    1 
ATOM   6528 H HA   . LEU   B 1 164 ? 37.457 -36.986 -7.274  1.00 19.33 ?  164 LEU   B HA   1 
ATOM   6529 H HB2  . LEU   B 1 164 ? 39.669 -35.675 -8.415  1.00 18.40 ?  164 LEU   B HB2  1 
ATOM   6530 H HB3  . LEU   B 1 164 ? 38.333 -34.890 -8.095  1.00 18.40 ?  164 LEU   B HB3  1 
ATOM   6531 H HG   . LEU   B 1 164 ? 39.799 -36.137 -6.049  1.00 19.31 ?  164 LEU   B HG   1 
ATOM   6532 H HD11 . LEU   B 1 164 ? 40.804 -34.088 -5.573  1.00 19.22 ?  164 LEU   B HD11 1 
ATOM   6533 H HD12 . LEU   B 1 164 ? 41.237 -34.605 -7.012  1.00 19.22 ?  164 LEU   B HD12 1 
ATOM   6534 H HD13 . LEU   B 1 164 ? 40.137 -33.467 -6.874  1.00 19.22 ?  164 LEU   B HD13 1 
ATOM   6535 H HD21 . LEU   B 1 164 ? 38.642 -34.664 -4.638  1.00 21.29 ?  164 LEU   B HD21 1 
ATOM   6536 H HD22 . LEU   B 1 164 ? 37.842 -34.114 -5.896  1.00 21.29 ?  164 LEU   B HD22 1 
ATOM   6537 H HD23 . LEU   B 1 164 ? 37.641 -35.617 -5.422  1.00 21.29 ?  164 LEU   B HD23 1 
ATOM   6538 N N    . VAL   B 1 165 ? 38.017 -37.096 -10.432 1.00 17.94 ?  165 VAL   B N    1 
ATOM   6539 C CA   . VAL   B 1 165 ? 37.372 -37.044 -11.740 1.00 19.26 ?  165 VAL   B CA   1 
ATOM   6540 C C    . VAL   B 1 165 ? 36.444 -38.239 -11.926 1.00 20.90 ?  165 VAL   B C    1 
ATOM   6541 O O    . VAL   B 1 165 ? 35.286 -38.094 -12.338 1.00 22.37 ?  165 VAL   B O    1 
ATOM   6542 C CB   . VAL   B 1 165 ? 38.429 -36.963 -12.858 1.00 20.56 ?  165 VAL   B CB   1 
ATOM   6543 C CG1  . VAL   B 1 165 ? 37.780 -37.077 -14.217 1.00 21.78 ?  165 VAL   B CG1  1 
ATOM   6544 C CG2  . VAL   B 1 165 ? 39.212 -35.668 -12.761 1.00 20.22 ?  165 VAL   B CG2  1 
ATOM   6545 H H    . VAL   B 1 165 ? 38.872 -37.245 -10.463 1.00 21.56 ?  165 VAL   B H    1 
ATOM   6546 H HA   . VAL   B 1 165 ? 36.839 -36.239 -11.793 1.00 23.15 ?  165 VAL   B HA   1 
ATOM   6547 H HB   . VAL   B 1 165 ? 39.063 -37.694 -12.761 1.00 24.71 ?  165 VAL   B HB   1 
ATOM   6548 H HG11 . VAL   B 1 165 ? 38.405 -36.783 -14.895 1.00 26.16 ?  165 VAL   B HG11 1 
ATOM   6549 H HG12 . VAL   B 1 165 ? 37.546 -38.009 -14.372 1.00 26.16 ?  165 VAL   B HG12 1 
ATOM   6550 H HG13 . VAL   B 1 165 ? 36.985 -36.529 -14.233 1.00 26.16 ?  165 VAL   B HG13 1 
ATOM   6551 H HG21 . VAL   B 1 165 ? 39.857 -35.626 -13.488 1.00 24.29 ?  165 VAL   B HG21 1 
ATOM   6552 H HG22 . VAL   B 1 165 ? 38.595 -34.919 -12.830 1.00 24.29 ?  165 VAL   B HG22 1 
ATOM   6553 H HG23 . VAL   B 1 165 ? 39.675 -35.634 -11.910 1.00 24.29 ?  165 VAL   B HG23 1 
ATOM   6554 N N    . SER   B 1 166 ? 36.942 -39.439 -11.616 1.00 21.65 ?  166 SER   B N    1 
ATOM   6555 C CA   . SER   B 1 166 ? 36.184 -40.646 -11.908 1.00 22.71 ?  166 SER   B CA   1 
ATOM   6556 C C    . SER   B 1 166 ? 34.919 -40.729 -11.071 1.00 22.97 ?  166 SER   B C    1 
ATOM   6557 O O    . SER   B 1 166 ? 33.949 -41.353 -11.501 1.00 24.14 ?  166 SER   B O    1 
ATOM   6558 C CB   . SER   B 1 166 ? 37.050 -41.899 -11.732 1.00 23.51 ?  166 SER   B CB   1 
ATOM   6559 O OG   . SER   B 1 166 ? 37.407 -42.109 -10.378 1.00 23.35 ?  166 SER   B OG   1 
ATOM   6560 H H    . SER   B 1 166 ? 37.711 -39.575 -11.244 1.00 26.01 ?  166 SER   B H    1 
ATOM   6561 H HA   . SER   B 1 166 ? 35.915 -40.618 -12.836 1.00 27.29 ?  166 SER   B HA   1 
ATOM   6562 H HB2  . SER   B 1 166 ? 36.552 -42.669 -12.047 1.00 28.24 ?  166 SER   B HB2  1 
ATOM   6563 H HB3  . SER   B 1 166 ? 37.860 -41.797 -12.259 1.00 28.24 ?  166 SER   B HB3  1 
ATOM   6564 H HG   . SER   B 1 166 ? 37.850 -41.456 -10.094 1.00 28.05 ?  166 SER   B HG   1 
ATOM   6565 N N    . SER   B 1 167 ? 34.894 -40.112 -9.892  1.00 21.30 ?  167 SER   B N    1 
ATOM   6566 C CA   . SER   B 1 167 ? 33.739 -40.170 -9.003  1.00 20.87 ?  167 SER   B CA   1 
ATOM   6567 C C    . SER   B 1 167 ? 32.827 -38.945 -9.090  1.00 20.44 ?  167 SER   B C    1 
ATOM   6568 O O    . SER   B 1 167 ? 31.746 -38.955 -8.491  1.00 20.84 ?  167 SER   B O    1 
ATOM   6569 C CB   . SER   B 1 167 ? 34.191 -40.357 -7.549  1.00 20.88 ?  167 SER   B CB   1 
ATOM   6570 O OG   . SER   B 1 167 ? 34.849 -39.191 -7.072  1.00 20.68 ?  167 SER   B OG   1 
ATOM   6571 H H    . SER   B 1 167 ? 35.540 -39.648 -9.582  1.00 25.59 ?  167 SER   B H    1 
ATOM   6572 H HA   . SER   B 1 167 ? 33.205 -40.946 -9.242  1.00 25.07 ?  167 SER   B HA   1 
ATOM   6573 H HB2  . SER   B 1 167 ? 33.411 -40.538 -6.998  1.00 25.09 ?  167 SER   B HB2  1 
ATOM   6574 H HB3  . SER   B 1 167 ? 34.798 -41.120 -7.508  1.00 25.09 ?  167 SER   B HB3  1 
ATOM   6575 H HG   . SER   B 1 167 ? 35.530 -39.047 -7.541  1.00 24.85 ?  167 SER   B HG   1 
ATOM   6576 N N    . PHE   B 1 168 ? 33.214 -37.900 -9.823  1.00 20.28 ?  168 PHE   B N    1 
ATOM   6577 C CA   . PHE   B 1 168 ? 32.371 -36.706 -9.901  1.00 19.48 ?  168 PHE   B CA   1 
ATOM   6578 C C    . PHE   B 1 168 ? 31.071 -36.977 -10.654 1.00 17.54 ?  168 PHE   B C    1 
ATOM   6579 O O    . PHE   B 1 168 ? 30.019 -36.385 -10.338 1.00 18.10 ?  168 PHE   B O    1 
ATOM   6580 C CB   . PHE   B 1 168 ? 33.139 -35.564 -10.566 1.00 20.06 ?  168 PHE   B CB   1 
ATOM   6581 C CG   . PHE   B 1 168 ? 32.331 -34.317 -10.715 1.00 19.64 ?  168 PHE   B CG   1 
ATOM   6582 C CD1  . PHE   B 1 168 ? 31.969 -33.583 -9.597  1.00 20.83 ?  168 PHE   B CD1  1 
ATOM   6583 C CD2  . PHE   B 1 168 ? 31.908 -33.891 -11.959 1.00 19.04 ?  168 PHE   B CD2  1 
ATOM   6584 C CE1  . PHE   B 1 168 ? 31.202 -32.441 -9.713  1.00 21.04 ?  168 PHE   B CE1  1 
ATOM   6585 C CE2  . PHE   B 1 168 ? 31.149 -32.734 -12.088 1.00 19.93 ?  168 PHE   B CE2  1 
ATOM   6586 C CZ   . PHE   B 1 168 ? 30.795 -32.008 -10.958 1.00 20.40 ?  168 PHE   B CZ   1 
ATOM   6587 H H    . PHE   B 1 168 ? 33.946 -37.855 -10.267 1.00 24.36 ?  168 PHE   B H    1 
ATOM   6588 H HA   . PHE   B 1 168 ? 32.136 -36.428 -9.005  1.00 23.40 ?  168 PHE   B HA   1 
ATOM   6589 H HB2  . PHE   B 1 168 ? 33.912 -35.350 -10.025 1.00 24.10 ?  168 PHE   B HB2  1 
ATOM   6590 H HB3  . PHE   B 1 168 ? 33.417 -35.843 -11.451 1.00 24.10 ?  168 PHE   B HB3  1 
ATOM   6591 H HD1  . PHE   B 1 168 ? 32.237 -33.875 -8.756  1.00 25.02 ?  168 PHE   B HD1  1 
ATOM   6592 H HD2  . PHE   B 1 168 ? 32.142 -34.369 -12.719 1.00 22.88 ?  168 PHE   B HD2  1 
ATOM   6593 H HE1  . PHE   B 1 168 ? 30.969 -31.961 -8.955  1.00 25.28 ?  168 PHE   B HE1  1 
ATOM   6594 H HE2  . PHE   B 1 168 ? 30.869 -32.448 -12.930 1.00 23.94 ?  168 PHE   B HE2  1 
ATOM   6595 H HZ   . PHE   B 1 168 ? 30.279 -31.237 -11.042 1.00 24.51 ?  168 PHE   B HZ   1 
ATOM   6596 N N    . LEU   B 1 169 ? 31.126 -37.852 -11.656 1.00 18.08 ?  169 LEU   B N    1 
ATOM   6597 C CA   . LEU   B 1 169 ? 29.955 -38.165 -12.466 1.00 19.77 ?  169 LEU   B CA   1 
ATOM   6598 C C    . LEU   B 1 169 ? 29.952 -39.607 -12.964 1.00 22.01 ?  169 LEU   B C    1 
ATOM   6599 O O    . LEU   B 1 169 ? 29.053 -40.023 -13.700 1.00 24.18 ?  169 LEU   B O    1 
ATOM   6600 C CB   . LEU   B 1 169 ? 29.885 -37.228 -13.669 1.00 21.23 ?  169 LEU   B CB   1 
ATOM   6601 C CG   . LEU   B 1 169 ? 28.614 -36.388 -13.800 1.00 23.94 ?  169 LEU   B CG   1 
ATOM   6602 C CD1  . LEU   B 1 169 ? 28.553 -35.779 -15.181 1.00 25.04 ?  169 LEU   B CD1  1 
ATOM   6603 C CD2  . LEU   B 1 169 ? 27.365 -37.204 -13.520 1.00 23.74 ?  169 LEU   B CD2  1 
ATOM   6604 O OXT  . LEU   B 1 169 ? 30.850 -40.382 -12.653 1.00 22.86 -1 169 LEU   B OXT  1 
ATOM   6605 H H    . LEU   B 1 169 ? 31.837 -38.275 -11.895 1.00 21.72 ?  169 LEU   B H    1 
ATOM   6606 H HA   . LEU   B 1 169 ? 29.168 -38.025 -11.923 1.00 23.76 ?  169 LEU   B HA   1 
ATOM   6607 H HB2  . LEU   B 1 169 ? 30.632 -36.609 -13.624 1.00 25.51 ?  169 LEU   B HB2  1 
ATOM   6608 H HB3  . LEU   B 1 169 ? 29.957 -37.758 -14.479 1.00 25.51 ?  169 LEU   B HB3  1 
ATOM   6609 H HG   . LEU   B 1 169 ? 28.648 -35.661 -13.156 1.00 28.75 ?  169 LEU   B HG   1 
ATOM   6610 H HD11 . LEU   B 1 169 ? 27.763 -35.220 -15.243 1.00 30.07 ?  169 LEU   B HD11 1 
ATOM   6611 H HD12 . LEU   B 1 169 ? 29.350 -35.245 -15.324 1.00 30.07 ?  169 LEU   B HD12 1 
ATOM   6612 H HD13 . LEU   B 1 169 ? 28.508 -36.492 -15.835 1.00 30.07 ?  169 LEU   B HD13 1 
ATOM   6613 H HD21 . LEU   B 1 169 ? 26.609 -36.791 -13.959 1.00 28.52 ?  169 LEU   B HD21 1 
ATOM   6614 H HD22 . LEU   B 1 169 ? 27.495 -38.105 -13.862 1.00 28.52 ?  169 LEU   B HD22 1 
ATOM   6615 H HD23 . LEU   B 1 169 ? 27.219 -37.235 -12.562 1.00 28.52 ?  169 LEU   B HD23 1 
HETATM 6616 C C1   T TFA   C 2 .   ? 12.115 -1.247  1.467   0.20 10.08 ?  201 TFA   A C1   1 
HETATM 6617 C C2   T TFA   C 2 .   ? 12.720 -1.699  0.111   0.20 11.73 ?  201 TFA   A C2   1 
HETATM 6618 O O    T TFA   C 2 .   ? 12.819 -1.547  2.439   0.20 9.13  ?  201 TFA   A O    1 
HETATM 6619 F F1   T TFA   C 2 .   ? 12.742 -3.043  0.043   0.20 12.54 ?  201 TFA   A F1   1 
HETATM 6620 F F2   T TFA   C 2 .   ? 12.018 -1.285  -0.959  0.20 12.01 ?  201 TFA   A F2   1 
HETATM 6621 F F3   T TFA   C 2 .   ? 13.969 -1.256  -0.077  0.20 13.17 ?  201 TFA   A F3   1 
HETATM 6622 O OXT  T TFA   C 2 .   ? 11.038 -0.656  1.396   0.20 9.97  ?  201 TFA   A OXT  1 
HETATM 6623 N N2   B A1A8J D 3 .   ? 14.934 0.191   4.319   0.40 11.30 ?  202 A1A8J A N2   1 
HETATM 6624 C C3   B A1A8J D 3 .   ? 15.199 0.455   -0.009  0.40 12.90 ?  202 A1A8J A C3   1 
HETATM 6625 C C6   B A1A8J D 3 .   ? 15.029 1.376   3.622   0.40 11.17 ?  202 A1A8J A C6   1 
HETATM 6626 C C9   B A1A8J D 3 .   ? 15.278 2.574   4.378   0.40 11.78 ?  202 A1A8J A C9   1 
HETATM 6627 C C12  B A1A8J D 3 .   ? 13.246 -1.672  0.348   0.40 14.39 ?  202 A1A8J A C12  1 
HETATM 6628 C C14  B A1A8J D 3 .   ? 12.355 -1.426  -1.936  0.40 16.47 ?  202 A1A8J A C14  1 
HETATM 6629 C C17  B A1A8J D 3 .   ? 10.990 0.905   -1.020  0.40 16.38 ?  202 A1A8J A C17  1 
HETATM 6630 C C19  B A1A8J D 3 .   ? 12.139 0.305   1.297   0.40 14.18 ?  202 A1A8J A C19  1 
HETATM 6631 C C1   B A1A8J D 3 .   ? 13.374 -0.646  1.499   0.40 13.26 ?  202 A1A8J A C1   1 
HETATM 6632 C C10  B A1A8J D 3 .   ? 15.468 4.005   4.176   0.40 12.62 ?  202 A1A8J A C10  1 
HETATM 6633 C C11  B A1A8J D 3 .   ? 15.647 4.606   5.427   0.40 12.20 ?  202 A1A8J A C11  1 
HETATM 6634 C C13  B A1A8J D 3 .   ? 12.426 -0.950  -0.606  0.40 15.20 ?  202 A1A8J A C13  1 
HETATM 6635 C C15  B A1A8J D 3 .   ? 11.543 -0.650  -2.783  0.40 17.20 ?  202 A1A8J A C15  1 
HETATM 6636 C C16  B A1A8J D 3 .   ? 10.889 0.460   -2.356  0.40 17.14 ?  202 A1A8J A C16  1 
HETATM 6637 C C18  B A1A8J D 3 .   ? 11.785 0.167   -0.154  0.40 15.30 ?  202 A1A8J A C18  1 
HETATM 6638 C C2   B A1A8J D 3 .   ? 14.811 0.022   1.427   0.40 12.35 ?  202 A1A8J A C2   1 
HETATM 6639 C C4   B A1A8J D 3 .   ? 14.852 1.915   -0.088  0.40 12.73 ?  202 A1A8J A C4   1 
HETATM 6640 C C5   B A1A8J D 3 .   ? 14.995 2.417   1.345   0.40 12.04 ?  202 A1A8J A C5   1 
HETATM 6641 C C7   B A1A8J D 3 .   ? 15.045 0.181   5.680   0.40 11.87 ?  202 A1A8J A C7   1 
HETATM 6642 C C8   B A1A8J D 3 .   ? 15.362 2.403   5.780   0.40 12.14 ?  202 A1A8J A C8   1 
HETATM 6643 N N1   B A1A8J D 3 .   ? 14.902 1.269   2.258   0.40 11.59 ?  202 A1A8J A N1   1 
HETATM 6644 N N3   B A1A8J D 3 .   ? 15.254 1.235   6.467   0.40 12.32 ?  202 A1A8J A N3   1 
HETATM 6645 N N4   B A1A8J D 3 .   ? 15.585 3.610   6.407   0.40 12.43 ?  202 A1A8J A N4   1 
HETATM 6646 O O1   B A1A8J D 3 .   ? 13.296 -1.299  2.756   0.40 12.59 ?  202 A1A8J A O1   1 
HETATM 6647 H H3   B A1A8J D 3 .   ? 16.268 0.258   -0.212  0.40 15.50 ?  202 A1A8J A H3   1 
HETATM 6648 H H4   B A1A8J D 3 .   ? 14.776 -0.128  -0.834  0.40 15.50 ?  202 A1A8J A H4   1 
HETATM 6649 H H13  B A1A8J D 3 .   ? 14.241 -1.933  -0.075  0.40 17.30 ?  202 A1A8J A H13  1 
HETATM 6650 H H14  B A1A8J D 3 .   ? 12.752 -2.577  0.675   0.40 17.30 ?  202 A1A8J A H14  1 
HETATM 6651 H H15  B A1A8J D 3 .   ? 12.864 -2.266  -2.266  0.40 19.79 ?  202 A1A8J A H15  1 
HETATM 6652 H H18  B A1A8J D 3 .   ? 10.385 1.791   -0.869  0.40 19.68 ?  202 A1A8J A H18  1 
HETATM 6653 H H20  B A1A8J D 3 .   ? 11.284 0.068   1.980   0.40 17.04 ?  202 A1A8J A H20  1 
HETATM 6654 H H19  B A1A8J D 3 .   ? 12.335 1.364   1.556   0.40 17.04 ?  202 A1A8J A H19  1 
HETATM 6655 H H10  B A1A8J D 3 .   ? 15.456 4.550   3.290   0.40 15.18 ?  202 A1A8J A H10  1 
HETATM 6656 H H11  B A1A8J D 3 .   ? 15.807 5.620   5.736   0.40 14.67 ?  202 A1A8J A H11  1 
HETATM 6657 H H16  B A1A8J D 3 .   ? 11.483 -1.008  -3.795  0.40 20.67 ?  202 A1A8J A H16  1 
HETATM 6658 H H17  B A1A8J D 3 .   ? 10.264 1.000   -3.080  0.40 20.59 ?  202 A1A8J A H17  1 
HETATM 6659 H H1   B A1A8J D 3 .   ? 15.571 -0.739  1.798   0.40 14.85 ?  202 A1A8J A H1   1 
HETATM 6660 H H5   B A1A8J D 3 .   ? 13.865 2.073   -0.550  0.40 15.31 ?  202 A1A8J A H5   1 
HETATM 6661 H H6   B A1A8J D 3 .   ? 15.529 2.402   -0.809  0.40 15.31 ?  202 A1A8J A H6   1 
HETATM 6662 H H8   B A1A8J D 3 .   ? 14.266 3.209   1.557   0.40 14.48 ?  202 A1A8J A H8   1 
HETATM 6663 H H7   B A1A8J D 3 .   ? 16.000 2.926   1.437   0.40 14.48 ?  202 A1A8J A H7   1 
HETATM 6664 H H9   B A1A8J D 3 .   ? 14.947 -0.772  6.279   0.40 14.28 ?  202 A1A8J A H9   1 
HETATM 6665 H H12  B A1A8J D 3 .   ? 15.688 3.795   7.417   0.40 14.95 ?  202 A1A8J A H12  1 
HETATM 6666 H H2   B A1A8J D 3 .   ? 12.415 -1.643  2.858   0.40 15.14 ?  202 A1A8J A H2   1 
HETATM 6667 O O    . HOH   E 4 .   ? 14.773 -4.557  20.571  1.00 49.66 ?  301 HOH   A O    1 
HETATM 6668 O O    . HOH   E 4 .   ? 34.408 -1.822  12.491  1.00 38.37 ?  302 HOH   A O    1 
HETATM 6669 O O    . HOH   E 4 .   ? 11.977 0.370   14.804  1.00 35.24 ?  303 HOH   A O    1 
HETATM 6670 O O    . HOH   E 4 .   ? 19.835 -12.359 -9.066  1.00 25.45 ?  304 HOH   A O    1 
HETATM 6671 O O    A HOH   E 4 .   ? 4.685  3.964   0.576   0.60 21.59 ?  305 HOH   A O    1 
HETATM 6672 O O    . HOH   E 4 .   ? 15.090 -12.200 18.652  1.00 39.96 ?  306 HOH   A O    1 
HETATM 6673 O O    . HOH   E 4 .   ? 28.260 -0.117  -13.424 1.00 38.13 ?  307 HOH   A O    1 
HETATM 6674 O O    . HOH   E 4 .   ? 28.974 0.462   -9.745  1.00 22.96 ?  308 HOH   A O    1 
HETATM 6675 O O    B HOH   E 4 .   ? 5.344  3.481   0.433   0.40 23.29 ?  309 HOH   A O    1 
HETATM 6676 O O    B HOH   E 4 .   ? 18.752 -0.278  -3.961  0.40 35.67 ?  310 HOH   A O    1 
HETATM 6677 O O    . HOH   E 4 .   ? 15.076 3.901   17.734  1.00 39.15 ?  311 HOH   A O    1 
HETATM 6678 O O    . HOH   E 4 .   ? 26.792 11.437  1.642   1.00 18.59 ?  312 HOH   A O    1 
HETATM 6679 O O    . HOH   E 4 .   ? 42.443 10.574  5.229   1.00 21.60 ?  313 HOH   A O    1 
HETATM 6680 O O    . HOH   E 4 .   ? 0.718  -4.209  0.049   1.00 28.37 ?  314 HOH   A O    1 
HETATM 6681 O O    . HOH   E 4 .   ? 28.130 -6.288  19.602  1.00 39.53 ?  315 HOH   A O    1 
HETATM 6682 O O    . HOH   E 4 .   ? -0.643 -8.395  2.130   1.00 50.67 ?  316 HOH   A O    1 
HETATM 6683 O O    . HOH   E 4 .   ? 7.997  -3.025  -5.827  1.00 53.22 ?  317 HOH   A O    1 
HETATM 6684 O O    . HOH   E 4 .   ? 13.535 -15.175 -7.562  1.00 27.93 ?  318 HOH   A O    1 
HETATM 6685 O O    . HOH   E 4 .   ? 14.671 -13.903 16.680  1.00 24.55 ?  319 HOH   A O    1 
HETATM 6686 O O    B HOH   E 4 .   ? 14.773 7.317   7.615   0.40 20.69 ?  320 HOH   A O    1 
HETATM 6687 O O    A HOH   E 4 .   ? 11.716 -10.756 -10.081 0.60 38.24 ?  321 HOH   A O    1 
HETATM 6688 O O    . HOH   E 4 .   ? 30.229 -13.329 -8.578  1.00 21.02 ?  322 HOH   A O    1 
HETATM 6689 O O    . HOH   E 4 .   ? 9.107  -10.084 19.325  1.00 38.43 ?  323 HOH   A O    1 
HETATM 6690 O O    . HOH   E 4 .   ? 18.879 -21.928 6.933   1.00 33.81 ?  324 HOH   A O    1 
HETATM 6691 O O    . HOH   E 4 .   ? 33.946 -1.006  -8.920  1.00 27.50 ?  325 HOH   A O    1 
HETATM 6692 O O    . HOH   E 4 .   ? 6.857  -8.016  11.841  1.00 18.80 ?  326 HOH   A O    1 
HETATM 6693 O O    B HOH   E 4 .   ? 21.385 2.877   0.105   0.40 12.54 ?  327 HOH   A O    1 
HETATM 6694 O O    B HOH   E 4 .   ? 15.698 1.158   -6.172  0.40 30.35 ?  328 HOH   A O    1 
HETATM 6695 O O    A HOH   E 4 .   ? -0.491 -3.037  3.069   0.60 28.75 ?  329 HOH   A O    1 
HETATM 6696 O O    . HOH   E 4 .   ? 26.454 -19.301 -1.807  1.00 15.52 ?  330 HOH   A O    1 
HETATM 6697 O O    . HOH   E 4 .   ? 8.927  -12.058 17.120  1.00 40.34 ?  331 HOH   A O    1 
HETATM 6698 O O    . HOH   E 4 .   ? 18.629 -19.348 13.553  1.00 36.64 ?  332 HOH   A O    1 
HETATM 6699 O O    . HOH   E 4 .   ? 3.594  -9.211  9.858   1.00 30.15 ?  333 HOH   A O    1 
HETATM 6700 O O    . HOH   E 4 .   ? 31.005 -18.059 7.797   1.00 21.19 ?  334 HOH   A O    1 
HETATM 6701 O O    . HOH   E 4 .   ? 36.227 -5.095  -0.548  1.00 31.25 ?  335 HOH   A O    1 
HETATM 6702 O O    . HOH   E 4 .   ? 44.285 7.100   6.361   1.00 27.56 ?  336 HOH   A O    1 
HETATM 6703 O O    A HOH   E 4 .   ? 14.621 -3.610  3.071   0.60 13.52 ?  337 HOH   A O    1 
HETATM 6704 O O    . HOH   E 4 .   ? 38.250 10.140  7.176   1.00 32.79 ?  338 HOH   A O    1 
HETATM 6705 O O    . HOH   E 4 .   ? 37.542 2.788   10.132  1.00 30.83 ?  339 HOH   A O    1 
HETATM 6706 O O    . HOH   E 4 .   ? 28.471 -10.762 -13.975 1.00 46.16 ?  340 HOH   A O    1 
HETATM 6707 O O    . HOH   E 4 .   ? 9.909  -21.343 5.717   1.00 21.89 ?  341 HOH   A O    1 
HETATM 6708 O O    . HOH   E 4 .   ? 27.359 13.798  2.815   1.00 31.09 ?  342 HOH   A O    1 
HETATM 6709 O O    . HOH   E 4 .   ? 39.726 -1.023  -5.191  1.00 21.15 ?  343 HOH   A O    1 
HETATM 6710 O O    B HOH   E 4 .   ? 14.648 -3.944  3.481   0.40 13.77 ?  344 HOH   A O    1 
HETATM 6711 O O    . HOH   E 4 .   ? 38.553 4.996   6.953   1.00 17.03 ?  345 HOH   A O    1 
HETATM 6712 O O    A HOH   E 4 .   ? 14.263 0.623   6.767   0.60 20.30 ?  346 HOH   A O    1 
HETATM 6713 O O    . HOH   E 4 .   ? 20.603 -19.718 -5.093  1.00 27.36 ?  347 HOH   A O    1 
HETATM 6714 O O    A HOH   E 4 .   ? 13.298 -1.405  -6.554  0.60 18.31 ?  348 HOH   A O    1 
HETATM 6715 O O    . HOH   E 4 .   ? 14.322 -21.137 -4.315  1.00 30.12 ?  349 HOH   A O    1 
HETATM 6716 O O    . HOH   E 4 .   ? 37.231 -2.839  9.625   1.00 44.65 ?  350 HOH   A O    1 
HETATM 6717 O O    . HOH   E 4 .   ? 22.673 12.494  1.570   1.00 16.61 ?  351 HOH   A O    1 
HETATM 6718 O O    A HOH   E 4 .   ? 17.085 -18.039 15.059  0.60 22.08 ?  352 HOH   A O    1 
HETATM 6719 O O    . HOH   E 4 .   ? 25.658 -0.756  -7.351  1.00 18.54 ?  353 HOH   A O    1 
HETATM 6720 O O    . HOH   E 4 .   ? 31.835 -9.296  -6.703  1.00 23.95 ?  354 HOH   A O    1 
HETATM 6721 O O    . HOH   E 4 .   ? 22.270 5.374   18.997  1.00 41.12 ?  355 HOH   A O    1 
HETATM 6722 O O    . HOH   E 4 .   ? 37.301 12.020  4.954   1.00 31.44 ?  356 HOH   A O    1 
HETATM 6723 O O    . HOH   E 4 .   ? 42.480 4.243   5.310   1.00 32.72 ?  357 HOH   A O    1 
HETATM 6724 O O    . HOH   E 4 .   ? 18.611 9.505   9.008   1.00 23.37 ?  358 HOH   A O    1 
HETATM 6725 O O    . HOH   E 4 .   ? 21.890 -21.852 8.464   1.00 30.72 ?  359 HOH   A O    1 
HETATM 6726 O O    . HOH   E 4 .   ? 17.082 -17.731 -5.123  1.00 27.74 ?  360 HOH   A O    1 
HETATM 6727 O O    A HOH   E 4 .   ? 7.977  -12.554 -0.896  0.60 19.41 ?  361 HOH   A O    1 
HETATM 6728 O O    . HOH   E 4 .   ? 43.995 8.464   -3.076  1.00 26.01 ?  362 HOH   A O    1 
HETATM 6729 O O    . HOH   E 4 .   ? 31.712 8.232   14.857  1.00 25.70 ?  363 HOH   A O    1 
HETATM 6730 O O    . HOH   E 4 .   ? 35.757 -12.616 6.786   1.00 17.20 ?  364 HOH   A O    1 
HETATM 6731 O O    . HOH   E 4 .   ? 24.008 -2.064  -2.143  1.00 12.07 ?  365 HOH   A O    1 
HETATM 6732 O O    A HOH   E 4 .   ? 17.484 -1.676  0.413   0.60 20.48 ?  366 HOH   A O    1 
HETATM 6733 O O    . HOH   E 4 .   ? 7.959  -21.435 4.011   1.00 50.33 ?  367 HOH   A O    1 
HETATM 6734 O O    . HOH   E 4 .   ? 31.053 -13.915 -2.489  1.00 15.03 ?  368 HOH   A O    1 
HETATM 6735 O O    . HOH   E 4 .   ? 22.605 -11.957 21.702  1.00 45.21 ?  369 HOH   A O    1 
HETATM 6736 O O    . HOH   E 4 .   ? 21.283 10.317  15.039  1.00 37.52 ?  370 HOH   A O    1 
HETATM 6737 O O    . HOH   E 4 .   ? 14.166 -4.368  -12.242 1.00 44.65 ?  371 HOH   A O    1 
HETATM 6738 O O    . HOH   E 4 .   ? 31.795 -7.282  -9.848  1.00 23.09 ?  372 HOH   A O    1 
HETATM 6739 O O    . HOH   E 4 .   ? 30.796 3.105   8.216   1.00 13.21 ?  373 HOH   A O    1 
HETATM 6740 O O    . HOH   E 4 .   ? 22.242 -19.223 11.405  1.00 37.72 ?  374 HOH   A O    1 
HETATM 6741 O O    A HOH   E 4 .   ? 21.234 -2.365  -2.078  0.60 15.09 ?  375 HOH   A O    1 
HETATM 6742 O O    . HOH   E 4 .   ? 33.628 -7.124  4.276   1.00 17.54 ?  376 HOH   A O    1 
HETATM 6743 O O    . HOH   E 4 .   ? 23.439 11.404  4.076   1.00 13.72 ?  377 HOH   A O    1 
HETATM 6744 O O    . HOH   E 4 .   ? 33.495 -16.906 8.050   1.00 20.43 ?  378 HOH   A O    1 
HETATM 6745 O O    . HOH   E 4 .   ? 13.865 -4.851  17.383  1.00 27.27 ?  379 HOH   A O    1 
HETATM 6746 O O    . HOH   E 4 .   ? 27.474 -10.569 14.052  1.00 18.84 ?  380 HOH   A O    1 
HETATM 6747 O O    . HOH   E 4 .   ? 16.983 -19.181 4.856   1.00 17.35 ?  381 HOH   A O    1 
HETATM 6748 O O    . HOH   E 4 .   ? 43.341 7.866   2.719   1.00 24.94 ?  382 HOH   A O    1 
HETATM 6749 O O    . HOH   E 4 .   ? 24.538 1.999   -7.017  1.00 23.41 ?  383 HOH   A O    1 
HETATM 6750 O O    . HOH   E 4 .   ? 26.903 4.192   -0.655  1.00 14.10 ?  384 HOH   A O    1 
HETATM 6751 O O    . HOH   E 4 .   ? 27.426 -6.169  -14.017 1.00 37.78 ?  385 HOH   A O    1 
HETATM 6752 O O    . HOH   E 4 .   ? 16.497 -21.990 0.952   1.00 30.85 ?  386 HOH   A O    1 
HETATM 6753 O O    . HOH   E 4 .   ? 24.248 -7.738  14.432  1.00 18.53 ?  387 HOH   A O    1 
HETATM 6754 O O    . HOH   E 4 .   ? 14.065 -22.995 7.429   1.00 20.36 ?  388 HOH   A O    1 
HETATM 6755 O O    B HOH   E 4 .   ? 21.659 -2.335  -3.118  0.40 21.23 ?  389 HOH   A O    1 
HETATM 6756 O O    . HOH   E 4 .   ? 21.750 -13.698 -8.120  1.00 33.22 ?  390 HOH   A O    1 
HETATM 6757 O O    . HOH   E 4 .   ? 32.747 -9.209  5.926   1.00 20.76 ?  391 HOH   A O    1 
HETATM 6758 O O    T HOH   E 4 .   ? 15.395 -0.379  2.355   0.20 10.51 ?  392 HOH   A O    1 
HETATM 6759 O O    . HOH   E 4 .   ? 37.526 -1.999  5.763   1.00 27.23 ?  393 HOH   A O    1 
HETATM 6760 O O    . HOH   E 4 .   ? 24.348 3.635   -1.798  1.00 16.70 ?  394 HOH   A O    1 
HETATM 6761 O O    A HOH   E 4 .   ? 15.788 -0.899  5.240   0.60 19.64 ?  395 HOH   A O    1 
HETATM 6762 O O    A HOH   E 4 .   ? 11.055 -0.335  1.902   0.40 24.66 ?  396 HOH   A O    1 
HETATM 6763 O O    A HOH   E 4 .   ? 7.699  -6.296  -6.535  0.60 37.21 ?  397 HOH   A O    1 
HETATM 6764 O O    . HOH   E 4 .   ? 30.719 1.885   16.653  1.00 21.68 ?  398 HOH   A O    1 
HETATM 6765 O O    . HOH   E 4 .   ? 27.435 2.356   18.756  1.00 30.67 ?  399 HOH   A O    1 
HETATM 6766 O O    . HOH   E 4 .   ? 23.907 -15.750 -9.228  1.00 35.96 ?  400 HOH   A O    1 
HETATM 6767 O O    . HOH   E 4 .   ? 6.357  -5.465  11.052  1.00 19.12 ?  401 HOH   A O    1 
HETATM 6768 O O    . HOH   E 4 .   ? 10.905 1.734   12.553  1.00 23.66 ?  402 HOH   A O    1 
HETATM 6769 O O    A HOH   E 4 .   ? 21.339 3.190   -0.384  0.60 12.61 ?  403 HOH   A O    1 
HETATM 6770 O O    . HOH   E 4 .   ? 23.866 -20.233 -1.379  1.00 18.15 ?  404 HOH   A O    1 
HETATM 6771 O O    . HOH   E 4 .   ? 24.681 -17.522 12.628  1.00 25.69 ?  405 HOH   A O    1 
HETATM 6772 O O    . HOH   E 4 .   ? 15.469 11.851  7.887   1.00 44.50 ?  406 HOH   A O    1 
HETATM 6773 O O    . HOH   E 4 .   ? 14.438 -24.665 11.545  1.00 41.51 ?  407 HOH   A O    1 
HETATM 6774 O O    . HOH   E 4 .   ? 38.126 -1.321  -1.951  1.00 19.94 ?  408 HOH   A O    1 
HETATM 6775 O O    . HOH   E 4 .   ? 40.846 -8.212  -6.872  1.00 36.05 ?  409 HOH   A O    1 
HETATM 6776 O O    . HOH   E 4 .   ? 20.533 -19.970 2.726   1.00 19.84 ?  410 HOH   A O    1 
HETATM 6777 O O    . HOH   E 4 .   ? 30.050 -10.082 12.964  1.00 23.17 ?  411 HOH   A O    1 
HETATM 6778 O O    . HOH   E 4 .   ? 16.187 16.682  8.624   1.00 35.80 ?  412 HOH   A O    1 
HETATM 6779 O O    . HOH   E 4 .   ? 30.970 6.179   -12.349 1.00 29.94 ?  413 HOH   A O    1 
HETATM 6780 O O    . HOH   E 4 .   ? 30.306 -12.887 13.465  1.00 20.78 ?  414 HOH   A O    1 
HETATM 6781 O O    A HOH   E 4 .   ? 20.092 4.567   -7.583  0.60 17.96 ?  415 HOH   A O    1 
HETATM 6782 O O    . HOH   E 4 .   ? 6.586  -3.186  12.772  1.00 27.81 ?  416 HOH   A O    1 
HETATM 6783 O O    A HOH   E 4 .   ? 18.947 -0.635  -1.656  0.60 14.31 ?  417 HOH   A O    1 
HETATM 6784 O O    . HOH   E 4 .   ? 32.640 -4.307  -9.933  1.00 26.87 ?  418 HOH   A O    1 
HETATM 6785 O O    . HOH   E 4 .   ? 24.017 3.992   -4.830  1.00 27.53 ?  419 HOH   A O    1 
HETATM 6786 O O    . HOH   E 4 .   ? 22.637 8.120   18.286  1.00 46.10 ?  420 HOH   A O    1 
HETATM 6787 O O    B HOH   E 4 .   ? 19.115 -2.575  -8.816  0.40 37.09 ?  421 HOH   A O    1 
HETATM 6788 O O    A HOH   E 4 .   ? 10.372 -13.686 -1.687  0.60 14.51 ?  422 HOH   A O    1 
HETATM 6789 O O    A HOH   E 4 .   ? 15.171 -21.540 14.161  0.60 16.52 ?  423 HOH   A O    1 
HETATM 6790 O O    . HOH   E 4 .   ? 27.887 0.870   -7.185  1.00 15.80 ?  424 HOH   A O    1 
HETATM 6791 O O    . HOH   E 4 .   ? 35.048 -5.220  -3.116  1.00 18.98 ?  425 HOH   A O    1 
HETATM 6792 O O    . HOH   E 4 .   ? 41.583 1.571   4.962   1.00 37.02 ?  426 HOH   A O    1 
HETATM 6793 O O    . HOH   E 4 .   ? 19.486 -11.030 24.144  1.00 65.52 ?  427 HOH   A O    1 
HETATM 6794 O O    . HOH   E 4 .   ? 32.509 -10.622 3.166   1.00 32.85 ?  428 HOH   A O    1 
HETATM 6795 O O    A HOH   E 4 .   ? 14.473 -0.422  -12.070 0.60 21.05 ?  429 HOH   A O    1 
HETATM 6796 O O    A HOH   E 4 .   ? 18.563 -2.450  -16.366 0.60 31.57 ?  430 HOH   A O    1 
HETATM 6797 O O    . HOH   E 4 .   ? 36.742 -4.918  5.339   1.00 25.39 ?  431 HOH   A O    1 
HETATM 6798 O O    B HOH   E 4 .   ? 18.397 -1.067  -0.389  0.40 25.65 ?  432 HOH   A O    1 
HETATM 6799 O O    . HOH   E 4 .   ? 11.662 -10.695 16.933  1.00 24.76 ?  433 HOH   A O    1 
HETATM 6800 O O    . HOH   E 4 .   ? 18.636 2.005   -0.664  1.00 15.60 ?  434 HOH   A O    1 
HETATM 6801 O O    . HOH   E 4 .   ? 5.452  2.920   5.020   1.00 32.84 ?  435 HOH   A O    1 
HETATM 6802 O O    B HOH   E 4 .   ? 7.135  1.753   6.942   0.40 29.62 ?  436 HOH   A O    1 
HETATM 6803 O O    . HOH   E 4 .   ? 15.923 2.254   24.692  1.00 48.84 ?  437 HOH   A O    1 
HETATM 6804 O O    A HOH   E 4 .   ? 16.010 6.998   2.949   0.60 13.80 ?  438 HOH   A O    1 
HETATM 6805 O O    . HOH   E 4 .   ? 16.189 -14.183 20.210  1.00 55.98 ?  439 HOH   A O    1 
HETATM 6806 O O    B HOH   E 4 .   ? 7.495  1.393   -3.087  0.40 24.64 ?  440 HOH   A O    1 
HETATM 6807 O O    . HOH   E 4 .   ? 8.990  -16.652 -2.466  1.00 52.74 ?  441 HOH   A O    1 
HETATM 6808 O O    . HOH   E 4 .   ? 44.986 -0.609  2.999   1.00 42.29 ?  442 HOH   A O    1 
HETATM 6809 O O    . HOH   E 4 .   ? 20.556 -17.649 24.769  1.00 54.34 ?  443 HOH   A O    1 
HETATM 6810 O O    . HOH   E 4 .   ? 29.727 -2.008  -12.861 1.00 43.97 ?  444 HOH   A O    1 
HETATM 6811 O O    B HOH   E 4 .   ? 22.688 5.917   -1.778  0.40 22.83 ?  445 HOH   A O    1 
HETATM 6812 O O    . HOH   E 4 .   ? 23.618 -8.021  17.089  1.00 23.87 ?  446 HOH   A O    1 
HETATM 6813 O O    B HOH   E 4 .   ? 11.465 6.347   10.690  0.40 27.35 ?  447 HOH   A O    1 
HETATM 6814 O O    . HOH   E 4 .   ? 18.474 4.969   -15.103 1.00 49.59 ?  448 HOH   A O    1 
HETATM 6815 O O    . HOH   E 4 .   ? 10.390 -22.186 -1.194  1.00 55.66 ?  449 HOH   A O    1 
HETATM 6816 O O    . HOH   E 4 .   ? 23.288 -20.890 1.270   1.00 19.72 ?  450 HOH   A O    1 
HETATM 6817 O O    . HOH   E 4 .   ? 37.693 -8.795  -3.443  1.00 24.96 ?  451 HOH   A O    1 
HETATM 6818 O O    A HOH   E 4 .   ? 16.249 2.984   -1.477  0.60 16.60 ?  452 HOH   A O    1 
HETATM 6819 O O    . HOH   E 4 .   ? 27.192 -3.235  19.311  1.00 39.05 ?  453 HOH   A O    1 
HETATM 6820 O O    . HOH   E 4 .   ? 31.284 -12.743 0.017   1.00 20.54 ?  454 HOH   A O    1 
HETATM 6821 O O    . HOH   E 4 .   ? 34.405 -8.076  -0.596  1.00 31.45 ?  455 HOH   A O    1 
HETATM 6822 O O    A HOH   E 4 .   ? 14.016 -0.294  3.430   0.40 33.98 ?  456 HOH   A O    1 
HETATM 6823 O O    . HOH   E 4 .   ? 21.420 -14.688 17.936  1.00 54.37 ?  457 HOH   A O    1 
HETATM 6824 O O    . HOH   E 4 .   ? 21.263 -9.152  21.369  1.00 55.66 ?  458 HOH   A O    1 
HETATM 6825 O O    . HOH   E 4 .   ? -1.435 -4.845  7.605   1.00 47.52 ?  459 HOH   A O    1 
HETATM 6826 O O    . HOH   E 4 .   ? 18.399 -16.045 16.383  1.00 41.47 ?  460 HOH   A O    1 
HETATM 6827 O O    B HOH   E 4 .   ? 15.823 7.257   2.817   0.40 26.32 ?  461 HOH   A O    1 
HETATM 6828 O O    . HOH   E 4 .   ? 30.584 14.804  2.715   1.00 20.49 ?  462 HOH   A O    1 
HETATM 6829 O O    B HOH   E 4 .   ? 19.566 -0.505  -7.041  0.40 28.78 ?  463 HOH   A O    1 
HETATM 6830 O O    . HOH   E 4 .   ? 23.188 7.543   -3.371  1.00 36.11 ?  464 HOH   A O    1 
HETATM 6831 O O    . HOH   E 4 .   ? 15.064 -8.407  -10.076 1.00 40.31 ?  465 HOH   A O    1 
HETATM 6832 O O    . HOH   E 4 .   ? 29.888 -16.000 10.727  1.00 38.59 ?  466 HOH   A O    1 
HETATM 6833 O O    . HOH   E 4 .   ? 24.854 5.659   20.703  1.00 55.79 ?  467 HOH   A O    1 
HETATM 6834 O O    . HOH   E 4 .   ? 27.745 7.067   -6.487  1.00 37.62 ?  468 HOH   A O    1 
HETATM 6835 O O    . HOH   E 4 .   ? 32.378 -15.903 10.825  1.00 34.67 ?  469 HOH   A O    1 
HETATM 6836 O O    . HOH   E 4 .   ? 25.360 8.244   -4.922  1.00 34.33 ?  470 HOH   A O    1 
HETATM 6837 O O    . HOH   E 4 .   ? 23.102 -22.262 -3.387  1.00 35.08 ?  471 HOH   A O    1 
HETATM 6838 O O    . HOH   E 4 .   ? 19.829 -17.308 -5.121  1.00 26.47 ?  472 HOH   A O    1 
HETATM 6839 O O    B HOH   E 4 .   ? 6.791  4.287   4.088   0.40 16.30 ?  473 HOH   A O    1 
HETATM 6840 O O    . HOH   E 4 .   ? 24.613 14.692  7.737   1.00 38.80 ?  474 HOH   A O    1 
HETATM 6841 O O    . HOH   E 4 .   ? 39.660 -7.096  -3.624  1.00 46.16 ?  475 HOH   A O    1 
HETATM 6842 O O    . HOH   E 4 .   ? 21.929 5.163   -5.934  1.00 39.49 ?  476 HOH   A O    1 
HETATM 6843 O O    . HOH   E 4 .   ? 18.833 11.020  11.243  1.00 31.95 ?  477 HOH   A O    1 
HETATM 6844 O O    . HOH   E 4 .   ? 27.443 -11.295 16.553  1.00 37.19 ?  478 HOH   A O    1 
HETATM 6845 O O    . HOH   E 4 .   ? 12.032 -13.376 16.337  1.00 55.82 ?  479 HOH   A O    1 
HETATM 6846 O O    . HOH   E 4 .   ? 26.829 11.669  -1.379  1.00 34.69 ?  480 HOH   A O    1 
HETATM 6847 O O    . HOH   E 4 .   ? 23.448 13.758  5.487   1.00 20.44 ?  481 HOH   A O    1 
HETATM 6848 O O    . HOH   E 4 .   ? 15.779 -21.513 3.706   1.00 25.25 ?  482 HOH   A O    1 
HETATM 6849 O O    . HOH   E 4 .   ? 12.352 1.524   17.309  1.00 42.83 ?  483 HOH   A O    1 
HETATM 6850 O O    . HOH   E 4 .   ? 28.618 -4.713  -12.334 1.00 34.05 ?  484 HOH   A O    1 
HETATM 6851 O O    . HOH   E 4 .   ? 15.707 -16.961 -7.014  1.00 33.93 ?  485 HOH   A O    1 
HETATM 6852 O O    . HOH   E 4 .   ? 13.973 -10.333 -11.015 1.00 35.05 ?  486 HOH   A O    1 
HETATM 6853 O O    . HOH   E 4 .   ? 25.768 10.794  -3.773  1.00 26.17 ?  487 HOH   A O    1 
HETATM 6854 O O    . HOH   E 4 .   ? 11.026 -15.082 -6.119  1.00 38.46 ?  488 HOH   A O    1 
HETATM 6855 O O    . HOH   E 4 .   ? 18.010 -16.241 -8.866  1.00 39.35 ?  489 HOH   A O    1 
HETATM 6856 O O    . HOH   E 4 .   ? 16.910 -20.482 16.101  1.00 31.13 ?  490 HOH   A O    1 
HETATM 6857 O O    . HOH   E 4 .   ? 28.974 9.010   17.500  1.00 38.09 ?  491 HOH   A O    1 
HETATM 6858 O O    . HOH   E 4 .   ? 35.266 7.469   12.196  1.00 45.34 ?  492 HOH   A O    1 
HETATM 6859 O O    . HOH   E 4 .   ? 20.480 -16.076 -7.448  1.00 27.41 ?  493 HOH   A O    1 
HETATM 6860 O O    . HOH   E 4 .   ? 41.027 -3.944  -0.417  1.00 37.89 ?  494 HOH   A O    1 
HETATM 6861 O O    . HOH   E 4 .   ? 28.609 -8.058  -15.321 1.00 51.90 ?  495 HOH   A O    1 
HETATM 6862 O O    . HOH   E 4 .   ? 17.306 -18.705 19.857  1.00 50.46 ?  496 HOH   A O    1 
HETATM 6863 O O    . HOH   E 4 .   ? 30.892 0.637   19.150  1.00 41.79 ?  497 HOH   A O    1 
HETATM 6864 O O    . HOH   E 4 .   ? 31.477 -0.549  -10.621 1.00 30.99 ?  498 HOH   A O    1 
HETATM 6865 O O    . HOH   E 4 .   ? 23.093 11.864  -4.102  1.00 21.04 ?  499 HOH   A O    1 
HETATM 6866 O O    . HOH   E 4 .   ? 41.725 9.318   -4.142  1.00 29.89 ?  500 HOH   A O    1 
HETATM 6867 O O    . HOH   E 4 .   ? 39.162 2.491   7.439   1.00 33.28 ?  501 HOH   A O    1 
HETATM 6868 O O    . HOH   E 4 .   ? 44.528 10.490  -1.620  1.00 32.19 ?  502 HOH   A O    1 
HETATM 6869 O O    . HOH   E 4 .   ? 23.358 -12.855 19.380  1.00 43.76 ?  503 HOH   A O    1 
HETATM 6870 O O    . HOH   E 4 .   ? 18.309 -23.108 1.902   1.00 44.75 ?  504 HOH   A O    1 
HETATM 6871 O O    . HOH   E 4 .   ? 15.980 -6.710  -11.889 1.00 48.39 ?  505 HOH   A O    1 
HETATM 6872 O O    . HOH   E 4 .   ? 13.838 -25.186 8.948   1.00 35.68 ?  506 HOH   A O    1 
HETATM 6873 O O    . HOH   E 4 .   ? 40.511 -0.277  -7.856  1.00 36.83 ?  507 HOH   A O    1 
HETATM 6874 O O    . HOH   E 4 .   ? 16.234 -23.379 5.807   1.00 31.22 ?  508 HOH   A O    1 
HETATM 6875 O O    . HOH   E 4 .   ? 19.999 -22.297 4.155   1.00 28.19 ?  509 HOH   A O    1 
HETATM 6876 O O    . HOH   E 4 .   ? 37.383 -6.590  7.533   1.00 24.23 ?  510 HOH   A O    1 
HETATM 6877 O O    . HOH   E 4 .   ? 23.116 -23.727 1.609   1.00 32.69 ?  511 HOH   A O    1 
HETATM 6878 O O    B HOH   E 4 .   ? 14.641 7.966   4.954   0.40 20.28 ?  512 HOH   A O    1 
HETATM 6879 O O    . HOH   E 4 .   ? 30.745 -5.771  -11.976 1.00 55.98 ?  513 HOH   A O    1 
HETATM 6880 O O    . HOH   E 4 .   ? 39.496 0.077   6.576   1.00 29.85 ?  514 HOH   A O    1 
HETATM 6881 O O    . HOH   E 4 .   ? 28.927 14.402  0.842   1.00 47.74 ?  515 HOH   A O    1 
HETATM 6882 O O    . HOH   E 4 .   ? 38.018 13.903  6.836   1.00 48.00 ?  516 HOH   A O    1 
HETATM 6883 O O    . HOH   E 4 .   ? 30.690 5.846   -14.790 1.00 37.52 ?  517 HOH   A O    1 
HETATM 6884 O O    . HOH   E 4 .   ? 21.988 -23.968 4.439   1.00 27.73 ?  518 HOH   A O    1 
HETATM 6885 O O    B HOH   E 4 .   ? 9.378  0.561   -5.509  0.40 27.29 ?  519 HOH   A O    1 
HETATM 6886 O O    . HOH   E 4 .   ? 36.422 -6.524  10.167  1.00 46.59 ?  520 HOH   A O    1 
HETATM 6887 O O    A HOH   E 4 .   ? 17.471 -6.502  -14.201 0.60 32.42 ?  521 HOH   A O    1 
HETATM 6888 O O    T HOH   E 4 .   ? 11.910 -2.113  -3.683  0.20 11.41 ?  522 HOH   A O    1 
HETATM 6889 O O    A HOH   E 4 .   ? 14.844 8.697   4.845   0.60 37.77 ?  523 HOH   A O    1 
HETATM 6890 O O    . HOH   E 4 .   ? 24.087 9.124   -7.197  1.00 42.02 ?  524 HOH   A O    1 
HETATM 6891 O O    . HOH   E 4 .   ? 16.342 -21.131 18.710  1.00 40.94 ?  525 HOH   A O    1 
HETATM 6892 O O    . HOH   E 4 .   ? 15.746 -12.172 27.497  1.00 47.50 ?  526 HOH   A O    1 
HETATM 6893 O O    . HOH   E 4 .   ? 14.710 -22.691 19.917  1.00 41.01 ?  527 HOH   A O    1 
HETATM 6894 O O    . HOH   F 4 .   ? 29.789 -22.380 5.487   1.00 22.69 ?  201 HOH   B O    1 
HETATM 6895 O O    . HOH   F 4 .   ? 52.893 -13.488 -20.417 1.00 36.04 ?  202 HOH   B O    1 
HETATM 6896 O O    . HOH   F 4 .   ? 41.420 -7.762  5.417   1.00 41.70 ?  203 HOH   B O    1 
HETATM 6897 O O    . HOH   F 4 .   ? 47.401 -7.438  -4.035  1.00 40.95 ?  204 HOH   B O    1 
HETATM 6898 O O    . HOH   F 4 .   ? 41.833 -36.094 -17.119 1.00 31.88 ?  205 HOH   B O    1 
HETATM 6899 O O    . HOH   F 4 .   ? 48.155 -6.905  15.558  1.00 30.66 ?  206 HOH   B O    1 
HETATM 6900 O O    . HOH   F 4 .   ? 37.968 -39.407 -0.094  1.00 40.84 ?  207 HOH   B O    1 
HETATM 6901 O O    . HOH   F 4 .   ? 27.680 -29.168 -1.840  1.00 36.43 ?  208 HOH   B O    1 
HETATM 6902 O O    . HOH   F 4 .   ? 49.390 -22.714 -19.685 1.00 50.26 ?  209 HOH   B O    1 
HETATM 6903 O O    . HOH   F 4 .   ? 37.181 -19.816 -18.145 1.00 41.53 ?  210 HOH   B O    1 
HETATM 6904 O O    . HOH   F 4 .   ? 30.215 -41.046 -8.075  1.00 18.38 ?  211 HOH   B O    1 
HETATM 6905 O O    . HOH   F 4 .   ? 29.839 -26.250 4.002   1.00 30.16 ?  212 HOH   B O    1 
HETATM 6906 O O    . HOH   F 4 .   ? 54.488 -9.386  -8.790  1.00 20.21 ?  213 HOH   B O    1 
HETATM 6907 O O    . HOH   F 4 .   ? 50.226 -3.288  7.143   1.00 36.98 ?  214 HOH   B O    1 
HETATM 6908 O O    . HOH   F 4 .   ? 59.154 -18.732 6.869   1.00 37.04 ?  215 HOH   B O    1 
HETATM 6909 O O    . HOH   F 4 .   ? 55.534 -16.625 -14.411 1.00 35.29 ?  216 HOH   B O    1 
HETATM 6910 O O    . HOH   F 4 .   ? 57.743 -24.472 5.066   1.00 36.41 ?  217 HOH   B O    1 
HETATM 6911 O O    . HOH   F 4 .   ? 56.637 -30.800 -7.747  1.00 34.85 ?  218 HOH   B O    1 
HETATM 6912 O O    . HOH   F 4 .   ? 56.365 -19.715 7.266   1.00 33.67 ?  219 HOH   B O    1 
HETATM 6913 O O    . HOH   F 4 .   ? 58.206 -12.870 8.373   1.00 32.81 ?  220 HOH   B O    1 
HETATM 6914 O O    . HOH   F 4 .   ? 57.198 -26.904 -7.615  1.00 40.05 ?  221 HOH   B O    1 
HETATM 6915 O O    . HOH   F 4 .   ? 44.443 -7.220  2.072   1.00 32.84 ?  222 HOH   B O    1 
HETATM 6916 O O    . HOH   F 4 .   ? 50.782 -6.084  0.193   1.00 28.08 ?  223 HOH   B O    1 
HETATM 6917 O O    . HOH   F 4 .   ? 34.511 -36.373 -7.172  1.00 19.89 ?  224 HOH   B O    1 
HETATM 6918 O O    . HOH   F 4 .   ? 27.836 -41.927 -15.160 1.00 34.32 ?  225 HOH   B O    1 
HETATM 6919 O O    . HOH   F 4 .   ? 45.124 -34.925 6.907   1.00 45.44 ?  226 HOH   B O    1 
HETATM 6920 O O    . HOH   F 4 .   ? 46.418 -1.556  13.239  1.00 31.19 ?  227 HOH   B O    1 
HETATM 6921 O O    . HOH   F 4 .   ? 29.800 -34.190 -0.359  1.00 37.98 ?  228 HOH   B O    1 
HETATM 6922 O O    . HOH   F 4 .   ? 32.821 -43.819 -11.339 1.00 21.59 ?  229 HOH   B O    1 
HETATM 6923 O O    . HOH   F 4 .   ? 35.943 -43.287 -8.412  1.00 33.86 ?  230 HOH   B O    1 
HETATM 6924 O O    . HOH   F 4 .   ? 30.834 -28.726 4.322   1.00 28.70 ?  231 HOH   B O    1 
HETATM 6925 O O    . HOH   F 4 .   ? 57.438 -16.298 -12.210 1.00 19.81 ?  232 HOH   B O    1 
HETATM 6926 O O    . HOH   F 4 .   ? 44.932 -43.585 -10.385 1.00 28.76 ?  233 HOH   B O    1 
HETATM 6927 O O    . HOH   F 4 .   ? 35.058 -7.989  -2.970  1.00 19.56 ?  234 HOH   B O    1 
HETATM 6928 O O    . HOH   F 4 .   ? 41.345 -9.583  13.081  1.00 24.62 ?  235 HOH   B O    1 
HETATM 6929 O O    . HOH   F 4 .   ? 51.748 -6.457  4.361   1.00 21.70 ?  236 HOH   B O    1 
HETATM 6930 O O    . HOH   F 4 .   ? 34.243 -18.411 11.381  1.00 25.05 ?  237 HOH   B O    1 
HETATM 6931 O O    . HOH   F 4 .   ? 39.312 -10.884 6.115   1.00 25.28 ?  238 HOH   B O    1 
HETATM 6932 O O    . HOH   F 4 .   ? 25.403 -25.920 -1.287  1.00 32.79 ?  239 HOH   B O    1 
HETATM 6933 O O    . HOH   F 4 .   ? 50.714 -12.966 -0.494  1.00 13.39 ?  240 HOH   B O    1 
HETATM 6934 O O    . HOH   F 4 .   ? 39.482 -11.107 0.315   1.00 17.59 ?  241 HOH   B O    1 
HETATM 6935 O O    . HOH   F 4 .   ? 48.045 -24.535 -17.704 1.00 32.34 ?  242 HOH   B O    1 
HETATM 6936 O O    . HOH   F 4 .   ? 51.552 -13.800 11.003  1.00 25.86 ?  243 HOH   B O    1 
HETATM 6937 O O    . HOH   F 4 .   ? 43.237 -32.456 -16.964 1.00 24.79 ?  244 HOH   B O    1 
HETATM 6938 O O    . HOH   F 4 .   ? 42.537 -25.346 2.665   1.00 16.88 ?  245 HOH   B O    1 
HETATM 6939 O O    . HOH   F 4 .   ? 42.599 -22.846 3.843   1.00 13.77 ?  246 HOH   B O    1 
HETATM 6940 O O    . HOH   F 4 .   ? 43.055 -43.266 -8.117  1.00 29.37 ?  247 HOH   B O    1 
HETATM 6941 O O    . HOH   F 4 .   ? 44.490 -27.688 -0.670  1.00 24.42 ?  248 HOH   B O    1 
HETATM 6942 O O    . HOH   F 4 .   ? 41.512 -39.202 -14.864 1.00 24.41 ?  249 HOH   B O    1 
HETATM 6943 O O    . HOH   F 4 .   ? 41.841 -23.459 9.291   1.00 19.43 ?  250 HOH   B O    1 
HETATM 6944 O O    . HOH   F 4 .   ? 50.938 -39.972 -8.124  1.00 33.80 ?  251 HOH   B O    1 
HETATM 6945 O O    . HOH   F 4 .   ? 28.389 -19.724 -13.185 1.00 25.39 ?  252 HOH   B O    1 
HETATM 6946 O O    . HOH   F 4 .   ? 38.934 -11.961 12.380  1.00 39.90 ?  253 HOH   B O    1 
HETATM 6947 O O    . HOH   F 4 .   ? 57.611 -24.387 -3.822  1.00 22.35 ?  254 HOH   B O    1 
HETATM 6948 O O    . HOH   F 4 .   ? 27.120 -31.851 -9.954  1.00 21.95 ?  255 HOH   B O    1 
HETATM 6949 O O    . HOH   F 4 .   ? 38.457 -11.040 -2.274  1.00 20.06 ?  256 HOH   B O    1 
HETATM 6950 O O    . HOH   F 4 .   ? 29.726 -25.250 -10.814 1.00 18.25 ?  257 HOH   B O    1 
HETATM 6951 O O    . HOH   F 4 .   ? 47.959 -22.721 5.831   1.00 19.19 ?  258 HOH   B O    1 
HETATM 6952 O O    . HOH   F 4 .   ? 40.678 -15.964 14.192  1.00 27.04 ?  259 HOH   B O    1 
HETATM 6953 O O    . HOH   F 4 .   ? 40.304 -12.764 -11.542 1.00 16.54 ?  260 HOH   B O    1 
HETATM 6954 O O    . HOH   F 4 .   ? 42.273 -10.157 -14.918 1.00 38.20 ?  261 HOH   B O    1 
HETATM 6955 O O    . HOH   F 4 .   ? 58.167 -10.632 -4.110  1.00 21.23 ?  262 HOH   B O    1 
HETATM 6956 O O    . HOH   F 4 .   ? 43.532 -15.381 18.243  1.00 34.94 ?  263 HOH   B O    1 
HETATM 6957 O O    . HOH   F 4 .   ? 34.910 -24.561 13.856  1.00 33.82 ?  264 HOH   B O    1 
HETATM 6958 O O    . HOH   F 4 .   ? 30.833 -15.696 2.647   1.00 15.21 ?  265 HOH   B O    1 
HETATM 6959 O O    . HOH   F 4 .   ? 31.745 -17.893 -14.538 1.00 31.99 ?  266 HOH   B O    1 
HETATM 6960 O O    . HOH   F 4 .   ? 59.785 -15.172 8.083   1.00 34.34 ?  267 HOH   B O    1 
HETATM 6961 O O    . HOH   F 4 .   ? 30.570 -42.257 -10.576 1.00 30.60 ?  268 HOH   B O    1 
HETATM 6962 O O    . HOH   F 4 .   ? 56.172 -23.566 -14.644 1.00 28.09 ?  269 HOH   B O    1 
HETATM 6963 O O    . HOH   F 4 .   ? 49.834 -0.482  10.218  1.00 29.97 ?  270 HOH   B O    1 
HETATM 6964 O O    . HOH   F 4 .   ? 28.263 -34.389 -9.409  1.00 19.98 ?  271 HOH   B O    1 
HETATM 6965 O O    . HOH   F 4 .   ? 43.346 -15.818 -12.185 1.00 15.53 ?  272 HOH   B O    1 
HETATM 6966 O O    . HOH   F 4 .   ? 42.329 -34.695 3.772   1.00 26.62 ?  273 HOH   B O    1 
HETATM 6967 O O    . HOH   F 4 .   ? 34.975 -33.433 -19.133 1.00 31.03 ?  274 HOH   B O    1 
HETATM 6968 O O    . HOH   F 4 .   ? 57.469 -9.198  1.367   1.00 21.22 ?  275 HOH   B O    1 
HETATM 6969 O O    . HOH   F 4 .   ? 49.321 -28.704 -6.838  1.00 16.87 ?  276 HOH   B O    1 
HETATM 6970 O O    . HOH   F 4 .   ? 56.946 -8.643  8.419   1.00 20.69 ?  277 HOH   B O    1 
HETATM 6971 O O    . HOH   F 4 .   ? 42.325 -9.817  9.364   1.00 22.59 ?  278 HOH   B O    1 
HETATM 6972 O O    . HOH   F 4 .   ? 27.946 -22.896 -8.015  1.00 19.01 ?  279 HOH   B O    1 
HETATM 6973 O O    . HOH   F 4 .   ? 28.482 -30.910 -14.666 1.00 30.56 ?  280 HOH   B O    1 
HETATM 6974 O O    . HOH   F 4 .   ? 46.845 -29.524 9.837   1.00 32.82 ?  281 HOH   B O    1 
HETATM 6975 O O    . HOH   F 4 .   ? 48.473 -36.562 -15.516 1.00 47.50 ?  282 HOH   B O    1 
HETATM 6976 O O    . HOH   F 4 .   ? 47.060 -34.005 -4.584  1.00 19.27 ?  283 HOH   B O    1 
HETATM 6977 O O    . HOH   F 4 .   ? 41.122 -5.504  11.508  1.00 46.76 ?  284 HOH   B O    1 
HETATM 6978 O O    . HOH   F 4 .   ? 50.060 -24.571 5.835   1.00 33.22 ?  285 HOH   B O    1 
HETATM 6979 O O    . HOH   F 4 .   ? 46.594 -31.248 -4.722  1.00 22.32 ?  286 HOH   B O    1 
HETATM 6980 O O    . HOH   F 4 .   ? 34.421 -12.740 2.562   1.00 25.07 ?  287 HOH   B O    1 
HETATM 6981 O O    . HOH   F 4 .   ? 48.687 -19.982 5.923   1.00 15.22 ?  288 HOH   B O    1 
HETATM 6982 O O    . HOH   F 4 .   ? 48.387 -25.034 3.134   1.00 14.66 ?  289 HOH   B O    1 
HETATM 6983 O O    . HOH   F 4 .   ? 52.611 -10.358 12.995  1.00 23.98 ?  290 HOH   B O    1 
HETATM 6984 O O    . HOH   F 4 .   ? 33.495 -15.341 -13.946 1.00 22.36 ?  291 HOH   B O    1 
HETATM 6985 O O    . HOH   F 4 .   ? 27.549 -26.704 -15.627 1.00 33.00 ?  292 HOH   B O    1 
HETATM 6986 O O    . HOH   F 4 .   ? 45.390 -33.434 -15.869 1.00 25.09 ?  293 HOH   B O    1 
HETATM 6987 O O    . HOH   F 4 .   ? 37.572 -18.046 13.096  1.00 31.47 ?  294 HOH   B O    1 
HETATM 6988 O O    . HOH   F 4 .   ? 37.306 -35.638 7.256   1.00 35.13 ?  295 HOH   B O    1 
HETATM 6989 O O    . HOH   F 4 .   ? 36.786 -12.737 -1.511  1.00 28.46 ?  296 HOH   B O    1 
HETATM 6990 O O    . HOH   F 4 .   ? 45.896 -40.400 -3.489  1.00 33.09 ?  297 HOH   B O    1 
HETATM 6991 O O    . HOH   F 4 .   ? 44.596 -27.433 2.040   1.00 17.07 ?  298 HOH   B O    1 
HETATM 6992 O O    . HOH   F 4 .   ? 51.237 -37.660 -9.502  1.00 27.45 ?  299 HOH   B O    1 
HETATM 6993 O O    . HOH   F 4 .   ? 44.013 -29.353 -4.650  1.00 24.87 ?  300 HOH   B O    1 
HETATM 6994 O O    . HOH   F 4 .   ? 52.576 -35.687 -8.528  1.00 29.87 ?  301 HOH   B O    1 
HETATM 6995 O O    . HOH   F 4 .   ? 42.740 -12.327 -18.567 1.00 31.70 ?  302 HOH   B O    1 
HETATM 6996 O O    . HOH   F 4 .   ? 53.482 -30.153 4.560   1.00 20.10 ?  303 HOH   B O    1 
HETATM 6997 O O    . HOH   F 4 .   ? 42.877 -20.357 -20.811 1.00 38.80 ?  304 HOH   B O    1 
HETATM 6998 O O    . HOH   F 4 .   ? 57.037 -12.032 12.402  1.00 40.09 ?  305 HOH   B O    1 
HETATM 6999 O O    . HOH   F 4 .   ? 25.919 -21.475 -3.540  1.00 17.58 ?  306 HOH   B O    1 
HETATM 7000 O O    . HOH   F 4 .   ? 40.241 -10.840 -9.588  1.00 18.44 ?  307 HOH   B O    1 
HETATM 7001 O O    . HOH   F 4 .   ? 53.290 -16.183 -12.682 1.00 30.78 ?  308 HOH   B O    1 
HETATM 7002 O O    . HOH   F 4 .   ? 62.735 -13.608 4.719   1.00 28.28 ?  309 HOH   B O    1 
HETATM 7003 O O    . HOH   F 4 .   ? 34.989 -33.476 4.557   1.00 27.78 ?  310 HOH   B O    1 
HETATM 7004 O O    . HOH   F 4 .   ? 37.854 -10.261 -10.809 1.00 18.67 ?  311 HOH   B O    1 
HETATM 7005 O O    . HOH   F 4 .   ? 48.083 -32.670 -16.531 1.00 43.32 ?  312 HOH   B O    1 
HETATM 7006 O O    . HOH   F 4 .   ? 41.729 -8.033  1.323   1.00 24.31 ?  313 HOH   B O    1 
HETATM 7007 O O    . HOH   F 4 .   ? 52.516 -29.262 -13.036 1.00 26.33 ?  314 HOH   B O    1 
HETATM 7008 O O    . HOH   F 4 .   ? 26.318 -21.017 -6.235  1.00 18.07 ?  315 HOH   B O    1 
HETATM 7009 O O    . HOH   F 4 .   ? 37.219 -30.625 -20.994 1.00 35.81 ?  316 HOH   B O    1 
HETATM 7010 O O    . HOH   F 4 .   ? 32.790 -34.597 -5.877  1.00 18.56 ?  317 HOH   B O    1 
HETATM 7011 O O    . HOH   F 4 .   ? 43.183 -21.369 10.704  1.00 17.88 ?  318 HOH   B O    1 
HETATM 7012 O O    . HOH   F 4 .   ? 44.557 -24.552 9.608   1.00 20.84 ?  319 HOH   B O    1 
HETATM 7013 O O    . HOH   F 4 .   ? 53.628 -12.590 -22.298 1.00 37.66 ?  320 HOH   B O    1 
HETATM 7014 O O    . HOH   F 4 .   ? 41.169 -24.506 15.781  1.00 47.08 ?  321 HOH   B O    1 
HETATM 7015 O O    . HOH   F 4 .   ? 44.148 -1.674  7.691   1.00 46.47 ?  322 HOH   B O    1 
HETATM 7016 O O    . HOH   F 4 .   ? 36.719 -12.393 4.249   1.00 19.08 ?  323 HOH   B O    1 
HETATM 7017 O O    . HOH   F 4 .   ? 51.394 -32.955 -10.689 1.00 40.12 ?  324 HOH   B O    1 
HETATM 7018 O O    . HOH   F 4 .   ? 38.370 -9.396  -13.341 1.00 28.11 ?  325 HOH   B O    1 
HETATM 7019 O O    . HOH   F 4 .   ? 38.338 -12.709 7.858   1.00 19.39 ?  326 HOH   B O    1 
HETATM 7020 O O    . HOH   F 4 .   ? 62.887 -20.145 -0.777  1.00 37.23 ?  327 HOH   B O    1 
HETATM 7021 O O    . HOH   F 4 .   ? 59.944 -17.231 -10.512 1.00 34.67 ?  328 HOH   B O    1 
HETATM 7022 O O    . HOH   F 4 .   ? 47.147 -24.436 8.246   1.00 29.17 ?  329 HOH   B O    1 
HETATM 7023 O O    . HOH   F 4 .   ? 51.729 -6.022  -7.898  1.00 51.32 ?  330 HOH   B O    1 
HETATM 7024 O O    . HOH   F 4 .   ? 33.608 -31.126 11.057  1.00 33.93 ?  331 HOH   B O    1 
HETATM 7025 O O    . HOH   F 4 .   ? 27.930 -14.769 -9.456  1.00 35.42 ?  332 HOH   B O    1 
HETATM 7026 O O    . HOH   F 4 .   ? 48.605 -11.968 -13.997 1.00 26.77 ?  333 HOH   B O    1 
HETATM 7027 O O    . HOH   F 4 .   ? 42.957 -43.491 -14.313 1.00 42.86 ?  334 HOH   B O    1 
HETATM 7028 O O    . HOH   F 4 .   ? 57.585 -22.017 3.332   1.00 30.90 ?  335 HOH   B O    1 
HETATM 7029 O O    . HOH   F 4 .   ? 43.102 -34.667 0.162   1.00 21.16 ?  336 HOH   B O    1 
HETATM 7030 O O    . HOH   F 4 .   ? 47.460 -27.416 2.046   1.00 16.47 ?  337 HOH   B O    1 
HETATM 7031 O O    . HOH   F 4 .   ? 45.781 -36.311 -16.013 1.00 36.22 ?  338 HOH   B O    1 
HETATM 7032 O O    . HOH   F 4 .   ? 39.453 -23.540 -20.332 1.00 38.73 ?  339 HOH   B O    1 
HETATM 7033 O O    . HOH   F 4 .   ? 46.836 -19.827 12.253  1.00 31.43 ?  340 HOH   B O    1 
HETATM 7034 O O    . HOH   F 4 .   ? 37.011 -15.121 -16.519 1.00 41.44 ?  341 HOH   B O    1 
HETATM 7035 O O    . HOH   F 4 .   ? 28.864 -42.959 -12.384 1.00 40.14 ?  342 HOH   B O    1 
HETATM 7036 O O    . HOH   F 4 .   ? 37.041 -45.247 -9.690  1.00 37.07 ?  343 HOH   B O    1 
HETATM 7037 O O    . HOH   F 4 .   ? 38.463 -12.223 -16.265 1.00 46.94 ?  344 HOH   B O    1 
HETATM 7038 O O    . HOH   F 4 .   ? 32.979 -14.646 1.050   1.00 19.94 ?  345 HOH   B O    1 
HETATM 7039 O O    . HOH   F 4 .   ? 38.545 -22.381 14.995  1.00 41.56 ?  346 HOH   B O    1 
HETATM 7040 O O    . HOH   F 4 .   ? 39.772 -44.354 -11.149 1.00 38.75 ?  347 HOH   B O    1 
