data_7HD6
# 
_entry.id   7HD6 
# 
_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   7HD6         pdb_00007hd6 10.2210/pdb7hd6/pdb 
WWPDB D_1001407324 ?            ?                   
# 
_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                        7HD6 
_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-[(2S)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]propan-2-ol' 246.308   1   ?                      ? 
? ?                                                                                    
4 water       nat water                                                                    18.015    418 ?                      ? 
? ?                                                                                    
# 
_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-[(2S)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]propan-2-ol' A1A65 
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 
A1A65 non-polymer         . '2-[(2S)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]propan-2-ol' ? 'C13 H18 N4 O'   246.308 
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 A1A65 1   202 201  A1A65 LA1 A . 
E 4 HOH   1   301 196  HOH   HOH A . 
E 4 HOH   2   302 292  HOH   HOH A . 
E 4 HOH   3   303 36   HOH   HOH A . 
E 4 HOH   4   304 625  HOH   HOH A . 
E 4 HOH   5   305 229  HOH   HOH A . 
E 4 HOH   6   306 493  HOH   HOH A . 
E 4 HOH   7   307 153  HOH   HOH A . 
E 4 HOH   8   308 209  HOH   HOH A . 
E 4 HOH   9   309 109  HOH   HOH A . 
E 4 HOH   10  310 247  HOH   HOH A . 
E 4 HOH   11  311 6    HOH   HOH A . 
E 4 HOH   12  312 1295 HOH   HOH A . 
E 4 HOH   13  313 76   HOH   HOH A . 
E 4 HOH   14  314 1289 HOH   HOH A . 
E 4 HOH   15  315 1275 HOH   HOH A . 
E 4 HOH   16  316 405  HOH   HOH A . 
E 4 HOH   17  317 236  HOH   HOH A . 
E 4 HOH   18  318 136  HOH   HOH A . 
E 4 HOH   19  319 661  HOH   HOH A . 
E 4 HOH   20  320 192  HOH   HOH A . 
E 4 HOH   21  321 124  HOH   HOH A . 
E 4 HOH   22  322 93   HOH   HOH A . 
E 4 HOH   23  323 18   HOH   HOH A . 
E 4 HOH   24  324 225  HOH   HOH A . 
E 4 HOH   25  325 1283 HOH   HOH A . 
E 4 HOH   26  326 164  HOH   HOH A . 
E 4 HOH   27  327 105  HOH   HOH A . 
E 4 HOH   28  328 39   HOH   HOH A . 
E 4 HOH   29  329 1300 HOH   HOH A . 
E 4 HOH   30  330 15   HOH   HOH A . 
E 4 HOH   31  331 151  HOH   HOH A . 
E 4 HOH   32  332 1301 HOH   HOH A . 
E 4 HOH   33  333 409  HOH   HOH A . 
E 4 HOH   34  334 662  HOH   HOH A . 
E 4 HOH   35  335 320  HOH   HOH A . 
E 4 HOH   36  336 337  HOH   HOH A . 
E 4 HOH   37  337 140  HOH   HOH A . 
E 4 HOH   38  338 33   HOH   HOH A . 
E 4 HOH   39  339 1290 HOH   HOH A . 
E 4 HOH   40  340 78   HOH   HOH A . 
E 4 HOH   41  341 8    HOH   HOH A . 
E 4 HOH   42  342 241  HOH   HOH A . 
E 4 HOH   43  343 630  HOH   HOH A . 
E 4 HOH   44  344 393  HOH   HOH A . 
E 4 HOH   45  345 74   HOH   HOH A . 
E 4 HOH   46  346 964  HOH   HOH A . 
E 4 HOH   47  347 165  HOH   HOH A . 
E 4 HOH   48  348 469  HOH   HOH A . 
E 4 HOH   49  349 21   HOH   HOH A . 
E 4 HOH   50  350 57   HOH   HOH A . 
E 4 HOH   51  351 396  HOH   HOH A . 
E 4 HOH   52  352 42   HOH   HOH A . 
E 4 HOH   53  353 17   HOH   HOH A . 
E 4 HOH   54  354 155  HOH   HOH A . 
E 4 HOH   55  355 139  HOH   HOH A . 
E 4 HOH   56  356 102  HOH   HOH A . 
E 4 HOH   57  357 354  HOH   HOH A . 
E 4 HOH   58  358 2    HOH   HOH A . 
E 4 HOH   59  359 92   HOH   HOH A . 
E 4 HOH   60  360 45   HOH   HOH A . 
E 4 HOH   61  361 85   HOH   HOH A . 
E 4 HOH   62  362 169  HOH   HOH A . 
E 4 HOH   63  363 162  HOH   HOH A . 
E 4 HOH   64  364 66   HOH   HOH A . 
E 4 HOH   65  365 138  HOH   HOH A . 
E 4 HOH   66  366 19   HOH   HOH A . 
E 4 HOH   67  367 5    HOH   HOH A . 
E 4 HOH   68  368 159  HOH   HOH A . 
E 4 HOH   69  369 46   HOH   HOH A . 
E 4 HOH   70  370 296  HOH   HOH A . 
E 4 HOH   71  371 86   HOH   HOH A . 
E 4 HOH   72  372 26   HOH   HOH A . 
E 4 HOH   73  373 24   HOH   HOH A . 
E 4 HOH   74  374 939  HOH   HOH A . 
E 4 HOH   75  375 27   HOH   HOH A . 
E 4 HOH   76  376 56   HOH   HOH A . 
E 4 HOH   77  377 81   HOH   HOH A . 
E 4 HOH   78  378 49   HOH   HOH A . 
E 4 HOH   79  379 154  HOH   HOH A . 
E 4 HOH   80  380 186  HOH   HOH A . 
E 4 HOH   81  381 134  HOH   HOH A . 
E 4 HOH   82  382 140  HOH   HOH A . 
E 4 HOH   83  383 351  HOH   HOH A . 
E 4 HOH   84  384 148  HOH   HOH A . 
E 4 HOH   85  385 1094 HOH   HOH A . 
E 4 HOH   86  386 35   HOH   HOH A . 
E 4 HOH   87  387 6    HOH   HOH A . 
E 4 HOH   88  388 366  HOH   HOH A . 
E 4 HOH   89  389 34   HOH   HOH A . 
E 4 HOH   90  390 116  HOH   HOH A . 
E 4 HOH   91  391 1308 HOH   HOH A . 
E 4 HOH   92  392 218  HOH   HOH A . 
E 4 HOH   93  393 303  HOH   HOH A . 
E 4 HOH   94  394 83   HOH   HOH A . 
E 4 HOH   95  395 67   HOH   HOH A . 
E 4 HOH   96  396 122  HOH   HOH A . 
E 4 HOH   97  397 115  HOH   HOH A . 
E 4 HOH   98  398 121  HOH   HOH A . 
E 4 HOH   99  399 461  HOH   HOH A . 
E 4 HOH   100 400 2    HOH   HOH A . 
E 4 HOH   101 401 1309 HOH   HOH A . 
E 4 HOH   102 402 195  HOH   HOH A . 
E 4 HOH   103 403 281  HOH   HOH A . 
E 4 HOH   104 404 1315 HOH   HOH A . 
E 4 HOH   105 405 4    HOH   HOH A . 
E 4 HOH   106 406 1310 HOH   HOH A . 
E 4 HOH   107 407 199  HOH   HOH A . 
E 4 HOH   108 408 3    HOH   HOH A . 
E 4 HOH   109 409 12   HOH   HOH A . 
E 4 HOH   110 410 333  HOH   HOH A . 
E 4 HOH   111 411 58   HOH   HOH A . 
E 4 HOH   112 412 96   HOH   HOH A . 
E 4 HOH   113 413 1068 HOH   HOH A . 
E 4 HOH   114 414 3    HOH   HOH A . 
E 4 HOH   115 415 1313 HOH   HOH A . 
E 4 HOH   116 416 397  HOH   HOH A . 
E 4 HOH   117 417 68   HOH   HOH A . 
E 4 HOH   118 418 25   HOH   HOH A . 
E 4 HOH   119 419 1279 HOH   HOH A . 
E 4 HOH   120 420 156  HOH   HOH A . 
E 4 HOH   121 421 125  HOH   HOH A . 
E 4 HOH   122 422 53   HOH   HOH A . 
E 4 HOH   123 423 7    HOH   HOH A . 
E 4 HOH   124 424 381  HOH   HOH A . 
E 4 HOH   125 425 278  HOH   HOH A . 
E 4 HOH   126 426 132  HOH   HOH A . 
E 4 HOH   127 427 123  HOH   HOH A . 
E 4 HOH   128 428 95   HOH   HOH A . 
E 4 HOH   129 429 1222 HOH   HOH A . 
E 4 HOH   130 430 582  HOH   HOH A . 
E 4 HOH   131 431 51   HOH   HOH A . 
E 4 HOH   132 432 7    HOH   HOH A . 
E 4 HOH   133 433 9    HOH   HOH A . 
E 4 HOH   134 434 70   HOH   HOH A . 
E 4 HOH   135 435 212  HOH   HOH A . 
E 4 HOH   136 436 40   HOH   HOH A . 
E 4 HOH   137 437 71   HOH   HOH A . 
E 4 HOH   138 438 8    HOH   HOH A . 
E 4 HOH   139 439 1189 HOH   HOH A . 
E 4 HOH   140 440 952  HOH   HOH A . 
E 4 HOH   141 441 1238 HOH   HOH A . 
E 4 HOH   142 442 1296 HOH   HOH A . 
E 4 HOH   143 443 80   HOH   HOH A . 
E 4 HOH   144 444 188  HOH   HOH A . 
E 4 HOH   145 445 94   HOH   HOH A . 
E 4 HOH   146 446 1286 HOH   HOH A . 
E 4 HOH   147 447 73   HOH   HOH A . 
E 4 HOH   148 448 104  HOH   HOH A . 
E 4 HOH   149 449 97   HOH   HOH A . 
E 4 HOH   150 450 79   HOH   HOH A . 
E 4 HOH   151 451 944  HOH   HOH A . 
E 4 HOH   152 452 16   HOH   HOH A . 
E 4 HOH   153 453 1    HOH   HOH A . 
E 4 HOH   154 454 576  HOH   HOH A . 
E 4 HOH   155 455 330  HOH   HOH A . 
E 4 HOH   156 456 1119 HOH   HOH A . 
E 4 HOH   157 457 1134 HOH   HOH A . 
E 4 HOH   158 458 509  HOH   HOH A . 
E 4 HOH   159 459 107  HOH   HOH A . 
E 4 HOH   160 460 163  HOH   HOH A . 
E 4 HOH   161 461 726  HOH   HOH A . 
E 4 HOH   162 462 408  HOH   HOH A . 
E 4 HOH   163 463 756  HOH   HOH A . 
E 4 HOH   164 464 361  HOH   HOH A . 
E 4 HOH   165 465 280  HOH   HOH A . 
E 4 HOH   166 466 126  HOH   HOH A . 
E 4 HOH   167 467 319  HOH   HOH A . 
E 4 HOH   168 468 801  HOH   HOH A . 
E 4 HOH   169 469 556  HOH   HOH A . 
E 4 HOH   170 470 63   HOH   HOH A . 
E 4 HOH   171 471 1307 HOH   HOH A . 
E 4 HOH   172 472 250  HOH   HOH A . 
E 4 HOH   173 473 1276 HOH   HOH A . 
E 4 HOH   174 474 342  HOH   HOH A . 
E 4 HOH   175 475 267  HOH   HOH A . 
E 4 HOH   176 476 1306 HOH   HOH A . 
E 4 HOH   177 477 1287 HOH   HOH A . 
E 4 HOH   178 478 224  HOH   HOH A . 
E 4 HOH   179 479 370  HOH   HOH A . 
E 4 HOH   180 480 695  HOH   HOH A . 
E 4 HOH   181 481 919  HOH   HOH A . 
E 4 HOH   182 482 674  HOH   HOH A . 
E 4 HOH   183 483 135  HOH   HOH A . 
E 4 HOH   184 484 202  HOH   HOH A . 
E 4 HOH   185 485 4    HOH   HOH A . 
E 4 HOH   186 486 521  HOH   HOH A . 
E 4 HOH   187 487 326  HOH   HOH A . 
E 4 HOH   188 488 309  HOH   HOH A . 
E 4 HOH   189 489 1299 HOH   HOH A . 
E 4 HOH   190 490 318  HOH   HOH A . 
E 4 HOH   191 491 315  HOH   HOH A . 
E 4 HOH   192 492 805  HOH   HOH A . 
E 4 HOH   193 493 1314 HOH   HOH A . 
E 4 HOH   194 494 331  HOH   HOH A . 
E 4 HOH   195 495 263  HOH   HOH A . 
E 4 HOH   196 496 711  HOH   HOH A . 
E 4 HOH   197 497 941  HOH   HOH A . 
E 4 HOH   198 498 152  HOH   HOH A . 
E 4 HOH   199 499 208  HOH   HOH A . 
E 4 HOH   200 500 1071 HOH   HOH A . 
E 4 HOH   201 501 356  HOH   HOH A . 
E 4 HOH   202 502 180  HOH   HOH A . 
E 4 HOH   203 503 1284 HOH   HOH A . 
E 4 HOH   204 504 350  HOH   HOH A . 
E 4 HOH   205 505 363  HOH   HOH A . 
E 4 HOH   206 506 371  HOH   HOH A . 
E 4 HOH   207 507 313  HOH   HOH A . 
E 4 HOH   208 508 376  HOH   HOH A . 
E 4 HOH   209 509 185  HOH   HOH A . 
E 4 HOH   210 510 429  HOH   HOH A . 
E 4 HOH   211 511 5    HOH   HOH A . 
E 4 HOH   212 512 70   HOH   HOH A . 
E 4 HOH   213 513 772  HOH   HOH A . 
E 4 HOH   214 514 1074 HOH   HOH A . 
E 4 HOH   215 515 346  HOH   HOH A . 
E 4 HOH   216 516 1292 HOH   HOH A . 
E 4 HOH   217 517 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 900  HOH   HOH B . 
F 4 HOH   3   203 358  HOH   HOH B . 
F 4 HOH   4   204 549  HOH   HOH B . 
F 4 HOH   5   205 1249 HOH   HOH B . 
F 4 HOH   6   206 531  HOH   HOH B . 
F 4 HOH   7   207 364  HOH   HOH B . 
F 4 HOH   8   208 758  HOH   HOH B . 
F 4 HOH   9   209 240  HOH   HOH B . 
F 4 HOH   10  210 120  HOH   HOH B . 
F 4 HOH   11  211 232  HOH   HOH B . 
F 4 HOH   12  212 398  HOH   HOH B . 
F 4 HOH   13  213 654  HOH   HOH B . 
F 4 HOH   14  214 743  HOH   HOH B . 
F 4 HOH   15  215 50   HOH   HOH B . 
F 4 HOH   16  216 444  HOH   HOH B . 
F 4 HOH   17  217 353  HOH   HOH B . 
F 4 HOH   18  218 343  HOH   HOH B . 
F 4 HOH   19  219 131  HOH   HOH B . 
F 4 HOH   20  220 1140 HOH   HOH B . 
F 4 HOH   21  221 332  HOH   HOH B . 
F 4 HOH   22  222 452  HOH   HOH B . 
F 4 HOH   23  223 264  HOH   HOH B . 
F 4 HOH   24  224 282  HOH   HOH B . 
F 4 HOH   25  225 276  HOH   HOH B . 
F 4 HOH   26  226 1278 HOH   HOH B . 
F 4 HOH   27  227 205  HOH   HOH B . 
F 4 HOH   28  228 54   HOH   HOH B . 
F 4 HOH   29  229 75   HOH   HOH B . 
F 4 HOH   30  230 82   HOH   HOH B . 
F 4 HOH   31  231 1312 HOH   HOH B . 
F 4 HOH   32  232 60   HOH   HOH B . 
F 4 HOH   33  233 723  HOH   HOH B . 
F 4 HOH   34  234 181  HOH   HOH B . 
F 4 HOH   35  235 272  HOH   HOH B . 
F 4 HOH   36  236 128  HOH   HOH B . 
F 4 HOH   37  237 133  HOH   HOH B . 
F 4 HOH   38  238 1    HOH   HOH B . 
F 4 HOH   39  239 252  HOH   HOH B . 
F 4 HOH   40  240 325  HOH   HOH B . 
F 4 HOH   41  241 110  HOH   HOH B . 
F 4 HOH   42  242 127  HOH   HOH B . 
F 4 HOH   43  243 300  HOH   HOH B . 
F 4 HOH   44  244 166  HOH   HOH B . 
F 4 HOH   45  245 14   HOH   HOH B . 
F 4 HOH   46  246 52   HOH   HOH B . 
F 4 HOH   47  247 103  HOH   HOH B . 
F 4 HOH   48  248 69   HOH   HOH B . 
F 4 HOH   49  249 9    HOH   HOH B . 
F 4 HOH   50  250 129  HOH   HOH B . 
F 4 HOH   51  251 31   HOH   HOH B . 
F 4 HOH   52  252 30   HOH   HOH B . 
F 4 HOH   53  253 231  HOH   HOH B . 
F 4 HOH   54  254 172  HOH   HOH B . 
F 4 HOH   55  255 144  HOH   HOH B . 
F 4 HOH   56  256 10   HOH   HOH B . 
F 4 HOH   57  257 47   HOH   HOH B . 
F 4 HOH   58  258 150  HOH   HOH B . 
F 4 HOH   59  259 271  HOH   HOH B . 
F 4 HOH   60  260 391  HOH   HOH B . 
F 4 HOH   61  261 41   HOH   HOH B . 
F 4 HOH   62  262 62   HOH   HOH B . 
F 4 HOH   63  263 175  HOH   HOH B . 
F 4 HOH   64  264 72   HOH   HOH B . 
F 4 HOH   65  265 59   HOH   HOH B . 
F 4 HOH   66  266 143  HOH   HOH B . 
F 4 HOH   67  267 242  HOH   HOH B . 
F 4 HOH   68  268 347  HOH   HOH B . 
F 4 HOH   69  269 77   HOH   HOH B . 
F 4 HOH   70  270 20   HOH   HOH B . 
F 4 HOH   71  271 302  HOH   HOH B . 
F 4 HOH   72  272 117  HOH   HOH B . 
F 4 HOH   73  273 61   HOH   HOH B . 
F 4 HOH   74  274 11   HOH   HOH B . 
F 4 HOH   75  275 1277 HOH   HOH B . 
F 4 HOH   76  276 221  HOH   HOH B . 
F 4 HOH   77  277 84   HOH   HOH B . 
F 4 HOH   78  278 114  HOH   HOH B . 
F 4 HOH   79  279 287  HOH   HOH B . 
F 4 HOH   80  280 243  HOH   HOH B . 
F 4 HOH   81  281 22   HOH   HOH B . 
F 4 HOH   82  282 147  HOH   HOH B . 
F 4 HOH   83  283 106  HOH   HOH B . 
F 4 HOH   84  284 1066 HOH   HOH B . 
F 4 HOH   85  285 387  HOH   HOH B . 
F 4 HOH   86  286 43   HOH   HOH B . 
F 4 HOH   87  287 88   HOH   HOH B . 
F 4 HOH   88  288 235  HOH   HOH B . 
F 4 HOH   89  289 216  HOH   HOH B . 
F 4 HOH   90  290 299  HOH   HOH B . 
F 4 HOH   91  291 220  HOH   HOH B . 
F 4 HOH   92  292 99   HOH   HOH B . 
F 4 HOH   93  293 416  HOH   HOH B . 
F 4 HOH   94  294 635  HOH   HOH B . 
F 4 HOH   95  295 13   HOH   HOH B . 
F 4 HOH   96  296 137  HOH   HOH B . 
F 4 HOH   97  297 1305 HOH   HOH B . 
F 4 HOH   98  298 89   HOH   HOH B . 
F 4 HOH   99  299 1106 HOH   HOH B . 
F 4 HOH   100 300 112  HOH   HOH B . 
F 4 HOH   101 301 311  HOH   HOH B . 
F 4 HOH   102 302 142  HOH   HOH B . 
F 4 HOH   103 303 160  HOH   HOH B . 
F 4 HOH   104 304 297  HOH   HOH B . 
F 4 HOH   105 305 316  HOH   HOH B . 
F 4 HOH   106 306 215  HOH   HOH B . 
F 4 HOH   107 307 101  HOH   HOH B . 
F 4 HOH   108 308 32   HOH   HOH B . 
F 4 HOH   109 309 118  HOH   HOH B . 
F 4 HOH   110 310 38   HOH   HOH B . 
F 4 HOH   111 311 37   HOH   HOH B . 
F 4 HOH   112 312 704  HOH   HOH B . 
F 4 HOH   113 313 341  HOH   HOH B . 
F 4 HOH   114 314 1126 HOH   HOH B . 
F 4 HOH   115 315 177  HOH   HOH B . 
F 4 HOH   116 316 23   HOH   HOH B . 
F 4 HOH   117 317 48   HOH   HOH B . 
F 4 HOH   118 318 170  HOH   HOH B . 
F 4 HOH   119 319 1291 HOH   HOH B . 
F 4 HOH   120 320 182  HOH   HOH B . 
F 4 HOH   121 321 91   HOH   HOH B . 
F 4 HOH   122 322 1285 HOH   HOH B . 
F 4 HOH   123 323 141  HOH   HOH B . 
F 4 HOH   124 324 28   HOH   HOH B . 
F 4 HOH   125 325 197  HOH   HOH B . 
F 4 HOH   126 326 1274 HOH   HOH B . 
F 4 HOH   127 327 100  HOH   HOH B . 
F 4 HOH   128 328 161  HOH   HOH B . 
F 4 HOH   129 329 44   HOH   HOH B . 
F 4 HOH   130 330 29   HOH   HOH B . 
F 4 HOH   131 331 334  HOH   HOH B . 
F 4 HOH   132 332 1294 HOH   HOH B . 
F 4 HOH   133 333 717  HOH   HOH B . 
F 4 HOH   134 334 98   HOH   HOH B . 
F 4 HOH   135 335 55   HOH   HOH B . 
F 4 HOH   136 336 207  HOH   HOH B . 
F 4 HOH   137 337 339  HOH   HOH B . 
F 4 HOH   138 338 65   HOH   HOH B . 
F 4 HOH   139 339 1293 HOH   HOH B . 
F 4 HOH   140 340 234  HOH   HOH B . 
F 4 HOH   141 341 619  HOH   HOH B . 
F 4 HOH   142 342 445  HOH   HOH B . 
F 4 HOH   143 343 362  HOH   HOH B . 
F 4 HOH   144 344 178  HOH   HOH B . 
F 4 HOH   145 345 90   HOH   HOH B . 
F 4 HOH   146 346 960  HOH   HOH B . 
F 4 HOH   147 347 463  HOH   HOH B . 
F 4 HOH   148 348 335  HOH   HOH B . 
F 4 HOH   149 349 191  HOH   HOH B . 
F 4 HOH   150 350 1304 HOH   HOH B . 
F 4 HOH   151 351 623  HOH   HOH B . 
F 4 HOH   152 352 1046 HOH   HOH B . 
F 4 HOH   153 353 304  HOH   HOH B . 
F 4 HOH   154 354 203  HOH   HOH B . 
F 4 HOH   155 355 1280 HOH   HOH B . 
F 4 HOH   156 356 290  HOH   HOH B . 
F 4 HOH   157 357 541  HOH   HOH B . 
F 4 HOH   158 358 87   HOH   HOH B . 
F 4 HOH   159 359 479  HOH   HOH B . 
F 4 HOH   160 360 1077 HOH   HOH B . 
F 4 HOH   161 361 389  HOH   HOH B . 
F 4 HOH   162 362 718  HOH   HOH B . 
F 4 HOH   163 363 283  HOH   HOH B . 
F 4 HOH   164 364 1072 HOH   HOH B . 
F 4 HOH   165 365 1316 HOH   HOH B . 
F 4 HOH   166 366 373  HOH   HOH B . 
F 4 HOH   167 367 898  HOH   HOH B . 
F 4 HOH   168 368 340  HOH   HOH B . 
F 4 HOH   169 369 615  HOH   HOH B . 
F 4 HOH   170 370 291  HOH   HOH B . 
F 4 HOH   171 371 1303 HOH   HOH B . 
F 4 HOH   172 372 667  HOH   HOH B . 
F 4 HOH   173 373 190  HOH   HOH B . 
F 4 HOH   174 374 310  HOH   HOH B . 
F 4 HOH   175 375 431  HOH   HOH B . 
F 4 HOH   176 376 149  HOH   HOH B . 
F 4 HOH   177 377 183  HOH   HOH B . 
F 4 HOH   178 378 1173 HOH   HOH B . 
F 4 HOH   179 379 1163 HOH   HOH B . 
F 4 HOH   180 380 1000 HOH   HOH B . 
F 4 HOH   181 381 418  HOH   HOH B . 
F 4 HOH   182 382 1311 HOH   HOH B . 
F 4 HOH   183 383 176  HOH   HOH B . 
F 4 HOH   184 384 424  HOH   HOH B . 
F 4 HOH   185 385 491  HOH   HOH B . 
F 4 HOH   186 386 981  HOH   HOH B . 
F 4 HOH   187 387 248  HOH   HOH B . 
F 4 HOH   188 388 470  HOH   HOH B . 
F 4 HOH   189 389 1298 HOH   HOH B . 
F 4 HOH   190 390 265  HOH   HOH B . 
F 4 HOH   191 391 184  HOH   HOH B . 
F 4 HOH   192 392 360  HOH   HOH B . 
F 4 HOH   193 393 355  HOH   HOH B . 
F 4 HOH   194 394 410  HOH   HOH B . 
F 4 HOH   195 395 566  HOH   HOH B . 
F 4 HOH   196 396 274  HOH   HOH B . 
F 4 HOH   197 397 314  HOH   HOH B . 
F 4 HOH   198 398 157  HOH   HOH B . 
F 4 HOH   199 399 792  HOH   HOH B . 
F 4 HOH   200 400 321  HOH   HOH B . 
F 4 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HD6 
_cell.length_a           88.824 
_cell.length_b           88.824 
_cell.length_c           39.578 
_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                         7HD6 
_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          7HD6 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.81 
_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                     7HD6 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.410 
_reflns.d_resolution_high            1.010 
_reflns.number_obs                   161060 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.600 
_reflns.pdbx_Rmerge_I_obs            0.053 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.700 
_reflns.B_iso_Wilson_estimate        12.350 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.058 
_reflns.pdbx_Rpim_I_all              0.023 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1025234 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 1.010 1.030  ? 36809 7382 ? 2.060 ? ? ? 5.000 ? 0.500  ? ? ? ? ? ? 93.400 2.297 0.993 0.338 ? 
1 2 5.530 44.410 ? 7334  1070 ? 0.030 ? ? ? 6.900 ? 48.800 ? ? ? ? ? ? 99.800 0.033 0.012 0.999 ? 
# 
_refine.entry_id                                 7HD6 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0100 
_refine.ls_d_res_low                             44.4100 
_refine.pdbx_ls_sigma_F                          1.330 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.3300 
_refine.ls_number_reflns_obs                     160598 
_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                          0.1494 
_refine.ls_R_factor_R_work                       0.1487 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1642 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  7751 
_refine.ls_number_reflns_R_work                  152847 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.9300 
_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                            0.1400 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                70.320 
_refine.B_iso_min                                9.830 
_refine.pdbx_overall_phase_error                 19.9300 
_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                       1.0100 
_refine_hist.d_res_low                        44.4100 
_refine_hist.pdbx_number_atoms_ligand         43 
_refine_hist.number_atoms_solvent             418 
_refine_hist.number_atoms_total               3003 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           17.56 
_refine_hist.pdbx_B_iso_mean_solvent          31.26 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.R_factor_obs 
1.0100 1.0200  30 85.0000  4312 . 0.4562 0.4663 . 219 0.0000 4531 . 'X-RAY DIFFRACTION' . 
1.0200 1.0300  30 98.0000  5030 . 0.4028 0.4283 . 219 0.0000 5249 . 'X-RAY DIFFRACTION' . 
1.0300 1.0500  30 100.0000 5069 . 0.3504 0.3212 . 280 0.0000 5349 . 'X-RAY DIFFRACTION' . 
1.0500 1.0600  30 100.0000 5049 . 0.3099 0.3184 . 299 0.0000 5348 . 'X-RAY DIFFRACTION' . 
1.0600 1.0700  30 100.0000 5064 . 0.3002 0.3173 . 272 0.0000 5336 . 'X-RAY DIFFRACTION' . 
1.0700 1.0900  30 100.0000 5109 . 0.2888 0.3277 . 235 0.0000 5344 . 'X-RAY DIFFRACTION' . 
1.0900 1.1000  30 100.0000 5123 . 0.2562 0.2682 . 268 0.0000 5391 . 'X-RAY DIFFRACTION' . 
1.1000 1.1200  30 100.0000 5091 . 0.2239 0.2269 . 259 0.0000 5350 . 'X-RAY DIFFRACTION' . 
1.1200 1.1400  30 100.0000 5146 . 0.2003 0.2494 . 230 0.0000 5376 . 'X-RAY DIFFRACTION' . 
1.1400 1.1600  30 100.0000 5124 . 0.1857 0.1862 . 253 0.0000 5377 . 'X-RAY DIFFRACTION' . 
1.1600 1.1800  30 100.0000 5085 . 0.1645 0.1996 . 267 0.0000 5352 . 'X-RAY DIFFRACTION' . 
1.1800 1.2000  30 100.0000 5121 . 0.1518 0.1890 . 251 0.0000 5372 . 'X-RAY DIFFRACTION' . 
1.2000 1.2200  30 100.0000 5042 . 0.1387 0.1722 . 279 0.0000 5321 . 'X-RAY DIFFRACTION' . 
1.2200 1.2500  30 100.0000 5157 . 0.1340 0.1579 . 243 0.0000 5400 . 'X-RAY DIFFRACTION' . 
1.2500 1.2700  30 100.0000 5110 . 0.1353 0.1622 . 237 0.0000 5347 . 'X-RAY DIFFRACTION' . 
1.2700 1.3000  30 100.0000 5105 . 0.1335 0.1542 . 252 0.0000 5357 . 'X-RAY DIFFRACTION' . 
1.3000 1.3300  30 100.0000 5104 . 0.1330 0.1559 . 292 0.0000 5396 . 'X-RAY DIFFRACTION' . 
1.3300 1.3700  30 100.0000 5131 . 0.1393 0.1699 . 271 0.0000 5402 . 'X-RAY DIFFRACTION' . 
1.3700 1.4100  30 100.0000 5158 . 0.1285 0.1822 . 228 0.0000 5386 . 'X-RAY DIFFRACTION' . 
1.4100 1.4600  30 100.0000 5076 . 0.1271 0.1514 . 267 0.0000 5343 . 'X-RAY DIFFRACTION' . 
1.4600 1.5100  30 100.0000 5116 . 0.1189 0.1334 . 252 0.0000 5368 . 'X-RAY DIFFRACTION' . 
1.5100 1.5700  30 100.0000 5151 . 0.1186 0.1381 . 271 0.0000 5422 . 'X-RAY DIFFRACTION' . 
1.5700 1.6400  30 100.0000 5102 . 0.1194 0.1371 . 267 0.0000 5369 . 'X-RAY DIFFRACTION' . 
1.6400 1.7300  30 100.0000 5202 . 0.1241 0.1499 . 229 0.0000 5431 . 'X-RAY DIFFRACTION' . 
1.7300 1.8400  30 100.0000 5110 . 0.1328 0.1397 . 260 0.0000 5370 . 'X-RAY DIFFRACTION' . 
1.8400 1.9800  30 100.0000 5151 . 0.1331 0.1353 . 283 0.0000 5434 . 'X-RAY DIFFRACTION' . 
1.9800 2.1800  30 100.0000 5115 . 0.1375 0.1536 . 285 0.0000 5400 . 'X-RAY DIFFRACTION' . 
2.1800 2.4900  30 100.0000 5163 . 0.1368 0.1388 . 265 0.0000 5428 . 'X-RAY DIFFRACTION' . 
2.4900 3.1400  30 100.0000 5208 . 0.1495 0.1594 . 257 0.0000 5465 . 'X-RAY DIFFRACTION' . 
3.1400 44.4100 30 100.0000 5323 . 0.1493 0.1693 . 261 0.0000 5584 . 'X-RAY DIFFRACTION' . 
# 
_struct.entry_id                  7HD6 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0001445' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HD6 
_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 7HD6 A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HD6 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 7HD6 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HD6 MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HD6 SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HD6 MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HD6 
_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_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              1.59 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 56.13  -132.83 
2 1 ASN A 101 ? B -76.65 22.56   
3 1 SER A 128 ? B 66.39  -4.21   
4 1 HIS B 86  ? ? 57.04  -127.60 
# 
_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 515 ? 5.91 . 
2 1 O ? A HOH 516 ? 5.97 . 
3 1 O ? A HOH 517 ? 7.59 . 
4 1 O ? B HOH 401 ? 6.29 . 
# 
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 
A1A65 N2   N Y N 1   
A1A65 C3   C N N 2   
A1A65 C6   C N N 3   
A1A65 C9   C Y N 4   
A1A65 C12  C Y N 5   
A1A65 C1   C N N 6   
A1A65 C10  C Y N 7   
A1A65 C11  C Y N 8   
A1A65 C13  C Y N 9   
A1A65 C2   C N N 10  
A1A65 C4   C N S 11  
A1A65 C5   C N N 12  
A1A65 C7   C N N 13  
A1A65 C8   C Y N 14  
A1A65 N1   N N N 15  
A1A65 N3   N Y N 16  
A1A65 N4   N Y N 17  
A1A65 O1   O N N 18  
A1A65 H6   H N N 19  
A1A65 H5   H N N 20  
A1A65 H7   H N N 21  
A1A65 H12  H N N 22  
A1A65 H11  H N N 23  
A1A65 H15  H N N 24  
A1A65 H16  H N N 25  
A1A65 H3   H N N 26  
A1A65 H4   H N N 27  
A1A65 H2   H N N 28  
A1A65 H17  H N N 29  
A1A65 H1   H N N 30  
A1A65 H10  H N N 31  
A1A65 H9   H N N 32  
A1A65 H14  H N N 33  
A1A65 H13  H N N 34  
A1A65 H18  H N N 35  
A1A65 H8   H N N 36  
ALA   N    N N N 37  
ALA   CA   C N S 38  
ALA   C    C N N 39  
ALA   O    O N N 40  
ALA   CB   C N N 41  
ALA   OXT  O N N 42  
ALA   H    H N N 43  
ALA   H2   H N N 44  
ALA   HA   H N N 45  
ALA   HB1  H N N 46  
ALA   HB2  H N N 47  
ALA   HB3  H N N 48  
ALA   HXT  H N N 49  
ARG   N    N N N 50  
ARG   CA   C N S 51  
ARG   C    C N N 52  
ARG   O    O N N 53  
ARG   CB   C N N 54  
ARG   CG   C N N 55  
ARG   CD   C N N 56  
ARG   NE   N N N 57  
ARG   CZ   C N N 58  
ARG   NH1  N N N 59  
ARG   NH2  N N N 60  
ARG   OXT  O N N 61  
ARG   H    H N N 62  
ARG   H2   H N N 63  
ARG   HA   H N N 64  
ARG   HB2  H N N 65  
ARG   HB3  H N N 66  
ARG   HG2  H N N 67  
ARG   HG3  H N N 68  
ARG   HD2  H N N 69  
ARG   HD3  H N N 70  
ARG   HE   H N N 71  
ARG   HH11 H N N 72  
ARG   HH12 H N N 73  
ARG   HH21 H N N 74  
ARG   HH22 H N N 75  
ARG   HXT  H N N 76  
ASN   N    N N N 77  
ASN   CA   C N S 78  
ASN   C    C N N 79  
ASN   O    O N N 80  
ASN   CB   C N N 81  
ASN   CG   C N N 82  
ASN   OD1  O N N 83  
ASN   ND2  N N N 84  
ASN   OXT  O N N 85  
ASN   H    H N N 86  
ASN   H2   H N N 87  
ASN   HA   H N N 88  
ASN   HB2  H N N 89  
ASN   HB3  H N N 90  
ASN   HD21 H N N 91  
ASN   HD22 H N N 92  
ASN   HXT  H N N 93  
ASP   N    N N N 94  
ASP   CA   C N S 95  
ASP   C    C N N 96  
ASP   O    O N N 97  
ASP   CB   C N N 98  
ASP   CG   C N N 99  
ASP   OD1  O N N 100 
ASP   OD2  O N N 101 
ASP   OXT  O N N 102 
ASP   H    H N N 103 
ASP   H2   H N N 104 
ASP   HA   H N N 105 
ASP   HB2  H N N 106 
ASP   HB3  H N N 107 
ASP   HD2  H N N 108 
ASP   HXT  H N N 109 
CYS   N    N N N 110 
CYS   CA   C N R 111 
CYS   C    C N N 112 
CYS   O    O N N 113 
CYS   CB   C N N 114 
CYS   SG   S N N 115 
CYS   OXT  O N N 116 
CYS   H    H N N 117 
CYS   H2   H N N 118 
CYS   HA   H N N 119 
CYS   HB2  H N N 120 
CYS   HB3  H N N 121 
CYS   HG   H N N 122 
CYS   HXT  H N N 123 
GLN   N    N N N 124 
GLN   CA   C N S 125 
GLN   C    C N N 126 
GLN   O    O N N 127 
GLN   CB   C N N 128 
GLN   CG   C N N 129 
GLN   CD   C N N 130 
GLN   OE1  O N N 131 
GLN   NE2  N N N 132 
GLN   OXT  O N N 133 
GLN   H    H N N 134 
GLN   H2   H N N 135 
GLN   HA   H N N 136 
GLN   HB2  H N N 137 
GLN   HB3  H N N 138 
GLN   HG2  H N N 139 
GLN   HG3  H N N 140 
GLN   HE21 H N N 141 
GLN   HE22 H N N 142 
GLN   HXT  H N N 143 
GLU   N    N N N 144 
GLU   CA   C N S 145 
GLU   C    C N N 146 
GLU   O    O N N 147 
GLU   CB   C N N 148 
GLU   CG   C N N 149 
GLU   CD   C N N 150 
GLU   OE1  O N N 151 
GLU   OE2  O N N 152 
GLU   OXT  O N N 153 
GLU   H    H N N 154 
GLU   H2   H N N 155 
GLU   HA   H N N 156 
GLU   HB2  H N N 157 
GLU   HB3  H N N 158 
GLU   HG2  H N N 159 
GLU   HG3  H N N 160 
GLU   HE2  H N N 161 
GLU   HXT  H N N 162 
GLY   N    N N N 163 
GLY   CA   C N N 164 
GLY   C    C N N 165 
GLY   O    O N N 166 
GLY   OXT  O N N 167 
GLY   H    H N N 168 
GLY   H2   H N N 169 
GLY   HA2  H N N 170 
GLY   HA3  H N N 171 
GLY   HXT  H N N 172 
HIS   N    N N N 173 
HIS   CA   C N S 174 
HIS   C    C N N 175 
HIS   O    O N N 176 
HIS   CB   C N N 177 
HIS   CG   C Y N 178 
HIS   ND1  N Y N 179 
HIS   CD2  C Y N 180 
HIS   CE1  C Y N 181 
HIS   NE2  N Y N 182 
HIS   OXT  O N N 183 
HIS   H    H N N 184 
HIS   H2   H N N 185 
HIS   HA   H N N 186 
HIS   HB2  H N N 187 
HIS   HB3  H N N 188 
HIS   HD1  H N N 189 
HIS   HD2  H N N 190 
HIS   HE1  H N N 191 
HIS   HE2  H N N 192 
HIS   HXT  H N N 193 
HOH   O    O N N 194 
HOH   H1   H N N 195 
HOH   H2   H N N 196 
ILE   N    N N N 197 
ILE   CA   C N S 198 
ILE   C    C N N 199 
ILE   O    O N N 200 
ILE   CB   C N S 201 
ILE   CG1  C N N 202 
ILE   CG2  C N N 203 
ILE   CD1  C N N 204 
ILE   OXT  O N N 205 
ILE   H    H N N 206 
ILE   H2   H N N 207 
ILE   HA   H N N 208 
ILE   HB   H N N 209 
ILE   HG12 H N N 210 
ILE   HG13 H N N 211 
ILE   HG21 H N N 212 
ILE   HG22 H N N 213 
ILE   HG23 H N N 214 
ILE   HD11 H N N 215 
ILE   HD12 H N N 216 
ILE   HD13 H N N 217 
ILE   HXT  H N N 218 
LEU   N    N N N 219 
LEU   CA   C N S 220 
LEU   C    C N N 221 
LEU   O    O N N 222 
LEU   CB   C N N 223 
LEU   CG   C N N 224 
LEU   CD1  C N N 225 
LEU   CD2  C N N 226 
LEU   OXT  O N N 227 
LEU   H    H N N 228 
LEU   H2   H N N 229 
LEU   HA   H N N 230 
LEU   HB2  H N N 231 
LEU   HB3  H N N 232 
LEU   HG   H N N 233 
LEU   HD11 H N N 234 
LEU   HD12 H N N 235 
LEU   HD13 H N N 236 
LEU   HD21 H N N 237 
LEU   HD22 H N N 238 
LEU   HD23 H N N 239 
LEU   HXT  H N N 240 
LYS   N    N N N 241 
LYS   CA   C N S 242 
LYS   C    C N N 243 
LYS   O    O N N 244 
LYS   CB   C N N 245 
LYS   CG   C N N 246 
LYS   CD   C N N 247 
LYS   CE   C N N 248 
LYS   NZ   N N N 249 
LYS   OXT  O N N 250 
LYS   H    H N N 251 
LYS   H2   H N N 252 
LYS   HA   H N N 253 
LYS   HB2  H N N 254 
LYS   HB3  H N N 255 
LYS   HG2  H N N 256 
LYS   HG3  H N N 257 
LYS   HD2  H N N 258 
LYS   HD3  H N N 259 
LYS   HE2  H N N 260 
LYS   HE3  H N N 261 
LYS   HZ1  H N N 262 
LYS   HZ2  H N N 263 
LYS   HZ3  H N N 264 
LYS   HXT  H N N 265 
MET   N    N N N 266 
MET   CA   C N S 267 
MET   C    C N N 268 
MET   O    O N N 269 
MET   CB   C N N 270 
MET   CG   C N N 271 
MET   SD   S N N 272 
MET   CE   C N N 273 
MET   OXT  O N N 274 
MET   H    H N N 275 
MET   H2   H N N 276 
MET   HA   H N N 277 
MET   HB2  H N N 278 
MET   HB3  H N N 279 
MET   HG2  H N N 280 
MET   HG3  H N N 281 
MET   HE1  H N N 282 
MET   HE2  H N N 283 
MET   HE3  H N N 284 
MET   HXT  H N N 285 
PHE   N    N N N 286 
PHE   CA   C N S 287 
PHE   C    C N N 288 
PHE   O    O N N 289 
PHE   CB   C N N 290 
PHE   CG   C Y N 291 
PHE   CD1  C Y N 292 
PHE   CD2  C Y N 293 
PHE   CE1  C Y N 294 
PHE   CE2  C Y N 295 
PHE   CZ   C Y N 296 
PHE   OXT  O N N 297 
PHE   H    H N N 298 
PHE   H2   H N N 299 
PHE   HA   H N N 300 
PHE   HB2  H N N 301 
PHE   HB3  H N N 302 
PHE   HD1  H N N 303 
PHE   HD2  H N N 304 
PHE   HE1  H N N 305 
PHE   HE2  H N N 306 
PHE   HZ   H N N 307 
PHE   HXT  H N N 308 
PRO   N    N N N 309 
PRO   CA   C N S 310 
PRO   C    C N N 311 
PRO   O    O N N 312 
PRO   CB   C N N 313 
PRO   CG   C N N 314 
PRO   CD   C N N 315 
PRO   OXT  O N N 316 
PRO   H    H N N 317 
PRO   HA   H N N 318 
PRO   HB2  H N N 319 
PRO   HB3  H N N 320 
PRO   HG2  H N N 321 
PRO   HG3  H N N 322 
PRO   HD2  H N N 323 
PRO   HD3  H N N 324 
PRO   HXT  H N N 325 
SER   N    N N N 326 
SER   CA   C N S 327 
SER   C    C N N 328 
SER   O    O N N 329 
SER   CB   C N N 330 
SER   OG   O N N 331 
SER   OXT  O N N 332 
SER   H    H N N 333 
SER   H2   H N N 334 
SER   HA   H N N 335 
SER   HB2  H N N 336 
SER   HB3  H N N 337 
SER   HG   H N N 338 
SER   HXT  H N N 339 
TFA   C1   C N N 340 
TFA   C2   C N N 341 
TFA   O    O N N 342 
TFA   F1   F N N 343 
TFA   F2   F N N 344 
TFA   F3   F N N 345 
TFA   OXT  O N N 346 
TFA   HXT  H N N 347 
THR   N    N N N 348 
THR   CA   C N S 349 
THR   C    C N N 350 
THR   O    O N N 351 
THR   CB   C N R 352 
THR   OG1  O N N 353 
THR   CG2  C N N 354 
THR   OXT  O N N 355 
THR   H    H N N 356 
THR   H2   H N N 357 
THR   HA   H N N 358 
THR   HB   H N N 359 
THR   HG1  H N N 360 
THR   HG21 H N N 361 
THR   HG22 H N N 362 
THR   HG23 H N N 363 
THR   HXT  H N N 364 
TYR   N    N N N 365 
TYR   CA   C N S 366 
TYR   C    C N N 367 
TYR   O    O N N 368 
TYR   CB   C N N 369 
TYR   CG   C Y N 370 
TYR   CD1  C Y N 371 
TYR   CD2  C Y N 372 
TYR   CE1  C Y N 373 
TYR   CE2  C Y N 374 
TYR   CZ   C Y N 375 
TYR   OH   O N N 376 
TYR   OXT  O N N 377 
TYR   H    H N N 378 
TYR   H2   H N N 379 
TYR   HA   H N N 380 
TYR   HB2  H N N 381 
TYR   HB3  H N N 382 
TYR   HD1  H N N 383 
TYR   HD2  H N N 384 
TYR   HE1  H N N 385 
TYR   HE2  H N N 386 
TYR   HH   H N N 387 
TYR   HXT  H N N 388 
VAL   N    N N N 389 
VAL   CA   C N S 390 
VAL   C    C N N 391 
VAL   O    O N N 392 
VAL   CB   C N N 393 
VAL   CG1  C N N 394 
VAL   CG2  C N N 395 
VAL   OXT  O N N 396 
VAL   H    H N N 397 
VAL   H2   H N N 398 
VAL   HA   H N N 399 
VAL   HB   H N N 400 
VAL   HG11 H N N 401 
VAL   HG12 H N N 402 
VAL   HG13 H N N 403 
VAL   HG21 H N N 404 
VAL   HG22 H N N 405 
VAL   HG23 H N N 406 
VAL   HXT  H N N 407 
# 
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 
A1A65 C1  C2   sing N N 1   
A1A65 C3  C2   sing N N 2   
A1A65 C5  C6   sing N N 3   
A1A65 C5  C4   sing N N 4   
A1A65 C2  C4   sing N N 5   
A1A65 C2  O1   sing N N 6   
A1A65 C6  C7   sing N N 7   
A1A65 C7  N1   sing N N 8   
A1A65 C4  N1   sing N N 9   
A1A65 N1  C8   sing N N 10  
A1A65 C8  C11  doub Y N 11  
A1A65 C8  N2   sing Y N 12  
A1A65 C12 C11  sing Y N 13  
A1A65 C12 C13  doub Y N 14  
A1A65 C11 C10  sing Y N 15  
A1A65 N2  C9   doub Y N 16  
A1A65 C13 N4   sing Y N 17  
A1A65 C9  N3   sing Y N 18  
A1A65 C10 N4   sing Y N 19  
A1A65 C10 N3   doub Y N 20  
A1A65 C3  H6   sing N N 21  
A1A65 C3  H5   sing N N 22  
A1A65 C3  H7   sing N N 23  
A1A65 C6  H12  sing N N 24  
A1A65 C6  H11  sing N N 25  
A1A65 C9  H15  sing N N 26  
A1A65 C12 H16  sing N N 27  
A1A65 C1  H3   sing N N 28  
A1A65 C1  H4   sing N N 29  
A1A65 C1  H2   sing N N 30  
A1A65 C13 H17  sing N N 31  
A1A65 C4  H1   sing N N 32  
A1A65 C5  H10  sing N N 33  
A1A65 C5  H9   sing N N 34  
A1A65 C7  H14  sing N N 35  
A1A65 C7  H13  sing N N 36  
A1A65 N4  H18  sing N N 37  
A1A65 O1  H8   sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
HIS   N   CA   sing N N 167 
HIS   N   H    sing N N 168 
HIS   N   H2   sing N N 169 
HIS   CA  C    sing N N 170 
HIS   CA  CB   sing N N 171 
HIS   CA  HA   sing N N 172 
HIS   C   O    doub N N 173 
HIS   C   OXT  sing N N 174 
HIS   CB  CG   sing N N 175 
HIS   CB  HB2  sing N N 176 
HIS   CB  HB3  sing N N 177 
HIS   CG  ND1  sing Y N 178 
HIS   CG  CD2  doub Y N 179 
HIS   ND1 CE1  doub Y N 180 
HIS   ND1 HD1  sing N N 181 
HIS   CD2 NE2  sing Y N 182 
HIS   CD2 HD2  sing N N 183 
HIS   CE1 NE2  sing Y N 184 
HIS   CE1 HE1  sing N N 185 
HIS   NE2 HE2  sing N N 186 
HIS   OXT HXT  sing N N 187 
HOH   O   H1   sing N N 188 
HOH   O   H2   sing N N 189 
ILE   N   CA   sing N N 190 
ILE   N   H    sing N N 191 
ILE   N   H2   sing N N 192 
ILE   CA  C    sing N N 193 
ILE   CA  CB   sing N N 194 
ILE   CA  HA   sing N N 195 
ILE   C   O    doub N N 196 
ILE   C   OXT  sing N N 197 
ILE   CB  CG1  sing N N 198 
ILE   CB  CG2  sing N N 199 
ILE   CB  HB   sing N N 200 
ILE   CG1 CD1  sing N N 201 
ILE   CG1 HG12 sing N N 202 
ILE   CG1 HG13 sing N N 203 
ILE   CG2 HG21 sing N N 204 
ILE   CG2 HG22 sing N N 205 
ILE   CG2 HG23 sing N N 206 
ILE   CD1 HD11 sing N N 207 
ILE   CD1 HD12 sing N N 208 
ILE   CD1 HD13 sing N N 209 
ILE   OXT HXT  sing N N 210 
LEU   N   CA   sing N N 211 
LEU   N   H    sing N N 212 
LEU   N   H2   sing N N 213 
LEU   CA  C    sing N N 214 
LEU   CA  CB   sing N N 215 
LEU   CA  HA   sing N N 216 
LEU   C   O    doub N N 217 
LEU   C   OXT  sing N N 218 
LEU   CB  CG   sing N N 219 
LEU   CB  HB2  sing N N 220 
LEU   CB  HB3  sing N N 221 
LEU   CG  CD1  sing N N 222 
LEU   CG  CD2  sing N N 223 
LEU   CG  HG   sing N N 224 
LEU   CD1 HD11 sing N N 225 
LEU   CD1 HD12 sing N N 226 
LEU   CD1 HD13 sing N N 227 
LEU   CD2 HD21 sing N N 228 
LEU   CD2 HD22 sing N N 229 
LEU   CD2 HD23 sing N N 230 
LEU   OXT HXT  sing N N 231 
LYS   N   CA   sing N N 232 
LYS   N   H    sing N N 233 
LYS   N   H2   sing N N 234 
LYS   CA  C    sing N N 235 
LYS   CA  CB   sing N N 236 
LYS   CA  HA   sing N N 237 
LYS   C   O    doub N N 238 
LYS   C   OXT  sing N N 239 
LYS   CB  CG   sing N N 240 
LYS   CB  HB2  sing N N 241 
LYS   CB  HB3  sing N N 242 
LYS   CG  CD   sing N N 243 
LYS   CG  HG2  sing N N 244 
LYS   CG  HG3  sing N N 245 
LYS   CD  CE   sing N N 246 
LYS   CD  HD2  sing N N 247 
LYS   CD  HD3  sing N N 248 
LYS   CE  NZ   sing N N 249 
LYS   CE  HE2  sing N N 250 
LYS   CE  HE3  sing N N 251 
LYS   NZ  HZ1  sing N N 252 
LYS   NZ  HZ2  sing N N 253 
LYS   NZ  HZ3  sing N N 254 
LYS   OXT HXT  sing N N 255 
MET   N   CA   sing N N 256 
MET   N   H    sing N N 257 
MET   N   H2   sing N N 258 
MET   CA  C    sing N N 259 
MET   CA  CB   sing N N 260 
MET   CA  HA   sing N N 261 
MET   C   O    doub N N 262 
MET   C   OXT  sing N N 263 
MET   CB  CG   sing N N 264 
MET   CB  HB2  sing N N 265 
MET   CB  HB3  sing N N 266 
MET   CG  SD   sing N N 267 
MET   CG  HG2  sing N N 268 
MET   CG  HG3  sing N N 269 
MET   SD  CE   sing N N 270 
MET   CE  HE1  sing N N 271 
MET   CE  HE2  sing N N 272 
MET   CE  HE3  sing N N 273 
MET   OXT HXT  sing N N 274 
PHE   N   CA   sing N N 275 
PHE   N   H    sing N N 276 
PHE   N   H2   sing N N 277 
PHE   CA  C    sing N N 278 
PHE   CA  CB   sing N N 279 
PHE   CA  HA   sing N N 280 
PHE   C   O    doub N N 281 
PHE   C   OXT  sing N N 282 
PHE   CB  CG   sing N N 283 
PHE   CB  HB2  sing N N 284 
PHE   CB  HB3  sing N N 285 
PHE   CG  CD1  doub Y N 286 
PHE   CG  CD2  sing Y N 287 
PHE   CD1 CE1  sing Y N 288 
PHE   CD1 HD1  sing N N 289 
PHE   CD2 CE2  doub Y N 290 
PHE   CD2 HD2  sing N N 291 
PHE   CE1 CZ   doub Y N 292 
PHE   CE1 HE1  sing N N 293 
PHE   CE2 CZ   sing Y N 294 
PHE   CE2 HE2  sing N N 295 
PHE   CZ  HZ   sing N N 296 
PHE   OXT HXT  sing N N 297 
PRO   N   CA   sing N N 298 
PRO   N   CD   sing N N 299 
PRO   N   H    sing N N 300 
PRO   CA  C    sing N N 301 
PRO   CA  CB   sing N N 302 
PRO   CA  HA   sing N N 303 
PRO   C   O    doub N N 304 
PRO   C   OXT  sing N N 305 
PRO   CB  CG   sing N N 306 
PRO   CB  HB2  sing N N 307 
PRO   CB  HB3  sing N N 308 
PRO   CG  CD   sing N N 309 
PRO   CG  HG2  sing N N 310 
PRO   CG  HG3  sing N N 311 
PRO   CD  HD2  sing N N 312 
PRO   CD  HD3  sing N N 313 
PRO   OXT HXT  sing N N 314 
SER   N   CA   sing N N 315 
SER   N   H    sing N N 316 
SER   N   H2   sing N N 317 
SER   CA  C    sing N N 318 
SER   CA  CB   sing N N 319 
SER   CA  HA   sing N N 320 
SER   C   O    doub N N 321 
SER   C   OXT  sing N N 322 
SER   CB  OG   sing N N 323 
SER   CB  HB2  sing N N 324 
SER   CB  HB3  sing N N 325 
SER   OG  HG   sing N N 326 
SER   OXT HXT  sing N N 327 
TFA   C1  C2   sing N N 328 
TFA   C1  O    doub N N 329 
TFA   C1  OXT  sing N N 330 
TFA   C2  F1   sing N N 331 
TFA   C2  F2   sing N N 332 
TFA   C2  F3   sing N N 333 
TFA   OXT HXT  sing N N 334 
THR   N   CA   sing N N 335 
THR   N   H    sing N N 336 
THR   N   H2   sing N N 337 
THR   CA  C    sing N N 338 
THR   CA  CB   sing N N 339 
THR   CA  HA   sing N N 340 
THR   C   O    doub N N 341 
THR   C   OXT  sing N N 342 
THR   CB  OG1  sing N N 343 
THR   CB  CG2  sing N N 344 
THR   CB  HB   sing N N 345 
THR   OG1 HG1  sing N N 346 
THR   CG2 HG21 sing N N 347 
THR   CG2 HG22 sing N N 348 
THR   CG2 HG23 sing N N 349 
THR   OXT HXT  sing N N 350 
TYR   N   CA   sing N N 351 
TYR   N   H    sing N N 352 
TYR   N   H2   sing N N 353 
TYR   CA  C    sing N N 354 
TYR   CA  CB   sing N N 355 
TYR   CA  HA   sing N N 356 
TYR   C   O    doub N N 357 
TYR   C   OXT  sing N N 358 
TYR   CB  CG   sing N N 359 
TYR   CB  HB2  sing N N 360 
TYR   CB  HB3  sing N N 361 
TYR   CG  CD1  doub Y N 362 
TYR   CG  CD2  sing Y N 363 
TYR   CD1 CE1  sing Y N 364 
TYR   CD1 HD1  sing N N 365 
TYR   CD2 CE2  doub Y N 366 
TYR   CD2 HD2  sing N N 367 
TYR   CE1 CZ   doub Y N 368 
TYR   CE1 HE1  sing N N 369 
TYR   CE2 CZ   sing Y N 370 
TYR   CE2 HE2  sing N N 371 
TYR   CZ  OH   sing N N 372 
TYR   OH  HH   sing N N 373 
TYR   OXT HXT  sing N N 374 
VAL   N   CA   sing N N 375 
VAL   N   H    sing N N 376 
VAL   N   H2   sing N N 377 
VAL   CA  C    sing N N 378 
VAL   CA  CB   sing N N 379 
VAL   CA  HA   sing N N 380 
VAL   C   O    doub N N 381 
VAL   C   OXT  sing N N 382 
VAL   CB  CG1  sing N N 383 
VAL   CB  CG2  sing N N 384 
VAL   CB  HB   sing N N 385 
VAL   CG1 HG11 sing N N 386 
VAL   CG1 HG12 sing N N 387 
VAL   CG1 HG13 sing N N 388 
VAL   CG2 HG21 sing N N 389 
VAL   CG2 HG22 sing N N 390 
VAL   CG2 HG23 sing N N 391 
VAL   OXT HXT  sing N N 392 
# 
_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                    7HD6 
_atom_sites.fract_transf_matrix[1][1]   0.011258 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011258 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.025267 
_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   ? 19.685 -16.286 22.254  0.76 52.22 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.589 -16.255 22.356  0.24 51.25 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.712 -15.214 22.428  0.76 51.86 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.652 -15.153 22.544  0.24 51.00 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.360 -13.862 22.141  0.76 50.53 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.322 -13.826 22.213  0.24 50.07 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.485 -13.601 22.567  0.76 50.86 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.428 -13.546 22.674  0.24 50.36 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.080 -15.255 23.835  0.76 52.50 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.079 -15.144 23.975  0.24 51.42 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.064 -14.133 24.001  0.76 52.73 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.105 -13.986 24.150  0.24 51.62 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.429 -16.609 24.084  0.76 52.79 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.400 -16.469 24.285  0.24 51.63 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.997 -15.334 21.788  0.76 62.23 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.908 -15.264 21.935  0.24 61.20 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.775 -15.131 24.500  0.76 63.00 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.804 -15.024 24.607  0.24 61.71 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.556 -14.286 24.814  0.76 63.28 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.618 -14.108 24.980  0.24 61.94 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.532 -13.286 24.061  0.76 63.28 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.602 -13.154 24.179  0.24 61.94 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.467 -14.131 23.237  0.76 63.28 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.486 -13.978 23.403  0.24 61.94 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.980 -16.590 24.944  0.76 63.35 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.987 -16.415 25.161  0.24 61.96 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.786 -16.784 23.379  0.76 63.35 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.724 -16.642 23.611  0.24 61.96 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.115 -17.295 24.084  0.76 63.35 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.065 -17.175 24.276  0.24 61.96 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.645 -13.012 21.406  1.00 48.46 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.099 -11.666 21.076  1.00 44.66 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 17.954 -10.684 21.314  1.00 41.59 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.842 -11.072 21.687  1.00 41.58 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.657 -11.579 19.647  1.00 43.78 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.637 -11.949 18.592  1.00 42.97 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.532 -11.408 18.562  1.00 42.41 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 19.008 -12.877 17.713  1.00 42.65 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.873 -13.202 21.076  0.76 58.16 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.898 -13.223 21.033  0.24 58.16 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.820 -11.430 21.674  1.00 53.59 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 19.946 -10.668 19.476  1.00 52.54 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.408 -12.185 19.563  1.00 52.54 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.468 -13.123 17.090  1.00 51.18 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.790 -13.233 17.767  1.00 51.18 ?  4   ASN   A HD22 1 
ATOM   46   N N    . SER   A 1 5   ? 18.229 -9.398  21.093  1.00 38.32 ?  5   SER   A N    1 
ATOM   47   C CA   . SER   A 1 5   ? 17.319 -8.326  21.475  1.00 35.38 ?  5   SER   A CA   1 
ATOM   48   C C    . SER   A 1 5   ? 16.443 -7.827  20.326  1.00 31.21 ?  5   SER   A C    1 
ATOM   49   O O    . SER   A 1 5   ? 15.728 -6.835  20.498  1.00 31.68 ?  5   SER   A O    1 
ATOM   50   C CB   . SER   A 1 5   ? 18.096 -7.162  22.097  1.00 36.32 ?  5   SER   A CB   1 
ATOM   51   O OG   . SER   A 1 5   ? 19.008 -6.599  21.171  1.00 37.06 ?  5   SER   A OG   1 
ATOM   52   H H    . SER   A 1 5   ? 18.951 -9.122  20.714  1.00 45.98 ?  5   SER   A H    1 
ATOM   53   H HA   . SER   A 1 5   ? 16.725 -8.662  22.159  1.00 42.46 ?  5   SER   A HA   1 
ATOM   54   H HB2  . SER   A 1 5   ? 17.468 -6.475  22.377  1.00 43.58 ?  5   SER   A HB2  1 
ATOM   55   H HB3  . SER   A 1 5   ? 18.590 -7.487  22.869  1.00 43.58 ?  5   SER   A HB3  1 
ATOM   56   H HG   . SER   A 1 5   ? 19.427 -5.962  21.530  1.00 44.48 ?  5   SER   A HG   1 
ATOM   57   N N    . PHE   A 1 6   ? 16.473 -8.483  19.169  1.00 26.66 ?  6   PHE   A N    1 
ATOM   58   C CA   . PHE   A 1 6   ? 15.561 -8.115  18.091  1.00 22.90 ?  6   PHE   A CA   1 
ATOM   59   C C    . PHE   A 1 6   ? 14.133 -8.484  18.480  1.00 23.16 ?  6   PHE   A C    1 
ATOM   60   O O    . PHE   A 1 6   ? 13.875 -9.598  18.941  1.00 24.71 ?  6   PHE   A O    1 
ATOM   61   C CB   . PHE   A 1 6   ? 15.958 -8.826  16.802  1.00 20.42 ?  6   PHE   A CB   1 
ATOM   62   C CG   . PHE   A 1 6   ? 17.245 -8.318  16.203  1.00 19.68 ?  6   PHE   A CG   1 
ATOM   63   C CD1  . PHE   A 1 6   ? 17.270 -7.130  15.498  1.00 19.40 ?  6   PHE   A CD1  1 
ATOM   64   C CD2  . PHE   A 1 6   ? 18.421 -9.035  16.337  1.00 20.39 ?  6   PHE   A CD2  1 
ATOM   65   C CE1  . PHE   A 1 6   ? 18.451 -6.659  14.943  1.00 19.82 ?  6   PHE   A CE1  1 
ATOM   66   C CE2  . PHE   A 1 6   ? 19.600 -8.576  15.784  1.00 20.82 ?  6   PHE   A CE2  1 
ATOM   67   C CZ   . PHE   A 1 6   ? 19.617 -7.386  15.086  1.00 20.21 ?  6   PHE   A CZ   1 
ATOM   68   H H    . PHE   A 1 6   ? 16.999 -9.140  18.989  1.00 31.99 ?  6   PHE   A H    1 
ATOM   69   H HA   . PHE   A 1 6   ? 15.602 -7.162  17.948  1.00 27.48 ?  6   PHE   A HA   1 
ATOM   70   H HB2  . PHE   A 1 6   ? 16.067 -9.775  16.987  1.00 24.51 ?  6   PHE   A HB2  1 
ATOM   71   H HB3  . PHE   A 1 6   ? 15.253 -8.702  16.147  1.00 24.51 ?  6   PHE   A HB3  1 
ATOM   72   H HD1  . PHE   A 1 6   ? 16.488 -6.639  15.397  1.00 23.28 ?  6   PHE   A HD1  1 
ATOM   73   H HD2  . PHE   A 1 6   ? 18.413 -9.840  16.809  1.00 24.47 ?  6   PHE   A HD2  1 
ATOM   74   H HE1  . PHE   A 1 6   ? 18.460 -5.856  14.470  1.00 23.79 ?  6   PHE   A HE1  1 
ATOM   75   H HE2  . PHE   A 1 6   ? 20.383 -9.066  15.886  1.00 24.99 ?  6   PHE   A HE2  1 
ATOM   76   H HZ   . PHE   A 1 6   ? 20.410 -7.072  14.715  1.00 24.25 ?  6   PHE   A HZ   1 
ATOM   77   N N    A SER   A 1 7   ? 13.198 -7.561  18.247  0.76 22.00 ?  7   SER   A N    1 
ATOM   78   N N    B SER   A 1 7   ? 13.208 -7.539  18.325  0.24 23.05 ?  7   SER   A N    1 
ATOM   79   C CA   A SER   A 1 7   ? 11.825 -7.700  18.719  0.76 22.75 ?  7   SER   A CA   1 
ATOM   80   C CA   B SER   A 1 7   ? 11.854 -7.689  18.839  0.24 23.19 ?  7   SER   A CA   1 
ATOM   81   C C    A SER   A 1 7   ? 10.831 -7.484  17.583  0.76 20.81 ?  7   SER   A C    1 
ATOM   82   C C    B SER   A 1 7   ? 10.840 -7.282  17.779  0.24 21.97 ?  7   SER   A C    1 
ATOM   83   O O    A SER   A 1 7   ? 11.014 -6.601  16.740  0.76 21.00 ?  7   SER   A O    1 
ATOM   84   O O    B SER   A 1 7   ? 11.084 -6.380  16.973  0.24 22.12 ?  7   SER   A O    1 
ATOM   85   C CB   A SER   A 1 7   ? 11.546 -6.688  19.842  0.76 25.21 ?  7   SER   A CB   1 
ATOM   86   C CB   B SER   A 1 7   ? 11.647 -6.848  20.111  0.24 24.28 ?  7   SER   A CB   1 
ATOM   87   O OG   A SER   A 1 7   ? 10.190 -6.719  20.243  0.76 27.32 ?  7   SER   A OG   1 
ATOM   88   O OG   B SER   A 1 7   ? 10.345 -7.028  20.638  0.24 25.17 ?  7   SER   A OG   1 
ATOM   89   H H    A SER   A 1 7   ? 13.340 -6.839  17.805  0.76 26.40 ?  7   SER   A H    1 
ATOM   90   H H    B SER   A 1 7   ? 13.343 -6.796  17.916  0.24 27.66 ?  7   SER   A H    1 
ATOM   91   H HA   A SER   A 1 7   ? 11.692 -8.593  19.076  0.76 27.30 ?  7   SER   A HA   1 
ATOM   92   H HA   B SER   A 1 7   ? 11.693 -8.616  19.065  0.24 27.83 ?  7   SER   A HA   1 
ATOM   93   H HB2  A SER   A 1 7   ? 12.111 -6.900  20.605  0.76 30.25 ?  7   SER   A HB2  1 
ATOM   94   H HB2  B SER   A 1 7   ? 12.291 -7.125  20.782  0.24 29.14 ?  7   SER   A HB2  1 
ATOM   95   H HB3  A SER   A 1 7   ? 11.753 -5.797  19.521  0.76 30.25 ?  7   SER   A HB3  1 
ATOM   96   H HB3  B SER   A 1 7   ? 11.779 -5.910  19.897  0.24 29.14 ?  7   SER   A HB3  1 
ATOM   97   H HG   A SER   A 1 7   ? 10.061 -6.168  20.865  0.76 32.79 ?  7   SER   A HG   1 
ATOM   98   H HG   B SER   A 1 7   ? 10.244 -6.555  21.325  0.24 30.20 ?  7   SER   A HG   1 
ATOM   99   N N    A GLY   A 1 8   ? 9.771  -8.294  17.570  0.76 19.64 ?  8   GLY   A N    1 
ATOM   100  N N    B GLY   A 1 8   ? 9.696  -7.964  17.792  0.24 20.73 ?  8   GLY   A N    1 
ATOM   101  C CA   A GLY   A 1 8   ? 8.668  -8.067  16.658  0.76 19.15 ?  8   GLY   A CA   1 
ATOM   102  C CA   B GLY   A 1 8   ? 8.622  -7.672  16.864  0.24 19.68 ?  8   GLY   A CA   1 
ATOM   103  C C    A GLY   A 1 8   ? 8.875  -8.548  15.242  0.76 17.84 ?  8   GLY   A C    1 
ATOM   104  C C    B GLY   A 1 8   ? 8.814  -8.215  15.468  0.24 18.24 ?  8   GLY   A C    1 
ATOM   105  O O    A GLY   A 1 8   ? 8.122  -8.141  14.349  0.76 18.55 ?  8   GLY   A O    1 
ATOM   106  O O    B GLY   A 1 8   ? 8.042  -7.856  14.571  0.24 18.55 ?  8   GLY   A O    1 
ATOM   107  H H    A GLY   A 1 8   ? 9.677  -8.982  18.079  0.76 23.57 ?  8   GLY   A H    1 
ATOM   108  H H    B GLY   A 1 8   ? 9.523  -8.608  18.337  0.24 24.87 ?  8   GLY   A H    1 
ATOM   109  H HA2  A GLY   A 1 8   ? 7.879  -8.508  17.013  0.76 22.98 ?  8   GLY   A HA2  1 
ATOM   110  H HA2  B GLY   A 1 8   ? 7.796  -8.041  17.215  0.24 23.61 ?  8   GLY   A HA2  1 
ATOM   111  H HA3  A GLY   A 1 8   ? 8.486  -7.117  16.621  0.76 22.98 ?  8   GLY   A HA3  1 
ATOM   112  H HA3  B GLY   A 1 8   ? 8.516  -6.711  16.799  0.24 23.61 ?  8   GLY   A HA3  1 
ATOM   113  N N    A TYR   A 1 9   ? 9.860  -9.411  15.004  0.76 16.18 ?  9   TYR   A N    1 
ATOM   114  N N    B TYR   A 1 9   ? 9.811  -9.069  15.251  0.24 17.02 ?  9   TYR   A N    1 
ATOM   115  C CA   A TYR   A 1 9   ? 10.118 -9.937  13.672  0.76 14.83 ?  9   TYR   A CA   1 
ATOM   116  C CA   B TYR   A 1 9   ? 10.072 -9.609  13.926  0.24 16.12 ?  9   TYR   A CA   1 
ATOM   117  C C    A TYR   A 1 9   ? 9.252  -11.157 13.394  0.76 14.02 ?  9   TYR   A C    1 
ATOM   118  C C    B TYR   A 1 9   ? 9.183  -10.812 13.638  0.24 15.46 ?  9   TYR   A C    1 
ATOM   119  O O    A TYR   A 1 9   ? 8.995  -11.977 14.281  0.76 15.56 ?  9   TYR   A O    1 
ATOM   120  O O    B TYR   A 1 9   ? 8.793  -11.560 14.539  0.24 15.60 ?  9   TYR   A O    1 
ATOM   121  C CB   A TYR   A 1 9   ? 11.595 -10.320 13.507  0.76 15.02 ?  9   TYR   A CB   1 
ATOM   122  C CB   B TYR   A 1 9   ? 11.536 -10.036 13.797  0.24 16.34 ?  9   TYR   A CB   1 
ATOM   123  C CG   A TYR   A 1 9   ? 12.497 -9.117  13.353  0.76 15.27 ?  9   TYR   A CG   1 
ATOM   124  C CG   B TYR   A 1 9   ? 12.504 -8.891  13.604  0.24 16.48 ?  9   TYR   A CG   1 
ATOM   125  C CD1  A TYR   A 1 9   ? 12.825 -8.336  14.449  0.76 15.54 ?  9   TYR   A CD1  1 
ATOM   126  C CD1  B TYR   A 1 9   ? 12.806 -8.030  14.648  0.24 16.91 ?  9   TYR   A CD1  1 
ATOM   127  C CD2  A TYR   A 1 9   ? 12.988 -8.744  12.109  0.76 14.91 ?  9   TYR   A CD2  1 
ATOM   128  C CD2  B TYR   A 1 9   ? 13.121 -8.677  12.378  0.24 16.01 ?  9   TYR   A CD2  1 
ATOM   129  C CE1  A TYR   A 1 9   ? 13.625 -7.214  14.317  0.76 16.42 ?  9   TYR   A CE1  1 
ATOM   130  C CE1  B TYR   A 1 9   ? 13.689 -6.982  14.477  0.24 16.97 ?  9   TYR   A CE1  1 
ATOM   131  C CE2  A TYR   A 1 9   ? 13.792 -7.625  11.963  0.76 15.28 ?  9   TYR   A CE2  1 
ATOM   132  C CE2  B TYR   A 1 9   ? 14.003 -7.629  12.195  0.24 16.23 ?  9   TYR   A CE2  1 
ATOM   133  C CZ   A TYR   A 1 9   ? 14.107 -6.862  13.067  0.76 16.41 ?  9   TYR   A CZ   1 
ATOM   134  C CZ   B TYR   A 1 9   ? 14.285 -6.786  13.249  0.24 16.86 ?  9   TYR   A CZ   1 
ATOM   135  O OH   A TYR   A 1 9   ? 14.900 -5.748  12.909  0.76 17.88 ?  9   TYR   A OH   1 
ATOM   136  O OH   B TYR   A 1 9   ? 15.165 -5.743  13.074  0.24 17.65 ?  9   TYR   A OH   1 
ATOM   137  H H    A TYR   A 1 9   ? 10.389 -9.718  15.608  0.76 19.42 ?  9   TYR   A H    1 
ATOM   138  H H    B TYR   A 1 9   ? 10.352 -9.347  15.859  0.24 20.43 ?  9   TYR   A H    1 
ATOM   139  H HA   A TYR   A 1 9   ? 9.907  -9.264  13.014  0.76 17.80 ?  9   TYR   A HA   1 
ATOM   140  H HA   B TYR   A 1 9   ? 9.892  -8.926  13.262  0.24 19.35 ?  9   TYR   A HA   1 
ATOM   141  H HB2  A TYR   A 1 9   ? 11.888 -10.825 14.284  0.76 18.02 ?  9   TYR   A HB2  1 
ATOM   142  H HB2  B TYR   A 1 9   ? 11.795 -10.511 14.600  0.24 19.61 ?  9   TYR   A HB2  1 
ATOM   143  H HB3  A TYR   A 1 9   ? 11.681 -10.865 12.708  0.76 18.02 ?  9   TYR   A HB3  1 
ATOM   144  H HB3  B TYR   A 1 9   ? 11.618 -10.623 13.029  0.24 19.61 ?  9   TYR   A HB3  1 
ATOM   145  H HD1  A TYR   A 1 9   ? 12.493 -8.571  15.289  0.76 18.65 ?  9   TYR   A HD1  1 
ATOM   146  H HD1  B TYR   A 1 9   ? 12.402 -8.158  15.476  0.24 20.30 ?  9   TYR   A HD1  1 
ATOM   147  H HD2  A TYR   A 1 9   ? 12.770 -9.254  11.360  0.76 17.89 ?  9   TYR   A HD2  1 
ATOM   148  H HD2  B TYR   A 1 9   ? 12.934 -9.243  11.664  0.24 19.21 ?  9   TYR   A HD2  1 
ATOM   149  H HE1  A TYR   A 1 9   ? 13.836 -6.703  15.065  0.76 19.71 ?  9   TYR   A HE1  1 
ATOM   150  H HE1  B TYR   A 1 9   ? 13.879 -6.410  15.186  0.24 20.36 ?  9   TYR   A HE1  1 
ATOM   151  H HE2  A TYR   A 1 9   ? 14.115 -7.387  11.123  0.76 18.33 ?  9   TYR   A HE2  1 
ATOM   152  H HE2  B TYR   A 1 9   ? 14.412 -7.496  11.369  0.24 19.48 ?  9   TYR   A HE2  1 
ATOM   153  H HH   A TYR   A 1 9   ? 15.024 -5.380  13.657  0.76 21.46 ?  9   TYR   A HH   1 
ATOM   154  H HH   B TYR   A 1 9   ? 15.244 -5.314  13.792  0.24 21.17 ?  9   TYR   A HH   1 
ATOM   155  N N    A LEU   A 1 10  ? 8.819  -11.272 12.145  0.76 13.72 ?  10  LEU   A N    1 
ATOM   156  N N    B LEU   A 1 10  ? 8.864  -10.985 12.359  0.24 15.16 ?  10  LEU   A N    1 
ATOM   157  C CA   A LEU   A 1 10  ? 8.237  -12.505 11.642  0.76 13.70 ?  10  LEU   A CA   1 
ATOM   158  C CA   B LEU   A 1 10  ? 8.163  -12.155 11.854  0.24 14.78 ?  10  LEU   A CA   1 
ATOM   159  C C    A LEU   A 1 10  ? 9.369  -13.438 11.217  0.76 13.51 ?  10  LEU   A C    1 
ATOM   160  C C    B LEU   A 1 10  ? 9.202  -13.139 11.334  0.24 14.38 ?  10  LEU   A C    1 
ATOM   161  O O    A LEU   A 1 10  ? 10.345 -13.002 10.603  0.76 13.33 ?  10  LEU   A O    1 
ATOM   162  O O    B LEU   A 1 10  ? 10.059 -12.772 10.523  0.24 14.28 ?  10  LEU   A O    1 
ATOM   163  C CB   A LEU   A 1 10  ? 7.356  -12.172 10.439  0.76 14.73 ?  10  LEU   A CB   1 
ATOM   164  C CB   B LEU   A 1 10  ? 7.226  -11.734 10.721  0.24 15.31 ?  10  LEU   A CB   1 
ATOM   165  C CG   A LEU   A 1 10  ? 6.623  -13.324 9.766   0.76 16.41 ?  10  LEU   A CG   1 
ATOM   166  C CG   B LEU   A 1 10  ? 6.286  -12.754 10.081  0.24 16.08 ?  10  LEU   A CG   1 
ATOM   167  C CD1  A LEU   A 1 10  ? 5.543  -13.882 10.673  0.76 18.11 ?  10  LEU   A CD1  1 
ATOM   168  C CD1  B LEU   A 1 10  ? 5.092  -12.003 9.533   0.24 16.79 ?  10  LEU   A CD1  1 
ATOM   169  C CD2  A LEU   A 1 10  ? 6.046  -12.870 8.427   0.76 18.10 ?  10  LEU   A CD2  1 
ATOM   170  C CD2  B LEU   A 1 10  ? 6.960  -13.541 8.967   0.24 15.77 ?  10  LEU   A CD2  1 
ATOM   171  H H    A LEU   A 1 10  ? 8.860  -10.643 11.556  0.76 16.47 ?  10  LEU   A H    1 
ATOM   172  H H    B LEU   A 1 10  ? 9.047  -10.412 11.742  0.24 18.19 ?  10  LEU   A H    1 
ATOM   173  H HA   A LEU   A 1 10  ? 7.701  -12.932 12.330  0.76 16.44 ?  10  LEU   A HA   1 
ATOM   174  H HA   B LEU   A 1 10  ? 7.640  -12.571 12.563  0.24 17.74 ?  10  LEU   A HA   1 
ATOM   175  H HB2  A LEU   A 1 10  ? 6.686  -11.537 10.724  0.76 17.68 ?  10  LEU   A HB2  1 
ATOM   176  H HB2  B LEU   A 1 10  ? 6.667  -11.014 11.056  0.24 18.38 ?  10  LEU   A HB2  1 
ATOM   177  H HB3  A LEU   A 1 10  ? 7.919  -11.765 9.763   0.76 17.68 ?  10  LEU   A HB3  1 
ATOM   178  H HB3  B LEU   A 1 10  ? 7.778  -11.387 10.004  0.24 18.38 ?  10  LEU   A HB3  1 
ATOM   179  H HG   A LEU   A 1 10  ? 7.253  -14.039 9.587   0.76 19.69 ?  10  LEU   A HG   1 
ATOM   180  H HG   B LEU   A 1 10  ? 5.968  -13.375 10.755  0.24 19.30 ?  10  LEU   A HG   1 
ATOM   181  H HD11 A LEU   A 1 10  ? 5.088  -14.609 10.216  0.76 21.73 ?  10  LEU   A HD11 1 
ATOM   182  H HD11 B LEU   A 1 10  ? 4.463  -12.637 9.161   0.24 20.15 ?  10  LEU   A HD11 1 
ATOM   183  H HD12 A LEU   A 1 10  ? 5.951  -14.212 11.489  0.76 21.73 ?  10  LEU   A HD12 1 
ATOM   184  H HD12 B LEU   A 1 10  ? 4.674  -11.503 10.251  0.24 20.15 ?  10  LEU   A HD12 1 
ATOM   185  H HD13 A LEU   A 1 10  ? 4.908  -13.179 10.883  0.76 21.73 ?  10  LEU   A HD13 1 
ATOM   186  H HD13 B LEU   A 1 10  ? 5.396  -11.390 8.843   0.24 20.15 ?  10  LEU   A HD13 1 
ATOM   187  H HD21 A LEU   A 1 10  ? 5.577  -13.617 8.019   0.76 21.72 ?  10  LEU   A HD21 1 
ATOM   188  H HD21 B LEU   A 1 10  ? 6.286  -14.054 8.491   0.24 18.93 ?  10  LEU   A HD21 1 
ATOM   189  H HD22 A LEU   A 1 10  ? 5.432  -12.138 8.581   0.76 21.72 ?  10  LEU   A HD22 1 
ATOM   190  H HD22 B LEU   A 1 10  ? 7.391  -12.920 8.359   0.24 18.93 ?  10  LEU   A HD22 1 
ATOM   191  H HD23 A LEU   A 1 10  ? 6.773  -12.584 7.854   0.76 21.72 ?  10  LEU   A HD23 1 
ATOM   192  H HD23 B LEU   A 1 10  ? 7.617  -14.136 9.354   0.24 18.93 ?  10  LEU   A HD23 1 
ATOM   193  N N    A LYS   A 1 11  ? 9.252  -14.717 11.570  0.76 13.65 ?  11  LYS   A N    1 
ATOM   194  N N    B LYS   A 1 11  ? 9.137  -14.378 11.811  0.24 14.08 ?  11  LYS   A N    1 
ATOM   195  C CA   A LYS   A 1 11  ? 10.258 -15.719 11.238  0.76 13.65 ?  11  LYS   A CA   1 
ATOM   196  C CA   B LYS   A 1 11  ? 10.103 -15.396 11.417  0.24 13.46 ?  11  LYS   A CA   1 
ATOM   197  C C    A LYS   A 1 11  ? 9.909  -16.314 9.881   0.76 13.54 ?  11  LYS   A C    1 
ATOM   198  C C    B LYS   A 1 11  ? 9.708  -15.950 10.054  0.24 12.64 ?  11  LYS   A C    1 
ATOM   199  O O    A LYS   A 1 11  ? 8.843  -16.915 9.729   0.76 15.46 ?  11  LYS   A O    1 
ATOM   200  O O    B LYS   A 1 11  ? 8.581  -16.420 9.873   0.24 12.60 ?  11  LYS   A O    1 
ATOM   201  C CB   A LYS   A 1 11  ? 10.285 -16.798 12.323  0.76 13.56 ?  11  LYS   A CB   1 
ATOM   202  C CB   B LYS   A 1 11  ? 10.154 -16.497 12.476  0.24 13.36 ?  11  LYS   A CB   1 
ATOM   203  C CG   A LYS   A 1 11  ? 11.308 -17.909 12.127  0.76 14.44 ?  11  LYS   A CG   1 
ATOM   204  C CG   B LYS   A 1 11  ? 11.153 -17.606 12.232  0.24 13.25 ?  11  LYS   A CG   1 
ATOM   205  C CD   A LYS   A 1 11  ? 11.395 -18.761 13.395  0.76 15.00 ?  11  LYS   A CD   1 
ATOM   206  C CD   B LYS   A 1 11  ? 11.223 -18.520 13.451  0.24 13.30 ?  11  LYS   A CD   1 
ATOM   207  C CE   A LYS   A 1 11  ? 12.399 -19.901 13.284  0.76 15.20 ?  11  LYS   A CE   1 
ATOM   208  C CE   B LYS   A 1 11  ? 12.131 -19.713 13.212  0.24 13.23 ?  11  LYS   A CE   1 
ATOM   209  N NZ   A LYS   A 1 11  ? 13.778 -19.428 13.015  0.76 15.52 ?  11  LYS   A NZ   1 
ATOM   210  N NZ   B LYS   A 1 11  ? 13.547 -19.310 12.990  0.24 13.57 ?  11  LYS   A NZ   1 
ATOM   211  H H    A LYS   A 1 11  ? 8.576  -15.034 11.999  0.76 16.38 ?  11  LYS   A H    1 
ATOM   212  H H    B LYS   A 1 11  ? 8.534  -14.656 12.357  0.24 16.89 ?  11  LYS   A H    1 
ATOM   213  H HA   A LYS   A 1 11  ? 11.131 -15.300 11.180  0.76 16.38 ?  11  LYS   A HA   1 
ATOM   214  H HA   B LYS   A 1 11  ? 10.978 -14.992 11.340  0.24 16.16 ?  11  LYS   A HA   1 
ATOM   215  H HB2  A LYS   A 1 11  ? 10.484 -16.365 13.168  0.76 16.28 ?  11  LYS   A HB2  1 
ATOM   216  H HB2  B LYS   A 1 11  ? 10.373 -16.088 13.328  0.24 16.03 ?  11  LYS   A HB2  1 
ATOM   217  H HB3  A LYS   A 1 11  ? 9.411  -17.207 12.364  0.76 16.28 ?  11  LYS   A HB3  1 
ATOM   218  H HB3  B LYS   A 1 11  ? 9.290  -16.919 12.526  0.24 16.03 ?  11  LYS   A HB3  1 
ATOM   219  H HG2  A LYS   A 1 11  ? 11.033 -18.475 11.387  0.76 17.33 ?  11  LYS   A HG2  1 
ATOM   220  H HG2  B LYS   A 1 11  ? 10.870 -18.132 11.468  0.24 15.90 ?  11  LYS   A HG2  1 
ATOM   221  H HG3  A LYS   A 1 11  ? 12.181 -17.521 11.951  0.76 17.33 ?  11  LYS   A HG3  1 
ATOM   222  H HG3  B LYS   A 1 11  ? 12.031 -17.226 12.079  0.24 15.90 ?  11  LYS   A HG3  1 
ATOM   223  H HD2  A LYS   A 1 11  ? 11.661 -18.195 14.134  0.76 18.00 ?  11  LYS   A HD2  1 
ATOM   224  H HD2  B LYS   A 1 11  ? 11.571 -18.017 14.206  0.24 15.96 ?  11  LYS   A HD2  1 
ATOM   225  H HD3  A LYS   A 1 11  ? 10.521 -19.147 13.571  0.76 18.00 ?  11  LYS   A HD3  1 
ATOM   226  H HD3  B LYS   A 1 11  ? 10.332 -18.850 13.654  0.24 15.96 ?  11  LYS   A HD3  1 
ATOM   227  H HE2  A LYS   A 1 11  ? 12.409 -20.393 14.119  0.76 18.24 ?  11  LYS   A HE2  1 
ATOM   228  H HE2  B LYS   A 1 11  ? 12.101 -20.295 13.987  0.24 15.87 ?  11  LYS   A HE2  1 
ATOM   229  H HE3  A LYS   A 1 11  ? 12.135 -20.485 12.557  0.76 18.24 ?  11  LYS   A HE3  1 
ATOM   230  H HE3  B LYS   A 1 11  ? 11.827 -20.191 12.424  0.24 15.87 ?  11  LYS   A HE3  1 
ATOM   231  H HZ1  A LYS   A 1 11  ? 14.317 -20.123 12.878  0.76 18.63 ?  11  LYS   A HZ1  1 
ATOM   232  H HZ1  B LYS   A 1 11  ? 14.055 -20.032 12.877  0.24 16.28 ?  11  LYS   A HZ1  1 
ATOM   233  H HZ2  A LYS   A 1 11  ? 13.787 -18.909 12.290  0.76 18.63 ?  11  LYS   A HZ2  1 
ATOM   234  H HZ2  B LYS   A 1 11  ? 13.608 -18.797 12.265  0.24 16.28 ?  11  LYS   A HZ2  1 
ATOM   235  H HZ3  A LYS   A 1 11  ? 14.082 -18.959 13.707  0.76 18.63 ?  11  LYS   A HZ3  1 
ATOM   236  H HZ3  B LYS   A 1 11  ? 13.848 -18.854 13.693  0.24 16.28 ?  11  LYS   A HZ3  1 
ATOM   237  N N    A LEU   A 1 12  ? 10.794 -16.157 8.895   0.76 12.71 ?  12  LEU   A N    1 
ATOM   238  N N    B LEU   A 1 12  ? 10.617 -15.855 9.085   0.24 12.42 ?  12  LEU   A N    1 
ATOM   239  C CA   A LEU   A 1 12  ? 10.543 -16.740 7.580   0.76 13.04 ?  12  LEU   A CA   1 
ATOM   240  C CA   B LEU   A 1 12  ? 10.359 -16.374 7.746   0.24 12.21 ?  12  LEU   A CA   1 
ATOM   241  C C    A LEU   A 1 12  ? 11.131 -18.136 7.438   0.76 13.21 ?  12  LEU   A C    1 
ATOM   242  C C    B LEU   A 1 12  ? 10.915 -17.782 7.571   0.24 12.21 ?  12  LEU   A C    1 
ATOM   243  O O    A LEU   A 1 12  ? 10.505 -19.012 6.829   0.76 13.70 ?  12  LEU   A O    1 
ATOM   244  O O    B LEU   A 1 12  ? 10.232 -18.660 7.033   0.24 12.40 ?  12  LEU   A O    1 
ATOM   245  C CB   A LEU   A 1 12  ? 11.113 -15.852 6.471   0.76 14.02 ?  12  LEU   A CB   1 
ATOM   246  C CB   B LEU   A 1 12  ? 10.952 -15.444 6.684   0.24 12.77 ?  12  LEU   A CB   1 
ATOM   247  C CG   A LEU   A 1 12  ? 10.459 -14.487 6.281   0.76 15.06 ?  12  LEU   A CG   1 
ATOM   248  C CG   B LEU   A 1 12  ? 10.274 -14.088 6.490   0.24 13.33 ?  12  LEU   A CG   1 
ATOM   249  C CD1  A LEU   A 1 12  ? 11.181 -13.730 5.181   0.76 15.52 ?  12  LEU   A CD1  1 
ATOM   250  C CD1  B LEU   A 1 12  ? 11.099 -13.226 5.554   0.24 13.33 ?  12  LEU   A CD1  1 
ATOM   251  C CD2  A LEU   A 1 12  ? 8.982  -14.649 5.954   0.76 16.02 ?  12  LEU   A CD2  1 
ATOM   252  C CD2  B LEU   A 1 12  ? 8.865  -14.256 5.946   0.24 13.76 ?  12  LEU   A CD2  1 
ATOM   253  H H    A LEU   A 1 12  ? 11.544 -15.723 8.956   0.76 15.25 ?  12  LEU   A H    1 
ATOM   254  H H    B LEU   A 1 12  ? 11.388 -15.483 9.179   0.24 14.90 ?  12  LEU   A H    1 
ATOM   255  H HA   A LEU   A 1 12  ? 9.587  -16.810 7.449   0.76 15.65 ?  12  LEU   A HA   1 
ATOM   256  H HA   B LEU   A 1 12  ? 9.402  -16.410 7.605   0.24 14.65 ?  12  LEU   A HA   1 
ATOM   257  H HB2  A LEU   A 1 12  ? 12.052 -15.698 6.656   0.76 16.83 ?  12  LEU   A HB2  1 
ATOM   258  H HB2  B LEU   A 1 12  ? 11.877 -15.273 6.916   0.24 15.33 ?  12  LEU   A HB2  1 
ATOM   259  H HB3  A LEU   A 1 12  ? 11.029 -16.328 5.628   0.76 16.83 ?  12  LEU   A HB3  1 
ATOM   260  H HB3  B LEU   A 1 12  ? 10.916 -15.907 5.831   0.24 15.33 ?  12  LEU   A HB3  1 
ATOM   261  H HG   A LEU   A 1 12  ? 10.540 -13.975 7.099   0.76 18.07 ?  12  LEU   A HG   1 
ATOM   262  H HG   B LEU   A 1 12  ? 10.214 -13.631 7.345   0.24 16.00 ?  12  LEU   A HG   1 
ATOM   263  H HD11 A LEU   A 1 12  ? 10.766 -12.864 5.063   0.76 18.63 ?  12  LEU   A HD11 1 
ATOM   264  H HD11 B LEU   A 1 12  ? 10.658 -12.370 5.439   0.24 16.00 ?  12  LEU   A HD11 1 
ATOM   265  H HD12 A LEU   A 1 12  ? 12.115 -13.619 5.431   0.76 18.63 ?  12  LEU   A HD12 1 
ATOM   266  H HD12 B LEU   A 1 12  ? 11.979 -13.096 5.940   0.24 16.00 ?  12  LEU   A HD12 1 
ATOM   267  H HD13 A LEU   A 1 12  ? 11.125 -14.240 4.355   0.76 18.63 ?  12  LEU   A HD13 1 
ATOM   268  H HD13 B LEU   A 1 12  ? 11.176 -13.676 4.698   0.24 16.00 ?  12  LEU   A HD13 1 
ATOM   269  H HD21 A LEU   A 1 12  ? 8.627  -13.795 5.665   0.76 19.22 ?  12  LEU   A HD21 1 
ATOM   270  H HD21 B LEU   A 1 12  ? 8.503  -13.383 5.728   0.24 16.52 ?  12  LEU   A HD21 1 
ATOM   271  H HD22 A LEU   A 1 12  ? 8.887  -15.304 5.244   0.76 19.22 ?  12  LEU   A HD22 1 
ATOM   272  H HD22 B LEU   A 1 12  ? 8.902  -14.807 5.147   0.24 16.52 ?  12  LEU   A HD22 1 
ATOM   273  H HD23 A LEU   A 1 12  ? 8.516  -14.953 6.747   0.76 19.22 ?  12  LEU   A HD23 1 
ATOM   274  H HD23 B LEU   A 1 12  ? 8.316  -14.685 6.619   0.24 16.52 ?  12  LEU   A HD23 1 
ATOM   275  N N    A THR   A 1 13  ? 12.337 -18.344 7.958   0.76 13.27 ?  13  THR   A N    1 
ATOM   276  N N    B THR   A 1 13  ? 12.152 -18.006 8.006   0.24 12.48 ?  13  THR   A N    1 
ATOM   277  C CA   A THR   A 1 13  ? 13.032 -19.622 7.870   0.76 13.48 ?  13  THR   A CA   1 
ATOM   278  C CA   B THR   A 1 13  ? 12.798 -19.308 7.914   0.24 12.88 ?  13  THR   A CA   1 
ATOM   279  C C    A THR   A 1 13  ? 13.805 -19.834 9.164   0.76 13.38 ?  13  THR   A C    1 
ATOM   280  C C    B THR   A 1 13  ? 13.543 -19.569 9.218   0.24 13.37 ?  13  THR   A C    1 
ATOM   281  O O    A THR   A 1 13  ? 13.728 -19.040 10.107  0.76 13.38 ?  13  THR   A O    1 
ATOM   282  O O    B THR   A 1 13  ? 13.384 -18.851 10.211  0.24 13.52 ?  13  THR   A O    1 
ATOM   283  C CB   A THR   A 1 13  ? 14.015 -19.663 6.694   0.76 14.68 ?  13  THR   A CB   1 
ATOM   284  C CB   B THR   A 1 13  ? 13.751 -19.374 6.712   0.24 13.00 ?  13  THR   A CB   1 
ATOM   285  O OG1  A THR   A 1 13  ? 15.085 -18.754 6.967   0.76 14.27 ?  13  THR   A OG1  1 
ATOM   286  O OG1  B THR   A 1 13  ? 14.781 -18.393 6.873   0.24 12.90 ?  13  THR   A OG1  1 
ATOM   287  C CG2  A THR   A 1 13  ? 13.359 -19.284 5.379   0.76 15.87 ?  13  THR   A CG2  1 
ATOM   288  C CG2  B THR   A 1 13  ? 13.010 -19.129 5.401   0.24 13.54 ?  13  THR   A CG2  1 
ATOM   289  H H    A THR   A 1 13  ? 12.789 -17.740 8.368   0.76 15.92 ?  13  THR   A H    1 
ATOM   290  H H    B THR   A 1 13  ? 12.649 -17.401 8.359   0.24 14.98 ?  13  THR   A H    1 
ATOM   291  H HA   A THR   A 1 13  ? 12.389 -20.343 7.763   0.76 16.18 ?  13  THR   A HA   1 
ATOM   292  H HA   B THR   A 1 13  ? 12.126 -19.997 7.808   0.24 15.45 ?  13  THR   A HA   1 
ATOM   293  H HB   A THR   A 1 13  ? 14.373 -20.562 6.601   0.76 17.61 ?  13  THR   A HB   1 
ATOM   294  H HB   B THR   A 1 13  ? 14.158 -20.256 6.671   0.24 15.61 ?  13  THR   A HB   1 
ATOM   295  H HG1  A THR   A 1 13  ? 15.775 -19.184 7.191   0.76 17.12 ?  13  THR   A HG1  1 
ATOM   296  H HG1  B THR   A 1 13  ? 15.311 -18.419 6.221   0.24 15.48 ?  13  THR   A HG1  1 
ATOM   297  H HG21 A THR   A 1 13  ? 13.981 -19.433 4.646   0.76 19.04 ?  13  THR   A HG21 1 
ATOM   298  H HG21 B THR   A 1 13  ? 13.621 -19.222 4.651   0.24 16.25 ?  13  THR   A HG21 1 
ATOM   299  H HG22 A THR   A 1 13  ? 12.571 -19.830 5.235   0.76 19.04 ?  13  THR   A HG22 1 
ATOM   300  H HG22 B THR   A 1 13  ? 12.293 -19.776 5.300   0.24 16.25 ?  13  THR   A HG22 1 
ATOM   301  H HG23 A THR   A 1 13  ? 13.104 -18.352 5.392   0.76 19.04 ?  13  THR   A HG23 1 
ATOM   302  H HG23 B THR   A 1 13  ? 12.633 -18.237 5.392   0.24 16.25 ?  13  THR   A HG23 1 
ATOM   303  N N    A ASP   A 1 14  ? 14.602 -20.902 9.186   0.76 14.28 ?  14  ASP   A N    1 
ATOM   304  N N    B ASP   A 1 14  ? 14.374 -20.611 9.196   0.24 14.17 ?  14  ASP   A N    1 
ATOM   305  C CA   A ASP   A 1 14  ? 15.448 -21.161 10.338  0.76 15.42 ?  14  ASP   A CA   1 
ATOM   306  C CA   B ASP   A 1 14  ? 15.188 -20.952 10.355  0.24 14.75 ?  14  ASP   A CA   1 
ATOM   307  C C    A ASP   A 1 14  ? 16.277 -19.942 10.733  0.76 14.64 ?  14  ASP   A C    1 
ATOM   308  C C    B ASP   A 1 14  ? 16.102 -19.797 10.746  0.24 14.20 ?  14  ASP   A C    1 
ATOM   309  O O    A ASP   A 1 14  ? 16.538 -19.732 11.923  0.76 15.85 ?  14  ASP   A O    1 
ATOM   310  O O    B ASP   A 1 14  ? 16.255 -19.493 11.935  0.24 14.14 ?  14  ASP   A O    1 
ATOM   311  C CB   A ASP   A 1 14  ? 16.386 -22.326 10.036  0.76 18.51 ?  14  ASP   A CB   1 
ATOM   312  C CB   B ASP   A 1 14  ? 16.008 -22.201 10.038  0.24 16.49 ?  14  ASP   A CB   1 
ATOM   313  C CG   A ASP   A 1 14  ? 17.326 -22.597 11.172  0.76 22.91 ?  14  ASP   A CG   1 
ATOM   314  C CG   B ASP   A 1 14  ? 16.873 -22.638 11.196  0.24 17.96 ?  14  ASP   A CG   1 
ATOM   315  O OD1  A ASP   A 1 14  ? 16.850 -22.999 12.252  0.76 24.55 ?  14  ASP   A OD1  1 
ATOM   316  O OD1  B ASP   A 1 14  ? 16.314 -23.009 12.251  0.24 18.20 ?  14  ASP   A OD1  1 
ATOM   317  O OD2  A ASP   A 1 14  ? 18.539 -22.375 10.991  0.76 25.87 -1 14  ASP   A OD2  1 
ATOM   318  O OD2  B ASP   A 1 14  ? 18.112 -22.620 11.049  0.24 18.97 -1 14  ASP   A OD2  1 
ATOM   319  H H    A ASP   A 1 14  ? 14.684 -21.480 8.550   0.76 17.13 ?  14  ASP   A H    1 
ATOM   320  H H    B ASP   A 1 14  ? 14.489 -21.127 8.526   0.24 17.01 ?  14  ASP   A H    1 
ATOM   321  H HA   A ASP   A 1 14  ? 14.899 -21.414 11.096  0.76 18.50 ?  14  ASP   A HA   1 
ATOM   322  H HA   B ASP   A 1 14  ? 14.615 -21.152 11.110  0.24 17.70 ?  14  ASP   A HA   1 
ATOM   323  H HB2  A ASP   A 1 14  ? 15.854 -23.132 9.865   0.76 22.22 ?  14  ASP   A HB2  1 
ATOM   324  H HB2  B ASP   A 1 14  ? 15.403 -22.931 9.826   0.24 19.78 ?  14  ASP   A HB2  1 
ATOM   325  H HB3  A ASP   A 1 14  ? 16.921 -22.123 9.254   0.76 22.22 ?  14  ASP   A HB3  1 
ATOM   326  H HB3  B ASP   A 1 14  ? 16.581 -22.020 9.273   0.24 19.78 ?  14  ASP   A HB3  1 
ATOM   327  N N    . ASN   A 1 15  ? 16.707 -19.131 9.759   1.00 14.22 ?  15  ASN   A N    1 
ATOM   328  C CA   . ASN   A 1 15  ? 17.701 -18.088 10.020  1.00 14.56 ?  15  ASN   A CA   1 
ATOM   329  C C    . ASN   A 1 15  ? 17.338 -16.691 9.528   1.00 14.78 ?  15  ASN   A C    1 
ATOM   330  O O    . ASN   A 1 15  ? 18.108 -15.757 9.780   1.00 16.30 ?  15  ASN   A O    1 
ATOM   331  C CB   . ASN   A 1 15  ? 19.071 -18.482 9.436   1.00 14.14 ?  15  ASN   A CB   1 
ATOM   332  C CG   . ASN   A 1 15  ? 19.054 -18.576 7.927   1.00 14.50 ?  15  ASN   A CG   1 
ATOM   333  O OD1  . ASN   A 1 15  ? 18.336 -19.402 7.357   1.00 15.51 ?  15  ASN   A OD1  1 
ATOM   334  N ND2  . ASN   A 1 15  ? 19.844 -17.731 7.266   1.00 14.68 ?  15  ASN   A ND2  1 
ATOM   335  H H    A ASN   A 1 15  ? 16.435 -19.165 8.949   0.76 17.06 ?  15  ASN   A H    1 
ATOM   336  H H    B ASN   A 1 15  ? 16.558 -19.270 8.927   0.24 17.06 ?  15  ASN   A H    1 
ATOM   337  H HA   . ASN   A 1 15  ? 17.827 -18.023 10.979  1.00 17.47 ?  15  ASN   A HA   1 
ATOM   338  H HB2  . ASN   A 1 15  ? 19.731 -17.810 9.691   1.00 16.96 ?  15  ASN   A HB2  1 
ATOM   339  H HB3  . ASN   A 1 15  ? 19.337 -19.347 9.786   1.00 16.96 ?  15  ASN   A HB3  1 
ATOM   340  H HD21 . ASN   A 1 15  ? 19.870 -17.743 6.405   1.00 17.62 ?  15  ASN   A HD21 1 
ATOM   341  H HD22 . ASN   A 1 15  ? 20.339 -17.164 7.696   1.00 17.62 ?  15  ASN   A HD22 1 
ATOM   342  N N    . VAL   A 1 16  ? 16.204 -16.508 8.852   1.00 14.26 ?  16  VAL   A N    1 
ATOM   343  C CA   . VAL   A 1 16  ? 15.817 -15.225 8.278   1.00 13.68 ?  16  VAL   A CA   1 
ATOM   344  C C    . VAL   A 1 16  ? 14.546 -14.723 8.950   1.00 13.38 ?  16  VAL   A C    1 
ATOM   345  O O    . VAL   A 1 16  ? 13.541 -15.446 9.033   1.00 13.85 ?  16  VAL   A O    1 
ATOM   346  C CB   . VAL   A 1 16  ? 15.641 -15.297 6.751   1.00 14.43 ?  16  VAL   A CB   1 
ATOM   347  C CG1  . VAL   A 1 16  ? 15.201 -13.937 6.194   1.00 15.13 ?  16  VAL   A CG1  1 
ATOM   348  C CG2  . VAL   A 1 16  ? 16.925 -15.764 6.078   1.00 15.30 ?  16  VAL   A CG2  1 
ATOM   349  H H    . VAL   A 1 16  ? 15.629 -17.134 8.718   1.00 17.12 ?  16  VAL   A H    1 
ATOM   350  H HA   . VAL   A 1 16  ? 16.522 -14.582 8.459   1.00 16.41 ?  16  VAL   A HA   1 
ATOM   351  H HB   . VAL   A 1 16  ? 14.949 -15.944 6.548   1.00 17.31 ?  16  VAL   A HB   1 
ATOM   352  H HG11 . VAL   A 1 16  ? 15.295 -13.953 5.229   1.00 18.16 ?  16  VAL   A HG11 1 
ATOM   353  H HG12 . VAL   A 1 16  ? 14.273 -13.786 6.432   1.00 18.16 ?  16  VAL   A HG12 1 
ATOM   354  H HG13 . VAL   A 1 16  ? 15.761 -13.246 6.572   1.00 18.16 ?  16  VAL   A HG13 1 
ATOM   355  H HG21 . VAL   A 1 16  ? 16.803 -15.745 5.116   1.00 18.36 ?  16  VAL   A HG21 1 
ATOM   356  H HG22 . VAL   A 1 16  ? 17.650 -15.168 6.329   1.00 18.36 ?  16  VAL   A HG22 1 
ATOM   357  H HG23 . VAL   A 1 16  ? 17.128 -16.666 6.369   1.00 18.36 ?  16  VAL   A HG23 1 
ATOM   358  N N    A TYR   A 1 17  ? 14.586 -13.464 9.376   0.76 13.50 ?  17  TYR   A N    1 
ATOM   359  N N    B TYR   A 1 17  ? 14.598 -13.470 9.409   0.24 13.23 ?  17  TYR   A N    1 
ATOM   360  C CA   A TYR   A 1 17  ? 13.510 -12.787 10.078  0.76 13.31 ?  17  TYR   A CA   1 
ATOM   361  C CA   B TYR   A 1 17  ? 13.502 -12.781 10.075  0.24 13.06 ?  17  TYR   A CA   1 
ATOM   362  C C    A TYR   A 1 17  ? 13.243 -11.458 9.386   0.76 13.69 ?  17  TYR   A C    1 
ATOM   363  C C    B TYR   A 1 17  ? 13.228 -11.472 9.338   0.24 12.49 ?  17  TYR   A C    1 
ATOM   364  O O    A TYR   A 1 17  ? 14.160 -10.850 8.830   0.76 13.20 ?  17  TYR   A O    1 
ATOM   365  O O    B TYR   A 1 17  ? 14.024 -11.031 8.504   0.24 12.15 ?  17  TYR   A O    1 
ATOM   366  C CB   A TYR   A 1 17  ? 13.933 -12.536 11.528  0.76 13.60 ?  17  TYR   A CB   1 
ATOM   367  C CB   B TYR   A 1 17  ? 13.849 -12.499 11.546  0.24 13.70 ?  17  TYR   A CB   1 
ATOM   368  C CG   A TYR   A 1 17  ? 14.105 -13.804 12.330  0.76 15.24 ?  17  TYR   A CG   1 
ATOM   369  C CG   B TYR   A 1 17  ? 14.112 -13.743 12.378  0.24 14.72 ?  17  TYR   A CG   1 
ATOM   370  C CD1  A TYR   A 1 17  ? 15.264 -14.565 12.240  0.76 16.09 ?  17  TYR   A CD1  1 
ATOM   371  C CD1  B TYR   A 1 17  ? 15.319 -14.428 12.288  0.24 15.26 ?  17  TYR   A CD1  1 
ATOM   372  C CD2  A TYR   A 1 17  ? 13.098 -14.253 13.167  0.76 15.46 ?  17  TYR   A CD2  1 
ATOM   373  C CD2  B TYR   A 1 17  ? 13.154 -14.228 13.260  0.24 15.22 ?  17  TYR   A CD2  1 
ATOM   374  C CE1  A TYR   A 1 17  ? 15.416 -15.739 12.967  0.76 16.66 ?  17  TYR   A CE1  1 
ATOM   375  C CE1  B TYR   A 1 17  ? 15.561 -15.565 13.047  0.24 15.73 ?  17  TYR   A CE1  1 
ATOM   376  C CE2  A TYR   A 1 17  ? 13.237 -15.431 13.900  0.76 16.34 ?  17  TYR   A CE2  1 
ATOM   377  C CE2  B TYR   A 1 17  ? 13.387 -15.367 14.024  0.24 15.62 ?  17  TYR   A CE2  1 
ATOM   378  C CZ   A TYR   A 1 17  ? 14.399 -16.166 13.798  0.76 16.49 ?  17  TYR   A CZ   1 
ATOM   379  C CZ   B TYR   A 1 17  ? 14.593 -16.028 13.912  0.24 15.72 ?  17  TYR   A CZ   1 
ATOM   380  O OH   A TYR   A 1 17  ? 14.541 -17.326 14.528  0.76 16.90 ?  17  TYR   A OH   1 
ATOM   381  O OH   B TYR   A 1 17  ? 14.828 -17.155 14.669  0.24 15.75 ?  17  TYR   A OH   1 
ATOM   382  H H    A TYR   A 1 17  ? 15.272 -12.948 9.254   0.76 16.19 ?  17  TYR   A H    1 
ATOM   383  H H    B TYR   A 1 17  ? 15.302 -12.973 9.334   0.24 15.88 ?  17  TYR   A H    1 
ATOM   384  H HA   A TYR   A 1 17  ? 12.706 -13.330 10.064  0.76 15.97 ?  17  TYR   A HA   1 
ATOM   385  H HA   B TYR   A 1 17  ? 12.707 -13.332 10.040  0.24 15.67 ?  17  TYR   A HA   1 
ATOM   386  H HB2  A TYR   A 1 17  ? 14.781 -12.069 11.531  0.76 16.32 ?  17  TYR   A HB2  1 
ATOM   387  H HB2  B TYR   A 1 17  ? 14.647 -11.949 11.576  0.24 16.43 ?  17  TYR   A HB2  1 
ATOM   388  H HB3  A TYR   A 1 17  ? 13.258 -12.002 11.964  0.76 16.32 ?  17  TYR   A HB3  1 
ATOM   389  H HB3  B TYR   A 1 17  ? 13.108 -12.023 11.951  0.24 16.43 ?  17  TYR   A HB3  1 
ATOM   390  H HD1  A TYR   A 1 17  ? 15.953 -14.283 11.679  0.76 19.31 ?  17  TYR   A HD1  1 
ATOM   391  H HD1  B TYR   A 1 17  ? 15.976 -14.122 11.706  0.24 18.32 ?  17  TYR   A HD1  1 
ATOM   392  H HD2  A TYR   A 1 17  ? 12.309 -13.768 13.240  0.76 18.55 ?  17  TYR   A HD2  1 
ATOM   393  H HD2  B TYR   A 1 17  ? 12.340 -13.786 13.340  0.24 18.26 ?  17  TYR   A HD2  1 
ATOM   394  H HE1  A TYR   A 1 17  ? 16.205 -16.235 12.896  0.76 19.99 ?  17  TYR   A HE1  1 
ATOM   395  H HE1  B TYR   A 1 17  ? 16.375 -16.016 12.977  0.24 18.88 ?  17  TYR   A HE1  1 
ATOM   396  H HE2  A TYR   A 1 17  ? 12.552 -15.718 14.461  0.76 19.60 ?  17  TYR   A HE2  1 
ATOM   397  H HE2  B TYR   A 1 17  ? 12.735 -15.679 14.612  0.24 18.75 ?  17  TYR   A HE2  1 
ATOM   398  H HH   A TYR   A 1 17  ? 13.812 -17.521 14.898  0.76 20.28 ?  17  TYR   A HH   1 
ATOM   399  H HH   B TYR   A 1 17  ? 15.589 -17.467 14.500  0.24 18.90 ?  17  TYR   A HH   1 
ATOM   400  N N    A ILE   A 1 18  ? 11.987 -10.990 9.417   0.76 13.59 ?  18  ILE   A N    1 
ATOM   401  N N    B ILE   A 1 18  ? 12.100 -10.829 9.654   0.24 12.14 ?  18  ILE   A N    1 
ATOM   402  C CA   A ILE   A 1 18  ? 11.598 -9.801  8.658   0.76 13.36 ?  18  ILE   A CA   1 
ATOM   403  C CA   B ILE   A 1 18  ? 11.693 -9.606  8.961   0.24 12.24 ?  18  ILE   A CA   1 
ATOM   404  C C    A ILE   A 1 18  ? 10.621 -8.933  9.449   0.76 13.40 ?  18  ILE   A C    1 
ATOM   405  C C    B ILE   A 1 18  ? 10.792 -8.772  9.863   0.24 12.37 ?  18  ILE   A C    1 
ATOM   406  O O    A ILE   A 1 18  ? 9.794  -9.436  10.216  0.76 13.74 ?  18  ILE   A O    1 
ATOM   407  O O    B ILE   A 1 18  ? 10.003 -9.302  10.651  0.24 12.88 ?  18  ILE   A O    1 
ATOM   408  C CB   A ILE   A 1 18  ? 11.056 -10.202 7.265   0.76 13.15 ?  18  ILE   A CB   1 
ATOM   409  C CB   B ILE   A 1 18  ? 11.007 -9.909  7.608   0.24 11.88 ?  18  ILE   A CB   1 
ATOM   410  C CG1  A ILE   A 1 18  ? 11.027 -9.002  6.320   0.76 13.04 ?  18  ILE   A CG1  1 
ATOM   411  C CG1  B ILE   A 1 18  ? 10.856 -8.630  6.777   0.24 12.41 ?  18  ILE   A CG1  1 
ATOM   412  C CG2  A ILE   A 1 18  ? 9.699  -10.907 7.378   0.76 13.78 ?  18  ILE   A CG2  1 
ATOM   413  C CG2  B ILE   A 1 18  ? 9.650  -10.572 7.828   0.24 11.90 ?  18  ILE   A CG2  1 
ATOM   414  C CD1  A ILE   A 1 18  ? 10.791 -9.387  4.893   0.76 14.57 ?  18  ILE   A CD1  1 
ATOM   415  C CD1  B ILE   A 1 18  ? 10.454 -8.887  5.343   0.24 13.04 ?  18  ILE   A CD1  1 
ATOM   416  H H    A ILE   A 1 18  ? 11.344 -11.354 9.865   0.76 16.30 ?  18  ILE   A H    1 
ATOM   417  H H    B ILE   A 1 18  ? 11.564 -11.080 10.274  0.24 14.57 ?  18  ILE   A H    1 
ATOM   418  H HA   A ILE   A 1 18  ? 12.397 -9.273  8.507   0.76 16.04 ?  18  ILE   A HA   1 
ATOM   419  H HA   B ILE   A 1 18  ? 12.489 -9.082  8.777   0.24 14.69 ?  18  ILE   A HA   1 
ATOM   420  H HB   A ILE   A 1 18  ? 11.681 -10.846 6.888   0.76 15.78 ?  18  ILE   A HB   1 
ATOM   421  H HB   B ILE   A 1 18  ? 11.571 -10.520 7.119   0.24 14.26 ?  18  ILE   A HB   1 
ATOM   422  H HG12 A ILE   A 1 18  ? 10.321 -8.403  6.590   0.76 15.64 ?  18  ILE   A HG12 1 
ATOM   423  H HG12 B ILE   A 1 18  ? 10.176 -8.067  7.178   0.24 14.90 ?  18  ILE   A HG12 1 
ATOM   424  H HG13 A ILE   A 1 18  ? 11.886 -8.546  6.362   0.76 15.64 ?  18  ILE   A HG13 1 
ATOM   425  H HG13 B ILE   A 1 18  ? 11.706 -8.158  6.764   0.24 14.90 ?  18  ILE   A HG13 1 
ATOM   426  H HG21 A ILE   A 1 18  ? 9.464  -11.283 6.512   0.76 16.54 ?  18  ILE   A HG21 1 
ATOM   427  H HG21 B ILE   A 1 18  ? 9.331  -10.919 6.979   0.24 14.28 ?  18  ILE   A HG21 1 
ATOM   428  H HG22 A ILE   A 1 18  ? 9.765  -11.617 8.036   0.76 16.54 ?  18  ILE   A HG22 1 
ATOM   429  H HG22 B ILE   A 1 18  ? 9.754  -11.297 8.463   0.24 14.28 ?  18  ILE   A HG22 1 
ATOM   430  H HG23 A ILE   A 1 18  ? 9.028  -10.264 7.650   0.76 16.54 ?  18  ILE   A HG23 1 
ATOM   431  H HG23 B ILE   A 1 18  ? 9.024  -9.917  8.173   0.24 14.28 ?  18  ILE   A HG23 1 
ATOM   432  H HD11 A ILE   A 1 18  ? 10.854 -8.593  4.337   0.76 17.49 ?  18  ILE   A HD11 1 
ATOM   433  H HD11 B ILE   A 1 18  ? 10.430 -8.044  4.863   0.24 15.65 ?  18  ILE   A HD11 1 
ATOM   434  H HD12 A ILE   A 1 18  ? 11.459 -10.034 4.622   0.76 17.49 ?  18  ILE   A HD12 1 
ATOM   435  H HD12 B ILE   A 1 18  ? 11.104 -9.481  4.935   0.24 15.65 ?  18  ILE   A HD12 1 
ATOM   436  H HD13 A ILE   A 1 18  ? 9.904  -9.773  4.815   0.76 17.49 ?  18  ILE   A HD13 1 
ATOM   437  H HD13 B ILE   A 1 18  ? 9.576  -9.299  5.330   0.24 15.65 ?  18  ILE   A HD13 1 
ATOM   438  N N    A LYS   A 1 19  ? 10.718 -7.613  9.247   0.76 13.39 ?  19  LYS   A N    1 
ATOM   439  N N    B LYS   A 1 19  ? 10.907 -7.449  9.724   0.24 12.50 ?  19  LYS   A N    1 
ATOM   440  C CA   A LYS   A 1 19  ? 9.900  -6.647  9.975   0.76 14.18 ?  19  LYS   A CA   1 
ATOM   441  C CA   B LYS   A 1 19  ? 10.135 -6.502  10.516  0.24 13.56 ?  19  LYS   A CA   1 
ATOM   442  C C    A LYS   A 1 19  ? 9.716  -5.392  9.131   0.76 14.21 ?  19  LYS   A C    1 
ATOM   443  C C    B LYS   A 1 19  ? 9.919  -5.241  9.693   0.24 14.07 ?  19  LYS   A C    1 
ATOM   444  O O    A LYS   A 1 19  ? 10.615 -4.998  8.385   0.76 14.14 ?  19  LYS   A O    1 
ATOM   445  O O    B LYS   A 1 19  ? 10.805 -4.823  8.945   0.24 14.39 ?  19  LYS   A O    1 
ATOM   446  C CB   A LYS   A 1 19  ? 10.595 -6.272  11.292  0.76 15.38 ?  19  LYS   A CB   1 
ATOM   447  C CB   B LYS   A 1 19  ? 10.875 -6.142  11.812  0.24 14.01 ?  19  LYS   A CB   1 
ATOM   448  C CG   A LYS   A 1 19  ? 9.838  -5.336  12.222  0.76 17.31 ?  19  LYS   A CG   1 
ATOM   449  C CG   B LYS   A 1 19  ? 10.136 -5.205  12.751  0.24 14.73 ?  19  LYS   A CG   1 
ATOM   450  C CD   A LYS   A 1 19  ? 10.696 -5.056  13.451  0.76 19.31 ?  19  LYS   A CD   1 
ATOM   451  C CD   B LYS   A 1 19  ? 11.027 -4.829  13.928  0.24 15.56 ?  19  LYS   A CD   1 
ATOM   452  C CE   A LYS   A 1 19  ? 10.036 -4.106  14.432  0.76 20.48 ?  19  LYS   A CE   1 
ATOM   453  C CE   B LYS   A 1 19  ? 10.295 -3.980  14.947  0.24 16.42 ?  19  LYS   A CE   1 
ATOM   454  N NZ   A LYS   A 1 19  ? 10.921 -3.848  15.606  0.76 20.74 ?  19  LYS   A NZ   1 
ATOM   455  N NZ   B LYS   A 1 19  ? 11.135 -3.750  16.154  0.24 16.85 ?  19  LYS   A NZ   1 
ATOM   456  H H    A LYS   A 1 19  ? 11.270 -7.251  8.687   0.76 16.06 ?  19  LYS   A H    1 
ATOM   457  H H    B LYS   A 1 19  ? 11.444 -7.064  9.167   0.24 15.00 ?  19  LYS   A H    1 
ATOM   458  H HA   A LYS   A 1 19  ? 9.032  -7.040  10.169  0.76 17.02 ?  19  LYS   A HA   1 
ATOM   459  H HA   B LYS   A 1 19  ? 9.275  -6.878  10.744  0.24 16.27 ?  19  LYS   A HA   1 
ATOM   460  H HB2  A LYS   A 1 19  ? 10.766 -7.088  11.784  0.76 18.46 ?  19  LYS   A HB2  1 
ATOM   461  H HB2  B LYS   A 1 19  ? 11.042 -6.957  12.306  0.24 16.81 ?  19  LYS   A HB2  1 
ATOM   462  H HB3  A LYS   A 1 19  ? 11.435 -5.844  11.073  0.76 18.46 ?  19  LYS   A HB3  1 
ATOM   463  H HB3  B LYS   A 1 19  ? 11.720 -5.718  11.588  0.24 16.81 ?  19  LYS   A HB3  1 
ATOM   464  H HG2  A LYS   A 1 19  ? 9.657  -4.497  11.769  0.76 20.77 ?  19  LYS   A HG2  1 
ATOM   465  H HG2  B LYS   A 1 19  ? 9.894  -4.392  12.283  0.24 17.68 ?  19  LYS   A HG2  1 
ATOM   466  H HG3  A LYS   A 1 19  ? 9.010  -5.755  12.508  0.76 20.77 ?  19  LYS   A HG3  1 
ATOM   467  H HG3  B LYS   A 1 19  ? 9.345  -5.648  13.097  0.24 17.68 ?  19  LYS   A HG3  1 
ATOM   468  H HD2  A LYS   A 1 19  ? 10.867 -5.892  13.914  0.76 23.18 ?  19  LYS   A HD2  1 
ATOM   469  H HD2  B LYS   A 1 19  ? 11.322 -5.639  14.372  0.24 18.68 ?  19  LYS   A HD2  1 
ATOM   470  H HD3  A LYS   A 1 19  ? 11.535 -4.658  13.167  0.76 23.18 ?  19  LYS   A HD3  1 
ATOM   471  H HD3  B LYS   A 1 19  ? 11.791 -4.327  13.604  0.24 18.68 ?  19  LYS   A HD3  1 
ATOM   472  H HE2  A LYS   A 1 19  ? 9.862  -3.258  13.993  0.76 24.57 ?  19  LYS   A HE2  1 
ATOM   473  H HE2  B LYS   A 1 19  ? 10.081 -3.119  14.553  0.24 19.71 ?  19  LYS   A HE2  1 
ATOM   474  H HE3  A LYS   A 1 19  ? 9.210  -4.495  14.755  0.76 24.57 ?  19  LYS   A HE3  1 
ATOM   475  H HE3  B LYS   A 1 19  ? 9.483  -4.435  15.220  0.24 19.71 ?  19  LYS   A HE3  1 
ATOM   476  H HZ1  A LYS   A 1 19  ? 10.520 -3.296  16.176  0.76 24.89 ?  19  LYS   A HZ1  1 
ATOM   477  H HZ1  B LYS   A 1 19  ? 10.692 -3.251  16.743  0.24 20.22 ?  19  LYS   A HZ1  1 
ATOM   478  H HZ2  A LYS   A 1 19  ? 11.101 -4.614  16.024  0.76 24.89 ?  19  LYS   A HZ2  1 
ATOM   479  H HZ2  B LYS   A 1 19  ? 11.342 -4.528  16.533  0.24 20.22 ?  19  LYS   A HZ2  1 
ATOM   480  H HZ3  A LYS   A 1 19  ? 11.685 -3.481  15.336  0.76 24.89 ?  19  LYS   A HZ3  1 
ATOM   481  H HZ3  B LYS   A 1 19  ? 11.886 -3.330  15.926  0.24 20.22 ?  19  LYS   A HZ3  1 
ATOM   482  N N    A ASN   A 1 20  ? 8.542  -4.761  9.249   0.76 15.04 ?  20  ASN   A N    1 
ATOM   483  N N    B ASN   A 1 20  ? 8.739  -4.641  9.832   0.24 15.02 ?  20  ASN   A N    1 
ATOM   484  C CA   A ASN   A 1 20  ? 8.320  -3.434  8.671   0.76 16.52 ?  20  ASN   A CA   1 
ATOM   485  C CA   B ASN   A 1 20  ? 8.459  -3.339  9.233   0.24 16.08 ?  20  ASN   A CA   1 
ATOM   486  C C    A ASN   A 1 20  ? 8.940  -2.420  9.624   0.76 17.11 ?  20  ASN   A C    1 
ATOM   487  C C    B ASN   A 1 20  ? 9.074  -2.283  10.140  0.24 16.22 ?  20  ASN   A C    1 
ATOM   488  O O    A ASN   A 1 20  ? 8.420  -2.189  10.720  0.76 18.50 ?  20  ASN   A O    1 
ATOM   489  O O    B ASN   A 1 20  ? 8.504  -1.922  11.172  0.24 16.49 ?  20  ASN   A O    1 
ATOM   490  C CB   A ASN   A 1 20  ? 6.822  -3.193  8.468   0.76 17.59 ?  20  ASN   A CB   1 
ATOM   491  C CB   B ASN   A 1 20  ? 6.956  -3.137  9.073   0.24 16.73 ?  20  ASN   A CB   1 
ATOM   492  C CG   A ASN   A 1 20  ? 6.489  -1.765  8.038   0.76 19.32 ?  20  ASN   A CG   1 
ATOM   493  C CG   B ASN   A 1 20  ? 6.582  -1.689  8.813   0.24 17.58 ?  20  ASN   A CG   1 
ATOM   494  O OD1  A ASN   A 1 20  ? 5.466  -1.215  8.449   0.76 21.68 ?  20  ASN   A OD1  1 
ATOM   495  O OD1  B ASN   A 1 20  ? 5.827  -1.088  9.576   0.24 17.84 ?  20  ASN   A OD1  1 
ATOM   496  N ND2  A ASN   A 1 20  ? 7.335  -1.169  7.204   0.76 19.70 ?  20  ASN   A ND2  1 
ATOM   497  N ND2  B ASN   A 1 20  ? 7.113  -1.120  7.738   0.24 17.87 ?  20  ASN   A ND2  1 
ATOM   498  H H    A ASN   A 1 20  ? 7.860  -5.086  9.660   0.76 18.04 ?  20  ASN   A H    1 
ATOM   499  H H    B ASN   A 1 20  ? 8.082  -4.971  10.272  0.24 18.03 ?  20  ASN   A H    1 
ATOM   500  H HA   A ASN   A 1 20  ? 8.766  -3.379  7.813   0.76 19.82 ?  20  ASN   A HA   1 
ATOM   501  H HA   B ASN   A 1 20  ? 8.876  -3.280  8.359   0.24 19.29 ?  20  ASN   A HA   1 
ATOM   502  H HB2  A ASN   A 1 20  ? 6.498  -3.787  7.776   0.76 21.10 ?  20  ASN   A HB2  1 
ATOM   503  H HB2  B ASN   A 1 20  ? 6.643  -3.665  8.321   0.24 20.07 ?  20  ASN   A HB2  1 
ATOM   504  H HB3  A ASN   A 1 20  ? 6.361  -3.372  9.301   0.76 21.10 ?  20  ASN   A HB3  1 
ATOM   505  H HB3  B ASN   A 1 20  ? 6.508  -3.423  9.884   0.24 20.07 ?  20  ASN   A HB3  1 
ATOM   506  H HD21 A ASN   A 1 20  ? 7.184  -0.364  6.947   0.76 23.64 ?  20  ASN   A HD21 1 
ATOM   507  H HD21 B ASN   A 1 20  ? 6.927  -0.302  7.549   0.24 21.45 ?  20  ASN   A HD21 1 
ATOM   508  H HD22 A ASN   A 1 20  ? 8.034  -1.586  6.929   0.76 23.64 ?  20  ASN   A HD22 1 
ATOM   509  H HD22 B ASN   A 1 20  ? 7.643  -1.569  7.232   0.24 21.45 ?  20  ASN   A HD22 1 
ATOM   510  N N    A ALA   A 1 21  ? 10.076 -1.842  9.236   0.76 17.02 ?  21  ALA   A N    1 
ATOM   511  N N    B ALA   A 1 21  ? 10.256 -1.800  9.772   0.24 16.43 ?  21  ALA   A N    1 
ATOM   512  C CA   A ALA   A 1 21  ? 10.772 -0.944  10.146  0.76 17.28 ?  21  ALA   A CA   1 
ATOM   513  C CA   B ALA   A 1 21  ? 10.932 -0.791  10.573  0.24 16.54 ?  21  ALA   A CA   1 
ATOM   514  C C    A ALA   A 1 21  ? 11.745 -0.066  9.379   0.76 16.75 ?  21  ALA   A C    1 
ATOM   515  C C    B ALA   A 1 21  ? 12.051 -0.172  9.754   0.24 16.35 ?  21  ALA   A C    1 
ATOM   516  O O    A ALA   A 1 21  ? 12.228 -0.437  8.306   0.76 16.44 ?  21  ALA   A O    1 
ATOM   517  O O    B ALA   A 1 21  ? 12.623 -0.820  8.873   0.24 16.45 ?  21  ALA   A O    1 
ATOM   518  C CB   A ALA   A 1 21  ? 11.525 -1.722  11.228  0.76 18.42 ?  21  ALA   A CB   1 
ATOM   519  C CB   B ALA   A 1 21  ? 11.496 -1.392  11.866  0.24 17.13 ?  21  ALA   A CB   1 
ATOM   520  H H    A ALA   A 1 21  ? 10.451 -1.949  8.471   0.76 20.42 ?  21  ALA   A H    1 
ATOM   521  H H    B ALA   A 1 21  ? 10.687 -2.042  9.069   0.24 19.72 ?  21  ALA   A H    1 
ATOM   522  H HA   A ALA   A 1 21  ? 10.118 -0.371  10.583  0.76 20.74 ?  21  ALA   A HA   1 
ATOM   523  H HA   B ALA   A 1 21  ? 10.305 -0.092  10.810  0.24 19.84 ?  21  ALA   A HA   1 
ATOM   524  H HB1  A ALA   A 1 21  ? 11.960 -1.091  11.820  0.76 22.10 ?  21  ALA   A HB1  1 
ATOM   525  H HB1  B ALA   A 1 21  ? 11.950 -0.695  12.366  0.24 20.56 ?  21  ALA   A HB1  1 
ATOM   526  H HB2  A ALA   A 1 21  ? 10.888 -2.260  11.730  0.76 22.10 ?  21  ALA   A HB2  1 
ATOM   527  H HB2  B ALA   A 1 21  ? 10.765 -1.752  12.392  0.24 20.56 ?  21  ALA   A HB2  1 
ATOM   528  H HB3  A ALA   A 1 21  ? 12.180 -2.295  10.806  0.76 22.10 ?  21  ALA   A HB3  1 
ATOM   529  H HB3  B ALA   A 1 21  ? 12.121 -2.099  11.641  0.24 20.56 ?  21  ALA   A HB3  1 
ATOM   530  N N    A ASP   A 1 22  ? 12.007 1.106   9.956   0.76 17.06 ?  22  ASP   A N    1 
ATOM   531  N N    B ASP   A 1 22  ? 12.333 1.096   10.041  0.24 16.03 ?  22  ASP   A N    1 
ATOM   532  C CA   A ASP   A 1 22  ? 13.066 2.002   9.509   0.76 17.57 ?  22  ASP   A CA   1 
ATOM   533  C CA   B ASP   A 1 22  ? 13.520 1.748   9.509   0.24 16.36 ?  22  ASP   A CA   1 
ATOM   534  C C    A ASP   A 1 22  ? 14.389 1.511   10.091  0.76 16.18 ?  22  ASP   A C    1 
ATOM   535  C C    B ASP   A 1 22  ? 14.754 1.067   10.087  0.24 15.10 ?  22  ASP   A C    1 
ATOM   536  O O    A ASP   A 1 22  ? 14.568 1.504   11.313  0.76 16.70 ?  22  ASP   A O    1 
ATOM   537  O O    B ASP   A 1 22  ? 14.880 0.920   11.307  0.24 14.75 ?  22  ASP   A O    1 
ATOM   538  C CB   A ASP   A 1 22  ? 12.746 3.412   10.003  0.76 19.70 ?  22  ASP   A CB   1 
ATOM   539  C CB   B ASP   A 1 22  ? 13.505 3.221   9.922   0.24 17.88 ?  22  ASP   A CB   1 
ATOM   540  C CG   A ASP   A 1 22  ? 13.779 4.443   9.579   0.76 22.27 ?  22  ASP   A CG   1 
ATOM   541  C CG   B ASP   A 1 22  ? 14.523 4.060   9.175   0.24 18.93 ?  22  ASP   A CG   1 
ATOM   542  O OD1  A ASP   A 1 22  ? 14.911 4.076   9.214   0.76 23.03 ?  22  ASP   A OD1  1 
ATOM   543  O OD1  B ASP   A 1 22  ? 15.521 3.496   8.684   0.24 18.81 ?  22  ASP   A OD1  1 
ATOM   544  O OD2  A ASP   A 1 22  ? 13.454 5.648   9.624   0.76 24.44 -1 22  ASP   A OD2  1 
ATOM   545  O OD2  B ASP   A 1 22  ? 14.326 5.292   9.090   0.24 19.76 -1 22  ASP   A OD2  1 
ATOM   546  H H    A ASP   A 1 22  ? 11.554 1.413   10.625  0.76 20.48 ?  22  ASP   A H    1 
ATOM   547  H H    B ASP   A 1 22  ? 11.842 1.602   10.536  0.24 19.23 ?  22  ASP   A H    1 
ATOM   548  H HA   A ASP   A 1 22  ? 13.116 2.002   8.541   0.76 21.09 ?  22  ASP   A HA   1 
ATOM   549  H HA   B ASP   A 1 22  ? 13.533 1.677   8.538   0.24 19.64 ?  22  ASP   A HA   1 
ATOM   550  H HB2  A ASP   A 1 22  ? 11.885 3.688   9.640   0.76 23.64 ?  22  ASP   A HB2  1 
ATOM   551  H HB2  B ASP   A 1 22  ? 12.632 3.590   9.744   0.24 21.46 ?  22  ASP   A HB2  1 
ATOM   552  H HB3  A ASP   A 1 22  ? 12.697 3.402   10.974  0.76 23.64 ?  22  ASP   A HB3  1 
ATOM   553  H HB3  B ASP   A 1 22  ? 13.712 3.280   10.865  0.24 21.46 ?  22  ASP   A HB3  1 
ATOM   554  N N    A ILE   A 1 23  ? 15.312 1.099   9.217   0.76 15.55 ?  23  ILE   A N    1 
ATOM   555  N N    B ILE   A 1 23  ? 15.664 0.640   9.210   0.24 14.87 ?  23  ILE   A N    1 
ATOM   556  C CA   A ILE   A 1 23  ? 16.559 0.484   9.672   0.76 14.60 ?  23  ILE   A CA   1 
ATOM   557  C CA   B ILE   A 1 23  ? 16.881 -0.017  9.675   0.24 14.43 ?  23  ILE   A CA   1 
ATOM   558  C C    A ILE   A 1 23  ? 17.356 1.428   10.563  0.76 15.06 ?  23  ILE   A C    1 
ATOM   559  C C    B ILE   A 1 23  ? 17.667 0.912   10.588  0.24 14.88 ?  23  ILE   A C    1 
ATOM   560  O O    A ILE   A 1 23  ? 18.067 0.980   11.470  0.76 15.73 ?  23  ILE   A O    1 
ATOM   561  O O    B ILE   A 1 23  ? 18.338 0.461   11.524  0.24 14.69 ?  23  ILE   A O    1 
ATOM   562  C CB   A ILE   A 1 23  ? 17.376 -0.030  8.467   0.76 14.24 ?  23  ILE   A CB   1 
ATOM   563  C CB   B ILE   A 1 23  ? 17.721 -0.530  8.485   0.24 13.58 ?  23  ILE   A CB   1 
ATOM   564  C CG1  A ILE   A 1 23  ? 18.502 -0.955  8.929   0.76 14.35 ?  23  ILE   A CG1  1 
ATOM   565  C CG1  B ILE   A 1 23  ? 18.821 -1.471  8.984   0.24 13.34 ?  23  ILE   A CG1  1 
ATOM   566  C CG2  A ILE   A 1 23  ? 17.898 1.140   7.627   0.76 14.76 ?  23  ILE   A CG2  1 
ATOM   567  C CG2  B ILE   A 1 23  ? 18.321 0.627   7.688   0.24 13.59 ?  23  ILE   A CG2  1 
ATOM   568  C CD1  A ILE   A 1 23  ? 19.207 -1.657  7.785   0.76 14.65 ?  23  ILE   A CD1  1 
ATOM   569  C CD1  B ILE   A 1 23  ? 19.697 -2.034  7.886   0.24 13.29 ?  23  ILE   A CD1  1 
ATOM   570  H H    A ILE   A 1 23  ? 15.226 1.155   8.371   0.76 18.66 ?  23  ILE   A H    1 
ATOM   571  H H    B ILE   A 1 23  ? 15.603 0.717   8.365   0.24 17.84 ?  23  ILE   A H    1 
ATOM   572  H HA   A ILE   A 1 23  ? 16.334 -0.287  10.214  0.76 17.52 ?  23  ILE   A HA   1 
ATOM   573  H HA   B ILE   A 1 23  ? 16.622 -0.791  10.195  0.24 17.31 ?  23  ILE   A HA   1 
ATOM   574  H HB   A ILE   A 1 23  ? 16.777 -0.547  7.909   0.76 17.09 ?  23  ILE   A HB   1 
ATOM   575  H HB   B ILE   A 1 23  ? 17.140 -1.035  7.895   0.24 16.29 ?  23  ILE   A HB   1 
ATOM   576  H HG12 A ILE   A 1 23  ? 19.162 -0.430  9.408   0.76 17.22 ?  23  ILE   A HG12 1 
ATOM   577  H HG12 B ILE   A 1 23  ? 19.393 -0.987  9.599   0.24 16.01 ?  23  ILE   A HG12 1 
ATOM   578  H HG13 A ILE   A 1 23  ? 18.130 -1.633  9.512   0.76 17.22 ?  23  ILE   A HG13 1 
ATOM   579  H HG13 B ILE   A 1 23  ? 18.404 -2.218  9.442   0.24 16.01 ?  23  ILE   A HG13 1 
ATOM   580  H HG21 A ILE   A 1 23  ? 18.255 0.795   6.795   0.76 17.71 ?  23  ILE   A HG21 1 
ATOM   581  H HG21 B ILE   A 1 23  ? 18.649 0.289   6.837   0.24 16.31 ?  23  ILE   A HG21 1 
ATOM   582  H HG22 A ILE   A 1 23  ? 17.160 1.747   7.440   0.76 17.71 ?  23  ILE   A HG22 1 
ATOM   583  H HG22 B ILE   A 1 23  ? 17.633 1.291   7.534   0.24 16.31 ?  23  ILE   A HG22 1 
ATOM   584  H HG23 A ILE   A 1 23  ? 18.588 1.604   8.121   0.76 17.71 ?  23  ILE   A HG23 1 
ATOM   585  H HG23 B ILE   A 1 23  ? 19.051 1.015   8.193   0.24 16.31 ?  23  ILE   A HG23 1 
ATOM   586  H HD11 A ILE   A 1 23  ? 19.853 -2.279  8.150   0.76 17.58 ?  23  ILE   A HD11 1 
ATOM   587  H HD11 B ILE   A 1 23  ? 20.272 -2.719  8.263   0.24 15.95 ?  23  ILE   A HD11 1 
ATOM   588  H HD12 A ILE   A 1 23  ? 18.547 -2.134  7.256   0.76 17.58 ?  23  ILE   A HD12 1 
ATOM   589  H HD12 B ILE   A 1 23  ? 19.132 -2.420  7.199   0.24 15.95 ?  23  ILE   A HD12 1 
ATOM   590  H HD13 A ILE   A 1 23  ? 19.654 -0.995  7.235   0.76 17.58 ?  23  ILE   A HD13 1 
ATOM   591  H HD13 B ILE   A 1 23  ? 20.235 -1.320  7.512   0.24 15.95 ?  23  ILE   A HD13 1 
ATOM   592  N N    A VAL   A 1 24  ? 17.238 2.740   10.340  0.76 15.75 ?  24  VAL   A N    1 
ATOM   593  N N    B VAL   A 1 24  ? 17.584 2.220   10.342  0.24 15.58 ?  24  VAL   A N    1 
ATOM   594  C CA   A VAL   A 1 24  ? 17.923 3.706   11.198  0.76 17.31 ?  24  VAL   A CA   1 
ATOM   595  C CA   B VAL   A 1 24  ? 18.217 3.196   11.224  0.24 16.69 ?  24  VAL   A CA   1 
ATOM   596  C C    A VAL   A 1 24  ? 17.399 3.616   12.626  0.76 18.40 ?  24  VAL   A C    1 
ATOM   597  C C    B VAL   A 1 24  ? 17.567 3.160   12.602  0.24 17.36 ?  24  VAL   A C    1 
ATOM   598  O O    A VAL   A 1 24  ? 18.172 3.547   13.590  0.76 18.85 ?  24  VAL   A O    1 
ATOM   599  O O    B VAL   A 1 24  ? 18.251 3.161   13.634  0.24 17.60 ?  24  VAL   A O    1 
ATOM   600  C CB   A VAL   A 1 24  ? 17.775 5.130   10.632  0.76 18.71 ?  24  VAL   A CB   1 
ATOM   601  C CB   B VAL   A 1 24  ? 18.144 4.597   10.591  0.24 17.35 ?  24  VAL   A CB   1 
ATOM   602  C CG1  A VAL   A 1 24  ? 18.296 6.159   11.631  0.76 19.56 ?  24  VAL   A CG1  1 
ATOM   603  C CG1  B VAL   A 1 24  ? 18.775 5.629   11.502  0.24 17.88 ?  24  VAL   A CG1  1 
ATOM   604  C CG2  A VAL   A 1 24  ? 18.496 5.249   9.299   0.76 19.42 ?  24  VAL   A CG2  1 
ATOM   605  C CG2  B VAL   A 1 24  ? 18.816 4.590   9.222   0.24 17.30 ?  24  VAL   A CG2  1 
ATOM   606  H H    A VAL   A 1 24  ? 16.773 3.093   9.705   0.76 18.90 ?  24  VAL   A H    1 
ATOM   607  H H    B VAL   A 1 24  ? 17.173 2.565   9.673   0.24 18.70 ?  24  VAL   A H    1 
ATOM   608  H HA   A VAL   A 1 24  ? 18.866 3.496   11.214  0.76 20.77 ?  24  VAL   A HA   1 
ATOM   609  H HA   B VAL   A 1 24  ? 19.154 2.964   11.329  0.24 20.03 ?  24  VAL   A HA   1 
ATOM   610  H HB   A VAL   A 1 24  ? 16.835 5.316   10.474  0.76 22.45 ?  24  VAL   A HB   1 
ATOM   611  H HB   B VAL   A 1 24  ? 17.213 4.835   10.461  0.24 20.82 ?  24  VAL   A HB   1 
ATOM   612  H HG11 A VAL   A 1 24  ? 18.460 6.993   11.164  0.76 23.48 ?  24  VAL   A HG11 1 
ATOM   613  H HG11 B VAL   A 1 24  ? 18.877 6.457   11.010  0.24 21.46 ?  24  VAL   A HG11 1 
ATOM   614  H HG12 A VAL   A 1 24  ? 17.631 6.293   12.322  0.76 23.48 ?  24  VAL   A HG12 1 
ATOM   615  H HG12 B VAL   A 1 24  ? 18.196 5.768   12.267  0.24 21.46 ?  24  VAL   A HG12 1 
ATOM   616  H HG13 A VAL   A 1 24  ? 19.122 5.829   12.017  0.76 23.48 ?  24  VAL   A HG13 1 
ATOM   617  H HG13 B VAL   A 1 24  ? 19.641 5.304   11.790  0.24 21.46 ?  24  VAL   A HG13 1 
ATOM   618  H HG21 A VAL   A 1 24  ? 18.294 6.112   8.904   0.76 23.31 ?  24  VAL   A HG21 1 
ATOM   619  H HG21 B VAL   A 1 24  ? 18.850 5.497   8.882   0.24 20.76 ?  24  VAL   A HG21 1 
ATOM   620  H HG22 A VAL   A 1 24  ? 19.452 5.174   9.450   0.76 23.31 ?  24  VAL   A HG22 1 
ATOM   621  H HG22 B VAL   A 1 24  ? 19.714 4.237   9.314   0.24 20.76 ?  24  VAL   A HG22 1 
ATOM   622  H HG23 A VAL   A 1 24  ? 18.198 4.538   8.709   0.76 23.31 ?  24  VAL   A HG23 1 
ATOM   623  H HG23 B VAL   A 1 24  ? 18.303 4.030   8.617   0.24 20.76 ?  24  VAL   A HG23 1 
ATOM   624  N N    A GLU   A 1 25  ? 16.075 3.636   12.783  0.76 19.19 ?  25  GLU   A N    1 
ATOM   625  N N    B GLU   A 1 25  ? 16.233 3.123   12.640  0.24 17.96 ?  25  GLU   A N    1 
ATOM   626  C CA   A GLU   A 1 25  ? 15.493 3.565   14.119  0.76 20.68 ?  25  GLU   A CA   1 
ATOM   627  C CA   B GLU   A 1 25  ? 15.533 3.042   13.918  0.24 18.84 ?  25  GLU   A CA   1 
ATOM   628  C C    A GLU   A 1 25  ? 15.735 2.207   14.764  0.76 19.34 ?  25  GLU   A C    1 
ATOM   629  C C    B GLU   A 1 25  ? 15.760 1.691   14.584  0.24 18.35 ?  25  GLU   A C    1 
ATOM   630  O O    A GLU   A 1 25  ? 15.952 2.132   15.978  0.76 20.39 ?  25  GLU   A O    1 
ATOM   631  O O    B GLU   A 1 25  ? 15.981 1.623   15.799  0.24 18.66 ?  25  GLU   A O    1 
ATOM   632  C CB   A GLU   A 1 25  ? 14.002 3.904   14.057  0.76 23.43 ?  25  GLU   A CB   1 
ATOM   633  C CB   B GLU   A 1 25  ? 14.044 3.335   13.727  0.24 20.06 ?  25  GLU   A CB   1 
ATOM   634  C CG   A GLU   A 1 25  ? 13.732 5.358   13.685  0.76 26.84 ?  25  GLU   A CG   1 
ATOM   635  C CG   B GLU   A 1 25  ? 13.752 4.793   13.404  0.24 21.63 ?  25  GLU   A CG   1 
ATOM   636  C CD   A GLU   A 1 25  ? 14.520 6.335   14.542  0.76 29.60 ?  25  GLU   A CD   1 
ATOM   637  C CD   B GLU   A 1 25  ? 14.233 5.736   14.489  0.24 22.80 ?  25  GLU   A CD   1 
ATOM   638  O OE1  A GLU   A 1 25  ? 14.544 6.158   15.779  0.76 30.38 ?  25  GLU   A OE1  1 
ATOM   639  O OE1  B GLU   A 1 25  ? 14.181 5.350   15.677  0.24 22.99 ?  25  GLU   A OE1  1 
ATOM   640  O OE2  A GLU   A 1 25  ? 15.135 7.264   13.976  0.76 31.14 -1 25  GLU   A OE2  1 
ATOM   641  O OE2  B GLU   A 1 25  ? 14.669 6.858   14.156  0.24 23.54 -1 25  GLU   A OE2  1 
ATOM   642  H H    A GLU   A 1 25  ? 15.501 3.702   12.144  0.76 23.03 ?  25  GLU   A H    1 
ATOM   643  H H    B GLU   A 1 25  ? 15.722 3.143   11.951  0.24 21.56 ?  25  GLU   A H    1 
ATOM   644  H HA   A GLU   A 1 25  ? 15.926 4.222   14.683  0.76 24.81 ?  25  GLU   A HA   1 
ATOM   645  H HA   B GLU   A 1 25  ? 15.896 3.715   14.511  0.24 22.61 ?  25  GLU   A HA   1 
ATOM   646  H HB2  A GLU   A 1 25  ? 13.574 3.346   13.386  0.76 28.12 ?  25  GLU   A HB2  1 
ATOM   647  H HB2  B GLU   A 1 25  ? 13.704 2.794   12.997  0.24 24.07 ?  25  GLU   A HB2  1 
ATOM   648  H HB3  A GLU   A 1 25  ? 13.599 3.742   14.924  0.76 28.12 ?  25  GLU   A HB3  1 
ATOM   649  H HB3  B GLU   A 1 25  ? 13.573 3.116   14.544  0.24 24.07 ?  25  GLU   A HB3  1 
ATOM   650  H HG2  A GLU   A 1 25  ? 13.993 5.503   12.764  0.76 32.21 ?  25  GLU   A HG2  1 
ATOM   651  H HG2  B GLU   A 1 25  ? 14.195 5.030   12.573  0.24 25.95 ?  25  GLU   A HG2  1 
ATOM   652  H HG3  A GLU   A 1 25  ? 12.785 5.544   13.798  0.76 32.21 ?  25  GLU   A HG3  1 
ATOM   653  H HG3  B GLU   A 1 25  ? 12.796 4.917   13.318  0.24 25.95 ?  25  GLU   A HG3  1 
ATOM   654  N N    A GLU   A 1 26  ? 15.731 1.133   13.971  0.76 18.94 ?  26  GLU   A N    1 
ATOM   655  N N    B GLU   A 1 26  ? 15.724 0.605   13.809  0.24 18.03 ?  26  GLU   A N    1 
ATOM   656  C CA   A GLU   A 1 26  ? 16.026 -0.190  14.513  0.76 18.50 ?  26  GLU   A CA   1 
ATOM   657  C CA   B GLU   A 1 26  ? 16.144 -0.680  14.354  0.24 17.71 ?  26  GLU   A CA   1 
ATOM   658  C C    A GLU   A 1 26  ? 17.453 -0.265  15.048  0.76 18.31 ?  26  GLU   A C    1 
ATOM   659  C C    B GLU   A 1 26  ? 17.566 -0.607  14.884  0.24 17.69 ?  26  GLU   A C    1 
ATOM   660  O O    A GLU   A 1 26  ? 17.690 -0.764  16.154  0.76 18.04 ?  26  GLU   A O    1 
ATOM   661  O O    B GLU   A 1 26  ? 17.892 -1.270  15.875  0.24 17.70 ?  26  GLU   A O    1 
ATOM   662  C CB   A GLU   A 1 26  ? 15.818 -1.248  13.431  0.76 19.85 ?  26  GLU   A CB   1 
ATOM   663  C CB   B GLU   A 1 26  ? 16.046 -1.782  13.295  0.24 17.81 ?  26  GLU   A CB   1 
ATOM   664  C CG   A GLU   A 1 26  ? 14.392 -1.698  13.234  0.76 22.51 ?  26  GLU   A CG   1 
ATOM   665  C CG   B GLU   A 1 26  ? 14.670 -2.390  13.141  0.24 16.95 ?  26  GLU   A CG   1 
ATOM   666  C CD   A GLU   A 1 26  ? 13.845 -2.457  14.417  0.76 24.74 ?  26  GLU   A CD   1 
ATOM   667  C CD   B GLU   A 1 26  ? 14.149 -2.978  14.439  0.24 16.01 ?  26  GLU   A CD   1 
ATOM   668  O OE1  A GLU   A 1 26  ? 14.448 -3.473  14.828  0.76 25.42 ?  26  GLU   A OE1  1 
ATOM   669  O OE1  B GLU   A 1 26  ? 14.496 -4.133  14.784  0.24 15.42 ?  26  GLU   A OE1  1 
ATOM   670  O OE2  A GLU   A 1 26  ? 12.803 -2.019  14.937  0.76 26.31 -1 26  GLU   A OE2  1 
ATOM   671  O OE2  B GLU   A 1 26  ? 13.399 -2.269  15.129  0.24 15.57 -1 26  GLU   A OE2  1 
ATOM   672  H H    A GLU   A 1 26  ? 15.572 1.153   13.124  0.76 22.73 ?  26  GLU   A H    1 
ATOM   673  H H    B GLU   A 1 26  ? 15.471 0.584   12.989  0.24 21.64 ?  26  GLU   A H    1 
ATOM   674  H HA   A GLU   A 1 26  ? 15.415 -0.372  15.240  0.76 22.20 ?  26  GLU   A HA   1 
ATOM   675  H HA   B GLU   A 1 26  ? 15.572 -0.912  15.099  0.24 21.25 ?  26  GLU   A HA   1 
ATOM   676  H HB2  A GLU   A 1 26  ? 16.126 -0.889  12.583  0.76 23.82 ?  26  GLU   A HB2  1 
ATOM   677  H HB2  B GLU   A 1 26  ? 16.300 -1.414  12.437  0.24 21.37 ?  26  GLU   A HB2  1 
ATOM   678  H HB3  A GLU   A 1 26  ? 16.345 -2.027  13.663  0.76 23.82 ?  26  GLU   A HB3  1 
ATOM   679  H HB3  B GLU   A 1 26  ? 16.654 -2.501  13.535  0.24 21.37 ?  26  GLU   A HB3  1 
ATOM   680  H HG2  A GLU   A 1 26  ? 13.824 -0.925  13.126  0.76 27.01 ?  26  GLU   A HG2  1 
ATOM   681  H HG2  B GLU   A 1 26  ? 14.058 -1.704  12.823  0.24 20.34 ?  26  GLU   A HG2  1 
ATOM   682  H HG3  A GLU   A 1 26  ? 14.343 -2.262  12.445  0.76 27.01 ?  26  GLU   A HG3  1 
ATOM   683  H HG3  B GLU   A 1 26  ? 14.709 -3.118  12.506  0.24 20.34 ?  26  GLU   A HG3  1 
ATOM   684  N N    . ALA   A 1 27  ? 18.424 0.200   14.256  1.00 17.78 ?  27  ALA   A N    1 
ATOM   685  C CA   . ALA   A 1 27  ? 19.815 0.203   14.696  1.00 18.23 ?  27  ALA   A CA   1 
ATOM   686  C C    . ALA   A 1 27  ? 19.989 0.997   15.984  1.00 19.95 ?  27  ALA   A C    1 
ATOM   687  O O    . ALA   A 1 27  ? 20.669 0.544   16.911  1.00 19.74 ?  27  ALA   A O    1 
ATOM   688  C CB   . ALA   A 1 27  ? 20.732 0.736   13.591  1.00 17.42 ?  27  ALA   A CB   1 
ATOM   689  H H    A ALA   A 1 27  ? 18.301 0.513   13.463  0.76 21.34 ?  27  ALA   A H    1 
ATOM   690  H H    B ALA   A 1 27  ? 18.231 0.736   13.609  0.24 21.34 ?  27  ALA   A H    1 
ATOM   691  H HA   . ALA   A 1 27  ? 20.080 -0.709  14.878  1.00 21.88 ?  27  ALA   A HA   1 
ATOM   692  H HB1  . ALA   A 1 27  ? 21.651 0.726   13.912  1.00 20.91 ?  27  ALA   A HB1  1 
ATOM   693  H HB2  . ALA   A 1 27  ? 20.653 0.164   12.810  1.00 20.91 ?  27  ALA   A HB2  1 
ATOM   694  H HB3  . ALA   A 1 27  ? 20.473 1.641   13.367  1.00 20.91 ?  27  ALA   A HB3  1 
ATOM   695  N N    A LYS   A 1 28  ? 19.371 2.178   16.067  0.76 21.12 ?  28  LYS   A N    1 
ATOM   696  N N    B LYS   A 1 28  ? 19.371 2.179   16.067  0.24 22.11 ?  28  LYS   A N    1 
ATOM   697  C CA   A LYS   A 1 28  ? 19.509 2.993   17.270  0.76 23.97 ?  28  LYS   A CA   1 
ATOM   698  C CA   B LYS   A 1 28  ? 19.504 2.997   17.270  0.24 24.63 ?  28  LYS   A CA   1 
ATOM   699  C C    A LYS   A 1 28  ? 18.953 2.285   18.498  0.76 25.01 ?  28  LYS   A C    1 
ATOM   700  C C    B LYS   A 1 28  ? 18.951 2.287   18.498  0.24 25.20 ?  28  LYS   A C    1 
ATOM   701  O O    A LYS   A 1 28  ? 19.495 2.439   19.598  0.76 26.46 ?  28  LYS   A O    1 
ATOM   702  O O    B LYS   A 1 28  ? 19.486 2.450   19.600  0.24 25.94 ?  28  LYS   A O    1 
ATOM   703  C CB   A LYS   A 1 28  ? 18.850 4.359   17.071  0.76 26.24 ?  28  LYS   A CB   1 
ATOM   704  C CB   B LYS   A 1 28  ? 18.820 4.352   17.073  0.24 26.54 ?  28  LYS   A CB   1 
ATOM   705  C CG   A LYS   A 1 28  ? 19.663 5.286   16.180  0.76 28.59 ?  28  LYS   A CG   1 
ATOM   706  C CG   B LYS   A 1 28  ? 19.559 5.272   16.115  0.24 28.27 ?  28  LYS   A CG   1 
ATOM   707  C CD   A LYS   A 1 28  ? 19.176 6.722   16.243  0.76 31.26 ?  28  LYS   A CD   1 
ATOM   708  C CD   B LYS   A 1 28  ? 19.112 6.722   16.248  0.24 29.80 ?  28  LYS   A CD   1 
ATOM   709  C CE   A LYS   A 1 28  ? 17.883 6.900   15.479  0.76 33.06 ?  28  LYS   A CE   1 
ATOM   710  C CE   B LYS   A 1 28  ? 17.772 6.965   15.579  0.24 30.95 ?  28  LYS   A CE   1 
ATOM   711  N NZ   A LYS   A 1 28  ? 17.474 8.330   15.428  0.76 34.23 ?  28  LYS   A NZ   1 
ATOM   712  N NZ   B LYS   A 1 28  ? 17.453 8.419   15.507  0.24 31.54 ?  28  LYS   A NZ   1 
ATOM   713  H H    A LYS   A 1 28  ? 18.879 2.522   15.454  0.76 25.34 ?  28  LYS   A H    1 
ATOM   714  H H    B LYS   A 1 28  ? 18.879 2.522   15.453  0.24 26.53 ?  28  LYS   A H    1 
ATOM   715  H HA   A LYS   A 1 28  ? 20.449 3.148   17.434  0.76 28.76 ?  28  LYS   A HA   1 
ATOM   716  H HA   B LYS   A 1 28  ? 20.442 3.164   17.430  0.24 29.55 ?  28  LYS   A HA   1 
ATOM   717  H HB2  A LYS   A 1 28  ? 17.982 4.237   16.659  0.76 31.49 ?  28  LYS   A HB2  1 
ATOM   718  H HB2  B LYS   A 1 28  ? 17.929 4.209   16.717  0.24 31.85 ?  28  LYS   A HB2  1 
ATOM   719  H HB3  A LYS   A 1 28  ? 18.749 4.792   17.935  0.76 31.49 ?  28  LYS   A HB3  1 
ATOM   720  H HB3  B LYS   A 1 28  ? 18.762 4.803   17.931  0.24 31.85 ?  28  LYS   A HB3  1 
ATOM   721  H HG2  A LYS   A 1 28  ? 20.590 5.270   16.466  0.76 34.31 ?  28  LYS   A HG2  1 
ATOM   722  H HG2  B LYS   A 1 28  ? 20.509 5.231   16.304  0.24 33.93 ?  28  LYS   A HG2  1 
ATOM   723  H HG3  A LYS   A 1 28  ? 19.592 4.985   15.261  0.76 34.31 ?  28  LYS   A HG3  1 
ATOM   724  H HG3  B LYS   A 1 28  ? 19.388 4.986   15.204  0.24 33.93 ?  28  LYS   A HG3  1 
ATOM   725  H HD2  A LYS   A 1 28  ? 19.018 6.968   17.169  0.76 37.51 ?  28  LYS   A HD2  1 
ATOM   726  H HD2  B LYS   A 1 28  ? 19.026 6.945   17.189  0.24 35.76 ?  28  LYS   A HD2  1 
ATOM   727  H HD3  A LYS   A 1 28  ? 19.845 7.306   15.851  0.76 37.51 ?  28  LYS   A HD3  1 
ATOM   728  H HD3  B LYS   A 1 28  ? 19.769 7.298   15.828  0.24 35.76 ?  28  LYS   A HD3  1 
ATOM   729  H HE2  A LYS   A 1 28  ? 18.005 6.585   14.569  0.76 39.67 ?  28  LYS   A HE2  1 
ATOM   730  H HE2  B LYS   A 1 28  ? 17.797 6.614   14.675  0.24 37.14 ?  28  LYS   A HE2  1 
ATOM   731  H HE3  A LYS   A 1 28  ? 17.180 6.396   15.917  0.76 39.67 ?  28  LYS   A HE3  1 
ATOM   732  H HE3  B LYS   A 1 28  ? 17.074 6.526   16.090  0.24 37.14 ?  28  LYS   A HE3  1 
ATOM   733  H HZ1  A LYS   A 1 28  ? 16.714 8.413   14.974  0.76 41.07 ?  28  LYS   A HZ1  1 
ATOM   734  H HZ1  B LYS   A 1 28  ? 16.666 8.540   15.111  0.24 37.84 ?  28  LYS   A HZ1  1 
ATOM   735  H HZ2  A LYS   A 1 28  ? 17.355 8.641   16.253  0.76 41.07 ?  28  LYS   A HZ2  1 
ATOM   736  H HZ2  B LYS   A 1 28  ? 17.422 8.765   16.327  0.24 37.84 ?  28  LYS   A HZ2  1 
ATOM   737  H HZ3  A LYS   A 1 28  ? 18.106 8.813   15.026  0.76 41.07 ?  28  LYS   A HZ3  1 
ATOM   738  H HZ3  B LYS   A 1 28  ? 18.080 8.845   15.039  0.24 37.84 ?  28  LYS   A HZ3  1 
ATOM   739  N N    . LYS   A 1 29  ? 17.889 1.497   18.332  1.00 25.13 ?  29  LYS   A N    1 
ATOM   740  C CA   . LYS   A 1 29  ? 17.301 0.784   19.464  1.00 27.05 ?  29  LYS   A CA   1 
ATOM   741  C C    . LYS   A 1 29  ? 18.129 -0.437  19.853  1.00 26.28 ?  29  LYS   A C    1 
ATOM   742  O O    . LYS   A 1 29  ? 18.407 -0.658  21.038  1.00 27.57 ?  29  LYS   A O    1 
ATOM   743  C CB   . LYS   A 1 29  ? 15.872 0.357   19.117  1.00 30.61 ?  29  LYS   A CB   1 
ATOM   744  C CG   . LYS   A 1 29  ? 15.108 -0.282  20.268  1.00 34.11 ?  29  LYS   A CG   1 
ATOM   745  C CD   . LYS   A 1 29  ? 14.748 0.744   21.330  1.00 37.04 ?  29  LYS   A CD   1 
ATOM   746  C CE   . LYS   A 1 29  ? 13.894 0.131   22.429  1.00 39.12 ?  29  LYS   A CE   1 
ATOM   747  N NZ   . LYS   A 1 29  ? 13.492 1.141   23.446  1.00 40.13 ?  29  LYS   A NZ   1 
ATOM   748  H H    A LYS   A 1 29  ? 17.490 1.361   17.581  0.76 30.16 ?  29  LYS   A H    1 
ATOM   749  H H    B LYS   A 1 29  ? 17.488 1.364   17.582  0.24 30.16 ?  29  LYS   A H    1 
ATOM   750  H HA   . LYS   A 1 29  ? 17.260 1.378   20.228  1.00 32.46 ?  29  LYS   A HA   1 
ATOM   751  H HB2  . LYS   A 1 29  ? 15.374 1.139   18.835  1.00 36.73 ?  29  LYS   A HB2  1 
ATOM   752  H HB3  . LYS   A 1 29  ? 15.906 -0.289  18.395  1.00 36.73 ?  29  LYS   A HB3  1 
ATOM   753  H HG2  . LYS   A 1 29  ? 14.284 -0.668  19.930  1.00 40.93 ?  29  LYS   A HG2  1 
ATOM   754  H HG3  . LYS   A 1 29  ? 15.653 -0.970  20.682  1.00 40.93 ?  29  LYS   A HG3  1 
ATOM   755  H HD2  . LYS   A 1 29  ? 15.561 1.088   21.733  1.00 44.45 ?  29  LYS   A HD2  1 
ATOM   756  H HD3  . LYS   A 1 29  ? 14.245 1.466   20.921  1.00 44.45 ?  29  LYS   A HD3  1 
ATOM   757  H HE2  . LYS   A 1 29  ? 13.089 -0.241  22.036  1.00 46.94 ?  29  LYS   A HE2  1 
ATOM   758  H HE3  . LYS   A 1 29  ? 14.401 -0.565  22.875  1.00 46.94 ?  29  LYS   A HE3  1 
ATOM   759  H HZ1  . LYS   A 1 29  ? 12.994 0.756   24.076  1.00 48.16 ?  29  LYS   A HZ1  1 
ATOM   760  H HZ2  . LYS   A 1 29  ? 14.215 1.495   23.825  1.00 48.16 ?  29  LYS   A HZ2  1 
ATOM   761  H HZ3  . LYS   A 1 29  ? 13.020 1.790   23.061  1.00 48.16 ?  29  LYS   A HZ3  1 
ATOM   762  N N    . VAL   A 1 30  ? 18.511 -1.252  18.870  1.00 25.48 ?  30  VAL   A N    1 
ATOM   763  C CA   . VAL   A 1 30  ? 19.154 -2.529  19.159  1.00 24.67 ?  30  VAL   A CA   1 
ATOM   764  C C    . VAL   A 1 30  ? 20.657 -2.378  19.378  1.00 23.63 ?  30  VAL   A C    1 
ATOM   765  O O    . VAL   A 1 30  ? 21.247 -3.120  20.171  1.00 24.21 ?  30  VAL   A O    1 
ATOM   766  C CB   . VAL   A 1 30  ? 18.849 -3.516  18.020  1.00 25.85 ?  30  VAL   A CB   1 
ATOM   767  C CG1  . VAL   A 1 30  ? 19.626 -4.811  18.202  1.00 26.39 ?  30  VAL   A CG1  1 
ATOM   768  C CG2  . VAL   A 1 30  ? 17.354 -3.790  17.944  1.00 26.61 ?  30  VAL   A CG2  1 
ATOM   769  H H    . VAL   A 1 30  ? 18.395 -1.096  18.031  1.00 30.58 ?  30  VAL   A H    1 
ATOM   770  H HA   . VAL   A 1 30  ? 18.767 -2.893  19.969  1.00 29.61 ?  30  VAL   A HA   1 
ATOM   771  H HB   . VAL   A 1 30  ? 19.122 -3.124  17.176  1.00 31.02 ?  30  VAL   A HB   1 
ATOM   772  H HG11 . VAL   A 1 30  ? 19.243 -5.491  17.624  1.00 31.67 ?  30  VAL   A HG11 1 
ATOM   773  H HG12 . VAL   A 1 30  ? 20.553 -4.661  17.966  1.00 31.67 ?  30  VAL   A HG12 1 
ATOM   774  H HG13 . VAL   A 1 30  ? 19.556 -5.091  19.128  1.00 31.67 ?  30  VAL   A HG13 1 
ATOM   775  H HG21 . VAL   A 1 30  ? 17.186 -4.449  17.251  1.00 31.93 ?  30  VAL   A HG21 1 
ATOM   776  H HG22 . VAL   A 1 30  ? 17.052 -4.130  18.801  1.00 31.93 ?  30  VAL   A HG22 1 
ATOM   777  H HG23 . VAL   A 1 30  ? 16.891 -2.965  17.734  1.00 31.93 ?  30  VAL   A HG23 1 
ATOM   778  N N    . LYS   A 1 31  ? 21.295 -1.436  18.693  1.00 22.18 ?  31  LYS   A N    1 
ATOM   779  C CA   . LYS   A 1 31  ? 22.750 -1.337  18.645  1.00 22.91 ?  31  LYS   A CA   1 
ATOM   780  C C    . LYS   A 1 31  ? 23.360 -2.694  18.284  1.00 20.60 ?  31  LYS   A C    1 
ATOM   781  O O    . LYS   A 1 31  ? 24.146 -3.256  19.055  1.00 21.57 ?  31  LYS   A O    1 
ATOM   782  C CB   . LYS   A 1 31  ? 23.329 -0.804  19.947  1.00 27.83 ?  31  LYS   A CB   1 
ATOM   783  C CG   . LYS   A 1 31  ? 22.642 0.452   20.459  1.00 33.88 ?  31  LYS   A CG   1 
ATOM   784  C CD   . LYS   A 1 31  ? 23.650 1.539   20.806  1.00 38.56 ?  31  LYS   A CD   1 
ATOM   785  C CE   . LYS   A 1 31  ? 23.043 2.590   21.722  1.00 41.08 ?  31  LYS   A CE   1 
ATOM   786  N NZ   . LYS   A 1 31  ? 21.815 3.211   21.156  1.00 42.80 ?  31  LYS   A NZ   1 
ATOM   787  H H    . LYS   A 1 31  ? 20.895 -0.824  18.239  1.00 26.62 ?  31  LYS   A H    1 
ATOM   788  H HA   . LYS   A 1 31  ? 22.985 -0.714  17.945  1.00 27.49 ?  31  LYS   A HA   1 
ATOM   789  H HB2  . LYS   A 1 31  ? 23.245 -1.490  20.621  1.00 33.40 ?  31  LYS   A HB2  1 
ATOM   790  H HB3  . LYS   A 1 31  ? 24.267 -0.595  19.805  1.00 33.40 ?  31  LYS   A HB3  1 
ATOM   791  H HG2  . LYS   A 1 31  ? 22.050 0.797   19.771  1.00 40.65 ?  31  LYS   A HG2  1 
ATOM   792  H HG3  . LYS   A 1 31  ? 22.138 0.237   21.259  1.00 40.65 ?  31  LYS   A HG3  1 
ATOM   793  H HD2  . LYS   A 1 31  ? 24.408 1.139   21.261  1.00 46.28 ?  31  LYS   A HD2  1 
ATOM   794  H HD3  . LYS   A 1 31  ? 23.941 1.977   19.990  1.00 46.28 ?  31  LYS   A HD3  1 
ATOM   795  H HE2  . LYS   A 1 31  ? 22.804 2.172   22.563  1.00 49.29 ?  31  LYS   A HE2  1 
ATOM   796  H HE3  . LYS   A 1 31  ? 23.695 3.293   21.874  1.00 49.29 ?  31  LYS   A HE3  1 
ATOM   797  H HZ1  . LYS   A 1 31  ? 21.501 3.829   21.715  1.00 51.37 ?  31  LYS   A HZ1  1 
ATOM   798  H HZ2  . LYS   A 1 31  ? 22.001 3.595   20.375  1.00 51.37 ?  31  LYS   A HZ2  1 
ATOM   799  H HZ3  . LYS   A 1 31  ? 21.190 2.590   21.031  1.00 51.37 ?  31  LYS   A HZ3  1 
ATOM   800  N N    . PRO   A 1 32  ? 23.010 -3.244  17.126  1.00 18.34 ?  32  PRO   A N    1 
ATOM   801  C CA   . PRO   A 1 32  ? 23.482 -4.581  16.769  1.00 18.59 ?  32  PRO   A CA   1 
ATOM   802  C C    . PRO   A 1 32  ? 24.982 -4.598  16.552  1.00 18.67 ?  32  PRO   A C    1 
ATOM   803  O O    . PRO   A 1 32  ? 25.626 -3.569  16.337  1.00 18.28 ?  32  PRO   A O    1 
ATOM   804  C CB   . PRO   A 1 32  ? 22.744 -4.865  15.456  1.00 18.70 ?  32  PRO   A CB   1 
ATOM   805  C CG   . PRO   A 1 32  ? 22.570 -3.504  14.847  1.00 17.48 ?  32  PRO   A CG   1 
ATOM   806  C CD   . PRO   A 1 32  ? 22.269 -2.614  16.021  1.00 17.29 ?  32  PRO   A CD   1 
ATOM   807  H HA   . PRO   A 1 32  ? 23.233 -5.231  17.439  1.00 22.31 ?  32  PRO   A HA   1 
ATOM   808  H HB2  . PRO   A 1 32  ? 23.282 -5.439  14.884  1.00 22.43 ?  32  PRO   A HB2  1 
ATOM   809  H HB3  . PRO   A 1 32  ? 21.882 -5.278  15.641  1.00 22.43 ?  32  PRO   A HB3  1 
ATOM   810  H HG2  . PRO   A 1 32  ? 23.388 -3.243  14.402  1.00 20.98 ?  32  PRO   A HG2  1 
ATOM   811  H HG3  . PRO   A 1 32  ? 21.826 -3.524  14.219  1.00 20.98 ?  32  PRO   A HG3  1 
ATOM   812  H HD2  . PRO   A 1 32  ? 22.602 -1.720  15.840  1.00 20.75 ?  32  PRO   A HD2  1 
ATOM   813  H HD3  . PRO   A 1 32  ? 21.319 -2.614  16.200  1.00 20.75 ?  32  PRO   A HD3  1 
ATOM   814  N N    . THR   A 1 33  ? 25.536 -5.808  16.584  1.00 18.51 ?  33  THR   A N    1 
ATOM   815  C CA   . THR   A 1 33  ? 26.948 -5.972  16.266  1.00 18.52 ?  33  THR   A CA   1 
ATOM   816  C C    . THR   A 1 33  ? 27.244 -5.507  14.846  1.00 17.03 ?  33  THR   A C    1 
ATOM   817  O O    . THR   A 1 33  ? 28.275 -4.864  14.598  1.00 17.39 ?  33  THR   A O    1 
ATOM   818  C CB   . THR   A 1 33  ? 27.359 -7.431  16.458  1.00 19.93 ?  33  THR   A CB   1 
ATOM   819  O OG1  . THR   A 1 33  ? 27.074 -7.825  17.802  1.00 21.76 ?  33  THR   A OG1  1 
ATOM   820  C CG2  . THR   A 1 33  ? 28.845 -7.610  16.194  1.00 21.08 ?  33  THR   A CG2  1 
ATOM   821  H H    . THR   A 1 33  ? 25.120 -6.537  16.777  1.00 22.21 ?  33  THR   A H    1 
ATOM   822  H HA   . THR   A 1 33  ? 27.471 -5.433  16.873  1.00 22.23 ?  33  THR   A HA   1 
ATOM   823  H HB   . THR   A 1 33  ? 26.864 -7.999  15.843  1.00 23.91 ?  33  THR   A HB   1 
ATOM   824  H HG1  . THR   A 1 33  ? 27.504 -7.345  18.344  1.00 26.11 ?  33  THR   A HG1  1 
ATOM   825  H HG21 . THR   A 1 33  ? 29.129 -8.490  16.486  1.00 25.29 ?  33  THR   A HG21 1 
ATOM   826  H HG22 . THR   A 1 33  ? 29.029 -7.518  15.247  1.00 25.29 ?  33  THR   A HG22 1 
ATOM   827  H HG23 . THR   A 1 33  ? 29.348 -6.940  16.682  1.00 25.29 ?  33  THR   A HG23 1 
ATOM   828  N N    . VAL   A 1 34  ? 26.349 -5.813  13.905  1.00 15.35 ?  34  VAL   A N    1 
ATOM   829  C CA   . VAL   A 1 34  ? 26.538 -5.477  12.499  1.00 14.16 ?  34  VAL   A CA   1 
ATOM   830  C C    . VAL   A 1 34  ? 25.239 -4.918  11.935  1.00 13.28 ?  34  VAL   A C    1 
ATOM   831  O O    . VAL   A 1 34  ? 24.196 -5.583  11.990  1.00 13.96 ?  34  VAL   A O    1 
ATOM   832  C CB   . VAL   A 1 34  ? 26.985 -6.687  11.659  1.00 14.72 ?  34  VAL   A CB   1 
ATOM   833  C CG1  . VAL   A 1 34  ? 27.166 -6.282  10.203  1.00 15.22 ?  34  VAL   A CG1  1 
ATOM   834  C CG2  . VAL   A 1 34  ? 28.267 -7.301  12.218  1.00 15.88 ?  34  VAL   A CG2  1 
ATOM   835  H H    . VAL   A 1 34  ? 25.606 -6.222  14.061  1.00 18.42 ?  34  VAL   A H    1 
ATOM   836  H HA   . VAL   A 1 34  ? 27.218 -4.788  12.420  1.00 17.00 ?  34  VAL   A HA   1 
ATOM   837  H HB   . VAL   A 1 34  ? 26.290 -7.363  11.693  1.00 17.67 ?  34  VAL   A HB   1 
ATOM   838  H HG11 . VAL   A 1 34  ? 27.661 -6.977  9.743   1.00 18.27 ?  34  VAL   A HG11 1 
ATOM   839  H HG12 . VAL   A 1 34  ? 26.297 -6.165  9.791   1.00 18.27 ?  34  VAL   A HG12 1 
ATOM   840  H HG13 . VAL   A 1 34  ? 27.665 -5.448  10.168  1.00 18.27 ?  34  VAL   A HG13 1 
ATOM   841  H HG21 . VAL   A 1 34  ? 28.542 -8.033  11.643  1.00 19.05 ?  34  VAL   A HG21 1 
ATOM   842  H HG22 . VAL   A 1 34  ? 28.957 -6.623  12.246  1.00 19.05 ?  34  VAL   A HG22 1 
ATOM   843  H HG23 . VAL   A 1 34  ? 28.092 -7.635  13.114  1.00 19.05 ?  34  VAL   A HG23 1 
ATOM   844  N N    . VAL   A 1 35  ? 25.298 -3.704  11.389  1.00 12.44 ?  35  VAL   A N    1 
ATOM   845  C CA   . VAL   A 1 35  ? 24.264 -3.189  10.501  1.00 12.05 ?  35  VAL   A CA   1 
ATOM   846  C C    . VAL   A 1 35  ? 24.815 -3.188  9.084   1.00 11.44 ?  35  VAL   A C    1 
ATOM   847  O O    . VAL   A 1 35  ? 25.959 -2.780  8.856   1.00 12.25 ?  35  VAL   A O    1 
ATOM   848  C CB   . VAL   A 1 35  ? 23.743 -1.794  10.912  1.00 12.83 ?  35  VAL   A CB   1 
ATOM   849  C CG1  . VAL   A 1 35  ? 24.821 -0.710  10.781  1.00 13.77 ?  35  VAL   A CG1  1 
ATOM   850  C CG2  . VAL   A 1 35  ? 22.500 -1.434  10.095  1.00 13.66 ?  35  VAL   A CG2  1 
ATOM   851  H H    . VAL   A 1 35  ? 25.937 -3.143  11.521  1.00 14.93 ?  35  VAL   A H    1 
ATOM   852  H HA   . VAL   A 1 35  ? 23.504 -3.794  10.522  1.00 14.46 ?  35  VAL   A HA   1 
ATOM   853  H HB   . VAL   A 1 35  ? 23.472 -1.823  11.839  1.00 15.40 ?  35  VAL   A HB   1 
ATOM   854  H HG11 . VAL   A 1 35  ? 24.484 0.124   11.153  1.00 16.53 ?  35  VAL   A HG11 1 
ATOM   855  H HG12 . VAL   A 1 35  ? 25.611 -0.989  11.270  1.00 16.53 ?  35  VAL   A HG12 1 
ATOM   856  H HG13 . VAL   A 1 35  ? 25.042 -0.582  9.844   1.00 16.53 ?  35  VAL   A HG13 1 
ATOM   857  H HG21 . VAL   A 1 35  ? 22.153 -0.582  10.401  1.00 16.40 ?  35  VAL   A HG21 1 
ATOM   858  H HG22 . VAL   A 1 35  ? 22.745 -1.369  9.155   1.00 16.40 ?  35  VAL   A HG22 1 
ATOM   859  H HG23 . VAL   A 1 35  ? 21.833 -2.126  10.212  1.00 16.40 ?  35  VAL   A HG23 1 
ATOM   860  N N    . VAL   A 1 36  ? 24.001 -3.646  8.136   1.00 10.87 ?  36  VAL   A N    1 
ATOM   861  C CA   . VAL   A 1 36  ? 24.380 -3.657  6.729   1.00 10.49 ?  36  VAL   A CA   1 
ATOM   862  C C    . VAL   A 1 36  ? 23.917 -2.364  6.072   1.00 10.91 ?  36  VAL   A C    1 
ATOM   863  O O    . VAL   A 1 36  ? 22.754 -1.961  6.218   1.00 11.36 ?  36  VAL   A O    1 
ATOM   864  C CB   . VAL   A 1 36  ? 23.776 -4.873  6.006   1.00 10.64 ?  36  VAL   A CB   1 
ATOM   865  C CG1  . VAL   A 1 36  ? 24.040 -4.794  4.522   1.00 11.00 ?  36  VAL   A CG1  1 
ATOM   866  C CG2  . VAL   A 1 36  ? 24.330 -6.170  6.582   1.00 11.93 ?  36  VAL   A CG2  1 
ATOM   867  H H    . VAL   A 1 36  ? 23.207 -3.960  8.286   1.00 13.04 ?  36  VAL   A H    1 
ATOM   868  H HA   . VAL   A 1 36  ? 25.347 -3.714  6.659   1.00 12.58 ?  36  VAL   A HA   1 
ATOM   869  H HB   . VAL   A 1 36  ? 22.816 -4.871  6.136   1.00 12.77 ?  36  VAL   A HB   1 
ATOM   870  H HG11 . VAL   A 1 36  ? 23.906 -5.670  4.130   1.00 13.20 ?  36  VAL   A HG11 1 
ATOM   871  H HG12 . VAL   A 1 36  ? 23.426 -4.156  4.121   1.00 13.20 ?  36  VAL   A HG12 1 
ATOM   872  H HG13 . VAL   A 1 36  ? 24.956 -4.505  4.380   1.00 13.20 ?  36  VAL   A HG13 1 
ATOM   873  H HG21 . VAL   A 1 36  ? 23.942 -6.923  6.106   1.00 14.31 ?  36  VAL   A HG21 1 
ATOM   874  H HG22 . VAL   A 1 36  ? 25.297 -6.179  6.472   1.00 14.31 ?  36  VAL   A HG22 1 
ATOM   875  H HG23 . VAL   A 1 36  ? 24.106 -6.226  7.524   1.00 14.31 ?  36  VAL   A HG23 1 
ATOM   876  N N    . ASN   A 1 37  ? 24.823 -1.738  5.325   1.00 10.10 ?  37  ASN   A N    1 
ATOM   877  C CA   . ASN   A 1 37  ? 24.490 -0.619  4.464   1.00 9.96  ?  37  ASN   A CA   1 
ATOM   878  C C    . ASN   A 1 37  ? 24.348 -1.086  3.025   1.00 10.06 ?  37  ASN   A C    1 
ATOM   879  O O    . ASN   A 1 37  ? 25.131 -1.911  2.540   1.00 10.77 ?  37  ASN   A O    1 
ATOM   880  C CB   . ASN   A 1 37  ? 25.568 0.458   4.540   1.00 10.35 ?  37  ASN   A CB   1 
ATOM   881  C CG   . ASN   A 1 37  ? 25.232 1.665   3.698   1.00 10.58 ?  37  ASN   A CG   1 
ATOM   882  O OD1  . ASN   A 1 37  ? 24.060 1.999   3.513   1.00 11.22 ?  37  ASN   A OD1  1 
ATOM   883  N ND2  . ASN   A 1 37  ? 26.262 2.330   3.182   1.00 11.07 ?  37  ASN   A ND2  1 
ATOM   884  H H    . ASN   A 1 37  ? 25.661 -1.946  5.312   1.00 12.12 ?  37  ASN   A H    1 
ATOM   885  H HA   . ASN   A 1 37  ? 23.652 -0.226  4.756   1.00 11.96 ?  37  ASN   A HA   1 
ATOM   886  H HB2  . ASN   A 1 37  ? 25.665 0.750   5.464   1.00 12.42 ?  37  ASN   A HB2  1 
ATOM   887  H HB3  . ASN   A 1 37  ? 26.411 0.086   4.226   1.00 12.42 ?  37  ASN   A HB3  1 
ATOM   888  H HD21 . ASN   A 1 37  ? 26.123 3.025   2.692   1.00 13.28 ?  37  ASN   A HD21 1 
ATOM   889  H HD22 . ASN   A 1 37  ? 27.064 2.076   3.334   1.00 13.28 ?  37  ASN   A HD22 1 
ATOM   890  N N    A ALA   A 1 38  ? 23.348 -0.522  2.346   0.76 10.39 ?  38  ALA   A N    1 
ATOM   891  N N    B ALA   A 1 38  ? 23.314 -0.581  2.353   0.24 10.64 ?  38  ALA   A N    1 
ATOM   892  C CA   A ALA   A 1 38  ? 23.142 -0.660  0.906   0.76 10.28 ?  38  ALA   A CA   1 
ATOM   893  C CA   B ALA   A 1 38  ? 23.123 -0.826  0.924   0.24 11.30 ?  38  ALA   A CA   1 
ATOM   894  C C    A ALA   A 1 38  ? 24.055 0.332   0.188   0.76 10.72 ?  38  ALA   A C    1 
ATOM   895  C C    B ALA   A 1 38  ? 23.942 0.211   0.160   0.24 11.45 ?  38  ALA   A C    1 
ATOM   896  O O    A ALA   A 1 38  ? 23.651 1.427   -0.212  0.76 10.53 ?  38  ALA   A O    1 
ATOM   897  O O    B ALA   A 1 38  ? 23.437 1.226   -0.326  0.24 11.45 ?  38  ALA   A O    1 
ATOM   898  C CB   A ALA   A 1 38  ? 21.673 -0.415  0.574   0.76 11.77 ?  38  ALA   A CB   1 
ATOM   899  C CB   B ALA   A 1 38  ? 21.644 -0.773  0.567   0.24 11.71 ?  38  ALA   A CB   1 
ATOM   900  H H    A ALA   A 1 38  ? 22.761 -0.015  2.722   0.76 12.47 ?  38  ALA   A H    1 
ATOM   901  H H    B ALA   A 1 38  ? 22.701 -0.089  2.712   0.24 12.76 ?  38  ALA   A H    1 
ATOM   902  H HA   A ALA   A 1 38  ? 23.380 -1.556  0.631   0.76 12.34 ?  38  ALA   A HA   1 
ATOM   903  H HA   B ALA   A 1 38  ? 23.461 -1.710  0.704   0.24 13.57 ?  38  ALA   A HA   1 
ATOM   904  H HB1  A ALA   A 1 38  ? 21.543 -0.521  -0.380  0.76 14.13 ?  38  ALA   A HB1  1 
ATOM   905  H HB1  B ALA   A 1 38  ? 21.551 -0.884  -0.391  0.24 14.06 ?  38  ALA   A HB1  1 
ATOM   906  H HB2  A ALA   A 1 38  ? 21.129 -1.061  1.056   0.76 14.13 ?  38  ALA   A HB2  1 
ATOM   907  H HB2  B ALA   A 1 38  ? 21.176 -1.485  1.031   0.24 14.06 ?  38  ALA   A HB2  1 
ATOM   908  H HB3  A ALA   A 1 38  ? 21.431 0.484   0.845   0.76 14.13 ?  38  ALA   A HB3  1 
ATOM   909  H HB3  B ALA   A 1 38  ? 21.287 0.088   0.835   0.24 14.06 ?  38  ALA   A HB3  1 
ATOM   910  N N    A ALA   A 1 39  ? 25.318 -0.059  0.042   0.76 10.66 ?  39  ALA   A N    1 
ATOM   911  N N    B ALA   A 1 39  ? 25.240 -0.056  0.063   0.24 11.83 ?  39  ALA   A N    1 
ATOM   912  C CA   A ALA   A 1 39  ? 26.373 0.816   -0.440  0.76 10.65 ?  39  ALA   A CA   1 
ATOM   913  C CA   B ALA   A 1 39  ? 26.196 0.913   -0.442  0.24 12.13 ?  39  ALA   A CA   1 
ATOM   914  C C    A ALA   A 1 39  ? 26.488 0.776   -1.962  0.76 10.63 ?  39  ALA   A C    1 
ATOM   915  C C    B ALA   A 1 39  ? 26.384 0.768   -1.950  0.24 11.50 ?  39  ALA   A C    1 
ATOM   916  O O    A ALA   A 1 39  ? 25.978 -0.126  -2.634  0.76 11.17 ?  39  ALA   A O    1 
ATOM   917  O O    B ALA   A 1 39  ? 25.986 -0.223  -2.566  0.24 11.61 ?  39  ALA   A O    1 
ATOM   918  C CB   A ALA   A 1 39  ? 27.702 0.394   0.187   0.76 10.98 ?  39  ALA   A CB   1 
ATOM   919  C CB   B ALA   A 1 39  ? 27.537 0.739   0.270   0.24 12.63 ?  39  ALA   A CB   1 
ATOM   920  H H    A ALA   A 1 39  ? 25.589 -0.857  0.224   0.76 12.79 ?  39  ALA   A H    1 
ATOM   921  H H    B ALA   A 1 39  ? 25.590 -0.811  0.283   0.24 14.20 ?  39  ALA   A H    1 
ATOM   922  H HA   A ALA   A 1 39  ? 26.176 1.727   -0.173  0.76 12.78 ?  39  ALA   A HA   1 
ATOM   923  H HA   B ALA   A 1 39  ? 25.868 1.806   -0.259  0.24 14.56 ?  39  ALA   A HA   1 
ATOM   924  H HB1  A ALA   A 1 39  ? 28.397 0.985   -0.138  0.76 13.18 ?  39  ALA   A HB1  1 
ATOM   925  H HB1  B ALA   A 1 39  ? 28.164 1.392   -0.078  0.24 15.16 ?  39  ALA   A HB1  1 
ATOM   926  H HB2  A ALA   A 1 39  ? 27.626 0.470   1.153   0.76 13.18 ?  39  ALA   A HB2  1 
ATOM   927  H HB2  B ALA   A 1 39  ? 27.409 0.877   1.222   0.24 15.16 ?  39  ALA   A HB2  1 
ATOM   928  H HB3  A ALA   A 1 39  ? 27.891 -0.519  -0.062  0.76 13.18 ?  39  ALA   A HB3  1 
ATOM   929  H HB3  B ALA   A 1 39  ? 27.868 -0.158  0.107   0.24 15.16 ?  39  ALA   A HB3  1 
ATOM   930  N N    A ASN   A 1 40  ? 27.190 1.772   -2.500  0.76 10.99 ?  40  ASN   A N    1 
ATOM   931  N N    B ASN   A 1 40  ? 27.002 1.784   -2.545  0.24 11.35 ?  40  ASN   A N    1 
ATOM   932  C CA   A ASN   A 1 40  ? 27.732 1.732   -3.851  0.76 11.25 ?  40  ASN   A CA   1 
ATOM   933  C CA   B ASN   A 1 40  ? 27.481 1.732   -3.918  0.24 11.49 ?  40  ASN   A CA   1 
ATOM   934  C C    A ASN   A 1 40  ? 29.259 1.632   -3.782  0.76 10.22 ?  40  ASN   A C    1 
ATOM   935  C C    B ASN   A 1 40  ? 29.001 1.589   -3.913  0.24 11.58 ?  40  ASN   A C    1 
ATOM   936  O O    A ASN   A 1 40  ? 29.857 1.743   -2.709  0.76 10.65 ?  40  ASN   A O    1 
ATOM   937  O O    B ASN   A 1 40  ? 29.647 1.599   -2.862  0.24 11.46 ?  40  ASN   A O    1 
ATOM   938  C CB   A ASN   A 1 40  ? 27.236 2.918   -4.702  0.76 12.08 ?  40  ASN   A CB   1 
ATOM   939  C CB   B ASN   A 1 40  ? 27.034 2.965   -4.709  0.24 12.02 ?  40  ASN   A CB   1 
ATOM   940  C CG   A ASN   A 1 40  ? 27.620 4.272   -4.131  0.76 13.03 ?  40  ASN   A CG   1 
ATOM   941  C CG   B ASN   A 1 40  ? 27.378 4.264   -4.011  0.24 12.58 ?  40  ASN   A CG   1 
ATOM   942  O OD1  A ASN   A 1 40  ? 28.792 4.520   -3.827  0.76 14.09 ?  40  ASN   A OD1  1 
ATOM   943  O OD1  B ASN   A 1 40  ? 28.549 4.588   -3.821  0.24 13.56 ?  40  ASN   A OD1  1 
ATOM   944  N ND2  A ASN   A 1 40  ? 26.626 5.155   -3.984  0.76 13.54 ?  40  ASN   A ND2  1 
ATOM   945  N ND2  B ASN   A 1 40  ? 26.355 5.020   -3.631  0.24 12.62 ?  40  ASN   A ND2  1 
ATOM   946  H H    A ASN   A 1 40  ? 27.376 2.497   -2.086  0.76 13.18 ?  40  ASN   A H    1 
ATOM   947  H H    B ASN   A 1 40  ? 27.162 2.535   -2.157  0.24 13.63 ?  40  ASN   A H    1 
ATOM   948  H HA   A ASN   A 1 40  ? 27.418 0.922   -4.284  0.76 13.50 ?  40  ASN   A HA   1 
ATOM   949  H HA   B ASN   A 1 40  ? 27.111 0.944   -4.353  0.24 13.79 ?  40  ASN   A HA   1 
ATOM   950  H HB2  A ASN   A 1 40  ? 27.616 2.845   -5.594  0.76 14.49 ?  40  ASN   A HB2  1 
ATOM   951  H HB2  B ASN   A 1 40  ? 27.474 2.961   -5.575  0.24 14.42 ?  40  ASN   A HB2  1 
ATOM   952  H HB3  A ASN   A 1 40  ? 26.267 2.878   -4.757  0.76 14.49 ?  40  ASN   A HB3  1 
ATOM   953  H HB3  B ASN   A 1 40  ? 26.073 2.927   -4.831  0.24 14.42 ?  40  ASN   A HB3  1 
ATOM   954  H HD21 A ASN   A 1 40  ? 26.787 5.942   -3.670  0.76 16.25 ?  40  ASN   A HD21 1 
ATOM   955  H HD21 B ASN   A 1 40  ? 26.499 5.766   -3.231  0.24 15.15 ?  40  ASN   A HD21 1 
ATOM   956  H HD22 A ASN   A 1 40  ? 25.821 4.941   -4.203  0.76 16.25 ?  40  ASN   A HD22 1 
ATOM   957  H HD22 B ASN   A 1 40  ? 25.549 4.759   -3.781  0.24 15.15 ?  40  ASN   A HD22 1 
ATOM   958  N N    A VAL   A 1 41  ? 29.885 1.365   -4.931  0.76 10.76 ?  41  VAL   A N    1 
ATOM   959  N N    B VAL   A 1 41  ? 29.572 1.449   -5.110  0.24 11.65 ?  41  VAL   A N    1 
ATOM   960  C CA   A VAL   A 1 41  ? 31.314 1.054   -4.950  0.76 11.49 ?  41  VAL   A CA   1 
ATOM   961  C CA   B VAL   A 1 41  ? 30.996 1.131   -5.208  0.24 11.61 ?  41  VAL   A CA   1 
ATOM   962  C C    A VAL   A 1 41  ? 32.166 2.219   -4.493  0.76 12.27 ?  41  VAL   A C    1 
ATOM   963  C C    B VAL   A 1 41  ? 31.879 2.240   -4.644  0.24 11.72 ?  41  VAL   A C    1 
ATOM   964  O O    A VAL   A 1 41  ? 33.315 2.014   -4.086  0.76 12.37 ?  41  VAL   A O    1 
ATOM   965  O O    B VAL   A 1 41  ? 32.996 1.968   -4.185  0.24 11.87 ?  41  VAL   A O    1 
ATOM   966  C CB   A VAL   A 1 41  ? 31.795 0.564   -6.334  0.76 11.85 ?  41  VAL   A CB   1 
ATOM   967  C CB   B VAL   A 1 41  ? 31.388 0.754   -6.651  0.24 11.79 ?  41  VAL   A CB   1 
ATOM   968  C CG1  A VAL   A 1 41  ? 31.099 -0.737  -6.721  0.76 12.98 ?  41  VAL   A CG1  1 
ATOM   969  C CG1  B VAL   A 1 41  ? 30.778 -0.587  -7.033  0.24 12.12 ?  41  VAL   A CG1  1 
ATOM   970  C CG2  A VAL   A 1 41  ? 31.629 1.635   -7.408  0.76 12.04 ?  41  VAL   A CG2  1 
ATOM   971  C CG2  B VAL   A 1 41  ? 30.969 1.841   -7.628  0.24 12.26 ?  41  VAL   A CG2  1 
ATOM   972  H H    A VAL   A 1 41  ? 29.510 1.348   -5.701  0.76 12.91 ?  41  VAL   A H    1 
ATOM   973  H H    B VAL   A 1 41  ? 29.155 1.509   -5.864  0.24 13.98 ?  41  VAL   A H    1 
ATOM   974  H HA   A VAL   A 1 41  ? 31.475 0.328   -4.325  0.76 13.79 ?  41  VAL   A HA   1 
ATOM   975  H HA   B VAL   A 1 41  ? 31.154 0.345   -4.666  0.24 13.93 ?  41  VAL   A HA   1 
ATOM   976  H HB   A VAL   A 1 41  ? 32.746 0.367   -6.273  0.76 14.22 ?  41  VAL   A HB   1 
ATOM   977  H HB   B VAL   A 1 41  ? 32.351 0.663   -6.699  0.24 14.15 ?  41  VAL   A HB   1 
ATOM   978  H HG11 A VAL   A 1 41  ? 31.437 -1.038  -7.578  0.76 15.57 ?  41  VAL   A HG11 1 
ATOM   979  H HG11 B VAL   A 1 41  ? 30.993 -0.779  -7.958  0.24 14.55 ?  41  VAL   A HG11 1 
ATOM   980  H HG12 A VAL   A 1 41  ? 31.275 -1.407  -6.042  0.76 15.57 ?  41  VAL   A HG12 1 
ATOM   981  H HG12 B VAL   A 1 41  ? 31.150 -1.276  -6.457  0.24 14.55 ?  41  VAL   A HG12 1 
ATOM   982  H HG13 A VAL   A 1 41  ? 30.142 -0.575  -6.782  0.76 15.57 ?  41  VAL   A HG13 1 
ATOM   983  H HG13 B VAL   A 1 41  ? 29.818 -0.545  -6.916  0.24 14.55 ?  41  VAL   A HG13 1 
ATOM   984  H HG21 A VAL   A 1 41  ? 31.853 1.249   -8.271  0.76 14.44 ?  41  VAL   A HG21 1 
ATOM   985  H HG21 B VAL   A 1 41  ? 31.356 1.649   -8.495  0.24 14.71 ?  41  VAL   A HG21 1 
ATOM   986  H HG22 A VAL   A 1 41  ? 30.712 1.939   -7.408  0.76 14.44 ?  41  VAL   A HG22 1 
ATOM   987  H HG22 B VAL   A 1 41  ? 30.001 1.856   -7.696  0.24 14.71 ?  41  VAL   A HG22 1 
ATOM   988  H HG23 A VAL   A 1 41  ? 32.228 2.372   -7.213  0.76 14.44 ?  41  VAL   A HG23 1 
ATOM   989  H HG23 B VAL   A 1 41  ? 31.291 2.694   -7.303  0.24 14.71 ?  41  VAL   A HG23 1 
ATOM   990  N N    A TYR   A 1 42  ? 31.643 3.443   -4.580  0.76 12.16 ?  42  TYR   A N    1 
ATOM   991  N N    B TYR   A 1 42  ? 31.420 3.494   -4.668  0.24 11.83 ?  42  TYR   A N    1 
ATOM   992  C CA   A TYR   A 1 42  ? 32.355 4.647   -4.170  0.76 11.96 ?  42  TYR   A CA   1 
ATOM   993  C CA   B TYR   A 1 42  ? 32.242 4.626   -4.239  0.24 12.23 ?  42  TYR   A CA   1 
ATOM   994  C C    A TYR   A 1 42  ? 32.095 5.004   -2.718  0.76 11.90 ?  42  TYR   A C    1 
ATOM   995  C C    B TYR   A 1 42  ? 32.001 5.034   -2.790  0.24 11.80 ?  42  TYR   A C    1 
ATOM   996  O O    A TYR   A 1 42  ? 32.675 5.977   -2.215  0.76 12.42 ?  42  TYR   A O    1 
ATOM   997  O O    B TYR   A 1 42  ? 32.522 6.067   -2.353  0.24 11.81 ?  42  TYR   A O    1 
ATOM   998  C CB   A TYR   A 1 42  ? 31.974 5.827   -5.087  0.76 13.01 ?  42  TYR   A CB   1 
ATOM   999  C CB   B TYR   A 1 42  ? 32.014 5.837   -5.147  0.24 13.22 ?  42  TYR   A CB   1 
ATOM   1000 C CG   A TYR   A 1 42  ? 32.165 5.510   -6.559  0.76 13.91 ?  42  TYR   A CG   1 
ATOM   1001 C CG   B TYR   A 1 42  ? 32.209 5.547   -6.613  0.24 14.03 ?  42  TYR   A CG   1 
ATOM   1002 C CD1  A TYR   A 1 42  ? 33.433 5.324   -7.090  0.76 14.90 ?  42  TYR   A CD1  1 
ATOM   1003 C CD1  B TYR   A 1 42  ? 33.476 5.334   -7.137  0.24 14.60 ?  42  TYR   A CD1  1 
ATOM   1004 C CD2  A TYR   A 1 42  ? 31.076 5.369   -7.412  0.76 15.52 ?  42  TYR   A CD2  1 
ATOM   1005 C CD2  B TYR   A 1 42  ? 31.125 5.485   -7.473  0.24 14.74 ?  42  TYR   A CD2  1 
ATOM   1006 C CE1  A TYR   A 1 42  ? 33.613 5.011   -8.431  0.76 15.49 ?  42  TYR   A CE1  1 
ATOM   1007 C CE1  B TYR   A 1 42  ? 33.653 5.063   -8.481  0.24 15.04 ?  42  TYR   A CE1  1 
ATOM   1008 C CE2  A TYR   A 1 42  ? 31.251 5.066   -8.758  0.76 16.57 ?  42  TYR   A CE2  1 
ATOM   1009 C CE2  B TYR   A 1 42  ? 31.292 5.219   -8.814  0.24 15.29 ?  42  TYR   A CE2  1 
ATOM   1010 C CZ   A TYR   A 1 42  ? 32.521 4.886   -9.259  0.76 16.45 ?  42  TYR   A CZ   1 
ATOM   1011 C CZ   B TYR   A 1 42  ? 32.557 5.008   -9.315  0.24 15.53 ?  42  TYR   A CZ   1 
ATOM   1012 O OH   A TYR   A 1 42  ? 32.703 4.580   -10.589 0.76 18.24 ?  42  TYR   A OH   1 
ATOM   1013 O OH   B TYR   A 1 42  ? 32.721 4.741   -10.654 0.24 16.34 ?  42  TYR   A OH   1 
ATOM   1014 H H    A TYR   A 1 42  ? 30.857 3.602   -4.889  0.76 14.60 ?  42  TYR   A H    1 
ATOM   1015 H H    B TYR   A 1 42  ? 30.629 3.714   -4.938  0.24 14.20 ?  42  TYR   A H    1 
ATOM   1016 H HA   A TYR   A 1 42  ? 33.307 4.499   -4.270  0.76 14.35 ?  42  TYR   A HA   1 
ATOM   1017 H HA   B TYR   A 1 42  ? 33.173 4.370   -4.326  0.24 14.68 ?  42  TYR   A HA   1 
ATOM   1018 H HB2  A TYR   A 1 42  ? 31.039 6.052   -4.948  0.76 15.62 ?  42  TYR   A HB2  1 
ATOM   1019 H HB2  B TYR   A 1 42  ? 31.106 6.153   -5.024  0.24 15.86 ?  42  TYR   A HB2  1 
ATOM   1020 H HB3  A TYR   A 1 42  ? 32.532 6.593   -4.872  0.76 15.62 ?  42  TYR   A HB3  1 
ATOM   1021 H HB3  B TYR   A 1 42  ? 32.641 6.535   -4.894  0.24 15.86 ?  42  TYR   A HB3  1 
ATOM   1022 H HD1  A TYR   A 1 42  ? 34.175 5.402   -6.536  0.76 17.88 ?  42  TYR   A HD1  1 
ATOM   1023 H HD1  B TYR   A 1 42  ? 34.217 5.370   -6.574  0.24 17.52 ?  42  TYR   A HD1  1 
ATOM   1024 H HD2  A TYR   A 1 42  ? 30.216 5.494   -7.080  0.76 18.62 ?  42  TYR   A HD2  1 
ATOM   1025 H HD2  B TYR   A 1 42  ? 30.269 5.627   -7.136  0.24 17.69 ?  42  TYR   A HD2  1 
ATOM   1026 H HE1  A TYR   A 1 42  ? 34.470 4.893   -8.770  0.76 18.58 ?  42  TYR   A HE1  1 
ATOM   1027 H HE1  B TYR   A 1 42  ? 34.508 4.923   -8.820  0.24 18.05 ?  42  TYR   A HE1  1 
ATOM   1028 H HE2  A TYR   A 1 42  ? 30.512 4.985   -9.320  0.76 19.89 ?  42  TYR   A HE2  1 
ATOM   1029 H HE2  B TYR   A 1 42  ? 30.554 5.182   -9.378  0.24 18.35 ?  42  TYR   A HE2  1 
ATOM   1030 H HH   A TYR   A 1 42  ? 33.526 4.500   -10.755 0.76 21.89 ?  42  TYR   A HH   1 
ATOM   1031 H HH   B TYR   A 1 42  ? 33.536 4.629   -10.824 0.24 19.61 ?  42  TYR   A HH   1 
ATOM   1032 N N    . LEU   A 1 43  ? 31.227 4.250   -2.044  1.00 11.34 ?  43  LEU   A N    1 
ATOM   1033 C CA   . LEU   A 1 43  ? 30.793 4.588   -0.691  1.00 10.94 ?  43  LEU   A CA   1 
ATOM   1034 C C    . LEU   A 1 43  ? 30.293 6.030   -0.586  1.00 11.24 ?  43  LEU   A C    1 
ATOM   1035 O O    . LEU   A 1 43  ? 30.560 6.734   0.390   1.00 12.60 ?  43  LEU   A O    1 
ATOM   1036 C CB   . LEU   A 1 43  ? 31.849 4.274   0.367   1.00 11.57 ?  43  LEU   A CB   1 
ATOM   1037 C CG   . LEU   A 1 43  ? 32.335 2.822   0.452   1.00 11.90 ?  43  LEU   A CG   1 
ATOM   1038 C CD1  . LEU   A 1 43  ? 33.381 2.717   1.548   1.00 12.88 ?  43  LEU   A CD1  1 
ATOM   1039 C CD2  . LEU   A 1 43  ? 31.194 1.839   0.700   1.00 12.40 ?  43  LEU   A CD2  1 
ATOM   1040 H H    A LEU   A 1 43  ? 30.877 3.523   -2.348  0.76 13.61 ?  43  LEU   A H    1 
ATOM   1041 H H    B LEU   A 1 43  ? 30.926 3.487   -2.310  0.24 13.61 ?  43  LEU   A H    1 
ATOM   1042 H HA   . LEU   A 1 43  ? 30.030 4.021   -0.486  1.00 13.13 ?  43  LEU   A HA   1 
ATOM   1043 H HB2  . LEU   A 1 43  ? 32.625 4.827   0.200   1.00 13.88 ?  43  LEU   A HB2  1 
ATOM   1044 H HB3  . LEU   A 1 43  ? 31.479 4.496   1.239   1.00 13.88 ?  43  LEU   A HB3  1 
ATOM   1045 H HG   . LEU   A 1 43  ? 32.762 2.583   -0.386  1.00 14.28 ?  43  LEU   A HG   1 
ATOM   1046 H HD11 . LEU   A 1 43  ? 33.691 1.797   1.601   1.00 15.45 ?  43  LEU   A HD11 1 
ATOM   1047 H HD12 . LEU   A 1 43  ? 34.122 3.304   1.337   1.00 15.45 ?  43  LEU   A HD12 1 
ATOM   1048 H HD13 . LEU   A 1 43  ? 32.980 2.978   2.392   1.00 15.45 ?  43  LEU   A HD13 1 
ATOM   1049 H HD21 . LEU   A 1 43  ? 31.569 0.955   0.836   1.00 14.88 ?  43  LEU   A HD21 1 
ATOM   1050 H HD22 . LEU   A 1 43  ? 30.708 2.120   1.489   1.00 14.88 ?  43  LEU   A HD22 1 
ATOM   1051 H HD23 . LEU   A 1 43  ? 30.612 1.839   -0.072  1.00 14.88 ?  43  LEU   A HD23 1 
ATOM   1052 N N    A LYS   A 1 44  ? 29.579 6.480   -1.617  0.76 11.14 ?  44  LYS   A N    1 
ATOM   1053 N N    B LYS   A 1 44  ? 29.522 6.454   -1.588  0.24 12.23 ?  44  LYS   A N    1 
ATOM   1054 C CA   A LYS   A 1 44  ? 28.952 7.799   -1.618  0.76 11.18 ?  44  LYS   A CA   1 
ATOM   1055 C CA   B LYS   A 1 44  ? 28.840 7.748   -1.575  0.24 13.29 ?  44  LYS   A CA   1 
ATOM   1056 C C    A LYS   A 1 44  ? 27.524 7.612   -1.121  0.76 10.81 ?  44  LYS   A C    1 
ATOM   1057 C C    B LYS   A 1 44  ? 27.430 7.508   -1.049  0.24 12.50 ?  44  LYS   A C    1 
ATOM   1058 O O    A LYS   A 1 44  ? 26.658 7.097   -1.837  0.76 12.25 ?  44  LYS   A O    1 
ATOM   1059 O O    B LYS   A 1 44  ? 26.564 6.996   -1.763  0.24 12.36 ?  44  LYS   A O    1 
ATOM   1060 C CB   A LYS   A 1 44  ? 29.003 8.417   -3.009  0.76 13.99 ?  44  LYS   A CB   1 
ATOM   1061 C CB   B LYS   A 1 44  ? 28.810 8.356   -2.974  0.24 15.13 ?  44  LYS   A CB   1 
ATOM   1062 C CG   A LYS   A 1 44  ? 30.379 8.911   -3.418  0.76 17.58 ?  44  LYS   A CG   1 
ATOM   1063 C CG   B LYS   A 1 44  ? 30.167 8.768   -3.519  0.24 17.17 ?  44  LYS   A CG   1 
ATOM   1064 C CD   A LYS   A 1 44  ? 31.022 9.793   -2.355  0.76 22.96 ?  44  LYS   A CD   1 
ATOM   1065 C CD   B LYS   A 1 44  ? 30.900 9.710   -2.578  0.24 19.54 ?  44  LYS   A CD   1 
ATOM   1066 C CE   A LYS   A 1 44  ? 32.352 10.338  -2.834  0.76 25.78 ?  44  LYS   A CE   1 
ATOM   1067 C CE   B LYS   A 1 44  ? 31.750 10.704  -3.357  0.24 20.94 ?  44  LYS   A CE   1 
ATOM   1068 N NZ   A LYS   A 1 44  ? 33.150 10.932  -1.728  0.76 27.46 ?  44  LYS   A NZ   1 
ATOM   1069 N NZ   B LYS   A 1 44  ? 33.077 10.941  -2.729  0.24 21.80 ?  44  LYS   A NZ   1 
ATOM   1070 H H    A LYS   A 1 44  ? 29.441 6.028   -2.337  0.76 13.37 ?  44  LYS   A H    1 
ATOM   1071 H H    B LYS   A 1 44  ? 29.365 5.996   -2.298  0.24 14.68 ?  44  LYS   A H    1 
ATOM   1072 H HA   A LYS   A 1 44  ? 29.408 8.371   -0.983  0.76 13.42 ?  44  LYS   A HA   1 
ATOM   1073 H HA   B LYS   A 1 44  ? 29.293 8.357   -0.974  0.24 15.95 ?  44  LYS   A HA   1 
ATOM   1074 H HB2  A LYS   A 1 44  ? 28.722 7.754   -3.658  0.76 16.79 ?  44  LYS   A HB2  1 
ATOM   1075 H HB2  B LYS   A 1 44  ? 28.436 7.707   -3.589  0.24 18.15 ?  44  LYS   A HB2  1 
ATOM   1076 H HB3  A LYS   A 1 44  ? 28.399 9.177   -3.033  0.76 16.79 ?  44  LYS   A HB3  1 
ATOM   1077 H HB3  B LYS   A 1 44  ? 28.252 9.150   -2.959  0.24 18.15 ?  44  LYS   A HB3  1 
ATOM   1078 H HG2  A LYS   A 1 44  ? 30.959 8.149   -3.570  0.76 21.10 ?  44  LYS   A HG2  1 
ATOM   1079 H HG2  B LYS   A 1 44  ? 30.716 7.978   -3.643  0.24 20.61 ?  44  LYS   A HG2  1 
ATOM   1080 H HG3  A LYS   A 1 44  ? 30.300 9.436   -4.234  0.76 21.10 ?  44  LYS   A HG3  1 
ATOM   1081 H HG3  B LYS   A 1 44  ? 30.043 9.223   -4.368  0.24 20.61 ?  44  LYS   A HG3  1 
ATOM   1082 H HD2  A LYS   A 1 44  ? 30.426 10.532  -2.151  0.76 27.55 ?  44  LYS   A HD2  1 
ATOM   1083 H HD2  B LYS   A 1 44  ? 30.252 10.204  -2.049  0.24 23.45 ?  44  LYS   A HD2  1 
ATOM   1084 H HD3  A LYS   A 1 44  ? 31.190 9.264   -1.558  0.76 27.55 ?  44  LYS   A HD3  1 
ATOM   1085 H HD3  B LYS   A 1 44  ? 31.484 9.194   -1.996  0.24 23.45 ?  44  LYS   A HD3  1 
ATOM   1086 H HE2  A LYS   A 1 44  ? 32.868 9.614   -3.223  0.76 30.94 ?  44  LYS   A HE2  1 
ATOM   1087 H HE2  B LYS   A 1 44  ? 31.899 10.360  -4.251  0.24 25.13 ?  44  LYS   A HE2  1 
ATOM   1088 H HE3  A LYS   A 1 44  ? 32.190 11.026  -3.496  0.76 30.94 ?  44  LYS   A HE3  1 
ATOM   1089 H HE3  B LYS   A 1 44  ? 31.279 11.551  -3.400  0.24 25.13 ?  44  LYS   A HE3  1 
ATOM   1090 H HZ1  A LYS   A 1 44  ? 33.921 11.242  -2.044  0.76 32.95 ?  44  LYS   A HZ1  1 
ATOM   1091 H HZ1  B LYS   A 1 44  ? 33.541 11.526  -3.215  0.24 26.17 ?  44  LYS   A HZ1  1 
ATOM   1092 H HZ2  A LYS   A 1 44  ? 32.699 11.605  -1.356  0.76 32.95 ?  44  LYS   A HZ2  1 