HETATM 7041 O O    . HOH   F 4 .   ? 62.486 -20.060 -4.826  1.00 44.61 ?  348 HOH   B O    1 
HETATM 7042 O O    . HOH   F 4 .   ? 34.550 -10.290 7.584   1.00 24.01 ?  349 HOH   B O    1 
HETATM 7043 O O    . HOH   F 4 .   ? 33.723 -9.371  -8.839  1.00 32.59 ?  350 HOH   B O    1 
HETATM 7044 O O    . HOH   F 4 .   ? 40.414 -43.504 -9.070  1.00 27.26 ?  351 HOH   B O    1 
HETATM 7045 O O    . HOH   F 4 .   ? 27.712 -26.593 -0.565  1.00 31.60 ?  352 HOH   B O    1 
HETATM 7046 O O    . HOH   F 4 .   ? 55.615 -8.256  10.848  1.00 28.34 ?  353 HOH   B O    1 
HETATM 7047 O O    . HOH   F 4 .   ? 36.039 -8.651  -9.703  1.00 36.26 ?  354 HOH   B O    1 
HETATM 7048 O O    . HOH   F 4 .   ? 23.197 -23.604 6.771   1.00 36.72 ?  355 HOH   B O    1 
HETATM 7049 O O    . HOH   F 4 .   ? 44.144 -37.315 -17.705 1.00 34.97 ?  356 HOH   B O    1 
HETATM 7050 O O    . HOH   F 4 .   ? 56.583 -7.232  3.027   1.00 27.75 ?  357 HOH   B O    1 
HETATM 7051 O O    . HOH   F 4 .   ? 34.065 -7.748  11.455  1.00 41.07 ?  358 HOH   B O    1 
HETATM 7052 O O    . HOH   F 4 .   ? 61.561 -19.831 1.718   1.00 38.95 ?  359 HOH   B O    1 
HETATM 7053 O O    . HOH   F 4 .   ? 43.130 -12.732 -21.244 1.00 42.68 ?  360 HOH   B O    1 
HETATM 7054 O O    . HOH   F 4 .   ? 56.940 -21.548 -16.397 1.00 39.99 ?  361 HOH   B O    1 
HETATM 7055 O O    . HOH   F 4 .   ? 27.113 -26.015 -11.307 1.00 33.70 ?  362 HOH   B O    1 
HETATM 7056 O O    . HOH   F 4 .   ? 40.303 -8.739  9.826   1.00 41.68 ?  363 HOH   B O    1 
HETATM 7057 O O    . HOH   F 4 .   ? 48.273 -26.560 8.944   1.00 39.33 ?  364 HOH   B O    1 
HETATM 7058 O O    . HOH   F 4 .   ? 40.201 -11.384 -13.996 1.00 31.13 ?  365 HOH   B O    1 
HETATM 7059 O O    . HOH   F 4 .   ? 54.204 -5.759  2.956   1.00 35.69 ?  366 HOH   B O    1 
HETATM 7060 O O    . HOH   F 4 .   ? 32.488 -23.598 14.113  1.00 40.27 ?  367 HOH   B O    1 
HETATM 7061 O O    . HOH   F 4 .   ? 41.858 -10.130 -17.454 1.00 54.43 ?  368 HOH   B O    1 
HETATM 7062 O O    . HOH   F 4 .   ? 36.191 -8.675  8.931   1.00 34.30 ?  369 HOH   B O    1 
HETATM 7063 O O    . HOH   F 4 .   ? 58.904 -10.360 9.265   1.00 43.43 ?  370 HOH   B O    1 
HETATM 7064 O O    . HOH   F 4 .   ? 39.883 -7.003  7.822   1.00 42.13 ?  371 HOH   B O    1 
HETATM 7065 O O    . HOH   F 4 .   ? 51.999 -12.894 13.438  1.00 36.11 ?  372 HOH   B O    1 
HETATM 7066 O O    . HOH   F 4 .   ? 55.987 -7.754  -0.645  1.00 35.08 ?  373 HOH   B O    1 
HETATM 7067 O O    . HOH   F 4 .   ? 63.067 -12.397 6.905   1.00 37.21 ?  374 HOH   B O    1 
HETATM 7068 O O    . HOH   F 4 .   ? 38.055 -10.568 10.013  1.00 30.58 ?  375 HOH   B O    1 
HETATM 7069 O O    . HOH   F 4 .   ? 36.557 -22.763 13.332  1.00 35.00 ?  376 HOH   B O    1 
HETATM 7070 O O    . HOH   F 4 .   ? 44.212 -5.562  -3.539  1.00 45.47 ?  377 HOH   B O    1 
HETATM 7071 O O    . HOH   F 4 .   ? 41.802 -6.757  -4.912  1.00 45.95 ?  378 HOH   B O    1 
HETATM 7072 O O    . HOH   F 4 .   ? 42.553 -17.138 -23.142 1.00 48.53 ?  379 HOH   B O    1 
HETATM 7073 O O    . HOH   F 4 .   ? 40.163 -7.555  3.145   1.00 34.58 ?  380 HOH   B O    1 
HETATM 7074 O O    . HOH   F 4 .   ? 39.623 -14.010 15.732  1.00 50.25 ?  381 HOH   B O    1 
HETATM 7075 O O    . HOH   F 4 .   ? 52.871 -29.865 7.266   1.00 25.04 ?  382 HOH   B O    1 
HETATM 7076 O O    . HOH   F 4 .   ? 60.504 -22.300 2.868   1.00 49.88 ?  383 HOH   B O    1 
HETATM 7077 O O    . HOH   F 4 .   ? 35.344 -33.707 7.288   1.00 41.10 ?  384 HOH   B O    1 
HETATM 7078 O O    . HOH   F 4 .   ? 25.663 -18.818 -11.887 1.00 42.39 ?  385 HOH   B O    1 
HETATM 7079 O O    . HOH   F 4 .   ? 35.161 -20.293 13.230  1.00 34.67 ?  386 HOH   B O    1 
HETATM 7080 O O    . HOH   F 4 .   ? 23.909 -20.851 -7.704  1.00 29.65 ?  387 HOH   B O    1 
HETATM 7081 O O    . HOH   F 4 .   ? 40.908 -9.761  15.815  1.00 50.27 ?  388 HOH   B O    1 
HETATM 7082 O O    . HOH   F 4 .   ? 46.778 -5.278  2.884   1.00 42.20 ?  389 HOH   B O    1 
HETATM 7083 O O    . HOH   F 4 .   ? 40.692 -6.599  -0.890  1.00 24.64 ?  390 HOH   B O    1 
HETATM 7084 O O    . HOH   F 4 .   ? 44.078 -31.747 -3.745  1.00 36.87 ?  391 HOH   B O    1 
HETATM 7085 O O    . HOH   F 4 .   ? 26.674 -28.070 -13.519 1.00 35.39 ?  392 HOH   B O    1 
HETATM 7086 O O    . HOH   F 4 .   ? 27.840 -27.063 2.193   1.00 32.32 ?  393 HOH   B O    1 
HETATM 7087 O O    . HOH   F 4 .   ? 24.615 -20.650 -10.541 1.00 36.03 ?  394 HOH   B O    1 
HETATM 7088 O O    . HOH   F 4 .   ? 34.379 -33.402 9.692   1.00 34.70 ?  395 HOH   B O    1 
HETATM 7089 O O    . HOH   F 4 .   ? 26.833 -30.699 -12.635 1.00 30.10 ?  396 HOH   B O    1 
HETATM 7090 O O    . HOH   F 4 .   ? 50.650 -30.774 8.662   1.00 28.89 ?  397 HOH   B O    1 
HETATM 7091 O O    . HOH   F 4 .   ? 45.722 -20.228 15.196  1.00 53.17 ?  398 HOH   B O    1 
HETATM 7092 O O    . HOH   F 4 .   ? 57.577 -6.454  -2.353  1.00 35.09 ?  399 HOH   B O    1 
HETATM 7093 O O    . HOH   F 4 .   ? 40.930 -11.826 -22.330 1.00 43.53 ?  400 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.6799 0.6900 0.7237 -0.0152 -0.0388 0.0721  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6787 0.6881 0.7160 -0.0173 -0.0325 0.0624  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6775 0.6879 0.7162 -0.0160 -0.0388 0.0723  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6764 0.6862 0.7091 -0.0181 -0.0329 0.0635  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.6645 0.6784 0.6878 -0.0229 -0.0391 0.0770  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6641 0.6776 0.6845 -0.0240 -0.0356 0.0721  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.6673 0.6807 0.6937 -0.0210 -0.0401 0.0785  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6671 0.6801 0.6912 -0.0224 -0.0360 0.0727  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6856 0.6935 0.7283 -0.0114 -0.0375 0.0690  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.6841 0.6914 0.7189 -0.0141 -0.0304 0.0577  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6881 0.6957 0.7346 -0.0105 -0.0371 0.0681  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.6866 0.6935 0.7243 -0.0132 -0.0294 0.0558  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6883 0.6949 0.7350 -0.0090 -0.0368 0.0680  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.6865 0.6927 0.7245 -0.0121 -0.0293 0.0558  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.6463 0.6648 0.6433 -0.0323 -0.0374 0.0805  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.6090 0.6367 0.5563 -0.0508 -0.0366 0.0907  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.5647 0.6072 0.5102 -0.0663 -0.0285 0.0716  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.5684 0.6098 0.5022 -0.0668 -0.0306 0.0766  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.6145 0.6374 0.5128 -0.0540 -0.0431 0.1179  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.6193 0.6371 0.4733 -0.0576 -0.0477 0.1429  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.6223 0.6363 0.4548 -0.0590 -0.0496 0.1517  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.6203 0.6372 0.4587 -0.0583 -0.0505 0.1541  4   ASN   A ND2 
46   N N   . SER   A 5   ? 0.5144 0.5716 0.4697 -0.0832 -0.0200 0.0482  5   SER   A N   
47   C CA  . SER   A 5   ? 0.4637 0.5361 0.4357 -0.0974 -0.0110 0.0255  5   SER   A CA  
48   C C   . SER   A 5   ? 0.4096 0.4921 0.3664 -0.1055 0.0049  0.0146  5   SER   A C   
49   O O   . SER   A 5   ? 0.4159 0.5005 0.3669 -0.0983 0.0070  0.0031  5   SER   A O   
50   C CB  . SER   A 5   ? 0.4699 0.5438 0.4637 -0.1011 -0.0144 0.0164  5   SER   A CB  
51   O OG  . SER   A 5   ? 0.4736 0.5485 0.4837 -0.1044 -0.0153 0.0115  5   SER   A OG  
57   N N   . PHE   A 6   ? 0.3461 0.4372 0.3000 -0.1173 0.0231  0.0186  6   PHE   A N   
58   C CA  . PHE   A 6   ? 0.2916 0.3831 0.2515 -0.1192 0.0266  0.0255  6   PHE   A CA  
59   C C   . PHE   A 6   ? 0.2809 0.3707 0.2572 -0.1117 0.0419  0.0208  6   PHE   A C   
60   O O   . PHE   A 6   ? 0.2867 0.3808 0.2933 -0.1164 0.0429  0.0345  6   PHE   A O   
61   C CB  . PHE   A 6   ? 0.2685 0.3492 0.2120 -0.1112 0.0169  0.0394  6   PHE   A CB  
62   C CG  . PHE   A 6   ? 0.2501 0.3228 0.2064 -0.1014 0.0065  0.0365  6   PHE   A CG  
63   C CD1 . PHE   A 6   ? 0.2386 0.3087 0.2024 -0.0929 -0.0001 0.0307  6   PHE   A CD1 
64   C CD2 . PHE   A 6   ? 0.2565 0.3182 0.2229 -0.0857 0.0047  0.0388  6   PHE   A CD2 
65   C CE1 . PHE   A 6   ? 0.2393 0.3035 0.2131 -0.0888 0.0021  0.0354  6   PHE   A CE1 
66   C CE2 . PHE   A 6   ? 0.2539 0.3131 0.2234 -0.0786 0.0065  0.0322  6   PHE   A CE2 
67   C CZ  . PHE   A 6   ? 0.2486 0.3080 0.2183 -0.0820 -0.0025 0.0270  6   PHE   A CZ  
77   N N   A SER   A 7   ? 0.2698 0.3565 0.2407 -0.1054 0.0531  0.0148  7   SER   A N   
78   N N   B SER   A 7   ? 0.2761 0.3626 0.2539 -0.0995 0.0473  0.0107  7   SER   A N   
79   C CA  A SER   A 7   ? 0.2664 0.3457 0.2428 -0.0924 0.0573  0.0025  7   SER   A CA  
80   C CA  B SER   A 7   ? 0.2753 0.3556 0.2618 -0.0841 0.0481  -0.0015 7   SER   A CA  
81   C C   A SER   A 7   ? 0.2461 0.3077 0.2168 -0.0851 0.0664  0.0108  7   SER   A C   
82   C C   B SER   A 7   ? 0.2633 0.3322 0.2429 -0.0745 0.0532  0.0027  7   SER   A C   
83   O O   A SER   A 7   ? 0.2526 0.2959 0.2162 -0.0893 0.0626  0.0150  7   SER   A O   
84   O O   B SER   A 7   ? 0.2654 0.3287 0.2398 -0.0773 0.0537  0.0038  7   SER   A O   
85   C CB  A SER   A 7   ? 0.2874 0.3683 0.2782 -0.0817 0.0563  -0.0034 7   SER   A CB  
86   C CB  B SER   A 7   ? 0.2876 0.3691 0.2931 -0.0765 0.0465  -0.0078 7   SER   A CB  
87   O OG  A SER   A 7   ? 0.3055 0.3872 0.3081 -0.0735 0.0539  -0.0106 7   SER   A OG  
88   O OG  B SER   A 7   ? 0.2979 0.3791 0.3196 -0.0709 0.0432  -0.0125 7   SER   A OG  
99   N N   A GLY   A 8   ? 0.2217 0.2811 0.2160 -0.0729 0.0607  0.0033  8   GLY   A N   
100  N N   B GLY   A 8   ? 0.2488 0.3119 0.2375 -0.0629 0.0510  0.0027  8   GLY   A N   
101  C CA  A GLY   A 8   ? 0.2045 0.2570 0.2235 -0.0526 0.0480  0.0027  8   GLY   A CA  
102  C CA  B GLY   A 8   ? 0.2360 0.2906 0.2349 -0.0509 0.0419  0.0057  8   GLY   A CA  
103  C C   A GLY   A 8   ? 0.1779 0.2370 0.2217 -0.0359 0.0377  0.0054  8   GLY   A C   
104  C C   B GLY   A 8   ? 0.2178 0.2712 0.2274 -0.0408 0.0344  0.0123  8   GLY   A C   
105  O O   A GLY   A 8   ? 0.1752 0.2393 0.2351 -0.0167 0.0422  -0.0175 8   GLY   A O   
106  O O   B GLY   A 8   ? 0.2175 0.2748 0.2385 -0.0334 0.0320  0.0008  8   GLY   A O   
113  N N   A TYR   A 9   ? 0.1607 0.2204 0.2141 -0.0299 0.0363  0.0194  9   TYR   A N   
114  N N   B TYR   A 9   ? 0.2022 0.2523 0.2224 -0.0339 0.0326  0.0271  9   TYR   A N   
115  C CA  A TYR   A 9   ? 0.1471 0.2010 0.1959 -0.0320 0.0229  0.0222  9   TYR   A CA  
116  C CA  B TYR   A 9   ? 0.1876 0.2347 0.2072 -0.0312 0.0268  0.0344  9   TYR   A CA  
117  C C   A TYR   A 9   ? 0.1428 0.1853 0.1825 -0.0222 0.0216  0.0436  9   TYR   A C   
118  C C   B TYR   A 9   ? 0.1871 0.2237 0.2078 -0.0263 0.0238  0.0401  9   TYR   A C   
119  O O   A TYR   A 9   ? 0.1647 0.2027 0.2050 -0.0218 0.0112  0.0424  9   TYR   A O   
120  O O   B TYR   A 9   ? 0.1942 0.2346 0.2137 -0.0312 0.0185  0.0417  9   TYR   A O   
121  C CB  A TYR   A 9   ? 0.1466 0.2040 0.2057 -0.0275 0.0243  0.0108  9   TYR   A CB  
122  C CB  B TYR   A 9   ? 0.1772 0.2321 0.1987 -0.0259 0.0267  0.0342  9   TYR   A CB  
123  C CG  A TYR   A 9   ? 0.1518 0.1970 0.2048 -0.0137 0.0331  0.0011  9   TYR   A CG  
124  C CG  B TYR   A 9   ? 0.1687 0.2265 0.1881 -0.0155 0.0262  0.0266  9   TYR   A CG  
125  C CD1 A TYR   A 9   ? 0.1566 0.1971 0.2088 -0.0205 0.0350  -0.0040 9   TYR   A CD1 
126  C CD1 B TYR   A 9   ? 0.1681 0.2214 0.1948 -0.0141 0.0293  0.0257  9   TYR   A CD1 
127  C CD2 A TYR   A 9   ? 0.1569 0.1893 0.2107 -0.0092 0.0273  -0.0017 9   TYR   A CD2 
128  C CD2 B TYR   A 9   ? 0.1615 0.2220 0.1762 -0.0073 0.0231  0.0232  9   TYR   A CD2 
129  C CE1 A TYR   A 9   ? 0.1593 0.1949 0.2231 -0.0151 0.0397  -0.0107 9   TYR   A CE1 
130  C CE1 B TYR   A 9   ? 0.1623 0.2145 0.1907 -0.0113 0.0389  0.0226  9   TYR   A CE1 
131  C CE2 A TYR   A 9   ? 0.1585 0.1860 0.2236 -0.0112 0.0346  -0.0089 9   TYR   A CE2 
132  C CE2 B TYR   A 9   ? 0.1555 0.2153 0.1791 -0.0014 0.0341  0.0217  9   TYR   A CE2 
133  C CZ  A TYR   A 9   ? 0.1593 0.1900 0.2325 -0.0204 0.0500  -0.0088 9   TYR   A CZ  
134  C CZ  B TYR   A 9   ? 0.1519 0.2060 0.1894 -0.0061 0.0457  0.0187  9   TYR   A CZ  
135  O OH  A TYR   A 9   ? 0.1727 0.1991 0.2635 -0.0286 0.0553  -0.0141 9   TYR   A OH  
136  O OH  B TYR   A 9   ? 0.1494 0.1980 0.2146 -0.0096 0.0468  0.0153  9   TYR   A OH  
155  N N   A LEU   A 10  ? 0.1445 0.1685 0.1877 -0.0163 0.0201  0.0482  10  LEU   A N   
156  N N   B LEU   A 10  ? 0.1849 0.2097 0.2139 -0.0168 0.0177  0.0409  10  LEU   A N   
157  C CA  A LEU   A 10  ? 0.1385 0.1696 0.1942 -0.0230 0.0068  0.0570  10  LEU   A CA  
158  C CA  B LEU   A 10  ? 0.1855 0.2050 0.2258 -0.0121 0.0120  0.0383  10  LEU   A CA  
159  C C   A LEU   A 10  ? 0.1369 0.1633 0.2068 -0.0265 0.0016  0.0557  10  LEU   A C   
160  C C   B LEU   A 10  ? 0.1700 0.1855 0.2130 -0.0134 0.0082  0.0421  10  LEU   A C   
161  O O   A LEU   A 10  ? 0.1388 0.1453 0.2039 -0.0250 0.0102  0.0594  10  LEU   A O   
162  O O   B LEU   A 10  ? 0.1682 0.1749 0.2007 -0.0209 0.0194  0.0380  10  LEU   A O   
163  C CB  A LEU   A 10  ? 0.1410 0.1755 0.2107 -0.0203 -0.0167 0.0746  10  LEU   A CB  
164  C CB  B LEU   A 10  ? 0.2042 0.2261 0.2536 -0.0068 0.0045  0.0317  10  LEU   A CB  
165  C CG  A LEU   A 10  ? 0.1568 0.1792 0.2414 -0.0152 -0.0316 0.0783  10  LEU   A CG  
166  C CG  B LEU   A 10  ? 0.2222 0.2437 0.2827 0.0008  -0.0060 0.0185  10  LEU   A CG  
167  C CD1 A LEU   A 10  ? 0.1786 0.1831 0.2719 -0.0200 -0.0178 0.0784  10  LEU   A CD1 
168  C CD1 B LEU   A 10  ? 0.2274 0.2523 0.2881 0.0036  -0.0142 0.0213  10  LEU   A CD1 
169  C CD2 A LEU   A 10  ? 0.1778 0.1983 0.2538 -0.0089 -0.0188 0.0676  10  LEU   A CD2 
170  C CD2 B LEU   A 10  ? 0.2291 0.2478 0.3006 0.0055  0.0027  0.0145  10  LEU   A CD2 
193  N N   A LYS   A 11  ? 0.1401 0.1704 0.2158 -0.0352 0.0053  0.0667  11  LYS   A N   
194  N N   B LYS   A 11  ? 0.1656 0.1793 0.2230 -0.0129 0.0184  0.0508  11  LYS   A N   
195  C CA  A LYS   A 11  ? 0.1501 0.1702 0.2217 -0.0391 -0.0006 0.0552  11  LYS   A CA  
196  C CA  B LYS   A 11  ? 0.1683 0.1780 0.2377 -0.0096 0.0183  0.0544  11  LYS   A CA  
197  C C   A LYS   A 11  ? 0.1478 0.1827 0.2146 -0.0374 -0.0086 0.0515  11  LYS   A C   
198  C C   B LYS   A 11  ? 0.1550 0.1707 0.2311 -0.0166 0.0120  0.0608  11  LYS   A C   
199  O O   A LYS   A 11  ? 0.1540 0.2001 0.2211 -0.0531 -0.0095 0.0514  11  LYS   A O   
200  O O   B LYS   A 11  ? 0.1449 0.1684 0.2351 -0.0234 0.0052  0.0732  11  LYS   A O   
201  C CB  A LYS   A 11  ? 0.1597 0.1528 0.1964 -0.0441 0.0037  0.0336  11  LYS   A CB  
202  C CB  B LYS   A 11  ? 0.1830 0.1866 0.2437 -0.0012 0.0220  0.0495  11  LYS   A CB  
203  C CG  A LYS   A 11  ? 0.1581 0.1477 0.1812 -0.0532 -0.0012 0.0428  11  LYS   A CG  
204  C CG  B LYS   A 11  ? 0.1993 0.2074 0.2525 0.0046  0.0232  0.0491  11  LYS   A CG  
205  C CD  A LYS   A 11  ? 0.1788 0.1474 0.1805 -0.0403 -0.0009 0.0310  11  LYS   A CD  
206  C CD  B LYS   A 11  ? 0.2201 0.2258 0.2688 0.0094  0.0156  0.0443  11  LYS   A CD  
207  C CE  A LYS   A 11  ? 0.1776 0.1374 0.1896 -0.0379 -0.0076 0.0343  11  LYS   A CE  
208  C CE  B LYS   A 11  ? 0.2322 0.2400 0.2823 0.0086  0.0076  0.0408  11  LYS   A CE  
209  N NZ  A LYS   A 11  ? 0.1768 0.1484 0.2151 -0.0225 -0.0041 0.0399  11  LYS   A NZ  
210  N NZ  B LYS   A 11  ? 0.2342 0.2423 0.2900 0.0107  -0.0001 0.0414  11  LYS   A NZ  
237  N N   A LEU   A 12  ? 0.1399 0.1719 0.2021 -0.0388 -0.0131 0.0462  12  LEU   A N   
238  N N   B LEU   A 12  ? 0.1491 0.1705 0.2257 -0.0220 0.0093  0.0438  12  LEU   A N   
239  C CA  A LEU   A 12  ? 0.1428 0.1812 0.2089 -0.0256 -0.0148 0.0479  12  LEU   A CA  
240  C CA  B LEU   A 12  ? 0.1535 0.1806 0.2199 -0.0194 0.0079  0.0437  12  LEU   A CA  
241  C C   A LEU   A 12  ? 0.1461 0.1764 0.2044 -0.0303 -0.0048 0.0543  12  LEU   A C   
242  C C   B LEU   A 12  ? 0.1628 0.1779 0.2166 -0.0220 0.0049  0.0484  12  LEU   A C   
243  O O   A LEU   A 12  ? 0.1591 0.1832 0.2027 -0.0360 -0.0075 0.0431  12  LEU   A O   
244  O O   B LEU   A 12  ? 0.1707 0.1744 0.2020 -0.0268 0.0083  0.0654  12  LEU   A O   
245  C CB  A LEU   A 12  ? 0.1549 0.1760 0.2243 -0.0167 -0.0157 0.0505  12  LEU   A CB  
246  C CB  B LEU   A 12  ? 0.1502 0.1811 0.2223 -0.0216 0.0109  0.0417  12  LEU   A CB  
247  C CG  A LEU   A 12  ? 0.1680 0.1807 0.2544 -0.0106 0.0028  0.0562  12  LEU   A CG  
248  C CG  B LEU   A 12  ? 0.1550 0.1860 0.2429 -0.0204 0.0248  0.0399  12  LEU   A CG  
249  C CD1 A LEU   A 12  ? 0.1812 0.1777 0.2616 -0.0002 0.0105  0.0648  12  LEU   A CD1 
250  C CD1 B LEU   A 12  ? 0.1648 0.1920 0.2463 -0.0163 0.0298  0.0435  12  LEU   A CD1 
251  C CD2 A LEU   A 12  ? 0.1715 0.1806 0.2598 -0.0067 -0.0077 0.0618  12  LEU   A CD2 
252  C CD2 B LEU   A 12  ? 0.1535 0.1843 0.2482 -0.0180 0.0199  0.0365  12  LEU   A CD2 
275  N N   A THR   A 13  ? 0.1330 0.1631 0.2019 -0.0289 -0.0006 0.0468  13  THR   A N   
276  N N   B THR   A 13  ? 0.1634 0.1752 0.2266 -0.0208 0.0039  0.0397  13  THR   A N   
277  C CA  A THR   A 13  ? 0.1401 0.1625 0.2191 -0.0230 0.0046  0.0412  13  THR   A CA  
278  C CA  B THR   A 13  ? 0.1741 0.1761 0.2382 -0.0225 0.0037  0.0373  13  THR   A CA  
279  C C   A THR   A 13  ? 0.1424 0.1527 0.2232 -0.0230 -0.0007 0.0495  13  THR   A C   
280  C C   B THR   A 13  ? 0.1789 0.1745 0.2439 -0.0304 -0.0055 0.0456  13  THR   A C   
281  O O   A THR   A 13  ? 0.1390 0.1481 0.2128 -0.0085 -0.0011 0.0611  13  THR   A O   
282  O O   B THR   A 13  ? 0.1789 0.1628 0.2490 -0.0333 -0.0146 0.0535  13  THR   A O   
283  C CB  A THR   A 13  ? 0.1485 0.1729 0.2328 -0.0281 0.0031  0.0385  13  THR   A CB  
284  C CB  B THR   A 13  ? 0.1777 0.1803 0.2484 -0.0241 -0.0019 0.0292  13  THR   A CB  
285  O OG1 A THR   A 13  ? 0.1384 0.1725 0.2435 -0.0318 0.0051  0.0514  13  THR   A OG1 
286  O OG1 B THR   A 13  ? 0.1730 0.1790 0.2590 -0.0257 -0.0073 0.0307  13  THR   A OG1 
287  C CG2 A THR   A 13  ? 0.1629 0.1832 0.2379 -0.0326 0.0035  0.0249  13  THR   A CG2 
288  C CG2 B THR   A 13  ? 0.1905 0.1868 0.2509 -0.0216 0.0016  0.0187  13  THR   A CG2 
303  N N   A ASP   A 14  ? 0.1426 0.1516 0.2482 -0.0284 -0.0035 0.0579  14  ASP   A N   
304  N N   B ASP   A 14  ? 0.1775 0.1805 0.2595 -0.0314 -0.0093 0.0493  14  ASP   A N   
305  C CA  A ASP   A 14  ? 0.1424 0.1593 0.2605 -0.0127 0.0019  0.0634  14  ASP   A CA  
306  C CA  B ASP   A 14  ? 0.1799 0.1867 0.2628 -0.0248 -0.0076 0.0645  14  ASP   A CA  
307  C C   A ASP   A 14  ? 0.1480 0.1570 0.2461 -0.0115 0.0043  0.0511  14  ASP   A C   
308  C C   B ASP   A 14  ? 0.1653 0.1771 0.2374 -0.0289 -0.0124 0.0739  14  ASP   A C   
309  O O   A ASP   A 14  ? 0.1665 0.1686 0.2494 -0.0145 -0.0007 0.0549  14  ASP   A O   
310  O O   B ASP   A 14  ? 0.1643 0.1790 0.2419 -0.0375 -0.0186 0.0763  14  ASP   A O   
311  C CB  A ASP   A 14  ? 0.1552 0.1884 0.3043 -0.0128 0.0092  0.0763  14  ASP   A CB  
312  C CB  B ASP   A 14  ? 0.2002 0.2075 0.3031 -0.0151 -0.0085 0.0627  14  ASP   A CB  
313  C CG  A ASP   A 14  ? 0.1779 0.2366 0.3563 -0.0059 0.0217  0.0707  14  ASP   A CG  
314  C CG  B ASP   A 14  ? 0.2135 0.2428 0.3434 -0.0095 -0.0003 0.0584  14  ASP   A CG  
315  O OD1 A ASP   A 14  ? 0.1868 0.2474 0.3658 0.0225  0.0055  0.0623  14  ASP   A OD1 
316  O OD1 B ASP   A 14  ? 0.2231 0.2538 0.3536 -0.0080 0.0070  0.0617  14  ASP   A OD1 
317  O OD2 A ASP   A 14  ? 0.2026 0.2766 0.3892 -0.0090 0.0276  0.0572  14  ASP   A OD2 
318  O OD2 B ASP   A 14  ? 0.2172 0.2666 0.3612 -0.0052 -0.0088 0.0497  14  ASP   A OD2 
327  N N   A ASN   A 15  ? 0.1397 0.1440 0.2512 -0.0157 0.0039  0.0460  15  ASN   A N   
328  N N   B ASN   A 15  ? 0.1549 0.1636 0.2284 -0.0237 -0.0106 0.0776  15  ASN   A N   
329  C CA  A ASN   A 15  ? 0.1342 0.1458 0.2715 -0.0115 -0.0035 0.0313  15  ASN   A CA  
330  C CA  B ASN   A 15  ? 0.1515 0.1616 0.2314 -0.0104 -0.0078 0.0622  15  ASN   A CA  
331  C C   A ASN   A 15  ? 0.1314 0.1411 0.2848 -0.0126 -0.0009 0.0271  15  ASN   A C   
332  C C   B ASN   A 15  ? 0.1470 0.1547 0.2347 -0.0147 0.0073  0.0520  15  ASN   A C   
333  O O   A ASN   A 15  ? 0.1282 0.1364 0.3180 -0.0022 -0.0080 0.0225  15  ASN   A O   
334  O O   B ASN   A 15  ? 0.1476 0.1635 0.2539 -0.0165 0.0173  0.0378  15  ASN   A O   
335  C CB  A ASN   A 15  ? 0.1305 0.1456 0.2715 -0.0132 0.0039  0.0330  15  ASN   A CB  
336  C CB  B ASN   A 15  ? 0.1530 0.1639 0.2285 0.0010  -0.0109 0.0621  15  ASN   A CB  
337  C CG  A ASN   A 15  ? 0.1332 0.1494 0.2830 -0.0136 0.0080  0.0184  15  ASN   A CG  
338  C CG  B ASN   A 15  ? 0.1549 0.1675 0.2416 0.0013  -0.0048 0.0460  15  ASN   A CG  
339  O OD1 A ASN   A 15  ? 0.1565 0.1524 0.3034 -0.0271 0.0001  0.0196  15  ASN   A OD1 
340  O OD1 B ASN   A 15  ? 0.1673 0.1632 0.2626 -0.0041 -0.0056 0.0555  15  ASN   A OD1 
341  N ND2 A ASN   A 15  ? 0.1309 0.1577 0.2721 -0.0164 0.0219  0.0165  15  ASN   A ND2 
342  N ND2 B ASN   A 15  ? 0.1504 0.1728 0.2346 0.0013  -0.0102 0.0378  15  ASN   A ND2 
355  N N   A VAL   A 16  ? 0.1346 0.1397 0.2713 -0.0116 0.0022  0.0390  16  VAL   A N   
356  N N   B VAL   A 16  ? 0.1474 0.1480 0.2275 -0.0194 0.0080  0.0565  16  VAL   A N   
357  C CA  A VAL   A 16  ? 0.1363 0.1469 0.2584 -0.0168 0.0065  0.0402  16  VAL   A CA  
358  C CA  B VAL   A 16  ? 0.1512 0.1581 0.2213 -0.0172 0.0098  0.0470  16  VAL   A CA  
359  C C   A VAL   A 16  ? 0.1294 0.1412 0.2484 -0.0182 0.0038  0.0351  16  VAL   A C   
360  C C   B VAL   A 16  ? 0.1463 0.1657 0.2134 -0.0219 0.0068  0.0448  16  VAL   A C   
361  O O   A VAL   A 16  ? 0.1213 0.1313 0.2504 -0.0149 0.0077  0.0306  16  VAL   A O   
362  O O   B VAL   A 16  ? 0.1465 0.1601 0.2117 -0.0223 0.0157  0.0548  16  VAL   A O   
363  C CB  A VAL   A 16  ? 0.1449 0.1611 0.2494 0.0009  0.0140  0.0534  16  VAL   A CB  
364  C CB  B VAL   A 16  ? 0.1621 0.1654 0.2202 -0.0015 0.0166  0.0500  16  VAL   A CB  
365  C CG1 A VAL   A 16  ? 0.1570 0.1766 0.2541 0.0082  0.0215  0.0552  16  VAL   A CG1 
366  C CG1 B VAL   A 16  ? 0.1704 0.1724 0.2257 0.0061  0.0231  0.0503  16  VAL   A CG1 
367  C CG2 A VAL   A 16  ? 0.1503 0.1698 0.2611 0.0027  0.0257  0.0474  16  VAL   A CG2 
368  C CG2 B VAL   A 16  ? 0.1640 0.1730 0.2309 0.0022  0.0222  0.0448  16  VAL   A CG2 
387  N N   A TYR   A 17  ? 0.1325 0.1401 0.2330 -0.0154 0.0127  0.0431  17  TYR   A N   
388  N N   B TYR   A 17  ? 0.1490 0.1707 0.1972 -0.0241 0.0049  0.0395  17  TYR   A N   
389  C CA  A TYR   A 17  ? 0.1393 0.1405 0.2170 -0.0206 0.0064  0.0364  17  TYR   A CA  
390  C CA  B TYR   A 17  ? 0.1525 0.1759 0.1782 -0.0290 -0.0003 0.0305  17  TYR   A CA  
391  C C   A TYR   A 17  ? 0.1393 0.1311 0.2178 -0.0130 0.0090  0.0255  17  TYR   A C   
392  C C   B TYR   A 17  ? 0.1457 0.1683 0.1669 -0.0277 0.0115  0.0344  17  TYR   A C   
393  O O   A TYR   A 17  ? 0.1303 0.1356 0.2202 -0.0169 0.0202  0.0241  17  TYR   A O   
394  O O   B TYR   A 17  ? 0.1399 0.1689 0.1660 -0.0333 0.0082  0.0425  17  TYR   A O   
395  C CB  A TYR   A 17  ? 0.1505 0.1458 0.2173 -0.0292 -0.0049 0.0395  17  TYR   A CB  
396  C CB  B TYR   A 17  ? 0.1692 0.1946 0.1987 -0.0235 -0.0078 0.0295  17  TYR   A CB  
397  C CG  A TYR   A 17  ? 0.1650 0.1547 0.2138 -0.0358 -0.0234 0.0367  17  TYR   A CG  
398  C CG  B TYR   A 17  ? 0.1881 0.2138 0.2136 -0.0186 -0.0087 0.0264  17  TYR   A CG  
399  C CD1 A TYR   A 17  ? 0.1679 0.1578 0.2271 -0.0369 -0.0267 0.0363  17  TYR   A CD1 
400  C CD1 B TYR   A 17  ? 0.1991 0.2240 0.2270 -0.0090 -0.0123 0.0268  17  TYR   A CD1 
401  C CD2 A TYR   A 17  ? 0.1702 0.1595 0.2005 -0.0421 -0.0268 0.0414  17  TYR   A CD2 
402  C CD2 B TYR   A 17  ? 0.1977 0.2267 0.2230 -0.0175 -0.0103 0.0271  17  TYR   A CD2 
403  C CE1 A TYR   A 17  ? 0.1658 0.1554 0.2196 -0.0457 -0.0323 0.0461  17  TYR   A CE1 
404  C CE1 B TYR   A 17  ? 0.2101 0.2354 0.2412 -0.0053 -0.0075 0.0347  17  TYR   A CE1 
405  C CE2 A TYR   A 17  ? 0.1724 0.1547 0.2051 -0.0419 -0.0381 0.0304  17  TYR   A CE2 
406  C CE2 B TYR   A 17  ? 0.2069 0.2344 0.2324 -0.0099 -0.0083 0.0314  17  TYR   A CE2 
407  C CZ  A TYR   A 17  ? 0.1697 0.1503 0.2168 -0.0479 -0.0381 0.0405  17  TYR   A CZ  
408  C CZ  B TYR   A 17  ? 0.2125 0.2405 0.2487 -0.0013 -0.0097 0.0361  17  TYR   A CZ  
409  O OH  A TYR   A 17  ? 0.1849 0.1531 0.2212 -0.0386 -0.0340 0.0437  17  TYR   A OH  
410  O OH  B TYR   A 17  ? 0.2202 0.2494 0.2708 0.0067  -0.0143 0.0406  17  TYR   A OH  
429  N N   A ILE   A 18  ? 0.1456 0.1390 0.2144 -0.0090 0.0162  0.0377  18  ILE   A N   
430  N N   B ILE   A 18  ? 0.1398 0.1615 0.1559 -0.0349 0.0267  0.0358  18  ILE   A N   
431  C CA  A ILE   A 18  ? 0.1497 0.1362 0.2001 -0.0045 0.0200  0.0227  18  ILE   A CA  
432  C CA  B ILE   A 18  ? 0.1379 0.1611 0.1529 -0.0328 0.0207  0.0229  18  ILE   A CA  
433  C C   A ILE   A 18  ? 0.1579 0.1427 0.2130 -0.0146 0.0257  0.0160  18  ILE   A C   
434  C C   B ILE   A 18  ? 0.1321 0.1681 0.1486 -0.0337 0.0168  0.0151  18  ILE   A C   
435  O O   A ILE   A 18  ? 0.1531 0.1510 0.2107 -0.0224 0.0258  0.0236  18  ILE   A O   
436  O O   B ILE   A 18  ? 0.1306 0.1753 0.1452 -0.0388 0.0182  0.0134  18  ILE   A O   
437  C CB  A ILE   A 18  ? 0.1532 0.1395 0.1859 0.0122  0.0166  0.0289  18  ILE   A CB  
438  C CB  B ILE   A 18  ? 0.1478 0.1605 0.1540 -0.0253 0.0317  0.0214  18  ILE   A CB  
439  C CG1 A ILE   A 18  ? 0.1632 0.1558 0.1779 0.0214  0.0070  0.0260  18  ILE   A CG1 
440  C CG1 B ILE   A 18  ? 0.1667 0.1718 0.1593 -0.0260 0.0378  0.0290  18  ILE   A CG1 
441  C CG2 A ILE   A 18  ? 0.1490 0.1415 0.1874 0.0113  0.0134  0.0136  18  ILE   A CG2 
442  C CG2 B ILE   A 18  ? 0.1490 0.1659 0.1665 -0.0345 0.0283  0.0182  18  ILE   A CG2 
443  C CD1 A ILE   A 18  ? 0.1804 0.1703 0.1908 0.0258  0.0142  0.0243  18  ILE   A CD1 
444  C CD1 B ILE   A 18  ? 0.1853 0.1876 0.1695 -0.0196 0.0373  0.0180  18  ILE   A CD1 
467  N N   A LYS   A 19  ? 0.1635 0.1453 0.2277 -0.0065 0.0374  0.0179  19  LYS   A N   
468  N N   B LYS   A 19  ? 0.1296 0.1685 0.1493 -0.0215 0.0365  0.0132  19  LYS   A N   
469  C CA  A LYS   A 19  ? 0.1799 0.1577 0.2271 -0.0082 0.0396  0.0266  19  LYS   A CA  
470  C CA  B LYS   A 19  ? 0.1426 0.1770 0.1609 -0.0143 0.0398  0.0190  19  LYS   A CA  
471  C C   A LYS   A 19  ? 0.1705 0.1552 0.2371 -0.0026 0.0444  0.0368  19  LYS   A C   
472  C C   B LYS   A 19  ? 0.1370 0.1728 0.1830 -0.0127 0.0272  0.0219  19  LYS   A C   
473  O O   A LYS   A 19  ? 0.1628 0.1531 0.2454 0.0019  0.0481  0.0460  19  LYS   A O   
474  O O   B LYS   A 19  ? 0.1398 0.1721 0.1946 -0.0184 0.0201  0.0187  19  LYS   A O   
475  C CB  A LYS   A 19  ? 0.2023 0.1807 0.2230 -0.0088 0.0428  0.0271  19  LYS   A CB  
476  C CB  B LYS   A 19  ? 0.1581 0.1904 0.1690 -0.0043 0.0468  0.0092  19  LYS   A CB  
477  C CG  A LYS   A 19  ? 0.2265 0.1961 0.2234 -0.0043 0.0452  0.0154  19  LYS   A CG  
478  C CG  B LYS   A 19  ? 0.1838 0.2137 0.1843 0.0044  0.0552  -0.0043 19  LYS   A CG  
479  C CD  A LYS   A 19  ? 0.2426 0.2022 0.2267 0.0026  0.0507  0.0082  19  LYS   A CD  
480  C CD  B LYS   A 19  ? 0.2041 0.2288 0.2022 0.0064  0.0618  -0.0087 19  LYS   A CD  
481  C CE  A LYS   A 19  ? 0.2512 0.2061 0.2314 0.0037  0.0608  0.0014  19  LYS   A CE  
482  C CE  B LYS   A 19  ? 0.2139 0.2401 0.2125 0.0038  0.0662  -0.0101 19  LYS   A CE  
483  N NZ  A LYS   A 19  ? 0.2561 0.2037 0.2276 -0.0056 0.0739  -0.0059 19  LYS   A NZ  
484  N NZ  B LYS   A 19  ? 0.2191 0.2408 0.2208 0.0051  0.0703  -0.0162 19  LYS   A NZ  
511  N N   A ASN   A 20  ? 0.1756 0.1638 0.2556 -0.0107 0.0482  0.0436  20  ASN   A N   
512  N N   B ASN   A 20  ? 0.1374 0.1764 0.2029 -0.0100 0.0300  0.0306  20  ASN   A N   
513  C CA  A ASN   A 20  ? 0.1869 0.1786 0.2640 0.0039  0.0587  0.0326  20  ASN   A CA  
514  C CA  B ASN   A 20  ? 0.1441 0.1870 0.2156 0.0066  0.0327  0.0277  20  ASN   A CA  
515  C C   A ASN   A 20  ? 0.1920 0.1798 0.2589 -0.0041 0.0756  0.0313  20  ASN   A C   
516  C C   B ASN   A 20  ? 0.1640 0.1923 0.2253 0.0066  0.0397  0.0214  20  ASN   A C   
517  O O   A ASN   A 20  ? 0.1983 0.1764 0.2649 -0.0113 0.0718  0.0280  20  ASN   A O   
518  O O   B ASN   A 20  ? 0.1673 0.1884 0.2430 0.0171  0.0380  0.0086  20  ASN   A O   
519  C CB  A ASN   A 20  ? 0.2012 0.1918 0.2752 0.0125  0.0565  0.0342  20  ASN   A CB  
520  C CB  B ASN   A 20  ? 0.1375 0.1936 0.2240 0.0122  0.0296  0.0320  20  ASN   A CB  
521  C CG  A ASN   A 20  ? 0.2187 0.2051 0.2999 0.0234  0.0556  0.0322  20  ASN   A CG  
522  C CG  B ASN   A 20  ? 0.1361 0.1970 0.2402 0.0188  0.0247  0.0357  20  ASN   A CG  
523  O OD1 A ASN   A 20  ? 0.2350 0.2200 0.3311 0.0275  0.0537  0.0235  20  ASN   A OD1 
524  O OD1 B ASN   A 20  ? 0.1349 0.1889 0.2402 0.0169  0.0207  0.0247  20  ASN   A OD1 
525  N ND2 A ASN   A 20  ? 0.2261 0.1975 0.3060 0.0266  0.0470  0.0427  20  ASN   A ND2 
526  N ND2 B ASN   A 20  ? 0.1424 0.1992 0.2619 0.0229  0.0184  0.0521  20  ASN   A ND2 
539  N N   A ALA   A 21  ? 0.1918 0.1866 0.2598 -0.0022 0.0720  0.0190  21  ALA   A N   
540  N N   B ALA   A 21  ? 0.1790 0.2008 0.2353 0.0022  0.0326  0.0101  21  ALA   A N   
541  C CA  A ALA   A 21  ? 0.1907 0.1847 0.2574 -0.0031 0.0675  0.0222  21  ALA   A CA  
542  C CA  B ALA   A 21  ? 0.1890 0.2036 0.2387 -0.0027 0.0281  0.0083  21  ALA   A CA  
543  C C   A ALA   A 21  ? 0.1745 0.1821 0.2483 -0.0034 0.0652  0.0117  21  ALA   A C   
544  C C   B ALA   A 21  ? 0.1807 0.1963 0.2285 -0.0073 0.0359  0.0093  21  ALA   A C   
545  O O   A ALA   A 21  ? 0.1699 0.1933 0.2613 0.0051  0.0676  0.0134  21  ALA   A O   
546  O O   B ALA   A 21  ? 0.1734 0.2022 0.2311 -0.0104 0.0334  0.0223  21  ALA   A O   
547  C CB  A ALA   A 21  ? 0.2006 0.1890 0.2664 -0.0029 0.0636  0.0200  21  ALA   A CB  
548  C CB  B ALA   A 21  ? 0.1971 0.2109 0.2511 0.0007  0.0191  -0.0042 21  ALA   A CB  
559  N N   A ASP   A 22  ? 0.1693 0.1738 0.2434 -0.0069 0.0560  0.0236  22  ASP   A N   
560  N N   B ASP   A 22  ? 0.1826 0.1860 0.2276 -0.0041 0.0483  0.0102  22  ASP   A N   
561  C CA  A ASP   A 22  ? 0.1661 0.1695 0.2369 -0.0006 0.0406  0.0367  22  ASP   A CA  
562  C CA  B ASP   A 22  ? 0.1845 0.1871 0.2253 0.0019  0.0523  0.0093  22  ASP   A CA  
563  C C   A ASP   A 22  ? 0.1640 0.1732 0.2159 0.0026  0.0345  0.0401  22  ASP   A C   
564  C C   B ASP   A 22  ? 0.1769 0.1797 0.1945 -0.0063 0.0519  0.0098  22  ASP   A C   
565  O O   A ASP   A 22  ? 0.1751 0.1774 0.2281 -0.0027 0.0392  0.0438  22  ASP   A O   
566  O O   B ASP   A 22  ? 0.1765 0.1804 0.1980 -0.0097 0.0626  0.0099  22  ASP   A O   
567  C CB  A ASP   A 22  ? 0.1810 0.1703 0.2699 0.0001  0.0354  0.0217  22  ASP   A CB  
568  C CB  B ASP   A 22  ? 0.1998 0.1932 0.2548 0.0174  0.0610  0.0031  22  ASP   A CB  
569  C CG  A ASP   A 22  ? 0.2010 0.1727 0.2937 0.0012  0.0255  0.0170  22  ASP   A CG  
570  C CG  B ASP   A 22  ? 0.2159 0.1991 0.2824 0.0265  0.0717  0.0044  22  ASP   A CG  
571  O OD1 A ASP   A 22  ? 0.1981 0.1688 0.3141 -0.0143 0.0147  0.0287  22  ASP   A OD1 
572  O OD1 B ASP   A 22  ? 0.2196 0.1991 0.2899 0.0256  0.0730  0.0069  22  ASP   A OD1 
573  O OD2 A ASP   A 22  ? 0.2240 0.1842 0.3135 0.0142  0.0393  -0.0087 22  ASP   A OD2 
574  O OD2 B ASP   A 22  ? 0.2292 0.2113 0.2998 0.0243  0.0722  0.0099  22  ASP   A OD2 
583  N N   A ILE   A 23  ? 0.1636 0.1779 0.1976 0.0016  0.0343  0.0361  23  ILE   A N   
584  N N   B ILE   A 23  ? 0.1719 0.1756 0.1845 -0.0040 0.0401  0.0156  23  ILE   A N   
585  C CA  A ILE   A 23  ? 0.1600 0.1689 0.1930 0.0026  0.0283  0.0312  23  ILE   A CA  
586  C CA  B ILE   A 23  ? 0.1684 0.1763 0.1812 -0.0045 0.0249  0.0202  23  ILE   A CA  
587  C C   A ILE   A 23  ? 0.1572 0.1762 0.1953 -0.0001 0.0343  0.0316  23  ILE   A C   
588  C C   B ILE   A 23  ? 0.1742 0.1830 0.1776 -0.0101 0.0311  0.0164  23  ILE   A C   
589  O O   A ILE   A 23  ? 0.1703 0.1851 0.1981 -0.0033 0.0208  0.0292  23  ILE   A O   
590  O O   B ILE   A 23  ? 0.1755 0.1735 0.1680 -0.0048 0.0359  0.0209  23  ILE   A O   
591  C CB  A ILE   A 23  ? 0.1661 0.1648 0.1747 0.0089  0.0180  0.0265  23  ILE   A CB  
592  C CB  B ILE   A 23  ? 0.1618 0.1702 0.1740 0.0035  0.0196  0.0191  23  ILE   A CB  
593  C CG1 A ILE   A 23  ? 0.1696 0.1622 0.1723 0.0056  0.0110  0.0195  23  ILE   A CG1 
594  C CG1 B ILE   A 23  ? 0.1647 0.1711 0.1782 0.0067  0.0117  0.0147  23  ILE   A CG1 
595  C CG2 A ILE   A 23  ? 0.1711 0.1703 0.1736 0.0141  0.0205  0.0348  23  ILE   A CG2 
596  C CG2 B ILE   A 23  ? 0.1572 0.1678 0.1747 0.0087  0.0254  0.0165  23  ILE   A CG2 
597  C CD1 A ILE   A 23  ? 0.1665 0.1600 0.1715 0.0059  -0.0012 0.0133  23  ILE   A CD1 
598  C CD1 B ILE   A 23  ? 0.1656 0.1712 0.1830 0.0029  0.0003  0.0104  23  ILE   A CD1 
621  N N   A VAL   A 24  ? 0.1621 0.1819 0.1927 0.0023  0.0334  0.0331  24  VAL   A N   
622  N N   B VAL   A 24  ? 0.1863 0.1944 0.1987 -0.0171 0.0286  0.0124  24  VAL   A N   
623  C CA  A VAL   A 24  ? 0.1828 0.1866 0.2011 -0.0052 0.0262  0.0325  24  VAL   A CA  
624  C CA  B VAL   A 24  ? 0.1981 0.1999 0.2130 -0.0197 0.0249  0.0118  24  VAL   A CA  
625  C C   A VAL   A 24  ? 0.1923 0.1982 0.2038 -0.0137 0.0289  0.0323  24  VAL   A C   
626  C C   B VAL   A 24  ? 0.2060 0.2137 0.2119 -0.0227 0.0367  -0.0014 24  VAL   A C   
627  O O   A VAL   A 24  ? 0.2110 0.2041 0.2169 -0.0141 0.0321  0.0331  24  VAL   A O   
628  O O   B VAL   A 24  ? 0.2081 0.2171 0.2136 -0.0122 0.0423  -0.0066 24  VAL   A O   
629  C CB  A VAL   A 24  ? 0.1851 0.1889 0.2221 -0.0001 0.0270  0.0343  24  VAL   A CB  
630  C CB  B VAL   A 24  ? 0.1993 0.2010 0.2345 -0.0212 0.0220  0.0263  24  VAL   A CB  
631  C CG1 A VAL   A 24  ? 0.1908 0.1931 0.2334 0.0093  0.0249  0.0210  24  VAL   A CG1 
632  C CG1 B VAL   A 24  ? 0.2079 0.2045 0.2430 -0.0187 0.0124  0.0287  24  VAL   A CG1 
633  C CG2 A VAL   A 24  ? 0.1958 0.1997 0.2296 0.0073  0.0288  0.0462  24  VAL   A CG2 
634  C CG2 B VAL   A 24  ? 0.2057 0.2086 0.2478 -0.0196 0.0261  0.0300  24  VAL   A CG2 
653  N N   A GLU   A 25  ? 0.1950 0.2171 0.2118 -0.0170 0.0421  0.0211  25  GLU   A N   
654  N N   B GLU   A 25  ? 0.2145 0.2228 0.2123 -0.0265 0.0617  -0.0044 25  GLU   A N   
655  C CA  A GLU   A 25  ? 0.2135 0.2381 0.2156 -0.0123 0.0454  0.0197  25  GLU   A CA  
656  C CA  B GLU   A 25  ? 0.2319 0.2379 0.2148 -0.0343 0.0767  -0.0059 25  GLU   A CA  
657  C C   A GLU   A 25  ? 0.1946 0.2429 0.1893 -0.0182 0.0509  0.0171  25  GLU   A C   
658  C C   B GLU   A 25  ? 0.2311 0.2397 0.1843 -0.0339 0.0756  -0.0093 25  GLU   A C   
659  O O   A GLU   A 25  ? 0.1968 0.2456 0.2180 -0.0150 0.0519  0.0082  25  GLU   A O   
660  O O   B GLU   A 25  ? 0.2369 0.2424 0.1829 -0.0310 0.0713  -0.0102 25  GLU   A O   
661  C CB  A GLU   A 25  ? 0.2440 0.2640 0.2546 -0.0057 0.0439  0.0252  25  GLU   A CB  
662  C CB  B GLU   A 25  ? 0.2471 0.2458 0.2380 -0.0394 0.0898  0.0022  25  GLU   A CB  
663  C CG  A GLU   A 25  ? 0.2741 0.2829 0.3085 -0.0132 0.0365  0.0216  25  GLU   A CG  
664  C CG  B GLU   A 25  ? 0.2680 0.2608 0.2790 -0.0399 0.0827  0.0063  25  GLU   A CG  
665  C CD  A GLU   A 25  ? 0.2984 0.2970 0.3601 -0.0238 0.0297  0.0207  25  GLU   A CD  
666  C CD  B GLU   A 25  ? 0.2844 0.2728 0.3191 -0.0443 0.0765  0.0141  25  GLU   A CD  
667  O OE1 A GLU   A 25  ? 0.3066 0.2999 0.3713 -0.0275 0.0236  0.0167  25  GLU   A OE1 
668  O OE1 B GLU   A 25  ? 0.2903 0.2760 0.3319 -0.0435 0.0761  0.0115  25  GLU   A OE1 
669  O OE2 A GLU   A 25  ? 0.3029 0.3039 0.3956 -0.0304 0.0263  0.0152  25  GLU   A OE2 
670  O OE2 B GLU   A 25  ? 0.2932 0.2788 0.3432 -0.0453 0.0781  0.0205  25  GLU   A OE2 
683  N N   A GLU   A 26  ? 0.1809 0.2479 0.1805 -0.0361 0.0467  0.0172  26  GLU   A N   
684  N N   B GLU   A 26  ? 0.2268 0.2350 0.1825 -0.0371 0.0798  -0.0157 26  GLU   A N   
685  C CA  A GLU   A 26  ? 0.1861 0.2543 0.1654 -0.0471 0.0439  0.0183  26  GLU   A CA  
686  C CA  B GLU   A 26  ? 0.2326 0.2350 0.1787 -0.0435 0.0755  -0.0136 26  GLU   A CA  
687  C C   A GLU   A 26  ? 0.1886 0.2464 0.1505 -0.0510 0.0345  0.0185  26  GLU   A C   
688  C C   B GLU   A 26  ? 0.2350 0.2349 0.1656 -0.0472 0.0627  -0.0111 26  GLU   A C   
689  O O   A GLU   A 26  ? 0.1970 0.2399 0.1540 -0.0544 0.0375  0.0182  26  GLU   A O   
690  O O   B GLU   A 26  ? 0.2354 0.2318 0.1777 -0.0476 0.0643  -0.0133 26  GLU   A O   
691  C CB  A GLU   A 26  ? 0.1981 0.2675 0.1873 -0.0514 0.0349  0.0184  26  GLU   A CB  
692  C CB  B GLU   A 26  ? 0.2411 0.2353 0.2008 -0.0500 0.0705  -0.0227 26  GLU   A CB  
693  C CG  A GLU   A 26  ? 0.2211 0.2939 0.2518 -0.0529 0.0315  0.0100  26  GLU   A CG  
694  C CG  B GLU   A 26  ? 0.2484 0.2273 0.2246 -0.0630 0.0807  -0.0281 26  GLU   A CG  
695  C CD  A GLU   A 26  ? 0.2349 0.3123 0.2985 -0.0603 0.0351  0.0120  26  GLU   A CD  
696  C CD  B GLU   A 26  ? 0.2555 0.2200 0.2353 -0.0802 0.0991  -0.0335 26  GLU   A CD  
697  O OE1 A GLU   A 26  ? 0.2409 0.3216 0.3024 -0.0681 0.0414  0.0178  26  GLU   A OE1 
698  O OE1 B GLU   A 26  ? 0.2543 0.2167 0.2386 -0.0896 0.1095  -0.0478 26  GLU   A OE1 
699  O OE2 A GLU   A 26  ? 0.2497 0.3253 0.3270 -0.0522 0.0274  0.0063  26  GLU   A OE2 
700  O OE2 B GLU   A 26  ? 0.2651 0.2266 0.2246 -0.0778 0.1180  -0.0355 26  GLU   A OE2 
713  N N   A ALA   A 27  ? 0.1784 0.2421 0.1553 -0.0569 0.0344  0.0122  27  ALA   A N   
714  N N   B ALA   A 27  ? 0.2351 0.2386 0.1645 -0.0524 0.0507  -0.0106 27  ALA   A N   
715  C CA  A ALA   A 27  ? 0.1935 0.2593 0.1590 -0.0572 0.0390  0.0084  27  ALA   A CA  
716  C CA  B ALA   A 27  ? 0.2442 0.2507 0.1623 -0.0555 0.0396  -0.0159 27  ALA   A CA  
717  C C   A ALA   A 27  ? 0.2251 0.2773 0.1698 -0.0684 0.0361  -0.0068 27  ALA   A C   
718  C C   B ALA   A 27  ? 0.2631 0.2722 0.1685 -0.0607 0.0327  -0.0219 27  ALA   A C   
719  O O   A ALA   A 27  ? 0.2296 0.2744 0.1872 -0.0717 0.0192  -0.0032 27  ALA   A O   
720  O O   B ALA   A 27  ? 0.2632 0.2712 0.1535 -0.0662 0.0160  -0.0240 27  ALA   A O   
721  C CB  A ALA   A 27  ? 0.1789 0.2595 0.1591 -0.0563 0.0355  0.0049  27  ALA   A CB  
722  C CB  B ALA   A 27  ? 0.2364 0.2409 0.1676 -0.0573 0.0381  -0.0141 27  ALA   A CB  
733  N N   A LYS   A 28  ? 0.2619 0.2981 0.1858 -0.0677 0.0305  -0.0331 28  LYS   A N   
734  N N   B LYS   A 28  ? 0.2861 0.2960 0.1925 -0.0589 0.0342  -0.0344 28  LYS   A N   
735  C CA  A LYS   A 28  ? 0.3067 0.3285 0.2285 -0.0587 0.0286  -0.0564 28  LYS   A CA  
736  C CA  B LYS   A 28  ? 0.3141 0.3263 0.2280 -0.0533 0.0375  -0.0461 28  LYS   A CA  
737  C C   A LYS   A 28  ? 0.3286 0.3517 0.2295 -0.0601 0.0428  -0.0520 28  LYS   A C   
738  C C   B LYS   A 28  ? 0.3306 0.3499 0.2280 -0.0586 0.0498  -0.0446 28  LYS   A C   
739  O O   A LYS   A 28  ? 0.3349 0.3592 0.2620 -0.0560 0.0329  -0.0487 28  LYS   A O   
740  O O   B LYS   A 28  ? 0.3352 0.3555 0.2523 -0.0559 0.0431  -0.0414 28  LYS   A O   
741  C CB  A LYS   A 28  ? 0.3285 0.3381 0.2753 -0.0459 0.0134  -0.0733 28  LYS   A CB  
742  C CB  B LYS   A 28  ? 0.3261 0.3345 0.2665 -0.0419 0.0284  -0.0530 28  LYS   A CB  
743  C CG  A LYS   A 28  ? 0.3461 0.3452 0.3234 -0.0346 0.0044  -0.0869 28  LYS   A CG  
744  C CG  B LYS   A 28  ? 0.3365 0.3412 0.3057 -0.0316 0.0232  -0.0617 28  LYS   A CG  
745  C CD  A LYS   A 28  ? 0.3609 0.3571 0.3795 -0.0243 -0.0043 -0.0940 28  LYS   A CD  
746  C CD  B LYS   A 28  ? 0.3458 0.3515 0.3528 -0.0220 0.0165  -0.0672 28  LYS   A CD  
747  C CE  A LYS   A 28  ? 0.3704 0.3653 0.4228 -0.0182 -0.0136 -0.0962 28  LYS   A CE  
748  C CE  B LYS   A 28  ? 0.3537 0.3585 0.3922 -0.0175 0.0094  -0.0701 28  LYS   A CE  
749  N NZ  A LYS   A 28  ? 0.3782 0.3689 0.4483 -0.0131 -0.0168 -0.0938 28  LYS   A NZ  
750  N NZ  B LYS   A 28  ? 0.3589 0.3616 0.4155 -0.0143 0.0049  -0.0697 28  LYS   A NZ  
777  N N   . LYS   A 29  ? 0.3389 0.3667 0.2228 -0.0698 0.0718  -0.0368 29  LYS   A N   
778  C CA  . LYS   A 29  ? 0.3671 0.3991 0.2509 -0.0842 0.0933  -0.0204 29  LYS   A CA  
779  C C   . LYS   A 29  ? 0.3731 0.3970 0.2263 -0.0965 0.0810  -0.0131 29  LYS   A C   
780  O O   . LYS   A 29  ? 0.3850 0.4066 0.2508 -0.0903 0.0736  -0.0134 29  LYS   A O   
781  C CB  . LYS   A 29  ? 0.3880 0.4328 0.3331 -0.0767 0.1086  -0.0144 29  LYS   A CB  
782  C CG  . LYS   A 29  ? 0.4103 0.4596 0.4116 -0.0665 0.1132  -0.0122 29  LYS   A CG  
783  C CD  . LYS   A 29  ? 0.4291 0.4819 0.4831 -0.0573 0.1161  -0.0123 29  LYS   A CD  
784  C CE  . LYS   A 29  ? 0.4434 0.4969 0.5323 -0.0504 0.1193  -0.0095 29  LYS   A CE  
785  N NZ  . LYS   A 29  ? 0.4504 0.5058 0.5621 -0.0460 0.1175  -0.0059 29  LYS   A NZ  
800  N N   . VAL   A 30  ? 0.3645 0.3801 0.2085 -0.1136 0.0815  0.0001  30  VAL   A N   
801  C CA  . VAL   A 30  ? 0.3635 0.3635 0.2003 -0.1264 0.0509  0.0129  30  VAL   A CA  
802  C C   . VAL   A 30  ? 0.3680 0.3508 0.1816 -0.1209 0.0323  0.0188  30  VAL   A C   
803  O O   . VAL   A 30  ? 0.3764 0.3516 0.1883 -0.1186 0.0318  0.0191  30  VAL   A O   
804  C CB  . VAL   A 30  ? 0.3611 0.3574 0.2351 -0.1371 0.0214  0.0093  30  VAL   A CB  
805  C CG1 . VAL   A 30  ? 0.3670 0.3595 0.2585 -0.1345 0.0081  0.0135  30  VAL   A CG1 
806  C CG2 . VAL   A 30  ? 0.3581 0.3545 0.2542 -0.1464 0.0186  0.0065  30  VAL   A CG2 
816  N N   A LYS   A 31  ? 0.3631 0.3419 0.1741 -0.1229 0.0179  0.0179  31  LYS   A N   
817  N N   B LYS   A 31  ? 0.3635 0.3431 0.1872 -0.1173 0.0208  0.0167  31  LYS   A N   
818  C CA  A LYS   A 31  ? 0.3693 0.3419 0.1975 -0.1102 -0.0087 0.0174  31  LYS   A CA  
819  C CA  B LYS   A 31  ? 0.3647 0.3409 0.2125 -0.1048 -0.0003 0.0163  31  LYS   A CA  
820  C C   A LYS   A 31  ? 0.3444 0.3230 0.1453 -0.1041 -0.0171 0.0424  31  LYS   A C   
821  C C   B LYS   A 31  ? 0.3412 0.3212 0.1659 -0.1028 -0.0098 0.0345  31  LYS   A C   
822  O O   A LYS   A 31  ? 0.3502 0.3335 0.1548 -0.0974 -0.0315 0.0496  31  LYS   A O   
823  O O   B LYS   A 31  ? 0.3458 0.3287 0.1752 -0.0984 -0.0172 0.0381  31  LYS   A O   
824  C CB  A LYS   A 31  ? 0.4007 0.3632 0.3067 -0.0992 -0.0227 -0.0049 31  LYS   A CB  
825  C CB  B LYS   A 31  ? 0.3887 0.3597 0.3047 -0.0917 -0.0101 0.0005  31  LYS   A CB  
826  C CG  A LYS   A 31  ? 0.4320 0.3862 0.4158 -0.0842 -0.0385 -0.0193 31  LYS   A CG  
827  C CG  B LYS   A 31  ? 0.4120 0.3786 0.3932 -0.0763 -0.0213 -0.0104 31  LYS   A CG  
828  C CD  A LYS   A 31  ? 0.4577 0.4046 0.5008 -0.0715 -0.0529 -0.0323 31  LYS   A CD  
829  C CD  B LYS   A 31  ? 0.4310 0.3934 0.4606 -0.0635 -0.0310 -0.0199 31  LYS   A CD  
830  C CE  A LYS   A 31  ? 0.4751 0.4167 0.5607 -0.0620 -0.0631 -0.0415 31  LYS   A CE  
831  C CE  B LYS   A 31  ? 0.4447 0.4040 0.5072 -0.0539 -0.0371 -0.0257 31  LYS   A CE  
832  N NZ  A LYS   A 31  ? 0.4852 0.4253 0.5893 -0.0565 -0.0674 -0.0457 31  LYS   A NZ  
833  N NZ  B LYS   A 31  ? 0.4530 0.4101 0.5285 -0.0480 -0.0394 -0.0279 31  LYS   A NZ  
860  N N   . PRO   A 32  ? 0.3102 0.2951 0.1342 -0.1050 -0.0165 0.0398  32  PRO   A N   
861  C CA  . PRO   A 32  ? 0.2899 0.2723 0.1671 -0.0952 -0.0252 0.0558  32  PRO   A CA  
862  C C   . PRO   A 32  ? 0.2794 0.2584 0.1859 -0.0784 -0.0350 0.0652  32  PRO   A C   
863  O O   . PRO   A 32  ? 0.2794 0.2501 0.1962 -0.0729 -0.0449 0.0684  32  PRO   A O   
864  C CB  . PRO   A 32  ? 0.2832 0.2746 0.1670 -0.0942 -0.0274 0.0424  32  PRO   A CB  
865  C CG  . PRO   A 32  ? 0.2786 0.2795 0.1294 -0.0907 -0.0429 0.0251  32  PRO   A CG  
866  C CD  . PRO   A 32  ? 0.2828 0.2829 0.1145 -0.1004 -0.0330 0.0357  32  PRO   A CD  
874  N N   . THR   A 33  ? 0.2817 0.2595 0.1889 -0.0659 -0.0319 0.0667  33  THR   A N   
875  C CA  . THR   A 33  ? 0.2761 0.2591 0.1892 -0.0531 -0.0501 0.0655  33  THR   A CA  
876  C C   . THR   A 33  ? 0.2383 0.2373 0.1775 -0.0540 -0.0555 0.0531  33  THR   A C   
877  O O   . THR   A 33  ? 0.2344 0.2333 0.1978 -0.0540 -0.0677 0.0575  33  THR   A O   
878  C CB  . THR   A 33  ? 0.3041 0.2816 0.2039 -0.0412 -0.0545 0.0839  33  THR   A CB  
879  O OG1 . THR   A 33  ? 0.3224 0.2921 0.2355 -0.0272 -0.0518 0.0964  33  THR   A OG1 
880  C CG2 . THR   A 33  ? 0.3105 0.2930 0.2039 -0.0342 -0.0636 0.0809  33  THR   A CG2 
888  N N   . VAL   A 34  ? 0.2166 0.2205 0.1598 -0.0523 -0.0339 0.0471  34  VAL   A N   
889  C CA  . VAL   A 34  ? 0.1894 0.1978 0.1397 -0.0417 -0.0223 0.0458  34  VAL   A CA  
890  C C   . VAL   A 34  ? 0.1757 0.1819 0.1569 -0.0344 -0.0094 0.0349  34  VAL   A C   
891  O O   . VAL   A 34  ? 0.1807 0.1873 0.1863 -0.0409 -0.0108 0.0465  34  VAL   A O   
892  C CB  . VAL   A 34  ? 0.1931 0.1969 0.1719 -0.0398 -0.0199 0.0341  34  VAL   A CB  
893  C CG1 . VAL   A 34  ? 0.2005 0.2012 0.1889 -0.0382 -0.0030 0.0223  34  VAL   A CG1 
894  C CG2 . VAL   A 34  ? 0.2009 0.2074 0.2078 -0.0325 -0.0210 0.0281  34  VAL   A CG2 
904  N N   . VAL   A 35  ? 0.1673 0.1731 0.1499 -0.0401 -0.0170 0.0235  35  VAL   A N   
905  C CA  . VAL   A 35  ? 0.1590 0.1679 0.1439 -0.0307 -0.0091 0.0178  35  VAL   A CA  
906  C C   . VAL   A 35  ? 0.1477 0.1538 0.1458 -0.0261 -0.0037 0.0121  35  VAL   A C   
907  O O   . VAL   A 35  ? 0.1399 0.1609 0.1660 -0.0261 0.0096  0.0111  35  VAL   A O   
908  C CB  . VAL   A 35  ? 0.1585 0.1763 0.1750 -0.0258 0.0064  0.0087  35  VAL   A CB  
909  C CG1 . VAL   A 35  ? 0.1729 0.1839 0.1824 -0.0205 0.0012  0.0082  35  VAL   A CG1 
910  C CG2 . VAL   A 35  ? 0.1556 0.1717 0.1923 -0.0165 0.0087  0.0086  35  VAL   A CG2 
920  N N   . VAL   A 36  ? 0.1388 0.1519 0.1307 -0.0262 0.0033  0.0162  36  VAL   A N   
921  C CA  . VAL   A 36  ? 0.1316 0.1395 0.1424 -0.0140 -0.0004 0.0167  36  VAL   A CA  
922  C C   . VAL   A 36  ? 0.1244 0.1372 0.1705 -0.0176 0.0111  0.0218  36  VAL   A C   
923  O O   . VAL   A 36  ? 0.1358 0.1408 0.1708 -0.0101 0.0180  0.0114  36  VAL   A O   
924  C CB  . VAL   A 36  ? 0.1346 0.1321 0.1423 -0.0132 0.0009  0.0140  36  VAL   A CB  
925  C CG1 . VAL   A 36  ? 0.1392 0.1306 0.1671 -0.0163 0.0104  0.0050  36  VAL   A CG1 
926  C CG2 . VAL   A 36  ? 0.1373 0.1414 0.1736 -0.0135 -0.0050 0.0249  36  VAL   A CG2 
936  N N   . ASN   A 37  ? 0.1279 0.1301 0.1474 -0.0069 0.0029  0.0163  37  ASN   A N   
937  C CA  . ASN   A 37  ? 0.1247 0.1225 0.1568 0.0007  0.0048  0.0141  37  ASN   A CA  
938  C C   . ASN   A 37  ? 0.1192 0.1272 0.1521 0.0004  0.0198  0.0257  37  ASN   A C   
939  O O   . ASN   A 37  ? 0.1317 0.1362 0.1456 0.0039  0.0104  0.0101  37  ASN   A O   
940  C CB  . ASN   A 37  ? 0.1293 0.1237 0.1723 -0.0000 0.0084  0.0210  37  ASN   A CB  
941  C CG  . ASN   A 37  ? 0.1270 0.1221 0.1834 -0.0018 0.0069  0.0103  37  ASN   A CG  
942  O OD1 . ASN   A 37  ? 0.1275 0.1236 0.1862 -0.0018 0.0120  0.0112  37  ASN   A OD1 
943  N ND2 . ASN   A 37  ? 0.1257 0.1278 0.1977 -0.0067 0.0072  0.0238  37  ASN   A ND2 
950  N N   . ALA   A 38  ? 0.1225 0.1316 0.1512 0.0044  0.0169  0.0136  38  ALA   A N   
951  C CA  . ALA   A 38  ? 0.1300 0.1384 0.1442 0.0027  0.0082  0.0104  38  ALA   A CA  
952  C C   . ALA   A 38  ? 0.1274 0.1341 0.1751 0.0029  -0.0001 0.0103  38  ALA   A C   
953  O O   . ALA   A 38  ? 0.1315 0.1328 0.1710 0.0072  0.0000  0.0142  38  ALA   A O   
954  C CB  . ALA   A 38  ? 0.1403 0.1704 0.1735 -0.0131 -0.0003 0.0113  38  ALA   A CB  
960  N N   . ALA   A 39  ? 0.1222 0.1285 0.1788 0.0011  0.0059  0.0162  39  ALA   A N   
961  C CA  . ALA   A 39  ? 0.1323 0.1352 0.1718 0.0004  0.0130  0.0162  39  ALA   A CA  
962  C C   . ALA   A 39  ? 0.1312 0.1272 0.1638 -0.0005 0.0081  0.0129  39  ALA   A C   
963  O O   . ALA   A 39  ? 0.1428 0.1335 0.1640 -0.0068 0.0092  0.0086  39  ALA   A O   
964  C CB  . ALA   A 39  ? 0.1375 0.1559 0.1714 -0.0018 0.0020  0.0039  39  ALA   A CB  
970  N N   . ASN   A 40  ? 0.1443 0.1295 0.1730 -0.0054 0.0256  0.0102  40  ASN   A N   
971  C CA  . ASN   A 40  ? 0.1495 0.1267 0.1751 -0.0062 0.0116  0.0066  40  ASN   A CA  
972  C C   . ASN   A 40  ? 0.1513 0.1178 0.1676 -0.0069 0.0180  0.0177  40  ASN   A C   
973  O O   . ASN   A 40  ? 0.1418 0.1276 0.1684 -0.0065 0.0229  0.0173  40  ASN   A O   
974  C CB  . ASN   A 40  ? 0.1552 0.1352 0.1882 -0.0007 -0.0008 0.0094  40  ASN   A CB  
975  C CG  . ASN   A 40  ? 0.1629 0.1365 0.2270 0.0001  0.0006  0.0166  40  ASN   A CG  
976  O OD1 . ASN   A 40  ? 0.1758 0.1360 0.2296 0.0003  -0.0085 0.0111  40  ASN   A OD1 
977  N ND2 . ASN   A 40  ? 0.1656 0.1519 0.2448 0.0080  0.0045  0.0016  40  ASN   A ND2 
984  N N   . VAL   A 41  ? 0.1608 0.1262 0.1768 -0.0053 0.0257  0.0157  41  VAL   A N   
985  C CA  . VAL   A 41  ? 0.1627 0.1285 0.1938 -0.0014 0.0364  0.0150  41  VAL   A CA  
986  C C   . VAL   A 41  ? 0.1548 0.1294 0.2028 0.0017  0.0428  0.0132  41  VAL   A C   