ATOM   1093 H HZ2  B LYS   A 1 44  ? 32.972 11.266  -1.908  0.24 26.17 ?  44  LYS   A HZ2  1 
ATOM   1094 H HZ3  A LYS   A 1 44  ? 33.316 10.318  -1.107  0.76 32.95 ?  44  LYS   A HZ3  1 
ATOM   1095 H HZ3  B LYS   A 1 44  ? 33.533 10.178  -2.684  0.24 26.17 ?  44  LYS   A HZ3  1 
ATOM   1096 N N    A HIS   A 1 45  ? 27.282 8.011   0.124   0.76 10.72 ?  45  HIS   A N    1 
ATOM   1097 N N    B HIS   A 1 45  ? 27.197 7.872   0.212   0.24 12.20 ?  45  HIS   A N    1 
ATOM   1098 C CA   A HIS   A 1 45  ? 26.054 7.643   0.826   0.76 11.06 ?  45  HIS   A CA   1 
ATOM   1099 C CA   B HIS   A 1 45  ? 25.919 7.605   0.872   0.24 12.19 ?  45  HIS   A CA   1 
ATOM   1100 C C    A HIS   A 1 45  ? 24.991 8.732   0.662   0.76 12.22 ?  45  HIS   A C    1 
ATOM   1101 C C    B HIS   A 1 45  ? 25.029 8.833   0.704   0.24 12.52 ?  45  HIS   A C    1 
ATOM   1102 O O    A HIS   A 1 45  ? 24.663 9.473   1.588   0.76 13.80 ?  45  HIS   A O    1 
ATOM   1103 O O    B HIS   A 1 45  ? 24.855 9.651   1.609   0.24 13.15 ?  45  HIS   A O    1 
ATOM   1104 C CB   A HIS   A 1 45  ? 26.364 7.395   2.290   0.76 10.61 ?  45  HIS   A CB   1 
ATOM   1105 C CB   B HIS   A 1 45  ? 26.145 7.269   2.339   0.24 12.08 ?  45  HIS   A CB   1 
ATOM   1106 C CG   A HIS   A 1 45  ? 27.475 6.418   2.514   0.76 10.43 ?  45  HIS   A CG   1 
ATOM   1107 C CG   B HIS   A 1 45  ? 27.324 6.378   2.575   0.24 11.45 ?  45  HIS   A CG   1 
ATOM   1108 N ND1  A HIS   A 1 45  ? 27.451 5.125   2.026   0.76 11.23 ?  45  HIS   A ND1  1 
ATOM   1109 N ND1  B HIS   A 1 45  ? 27.406 5.098   2.069   0.24 11.51 ?  45  HIS   A ND1  1 
ATOM   1110 C CD2  A HIS   A 1 45  ? 28.651 6.558   3.175   0.76 10.99 ?  45  HIS   A CD2  1 
ATOM   1111 C CD2  B HIS   A 1 45  ? 28.471 6.589   3.262   0.24 11.25 ?  45  HIS   A CD2  1 
ATOM   1112 C CE1  A HIS   A 1 45  ? 28.565 4.512   2.391   0.76 10.97 ?  45  HIS   A CE1  1 
ATOM   1113 C CE1  B HIS   A 1 45  ? 28.555 4.559   2.438   0.24 11.30 ?  45  HIS   A CE1  1 
ATOM   1114 N NE2  A HIS   A 1 45  ? 29.306 5.355   3.090   0.76 11.26 ?  45  HIS   A NE2  1 
ATOM   1115 N NE2  B HIS   A 1 45  ? 29.218 5.442   3.163   0.24 11.18 ?  45  HIS   A NE2  1 
ATOM   1116 H H    A HIS   A 1 45  ? 27.821 8.501   0.590   0.76 12.86 ?  45  HIS   A H    1 
ATOM   1117 H H    B HIS   A 1 45  ? 27.764 8.285   0.708   0.24 14.65 ?  45  HIS   A H    1 
ATOM   1118 H HA   A HIS   A 1 45  ? 25.706 6.826   0.446   0.76 13.28 ?  45  HIS   A HA   1 
ATOM   1119 H HA   B HIS   A 1 45  ? 25.493 6.842   0.450   0.24 14.63 ?  45  HIS   A HA   1 
ATOM   1120 H HB2  A HIS   A 1 45  ? 26.616 8.237   2.705   0.76 12.73 ?  45  HIS   A HB2  1 
ATOM   1121 H HB2  B HIS   A 1 45  ? 26.293 8.092   2.830   0.24 14.50 ?  45  HIS   A HB2  1 
ATOM   1122 H HB3  A HIS   A 1 45  ? 25.571 7.043   2.721   0.76 12.73 ?  45  HIS   A HB3  1 
ATOM   1123 H HB3  B HIS   A 1 45  ? 25.361 6.817   2.684   0.24 14.50 ?  45  HIS   A HB3  1 
ATOM   1124 H HD2  A HIS   A 1 45  ? 28.958 7.327   3.612   0.76 13.19 ?  45  HIS   A HD2  1 
ATOM   1125 H HD2  B HIS   A 1 45  ? 28.709 7.368   3.717   0.24 13.50 ?  45  HIS   A HD2  1 
ATOM   1126 H HE1  A HIS   A 1 45  ? 28.784 3.632   2.201   0.76 13.16 ?  45  HIS   A HE1  1 
ATOM   1127 H HE1  B HIS   A 1 45  ? 28.843 3.703   2.226   0.24 13.55 ?  45  HIS   A HE1  1 
ATOM   1128 H HE2  A HIS   A 1 45  ? 30.078 5.183   3.430   0.76 13.51 ?  45  HIS   A HE2  1 
ATOM   1129 H HE2  B HIS   A 1 45  ? 29.993 5.319   3.514   0.24 13.41 ?  45  HIS   A HE2  1 
ATOM   1130 N N    A GLY   A 1 46  ? 24.416 8.789   -0.534  0.76 12.97 ?  46  GLY   A N    1 
ATOM   1131 N N    B GLY   A 1 46  ? 24.462 8.961   -0.492  0.24 12.45 ?  46  GLY   A N    1 
ATOM   1132 C CA   A GLY   A 1 46  ? 23.579 9.918   -0.893  0.76 14.03 ?  46  GLY   A CA   1 
ATOM   1133 C CA   B GLY   A 1 46  ? 23.666 10.128  -0.820  0.24 12.33 ?  46  GLY   A CA   1 
ATOM   1134 C C    A GLY   A 1 46  ? 22.100 9.772   -0.601  0.76 14.15 ?  46  GLY   A C    1 
ATOM   1135 C C    B GLY   A 1 46  ? 22.188 10.015  -0.503  0.24 11.60 ?  46  GLY   A C    1 
ATOM   1136 O O    A GLY   A 1 46  ? 21.445 10.746  -0.217  0.76 15.75 ?  46  GLY   A O    1 
ATOM   1137 O O    B GLY   A 1 46  ? 21.536 11.027  -0.224  0.24 12.22 ?  46  GLY   A O    1 
ATOM   1138 H H    A GLY   A 1 46  ? 24.479 8.188   -1.144  0.76 15.56 ?  46  GLY   A H    1 
ATOM   1139 H H    B GLY   A 1 46  ? 24.541 8.392   -1.133  0.24 14.94 ?  46  GLY   A H    1 
ATOM   1140 H HA2  A GLY   A 1 46  ? 23.883 10.704  -0.411  0.76 16.84 ?  46  GLY   A HA2  1 
ATOM   1141 H HA2  B GLY   A 1 46  ? 24.020 10.890  -0.337  0.24 14.80 ?  46  GLY   A HA2  1 
ATOM   1142 H HA3  A GLY   A 1 46  ? 23.675 10.095  -1.840  0.76 16.84 ?  46  GLY   A HA3  1 
ATOM   1143 H HA3  B GLY   A 1 46  ? 23.749 10.305  -1.767  0.24 14.80 ?  46  GLY   A HA3  1 
ATOM   1144 N N    A GLY   A 1 47  ? 21.556 8.574   -0.792  0.76 13.76 ?  47  GLY   A N    1 
ATOM   1145 N N    B GLY   A 1 47  ? 21.642 8.806   -0.562  0.24 11.39 ?  47  GLY   A N    1 
ATOM   1146 C CA   A GLY   A 1 47  ? 20.124 8.374   -0.722  0.76 14.03 ?  47  GLY   A CA   1 
ATOM   1147 C CA   B GLY   A 1 47  ? 20.227 8.607   -0.346  0.24 12.14 ?  47  GLY   A CA   1 
ATOM   1148 C C    A GLY   A 1 47  ? 19.782 6.958   -0.308  0.76 13.48 ?  47  GLY   A C    1 
ATOM   1149 C C    B GLY   A 1 47  ? 19.915 7.151   -0.070  0.24 12.37 ?  47  GLY   A C    1 
ATOM   1150 O O    A GLY   A 1 47  ? 20.660 6.121   -0.084  0.76 13.48 ?  47  GLY   A O    1 
ATOM   1151 O O    B GLY   A 1 47  ? 20.814 6.325   0.108   0.24 12.58 ?  47  GLY   A O    1 
ATOM   1152 H H    A GLY   A 1 47  ? 22.000 7.853   -0.954  0.76 16.52 ?  47  GLY   A H    1 
ATOM   1153 H H    B GLY   A 1 47  ? 22.076 8.082   -0.725  0.24 13.67 ?  47  GLY   A H    1 
ATOM   1154 H HA2  A GLY   A 1 47  ? 19.735 8.989   -0.080  0.76 16.83 ?  47  GLY   A HA2  1 
ATOM   1155 H HA2  B GLY   A 1 47  ? 19.925 9.145   0.404   0.24 14.56 ?  47  GLY   A HA2  1 
ATOM   1156 H HA3  A GLY   A 1 47  ? 19.724 8.543   -1.592  0.76 16.83 ?  47  GLY   A HA3  1 
ATOM   1157 H HA3  B GLY   A 1 47  ? 19.735 8.878   -1.137  0.24 14.56 ?  47  GLY   A HA3  1 
ATOM   1158 N N    A GLY   A 1 48  ? 18.483 6.689   -0.218  0.76 14.14 ?  48  GLY   A N    1 
ATOM   1159 N N    B GLY   A 1 48  ? 18.618 6.843   -0.033  0.24 12.92 ?  48  GLY   A N    1 
ATOM   1160 C CA   A GLY   A 1 48  ? 18.039 5.390   0.234   0.76 14.08 ?  48  GLY   A CA   1 
ATOM   1161 C CA   B GLY   A 1 48  ? 18.194 5.481   0.244   0.24 12.64 ?  48  GLY   A CA   1 
ATOM   1162 C C    A GLY   A 1 48  ? 18.581 5.074   1.615   0.76 13.08 ?  48  GLY   A C    1 
ATOM   1163 C C    B GLY   A 1 48  ? 18.543 5.076   1.666   0.24 12.06 ?  48  GLY   A C    1 
ATOM   1164 O O    A GLY   A 1 48  ? 18.796 5.960   2.453   0.76 13.64 ?  48  GLY   A O    1 
ATOM   1165 O O    B GLY   A 1 48  ? 18.561 5.897   2.589   0.24 11.46 ?  48  GLY   A O    1 
ATOM   1166 H H    A GLY   A 1 48  ? 17.849 7.243   -0.399  0.76 16.96 ?  48  GLY   A H    1 
ATOM   1167 H H    B GLY   A 1 48  ? 17.975 7.402   -0.150  0.24 15.50 ?  48  GLY   A H    1 
ATOM   1168 H HA2  A GLY   A 1 48  ? 17.071 5.362   0.266   0.76 16.90 ?  48  GLY   A HA2  1 
ATOM   1169 H HA2  B GLY   A 1 48  ? 17.235 5.402   0.120   0.24 15.17 ?  48  GLY   A HA2  1 
ATOM   1170 H HA3  A GLY   A 1 48  ? 18.353 4.707   -0.376  0.76 16.90 ?  48  GLY   A HA3  1 
ATOM   1171 H HA3  B GLY   A 1 48  ? 18.638 4.870   -0.362  0.24 15.17 ?  48  GLY   A HA3  1 
ATOM   1172 N N    . VAL   A 1 49  ? 18.826 3.782   1.848   1.00 12.28 ?  49  VAL   A N    1 
ATOM   1173 C CA   . VAL   A 1 49  ? 19.349 3.330   3.134   1.00 12.09 ?  49  VAL   A CA   1 
ATOM   1174 C C    . VAL   A 1 49  ? 20.663 4.034   3.464   1.00 11.14 ?  49  VAL   A C    1 
ATOM   1175 O O    . VAL   A 1 49  ? 20.886 4.449   4.605   1.00 11.65 ?  49  VAL   A O    1 
ATOM   1176 C CB   . VAL   A 1 49  ? 19.515 1.797   3.129   1.00 12.68 ?  49  VAL   A CB   1 
ATOM   1177 C CG1  . VAL   A 1 49  ? 20.332 1.335   4.332   1.00 13.38 ?  49  VAL   A CG1  1 
ATOM   1178 C CG2  . VAL   A 1 49  ? 18.155 1.105   3.107   1.00 15.26 ?  49  VAL   A CG2  1 
ATOM   1179 H H    A VAL   A 1 49  ? 18.697 3.149   1.280   0.76 14.73 ?  49  VAL   A H    1 
ATOM   1180 H H    B VAL   A 1 49  ? 18.731 3.161   1.261   0.24 14.73 ?  49  VAL   A H    1 
ATOM   1181 H HA   . VAL   A 1 49  ? 18.708 3.553   3.830   1.00 14.51 ?  49  VAL   A HA   1 
ATOM   1182 H HB   . VAL   A 1 49  ? 19.995 1.535   2.328   1.00 15.22 ?  49  VAL   A HB   1 
ATOM   1183 H HG11 . VAL   A 1 49  ? 20.181 0.387   4.464   1.00 16.06 ?  49  VAL   A HG11 1 
ATOM   1184 H HG12 . VAL   A 1 49  ? 21.268 1.505   4.165   1.00 16.06 ?  49  VAL   A HG12 1 
ATOM   1185 H HG13 . VAL   A 1 49  ? 20.035 1.827   5.116   1.00 16.06 ?  49  VAL   A HG13 1 
ATOM   1186 H HG21 . VAL   A 1 49  ? 18.289 0.145   3.095   1.00 18.31 ?  49  VAL   A HG21 1 
ATOM   1187 H HG22 . VAL   A 1 49  ? 17.659 1.361   3.902   1.00 18.31 ?  49  VAL   A HG22 1 
ATOM   1188 H HG23 . VAL   A 1 49  ? 17.673 1.384   2.313   1.00 18.31 ?  49  VAL   A HG23 1 
ATOM   1189 N N    . ALA   A 1 50  ? 21.568 4.135   2.486   1.00 10.76 ?  50  ALA   A N    1 
ATOM   1190 C CA   . ALA   A 1 50  ? 22.890 4.696   2.760   1.00 10.79 ?  50  ALA   A CA   1 
ATOM   1191 C C    . ALA   A 1 50  ? 22.793 6.155   3.190   1.00 10.51 ?  50  ALA   A C    1 
ATOM   1192 O O    . ALA   A 1 50  ? 23.427 6.575   4.165   1.00 11.08 ?  50  ALA   A O    1 
ATOM   1193 C CB   . ALA   A 1 50  ? 23.759 4.573   1.517   1.00 10.79 ?  50  ALA   A CB   1 
ATOM   1194 H H    . ALA   A 1 50  ? 21.440 3.895   1.667   1.00 12.91 ?  50  ALA   A H    1 
ATOM   1195 H HA   . ALA   A 1 50  ? 23.304 4.200   3.480   1.00 12.95 ?  50  ALA   A HA   1 
ATOM   1196 H HB1  . ALA   A 1 50  ? 24.642 4.916   1.714   1.00 12.95 ?  50  ALA   A HB1  1 
ATOM   1197 H HB2  . ALA   A 1 50  ? 23.814 3.637   1.266   1.00 12.95 ?  50  ALA   A HB2  1 
ATOM   1198 H HB3  . ALA   A 1 50  ? 23.354 5.083   0.797   1.00 12.95 ?  50  ALA   A HB3  1 
ATOM   1199 N N    . GLY   A 1 51  ? 21.996 6.945   2.470   1.00 10.93 ?  51  GLY   A N    1 
ATOM   1200 C CA   . GLY   A 1 51  ? 21.837 8.338   2.848   1.00 11.46 ?  51  GLY   A CA   1 
ATOM   1201 C C    . GLY   A 1 51  ? 21.242 8.482   4.232   1.00 11.51 ?  51  GLY   A C    1 
ATOM   1202 O O    . GLY   A 1 51  ? 21.635 9.365   5.000   1.00 12.21 ?  51  GLY   A O    1 
ATOM   1203 H H    . GLY   A 1 51  ? 21.558 6.701   1.769   1.00 13.12 ?  51  GLY   A H    1 
ATOM   1204 H HA2  . GLY   A 1 51  ? 22.700 8.779   2.836   1.00 13.75 ?  51  GLY   A HA2  1 
ATOM   1205 H HA3  . GLY   A 1 51  ? 21.254 8.783   2.212   1.00 13.75 ?  51  GLY   A HA3  1 
ATOM   1206 N N    . ALA   A 1 52  ? 20.281 7.616   4.567   1.00 11.68 ?  52  ALA   A N    1 
ATOM   1207 C CA   . ALA   A 1 52  ? 19.645 7.669   5.878   1.00 12.03 ?  52  ALA   A CA   1 
ATOM   1208 C C    . ALA   A 1 52  ? 20.607 7.260   6.991   1.00 11.64 ?  52  ALA   A C    1 
ATOM   1209 O O    . ALA   A 1 52  ? 20.684 7.921   8.033   1.00 13.03 ?  52  ALA   A O    1 
ATOM   1210 C CB   . ALA   A 1 52  ? 18.394 6.785   5.874   1.00 13.96 ?  52  ALA   A CB   1 
ATOM   1211 H H    . ALA   A 1 52  ? 19.996 6.978   4.055   1.00 14.01 ?  52  ALA   A H    1 
ATOM   1212 H HA   . ALA   A 1 52  ? 19.365 8.575   6.046   1.00 14.44 ?  52  ALA   A HA   1 
ATOM   1213 H HB1  . ALA   A 1 52  ? 17.965 6.841   6.744   1.00 16.75 ?  52  ALA   A HB1  1 
ATOM   1214 H HB2  . ALA   A 1 52  ? 17.783 7.104   5.188   1.00 16.75 ?  52  ALA   A HB2  1 
ATOM   1215 H HB3  . ALA   A 1 52  ? 18.646 5.868   5.688   1.00 16.75 ?  52  ALA   A HB3  1 
ATOM   1216 N N    A LEU   A 1 53  ? 21.332 6.156   6.806   0.76 11.44 ?  53  LEU   A N    1 
ATOM   1217 N N    B LEU   A 1 53  ? 21.344 6.161   6.788   0.24 11.32 ?  53  LEU   A N    1 
ATOM   1218 C CA   A LEU   A 1 53  ? 22.306 5.757   7.820   0.76 11.52 ?  53  LEU   A CA   1 
ATOM   1219 C CA   B LEU   A 1 53  ? 22.314 5.720   7.789   0.24 11.10 ?  53  LEU   A CA   1 
ATOM   1220 C C    A LEU   A 1 53  ? 23.347 6.849   8.013   0.76 11.03 ?  53  LEU   A C    1 
ATOM   1221 C C    B LEU   A 1 53  ? 23.397 6.770   7.999   0.24 10.99 ?  53  LEU   A C    1 
ATOM   1222 O O    A LEU   A 1 53  ? 23.661 7.234   9.143   0.76 12.05 ?  53  LEU   A O    1 
ATOM   1223 O O    B LEU   A 1 53  ? 23.806 7.033   9.135   0.24 11.35 ?  53  LEU   A O    1 
ATOM   1224 C CB   A LEU   A 1 53  ? 22.986 4.433   7.443   0.76 12.23 ?  53  LEU   A CB   1 
ATOM   1225 C CB   B LEU   A 1 53  ? 22.954 4.392   7.364   0.24 11.12 ?  53  LEU   A CB   1 
ATOM   1226 C CG   A LEU   A 1 53  ? 22.111 3.171   7.463   0.76 13.54 ?  53  LEU   A CG   1 
ATOM   1227 C CG   B LEU   A 1 53  ? 22.184 3.078   7.547   0.24 10.86 ?  53  LEU   A CG   1 
ATOM   1228 C CD1  A LEU   A 1 53  ? 22.886 1.975   6.921   0.76 14.27 ?  53  LEU   A CD1  1 
ATOM   1229 C CD1  B LEU   A 1 53  ? 22.865 1.969   6.757   0.24 11.34 ?  53  LEU   A CD1  1 
ATOM   1230 C CD2  A LEU   A 1 53  ? 21.591 2.879   8.860   0.76 14.58 ?  53  LEU   A CD2  1 
ATOM   1231 C CD2  B LEU   A 1 53  ? 22.091 2.687   9.011   0.24 10.58 ?  53  LEU   A CD2  1 
ATOM   1232 H H    A LEU   A 1 53  ? 21.278 5.628   6.123   0.76 13.73 ?  53  LEU   A H    1 
ATOM   1233 H H    B LEU   A 1 53  ? 21.304 5.660   6.088   0.24 13.58 ?  53  LEU   A H    1 
ATOM   1234 H HA   A LEU   A 1 53  ? 21.848 5.624   8.663   0.76 13.83 ?  53  LEU   A HA   1 
ATOM   1235 H HA   B LEU   A 1 53  ? 21.860 5.578   8.634   0.24 13.32 ?  53  LEU   A HA   1 
ATOM   1236 H HB2  A LEU   A 1 53  ? 23.343 4.519   6.543   0.76 14.67 ?  53  LEU   A HB2  1 
ATOM   1237 H HB2  B LEU   A 1 53  ? 23.162 4.456   6.419   0.24 13.34 ?  53  LEU   A HB2  1 
ATOM   1238 H HB3  A LEU   A 1 53  ? 23.719 4.280   8.061   0.76 14.67 ?  53  LEU   A HB3  1 
ATOM   1239 H HB3  B LEU   A 1 53  ? 23.780 4.292   7.859   0.24 13.34 ?  53  LEU   A HB3  1 
ATOM   1240 H HG   A LEU   A 1 53  ? 21.348 3.312   6.881   0.76 16.25 ?  53  LEU   A HG   1 
ATOM   1241 H HG   B LEU   A 1 53  ? 21.284 3.181   7.200   0.24 13.03 ?  53  LEU   A HG   1 
ATOM   1242 H HD11 A LEU   A 1 53  ? 22.310 1.193   6.942   0.76 17.12 ?  53  LEU   A HD11 1 
ATOM   1243 H HD11 B LEU   A 1 53  ? 22.377 1.141   6.891   0.24 13.61 ?  53  LEU   A HD11 1 
ATOM   1244 H HD12 A LEU   A 1 53  ? 23.157 2.161   6.009   0.76 17.12 ?  53  LEU   A HD12 1 
ATOM   1245 H HD12 B LEU   A 1 53  ? 22.866 2.205   5.817   0.24 13.61 ?  53  LEU   A HD12 1 
ATOM   1246 H HD13 A LEU   A 1 53  ? 23.665 1.828   7.477   0.76 17.12 ?  53  LEU   A HD13 1 
ATOM   1247 H HD13 B LEU   A 1 53  ? 23.776 1.871   7.076   0.24 13.61 ?  53  LEU   A HD13 1 
ATOM   1248 H HD21 A LEU   A 1 53  ? 21.112 2.034   8.849   0.76 17.50 ?  53  LEU   A HD21 1 
ATOM   1249 H HD21 B LEU   A 1 53  ? 21.466 1.949   9.102   0.24 12.70 ?  53  LEU   A HD21 1 
ATOM   1250 H HD22 A LEU   A 1 53  ? 22.340 2.827   9.472   0.76 17.50 ?  53  LEU   A HD22 1 
ATOM   1251 H HD22 B LEU   A 1 53  ? 22.968 2.416   9.323   0.24 12.70 ?  53  LEU   A HD22 1 
ATOM   1252 H HD23 A LEU   A 1 53  ? 20.991 3.593   9.129   0.76 17.50 ?  53  LEU   A HD23 1 
ATOM   1253 H HD23 B LEU   A 1 53  ? 21.778 3.449   9.520   0.24 12.70 ?  53  LEU   A HD23 1 
ATOM   1254 N N    . ASN   A 1 54  ? 23.879 7.377   6.914   1.00 10.76 ?  54  ASN   A N    1 
ATOM   1255 C CA   . ASN   A 1 54  ? 24.936 8.371   7.043   1.00 10.77 ?  54  ASN   A CA   1 
ATOM   1256 C C    . ASN   A 1 54  ? 24.431 9.620   7.764   1.00 11.48 ?  54  ASN   A C    1 
ATOM   1257 O O    . ASN   A 1 54  ? 25.120 10.170  8.636   1.00 11.91 ?  54  ASN   A O    1 
ATOM   1258 C CB   . ASN   A 1 54  ? 25.499 8.734   5.680   1.00 11.11 ?  54  ASN   A CB   1 
ATOM   1259 C CG   . ASN   A 1 54  ? 26.508 9.838   5.785   1.00 11.37 ?  54  ASN   A CG   1 
ATOM   1260 O OD1  . ASN   A 1 54  ? 27.518 9.693   6.483   1.00 11.71 ?  54  ASN   A OD1  1 
ATOM   1261 N ND2  . ASN   A 1 54  ? 26.244 10.956  5.126   1.00 12.18 ?  54  ASN   A ND2  1 
ATOM   1262 H H    A ASN   A 1 54  ? 23.651 7.179   6.109   0.76 12.91 ?  54  ASN   A H    1 
ATOM   1263 H H    B ASN   A 1 54  ? 23.605 7.235   6.112   0.24 12.91 ?  54  ASN   A H    1 
ATOM   1264 H HA   . ASN   A 1 54  ? 25.652 7.995   7.571   1.00 12.92 ?  54  ASN   A HA   1 
ATOM   1265 H HB2  . ASN   A 1 54  ? 25.930 7.947   5.299   1.00 13.34 ?  54  ASN   A HB2  1 
ATOM   1266 H HB3  . ASN   A 1 54  ? 24.775 9.025   5.103   1.00 13.34 ?  54  ASN   A HB3  1 
ATOM   1267 H HD21 . ASN   A 1 54  ? 26.797 11.614  5.162   1.00 14.62 ?  54  ASN   A HD21 1 
ATOM   1268 H HD22 . ASN   A 1 54  ? 25.525 11.022  4.661   1.00 14.62 ?  54  ASN   A HD22 1 
ATOM   1269 N N    . LYS   A 1 55  ? 23.219 10.075  7.421   1.00 11.66 ?  55  LYS   A N    1 
ATOM   1270 C CA   . LYS   A 1 55  ? 22.630 11.227  8.094   1.00 12.46 ?  55  LYS   A CA   1 
ATOM   1271 C C    . LYS   A 1 55  ? 22.546 10.990  9.596   1.00 12.31 ?  55  LYS   A C    1 
ATOM   1272 O O    . LYS   A 1 55  ? 22.832 11.892  10.395  1.00 13.39 ?  55  LYS   A O    1 
ATOM   1273 C CB   . LYS   A 1 55  ? 21.256 11.524  7.485   1.00 13.41 ?  55  LYS   A CB   1 
ATOM   1274 C CG   . LYS   A 1 55  ? 20.518 12.698  8.101   1.00 15.06 ?  55  LYS   A CG   1 
ATOM   1275 C CD   . LYS   A 1 55  ? 19.194 12.932  7.366   1.00 16.22 ?  55  LYS   A CD   1 
ATOM   1276 C CE   . LYS   A 1 55  ? 18.351 14.030  8.010   1.00 18.25 ?  55  LYS   A CE   1 
ATOM   1277 N NZ   . LYS   A 1 55  ? 17.002 14.162  7.375   1.00 19.18 ?  55  LYS   A NZ   1 
ATOM   1278 H H    . LYS   A 1 55  ? 22.714 9.725   6.807   1.00 14.00 ?  55  LYS   A H    1 
ATOM   1279 H HA   . LYS   A 1 55  ? 23.193 11.996  7.944   1.00 14.96 ?  55  LYS   A HA   1 
ATOM   1280 H HB2  . LYS   A 1 55  ? 21.370 11.719  6.541   1.00 16.09 ?  55  LYS   A HB2  1 
ATOM   1281 H HB3  . LYS   A 1 55  ? 20.691 10.740  7.587   1.00 16.09 ?  55  LYS   A HB3  1 
ATOM   1282 H HG2  . LYS   A 1 55  ? 20.316 12.505  9.032   1.00 18.08 ?  55  LYS   A HG2  1 
ATOM   1283 H HG3  . LYS   A 1 55  ? 21.056 13.498  8.027   1.00 18.08 ?  55  LYS   A HG3  1 
ATOM   1284 H HD2  . LYS   A 1 55  ? 19.385 13.194  6.450   1.00 19.46 ?  55  LYS   A HD2  1 
ATOM   1285 H HD3  . LYS   A 1 55  ? 18.678 12.110  7.372   1.00 19.46 ?  55  LYS   A HD3  1 
ATOM   1286 H HE2  . LYS   A 1 55  ? 18.224 13.820  8.949   1.00 21.90 ?  55  LYS   A HE2  1 
ATOM   1287 H HE3  . LYS   A 1 55  ? 18.813 14.878  7.917   1.00 21.90 ?  55  LYS   A HE3  1 
ATOM   1288 H HZ1  . LYS   A 1 55  ? 16.443 14.573  7.934   1.00 23.01 ?  55  LYS   A HZ1  1 
ATOM   1289 H HZ2  . LYS   A 1 55  ? 17.060 14.639  6.626   1.00 23.01 ?  55  LYS   A HZ2  1 
ATOM   1290 H HZ3  . LYS   A 1 55  ? 16.673 13.357  7.183   1.00 23.01 ?  55  LYS   A HZ3  1 
ATOM   1291 N N    . ALA   A 1 56  ? 22.157 9.778   9.997   1.00 13.01 ?  56  ALA   A N    1 
ATOM   1292 C CA   . ALA   A 1 56  ? 22.041 9.443   11.412  1.00 13.91 ?  56  ALA   A CA   1 
ATOM   1293 C C    . ALA   A 1 56  ? 23.384 9.479   12.135  1.00 13.73 ?  56  ALA   A C    1 
ATOM   1294 O O    . ALA   A 1 56  ? 23.407 9.669   13.355  1.00 15.12 ?  56  ALA   A O    1 
ATOM   1295 C CB   . ALA   A 1 56  ? 21.372 8.072   11.576  1.00 14.81 ?  56  ALA   A CB   1 
ATOM   1296 H H    . ALA   A 1 56  ? 21.949 9.132   9.465   1.00 15.61 ?  56  ALA   A H    1 
ATOM   1297 H HA   . ALA   A 1 56  ? 21.472 10.092  11.837  1.00 16.70 ?  56  ALA   A HA   1 
ATOM   1298 H HB1  . ALA   A 1 56  ? 21.306 7.864   12.523  1.00 17.77 ?  56  ALA   A HB1  1 
ATOM   1299 H HB2  . ALA   A 1 56  ? 20.487 8.105   11.183  1.00 17.77 ?  56  ALA   A HB2  1 
ATOM   1300 H HB3  . ALA   A 1 56  ? 21.908 7.397   11.128  1.00 17.77 ?  56  ALA   A HB3  1 
ATOM   1301 N N    . THR   A 1 57  ? 24.499 9.297   11.420  1.00 12.81 ?  57  THR   A N    1 
ATOM   1302 C CA   . THR   A 1 57  ? 25.839 9.431   11.997  1.00 12.89 ?  57  THR   A CA   1 
ATOM   1303 C C    . THR   A 1 57  ? 26.385 10.852  11.920  1.00 13.31 ?  57  THR   A C    1 
ATOM   1304 O O    . THR   A 1 57  ? 27.571 11.063  12.201  1.00 13.87 ?  57  THR   A O    1 
ATOM   1305 C CB   . THR   A 1 57  ? 26.851 8.484   11.325  1.00 12.98 ?  57  THR   A CB   1 
ATOM   1306 O OG1  . THR   A 1 57  ? 27.220 8.982   10.028  1.00 12.55 ?  57  THR   A OG1  1 
ATOM   1307 C CG2  . THR   A 1 57  ? 26.315 7.058   11.224  1.00 12.79 ?  57  THR   A CG2  1 
ATOM   1308 H H    . THR   A 1 57  ? 24.505 9.076   10.586  1.00 15.37 ?  57  THR   A H    1 
ATOM   1309 H HA   . THR   A 1 57  ? 25.791 9.178   12.936  1.00 15.47 ?  57  THR   A HA   1 
ATOM   1310 H HB   . THR   A 1 57  ? 27.651 8.447   11.878  1.00 15.58 ?  57  THR   A HB   1 
ATOM   1311 H HG1  . THR   A 1 57  ? 26.536 9.035   9.542   1.00 15.05 ?  57  THR   A HG1  1 
ATOM   1312 H HG21 . THR   A 1 57  ? 26.936 6.501   10.726  1.00 15.35 ?  57  THR   A HG21 1 
ATOM   1313 H HG22 . THR   A 1 57  ? 26.201 6.679   12.111  1.00 15.35 ?  57  THR   A HG22 1 
ATOM   1314 H HG23 . THR   A 1 57  ? 25.460 7.050   10.771  1.00 15.35 ?  57  THR   A HG23 1 
ATOM   1315 N N    . ASN   A 1 58  ? 25.568 11.821  11.513  1.00 13.63 ?  58  ASN   A N    1 
ATOM   1316 C CA   . ASN   A 1 58  ? 26.026 13.202  11.412  1.00 14.74 ?  58  ASN   A CA   1 
ATOM   1317 C C    . ASN   A 1 58  ? 27.178 13.326  10.410  1.00 13.58 ?  58  ASN   A C    1 
ATOM   1318 O O    . ASN   A 1 58  ? 28.075 14.161  10.572  1.00 14.11 ?  58  ASN   A O    1 
ATOM   1319 C CB   . ASN   A 1 58  ? 26.397 13.744  12.803  1.00 17.11 ?  58  ASN   A CB   1 
ATOM   1320 C CG   . ASN   A 1 58  ? 26.786 15.209  12.796  1.00 21.17 ?  58  ASN   A CG   1 
ATOM   1321 O OD1  . ASN   A 1 58  ? 26.148 16.025  12.141  1.00 23.00 ?  58  ASN   A OD1  1 
ATOM   1322 N ND2  . ASN   A 1 58  ? 27.837 15.552  13.541  1.00 22.74 ?  58  ASN   A ND2  1 
ATOM   1323 H H    . ASN   A 1 58  ? 24.742 11.696  11.281  1.00 16.35 ?  58  ASN   A H    1 
ATOM   1324 H HA   . ASN   A 1 58  ? 25.292 13.734  11.078  1.00 17.69 ?  58  ASN   A HA   1 
ATOM   1325 H HB2  . ASN   A 1 58  ? 25.629 13.637  13.397  1.00 20.53 ?  58  ASN   A HB2  1 
ATOM   1326 H HB3  . ASN   A 1 58  ? 27.148 13.245  13.153  1.00 20.53 ?  58  ASN   A HB3  1 
ATOM   1327 H HD21 . ASN   A 1 58  ? 28.085 16.377  13.576  1.00 27.29 ?  58  ASN   A HD21 1 
ATOM   1328 H HD22 . ASN   A 1 58  ? 28.253 14.957  13.992  1.00 27.29 ?  58  ASN   A HD22 1 
ATOM   1329 N N    . ASN   A 1 59  ? 27.150 12.512  9.350   1.00 12.20 ?  59  ASN   A N    1 
ATOM   1330 C CA   . ASN   A 1 59  ? 28.129 12.486  8.259   1.00 11.77 ?  59  ASN   A CA   1 
ATOM   1331 C C    . ASN   A 1 59  ? 29.447 11.805  8.648   1.00 11.90 ?  59  ASN   A C    1 
ATOM   1332 O O    . ASN   A 1 59  ? 30.366 11.768  7.821   1.00 11.94 ?  59  ASN   A O    1 
ATOM   1333 C CB   . ASN   A 1 59  ? 28.422 13.873  7.653   1.00 12.16 ?  59  ASN   A CB   1 
ATOM   1334 C CG   . ASN   A 1 59  ? 28.779 13.805  6.180   1.00 12.53 ?  59  ASN   A CG   1 
ATOM   1335 O OD1  . ASN   A 1 59  ? 28.075 13.182  5.382   1.00 12.78 ?  59  ASN   A OD1  1 
ATOM   1336 N ND2  . ASN   A 1 59  ? 29.861 14.478  5.805   1.00 13.57 ?  59  ASN   A ND2  1 
ATOM   1337 H H    . ASN   A 1 59  ? 26.535 11.923  9.234   1.00 14.64 ?  59  ASN   A H    1 
ATOM   1338 H HA   . ASN   A 1 59  ? 27.753 11.954  7.546   1.00 14.13 ?  59  ASN   A HA   1 
ATOM   1339 H HB2  . ASN   A 1 59  ? 27.636 14.432  7.739   1.00 14.59 ?  59  ASN   A HB2  1 
ATOM   1340 H HB3  . ASN   A 1 59  ? 29.171 14.277  8.118   1.00 14.59 ?  59  ASN   A HB3  1 
ATOM   1341 H HD21 . ASN   A 1 59  ? 30.109 14.471  4.980   1.00 16.28 ?  59  ASN   A HD21 1 
ATOM   1342 H HD22 . ASN   A 1 59  ? 30.332 14.903  6.388   1.00 16.28 ?  59  ASN   A HD22 1 
ATOM   1343 N N    . ALA   A 1 60  ? 29.576 11.257  9.857   1.00 11.70 ?  60  ALA   A N    1 
ATOM   1344 C CA   . ALA   A 1 60  ? 30.816 10.574  10.211  1.00 12.02 ?  60  ALA   A CA   1 
ATOM   1345 C C    . ALA   A 1 60  ? 31.042 9.340   9.343   1.00 12.00 ?  60  ALA   A C    1 
ATOM   1346 O O    . ALA   A 1 60  ? 32.188 9.008   9.011   1.00 12.55 ?  60  ALA   A O    1 
ATOM   1347 C CB   . ALA   A 1 60  ? 30.807 10.205  11.694  1.00 12.78 ?  60  ALA   A CB   1 
ATOM   1348 H H    . ALA   A 1 60  ? 28.979 11.265  10.475  1.00 14.04 ?  60  ALA   A H    1 
ATOM   1349 H HA   . ALA   A 1 60  ? 31.562 11.180  10.063  1.00 14.42 ?  60  ALA   A HA   1 
ATOM   1350 H HB1  . ALA   A 1 60  ? 31.634 9.754   11.915  1.00 15.33 ?  60  ALA   A HB1  1 
ATOM   1351 H HB2  . ALA   A 1 60  ? 30.720 11.017  12.221  1.00 15.33 ?  60  ALA   A HB2  1 
ATOM   1352 H HB3  . ALA   A 1 60  ? 30.052 9.619   11.867  1.00 15.33 ?  60  ALA   A HB3  1 
ATOM   1353 N N    . MET   A 1 61  ? 29.967 8.650   8.961   1.00 11.58 ?  61  MET   A N    1 
ATOM   1354 C CA   . MET   A 1 61  ? 30.111 7.510   8.060   1.00 11.27 ?  61  MET   A CA   1 
ATOM   1355 C C    . MET   A 1 61  ? 30.736 7.935   6.733   1.00 11.20 ?  61  MET   A C    1 
ATOM   1356 O O    . MET   A 1 61  ? 31.623 7.252   6.208   1.00 11.46 ?  61  MET   A O    1 
ATOM   1357 C CB   . MET   A 1 61  ? 28.753 6.830   7.858   1.00 11.39 ?  61  MET   A CB   1 
ATOM   1358 C CG   . MET   A 1 61  ? 28.759 5.672   6.873   1.00 11.74 ?  61  MET   A CG   1 
ATOM   1359 S SD   . MET   A 1 61  ? 27.130 4.930   6.663   1.00 13.10 ?  61  MET   A SD   1 
ATOM   1360 C CE   . MET   A 1 61  ? 26.978 4.058   8.220   1.00 14.41 ?  61  MET   A CE   1 
ATOM   1361 H H    . MET   A 1 61  ? 29.159 8.823   9.195   1.00 13.90 ?  61  MET   A H    1 
ATOM   1362 H HA   . MET   A 1 61  ? 30.698 6.863   8.479   1.00 13.53 ?  61  MET   A HA   1 
ATOM   1363 H HB2  . MET   A 1 61  ? 28.450 6.485   8.711   1.00 13.66 ?  61  MET   A HB2  1 
ATOM   1364 H HB3  . MET   A 1 61  ? 28.121 7.488   7.530   1.00 13.66 ?  61  MET   A HB3  1 
ATOM   1365 H HG2  . MET   A 1 61  ? 29.044 5.985   6.002   1.00 14.09 ?  61  MET   A HG2  1 
ATOM   1366 H HG3  . MET   A 1 61  ? 29.356 4.979   7.192   1.00 14.09 ?  61  MET   A HG3  1 
ATOM   1367 H HE1  . MET   A 1 61  ? 26.135 3.573   8.235   1.00 17.29 ?  61  MET   A HE1  1 
ATOM   1368 H HE2  . MET   A 1 61  ? 27.717 3.436   8.309   1.00 17.29 ?  61  MET   A HE2  1 
ATOM   1369 H HE3  . MET   A 1 61  ? 26.998 4.700   8.950   1.00 17.29 ?  61  MET   A HE3  1 
ATOM   1370 N N    . GLN   A 1 62  ? 30.301 9.069   6.181   1.00 11.37 ?  62  GLN   A N    1 
ATOM   1371 C CA   . GLN   A 1 62  ? 30.855 9.543   4.917   1.00 11.39 ?  62  GLN   A CA   1 
ATOM   1372 C C    . GLN   A 1 62  ? 32.326 9.921   5.056   1.00 11.38 ?  62  GLN   A C    1 
ATOM   1373 O O    . GLN   A 1 62  ? 33.134 9.608   4.174   1.00 11.91 ?  62  GLN   A O    1 
ATOM   1374 C CB   . GLN   A 1 62  ? 30.050 10.731  4.390   1.00 11.78 ?  62  GLN   A CB   1 
ATOM   1375 C CG   . GLN   A 1 62  ? 30.418 11.094  2.963   1.00 11.41 ?  62  GLN   A CG   1 
ATOM   1376 C CD   . GLN   A 1 62  ? 30.091 9.964   2.014   1.00 11.76 ?  62  GLN   A CD   1 
ATOM   1377 O OE1  . GLN   A 1 62  ? 28.913 9.654   1.808   1.00 12.41 ?  62  GLN   A OE1  1 
ATOM   1378 N NE2  . GLN   A 1 62  ? 31.112 9.295   1.482   1.00 12.42 ?  62  GLN   A NE2  1 
ATOM   1379 H H    . GLN   A 1 62  ? 29.692 9.572   6.517   1.00 13.64 ?  62  GLN   A H    1 
ATOM   1380 H HA   . GLN   A 1 62  ? 30.796 8.826   4.268   1.00 13.67 ?  62  GLN   A HA   1 
ATOM   1381 H HB2  . GLN   A 1 62  ? 29.108 10.516  4.416   1.00 14.14 ?  62  GLN   A HB2  1 
ATOM   1382 H HB3  . GLN   A 1 62  ? 30.230 11.506  4.951   1.00 14.14 ?  62  GLN   A HB3  1 
ATOM   1383 H HG2  . GLN   A 1 62  ? 29.908 11.872  2.692   1.00 13.69 ?  62  GLN   A HG2  1 
ATOM   1384 H HG3  . GLN   A 1 62  ? 31.368 11.276  2.909   1.00 13.69 ?  62  GLN   A HG3  1 
ATOM   1385 H HE21 . GLN   A 1 62  ? 31.920 9.531   1.662   1.00 14.91 ?  62  GLN   A HE21 1 
ATOM   1386 H HE22 . GLN   A 1 62  ? 30.967 8.639   0.946   1.00 14.91 ?  62  GLN   A HE22 1 
ATOM   1387 N N    . VAL   A 1 63  ? 32.695 10.591  6.150   1.00 11.71 ?  63  VAL   A N    1 
ATOM   1388 C CA   . VAL   A 1 63  ? 34.087 10.993  6.357   1.00 12.41 ?  63  VAL   A CA   1 
ATOM   1389 C C    . VAL   A 1 63  ? 34.984 9.760   6.420   1.00 12.04 ?  63  VAL   A C    1 
ATOM   1390 O O    . VAL   A 1 63  ? 36.028 9.688   5.757   1.00 12.64 ?  63  VAL   A O    1 
ATOM   1391 C CB   . VAL   A 1 63  ? 34.197 11.861  7.623   1.00 14.45 ?  63  VAL   A CB   1 
ATOM   1392 C CG1  . VAL   A 1 63  ? 35.646 12.094  7.996   1.00 16.28 ?  63  VAL   A CG1  1 
ATOM   1393 C CG2  . VAL   A 1 63  ? 33.474 13.198  7.423   1.00 15.10 ?  63  VAL   A CG2  1 
ATOM   1394 H H    . VAL   A 1 63  ? 32.157 10.825  6.787   1.00 14.05 ?  63  VAL   A H    1 
ATOM   1395 H HA   . VAL   A 1 63  ? 34.367 11.529  5.605   1.00 14.90 ?  63  VAL   A HA   1 
ATOM   1396 H HB   . VAL   A 1 63  ? 33.770 11.400  8.363   1.00 17.34 ?  63  VAL   A HB   1 
ATOM   1397 H HG11 . VAL   A 1 63  ? 35.692 12.830  8.623   1.00 19.54 ?  63  VAL   A HG11 1 
ATOM   1398 H HG12 . VAL   A 1 63  ? 36.000 11.288  8.401   1.00 19.54 ?  63  VAL   A HG12 1 
ATOM   1399 H HG13 . VAL   A 1 63  ? 36.143 12.311  7.192   1.00 19.54 ?  63  VAL   A HG13 1 
ATOM   1400 H HG21 . VAL   A 1 63  ? 33.562 13.728  8.232   1.00 18.12 ?  63  VAL   A HG21 1 
ATOM   1401 H HG22 . VAL   A 1 63  ? 33.878 13.665  6.676   1.00 18.12 ?  63  VAL   A HG22 1 
ATOM   1402 H HG23 . VAL   A 1 63  ? 32.538 13.026  7.241   1.00 18.12 ?  63  VAL   A HG23 1 
ATOM   1403 N N    . GLU   A 1 64  ? 34.564 8.752   7.193   1.00 12.17 ?  64  GLU   A N    1 
ATOM   1404 C CA   . GLU   A 1 64  ? 35.328 7.511   7.283   1.00 12.09 ?  64  GLU   A CA   1 
ATOM   1405 C C    . GLU   A 1 64  ? 35.410 6.825   5.924   1.00 12.03 ?  64  GLU   A C    1 
ATOM   1406 O O    . GLU   A 1 64  ? 36.457 6.269   5.545   1.00 12.43 ?  64  GLU   A O    1 
ATOM   1407 C CB   . GLU   A 1 64  ? 34.644 6.603   8.307   1.00 12.98 ?  64  GLU   A CB   1 
ATOM   1408 C CG   . GLU   A 1 64  ? 35.298 5.251   8.465   1.00 13.56 ?  64  GLU   A CG   1 
ATOM   1409 C CD   . GLU   A 1 64  ? 34.419 4.253   9.188   1.00 14.19 ?  64  GLU   A CD   1 
ATOM   1410 O OE1  . GLU   A 1 64  ? 33.179 4.337   9.055   1.00 15.19 ?  64  GLU   A OE1  1 
ATOM   1411 O OE2  . GLU   A 1 64  ? 34.965 3.361   9.876   1.00 14.82 -1 64  GLU   A OE2  1 
ATOM   1412 H H    . GLU   A 1 64  ? 33.843 8.763   7.662   1.00 14.61 ?  64  GLU   A H    1 
ATOM   1413 H HA   . GLU   A 1 64  ? 36.227 7.709   7.595   1.00 14.51 ?  64  GLU   A HA   1 
ATOM   1414 H HB2  . GLU   A 1 64  ? 34.666 7.049   9.178   1.00 15.58 ?  64  GLU   A HB2  1 
ATOM   1415 H HB3  . GLU   A 1 64  ? 33.726 6.471   8.037   1.00 15.58 ?  64  GLU   A HB3  1 
ATOM   1416 H HG2  . GLU   A 1 64  ? 35.503 4.888   7.588   1.00 16.27 ?  64  GLU   A HG2  1 
ATOM   1417 H HG3  . GLU   A 1 64  ? 36.117 5.359   8.974   1.00 16.27 ?  64  GLU   A HG3  1 
ATOM   1418 N N    . SER   A 1 65  ? 34.286 6.812   5.200   1.00 11.63 ?  65  SER   A N    1 
ATOM   1419 C CA   . SER   A 1 65  ? 34.231 6.154   3.901   1.00 11.49 ?  65  SER   A CA   1 
ATOM   1420 C C    . SER   A 1 65  ? 35.159 6.820   2.895   1.00 11.59 ?  65  SER   A C    1 
ATOM   1421 O O    . SER   A 1 65  ? 35.791 6.139   2.082   1.00 12.35 ?  65  SER   A O    1 
ATOM   1422 C CB   . SER   A 1 65  ? 32.794 6.170   3.373   1.00 11.62 ?  65  SER   A CB   1 
ATOM   1423 O OG   . SER   A 1 65  ? 31.951 5.340   4.158   1.00 11.92 ?  65  SER   A OG   1 
ATOM   1424 H H    . SER   A 1 65  ? 33.551 7.185   5.440   1.00 13.96 ?  65  SER   A H    1 
ATOM   1425 H HA   . SER   A 1 65  ? 34.513 5.234   3.999   1.00 13.78 ?  65  SER   A HA   1 
ATOM   1426 H HB2  . SER   A 1 65  ? 32.456 7.074   3.400   1.00 13.94 ?  65  SER   A HB2  1 
ATOM   1427 H HB3  . SER   A 1 65  ? 32.796 5.839   2.460   1.00 13.94 ?  65  SER   A HB3  1 
ATOM   1428 H HG   . SER   A 1 65  ? 31.948 5.609   4.958   1.00 14.31 ?  65  SER   A HG   1 
ATOM   1429 N N    . ASP   A 1 66  ? 35.229 8.155   2.910   1.00 11.78 ?  66  ASP   A N    1 
ATOM   1430 C CA   . ASP   A 1 66  ? 36.084 8.853   1.956   1.00 12.57 ?  66  ASP   A CA   1 
ATOM   1431 C C    . ASP   A 1 66  ? 37.551 8.504   2.186   1.00 12.96 ?  66  ASP   A C    1 
ATOM   1432 O O    . ASP   A 1 66  ? 38.318 8.335   1.230   1.00 13.89 ?  66  ASP   A O    1 
ATOM   1433 C CB   . ASP   A 1 66  ? 35.868 10.363  2.063   1.00 14.10 ?  66  ASP   A CB   1 
ATOM   1434 C CG   . ASP   A 1 66  ? 34.524 10.832  1.481   1.00 16.09 ?  66  ASP   A CG   1 
ATOM   1435 O OD1  . ASP   A 1 66  ? 33.809 10.040  0.837   1.00 15.87 ?  66  ASP   A OD1  1 
ATOM   1436 O OD2  . ASP   A 1 66  ? 34.216 12.031  1.644   1.00 19.16 -1 66  ASP   A OD2  1 
ATOM   1437 H H    . ASP   A 1 66  ? 34.784 8.670   3.444   1.00 14.13 ?  66  ASP   A H    1 
ATOM   1438 H HA   . ASP   A 1 66  ? 35.843 8.580   1.057   1.00 15.08 ?  66  ASP   A HA   1 
ATOM   1439 H HB2  . ASP   A 1 66  ? 35.891 10.621  2.996   1.00 16.92 ?  66  ASP   A HB2  1 
ATOM   1440 H HB3  . ASP   A 1 66  ? 36.581 10.815  1.578   1.00 16.92 ?  66  ASP   A HB3  1 
ATOM   1441 N N    . ASP   A 1 67  ? 37.954 8.367   3.449   1.00 13.09 ?  67  ASP   A N    1 
ATOM   1442 C CA   . ASP   A 1 67  ? 39.309 7.921   3.744   1.00 14.10 ?  67  ASP   A CA   1 
ATOM   1443 C C    . ASP   A 1 67  ? 39.529 6.487   3.278   1.00 14.07 ?  67  ASP   A C    1 
ATOM   1444 O O    . ASP   A 1 67  ? 40.589 6.164   2.730   1.00 14.50 ?  67  ASP   A O    1 
ATOM   1445 C CB   . ASP   A 1 67  ? 39.578 8.056   5.239   1.00 15.40 ?  67  ASP   A CB   1 
ATOM   1446 C CG   . ASP   A 1 67  ? 40.877 7.395   5.658   1.00 16.49 ?  67  ASP   A CG   1 
ATOM   1447 O OD1  . ASP   A 1 67  ? 41.953 8.026   5.517   1.00 19.33 ?  67  ASP   A OD1  1 
ATOM   1448 O OD2  . ASP   A 1 67  ? 40.822 6.234   6.125   1.00 16.13 -1 67  ASP   A OD2  1 
ATOM   1449 H H    . ASP   A 1 67  ? 37.472 8.520   4.138   1.00 15.71 ?  67  ASP   A H    1 
ATOM   1450 H HA   . ASP   A 1 67  ? 39.941 8.486   3.270   1.00 16.92 ?  67  ASP   A HA   1 
ATOM   1451 H HB2  . ASP   A 1 67  ? 39.635 8.994   5.461   1.00 18.47 ?  67  ASP   A HB2  1 
ATOM   1452 H HB3  . ASP   A 1 67  ? 38.851 7.637   5.725   1.00 18.47 ?  67  ASP   A HB3  1 
ATOM   1453 N N    . TYR   A 1 68  ? 38.538 5.611   3.475   1.00 13.34 ?  68  TYR   A N    1 
ATOM   1454 C CA   . TYR   A 1 68  ? 38.657 4.231   3.004   1.00 13.37 ?  68  TYR   A CA   1 
ATOM   1455 C C    . TYR   A 1 68  ? 38.894 4.182   1.494   1.00 12.99 ?  68  TYR   A C    1 
ATOM   1456 O O    . TYR   A 1 68  ? 39.767 3.447   1.016   1.00 13.36 ?  68  TYR   A O    1 
ATOM   1457 C CB   . TYR   A 1 68  ? 37.408 3.414   3.387   1.00 13.73 ?  68  TYR   A CB   1 
ATOM   1458 C CG   . TYR   A 1 68  ? 37.431 2.029   2.755   1.00 15.44 ?  68  TYR   A CG   1 
ATOM   1459 C CD1  . TYR   A 1 68  ? 36.975 1.839   1.455   1.00 16.62 ?  68  TYR   A CD1  1 
ATOM   1460 C CD2  . TYR   A 1 68  ? 37.969 0.938   3.420   1.00 17.03 ?  68  TYR   A CD2  1 
ATOM   1461 C CE1  . TYR   A 1 68  ? 37.040 0.621   0.836   1.00 18.07 ?  68  TYR   A CE1  1 
ATOM   1462 C CE2  . TYR   A 1 68  ? 38.032 -0.323  2.797   1.00 18.03 ?  68  TYR   A CE2  1 
ATOM   1463 C CZ   . TYR   A 1 68  ? 37.576 -0.456  1.506   1.00 18.53 ?  68  TYR   A CZ   1 
ATOM   1464 O OH   . TYR   A 1 68  ? 37.649 -1.674  0.877   1.00 20.06 ?  68  TYR   A OH   1 
ATOM   1465 H H    . TYR   A 1 68  ? 37.793 5.788   3.868   1.00 16.01 ?  68  TYR   A H    1 
ATOM   1466 H HA   . TYR   A 1 68  ? 39.420 3.819   3.435   1.00 16.05 ?  68  TYR   A HA   1 
ATOM   1467 H HB2  . TYR   A 1 68  ? 37.381 3.302   4.351   1.00 16.47 ?  68  TYR   A HB2  1 
ATOM   1468 H HB3  . TYR   A 1 68  ? 36.613 3.873   3.078   1.00 16.47 ?  68  TYR   A HB3  1 
ATOM   1469 H HD1  . TYR   A 1 68  ? 36.629 2.571   0.988   1.00 19.94 ?  68  TYR   A HD1  1 
ATOM   1470 H HD2  . TYR   A 1 68  ? 38.298 1.036   4.281   1.00 20.43 ?  68  TYR   A HD2  1 
ATOM   1471 H HE1  . TYR   A 1 68  ? 36.723 0.526   -0.034  1.00 21.68 ?  68  TYR   A HE1  1 
ATOM   1472 H HE2  . TYR   A 1 68  ? 38.393 -1.057  3.236   1.00 21.63 ?  68  TYR   A HE2  1 
ATOM   1473 H HH   . TYR   A 1 68  ? 37.980 -2.242  1.395   1.00 24.08 ?  68  TYR   A HH   1 
ATOM   1474 N N    . ILE   A 1 69  ? 38.108 4.942   0.724   1.00 12.52 ?  69  ILE   A N    1 
ATOM   1475 C CA   . ILE   A 1 69  ? 38.248 4.938   -0.732  1.00 13.06 ?  69  ILE   A CA   1 
ATOM   1476 C C    . ILE   A 1 69  ? 39.580 5.548   -1.159  1.00 12.90 ?  69  ILE   A C    1 
ATOM   1477 O O    . ILE   A 1 69  ? 40.231 5.061   -2.092  1.00 13.36 ?  69  ILE   A O    1 
ATOM   1478 C CB   . ILE   A 1 69  ? 37.052 5.651   -1.397  1.00 13.83 ?  69  ILE   A CB   1 
ATOM   1479 C CG1  . ILE   A 1 69  ? 35.731 4.925   -1.123  1.00 14.26 ?  69  ILE   A CG1  1 
ATOM   1480 C CG2  . ILE   A 1 69  ? 37.297 5.850   -2.905  1.00 15.74 ?  69  ILE   A CG2  1 
ATOM   1481 C CD1  . ILE   A 1 69  ? 35.550 3.645   -1.907  1.00 14.85 ?  69  ILE   A CD1  1 
ATOM   1482 H H    . ILE   A 1 69  ? 37.498 5.467   1.020   1.00 15.03 ?  69  ILE   A H    1 
ATOM   1483 H HA   . ILE   A 1 69  ? 38.242 4.016   -1.037  1.00 15.67 ?  69  ILE   A HA   1 
ATOM   1484 H HB   . ILE   A 1 69  ? 36.986 6.531   -1.000  1.00 16.60 ?  69  ILE   A HB   1 
ATOM   1485 H HG12 . ILE   A 1 69  ? 35.694 4.702   -0.178  1.00 17.11 ?  69  ILE   A HG12 1 
ATOM   1486 H HG13 . ILE   A 1 69  ? 35.001 5.521   -1.347  1.00 17.11 ?  69  ILE   A HG13 1 
ATOM   1487 H HG21 . ILE   A 1 69  ? 36.451 6.065   -3.335  1.00 18.88 ?  69  ILE   A HG21 1 
ATOM   1488 H HG22 . ILE   A 1 69  ? 37.919 6.589   -3.032  1.00 18.88 ?  69  ILE   A HG22 1 
ATOM   1489 H HG23 . ILE   A 1 69  ? 37.662 5.040   -3.282  1.00 18.88 ?  69  ILE   A HG23 1 
ATOM   1490 H HD11 . ILE   A 1 69  ? 34.751 3.199   -1.587  1.00 17.82 ?  69  ILE   A HD11 1 
ATOM   1491 H HD12 . ILE   A 1 69  ? 35.450 3.866   -2.846  1.00 17.82 ?  69  ILE   A HD12 1 
ATOM   1492 H HD13 . ILE   A 1 69  ? 36.323 3.081   -1.775  1.00 17.82 ?  69  ILE   A HD13 1 
ATOM   1493 N N    . ALA   A 1 70  ? 39.992 6.634   -0.510  1.00 13.20 ?  70  ALA   A N    1 
ATOM   1494 C CA   . ALA   A 1 70  ? 41.269 7.242   -0.861  1.00 14.24 ?  70  ALA   A CA   1 
ATOM   1495 C C    . ALA   A 1 70  ? 42.416 6.254   -0.695  1.00 14.94 ?  70  ALA   A C    1 
ATOM   1496 O O    . ALA   A 1 70  ? 43.376 6.282   -1.469  1.00 17.02 ?  70  ALA   A O    1 
ATOM   1497 C CB   . ALA   A 1 70  ? 41.505 8.490   -0.012  1.00 14.90 ?  70  ALA   A CB   1 
ATOM   1498 H H    . ALA   A 1 70  ? 39.556 7.032   0.114   1.00 15.84 ?  70  ALA   A H    1 
ATOM   1499 H HA   . ALA   A 1 70  ? 41.240 7.523   -1.792  1.00 17.08 ?  70  ALA   A HA   1 
ATOM   1500 H HB1  . ALA   A 1 70  ? 42.363 8.880   -0.257  1.00 17.88 ?  70  ALA   A HB1  1 
ATOM   1501 H HB2  . ALA   A 1 70  ? 40.795 9.128   -0.173  1.00 17.88 ?  70  ALA   A HB2  1 
ATOM   1502 H HB3  . ALA   A 1 70  ? 41.519 8.236   0.925   1.00 17.88 ?  70  ALA   A HB3  1 
ATOM   1503 N N    . THR   A 1 71  ? 42.317 5.358   0.283   1.00 14.25 ?  71  THR   A N    1 
ATOM   1504 C CA   . THR   A 1 71  ? 43.367 4.374   0.526   1.00 15.95 ?  71  THR   A CA   1 
ATOM   1505 C C    . THR   A 1 71  ? 43.244 3.151   -0.375  1.00 15.80 ?  71  THR   A C    1 
ATOM   1506 O O    . THR   A 1 71  ? 44.257 2.647   -0.883  1.00 17.98 ?  71  THR   A O    1 
ATOM   1507 C CB   . THR   A 1 71  ? 43.308 3.919   1.981   1.00 17.77 ?  71  THR   A CB   1 
ATOM   1508 O OG1  . THR   A 1 71  ? 43.563 5.041   2.831   1.00 19.10 ?  71  THR   A OG1  1 
ATOM   1509 C CG2  . THR   A 1 71  ? 44.325 2.816   2.255   1.00 19.24 ?  71  THR   A CG2  1 
ATOM   1510 H H    . THR   A 1 71  ? 41.645 5.291   0.812   1.00 17.10 ?  71  THR   A H    1 
ATOM   1511 H HA   . THR   A 1 71  ? 44.230 4.780   0.361   1.00 19.14 ?  71  THR   A HA   1 
ATOM   1512 H HB   . THR   A 1 71  ? 42.420 3.565   2.163   1.00 21.33 ?  71  THR   A HB   1 
ATOM   1513 H HG1  . THR   A 1 71  ? 42.976 5.631   2.699   1.00 22.92 ?  71  THR   A HG1  1 
ATOM   1514 H HG21 . THR   A 1 71  ? 44.472 2.736   3.210   1.00 23.09 ?  71  THR   A HG21 1 
ATOM   1515 H HG22 . THR   A 1 71  ? 44.006 1.966   1.913   1.00 23.09 ?  71  THR   A HG22 1 
ATOM   1516 H HG23 . THR   A 1 71  ? 45.171 3.031   1.826   1.00 23.09 ?  71  THR   A HG23 1 
ATOM   1517 N N    . ASN   A 1 72  ? 42.023 2.639   -0.557  1.00 14.62 ?  72  ASN   A N    1 
ATOM   1518 C CA   . ASN   A 1 72  ? 41.809 1.312   -1.122  1.00 15.03 ?  72  ASN   A CA   1 
ATOM   1519 C C    . ASN   A 1 72  ? 41.191 1.306   -2.506  1.00 15.07 ?  72  ASN   A C    1 
ATOM   1520 O O    . ASN   A 1 72  ? 41.207 0.258   -3.163  1.00 16.14 ?  72  ASN   A O    1 
ATOM   1521 C CB   . ASN   A 1 72  ? 40.915 0.492   -0.185  1.00 15.76 ?  72  ASN   A CB   1 
ATOM   1522 C CG   . ASN   A 1 72  ? 41.528 0.333   1.181   1.00 16.75 ?  72  ASN   A CG   1 
ATOM   1523 O OD1  . ASN   A 1 72  ? 41.078 0.931   2.154   1.00 18.74 ?  72  ASN   A OD1  1 
ATOM   1524 N ND2  . ASN   A 1 72  ? 42.586 -0.442  1.253   1.00 17.27 ?  72  ASN   A ND2  1 
ATOM   1525 H H    . ASN   A 1 72  ? 41.290 3.049   -0.358  1.00 17.55 ?  72  ASN   A H    1 
ATOM   1526 H HA   . ASN   A 1 72  ? 42.662 0.861   -1.188  1.00 18.04 ?  72  ASN   A HA   1 
ATOM   1527 H HB2  . ASN   A 1 72  ? 40.058 0.936   -0.089  1.00 18.91 ?  72  ASN   A HB2  1 
ATOM   1528 H HB3  . ASN   A 1 72  ? 40.787 -0.395  -0.565  1.00 18.91 ?  72  ASN   A HB3  1 
ATOM   1529 H HD21 . ASN   A 1 72  ? 42.977 -0.559  2.011   1.00 20.73 ?  72  ASN   A HD21 1 
ATOM   1530 H HD22 . ASN   A 1 72  ? 42.881 -0.836  0.550   1.00 20.73 ?  72  ASN   A HD22 1 
ATOM   1531 N N    . GLY   A 1 73  ? 40.632 2.421   -2.959  1.00 14.72 ?  73  GLY   A N    1 
ATOM   1532 C CA   . GLY   A 1 73  ? 39.895 2.447   -4.197  1.00 14.38 ?  73  GLY   A CA   1 
ATOM   1533 C C    . GLY   A 1 73  ? 38.501 1.868   -4.034  1.00 13.38 ?  73  GLY   A C    1 
ATOM   1534 O O    . GLY   A 1 73  ? 38.117 1.403   -2.956  1.00 14.04 ?  73  GLY   A O    1 
ATOM   1535 H H    . GLY   A 1 73  ? 40.670 3.190   -2.562  1.00 17.66 ?  73  GLY   A H    1 
ATOM   1536 H HA2  . GLY   A 1 73  ? 39.816 3.366   -4.508  1.00 17.26 ?  73  GLY   A HA2  1 
ATOM   1537 H HA3  . GLY   A 1 73  ? 40.369 1.935   -4.869  1.00 17.26 ?  73  GLY   A HA3  1 
ATOM   1538 N N    . PRO   A 1 74  ? 37.725 1.884   -5.115  1.00 14.23 ?  74  PRO   A N    1 
ATOM   1539 C CA   . PRO   A 1 74  ? 36.327 1.453   -5.033  1.00 14.42 ?  74  PRO   A CA   1 
ATOM   1540 C C    . PRO   A 1 74  ? 36.182 -0.029  -4.711  1.00 13.41 ?  74  PRO   A C    1 
ATOM   1541 O O    . PRO   A 1 74  ? 37.056 -0.856  -4.994  1.00 14.24 ?  74  PRO   A O    1 
ATOM   1542 C CB   . PRO   A 1 74  ? 35.781 1.753   -6.434  1.00 16.12 ?  74  PRO   A CB   1 
ATOM   1543 C CG   . PRO   A 1 74  ? 36.726 2.746   -7.029  1.00 18.81 ?  74  PRO   A CG   1 
ATOM   1544 C CD   . PRO   A 1 74  ? 38.062 2.419   -6.445  1.00 16.57 ?  74  PRO   A CD   1 
ATOM   1545 H HA   . PRO   A 1 74  ? 35.843 1.983   -4.377  1.00 17.30 ?  74  PRO   A HA   1 
ATOM   1546 H HB2  . PRO   A 1 74  ? 35.764 0.938   -6.958  1.00 19.34 ?  74  PRO   A HB2  1 
ATOM   1547 H HB3  . PRO   A 1 74  ? 34.889 2.132   -6.363  1.00 19.34 ?  74  PRO   A HB3  1 
ATOM   1548 H HG2  . PRO   A 1 74  ? 36.743 2.645   -7.994  1.00 22.57 ?  74  PRO   A HG2  1 
ATOM   1549 H HG3  . PRO   A 1 74  ? 36.457 3.644   -6.783  1.00 22.57 ?  74  PRO   A HG3  1 
ATOM   1550 H HD2  . PRO   A 1 74  ? 38.517 1.744   -6.977  1.00 19.89 ?  74  PRO   A HD2  1 
ATOM   1551 H HD3  . PRO   A 1 74  ? 38.603 3.227   -6.371  1.00 19.89 ?  74  PRO   A HD3  1 
ATOM   1552 N N    . LEU   A 1 75  ? 35.037 -0.356  -4.118  1.00 12.57 ?  75  LEU   A N    1 
ATOM   1553 C CA   . LEU   A 1 75  ? 34.631 -1.744  -3.970  1.00 12.36 ?  75  LEU   A CA   1 
ATOM   1554 C C    . LEU   A 1 75  ? 34.253 -2.322  -5.329  1.00 12.73 ?  75  LEU   A C    1 
ATOM   1555 O O    . LEU   A 1 75  ? 34.125 -1.610  -6.327  1.00 14.34 ?  75  LEU   A O    1 
ATOM   1556 C CB   . LEU   A 1 75  ? 33.439 -1.862  -3.018  1.00 12.41 ?  75  LEU   A CB   1 
ATOM   1557 C CG   . LEU   A 1 75  ? 33.657 -1.458  -1.564  1.00 13.98 ?  75  LEU   A CG   1 
ATOM   1558 C CD1  . LEU   A 1 75  ? 32.378 -1.655  -0.753  1.00 15.95 ?  75  LEU   A CD1  1 
ATOM   1559 C CD2  . LEU   A 1 75  ? 34.814 -2.175  -0.924  1.00 17.98 ?  75  LEU   A CD2  1 
ATOM   1560 H H    . LEU   A 1 75  ? 34.476 0.216   -3.799  1.00 15.09 ?  75  LEU   A H    1 
ATOM   1561 H HA   . LEU   A 1 75  ? 35.368 -2.256  -3.617  1.00 14.83 ?  75  LEU   A HA   1 
ATOM   1562 H HB2  . LEU   A 1 75  ? 32.719 -1.312  -3.363  1.00 14.89 ?  75  LEU   A HB2  1 
ATOM   1563 H HB3  . LEU   A 1 75  ? 33.154 -2.791  -3.015  1.00 14.89 ?  75  LEU   A HB3  1 
ATOM   1564 H HG   . LEU   A 1 75  ? 33.867 -0.510  -1.546  1.00 16.77 ?  75  LEU   A HG   1 
ATOM   1565 H HD11 . LEU   A 1 75  ? 32.544 -1.385  0.165   1.00 19.14 ?  75  LEU   A HD11 1 
ATOM   1566 H HD12 . LEU   A 1 75  ? 31.676 -1.104  -1.136  1.00 19.14 ?  75  LEU   A HD12 1 
ATOM   1567 H HD13 . LEU   A 1 75  ? 32.125 -2.587  -0.785  1.00 19.14 ?  75  LEU   A HD13 1 
ATOM   1568 H HD21 . LEU   A 1 75  ? 34.861 -1.927  0.012   1.00 21.58 ?  75  LEU   A HD21 1 
ATOM   1569 H HD22 . LEU   A 1 75  ? 34.680 -3.130  -1.010  1.00 21.58 ?  75  LEU   A HD22 1 
ATOM   1570 H HD23 . LEU   A 1 75  ? 35.637 -1.916  -1.374  1.00 21.58 ?  75  LEU   A HD23 1 
ATOM   1571 N N    . LYS   A 1 76  ? 34.079 -3.643  -5.354  1.00 13.20 ?  76  LYS   A N    1 
ATOM   1572 C CA   . LYS   A 1 76  ? 33.481 -4.353  -6.479  1.00 13.61 ?  76  LYS   A CA   1 
ATOM   1573 C C    . LYS   A 1 76  ? 31.971 -4.445  -6.279  1.00 12.21 ?  76  LYS   A C    1 
ATOM   1574 O O    . LYS   A 1 76  ? 31.493 -4.576  -5.153  1.00 12.24 ?  76  LYS   A O    1 
ATOM   1575 C CB   . LYS   A 1 76  ? 34.025 -5.791  -6.550  1.00 15.84 ?  76  LYS   A CB   1 
ATOM   1576 C CG   . LYS   A 1 76  ? 35.535 -5.908  -6.735  1.00 17.29 ?  76  LYS   A CG   1 
ATOM   1577 C CD   . LYS   A 1 76  ? 36.042 -7.321  -6.527  1.00 18.70 ?  76  LYS   A CD   1 
ATOM   1578 C CE   . LYS   A 1 76  ? 37.546 -7.384  -6.707  1.00 21.18 ?  76  LYS   A CE   1 
ATOM   1579 N NZ   . LYS   A 1 76  ? 38.072 -8.750  -6.528  1.00 22.14 ?  76  LYS   A NZ   1 
ATOM   1580 H H    . LYS   A 1 76  ? 34.306 -4.165  -4.706  1.00 15.85 ?  76  LYS   A H    1 
ATOM   1581 H HA   . LYS   A 1 76  ? 33.675 -3.891  -7.312  1.00 16.33 ?  76  LYS   A HA   1 
ATOM   1582 H HB2  . LYS   A 1 76  ? 33.796 -6.245  -5.725  1.00 19.01 ?  76  LYS   A HB2  1 
ATOM   1583 H HB3  . LYS   A 1 76  ? 33.604 -6.240  -7.298  1.00 19.01 ?  76  LYS   A HB3  1 
ATOM   1584 H HG2  . LYS   A 1 76  ? 35.765 -5.633  -7.637  1.00 20.75 ?  76  LYS   A HG2  1 
ATOM   1585 H HG3  . LYS   A 1 76  ? 35.978 -5.329  -6.092  1.00 20.75 ?  76  LYS   A HG3  1 
ATOM   1586 H HD2  . LYS   A 1 76  ? 35.827 -7.610  -5.625  1.00 22.44 ?  76  LYS   A HD2  1 
ATOM   1587 H HD3  . LYS   A 1 76  ? 35.628 -7.910  -7.178  1.00 22.44 ?  76  LYS   A HD3  1 
ATOM   1588 H HE2  . LYS   A 1 76  ? 37.770 -7.086  -7.601  1.00 25.41 ?  76  LYS   A HE2  1 
ATOM   1589 H HE3  . LYS   A 1 76  ? 37.967 -6.810  -6.047  1.00 25.41 ?  76  LYS   A HE3  1 
ATOM   1590 H HZ1  . LYS   A 1 76  ? 38.954 -8.761  -6.641  1.00 26.56 ?  76  LYS   A HZ1  1 
ATOM   1591 H HZ2  . LYS   A 1 76  ? 37.881 -9.052  -5.711  1.00 26.56 ?  76  LYS   A HZ2  1 
ATOM   1592 H HZ3  . LYS   A 1 76  ? 37.702 -9.303  -7.127  1.00 26.56 ?  76  LYS   A HZ3  1 
ATOM   1593 N N    . VAL   A 1 77  ? 31.217 -4.409  -7.382  1.00 12.54 ?  77  VAL   A N    1 
ATOM   1594 C CA   . VAL   A 1 77  ? 29.808 -4.796  -7.294  1.00 12.65 ?  77  VAL   A CA   1 
ATOM   1595 C C    . VAL   A 1 77  ? 29.741 -6.251  -6.855  1.00 12.39 ?  77  VAL   A C    1 
ATOM   1596 O O    . VAL   A 1 77  ? 30.390 -7.123  -7.445  1.00 12.99 ?  77  VAL   A O    1 
ATOM   1597 C CB   . VAL   A 1 77  ? 29.082 -4.575  -8.629  1.00 13.94 ?  77  VAL   A CB   1 
ATOM   1598 C CG1  . VAL   A 1 77  ? 27.624 -5.010  -8.509  1.00 14.77 ?  77  VAL   A CG1  1 
ATOM   1599 C CG2  . VAL   A 1 77  ? 29.169 -3.121  -9.054  1.00 15.62 ?  77  VAL   A CG2  1 
ATOM   1600 H H    . VAL   A 1 77  ? 31.488 -4.165  -8.161  1.00 15.05 ?  77  VAL   A H    1 
ATOM   1601 H HA   . VAL   A 1 77  ? 29.375 -4.252  -6.617  1.00 15.18 ?  77  VAL   A HA   1 
ATOM   1602 H HB   . VAL   A 1 77  ? 29.506 -5.116  -9.313  1.00 16.72 ?  77  VAL   A HB   1 
ATOM   1603 H HG11 . VAL   A 1 77  ? 27.141 -4.701  -9.287  1.00 17.73 ?  77  VAL   A HG11 1 
ATOM   1604 H HG12 . VAL   A 1 77  ? 27.587 -5.979  -8.457  1.00 17.73 ?  77  VAL   A HG12 1 
ATOM   1605 H HG13 . VAL   A 1 77  ? 27.246 -4.621  -7.705  1.00 17.73 ?  77  VAL   A HG13 1 
ATOM   1606 H HG21 . VAL   A 1 77  ? 28.656 -3.001  -9.868  1.00 18.74 ?  77  VAL   A HG21 1 
ATOM   1607 H HG22 . VAL   A 1 77  ? 28.803 -2.564  -8.348  1.00 18.74 ?  77  VAL   A HG22 1 
ATOM   1608 H HG23 . VAL   A 1 77  ? 30.097 -2.890  -9.209  1.00 18.74 ?  77  VAL   A HG23 1 
ATOM   1609 N N    . GLY   A 1 78  ? 28.963 -6.519  -5.805  1.00 11.83 ?  78  GLY   A N    1 
ATOM   1610 C CA   . GLY   A 1 78  ? 28.941 -7.812  -5.154  1.00 12.08 ?  78  GLY   A CA   1 
ATOM   1611 C C    . GLY   A 1 78  ? 29.859 -7.908  -3.957  1.00 11.67 ?  78  GLY   A C    1 
ATOM   1612 O O    . GLY   A 1 78  ? 29.800 -8.906  -3.227  1.00 12.24 ?  78  GLY   A O    1 
ATOM   1613 H H    . GLY   A 1 78  ? 28.421 -5.944  -5.451  1.00 14.20 ?  78  GLY   A H    1 
ATOM   1614 H HA2  . GLY   A 1 78  ? 28.037 -8.003  -4.864  1.00 14.50 ?  78  GLY   A HA2  1 
ATOM   1615 H HA3  . GLY   A 1 78  ? 29.205 -8.489  -5.796  1.00 14.50 ?  78  GLY   A HA3  1 
ATOM   1616 N N    . GLY   A 1 79  ? 30.711 -6.904  -3.734  1.00 11.69 ?  79  GLY   A N    1 
ATOM   1617 C CA   . GLY   A 1 79  ? 31.674 -6.927  -2.658  1.00 12.15 ?  79  GLY   A CA   1 
ATOM   1618 C C    . GLY   A 1 79  ? 31.230 -6.129  -1.446  1.00 11.34 ?  79  GLY   A C    1 
ATOM   1619 O O    . GLY   A 1 79  ? 30.110 -5.618  -1.370  1.00 11.81 ?  79  GLY   A O    1 
ATOM   1620 H H    . GLY   A 1 79  ? 30.751 -6.189  -4.213  1.00 14.03 ?  79  GLY   A H    1 
ATOM   1621 H HA2  . GLY   A 1 79  ? 31.825 -7.851  -2.386  1.00 14.58 ?  79  GLY   A HA2  1 
ATOM   1622 H HA3  . GLY   A 1 79  ? 32.518 -6.568  -2.976  1.00 14.58 ?  79  GLY   A HA3  1 
ATOM   1623 N N    . SER   A 1 80  ? 32.138 -6.027  -0.479  1.00 12.12 ?  80  SER   A N    1 
ATOM   1624 C CA   . SER   A 1 80  ? 31.812 -5.407  0.794   1.00 11.53 ?  80  SER   A CA   1 
ATOM   1625 C C    . SER   A 1 80  ? 33.087 -4.957  1.491   1.00 11.76 ?  80  SER   A C    1 
ATOM   1626 O O    . SER   A 1 80  ? 34.200 -5.385  1.156   1.00 12.99 ?  80  SER   A O    1 
ATOM   1627 C CB   . SER   A 1 80  ? 31.053 -6.374  1.712   1.00 12.90 ?  80  SER   A CB   1 
ATOM   1628 O OG   . SER   A 1 80  ? 31.888 -7.420  2.190   1.00 14.52 ?  80  SER   A OG   1 
ATOM   1629 H H    . SER   A 1 80  ? 32.954 -6.299  -0.542  1.00 14.54 ?  80  SER   A H    1 
ATOM   1630 H HA   . SER   A 1 80  ? 31.259 -4.623  0.622   1.00 13.84 ?  80  SER   A HA   1 
ATOM   1631 H HB2  . SER   A 1 80  ? 30.708 -5.877  2.468   1.00 15.48 ?  80  SER   A HB2  1 
ATOM   1632 H HB3  . SER   A 1 80  ? 30.320 -6.764  1.210   1.00 15.48 ?  80  SER   A HB3  1 
ATOM   1633 H HG   . SER   A 1 80  ? 32.197 -7.851  1.536   1.00 17.43 ?  80  SER   A HG   1 
ATOM   1634 N N    . CYS   A 1 81  ? 32.899 -4.113  2.503   1.00 11.28 ?  81  CYS   A N    1 
ATOM   1635 C CA   . CYS   A 1 81  ? 33.953 -3.824  3.462   1.00 11.58 ?  81  CYS   A CA   1 
ATOM   1636 C C    . CYS   A 1 81  ? 33.319 -3.588  4.822   1.00 11.52 ?  81  CYS   A C    1 
ATOM   1637 O O    . CYS   A 1 81  ? 32.152 -3.194  4.914   1.00 12.49 ?  81  CYS   A O    1 
ATOM   1638 C CB   . CYS   A 1 81  ? 34.812 -2.631  3.038   1.00 12.41 ?  81  CYS   A CB   1 
ATOM   1639 S SG   . CYS   A 1 81  ? 33.933 -1.055  3.068   1.00 12.68 ?  81  CYS   A SG   1 
ATOM   1640 H H    . CYS   A 1 81  ? 32.160 -3.688  2.660   1.00 13.53 ?  81  CYS   A H    1 
ATOM   1641 H HA   . CYS   A 1 81  ? 34.530 -4.596  3.530   1.00 13.90 ?  81  CYS   A HA   1 
ATOM   1642 H HB2  . CYS   A 1 81  ? 35.574 -2.563  3.640   1.00 14.90 ?  81  CYS   A HB2  1 
ATOM   1643 H HB3  . CYS   A 1 81  ? 35.132 -2.781  2.130   1.00 14.90 ?  81  CYS   A HB3  1 
ATOM   1644 H HG   . CYS   A 1 81  ? 34.679 -0.180  2.725   1.00 15.21 ?  81  CYS   A HG   1 
ATOM   1645 N N    . VAL   A 1 82  ? 34.084 -3.859  5.876   1.00 11.95 ?  82  VAL   A N    1 
ATOM   1646 C CA   . VAL   A 1 82  ? 33.661 -3.614  7.248   1.00 12.43 ?  82  VAL   A CA   1 
ATOM   1647 C C    . VAL   A 1 82  ? 34.258 -2.296  7.714   1.00 12.72 ?  82  VAL   A C    1 
ATOM   1648 O O    . VAL   A 1 82  ? 35.483 -2.116  7.685   1.00 13.43 ?  82  VAL   A O    1 
ATOM   1649 C CB   . VAL   A 1 82  ? 34.086 -4.757  8.184   1.00 14.22 ?  82  VAL   A CB   1 
ATOM   1650 C CG1  . VAL   A 1 82  ? 33.638 -4.463  9.607   1.00 15.75 ?  82  VAL   A CG1  1 
ATOM   1651 C CG2  . VAL   A 1 82  ? 33.515 -6.083  7.709   1.00 15.10 ?  82  VAL   A CG2  1 
ATOM   1652 H H    . VAL   A 1 82  ? 34.875 -4.206  5.818   1.00 14.34 ?  82  VAL   A H    1 
ATOM   1653 H HA   . VAL   A 1 82  ? 32.695 -3.536  7.272   1.00 14.91 ?  82  VAL   A HA   1 
ATOM   1654 H HB   . VAL   A 1 82  ? 35.051 -4.820  8.183   1.00 17.07 ?  82  VAL   A HB   1 
ATOM   1655 H HG11 . VAL   A 1 82  ? 33.731 -5.269  10.137  1.00 18.90 ?  82  VAL   A HG11 1 
ATOM   1656 H HG12 . VAL   A 1 82  ? 34.188 -3.757  9.979   1.00 18.90 ?  82  VAL   A HG12 1 
ATOM   1657 H HG13 . VAL   A 1 82  ? 32.705 -4.185  9.596   1.00 18.90 ?  82  VAL   A HG13 1 
ATOM   1658 H HG21 . VAL   A 1 82  ? 33.760 -6.775  8.342   1.00 18.12 ?  82  VAL   A HG21 1 
ATOM   1659 H HG22 . VAL   A 1 82  ? 32.548 -6.011  7.655   1.00 18.12 ?  82  VAL   A HG22 1 
ATOM   1660 H HG23 . VAL   A 1 82  ? 33.880 -6.288  6.835   1.00 18.12 ?  82  VAL   A HG23 1 
ATOM   1661 N N    . LEU   A 1 83  ? 33.405 -1.377  8.144   1.00 12.12 ?  83  LEU   A N    1 
ATOM   1662 C CA   . LEU   A 1 83  ? 33.825 -0.110  8.725   1.00 12.17 ?  83  LEU   A CA   1 
ATOM   1663 C C    . LEU   A 1 83  ? 33.106 0.072   10.059  1.00 12.39 ?  83  LEU   A C    1 
ATOM   1664 O O    . LEU   A 1 83  ? 32.387 -0.819  10.527  1.00 12.75 ?  83  LEU   A O    1 
ATOM   1665 C CB   . LEU   A 1 83  ? 33.574 1.051   7.749   1.00 12.74 ?  83  LEU   A CB   1 
ATOM   1666 C CG   . LEU   A 1 83  ? 34.469 1.048   6.505   1.00 13.59 ?  83  LEU   A CG   1 
ATOM   1667 C CD1  . LEU   A 1 83  ? 34.032 2.096   5.503   1.00 13.73 ?  83  LEU   A CD1  1 
ATOM   1668 C CD2  . LEU   A 1 83  ? 35.939 1.263   6.884   1.00 14.32 ?  83  LEU   A CD2  1 
ATOM   1669 H H    . LEU   A 1 83  ? 32.551 -1.466  8.102   1.00 14.55 ?  83  LEU   A H    1 
ATOM   1670 H HA   . LEU   A 1 83  ? 34.774 -0.140  8.906   1.00 14.61 ?  83  LEU   A HA   1 
ATOM   1671 H HB2  . LEU   A 1 83  ? 32.654 1.013   7.442   1.00 15.29 ?  83  LEU   A HB2  1 
ATOM   1672 H HB3  . LEU   A 1 83  ? 33.724 1.891   8.212   1.00 15.29 ?  83  LEU   A HB3  1 
ATOM   1673 H HG   . LEU   A 1 83  ? 34.405 0.182   6.076   1.00 16.31 ?  83  LEU   A HG   1 
ATOM   1674 H HD11 . LEU   A 1 83  ? 34.621 2.057   4.729   1.00 16.48 ?  83  LEU   A HD11 1 
ATOM   1675 H HD12 . LEU   A 1 83  ? 33.121 1.910   5.232   1.00 16.48 ?  83  LEU   A HD12 1 
ATOM   1676 H HD13 . LEU   A 1 83  ? 34.088 2.971   5.915   1.00 16.48 ?  83  LEU   A HD13 1 
ATOM   1677 H HD21 . LEU   A 1 83  ? 36.458 1.411   6.074   1.00 17.19 ?  83  LEU   A HD21 1 
ATOM   1678 H HD22 . LEU   A 1 83  ? 36.009 2.041   7.461   1.00 17.19 ?  83  LEU   A HD22 1 
ATOM   1679 H HD23 . LEU   A 1 83  ? 36.270 0.478   7.347   1.00 17.19 ?  83  LEU   A HD23 1 
ATOM   1680 N N    . SER   A 1 84  ? 33.321 1.222   10.693  1.00 12.89 ?  84  SER   A N    1 
ATOM   1681 C CA   . SER   A 1 84  ? 32.682 1.482   11.973  1.00 13.00 ?  84  SER   A CA   1 
ATOM   1682 C C    . SER   A 1 84  ? 31.163 1.563   11.826  1.00 12.94 ?  84  SER   A C    1 
ATOM   1683 O O    . SER   A 1 84  ? 30.640 2.024   10.813  1.00 13.23 ?  84  SER   A O    1 
ATOM   1684 C CB   . SER   A 1 84  ? 33.191 2.800   12.549  1.00 14.19 ?  84  SER   A CB   1 
ATOM   1685 O OG   . SER   A 1 84  ? 32.542 3.081   13.775  1.00 14.96 ?  84  SER   A OG   1 
ATOM   1686 H H    . SER   A 1 84  ? 33.820 1.864   10.399  1.00 15.47 ?  84  SER   A H    1 
ATOM   1687 H HA   . SER   A 1 84  ? 32.899 0.767   12.586  1.00 15.60 ?  84  SER   A HA   1 
ATOM   1688 H HB2  . SER   A 1 84  ? 34.148 2.732   12.696  1.00 17.03 ?  84  SER   A HB2  1 
ATOM   1689 H HB3  . SER   A 1 84  ? 33.003 3.515   11.918  1.00 17.03 ?  84  SER   A HB3  1 
ATOM   1690 H HG   . SER   A 1 84  ? 32.831 3.804   14.088  1.00 17.95 ?  84  SER   A HG   1 
ATOM   1691 N N    . GLY   A 1 85  ? 30.450 1.151   12.873  1.00 13.89 ?  85  GLY   A N    1 
ATOM   1692 C CA   . GLY   A 1 85  ? 29.026 1.389   12.954  1.00 14.41 ?  85  GLY   A CA   1 
ATOM   1693 C C    . GLY   A 1 85  ? 28.656 2.693   13.620  1.00 14.15 ?  85  GLY   A C    1 
ATOM   1694 O O    . GLY   A 1 85  ? 27.465 3.003   13.737  1.00 14.86 ?  85  GLY   A O    1 
ATOM   1695 H H    . GLY   A 1 85  ? 30.779 0.730   13.545  1.00 16.66 ?  85  GLY   A H    1 
ATOM   1696 H HA2  . GLY   A 1 85  ? 28.656 1.386   12.052  1.00 17.29 ?  85  GLY   A HA2  1 
ATOM   1697 H HA3  . GLY   A 1 85  ? 28.614 0.672   13.448  1.00 17.29 ?  85  GLY   A HA3  1 
ATOM   1698 N N    . HIS   A 1 86  ? 29.645 3.465   14.062  1.00 13.66 ?  86  HIS   A N    1 
ATOM   1699 C CA   . HIS   A 1 86  ? 29.429 4.805   14.625  1.00 14.20 ?  86  HIS   A CA   1 
ATOM   1700 C C    . HIS   A 1 86  ? 28.450 4.689   15.786  1.00 15.26 ?  86  HIS   A C    1 
ATOM   1701 O O    . HIS   A 1 86  ? 28.642 3.815   16.648  1.00 16.51 ?  86  HIS   A O    1 
ATOM   1702 C CB   . HIS   A 1 86  ? 29.058 5.792   13.527  1.00 14.38 ?  86  HIS   A CB   1 
ATOM   1703 C CG   . HIS   A 1 86  ? 30.110 5.890   12.484  1.00 14.49 ?  86  HIS   A CG   1 
ATOM   1704 N ND1  . HIS   A 1 86  ? 31.198 6.728   12.608  1.00 15.46 ?  86  HIS   A ND1  1 
ATOM   1705 C CD2  . HIS   A 1 86  ? 30.288 5.197   11.338  1.00 14.19 ?  86  HIS   A CD2  1 
ATOM   1706 C CE1  . HIS   A 1 86  ? 31.986 6.564   11.561  1.00 15.08 ?  86  HIS   A CE1  1 
ATOM   1707 N NE2  . HIS   A 1 86  ? 31.462 5.636   10.782  1.00 14.46 ?  86  HIS   A NE2  1 
ATOM   1708 H H    . HIS   A 1 86  ? 30.466 3.233   14.058  1.00 16.40 ?  86  HIS   A H    1 
ATOM   1709 H HA   . HIS   A 1 86  ? 30.268 5.112   14.995  1.00 17.04 ?  86  HIS   A HA   1 
ATOM   1710 H HB2  . HIS   A 1 86  ? 28.234 5.510   13.100  1.00 17.25 ?  86  HIS   A HB2  1 
ATOM   1711 H HB3  . HIS   A 1 86  ? 28.940 6.679   13.915  1.00 17.25 ?  86  HIS   A HB3  1 
ATOM   1712 H HD2  . HIS   A 1 86  ? 29.726 4.537   10.992  1.00 17.03 ?  86  HIS   A HD2  1 
ATOM   1713 H HE1  . HIS   A 1 86  ? 32.776 7.025   11.388  1.00 18.10 ?  86  HIS   A HE1  1 
ATOM   1714 H HE2  . HIS   A 1 86  ? 31.795 5.358   10.032  1.00 17.35 ?  86  HIS   A HE2  1 
ATOM   1715 N N    . ASN   A 1 87  ? 27.434 5.539   15.858  1.00 16.49 ?  87  ASN   A N    1 
ATOM   1716 C CA   . ASN   A 1 87  ? 26.454 5.523   16.927  1.00 17.50 ?  87  ASN   A CA   1 
ATOM   1717 C C    . ASN   A 1 87  ? 25.336 4.521   16.690  1.00 18.78 ?  87  ASN   A C    1 
ATOM   1718 O O    . ASN   A 1 87  ? 24.417 4.452   17.511  1.00 20.97 ?  87  ASN   A O    1 
ATOM   1719 C CB   . ASN   A 1 87  ? 25.856 6.927   17.088  1.00 18.34 ?  87  ASN   A CB   1 
ATOM   1720 C CG   . ASN   A 1 87  ? 25.343 7.502   15.773  1.00 18.88 ?  87  ASN   A CG   1 
ATOM   1721 O OD1  . ASN   A 1 87  ? 25.993 7.397   14.733  1.00 19.58 ?  87  ASN   A OD1  1 
ATOM   1722 N ND2  . ASN   A 1 87  ? 24.173 8.118   15.818  1.00 19.96 ?  87  ASN   A ND2  1 
ATOM   1723 H H    . ASN   A 1 87  ? 27.288 6.154   15.278  1.00 19.79 ?  87  ASN   A H    1 
ATOM   1724 H HA   . ASN   A 1 87  ? 26.889 5.287   17.762  1.00 21.00 ?  87  ASN   A HA   1 
ATOM   1725 H HB2  . ASN   A 1 87  ? 25.111 6.884   17.715  1.00 22.01 ?  87  ASN   A HB2  1 
ATOM   1726 H HB3  . ASN   A 1 87  ? 26.539 7.523   17.432  1.00 22.01 ?  87  ASN   A HB3  1 
ATOM   1727 H HD21 . ASN   A 1 87  ? 23.842 8.453   15.102  1.00 23.96 ?  87  ASN   A HD21 1 
ATOM   1728 H HD22 . ASN   A 1 87  ? 23.745 8.180   16.563  1.00 23.96 ?  87  ASN   A HD22 1 
ATOM   1729 N N    . LEU   A 1 88  ? 25.391 3.741   15.612  1.00 17.75 ?  88  LEU   A N    1 
ATOM   1730 C CA   . LEU   A 1 88  ? 24.278 2.877   15.226  1.00 17.64 ?  88  LEU   A CA   1 
ATOM   1731 C C    . LEU   A 1 88  ? 24.497 1.401   15.525  1.00 17.09 ?  88  LEU   A C    1 
ATOM   1732 O O    . LEU   A 1 88  ? 23.519 0.673   15.717  1.00 18.40 ?  88  LEU   A O    1 
ATOM   1733 C CB   . LEU   A 1 88  ? 24.004 3.028   13.728  1.00 18.48 ?  88  LEU   A CB   1 
ATOM   1734 C CG   . LEU   A 1 88  ? 23.707 4.447   13.245  1.00 19.87 ?  88  LEU   A CG   1 
ATOM   1735 C CD1  . LEU   A 1 88  ? 23.545 4.461   11.740  1.00 20.10 ?  88  LEU   A CD1  1 
ATOM   1736 C CD2  . LEU   A 1 88  ? 22.468 5.017   13.928  1.00 21.61 ?  88  LEU   A CD2  1 
ATOM   1737 H H    . LEU   A 1 88  ? 26.067 3.699   15.085  1.00 21.30 ?  88  LEU   A H    1 
ATOM   1738 H HA   . LEU   A 1 88  ? 23.485 3.162   15.702  1.00 21.17 ?  88  LEU   A HA   1 
ATOM   1739 H HB2  . LEU   A 1 88  ? 24.775 2.712   13.237  1.00 22.18 ?  88  LEU   A HB2  1 
ATOM   1740 H HB3  . LEU   A 1 88  ? 23.231 2.483   13.504  1.00 22.18 ?  88  LEU   A HB3  1 
ATOM   1741 H HG   . LEU   A 1 88  ? 24.458 5.018   13.466  1.00 23.84 ?  88  LEU   A HG   1 
ATOM   1742 H HD11 . LEU   A 1 88  ? 23.363 5.371   11.450  1.00 24.12 ?  88  LEU   A HD11 1 
ATOM   1743 H HD12 . LEU   A 1 88  ? 24.366 4.144   11.331  1.00 24.12 ?  88  LEU   A HD12 1 
ATOM   1744 H HD13 . LEU   A 1 88  ? 22.808 3.883   11.497  1.00 24.12 ?  88  LEU   A HD13 1 
ATOM   1745 H HD21 . LEU   A 1 88  ? 22.252 5.872   13.523  1.00 25.93 ?  88  LEU   A HD21 1 
ATOM   1746 H HD22 . LEU   A 1 88  ? 21.733 4.398   13.811  1.00 25.93 ?  88  LEU   A HD22 1 
ATOM   1747 H HD23 . LEU   A 1 88  ? 22.659 5.135   14.871  1.00 25.93 ?  88  LEU   A HD23 1 
ATOM   1748 N N    . ALA   A 1 89  ? 25.746 0.948   15.544  1.00 16.14 ?  89  ALA   A N    1 
ATOM   1749 C CA   . ALA   A 1 89  ? 26.086 -0.463  15.652  1.00 15.73 ?  89  ALA   A CA   1 
ATOM   1750 C C    . ALA   A 1 89  ? 27.571 -0.522  15.965  1.00 16.23 ?  89  ALA   A C    1 
ATOM   1751 O O    . ALA   A 1 89  ? 28.278 0.481   15.857  1.00 17.09 ?  89  ALA   A O    1 
ATOM   1752 C CB   . ALA   A 1 89  ? 25.804 -1.182  14.334  1.00 15.01 ?  89  ALA   A CB   1 
ATOM   1753 H H    . ALA   A 1 89  ? 26.434 1.459   15.485  1.00 19.37 ?  89  ALA   A H    1 
ATOM   1754 H HA   . ALA   A 1 89  ? 25.578 -0.878  16.369  1.00 18.88 ?  89  ALA   A HA   1 
ATOM   1755 H HB1  . ALA   A 1 89  ? 26.056 -2.115  14.424  1.00 18.01 ?  89  ALA   A HB1  1 
ATOM   1756 H HB2  . ALA   A 1 89  ? 24.856 -1.117  14.130  1.00 18.01 ?  89  ALA   A HB2  1 
ATOM   1757 H HB3  . ALA   A 1 89  ? 26.323 -0.767  13.629  1.00 18.01 ?  89  ALA   A HB3  1 
ATOM   1758 N N    . LYS   A 1 90  ? 28.053 -1.703  16.342  1.00 16.88 ?  90  LYS   A N    1 
ATOM   1759 C CA   . LYS   A 1 90  ? 29.496 -1.852  16.486  1.00 17.45 ?  90  LYS   A CA   1 
ATOM   1760 C C    . LYS   A 1 90  ? 30.191 -1.658  15.141  1.00 16.01 ?  90  LYS   A C    1 
ATOM   1761 O O    . LYS   A 1 90  ? 31.125 -0.849  15.015  1.00 17.72 ?  90  LYS   A O    1 
ATOM   1762 C CB   . LYS   A 1 90  ? 29.833 -3.214  17.095  1.00 20.20 ?  90  LYS   A CB   1 
ATOM   1763 C CG   . LYS   A 1 90  ? 31.315 -3.384  17.398  1.00 25.14 ?  90  LYS   A CG   1 
ATOM   1764 C CD   . LYS   A 1 90  ? 31.561 -4.599  18.279  1.00 29.60 ?  90  LYS   A CD   1 
ATOM   1765 C CE   . LYS   A 1 90  ? 32.980 -4.622  18.830  1.00 32.30 ?  90  LYS   A CE   1 
ATOM   1766 N NZ   . LYS   A 1 90  ? 33.984 -5.074  17.829  1.00 35.25 ?  90  LYS   A NZ   1 
ATOM   1767 H H    . LYS   A 1 90  ? 27.582 -2.402  16.508  1.00 20.25 ?  90  LYS   A H    1 
ATOM   1768 H HA   . LYS   A 1 90  ? 29.820 -1.168  17.088  1.00 20.94 ?  90  LYS   A HA   1 
ATOM   1769 H HB2  . LYS   A 1 90  ? 29.341 -3.315  17.928  1.00 24.24 ?  90  LYS   A HB2  1 
ATOM   1770 H HB3  . LYS   A 1 90  ? 29.570 -3.912  16.474  1.00 24.24 ?  90  LYS   A HB3  1 
ATOM   1771 H HG2  . LYS   A 1 90  ? 31.800 -3.505  16.567  1.00 30.16 ?  90  LYS   A HG2  1 
ATOM   1772 H HG3  . LYS   A 1 90  ? 31.638 -2.597  17.865  1.00 30.16 ?  90  LYS   A HG3  1 
ATOM   1773 H HD2  . LYS   A 1 90  ? 30.944 -4.580  19.029  1.00 35.52 ?  90  LYS   A HD2  1 
ATOM   1774 H HD3  . LYS   A 1 90  ? 31.424 -5.405  17.756  1.00 35.52 ?  90  LYS   A HD3  1 
ATOM   1775 H HE2  . LYS   A 1 90  ? 33.223 -3.727  19.114  1.00 38.76 ?  90  LYS   A HE2  1 
ATOM   1776 H HE3  . LYS   A 1 90  ? 33.015 -5.230  19.585  1.00 38.76 ?  90  LYS   A HE3  1 
ATOM   1777 H HZ1  . LYS   A 1 90  ? 33.781 -5.892  17.542  1.00 42.30 ?  90  LYS   A HZ1  1 
ATOM   1778 H HZ2  . LYS   A 1 90  ? 33.994 -4.518  17.135  1.00 42.30 ?  90  LYS   A HZ2  1 
ATOM   1779 H HZ3  . LYS   A 1 90  ? 34.795 -5.091  18.197  1.00 42.30 ?  90  LYS   A HZ3  1 
ATOM   1780 N N    . HIS   A 1 91  ? 29.722 -2.372  14.119  1.00 14.50 ?  91  HIS   A N    1 
ATOM   1781 C CA   . HIS   A 1 91  ? 30.297 -2.351  12.789  1.00 13.88 ?  91  HIS   A CA   1 
ATOM   1782 C C    . HIS   A 1 91  ? 29.207 -2.076  11.772  1.00 12.69 ?  91  HIS   A C    1 
ATOM   1783 O O    . HIS   A 1 91  ? 28.041 -2.445  11.967  1.00 13.31 ?  91  HIS   A O    1 
ATOM   1784 C CB   . HIS   A 1 91  ? 30.885 -3.722  12.419  1.00 16.85 ?  91  HIS   A CB   1 
ATOM   1785 C CG   . HIS   A 1 91  ? 31.899 -4.234  13.391  1.00 21.38 ?  91  HIS   A CG   1 
ATOM   1786 N ND1  . HIS   A 1 91  ? 33.177 -3.724  13.473  1.00 23.44 ?  91  HIS   A ND1  1 
ATOM   1787 C CD2  . HIS   A 1 91  ? 31.829 -5.223  14.314  1.00 23.15 ?  91  HIS   A CD2  1 
ATOM   1788 C CE1  . HIS   A 1 91  ? 33.849 -4.372  14.409  1.00 24.51 ?  91  HIS   A CE1  1 
ATOM   1789 N NE2  . HIS   A 1 91  ? 33.052 -5.288  14.934  1.00 24.53 ?  91  HIS   A NE2  1 
ATOM   1790 H H    . HIS   A 1 91  ? 29.045 -2.909  14.185  1.00 17.41 ?  91  HIS   A H    1 
ATOM   1791 H HA   . HIS   A 1 91  ? 30.986 -1.676  12.725  1.00 16.66 ?  91  HIS   A HA   1 
ATOM   1792 H HB2  . HIS   A 1 91  ? 30.164 -4.372  12.379  1.00 20.22 ?  91  HIS   A HB2  1 
ATOM   1793 H HB3  . HIS   A 1 91  ? 31.312 -3.655  11.552  1.00 20.22 ?  91  HIS   A HB3  1 
ATOM   1794 H HD1  . HIS   A 1 91  ? 33.489 -3.082  12.987  1.00 28.12 ?  91  HIS   A HD1  1 
ATOM   1795 H HD2  . HIS   A 1 91  ? 31.096 -5.756  14.498  1.00 27.78 ?  91  HIS   A HD2  1 
ATOM   1796 H HE1  . HIS   A 1 91  ? 34.735 -4.206  14.652  1.00 29.41 ?  91  HIS   A HE1  1 
ATOM   1797 N N    . CYS   A 1 92  ? 29.608 -1.480  10.654  1.00 11.85 ?  92  CYS   A N    1 
ATOM   1798 C CA   . CYS   A 1 92  ? 28.766 -1.409  9.469   1.00 12.00 ?  92  CYS   A CA   1 
ATOM   1799 C C    . CYS   A 1 92  ? 29.414 -2.218  8.357   1.00 11.81 ?  92  CYS   A C    1 
ATOM   1800 O O    . CYS   A 1 92  ? 30.570 -1.965  7.990   1.00 12.30 ?  92  CYS   A O    1 
ATOM   1801 C CB   . CYS   A 1 92  ? 28.542 0.031   9.012   1.00 12.64 ?  92  CYS   A CB   1 
ATOM   1802 S SG   . CYS   A 1 92  ? 27.539 0.147   7.507   1.00 11.68 ?  92  CYS   A SG   1 
ATOM   1803 H H    . CYS   A 1 92  ? 30.375 -1.097  10.557  1.00 14.23 ?  92  CYS   A H    1 
ATOM   1804 H HA   . CYS   A 1 92  ? 27.901 -1.797  9.668   1.00 14.40 ?  92  CYS   A HA   1 
ATOM   1805 H HB2  . CYS   A 1 92  ? 28.086 0.522   9.715   1.00 15.17 ?  92  CYS   A HB2  1 
ATOM   1806 H HB3  . CYS   A 1 92  ? 29.401 0.443   8.827   1.00 15.17 ?  92  CYS   A HB3  1 
ATOM   1807 H HG   . CYS   A 1 92  ? 27.396 1.303   7.225   1.00 14.02 ?  92  CYS   A HG   1 
ATOM   1808 N N    . LEU   A 1 93  ? 28.685 -3.207  7.855   1.00 11.53 ?  93  LEU   A N    1 
ATOM   1809 C CA   . LEU   A 1 93  ? 29.083 -3.963  6.675   1.00 10.88 ?  93  LEU   A CA   1 
ATOM   1810 C C    . LEU   A 1 93  ? 28.480 -3.274  5.458   1.00 10.61 ?  93  LEU   A C    1 
ATOM   1811 O O    . LEU   A 1 93  ? 27.262 -3.336  5.239   1.00 10.71 ?  93  LEU   A O    1 
ATOM   1812 C CB   . LEU   A 1 93  ? 28.602 -5.412  6.787   1.00 11.65 ?  93  LEU   A CB   1 
ATOM   1813 C CG   . LEU   A 1 93  ? 28.986 -6.302  5.609   1.00 11.77 ?  93  LEU   A CG   1 
ATOM   1814 C CD1  . LEU   A 1 93  ? 30.504 -6.560  5.597   1.00 12.84 ?  93  LEU   A CD1  1 
ATOM   1815 C CD2  . LEU   A 1 93  ? 28.216 -7.626  5.622   1.00 12.41 ?  93  LEU   A CD2  1 
ATOM   1816 H H    . LEU   A 1 93  ? 27.934 -3.462  8.198   1.00 13.83 ?  93  LEU   A H    1 
ATOM   1817 H HA   . LEU   A 1 93  ? 30.043 -3.953  6.596   1.00 13.06 ?  93  LEU   A HA   1 
ATOM   1818 H HB2  . LEU   A 1 93  ? 28.987 -5.801  7.592   1.00 13.98 ?  93  LEU   A HB2  1 
ATOM   1819 H HB3  . LEU   A 1 93  ? 27.636 -5.417  6.856   1.00 13.98 ?  93  LEU   A HB3  1 
ATOM   1820 H HG   . LEU   A 1 93  ? 28.773 -5.842  4.787   1.00 14.13 ?  93  LEU   A HG   1 
ATOM   1821 H HD11 . LEU   A 1 93  ? 30.719 -7.169  4.875   1.00 15.40 ?  93  LEU   A HD11 1 
ATOM   1822 H HD12 . LEU   A 1 93  ? 30.972 -5.719  5.473   1.00 15.40 ?  93  LEU   A HD12 1 
ATOM   1823 H HD13 . LEU   A 1 93  ? 30.766 -6.957  6.448   1.00 15.40 ?  93  LEU   A HD13 1 
ATOM   1824 H HD21 . LEU   A 1 93  ? 28.495 -8.158  4.857   1.00 14.89 ?  93  LEU   A HD21 1 
ATOM   1825 H HD22 . LEU   A 1 93  ? 28.412 -8.099  6.443   1.00 14.89 ?  93  LEU   A HD22 1 
ATOM   1826 H HD23 . LEU   A 1 93  ? 27.269 -7.434  5.562   1.00 14.89 ?  93  LEU   A HD23 1 
ATOM   1827 N N    . HIS   A 1 94  ? 29.322 -2.575  4.698   1.00 10.19 ?  94  HIS   A N    1 
ATOM   1828 C CA   . HIS   A 1 94  ? 28.898 -1.899  3.477   1.00 10.24 ?  94  HIS   A CA   1 
ATOM   1829 C C    . HIS   A 1 94  ? 28.908 -2.932  2.366   1.00 10.53 ?  94  HIS   A C    1 
ATOM   1830 O O    . HIS   A 1 94  ? 29.976 -3.452  2.023   1.00 11.78 ?  94  HIS   A O    1 
ATOM   1831 C CB   . HIS   A 1 94  ? 29.852 -0.752  3.145   1.00 10.58 ?  94  HIS   A CB   1 
ATOM   1832 C CG   . HIS   A 1 94  ? 29.847 0.340   4.160   1.00 10.33 ?  94  HIS   A CG   1 
ATOM   1833 N ND1  . HIS   A 1 94  ? 28.968 1.397   4.107   1.00 10.72 ?  94  HIS   A ND1  1 
ATOM   1834 C CD2  . HIS   A 1 94  ? 30.587 0.513   5.278   1.00 11.20 ?  94  HIS   A CD2  1 
ATOM   1835 C CE1  . HIS   A 1 94  ? 29.182 2.180   5.148   1.00 10.68 ?  94  HIS   A CE1  1 
ATOM   1836 N NE2  . HIS   A 1 94  ? 30.158 1.668   5.874   1.00 11.05 ?  94  HIS   A NE2  1 
ATOM   1837 H H    . HIS   A 1 94  ? 30.158 -2.476  4.873   1.00 12.22 ?  94  HIS   A H    1 
ATOM   1838 H HA   . HIS   A 1 94  ? 27.995 -1.549  3.583   1.00 12.28 ?  94  HIS   A HA   1 
ATOM   1839 H HB2  . HIS   A 1 94  ? 30.748 -1.101  3.090   1.00 12.70 ?  94  HIS   A HB2  1 
ATOM   1840 H HB3  . HIS   A 1 94  ? 29.587 -0.365  2.295   1.00 12.70 ?  94  HIS   A HB3  1 
ATOM   1841 H HD2  . HIS   A 1 94  ? 31.262 -0.041  5.582   1.00 13.44 ?  94  HIS   A HD2  1 
ATOM   1842 H HE1  . HIS   A 1 94  ? 28.710 2.965   5.335   1.00 12.82 ?  94  HIS   A HE1  1 
ATOM   1843 H HE2  . HIS   A 1 94  ? 30.471 2.014   6.594   1.00 13.26 ?  94  HIS   A HE2  1 
ATOM   1844 N N    . VAL   A 1 95  ? 27.733 -3.257  1.821   1.00 9.83  ?  95  VAL   A N    1 
ATOM   1845 C CA   . VAL   A 1 95  ? 27.596 -4.287  0.796   1.00 10.19 ?  95  VAL   A CA   1 
ATOM   1846 C C    . VAL   A 1 95  ? 27.045 -3.653  -0.468  1.00 9.86  ?  95  VAL   A C    1 
ATOM   1847 O O    . VAL   A 1 95  ? 26.043 -2.930  -0.418  1.00 10.63 ?  95  VAL   A O    1 
ATOM   1848 C CB   . VAL   A 1 95  ? 26.681 -5.439  1.249   1.00 10.95 ?  95  VAL   A CB   1 
ATOM   1849 C CG1  . VAL   A 1 95  ? 26.593 -6.484  0.153   1.00 11.79 ?  95  VAL   A CG1  1 
ATOM   1850 C CG2  . VAL   A 1 95  ? 27.177 -6.045  2.544   1.00 11.25 ?  95  VAL   A CG2  1 
ATOM   1851 H H    . VAL   A 1 95  ? 26.982 -2.886  2.031   1.00 11.80 ?  95  VAL   A H    1 
ATOM   1852 H HA   . VAL   A 1 95  ? 28.466 -4.656  0.593   1.00 12.23 ?  95  VAL   A HA   1 
ATOM   1853 H HB   . VAL   A 1 95  ? 25.790 -5.096  1.401   1.00 13.14 ?  95  VAL   A HB   1 
ATOM   1854 H HG11 . VAL   A 1 95  ? 26.208 -7.299  0.520   1.00 14.14 ?  95  VAL   A HG11 1 
ATOM   1855 H HG12 . VAL   A 1 95  ? 26.034 -6.155  -0.566  1.00 14.14 ?  95  VAL   A HG12 1 
ATOM   1856 H HG13 . VAL   A 1 95  ? 27.487 -6.674  -0.182  1.00 14.14 ?  95  VAL   A HG13 1 
ATOM   1857 H HG21 . VAL   A 1 95  ? 26.620 -6.807  2.768   1.00 13.50 ?  95  VAL   A HG21 1 
ATOM   1858 H HG22 . VAL   A 1 95  ? 28.096 -6.324  2.432   1.00 13.50 ?  95  VAL   A HG22 1 
ATOM   1859 H HG23 . VAL   A 1 95  ? 27.114 -5.375  3.244   1.00 13.50 ?  95  VAL   A HG23 1 
ATOM   1860 N N    . VAL   A 1 96  ? 27.677 -3.941  -1.602  1.00 9.84  ?  96  VAL   A N    1 
ATOM   1861 C CA   . VAL   A 1 96  ? 27.268 -3.384  -2.887  1.00 10.54 ?  96  VAL   A CA   1 
ATOM   1862 C C    . VAL   A 1 96  ? 26.465 -4.433  -3.646  1.00 11.16 ?  96  VAL   A C    1 
ATOM   1863 O O    . VAL   A 1 96  ? 27.023 -5.371  -4.220  1.00 11.84 ?  96  VAL   A O    1 
ATOM   1864 C CB   . VAL   A 1 96  ? 28.462 -2.904  -3.712  1.00 11.28 ?  96  VAL   A CB   1 
ATOM   1865 C CG1  . VAL   A 1 96  ? 27.953 -2.278  -4.990  1.00 11.42 ?  96  VAL   A CG1  1 
ATOM   1866 C CG2  . VAL   A 1 96  ? 29.319 -1.935  -2.920  1.00 12.12 ?  96  VAL   A CG2  1 
ATOM   1867 H H    . VAL   A 1 96  ? 28.367 -4.459  -1.652  1.00 11.81 ?  96  VAL   A H    1 
ATOM   1868 H HA   . VAL   A 1 96  ? 26.693 -2.621  -2.728  1.00 12.65 ?  96  VAL   A HA   1 
ATOM   1869 H HB   . VAL   A 1 96  ? 29.012 -3.667  -3.949  1.00 13.54 ?  96  VAL   A HB   1 
ATOM   1870 H HG11 . VAL   A 1 96  ? 28.686 -1.795  -5.410  1.00 13.71 ?  96  VAL   A HG11 1 
ATOM   1871 H HG12 . VAL   A 1 96  ? 27.635 -2.971  -5.582  1.00 13.71 ?  96  VAL   A HG12 1 
ATOM   1872 H HG13 . VAL   A 1 96  ? 27.238 -1.660  -4.775  1.00 13.71 ?  96  VAL   A HG13 1 
ATOM   1873 H HG21 . VAL   A 1 96  ? 30.024 -1.592  -3.491  1.00 14.55 ?  96  VAL   A HG21 1 
ATOM   1874 H HG22 . VAL   A 1 96  ? 28.763 -1.202  -2.606  1.00 14.55 ?  96  VAL   A HG22 1 
ATOM   1875 H HG23 . VAL   A 1 96  ? 29.707 -2.399  -2.160  1.00 14.55 ?  96  VAL   A HG23 1 
ATOM   1876 N N    . GLY   A 1 97  ? 25.147 -4.275  -3.676  1.00 11.13 ?  97  GLY   A N    1 
ATOM   1877 C CA   . GLY   A 1 97  ? 24.332 -5.033  -4.589  1.00 11.93 ?  97  GLY   A CA   1 
ATOM   1878 C C    . GLY   A 1 97  ? 24.333 -4.382  -5.956  1.00 12.01 ?  97  GLY   A C    1 
ATOM   1879 O O    . GLY   A 1 97  ? 24.608 -3.187  -6.094  1.00 12.82 ?  97  GLY   A O    1 
ATOM   1880 H H    . GLY   A 1 97  ? 24.703 -3.731  -3.168  1.00 13.35 ?  97  GLY   A H    1 
ATOM   1881 H HA2  . GLY   A 1 97  ? 24.688 -5.931  -4.650  1.00 14.32 ?  97  GLY   A HA2  1 
ATOM   1882 H HA3  . GLY   A 1 97  ? 23.421 -5.078  -4.257  1.00 14.32 ?  97  GLY   A HA3  1 
ATOM   1883 N N    A PRO   A 1 98  ? 23.996 -5.131  -7.001  0.76 11.70 ?  98  PRO   A N    1 
ATOM   1884 N N    B PRO   A 1 98  ? 24.049 -5.169  -6.992  0.24 12.53 ?  98  PRO   A N    1 
ATOM   1885 C CA   A PRO   A 1 98  ? 23.865 -4.510  -8.326  0.76 13.19 ?  98  PRO   A CA   1 
ATOM   1886 C CA   B PRO   A 1 98  ? 24.008 -4.617  -8.348  0.24 13.40 ?  98  PRO   A CA   1 
ATOM   1887 C C    A PRO   A 1 98  ? 22.750 -3.473  -8.353  0.76 13.31 ?  98  PRO   A C    1 
ATOM   1888 C C    B PRO   A 1 98  ? 22.885 -3.605  -8.499  0.24 13.93 ?  98  PRO   A C    1 
ATOM   1889 O O    A PRO   A 1 98  ? 21.673 -3.668  -7.787  0.76 13.21 ?  98  PRO   A O    1 
ATOM   1890 O O    B PRO   A 1 98  ? 21.810 -3.735  -7.907  0.24 14.15 ?  98  PRO   A O    1 
ATOM   1891 C CB   A PRO   A 1 98  ? 23.552 -5.697  -9.245  0.76 13.66 ?  98  PRO   A CB   1 
ATOM   1892 C CB   B PRO   A 1 98  ? 23.764 -5.851  -9.225  0.24 13.34 ?  98  PRO   A CB   1 
ATOM   1893 C CG   A PRO   A 1 98  ? 22.952 -6.730  -8.341  0.76 13.35 ?  98  PRO   A CG   1 
ATOM   1894 C CG   B PRO   A 1 98  ? 23.108 -6.836  -8.310  0.24 13.32 ?  98  PRO   A CG   1 
ATOM   1895 C CD   A PRO   A 1 98  ? 23.678 -6.570  -7.027  0.76 12.31 ?  98  PRO   A CD   1 
ATOM   1896 C CD   B PRO   A 1 98  ? 23.755 -6.613  -6.975  0.24 12.81 ?  98  PRO   A CD   1 
ATOM   1897 H HA   A PRO   A 1 98  ? 24.701 -4.096  -8.585  0.76 15.83 ?  98  PRO   A HA   1 
ATOM   1898 H HA   B PRO   A 1 98  ? 24.858 -4.207  -8.577  0.24 16.08 ?  98  PRO   A HA   1 
ATOM   1899 H HB2  A PRO   A 1 98  ? 22.917 -5.418  -9.923  0.76 16.39 ?  98  PRO   A HB2  1 
ATOM   1900 H HB2  B PRO   A 1 98  ? 23.176 -5.615  -9.959  0.24 16.01 ?  98  PRO   A HB2  1 
ATOM   1901 H HB3  A PRO   A 1 98  ? 24.371 -6.017  -9.647  0.76 16.39 ?  98  PRO   A HB3  1 
ATOM   1902 H HB3  B PRO   A 1 98  ? 24.610 -6.192  -9.552  0.24 16.01 ?  98  PRO   A HB3  1 
ATOM   1903 H HG2  A PRO   A 1 98  ? 22.004 -6.559  -8.233  0.76 16.02 ?  98  PRO   A HG2  1 
ATOM   1904 H HG2  B PRO   A 1 98  ? 22.156 -6.655  -8.264  0.24 15.98 ?  98  PRO   A HG2  1 
ATOM   1905 H HG3  A PRO   A 1 98  ? 23.105 -7.611  -8.712  0.76 16.02 ?  98  PRO   A HG3  1 
ATOM   1906 H HG3  B PRO   A 1 98  ? 23.274 -7.735  -8.627  0.24 15.98 ?  98  PRO   A HG3  1 
ATOM   1907 H HD2  A PRO   A 1 98  ? 23.097 -6.808  -6.286  0.76 14.77 ?  98  PRO   A HD2  1 
ATOM   1908 H HD2  B PRO   A 1 98  ? 23.139 -6.828  -6.257  0.24 15.37 ?  98  PRO   A HD2  1 
ATOM   1909 H HD3  A PRO   A 1 98  ? 24.495 -7.093  -7.021  0.76 14.77 ?  98  PRO   A HD3  1 
ATOM   1910 H HD3  B PRO   A 1 98  ? 24.577 -7.125  -6.904  0.24 15.37 ?  98  PRO   A HD3  1 
ATOM   1911 N N    A ASN   A 1 99  ? 23.024 -2.349  -9.018  0.76 14.23 ?  99  ASN   A N    1 
ATOM   1912 N N    B ASN   A 1 99  ? 23.150 -2.584  -9.304  0.24 14.64 ?  99  ASN   A N    1 
ATOM   1913 C CA   A ASN   A 1 99  ? 22.040 -1.289  -9.242  0.76 15.27 ?  99  ASN   A CA   1 
ATOM   1914 C CA   B ASN   A 1 99  ? 22.197 -1.517  -9.570  0.24 15.59 ?  99  ASN   A CA   1 
ATOM   1915 C C    A ASN   A 1 99  ? 21.513 -1.462  -10.664 0.76 16.40 ?  99  ASN   A C    1 
ATOM   1916 C C    B ASN   A 1 99  ? 21.481 -1.807  -10.884 0.24 16.70 ?  99  ASN   A C    1 
ATOM   1917 O O    A ASN   A 1 99  ? 22.203 -1.153  -11.641 0.76 17.73 ?  99  ASN   A O    1 
ATOM   1918 O O    B ASN   A 1 99  ? 22.125 -1.927  -11.933 0.24 16.03 ?  99  ASN   A O    1 
ATOM   1919 C CB   A ASN   A 1 99  ? 22.674 0.086   -9.038  0.76 15.62 ?  99  ASN   A CB   1 
ATOM   1920 C CB   B ASN   A 1 99  ? 22.926 -0.178  -9.653  0.24 16.03 ?  99  ASN   A CB   1 
ATOM   1921 C CG   A ASN   A 1 99  ? 21.647 1.225   -9.028  0.76 15.69 ?  99  ASN   A CG   1 
ATOM   1922 C CG   B ASN   A 1 99  ? 21.981 0.994   -9.791  0.24 16.41 ?  99  ASN   A CG   1 
ATOM   1923 O OD1  A ASN   A 1 99  ? 20.633 1.176   -9.726  0.76 16.55 ?  99  ASN   A OD1  1 
ATOM   1924 O OD1  B ASN   A 1 99  ? 20.942 0.892   -10.441 0.24 16.31 ?  99  ASN   A OD1  1 
ATOM   1925 N ND2  A ASN   A 1 99  ? 21.922 2.259   -8.238  0.76 16.23 ?  99  ASN   A ND2  1 
ATOM   1926 N ND2  B ASN   A 1 99  ? 22.337 2.119   -9.175  0.24 17.06 ?  99  ASN   A ND2  1 
ATOM   1927 H H    A ASN   A 1 99  ? 23.795 -2.169  -9.346  0.76 17.07 ?  99  ASN   A H    1 
ATOM   1928 H H    B ASN   A 1 99  ? 23.901 -2.480  -9.707  0.24 17.57 ?  99  ASN   A H    1 
ATOM   1929 H HA   A ASN   A 1 99  ? 21.304 -1.385  -8.610  0.76 18.33 ?  99  ASN   A HA   1 
ATOM   1930 H HA   B ASN   A 1 99  ? 21.541 -1.473  -8.853  0.24 18.71 ?  99  ASN   A HA   1 
ATOM   1931 H HB2  A ASN   A 1 99  ? 23.146 0.102   -8.192  0.76 18.75 ?  99  ASN   A HB2  1 
ATOM   1932 H HB2  B ASN   A 1 99  ? 23.453 -0.047  -8.850  0.24 19.24 ?  99  ASN   A HB2  1 
ATOM   1933 H HB3  A ASN   A 1 99  ? 23.300 0.251   -9.766  0.76 18.75 ?  99  ASN   A HB3  1 
ATOM   1934 H HB3  B ASN   A 1 99  ? 23.499 -0.191  -10.433 0.24 19.24 ?  99  ASN   A HB3  1 
ATOM   1935 H HD21 A ASN   A 1 99  ? 21.382 2.926   -8.199  0.76 19.47 ?  99  ASN   A HD21 1 
ATOM   1936 H HD21 B ASN   A 1 99  ? 21.836 2.818   -9.217  0.24 20.47 ?  99  ASN   A HD21 1 
ATOM   1937 H HD22 A ASN   A 1 99  ? 22.641 2.259   -7.764  0.76 19.47 ?  99  ASN   A HD22 1 
ATOM   1938 H HD22 B ASN   A 1 99  ? 23.074 2.148   -8.729  0.24 20.47 ?  99  ASN   A HD22 1 
ATOM   1939 N N    A VAL   A 1 100 ? 20.287 -1.983  -10.772 0.76 17.92 ?  100 VAL   A N    1 
ATOM   1940 N N    B VAL   A 1 100 ? 20.151 -1.906  -10.821 0.24 18.66 ?  100 VAL   A N    1 
ATOM   1941 C CA   A VAL   A 1 100 ? 19.677 -2.210  -12.078 0.76 20.73 ?  100 VAL   A CA   1 
ATOM   1942 C CA   B VAL   A 1 100 ? 19.361 -2.197  -12.015 0.24 20.87 ?  100 VAL   A CA   1 
ATOM   1943 C C    A VAL   A 1 100 ? 19.551 -0.905  -12.854 0.76 21.37 ?  100 VAL   A C    1 
ATOM   1944 C C    B VAL   A 1 100 ? 19.341 -1.003  -12.961 0.24 22.59 ?  100 VAL   A C    1 
ATOM   1945 O O    A VAL   A 1 100 ? 19.644 -0.894  -14.088 0.76 23.03 ?  100 VAL   A O    1 
ATOM   1946 O O    B VAL   A 1 100 ? 19.374 -1.168  -14.187 0.24 23.29 ?  100 VAL   A O    1 
ATOM   1947 C CB   A VAL   A 1 100 ? 18.327 -2.940  -11.908 0.76 22.31 ?  100 VAL   A CB   1 
ATOM   1948 C CB   B VAL   A 1 100 ? 17.943 -2.646  -11.624 0.24 21.23 ?  100 VAL   A CB   1 
ATOM   1949 C CG1  A VAL   A 1 100 ? 17.635 -3.148  -13.250 0.76 23.09 ?  100 VAL   A CG1  1 
ATOM   1950 C CG1  B VAL   A 1 100 ? 16.975 -2.435  -12.775 0.24 21.51 ?  100 VAL   A CG1  1 
ATOM   1951 C CG2  A VAL   A 1 100 ? 18.546 -4.272  -11.210 0.76 22.87 ?  100 VAL   A CG2  1 
ATOM   1952 C CG2  B VAL   A 1 100 ? 17.945 -4.097  -11.193 0.24 21.17 ?  100 VAL   A CG2  1 
ATOM   1953 H H    A VAL   A 1 100 ? 19.788 -2.215  -10.102 0.76 21.51 ?  100 VAL   A H    1 
ATOM   1954 H H    B VAL   A 1 100 ? 19.691 -1.818  -10.101 0.24 22.39 ?  100 VAL   A H    1 
ATOM   1955 H HA   A VAL   A 1 100 ? 20.256 -2.794  -12.587 0.76 24.88 ?  100 VAL   A HA   1 
ATOM   1956 H HA   B VAL   A 1 100 ? 19.780 -2.929  -12.485 0.24 25.04 ?  100 VAL   A HA   1 
ATOM   1957 H HB   A VAL   A 1 100 ? 17.743 -2.404  -11.350 0.76 26.78 ?  100 VAL   A HB   1 
ATOM   1958 H HB   B VAL   A 1 100 ? 17.650 -2.114  -10.876 0.24 25.47 ?  100 VAL   A HB   1 
ATOM   1959 H HG11 A VAL   A 1 100 ? 16.877 -3.743  -13.126 0.76 27.71 ?  100 VAL   A HG11 1 
ATOM   1960 H HG11 B VAL   A 1 100 ? 16.169 -2.942  -12.596 0.24 25.81 ?  100 VAL   A HG11 1 
ATOM   1961 H HG12 A VAL   A 1 100 ? 17.327 -2.292  -13.586 0.76 27.71 ?  100 VAL   A HG12 1 
ATOM   1962 H HG12 B VAL   A 1 100 ? 16.759 -1.491  -12.847 0.24 25.81 ?  100 VAL   A HG12 1 
ATOM   1963 H HG13 A VAL   A 1 100 ? 18.263 -3.544  -13.874 0.76 27.71 ?  100 VAL   A HG13 1 
ATOM   1964 H HG13 B VAL   A 1 100 ? 17.387 -2.748  -13.594 0.24 25.81 ?  100 VAL   A HG13 1 
ATOM   1965 H HG21 A VAL   A 1 100 ? 17.709 -4.764  -11.199 0.76 27.44 ?  100 VAL   A HG21 1 
ATOM   1966 H HG21 B VAL   A 1 100 ? 17.043 -4.353  -10.945 0.24 25.40 ?  100 VAL   A HG21 1 
ATOM   1967 H HG22 A VAL   A 1 100 ? 19.218 -4.776  -11.695 0.76 27.44 ?  100 VAL   A HG22 1 
ATOM   1968 H HG22 B VAL   A 1 100 ? 18.254 -4.644  -11.932 0.24 25.40 ?  100 VAL   A HG22 1 
ATOM   1969 H HG23 A VAL   A 1 100 ? 18.845 -4.110  -10.302 0.76 27.44 ?  100 VAL   A HG23 1 
ATOM   1970 H HG23 B VAL   A 1 100 ? 18.540 -4.198  -10.434 0.24 25.40 ?  100 VAL   A HG23 1 
ATOM   1971 N N    A ASN   A 1 101 ? 19.345 0.212   -12.159 0.76 22.46 ?  101 ASN   A N    1 
ATOM   1972 N N    B ASN   A 1 101 ? 19.281 0.215   -12.420 0.24 23.76 ?  101 ASN   A N    1 
ATOM   1973 C CA   A ASN   A 1 101 ? 19.273 1.506   -12.832 0.76 24.61 ?  101 ASN   A CA   1 
ATOM   1974 C CA   B ASN   A 1 101 ? 19.309 1.418   -13.243 0.24 24.66 ?  101 ASN   A CA   1 
ATOM   1975 C C    A ASN   A 1 101 ? 20.621 1.965   -13.386 0.76 26.37 ?  101 ASN   A C    1 
ATOM   1976 C C    B ASN   A 1 101 ? 20.714 1.741   -13.751 0.24 25.74 ?  101 ASN   A C    1 
ATOM   1977 O O    A ASN   A 1 101 ? 20.665 3.001   -14.063 0.76 28.79 ?  101 ASN   A O    1 
ATOM   1978 O O    B ASN   A 1 101 ? 21.004 2.895   -14.091 0.24 26.41 ?  101 ASN   A O    1 
ATOM   1979 C CB   A ASN   A 1 101 ? 18.653 2.543   -11.892 0.76 24.06 ?  101 ASN   A CB   1 
ATOM   1980 C CB   B ASN   A 1 101 ? 18.681 2.593   -12.483 0.24 24.33 ?  101 ASN   A CB   1 
ATOM   1981 C CG   A ASN   A 1 101 ? 17.259 2.140   -11.425 0.76 23.65 ?  101 ASN   A CG   1 
ATOM   1982 C CG   B ASN   A 1 101 ? 17.514 2.160   -11.622 0.24 23.73 ?  101 ASN   A CG   1 
ATOM   1983 O OD1  A ASN   A 1 101 ? 16.467 1.585   -12.195 0.76 24.39 ?  101 ASN   A OD1  1 
ATOM   1984 O OD1  B ASN   A 1 101 ? 16.429 1.866   -12.127 0.24 23.59 ?  101 ASN   A OD1  1 
ATOM   1985 N ND2  A ASN   A 1 101 ? 16.958 2.398   -10.155 0.76 23.70 ?  101 ASN   A ND2  1 
ATOM   1986 N ND2  B ASN   A 1 101 ? 17.734 2.106   -10.314 0.24 23.49 ?  101 ASN   A ND2  1 
ATOM   1987 H H    A ASN   A 1 101 ? 19.238 0.245   -11.307 0.76 26.96 ?  101 ASN   A H    1 
ATOM   1988 H H    B ASN   A 1 101 ? 19.236 0.369   -11.574 0.24 28.51 ?  101 ASN   A H    1 
ATOM   1989 H HA   A ASN   A 1 101 ? 18.677 1.418   -13.585 0.76 29.54 ?  101 ASN   A HA   1 
ATOM   1990 H HA   B ASN   A 1 101 ? 18.766 1.271   -14.032 0.24 29.59 ?  101 ASN   A HA   1 
ATOM   1991 H HB2  A ASN   A 1 101 ? 19.216 2.646   -11.108 0.76 28.87 ?  101 ASN   A HB2  1 
ATOM   1992 H HB2  B ASN   A 1 101 ? 19.336 2.998   -11.899 0.24 29.19 ?  101 ASN   A HB2  1 
ATOM   1993 H HB3  A ASN   A 1 101 ? 18.580 3.391   -12.360 0.76 28.87 ?  101 ASN   A HB3  1 
ATOM   1994 H HB3  B ASN   A 1 101 ? 18.341 3.252   -13.113 0.24 29.19 ?  101 ASN   A HB3  1 
ATOM   1995 H HD21 A ASN   A 1 101 ? 16.182 2.189   -9.849  0.76 28.44 ?  101 ASN   A HD21 1 
ATOM   1996 H HD21 B ASN   A 1 101 ? 17.107 1.858   -9.781  0.24 28.19 ?  101 ASN   A HD21 1 
ATOM   1997 H HD22 A ASN   A 1 101 ? 17.531 2.784   -9.646  0.76 28.44 ?  101 ASN   A HD22 1 
ATOM   1998 H HD22 B ASN   A 1 101 ? 18.506 2.319   -10.002 0.24 28.19 ?  101 ASN   A HD22 1 
ATOM   1999 N N    A LYS   A 1 102 ? 21.702 1.216   -13.129 0.76 27.59 ?  102 LYS   A N    1 
ATOM   2000 N N    B LYS   A 1 102 ? 21.582 0.724   -13.801 0.24 26.02 ?  102 LYS   A N    1 
ATOM   2001 C CA   A LYS   A 1 102 ? 22.988 1.410   -13.790 0.76 28.85 ?  102 LYS   A CA   1 
ATOM   2002 C CA   B LYS   A 1 102 ? 22.898 0.835   -14.410 0.24 26.09 ?  102 LYS   A CA   1 
ATOM   2003 C C    A LYS   A 1 102 ? 23.309 0.309   -14.792 0.76 29.08 ?  102 LYS   A C    1 
ATOM   2004 C C    B LYS   A 1 102 ? 23.258 -0.354  -15.296 0.24 25.25 ?  102 LYS   A C    1 
ATOM   2005 O O    A LYS   A 1 102 ? 24.399 0.324   -15.373 0.76 29.65 ?  102 LYS   A O    1 
ATOM   2006 O O    B LYS   A 1 102 ? 24.375 -0.384  -15.821 0.24 25.23 ?  102 LYS   A O    1 
ATOM   2007 C CB   A LYS   A 1 102 ? 24.127 1.474   -12.761 0.76 30.22 ?  102 LYS   A CB   1 
ATOM   2008 C CB   B LYS   A 1 102 ? 23.987 0.974   -13.332 0.24 27.08 ?  102 LYS   A CB   1 
ATOM   2009 C CG   A LYS   A 1 102 ? 24.019 2.595   -11.749 0.76 31.31 ?  102 LYS   A CG   1 
ATOM   2010 C CG   B LYS   A 1 102 ? 23.959 2.282   -12.560 0.24 28.00 ?  102 LYS   A CG   1 
ATOM   2011 C CD   A LYS   A 1 102 ? 25.185 2.546   -10.767 0.76 32.54 ?  102 LYS   A CD   1 
ATOM   2012 C CD   B LYS   A 1 102 ? 24.934 2.259   -11.395 0.24 28.85 ?  102 LYS   A CD   1 
ATOM   2013 C CE   A LYS   A 1 102 ? 25.120 3.682   -9.757  0.76 33.29 ?  102 LYS   A CE   1 
ATOM   2014 C CE   B LYS   A 1 102 ? 24.894 3.567   -10.624 0.24 29.50 ?  102 LYS   A CE   1 
ATOM   2015 N NZ   A LYS   A 1 102 ? 26.224 3.596   -8.755  0.76 33.86 ?  102 LYS   A NZ   1 
ATOM   2016 N NZ   B LYS   A 1 102 ? 25.377 3.419   -9.222  0.24 29.91 ?  102 LYS   A NZ   1 
ATOM   2017 H H    A LYS   A 1 102 ? 21.713 0.568   -12.559 0.76 33.11 ?  102 LYS   A H    1 
ATOM   2018 H H    B LYS   A 1 102 ? 21.423 -0.049  -13.473 0.24 31.22 ?  102 LYS   A H    1 
ATOM   2019 H HA   A LYS   A 1 102 ? 22.973 2.248   -14.271 0.76 34.62 ?  102 LYS   A HA   1 
ATOM   2020 H HA   B LYS   A 1 102 ? 22.910 1.649   -14.940 0.24 31.31 ?  102 LYS   A HA   1 
ATOM   2021 H HB2  A LYS   A 1 102 ? 24.149 0.637   -12.270 0.76 36.26 ?  102 LYS   A HB2  1 
ATOM   2022 H HB2  B LYS   A 1 102 ? 23.885 0.251   -12.692 0.24 32.50 ?  102 LYS   A HB2  1 
ATOM   2023 H HB3  A LYS   A 1 102 ? 24.967 1.590   -13.237 0.76 36.26 ?  102 LYS   A HB3  1 
ATOM   2024 H HB3  B LYS   A 1 102 ? 24.853 0.905   -13.765 0.24 32.50 ?  102 LYS   A HB3  1 
ATOM   2025 H HG2  A LYS   A 1 102 ? 24.040 3.448   -12.210 0.76 37.57 ?  102 LYS   A HG2  1 
ATOM   2026 H HG2  B LYS   A 1 102 ? 24.213 3.011   -13.149 0.24 33.61 ?  102 LYS   A HG2  1 
ATOM   2027 H HG3  A LYS   A 1 102 ? 23.193 2.499   -11.250 0.76 37.57 ?  102 LYS   A HG3  1 
ATOM   2028 H HG3  B LYS   A 1 102 ? 23.069 2.430   -12.206 0.24 33.61 ?  102 LYS   A HG3  1 
ATOM   2029 H HD2  A LYS   A 1 102 ? 25.160 1.705   -10.283 0.76 39.04 ?  102 LYS   A HD2  1 
ATOM   2030 H HD2  B LYS   A 1 102 ? 24.699 1.539   -10.789 0.24 34.62 ?  102 LYS   A HD2  1 
ATOM   2031 H HD3  A LYS   A 1 102 ? 26.019 2.622   -11.259 0.76 39.04 ?  102 LYS   A HD3  1 
ATOM   2032 H HD3  B LYS   A 1 102 ? 25.834 2.128   -11.734 0.24 34.62 ?  102 LYS   A HD3  1 
ATOM   2033 H HE2  A LYS   A 1 102 ? 25.198 4.529   -10.226 0.76 39.94 ?  102 LYS   A HE2  1 
ATOM   2034 H HE2  B LYS   A 1 102 ? 25.462 4.214   -11.072 0.24 35.40 ?  102 LYS   A HE2  1 
ATOM   2035 H HE3  A LYS   A 1 102 ? 24.274 3.639   -9.284  0.76 39.94 ?  102 LYS   A HE3  1 
ATOM   2036 H HE3  B LYS   A 1 102 ? 23.980 3.890   -10.598 0.24 35.40 ?  102 LYS   A HE3  1 
ATOM   2037 H HZ1  A LYS   A 1 102 ? 26.163 4.270   -8.178  0.76 40.63 ?  102 LYS   A HZ1  1 
ATOM   2038 H HZ1  B LYS   A 1 102 ? 25.298 4.194   -8.790  0.24 35.89 ?  102 LYS   A HZ1  1 
ATOM   2039 H HZ2  A LYS   A 1 102 ? 26.171 2.827   -8.310  0.76 40.63 ?  102 LYS   A HZ2  1 
ATOM   2040 H HZ2  B LYS   A 1 102 ? 24.895 2.802   -8.797  0.24 35.89 ?  102 LYS   A HZ2  1 
ATOM   2041 H HZ3  A LYS   A 1 102 ? 27.012 3.638   -9.168  0.76 40.63 ?  102 LYS   A HZ3  1 
ATOM   2042 H HZ3  B LYS   A 1 102 ? 26.231 3.171   -9.218  0.24 35.89 ?  102 LYS   A HZ3  1 
ATOM   2043 N N    A GLY   A 1 103 ? 22.409 -0.652  -14.997 0.76 29.34 ?  103 GLY   A N    1 
ATOM   2044 N N    B GLY   A 1 103 ? 22.375 -1.342  -15.465 0.24 24.59 ?  103 GLY   A N    1 
ATOM   2045 C CA   A GLY   A 1 103 ? 22.661 -1.735  -15.929 0.76 29.34 ?  103 GLY   A CA   1 
ATOM   2046 C CA   B GLY   A 1 103 ? 22.713 -2.511  -16.257 0.24 24.01 ?  103 GLY   A CA   1 
ATOM   2047 C C    A GLY   A 1 103 ? 23.502 -2.871  -15.392 0.76 29.30 ?  103 GLY   A C    1 
ATOM   2048 C C    B GLY   A 1 103 ? 23.536 -3.559  -15.544 0.24 23.12 ?  103 GLY   A C    1 
ATOM   2049 O O    A GLY   A 1 103 ? 24.081 -3.621  -16.184 0.76 30.24 ?  103 GLY   A O    1 
ATOM   2050 O O    B GLY   A 1 103 ? 23.947 -4.537  -16.179 0.24 22.62 ?  103 GLY   A O    1 
ATOM   2051 H H    A GLY   A 1 103 ? 21.645 -0.701  -14.608 0.76 35.21 ?  103 GLY   A H    1 
ATOM   2052 H H    B GLY   A 1 103 ? 21.574 -1.361  -15.139 0.24 29.51 ?  103 GLY   A H    1 
ATOM   2053 H HA2  A GLY   A 1 103 ? 21.813 -2.102  -16.229 0.76 35.21 ?  103 GLY   A HA2  1 
ATOM   2054 H HA2  B GLY   A 1 103 ? 21.902 -2.937  -16.573 0.24 28.81 ?  103 GLY   A HA2  1 
ATOM   2055 H HA3  A GLY   A 1 103 ? 23.120 -1.381  -16.708 0.76 35.21 ?  103 GLY   A HA3  1 
ATOM   2056 H HA3  B GLY   A 1 103 ? 23.223 -2.226  -17.032 0.24 28.81 ?  103 GLY   A HA3  1 
ATOM   2057 N N    A GLU   A 1 104 ? 23.585 -3.034  -14.076 0.76 27.14 ?  104 GLU   A N    1 
ATOM   2058 N N    B GLU   A 1 104 ? 23.786 -3.395  -14.249 0.24 22.70 ?  104 GLU   A N    1 
ATOM   2059 C CA   A GLU   A 1 104 ? 24.458 -4.037  -13.481 0.76 25.31 ?  104 GLU   A CA   1 
ATOM   2060 C CA   B GLU   A 1 104 ? 24.652 -4.319  -13.532 0.24 22.43 ?  104 GLU   A CA   1 
ATOM   2061 C C    A GLU   A 1 104 ? 23.766 -5.397  -13.386 0.76 25.13 ?  104 GLU   A C    1 
ATOM   2062 C C    B GLU   A 1 104 ? 23.958 -5.665  -13.343 0.24 22.93 ?  104 GLU   A C    1 
ATOM   2063 O O    A GLU   A 1 104 ? 22.540 -5.493  -13.280 0.76 25.60 ?  104 GLU   A O    1 
ATOM   2064 O O    B GLU   A 1 104 ? 22.779 -5.737  -12.985 0.24 22.68 ?  104 GLU   A O    1 
ATOM   2065 C CB   A GLU   A 1 104 ? 24.962 -3.553  -12.117 0.76 23.34 ?  104 GLU   A CB   1 
ATOM   2066 C CB   B GLU   A 1 104 ? 25.058 -3.705  -12.191 0.24 21.92 ?  104 GLU   A CB   1 
ATOM   2067 C CG   A GLU   A 1 104 ? 25.890 -2.341  -12.273 0.76 22.76 ?  104 GLU   A CG   1 
ATOM   2068 C CG   B GLU   A 1 104 ? 25.776 -2.364  -12.350 0.24 21.82 ?  104 GLU   A CG   1 
ATOM   2069 C CD   A GLU   A 1 104 ? 26.215 -1.573  -10.998 0.76 21.58 ?  104 GLU   A CD   1 
ATOM   2070 C CD   B GLU   A 1 104 ? 26.254 -1.773  -11.037 0.24 21.65 ?  104 GLU   A CD   1 
ATOM   2071 O OE1  A GLU   A 1 104 ? 25.645 -1.860  -9.925  0.76 20.01 ?  104 GLU   A OE1  1 
ATOM   2072 O OE1  B GLU   A 1 104 ? 25.762 -2.190  -9.969  0.24 21.41 ?  104 GLU   A OE1  1 
ATOM   2073 O OE2  A GLU   A 1 104 ? 27.055 -0.647  -11.099 0.76 22.64 -1 104 GLU   A OE2  1 
ATOM   2074 O OE2  B GLU   A 1 104 ? 27.127 -0.881  -11.080 0.24 22.05 -1 104 GLU   A OE2  1 
ATOM   2075 H H    A GLU   A 1 104 ? 23.147 -2.565  -13.502 0.76 32.56 ?  104 GLU   A H    1 
ATOM   2076 H H    B GLU   A 1 104 ? 23.466 -2.762  -13.764 0.24 27.24 ?  104 GLU   A H    1 
ATOM   2077 H HA   A GLU   A 1 104 ? 25.229 -4.146  -14.056 0.76 30.37 ?  104 GLU   A HA   1 
ATOM   2078 H HA   B GLU   A 1 104 ? 25.463 -4.463  -14.048 0.24 26.92 ?  104 GLU   A HA   1 
ATOM   2079 H HB2  A GLU   A 1 104 ? 24.204 -3.298  -11.571 0.76 28.01 ?  104 GLU   A HB2  1 
ATOM   2080 H HB2  B GLU   A 1 104 ? 24.263 -3.554  -11.658 0.24 26.31 ?  104 GLU   A HB2  1 
ATOM   2081 H HB3  A GLU   A 1 104 ? 25.459 -4.270  -11.693 0.76 28.01 ?  104 GLU   A HB3  1 
ATOM   2082 H HB3  B GLU   A 1 104 ? 25.659 -4.310  -11.731 0.24 26.31 ?  104 GLU   A HB3  1 
ATOM   2083 H HG2  A GLU   A 1 104 ? 26.728 -2.646  -12.645 0.76 27.31 ?  104 GLU   A HG2  1 
ATOM   2084 H HG2  B GLU   A 1 104 ? 26.553 -2.485  -12.920 0.24 26.19 ?  104 GLU   A HG2  1 
ATOM   2085 H HG3  A GLU   A 1 104 ? 25.469 -1.712  -12.877 0.76 27.31 ?  104 GLU   A HG3  1 
ATOM   2086 H HG3  B GLU   A 1 104 ? 25.169 -1.723  -12.755 0.24 26.19 ?  104 GLU   A HG3  1 
ATOM   2087 N N    A ASP   A 1 105 ? 24.579 -6.453  -13.425 0.76 25.74 ?  105 ASP   A N    1 
ATOM   2088 N N    B ASP   A 1 105 ? 24.708 -6.735  -13.599 0.24 23.96 ?  105 ASP   A N    1 
ATOM   2089 C CA   A ASP   A 1 105 ? 24.088 -7.820  -13.580 0.76 27.13 ?  105 ASP   A CA   1 
ATOM   2090 C CA   B ASP   A 1 105 ? 24.171 -8.091  -13.612 0.24 25.09 ?  105 ASP   A CA   1 
ATOM   2091 C C    A ASP   A 1 105 ? 23.408 -8.298  -12.299 0.76 24.65 ?  105 ASP   A C    1 
ATOM   2092 C C    B ASP   A 1 105 ? 23.464 -8.413  -12.301 0.24 24.85 ?  105 ASP   A C    1 
ATOM   2093 O O    A ASP   A 1 105 ? 24.045 -8.391  -11.247 0.76 22.57 ?  105 ASP   A O    1 
ATOM   2094 O O    B ASP   A 1 105 ? 24.080 -8.397  -11.231 0.24 24.59 ?  105 ASP   A O    1 
ATOM   2095 C CB   A ASP   A 1 105 ? 25.270 -8.725  -13.922 0.76 30.40 ?  105 ASP   A CB   1 
ATOM   2096 C CB   B ASP   A 1 105 ? 25.328 -9.062  -13.845 0.24 26.32 ?  105 ASP   A CB   1 
ATOM   2097 C CG   A ASP   A 1 105 ? 24.855 -10.147 -14.210 0.76 33.26 ?  105 ASP   A CG   1 
ATOM   2098 C CG   B ASP   A 1 105 ? 24.899 -10.517 -13.802 0.24 27.26 ?  105 ASP   A CG   1 
ATOM   2099 O OD1  A ASP   A 1 105 ? 23.638 -10.401 -14.313 0.76 33.79 ?  105 ASP   A OD1  1 
ATOM   2100 O OD1  B ASP   A 1 105 ? 23.686 -10.795 -13.899 0.24 27.45 ?  105 ASP   A OD1  1 
ATOM   2101 O OD2  A ASP   A 1 105 ? 25.754 -11.009 -14.340 0.76 35.02 -1 105 ASP   A OD2  1 
ATOM   2102 O OD2  B ASP   A 1 105 ? 25.787 -11.386 -13.666 0.24 27.93 -1 105 ASP   A OD2  1 
ATOM   2103 H H    A ASP   A 1 105 ? 25.437 -6.400  -13.364 0.76 30.89 ?  105 ASP   A H    1 
ATOM   2104 H H    B ASP   A 1 105 ? 25.544 -6.695  -13.774 0.24 28.76 ?  105 ASP   A H    1 
ATOM   2105 H HA   A ASP   A 1 105 ? 23.447 -7.859  -14.305 0.76 32.55 ?  105 ASP   A HA   1 
ATOM   2106 H HA   B ASP   A 1 105 ? 23.530 -8.180  -14.334 0.24 30.11 ?  105 ASP   A HA   1 
ATOM   2107 H HB2  A ASP   A 1 105 ? 25.712 -8.386  -14.715 0.76 36.49 ?  105 ASP   A HB2  1 
ATOM   2108 H HB2  B ASP   A 1 105 ? 25.713 -8.882  -14.718 0.24 31.59 ?  105 ASP   A HB2  1 
ATOM   2109 H HB3  A ASP   A 1 105 ? 25.889 -8.736  -13.175 0.76 36.49 ?  105 ASP   A HB3  1 
ATOM   2110 H HB3  B ASP   A 1 105 ? 25.995 -8.925  -13.154 0.24 31.59 ?  105 ASP   A HB3  1 
ATOM   2111 N N    A ILE   A 1 106 ? 22.121 -8.642  -12.398 0.76 24.50 ?  106 ILE   A N    1 
ATOM   2112 N N    B ILE   A 1 106 ? 22.168 -8.722  -12.392 0.24 24.99 ?  106 ILE   A N    1 
ATOM   2113 C CA   A ILE   A 1 106 ? 21.358 -9.050  -11.224 0.76 23.71 ?  106 ILE   A CA   1 
ATOM   2114 C CA   B ILE   A 1 106 ? 21.398 -9.070  -11.204 0.24 25.10 ?  106 ILE   A CA   1 
ATOM   2115 C C    A ILE   A 1 106 ? 21.896 -10.336 -10.619 0.76 22.76 ?  106 ILE   A C    1 
ATOM   2116 C C    B ILE   A 1 106 ? 21.897 -10.363 -10.578 0.24 24.74 ?  106 ILE   A C    1 
ATOM   2117 O O    A ILE   A 1 106 ? 21.691 -10.583 -9.426  0.76 21.94 ?  106 ILE   A O    1 
ATOM   2118 O O    B ILE   A 1 106 ? 21.675 -10.595 -9.384  0.24 24.61 ?  106 ILE   A O    1 
ATOM   2119 C CB   A ILE   A 1 106 ? 19.851 -9.148  -11.556 0.76 25.62 ?  106 ILE   A CB   1 
ATOM   2120 C CB   B ILE   A 1 106 ? 19.889 -9.120  -11.522 0.24 25.84 ?  106 ILE   A CB   1 
ATOM   2121 C CG1  A ILE   A 1 106 ? 19.015 -9.226  -10.275 0.76 26.22 ?  106 ILE   A CG1  1 
ATOM   2122 C CG1  B ILE   A 1 106 ? 19.059 -9.183  -10.235 0.24 26.23 ?  106 ILE   A CG1  1 
ATOM   2123 C CG2  A ILE   A 1 106 ? 19.569 -10.356 -12.433 0.76 26.43 ?  106 ILE   A CG2  1 
ATOM   2124 C CG2  B ILE   A 1 106 ? 19.564 -10.316 -12.401 0.24 26.06 ?  106 ILE   A CG2  1 
ATOM   2125 C CD1  A ILE   A 1 106 ? 19.107 -7.990  -9.406  0.76 26.81 ?  106 ILE   A CD1  1 
ATOM   2126 C CD1  B ILE   A 1 106 ? 19.283 -8.014  -9.300  0.24 26.42 ?  106 ILE   A CD1  1 
ATOM   2127 H H    A ILE   A 1 106 ? 21.678 -8.648  -13.130 0.76 29.40 ?  106 ILE   A H    1 
ATOM   2128 H H    B ILE   A 1 106 ? 21.720 -8.733  -13.123 0.24 29.98 ?  106 ILE   A H    1 
ATOM   2129 H HA   A ILE   A 1 106 ? 21.467 -8.371  -10.550 0.76 28.45 ?  106 ILE   A HA   1 
ATOM   2130 H HA   B ILE   A 1 106 ? 21.538 -8.372  -10.550 0.24 30.12 ?  106 ILE   A HA   1 
ATOM   2131 H HB   A ILE   A 1 106 ? 19.596 -8.349  -12.041 0.76 30.75 ?  106 ILE   A HB   1 
ATOM   2132 H HB   B ILE   A 1 106 ? 19.647 -8.314  -12.003 0.24 31.01 ?  106 ILE   A HB   1 
ATOM   2133 H HG12 A ILE   A 1 106 ? 18.085 -9.345  -10.517 0.76 31.46 ?  106 ILE   A HG12 1 
ATOM   2134 H HG12 B ILE   A 1 106 ? 18.117 -9.193  -10.471 0.24 31.48 ?  106 ILE   A HG12 1 
ATOM   2135 H HG13 A ILE   A 1 106 ? 19.316 -9.981  -9.746  0.76 31.46 ?  106 ILE   A HG13 1 
ATOM   2136 H HG13 B ILE   A 1 106 ? 19.284 -9.994  -9.755  0.24 31.48 ?  106 ILE   A HG13 1 
ATOM   2137 H HG21 A ILE   A 1 106 ? 18.672 -10.279 -12.791 0.76 31.71 ?  106 ILE   A HG21 1 
ATOM   2138 H HG21 B ILE   A 1 106 ? 18.659 -10.223 -12.737 0.24 31.27 ?  106 ILE   A HG21 1 
ATOM   2139 H HG22 A ILE   A 1 106 ? 20.215 -10.375 -13.156 0.76 31.71 ?  106 ILE   A HG22 1 
ATOM   2140 H HG22 B ILE   A 1 106 ? 20.191 -10.340 -13.139 0.24 31.27 ?  106 ILE   A HG22 1 
ATOM   2141 H HG23 A ILE   A 1 106 ? 19.646 -11.160 -11.898 0.76 31.71 ?  106 ILE   A HG23 1 
ATOM   2142 H HG23 B ILE   A 1 106 ? 19.640 -11.126 -11.874 0.24 31.27 ?  106 ILE   A HG23 1 
ATOM   2143 H HD11 A ILE   A 1 106 ? 18.388 -8.006  -8.758  0.76 32.17 ?  106 ILE   A HD11 1 
ATOM   2144 H HD11 B ILE   A 1 106 ? 18.556 -7.979  -8.661  0.24 31.71 ?  106 ILE   A HD11 1 
ATOM   2145 H HD12 A ILE   A 1 106 ? 19.964 -7.985  -8.949  0.76 32.17 ?  106 ILE   A HD12 1 
ATOM   2146 H HD12 B ILE   A 1 106 ? 20.126 -8.137  -8.836  0.24 31.71 ?  106 ILE   A HD12 1 
ATOM   2147 H HD13 A ILE   A 1 106 ? 19.028 -7.203  -9.969  0.76 32.17 ?  106 ILE   A HD13 1 
ATOM   2148 H HD13 B ILE   A 1 106 ? 19.306 -7.195  -9.820  0.24 31.71 ?  106 ILE   A HD13 1 
ATOM   2149 N N    A GLN   A 1 107 ? 22.599 -11.157 -11.410 0.76 23.33 ?  107 GLN   A N    1 
ATOM   2150 N N    B GLN   A 1 107 ? 22.577 -11.214 -11.353 0.24 24.63 ?  107 GLN   A N    1 
ATOM   2151 C CA   A GLN   A 1 107 ? 23.223 -12.364 -10.878 0.76 25.79 ?  107 GLN   A CA   1 
ATOM   2152 C CA   B GLN   A 1 107 ? 23.189 -12.406 -10.781 0.24 24.81 ?  107 GLN   A CA   1 
ATOM   2153 C C    A GLN   A 1 107 ? 24.195 -12.045 -9.750  0.76 23.44 ?  107 GLN   A C    1 
ATOM   2154 C C    B GLN   A 1 107 ? 24.222 -12.058 -9.719  0.24 22.60 ?  107 GLN   A C    1 
ATOM   2155 O O    A GLN   A 1 107 ? 24.411 -12.884 -8.869  0.76 25.20 ?  107 GLN   A O    1 
ATOM   2156 O O    B GLN   A 1 107 ? 24.530 -12.901 -8.869  0.24 23.38 ?  107 GLN   A O    1 
ATOM   2157 C CB   A GLN   A 1 107 ? 23.942 -13.118 -12.005 0.76 30.10 ?  107 GLN   A CB   1 
ATOM   2158 C CB   B GLN   A 1 107 ? 23.826 -13.258 -11.883 0.24 27.06 ?  107 GLN   A CB   1 
ATOM   2159 C CG   A GLN   A 1 107 ? 23.088 -13.330 -13.253 0.76 34.67 ?  107 GLN   A CG   1 
ATOM   2160 C CG   B GLN   A 1 107 ? 22.838 -13.748 -12.932 0.24 29.34 ?  107 GLN   A CG   1 
ATOM   2161 C CD   A GLN   A 1 107 ? 21.825 -14.119 -12.970 0.76 38.12 ?  107 GLN   A CD   1 
ATOM   2162 C CD   B GLN   A 1 107 ? 21.659 -14.483 -12.323 0.24 31.36 ?  107 GLN   A CD   1 
ATOM   2163 O OE1  A GLN   A 1 107 ? 21.871 -15.192 -12.367 0.76 39.89 ?  107 GLN   A OE1  1 
ATOM   2164 O OE1  B GLN   A 1 107 ? 21.824 -15.311 -11.426 0.24 31.93 ?  107 GLN   A OE1  1 
ATOM   2165 N NE2  A GLN   A 1 107 ? 20.685 -13.588 -13.400 0.76 39.73 ?  107 GLN   A NE2  1 
ATOM   2166 N NE2  B GLN   A 1 107 ? 20.460 -14.173 -12.799 0.24 32.24 ?  107 GLN   A NE2  1 
ATOM   2167 H H    A GLN   A 1 107 ? 22.737 -11.031 -12.248 0.76 28.00 ?  107 GLN   A H    1 
ATOM   2168 H H    B GLN   A 1 107 ? 22.693 -11.122 -12.200 0.24 29.56 ?  107 GLN   A H    1 
ATOM   2169 H HA   A GLN   A 1 107 ? 22.543 -12.952 -10.522 0.76 30.95 ?  107 GLN   A HA   1 
ATOM   2170 H HA   B GLN   A 1 107 ? 22.502 -12.938 -10.357 0.24 29.77 ?  107 GLN   A HA   1 
ATOM   2171 H HB2  A GLN   A 1 107 ? 24.730 -12.618 -12.272 0.76 36.12 ?  107 GLN   A HB2  1 
ATOM   2172 H HB2  B GLN   A 1 107 ? 24.504 -12.734 -12.337 0.24 32.47 ?  107 GLN   A HB2  1 
ATOM   2173 H HB3  A GLN   A 1 107 ? 24.207 -13.997 -11.684 0.76 36.12 ?  107 GLN   A HB3  1 
ATOM   2174 H HB3  B GLN   A 1 107 ? 24.235 -14.038 -11.479 0.24 32.47 ?  107 GLN   A HB3  1 
ATOM   2175 H HG2  A GLN   A 1 107 ? 22.827 -12.470 -13.617 0.76 41.60 ?  107 GLN   A HG2  1 
ATOM   2176 H HG2  B GLN   A 1 107 ? 22.497 -12.986 -13.426 0.24 35.20 ?  107 GLN   A HG2  1 
ATOM   2177 H HG3  A GLN   A 1 107 ? 23.605 -13.820 -13.910 0.76 41.60 ?  107 GLN   A HG3  1 
ATOM   2178 H HG3  B GLN   A 1 107 ? 23.292 -14.359 -13.534 0.24 35.20 ?  107 GLN   A HG3  1 
ATOM   2179 H HE21 A GLN   A 1 107 ? 20.690 -12.837 -13.817 0.76 47.67 ?  107 GLN   A HE21 1 
ATOM   2180 H HE21 B GLN   A 1 107 ? 20.384 -13.586 -13.424 0.24 38.68 ?  107 GLN   A HE21 1 
ATOM   2181 H HE22 A GLN   A 1 107 ? 19.942 -13.998 -13.262 0.76 47.67 ?  107 GLN   A HE22 1 
ATOM   2182 H HE22 B GLN   A 1 107 ? 19.759 -14.558 -12.484 0.24 38.68 ?  107 GLN   A HE22 1 
ATOM   2183 N N    . LEU   A 1 108 ? 24.753 -10.833 -9.735  1.00 19.74 ?  108 LEU   A N    1 
ATOM   2184 C CA   . LEU   A 1 108 ? 25.674 -10.422 -8.687  1.00 16.40 ?  108 LEU   A CA   1 
ATOM   2185 C C    . LEU   A 1 108 ? 24.978 -10.249 -7.346  1.00 14.62 ?  108 LEU   A C    1 
ATOM   2186 O O    . LEU   A 1 108 ? 25.662 -10.085 -6.334  1.00 15.02 ?  108 LEU   A O    1 
ATOM   2187 C CB   . LEU   A 1 108 ? 26.398 -9.128  -9.083  1.00 16.20 ?  108 LEU   A CB   1 
ATOM   2188 C CG   . LEU   A 1 108 ? 27.397 -9.311  -10.226 1.00 18.08 ?  108 LEU   A CG   1 
ATOM   2189 C CD1  . LEU   A 1 108 ? 27.874 -7.977  -10.773 1.00 18.52 ?  108 LEU   A CD1  1 
ATOM   2190 C CD2  . LEU   A 1 108 ? 28.589 -10.139 -9.768  1.00 19.94 ?  108 LEU   A CD2  1 
ATOM   2191 H H    A LEU   A 1 108 ? 24.600 -10.228 -10.320 0.76 23.69 ?  108 LEU   A H    1 
ATOM   2192 H H    B LEU   A 1 108 ? 24.599 -10.240 -10.332 0.24 23.69 ?  108 LEU   A H    1 
ATOM   2193 H HA   . LEU   A 1 108 ? 26.343 -11.112 -8.573  1.00 19.68 ?  108 LEU   A HA   1 
ATOM   2194 H HB2  . LEU   A 1 108 ? 25.740 -8.474  -9.368  1.00 19.44 ?  108 LEU   A HB2  1 
ATOM   2195 H HB3  . LEU   A 1 108 ? 26.884 -8.792  -8.315  1.00 19.44 ?  108 LEU   A HB3  1 
ATOM   2196 H HG   . LEU   A 1 108 ? 26.966 -9.791  -10.950 1.00 21.69 ?  108 LEU   A HG   1 
ATOM   2197 H HD11 . LEU   A 1 108 ? 28.483 -8.136  -11.515 1.00 22.23 ?  108 LEU   A HD11 1 
ATOM   2198 H HD12 . LEU   A 1 108 ? 27.109 -7.467  -11.080 1.00 22.23 ?  108 LEU   A HD12 1 
ATOM   2199 H HD13 . LEU   A 1 108 ? 28.336 -7.491  -10.071 1.00 22.23 ?  108 LEU   A HD13 1 
ATOM   2200 H HD21 . LEU   A 1 108 ? 29.281 -10.095 -10.443 1.00 23.92 ?  108 LEU   A HD21 1 
ATOM   2201 H HD22 . LEU   A 1 108 ? 28.918 -9.776  -8.930  1.00 23.92 ?  108 LEU   A HD22 1 
ATOM   2202 H HD23 . LEU   A 1 108 ? 28.304 -11.057 -9.642  1.00 23.92 ?  108 LEU   A HD23 1 
ATOM   2203 N N    . LEU   A 1 109 ? 23.645 -10.306 -7.304  1.00 13.71 ?  109 LEU   A N    1 
ATOM   2204 C CA   . LEU   A 1 109 ? 22.951 -10.180 -6.029  1.00 12.97 ?  109 LEU   A CA   1 
ATOM   2205 C C    . LEU   A 1 109 ? 23.299 -11.335 -5.094  1.00 12.17 ?  109 LEU   A C    1 
ATOM   2206 O O    . LEU   A 1 109 ? 23.448 -11.138 -3.884  1.00 12.51 ?  109 LEU   A O    1 
ATOM   2207 C CB   . LEU   A 1 109 ? 21.445 -10.102 -6.269  1.00 13.79 ?  109 LEU   A CB   1 
ATOM   2208 C CG   . LEU   A 1 109 ? 20.567 -9.808  -5.054  1.00 14.10 ?  109 LEU   A CG   1 
ATOM   2209 C CD1  . LEU   A 1 109 ? 21.026 -8.541  -4.353  1.00 14.56 ?  109 LEU   A CD1  1 
ATOM   2210 C CD2  . LEU   A 1 109 ? 19.100 -9.687  -5.469  1.00 15.35 ?  109 LEU   A CD2  1 
ATOM   2211 H H    . LEU   A 1 109 ? 23.130 -10.421 -7.984  1.00 16.46 ?  109 LEU   A H    1 
ATOM   2212 H HA   . LEU   A 1 109 ? 23.233 -9.356  -5.603  1.00 15.56 ?  109 LEU   A HA   1 
ATOM   2213 H HB2  . LEU   A 1 109 ? 21.277 -9.396  -6.914  1.00 16.54 ?  109 LEU   A HB2  1 
ATOM   2214 H HB3  . LEU   A 1 109 ? 21.149 -10.947 -6.634  1.00 16.54 ?  109 LEU   A HB3  1 
ATOM   2215 H HG   . LEU   A 1 109 ? 20.637 -10.542 -4.426  1.00 16.92 ?  109 LEU   A HG   1 
ATOM   2216 H HD11 . LEU   A 1 109 ? 20.346 -8.259  -3.723  1.00 17.48 ?  109 LEU   A HD11 1 
ATOM   2217 H HD12 . LEU   A 1 109 ? 21.857 -8.720  -3.887  1.00 17.48 ?  109 LEU   A HD12 1 
ATOM   2218 H HD13 . LEU   A 1 109 ? 21.164 -7.845  -5.019  1.00 17.48 ?  109 LEU   A HD13 1 
ATOM   2219 H HD21 . LEU   A 1 109 ? 18.582 -9.361  -4.714  1.00 18.41 ?  109 LEU   A HD21 1 
ATOM   2220 H HD22 . LEU   A 1 109 ? 19.027 -9.070  -6.211  1.00 18.41 ?  109 LEU   A HD22 1 
ATOM   2221 H HD23 . LEU   A 1 109 ? 18.772 -10.564 -5.736  1.00 18.41 ?  109 LEU   A HD23 1 
ATOM   2222 N N    . LYS   A 1 110 ? 23.434 -12.553 -5.630  1.00 12.35 ?  110 LYS   A N    1 
ATOM   2223 C CA   . LYS   A 1 110 ? 23.816 -13.672 -4.772  1.00 12.52 ?  110 LYS   A CA   1 
ATOM   2224 C C    . LYS   A 1 110 ? 25.205 -13.446 -4.175  1.00 11.88 ?  110 LYS   A C    1 
ATOM   2225 O O    . LYS   A 1 110 ? 25.413 -13.649 -2.977  1.00 12.06 ?  110 LYS   A O    1 
ATOM   2226 C CB   . LYS   A 1 110 ? 23.737 -14.999 -5.533  1.00 13.55 ?  110 LYS   A CB   1 
ATOM   2227 C CG   . LYS   A 1 110 ? 23.948 -16.213 -4.626  1.00 13.52 ?  110 LYS   A CG   1 
ATOM   2228 C CD   . LYS   A 1 110 ? 23.720 -17.534 -5.342  1.00 14.23 ?  110 LYS   A CD   1 
ATOM   2229 C CE   . LYS   A 1 110 ? 23.820 -18.715 -4.389  1.00 15.36 ?  110 LYS   A CE   1 
ATOM   2230 N NZ   . LYS   A 1 110 ? 22.628 -18.842 -3.507  1.00 15.47 ?  110 LYS   A NZ   1 
ATOM   2231 H H    . LYS   A 1 110 ? 23.314 -12.750 -6.457  1.00 14.81 ?  110 LYS   A H    1 
ATOM   2232 H HA   . LYS   A 1 110 ? 23.182 -13.720 -4.034  1.00 15.03 ?  110 LYS   A HA   1 
ATOM   2233 H HB2  . LYS   A 1 110 ? 22.859 -15.076 -5.941  1.00 16.25 ?  110 LYS   A HB2  1 
ATOM   2234 H HB3  . LYS   A 1 110 ? 24.423 -15.009 -6.215  1.00 16.25 ?  110 LYS   A HB3  1 
ATOM   2235 H HG2  . LYS   A 1 110 ? 24.858 -16.200 -4.290  1.00 16.22 ?  110 LYS   A HG2  1 
ATOM   2236 H HG3  . LYS   A 1 110 ? 23.324 -16.160 -3.882  1.00 16.22 ?  110 LYS   A HG3  1 
ATOM   2237 H HD2  . LYS   A 1 110 ? 22.837 -17.538 -5.734  1.00 17.08 ?  110 LYS   A HD2  1 
ATOM   2238 H HD3  . LYS   A 1 110 ? 24.397 -17.642 -6.028  1.00 17.08 ?  110 LYS   A HD3  1 
ATOM   2239 H HE2  . LYS   A 1 110 ? 23.905 -19.534 -4.902  1.00 18.43 ?  110 LYS   A HE2  1 
ATOM   2240 H HE3  . LYS   A 1 110 ? 24.603 -18.603 -3.820  1.00 18.43 ?  110 LYS   A HE3  1 
ATOM   2241 H HZ1  . LYS   A 1 110 ? 22.719 -19.541 -2.965  1.00 18.56 ?  110 LYS   A HZ1  1 
ATOM   2242 H HZ2  . LYS   A 1 110 ? 22.533 -18.105 -3.016  1.00 18.56 ?  110 LYS   A HZ2  1 
ATOM   2243 H HZ3  . LYS   A 1 110 ? 21.896 -18.954 -4.003  1.00 18.56 ?  110 LYS   A HZ3  1 
ATOM   2244 N N    . SER   A 1 111 ? 26.161 -13.007 -4.997  1.00 12.33 ?  111 SER   A N    1 
ATOM   2245 C CA   . SER   A 1 111 ? 27.494 -12.689 -4.488  1.00 12.01 ?  111 SER   A CA   1 
ATOM   2246 C C    . SER   A 1 111 ? 27.431 -11.645 -3.378  1.00 11.82 ?  111 SER   A C    1 
ATOM   2247 O O    . SER   A 1 111 ? 28.130 -11.752 -2.365  1.00 12.40 ?  111 SER   A O    1 
ATOM   2248 C CB   . SER   A 1 111 ? 28.374 -12.189 -5.633  1.00 13.68 ?  111 SER   A CB   1 
ATOM   2249 O OG   . SER   A 1 111 ? 28.489 -13.184 -6.637  1.00 15.59 ?  111 SER   A OG   1 
ATOM   2250 H H    . SER   A 1 111 ? 26.059 -12.888 -5.841  1.00 14.80 ?  111 SER   A H    1 
ATOM   2251 H HA   . SER   A 1 111 ? 27.896 -13.492 -4.127  1.00 14.42 ?  111 SER   A HA   1 
ATOM   2252 H HB2  . SER   A 1 111 ? 27.966 -11.401 -6.027  1.00 16.41 ?  111 SER   A HB2  1 
ATOM   2253 H HB3  . SER   A 1 111 ? 29.252 -11.970 -5.286  1.00 16.41 ?  111 SER   A HB3  1 
ATOM   2254 H HG   . SER   A 1 111 ? 28.994 -12.904 -7.260  1.00 18.71 ?  111 SER   A HG   1 
ATOM   2255 N N    . ALA   A 1 112 ? 26.581 -10.630 -3.549  1.00 12.09 ?  112 ALA   A N    1 
ATOM   2256 C CA   . ALA   A 1 112 ? 26.438 -9.595  -2.528  1.00 11.41 ?  112 ALA   A CA   1 
ATOM   2257 C C    . ALA   A 1 112 ? 25.963 -10.193 -1.204  1.00 11.60 ?  112 ALA   A C    1 
ATOM   2258 O O    . ALA   A 1 112 ? 26.513 -9.897  -0.137  1.00 12.00 ?  112 ALA   A O    1 
ATOM   2259 C CB   . ALA   A 1 112 ? 25.486 -8.502  -3.025  1.00 12.27 ?  112 ALA   A CB   1 
ATOM   2260 H H    . ALA   A 1 112 ? 26.085 -10.514 -4.242  1.00 14.51 ?  112 ALA   A H    1 
ATOM   2261 H HA   . ALA   A 1 112 ? 27.301 -9.181  -2.374  1.00 13.69 ?  112 ALA   A HA   1 
ATOM   2262 H HB1  . ALA   A 1 112 ? 25.413 -7.811  -2.340  1.00 14.72 ?  112 ALA   A HB1  1 
ATOM   2263 H HB2  . ALA   A 1 112 ? 25.839 -8.115  -3.840  1.00 14.72 ?  112 ALA   A HB2  1 
ATOM   2264 H HB3  . ALA   A 1 112 ? 24.613 -8.889  -3.191  1.00 14.72 ?  112 ALA   A HB3  1 
ATOM   2265 N N    . TYR   A 1 113 ? 24.928 -11.037 -1.251  1.00 11.72 ?  113 TYR   A N    1 
ATOM   2266 C CA   . TYR   A 1 113 ? 24.422 -11.646 -0.025  1.00 11.35 ?  113 TYR   A CA   1 
ATOM   2267 C C    . TYR   A 1 113 ? 25.427 -12.599 0.620   1.00 11.30 ?  113 TYR   A C    1 
ATOM   2268 O O    . TYR   A 1 113 ? 25.384 -12.791 1.840   1.00 11.72 ?  113 TYR   A O    1 
ATOM   2269 C CB   . TYR   A 1 113 ? 23.105 -12.372 -0.294  1.00 11.81 ?  113 TYR   A CB   1 
ATOM   2270 C CG   . TYR   A 1 113 ? 21.886 -11.483 -0.209  1.00 11.54 ?  113 TYR   A CG   1 
ATOM   2271 C CD1  . TYR   A 1 113 ? 21.524 -10.882 0.991   1.00 12.01 ?  113 TYR   A CD1  1 
ATOM   2272 C CD2  . TYR   A 1 113 ? 21.085 -11.258 -1.316  1.00 11.91 ?  113 TYR   A CD2  1 
ATOM   2273 C CE1  . TYR   A 1 113 ? 20.396 -10.086 1.087   1.00 12.13 ?  113 TYR   A CE1  1 
ATOM   2274 C CE2  . TYR   A 1 113 ? 19.935 -10.454 -1.228  1.00 11.88 ?  113 TYR   A CE2  1 
ATOM   2275 C CZ   . TYR   A 1 113 ? 19.607 -9.874  -0.023  1.00 11.76 ?  113 TYR   A CZ   1 
ATOM   2276 O OH   . TYR   A 1 113 ? 18.485 -9.082  0.105   1.00 12.82 ?  113 TYR   A OH   1 
ATOM   2277 H H    . TYR   A 1 113 ? 24.510 -11.262 -1.972  1.00 14.06 ?  113 TYR   A H    1 
ATOM   2278 H HA   . TYR   A 1 113 ? 24.246 -10.941 0.613   1.00 13.62 ?  113 TYR   A HA   1 
ATOM   2279 H HB2  . TYR   A 1 113 ? 23.130 -12.748 -1.187  1.00 14.17 ?  113 TYR   A HB2  1 
ATOM   2280 H HB3  . TYR   A 1 113 ? 23.002 -13.080 0.359   1.00 14.17 ?  113 TYR   A HB3  1 
ATOM   2281 H HD1  . TYR   A 1 113 ? 22.054 -11.027 1.747   1.00 14.42 ?  113 TYR   A HD1  1 
ATOM   2282 H HD2  . TYR   A 1 113 ? 21.298 -11.659 -2.124  1.00 14.29 ?  113 TYR   A HD2  1 
ATOM   2283 H HE1  . TYR   A 1 113 ? 20.176 -9.691  1.902   1.00 14.56 ?  113 TYR   A HE1  1 
ATOM   2284 H HE2  . TYR   A 1 113 ? 19.398 -10.310 -1.974  1.00 14.26 ?  113 TYR   A HE2  1 
ATOM   2285 H HH   . TYR   A 1 113 ? 18.092 -9.025  -0.639  1.00 15.39 ?  113 TYR   A HH   1 
ATOM   2286 N N    . GLU   A 1 114 ? 26.320 -13.212 -0.165  1.00 11.51 ?  114 GLU   A N    1 
ATOM   2287 C CA   . GLU   A 1 114 ? 27.317 -14.104 0.428   1.00 11.48 ?  114 GLU   A CA   1 
ATOM   2288 C C    . GLU   A 1 114 ? 28.169 -13.397 1.476   1.00 11.38 ?  114 GLU   A C    1 
ATOM   2289 O O    . GLU   A 1 114 ? 28.647 -14.035 2.426   1.00 11.96 ?  114 GLU   A O    1 
ATOM   2290 C CB   . GLU   A 1 114 ? 28.183 -14.748 -0.663  1.00 11.55 ?  114 GLU   A CB   1 
ATOM   2291 C CG   . GLU   A 1 114 ? 27.424 -15.804 -1.439  1.00 11.95 ?  114 GLU   A CG   1 
ATOM   2292 C CD   . GLU   A 1 114 ? 28.127 -16.327 -2.682  1.00 12.72 ?  114 GLU   A CD   1 
ATOM   2293 O OE1  . GLU   A 1 114 ? 29.078 -15.701 -3.186  1.00 12.57 ?  114 GLU   A OE1  1 
ATOM   2294 O OE2  . GLU   A 1 114 ? 27.688 -17.389 -3.177  1.00 13.85 -1 114 GLU   A OE2  1 
ATOM   2295 H H    . GLU   A 1 114 ? 26.370 -13.127 -1.027  1.00 13.82 ?  114 GLU   A H    1 
ATOM   2296 H HA   . GLU   A 1 114 ? 26.849 -14.821 0.872   1.00 13.78 ?  114 GLU   A HA   1 
ATOM   2297 H HB2  . GLU   A 1 114 ? 28.470 -14.064 -1.293  1.00 13.85 ?  114 GLU   A HB2  1 
ATOM   2298 H HB3  . GLU   A 1 114 ? 28.953 -15.169 -0.255  1.00 13.85 ?  114 GLU   A HB3  1 
ATOM   2299 H HG2  . GLU   A 1 114 ? 27.272 -16.565 -0.857  1.00 14.34 ?  114 GLU   A HG2  1 
ATOM   2300 H HG3  . GLU   A 1 114 ? 26.573 -15.435 -1.720  1.00 14.34 ?  114 GLU   A HG3  1 
ATOM   2301 N N    . ASN   A 1 115 ? 28.348 -12.079 1.350   1.00 11.24 ?  115 ASN   A N    1 
ATOM   2302 C CA   . ASN   A 1 115 ? 29.108 -11.348 2.357   1.00 11.76 ?  115 ASN   A CA   1 
ATOM   2303 C C    . ASN   A 1 115 ? 28.490 -11.484 3.743   1.00 11.56 ?  115 ASN   A C    1 
ATOM   2304 O O    . ASN   A 1 115 ? 29.203 -11.416 4.749   1.00 12.04 ?  115 ASN   A O    1 
ATOM   2305 C CB   . ASN   A 1 115 ? 29.214 -9.871  1.982   1.00 12.05 ?  115 ASN   A CB   1 
ATOM   2306 C CG   . ASN   A 1 115 ? 30.013 -9.654  0.724   1.00 12.76 ?  115 ASN   A CG   1 
ATOM   2307 O OD1  . ASN   A 1 115 ? 31.231 -9.774  0.741   1.00 15.79 ?  115 ASN   A OD1  1 
ATOM   2308 N ND2  . ASN   A 1 115 ? 29.343 -9.343  -0.372  1.00 12.43 ?  115 ASN   A ND2  1 
ATOM   2309 H H    . ASN   A 1 115 ? 28.038 -11.593 0.709   1.00 13.49 ?  115 ASN   A H    1 
ATOM   2310 H HA   . ASN   A 1 115 ? 30.003 -11.712 2.398   1.00 14.11 ?  115 ASN   A HA   1 
ATOM   2311 H HB2  . ASN   A 1 115 ? 28.319 -9.518  1.846   1.00 14.46 ?  115 ASN   A HB2  1 
ATOM   2312 H HB3  . ASN   A 1 115 ? 29.647 -9.395  2.710   1.00 14.46 ?  115 ASN   A HB3  1 
ATOM   2313 H HD21 . ASN   A 1 115 ? 29.761 -9.209  -1.108  1.00 14.91 ?  115 ASN   A HD21 1 
ATOM   2314 H HD22 . ASN   A 1 115 ? 28.482 -9.286  -0.347  1.00 14.91 ?  115 ASN   A HD22 1 
ATOM   2315 N N    . PHE   A 1 116 ? 27.165 -11.647 3.824   1.00 11.63 ?  116 PHE   A N    1 
ATOM   2316 C CA   . PHE   A 1 116 ? 26.516 -11.752 5.127   1.00 11.70 ?  116 PHE   A CA   1 
ATOM   2317 C C    . PHE   A 1 116 ? 26.991 -12.988 5.891   1.00 12.08 ?  116 PHE   A C    1 
ATOM   2318 O O    . PHE   A 1 116 ? 26.918 -13.013 7.122   1.00 12.46 ?  116 PHE   A O    1 
ATOM   2319 C CB   . PHE   A 1 116 ? 24.990 -11.886 4.985   1.00 11.90 ?  116 PHE   A CB   1 
ATOM   2320 C CG   . PHE   A 1 116 ? 24.238 -10.636 4.525   1.00 11.63 ?  116 PHE   A CG   1 
ATOM   2321 C CD1  . PHE   A 1 116 ? 24.812 -9.610  3.783   1.00 11.50 ?  116 PHE   A CD1  1 
ATOM   2322 C CD2  . PHE   A 1 116 ? 22.880 -10.538 4.833   1.00 12.18 ?  116 PHE   A CD2  1 
ATOM   2323 C CE1  . PHE   A 1 116 ? 24.047 -8.532  3.363   1.00 11.95 ?  116 PHE   A CE1  1 
ATOM   2324 C CE2  . PHE   A 1 116 ? 22.121 -9.460  4.423   1.00 12.43 ?  116 PHE   A CE2  1 
ATOM   2325 C CZ   . PHE   A 1 116 ? 22.698 -8.454  3.687   1.00 11.77 ?  116 PHE   A CZ   1 
ATOM   2326 H H    . PHE   A 1 116 ? 26.626 -11.688 3.150   1.00 13.96 ?  116 PHE   A H    1 
ATOM   2327 H HA   . PHE   A 1 116 ? 26.703 -10.964 5.659   1.00 14.04 ?  116 PHE   A HA   1 
ATOM   2328 H HB2  . PHE   A 1 116 ? 24.803 -12.588 4.339   1.00 14.28 ?  116 PHE   A HB2  1 
ATOM   2329 H HB3  . PHE   A 1 116 ? 24.622 -12.144 5.847   1.00 14.28 ?  116 PHE   A HB3  1 
ATOM   2330 H HD1  . PHE   A 1 116 ? 25.707 -9.670  3.555   1.00 13.80 ?  116 PHE   A HD1  1 
ATOM   2331 H HD2  . PHE   A 1 116 ? 22.472 -11.226 5.324   1.00 14.61 ?  116 PHE   A HD2  1 
ATOM   2332 H HE1  . PHE   A 1 116 ? 24.446 -7.853  2.874   1.00 14.34 ?  116 PHE   A HE1  1 
ATOM   2333 H HE2  . PHE   A 1 116 ? 21.218 -9.423  4.649   1.00 14.91 ?  116 PHE   A HE2  1 
ATOM   2334 H HZ   . PHE   A 1 116 ? 22.191 -7.724  3.422   1.00 14.13 ?  116 PHE   A HZ   1 
ATOM   2335 N N    . ASN   A 1 117 ? 27.432 -14.036 5.184   1.00 12.30 ?  117 ASN   A N    1 
ATOM   2336 C CA   . ASN   A 1 117 ? 27.806 -15.285 5.849   1.00 12.77 ?  117 ASN   A CA   1 
ATOM   2337 C C    . ASN   A 1 117 ? 29.071 -15.166 6.682   1.00 13.15 ?  117 ASN   A C    1 
ATOM   2338 O O    . ASN   A 1 117 ? 29.371 -16.086 7.451   1.00 13.99 ?  117 ASN   A O    1 
ATOM   2339 C CB   . ASN   A 1 117 ? 27.925 -16.405 4.828   1.00 12.60 ?  117 ASN   A CB   1 
ATOM   2340 C CG   . ASN   A 1 117 ? 26.571 -16.796 4.288   1.00 12.38 ?  117 ASN   A CG   1 
ATOM   2341 O OD1  . ASN   A 1 117 ? 25.590 -16.822 5.037   1.00 13.29 ?  117 ASN   A OD1  1 
ATOM   2342 N ND2  . ASN   A 1 117 ? 26.488 -17.049 2.992   1.00 12.51 ?  117 ASN   A ND2  1 
ATOM   2343 H H    . ASN   A 1 117 ? 27.500 -14.049 4.323   1.00 14.75 ?  117 ASN   A H    1 
ATOM   2344 H HA   . ASN   A 1 117 ? 27.084 -15.524 6.453   1.00 15.32 ?  117 ASN   A HA   1 
ATOM   2345 H HB2  . ASN   A 1 117 ? 28.474 -16.106 4.085   1.00 15.12 ?  117 ASN   A HB2  1 
ATOM   2346 H HB3  . ASN   A 1 117 ? 28.318 -17.180 5.250   1.00 15.12 ?  117 ASN   A HB3  1 
ATOM   2347 H HD21 . ASN   A 1 117 ? 25.736 -17.264 2.646   1.00 15.02 ?  117 ASN   A HD21 1 
ATOM   2348 H HD22 . ASN   A 1 117 ? 27.195 -17.002 2.499   1.00 15.02 ?  117 ASN   A HD22 1 
ATOM   2349 N N    . GLN   A 1 118 ? 29.800 -14.057 6.565   1.00 12.99 ?  118 GLN   A N    1 
ATOM   2350 C CA   . GLN   A 1 118 ? 30.982 -13.822 7.383   1.00 13.65 ?  118 GLN   A CA   1 
ATOM   2351 C C    . GLN   A 1 118 ? 30.641 -13.251 8.754   1.00 13.49 ?  118 GLN   A C    1 
ATOM   2352 O O    . GLN   A 1 118 ? 31.554 -12.974 9.542   1.00 15.30 ?  118 GLN   A O    1 
ATOM   2353 C CB   . GLN   A 1 118 ? 31.968 -12.914 6.644   1.00 13.70 ?  118 GLN   A CB   1 
ATOM   2354 C CG   . GLN   A 1 118 ? 32.450 -13.491 5.323   1.00 13.37 ?  118 GLN   A CG   1 
ATOM   2355 C CD   . GLN   A 1 118 ? 33.273 -14.753 5.499   1.00 13.94 ?  118 GLN   A CD   1 
ATOM   2356 O OE1  . GLN   A 1 118 ? 34.126 -14.828 6.391   1.00 14.58 ?  118 GLN   A OE1  1 
ATOM   2357 N NE2  . GLN   A 1 118 ? 33.025 -15.756 4.648   1.00 14.10 ?  118 GLN   A NE2  1 
ATOM   2358 H H    . GLN   A 1 118 ? 29.617 -13.412 6.017   1.00 15.59 ?  118 GLN   A H    1 
ATOM   2359 H HA   . GLN   A 1 118 ? 31.415 -14.679 7.523   1.00 16.39 ?  118 GLN   A HA   1 
ATOM   2360 H HB2  . GLN   A 1 118 ? 31.534 -12.066 6.466   1.00 16.44 ?  118 GLN   A HB2  1 
ATOM   2361 H HB3  . GLN   A 1 118 ? 32.741 -12.778 7.213   1.00 16.44 ?  118 GLN   A HB3  1 
ATOM   2362 H HG2  . GLN   A 1 118 ? 31.680 -13.699 4.767   1.00 16.05 ?  118 GLN   A HG2  1 
ATOM   2363 H HG3  . GLN   A 1 118 ? 33.007 -12.832 4.878   1.00 16.05 ?  118 GLN   A HG3  1 
ATOM   2364 H HE21 . GLN   A 1 118 ? 32.418 -15.665 4.034   1.00 16.92 ?  118 GLN   A HE21 1 
ATOM   2365 H HE22 . GLN   A 1 118 ? 33.457 -16.495 4.705   1.00 16.92 ?  118 GLN   A HE22 1 
ATOM   2366 N N    . HIS   A 1 119 ? 29.351 -13.092 9.064   1.00 13.03 ?  119 HIS   A N    1 
ATOM   2367 C CA   . HIS   A 1 119 ? 28.884 -12.490 10.310  1.00 13.55 ?  119 HIS   A CA   1 
ATOM   2368 C C    . HIS   A 1 119 ? 27.745 -13.315 10.889  1.00 13.75 ?  119 HIS   A C    1 
ATOM   2369 O O    . HIS   A 1 119 ? 26.792 -13.644 10.179  1.00 14.38 ?  119 HIS   A O    1 
ATOM   2370 C CB   . HIS   A 1 119 ? 28.427 -11.057 10.038  1.00 14.03 ?  119 HIS   A CB   1 
ATOM   2371 C CG   . HIS   A 1 119 ? 29.513 -10.236 9.445   1.00 15.20 ?  119 HIS   A CG   1 
ATOM   2372 N ND1  . HIS   A 1 119 ? 30.474 -9.627  10.218  1.00 17.59 ?  119 HIS   A ND1  1 
ATOM   2373 C CD2  . HIS   A 1 119 ? 29.869 -10.027 8.157   1.00 16.05 ?  119 HIS   A CD2  1 
ATOM   2374 C CE1  . HIS   A 1 119 ? 31.350 -9.030  9.430   1.00 18.43 ?  119 HIS   A CE1  1 
ATOM   2375 N NE2  . HIS   A 1 119 ? 31.016 -9.269  8.174   1.00 17.97 ?  119 HIS   A NE2  1 
ATOM   2376 H H    . HIS   A 1 119 ? 28.701 -13.347 8.553   1.00 15.64 ?  119 HIS   A H    1 
ATOM   2377 H HA   . HIS   A 1 119 ? 29.612 -12.475 10.952  1.00 16.26 ?  119 HIS   A HA   1 
ATOM   2378 H HB2  . HIS   A 1 119 ? 27.683 -11.081 9.416   1.00 16.83 ?  119 HIS   A HB2  1 
ATOM   2379 H HB3  . HIS   A 1 119 ? 28.155 -10.654 10.875  1.00 16.83 ?  119 HIS   A HB3  1 
ATOM   2380 H HD1  . HIS   A 1 119 ? 30.488 -9.623  11.080  1.00 21.11 ?  119 HIS   A HD1  1 
ATOM   2381 H HD2  . HIS   A 1 119 ? 29.426 -10.338 7.402   1.00 19.26 ?  119 HIS   A HD2  1 
ATOM   2382 H HE1  . HIS   A 1 119 ? 32.078 -8.527  9.717   1.00 22.11 ?  119 HIS   A HE1  1 
ATOM   2383 N N    . GLU   A 1 120 ? 27.836 -13.626 12.185  1.00 15.12 ?  120 GLU   A N    1 
ATOM   2384 C CA   . GLU   A 1 120 ? 26.883 -14.555 12.787  1.00 17.18 ?  120 GLU   A CA   1 
ATOM   2385 C C    . GLU   A 1 120 ? 25.466 -13.989 12.844  1.00 15.54 ?  120 GLU   A C    1 
ATOM   2386 O O    . GLU   A 1 120 ? 24.490 -14.748 12.735  1.00 15.47 ?  120 GLU   A O    1 
ATOM   2387 C CB   . GLU   A 1 120 ? 27.352 -14.969 14.184  1.00 22.67 ?  120 GLU   A CB   1 
ATOM   2388 C CG   . GLU   A 1 120 ? 28.555 -15.898 14.181  1.00 29.27 ?  120 GLU   A CG   1 
ATOM   2389 C CD   . GLU   A 1 120 ? 28.715 -16.642 15.492  1.00 36.91 ?  120 GLU   A CD   1 
ATOM   2390 O OE1  . GLU   A 1 120 ? 28.387 -16.063 16.550  1.00 39.30 ?  120 GLU   A OE1  1 
ATOM   2391 O OE2  . GLU   A 1 120 ? 29.164 -17.807 15.462  1.00 42.83 -1 120 GLU   A OE2  1 
ATOM   2392 H H    . GLU   A 1 120 ? 28.436 -13.324 12.726  1.00 18.15 ?  120 GLU   A H    1 
ATOM   2393 H HA   . GLU   A 1 120 ? 26.850 -15.356 12.249  1.00 20.61 ?  120 GLU   A HA   1 
ATOM   2394 H HB2  . GLU   A 1 120 ? 27.597 -14.179 14.687  1.00 27.21 ?  120 GLU   A HB2  1 
ATOM   2395 H HB3  . GLU   A 1 120 ? 26.627 -15.434 14.636  1.00 27.21 ?  120 GLU   A HB3  1 
ATOM   2396 H HG2  . GLU   A 1 120 ? 28.457 -16.544 13.463  1.00 35.13 ?  120 GLU   A HG2  1 
ATOM   2397 H HG3  . GLU   A 1 120 ? 29.361 -15.377 14.055  1.00 35.13 ?  120 GLU   A HG3  1 
ATOM   2398 N N    . VAL   A 1 121 ? 25.333 -12.678 13.066  1.00 15.14 ?  121 VAL   A N    1 
ATOM   2399 C CA   . VAL   A 1 121 ? 24.040 -12.009 13.196  1.00 14.85 ?  121 VAL   A CA   1 
ATOM   2400 C C    . VAL   A 1 121 ? 24.152 -10.630 12.560  1.00 13.65 ?  121 VAL   A C    1 
ATOM   2401 O O    . VAL   A 1 121 ? 25.124 -9.908  12.803  1.00 14.73 ?  121 VAL   A O    1 
ATOM   2402 C CB   . VAL   A 1 121 ? 23.618 -11.856 14.675  1.00 17.85 ?  121 VAL   A CB   1 
ATOM   2403 C CG1  . VAL   A 1 121 ? 22.226 -11.245 14.777  1.00 18.57 ?  121 VAL   A CG1  1 
ATOM   2404 C CG2  . VAL   A 1 121 ? 23.660 -13.183 15.411  1.00 20.59 ?  121 VAL   A CG2  1 
ATOM   2405 H H    . VAL   A 1 121 ? 26.000 -12.135 13.145  1.00 18.16 ?  121 VAL   A H    1 
ATOM   2406 H HA   . VAL   A 1 121 ? 23.361 -12.521 12.733  1.00 17.82 ?  121 VAL   A HA   1 
ATOM   2407 H HB   . VAL   A 1 121 ? 24.234 -11.256 15.120  1.00 21.42 ?  121 VAL   A HB   1 
ATOM   2408 H HG11 . VAL   A 1 121 ? 21.922 -11.297 15.699  1.00 22.29 ?  121 VAL   A HG11 1 
ATOM   2409 H HG12 . VAL   A 1 121 ? 22.262 -10.319 14.495  1.00 22.29 ?  121 VAL   A HG12 1 
ATOM   2410 H HG13 . VAL   A 1 121 ? 21.618 -11.744 14.206  1.00 22.29 ?  121 VAL   A HG13 1 
ATOM   2411 H HG21 . VAL   A 1 121 ? 23.313 -13.058 16.314  1.00 24.71 ?  121 VAL   A HG21 1 
ATOM   2412 H HG22 . VAL   A 1 121 ? 23.107 -13.827 14.939  1.00 24.71 ?  121 VAL   A HG22 1 
ATOM   2413 H HG23 . VAL   A 1 121 ? 24.574 -13.497 15.452  1.00 24.71 ?  121 VAL   A HG23 1 
ATOM   2414 N N    . LEU   A 1 122 ? 23.146 -10.248 11.770  1.00 13.35 ?  122 LEU   A N    1 
ATOM   2415 C CA   . LEU   A 1 122 ? 23.145 -8.945  11.112  1.00 13.11 ?  122 LEU   A CA   1 
ATOM   2416 C C    . LEU   A 1 122 ? 21.750 -8.348  11.067  1.00 13.02 ?  122 LEU   A C    1 
ATOM   2417 O O    . LEU   A 1 122 ? 20.762 -9.067  10.924  1.00 13.96 ?  122 LEU   A O    1 
ATOM   2418 C CB   . LEU   A 1 122 ? 23.587 -9.027  9.647   1.00 14.79 ?  122 LEU   A CB   1 
ATOM   2419 C CG   . LEU   A 1 122 ? 24.782 -9.884  9.267   1.00 14.60 ?  122 LEU   A CG   1 
ATOM   2420 C CD1  . LEU   A 1 122 ? 24.347 -11.321 9.031   1.00 15.56 ?  122 LEU   A CD1  1 
ATOM   2421 C CD2  . LEU   A 1 122 ? 25.444 -9.308  8.031   1.00 14.00 ?  122 LEU   A CD2  1 
ATOM   2422 H H    . LEU   A 1 122 ? 22.445 -10.728 11.595  1.00 16.02 ?  122 LEU   A H    1 
ATOM   2423 H HA   . LEU   A 1 122 ? 23.734 -8.336  11.586  1.00 15.73 ?  122 LEU   A HA   1 
ATOM   2424 H HB2  . LEU   A 1 122 ? 22.844 -9.361  9.130   1.00 17.74 ?  122 LEU   A HB2  1 
ATOM   2425 H HB3  . LEU   A 1 122 ? 23.798 -8.127  9.352   1.00 17.74 ?  122 LEU   A HB3  1 
ATOM   2426 H HG   . LEU   A 1 122 ? 25.442 -9.878  9.985   1.00 17.52 ?  122 LEU   A HG   1 
ATOM   2427 H HD11 . LEU   A 1 122 ? 25.110 -11.847 8.747   1.00 18.67 ?  122 LEU   A HD11 1 
ATOM   2428 H HD12 . LEU   A 1 122 ? 23.987 -11.681 9.856   1.00 18.67 ?  122 LEU   A HD12 1 
ATOM   2429 H HD13 . LEU   A 1 122 ? 23.665 -11.332 8.340   1.00 18.67 ?  122 LEU   A HD13 1 
ATOM   2430 H HD21 . LEU   A 1 122 ? 26.180 -9.888  7.757   1.00 16.80 ?  122 LEU   A HD21 1 
ATOM   2431 H HD22 . LEU   A 1 122 ? 24.791 -9.253  7.317   1.00 16.80 ?  122 LEU   A HD22 1 
ATOM   2432 H HD23 . LEU   A 1 122 ? 25.789 -8.423  8.233   1.00 16.80 ?  122 LEU   A HD23 1 
ATOM   2433 N N    A LEU   A 1 123 ? 21.679 -7.020  11.167  0.76 12.49 ?  123 LEU   A N    1 
ATOM   2434 N N    B LEU   A 1 123 ? 21.699 -7.022  11.206  0.24 12.85 ?  123 LEU   A N    1 
ATOM   2435 C CA   A LEU   A 1 123 ? 20.506 -6.232  10.789  0.76 12.68 ?  123 LEU   A CA   1 
ATOM   2436 C CA   B LEU   A 1 123 ? 20.527 -6.211  10.895  0.24 12.87 ?  123 LEU   A CA   1 
ATOM   2437 C C    A LEU   A 1 123 ? 20.748 -5.707  9.382   0.76 11.77 ?  123 LEU   A C    1 
ATOM   2438 C C    B LEU   A 1 123 ? 20.763 -5.638  9.501   0.24 12.25 ?  123 LEU   A C    1 
ATOM   2439 O O    A LEU   A 1 123 ? 21.829 -5.176  9.110   0.76 11.66 ?  123 LEU   A O    1 
ATOM   2440 O O    B LEU   A 1 123 ? 21.650 -4.798  9.315   0.24 11.79 ?  123 LEU   A O    1 
ATOM   2441 C CB   A LEU   A 1 123 ? 20.358 -5.043  11.741  0.76 12.99 ?  123 LEU   A CB   1 
ATOM   2442 C CB   B LEU   A 1 123 ? 20.382 -5.094  11.928  0.24 13.27 ?  123 LEU   A CB   1 
ATOM   2443 C CG   A LEU   A 1 123 ? 19.303 -3.984  11.411  0.76 14.18 ?  123 LEU   A CG   1 
ATOM   2444 C CG   B LEU   A 1 123 ? 19.410 -3.969  11.560  0.24 13.65 ?  123 LEU   A CG   1 
ATOM   2445 C CD1  A LEU   A 1 123 ? 17.904 -4.575  11.414  0.76 14.77 ?  123 LEU   A CD1  1 
ATOM   2446 C CD1  B LEU   A 1 123 ? 17.977 -4.479  11.522  0.24 13.87 ?  123 LEU   A CD1  1 
ATOM   2447 C CD2  A LEU   A 1 123 ? 19.408 -2.823  12.402  0.76 14.76 ?  123 LEU   A CD2  1 
ATOM   2448 C CD2  B LEU   A 1 123 ? 19.549 -2.789  12.514  0.24 13.84 ?  123 LEU   A CD2  1 
ATOM   2449 H H    A LEU   A 1 123 ? 22.333 -6.533  11.459  0.76 14.99 ?  123 LEU   A H    1 
ATOM   2450 H H    B LEU   A 1 123 ? 22.364 -6.548  11.486  0.24 15.42 ?  123 LEU   A H    1 
ATOM   2451 H HA   A LEU   A 1 123 ? 19.709 -6.779  10.806  0.76 15.22 ?  123 LEU   A HA   1 
ATOM   2452 H HA   B LEU   A 1 123 ? 19.726 -6.756  10.891  0.24 15.44 ?  123 LEU   A HA   1 
ATOM   2453 H HB2  A LEU   A 1 123 ? 20.130 -5.393  12.617  0.76 15.59 ?  123 LEU   A HB2  1 
ATOM   2454 H HB2  B LEU   A 1 123 ? 20.070 -5.486  12.762  0.24 15.93 ?  123 LEU   A HB2  1 
ATOM   2455 H HB3  A LEU   A 1 123 ? 21.206 -4.587  11.788  0.76 15.59 ?  123 LEU   A HB3  1 
ATOM   2456 H HB3  B LEU   A 1 123 ? 21.253 -4.690  12.072  0.24 15.93 ?  123 LEU   A HB3  1 
ATOM   2457 H HG   A LEU   A 1 123 ? 19.471 -3.622  10.525  0.76 17.02 ?  123 LEU   A HG   1 
ATOM   2458 H HG   B LEU   A 1 123 ? 19.627 -3.644  10.676  0.24 16.38 ?  123 LEU   A HG   1 
ATOM   2459 H HD11 A LEU   A 1 123 ? 17.260 -3.873  11.225  0.76 17.73 ?  123 LEU   A HD11 1 
ATOM   2460 H HD11 B LEU   A 1 123 ? 17.388 -3.741  11.300  0.24 16.64 ?  123 LEU   A HD11 1 
ATOM   2461 H HD12 A LEU   A 1 123 ? 17.852 -5.263  10.734  0.76 17.73 ?  123 LEU   A HD12 1 
ATOM   2462 H HD12 B LEU   A 1 123 ? 17.906 -5.173  10.847  0.24 16.64 ?  123 LEU   A HD12 1 
ATOM   2463 H HD13 A LEU   A 1 123 ? 17.726 -4.957  12.288  0.76 17.73 ?  123 LEU   A HD13 1 
ATOM   2464 H HD13 B LEU   A 1 123 ? 17.745 -4.838  12.392  0.24 16.64 ?  123 LEU   A HD13 1 
ATOM   2465 H HD21 A LEU   A 1 123 ? 18.737 -2.155  12.188  0.76 17.71 ?  123 LEU   A HD21 1 
ATOM   2466 H HD21 B LEU   A 1 123 ? 18.921 -2.097  12.252  0.24 16.61 ?  123 LEU   A HD21 1 
ATOM   2467 H HD22 A LEU   A 1 123 ? 19.257 -3.163  13.302  0.76 17.71 ?  123 LEU   A HD22 1 
ATOM   2468 H HD22 B LEU   A 1 123 ? 19.356 -3.086  13.417  0.24 16.61 ?  123 LEU   A HD22 1 
ATOM   2469 H HD23 A LEU   A 1 123 ? 20.294 -2.433  12.344  0.76 17.71 ?  123 LEU   A HD23 1 
ATOM   2470 H HD23 B LEU   A 1 123 ? 20.456 -2.448  12.464  0.24 16.61 ?  123 LEU   A HD23 1 
ATOM   2471 N N    A ALA   A 1 124 ? 19.760 -5.827  8.494   0.76 10.99 ?  124 ALA   A N    1 
ATOM   2472 N N    B ALA   A 1 124 ? 19.978 -6.087  8.526   0.24 11.97 ?  124 ALA   A N    1 
ATOM   2473 C CA   A ALA   A 1 124 ? 20.044 -5.547  7.094   0.76 10.86 ?  124 ALA   A CA   1 
ATOM   2474 C CA   B ALA   A 1 124 ? 20.264 -5.818  7.127   0.24 12.35 ?  124 ALA   A CA   1 
ATOM   2475 C C    A ALA   A 1 124 ? 18.797 -5.103  6.340   0.76 11.04 ?  124 ALA   A C    1 
ATOM   2476 C C    B ALA   A 1 124 ? 19.036 -5.298  6.392   0.24 11.97 ?  124 ALA   A C    1 
ATOM   2477 O O    A ALA   A 1 124 ? 17.670 -5.470  6.704   0.76 11.74 ?  124 ALA   A O    1 
ATOM   2478 O O    B ALA   A 1 124 ? 17.901 -5.592  6.779   0.24 12.27 ?  124 ALA   A O    1 
ATOM   2479 C CB   A ALA   A 1 124 ? 20.643 -6.776  6.404   0.76 11.43 ?  124 ALA   A CB   1 
ATOM   2480 C CB   B ALA   A 1 124 ? 20.755 -7.092  6.422   0.24 12.97 ?  124 ALA   A CB   1 
ATOM   2481 H H    A ALA   A 1 124 ? 18.945 -6.047  8.671   0.76 13.19 ?  124 ALA   A H    1 
ATOM   2482 H H    B ALA   A 1 124 ? 19.271 -6.553  8.656   0.24 14.36 ?  124 ALA   A H    1 
ATOM   2483 H HA   A ALA   A 1 124 ? 20.701 -4.834  7.053   0.76 13.03 ?  124 ALA   A HA   1 
ATOM   2484 H HA   B ALA   A 1 124 ? 20.966 -5.157  7.080   0.24 14.82 ?  124 ALA   A HA   1 
ATOM   2485 H HB1  A ALA   A 1 124 ? 20.828 -6.564  5.478   0.76 13.72 ?  124 ALA   A HB1  1 
ATOM   2486 H HB1  B ALA   A 1 124 ? 20.941 -6.888  5.491   0.24 15.57 ?  124 ALA   A HB1  1 
ATOM   2487 H HB2  A ALA   A 1 124 ? 21.471 -7.020  6.857   0.76 13.72 ?  124 ALA   A HB2  1 
ATOM   2488 H HB2  B ALA   A 1 124 ? 21.565 -7.408  6.857   0.24 15.57 ?  124 ALA   A HB2  1 
ATOM   2489 H HB3  A ALA   A 1 124 ? 20.013 -7.510  6.459   0.76 13.72 ?  124 ALA   A HB3  1 
ATOM   2490 H HB3  B ALA   A 1 124 ? 20.066 -7.773  6.479   0.24 15.57 ?  124 ALA   A HB3  1 
ATOM   2491 N N    A PRO   A 1 125 ? 18.978 -4.354  5.251   0.76 10.90 ?  125 PRO   A N    1 
ATOM   2492 N N    B PRO   A 1 125 ? 19.238 -4.529  5.323   0.24 10.82 ?  125 PRO   A N    1 
ATOM   2493 C CA   A PRO   A 1 125 ? 17.923 -4.140  4.263   0.76 11.68 ?  125 PRO   A CA   1 
ATOM   2494 C CA   B PRO   A 1 125 ? 18.134 -4.153  4.441   0.24 10.73 ?  125 PRO   A CA   1 
ATOM   2495 C C    A PRO   A 1 125 ? 17.999 -5.217  3.185   0.76 12.10 ?  125 PRO   A C    1 
ATOM   2496 C C    B PRO   A 1 125 ? 18.078 -5.133  3.272   0.24 11.38 ?  125 PRO   A C    1 
ATOM   2497 O O    A PRO   A 1 125 ? 18.974 -5.962  3.083   0.76 12.39 ?  125 PRO   A O    1 
ATOM   2498 O O    B PRO   A 1 125 ? 18.981 -5.948  3.074   0.24 11.42 ?  125 PRO   A O    1 
ATOM   2499 C CB   A PRO   A 1 125 ? 18.343 -2.791  3.661   0.76 11.92 ?  125 PRO   A CB   1 
ATOM   2500 C CB   B PRO   A 1 125 ? 18.578 -2.769  3.952   0.24 10.11 ?  125 PRO   A CB   1 
ATOM   2501 C CG   A PRO   A 1 125 ? 19.846 -2.942  3.559   0.76 11.97 ?  125 PRO   A CG   1 
ATOM   2502 C CG   B PRO   A 1 125 ? 20.076 -2.907  3.827   0.24 10.20 ?  125 PRO   A CG   1 
ATOM   2503 C CD   A PRO   A 1 125 ? 20.228 -3.677  4.845   0.76 11.66 ?  125 PRO   A CD   1 
ATOM   2504 C CD   B PRO   A 1 125 ? 20.510 -3.925  4.878   0.24 10.41 ?  125 PRO   A CD   1 
ATOM   2505 H HA   A PRO   A 1 125 ? 17.040 -4.097  4.666   0.76 14.02 ?  125 PRO   A HA   1 
ATOM   2506 H HA   B PRO   A 1 125 ? 17.296 -4.095  4.929   0.24 12.88 ?  125 PRO   A HA   1 
ATOM   2507 H HB2  A PRO   A 1 125 ? 17.931 -2.672  2.789   0.76 14.31 ?  125 PRO   A HB2  1 
ATOM   2508 H HB2  B PRO   A 1 125 ? 18.169 -2.575  3.093   0.24 12.13 ?  125 PRO   A HB2  1 
ATOM   2509 H HB3  A PRO   A 1 125 ? 18.097 -2.068  4.265   0.76 14.31 ?  125 PRO   A HB3  1 
ATOM   2510 H HB3  B PRO   A 1 125 ? 18.342 -2.090  4.608   0.24 12.13 ?  125 PRO   A HB3  1 
ATOM   2511 H HG2  A PRO   A 1 125 ? 20.073 -3.472  2.776   0.76 14.37 ?  125 PRO   A HG2  1 
ATOM   2512 H HG2  B PRO   A 1 125 ? 20.297 -3.222  2.936   0.24 12.24 ?  125 PRO   A HG2  1 
ATOM   2513 H HG3  A PRO   A 1 125 ? 20.263 -2.067  3.515   0.76 14.37 ?  125 PRO   A HG3  1 
ATOM   2514 H HG3  B PRO   A 1 125 ? 20.495 -2.047  3.992   0.24 12.24 ?  125 PRO   A HG3  1 
ATOM   2515 H HD2  A PRO   A 1 125 ? 20.932 -4.317  4.671   0.76 13.99 ?  125 PRO   A HD2  1 
ATOM   2516 H HD2  B PRO   A 1 125 ? 21.095 -4.592  4.476   0.24 12.50 ?  125 PRO   A HD2  1 
ATOM   2517 H HD3  A PRO   A 1 125 ? 20.497 -3.033  5.526   0.76 13.99 ?  125 PRO   A HD3  1 
ATOM   2518 H HD3  B PRO   A 1 125 ? 20.951 -3.473  5.616   0.24 12.50 ?  125 PRO   A HD3  1 
ATOM   2519 N N    A LEU   A 1 126 ? 16.961 -5.256  2.351   0.76 12.28 ?  126 LEU   A N    1 
ATOM   2520 N N    B LEU   A 1 126 ? 17.003 -5.040  2.484   0.24 11.94 ?  126 LEU   A N    1 
ATOM   2521 C CA   A LEU   A 1 126 ? 16.984 -6.087  1.154   0.76 12.39 ?  126 LEU   A CA   1 
ATOM   2522 C CA   B LEU   A 1 126 ? 16.933 -5.830  1.260   0.24 12.09 ?  126 LEU   A CA   1 
ATOM   2523 C C    A LEU   A 1 126 ? 17.908 -5.472  0.105   0.76 12.19 ?  126 LEU   A C    1 
ATOM   2524 C C    B LEU   A 1 126 ? 17.850 -5.213  0.210   0.24 11.82 ?  126 LEU   A C    1 
ATOM   2525 O O    A LEU   A 1 126 ? 17.667 -4.366  -0.394  0.76 13.16 ?  126 LEU   A O    1 
ATOM   2526 O O    B LEU   A 1 126 ? 17.619 -4.085  -0.239  0.24 12.73 ?  126 LEU   A O    1 
ATOM   2527 C CB   A LEU   A 1 126 ? 15.575 -6.249  0.597   0.76 12.99 ?  126 LEU   A CB   1 
ATOM   2528 C CB   B LEU   A 1 126 ? 15.504 -5.897  0.729   0.24 12.80 ?  126 LEU   A CB   1 
ATOM   2529 C CG   A LEU   A 1 126 ? 14.676 -7.209  1.377   0.76 14.26 ?  126 LEU   A CG   1 
ATOM   2530 C CG   B LEU   A 1 126 ? 14.547 -6.853  1.439   0.24 13.07 ?  126 LEU   A CG   1 
ATOM   2531 C CD1  A LEU   A 1 126 ? 13.235 -7.071  0.917   0.76 16.13 ?  126 LEU   A CD1  1 
ATOM   2532 C CD1  B LEU   A 1 126 ? 13.186 -6.819  0.765   0.24 13.68 ?  126 LEU   A CD1  1 
ATOM   2533 C CD2  A LEU   A 1 126 ? 15.151 -8.651  1.218   0.76 13.81 ?  126 LEU   A CD2  1 
ATOM   2534 C CD2  B LEU   A 1 126 ? 15.099 -8.271  1.456   0.24 13.07 ?  126 LEU   A CD2  1 
ATOM   2535 H H    A LEU   A 1 126 ? 16.237 -4.802  2.450   0.76 14.73 ?  126 LEU   A H    1 
ATOM   2536 H H    B LEU   A 1 126 ? 16.300 -4.543  2.623   0.24 14.33 ?  126 LEU   A H    1 
ATOM   2537 H HA   A LEU   A 1 126 ? 17.328 -6.963  1.380   0.76 14.87 ?  126 LEU   A HA   1 
ATOM   2538 H HA   B LEU   A 1 126 ? 17.244 -6.732  1.446   0.24 14.51 ?  126 LEU   A HA   1 
ATOM   2539 H HB2  A LEU   A 1 126 ? 15.139 -5.382  0.598   0.76 15.59 ?  126 LEU   A HB2  1 
ATOM   2540 H HB2  B LEU   A 1 126 ? 15.121 -5.009  0.787   0.24 15.36 ?  126 LEU   A HB2  1 
ATOM   2541 H HB3  A LEU   A 1 126 ? 15.636 -6.582  -0.311  0.76 15.59 ?  126 LEU   A HB3  1 
ATOM   2542 H HB3  B LEU   A 1 126 ? 15.544 -6.168  -0.203  0.24 15.36 ?  126 LEU   A HB3  1 
ATOM   2543 H HG   A LEU   A 1 126 ? 14.714 -6.986  2.321   0.76 17.11 ?  126 LEU   A HG   1 
ATOM   2544 H HG   B LEU   A 1 126 ? 14.435 -6.563  2.357   0.24 15.68 ?  126 LEU   A HG   1 
ATOM   2545 H HD11 A LEU   A 1 126 ? 12.684 -7.689  1.417   0.76 19.36 ?  126 LEU   A HD11 1 
ATOM   2546 H HD11 B LEU   A 1 126 ? 12.590 -7.425  1.231   0.24 16.42 ?  126 LEU   A HD11 1 
ATOM   2547 H HD12 A LEU   A 1 126 ? 12.944 -6.160  1.074   0.76 19.36 ?  126 LEU   A HD12 1 
ATOM   2548 H HD12 B LEU   A 1 126 ? 12.839 -5.917  0.800   0.24 16.42 ?  126 LEU   A HD12 1 
ATOM   2549 H HD13 A LEU   A 1 126 ? 13.189 -7.276  -0.031  0.76 19.36 ?  126 LEU   A HD13 1 
ATOM   2550 H HD13 B LEU   A 1 126 ? 13.287 -7.101  -0.159  0.24 16.42 ?  126 LEU   A HD13 1 
ATOM   2551 H HD21 A LEU   A 1 126 ? 14.497 -9.248  1.610   0.76 16.57 ?  126 LEU   A HD21 1 
ATOM   2552 H HD21 B LEU   A 1 126 ? 14.389 -8.883  1.696   0.24 15.69 ?  126 LEU   A HD21 1 
ATOM   2553 H HD22 A LEU   A 1 126 ? 15.257 -8.847  0.273   0.76 16.57 ?  126 LEU   A HD22 1 
ATOM   2554 H HD22 B LEU   A 1 126 ? 15.441 -8.487  0.574   0.24 15.69 ?  126 LEU   A HD22 1 
ATOM   2555 H HD23 A LEU   A 1 126 ? 16.006 -8.756  1.671   0.76 16.57 ?  126 LEU   A HD23 1 
ATOM   2556 H HD23 B LEU   A 1 126 ? 15.816 -8.323  2.109   0.24 15.69 ?  126 LEU   A HD23 1 
ATOM   2557 N N    A LEU   A 1 127 ? 18.958 -6.202  -0.246  0.76 12.03 ?  127 LEU   A N    1 
ATOM   2558 N N    B LEU   A 1 127 ? 18.877 -5.953  -0.196  0.24 11.13 ?  127 LEU   A N    1 
ATOM   2559 C CA   A LEU   A 1 127 ? 19.939 -5.696  -1.192  0.76 11.76 ?  127 LEU   A CA   1 
ATOM   2560 C CA   B LEU   A 1 127 ? 19.855 -5.413  -1.127  0.24 10.76 ?  127 LEU   A CA   1 
ATOM   2561 C C    A LEU   A 1 127 ? 19.317 -5.496  -2.564  0.76 11.44 ?  127 LEU   A C    1 
ATOM   2562 C C    B LEU   A 1 127 ? 19.286 -5.346  -2.538  0.24 11.25 ?  127 LEU   A C    1 
ATOM   2563 O O    A LEU   A 1 127 ? 18.503 -6.298  -3.031  0.76 11.93 ?  127 LEU   A O    1 
ATOM   2564 O O    B LEU   A 1 127 ? 18.416 -6.131  -2.927  0.24 11.54 ?  127 LEU   A O    1 
ATOM   2565 C CB   A LEU   A 1 127 ? 21.111 -6.673  -1.295  0.76 12.76 ?  127 LEU   A CB   1 
ATOM   2566 C CB   B LEU   A 1 127 ? 21.122 -6.269  -1.133  0.24 10.86 ?  127 LEU   A CB   1 
ATOM   2567 C CG   A LEU   A 1 127 ? 21.902 -6.917  -0.013  0.76 13.13 ?  127 LEU   A CG   1 
ATOM   2568 C CG   B LEU   A 1 127 ? 21.901 -6.314  0.183   0.24 10.98 ?  127 LEU   A CG   1 
ATOM   2569 C CD1  A LEU   A 1 127 ? 23.004 -7.910  -0.281  0.76 13.39 ?  127 LEU   A CD1  1 
ATOM   2570 C CD1  B LEU   A 1 127 ? 23.082 -7.270  0.077   0.24 11.34 ?  127 LEU   A CD1  1 
ATOM   2571 C CD2  A LEU   A 1 127 ? 22.509 -5.630  0.501   0.76 14.34 ?  127 LEU   A CD2  1 
ATOM   2572 C CD2  B LEU   A 1 127 ? 22.370 -4.920  0.577   0.24 11.15 ?  127 LEU   A CD2  1 
ATOM   2573 H H    A LEU   A 1 127 ? 19.131 -6.987  0.060   0.76 14.43 ?  127 LEU   A H    1 
ATOM   2574 H H    B LEU   A 1 127 ? 19.027 -6.765  0.051   0.24 13.36 ?  127 LEU   A H    1 
ATOM   2575 H HA   A LEU   A 1 127 ? 20.280 -4.846  -0.881  0.76 14.11 ?  127 LEU   A HA   1 
ATOM   2576 H HA   B LEU   A 1 127 ? 20.095 -4.515  -0.848  0.24 12.91 ?  127 LEU   A HA   1 
ATOM   2577 H HB2  A LEU   A 1 127 ? 20.768 -7.532  -1.592  0.76 15.31 ?  127 LEU   A HB2  1 
ATOM   2578 H HB2  B LEU   A 1 127 ? 20.875 -7.179  -1.359  0.24 13.03 ?  127 LEU   A HB2  1 
ATOM   2579 H HB3  A LEU   A 1 127 ? 21.735 -6.333  -1.956  0.76 15.31 ?  127 LEU   A HB3  1 
ATOM   2580 H HB3  B LEU   A 1 127 ? 21.720 -5.919  -1.814  0.24 13.03 ?  127 LEU   A HB3  1 
ATOM   2581 H HG   A LEU   A 1 127 ? 21.315 -7.285  0.672   0.76 15.75 ?  127 LEU   A HG   1 
ATOM   2582 H HG   B LEU   A 1 127 ? 21.315 -6.643  0.881   0.24 13.18 ?  127 LEU   A HG   1 
ATOM   2583 H HD11 A LEU   A 1 127 ? 23.482 -8.086  0.545   0.76 16.07 ?  127 LEU   A HD11 1 
ATOM   2584 H HD11 B LEU   A 1 127 ? 23.587 -7.238  0.904   0.24 13.61 ?  127 LEU   A HD11 1 
ATOM   2585 H HD12 A LEU   A 1 127 ? 22.616 -8.734  -0.618  0.76 16.07 ?  127 LEU   A HD12 1 
ATOM   2586 H HD12 B LEU   A 1 127 ? 22.749 -8.169  -0.074  0.24 13.61 ?  127 LEU   A HD12 1 
ATOM   2587 H HD13 A LEU   A 1 127 ? 23.609 -7.537  -0.940  0.76 16.07 ?  127 LEU   A HD13 1 
ATOM   2588 H HD13 B LEU   A 1 127 ? 23.644 -6.996  -0.664  0.24 13.61 ?  127 LEU   A HD13 1 
ATOM   2589 H HD21 A LEU   A 1 127 ? 23.111 -5.832  1.231   0.76 17.20 ?  127 LEU   A HD21 1 
ATOM   2590 H HD21 B LEU   A 1 127 ? 22.986 -4.996  1.322   0.24 13.38 ?  127 LEU   A HD21 1 
ATOM   2591 H HD22 A LEU   A 1 127 ? 22.998 -5.206  -0.224  0.76 17.20 ?  127 LEU   A HD22 1 
ATOM   2592 H HD22 B LEU   A 1 127 ? 22.814 -4.512  -0.181  0.24 13.38 ?  127 LEU   A HD22 1 
ATOM   2593 H HD23 A LEU   A 1 127 ? 21.799 -5.045  0.805   0.76 17.20 ?  127 LEU   A HD23 1 
ATOM   2594 H HD23 B LEU   A 1 127 ? 21.600 -4.391  0.836   0.24 13.38 ?  127 LEU   A HD23 1 
ATOM   2595 N N    A SER   A 1 128 ? 19.735 -4.423  -3.220  0.76 11.50 ?  128 SER   A N    1 
ATOM   2596 N N    B SER   A 1 128 ? 19.801 -4.391  -3.309  0.24 11.72 ?  128 SER   A N    1 
ATOM   2597 C CA   A SER   A 1 128 ? 19.330 -4.031  -4.561  0.76 11.45 ?  128 SER   A CA   1 
ATOM   2598 C CA   B SER   A 1 128 ? 19.434 -4.102  -4.691  0.24 11.59 ?  128 SER   A CA   1 
ATOM   2599 C C    A SER   A 1 128 ? 17.868 -3.602  -4.655  0.76 11.95 ?  128 SER   A C    1 
ATOM   2600 C C    B SER   A 1 128 ? 18.009 -3.582  -4.861  0.24 11.34 ?  128 SER   A C    1 
ATOM   2601 O O    A SER   A 1 128 ? 17.408 -3.296  -5.756  0.76 13.78 ?  128 SER   A O    1 
ATOM   2602 O O    B SER   A 1 128 ? 17.639 -3.213  -5.981  0.24 11.30 ?  128 SER   A O    1 
ATOM   2603 C CB   A SER   A 1 128 ? 19.675 -5.072  -5.635  0.76 11.77 ?  128 SER   A CB   1 
ATOM   2604 C CB   B SER   A 1 128 ? 19.702 -5.268  -5.657  0.24 11.82 ?  128 SER   A CB   1 
ATOM   2605 O OG   A SER   A 1 128 ? 21.087 -5.268  -5.699  0.76 12.37 ?  128 SER   A OG   1 
ATOM   2606 O OG   B SER   A 1 128 ? 21.096 -5.515  -5.775  0.24 12.09 ?  128 SER   A OG   1 
ATOM   2607 H H    A SER   A 1 128 ? 20.316 -3.877  -2.887  0.76 13.79 ?  128 SER   A H    1 
ATOM   2608 H H    B SER   A 1 128 ? 20.421 -3.864  -3.028  0.24 14.06 ?  128 SER   A H    1 
ATOM   2609 H HA   A SER   A 1 128 ? 19.847 -3.247  -4.783  0.76 13.74 ?  128 SER   A HA   1 
ATOM   2610 H HA   B SER   A 1 128 ? 20.007 -3.381  -4.980  0.24 13.90 ?  128 SER   A HA   1 