987  O O   . VAL   A 41  ? 0.1610 0.1220 0.2102 0.0028  0.0304  0.0097  41  VAL   A O   
988  C CB  . VAL   A 41  ? 0.1790 0.1451 0.1834 -0.0108 0.0496  0.0104  41  VAL   A CB  
989  C CG1 . VAL   A 41  ? 0.1876 0.1514 0.2058 -0.0083 0.0477  0.0060  41  VAL   A CG1 
990  C CG2 . VAL   A 41  ? 0.1990 0.1619 0.1844 -0.0207 0.0502  0.0128  41  VAL   A CG2 
1000 N N   . TYR   A 42  ? 0.1404 0.1307 0.1984 0.0026  0.0384  0.0282  42  TYR   A N   
1001 C CA  . TYR   A 42  ? 0.1464 0.1227 0.1982 0.0001  0.0369  0.0252  42  TYR   A CA  
1002 C C   . TYR   A 42  ? 0.1375 0.1254 0.2076 0.0001  0.0356  0.0321  42  TYR   A C   
1003 O O   . TYR   A 42  ? 0.1355 0.1242 0.2203 -0.0166 0.0200  0.0084  42  TYR   A O   
1004 C CB  . TYR   A 42  ? 0.1686 0.1335 0.1747 -0.0043 0.0345  0.0224  42  TYR   A CB  
1005 C CG  . TYR   A 42  ? 0.1917 0.1443 0.1747 -0.0034 0.0256  0.0336  42  TYR   A CG  
1006 C CD1 . TYR   A 42  ? 0.2036 0.1582 0.1907 -0.0150 0.0337  0.0254  42  TYR   A CD1 
1007 C CD2 . TYR   A 42  ? 0.2134 0.1679 0.2038 -0.0029 0.0209  0.0251  42  TYR   A CD2 
1008 C CE1 . TYR   A 42  ? 0.2163 0.1709 0.1924 -0.0176 0.0406  0.0191  42  TYR   A CE1 
1009 C CE2 . TYR   A 42  ? 0.2264 0.1804 0.2077 -0.0122 0.0268  0.0263  42  TYR   A CE2 
1010 C CZ  . TYR   A 42  ? 0.2353 0.1856 0.1992 -0.0191 0.0429  0.0204  42  TYR   A CZ  
1011 O OH  . TYR   A 42  ? 0.2504 0.2024 0.2388 -0.0370 0.0414  0.0095  42  TYR   A OH  
1021 N N   . LEU   A 43  ? 0.1335 0.1256 0.2064 -0.0049 0.0219  0.0154  43  LEU   A N   
1022 C CA  . LEU   A 43  ? 0.1278 0.1253 0.1918 -0.0061 0.0154  0.0107  43  LEU   A CA  
1023 C C   . LEU   A 43  ? 0.1307 0.1302 0.1946 -0.0079 0.0062  0.0066  43  LEU   A C   
1024 O O   . LEU   A 43  ? 0.1465 0.1324 0.2078 0.0002  -0.0019 -0.0002 43  LEU   A O   
1025 C CB  . LEU   A 43  ? 0.1339 0.1213 0.2084 -0.0073 0.0127  0.0095  43  LEU   A CB  
1026 C CG  . LEU   A 43  ? 0.1396 0.1228 0.2052 -0.0060 0.0082  0.0152  43  LEU   A CG  
1027 C CD1 . LEU   A 43  ? 0.1481 0.1340 0.2236 -0.0044 -0.0068 0.0181  43  LEU   A CD1 
1028 C CD2 . LEU   A 43  ? 0.1549 0.1316 0.2110 -0.0051 0.0125  0.0247  43  LEU   A CD2 
1040 N N   . LYS   A 44  ? 0.1411 0.1288 0.1917 -0.0021 0.0024  0.0105  44  LYS   A N   
1041 C CA  . LYS   A 44  ? 0.1545 0.1275 0.1997 -0.0046 0.0152  0.0159  44  LYS   A CA  
1042 C C   . LYS   A 44  ? 0.1371 0.1272 0.1868 0.0017  0.0024  0.0128  44  LYS   A C   
1043 O O   . LYS   A 44  ? 0.1480 0.1469 0.1961 -0.0010 0.0062  0.0008  44  LYS   A O   
1044 C CB  . LYS   A 44  ? 0.1828 0.1445 0.2240 -0.0000 0.0256  0.0381  44  LYS   A CB  
1045 C CG  . LYS   A 44  ? 0.2152 0.1743 0.2837 -0.0086 0.0423  0.0425  44  LYS   A CG  
1046 C CD  . LYS   A 44  ? 0.2558 0.2416 0.3653 -0.0194 0.0314  0.0336  44  LYS   A CD  
1047 C CE  . LYS   A 44  ? 0.2838 0.2771 0.4195 -0.0280 0.0263  0.0367  44  LYS   A CE  
1048 N NZ  . LYS   A 44  ? 0.2818 0.2902 0.4452 -0.0338 0.0304  0.0423  44  LYS   A NZ  
1062 N N   A HIS   A 45  ? 0.1259 0.1182 0.1873 0.0039  0.0082  0.0188  45  HIS   A N   
1063 N N   B HIS   A 45  ? 0.1356 0.1245 0.1838 0.0014  0.0031  0.0142  45  HIS   A N   
1064 C CA  A HIS   A 45  ? 0.1280 0.1206 0.1833 -0.0000 0.0041  0.0210  45  HIS   A CA  
1065 C CA  B HIS   A 45  ? 0.1417 0.1286 0.1815 -0.0012 -0.0025 0.0138  45  HIS   A CA  
1066 C C   A HIS   A 45  ? 0.1349 0.1295 0.1877 0.0015  0.0083  0.0322  45  HIS   A C   
1067 C C   B HIS   A 45  ? 0.1527 0.1375 0.1898 0.0048  -0.0045 0.0152  45  HIS   A C   
1068 O O   A HIS   A 45  ? 0.1439 0.1283 0.1881 0.0063  0.0148  0.0320  45  HIS   A O   
1069 O O   B HIS   A 45  ? 0.1655 0.1408 0.2036 0.0144  0.0016  0.0151  45  HIS   A O   
1070 C CB  A HIS   A 45  ? 0.1288 0.1190 0.1754 0.0011  0.0006  0.0095  45  HIS   A CB  
1071 C CB  B HIS   A 45  ? 0.1371 0.1274 0.1723 -0.0016 -0.0009 0.0080  45  HIS   A CB  
1072 C CG  A HIS   A 45  ? 0.1234 0.1126 0.1623 -0.0025 0.0063  0.0157  45  HIS   A CG  
1073 C CG  B HIS   A 45  ? 0.1249 0.1319 0.1718 -0.0023 0.0130  0.0084  45  HIS   A CG  
1074 N ND1 A HIS   A 45  ? 0.1195 0.1197 0.1555 -0.0072 -0.0007 0.0153  45  HIS   A ND1 
1075 N ND1 B HIS   A 45  ? 0.1215 0.1348 0.1922 -0.0027 0.0055  0.0126  45  HIS   A ND1 
1076 C CD2 A HIS   A 45  ? 0.1267 0.1207 0.1677 -0.0015 -0.0029 0.0233  45  HIS   A CD2 
1077 C CD2 B HIS   A 45  ? 0.1160 0.1266 0.1664 -0.0065 0.0090  0.0016  45  HIS   A CD2 
1078 C CE1 A HIS   A 45  ? 0.1236 0.1341 0.1456 -0.0055 -0.0068 0.0166  45  HIS   A CE1 
1079 C CE1 B HIS   A 45  ? 0.1164 0.1290 0.1727 -0.0066 0.0049  -0.0023 45  HIS   A CE1 
1080 N NE2 A HIS   A 45  ? 0.1272 0.1321 0.1643 0.0005  0.0027  0.0209  45  HIS   A NE2 
1081 N NE2 B HIS   A 45  ? 0.1153 0.1313 0.1671 -0.0072 0.0070  -0.0000 45  HIS   A NE2 
1096 N N   A GLY   A 46  ? 0.1383 0.1325 0.1999 0.0034  -0.0163 0.0285  46  GLY   A N   
1097 N N   B GLY   A 46  ? 0.1532 0.1339 0.1927 -0.0008 -0.0165 0.0115  46  GLY   A N   
1098 C CA  A GLY   A 46  ? 0.1397 0.1387 0.2041 0.0065  -0.0208 0.0214  46  GLY   A CA  
1099 C CA  B GLY   A 46  ? 0.1530 0.1438 0.1978 -0.0029 -0.0172 0.0012  46  GLY   A CA  
1100 C C   A GLY   A 46  ? 0.1445 0.1390 0.2229 0.0173  -0.0244 0.0316  46  GLY   A C   
1101 C C   B GLY   A 46  ? 0.1541 0.1495 0.2075 -0.0022 -0.0111 0.0015  46  GLY   A C   
1102 O O   A GLY   A 46  ? 0.1494 0.1513 0.2691 0.0248  -0.0393 0.0172  46  GLY   A O   
1103 O O   B GLY   A 46  ? 0.1611 0.1583 0.2380 -0.0030 -0.0190 -0.0195 46  GLY   A O   
1110 N N   A GLY   A 47  ? 0.1497 0.1405 0.2050 0.0154  -0.0160 0.0395  47  GLY   A N   
1111 N N   B GLY   A 47  ? 0.1535 0.1518 0.1853 -0.0027 0.0006  0.0028  47  GLY   A N   
1112 C CA  A GLY   A 47  ? 0.1509 0.1472 0.1895 0.0201  -0.0169 0.0324  47  GLY   A CA  
1113 C CA  B GLY   A 47  ? 0.1451 0.1567 0.1670 0.0004  -0.0007 0.0115  47  GLY   A CA  
1114 C C   A GLY   A 47  ? 0.1395 0.1478 0.1652 0.0150  -0.0155 0.0133  47  GLY   A C   
1115 C C   B GLY   A 47  ? 0.1337 0.1492 0.1326 0.0091  0.0031  0.0112  47  GLY   A C   
1116 O O   A GLY   A 47  ? 0.1393 0.1431 0.1707 0.0146  -0.0077 0.0211  47  GLY   A O   
1117 O O   B GLY   A 47  ? 0.1332 0.1405 0.1169 0.0181  0.0071  0.0314  47  GLY   A O   
1124 N N   A GLY   A 48  ? 0.1362 0.1469 0.1561 0.0158  -0.0107 0.0019  48  GLY   A N   
1125 N N   B GLY   A 48  ? 0.1309 0.1477 0.1187 0.0097  0.0049  0.0032  48  GLY   A N   
1126 C CA  A GLY   A 48  ? 0.1288 0.1402 0.1503 0.0073  -0.0047 -0.0080 48  GLY   A CA  
1127 C CA  B GLY   A 48  ? 0.1313 0.1352 0.1095 0.0077  0.0071  -0.0020 48  GLY   A CA  
1128 C C   A GLY   A 48  ? 0.1250 0.1363 0.1347 0.0039  0.0017  -0.0074 48  GLY   A C   
1129 C C   B GLY   A 48  ? 0.1329 0.1310 0.1274 0.0088  0.0023  0.0030  48  GLY   A C   
1130 O O   A GLY   A 48  ? 0.1450 0.1395 0.1258 0.0049  -0.0024 -0.0013 48  GLY   A O   
1131 O O   B GLY   A 48  ? 0.1448 0.1337 0.1264 0.0115  0.0109  -0.0068 48  GLY   A O   
1138 N N   A VAL   A 49  ? 0.1179 0.1317 0.1698 -0.0014 -0.0068 0.0027  49  VAL   A N   
1139 N N   B VAL   A 49  ? 0.1263 0.1235 0.1368 0.0039  0.0000  -0.0025 49  VAL   A N   
1140 C CA  A VAL   A 49  ? 0.1328 0.1334 0.1715 -0.0092 -0.0070 0.0140  49  VAL   A CA  
1141 C CA  B VAL   A 49  ? 0.1263 0.1268 0.1508 -0.0007 -0.0017 0.0020  49  VAL   A CA  
1142 C C   A VAL   A 49  ? 0.1305 0.1294 0.1439 -0.0056 0.0018  0.0096  49  VAL   A C   
1143 C C   B VAL   A 49  ? 0.1310 0.1227 0.1574 -0.0021 0.0064  -0.0138 49  VAL   A C   
1144 O O   A VAL   A 49  ? 0.1305 0.1373 0.1400 -0.0114 0.0026  0.0042  49  VAL   A O   
1145 O O   B VAL   A 49  ? 0.1356 0.1294 0.1604 -0.0028 0.0133  -0.0115 49  VAL   A O   
1146 C CB  A VAL   A 49  ? 0.1443 0.1354 0.2022 -0.0106 -0.0111 0.0142  49  VAL   A CB  
1147 C CB  B VAL   A 49  ? 0.1152 0.1316 0.1795 0.0027  -0.0098 0.0091  49  VAL   A CB  
1148 C CG1 A VAL   A 49  ? 0.1447 0.1319 0.2172 -0.0124 -0.0108 0.0141  49  VAL   A CG1 
1149 C CG1 B VAL   A 49  ? 0.1070 0.1278 0.1951 0.0096  -0.0047 0.0175  49  VAL   A CG1 
1150 C CG2 A VAL   A 49  ? 0.1608 0.1460 0.2263 -0.0271 -0.0233 0.0271  49  VAL   A CG2 
1151 C CG2 B VAL   A 49  ? 0.1261 0.1401 0.2007 -0.0030 -0.0234 0.0158  49  VAL   A CG2 
1170 N N   A ALA   A 50  ? 0.1222 0.1293 0.1327 -0.0034 -0.0063 0.0113  50  ALA   A N   
1171 N N   B ALA   A 50  ? 0.1301 0.1191 0.1497 0.0038  0.0034  -0.0192 50  ALA   A N   
1172 C CA  A ALA   A 50  ? 0.1201 0.1282 0.1499 -0.0055 -0.0040 0.0155  50  ALA   A CA  
1173 C CA  B ALA   A 50  ? 0.1262 0.1152 0.1445 -0.0037 0.0069  -0.0203 50  ALA   A CA  
1174 C C   A ALA   A 50  ? 0.1174 0.1301 0.1559 -0.0040 -0.0035 0.0096  50  ALA   A C   
1175 C C   B ALA   A 50  ? 0.1280 0.1160 0.1398 -0.0092 0.0080  -0.0156 50  ALA   A C   
1176 O O   A ALA   A 50  ? 0.1185 0.1312 0.1675 0.0003  -0.0114 0.0088  50  ALA   A O   
1177 O O   B ALA   A 50  ? 0.1296 0.1215 0.1370 -0.0039 0.0148  -0.0238 50  ALA   A O   
1178 C CB  A ALA   A 50  ? 0.1203 0.1376 0.1613 -0.0056 -0.0066 0.0066  50  ALA   A CB  
1179 C CB  B ALA   A 50  ? 0.1314 0.1120 0.1474 -0.0000 0.0087  -0.0297 50  ALA   A CB  
1190 N N   A GLY   A 51  ? 0.1199 0.1306 0.1583 0.0122  -0.0014 0.0118  51  GLY   A N   
1191 N N   B GLY   A 51  ? 0.1353 0.1110 0.1430 -0.0086 0.0043  -0.0187 51  GLY   A N   
1192 C CA  A GLY   A 51  ? 0.1270 0.1290 0.1651 0.0101  0.0067  0.0229  51  GLY   A CA  
1193 C CA  B GLY   A 51  ? 0.1459 0.1117 0.1424 -0.0090 0.0011  -0.0215 51  GLY   A CA  
1194 C C   A GLY   A 51  ? 0.1189 0.1338 0.1505 0.0087  0.0103  0.0113  51  GLY   A C   
1195 C C   B GLY   A 51  ? 0.1455 0.1246 0.1579 -0.0059 0.0055  -0.0212 51  GLY   A C   
1196 O O   A GLY   A 51  ? 0.1208 0.1426 0.1535 0.0022  -0.0031 0.0078  51  GLY   A O   
1197 O O   B GLY   A 51  ? 0.1513 0.1369 0.1600 -0.0043 0.0112  -0.0244 51  GLY   A O   
1204 N N   A ALA   A 52  ? 0.1186 0.1489 0.1513 0.0004  0.0020  0.0089  52  ALA   A N   
1205 N N   B ALA   A 52  ? 0.1392 0.1298 0.1558 -0.0116 0.0036  -0.0372 52  ALA   A N   
1206 C CA  A ALA   A 52  ? 0.1218 0.1589 0.1518 0.0009  -0.0015 0.0110  52  ALA   A CA  
1207 C CA  B ALA   A 52  ? 0.1371 0.1366 0.1642 -0.0079 0.0105  -0.0314 52  ALA   A CA  
1208 C C   A ALA   A 52  ? 0.1262 0.1558 0.1554 -0.0053 0.0078  0.0107  52  ALA   A C   
1209 C C   B ALA   A 52  ? 0.1338 0.1305 0.1559 -0.0116 0.0169  -0.0261 52  ALA   A C   
1210 O O   A ALA   A 52  ? 0.1358 0.1622 0.1619 0.0015  0.0053  0.0136  52  ALA   A O   
1211 O O   B ALA   A 52  ? 0.1408 0.1378 0.1628 -0.0061 0.0176  -0.0204 52  ALA   A O   
1212 C CB  A ALA   A 52  ? 0.1357 0.1821 0.1527 -0.0110 -0.0026 0.0228  52  ALA   A CB  
1213 C CB  B ALA   A 52  ? 0.1433 0.1613 0.1839 -0.0095 0.0102  -0.0265 52  ALA   A CB  
1224 N N   A LEU   A 53  ? 0.1268 0.1560 0.1491 -0.0120 0.0057  0.0217  53  LEU   A N   
1225 N N   B LEU   A 53  ? 0.1298 0.1348 0.1495 -0.0062 0.0091  -0.0253 53  LEU   A N   
1226 C CA  A LEU   A 53  ? 0.1386 0.1562 0.1545 -0.0116 0.0050  0.0189  53  LEU   A CA  
1227 C CA  B LEU   A 53  ? 0.1320 0.1437 0.1372 -0.0035 0.0006  -0.0172 53  LEU   A CA  
1228 C C   A LEU   A 53  ? 0.1404 0.1583 0.1481 -0.0034 0.0008  0.0091  53  LEU   A C   
1229 C C   B LEU   A 53  ? 0.1400 0.1500 0.1354 -0.0004 0.0068  -0.0133 53  LEU   A C   
1230 O O   A LEU   A 53  ? 0.1552 0.1718 0.1565 -0.0193 -0.0052 -0.0029 53  LEU   A O   
1231 O O   B LEU   A 53  ? 0.1491 0.1569 0.1381 -0.0114 0.0072  -0.0141 53  LEU   A O   
1232 C CB  A LEU   A 53  ? 0.1402 0.1509 0.1714 -0.0134 0.0115  0.0253  53  LEU   A CB  
1233 C CB  B LEU   A 53  ? 0.1171 0.1408 0.1325 -0.0089 -0.0073 -0.0141 53  LEU   A CB  
1234 C CG  A LEU   A 53  ? 0.1362 0.1516 0.1704 -0.0075 0.0059  0.0216  53  LEU   A CG  
1235 C CG  B LEU   A 53  ? 0.1168 0.1467 0.1417 -0.0099 -0.0044 -0.0155 53  LEU   A CG  
1236 C CD1 A LEU   A 53  ? 0.1362 0.1552 0.1644 -0.0031 -0.0054 0.0190  53  LEU   A CD1 
1237 C CD1 B LEU   A 53  ? 0.1122 0.1489 0.1420 -0.0091 0.0001  -0.0189 53  LEU   A CD1 
1238 C CD2 A LEU   A 53  ? 0.1431 0.1637 0.1787 -0.0190 0.0061  0.0160  53  LEU   A CD2 
1239 C CD2 B LEU   A 53  ? 0.1205 0.1507 0.1527 -0.0046 0.0007  -0.0114 53  LEU   A CD2 
1262 N N   A ASN   A 54  ? 0.1235 0.1462 0.1467 -0.0069 -0.0046 0.0091  54  ASN   A N   
1263 N N   B ASN   A 54  ? 0.1318 0.1469 0.1514 -0.0006 0.0024  -0.0096 54  ASN   A N   
1264 C CA  A ASN   A 54  ? 0.1243 0.1386 0.1790 -0.0065 -0.0053 0.0017  54  ASN   A CA  
1265 C CA  B ASN   A 54  ? 0.1288 0.1450 0.1687 -0.0008 -0.0039 -0.0089 54  ASN   A CA  
1266 C C   A ASN   A 54  ? 0.1347 0.1408 0.1827 -0.0092 0.0061  -0.0026 54  ASN   A C   
1267 C C   B ASN   A 54  ? 0.1361 0.1436 0.1715 -0.0085 0.0013  -0.0084 54  ASN   A C   
1268 O O   A ASN   A 54  ? 0.1365 0.1488 0.1972 -0.0036 0.0034  -0.0026 54  ASN   A O   
1269 O O   B ASN   A 54  ? 0.1390 0.1471 0.1763 -0.0105 -0.0037 -0.0064 54  ASN   A O   
1270 C CB  A ASN   A 54  ? 0.1187 0.1291 0.1982 -0.0150 -0.0062 0.0000  54  ASN   A CB  
1271 C CB  B ASN   A 54  ? 0.1267 0.1463 0.1785 0.0059  -0.0097 -0.0037 54  ASN   A CB  
1272 C CG  A ASN   A 54  ? 0.1227 0.1314 0.1922 -0.0142 0.0004  -0.0027 54  ASN   A CG  
1273 C CG  B ASN   A 54  ? 0.1278 0.1505 0.1750 0.0124  -0.0105 -0.0007 54  ASN   A CG  
1274 O OD1 A ASN   A 54  ? 0.1217 0.1281 0.1734 -0.0197 0.0053  -0.0025 54  ASN   A OD1 
1275 O OD1 B ASN   A 54  ? 0.1263 0.1600 0.1768 0.0076  -0.0107 0.0015  54  ASN   A OD1 
1276 N ND2 A ASN   A 54  ? 0.1280 0.1384 0.2091 -0.0192 -0.0036 0.0064  54  ASN   A ND2 
1277 N ND2 B ASN   A 54  ? 0.1335 0.1482 0.1765 0.0141  -0.0108 0.0053  54  ASN   A ND2 
1290 N N   . LYS   A 55  ? 0.1322 0.1401 0.1812 -0.0037 0.0024  -0.0113 55  LYS   A N   
1291 C CA  . LYS   A 55  ? 0.1447 0.1516 0.1923 0.0064  -0.0055 -0.0229 55  LYS   A CA  
1292 C C   . LYS   A 55  ? 0.1428 0.1599 0.1830 -0.0024 0.0100  -0.0313 55  LYS   A C   
1293 O O   . LYS   A 55  ? 0.1540 0.1676 0.1886 0.0016  0.0019  -0.0333 55  LYS   A O   
1294 C CB  . LYS   A 55  ? 0.1498 0.1652 0.2192 0.0160  -0.0021 -0.0326 55  LYS   A CB  
1295 C CG  . LYS   A 55  ? 0.1720 0.1996 0.2297 0.0288  -0.0199 -0.0269 55  LYS   A CG  
1296 C CD  . LYS   A 55  ? 0.1865 0.2289 0.2362 0.0374  -0.0108 -0.0328 55  LYS   A CD  
1297 C CE  . LYS   A 55  ? 0.2027 0.2576 0.2514 0.0417  -0.0177 -0.0393 55  LYS   A CE  
1298 N NZ  . LYS   A 55  ? 0.2113 0.2662 0.2741 0.0533  -0.0220 -0.0353 55  LYS   A NZ  
1313 N N   . ALA   A 56  ? 0.1460 0.1702 0.1857 -0.0135 0.0096  -0.0343 56  ALA   A N   
1314 C CA  . ALA   A 56  ? 0.1559 0.1826 0.1808 -0.0130 0.0157  -0.0302 56  ALA   A CA  
1315 C C   . ALA   A 56  ? 0.1635 0.1971 0.1618 -0.0122 0.0266  -0.0436 56  ALA   A C   
1316 O O   . ALA   A 56  ? 0.1681 0.2309 0.1795 -0.0028 0.0298  -0.0313 56  ALA   A O   
1317 C CB  . ALA   A 56  ? 0.1684 0.2036 0.2034 -0.0259 0.0175  -0.0184 56  ALA   A CB  
1323 N N   . THR   A 57  ? 0.1490 0.1796 0.1658 -0.0177 0.0159  -0.0266 57  THR   A N   
1324 C CA  . THR   A 57  ? 0.1505 0.1739 0.1770 -0.0177 0.0014  -0.0138 57  THR   A CA  
1325 C C   . THR   A 57  ? 0.1489 0.1820 0.1911 -0.0089 0.0036  -0.0279 57  THR   A C   
1326 O O   . THR   A 57  ? 0.1469 0.1849 0.2112 -0.0131 -0.0127 -0.0335 57  THR   A O   
1327 C CB  . THR   A 57  ? 0.1481 0.1728 0.1753 -0.0100 0.0109  -0.0165 57  THR   A CB  
1328 O OG1 . THR   A 57  ? 0.1403 0.1659 0.1704 -0.0085 0.0053  -0.0159 57  THR   A OG1 
1329 C CG2 . THR   A 57  ? 0.1528 0.1753 0.1558 -0.0101 0.0019  -0.0066 57  THR   A CG2 
1337 N N   . ASN   A 58  ? 0.1528 0.1747 0.2092 -0.0144 0.0098  -0.0463 58  ASN   A N   
1338 C CA  . ASN   A 58  ? 0.1698 0.1683 0.2363 -0.0157 0.0186  -0.0480 58  ASN   A CA  
1339 C C   . ASN   A 58  ? 0.1476 0.1541 0.2277 -0.0034 -0.0010 -0.0301 58  ASN   A C   
1340 O O   . ASN   A 58  ? 0.1504 0.1633 0.2384 -0.0122 -0.0024 -0.0334 58  ASN   A O   
1341 C CB  . ASN   A 58  ? 0.2252 0.1857 0.2724 -0.0249 0.0470  -0.0623 58  ASN   A CB  
1342 C CG  . ASN   A 58  ? 0.2707 0.2161 0.3433 -0.0219 0.0537  -0.0406 58  ASN   A CG  
1343 O OD1 . ASN   A 58  ? 0.3018 0.2126 0.3818 0.0080  0.0854  -0.0349 58  ASN   A OD1 
1344 N ND2 . ASN   A 58  ? 0.2780 0.2348 0.3631 -0.0206 0.0476  -0.0348 58  ASN   A ND2 
1351 N N   . ASN   A 59  ? 0.1350 0.1437 0.2123 -0.0084 -0.0046 -0.0157 59  ASN   A N   
1352 C CA  . ASN   A 59  ? 0.1368 0.1354 0.2002 -0.0034 -0.0013 -0.0102 59  ASN   A CA  
1353 C C   . ASN   A 59  ? 0.1416 0.1398 0.1934 -0.0115 -0.0052 -0.0013 59  ASN   A C   
1354 O O   . ASN   A 59  ? 0.1397 0.1436 0.1831 -0.0127 -0.0037 0.0020  59  ASN   A O   
1355 C CB  . ASN   A 59  ? 0.1423 0.1329 0.1974 -0.0034 -0.0101 -0.0174 59  ASN   A CB  
1356 C CG  . ASN   A 59  ? 0.1436 0.1387 0.2018 -0.0027 -0.0187 0.0059  59  ASN   A CG  
1357 O OD1 . ASN   A 59  ? 0.1546 0.1487 0.2031 -0.0153 -0.0213 0.0069  59  ASN   A OD1 
1358 N ND2 . ASN   A 59  ? 0.1519 0.1452 0.2153 -0.0104 -0.0131 0.0088  59  ASN   A ND2 
1365 N N   . ALA   A 60  ? 0.1293 0.1465 0.1875 -0.0047 0.0002  -0.0010 60  ALA   A N   
1366 C CA  . ALA   A 60  ? 0.1365 0.1479 0.1854 -0.0079 -0.0125 0.0001  60  ALA   A CA  
1367 C C   . ALA   A 60  ? 0.1349 0.1430 0.1983 -0.0064 -0.0122 -0.0085 60  ALA   A C   
1368 O O   . ALA   A 60  ? 0.1292 0.1403 0.2222 -0.0069 -0.0108 -0.0086 60  ALA   A O   
1369 C CB  . ALA   A 60  ? 0.1412 0.1589 0.1935 -0.0075 -0.0124 -0.0211 60  ALA   A CB  
1375 N N   . MET   A 61  ? 0.1328 0.1350 0.1860 -0.0046 -0.0007 -0.0110 61  MET   A N   
1376 C CA  . MET   A 61  ? 0.1313 0.1315 0.1931 -0.0099 0.0025  0.0036  61  MET   A CA  
1377 C C   . MET   A 61  ? 0.1262 0.1282 0.1961 -0.0103 -0.0017 0.0019  61  MET   A C   
1378 O O   . MET   A 61  ? 0.1312 0.1306 0.1953 -0.0072 0.0097  0.0020  61  MET   A O   
1379 C CB  . MET   A 61  ? 0.1381 0.1282 0.1861 -0.0070 -0.0016 -0.0036 61  MET   A CB  
1380 C CG  . MET   A 61  ? 0.1382 0.1384 0.1983 -0.0069 -0.0047 -0.0032 61  MET   A CG  
1381 S SD  . MET   A 61  ? 0.1395 0.1446 0.2266 -0.0138 0.0034  -0.0134 61  MET   A SD  
1382 C CE  . MET   A 61  ? 0.1586 0.1640 0.2560 -0.0124 0.0192  -0.0168 61  MET   A CE  
1392 N N   . GLN   A 62  ? 0.1262 0.1221 0.2051 -0.0120 0.0001  -0.0043 62  GLN   A N   
1393 C CA  . GLN   A 62  ? 0.1339 0.1201 0.2076 -0.0079 0.0030  0.0087  62  GLN   A CA  
1394 C C   . GLN   A 62  ? 0.1321 0.1134 0.2025 -0.0015 0.0053  0.0049  62  GLN   A C   
1395 O O   . GLN   A 62  ? 0.1351 0.1322 0.1925 -0.0015 0.0101  -0.0008 62  GLN   A O   
1396 C CB  . GLN   A 62  ? 0.1348 0.1221 0.2199 -0.0068 0.0119  0.0036  62  GLN   A CB  
1397 C CG  . GLN   A 62  ? 0.1362 0.1225 0.2164 -0.0070 0.0073  0.0178  62  GLN   A CG  
1398 C CD  . GLN   A 62  ? 0.1420 0.1225 0.2149 -0.0082 0.0154  0.0104  62  GLN   A CD  
1399 O OE1 . GLN   A 62  ? 0.1409 0.1385 0.2159 -0.0063 0.0120  0.0067  62  GLN   A OE1 
1400 N NE2 . GLN   A 62  ? 0.1476 0.1334 0.2253 -0.0018 0.0120  -0.0012 62  GLN   A NE2 
1409 N N   . VAL   A 63  ? 0.1298 0.1253 0.2286 -0.0121 0.0084  -0.0182 63  VAL   A N   
1410 C CA  . VAL   A 63  ? 0.1335 0.1340 0.2485 -0.0189 0.0013  -0.0144 63  VAL   A CA  
1411 C C   . VAL   A 63  ? 0.1207 0.1341 0.2248 -0.0158 -0.0001 -0.0133 63  VAL   A C   
1412 O O   . VAL   A 63  ? 0.1243 0.1383 0.2426 -0.0148 -0.0027 -0.0082 63  VAL   A O   
1413 C CB  . VAL   A 63  ? 0.1474 0.1526 0.2722 -0.0161 -0.0002 -0.0382 63  VAL   A CB  
1414 C CG1 . VAL   A 63  ? 0.1648 0.1703 0.2943 -0.0158 -0.0120 -0.0499 63  VAL   A CG1 
1415 C CG2 . VAL   A 63  ? 0.1521 0.1485 0.2777 -0.0145 0.0136  -0.0394 63  VAL   A CG2 
1425 N N   . GLU   A 64  ? 0.1277 0.1456 0.2129 -0.0060 0.0055  -0.0100 64  GLU   A N   
1426 C CA  . GLU   A 64  ? 0.1234 0.1416 0.2172 -0.0055 -0.0035 -0.0045 64  GLU   A CA  
1427 C C   . GLU   A 64  ? 0.1219 0.1344 0.2124 -0.0089 0.0025  0.0014  64  GLU   A C   
1428 O O   . GLU   A 64  ? 0.1265 0.1413 0.2174 -0.0057 0.0024  -0.0061 64  GLU   A O   
1429 C CB  . GLU   A 64  ? 0.1333 0.1460 0.2193 -0.0098 -0.0015 -0.0032 64  GLU   A CB  
1430 C CG  . GLU   A 64  ? 0.1475 0.1591 0.2186 -0.0106 -0.0002 -0.0015 64  GLU   A CG  
1431 C CD  . GLU   A 64  ? 0.1574 0.1658 0.2278 -0.0201 0.0015  -0.0052 64  GLU   A CD  
1432 O OE1 . GLU   A 64  ? 0.1567 0.1789 0.2377 -0.0265 0.0134  0.0013  64  GLU   A OE1 
1433 O OE2 . GLU   A 64  ? 0.1650 0.1664 0.2230 -0.0272 -0.0083 0.0085  64  GLU   A OE2 
1440 N N   . SER   A 65  ? 0.1192 0.1366 0.2090 0.0015  -0.0037 -0.0008 65  SER   A N   
1441 C CA  . SER   A 65  ? 0.1288 0.1290 0.2025 -0.0043 -0.0049 -0.0008 65  SER   A CA  
1442 C C   . SER   A 65  ? 0.1285 0.1318 0.2040 -0.0098 0.0043  0.0010  65  SER   A C   
1443 O O   . SER   A 65  ? 0.1373 0.1385 0.2204 -0.0052 0.0149  -0.0047 65  SER   A O   
1444 C CB  . SER   A 65  ? 0.1259 0.1275 0.2023 -0.0077 -0.0036 0.0108  65  SER   A CB  
1445 O OG  . SER   A 65  ? 0.1243 0.1406 0.2085 -0.0055 -0.0019 0.0132  65  SER   A OG  
1451 N N   . ASP   A 66  ? 0.1304 0.1296 0.2124 -0.0081 0.0163  0.0090  66  ASP   A N   
1452 C CA  . ASP   A 66  ? 0.1424 0.1398 0.2281 -0.0060 0.0034  0.0178  66  ASP   A CA  
1453 C C   . ASP   A 66  ? 0.1369 0.1325 0.2402 -0.0089 0.0094  0.0167  66  ASP   A C   
1454 O O   . ASP   A 66  ? 0.1426 0.1435 0.2599 -0.0053 0.0293  0.0249  66  ASP   A O   
1455 C CB  . ASP   A 66  ? 0.1506 0.1490 0.2541 0.0069  0.0087  0.0322  66  ASP   A CB  
1456 C CG  . ASP   A 66  ? 0.1727 0.1621 0.2748 -0.0010 0.0033  0.0486  66  ASP   A CG  
1457 O OD1 . ASP   A 66  ? 0.1783 0.1909 0.2584 -0.0083 0.0011  0.0587  66  ASP   A OD1 
1458 O OD2 . ASP   A 66  ? 0.1843 0.1720 0.3502 0.0196  -0.0196 0.0251  66  ASP   A OD2 
1463 N N   . ASP   A 67  ? 0.1316 0.1320 0.2459 -0.0032 0.0080  0.0168  67  ASP   A N   
1464 C CA  . ASP   A 67  ? 0.1341 0.1520 0.2499 -0.0056 0.0059  0.0239  67  ASP   A CA  
1465 C C   . ASP   A 67  ? 0.1374 0.1517 0.2376 -0.0018 0.0139  0.0269  67  ASP   A C   
1466 O O   . ASP   A 67  ? 0.1346 0.1663 0.2472 0.0002  0.0265  0.0285  67  ASP   A O   
1467 C CB  . ASP   A 67  ? 0.1431 0.1622 0.2756 -0.0095 -0.0107 0.0236  67  ASP   A CB  
1468 C CG  . ASP   A 67  ? 0.1409 0.1759 0.3030 -0.0142 -0.0242 0.0259  67  ASP   A CG  
1469 O OD1 . ASP   A 67  ? 0.1459 0.1985 0.3695 -0.0153 -0.0291 0.0409  67  ASP   A OD1 
1470 O OD2 . ASP   A 67  ? 0.1445 0.1810 0.3001 -0.0033 -0.0144 0.0214  67  ASP   A OD2 
1475 N N   . TYR   A 68  ? 0.1360 0.1406 0.2373 0.0019  0.0185  0.0289  68  TYR   A N   
1476 C CA  . TYR   A 68  ? 0.1480 0.1442 0.2326 -0.0013 0.0262  0.0266  68  TYR   A CA  
1477 C C   . TYR   A 68  ? 0.1356 0.1445 0.2248 -0.0001 0.0294  0.0206  68  TYR   A C   
1478 O O   . TYR   A 68  ? 0.1423 0.1477 0.2317 0.0079  0.0346  0.0177  68  TYR   A O   
1479 C CB  . TYR   A 68  ? 0.1521 0.1349 0.2514 0.0033  0.0508  0.0335  68  TYR   A CB  
1480 C CG  . TYR   A 68  ? 0.1641 0.1508 0.2742 0.0020  0.0591  0.0347  68  TYR   A CG  
1481 C CD1 . TYR   A 68  ? 0.1681 0.1608 0.2954 -0.0135 0.0499  -0.0011 68  TYR   A CD1 
1482 C CD2 . TYR   A 68  ? 0.1847 0.1555 0.3012 0.0097  0.0587  0.0319  68  TYR   A CD2 
1483 C CE1 . TYR   A 68  ? 0.1731 0.1733 0.3164 -0.0167 0.0574  -0.0066 68  TYR   A CE1 
1484 C CE2 . TYR   A 68  ? 0.1799 0.1556 0.3170 0.0003  0.0689  0.0075  68  TYR   A CE2 
1485 C CZ  . TYR   A 68  ? 0.1765 0.1619 0.3302 -0.0231 0.0613  -0.0112 68  TYR   A CZ  
1486 O OH  . TYR   A 68  ? 0.2014 0.1650 0.3543 -0.0172 0.0382  -0.0356 68  TYR   A OH  
1496 N N   . ILE   A 69  ? 0.1286 0.1307 0.2175 -0.0040 0.0205  0.0162  69  ILE   A N   
1497 C CA  . ILE   A 69  ? 0.1358 0.1389 0.2090 0.0042  0.0188  0.0100  69  ILE   A CA  
1498 C C   . ILE   A 69  ? 0.1425 0.1432 0.2101 0.0038  0.0200  0.0271  69  ILE   A C   
1499 O O   . ILE   A 69  ? 0.1495 0.1494 0.2031 -0.0011 0.0223  0.0232  69  ILE   A O   
1500 C CB  . ILE   A 69  ? 0.1446 0.1618 0.2230 -0.0021 0.0176  0.0006  69  ILE   A CB  
1501 C CG1 . ILE   A 69  ? 0.1490 0.1738 0.2345 0.0054  0.0194  -0.0095 69  ILE   A CG1 
1502 C CG2 . ILE   A 69  ? 0.1639 0.1797 0.2397 0.0080  0.0004  -0.0064 69  ILE   A CG2 
1503 C CD1 . ILE   A 69  ? 0.1484 0.1813 0.2371 -0.0046 0.0178  -0.0141 69  ILE   A CD1 
1515 N N   . ALA   A 70  ? 0.1439 0.1431 0.2207 -0.0087 0.0196  0.0216  70  ALA   A N   
1516 C CA  . ALA   A 70  ? 0.1484 0.1551 0.2433 -0.0123 0.0267  0.0265  70  ALA   A CA  
1517 C C   . ALA   A 70  ? 0.1502 0.1682 0.2409 -0.0105 0.0382  0.0213  70  ALA   A C   
1518 O O   . ALA   A 70  ? 0.1650 0.2000 0.2603 0.0031  0.0532  0.0433  70  ALA   A O   
1519 C CB  . ALA   A 70  ? 0.1514 0.1486 0.2692 -0.0123 0.0232  0.0254  70  ALA   A CB  
1525 N N   . THR   A 71  ? 0.1427 0.1644 0.2371 -0.0061 0.0357  0.0238  71  THR   A N   
1526 C CA  . THR   A 71  ? 0.1513 0.1786 0.2601 0.0077  0.0213  0.0298  71  THR   A CA  
1527 C C   . THR   A 71  ? 0.1450 0.1779 0.2815 0.0126  0.0284  0.0290  71  THR   A C   
1528 O O   . THR   A 71  ? 0.1427 0.2071 0.3107 0.0077  0.0334  0.0011  71  THR   A O   
1529 C CB  . THR   A 71  ? 0.1764 0.2044 0.2771 0.0163  -0.0074 0.0324  71  THR   A CB  
1530 O OG1 . THR   A 71  ? 0.1978 0.2230 0.2850 0.0087  -0.0271 0.0198  71  THR   A OG1 
1531 C CG2 . THR   A 71  ? 0.1865 0.2211 0.3020 0.0251  -0.0192 0.0422  71  THR   A CG2 
1539 N N   . ASN   A 72  ? 0.1478 0.1607 0.2693 0.0105  0.0310  0.0246  72  ASN   A N   
1540 C CA  . ASN   A 72  ? 0.1524 0.1586 0.2698 0.0097  0.0391  0.0230  72  ASN   A CA  
1541 C C   . ASN   A 72  ? 0.1589 0.1558 0.2626 0.0086  0.0496  0.0170  72  ASN   A C   
1542 O O   . ASN   A 72  ? 0.1777 0.1578 0.2811 0.0162  0.0461  0.0083  72  ASN   A O   
1543 C CB  . ASN   A 72  ? 0.1709 0.1621 0.2577 0.0107  0.0379  0.0222  72  ASN   A CB  
1544 C CG  . ASN   A 72  ? 0.1954 0.1795 0.2479 0.0155  0.0329  0.0271  72  ASN   A CG  
1545 O OD1 . ASN   A 72  ? 0.2138 0.2189 0.2690 0.0157  0.0423  0.0282  72  ASN   A OD1 
1546 N ND2 . ASN   A 72  ? 0.2085 0.1838 0.2444 0.0488  0.0146  0.0164  72  ASN   A ND2 
1553 N N   . GLY   A 73  ? 0.1556 0.1557 0.2485 0.0008  0.0477  0.0096  73  GLY   A N   
1554 C CA  . GLY   A 73  ? 0.1648 0.1530 0.2355 -0.0040 0.0340  0.0173  73  GLY   A CA  
1555 C C   . GLY   A 73  ? 0.1675 0.1460 0.2080 0.0031  0.0510  0.0202  73  GLY   A C   
1556 O O   . GLY   A 73  ? 0.1655 0.1548 0.2249 0.0152  0.0430  0.0295  73  GLY   A O   
1560 N N   . PRO   A 74  ? 0.1778 0.1454 0.2170 -0.0080 0.0457  0.0125  74  PRO   A N   
1561 C CA  . PRO   A 74  ? 0.1687 0.1450 0.2357 -0.0055 0.0389  0.0217  74  PRO   A CA  
1562 C C   . PRO   A 74  ? 0.1610 0.1330 0.2245 -0.0042 0.0283  0.0088  74  PRO   A C   
1563 O O   . PRO   A 74  ? 0.1699 0.1409 0.2473 0.0048  0.0369  -0.0022 74  PRO   A O   
1564 C CB  . PRO   A 74  ? 0.1853 0.1730 0.2522 -0.0020 0.0369  0.0197  74  PRO   A CB  
1565 C CG  . PRO   A 74  ? 0.2126 0.2073 0.2736 -0.0244 0.0292  0.0060  74  PRO   A CG  
1566 C CD  . PRO   A 74  ? 0.1971 0.1828 0.2327 -0.0234 0.0325  0.0002  74  PRO   A CD  
1574 N N   . LEU   A 75  ? 0.1623 0.1258 0.1981 -0.0020 0.0238  0.0052  75  LEU   A N   
1575 C CA  . LEU   A 75  ? 0.1635 0.1296 0.1815 -0.0044 0.0167  0.0114  75  LEU   A CA  
1576 C C   . LEU   A 75  ? 0.1712 0.1413 0.1795 0.0033  0.0139  0.0191  75  LEU   A C   
1577 O O   . LEU   A 75  ? 0.2022 0.1592 0.1816 0.0131  0.0105  0.0077  75  LEU   A O   
1578 C CB  . LEU   A 75  ? 0.1688 0.1367 0.1828 -0.0128 0.0119  0.0161  75  LEU   A CB  
1579 C CG  . LEU   A 75  ? 0.1821 0.1630 0.2013 -0.0390 0.0022  0.0052  75  LEU   A CG  
1580 C CD1 . LEU   A 75  ? 0.1936 0.2143 0.2066 -0.0443 -0.0034 -0.0076 75  LEU   A CD1 
1581 C CD2 . LEU   A 75  ? 0.2040 0.2094 0.2410 -0.0114 0.0108  0.0189  75  LEU   A CD2 
1593 N N   . LYS   A 76  ? 0.1713 0.1343 0.2014 -0.0022 0.0102  0.0020  76  LYS   A N   
1594 C CA  . LYS   A 76  ? 0.1688 0.1536 0.2135 -0.0076 0.0135  -0.0069 76  LYS   A CA  
1595 C C   . LYS   A 76  ? 0.1641 0.1393 0.1773 0.0036  0.0124  0.0109  76  LYS   A C   
1596 O O   . LYS   A 76  ? 0.1691 0.1333 0.1822 -0.0015 0.0217  0.0124  76  LYS   A O   
1597 C CB  . LYS   A 76  ? 0.1687 0.1754 0.2551 0.0051  0.0173  -0.0374 76  LYS   A CB  
1598 C CG  . LYS   A 76  ? 0.1820 0.1709 0.2995 0.0061  0.0075  -0.0284 76  LYS   A CG  
1599 C CD  . LYS   A 76  ? 0.1868 0.1731 0.3432 0.0042  -0.0002 -0.0307 76  LYS   A CD  
1600 C CE  . LYS   A 76  ? 0.2066 0.1974 0.3853 -0.0019 0.0081  -0.0450 76  LYS   A CE  
1601 N NZ  . LYS   A 76  ? 0.2063 0.1893 0.4151 -0.0098 0.0127  -0.0556 76  LYS   A NZ  
1615 N N   . VAL   A 77  ? 0.1752 0.1520 0.1720 0.0009  0.0212  0.0198  77  VAL   A N   
1616 C CA  . VAL   A 77  ? 0.1718 0.1528 0.1812 0.0024  0.0191  0.0178  77  VAL   A CA  
1617 C C   . VAL   A 77  ? 0.1680 0.1494 0.1848 0.0077  0.0203  0.0082  77  VAL   A C   
1618 O O   . VAL   A 77  ? 0.1739 0.1496 0.1747 0.0113  0.0357  -0.0002 77  VAL   A O   
1619 C CB  . VAL   A 77  ? 0.1904 0.1724 0.1808 -0.0032 0.0155  0.0278  77  VAL   A CB  
1620 C CG1 . VAL   A 77  ? 0.1846 0.1930 0.2057 0.0059  0.0087  0.0097  77  VAL   A CG1 
1621 C CG2 . VAL   A 77  ? 0.2203 0.1824 0.2015 -0.0056 0.0051  0.0272  77  VAL   A CG2 
1631 N N   . GLY   A 78  ? 0.1622 0.1427 0.1728 0.0032  0.0240  0.0018  78  GLY   A N   
1632 C CA  . GLY   A 78  ? 0.1594 0.1444 0.1801 -0.0022 0.0302  0.0079  78  GLY   A CA  
1633 C C   . GLY   A 78  ? 0.1489 0.1312 0.1882 0.0017  0.0266  0.0121  78  GLY   A C   
1634 O O   . GLY   A 78  ? 0.1476 0.1375 0.2034 -0.0026 0.0199  0.0232  78  GLY   A O   
1638 N N   . GLY   A 79  ? 0.1488 0.1297 0.1801 0.0003  0.0198  0.0097  79  GLY   A N   
1639 C CA  . GLY   A 79  ? 0.1451 0.1387 0.1901 -0.0022 0.0212  0.0158  79  GLY   A CA  
1640 C C   . GLY   A 79  ? 0.1329 0.1283 0.1863 -0.0040 0.0161  0.0139  79  GLY   A C   
1641 O O   . GLY   A 79  ? 0.1400 0.1372 0.2094 0.0160  0.0154  0.0055  79  GLY   A O   
1645 N N   . SER   A 80  ? 0.1297 0.1414 0.2081 -0.0055 0.0134  0.0013  80  SER   A N   
1646 C CA  . SER   A 80  ? 0.1316 0.1377 0.1930 -0.0066 0.0106  0.0020  80  SER   A CA  
1647 C C   . SER   A 80  ? 0.1302 0.1358 0.1960 -0.0047 0.0064  0.0095  80  SER   A C   
1648 O O   . SER   A 80  ? 0.1335 0.1607 0.2267 0.0039  0.0098  0.0027  80  SER   A O   
1649 C CB  . SER   A 80  ? 0.1467 0.1419 0.2256 -0.0107 0.0103  0.0062  80  SER   A CB  
1650 O OG  . SER   A 80  ? 0.1677 0.1387 0.2566 0.0040  0.0011  0.0222  80  SER   A OG  
1656 N N   . CYS   A 81  ? 0.1295 0.1302 0.1939 -0.0042 -0.0021 0.0156  81  CYS   A N   
1657 C CA  . CYS   A 81  ? 0.1258 0.1430 0.1912 -0.0075 -0.0083 0.0259  81  CYS   A CA  
1658 C C   . CYS   A 81  ? 0.1278 0.1367 0.1904 -0.0113 -0.0001 0.0297  81  CYS   A C   
1659 O O   . CYS   A 81  ? 0.1257 0.1626 0.2016 0.0012  0.0044  0.0320  81  CYS   A O   
1660 C CB  . CYS   A 81  ? 0.1371 0.1424 0.2111 -0.0165 -0.0089 0.0287  81  CYS   A CB  
1661 S SG  . CYS   A 81  ? 0.1466 0.1347 0.2183 -0.0135 -0.0002 0.0142  81  CYS   A SG  
1667 N N   . VAL   A 82  ? 0.1335 0.1432 0.1847 -0.0018 -0.0106 0.0262  82  VAL   A N   
1668 C CA  . VAL   A 82  ? 0.1436 0.1546 0.1852 -0.0028 -0.0027 0.0304  82  VAL   A CA  
1669 C C   . VAL   A 82  ? 0.1411 0.1575 0.1959 -0.0050 -0.0080 0.0249  82  VAL   A C   
1670 O O   . VAL   A 82  ? 0.1345 0.1647 0.2273 -0.0037 -0.0051 0.0044  82  VAL   A O   
1671 C CB  . VAL   A 82  ? 0.1724 0.1655 0.1889 0.0000  -0.0006 0.0406  82  VAL   A CB  
1672 C CG1 . VAL   A 82  ? 0.1934 0.1789 0.2184 0.0022  0.0025  0.0344  82  VAL   A CG1 
1673 C CG2 . VAL   A 82  ? 0.1775 0.1724 0.2283 -0.0052 -0.0006 0.0313  82  VAL   A CG2 
1683 N N   . LEU   A 83  ? 0.1383 0.1477 0.1809 -0.0158 -0.0081 0.0085  83  LEU   A N   
1684 C CA  . LEU   A 83  ? 0.1431 0.1487 0.1828 -0.0157 -0.0097 0.0058  83  LEU   A CA  
1685 C C   . LEU   A 83  ? 0.1434 0.1568 0.1808 -0.0163 -0.0208 0.0167  83  LEU   A C   
1686 O O   . LEU   A 83  ? 0.1500 0.1648 0.1927 -0.0213 -0.0085 0.0179  83  LEU   A O   
1687 C CB  . LEU   A 83  ? 0.1483 0.1504 0.1881 -0.0188 -0.0088 0.0174  83  LEU   A CB  
1688 C CG  . LEU   A 83  ? 0.1607 0.1616 0.1918 -0.0167 0.0095  0.0045  83  LEU   A CG  
1689 C CD1 . LEU   A 83  ? 0.1720 0.1631 0.1834 -0.0226 -0.0005 0.0204  83  LEU   A CD1 
1690 C CD2 . LEU   A 83  ? 0.1613 0.1731 0.2016 -0.0144 0.0163  0.0064  83  LEU   A CD2 
1702 N N   . SER   A 84  ? 0.1527 0.1628 0.1873 -0.0198 -0.0153 0.0202  84  SER   A N   
1703 C CA  . SER   A 84  ? 0.1675 0.1697 0.1829 -0.0178 -0.0128 0.0103  84  SER   A CA  
1704 C C   . SER   A 84  ? 0.1687 0.1638 0.1705 -0.0258 -0.0060 0.0211  84  SER   A C   
1705 O O   . SER   A 84  ? 0.1609 0.1808 0.1664 -0.0204 -0.0101 0.0118  84  SER   A O   
1706 C CB  . SER   A 84  ? 0.1752 0.1886 0.1901 -0.0167 -0.0114 0.0103  84  SER   A CB  
1707 O OG  . SER   A 84  ? 0.1820 0.2103 0.1997 -0.0181 -0.0207 -0.0057 84  SER   A OG  
1713 N N   . GLY   A 85  ? 0.1894 0.1804 0.1646 -0.0277 0.0011  0.0084  85  GLY   A N   
1714 C CA  . GLY   A 85  ? 0.1925 0.1902 0.1717 -0.0332 0.0020  -0.0073 85  GLY   A CA  
1715 C C   . GLY   A 85  ? 0.1821 0.1980 0.1721 -0.0324 -0.0039 -0.0030 85  GLY   A C   
1716 O O   . GLY   A 85  ? 0.1856 0.2091 0.1830 -0.0336 0.0128  -0.0165 85  GLY   A O   
1720 N N   . HIS   A 86  ? 0.1810 0.1905 0.1631 -0.0301 -0.0048 0.0033  86  HIS   A N   
1721 C CA  . HIS   A 86  ? 0.1943 0.2005 0.1543 -0.0337 -0.0026 0.0039  86  HIS   A CA  
1722 C C   . HIS   A 86  ? 0.2155 0.2077 0.1536 -0.0373 -0.0073 0.0029  86  HIS   A C   
1723 O O   . HIS   A 86  ? 0.2269 0.2315 0.1564 -0.0304 0.0061  0.0135  86  HIS   A O   
1724 C CB  . HIS   A 86  ? 0.1929 0.1955 0.1653 -0.0240 0.0065  0.0060  86  HIS   A CB  
1725 C CG  . HIS   A 86  ? 0.1825 0.1860 0.1771 -0.0150 0.0007  0.0117  86  HIS   A CG  
1726 N ND1 . HIS   A 86  ? 0.1927 0.1853 0.2128 -0.0227 0.0056  0.0076  86  HIS   A ND1 
1727 C CD2 . HIS   A 86  ? 0.1867 0.1810 0.1752 -0.0037 0.0101  0.0086  86  HIS   A CD2 
1728 C CE1 . HIS   A 86  ? 0.1849 0.1831 0.2038 -0.0186 0.0184  0.0166  86  HIS   A CE1 
1729 N NE2 . HIS   A 86  ? 0.1880 0.1754 0.1904 -0.0024 0.0158  0.0254  86  HIS   A NE2 
1737 N N   . ASN   A 87  ? 0.2336 0.2133 0.1709 -0.0343 0.0144  -0.0195 87  ASN   A N   
1738 C CA  . ASN   A 87  ? 0.2476 0.2289 0.1803 -0.0278 0.0423  -0.0195 87  ASN   A CA  
1739 C C   . ASN   A 87  ? 0.2464 0.2462 0.1991 -0.0370 0.0486  -0.0068 87  ASN   A C   
1740 O O   . ASN   A 87  ? 0.2684 0.2679 0.2361 -0.0427 0.0738  -0.0160 87  ASN   A O   
1741 C CB  . ASN   A 87  ? 0.2634 0.2325 0.1778 -0.0250 0.0482  -0.0216 87  ASN   A CB  
1742 C CG  . ASN   A 87  ? 0.2754 0.2482 0.1802 -0.0157 0.0590  -0.0142 87  ASN   A CG  
1743 O OD1 . ASN   A 87  ? 0.2910 0.2521 0.1741 0.0064  0.0495  -0.0103 87  ASN   A OD1 
1744 N ND2 . ASN   A 87  ? 0.2785 0.2675 0.2065 -0.0156 0.0524  -0.0116 87  ASN   A ND2 
1751 N N   A LEU   A 88  ? 0.2268 0.2343 0.1865 -0.0441 0.0336  -0.0010 88  LEU   A N   
1752 N N   B LEU   A 88  ? 0.2327 0.2383 0.1892 -0.0408 0.0397  -0.0065 88  LEU   A N   
1753 C CA  A LEU   A 88  ? 0.2118 0.2296 0.1934 -0.0484 0.0325  0.0162  88  LEU   A CA  
1754 C CA  B LEU   A 88  ? 0.2211 0.2352 0.1952 -0.0417 0.0392  0.0016  88  LEU   A CA  
1755 C C   A LEU   A 88  ? 0.2083 0.2289 0.2000 -0.0465 0.0339  0.0210  88  LEU   A C   
1756 C C   B LEU   A 88  ? 0.2139 0.2316 0.1973 -0.0423 0.0358  0.0101  88  LEU   A C   
1757 O O   A LEU   A 88  ? 0.2161 0.2315 0.2246 -0.0415 0.0329  0.0312  88  LEU   A O   
1758 O O   B LEU   A 88  ? 0.2197 0.2340 0.2125 -0.0384 0.0357  0.0181  88  LEU   A O   
1759 C CB  A LEU   A 88  ? 0.2145 0.2305 0.2044 -0.0512 0.0030  0.0220  88  LEU   A CB  
1760 C CB  B LEU   A 88  ? 0.2252 0.2381 0.2051 -0.0400 0.0262  -0.0018 88  LEU   A CB  
1761 C CG  A LEU   A 88  ? 0.2277 0.2395 0.2262 -0.0482 0.0002  0.0230  88  LEU   A CG  
1762 C CG  B LEU   A 88  ? 0.2316 0.2447 0.2166 -0.0349 0.0273  -0.0064 88  LEU   A CG  
1763 C CD1 A LEU   A 88  ? 0.2356 0.2451 0.2312 -0.0454 -0.0040 0.0137  88  LEU   A CD1 
1764 C CD1 B LEU   A 88  ? 0.2341 0.2483 0.2157 -0.0325 0.0290  -0.0161 88  LEU   A CD1 
1765 C CD2 A LEU   A 88  ? 0.2366 0.2484 0.2560 -0.0426 -0.0004 0.0163  88  LEU   A CD2 
1766 C CD2 B LEU   A 88  ? 0.2361 0.2507 0.2327 -0.0301 0.0278  -0.0098 88  LEU   A CD2 
1789 N N   . ALA   A 89  ? 0.2071 0.2243 0.1875 -0.0427 0.0280  0.0020  89  ALA   A N   
1790 C CA  . ALA   A 89  ? 0.2135 0.2225 0.1700 -0.0394 0.0017  0.0147  89  ALA   A CA  
1791 C C   . ALA   A 89  ? 0.2233 0.2269 0.1811 -0.0356 -0.0153 0.0195  89  ALA   A C   
1792 O O   . ALA   A 89  ? 0.2158 0.2202 0.2154 -0.0425 -0.0228 0.0003  89  ALA   A O   
1793 C CB  . ALA   A 89  ? 0.2085 0.2204 0.1664 -0.0398 -0.0023 0.0174  89  ALA   A CB  
1800 N N   . LYS   A 90  ? 0.2374 0.2449 0.1772 -0.0421 -0.0273 0.0182  90  LYS   A N   
1801 C CA  . LYS   A 90  ? 0.2469 0.2601 0.1643 -0.0370 -0.0415 0.0180  90  LYS   A CA  
1802 C C   . LYS   A 90  ? 0.2213 0.2387 0.1485 -0.0366 -0.0404 0.0130  90  LYS   A C   
1803 O O   . LYS   A 90  ? 0.2191 0.2492 0.2010 -0.0410 -0.0450 0.0031  90  LYS   A O   
1804 C CB  . LYS   A 90  ? 0.2797 0.3006 0.2181 -0.0324 -0.0537 0.0304  90  LYS   A CB  
1805 C CG  . LYS   A 90  ? 0.3253 0.3408 0.3082 -0.0311 -0.0500 0.0370  90  LYS   A CG  
1806 C CD  . LYS   A 90  ? 0.3609 0.3721 0.4008 -0.0362 -0.0390 0.0416  90  LYS   A CD  
1807 C CE  . LYS   A 90  ? 0.3835 0.3889 0.4790 -0.0407 -0.0263 0.0366  90  LYS   A CE  
1808 N NZ  . LYS   A 90  ? 0.4179 0.4179 0.5230 -0.0450 -0.0179 0.0294  90  LYS   A NZ  
1822 N N   . HIS   A 91  ? 0.2129 0.2129 0.1107 -0.0318 -0.0394 0.0262  91  HIS   A N   
1823 C CA  . HIS   A 91  ? 0.1943 0.1891 0.1283 -0.0251 -0.0385 0.0221  91  HIS   A CA  
1824 C C   . HIS   A 91  ? 0.1734 0.1785 0.1244 -0.0226 -0.0239 0.0300  91  HIS   A C   
1825 O O   . HIS   A 91  ? 0.1653 0.1881 0.1625 -0.0309 -0.0133 0.0274  91  HIS   A O   
1826 C CB  . HIS   A 91  ? 0.2088 0.2191 0.2001 -0.0038 -0.0502 0.0188  91  HIS   A CB  
1827 C CG  . HIS   A 91  ? 0.2516 0.2704 0.2680 0.0042  -0.0656 0.0109  91  HIS   A CG  
1828 N ND1 . HIS   A 91  ? 0.2657 0.2985 0.3022 0.0078  -0.0818 -0.0097 91  HIS   A ND1 
1829 C CD2 . HIS   A 91  ? 0.2729 0.2954 0.2908 0.0105  -0.0731 0.0147  91  HIS   A CD2 
1830 C CE1 . HIS   A 91  ? 0.2768 0.3109 0.3207 0.0108  -0.0791 -0.0021 91  HIS   A CE1 
1831 N NE2 . HIS   A 91  ? 0.2843 0.3125 0.3161 0.0142  -0.0803 0.0062  91  HIS   A NE2 
1839 N N   . CYS   A 92  ? 0.1573 0.1689 0.1433 -0.0213 -0.0142 0.0220  92  CYS   A N   
1840 C CA  . CYS   A 92  ? 0.1525 0.1603 0.1545 -0.0155 -0.0036 0.0201  92  CYS   A CA  
1841 C C   . CYS   A 92  ? 0.1444 0.1514 0.1675 -0.0239 0.0041  0.0110  92  CYS   A C   
1842 O O   . CYS   A 92  ? 0.1417 0.1564 0.1748 -0.0233 -0.0011 0.0089  92  CYS   A O   
1843 C CB  . CYS   A 92  ? 0.1484 0.1578 0.1872 -0.0063 -0.0025 0.0073  92  CYS   A CB  
1844 S SG  . CYS   A 92  ? 0.1414 0.1443 0.1925 -0.0167 -0.0023 0.0133  92  CYS   A SG  
1850 N N   . LEU   A 93  ? 0.1453 0.1394 0.1773 -0.0158 0.0123  0.0126  93  LEU   A N   
1851 C CA  . LEU   A 93  ? 0.1298 0.1355 0.1724 -0.0087 -0.0055 0.0185  93  LEU   A CA  
1852 C C   . LEU   A 93  ? 0.1276 0.1272 0.1729 -0.0086 0.0047  0.0102  93  LEU   A C   
1853 O O   . LEU   A 93  ? 0.1230 0.1378 0.1679 -0.0089 0.0004  0.0107  93  LEU   A O   
1854 C CB  . LEU   A 93  ? 0.1359 0.1367 0.1873 -0.0085 -0.0113 0.0257  93  LEU   A CB  
1855 C CG  . LEU   A 93  ? 0.1462 0.1364 0.1923 -0.0084 -0.0046 0.0275  93  LEU   A CG  
1856 C CD1 . LEU   A 93  ? 0.1479 0.1425 0.2213 -0.0035 0.0112  0.0101  93  LEU   A CD1 
1857 C CD2 . LEU   A 93  ? 0.1522 0.1326 0.2047 -0.0125 -0.0114 0.0177  93  LEU   A CD2 
1869 N N   . HIS   A 94  ? 0.1211 0.1235 0.1641 -0.0098 0.0068  0.0177  94  HIS   A N   
1870 C CA  . HIS   A 94  ? 0.1234 0.1222 0.1734 -0.0073 0.0027  0.0193  94  HIS   A CA  
1871 C C   . HIS   A 94  ? 0.1174 0.1195 0.1800 -0.0104 0.0027  0.0093  94  HIS   A C   
1872 O O   . HIS   A 94  ? 0.1203 0.1403 0.2022 -0.0009 0.0024  -0.0072 94  HIS   A O   
1873 C CB  . HIS   A 94  ? 0.1204 0.1183 0.1767 -0.0028 -0.0016 0.0203  94  HIS   A CB  
1874 C CG  . HIS   A 94  ? 0.1233 0.1190 0.1790 -0.0078 -0.0010 0.0153  94  HIS   A CG  
1875 N ND1 . HIS   A 94  ? 0.1270 0.1201 0.1800 -0.0018 0.0003  0.0132  94  HIS   A ND1 
1876 C CD2 . HIS   A 94  ? 0.1327 0.1301 0.1837 -0.0092 -0.0051 0.0103  94  HIS   A CD2 
1877 C CE1 . HIS   A 94  ? 0.1321 0.1286 0.1829 -0.0111 -0.0072 0.0086  94  HIS   A CE1 
1878 N NE2 . HIS   A 94  ? 0.1389 0.1277 0.1656 -0.0151 -0.0028 0.0066  94  HIS   A NE2 
1886 N N   . VAL   A 95  ? 0.1189 0.1193 0.1478 -0.0041 0.0054  0.0060  95  VAL   A N   
1887 C CA  . VAL   A 95  ? 0.1242 0.1233 0.1548 -0.0062 0.0047  0.0094  95  VAL   A CA  
1888 C C   . VAL   A 95  ? 0.1270 0.1185 0.1558 -0.0147 0.0063  0.0126  95  VAL   A C   
1889 O O   . VAL   A 95  ? 0.1276 0.1324 0.1536 0.0050  0.0082  0.0101  95  VAL   A O   
1890 C CB  . VAL   A 95  ? 0.1273 0.1224 0.1776 -0.0094 0.0072  0.0152  95  VAL   A CB  
1891 C CG1 . VAL   A 95  ? 0.1414 0.1257 0.1870 -0.0147 0.0090  0.0065  95  VAL   A CG1 
1892 C CG2 . VAL   A 95  ? 0.1256 0.1339 0.1895 -0.0154 0.0119  0.0275  95  VAL   A CG2 
1902 N N   . VAL   A 96  ? 0.1293 0.1201 0.1538 -0.0050 0.0116  0.0128  96  VAL   A N   
1903 C CA  . VAL   A 96  ? 0.1382 0.1255 0.1512 -0.0057 0.0160  0.0209  96  VAL   A CA  
1904 C C   . VAL   A 96  ? 0.1448 0.1339 0.1651 -0.0011 0.0165  0.0188  96  VAL   A C   
1905 O O   . VAL   A 96  ? 0.1515 0.1413 0.1745 -0.0084 0.0204  -0.0007 96  VAL   A O   
1906 C CB  . VAL   A 96  ? 0.1426 0.1262 0.1690 -0.0052 0.0250  0.0179  96  VAL   A CB  
1907 C CG1 . VAL   A 96  ? 0.1597 0.1363 0.1659 -0.0030 0.0226  0.0121  96  VAL   A CG1 
1908 C CG2 . VAL   A 96  ? 0.1448 0.1334 0.1948 -0.0163 0.0174  0.0182  96  VAL   A CG2 
1918 N N   A GLY   A 97  ? 0.1406 0.1322 0.1607 -0.0041 0.0154  0.0161  97  GLY   A N   
1919 N N   B GLY   A 97  ? 0.1465 0.1415 0.1536 -0.0019 0.0091  0.0127  97  GLY   A N   
1920 C CA  A GLY   A 97  ? 0.1509 0.1475 0.1705 -0.0071 0.0012  0.0178  97  GLY   A CA  
1921 C CA  B GLY   A 97  ? 0.1540 0.1573 0.1544 -0.0046 0.0007  0.0167  97  GLY   A CA  
1922 C C   A GLY   A 97  ? 0.1536 0.1541 0.1501 -0.0070 0.0039  0.0124  97  GLY   A C   
1923 C C   B GLY   A 97  ? 0.1570 0.1670 0.1465 -0.0064 0.0034  0.0172  97  GLY   A C   
1924 O O   A GLY   A 97  ? 0.1635 0.1542 0.1649 -0.0058 0.0089  0.0059  97  GLY   A O   
1925 O O   B GLY   A 97  ? 0.1525 0.1685 0.1586 -0.0068 0.0110  0.0193  97  GLY   A O   
1932 N N   A PRO   A 98  ? 0.1521 0.1532 0.1311 -0.0049 0.0013  0.0108  98  PRO   A N   
1933 N N   B PRO   A 98  ? 0.1709 0.1666 0.1484 -0.0039 -0.0016 0.0218  98  PRO   A N   
1934 C CA  A PRO   A 98  ? 0.1531 0.1631 0.1240 -0.0015 0.0026  0.0040  98  PRO   A CA  
1935 C CA  B PRO   A 98  ? 0.1881 0.1765 0.1568 -0.0053 -0.0009 0.0072  98  PRO   A CA  
1936 C C   A PRO   A 98  ? 0.1516 0.1662 0.1192 -0.0091 0.0086  0.0039  98  PRO   A C   
1937 C C   B PRO   A 98  ? 0.2083 0.1857 0.1666 -0.0059 -0.0005 0.0128  98  PRO   A C   
1938 O O   A PRO   A 98  ? 0.1469 0.1616 0.1368 -0.0030 0.0169  0.0053  98  PRO   A O   
1939 O O   B PRO   A 98  ? 0.2047 0.1786 0.1827 -0.0034 0.0010  0.0097  98  PRO   A O   
1940 C CB  A PRO   A 98  ? 0.1637 0.1660 0.1244 0.0083  0.0049  -0.0012 98  PRO   A CB  
1941 C CB  B PRO   A 98  ? 0.1906 0.1745 0.1579 0.0012  -0.0006 0.0048  98  PRO   A CB  
1942 C CG  A PRO   A 98  ? 0.1624 0.1597 0.1386 0.0166  0.0031  -0.0049 98  PRO   A CG  
1943 C CG  B PRO   A 98  ? 0.1912 0.1704 0.1651 0.0013  -0.0007 0.0097  98  PRO   A CG  
1944 C CD  A PRO   A 98  ? 0.1567 0.1539 0.1395 0.0035  0.0053  -0.0022 98  PRO   A CD  
1945 C CD  B PRO   A 98  ? 0.1791 0.1657 0.1557 0.0006  0.0016  0.0219  98  PRO   A CD  
1960 N N   A ASN   A 99  ? 0.1571 0.1841 0.1166 -0.0118 0.0166  0.0211  99  ASN   A N   
1961 N N   B ASN   A 99  ? 0.2344 0.2010 0.1702 -0.0014 -0.0041 0.0244  99  ASN   A N   
1962 C CA  A ASN   A 99  ? 0.1767 0.1982 0.1123 -0.0099 0.0078  0.0377  99  ASN   A CA  
1963 C CA  B ASN   A 99  ? 0.2608 0.2204 0.1911 0.0037  -0.0002 0.0272  99  ASN   A CA  
1964 C C   A ASN   A 99  ? 0.1914 0.2298 0.0889 -0.0155 0.0081  0.0510  99  ASN   A C   
1965 C C   B ASN   A 99  ? 0.2777 0.2461 0.2033 0.0084  0.0010  0.0186  99  ASN   A C   
1966 O O   A ASN   A 99  ? 0.2053 0.2547 0.1002 -0.0097 0.0060  0.0336  99  ASN   A O   
1967 O O   B ASN   A 99  ? 0.2781 0.2355 0.1847 0.0136  -0.0000 0.0329  99  ASN   A O   
1968 C CB  A ASN   A 99  ? 0.1727 0.1892 0.1322 -0.0114 0.0049  0.0417  99  ASN   A CB  
1969 C CB  B ASN   A 99  ? 0.2684 0.2131 0.2156 0.0065  -0.0009 0.0426  99  ASN   A CB  
1970 C CG  A ASN   A 99  ? 0.1767 0.1858 0.1627 0.0057  -0.0107 0.0322  99  ASN   A CG  
1971 C CG  B ASN   A 99  ? 0.2754 0.2106 0.2304 0.0040  0.0024  0.0585  99  ASN   A CG  
1972 O OD1 A ASN   A 99  ? 0.1861 0.1899 0.1652 0.0092  -0.0111 0.0222  99  ASN   A OD1 
1973 O OD1 B ASN   A 99  ? 0.2773 0.2114 0.2218 0.0103  -0.0038 0.0716  99  ASN   A OD1 
1974 N ND2 A ASN   A 99  ? 0.1801 0.1865 0.1970 0.0141  -0.0210 0.0418  99  ASN   A ND2 
1975 N ND2 B ASN   A 99  ? 0.2776 0.2115 0.2624 0.0036  -0.0011 0.0558  99  ASN   A ND2 
1988 N N   A VAL   A 100 ? 0.2043 0.2445 0.1100 -0.0296 -0.0144 0.0414  100 VAL   A N   
1989 N N   B VAL   A 100 ? 0.2977 0.2842 0.2549 0.0106  0.0047  0.0091  100 VAL   A N   
1990 C CA  A VAL   A 100 ? 0.2353 0.2695 0.1583 -0.0365 -0.0248 0.0367  100 VAL   A CA  
1991 C CA  B VAL   A 100 ? 0.3178 0.3182 0.2997 0.0186  0.0026  0.0017  100 VAL   A CA  
1992 C C   A VAL   A 100 ? 0.2396 0.2838 0.1476 -0.0468 -0.0262 0.0613  100 VAL   A C   
1993 C C   B VAL   A 100 ? 0.3360 0.3444 0.3198 0.0238  0.0013  0.0041  100 VAL   A C   
1994 O O   A VAL   A 100 ? 0.2475 0.2975 0.1790 -0.0455 -0.0066 0.0614  100 VAL   A O   
1995 O O   B VAL   A 100 ? 0.3379 0.3538 0.3240 0.0257  -0.0009 0.0066  100 VAL   A O   
1996 C CB  A VAL   A 100 ? 0.2562 0.2780 0.2038 -0.0374 -0.0338 0.0283  100 VAL   A CB  
1997 C CB  B VAL   A 100 ? 0.3172 0.3226 0.3195 0.0214  0.0035  -0.0094 100 VAL   A CB  
1998 C CG1 A VAL   A 100 ? 0.2555 0.2859 0.2276 -0.0381 -0.0291 0.0329  100 VAL   A CG1 
1999 C CG1 B VAL   A 100 ? 0.3175 0.3254 0.3256 0.0219  0.0034  -0.0106 100 VAL   A CG1 
2000 C CG2 A VAL   A 100 ? 0.2680 0.2826 0.2107 -0.0342 -0.0413 0.0229  100 VAL   A CG2 
2001 C CG2 B VAL   A 100 ? 0.3186 0.3238 0.3265 0.0218  0.0029  -0.0131 100 VAL   A CG2 
2020 N N   A ASN   A 101 ? 0.2421 0.2889 0.1567 -0.0539 -0.0354 0.0826  101 ASN   A N   
2021 N N   B ASN   A 101 ? 0.3484 0.3568 0.3241 0.0265  0.0029  0.0102  101 ASN   A N   
2022 C CA  A ASN   A 101 ? 0.2610 0.2984 0.1740 -0.0594 -0.0325 0.0934  101 ASN   A CA  
2023 C CA  B ASN   A 101 ? 0.3578 0.3635 0.3289 0.0305  0.0049  0.0164  101 ASN   A CA  
2024 C C   A ASN   A 101 ? 0.2817 0.3238 0.1915 -0.0627 -0.0167 0.1037  101 ASN   A C   
2025 C C   B ASN   A 101 ? 0.3618 0.3613 0.3293 0.0328  0.0097  0.0231  101 ASN   A C   
2026 O O   A ASN   A 101 ? 0.2971 0.3272 0.2270 -0.0591 -0.0197 0.0958  101 ASN   A O   
2027 O O   B ASN   A 101 ? 0.3646 0.3645 0.3470 0.0346  0.0138  0.0177  101 ASN   A O   
2028 C CB  A ASN   A 101 ? 0.2627 0.2877 0.1699 -0.0567 -0.0449 0.0806  101 ASN   A CB  
2029 C CB  B ASN   A 101 ? 0.3620 0.3690 0.3280 0.0326  0.0042  0.0179  101 ASN   A CB  
2030 C CG  A ASN   A 101 ? 0.2667 0.2731 0.1641 -0.0563 -0.0478 0.0581  101 ASN   A CG  
2031 C CG  B ASN   A 101 ? 0.3650 0.3705 0.3303 0.0361  0.0053  0.0190  101 ASN   A CG  
2032 O OD1 A ASN   A 101 ? 0.2612 0.2817 0.1717 -0.0428 -0.0521 0.0383  101 ASN   A OD1 
2033 O OD1 B ASN   A 101 ? 0.3668 0.3698 0.3287 0.0395  0.0006  0.0197  101 ASN   A OD1 
2034 N ND2 A ASN   A 101 ? 0.2720 0.2590 0.1789 -0.0635 -0.0473 0.0589  101 ASN   A ND2 
2035 N ND2 B ASN   A 101 ? 0.3655 0.3726 0.3252 0.0358  0.0093  0.0182  101 ASN   A ND2 
2048 N N   A LYS   A 102 ? 0.2807 0.3486 0.2127 -0.0705 -0.0086 0.1041  102 LYS   A N   
2049 N N   B LYS   A 102 ? 0.3617 0.3553 0.3084 0.0307  0.0109  0.0273  102 LYS   A N   
2050 C CA  A LYS   A 102 ? 0.2891 0.3692 0.2217 -0.0742 -0.0086 0.0937  102 LYS   A CA  
2051 C CA  B LYS   A 102 ? 0.3621 0.3476 0.2903 0.0267  0.0099  0.0355  102 LYS   A CA  
2052 C C   A LYS   A 102 ? 0.2998 0.3844 0.2215 -0.0678 -0.0000 0.0770  102 LYS   A C   
2053 C C   B LYS   A 102 ? 0.3558 0.3342 0.2662 0.0215  0.0088  0.0485  102 LYS   A C   
2054 O O   A LYS   A 102 ? 0.3039 0.3902 0.2230 -0.0655 0.0121  0.0740  102 LYS   A O   
2055 O O   B LYS   A 102 ? 0.3571 0.3313 0.2639 0.0161  0.0070  0.0555  102 LYS   A O   
2056 C CB  A LYS   A 102 ? 0.2920 0.3723 0.2460 -0.0782 -0.0172 0.0951  102 LYS   A CB  
2057 C CB  B LYS   A 102 ? 0.3696 0.3555 0.3088 0.0223  0.0058  0.0290  102 LYS   A CB  