ATOM   2611 H HB2  A SER   A 1 128 ? 19.238 -5.910  -5.422  0.76 14.12 ?  128 SER   A HB2  1 
ATOM   2612 H HB2  B SER   A 1 128 ? 19.263 -6.063  -5.325  0.24 14.19 ?  128 SER   A HB2  1 
ATOM   2613 H HB3  A SER   A 1 128 ? 19.358 -4.745  -6.499  0.76 14.12 ?  128 SER   A HB3  1 
ATOM   2614 H HB3  B SER   A 1 128 ? 19.350 -5.033  -6.533  0.24 14.19 ?  128 SER   A HB3  1 
ATOM   2615 H HG   A SER   A 1 128 ? 21.465 -4.541  -5.879  0.76 14.85 ?  128 SER   A HG   1 
ATOM   2616 H HG   B SER   A 1 128 ? 21.484 -4.822  -6.054  0.24 14.50 ?  128 SER   A HG   1 
ATOM   2617 N N    A ALA   A 1 129 ? 17.141 -3.537  -3.540  0.76 12.91 ?  129 ALA   A N    1 
ATOM   2618 N N    B ALA   A 1 129 ? 17.209 -3.515  -3.799  0.24 12.05 ?  129 ALA   A N    1 
ATOM   2619 C CA   A ALA   A 1 129 ? 15.769 -3.052  -3.538  0.76 13.44 ?  129 ALA   A CA   1 
ATOM   2620 C CA   B ALA   A 1 129 ? 15.872 -2.942  -3.884  0.24 12.82 ?  129 ALA   A CA   1 
ATOM   2621 C C    A ALA   A 1 129 ? 15.754 -1.523  -3.501  0.76 12.80 ?  129 ALA   A C    1 
ATOM   2622 C C    B ALA   A 1 129 ? 15.952 -1.419  -3.801  0.24 13.10 ?  129 ALA   A C    1 
ATOM   2623 O O    A ALA   A 1 129 ? 16.793 -0.860  -3.568  0.76 12.81 ?  129 ALA   A O    1 
ATOM   2624 O O    B ALA   A 1 129 ? 17.031 -0.819  -3.800  0.24 13.23 ?  129 ALA   A O    1 
ATOM   2625 C CB   A ALA   A 1 129 ? 14.993 -3.663  -2.369  0.76 14.88 ?  129 ALA   A CB   1 
ATOM   2626 C CB   B ALA   A 1 129 ? 14.971 -3.517  -2.794  0.24 13.53 ?  129 ALA   A CB   1 
ATOM   2627 H H    A ALA   A 1 129 ? 17.428 -3.769  -2.759  0.76 15.49 ?  129 ALA   A H    1 
ATOM   2628 H H    B ALA   A 1 129 ? 17.410 -3.803  -3.013  0.24 14.46 ?  129 ALA   A H    1 
ATOM   2629 H HA   A ALA   A 1 129 ? 15.340 -3.328  -4.357  0.76 16.13 ?  129 ALA   A HA   1 
ATOM   2630 H HA   B ALA   A 1 129 ? 15.486 -3.158  -4.744  0.24 15.38 ?  129 ALA   A HA   1 
ATOM   2631 H HB1  A ALA   A 1 129 ? 14.079 -3.330  -2.393  0.76 17.86 ?  129 ALA   A HB1  1 
ATOM   2632 H HB1  B ALA   A 1 129 ? 14.088 -3.116  -2.869  0.24 16.23 ?  129 ALA   A HB1  1 
ATOM   2633 H HB2  A ALA   A 1 129 ? 14.999 -4.624  -2.457  0.76 17.86 ?  129 ALA   A HB2  1 
ATOM   2634 H HB2  B ALA   A 1 129 ? 14.911 -4.474  -2.907  0.24 16.23 ?  129 ALA   A HB2  1 
ATOM   2635 H HB3  A ALA   A 1 129 ? 15.416 -3.399  -1.536  0.76 17.86 ?  129 ALA   A HB3  1 
ATOM   2636 H HB3  B ALA   A 1 129 ? 15.354 -3.306  -1.927  0.24 16.23 ?  129 ALA   A HB3  1 
ATOM   2637 N N    A GLY   A 1 130 ? 14.555 -0.954  -3.414  0.76 12.98 ?  130 GLY   A N    1 
ATOM   2638 N N    B GLY   A 1 130 ? 14.791 -0.780  -3.742  0.24 13.14 ?  130 GLY   A N    1 
ATOM   2639 C CA   A GLY   A 1 130 ? 14.434 0.494   -3.356  0.76 13.78 ?  130 GLY   A CA   1 
ATOM   2640 C CA   B GLY   A 1 130 ? 14.757 0.666   -3.622  0.24 13.75 ?  130 GLY   A CA   1 
ATOM   2641 C C    A GLY   A 1 130 ? 15.042 1.138   -4.583  0.76 12.96 ?  130 GLY   A C    1 
ATOM   2642 C C    B GLY   A 1 130 ? 15.377 1.305   -4.845  0.24 13.97 ?  130 GLY   A C    1 
ATOM   2643 O O    A GLY   A 1 130 ? 14.814 0.696   -5.714  0.76 12.87 ?  130 GLY   A O    1 
ATOM   2644 O O    B GLY   A 1 130 ? 15.113 0.906   -5.984  0.24 14.60 ?  130 GLY   A O    1 
ATOM   2645 H H    A GLY   A 1 130 ? 13.807 -1.378  -3.390  0.76 15.57 ?  130 GLY   A H    1 
ATOM   2646 H H    B GLY   A 1 130 ? 14.025 -1.158  -3.787  0.24 15.77 ?  130 GLY   A H    1 
ATOM   2647 H HA2  A GLY   A 1 130 ? 13.493 0.744   -3.311  0.76 16.54 ?  130 GLY   A HA2  1 
ATOM   2648 H HA2  B GLY   A 1 130 ? 13.835 0.966   -3.536  0.24 16.50 ?  130 GLY   A HA2  1 
ATOM   2649 H HA3  A GLY   A 1 130 ? 14.885 0.834   -2.576  0.76 16.54 ?  130 GLY   A HA3  1 
ATOM   2650 H HA3  B GLY   A 1 130 ? 15.251 0.951   -2.839  0.24 16.50 ?  130 GLY   A HA3  1 
ATOM   2651 N N    A ILE   A 1 131 ? 15.826 2.203   -4.364  0.76 13.18 ?  131 ILE   A N    1 
ATOM   2652 N N    B ILE   A 1 131 ? 16.242 2.294   -4.609  0.24 13.84 ?  131 ILE   A N    1 
ATOM   2653 C CA   A ILE   A 1 131 ? 16.388 2.979   -5.469  0.76 12.56 ?  131 ILE   A CA   1 
ATOM   2654 C CA   B ILE   A 1 131 ? 16.832 3.049   -5.709  0.24 13.79 ?  131 ILE   A CA   1 
ATOM   2655 C C    A ILE   A 1 131 ? 17.427 2.222   -6.285  0.76 12.45 ?  131 ILE   A C    1 
ATOM   2656 C C    B ILE   A 1 131 ? 17.779 2.220   -6.558  0.24 13.85 ?  131 ILE   A C    1 
ATOM   2657 O O    A ILE   A 1 131 ? 17.852 2.729   -7.329  0.76 13.34 ?  131 ILE   A O    1 
ATOM   2658 O O    B ILE   A 1 131 ? 18.158 2.663   -7.649  0.24 14.48 ?  131 ILE   A O    1 
ATOM   2659 C CB   A ILE   A 1 131 ? 16.927 4.354   -5.014  0.76 14.24 ?  131 ILE   A CB   1 
ATOM   2660 C CB   B ILE   A 1 131 ? 17.502 4.353   -5.224  0.24 13.96 ?  131 ILE   A CB   1 
ATOM   2661 C CG1  A ILE   A 1 131 ? 18.152 4.201   -4.109  0.76 15.83 ?  131 ILE   A CG1  1 
ATOM   2662 C CG1  B ILE   A 1 131 ? 18.694 4.057   -4.310  0.24 14.50 ?  131 ILE   A CG1  1 
ATOM   2663 C CG2  A ILE   A 1 131 ? 15.831 5.149   -4.313  0.76 15.16 ?  131 ILE   A CG2  1 
ATOM   2664 C CG2  B ILE   A 1 131 ? 16.487 5.233   -4.509  0.24 13.98 ?  131 ILE   A CG2  1 
ATOM   2665 C CD1  A ILE   A 1 131 ? 18.781 5.534   -3.709  0.76 17.78 ?  131 ILE   A CD1  1 
ATOM   2666 C CD1  B ILE   A 1 131 ? 19.389 5.309   -3.785  0.24 14.96 ?  131 ILE   A CD1  1 
ATOM   2667 H H    A ILE   A 1 131 ? 16.028 2.502   -3.583  0.76 15.82 ?  131 ILE   A H    1 
ATOM   2668 H H    B ILE   A 1 131 ? 16.504 2.532   -3.827  0.24 16.61 ?  131 ILE   A H    1 
ATOM   2669 H HA   A ILE   A 1 131 ? 15.666 3.168   -6.080  0.76 15.07 ?  131 ILE   A HA   1 
ATOM   2670 H HA   B ILE   A 1 131 ? 16.116 3.312   -6.295  0.24 16.55 ?  131 ILE   A HA   1 
ATOM   2671 H HB   A ILE   A 1 131 ? 17.195 4.847   -5.802  0.76 17.09 ?  131 ILE   A HB   1 
ATOM   2672 H HB   B ILE   A 1 131 ? 17.826 4.835   -6.000  0.24 16.75 ?  131 ILE   A HB   1 
ATOM   2673 H HG12 A ILE   A 1 131 ? 17.891 3.742   -3.296  0.76 19.00 ?  131 ILE   A HG12 1 
ATOM   2674 H HG12 B ILE   A 1 131 ? 18.386 3.549   -3.546  0.24 17.40 ?  131 ILE   A HG12 1 
ATOM   2675 H HG13 A ILE   A 1 131 ? 18.830 3.687   -4.574  0.76 19.00 ?  131 ILE   A HG13 1 
ATOM   2676 H HG13 B ILE   A 1 131 ? 19.352 3.547   -4.805  0.24 17.40 ?  131 ILE   A HG13 1 
ATOM   2677 H HG21 A ILE   A 1 131 ? 16.130 6.062   -4.187  0.76 18.19 ?  131 ILE   A HG21 1 
ATOM   2678 H HG21 B ILE   A 1 131 ? 16.861 6.121   -4.391  0.24 16.77 ?  131 ILE   A HG21 1 
ATOM   2679 H HG22 A ILE   A 1 131 ? 15.033 5.136   -4.866  0.76 18.19 ?  131 ILE   A HG22 1 
ATOM   2680 H HG22 B ILE   A 1 131 ? 15.682 5.285   -5.048  0.24 16.77 ?  131 ILE   A HG22 1 
ATOM   2681 H HG23 A ILE   A 1 131 ? 15.642 4.739   -3.454  0.76 18.19 ?  131 ILE   A HG23 1 
ATOM   2682 H HG23 B ILE   A 1 131 ? 16.281 4.842   -3.646  0.24 16.77 ?  131 ILE   A HG23 1 
ATOM   2683 H HD11 A ILE   A 1 131 ? 19.619 5.364   -3.246  0.76 21.33 ?  131 ILE   A HD11 1 
ATOM   2684 H HD11 B ILE   A 1 131 ? 20.215 5.054   -3.347  0.24 17.96 ?  131 ILE   A HD11 1 
ATOM   2685 H HD12 A ILE   A 1 131 ? 18.950 6.058   -4.508  0.76 21.33 ?  131 ILE   A HD12 1 
ATOM   2686 H HD12 B ILE   A 1 131 ? 19.580 5.903   -4.529  0.24 17.96 ?  131 ILE   A HD12 1 
ATOM   2687 H HD13 A ILE   A 1 131 ? 18.174 6.012   -3.123  0.76 21.33 ?  131 ILE   A HD13 1 
ATOM   2688 H HD13 B ILE   A 1 131 ? 18.804 5.757   -3.150  0.24 17.96 ?  131 ILE   A HD13 1 
ATOM   2689 N N    A PHE   A 1 132 ? 17.846 1.023   -5.852  0.76 12.60 ?  132 PHE   A N    1 
ATOM   2690 N N    B PHE   A 1 132 ? 18.164 1.024   -6.101  0.24 13.64 ?  132 PHE   A N    1 
ATOM   2691 C CA   A PHE   A 1 132 ? 18.711 0.180   -6.674  0.76 12.64 ?  132 PHE   A CA   1 
ATOM   2692 C CA   B PHE   A 1 132 ? 19.032 0.173   -6.905  0.24 13.64 ?  132 PHE   A CA   1 
ATOM   2693 C C    A PHE   A 1 132 ? 17.945 -0.587  -7.755  0.76 13.43 ?  132 PHE   A C    1 
ATOM   2694 C C    B PHE   A 1 132 ? 18.280 -0.536  -8.029  0.24 14.15 ?  132 PHE   A C    1 
ATOM   2695 O O    A PHE   A 1 132 ? 18.574 -1.230  -8.604  0.76 13.99 ?  132 PHE   A O    1 
ATOM   2696 O O    B PHE   A 1 132 ? 18.918 -1.053  -8.953  0.24 14.70 ?  132 PHE   A O    1 
ATOM   2697 C CB   A PHE   A 1 132 ? 19.516 -0.797  -5.804  0.76 12.24 ?  132 PHE   A CB   1 
ATOM   2698 C CB   B PHE   A 1 132 ? 19.787 -0.823  -6.018  0.24 12.70 ?  132 PHE   A CB   1 
ATOM   2699 C CG   A PHE   A 1 132 ? 20.755 -0.201  -5.159  0.76 12.38 ?  132 PHE   A CG   1 
ATOM   2700 C CG   B PHE   A 1 132 ? 20.930 -0.207  -5.245  0.24 12.52 ?  132 PHE   A CG   1 
ATOM   2701 C CD1  A PHE   A 1 132 ? 20.664 0.859   -4.274  0.76 13.80 ?  132 PHE   A CD1  1 
ATOM   2702 C CD1  B PHE   A 1 132 ? 20.692 0.691   -4.216  0.24 12.99 ?  132 PHE   A CD1  1 
ATOM   2703 C CD2  A PHE   A 1 132 ? 22.007 -0.756  -5.402  0.76 13.03 ?  132 PHE   A CD2  1 
ATOM   2704 C CD2  B PHE   A 1 132 ? 22.243 -0.540  -5.543  0.24 12.42 ?  132 PHE   A CD2  1 
ATOM   2705 C CE1  A PHE   A 1 132 ? 21.805 1.380   -3.671  0.76 14.29 ?  132 PHE   A CE1  1 
ATOM   2706 C CE1  B PHE   A 1 132 ? 21.744 1.251   -3.505  0.24 12.92 ?  132 PHE   A CE1  1 
ATOM   2707 C CE2  A PHE   A 1 132 ? 23.145 -0.246  -4.799  0.76 13.86 ?  132 PHE   A CE2  1 
ATOM   2708 C CE2  B PHE   A 1 132 ? 23.297 0.015   -4.835  0.24 12.72 ?  132 PHE   A CE2  1 
ATOM   2709 C CZ   A PHE   A 1 132 ? 23.042 0.824   -3.931  0.76 14.23 ?  132 PHE   A CZ   1 
ATOM   2710 C CZ   B PHE   A 1 132 ? 23.045 0.911   -3.815  0.24 12.84 ?  132 PHE   A CZ   1 
ATOM   2711 H H    A PHE   A 1 132 ? 17.644 0.679   -5.084  0.76 15.12 ?  132 PHE   A H    1 
ATOM   2712 H H    B PHE   A 1 132 ? 17.938 0.688   -5.337  0.24 16.37 ?  132 PHE   A H    1 
ATOM   2713 H HA   A PHE   A 1 132 ? 19.352 0.753   -7.118  0.76 15.16 ?  132 PHE   A HA   1 
ATOM   2714 H HA   B PHE   A 1 132 ? 19.700 0.740   -7.314  0.24 16.36 ?  132 PHE   A HA   1 
ATOM   2715 H HB2  A PHE   A 1 132 ? 18.943 -1.121  -5.088  0.76 14.69 ?  132 PHE   A HB2  1 
ATOM   2716 H HB2  B PHE   A 1 132 ? 19.171 -1.203  -5.374  0.24 15.24 ?  132 PHE   A HB2  1 
ATOM   2717 H HB3  A PHE   A 1 132 ? 19.799 -1.545  -6.354  0.76 14.69 ?  132 PHE   A HB3  1 
ATOM   2718 H HB3  B PHE   A 1 132 ? 20.155 -1.526  -6.578  0.24 15.24 ?  132 PHE   A HB3  1 
ATOM   2719 H HD1  A PHE   A 1 132 ? 19.834 1.234   -4.092  0.76 16.56 ?  132 PHE   A HD1  1 
ATOM   2720 H HD1  B PHE   A 1 132 ? 19.819 0.926   -4.001  0.24 15.59 ?  132 PHE   A HD1  1 
ATOM   2721 H HD2  A PHE   A 1 132 ? 22.085 -1.483  -5.986  0.76 15.63 ?  132 PHE   A HD2  1 
ATOM   2722 H HD2  B PHE   A 1 132 ? 22.419 -1.145  -6.228  0.24 14.91 ?  132 PHE   A HD2  1 
ATOM   2723 H HE1  A PHE   A 1 132 ? 21.735 2.100   -3.086  0.76 17.14 ?  132 PHE   A HE1  1 
ATOM   2724 H HE1  B PHE   A 1 132 ? 21.574 1.857   -2.819  0.24 15.51 ?  132 PHE   A HE1  1 
ATOM   2725 H HE2  A PHE   A 1 132 ? 23.979 -0.622  -4.984  0.76 16.63 ?  132 PHE   A HE2  1 
ATOM   2726 H HE2  B PHE   A 1 132 ? 24.173 -0.216  -5.048  0.24 15.27 ?  132 PHE   A HE2  1 
ATOM   2727 H HZ   A PHE   A 1 132 ? 23.806 1.176   -3.532  0.76 17.08 ?  132 PHE   A HZ   1 
ATOM   2728 H HZ   B PHE   A 1 132 ? 23.752 1.287   -3.341  0.24 15.41 ?  132 PHE   A HZ   1 
ATOM   2729 N N    A GLY   A 1 133 ? 16.612 -0.555  -7.738  0.76 13.35 ?  133 GLY   A N    1 
ATOM   2730 N N    B GLY   A 1 133 ? 16.947 -0.583  -7.968  0.24 14.22 ?  133 GLY   A N    1 
ATOM   2731 C CA   A GLY   A 1 133 ? 15.822 -0.916  -8.901  0.76 14.75 ?  133 GLY   A CA   1 
ATOM   2732 C CA   B GLY   A 1 133 ? 16.113 -0.895  -9.109  0.24 14.51 ?  133 GLY   A CA   1 
ATOM   2733 C C    A GLY   A 1 133 ? 15.518 -2.386  -9.117  0.76 15.03 ?  133 GLY   A C    1 
ATOM   2734 C C    B GLY   A 1 133 ? 15.512 -2.289  -9.131  0.24 14.54 ?  133 GLY   A C    1 
ATOM   2735 O O    A GLY   A 1 133 ? 14.918 -2.716  -10.147 0.76 16.36 ?  133 GLY   A O    1 
ATOM   2736 O O    B GLY   A 1 133 ? 14.555 -2.515  -9.883  0.24 14.72 ?  133 GLY   A O    1 
ATOM   2737 H H    A GLY   A 1 133 ? 16.139 -0.320  -7.056  0.76 16.02 ?  133 GLY   A H    1 
ATOM   2738 H H    B GLY   A 1 133 ? 16.500 -0.434  -7.251  0.24 17.07 ?  133 GLY   A H    1 
ATOM   2739 H HA2  A GLY   A 1 133 ? 14.971 -0.457  -8.848  0.76 17.69 ?  133 GLY   A HA2  1 
ATOM   2740 H HA2  B GLY   A 1 133 ? 15.377 -0.276  -9.114  0.24 17.42 ?  133 GLY   A HA2  1 
ATOM   2741 H HA3  A GLY   A 1 133 ? 16.280 -0.594  -9.693  0.76 17.69 ?  133 GLY   A HA3  1 
ATOM   2742 H HA3  B GLY   A 1 133 ? 16.610 -0.748  -9.928  0.24 17.42 ?  133 GLY   A HA3  1 
ATOM   2743 N N    A ALA   A 1 134 ? 15.909 -3.282  -8.213  0.76 14.64 ?  134 ALA   A N    1 
ATOM   2744 N N    B ALA   A 1 134 ? 16.032 -3.223  -8.340  0.24 14.43 ?  134 ALA   A N    1 
ATOM   2745 C CA   A ALA   A 1 134 ? 15.583 -4.690  -8.392  0.76 15.70 ?  134 ALA   A CA   1 
ATOM   2746 C CA   B ALA   A 1 134 ? 15.571 -4.601  -8.429  0.24 14.46 ?  134 ALA   A CA   1 
ATOM   2747 C C    A ALA   A 1 134 ? 14.219 -5.007  -7.780  0.76 15.96 ?  134 ALA   A C    1 
ATOM   2748 C C    B ALA   A 1 134 ? 14.281 -4.812  -7.636  0.24 14.09 ?  134 ALA   A C    1 
ATOM   2749 O O    A ALA   A 1 134 ? 13.644 -4.221  -7.024  0.76 16.42 ?  134 ALA   A O    1 
ATOM   2750 O O    B ALA   A 1 134 ? 13.916 -4.024  -6.760  0.24 13.90 ?  134 ALA   A O    1 
ATOM   2751 C CB   A ALA   A 1 134 ? 16.660 -5.587  -7.784  0.76 16.29 ?  134 ALA   A CB   1 
ATOM   2752 C CB   B ALA   A 1 134 ? 16.648 -5.562  -7.930  0.24 14.74 ?  134 ALA   A CB   1 
ATOM   2753 H H    A ALA   A 1 134 ? 16.369 -3.099  -7.504  0.76 17.57 ?  134 ALA   A H    1 
ATOM   2754 H H    B ALA   A 1 134 ? 16.649 -3.086  -7.755  0.24 17.32 ?  134 ALA   A H    1 
ATOM   2755 H HA   A ALA   A 1 134 ? 15.539 -4.880  -9.343  0.76 18.84 ?  134 ALA   A HA   1 
ATOM   2756 H HA   B ALA   A 1 134 ? 15.390 -4.807  -9.359  0.24 17.35 ?  134 ALA   A HA   1 
ATOM   2757 H HB1  A ALA   A 1 134 ? 16.418 -6.512  -7.941  0.76 19.55 ?  134 ALA   A HB1  1 
ATOM   2758 H HB1  B ALA   A 1 134 ? 16.319 -6.469  -8.010  0.24 17.69 ?  134 ALA   A HB1  1 
ATOM   2759 H HB2  A ALA   A 1 134 ? 17.511 -5.390  -8.210  0.76 19.55 ?  134 ALA   A HB2  1 
ATOM   2760 H HB2  B ALA   A 1 134 ? 17.444 -5.448  -8.472  0.24 17.69 ?  134 ALA   A HB2  1 
ATOM   2761 H HB3  A ALA   A 1 134 ? 16.716 -5.412  -6.834  0.76 19.55 ?  134 ALA   A HB3  1 
ATOM   2762 H HB3  B ALA   A 1 134 ? 16.845 -5.359  -7.003  0.24 17.69 ?  134 ALA   A HB3  1 
ATOM   2763 N N    A ASP   A 1 135 ? 13.704 -6.181  -8.125  0.76 15.98 ?  135 ASP   A N    1 
ATOM   2764 N N    B ASP   A 1 135 ? 13.598 -5.908  -7.957  0.24 14.23 ?  135 ASP   A N    1 
ATOM   2765 C CA   A ASP   A 1 135 ? 12.445 -6.667  -7.572  0.76 16.55 ?  135 ASP   A CA   1 
ATOM   2766 C CA   B ASP   A 1 135 ? 12.346 -6.270  -7.300  0.24 14.38 ?  135 ASP   A CA   1 
ATOM   2767 C C    A ASP   A 1 135 ? 12.676 -7.115  -6.135  0.76 15.69 ?  135 ASP   A C    1 
ATOM   2768 C C    B ASP   A 1 135 ? 12.638 -6.761  -5.887  0.24 13.70 ?  135 ASP   A C    1 
ATOM   2769 O O    A ASP   A 1 135 ? 13.464 -8.041  -5.909  0.76 15.48 ?  135 ASP   A O    1 
ATOM   2770 O O    B ASP   A 1 135 ? 13.384 -7.736  -5.723  0.24 13.23 ?  135 ASP   A O    1 
ATOM   2771 C CB   A ASP   A 1 135 ? 11.973 -7.845  -8.419  0.76 19.21 ?  135 ASP   A CB   1 
ATOM   2772 C CB   B ASP   A 1 135 ? 11.675 -7.382  -8.103  0.24 15.29 ?  135 ASP   A CB   1 
ATOM   2773 C CG   A ASP   A 1 135 ? 10.683 -8.475  -7.906  0.76 21.60 ?  135 ASP   A CG   1 
ATOM   2774 C CG   B ASP   A 1 135 ? 10.261 -7.686  -7.629  0.24 16.27 ?  135 ASP   A CG   1 
ATOM   2775 O OD1  A ASP   A 1 135 ? 10.137 -8.020  -6.881  0.76 21.50 ?  135 ASP   A OD1  1 
ATOM   2776 O OD1  B ASP   A 1 135 ? 9.923  -7.332  -6.478  0.24 16.40 ?  135 ASP   A OD1  1 
ATOM   2777 O OD2  A ASP   A 1 135 ? 10.209 -9.436  -8.547  0.76 24.43 -1 135 ASP   A OD2  1 
ATOM   2778 O OD2  B ASP   A 1 135 ? 9.493  -8.297  -8.404  0.24 16.90 -1 135 ASP   A OD2  1 
ATOM   2779 H H    A ASP   A 1 135 ? 14.067 -6.718  -8.686  0.76 19.17 ?  135 ASP   A H    1 
ATOM   2780 H H    B ASP   A 1 135 ? 13.840 -6.467  -8.559  0.24 17.08 ?  135 ASP   A H    1 
ATOM   2781 H HA   A ASP   A 1 135 ? 11.776 -5.963  -7.605  0.76 19.86 ?  135 ASP   A HA   1 
ATOM   2782 H HA   B ASP   A 1 135 ? 11.750 -5.503  -7.275  0.24 17.25 ?  135 ASP   A HA   1 
ATOM   2783 H HB2  A ASP   A 1 135 ? 11.810 -7.538  -9.321  0.76 23.05 ?  135 ASP   A HB2  1 
ATOM   2784 H HB2  B ASP   A 1 135 ? 11.650 -7.121  -9.037  0.24 18.34 ?  135 ASP   A HB2  1 
ATOM   2785 H HB3  A ASP   A 1 135 ? 12.664 -8.526  -8.416  0.76 23.05 ?  135 ASP   A HB3  1 
ATOM   2786 H HB3  B ASP   A 1 135 ? 12.187 -8.197  -8.000  0.24 18.34 ?  135 ASP   A HB3  1 
ATOM   2787 N N    A PRO   A 1 136 ? 12.039 -6.491  -5.142  0.76 15.55 ?  136 PRO   A N    1 
ATOM   2788 N N    B PRO   A 1 136 ? 12.091 -6.126  -4.847  0.24 13.35 ?  136 PRO   A N    1 
ATOM   2789 C CA   A PRO   A 1 136 ? 12.289 -6.898  -3.746  0.76 15.51 ?  136 PRO   A CA   1 
ATOM   2790 C CA   B PRO   A 1 136 ? 12.365 -6.594  -3.477  0.24 13.38 ?  136 PRO   A CA   1 
ATOM   2791 C C    A PRO   A 1 136 ? 11.884 -8.329  -3.436  0.76 14.40 ?  136 PRO   A C    1 
ATOM   2792 C C    B PRO   A 1 136 ? 11.874 -8.004  -3.199  0.24 13.02 ?  136 PRO   A C    1 
ATOM   2793 O O    A PRO   A 1 136 ? 12.490 -8.955  -2.558  0.76 14.22 ?  136 PRO   A O    1 
ATOM   2794 O O    B PRO   A 1 136 ? 12.431 -8.680  -2.325  0.24 12.25 ?  136 PRO   A O    1 
ATOM   2795 C CB   A PRO   A 1 136 ? 11.483 -5.875  -2.931  0.76 16.51 ?  136 PRO   A CB   1 
ATOM   2796 C CB   B PRO   A 1 136 ? 11.663 -5.545  -2.599  0.24 13.83 ?  136 PRO   A CB   1 
ATOM   2797 C CG   A PRO   A 1 136 ? 10.451 -5.356  -3.881  0.76 17.65 ?  136 PRO   A CG   1 
ATOM   2798 C CG   B PRO   A 1 136 ? 10.653 -4.906  -3.499  0.24 14.16 ?  136 PRO   A CG   1 
ATOM   2799 C CD   A PRO   A 1 136 ? 11.080 -5.376  -5.235  0.76 16.95 ?  136 PRO   A CD   1 
ATOM   2800 C CD   B PRO   A 1 136 ? 11.264 -4.910  -4.859  0.24 13.67 ?  136 PRO   A CD   1 
ATOM   2801 H HA   A PRO   A 1 136 ? 13.231 -6.785  -3.531  0.76 18.61 ?  136 PRO   A HA   1 
ATOM   2802 H HA   B PRO   A 1 136 ? 13.316 -6.556  -3.297  0.24 16.05 ?  136 PRO   A HA   1 
ATOM   2803 H HB2  A PRO   A 1 136 ? 11.064 -6.316  -2.175  0.76 19.81 ?  136 PRO   A HB2  1 
ATOM   2804 H HB2  B PRO   A 1 136 ? 11.228 -5.976  -1.848  0.24 16.59 ?  136 PRO   A HB2  1 
ATOM   2805 H HB3  A PRO   A 1 136 ? 12.067 -5.159  -2.629  0.76 19.81 ?  136 PRO   A HB3  1 
ATOM   2806 H HB3  B PRO   A 1 136 ? 12.308 -4.886  -2.290  0.24 16.59 ?  136 PRO   A HB3  1 
ATOM   2807 H HG2  A PRO   A 1 136 ? 9.673  -5.931  -3.860  0.76 21.18 ?  136 PRO   A HG2  1 
ATOM   2808 H HG2  B PRO   A 1 136 ? 9.836  -5.430  -3.495  0.24 16.99 ?  136 PRO   A HG2  1 
ATOM   2809 H HG3  A PRO   A 1 136 ? 10.211 -4.448  -3.634  0.76 21.18 ?  136 PRO   A HG3  1 
ATOM   2810 H HG3  B PRO   A 1 136 ? 10.478 -3.998  -3.207  0.24 16.99 ?  136 PRO   A HG3  1 
ATOM   2811 H HD2  A PRO   A 1 136 ? 10.410 -5.568  -5.913  0.76 20.34 ?  136 PRO   A HD2  1 
ATOM   2812 H HD2  B PRO   A 1 136 ? 10.571 -4.974  -5.537  0.24 16.40 ?  136 PRO   A HD2  1 
ATOM   2813 H HD3  A PRO   A 1 136 ? 11.536 -4.539  -5.415  0.76 20.34 ?  136 PRO   A HD3  1 
ATOM   2814 H HD3  B PRO   A 1 136 ? 11.817 -4.122  -4.989  0.24 16.40 ?  136 PRO   A HD3  1 
ATOM   2815 N N    A ILE   A 1 137 ? 10.860 -8.859  -4.105  0.76 14.51 ?  137 ILE   A N    1 
ATOM   2816 N N    B ILE   A 1 137 ? 10.837 -8.465  -3.902  0.24 13.49 ?  137 ILE   A N    1 
ATOM   2817 C CA   A ILE   A 1 137 ? 10.493 -10.258 -3.902  0.76 14.78 ?  137 ILE   A CA   1 
ATOM   2818 C CA   B ILE   A 1 137 ? 10.411 -9.855  -3.763  0.24 13.82 ?  137 ILE   A CA   1 
ATOM   2819 C C    A ILE   A 1 137 ? 11.648 -11.165 -4.298  0.76 14.40 ?  137 ILE   A C    1 
ATOM   2820 C C    B ILE   A 1 137 ? 11.535 -10.793 -4.179  0.24 13.43 ?  137 ILE   A C    1 
ATOM   2821 O O    A ILE   A 1 137 ? 11.967 -12.134 -3.601  0.76 14.73 ?  137 ILE   A O    1 
ATOM   2822 O O    B ILE   A 1 137 ? 11.807 -11.801 -3.514  0.24 13.30 ?  137 ILE   A O    1 
ATOM   2823 C CB   A ILE   A 1 137 ? 9.205  -10.590 -4.679  0.76 16.47 ?  137 ILE   A CB   1 
ATOM   2824 C CB   B ILE   A 1 137 ? 9.127  -10.102 -4.577  0.24 14.60 ?  137 ILE   A CB   1 
ATOM   2825 C CG1  A ILE   A 1 137 ? 8.032  -9.740  -4.174  0.76 18.81 ?  137 ILE   A CG1  1 
ATOM   2826 C CG1  B ILE   A 1 137 ? 7.991  -9.209  -4.065  0.24 15.53 ?  137 ILE   A CG1  1 
ATOM   2827 C CG2  A ILE   A 1 137 ? 8.874  -12.083 -4.559  0.76 17.11 ?  137 ILE   A CG2  1 
ATOM   2828 C CG2  B ILE   A 1 137 ? 8.734  -11.574 -4.525  0.24 14.86 ?  137 ILE   A CG2  1 
ATOM   2829 C CD1  A ILE   A 1 137 ? 6.746  -9.930  -4.952  0.76 20.54 ?  137 ILE   A CD1  1 
ATOM   2830 C CD1  B ILE   A 1 137 ? 6.752  -9.248  -4.927  0.24 16.03 ?  137 ILE   A CD1  1 
ATOM   2831 H H    A ILE   A 1 137 ? 10.372 -8.436  -4.672  0.76 17.41 ?  137 ILE   A H    1 
ATOM   2832 H H    B ILE   A 1 137 ? 10.371 -7.995  -4.454  0.24 16.19 ?  137 ILE   A H    1 
ATOM   2833 H HA   A ILE   A 1 137 ? 10.317 -10.404 -2.963  0.76 17.74 ?  137 ILE   A HA   1 
ATOM   2834 H HA   B ILE   A 1 137 ? 10.207 -10.025 -2.831  0.24 16.58 ?  137 ILE   A HA   1 
ATOM   2835 H HB   A ILE   A 1 137 ? 9.347  -10.384 -5.615  0.76 19.77 ?  137 ILE   A HB   1 
ATOM   2836 H HB   B ILE   A 1 137 ? 9.301  -9.865  -5.499  0.24 17.52 ?  137 ILE   A HB   1 
ATOM   2837 H HG12 A ILE   A 1 137 ? 7.858  -9.965  -3.248  0.76 22.57 ?  137 ILE   A HG12 1 
ATOM   2838 H HG12 B ILE   A 1 137 ? 7.742  -9.496  -3.174  0.24 18.63 ?  137 ILE   A HG12 1 
ATOM   2839 H HG13 A ILE   A 1 137 ? 8.280  -8.800  -4.239  0.76 22.57 ?  137 ILE   A HG13 1 
ATOM   2840 H HG13 B ILE   A 1 137 ? 8.299  -8.288  -4.040  0.24 18.63 ?  137 ILE   A HG13 1 
ATOM   2841 H HG21 A ILE   A 1 137 ? 7.997  -12.257 -4.937  0.76 20.53 ?  137 ILE   A HG21 1 
ATOM   2842 H HG21 B ILE   A 1 137 ? 7.839  -11.681 -4.882  0.24 17.83 ?  137 ILE   A HG21 1 
ATOM   2843 H HG22 A ILE   A 1 137 ? 9.540  -12.593 -5.042  0.76 20.53 ?  137 ILE   A HG22 1 
ATOM   2844 H HG22 B ILE   A 1 137 ? 9.362  -12.084 -5.059  0.24 17.83 ?  137 ILE   A HG22 1 
ATOM   2845 H HG23 A ILE   A 1 137 ? 8.880  -12.330 -3.622  0.76 20.53 ?  137 ILE   A HG23 1 
ATOM   2846 H HG23 B ILE   A 1 137 ? 8.759  -11.872 -3.604  0.24 17.83 ?  137 ILE   A HG23 1 
ATOM   2847 H HD11 A ILE   A 1 137 ? 6.052  -10.231 -4.347  0.76 24.65 ?  137 ILE   A HD11 1 
ATOM   2848 H HD11 B ILE   A 1 137 ? 6.006  -9.565  -4.394  0.24 19.23 ?  137 ILE   A HD11 1 
ATOM   2849 H HD12 A ILE   A 1 137 ? 6.503  -9.081  -5.348  0.76 24.65 ?  137 ILE   A HD12 1 
ATOM   2850 H HD12 B ILE   A 1 137 ? 6.571  -8.354  -5.254  0.24 19.23 ?  137 ILE   A HD12 1 
ATOM   2851 H HD13 A ILE   A 1 137 ? 6.887  -10.584 -5.653  0.76 24.65 ?  137 ILE   A HD13 1 
ATOM   2852 H HD13 B ILE   A 1 137 ? 6.903  -9.847  -5.675  0.24 19.23 ?  137 ILE   A HD13 1 
ATOM   2853 N N    A HIS   A 1 138 ? 12.287 -10.862 -5.425  0.76 14.56 ?  138 HIS   A N    1 
ATOM   2854 N N    B HIS   A 1 138 ? 12.203 -10.475 -5.290  0.24 13.27 ?  138 HIS   A N    1 
ATOM   2855 C CA   A HIS   A 1 138 ? 13.462 -11.622 -5.835  0.76 14.47 ?  138 HIS   A CA   1 
ATOM   2856 C CA   B HIS   A 1 138 ? 13.340 -11.277 -5.729  0.24 12.89 ?  138 HIS   A CA   1 
ATOM   2857 C C    A HIS   A 1 138 ? 14.597 -11.475 -4.827  0.76 14.23 ?  138 HIS   A C    1 
ATOM   2858 C C    B HIS   A 1 138 ? 14.505 -11.169 -4.750  0.24 12.48 ?  138 HIS   A C    1 
ATOM   2859 O O    A HIS   A 1 138 ? 15.245 -12.464 -4.461  0.76 14.67 ?  138 HIS   A O    1 
ATOM   2860 O O    B HIS   A 1 138 ? 15.196 -12.160 -4.485  0.24 12.25 ?  138 HIS   A O    1 
ATOM   2861 C CB   A HIS   A 1 138 ? 13.894 -11.178 -7.230  0.76 15.13 ?  138 HIS   A CB   1 
ATOM   2862 C CB   B HIS   A 1 138 ? 13.757 -10.847 -7.137  0.24 12.95 ?  138 HIS   A CB   1 
ATOM   2863 C CG   A HIS   A 1 138 ? 15.165 -11.815 -7.689  0.76 16.40 ?  138 HIS   A CG   1 
ATOM   2864 C CG   B HIS   A 1 138 ? 15.014 -11.499 -7.621  0.24 13.35 ?  138 HIS   A CG   1 
ATOM   2865 N ND1  A HIS   A 1 138 ? 15.277 -13.170 -7.923  0.76 17.96 ?  138 HIS   A ND1  1 
ATOM   2866 N ND1  B HIS   A 1 138 ? 15.079 -12.833 -7.963  0.24 14.32 ?  138 HIS   A ND1  1 
ATOM   2867 C CD2  A HIS   A 1 138 ? 16.386 -11.287 -7.935  0.76 17.22 ?  138 HIS   A CD2  1 
ATOM   2868 C CD2  B HIS   A 1 138 ? 16.257 -10.999 -7.819  0.24 13.63 ?  138 HIS   A CD2  1 
ATOM   2869 C CE1  A HIS   A 1 138 ? 16.511 -13.446 -8.304  0.76 18.88 ?  138 HIS   A CE1  1 
ATOM   2870 C CE1  B HIS   A 1 138 ? 16.308 -13.126 -8.351  0.24 14.62 ?  138 HIS   A CE1  1 
ATOM   2871 N NE2  A HIS   A 1 138 ? 17.205 -12.322 -8.319  0.76 18.14 ?  138 HIS   A NE2  1 
ATOM   2872 N NE2  B HIS   A 1 138 ? 17.042 -12.030 -8.273  0.24 14.20 ?  138 HIS   A NE2  1 
ATOM   2873 H H    A HIS   A 1 138 ? 12.066 -10.225 -5.964  0.76 17.47 ?  138 HIS   A H    1 
ATOM   2874 H H    B HIS   A 1 138 ? 12.013 -9.807  -5.802  0.24 15.92 ?  138 HIS   A H    1 
ATOM   2875 H HA   A HIS   A 1 138 ? 13.225 -12.558 -5.885  0.76 17.36 ?  138 HIS   A HA   1 
ATOM   2876 H HA   B HIS   A 1 138 ? 13.066 -12.205 -5.773  0.24 15.47 ?  138 HIS   A HA   1 
ATOM   2877 H HB2  A HIS   A 1 138 ? 13.194 -11.413 -7.865  0.76 18.16 ?  138 HIS   A HB2  1 
ATOM   2878 H HB2  B HIS   A 1 138 ? 13.045 -11.075 -7.759  0.24 15.55 ?  138 HIS   A HB2  1 
ATOM   2879 H HB3  A HIS   A 1 138 ? 14.023 -10.216 -7.230  0.76 18.16 ?  138 HIS   A HB3  1 
ATOM   2880 H HB3  B HIS   A 1 138 ? 13.898 -9.887  -7.144  0.24 15.55 ?  138 HIS   A HB3  1 
ATOM   2881 H HD1  A HIS   A 1 138 ? 14.637 -13.742 -7.840  0.76 21.55 ?  138 HIS   A HD1  1 
ATOM   2882 H HD1  B HIS   A 1 138 ? 14.420 -13.387 -7.929  0.24 17.19 ?  138 HIS   A HD1  1 
ATOM   2883 H HD2  A HIS   A 1 138 ? 16.620 -10.390 -7.857  0.76 20.66 ?  138 HIS   A HD2  1 
ATOM   2884 H HD2  B HIS   A 1 138 ? 16.528 -10.122 -7.675  0.24 16.36 ?  138 HIS   A HD2  1 
ATOM   2885 H HE1  A HIS   A 1 138 ? 16.832 -14.287 -8.522  0.76 22.66 ?  138 HIS   A HE1  1 
ATOM   2886 H HE1  B HIS   A 1 138 ? 16.603 -13.963 -8.630  0.24 17.55 ?  138 HIS   A HE1  1 
ATOM   2887 N N    A SER   A 1 139 ? 14.853 -10.252 -4.362  0.76 13.35 ?  139 SER   A N    1 
ATOM   2888 N N    B SER   A 1 139 ? 14.733 -9.976  -4.194  0.24 12.32 ?  139 SER   A N    1 
ATOM   2889 C CA   A SER   A 1 139 ? 15.931 -10.055 -3.400  0.76 13.10 ?  139 SER   A CA   1 
ATOM   2890 C CA   B SER   A 1 139 ? 15.833 -9.794  -3.252  0.24 12.17 ?  139 SER   A CA   1 
ATOM   2891 C C    A SER   A 1 139 ? 15.702 -10.874 -2.135  0.76 12.77 ?  139 SER   A C    1 
ATOM   2892 C C    B SER   A 1 139 ? 15.659 -10.671 -2.017  0.24 12.00 ?  139 SER   A C    1 
ATOM   2893 O O    A SER   A 1 139 ? 16.643 -11.471 -1.598  0.76 12.82 ?  139 SER   A O    1 
ATOM   2894 O O    B SER   A 1 139 ? 16.634 -11.231 -1.502  0.24 12.10 ?  139 SER   A O    1 
ATOM   2895 C CB   A SER   A 1 139 ? 16.087 -8.573  -3.068  0.76 12.78 ?  139 SER   A CB   1 
ATOM   2896 C CB   B SER   A 1 139 ? 15.941 -8.317  -2.864  0.24 12.10 ?  139 SER   A CB   1 
ATOM   2897 O OG   A SER   A 1 139 ? 17.173 -8.402  -2.173  0.76 12.45 ?  139 SER   A OG   1 
ATOM   2898 O OG   B SER   A 1 139 ? 16.955 -8.108  -1.897  0.24 12.19 ?  139 SER   A OG   1 
ATOM   2899 H H    A SER   A 1 139 ? 14.428 -9.537  -4.578  0.76 16.01 ?  139 SER   A H    1 
ATOM   2900 H H    B SER   A 1 139 ? 14.272 -9.267  -4.347  0.24 14.79 ?  139 SER   A H    1 
ATOM   2901 H HA   A SER   A 1 139 ? 16.765 -10.352 -3.797  0.76 15.73 ?  139 SER   A HA   1 
ATOM   2902 H HA   B SER   A 1 139 ? 16.663 -10.050 -3.684  0.24 14.61 ?  139 SER   A HA   1 
ATOM   2903 H HB2  A SER   A 1 139 ? 16.263 -8.075  -3.887  0.76 15.34 ?  139 SER   A HB2  1 
ATOM   2904 H HB2  B SER   A 1 139 ? 16.153 -7.799  -3.658  0.24 14.52 ?  139 SER   A HB2  1 
ATOM   2905 H HB3  A SER   A 1 139 ? 15.277 -8.246  -2.649  0.76 15.34 ?  139 SER   A HB3  1 
ATOM   2906 H HB3  B SER   A 1 139 ? 15.094 -8.025  -2.498  0.24 14.52 ?  139 SER   A HB3  1 
ATOM   2907 H HG   A SER   A 1 139 ? 17.272 -7.585  -1.992  0.76 14.94 ?  139 SER   A HG   1 
ATOM   2908 H HG   B SER   A 1 139 ? 17.000 -7.288  -1.700  0.24 14.63 ?  139 SER   A HG   1 
ATOM   2909 N N    A LEU   A 1 140 ? 14.459 -10.921 -1.647  0.76 12.80 ?  140 LEU   A N    1 
ATOM   2910 N N    B LEU   A 1 140 ? 14.425 -10.802 -1.525  0.24 12.20 ?  140 LEU   A N    1 
ATOM   2911 C CA   A LEU   A 1 140 ? 14.167 -11.728 -0.465  0.76 12.93 ?  140 LEU   A CA   1 
ATOM   2912 C CA   B LEU   A 1 140 ? 14.182 -11.642 -0.354  0.24 12.38 ?  140 LEU   A CA   1 
ATOM   2913 C C    A LEU   A 1 140 ? 14.436 -13.203 -0.734  0.76 12.71 ?  140 LEU   A C    1 
ATOM   2914 C C    B LEU   A 1 140 ? 14.409 -13.117 -0.671  0.24 13.10 ?  140 LEU   A C    1 
ATOM   2915 O O    A LEU   A 1 140 ? 15.012 -13.901 0.110   0.76 13.66 ?  140 LEU   A O    1 
ATOM   2916 O O    B LEU   A 1 140 ? 14.890 -13.874 0.181   0.24 13.43 ?  140 LEU   A O    1 
ATOM   2917 C CB   A LEU   A 1 140 ? 12.722 -11.516 -0.015  0.76 14.05 ?  140 LEU   A CB   1 
ATOM   2918 C CB   B LEU   A 1 140 ? 12.764 -11.406 0.167   0.24 12.30 ?  140 LEU   A CB   1 
ATOM   2919 C CG   A LEU   A 1 140 ? 12.278 -12.364 1.178   0.76 14.60 ?  140 LEU   A CG   1 
ATOM   2920 C CG   B LEU   A 1 140 ? 12.292 -12.267 1.339   0.24 12.38 ?  140 LEU   A CG   1 
ATOM   2921 C CD1  A LEU   A 1 140 ? 13.162 -12.144 2.406   0.76 14.92 ?  140 LEU   A CD1  1 
ATOM   2922 C CD1  B LEU   A 1 140 ? 13.238 -12.155 2.525   0.24 12.33 ?  140 LEU   A CD1  1 
ATOM   2923 C CD2  A LEU   A 1 140 ? 10.809 -12.090 1.507   0.76 15.71 ?  140 LEU   A CD2  1 
ATOM   2924 C CD2  B LEU   A 1 140 ? 10.874 -11.875 1.740   0.24 12.84 ?  140 LEU   A CD2  1 
ATOM   2925 H H    A LEU   A 1 140 ? 13.783 -10.506 -1.975  0.76 15.35 ?  140 LEU   A H    1 
ATOM   2926 H H    B LEU   A 1 140 ? 13.725 -10.414 -1.842  0.24 14.64 ?  140 LEU   A H    1 
ATOM   2927 H HA   A LEU   A 1 140 ? 14.748 -11.450 0.257   0.76 15.51 ?  140 LEU   A HA   1 
ATOM   2928 H HA   B LEU   A 1 140 ? 14.802 -11.386 0.345   0.24 14.86 ?  140 LEU   A HA   1 
ATOM   2929 H HB2  A LEU   A 1 140 ? 12.610 -10.588 0.232   0.76 16.86 ?  140 LEU   A HB2  1 
ATOM   2930 H HB2  B LEU   A 1 140 ? 12.700 -10.482 0.451   0.24 14.76 ?  140 LEU   A HB2  1 
ATOM   2931 H HB3  A LEU   A 1 140 ? 12.135 -11.731 -0.757  0.76 16.86 ?  140 LEU   A HB3  1 
ATOM   2932 H HB3  B LEU   A 1 140 ? 12.148 -11.561 -0.564  0.24 14.76 ?  140 LEU   A HB3  1 
ATOM   2933 H HG   A LEU   A 1 140 ? 12.342 -13.303 0.937   0.76 17.52 ?  140 LEU   A HG   1 
ATOM   2934 H HG   B LEU   A 1 140 ? 12.273 -13.196 1.061   0.24 14.85 ?  140 LEU   A HG   1 
ATOM   2935 H HD11 A LEU   A 1 140 ? 12.787 -12.634 3.156   0.76 17.90 ?  140 LEU   A HD11 1 
ATOM   2936 H HD11 B LEU   A 1 140 ? 12.867 -12.653 3.270   0.24 14.80 ?  140 LEU   A HD11 1 
ATOM   2937 H HD12 A LEU   A 1 140 ? 14.055 -12.473 2.213   0.76 17.90 ?  140 LEU   A HD12 1 
ATOM   2938 H HD12 B LEU   A 1 140 ? 14.099 -12.525 2.276   0.24 14.80 ?  140 LEU   A HD12 1 
ATOM   2939 H HD13 A LEU   A 1 140 ? 13.192 -11.199 2.609   0.76 17.90 ?  140 LEU   A HD13 1 
ATOM   2940 H HD13 B LEU   A 1 140 ? 13.333 -11.221 2.764   0.24 14.80 ?  140 LEU   A HD13 1 
ATOM   2941 H HD21 A LEU   A 1 140 ? 10.547 -12.639 2.267   0.76 18.85 ?  140 LEU   A HD21 1 
ATOM   2942 H HD21 B LEU   A 1 140 ? 10.591 -12.433 2.483   0.24 15.41 ?  140 LEU   A HD21 1 
ATOM   2943 H HD22 A LEU   A 1 140 ? 10.703 -11.153 1.727   0.76 18.85 ?  140 LEU   A HD22 1 
ATOM   2944 H HD22 B LEU   A 1 140 ? 10.865 -10.943 2.003   0.24 15.41 ?  140 LEU   A HD22 1 
ATOM   2945 H HD23 A LEU   A 1 140 ? 10.263 -12.315 0.737   0.76 18.85 ?  140 LEU   A HD23 1 
ATOM   2946 H HD23 B LEU   A 1 140 ? 10.283 -12.013 0.982   0.24 15.41 ?  140 LEU   A HD23 1 
ATOM   2947 N N    A ARG   A 1 141 ? 14.034 -13.689 -1.911  0.76 13.22 ?  141 ARG   A N    1 
ATOM   2948 N N    B ARG   A 1 141 ? 14.067 -13.542 -1.890  0.24 13.70 ?  141 ARG   A N    1 
ATOM   2949 C CA   A ARG   A 1 141 ? 14.298 -15.078 -2.276  0.76 14.49 ?  141 ARG   A CA   1 
ATOM   2950 C CA   B ARG   A 1 141 ? 14.267 -14.933 -2.290  0.24 14.62 ?  141 ARG   A CA   1 
ATOM   2951 C C    A ARG   A 1 141 ? 15.796 -15.359 -2.296  0.76 13.87 ?  141 ARG   A C    1 
ATOM   2952 C C    B ARG   A 1 141 ? 15.750 -15.299 -2.278  0.24 13.99 ?  141 ARG   A C    1 
ATOM   2953 O O    A ARG   A 1 141 ? 16.256 -16.375 -1.759  0.76 14.16 ?  141 ARG   A O    1 
ATOM   2954 O O    B ARG   A 1 141 ? 16.150 -16.316 -1.699  0.24 14.04 ?  141 ARG   A O    1 
ATOM   2955 C CB   A ARG   A 1 141 ? 13.677 -15.364 -3.645  0.76 16.30 ?  141 ARG   A CB   1 
ATOM   2956 C CB   B ARG   A 1 141 ? 13.664 -15.136 -3.684  0.24 16.15 ?  141 ARG   A CB   1 
ATOM   2957 C CG   A ARG   A 1 141 ? 13.702 -16.818 -4.074  0.76 19.18 ?  141 ARG   A CG   1 
ATOM   2958 C CG   B ARG   A 1 141 ? 13.565 -16.576 -4.157  0.24 17.71 ?  141 ARG   A CG   1 
ATOM   2959 C CD   A ARG   A 1 141 ? 12.661 -17.602 -3.336  0.76 22.02 ?  141 ARG   A CD   1 
ATOM   2960 C CD   B ARG   A 1 141 ? 12.545 -17.349 -3.352  0.24 18.90 ?  141 ARG   A CD   1 
ATOM   2961 N NE   A ARG   A 1 141 ? 13.256 -18.397 -2.275  0.76 23.35 ?  141 ARG   A NE   1 
ATOM   2962 N NE   B ARG   A 1 141 ? 13.184 -18.175 -2.339  0.24 19.36 ?  141 ARG   A NE   1 
ATOM   2963 C CZ   A ARG   A 1 141 ? 12.571 -18.921 -1.267  0.76 23.81 ?  141 ARG   A CZ   1 
ATOM   2964 C CZ   B ARG   A 1 141 ? 12.530 -18.859 -1.410  0.24 20.09 ?  141 ARG   A CZ   1 
ATOM   2965 N NH1  A ARG   A 1 141 ? 11.290 -18.647 -1.086  0.76 22.85 ?  141 ARG   A NH1  1 
ATOM   2966 N NH1  B ARG   A 1 141 ? 11.213 -18.792 -1.302  0.24 20.81 ?  141 ARG   A NH1  1 
ATOM   2967 N NH2  A ARG   A 1 141 ? 13.192 -19.726 -0.411  0.76 25.06 ?  141 ARG   A NH2  1 
ATOM   2968 N NH2  B ARG   A 1 141 ? 13.214 -19.627 -0.567  0.24 20.07 ?  141 ARG   A NH2  1 
ATOM   2969 H H    A ARG   A 1 141 ? 13.613 -13.240 -2.511  0.76 15.86 ?  141 ARG   A H    1 
ATOM   2970 H H    B ARG   A 1 141 ? 13.713 -13.047 -2.497  0.24 16.44 ?  141 ARG   A H    1 
ATOM   2971 H HA   A ARG   A 1 141 ? 13.889 -15.667 -1.627  0.76 17.39 ?  141 ARG   A HA   1 
ATOM   2972 H HA   B ARG   A 1 141 ? 13.807 -15.517 -1.671  0.24 17.54 ?  141 ARG   A HA   1 
ATOM   2973 H HB2  A ARG   A 1 141 ? 12.752 -15.074 -3.633  0.76 19.56 ?  141 ARG   A HB2  1 
ATOM   2974 H HB2  B ARG   A 1 141 ? 12.765 -14.768 -3.686  0.24 19.37 ?  141 ARG   A HB2  1 
ATOM   2975 H HB3  A ARG   A 1 141 ? 14.164 -14.858 -4.314  0.76 19.56 ?  141 ARG   A HB3  1 
ATOM   2976 H HB3  B ARG   A 1 141 ? 14.207 -14.658 -4.328  0.24 19.37 ?  141 ARG   A HB3  1 
ATOM   2977 H HG2  A ARG   A 1 141 ? 13.518 -16.880 -5.025  0.76 23.01 ?  141 ARG   A HG2  1 
ATOM   2978 H HG2  B ARG   A 1 141 ? 13.292 -16.591 -5.089  0.24 21.26 ?  141 ARG   A HG2  1 
ATOM   2979 H HG3  A ARG   A 1 141 ? 14.574 -17.203 -3.876  0.76 23.01 ?  141 ARG   A HG3  1 
ATOM   2980 H HG3  B ARG   A 1 141 ? 14.427 -17.009 -4.054  0.24 21.26 ?  141 ARG   A HG3  1 
ATOM   2981 H HD2  A ARG   A 1 141 ? 12.023 -16.991 -2.931  0.76 26.42 ?  141 ARG   A HD2  1 
ATOM   2982 H HD2  B ARG   A 1 141 ? 11.951 -16.728 -2.901  0.24 22.68 ?  141 ARG   A HD2  1 
ATOM   2983 H HD3  A ARG   A 1 141 ? 12.205 -18.195 -3.956  0.76 26.42 ?  141 ARG   A HD3  1 
ATOM   2984 H HD3  B ARG   A 1 141 ? 12.037 -17.926 -3.946  0.24 22.68 ?  141 ARG   A HD3  1 
ATOM   2985 H HE   A ARG   A 1 141 ? 14.075 -18.635 -2.367  0.76 28.02 ?  141 ARG   A HE   1 
ATOM   2986 H HE   B ARG   A 1 141 ? 14.042 -18.212 -2.333  0.24 23.23 ?  141 ARG   A HE   1 
ATOM   2987 H HH11 A ARG   A 1 141 ? 10.869 -18.140 -1.640  0.76 27.43 ?  141 ARG   A HH11 1 
ATOM   2988 H HH11 B ARG   A 1 141 ? 10.759 -18.303 -1.844  0.24 24.97 ?  141 ARG   A HH11 1 
ATOM   2989 H HH12 A ARG   A 1 141 ? 10.864 -18.997 -0.424  0.76 27.43 ?  141 ARG   A HH12 1 
ATOM   2990 H HH12 B ARG   A 1 141 ? 10.810 -19.243 -0.690  0.24 24.97 ?  141 ARG   A HH12 1 
ATOM   2991 H HH21 A ARG   A 1 141 ? 14.027 -19.904 -0.518  0.76 30.07 ?  141 ARG   A HH21 1 
ATOM   2992 H HH21 B ARG   A 1 141 ? 14.070 -19.679 -0.630  0.24 24.09 ?  141 ARG   A HH21 1 
ATOM   2993 H HH22 A ARG   A 1 141 ? 12.762 -20.061 0.254   0.76 30.07 ?  141 ARG   A HH22 1 
ATOM   2994 H HH22 B ARG   A 1 141 ? 12.801 -20.072 0.042   0.24 24.09 ?  141 ARG   A HH22 1 
ATOM   2995 N N    . VAL   A 1 142 ? 16.579 -14.471 -2.917  1.00 13.40 ?  142 VAL   A N    1 
ATOM   2996 C CA   . VAL   A 1 142 ? 18.023 -14.696 -2.951  1.00 13.41 ?  142 VAL   A CA   1 
ATOM   2997 C C    . VAL   A 1 142 ? 18.598 -14.676 -1.542  1.00 12.66 ?  142 VAL   A C    1 
ATOM   2998 O O    . VAL   A 1 142 ? 19.465 -15.488 -1.200  1.00 13.21 ?  142 VAL   A O    1 
ATOM   2999 C CB   . VAL   A 1 142 ? 18.717 -13.673 -3.869  1.00 13.71 ?  142 VAL   A CB   1 
ATOM   3000 C CG1  . VAL   A 1 142 ? 20.230 -13.873 -3.824  1.00 13.70 ?  142 VAL   A CG1  1 
ATOM   3001 C CG2  . VAL   A 1 142 ? 18.220 -13.809 -5.296  1.00 14.52 ?  142 VAL   A CG2  1 
ATOM   3002 H H    A VAL   A 1 142 ? 16.308 -13.751 -3.311  0.76 16.08 ?  142 VAL   A H    1 
ATOM   3003 H H    B VAL   A 1 142 ? 16.326 -13.759 -3.337  0.24 16.08 ?  142 VAL   A H    1 
ATOM   3004 H HA   . VAL   A 1 142 ? 18.189 -15.569 -3.322  1.00 16.09 ?  142 VAL   A HA   1 
ATOM   3005 H HB   . VAL   A 1 142 ? 18.526 -12.768 -3.563  1.00 16.45 ?  142 VAL   A HB   1 
ATOM   3006 H HG11 . VAL   A 1 142 ? 20.640 -13.380 -4.555  1.00 16.44 ?  142 VAL   A HG11 1 
ATOM   3007 H HG12 . VAL   A 1 142 ? 20.575 -13.536 -2.977  1.00 16.44 ?  142 VAL   A HG12 1 
ATOM   3008 H HG13 . VAL   A 1 142 ? 20.429 -14.815 -3.910  1.00 16.44 ?  142 VAL   A HG13 1 
ATOM   3009 H HG21 . VAL   A 1 142 ? 18.690 -13.170 -5.856  1.00 17.42 ?  142 VAL   A HG21 1 
ATOM   3010 H HG22 . VAL   A 1 142 ? 18.402 -14.712 -5.600  1.00 17.42 ?  142 VAL   A HG22 1 
ATOM   3011 H HG23 . VAL   A 1 142 ? 17.271 -13.634 -5.313  1.00 17.42 ?  142 VAL   A HG23 1 
ATOM   3012 N N    . CYS   A 1 143 ? 18.119 -13.761 -0.699  1.00 12.61 ?  143 CYS   A N    1 
ATOM   3013 C CA   . CYS   A 1 143 ? 18.594 -13.713 0.679   1.00 12.82 ?  143 CYS   A CA   1 
ATOM   3014 C C    . CYS   A 1 143 ? 18.374 -15.053 1.370   1.00 12.59 ?  143 CYS   A C    1 
ATOM   3015 O O    . CYS   A 1 143 ? 19.296 -15.631 1.950   1.00 12.81 ?  143 CYS   A O    1 
ATOM   3016 C CB   . CYS   A 1 143 ? 17.861 -12.603 1.428   1.00 13.26 ?  143 CYS   A CB   1 
ATOM   3017 S SG   . CYS   A 1 143 ? 18.351 -12.412 3.144   1.00 13.80 ?  143 CYS   A SG   1 
ATOM   3018 H H    . CYS   A 1 143 ? 17.515 -13.180 -0.892  1.00 15.14 ?  143 CYS   A H    1 
ATOM   3019 H HA   . CYS   A 1 143 ? 19.541 -13.523 0.684   1.00 15.38 ?  143 CYS   A HA   1 
ATOM   3020 H HB2  . CYS   A 1 143 ? 18.027 -11.763 0.976   1.00 15.91 ?  143 CYS   A HB2  1 
ATOM   3021 H HB3  . CYS   A 1 143 ? 16.912 -12.796 1.414   1.00 15.91 ?  143 CYS   A HB3  1 
ATOM   3022 H HG   . CYS   A 1 143 ? 17.780 -11.458 3.600   1.00 16.56 ?  143 CYS   A HG   1 
ATOM   3023 N N    . VAL   A 1 144 ? 17.142 -15.559 1.317   1.00 13.42 ?  144 VAL   A N    1 
ATOM   3024 C CA   . VAL   A 1 144 ? 16.799 -16.794 2.016   1.00 14.82 ?  144 VAL   A CA   1 
ATOM   3025 C C    . VAL   A 1 144 ? 17.613 -17.965 1.489   1.00 14.36 ?  144 VAL   A C    1 
ATOM   3026 O O    . VAL   A 1 144 ? 17.984 -18.868 2.249   1.00 15.19 ?  144 VAL   A O    1 
ATOM   3027 C CB   . VAL   A 1 144 ? 15.282 -17.037 1.892   1.00 17.83 ?  144 VAL   A CB   1 
ATOM   3028 C CG1  . VAL   A 1 144 ? 14.920 -18.477 2.224   1.00 19.90 ?  144 VAL   A CG1  1 
ATOM   3029 C CG2  . VAL   A 1 144 ? 14.522 -16.037 2.771   1.00 17.71 ?  144 VAL   A CG2  1 
ATOM   3030 H H    . VAL   A 1 144 ? 16.482 -15.201 0.882   1.00 16.10 ?  144 VAL   A H    1 
ATOM   3031 H HA   . VAL   A 1 144 ? 16.999 -16.684 2.954   1.00 17.79 ?  144 VAL   A HA   1 
ATOM   3032 H HB   . VAL   A 1 144 ? 15.011 -16.871 0.972   1.00 21.39 ?  144 VAL   A HB   1 
ATOM   3033 H HG11 . VAL   A 1 144 ? 13.968 -18.529 2.411   1.00 23.88 ?  144 VAL   A HG11 1 
ATOM   3034 H HG12 . VAL   A 1 144 ? 15.135 -19.042 1.466   1.00 23.88 ?  144 VAL   A HG12 1 
ATOM   3035 H HG13 . VAL   A 1 144 ? 15.423 -18.756 3.004   1.00 23.88 ?  144 VAL   A HG13 1 
ATOM   3036 H HG21 . VAL   A 1 144 ? 13.568 -16.204 2.698   1.00 21.25 ?  144 VAL   A HG21 1 
ATOM   3037 H HG22 . VAL   A 1 144 ? 14.806 -16.144 3.692   1.00 21.25 ?  144 VAL   A HG22 1 
ATOM   3038 H HG23 . VAL   A 1 144 ? 14.719 -15.133 2.470   1.00 21.25 ?  144 VAL   A HG23 1 
ATOM   3039 N N    . ASP   A 1 145 ? 17.868 -17.992 0.183   1.00 14.55 ?  145 ASP   A N    1 
ATOM   3040 C CA   . ASP   A 1 145 ? 18.592 -19.092 -0.446  1.00 15.01 ?  145 ASP   A CA   1 
ATOM   3041 C C    . ASP   A 1 145 ? 20.111 -18.936 -0.405  1.00 14.75 ?  145 ASP   A C    1 
ATOM   3042 O O    . ASP   A 1 145 ? 20.817 -19.828 -0.890  1.00 16.86 ?  145 ASP   A O    1 
ATOM   3043 C CB   . ASP   A 1 145 ? 18.149 -19.240 -1.904  1.00 16.95 ?  145 ASP   A CB   1 
ATOM   3044 C CG   . ASP   A 1 145 ? 16.692 -19.650 -2.038  1.00 18.81 ?  145 ASP   A CG   1 
ATOM   3045 O OD1  . ASP   A 1 145 ? 16.117 -20.172 -1.058  1.00 19.48 ?  145 ASP   A OD1  1 
ATOM   3046 O OD2  . ASP   A 1 145 ? 16.122 -19.446 -3.128  1.00 20.35 -1 145 ASP   A OD2  1 
ATOM   3047 H H    . ASP   A 1 145 ? 17.614 -17.381 -0.370  1.00 17.46 ?  145 ASP   A H    1 
ATOM   3048 H HA   . ASP   A 1 145 ? 18.365 -19.912 0.017   1.00 18.01 ?  145 ASP   A HA   1 
ATOM   3049 H HB2  . ASP   A 1 145 ? 18.270 -18.394 -2.359  1.00 20.34 ?  145 ASP   A HB2  1 
ATOM   3050 H HB3  . ASP   A 1 145 ? 18.689 -19.927 -2.325  1.00 20.34 ?  145 ASP   A HB3  1 
ATOM   3051 N N    . THR   A 1 146 ? 20.637 -17.842 0.147   1.00 13.25 ?  146 THR   A N    1 
ATOM   3052 C CA   . THR   A 1 146 ? 22.075 -17.590 0.160   1.00 12.49 ?  146 THR   A CA   1 
ATOM   3053 C C    . THR   A 1 146 ? 22.634 -17.404 1.557   1.00 12.71 ?  146 THR   A C    1 
ATOM   3054 O O    . THR   A 1 146 ? 23.708 -17.934 1.864   1.00 13.50 ?  146 THR   A O    1 
ATOM   3055 C CB   . THR   A 1 146 ? 22.395 -16.342 -0.678  1.00 12.34 ?  146 THR   A CB   1 
ATOM   3056 O OG1  . THR   A 1 146 ? 21.870 -16.513 -1.995  1.00 13.56 ?  146 THR   A OG1  1 
ATOM   3057 C CG2  . THR   A 1 146 ? 23.900 -16.108 -0.767  1.00 13.53 ?  146 THR   A CG2  1 
ATOM   3058 H H    . THR   A 1 146 ? 20.172 -17.217 0.522   1.00 15.90 ?  146 THR   A H    1 
ATOM   3059 H HA   . THR   A 1 146 ? 22.532 -18.339 -0.243  1.00 14.99 ?  146 THR   A HA   1 
ATOM   3060 H HB   . THR   A 1 146 ? 21.994 -15.560 -0.266  1.00 14.81 ?  146 THR   A HB   1 
ATOM   3061 H HG1  . THR   A 1 146 ? 21.033 -16.586 -1.961  1.00 16.27 ?  146 THR   A HG1  1 
ATOM   3062 H HG21 . THR   A 1 146 ? 24.091 -15.444 -1.449  1.00 16.23 ?  146 THR   A HG21 1 
ATOM   3063 H HG22 . THR   A 1 146 ? 24.239 -15.789 0.084   1.00 16.23 ?  146 THR   A HG22 1 
ATOM   3064 H HG23 . THR   A 1 146 ? 24.349 -16.934 -0.999  1.00 16.23 ?  146 THR   A HG23 1 
ATOM   3065 N N    . VAL   A 1 147 ? 21.953 -16.637 2.399   1.00 12.47 ?  147 VAL   A N    1 
ATOM   3066 C CA   . VAL   A 1 147 ? 22.444 -16.336 3.736   1.00 12.65 ?  147 VAL   A CA   1 
ATOM   3067 C C    . VAL   A 1 147 ? 22.124 -17.502 4.658   1.00 13.18 ?  147 VAL   A C    1 
ATOM   3068 O O    . VAL   A 1 147 ? 20.983 -17.986 4.701   1.00 13.66 ?  147 VAL   A O    1 
ATOM   3069 C CB   . VAL   A 1 147 ? 21.825 -15.027 4.252   1.00 12.88 ?  147 VAL   A CB   1 
ATOM   3070 C CG1  . VAL   A 1 147 ? 22.359 -14.712 5.634   1.00 13.91 ?  147 VAL   A CG1  1 
ATOM   3071 C CG2  . VAL   A 1 147 ? 22.108 -13.891 3.286   1.00 13.10 ?  147 VAL   A CG2  1 
ATOM   3072 H H    . VAL   A 1 147 ? 21.187 -16.283 2.223   1.00 14.97 ?  147 VAL   A H    1 
ATOM   3073 H HA   . VAL   A 1 147 ? 23.408 -16.227 3.703   1.00 15.18 ?  147 VAL   A HA   1 
ATOM   3074 H HB   . VAL   A 1 147 ? 20.866 -15.137 4.321   1.00 15.46 ?  147 VAL   A HB   1 
ATOM   3075 H HG11 . VAL   A 1 147 ? 22.109 -13.809 5.870   1.00 16.69 ?  147 VAL   A HG11 1 
ATOM   3076 H HG12 . VAL   A 1 147 ? 21.976 -15.339 6.273   1.00 16.69 ?  147 VAL   A HG12 1 
ATOM   3077 H HG13 . VAL   A 1 147 ? 23.325 -14.800 5.629   1.00 16.69 ?  147 VAL   A HG13 1 
ATOM   3078 H HG21 . VAL   A 1 147 ? 21.792 -13.063 3.675   1.00 15.72 ?  147 VAL   A HG21 1 
ATOM   3079 H HG22 . VAL   A 1 147 ? 23.064 -13.843 3.129   1.00 15.72 ?  147 VAL   A HG22 1 
ATOM   3080 H HG23 . VAL   A 1 147 ? 21.644 -14.067 2.453   1.00 15.72 ?  147 VAL   A HG23 1 
ATOM   3081 N N    . ARG   A 1 148 ? 23.148 -17.979 5.365   1.00 13.44 ?  148 ARG   A N    1 
ATOM   3082 C CA   . ARG   A 1 148 ? 23.013 -19.058 6.327   1.00 13.52 ?  148 ARG   A CA   1 
ATOM   3083 C C    . ARG   A 1 148 ? 23.143 -18.582 7.763   1.00 13.79 ?  148 ARG   A C    1 
ATOM   3084 O O    . ARG   A 1 148 ? 22.733 -19.304 8.682   1.00 15.65 ?  148 ARG   A O    1 
ATOM   3085 C CB   . ARG   A 1 148 ? 24.055 -20.150 6.045   1.00 14.14 ?  148 ARG   A CB   1 
ATOM   3086 C CG   . ARG   A 1 148 ? 23.878 -20.794 4.681   1.00 15.26 ?  148 ARG   A CG   1 
ATOM   3087 C CD   . ARG   A 1 148 ? 24.961 -21.822 4.376   1.00 16.46 ?  148 ARG   A CD   1 
ATOM   3088 N NE   . ARG   A 1 148 ? 26.300 -21.240 4.409   1.00 16.73 ?  148 ARG   A NE   1 
ATOM   3089 C CZ   . ARG   A 1 148 ? 26.821 -20.509 3.433   1.00 15.68 ?  148 ARG   A CZ   1 
ATOM   3090 N NH1  . ARG   A 1 148 ? 26.150 -20.265 2.319   1.00 16.37 ?  148 ARG   A NH1  1 
ATOM   3091 N NH2  . ARG   A 1 148 ? 28.043 -19.991 3.584   1.00 16.27 ?  148 ARG   A NH2  1 
ATOM   3092 H H    . ARG   A 1 148 ? 23.954 -17.682 5.288   1.00 16.13 ?  148 ARG   A H    1 
ATOM   3093 H HA   . ARG   A 1 148 ? 22.139 -19.455 6.229   1.00 16.23 ?  148 ARG   A HA   1 
ATOM   3094 H HB2  . ARG   A 1 148 ? 24.942 -19.767 6.081   1.00 16.96 ?  148 ARG   A HB2  1 
ATOM   3095 H HB3  . ARG   A 1 148 ? 23.967 -20.851 6.713   1.00 16.96 ?  148 ARG   A HB3  1 
ATOM   3096 H HG2  . ARG   A 1 148 ? 23.018 -21.240 4.651   1.00 18.32 ?  148 ARG   A HG2  1 
ATOM   3097 H HG3  . ARG   A 1 148 ? 23.917 -20.101 4.001   1.00 18.32 ?  148 ARG   A HG3  1 
ATOM   3098 H HD2  . ARG   A 1 148 ? 24.926 -22.528 5.040   1.00 19.75 ?  148 ARG   A HD2  1 
ATOM   3099 H HD3  . ARG   A 1 148 ? 24.811 -22.192 3.491   1.00 19.75 ?  148 ARG   A HD3  1 
ATOM   3100 H HE   . ARG   A 1 148 ? 26.785 -21.384 5.100   1.00 20.07 ?  148 ARG   A HE   1 
ATOM   3101 H HH11 . ARG   A 1 148 ? 25.362 -20.581 2.208   1.00 19.65 ?  148 ARG   A HH11 1 
ATOM   3102 H HH12 . ARG   A 1 148 ? 26.505 -19.775 1.701   1.00 19.65 ?  148 ARG   A HH12 1 
ATOM   3103 H HH21 . ARG   A 1 148 ? 28.484 -20.135 4.306   1.00 19.52 ?  148 ARG   A HH21 1 
ATOM   3104 H HH22 . ARG   A 1 148 ? 28.387 -19.504 2.961   1.00 19.52 ?  148 ARG   A HH22 1 
ATOM   3105 N N    . THR   A 1 149 ? 23.689 -17.387 7.970   1.00 13.84 ?  149 THR   A N    1 
ATOM   3106 C CA   . THR   A 1 149 ? 23.763 -16.783 9.286   1.00 14.09 ?  149 THR   A CA   1 
ATOM   3107 C C    . THR   A 1 149 ? 22.434 -16.090 9.593   1.00 13.82 ?  149 THR   A C    1 
ATOM   3108 O O    . THR   A 1 149 ? 21.498 -16.092 8.784   1.00 14.42 ?  149 THR   A O    1 
ATOM   3109 C CB   . THR   A 1 149 ? 24.965 -15.845 9.347   1.00 14.77 ?  149 THR   A CB   1 
ATOM   3110 O OG1  . THR   A 1 149 ? 24.842 -14.906 8.277   1.00 14.85 ?  149 THR   A OG1  1 
ATOM   3111 C CG2  . THR   A 1 149 ? 26.278 -16.638 9.218   1.00 15.44 ?  149 THR   A CG2  1 
ATOM   3112 H H    . THR   A 1 149 ? 24.035 -16.895 7.349   1.00 16.60 ?  149 THR   A H    1 
ATOM   3113 H HA   . THR   A 1 149 ? 23.893 -17.487 9.943   1.00 16.91 ?  149 THR   A HA   1 
ATOM   3114 H HB   . THR   A 1 149 ? 24.959 -15.377 10.195  1.00 17.72 ?  149 THR   A HB   1 
ATOM   3115 H HG1  . THR   A 1 149 ? 25.492 -14.379 8.283   1.00 17.82 ?  149 THR   A HG1  1 
ATOM   3116 H HG21 . THR   A 1 149 ? 27.034 -16.038 9.277   1.00 18.53 ?  149 THR   A HG21 1 
ATOM   3117 H HG22 . THR   A 1 149 ? 26.341 -17.298 9.929   1.00 18.53 ?  149 THR   A HG22 1 
ATOM   3118 H HG23 . THR   A 1 149 ? 26.306 -17.100 8.362   1.00 18.53 ?  149 THR   A HG23 1 
ATOM   3119 N N    . ASN   A 1 150 ? 22.321 -15.543 10.798  1.00 13.61 ?  150 ASN   A N    1 
ATOM   3120 C CA   . ASN   A 1 150 ? 21.042 -15.039 11.296  1.00 14.53 ?  150 ASN   A CA   1 
ATOM   3121 C C    . ASN   A 1 150 ? 20.855 -13.597 10.844  1.00 13.77 ?  150 ASN   A C    1 
ATOM   3122 O O    . ASN   A 1 150 ? 21.594 -12.702 11.274  1.00 15.46 ?  150 ASN   A O    1 
ATOM   3123 C CB   . ASN   A 1 150 ? 21.000 -15.161 12.814  1.00 17.49 ?  150 ASN   A CB   1 
ATOM   3124 C CG   . ASN   A 1 150 ? 20.872 -16.593 13.267  1.00 21.87 ?  150 ASN   A CG   1 
ATOM   3125 O OD1  . ASN   A 1 150 ? 20.254 -17.409 12.587  1.00 23.24 ?  150 ASN   A OD1  1 
ATOM   3126 N ND2  . ASN   A 1 150 ? 21.461 -16.913 14.411  1.00 24.16 ?  150 ASN   A ND2  1 
ATOM   3127 H H    . ASN   A 1 150 ? 22.975 -15.442 11.346  1.00 16.33 ?  150 ASN   A H    1 
ATOM   3128 H HA   . ASN   A 1 150 ? 20.320 -15.579 10.928  1.00 17.43 ?  150 ASN   A HA   1 
ATOM   3129 H HB2  . ASN   A 1 150 ? 21.822 -14.803 13.184  1.00 20.99 ?  150 ASN   A HB2  1 
ATOM   3130 H HB3  . ASN   A 1 150 ? 20.237 -14.670 13.153  1.00 20.99 ?  150 ASN   A HB3  1 
ATOM   3131 H HD21 . ASN   A 1 150 ? 21.416 -17.721 14.712  1.00 28.99 ?  150 ASN   A HD21 1 
ATOM   3132 H HD22 . ASN   A 1 150 ? 21.886 -16.316 14.860  1.00 28.99 ?  150 ASN   A HD22 1 
ATOM   3133 N N    . VAL   A 1 151 ? 19.876 -13.365 9.979   1.00 13.40 ?  151 VAL   A N    1 
ATOM   3134 C CA   . VAL   A 1 151 ? 19.660 -12.052 9.391   1.00 13.32 ?  151 VAL   A CA   1 
ATOM   3135 C C    . VAL   A 1 151 ? 18.270 -11.542 9.753   1.00 13.32 ?  151 VAL   A C    1 
ATOM   3136 O O    . VAL   A 1 151 ? 17.266 -12.258 9.605   1.00 14.62 ?  151 VAL   A O    1 
ATOM   3137 C CB   . VAL   A 1 151 ? 19.951 -12.036 7.874   1.00 14.84 ?  151 VAL   A CB   1 
ATOM   3138 C CG1  . VAL   A 1 151 ? 19.114 -13.053 7.116   1.00 15.89 ?  151 VAL   A CG1  1 
ATOM   3139 C CG2  . VAL   A 1 151 ? 19.771 -10.628 7.307   1.00 15.14 ?  151 VAL   A CG2  1 
ATOM   3140 H H    . VAL   A 1 151 ? 19.313 -13.963 9.713   1.00 16.08 ?  151 VAL   A H    1 
ATOM   3141 H HA   . VAL   A 1 151 ? 20.297 -11.440 9.791   1.00 15.98 ?  151 VAL   A HA   1 
ATOM   3142 H HB   . VAL   A 1 151 ? 20.884 -12.278 7.740   1.00 17.81 ?  151 VAL   A HB   1 
ATOM   3143 H HG11 . VAL   A 1 151 ? 19.323 -13.000 6.168   1.00 19.07 ?  151 VAL   A HG11 1 
ATOM   3144 H HG12 . VAL   A 1 151 ? 19.326 -13.947 7.444   1.00 19.07 ?  151 VAL   A HG12 1 
ATOM   3145 H HG13 . VAL   A 1 151 ? 18.175 -12.868 7.259   1.00 19.07 ?  151 VAL   A HG13 1 
ATOM   3146 H HG21 . VAL   A 1 151 ? 20.093 -10.613 6.389   1.00 18.17 ?  151 VAL   A HG21 1 
ATOM   3147 H HG22 . VAL   A 1 151 ? 18.831 -10.394 7.327   1.00 18.17 ?  151 VAL   A HG22 1 
ATOM   3148 H HG23 . VAL   A 1 151 ? 20.282 -10.002 7.843   1.00 18.17 ?  151 VAL   A HG23 1 
ATOM   3149 N N    . TYR   A 1 152 ? 18.248 -10.294 10.235  1.00 13.46 ?  152 TYR   A N    1 
ATOM   3150 C CA   . TYR   A 1 152 ? 17.051 -9.561  10.621  1.00 13.12 ?  152 TYR   A CA   1 
ATOM   3151 C C    . TYR   A 1 152 ? 16.860 -8.455  9.595   1.00 12.51 ?  152 TYR   A C    1 
ATOM   3152 O O    . TYR   A 1 152 ? 17.639 -7.492  9.556   1.00 12.93 ?  152 TYR   A O    1 
ATOM   3153 C CB   . TYR   A 1 152 ? 17.234 -9.012  12.034  1.00 13.58 ?  152 TYR   A CB   1 
ATOM   3154 C CG   . TYR   A 1 152 ? 17.194 -10.139 13.032  1.00 14.60 ?  152 TYR   A CG   1 
ATOM   3155 C CD1  . TYR   A 1 152 ? 18.328 -10.894 13.313  1.00 16.12 ?  152 TYR   A CD1  1 
ATOM   3156 C CD2  . TYR   A 1 152 ? 16.005 -10.495 13.654  1.00 14.95 ?  152 TYR   A CD2  1 
ATOM   3157 C CE1  . TYR   A 1 152 ? 18.287 -11.955 14.196  1.00 17.21 ?  152 TYR   A CE1  1 
ATOM   3158 C CE2  . TYR   A 1 152 ? 15.951 -11.560 14.546  1.00 16.58 ?  152 TYR   A CE2  1 
ATOM   3159 C CZ   . TYR   A 1 152 ? 17.097 -12.286 14.812  1.00 17.00 ?  152 TYR   A CZ   1 
ATOM   3160 O OH   . TYR   A 1 152 ? 17.054 -13.349 15.691  1.00 19.72 ?  152 TYR   A OH   1 
ATOM   3161 H H    . TYR   A 1 152 ? 18.965 -9.822  10.338  1.00 16.15 ?  152 TYR   A H    1 
ATOM   3162 H HA   . TYR   A 1 152 ? 16.282 -10.151 10.604  1.00 15.75 ?  152 TYR   A HA   1 
ATOM   3163 H HB2  . TYR   A 1 152 ? 18.098 -8.577  12.100  1.00 16.30 ?  152 TYR   A HB2  1 
ATOM   3164 H HB3  . TYR   A 1 152 ? 16.526 -8.388  12.239  1.00 16.30 ?  152 TYR   A HB3  1 
ATOM   3165 H HD1  . TYR   A 1 152 ? 19.130 -10.674 12.891  1.00 19.34 ?  152 TYR   A HD1  1 
ATOM   3166 H HD2  . TYR   A 1 152 ? 15.229 -10.010 13.471  1.00 17.94 ?  152 TYR   A HD2  1 
ATOM   3167 H HE1  . TYR   A 1 152 ? 19.058 -12.440 14.378  1.00 20.66 ?  152 TYR   A HE1  1 
ATOM   3168 H HE2  . TYR   A 1 152 ? 15.150 -11.778 14.963  1.00 19.89 ?  152 TYR   A HE2  1 
ATOM   3169 H HH   . TYR   A 1 152 ? 16.277 -13.427 16.002  1.00 23.67 ?  152 TYR   A HH   1 
ATOM   3170 N N    A LEU   A 1 153 ? 15.856 -8.626  8.737   0.76 12.73 ?  153 LEU   A N    1 
ATOM   3171 N N    B LEU   A 1 153 ? 15.825 -8.581  8.772   0.24 12.66 ?  153 LEU   A N    1 
ATOM   3172 C CA   A LEU   A 1 153 ? 15.601 -7.735  7.613   0.76 12.95 ?  153 LEU   A CA   1 
ATOM   3173 C CA   B LEU   A 1 153 ? 15.569 -7.617  7.713   0.24 12.71 ?  153 LEU   A CA   1 
ATOM   3174 C C    A LEU   A 1 153 ? 14.601 -6.652  7.996   0.76 13.01 ?  153 LEU   A C    1 
ATOM   3175 C C    B LEU   A 1 153 ? 14.610 -6.540  8.201   0.24 12.53 ?  153 LEU   A C    1 
ATOM   3176 O O    A LEU   A 1 153 ? 13.495 -6.954  8.459   0.76 14.35 ?  153 LEU   A O    1 
ATOM   3177 O O    B LEU   A 1 153 ? 13.526 -6.845  8.708   0.24 13.21 ?  153 LEU   A O    1 
ATOM   3178 C CB   A LEU   A 1 153 ? 15.036 -8.528  6.434   0.76 12.67 ?  153 LEU   A CB   1 
ATOM   3179 C CB   B LEU   A 1 153 ? 14.989 -8.318  6.487   0.24 12.91 ?  153 LEU   A CB   1 
ATOM   3180 C CG   A LEU   A 1 153 ? 15.979 -9.527  5.768   0.76 12.76 ?  153 LEU   A CG   1 
ATOM   3181 C CG   B LEU   A 1 153 ? 15.913 -9.374  5.880   0.24 13.13 ?  153 LEU   A CG   1 
ATOM   3182 C CD1  A LEU   A 1 153 ? 15.195 -10.420 4.823   0.76 13.12 ?  153 LEU   A CD1  1 
ATOM   3183 C CD1  B LEU   A 1 153 ? 15.169 -10.196 4.845   0.24 13.39 ?  153 LEU   A CD1  1 
ATOM   3184 C CD2  A LEU   A 1 153 ? 17.078 -8.791  5.017   0.76 13.38 ?  153 LEU   A CD2  1 
ATOM   3185 C CD2  B LEU   A 1 153 ? 17.155 -8.727  5.274   0.24 13.53 ?  153 LEU   A CD2  1 
ATOM   3186 H H    A LEU   A 1 153 ? 15.281 -9.272  8.797   0.76 15.27 ?  153 LEU   A H    1 
ATOM   3187 H H    B LEU   A 1 153 ? 15.247 -9.223  8.809   0.24 15.19 ?  153 LEU   A H    1 
ATOM   3188 H HA   A LEU   A 1 153 ? 16.426 -7.318  7.343   0.76 15.54 ?  153 LEU   A HA   1 
ATOM   3189 H HA   B LEU   A 1 153 ? 16.401 -7.195  7.463   0.24 15.25 ?  153 LEU   A HA   1 
ATOM   3190 H HB2  A LEU   A 1 153 ? 14.263 -9.026  6.742   0.76 15.20 ?  153 LEU   A HB2  1 
ATOM   3191 H HB2  B LEU   A 1 153 ? 14.162 -8.756  6.742   0.24 15.49 ?  153 LEU   A HB2  1 
ATOM   3192 H HB3  A LEU   A 1 153 ? 14.759 -7.897  5.750   0.76 15.20 ?  153 LEU   A HB3  1 
ATOM   3193 H HB3  B LEU   A 1 153 ? 14.810 -7.650  5.806   0.24 15.49 ?  153 LEU   A HB3  1 
ATOM   3194 H HG   A LEU   A 1 153 ? 16.395 -10.083 6.449   0.76 15.31 ?  153 LEU   A HG   1 
ATOM   3195 H HG   B LEU   A 1 153 ? 16.206 -9.973  6.584   0.24 15.76 ?  153 LEU   A HG   1 
ATOM   3196 H HD11 A LEU   A 1 153 ? 15.778 -11.121 4.494   0.76 15.74 ?  153 LEU   A HD11 1 
ATOM   3197 H HD11 B LEU   A 1 153 ? 15.761 -10.883 4.505   0.24 16.07 ?  153 LEU   A HD11 1 
ATOM   3198 H HD12 A LEU   A 1 153 ? 14.449 -10.806 5.304   0.76 15.74 ?  153 LEU   A HD12 1 
ATOM   3199 H HD12 B LEU   A 1 153 ? 14.395 -10.602 5.265   0.24 16.07 ?  153 LEU   A HD12 1 
ATOM   3200 H HD13 A LEU   A 1 153 ? 14.871 -9.882  4.083   0.76 15.74 ?  153 LEU   A HD13 1 
ATOM   3201 H HD13 B LEU   A 1 153 ? 14.887 -9.613  4.123   0.24 16.07 ?  153 LEU   A HD13 1 
ATOM   3202 H HD21 A LEU   A 1 153 ? 17.649 -9.439  4.582   0.76 16.06 ?  153 LEU   A HD21 1 
ATOM   3203 H HD21 B LEU   A 1 153 ? 17.667 -9.406  4.807   0.24 16.24 ?  153 LEU   A HD21 1 
ATOM   3204 H HD22 A LEU   A 1 153 ? 16.667 -8.211  4.358   0.76 16.06 ?  153 LEU   A HD22 1 
ATOM   3205 H HD22 B LEU   A 1 153 ? 16.880 -8.034  4.654   0.24 16.24 ?  153 LEU   A HD22 1 
ATOM   3206 H HD23 A LEU   A 1 153 ? 17.592 -8.264  5.648   0.76 16.06 ?  153 LEU   A HD23 1 
ATOM   3207 H HD23 B LEU   A 1 153 ? 17.692 -8.341  5.985   0.24 16.24 ?  153 LEU   A HD23 1 
ATOM   3208 N N    A ALA   A 1 154 ? 14.979 -5.398  7.758   0.76 12.95 ?  154 ALA   A N    1 
ATOM   3209 N N    B ALA   A 1 154 ? 15.016 -5.284  8.043   0.24 12.25 ?  154 ALA   A N    1 
ATOM   3210 C CA   A ALA   A 1 154 ? 14.116 -4.243  7.974   0.76 13.59 ?  154 ALA   A CA   1 
ATOM   3211 C CA   B ALA   A 1 154 ? 14.181 -4.130  8.347   0.24 12.83 ?  154 ALA   A CA   1 
ATOM   3212 C C    A ALA   A 1 154 ? 13.614 -3.744  6.625   0.76 12.71 ?  154 ALA   A C    1 
ATOM   3213 C C    B ALA   A 1 154 ? 13.734 -3.521  7.025   0.24 12.67 ?  154 ALA   A C    1 
ATOM   3214 O O    A ALA   A 1 154 ? 14.410 -3.360  5.764   0.76 13.42 ?  154 ALA   A O    1 
ATOM   3215 O O    B ALA   A 1 154 ? 14.570 -3.096  6.221   0.24 12.54 ?  154 ALA   A O    1 
ATOM   3216 C CB   A ALA   A 1 154 ? 14.880 -3.130  8.688   0.76 14.06 ?  154 ALA   A CB   1 
ATOM   3217 C CB   B ALA   A 1 154 ? 14.955 -3.107  9.177   0.24 13.33 ?  154 ALA   A CB   1 
ATOM   3218 H H    A ALA   A 1 154 ? 15.757 -5.190  7.454   0.76 15.55 ?  154 ALA   A H    1 
ATOM   3219 H H    B ALA   A 1 154 ? 15.796 -5.067  7.746   0.24 14.70 ?  154 ALA   A H    1 
ATOM   3220 H HA   A ALA   A 1 154 ? 13.355 -4.499  8.516   0.76 16.30 ?  154 ALA   A HA   1 
ATOM   3221 H HA   B ALA   A 1 154 ? 13.398 -4.409  8.844   0.24 15.40 ?  154 ALA   A HA   1 
ATOM   3222 H HB1  A ALA   A 1 154 ? 14.285 -2.375  8.819   0.76 16.87 ?  154 ALA   A HB1  1 
ATOM   3223 H HB1  B ALA   A 1 154 ? 14.368 -2.368  9.400   0.24 15.99 ?  154 ALA   A HB1  1 
ATOM   3224 H HB2  A ALA   A 1 154 ? 15.192 -3.460  9.544   0.76 16.87 ?  154 ALA   A HB2  1 
ATOM   3225 H HB2  B ALA   A 1 154 ? 15.269 -3.534  9.990   0.24 15.99 ?  154 ALA   A HB2  1 
ATOM   3226 H HB3  A ALA   A 1 154 ? 15.636 -2.864  8.140   0.76 16.87 ?  154 ALA   A HB3  1 
ATOM   3227 H HB3  B ALA   A 1 154 ? 15.711 -2.786  8.661   0.24 15.99 ?  154 ALA   A HB3  1 
ATOM   3228 N N    A VAL   A 1 155 ? 12.294 -3.751  6.448   0.46 10.71 ?  155 VAL   A N    1 
ATOM   3229 N N    B VAL   A 1 155 ? 12.423 -3.496  6.795   0.24 13.16 ?  155 VAL   A N    1 
ATOM   3230 C CA   A VAL   A 1 155 ? 11.632 -3.295  5.229   0.46 13.21 ?  155 VAL   A CA   1 
ATOM   3231 C CA   B VAL   A 1 155 ? 11.841 -2.970  5.564   0.24 14.76 ?  155 VAL   A CA   1 
ATOM   3232 C CA   T VAL   A 1 155 ? 11.627 -3.314  5.310   0.30 15.48 ?  155 VAL   A CA   1 
ATOM   3233 C C    A VAL   A 1 155 ? 10.898 -2.002  5.561   0.46 14.74 ?  155 VAL   A C    1 
ATOM   3234 C C    B VAL   A 1 155 ? 10.995 -1.760  5.937   0.24 16.64 ?  155 VAL   A C    1 
ATOM   3235 C C    T VAL   A 1 155 ? 11.004 -1.945  5.602   0.30 15.22 ?  155 VAL   A C    1 
ATOM   3236 O O    A VAL   A 1 155 ? 9.915  -2.016  6.311   0.46 15.80 ?  155 VAL   A O    1 
ATOM   3237 O O    B VAL   A 1 155 ? 9.941  -1.901  6.571   0.24 17.18 ?  155 VAL   A O    1 
ATOM   3238 O O    T VAL   A 1 155 ? 10.167 -1.809  6.493   0.30 15.23 ?  155 VAL   A O    1 
ATOM   3239 C CB   A VAL   A 1 155 ? 10.658 -4.352  4.688   0.46 14.21 ?  155 VAL   A CB   1 
ATOM   3240 C CB   B VAL   A 1 155 ? 11.011 -4.028  4.823   0.24 14.74 ?  155 VAL   A CB   1 
ATOM   3241 C CB   T VAL   A 1 155 ? 10.606 -4.332  4.753   0.30 15.82 ?  155 VAL   A CB   1 
ATOM   3242 C CG1  A VAL   A 1 155 ? 9.960  -3.846  3.429   0.46 14.99 ?  155 VAL   A CG1  1 
ATOM   3243 C CG1  B VAL   A 1 155 ? 10.409 -3.441  3.558   0.24 15.01 ?  155 VAL   A CG1  1 
ATOM   3244 C CG1  T VAL   A 1 155 ? 9.910  -3.776  3.521   0.30 16.08 ?  155 VAL   A CG1  1 
ATOM   3245 C CG2  A VAL   A 1 155 ? 11.389 -5.663  4.413   0.46 15.23 ?  155 VAL   A CG2  1 
ATOM   3246 C CG2  B VAL   A 1 155 ? 11.875 -5.239  4.493   0.24 14.51 ?  155 VAL   A CG2  1 
ATOM   3247 C CG2  T VAL   A 1 155 ? 11.298 -5.656  4.426   0.30 16.30 ?  155 VAL   A CG2  1 
ATOM   3248 H H    A VAL   A 1 155 ? 11.743 -4.048  7.039   0.46 12.86 ?  155 VAL   A H    1 
ATOM   3249 H H    B VAL   A 1 155 ? 11.835 -3.782  7.355   0.24 15.79 ?  155 VAL   A H    1 
ATOM   3250 H HA   A VAL   A 1 155 ? 12.297 -3.108  4.549   0.46 15.85 ?  155 VAL   A HA   1 
ATOM   3251 H HA   B VAL   A 1 155 ? 12.549 -2.673  4.972   0.24 17.71 ?  155 VAL   A HA   1 
ATOM   3252 H HB   A VAL   A 1 155 ? 9.977  -4.524  5.359   0.46 17.05 ?  155 VAL   A HB   1 
ATOM   3253 H HB   B VAL   A 1 155 ? 10.287 -4.323  5.395   0.24 17.68 ?  155 VAL   A HB   1 
ATOM   3254 H HB   T VAL   A 1 155 ? 9.932  -4.509  5.428   0.30 18.98 ?  155 VAL   A HB   1 
ATOM   3255 H HG11 A VAL   A 1 155 ? 9.474  -4.581  3.023   0.46 17.99 ?  155 VAL   A HG11 1 
ATOM   3256 H HG11 B VAL   A 1 155 ? 10.061 -4.163  3.013   0.24 18.02 ?  155 VAL   A HG11 1 
ATOM   3257 H HG11 T VAL   A 1 155 ? 9.415  -4.490  3.089   0.30 19.30 ?  155 VAL   A HG11 1 
ATOM   3258 H HG12 A VAL   A 1 155 ? 9.342  -3.137  3.669   0.46 17.99 ?  155 VAL   A HG12 1 
ATOM   3259 H HG12 B VAL   A 1 155 ? 9.693  -2.834  3.800   0.24 18.02 ?  155 VAL   A HG12 1 
ATOM   3260 H HG12 T VAL   A 1 155 ? 9.304  -3.070  3.792   0.30 19.30 ?  155 VAL   A HG12 1 
ATOM   3261 H HG13 A VAL   A 1 155 ? 10.628 -3.511  2.811   0.46 17.99 ?  155 VAL   A HG13 1 
ATOM   3262 H HG13 B VAL   A 1 155 ? 11.100 -2.964  3.073   0.24 18.02 ?  155 VAL   A HG13 1 
ATOM   3263 H HG13 T VAL   A 1 155 ? 10.580 -3.426  2.913   0.30 19.30 ?  155 VAL   A HG13 1 
ATOM   3264 H HG21 A VAL   A 1 155 ? 10.771 -6.289  4.006   0.46 18.27 ?  155 VAL   A HG21 1 
ATOM   3265 H HG21 B VAL   A 1 155 ? 11.345 -5.876  3.988   0.24 17.42 ?  155 VAL   A HG21 1 
ATOM   3266 H HG21 T VAL   A 1 155 ? 10.641 -6.282  4.082   0.30 19.56 ?  155 VAL   A HG21 1 
ATOM   3267 H HG22 A VAL   A 1 155 ? 12.129 -5.488  3.810   0.46 18.27 ?  155 VAL   A HG22 1 
ATOM   3268 H HG22 B VAL   A 1 155 ? 12.636 -4.951  3.965   0.24 17.42 ?  155 VAL   A HG22 1 
ATOM   3269 H HG22 T VAL   A 1 155 ? 11.984 -5.498  3.757   0.30 19.56 ?  155 VAL   A HG22 1 
ATOM   3270 H HG23 A VAL   A 1 155 ? 11.723 -6.021  5.250   0.46 18.27 ?  155 VAL   A HG23 1 
ATOM   3271 H HG23 B VAL   A 1 155 ? 12.180 -5.646  5.320   0.24 17.42 ?  155 VAL   A HG23 1 
ATOM   3272 H HG23 T VAL   A 1 155 ? 11.702 -6.012  5.233   0.30 19.56 ?  155 VAL   A HG23 1 
ATOM   3273 N N    A PHE   A 1 156 ? 11.352 -0.884  4.983   0.46 16.04 ?  156 PHE   A N    1 
ATOM   3274 N N    B PHE   A 1 156 ? 11.459 -0.571  5.554   0.24 17.69 ?  156 PHE   A N    1 
ATOM   3275 N N    T PHE   A 1 156 ? 11.436 -0.932  4.845   0.30 15.43 ?  156 PHE   A N    1 
ATOM   3276 C CA   A PHE   A 1 156 ? 10.818 0.426   5.367   0.46 17.88 ?  156 PHE   A CA   1 
ATOM   3277 C CA   B PHE   A 1 156 ? 10.785 0.681   5.902   0.24 18.91 ?  156 PHE   A CA   1 
ATOM   3278 C CA   T PHE   A 1 156 ? 11.003 0.441   5.105   0.30 15.87 ?  156 PHE   A CA   1 
ATOM   3279 C C    A PHE   A 1 156 ? 9.351  0.580   4.983   0.46 18.22 ?  156 PHE   A C    1 
ATOM   3280 C C    B PHE   A 1 156 ? 9.690  1.015   4.884   0.24 19.80 ?  156 PHE   A C    1 
ATOM   3281 C C    T PHE   A 1 156 ? 9.538  0.648   4.743   0.30 16.80 ?  156 PHE   A C    1 
ATOM   3282 O O    A PHE   A 1 156 ? 8.545  1.092   5.772   0.46 19.05 ?  156 PHE   A O    1 
ATOM   3283 O O    B PHE   A 1 156 ? 9.735  2.022   4.178   0.24 19.97 ?  156 PHE   A O    1 
ATOM   3284 O O    T PHE   A 1 156 ? 8.789  1.288   5.493   0.30 17.01 ?  156 PHE   A O    1 
ATOM   3285 C CB   A PHE   A 1 156 ? 11.647 1.542   4.727   0.46 18.79 ?  156 PHE   A CB   1 
ATOM   3286 C CB   B PHE   A 1 156 ? 11.807 1.812   6.003   0.24 19.30 ?  156 PHE   A CB   1 
ATOM   3287 C CB   T PHE   A 1 156 ? 11.885 1.408   4.311   0.30 15.19 ?  156 PHE   A CB   1 
ATOM   3288 C CG   A PHE   A 1 156 ? 11.143 2.931   5.040   0.46 20.10 ?  156 PHE   A CG   1 
ATOM   3289 C CG   B PHE   A 1 156 ? 11.346 2.988   6.824   0.24 19.78 ?  156 PHE   A CG   1 
ATOM   3290 C CG   T PHE   A 1 156 ? 11.554 2.866   4.524   0.30 14.81 ?  156 PHE   A CG   1 
ATOM   3291 C CD1  A PHE   A 1 156 ? 11.068 3.368   6.352   0.46 20.36 ?  156 PHE   A CD1  1 
ATOM   3292 C CD1  B PHE   A 1 156 ? 10.235 2.898   7.650   0.24 19.91 ?  156 PHE   A CD1  1 
ATOM   3293 C CD1  T PHE   A 1 156 ? 11.956 3.519   5.682   0.30 15.24 ?  156 PHE   A CD1  1 
ATOM   3294 C CD2  A PHE   A 1 156 ? 10.760 3.799   4.028   0.46 21.11 ?  156 PHE   A CD2  1 
ATOM   3295 C CD2  B PHE   A 1 156 ? 12.034 4.189   6.769   0.24 20.00 ?  156 PHE   A CD2  1 
ATOM   3296 C CD2  T PHE   A 1 156 ? 10.864 3.588   3.560   0.30 15.11 ?  156 PHE   A CD2  1 
ATOM   3297 C CE1  A PHE   A 1 156 ? 10.612 4.638   6.653   0.46 21.22 ?  156 PHE   A CE1  1 
ATOM   3298 C CE1  B PHE   A 1 156 ? 9.822  3.976   8.400   0.24 20.11 ?  156 PHE   A CE1  1 
ATOM   3299 C CE1  T PHE   A 1 156 ? 11.661 4.856   5.883   0.30 15.70 ?  156 PHE   A CE1  1 
ATOM   3300 C CE2  A PHE   A 1 156 ? 10.300 5.073   4.323   0.46 21.79 ?  156 PHE   A CE2  1 
ATOM   3301 C CE2  B PHE   A 1 156 ? 11.623 5.274   7.518   0.24 20.17 ?  156 PHE   A CE2  1 
ATOM   3302 C CE2  T PHE   A 1 156 ? 10.568 4.927   3.755   0.30 15.69 ?  156 PHE   A CE2  1 
ATOM   3303 C CZ   A PHE   A 1 156 ? 10.230 5.493   5.637   0.46 21.72 ?  156 PHE   A CZ   1 
ATOM   3304 C CZ   B PHE   A 1 156 ? 10.516 5.165   8.336   0.24 20.19 ?  156 PHE   A CZ   1 
ATOM   3305 C CZ   T PHE   A 1 156 ? 10.968 5.561   4.918   0.30 15.83 ?  156 PHE   A CZ   1 
ATOM   3306 H H    A PHE   A 1 156 ? 11.958 -0.863  4.372   0.46 19.25 ?  156 PHE   A H    1 
ATOM   3307 H H    B PHE   A 1 156 ? 12.182 -0.458  5.105   0.24 21.23 ?  156 PHE   A H    1 
ATOM   3308 H H    T PHE   A 1 156 ? 11.983 -1.018  4.186   0.30 18.51 ?  156 PHE   A H    1 
ATOM   3309 H HA   A PHE   A 1 156 ? 10.889 0.520   6.327   0.46 21.46 ?  156 PHE   A HA   1 
ATOM   3310 H HA   B PHE   A 1 156 ? 10.371 0.544   6.768   0.24 22.69 ?  156 PHE   A HA   1 
ATOM   3311 H HA   T PHE   A 1 156 ? 11.115 0.629   6.049   0.30 19.04 ?  156 PHE   A HA   1 
ATOM   3312 H HB2  A PHE   A 1 156 ? 12.563 1.479   5.049   0.46 22.55 ?  156 PHE   A HB2  1 
ATOM   3313 H HB2  B PHE   A 1 156 ? 12.614 1.471   6.416   0.24 23.16 ?  156 PHE   A HB2  1 
ATOM   3314 H HB2  T PHE   A 1 156 ? 12.808 1.270   4.575   0.30 18.23 ?  156 PHE   A HB2  1 
ATOM   3315 H HB3  A PHE   A 1 156 ? 11.633 1.432   3.763   0.46 22.55 ?  156 PHE   A HB3  1 
ATOM   3316 H HB3  B PHE   A 1 156 ? 12.010 2.136   5.109   0.24 23.16 ?  156 PHE   A HB3  1 
ATOM   3317 H HB3  T PHE   A 1 156 ? 11.782 1.215   3.367   0.30 18.23 ?  156 PHE   A HB3  1 
ATOM   3318 H HD1  A PHE   A 1 156 ? 11.327 2.795   7.041   0.46 24.43 ?  156 PHE   A HD1  1 
ATOM   3319 H HD1  B PHE   A 1 156 ? 9.762  2.098   7.701   0.24 23.90 ?  156 PHE   A HD1  1 
ATOM   3320 H HD1  T PHE   A 1 156 ? 12.419 3.046   6.340   0.30 18.29 ?  156 PHE   A HD1  1 
ATOM   3321 H HD2  A PHE   A 1 156 ? 10.808 3.519   3.143   0.46 25.34 ?  156 PHE   A HD2  1 
ATOM   3322 H HD2  B PHE   A 1 156 ? 12.781 4.268   6.220   0.24 24.00 ?  156 PHE   A HD2  1 
ATOM   3323 H HD2  T PHE   A 1 156 ? 10.590 3.161   2.781   0.30 18.13 ?  156 PHE   A HD2  1 
ATOM   3324 H HE1  A PHE   A 1 156 ? 10.567 4.917   7.541   0.46 25.46 ?  156 PHE   A HE1  1 
ATOM   3325 H HE1  B PHE   A 1 156 ? 9.076  3.897   8.949   0.24 24.13 ?  156 PHE   A HE1  1 
ATOM   3326 H HE1  T PHE   A 1 156 ? 11.928 5.278   6.668   0.30 18.84 ?  156 PHE   A HE1  1 
ATOM   3327 H HE2  A PHE   A 1 156 ? 10.046 5.645   3.637   0.46 26.15 ?  156 PHE   A HE2  1 
ATOM   3328 H HE2  B PHE   A 1 156 ? 12.093 6.076   7.473   0.24 24.21 ?  156 PHE   A HE2  1 
ATOM   3329 H HE2  T PHE   A 1 156 ? 10.098 5.397   3.108   0.30 18.83 ?  156 PHE   A HE2  1 
ATOM   3330 H HZ   A PHE   A 1 156 ? 9.924  6.348   5.839   0.46 26.06 ?  156 PHE   A HZ   1 
ATOM   3331 H HZ   B PHE   A 1 156 ? 10.237 5.893   8.842   0.24 24.23 ?  156 PHE   A HZ   1 
ATOM   3332 H HZ   T PHE   A 1 156 ? 10.766 6.458   5.053   0.30 19.00 ?  156 PHE   A HZ   1 
ATOM   3333 N N    A ASP   A 1 157 ? 8.994  0.173   3.773   0.46 17.90 ?  157 ASP   A N    1 
ATOM   3334 N N    B ASP   A 1 157 ? 8.684  0.143   4.828   0.24 20.47 ?  157 ASP   A N    1 
ATOM   3335 N N    T ASP   A 1 157 ? 9.117  0.126   3.599   0.30 17.23 ?  157 ASP   A N    1 
ATOM   3336 C CA   A ASP   A 1 157 ? 7.669  0.444   3.233   0.46 18.94 ?  157 ASP   A CA   1 
ATOM   3337 C CA   B ASP   A 1 157 ? 7.555  0.315   3.919   0.24 21.19 ?  157 ASP   A CA   1 
ATOM   3338 C CA   T ASP   A 1 157 ? 7.802  0.402   3.041   0.30 17.64 ?  157 ASP   A CA   1 
ATOM   3339 C C    A ASP   A 1 157 ? 6.686  -0.610  3.735   0.46 19.50 ?  157 ASP   A C    1 
ATOM   3340 C C    B ASP   A 1 157 ? 6.449  -0.669  4.278   0.24 21.77 ?  157 ASP   A C    1 
ATOM   3341 C C    T ASP   A 1 157 ? 6.790  -0.583  3.617   0.30 18.51 ?  157 ASP   A C    1 
ATOM   3342 O O    A ASP   A 1 157 ? 6.850  -1.805  3.457   0.46 18.57 ?  157 ASP   A O    1 
ATOM   3343 O O    B ASP   A 1 157 ? 6.699  -1.873  4.399   0.24 21.86 ?  157 ASP   A O    1 
ATOM   3344 O O    T ASP   A 1 157 ? 6.922  -1.798  3.429   0.30 18.15 ?  157 ASP   A O    1 
ATOM   3345 C CB   A ASP   A 1 157 ? 7.744  0.444   1.709   0.46 20.04 ?  157 ASP   A CB   1 
ATOM   3346 C CB   B ASP   A 1 157 ? 8.009  0.103   2.473   0.24 21.22 ?  157 ASP   A CB   1 
ATOM   3347 C CB   T ASP   A 1 157 ? 7.881  0.260   1.525   0.30 17.61 ?  157 ASP   A CB   1 
ATOM   3348 C CG   A ASP   A 1 157 ? 6.443  0.862   1.063   0.46 21.44 ?  157 ASP   A CG   1 
ATOM   3349 C CG   B ASP   A 1 157 ? 6.906  0.365   1.463   0.24 21.12 ?  157 ASP   A CG   1 
ATOM   3350 C CG   T ASP   A 1 157 ? 6.730  0.918   0.822   0.30 17.55 ?  157 ASP   A CG   1 
ATOM   3351 O OD1  A ASP   A 1 157 ? 6.048  2.036   1.214   0.46 22.44 ?  157 ASP   A OD1  1 
ATOM   3352 O OD1  B ASP   A 1 157 ? 5.730  0.475   1.867   0.24 20.80 ?  157 ASP   A OD1  1 
ATOM   3353 O OD1  T ASP   A 1 157 ? 5.620  0.351   0.860   0.30 17.91 ?  157 ASP   A OD1  1 
ATOM   3354 O OD2  A ASP   A 1 157 ? 5.813  0.008   0.406   0.46 21.70 -1 157 ASP   A OD2  1 
ATOM   3355 O OD2  B ASP   A 1 157 ? 7.218  0.464   0.257   0.24 21.26 -1 157 ASP   A OD2  1 
ATOM   3356 O OD2  T ASP   A 1 157 ? 6.931  2.007   0.250   0.30 16.95 -1 157 ASP   A OD2  1 
ATOM   3357 H H    A ASP   A 1 157 ? 9.509  -0.267  3.239   0.46 21.48 ?  157 ASP   A H    1 
ATOM   3358 H H    B ASP   A 1 157 ? 8.632  -0.561  5.314   0.24 24.56 ?  157 ASP   A H    1 
ATOM   3359 H H    T ASP   A 1 157 ? 9.591  -0.398  3.109   0.30 20.68 ?  157 ASP   A H    1 
ATOM   3360 H HA   A ASP   A 1 157 ? 7.372  1.318   3.533   0.46 22.73 ?  157 ASP   A HA   1 
ATOM   3361 H HA   B ASP   A 1 157 ? 7.203  1.216   4.002   0.24 25.42 ?  157 ASP   A HA   1 
ATOM   3362 H HA   T ASP   A 1 157 ? 7.529  1.310   3.260   0.30 21.17 ?  157 ASP   A HA   1 
ATOM   3363 H HB2  A ASP   A 1 157 ? 8.463  1.040   1.430   0.46 24.04 ?  157 ASP   A HB2  1 
ATOM   3364 H HB2  B ASP   A 1 157 ? 8.743  0.703   2.285   0.24 25.46 ?  157 ASP   A HB2  1 
ATOM   3365 H HB2  T ASP   A 1 157 ? 8.703  0.661   1.209   0.30 21.13 ?  157 ASP   A HB2  1 
ATOM   3366 H HB3  A ASP   A 1 157 ? 7.923  -0.454  1.401   0.46 24.04 ?  157 ASP   A HB3  1 
ATOM   3367 H HB3  B ASP   A 1 157 ? 8.298  -0.814  2.365   0.24 25.46 ?  157 ASP   A HB3  1 
ATOM   3368 H HB3  T ASP   A 1 157 ? 7.868  -0.682  1.298   0.30 21.13 ?  157 ASP   A HB3  1 
ATOM   3369 N N    A LYS   A 1 158 ? 5.670  -0.169  4.485   0.46 21.28 ?  158 LYS   A N    1 
ATOM   3370 N N    B LYS   A 1 158 ? 5.220  -0.173  4.437   0.24 22.40 ?  158 LYS   A N    1 
ATOM   3371 N N    T LYS   A 1 158 ? 5.778  -0.060  4.318   0.30 20.12 ?  158 LYS   A N    1 
ATOM   3372 C CA   A LYS   A 1 158 ? 4.704  -1.110  5.047   0.46 22.39 ?  158 LYS   A CA   1 
ATOM   3373 C CA   B LYS   A 1 158 ? 4.127  -1.028  4.890   0.24 22.82 ?  158 LYS   A CA   1 
ATOM   3374 C CA   T LYS   A 1 158 ? 4.789  -0.937  4.938   0.30 21.76 ?  158 LYS   A CA   1 
ATOM   3375 C C    A LYS   A 1 158 ? 3.973  -1.868  3.947   0.46 21.83 ?  158 LYS   A C    1 
ATOM   3376 C C    B LYS   A 1 158 ? 3.636  -1.936  3.767   0.24 22.14 ?  158 LYS   A C    1 
ATOM   3377 C C    T LYS   A 1 158 ? 4.028  -1.739  3.890   0.30 21.97 ?  158 LYS   A C    1 
ATOM   3378 O O    A LYS   A 1 158 ? 3.754  -3.081  4.055   0.46 22.10 ?  158 LYS   A O    1 
ATOM   3379 O O    B LYS   A 1 158 ? 3.639  -3.165  3.899   0.24 22.07 ?  158 LYS   A O    1 
ATOM   3380 O O    T LYS   A 1 158 ? 3.782  -2.937  4.072   0.30 22.32 ?  158 LYS   A O    1 
ATOM   3381 C CB   A LYS   A 1 158 ? 3.712  -0.377  5.957   0.46 24.11 ?  158 LYS   A CB   1 
ATOM   3382 C CB   B LYS   A 1 158 ? 2.976  -0.172  5.432   0.24 23.91 ?  158 LYS   A CB   1 
ATOM   3383 C CB   T LYS   A 1 158 ? 3.822  -0.127  5.806   0.30 23.61 ?  158 LYS   A CB   1 
ATOM   3384 C CG   A LYS   A 1 158 ? 2.482  -1.199  6.374   0.46 25.78 ?  158 LYS   A CG   1 
ATOM   3385 C CG   B LYS   A 1 158 ? 2.388  -0.652  6.758   0.24 24.92 ?  158 LYS   A CG   1 
ATOM   3386 C CG   T LYS   A 1 158 ? 2.602  -0.914  6.289   0.30 25.29 ?  158 LYS   A CG   1 
ATOM   3387 C CD   A LYS   A 1 158 ? 2.844  -2.460  7.163   0.46 27.13 ?  158 LYS   A CD   1 
ATOM   3388 C CD   B LYS   A 1 158 ? 2.256  -2.168  6.823   0.24 25.65 ?  158 LYS   A CD   1 
ATOM   3389 C CD   T LYS   A 1 158 ? 2.995  -2.118  7.141   0.30 26.75 ?  158 LYS   A CD   1 
ATOM   3390 C CE   A LYS   A 1 158 ? 1.589  -3.164  7.681   0.46 27.93 ?  158 LYS   A CE   1 
ATOM   3391 C CE   B LYS   A 1 158 ? 1.472  -2.598  8.049   0.24 26.17 ?  158 LYS   A CE   1 
ATOM   3392 C CE   T LYS   A 1 158 ? 1.775  -2.949  7.523   0.30 27.78 ?  158 LYS   A CE   1 
ATOM   3393 N NZ   A LYS   A 1 158 ? 1.877  -4.491  8.300   0.46 28.38 ?  158 LYS   A NZ   1 
ATOM   3394 N NZ   B LYS   A 1 158 ? 1.598  -4.056  8.328   0.24 26.37 ?  158 LYS   A NZ   1 
ATOM   3395 N NZ   T LYS   A 1 158 ? 2.133  -4.148  8.333   0.30 28.32 ?  158 LYS   A NZ   1 
ATOM   3396 H H    A LYS   A 1 158 ? 5.525  0.655   4.679   0.46 25.54 ?  158 LYS   A H    1 
ATOM   3397 H H    B LYS   A 1 158 ? 4.993  0.642   4.284   0.24 26.88 ?  158 LYS   A H    1 
ATOM   3398 H H    T LYS   A 1 158 ? 5.646  0.780   4.446   0.30 24.14 ?  158 LYS   A H    1 
ATOM   3399 H HA   A LYS   A 1 158 ? 5.177  -1.759  5.591   0.46 26.87 ?  158 LYS   A HA   1 
ATOM   3400 H HA   B LYS   A 1 158 ? 4.463  -1.586  5.606   0.24 27.38 ?  158 LYS   A HA   1 
ATOM   3401 H HA   T LYS   A 1 158 ? 5.249  -1.564  5.518   0.30 26.11 ?  158 LYS   A HA   1 
ATOM   3402 H HB2  A LYS   A 1 158 ? 4.174  -0.110  6.770   0.46 28.93 ?  158 LYS   A HB2  1 
ATOM   3403 H HB2  B LYS   A 1 158 ? 3.299  0.732   5.569   0.24 28.69 ?  158 LYS   A HB2  1 
ATOM   3404 H HB2  T LYS   A 1 158 ? 4.296  0.188   6.594   0.30 28.33 ?  158 LYS   A HB2  1 
ATOM   3405 H HB3  A LYS   A 1 158 ? 3.393  0.413   5.495   0.46 28.93 ?  158 LYS   A HB3  1 
ATOM   3406 H HB3  B LYS   A 1 158 ? 2.257  -0.166  4.781   0.24 28.69 ?  158 LYS   A HB3  1 
ATOM   3407 H HB3  T LYS   A 1 158 ? 3.500  0.630   5.295   0.30 28.33 ?  158 LYS   A HB3  1 
ATOM   3408 H HG2  A LYS   A 1 158 ? 1.919  -0.649  6.940   0.46 30.93 ?  158 LYS   A HG2  1 
ATOM   3409 H HG2  B LYS   A 1 158 ? 2.966  -0.367  7.483   0.24 29.91 ?  158 LYS   A HG2  1 
ATOM   3410 H HG2  T LYS   A 1 158 ? 2.050  -0.334  6.834   0.30 30.34 ?  158 LYS   A HG2  1 
ATOM   3411 H HG3  A LYS   A 1 158 ? 1.986  -1.467  5.584   0.46 30.93 ?  158 LYS   A HG3  1 
ATOM   3412 H HG3  B LYS   A 1 158 ? 1.502  -0.270  6.869   0.24 29.91 ?  158 LYS   A HG3  1 
ATOM   3413 H HG3  T LYS   A 1 158 ? 2.091  -1.233  5.528   0.30 30.34 ?  158 LYS   A HG3  1 
ATOM   3414 H HD2  A LYS   A 1 158 ? 3.325  -3.074  6.588   0.46 32.55 ?  158 LYS   A HD2  1 
ATOM   3415 H HD2  B LYS   A 1 158 ? 1.797  -2.484  6.030   0.24 30.78 ?  158 LYS   A HD2  1 
ATOM   3416 H HD2  T LYS   A 1 158 ? 3.602  -2.686  6.642   0.30 32.10 ?  158 LYS   A HD2  1 
ATOM   3417 H HD3  A LYS   A 1 158 ? 3.389  -2.215  7.927   0.46 32.55 ?  158 LYS   A HD3  1 
ATOM   3418 H HD3  B LYS   A 1 158 ? 3.138  -2.569  6.886   0.24 30.78 ?  158 LYS   A HD3  1 
ATOM   3419 H HD3  T LYS   A 1 158 ? 3.419  -1.807  7.957   0.30 32.10 ?  158 LYS   A HD3  1 
ATOM   3420 H HE2  A LYS   A 1 158 ? 1.168  -2.603  8.353   0.46 33.51 ?  158 LYS   A HE2  1 
ATOM   3421 H HE2  B LYS   A 1 158 ? 1.803  -2.114  8.820   0.24 31.40 ?  158 LYS   A HE2  1 
ATOM   3422 H HE2  T LYS   A 1 158 ? 1.168  -2.403  8.046   0.30 33.34 ?  158 LYS   A HE2  1 
ATOM   3423 H HE3  A LYS   A 1 158 ? 0.980  -3.304  6.940   0.46 33.51 ?  158 LYS   A HE3  1 
ATOM   3424 H HE3  B LYS   A 1 158 ? 0.535  -2.399  7.905   0.24 31.40 ?  158 LYS   A HE3  1 
ATOM   3425 H HE3  T LYS   A 1 158 ? 1.333  -3.254  6.714   0.30 33.34 ?  158 LYS   A HE3  1 
ATOM   3426 H HZ1  A LYS   A 1 158 ? 1.121  -4.863  8.586   0.46 34.06 ?  158 LYS   A HZ1  1 
ATOM   3427 H HZ1  B LYS   A 1 158 ? 0.978  -4.507  7.876   0.24 31.64 ?  158 LYS   A HZ1  1 
ATOM   3428 H HZ1  T LYS   A 1 158 ? 1.399  -4.609  8.537   0.30 33.99 ?  158 LYS   A HZ1  1 
ATOM   3429 H HZ2  A LYS   A 1 158 ? 2.256  -5.029  7.701   0.46 34.06 ?  158 LYS   A HZ2  1 
ATOM   3430 H HZ2  B LYS   A 1 158 ? 2.404  -4.347  8.083   0.24 31.64 ?  158 LYS   A HZ2  1 
ATOM   3431 H HZ2  T LYS   A 1 158 ? 2.685  -4.673  7.872   0.30 33.99 ?  158 LYS   A HZ2  1 
ATOM   3432 H HZ3  A LYS   A 1 158 ? 2.430  -4.391  8.990   0.46 34.06 ?  158 LYS   A HZ3  1 
ATOM   3433 H HZ3  B LYS   A 1 158 ? 1.486  -4.209  9.197   0.24 31.64 ?  158 LYS   A HZ3  1 
ATOM   3434 H HZ3  T LYS   A 1 158 ? 2.535  -3.898  9.086   0.30 33.99 ?  158 LYS   A HZ3  1 
ATOM   3435 N N    A ASN   A 1 159 ? 3.587  -1.172  2.878   0.46 21.94 ?  159 ASN   A N    1 
ATOM   3436 N N    B ASN   A 1 159 ? 3.200  -1.342  2.652   0.24 21.80 ?  159 ASN   A N    1 
ATOM   3437 N N    T ASN   A 1 159 ? 3.640  -1.098  2.794   0.30 22.41 ?  159 ASN   A N    1 
ATOM   3438 C CA   A ASN   A 1 159 ? 2.892  -1.846  1.788   0.46 21.76 ?  159 ASN   A CA   1 
ATOM   3439 C CA   B ASN   A 1 159 ? 2.743  -2.143  1.522   0.24 21.38 ?  159 ASN   A CA   1 
ATOM   3440 C CA   T ASN   A 1 159 ? 2.904  -1.786  1.742   0.30 22.71 ?  159 ASN   A CA   1 
ATOM   3441 C C    A ASN   A 1 159 ? 3.763  -2.939  1.172   0.46 20.67 ?  159 ASN   A C    1 
ATOM   3442 C C    B ASN   A 1 159 ? 3.803  -3.141  1.085   0.24 20.65 ?  159 ASN   A C    1 
ATOM   3443 C C    T ASN   A 1 159 ? 3.731  -2.895  1.097   0.30 22.58 ?  159 ASN   A C    1 
ATOM   3444 O O    A ASN   A 1 159 ? 3.303  -4.067  0.958   0.46 20.24 ?  159 ASN   A O    1 
ATOM   3445 O O    B ASN   A 1 159 ? 3.471  -4.238  0.620   0.24 20.85 ?  159 ASN   A O    1 
ATOM   3446 O O    T ASN   A 1 159 ? 3.200  -3.953  0.768   0.30 22.72 ?  159 ASN   A O    1 
ATOM   3447 C CB   A ASN   A 1 159 ? 2.416  -0.822  0.755   0.46 23.53 ?  159 ASN   A CB   1 
ATOM   3448 C CB   B ASN   A 1 159 ? 2.348  -1.238  0.353   0.24 21.77 ?  159 ASN   A CB   1 
ATOM   3449 C CB   T ASN   A 1 159 ? 2.413  -0.792  0.687   0.30 23.61 ?  159 ASN   A CB   1 
ATOM   3450 C CG   A ASN   A 1 159 ? 1.210  -0.028  1.238   0.46 25.42 ?  159 ASN   A CG   1 
ATOM   3451 C CG   B ASN   A 1 159 ? 0.901  -0.792  0.424   0.24 22.16 ?  159 ASN   A CG   1 
ATOM   3452 C CG   T ASN   A 1 159 ? 1.220  0.018   1.163   0.30 24.63 ?  159 ASN   A CG   1 
ATOM   3453 O OD1  A ASN   A 1 159 ? 0.367  -0.553  1.965   0.46 26.53 ?  159 ASN   A OD1  1 
ATOM   3454 O OD1  B ASN   A 1 159 ? 0.356  -0.575  1.506   0.24 22.78 ?  159 ASN   A OD1  1 
ATOM   3455 O OD1  T ASN   A 1 159 ? 0.409  -0.462  1.955   0.30 25.37 ?  159 ASN   A OD1  1 
ATOM   3456 N ND2  A ASN   A 1 159 ? 1.122  1.235   0.837   0.46 26.08 ?  159 ASN   A ND2  1 
ATOM   3457 N ND2  B ASN   A 1 159 ? 0.268  -0.660  -0.734  0.24 22.15 ?  159 ASN   A ND2  1 
ATOM   3458 N ND2  T ASN   A 1 159 ? 1.106  1.248   0.683   0.30 24.93 ?  159 ASN   A ND2  1 
ATOM   3459 H H    A ASN   A 1 159 ? 3.716  -0.328  2.765   0.46 26.33 ?  159 ASN   A H    1 
ATOM   3460 H H    B ASN   A 1 159 ? 3.164  -0.492  2.532   0.24 26.17 ?  159 ASN   A H    1 
ATOM   3461 H H    T ASN   A 1 159 ? 3.784  -0.266  2.643   0.30 26.89 ?  159 ASN   A H    1 
ATOM   3462 H HA   A ASN   A 1 159 ? 2.102  -2.276  2.151   0.46 26.11 ?  159 ASN   A HA   1 
ATOM   3463 H HA   B ASN   A 1 159 ? 1.959  -2.643  1.787   0.24 25.65 ?  159 ASN   A HA   1 
ATOM   3464 H HA   T ASN   A 1 159 ? 2.127  -2.206  2.136   0.30 27.25 ?  159 ASN   A HA   1 
ATOM   3465 H HB2  A ASN   A 1 159 ? 3.128  -0.192  0.575   0.46 28.24 ?  159 ASN   A HB2  1 
ATOM   3466 H HB2  B ASN   A 1 159 ? 2.907  -0.444  0.361   0.24 26.13 ?  159 ASN   A HB2  1 
ATOM   3467 H HB2  T ASN   A 1 159 ? 3.128  -0.175  0.474   0.30 28.34 ?  159 ASN   A HB2  1 
ATOM   3468 H HB3  A ASN   A 1 159 ? 2.162  -1.284  -0.058  0.46 28.24 ?  159 ASN   A HB3  1 
ATOM   3469 H HB3  B ASN   A 1 159 ? 2.469  -1.721  -0.478  0.24 26.13 ?  159 ASN   A HB3  1 
ATOM   3470 H HB3  T ASN   A 1 159 ? 2.149  -1.284  -0.109  0.30 28.34 ?  159 ASN   A HB3  1 
ATOM   3471 H HD21 A ASN   A 1 159 ? 0.456  1.721   1.085   0.46 31.29 ?  159 ASN   A HD21 1 
ATOM   3472 H HD21 B ASN   A 1 159 ? -0.554 -0.411  -0.747  0.24 26.59 ?  159 ASN   A HD21 1 
ATOM   3473 H HD21 T ASN   A 1 159 ? 0.444  1.741   0.924   0.30 29.91 ?  159 ASN   A HD21 1 
ATOM   3474 H HD22 A ASN   A 1 159 ? 1.733  1.567   0.334   0.46 31.29 ?  159 ASN   A HD22 1 
ATOM   3475 H HD22 B ASN   A 1 159 ? 0.681  -0.823  -1.470  0.24 26.59 ?  159 ASN   A HD22 1 
ATOM   3476 H HD22 T ASN   A 1 159 ? 1.693  1.550   0.135   0.30 29.91 ?  159 ASN   A HD22 1 
ATOM   3477 N N    A LEU   A 1 160 ? 5.039  -2.637  0.916   0.46 19.31 ?  160 LEU   A N    1 
ATOM   3478 N N    B LEU   A 1 160 ? 5.079  -2.787  1.235   0.24 19.60 ?  160 LEU   A N    1 
ATOM   3479 N N    T LEU   A 1 160 ? 5.028  -2.661  0.926   0.30 22.13 ?  160 LEU   A N    1 
ATOM   3480 C CA   A LEU   A 1 160 ? 5.928  -3.657  0.366   0.46 17.88 ?  160 LEU   A CA   1 
ATOM   3481 C CA   B LEU   A 1 160 ? 6.142  -3.712  0.868   0.24 18.14 ?  160 LEU   A CA   1 
ATOM   3482 C CA   T LEU   A 1 160 ? 5.902  -3.678  0.354   0.30 21.56 ?  160 LEU   A CA   1 
ATOM   3483 C C    A LEU   A 1 160 ? 6.113  -4.812  1.342   0.46 16.17 ?  160 LEU   A C    1 
ATOM   3484 C C    B LEU   A 1 160 ? 6.276  -4.828  1.896   0.24 16.65 ?  160 LEU   A C    1 
ATOM   3485 O O    A LEU   A 1 160 ? 6.144  -5.981  0.938   0.46 15.55 ?  160 LEU   A O    1 
ATOM   3486 O O    B LEU   A 1 160 ? 6.286  -6.013  1.540   0.24 15.98 ?  160 LEU   A O    1 
ATOM   3487 C CB   A LEU   A 1 160 ? 7.278  -3.040  0.013   0.46 17.78 ?  160 LEU   A CB   1 
ATOM   3488 C CB   B LEU   A 1 160 ? 7.465  -2.962  0.710   0.24 18.15 ?  160 LEU   A CB   1 
ATOM   3489 C CB   T LEU   A 1 160 ? 7.287  -3.103  0.062   0.30 20.96 ?  160 LEU   A CB   1 
ATOM   3490 C CG   A LEU   A 1 160 ? 8.337  -4.061  -0.396  0.46 18.86 ?  160 LEU   A CG   1 
ATOM   3491 C CG   B LEU   A 1 160 ? 8.617  -3.834  0.215   0.24 18.26 ?  160 LEU   A CG   1 
ATOM   3492 C CG   T LEU   A 1 160 ? 8.335  -4.131  -0.363  0.30 20.88 ?  160 LEU   A CG   1 
ATOM   3493 C CD1  A LEU   A 1 160 ? 7.854  -4.866  -1.589  0.46 19.48 ?  160 LEU   A CD1  1 
ATOM   3494 C CD1  B LEU   A 1 160 ? 8.192  -4.579  -1.037  0.24 18.39 ?  160 LEU   A CD1  1 
ATOM   3495 C CD1  T LEU   A 1 160 ? 7.876  -4.890  -1.593  0.30 21.03 ?  160 LEU   A CD1  1 
ATOM   3496 C CD2  A LEU   A 1 160 ? 9.645  -3.368  -0.705  0.46 19.11 ?  160 LEU   A CD2  1 
ATOM   3497 C CD2  B LEU   A 1 160 ? 9.854  -2.994  -0.050  0.24 18.12 ?  160 LEU   A CD2  1 
ATOM   3498 C CD2  T LEU   A 1 160 ? 9.668  -3.454  -0.616  0.30 20.73 ?  160 LEU   A CD2  1 
ATOM   3499 H H    A LEU   A 1 160 ? 5.406  -1.870  1.060   0.46 23.17 ?  160 LEU   A H    1 
ATOM   3500 H H    B LEU   A 1 160 ? 5.349  -2.030  1.539   0.24 23.52 ?  160 LEU   A H    1 
ATOM   3501 H H    T LEU   A 1 160 ? 5.427  -1.927  1.135   0.30 26.56 ?  160 LEU   A H    1 
ATOM   3502 H HA   A LEU   A 1 160 ? 5.532  -4.004  -0.446  0.46 21.46 ?  160 LEU   A HA   1 
ATOM   3503 H HA   B LEU   A 1 160 ? 5.911  -4.114  0.021   0.24 21.77 ?  160 LEU   A HA   1 
ATOM   3504 H HB2  A LEU   A 1 160 ? 7.157  -2.423  -0.727  0.46 21.33 ?  160 LEU   A HB2  1 
ATOM   3505 H HB2  B LEU   A 1 160 ? 7.349  -2.230  0.082   0.24 21.78 ?  160 LEU   A HB2  1 
ATOM   3506 H HB2  T LEU   A 1 160 ? 7.206  -2.444  -0.649  0.30 25.15 ?  160 LEU   A HB2  1 
ATOM   3507 H HB3  A LEU   A 1 160 ? 7.613  -2.561  0.787   0.46 21.33 ?  160 LEU   A HB3  1 
ATOM   3508 H HB3  B LEU   A 1 160 ? 7.722  -2.618  1.577   0.24 21.78 ?  160 LEU   A HB3  1 
ATOM   3509 H HB3  T LEU   A 1 160 ? 7.622  -2.679  0.866   0.30 25.15 ?  160 LEU   A HB3  1 
ATOM   3510 H HG   A LEU   A 1 160 ? 8.496  -4.674  0.338   0.46 22.64 ?  160 LEU   A HG   1 
ATOM   3511 H HG   B LEU   A 1 160 ? 8.840  -4.488  0.897   0.24 21.91 ?  160 LEU   A HG   1 
ATOM   3512 H HG   T LEU   A 1 160 ? 8.457  -4.770  0.358   0.30 25.05 ?  160 LEU   A HG   1 
ATOM   3513 H HD11 A LEU   A 1 160 ? 8.576  -5.431  -1.896  0.46 23.37 ?  160 LEU   A HD11 1 
ATOM   3514 H HD11 B LEU   A 1 160 ? 8.976  -4.949  -1.459  0.24 22.07 ?  160 LEU   A HD11 1 
ATOM   3515 H HD11 T LEU   A 1 160 ? 8.602  -5.452  -1.904  0.30 25.24 ?  160 LEU   A HD11 1 
ATOM   3516 H HD12 A LEU   A 1 160 ? 7.098  -5.412  -1.320  0.46 23.37 ?  160 LEU   A HD12 1 
ATOM   3517 H HD12 B LEU   A 1 160 ? 7.583  -5.293  -0.790  0.24 22.07 ?  160 LEU   A HD12 1 
ATOM   3518 H HD12 T LEU   A 1 160 ? 7.110  -5.437  -1.359  0.30 25.24 ?  160 LEU   A HD12 1 
ATOM   3519 H HD13 A LEU   A 1 160 ? 7.586  -4.254  -2.293  0.46 23.37 ?  160 LEU   A HD13 1 
ATOM   3520 H HD13 B LEU   A 1 160 ? 7.749  -3.957  -1.638  0.24 22.07 ?  160 LEU   A HD13 1 
ATOM   3521 H HD13 T LEU   A 1 160 ? 7.632  -4.252  -2.282  0.30 25.24 ?  160 LEU   A HD13 1 
ATOM   3522 H HD21 A LEU   A 1 160 ? 10.302 -4.034  -0.961  0.46 22.93 ?  160 LEU   A HD21 1 
ATOM   3523 H HD21 B LEU   A 1 160 ? 10.570 -3.572  -0.358  0.24 21.75 ?  160 LEU   A HD21 1 
ATOM   3524 H HD21 T LEU   A 1 160 ? 10.317 -4.124  -0.881  0.30 24.87 ?  160 LEU   A HD21 1 
ATOM   3525 H HD22 A LEU   A 1 160 ? 9.508  -2.742  -1.434  0.46 22.93 ?  160 LEU   A HD22 1 
ATOM   3526 H HD22 B LEU   A 1 160 ? 9.647  -2.334  -0.731  0.24 21.75 ?  160 LEU   A HD22 1 
ATOM   3527 H HD22 T LEU   A 1 160 ? 9.559  -2.799  -1.324  0.30 24.87 ?  160 LEU   A HD22 1 
ATOM   3528 H HD23 A LEU   A 1 160 ? 9.947  -2.893  0.086   0.46 22.93 ?  160 LEU   A HD23 1 
ATOM   3529 H HD23 B LEU   A 1 160 ? 10.118 -2.549  0.771   0.24 21.75 ?  160 LEU   A HD23 1 
ATOM   3530 H HD23 T LEU   A 1 160 ? 9.959  -3.014  0.198   0.30 24.87 ?  160 LEU   A HD23 1 
ATOM   3531 N N    A TYR   A 1 161 ? 6.250  -4.504  2.632   0.76 16.85 ?  161 TYR   A N    1 
ATOM   3532 N N    B TYR   A 1 161 ? 6.377  -4.470  3.179   0.24 16.41 ?  161 TYR   A N    1 
ATOM   3533 C CA   A TYR   A 1 161 ? 6.380  -5.551  3.639   0.76 16.46 ?  161 TYR   A CA   1 
ATOM   3534 C CA   B TYR   A 1 161 ? 6.526  -5.484  4.219   0.24 16.37 ?  161 TYR   A CA   1 
ATOM   3535 C C    A TYR   A 1 161 ? 5.228  -6.548  3.560   0.76 17.36 ?  161 TYR   A C    1 
ATOM   3536 C C    B TYR   A 1 161 ? 5.358  -6.464  4.200   0.24 16.79 ?  161 TYR   A C    1 
ATOM   3537 O O    A TYR   A 1 161 ? 5.444  -7.765  3.570   0.76 16.75 ?  161 TYR   A O    1 
ATOM   3538 O O    B TYR   A 1 161 ? 5.556  -7.685  4.191   0.24 16.55 ?  161 TYR   A O    1 
ATOM   3539 C CB   A TYR   A 1 161 ? 6.459  -4.929  5.033   0.76 16.10 ?  161 TYR   A CB   1 
ATOM   3540 C CB   B TYR   A 1 161 ? 6.667  -4.822  5.591   0.24 16.11 ?  161 TYR   A CB   1 
ATOM   3541 C CG   A TYR   A 1 161 ? 6.378  -5.952  6.134   0.76 15.76 ?  161 TYR   A CG   1 
ATOM   3542 C CG   B TYR   A 1 161 ? 6.522  -5.789  6.745   0.24 15.97 ?  161 TYR   A CG   1 
ATOM   3543 C CD1  A TYR   A 1 161 ? 7.511  -6.637  6.551   0.76 15.56 ?  161 TYR   A CD1  1 
ATOM   3544 C CD1  B TYR   A 1 161 ? 7.609  -6.518  7.208   0.24 15.82 ?  161 TYR   A CD1  1 
ATOM   3545 C CD2  A TYR   A 1 161 ? 5.165  -6.245  6.754   0.76 15.77 ?  161 TYR   A CD2  1 
ATOM   3546 C CD2  B TYR   A 1 161 ? 5.297  -5.968  7.375   0.24 16.12 ?  161 TYR   A CD2  1 
ATOM   3547 C CE1  A TYR   A 1 161 ? 7.441  -7.590  7.549   0.76 15.20 ?  161 TYR   A CE1  1 
ATOM   3548 C CE1  B TYR   A 1 161 ? 7.479  -7.404  8.262   0.24 16.24 ?  161 TYR   A CE1  1 
ATOM   3549 C CE2  A TYR   A 1 161 ? 5.088  -7.195  7.752   0.76 15.41 ?  161 TYR   A CE2  1 
ATOM   3550 C CE2  B TYR   A 1 161 ? 5.157  -6.848  8.428   0.24 16.53 ?  161 TYR   A CE2  1 
ATOM   3551 C CZ   A TYR   A 1 161 ? 6.226  -7.868  8.145   0.76 15.37 ?  161 TYR   A CZ   1 
ATOM   3552 C CZ   B TYR   A 1 161 ? 6.249  -7.564  8.869   0.24 16.81 ?  161 TYR   A CZ   1 
ATOM   3553 O OH   A TYR   A 1 161 ? 6.166  -8.817  9.139   0.76 15.93 ?  161 TYR   A OH   1 
ATOM   3554 O OH   B TYR   A 1 161 ? 6.101  -8.439  9.921   0.24 17.62 ?  161 TYR   A OH   1 
ATOM   3555 H H    A TYR   A 1 161 ? 6.257  -3.706  2.946   0.76 20.22 ?  161 TYR   A H    1 
ATOM   3556 H H    B TYR   A 1 161 ? 6.354  -3.659  3.470   0.24 19.70 ?  161 TYR   A H    1 
ATOM   3557 H HA   A TYR   A 1 161 ? 7.198  -6.039  3.480   0.76 19.75 ?  161 TYR   A HA   1 
ATOM   3558 H HA   B TYR   A 1 161 ? 7.335  -5.986  4.053   0.24 19.64 ?  161 TYR   A HA   1 
ATOM   3559 H HB2  A TYR   A 1 161 ? 7.305  -4.464  5.119   0.76 19.32 ?  161 TYR   A HB2  1 
ATOM   3560 H HB2  B TYR   A 1 161 ? 7.546  -4.414  5.656   0.24 19.33 ?  161 TYR   A HB2  1 
ATOM   3561 H HB3  A TYR   A 1 161 ? 5.724  -4.308  5.146   0.76 19.32 ?  161 TYR   A HB3  1 
ATOM   3562 H HB3  B TYR   A 1 161 ? 5.983  -4.141  5.688   0.24 19.33 ?  161 TYR   A HB3  1 
ATOM   3563 H HD1  A TYR   A 1 161 ? 8.328  -6.458  6.144   0.76 18.67 ?  161 TYR   A HD1  1 
ATOM   3564 H HD1  B TYR   A 1 161 ? 8.439  -6.411  6.803   0.24 18.98 ?  161 TYR   A HD1  1 
ATOM   3565 H HD2  A TYR   A 1 161 ? 4.391  -5.802  6.489   0.76 18.93 ?  161 TYR   A HD2  1 
ATOM   3566 H HD2  B TYR   A 1 161 ? 4.556  -5.487  7.083   0.24 19.35 ?  161 TYR   A HD2  1 
ATOM   3567 H HE1  A TYR   A 1 161 ? 8.210  -8.041  7.815   0.76 18.24 ?  161 TYR   A HE1  1 
ATOM   3568 H HE1  B TYR   A 1 161 ? 8.215  -7.887  8.563   0.24 19.49 ?  161 TYR   A HE1  1 
ATOM   3569 H HE2  A TYR   A 1 161 ? 4.268  -7.383  8.157   0.76 18.49 ?  161 TYR   A HE2  1 
ATOM   3570 H HE2  B TYR   A 1 161 ? 4.329  -6.958  8.839   0.24 19.84 ?  161 TYR   A HE2  1 
ATOM   3571 H HH   A TYR   A 1 161 ? 6.925  -9.143  9.280   0.76 19.12 ?  161 TYR   A HH   1 
ATOM   3572 H HH   B TYR   A 1 161 ? 5.301  -8.433  10.186  0.24 21.14 ?  161 TYR   A HH   1 
ATOM   3573 N N    A ASP   A 1 162 ? 3.992  -6.047  3.485   0.76 18.12 ?  162 ASP   A N    1 
ATOM   3574 N N    B ASP   A 1 162 ? 4.127  -5.946  4.192   0.24 17.45 ?  162 ASP   A N    1 
ATOM   3575 C CA   A ASP   A 1 162 ? 2.839  -6.942  3.424   0.76 18.56 ?  162 ASP   A CA   1 
ATOM   3576 C CA   B ASP   A 1 162 ? 2.965  -6.828  4.147   0.24 18.42 ?  162 ASP   A CA   1 
ATOM   3577 C C    A ASP   A 1 162 ? 2.883  -7.806  2.171   0.76 18.50 ?  162 ASP   A C    1 
ATOM   3578 C C    B ASP   A 1 162 ? 2.980  -7.695  2.897   0.24 18.70 ?  162 ASP   A C    1 
ATOM   3579 O O    A ASP   A 1 162 ? 2.529  -8.990  2.210   0.76 18.80 ?  162 ASP   A O    1 
ATOM   3580 O O    B ASP   A 1 162 ? 2.548  -8.853  2.935   0.24 18.47 ?  162 ASP   A O    1 
ATOM   3581 C CB   A ASP   A 1 162 ? 1.532  -6.145  3.471   0.76 19.98 ?  162 ASP   A CB   1 
ATOM   3582 C CB   B ASP   A 1 162 ? 1.676  -6.007  4.204   0.24 19.05 ?  162 ASP   A CB   1 
ATOM   3583 C CG   A ASP   A 1 162 ? 1.249  -5.547  4.831   0.76 22.05 ?  162 ASP   A CG   1 
ATOM   3584 C CG   B ASP   A 1 162 ? 1.484  -5.317  5.540   0.24 20.06 ?  162 ASP   A CG   1 
ATOM   3585 O OD1  A ASP   A 1 162 ? 1.860  -5.983  5.827   0.76 22.61 ?  162 ASP   A OD1  1 
ATOM   3586 O OD1  B ASP   A 1 162 ? 2.281  -5.576  6.466   0.24 20.49 ?  162 ASP   A OD1  1 
ATOM   3587 O OD2  A ASP   A 1 162 ? 0.373  -4.656  4.902   0.76 23.33 -1 162 ASP   A OD2  1 
ATOM   3588 O OD2  B ASP   A 1 162 ? 0.537  -4.514  5.666   0.24 20.49 -1 162 ASP   A OD2  1 
ATOM   3589 H H    A ASP   A 1 162 ? 3.794  -5.210  3.469   0.76 21.75 ?  162 ASP   A H    1 
ATOM   3590 H H    B ASP   A 1 162 ? 3.944  -5.105  4.207   0.24 20.94 ?  162 ASP   A H    1 
ATOM   3591 H HA   A ASP   A 1 162 ? 2.852  -7.534  4.187   0.76 22.27 ?  162 ASP   A HA   1 
ATOM   3592 H HA   B ASP   A 1 162 ? 2.979  -7.409  4.922   0.24 22.10 ?  162 ASP   A HA   1 
ATOM   3593 H HB2  A ASP   A 1 162 ? 1.574  -5.417  2.839   0.76 23.98 ?  162 ASP   A HB2  1 
ATOM   3594 H HB2  B ASP   A 1 162 ? 1.703  -5.320  3.522   0.24 22.86 ?  162 ASP   A HB2  1 
ATOM   3595 H HB3  A ASP   A 1 162 ? 0.789  -6.731  3.264   0.76 23.98 ?  162 ASP   A HB3  1 
ATOM   3596 H HB3  B ASP   A 1 162 ? 0.917  -6.596  4.051   0.24 22.86 ?  162 ASP   A HB3  1 
ATOM   3597 N N    A LYS   A 1 163 ? 3.315  -7.232  1.048   0.76 19.74 ?  163 LYS   A N    1 
ATOM   3598 N N    B LYS   A 1 163 ? 3.480  -7.157  1.785   0.24 19.29 ?  163 LYS   A N    1 
ATOM   3599 C CA   A LYS   A 1 163 ? 3.416  -8.014  -0.178  0.76 20.49 ?  163 LYS   A CA   1 
ATOM   3600 C CA   B LYS   A 1 163 ? 3.521  -7.924  0.546   0.24 20.04 ?  163 LYS   A CA   1 
ATOM   3601 C C    A LYS   A 1 163 ? 4.506  -9.073  -0.063  0.76 19.66 ?  163 LYS   A C    1 
ATOM   3602 C C    B LYS   A 1 163 ? 4.611  -8.987  0.587   0.24 19.09 ?  163 LYS   A C    1 
ATOM   3603 O O    A LYS   A 1 163 ? 4.345  -10.194 -0.555  0.76 20.39 ?  163 LYS   A O    1 
ATOM   3604 O O    B LYS   A 1 163 ? 4.420  -10.099 0.082   0.24 19.00 ?  163 LYS   A O    1 
ATOM   3605 C CB   A LYS   A 1 163 ? 3.680  -7.086  -1.364  0.76 23.56 ?  163 LYS   A CB   1 
ATOM   3606 C CB   B LYS   A 1 163 ? 3.737  -6.972  -0.627  0.24 21.73 ?  163 LYS   A CB   1 
ATOM   3607 C CG   A LYS   A 1 163 ? 3.723  -7.793  -2.704  0.76 27.16 ?  163 LYS   A CG   1 
ATOM   3608 C CG   B LYS   A 1 163 ? 3.929  -7.637  -1.969  0.24 23.37 ?  163 LYS   A CG   1 
ATOM   3609 C CD   A LYS   A 1 163 ? 4.144  -6.841  -3.806  0.76 30.33 ?  163 LYS   A CD   1 
ATOM   3610 C CD   B LYS   A 1 163 ? 4.277  -6.584  -2.999  0.24 24.86 ?  163 LYS   A CD   1 
ATOM   3611 C CE   A LYS   A 1 163 ? 4.091  -7.513  -5.165  0.76 32.51 ?  163 LYS   A CE   1 
ATOM   3612 C CE   B LYS   A 1 163 ? 3.927  -7.028  -4.403  0.24 25.89 ?  163 LYS   A CE   1 
ATOM   3613 N NZ   A LYS   A 1 163 ? 4.778  -6.706  -6.209  0.76 33.79 ?  163 LYS   A NZ   1 
ATOM   3614 N NZ   B LYS   A 1 163 ? 4.021  -5.897  -5.368  0.24 26.39 ?  163 LYS   A NZ   1 
ATOM   3615 H H    A LYS   A 1 163 ? 3.551  -6.405  0.970   0.76 23.69 ?  163 LYS   A H    1 
ATOM   3616 H H    B LYS   A 1 163 ? 3.800  -6.358  1.726   0.24 23.15 ?  163 LYS   A H    1 
ATOM   3617 H HA   A LYS   A 1 163 ? 2.570  -8.463  -0.337  0.76 24.58 ?  163 LYS   A HA   1 
ATOM   3618 H HA   B LYS   A 1 163 ? 2.670  -8.370  0.423   0.24 24.04 ?  163 LYS   A HA   1 
ATOM   3619 H HB2  A LYS   A 1 163 ? 2.970  -6.421  -1.407  0.76 28.28 ?  163 LYS   A HB2  1 
ATOM   3620 H HB2  B LYS   A 1 163 ? 2.960  -6.395  -0.700  0.24 26.08 ?  163 LYS   A HB2  1 
ATOM   3621 H HB3  A LYS   A 1 163 ? 4.532  -6.645  -1.235  0.76 28.28 ?  163 LYS   A HB3  1 
ATOM   3622 H HB3  B LYS   A 1 163 ? 4.524  -6.437  -0.452  0.24 26.08 ?  163 LYS   A HB3  1 
ATOM   3623 H HG2  A LYS   A 1 163 ? 4.367  -8.518  -2.668  0.76 32.59 ?  163 LYS   A HG2  1 
ATOM   3624 H HG2  B LYS   A 1 163 ? 4.660  -8.275  -1.921  0.24 28.04 ?  163 LYS   A HG2  1 
ATOM   3625 H HG3  A LYS   A 1 163 ? 2.841  -8.137  -2.916  0.76 32.59 ?  163 LYS   A HG3  1 
ATOM   3626 H HG3  B LYS   A 1 163 ? 3.107  -8.080  -2.233  0.24 28.04 ?  163 LYS   A HG3  1 
ATOM   3627 H HD2  A LYS   A 1 163 ? 3.542  -6.080  -3.818  0.76 36.40 ?  163 LYS   A HD2  1 
ATOM   3628 H HD2  B LYS   A 1 163 ? 3.781  -5.773  -2.802  0.24 29.83 ?  163 LYS   A HD2  1 
ATOM   3629 H HD3  A LYS   A 1 163 ? 5.054  -6.546  -3.643  0.76 36.40 ?  163 LYS   A HD3  1 
ATOM   3630 H HD3  B LYS   A 1 163 ? 5.231  -6.408  -2.961  0.24 29.83 ?  163 LYS   A HD3  1 
ATOM   3631 H HE2  A LYS   A 1 163 ? 4.519  -8.381  -5.110  0.76 39.02 ?  163 LYS   A HE2  1 
ATOM   3632 H HE2  B LYS   A 1 163 ? 4.543  -7.722  -4.682  0.24 31.07 ?  163 LYS   A HE2  1 
ATOM   3633 H HE3  A LYS   A 1 163 ? 3.165  -7.618  -5.428  0.76 39.02 ?  163 LYS   A HE3  1 
ATOM   3634 H HE3  B LYS   A 1 163 ? 3.019  -7.364  -4.413  0.24 31.07 ?  163 LYS   A HE3  1 
ATOM   3635 H HZ1  A LYS   A 1 163 ? 4.733  -7.122  -6.994  0.76 40.54 ?  163 LYS   A HZ1  1 
ATOM   3636 H HZ1  B LYS   A 1 163 ? 3.812  -6.178  -6.185  0.24 31.67 ?  163 LYS   A HZ1  1 
ATOM   3637 H HZ2  A LYS   A 1 163 ? 4.387  -5.909  -6.282  0.76 40.54 ?  163 LYS   A HZ2  1 
ATOM   3638 H HZ2  B LYS   A 1 163 ? 3.456  -5.250  -5.131  0.24 31.67 ?  163 LYS   A HZ2  1 
ATOM   3639 H HZ3  A LYS   A 1 163 ? 5.633  -6.589  -5.991  0.76 40.54 ?  163 LYS   A HZ3  1 
ATOM   3640 H HZ3  B LYS   A 1 163 ? 4.848  -5.570  -5.375  0.24 31.67 ?  163 LYS   A HZ3  1 
ATOM   3641 N N    A LEU   A 1 164 ? 5.626  -8.729  0.576   0.76 17.73 ?  164 LEU   A N    1 
ATOM   3642 N N    B LEU   A 1 164 ? 5.762  -8.664  1.181   0.24 18.41 ?  164 LEU   A N    1 
ATOM   3643 C CA   A LEU   A 1 164 ? 6.706  -9.694  0.760   0.76 17.13 ?  164 LEU   A CA   1 
ATOM   3644 C CA   B LEU   A 1 164 ? 6.857  -9.628  1.248   0.24 17.75 ?  164 LEU   A CA   1 
ATOM   3645 C C    A LEU   A 1 164 ? 6.257  -10.860 1.632   0.76 17.37 ?  164 LEU   A C    1 
ATOM   3646 C C    B LEU   A 1 164 ? 6.461  -10.853 2.061   0.24 17.75 ?  164 LEU   A C    1 
ATOM   3647 O O    A LEU   A 1 164 ? 6.537  -12.024 1.323   0.76 17.88 ?  164 LEU   A O    1 
ATOM   3648 O O    B LEU   A 1 164 ? 6.844  -11.981 1.726   0.24 17.66 ?  164 LEU   A O    1 
ATOM   3649 C CB   A LEU   A 1 164 ? 7.912  -8.998  1.387   0.76 16.64 ?  164 LEU   A CB   1 
ATOM   3650 C CB   B LEU   A 1 164 ? 8.095  -8.965  1.851   0.24 17.06 ?  164 LEU   A CB   1 
ATOM   3651 C CG   A LEU   A 1 164 ? 8.685  -8.043  0.477   0.76 16.79 ?  164 LEU   A CG   1 
ATOM   3652 C CG   B LEU   A 1 164 ? 8.852  -7.963  0.978   0.24 16.81 ?  164 LEU   A CG   1 
ATOM   3653 C CD1  A LEU   A 1 164 ? 9.612  -7.167  1.304   0.76 16.45 ?  164 LEU   A CD1  1 
ATOM   3654 C CD1  B LEU   A 1 164 ? 9.764  -7.111  1.843   0.24 16.72 ?  164 LEU   A CD1  1 
ATOM   3655 C CD2  A LEU   A 1 164 ? 9.475  -8.802  -0.579  0.76 17.33 ?  164 LEU   A CD2  1 
ATOM   3656 C CD2  B LEU   A 1 164 ? 9.654  -8.681  -0.097  0.24 16.53 ?  164 LEU   A CD2  1 
ATOM   3657 H H    A LEU   A 1 164 ? 5.782  -7.946  0.901   0.76 21.28 ?  164 LEU   A H    1 
ATOM   3658 H H    B LEU   A 1 164 ? 5.929  -7.907  1.551   0.24 22.09 ?  164 LEU   A H    1 
ATOM   3659 H HA   A LEU   A 1 164 ? 6.971  -10.041 -0.107  0.76 20.55 ?  164 LEU   A HA   1 
ATOM   3660 H HA   B LEU   A 1 164 ? 7.078  -9.926  0.355   0.24 21.30 ?  164 LEU   A HA   1 
ATOM   3661 H HB2  A LEU   A 1 164 ? 7.603  -8.483  2.147   0.76 19.97 ?  164 LEU   A HB2  1 
ATOM   3662 H HB2  B LEU   A 1 164 ? 7.824  -8.492  2.652   0.24 20.47 ?  164 LEU   A HB2  1 
ATOM   3663 H HB3  A LEU   A 1 164 ? 8.532  -9.678  1.684   0.76 19.97 ?  164 LEU   A HB3  1 
ATOM   3664 H HB3  B LEU   A 1 164 ? 8.725  -9.661  2.089   0.24 20.47 ?  164 LEU   A HB3  1 
ATOM   3665 H HG   A LEU   A 1 164 ? 8.056  -7.462  0.020   0.76 20.15 ?  164 LEU   A HG   1 
ATOM   3666 H HG   B LEU   A 1 164 ? 8.217  -7.374  0.540   0.24 20.17 ?  164 LEU   A HG   1 
ATOM   3667 H HD11 A LEU   A 1 164 ? 10.097 -6.572  0.712   0.76 19.74 ?  164 LEU   A HD11 1 
ATOM   3668 H HD11 B LEU   A 1 164 ? 10.250 -6.492  1.277   0.24 20.07 ?  164 LEU   A HD11 1 
ATOM   3669 H HD12 A LEU   A 1 164 ? 9.082  -6.650  1.931   0.76 19.74 ?  164 LEU   A HD12 1 
ATOM   3670 H HD12 B LEU   A 1 164 ? 9.223  -6.620  2.483   0.24 20.07 ?  164 LEU   A HD12 1 
ATOM   3671 H HD13 A LEU   A 1 164 ? 10.234 -7.734  1.787   0.76 19.74 ?  164 LEU   A HD13 1 
ATOM   3672 H HD13 B LEU   A 1 164 ? 10.385 -7.690  2.312   0.24 20.07 ?  164 LEU   A HD13 1 
ATOM   3673 H HD21 A LEU   A 1 164 ? 9.993  -8.168  -1.101  0.76 20.80 ?  164 LEU   A HD21 1 
ATOM   3674 H HD21 B LEU   A 1 164 ? 10.132 -8.023  -0.627  0.24 19.83 ?  164 LEU   A HD21 1 
ATOM   3675 H HD22 A LEU   A 1 164 ? 10.066 -9.431  -0.140  0.76 20.80 ?  164 LEU   A HD22 1 
ATOM   3676 H HD22 B LEU   A 1 164 ? 10.283 -9.284  0.328   0.24 19.83 ?  164 LEU   A HD22 1 
ATOM   3677 H HD23 A LEU   A 1 164 ? 8.855  -9.276  -1.157  0.76 20.80 ?  164 LEU   A HD23 1 
ATOM   3678 H HD23 B LEU   A 1 164 ? 9.045  -9.181  -0.663  0.24 19.83 ?  164 LEU   A HD23 1 
ATOM   3679 N N    A VAL   A 1 165 ? 5.574  -10.560 2.738   0.76 16.98 ?  165 VAL   A N    1 
ATOM   3680 N N    B VAL   A 1 165 ? 5.699  -10.651 3.135   0.24 17.74 ?  165 VAL   A N    1 
ATOM   3681 C CA   A VAL   A 1 165 ? 5.076  -11.613 3.621   0.76 16.74 ?  165 VAL   A CA   1 
ATOM   3682 C CA   B VAL   A 1 165 ? 5.272  -11.775 3.961   0.24 17.98 ?  165 VAL   A CA   1 
ATOM   3683 C C    A VAL   A 1 165 ? 4.057  -12.481 2.892   0.76 17.11 ?  165 VAL   A C    1 
ATOM   3684 C C    B VAL   A 1 165 ? 4.110  -12.529 3.317   0.24 18.19 ?  165 VAL   A C    1 
ATOM   3685 O O    A VAL   A 1 165 ? 4.175  -13.713 2.855   0.76 16.79 ?  165 VAL   A O    1 
ATOM   3686 O O    B VAL   A 1 165 ? 4.004  -13.753 3.466   0.24 18.07 ?  165 VAL   A O    1 
ATOM   3687 C CB   A VAL   A 1 165 ? 4.494  -11.003 4.911   0.76 17.10 ?  165 VAL   A CB   1 
ATOM   3688 C CB   B VAL   A 1 165 ? 4.952  -11.285 5.385   0.24 18.09 ?  165 VAL   A CB   1 
ATOM   3689 C CG1  A VAL   A 1 165 ? 3.723  -12.050 5.708   0.76 17.89 ?  165 VAL   A CG1  1 
ATOM   3690 C CG1  B VAL   A 1 165 ? 4.059  -12.272 6.121   0.24 17.61 ?  165 VAL   A CG1  1 
ATOM   3691 C CG2  A VAL   A 1 165 ? 5.607  -10.388 5.759   0.76 17.61 ?  165 VAL   A CG2  1 
ATOM   3692 C CG2  B VAL   A 1 165 ? 6.245  -11.057 6.163   0.24 18.51 ?  165 VAL   A CG2  1 
ATOM   3693 H H    A VAL   A 1 165 ? 5.387  -9.760  2.997   0.76 20.37 ?  165 VAL   A H    1 
ATOM   3694 H H    B VAL   A 1 165 ? 5.427  -9.881  3.408   0.24 21.29 ?  165 VAL   A H    1 
ATOM   3695 H HA   A VAL   A 1 165 ? 5.818  -12.180 3.878   0.76 20.09 ?  165 VAL   A HA   1 
ATOM   3696 H HA   B VAL   A 1 165 ? 6.014  -12.393 4.037   0.24 21.57 ?  165 VAL   A HA   1 
ATOM   3697 H HB   A VAL   A 1 165 ? 3.876  -10.291 4.676   0.76 20.52 ?  165 VAL   A HB   1 
ATOM   3698 H HB   B VAL   A 1 165 ? 4.486  -10.438 5.336   0.24 21.71 ?  165 VAL   A HB   1 
ATOM   3699 H HG11 A VAL   A 1 165 ? 3.608  -11.731 6.618   0.76 21.47 ?  165 VAL   A HG11 1 
ATOM   3700 H HG11 B VAL   A 1 165 ? 4.035  -12.030 7.060   0.24 21.13 ?  165 VAL   A HG11 1 
ATOM   3701 H HG12 A VAL   A 1 165 ? 2.854  -12.186 5.297   0.76 21.47 ?  165 VAL   A HG12 1 
ATOM   3702 H HG12 B VAL   A 1 165 ? 3.165  -12.226 5.752   0.24 21.13 ?  165 VAL   A HG12 1 
ATOM   3703 H HG13 A VAL   A 1 165 ? 4.226  -12.877 5.710   0.76 21.47 ?  165 VAL   A HG13 1 
ATOM   3704 H HG13 B VAL   A 1 165 ? 4.422  -13.164 6.019   0.24 21.13 ?  165 VAL   A HG13 1 
ATOM   3705 H HG21 A VAL   A 1 165 ? 5.222  -10.018 6.570   0.76 21.14 ?  165 VAL   A HG21 1 
ATOM   3706 H HG21 B VAL   A 1 165 ? 6.060  -10.495 6.931   0.24 22.22 ?  165 VAL   A HG21 1 
ATOM   3707 H HG22 A VAL   A 1 165 ? 6.252  -11.075 5.982   0.76 21.14 ?  165 VAL   A HG22 1 
ATOM   3708 H HG22 B VAL   A 1 165 ? 6.595  -11.915 6.457   0.24 22.22 ?  165 VAL   A HG22 1 
ATOM   3709 H HG23 A VAL   A 1 165 ? 6.040  -9.682  5.249   0.76 21.14 ?  165 VAL   A HG23 1 
ATOM   3710 H HG23 B VAL   A 1 165 ? 6.888  -10.619 5.583   0.24 22.22 ?  165 VAL   A HG23 1 
ATOM   3711 N N    A SER   A 1 166 ? 3.043  -11.849 2.297   0.76 18.16 ?  166 SER   A N    1 
ATOM   3712 N N    B SER   A 1 166 ? 3.235  -11.833 2.585   0.24 18.30 ?  166 SER   A N    1 
ATOM   3713 C CA   A SER   A 1 166 ? 1.939  -12.609 1.720   0.76 19.67 ?  166 SER   A CA   1 
ATOM   3714 C CA   B SER   A 1 166 ? 2.050  -12.474 2.024   0.24 18.10 ?  166 SER   A CA   1 
ATOM   3715 C C    A SER   A 1 166 ? 2.404  -13.483 0.567   0.76 20.40 ?  166 SER   A C    1 
ATOM   3716 C C    B SER   A 1 166 ? 2.327  -13.248 0.740   0.24 18.53 ?  166 SER   A C    1 
ATOM   3717 O O    A SER   A 1 166 ? 1.820  -14.550 0.323   0.76 22.53 ?  166 SER   A O    1 
ATOM   3718 O O    B SER   A 1 166 ? 1.471  -14.032 0.317   0.24 18.81 ?  166 SER   A O    1 
ATOM   3719 C CB   A SER   A 1 166 ? 0.832  -11.659 1.256   0.76 20.93 ?  166 SER   A CB   1 
ATOM   3720 C CB   B SER   A 1 166 ? 0.970  -11.433 1.728   0.24 17.72 ?  166 SER   A CB   1 
ATOM   3721 O OG   A SER   A 1 166 ? 0.214  -11.010 2.357   0.76 22.16 ?  166 SER   A OG   1 
ATOM   3722 O OG   B SER   A 1 166 ? 1.177  -10.843 0.456   0.24 17.57 ?  166 SER   A OG   1 
ATOM   3723 H H    A SER   A 1 166 ? 2.968  -11.000 2.224   0.76 21.79 ?  166 SER   A H    1 
ATOM   3724 H H    B SER   A 1 166 ? 3.301  -10.993 2.417   0.24 21.97 ?  166 SER   A H    1 
ATOM   3725 H HA   A SER   A 1 166 ? 1.561  -13.193 2.396   0.76 23.61 ?  166 SER   A HA   1 
ATOM   3726 H HA   B SER   A 1 166 ? 1.693  -13.089 2.684   0.24 21.72 ?  166 SER   A HA   1 
ATOM   3727 H HB2  A SER   A 1 166 ? 1.215  -10.992 0.666   0.76 25.11 ?  166 SER   A HB2  1 
ATOM   3728 H HB2  B SER   A 1 166 ? 0.103  -11.869 1.738   0.24 21.26 ?  166 SER   A HB2  1 
ATOM   3729 H HB3  A SER   A 1 166 ? 0.153  -12.167 0.784   0.76 25.11 ?  166 SER   A HB3  1 
ATOM   3730 H HB3  B SER   A 1 166 ? 1.000  -10.741 2.405   0.24 21.26 ?  166 SER   A HB3  1 
ATOM   3731 H HG   A SER   A 1 166 ? -0.379 -10.480 2.085   0.76 26.59 ?  166 SER   A HG   1 
ATOM   3732 H HG   B SER   A 1 166 ? 1.925  -10.461 0.437   0.24 21.09 ?  166 SER   A HG   1 
ATOM   3733 N N    A SER   A 1 167 ? 3.445  -13.059 -0.147  0.76 19.93 ?  167 SER   A N    1 
ATOM   3734 N N    B SER   A 1 167 ? 3.472  -13.031 0.092   0.24 19.12 ?  167 SER   A N    1 
ATOM   3735 C CA   A SER   A 1 167 ? 3.931  -13.790 -1.305  0.76 20.65 ?  167 SER   A CA   1 
ATOM   3736 C CA   B SER   A 1 167 ? 3.825  -13.749 -1.128  0.24 20.06 ?  167 SER   A CA   1 
ATOM   3737 C C    A SER   A 1 167 ? 5.076  -14.737 -0.972  0.76 20.71 ?  167 SER   A C    1 
ATOM   3738 C C    B SER   A 1 167 ? 5.044  -14.648 -0.946  0.24 20.26 ?  167 SER   A C    1 
ATOM   3739 O O    A SER   A 1 167 ? 5.584  -15.405 -1.880  0.76 21.90 ?  167 SER   A O    1 
ATOM   3740 O O    B SER   A 1 167 ? 5.568  -15.182 -1.930  0.24 20.63 ?  167 SER   A O    1 
ATOM   3741 C CB   A SER   A 1 167 ? 4.379  -12.816 -2.406  0.76 21.11 ?  167 SER   A CB   1 
ATOM   3742 C CB   B SER   A 1 167 ? 4.058  -12.765 -2.276  0.24 20.99 ?  167 SER   A CB   1 
ATOM   3743 O OG   A SER   A 1 167 ? 5.474  -12.021 -1.976  0.76 20.58 ?  167 SER   A OG   1 
ATOM   3744 O OG   B SER   A 1 167 ? 5.080  -11.837 -1.950  0.24 21.60 ?  167 SER   A OG   1 
ATOM   3745 H H    A SER   A 1 167 ? 3.884  -12.337 0.023   0.76 23.91 ?  167 SER   A H    1 
ATOM   3746 H H    B SER   A 1 167 ? 4.063  -12.457 0.344   0.24 22.94 ?  167 SER   A H    1 
ATOM   3747 H HA   A SER   A 1 167 ? 3.205  -14.317 -1.664  0.76 24.78 ?  167 SER   A HA   1 
ATOM   3748 H HA   B SER   A 1 167 ? 3.073  -14.310 -1.377  0.24 24.07 ?  167 SER   A HA   1 
ATOM   3749 H HB2  A SER   A 1 167 ? 4.650  -13.327 -3.185  0.76 25.34 ?  167 SER   A HB2  1 
ATOM   3750 H HB2  B SER   A 1 167 ? 4.324  -13.264 -3.064  0.24 25.18 ?  167 SER   A HB2  1 
ATOM   3751 H HB3  A SER   A 1 167 ? 3.628  -12.240 -2.640  0.76 25.34 ?  167 SER   A HB3  1 
ATOM   3752 H HB3  B SER   A 1 167 ? 3.232  -12.286 -2.452  0.24 25.18 ?  167 SER   A HB3  1 
ATOM   3753 H HG   A SER   A 1 167 ? 5.237  -11.555 -1.314  0.76 24.69 ?  167 SER   A HG   1 
ATOM   3754 H HG   B SER   A 1 167 ? 4.853  -11.390 -1.275  0.24 25.92 ?  167 SER   A HG   1 
ATOM   3755 N N    . PHE   A 1 168 ? 5.503  -14.818 0.289   1.00 20.30 ?  168 PHE   A N    1 
ATOM   3756 C CA   . PHE   A 1 168 ? 6.685  -15.618 0.585   1.00 21.50 ?  168 PHE   A CA   1 
ATOM   3757 C C    . PHE   A 1 168 ? 6.383  -17.103 0.475   1.00 25.52 ?  168 PHE   A C    1 
ATOM   3758 O O    . PHE   A 1 168 ? 5.409  -17.597 1.054   1.00 26.26 ?  168 PHE   A O    1 
ATOM   3759 C CB   . PHE   A 1 168 ? 7.198  -15.329 1.991   1.00 19.86 ?  168 PHE   A CB   1 
ATOM   3760 C CG   . PHE   A 1 168 ? 8.464  -16.067 2.314   1.00 19.05 ?  168 PHE   A CG   1 
ATOM   3761 C CD1  . PHE   A 1 168 ? 9.655  -15.685 1.727   1.00 19.26 ?  168 PHE   A CD1  1 
ATOM   3762 C CD2  . PHE   A 1 168 ? 8.467  -17.164 3.162   1.00 18.84 ?  168 PHE   A CD2  1 
ATOM   3763 C CE1  . PHE   A 1 168 ? 10.827 -16.361 1.998   1.00 18.76 ?  168 PHE   A CE1  1 
ATOM   3764 C CE2  . PHE   A 1 168 ? 9.644  -17.842 3.439   1.00 18.97 ?  168 PHE   A CE2  1 
ATOM   3765 C CZ   . PHE   A 1 168 ? 10.820 -17.439 2.854   1.00 18.79 ?  168 PHE   A CZ   1 
ATOM   3766 H H    A PHE   A 1 168 ? 5.142  -14.430 0.967   0.76 24.36 ?  168 PHE   A H    1 
ATOM   3767 H H    B PHE   A 1 168 ? 5.151  -14.458 0.986   0.24 24.36 ?  168 PHE   A H    1 
ATOM   3768 H HA   . PHE   A 1 168 ? 7.388  -15.400 -0.049  1.00 25.80 ?  168 PHE   A HA   1 
ATOM   3769 H HB2  . PHE   A 1 168 ? 7.376  -14.379 2.072   1.00 23.84 ?  168 PHE   A HB2  1 
ATOM   3770 H HB3  . PHE   A 1 168 ? 6.523  -15.597 2.633   1.00 23.84 ?  168 PHE   A HB3  1 
ATOM   3771 H HD1  . PHE   A 1 168 ? 9.674  -14.955 1.150   1.00 23.11 ?  168 PHE   A HD1  1 
ATOM   3772 H HD2  . PHE   A 1 168 ? 7.674  -17.440 3.560   1.00 22.61 ?  168 PHE   A HD2  1 
ATOM   3773 H HE1  . PHE   A 1 168 ? 11.629 -16.087 1.605   1.00 22.51 ?  168 PHE   A HE1  1 
ATOM   3774 H HE2  . PHE   A 1 168 ? 9.637  -18.573 4.014   1.00 22.77 ?  168 PHE   A HE2  1 
ATOM   3775 H HZ   . PHE   A 1 168 ? 11.614 -17.894 3.036   1.00 22.54 ?  168 PHE   A HZ   1 
ATOM   3776 N N    A LEU   A 1 169 ? 7.236  -17.819 -0.248  0.76 28.60 ?  169 LEU   A N    1 
ATOM   3777 N N    B LEU   A 1 169 ? 7.231  -17.823 -0.252  0.24 28.42 ?  169 LEU   A N    1 
ATOM   3778 C CA   A LEU   A 1 169 ? 7.054  -19.249 -0.423  0.76 32.90 ?  169 LEU   A CA   1 
ATOM   3779 C CA   B LEU   A 1 169 ? 7.052  -19.259 -0.403  0.24 31.30 ?  169 LEU   A CA   1 
ATOM   3780 C C    A LEU   A 1 169 ? 7.946  -19.999 0.554   0.76 34.36 ?  169 LEU   A C    1 
ATOM   3781 C C    B LEU   A 1 169 ? 7.900  -20.011 0.616   0.24 32.01 ?  169 LEU   A C    1 
ATOM   3782 O O    A LEU   A 1 169 ? 7.475  -20.448 1.601   0.76 34.97 ?  169 LEU   A O    1 
ATOM   3783 O O    B LEU   A 1 169 ? 7.376  -20.556 1.587   0.24 32.14 ?  169 LEU   A O    1 
ATOM   3784 C CB   A LEU   A 1 169 ? 7.358  -19.656 -1.868  0.76 35.22 ?  169 LEU   A CB   1 
ATOM   3785 C CB   B LEU   A 1 169 ? 7.409  -19.702 -1.824  0.24 33.00 ?  169 LEU   A CB   1 
ATOM   3786 C CG   A LEU   A 1 169 ? 7.043  -21.108 -2.237  0.76 36.92 ?  169 LEU   A CG   1 
ATOM   3787 C CG   B LEU   A 1 169 ? 7.062  -21.150 -2.179  0.24 34.14 ?  169 LEU   A CG   1 
ATOM   3788 C CD1  A LEU   A 1 169 ? 5.615  -21.464 -1.852  0.76 37.77 ?  169 LEU   A CD1  1 
ATOM   3789 C CD1  B LEU   A 1 169 ? 5.644  -21.485 -1.742  0.24 34.64 ?  169 LEU   A CD1  1 
ATOM   3790 C CD2  A LEU   A 1 169 ? 7.270  -21.347 -3.724  0.76 37.42 ?  169 LEU   A CD2  1 
ATOM   3791 C CD2  B LEU   A 1 169 ? 7.227  -21.385 -3.673  0.24 34.50 ?  169 LEU   A CD2  1 
ATOM   3792 O OXT  A LEU   A 1 169 ? 9.148  -20.157 0.334   0.76 34.59 -1 169 LEU   A OXT  1 
ATOM   3793 O OXT  B LEU   A 1 169 ? 9.124  -20.082 0.498   0.24 32.30 -1 169 LEU   A OXT  1 
ATOM   3794 H H    A LEU   A 1 169 ? 7.931  -17.499 -0.643  0.76 34.32 ?  169 LEU   A H    1 
ATOM   3795 H H    B LEU   A 1 169 ? 7.915  -17.504 -0.666  0.24 34.10 ?  169 LEU   A H    1 
ATOM   3796 H HA   A LEU   A 1 169 ? 6.136  -19.477 -0.224  0.76 39.49 ?  169 LEU   A HA   1 
ATOM   3797 H HA   B LEU   A 1 169 ? 6.123  -19.471 -0.237  0.24 37.56 ?  169 LEU   A HA   1 
ATOM   3798 H HB2  A LEU   A 1 169 ? 6.837  -19.090 -2.459  0.76 42.26 ?  169 LEU   A HB2  1 
ATOM   3799 H HB2  B LEU   A 1 169 ? 6.938  -19.131 -2.449  0.24 39.60 ?  169 LEU   A HB2  1 
ATOM   3800 H HB3  A LEU   A 1 169 ? 8.302  -19.514 -2.036  0.76 42.26 ?  169 LEU   A HB3  1 
ATOM   3801 H HB3  B LEU   A 1 169 ? 8.365  -19.597 -1.947  0.24 39.60 ?  169 LEU   A HB3  1 
ATOM   3802 H HG   A LEU   A 1 169 ? 7.640  -21.695 -1.748  0.76 44.30 ?  169 LEU   A HG   1 
ATOM   3803 H HG   B LEU   A 1 169 ? 7.669  -21.747 -1.713  0.24 40.96 ?  169 LEU   A HG   1 
ATOM   3804 H HD11 A LEU   A 1 169 ? 5.371  -22.297 -2.282  0.76 45.32 ?  169 LEU   A HD11 1 
ATOM   3805 H HD11 B LEU   A 1 169 ? 5.360  -22.296 -2.187  0.24 41.57 ?  169 LEU   A HD11 1 
ATOM   3806 H HD12 A LEU   A 1 169 ? 5.564  -21.562 -0.888  0.76 45.32 ?  169 LEU   A HD12 1 
ATOM   3807 H HD12 B LEU   A 1 169 ? 5.633  -21.613 -0.780  0.24 41.57 ?  169 LEU   A HD12 1 
ATOM   3808 H HD13 A LEU   A 1 169 ? 5.024  -20.753 -2.145  0.76 45.32 ?  169 LEU   A HD13 1 
ATOM   3809 H HD13 B LEU   A 1 169 ? 5.059  -20.750 -1.986  0.24 41.57 ?  169 LEU   A HD13 1 
ATOM   3810 H HD21 A LEU   A 1 169 ? 7.070  -22.274 -3.929  0.76 44.90 ?  169 LEU   A HD21 1 
ATOM   3811 H HD21 B LEU   A 1 169 ? 7.011  -22.310 -3.873  0.24 41.40 ?  169 LEU   A HD21 1 
ATOM   3812 H HD22 A LEU   A 1 169 ? 6.683  -20.763 -4.230  0.76 44.90 ?  169 LEU   A HD22 1 
ATOM   3813 H HD22 B LEU   A 1 169 ? 6.625  -20.794 -4.153  0.24 41.40 ?  169 LEU   A HD22 1 
ATOM   3814 H HD23 A LEU   A 1 169 ? 8.195  -21.152 -3.937  0.76 44.90 ?  169 LEU   A HD23 1 
ATOM   3815 H HD23 B LEU   A 1 169 ? 8.144  -21.197 -3.923  0.24 41.40 ?  169 LEU   A HD23 1 
ATOM   3816 N N    A SER   B 1 1   ? 50.828 -9.236  -23.739 0.76 30.61 ?  1   SER   B N    1 
ATOM   3817 N N    B SER   B 1 1   ? 50.776 -9.262  -23.760 0.24 28.30 ?  1   SER   B N    1 
ATOM   3818 C CA   A SER   B 1 1   ? 51.323 -10.300 -22.844 0.76 30.04 ?  1   SER   B CA   1 
ATOM   3819 C CA   B SER   B 1 1   ? 51.272 -10.264 -22.792 0.24 28.02 ?  1   SER   B CA   1 
ATOM   3820 C C    A SER   B 1 1   ? 50.242 -11.340 -22.582 0.76 28.73 ?  1   SER   B C    1 
ATOM   3821 C C    B SER   B 1 1   ? 50.215 -11.332 -22.553 0.24 27.54 ?  1   SER   B C    1 
ATOM   3822 O O    A SER   B 1 1   ? 49.049 -11.131 -22.850 0.76 28.60 ?  1   SER   B O    1 
ATOM   3823 O O    B SER   B 1 1   ? 49.055 -11.184 -22.947 0.24 27.45 ?  1   SER   B O    1 
ATOM   3824 C CB   A SER   B 1 1   ? 51.809 -9.712  -21.521 0.76 31.00 ?  1   SER   B CB   1 
ATOM   3825 C CB   B SER   B 1 1   ? 51.644 -9.595  -21.473 0.24 28.43 ?  1   SER   B CB   1 
ATOM   3826 O OG   A SER   B 1 1   ? 50.717 -9.410  -20.673 0.76 32.42 ?  1   SER   B OG   1 
ATOM   3827 O OG   B SER   B 1 1   ? 50.513 -9.495  -20.628 0.24 28.78 ?  1   SER   B OG   1 
ATOM   3828 H H1   A SER   B 1 1   ? 50.642 -9.589  -24.531 0.76 36.73 ?  1   SER   B H1   1 
ATOM   3829 H H1   B SER   B 1 1   ? 51.456 -8.754  -24.021 0.24 33.95 ?  1   SER   B H1   1 
ATOM   3830 H H2   A SER   B 1 1   ? 50.098 -8.879  -23.386 0.76 36.73 ?  1   SER   B H2   1 
ATOM   3831 H H2   B SER   B 1 1   ? 50.429 -9.684  -24.460 0.24 33.95 ?  1   SER   B H2   1 
ATOM   3832 H H3   A SER   B 1 1   ? 51.458 -8.616  -23.824 0.76 36.73 ?  1   SER   B H3   1 
ATOM   3833 H H3   B SER   B 1 1   ? 50.157 -8.763  -23.369 0.24 33.95 ?  1   SER   B H3   1 
ATOM   3834 H HA   A SER   B 1 1   ? 52.072 -10.734 -23.276 0.76 36.05 ?  1   SER   B HA   1 
ATOM   3835 H HA   B SER   B 1 1   ? 52.060 -10.682 -23.162 0.24 33.62 ?  1   SER   B HA   1 
ATOM   3836 H HB2  A SER   B 1 1   ? 52.378 -10.362 -21.084 0.76 37.21 ?  1   SER   B HB2  1 
ATOM   3837 H HB2  B SER   B 1 1   ? 52.329 -10.127 -21.041 0.24 34.11 ?  1   SER   B HB2  1 
ATOM   3838 H HB3  A SER   B 1 1   ? 52.309 -8.899  -21.699 0.76 37.21 ?  1   SER   B HB3  1 
ATOM   3839 H HB3  B SER   B 1 1   ? 51.980 -8.703  -21.653 0.24 34.11 ?  1   SER   B HB3  1 
ATOM   3840 H HG   A SER   B 1 1   ? 50.974 -8.902  -20.054 0.76 38.90 ?  1   SER   B HG   1 
ATOM   3841 H HG   B SER   B 1 1   ? 50.655 -8.920  -20.034 0.24 34.53 ?  1   SER   B HG   1 
ATOM   3842 N N    A MET   B 1 2   ? 50.684 -12.465 -22.039 0.76 27.75 ?  2   MET   B N    1 
ATOM   3843 N N    B MET   B 1 2   ? 50.626 -12.407 -21.890 0.24 27.17 ?  2   MET   B N    1 
ATOM   3844 C CA   A MET   B 1 2   ? 49.860 -13.653 -21.874 0.76 27.74 ?  2   MET   B CA   1 
ATOM   3845 C CA   B MET   B 1 2   ? 49.812 -13.608 -21.731 0.24 26.71 ?  2   MET   B CA   1 
ATOM   3846 C C    A MET   B 1 2   ? 49.622 -13.854 -20.384 0.76 25.29 ?  2   MET   B C    1 
ATOM   3847 C C    B MET   B 1 2   ? 49.538 -13.816 -20.246 0.24 24.96 ?  2   MET   B C    1 
ATOM   3848 O O    A MET   B 1 2   ? 50.561 -14.131 -19.631 0.76 25.64 ?  2   MET   B O    1 
ATOM   3849 O O    B MET   B 1 2   ? 50.421 -14.248 -19.498 0.24 25.25 ?  2   MET   B O    1 
ATOM   3850 C CB   A MET   B 1 2   ? 50.588 -14.844 -22.487 0.76 31.75 ?  2   MET   B CB   1 
ATOM   3851 C CB   B MET   B 1 2   ? 50.554 -14.794 -22.323 0.24 28.22 ?  2   MET   B CB   1 
ATOM   3852 C CG   A MET   B 1 2   ? 49.747 -16.096 -22.655 0.76 35.49 ?  2   MET   B CG   1 
ATOM   3853 C CG   B MET   B 1 2   ? 49.671 -15.948 -22.773 0.24 29.33 ?  2   MET   B CG   1 
ATOM   3854 S SD   A MET   B 1 2   ? 50.581 -17.311 -23.693 0.76 38.78 ?  2   MET   B SD   1 
ATOM   3855 S SD   B MET   B 1 2   ? 50.551 -17.026 -23.910 0.24 30.32 ?  2   MET   B SD   1 
ATOM   3856 C CE   A MET   B 1 2   ? 51.112 -16.253 -25.031 0.76 39.01 ?  2   MET   B CE   1 
ATOM   3857 C CE   B MET   B 1 2   ? 51.388 -15.806 -24.908 0.24 30.54 ?  2   MET   B CE   1 
ATOM   3858 H H    A MET   B 1 2   ? 51.487 -12.572 -21.747 0.76 33.30 ?  2   MET   B H    1 
ATOM   3859 H H    B MET   B 1 2   ? 51.401 -12.470 -21.521 0.24 32.61 ?  2   MET   B H    1 
ATOM   3860 H HA   A MET   B 1 2   ? 49.016 -13.543 -22.337 0.76 33.28 ?  2   MET   B HA   1 
ATOM   3861 H HA   B MET   B 1 2   ? 48.980 -13.505 -22.218 0.24 32.05 ?  2   MET   B HA   1 
ATOM   3862 H HB2  A MET   B 1 2   ? 50.904 -14.554 -23.354 0.76 38.10 ?  2   MET   B HB2  1 
ATOM   3863 H HB2  B MET   B 1 2   ? 51.060 -14.442 -23.067 0.24 33.87 ?  2   MET   B HB2  1 
ATOM   3864 H HB3  A MET   B 1 2   ? 51.343 -15.083 -21.932 0.76 38.10 ?  2   MET   B HB3  1 
ATOM   3865 H HB3  B MET   B 1 2   ? 51.164 -15.159 -21.673 0.24 33.87 ?  2   MET   B HB3  1 
ATOM   3866 H HG2  A MET   B 1 2   ? 49.587 -16.492 -21.780 0.76 42.59 ?  2   MET   B HG2  1 
ATOM   3867 H HG2  B MET   B 1 2   ? 49.405 -16.471 -21.996 0.24 35.20 ?  2   MET   B HG2  1 
ATOM   3868 H HG3  A MET   B 1 2   ? 48.909 -15.873 -23.084 0.76 42.59 ?  2   MET   B HG3  1 
ATOM   3869 H HG3  B MET   B 1 2   ? 48.889 -15.612 -23.231 0.24 35.20 ?  2   MET   B HG3  1 
ATOM   3870 H HE1  A MET   B 1 2   ? 51.262 -16.797 -25.807 0.76 46.81 ?  2   MET   B HE1  1 
ATOM   3871 H HE1  B MET   B 1 2   ? 51.585 -16.208 -25.747 0.24 36.65 ?  2   MET   B HE1  1 
ATOM   3872 H HE2  A MET   B 1 2   ? 50.407 -15.606 -25.202 0.76 46.81 ?  2   MET   B HE2  1 
ATOM   3873 H HE2  B MET   B 1 2   ? 50.799 -15.042 -25.036 0.24 36.65 ?  2   MET   B HE2  1 
ATOM   3874 H HE3  A MET   B 1 2   ? 51.931 -15.788 -24.782 0.76 46.81 ?  2   MET   B HE3  1 
ATOM   3875 H HE3  B MET   B 1 2   ? 52.210 -15.525 -24.461 0.24 36.65 ?  2   MET   B HE3  1 
ATOM   3876 N N    A VAL   B 1 3   ? 48.375 -13.670 -19.958 0.76 22.44 ?  3   VAL   B N    1 
ATOM   3877 N N    B VAL   B 1 3   ? 48.320 -13.499 -19.820 0.24 22.94 ?  3   VAL   B N    1 
ATOM   3878 C CA   A VAL   B 1 3   ? 47.961 -13.916 -18.585 0.76 21.38 ?  3   VAL   B CA   1 
ATOM   3879 C CA   B VAL   B 1 3   ? 47.876 -13.767 -18.459 0.24 21.28 ?  3   VAL   B CA   1 
ATOM   3880 C C    A VAL   B 1 3   ? 46.724 -14.805 -18.609 0.76 19.24 ?  3   VAL   B C    1 
ATOM   3881 C C    B VAL   B 1 3   ? 46.630 -14.640 -18.509 0.24 19.34 ?  3   VAL   B C    1 
ATOM   3882 O O    A VAL   B 1 3   ? 46.004 -14.889 -19.607 0.76 19.62 ?  3   VAL   B O    1 
ATOM   3883 O O    B VAL   B 1 3   ? 45.816 -14.549 -19.433 0.24 19.31 ?  3   VAL   B O    1 
ATOM   3884 C CB   A VAL   B 1 3   ? 47.682 -12.604 -17.816 0.76 23.08 ?  3   VAL   B CB   1 
ATOM   3885 C CB   B VAL   B 1 3   ? 47.605 -12.477 -17.653 0.24 21.72 ?  3   VAL   B CB   1 
ATOM   3886 C CG1  A VAL   B 1 3   ? 48.955 -11.752 -17.723 0.76 23.68 ?  3   VAL   B CG1  1 
ATOM   3887 C CG1  B VAL   B 1 3   ? 48.871 -11.639 -17.541 0.24 21.87 ?  3   VAL   B CG1  1 
ATOM   3888 C CG2  A VAL   B 1 3   ? 46.555 -11.823 -18.477 0.76 23.89 ?  3   VAL   B CG2  1 
ATOM   3889 C CG2  B VAL   B 1 3   ? 46.473 -11.680 -18.281 0.24 21.92 ?  3   VAL   B CG2  1 
ATOM   3890 H H    A VAL   B 1 3   ? 47.739 -13.388 -20.463 0.76 26.92 ?  3   VAL   B H    1 
ATOM   3891 H H    B VAL   B 1 3   ? 47.731 -13.115 -20.315 0.24 27.53 ?  3   VAL   B H    1 
ATOM   3892 H HA   A VAL   B 1 3   ? 48.666 -14.393 -18.119 0.76 25.66 ?  3   VAL   B HA   1 
ATOM   3893 H HA   B VAL   B 1 3   ? 48.571 -14.262 -18.000 0.24 25.54 ?  3   VAL   B HA   1 
ATOM   3894 H HB   A VAL   B 1 3   ? 47.409 -12.823 -16.912 0.76 27.70 ?  3   VAL   B HB   1 
ATOM   3895 H HB   B VAL   B 1 3   ? 47.334 -12.727 -16.757 0.24 26.06 ?  3   VAL   B HB   1 
ATOM   3896 H HG11 A VAL   B 1 3   ? 48.756 -10.943 -17.225 0.76 28.41 ?  3   VAL   B HG11 1 
ATOM   3897 H HG11 B VAL   B 1 3   ? 48.678 -10.847 -17.015 0.24 26.25 ?  3   VAL   B HG11 1 
ATOM   3898 H HG12 A VAL   B 1 3   ? 49.643 -12.261 -17.266 0.76 28.41 ?  3   VAL   B HG12 1 
ATOM   3899 H HG12 B VAL   B 1 3   ? 49.561 -12.165 -17.107 0.24 26.25 ?  3   VAL   B HG12 1 
ATOM   3900 H HG13 A VAL   B 1 3   ? 49.250 -11.526 -18.618 0.76 28.41 ?  3   VAL   B HG13 1 
ATOM   3901 H HG13 B VAL   B 1 3   ? 49.160 -11.383 -18.431 0.24 26.25 ?  3   VAL   B HG13 1 
ATOM   3902 H HG21 A VAL   B 1 3   ? 46.498 -10.948 -18.068 0.76 28.66 ?  3   VAL   B HG21 1 
ATOM   3903 H HG21 B VAL   B 1 3   ? 46.423 -10.815 -17.848 0.24 26.31 ?  3   VAL   B HG21 1 
ATOM   3904 H HG22 A VAL   B 1 3   ? 46.744 -11.737 -19.423 0.76 28.66 ?  3   VAL   B HG22 1 
ATOM   3905 H HG22 B VAL   B 1 3   ? 46.651 -11.570 -19.227 0.24 26.31 ?  3   VAL   B HG22 1 
ATOM   3906 H HG23 A VAL   B 1 3   ? 45.722 -12.305 -18.347 0.76 28.66 ?  3   VAL   B HG23 1 
ATOM   3907 H HG23 B VAL   B 1 3   ? 45.639 -12.161 -18.155 0.24 26.31 ?  3   VAL   B HG23 1 
ATOM   3908 N N    . ASN   B 1 4   ? 46.483 -15.485 -17.490 1.00 17.65 ?  4   ASN   B N    1 
ATOM   3909 C CA   . ASN   B 1 4   ? 45.346 -16.401 -17.383 1.00 16.68 ?  4   ASN   B CA   1 
ATOM   3910 C C    . ASN   B 1 4   ? 45.291 -17.366 -18.566 1.00 17.23 ?  4   ASN   B C    1 
ATOM   3911 O O    . ASN   B 1 4   ? 44.229 -17.622 -19.130 1.00 17.97 ?  4   ASN   B O    1 
ATOM   3912 C CB   . ASN   B 1 4   ? 44.023 -15.645 -17.223 1.00 16.15 ?  4   ASN   B CB   1 
ATOM   3913 C CG   . ASN   B 1 4   ? 43.972 -14.836 -15.944 1.00 15.13 ?  4   ASN   B CG   1 
ATOM   3914 O OD1  . ASN   B 1 4   ? 44.267 -15.346 -14.862 1.00 15.17 ?  4   ASN   B OD1  1 
ATOM   3915 N ND2  . ASN   B 1 4   ? 43.621 -13.561 -16.064 1.00 15.87 ?  4   ASN   B ND2  1 
ATOM   3916 H H    A ASN   B 1 4   ? 46.968 -15.440 -16.784 0.76 21.18 ?  4   ASN   B H    1 
ATOM   3917 H H    B ASN   B 1 4   ? 47.036 -15.541 -16.836 0.24 21.18 ?  4   ASN   B H    1 
ATOM   3918 H HA   . ASN   B 1 4   ? 45.471 -16.937 -16.585 1.00 20.02 ?  4   ASN   B HA   1 
ATOM   3919 H HB2  . ASN   B 1 4   ? 43.911 -15.041 -17.970 1.00 19.38 ?  4   ASN   B HB2  1 
ATOM   3920 H HB3  . ASN   B 1 4   ? 43.296 -16.290 -17.203 1.00 19.38 ?  4   ASN   B HB3  1 
ATOM   3921 H HD21 . ASN   B 1 4   ? 43.581 -13.055 -15.367 1.00 19.04 ?  4   ASN   B HD21 1 
ATOM   3922 H HD22 . ASN   B 1 4   ? 43.433 -13.233 -16.838 1.00 19.04 ?  4   ASN   B HD22 1 
ATOM   3923 N N    . SER   B 1 5   ? 46.449 -17.906 -18.948 1.00 17.55 ?  5   SER   B N    1 
ATOM   3924 C CA   . SER   B 1 5   ? 46.538 -18.827 -20.083 1.00 20.36 ?  5   SER   B CA   1 
ATOM   3925 C C    . SER   B 1 5   ? 46.534 -20.261 -19.563 1.00 21.97 ?  5   SER   B C    1 
ATOM   3926 O O    . SER   B 1 5   ? 47.549 -20.950 -19.536 1.00 24.44 ?  5   SER   B O    1 
ATOM   3927 C CB   . SER   B 1 5   ? 47.783 -18.535 -20.919 1.00 21.93 ?  5   SER   B CB   1 
ATOM   3928 O OG   . SER   B 1 5   ? 48.965 -18.721 -20.157 1.00 25.52 ?  5   SER   B OG   1 
ATOM   3929 H H    . SER   B 1 5   ? 47.206 -17.768 -18.556 1.00 21.05 ?  5   SER   B H    1 
ATOM   3930 H HA   . SER   B 1 5   ? 45.766 -18.713 -20.653 1.00 24.44 ?  5   SER   B HA   1 
ATOM   3931 H HB2  . SER   B 1 5   ? 47.798 -19.135 -21.688 1.00 26.32 ?  5   SER   B HB2  1 
ATOM   3932 H HB3  . SER   B 1 5   ? 47.742 -17.617 -21.225 1.00 26.32 ?  5   SER   B HB3  1 
ATOM   3933 H HG   . SER   B 1 5   ? 49.030 -19.526 -19.922 1.00 30.63 ?  5   SER   B HG   1 
ATOM   3934 N N    . PHE   B 1 6   ? 45.351 -20.692 -19.132 1.00 22.54 ?  6   PHE   B N    1 
ATOM   3935 C CA   . PHE   B 1 6   ? 45.170 -22.033 -18.595 1.00 21.51 ?  6   PHE   B CA   1 
ATOM   3936 C C    . PHE   B 1 6   ? 45.109 -23.026 -19.745 1.00 24.76 ?  6   PHE   B C    1 
ATOM   3937 O O    . PHE   B 1 6   ? 44.451 -22.770 -20.757 1.00 27.07 ?  6   PHE   B O    1 
ATOM   3938 C CB   . PHE   B 1 6   ? 43.878 -22.094 -17.779 1.00 19.46 ?  6   PHE   B CB   1 
ATOM   3939 C CG   . PHE   B 1 6   ? 43.894 -21.228 -16.547 1.00 17.48 ?  6   PHE   B CG   1 
ATOM   3940 C CD1  . PHE   B 1 6   ? 44.414 -21.710 -15.362 1.00 16.55 ?  6   PHE   B CD1  1 
ATOM   3941 C CD2  . PHE   B 1 6   ? 43.400 -19.931 -16.582 1.00 17.00 ?  6   PHE   B CD2  1 
ATOM   3942 C CE1  . PHE   B 1 6   ? 44.428 -20.924 -14.223 1.00 15.95 ?  6   PHE   B CE1  1 
ATOM   3943 C CE2  . PHE   B 1 6   ? 43.424 -19.127 -15.451 1.00 17.66 ?  6   PHE   B CE2  1 
ATOM   3944 C CZ   . PHE   B 1 6   ? 43.941 -19.619 -14.273 1.00 16.53 ?  6   PHE   B CZ   1 
ATOM   3945 H H    . PHE   B 1 6   ? 44.628 -20.228 -19.150 1.00 27.05 ?  6   PHE   B H    1 
ATOM   3946 H HA   . PHE   B 1 6   ? 45.914 -22.268 -18.021 1.00 25.81 ?  6   PHE   B HA   1 
ATOM   3947 H HB2  . PHE   B 1 6   ? 43.140 -21.800 -18.337 1.00 23.35 ?  6   PHE   B HB2  1 
ATOM   3948 H HB3  . PHE   B 1 6   ? 43.727 -23.009 -17.493 1.00 23.35 ?  6   PHE   B HB3  1 
ATOM   3949 H HD1  . PHE   B 1 6   ? 44.753 -22.574 -15.325 1.00 19.87 ?  6   PHE   B HD1  1 
ATOM   3950 H HD2  . PHE   B 1 6   ? 43.049 -19.597 -17.374 1.00 20.40 ?  6   PHE   B HD2  1 
ATOM   3951 H HE1  . PHE   B 1 6   ? 44.791 -21.252 -13.431 1.00 19.13 ?  6   PHE   B HE1  1 
ATOM   3952 H HE2  . PHE   B 1 6   ? 43.082 -18.262 -15.484 1.00 21.20 ?  6   PHE   B HE2  1 
ATOM   3953 H HZ   . PHE   B 1 6   ? 43.953 -19.089 -13.509 1.00 19.83 ?  6   PHE   B HZ   1 
ATOM   3954 N N    . SER   B 1 7   ? 45.811 -24.150 -19.598 1.00 25.41 ?  7   SER   B N    1 
ATOM   3955 C CA   . SER   B 1 7   ? 45.910 -25.139 -20.660 1.00 27.87 ?  7   SER   B CA   1 
ATOM   3956 C C    . SER   B 1 7   ? 45.870 -26.542 -20.071 1.00 26.96 ?  7   SER   B C    1 
ATOM   3957 O O    . SER   B 1 7   ? 46.459 -26.803 -19.018 1.00 28.18 ?  7   SER   B O    1 
ATOM   3958 C CB   . SER   B 1 7   ? 47.205 -24.953 -21.463 1.00 30.39 ?  7   SER   B CB   1 
ATOM   3959 O OG   . SER   B 1 7   ? 47.212 -25.774 -22.617 1.00 33.87 ?  7   SER   B OG   1 
ATOM   3960 H H    . SER   B 1 7   ? 46.250 -24.358 -18.884 1.00 30.49 ?  7   SER   B H    1 
ATOM   3961 H HA   . SER   B 1 7   ? 45.160 -25.044 -21.262 1.00 33.45 ?  7   SER   B HA   1 
ATOM   3962 H HB2  . SER   B 1 7   ? 47.275 -24.022 -21.736 1.00 36.47 ?  7   SER   B HB2  1 
ATOM   3963 H HB3  . SER   B 1 7   ? 47.963 -25.189 -20.906 1.00 36.47 ?  7   SER   B HB3  1 
ATOM   3964 H HG   . SER   B 1 7   ? 47.924 -25.656 -23.050 1.00 40.65 ?  7   SER   B HG   1 
ATOM   3965 N N    A GLY   B 1 8   ? 45.163 -27.440 -20.756 0.76 26.75 ?  8   GLY   B N    1 
ATOM   3966 N N    B GLY   B 1 8   ? 45.170 -27.440 -20.760 0.24 26.44 ?  8   GLY   B N    1 
ATOM   3967 C CA   A GLY   B 1 8   ? 45.133 -28.832 -20.362 0.76 26.31 ?  8   GLY   B CA   1 
ATOM   3968 C CA   B GLY   B 1 8   ? 45.132 -28.831 -20.359 0.24 25.80 ?  8   GLY   B CA   1 
ATOM   3969 C C    A GLY   B 1 8   ? 44.157 -29.170 -19.262 0.76 25.32 ?  8   GLY   B C    1 
ATOM   3970 C C    B GLY   B 1 8   ? 44.182 -29.148 -19.231 0.24 24.99 ?  8   GLY   B C    1 
ATOM   3971 O O    A GLY   B 1 8   ? 44.276 -30.242 -18.657 0.76 26.62 ?  8   GLY   B O    1 
ATOM   3972 O O    B GLY   B 1 8   ? 44.354 -30.175 -18.566 0.24 25.48 ?  8   GLY   B O    1 
ATOM   3973 H H    A GLY   B 1 8   ? 44.696 -27.258 -21.453 0.76 32.10 ?  8   GLY   B H    1 
ATOM   3974 H H    B GLY   B 1 8   ? 44.708 -27.261 -21.461 0.24 31.73 ?  8   GLY   B H    1 
ATOM   3975 H HA2  A GLY   B 1 8   ? 44.905 -29.371 -21.134 0.76 31.57 ?  8   GLY   B HA2  1 
ATOM   3976 H HA2  B GLY   B 1 8   ? 44.878 -29.370 -21.124 0.24 30.96 ?  8   GLY   B HA2  1 
ATOM   3977 H HA3  A GLY   B 1 8   ? 46.016 -29.095 -20.061 0.76 31.57 ?  8   GLY   B HA3  1 
ATOM   3978 H HA3  B GLY   B 1 8   ? 46.018 -29.104 -20.080 0.24 30.96 ?  8   GLY   B HA3  1 
ATOM   3979 N N    . TYR   B 1 9   ? 43.178 -28.308 -18.993 1.00 23.71 ?  9   TYR   B N    1 
ATOM   3980 C CA   . TYR   B 1 9   ? 42.208 -28.564 -17.941 1.00 21.13 ?  9   TYR   B CA   1 
ATOM   3981 C C    . TYR   B 1 9   ? 41.025 -29.354 -18.466 1.00 20.31 ?  9   TYR   B C    1 
ATOM   3982 O O    . TYR   B 1 9   ? 40.615 -29.213 -19.622 1.00 22.36 ?  9   TYR   B O    1 
ATOM   3983 C CB   . TYR   B 1 9   ? 41.699 -27.268 -17.317 1.00 20.44 ?  9   TYR   B CB   1 
ATOM   3984 C CG   . TYR   B 1 9   ? 42.715 -26.642 -16.396 1.00 19.58 ?  9   TYR   B CG   1 
ATOM   3985 C CD1  . TYR   B 1 9   ? 43.825 -25.984 -16.910 1.00 20.28 ?  9   TYR   B CD1  1 
ATOM   3986 C CD2  . TYR   B 1 9   ? 42.587 -26.731 -15.018 1.00 18.52 ?  9   TYR   B CD2  1 
ATOM   3987 C CE1  . TYR   B 1 9   ? 44.773 -25.422 -16.078 1.00 20.55 ?  9   TYR   B CE1  1 
ATOM   3988 C CE2  . TYR   B 1 9   ? 43.531 -26.173 -14.176 1.00 18.98 ?  9   TYR   B CE2  1 
ATOM   3989 C CZ   . TYR   B 1 9   ? 44.622 -25.518 -14.715 1.00 20.13 ?  9   TYR   B CZ   1 
ATOM   3990 O OH   . TYR   B 1 9   ? 45.568 -24.964 -13.889 1.00 20.90 ?  9   TYR   B OH   1 
ATOM   3991 H H    A TYR   B 1 9   ? 43.046 -27.572 -19.418 0.76 28.45 ?  9   TYR   B H    1 
ATOM   3992 H H    B TYR   B 1 9   ? 43.031 -27.585 -19.437 0.24 28.45 ?  9   TYR   B H    1 
ATOM   3993 H HA   . TYR   B 1 9   ? 42.624 -29.083 -17.241 1.00 25.36 ?  9   TYR   B HA   1 
ATOM   3994 H HB2  . TYR   B 1 9   ? 41.486 -26.627 -18.017 1.00 24.53 ?  9   TYR   B HB2  1 
ATOM   3995 H HB3  . TYR   B 1 9   ? 40.909 -27.468 -16.796 1.00 24.53 ?  9   TYR   B HB3  1 
ATOM   3996 H HD1  . TYR   B 1 9   ? 43.930 -25.921 -17.832 1.00 24.34 ?  9   TYR   B HD1  1 
ATOM   3997 H HD2  . TYR   B 1 9   ? 41.849 -27.172 -14.654 1.00 22.22 ?  9   TYR   B HD2  1 
ATOM   3998 H HE1  . TYR   B 1 9   ? 45.507 -24.986 -16.437 1.00 24.65 ?  9   TYR   B HE1  1 
ATOM   3999 H HE2  . TYR   B 1 9   ? 43.424 -26.239 -13.252 1.00 22.78 ?  9   TYR   B HE2  1 
ATOM   4000 H HH   . TYR   B 1 9   ? 46.168 -24.601 -14.348 1.00 25.08 ?  9   TYR   B HH   1 
ATOM   4001 N N    . LEU   B 1 10  ? 40.487 -30.198 -17.594 1.00 18.61 ?  10  LEU   B N    1 
ATOM   4002 C CA   . LEU   B 1 10  ? 39.277 -30.950 -17.872 1.00 18.38 ?  10  LEU   B CA   1 
ATOM   4003 C C    . LEU   B 1 10  ? 38.091 -30.177 -17.314 1.00 18.12 ?  10  LEU   B C    1 
ATOM   4004 O O    . LEU   B 1 10  ? 38.107 -29.753 -16.155 1.00 17.76 ?  10  LEU   B O    1 
ATOM   4005 C CB   . LEU   B 1 10  ? 39.366 -32.320 -17.201 1.00 19.51 ?  10  LEU   B CB   1 
ATOM   4006 C CG   . LEU   B 1 10  ? 38.204 -33.263 -17.497 1.00 21.22 ?  10  LEU   B CG   1 
ATOM   4007 C CD1  . LEU   B 1 10  ? 38.281 -33.771 -18.931 1.00 22.82 ?  10  LEU   B CD1  1 
ATOM   4008 C CD2  . LEU   B 1 10  ? 38.184 -34.415 -16.509 1.00 22.26 ?  10  LEU   B CD2  1 
ATOM   4009 H H    . LEU   B 1 10  ? 40.814 -30.362 -16.810 1.00 22.33 ?  10  LEU   B H    1 
ATOM   4010 H HA   . LEU   B 1 10  ? 39.163 -31.074 -18.825 1.00 22.06 ?  10  LEU   B HA   1 
ATOM   4011 H HB2  . LEU   B 1 10  ? 40.179 -32.763 -17.498 1.00 23.41 ?  10  LEU   B HB2  1 
ATOM   4012 H HB3  . LEU   B 1 10  ? 39.401 -32.197 -16.238 1.00 23.41 ?  10  LEU   B HB3  1 
ATOM   4013 H HG   . LEU   B 1 10  ? 37.370 -32.779 -17.397 1.00 25.46 ?  10  LEU   B HG   1 
ATOM   4014 H HD11 . LEU   B 1 10  ? 37.565 -34.407 -19.078 1.00 27.39 ?  10  LEU   B HD11 1 
ATOM   4015 H HD12 . LEU   B 1 10  ? 38.186 -33.019 -19.535 1.00 27.39 ?  10  LEU   B HD12 1 
ATOM   4016 H HD13 . LEU   B 1 10  ? 39.140 -34.200 -19.066 1.00 27.39 ?  10  LEU   B HD13 1 
ATOM   4017 H HD21 . LEU   B 1 10  ? 37.440 -34.998 -16.723 1.00 26.71 ?  10  LEU   B HD21 1 
ATOM   4018 H HD22 . LEU   B 1 10  ? 39.019 -34.899 -16.577 1.00 26.71 ?  10  LEU   B HD22 1 
ATOM   4019 H HD23 . LEU   B 1 10  ? 38.077 -34.056 -15.614 1.00 26.71 ?  10  LEU   B HD23 1 
ATOM   4020 N N    . LYS   B 1 11  ? 37.070 -29.995 -18.140 1.00 19.42 ?  11  LYS   B N    1 
ATOM   4021 C CA   . LYS   B 1 11  ? 35.875 -29.276 -17.726 1.00 20.72 ?  11  LYS   B CA   1 
ATOM   4022 C C    . LYS   B 1 11  ? 34.987 -30.200 -16.897 1.00 20.09 ?  11  LYS   B C    1 
ATOM   4023 O O    . LYS   B 1 11  ? 34.596 -31.279 -17.363 1.00 22.42 ?  11  LYS   B O    1 
ATOM   4024 C CB   . LYS   B 1 11  ? 35.134 -28.788 -18.969 1.00 24.54 ?  11  LYS   B CB   1 
ATOM   4025 C CG   . LYS   B 1 11  ? 33.950 -27.882 -18.700 1.00 28.21 ?  11  LYS   B CG   1 
ATOM   4026 C CD   . LYS   B 1 11  ? 33.189 -27.606 -19.991 1.00 31.34 ?  11  LYS   B CD   1 
ATOM   4027 C CE   . LYS   B 1 11  ? 32.190 -26.475 -19.824 1.00 33.54 ?  11  LYS   B CE   1 
ATOM   4028 N NZ   . LYS   B 1 11  ? 32.870 -25.167 -19.629 1.00 34.96 ?  11  LYS   B NZ   1 
ATOM   4029 H H    . LYS   B 1 11  ? 37.043 -30.285 -18.950 1.00 23.30 ?  11  LYS   B H    1 
ATOM   4030 H HA   . LYS   B 1 11  ? 36.126 -28.510 -17.185 1.00 24.86 ?  11  LYS   B HA   1 
ATOM   4031 H HB2  . LYS   B 1 11  ? 35.760 -28.294 -19.523 1.00 29.45 ?  11  LYS   B HB2  1 
ATOM   4032 H HB3  . LYS   B 1 11  ? 34.809 -29.560 -19.455 1.00 29.45 ?  11  LYS   B HB3  1 
ATOM   4033 H HG2  . LYS   B 1 11  ? 33.348 -28.315 -18.076 1.00 33.86 ?  11  LYS   B HG2  1 
ATOM   4034 H HG3  . LYS   B 1 11  ? 34.264 -27.038 -18.341 1.00 33.86 ?  11  LYS   B HG3  1 
ATOM   4035 H HD2  . LYS   B 1 11  ? 33.819 -27.355 -20.686 1.00 37.60 ?  11  LYS   B HD2  1 
ATOM   4036 H HD3  . LYS   B 1 11  ? 32.704 -28.405 -20.253 1.00 37.60 ?  11  LYS   B HD3  1 
ATOM   4037 H HE2  . LYS   B 1 11  ? 31.637 -26.415 -20.620 1.00 40.25 ?  11  LYS   B HE2  1 
ATOM   4038 H HE3  . LYS   B 1 11  ? 31.638 -26.652 -19.046 1.00 40.25 ?  11  LYS   B HE3  1 
ATOM   4039 H HZ1  . LYS   B 1 11  ? 32.266 -24.517 -19.566 1.00 41.95 ?  11  LYS   B HZ1  1 
ATOM   4040 H HZ2  . LYS   B 1 11  ? 33.356 -25.184 -18.885 1.00 41.95 ?  11  LYS   B HZ2  1 
ATOM   4041 H HZ3  . LYS   B 1 11  ? 33.405 -24.998 -20.321 1.00 41.95 ?  11  LYS   B HZ3  1 
ATOM   4042 N N    . LEU   B 1 12  ? 34.662 -29.778 -15.674 1.00 18.50 ?  12  LEU   B N    1 
ATOM   4043 C CA   . LEU   B 1 12  ? 33.702 -30.487 -14.832 1.00 18.04 ?  12  LEU   B CA   1 
ATOM   4044 C C    . LEU   B 1 12  ? 32.308 -29.881 -14.923 1.00 18.09 ?  12  LEU   B C    1 
ATOM   4045 O O    . LEU   B 1 12  ? 31.324 -30.601 -15.102 1.00 18.64 ?  12  LEU   B O    1 
ATOM   4046 C CB   . LEU   B 1 12  ? 34.161 -30.502 -13.369 1.00 17.52 ?  12  LEU   B CB   1 
ATOM   4047 C CG   . LEU   B 1 12  ? 35.496 -31.189 -13.094 1.00 17.58 ?  12  LEU   B CG   1 
ATOM   4048 C CD1  . LEU   B 1 12  ? 35.819 -31.132 -11.611 1.00 17.34 ?  12  LEU   B CD1  1 
ATOM   4049 C CD2  . LEU   B 1 12  ? 35.504 -32.630 -13.600 1.00 18.48 ?  12  LEU   B CD2  1 
ATOM   4050 H H    . LEU   B 1 12  ? 34.985 -29.069 -15.305 1.00 22.20 ?  12  LEU   B H    1 
ATOM   4051 H HA   . LEU   B 1 12  ? 33.638 -31.404 -15.138 1.00 21.65 ?  12  LEU   B HA   1 
ATOM   4052 H HB2  . LEU   B 1 12  ? 34.235 -29.586 -13.064 1.00 21.03 ?  12  LEU   B HB2  1 
ATOM   4053 H HB3  . LEU   B 1 12  ? 33.485 -30.963 -12.845 1.00 21.03 ?  12  LEU   B HB3  1 
ATOM   4054 H HG   . LEU   B 1 12  ? 36.194 -30.705 -13.563 1.00 21.09 ?  12  LEU   B HG   1 
ATOM   4055 H HD11 . LEU   B 1 12  ? 36.673 -31.571 -11.458 1.00 20.81 ?  12  LEU   B HD11 1 
ATOM   4056 H HD12 . LEU   B 1 12  ? 35.871 -30.205 -11.332 1.00 20.81 ?  12  LEU   B HD12 1 
ATOM   4057 H HD13 . LEU   B 1 12  ? 35.121 -31.590 -11.117 1.00 20.81 ?  12  LEU   B HD13 1 
ATOM   4058 H HD21 . LEU   B 1 12  ? 36.312 -33.066 -13.288 1.00 22.18 ?  12  LEU   B HD21 1 
ATOM   4059 H HD22 . LEU   B 1 12  ? 34.724 -33.087 -13.256 1.00 22.18 ?  12  LEU   B HD22 1 
ATOM   4060 H HD23 . LEU   B 1 12  ? 35.485 -32.621 -14.570 1.00 22.18 ?  12  LEU   B HD23 1 
ATOM   4061 N N    . THR   B 1 13  ? 32.213 -28.562 -14.800 1.00 18.12 ?  13  THR   B N    1 
ATOM   4062 C CA   . THR   B 1 13  ? 30.983 -27.813 -15.000 1.00 18.00 ?  13  THR   B CA   1 
ATOM   4063 C C    . THR   B 1 13  ? 31.310 -26.609 -15.876 1.00 19.76 ?  13  THR   B C    1 
ATOM   4064 O O    . THR   B 1 13  ? 32.454 -26.411 -16.296 1.00 20.75 ?  13  THR   B O    1 
ATOM   4065 C CB   . THR   B 1 13  ? 30.388 -27.345 -13.669 1.00 18.25 ?  13  THR   B CB   1 
ATOM   4066 O OG1  . THR   B 1 13  ? 31.223 -26.314 -13.127 1.00 17.85 ?  13  THR   B OG1  1 
ATOM   4067 C CG2  . THR   B 1 13  ? 30.287 -28.501 -12.675 1.00 18.60 ?  13  THR   B CG2  1 
ATOM   4068 H H    . THR   B 1 13  ? 32.881 -28.057 -14.595 1.00 21.75 ?  13  THR   B H    1 
ATOM   4069 H HA   . THR   B 1 13  ? 30.329 -28.373 -15.448 1.00 21.60 ?  13  THR   B HA   1 
ATOM   4070 H HB   . THR   B 1 13  ? 29.495 -26.992 -13.819 1.00 21.90 ?  13  THR   B HB   1 
ATOM   4071 H HG1  . THR   B 1 13  ? 30.888 -25.554 -13.294 1.00 21.43 ?  13  THR   B HG1  1 
ATOM   4072 H HG21 . THR   B 1 13  ? 29.770 -28.229 -11.901 1.00 22.32 ?  13  THR   B HG21 1 
ATOM   4073 H HG22 . THR   B 1 13  ? 29.853 -29.259 -13.093 1.00 22.32 ?  13  THR   B HG22 1 
ATOM   4074 H HG23 . THR   B 1 13  ? 31.175 -28.766 -12.384 1.00 22.32 ?  13  THR   B HG23 1 
ATOM   4075 N N    A ASP   B 1 14  ? 30.292 -25.791 -16.145 0.76 20.81 ?  14  ASP   B N    1 
ATOM   4076 N N    B ASP   B 1 14  ? 30.298 -25.778 -16.134 0.24 20.72 ?  14  ASP   B N    1 
ATOM   4077 C CA   A ASP   B 1 14  ? 30.501 -24.623 -16.993 0.76 22.44 ?  14  ASP   B CA   1 
ATOM   4078 C CA   B ASP   B 1 14  ? 30.498 -24.619 -16.998 0.24 21.50 ?  14  ASP   B CA   1 
ATOM   4079 C C    A ASP   B 1 14  ? 31.600 -23.714 -16.455 0.76 20.31 ?  14  ASP   B C    1 
ATOM   4080 C C    B ASP   B 1 14  ? 31.497 -23.621 -16.429 0.24 19.69 ?  14  ASP   B C    1 
ATOM   4081 O O    A ASP   B 1 14  ? 32.252 -23.009 -17.237 0.76 22.23 ?  14  ASP   B O    1 
ATOM   4082 O O    B ASP   B 1 14  ? 31.952 -22.739 -17.165 0.24 19.97 ?  14  ASP   B O    1 
ATOM   4083 C CB   A ASP   B 1 14  ? 29.192 -23.853 -17.155 0.76 26.19 ?  14  ASP   B CB   1 
ATOM   4084 C CB   B ASP   B 1 14  ? 29.170 -23.908 -17.256 0.24 23.89 ?  14  ASP   B CB   1 
ATOM   4085 C CG   A ASP   B 1 14  ? 28.239 -24.519 -18.121 0.76 30.16 ?  14  ASP   B CG   1 
ATOM   4086 C CG   B ASP   B 1 14  ? 28.300 -24.649 -18.255 0.24 26.02 ?  14  ASP   B CG   1 
ATOM   4087 O OD1  A ASP   B 1 14  ? 28.653 -25.464 -18.830 0.76 31.89 ?  14  ASP   B OD1  1 
ATOM   4088 O OD1  B ASP   B 1 14  ? 28.860 -25.321 -19.146 0.24 26.76 ?  14  ASP   B OD1  1 
ATOM   4089 O OD2  A ASP   B 1 14  ? 27.067 -24.097 -18.166 0.76 32.08 -1 14  ASP   B OD2  1 
ATOM   4090 O OD2  B ASP   B 1 14  ? 27.058 -24.564 -18.150 0.24 26.89 -1 14  ASP   B OD2  1 
ATOM   4091 H H    A ASP   B 1 14  ? 29.491 -25.879 -15.842 0.76 24.97 ?  14  ASP   B H    1 
ATOM   4092 H H    B ASP   B 1 14  ? 29.500 -25.860 -15.824 0.24 24.86 ?  14  ASP   B H    1 
ATOM   4093 H HA   A ASP   B 1 14  ? 30.780 -24.919 -17.869 0.76 26.93 ?  14  ASP   B HA   1 
ATOM   4094 H HA   B ASP   B 1 14  ? 30.838 -24.926 -17.852 0.24 25.81 ?  14  ASP   B HA   1 
ATOM   4095 H HB2  A ASP   B 1 14  ? 28.740 -23.799 -16.300 0.76 31.43 ?  14  ASP   B HB2  1 
ATOM   4096 H HB2  B ASP   B 1 14  ? 28.681 -23.842 -16.421 0.24 28.67 ?  14  ASP   B HB2  1 
ATOM   4097 H HB3  A ASP   B 1 14  ? 29.381 -22.963 -17.490 0.76 31.43 ?  14  ASP   B HB3  1 
ATOM   4098 H HB3  B ASP   B 1 14  ? 29.356 -23.016 -17.600 0.24 28.67 ?  14  ASP   B HB3  1 
ATOM   4099 N N    . ASN   B 1 15  ? 31.830 -23.716 -15.139 1.00 17.89 ?  15  ASN   B N    1 
ATOM   4100 C CA   . ASN   B 1 15  ? 32.791 -22.797 -14.535 1.00 15.66 ?  15  ASN   B CA   1 
ATOM   4101 C C    . ASN   B 1 15  ? 33.884 -23.446 -13.699 1.00 14.56 ?  15  ASN   B C    1 
ATOM   4102 O O    . ASN   B 1 15  ? 34.724 -22.714 -13.168 1.00 15.18 ?  15  ASN   B O    1 
ATOM   4103 C CB   . ASN   B 1 15  ? 32.080 -21.741 -13.677 1.00 16.04 ?  15  ASN   B CB   1 
ATOM   4104 C CG   . ASN   B 1 15  ? 31.445 -22.339 -12.441 1.00 15.68 ?  15  ASN   B CG   1 
ATOM   4105 O OD1  . ASN   B 1 15  ? 30.495 -23.129 -12.531 1.00 17.55 ?  15  ASN   B OD1  1 
ATOM   4106 N ND2  . ASN   B 1 15  ? 31.967 -21.984 -11.279 1.00 14.85 ?  15  ASN   B ND2  1 
ATOM   4107 H H    A ASN   B 1 15  ? 31.441 -24.242 -14.576 0.76 21.47 ?  15  ASN   B H    1 
ATOM   4108 H H    B ASN   B 1 15  ? 31.487 -24.283 -14.587 0.24 21.47 ?  15  ASN   B H    1 
ATOM   4109 H HA   . ASN   B 1 15  ? 33.239 -22.318 -15.240 1.00 18.79 ?  15  ASN   B HA   1 
ATOM   4110 H HB2  . ASN   B 1 15  ? 32.729 -21.068 -13.395 1.00 19.25 ?  15  ASN   B HB2  1 
ATOM   4111 H HB3  . ASN   B 1 15  ? 31.381 -21.314 -14.202 1.00 19.25 ?  15  ASN   B HB3  1 
ATOM   4112 H HD21 . ASN   B 1 15  ? 31.640 -22.293 -10.545 1.00 17.82 ?  15  ASN   B HD21 1 
ATOM   4113 H HD22 . ASN   B 1 15  ? 32.639 -21.441 -11.248 1.00 17.82 ?  15  ASN   B HD22 1 
ATOM   4114 N N    . VAL   B 1 16  ? 33.907 -24.771 -13.557 1.00 14.37 ?  16  VAL   B N    1 
ATOM   4115 C CA   . VAL   B 1 16  ? 34.906 -25.462 -12.747 1.00 14.11 ?  16  VAL   B CA   1 
ATOM   4116 C C    . VAL   B 1 16  ? 35.697 -26.401 -13.644 1.00 14.42 ?  16  VAL   B C    1 
ATOM   4117 O O    . VAL   B 1 16  ? 35.116 -27.271 -14.310 1.00 15.35 ?  16  VAL   B O    1 
ATOM   4118 C CB   . VAL   B 1 16  ? 34.276 -26.225 -11.567 1.00 14.59 ?  16  VAL   B CB   1 
ATOM   4119 C CG1  . VAL   B 1 16  ? 35.357 -26.952 -10.765 1.00 14.18 ?  16  VAL   B CG1  1 
ATOM   4120 C CG2  . VAL   B 1 16  ? 33.478 -25.277 -10.675 1.00 15.44 ?  16  VAL   B CG2  1 
ATOM   4121 H H    . VAL   B 1 16  ? 33.335 -25.304 -13.920 1.00 17.25 ?  16  VAL   B H    1 
ATOM   4122 H HA   . VAL   B 1 16  ? 35.523 -24.809 -12.377 1.00 16.93 ?  16  VAL   B HA   1 
ATOM   4123 H HB   . VAL   B 1 16  ? 33.668 -26.896 -11.915 1.00 17.51 ?  16  VAL   B HB   1 
ATOM   4124 H HG11 . VAL   B 1 16  ? 34.972 -27.260 -9.928  1.00 17.02 ?  16  VAL   B HG11 1 
ATOM   4125 H HG12 . VAL   B 1 16  ? 35.683 -27.707 -11.276 1.00 17.02 ?  16  VAL   B HG12 1 
ATOM   4126 H HG13 . VAL   B 1 16  ? 36.083 -26.333 -10.583 1.00 17.02 ?  16  VAL   B HG13 1 
ATOM   4127 H HG21 . VAL   B 1 16  ? 33.139 -25.771 -9.913  1.00 18.52 ?  16  VAL   B HG21 1 
ATOM   4128 H HG22 . VAL   B 1 16  ? 34.057 -24.561 -10.378 1.00 18.52 ?  16  VAL   B HG22 1 
ATOM   4129 H HG23 . VAL   B 1 16  ? 32.738 -24.914 -11.189 1.00 18.52 ?  16  VAL   B HG23 1 