2058 C CG  A LYS   A 102 ? 0.2979 0.3703 0.2705 -0.0837 -0.0247 0.0934  102 LYS   A CG  
2059 C CG  B LYS   A 102 ? 0.3754 0.3605 0.3319 0.0189  -0.0017 0.0217  102 LYS   A CG  
2060 C CD  A LYS   A 102 ? 0.3073 0.3685 0.2933 -0.0884 -0.0333 0.0856  102 LYS   A CD  
2061 C CD  B LYS   A 102 ? 0.3826 0.3642 0.3522 0.0164  -0.0113 0.0135  102 LYS   A CD  
2062 C CE  A LYS   A 102 ? 0.3179 0.3700 0.3075 -0.0876 -0.0383 0.0801  102 LYS   A CE  
2063 C CE  B LYS   A 102 ? 0.3879 0.3674 0.3732 0.0163  -0.0199 0.0058  102 LYS   A CE  
2064 N NZ  A LYS   A 102 ? 0.3233 0.3696 0.3174 -0.0912 -0.0359 0.0728  102 LYS   A NZ  
2065 N NZ  B LYS   A 102 ? 0.3901 0.3688 0.3826 0.0163  -0.0271 0.0020  102 LYS   A NZ  
2092 N N   A GLY   A 103 ? 0.3058 0.3960 0.2384 -0.0593 0.0041  0.0551  103 GLY   A N   
2093 N N   B GLY   A 103 ? 0.3479 0.3245 0.2496 0.0214  0.0039  0.0483  103 GLY   A N   
2094 C CA  A GLY   A 103 ? 0.3146 0.4042 0.2550 -0.0490 0.0100  0.0351  103 GLY   A CA  
2095 C CA  B GLY   A 103 ? 0.3393 0.3160 0.2430 0.0184  -0.0015 0.0530  103 GLY   A CA  
2096 C C   A GLY   A 103 ? 0.3199 0.4136 0.2674 -0.0405 0.0212  0.0239  103 GLY   A C   
2097 C C   B GLY   A 103 ? 0.3276 0.3067 0.2266 0.0126  -0.0017 0.0579  103 GLY   A C   
2098 O O   A GLY   A 103 ? 0.3322 0.4171 0.2921 -0.0349 0.0215  0.0137  103 GLY   A O   
2099 O O   B GLY   A 103 ? 0.3336 0.3024 0.2297 0.0112  -0.0044 0.0619  103 GLY   A O   
2106 N N   A GLU   A 104 ? 0.3092 0.4159 0.2420 -0.0422 0.0383  0.0197  104 GLU   A N   
2107 N N   B GLU   A 104 ? 0.3111 0.3023 0.2172 0.0081  -0.0102 0.0561  104 GLU   A N   
2108 C CA  A GLU   A 104 ? 0.2972 0.4149 0.2287 -0.0458 0.0516  0.0150  104 GLU   A CA  
2109 C CA  B GLU   A 104 ? 0.2953 0.2966 0.2049 -0.0044 -0.0128 0.0563  104 GLU   A CA  
2110 C C   A GLU   A 104 ? 0.3048 0.4291 0.2224 -0.0457 0.0568  0.0009  104 GLU   A C   
2111 C C   B GLU   A 104 ? 0.2878 0.2968 0.2069 -0.0085 -0.0117 0.0402  104 GLU   A C   
2112 O O   A GLU   A 104 ? 0.3041 0.4336 0.2300 -0.0436 0.0457  0.0010  104 GLU   A O   
2113 O O   B GLU   A 104 ? 0.2869 0.2903 0.2126 -0.0073 -0.0108 0.0467  104 GLU   A O   
2114 C CB  A GLU   A 104 ? 0.2726 0.3988 0.2157 -0.0493 0.0624  0.0306  104 GLU   A CB  
2115 C CB  B GLU   A 104 ? 0.2881 0.2915 0.1969 -0.0100 -0.0091 0.0716  104 GLU   A CB  
2116 C CG  A GLU   A 104 ? 0.2543 0.3818 0.2131 -0.0487 0.0552  0.0404  104 GLU   A CG  
2117 C CG  B GLU   A 104 ? 0.2845 0.2910 0.2016 -0.0164 -0.0155 0.0776  104 GLU   A CG  
2118 C CD  A GLU   A 104 ? 0.2337 0.3626 0.2131 -0.0468 0.0491  0.0482  104 GLU   A CD  
2119 C CD  B GLU   A 104 ? 0.2778 0.2905 0.2033 -0.0207 -0.0222 0.0800  104 GLU   A CD  
2120 O OE1 A GLU   A 104 ? 0.2176 0.3520 0.1870 -0.0482 0.0414  0.0574  104 GLU   A OE1 
2121 O OE1 B GLU   A 104 ? 0.2755 0.2916 0.1971 -0.0208 -0.0288 0.0814  104 GLU   A OE1 
2122 O OE2 A GLU   A 104 ? 0.2418 0.3568 0.2264 -0.0409 0.0420  0.0514  104 GLU   A OE2 
2123 O OE2 B GLU   A 104 ? 0.2788 0.2895 0.2129 -0.0246 -0.0180 0.0817  104 GLU   A OE2 
2136 N N   A ASP   A 105 ? 0.3147 0.4365 0.2331 -0.0403 0.0617  -0.0243 105 ASP   A N   
2137 N N   B ASP   A 105 ? 0.2892 0.3053 0.2227 -0.0170 -0.0161 0.0198  105 ASP   A N   
2138 C CA  A ASP   A 105 ? 0.3195 0.4429 0.2579 -0.0380 0.0629  -0.0418 105 ASP   A CA  
2139 C CA  B ASP   A 105 ? 0.2915 0.3140 0.2430 -0.0163 -0.0127 -0.0051 105 ASP   A CA  
2140 C C   A ASP   A 105 ? 0.2929 0.4333 0.2412 -0.0481 0.0541  -0.0650 105 ASP   A C   
2141 C C   B ASP   A 105 ? 0.2858 0.3166 0.2227 -0.0274 -0.0107 -0.0226 105 ASP   A C   
2142 O O   A ASP   A 105 ? 0.2835 0.4310 0.2235 -0.0469 0.0564  -0.0875 105 ASP   A O   
2143 O O   B ASP   A 105 ? 0.2750 0.3138 0.1769 -0.0273 -0.0066 -0.0413 105 ASP   A O   
2144 C CB  A ASP   A 105 ? 0.3458 0.4548 0.3035 -0.0251 0.0643  -0.0398 105 ASP   A CB  
2145 C CB  B ASP   A 105 ? 0.3004 0.3213 0.2864 -0.0067 -0.0110 -0.0130 105 ASP   A CB  
2146 C CG  A ASP   A 105 ? 0.3693 0.4645 0.3438 -0.0136 0.0627  -0.0408 105 ASP   A CG  
2147 C CG  B ASP   A 105 ? 0.3099 0.3282 0.3198 0.0050  -0.0109 -0.0192 105 ASP   A CG  
2148 O OD1 A ASP   A 105 ? 0.3759 0.4704 0.3512 -0.0129 0.0611  -0.0494 105 ASP   A OD1 
2149 O OD1 B ASP   A 105 ? 0.3162 0.3290 0.3270 0.0062  -0.0123 -0.0222 105 ASP   A OD1 
2150 O OD2 A ASP   A 105 ? 0.3813 0.4669 0.3627 -0.0067 0.0647  -0.0336 105 ASP   A OD2 
2151 O OD2 B ASP   A 105 ? 0.3113 0.3325 0.3420 0.0097  -0.0170 -0.0200 105 ASP   A OD2 
2160 N N   A ILE   A 106 ? 0.2751 0.4251 0.2581 -0.0617 0.0256  -0.0674 106 ILE   A N   
2161 N N   B ILE   A 106 ? 0.2905 0.3220 0.2538 -0.0365 -0.0164 -0.0221 106 ILE   A N   
2162 C CA  A ILE   A 106 ? 0.2503 0.4107 0.2686 -0.0739 -0.0011 -0.0753 106 ILE   A CA  
2163 C CA  B ILE   A 106 ? 0.2972 0.3290 0.2826 -0.0470 -0.0254 -0.0226 106 ILE   A CA  
2164 C C   A ILE   A 106 ? 0.2294 0.3803 0.2714 -0.0961 0.0004  -0.1054 106 ILE   A C   
2165 C C   B ILE   A 106 ? 0.2983 0.3249 0.2785 -0.0528 -0.0160 -0.0217 106 ILE   A C   
2166 O O   A ILE   A 106 ? 0.2036 0.3710 0.2786 -0.1100 0.0144  -0.1152 106 ILE   A O   
2167 O O   B ILE   A 106 ? 0.2960 0.3302 0.2836 -0.0557 -0.0192 -0.0263 106 ILE   A O   
2168 C CB  A ILE   A 106 ? 0.2482 0.4220 0.2965 -0.0640 -0.0171 -0.0451 106 ILE   A CB  
2169 C CB  B ILE   A 106 ? 0.3036 0.3411 0.3206 -0.0519 -0.0390 -0.0155 106 ILE   A CB  
2170 C CG1 A ILE   A 106 ? 0.2398 0.4265 0.3186 -0.0547 -0.0223 -0.0238 106 ILE   A CG1 
2171 C CG1 B ILE   A 106 ? 0.3059 0.3502 0.3503 -0.0565 -0.0474 -0.0094 106 ILE   A CG1 
2172 C CG2 A ILE   A 106 ? 0.2525 0.4233 0.3007 -0.0658 -0.0210 -0.0418 106 ILE   A CG2 
2173 C CG2 B ILE   A 106 ? 0.3047 0.3409 0.3259 -0.0529 -0.0386 -0.0138 106 ILE   A CG2 
2174 C CD1 A ILE   A 106 ? 0.2389 0.4272 0.3295 -0.0448 -0.0158 -0.0136 106 ILE   A CD1 
2175 C CD1 B ILE   A 106 ? 0.3091 0.3523 0.3660 -0.0588 -0.0489 -0.0082 106 ILE   A CD1 
2198 N N   A GLN   A 107 ? 0.2446 0.3610 0.2911 -0.0935 0.0096  -0.1238 107 GLN   A N   
2199 N N   B GLN   A 107 ? 0.3038 0.3113 0.2862 -0.0487 -0.0006 -0.0181 107 GLN   A N   
2200 C CA  A GLN   A 107 ? 0.2651 0.3378 0.3486 -0.0757 0.0307  -0.1115 107 GLN   A CA  
2201 C CA  B GLN   A 107 ? 0.3111 0.3054 0.3198 -0.0434 0.0174  -0.0155 107 GLN   A CA  
2202 C C   A GLN   A 107 ? 0.2409 0.2854 0.3298 -0.0630 0.0525  -0.0910 107 GLN   A C   
2203 C C   B GLN   A 107 ? 0.2859 0.2733 0.2926 -0.0340 0.0323  -0.0057 107 GLN   A C   
2204 O O   A GLN   A 107 ? 0.2484 0.2725 0.3790 -0.0546 0.0648  -0.0910 107 GLN   A O   
2205 O O   B GLN   A 107 ? 0.2881 0.2723 0.3009 -0.0361 0.0355  -0.0064 107 GLN   A O   
2206 C CB  A GLN   A 107 ? 0.3048 0.3637 0.4296 -0.0735 0.0217  -0.1042 107 GLN   A CB  
2207 C CB  B GLN   A 107 ? 0.3385 0.3309 0.3826 -0.0493 0.0136  -0.0208 107 GLN   A CB  
2208 C CG  A GLN   A 107 ? 0.3380 0.3872 0.5163 -0.0691 0.0118  -0.0906 107 GLN   A CG  
2209 C CG  B GLN   A 107 ? 0.3606 0.3541 0.4466 -0.0535 0.0113  -0.0209 107 GLN   A CG  
2210 C CD  A GLN   A 107 ? 0.3629 0.4061 0.5900 -0.0664 0.0084  -0.0736 107 GLN   A CD  
2211 C CD  B GLN   A 107 ? 0.3780 0.3721 0.4989 -0.0548 0.0108  -0.0163 107 GLN   A CD  
2212 O OE1 A GLN   A 107 ? 0.3715 0.4090 0.6205 -0.0661 0.0090  -0.0713 107 GLN   A OE1 
2213 O OE1 B GLN   A 107 ? 0.3842 0.3787 0.5193 -0.0533 0.0137  -0.0129 107 GLN   A OE1 
2214 N NE2 A GLN   A 107 ? 0.3778 0.4160 0.6159 -0.0672 0.0058  -0.0686 107 GLN   A NE2 
2215 N NE2 B GLN   A 107 ? 0.3834 0.3792 0.5163 -0.0570 0.0071  -0.0167 107 GLN   A NE2 
2232 N N   A LEU   A 108 ? 0.2049 0.2319 0.2616 -0.0570 0.0558  -0.0885 108 LEU   A N   
2233 N N   B LEU   A 108 ? 0.2557 0.2416 0.2586 -0.0264 0.0396  -0.0062 108 LEU   A N   
2234 C CA  A LEU   A 108 ? 0.1909 0.1937 0.2377 -0.0390 0.0450  -0.0484 108 LEU   A CA  
2235 C CA  B LEU   A 108 ? 0.2255 0.2104 0.2349 -0.0110 0.0402  -0.0041 108 LEU   A CA  
2236 C C   A LEU   A 108 ? 0.1694 0.1568 0.2339 -0.0159 0.0424  -0.0172 108 LEU   A C   
2237 C C   B LEU   A 108 ? 0.1895 0.1748 0.2272 -0.0048 0.0401  -0.0044 108 LEU   A C   
2238 O O   A LEU   A 108 ? 0.1612 0.1443 0.2525 -0.0003 0.0433  0.0025  108 LEU   A O   
2239 O O   B LEU   A 108 ? 0.1855 0.1715 0.2296 0.0012  0.0474  0.0009  108 LEU   A O   
2240 C CB  A LEU   A 108 ? 0.1951 0.1998 0.2277 -0.0466 0.0531  -0.0409 108 LEU   A CB  
2241 C CB  B LEU   A 108 ? 0.2277 0.2188 0.2248 -0.0018 0.0457  -0.0047 108 LEU   A CB  
2242 C CG  A LEU   A 108 ? 0.2163 0.2233 0.2492 -0.0397 0.0525  -0.0325 108 LEU   A CG  
2243 C CG  B LEU   A 108 ? 0.2353 0.2301 0.2406 0.0042  0.0441  -0.0043 108 LEU   A CG  
2244 C CD1 A LEU   A 108 ? 0.2253 0.2277 0.2476 -0.0400 0.0536  -0.0226 108 LEU   A CD1 
2245 C CD1 B LEU   A 108 ? 0.2418 0.2332 0.2373 0.0004  0.0430  -0.0024 108 LEU   A CD1 
2246 C CD2 A LEU   A 108 ? 0.2265 0.2352 0.2798 -0.0364 0.0480  -0.0217 108 LEU   A CD2 
2247 C CD2 B LEU   A 108 ? 0.2386 0.2358 0.2580 0.0113  0.0420  -0.0034 108 LEU   A CD2 
2270 N N   . LEU   A 109 ? 0.1611 0.1537 0.2272 -0.0031 0.0302  -0.0026 109 LEU   A N   
2271 C CA  . LEU   A 109 ? 0.1543 0.1419 0.2134 -0.0015 0.0124  0.0085  109 LEU   A CA  
2272 C C   . LEU   A 109 ? 0.1373 0.1391 0.2090 -0.0069 0.0066  0.0062  109 LEU   A C   
2273 O O   . LEU   A 109 ? 0.1413 0.1306 0.2270 -0.0023 0.0028  -0.0003 109 LEU   A O   
2274 C CB  . LEU   A 109 ? 0.1573 0.1513 0.2280 0.0071  0.0073  0.0260  109 LEU   A CB  
2275 C CG  . LEU   A 109 ? 0.1481 0.1563 0.2408 0.0015  0.0133  0.0271  109 LEU   A CG  
2276 C CD1 . LEU   A 109 ? 0.1562 0.1467 0.2423 0.0033  0.0203  0.0056  109 LEU   A CD1 
2277 C CD2 . LEU   A 109 ? 0.1481 0.1702 0.2664 -0.0003 0.0079  0.0283  109 LEU   A CD2 
2290 N N   . LYS   A 110 ? 0.1397 0.1398 0.2110 -0.0087 -0.0035 0.0042  110 LYS   A N   
2291 C CA  . LYS   A 110 ? 0.1416 0.1294 0.2292 -0.0101 -0.0056 0.0059  110 LYS   A CA  
2292 C C   . LYS   A 110 ? 0.1421 0.1246 0.2186 -0.0077 0.0064  -0.0076 110 LYS   A C   
2293 O O   . LYS   A 110 ? 0.1379 0.1267 0.2113 -0.0125 0.0140  -0.0112 110 LYS   A O   
2294 C CB  . LYS   A 110 ? 0.1482 0.1357 0.2537 -0.0069 -0.0086 -0.0053 110 LYS   A CB  
2295 C CG  . LYS   A 110 ? 0.1506 0.1325 0.2590 -0.0009 -0.0107 -0.0036 110 LYS   A CG  
2296 C CD  . LYS   A 110 ? 0.1499 0.1442 0.2576 -0.0117 -0.0104 -0.0149 110 LYS   A CD  
2297 C CE  . LYS   A 110 ? 0.1596 0.1496 0.2731 -0.0110 0.0075  -0.0186 110 LYS   A CE  
2298 N NZ  . LYS   A 110 ? 0.1621 0.1522 0.2830 -0.0190 0.0138  -0.0172 110 LYS   A NZ  
2312 N N   . SER   A 111 ? 0.1408 0.1259 0.2063 -0.0052 0.0051  -0.0020 111 SER   A N   
2313 C CA  . SER   A 111 ? 0.1320 0.1318 0.2148 -0.0084 0.0089  -0.0031 111 SER   A CA  
2314 C C   . SER   A 111 ? 0.1276 0.1294 0.2263 -0.0112 0.0092  0.0058  111 SER   A C   
2315 O O   . SER   A 111 ? 0.1397 0.1237 0.2392 -0.0067 0.0128  0.0050  111 SER   A O   
2316 C CB  . SER   A 111 ? 0.1543 0.1608 0.2273 -0.0058 0.0178  -0.0117 111 SER   A CB  
2317 O OG  . SER   A 111 ? 0.1994 0.1791 0.2302 0.0080  0.0202  -0.0229 111 SER   A OG  
2323 N N   . ALA   A 112 ? 0.1370 0.1258 0.2217 -0.0072 0.0194  0.0003  112 ALA   A N   
2324 C CA  . ALA   A 112 ? 0.1357 0.1235 0.2139 -0.0055 0.0232  0.0007  112 ALA   A CA  
2325 C C   . ALA   A 112 ? 0.1329 0.1164 0.2309 -0.0054 0.0176  0.0003  112 ALA   A C   
2326 O O   . ALA   A 112 ? 0.1341 0.1186 0.2275 -0.0146 0.0186  0.0075  112 ALA   A O   
2327 C CB  . ALA   A 112 ? 0.1458 0.1271 0.2245 -0.0074 0.0183  -0.0005 112 ALA   A CB  
2333 N N   . TYR   A 113 ? 0.1279 0.1248 0.2236 -0.0070 0.0170  0.0081  113 TYR   A N   
2334 C CA  . TYR   A 113 ? 0.1228 0.1254 0.2180 -0.0062 0.0205  0.0149  113 TYR   A CA  
2335 C C   . TYR   A 113 ? 0.1199 0.1233 0.2184 -0.0116 0.0174  0.0057  113 TYR   A C   
2336 O O   . TYR   A 113 ? 0.1288 0.1272 0.2286 -0.0101 0.0170  0.0065  113 TYR   A O   
2337 C CB  . TYR   A 113 ? 0.1217 0.1374 0.2249 -0.0042 0.0089  0.0146  113 TYR   A CB  
2338 C CG  . TYR   A 113 ? 0.1291 0.1403 0.2151 -0.0204 0.0203  0.0156  113 TYR   A CG  
2339 C CD1 . TYR   A 113 ? 0.1268 0.1595 0.2108 -0.0069 0.0167  0.0128  113 TYR   A CD1 
2340 C CD2 . TYR   A 113 ? 0.1338 0.1403 0.2122 -0.0203 0.0132  0.0145  113 TYR   A CD2 
2341 C CE1 . TYR   A 113 ? 0.1343 0.1665 0.2178 -0.0113 0.0133  -0.0006 113 TYR   A CE1 
2342 C CE2 . TYR   A 113 ? 0.1316 0.1527 0.2059 -0.0152 0.0122  0.0157  113 TYR   A CE2 
2343 C CZ  . TYR   A 113 ? 0.1314 0.1567 0.2129 -0.0005 0.0153  0.0072  113 TYR   A CZ  
2344 O OH  . TYR   A 113 ? 0.1361 0.1643 0.2421 0.0014  0.0150  0.0012  113 TYR   A OH  
2354 N N   . GLU   A 114 ? 0.1223 0.1220 0.2160 -0.0068 0.0200  0.0063  114 GLU   A N   
2355 C CA  . GLU   A 114 ? 0.1304 0.1162 0.2344 -0.0013 0.0122  0.0131  114 GLU   A CA  
2356 C C   . GLU   A 114 ? 0.1267 0.1241 0.2334 -0.0040 0.0174  0.0080  114 GLU   A C   
2357 O O   . GLU   A 114 ? 0.1400 0.1262 0.2252 -0.0035 0.0120  0.0127  114 GLU   A O   
2358 C CB  . GLU   A 114 ? 0.1342 0.1233 0.2306 -0.0048 0.0140  0.0085  114 GLU   A CB  
2359 C CG  . GLU   A 114 ? 0.1379 0.1226 0.2447 -0.0010 0.0106  -0.0045 114 GLU   A CG  
2360 C CD  . GLU   A 114 ? 0.1425 0.1202 0.2505 -0.0079 0.0036  0.0027  114 GLU   A CD  
2361 O OE1 . GLU   A 114 ? 0.1437 0.1260 0.2571 -0.0124 0.0113  -0.0096 114 GLU   A OE1 
2362 O OE2 . GLU   A 114 ? 0.1606 0.1302 0.2625 -0.0136 0.0105  -0.0141 114 GLU   A OE2 
2369 N N   . ASN   A 115 ? 0.1304 0.1205 0.2168 -0.0107 0.0106  -0.0013 115 ASN   A N   
2370 C CA  . ASN   A 115 ? 0.1345 0.1284 0.2215 -0.0103 0.0107  0.0064  115 ASN   A CA  
2371 C C   . ASN   A 115 ? 0.1344 0.1284 0.2158 -0.0121 0.0044  0.0103  115 ASN   A C   
2372 O O   . ASN   A 115 ? 0.1364 0.1374 0.2137 -0.0130 0.0092  0.0168  115 ASN   A O   
2373 C CB  . ASN   A 115 ? 0.1382 0.1380 0.2080 -0.0173 0.0140  0.0032  115 ASN   A CB  
2374 C CG  . ASN   A 115 ? 0.1374 0.1573 0.2224 -0.0190 0.0160  0.0056  115 ASN   A CG  
2375 O OD1 . ASN   A 115 ? 0.1414 0.2544 0.2349 -0.0167 0.0227  0.0136  115 ASN   A OD1 
2376 N ND2 . ASN   A 115 ? 0.1377 0.1363 0.2252 -0.0149 0.0349  0.0060  115 ASN   A ND2 
2383 N N   . PHE   A 116 ? 0.1323 0.1282 0.2279 -0.0099 0.0120  0.0131  116 PHE   A N   
2384 C CA  . PHE   A 116 ? 0.1322 0.1385 0.2077 -0.0060 0.0196  0.0103  116 PHE   A CA  
2385 C C   . PHE   A 116 ? 0.1283 0.1427 0.2013 -0.0138 0.0212  0.0217  116 PHE   A C   
2386 O O   . PHE   A 116 ? 0.1318 0.1466 0.2130 -0.0042 0.0162  0.0232  116 PHE   A O   
2387 C CB  . PHE   A 116 ? 0.1292 0.1290 0.2167 -0.0089 0.0171  0.0189  116 PHE   A CB  
2388 C CG  . PHE   A 116 ? 0.1304 0.1276 0.2062 -0.0109 0.0177  0.0084  116 PHE   A CG  
2389 C CD1 . PHE   A 116 ? 0.1360 0.1294 0.2027 -0.0095 0.0169  0.0066  116 PHE   A CD1 
2390 C CD2 . PHE   A 116 ? 0.1387 0.1377 0.2111 -0.0091 0.0184  0.0123  116 PHE   A CD2 
2391 C CE1 . PHE   A 116 ? 0.1401 0.1297 0.2067 -0.0173 0.0175  0.0010  116 PHE   A CE1 
2392 C CE2 . PHE   A 116 ? 0.1344 0.1364 0.2174 -0.0075 0.0193  0.0048  116 PHE   A CE2 
2393 C CZ  . PHE   A 116 ? 0.1408 0.1277 0.2089 -0.0079 0.0072  0.0037  116 PHE   A CZ  
2403 N N   . ASN   A 117 ? 0.1318 0.1327 0.2171 -0.0130 0.0151  0.0195  117 ASN   A N   
2404 C CA  . ASN   A 117 ? 0.1331 0.1345 0.2389 -0.0075 0.0131  0.0243  117 ASN   A CA  
2405 C C   . ASN   A 117 ? 0.1331 0.1421 0.2515 -0.0071 0.0181  0.0229  117 ASN   A C   
2406 O O   . ASN   A 117 ? 0.1449 0.1495 0.2687 -0.0075 -0.0003 0.0446  117 ASN   A O   
2407 C CB  . ASN   A 117 ? 0.1344 0.1403 0.2409 -0.0063 0.0079  0.0329  117 ASN   A CB  
2408 C CG  . ASN   A 117 ? 0.1352 0.1371 0.2266 -0.0104 0.0111  0.0379  117 ASN   A CG  
2409 O OD1 . ASN   A 117 ? 0.1343 0.1558 0.2449 -0.0193 0.0063  0.0244  117 ASN   A OD1 
2410 N ND2 . ASN   A 117 ? 0.1323 0.1344 0.2240 -0.0065 0.0139  0.0268  117 ASN   A ND2 
2417 N N   . GLN   A 118 ? 0.1326 0.1468 0.2445 -0.0152 0.0041  0.0272  118 GLN   A N   
2418 C CA  . GLN   A 118 ? 0.1390 0.1523 0.2431 -0.0146 -0.0075 0.0316  118 GLN   A CA  
2419 C C   . GLN   A 118 ? 0.1452 0.1627 0.2406 -0.0180 -0.0028 0.0341  118 GLN   A C   
2420 O O   . GLN   A 118 ? 0.1426 0.1990 0.2652 -0.0084 -0.0127 0.0187  118 GLN   A O   
2421 C CB  . GLN   A 118 ? 0.1391 0.1589 0.2432 -0.0093 0.0085  0.0296  118 GLN   A CB  
2422 C CG  . GLN   A 118 ? 0.1354 0.1571 0.2490 -0.0082 0.0044  0.0249  118 GLN   A CG  
2423 C CD  . GLN   A 118 ? 0.1327 0.1572 0.2656 -0.0051 0.0070  0.0234  118 GLN   A CD  
2424 O OE1 . GLN   A 118 ? 0.1417 0.1707 0.2946 0.0036  -0.0048 0.0120  118 GLN   A OE1 
2425 N NE2 . GLN   A 118 ? 0.1448 0.1536 0.2552 -0.0006 0.0097  0.0228  118 GLN   A NE2 
2434 N N   . HIS   A 119 ? 0.1520 0.1565 0.2269 -0.0084 0.0080  0.0329  119 HIS   A N   
2435 C CA  . HIS   A 119 ? 0.1539 0.1665 0.2200 -0.0107 0.0051  0.0393  119 HIS   A CA  
2436 C C   . HIS   A 119 ? 0.1627 0.1766 0.2133 -0.0140 0.0044  0.0523  119 HIS   A C   
2437 O O   . HIS   A 119 ? 0.1618 0.1873 0.2205 -0.0300 -0.0120 0.0508  119 HIS   A O   
2438 C CB  . HIS   A 119 ? 0.1563 0.1707 0.2332 -0.0123 0.0158  0.0377  119 HIS   A CB  
2439 C CG  . HIS   A 119 ? 0.1587 0.1746 0.2691 -0.0095 0.0125  0.0479  119 HIS   A CG  
2440 N ND1 . HIS   A 119 ? 0.1722 0.1934 0.3190 -0.0188 0.0097  0.0324  119 HIS   A ND1 
2441 C CD2 . HIS   A 119 ? 0.1662 0.1764 0.2828 0.0049  0.0318  0.0594  119 HIS   A CD2 
2442 C CE1 . HIS   A 119 ? 0.1681 0.1839 0.3251 -0.0241 0.0166  0.0523  119 HIS   A CE1 
2443 N NE2 . HIS   A 119 ? 0.1789 0.1830 0.3230 -0.0069 0.0412  0.0603  119 HIS   A NE2 
2451 N N   . GLU   A 120 ? 0.1690 0.2027 0.2110 -0.0139 -0.0083 0.0775  120 GLU   A N   
2452 C CA  . GLU   A 120 ? 0.2003 0.2369 0.2380 -0.0062 -0.0134 0.1110  120 GLU   A CA  
2453 C C   . GLU   A 120 ? 0.1706 0.2237 0.2345 -0.0227 -0.0075 0.0995  120 GLU   A C   
2454 O O   . GLU   A 120 ? 0.1740 0.2184 0.2507 -0.0274 -0.0168 0.1001  120 GLU   A O   
2455 C CB  . GLU   A 120 ? 0.2693 0.3022 0.2989 0.0065  -0.0054 0.1459  120 GLU   A CB  
2456 C CG  . GLU   A 120 ? 0.3519 0.3685 0.3997 0.0166  0.0038  0.1383  120 GLU   A CG  
2457 C CD  . GLU   A 120 ? 0.4367 0.4374 0.5034 0.0262  0.0149  0.1223  120 GLU   A CD  
2458 O OE1 . GLU   A 120 ? 0.4564 0.4528 0.5335 0.0270  0.0177  0.1154  120 GLU   A OE1 
2459 O OE2 . GLU   A 120 ? 0.5036 0.5036 0.5533 0.0300  0.0181  0.1149  120 GLU   A OE2 
2466 N N   . VAL   A 121 ? 0.1659 0.2305 0.2078 -0.0261 -0.0002 0.0840  121 VAL   A N   
2467 C CA  . VAL   A 121 ? 0.1750 0.2331 0.1860 -0.0237 0.0129  0.0781  121 VAL   A CA  
2468 C C   . VAL   A 121 ? 0.1649 0.2117 0.1721 -0.0270 0.0054  0.0580  121 VAL   A C   
2469 O O   . VAL   A 121 ? 0.1674 0.2138 0.2034 -0.0365 -0.0104 0.0522  121 VAL   A O   
2470 C CB  . VAL   A 121 ? 0.2075 0.2677 0.2077 -0.0142 0.0212  0.0777  121 VAL   A CB  
2471 C CG1 . VAL   A 121 ? 0.2086 0.2810 0.2191 -0.0103 0.0265  0.0726  121 VAL   A CG1 
2472 C CG2 . VAL   A 121 ? 0.2239 0.2841 0.2368 -0.0220 0.0164  0.0618  121 VAL   A CG2 
2482 N N   . LEU   A 122 ? 0.1570 0.1836 0.1729 -0.0254 0.0019  0.0418  122 LEU   A N   
2483 C CA  . LEU   A 122 ? 0.1680 0.1669 0.1849 -0.0228 0.0191  0.0395  122 LEU   A CA  
2484 C C   . LEU   A 122 ? 0.1543 0.1686 0.1980 -0.0282 0.0076  0.0397  122 LEU   A C   
2485 O O   . LEU   A 122 ? 0.1575 0.1758 0.2159 -0.0340 -0.0024 0.0408  122 LEU   A O   
2486 C CB  . LEU   A 122 ? 0.1835 0.1631 0.2151 -0.0111 0.0124  0.0475  122 LEU   A CB  
2487 C CG  . LEU   A 122 ? 0.1830 0.1716 0.2180 -0.0129 0.0199  0.0283  122 LEU   A CG  
2488 C CD1 . LEU   A 122 ? 0.1993 0.1750 0.2180 -0.0268 0.0331  0.0392  122 LEU   A CD1 
2489 C CD2 . LEU   A 122 ? 0.1739 0.1664 0.2075 -0.0116 0.0338  0.0245  122 LEU   A CD2 
2501 N N   A LEU   A 123 ? 0.1506 0.1660 0.1911 -0.0295 0.0017  0.0375  123 LEU   A N   
2502 N N   B LEU   A 123 ? 0.1515 0.1677 0.1761 -0.0279 -0.0004 0.0247  123 LEU   A N   
2503 C CA  A LEU   A 123 ? 0.1527 0.1612 0.1667 -0.0242 0.0087  0.0378  123 LEU   A CA  
2504 C CA  B LEU   A 123 ? 0.1542 0.1660 0.1498 -0.0235 -0.0005 0.0126  123 LEU   A CA  
2505 C C   A LEU   A 123 ? 0.1426 0.1425 0.1711 -0.0225 0.0112  0.0385  123 LEU   A C   
2506 C C   B LEU   A 123 ? 0.1435 0.1581 0.1278 -0.0179 0.0043  0.0126  123 LEU   A C   
2507 O O   A LEU   A 123 ? 0.1335 0.1396 0.1840 -0.0236 0.0132  0.0200  123 LEU   A O   
2508 O O   B LEU   A 123 ? 0.1398 0.1588 0.1322 -0.0185 0.0123  -0.0003 123 LEU   A O   
2509 C CB  A LEU   A 123 ? 0.1620 0.1704 0.1579 -0.0263 0.0244  0.0470  123 LEU   A CB  
2510 C CB  B LEU   A 123 ? 0.1653 0.1743 0.1639 -0.0276 -0.0040 0.0159  123 LEU   A CB  
2511 C CG  A LEU   A 123 ? 0.1617 0.1846 0.1623 -0.0197 0.0199  0.0192  123 LEU   A CG  
2512 C CG  B LEU   A 123 ? 0.1670 0.1843 0.1662 -0.0313 -0.0007 0.0072  123 LEU   A CG  
2513 C CD1 A LEU   A 123 ? 0.1668 0.1930 0.1711 -0.0155 0.0229  0.0089  123 LEU   A CD1 
2514 C CD1 B LEU   A 123 ? 0.1703 0.1902 0.1751 -0.0326 0.0004  -0.0016 123 LEU   A CD1 
2515 C CD2 A LEU   A 123 ? 0.1644 0.1932 0.1612 -0.0152 0.0101  0.0216  123 LEU   A CD2 
2516 C CD2 B LEU   A 123 ? 0.1715 0.1888 0.1699 -0.0319 0.0031  0.0055  123 LEU   A CD2 
2539 N N   A ALA   A 124 ? 0.1467 0.1430 0.1630 -0.0263 0.0153  0.0352  124 ALA   A N   
2540 N N   B ALA   A 124 ? 0.1430 0.1530 0.1199 -0.0113 0.0022  0.0097  124 ALA   A N   
2541 C CA  A ALA   A 124 ? 0.1388 0.1416 0.1818 -0.0231 0.0182  0.0314  124 ALA   A CA  
2542 C CA  B ALA   A 124 ? 0.1320 0.1445 0.1204 -0.0008 0.0090  0.0131  124 ALA   A CA  
2543 C C   A ALA   A 124 ? 0.1289 0.1300 0.1782 -0.0132 0.0218  0.0161  124 ALA   A C   
2544 C C   B ALA   A 124 ? 0.1284 0.1429 0.1249 -0.0037 0.0194  0.0024  124 ALA   A C   
2545 O O   A ALA   A 124 ? 0.1301 0.1298 0.1854 -0.0116 0.0181  0.0140  124 ALA   A O   
2546 O O   B ALA   A 124 ? 0.1302 0.1429 0.1336 -0.0100 0.0299  0.0065  124 ALA   A O   
2547 C CB  A ALA   A 124 ? 0.1461 0.1372 0.2041 -0.0208 0.0106  0.0283  124 ALA   A CB  
2548 C CB  B ALA   A 124 ? 0.1271 0.1324 0.1341 0.0089  0.0012  0.0267  124 ALA   A CB  
2559 N N   A PRO   A 125 ? 0.1199 0.1216 0.1771 -0.0118 0.0143  0.0121  125 PRO   A N   
2560 N N   B PRO   A 125 ? 0.1331 0.1478 0.1314 -0.0028 0.0158  -0.0011 125 PRO   A N   
2561 C CA  A PRO   A 125 ? 0.1241 0.1239 0.1695 -0.0005 0.0155  0.0153  125 PRO   A CA  
2562 C CA  B PRO   A 125 ? 0.1472 0.1532 0.1355 -0.0028 0.0101  -0.0003 125 PRO   A CA  
2563 C C   A PRO   A 125 ? 0.1183 0.1301 0.1700 -0.0051 0.0145  0.0195  125 PRO   A C   
2564 C C   B PRO   A 125 ? 0.1498 0.1521 0.1296 -0.0079 0.0095  0.0003  125 PRO   A C   
2565 O O   A PRO   A 125 ? 0.1219 0.1322 0.1824 -0.0006 0.0113  0.0192  125 PRO   A O   
2566 O O   B PRO   A 125 ? 0.1499 0.1472 0.1410 -0.0086 0.0134  0.0083  125 PRO   A O   
2567 C CB  A PRO   A 125 ? 0.1281 0.1172 0.1642 -0.0050 0.0251  0.0187  125 PRO   A CB  
2568 C CB  B PRO   A 125 ? 0.1524 0.1563 0.1500 0.0013  0.0221  -0.0054 125 PRO   A CB  
2569 C CG  A PRO   A 125 ? 0.1230 0.1062 0.1614 -0.0029 0.0278  0.0073  125 PRO   A CG  
2570 C CG  B PRO   A 125 ? 0.1550 0.1546 0.1552 -0.0013 0.0168  -0.0019 125 PRO   A CG  
2571 C CD  A PRO   A 125 ? 0.1183 0.1100 0.1611 -0.0104 0.0228  0.0162  125 PRO   A CD  
2572 C CD  B PRO   A 125 ? 0.1421 0.1522 0.1438 -0.0013 0.0239  -0.0012 125 PRO   A CD  
2587 N N   A LEU   A 126 ? 0.1101 0.1426 0.1817 -0.0028 0.0118  0.0223  126 LEU   A N   
2588 N N   B LEU   A 126 ? 0.1535 0.1637 0.1353 -0.0106 0.0086  -0.0020 126 LEU   A N   
2589 C CA  A LEU   A 126 ? 0.1179 0.1388 0.1822 -0.0053 0.0088  0.0298  126 LEU   A CA  
2590 C CA  B LEU   A 126 ? 0.1588 0.1674 0.1502 -0.0127 0.0130  0.0001  126 LEU   A CA  
2591 C C   A LEU   A 126 ? 0.1295 0.1292 0.1772 -0.0053 -0.0038 0.0184  126 LEU   A C   
2592 C C   B LEU   A 126 ? 0.1714 0.1698 0.1556 -0.0153 0.0263  -0.0004 126 LEU   A C   
2593 O O   A LEU   A 126 ? 0.1393 0.1302 0.1754 -0.0038 -0.0026 0.0119  126 LEU   A O   
2594 O O   B LEU   A 126 ? 0.1842 0.1673 0.1967 -0.0216 0.0251  -0.0023 126 LEU   A O   
2595 C CB  A LEU   A 126 ? 0.1243 0.1555 0.1966 -0.0108 0.0001  0.0209  126 LEU   A CB  
2596 C CB  B LEU   A 126 ? 0.1617 0.1765 0.1690 -0.0090 0.0054  -0.0016 126 LEU   A CB  
2597 C CG  A LEU   A 126 ? 0.1259 0.1727 0.2106 -0.0216 0.0121  0.0076  126 LEU   A CG  
2598 C CG  B LEU   A 126 ? 0.1642 0.1866 0.1834 -0.0032 0.0148  -0.0050 126 LEU   A CG  
2599 C CD1 A LEU   A 126 ? 0.1292 0.1844 0.2246 -0.0228 0.0102  -0.0012 126 LEU   A CD1 
2600 C CD1 B LEU   A 126 ? 0.1633 0.1930 0.1932 0.0027  0.0180  -0.0145 126 LEU   A CD1 
2601 C CD2 A LEU   A 126 ? 0.1321 0.1739 0.2167 -0.0313 0.0149  0.0228  126 LEU   A CD2 
2602 C CD2 B LEU   A 126 ? 0.1715 0.1852 0.1896 -0.0030 0.0172  0.0036  126 LEU   A CD2 
2625 N N   A LEU   A 127 ? 0.1194 0.1421 0.1666 -0.0005 0.0014  0.0257  127 LEU   A N   
2626 N N   B LEU   A 127 ? 0.1731 0.1855 0.1429 -0.0158 0.0358  0.0090  127 LEU   A N   
2627 C CA  A LEU   A 127 ? 0.1139 0.1343 0.1525 0.0034  -0.0024 0.0240  127 LEU   A CA  
2628 C CA  B LEU   A 127 ? 0.1877 0.2001 0.1753 -0.0186 0.0294  0.0198  127 LEU   A CA  
2629 C C   A LEU   A 127 ? 0.1119 0.1226 0.1434 0.0014  0.0016  0.0191  127 LEU   A C   
2630 C C   B LEU   A 127 ? 0.2021 0.2151 0.1945 -0.0283 0.0129  0.0152  127 LEU   A C   
2631 O O   A LEU   A 127 ? 0.1093 0.1188 0.1627 0.0045  -0.0016 0.0232  127 LEU   A O   
2632 O O   B LEU   A 127 ? 0.2035 0.2146 0.1981 -0.0407 0.0090  0.0178  127 LEU   A O   
2633 C CB  A LEU   A 127 ? 0.1201 0.1433 0.1597 0.0069  0.0035  0.0223  127 LEU   A CB  
2634 C CB  B LEU   A 127 ? 0.1889 0.2027 0.1901 -0.0149 0.0384  0.0270  127 LEU   A CB  
2635 C CG  A LEU   A 127 ? 0.1270 0.1569 0.1678 0.0100  -0.0116 0.0310  127 LEU   A CG  
2636 C CG  B LEU   A 127 ? 0.1864 0.2029 0.2016 -0.0076 0.0346  0.0340  127 LEU   A CG  
2637 C CD1 A LEU   A 127 ? 0.1317 0.1435 0.1867 0.0038  -0.0010 0.0344  127 LEU   A CD1 
2638 C CD1 B LEU   A 127 ? 0.1868 0.2082 0.2139 -0.0037 0.0343  0.0358  127 LEU   A CD1 
2639 C CD2 A LEU   A 127 ? 0.1419 0.1698 0.1828 0.0160  -0.0149 0.0207  127 LEU   A CD2 
2640 C CD2 B LEU   A 127 ? 0.1878 0.2013 0.1979 -0.0011 0.0187  0.0285  127 LEU   A CD2 
2663 N N   A SER   A 128 ? 0.1200 0.1251 0.1530 -0.0086 0.0007  0.0188  128 SER   A N   
2664 N N   B SER   A 128 ? 0.2143 0.2330 0.2049 -0.0240 0.0107  0.0116  128 SER   A N   
2665 C CA  A SER   A 128 ? 0.1327 0.1208 0.1392 -0.0137 -0.0003 0.0208  128 SER   A CA  
2666 C CA  B SER   A 128 ? 0.2314 0.2510 0.2218 -0.0185 0.0069  0.0010  128 SER   A CA  
2667 C C   A SER   A 128 ? 0.1340 0.1211 0.1454 0.0015  -0.0144 0.0255  128 SER   A C   
2668 C C   B SER   A 128 ? 0.2462 0.2719 0.2617 -0.0147 -0.0057 -0.0089 128 SER   A C   
2669 O O   A SER   A 128 ? 0.1424 0.1281 0.1520 0.0066  -0.0226 0.0064  128 SER   A O   
2670 O O   B SER   A 128 ? 0.2484 0.2802 0.2852 -0.0198 -0.0015 -0.0264 128 SER   A O   
2671 C CB  A SER   A 128 ? 0.1356 0.1364 0.1595 -0.0089 0.0003  0.0183  128 SER   A CB  
2672 C CB  B SER   A 128 ? 0.2315 0.2491 0.2074 -0.0157 0.0126  0.0084  128 SER   A CB  
2673 O OG  A SER   A 128 ? 0.1383 0.1491 0.1771 -0.0029 0.0114  0.0194  128 SER   A OG  
2674 O OG  B SER   A 128 ? 0.2329 0.2469 0.1960 -0.0131 0.0223  0.0156  128 SER   A OG  
2685 N N   A ALA   A 129 ? 0.1243 0.1279 0.1546 0.0090  -0.0065 0.0362  129 ALA   A N   
2686 N N   B ALA   A 129 ? 0.2643 0.2917 0.2804 -0.0054 -0.0073 -0.0017 129 ALA   A N   
2687 C CA  A ALA   A 129 ? 0.1299 0.1333 0.1894 0.0105  -0.0074 0.0323  129 ALA   A CA  
2688 C CA  B ALA   A 129 ? 0.2814 0.3085 0.2932 0.0056  -0.0069 0.0023  129 ALA   A CA  
2689 C C   A ALA   A 129 ? 0.1448 0.1235 0.1838 0.0084  -0.0146 0.0175  129 ALA   A C   
2690 C C   B ALA   A 129 ? 0.2878 0.3174 0.3028 0.0168  -0.0074 0.0060  129 ALA   A C   
2691 O O   A ALA   A 129 ? 0.1509 0.1350 0.1913 -0.0018 -0.0115 0.0267  129 ALA   A O   
2692 O O   B ALA   A 129 ? 0.2838 0.3194 0.3128 0.0227  -0.0112 0.0055  129 ALA   A O   
2693 C CB  A ALA   A 129 ? 0.1329 0.1457 0.2049 0.0086  0.0076  0.0407  129 ALA   A CB  
2694 C CB  B ALA   A 129 ? 0.2891 0.3122 0.2955 0.0051  -0.0032 0.0018  129 ALA   A CB  
2705 N N   A GLY   A 130 ? 0.1568 0.1302 0.1797 0.0131  -0.0137 0.0102  130 GLY   A N   
2706 N N   B GLY   A 130 ? 0.2992 0.3248 0.3007 0.0190  -0.0056 0.0087  130 GLY   A N   
2707 C CA  A GLY   A 130 ? 0.1800 0.1399 0.1695 0.0060  -0.0102 0.0062  130 GLY   A CA  
2708 C CA  B GLY   A 130 ? 0.3098 0.3342 0.2984 0.0190  -0.0047 0.0127  130 GLY   A CA  
2709 C C   A GLY   A 130 ? 0.1751 0.1311 0.1674 0.0099  -0.0120 -0.0016 130 GLY   A C   
2710 C C   B GLY   A 130 ? 0.3164 0.3446 0.3039 0.0156  -0.0044 0.0150  130 GLY   A C   
2711 O O   A GLY   A 130 ? 0.1655 0.1401 0.1751 0.0118  -0.0147 0.0007  130 GLY   A O   
2712 O O   B GLY   A 130 ? 0.3178 0.3443 0.2988 0.0158  -0.0008 0.0176  130 GLY   A O   
2719 N N   A ILE   A 131 ? 0.1922 0.1333 0.1739 0.0040  -0.0147 0.0061  131 ILE   A N   
2720 N N   B ILE   A 131 ? 0.3223 0.3547 0.3214 0.0110  -0.0016 0.0115  131 ILE   A N   
2721 C CA  A ILE   A 131 ? 0.2041 0.1373 0.1499 -0.0074 -0.0272 0.0060  131 ILE   A CA  
2722 C CA  B ILE   A 131 ? 0.3288 0.3665 0.3410 0.0123  0.0013  0.0082  131 ILE   A CA  
2723 C C   A ILE   A 131 ? 0.1803 0.1377 0.1470 -0.0113 -0.0268 0.0238  131 ILE   A C   
2724 C C   B ILE   A 131 ? 0.3265 0.3751 0.3522 0.0138  -0.0023 0.0142  131 ILE   A C   
2725 O O   A ILE   A 131 ? 0.1843 0.1412 0.1633 -0.0018 -0.0316 0.0337  131 ILE   A O   
2726 O O   B ILE   A 131 ? 0.3253 0.3762 0.3631 0.0139  -0.0012 0.0145  131 ILE   A O   
2727 C CB  A ILE   A 131 ? 0.2414 0.1588 0.1506 -0.0176 -0.0195 -0.0086 131 ILE   A CB  
2728 C CB  B ILE   A 131 ? 0.3343 0.3681 0.3502 0.0134  0.0068  0.0052  131 ILE   A CB  
2729 C CG1 A ILE   A 131 ? 0.2520 0.1908 0.1686 -0.0339 -0.0221 -0.0191 131 ILE   A CG1 
2730 C CG1 B ILE   A 131 ? 0.3378 0.3698 0.3577 0.0120  0.0074  0.0067  131 ILE   A CG1 
2731 C CG2 A ILE   A 131 ? 0.2632 0.1468 0.1612 -0.0115 0.0004  -0.0142 131 ILE   A CG2 
2732 C CG2 B ILE   A 131 ? 0.3366 0.3688 0.3468 0.0142  0.0074  0.0027  131 ILE   A CG2 
2733 C CD1 A ILE   A 131 ? 0.2582 0.2041 0.1901 -0.0422 -0.0204 -0.0255 131 ILE   A CD1 
2734 C CD1 B ILE   A 131 ? 0.3401 0.3713 0.3662 0.0104  0.0078  0.0106  131 ILE   A CD1 
2757 N N   A PHE   A 132 ? 0.1645 0.1360 0.1415 -0.0118 -0.0241 0.0257  132 PHE   A N   
2758 N N   B PHE   A 132 ? 0.3228 0.3823 0.3460 0.0165  -0.0080 0.0251  132 PHE   A N   
2759 C CA  A PHE   A 132 ? 0.1677 0.1471 0.1428 -0.0154 -0.0089 0.0136  132 PHE   A CA  
2760 C CA  B PHE   A 132 ? 0.3185 0.3888 0.3360 0.0208  -0.0160 0.0414  132 PHE   A CA  
2761 C C   A PHE   A 132 ? 0.1690 0.1548 0.1482 -0.0083 -0.0156 0.0236  132 PHE   A C   
2762 C C   B PHE   A 132 ? 0.3332 0.3959 0.3424 0.0175  -0.0300 0.0375  132 PHE   A C   
2763 O O   A PHE   A 132 ? 0.1750 0.1673 0.1614 -0.0019 -0.0192 0.0272  132 PHE   A O   
2764 O O   B PHE   A 132 ? 0.3333 0.3958 0.3381 0.0142  -0.0417 0.0393  132 PHE   A O   
2765 C CB  A PHE   A 132 ? 0.1622 0.1349 0.1319 -0.0106 -0.0061 0.0148  132 PHE   A CB  
2766 C CB  B PHE   A 132 ? 0.3022 0.3874 0.3197 0.0274  -0.0070 0.0581  132 PHE   A CB  
2767 C CG  A PHE   A 132 ? 0.1569 0.1326 0.1328 0.0020  -0.0121 0.0086  132 PHE   A CG  
2768 C CG  B PHE   A 132 ? 0.2892 0.3870 0.3066 0.0329  0.0065  0.0733  132 PHE   A CG  
2769 C CD1 A PHE   A 132 ? 0.1599 0.1457 0.1593 0.0064  -0.0165 -0.0001 132 PHE   A CD1 
2770 C CD1 B PHE   A 132 ? 0.2847 0.3881 0.3074 0.0323  0.0097  0.0793  132 PHE   A CD1 
2771 C CD2 A PHE   A 132 ? 0.1552 0.1433 0.1380 0.0041  -0.0146 0.0171  132 PHE   A CD2 
2772 C CD2 B PHE   A 132 ? 0.2815 0.3863 0.3008 0.0357  0.0145  0.0821  132 PHE   A CD2 
2773 C CE1 A PHE   A 132 ? 0.1606 0.1474 0.1697 -0.0015 -0.0311 0.0016  132 PHE   A CE1 
2774 C CE1 B PHE   A 132 ? 0.2831 0.3900 0.3092 0.0319  0.0149  0.0823  132 PHE   A CE1 
2775 C CE2 A PHE   A 132 ? 0.1541 0.1446 0.1485 0.0024  -0.0290 0.0123  132 PHE   A CE2 
2776 C CE2 B PHE   A 132 ? 0.2802 0.3884 0.3033 0.0349  0.0150  0.0854  132 PHE   A CE2 
2777 C CZ  A PHE   A 132 ? 0.1536 0.1457 0.1610 -0.0134 -0.0316 0.0070  132 PHE   A CZ  
2778 C CZ  B PHE   A 132 ? 0.2808 0.3897 0.3094 0.0317  0.0159  0.0849  132 PHE   A CZ  
2797 N N   A GLY   A 133 ? 0.1617 0.1616 0.1318 -0.0073 -0.0296 0.0260  133 GLY   A N   
2798 N N   B GLY   A 133 ? 0.3466 0.4011 0.3653 0.0160  -0.0332 0.0313  133 GLY   A N   
2799 C CA  A GLY   A 133 ? 0.1712 0.1751 0.1329 -0.0156 -0.0322 0.0228  133 GLY   A CA  
2800 C CA  B GLY   A 133 ? 0.3602 0.4057 0.3885 0.0127  -0.0317 0.0257  133 GLY   A CA  
2801 C C   A GLY   A 133 ? 0.1747 0.1859 0.1278 -0.0200 -0.0373 0.0073  133 GLY   A C   
2802 C C   B GLY   A 133 ? 0.3725 0.4081 0.4114 0.0085  -0.0260 0.0220  133 GLY   A C   
2803 O O   A GLY   A 133 ? 0.1979 0.2000 0.1556 -0.0212 -0.0436 -0.0146 133 GLY   A O   
2804 O O   B GLY   A 133 ? 0.3746 0.4077 0.4266 0.0088  -0.0246 0.0214  133 GLY   A O   
2811 N N   A ALA   A 134 ? 0.1736 0.1671 0.1330 -0.0224 -0.0163 0.0058  134 ALA   A N   
2812 N N   B ALA   A 134 ? 0.3809 0.4095 0.4136 0.0053  -0.0203 0.0198  134 ALA   A N   
2813 C CA  A ALA   A 134 ? 0.1688 0.1657 0.1584 -0.0174 -0.0195 0.0027  134 ALA   A CA  
2814 C CA  B ALA   A 134 ? 0.3867 0.4103 0.4060 0.0022  -0.0134 0.0156  134 ALA   A CA  
2815 C C   A ALA   A 134 ? 0.1620 0.1709 0.1656 -0.0166 -0.0170 0.0116  134 ALA   A C   
2816 C C   B ALA   A 134 ? 0.3885 0.4082 0.3952 0.0014  -0.0090 0.0146  134 ALA   A C   
2817 O O   A ALA   A 134 ? 0.1736 0.1791 0.1861 -0.0141 0.0035  0.0119  134 ALA   A O   
2818 O O   B ALA   A 134 ? 0.3910 0.4094 0.3966 0.0017  -0.0094 0.0132  134 ALA   A O   
2819 C CB  A ALA   A 134 ? 0.1776 0.1600 0.1748 -0.0206 -0.0165 -0.0060 134 ALA   A CB  
2820 C CB  B ALA   A 134 ? 0.3888 0.4114 0.4096 0.0017  -0.0104 0.0144  134 ALA   A CB  
2831 N N   A ASP   A 135 ? 0.1683 0.1690 0.1638 -0.0233 -0.0254 0.0244  135 ASP   A N   
2832 N N   B ASP   A 135 ? 0.3886 0.4048 0.3783 0.0018  -0.0042 0.0150  135 ASP   A N   
2833 C CA  A ASP   A 135 ? 0.1657 0.1805 0.1923 -0.0315 -0.0322 0.0208  135 ASP   A CA  
2834 C CA  B ASP   A 135 ? 0.3874 0.4004 0.3641 0.0035  0.0006  0.0176  135 ASP   A CA  
2835 C C   A ASP   A 135 ? 0.1461 0.1678 0.1980 -0.0283 -0.0288 0.0294  135 ASP   A C   
2836 C C   B ASP   A 135 ? 0.3778 0.3902 0.3524 0.0079  -0.0000 0.0198  135 ASP   A C   
2837 O O   A ASP   A 135 ? 0.1468 0.1533 0.1959 -0.0235 -0.0360 0.0441  135 ASP   A O   
2838 O O   B ASP   A 135 ? 0.3774 0.3918 0.3503 0.0086  -0.0029 0.0159  135 ASP   A O   
2839 C CB  A ASP   A 135 ? 0.1940 0.2201 0.2265 -0.0477 -0.0458 0.0083  135 ASP   A CB  
2840 C CB  B ASP   A 135 ? 0.3954 0.4048 0.3649 0.0002  0.0090  0.0176  135 ASP   A CB  
2841 C CG  A ASP   A 135 ? 0.2094 0.2549 0.2682 -0.0603 -0.0582 -0.0003 135 ASP   A CG  
2842 C CG  B ASP   A 135 ? 0.4007 0.4068 0.3675 -0.0013 0.0141  0.0162  135 ASP   A CG  
2843 O OD1 A ASP   A 135 ? 0.1961 0.2666 0.2807 -0.0684 -0.0644 0.0147  135 ASP   A OD1 
2844 O OD1 B ASP   A 135 ? 0.4013 0.4076 0.3660 -0.0024 0.0165  0.0163  135 ASP   A OD1 
2845 O OD2 A ASP   A 135 ? 0.2423 0.2790 0.3154 -0.0570 -0.0329 -0.0008 135 ASP   A OD2 
2846 O OD2 B ASP   A 135 ? 0.4033 0.4069 0.3705 -0.0025 0.0132  0.0159  135 ASP   A OD2 
2855 N N   A PRO   A 136 ? 0.1310 0.1625 0.2050 -0.0037 -0.0096 0.0356  136 PRO   A N   
2856 N N   B PRO   A 136 ? 0.3667 0.3772 0.3414 0.0115  -0.0017 0.0261  136 PRO   A N   
2857 C CA  A PRO   A 136 ? 0.1260 0.1633 0.2137 -0.0039 0.0041  0.0153  136 PRO   A CA  
2858 C CA  B PRO   A 136 ? 0.3562 0.3644 0.3335 0.0137  -0.0017 0.0309  136 PRO   A CA  
2859 C C   A PRO   A 136 ? 0.1123 0.1580 0.2067 -0.0035 0.0056  0.0125  136 PRO   A C   
2860 C C   B PRO   A 136 ? 0.3409 0.3451 0.3296 0.0161  0.0023  0.0324  136 PRO   A C   
2861 O O   A PRO   A 136 ? 0.0970 0.1466 0.1870 -0.0070 0.0054  0.0218  136 PRO   A O   
2862 O O   B PRO   A 136 ? 0.3436 0.3491 0.3305 0.0159  0.0014  0.0335  136 PRO   A O   
2863 C CB  A PRO   A 136 ? 0.1517 0.1632 0.2313 0.0082  0.0087  0.0232  136 PRO   A CB  
2864 C CB  B PRO   A 136 ? 0.3600 0.3698 0.3346 0.0130  -0.0026 0.0300  136 PRO   A CB  
2865 C CG  A PRO   A 136 ? 0.1613 0.1748 0.2513 0.0146  0.0056  0.0253  136 PRO   A CG  
2866 C CG  B PRO   A 136 ? 0.3631 0.3732 0.3356 0.0131  -0.0039 0.0285  136 PRO   A CG  
2867 C CD  A PRO   A 136 ? 0.1450 0.1707 0.2273 0.0110  -0.0003 0.0393  136 PRO   A CD  
2868 C CD  B PRO   A 136 ? 0.3647 0.3760 0.3379 0.0129  -0.0031 0.0281  136 PRO   A CD  
2883 N N   A ILE   A 137 ? 0.1086 0.1593 0.2080 0.0027  -0.0098 0.0201  137 ILE   A N   
2884 N N   B ILE   A 137 ? 0.3222 0.3221 0.3205 0.0171  0.0031  0.0335  137 ILE   A N   
2885 C CA  A ILE   A 137 ? 0.1193 0.1671 0.2109 -0.0055 -0.0113 0.0286  137 ILE   A CA  
2886 C CA  B ILE   A 137 ? 0.2974 0.2975 0.3068 0.0159  0.0009  0.0314  137 ILE   A CA  
2887 C C   A ILE   A 137 ? 0.1173 0.1587 0.1978 -0.0201 -0.0116 0.0192  137 ILE   A C   
2888 C C   B ILE   A 137 ? 0.2640 0.2718 0.2772 0.0071  0.0008  0.0256  137 ILE   A C   
2889 O O   A ILE   A 137 ? 0.1197 0.1511 0.2180 -0.0202 -0.0116 0.0163  137 ILE   A O   
2890 O O   B ILE   A 137 ? 0.2616 0.2732 0.2805 0.0081  0.0004  0.0260  137 ILE   A O   
2891 C CB  A ILE   A 137 ? 0.1283 0.1849 0.2376 -0.0099 -0.0196 0.0314  137 ILE   A CB  
2892 C CB  B ILE   A 137 ? 0.3047 0.3016 0.3233 0.0246  -0.0020 0.0291  137 ILE   A CB  
2893 C CG1 A ILE   A 137 ? 0.1390 0.2122 0.2680 -0.0024 -0.0261 0.0227  137 ILE   A CG1 
2894 C CG1 B ILE   A 137 ? 0.3102 0.3047 0.3268 0.0277  0.0016  0.0231  137 ILE   A CG1 
2895 C CG2 A ILE   A 137 ? 0.1314 0.1851 0.2438 -0.0240 -0.0290 0.0360  137 ILE   A CG2 
2896 C CG2 B ILE   A 137 ? 0.3053 0.3017 0.3316 0.0295  -0.0048 0.0280  137 ILE   A CG2 
2897 C CD1 A ILE   A 137 ? 0.1529 0.2304 0.2902 0.0062  -0.0309 0.0181  137 ILE   A CD1 
2898 C CD1 B ILE   A 137 ? 0.3141 0.3071 0.3295 0.0281  0.0034  0.0165  137 ILE   A CD1 
2921 N N   A HIS   A 138 ? 0.1234 0.1736 0.2087 -0.0169 -0.0078 0.0231  138 HIS   A N   
2922 N N   B HIS   A 138 ? 0.2316 0.2466 0.2557 -0.0005 -0.0009 0.0169  138 HIS   A N   
2923 C CA  A HIS   A 138 ? 0.1382 0.1827 0.2101 -0.0198 0.0045  0.0215  138 HIS   A CA  
2924 C CA  B HIS   A 138 ? 0.2016 0.2181 0.2310 -0.0092 0.0002  0.0080  138 HIS   A CA  
2925 C C   A HIS   A 138 ? 0.1382 0.1761 0.2236 -0.0125 -0.0002 0.0224  138 HIS   A C   
2926 C C   B HIS   A 138 ? 0.1730 0.1968 0.2267 -0.0066 0.0011  0.0162  138 HIS   A C   
2927 O O   A HIS   A 138 ? 0.1408 0.1729 0.2310 -0.0167 0.0071  0.0144  138 HIS   A O   
2928 O O   B HIS   A 138 ? 0.1767 0.1988 0.2256 -0.0056 0.0039  0.0124  138 HIS   A O   
2929 C CB  A HIS   A 138 ? 0.1532 0.2056 0.2183 -0.0213 0.0051  0.0136  138 HIS   A CB  
2930 C CB  B HIS   A 138 ? 0.2002 0.2173 0.2247 -0.0157 -0.0071 -0.0112 138 HIS   A CB  
2931 C CG  A HIS   A 138 ? 0.1736 0.2182 0.2245 -0.0296 0.0006  0.0137  138 HIS   A CG  
2932 C CG  B HIS   A 138 ? 0.2006 0.2156 0.2264 -0.0243 -0.0107 -0.0254 138 HIS   A CG  
2933 N ND1 A HIS   A 138 ? 0.1871 0.2240 0.2378 -0.0350 0.0041  0.0099  138 HIS   A ND1 
2934 N ND1 B HIS   A 138 ? 0.2032 0.2169 0.2349 -0.0209 -0.0087 -0.0319 138 HIS   A ND1 
2935 C CD2 A HIS   A 138 ? 0.1767 0.2275 0.2255 -0.0242 0.0042  0.0230  138 HIS   A CD2 
2936 C CD2 B HIS   A 138 ? 0.1983 0.2124 0.2234 -0.0234 -0.0135 -0.0288 138 HIS   A CD2 
2937 C CE1 A HIS   A 138 ? 0.1915 0.2310 0.2426 -0.0228 0.0017  0.0147  138 HIS   A CE1 
2938 C CE1 B HIS   A 138 ? 0.2008 0.2141 0.2300 -0.0183 -0.0097 -0.0323 138 HIS   A CE1 
2939 N NE2 A HIS   A 138 ? 0.1853 0.2339 0.2334 -0.0206 0.0106  0.0193  138 HIS   A NE2 
2940 N NE2 B HIS   A 138 ? 0.1992 0.2136 0.2275 -0.0183 -0.0113 -0.0358 138 HIS   A NE2 
2955 N N   . SER   A 139 ? 0.1418 0.1746 0.2276 -0.0087 0.0041  0.0272  139 SER   A N   
2956 C CA  . SER   A 139 ? 0.1359 0.1677 0.2398 -0.0106 0.0082  0.0235  139 SER   A CA  
2957 C C   . SER   A 139 ? 0.1295 0.1585 0.2440 -0.0137 0.0155  0.0155  139 SER   A C   
2958 O O   . SER   A 139 ? 0.1252 0.1566 0.2478 -0.0174 0.0127  0.0182  139 SER   A O   
2959 C CB  . SER   A 139 ? 0.1368 0.1673 0.2392 -0.0170 0.0005  0.0268  139 SER   A CB  
2960 O OG  . SER   A 139 ? 0.1490 0.1706 0.2359 -0.0245 -0.0061 0.0231  139 SER   A OG  
2967 N N   . LEU   A 140 ? 0.1319 0.1614 0.2245 -0.0124 0.0019  0.0223  140 LEU   A N   
2968 C CA  . LEU   A 140 ? 0.1311 0.1595 0.2268 -0.0111 0.0005  0.0210  140 LEU   A CA  
2969 C C   . LEU   A 140 ? 0.1240 0.1664 0.2316 -0.0185 0.0052  0.0196  140 LEU   A C   
2970 O O   . LEU   A 140 ? 0.1274 0.1711 0.2453 -0.0118 0.0016  0.0279  140 LEU   A O   
2971 C CB  . LEU   A 140 ? 0.1376 0.1700 0.2211 -0.0128 -0.0065 0.0196  140 LEU   A CB  
2972 C CG  . LEU   A 140 ? 0.1379 0.1804 0.2180 -0.0189 0.0020  0.0312  140 LEU   A CG  
2973 C CD1 . LEU   A 140 ? 0.1479 0.1836 0.2236 -0.0136 0.0014  0.0247  140 LEU   A CD1 
2974 C CD2 . LEU   A 140 ? 0.1409 0.1993 0.2359 -0.0128 0.0072  0.0386  140 LEU   A CD2 
2986 N N   . ARG   A 141 ? 0.1337 0.1697 0.2401 -0.0169 0.0041  0.0146  141 ARG   A N   
2987 C CA  . ARG   A 141 ? 0.1440 0.1786 0.2509 -0.0215 -0.0027 -0.0045 141 ARG   A CA  
2988 C C   . ARG   A 141 ? 0.1455 0.1630 0.2485 -0.0174 -0.0013 0.0057  141 ARG   A C   
2989 O O   . ARG   A 141 ? 0.1431 0.1614 0.2560 -0.0196 0.0069  0.0073  141 ARG   A O   
2990 C CB  . ARG   A 141 ? 0.1668 0.2042 0.2652 -0.0338 -0.0046 -0.0199 141 ARG   A CB  
2991 C CG  . ARG   A 141 ? 0.2047 0.2473 0.2953 -0.0373 0.0065  -0.0262 141 ARG   A CG  
2992 C CD  . ARG   A 141 ? 0.2372 0.2761 0.3267 -0.0513 0.0032  -0.0254 141 ARG   A CD  
2993 N NE  . ARG   A 141 ? 0.2318 0.3027 0.3452 -0.0601 0.0023  -0.0086 141 ARG   A NE  
2994 C CZ  . ARG   A 141 ? 0.2392 0.3248 0.3446 -0.0737 0.0084  0.0040  141 ARG   A CZ  
2995 N NH1 . ARG   A 141 ? 0.2278 0.3319 0.3382 -0.0829 0.0252  -0.0092 141 ARG   A NH1 
2996 N NH2 . ARG   A 141 ? 0.2413 0.3445 0.3626 -0.0606 -0.0050 0.0123  141 ARG   A NH2 
3010 N N   . VAL   A 142 ? 0.1397 0.1552 0.2374 -0.0155 0.0047  0.0120  142 VAL   A N   
3011 C CA  . VAL   A 142 ? 0.1447 0.1506 0.2343 -0.0127 0.0146  0.0088  142 VAL   A CA  
3012 C C   . VAL   A 142 ? 0.1282 0.1468 0.2276 -0.0172 0.0110  0.0108  142 VAL   A C   
3013 O O   . VAL   A 142 ? 0.1350 0.1551 0.2450 -0.0069 0.0115  0.0150  142 VAL   A O   
3014 C CB  . VAL   A 142 ? 0.1482 0.1668 0.2327 -0.0186 0.0136  0.0092  142 VAL   A CB  
3015 C CG1 . VAL   A 142 ? 0.1517 0.1630 0.2357 -0.0193 0.0166  0.0117  142 VAL   A CG1 
3016 C CG2 . VAL   A 142 ? 0.1646 0.1841 0.2438 -0.0086 0.0079  0.0107  142 VAL   A CG2 
3026 N N   . CYS   A 143 ? 0.1345 0.1470 0.2192 -0.0142 0.0078  0.0099  143 CYS   A N   
3027 C CA  . CYS   A 143 ? 0.1312 0.1557 0.2237 -0.0142 0.0166  0.0127  143 CYS   A CA  
3028 C C   . CYS   A 143 ? 0.1324 0.1560 0.2383 -0.0144 0.0086  0.0211  143 CYS   A C   
3029 O O   . CYS   A 143 ? 0.1297 0.1593 0.2445 -0.0123 0.0088  0.0214  143 CYS   A O   
3030 C CB  . CYS   A 143 ? 0.1404 0.1568 0.2337 -0.0112 0.0261  0.0221  143 CYS   A CB  
3031 S SG  . CYS   A 143 ? 0.1554 0.1725 0.2209 -0.0026 0.0134  0.0083  143 CYS   A SG  
3037 N N   . VAL   A 144 ? 0.1301 0.1576 0.2525 -0.0184 0.0120  0.0290  144 VAL   A N   
3038 C CA  . VAL   A 144 ? 0.1401 0.1657 0.2909 -0.0196 0.0211  0.0302  144 VAL   A CA  
3039 C C   . VAL   A 144 ? 0.1421 0.1582 0.2868 -0.0275 -0.0126 0.0237  144 VAL   A C   
3040 O O   . VAL   A 144 ? 0.1537 0.1647 0.2956 -0.0151 -0.0136 0.0368  144 VAL   A O   
3041 C CB  . VAL   A 144 ? 0.1608 0.1919 0.3403 -0.0125 0.0333  0.0394  144 VAL   A CB  
3042 C CG1 . VAL   A 144 ? 0.1826 0.2164 0.3763 -0.0310 0.0136  0.0408  144 VAL   A CG1 
3043 C CG2 . VAL   A 144 ? 0.1426 0.1947 0.3394 -0.0063 0.0432  0.0546  144 VAL   A CG2 
3053 N N   . ASP   A 145 ? 0.1468 0.1573 0.2908 -0.0241 -0.0067 0.0115  145 ASP   A N   
3054 C CA  . ASP   A 145 ? 0.1582 0.1634 0.3021 -0.0263 -0.0054 0.0062  145 ASP   A CA  
3055 C C   . ASP   A 145 ? 0.1532 0.1530 0.2954 -0.0159 -0.0047 0.0020  145 ASP   A C   
3056 O O   . ASP   A 145 ? 0.1650 0.1560 0.3322 -0.0184 -0.0050 -0.0233 145 ASP   A O   
3057 C CB  . ASP   A 145 ? 0.1780 0.1908 0.3220 -0.0350 -0.0143 0.0123  145 ASP   A CB  
3058 C CG  . ASP   A 145 ? 0.1979 0.2298 0.3433 -0.0496 -0.0261 0.0240  145 ASP   A CG  
3059 O OD1 . ASP   A 145 ? 0.1919 0.2504 0.3482 -0.0691 -0.0210 0.0286  145 ASP   A OD1 
3060 O OD2 . ASP   A 145 ? 0.2098 0.2527 0.3599 -0.0543 -0.0508 0.0168  145 ASP   A OD2 
3065 N N   . THR   A 146 ? 0.1402 0.1427 0.2601 -0.0221 0.0020  0.0009  146 THR   A N   
3066 C CA  . THR   A 146 ? 0.1374 0.1372 0.2514 -0.0129 0.0037  0.0002  146 THR   A CA  
3067 C C   . THR   A 146 ? 0.1340 0.1330 0.2547 -0.0073 0.0072  0.0086  146 THR   A C   
3068 O O   . THR   A 146 ? 0.1441 0.1534 0.2633 0.0017  0.0005  0.0175  146 THR   A O   
3069 C CB  . THR   A 146 ? 0.1350 0.1424 0.2518 -0.0079 0.0049  0.0037  146 THR   A CB  
3070 O OG1 . THR   A 146 ? 0.1370 0.1524 0.2516 -0.0056 0.0040  -0.0090 146 THR   A OG1 
3071 C CG2 . THR   A 146 ? 0.1375 0.1468 0.2553 -0.0074 0.0072  0.0113  146 THR   A CG2 
3079 N N   . VAL   A 147 ? 0.1277 0.1386 0.2519 -0.0087 0.0050  0.0145  147 VAL   A N   
3080 C CA  . VAL   A 147 ? 0.1335 0.1426 0.2505 -0.0145 0.0197  0.0212  147 VAL   A CA  
3081 C C   . VAL   A 147 ? 0.1382 0.1437 0.2591 -0.0195 0.0136  0.0330  147 VAL   A C   
3082 O O   . VAL   A 147 ? 0.1385 0.1498 0.2882 -0.0209 0.0104  0.0374  147 VAL   A O   
3083 C CB  . VAL   A 147 ? 0.1465 0.1493 0.2404 -0.0234 0.0217  0.0259  147 VAL   A CB  
3084 C CG1 . VAL   A 147 ? 0.1733 0.1621 0.2369 -0.0172 0.0229  0.0319  147 VAL   A CG1 
3085 C CG2 . VAL   A 147 ? 0.1542 0.1474 0.2480 -0.0205 0.0067  0.0218  147 VAL   A CG2 
3095 N N   . ARG   A 148 ? 0.1348 0.1473 0.2663 -0.0224 0.0141  0.0435  148 ARG   A N   
3096 C CA  . ARG   A 148 ? 0.1425 0.1519 0.2615 -0.0195 0.0069  0.0490  148 ARG   A CA  
3097 C C   . ARG   A 148 ? 0.1542 0.1584 0.2599 -0.0254 0.0063  0.0605  148 ARG   A C   
3098 O O   . ARG   A 148 ? 0.1830 0.1702 0.2723 -0.0294 0.0226  0.0590  148 ARG   A O   
3099 C CB  . ARG   A 148 ? 0.1515 0.1557 0.2762 -0.0172 0.0160  0.0469  148 ARG   A CB  
3100 C CG  . ARG   A 148 ? 0.1704 0.1615 0.2929 -0.0132 0.0209  0.0458  148 ARG   A CG  
3101 C CD  . ARG   A 148 ? 0.1796 0.1526 0.3128 -0.0077 0.0309  0.0581  148 ARG   A CD  
3102 N NE  . ARG   A 148 ? 0.1679 0.1584 0.3245 0.0028  0.0396  0.0536  148 ARG   A NE  
3103 C CZ  . ARG   A 148 ? 0.1639 0.1450 0.3144 0.0004  0.0459  0.0453  148 ARG   A CZ  
3104 N NH1 . ARG   A 148 ? 0.1759 0.1471 0.3297 -0.0124 0.0435  0.0264  148 ARG   A NH1 
3105 N NH2 . ARG   A 148 ? 0.1630 0.1576 0.3234 0.0102  0.0497  0.0403  148 ARG   A NH2 
3119 N N   . THR   A 149 ? 0.1556 0.1646 0.2614 -0.0252 -0.0049 0.0552  149 THR   A N   
3120 C CA  . THR   A 149 ? 0.1584 0.1672 0.2576 -0.0157 -0.0003 0.0472  149 THR   A CA  
3121 C C   . THR   A 149 ? 0.1530 0.1607 0.2422 -0.0249 0.0090  0.0603  149 THR   A C   
3122 O O   . THR   A 149 ? 0.1490 0.1775 0.2475 -0.0303 0.0022  0.0528  149 THR   A O   
3123 C CB  . THR   A 149 ? 0.1602 0.1766 0.2522 -0.0188 0.0013  0.0466  149 THR   A CB  
3124 O OG1 . THR   A 149 ? 0.1595 0.1655 0.2714 -0.0334 0.0037  0.0406  149 THR   A OG1 
3125 C CG2 . THR   A 149 ? 0.1635 0.1889 0.2486 -0.0149 -0.0081 0.0344  149 THR   A CG2 
3133 N N   . ASN   A 150 ? 0.1555 0.1691 0.2382 -0.0189 0.0011  0.0687  150 ASN   A N   
3134 C CA  . ASN   A 150 ? 0.1671 0.1824 0.2344 -0.0171 0.0088  0.0567  150 ASN   A CA  
3135 C C   . ASN   A 150 ? 0.1520 0.1737 0.2338 -0.0224 0.0037  0.0509  150 ASN   A C   
3136 O O   . ASN   A 150 ? 0.1620 0.1832 0.2731 -0.0206 -0.0118 0.0470  150 ASN   A O   
3137 C CB  . ASN   A 150 ? 0.2040 0.2147 0.2507 -0.0277 0.0305  0.0719  150 ASN   A CB  
3138 C CG  . ASN   A 150 ? 0.2633 0.2498 0.3104 -0.0231 0.0085  0.0748  150 ASN   A CG  
3139 O OD1 . ASN   A 150 ? 0.2907 0.2589 0.3316 -0.0333 0.0056  0.0953  150 ASN   A OD1 
3140 N ND2 . ASN   A 150 ? 0.2932 0.2712 0.3335 -0.0141 -0.0020 0.0704  150 ASN   A ND2 
3147 N N   . VAL   A 151 ? 0.1473 0.1577 0.2260 -0.0217 0.0007  0.0530  151 VAL   A N   
3148 C CA  . VAL   A 151 ? 0.1514 0.1588 0.2181 -0.0177 0.0054  0.0464  151 VAL   A CA  
3149 C C   . VAL   A 151 ? 0.1440 0.1537 0.2312 -0.0301 0.0059  0.0459  151 VAL   A C   
3150 O O   . VAL   A 151 ? 0.1500 0.1656 0.2600 -0.0255 0.0072  0.0393  151 VAL   A O   
3151 C CB  . VAL   A 151 ? 0.1725 0.1759 0.2079 -0.0058 0.0111  0.0468  151 VAL   A CB  
3152 C CG1 . VAL   A 151 ? 0.1717 0.1997 0.2189 -0.0111 0.0053  0.0350  151 VAL   A CG1 
3153 C CG2 . VAL   A 151 ? 0.1899 0.1794 0.2098 -0.0046 0.0140  0.0435  151 VAL   A CG2 