ATOM   4130 N N    . TYR   B 1 17  ? 37.022 -26.241 -13.622 1.00 14.77 ?  17  TYR   B N    1 
ATOM   4131 C CA   . TYR   B 1 17  ? 37.965 -26.995 -14.434 1.00 15.15 ?  17  TYR   B CA   1 
ATOM   4132 C C    . TYR   B 1 17  ? 39.015 -27.599 -13.514 1.00 14.30 ?  17  TYR   B C    1 
ATOM   4133 O O    . TYR   B 1 17  ? 39.286 -27.068 -12.434 1.00 14.94 ?  17  TYR   B O    1 
ATOM   4134 C CB   . TYR   B 1 17  ? 38.677 -26.070 -15.431 1.00 17.43 ?  17  TYR   B CB   1 
ATOM   4135 C CG   . TYR   B 1 17  ? 37.753 -25.295 -16.336 1.00 20.55 ?  17  TYR   B CG   1 
ATOM   4136 C CD1  . TYR   B 1 17  ? 37.157 -24.111 -15.916 1.00 21.72 ?  17  TYR   B CD1  1 
ATOM   4137 C CD2  . TYR   B 1 17  ? 37.475 -25.748 -17.617 1.00 22.76 ?  17  TYR   B CD2  1 
ATOM   4138 C CE1  . TYR   B 1 17  ? 36.305 -23.399 -16.749 1.00 23.79 ?  17  TYR   B CE1  1 
ATOM   4139 C CE2  . TYR   B 1 17  ? 36.630 -25.045 -18.458 1.00 24.21 ?  17  TYR   B CE2  1 
ATOM   4140 C CZ   . TYR   B 1 17  ? 36.046 -23.874 -18.019 1.00 24.80 ?  17  TYR   B CZ   1 
ATOM   4141 O OH   . TYR   B 1 17  ? 35.207 -23.176 -18.856 1.00 26.42 ?  17  TYR   B OH   1 
ATOM   4142 H H    . TYR   B 1 17  ? 37.423 -25.666 -13.114 1.00 17.72 ?  17  TYR   B H    1 
ATOM   4143 H HA   . TYR   B 1 17  ? 37.505 -27.702 -14.918 1.00 18.18 ?  17  TYR   B HA   1 
ATOM   4144 H HB2  . TYR   B 1 17  ? 39.217 -25.432 -14.941 1.00 20.92 ?  17  TYR   B HB2  1 
ATOM   4145 H HB3  . TYR   B 1 17  ? 39.242 -26.611 -16.000 1.00 20.92 ?  17  TYR   B HB3  1 
ATOM   4146 H HD1  . TYR   B 1 17  ? 37.329 -23.789 -15.062 1.00 26.07 ?  17  TYR   B HD1  1 
ATOM   4147 H HD2  . TYR   B 1 17  ? 37.861 -26.536 -17.919 1.00 27.32 ?  17  TYR   B HD2  1 
ATOM   4148 H HE1  . TYR   B 1 17  ? 35.911 -22.607 -16.457 1.00 28.54 ?  17  TYR   B HE1  1 
ATOM   4149 H HE2  . TYR   B 1 17  ? 36.449 -25.364 -19.315 1.00 29.05 ?  17  TYR   B HE2  1 
ATOM   4150 H HH   . TYR   B 1 17  ? 35.132 -23.573 -19.592 1.00 31.70 ?  17  TYR   B HH   1 
ATOM   4151 N N    . ILE   B 1 18  ? 39.635 -28.701 -13.949 1.00 14.39 ?  18  ILE   B N    1 
ATOM   4152 C CA   . ILE   B 1 18  ? 40.567 -29.423 -13.088 1.00 14.16 ?  18  ILE   B CA   1 
ATOM   4153 C C    . ILE   B 1 18  ? 41.729 -29.977 -13.905 1.00 14.77 ?  18  ILE   B C    1 
ATOM   4154 O O    . ILE   B 1 18  ? 41.571 -30.372 -15.065 1.00 15.90 ?  18  ILE   B O    1 
ATOM   4155 C CB   . ILE   B 1 18  ? 39.814 -30.527 -12.295 1.00 14.69 ?  18  ILE   B CB   1 
ATOM   4156 C CG1  . ILE   B 1 18  ? 40.668 -31.074 -11.147 1.00 15.21 ?  18  ILE   B CG1  1 
ATOM   4157 C CG2  . ILE   B 1 18  ? 39.316 -31.643 -13.221 1.00 15.14 ?  18  ILE   B CG2  1 
ATOM   4158 C CD1  . ILE   B 1 18  ? 39.862 -31.898 -10.146 1.00 16.87 ?  18  ILE   B CD1  1 
ATOM   4159 H H    . ILE   B 1 18  ? 39.540 -29.044 -14.731 1.00 17.26 ?  18  ILE   B H    1 
ATOM   4160 H HA   . ILE   B 1 18  ? 40.931 -28.806 -12.436 1.00 16.99 ?  18  ILE   B HA   1 
ATOM   4161 H HB   . ILE   B 1 18  ? 39.032 -30.121 -11.890 1.00 17.63 ?  18  ILE   B HB   1 
ATOM   4162 H HG12 . ILE   B 1 18  ? 41.365 -31.640 -11.507 1.00 18.25 ?  18  ILE   B HG12 1 
ATOM   4163 H HG13 . ILE   B 1 18  ? 41.063 -30.328 -10.663 1.00 18.25 ?  18  ILE   B HG13 1 
ATOM   4164 H HG21 . ILE   B 1 18  ? 38.724 -32.230 -12.722 1.00 18.17 ?  18  ILE   B HG21 1 
ATOM   4165 H HG22 . ILE   B 1 18  ? 38.834 -31.241 -13.959 1.00 18.17 ?  18  ILE   B HG22 1 
ATOM   4166 H HG23 . ILE   B 1 18  ? 40.076 -32.144 -13.552 1.00 18.17 ?  18  ILE   B HG23 1 
ATOM   4167 H HD11 . ILE   B 1 18  ? 40.443 -32.171 -9.417  1.00 20.24 ?  18  ILE   B HD11 1 
ATOM   4168 H HD12 . ILE   B 1 18  ? 39.133 -31.359 -9.803  1.00 20.24 ?  18  ILE   B HD12 1 
ATOM   4169 H HD13 . ILE   B 1 18  ? 39.509 -32.683 -10.596 1.00 20.24 ?  18  ILE   B HD13 1 
ATOM   4170 N N    . LYS   B 1 19  ? 42.908 -30.017 -13.279 1.00 15.29 ?  19  LYS   B N    1 
ATOM   4171 C CA   . LYS   B 1 19  ? 44.122 -30.490 -13.930 1.00 15.63 ?  19  LYS   B CA   1 
ATOM   4172 C C    . LYS   B 1 19  ? 45.011 -31.173 -12.902 1.00 15.57 ?  19  LYS   B C    1 
ATOM   4173 O O    . LYS   B 1 19  ? 45.095 -30.735 -11.751 1.00 15.20 ?  19  LYS   B O    1 
ATOM   4174 C CB   . LYS   B 1 19  ? 44.894 -29.318 -14.559 1.00 16.97 ?  19  LYS   B CB   1 
ATOM   4175 C CG   . LYS   B 1 19  ? 46.094 -29.721 -15.401 1.00 19.14 ?  19  LYS   B CG   1 
ATOM   4176 C CD   . LYS   B 1 19  ? 46.815 -28.484 -15.930 1.00 21.11 ?  19  LYS   B CD   1 
ATOM   4177 C CE   . LYS   B 1 19  ? 47.971 -28.852 -16.842 1.00 22.97 ?  19  LYS   B CE   1 
ATOM   4178 N NZ   . LYS   B 1 19  ? 48.758 -27.666 -17.269 1.00 24.42 ?  19  LYS   B NZ   1 
ATOM   4179 H H    . LYS   B 1 19  ? 43.023 -29.766 -12.460 1.00 18.34 ?  19  LYS   B H    1 
ATOM   4180 H HA   . LYS   B 1 19  ? 43.890 -31.128 -14.623 1.00 18.76 ?  19  LYS   B HA   1 
ATOM   4181 H HB2  . LYS   B 1 19  ? 44.285 -28.825 -15.131 1.00 20.37 ?  19  LYS   B HB2  1 
ATOM   4182 H HB3  . LYS   B 1 19  ? 45.207 -28.740 -13.844 1.00 20.37 ?  19  LYS   B HB3  1 
ATOM   4183 H HG2  . LYS   B 1 19  ? 46.712 -30.231 -14.857 1.00 22.96 ?  19  LYS   B HG2  1 
ATOM   4184 H HG3  . LYS   B 1 19  ? 45.790 -30.249 -16.157 1.00 22.96 ?  19  LYS   B HG3  1 
ATOM   4185 H HD2  . LYS   B 1 19  ? 46.189 -27.940 -16.434 1.00 25.33 ?  19  LYS   B HD2  1 
ATOM   4186 H HD3  . LYS   B 1 19  ? 47.168 -27.977 -15.180 1.00 25.33 ?  19  LYS   B HD3  1 
ATOM   4187 H HE2  . LYS   B 1 19  ? 48.564 -29.457 -16.370 1.00 27.56 ?  19  LYS   B HE2  1 
ATOM   4188 H HE3  . LYS   B 1 19  ? 47.618 -29.286 -17.636 1.00 27.56 ?  19  LYS   B HE3  1 
ATOM   4189 H HZ1  . LYS   B 1 19  ? 49.390 -27.913 -17.846 1.00 29.30 ?  19  LYS   B HZ1  1 
ATOM   4190 H HZ2  . LYS   B 1 19  ? 48.224 -27.072 -17.663 1.00 29.30 ?  19  LYS   B HZ2  1 
ATOM   4191 H HZ3  . LYS   B 1 19  ? 49.143 -27.286 -16.564 1.00 29.30 ?  19  LYS   B HZ3  1 
ATOM   4192 N N    . ASN   B 1 20  ? 45.699 -32.227 -13.333 1.00 16.81 ?  20  ASN   B N    1 
ATOM   4193 C CA   . ASN   B 1 20  ? 46.734 -32.850 -12.517 1.00 17.71 ?  20  ASN   B CA   1 
ATOM   4194 C C    . ASN   B 1 20  ? 48.002 -32.028 -12.706 1.00 18.18 ?  20  ASN   B C    1 
ATOM   4195 O O    . ASN   B 1 20  ? 48.634 -32.092 -13.768 1.00 20.45 ?  20  ASN   B O    1 
ATOM   4196 C CB   . ASN   B 1 20  ? 46.913 -34.300 -12.963 1.00 19.20 ?  20  ASN   B CB   1 
ATOM   4197 C CG   . ASN   B 1 20  ? 48.069 -35.012 -12.272 1.00 20.59 ?  20  ASN   B CG   1 
ATOM   4198 O OD1  . ASN   B 1 20  ? 48.736 -35.862 -12.876 1.00 23.21 ?  20  ASN   B OD1  1 
ATOM   4199 N ND2  . ASN   B 1 20  ? 48.301 -34.691 -11.009 1.00 20.06 ?  20  ASN   B ND2  1 
ATOM   4200 H H    . ASN   B 1 20  ? 45.588 -32.596 -14.100 1.00 20.17 ?  20  ASN   B H    1 
ATOM   4201 H HA   . ASN   B 1 20  ? 46.461 -32.834 -11.582 1.00 21.26 ?  20  ASN   B HA   1 
ATOM   4202 H HB2  . ASN   B 1 20  ? 46.100 -34.792 -12.765 1.00 23.04 ?  20  ASN   B HB2  1 
ATOM   4203 H HB3  . ASN   B 1 20  ? 47.080 -34.310 -13.917 1.00 23.04 ?  20  ASN   B HB3  1 
ATOM   4204 H HD21 . ASN   B 1 20  ? 48.946 -35.062 -10.583 1.00 24.07 ?  20  ASN   B HD21 1 
ATOM   4205 H HD22 . ASN   B 1 20  ? 47.812 -34.099 -10.611 1.00 24.07 ?  20  ASN   B HD22 1 
ATOM   4206 N N    . ALA   B 1 21  ? 48.361 -31.234 -11.696 1.00 17.68 ?  21  ALA   B N    1 
ATOM   4207 C CA   . ALA   B 1 21  ? 49.461 -30.293 -11.845 1.00 19.10 ?  21  ALA   B CA   1 
ATOM   4208 C C    . ALA   B 1 21  ? 49.924 -29.805 -10.480 1.00 17.95 ?  21  ALA   B C    1 
ATOM   4209 O O    . ALA   B 1 21  ? 49.181 -29.835 -9.496  1.00 17.55 ?  21  ALA   B O    1 
ATOM   4210 C CB   . ALA   B 1 21  ? 49.052 -29.106 -12.716 1.00 20.51 ?  21  ALA   B CB   1 
ATOM   4211 H H    . ALA   B 1 21  ? 47.983 -31.226 -10.916 1.00 21.22 ?  21  ALA   B H    1 
ATOM   4212 H HA   . ALA   B 1 21  ? 50.205 -30.746 -12.269 1.00 22.92 ?  21  ALA   B HA   1 
ATOM   4213 H HB1  . ALA   B 1 21  ? 49.828 -28.550 -12.855 1.00 24.61 ?  21  ALA   B HB1  1 
ATOM   4214 H HB2  . ALA   B 1 21  ? 48.725 -29.446 -13.562 1.00 24.61 ?  21  ALA   B HB2  1 
ATOM   4215 H HB3  . ALA   B 1 21  ? 48.353 -28.612 -12.262 1.00 24.61 ?  21  ALA   B HB3  1 
ATOM   4216 N N    . ASP   B 1 22  ? 51.180 -29.359 -10.455 1.00 17.09 ?  22  ASP   B N    1 
ATOM   4217 C CA   . ASP   B 1 22  ? 51.790 -28.659 -9.328  1.00 16.36 ?  22  ASP   B CA   1 
ATOM   4218 C C    . ASP   B 1 22  ? 51.381 -27.189 -9.413  1.00 15.02 ?  22  ASP   B C    1 
ATOM   4219 O O    . ASP   B 1 22  ? 51.696 -26.512 -10.397 1.00 15.39 ?  22  ASP   B O    1 
ATOM   4220 C CB   . ASP   B 1 22  ? 53.308 -28.840 -9.474  1.00 17.96 ?  22  ASP   B CB   1 
ATOM   4221 C CG   . ASP   B 1 22  ? 54.136 -28.078 -8.445  1.00 19.87 ?  22  ASP   B CG   1 
ATOM   4222 O OD1  . ASP   B 1 22  ? 53.777 -26.955 -8.056  1.00 19.68 ?  22  ASP   B OD1  1 
ATOM   4223 O OD2  . ASP   B 1 22  ? 55.203 -28.601 -8.052  1.00 22.21 -1 22  ASP   B OD2  1 
ATOM   4224 H H    . ASP   B 1 22  ? 51.725 -29.453 -11.117 1.00 20.51 ?  22  ASP   B H    1 
ATOM   4225 H HA   . ASP   B 1 22  ? 51.493 -29.043 -8.483  1.00 19.63 ?  22  ASP   B HA   1 
ATOM   4226 H HB2  . ASP   B 1 22  ? 53.526 -29.778 -9.385  1.00 21.55 ?  22  ASP   B HB2  1 
ATOM   4227 H HB3  . ASP   B 1 22  ? 53.577 -28.516 -10.346 1.00 21.55 ?  22  ASP   B HB3  1 
ATOM   4228 N N    . ILE   B 1 23  ? 50.667 -26.698 -8.393  1.00 14.24 ?  23  ILE   B N    1 
ATOM   4229 C CA   . ILE   B 1 23  ? 50.080 -25.356 -8.463  1.00 13.51 ?  23  ILE   B CA   1 
ATOM   4230 C C    . ILE   B 1 23  ? 51.135 -24.265 -8.608  1.00 13.39 ?  23  ILE   B C    1 
ATOM   4231 O O    . ILE   B 1 23  ? 50.865 -23.220 -9.214  1.00 13.19 ?  23  ILE   B O    1 
ATOM   4232 C CB   . ILE   B 1 23  ? 49.143 -25.112 -7.265  1.00 14.12 ?  23  ILE   B CB   1 
ATOM   4233 C CG1  . ILE   B 1 23  ? 48.310 -23.845 -7.474  1.00 14.97 ?  23  ILE   B CG1  1 
ATOM   4234 C CG2  . ILE   B 1 23  ? 49.908 -25.074 -5.966  1.00 15.40 ?  23  ILE   B CG2  1 
ATOM   4235 C CD1  . ILE   B 1 23  ? 47.194 -23.680 -6.460  1.00 15.68 ?  23  ILE   B CD1  1 
ATOM   4236 H H    . ILE   B 1 23  ? 50.515 -27.117 -7.656  1.00 17.08 ?  23  ILE   B H    1 
ATOM   4237 H HA   . ILE   B 1 23  ? 49.531 -25.320 -9.260  1.00 16.21 ?  23  ILE   B HA   1 
ATOM   4238 H HB   . ILE   B 1 23  ? 48.527 -25.859 -7.222  1.00 16.94 ?  23  ILE   B HB   1 
ATOM   4239 H HG12 . ILE   B 1 23  ? 48.895 -23.071 -7.404  1.00 17.96 ?  23  ILE   B HG12 1 
ATOM   4240 H HG13 . ILE   B 1 23  ? 47.912 -23.873 -8.360  1.00 17.96 ?  23  ILE   B HG13 1 
ATOM   4241 H HG21 . ILE   B 1 23  ? 49.278 -25.071 -5.231  1.00 18.48 ?  23  ILE   B HG21 1 
ATOM   4242 H HG22 . ILE   B 1 23  ? 50.476 -25.858 -5.914  1.00 18.48 ?  23  ILE   B HG22 1 
ATOM   4243 H HG23 . ILE   B 1 23  ? 50.451 -24.270 -5.944  1.00 18.48 ?  23  ILE   B HG23 1 
ATOM   4244 H HD11 . ILE   B 1 23  ? 46.662 -22.908 -6.703  1.00 18.81 ?  23  ILE   B HD11 1 
ATOM   4245 H HD12 . ILE   B 1 23  ? 46.645 -24.480 -6.471  1.00 18.81 ?  23  ILE   B HD12 1 
ATOM   4246 H HD13 . ILE   B 1 23  ? 47.583 -23.557 -5.583  1.00 18.81 ?  23  ILE   B HD13 1 
ATOM   4247 N N    . VAL   B 1 24  ? 52.332 -24.468 -8.048  1.00 13.71 ?  24  VAL   B N    1 
ATOM   4248 C CA   . VAL   B 1 24  ? 53.407 -23.488 -8.210  1.00 14.44 ?  24  VAL   B CA   1 
ATOM   4249 C C    . VAL   B 1 24  ? 53.859 -23.439 -9.662  1.00 14.94 ?  24  VAL   B C    1 
ATOM   4250 O O    . VAL   B 1 24  ? 54.001 -22.362 -10.257 1.00 15.13 ?  24  VAL   B O    1 
ATOM   4251 C CB   . VAL   B 1 24  ? 54.585 -23.815 -7.268  1.00 15.39 ?  24  VAL   B CB   1 
ATOM   4252 C CG1  . VAL   B 1 24  ? 55.799 -22.939 -7.594  1.00 16.52 ?  24  VAL   B CG1  1 
ATOM   4253 C CG2  . VAL   B 1 24  ? 54.175 -23.626 -5.829  1.00 16.62 ?  24  VAL   B CG2  1 
ATOM   4254 H H    . VAL   B 1 24  ? 52.545 -25.155 -7.576  1.00 16.45 ?  24  VAL   B H    1 
ATOM   4255 H HA   . VAL   B 1 24  ? 53.074 -22.612 -7.972  1.00 17.33 ?  24  VAL   B HA   1 
ATOM   4256 H HB   . VAL   B 1 24  ? 54.843 -24.743 -7.383  1.00 18.47 ?  24  VAL   B HB   1 
ATOM   4257 H HG11 . VAL   B 1 24  ? 56.395 -22.929 -6.829  1.00 19.83 ?  24  VAL   B HG11 1 
ATOM   4258 H HG12 . VAL   B 1 24  ? 56.255 -23.308 -8.364  1.00 19.83 ?  24  VAL   B HG12 1 
ATOM   4259 H HG13 . VAL   B 1 24  ? 55.494 -22.037 -7.785  1.00 19.83 ?  24  VAL   B HG13 1 
ATOM   4260 H HG21 . VAL   B 1 24  ? 54.891 -23.930 -5.252  1.00 19.94 ?  24  VAL   B HG21 1 
ATOM   4261 H HG22 . VAL   B 1 24  ? 54.002 -22.683 -5.674  1.00 19.94 ?  24  VAL   B HG22 1 
ATOM   4262 H HG23 . VAL   B 1 24  ? 53.370 -24.142 -5.659  1.00 19.94 ?  24  VAL   B HG23 1 
ATOM   4263 N N    . GLU   B 1 25  ? 54.115 -24.613 -10.250 1.00 15.73 ?  25  GLU   B N    1 
ATOM   4264 C CA   . GLU   B 1 25  ? 54.506 -24.653 -11.652 1.00 17.09 ?  25  GLU   B CA   1 
ATOM   4265 C C    . GLU   B 1 25  ? 53.400 -24.104 -12.540 1.00 15.83 ?  25  GLU   B C    1 
ATOM   4266 O O    . GLU   B 1 25  ? 53.672 -23.391 -13.515 1.00 16.93 ?  25  GLU   B O    1 
ATOM   4267 C CB   . GLU   B 1 25  ? 54.902 -26.075 -12.048 1.00 20.79 ?  25  GLU   B CB   1 
ATOM   4268 C CG   . GLU   B 1 25  ? 56.202 -26.523 -11.396 1.00 25.93 ?  25  GLU   B CG   1 
ATOM   4269 C CD   . GLU   B 1 25  ? 57.313 -25.487 -11.501 1.00 30.98 ?  25  GLU   B CD   1 
ATOM   4270 O OE1  . GLU   B 1 25  ? 57.696 -25.137 -12.637 1.00 32.95 ?  25  GLU   B OE1  1 
ATOM   4271 O OE2  . GLU   B 1 25  ? 57.792 -25.006 -10.446 1.00 32.90 -1 25  GLU   B OE2  1 
ATOM   4272 H H    . GLU   B 1 25  ? 54.067 -25.381 -9.863  1.00 18.88 ?  25  GLU   B H    1 
ATOM   4273 H HA   . GLU   B 1 25  ? 55.264 -24.070 -11.778 1.00 20.51 ?  25  GLU   B HA   1 
ATOM   4274 H HB2  . GLU   B 1 25  ? 54.201 -26.690 -11.770 1.00 24.95 ?  25  GLU   B HB2  1 
ATOM   4275 H HB3  . GLU   B 1 25  ? 55.013 -26.117 -13.011 1.00 24.95 ?  25  GLU   B HB3  1 
ATOM   4276 H HG2  . GLU   B 1 25  ? 56.048 -26.676 -10.457 1.00 31.12 ?  25  GLU   B HG2  1 
ATOM   4277 H HG3  . GLU   B 1 25  ? 56.508 -27.333 -11.830 1.00 31.12 ?  25  GLU   B HG3  1 
ATOM   4278 N N    . GLU   B 1 26  ? 52.144 -24.414 -12.207 1.00 14.91 ?  26  GLU   B N    1 
ATOM   4279 C CA   . GLU   B 1 26  ? 51.021 -23.882 -12.971 1.00 15.65 ?  26  GLU   B CA   1 
ATOM   4280 C C    . GLU   B 1 26  ? 50.977 -22.366 -12.891 1.00 14.48 ?  26  GLU   B C    1 
ATOM   4281 O O    . GLU   B 1 26  ? 50.766 -21.692 -13.902 1.00 15.59 ?  26  GLU   B O    1 
ATOM   4282 C CB   . GLU   B 1 26  ? 49.701 -24.466 -12.458 1.00 17.98 ?  26  GLU   B CB   1 
ATOM   4283 C CG   . GLU   B 1 26  ? 49.273 -25.751 -13.130 1.00 21.53 ?  26  GLU   B CG   1 
ATOM   4284 C CD   . GLU   B 1 26  ? 49.040 -25.608 -14.633 1.00 23.32 ?  26  GLU   B CD   1 
ATOM   4285 O OE1  . GLU   B 1 26  ? 48.069 -24.947 -15.064 1.00 23.46 ?  26  GLU   B OE1  1 
ATOM   4286 O OE2  . GLU   B 1 26  ? 49.832 -26.191 -15.381 1.00 25.42 -1 26  GLU   B OE2  1 
ATOM   4287 H H    . GLU   B 1 26  ? 51.914 -24.930 -11.550 1.00 17.90 ?  26  GLU   B H    1 
ATOM   4288 H HA   . GLU   B 1 26  ? 51.121 -24.132 -13.898 1.00 18.79 ?  26  GLU   B HA   1 
ATOM   4289 H HB2  . GLU   B 1 26  ? 49.784 -24.647 -11.506 1.00 21.58 ?  26  GLU   B HB2  1 
ATOM   4290 H HB3  . GLU   B 1 26  ? 48.994 -23.811 -12.598 1.00 21.58 ?  26  GLU   B HB3  1 
ATOM   4291 H HG2  . GLU   B 1 26  ? 49.973 -26.402 -13.010 1.00 25.84 ?  26  GLU   B HG2  1 
ATOM   4292 H HG3  . GLU   B 1 26  ? 48.447 -26.058 -12.723 1.00 25.84 ?  26  GLU   B HG3  1 
ATOM   4293 N N    . ALA   B 1 27  ? 51.133 -21.814 -11.686 1.00 13.91 ?  27  ALA   B N    1 
ATOM   4294 C CA   . ALA   B 1 27  ? 51.091 -20.363 -11.540 1.00 14.21 ?  27  ALA   B CA   1 
ATOM   4295 C C    . ALA   B 1 27  ? 52.163 -19.695 -12.392 1.00 15.24 ?  27  ALA   B C    1 
ATOM   4296 O O    . ALA   B 1 27  ? 51.901 -18.686 -13.063 1.00 16.10 ?  27  ALA   B O    1 
ATOM   4297 C CB   . ALA   B 1 27  ? 51.235 -19.983 -10.069 1.00 14.75 ?  27  ALA   B CB   1 
ATOM   4298 H H    . ALA   B 1 27  ? 51.258 -22.249 -10.950 1.00 16.69 ?  27  ALA   B H    1 
ATOM   4299 H HA   . ALA   B 1 27  ? 50.230 -20.044 -11.843 1.00 17.06 ?  27  ALA   B HA   1 
ATOM   4300 H HB1  . ALA   B 1 27  ? 51.197 -19.015 -9.988  1.00 17.71 ?  27  ALA   B HB1  1 
ATOM   4301 H HB2  . ALA   B 1 27  ? 50.504 -20.381 -9.566  1.00 17.71 ?  27  ALA   B HB2  1 
ATOM   4302 H HB3  . ALA   B 1 27  ? 52.082 -20.310 -9.735  1.00 17.71 ?  27  ALA   B HB3  1 
ATOM   4303 N N    . LYS   B 1 28  ? 53.375 -20.252 -12.393 1.00 16.87 ?  28  LYS   B N    1 
ATOM   4304 C CA   . LYS   B 1 28  ? 54.448 -19.635 -13.162 1.00 18.92 ?  28  LYS   B CA   1 
ATOM   4305 C C    . LYS   B 1 28  ? 54.186 -19.712 -14.663 1.00 19.76 ?  28  LYS   B C    1 
ATOM   4306 O O    . LYS   B 1 28  ? 54.593 -18.812 -15.407 1.00 20.99 ?  28  LYS   B O    1 
ATOM   4307 C CB   . LYS   B 1 28  ? 55.798 -20.243 -12.772 1.00 21.73 ?  28  LYS   B CB   1 
ATOM   4308 C CG   . LYS   B 1 28  ? 56.205 -19.899 -11.341 1.00 25.06 ?  28  LYS   B CG   1 
ATOM   4309 C CD   . LYS   B 1 28  ? 57.642 -20.287 -11.020 1.00 28.40 ?  28  LYS   B CD   1 
ATOM   4310 C CE   . LYS   B 1 28  ? 57.751 -21.732 -10.601 1.00 31.12 ?  28  LYS   B CE   1 
ATOM   4311 N NZ   . LYS   B 1 28  ? 59.102 -22.031 -10.047 1.00 34.90 ?  28  LYS   B NZ   1 
ATOM   4312 H H    . LYS   B 1 28  ? 53.596 -20.966 -11.966 1.00 20.25 ?  28  LYS   B H    1 
ATOM   4313 H HA   . LYS   B 1 28  ? 54.486 -18.695 -12.933 1.00 22.70 ?  28  LYS   B HA   1 
ATOM   4314 H HB2  . LYS   B 1 28  ? 55.750 -21.207 -12.842 1.00 26.08 ?  28  LYS   B HB2  1 
ATOM   4315 H HB3  . LYS   B 1 28  ? 56.486 -19.899 -13.365 1.00 26.08 ?  28  LYS   B HB3  1 
ATOM   4316 H HG2  . LYS   B 1 28  ? 56.118 -18.940 -11.212 1.00 30.08 ?  28  LYS   B HG2  1 
ATOM   4317 H HG3  . LYS   B 1 28  ? 55.622 -20.369 -10.727 1.00 30.08 ?  28  LYS   B HG3  1 
ATOM   4318 H HD2  . LYS   B 1 28  ? 58.190 -20.155 -11.809 1.00 34.08 ?  28  LYS   B HD2  1 
ATOM   4319 H HD3  . LYS   B 1 28  ? 57.964 -19.732 -10.292 1.00 34.08 ?  28  LYS   B HD3  1 
ATOM   4320 H HE2  . LYS   B 1 28  ? 57.091 -21.918 -9.914  1.00 37.34 ?  28  LYS   B HE2  1 
ATOM   4321 H HE3  . LYS   B 1 28  ? 57.602 -22.303 -11.372 1.00 37.34 ?  28  LYS   B HE3  1 
ATOM   4322 H HZ1  . LYS   B 1 28  ? 59.149 -22.886 -9.805  1.00 41.88 ?  28  LYS   B HZ1  1 
ATOM   4323 H HZ2  . LYS   B 1 28  ? 59.724 -21.869 -10.662 1.00 41.88 ?  28  LYS   B HZ2  1 
ATOM   4324 H HZ3  . LYS   B 1 28  ? 59.257 -21.520 -9.335  1.00 41.88 ?  28  LYS   B HZ3  1 
ATOM   4325 N N    . LYS   B 1 29  ? 53.490 -20.756 -15.119 1.00 20.70 ?  29  LYS   B N    1 
ATOM   4326 C CA   . LYS   B 1 29  ? 53.204 -20.904 -16.543 1.00 23.38 ?  29  LYS   B CA   1 
ATOM   4327 C C    . LYS   B 1 29  ? 51.965 -20.125 -16.972 1.00 22.49 ?  29  LYS   B C    1 
ATOM   4328 O O    . LYS   B 1 29  ? 51.973 -19.487 -18.030 1.00 23.94 ?  29  LYS   B O    1 
ATOM   4329 C CB   . LYS   B 1 29  ? 53.035 -22.385 -16.887 1.00 27.67 ?  29  LYS   B CB   1 
ATOM   4330 C CG   . LYS   B 1 29  ? 52.904 -22.663 -18.375 1.00 31.67 ?  29  LYS   B CG   1 
ATOM   4331 C CD   . LYS   B 1 29  ? 53.199 -24.122 -18.707 1.00 34.87 ?  29  LYS   B CD   1 
ATOM   4332 C CE   . LYS   B 1 29  ? 52.166 -25.061 -18.107 1.00 36.72 ?  29  LYS   B CE   1 
ATOM   4333 N NZ   . LYS   B 1 29  ? 52.461 -26.488 -18.429 1.00 38.04 ?  29  LYS   B NZ   1 
ATOM   4334 H H    . LYS   B 1 29  ? 53.178 -21.387 -14.623 1.00 24.84 ?  29  LYS   B H    1 
ATOM   4335 H HA   . LYS   B 1 29  ? 53.954 -20.563 -17.048 1.00 28.06 ?  29  LYS   B HA   1 
ATOM   4336 H HB2  . LYS   B 1 29  ? 53.811 -22.869 -16.563 1.00 33.20 ?  29  LYS   B HB2  1 
ATOM   4337 H HB3  . LYS   B 1 29  ? 52.236 -22.719 -16.452 1.00 33.20 ?  29  LYS   B HB3  1 
ATOM   4338 H HG2  . LYS   B 1 29  ? 51.997 -22.466 -18.657 1.00 38.01 ?  29  LYS   B HG2  1 
ATOM   4339 H HG3  . LYS   B 1 29  ? 53.534 -22.108 -18.861 1.00 38.01 ?  29  LYS   B HG3  1 
ATOM   4340 H HD2  . LYS   B 1 29  ? 53.191 -24.239 -19.670 1.00 41.85 ?  29  LYS   B HD2  1 
ATOM   4341 H HD3  . LYS   B 1 29  ? 54.069 -24.362 -18.349 1.00 41.85 ?  29  LYS   B HD3  1 
ATOM   4342 H HE2  . LYS   B 1 29  ? 52.166 -24.964 -17.142 1.00 44.06 ?  29  LYS   B HE2  1 
ATOM   4343 H HE3  . LYS   B 1 29  ? 51.291 -24.844 -18.466 1.00 44.06 ?  29  LYS   B HE3  1 
ATOM   4344 H HZ1  . LYS   B 1 29  ? 51.842 -27.015 -18.067 1.00 45.65 ?  29  LYS   B HZ1  1 
ATOM   4345 H HZ2  . LYS   B 1 29  ? 52.462 -26.607 -19.311 1.00 45.65 ?  29  LYS   B HZ2  1 
ATOM   4346 H HZ3  . LYS   B 1 29  ? 53.259 -26.714 -18.106 1.00 45.65 ?  29  LYS   B HZ3  1 
ATOM   4347 N N    . VAL   B 1 30  ? 50.894 -20.184 -16.175 1.00 20.59 ?  30  VAL   B N    1 
ATOM   4348 C CA   . VAL   B 1 30  ? 49.604 -19.596 -16.547 1.00 20.64 ?  30  VAL   B CA   1 
ATOM   4349 C C    . VAL   B 1 30  ? 49.603 -18.083 -16.383 1.00 19.64 ?  30  VAL   B C    1 
ATOM   4350 O O    . VAL   B 1 30  ? 48.855 -17.372 -17.072 1.00 20.58 ?  30  VAL   B O    1 
ATOM   4351 C CB   . VAL   B 1 30  ? 48.502 -20.229 -15.674 1.00 21.94 ?  30  VAL   B CB   1 
ATOM   4352 C CG1  . VAL   B 1 30  ? 47.211 -19.425 -15.742 1.00 22.25 ?  30  VAL   B CG1  1 
ATOM   4353 C CG2  . VAL   B 1 30  ? 48.271 -21.683 -16.074 1.00 22.67 ?  30  VAL   B CG2  1 
ATOM   4354 H H    . VAL   B 1 30  ? 50.882 -20.584 -15.404 1.00 24.71 ?  30  VAL   B H    1 
ATOM   4355 H HA   . VAL   B 1 30  ? 49.409 -19.819 -17.472 1.00 24.77 ?  30  VAL   B HA   1 
ATOM   4356 H HB   . VAL   B 1 30  ? 48.796 -20.235 -14.749 1.00 26.32 ?  30  VAL   B HB   1 
ATOM   4357 H HG11 . VAL   B 1 30  ? 46.471 -20.012 -15.517 1.00 26.70 ?  30  VAL   B HG11 1 
ATOM   4358 H HG12 . VAL   B 1 30  ? 47.255 -18.698 -15.104 1.00 26.70 ?  30  VAL   B HG12 1 
ATOM   4359 H HG13 . VAL   B 1 30  ? 47.092 -19.089 -16.638 1.00 26.70 ?  30  VAL   B HG13 1 
ATOM   4360 H HG21 . VAL   B 1 30  ? 47.577 -22.066 -15.507 1.00 27.21 ?  30  VAL   B HG21 1 
ATOM   4361 H HG22 . VAL   B 1 30  ? 47.986 -21.716 -17.002 1.00 27.21 ?  30  VAL   B HG22 1 
ATOM   4362 H HG23 . VAL   B 1 30  ? 49.095 -22.180 -15.963 1.00 27.21 ?  30  VAL   B HG23 1 
ATOM   4363 N N    . LYS   B 1 31  ? 50.396 -17.583 -15.446 1.00 19.30 ?  31  LYS   B N    1 
ATOM   4364 C CA   . LYS   B 1 31  ? 50.409 -16.174 -15.081 1.00 19.97 ?  31  LYS   B CA   1 
ATOM   4365 C C    . LYS   B 1 31  ? 49.009 -15.685 -14.693 1.00 17.62 ?  31  LYS   B C    1 
ATOM   4366 O O    . LYS   B 1 31  ? 48.469 -14.768 -15.316 1.00 18.82 ?  31  LYS   B O    1 
ATOM   4367 C CB   . LYS   B 1 31  ? 51.018 -15.335 -16.197 1.00 23.29 ?  31  LYS   B CB   1 
ATOM   4368 C CG   . LYS   B 1 31  ? 52.451 -15.781 -16.547 1.00 26.63 ?  31  LYS   B CG   1 
ATOM   4369 C CD   . LYS   B 1 31  ? 53.025 -14.993 -17.704 1.00 29.07 ?  31  LYS   B CD   1 
ATOM   4370 C CE   . LYS   B 1 31  ? 54.504 -15.265 -17.864 1.00 31.39 ?  31  LYS   B CE   1 
ATOM   4371 N NZ   . LYS   B 1 31  ? 55.262 -14.852 -16.650 1.00 33.34 ?  31  LYS   B NZ   1 
ATOM   4372 H H    . LYS   B 1 31  ? 50.949 -18.065 -15.001 1.00 23.15 ?  31  LYS   B H    1 
ATOM   4373 H HA   . LYS   B 1 31  ? 50.966 -16.081 -14.308 1.00 23.97 ?  31  LYS   B HA   1 
ATOM   4374 H HB2  . LYS   B 1 31  ? 50.479 -15.418 -16.999 1.00 27.95 ?  31  LYS   B HB2  1 
ATOM   4375 H HB3  . LYS   B 1 31  ? 51.057 -14.414 -15.910 1.00 27.95 ?  31  LYS   B HB3  1 
ATOM   4376 H HG2  . LYS   B 1 31  ? 53.021 -15.651 -15.773 1.00 31.95 ?  31  LYS   B HG2  1 
ATOM   4377 H HG3  . LYS   B 1 31  ? 52.444 -16.722 -16.797 1.00 31.95 ?  31  LYS   B HG3  1 
ATOM   4378 H HD2  . LYS   B 1 31  ? 52.574 -15.255 -18.522 1.00 34.88 ?  31  LYS   B HD2  1 
ATOM   4379 H HD3  . LYS   B 1 31  ? 52.902 -14.048 -17.535 1.00 34.88 ?  31  LYS   B HD3  1 
ATOM   4380 H HE2  . LYS   B 1 31  ? 54.643 -16.216 -18.002 1.00 37.67 ?  31  LYS   B HE2  1 
ATOM   4381 H HE3  . LYS   B 1 31  ? 54.841 -14.762 -18.621 1.00 37.67 ?  31  LYS   B HE3  1 
ATOM   4382 H HZ1  . LYS   B 1 31  ? 56.136 -14.886 -16.811 1.00 40.01 ?  31  LYS   B HZ1  1 
ATOM   4383 H HZ2  . LYS   B 1 31  ? 55.041 -14.020 -16.423 1.00 40.01 ?  31  LYS   B HZ2  1 
ATOM   4384 H HZ3  . LYS   B 1 31  ? 55.071 -15.396 -15.971 1.00 40.01 ?  31  LYS   B HZ3  1 
ATOM   4385 N N    . PRO   B 1 32  ? 48.398 -16.283 -13.665 1.00 15.27 ?  32  PRO   B N    1 
ATOM   4386 C CA   . PRO   B 1 32  ? 47.017 -15.930 -13.314 1.00 14.19 ?  32  PRO   B CA   1 
ATOM   4387 C C    . PRO   B 1 32  ? 46.929 -14.589 -12.603 1.00 14.55 ?  32  PRO   B C    1 
ATOM   4388 O O    . PRO   B 1 32  ? 47.846 -14.166 -11.894 1.00 16.11 ?  32  PRO   B O    1 
ATOM   4389 C CB   . PRO   B 1 32  ? 46.618 -17.048 -12.345 1.00 14.58 ?  32  PRO   B CB   1 
ATOM   4390 C CG   . PRO   B 1 32  ? 47.922 -17.384 -11.661 1.00 14.78 ?  32  PRO   B CG   1 
ATOM   4391 C CD   . PRO   B 1 32  ? 48.966 -17.279 -12.733 1.00 15.25 ?  32  PRO   B CD   1 
ATOM   4392 H HA   . PRO   B 1 32  ? 46.440 -15.945 -14.099 1.00 17.02 ?  32  PRO   B HA   1 
ATOM   4393 H HB2  . PRO   B 1 32  ? 45.960 -16.719 -11.709 1.00 17.50 ?  32  PRO   B HB2  1 
ATOM   4394 H HB3  . PRO   B 1 32  ? 46.273 -17.813 -12.836 1.00 17.50 ?  32  PRO   B HB3  1 
ATOM   4395 H HG2  . PRO   B 1 32  ? 48.096 -16.738 -10.952 1.00 17.74 ?  32  PRO   B HG2  1 
ATOM   4396 H HG3  . PRO   B 1 32  ? 47.888 -18.282 -11.301 1.00 17.74 ?  32  PRO   B HG3  1 
ATOM   4397 H HD2  . PRO   B 1 32  ? 49.799 -16.954 -12.361 1.00 18.29 ?  32  PRO   B HD2  1 
ATOM   4398 H HD3  . PRO   B 1 32  ? 49.077 -18.133 -13.173 1.00 18.29 ?  32  PRO   B HD3  1 
ATOM   4399 N N    . THR   B 1 33  ? 45.777 -13.938 -12.773 1.00 14.16 ?  33  THR   B N    1 
ATOM   4400 C CA   . THR   B 1 33  ? 45.483 -12.759 -11.968 1.00 14.49 ?  33  THR   B CA   1 
ATOM   4401 C C    . THR   B 1 33  ? 45.435 -13.112 -10.487 1.00 13.78 ?  33  THR   B C    1 
ATOM   4402 O O    . THR   B 1 33  ? 45.912 -12.340 -9.646  1.00 14.99 ?  33  THR   B O    1 
ATOM   4403 C CB   . THR   B 1 33  ? 44.165 -12.126 -12.418 1.00 15.09 ?  33  THR   B CB   1 
ATOM   4404 O OG1  . THR   B 1 33  ? 44.211 -11.863 -13.823 1.00 15.24 ?  33  THR   B OG1  1 
ATOM   4405 C CG2  . THR   B 1 33  ? 43.911 -10.825 -11.666 1.00 16.13 ?  33  THR   B CG2  1 
ATOM   4406 H H    . THR   B 1 33  ? 45.162 -14.158 -13.336 1.00 16.99 ?  33  THR   B H    1 
ATOM   4407 H HA   . THR   B 1 33  ? 46.188 -12.108 -12.099 1.00 17.39 ?  33  THR   B HA   1 
ATOM   4408 H HB   . THR   B 1 33  ? 43.432 -12.736 -12.227 1.00 18.11 ?  33  THR   B HB   1 
ATOM   4409 H HG1  . THR   B 1 33  ? 43.489 -11.501 -14.073 1.00 18.28 ?  33  THR   B HG1  1 
ATOM   4410 H HG21 . THR   B 1 33  ? 43.157 -10.362 -12.055 1.00 19.36 ?  33  THR   B HG21 1 
ATOM   4411 H HG22 . THR   B 1 33  ? 43.724 -11.010 -10.733 1.00 19.36 ?  33  THR   B HG22 1 
ATOM   4412 H HG23 . THR   B 1 33  ? 44.696 -10.257 -11.723 1.00 19.36 ?  33  THR   B HG23 1 
ATOM   4413 N N    . VAL   B 1 34  ? 44.886 -14.282 -10.149 1.00 12.83 ?  34  VAL   B N    1 
ATOM   4414 C CA   . VAL   B 1 34  ? 44.699 -14.683 -8.757  1.00 12.40 ?  34  VAL   B CA   1 
ATOM   4415 C C    . VAL   B 1 34  ? 45.127 -16.132 -8.594  1.00 11.71 ?  34  VAL   B C    1 
ATOM   4416 O O    . VAL   B 1 34  ? 44.606 -17.019 -9.281  1.00 12.13 ?  34  VAL   B O    1 
ATOM   4417 C CB   . VAL   B 1 34  ? 43.229 -14.538 -8.309  1.00 13.60 ?  34  VAL   B CB   1 
ATOM   4418 C CG1  . VAL   B 1 34  ? 43.064 -14.983 -6.869  1.00 14.28 ?  34  VAL   B CG1  1 
ATOM   4419 C CG2  . VAL   B 1 34  ? 42.737 -13.108 -8.494  1.00 14.68 ?  34  VAL   B CG2  1 
ATOM   4420 H H    . VAL   B 1 34  ? 44.622 -14.873 -10.716 1.00 15.40 ?  34  VAL   B H    1 
ATOM   4421 H HA   . VAL   B 1 34  ? 45.256 -14.134 -8.182  1.00 14.89 ?  34  VAL   B HA   1 
ATOM   4422 H HB   . VAL   B 1 34  ? 42.680 -15.112 -8.863  1.00 16.32 ?  34  VAL   B HB   1 
ATOM   4423 H HG11 . VAL   B 1 34  ? 42.203 -14.674 -6.543  1.00 17.14 ?  34  VAL   B HG11 1 
ATOM   4424 H HG12 . VAL   B 1 34  ? 43.099 -15.952 -6.829  1.00 17.14 ?  34  VAL   B HG12 1 
ATOM   4425 H HG13 . VAL   B 1 34  ? 43.775 -14.601 -6.334  1.00 17.14 ?  34  VAL   B HG13 1 
ATOM   4426 H HG21 . VAL   B 1 34  ? 41.821 -13.047 -8.182  1.00 17.62 ?  34  VAL   B HG21 1 
ATOM   4427 H HG22 . VAL   B 1 34  ? 43.302 -12.508 -7.986  1.00 17.62 ?  34  VAL   B HG22 1 
ATOM   4428 H HG23 . VAL   B 1 34  ? 42.777 -12.879 -9.439  1.00 17.62 ?  34  VAL   B HG23 1 
ATOM   4429 N N    . VAL   B 1 35  ? 46.033 -16.377 -7.652  1.00 11.21 ?  35  VAL   B N    1 
ATOM   4430 C CA   . VAL   B 1 35  ? 46.274 -17.721 -7.133  1.00 11.22 ?  35  VAL   B CA   1 
ATOM   4431 C C    . VAL   B 1 35  ? 45.730 -17.778 -5.714  1.00 10.88 ?  35  VAL   B C    1 
ATOM   4432 O O    . VAL   B 1 35  ? 45.946 -16.854 -4.923  1.00 11.25 ?  35  VAL   B O    1 
ATOM   4433 C CB   . VAL   B 1 35  ? 47.759 -18.141 -7.210  1.00 11.99 ?  35  VAL   B CB   1 
ATOM   4434 C CG1  . VAL   B 1 35  ? 48.651 -17.306 -6.279  1.00 12.76 ?  35  VAL   B CG1  1 
ATOM   4435 C CG2  . VAL   B 1 35  ? 47.894 -19.642 -6.908  1.00 12.57 ?  35  VAL   B CG2  1 
ATOM   4436 H H    . VAL   B 1 35  ? 46.539 -15.775 -7.293  1.00 13.45 ?  35  VAL   B H    1 
ATOM   4437 H HA   . VAL   B 1 35  ? 45.760 -18.351 -7.660  1.00 13.47 ?  35  VAL   B HA   1 
ATOM   4438 H HB   . VAL   B 1 35  ? 48.068 -18.003 -8.120  1.00 14.38 ?  35  VAL   B HB   1 
ATOM   4439 H HG11 . VAL   B 1 35  ? 49.575 -17.522 -6.460  1.00 15.32 ?  35  VAL   B HG11 1 
ATOM   4440 H HG12 . VAL   B 1 35  ? 48.480 -16.371 -6.444  1.00 15.32 ?  35  VAL   B HG12 1 
ATOM   4441 H HG13 . VAL   B 1 35  ? 48.430 -17.529 -5.358  1.00 15.32 ?  35  VAL   B HG13 1 
ATOM   4442 H HG21 . VAL   B 1 35  ? 48.816 -19.906 -7.010  1.00 15.08 ?  35  VAL   B HG21 1 
ATOM   4443 H HG22 . VAL   B 1 35  ? 47.598 -19.809 -5.996  1.00 15.08 ?  35  VAL   B HG22 1 
ATOM   4444 H HG23 . VAL   B 1 35  ? 47.333 -20.144 -7.527  1.00 15.08 ?  35  VAL   B HG23 1 
ATOM   4445 N N    . VAL   B 1 36  ? 45.006 -18.854 -5.397  1.00 10.87 ?  36  VAL   B N    1 
ATOM   4446 C CA   . VAL   B 1 36  ? 44.458 -19.063 -4.064  1.00 10.64 ?  36  VAL   B CA   1 
ATOM   4447 C C    . VAL   B 1 36  ? 45.467 -19.826 -3.213  1.00 10.51 ?  36  VAL   B C    1 
ATOM   4448 O O    . VAL   B 1 36  ? 46.016 -20.854 -3.641  1.00 11.45 ?  36  VAL   B O    1 
ATOM   4449 C CB   . VAL   B 1 36  ? 43.120 -19.818 -4.140  1.00 11.07 ?  36  VAL   B CB   1 
ATOM   4450 C CG1  . VAL   B 1 36  ? 42.625 -20.191 -2.745  1.00 11.70 ?  36  VAL   B CG1  1 
ATOM   4451 C CG2  . VAL   B 1 36  ? 42.094 -18.989 -4.879  1.00 11.56 ?  36  VAL   B CG2  1 
ATOM   4452 H H    . VAL   B 1 36  ? 44.826 -19.488 -5.948  1.00 13.04 ?  36  VAL   B H    1 
ATOM   4453 H HA   . VAL   B 1 36  ? 44.296 -18.201 -3.646  1.00 12.76 ?  36  VAL   B HA   1 
ATOM   4454 H HB   . VAL   B 1 36  ? 43.251 -20.639 -4.639  1.00 13.28 ?  36  VAL   B HB   1 
ATOM   4455 H HG11 . VAL   B 1 36  ? 41.685 -20.424 -2.798  1.00 14.04 ?  36  VAL   B HG11 1 
ATOM   4456 H HG12 . VAL   B 1 36  ? 43.135 -20.944 -2.416  1.00 14.04 ?  36  VAL   B HG12 1 
ATOM   4457 H HG13 . VAL   B 1 36  ? 42.739 -19.425 -2.157  1.00 14.04 ?  36  VAL   B HG13 1 
ATOM   4458 H HG21 . VAL   B 1 36  ? 41.252 -19.471 -4.898  1.00 13.87 ?  36  VAL   B HG21 1 
ATOM   4459 H HG22 . VAL   B 1 36  ? 41.980 -18.143 -4.418  1.00 13.87 ?  36  VAL   B HG22 1 
ATOM   4460 H HG23 . VAL   B 1 36  ? 42.405 -18.832 -5.785  1.00 13.87 ?  36  VAL   B HG23 1 
ATOM   4461 N N    . ASN   B 1 37  ? 45.695 -19.333 -1.997  1.00 10.55 ?  37  ASN   B N    1 
ATOM   4462 C CA   . ASN   B 1 37  ? 46.449 -20.052 -0.984  1.00 11.16 ?  37  ASN   B CA   1 
ATOM   4463 C C    . ASN   B 1 37  ? 45.501 -20.726 0.002   1.00 11.15 ?  37  ASN   B C    1 
ATOM   4464 O O    . ASN   B 1 37  ? 44.485 -20.151 0.409   1.00 11.45 ?  37  ASN   B O    1 
ATOM   4465 C CB   . ASN   B 1 37  ? 47.385 -19.103 -0.233  1.00 11.15 ?  37  ASN   B CB   1 
ATOM   4466 C CG   . ASN   B 1 37  ? 48.227 -19.821 0.786   1.00 11.32 ?  37  ASN   B CG   1 
ATOM   4467 O OD1  . ASN   B 1 37  ? 48.572 -21.001 0.611   1.00 11.88 ?  37  ASN   B OD1  1 
ATOM   4468 N ND2  . ASN   B 1 37  ? 48.568 -19.128 1.864   1.00 11.26 ?  37  ASN   B ND2  1 
ATOM   4469 H H    . ASN   B 1 37  ? 45.414 -18.562 -1.727  1.00 12.66 ?  37  ASN   B H    1 
ATOM   4470 H HA   . ASN   B 1 37  ? 46.983 -20.741 -1.406  1.00 13.39 ?  37  ASN   B HA   1 
ATOM   4471 H HB2  . ASN   B 1 37  ? 47.985 -18.684 -0.868  1.00 13.38 ?  37  ASN   B HB2  1 
ATOM   4472 H HB3  . ASN   B 1 37  ? 46.862 -18.434 0.229   1.00 13.38 ?  37  ASN   B HB3  1 
ATOM   4473 H HD21 . ASN   B 1 37  ? 49.051 -19.493 2.479   1.00 13.52 ?  37  ASN   B HD21 1 
ATOM   4474 H HD22 . ASN   B 1 37  ? 48.313 -18.317 1.957   1.00 13.52 ?  37  ASN   B HD22 1 
ATOM   4475 N N    . ALA   B 1 38  ? 45.845 -21.963 0.375   1.00 11.39 ?  38  ALA   B N    1 
ATOM   4476 C CA   . ALA   B 1 38  ? 45.190 -22.704 1.456   1.00 11.62 ?  38  ALA   B CA   1 
ATOM   4477 C C    . ALA   B 1 38  ? 45.782 -22.223 2.779   1.00 11.84 ?  38  ALA   B C    1 
ATOM   4478 O O    . ALA   B 1 38  ? 46.685 -22.834 3.361   1.00 12.36 ?  38  ALA   B O    1 
ATOM   4479 C CB   . ALA   B 1 38  ? 45.394 -24.202 1.269   1.00 13.01 ?  38  ALA   B CB   1 
ATOM   4480 H H    . ALA   B 1 38  ? 46.489 -22.404 0.013   1.00 13.67 ?  38  ALA   B H    1 
ATOM   4481 H HA   . ALA   B 1 38  ? 44.239 -22.513 1.456   1.00 13.95 ?  38  ALA   B HA   1 
ATOM   4482 H HB1  . ALA   B 1 38  ? 44.945 -24.673 1.998   1.00 15.61 ?  38  ALA   B HB1  1 
ATOM   4483 H HB2  . ALA   B 1 38  ? 45.001 -24.469 0.423   1.00 15.61 ?  38  ALA   B HB2  1 
ATOM   4484 H HB3  . ALA   B 1 38  ? 46.337 -24.401 1.281   1.00 15.61 ?  38  ALA   B HB3  1 
ATOM   4485 N N    . ALA   B 1 39  ? 45.263 -21.082 3.242   1.00 11.54 ?  39  ALA   B N    1 
ATOM   4486 C CA   . ALA   B 1 39  ? 45.809 -20.348 4.373   1.00 11.47 ?  39  ALA   B CA   1 
ATOM   4487 C C    . ALA   B 1 39  ? 45.191 -20.796 5.695   1.00 11.57 ?  39  ALA   B C    1 
ATOM   4488 O O    . ALA   B 1 39  ? 44.160 -21.467 5.741   1.00 12.69 ?  39  ALA   B O    1 
ATOM   4489 C CB   . ALA   B 1 39  ? 45.565 -18.847 4.185   1.00 12.49 ?  39  ALA   B CB   1 
ATOM   4490 H H    . ALA   B 1 39  ? 44.571 -20.709 2.901   1.00 13.85 ?  39  ALA   B H    1 
ATOM   4491 H HA   . ALA   B 1 39  ? 46.762 -20.495 4.422   1.00 13.77 ?  39  ALA   B HA   1 
ATOM   4492 H HB1  . ALA   B 1 39  ? 45.931 -18.368 4.946   1.00 14.99 ?  39  ALA   B HB1  1 
ATOM   4493 H HB2  . ALA   B 1 39  ? 46.005 -18.556 3.370   1.00 14.99 ?  39  ALA   B HB2  1 
ATOM   4494 H HB3  . ALA   B 1 39  ? 44.611 -18.684 4.121   1.00 14.99 ?  39  ALA   B HB3  1 
ATOM   4495 N N    . ASN   B 1 40  ? 45.834 -20.382 6.786   1.00 12.32 ?  40  ASN   B N    1 
ATOM   4496 C CA   . ASN   B 1 40  ? 45.265 -20.427 8.123   1.00 13.08 ?  40  ASN   B CA   1 
ATOM   4497 C C    . ASN   B 1 40  ? 45.083 -19.000 8.646   1.00 12.84 ?  40  ASN   B C    1 
ATOM   4498 O O    . ASN   B 1 40  ? 45.498 -18.018 8.019   1.00 12.79 ?  40  ASN   B O    1 
ATOM   4499 C CB   . ASN   B 1 40  ? 46.112 -21.292 9.072   1.00 14.08 ?  40  ASN   B CB   1 
ATOM   4500 C CG   . ASN   B 1 40  ? 47.570 -20.901 9.082   1.00 15.06 ?  40  ASN   B CG   1 
ATOM   4501 O OD1  . ASN   B 1 40  ? 47.900 -19.724 9.126   1.00 17.16 ?  40  ASN   B OD1  1 
ATOM   4502 N ND2  . ASN   B 1 40  ? 48.455 -21.885 9.052   1.00 15.34 ?  40  ASN   B ND2  1 
ATOM   4503 H H    . ASN   B 1 40  ? 46.636 -20.071 6.768   1.00 14.78 ?  40  ASN   B H    1 
ATOM   4504 H HA   . ASN   B 1 40  ? 44.384 -20.827 8.076   1.00 15.70 ?  40  ASN   B HA   1 
ATOM   4505 H HB2  . ASN   B 1 40  ? 45.774 -21.195 9.975   1.00 16.90 ?  40  ASN   B HB2  1 
ATOM   4506 H HB3  . ASN   B 1 40  ? 46.054 -22.217 8.791   1.00 16.90 ?  40  ASN   B HB3  1 
ATOM   4507 H HD21 . ASN   B 1 40  ? 49.298 -21.710 9.058   1.00 18.41 ?  40  ASN   B HD21 1 
ATOM   4508 H HD22 . ASN   B 1 40  ? 48.186 -22.701 9.025   1.00 18.41 ?  40  ASN   B HD22 1 
ATOM   4509 N N    . VAL   B 1 41  ? 44.436 -18.879 9.806   1.00 13.20 ?  41  VAL   B N    1 
ATOM   4510 C CA   . VAL   B 1 41  ? 43.982 -17.559 10.254  1.00 14.20 ?  41  VAL   B CA   1 
ATOM   4511 C C    . VAL   B 1 41  ? 45.133 -16.608 10.558  1.00 13.93 ?  41  VAL   B C    1 
ATOM   4512 O O    . VAL   B 1 41  ? 44.958 -15.386 10.472  1.00 14.59 ?  41  VAL   B O    1 
ATOM   4513 C CB   . VAL   B 1 41  ? 43.006 -17.640 11.443  1.00 15.84 ?  41  VAL   B CB   1 
ATOM   4514 C CG1  . VAL   B 1 41  ? 41.706 -18.313 11.028  1.00 16.33 ?  41  VAL   B CG1  1 
ATOM   4515 C CG2  . VAL   B 1 41  ? 43.649 -18.334 12.634  1.00 16.90 ?  41  VAL   B CG2  1 
ATOM   4516 H H    . VAL   B 1 41  ? 44.250 -19.522 10.334  1.00 15.84 ?  41  VAL   B H    1 
ATOM   4517 H HA   . VAL   B 1 41  ? 43.488 -17.156 9.525   1.00 17.03 ?  41  VAL   B HA   1 
ATOM   4518 H HB   . VAL   B 1 41  ? 42.786 -16.738 11.725  1.00 19.01 ?  41  VAL   B HB   1 
ATOM   4519 H HG11 . VAL   B 1 41  ? 41.098 -18.317 11.785  1.00 19.59 ?  41  VAL   B HG11 1 
ATOM   4520 H HG12 . VAL   B 1 41  ? 41.317 -17.816 10.293  1.00 19.59 ?  41  VAL   B HG12 1 
ATOM   4521 H HG13 . VAL   B 1 41  ? 41.897 -19.222 10.753  1.00 19.59 ?  41  VAL   B HG13 1 
ATOM   4522 H HG21 . VAL   B 1 41  ? 43.014 -18.363 13.363  1.00 20.28 ?  41  VAL   B HG21 1 
ATOM   4523 H HG22 . VAL   B 1 41  ? 43.900 -19.235 12.376  1.00 20.28 ?  41  VAL   B HG22 1 
ATOM   4524 H HG23 . VAL   B 1 41  ? 44.439 -17.836 12.900  1.00 20.28 ?  41  VAL   B HG23 1 
ATOM   4525 N N    . TYR   B 1 42  ? 46.299 -17.123 10.947  1.00 14.52 ?  42  TYR   B N    1 
ATOM   4526 C CA   . TYR   B 1 42  ? 47.455 -16.276 11.213  1.00 14.90 ?  42  TYR   B CA   1 
ATOM   4527 C C    . TYR   B 1 42  ? 48.416 -16.198 10.029  1.00 14.17 ?  42  TYR   B C    1 
ATOM   4528 O O    . TYR   B 1 42  ? 49.506 -15.628 10.164  1.00 15.59 ?  42  TYR   B O    1 
ATOM   4529 C CB   . TYR   B 1 42  ? 48.157 -16.681 12.517  1.00 16.80 ?  42  TYR   B CB   1 
ATOM   4530 C CG   . TYR   B 1 42  ? 47.559 -15.994 13.742  1.00 17.28 ?  42  TYR   B CG   1 
ATOM   4531 C CD1  . TYR   B 1 42  ? 47.778 -14.639 13.976  1.00 16.65 ?  42  TYR   B CD1  1 
ATOM   4532 C CD2  . TYR   B 1 42  ? 46.770 -16.690 14.645  1.00 19.67 ?  42  TYR   B CD2  1 
ATOM   4533 C CE1  . TYR   B 1 42  ? 47.231 -14.000 15.076  1.00 17.57 ?  42  TYR   B CE1  1 
ATOM   4534 C CE2  . TYR   B 1 42  ? 46.223 -16.061 15.752  1.00 19.86 ?  42  TYR   B CE2  1 
ATOM   4535 C CZ   . TYR   B 1 42  ? 46.454 -14.712 15.962  1.00 19.84 ?  42  TYR   B CZ   1 
ATOM   4536 O OH   . TYR   B 1 42  ? 45.917 -14.073 17.062  1.00 23.13 ?  42  TYR   B OH   1 
ATOM   4537 H H    . TYR   B 1 42  ? 46.445 -17.969 11.051  1.00 17.43 ?  42  TYR   B H    1 
ATOM   4538 H HA   . TYR   B 1 42  ? 47.126 -15.379 11.348  1.00 17.88 ?  42  TYR   B HA   1 
ATOM   4539 H HB2  . TYR   B 1 42  ? 48.074 -17.638 12.638  1.00 20.16 ?  42  TYR   B HB2  1 
ATOM   4540 H HB3  . TYR   B 1 42  ? 49.093 -16.432 12.459  1.00 20.16 ?  42  TYR   B HB3  1 
ATOM   4541 H HD1  . TYR   B 1 42  ? 48.304 -14.153 13.373  1.00 19.97 ?  42  TYR   B HD1  1 
ATOM   4542 H HD2  . TYR   B 1 42  ? 46.606 -17.596 14.502  1.00 23.60 ?  42  TYR   B HD2  1 
ATOM   4543 H HE1  . TYR   B 1 42  ? 47.394 -13.096 15.214  1.00 21.08 ?  42  TYR   B HE1  1 
ATOM   4544 H HE2  . TYR   B 1 42  ? 45.695 -16.542 16.345  1.00 23.83 ?  42  TYR   B HE2  1 
ATOM   4545 H HH   . TYR   B 1 42  ? 46.144 -13.268 17.055  1.00 27.75 ?  42  TYR   B HH   1 
ATOM   4546 N N    . LEU   B 1 43  ? 48.017 -16.711 8.864   1.00 13.00 ?  43  LEU   B N    1 
ATOM   4547 C CA   . LEU   B 1 43  ? 48.836 -16.639 7.655   1.00 12.76 ?  43  LEU   B CA   1 
ATOM   4548 C C    . LEU   B 1 43  ? 50.251 -17.147 7.913   1.00 13.10 ?  43  LEU   B C    1 
ATOM   4549 O O    . LEU   B 1 43  ? 51.232 -16.557 7.461   1.00 13.90 ?  43  LEU   B O    1 
ATOM   4550 C CB   . LEU   B 1 43  ? 48.856 -15.233 7.053   1.00 13.14 ?  43  LEU   B CB   1 
ATOM   4551 C CG   . LEU   B 1 43  ? 47.498 -14.622 6.686   1.00 12.96 ?  43  LEU   B CG   1 
ATOM   4552 C CD1  . LEU   B 1 43  ? 47.706 -13.218 6.116   1.00 14.75 ?  43  LEU   B CD1  1 
ATOM   4553 C CD2  . LEU   B 1 43  ? 46.721 -15.505 5.719   1.00 13.67 ?  43  LEU   B CD2  1 
ATOM   4554 H H    . LEU   B 1 43  ? 47.276 -17.131 8.751   1.00 15.60 ?  43  LEU   B H    1 
ATOM   4555 H HA   . LEU   B 1 43  ? 48.439 -17.228 6.988   1.00 15.32 ?  43  LEU   B HA   1 
ATOM   4556 H HB2  . LEU   B 1 43  ? 49.279 -14.638 7.692   1.00 15.76 ?  43  LEU   B HB2  1 
ATOM   4557 H HB3  . LEU   B 1 43  ? 49.387 -15.260 6.241   1.00 15.76 ?  43  LEU   B HB3  1 
ATOM   4558 H HG   . LEU   B 1 43  ? 46.973 -14.532 7.494   1.00 15.55 ?  43  LEU   B HG   1 
ATOM   4559 H HD11 . LEU   B 1 43  ? 46.842 -12.839 5.889   1.00 17.70 ?  43  LEU   B HD11 1 
ATOM   4560 H HD12 . LEU   B 1 43  ? 48.141 -12.665 6.786   1.00 17.70 ?  43  LEU   B HD12 1 
ATOM   4561 H HD13 . LEU   B 1 43  ? 48.262 -13.275 5.324   1.00 17.70 ?  43  LEU   B HD13 1 
ATOM   4562 H HD21 . LEU   B 1 43  ? 45.916 -15.036 5.442   1.00 16.41 ?  43  LEU   B HD21 1 
ATOM   4563 H HD22 . LEU   B 1 43  ? 47.274 -15.694 4.947   1.00 16.41 ?  43  LEU   B HD22 1 
ATOM   4564 H HD23 . LEU   B 1 43  ? 46.482 -16.330 6.168   1.00 16.41 ?  43  LEU   B HD23 1 
ATOM   4565 N N    . LYS   B 1 44  ? 50.351 -18.268 8.632   1.00 13.28 ?  44  LYS   B N    1 
ATOM   4566 C CA   . LYS   B 1 44  ? 51.617 -18.957 8.874   1.00 13.66 ?  44  LYS   B CA   1 
ATOM   4567 C C    . LYS   B 1 44  ? 51.728 -20.073 7.844   1.00 13.49 ?  44  LYS   B C    1 
ATOM   4568 O O    . LYS   B 1 44  ? 51.039 -21.092 7.934   1.00 14.76 ?  44  LYS   B O    1 
ATOM   4569 C CB   . LYS   B 1 44  ? 51.665 -19.471 10.309  1.00 15.40 ?  44  LYS   B CB   1 
ATOM   4570 C CG   . LYS   B 1 44  ? 51.857 -18.368 11.336  1.00 18.06 ?  44  LYS   B CG   1 
ATOM   4571 C CD   . LYS   B 1 44  ? 53.081 -17.523 10.964  1.00 21.65 ?  44  LYS   B CD   1 
ATOM   4572 C CE   . LYS   B 1 44  ? 53.530 -16.611 12.074  1.00 24.63 ?  44  LYS   B CE   1 
ATOM   4573 N NZ   . LYS   B 1 44  ? 54.731 -15.823 11.699  1.00 26.01 ?  44  LYS   B NZ   1 
ATOM   4574 H H    . LYS   B 1 44  ? 49.677 -18.651 9.008   1.00 15.93 ?  44  LYS   B H    1 
ATOM   4575 H HA   . LYS   B 1 44  ? 52.348 -18.343 8.713   1.00 16.39 ?  44  LYS   B HA   1 
ATOM   4576 H HB2  . LYS   B 1 44  ? 50.825 -19.922 10.509  1.00 18.48 ?  44  LYS   B HB2  1 
ATOM   4577 H HB3  . LYS   B 1 44  ? 52.400 -20.095 10.393  1.00 18.48 ?  44  LYS   B HB3  1 
ATOM   4578 H HG2  . LYS   B 1 44  ? 51.077 -17.797 11.355  1.00 21.67 ?  44  LYS   B HG2  1 
ATOM   4579 H HG3  . LYS   B 1 44  ? 52.012 -18.766 12.212  1.00 21.67 ?  44  LYS   B HG3  1 
ATOM   4580 H HD2  . LYS   B 1 44  ? 53.812 -18.124 10.728  1.00 25.98 ?  44  LYS   B HD2  1 
ATOM   4581 H HD3  . LYS   B 1 44  ? 52.852 -16.968 10.202  1.00 25.98 ?  44  LYS   B HD3  1 
ATOM   4582 H HE2  . LYS   B 1 44  ? 52.821 -15.982 12.246  1.00 29.55 ?  44  LYS   B HE2  1 
ATOM   4583 H HE3  . LYS   B 1 44  ? 53.731 -17.137 12.864  1.00 29.55 ?  44  LYS   B HE3  1 
ATOM   4584 H HZ1  . LYS   B 1 44  ? 54.968 -15.294 12.373  1.00 31.21 ?  44  LYS   B HZ1  1 
ATOM   4585 H HZ2  . LYS   B 1 44  ? 55.408 -16.365 11.504  1.00 31.21 ?  44  LYS   B HZ2  1 
ATOM   4586 H HZ3  . LYS   B 1 44  ? 54.553 -15.317 10.986  1.00 31.21 ?  44  LYS   B HZ3  1 
ATOM   4587 N N    . HIS   B 1 45  ? 52.575 -19.854 6.840   1.00 13.23 ?  45  HIS   B N    1 
ATOM   4588 C CA   . HIS   B 1 45  ? 52.601 -20.684 5.636   1.00 13.29 ?  45  HIS   B CA   1 
ATOM   4589 C C    . HIS   B 1 45  ? 53.620 -21.807 5.802   1.00 15.24 ?  45  HIS   B C    1 
ATOM   4590 O O    . HIS   B 1 45  ? 54.685 -21.822 5.192   1.00 17.53 ?  45  HIS   B O    1 
ATOM   4591 C CB   . HIS   B 1 45  ? 52.917 -19.829 4.421   1.00 13.32 ?  45  HIS   B CB   1 
ATOM   4592 C CG   . HIS   B 1 45  ? 52.054 -18.621 4.309   1.00 12.72 ?  45  HIS   B CG   1 
ATOM   4593 N ND1  . HIS   B 1 45  ? 50.675 -18.692 4.272   1.00 13.39 ?  45  HIS   B ND1  1 
ATOM   4594 C CD2  . HIS   B 1 45  ? 52.376 -17.309 4.232   1.00 13.92 ?  45  HIS   B CD2  1 
ATOM   4595 C CE1  . HIS   B 1 45  ? 50.193 -17.467 4.165   1.00 13.36 ?  45  HIS   B CE1  1 
ATOM   4596 N NE2  . HIS   B 1 45  ? 51.200 -16.611 4.142   1.00 13.81 ?  45  HIS   B NE2  1 
ATOM   4597 H H    . HIS   B 1 45  ? 53.146 -19.209 6.827   1.00 15.88 ?  45  HIS   B H    1 
ATOM   4598 H HA   . HIS   B 1 45  ? 51.722 -21.082 5.507   1.00 15.94 ?  45  HIS   B HA   1 
ATOM   4599 H HB2  . HIS   B 1 45  ? 53.837 -19.535 4.474   1.00 15.98 ?  45  HIS   B HB2  1 
ATOM   4600 H HB3  . HIS   B 1 45  ? 52.788 -20.367 3.619   1.00 15.98 ?  45  HIS   B HB3  1 
ATOM   4601 H HD2  . HIS   B 1 45  ? 53.232 -16.951 4.239   1.00 16.70 ?  45  HIS   B HD2  1 
ATOM   4602 H HE1  . HIS   B 1 45  ? 49.290 -17.246 4.111   1.00 16.03 ?  45  HIS   B HE1  1 
ATOM   4603 H HE2  . HIS   B 1 45  ? 51.127 -15.758 4.083   1.00 16.57 ?  45  HIS   B HE2  1 
ATOM   4604 N N    A GLY   B 1 46  ? 53.250 -22.779 6.631   0.76 16.31 ?  46  GLY   B N    1 
ATOM   4605 N N    B GLY   B 1 46  ? 53.263 -22.765 6.649   0.24 16.41 ?  46  GLY   B N    1 
ATOM   4606 C CA   A GLY   B 1 46  ? 54.168 -23.835 7.014   0.76 17.79 ?  46  GLY   B CA   1 
ATOM   4607 C CA   B GLY   B 1 46  ? 54.182 -23.832 6.987   0.24 17.52 ?  46  GLY   B CA   1 
ATOM   4608 C C    A GLY   B 1 46  ? 54.224 -25.047 6.103   0.76 19.56 ?  46  GLY   B C    1 
ATOM   4609 C C    B GLY   B 1 46  ? 54.205 -24.975 5.992   0.24 18.61 ?  46  GLY   B C    1 
ATOM   4610 O O    A GLY   B 1 46  ? 55.303 -25.453 5.660   0.76 22.88 ?  46  GLY   B O    1 
ATOM   4611 O O    B GLY   B 1 46  ? 55.231 -25.238 5.357   0.24 19.32 ?  46  GLY   B O    1 
ATOM   4612 H H    A GLY   B 1 46  ? 52.473 -22.830 7.005   0.76 19.57 ?  46  GLY   B H    1 
ATOM   4613 H H    B GLY   B 1 46  ? 52.497 -22.812 7.044   0.24 19.69 ?  46  GLY   B H    1 
ATOM   4614 H HA2  A GLY   B 1 46  ? 55.060 -23.461 7.073   0.76 21.35 ?  46  GLY   B HA2  1 
ATOM   4615 H HA2  B GLY   B 1 46  ? 55.078 -23.464 7.048   0.24 21.02 ?  46  GLY   B HA2  1 
ATOM   4616 H HA3  A GLY   B 1 46  ? 53.920 -24.154 7.896   0.76 21.35 ?  46  GLY   B HA3  1 
ATOM   4617 H HA3  B GLY   B 1 46  ? 53.944 -24.185 7.859   0.24 21.02 ?  46  GLY   B HA3  1 
ATOM   4618 N N    . GLY   B 1 47  ? 53.072 -25.657 5.834   1.00 19.20 ?  47  GLY   B N    1 
ATOM   4619 C CA   . GLY   B 1 47  ? 53.016 -26.912 5.114   1.00 16.74 ?  47  GLY   B CA   1 
ATOM   4620 C C    . GLY   B 1 47  ? 52.109 -26.874 3.899   1.00 14.70 ?  47  GLY   B C    1 
ATOM   4621 O O    . GLY   B 1 47  ? 51.455 -25.871 3.609   1.00 14.73 ?  47  GLY   B O    1 
ATOM   4622 H H    A GLY   B 1 47  ? 52.302 -25.371 6.091   0.76 23.04 ?  47  GLY   B H    1 
ATOM   4623 H H    B GLY   B 1 47  ? 52.311 -25.404 6.147   0.24 23.04 ?  47  GLY   B H    1 
ATOM   4624 H HA2  . GLY   B 1 47  ? 53.907 -27.159 4.821   1.00 20.09 ?  47  GLY   B HA2  1 
ATOM   4625 H HA3  . GLY   B 1 47  ? 52.694 -27.605 5.714   1.00 20.09 ?  47  GLY   B HA3  1 
ATOM   4626 N N    . GLY   B 1 48  ? 52.069 -28.010 3.202   1.00 14.10 ?  48  GLY   B N    1 
ATOM   4627 C CA   . GLY   B 1 48  ? 51.131 -28.160 2.104   1.00 13.72 ?  48  GLY   B CA   1 
ATOM   4628 C C    . GLY   B 1 48  ? 51.276 -27.057 1.080   1.00 12.78 ?  48  GLY   B C    1 
ATOM   4629 O O    . GLY   B 1 48  ? 52.384 -26.601 0.764   1.00 13.53 ?  48  GLY   B O    1 
ATOM   4630 H H    . GLY   B 1 48  ? 52.571 -28.689 3.341   1.00 16.92 ?  48  GLY   B H    1 
ATOM   4631 H HA2  . GLY   B 1 48  ? 51.277 -29.014 1.668   1.00 16.47 ?  48  GLY   B HA2  1 
ATOM   4632 H HA3  . GLY   B 1 48  ? 50.222 -28.142 2.447   1.00 16.47 ?  48  GLY   B HA3  1 
ATOM   4633 N N    . VAL   B 1 49  ? 50.134 -26.626 0.543   1.00 13.10 ?  49  VAL   B N    1 
ATOM   4634 C CA   . VAL   B 1 49  ? 50.119 -25.601 -0.497  1.00 12.87 ?  49  VAL   B CA   1 
ATOM   4635 C C    . VAL   B 1 49  ? 50.775 -24.315 -0.005  1.00 11.88 ?  49  VAL   B C    1 
ATOM   4636 O O    . VAL   B 1 49  ? 51.563 -23.690 -0.725  1.00 13.00 ?  49  VAL   B O    1 
ATOM   4637 C CB   . VAL   B 1 49  ? 48.674 -25.345 -0.971  1.00 14.27 ?  49  VAL   B CB   1 
ATOM   4638 C CG1  . VAL   B 1 49  ? 48.593 -24.080 -1.830  1.00 14.53 ?  49  VAL   B CG1  1 
ATOM   4639 C CG2  . VAL   B 1 49  ? 48.129 -26.547 -1.731  1.00 15.89 ?  49  VAL   B CG2  1 
ATOM   4640 H H    . VAL   B 1 49  ? 49.350 -26.912 0.759   1.00 15.71 ?  49  VAL   B H    1 
ATOM   4641 H HA   . VAL   B 1 49  ? 50.625 -25.915 -1.261  1.00 15.45 ?  49  VAL   B HA   1 
ATOM   4642 H HB   . VAL   B 1 49  ? 48.111 -25.209 -0.194  1.00 17.13 ?  49  VAL   B HB   1 
ATOM   4643 H HG11 . VAL   B 1 49  ? 47.761 -24.091 -2.329  1.00 17.44 ?  49  VAL   B HG11 1 
ATOM   4644 H HG12 . VAL   B 1 49  ? 48.616 -23.300 -1.251  1.00 17.44 ?  49  VAL   B HG12 1 
ATOM   4645 H HG13 . VAL   B 1 49  ? 49.344 -24.062 -2.441  1.00 17.44 ?  49  VAL   B HG13 1 
ATOM   4646 H HG21 . VAL   B 1 49  ? 47.220 -26.358 -2.011  1.00 19.07 ?  49  VAL   B HG21 1 
ATOM   4647 H HG22 . VAL   B 1 49  ? 48.688 -26.707 -2.509  1.00 19.07 ?  49  VAL   B HG22 1 
ATOM   4648 H HG23 . VAL   B 1 49  ? 48.144 -27.320 -1.148  1.00 19.07 ?  49  VAL   B HG23 1 
ATOM   4649 N N    . ALA   B 1 50  ? 50.427 -23.875 1.207   1.00 11.98 ?  50  ALA   B N    1 
ATOM   4650 C CA   . ALA   B 1 50  ? 50.945 -22.596 1.685   1.00 11.94 ?  50  ALA   B CA   1 
ATOM   4651 C C    . ALA   B 1 50  ? 52.466 -22.625 1.795   1.00 12.11 ?  50  ALA   B C    1 
ATOM   4652 O O    . ALA   B 1 50  ? 53.146 -21.657 1.429   1.00 12.33 ?  50  ALA   B O    1 
ATOM   4653 C CB   . ALA   B 1 50  ? 50.318 -22.231 3.029   1.00 12.64 ?  50  ALA   B CB   1 
ATOM   4654 H H    . ALA   B 1 50  ? 49.907 -24.285 1.755   1.00 14.38 ?  50  ALA   B H    1 
ATOM   4655 H HA   . ALA   B 1 50  ? 50.713 -21.903 1.054   1.00 14.33 ?  50  ALA   B HA   1 
ATOM   4656 H HB1  . ALA   B 1 50  ? 50.677 -21.377 3.327   1.00 15.17 ?  50  ALA   B HB1  1 
ATOM   4657 H HB2  . ALA   B 1 50  ? 49.357 -22.163 2.922   1.00 15.17 ?  50  ALA   B HB2  1 
ATOM   4658 H HB3  . ALA   B 1 50  ? 50.531 -22.920 3.679   1.00 15.17 ?  50  ALA   B HB3  1 
ATOM   4659 N N    . GLY   B 1 51  ? 53.019 -23.717 2.311   1.00 12.76 ?  51  GLY   B N    1 
ATOM   4660 C CA   . GLY   B 1 51  ? 54.465 -23.810 2.383   1.00 13.42 ?  51  GLY   B CA   1 
ATOM   4661 C C    . GLY   B 1 51  ? 55.114 -23.764 1.014   1.00 13.26 ?  51  GLY   B C    1 
ATOM   4662 O O    . GLY   B 1 51  ? 56.155 -23.127 0.827   1.00 14.24 ?  51  GLY   B O    1 
ATOM   4663 H H    . GLY   B 1 51  ? 52.595 -24.397 2.622   1.00 15.32 ?  51  GLY   B H    1 
ATOM   4664 H HA2  . GLY   B 1 51  ? 54.814 -23.072 2.914   1.00 16.11 ?  51  GLY   B HA2  1 
ATOM   4665 H HA3  . GLY   B 1 51  ? 54.719 -24.641 2.815   1.00 16.11 ?  51  GLY   B HA3  1 
ATOM   4666 N N    . ALA   B 1 52  ? 54.506 -24.428 0.033   1.00 12.88 ?  52  ALA   B N    1 
ATOM   4667 C CA   . ALA   B 1 52  ? 55.068 -24.436 -1.311  1.00 13.48 ?  52  ALA   B CA   1 
ATOM   4668 C C    . ALA   B 1 52  ? 54.991 -23.056 -1.958  1.00 12.67 ?  52  ALA   B C    1 
ATOM   4669 O O    . ALA   B 1 52  ? 55.957 -22.611 -2.598  1.00 13.53 ?  52  ALA   B O    1 
ATOM   4670 C CB   . ALA   B 1 52  ? 54.342 -25.462 -2.172  1.00 14.16 ?  52  ALA   B CB   1 
ATOM   4671 H H    . ALA   B 1 52  ? 53.765 -24.862 0.120   1.00 15.45 ?  52  ALA   B H    1 
ATOM   4672 H HA   . ALA   B 1 52  ? 55.998 -24.688 -1.256  1.00 16.17 ?  52  ALA   B HA   1 
ATOM   4673 H HB1  . ALA   B 1 52  ? 54.731 -25.457 -3.061  1.00 16.99 ?  52  ALA   B HB1  1 
ATOM   4674 H HB2  . ALA   B 1 52  ? 54.448 -26.339 -1.770  1.00 16.99 ?  52  ALA   B HB2  1 
ATOM   4675 H HB3  . ALA   B 1 52  ? 53.402 -25.230 -2.220  1.00 16.99 ?  52  ALA   B HB3  1 
ATOM   4676 N N    . LEU   B 1 53  ? 53.847 -22.375 -1.834  1.00 12.28 ?  53  LEU   B N    1 
ATOM   4677 C CA   . LEU   B 1 53  ? 53.732 -21.037 -2.404  1.00 12.58 ?  53  LEU   B CA   1 
ATOM   4678 C C    . LEU   B 1 53  ? 54.739 -20.095 -1.760  1.00 12.47 ?  53  LEU   B C    1 
ATOM   4679 O O    . LEU   B 1 53  ? 55.431 -19.339 -2.452  1.00 13.20 ?  53  LEU   B O    1 
ATOM   4680 C CB   . LEU   B 1 53  ? 52.307 -20.502 -2.238  1.00 13.18 ?  53  LEU   B CB   1 
ATOM   4681 C CG   . LEU   B 1 53  ? 51.174 -21.235 -2.973  1.00 13.44 ?  53  LEU   B CG   1 
ATOM   4682 C CD1  . LEU   B 1 53  ? 49.830 -20.612 -2.656  1.00 14.95 ?  53  LEU   B CD1  1 
ATOM   4683 C CD2  . LEU   B 1 53  ? 51.410 -21.260 -4.475  1.00 15.62 ?  53  LEU   B CD2  1 
ATOM   4684 H H    . LEU   B 1 53  ? 53.145 -22.656 -1.427  1.00 14.74 ?  53  LEU   B H    1 
ATOM   4685 H HA   . LEU   B 1 53  ? 53.931 -21.083 -3.355  1.00 15.10 ?  53  LEU   B HA   1 
ATOM   4686 H HB2  . LEU   B 1 53  ? 52.091 -20.524 -1.296  1.00 15.82 ?  53  LEU   B HB2  1 
ATOM   4687 H HB3  . LEU   B 1 53  ? 52.295 -19.587 -2.550  1.00 15.82 ?  53  LEU   B HB3  1 
ATOM   4688 H HG   . LEU   B 1 53  ? 51.149 -22.156 -2.663  1.00 16.13 ?  53  LEU   B HG   1 
ATOM   4689 H HD11 . LEU   B 1 53  ? 49.135 -21.100 -3.130  1.00 17.94 ?  53  LEU   B HD11 1 
ATOM   4690 H HD12 . LEU   B 1 53  ? 49.672 -20.670 -1.698  1.00 17.94 ?  53  LEU   B HD12 1 
ATOM   4691 H HD13 . LEU   B 1 53  ? 49.834 -19.687 -2.936  1.00 17.94 ?  53  LEU   B HD13 1 
ATOM   4692 H HD21 . LEU   B 1 53  ? 50.669 -21.715 -4.905  1.00 18.74 ?  53  LEU   B HD21 1 
ATOM   4693 H HD22 . LEU   B 1 53  ? 51.474 -20.351 -4.800  1.00 18.74 ?  53  LEU   B HD22 1 
ATOM   4694 H HD23 . LEU   B 1 53  ? 52.237 -21.738 -4.658  1.00 18.74 ?  53  LEU   B HD23 1 
ATOM   4695 N N    . ASN   B 1 54  ? 54.830 -20.117 -0.433  1.00 12.19 ?  54  ASN   B N    1 
ATOM   4696 C CA   . ASN   B 1 54  ? 55.748 -19.205 0.236   1.00 13.16 ?  54  ASN   B CA   1 
ATOM   4697 C C    . ASN   B 1 54  ? 57.190 -19.489 -0.163  1.00 13.60 ?  54  ASN   B C    1 
ATOM   4698 O O    . ASN   B 1 54  ? 57.964 -18.554 -0.401  1.00 13.96 ?  54  ASN   B O    1 
ATOM   4699 C CB   . ASN   B 1 54  ? 55.584 -19.281 1.746   1.00 14.06 ?  54  ASN   B CB   1 
ATOM   4700 C CG   . ASN   B 1 54  ? 56.562 -18.376 2.455   1.00 13.86 ?  54  ASN   B CG   1 
ATOM   4701 O OD1  . ASN   B 1 54  ? 56.582 -17.164 2.212   1.00 14.01 ?  54  ASN   B OD1  1 
ATOM   4702 N ND2  . ASN   B 1 54  ? 57.405 -18.952 3.306   1.00 15.50 ?  54  ASN   B ND2  1 
ATOM   4703 H H    . ASN   B 1 54  ? 54.379 -20.632 0.088   1.00 14.63 ?  54  ASN   B H    1 
ATOM   4704 H HA   . ASN   B 1 54  ? 55.538 -18.299 -0.038  1.00 15.79 ?  54  ASN   B HA   1 
ATOM   4705 H HB2  . ASN   B 1 54  ? 54.685 -19.001 1.987   1.00 16.87 ?  54  ASN   B HB2  1 
ATOM   4706 H HB3  . ASN   B 1 54  ? 55.742 -20.191 2.041   1.00 16.87 ?  54  ASN   B HB3  1 
ATOM   4707 H HD21 . ASN   B 1 54  ? 57.987 -18.478 3.728   1.00 18.60 ?  54  ASN   B HD21 1 
ATOM   4708 H HD22 . ASN   B 1 54  ? 57.369 -19.803 3.441   1.00 18.60 ?  54  ASN   B HD22 1 
ATOM   4709 N N    . LYS   B 1 55  ? 57.573 -20.768 -0.228  1.00 14.06 ?  55  LYS   B N    1 
ATOM   4710 C CA   . LYS   B 1 55  ? 58.929 -21.108 -0.644  1.00 15.42 ?  55  LYS   B CA   1 
ATOM   4711 C C    . LYS   B 1 55  ? 59.225 -20.565 -2.035  1.00 14.72 ?  55  LYS   B C    1 
ATOM   4712 O O    . LYS   B 1 55  ? 60.323 -20.059 -2.292  1.00 15.33 ?  55  LYS   B O    1 
ATOM   4713 C CB   . LYS   B 1 55  ? 59.134 -22.623 -0.592  1.00 16.55 ?  55  LYS   B CB   1 
ATOM   4714 C CG   . LYS   B 1 55  ? 60.526 -23.077 -1.008  1.00 20.93 ?  55  LYS   B CG   1 
ATOM   4715 C CD   . LYS   B 1 55  ? 60.703 -24.577 -0.849  1.00 24.59 ?  55  LYS   B CD   1 
ATOM   4716 C CE   . LYS   B 1 55  ? 60.682 -25.002 0.618   1.00 27.32 ?  55  LYS   B CE   1 
ATOM   4717 N NZ   . LYS   B 1 55  ? 61.110 -26.412 0.800   1.00 28.86 ?  55  LYS   B NZ   1 
ATOM   4718 H H    . LYS   B 1 55  ? 57.069 -21.442 -0.045  1.00 16.87 ?  55  LYS   B H    1 
ATOM   4719 H HA   . LYS   B 1 55  ? 59.555 -20.699 -0.029  1.00 18.51 ?  55  LYS   B HA   1 
ATOM   4720 H HB2  . LYS   B 1 55  ? 58.980 -22.919 0.319   1.00 19.86 ?  55  LYS   B HB2  1 
ATOM   4721 H HB3  . LYS   B 1 55  ? 58.494 -23.044 -1.186  1.00 19.86 ?  55  LYS   B HB3  1 
ATOM   4722 H HG2  . LYS   B 1 55  ? 60.669 -22.852 -1.941  1.00 25.11 ?  55  LYS   B HG2  1 
ATOM   4723 H HG3  . LYS   B 1 55  ? 61.185 -22.630 -0.452  1.00 25.11 ?  55  LYS   B HG3  1 
ATOM   4724 H HD2  . LYS   B 1 55  ? 59.982 -25.037 -1.307  1.00 29.51 ?  55  LYS   B HD2  1 
ATOM   4725 H HD3  . LYS   B 1 55  ? 61.559 -24.841 -1.225  1.00 29.51 ?  55  LYS   B HD3  1 
ATOM   4726 H HE2  . LYS   B 1 55  ? 61.286 -24.428 1.120   1.00 32.78 ?  55  LYS   B HE2  1 
ATOM   4727 H HE3  . LYS   B 1 55  ? 59.777 -24.908 0.960   1.00 32.78 ?  55  LYS   B HE3  1 
ATOM   4728 H HZ1  . LYS   B 1 55  ? 61.066 -26.631 1.662   1.00 34.63 ?  55  LYS   B HZ1  1 
ATOM   4729 H HZ2  . LYS   B 1 55  ? 60.573 -26.952 0.338   1.00 34.63 ?  55  LYS   B HZ2  1 
ATOM   4730 H HZ3  . LYS   B 1 55  ? 61.943 -26.516 0.514   1.00 34.63 ?  55  LYS   B HZ3  1 
ATOM   4731 N N    . ALA   B 1 56  ? 58.252 -20.651 -2.948  1.00 14.29 ?  56  ALA   B N    1 
ATOM   4732 C CA   . ALA   B 1 56  ? 58.477 -20.145 -4.297  1.00 15.11 ?  56  ALA   B CA   1 
ATOM   4733 C C    . ALA   B 1 56  ? 58.743 -18.647 -4.296  1.00 14.55 ?  56  ALA   B C    1 
ATOM   4734 O O    . ALA   B 1 56  ? 59.471 -18.148 -5.166  1.00 16.16 ?  56  ALA   B O    1 
ATOM   4735 C CB   . ALA   B 1 56  ? 57.287 -20.483 -5.198  1.00 16.11 ?  56  ALA   B CB   1 
ATOM   4736 H H    . ALA   B 1 56  ? 57.465 -20.975 -2.813  1.00 17.14 ?  56  ALA   B H    1 
ATOM   4737 H HA   . ALA   B 1 56  ? 59.258 -20.575 -4.666  1.00 18.13 ?  56  ALA   B HA   1 
ATOM   4738 H HB1  . ALA   B 1 56  ? 57.460 -20.143 -6.093  1.00 19.33 ?  56  ALA   B HB1  1 
ATOM   4739 H HB2  . ALA   B 1 56  ? 57.181 -21.447 -5.228  1.00 19.33 ?  56  ALA   B HB2  1 
ATOM   4740 H HB3  . ALA   B 1 56  ? 56.486 -20.072 -4.839  1.00 19.33 ?  56  ALA   B HB3  1 
ATOM   4741 N N    . THR   B 1 57  ? 58.166 -17.911 -3.340  1.00 14.50 ?  57  THR   B N    1 
ATOM   4742 C CA   . THR   B 1 57  ? 58.415 -16.478 -3.213  1.00 14.67 ?  57  THR   B CA   1 
ATOM   4743 C C    . THR   B 1 57  ? 59.664 -16.156 -2.400  1.00 15.27 ?  57  THR   B C    1 
ATOM   4744 O O    . THR   B 1 57  ? 59.901 -14.981 -2.088  1.00 15.76 ?  57  THR   B O    1 
ATOM   4745 C CB   . THR   B 1 57  ? 57.220 -15.745 -2.574  1.00 13.72 ?  57  THR   B CB   1 
ATOM   4746 O OG1  . THR   B 1 57  ? 57.195 -15.978 -1.158  1.00 14.47 ?  57  THR   B OG1  1 
ATOM   4747 C CG2  . THR   B 1 57  ? 55.899 -16.153 -3.220  1.00 13.88 ?  57  THR   B CG2  1 
ATOM   4748 H H    . THR   B 1 57  ? 57.617 -18.220 -2.754  1.00 17.40 ?  57  THR   B H    1 
ATOM   4749 H HA   . THR   B 1 57  ? 58.538 -16.108 -4.100  1.00 17.60 ?  57  THR   B HA   1 
ATOM   4750 H HB   . THR   B 1 57  ? 57.331 -14.791 -2.729  1.00 16.46 ?  57  THR   B HB   1 
ATOM   4751 H HG1  . THR   B 1 57  ? 57.108 -16.797 -1.006  1.00 17.36 ?  57  THR   B HG1  1 
ATOM   4752 H HG21 . THR   B 1 57  ? 55.178 -15.609 -2.873  1.00 16.66 ?  57  THR   B HG21 1 
ATOM   4753 H HG22 . THR   B 1 57  ? 55.950 -16.034 -4.183  1.00 16.66 ?  57  THR   B HG22 1 
ATOM   4754 H HG23 . THR   B 1 57  ? 55.712 -17.085 -3.031  1.00 16.66 ?  57  THR   B HG23 1 
ATOM   4755 N N    . ASN   B 1 58  ? 60.455 -17.162 -2.038  1.00 16.31 ?  58  ASN   B N    1 
ATOM   4756 C CA   . ASN   B 1 58  ? 61.659 -16.945 -1.239  1.00 19.27 ?  58  ASN   B CA   1 
ATOM   4757 C C    . ASN   B 1 58  ? 61.327 -16.239 0.077   1.00 17.08 ?  58  ASN   B C    1 
ATOM   4758 O O    . ASN   B 1 58  ? 62.065 -15.369 0.546   1.00 17.66 ?  58  ASN   B O    1 
ATOM   4759 C CB   . ASN   B 1 58  ? 62.738 -16.189 -2.022  1.00 25.90 ?  58  ASN   B CB   1 
ATOM   4760 C CG   . ASN   B 1 58  ? 64.116 -16.333 -1.402  1.00 35.36 ?  58  ASN   B CG   1 
ATOM   4761 O OD1  . ASN   B 1 58  ? 64.426 -17.350 -0.782  1.00 38.66 ?  58  ASN   B OD1  1 
ATOM   4762 N ND2  . ASN   B 1 58  ? 64.949 -15.311 -1.564  1.00 42.63 ?  58  ASN   B ND2  1 
ATOM   4763 H H    . ASN   B 1 58  ? 60.318 -17.987 -2.244  1.00 19.58 ?  58  ASN   B H    1 
ATOM   4764 H HA   . ASN   B 1 58  ? 62.028 -17.814 -1.019  1.00 23.12 ?  58  ASN   B HA   1 
ATOM   4765 H HB2  . ASN   B 1 58  ? 62.778 -16.539 -2.928  1.00 31.08 ?  58  ASN   B HB2  1 
ATOM   4766 H HB3  . ASN   B 1 58  ? 62.517 -15.246 -2.041  1.00 31.08 ?  58  ASN   B HB3  1 
ATOM   4767 H HD21 . ASN   B 1 58  ? 65.742 -15.346 -1.232  1.00 51.15 ?  58  ASN   B HD21 1 
ATOM   4768 H HD22 . ASN   B 1 58  ? 64.695 -14.616 -2.000  1.00 51.15 ?  58  ASN   B HD22 1 
ATOM   4769 N N    . ASN   B 1 59  ? 60.203 -16.622 0.682   1.00 15.99 ?  59  ASN   B N    1 
ATOM   4770 C CA   . ASN   B 1 59  ? 59.722 -16.149 1.983   1.00 16.05 ?  59  ASN   B CA   1 
ATOM   4771 C C    . ASN   B 1 59  ? 59.130 -14.741 1.925   1.00 15.32 ?  59  ASN   B C    1 
ATOM   4772 O O    . ASN   B 1 59  ? 58.693 -14.237 2.967   1.00 15.50 ?  59  ASN   B O    1 
ATOM   4773 C CB   . ASN   B 1 59  ? 60.793 -16.205 3.088   1.00 17.19 ?  59  ASN   B CB   1 
ATOM   4774 C CG   . ASN   B 1 59  ? 60.205 -16.390 4.466   1.00 18.32 ?  59  ASN   B CG   1 
ATOM   4775 O OD1  . ASN   B 1 59  ? 59.377 -17.279 4.684   1.00 18.39 ?  59  ASN   B OD1  1 
ATOM   4776 N ND2  . ASN   B 1 59  ? 60.625 -15.553 5.409   1.00 19.03 ?  59  ASN   B ND2  1 
ATOM   4777 H H    . ASN   B 1 59  ? 59.663 -17.200 0.334   1.00 19.19 ?  59  ASN   B H    1 
ATOM   4778 H HA   . ASN   B 1 59  ? 59.012 -16.745 2.264   1.00 19.26 ?  59  ASN   B HA   1 
ATOM   4779 H HB2  . ASN   B 1 59  ? 61.387 -16.952 2.924   1.00 20.63 ?  59  ASN   B HB2  1 
ATOM   4780 H HB3  . ASN   B 1 59  ? 61.291 -15.375 3.093   1.00 20.63 ?  59  ASN   B HB3  1 
ATOM   4781 H HD21 . ASN   B 1 59  ? 60.316 -15.614 6.212   1.00 22.84 ?  59  ASN   B HD21 1 
ATOM   4782 H HD22 . ASN   B 1 59  ? 61.199 -14.944 5.218   1.00 22.84 ?  59  ASN   B HD22 1 
ATOM   4783 N N    . ALA   B 1 60  ? 59.071 -14.098 0.753   1.00 15.03 ?  60  ALA   B N    1 
ATOM   4784 C CA   . ALA   B 1 60  ? 58.472 -12.767 0.681   1.00 14.97 ?  60  ALA   B CA   1 
ATOM   4785 C C    . ALA   B 1 60  ? 57.001 -12.791 1.081   1.00 14.33 ?  60  ALA   B C    1 
ATOM   4786 O O    . ALA   B 1 60  ? 56.502 -11.842 1.698   1.00 14.91 ?  60  ALA   B O    1 
ATOM   4787 C CB   . ALA   B 1 60  ? 58.646 -12.184 -0.722  1.00 16.15 ?  60  ALA   B CB   1 
ATOM   4788 H H    . ALA   B 1 60  ? 59.371 -14.408 0.008   1.00 18.04 ?  60  ALA   B H    1 
ATOM   4789 H HA   . ALA   B 1 60  ? 58.935 -12.191 1.306   1.00 17.97 ?  60  ALA   B HA   1 
ATOM   4790 H HB1  . ALA   B 1 60  ? 58.242 -11.305 -0.744  1.00 19.38 ?  60  ALA   B HB1  1 
ATOM   4791 H HB2  . ALA   B 1 60  ? 59.594 -12.121 -0.921  1.00 19.38 ?  60  ALA   B HB2  1 
ATOM   4792 H HB3  . ALA   B 1 60  ? 58.211 -12.768 -1.362  1.00 19.38 ?  60  ALA   B HB3  1 
ATOM   4793 N N    . MET   B 1 61  ? 56.291 -13.869 0.739   1.00 13.46 ?  61  MET   B N    1 
ATOM   4794 C CA   . MET   B 1 61  ? 54.891 -13.987 1.129   1.00 13.40 ?  61  MET   B CA   1 
ATOM   4795 C C    . MET   B 1 61  ? 54.750 -14.002 2.651   1.00 13.37 ?  61  MET   B C    1 
ATOM   4796 O O    . MET   B 1 61  ? 53.857 -13.352 3.209   1.00 13.11 ?  61  MET   B O    1 
ATOM   4797 C CB   . MET   B 1 61  ? 54.303 -15.252 0.498   1.00 13.21 ?  61  MET   B CB   1 
ATOM   4798 C CG   . MET   B 1 61  ? 52.856 -15.547 0.907   1.00 12.89 ?  61  MET   B CG   1 
ATOM   4799 S SD   . MET   B 1 61  ? 52.233 -17.063 0.152   1.00 13.72 ?  61  MET   B SD   1 
ATOM   4800 C CE   . MET   B 1 61  ? 51.977 -16.494 -1.522  1.00 15.01 ?  61  MET   B CE   1 
ATOM   4801 H H    . MET   B 1 61  ? 56.592 -14.542 0.285   1.00 16.15 ?  61  MET   B H    1 
ATOM   4802 H HA   . MET   B 1 61  ? 54.401 -13.229 0.772   1.00 16.08 ?  61  MET   B HA   1 
ATOM   4803 H HB2  . MET   B 1 61  ? 54.320 -15.157 -0.470  1.00 15.85 ?  61  MET   B HB2  1 
ATOM   4804 H HB3  . MET   B 1 61  ? 54.844 -16.013 0.759   1.00 15.85 ?  61  MET   B HB3  1 
ATOM   4805 H HG2  . MET   B 1 61  ? 52.810 -15.653 1.871   1.00 15.47 ?  61  MET   B HG2  1 
ATOM   4806 H HG3  . MET   B 1 61  ? 52.289 -14.811 0.626   1.00 15.47 ?  61  MET   B HG3  1 
ATOM   4807 H HE1  . MET   B 1 61  ? 51.604 -17.219 -2.048  1.00 18.01 ?  61  MET   B HE1  1 
ATOM   4808 H HE2  . MET   B 1 61  ? 51.359 -15.743 -1.514  1.00 18.01 ?  61  MET   B HE2  1 
ATOM   4809 H HE3  . MET   B 1 61  ? 52.826 -16.216 -1.897  1.00 18.01 ?  61  MET   B HE3  1 
ATOM   4810 N N    . GLN   B 1 62  ? 55.631 -14.720 3.348   1.00 13.10 ?  62  GLN   B N    1 
ATOM   4811 C CA   . GLN   B 1 62  ? 55.527 -14.780 4.803   1.00 13.75 ?  62  GLN   B CA   1 
ATOM   4812 C C    . GLN   B 1 62  ? 55.811 -13.426 5.440   1.00 14.05 ?  62  GLN   B C    1 
ATOM   4813 O O    . GLN   B 1 62  ? 55.128 -13.029 6.389   1.00 14.68 ?  62  GLN   B O    1 
ATOM   4814 C CB   . GLN   B 1 62  ? 56.478 -15.839 5.364   1.00 13.60 ?  62  GLN   B CB   1 
ATOM   4815 C CG   . GLN   B 1 62  ? 56.262 -16.107 6.842   1.00 14.14 ?  62  GLN   B CG   1 
ATOM   4816 C CD   . GLN   B 1 62  ? 54.888 -16.694 7.095   1.00 13.82 ?  62  GLN   B CD   1 
ATOM   4817 O OE1  . GLN   B 1 62  ? 54.626 -17.844 6.749   1.00 14.06 ?  62  GLN   B OE1  1 
ATOM   4818 N NE2  . GLN   B 1 62  ? 53.988 -15.898 7.659   1.00 14.28 ?  62  GLN   B NE2  1 
ATOM   4819 H H    . GLN   B 1 62  ? 56.280 -15.173 3.009   1.00 15.72 ?  62  GLN   B H    1 
ATOM   4820 H HA   . GLN   B 1 62  ? 54.622 -15.036 5.037   1.00 16.50 ?  62  GLN   B HA   1 
ATOM   4821 H HB2  . GLN   B 1 62  ? 56.344 -16.672 4.885   1.00 16.32 ?  62  GLN   B HB2  1 
ATOM   4822 H HB3  . GLN   B 1 62  ? 57.393 -15.535 5.244   1.00 16.32 ?  62  GLN   B HB3  1 
ATOM   4823 H HG2  . GLN   B 1 62  ? 56.928 -16.744 7.149   1.00 16.97 ?  62  GLN   B HG2  1 
ATOM   4824 H HG3  . GLN   B 1 62  ? 56.338 -15.277 7.335   1.00 16.97 ?  62  GLN   B HG3  1 
ATOM   4825 H HE21 . GLN   B 1 62  ? 54.206 -15.095 7.875   1.00 17.14 ?  62  GLN   B HE21 1 
ATOM   4826 H HE22 . GLN   B 1 62  ? 53.197 -16.189 7.811   1.00 17.14 ?  62  GLN   B HE22 1 
ATOM   4827 N N    . VAL   B 1 63  ? 56.831 -12.714 4.954   1.00 14.44 ?  63  VAL   B N    1 
ATOM   4828 C CA   . VAL   B 1 63  ? 57.140 -11.396 5.509   1.00 15.58 ?  63  VAL   B CA   1 
ATOM   4829 C C    . VAL   B 1 63  ? 55.948 -10.461 5.330   1.00 14.72 ?  63  VAL   B C    1 
ATOM   4830 O O    . VAL   B 1 63  ? 55.528 -9.765  6.264   1.00 15.43 ?  63  VAL   B O    1 
ATOM   4831 C CB   . VAL   B 1 63  ? 58.431 -10.837 4.883   1.00 17.10 ?  63  VAL   B CB   1 
ATOM   4832 C CG1  . VAL   B 1 63  ? 58.661 -9.389  5.324   1.00 18.06 ?  63  VAL   B CG1  1 
ATOM   4833 C CG2  . VAL   B 1 63  ? 59.623 -11.710 5.269   1.00 18.06 ?  63  VAL   B CG2  1 
ATOM   4834 H H    . VAL   B 1 63  ? 57.348 -12.969 4.312   1.00 17.33 ?  63  VAL   B H    1 
ATOM   4835 H HA   . VAL   B 1 63  ? 57.298 -11.496 6.459   1.00 18.70 ?  63  VAL   B HA   1 
ATOM   4836 H HB   . VAL   B 1 63  ? 58.355 -10.853 3.916   1.00 20.52 ?  63  VAL   B HB   1 
ATOM   4837 H HG11 . VAL   B 1 63  ? 59.577 -9.140  5.121   1.00 21.67 ?  63  VAL   B HG11 1 
ATOM   4838 H HG12 . VAL   B 1 63  ? 58.048 -8.813  4.847   1.00 21.67 ?  63  VAL   B HG12 1 
ATOM   4839 H HG13 . VAL   B 1 63  ? 58.507 -9.325  6.280   1.00 21.67 ?  63  VAL   B HG13 1 
ATOM   4840 H HG21 . VAL   B 1 63  ? 60.431 -11.333 4.883   1.00 21.67 ?  63  VAL   B HG21 1 
ATOM   4841 H HG22 . VAL   B 1 63  ? 59.700 -11.728 6.238   1.00 21.67 ?  63  VAL   B HG22 1 
ATOM   4842 H HG23 . VAL   B 1 63  ? 59.483 -12.608 4.933   1.00 21.67 ?  63  VAL   B HG23 1 
ATOM   4843 N N    . GLU   B 1 64  ? 55.385 -10.441 4.122   1.00 14.43 ?  64  GLU   B N    1 
ATOM   4844 C CA   . GLU   B 1 64  ? 54.212 -9.614  3.848   1.00 13.73 ?  64  GLU   B CA   1 
ATOM   4845 C C    . GLU   B 1 64  ? 53.033 -10.019 4.729   1.00 13.54 ?  64  GLU   B C    1 
ATOM   4846 O O    . GLU   B 1 64  ? 52.288 -9.159  5.229   1.00 14.16 ?  64  GLU   B O    1 
ATOM   4847 C CB   . GLU   B 1 64  ? 53.849 -9.764  2.369   1.00 14.34 ?  64  GLU   B CB   1 
ATOM   4848 C CG   . GLU   B 1 64  ? 52.582 -9.030  1.940   1.00 14.56 ?  64  GLU   B CG   1 
ATOM   4849 C CD   . GLU   B 1 64  ? 52.046 -9.517  0.603   1.00 15.27 ?  64  GLU   B CD   1 
ATOM   4850 O OE1  . GLU   B 1 64  ? 52.224 -10.720 0.278   1.00 15.80 ?  64  GLU   B OE1  1 
ATOM   4851 O OE2  . GLU   B 1 64  ? 51.423 -8.702  -0.120  1.00 15.94 -1 64  GLU   B OE2  1 
ATOM   4852 H H    . GLU   B 1 64  ? 55.667 -10.894 3.442   1.00 17.32 ?  64  GLU   B H    1 
ATOM   4853 H HA   . GLU   B 1 64  ? 54.424 -8.685  4.022   1.00 16.48 ?  64  GLU   B HA   1 
ATOM   4854 H HB2  . GLU   B 1 64  ? 54.579 -9.409  1.832   1.00 17.21 ?  64  GLU   B HB2  1 
ATOM   4855 H HB3  . GLU   B 1 64  ? 53.727 -10.701 2.172   1.00 17.21 ?  64  GLU   B HB3  1 
ATOM   4856 H HG2  . GLU   B 1 64  ? 51.883 -9.166  2.603   1.00 17.47 ?  64  GLU   B HG2  1 
ATOM   4857 H HG3  . GLU   B 1 64  ? 52.774 -8.084  1.857   1.00 17.47 ?  64  GLU   B HG3  1 
ATOM   4858 N N    . SER   B 1 65  ? 52.842 -11.328 4.915   1.00 13.26 ?  65  SER   B N    1 
ATOM   4859 C CA   . SER   B 1 65  ? 51.729 -11.828 5.715   1.00 13.36 ?  65  SER   B CA   1 
ATOM   4860 C C    . SER   B 1 65  ? 51.864 -11.428 7.179   1.00 13.74 ?  65  SER   B C    1 
ATOM   4861 O O    . SER   B 1 65  ? 50.868 -11.057 7.819   1.00 13.97 ?  65  SER   B O    1 
ATOM   4862 C CB   . SER   B 1 65  ? 51.648 -13.348 5.587   1.00 13.52 ?  65  SER   B CB   1 
ATOM   4863 O OG   . SER   B 1 65  ? 51.303 -13.748 4.271   1.00 13.85 ?  65  SER   B OG   1 
ATOM   4864 H H    . SER   B 1 65  ? 53.344 -11.951 4.585   1.00 15.92 ?  65  SER   B H    1 
ATOM   4865 H HA   . SER   B 1 65  ? 50.900 -11.458 5.375   1.00 16.03 ?  65  SER   B HA   1 
ATOM   4866 H HB2  . SER   B 1 65  ? 52.507 -13.733 5.806   1.00 16.22 ?  65  SER   B HB2  1 
ATOM   4867 H HB3  . SER   B 1 65  ? 50.970 -13.680 6.198   1.00 16.22 ?  65  SER   B HB3  1 
ATOM   4868 H HG   . SER   B 1 65  ? 51.874 -13.459 3.720   1.00 16.62 ?  65  SER   B HG   1 
ATOM   4869 N N    . ASP   B 1 66  ? 53.073 -11.530 7.740   1.00 14.02 ?  66  ASP   B N    1 
ATOM   4870 C CA   . ASP   B 1 66  ? 53.266 -11.141 9.136   1.00 14.18 ?  66  ASP   B CA   1 
ATOM   4871 C C    . ASP   B 1 66  ? 52.954 -9.664  9.343   1.00 14.61 ?  66  ASP   B C    1 
ATOM   4872 O O    . ASP   B 1 66  ? 52.377 -9.277  10.367  1.00 14.83 ?  66  ASP   B O    1 
ATOM   4873 C CB   . ASP   B 1 66  ? 54.695 -11.452 9.584   1.00 15.88 ?  66  ASP   B CB   1 
ATOM   4874 C CG   . ASP   B 1 66  ? 54.957 -12.945 9.750   1.00 17.87 ?  66  ASP   B CG   1 
ATOM   4875 O OD1  . ASP   B 1 66  ? 54.011 -13.761 9.677   1.00 18.55 ?  66  ASP   B OD1  1 
ATOM   4876 O OD2  . ASP   B 1 66  ? 56.132 -13.306 9.970   1.00 20.32 -1 66  ASP   B OD2  1 
ATOM   4877 H H    . ASP   B 1 66  ? 53.780 -11.819 7.345   1.00 16.83 ?  66  ASP   B H    1 
ATOM   4878 H HA   . ASP   B 1 66  ? 52.663 -11.648 9.697   1.00 17.01 ?  66  ASP   B HA   1 
ATOM   4879 H HB2  . ASP   B 1 66  ? 55.320 -11.113 8.923   1.00 19.05 ?  66  ASP   B HB2  1 
ATOM   4880 H HB3  . ASP   B 1 66  ? 54.862 -11.023 10.442  1.00 19.05 ?  66  ASP   B HB3  1 
ATOM   4881 N N    . ASP   B 1 67  ? 53.329 -8.819  8.383   1.00 14.22 ?  67  ASP   B N    1 
ATOM   4882 C CA   . ASP   B 1 67  ? 52.980 -7.409  8.476   1.00 14.69 ?  67  ASP   B CA   1 
ATOM   4883 C C    . ASP   B 1 67  ? 51.466 -7.202  8.393   1.00 14.78 ?  67  ASP   B C    1 
ATOM   4884 O O    . ASP   B 1 67  ? 50.903 -6.394  9.140   1.00 15.85 ?  67  ASP   B O    1 
ATOM   4885 C CB   . ASP   B 1 67  ? 53.695 -6.637  7.376   1.00 16.18 ?  67  ASP   B CB   1 
ATOM   4886 C CG   . ASP   B 1 67  ? 53.271 -5.197  7.337   1.00 17.54 ?  67  ASP   B CG   1 
ATOM   4887 O OD1  . ASP   B 1 67  ? 53.755 -4.396  8.171   1.00 19.02 ?  67  ASP   B OD1  1 
ATOM   4888 O OD2  . ASP   B 1 67  ? 52.418 -4.879  6.495   1.00 18.80 -1 67  ASP   B OD2  1 