3163 N N   . TYR   A 152 ? 0.1416 0.1579 0.2273 -0.0291 0.0042  0.0438  152 TYR   A N   
3164 C CA  . TYR   A 152 ? 0.1489 0.1716 0.1957 -0.0265 0.0087  0.0424  152 TYR   A CA  
3165 C C   . TYR   A 152 ? 0.1406 0.1643 0.1867 -0.0195 0.0141  0.0409  152 TYR   A C   
3166 O O   . TYR   A 152 ? 0.1503 0.1540 0.2079 -0.0319 0.0143  0.0300  152 TYR   A O   
3167 C CB  . TYR   A 152 ? 0.1665 0.1859 0.2060 -0.0259 0.0116  0.0504  152 TYR   A CB  
3168 C CG  . TYR   A 152 ? 0.1735 0.2016 0.1945 -0.0251 0.0148  0.0659  152 TYR   A CG  
3169 C CD1 . TYR   A 152 ? 0.1789 0.2275 0.2230 -0.0210 0.0192  0.0664  152 TYR   A CD1 
3170 C CD2 . TYR   A 152 ? 0.1770 0.2097 0.2009 -0.0388 0.0106  0.0483  152 TYR   A CD2 
3171 C CE1 . TYR   A 152 ? 0.2082 0.2401 0.2301 -0.0162 0.0130  0.0769  152 TYR   A CE1 
3172 C CE2 . TYR   A 152 ? 0.2041 0.2282 0.2144 -0.0343 0.0151  0.0562  152 TYR   A CE2 
3173 C CZ  . TYR   A 152 ? 0.2260 0.2376 0.2182 -0.0267 0.0127  0.0787  152 TYR   A CZ  
3174 O OH  . TYR   A 152 ? 0.2579 0.2611 0.2470 -0.0216 0.0170  0.0985  152 TYR   A OH  
3184 N N   A LEU   A 153 ? 0.1335 0.1566 0.1937 -0.0195 0.0202  0.0464  153 LEU   A N   
3185 N N   B LEU   A 153 ? 0.1406 0.1640 0.1751 -0.0257 0.0122  0.0344  153 LEU   A N   
3186 C CA  A LEU   A 153 ? 0.1316 0.1403 0.2079 -0.0052 0.0214  0.0371  153 LEU   A CA  
3187 C CA  B LEU   A 153 ? 0.1352 0.1528 0.1651 -0.0177 0.0102  0.0202  153 LEU   A CA  
3188 C C   A LEU   A 153 ? 0.1398 0.1365 0.1980 -0.0054 0.0327  0.0343  153 LEU   A C   
3189 C C   B LEU   A 153 ? 0.1392 0.1627 0.1647 -0.0188 0.0151  0.0137  153 LEU   A C   
3190 O O   A LEU   A 153 ? 0.1467 0.1433 0.2077 -0.0093 0.0410  0.0252  153 LEU   A O   
3191 O O   B LEU   A 153 ? 0.1372 0.1704 0.1438 -0.0242 0.0226  0.0089  153 LEU   A O   
3192 C CB  A LEU   A 153 ? 0.1292 0.1359 0.2228 -0.0114 0.0207  0.0276  153 LEU   A CB  
3193 C CB  B LEU   A 153 ? 0.1277 0.1380 0.1623 -0.0081 0.0045  0.0248  153 LEU   A CB  
3194 C CG  A LEU   A 153 ? 0.1302 0.1403 0.2264 -0.0053 0.0313  0.0218  153 LEU   A CG  
3195 C CG  B LEU   A 153 ? 0.1324 0.1287 0.1606 0.0004  0.0055  0.0361  153 LEU   A CG  
3196 C CD1 A LEU   A 153 ? 0.1431 0.1362 0.2309 0.0015  0.0222  0.0183  153 LEU   A CD1 
3197 C CD1 B LEU   A 153 ? 0.1384 0.1356 0.1633 0.0005  0.0130  0.0338  153 LEU   A CD1 
3198 C CD2 A LEU   A 153 ? 0.1364 0.1449 0.2219 -0.0022 0.0421  0.0084  153 LEU   A CD2 
3199 C CD2 B LEU   A 153 ? 0.1397 0.1258 0.1819 -0.0003 0.0077  0.0224  153 LEU   A CD2 
3222 N N   A ALA   A 154 ? 0.1370 0.1324 0.1994 0.0002  0.0254  0.0371  154 ALA   A N   
3223 N N   B ALA   A 154 ? 0.1395 0.1656 0.1669 -0.0147 0.0220  0.0131  154 ALA   A N   
3224 C CA  A ALA   A 154 ? 0.1497 0.1338 0.2004 -0.0045 0.0316  0.0314  154 ALA   A CA  
3225 C CA  B ALA   A 154 ? 0.1489 0.1634 0.1799 -0.0160 0.0247  0.0104  154 ALA   A CA  
3226 C C   A ALA   A 154 ? 0.1430 0.1286 0.1998 0.0040  0.0285  0.0309  154 ALA   A C   
3227 C C   B ALA   A 154 ? 0.1511 0.1632 0.1884 -0.0158 0.0197  0.0090  154 ALA   A C   
3228 O O   A ALA   A 154 ? 0.1358 0.1321 0.1906 -0.0026 0.0276  0.0281  154 ALA   A O   
3229 O O   B ALA   A 154 ? 0.1541 0.1624 0.1814 -0.0175 0.0232  0.0101  154 ALA   A O   
3230 C CB  A ALA   A 154 ? 0.1627 0.1454 0.2117 0.0027  0.0334  0.0153  154 ALA   A CB  
3231 C CB  B ALA   A 154 ? 0.1541 0.1671 0.1917 -0.0124 0.0220  -0.0027 154 ALA   A CB  
3242 N N   A VAL   A 155 ? 0.1321 0.1194 0.1900 0.0113  0.0363  0.0473  155 VAL   A N   
3243 N N   B VAL   A 155 ? 0.1451 0.1617 0.1988 -0.0146 0.0244  0.0262  155 VAL   A N   
3244 C CA  A VAL   A 155 ? 0.1454 0.1347 0.2145 0.0108  0.0347  0.0465  155 VAL   A CA  
3245 C CA  B VAL   A 155 ? 0.1547 0.1782 0.2219 -0.0112 0.0238  0.0285  155 VAL   A CA  
3246 C CA  T VAL   A 155 ? 0.1693 0.1666 0.1969 -0.0141 0.0269  0.0320  155 VAL   A CA  
3247 C C   A VAL   A 155 ? 0.1583 0.1502 0.2323 0.0236  0.0397  0.0546  155 VAL   A C   
3248 C C   B VAL   A 155 ? 0.1598 0.1901 0.2474 -0.0031 0.0249  0.0358  155 VAL   A C   
3249 C C   T VAL   A 155 ? 0.1714 0.1668 0.1907 -0.0091 0.0291  0.0357  155 VAL   A C   
3250 O O   A VAL   A 155 ? 0.1577 0.1558 0.2455 0.0299  0.0533  0.0499  155 VAL   A O   
3251 O O   B VAL   A 155 ? 0.1609 0.2000 0.2576 0.0007  0.0301  0.0320  155 VAL   A O   
3252 O O   T VAL   A 155 ? 0.1711 0.1724 0.1896 -0.0064 0.0297  0.0290  155 VAL   A O   
3253 C CB  A VAL   A 155 ? 0.1464 0.1437 0.2154 0.0120  0.0148  0.0406  155 VAL   A CB  
3254 C CB  B VAL   A 155 ? 0.1571 0.1871 0.2225 -0.0056 0.0076  0.0227  155 VAL   A CB  
3255 C CB  T VAL   A 155 ? 0.1680 0.1696 0.1987 -0.0133 0.0176  0.0300  155 VAL   A CB  
3256 C CG1 A VAL   A 155 ? 0.1539 0.1509 0.2152 0.0190  0.0068  0.0411  155 VAL   A CG1 
3257 C CG1 B VAL   A 155 ? 0.1606 0.1911 0.2236 -0.0052 -0.0010 0.0223  155 VAL   A CG1 
3258 C CG1 T VAL   A 155 ? 0.1716 0.1731 0.1994 -0.0094 0.0136  0.0303  155 VAL   A CG1 
3259 C CG2 A VAL   A 155 ? 0.1550 0.1511 0.2303 0.0096  -0.0008 0.0317  155 VAL   A CG2 
3260 C CG2 B VAL   A 155 ? 0.1656 0.1946 0.2332 0.0004  -0.0042 0.0166  155 VAL   A CG2 
3261 C CG2 T VAL   A 155 ? 0.1706 0.1721 0.2043 -0.0147 0.0098  0.0262  155 VAL   A CG2 
3287 N N   A PHE   A 156 ? 0.1777 0.1580 0.2490 0.0343  0.0377  0.0651  156 PHE   A N   
3288 N N   B PHE   A 156 ? 0.1691 0.1932 0.2667 0.0050  0.0243  0.0372  156 PHE   A N   
3289 N N   T PHE   A 156 ? 0.1773 0.1618 0.1888 -0.0049 0.0306  0.0440  156 PHE   A N   
3290 C CA  A PHE   A 156 ? 0.2051 0.1682 0.2604 0.0411  0.0374  0.0690  156 PHE   A CA  
3291 C CA  B PHE   A 156 ? 0.1853 0.2061 0.2816 0.0076  0.0205  0.0331  156 PHE   A CA  
3292 C CA  T PHE   A 156 ? 0.1850 0.1564 0.1818 0.0021  0.0327  0.0483  156 PHE   A CA  
3293 C C   A PHE   A 156 ? 0.2070 0.1740 0.2530 0.0529  0.0496  0.0768  156 PHE   A C   
3294 C C   B PHE   A 156 ? 0.1889 0.2220 0.2889 0.0123  0.0180  0.0340  156 PHE   A C   
3295 C C   T PHE   A 156 ? 0.1844 0.1712 0.1940 0.0056  0.0403  0.0406  156 PHE   A C   
3296 O O   A PHE   A 156 ? 0.2165 0.1841 0.2485 0.0431  0.0638  0.0644  156 PHE   A O   
3297 O O   B PHE   A 156 ? 0.1961 0.2256 0.3043 0.0112  0.0086  0.0285  156 PHE   A O   
3298 O O   T PHE   A 156 ? 0.1872 0.1760 0.1966 0.0037  0.0450  0.0249  156 PHE   A O   
3299 C CB  A PHE   A 156 ? 0.2252 0.1774 0.2679 0.0343  0.0245  0.0684  156 PHE   A CB  
3300 C CB  B PHE   A 156 ? 0.1973 0.2139 0.2908 -0.0030 0.0215  0.0217  156 PHE   A CB  
3301 C CB  T PHE   A 156 ? 0.1845 0.1372 0.1599 0.0039  0.0323  0.0562  156 PHE   A CB  
3302 C CG  A PHE   A 156 ? 0.2499 0.1915 0.2743 0.0395  0.0127  0.0549  156 PHE   A CG  
3303 C CG  B PHE   A 156 ? 0.2148 0.2268 0.3051 -0.0081 0.0156  0.0019  156 PHE   A CG  
3304 C CG  T PHE   A 156 ? 0.1879 0.1297 0.1537 0.0134  0.0310  0.0594  156 PHE   A CG  
3305 C CD1 A PHE   A 156 ? 0.2598 0.1991 0.2742 0.0423  0.0175  0.0446  156 PHE   A CD1 
3306 C CD1 B PHE   A 156 ? 0.2228 0.2320 0.3149 -0.0086 0.0145  -0.0065 156 PHE   A CD1 
3307 C CD1 T PHE   A 156 ? 0.1874 0.1295 0.1551 0.0175  0.0346  0.0542  156 PHE   A CD1 
3308 C CD2 A PHE   A 156 ? 0.2620 0.2027 0.2775 0.0421  0.0058  0.0493  156 PHE   A CD2 
3309 C CD2 B PHE   A 156 ? 0.2147 0.2316 0.3071 -0.0144 0.0169  -0.0086 156 PHE   A CD2 
3310 C CD2 T PHE   A 156 ? 0.1951 0.1317 0.1618 0.0169  0.0266  0.0566  156 PHE   A CD2 
3311 C CE1 A PHE   A 156 ? 0.2666 0.2049 0.2807 0.0417  0.0254  0.0389  156 PHE   A CE1 
3312 C CE1 B PHE   A 156 ? 0.2279 0.2376 0.3186 -0.0109 0.0134  -0.0128 156 PHE   A CE1 
3313 C CE1 T PHE   A 156 ? 0.1919 0.1337 0.1713 0.0216  0.0283  0.0389  156 PHE   A CE1 
3314 C CE2 A PHE   A 156 ? 0.2696 0.2110 0.2798 0.0439  0.0094  0.0404  156 PHE   A CE2 
3315 C CE2 B PHE   A 156 ? 0.2192 0.2354 0.3129 -0.0172 0.0145  -0.0160 156 PHE   A CE2 
3316 C CE2 T PHE   A 156 ? 0.1982 0.1345 0.1708 0.0186  0.0228  0.0475  156 PHE   A CE2 
3317 C CZ  A PHE   A 156 ? 0.2690 0.2118 0.2795 0.0471  0.0261  0.0365  156 PHE   A CZ  
3318 C CZ  B PHE   A 156 ? 0.2249 0.2401 0.3127 -0.0108 0.0122  -0.0212 156 PHE   A CZ  
3319 C CZ  T PHE   A 156 ? 0.1970 0.1335 0.1788 0.0151  0.0242  0.0426  156 PHE   A CZ  
3347 N N   A ASP   A 157 ? 0.2065 0.1855 0.2661 0.0613  0.0445  0.0810  157 ASP   A N   
3348 N N   B ASP   A 157 ? 0.1764 0.2272 0.2803 0.0154  0.0167  0.0499  157 ASP   A N   
3349 N N   T ASP   A 157 ? 0.1808 0.1837 0.2052 0.0091  0.0366  0.0480  157 ASP   A N   
3350 C CA  A ASP   A 157 ? 0.2140 0.2081 0.2815 0.0650  0.0375  0.0836  157 ASP   A CA  
3351 C CA  B ASP   A 157 ? 0.1678 0.2387 0.2703 0.0145  0.0135  0.0644  157 ASP   A CA  
3352 C CA  T ASP   A 157 ? 0.1804 0.1978 0.2207 0.0184  0.0323  0.0496  157 ASP   A CA  
3353 C C   A ASP   A 157 ? 0.1967 0.2256 0.2807 0.0666  0.0326  0.0887  157 ASP   A C   
3354 C C   B ASP   A 157 ? 0.1577 0.2561 0.2608 0.0332  0.0196  0.0761  157 ASP   A C   
3355 C C   T ASP   A 157 ? 0.1876 0.2139 0.2313 0.0230  0.0243  0.0507  157 ASP   A C   
3356 O O   A ASP   A 157 ? 0.1911 0.2229 0.2656 0.0656  0.0249  0.0938  157 ASP   A O   
3357 O O   B ASP   A 157 ? 0.1502 0.2585 0.2551 0.0312  0.0253  0.0724  157 ASP   A O   
3358 O O   T ASP   A 157 ? 0.1838 0.2120 0.2235 0.0247  0.0215  0.0504  157 ASP   A O   
3359 C CB  A ASP   A 157 ? 0.2335 0.2145 0.3043 0.0735  0.0357  0.0716  157 ASP   A CB  
3360 C CB  B ASP   A 157 ? 0.1640 0.2329 0.2764 0.0054  0.0094  0.0684  157 ASP   A CB  
3361 C CB  T ASP   A 157 ? 0.1704 0.1946 0.2262 0.0288  0.0402  0.0491  157 ASP   A CB  
3362 C CG  A ASP   A 157 ? 0.2525 0.2207 0.3333 0.0774  0.0294  0.0621  157 ASP   A CG  
3363 C CG  B ASP   A 157 ? 0.1560 0.2271 0.2876 -0.0030 0.0048  0.0752  157 ASP   A CG  
3364 C CG  T ASP   A 157 ? 0.1606 0.1877 0.2308 0.0369  0.0424  0.0506  157 ASP   A CG  
3365 O OD1 A ASP   A 157 ? 0.2650 0.2260 0.3488 0.0735  0.0212  0.0499  157 ASP   A OD1 
3366 O OD1 B ASP   A 157 ? 0.1557 0.2212 0.3132 -0.0130 0.0024  0.0628  157 ASP   A OD1 
3367 O OD1 T ASP   A 157 ? 0.1612 0.1883 0.2495 0.0348  0.0406  0.0340  157 ASP   A OD1 
3368 O OD2 A ASP   A 157 ? 0.2562 0.2170 0.3464 0.0791  0.0314  0.0709  157 ASP   A OD2 
3369 O OD2 B ASP   A 157 ? 0.1577 0.2311 0.2884 0.0004  -0.0109 0.0786  157 ASP   A OD2 
3370 O OD2 T ASP   A 157 ? 0.1496 0.1807 0.2262 0.0462  0.0403  0.0663  157 ASP   A OD2 
3383 N N   A LYS   A 158 ? 0.1960 0.2455 0.2867 0.0641  0.0378  0.0893  158 LYS   A N   
3384 N N   B LYS   A 158 ? 0.1687 0.2713 0.2573 0.0452  0.0266  0.0869  158 LYS   A N   
3385 N N   T LYS   A 158 ? 0.2029 0.2306 0.2441 0.0241  0.0242  0.0506  158 LYS   A N   
3386 C CA  A LYS   A 158 ? 0.1910 0.2671 0.2951 0.0584  0.0431  0.0824  158 LYS   A CA  
3387 C CA  B LYS   A 158 ? 0.1790 0.2848 0.2563 0.0491  0.0311  0.0892  158 LYS   A CA  
3388 C CA  T LYS   A 158 ? 0.2141 0.2465 0.2553 0.0239  0.0233  0.0478  158 LYS   A CA  
3389 C C   A LYS   A 158 ? 0.1693 0.2707 0.2904 0.0548  0.0368  0.0843  158 LYS   A C   
3390 C C   B LYS   A 158 ? 0.1779 0.2906 0.2496 0.0540  0.0308  0.0936  158 LYS   A C   
3391 C C   T LYS   A 158 ? 0.2121 0.2499 0.2547 0.0209  0.0204  0.0462  158 LYS   A C   
3392 O O   A LYS   A 158 ? 0.1605 0.2770 0.2851 0.0467  0.0437  0.0864  158 LYS   A O   
3393 O O   B LYS   A 158 ? 0.1680 0.2937 0.2446 0.0482  0.0401  0.0857  158 LYS   A O   
3394 O O   T LYS   A 158 ? 0.2099 0.2506 0.2523 0.0192  0.0213  0.0453  158 LYS   A O   
3395 C CB  A LYS   A 158 ? 0.2057 0.2776 0.3085 0.0547  0.0633  0.0759  158 LYS   A CB  
3396 C CB  B LYS   A 158 ? 0.1877 0.2906 0.2715 0.0404  0.0357  0.0778  158 LYS   A CB  
3397 C CB  T LYS   A 158 ? 0.2268 0.2553 0.2714 0.0248  0.0303  0.0443  158 LYS   A CB  
3398 C CG  A LYS   A 158 ? 0.2268 0.2899 0.3244 0.0502  0.0751  0.0703  158 LYS   A CG  
3399 C CG  B LYS   A 158 ? 0.1974 0.2991 0.2890 0.0310  0.0352  0.0653  158 LYS   A CG  
3400 C CG  T LYS   A 158 ? 0.2409 0.2641 0.2891 0.0255  0.0347  0.0410  158 LYS   A CG  
3401 C CD  A LYS   A 158 ? 0.2400 0.3005 0.3349 0.0487  0.0878  0.0649  158 LYS   A CD  
3402 C CD  B LYS   A 158 ? 0.2063 0.3085 0.3088 0.0239  0.0370  0.0498  158 LYS   A CD  
3403 C CD  T LYS   A 158 ? 0.2523 0.2716 0.3058 0.0285  0.0365  0.0371  158 LYS   A CD  
3404 C CE  A LYS   A 158 ? 0.2480 0.3045 0.3371 0.0436  0.0970  0.0706  158 LYS   A CE  
3405 C CE  B LYS   A 158 ? 0.2109 0.3120 0.3231 0.0222  0.0373  0.0403  158 LYS   A CE  
3406 C CE  T LYS   A 158 ? 0.2606 0.2757 0.3180 0.0298  0.0357  0.0344  158 LYS   A CE  
3407 N NZ  A LYS   A 158 ? 0.2500 0.3052 0.3409 0.0356  0.1035  0.0761  158 LYS   A NZ  
3408 N NZ  B LYS   A 158 ? 0.2155 0.3136 0.3253 0.0232  0.0375  0.0330  158 LYS   A NZ  
3409 N NZ  T LYS   A 158 ? 0.2650 0.2773 0.3259 0.0309  0.0353  0.0312  158 LYS   A NZ  
3449 N N   A ASN   A 159 ? 0.1601 0.2657 0.2926 0.0518  0.0210  0.0841  159 ASN   A N   
3450 N N   B ASN   A 159 ? 0.1873 0.2951 0.2666 0.0601  0.0241  0.0894  159 ASN   A N   
3451 N N   T ASN   A 159 ? 0.2138 0.2519 0.2587 0.0166  0.0158  0.0449  159 ASN   A N   
3452 C CA  A ASN   A 159 ? 0.1555 0.2584 0.2865 0.0373  0.0090  0.0906  159 ASN   A CA  
3453 C CA  B ASN   A 159 ? 0.2069 0.2990 0.2913 0.0481  0.0266  0.0767  159 ASN   A CA  
3454 C CA  T ASN   A 159 ? 0.2160 0.2517 0.2588 0.0090  0.0128  0.0470  159 ASN   A CA  
3455 C C   A ASN   A 159 ? 0.1429 0.2512 0.2700 0.0242  0.0111  0.0738  159 ASN   A C   
3456 C C   B ASN   A 159 ? 0.1984 0.2951 0.2673 0.0365  0.0275  0.0613  159 ASN   A C   
3457 C C   T ASN   A 159 ? 0.2172 0.2516 0.2503 0.0028  0.0176  0.0394  159 ASN   A C   
3458 O O   A ASN   A 159 ? 0.1330 0.2463 0.2640 0.0235  -0.0087 0.0521  159 ASN   A O   
3459 O O   B ASN   A 159 ? 0.1929 0.3005 0.2623 0.0340  0.0175  0.0477  159 ASN   A O   
3460 O O   T ASN   A 159 ? 0.2175 0.2505 0.2500 0.0005  0.0137  0.0292  159 ASN   A O   
3461 C CB  A ASN   A 159 ? 0.1657 0.2628 0.3045 0.0349  0.0076  0.1105  159 ASN   A CB  
3462 C CB  B ASN   A 159 ? 0.2306 0.3053 0.3398 0.0465  0.0326  0.0804  159 ASN   A CB  
3463 C CB  T ASN   A 159 ? 0.2176 0.2532 0.2699 0.0080  0.0094  0.0563  159 ASN   A CB  
3464 C CG  A ASN   A 159 ? 0.1745 0.2732 0.3346 0.0324  0.0137  0.1172  159 ASN   A CG  
3465 C CG  B ASN   A 159 ? 0.2496 0.3101 0.3844 0.0409  0.0438  0.0809  159 ASN   A CG  
3466 C CG  T ASN   A 159 ? 0.2190 0.2563 0.2865 0.0071  0.0103  0.0622  159 ASN   A CG  
3467 O OD1 A ASN   A 159 ? 0.1878 0.2803 0.3538 0.0271  0.0182  0.1276  159 ASN   A OD1 
3468 O OD1 B ASN   A 159 ? 0.2613 0.3146 0.4025 0.0376  0.0406  0.0819  159 ASN   A OD1 
3469 O OD1 T ASN   A 159 ? 0.2229 0.2590 0.2984 0.0064  0.0121  0.0675  159 ASN   A OD1 
3470 N ND2 A ASN   A 159 ? 0.1690 0.2754 0.3403 0.0350  0.0142  0.1149  159 ASN   A ND2 
3471 N ND2 B ASN   A 159 ? 0.2518 0.3131 0.3960 0.0426  0.0543  0.0804  159 ASN   A ND2 
3472 N ND2 T ASN   A 159 ? 0.2154 0.2572 0.2878 0.0075  0.0112  0.0627  159 ASN   A ND2 
3491 N N   A LEU   A 160 ? 0.1382 0.2432 0.2618 0.0205  0.0151  0.0803  160 LEU   A N   
3492 N N   B LEU   A 160 ? 0.1907 0.2802 0.2488 0.0307  0.0239  0.0635  160 LEU   A N   
3493 N N   T LEU   A 160 ? 0.2159 0.2497 0.2456 0.0005  0.0208  0.0424  160 LEU   A N   
3494 C CA  A LEU   A 160 ? 0.1382 0.2407 0.2522 0.0131  0.0255  0.0820  160 LEU   A CA  
3495 C CA  B LEU   A 160 ? 0.1883 0.2664 0.2347 0.0200  0.0296  0.0616  160 LEU   A CA  
3496 C CA  T LEU   A 160 ? 0.2173 0.2482 0.2383 -0.0031 0.0250  0.0449  160 LEU   A CA  
3497 C C   A LEU   A 160 ? 0.1234 0.2355 0.2529 0.0050  0.0313  0.0740  160 LEU   A C   
3498 C C   B LEU   A 160 ? 0.1715 0.2504 0.2297 0.0102  0.0326  0.0546  160 LEU   A C   
3499 O O   A LEU   A 160 ? 0.1111 0.2363 0.2621 -0.0003 0.0269  0.0750  160 LEU   A O   
3500 O O   B LEU   A 160 ? 0.1622 0.2534 0.2297 0.0046  0.0310  0.0546  160 LEU   A O   
3501 C CB  A LEU   A 160 ? 0.1455 0.2449 0.2528 0.0093  0.0251  0.0815  160 LEU   A CB  
3502 C CB  B LEU   A 160 ? 0.1969 0.2690 0.2338 0.0141  0.0306  0.0606  160 LEU   A CB  
3503 C CB  T LEU   A 160 ? 0.2168 0.2482 0.2361 -0.0072 0.0267  0.0441  160 LEU   A CB  
3504 C CG  A LEU   A 160 ? 0.1482 0.2515 0.2634 0.0040  0.0197  0.0637  160 LEU   A CG  
3505 C CG  B LEU   A 160 ? 0.2029 0.2734 0.2474 0.0084  0.0263  0.0469  160 LEU   A CG  
3506 C CG  T LEU   A 160 ? 0.2163 0.2490 0.2382 -0.0115 0.0268  0.0380  160 LEU   A CG  
3507 C CD1 A LEU   A 160 ? 0.1552 0.2567 0.2707 0.0011  0.0279  0.0508  160 LEU   A CD1 
3508 C CD1 B LEU   A 160 ? 0.2041 0.2773 0.2553 0.0053  0.0289  0.0373  160 LEU   A CD1 
3509 C CD1 T LEU   A 160 ? 0.2176 0.2510 0.2424 -0.0129 0.0299  0.0323  160 LEU   A CD1 
3510 C CD2 A LEU   A 160 ? 0.1449 0.2515 0.2558 -0.0001 0.0200  0.0629  160 LEU   A CD2 
3511 C CD2 B LEU   A 160 ? 0.2051 0.2733 0.2435 0.0024  0.0342  0.0451  160 LEU   A CD2 
3512 C CD2 T LEU   A 160 ? 0.2151 0.2485 0.2337 -0.0138 0.0285  0.0376  160 LEU   A CD2 
3545 N N   A TYR   A 161 ? 0.1331 0.2270 0.2572 0.0012  0.0300  0.0793  161 TYR   A N   
3546 N N   B TYR   A 161 ? 0.1705 0.2291 0.2240 0.0045  0.0339  0.0546  161 TYR   A N   
3547 C CA  A TYR   A 161 ? 0.1352 0.2224 0.2605 0.0003  0.0270  0.0731  161 TYR   A CA  
3548 C CA  B TYR   A 161 ? 0.1711 0.2145 0.2218 -0.0035 0.0301  0.0489  161 TYR   A CA  
3549 C C   A TYR   A 161 ? 0.1366 0.2375 0.2671 0.0026  0.0208  0.0768  161 TYR   A C   
3550 C C   B TYR   A 161 ? 0.1732 0.2152 0.2244 -0.0120 0.0227  0.0437  161 TYR   A C   
3551 O O   A TYR   A 161 ? 0.1376 0.2427 0.2702 -0.0011 0.0242  0.0689  161 TYR   A O   
3552 O O   B TYR   A 161 ? 0.1705 0.2082 0.2242 -0.0110 0.0234  0.0316  161 TYR   A O   
3553 C CB  A TYR   A 161 ? 0.1435 0.2107 0.2655 0.0004  0.0355  0.0628  161 TYR   A CB  
3554 C CB  B TYR   A 161 ? 0.1750 0.2046 0.2214 0.0008  0.0332  0.0444  161 TYR   A CB  
3555 C CG  A TYR   A 161 ? 0.1430 0.1955 0.2594 0.0057  0.0273  0.0464  161 TYR   A CG  
3556 C CG  B TYR   A 161 ? 0.1725 0.1886 0.2160 0.0063  0.0314  0.0405  161 TYR   A CG  
3557 C CD1 A TYR   A 161 ? 0.1432 0.1875 0.2704 0.0057  0.0213  0.0346  161 TYR   A CD1 
3558 C CD1 B TYR   A 161 ? 0.1723 0.1819 0.2249 0.0088  0.0259  0.0335  161 TYR   A CD1 
3559 C CD2 A TYR   A 161 ? 0.1413 0.1864 0.2576 0.0132  0.0284  0.0440  161 TYR   A CD2 
3560 C CD2 B TYR   A 161 ? 0.1708 0.1802 0.2156 0.0097  0.0305  0.0448  161 TYR   A CD2 
3561 C CE1 A TYR   A 161 ? 0.1503 0.1732 0.2673 0.0092  0.0101  0.0319  161 TYR   A CE1 
3562 C CE1 B TYR   A 161 ? 0.1729 0.1803 0.2241 0.0129  0.0210  0.0320  161 TYR   A CE1 
3563 C CE2 A TYR   A 161 ? 0.1492 0.1693 0.2597 0.0059  0.0170  0.0475  161 TYR   A CE2 
3564 C CE2 B TYR   A 161 ? 0.1722 0.1787 0.2185 0.0071  0.0313  0.0486  161 TYR   A CE2 
3565 C CZ  A TYR   A 161 ? 0.1575 0.1664 0.2539 0.0048  0.0090  0.0389  161 TYR   A CZ  
3566 C CZ  B TYR   A 161 ? 0.1791 0.1767 0.2232 0.0083  0.0236  0.0437  161 TYR   A CZ  
3567 O OH  A TYR   A 161 ? 0.1706 0.1553 0.2641 0.0031  -0.0029 0.0434  161 TYR   A OH  
3568 O OH  B TYR   A 161 ? 0.1898 0.1740 0.2458 0.0029  0.0139  0.0414  161 TYR   A OH  
3587 N N   A ASP   A 162 ? 0.1360 0.2539 0.2745 0.0036  0.0321  0.0827  162 ASP   A N   
3588 N N   B ASP   A 162 ? 0.1752 0.2300 0.2316 -0.0192 0.0313  0.0479  162 ASP   A N   
3589 C CA  A ASP   A 162 ? 0.1381 0.2793 0.2721 0.0003  0.0358  0.0705  162 ASP   A CA  
3590 C CA  B ASP   A 162 ? 0.1801 0.2454 0.2369 -0.0123 0.0303  0.0453  162 ASP   A CA  
3591 C C   A ASP   A 162 ? 0.1314 0.2972 0.2529 0.0004  0.0214  0.0542  162 ASP   A C   
3592 C C   B ASP   A 162 ? 0.1906 0.2640 0.2362 -0.0206 0.0253  0.0418  162 ASP   A C   
3593 O O   A ASP   A 162 ? 0.1376 0.3038 0.2580 0.0044  0.0230  0.0305  162 ASP   A O   
3594 O O   B ASP   A 162 ? 0.1978 0.2632 0.2397 -0.0190 0.0283  0.0251  162 ASP   A O   
3595 C CB  A ASP   A 162 ? 0.1508 0.2863 0.3013 -0.0001 0.0471  0.0741  162 ASP   A CB  
3596 C CB  B ASP   A 162 ? 0.1726 0.2402 0.2486 0.0002  0.0357  0.0560  162 ASP   A CB  
3597 C CG  A ASP   A 162 ? 0.1656 0.2970 0.3343 0.0054  0.0485  0.0656  162 ASP   A CG  
3598 C CG  B ASP   A 162 ? 0.1674 0.2322 0.2554 0.0100  0.0369  0.0689  162 ASP   A CG  
3599 O OD1 A ASP   A 162 ? 0.1732 0.3026 0.3426 0.0064  0.0406  0.0640  162 ASP   A OD1 
3600 O OD1 B ASP   A 162 ? 0.1656 0.2286 0.2616 0.0147  0.0342  0.0695  162 ASP   A OD1 
3601 O OD2 A ASP   A 162 ? 0.1769 0.3005 0.3481 0.0131  0.0633  0.0567  162 ASP   A OD2 
3602 O OD2 B ASP   A 162 ? 0.1741 0.2323 0.2725 0.0195  0.0338  0.0795  162 ASP   A OD2 
3611 N N   A LYS   A 163 ? 0.1362 0.3107 0.2514 0.0031  -0.0008 0.0473  163 LYS   A N   
3612 N N   B LYS   A 163 ? 0.2007 0.2880 0.2454 -0.0231 0.0138  0.0505  163 LYS   A N   
3613 C CA  A LYS   A 163 ? 0.1477 0.3192 0.2482 0.0033  -0.0038 0.0388  163 LYS   A CA  
3614 C CA  B LYS   A 163 ? 0.2109 0.3071 0.2568 -0.0277 0.0074  0.0589  163 LYS   A CA  
3615 C C   A LYS   A 163 ? 0.1469 0.3042 0.2178 -0.0050 0.0090  0.0426  163 LYS   A C   
3616 C C   B LYS   A 163 ? 0.2052 0.3062 0.2400 -0.0313 0.0090  0.0677  163 LYS   A C   
3617 O O   A LYS   A 163 ? 0.1472 0.3019 0.2067 -0.0174 0.0141  0.0326  163 LYS   A O   
3618 O O   B LYS   A 163 ? 0.2041 0.3077 0.2268 -0.0274 0.0067  0.0756  163 LYS   A O   
3619 C CB  A LYS   A 163 ? 0.1813 0.3402 0.2909 0.0154  -0.0051 0.0303  163 LYS   A CB  
3620 C CB  B LYS   A 163 ? 0.2339 0.3255 0.2986 -0.0255 0.0067  0.0556  163 LYS   A CB  
3621 C CG  A LYS   A 163 ? 0.2100 0.3583 0.3394 0.0204  0.0026  0.0238  163 LYS   A CG  
3622 C CG  B LYS   A 163 ? 0.2563 0.3415 0.3462 -0.0286 0.0106  0.0507  163 LYS   A CG  
3623 C CD  A LYS   A 163 ? 0.2359 0.3743 0.3866 0.0213  0.0015  0.0211  163 LYS   A CD  
3624 C CD  B LYS   A 163 ? 0.2750 0.3545 0.3892 -0.0324 0.0154  0.0442  163 LYS   A CD  
3625 C CE  A LYS   A 163 ? 0.2551 0.3854 0.4238 0.0170  0.0019  0.0199  163 LYS   A CE  
3626 C CE  B LYS   A 163 ? 0.2849 0.3653 0.4266 -0.0349 0.0175  0.0373  163 LYS   A CE  
3627 N NZ  A LYS   A 163 ? 0.2656 0.3926 0.4473 0.0108  0.0020  0.0165  163 LYS   A NZ  
3628 N NZ  B LYS   A 163 ? 0.2936 0.3709 0.4461 -0.0355 0.0194  0.0345  163 LYS   A NZ  
3655 N N   A LEU   A 164 ? 0.1302 0.2796 0.1888 -0.0050 0.0136  0.0502  164 LEU   A N   
3656 N N   B LEU   A 164 ? 0.1954 0.2974 0.2411 -0.0394 0.0128  0.0690  164 LEU   A N   
3657 C CA  A LEU   A 164 ? 0.1393 0.2641 0.1831 -0.0088 0.0194  0.0456  164 LEU   A CA  
3658 C CA  B LEU   A 164 ? 0.1994 0.2895 0.2400 -0.0444 0.0179  0.0758  164 LEU   A CA  
3659 C C   A LEU   A 164 ? 0.1508 0.2567 0.1695 -0.0123 0.0161  0.0413  164 LEU   A C   
3660 C C   B LEU   A 164 ? 0.2123 0.2872 0.2435 -0.0454 0.0093  0.0818  164 LEU   A C   
3661 O O   A LEU   A 164 ? 0.1539 0.2521 0.1662 -0.0129 0.0260  0.0327  164 LEU   A O   
3662 O O   B LEU   A 164 ? 0.2171 0.2863 0.2325 -0.0459 0.0070  0.0819  164 LEU   A O   
3663 C CB  A LEU   A 164 ? 0.1392 0.2549 0.1991 -0.0071 0.0232  0.0434  164 LEU   A CB  
3664 C CB  B LEU   A 164 ? 0.1951 0.2835 0.2334 -0.0442 0.0253  0.0775  164 LEU   A CB  
3665 C CG  A LEU   A 164 ? 0.1387 0.2432 0.2080 -0.0088 0.0181  0.0482  164 LEU   A CG  
3666 C CG  B LEU   A 164 ? 0.1965 0.2819 0.2426 -0.0375 0.0229  0.0689  164 LEU   A CG  
3667 C CD1 A LEU   A 164 ? 0.1256 0.2376 0.2146 -0.0004 0.0016  0.0583  164 LEU   A CD1 
3668 C CD1 B LEU   A 164 ? 0.1929 0.2833 0.2549 -0.0281 0.0160  0.0625  164 LEU   A CD1 
3669 C CD2 A LEU   A 164 ? 0.1383 0.2431 0.2055 -0.0192 0.0358  0.0442  164 LEU   A CD2 
3670 C CD2 B LEU   A 164 ? 0.1999 0.2824 0.2372 -0.0395 0.0277  0.0686  164 LEU   A CD2 
3693 N N   A VAL   A 165 ? 0.1381 0.2557 0.1633 -0.0243 0.0187  0.0381  165 VAL   A N   
3694 N N   B VAL   A 165 ? 0.2153 0.2866 0.2552 -0.0472 0.0011  0.0895  165 VAL   A N   
3695 C CA  A VAL   A 165 ? 0.1486 0.2558 0.1651 -0.0258 0.0190  0.0363  165 VAL   A CA  
3696 C CA  B VAL   A 165 ? 0.2293 0.2917 0.2843 -0.0426 -0.0136 0.0822  165 VAL   A CA  
3697 C C   A VAL   A 165 ? 0.1468 0.2683 0.1809 -0.0269 0.0260  0.0277  165 VAL   A C   
3698 C C   B VAL   A 165 ? 0.2378 0.3004 0.2994 -0.0379 -0.0207 0.0721  165 VAL   A C   
3699 O O   A VAL   A 165 ? 0.1390 0.2659 0.1810 -0.0302 0.0430  0.0224  165 VAL   A O   
3700 O O   B VAL   A 165 ? 0.2468 0.3064 0.3181 -0.0386 -0.0341 0.0711  165 VAL   A O   
3701 C CB  A VAL   A 165 ? 0.1661 0.2488 0.1683 -0.0312 0.0152  0.0371  165 VAL   A CB  
3702 C CB  B VAL   A 165 ? 0.2368 0.2948 0.2982 -0.0378 -0.0233 0.0784  165 VAL   A CB  
3703 C CG1 A VAL   A 165 ? 0.1671 0.2527 0.1675 -0.0303 0.0131  0.0281  165 VAL   A CG1 
3704 C CG1 B VAL   A 165 ? 0.2402 0.2942 0.3049 -0.0366 -0.0290 0.0734  165 VAL   A CG1 
3705 C CG2 A VAL   A 165 ? 0.1803 0.2460 0.1816 -0.0279 -0.0007 0.0406  165 VAL   A CG2 
3706 C CG2 B VAL   A 165 ? 0.2396 0.2979 0.3058 -0.0388 -0.0220 0.0790  165 VAL   A CG2 
3725 N N   A SER   A 166 ? 0.1306 0.2803 0.1861 -0.0270 0.0357  0.0239  166 SER   A N   
3726 N N   B SER   A 166 ? 0.2374 0.3044 0.2955 -0.0310 -0.0142 0.0680  166 SER   A N   
3727 C CA  A SER   A 166 ? 0.1358 0.2945 0.2140 -0.0301 0.0260  0.0168  166 SER   A CA  
3728 C CA  B SER   A 166 ? 0.2430 0.3125 0.2995 -0.0256 -0.0028 0.0559  166 SER   A CA  
3729 C C   A SER   A 166 ? 0.1374 0.2997 0.2248 -0.0283 0.0087  -0.0010 166 SER   A C   
3730 C C   B SER   A 166 ? 0.2634 0.3228 0.3083 -0.0225 0.0093  0.0455  166 SER   A C   
3731 O O   A SER   A 166 ? 0.1624 0.3101 0.2691 -0.0322 0.0198  -0.0200 166 SER   A O   
3732 O O   B SER   A 166 ? 0.2633 0.3206 0.3094 -0.0188 0.0117  0.0443  166 SER   A O   
3733 C CB  A SER   A 166 ? 0.1475 0.3017 0.2433 -0.0283 0.0187  0.0175  166 SER   A CB  
3734 C CB  B SER   A 166 ? 0.2312 0.3105 0.2979 -0.0239 -0.0044 0.0558  166 SER   A CB  
3735 O OG  A SER   A 166 ? 0.1722 0.3093 0.2732 -0.0244 0.0110  0.0255  166 SER   A OG  
3736 O OG  B SER   A 166 ? 0.2206 0.3078 0.3065 -0.0261 -0.0066 0.0588  166 SER   A OG  
3747 N N   A SER   A 167 ? 0.1369 0.2954 0.1908 -0.0146 0.0021  0.0092  167 SER   A N   
3748 N N   B SER   A 167 ? 0.2887 0.3377 0.3244 -0.0228 0.0261  0.0418  167 SER   A N   
3749 C CA  A SER   A 167 ? 0.1550 0.2916 0.1871 -0.0006 -0.0114 0.0078  167 SER   A CA  
3750 C CA  B SER   A 167 ? 0.3147 0.3520 0.3376 -0.0207 0.0399  0.0432  167 SER   A CA  
3751 C C   A SER   A 167 ? 0.1662 0.2911 0.1905 0.0092  0.0069  0.0157  167 SER   A C   
3752 C C   B SER   A 167 ? 0.3296 0.3611 0.3470 -0.0125 0.0443  0.0446  167 SER   A C   
3753 O O   A SER   A 167 ? 0.1855 0.2965 0.1998 0.0179  0.0024  0.0229  167 SER   A O   
3754 O O   B SER   A 167 ? 0.3292 0.3605 0.3527 -0.0154 0.0371  0.0451  167 SER   A O   
3755 C CB  A SER   A 167 ? 0.1713 0.2949 0.2014 0.0117  -0.0015 0.0167  167 SER   A CB  
3756 C CB  B SER   A 167 ? 0.3252 0.3603 0.3529 -0.0198 0.0446  0.0398  167 SER   A CB  
3757 O OG  A SER   A 167 ? 0.1773 0.2976 0.2097 0.0191  0.0164  0.0089  167 SER   A OG  
3758 O OG  B SER   A 167 ? 0.3329 0.3680 0.3672 -0.0209 0.0459  0.0378  167 SER   A OG  
3769 N N   A PHE   A 168 ? 0.1626 0.2862 0.1968 0.0188  0.0158  0.0164  168 PHE   A N   
3770 N N   B PHE   A 168 ? 0.3504 0.3707 0.3576 -0.0002 0.0506  0.0490  168 PHE   A N   
3771 C CA  A PHE   A 168 ? 0.1546 0.2849 0.2085 0.0153  0.0199  0.0190  168 PHE   A CA  
3772 C CA  B PHE   A 168 ? 0.3694 0.3801 0.3799 0.0091  0.0489  0.0483  168 PHE   A CA  
3773 C C   A PHE   A 168 ? 0.1666 0.2943 0.2404 0.0083  0.0412  0.0107  168 PHE   A C   
3774 C C   B PHE   A 168 ? 0.3819 0.3804 0.3939 0.0093  0.0422  0.0452  168 PHE   A C   
3775 O O   A PHE   A 168 ? 0.1799 0.2990 0.2846 -0.0032 0.0437  0.0186  168 PHE   A O   
3776 O O   B PHE   A 168 ? 0.3831 0.3816 0.4014 0.0090  0.0408  0.0445  168 PHE   A O   
3777 C CB  A PHE   A 168 ? 0.1537 0.2808 0.1911 0.0102  0.0122  0.0192  168 PHE   A CB  
3778 C CB  B PHE   A 168 ? 0.3768 0.3882 0.3845 0.0171  0.0520  0.0499  168 PHE   A CB  
3779 C CG  A PHE   A 168 ? 0.1469 0.2798 0.1818 0.0001  0.0049  0.0203  168 PHE   A CG  
3780 C CG  B PHE   A 168 ? 0.3827 0.3943 0.3878 0.0242  0.0568  0.0536  168 PHE   A CG  
3781 C CD1 A PHE   A 168 ? 0.1525 0.2846 0.1816 -0.0016 0.0026  0.0211  168 PHE   A CD1 
3782 C CD1 B PHE   A 168 ? 0.3841 0.3955 0.3887 0.0269  0.0602  0.0556  168 PHE   A CD1 
3783 C CD2 A PHE   A 168 ? 0.1397 0.2752 0.1684 -0.0063 0.0148  0.0253  168 PHE   A CD2 
3784 C CD2 B PHE   A 168 ? 0.3851 0.3971 0.3888 0.0263  0.0595  0.0546  168 PHE   A CD2 
3785 C CE1 A PHE   A 168 ? 0.1435 0.2816 0.1758 -0.0087 0.0062  0.0271  168 PHE   A CE1 
3786 C CE1 B PHE   A 168 ? 0.3848 0.3958 0.3888 0.0281  0.0596  0.0564  168 PHE   A CE1 
3787 C CE2 A PHE   A 168 ? 0.1502 0.2708 0.1790 -0.0066 0.0137  0.0330  168 PHE   A CE2 
3788 C CE2 B PHE   A 168 ? 0.3863 0.3973 0.3906 0.0263  0.0585  0.0572  168 PHE   A CE2 
3789 C CZ  A PHE   A 168 ? 0.1474 0.2746 0.1766 -0.0080 0.0114  0.0268  168 PHE   A CZ  
3790 C CZ  B PHE   A 168 ? 0.3855 0.3968 0.3905 0.0270  0.0588  0.0574  168 PHE   A CZ  
3809 N N   A LEU   A 169 ? 0.1908 0.2989 0.2696 -0.0067 0.0327  -0.0098 169 LEU   A N   
3810 N N   B LEU   A 169 ? 0.3925 0.3797 0.3983 0.0093  0.0347  0.0398  169 LEU   A N   
3811 C CA  A LEU   A 169 ? 0.2321 0.3125 0.3205 -0.0011 0.0154  -0.0161 169 LEU   A CA  
3812 C CA  B LEU   A 169 ? 0.4010 0.3792 0.4032 0.0081  0.0278  0.0359  169 LEU   A CA  
3813 C C   A LEU   A 169 ? 0.2342 0.3126 0.3352 -0.0030 0.0095  -0.0049 169 LEU   A C   
3814 C C   B LEU   A 169 ? 0.4065 0.3840 0.4267 0.0090  0.0179  0.0284  169 LEU   A C   
3815 O O   A LEU   A 169 ? 0.2438 0.3150 0.3400 0.0004  0.0099  -0.0089 169 LEU   A O   
3816 O O   B LEU   A 169 ? 0.4071 0.3859 0.4342 0.0090  0.0172  0.0281  169 LEU   A O   
3817 C CB  A LEU   A 169 ? 0.2627 0.3259 0.3577 0.0019  0.0022  -0.0334 169 LEU   A CB  
3818 C CB  B LEU   A 169 ? 0.4032 0.3763 0.3808 0.0060  0.0287  0.0387  169 LEU   A CB  
3819 C CG  A LEU   A 169 ? 0.2876 0.3367 0.3846 -0.0006 -0.0111 -0.0489 169 LEU   A CG  
3820 C CG  B LEU   A 169 ? 0.4022 0.3730 0.3615 0.0029  0.0290  0.0431  169 LEU   A CG  
3821 C CD1 A LEU   A 169 ? 0.2972 0.3383 0.3979 -0.0002 -0.0172 -0.0537 169 LEU   A CD1 
3822 C CD1 B LEU   A 169 ? 0.4033 0.3735 0.3548 0.0032  0.0298  0.0411  169 LEU   A CD1 
3823 C CD2 A LEU   A 169 ? 0.2952 0.3415 0.3917 -0.0031 -0.0125 -0.0536 169 LEU   A CD2 
3824 C CD2 B LEU   A 169 ? 0.4005 0.3704 0.3536 0.0011  0.0277  0.0447  169 LEU   A CD2 
3825 O OXT A LEU   A 169 ? 0.2307 0.3157 0.3467 -0.0082 0.0074  0.0029  169 LEU   A OXT 
3826 O OXT B LEU   A 169 ? 0.4107 0.3868 0.4333 0.0076  0.0104  0.0247  169 LEU   A OXT 
3849 N N   A SER   B 1   ? 0.3703 0.3613 0.3640 -0.1069 -0.0730 0.0505  1   SER   B N   
3850 N N   B SER   B 1   ? 0.3397 0.3434 0.3388 -0.0961 -0.0676 0.0350  1   SER   B N   
3851 C CA  A SER   B 1   ? 0.3630 0.3625 0.3623 -0.1095 -0.0724 0.0504  1   SER   B CA  
3852 C CA  B SER   B 1   ? 0.3338 0.3439 0.3338 -0.0975 -0.0680 0.0351  1   SER   B CA  
3853 C C   A SER   B 1   ? 0.3389 0.3591 0.3485 -0.1089 -0.0716 0.0610  1   SER   B C   
3854 C C   B SER   B 1   ? 0.3157 0.3432 0.3156 -0.0935 -0.0721 0.0458  1   SER   B C   
3855 O O   A SER   B 1   ? 0.3461 0.3602 0.3365 -0.1027 -0.0596 0.0640  1   SER   B O   
3856 O O   B SER   B 1   ? 0.3154 0.3414 0.2993 -0.0921 -0.0725 0.0478  1   SER   B O   
3857 C CB  A SER   B 1   ? 0.3743 0.3609 0.3861 -0.1102 -0.0653 0.0396  1   SER   B CB  
3858 C CB  B SER   B 1   ? 0.3418 0.3414 0.3568 -0.1002 -0.0583 0.0234  1   SER   B CB  
3859 O OG  A SER   B 1   ? 0.3889 0.3697 0.4171 -0.1049 -0.0531 0.0329  1   SER   B OG  
3860 O OG  B SER   B 1   ? 0.3516 0.3466 0.3815 -0.0988 -0.0493 0.0162  1   SER   B OG  
3875 N N   A MET   B 2   ? 0.3142 0.3492 0.3556 -0.1106 -0.0717 0.0846  2   MET   B N   
3876 N N   B MET   B 2   ? 0.3037 0.3414 0.3209 -0.0870 -0.0684 0.0659  2   MET   B N   
3877 C CA  A MET   B 2   ? 0.2969 0.3432 0.3703 -0.0910 -0.0740 0.1010  2   MET   B CA  
3878 C CA  B MET   B 2   ? 0.2971 0.3421 0.3308 -0.0675 -0.0647 0.0785  2   MET   B CA  
3879 C C   A MET   B 2   ? 0.2586 0.3179 0.3304 -0.0780 -0.0860 0.1244  2   MET   B C   
3880 C C   B MET   B 2   ? 0.2759 0.3244 0.3073 -0.0541 -0.0639 0.0878  2   MET   B C   
3881 O O   A MET   B 2   ? 0.2496 0.3248 0.3237 -0.0691 -0.0927 0.1371  2   MET   B O   
3882 O O   B MET   B 2   ? 0.2766 0.3310 0.3143 -0.0466 -0.0627 0.0891  2   MET   B O   
3883 C CB  A MET   B 2   ? 0.3264 0.3722 0.4449 -0.0690 -0.0576 0.0792  2   MET   B CB  
3884 C CB  B MET   B 2   ? 0.3175 0.3651 0.3780 -0.0530 -0.0593 0.0737  2   MET   B CB  
3885 C CG  A MET   B 2   ? 0.3505 0.3953 0.5195 -0.0491 -0.0411 0.0666  2   MET   B CG  
3886 C CG  B MET   B 2   ? 0.3333 0.3827 0.4245 -0.0397 -0.0535 0.0743  2   MET   B CG  
3887 S SD  A MET   B 2   ? 0.3743 0.4156 0.5890 -0.0324 -0.0276 0.0542  2   MET   B SD  
3888 S SD  B MET   B 2   ? 0.3494 0.3988 0.4653 -0.0279 -0.0491 0.0728  2   MET   B SD  
3889 C CE  A MET   B 2   ? 0.3745 0.4181 0.5897 -0.0317 -0.0199 0.0521  2   MET   B CE  
3890 C CE  B MET   B 2   ? 0.3482 0.3979 0.4664 -0.0277 -0.0459 0.0694  2   MET   B CE  
3909 N N   A VAL   B 3   ? 0.2326 0.2819 0.3084 -0.0810 -0.0839 0.1323  3   VAL   B N   
3910 N N   B VAL   B 3   ? 0.2554 0.2986 0.2818 -0.0516 -0.0612 0.0921  3   VAL   B N   
3911 C CA  A VAL   B 3   ? 0.2245 0.2557 0.2965 -0.0734 -0.0753 0.1162  3   VAL   B CA  
3912 C CA  B VAL   B 3   ? 0.2418 0.2759 0.2682 -0.0450 -0.0567 0.0818  3   VAL   B CA  
3913 C C   A VAL   B 3   ? 0.2127 0.2454 0.2635 -0.0623 -0.0672 0.1062  3   VAL   B C   
3914 C C   B VAL   B 3   ? 0.2235 0.2606 0.2473 -0.0435 -0.0573 0.0837  3   VAL   B C   
3915 O O   A VAL   B 3   ? 0.2065 0.2441 0.2718 -0.0653 -0.0649 0.1136  3   VAL   B O   
3916 O O   B VAL   B 3   ? 0.2198 0.2677 0.2393 -0.0293 -0.0622 0.0900  3   VAL   B O   
3917 C CB  A VAL   B 3   ? 0.2401 0.2501 0.3307 -0.0747 -0.0643 0.1036  3   VAL   B CB  
3918 C CB  B VAL   B 3   ? 0.2507 0.2708 0.2783 -0.0423 -0.0483 0.0739  3   VAL   B CB  
3919 C CG1 A VAL   B 3   ? 0.2485 0.2456 0.3444 -0.0717 -0.0616 0.1044  3   VAL   B CG1 
3920 C CG1 B VAL   B 3   ? 0.2550 0.2673 0.2837 -0.0414 -0.0466 0.0743  3   VAL   B CG1 
3921 C CG2 A VAL   B 3   ? 0.2450 0.2560 0.3446 -0.0740 -0.0556 0.1036  3   VAL   B CG2 
3922 C CG2 B VAL   B 3   ? 0.2537 0.2718 0.2795 -0.0401 -0.0462 0.0746  3   VAL   B CG2 
3941 N N   . ASN   B 4   ? 0.2080 0.2372 0.2417 -0.0587 -0.0559 0.0833  4   ASN   B N   
3942 C CA  . ASN   B 4   ? 0.2090 0.2321 0.2240 -0.0632 -0.0499 0.0494  4   ASN   B CA  
3943 C C   . ASN   B 4   ? 0.2184 0.2450 0.2271 -0.0647 -0.0401 0.0373  4   ASN   B C   
3944 O O   . ASN   B 4   ? 0.2184 0.2473 0.2465 -0.0630 -0.0427 0.0307  4   ASN   B O   
3945 C CB  . ASN   B 4   ? 0.2014 0.2269 0.2228 -0.0565 -0.0510 0.0442  4   ASN   B CB  
3946 C CG  . ASN   B 4   ? 0.2011 0.2070 0.2145 -0.0525 -0.0538 0.0343  4   ASN   B CG  
3947 O OD1 . ASN   B 4   ? 0.2035 0.1843 0.2153 -0.0514 -0.0591 0.0300  4   ASN   B OD1 
3948 N ND2 . ASN   B 4   ? 0.2217 0.2151 0.2227 -0.0333 -0.0468 0.0255  4   ASN   B ND2 
3956 N N   . SER   B 5   ? 0.2394 0.2641 0.2388 -0.0678 -0.0147 0.0344  5   SER   B N   
3957 C CA  . SER   B 5   ? 0.2662 0.2966 0.2705 -0.0618 0.0102  0.0280  5   SER   B CA  
3958 C C   . SER   B 5   ? 0.2854 0.2991 0.2949 -0.0765 0.0335  0.0309  5   SER   B C   
3959 O O   . SER   B 5   ? 0.2975 0.2918 0.3361 -0.0707 0.0527  0.0276  5   SER   B O   
3960 C CB  . SER   B 5   ? 0.2820 0.3185 0.3033 -0.0465 0.0106  0.0336  5   SER   B CB  
3961 O OG  . SER   B 5   ? 0.3087 0.3452 0.3476 -0.0287 0.0080  0.0421  5   SER   B OG  
3967 N N   . PHE   B 6   ? 0.3024 0.3122 0.2803 -0.0816 0.0445  0.0364  6   PHE   B N   
3968 C CA  . PHE   B 6   ? 0.3093 0.3136 0.2490 -0.0957 0.0456  0.0212  6   PHE   B CA  
3969 C C   . PHE   B 6   ? 0.3620 0.3443 0.2971 -0.0948 0.0581  -0.0134 6   PHE   B C   
3970 O O   . PHE   B 6   ? 0.3733 0.3764 0.3222 -0.0812 0.0424  -0.0262 6   PHE   B O   
3971 C CB  . PHE   B 6   ? 0.2754 0.2899 0.2073 -0.0904 0.0199  0.0201  6   PHE   B CB  
3972 C CG  . PHE   B 6   ? 0.2408 0.2605 0.1972 -0.0845 -0.0021 0.0150  6   PHE   B CG  
3973 C CD1 . PHE   B 6   ? 0.2372 0.2366 0.1875 -0.0802 -0.0254 0.0058  6   PHE   B CD1 
3974 C CD2 . PHE   B 6   ? 0.2172 0.2566 0.1902 -0.0687 0.0014  0.0372  6   PHE   B CD2 
3975 C CE1 . PHE   B 6   ? 0.2279 0.2223 0.1923 -0.0728 -0.0243 0.0067  6   PHE   B CE1 
3976 C CE2 . PHE   B 6   ? 0.2187 0.2448 0.2215 -0.0588 0.0074  0.0367  6   PHE   B CE2 
3977 C CZ  . PHE   B 6   ? 0.2189 0.2269 0.2105 -0.0651 -0.0065 0.0157  6   PHE   B CZ  
3987 N N   A SER   B 7   ? 0.3846 0.3298 0.2999 -0.1105 0.0741  -0.0339 7   SER   B N   
3988 N N   B SER   B 7   ? 0.3802 0.3394 0.3104 -0.1023 0.0677  -0.0222 7   SER   B N   
3989 C CA  A SER   B 7   ? 0.4068 0.3333 0.3289 -0.1109 0.0891  -0.0443 7   SER   B CA  
3990 C CA  B SER   B 7   ? 0.3972 0.3428 0.3391 -0.1010 0.0766  -0.0262 7   SER   B CA  
3991 C C   A SER   B 7   ? 0.4065 0.3184 0.3169 -0.1193 0.0997  -0.0553 7   SER   B C   
3992 C C   B SER   B 7   ? 0.3981 0.3311 0.3315 -0.1061 0.0818  -0.0341 7   SER   B C   
3993 O O   A SER   B 7   ? 0.4144 0.3174 0.3240 -0.1228 0.1017  -0.0545 7   SER   B O   
3994 O O   B SER   B 7   ? 0.4037 0.3324 0.3355 -0.1081 0.0827  -0.0315 7   SER   B O   
3995 C CB  A SER   B 7   ? 0.4230 0.3486 0.3744 -0.1043 0.0975  -0.0430 7   SER   B CB  
3996 C CB  B SER   B 7   ? 0.4086 0.3540 0.3784 -0.0952 0.0818  -0.0244 7   SER   B CB  
3997 O OG  A SER   B 7   ? 0.4339 0.3630 0.4117 -0.1018 0.0986  -0.0454 7   SER   B OG  
3998 O OG  B SER   B 7   ? 0.4163 0.3635 0.4065 -0.0917 0.0819  -0.0259 7   SER   B OG  
4009 N N   A GLY   B 8   ? 0.4014 0.3077 0.3162 -0.1133 0.1016  -0.0671 8   GLY   B N   
4010 N N   B GLY   B 8   ? 0.3941 0.3184 0.3281 -0.1033 0.0832  -0.0462 8   GLY   B N   
4011 C CA  A GLY   B 8   ? 0.3900 0.2956 0.3156 -0.1116 0.1041  -0.0699 8   GLY   B CA  
4012 C CA  B GLY   B 8   ? 0.3856 0.3034 0.3228 -0.1039 0.0861  -0.0541 8   GLY   B CA  
4013 C C   A GLY   B 8   ? 0.3774 0.2784 0.3092 -0.1118 0.1061  -0.0651 8   GLY   B C   
4014 C C   B GLY   B 8   ? 0.3762 0.2848 0.3136 -0.1057 0.0899  -0.0584 8   GLY   B C   
4015 O O   A GLY   B 8   ? 0.3830 0.2820 0.3255 -0.1071 0.1107  -0.0693 8   GLY   B O   
4016 O O   B GLY   B 8   ? 0.3807 0.2916 0.3225 -0.0995 0.0885  -0.0623 8   GLY   B O   
4023 N N   . TYR   B 9   ? 0.3686 0.2635 0.3010 -0.1036 0.0888  -0.0657 9   TYR   B N   
4024 C CA  . TYR   B 9   ? 0.3502 0.2297 0.2647 -0.0852 0.0657  -0.0560 9   TYR   B CA  
4025 C C   . TYR   B 9   ? 0.3453 0.2324 0.2630 -0.0795 0.0362  -0.0456 9   TYR   B C   
4026 O O   . TYR   B 9   ? 0.3554 0.2517 0.2881 -0.0810 0.0356  -0.0345 9   TYR   B O   
4027 C CB  . TYR   B 9   ? 0.3396 0.2019 0.2633 -0.0756 0.0624  -0.0476 9   TYR   B CB  
4028 C CG  . TYR   B 9   ? 0.3250 0.1820 0.2641 -0.0815 0.0531  -0.0505 9   TYR   B CG  
4029 C CD1 . TYR   B 9   ? 0.3225 0.1848 0.2755 -0.0904 0.0573  -0.0435 9   TYR   B CD1 
4030 C CD2 . TYR   B 9   ? 0.3114 0.1752 0.2555 -0.0737 0.0456  -0.0484 9   TYR   B CD2 
4031 C CE1 . TYR   B 9   ? 0.3168 0.1964 0.2753 -0.0916 0.0569  -0.0594 9   TYR   B CE1 
4032 C CE2 . TYR   B 9   ? 0.3079 0.1807 0.2618 -0.0724 0.0474  -0.0565 9   TYR   B CE2 
4033 C CZ  . TYR   B 9   ? 0.3093 0.1949 0.2708 -0.0841 0.0528  -0.0708 9   TYR   B CZ  
4034 O OH  . TYR   B 9   ? 0.3041 0.2086 0.2851 -0.0895 0.0614  -0.0760 9   TYR   B OH  
4045 N N   . LEU   B 10  ? 0.3284 0.2063 0.2411 -0.0767 0.0123  -0.0534 10  LEU   B N   
4046 C CA  . LEU   B 10  ? 0.3227 0.2009 0.2459 -0.0817 -0.0184 -0.0419 10  LEU   B CA  
4047 C C   . LEU   B 10  ? 0.2995 0.2025 0.2432 -0.0838 -0.0395 -0.0358 10  LEU   B C   
4048 O O   . LEU   B 10  ? 0.2852 0.2031 0.2466 -0.0686 -0.0401 -0.0200 10  LEU   B O   
4049 C CB  . LEU   B 10  ? 0.3364 0.1973 0.2665 -0.0809 -0.0401 -0.0232 10  LEU   B CB  
4050 C CG  . LEU   B 10  ? 0.3526 0.2024 0.2983 -0.0733 -0.0635 -0.0104 10  LEU   B CG  
4051 C CD1 . LEU   B 10  ? 0.3621 0.2179 0.3178 -0.0686 -0.0608 -0.0099 10  LEU   B CD1 
4052 C CD2 . LEU   B 10  ? 0.3605 0.2019 0.3214 -0.0738 -0.0588 0.0139  10  LEU   B CD2 
4064 N N   . LYS   B 11  ? 0.3090 0.2325 0.2550 -0.0766 -0.0411 -0.0306 11  LYS   B N   
4065 C CA  . LYS   B 11  ? 0.3228 0.2572 0.2942 -0.0616 -0.0550 -0.0402 11  LYS   B CA  
4066 C C   . LYS   B 11  ? 0.3021 0.2357 0.2952 -0.0793 -0.0590 -0.0500 11  LYS   B C   
4067 O O   . LYS   B 11  ? 0.3225 0.2520 0.3204 -0.0888 -0.0549 -0.0788 11  LYS   B O   
4068 C CB  . LYS   B 11  ? 0.3561 0.3098 0.3646 -0.0362 -0.0507 -0.0355 11  LYS   B CB  
4069 C CG  . LYS   B 11  ? 0.3857 0.3435 0.4394 -0.0204 -0.0502 -0.0392 11  LYS   B CG  
4070 C CD  . LYS   B 11  ? 0.4070 0.3682 0.4960 -0.0102 -0.0494 -0.0462 11  LYS   B CD  
4071 C CE  . LYS   B 11  ? 0.4219 0.3867 0.5365 -0.0050 -0.0451 -0.0504 11  LYS   B CE  
4072 N NZ  . LYS   B 11  ? 0.4297 0.3982 0.5602 -0.0017 -0.0402 -0.0480 11  LYS   B NZ  
4086 N N   . LEU   B 12  ? 0.2697 0.2109 0.2923 -0.0740 -0.0607 -0.0413 12  LEU   B N   
4087 C CA  . LEU   B 12  ? 0.2538 0.1894 0.2988 -0.0639 -0.0466 -0.0282 12  LEU   B CA  
4088 C C   . LEU   B 12  ? 0.2416 0.1903 0.3108 -0.0639 -0.0599 -0.0257 12  LEU   B C   
4089 O O   . LEU   B 12  ? 0.2381 0.1926 0.3214 -0.0724 -0.0669 -0.0245 12  LEU   B O   
4090 C CB  . LEU   B 12  ? 0.2538 0.1674 0.2912 -0.0499 -0.0320 -0.0272 12  LEU   B CB  
4091 C CG  . LEU   B 12  ? 0.2501 0.1611 0.2991 -0.0462 -0.0256 -0.0221 12  LEU   B CG  
4092 C CD1 . LEU   B 12  ? 0.2581 0.1612 0.3071 -0.0346 -0.0219 -0.0082 12  LEU   B CD1 
4093 C CD2 . LEU   B 12  ? 0.2505 0.1700 0.3111 -0.0469 -0.0205 -0.0259 12  LEU   B CD2 
4105 N N   . THR   B 13  ? 0.2304 0.1900 0.3128 -0.0604 -0.0612 -0.0358 13  THR   B N   
4106 C CA  . THR   B 13  ? 0.2268 0.1996 0.3010 -0.0610 -0.0699 -0.0214 13  THR   B CA  
4107 C C   . THR   B 13  ? 0.2703 0.2142 0.3170 -0.0709 -0.0806 -0.0143 13  THR   B C   
4108 O O   . THR   B 13  ? 0.2862 0.2105 0.3361 -0.0677 -0.0521 -0.0127 13  THR   B O   
4109 C CB  . THR   B 13  ? 0.2023 0.1987 0.3046 -0.0517 -0.0660 -0.0170 13  THR   B CB  
4110 O OG1 . THR   B 13  ? 0.1965 0.1884 0.3150 -0.0448 -0.0554 -0.0264 13  THR   B OG1 
4111 C CG2 . THR   B 13  ? 0.2124 0.2072 0.3111 -0.0447 -0.0556 -0.0030 13  THR   B CG2 
4119 N N   A ASP   B 14  ? 0.2815 0.2288 0.3214 -0.0773 -0.1062 -0.0031 14  ASP   B N   
4120 N N   B ASP   B 14  ? 0.2800 0.2289 0.3191 -0.0726 -0.0937 -0.0023 14  ASP   B N   
4121 C CA  A ASP   B 14  ? 0.2949 0.2454 0.3477 -0.0762 -0.1065 0.0141  14  ASP   B CA  
4122 C CA  B ASP   B 14  ? 0.2886 0.2430 0.3364 -0.0698 -0.0929 0.0128  14  ASP   B CA  
4123 C C   A ASP   B 14  ? 0.2791 0.2270 0.3163 -0.0785 -0.0952 0.0190  14  ASP   B C   
4124 C C   B ASP   B 14  ? 0.2731 0.2249 0.3106 -0.0705 -0.0904 0.0159  14  ASP   B C   
4125 O O   A ASP   B 14  ? 0.3022 0.2431 0.3218 -0.0754 -0.0914 0.0322  14  ASP   B O   
4126 O O   B ASP   B 14  ? 0.2884 0.2323 0.3120 -0.0661 -0.0892 0.0239  14  ASP   B O   
4127 C CB  A ASP   B 14  ? 0.3199 0.2799 0.4156 -0.0700 -0.1142 0.0130  14  ASP   B CB  
4128 C CB  B ASP   B 14  ? 0.3086 0.2731 0.3882 -0.0635 -0.0923 0.0155  14  ASP   B CB  
4129 C CG  A ASP   B 14  ? 0.3446 0.3093 0.4800 -0.0633 -0.1112 0.0047  14  ASP   B CG  
4130 C CG  B ASP   B 14  ? 0.3266 0.2978 0.4351 -0.0566 -0.0867 0.0113  14  ASP   B CG  
4131 O OD1 A ASP   B 14  ? 0.3605 0.3186 0.4993 -0.0650 -0.1102 -0.0039 14  ASP   B OD1 
4132 O OD1 B ASP   B 14  ? 0.3339 0.3105 0.4518 -0.0541 -0.0803 0.0077  14  ASP   B OD1 
4133 O OD2 A ASP   B 14  ? 0.3469 0.3224 0.5114 -0.0615 -0.1087 0.0085  14  ASP   B OD2 
4134 O OD2 B ASP   B 14  ? 0.3305 0.3040 0.4560 -0.0587 -0.0889 0.0119  14  ASP   B OD2 
4143 N N   . ASN   B 15  ? 0.2443 0.2020 0.2968 -0.0658 -0.0959 0.0111  15  ASN   B N   
4144 C CA  . ASN   B 15  ? 0.1991 0.1738 0.2797 -0.0423 -0.0782 0.0069  15  ASN   B CA  
4145 C C   . ASN   B 15  ? 0.1852 0.1574 0.2698 -0.0301 -0.0602 -0.0012 15  ASN   B C   
4146 O O   . ASN   B 15  ? 0.1796 0.1449 0.2774 -0.0290 -0.0567 -0.0082 15  ASN   B O   
4147 C CB  . ASN   B 15  ? 0.1834 0.1755 0.2899 -0.0237 -0.0714 0.0046  15  ASN   B CB  
4148 C CG  . ASN   B 15  ? 0.1713 0.1678 0.3028 -0.0240 -0.0430 0.0091  15  ASN   B CG  
4149 O OD1 . ASN   B 15  ? 0.1795 0.1899 0.3244 -0.0462 -0.0525 0.0189  15  ASN   B OD1 
4150 N ND2 . ASN   B 15  ? 0.1648 0.1420 0.2899 -0.0142 -0.0122 -0.0090 15  ASN   B ND2 
4158 N N   . VAL   B 16  ? 0.1879 0.1523 0.2609 -0.0355 -0.0626 -0.0084 16  VAL   B N   
4159 C CA  . VAL   B 16  ? 0.1858 0.1573 0.2563 -0.0342 -0.0488 -0.0258 16  VAL   B CA  
4160 C C   . VAL   B 16  ? 0.1834 0.1659 0.2539 -0.0415 -0.0551 -0.0173 16  VAL   B C   
4161 O O   . VAL   B 16  ? 0.1899 0.1808 0.2775 -0.0375 -0.0470 -0.0302 16  VAL   B O   
4162 C CB  . VAL   B 16  ? 0.1819 0.1569 0.2574 -0.0213 -0.0396 -0.0239 16  VAL   B CB  
4163 C CG1 . VAL   B 16  ? 0.1873 0.1498 0.2515 -0.0048 -0.0419 -0.0181 16  VAL   B CG1 
4164 C CG2 . VAL   B 16  ? 0.1810 0.1648 0.2644 -0.0174 -0.0240 -0.0265 16  VAL   B CG2 
4174 N N   . TYR   B 17  ? 0.1916 0.1710 0.2452 -0.0404 -0.0473 -0.0174 17  TYR   B N   
4175 C CA  . TYR   B 17  ? 0.2055 0.1878 0.2383 -0.0487 -0.0424 -0.0032 17  TYR   B CA  
4176 C C   . TYR   B 17  ? 0.1931 0.1600 0.2442 -0.0454 -0.0290 -0.0141 17  TYR   B C   
4177 O O   . TYR   B 17  ? 0.1835 0.1653 0.2530 -0.0340 -0.0329 -0.0330 17  TYR   B O   
4178 C CB  . TYR   B 17  ? 0.2350 0.2298 0.2585 -0.0372 -0.0530 0.0256  17  TYR   B CB  
4179 C CG  . TYR   B 17  ? 0.2664 0.2782 0.3060 -0.0295 -0.0608 0.0326  17  TYR   B CG  
4180 C CD1 . TYR   B 17  ? 0.2830 0.2925 0.3276 -0.0290 -0.0653 0.0450  17  TYR   B CD1 
4181 C CD2 . TYR   B 17  ? 0.2886 0.3073 0.3351 -0.0233 -0.0663 0.0300  17  TYR   B CD2 
4182 C CE1 . TYR   B 17  ? 0.3036 0.3176 0.3504 -0.0195 -0.0768 0.0398  17  TYR   B CE1 
4183 C CE2 . TYR   B 17  ? 0.3037 0.3243 0.3559 -0.0096 -0.0813 0.0362  17  TYR   B CE2 
4184 C CZ  . TYR   B 17  ? 0.3157 0.3284 0.3650 -0.0087 -0.0853 0.0366  17  TYR   B CZ  
4185 O OH  . TYR   B 17  ? 0.3316 0.3444 0.3819 -0.0004 -0.0920 0.0332  17  TYR   B OH  
4195 N N   . ILE   B 18  ? 0.1998 0.1629 0.2340 -0.0385 -0.0219 -0.0175 18  ILE   B N   
4196 C CA  . ILE   B 18  ? 0.2048 0.1552 0.2323 -0.0387 -0.0186 -0.0312 18  ILE   B CA  
4197 C C   . ILE   B 18  ? 0.2246 0.1569 0.2186 -0.0489 -0.0145 -0.0389 18  ILE   B C   
4198 O O   . ILE   B 18  ? 0.2471 0.1774 0.2432 -0.0542 -0.0119 -0.0417 18  ILE   B O   
4199 C CB  . ILE   B 18  ? 0.2067 0.1507 0.2510 -0.0461 -0.0232 -0.0280 18  ILE   B CB  
4200 C CG1 . ILE   B 18  ? 0.2019 0.1541 0.2506 -0.0451 -0.0193 -0.0215 18  ILE   B CG1 
4201 C CG2 . ILE   B 18  ? 0.2096 0.1619 0.2618 -0.0498 -0.0300 -0.0142 18  ILE   B CG2 
4202 C CD1 . ILE   B 18  ? 0.2116 0.1852 0.2634 -0.0369 -0.0322 -0.0006 18  ILE   B CD1 
4214 N N   . LYS   B 19  ? 0.2256 0.1571 0.2288 -0.0334 0.0188  -0.0394 19  LYS   B N   
4215 C CA  . LYS   B 19  ? 0.2281 0.1642 0.2450 -0.0362 0.0149  -0.0446 19  LYS   B CA  
4216 C C   . LYS   B 19  ? 0.2092 0.1592 0.2675 -0.0312 0.0198  -0.0513 19  LYS   B C   
4217 O O   . LYS   B 19  ? 0.1978 0.1643 0.2553 -0.0237 0.0093  -0.0483 19  LYS   B O   
4218 C CB  . LYS   B 19  ? 0.2518 0.1873 0.2577 -0.0376 0.0245  -0.0403 19  LYS   B CB  
4219 C CG  . LYS   B 19  ? 0.2797 0.2038 0.2692 -0.0405 0.0251  -0.0301 19  LYS   B CG  
4220 C CD  . LYS   B 19  ? 0.3056 0.2333 0.2820 -0.0509 0.0339  -0.0183 19  LYS   B CD  
4221 C CE  . LYS   B 19  ? 0.3290 0.2604 0.2979 -0.0540 0.0342  -0.0190 19  LYS   B CE  
4222 N NZ  . LYS   B 19  ? 0.3429 0.2760 0.3005 -0.0593 0.0431  -0.0097 19  LYS   B NZ  
4236 N N   . ASN   B 20  ? 0.2048 0.1702 0.3053 -0.0246 0.0322  -0.0648 20  ASN   B N   
4237 C CA  . ASN   B 20  ? 0.2026 0.1860 0.3312 -0.0204 0.0304  -0.0750 20  ASN   B CA  
4238 C C   . ASN   B 20  ? 0.2050 0.2067 0.3346 -0.0221 0.0446  -0.0834 20  ASN   B C   
4239 O O   . ASN   B 20  ? 0.2229 0.2425 0.3559 -0.0325 0.0501  -0.0858 20  ASN   B O   
4240 C CB  . ASN   B 20  ? 0.2260 0.1889 0.3603 0.0039  0.0241  -0.0704 20  ASN   B CB  
4241 C CG  . ASN   B 20  ? 0.2498 0.1991 0.3809 0.0341  0.0289  -0.0850 20  ASN   B CG  
4242 O OD1 . ASN   B 20  ? 0.2853 0.2258 0.4117 0.0558  0.0319  -0.0860 20  ASN   B OD1 
4243 N ND2 . ASN   B 20  ? 0.2353 0.1962 0.3782 0.0279  0.0087  -0.0844 20  ASN   B ND2 
4250 N N   . ALA   B 21  ? 0.2034 0.1899 0.3319 -0.0297 0.0406  -0.0648 21  ALA   B N   
4251 C CA  . ALA   B 21  ? 0.2079 0.2002 0.3328 -0.0337 0.0404  -0.0475 21  ALA   B CA  
4252 C C   . ALA   B 21  ? 0.2072 0.1757 0.3181 -0.0214 0.0390  -0.0385 21  ALA   B C   
4253 O O   . ALA   B 21  ? 0.2121 0.1633 0.3288 -0.0328 0.0285  -0.0330 21  ALA   B O   
4254 C CB  . ALA   B 21  ? 0.2224 0.2274 0.3359 -0.0436 0.0434  -0.0338 21  ALA   B CB  
4260 N N   . ASP   B 22  ? 0.2016 0.1654 0.3170 -0.0210 0.0304  -0.0279 22  ASP   B N   
4261 C CA  . ASP   B 22  ? 0.1929 0.1574 0.3111 -0.0114 0.0216  -0.0271 22  ASP   B CA  
4262 C C   . ASP   B 22  ? 0.1878 0.1506 0.2798 -0.0189 0.0119  -0.0193 22  ASP   B C   
4263 O O   . ASP   B 22  ? 0.1914 0.1532 0.2842 -0.0106 0.0109  -0.0088 22  ASP   B O   
4264 C CB  . ASP   B 22  ? 0.2026 0.1676 0.3443 -0.0079 0.0171  -0.0108 22  ASP   B CB  
4265 C CG  . ASP   B 22  ? 0.2042 0.1827 0.3763 -0.0050 -0.0018 0.0015  22  ASP   B CG  
4266 O OD1 . ASP   B 22  ? 0.2128 0.1714 0.3772 -0.0031 -0.0192 0.0019  22  ASP   B OD1 
4267 O OD2 . ASP   B 22  ? 0.2180 0.2114 0.4189 0.0074  -0.0276 -0.0095 22  ASP   B OD2 
4272 N N   . ILE   B 23  ? 0.1904 0.1473 0.2494 -0.0165 0.0031  0.0113  23  ILE   B N   
4273 C CA  . ILE   B 23  ? 0.1792 0.1444 0.2335 -0.0184 -0.0076 0.0026  23  ILE   B CA  
4274 C C   . ILE   B 23  ? 0.1706 0.1451 0.2325 -0.0142 -0.0204 -0.0024 23  ILE   B C   
4275 O O   . ILE   B 23  ? 0.1641 0.1429 0.2302 -0.0148 -0.0084 0.0053  23  ILE   B O   
4276 C CB  . ILE   B 23  ? 0.1761 0.1485 0.2511 -0.0250 -0.0079 0.0124  23  ILE   B CB  
4277 C CG1 . ILE   B 23  ? 0.1786 0.1603 0.2629 -0.0153 0.0023  0.0319  23  ILE   B CG1 
4278 C CG2 . ILE   B 23  ? 0.1885 0.1729 0.2705 -0.0282 -0.0056 0.0081  23  ILE   B CG2 
4279 C CD1 . ILE   B 23  ? 0.1842 0.1710 0.2640 -0.0140 0.0075  0.0278  23  ILE   B CD1 
4291 N N   . VAL   B 24  ? 0.1688 0.1463 0.2466 -0.0116 -0.0154 -0.0020 24  VAL   B N   
4292 C CA  . VAL   B 24  ? 0.1636 0.1545 0.2629 -0.0064 -0.0238 -0.0053 24  VAL   B CA  
4293 C C   . VAL   B 24  ? 0.1660 0.1574 0.2743 -0.0088 -0.0179 0.0010  24  VAL   B C   
4294 O O   . VAL   B 24  ? 0.1634 0.1666 0.2781 -0.0207 -0.0063 0.0094  24  VAL   B O   
4295 C CB  . VAL   B 24  ? 0.1755 0.1706 0.2664 -0.0001 -0.0298 -0.0040 24  VAL   B CB  
4296 C CG1 . VAL   B 24  ? 0.1713 0.1754 0.2990 -0.0148 -0.0317 -0.0004 24  VAL   B CG1 
4297 C CG2 . VAL   B 24  ? 0.1832 0.1979 0.2636 0.0116  -0.0341 -0.0078 24  VAL   B CG2 
4307 N N   . GLU   B 25  ? 0.1867 0.1678 0.2833 -0.0062 -0.0096 0.0043  25  GLU   B N   
4308 C CA  . GLU   B 25  ? 0.2008 0.1997 0.2907 0.0001  0.0045  -0.0100 25  GLU   B CA  
4309 C C   . GLU   B 25  ? 0.1942 0.1860 0.2466 -0.0090 0.0071  -0.0037 25  GLU   B C   
4310 O O   . GLU   B 25  ? 0.1990 0.2057 0.2596 -0.0104 0.0137  0.0038  25  GLU   B O   
4311 C CB  . GLU   B 25  ? 0.2282 0.2593 0.3583 0.0203  0.0103  -0.0147 25  GLU   B CB  
4312 C CG  . GLU   B 25  ? 0.2777 0.3169 0.4489 0.0305  0.0119  -0.0213 25  GLU   B CG  
4313 C CD  . GLU   B 25  ? 0.3314 0.3729 0.5249 0.0253  0.0112  -0.0200 25  GLU   B CD  
4314 O OE1 . GLU   B 25  ? 0.3407 0.4056 0.5549 0.0291  0.0157  -0.0178 25  GLU   B OE1 
4315 O OE2 . GLU   B 25  ? 0.3361 0.3943 0.5548 0.0235  0.0083  -0.0218 25  GLU   B OE2 
4322 N N   . GLU   B 26  ? 0.1899 0.1749 0.2259 -0.0272 0.0019  -0.0019 26  GLU   B N   
4323 C CA  . GLU   B 26  ? 0.1891 0.1907 0.2422 -0.0381 -0.0045 0.0073  26  GLU   B CA  
4324 C C   . GLU   B 26  ? 0.1704 0.1901 0.2311 -0.0235 0.0034  0.0171  26  GLU   B C   
4325 O O   . GLU   B 26  ? 0.1901 0.2155 0.2249 -0.0255 -0.0036 0.0200  26  GLU   B O   
4326 C CB  . GLU   B 26  ? 0.2235 0.2122 0.2552 -0.0468 0.0036  0.0175  26  GLU   B CB  
4327 C CG  . GLU   B 26  ? 0.2685 0.2507 0.2939 -0.0524 0.0105  -0.0070 26  GLU   B CG  
4328 C CD  . GLU   B 26  ? 0.2934 0.2769 0.3155 -0.0777 0.0210  -0.0465 26  GLU   B CD  
4329 O OE1 . GLU   B 26  ? 0.3132 0.2656 0.3250 -0.0848 0.0555  -0.0520 26  GLU   B OE1 
4330 O OE2 . GLU   B 26  ? 0.2954 0.3170 0.3485 -0.0787 0.0164  -0.0407 26  GLU   B OE2 
4337 N N   . ALA   B 27  ? 0.1570 0.1738 0.2342 -0.0260 0.0087  0.0222  27  ALA   B N   
4338 C CA  . ALA   B 27  ? 0.1630 0.1696 0.2359 -0.0180 0.0072  0.0310  27  ALA   B CA  
4339 C C   . ALA   B 27  ? 0.1702 0.1813 0.2625 -0.0141 0.0176  0.0410  27  ALA   B C   
4340 O O   . ALA   B 27  ? 0.1767 0.1882 0.2721 -0.0035 0.0197  0.0480  27  ALA   B O   
4341 C CB  . ALA   B 27  ? 0.1745 0.1528 0.2341 -0.0153 0.0074  0.0242  27  ALA   B CB  
4347 N N   . LYS   B 28  ? 0.1649 0.1953 0.3022 -0.0163 0.0253  0.0568  28  LYS   B N   
4348 C CA  . LYS   B 28  ? 0.1814 0.2346 0.3209 -0.0123 0.0582  0.0777  28  LYS   B CA  
4349 C C   . LYS   B 28  ? 0.2053 0.2536 0.3079 -0.0057 0.0639  0.0677  28  LYS   B C   
4350 O O   . LYS   B 28  ? 0.2256 0.2625 0.3081 -0.0088 0.0544  0.0710  28  LYS   B O   
4351 C CB  . LYS   B 28  ? 0.2064 0.2775 0.3606 -0.0009 0.0829  0.0876  28  LYS   B CB  
4352 C CG  . LYS   B 28  ? 0.2325 0.3323 0.3960 0.0055  0.0994  0.1011  28  LYS   B CG  
4353 C CD  . LYS   B 28  ? 0.2752 0.3830 0.4483 0.0138  0.1054  0.1022  28  LYS   B CD  
4354 C CE  . LYS   B 28  ? 0.3428 0.4264 0.4883 0.0214  0.1074  0.1055  28  LYS   B CE  
4355 N NZ  . LYS   B 28  ? 0.3829 0.4785 0.5137 0.0278  0.1106  0.1125  28  LYS   B NZ  
4369 N N   . LYS   B 29  ? 0.2189 0.2816 0.3140 0.0064  0.0660  0.0532  29  LYS   B N   
4370 C CA  . LYS   B 29  ? 0.2666 0.3182 0.3455 0.0067  0.0605  0.0567  29  LYS   B CA  
4371 C C   . LYS   B 29  ? 0.2569 0.3184 0.3150 0.0080  0.0464  0.0664  29  LYS   B C   
4372 O O   . LYS   B 29  ? 0.2685 0.3373 0.3230 0.0125  0.0554  0.0712  29  LYS   B O   
4373 C CB  . LYS   B 29  ? 0.3306 0.3610 0.4282 0.0083  0.0576  0.0474  29  LYS   B CB  
4374 C CG  . LYS   B 29  ? 0.3879 0.4014 0.5090 0.0076  0.0581  0.0457  29  LYS   B CG  
4375 C CD  . LYS   B 29  ? 0.4280 0.4298 0.5770 0.0060  0.0619  0.0403  29  LYS   B CD  
4376 C CE  . LYS   B 29  ? 0.4536 0.4396 0.6265 0.0036  0.0685  0.0384  29  LYS   B CE  
4377 N NZ  . LYS   B 29  ? 0.4914 0.4514 0.6490 0.0023  0.0719  0.0388  29  LYS   B NZ  
4391 N N   . VAL   B 30  ? 0.2294 0.2975 0.2879 -0.0031 0.0330  0.0655  30  VAL   B N   
4392 C CA  . VAL   B 30  ? 0.2148 0.2822 0.2972 -0.0115 0.0037  0.0688  30  VAL   B CA  
4393 C C   . VAL   B 30  ? 0.1912 0.2730 0.2957 -0.0127 0.0082  0.0934  30  VAL   B C   
4394 O O   . VAL   B 30  ? 0.2147 0.2932 0.3085 -0.0024 0.0157  0.1083  30  VAL   B O   
4395 C CB  . VAL   B 30  ? 0.2188 0.2725 0.3111 -0.0212 -0.0253 0.0591  30  VAL   B CB  
4396 C CG1 . VAL   B 30  ? 0.2253 0.2833 0.3125 -0.0160 -0.0272 0.0465  30  VAL   B CG1 
4397 C CG2 . VAL   B 30  ? 0.2326 0.2691 0.3255 -0.0282 -0.0327 0.0402  30  VAL   B CG2 
4407 N N   A LYS   B 31  ? 0.1754 0.2496 0.3125 -0.0266 0.0058  0.1043  31  LYS   B N   
4408 N N   B LYS   B 31  ? 0.1897 0.2559 0.3024 -0.0202 -0.0017 0.0903  31  LYS   B N   
4409 C CA  A LYS   B 31  ? 0.1662 0.2448 0.3354 -0.0392 0.0078  0.1073  31  LYS   B CA  
4410 C CA  B LYS   B 31  ? 0.1918 0.2486 0.3152 -0.0269 -0.0095 0.0837  31  LYS   B CA  
4411 C C   A LYS   B 31  ? 0.1658 0.2089 0.3068 -0.0343 -0.0170 0.0868  31  LYS   B C   
4412 C C   B LYS   B 31  ? 0.1821 0.2106 0.2890 -0.0288 -0.0286 0.0714  31  LYS   B C   
4413 O O   A LYS   B 31  ? 0.1675 0.2182 0.3246 -0.0282 -0.0098 0.0979  31  LYS   B O   
4414 O O   B LYS   B 31  ? 0.1842 0.2162 0.2957 -0.0260 -0.0298 0.0757  31  LYS   B O   
4415 C CB  A LYS   B 31  ? 0.1824 0.2847 0.3875 -0.0351 0.0252  0.1207  31  LYS   B CB  
4416 C CB  B LYS   B 31  ? 0.2131 0.2811 0.3562 -0.0215 -0.0016 0.0839  31  LYS   B CB  
4417 C CG  A LYS   B 31  ? 0.2085 0.3198 0.4307 -0.0331 0.0324  0.1172  31  LYS   B CG  
4418 C CG  B LYS   B 31  ? 0.2364 0.3075 0.3901 -0.0197 0.0014  0.0732  31  LYS   B CG  
4419 C CD  A LYS   B 31  ? 0.2374 0.3493 0.4695 -0.0230 0.0283  0.1044  31  LYS   B CD  
4420 C CD  B LYS   B 31  ? 0.2565 0.3299 0.4215 -0.0175 0.0027  0.0629  31  LYS   B CD  
4421 C CE  A LYS   B 31  ? 0.2528 0.3679 0.4994 -0.0164 0.0212  0.0938  31  LYS   B CE  
4422 C CE  B LYS   B 31  ? 0.2698 0.3443 0.4468 -0.0180 0.0035  0.0559  31  LYS   B CE  
4423 N NZ  A LYS   B 31  ? 0.2686 0.3811 0.5160 -0.0071 0.0109  0.0831  31  LYS   B NZ  
4424 N NZ  B LYS   B 31  ? 0.2796 0.3546 0.4593 -0.0149 -0.0014 0.0488  31  LYS   B NZ  
4451 N N   . PRO   B 32  ? 0.1763 0.1706 0.2576 -0.0337 -0.0407 0.0563  32  PRO   B N   
4452 C CA  . PRO   B 32  ? 0.1864 0.1552 0.2314 -0.0326 -0.0358 0.0356  32  PRO   B CA  
4453 C C   . PRO   B 32  ? 0.1961 0.1442 0.2270 -0.0405 -0.0597 0.0366  32  PRO   B C   
4454 O O   . PRO   B 32  ? 0.2136 0.1506 0.2570 -0.0477 -0.0819 0.0363  32  PRO   B O   
4455 C CB  . PRO   B 32  ? 0.1926 0.1573 0.2235 -0.0354 -0.0365 0.0152  32  PRO   B CB  
4456 C CG  . PRO   B 32  ? 0.2125 0.1435 0.2314 -0.0268 -0.0548 0.0201  32  PRO   B CG  
4457 C CD  . PRO   B 32  ? 0.2002 0.1536 0.2377 -0.0266 -0.0674 0.0264  32  PRO   B CD  
4465 N N   . THR   B 33  ? 0.1970 0.1432 0.2148 -0.0341 -0.0585 0.0285  33  THR   B N   
4466 C CA  . THR   B 33  ? 0.1995 0.1473 0.1959 -0.0370 -0.0594 0.0346  33  THR   B CA  
4467 C C   . THR   B 33  ? 0.2043 0.1411 0.1980 -0.0343 -0.0512 0.0281  33  THR   B C   
4468 O O   . THR   B 33  ? 0.2267 0.1428 0.2071 -0.0438 -0.0630 0.0199  33  THR   B O   
4469 C CB  . THR   B 33  ? 0.2088 0.1597 0.2086 -0.0211 -0.0593 0.0348  33  THR   B CB  
4470 O OG1 . THR   B 33  ? 0.1977 0.1698 0.2148 -0.0292 -0.0609 0.0403  33  THR   B OG1 
4471 C CG2 . THR   B 33  ? 0.2251 0.1630 0.2291 -0.0163 -0.0487 0.0245  33  THR   B CG2 
4479 N N   . VAL   B 34  ? 0.1854 0.1364 0.1925 -0.0343 -0.0466 0.0155  34  VAL   B N   
4480 C CA  . VAL   B 34  ? 0.1742 0.1335 0.1958 -0.0292 -0.0345 0.0093  34  VAL   B CA  
4481 C C   . VAL   B 34  ? 0.1592 0.1265 0.1844 -0.0282 -0.0255 0.0005  34  VAL   B C   
4482 O O   . VAL   B 34  ? 0.1781 0.1281 0.1853 -0.0245 -0.0414 0.0051  34  VAL   B O   
4483 C CB  . VAL   B 34  ? 0.1778 0.1429 0.2240 -0.0151 -0.0273 0.0086  34  VAL   B CB  
4484 C CG1 . VAL   B 34  ? 0.1754 0.1497 0.2312 -0.0142 -0.0105 0.0050  34  VAL   B CG1 
4485 C CG2 . VAL   B 34  ? 0.1852 0.1499 0.2430 -0.0091 -0.0259 0.0119  34  VAL   B CG2 
4495 N N   . VAL   B 35  ? 0.1488 0.1256 0.1712 -0.0279 -0.0132 0.0064  35  VAL   B N   
4496 C CA  . VAL   B 35  ? 0.1457 0.1218 0.1756 -0.0231 -0.0071 -0.0014 35  VAL   B CA  
4497 C C   . VAL   B 35  ? 0.1348 0.1165 0.1677 -0.0199 -0.0144 0.0067  35  VAL   B C   
4498 O O   . VAL   B 35  ? 0.1412 0.1240 0.1747 -0.0216 -0.0069 -0.0047 35  VAL   B O   
4499 C CB  . VAL   B 35  ? 0.1459 0.1358 0.1936 -0.0213 -0.0054 0.0038  35  VAL   B CB  
4500 C CG1 . VAL   B 35  ? 0.1469 0.1467 0.2141 -0.0257 -0.0047 0.0008  35  VAL   B CG1 
4501 C CG2 . VAL   B 35  ? 0.1504 0.1453 0.2073 -0.0141 -0.0112 0.0034  35  VAL   B CG2 
4511 N N   . VAL   B 36  ? 0.1409 0.1208 0.1757 -0.0163 -0.0143 0.0065  36  VAL   B N   
4512 C CA  . VAL   B 36  ? 0.1371 0.1163 0.1751 -0.0144 -0.0189 0.0013  36  VAL   B CA  
4513 C C   . VAL   B 36  ? 0.1318 0.1184 0.1748 -0.0162 -0.0097 -0.0006 36  VAL   B C   
4514 O O   . VAL   B 36  ? 0.1367 0.1296 0.1892 -0.0141 -0.0021 -0.0063 36  VAL   B O   
4515 C CB  . VAL   B 36  ? 0.1351 0.1263 0.1835 -0.0175 -0.0141 0.0041  36  VAL   B CB  
4516 C CG1 . VAL   B 36  ? 0.1337 0.1406 0.1967 -0.0182 -0.0163 0.0037  36  VAL   B CG1 
4517 C CG2 . VAL   B 36  ? 0.1405 0.1318 0.1930 -0.0179 -0.0103 0.0053  36  VAL   B CG2 
4527 N N   . ASN   B 37  ? 0.1357 0.1281 0.1680 -0.0046 -0.0095 0.0036  37  ASN   B N   
4528 C CA  . ASN   B 37  ? 0.1378 0.1256 0.1765 -0.0029 -0.0165 0.0103  37  ASN   B CA  
4529 C C   . ASN   B 37  ? 0.1317 0.1255 0.1846 -0.0030 -0.0141 0.0078  37  ASN   B C   
4530 O O   . ASN   B 37  ? 0.1426 0.1388 0.1701 -0.0033 -0.0042 0.0016  37  ASN   B O   
4531 C CB  . ASN   B 37  ? 0.1336 0.1299 0.1722 -0.0077 -0.0201 0.0019  37  ASN   B CB  
4532 C CG  . ASN   B 37  ? 0.1391 0.1338 0.1906 -0.0054 -0.0173 0.0015  37  ASN   B CG  
4533 O OD1 . ASN   B 37  ? 0.1466 0.1388 0.2020 0.0057  -0.0158 0.0021  37  ASN   B OD1 
4534 N ND2 . ASN   B 37  ? 0.1489 0.1269 0.1864 -0.0003 -0.0235 0.0081  37  ASN   B ND2 
4541 N N   . ALA   B 38  ? 0.1453 0.1236 0.1882 0.0017  -0.0053 0.0079  38  ALA   B N   
4542 C CA  . ALA   B 38  ? 0.1541 0.1305 0.1898 -0.0059 -0.0069 0.0053  38  ALA   B CA  
4543 C C   . ALA   B 38  ? 0.1479 0.1237 0.1999 -0.0058 -0.0064 0.0082  38  ALA   B C   
4544 O O   . ALA   B 38  ? 0.1599 0.1354 0.1988 0.0048  -0.0075 0.0068  38  ALA   B O   
4545 C CB  . ALA   B 38  ? 0.1775 0.1341 0.1942 -0.0083 0.0050  -0.0046 38  ALA   B CB  
4551 N N   . ALA   B 39  ? 0.1482 0.1262 0.1919 0.0017  -0.0103 0.0079  39  ALA   B N   
4552 C CA  . ALA   B 39  ? 0.1638 0.1351 0.1797 0.0030  -0.0105 0.0082  39  ALA   B CA  
4553 C C   . ALA   B 39  ? 0.1676 0.1418 0.1669 0.0060  -0.0050 -0.0079 39  ALA   B C   
4554 O O   . ALA   B 39  ? 0.1715 0.1519 0.1946 -0.0022 -0.0080 0.0106  39  ALA   B O   
4555 C CB  . ALA   B 39  ? 0.1560 0.1403 0.1965 -0.0097 -0.0020 0.0069  39  ALA   B CB  
4561 N N   . ASN   B 40  ? 0.1691 0.1666 0.1599 -0.0061 0.0005  -0.0150 40  ASN   B N   
4562 C CA  . ASN   B 40  ? 0.1750 0.1703 0.1777 -0.0040 -0.0072 -0.0097 40  ASN   B CA  
4563 C C   . ASN   B 40  ? 0.1795 0.1730 0.1739 0.0023  -0.0163 -0.0063 40  ASN   B C   
4564 O O   . ASN   B 40  ? 0.1734 0.1639 0.1849 0.0028  -0.0140 -0.0048 40  ASN   B O   
4565 C CB  . ASN   B 40  ? 0.1884 0.1681 0.1978 0.0078  -0.0131 0.0111  40  ASN   B CB  
4566 C CG  . ASN   B 40  ? 0.1912 0.1755 0.2383 -0.0012 -0.0346 0.0147  40  ASN   B CG  
4567 O OD1 . ASN   B 40  ? 0.1915 0.1708 0.3171 -0.0008 -0.0375 0.0135  40  ASN   B OD1 
4568 N ND2 . ASN   B 40  ? 0.1938 0.1732 0.2424 -0.0002 -0.0357 0.0185  40  ASN   B ND2 
4575 N N   . VAL   B 41  ? 0.1873 0.1773 0.1772 0.0145  -0.0019 -0.0098 41  VAL   B N   
4576 C CA  . VAL   B 41  ? 0.1964 0.1874 0.1853 0.0083  0.0012  -0.0163 41  VAL   B CA  
4577 C C   . VAL   B 41  ? 0.1936 0.1883 0.1832 0.0129  -0.0086 -0.0197 41  VAL   B C   
4578 O O   . VAL   B 41  ? 0.1919 0.1866 0.2037 0.0110  -0.0122 -0.0205 41  VAL   B O   
4579 C CB  . VAL   B 41  ? 0.2111 0.2044 0.2063 -0.0034 0.0218  -0.0307 41  VAL   B CB  
4580 C CG1 . VAL   B 41  ? 0.2080 0.2070 0.2123 -0.0144 0.0335  -0.0344 41  VAL   B CG1 
4581 C CG2 . VAL   B 41  ? 0.2266 0.2254 0.2210 -0.0102 0.0127  -0.0216 41  VAL   B CG2 
4591 N N   . TYR   B 42  ? 0.1990 0.1921 0.1832 0.0105  -0.0276 0.0021  42  TYR   B N   
4592 C CA  . TYR   B 42  ? 0.2005 0.1979 0.1940 0.0176  -0.0346 -0.0105 42  TYR   B CA  
4593 C C   . TYR   B 42  ? 0.1855 0.1777 0.1998 0.0185  -0.0244 -0.0178 42  TYR   B C   
4594 O O   . TYR   B 42  ? 0.1842 0.1835 0.2332 0.0102  -0.0290 -0.0273 42  TYR   B O   
4595 C CB  . TYR   B 42  ? 0.2248 0.2264 0.2177 0.0162  -0.0345 0.0012  42  TYR   B CB  
4596 C CG  . TYR   B 42  ? 0.2324 0.2371 0.2134 0.0025  -0.0317 0.0034  42  TYR   B CG  
4597 C CD1 . TYR   B 42  ? 0.2330 0.2348 0.1924 -0.0023 -0.0154 0.0015  42  TYR   B CD1 
4598 C CD2 . TYR   B 42  ? 0.2552 0.2478 0.2368 0.0003  -0.0182 0.0133  42  TYR   B CD2 
4599 C CE1 . TYR   B 42  ? 0.2444 0.2500 0.2042 -0.0007 -0.0079 -0.0012 42  TYR   B CE1 
4600 C CE2 . TYR   B 42  ? 0.2611 0.2568 0.2347 0.0003  0.0118  0.0263  42  TYR   B CE2 
4601 C CZ  . TYR   B 42  ? 0.2686 0.2695 0.2339 0.0143  0.0198  0.0106  42  TYR   B CZ  
4602 O OH  . TYR   B 42  ? 0.3007 0.3015 0.2755 0.0341  0.0300  0.0277  42  TYR   B OH  
4612 N N   . LEU   B 43  ? 0.1757 0.1601 0.1879 0.0120  -0.0187 -0.0156 43  LEU   B N   
4613 C CA  . LEU   B 43  ? 0.1686 0.1578 0.1753 -0.0002 -0.0127 -0.0084 43  LEU   B CA  
4614 C C   . LEU   B 43  ? 0.1755 0.1587 0.1778 -0.0014 -0.0224 -0.0081 43  LEU   B C   
4615 O O   . LEU   B 43  ? 0.1725 0.1626 0.2050 0.0005  -0.0292 -0.0039 43  LEU   B O   
4616 C CB  . LEU   B 43  ? 0.1666 0.1503 0.1904 -0.0046 -0.0188 -0.0080 43  LEU   B CB  
4617 C CG  . LEU   B 43  ? 0.1770 0.1436 0.1972 0.0009  -0.0351 -0.0109 43  LEU   B CG  
4618 C CD1 . LEU   B 43  ? 0.1845 0.1465 0.2354 0.0003  -0.0419 -0.0156 43  LEU   B CD1 
4619 C CD2 . LEU   B 43  ? 0.1796 0.1435 0.2028 -0.0057 -0.0319 -0.0027 43  LEU   B CD2 
4631 N N   . LYS   B 44  ? 0.1750 0.1554 0.1929 0.0069  -0.0141 -0.0081 44  LYS   B N   
4632 C CA  . LYS   B 44  ? 0.1882 0.1653 0.1887 0.0023  -0.0234 0.0038  44  LYS   B CA  
4633 C C   . LYS   B 44  ? 0.1783 0.1605 0.1889 0.0057  -0.0262 0.0039  44  LYS   B C   
4634 O O   . LYS   B 44  ? 0.1996 0.1609 0.2153 -0.0046 -0.0205 -0.0014 44  LYS   B O   
4635 C CB  . LYS   B 44  ? 0.2230 0.1769 0.2100 0.0080  -0.0438 -0.0012 44  LYS   B CB  
4636 C CG  . LYS   B 44  ? 0.2666 0.2091 0.2384 0.0016  -0.0664 0.0031  44  LYS   B CG  
4637 C CD  . LYS   B 44  ? 0.3052 0.2345 0.2900 -0.0169 -0.0771 0.0035  44  LYS   B CD  
4638 C CE  . LYS   B 44  ? 0.3357 0.2617 0.3329 -0.0262 -0.0806 0.0123  44  LYS   B CE  
4639 N NZ  . LYS   B 44  ? 0.3481 0.2696 0.3576 -0.0262 -0.0884 0.0244  44  LYS   B NZ  
4653 N N   . HIS   B 45  ? 0.1700 0.1607 0.1948 -0.0007 -0.0250 0.0152  45  HIS   B N   
4654 C CA  . HIS   B 45  ? 0.1738 0.1576 0.1968 0.0070  -0.0167 0.0024  45  HIS   B CA  
4655 C C   . HIS   B 45  ? 0.2019 0.1804 0.2262 0.0158  -0.0253 -0.0017 45  HIS   B C   
4656 O O   . HIS   B 45  ? 0.2149 0.2024 0.2727 0.0451  -0.0105 -0.0029 45  HIS   B O   
4657 C CB  . HIS   B 45  ? 0.1636 0.1597 0.2001 0.0020  -0.0090 -0.0055 45  HIS   B CB  
4658 C CG  . HIS   B 45  ? 0.1658 0.1513 0.2063 -0.0048 -0.0174 -0.0009 45  HIS   B CG  
4659 N ND1 . HIS   B 45  ? 0.1651 0.1534 0.2052 -0.0044 -0.0226 -0.0085 45  HIS   B ND1 
4660 C CD2 . HIS   B 45  ? 0.1720 0.1576 0.2078 -0.0100 -0.0271 -0.0024 45  HIS   B CD2 
4661 C CE1 . HIS   B 45  ? 0.1760 0.1413 0.1937 -0.0061 -0.0339 -0.0096 45  HIS   B CE1 
4662 N NE2 . HIS   B 45  ? 0.1827 0.1494 0.1899 -0.0048 -0.0273 -0.0066 45  HIS   B NE2 
4670 N N   A GLY   B 46  ? 0.2133 0.1817 0.2461 0.0185  -0.0474 0.0057  46  GLY   B N   
4671 N N   B GLY   B 46  ? 0.2136 0.1885 0.2358 0.0173  -0.0400 0.0095  46  GLY   B N   
4672 C CA  A GLY   B 46  ? 0.2207 0.1945 0.2799 0.0190  -0.0586 0.0023  46  GLY   B CA  
4673 C CA  B GLY   B 46  ? 0.2214 0.2016 0.2565 0.0164  -0.0492 0.0125  46  GLY   B CA  
4674 C C   A GLY   B 46  ? 0.2195 0.2045 0.3140 0.0271  -0.0560 0.0040  46  GLY   B C   
4675 C C   B GLY   B 46  ? 0.2218 0.2110 0.2805 0.0201  -0.0476 0.0170  46  GLY   B C   
4676 O O   A GLY   B 46  ? 0.2284 0.2134 0.3918 0.0348  -0.0361 -0.0194 46  GLY   B O   
4677 O O   B GLY   B 46  ? 0.2300 0.2214 0.3097 0.0239  -0.0363 0.0216  46  GLY   B O   
4684 N N   . GLY   B 47  ? 0.2164 0.2118 0.2890 0.0088  -0.0383 0.0070  47  GLY   B N   
4685 C CA  . GLY   B 47  ? 0.2038 0.1849 0.2629 0.0015  -0.0282 0.0067  47  GLY   B CA  
4686 C C   . GLY   B 47  ? 0.1825 0.1606 0.2348 -0.0021 -0.0098 0.0137  47  GLY   B C   
4687 O O   . GLY   B 47  ? 0.1868 0.1454 0.2409 0.0041  -0.0177 0.0156  47  GLY   B O   
4692 N N   . GLY   B 48  ? 0.1622 0.1551 0.2396 -0.0025 -0.0200 0.0199  48  GLY   B N   
4693 C CA  . GLY   B 48  ? 0.1627 0.1455 0.2382 -0.0090 -0.0157 0.0121  48  GLY   B CA  
4694 C C   . GLY   B 48  ? 0.1548 0.1410 0.2276 0.0013  -0.0046 0.0055  48  GLY   B C   
4695 O O   . GLY   B 48  ? 0.1480 0.1492 0.2485 0.0042  -0.0159 0.0017  48  GLY   B O   
4699 N N   . VAL   B 49  ? 0.1560 0.1497 0.2135 0.0096  -0.0040 0.0078  49  VAL   B N   
4700 C CA  . VAL   B 49  ? 0.1606 0.1545 0.2082 0.0078  -0.0187 -0.0016 49  VAL   B CA  
4701 C C   . VAL   B 49  ? 0.1520 0.1477 0.1925 0.0099  -0.0104 0.0003  49  VAL   B C   
4702 O O   . VAL   B 49  ? 0.1559 0.1505 0.2015 -0.0001 -0.0040 0.0054  49  VAL   B O   
4703 C CB  . VAL   B 49  ? 0.1629 0.1735 0.2242 0.0007  -0.0329 0.0027  49  VAL   B CB  
4704 C CG1 . VAL   B 49  ? 0.1652 0.1820 0.2246 0.0076  -0.0360 0.0050  49  VAL   B CG1 
4705 C CG2 . VAL   B 49  ? 0.1819 0.1865 0.2478 -0.0145 -0.0409 -0.0007 49  VAL   B CG2 
4715 N N   . ALA   B 50  ? 0.1456 0.1429 0.1948 0.0038  -0.0070 0.0036  50  ALA   B N   
4716 C CA  . ALA   B 50  ? 0.1479 0.1361 0.1971 0.0056  -0.0061 0.0055  50  ALA   B CA  
4717 C C   . ALA   B 50  ? 0.1577 0.1401 0.1983 0.0031  -0.0085 0.0032  50  ALA   B C   
4718 O O   . ALA   B 50  ? 0.1533 0.1435 0.1871 -0.0006 -0.0110 0.0044  50  ALA   B O   
4719 C CB  . ALA   B 50  ? 0.1505 0.1407 0.2019 0.0009  -0.0036 0.0133  50  ALA   B CB  
4725 N N   . GLY   B 51  ? 0.1468 0.1555 0.2013 0.0100  -0.0201 0.0061  51  GLY   B N   
4726 C CA  . GLY   B 51  ? 0.1514 0.1634 0.2238 0.0165  -0.0261 0.0086  51  GLY   B CA  
4727 C C   . GLY   B 51  ? 0.1489 0.1543 0.2239 0.0164  -0.0140 0.0117  51  GLY   B C   
4728 O O   . GLY   B 51  ? 0.1524 0.1609 0.2473 0.0049  -0.0164 0.0063  51  GLY   B O   
4732 N N   . ALA   B 52  ? 0.1490 0.1439 0.2085 0.0169  -0.0118 0.0140  52  ALA   B N   
4733 C CA  . ALA   B 52  ? 0.1546 0.1509 0.2111 0.0090  0.0030  0.0063  52  ALA   B CA  
4734 C C   . ALA   B 52  ? 0.1442 0.1532 0.1988 0.0013  -0.0062 0.0027  52  ALA   B C   
4735 O O   . ALA   B 52  ? 0.1470 0.1549 0.2165 0.0074  -0.0079 0.0028  52  ALA   B O   
4736 C CB  . ALA   B 52  ? 0.1779 0.1500 0.2139 0.0012  0.0027  -0.0020 52  ALA   B CB  
4742 N N   . LEU   B 53  ? 0.1374 0.1437 0.1963 0.0118  -0.0028 0.0030  53  LEU   B N   
4743 C CA  . LEU   B 53  ? 0.1410 0.1512 0.1825 0.0101  -0.0060 -0.0019 53  LEU   B CA  
4744 C C   . LEU   B 53  ? 0.1471 0.1480 0.1709 0.0117  -0.0068 0.0028  53  LEU   B C   
4745 O O   . LEU   B 53  ? 0.1561 0.1539 0.1932 0.0003  0.0020  0.0119  53  LEU   B O   
4746 C CB  . LEU   B 53  ? 0.1426 0.1599 0.2052 0.0084  -0.0084 0.0087  53  LEU   B CB  
4747 C CG  . LEU   B 53  ? 0.1431 0.1737 0.2099 0.0036  -0.0052 0.0161  53  LEU   B CG  
4748 C CD1 . LEU   B 53  ? 0.1473 0.1931 0.2300 0.0170  -0.0019 0.0086  53  LEU   B CD1 
4749 C CD2 . LEU   B 53  ? 0.1585 0.1973 0.2308 -0.0073 -0.0210 -0.0113 53  LEU   B CD2 
4761 N N   . ASN   B 54  ? 0.1512 0.1367 0.1716 0.0017  -0.0130 0.0008  54  ASN   B N   
4762 C CA  . ASN   B 54  ? 0.1523 0.1505 0.1893 0.0017  -0.0189 -0.0043 54  ASN   B CA  
4763 C C   . ASN   B 54  ? 0.1457 0.1484 0.2289 -0.0030 -0.0108 0.0023  54  ASN   B C   
4764 O O   . ASN   B 54  ? 0.1480 0.1577 0.2296 -0.0036 -0.0048 0.0047  54  ASN   B O   
4765 C CB  . ASN   B 54  ? 0.1552 0.1654 0.2029 0.0025  -0.0156 -0.0022 54  ASN   B CB  
4766 C CG  . ASN   B 54  ? 0.1546 0.1703 0.2111 0.0036  -0.0190 0.0033  54  ASN   B CG  
4767 O OD1 . ASN   B 54  ? 0.1557 0.1643 0.2361 0.0034  -0.0211 -0.0087 54  ASN   B OD1 
4768 N ND2 . ASN   B 54  ? 0.1706 0.1952 0.2372 -0.0036 -0.0364 0.0098  54  ASN   B ND2 
4775 N N   . LYS   B 55  ? 0.1464 0.1534 0.2454 0.0073  -0.0076 -0.0029 55  LYS   B N   
4776 C CA  . LYS   B 55  ? 0.1497 0.1666 0.2631 0.0160  0.0007  0.0064  55  LYS   B CA  
4777 C C   . LYS   B 55  ? 0.1465 0.1722 0.2524 0.0133  0.0072  -0.0017 55  LYS   B C   
4778 O O   . LYS   B 55  ? 0.1432 0.1876 0.2637 0.0103  0.0042  -0.0040 55  LYS   B O   
4779 C CB  . LYS   B 55  ? 0.1628 0.1857 0.3074 0.0245  0.0039  0.0072  55  LYS   B CB  
4780 C CG  . LYS   B 55  ? 0.2090 0.2118 0.3700 0.0327  0.0208  0.0168  55  LYS   B CG  
4781 C CD  . LYS   B 55  ? 0.2511 0.2366 0.4253 0.0423  0.0434  0.0238  55  LYS   B CD  
4782 C CE  . LYS   B 55  ? 0.2866 0.2623 0.4804 0.0417  0.0611  0.0212  55  LYS   B CE  
4783 N NZ  . LYS   B 55  ? 0.2993 0.2810 0.5127 0.0381  0.0556  0.0290  55  LYS   B NZ  
4797 N N   . ALA   B 56  ? 0.1434 0.1714 0.2368 0.0065  -0.0018 -0.0013 56  ALA   B N   
4798 C CA  . ALA   B 56  ? 0.1588 0.1934 0.2328 0.0009  0.0010  -0.0020 56  ALA   B CA  
4799 C C   . ALA   B 56  ? 0.1613 0.1893 0.2256 0.0007  0.0095  0.0032  56  ALA   B C   
4800 O O   . ALA   B 56  ? 0.1735 0.1949 0.2408 0.0073  0.0286  0.0081  56  ALA   B O   
4801 C CB  . ALA   B 56  ? 0.1710 0.2175 0.2204 -0.0128 -0.0085 -0.0005 56  ALA   B CB  
4807 N N   . THR   B 57  ? 0.1528 0.1769 0.2348 -0.0022 0.0185  0.0056  57  THR   B N   
4808 C CA  . THR   B 57  ? 0.1587 0.1783 0.2352 -0.0020 0.0117  0.0113  57  THR   B CA  
4809 C C   . THR   B 57  ? 0.1548 0.1877 0.2554 -0.0023 0.0172  0.0092  57  THR   B C   
4810 O O   . THR   B 57  ? 0.1649 0.1898 0.2683 -0.0212 0.0110  0.0031  57  THR   B O   
4811 C CB  . THR   B 57  ? 0.1657 0.1602 0.2174 -0.0009 0.0088  0.0150  57  THR   B CB  
4812 O OG1 . THR   B 57  ? 0.1641 0.1540 0.2438 -0.0043 0.0063  0.0069  57  THR   B OG1 
4813 C CG2 . THR   B 57  ? 0.1718 0.1621 0.2190 -0.0051 0.0056  0.0084  57  THR   B CG2 
4821 N N   . ASN   B 58  ? 0.1408 0.2091 0.2800 -0.0149 0.0073  -0.0012 58  ASN   B N   
4822 C CA  . ASN   B 58  ? 0.1579 0.2464 0.3207 -0.0242 0.0271  0.0056  58  ASN   B CA  
4823 C C   . ASN   B 58  ? 0.1501 0.2246 0.2828 -0.0170 -0.0112 0.0026  58  ASN   B C   
4824 O O   . ASN   B 58  ? 0.1621 0.2324 0.2932 -0.0218 -0.0097 -0.0084 58  ASN   B O   
4825 C CB  . ASN   B 58  ? 0.2241 0.3022 0.4158 -0.0372 0.0631  0.0194  58  ASN   B CB  
4826 C CG  . ASN   B 58  ? 0.3456 0.3651 0.5370 -0.0399 0.0751  0.0473  58  ASN   B CG  
4827 O OD1 . ASN   B 58  ? 0.3742 0.3799 0.5822 -0.0400 0.0733  0.0570  58  ASN   B OD1 
4828 N ND2 . ASN   B 58  ? 0.4324 0.4324 0.5794 -0.0417 0.0824  0.0556  58  ASN   B ND2 
4835 N N   . ASN   B 59  ? 0.1497 0.2048 0.2737 -0.0153 -0.0093 0.0054  59  ASN   B N   
4836 C CA  . ASN   B 59  ? 0.1553 0.2038 0.2477 -0.0131 -0.0229 0.0076  59  ASN   B CA  
4837 C C   . ASN   B 59  ? 0.1527 0.1935 0.2457 -0.0170 -0.0182 -0.0017 59  ASN   B C   
4838 O O   . ASN   B 59  ? 0.1579 0.1971 0.2420 -0.0210 -0.0196 -0.0042 59  ASN   B O   
4839 C CB  . ASN   B 59  ? 0.1646 0.2219 0.2556 -0.0104 -0.0304 0.0067  59  ASN   B CB  
4840 C CG  . ASN   B 59  ? 0.1757 0.2372 0.2668 -0.0124 -0.0370 0.0028  59  ASN   B CG  
4841 O OD1 . ASN   B 59  ? 0.1715 0.2472 0.2776 -0.0103 -0.0285 0.0197  59  ASN   B OD1 
4842 N ND2 . ASN   B 59  ? 0.1879 0.2468 0.2780 -0.0169 -0.0429 -0.0028 59  ASN   B ND2 
4849 N N   . ALA   B 60  ? 0.1543 0.1847 0.2376 -0.0121 -0.0137 0.0019  60  ALA   B N   
4850 C CA  . ALA   B 60  ? 0.1620 0.1723 0.2369 -0.0183 -0.0113 0.0031  60  ALA   B CA  
4851 C C   . ALA   B 60  ? 0.1616 0.1569 0.2253 -0.0158 -0.0144 0.0084  60  ALA   B C   
4852 O O   . ALA   B 60  ? 0.1634 0.1644 0.2294 -0.0196 -0.0079 -0.0013 60  ALA   B O   
4853 C CB  . ALA   B 60  ? 0.1749 0.1730 0.2649 -0.0184 0.0038  0.0010  60  ALA   B CB  
4859 N N   . MET   B 61  ? 0.1561 0.1524 0.2209 -0.0118 -0.0058 0.0030  61  MET   B N   
4860 C CA  . MET   B 61  ? 0.1504 0.1498 0.2116 -0.0075 -0.0206 0.0034  61  MET   B CA  
4861 C C   . MET   B 61  ? 0.1558 0.1468 0.2201 -0.0127 -0.0194 0.0010  61  MET   B C   
4862 O O   . MET   B 61  ? 0.1543 0.1482 0.2109 -0.0057 -0.0150 -0.0126 61  MET   B O   
4863 C CB  . MET   B 61  ? 0.1463 0.1594 0.2167 -0.0032 -0.0190 -0.0006 61  MET   B CB  
4864 C CG  . MET   B 61  ? 0.1452 0.1554 0.2131 -0.0047 -0.0096 0.0053  61  MET   B CG  
4865 S SD  . MET   B 61  ? 0.1499 0.1494 0.2220 -0.0075 -0.0112 -0.0087 61  MET   B SD  
4866 C CE  . MET   B 61  ? 0.1584 0.1733 0.2537 -0.0076 -0.0063 -0.0228 61  MET   B CE  
4876 N N   . GLN   B 62  ? 0.1554 0.1580 0.2072 -0.0121 -0.0253 0.0016  62  GLN   B N   
4877 C CA  . GLN   B 62  ? 0.1606 0.1571 0.2158 -0.0064 -0.0291 -0.0025 62  GLN   B CA  
4878 C C   . GLN   B 62  ? 0.1576 0.1691 0.2240 -0.0089 -0.0337 -0.0066 62  GLN   B C   
4879 O O   . GLN   B 62  ? 0.1709 0.1666 0.2220 -0.0049 -0.0323 -0.0185 62  GLN   B O   
4880 C CB  . GLN   B 62  ? 0.1646 0.1628 0.2173 -0.0022 -0.0226 0.0060  62  GLN   B CB  
4881 C CG  . GLN   B 62  ? 0.1669 0.1640 0.2215 -0.0001 -0.0329 -0.0021 62  GLN   B CG  
4882 C CD  . GLN   B 62  ? 0.1694 0.1658 0.2220 0.0029  -0.0364 0.0023  62  GLN   B CD  
4883 O OE1 . GLN   B 62  ? 0.1706 0.1595 0.2291 -0.0039 -0.0432 -0.0078 62  GLN   B OE1 
4884 N NE2 . GLN   B 62  ? 0.1733 0.1718 0.2225 0.0055  -0.0285 -0.0108 62  GLN   B NE2 
4893 N N   . VAL   B 63  ? 0.1595 0.1694 0.2400 -0.0148 -0.0312 -0.0193 63  VAL   B N   
4894 C CA  . VAL   B 63  ? 0.1735 0.1722 0.2555 -0.0186 -0.0360 -0.0118 63  VAL   B CA  
4895 C C   . VAL   B 63  ? 0.1724 0.1604 0.2395 -0.0218 -0.0367 -0.0152 63  VAL   B C   
4896 O O   . VAL   B 63  ? 0.1833 0.1649 0.2435 -0.0223 -0.0523 -0.0184 63  VAL   B O   
4897 C CB  . VAL   B 63  ? 0.1677 0.1925 0.2827 -0.0235 -0.0354 -0.0154 63  VAL   B CB  
4898 C CG1 . VAL   B 63  ? 0.1729 0.1898 0.2939 -0.0316 -0.0221 -0.0153 63  VAL   B CG1 
4899 C CG2 . VAL   B 63  ? 0.1636 0.2157 0.2920 -0.0150 -0.0322 -0.0201 63  VAL   B CG2 
4909 N N   . GLU   B 64  ? 0.1662 0.1527 0.2368 -0.0148 -0.0273 -0.0132 64  GLU   B N   
4910 C CA  . GLU   B 64  ? 0.1715 0.1449 0.2254 -0.0168 -0.0393 -0.0084 64  GLU   B CA  
4911 C C   . GLU   B 64  ? 0.1614 0.1480 0.2149 -0.0059 -0.0357 -0.0151 64  GLU   B C   
4912 O O   . GLU   B 64  ? 0.1728 0.1598 0.2094 -0.0130 -0.0284 -0.0189 64  GLU   B O   
4913 C CB  . GLU   B 64  ? 0.1748 0.1534 0.2253 -0.0167 -0.0361 -0.0059 64  GLU   B CB  
4914 C CG  . GLU   B 64  ? 0.1811 0.1589 0.2251 -0.0243 -0.0431 -0.0096 64  GLU   B CG  
4915 C CD  . GLU   B 64  ? 0.1831 0.1695 0.2392 -0.0327 -0.0382 -0.0059 64  GLU   B CD  
4916 O OE1 . GLU   B 64  ? 0.1861 0.1818 0.2523 -0.0338 -0.0309 -0.0244 64  GLU   B OE1 
4917 O OE2 . GLU   B 64  ? 0.1941 0.1819 0.2397 -0.0380 -0.0532 -0.0107 64  GLU   B OE2 
4924 N N   . SER   B 65  ? 0.1603 0.1448 0.2000 -0.0114 -0.0226 -0.0182 65  SER   B N   
4925 C CA  . SER   B 65  ? 0.1638 0.1486 0.2139 -0.0029 -0.0241 -0.0253 65  SER   B CA  
4926 C C   . SER   B 65  ? 0.1684 0.1506 0.2098 -0.0048 -0.0322 -0.0273 65  SER   B C   
4927 O O   . SER   B 65  ? 0.1697 0.1581 0.2072 -0.0030 -0.0288 -0.0235 65  SER   B O   
4928 C CB  . SER   B 65  ? 0.1662 0.1498 0.2134 -0.0112 -0.0207 -0.0187 65  SER   B CB  
4929 O OG  . SER   B 65  ? 0.1642 0.1489 0.2122 -0.0094 -0.0133 -0.0253 65  SER   B OG  
4935 N N   . ASP   B 66  ? 0.1767 0.1577 0.2102 -0.0064 -0.0395 -0.0248 66  ASP   B N   
4936 C CA  . ASP   B 66  ? 0.1861 0.1635 0.2066 0.0021  -0.0365 -0.0185 66  ASP   B CA  
4937 C C   . ASP   B 66  ? 0.1894 0.1652 0.2050 -0.0055 -0.0288 -0.0222 66  ASP   B C   
4938 O O   . ASP   B 66  ? 0.1898 0.1756 0.2082 0.0043  -0.0227 -0.0231 66  ASP   B O   
4939 C CB  . ASP   B 66  ? 0.2020 0.1762 0.2213 0.0068  -0.0529 -0.0063 66  ASP   B CB  
4940 C CG  . ASP   B 66  ? 0.2264 0.1929 0.2481 0.0184  -0.0542 0.0006  66  ASP   B CG  
4941 O OD1 . ASP   B 66  ? 0.2559 0.1920 0.2567 0.0049  -0.0662 0.0072  66  ASP   B OD1 
4942 O OD2 . ASP   B 66  ? 0.2432 0.2156 0.2942 0.0332  -0.0526 -0.0039 66  ASP   B OD2 
4947 N N   . ASP   B 67  ? 0.1879 0.1577 0.2123 -0.0145 -0.0329 -0.0228 67  ASP   B N   
4948 C CA  . ASP   B 67  ? 0.2005 0.1573 0.2251 -0.0104 -0.0352 -0.0139 67  ASP   B CA  
4949 C C   . ASP   B 67  ? 0.1945 0.1590 0.2249 -0.0016 -0.0372 -0.0185 67  ASP   B C   
4950 O O   . ASP   B 67  ? 0.1948 0.1701 0.2319 -0.0022 -0.0328 -0.0223 67  ASP   B O   
4951 C CB  . ASP   B 67  ? 0.2217 0.1641 0.2472 -0.0148 -0.0447 -0.0114 67  ASP   B CB  
4952 C CG  . ASP   B 67  ? 0.2605 0.1720 0.2646 -0.0140 -0.0716 -0.0099 67  ASP   B CG  
4953 O OD1 . ASP   B 67  ? 0.2854 0.1715 0.2767 -0.0143 -0.0785 -0.0054 67  ASP   B OD1 
4954 O OD2 . ASP   B 67  ? 0.2765 0.1844 0.2768 0.0024  -0.0772 -0.0076 67  ASP   B OD2 
4959 N N   . TYR   B 68  ? 0.1854 0.1602 0.2286 -0.0024 -0.0461 -0.0304 68  TYR   B N   
4960 C CA  . TYR   B 68  ? 0.1864 0.1800 0.2392 0.0079  -0.0468 -0.0421 68  TYR   B CA  
4961 C C   . TYR   B 68  ? 0.1792 0.1759 0.2326 0.0082  -0.0399 -0.0480 68  TYR   B C   
4962 O O   . TYR   B 68  ? 0.1929 0.1878 0.2410 0.0103  -0.0413 -0.0653 68  TYR   B O   
4963 C CB  . TYR   B 68  ? 0.1914 0.2097 0.2364 0.0105  -0.0552 -0.0558 68  TYR   B CB  
4964 C CG  . TYR   B 68  ? 0.2019 0.2330 0.2517 0.0156  -0.0438 -0.0751 68  TYR   B CG  
4965 C CD1 . TYR   B 68  ? 0.2020 0.2390 0.2779 -0.0033 -0.0443 -0.0908 68  TYR   B CD1 
4966 C CD2 . TYR   B 68  ? 0.1983 0.2543 0.2623 0.0185  -0.0582 -0.0742 68  TYR   B CD2 
4967 C CE1 . TYR   B 68  ? 0.2062 0.2592 0.2991 0.0006  -0.0373 -0.0915 68  TYR   B CE1 
4968 C CE2 . TYR   B 68  ? 0.2007 0.2632 0.2811 0.0146  -0.0475 -0.0896 68  TYR   B CE2 
4969 C CZ  . TYR   B 68  ? 0.1987 0.2680 0.2973 0.0048  -0.0424 -0.0916 68  TYR   B CZ  
4970 O OH  . TYR   B 68  ? 0.1982 0.2861 0.3422 -0.0020 -0.0301 -0.0705 68  TYR   B OH  
4980 N N   . ILE   B 69  ? 0.1783 0.1657 0.2371 0.0040  -0.0292 -0.0461 69  ILE   B N   
4981 C CA  . ILE   B 69  ? 0.1908 0.1727 0.2436 -0.0037 -0.0268 -0.0504 69  ILE   B CA  
4982 C C   . ILE   B 69  ? 0.1899 0.1690 0.2413 0.0068  -0.0359 -0.0344 69  ILE   B C   
4983 O O   . ILE   B 69  ? 0.1948 0.1803 0.2359 0.0077  -0.0265 -0.0370 69  ILE   B O   
4984 C CB  . ILE   B 69  ? 0.1970 0.1796 0.2624 -0.0077 0.0008  -0.0396 69  ILE   B CB  
4985 C CG1 . ILE   B 69  ? 0.2003 0.1809 0.2745 -0.0123 0.0079  -0.0398 69  ILE   B CG1 
4986 C CG2 . ILE   B 69  ? 0.2140 0.1945 0.2742 -0.0058 0.0033  -0.0291 69  ILE   B CG2 
4987 C CD1 . ILE   B 69  ? 0.1983 0.1867 0.2888 -0.0253 0.0146  -0.0463 69  ILE   B CD1 
4999 N N   . ALA   B 70  ? 0.1875 0.1655 0.2363 0.0079  -0.0358 -0.0309 70  ALA   B N   
5000 C CA  . ALA   B 70  ? 0.1912 0.1670 0.2143 0.0053  -0.0436 -0.0309 70  ALA   B CA  
5001 C C   . ALA   B 70  ? 0.1917 0.1660 0.2266 -0.0009 -0.0549 -0.0371 70  ALA   B C   
5002 O O   . ALA   B 70  ? 0.2033 0.1690 0.2263 0.0050  -0.0510 -0.0347 70  ALA   B O   
5003 C CB  . ALA   B 70  ? 0.1925 0.1850 0.2074 -0.0012 -0.0423 -0.0176 70  ALA   B CB  
5009 N N   . THR   B 71  ? 0.1977 0.1671 0.2421 0.0073  -0.0657 -0.0367 71  THR   B N   
5010 C CA  . THR   B 71  ? 0.2086 0.1783 0.2570 0.0133  -0.0659 -0.0413 71  THR   B CA  
5011 C C   . THR   B 71  ? 0.2058 0.1854 0.2805 0.0267  -0.0679 -0.0515 71  THR   B C   
5012 O O   . THR   B 71  ? 0.2169 0.1935 0.3018 0.0338  -0.0683 -0.0640 71  THR   B O   
5013 C CB  . THR   B 71  ? 0.2307 0.2001 0.2690 0.0090  -0.0771 -0.0254 71  THR   B CB  
5014 O OG1 . THR   B 71  ? 0.2449 0.2210 0.3001 -0.0111 -0.0787 -0.0087 71  THR   B OG1 
5015 C CG2 . THR   B 71  ? 0.2518 0.1946 0.2840 0.0156  -0.0642 -0.0146 71  THR   B CG2 
5023 N N   . ASN   B 72  ? 0.1989 0.1904 0.2678 0.0127  -0.0702 -0.0721 72  ASN   B N   
5024 C CA  . ASN   B 72  ? 0.1993 0.2069 0.2606 0.0133  -0.0538 -0.0788 72  ASN   B CA  
5025 C C   . ASN   B 72  ? 0.1978 0.2166 0.2734 -0.0004 -0.0327 -0.0779 72  ASN   B C   
5026 O O   . ASN   B 72  ? 0.1999 0.2282 0.3051 0.0071  -0.0187 -0.0856 72  ASN   B O   
5027 C CB  . ASN   B 72  ? 0.2026 0.2197 0.2716 0.0168  -0.0640 -0.0680 72  ASN   B CB  
5028 C CG  . ASN   B 72  ? 0.2177 0.2351 0.2798 0.0326  -0.0554 -0.0431 72  ASN   B CG  
5029 O OD1 . ASN   B 72  ? 0.2373 0.2519 0.2868 0.0224  -0.0400 -0.0464 72  ASN   B OD1 
5030 N ND2 . ASN   B 72  ? 0.2306 0.2423 0.3068 0.0458  -0.0528 -0.0145 72  ASN   B ND2 
5037 N N   . GLY   B 73  ? 0.2042 0.2186 0.2585 -0.0076 -0.0348 -0.0804 73  GLY   B N   
5038 C CA  . GLY   B 73  ? 0.2011 0.2216 0.2280 -0.0072 -0.0214 -0.0640 73  GLY   B CA  
5039 C C   . GLY   B 73  ? 0.1925 0.2181 0.2002 0.0014  -0.0222 -0.0567 73  GLY   B C   
5040 O O   . GLY   B 73  ? 0.1825 0.2061 0.2113 0.0014  -0.0242 -0.0474 73  GLY   B O   
5044 N N   . PRO   B 74  ? 0.1973 0.2334 0.1869 0.0011  -0.0285 -0.0440 74  PRO   B N   
5045 C CA  . PRO   B 74  ? 0.1895 0.2272 0.1826 0.0022  -0.0243 -0.0321 74  PRO   B CA  
5046 C C   . PRO   B 74  ? 0.1758 0.2144 0.1974 0.0033  -0.0251 -0.0290 74  PRO   B C   
5047 O O   . PRO   B 74  ? 0.1753 0.2087 0.2289 0.0010  -0.0116 -0.0412 74  PRO   B O   
5048 C CB  . PRO   B 74  ? 0.2018 0.2412 0.2006 0.0031  -0.0210 -0.0272 74  PRO   B CB  
5049 C CG  . PRO   B 74  ? 0.2199 0.2540 0.2180 0.0049  -0.0170 -0.0212 74  PRO   B CG  
5050 C CD  . PRO   B 74  ? 0.2209 0.2460 0.2055 0.0085  -0.0161 -0.0352 74  PRO   B CD  
5058 N N   . LEU   B 75  ? 0.1725 0.2035 0.1770 0.0015  -0.0293 -0.0224 75  LEU   B N   
5059 C CA  . LEU   B 75  ? 0.1748 0.2017 0.1600 -0.0021 -0.0207 -0.0076 75  LEU   B CA  
5060 C C   . LEU   B 75  ? 0.1771 0.2107 0.1578 0.0016  -0.0057 -0.0054 75  LEU   B C   
5061 O O   . LEU   B 75  ? 0.1945 0.2205 0.1756 -0.0034 -0.0072 -0.0068 75  LEU   B O   
5062 C CB  . LEU   B 75  ? 0.1833 0.2019 0.1521 -0.0125 -0.0248 0.0081  75  LEU   B CB  
5063 C CG  . LEU   B 75  ? 0.2124 0.2122 0.1831 -0.0303 -0.0142 0.0057  75  LEU   B CG  
5064 C CD1 . LEU   B 75  ? 0.2370 0.2214 0.1836 -0.0419 0.0064  -0.0006 75  LEU   B CD1 
5065 C CD2 . LEU   B 75  ? 0.2500 0.2329 0.2375 -0.0226 -0.0078 0.0102  75  LEU   B CD2 
5077 N N   . LYS   B 76  ? 0.1750 0.2281 0.1902 -0.0003 0.0070  0.0012  76  LYS   B N   
5078 C CA  . LYS   B 76  ? 0.1906 0.2325 0.2287 -0.0170 0.0214  0.0039  76  LYS   B CA  
5079 C C   . LYS   B 76  ? 0.1768 0.2149 0.2038 -0.0083 0.0118  0.0152  76  LYS   B C   
5080 O O   . LYS   B 76  ? 0.1765 0.1984 0.2074 -0.0066 0.0006  0.0170  76  LYS   B O   
5081 C CB  . LYS   B 76  ? 0.2104 0.2404 0.2818 -0.0264 0.0359  -0.0211 76  LYS   B CB  
5082 C CG  . LYS   B 76  ? 0.2202 0.2615 0.3186 -0.0111 0.0266  -0.0308 76  LYS   B CG  
5083 C CD  . LYS   B 76  ? 0.2234 0.2756 0.3501 -0.0057 0.0211  -0.0446 76  LYS   B CD  
5084 C CE  . LYS   B 76  ? 0.2369 0.2976 0.3889 -0.0011 0.0027  -0.0492 76  LYS   B CE  
5085 N NZ  . LYS   B 76  ? 0.2362 0.3086 0.4103 -0.0057 -0.0207 -0.0662 76  LYS   B NZ  
5099 N N   . VAL   B 77  ? 0.1913 0.2227 0.2157 -0.0017 0.0063  0.0192  77  VAL   B N   
5100 C CA  . VAL   B 77  ? 0.1905 0.2138 0.2247 0.0083  0.0112  0.0470  77  VAL   B CA  
5101 C C   . VAL   B 77  ? 0.1768 0.1927 0.2157 0.0110  0.0269  0.0416  77  VAL   B C   
5102 O O   . VAL   B 77  ? 0.1834 0.1938 0.2115 0.0186  0.0274  0.0347  77  VAL   B O   
5103 C CB  . VAL   B 77  ? 0.1975 0.2236 0.2498 0.0170  0.0306  0.0581  77  VAL   B CB  
5104 C CG1 . VAL   B 77  ? 0.2004 0.2114 0.2745 0.0108  0.0272  0.0758  77  VAL   B CG1 
5105 C CG2 . VAL   B 77  ? 0.2135 0.2445 0.2745 0.0129  0.0135  0.0581  77  VAL   B CG2 
5115 N N   . GLY   B 78  ? 0.1692 0.1741 0.2034 0.0100  0.0223  0.0247  78  GLY   B N   
5116 C CA  . GLY   B 78  ? 0.1635 0.1731 0.1911 0.0131  0.0234  0.0129  78  GLY   B CA  
5117 C C   . GLY   B 78  ? 0.1595 0.1649 0.1998 0.0081  0.0214  0.0164  78  GLY   B C   
5118 O O   . GLY   B 78  ? 0.1594 0.1683 0.2284 0.0128  0.0090  0.0264  78  GLY   B O   
5122 N N   . GLY   B 79  ? 0.1549 0.1671 0.2023 0.0026  0.0239  0.0084  79  GLY   B N   
5123 C CA  . GLY   B 79  ? 0.1620 0.1570 0.2079 0.0038  0.0137  0.0107  79  GLY   B CA  
5124 C C   . GLY   B 79  ? 0.1520 0.1545 0.2056 0.0095  0.0143  0.0037  79  GLY   B C   
5125 O O   . GLY   B 79  ? 0.1578 0.1492 0.2150 0.0087  0.0166  0.0162  79  GLY   B O   
5129 N N   . SER   B 80  ? 0.1495 0.1506 0.2117 0.0020  0.0117  0.0035  80  SER   B N   
5130 C CA  . SER   B 80  ? 0.1417 0.1431 0.2114 -0.0038 -0.0052 0.0052  80  SER   B CA  
5131 C C   . SER   B 80  ? 0.1459 0.1423 0.2059 0.0073  -0.0083 -0.0017 80  SER   B C   
5132 O O   . SER   B 80  ? 0.1564 0.1430 0.2428 0.0050  -0.0059 -0.0022 80  SER   B O   
5133 C CB  . SER   B 80  ? 0.1433 0.1491 0.2156 -0.0099 -0.0071 0.0047  80  SER   B CB  
5134 O OG  . SER   B 80  ? 0.1514 0.1656 0.2291 -0.0030 -0.0155 0.0070  80  SER   B OG  
5140 N N   . CYS   B 81  ? 0.1436 0.1301 0.2099 0.0005  -0.0084 -0.0068 81  CYS   B N   
5141 C CA  . CYS   B 81  ? 0.1487 0.1231 0.2093 0.0045  -0.0116 -0.0076 81  CYS   B CA  
5142 C C   . CYS   B 81  ? 0.1460 0.1259 0.2007 0.0011  -0.0102 -0.0092 81  CYS   B C   
5143 O O   . CYS   B 81  ? 0.1646 0.1291 0.2088 0.0007  -0.0008 -0.0008 81  CYS   B O   
5144 C CB  . CYS   B 81  ? 0.1701 0.1398 0.2069 -0.0016 -0.0210 -0.0067 81  CYS   B CB  
5145 S SG  . CYS   B 81  ? 0.1685 0.1602 0.2070 -0.0050 -0.0263 -0.0131 81  CYS   B SG  
5151 N N   . VAL   B 82  ? 0.1511 0.1244 0.1953 -0.0016 -0.0116 -0.0048 82  VAL   B N   
5152 C CA  . VAL   B 82  ? 0.1543 0.1275 0.1993 -0.0087 -0.0144 -0.0045 82  VAL   B CA  
5153 C C   . VAL   B 82  ? 0.1612 0.1279 0.2077 -0.0078 -0.0059 -0.0030 82  VAL   B C   
5154 O O   . VAL   B 82  ? 0.1706 0.1242 0.2298 -0.0097 -0.0142 -0.0140 82  VAL   B O   
5155 C CB  . VAL   B 82  ? 0.1641 0.1481 0.2117 -0.0030 -0.0140 0.0033  82  VAL   B CB  
5156 C CG1 . VAL   B 82  ? 0.1835 0.1736 0.2212 0.0061  -0.0103 0.0129  82  VAL   B CG1 
5157 C CG2 . VAL   B 82  ? 0.1744 0.1618 0.2303 -0.0137 -0.0315 0.0051  82  VAL   B CG2 
5167 N N   . LEU   B 83  ? 0.1484 0.1254 0.2063 -0.0161 -0.0191 -0.0139 83  LEU   B N   
5168 C CA  . LEU   B 83  ? 0.1504 0.1277 0.2108 -0.0115 -0.0190 -0.0051 83  LEU   B CA  
5169 C C   . LEU   B 83  ? 0.1533 0.1216 0.2089 -0.0203 -0.0218 -0.0053 83  LEU   B C   
5170 O O   . LEU   B 83  ? 0.1531 0.1351 0.1770 -0.0231 -0.0203 0.0044  83  LEU   B O   
5171 C CB  . LEU   B 83  ? 0.1605 0.1371 0.2113 -0.0117 -0.0238 -0.0159 83  LEU   B CB  
5172 C CG  . LEU   B 83  ? 0.1766 0.1605 0.2081 -0.0167 -0.0154 -0.0167 83  LEU   B CG  
5173 C CD1 . LEU   B 83  ? 0.1823 0.1652 0.2107 -0.0078 -0.0223 -0.0090 83  LEU   B CD1 
5174 C CD2 . LEU   B 83  ? 0.1974 0.1651 0.2185 -0.0088 -0.0231 -0.0303 83  LEU   B CD2 
5186 N N   . SER   B 84  ? 0.1609 0.1340 0.2191 -0.0228 -0.0224 -0.0035 84  SER   B N   
5187 C CA  . SER   B 84  ? 0.1589 0.1550 0.2116 -0.0251 -0.0236 0.0100  84  SER   B CA  
5188 C C   . SER   B 84  ? 0.1497 0.1715 0.1671 -0.0249 -0.0253 0.0189  84  SER   B C   
5189 O O   . SER   B 84  ? 0.1546 0.1587 0.1688 -0.0234 -0.0166 0.0012  84  SER   B O   
5190 C CB  . SER   B 84  ? 0.1760 0.1609 0.2600 -0.0327 0.0034  0.0168  84  SER   B CB  
5191 O OG  . SER   B 84  ? 0.1770 0.1799 0.3108 -0.0412 0.0146  0.0251  84  SER   B OG  
5197 N N   . GLY   B 85  ? 0.1565 0.1916 0.1763 -0.0264 -0.0251 0.0298  85  GLY   B N   
5198 C CA  . GLY   B 85  ? 0.1570 0.1956 0.1894 -0.0317 -0.0118 0.0039  85  GLY   B CA  
5199 C C   . GLY   B 85  ? 0.1535 0.1776 0.1980 -0.0373 -0.0113 0.0089  85  GLY   B C   
5200 O O   . GLY   B 85  ? 0.1584 0.1767 0.2043 -0.0472 0.0042  0.0009  85  GLY   B O   
5204 N N   . HIS   B 86  ? 0.1550 0.1647 0.2073 -0.0344 -0.0200 0.0172  86  HIS   B N   
5205 C CA  . HIS   B 86  ? 0.1525 0.1678 0.1965 -0.0353 -0.0175 0.0187  86  HIS   B CA  
5206 C C   . HIS   B 86  ? 0.1567 0.1830 0.1958 -0.0415 -0.0035 0.0334  86  HIS   B C   
5207 O O   . HIS   B 86  ? 0.1709 0.1958 0.1999 -0.0360 0.0060  0.0293  86  HIS   B O   
5208 C CB  . HIS   B 86  ? 0.1635 0.1729 0.1965 -0.0260 -0.0332 0.0133  86  HIS   B CB  
5209 C CG  . HIS   B 86  ? 0.1715 0.1749 0.1929 -0.0205 -0.0338 0.0141  86  HIS   B CG  
5210 N ND1 . HIS   B 86  ? 0.1855 0.1963 0.2164 -0.0275 -0.0402 -0.0010 86  HIS   B ND1 
5211 C CD2 . HIS   B 86  ? 0.1666 0.1695 0.2167 -0.0175 -0.0337 0.0133  86  HIS   B CD2 
5212 C CE1 . HIS   B 86  ? 0.1887 0.1878 0.2087 -0.0237 -0.0244 -0.0169 86  HIS   B CE1 
5213 N NE2 . HIS   B 86  ? 0.1799 0.1795 0.2066 -0.0062 -0.0244 0.0012  86  HIS   B NE2 
5221 N N   . ASN   B 87  ? 0.1559 0.1884 0.2054 -0.0346 -0.0036 0.0257  87  ASN   B N   
5222 C CA  . ASN   B 87  ? 0.1615 0.2064 0.2105 -0.0368 0.0225  0.0182  87  ASN   B CA  
5223 C C   . ASN   B 87  ? 0.1733 0.1924 0.2057 -0.0255 0.0308  0.0145  87  ASN   B C   
5224 O O   . ASN   B 87  ? 0.2017 0.2016 0.2272 -0.0164 0.0452  0.0161  87  ASN   B O   
5225 C CB  . ASN   B 87  ? 0.1632 0.2418 0.2383 -0.0294 0.0170  0.0099  87  ASN   B CB  
5226 C CG  . ASN   B 87  ? 0.1704 0.2631 0.2367 0.0052  0.0213  0.0309  87  ASN   B CG  
5227 O OD1 . ASN   B 87  ? 0.1717 0.2456 0.2364 0.0109  0.0412  0.0507  87  ASN   B OD1 
5228 N ND2 . ASN   B 87  ? 0.2043 0.2758 0.2726 0.0089  0.0208  0.0236  87  ASN   B ND2 
5235 N N   . LEU   B 88  ? 0.1638 0.1741 0.1854 -0.0322 0.0108  0.0167  88  LEU   B N   
5236 C CA  . LEU   B 88  ? 0.1762 0.1644 0.1877 -0.0322 0.0061  0.0104  88  LEU   B CA  
5237 C C   . LEU   B 88  ? 0.1777 0.1551 0.1916 -0.0378 -0.0029 0.0113  88  LEU   B C   
5238 O O   . LEU   B 88  ? 0.2013 0.1620 0.2232 -0.0204 -0.0226 -0.0090 88  LEU   B O   
5239 C CB  . LEU   B 88  ? 0.1924 0.1738 0.2064 -0.0373 -0.0131 0.0095  88  LEU   B CB  
5240 C CG  . LEU   B 88  ? 0.2312 0.1983 0.2263 -0.0327 -0.0307 0.0312  88  LEU   B CG  
5241 C CD1 . LEU   B 88  ? 0.2446 0.2302 0.2313 -0.0444 -0.0280 0.0433  88  LEU   B CD1 
5242 C CD2 . LEU   B 88  ? 0.2694 0.2273 0.2721 0.0010  -0.0444 0.0073  88  LEU   B CD2 
5254 N N   . ALA   B 89  ? 0.1668 0.1528 0.1860 -0.0369 0.0131  0.0070  89  ALA   B N   
5255 C CA  . ALA   B 89  ? 0.1594 0.1520 0.1728 -0.0358 0.0062  0.0100  89  ALA   B CA  
5256 C C   . ALA   B 89  ? 0.1708 0.1514 0.1844 -0.0425 0.0143  -0.0026 89  ALA   B C   
5257 O O   . ALA   B 89  ? 0.1568 0.1614 0.2152 -0.0408 0.0097  -0.0223 89  ALA   B O   
5258 C CB  . ALA   B 89  ? 0.1569 0.1543 0.1835 -0.0376 0.0112  0.0140  89  ALA   B CB  
5264 N N   . LYS   B 90  ? 0.2063 0.1399 0.1849 -0.0452 -0.0085 0.0041  90  LYS   B N   
5265 C CA  . LYS   B 90  ? 0.2198 0.1429 0.1774 -0.0435 -0.0059 0.0091  90  LYS   B CA  
5266 C C   . LYS   B 90  ? 0.1992 0.1320 0.1916 -0.0419 -0.0109 -0.0012 90  LYS   B C   
5267 O O   . LYS   B 90  ? 0.2102 0.1515 0.2095 -0.0553 -0.0015 -0.0047 90  LYS   B O   
5268 C CB  . LYS   B 90  ? 0.2419 0.1528 0.2058 -0.0298 -0.0016 0.0233  90  LYS   B CB  
5269 C CG  . LYS   B 90  ? 0.2441 0.1681 0.2105 -0.0149 0.0193  0.0236  90  LYS   B CG  
5270 C CD  . LYS   B 90  ? 0.2755 0.1983 0.2465 -0.0110 0.0355  0.0014  90  LYS   B CD  
5271 C CE  . LYS   B 90  ? 0.2908 0.2122 0.2828 -0.0247 0.0412  -0.0118 90  LYS   B CE  
5272 N NZ  . LYS   B 90  ? 0.2900 0.2061 0.2854 -0.0410 0.0526  -0.0142 90  LYS   B NZ  
5286 N N   . HIS   B 91  ? 0.1734 0.1253 0.1763 -0.0329 -0.0195 0.0101  91  HIS   B N   
5287 C CA  . HIS   B 91  ? 0.1649 0.1290 0.1875 -0.0270 -0.0164 0.0035  91  HIS   B CA  
5288 C C   . HIS   B 91  ? 0.1582 0.1294 0.1656 -0.0308 -0.0074 0.0084  91  HIS   B C   
5289 O O   . HIS   B 91  ? 0.1696 0.1322 0.1645 -0.0268 -0.0286 0.0027  91  HIS   B O   
5290 C CB  . HIS   B 91  ? 0.1832 0.1381 0.2342 -0.0128 -0.0127 0.0197  91  HIS   B CB  
5291 C CG  . HIS   B 91  ? 0.2214 0.1540 0.2892 -0.0012 0.0185  0.0261  91  HIS   B CG  
5292 N ND1 . HIS   B 91  ? 0.2492 0.1593 0.3353 -0.0050 0.0245  0.0210  91  HIS   B ND1 
5293 C CD2 . HIS   B 91  ? 0.2348 0.1877 0.3231 0.0162  0.0120  0.0515  91  HIS   B CD2 
5294 C CE1 . HIS   B 91  ? 0.2542 0.1772 0.3542 0.0152  0.0283  0.0249  91  HIS   B CE1 
5295 N NE2 . HIS   B 91  ? 0.2460 0.1948 0.3508 0.0285  0.0273  0.0566  91  HIS   B NE2 
5303 N N   . CYS   B 92  ? 0.1511 0.1301 0.1623 -0.0291 -0.0196 -0.0037 92  CYS   B N   
5304 C CA  . CYS   B 92  ? 0.1497 0.1289 0.1653 -0.0224 -0.0140 0.0022  92  CYS   B CA  
5305 C C   . CYS   B 92  ? 0.1451 0.1190 0.1648 -0.0167 -0.0107 0.0069  92  CYS   B C   
5306 O O   . CYS   B 92  ? 0.1526 0.1274 0.1788 -0.0176 -0.0086 0.0020  92  CYS   B O   
5307 C CB  . CYS   B 92  ? 0.1536 0.1375 0.1720 -0.0142 -0.0111 -0.0025 92  CYS   B CB  
5308 S SG  . CYS   B 92  ? 0.1459 0.1378 0.1964 -0.0131 -0.0143 0.0065  92  CYS   B SG  
5314 N N   . LEU   B 93  ? 0.1340 0.1265 0.1717 -0.0124 -0.0049 -0.0064 93  LEU   B N   
5315 C CA  . LEU   B 93  ? 0.1343 0.1258 0.1783 -0.0038 -0.0076 0.0032  93  LEU   B CA  
5316 C C   . LEU   B 93  ? 0.1306 0.1180 0.1690 -0.0044 -0.0097 0.0070  93  LEU   B C   
5317 O O   . LEU   B 93  ? 0.1416 0.1211 0.1861 -0.0070 -0.0090 -0.0015 93  LEU   B O   
5318 C CB  . LEU   B 93  ? 0.1322 0.1295 0.1966 -0.0014 -0.0075 -0.0016 93  LEU   B CB  
5319 C CG  . LEU   B 93  ? 0.1332 0.1372 0.2003 -0.0030 -0.0111 0.0050  93  LEU   B CG  
5320 C CD1 . LEU   B 93  ? 0.1420 0.1481 0.2029 0.0069  -0.0055 -0.0002 93  LEU   B CD1 
5321 C CD2 . LEU   B 93  ? 0.1406 0.1395 0.2131 -0.0083 -0.0196 0.0083  93  LEU   B CD2 
5333 N N   . HIS   B 94  ? 0.1401 0.1225 0.1719 -0.0063 -0.0169 0.0044  94  HIS   B N   
5334 C CA  . HIS   B 94  ? 0.1407 0.1207 0.1776 -0.0020 -0.0082 0.0014  94  HIS   B CA  
5335 C C   . HIS   B 94  ? 0.1327 0.1244 0.2045 -0.0043 -0.0057 0.0074  94  HIS   B C   
5336 O O   . HIS   B 94  ? 0.1388 0.1334 0.2297 -0.0081 0.0076  -0.0051 94  HIS   B O   
5337 C CB  . HIS   B 94  ? 0.1380 0.1260 0.1820 -0.0030 -0.0124 -0.0046 94  HIS   B CB  
5338 C CG  . HIS   B 94  ? 0.1430 0.1239 0.1815 -0.0038 -0.0225 -0.0063 94  HIS   B CG  
5339 N ND1 . HIS   B 94  ? 0.1433 0.1320 0.1855 -0.0095 -0.0276 -0.0078 94  HIS   B ND1 
5340 C CD2 . HIS   B 94  ? 0.1467 0.1285 0.1876 -0.0001 -0.0207 0.0008  94  HIS   B CD2 
5341 C CE1 . HIS   B 94  ? 0.1463 0.1267 0.1862 -0.0150 -0.0277 0.0001  94  HIS   B CE1 
5342 N NE2 . HIS   B 94  ? 0.1428 0.1347 0.1998 -0.0135 -0.0210 -0.0003 94  HIS   B NE2 
5350 N N   . VAL   B 95  ? 0.1305 0.1230 0.1883 -0.0071 -0.0060 0.0026  95  VAL   B N   
5351 C CA  . VAL   B 95  ? 0.1338 0.1337 0.1884 -0.0002 -0.0047 0.0161  95  VAL   B CA  
5352 C C   . VAL   B 95  ? 0.1385 0.1312 0.2018 -0.0116 0.0087  0.0121  95  VAL   B C   
5353 O O   . VAL   B 95  ? 0.1451 0.1300 0.2073 0.0037  0.0008  0.0112  95  VAL   B O   
5354 C CB  . VAL   B 95  ? 0.1357 0.1331 0.1903 -0.0029 -0.0158 0.0031  95  VAL   B CB  
5355 C CG1 . VAL   B 95  ? 0.1452 0.1523 0.2111 -0.0089 -0.0111 0.0175  95  VAL   B CG1 
5356 C CG2 . VAL   B 95  ? 0.1494 0.1351 0.1809 0.0014  -0.0168 0.0120  95  VAL   B CG2 
5366 N N   . VAL   B 96  ? 0.1500 0.1366 0.1857 0.0028  0.0043  0.0165  96  VAL   B N   
5367 C CA  . VAL   B 96  ? 0.1589 0.1486 0.1804 0.0031  0.0008  0.0149  96  VAL   B CA  
5368 C C   . VAL   B 96  ? 0.1649 0.1480 0.2056 0.0031  0.0043  0.0160  96  VAL   B C   
5369 O O   . VAL   B 96  ? 0.1681 0.1525 0.2263 0.0025  0.0145  0.0096  96  VAL   B O   
5370 C CB  . VAL   B 96  ? 0.1665 0.1669 0.1895 0.0050  0.0010  0.0149  96  VAL   B CB  
5371 C CG1 . VAL   B 96  ? 0.1667 0.1814 0.1974 0.0145  0.0058  0.0053  96  VAL   B CG1 
5372 C CG2 . VAL   B 96  ? 0.1678 0.1694 0.2015 -0.0013 0.0044  0.0024  96  VAL   B CG2 
5382 N N   . GLY   B 97  ? 0.1657 0.1466 0.1933 0.0011  0.0006  0.0125  97  GLY   B N   
5383 C CA  . GLY   B 97  ? 0.1803 0.1565 0.2006 0.0009  0.0021  0.0163  97  GLY   B CA  
5384 C C   . GLY   B 97  ? 0.1977 0.1663 0.2136 0.0050  -0.0002 0.0140  97  GLY   B C   
5385 O O   . GLY   B 97  ? 0.2097 0.1750 0.1922 0.0034  0.0085  0.0165  97  GLY   B O   
5389 N N   . PRO   B 98  ? 0.2129 0.1661 0.2186 0.0027  0.0184  0.0322  98  PRO   B N   
5390 C CA  . PRO   B 98  ? 0.2226 0.1843 0.2156 0.0053  0.0219  0.0215  98  PRO   B CA  
5391 C C   . PRO   B 98  ? 0.2340 0.1861 0.1935 0.0241  0.0300  0.0376  98  PRO   B C   
5392 O O   . PRO   B 98  ? 0.2271 0.1813 0.2140 0.0252  0.0321  0.0455  98  PRO   B O   
5393 C CB  . PRO   B 98  ? 0.2105 0.1868 0.2218 -0.0012 0.0254  0.0230  98  PRO   B CB  
5394 C CG  . PRO   B 98  ? 0.2069 0.1801 0.2248 -0.0029 0.0259  0.0406  98  PRO   B CG  
5395 C CD  . PRO   B 98  ? 0.1999 0.1710 0.2237 -0.0012 0.0209  0.0352  98  PRO   B CD  
5403 N N   . ASN   B 99  ? 0.2380 0.2041 0.2122 0.0335  0.0344  0.0214  99  ASN   B N   
5404 C CA  . ASN   B 99  ? 0.2620 0.2117 0.2200 0.0436  0.0240  0.0502  99  ASN   B CA  
5405 C C   . ASN   B 99  ? 0.2973 0.2481 0.2498 0.0376  0.0331  0.0838  99  ASN   B C   
5406 O O   . ASN   B 99  ? 0.3032 0.2569 0.2644 0.0400  0.0248  0.0868  99  ASN   B O   
5407 C CB  . ASN   B 99  ? 0.2672 0.2128 0.2199 0.0461  0.0160  0.0455  99  ASN   B CB  
5408 C CG  . ASN   B 99  ? 0.2727 0.2197 0.2358 0.0451  0.0078  0.0444  99  ASN   B CG  
5409 O OD1 . ASN   B 99  ? 0.2774 0.2207 0.2610 0.0525  0.0117  0.0443  99  ASN   B OD1 
5410 N ND2 . ASN   B 99  ? 0.2708 0.2210 0.2455 0.0451  -0.0066 0.0378  99  ASN   B ND2 
5417 N N   A VAL   B 100 ? 0.3166 0.2607 0.2764 0.0276  0.0405  0.1056  100 VAL   B N   
5418 N N   B VAL   B 100 ? 0.3189 0.2622 0.2759 0.0294  0.0350  0.1004  100 VAL   B N   
5419 C CA  A VAL   B 100 ? 0.3462 0.2856 0.3277 0.0179  0.0393  0.1152  100 VAL   B CA  
5420 C CA  B VAL   B 100 ? 0.3469 0.2842 0.3180 0.0208  0.0314  0.1090  100 VAL   B CA  
5421 C C   A VAL   B 100 ? 0.3687 0.2964 0.3272 0.0249  0.0317  0.1254  100 VAL   B C   
5422 C C   B VAL   B 100 ? 0.3683 0.2949 0.3205 0.0263  0.0259  0.1218  100 VAL   B C   
5423 O O   A VAL   B 100 ? 0.3736 0.3079 0.3344 0.0233  0.0366  0.1160  100 VAL   B O   
5424 O O   B VAL   B 100 ? 0.3717 0.3025 0.3233 0.0241  0.0287  0.1157  100 VAL   B O   
5425 C CB  A VAL   B 100 ? 0.3549 0.2990 0.3831 0.0021  0.0391  0.1191  100 VAL   B CB  
5426 C CB  B VAL   B 100 ? 0.3539 0.2949 0.3599 0.0075  0.0300  0.1086  100 VAL   B CB  
5427 C CG1 A VAL   B 100 ? 0.3598 0.3059 0.4048 -0.0018 0.0383  0.1135  100 VAL   B CG1 
5428 C CG1 B VAL   B 100 ? 0.3578 0.3001 0.3752 0.0042  0.0293  0.1041  100 VAL   B CG1 
5429 C CG2 A VAL   B 100 ? 0.3567 0.3039 0.3950 -0.0039 0.0429  0.1275  100 VAL   B CG2 
5430 C CG2 B VAL   B 100 ? 0.3555 0.2988 0.3701 0.0022  0.0316  0.1125  100 VAL   B CG2 
5449 N N   . ASN   B 101 ? 0.3842 0.3003 0.3234 0.0355  0.0191  0.1336  101 ASN   B N   
5450 C CA  . ASN   B 101 ? 0.4225 0.3231 0.3356 0.0425  0.0082  0.1385  101 ASN   B CA  
5451 C C   . ASN   B 101 ? 0.4626 0.3661 0.3441 0.0399  -0.0031 0.1443  101 ASN   B C   
5452 O O   . ASN   B 101 ? 0.4664 0.3770 0.3651 0.0448  -0.0047 0.1227  101 ASN   B O   
5453 C CB  . ASN   B 101 ? 0.4241 0.3078 0.3408 0.0439  0.0154  0.1221  101 ASN   B CB  
5454 C CG  . ASN   B 101 ? 0.4226 0.2966 0.3475 0.0447  0.0131  0.1107  101 ASN   B CG  
5455 O OD1 . ASN   B 101 ? 0.4247 0.2949 0.3762 0.0423  0.0257  0.0992  101 ASN   B OD1 
5456 N ND2 . ASN   B 101 ? 0.4182 0.2890 0.3538 0.0418  0.0091  0.1044  101 ASN   B ND2 
5464 N N   . LYS   B 102 ? 0.4970 0.4020 0.3556 0.0291  -0.0014 0.1470  102 LYS   B N   
5465 C CA  . LYS   B 102 ? 0.5296 0.4436 0.3918 0.0161  0.0066  0.1268  102 LYS   B CA  
5466 C C   . LYS   B 102 ? 0.5266 0.4463 0.3746 0.0199  0.0116  0.1306  102 LYS   B C   
5467 O O   . LYS   B 102 ? 0.5348 0.4533 0.3805 0.0193  0.0021  0.1284  102 LYS   B O   
5468 C CB  . LYS   B 102 ? 0.5596 0.4780 0.4541 0.0034  0.0172  0.0907  102 LYS   B CB  
5469 C CG  . LYS   B 102 ? 0.5835 0.5054 0.5289 -0.0060 0.0270  0.0531  102 LYS   B CG  
5470 C CD  . LYS   B 102 ? 0.6025 0.5270 0.5882 -0.0132 0.0361  0.0224  102 LYS   B CD  
5471 C CE  . LYS   B 102 ? 0.6160 0.5426 0.6359 -0.0197 0.0437  0.0016  102 LYS   B CE  
5472 N NZ  . LYS   B 102 ? 0.6249 0.5515 0.6634 -0.0232 0.0485  -0.0097 102 LYS   B NZ  
5486 N N   . GLY   B 103 ? 0.5106 0.4385 0.3573 0.0219  0.0271  0.1313  103 GLY   B N   
5487 C CA  . GLY   B 103 ? 0.4933 0.4283 0.3571 0.0233  0.0447  0.1214  103 GLY   B CA  
5488 C C   . GLY   B 103 ? 0.4713 0.4135 0.3514 0.0212  0.0591  0.1035  103 GLY   B C   
5489 O O   . GLY   B 103 ? 0.4749 0.4200 0.3580 0.0166  0.0610  0.1039  103 GLY   B O   
5493 N N   . GLU   B 104 ? 0.4409 0.3874 0.3340 0.0218  0.0725  0.0765  104 GLU   B N   
5494 C CA  . GLU   B 104 ? 0.4100 0.3635 0.3163 0.0261  0.0735  0.0435  104 GLU   B CA  
5495 C C   . GLU   B 104 ? 0.4046 0.3582 0.3346 0.0071  0.1034  0.0391  104 GLU   B C   
5496 O O   . GLU   B 104 ? 0.4006 0.3556 0.3519 0.0101  0.1012  0.0327  104 GLU   B O   
5497 C CB  . GLU   B 104 ? 0.3916 0.3419 0.2990 0.0441  0.0317  0.0085  104 GLU   B CB  
5498 C CG  . GLU   B 104 ? 0.3755 0.3250 0.2826 0.0562  -0.0078 -0.0265 104 GLU   B CG  
5499 C CD  . GLU   B 104 ? 0.3626 0.3077 0.2693 0.0640  -0.0342 -0.0439 104 GLU   B CD  
5500 O OE1 . GLU   B 104 ? 0.3439 0.2928 0.2490 0.0735  -0.0259 -0.0392 104 GLU   B OE1 
5501 O OE2 . GLU   B 104 ? 0.3663 0.3130 0.2766 0.0566  -0.0579 -0.0609 104 GLU   B OE2 
5508 N N   A ASP   B 105 ? 0.4031 0.3591 0.3444 -0.0055 0.1285  0.0395  105 ASP   B N   
5509 N N   B ASP   B 105 ? 0.4011 0.3568 0.3422 -0.0013 0.1084  0.0410  105 ASP   B N   
5510 C CA  A ASP   B 105 ? 0.4036 0.3593 0.3593 -0.0172 0.1515  0.0283  105 ASP   B CA  
5511 C CA  B ASP   B 105 ? 0.3980 0.3547 0.3491 -0.0090 0.1134  0.0348  105 ASP   B CA  
5512 C C   A ASP   B 105 ? 0.3864 0.3311 0.3236 -0.0291 0.1569  0.0271  105 ASP   B C   
5513 C C   B ASP   B 105 ? 0.3874 0.3402 0.3280 -0.0126 0.1090  0.0276  105 ASP   B C   
5514 O O   A ASP   B 105 ? 0.3793 0.3208 0.3102 -0.0276 0.1653  0.0278  105 ASP   B O   
5515 O O   B ASP   B 105 ? 0.3849 0.3355 0.3192 -0.0113 0.1118  0.0271  105 ASP   B O   
5516 C CB  A ASP   B 105 ? 0.4175 0.3838 0.4211 -0.0133 0.1616  0.0126  105 ASP   B CB  
5517 C CB  B ASP   B 105 ? 0.4024 0.3650 0.3810 -0.0103 0.1209  0.0322  105 ASP   B CB  
5518 C CG  A ASP   B 105 ? 0.4278 0.4016 0.4777 -0.0127 0.1686  0.0022  105 ASP   B CG  
5519 C CG  B ASP   B 105 ? 0.4046 0.3707 0.4061 -0.0138 0.1276  0.0334  105 ASP   B CG  
5520 O OD1 A ASP   B 105 ? 0.4261 0.4072 0.4898 -0.0175 0.1776  0.0052  105 ASP   B OD1 
5521 O OD1 B ASP   B 105 ? 0.4034 0.3733 0.4165 -0.0166 0.1298  0.0347  105 ASP   B OD1 
5522 O OD2 A ASP   B 105 ? 0.4348 0.4094 0.5110 -0.0093 0.1618  -0.0073 105 ASP   B OD2 
5523 O OD2 B ASP   B 105 ? 0.4028 0.3721 0.4089 -0.0171 0.1360  0.0376  105 ASP   B OD2 
5532 N N   A ILE   B 106 ? 0.3758 0.3116 0.3298 -0.0352 0.1440  0.0235  106 ILE   B N   
5533 N N   B ILE   B 106 ? 0.3785 0.3288 0.3295 -0.0128 0.0974  0.0208  106 ILE   B N   
5534 C CA  A ILE   B 106 ? 0.3582 0.2896 0.3277 -0.0479 0.1481  0.0256  106 ILE   B CA  
5535 C CA  B ILE   B 106 ? 0.3663 0.3173 0.3291 -0.0157 0.0951  0.0148  106 ILE   B CA  
5536 C C   A ILE   B 106 ? 0.3304 0.2824 0.3123 -0.0450 0.1405  0.0086  106 ILE   B C   
5537 C C   B ILE   B 106 ? 0.3464 0.3124 0.3188 -0.0126 0.0925  0.0035  106 ILE   B C   
5538 O O   A ILE   B 106 ? 0.3181 0.2600 0.3002 -0.0497 0.1375  -0.0058 106 ILE   B O   
5539 O O   B ILE   B 106 ? 0.3406 0.3019 0.3105 -0.0129 0.0912  -0.0051 106 ILE   B O   
5540 C CB  A ILE   B 106 ? 0.3739 0.2830 0.3480 -0.0573 0.1449  0.0331  106 ILE   B CB  
5541 C CB  B ILE   B 106 ? 0.3754 0.3152 0.3401 -0.0205 0.0924  0.0162  106 ILE   B CB  
5542 C CG1 A ILE   B 106 ? 0.3819 0.2849 0.3593 -0.0538 0.1370  0.0284  106 ILE   B CG1 
5543 C CG1 B ILE   B 106 ? 0.3803 0.3153 0.3474 -0.0191 0.0870  0.0138  106 ILE   B CG1 
5544 C CG2 A ILE   B 106 ? 0.3797 0.2823 0.3653 -0.0639 0.1451  0.0378  106 ILE   B CG2 
5545 C CG2 B ILE   B 106 ? 0.3787 0.3165 0.3499 -0.0235 0.0935  0.0173  106 ILE   B CG2 
5546 C CD1 A ILE   B 106 ? 0.3873 0.2891 0.3581 -0.0498 0.1347  0.0282  106 ILE   B CD1 
5547 C CD1 B ILE   B 106 ? 0.3835 0.3168 0.3478 -0.0175 0.0848  0.0138  106 ILE   B CD1 
5570 N N   A GLN   B 107 ? 0.3202 0.3020 0.3271 -0.0408 0.1277  0.0093  107 GLN   B N   
5571 N N   B GLN   B 107 ? 0.3344 0.3209 0.3295 -0.0128 0.0877  0.0030  107 GLN   B N   
5572 C CA  A GLN   B 107 ? 0.3108 0.3181 0.3509 -0.0320 0.1067  0.0139  107 GLN   B CA  
5573 C CA  B GLN   B 107 ? 0.3226 0.3265 0.3476 -0.0101 0.0780  0.0069  107 GLN   B CA  
5574 C C   A GLN   B 107 ? 0.2855 0.2962 0.3253 -0.0164 0.0816  0.0100  107 GLN   B C   
5575 C C   B GLN   B 107 ? 0.2934 0.3026 0.3192 -0.0043 0.0709  0.0065  107 GLN   B C   
5576 O O   A GLN   B 107 ? 0.2785 0.2964 0.3391 -0.0119 0.0635  0.0054  107 GLN   B O   
5577 O O   B GLN   B 107 ? 0.2898 0.3045 0.3244 -0.0012 0.0612  0.0042  107 GLN   B O   
5578 C CB  A GLN   B 107 ? 0.3362 0.3573 0.4181 -0.0295 0.0943  0.0142  107 GLN   B CB  
5579 C CB  B GLN   B 107 ? 0.3441 0.3555 0.4049 -0.0093 0.0688  0.0077  107 GLN   B CB  
5580 C CG  A GLN   B 107 ? 0.3626 0.3899 0.4922 -0.0218 0.0709  0.0121  107 GLN   B CG  
5581 C CG  B GLN   B 107 ? 0.3650 0.3796 0.4666 -0.0053 0.0539  0.0075  107 GLN   B CG  
5582 C CD  A GLN   B 107 ? 0.3833 0.4135 0.5510 -0.0174 0.0522  0.0114  107 GLN   B CD  
5583 C CD  B GLN   B 107 ? 0.3818 0.3964 0.5157 -0.0032 0.0415  0.0082  107 GLN   B CD  
5584 O OE1 A GLN   B 107 ? 0.3905 0.4231 0.5745 -0.0108 0.0477  0.0087  107 GLN   B OE1 
5585 O OE1 B GLN   B 107 ? 0.3876 0.4024 0.5337 0.0004  0.0396  0.0077  107 GLN   B OE1 
5586 N NE2 A GLN   B 107 ? 0.3932 0.4203 0.5721 -0.0167 0.0441  0.0156  107 GLN   B NE2 
5587 N NE2 B GLN   B 107 ? 0.3897 0.4020 0.5341 -0.0026 0.0361  0.0112  107 GLN   B NE2 
5604 N N   . LEU   B 108 ? 0.2661 0.2767 0.2947 0.0040  0.0715  0.0089  108 LEU   B N   
5605 C CA  . LEU   B 108 ? 0.2424 0.2449 0.2569 0.0173  0.0566  0.0222  108 LEU   B CA  
5606 C C   . LEU   B 108 ? 0.2054 0.2010 0.2600 0.0178  0.0395  0.0318  108 LEU   B C   
5607 O O   . LEU   B 108 ? 0.2008 0.1845 0.2566 0.0184  0.0349  0.0373  108 LEU   B O   
5608 C CB  . LEU   B 108 ? 0.2537 0.2636 0.2513 0.0148  0.0613  0.0366  108 LEU   B CB  
5609 C CG  . LEU   B 108 ? 0.2752 0.2948 0.2654 0.0175  0.0603  0.0137  108 LEU   B CG  
5610 C CD1 . LEU   B 108 ? 0.2880 0.3090 0.2586 0.0061  0.0606  0.0094  108 LEU   B CD1 
5611 C CD2 . LEU   B 108 ? 0.2888 0.3092 0.2810 0.0268  0.0499  -0.0040 108 LEU   B CD2 
5624 N N   . LEU   B 109 ? 0.1870 0.1811 0.2593 0.0146  0.0423  0.0228  109 LEU   B N   
5625 C CA  . LEU   B 109 ? 0.1622 0.1541 0.2724 0.0077  0.0369  0.0303  109 LEU   B CA  
5626 C C   . LEU   B 109 ? 0.1549 0.1400 0.2673 0.0046  0.0329  0.0246  109 LEU   B C   
5627 O O   . LEU   B 109 ? 0.1563 0.1371 0.2547 0.0058  0.0328  0.0273  109 LEU   B O   
5628 C CB  . LEU   B 109 ? 0.1671 0.1434 0.2942 0.0048  0.0236  0.0404  109 LEU   B CB  
5629 C CG  . LEU   B 109 ? 0.1693 0.1414 0.2870 0.0019  0.0233  0.0286  109 LEU   B CG  
5630 C CD1 . LEU   B 109 ? 0.1602 0.1525 0.2798 0.0115  0.0253  0.0382  109 LEU   B CD1 
5631 C CD2 . LEU   B 109 ? 0.1821 0.1465 0.3072 0.0042  0.0166  0.0306  109 LEU   B CD2 
5643 N N   . LYS   B 110 ? 0.1517 0.1393 0.2691 -0.0039 0.0337  0.0287  110 LYS   B N   
5644 C CA  . LYS   B 110 ? 0.1465 0.1361 0.2815 -0.0024 0.0229  0.0208  110 LYS   B CA  
5645 C C   . LYS   B 110 ? 0.1435 0.1403 0.2670 -0.0028 0.0195  0.0134  110 LYS   B C   
5646 O O   . LYS   B 110 ? 0.1414 0.1411 0.2601 -0.0072 0.0166  0.0052  110 LYS   B O   
5647 C CB  . LYS   B 110 ? 0.1471 0.1389 0.3044 -0.0053 0.0301  0.0144  110 LYS   B CB  
5648 C CG  . LYS   B 110 ? 0.1455 0.1349 0.3090 -0.0006 0.0062  0.0184  110 LYS   B CG  
5649 C CD  . LYS   B 110 ? 0.1489 0.1368 0.3185 -0.0087 0.0127  0.0151  110 LYS   B CD  
5650 C CE  . LYS   B 110 ? 0.1490 0.1515 0.3339 -0.0015 0.0150  0.0032  110 LYS   B CE  
5651 N NZ  . LYS   B 110 ? 0.1469 0.1711 0.3240 -0.0015 0.0005  0.0023  110 LYS   B NZ  
5665 N N   . SER   B 111 ? 0.1503 0.1391 0.2756 -0.0012 0.0269  0.0188  111 SER   B N   
5666 C CA  . SER   B 111 ? 0.1556 0.1426 0.2556 -0.0014 0.0237  0.0227  111 SER   B CA  
5667 C C   . SER   B 111 ? 0.1477 0.1369 0.2501 -0.0077 0.0146  0.0122  111 SER   B C   
5668 O O   . SER   B 111 ? 0.1436 0.1352 0.2679 -0.0038 0.0162  0.0140  111 SER   B O   
5669 C CB  . SER   B 111 ? 0.1669 0.1659 0.2658 0.0031  0.0435  0.0312  111 SER   B CB  
5670 O OG  . SER   B 111 ? 0.1852 0.2007 0.2797 0.0067  0.0482  0.0281  111 SER   B OG  
5676 N N   . ALA   B 112 ? 0.1402 0.1411 0.2526 -0.0014 0.0213  0.0120  112 ALA   B N   
5677 C CA  . ALA   B 112 ? 0.1385 0.1429 0.2361 -0.0001 0.0035  0.0042  112 ALA   B CA  
5678 C C   . ALA   B 112 ? 0.1311 0.1366 0.2308 -0.0033 0.0078  0.0018  112 ALA   B C   
5679 O O   . ALA   B 112 ? 0.1363 0.1407 0.2233 -0.0102 0.0065  0.0033  112 ALA   B O   
5680 C CB  . ALA   B 112 ? 0.1480 0.1506 0.2504 0.0055  0.0014  0.0104  112 ALA   B CB  
5686 N N   . TYR   B 113 ? 0.1308 0.1263 0.2429 -0.0022 0.0125  0.0006  113 TYR   B N   
5687 C CA  . TYR   B 113 ? 0.1275 0.1255 0.2361 -0.0074 0.0071  -0.0042 113 TYR   B CA  
5688 C C   . TYR   B 113 ? 0.1258 0.1222 0.2477 -0.0106 0.0100  0.0105  113 TYR   B C   
5689 O O   . TYR   B 113 ? 0.1289 0.1237 0.2330 -0.0090 0.0033  -0.0005 113 TYR   B O   
5690 C CB  . TYR   B 113 ? 0.1324 0.1201 0.2384 -0.0058 0.0199  0.0010  113 TYR   B CB  
5691 C CG  . TYR   B 113 ? 0.1394 0.1186 0.2520 -0.0100 0.0108  0.0051  113 TYR   B CG  
5692 C CD1 . TYR   B 113 ? 0.1392 0.1247 0.2622 -0.0065 0.0151  0.0117  113 TYR   B CD1 
5693 C CD2 . TYR   B 113 ? 0.1451 0.1221 0.2532 -0.0100 0.0074  0.0130  113 TYR   B CD2 
5694 C CE1 . TYR   B 113 ? 0.1433 0.1311 0.2632 -0.0036 0.0157  0.0024  113 TYR   B CE1 
5695 C CE2 . TYR   B 113 ? 0.1517 0.1178 0.2643 -0.0034 0.0021  0.0108  113 TYR   B CE2 
5696 C CZ  . TYR   B 113 ? 0.1413 0.1252 0.2798 0.0029  0.0024  0.0090  113 TYR   B CZ  
5697 O OH  . TYR   B 113 ? 0.1449 0.1240 0.3057 0.0052  0.0166  0.0079  113 TYR   B OH  
5707 N N   . GLU   B 114 ? 0.1294 0.1147 0.2503 -0.0033 0.0065  0.0113  114 GLU   B N   
5708 C CA  . GLU   B 114 ? 0.1245 0.1180 0.2488 0.0001  0.0087  0.0009  114 GLU   B CA  
5709 C C   . GLU   B 114 ? 0.1264 0.1214 0.2404 0.0025  0.0084  0.0005  114 GLU   B C   
5710 O O   . GLU   B 114 ? 0.1217 0.1242 0.2546 0.0005  -0.0015 0.0052  114 GLU   B O   
5711 C CB  . GLU   B 114 ? 0.1303 0.1278 0.2644 -0.0016 0.0107  0.0007  114 GLU   B CB  
5712 C CG  . GLU   B 114 ? 0.1323 0.1285 0.2627 -0.0017 0.0145  0.0038  114 GLU   B CG  
5713 C CD  . GLU   B 114 ? 0.1286 0.1281 0.2582 -0.0107 0.0063  0.0050  114 GLU   B CD  
5714 O OE1 . GLU   B 114 ? 0.1286 0.1402 0.2687 -0.0127 0.0111  0.0013  114 GLU   B OE1 
5715 O OE2 . GLU   B 114 ? 0.1349 0.1471 0.2689 -0.0225 0.0111  0.0043  114 GLU   B OE2 
5722 N N   . ASN   B 115 ? 0.1289 0.1154 0.2311 -0.0038 -0.0018 0.0006  115 ASN   B N   
5723 C CA  . ASN   B 115 ? 0.1329 0.1229 0.2135 -0.0083 -0.0027 0.0086  115 ASN   B CA  
5724 C C   . ASN   B 115 ? 0.1256 0.1191 0.2143 -0.0119 -0.0050 -0.0011 115 ASN   B C   
5725 O O   . ASN   B 115 ? 0.1395 0.1247 0.2164 -0.0156 -0.0019 0.0029  115 ASN   B O   
5726 C CB  . ASN   B 115 ? 0.1387 0.1348 0.2169 -0.0135 -0.0065 0.0104  115 ASN   B CB  
5727 C CG  . ASN   B 115 ? 0.1464 0.1368 0.2194 -0.0052 0.0002  -0.0026 115 ASN   B CG  
5728 O OD1 . ASN   B 115 ? 0.1906 0.1486 0.2511 -0.0063 0.0115  -0.0054 115 ASN   B OD1 
5729 N ND2 . ASN   B 115 ? 0.1508 0.1519 0.2166 -0.0121 0.0087  0.0059  115 ASN   B ND2 
5736 N N   . PHE   B 116 ? 0.1240 0.1185 0.2034 -0.0059 0.0015  -0.0005 116 PHE   B N   
5737 C CA  . PHE   B 116 ? 0.1317 0.1243 0.2190 -0.0069 -0.0054 -0.0009 116 PHE   B CA  
5738 C C   . PHE   B 116 ? 0.1343 0.1164 0.2183 -0.0117 -0.0068 -0.0000 116 PHE   B C   
5739 O O   . PHE   B 116 ? 0.1373 0.1284 0.2153 -0.0023 -0.0076 0.0052  116 PHE   B O   
5740 C CB  . PHE   B 116 ? 0.1235 0.1248 0.2147 -0.0041 -0.0156 0.0016  116 PHE   B CB  
5741 C CG  . PHE   B 116 ? 0.1256 0.1184 0.2206 -0.0075 -0.0122 0.0022  116 PHE   B CG  
5742 C CD1 . PHE   B 116 ? 0.1364 0.1273 0.2314 -0.0067 -0.0004 0.0087  116 PHE   B CD1 
5743 C CD2 . PHE   B 116 ? 0.1278 0.1266 0.2189 -0.0069 -0.0074 -0.0030 116 PHE   B CD2 
5744 C CE1 . PHE   B 116 ? 0.1366 0.1309 0.2194 -0.0114 -0.0198 0.0096  116 PHE   B CE1 
5745 C CE2 . PHE   B 116 ? 0.1347 0.1297 0.2180 -0.0051 -0.0017 0.0028  116 PHE   B CE2 
5746 C CZ  . PHE   B 116 ? 0.1290 0.1324 0.2213 -0.0058 -0.0087 0.0011  116 PHE   B CZ  
5756 N N   . ASN   B 117 ? 0.1286 0.1163 0.2269 -0.0067 -0.0126 0.0072  117 ASN   B N   
5757 C CA  . ASN   B 117 ? 0.1358 0.1200 0.2333 -0.0043 -0.0114 -0.0042 117 ASN   B CA  
5758 C C   . ASN   B 117 ? 0.1365 0.1224 0.2463 0.0045  -0.0165 0.0025  117 ASN   B C   
5759 O O   . ASN   B 117 ? 0.1485 0.1259 0.2667 -0.0057 -0.0412 0.0038  117 ASN   B O   
5760 C CB  . ASN   B 117 ? 0.1359 0.1275 0.2338 -0.0070 -0.0030 -0.0065 117 ASN   B CB  
5761 C CG  . ASN   B 117 ? 0.1300 0.1269 0.2477 -0.0020 -0.0049 -0.0058 117 ASN   B CG  
5762 O OD1 . ASN   B 117 ? 0.1556 0.1214 0.2628 -0.0146 0.0008  -0.0050 117 ASN   B OD1 
5763 N ND2 . ASN   B 117 ? 0.1349 0.1313 0.2448 -0.0050 -0.0051 -0.0053 117 ASN   B ND2 
5770 N N   . GLN   B 118 ? 0.1326 0.1211 0.2415 -0.0082 -0.0212 0.0028  118 GLN   B N   
5771 C CA  . GLN   B 118 ? 0.1461 0.1254 0.2508 0.0008  -0.0132 -0.0002 118 GLN   B CA  
5772 C C   . GLN   B 118 ? 0.1452 0.1214 0.2535 -0.0012 -0.0138 -0.0033 118 GLN   B C   
5773 O O   . GLN   B 118 ? 0.1632 0.1203 0.2960 -0.0117 -0.0078 0.0016  118 GLN   B O   
5774 C CB  . GLN   B 118 ? 0.1557 0.1277 0.2550 0.0006  -0.0114 0.0008  118 GLN   B CB  
5775 C CG  . GLN   B 118 ? 0.1593 0.1240 0.2559 0.0057  -0.0074 -0.0072 118 GLN   B CG  
5776 C CD  . GLN   B 118 ? 0.1618 0.1250 0.2605 -0.0030 -0.0159 -0.0198 118 GLN   B CD  
5777 O OE1 . GLN   B 118 ? 0.1659 0.1247 0.2711 0.0004  0.0032  0.0010  118 GLN   B OE1 
5778 N NE2 . GLN   B 118 ? 0.1708 0.1258 0.2655 0.0031  -0.0167 -0.0023 118 GLN   B NE2 
5787 N N   . HIS   B 119 ? 0.1498 0.1239 0.2082 -0.0064 -0.0176 0.0025  119 HIS   B N   
5788 C CA  . HIS   B 119 ? 0.1561 0.1382 0.2045 -0.0050 -0.0155 0.0048  119 HIS   B CA  
5789 C C   . HIS   B 119 ? 0.1640 0.1376 0.2074 -0.0070 -0.0284 0.0120  119 HIS   B C   
5790 O O   . HIS   B 119 ? 0.1662 0.1366 0.2328 -0.0265 -0.0227 0.0099  119 HIS   B O   
5791 C CB  . HIS   B 119 ? 0.1640 0.1497 0.2115 -0.0024 -0.0239 -0.0034 119 HIS   B CB  
5792 C CG  . HIS   B 119 ? 0.1675 0.1717 0.2330 0.0077  -0.0439 -0.0203 119 HIS   B CG  
5793 N ND1 . HIS   B 119 ? 0.1816 0.1861 0.2617 -0.0011 -0.0541 -0.0327 119 HIS   B ND1 
5794 C CD2 . HIS   B 119 ? 0.1832 0.1934 0.2436 0.0377  -0.0511 -0.0192 119 HIS   B CD2 
5795 C CE1 . HIS   B 119 ? 0.2016 0.1995 0.2638 0.0182  -0.0559 -0.0462 119 HIS   B CE1 
5796 N NE2 . HIS   B 119 ? 0.1995 0.2157 0.2527 0.0326  -0.0551 -0.0406 119 HIS   B NE2 
5804 N N   . GLU   B 120 ? 0.1815 0.1440 0.2023 -0.0071 -0.0381 0.0122  120 GLU   B N   
5805 C CA  . GLU   B 120 ? 0.2056 0.1555 0.2290 -0.0066 -0.0475 0.0277  120 GLU   B CA  
5806 C C   . GLU   B 120 ? 0.1871 0.1466 0.2189 -0.0159 -0.0380 0.0280  120 GLU   B C   
5807 O O   . GLU   B 120 ? 0.1807 0.1551 0.2102 -0.0174 -0.0343 0.0156  120 GLU   B O   
5808 C CB  . GLU   B 120 ? 0.2671 0.1871 0.2987 0.0197  -0.0678 0.0526  120 GLU   B CB  
5809 C CG  . GLU   B 120 ? 0.3185 0.2503 0.3917 0.0297  -0.0803 0.0568  120 GLU   B CG  
5810 C CD  . GLU   B 120 ? 0.3594 0.3163 0.4843 0.0280  -0.0859 0.0648  120 GLU   B CD  
5811 O OE1 . GLU   B 120 ? 0.3768 0.3358 0.5185 0.0192  -0.0781 0.0711  120 GLU   B OE1 
5812 O OE2 . GLU   B 120 ? 0.3885 0.3371 0.5333 0.0255  -0.0902 0.0583  120 GLU   B OE2 
5819 N N   . VAL   B 121 ? 0.1767 0.1373 0.2121 -0.0208 -0.0281 0.0223  121 VAL   B N   
5820 C CA  . VAL   B 121 ? 0.1736 0.1535 0.2031 -0.0175 -0.0289 0.0191  121 VAL   B CA  
5821 C C   . VAL   B 121 ? 0.1655 0.1423 0.1968 -0.0263 -0.0234 0.0148  121 VAL   B C   
5822 O O   . VAL   B 121 ? 0.1724 0.1366 0.2127 -0.0335 -0.0272 0.0085  121 VAL   B O   
5823 C CB  . VAL   B 121 ? 0.1901 0.1883 0.2101 -0.0119 -0.0297 0.0175  121 VAL   B CB  
5824 C CG1 . VAL   B 121 ? 0.1968 0.2075 0.2442 -0.0210 -0.0177 0.0154  121 VAL   B CG1 
5825 C CG2 . VAL   B 121 ? 0.2182 0.2111 0.2199 0.0003  -0.0231 0.0070  121 VAL   B CG2 
5835 N N   . LEU   B 122 ? 0.1563 0.1349 0.1829 -0.0216 -0.0223 0.0126  122 LEU   B N   
5836 C CA  . LEU   B 122 ? 0.1461 0.1460 0.1950 -0.0257 -0.0207 0.0165  122 LEU   B CA  
5837 C C   . LEU   B 122 ? 0.1499 0.1307 0.1942 -0.0297 -0.0221 0.0120  122 LEU   B C   
5838 O O   . LEU   B 122 ? 0.1587 0.1329 0.2122 -0.0342 -0.0273 0.0038  122 LEU   B O   
5839 C CB  . LEU   B 122 ? 0.1700 0.1558 0.2143 -0.0132 -0.0272 0.0144  122 LEU   B CB  
5840 C CG  . LEU   B 122 ? 0.1597 0.1596 0.2171 -0.0176 -0.0138 0.0071  122 LEU   B CG  
5841 C CD1 . LEU   B 122 ? 0.1654 0.1778 0.2301 -0.0186 -0.0261 0.0086  122 LEU   B CD1 
5842 C CD2 . LEU   B 122 ? 0.1631 0.1577 0.1914 -0.0097 -0.0076 -0.0117 122 LEU   B CD2 
5854 N N   . LEU   B 123 ? 0.1476 0.1243 0.1845 -0.0266 -0.0191 0.0109  123 LEU   B N   
5855 C CA  . LEU   B 123 ? 0.1519 0.1253 0.1933 -0.0229 -0.0202 -0.0028 123 LEU   B CA  
5856 C C   . LEU   B 123 ? 0.1439 0.1187 0.1938 -0.0241 -0.0243 0.0010  123 LEU   B C   
5857 O O   . LEU   B 123 ? 0.1548 0.1271 0.1876 -0.0304 -0.0204 -0.0027 123 LEU   B O   
5858 C CB  . LEU   B 123 ? 0.1571 0.1274 0.2096 -0.0223 -0.0155 -0.0040 123 LEU   B CB  
5859 C CG  . LEU   B 123 ? 0.1505 0.1357 0.2149 -0.0192 -0.0094 0.0039  123 LEU   B CG  
5860 C CD1 . LEU   B 123 ? 0.1639 0.1381 0.2357 -0.0162 -0.0013 -0.0106 123 LEU   B CD1 
5861 C CD2 . LEU   B 123 ? 0.1561 0.1481 0.2201 -0.0205 -0.0028 0.0152  123 LEU   B CD2 
5873 N N   . ALA   B 124 ? 0.1490 0.1230 0.1870 -0.0190 -0.0184 -0.0039 124 ALA   B N   
5874 C CA  . ALA   B 124 ? 0.1399 0.1259 0.2004 -0.0154 -0.0169 -0.0092 124 ALA   B CA  
5875 C C   . ALA   B 124 ? 0.1339 0.1229 0.1833 -0.0232 -0.0174 0.0055  124 ALA   B C   
5876 O O   . ALA   B 124 ? 0.1443 0.1271 0.1951 -0.0203 -0.0210 0.0033  124 ALA   B O   
5877 C CB  . ALA   B 124 ? 0.1386 0.1234 0.2156 -0.0094 -0.0026 -0.0010 124 ALA   B CB  
5883 N N   . PRO   B 125 ? 0.1439 0.1227 0.1856 -0.0191 -0.0160 0.0088  125 PRO   B N   
5884 C CA  . PRO   B 125 ? 0.1508 0.1293 0.2042 -0.0184 -0.0219 0.0236  125 PRO   B CA  
5885 C C   . PRO   B 125 ? 0.1379 0.1258 0.2300 -0.0159 -0.0147 0.0153  125 PRO   B C   
5886 O O   . PRO   B 125 ? 0.1455 0.1221 0.2400 -0.0152 -0.0131 0.0119  125 PRO   B O   
5887 C CB  . PRO   B 125 ? 0.1545 0.1508 0.2239 -0.0232 -0.0211 0.0322  125 PRO   B CB  
5888 C CG  . PRO   B 125 ? 0.1548 0.1532 0.2138 -0.0312 -0.0257 0.0175  125 PRO   B CG  
5889 C CD  . PRO   B 125 ? 0.1524 0.1361 0.1970 -0.0301 -0.0204 0.0115  125 PRO   B CD  
5897 N N   . LEU   B 126 ? 0.1394 0.1217 0.2446 -0.0160 0.0012  0.0153  126 LEU   B N   
5898 C CA  . LEU   B 126 ? 0.1521 0.1332 0.2481 -0.0104 0.0125  0.0200  126 LEU   B CA  
5899 C C   . LEU   B 126 ? 0.1491 0.1393 0.2433 -0.0063 0.0171  0.0279  126 LEU   B C   
5900 O O   . LEU   B 126 ? 0.1712 0.1682 0.2673 0.0161  -0.0127 0.0047  126 LEU   B O   
5901 C CB  . LEU   B 126 ? 0.1719 0.1356 0.2724 -0.0132 0.0269  0.0133  126 LEU   B CB  
5902 C CG  . LEU   B 126 ? 0.1898 0.1424 0.2910 -0.0247 0.0251  -0.0134 126 LEU   B CG  
5903 C CD1 . LEU   B 126 ? 0.2016 0.1590 0.3328 -0.0283 0.0199  -0.0204 126 LEU   B CD1 
5904 C CD2 . LEU   B 126 ? 0.1926 0.1530 0.2974 -0.0275 0.0196  -0.0113 126 LEU   B CD2 
5916 N N   . LEU   B 127 ? 0.1434 0.1254 0.2489 -0.0009 0.0150  0.0117  127 LEU   B N   
5917 C CA  . LEU   B 127 ? 0.1473 0.1366 0.2572 -0.0069 0.0237  0.0215  127 LEU   B CA  
5918 C C   . LEU   B 127 ? 0.1475 0.1308 0.2735 -0.0039 0.0178  0.0242  127 LEU   B C   
5919 O O   . LEU   B 127 ? 0.1477 0.1368 0.2891 -0.0149 0.0147  0.0155  127 LEU   B O   
5920 C CB  . LEU   B 127 ? 0.1607 0.1318 0.2738 -0.0071 0.0175  0.0254  127 LEU   B CB  
5921 C CG  . LEU   B 127 ? 0.1742 0.1364 0.2757 -0.0019 0.0192  0.0293  127 LEU   B CG  
5922 C CD1 . LEU   B 127 ? 0.1833 0.1352 0.2714 0.0065  0.0179  0.0166  127 LEU   B CD1 
5923 C CD2 . LEU   B 127 ? 0.1779 0.1486 0.2806 -0.0142 0.0180  0.0374  127 LEU   B CD2 
5935 N N   . SER   B 128 ? 0.1459 0.1337 0.2670 0.0036  -0.0008 0.0162  128 SER   B N   
5936 C CA  . SER   B 128 ? 0.1636 0.1411 0.2662 0.0071  -0.0090 0.0176  128 SER   B CA  
5937 C C   . SER   B 128 ? 0.1704 0.1435 0.2882 0.0093  -0.0302 0.0142  128 SER   B C   
5938 O O   . SER   B 128 ? 0.1901 0.1463 0.3199 -0.0010 -0.0264 0.0279  128 SER   B O   
5939 C CB  . SER   B 128 ? 0.1776 0.1464 0.2610 0.0087  0.0012  0.0339  128 SER   B CB  
5940 O OG  . SER   B 128 ? 0.1773 0.1550 0.2736 0.0120  0.0042  0.0372  128 SER   B OG  
5946 N N   . ALA   B 129 ? 0.1831 0.1511 0.3126 0.0244  -0.0158 0.0114  129 ALA   B N   
5947 C CA  . ALA   B 129 ? 0.1983 0.1561 0.3193 0.0297  -0.0103 0.0009  129 ALA   B CA  
5948 C C   . ALA   B 129 ? 0.1857 0.1505 0.3063 0.0212  0.0040  0.0045  129 ALA   B C   
5949 O O   . ALA   B 129 ? 0.1807 0.1505 0.3035 0.0140  -0.0051 0.0060  129 ALA   B O   
5950 C CB  . ALA   B 129 ? 0.2210 0.1842 0.3493 0.0257  -0.0002 -0.0049 129 ALA   B CB  
5956 N N   . GLY   B 130 ? 0.1832 0.1509 0.3126 0.0261  0.0091  0.0000  130 GLY   B N   
5957 C CA  . GLY   B 130 ? 0.1889 0.1598 0.3181 0.0247  0.0289  0.0016  130 GLY   B CA  
5958 C C   . GLY   B 130 ? 0.1923 0.1664 0.3101 0.0164  0.0159  0.0055  130 GLY   B C   
5959 O O   . GLY   B 130 ? 0.2088 0.1774 0.3107 0.0201  0.0071  0.0153  130 GLY   B O   
5963 N N   . ILE   B 131 ? 0.1892 0.1797 0.3198 0.0306  0.0074  0.0062  131 ILE   B N   
5964 C CA  . ILE   B 131 ? 0.2103 0.1923 0.3114 0.0258  -0.0102 0.0178  131 ILE   B CA  
5965 C C   . ILE   B 131 ? 0.2231 0.1810 0.2782 0.0182  -0.0028 0.0183  131 ILE   B C   
5966 O O   . ILE   B 131 ? 0.2514 0.2004 0.2893 0.0195  -0.0234 0.0278  131 ILE   B O   
5967 C CB  . ILE   B 131 ? 0.2102 0.2189 0.3498 0.0218  -0.0176 0.0218  131 ILE   B CB  
5968 C CG1 . ILE   B 131 ? 0.2139 0.2317 0.3657 -0.0019 -0.0102 0.0260  131 ILE   B CG1 
5969 C CG2 . ILE   B 131 ? 0.2127 0.2342 0.3687 0.0310  -0.0175 0.0195  131 ILE   B CG2 
5970 C CD1 . ILE   B 131 ? 0.2229 0.2488 0.3748 -0.0131 -0.0141 0.0366  131 ILE   B CD1 
5982 N N   . PHE   B 132 ? 0.2033 0.1591 0.2650 0.0092  0.0084  0.0246  132 PHE   B N   
5983 C CA  . PHE   B 132 ? 0.2090 0.1646 0.2645 0.0020  0.0263  0.0194  132 PHE   B CA  
5984 C C   . PHE   B 132 ? 0.2277 0.1791 0.2820 0.0056  0.0317  0.0176  132 PHE   B C   
5985 O O   . PHE   B 132 ? 0.2455 0.2002 0.2987 0.0018  0.0515  0.0257  132 PHE   B O   
5986 C CB  . PHE   B 132 ? 0.1971 0.1707 0.2485 0.0062  0.0278  0.0252  132 PHE   B CB  
5987 C CG  . PHE   B 132 ? 0.1971 0.1759 0.2494 0.0123  0.0198  0.0289  132 PHE   B CG  
5988 C CD1 . PHE   B 132 ? 0.2019 0.1749 0.2774 0.0122  0.0217  0.0234  132 PHE   B CD1 
5989 C CD2 . PHE   B 132 ? 0.1997 0.1769 0.2344 0.0205  0.0236  0.0301  132 PHE   B CD2 
5990 C CE1 . PHE   B 132 ? 0.2114 0.1807 0.2861 0.0027  0.0176  0.0262  132 PHE   B CE1 
5991 C CE2 . PHE   B 132 ? 0.2069 0.1806 0.2419 0.0175  0.0117  0.0199  132 PHE   B CE2 
5992 C CZ  . PHE   B 132 ? 0.2087 0.1804 0.2696 0.0071  -0.0037 0.0325  132 PHE   B CZ  
6002 N N   . GLY   B 133 ? 0.2307 0.1689 0.2809 0.0002  0.0138  0.0448  133 GLY   B N   
6003 C CA  . GLY   B 133 ? 0.2409 0.1837 0.2914 -0.0187 0.0078  0.0367  133 GLY   B CA  
6004 C C   . GLY   B 133 ? 0.2465 0.1941 0.2906 -0.0273 0.0170  0.0440  133 GLY   B C   
6005 O O   . GLY   B 133 ? 0.2662 0.2077 0.3222 -0.0344 0.0244  0.0589  133 GLY   B O   
6009 N N   . ALA   B 134 ? 0.2292 0.1942 0.2720 -0.0274 0.0158  0.0330  134 ALA   B N   
6010 C CA  . ALA   B 134 ? 0.2245 0.1956 0.2832 -0.0225 0.0196  0.0164  134 ALA   B CA  
6011 C C   . ALA   B 134 ? 0.2237 0.1832 0.2886 -0.0197 0.0257  0.0276  134 ALA   B C   
6012 O O   . ALA   B 134 ? 0.2254 0.2070 0.3035 -0.0076 0.0296  0.0255  134 ALA   B O   
6013 C CB  . ALA   B 134 ? 0.2270 0.1990 0.2965 -0.0171 0.0189  0.0099  134 ALA   B CB  
6019 N N   . ASP   B 135 ? 0.2364 0.1707 0.2898 -0.0235 0.0199  0.0353  135 ASP   B N   
6020 C CA  . ASP   B 135 ? 0.2518 0.1685 0.3087 -0.0200 0.0073  0.0355  135 ASP   B CA  
6021 C C   . ASP   B 135 ? 0.2295 0.1574 0.2918 -0.0038 -0.0018 0.0269  135 ASP   B C   
6022 O O   . ASP   B 135 ? 0.2179 0.1495 0.3145 -0.0040 -0.0034 0.0250  135 ASP   B O   
6023 C CB  . ASP   B 135 ? 0.2871 0.1800 0.3400 -0.0388 0.0105  0.0380  135 ASP   B CB  
6024 C CG  . ASP   B 135 ? 0.3189 0.1735 0.3745 -0.0609 0.0112  0.0358  135 ASP   B CG  
6025 O OD1 . ASP   B 135 ? 0.3301 0.1568 0.3723 -0.0468 -0.0062 0.0320  135 ASP   B OD1 
6026 O OD2 . ASP   B 135 ? 0.3454 0.2102 0.4198 -0.0733 0.0182  0.0179  135 ASP   B OD2 
6031 N N   . PRO   B 136 ? 0.2220 0.1585 0.3161 0.0160  -0.0163 0.0238  136 PRO   B N   
6032 C CA  . PRO   B 136 ? 0.2016 0.1447 0.3218 0.0161  -0.0199 0.0119  136 PRO   B CA  
6033 C C   . PRO   B 136 ? 0.1791 0.1314 0.3319 0.0085  -0.0142 0.0025  136 PRO   B C   
6034 O O   . PRO   B 136 ? 0.1614 0.1333 0.3407 -0.0011 -0.0051 0.0119  136 PRO   B O   
6035 C CB  . PRO   B 136 ? 0.2096 0.1718 0.3218 0.0240  -0.0155 -0.0071 136 PRO   B CB  
6036 C CG  . PRO   B 136 ? 0.2280 0.1858 0.3388 0.0257  -0.0074 0.0014  136 PRO   B CG  
6037 C CD  . PRO   B 136 ? 0.2296 0.1769 0.3241 0.0356  -0.0055 0.0107  136 PRO   B CD  
6045 N N   . ILE   B 137 ? 0.1943 0.1302 0.3395 0.0098  -0.0174 0.0038  137 ILE   B N   
6046 C CA  . ILE   B 137 ? 0.1990 0.1296 0.3425 -0.0059 -0.0108 -0.0016 137 ILE   B CA  
6047 C C   . ILE   B 137 ? 0.1898 0.1338 0.3236 -0.0167 0.0055  0.0144  137 ILE   B C   
6048 O O   . ILE   B 137 ? 0.1837 0.1359 0.3193 -0.0146 0.0041  0.0057  137 ILE   B O   
6049 C CB  . ILE   B 137 ? 0.2193 0.1361 0.3825 -0.0066 -0.0096 -0.0013 137 ILE   B CB  
6050 C CG1 . ILE   B 137 ? 0.2399 0.1575 0.4273 0.0003  -0.0014 -0.0095 137 ILE   B CG1 
6051 C CG2 . ILE   B 137 ? 0.2215 0.1382 0.3988 -0.0291 -0.0155 -0.0002 137 ILE   B CG2 
6052 C CD1 . ILE   B 137 ? 0.2622 0.1895 0.4625 0.0133  -0.0042 -0.0009 137 ILE   B CD1 
6064 N N   . HIS   B 138 ? 0.1951 0.1369 0.3203 -0.0084 0.0183  0.0182  138 HIS   B N   
6065 C CA  . HIS   B 138 ? 0.2058 0.1444 0.3160 -0.0057 0.0329  0.0288  138 HIS   B CA  
6066 C C   . HIS   B 138 ? 0.1862 0.1411 0.3142 -0.0109 0.0255  0.0292  138 HIS   B C   
6067 O O   . HIS   B 138 ? 0.1730 0.1493 0.3433 -0.0095 0.0241  0.0334  138 HIS   B O   
6068 C CB  . HIS   B 138 ? 0.2324 0.1603 0.3202 -0.0131 0.0460  0.0219  138 HIS   B CB  
6069 C CG  . HIS   B 138 ? 0.2442 0.1734 0.3289 -0.0163 0.0598  0.0435  138 HIS   B CG  
6070 N ND1 . HIS   B 138 ? 0.2521 0.1955 0.3509 -0.0117 0.0698  0.0294  138 HIS   B ND1 
6071 C CD2 . HIS   B 138 ? 0.2589 0.1899 0.3190 -0.0129 0.0637  0.0345  138 HIS   B CD2 
6072 C CE1 . HIS   B 138 ? 0.2593 0.1966 0.3385 -0.0101 0.0672  0.0335  138 HIS   B CE1 
6073 N NE2 . HIS   B 138 ? 0.2658 0.1880 0.3228 -0.0053 0.0697  0.0317  138 HIS   B NE2 
6081 N N   . SER   B 139 ? 0.1856 0.1253 0.3141 -0.0009 0.0261  0.0113  139 SER   B N   
6082 C CA  . SER   B 139 ? 0.1799 0.1227 0.3005 -0.0070 0.0230  0.0054  139 SER   B CA  
6083 C C   . SER   B 139 ? 0.1619 0.1203 0.2976 -0.0090 0.0191  0.0042  139 SER   B C   
6084 O O   . SER   B 139 ? 0.1542 0.1201 0.3031 -0.0023 0.0056  0.0086  139 SER   B O   
6085 C CB  . SER   B 139 ? 0.1832 0.1300 0.3135 -0.0034 0.0069  -0.0001 139 SER   B CB  
6086 O OG  . SER   B 139 ? 0.1839 0.1265 0.3234 -0.0086 -0.0079 0.0167  139 SER   B OG  
6092 N N   . LEU   B 140 ? 0.1563 0.1157 0.2789 -0.0103 0.0133  -0.0017 140 LEU   B N   
6093 C CA  . LEU   B 140 ? 0.1554 0.1202 0.2892 -0.0070 0.0137  -0.0026 140 LEU   B CA  
6094 C C   . LEU   B 140 ? 0.1516 0.1168 0.3038 -0.0070 -0.0029 -0.0098 140 LEU   B C   
6095 O O   . LEU   B 140 ? 0.1421 0.1269 0.3008 -0.0032 0.0013  0.0009  140 LEU   B O   
6096 C CB  . LEU   B 140 ? 0.1486 0.1232 0.2866 -0.0144 0.0211  -0.0067 140 LEU   B CB  
6097 C CG  . LEU   B 140 ? 0.1635 0.1231 0.2852 -0.0163 -0.0003 0.0072  140 LEU   B CG  
6098 C CD1 . LEU   B 140 ? 0.1692 0.1317 0.2963 -0.0146 0.0096  0.0065  140 LEU   B CD1 
6099 C CD2 . LEU   B 140 ? 0.1845 0.1301 0.2927 -0.0144 -0.0062 -0.0143 140 LEU   B CD2 
6111 N N   . ARG   B 141 ? 0.1416 0.1157 0.3063 -0.0133 0.0000  -0.0084 141 ARG   B N   
6112 C CA  . ARG   B 141 ? 0.1442 0.1190 0.3440 -0.0173 0.0169  -0.0057 141 ARG   B CA  
6113 C C   . ARG   B 141 ? 0.1374 0.1235 0.3452 -0.0169 0.0097  -0.0055 141 ARG   B C   
6114 O O   . ARG   B 141 ? 0.1440 0.1278 0.3389 -0.0145 -0.0104 -0.0136 141 ARG   B O   
6115 C CB  . ARG   B 141 ? 0.1592 0.1322 0.3570 -0.0222 0.0229  -0.0034 141 ARG   B CB  
6116 C CG  . ARG   B 141 ? 0.1943 0.1579 0.3679 -0.0200 0.0266  0.0050  141 ARG   B CG  
6117 C CD  . ARG   B 141 ? 0.2363 0.1812 0.3656 -0.0121 0.0225  -0.0057 141 ARG   B CD  
6118 N NE  . ARG   B 141 ? 0.2563 0.1854 0.3619 -0.0347 0.0299  -0.0096 141 ARG   B NE  
6119 C CZ  . ARG   B 141 ? 0.2694 0.1741 0.3484 -0.0344 0.0335  -0.0284 141 ARG   B CZ  
6120 N NH1 . ARG   B 141 ? 0.2817 0.1614 0.3368 -0.0353 0.0248  -0.0278 141 ARG   B NH1 
6121 N NH2 . ARG   B 141 ? 0.2725 0.1834 0.3565 -0.0196 0.0260  -0.0255 141 ARG   B NH2 
6135 N N   . VAL   B 142 ? 0.1426 0.1215 0.3335 -0.0126 0.0110  -0.0063 142 VAL   B N   
6136 C CA  . VAL   B 142 ? 0.1406 0.1213 0.3142 -0.0089 0.0137  -0.0001 142 VAL   B CA  
6137 C C   . VAL   B 142 ? 0.1378 0.1183 0.3132 -0.0021 0.0043  -0.0071 142 VAL   B C   
6138 O O   . VAL   B 142 ? 0.1441 0.1187 0.3305 -0.0009 0.0108  -0.0041 142 VAL   B O   
6139 C CB  . VAL   B 142 ? 0.1502 0.1318 0.3114 -0.0067 0.0176  0.0074  142 VAL   B CB  
6140 C CG1 . VAL   B 142 ? 0.1526 0.1335 0.3118 0.0042  0.0306  0.0057  142 VAL   B CG1 
6141 C CG2 . VAL   B 142 ? 0.1676 0.1443 0.3102 -0.0049 0.0072  0.0101  142 VAL   B CG2 
6151 N N   . CYS   B 143 ? 0.1341 0.1238 0.3021 -0.0041 0.0005  0.0008  143 CYS   B N   
6152 C CA  . CYS   B 143 ? 0.1342 0.1173 0.3028 -0.0073 -0.0070 -0.0009 143 CYS   B CA  
6153 C C   . CYS   B 143 ? 0.1340 0.1213 0.3017 -0.0090 0.0006  0.0023  143 CYS   B C   
6154 O O   . CYS   B 143 ? 0.1398 0.1289 0.2952 -0.0090 -0.0028 -0.0070 143 CYS   B O   
6155 C CB  . CYS   B 143 ? 0.1423 0.1319 0.2991 -0.0128 -0.0048 -0.0029 143 CYS   B CB  
6156 S SG  . CYS   B 143 ? 0.1451 0.1461 0.2736 -0.0061 0.0005  0.0055  143 CYS   B SG  
6162 N N   . VAL   B 144 ? 0.1347 0.1232 0.3216 -0.0092 -0.0055 -0.0122 144 VAL   B N   
6163 C CA  . VAL   B 144 ? 0.1442 0.1352 0.3352 -0.0160 -0.0129 -0.0209 144 VAL   B CA  
6164 C C   . VAL   B 144 ? 0.1426 0.1378 0.3371 -0.0133 -0.0158 -0.0043 144 VAL   B C   
6165 O O   . VAL   B 144 ? 0.1525 0.1518 0.3513 -0.0063 -0.0206 0.0156  144 VAL   B O   
6166 C CB  . VAL   B 144 ? 0.1633 0.1534 0.3679 -0.0166 -0.0218 -0.0397 144 VAL   B CB  
6167 C CG1 . VAL   B 144 ? 0.1880 0.1934 0.3823 -0.0108 -0.0210 -0.0338 144 VAL   B CG1 
6168 C CG2 . VAL   B 144 ? 0.1795 0.1549 0.3547 0.0007  -0.0328 -0.0547 144 VAL   B CG2 
6178 N N   . ASP   B 145 ? 0.1395 0.1318 0.3407 -0.0075 -0.0038 -0.0185 145 ASP   B N   
6179 C CA  . ASP   B 145 ? 0.1427 0.1373 0.3560 -0.0098 0.0031  -0.0063 145 ASP   B CA  
6180 C C   . ASP   B 145 ? 0.1373 0.1399 0.3493 -0.0091 0.0009  -0.0129 145 ASP   B C   
6181 O O   . ASP   B 145 ? 0.1410 0.1508 0.3970 -0.0144 0.0087  -0.0264 145 ASP   B O   
6182 C CB  . ASP   B 145 ? 0.1552 0.1451 0.3970 -0.0154 0.0214  -0.0108 145 ASP   B CB  
6183 C CG  . ASP   B 145 ? 0.1676 0.1465 0.4335 -0.0259 0.0250  -0.0174 145 ASP   B CG  
6184 O OD1 . ASP   B 145 ? 0.1720 0.1431 0.4496 -0.0241 -0.0078 -0.0271 145 ASP   B OD1 
6185 O OD2 . ASP   B 145 ? 0.1991 0.1546 0.4735 -0.0320 0.0490  -0.0071 145 ASP   B OD2 
6190 N N   . THR   B 146 ? 0.1297 0.1286 0.3035 -0.0098 0.0005  -0.0009 146 THR   B N   
6191 C CA  . THR   B 146 ? 0.1373 0.1268 0.2835 -0.0131 0.0016  -0.0044 146 THR   B CA  
6192 C C   . THR   B 146 ? 0.1433 0.1255 0.2870 -0.0119 -0.0083 -0.0022 146 THR   B C   
6193 O O   . THR   B 146 ? 0.1467 0.1234 0.2955 -0.0078 -0.0101 0.0034  146 THR   B O   
6194 C CB  . THR   B 146 ? 0.1469 0.1274 0.2877 -0.0085 0.0137  -0.0044 146 THR   B CB  
6195 O OG1 . THR   B 146 ? 0.1468 0.1295 0.2974 -0.0124 0.0182  0.0113  146 THR   B OG1 
6196 C CG2 . THR   B 146 ? 0.1559 0.1276 0.2804 -0.0060 0.0142  -0.0067 146 THR   B CG2 
6204 N N   . VAL   B 147 ? 0.1395 0.1301 0.2674 -0.0097 -0.0049 0.0037  147 VAL   B N   
6205 C CA  . VAL   B 147 ? 0.1431 0.1237 0.2647 -0.0095 -0.0129 0.0000  147 VAL   B CA  
6206 C C   . VAL   B 147 ? 0.1387 0.1227 0.2705 -0.0210 -0.0152 0.0021  147 VAL   B C   
6207 O O   . VAL   B 147 ? 0.1525 0.1380 0.2783 -0.0244 -0.0352 -0.0087 147 VAL   B O   
6208 C CB  . VAL   B 147 ? 0.1491 0.1362 0.2487 -0.0096 -0.0076 -0.0020 147 VAL   B CB  
6209 C CG1 . VAL   B 147 ? 0.1476 0.1527 0.2327 -0.0181 0.0019  -0.0043 147 VAL   B CG1 
6210 C CG2 . VAL   B 147 ? 0.1563 0.1316 0.2525 -0.0121 0.0008  0.0005  147 VAL   B CG2 
6220 N N   . ARG   B 148 ? 0.1415 0.1280 0.2554 -0.0132 -0.0227 -0.0074 148 ARG   B N   
6221 C CA  . ARG   B 148 ? 0.1484 0.1433 0.2515 -0.0083 -0.0311 -0.0077 148 ARG   B CA  
6222 C C   . ARG   B 148 ? 0.1476 0.1471 0.2354 -0.0085 -0.0324 -0.0030 148 ARG   B C   
6223 O O   . ARG   B 148 ? 0.1716 0.1762 0.2491 -0.0243 -0.0396 0.0026  148 ARG   B O   
6224 C CB  . ARG   B 148 ? 0.1517 0.1465 0.2488 -0.0038 -0.0363 -0.0228 148 ARG   B CB  
6225 C CG  . ARG   B 148 ? 0.1511 0.1609 0.2611 -0.0096 -0.0360 -0.0388 148 ARG   B CG  
6226 C CD  . ARG   B 148 ? 0.1583 0.1796 0.2766 0.0076  -0.0325 -0.0412 148 ARG   B CD  
6227 N NE  . ARG   B 148 ? 0.1641 0.1780 0.2810 0.0227  -0.0318 -0.0362 148 ARG   B NE  
6228 C CZ  . ARG   B 148 ? 0.1549 0.1697 0.2516 0.0123  -0.0230 -0.0229 148 ARG   B CZ  
6229 N NH1 . ARG   B 148 ? 0.1507 0.1720 0.2562 -0.0041 -0.0067 -0.0182 148 ARG   B NH1 
6230 N NH2 . ARG   B 148 ? 0.1797 0.1535 0.2404 0.0174  -0.0260 -0.0139 148 ARG   B NH2 
6244 N N   . THR   B 149 ? 0.1556 0.1412 0.2401 -0.0119 -0.0275 0.0003  149 THR   B N   
6245 C CA  . THR   B 149 ? 0.1595 0.1454 0.2366 -0.0160 -0.0263 0.0005  149 THR   B CA  
6246 C C   . THR   B 149 ? 0.1562 0.1448 0.2347 -0.0168 -0.0312 0.0029  149 THR   B C   
6247 O O   . THR   B 149 ? 0.1604 0.1379 0.2382 -0.0236 -0.0176 -0.0001 149 THR   B O   
6248 C CB  . THR   B 149 ? 0.1612 0.1435 0.2481 -0.0161 -0.0347 -0.0036 149 THR   B CB  
6249 O OG1 . THR   B 149 ? 0.1596 0.1470 0.2460 -0.0244 -0.0408 -0.0025 149 THR   B OG1 
6250 C CG2 . THR   B 149 ? 0.1724 0.1418 0.2675 -0.0107 -0.0222 -0.0029 149 THR   B CG2 
6258 N N   . ASN   B 150 ? 0.1648 0.1444 0.2200 -0.0188 -0.0420 -0.0028 150 ASN   B N   
6259 C CA  . ASN   B 150 ? 0.1766 0.1535 0.2129 -0.0180 -0.0313 -0.0106 150 ASN   B CA  
6260 C C   . ASN   B 150 ? 0.1622 0.1497 0.2204 -0.0176 -0.0324 -0.0071 150 ASN   B C   
6261 O O   . ASN   B 150 ? 0.1685 0.1481 0.2451 -0.0300 -0.0459 -0.0034 150 ASN   B O   
6262 C CB  . ASN   B 150 ? 0.2004 0.1869 0.2176 -0.0228 -0.0378 0.0011  150 ASN   B CB  
6263 C CG  . ASN   B 150 ? 0.2223 0.2305 0.2517 -0.0255 -0.0419 0.0203  150 ASN   B CG  
6264 O OD1 . ASN   B 150 ? 0.2302 0.2509 0.2683 -0.0294 -0.0538 0.0221  150 ASN   B OD1 
6265 N ND2 . ASN   B 150 ? 0.2343 0.2489 0.2787 -0.0160 -0.0421 0.0524  150 ASN   B ND2 
6272 N N   . VAL   B 151 ? 0.1536 0.1488 0.2153 -0.0248 -0.0403 0.0031  151 VAL   B N   
6273 C CA  . VAL   B 151 ? 0.1563 0.1501 0.2229 -0.0266 -0.0277 0.0019  151 VAL   B CA  
6274 C C   . VAL   B 151 ? 0.1579 0.1378 0.2185 -0.0294 -0.0323 -0.0048 151 VAL   B C   
6275 O O   . VAL   B 151 ? 0.1717 0.1451 0.2390 -0.0323 -0.0256 -0.0128 151 VAL   B O   
6276 C CB  . VAL   B 151 ? 0.1781 0.1603 0.2410 -0.0111 -0.0313 0.0061  151 VAL   B CB  
6277 C CG1 . VAL   B 151 ? 0.1889 0.1636 0.2671 -0.0162 -0.0277 -0.0088 151 VAL   B CG1 
6278 C CG2 . VAL   B 151 ? 0.1889 0.1693 0.2260 0.0068  -0.0393 0.0118  151 VAL   B CG2 
6288 N N   . TYR   B 152 ? 0.1573 0.1251 0.2238 -0.0270 -0.0319 -0.0020 152 TYR   B N   
6289 C CA  . TYR   B 152 ? 0.1612 0.1403 0.2138 -0.0262 -0.0253 -0.0093 152 TYR   B CA  
6290 C C   . TYR   B 152 ? 0.1545 0.1290 0.2026 -0.0224 -0.0136 -0.0100 152 TYR   B C   
6291 O O   . TYR   B 152 ? 0.1607 0.1358 0.2099 -0.0304 -0.0132 -0.0046 152 TYR   B O   
6292 C CB  . TYR   B 152 ? 0.1771 0.1540 0.2007 -0.0303 -0.0207 0.0057  152 TYR   B CB  
6293 C CG  . TYR   B 152 ? 0.1947 0.1728 0.1965 -0.0404 -0.0288 0.0055  152 TYR   B CG  
6294 C CD1 . TYR   B 152 ? 0.2093 0.1823 0.1872 -0.0354 -0.0325 0.0137  152 TYR   B CD1 
6295 C CD2 . TYR   B 152 ? 0.2123 0.1877 0.1886 -0.0431 -0.0274 0.0020  152 TYR   B CD2 
6296 C CE1 . TYR   B 152 ? 0.2249 0.2000 0.2048 -0.0323 -0.0326 0.0241  152 TYR   B CE1 
6297 C CE2 . TYR   B 152 ? 0.2252 0.2089 0.1934 -0.0393 -0.0254 -0.0058 152 TYR   B CE2 
6298 C CZ  . TYR   B 152 ? 0.2255 0.2179 0.1932 -0.0367 -0.0512 0.0222  152 TYR   B CZ  
6299 O OH  . TYR   B 152 ? 0.2440 0.2511 0.2405 -0.0215 -0.0490 0.0315  152 TYR   B OH  
6309 N N   . LEU   B 153 ? 0.1543 0.1337 0.1977 -0.0303 -0.0212 -0.0028 153 LEU   B N   
6310 C CA  . LEU   B 153 ? 0.1555 0.1310 0.2064 -0.0225 -0.0203 -0.0085 153 LEU   B CA  
6311 C C   . LEU   B 153 ? 0.1602 0.1313 0.2201 -0.0239 -0.0183 -0.0184 153 LEU   B C   
6312 O O   . LEU   B 153 ? 0.1687 0.1536 0.2257 -0.0188 -0.0213 -0.0313 153 LEU   B O   
6313 C CB  . LEU   B 153 ? 0.1569 0.1261 0.2144 -0.0234 -0.0126 -0.0102 153 LEU   B CB  
6314 C CG  . LEU   B 153 ? 0.1542 0.1387 0.2570 -0.0270 -0.0072 0.0002  153 LEU   B CG  
6315 C CD1 . LEU   B 153 ? 0.1641 0.1533 0.2605 -0.0258 -0.0068 0.0061  153 LEU   B CD1 
6316 C CD2 . LEU   B 153 ? 0.1559 0.1510 0.2718 -0.0345 0.0078  0.0049  153 LEU   B CD2 
6328 N N   . ALA   B 154 ? 0.1526 0.1296 0.2273 -0.0091 -0.0224 -0.0157 154 ALA   B N   
6329 C CA  . ALA   B 154 ? 0.1602 0.1376 0.2552 -0.0033 -0.0168 -0.0199 154 ALA   B CA  
6330 C C   . ALA   B 154 ? 0.1723 0.1408 0.2584 -0.0017 -0.0211 -0.0326 154 ALA   B C   
6331 O O   . ALA   B 154 ? 0.2084 0.1397 0.2716 0.0033  -0.0163 -0.0120 154 ALA   B O   
6332 C CB  . ALA   B 154 ? 0.1550 0.1501 0.2821 -0.0048 -0.0072 -0.0273 154 ALA   B CB  
6338 N N   . VAL   B 155 ? 0.1422 0.1345 0.2663 -0.0072 -0.0016 -0.0213 155 VAL   B N   
6339 C CA  . VAL   B 155 ? 0.1385 0.1340 0.2952 -0.0036 -0.0105 -0.0048 155 VAL   B CA  
6340 C C   . VAL   B 155 ? 0.1402 0.1351 0.2874 -0.0041 -0.0163 -0.0187 155 VAL   B C   
6341 O O   . VAL   B 155 ? 0.1617 0.1553 0.3165 0.0040  -0.0175 -0.0389 155 VAL   B O   
6342 C CB  . VAL   B 155 ? 0.1447 0.1480 0.3223 -0.0086 -0.0191 0.0121  155 VAL   B CB  
6343 C CG1 . VAL   B 155 ? 0.1618 0.1439 0.3207 -0.0127 -0.0184 0.0109  155 VAL   B CG1 
6344 C CG2 . VAL   B 155 ? 0.1349 0.1677 0.3473 -0.0134 -0.0147 0.0313  155 VAL   B CG2 
6354 N N   . PHE   B 156 ? 0.1306 0.1421 0.3003 0.0033  -0.0134 -0.0163 156 PHE   B N   
6355 C CA  . PHE   B 156 ? 0.1374 0.1472 0.3277 0.0113  -0.0168 -0.0101 156 PHE   B CA  
6356 C C   . PHE   B 156 ? 0.1338 0.1646 0.3586 0.0121  -0.0178 -0.0266 156 PHE   B C   
6357 O O   . PHE   B 156 ? 0.1577 0.1835 0.3852 0.0224  -0.0129 -0.0430 156 PHE   B O   
6358 C CB  . PHE   B 156 ? 0.1506 0.1466 0.3336 0.0027  -0.0269 -0.0028 156 PHE   B CB  
6359 C CG  . PHE   B 156 ? 0.1490 0.1643 0.3406 -0.0036 -0.0236 0.0121  156 PHE   B CG  
6360 C CD1 . PHE   B 156 ? 0.1498 0.1873 0.3617 0.0079  -0.0171 0.0410  156 PHE   B CD1 
6361 C CD2 . PHE   B 156 ? 0.1535 0.1787 0.3440 0.0066  -0.0228 0.0152  156 PHE   B CD2 
6362 C CE1 . PHE   B 156 ? 0.1553 0.2033 0.3730 0.0064  -0.0117 0.0426  156 PHE   B CE1 
6363 C CE2 . PHE   B 156 ? 0.1579 0.1995 0.3714 0.0136  -0.0236 0.0073  156 PHE   B CE2 
6364 C CZ  . PHE   B 156 ? 0.1504 0.2019 0.3799 0.0178  -0.0287 0.0254  156 PHE   B CZ  
6374 N N   . ASP   B 157 ? 0.1441 0.1511 0.3645 0.0095  -0.0327 -0.0091 157 ASP   B N   
6375 C CA  . ASP   B 157 ? 0.1601 0.1560 0.3944 0.0091  -0.0299 -0.0252 157 ASP   B CA  
6376 C C   . ASP   B 157 ? 0.1587 0.1496 0.4120 0.0092  -0.0264 -0.0470 157 ASP   B C   
6377 O O   . ASP   B 157 ? 0.1469 0.1527 0.4098 0.0066  -0.0295 -0.0353 157 ASP   B O   
6378 C CB  . ASP   B 157 ? 0.1792 0.1751 0.3992 0.0046  -0.0497 -0.0109 157 ASP   B CB  
6379 C CG  . ASP   B 157 ? 0.2155 0.1905 0.4231 -0.0014 -0.0363 -0.0174 157 ASP   B CG  
6380 O OD1 . ASP   B 157 ? 0.2297 0.1808 0.4422 0.0120  -0.0362 -0.0203 157 ASP   B OD1 
6381 O OD2 . ASP   B 157 ? 0.2465 0.2097 0.4477 -0.0078 -0.0199 -0.0095 157 ASP   B OD2 
6386 N N   . LYS   B 158 ? 0.1638 0.1754 0.4231 0.0075  -0.0095 -0.0716 158 LYS   B N   
6387 C CA  . LYS   B 158 ? 0.1809 0.1985 0.4285 0.0018  -0.0039 -0.0914 158 LYS   B CA  
6388 C C   . LYS   B 158 ? 0.1761 0.1812 0.4362 0.0032  -0.0131 -0.0809 158 LYS   B C   
6389 O O   . LYS   B 158 ? 0.1759 0.1842 0.4391 -0.0062 -0.0016 -0.0822 158 LYS   B O   
6390 C CB  . LYS   B 158 ? 0.2111 0.2474 0.4248 0.0048  0.0075  -0.1080 158 LYS   B CB  
6391 C CG  . LYS   B 158 ? 0.2483 0.2879 0.4292 0.0056  0.0156  -0.1180 158 LYS   B CG  
6392 C CD  . LYS   B 158 ? 0.2735 0.3305 0.4374 0.0033  0.0224  -0.1143 158 LYS   B CD  
6393 C CE  . LYS   B 158 ? 0.2947 0.3577 0.4509 0.0066  0.0256  -0.1092 158 LYS   B CE  
6394 N NZ  . LYS   B 158 ? 0.2907 0.3688 0.4510 0.0067  0.0293  -0.1105 158 LYS   B NZ  
6408 N N   . ASN   B 159 ? 0.1804 0.1709 0.4578 0.0033  -0.0253 -0.0698 159 ASN   B N   
6409 C CA  . ASN   B 159 ? 0.1884 0.1650 0.4757 0.0162  -0.0367 -0.0489 159 ASN   B CA  
6410 C C   . ASN   B 159 ? 0.1724 0.1473 0.4704 0.0109  -0.0505 -0.0352 159 ASN   B C   
6411 O O   . ASN   B 159 ? 0.1745 0.1384 0.4951 -0.0033 -0.0619 -0.0270 159 ASN   B O   
6412 C CB  . ASN   B 159 ? 0.2131 0.1846 0.5036 0.0273  -0.0410 -0.0362 159 ASN   B CB  
6413 C CG  . ASN   B 159 ? 0.2464 0.2068 0.5183 0.0364  -0.0453 -0.0429 159 ASN   B CG  
6414 O OD1 . ASN   B 159 ? 0.2620 0.2097 0.5277 0.0438  -0.0485 -0.0495 159 ASN   B OD1 
6415 N ND2 . ASN   B 159 ? 0.2462 0.2155 0.5337 0.0416  -0.0415 -0.0420 159 ASN   B ND2 
6422 N N   . LEU   B 160 ? 0.1596 0.1476 0.4407 0.0031  -0.0479 -0.0346 160 LEU   B N   
6423 C CA  . LEU   B 160 ? 0.1553 0.1519 0.4050 0.0057  -0.0372 -0.0154 160 LEU   B CA  
6424 C C   . LEU   B 160 ? 0.1506 0.1404 0.4004 0.0013  -0.0283 -0.0258 160 LEU   B C   
6425 O O   . LEU   B 160 ? 0.1415 0.1448 0.4008 -0.0047 -0.0329 -0.0163 160 LEU   B O   
6426 C CB  . LEU   B 160 ? 0.1560 0.1628 0.3773 0.0019  -0.0404 -0.0059 160 LEU   B CB  
6427 C CG  . LEU   B 160 ? 0.1565 0.1825 0.3545 0.0049  -0.0347 -0.0043 160 LEU   B CG  
6428 C CD1 . LEU   B 160 ? 0.1733 0.1978 0.3559 -0.0026 -0.0261 0.0010  160 LEU   B CD1 
6429 C CD2 . LEU   B 160 ? 0.1644 0.1920 0.3447 0.0103  -0.0309 -0.0165 160 LEU   B CD2 
6441 N N   . TYR   B 161 ? 0.1513 0.1543 0.3959 -0.0079 -0.0112 -0.0401 161 TYR   B N   
6442 C CA  . TYR   B 161 ? 0.1612 0.1514 0.3774 -0.0185 0.0094  -0.0457 161 TYR   B CA  
6443 C C   . TYR   B 161 ? 0.1689 0.1521 0.3737 -0.0133 0.0157  -0.0426 161 TYR   B C   
6444 O O   . TYR   B 161 ? 0.1735 0.1525 0.3656 -0.0161 0.0011  -0.0424 161 TYR   B O   
6445 C CB  . TYR   B 161 ? 0.1786 0.1653 0.3638 -0.0281 0.0219  -0.0583 161 TYR   B CB  
6446 C CG  . TYR   B 161 ? 0.2092 0.1684 0.3467 -0.0358 0.0323  -0.0706 161 TYR   B CG  
6447 C CD1 . TYR   B 161 ? 0.2178 0.1652 0.3421 -0.0475 0.0405  -0.0650 161 TYR   B CD1 
6448 C CD2 . TYR   B 161 ? 0.2340 0.1782 0.3439 -0.0332 0.0281  -0.0606 161 TYR   B CD2 
6449 C CE1 . TYR   B 161 ? 0.2316 0.1898 0.3379 -0.0519 0.0358  -0.0651 161 TYR   B CE1 
6450 C CE2 . TYR   B 161 ? 0.2494 0.2003 0.3371 -0.0359 0.0340  -0.0547 161 TYR   B CE2 
6451 C CZ  . TYR   B 161 ? 0.2501 0.2019 0.3303 -0.0565 0.0292  -0.0491 161 TYR   B CZ  
6452 O OH  . TYR   B 161 ? 0.2840 0.2239 0.3525 -0.0586 0.0298  -0.0456 161 TYR   B OH  
6462 N N   . ASP   B 162 ? 0.1679 0.1480 0.3784 -0.0170 0.0006  -0.0571 162 ASP   B N   
6463 C CA  . ASP   B 162 ? 0.1764 0.1583 0.3824 -0.0097 -0.0096 -0.0525 162 ASP   B CA  
6464 C C   . ASP   B 162 ? 0.1717 0.1462 0.3721 -0.0135 -0.0136 -0.0345 162 ASP   B C   
6465 O O   . ASP   B 162 ? 0.1799 0.1516 0.3899 -0.0200 -0.0294 -0.0352 162 ASP   B O   
6466 C CB  . ASP   B 162 ? 0.1954 0.1792 0.4030 -0.0002 -0.0122 -0.0731 162 ASP   B CB  
6467 C CG  . ASP   B 162 ? 0.2006 0.2063 0.4303 0.0091  -0.0117 -0.0795 162 ASP   B CG  
6468 O OD1 . ASP   B 162 ? 0.2015 0.2247 0.4331 0.0042  -0.0066 -0.0831 162 ASP   B OD1 
6469 O OD2 . ASP   B 162 ? 0.2126 0.2240 0.4550 0.0209  0.0004  -0.0793 162 ASP   B OD2 
6474 N N   A LYS   B 163 ? 0.1690 0.1354 0.3583 -0.0174 -0.0310 -0.0280 163 LYS   B N   
6475 N N   B LYS   B 163 ? 0.1740 0.1491 0.3576 -0.0157 -0.0260 -0.0240 163 LYS   B N   
6476 C CA  A LYS   B 163 ? 0.1843 0.1418 0.3623 -0.0205 -0.0192 -0.0144 163 LYS   B CA  
6477 C CA  B LYS   B 163 ? 0.1855 0.1599 0.3568 -0.0181 -0.0199 -0.0104 163 LYS   B CA  
6478 C C   A LYS   B 163 ? 0.1554 0.1376 0.3559 -0.0220 -0.0181 -0.0004 163 LYS   B C   
6479 C C   B LYS   B 163 ? 0.1594 0.1466 0.3496 -0.0192 -0.0204 0.0008  163 LYS   B C   
6480 O O   A LYS   B 163 ? 0.1478 0.1504 0.3688 -0.0253 -0.0162 -0.0037 163 LYS   B O   
6481 O O   B LYS   B 163 ? 0.1543 0.1545 0.3558 -0.0205 -0.0209 0.0025  163 LYS   B O   
6482 C CB  A LYS   B 163 ? 0.2330 0.1672 0.3840 -0.0156 -0.0217 -0.0114 163 LYS   B CB  
6483 C CB  B LYS   B 163 ? 0.2246 0.1911 0.3755 -0.0164 -0.0212 -0.0071 163 LYS   B CB  
6484 C CG  A LYS   B 163 ? 0.2913 0.2281 0.4131 -0.0177 -0.0129 -0.0102 163 LYS   B CG  
6485 C CG  B LYS   B 163 ? 0.2701 0.2413 0.4001 -0.0186 -0.0156 -0.0048 163 LYS   B CG  
6486 C CD  A LYS   B 163 ? 0.3346 0.2670 0.4435 -0.0243 -0.0066 -0.0202 163 LYS   B CD  
6487 C CD  B LYS   B 163 ? 0.3034 0.2759 0.4285 -0.0232 -0.0111 -0.0086 163 LYS   B CD  
6488 C CE  A LYS   B 163 ? 0.3631 0.2896 0.4670 -0.0275 -0.0006 -0.0229 163 LYS   B CE  
6489 C CE  B LYS   B 163 ? 0.3253 0.2926 0.4521 -0.0262 -0.0063 -0.0100 163 LYS   B CE  
6490 N NZ  A LYS   B 163 ? 0.3952 0.3112 0.4805 -0.0306 -0.0004 -0.0282 163 LYS   B NZ  
6491 N NZ  B LYS   B 163 ? 0.3359 0.3052 0.4658 -0.0283 -0.0061 -0.0121 163 LYS   B NZ  
6518 N N   . LEU   B 164 ? 0.1454 0.1316 0.3466 -0.0180 -0.0215 -0.0009 164 LEU   B N   
6519 C CA  . LEU   B 164 ? 0.1502 0.1326 0.3283 -0.0122 -0.0218 -0.0037 164 LEU   B CA  
6520 C C   . LEU   B 164 ? 0.1575 0.1336 0.3360 -0.0117 -0.0302 -0.0062 164 LEU   B C   
6521 O O   . LEU   B 164 ? 0.1533 0.1571 0.3592 -0.0152 -0.0358 -0.0051 164 LEU   B O   
6522 C CB  . LEU   B 164 ? 0.1475 0.1288 0.3055 -0.0107 -0.0232 0.0004  164 LEU   B CB  
6523 C CG  . LEU   B 164 ? 0.1553 0.1466 0.3086 -0.0102 -0.0133 0.0051  164 LEU   B CG  
6524 C CD1 . LEU   B 164 ? 0.1583 0.1495 0.2997 -0.0145 -0.0291 -0.0048 164 LEU   B CD1 
6525 C CD2 . LEU   B 164 ? 0.1691 0.1808 0.3233 -0.0078 0.0142  -0.0074 164 LEU   B CD2 
6538 N N   . VAL   B 165 ? 0.1911 0.1467 0.3439 -0.0235 -0.0431 -0.0146 165 VAL   B N   
6539 C CA  . VAL   B 165 ? 0.2257 0.1566 0.3497 -0.0319 -0.0578 -0.0136 165 VAL   B CA  
6540 C C   . VAL   B 165 ? 0.2511 0.1687 0.3742 -0.0409 -0.0858 -0.0127 165 VAL   B C   
6541 O O   . VAL   B 165 ? 0.2718 0.1867 0.3915 -0.0489 -0.0818 0.0013  165 VAL   B O   
6542 C CB  . VAL   B 165 ? 0.2514 0.1782 0.3517 -0.0201 -0.0249 -0.0181 165 VAL   B CB  
6543 C CG1 . VAL   B 165 ? 0.2662 0.1904 0.3708 -0.0221 -0.0108 -0.0196 165 VAL   B CG1 
6544 C CG2 . VAL   B 165 ? 0.2501 0.1795 0.3385 -0.0157 -0.0174 -0.0165 165 VAL   B CG2 
6554 N N   . SER   B 166 ? 0.2585 0.1549 0.4093 -0.0339 -0.0934 -0.0347 166 SER   B N   
6555 C CA  . SER   B 166 ? 0.2533 0.1606 0.4492 -0.0334 -0.0738 -0.0446 166 SER   B CA  
6556 C C   . SER   B 166 ? 0.2393 0.1728 0.4608 -0.0342 -0.0722 -0.0174 166 SER   B C   
6557 O O   . SER   B 166 ? 0.2467 0.1905 0.4800 -0.0481 -0.0896 -0.0401 166 SER   B O   
6558 C CB  . SER   B 166 ? 0.2511 0.1681 0.4741 -0.0260 -0.0554 -0.0494 166 SER   B CB  
6559 O OG  . SER   B 166 ? 0.2317 0.1641 0.4915 -0.0257 -0.0613 -0.0336 166 SER   B OG  
6565 N N   . SER   B 167 ? 0.2120 0.1630 0.4345 -0.0409 -0.0708 0.0161  167 SER   B N   
6566 C CA  . SER   B 167 ? 0.2059 0.1709 0.4160 -0.0325 -0.0524 0.0235  167 SER   B CA  
6567 C C   . SER   B 167 ? 0.1980 0.1802 0.3985 -0.0433 -0.0528 0.0334  167 SER   B C   
6568 O O   . SER   B 167 ? 0.1960 0.1943 0.4017 -0.0447 -0.0536 0.0345  167 SER   B O   
6569 C CB  . SER   B 167 ? 0.1983 0.1748 0.4204 -0.0321 -0.0377 0.0179  167 SER   B CB  
6570 O OG  . SER   B 167 ? 0.1870 0.1857 0.4132 -0.0221 -0.0236 0.0151  167 SER   B OG  
6576 N N   . PHE   B 168 ? 0.1954 0.1830 0.3921 -0.0432 -0.0404 0.0432  168 PHE   B N   
6577 C CA  . PHE   B 168 ? 0.1971 0.1808 0.3622 -0.0492 -0.0345 0.0300  168 PHE   B CA  
6578 C C   . PHE   B 168 ? 0.1731 0.1705 0.3229 -0.0269 -0.0149 0.0146  168 PHE   B C   
6579 O O   . PHE   B 168 ? 0.2012 0.1552 0.3314 -0.0080 -0.0154 -0.0088 168 PHE   B O   
6580 C CB  . PHE   B 168 ? 0.2164 0.1825 0.3633 -0.0532 -0.0439 0.0387  168 PHE   B CB  
6581 C CG  . PHE   B 168 ? 0.2376 0.1704 0.3382 -0.0531 -0.0462 0.0123  168 PHE   B CG  
6582 C CD1 . PHE   B 168 ? 0.2685 0.1731 0.3497 -0.0490 -0.0434 0.0139  168 PHE   B CD1 
6583 C CD2 . PHE   B 168 ? 0.2304 0.1706 0.3225 -0.0521 -0.0496 0.0096  168 PHE   B CD2 
6584 C CE1 . PHE   B 168 ? 0.2803 0.1840 0.3352 -0.0385 -0.0358 0.0207  168 PHE   B CE1 
6585 C CE2 . PHE   B 168 ? 0.2558 0.1753 0.3260 -0.0356 -0.0542 0.0081  168 PHE   B CE2 
6586 C CZ  . PHE   B 168 ? 0.2688 0.1742 0.3321 -0.0257 -0.0530 0.0187  168 PHE   B CZ  
6596 N N   . LEU   B 169 ? 0.1830 0.1875 0.3163 -0.0015 -0.0016 0.0124  169 LEU   B N   
6597 C CA  . LEU   B 169 ? 0.2043 0.2150 0.3320 -0.0023 0.0009  -0.0223 169 LEU   B CA  
6598 C C   . LEU   B 169 ? 0.2314 0.2344 0.3706 0.0107  -0.0018 -0.0453 169 LEU   B C   
6599 O O   . LEU   B 169 ? 0.2539 0.2517 0.4133 0.0061  -0.0021 -0.0640 169 LEU   B O   
6600 C CB  . LEU   B 169 ? 0.2194 0.2586 0.3287 -0.0150 -0.0059 -0.0065 169 LEU   B CB  
6601 C CG  . LEU   B 169 ? 0.2589 0.3004 0.3502 -0.0054 -0.0014 -0.0024 169 LEU   B CG  
6602 C CD1 . LEU   B 169 ? 0.2792 0.3207 0.3514 -0.0046 0.0025  0.0080  169 LEU   B CD1 
6603 C CD2 . LEU   B 169 ? 0.2481 0.3107 0.3434 0.0085  0.0163  -0.0160 169 LEU   B CD2 
6604 O OXT . LEU   B 169 ? 0.2534 0.2485 0.3669 0.0355  0.0027  -0.0379 169 LEU   B OXT 
6616 C C1  T TFA   C .   ? 0.1224 0.1447 0.1158 0.0023  0.0179  0.0152  201 TFA   A C1  
6617 C C2  T TFA   C .   ? 0.1408 0.1652 0.1398 -0.0125 0.0189  0.0014  201 TFA   A C2  
6618 O O   T TFA   C .   ? 0.1017 0.1294 0.1158 -0.0012 0.0305  0.0243  201 TFA   A O   
6619 F F1  T TFA   C .   ? 0.1500 0.1682 0.1582 -0.0160 0.0102  -0.0047 201 TFA   A F1  
6620 F F2  T TFA   C .   ? 0.1496 0.1753 0.1315 -0.0135 0.0354  0.0108  201 TFA   A F2  
6621 F F3  T TFA   C .   ? 0.1510 0.1782 0.1712 -0.0212 0.0305  -0.0013 201 TFA   A F3  
6622 O OXT T TFA   C .   ? 0.1214 0.1411 0.1164 0.0269  0.0170  0.0190  201 TFA   A OXT 
6623 N N2  B A1A8J D .   ? 0.1320 0.1394 0.1580 0.0017  0.0118  0.0157  202 A1A8J A N2  
6624 C C3  B A1A8J D .   ? 0.1518 0.1588 0.1794 -0.0119 0.0030  0.0304  202 A1A8J A C3  
6625 C C6  B A1A8J D .   ? 0.1351 0.1353 0.1541 0.0038  0.0135  0.0225  202 A1A8J A C6  
6626 C C9  B A1A8J D .   ? 0.1320 0.1389 0.1767 0.0024  0.0163  0.0125  202 A1A8J A C9  
6627 C C12 B A1A8J D .   ? 0.1593 0.1957 0.1917 -0.0370 0.0223  0.0199  202 A1A8J A C12 
6628 C C14 B A1A8J D .   ? 0.1791 0.2307 0.2160 -0.0365 0.0237  0.0129  202 A1A8J A C14 
6629 C C17 B A1A8J D .   ? 0.1747 0.2342 0.2132 -0.0355 0.0012  0.0380  202 A1A8J A C17 
6630 C C19 B A1A8J D .   ? 0.1556 0.1978 0.1853 -0.0231 0.0065  0.0210  202 A1A8J A C19 
6631 C C1  B A1A8J D .   ? 0.1471 0.1740 0.1826 -0.0182 0.0137  0.0167  202 A1A8J A C1  
6632 C C10 B A1A8J D .   ? 0.1428 0.1386 0.1983 -0.0028 0.0156  0.0275  202 A1A8J A C10 
6633 C C11 B A1A8J D .   ? 0.1321 0.1348 0.1968 -0.0054 0.0078  0.0165  202 A1A8J A C11 
6634 C C13 B A1A8J D .   ? 0.1638 0.2161 0.1976 -0.0440 0.0180  0.0202  202 A1A8J A C13 
6635 C C15 B A1A8J D .   ? 0.1897 0.2390 0.2250 -0.0324 0.0174  0.0206  202 A1A8J A C15 
6636 C C16 B A1A8J D .   ? 0.1894 0.2391 0.2226 -0.0305 0.0078  0.0292  202 A1A8J A C16 
6637 C C18 B A1A8J D .   ? 0.1677 0.2176 0.1959 -0.0354 0.0086  0.0288  202 A1A8J A C18 
6638 C C2  B A1A8J D .   ? 0.1437 0.1584 0.1672 -0.0110 0.0172  0.0194  202 A1A8J A C2  
6639 C C4  B A1A8J D .   ? 0.1521 0.1524 0.1793 -0.0080 -0.0075 0.0405  202 A1A8J A C4  
6640 C C5  B A1A8J D .   ? 0.1491 0.1375 0.1709 0.0068  0.0323  0.0396  202 A1A8J A C5  
6641 C C7  B A1A8J D .   ? 0.1362 0.1512 0.1637 0.0044  0.0075  0.0036  202 A1A8J A C7  
6642 C C8  B A1A8J D .   ? 0.1365 0.1481 0.1766 0.0031  0.0074  0.0018  202 A1A8J A C8  
6643 N N1  B A1A8J D .   ? 0.1405 0.1412 0.1587 0.0001  0.0139  0.0339  202 A1A8J A N1  
6644 N N3  B A1A8J D .   ? 0.1487 0.1545 0.1649 -0.0021 0.0217  0.0032  202 A1A8J A N3  
6645 N N4  B A1A8J D .   ? 0.1332 0.1439 0.1953 -0.0026 0.0086  0.0069  202 A1A8J A N4  
6646 O O1  B A1A8J D .   ? 0.1399 0.1485 0.1901 -0.0071 0.0243  0.0053  202 A1A8J A O1  
6667 O O   . HOH   E .   ? 0.4634 0.8793 0.5444 -0.1221 0.0804  0.0862  301 HOH   A O   
6668 O O   . HOH   E .   ? 0.6503 0.4779 0.3297 0.2140  -0.1353 0.0122  302 HOH   A O   
6669 O O   . HOH   E .   ? 0.4743 0.3587 0.5060 -0.0278 0.1229  -0.0589 303 HOH   A O   
6670 O O   . HOH   E .   ? 0.2064 0.3648 0.3960 -0.0367 0.0332  -0.1037 304 HOH   A O   
6671 O O   A HOH   E .   ? 0.2439 0.2518 0.3245 -0.0094 -0.0439 0.0431  305 HOH   A O   
6672 O O   . HOH   E .   ? 0.6449 0.3759 0.4976 -0.1032 0.1799  0.0645  306 HOH   A O   
6673 O O   . HOH   E .   ? 0.5094 0.5532 0.3862 -0.1129 0.1745  0.0803  307 HOH   A O   
6674 O O   . HOH   E .   ? 0.2965 0.3543 0.2215 -0.0078 0.0419  0.0669  308 HOH   A O   
6675 O O   B HOH   E .   ? 0.4338 0.1727 0.2783 -0.0431 -0.0101 0.0286  309 HOH   A O   
6676 O O   B HOH   E .   ? 0.4784 0.4953 0.3817 0.0773  0.0405  -0.1097 310 HOH   A O   
6677 O O   . HOH   E .   ? 0.4631 0.5678 0.4568 0.0982  0.0933  -0.1196 311 HOH   A O   
6678 O O   . HOH   E .   ? 0.2308 0.1830 0.2926 0.0274  -0.0361 0.0216  312 HOH   A O   
6679 O O   . HOH   E .   ? 0.2174 0.2059 0.3976 -0.0511 0.0212  -0.0238 313 HOH   A O   
6680 O O   . HOH   E .   ? 0.2746 0.3767 0.4268 0.0102  -0.0625 0.0256  314 HOH   A O   
6681 O O   . HOH   E .   ? 0.5963 0.5583 0.3472 0.0291  -0.0289 0.1072  315 HOH   A O   
6682 O O   . HOH   E .   ? 0.6764 0.5113 0.7375 0.1149  0.0157  -0.0107 316 HOH   A O   
6683 O O   . HOH   E .   ? 0.7657 0.7452 0.5110 0.1043  -0.1356 0.0814  317 HOH   A O   
6684 O O   . HOH   E .   ? 0.3982 0.3183 0.3448 -0.1248 -0.0084 -0.0310 318 HOH   A O   
6685 O O   . HOH   E .   ? 0.3151 0.3133 0.3046 -0.0971 0.0121  0.0790  319 HOH   A O   
6686 O O   B HOH   E .   ? 0.3511 0.2445 0.1908 -0.0938 -0.0050 0.0268  320 HOH   A O   
6687 O O   A HOH   E .   ? 0.4289 0.6088 0.4152 -0.0882 -0.0678 -0.0576 321 HOH   A O   
6688 O O   . HOH   E .   ? 0.1884 0.2732 0.3372 0.0250  -0.0136 -0.0211 322 HOH   A O   
6689 O O   . HOH   E .   ? 0.5107 0.5012 0.4481 -0.0462 0.0960  0.2062  323 HOH   A O   
6690 O O   . HOH   E .   ? 0.5621 0.2221 0.5004 0.0787  -0.0355 -0.0099 324 HOH   A O   
6691 O O   . HOH   E .   ? 0.3155 0.4769 0.2525 0.0051  0.0411  0.0467  325 HOH   A O   
6692 O O   . HOH   E .   ? 0.2085 0.2485 0.2572 -0.0103 0.0385  0.0523  326 HOH   A O   
6693 O O   B HOH   E .   ? 0.1729 0.1372 0.1664 0.0100  -0.0111 0.0340  327 HOH   A O   
6694 O O   B HOH   E .   ? 0.3706 0.3566 0.4259 0.1874  -0.0722 0.0188  328 HOH   A O   
6695 O O   A HOH   E .   ? 0.2178 0.4358 0.4390 0.0502  0.0438  0.0533  329 HOH   A O   
6696 O O   . HOH   E .   ? 0.1598 0.1529 0.2770 -0.0227 0.0040  0.0028  330 HOH   A O   
6697 O O   . HOH   E .   ? 0.6194 0.4556 0.4576 -0.1405 0.0489  0.1541  331 HOH   A O   
6698 O O   . HOH   E .   ? 0.5757 0.4010 0.4156 -0.2188 -0.1032 0.1739  332 HOH   A O   
6699 O O   . HOH   E .   ? 0.2474 0.3515 0.5469 0.0083  0.1261  0.1851  333 HOH   A O   
6700 O O   . HOH   E .   ? 0.2531 0.2378 0.3140 0.0307  0.0276  0.0508  334 HOH   A O   
6701 O O   . HOH   E .   ? 0.3650 0.3528 0.4694 -0.0864 0.1462  0.0428  335 HOH   A O   
6702 O O   . HOH   E .   ? 0.2407 0.4268 0.3799 0.0964  -0.0540 0.0013  336 HOH   A O   
6703 O O   A HOH   E .   ? 0.1610 0.1591 0.1935 0.0354  0.0367  0.0617  337 HOH   A O   
6704 O O   . HOH   E .   ? 0.5354 0.3254 0.3850 -0.0589 -0.0288 -0.0637 338 HOH   A O   
6705 O O   . HOH   E .   ? 0.2231 0.5348 0.4137 -0.0178 -0.0629 0.1748  339 HOH   A O   
6706 O O   . HOH   E .   ? 0.6007 0.7097 0.4435 0.2556  -0.0457 -0.0380 340 HOH   A O   
6707 O O   . HOH   E .   ? 0.3019 0.2435 0.2863 -0.0634 0.0170  -0.0210 341 HOH   A O   
6708 O O   . HOH   E .   ? 0.5114 0.1992 0.4706 0.0231  -0.0977 0.0573  342 HOH   A O   
6709 O O   . HOH   E .   ? 0.2041 0.2018 0.3978 0.0088  0.1012  -0.0061 343 HOH   A O   
6710 O O   B HOH   E .   ? 0.1571 0.1268 0.2395 -0.0019 0.0167  0.0683  344 HOH   A O   
6711 O O   . HOH   E .   ? 0.1528 0.2253 0.2690 -0.0025 -0.0121 0.0490  345 HOH   A O   
6712 O O   A HOH   E .   ? 0.2042 0.3538 0.2133 0.0766  0.0220  0.0361  346 HOH   A O   
6713 O O   . HOH   E .   ? 0.2970 0.2845 0.4579 -0.0557 -0.0873 -0.0566 347 HOH   A O   
6714 O O   A HOH   E .   ? 0.2362 0.1776 0.2818 -0.0060 -0.0367 -0.0069 348 HOH   A O   
6715 O O   . HOH   E .   ? 0.2984 0.3389 0.5070 -0.0628 -0.0930 -0.0720 349 HOH   A O   
6716 O O   . HOH   E .   ? 0.4227 0.7588 0.5150 -0.0785 -0.1542 0.0599  350 HOH   A O   
6717 O O   . HOH   E .   ? 0.1833 0.1849 0.2630 0.0178  -0.0241 0.0248  351 HOH   A O   
6718 O O   A HOH   E .   ? 0.2879 0.2166 0.3344 -0.0235 -0.0985 0.0795  352 HOH   A O   
6719 O O   . HOH   E .   ? 0.2050 0.2506 0.2489 -0.0379 -0.0164 0.0815  353 HOH   A O   
6720 O O   . HOH   E .   ? 0.4079 0.2193 0.2826 0.1158  0.0673  0.0272  354 HOH   A O   
6721 O O   . HOH   E .   ? 0.5685 0.4689 0.5247 0.0976  0.1927  -0.0708 355 HOH   A O   
6722 O O   . HOH   E .   ? 0.4868 0.2640 0.4438 -0.1492 0.1820  -0.0460 356 HOH   A O   
6723 O O   . HOH   E .   ? 0.4181 0.4360 0.3893 0.2242  0.0932  0.0489  357 HOH   A O   
6724 O O   . HOH   E .   ? 0.2279 0.2833 0.3766 0.0434  0.0764  -0.0558 358 HOH   A O   
6725 O O   . HOH   E .   ? 0.4224 0.2713 0.4736 -0.1454 0.0874  0.0450  359 HOH   A O   
6726 O O   . HOH   E .   ? 0.2684 0.4081 0.3776 -0.0423 0.0605  -0.0095 360 HOH   A O   
6727 O O   A HOH   E .   ? 0.1222 0.3739 0.2412 -0.0085 0.0235  0.0458  361 HOH   A O   
6728 O O   . HOH   E .   ? 0.2744 0.3957 0.3180 0.0630  0.0768  0.1669  362 HOH   A O   
6729 O O   . HOH   E .   ? 0.3235 0.3892 0.2640 -0.1139 -0.0139 -0.0678 363 HOH   A O   
6730 O O   . HOH   E .   ? 0.1575 0.1890 0.3070 0.0035  -0.0097 0.0139  364 HOH   A O   
6731 O O   . HOH   E .   ? 0.1427 0.1340 0.1821 -0.0074 0.0151  0.0102  365 HOH   A O   
6732 O O   A HOH   E .   ? 0.3455 0.1964 0.2361 0.0583  0.0067  -0.0123 366 HOH   A O   
6733 O O   . HOH   E .   ? 0.8218 0.4532 0.6372 -0.1030 -0.1370 -0.0243 367 HOH   A O   
6734 O O   . HOH   E .   ? 0.1568 0.1376 0.2767 -0.0123 0.0220  -0.0129 368 HOH   A O   
6735 O O   . HOH   E .   ? 0.5876 0.5328 0.5973 -0.0443 -0.0140 0.1284  369 HOH   A O   
6736 O O   . HOH   E .   ? 0.3279 0.7601 0.3374 0.1471  0.0666  -0.1019 370 HOH   A O   
6737 O O   . HOH   E .   ? 0.6395 0.5969 0.4601 -0.0961 -0.1092 -0.0791 371 HOH   A O   
6738 O O   . HOH   E .   ? 0.3377 0.2839 0.2557 0.0369  0.1006  0.0104  372 HOH   A O   
6739 O O   . HOH   E .   ? 0.1486 0.1578 0.1954 -0.0069 -0.0112 -0.0034 373 HOH   A O   
6740 O O   . HOH   E .   ? 0.6615 0.4507 0.3209 0.0241  -0.0241 0.1738  374 HOH   A O   
6741 O O   A HOH   E .   ? 0.1329 0.1692 0.2711 0.0177  -0.0260 -0.0590 375 HOH   A O   
6742 O O   . HOH   E .   ? 0.1872 0.1890 0.2901 -0.0368 0.0029  0.0285  376 HOH   A O   
6743 O O   . HOH   E .   ? 0.1415 0.1451 0.2347 -0.0025 -0.0081 0.0089  377 HOH   A O   
6744 O O   . HOH   E .   ? 0.1861 0.2780 0.3122 0.0302  0.0330  0.0955  378 HOH   A O   
6745 O O   . HOH   E .   ? 0.3176 0.3841 0.3343 -0.1448 0.0722  -0.0097 379 HOH   A O   
6746 O O   . HOH   E .   ? 0.2072 0.2559 0.2528 -0.0378 -0.0427 0.0512  380 HOH   A O   
6747 O O   . HOH   E .   ? 0.1761 0.1754 0.3078 -0.0227 0.0123  0.0405  381 HOH   A O   
6748 O O   . HOH   E .   ? 0.2335 0.3630 0.3511 -0.0202 0.0055  0.0494  382 HOH   A O   
6749 O O   . HOH   E .   ? 0.2251 0.2525 0.4120 -0.0104 -0.0792 0.0276  383 HOH   A O   
6750 O O   . HOH   E .   ? 0.1724 0.1367 0.2267 -0.0194 0.0114  -0.0005 384 HOH   A O   
6751 O O   . HOH   E .   ? 0.4073 0.6253 0.4027 -0.1085 0.0463  0.1242  385 HOH   A O   
6752 O O   . HOH   E .   ? 0.3777 0.2792 0.5154 -0.0783 -0.0005 0.0288  386 HOH   A O   
6753 O O   . HOH   E .   ? 0.2677 0.2193 0.2172 -0.0684 -0.0005 0.0418  387 HOH   A O   
6754 O O   . HOH   E .   ? 0.2694 0.1931 0.3110 -0.0182 0.0004  0.0231  388 HOH   A O   
6755 O O   B HOH   E .   ? 0.3293 0.2463 0.2308 -0.0700 -0.0830 0.0892  389 HOH   A O   
6756 O O   . HOH   E .   ? 0.3101 0.4116 0.5406 -0.0743 0.0976  -0.0056 390 HOH   A O   
6757 O O   . HOH   E .   ? 0.1820 0.1970 0.4097 0.0238  0.0712  0.0931  391 HOH   A O   
6758 O O   T HOH   E .   ? 0.0992 0.0984 0.2018 -0.0186 -0.0036 0.0477  392 HOH   A O   
6759 O O   . HOH   E .   ? 0.2953 0.3557 0.3835 -0.0285 0.1207  -0.0750 393 HOH   A O   
6760 O O   . HOH   E .   ? 0.2034 0.1977 0.2335 0.0012  0.0070  0.0119  394 HOH   A O   
6761 O O   A HOH   E .   ? 0.2136 0.2290 0.3036 -0.0415 0.0537  -0.0106 395 HOH   A O   
6762 O O   A HOH   E .   ? 0.4220 0.2333 0.2817 0.0741  0.0644  0.0630  396 HOH   A O   
6763 O O   A HOH   E .   ? 0.2873 0.6532 0.4734 -0.0336 -0.0753 0.0455  397 HOH   A O   
6764 O O   . HOH   E .   ? 0.3080 0.2638 0.2520 -0.0745 -0.0782 0.0326  398 HOH   A O   
6765 O O   . HOH   E .   ? 0.4918 0.4382 0.2354 -0.0850 0.0863  0.0390  399 HOH   A O   
6766 O O   . HOH   E .   ? 0.6031 0.3029 0.4604 0.0955  -0.0323 -0.0347 400 HOH   A O   
6767 O O   . HOH   E .   ? 0.1752 0.2449 0.3062 -0.0138 0.0582  0.0634  401 HOH   A O   
6768 O O   . HOH   E .   ? 0.2548 0.3509 0.2932 -0.0354 0.0843  -0.0393 402 HOH   A O   
6769 O O   A HOH   E .   ? 0.1459 0.1564 0.1768 0.0298  -0.0341 0.0056  403 HOH   A O   
6770 O O   . HOH   E .   ? 0.1523 0.1743 0.3629 -0.0106 -0.0011 0.0170  404 HOH   A O   
6771 O O   . HOH   E .   ? 0.3439 0.2855 0.3468 -0.0003 -0.0280 0.1045  405 HOH   A O   
6772 O O   . HOH   E .   ? 0.5232 0.6551 0.5125 0.1026  -0.0859 0.1490  406 HOH   A O   
6773 O O   . HOH   E .   ? 0.5699 0.3835 0.6238 0.1171  0.1876  -0.1015 407 HOH   A O   
6774 O O   . HOH   E .   ? 0.2406 0.2101 0.3069 -0.0544 -0.0072 0.0680  408 HOH   A O   
6775 O O   . HOH   E .   ? 0.2797 0.3833 0.7068 -0.0382 0.0828  -0.0553 409 HOH   A O   
6776 O O   . HOH   E .   ? 0.2089 0.1875 0.3574 -0.0110 -0.0236 0.0088  410 HOH   A O   
6777 O O   . HOH   E .   ? 0.1917 0.2688 0.4200 -0.0147 -0.0130 -0.0020 411 HOH   A O   
6778 O O   . HOH   E .   ? 0.4630 0.4660 0.4313 0.1738  -0.0645 -0.1711 412 HOH   A O   
6779 O O   . HOH   E .   ? 0.5373 0.2811 0.3190 -0.1180 0.0451  0.0260  413 HOH   A O   
6780 O O   . HOH   E .   ? 0.2115 0.2939 0.2842 -0.0125 -0.0625 0.0567  414 HOH   A O   
6781 O O   A HOH   E .   ? 0.2447 0.2101 0.2275 0.0207  -0.0085 0.0476  415 HOH   A O   
6782 O O   . HOH   E .   ? 0.2769 0.3667 0.4131 -0.0503 0.1343  0.0213  416 HOH   A O   
6783 O O   A HOH   E .   ? 0.1462 0.1491 0.2483 0.0116  -0.0304 0.0101  417 HOH   A O   
6784 O O   . HOH   E .   ? 0.2930 0.5341 0.1940 -0.0441 0.0286  -0.0138 418 HOH   A O   
6785 O O   . HOH   E .   ? 0.2234 0.2858 0.5370 0.0090  -0.0646 -0.1146 419 HOH   A O   
6786 O O   . HOH   E .   ? 0.4781 0.8170 0.4564 0.0736  0.2279  -0.0944 420 HOH   A O   
6787 O O   B HOH   E .   ? 0.4415 0.5697 0.3980 -0.1041 0.1360  0.0963  421 HOH   A O   
6788 O O   A HOH   E .   ? 0.1368 0.1743 0.2402 -0.0084 0.0029  0.0129  422 HOH   A O   
6789 O O   A HOH   E .   ? 0.1619 0.2013 0.2646 -0.0193 -0.0296 0.0765  423 HOH   A O   
6790 O O   . HOH   E .   ? 0.2093 0.1762 0.2150 -0.0022 0.0259  0.0253  424 HOH   A O   
6791 O O   . HOH   E .   ? 0.3368 0.1374 0.2471 -0.0007 -0.0540 0.0128  425 HOH   A O   
6792 O O   . HOH   E .   ? 0.4916 0.5652 0.3499 -0.1279 -0.0332 0.1262  426 HOH   A O   
6793 O O   . HOH   E .   ? 0.8720 0.9001 0.7173 0.0398  -0.0907 -0.1148 427 HOH   A O   
6794 O O   . HOH   E .   ? 0.4370 0.2349 0.5765 -0.0963 -0.2279 0.1043  428 HOH   A O   
6795 O O   A HOH   E .   ? 0.2470 0.3446 0.2080 -0.0180 -0.0581 0.0166  429 HOH   A O   
6796 O O   A HOH   E .   ? 0.4979 0.4235 0.2783 -0.1079 -0.0238 0.1072  430 HOH   A O   
6797 O O   . HOH   E .   ? 0.2390 0.4251 0.3005 0.1464  -0.0083 0.0149  431 HOH   A O   
6798 O O   B HOH   E .   ? 0.2233 0.4194 0.3319 -0.0472 0.0363  0.0509  432 HOH   A O   
6799 O O   . HOH   E .   ? 0.3298 0.3624 0.2487 -0.0326 -0.0412 0.0344  433 HOH   A O   
6800 O O   . HOH   E .   ? 0.1864 0.1498 0.2566 -0.0216 0.0400  -0.0347 434 HOH   A O   
6801 O O   . HOH   E .   ? 0.5030 0.3523 0.3924 0.1487  -0.0312 -0.0757 435 HOH   A O   
6802 O O   B HOH   E .   ? 0.5097 0.2434 0.3724 -0.0259 0.0795  0.0692  436 HOH   A O   
6803 O O   . HOH   E .   ? 0.5498 0.7182 0.5876 0.0737  0.0950  0.1608  437 HOH   A O   
6804 O O   A HOH   E .   ? 0.1618 0.1452 0.2173 0.0265  -0.0304 0.0207  438 HOH   A O   
6805 O O   . HOH   E .   ? 0.7219 0.7925 0.6127 -0.1011 -0.0802 -0.0995 439 HOH   A O   
6806 O O   B HOH   E .   ? 0.4105 0.3221 0.2036 0.1203  0.0338  0.0214  440 HOH   A O   
6807 O O   . HOH   E .   ? 0.7303 0.7457 0.5279 0.0986  0.2392  -0.0886 441 HOH   A O   
6808 O O   . HOH   E .   ? 0.6969 0.4264 0.4835 0.1599  -0.0959 0.1516  442 HOH   A O   
6809 O O   . HOH   E .   ? 0.6982 0.6956 0.6709 0.1240  -0.1331 -0.0020 443 HOH   A O   
6810 O O   . HOH   E .   ? 0.5907 0.6329 0.4471 -0.1000 0.0740  0.0865  444 HOH   A O   
6811 O O   B HOH   E .   ? 0.2847 0.3621 0.2208 0.1750  -0.0034 0.0359  445 HOH   A O   
6812 O O   . HOH   E .   ? 0.3726 0.3039 0.2305 -0.0752 0.0300  0.0566  446 HOH   A O   
6813 O O   B HOH   E .   ? 0.2922 0.2696 0.4771 0.0373  0.1158  -0.0615 447 HOH   A O   
6814 O O   . HOH   E .   ? 0.6341 0.8230 0.4270 0.2406  -0.0479 0.1991  448 HOH   A O   
6815 O O   . HOH   E .   ? 0.7340 0.7443 0.6367 -0.1335 0.0136  0.0146  449 HOH   A O   
6816 O O   . HOH   E .   ? 0.2400 0.1673 0.3418 0.0085  -0.0004 0.0241  450 HOH   A O   
6817 O O   . HOH   E .   ? 0.1895 0.2237 0.5352 -0.0316 -0.0780 0.0623  451 HOH   A O   
6818 O O   A HOH   E .   ? 0.2237 0.2051 0.2019 0.0014  0.0010  -0.0194 452 HOH   A O   
6819 O O   . HOH   E .   ? 0.5870 0.5271 0.3696 -0.0447 -0.1530 0.0280  453 HOH   A O   
6820 O O   . HOH   E .   ? 0.2180 0.2794 0.2829 0.0023  -0.0109 -0.0451 454 HOH   A O   
6821 O O   . HOH   E .   ? 0.4618 0.4013 0.3318 0.2545  -0.0499 -0.0490 455 HOH   A O   
6822 O O   A HOH   E .   ? 0.5598 0.4304 0.3008 0.2501  0.1351  0.0896  456 HOH   A O   
6823 O O   . HOH   E .   ? 0.7009 0.5565 0.8084 0.0655  -0.1032 0.2264  457 HOH   A O   
6824 O O   . HOH   E .   ? 0.7406 0.6944 0.6798 -0.1497 -0.0566 -0.1301 458 HOH   A O   
6825 O O   . HOH   E .   ? 0.9255 0.4406 0.4395 -0.0385 0.2087  0.1211  459 HOH   A O   
6826 O O   . HOH   E .   ? 0.5154 0.5558 0.5046 0.0051  -0.1155 -0.1493 460 HOH   A O   
6827 O O   B HOH   E .   ? 0.1495 0.4688 0.3819 0.0211  -0.0808 -0.0448 461 HOH   A O   
6828 O O   . HOH   E .   ? 0.2504 0.2026 0.3254 0.0079  0.0287  0.0194  462 HOH   A O   
6829 O O   B HOH   E .   ? 0.3063 0.3949 0.3923 -0.1364 0.0321  -0.0450 463 HOH   A O   
6830 O O   . HOH   E .   ? 0.3428 0.4146 0.6146 0.0060  0.1083  -0.1725 464 HOH   A O   
6831 O O   . HOH   E .   ? 0.5424 0.5640 0.4252 0.2077  0.0512  0.0885  465 HOH   A O   
6832 O O   . HOH   E .   ? 0.6155 0.4430 0.4076 -0.0335 0.0558  0.0690  466 HOH   A O   
6833 O O   . HOH   E .   ? 0.7879 0.7945 0.5373 0.0680  -0.1114 -0.0770 467 HOH   A O   
6834 O O   . HOH   E .   ? 0.4486 0.5214 0.4594 0.0823  0.0276  0.0516  468 HOH   A O   
6835 O O   . HOH   E .   ? 0.4145 0.3983 0.5043 0.0283  0.0241  0.0946  469 HOH   A O   
6836 O O   . HOH   E .   ? 0.3464 0.4717 0.4862 0.1367  -0.0682 0.1436  470 HOH   A O   
6837 O O   . HOH   E .   ? 0.3718 0.4576 0.5035 -0.1640 0.0570  -0.1521 471 HOH   A O   
6838 O O   . HOH   E .   ? 0.2999 0.2584 0.4475 -0.0614 0.0616  -0.0751 472 HOH   A O   
6839 O O   B HOH   E .   ? 0.3057 0.1238 0.1898 -0.0507 -0.1041 -0.0038 473 HOH   A O   
6840 O O   . HOH   E .   ? 0.4117 0.5061 0.5566 0.0417  -0.0269 0.1027  474 HOH   A O   
6841 O O   . HOH   E .   ? 0.6201 0.3609 0.7727 0.0352  0.1137  0.2251  475 HOH   A O   
6842 O O   . HOH   E .   ? 0.4449 0.3470 0.7087 0.0601  -0.1895 -0.0761 476 HOH   A O   
6843 O O   . HOH   E .   ? 0.2694 0.4786 0.4660 0.0849  -0.0111 -0.1690 477 HOH   A O   
6844 O O   . HOH   E .   ? 0.4038 0.6550 0.3542 -0.1197 -0.1162 0.1830  478 HOH   A O   
6845 O O   . HOH   E .   ? 0.7379 0.6611 0.7218 -0.0733 0.0705  0.2871  479 HOH   A O   
6846 O O   . HOH   E .   ? 0.3920 0.5014 0.4246 -0.0805 -0.0028 -0.0414 480 HOH   A O   
6847 O O   . HOH   E .   ? 0.2854 0.1816 0.3098 0.0181  -0.0854 -0.0277 481 HOH   A O   
6848 O O   . HOH   E .   ? 0.2792 0.2942 0.3858 -0.1002 0.0493  -0.0096 482 HOH   A O   
6849 O O   . HOH   E .   ? 0.5539 0.6331 0.4404 0.0208  0.0872  0.0892  483 HOH   A O   
6850 O O   . HOH   E .   ? 0.4616 0.4342 0.3978 -0.0287 0.0870  0.0093  484 HOH   A O   
6851 O O   . HOH   E .   ? 0.4828 0.5110 0.2953 -0.0173 -0.0077 -0.0080 485 HOH   A O   
6852 O O   . HOH   E .   ? 0.5304 0.4216 0.3796 -0.0157 -0.0891 -0.0405 486 HOH   A O   
6853 O O   . HOH   E .   ? 0.3371 0.3152 0.3422 0.0213  0.0359  -0.0032 487 HOH   A O   
6854 O O   . HOH   E .   ? 0.4506 0.5780 0.4327 0.0590  -0.0798 -0.1052 488 HOH   A O   
6855 O O   . HOH   E .   ? 0.4531 0.4977 0.5443 0.0399  0.0303  -0.0877 489 HOH   A O   
6856 O O   . HOH   E .   ? 0.5052 0.3020 0.3758 -0.0835 -0.0775 0.0517  490 HOH   A O   
6857 O O   . HOH   E .   ? 0.4735 0.4398 0.5339 -0.2265 -0.0379 -0.0188 491 HOH   A O   
6858 O O   . HOH   E .   ? 0.5163 0.6316 0.5747 -0.1802 -0.1332 -0.0065 492 HOH   A O   
6859 O O   . HOH   E .   ? 0.3075 0.4030 0.3312 -0.0099 -0.0418 -0.0680 493 HOH   A O   
6860 O O   . HOH   E .   ? 0.6441 0.3508 0.4446 0.0550  -0.0246 -0.1138 494 HOH   A O   
6861 O O   . HOH   E .   ? 0.6029 0.6519 0.7173 0.0841  0.2198  -0.1223 495 HOH   A O   
6862 O O   . HOH   E .   ? 0.6511 0.5574 0.7090 0.0508  0.0832  -0.1086 496 HOH   A O   
6863 O O   . HOH   E .   ? 0.8484 0.3980 0.3416 -0.0207 -0.1237 0.0439  497 HOH   A O   
6864 O O   . HOH   E .   ? 0.4917 0.4002 0.2857 -0.1327 0.1296  -0.0586 498 HOH   A O   
6865 O O   . HOH   E .   ? 0.2586 0.2454 0.2954 0.0367  -0.0185 0.0032  499 HOH   A O   
6866 O O   . HOH   E .   ? 0.2822 0.4966 0.3569 0.0807  0.0869  0.2201  500 HOH   A O   
6867 O O   . HOH   E .   ? 0.2639 0.2787 0.7220 -0.0134 -0.1365 0.0575  501 HOH   A O   
6868 O O   . HOH   E .   ? 0.2818 0.3914 0.5499 0.0093  0.1087  0.1258  502 HOH   A O   
6869 O O   . HOH   E .   ? 0.6197 0.6326 0.4104 -0.0420 0.0007  0.1618  503 HOH   A O   
6870 O O   . HOH   E .   ? 0.5531 0.4977 0.6496 0.0611  -0.1317 0.0853  504 HOH   A O   
6871 O O   . HOH   E .   ? 0.6964 0.4922 0.6498 -0.0727 -0.1060 -0.0846 505 HOH   A O   
6872 O O   . HOH   E .   ? 0.5144 0.3613 0.4799 -0.1441 -0.0228 0.0918  506 HOH   A O   
6873 O O   . HOH   E .   ? 0.5560 0.3508 0.4926 -0.0313 0.2787  0.0192  507 HOH   A O   
6874 O O   . HOH   E .   ? 0.2825 0.3638 0.5398 -0.0134 0.0930  -0.0712 508 HOH   A O   
6875 O O   . HOH   E .   ? 0.3017 0.2325 0.5371 -0.0068 -0.0092 0.0763  509 HOH   A O   
6876 O O   . HOH   E .   ? 0.2226 0.3464 0.3516 0.0270  -0.0187 0.0665  510 HOH   A O   
6877 O O   . HOH   E .   ? 0.5366 0.2572 0.4481 -0.1569 0.0010  0.0255  511 HOH   A O   
6878 O O   B HOH   E .   ? 0.2565 0.2621 0.2518 0.0337  0.0524  0.0668  512 HOH   A O   
6879 O O   . HOH   E .   ? 0.6031 0.9032 0.6208 -0.1017 -0.0885 0.2638  513 HOH   A O   
6880 O O   . HOH   E .   ? 0.2771 0.4134 0.4438 0.0123  -0.0406 0.0043  514 HOH   A O   
6881 O O   . HOH   E .   ? 0.6034 0.6992 0.5111 0.0973  -0.0461 0.0159  515 HOH   A O   
6882 O O   . HOH   E .   ? 0.7295 0.4909 0.6033 0.2073  -0.0591 0.0911  516 HOH   A O   
6883 O O   . HOH   E .   ? 0.6312 0.2664 0.5281 -0.0625 0.0837  0.0906  517 HOH   A O   
6884 O O   . HOH   E .   ? 0.2974 0.2650 0.4913 0.0312  0.0335  0.0526  518 HOH   A O   
6885 O O   B HOH   E .   ? 0.3582 0.3276 0.3510 0.1093  0.0077  0.0976  519 HOH   A O   
6886 O O   . HOH   E .   ? 0.6059 0.6630 0.5012 0.3286  -0.0464 0.1192  520 HOH   A O   
6887 O O   A HOH   E .   ? 0.4239 0.4757 0.3324 -0.0268 -0.0583 -0.1073 521 HOH   A O   
6888 O O   T HOH   E .   ? 0.1076 0.1452 0.1808 -0.0475 -0.0195 0.0635  522 HOH   A O   
6889 O O   A HOH   E .   ? 0.3729 0.6720 0.3902 0.1879  0.0111  -0.0600 523 HOH   A O   
6890 O O   . HOH   E .   ? 0.3387 0.7445 0.5134 0.1005  0.0150  -0.1149 524 HOH   A O   
6891 O O   . HOH   E .   ? 0.5047 0.4738 0.5772 0.1116  -0.0934 0.1069  525 HOH   A O   
6892 O O   . HOH   E .   ? 0.5169 0.7409 0.5469 -0.0753 -0.0468 0.0795  526 HOH   A O   
6893 O O   . HOH   E .   ? 0.3648 0.5587 0.6347 -0.0692 -0.0911 0.3234  527 HOH   A O   
6894 O O   . HOH   F .   ? 0.2470 0.2223 0.3928 -0.0016 0.0966  0.0314  201 HOH   B O   
6895 O O   . HOH   F .   ? 0.4197 0.4595 0.4903 -0.1181 -0.0189 -0.1540 202 HOH   B O   
6896 O O   . HOH   F .   ? 0.5139 0.6699 0.4007 0.3114  -0.1257 -0.0402 203 HOH   B O   
6897 O O   . HOH   F .   ? 0.4633 0.4209 0.6719 0.0263  -0.1019 0.2782  204 HOH   B O   
6898 O O   . HOH   F .   ? 0.4574 0.3380 0.4157 -0.0287 -0.0117 -0.1197 205 HOH   B O   
6899 O O   . HOH   F .   ? 0.4522 0.4374 0.2752 -0.0121 -0.0194 -0.0935 206 HOH   B O   
6900 O O   . HOH   F .   ? 0.7912 0.3452 0.4152 0.0027  0.0548  0.0095  207 HOH   B O   
6901 O O   . HOH   F .   ? 0.3359 0.3509 0.6974 -0.0358 0.0272  -0.0573 208 HOH   B O   
6902 O O   . HOH   F .   ? 0.6276 0.5411 0.7411 0.1950  0.0772  0.0263  209 HOH   B O   
6903 O O   . HOH   F .   ? 0.4813 0.6858 0.4110 0.1923  0.0147  -0.0590 210 HOH   B O   
6904 O O   . HOH   F .   ? 0.1645 0.1983 0.3356 -0.0209 -0.0033 0.0120  211 HOH   B O   
6905 O O   . HOH   F .   ? 0.3282 0.1978 0.6200 0.0174  0.2127  0.0618  212 HOH   B O   
6906 O O   . HOH   F .   ? 0.1904 0.2520 0.3254 0.0066  0.0068  -0.0170 213 HOH   B O   
6907 O O   . HOH   F .   ? 0.4538 0.5878 0.3634 0.1894  -0.0622 -0.0691 214 HOH   B O   
6908 O O   . HOH   F .   ? 0.2948 0.6790 0.4334 0.0399  0.0071  0.2470  215 HOH   B O   
6909 O O   . HOH   F .   ? 0.6476 0.3176 0.3758 -0.1736 0.0351  0.0208  216 HOH   B O   
6910 O O   . HOH   F .   ? 0.3280 0.5438 0.5115 0.2227  0.0468  -0.0051 217 HOH   B O   
6911 O O   . HOH   F .   ? 0.3999 0.4390 0.4854 0.1644  -0.0531 -0.0141 218 HOH   B O   
6912 O O   . HOH   F .   ? 0.2952 0.2937 0.6904 0.0594  -0.1163 0.0543  219 HOH   B O   
6913 O O   . HOH   F .   ? 0.5018 0.3922 0.3525 -0.0092 -0.1143 0.0701  220 HOH   B O   
6914 O O   . HOH   F .   ? 0.4610 0.4019 0.6588 -0.0690 -0.1656 -0.0793 221 HOH   B O   
6915 O O   . HOH   F .   ? 0.3749 0.4738 0.3990 -0.0084 0.0491  -0.1044 222 HOH   B O   
6916 O O   . HOH   F .   ? 0.5105 0.1963 0.3603 -0.0194 -0.1039 -0.0032 223 HOH   B O   
6917 O O   . HOH   F .   ? 0.1870 0.2047 0.3639 -0.0187 0.0042  -0.0008 224 HOH   B O   
6918 O O   . HOH   F .   ? 0.2710 0.5279 0.5053 -0.0541 0.1268  -0.2165 225 HOH   B O   
6919 O O   . HOH   F .   ? 0.7088 0.6115 0.4061 0.0409  -0.0026 0.1263  226 HOH   B O   
6920 O O   . HOH   F .   ? 0.3703 0.3760 0.4387 0.0670  -0.1198 -0.2045 227 HOH   B O   
6921 O O   . HOH   F .   ? 0.3795 0.4744 0.5891 -0.1700 -0.0356 0.1211  228 HOH   B O   
6922 O O   . HOH   F .   ? 0.2211 0.2552 0.3438 -0.0602 0.0169  -0.0315 229 HOH   B O   
6923 O O   . HOH   F .   ? 0.3109 0.2683 0.7075 -0.0455 0.0546  0.0008  230 HOH   B O   
6924 O O   . HOH   F .   ? 0.3573 0.2368 0.4966 0.0028  0.1756  0.0453  231 HOH   B O   
6925 O O   . HOH   F .   ? 0.2497 0.1797 0.3234 -0.0261 0.1055  -0.0045 232 HOH   B O   
6926 O O   . HOH   F .   ? 0.3780 0.2698 0.4450 0.1024  -0.0274 -0.0463 233 HOH   B O   
6927 O O   . HOH   F .   ? 0.2166 0.1342 0.3923 0.0095  -0.0760 -0.0162 234 HOH   B O   
6928 O O   . HOH   F .   ? 0.2947 0.2917 0.3489 0.0393  0.0202  -0.0997 235 HOH   B O   
6929 O O   . HOH   F .   ? 0.3916 0.1840 0.2490 -0.0003 -0.0803 0.0044  236 HOH   B O   
6930 O O   . HOH   F .   ? 0.3207 0.3803 0.2507 0.0449  0.0550  0.0311  237 HOH   B O   
6931 O O   . HOH   F .   ? 0.2837 0.3519 0.3250 -0.0848 -0.0252 0.0055  238 HOH   B O   
6932 O O   . HOH   F .   ? 0.4706 0.3487 0.4265 -0.2363 -0.0225 0.0338  239 HOH   B O   
6933 O O   . HOH   F .   ? 0.1511 0.1432 0.2146 -0.0182 -0.0091 -0.0008 240 HOH   B O   
6934 O O   . HOH   F .   ? 0.2328 0.1885 0.2469 -0.0313 -0.0360 0.0080  241 HOH   B O   
6935 O O   . HOH   F .   ? 0.4475 0.3589 0.4225 -0.1127 0.0509  -0.1199 242 HOH   B O   
6936 O O   . HOH   F .   ? 0.3013 0.3570 0.3241 -0.0765 -0.0542 -0.0163 243 HOH   B O   
6937 O O   . HOH   F .   ? 0.3289 0.2411 0.3717 -0.0136 0.0019  -0.0620 244 HOH   B O   
6938 O O   . HOH   F .   ? 0.1636 0.1594 0.3182 -0.0066 -0.0013 -0.0021 245 HOH   B O   
6939 O O   . HOH   F .   ? 0.1579 0.1343 0.2312 -0.0026 -0.0176 0.0102  246 HOH   B O   
6940 O O   . HOH   F .   ? 0.3366 0.1774 0.6019 -0.0315 -0.1344 -0.0198 247 HOH   B O   
6941 O O   . HOH   F .   ? 0.2175 0.4418 0.2685 -0.0517 -0.0250 0.0356  248 HOH   B O   
6942 O O   . HOH   F .   ? 0.2274 0.2442 0.4557 -0.0355 0.0050  -0.0781 249 HOH   B O   
6943 O O   . HOH   F .   ? 0.2533 0.2303 0.2545 -0.0049 -0.0126 0.0034  250 HOH   B O   
6944 O O   . HOH   F .   ? 0.2332 0.4227 0.6282 0.1108  -0.0683 -0.1432 251 HOH   B O   
6945 O O   . HOH   F .   ? 0.2399 0.3860 0.3390 -0.0492 -0.0819 -0.0470 252 HOH   B O   
6946 O O   . HOH   F .   ? 0.3635 0.5061 0.6464 0.0911  0.0488  -0.1438 253 HOH   B O   
6947 O O   . HOH   F .   ? 0.2777 0.2167 0.3547 0.0765  0.0656  0.0054  254 HOH   B O   
6948 O O   . HOH   F .   ? 0.2381 0.1863 0.4096 0.0003  -0.0606 -0.0205 255 HOH   B O   
6949 O O   . HOH   F .   ? 0.2414 0.2176 0.3034 0.0679  -0.0814 -0.0640 256 HOH   B O   
6950 O O   . HOH   F .   ? 0.1674 0.1721 0.3538 -0.0232 -0.0312 0.0175  257 HOH   B O   
6951 O O   . HOH   F .   ? 0.2566 0.2205 0.2519 0.0133  -0.0121 0.0078  258 HOH   B O   
6952 O O   . HOH   F .   ? 0.3944 0.3576 0.2754 0.0526  0.0554  0.0460  259 HOH   B O   
6953 O O   . HOH   F .   ? 0.2112 0.1536 0.2637 -0.0279 -0.0367 0.0278  260 HOH   B O   
6954 O O   . HOH   F .   ? 0.3773 0.7333 0.3409 0.1880  -0.0627 0.0472  261 HOH   B O   
6955 O O   . HOH   F .   ? 0.2272 0.3155 0.2639 -0.0491 0.0226  0.0637  262 HOH   B O   
6956 O O   . HOH   F .   ? 0.4759 0.5590 0.2928 0.1383  -0.0725 -0.0488 263 HOH   B O   
6957 O O   . HOH   F .   ? 0.6219 0.3662 0.2971 -0.0471 -0.0517 0.0341  264 HOH   B O   
6958 O O   . HOH   F .   ? 0.1435 0.1739 0.2605 -0.0113 0.0141  0.0094  265 HOH   B O   
6959 O O   . HOH   F .   ? 0.3326 0.4929 0.3901 -0.0421 -0.1060 0.1078  266 HOH   B O   
6960 O O   . HOH   F .   ? 0.2706 0.7387 0.2956 0.0764  -0.0382 -0.0707 267 HOH   B O   
6961 O O   . HOH   F .   ? 0.4908 0.3567 0.3152 0.0310  -0.0218 -0.0554 268 HOH   B O   
6962 O O   . HOH   F .   ? 0.2900 0.3758 0.4015 0.0096  0.1286  0.0058  269 HOH   B O   
6963 O O   . HOH   F .   ? 0.4123 0.2660 0.4605 -0.0228 -0.0804 -0.0405 270 HOH   B O   
6964 O O   . HOH   F .   ? 0.1851 0.1469 0.4271 -0.0110 -0.0400 -0.0217 271 HOH   B O   
6965 O O   . HOH   F .   ? 0.2000 0.1874 0.2028 -0.0501 -0.0492 0.0086  272 HOH   B O   
6966 O O   . HOH   F .   ? 0.2897 0.2142 0.5076 0.0026  0.0475  0.0449  273 HOH   B O   
6967 O O   . HOH   F .   ? 0.3274 0.3280 0.5236 -0.0343 -0.0283 -0.1344 274 HOH   B O   
6968 O O   . HOH   F .   ? 0.2770 0.2081 0.3210 -0.0713 0.0095  -0.0179 275 HOH   B O   
6969 O O   . HOH   F .   ? 0.2020 0.1588 0.2800 -0.0252 -0.0203 0.0173  276 HOH   B O   
6970 O O   . HOH   F .   ? 0.2520 0.2566 0.2774 -0.0458 -0.0625 -0.0339 277 HOH   B O   
6971 O O   . HOH   F .   ? 0.2677 0.3182 0.2725 -0.0486 -0.0765 0.0200  278 HOH   B O   
6972 O O   . HOH   F .   ? 0.1716 0.1693 0.3815 -0.0144 0.0069  -0.0052 279 HOH   B O   
6973 O O   . HOH   F .   ? 0.2222 0.4752 0.4637 -0.0486 -0.0232 -0.1392 280 HOH   B O   
6974 O O   . HOH   F .   ? 0.3900 0.4223 0.4347 0.1510  -0.0759 -0.0850 281 HOH   B O   
6975 O O   . HOH   F .   ? 0.7404 0.5236 0.5407 0.1147  0.0038  -0.1332 282 HOH   B O   
6976 O O   . HOH   F .   ? 0.1819 0.2032 0.3469 0.0249  -0.0028 0.0162  283 HOH   B O   
6977 O O   . HOH   F .   ? 0.2884 0.7136 0.7747 0.1297  -0.0887 -0.1301 284 HOH   B O   
6978 O O   . HOH   F .   ? 0.5345 0.3765 0.3514 0.2421  0.1091  0.1001  285 HOH   B O   
6979 O O   . HOH   F .   ? 0.2629 0.3246 0.2606 0.0924  -0.0301 -0.0365 286 HOH   B O   
6980 O O   . HOH   F .   ? 0.2273 0.3520 0.3731 -0.0669 0.0580  -0.1178 287 HOH   B O   
6981 O O   . HOH   F .   ? 0.1682 0.2034 0.2069 -0.0082 -0.0123 -0.0101 288 HOH   B O   
6982 O O   . HOH   F .   ? 0.1698 0.1559 0.2312 -0.0010 -0.0052 -0.0040 289 HOH   B O   
6983 O O   . HOH   F .   ? 0.3892 0.2785 0.2436 0.0211  -0.0816 -0.0241 290 HOH   B O   
6984 O O   . HOH   F .   ? 0.2418 0.2880 0.3197 0.0181  -0.0830 0.0221  291 HOH   B O   
6985 O O   . HOH   F .   ? 0.3035 0.4831 0.4671 -0.0956 -0.1143 0.0700  292 HOH   B O   
6986 O O   . HOH   F .   ? 0.3388 0.2878 0.3266 -0.0314 0.0237  -0.1369 293 HOH   B O   
6987 O O   . HOH   F .   ? 0.4372 0.4936 0.2649 -0.0100 0.0526  0.0976  294 HOH   B O   
6988 O O   . HOH   F .   ? 0.4666 0.4242 0.4441 -0.1427 -0.0330 0.1629  295 HOH   B O   
6989 O O   . HOH   F .   ? 0.4084 0.2243 0.4485 -0.1119 -0.2075 0.0812  296 HOH   B O   
6990 O O   . HOH   F .   ? 0.3324 0.3097 0.6152 -0.0585 -0.1266 0.1666  297 HOH   B O   
6991 O O   . HOH   F .   ? 0.1869 0.1678 0.2939 0.0073  -0.0055 0.0222  298 HOH   B O   
6992 O O   . HOH   F .   ? 0.1766 0.3319 0.5343 0.0117  -0.0035 -0.1344 299 HOH   B O   
6993 O O   . HOH   F .   ? 0.3750 0.1959 0.3742 0.0803  0.1157  0.0578  300 HOH   B O   
6994 O O   . HOH   F .   ? 0.2125 0.2780 0.6446 0.0511  -0.0222 -0.0984 301 HOH   B O   
6995 O O   . HOH   F .   ? 0.5122 0.4085 0.2837 0.1093  -0.1178 0.0464  302 HOH   B O   
6996 O O   . HOH   F .   ? 0.2156 0.1697 0.3785 0.0322  -0.1036 0.0010  303 HOH   B O   
6997 O O   . HOH   F .   ? 0.5662 0.6329 0.2750 0.1720  -0.0821 0.0844  304 HOH   B O   
6998 O O   . HOH   F .   ? 0.4856 0.6234 0.4145 0.0415  -0.1567 -0.0014 305 HOH   B O   
6999 O O   . HOH   F .   ? 0.1656 0.1528 0.3497 0.0050  -0.0071 -0.0118 306 HOH   B O   
7000 O O   . HOH   F .   ? 0.2212 0.1716 0.3077 -0.0285 -0.0201 -0.0027 307 HOH   B O   
7001 O O   . HOH   F .   ? 0.5910 0.3065 0.2721 -0.2043 0.0994  -0.0103 308 HOH   B O   
7002 O O   . HOH   F .   ? 0.2379 0.3237 0.5129 -0.0345 -0.0653 -0.0014 309 HOH   B O   
7003 O O   . HOH   F .   ? 0.2958 0.3541 0.4055 -0.1245 0.0812  -0.0292 310 HOH   B O   
7004 O O   . HOH   F .   ? 0.2608 0.1527 0.2960 -0.0150 -0.0284 0.0329  311 HOH   B O   
7005 O O   . HOH   F .   ? 0.6531 0.4734 0.5193 0.1572  0.0451  -0.0306 312 HOH   B O   
7006 O O   . HOH   F .   ? 0.3898 0.2302 0.3035 0.1301  0.0544  0.0060  313 HOH   B O   
7007 O O   . HOH   F .   ? 0.2880 0.3128 0.3997 -0.0586 0.1001  -0.0990 314 HOH   B O   
7008 O O   . HOH   F .   ? 0.1675 0.1618 0.3573 -0.0147 -0.0257 -0.0129 315 HOH   B O   
7009 O O   . HOH   F .   ? 0.5545 0.5273 0.2788 -0.0321 -0.0705 -0.1148 316 HOH   B O   
7010 O O   . HOH   F .   ? 0.1664 0.1857 0.3533 -0.0235 -0.0068 0.0129  317 HOH   B O   
7011 O O   . HOH   F .   ? 0.2370 0.1986 0.2437 -0.0120 0.0195  0.0064  318 HOH   B O   
7012 O O   . HOH   F .   ? 0.2982 0.2247 0.2691 0.0171  -0.0236 0.0155  319 HOH   B O   
7013 O O   . HOH   F .   ? 0.2450 0.6339 0.5521 -0.0977 -0.0417 0.0562  320 HOH   B O   
7014 O O   . HOH   F .   ? 0.6533 0.6410 0.4945 -0.1161 -0.0347 0.1385  321 HOH   B O   
7015 O O   . HOH   F .   ? 0.5697 0.4763 0.7197 0.0627  -0.1035 0.2167  322 HOH   B O   
7016 O O   . HOH   F .   ? 0.1950 0.1954 0.3343 0.0197  0.0428  0.0208  323 HOH   B O   
7017 O O   . HOH   F .   ? 0.3126 0.4437 0.7679 -0.0085 -0.0928 0.2265  324 HOH   B O   
7018 O O   . HOH   F .   ? 0.4846 0.2518 0.3316 0.0215  0.0160  0.0731  325 HOH   B O   
7019 O O   . HOH   F .   ? 0.1805 0.2761 0.2801 -0.0144 -0.0166 0.0496  326 HOH   B O   
7020 O O   . HOH   F .   ? 0.4821 0.3871 0.5452 0.0791  -0.0222 0.0647  327 HOH   B O   
7021 O O   . HOH   F .   ? 0.4201 0.3362 0.5610 0.0954  0.1908  0.1747  328 HOH   B O   
7022 O O   . HOH   F .   ? 0.2613 0.2201 0.6267 -0.0133 -0.0005 0.0716  329 HOH   B O   
7023 O O   . HOH   F .   ? 0.6762 0.6670 0.6068 0.3542  -0.0294 -0.0669 330 HOH   B O   
7024 O O   . HOH   F .   ? 0.5815 0.3467 0.3610 0.0193  0.0898  0.1104  331 HOH   B O   
7025 O O   . HOH   F .   ? 0.7648 0.2178 0.3630 0.0308  -0.1078 -0.0111 332 HOH   B O   
7026 O O   . HOH   F .   ? 0.2184 0.2337 0.5649 -0.0538 -0.0119 0.1296  333 HOH   B O   
7027 O O   . HOH   F .   ? 0.5654 0.4406 0.6224 -0.0468 -0.0911 -0.0749 334 HOH   B O   
7028 O O   . HOH   F .   ? 0.3115 0.3239 0.5388 -0.0577 -0.1680 0.1367  335 HOH   B O   
7029 O O   . HOH   F .   ? 0.1688 0.2808 0.3544 0.0209  -0.0250 -0.0533 336 HOH   B O   
7030 O O   . HOH   F .   ? 0.1814 0.1475 0.2968 0.0049  -0.0265 0.0104  337 HOH   B O   
7031 O O   . HOH   F .   ? 0.5305 0.3804 0.4651 0.0363  0.0202  -0.1695 338 HOH   B O   
7032 O O   . HOH   F .   ? 0.5323 0.5772 0.3620 0.0533  -0.1161 -0.0261 339 HOH   B O   
7033 O O   . HOH   F .   ? 0.5301 0.3032 0.3611 0.0407  -0.1171 -0.0706 340 HOH   B O   
7034 O O   . HOH   F .   ? 0.4744 0.7115 0.3886 -0.0142 -0.0342 0.2099  341 HOH   B O   
7035 O O   . HOH   F .   ? 0.2141 0.6515 0.6595 -0.0195 -0.1018 0.0109  342 HOH   B O   
7036 O O   . HOH   F .   ? 0.3821 0.6466 0.3797 -0.0783 -0.0770 -0.0733 343 HOH   B O   
7037 O O   . HOH   F .   ? 0.8075 0.6371 0.3391 -0.0501 -0.0419 0.1193  344 HOH   B O   
7038 O O   . HOH   F .   ? 0.2062 0.1963 0.3551 -0.0066 0.0520  -0.0072 345 HOH   B O   
7039 O O   . HOH   F .   ? 0.4334 0.6601 0.4856 -0.1048 -0.0082 0.1780  346 HOH   B O   
7040 O O   . HOH   F .   ? 0.4301 0.5458 0.4965 0.0012  -0.0974 0.1475  347 HOH   B O   
7041 O O   . HOH   F .   ? 0.4437 0.5638 0.6875 0.0008  0.0134  0.0084  348 HOH   B O   
7042 O O   . HOH   F .   ? 0.3069 0.2045 0.4008 0.0398  -0.1098 -0.0599 349 HOH   B O   
7043 O O   . HOH   F .   ? 0.2283 0.5910 0.4190 0.1283  -0.0369 -0.1316 350 HOH   B O   
7044 O O   . HOH   F .   ? 0.2988 0.2254 0.5116 -0.0173 -0.0970 -0.0505 351 HOH   B O   
7045 O O   . HOH   F .   ? 0.2299 0.4353 0.5356 0.0134  0.0384  -0.0251 352 HOH   B O   
7046 O O   . HOH   F .   ? 0.4477 0.2399 0.3893 -0.0906 0.0730  -0.1013 353 HOH   B O   
7047 O O   . HOH   F .   ? 0.5380 0.3971 0.4428 0.0774  0.1349  -0.0615 354 HOH   B O   
7048 O O   . HOH   F .   ? 0.5192 0.3293 0.5467 -0.1157 0.1112  0.0802  355 HOH   B O   
7049 O O   . HOH   F .   ? 0.3682 0.4625 0.4981 -0.1621 0.0179  -0.0435 356 HOH   B O   
7050 O O   . HOH   F .   ? 0.3718 0.2917 0.3907 -0.0910 -0.0204 -0.0517 357 HOH   B O   
7051 O O   . HOH   F .   ? 0.4948 0.6121 0.4534 0.2080  -0.1279 0.1484  358 HOH   B O   
7052 O O   . HOH   F .   ? 0.6035 0.3585 0.5181 -0.0099 -0.1682 -0.0257 359 HOH   B O   
7053 O O   . HOH   F .   ? 0.5728 0.4806 0.5685 -0.0477 -0.0548 0.0527  360 HOH   B O   
7054 O O   . HOH   F .   ? 0.5028 0.4015 0.6154 -0.0002 0.0970  0.0886  361 HOH   B O   
7055 O O   . HOH   F .   ? 0.2163 0.3887 0.6753 -0.0646 -0.0707 -0.0869 362 HOH   B O   
7056 O O   . HOH   F .   ? 0.5670 0.6518 0.3648 0.2473  0.0701  0.0674  363 HOH   B O   
7057 O O   . HOH   F .   ? 0.5143 0.5282 0.4518 -0.0523 -0.0689 -0.1157 364 HOH   B O   
7058 O O   . HOH   F .   ? 0.5790 0.2444 0.3593 -0.0024 0.0240  0.0541  365 HOH   B O   
7059 O O   . HOH   F .   ? 0.5128 0.3333 0.5100 -0.1425 -0.0733 0.0266  366 HOH   B O   
7060 O O   . HOH   F .   ? 0.6158 0.4709 0.4434 0.0943  0.0368  0.0788  367 HOH   B O   
7061 O O   . HOH   F .   ? 0.7346 0.8288 0.5047 0.2954  -0.1203 0.1015  368 HOH   B O   
7062 O O   . HOH   F .   ? 0.4158 0.3338 0.5538 0.0414  -0.1909 0.0223  369 HOH   B O   
7063 O O   . HOH   F .   ? 0.6801 0.5245 0.4455 0.0956  -0.1092 0.0783  370 HOH   B O   
7064 O O   . HOH   F .   ? 0.4606 0.6092 0.5311 0.2923  0.1328  0.1261  371 HOH   B O   
7065 O O   . HOH   F .   ? 0.4829 0.3658 0.5233 0.0710  -0.1654 -0.0574 372 HOH   B O   
7066 O O   . HOH   F .   ? 0.5414 0.4609 0.3307 -0.1211 -0.0802 -0.0816 373 HOH   B O   
7067 O O   . HOH   F .   ? 0.4541 0.5114 0.4484 -0.0831 -0.0499 0.0389  374 HOH   B O   
7068 O O   . HOH   F .   ? 0.2475 0.4584 0.4561 0.0125  -0.0506 -0.0700 375 HOH   B O   
7069 O O   . HOH   F .   ? 0.5207 0.5354 0.2738 -0.0969 0.1080  -0.0291 376 HOH   B O   
7070 O O   . HOH   F .   ? 0.7485 0.3995 0.5797 -0.0722 -0.0555 -0.0152 377 HOH   B O   
7071 O O   . HOH   F .   ? 0.4660 0.6695 0.6103 0.0961  0.0293  0.2723  378 HOH   B O   
7072 O O   . HOH   F .   ? 0.6419 0.7314 0.4707 -0.1364 -0.0241 -0.1405 379 HOH   B O   
7073 O O   . HOH   F .   ? 0.3597 0.4448 0.5093 0.1106  -0.0293 0.1058  380 HOH   B O   
7074 O O   . HOH   F .   ? 0.6033 0.6277 0.6782 0.0582  0.2899  0.1055  381 HOH   B O   
7075 O O   . HOH   F .   ? 0.3486 0.2687 0.3340 0.0063  0.0366  0.0157  382 HOH   B O   
7076 O O   . HOH   F .   ? 0.5479 0.7750 0.5724 0.1239  0.2659  0.1046  383 HOH   B O   
7077 O O   . HOH   F .   ? 0.5705 0.4310 0.5601 -0.0636 -0.0204 -0.0598 384 HOH   B O   
7078 O O   . HOH   F .   ? 0.6098 0.5979 0.4030 0.0566  -0.1011 -0.0166 385 HOH   B O   
7079 O O   . HOH   F .   ? 0.5302 0.4331 0.3540 0.0424  0.0313  -0.0338 386 HOH   B O   
7080 O O   . HOH   F .   ? 0.2463 0.4532 0.4272 -0.0809 -0.0870 -0.0254 387 HOH   B O   
7081 O O   . HOH   F .   ? 0.7889 0.6096 0.5114 0.2736  0.0321  0.0827  388 HOH   B O   
7082 O O   . HOH   F .   ? 0.6538 0.4497 0.4999 0.0512  0.1529  -0.1130 389 HOH   B O   
7083 O O   . HOH   F .   ? 0.3662 0.2323 0.3378 0.0589  -0.0276 -0.0051 390 HOH   B O   
7084 O O   . HOH   F .   ? 0.5162 0.4118 0.4730 -0.0004 0.0416  0.0499  391 HOH   B O   
7085 O O   . HOH   F .   ? 0.2713 0.3935 0.6797 -0.1252 -0.1145 0.0621  392 HOH   B O   
7086 O O   . HOH   F .   ? 0.4142 0.2524 0.5616 -0.0342 0.0645  0.0636  393 HOH   B O   
7087 O O   . HOH   F .   ? 0.3486 0.6246 0.3960 0.0469  -0.0175 -0.1266 394 HOH   B O   
7088 O O   . HOH   F .   ? 0.4372 0.4847 0.3966 -0.0743 0.0641  0.0953  395 HOH   B O   
7089 O O   . HOH   F .   ? 0.2219 0.2843 0.6376 -0.0640 -0.1030 0.0408  396 HOH   B O   
7090 O O   . HOH   F .   ? 0.3209 0.3339 0.4428 0.0458  -0.0035 -0.0334 397 HOH   B O   
7091 O O   . HOH   F .   ? 0.5744 0.6496 0.7963 0.1245  -0.0970 0.1328  398 HOH   B O   
7092 O O   . HOH   F .   ? 0.5741 0.4271 0.3320 -0.2412 -0.0793 0.0973  399 HOH   B O   
7093 O O   . HOH   F .   ? 0.6161 0.6272 0.4107 0.2168  0.0304  -0.0152 400 HOH   B O   
# 