ATOM   4889 H H    . ASP   B 1 67  ? 53.783 -9.034  7.684   1.00 17.07 ?  67  ASP   B H    1 
ATOM   4890 H HA   . ASP   B 1 67  ? 53.286 -7.061  9.327   1.00 17.63 ?  67  ASP   B HA   1 
ATOM   4891 H HB2  . ASP   B 1 67  ? 54.655 -6.665  7.533   1.00 19.41 ?  67  ASP   B HB2  1 
ATOM   4892 H HB3  . ASP   B 1 67  ? 53.494 -7.042  6.514   1.00 19.41 ?  67  ASP   B HB3  1 
ATOM   4893 N N    . TYR   B 1 68  ? 50.788 -7.930  7.500   1.00 14.16 ?  68  TYR   B N    1 
ATOM   4894 C CA   . TYR   B 1 68  ? 49.330 -7.851  7.427   1.00 15.20 ?  68  TYR   B CA   1 
ATOM   4895 C C    . TYR   B 1 68  ? 48.694 -8.201  8.769   1.00 14.85 ?  68  TYR   B C    1 
ATOM   4896 O O    . TYR   B 1 68  ? 47.763 -7.522  9.220   1.00 15.77 ?  68  TYR   B O    1 
ATOM   4897 C CB   . TYR   B 1 68  ? 48.795 -8.773  6.324   1.00 16.16 ?  68  TYR   B CB   1 
ATOM   4898 C CG   . TYR   B 1 68  ? 47.284 -8.927  6.377   1.00 17.07 ?  68  TYR   B CG   1 
ATOM   4899 C CD1  . TYR   B 1 68  ? 46.692 -9.888  7.193   1.00 17.87 ?  68  TYR   B CD1  1 
ATOM   4900 C CD2  . TYR   B 1 68  ? 46.455 -8.091  5.648   1.00 18.25 ?  68  TYR   B CD2  1 
ATOM   4901 C CE1  . TYR   B 1 68  ? 45.327 -10.011 7.277   1.00 18.95 ?  68  TYR   B CE1  1 
ATOM   4902 C CE2  . TYR   B 1 68  ? 45.072 -8.218  5.719   1.00 18.65 ?  68  TYR   B CE2  1 
ATOM   4903 C CZ   . TYR   B 1 68  ? 44.530 -9.176  6.538   1.00 19.03 ?  68  TYR   B CZ   1 
ATOM   4904 O OH   . TYR   B 1 68  ? 43.165 -9.300  6.628   1.00 20.53 ?  68  TYR   B OH   1 
ATOM   4905 H H    . TYR   B 1 68  ? 51.147 -8.480  6.939   1.00 16.99 ?  68  TYR   B H    1 
ATOM   4906 H HA   . TYR   B 1 68  ? 49.081 -6.944  7.209   1.00 18.24 ?  68  TYR   B HA   1 
ATOM   4907 H HB2  . TYR   B 1 68  ? 49.027 -8.400  5.462   1.00 19.39 ?  68  TYR   B HB2  1 
ATOM   4908 H HB3  . TYR   B 1 68  ? 49.192 -9.654  6.427   1.00 19.39 ?  68  TYR   B HB3  1 
ATOM   4909 H HD1  . TYR   B 1 68  ? 47.232 -10.457 7.699   1.00 21.44 ?  68  TYR   B HD1  1 
ATOM   4910 H HD2  . TYR   B 1 68  ? 46.832 -7.437  5.109   1.00 21.90 ?  68  TYR   B HD2  1 
ATOM   4911 H HE1  . TYR   B 1 68  ? 44.946 -10.669 7.818   1.00 22.74 ?  68  TYR   B HE1  1 
ATOM   4912 H HE2  . TYR   B 1 68  ? 44.522 -7.654  5.229   1.00 22.38 ?  68  TYR   B HE2  1 
ATOM   4913 H HH   . TYR   B 1 68  ? 42.780 -8.744  6.119   1.00 24.64 ?  68  TYR   B HH   1 
ATOM   4914 N N    . ILE   B 1 69  ? 49.172 -9.272  9.412   1.00 14.42 ?  69  ILE   B N    1 
ATOM   4915 C CA   . ILE   B 1 69  ? 48.611 -9.699  10.691  1.00 15.33 ?  69  ILE   B CA   1 
ATOM   4916 C C    . ILE   B 1 69  ? 48.868 -8.654  11.768  1.00 14.94 ?  69  ILE   B C    1 
ATOM   4917 O O    . ILE   B 1 69  ? 48.005 -8.379  12.608  1.00 15.39 ?  69  ILE   B O    1 
ATOM   4918 C CB   . ILE   B 1 69  ? 49.185 -11.075 11.083  1.00 15.90 ?  69  ILE   B CB   1 
ATOM   4919 C CG1  . ILE   B 1 69  ? 48.664 -12.178 10.151  1.00 16.34 ?  69  ILE   B CG1  1 
ATOM   4920 C CG2  . ILE   B 1 69  ? 48.897 -11.390 12.548  1.00 16.80 ?  69  ILE   B CG2  1 
ATOM   4921 C CD1  . ILE   B 1 69  ? 47.187 -12.492 10.297  1.00 16.89 ?  69  ILE   B CD1  1 
ATOM   4922 H H    . ILE   B 1 69  ? 49.815 -9.768  9.129   1.00 17.31 ?  69  ILE   B H    1 
ATOM   4923 H HA   . ILE   B 1 69  ? 47.652 -9.795  10.597  1.00 18.40 ?  69  ILE   B HA   1 
ATOM   4924 H HB   . ILE   B 1 69  ? 50.149 -11.033 10.979  1.00 19.08 ?  69  ILE   B HB   1 
ATOM   4925 H HG12 . ILE   B 1 69  ? 48.818 -11.901 9.233   1.00 19.61 ?  69  ILE   B HG12 1 
ATOM   4926 H HG13 . ILE   B 1 69  ? 49.160 -12.993 10.331  1.00 19.61 ?  69  ILE   B HG13 1 
ATOM   4927 H HG21 . ILE   B 1 69  ? 49.036 -12.339 12.696  1.00 20.16 ?  69  ILE   B HG21 1 
ATOM   4928 H HG22 . ILE   B 1 69  ? 49.502 -10.880 13.110  1.00 20.16 ?  69  ILE   B HG22 1 
ATOM   4929 H HG23 . ILE   B 1 69  ? 47.978 -11.156 12.747  1.00 20.16 ?  69  ILE   B HG23 1 
ATOM   4930 H HD11 . ILE   B 1 69  ? 46.960 -13.209 9.686   1.00 20.27 ?  69  ILE   B HD11 1 
ATOM   4931 H HD12 . ILE   B 1 69  ? 47.011 -12.769 11.210  1.00 20.27 ?  69  ILE   B HD12 1 
ATOM   4932 H HD13 . ILE   B 1 69  ? 46.671 -11.700 10.085  1.00 20.27 ?  69  ILE   B HD13 1 
ATOM   4933 N N    . ALA   B 1 70  ? 50.064 -8.069  11.785  1.00 15.16 ?  70  ALA   B N    1 
ATOM   4934 C CA   . ALA   B 1 70  ? 50.348 -7.039  12.779  1.00 15.21 ?  70  ALA   B CA   1 
ATOM   4935 C C    . ALA   B 1 70  ? 49.355 -5.888  12.669  1.00 15.75 ?  70  ALA   B C    1 
ATOM   4936 O O    . ALA   B 1 70  ? 48.910 -5.342  13.684  1.00 15.66 ?  70  ALA   B O    1 
ATOM   4937 C CB   . ALA   B 1 70  ? 51.786 -6.539  12.628  1.00 15.75 ?  70  ALA   B CB   1 
ATOM   4938 H H    . ALA   B 1 70  ? 50.706 -8.246  11.248  1.00 18.19 ?  70  ALA   B H    1 
ATOM   4939 H HA   . ALA   B 1 70  ? 50.264 -7.424  13.665  1.00 18.26 ?  70  ALA   B HA   1 
ATOM   4940 H HB1  . ALA   B 1 70  ? 51.967 -5.874  13.311  1.00 18.91 ?  70  ALA   B HB1  1 
ATOM   4941 H HB2  . ALA   B 1 70  ? 52.397 -7.290  12.733  1.00 18.91 ?  70  ALA   B HB2  1 
ATOM   4942 H HB3  . ALA   B 1 70  ? 51.898 -6.149  11.747  1.00 18.91 ?  70  ALA   B HB3  1 
ATOM   4943 N N    . THR   B 1 71  ? 48.985 -5.516  11.446  1.00 16.25 ?  71  THR   B N    1 
ATOM   4944 C CA   . THR   B 1 71  ? 48.091 -4.382  11.239  1.00 16.97 ?  71  THR   B CA   1 
ATOM   4945 C C    . THR   B 1 71  ? 46.624 -4.752  11.444  1.00 17.62 ?  71  THR   B C    1 
ATOM   4946 O O    . THR   B 1 71  ? 45.843 -3.939  11.958  1.00 19.22 ?  71  THR   B O    1 
ATOM   4947 C CB   . THR   B 1 71  ? 48.314 -3.811  9.837   1.00 18.97 ?  71  THR   B CB   1 
ATOM   4948 O OG1  . THR   B 1 71  ? 49.641 -3.278  9.745   1.00 21.12 ?  71  THR   B OG1  1 
ATOM   4949 C CG2  . THR   B 1 71  ? 47.302 -2.719  9.520   1.00 20.07 ?  71  THR   B CG2  1 
ATOM   4950 H H    . THR   B 1 71  ? 49.241 -5.902  10.722  1.00 19.49 ?  71  THR   B H    1 
ATOM   4951 H HA   . THR   B 1 71  ? 48.316 -3.686  11.877  1.00 20.37 ?  71  THR   B HA   1 
ATOM   4952 H HB   . THR   B 1 71  ? 48.218 -4.516  9.180   1.00 22.76 ?  71  THR   B HB   1 
ATOM   4953 H HG1  . THR   B 1 71  ? 49.774 -2.949  8.980   1.00 25.35 ?  71  THR   B HG1  1 
ATOM   4954 H HG21 . THR   B 1 71  ? 47.608 -2.193  8.762   1.00 24.09 ?  71  THR   B HG21 1 
ATOM   4955 H HG22 . THR   B 1 71  ? 46.444 -3.110  9.304   1.00 24.09 ?  71  THR   B HG22 1 
ATOM   4956 H HG23 . THR   B 1 71  ? 47.201 -2.129  10.285  1.00 24.09 ?  71  THR   B HG23 1 
ATOM   4957 N N    . ASN   B 1 72  ? 46.229 -5.964  11.047  1.00 17.34 ?  72  ASN   B N    1 
ATOM   4958 C CA   . ASN   B 1 72  ? 44.825 -6.321  10.915  1.00 17.38 ?  72  ASN   B CA   1 
ATOM   4959 C C    . ASN   B 1 72  ? 44.348 -7.420  11.853  1.00 18.25 ?  72  ASN   B C    1 
ATOM   4960 O O    . ASN   B 1 72  ? 43.132 -7.588  12.005  1.00 19.22 ?  72  ASN   B O    1 
ATOM   4961 C CB   . ASN   B 1 72  ? 44.529 -6.753  9.471   1.00 18.18 ?  72  ASN   B CB   1 
ATOM   4962 C CG   . ASN   B 1 72  ? 44.798 -5.652  8.477   1.00 19.26 ?  72  ASN   B CG   1 
ATOM   4963 O OD1  . ASN   B 1 72  ? 45.818 -5.650  7.783   1.00 20.41 ?  72  ASN   B OD1  1 
ATOM   4964 N ND2  . ASN   B 1 72  ? 43.901 -4.686  8.424   1.00 20.59 ?  72  ASN   B ND2  1 
ATOM   4965 H H    . ASN   B 1 72  ? 46.773 -6.608  10.847  1.00 20.81 ?  72  ASN   B H    1 
ATOM   4966 H HA   . ASN   B 1 72  ? 44.294 -5.533  11.093  1.00 20.86 ?  72  ASN   B HA   1 
ATOM   4967 H HB2  . ASN   B 1 72  ? 45.097 -7.511  9.244   1.00 21.82 ?  72  ASN   B HB2  1 
ATOM   4968 H HB3  . ASN   B 1 72  ? 43.597 -7.006  9.401   1.00 21.82 ?  72  ASN   B HB3  1 
ATOM   4969 H HD21 . ASN   B 1 72  ? 44.004 -4.035  7.873   1.00 24.71 ?  72  ASN   B HD21 1 
ATOM   4970 H HD22 . ASN   B 1 72  ? 43.202 -4.720  8.925   1.00 24.71 ?  72  ASN   B HD22 1 
ATOM   4971 N N    . GLY   B 1 73  ? 45.245 -8.170  12.479  1.00 17.33 ?  73  GLY   B N    1 
ATOM   4972 C CA   . GLY   B 1 73  ? 44.848 -9.314  13.263  1.00 16.77 ?  73  GLY   B CA   1 
ATOM   4973 C C    . GLY   B 1 73  ? 44.491 -10.498 12.392  1.00 15.20 ?  73  GLY   B C    1 
ATOM   4974 O O    . GLY   B 1 73  ? 44.479 -10.417 11.161  1.00 15.18 ?  73  GLY   B O    1 
ATOM   4975 H H    . GLY   B 1 73  ? 46.095 -8.026  12.466  1.00 20.80 ?  73  GLY   B H    1 
ATOM   4976 H HA2  . GLY   B 1 73  ? 45.575 -9.568  13.852  1.00 20.12 ?  73  GLY   B HA2  1 
ATOM   4977 H HA3  . GLY   B 1 73  ? 44.077 -9.082  13.804  1.00 20.12 ?  73  GLY   B HA3  1 
ATOM   4978 N N    . PRO   B 1 74  ? 44.184 -11.623 13.027  1.00 15.52 ?  74  PRO   B N    1 
ATOM   4979 C CA   . PRO   B 1 74  ? 43.939 -12.855 12.277  1.00 15.02 ?  74  PRO   B CA   1 
ATOM   4980 C C    . PRO   B 1 74  ? 42.635 -12.808 11.493  1.00 14.24 ?  74  PRO   B C    1 
ATOM   4981 O O    . PRO   B 1 74  ? 41.691 -12.075 11.814  1.00 15.70 ?  74  PRO   B O    1 
ATOM   4982 C CB   . PRO   B 1 74  ? 43.882 -13.921 13.378  1.00 16.03 ?  74  PRO   B CB   1 
ATOM   4983 C CG   . PRO   B 1 74  ? 43.436 -13.185 14.589  1.00 17.98 ?  74  PRO   B CG   1 
ATOM   4984 C CD   . PRO   B 1 74  ? 44.076 -11.832 14.481  1.00 17.17 ?  74  PRO   B CD   1 
ATOM   4985 H HA   . PRO   B 1 74  ? 44.684 -13.039 11.675  1.00 18.03 ?  74  PRO   B HA   1 
ATOM   4986 H HB2  . PRO   B 1 74  ? 43.241 -14.605 13.129  1.00 19.23 ?  74  PRO   B HB2  1 
ATOM   4987 H HB3  . PRO   B 1 74  ? 44.764 -14.302 13.507  1.00 19.23 ?  74  PRO   B HB3  1 
ATOM   4988 H HG2  . PRO   B 1 74  ? 42.469 -13.108 14.583  1.00 21.57 ?  74  PRO   B HG2  1 
ATOM   4989 H HG3  . PRO   B 1 74  ? 43.743 -13.648 15.380  1.00 21.57 ?  74  PRO   B HG3  1 
ATOM   4990 H HD2  . PRO   B 1 74  ? 43.505 -11.155 14.884  1.00 20.60 ?  74  PRO   B HD2  1 
ATOM   4991 H HD3  . PRO   B 1 74  ? 44.957 -11.838 14.886  1.00 20.60 ?  74  PRO   B HD3  1 
ATOM   4992 N N    . LEU   B 1 75  ? 42.605 -13.614 10.437  1.00 13.56 ?  75  LEU   B N    1 
ATOM   4993 C CA   . LEU   B 1 75  ? 41.387 -13.837 9.676   1.00 13.72 ?  75  LEU   B CA   1 
ATOM   4994 C C    . LEU   B 1 75  ? 40.417 -14.698 10.484  1.00 14.16 ?  75  LEU   B C    1 
ATOM   4995 O O    . LEU   B 1 75  ? 40.760 -15.254 11.529  1.00 15.19 ?  75  LEU   B O    1 
ATOM   4996 C CB   . LEU   B 1 75  ? 41.709 -14.544 8.358   1.00 14.06 ?  75  LEU   B CB   1 
ATOM   4997 C CG   . LEU   B 1 75  ? 42.555 -13.793 7.326   1.00 15.48 ?  75  LEU   B CG   1 
ATOM   4998 C CD1  . LEU   B 1 75  ? 42.726 -14.608 6.049   1.00 16.49 ?  75  LEU   B CD1  1 
ATOM   4999 C CD2  . LEU   B 1 75  ? 41.977 -12.440 7.006   1.00 19.06 ?  75  LEU   B CD2  1 
ATOM   5000 H H    . LEU   B 1 75  ? 43.285 -14.053 10.134  1.00 16.27 ?  75  LEU   B H    1 
ATOM   5001 H HA   . LEU   B 1 75  ? 40.958 -12.992 9.481   1.00 16.46 ?  75  LEU   B HA   1 
ATOM   5002 H HB2  . LEU   B 1 75  ? 42.184 -15.366 8.564   1.00 16.87 ?  75  LEU   B HB2  1 
ATOM   5003 H HB3  . LEU   B 1 75  ? 40.871 -14.768 7.921   1.00 16.87 ?  75  LEU   B HB3  1 
ATOM   5004 H HG   . LEU   B 1 75  ? 43.440 -13.652 7.697   1.00 18.58 ?  75  LEU   B HG   1 
ATOM   5005 H HD11 . LEU   B 1 75  ? 43.274 -14.104 5.419   1.00 19.79 ?  75  LEU   B HD11 1 
ATOM   5006 H HD12 . LEU   B 1 75  ? 43.167 -15.447 6.261   1.00 19.79 ?  75  LEU   B HD12 1 
ATOM   5007 H HD13 . LEU   B 1 75  ? 41.856 -14.781 5.659   1.00 19.79 ?  75  LEU   B HD13 1 
ATOM   5008 H HD21 . LEU   B 1 75  ? 42.485 -12.040 6.285   1.00 22.87 ?  75  LEU   B HD21 1 
ATOM   5009 H HD22 . LEU   B 1 75  ? 41.051 -12.549 6.741   1.00 22.87 ?  75  LEU   B HD22 1 
ATOM   5010 H HD23 . LEU   B 1 75  ? 42.031 -11.881 7.799   1.00 22.87 ?  75  LEU   B HD23 1 
ATOM   5011 N N    . LYS   B 1 76  ? 39.185 -14.805 9.978   1.00 15.42 ?  76  LYS   B N    1 
ATOM   5012 C CA   . LYS   B 1 76  ? 38.204 -15.770 10.457  1.00 16.92 ?  76  LYS   B CA   1 
ATOM   5013 C C    . LYS   B 1 76  ? 38.287 -17.038 9.610   1.00 14.98 ?  76  LYS   B C    1 
ATOM   5014 O O    . LYS   B 1 76  ? 38.554 -16.975 8.409   1.00 14.64 ?  76  LYS   B O    1 
ATOM   5015 C CB   . LYS   B 1 76  ? 36.782 -15.202 10.293  1.00 19.29 ?  76  LYS   B CB   1 
ATOM   5016 C CG   . LYS   B 1 76  ? 36.513 -13.805 10.884  1.00 21.36 ?  76  LYS   B CG   1 
ATOM   5017 C CD   . LYS   B 1 76  ? 35.101 -13.286 10.530  1.00 23.32 ?  76  LYS   B CD   1 
ATOM   5018 C CE   . LYS   B 1 76  ? 34.816 -11.928 11.161  1.00 25.20 ?  76  LYS   B CE   1 
ATOM   5019 N NZ   . LYS   B 1 76  ? 33.536 -11.333 10.683  1.00 25.93 ?  76  LYS   B NZ   1 
ATOM   5020 H H    . LYS   B 1 76  ? 38.892 -14.318 9.335   1.00 18.51 ?  76  LYS   B H    1 
ATOM   5021 H HA   . LYS   B 1 76  ? 38.363 -15.991 11.390  1.00 20.31 ?  76  LYS   B HA   1 
ATOM   5022 H HB2  . LYS   B 1 76  ? 36.585 -15.154 9.344   1.00 23.15 ?  76  LYS   B HB2  1 
ATOM   5023 H HB3  . LYS   B 1 76  ? 36.160 -15.814 10.717  1.00 23.15 ?  76  LYS   B HB3  1 
ATOM   5024 H HG2  . LYS   B 1 76  ? 36.589 -13.847 11.849  1.00 25.63 ?  76  LYS   B HG2  1 
ATOM   5025 H HG3  . LYS   B 1 76  ? 37.165 -13.178 10.526  1.00 25.63 ?  76  LYS   B HG3  1 
ATOM   5026 H HD2  . LYS   B 1 76  ? 35.030 -13.194 9.566   1.00 27.99 ?  76  LYS   B HD2  1 
ATOM   5027 H HD3  . LYS   B 1 76  ? 34.442 -13.918 10.855  1.00 27.99 ?  76  LYS   B HD3  1 
ATOM   5028 H HE2  . LYS   B 1 76  ? 34.757 -12.035 12.123  1.00 30.24 ?  76  LYS   B HE2  1 
ATOM   5029 H HE3  . LYS   B 1 76  ? 35.535 -11.318 10.937  1.00 30.24 ?  76  LYS   B HE3  1 
ATOM   5030 H HZ1  . LYS   B 1 76  ? 33.401 -10.543 11.072  1.00 31.11 ?  76  LYS   B HZ1  1 
ATOM   5031 H HZ2  . LYS   B 1 76  ? 33.562 -11.217 9.800   1.00 31.11 ?  76  LYS   B HZ2  1 
ATOM   5032 H HZ3  . LYS   B 1 76  ? 32.853 -11.871 10.882  1.00 31.11 ?  76  LYS   B HZ3  1 
ATOM   5033 N N    . VAL   B 1 77  ? 38.033 -18.198 10.233  1.00 15.40 ?  77  VAL   B N    1 
ATOM   5034 C CA   . VAL   B 1 77  ? 37.824 -19.406 9.442   1.00 15.30 ?  77  VAL   B CA   1 
ATOM   5035 C C    . VAL   B 1 77  ? 36.635 -19.164 8.525   1.00 14.02 ?  77  VAL   B C    1 
ATOM   5036 O O    . VAL   B 1 77  ? 35.568 -18.722 8.971   1.00 14.06 ?  77  VAL   B O    1 
ATOM   5037 C CB   . VAL   B 1 77  ? 37.622 -20.635 10.342  1.00 16.84 ?  77  VAL   B CB   1 
ATOM   5038 C CG1  . VAL   B 1 77  ? 37.359 -21.871 9.486   1.00 17.71 ?  77  VAL   B CG1  1 
ATOM   5039 C CG2  . VAL   B 1 77  ? 38.844 -20.859 11.237  1.00 18.65 ?  77  VAL   B CG2  1 
ATOM   5040 H H    . VAL   B 1 77  ? 37.982 -18.306 11.083  1.00 18.48 ?  77  VAL   B H    1 
ATOM   5041 H HA   . VAL   B 1 77  ? 38.601 -19.564 8.887   1.00 18.36 ?  77  VAL   B HA   1 
ATOM   5042 H HB   . VAL   B 1 77  ? 36.847 -20.493 10.910  1.00 20.20 ?  77  VAL   B HB   1 
ATOM   5043 H HG11 . VAL   B 1 77  ? 37.403 -22.658 10.051  1.00 21.26 ?  77  VAL   B HG11 1 
ATOM   5044 H HG12 . VAL   B 1 77  ? 36.474 -21.803 9.090   1.00 21.26 ?  77  VAL   B HG12 1 
ATOM   5045 H HG13 . VAL   B 1 77  ? 38.031 -21.923 8.792   1.00 21.26 ?  77  VAL   B HG13 1 
ATOM   5046 H HG21 . VAL   B 1 77  ? 38.705 -21.664 11.758  1.00 22.38 ?  77  VAL   B HG21 1 
ATOM   5047 H HG22 . VAL   B 1 77  ? 39.627 -20.955 10.676  1.00 22.38 ?  77  VAL   B HG22 1 
ATOM   5048 H HG23 . VAL   B 1 77  ? 38.944 -20.095 11.824  1.00 22.38 ?  77  VAL   B HG23 1 
ATOM   5049 N N    . GLY   B 1 78  ? 36.827 -19.429 7.234   1.00 13.73 ?  78  GLY   B N    1 
ATOM   5050 C CA   . GLY   B 1 78  ? 35.856 -19.115 6.213   1.00 13.40 ?  78  GLY   B CA   1 
ATOM   5051 C C    . GLY   B 1 78  ? 36.094 -17.797 5.518   1.00 12.97 ?  78  GLY   B C    1 
ATOM   5052 O O    . GLY   B 1 78  ? 35.405 -17.507 4.534   1.00 13.45 ?  78  GLY   B O    1 
ATOM   5053 H H    . GLY   B 1 78  ? 37.537 -19.806 6.923   1.00 16.47 ?  78  GLY   B H    1 
ATOM   5054 H HA2  . GLY   B 1 78  ? 35.862 -19.813 5.544   1.00 16.08 ?  78  GLY   B HA2  1 
ATOM   5055 H HA3  . GLY   B 1 78  ? 34.974 -19.086 6.615   1.00 16.08 ?  78  GLY   B HA3  1 
ATOM   5056 N N    . GLY   B 1 79  ? 37.041 -16.992 6.007   1.00 13.22 ?  79  GLY   B N    1 
ATOM   5057 C CA   . GLY   B 1 79  ? 37.336 -15.694 5.439   1.00 12.66 ?  79  GLY   B CA   1 
ATOM   5058 C C    . GLY   B 1 79  ? 38.574 -15.712 4.551   1.00 12.63 ?  79  GLY   B C    1 
ATOM   5059 O O    . GLY   B 1 79  ? 39.184 -16.747 4.296   1.00 13.05 ?  79  GLY   B O    1 
ATOM   5060 H H    . GLY   B 1 79  ? 37.537 -17.189 6.680   1.00 15.87 ?  79  GLY   B H    1 
ATOM   5061 H HA2  . GLY   B 1 79  ? 36.582 -15.394 4.906   1.00 15.19 ?  79  GLY   B HA2  1 
ATOM   5062 H HA3  . GLY   B 1 79  ? 37.480 -15.055 6.153   1.00 15.19 ?  79  GLY   B HA3  1 
ATOM   5063 N N    . SER   B 1 80  ? 38.946 -14.518 4.084   1.00 12.40 ?  80  SER   B N    1 
ATOM   5064 C CA   . SER   B 1 80  ? 40.052 -14.382 3.147   1.00 12.23 ?  80  SER   B CA   1 
ATOM   5065 C C    . SER   B 1 80  ? 40.625 -12.972 3.204   1.00 12.16 ?  80  SER   B C    1 
ATOM   5066 O O    . SER   B 1 80  ? 40.003 -12.039 3.719   1.00 13.64 ?  80  SER   B O    1 
ATOM   5067 C CB   . SER   B 1 80  ? 39.602 -14.681 1.711   1.00 13.03 ?  80  SER   B CB   1 
ATOM   5068 O OG   . SER   B 1 80  ? 38.767 -13.653 1.205   1.00 13.93 ?  80  SER   B OG   1 
ATOM   5069 H H    . SER   B 1 80  ? 38.574 -13.773 4.299   1.00 14.88 ?  80  SER   B H    1 
ATOM   5070 H HA   . SER   B 1 80  ? 40.746 -15.008 3.394   1.00 14.67 ?  80  SER   B HA   1 
ATOM   5071 H HB2  . SER   B 1 80  ? 40.384 -14.753 1.143   1.00 15.63 ?  80  SER   B HB2  1 
ATOM   5072 H HB3  . SER   B 1 80  ? 39.111 -15.520 1.703   1.00 15.63 ?  80  SER   B HB3  1 
ATOM   5073 H HG   . SER   B 1 80  ? 38.075 -13.585 1.685   1.00 16.72 ?  80  SER   B HG   1 
ATOM   5074 N N    . CYS   B 1 81  ? 41.812 -12.826 2.621   1.00 12.09 ?  81  CYS   B N    1 
ATOM   5075 C CA   . CYS   B 1 81  ? 42.358 -11.511 2.315   1.00 12.50 ?  81  CYS   B CA   1 
ATOM   5076 C C    . CYS   B 1 81  ? 43.130 -11.595 1.007   1.00 11.65 ?  81  CYS   B C    1 
ATOM   5077 O O    . CYS   B 1 81  ? 43.636 -12.660 0.631   1.00 12.71 ?  81  CYS   B O    1 
ATOM   5078 C CB   . CYS   B 1 81  ? 43.251 -10.968 3.438   1.00 13.11 ?  81  CYS   B CB   1 
ATOM   5079 S SG   . CYS   B 1 81  ? 44.773 -11.897 3.684   1.00 13.86 ?  81  CYS   B SG   1 
ATOM   5080 H H    . CYS   B 1 81  ? 42.324 -13.481 2.387   1.00 14.51 ?  81  CYS   B H    1 
ATOM   5081 H HA   . CYS   B 1 81  ? 41.625 -10.889 2.190   1.00 15.00 ?  81  CYS   B HA   1 
ATOM   5082 H HB2  . CYS   B 1 81  ? 43.495 -10.054 3.229   1.00 15.73 ?  81  CYS   B HB2  1 
ATOM   5083 H HB3  . CYS   B 1 81  ? 42.748 -10.988 4.271   1.00 15.73 ?  81  CYS   B HB3  1 
ATOM   5084 H HG   . CYS   B 1 81  ? 45.393 -11.401 4.589   1.00 16.63 ?  81  CYS   B HG   1 
ATOM   5085 N N    . VAL   B 1 82  ? 43.234 -10.452 0.333   1.00 11.93 ?  82  VAL   B N    1 
ATOM   5086 C CA   . VAL   B 1 82  ? 44.001 -10.326 -0.904  1.00 12.42 ?  82  VAL   B CA   1 
ATOM   5087 C C    . VAL   B 1 82  ? 45.342 -9.687  -0.579  1.00 12.70 ?  82  VAL   B C    1 
ATOM   5088 O O    . VAL   B 1 82  ? 45.391 -8.570  -0.043  1.00 13.68 ?  82  VAL   B O    1 
ATOM   5089 C CB   . VAL   B 1 82  ? 43.257 -9.485  -1.951  1.00 13.57 ?  82  VAL   B CB   1 
ATOM   5090 C CG1  . VAL   B 1 82  ? 44.095 -9.335  -3.220  1.00 14.85 ?  82  VAL   B CG1  1 
ATOM   5091 C CG2  . VAL   B 1 82  ? 41.894 -10.077 -2.252  1.00 14.43 ?  82  VAL   B CG2  1 
ATOM   5092 H H    . VAL   B 1 82  ? 42.855 -9.715  0.575   1.00 14.31 ?  82  VAL   B H    1 
ATOM   5093 H HA   . VAL   B 1 82  ? 44.162 -11.205 -1.274  1.00 14.90 ?  82  VAL   B HA   1 
ATOM   5094 H HB   . VAL   B 1 82  ? 43.116 -8.597  -1.592  1.00 16.28 ?  82  VAL   B HB   1 
ATOM   5095 H HG11 . VAL   B 1 82  ? 43.532 -8.995  -3.933  1.00 17.82 ?  82  VAL   B HG11 1 
ATOM   5096 H HG12 . VAL   B 1 82  ? 44.822 -8.712  -3.051  1.00 17.82 ?  82  VAL   B HG12 1 
ATOM   5097 H HG13 . VAL   B 1 82  ? 44.453 -10.202 -3.468  1.00 17.82 ?  82  VAL   B HG13 1 
ATOM   5098 H HG21 . VAL   B 1 82  ? 41.467 -9.557  -2.952  1.00 17.31 ?  82  VAL   B HG21 1 
ATOM   5099 H HG22 . VAL   B 1 82  ? 42.003 -10.996 -2.547  1.00 17.31 ?  82  VAL   B HG22 1 
ATOM   5100 H HG23 . VAL   B 1 82  ? 41.352 -10.053 -1.447  1.00 17.31 ?  82  VAL   B HG23 1 
ATOM   5101 N N    . LEU   B 1 83  ? 46.426 -10.361 -0.958  1.00 12.24 ?  83  LEU   B N    1 
ATOM   5102 C CA   . LEU   B 1 83  ? 47.781 -9.844  -0.833  1.00 12.07 ?  83  LEU   B CA   1 
ATOM   5103 C C    . LEU   B 1 83  ? 48.485 -9.983  -2.183  1.00 12.24 ?  83  LEU   B C    1 
ATOM   5104 O O    . LEU   B 1 83  ? 47.889 -10.406 -3.179  1.00 12.06 ?  83  LEU   B O    1 
ATOM   5105 C CB   . LEU   B 1 83  ? 48.527 -10.523 0.323   1.00 12.64 ?  83  LEU   B CB   1 
ATOM   5106 C CG   . LEU   B 1 83  ? 48.017 -10.163 1.722   1.00 14.04 ?  83  LEU   B CG   1 
ATOM   5107 C CD1  . LEU   B 1 83  ? 48.645 -11.028 2.789   1.00 14.77 ?  83  LEU   B CD1  1 
ATOM   5108 C CD2  . LEU   B 1 83  ? 48.233 -8.684  2.037   1.00 15.11 ?  83  LEU   B CD2  1 
ATOM   5109 H H    . LEU   B 1 83  ? 46.390 -11.154 -1.305  1.00 14.69 ?  83  LEU   B H    1 
ATOM   5110 H HA   . LEU   B 1 83  ? 47.722 -8.898  -0.635  1.00 14.48 ?  83  LEU   B HA   1 
ATOM   5111 H HB2  . LEU   B 1 83  ? 48.448 -11.482 0.217   1.00 15.17 ?  83  LEU   B HB2  1 
ATOM   5112 H HB3  . LEU   B 1 83  ? 49.458 -10.264 0.274   1.00 15.17 ?  83  LEU   B HB3  1 
ATOM   5113 H HG   . LEU   B 1 83  ? 47.063 -10.327 1.743   1.00 16.85 ?  83  LEU   B HG   1 
ATOM   5114 H HD11 . LEU   B 1 83  ? 48.283 -10.774 3.654   1.00 17.72 ?  83  LEU   B HD11 1 
ATOM   5115 H HD12 . LEU   B 1 83  ? 48.432 -11.961 2.608   1.00 17.72 ?  83  LEU   B HD12 1 
ATOM   5116 H HD13 . LEU   B 1 83  ? 49.604 -10.902 2.781   1.00 17.72 ?  83  LEU   B HD13 1 
ATOM   5117 H HD21 . LEU   B 1 83  ? 48.042 -8.532  2.974   1.00 18.13 ?  83  LEU   B HD21 1 
ATOM   5118 H HD22 . LEU   B 1 83  ? 49.155 -8.452  1.843   1.00 18.13 ?  83  LEU   B HD22 1 
ATOM   5119 H HD23 . LEU   B 1 83  ? 47.636 -8.154  1.485   1.00 18.13 ?  83  LEU   B HD23 1 
ATOM   5120 N N    . SER   B 1 84  ? 49.758 -9.601  -2.233  1.00 13.34 ?  84  SER   B N    1 
ATOM   5121 C CA   . SER   B 1 84  ? 50.495 -9.721  -3.482  1.00 13.56 ?  84  SER   B CA   1 
ATOM   5122 C C    . SER   B 1 84  ? 50.643 -11.180 -3.896  1.00 12.84 ?  84  SER   B C    1 
ATOM   5123 O O    . SER   B 1 84  ? 50.758 -12.079 -3.065  1.00 12.36 ?  84  SER   B O    1 
ATOM   5124 C CB   . SER   B 1 84  ? 51.888 -9.112  -3.337  1.00 15.63 ?  84  SER   B CB   1 
ATOM   5125 O OG   . SER   B 1 84  ? 52.645 -9.339  -4.513  1.00 17.44 ?  84  SER   B OG   1 
ATOM   5126 H H    . SER   B 1 84  ? 50.200 -9.264  -1.578  1.00 16.01 ?  84  SER   B H    1 
ATOM   5127 H HA   . SER   B 1 84  ? 50.023 -9.256  -4.186  1.00 16.27 ?  84  SER   B HA   1 
ATOM   5128 H HB2  . SER   B 1 84  ? 51.798 -8.156  -3.188  1.00 18.75 ?  84  SER   B HB2  1 
ATOM   5129 H HB3  . SER   B 1 84  ? 52.340 -9.524  -2.587  1.00 18.75 ?  84  SER   B HB3  1 
ATOM   5130 H HG   . SER   B 1 84  ? 53.408 -8.988  -4.433  1.00 20.93 ?  84  SER   B HG   1 
ATOM   5131 N N    . GLY   B 1 85  ? 50.716 -11.399 -5.206  1.00 13.60 ?  85  GLY   B N    1 
ATOM   5132 C CA   . GLY   B 1 85  ? 51.063 -12.685 -5.760  1.00 14.04 ?  85  GLY   B CA   1 
ATOM   5133 C C    . GLY   B 1 85  ? 52.532 -12.881 -6.055  1.00 13.28 ?  85  GLY   B C    1 
ATOM   5134 O O    . GLY   B 1 85  ? 52.915 -13.957 -6.514  1.00 13.88 ?  85  GLY   B O    1 
ATOM   5135 H H    . GLY   B 1 85  ? 50.578 -10.801 -5.798  1.00 16.32 ?  85  GLY   B H    1 
ATOM   5136 H HA2  . GLY   B 1 85  ? 50.793 -13.383 -5.139  1.00 16.85 ?  85  GLY   B HA2  1 
ATOM   5137 H HA3  . GLY   B 1 85  ? 50.575 -12.818 -6.584  1.00 16.85 ?  85  GLY   B HA3  1 
ATOM   5138 N N    . HIS   B 1 86  ? 53.384 -11.885 -5.822  1.00 13.50 ?  86  HIS   B N    1 
ATOM   5139 C CA   . HIS   B 1 86  ? 54.850 -12.052 -5.906  1.00 13.46 ?  86  HIS   B CA   1 
ATOM   5140 C C    . HIS   B 1 86  ? 55.218 -12.561 -7.297  1.00 13.53 ?  86  HIS   B C    1 
ATOM   5141 O O    . HIS   B 1 86  ? 54.827 -11.947 -8.302  1.00 14.39 ?  86  HIS   B O    1 
ATOM   5142 C CB   . HIS   B 1 86  ? 55.335 -12.902 -4.735  1.00 13.97 ?  86  HIS   B CB   1 
ATOM   5143 C CG   . HIS   B 1 86  ? 55.020 -12.301 -3.408  1.00 14.08 ?  86  HIS   B CG   1 
ATOM   5144 N ND1  . HIS   B 1 86  ? 55.850 -11.391 -2.789  1.00 15.59 ?  86  HIS   B ND1  1 
ATOM   5145 C CD2  . HIS   B 1 86  ? 53.942 -12.442 -2.601  1.00 14.39 ?  86  HIS   B CD2  1 
ATOM   5146 C CE1  . HIS   B 1 86  ? 55.295 -11.002 -1.657  1.00 15.14 ?  86  HIS   B CE1  1 
ATOM   5147 N NE2  . HIS   B 1 86  ? 54.136 -11.622 -1.519  1.00 14.57 ?  86  HIS   B NE2  1 
ATOM   5148 H H    . HIS   B 1 86  ? 53.144 -11.091 -5.616  1.00 16.20 ?  86  HIS   B H    1 
ATOM   5149 H HA   . HIS   B 1 86  ? 55.258 -11.180 -5.808  1.00 16.15 ?  86  HIS   B HA   1 
ATOM   5150 H HB2  . HIS   B 1 86  ? 54.913 -13.775 -4.780  1.00 16.77 ?  86  HIS   B HB2  1 
ATOM   5151 H HB3  . HIS   B 1 86  ? 56.300 -13.001 -4.794  1.00 16.77 ?  86  HIS   B HB3  1 
ATOM   5152 H HD2  . HIS   B 1 86  ? 53.199 -12.987 -2.758  1.00 17.26 ?  86  HIS   B HD2  1 
ATOM   5153 H HE1  . HIS   B 1 86  ? 55.661 -10.405 -1.050  1.00 18.17 ?  86  HIS   B HE1  1 
ATOM   5154 H HE2  . HIS   B 1 86  ? 53.596 -11.542 -0.852  1.00 17.48 ?  86  HIS   B HE2  1 
ATOM   5155 N N    . ASN   B 1 87  ? 55.977 -13.647 -7.409  1.00 13.86 ?  87  ASN   B N    1 
ATOM   5156 C CA   . ASN   B 1 87  ? 56.376 -14.216 -8.688  1.00 14.85 ?  87  ASN   B CA   1 
ATOM   5157 C C    . ASN   B 1 87  ? 55.399 -15.265 -9.189  1.00 14.58 ?  87  ASN   B C    1 
ATOM   5158 O O    . ASN   B 1 87  ? 55.717 -15.973 -10.150 1.00 16.43 ?  87  ASN   B O    1 
ATOM   5159 C CB   . ASN   B 1 87  ? 57.775 -14.835 -8.570  1.00 16.74 ?  87  ASN   B CB   1 
ATOM   5160 C CG   . ASN   B 1 87  ? 57.835 -15.951 -7.533  1.00 17.66 ?  87  ASN   B CG   1 
ATOM   5161 O OD1  . ASN   B 1 87  ? 57.195 -15.878 -6.480  1.00 16.99 ?  87  ASN   B OD1  1 
ATOM   5162 N ND2  . ASN   B 1 87  ? 58.586 -17.009 -7.844  1.00 19.59 ?  87  ASN   B ND2  1 
ATOM   5163 H H    . ASN   B 1 87  ? 56.282 -14.087 -6.736  1.00 16.64 ?  87  ASN   B H    1 
ATOM   5164 H HA   . ASN   B 1 87  ? 56.418 -13.508 -9.347  1.00 17.82 ?  87  ASN   B HA   1 
ATOM   5165 H HB2  . ASN   B 1 87  ? 58.029 -15.208 -9.431  1.00 20.08 ?  87  ASN   B HB2  1 
ATOM   5166 H HB3  . ASN   B 1 87  ? 58.406 -14.147 -8.309  1.00 20.08 ?  87  ASN   B HB3  1 
ATOM   5167 H HD21 . ASN   B 1 87  ? 58.652 -17.664 -7.295  1.00 23.51 ?  87  ASN   B HD21 1 
ATOM   5168 H HD22 . ASN   B 1 87  ? 59.014 -17.028 -8.592  1.00 23.51 ?  87  ASN   B HD22 1 
ATOM   5169 N N    . LEU   B 1 88  ? 54.221 -15.374 -8.566  1.00 13.76 ?  88  LEU   B N    1 
ATOM   5170 C CA   . LEU   B 1 88  ? 53.240 -16.405 -8.895  1.00 13.75 ?  88  LEU   B CA   1 
ATOM   5171 C C    . LEU   B 1 88  ? 52.010 -15.882 -9.616  1.00 13.44 ?  88  LEU   B C    1 
ATOM   5172 O O    . LEU   B 1 88  ? 51.409 -16.621 -10.406 1.00 15.05 ?  88  LEU   B O    1 
ATOM   5173 C CB   . LEU   B 1 88  ? 52.761 -17.095 -7.615  1.00 14.59 ?  88  LEU   B CB   1 
ATOM   5174 C CG   . LEU   B 1 88  ? 53.887 -17.733 -6.818  1.00 16.83 ?  88  LEU   B CG   1 
ATOM   5175 C CD1  . LEU   B 1 88  ? 53.388 -18.126 -5.440  1.00 18.36 ?  88  LEU   B CD1  1 
ATOM   5176 C CD2  . LEU   B 1 88  ? 54.422 -18.936 -7.569  1.00 19.93 ?  88  LEU   B CD2  1 
ATOM   5177 H H    . LEU   B 1 88  ? 53.964 -14.855 -7.924  1.00 16.51 ?  88  LEU   B H    1 
ATOM   5178 H HA   . LEU   B 1 88  ? 53.651 -17.068 -9.459  1.00 16.49 ?  88  LEU   B HA   1 
ATOM   5179 H HB2  . LEU   B 1 88  ? 52.322 -16.447 -7.043  1.00 17.51 ?  88  LEU   B HB2  1 
ATOM   5180 H HB3  . LEU   B 1 88  ? 52.131 -17.800 -7.853  1.00 17.51 ?  88  LEU   B HB3  1 
ATOM   5181 H HG   . LEU   B 1 88  ? 54.607 -17.093 -6.712  1.00 20.20 ?  88  LEU   B HG   1 
ATOM   5182 H HD11 . LEU   B 1 88  ? 54.036 -18.717 -5.027  1.00 22.03 ?  88  LEU   B HD11 1 
ATOM   5183 H HD12 . LEU   B 1 88  ? 53.279 -17.325 -4.905  1.00 22.03 ?  88  LEU   B HD12 1 
ATOM   5184 H HD13 . LEU   B 1 88  ? 52.537 -18.581 -5.534  1.00 22.03 ?  88  LEU   B HD13 1 
ATOM   5185 H HD21 . LEU   B 1 88  ? 55.058 -19.399 -7.004  1.00 23.92 ?  88  LEU   B HD21 1 
ATOM   5186 H HD22 . LEU   B 1 88  ? 53.683 -19.523 -7.790  1.00 23.92 ?  88  LEU   B HD22 1 
ATOM   5187 H HD23 . LEU   B 1 88  ? 54.858 -18.633 -8.381  1.00 23.92 ?  88  LEU   B HD23 1 
ATOM   5188 N N    . ALA   B 1 89  ? 51.606 -14.648 -9.342  1.00 12.65 ?  89  ALA   B N    1 
ATOM   5189 C CA   . ALA   B 1 89  ? 50.319 -14.149 -9.802  1.00 12.09 ?  89  ALA   B CA   1 
ATOM   5190 C C    . ALA   B 1 89  ? 50.284 -12.657 -9.517  1.00 12.42 ?  89  ALA   B C    1 
ATOM   5191 O O    . ALA   B 1 89  ? 51.115 -12.134 -8.775  1.00 13.47 ?  89  ALA   B O    1 
ATOM   5192 C CB   . ALA   B 1 89  ? 49.173 -14.824 -9.059  1.00 12.53 ?  89  ALA   B CB   1 
ATOM   5193 H H    . ALA   B 1 89  ? 52.052 -14.074 -8.875  1.00 15.18 ?  89  ALA   B H    1 
ATOM   5194 H HA   . ALA   B 1 89  ? 50.221 -14.295 -10.758 1.00 14.51 ?  89  ALA   B HA   1 
ATOM   5195 H HB1  . ALA   B 1 89  ? 48.330 -14.486 -9.408  1.00 15.03 ?  89  ALA   B HB1  1 
ATOM   5196 H HB2  . ALA   B 1 89  ? 49.228 -15.781 -9.205  1.00 15.03 ?  89  ALA   B HB2  1 
ATOM   5197 H HB3  . ALA   B 1 89  ? 49.247 -14.624 -8.118  1.00 15.03 ?  89  ALA   B HB3  1 
ATOM   5198 N N    . LYS   B 1 90  ? 49.287 -11.973 -10.078 1.00 13.43 ?  90  LYS   B N    1 
ATOM   5199 C CA   . LYS   B 1 90  ? 49.093 -10.583 -9.680  1.00 13.70 ?  90  LYS   B CA   1 
ATOM   5200 C C    . LYS   B 1 90  ? 48.774 -10.504 -8.191  1.00 13.51 ?  90  LYS   B C    1 
ATOM   5201 O O    . LYS   B 1 90  ? 49.415 -9.755  -7.443  1.00 14.73 ?  90  LYS   B O    1 
ATOM   5202 C CB   . LYS   B 1 90  ? 48.010 -9.924  -10.534 1.00 15.85 ?  90  LYS   B CB   1 
ATOM   5203 C CG   . LYS   B 1 90  ? 47.717 -8.477  -10.161 1.00 16.34 ?  90  LYS   B CG   1 
ATOM   5204 C CD   . LYS   B 1 90  ? 48.935 -7.591  -10.225 1.00 19.16 ?  90  LYS   B CD   1 
ATOM   5205 C CE   . LYS   B 1 90  ? 48.502 -6.153  -10.013 1.00 22.07 ?  90  LYS   B CE   1 
ATOM   5206 N NZ   . LYS   B 1 90  ? 49.661 -5.238  -9.901  1.00 21.85 ?  90  LYS   B NZ   1 
ATOM   5207 H H    . LYS   B 1 90  ? 48.733 -12.281 -10.661 1.00 16.11 ?  90  LYS   B H    1 
ATOM   5208 H HA   . LYS   B 1 90  ? 49.918 -10.105 -9.830  1.00 16.44 ?  90  LYS   B HA   1 
ATOM   5209 H HB2  . LYS   B 1 90  ? 48.296 -9.934  -11.463 1.00 19.03 ?  90  LYS   B HB2  1 
ATOM   5210 H HB3  . LYS   B 1 90  ? 47.185 -10.427 -10.444 1.00 19.03 ?  90  LYS   B HB3  1 
ATOM   5211 H HG2  . LYS   B 1 90  ? 47.054 -8.123  -10.776 1.00 19.60 ?  90  LYS   B HG2  1 
ATOM   5212 H HG3  . LYS   B 1 90  ? 47.367 -8.450  -9.254  1.00 19.60 ?  90  LYS   B HG3  1 
ATOM   5213 H HD2  . LYS   B 1 90  ? 49.558 -7.835  -9.521  1.00 22.99 ?  90  LYS   B HD2  1 
ATOM   5214 H HD3  . LYS   B 1 90  ? 49.353 -7.667  -11.096 1.00 22.99 ?  90  LYS   B HD3  1 
ATOM   5215 H HE2  . LYS   B 1 90  ? 47.966 -5.859  -10.768 1.00 26.48 ?  90  LYS   B HE2  1 
ATOM   5216 H HE3  . LYS   B 1 90  ? 47.990 -6.082  -9.193  1.00 26.48 ?  90  LYS   B HE3  1 
ATOM   5217 H HZ1  . LYS   B 1 90  ? 49.385 -4.396  -9.779  1.00 26.22 ?  90  LYS   B HZ1  1 
ATOM   5218 H HZ2  . LYS   B 1 90  ? 50.174 -5.470  -9.211  1.00 26.22 ?  90  LYS   B HZ2  1 
ATOM   5219 H HZ3  . LYS   B 1 90  ? 50.153 -5.267  -10.645 1.00 26.22 ?  90  LYS   B HZ3  1 
ATOM   5220 N N    . HIS   B 1 91  ? 47.808 -11.310 -7.741  1.00 12.09 ?  91  HIS   B N    1 
ATOM   5221 C CA   . HIS   B 1 91  ? 47.355 -11.341 -6.364  1.00 12.42 ?  91  HIS   B CA   1 
ATOM   5222 C C    . HIS   B 1 91  ? 47.359 -12.773 -5.853  1.00 11.72 ?  91  HIS   B C    1 
ATOM   5223 O O    . HIS   B 1 91  ? 47.122 -13.726 -6.609  1.00 12.16 ?  91  HIS   B O    1 
ATOM   5224 C CB   . HIS   B 1 91  ? 45.898 -10.876 -6.255  1.00 13.81 ?  91  HIS   B CB   1 
ATOM   5225 C CG   . HIS   B 1 91  ? 45.673 -9.476  -6.710  1.00 17.23 ?  91  HIS   B CG   1 
ATOM   5226 N ND1  . HIS   B 1 91  ? 46.267 -8.390  -6.103  1.00 20.06 ?  91  HIS   B ND1  1 
ATOM   5227 C CD2  . HIS   B 1 91  ? 44.897 -8.978  -7.697  1.00 19.78 ?  91  HIS   B CD2  1 
ATOM   5228 C CE1  . HIS   B 1 91  ? 45.878 -7.281  -6.709  1.00 21.06 ?  91  HIS   B CE1  1 
ATOM   5229 N NE2  . HIS   B 1 91  ? 45.043 -7.612  -7.678  1.00 21.52 ?  91  HIS   B NE2  1 
ATOM   5230 H H    . HIS   B 1 91  ? 47.380 -11.861 -8.240  1.00 14.51 ?  91  HIS   B H    1 
ATOM   5231 H HA   . HIS   B 1 91  ? 47.917 -10.782 -5.797  1.00 14.90 ?  91  HIS   B HA   1 
ATOM   5232 H HB2  . HIS   B 1 91  ? 45.343 -11.454 -6.797  1.00 16.57 ?  91  HIS   B HB2  1 
ATOM   5233 H HB3  . HIS   B 1 91  ? 45.619 -10.932 -5.324  1.00 16.57 ?  91  HIS   B HB3  1 
ATOM   5234 H HD1  . HIS   B 1 91  ? 46.810 -8.426  -5.435  1.00 24.07 ?  91  HIS   B HD1  1 
ATOM   5235 H HD2  . HIS   B 1 91  ? 44.368 -9.463  -8.285  1.00 23.74 ?  91  HIS   B HD2  1 
ATOM   5236 H HE1  . HIS   B 1 91  ? 46.144 -6.416  -6.485  1.00 25.27 ?  91  HIS   B HE1  1 
ATOM   5237 N N    . CYS   B 1 92  ? 47.561 -12.915 -4.550  1.00 11.38 ?  92  CYS   B N    1 
ATOM   5238 C CA   . CYS   B 1 92  ? 47.255 -14.149 -3.840  1.00 11.35 ?  92  CYS   B CA   1 
ATOM   5239 C C    . CYS   B 1 92  ? 46.029 -13.914 -2.964  1.00 10.94 ?  92  CYS   B C    1 
ATOM   5240 O O    . CYS   B 1 92  ? 46.022 -13.011 -2.117  1.00 11.92 ?  92  CYS   B O    1 
ATOM   5241 C CB   . CYS   B 1 92  ? 48.426 -14.596 -2.976  1.00 11.80 ?  92  CYS   B CB   1 
ATOM   5242 S SG   . CYS   B 1 92  ? 48.070 -16.140 -2.092  1.00 11.87 ?  92  CYS   B SG   1 
ATOM   5243 H H    . CYS   B 1 92  ? 47.891 -12.298 -4.044  1.00 13.65 ?  92  CYS   B H    1 
ATOM   5244 H HA   . CYS   B 1 92  ? 47.058 -14.849 -4.483  1.00 13.62 ?  92  CYS   B HA   1 
ATOM   5245 H HB2  . CYS   B 1 92  ? 49.199 -14.735 -3.535  1.00 14.17 ?  92  CYS   B HB2  1 
ATOM   5246 H HB3  . CYS   B 1 92  ? 48.604 -13.907 -2.314  1.00 14.17 ?  92  CYS   B HB3  1 
ATOM   5247 H HG   . CYS   B 1 92  ? 49.039 -16.451 -1.459  1.00 14.24 ?  92  CYS   B HG   1 
ATOM   5248 N N    . LEU   B 1 93  ? 44.994 -14.724 -3.174  1.00 10.80 ?  93  LEU   B N    1 
ATOM   5249 C CA   . LEU   B 1 93  ? 43.821 -14.737 -2.310  1.00 11.22 ?  93  LEU   B CA   1 
ATOM   5250 C C    . LEU   B 1 93  ? 44.047 -15.801 -1.243  1.00 10.44 ?  93  LEU   B C    1 
ATOM   5251 O O    . LEU   B 1 93  ? 43.996 -17.002 -1.535  1.00 11.20 ?  93  LEU   B O    1 
ATOM   5252 C CB   . LEU   B 1 93  ? 42.554 -15.033 -3.113  1.00 11.80 ?  93  LEU   B CB   1 
ATOM   5253 C CG   . LEU   B 1 93  ? 41.250 -15.053 -2.311  1.00 12.41 ?  93  LEU   B CG   1 
ATOM   5254 C CD1  . LEU   B 1 93  ? 40.900 -13.662 -1.826  1.00 12.58 ?  93  LEU   B CD1  1 
ATOM   5255 C CD2  . LEU   B 1 93  ? 40.112 -15.653 -3.127  1.00 12.21 ?  93  LEU   B CD2  1 
ATOM   5256 H H    . LEU   B 1 93  ? 44.952 -15.299 -3.824  1.00 12.96 ?  93  LEU   B H    1 
ATOM   5257 H HA   . LEU   B 1 93  ? 43.728 -13.874 -1.880  1.00 13.47 ?  93  LEU   B HA   1 
ATOM   5258 H HB2  . LEU   B 1 93  ? 42.461 -14.346 -3.796  1.00 14.16 ?  93  LEU   B HB2  1 
ATOM   5259 H HB3  . LEU   B 1 93  ? 42.652 -15.896 -3.535  1.00 14.16 ?  93  LEU   B HB3  1 
ATOM   5260 H HG   . LEU   B 1 93  ? 41.375 -15.613 -1.531  1.00 14.89 ?  93  LEU   B HG   1 
ATOM   5261 H HD11 . LEU   B 1 93  ? 40.047 -13.691 -1.373  1.00 15.10 ?  93  LEU   B HD11 1 
ATOM   5262 H HD12 . LEU   B 1 93  ? 41.592 -13.357 -1.218  1.00 15.10 ?  93  LEU   B HD12 1 
ATOM   5263 H HD13 . LEU   B 1 93  ? 40.850 -13.066 -2.593  1.00 15.10 ?  93  LEU   B HD13 1 
ATOM   5264 H HD21 . LEU   B 1 93  ? 39.301 -15.648 -2.591  1.00 14.65 ?  93  LEU   B HD21 1 
ATOM   5265 H HD22 . LEU   B 1 93  ? 39.977 -15.119 -3.928  1.00 14.65 ?  93  LEU   B HD22 1 
ATOM   5266 H HD23 . LEU   B 1 93  ? 40.338 -16.563 -3.373  1.00 14.65 ?  93  LEU   B HD23 1 
ATOM   5267 N N    . HIS   B 1 94  ? 44.325 -15.370 -0.020  1.00 10.39 ?  94  HIS   B N    1 
ATOM   5268 C CA   . HIS   B 1 94  ? 44.541 -16.280 1.099   1.00 10.82 ?  94  HIS   B CA   1 
ATOM   5269 C C    . HIS   B 1 94  ? 43.176 -16.631 1.678   1.00 11.17 ?  94  HIS   B C    1 
ATOM   5270 O O    . HIS   B 1 94  ? 42.511 -15.763 2.246   1.00 12.47 ?  94  HIS   B O    1 
ATOM   5271 C CB   . HIS   B 1 94  ? 45.412 -15.603 2.155   1.00 11.39 ?  94  HIS   B CB   1 
ATOM   5272 C CG   . HIS   B 1 94  ? 46.795 -15.296 1.684   1.00 11.45 ?  94  HIS   B CG   1 
ATOM   5273 N ND1  . HIS   B 1 94  ? 47.826 -16.206 1.764   1.00 11.60 ?  94  HIS   B ND1  1 
ATOM   5274 C CD2  . HIS   B 1 94  ? 47.300 -14.189 1.090   1.00 11.58 ?  94  HIS   B CD2  1 
ATOM   5275 C CE1  . HIS   B 1 94  ? 48.916 -15.659 1.256   1.00 11.74 ?  94  HIS   B CE1  1 
ATOM   5276 N NE2  . HIS   B 1 94  ? 48.625 -14.438 0.839   1.00 11.75 ?  94  HIS   B NE2  1 
ATOM   5277 H H    . HIS   B 1 94  ? 44.401 -14.535 0.189   1.00 12.47 ?  94  HIS   B H    1 
ATOM   5278 H HA   . HIS   B 1 94  ? 44.980 -17.089 0.789   1.00 12.99 ?  94  HIS   B HA   1 
ATOM   5279 H HB2  . HIS   B 1 94  ? 44.996 -14.768 2.412   1.00 13.67 ?  94  HIS   B HB2  1 
ATOM   5280 H HB3  . HIS   B 1 94  ? 45.484 -16.191 2.920   1.00 13.67 ?  94  HIS   B HB3  1 
ATOM   5281 H HD2  . HIS   B 1 94  ? 46.843 -13.406 0.894   1.00 13.90 ?  94  HIS   B HD2  1 
ATOM   5282 H HE1  . HIS   B 1 94  ? 49.746 -16.076 1.196   1.00 14.09 ?  94  HIS   B HE1  1 
ATOM   5283 H HE2  . HIS   B 1 94  ? 49.181 -13.894 0.471   1.00 14.10 ?  94  HIS   B HE2  1 
ATOM   5284 N N    . VAL   B 1 95  ? 42.744 -17.887 1.527   1.00 10.96 ?  95  VAL   B N    1 
ATOM   5285 C CA   . VAL   B 1 95  ? 41.417 -18.332 1.958   1.00 11.16 ?  95  VAL   B CA   1 
ATOM   5286 C C    . VAL   B 1 95  ? 41.583 -19.372 3.051   1.00 11.66 ?  95  VAL   B C    1 
ATOM   5287 O O    . VAL   B 1 95  ? 42.361 -20.318 2.890   1.00 11.87 ?  95  VAL   B O    1 
ATOM   5288 C CB   . VAL   B 1 95  ? 40.604 -18.929 0.795   1.00 11.55 ?  95  VAL   B CB   1 
ATOM   5289 C CG1  . VAL   B 1 95  ? 39.216 -19.381 1.271   1.00 12.71 ?  95  VAL   B CG1  1 
ATOM   5290 C CG2  . VAL   B 1 95  ? 40.488 -17.938 -0.340  1.00 11.74 ?  95  VAL   B CG2  1 
ATOM   5291 H H    . VAL   B 1 95  ? 43.210 -18.516 1.166   1.00 13.15 ?  95  VAL   B H    1 
ATOM   5292 H HA   . VAL   B 1 95  ? 40.921 -17.581 2.320   1.00 13.40 ?  95  VAL   B HA   1 
ATOM   5293 H HB   . VAL   B 1 95  ? 41.066 -19.709 0.454   1.00 13.86 ?  95  VAL   B HB   1 
ATOM   5294 H HG11 . VAL   B 1 95  ? 38.662 -19.579 0.494   1.00 15.25 ?  95  VAL   B HG11 1 
ATOM   5295 H HG12 . VAL   B 1 95  ? 39.307 -20.178 1.816   1.00 15.25 ?  95  VAL   B HG12 1 
ATOM   5296 H HG13 . VAL   B 1 95  ? 38.808 -18.669 1.787   1.00 15.25 ?  95  VAL   B HG13 1 
ATOM   5297 H HG21 . VAL   B 1 95  ? 39.908 -18.307 -1.024  1.00 14.08 ?  95  VAL   B HG21 1 
ATOM   5298 H HG22 . VAL   B 1 95  ? 40.111 -17.111 0.003   1.00 14.08 ?  95  VAL   B HG22 1 
ATOM   5299 H HG23 . VAL   B 1 95  ? 41.370 -17.774 -0.703  1.00 14.08 ?  95  VAL   B HG23 1 
ATOM   5300 N N    . VAL   B 1 96  ? 40.857 -19.201 4.151   1.00 11.69 ?  96  VAL   B N    1 
ATOM   5301 C CA   . VAL   B 1 96  ? 40.940 -20.114 5.292   1.00 12.05 ?  96  VAL   B CA   1 
ATOM   5302 C C    . VAL   B 1 96  ? 39.754 -21.077 5.245   1.00 12.62 ?  96  VAL   B C    1 
ATOM   5303 O O    . VAL   B 1 96  ? 38.633 -20.727 5.626   1.00 13.35 ?  96  VAL   B O    1 
ATOM   5304 C CB   . VAL   B 1 96  ? 40.982 -19.367 6.628   1.00 12.95 ?  96  VAL   B CB   1 
ATOM   5305 C CG1  . VAL   B 1 96  ? 41.169 -20.353 7.771   1.00 13.80 ?  96  VAL   B CG1  1 
ATOM   5306 C CG2  . VAL   B 1 96  ? 42.083 -18.312 6.640   1.00 13.66 ?  96  VAL   B CG2  1 
ATOM   5307 H H    . VAL   B 1 96  ? 40.296 -18.558 4.266   1.00 14.03 ?  96  VAL   B H    1 
ATOM   5308 H HA   . VAL   B 1 96  ? 41.755 -20.638 5.222   1.00 14.46 ?  96  VAL   B HA   1 
ATOM   5309 H HB   . VAL   B 1 96  ? 40.131 -18.918 6.764   1.00 15.54 ?  96  VAL   B HB   1 
ATOM   5310 H HG11 . VAL   B 1 96  ? 41.348 -19.858 8.589   1.00 16.56 ?  96  VAL   B HG11 1 
ATOM   5311 H HG12 . VAL   B 1 96  ? 40.364 -20.881 7.878   1.00 16.56 ?  96  VAL   B HG12 1 
ATOM   5312 H HG13 . VAL   B 1 96  ? 41.922 -20.931 7.570   1.00 16.56 ?  96  VAL   B HG13 1 
ATOM   5313 H HG21 . VAL   B 1 96  ? 42.117 -17.897 7.521   1.00 16.39 ?  96  VAL   B HG21 1 
ATOM   5314 H HG22 . VAL   B 1 96  ? 42.930 -18.728 6.439   1.00 16.39 ?  96  VAL   B HG22 1 
ATOM   5315 H HG23 . VAL   B 1 96  ? 41.878 -17.632 5.973   1.00 16.39 ?  96  VAL   B HG23 1 
ATOM   5316 N N    . GLY   B 1 97  ? 39.992 -22.309 4.807   1.00 12.37 ?  97  GLY   B N    1 
ATOM   5317 C CA   . GLY   B 1 97  ? 39.016 -23.366 4.960   1.00 13.30 ?  97  GLY   B CA   1 
ATOM   5318 C C    . GLY   B 1 97  ? 39.125 -23.974 6.341   1.00 14.16 ?  97  GLY   B C    1 
ATOM   5319 O O    . GLY   B 1 97  ? 40.157 -23.844 7.011   1.00 14.40 ?  97  GLY   B O    1 
ATOM   5320 H H    . GLY   B 1 97  ? 40.728 -22.555 4.420   1.00 14.84 ?  97  GLY   B H    1 
ATOM   5321 H HA2  . GLY   B 1 97  ? 38.126 -22.997 4.837   1.00 15.96 ?  97  GLY   B HA2  1 
ATOM   5322 H HA3  . GLY   B 1 97  ? 39.166 -24.051 4.289   1.00 15.96 ?  97  GLY   B HA3  1 
ATOM   5323 N N    . PRO   B 1 98  ? 38.079 -24.663 6.794   1.00 14.57 ?  98  PRO   B N    1 
ATOM   5324 C CA   . PRO   B 1 98  ? 38.167 -25.355 8.082   1.00 15.05 ?  98  PRO   B CA   1 
ATOM   5325 C C    . PRO   B 1 98  ? 39.197 -26.472 8.038   1.00 14.95 ?  98  PRO   B C    1 
ATOM   5326 O O    . PRO   B 1 98  ? 39.305 -27.207 7.058   1.00 15.45 ?  98  PRO   B O    1 
ATOM   5327 C CB   . PRO   B 1 98  ? 36.751 -25.907 8.285   1.00 15.36 ?  98  PRO   B CB   1 
ATOM   5328 C CG   . PRO   B 1 98  ? 36.193 -26.031 6.912   1.00 15.13 ?  98  PRO   B CG   1 
ATOM   5329 C CD   . PRO   B 1 98  ? 36.761 -24.856 6.159   1.00 14.53 ?  98  PRO   B CD   1 
ATOM   5330 H HA   . PRO   B 1 98  ? 38.390 -24.735 8.787   1.00 18.06 ?  98  PRO   B HA   1 
ATOM   5331 H HB2  . PRO   B 1 98  ? 36.801 -26.778 8.716   1.00 18.44 ?  98  PRO   B HB2  1 
ATOM   5332 H HB3  . PRO   B 1 98  ? 36.233 -25.288 8.813   1.00 18.44 ?  98  PRO   B HB3  1 
ATOM   5333 H HG2  . PRO   B 1 98  ? 36.485 -26.871 6.514   1.00 18.16 ?  98  PRO   B HG2  1 
ATOM   5334 H HG3  . PRO   B 1 98  ? 35.227 -25.987 6.948   1.00 18.16 ?  98  PRO   B HG3  1 
ATOM   5335 H HD2  . PRO   B 1 98  ? 36.860 -25.070 5.215   1.00 17.44 ?  98  PRO   B HD2  1 
ATOM   5336 H HD3  . PRO   B 1 98  ? 36.210 -24.069 6.288   1.00 17.44 ?  98  PRO   B HD3  1 
ATOM   5337 N N    . ASN   B 1 99  ? 39.945 -26.601 9.125   1.00 16.00 ?  99  ASN   B N    1 
ATOM   5338 C CA   . ASN   B 1 99  ? 40.923 -27.675 9.290   1.00 16.77 ?  99  ASN   B CA   1 
ATOM   5339 C C    . ASN   B 1 99  ? 40.285 -28.759 10.161  1.00 19.11 ?  99  ASN   B C    1 
ATOM   5340 O O    . ASN   B 1 99  ? 40.191 -28.615 11.383  1.00 20.17 ?  99  ASN   B O    1 
ATOM   5341 C CB   . ASN   B 1 99  ? 42.196 -27.120 9.915   1.00 17.33 ?  99  ASN   B CB   1 
ATOM   5342 C CG   . ASN   B 1 99  ? 43.327 -28.124 9.920   1.00 18.26 ?  99  ASN   B CG   1 
ATOM   5343 O OD1  . ASN   B 1 99  ? 43.101 -29.318 10.069  1.00 19.23 ?  99  ASN   B OD1  1 
ATOM   5344 N ND2  . ASN   B 1 99  ? 44.549 -27.645 9.748   1.00 18.38 ?  99  ASN   B ND2  1 
ATOM   5345 H H    . ASN   B 1 99  ? 39.910 -26.065 9.792   1.00 19.20 ?  99  ASN   B H    1 
ATOM   5346 H HA   . ASN   B 1 99  ? 41.141 -28.062 8.427   1.00 20.13 ?  99  ASN   B HA   1 
ATOM   5347 H HB2  . ASN   B 1 99  ? 42.482 -26.346 9.414   1.00 20.80 ?  99  ASN   B HB2  1 
ATOM   5348 H HB3  . ASN   B 1 99  ? 42.008 -26.873 10.837  1.00 20.80 ?  99  ASN   B HB3  1 
ATOM   5349 H HD21 . ASN   B 1 99  ? 45.222 -28.179 9.742   1.00 22.06 ?  99  ASN   B HD21 1 
ATOM   5350 H HD22 . ASN   B 1 99  ? 44.664 -26.801 9.646   1.00 22.06 ?  99  ASN   B HD22 1 
ATOM   5351 N N    A VAL   B 1 100 ? 39.828 -29.841 9.523   0.76 20.44 ?  100 VAL   B N    1 
ATOM   5352 N N    B VAL   B 1 100 ? 39.837 -29.840 9.516   0.24 20.91 ?  100 VAL   B N    1 
ATOM   5353 C CA   A VAL   B 1 100 ? 39.205 -30.939 10.261  0.76 23.32 ?  100 VAL   B CA   1 
ATOM   5354 C CA   B VAL   B 1 100 ? 39.213 -30.948 10.236  0.24 23.15 ?  100 VAL   B CA   1 
ATOM   5355 C C    A VAL   B 1 100 ? 40.207 -31.617 11.187  0.76 23.95 ?  100 VAL   B C    1 
ATOM   5356 C C    B VAL   B 1 100 ? 40.207 -31.609 11.181  0.24 23.92 ?  100 VAL   B C    1 
ATOM   5357 O O    A VAL   B 1 100 ? 39.831 -32.151 12.237  0.76 24.47 ?  100 VAL   B O    1 
ATOM   5358 O O    B VAL   B 1 100 ? 39.826 -32.106 12.248  0.24 24.28 ?  100 VAL   B O    1 
ATOM   5359 C CB   A VAL   B 1 100 ? 38.553 -31.940 9.284   0.76 26.12 ?  100 VAL   B CB   1 
ATOM   5360 C CB   B VAL   B 1 100 ? 38.605 -31.952 9.235   0.24 24.68 ?  100 VAL   B CB   1 
ATOM   5361 C CG1  A VAL   B 1 100 ? 38.078 -33.184 10.023  0.76 27.14 ?  100 VAL   B CG1  1 
ATOM   5362 C CG1  B VAL   B 1 100 ? 38.092 -33.192 9.955   0.24 25.24 ?  100 VAL   B CG1  1 
ATOM   5363 C CG2  A VAL   B 1 100 ? 37.392 -31.285 8.551   0.76 26.63 ?  100 VAL   B CG2  1 
ATOM   5364 C CG2  B VAL   B 1 100 ? 37.485 -31.295 8.443   0.24 24.99 ?  100 VAL   B CG2  1 
ATOM   5365 H H    A VAL   B 1 100 ? 39.850 -29.951 8.668   0.76 24.53 ?  100 VAL   B H    1 
ATOM   5366 H H    B VAL   B 1 100 ? 39.877 -29.952 8.664   0.24 25.09 ?  100 VAL   B H    1 
ATOM   5367 H HA   A VAL   B 1 100 ? 38.493 -30.572 10.812  0.76 27.99 ?  100 VAL   B HA   1 
ATOM   5368 H HA   B VAL   B 1 100 ? 38.486 -30.598 10.773  0.24 27.78 ?  100 VAL   B HA   1 
ATOM   5369 H HB   A VAL   B 1 100 ? 39.210 -32.217 8.627   0.76 31.34 ?  100 VAL   B HB   1 
ATOM   5370 H HB   B VAL   B 1 100 ? 39.291 -32.232 8.609   0.24 29.62 ?  100 VAL   B HB   1 
ATOM   5371 H HG11 A VAL   B 1 100 ? 37.481 -33.685 9.443   0.76 32.57 ?  100 VAL   B HG11 1 
ATOM   5372 H HG11 B VAL   B 1 100 ? 37.527 -33.697 9.347   0.24 30.28 ?  100 VAL   B HG11 1 
ATOM   5373 H HG12 A VAL   B 1 100 ? 38.844 -33.732 10.255  0.76 32.57 ?  100 VAL   B HG12 1 
ATOM   5374 H HG12 B VAL   B 1 100 ? 38.847 -33.736 10.229  0.24 30.28 ?  100 VAL   B HG12 1 
ATOM   5375 H HG13 A VAL   B 1 100 ? 37.605 -32.915 10.826  0.76 32.57 ?  100 VAL   B HG13 1 
ATOM   5376 H HG13 B VAL   B 1 100 ? 37.579 -32.918 10.730  0.24 30.28 ?  100 VAL   B HG13 1 
ATOM   5377 H HG21 A VAL   B 1 100 ? 36.994 -31.932 7.946   0.76 31.96 ?  100 VAL   B HG21 1 
ATOM   5378 H HG21 B VAL   B 1 100 ? 37.099 -31.948 7.839   0.24 29.98 ?  100 VAL   B HG21 1 
ATOM   5379 H HG22 A VAL   B 1 100 ? 36.731 -30.994 9.200   0.76 31.96 ?  100 VAL   B HG22 1 
ATOM   5380 H HG22 B VAL   B 1 100 ? 36.809 -30.975 9.061   0.24 29.98 ?  100 VAL   B HG22 1 
ATOM   5381 H HG23 A VAL   B 1 100 ? 37.722 -30.524 8.051   0.76 31.96 ?  100 VAL   B HG23 1 
ATOM   5382 H HG23 B VAL   B 1 100 ? 37.850 -30.552 7.939   0.24 29.98 ?  100 VAL   B HG23 1 
ATOM   5383 N N    . ASN   B 1 101 ? 41.488 -31.637 10.809  1.00 24.42 ?  101 ASN   B N    1 
ATOM   5384 C CA   . ASN   B 1 101 ? 42.518 -32.183 11.690  1.00 26.71 ?  101 ASN   B CA   1 
ATOM   5385 C C    . ASN   B 1 101 ? 42.707 -31.355 12.955  1.00 28.44 ?  101 ASN   B C    1 
ATOM   5386 O O    . ASN   B 1 101 ? 43.347 -31.835 13.900  1.00 29.85 ?  101 ASN   B O    1 
ATOM   5387 C CB   . ASN   B 1 101 ? 43.848 -32.307 10.943  1.00 26.86 ?  101 ASN   B CB   1 
ATOM   5388 C CG   . ASN   B 1 101 ? 43.848 -33.446 9.942   1.00 26.56 ?  101 ASN   B CG   1 
ATOM   5389 O OD1  . ASN   B 1 101 ? 43.195 -34.461 10.150  1.00 27.69 ?  101 ASN   B OD1  1 
ATOM   5390 N ND2  . ASN   B 1 101 ? 44.576 -33.277 8.848   1.00 26.15 ?  101 ASN   B ND2  1 
ATOM   5391 H H    A ASN   B 1 101 ? 41.776 -31.360 10.048  0.76 29.30 ?  101 ASN   B H    1 
ATOM   5392 H H    B ASN   B 1 101 ? 41.780 -31.354 10.052  0.24 29.30 ?  101 ASN   B H    1 
ATOM   5393 H HA   . ASN   B 1 101 ? 42.250 -33.071 11.963  1.00 32.05 ?  101 ASN   B HA   1 
ATOM   5394 H HB2  . ASN   B 1 101 ? 44.025 -31.487 10.459  1.00 32.23 ?  101 ASN   B HB2  1 
ATOM   5395 H HB3  . ASN   B 1 101 ? 44.557 -32.470 11.588  1.00 32.23 ?  101 ASN   B HB3  1 
ATOM   5396 H HD21 . ASN   B 1 101 ? 44.608 -33.900 8.255   1.00 31.37 ?  101 ASN   B HD21 1 
ATOM   5397 H HD22 . ASN   B 1 101 ? 45.014 -32.548 8.732   1.00 31.37 ?  101 ASN   B HD22 1 
ATOM   5398 N N    . LYS   B 1 102 ? 42.180 -30.129 12.986  1.00 30.18 ?  102 LYS   B N    1 
ATOM   5399 C CA   . LYS   B 1 102 ? 42.151 -29.296 14.182  1.00 33.06 ?  102 LYS   B CA   1 
ATOM   5400 C C    . LYS   B 1 102 ? 40.766 -29.243 14.814  1.00 32.55 ?  102 LYS   B C    1 
ATOM   5401 O O    . LYS   B 1 102 ? 40.542 -28.437 15.723  1.00 33.41 ?  102 LYS   B O    1 
ATOM   5402 C CB   . LYS   B 1 102 ? 42.596 -27.872 13.851  1.00 36.37 ?  102 LYS   B CB   1 
ATOM   5403 C CG   . LYS   B 1 102 ? 44.056 -27.717 13.473  1.00 39.95 ?  102 LYS   B CG   1 
ATOM   5404 C CD   . LYS   B 1 102 ? 44.299 -26.310 12.950  1.00 42.93 ?  102 LYS   B CD   1 
ATOM   5405 C CE   . LYS   B 1 102 ? 45.776 -25.972 12.867  1.00 45.32 ?  102 LYS   B CE   1 
ATOM   5406 N NZ   . LYS   B 1 102 ? 45.978 -24.575 12.383  1.00 46.81 ?  102 LYS   B NZ   1 
ATOM   5407 H H    . LYS   B 1 102 ? 41.821 -29.747 12.305  1.00 36.21 ?  102 LYS   B H    1 
ATOM   5408 H HA   . LYS   B 1 102 ? 42.769 -29.657 14.835  1.00 39.67 ?  102 LYS   B HA   1 
ATOM   5409 H HB2  . LYS   B 1 102 ? 42.064 -27.551 13.106  1.00 43.65 ?  102 LYS   B HB2  1 
ATOM   5410 H HB3  . LYS   B 1 102 ? 42.434 -27.312 14.627  1.00 43.65 ?  102 LYS   B HB3  1 
ATOM   5411 H HG2  . LYS   B 1 102 ? 44.613 -27.857 14.255  1.00 47.94 ?  102 LYS   B HG2  1 
ATOM   5412 H HG3  . LYS   B 1 102 ? 44.281 -28.351 12.774  1.00 47.94 ?  102 LYS   B HG3  1 
ATOM   5413 H HD2  . LYS   B 1 102 ? 43.921 -26.234 12.060  1.00 51.51 ?  102 LYS   B HD2  1 
ATOM   5414 H HD3  . LYS   B 1 102 ? 43.876 -25.673 13.547  1.00 51.51 ?  102 LYS   B HD3  1 
ATOM   5415 H HE2  . LYS   B 1 102 ? 46.174 -26.052 13.748  1.00 54.38 ?  102 LYS   B HE2  1 
ATOM   5416 H HE3  . LYS   B 1 102 ? 46.210 -26.577 12.245  1.00 54.38 ?  102 LYS   B HE3  1 
ATOM   5417 H HZ1  . LYS   B 1 102 ? 46.847 -24.391 12.339  1.00 56.17 ?  102 LYS   B HZ1  1 
ATOM   5418 H HZ2  . LYS   B 1 102 ? 45.620 -24.479 11.573  1.00 56.17 ?  102 LYS   B HZ2  1 
ATOM   5419 H HZ3  . LYS   B 1 102 ? 45.587 -24.001 12.941  1.00 56.17 ?  102 LYS   B HZ3  1 
ATOM   5420 N N    . GLY   B 1 103 ? 39.826 -30.057 14.341  1.00 31.30 ?  103 GLY   B N    1 
ATOM   5421 C CA   . GLY   B 1 103 ? 38.496 -30.097 14.913  1.00 30.91 ?  103 GLY   B CA   1 
ATOM   5422 C C    . GLY   B 1 103 ? 37.560 -29.002 14.457  1.00 29.77 ?  103 GLY   B C    1 
ATOM   5423 O O    . GLY   B 1 103 ? 36.481 -28.851 15.041  1.00 30.40 ?  103 GLY   B O    1 
ATOM   5424 H H    . GLY   B 1 103 ? 39.939 -30.596 13.683  1.00 37.56 ?  103 GLY   B H    1 
ATOM   5425 H HA2  . GLY   B 1 103 ? 38.085 -30.946 14.692  1.00 37.10 ?  103 GLY   B HA2  1 
ATOM   5426 H HA3  . GLY   B 1 103 ? 38.567 -30.043 15.880  1.00 37.10 ?  103 GLY   B HA3  1 
ATOM   5427 N N    A GLU   B 1 104 ? 37.938 -28.230 13.442  0.76 28.02 ?  104 GLU   B N    1 
ATOM   5428 N N    B GLU   B 1 104 ? 37.922 -28.242 13.428  0.24 29.34 ?  104 GLU   B N    1 
ATOM   5429 C CA   A GLU   B 1 104 ? 37.107 -27.129 12.982  0.76 26.31 ?  104 GLU   B CA   1 
ATOM   5430 C CA   B GLU   B 1 104 ? 37.074 -27.155 12.964  0.24 28.66 ?  104 GLU   B CA   1 
ATOM   5431 C C    A GLU   B 1 104 ? 35.925 -27.652 12.166  0.76 27.11 ?  104 GLU   B C    1 
ATOM   5432 C C    B GLU   B 1 104 ? 35.915 -27.689 12.128  0.24 28.60 ?  104 GLU   B C    1 
ATOM   5433 O O    A GLU   B 1 104 ? 35.961 -28.743 11.590  0.76 28.14 ?  104 GLU   B O    1 
ATOM   5434 O O    B GLU   B 1 104 ? 35.998 -28.760 11.519  0.24 28.82 ?  104 GLU   B O    1 
ATOM   5435 C CB   A GLU   B 1 104 ? 37.950 -26.130 12.186  0.76 24.72 ?  104 GLU   B CB   1 
ATOM   5436 C CB   B GLU   B 1 104 ? 37.902 -26.142 12.173  0.24 28.02 ?  104 GLU   B CB   1 
ATOM   5437 C CG   A GLU   B 1 104 ? 39.047 -25.506 13.037  0.76 23.01 ?  104 GLU   B CG   1 
ATOM   5438 C CG   B GLU   B 1 104 ? 38.980 -25.485 13.024  0.24 27.32 ?  104 GLU   B CG   1 
ATOM   5439 C CD   A GLU   B 1 104 ? 39.994 -24.614 12.268  0.76 21.41 ?  104 GLU   B CD   1 
ATOM   5440 C CD   B GLU   B 1 104 ? 39.936 -24.627 12.220  0.24 26.71 ?  104 GLU   B CD   1 
ATOM   5441 O OE1  A GLU   B 1 104 ? 39.999 -24.635 11.017  0.76 19.57 ?  104 GLU   B OE1  1 
ATOM   5442 O OE1  B GLU   B 1 104 ? 39.848 -24.628 10.975  0.24 26.27 ?  104 GLU   B OE1  1 
ATOM   5443 O OE2  A GLU   B 1 104 ? 40.748 -23.884 12.944  0.76 22.43 -1 104 GLU   B OE2  1 
ATOM   5444 O OE2  B GLU   B 1 104 ? 40.782 -23.951 12.843  0.24 26.87 -1 104 GLU   B OE2  1 
ATOM   5445 H H    A GLU   B 1 104 ? 38.677 -28.320 13.009  0.76 33.63 ?  104 GLU   B H    1 
ATOM   5446 H H    B GLU   B 1 104 ? 38.654 -28.334 12.987  0.24 35.21 ?  104 GLU   B H    1 
ATOM   5447 H HA   A GLU   B 1 104 ? 36.754 -26.660 13.756  0.76 31.57 ?  104 GLU   B HA   1 
ATOM   5448 H HA   B GLU   B 1 104 ? 36.702 -26.696 13.732  0.24 34.39 ?  104 GLU   B HA   1 
ATOM   5449 H HB2  A GLU   B 1 104 ? 38.371 -26.586 11.442  0.76 29.67 ?  104 GLU   B HB2  1 
ATOM   5450 H HB2  B GLU   B 1 104 ? 38.336 -26.594 11.433  0.24 33.62 ?  104 GLU   B HB2  1 
ATOM   5451 H HB3  A GLU   B 1 104 ? 37.380 -25.415 11.862  0.76 29.67 ?  104 GLU   B HB3  1 
ATOM   5452 H HB3  B GLU   B 1 104 ? 37.316 -25.444 11.839  0.24 33.62 ?  104 GLU   B HB3  1 
ATOM   5453 H HG2  A GLU   B 1 104 ? 38.643 -24.964 13.733  0.76 27.61 ?  104 GLU   B HG2  1 
ATOM   5454 H HG2  B GLU   B 1 104 ? 38.554 -24.919 13.688  0.24 32.78 ?  104 GLU   B HG2  1 
ATOM   5455 H HG3  A GLU   B 1 104 ? 39.580 -26.209 13.440  0.76 27.61 ?  104 GLU   B HG3  1 
ATOM   5456 H HG3  B GLU   B 1 104 ? 39.497 -26.177 13.466  0.24 32.78 ?  104 GLU   B HG3  1 
ATOM   5457 N N    A ASP   B 1 105 ? 34.861 -26.851 12.135  0.76 27.52 ?  105 ASP   B N    1 
ATOM   5458 N N    B ASP   B 1 105 ? 34.825 -26.925 12.109  0.24 28.40 ?  105 ASP   B N    1 
ATOM   5459 C CA   A ASP   B 1 105 ? 33.582 -27.297 11.595  0.76 28.30 ?  105 ASP   B CA   1 
ATOM   5460 C CA   B ASP   B 1 105 ? 33.568 -27.399 11.541  0.24 28.30 ?  105 ASP   B CA   1 
ATOM   5461 C C    A ASP   B 1 105 ? 33.634 -27.345 10.072  0.76 26.47 ?  105 ASP   B C    1 
ATOM   5462 C C    B ASP   B 1 105 ? 33.646 -27.416 10.019  0.24 27.41 ?  105 ASP   B C    1 
ATOM   5463 O O    A ASP   B 1 105 ? 33.783 -26.310 9.413   0.76 26.09 ?  105 ASP   B O    1 
ATOM   5464 O O    B ASP   B 1 105 ? 33.867 -26.378 9.386   0.24 27.23 ?  105 ASP   B O    1 
ATOM   5465 C CB   A ASP   B 1 105 ? 32.471 -26.359 12.064  0.76 31.58 ?  105 ASP   B CB   1 
ATOM   5466 C CB   B ASP   B 1 105 ? 32.422 -26.503 12.010  0.24 29.04 ?  105 ASP   B CB   1 
ATOM   5467 C CG   A ASP   B 1 105 ? 31.091 -26.829 11.643  0.76 34.01 ?  105 ASP   B CG   1 
ATOM   5468 C CG   B ASP   B 1 105 ? 31.058 -27.098 11.708  0.24 29.51 ?  105 ASP   B CG   1 
ATOM   5469 O OD1  A ASP   B 1 105 ? 30.989 -27.904 11.014  0.76 34.16 ?  105 ASP   B OD1  1 
ATOM   5470 O OD1  B ASP   B 1 105 ? 30.993 -28.080 10.938  0.24 29.60 ?  105 ASP   B OD1  1 
ATOM   5471 O OD2  A ASP   B 1 105 ? 30.103 -26.122 11.941  0.76 35.84 -1 105 ASP   B OD2  1 
ATOM   5472 O OD2  B ASP   B 1 105 ? 30.051 -26.594 12.249  0.24 29.66 -1 105 ASP   B OD2  1 
ATOM   5473 H H    A ASP   B 1 105 ? 34.859 -26.040 12.417  0.76 33.02 ?  105 ASP   B H    1 
ATOM   5474 H H    B ASP   B 1 105 ? 34.788 -26.125 12.417  0.24 34.08 ?  105 ASP   B H    1 
ATOM   5475 H HA   A ASP   B 1 105 ? 33.386 -28.187 11.926  0.76 33.96 ?  105 ASP   B HA   1 
ATOM   5476 H HA   B ASP   B 1 105 ? 33.390 -28.301 11.848  0.24 33.96 ?  105 ASP   B HA   1 
ATOM   5477 H HB2  A ASP   B 1 105 ? 32.499 -26.293 13.035  0.76 37.89 ?  105 ASP   B HB2  1 
ATOM   5478 H HB2  B ASP   B 1 105 ? 32.489 -26.376 12.971  0.24 34.85 ?  105 ASP   B HB2  1 
ATOM   5479 H HB3  A ASP   B 1 105 ? 32.609 -25.482 11.673  0.76 37.89 ?  105 ASP   B HB3  1 
ATOM   5480 H HB3  B ASP   B 1 105 ? 32.487 -25.642 11.561  0.24 34.85 ?  105 ASP   B HB3  1 
ATOM   5481 N N    A ILE   B 1 106 ? 33.487 -28.550 9.515   0.76 25.95 ?  106 ILE   B N    1 
ATOM   5482 N N    B ILE   B 1 106 ? 33.453 -28.601 9.432   0.24 26.88 ?  106 ILE   B N    1 
ATOM   5483 C CA   A ILE   B 1 106 ? 33.480 -28.734 8.069   0.76 25.10 ?  106 ILE   B CA   1 
ATOM   5484 C CA   B ILE   B 1 106 ? 33.465 -28.749 7.982   0.24 26.44 ?  106 ILE   B CA   1 
ATOM   5485 C C    A ILE   B 1 106 ? 32.379 -27.915 7.399   0.76 23.55 ?  106 ILE   B C    1 
ATOM   5486 C C    B ILE   B 1 106 ? 32.367 -27.926 7.319   0.24 25.90 ?  106 ILE   B C    1 
ATOM   5487 O O    A ILE   B 1 106 ? 32.481 -27.594 6.210   0.76 22.71 ?  106 ILE   B O    1 
ATOM   5488 O O    B ILE   B 1 106 ? 32.453 -27.630 6.122   0.24 25.72 ?  106 ILE   B O    1 
ATOM   5489 C CB   A ILE   B 1 106 ? 33.379 -30.243 7.742   0.76 26.20 ?  106 ILE   B CB   1 
ATOM   5490 C CB   B ILE   B 1 106 ? 33.368 -30.247 7.612   0.24 26.63 ?  106 ILE   B CB   1 
ATOM   5491 C CG1  A ILE   B 1 106 ? 33.638 -30.498 6.257   0.76 26.76 ?  106 ILE   B CG1  1 
ATOM   5492 C CG1  B ILE   B 1 106 ? 33.650 -30.464 6.123   0.24 26.76 ?  106 ILE   B CG1  1 
ATOM   5493 C CG2  A ILE   B 1 106 ? 32.017 -30.794 8.157   0.76 27.21 ?  106 ILE   B CG2  1 
ATOM   5494 C CG2  B ILE   B 1 106 ? 32.000 -30.805 7.981   0.24 26.90 ?  106 ILE   B CG2  1 
ATOM   5495 C CD1  A ILE   B 1 106 ? 35.004 -30.041 5.800   0.76 26.94 ?  106 ILE   B CD1  1 
ATOM   5496 C CD1  B ILE   B 1 106 ? 35.020 -29.994 5.690   0.24 26.85 ?  106 ILE   B CD1  1 
ATOM   5497 H H    A ILE   B 1 106 ? 33.393 -29.277 9.964   0.76 31.14 ?  106 ILE   B H    1 
ATOM   5498 H H    B ILE   B 1 106 ? 33.323 -29.335 9.858   0.24 32.26 ?  106 ILE   B H    1 
ATOM   5499 H HA   A ILE   B 1 106 ? 34.326 -28.415 7.728   0.76 30.11 ?  106 ILE   B HA   1 
ATOM   5500 H HA   B ILE   B 1 106 ? 34.312 -28.417 7.654   0.24 31.73 ?  106 ILE   B HA   1 
ATOM   5501 H HB   A ILE   B 1 106 ? 34.058 -30.711 8.253   0.76 31.44 ?  106 ILE   B HB   1 
ATOM   5502 H HB   B ILE   B 1 106 ? 34.036 -30.730 8.120   0.24 31.95 ?  106 ILE   B HB   1 
ATOM   5503 H HG12 A ILE   B 1 106 ? 33.575 -31.452 6.088   0.76 32.12 ?  106 ILE   B HG12 1 
ATOM   5504 H HG12 B ILE   B 1 106 ? 33.592 -31.415 5.930   0.24 32.12 ?  106 ILE   B HG12 1 
ATOM   5505 H HG13 A ILE   B 1 106 ? 32.975 -30.026 5.734   0.76 32.12 ?  106 ILE   B HG13 1 
ATOM   5506 H HG13 B ILE   B 1 106 ? 32.991 -29.983 5.601   0.24 32.12 ?  106 ILE   B HG13 1 
ATOM   5507 H HG21 A ILE   B 1 106 ? 32.030 -31.759 8.072   0.76 32.65 ?  106 ILE   B HG21 1 
ATOM   5508 H HG21 B ILE   B 1 106 ? 32.017 -31.770 7.884   0.24 32.28 ?  106 ILE   B HG21 1 
ATOM   5509 H HG22 A ILE   B 1 106 ? 31.844 -30.544 9.078   0.76 32.65 ?  106 ILE   B HG22 1 
ATOM   5510 H HG22 B ILE   B 1 106 ? 31.802 -30.569 8.901   0.24 32.28 ?  106 ILE   B HG22 1 
ATOM   5511 H HG23 A ILE   B 1 106 ? 31.335 -30.419 7.579   0.76 32.65 ?  106 ILE   B HG23 1 
ATOM   5512 H HG23 B ILE   B 1 106 ? 31.331 -30.425 7.391   0.24 32.28 ?  106 ILE   B HG23 1 
ATOM   5513 H HD11 A ILE   B 1 106 ? 35.208 -30.457 4.949   0.76 32.33 ?  106 ILE   B HD11 1 
ATOM   5514 H HD11 B ILE   B 1 106 ? 35.229 -30.385 4.829   0.24 32.22 ?  106 ILE   B HD11 1 
ATOM   5515 H HD12 A ILE   B 1 106 ? 35.001 -29.075 5.703   0.76 32.33 ?  106 ILE   B HD12 1 
ATOM   5516 H HD12 B ILE   B 1 106 ? 35.013 -29.026 5.620   0.24 32.22 ?  106 ILE   B HD12 1 
ATOM   5517 H HD13 A ILE   B 1 106 ? 35.665 -30.304 6.462   0.76 32.33 ?  106 ILE   B HD13 1 
ATOM   5518 H HD13 B ILE   B 1 106 ? 35.673 -30.276 6.349   0.24 32.22 ?  106 ILE   B HD13 1 
ATOM   5519 N N    A GLN   B 1 107 ? 31.329 -27.553 8.138   0.76 24.42 ?  107 GLN   B N    1 
ATOM   5520 N N    B GLN   B 1 107 ? 31.332 -27.543 8.071   0.24 25.89 ?  107 GLN   B N    1 
ATOM   5521 C CA   A GLN   B 1 107 ? 30.256 -26.744 7.568   0.76 24.94 ?  107 GLN   B CA   1 
ATOM   5522 C CA   B GLN   B 1 107 ? 30.255 -26.736 7.508   0.24 25.85 ?  107 GLN   B CA   1 
ATOM   5523 C C    A GLN   B 1 107 ? 30.753 -25.400 7.045   0.76 23.04 ?  107 GLN   B C    1 
ATOM   5524 C C    B GLN   B 1 107 ? 30.742 -25.369 7.045   0.24 23.49 ?  107 GLN   B C    1 
ATOM   5525 O O    A GLN   B 1 107 ? 30.129 -24.833 6.145   0.76 23.95 ?  107 GLN   B O    1 
ATOM   5526 O O    B GLN   B 1 107 ? 30.086 -24.744 6.204   0.24 23.90 ?  107 GLN   B O    1 
ATOM   5527 C CB   A GLN   B 1 107 ? 29.154 -26.538 8.612   0.76 28.83 ?  107 GLN   B CB   1 
ATOM   5528 C CB   B GLN   B 1 107 ? 29.133 -26.582 8.540   0.24 28.24 ?  107 GLN   B CB   1 
ATOM   5529 C CG   A GLN   B 1 107 ? 27.824 -26.053 8.046   0.76 32.84 ?  107 GLN   B CG   1 
ATOM   5530 C CG   B GLN   B 1 107 ? 27.808 -26.088 7.974   0.24 30.54 ?  107 GLN   B CG   1 
ATOM   5531 C CD   A GLN   B 1 107 ? 27.748 -24.541 7.918   0.76 35.63 ?  107 GLN   B CD   1 
ATOM   5532 C CD   B GLN   B 1 107 ? 27.689 -24.575 7.981   0.24 32.28 ?  107 GLN   B CD   1 
ATOM   5533 O OE1  A GLN   B 1 107 ? 28.583 -23.815 8.462   0.76 37.02 ?  107 GLN   B OE1  1 
ATOM   5534 O OE1  B GLN   B 1 107 ? 28.529 -23.875 8.549   0.24 32.92 ?  107 GLN   B OE1  1 
ATOM   5535 N NE2  A GLN   B 1 107 ? 26.737 -24.058 7.197   0.76 36.76 ?  107 GLN   B NE2  1 
ATOM   5536 N NE2  B GLN   B 1 107 ? 26.638 -24.062 7.351   0.24 32.97 ?  107 GLN   B NE2  1 
ATOM   5537 H H    A GLN   B 1 107 ? 31.218 -27.761 8.960   0.76 29.31 ?  107 GLN   B H    1 
ATOM   5538 H H    B GLN   B 1 107 ? 31.229 -27.740 8.899   0.24 31.06 ?  107 GLN   B H    1 
ATOM   5539 H HA   A GLN   B 1 107 ? 29.868 -27.227 6.820   0.76 29.93 ?  107 GLN   B HA   1 
ATOM   5540 H HA   B GLN   B 1 107 ? 29.887 -27.198 6.739   0.24 31.02 ?  107 GLN   B HA   1 
ATOM   5541 H HB2  A GLN   B 1 107 ? 28.991 -27.383 9.057   0.76 34.60 ?  107 GLN   B HB2  1 
ATOM   5542 H HB2  B GLN   B 1 107 ? 28.969 -27.445 8.946   0.24 33.89 ?  107 GLN   B HB2  1 
ATOM   5543 H HB3  A GLN   B 1 107 ? 29.459 -25.883 9.259   0.76 34.60 ?  107 GLN   B HB3  1 
ATOM   5544 H HB3  B GLN   B 1 107 ? 29.419 -25.952 9.220   0.24 33.89 ?  107 GLN   B HB3  1 
ATOM   5545 H HG2  A GLN   B 1 107 ? 27.696 -26.431 7.163   0.76 39.41 ?  107 GLN   B HG2  1 
ATOM   5546 H HG2  B GLN   B 1 107 ? 27.722 -26.390 7.057   0.24 36.64 ?  107 GLN   B HG2  1 
ATOM   5547 H HG3  A GLN   B 1 107 ? 27.106 -26.342 8.635   0.76 39.41 ?  107 GLN   B HG3  1 
ATOM   5548 H HG3  B GLN   B 1 107 ? 27.082 -26.451 8.510   0.24 36.64 ?  107 GLN   B HG3  1 
ATOM   5549 H HE21 A GLN   B 1 107 ? 26.173 -24.595 6.830   0.76 44.11 ?  107 GLN   B HE21 1 
ATOM   5550 H HE21 B GLN   B 1 107 ? 26.071 -24.581 6.964   0.24 39.56 ?  107 GLN   B HE21 1 
ATOM   5551 H HE22 A GLN   B 1 107 ? 26.645 -23.208 7.098   0.76 44.11 ?  107 GLN   B HE22 1 
ATOM   5552 H HE22 B GLN   B 1 107 ? 26.524 -23.210 7.330   0.24 39.56 ?  107 GLN   B HE22 1 
ATOM   5553 N N    . LEU   B 1 108 ? 31.876 -24.892 7.564   1.00 20.73 ?  108 LEU   B N    1 
ATOM   5554 C CA   . LEU   B 1 108 ? 32.426 -23.599 7.148   1.00 18.67 ?  108 LEU   B CA   1 
ATOM   5555 C C    . LEU   B 1 108 ? 33.079 -23.630 5.774   1.00 16.58 ?  108 LEU   B C    1 
ATOM   5556 O O    . LEU   B 1 108 ? 33.508 -22.574 5.280   1.00 16.12 ?  108 LEU   B O    1 
ATOM   5557 C CB   . LEU   B 1 108 ? 33.430 -23.107 8.188   1.00 19.56 ?  108 LEU   B CB   1 
ATOM   5558 C CG   . LEU   B 1 108 ? 32.808 -22.649 9.505   1.00 21.08 ?  108 LEU   B CG   1 
ATOM   5559 C CD1  . LEU   B 1 108 ? 33.846 -22.576 10.608  1.00 21.06 ?  108 LEU   B CD1  1 
ATOM   5560 C CD2  . LEU   B 1 108 ? 32.149 -21.294 9.318   1.00 22.48 ?  108 LEU   B CD2  1 
ATOM   5561 H H    A LEU   B 1 108 ? 32.335 -25.284 8.172   0.76 24.88 ?  108 LEU   B H    1 
ATOM   5562 H H    B LEU   B 1 108 ? 32.335 -25.297 8.164   0.24 24.88 ?  108 LEU   B H    1 
ATOM   5563 H HA   . LEU   B 1 108 ? 31.702 -22.961 7.110   1.00 22.40 ?  108 LEU   B HA   1 
ATOM   5564 H HB2  . LEU   B 1 108 ? 34.044 -23.825 8.395   1.00 23.47 ?  108 LEU   B HB2  1 
ATOM   5565 H HB3  . LEU   B 1 108 ? 33.911 -22.354 7.819   1.00 23.47 ?  108 LEU   B HB3  1 
ATOM   5566 H HG   . LEU   B 1 108 ? 32.121 -23.281 9.779   1.00 25.30 ?  108 LEU   B HG   1 
ATOM   5567 H HD11 . LEU   B 1 108 ? 33.414 -22.299 11.433  1.00 25.27 ?  108 LEU   B HD11 1 
ATOM   5568 H HD12 . LEU   B 1 108 ? 34.247 -23.450 10.722  1.00 25.27 ?  108 LEU   B HD12 1 
ATOM   5569 H HD13 . LEU   B 1 108 ? 34.524 -21.928 10.359  1.00 25.27 ?  108 LEU   B HD13 1 
ATOM   5570 H HD21 . LEU   B 1 108 ? 31.817 -20.980 10.175  1.00 26.97 ?  108 LEU   B HD21 1 
ATOM   5571 H HD22 . LEU   B 1 108 ? 32.803 -20.670 8.969   1.00 26.97 ?  108 LEU   B HD22 1 
ATOM   5572 H HD23 . LEU   B 1 108 ? 31.411 -21.383 8.693   1.00 26.97 ?  108 LEU   B HD23 1 
ATOM   5573 N N    . LEU   B 1 109 ? 33.149 -24.801 5.144   1.00 15.29 ?  109 LEU   B N    1 
ATOM   5574 C CA   . LEU   B 1 109 ? 33.776 -24.901 3.835   1.00 14.68 ?  109 LEU   B CA   1 
ATOM   5575 C C    . LEU   B 1 109 ? 33.012 -24.110 2.779   1.00 13.94 ?  109 LEU   B C    1 
ATOM   5576 O O    . LEU   B 1 109 ? 33.626 -23.519 1.883   1.00 13.97 ?  109 LEU   B O    1 
ATOM   5577 C CB   . LEU   B 1 109 ? 33.894 -26.373 3.443   1.00 14.94 ?  109 LEU   B CB   1 
ATOM   5578 C CG   . LEU   B 1 109 ? 34.680 -26.703 2.180   1.00 14.23 ?  109 LEU   B CG   1 
ATOM   5579 C CD1  . LEU   B 1 109 ? 36.056 -26.054 2.200   1.00 14.63 ?  109 LEU   B CD1  1 
ATOM   5580 C CD2  . LEU   B 1 109 ? 34.793 -28.216 2.038   1.00 15.41 ?  109 LEU   B CD2  1 
ATOM   5581 H H    . LEU   B 1 109 ? 32.850 -25.546 5.447   1.00 18.35 ?  109 LEU   B H    1 
ATOM   5582 H HA   . LEU   B 1 109 ? 34.671 -24.534 3.884   1.00 17.62 ?  109 LEU   B HA   1 
ATOM   5583 H HB2  . LEU   B 1 109 ? 34.325 -26.846 4.171   1.00 17.93 ?  109 LEU   B HB2  1 
ATOM   5584 H HB3  . LEU   B 1 109 ? 32.999 -26.728 3.320   1.00 17.93 ?  109 LEU   B HB3  1 
ATOM   5585 H HG   . LEU   B 1 109 ? 34.195 -26.375 1.404   1.00 17.08 ?  109 LEU   B HG   1 
ATOM   5586 H HD11 . LEU   B 1 109 ? 36.587 -26.418 1.473   1.00 17.55 ?  109 LEU   B HD11 1 
ATOM   5587 H HD12 . LEU   B 1 109 ? 35.952 -25.099 2.088   1.00 17.55 ?  109 LEU   B HD12 1 
ATOM   5588 H HD13 . LEU   B 1 109 ? 36.482 -26.250 3.049   1.00 17.55 ?  109 LEU   B HD13 1 
ATOM   5589 H HD21 . LEU   B 1 109 ? 35.357 -28.422 1.274   1.00 18.50 ?  109 LEU   B HD21 1 
ATOM   5590 H HD22 . LEU   B 1 109 ? 35.188 -28.581 2.845   1.00 18.50 ?  109 LEU   B HD22 1 
ATOM   5591 H HD23 . LEU   B 1 109 ? 33.908 -28.593 1.904   1.00 18.50 ?  109 LEU   B HD23 1 
ATOM   5592 N N    . LYS   B 1 110 ? 31.677 -24.075 2.860   1.00 13.69 ?  110 LYS   B N    1 
ATOM   5593 C CA   . LYS   B 1 110 ? 30.922 -23.314 1.868   1.00 13.52 ?  110 LYS   B CA   1 
ATOM   5594 C C    . LYS   B 1 110 ? 31.258 -21.826 1.958   1.00 13.17 ?  110 LYS   B C    1 
ATOM   5595 O O    . LYS   B 1 110 ? 31.507 -21.174 0.940   1.00 13.00 ?  110 LYS   B O    1 
ATOM   5596 C CB   . LYS   B 1 110 ? 29.418 -23.562 2.014   1.00 14.57 ?  110 LYS   B CB   1 
ATOM   5597 C CG   . LYS   B 1 110 ? 28.615 -22.952 0.867   1.00 14.57 ?  110 LYS   B CG   1 
ATOM   5598 C CD   . LYS   B 1 110 ? 27.143 -23.378 0.903   1.00 15.13 ?  110 LYS   B CD   1 
ATOM   5599 C CE   . LYS   B 1 110 ? 26.376 -22.846 -0.305  1.00 15.88 ?  110 LYS   B CE   1 
ATOM   5600 N NZ   . LYS   B 1 110 ? 26.718 -23.558 -1.563  1.00 15.77 ?  110 LYS   B NZ   1 
ATOM   5601 H H    . LYS   B 1 110 ? 31.204 -24.475 3.453   1.00 16.42 ?  110 LYS   B H    1 
ATOM   5602 H HA   . LYS   B 1 110 ? 31.185 -23.619 0.981   1.00 16.22 ?  110 LYS   B HA   1 
ATOM   5603 H HB2  . LYS   B 1 110 ? 29.256 -24.521 2.017   1.00 17.48 ?  110 LYS   B HB2  1 
ATOM   5604 H HB3  . LYS   B 1 110 ? 29.111 -23.170 2.842   1.00 17.48 ?  110 LYS   B HB3  1 
ATOM   5605 H HG2  . LYS   B 1 110 ? 28.644 -21.985 0.932   1.00 17.48 ?  110 LYS   B HG2  1 
ATOM   5606 H HG3  . LYS   B 1 110 ? 28.986 -23.241 0.020   1.00 17.48 ?  110 LYS   B HG3  1 
ATOM   5607 H HD2  . LYS   B 1 110 ? 27.088 -24.351 0.895   1.00 18.16 ?  110 LYS   B HD2  1 
ATOM   5608 H HD3  . LYS   B 1 110 ? 26.724 -23.030 1.709   1.00 18.16 ?  110 LYS   B HD3  1 
ATOM   5609 H HE2  . LYS   B 1 110 ? 25.427 -22.950 -0.150  1.00 19.05 ?  110 LYS   B HE2  1 
ATOM   5610 H HE3  . LYS   B 1 110 ? 26.595 -21.908 -0.423  1.00 19.05 ?  110 LYS   B HE3  1 
ATOM   5611 H HZ1  . LYS   B 1 110 ? 26.258 -23.218 -2.240  1.00 18.93 ?  110 LYS   B HZ1  1 
ATOM   5612 H HZ2  . LYS   B 1 110 ? 27.590 -23.474 -1.732  1.00 18.93 ?  110 LYS   B HZ2  1 
ATOM   5613 H HZ3  . LYS   B 1 110 ? 26.525 -24.424 -1.483  1.00 18.93 ?  110 LYS   B HZ3  1 
ATOM   5614 N N    . SER   B 1 111 ? 31.281 -21.276 3.176   1.00 13.75 ?  111 SER   B N    1 
ATOM   5615 C CA   . SER   B 1 111 ? 31.677 -19.876 3.351   1.00 13.32 ?  111 SER   B CA   1 
ATOM   5616 C C    . SER   B 1 111 ? 33.059 -19.617 2.768   1.00 13.05 ?  111 SER   B C    1 
ATOM   5617 O O    . SER   B 1 111 ? 33.283 -18.588 2.115   1.00 13.32 ?  111 SER   B O    1 
ATOM   5618 C CB   . SER   B 1 111 ? 31.659 -19.505 4.834   1.00 14.68 ?  111 SER   B CB   1 
ATOM   5619 O OG   . SER   B 1 111 ? 30.350 -19.525 5.359   1.00 16.69 ?  111 SER   B OG   1 
ATOM   5620 H H    . SER   B 1 111 ? 31.087 -21.692 3.903   1.00 16.50 ?  111 SER   B H    1 
ATOM   5621 H HA   . SER   B 1 111 ? 31.044 -19.310 2.889   1.00 15.98 ?  111 SER   B HA   1 
ATOM   5622 H HB2  . SER   B 1 111 ? 32.204 -20.138 5.327   1.00 17.61 ?  111 SER   B HB2  1 
ATOM   5623 H HB3  . SER   B 1 111 ? 32.017 -18.611 4.939   1.00 17.61 ?  111 SER   B HB3  1 
ATOM   5624 H HG   . SER   B 1 111 ? 30.361 -19.322 6.183   1.00 20.03 ?  111 SER   B HG   1 
ATOM   5625 N N    . ALA   B 1 112 ? 33.999 -20.533 2.998   1.00 13.29 ?  112 ALA   B N    1 
ATOM   5626 C CA   . ALA   B 1 112 ? 35.344 -20.362 2.457   1.00 12.74 ?  112 ALA   B CA   1 
ATOM   5627 C C    . ALA   B 1 112 ? 35.308 -20.267 0.932   1.00 12.00 ?  112 ALA   B C    1 
ATOM   5628 O O    . ALA   B 1 112 ? 35.931 -19.381 0.337   1.00 12.60 ?  112 ALA   B O    1 
ATOM   5629 C CB   . ALA   B 1 112 ? 36.245 -21.509 2.928   1.00 13.69 ?  112 ALA   B CB   1 
ATOM   5630 H H    . ALA   B 1 112 ? 33.886 -21.251 3.465   1.00 15.95 ?  112 ALA   B H    1 
ATOM   5631 H HA   . ALA   B 1 112 ? 35.714 -19.535 2.800   1.00 15.28 ?  112 ALA   B HA   1 
ATOM   5632 H HB1  . ALA   B 1 112 ? 37.138 -21.376 2.565   1.00 16.43 ?  112 ALA   B HB1  1 
ATOM   5633 H HB2  . ALA   B 1 112 ? 36.286 -21.502 3.900   1.00 16.43 ?  112 ALA   B HB2  1 
ATOM   5634 H HB3  . ALA   B 1 112 ? 35.883 -22.349 2.618   1.00 16.43 ?  112 ALA   B HB3  1 
ATOM   5635 N N    . TYR   B 1 113 ? 34.576 -21.172 0.277   1.00 12.31 ?  113 TYR   B N    1 
ATOM   5636 C CA   . TYR   B 1 113 ? 34.502 -21.116 -1.179  1.00 12.15 ?  113 TYR   B CA   1 
ATOM   5637 C C    . TYR   B 1 113 ? 33.792 -19.865 -1.693  1.00 11.88 ?  113 TYR   B C    1 
ATOM   5638 O O    . TYR   B 1 113 ? 34.059 -19.439 -2.819  1.00 11.86 ?  113 TYR   B O    1 
ATOM   5639 C CB   . TYR   B 1 113 ? 33.832 -22.377 -1.736  1.00 12.49 ?  113 TYR   B CB   1 
ATOM   5640 C CG   . TYR   B 1 113 ? 34.790 -23.531 -2.003  1.00 12.74 ?  113 TYR   B CG   1 
ATOM   5641 C CD1  . TYR   B 1 113 ? 35.774 -23.426 -2.973  1.00 13.19 ?  113 TYR   B CD1  1 
ATOM   5642 C CD2  . TYR   B 1 113 ? 34.693 -24.728 -1.302  1.00 12.86 ?  113 TYR   B CD2  1 
ATOM   5643 C CE1  . TYR   B 1 113 ? 36.650 -24.457 -3.223  1.00 13.14 ?  113 TYR   B CE1  1 
ATOM   5644 C CE2  . TYR   B 1 113 ? 35.564 -25.776 -1.549  1.00 13.01 ?  113 TYR   B CE2  1 
ATOM   5645 C CZ   . TYR   B 1 113 ? 36.537 -25.639 -2.514  1.00 13.03 ?  113 TYR   B CZ   1 
ATOM   5646 O OH   . TYR   B 1 113 ? 37.415 -26.656 -2.792  1.00 13.75 ?  113 TYR   B OH   1 
ATOM   5647 H H    . TYR   B 1 113 ? 34.115 -21.804 0.649   1.00 14.77 ?  113 TYR   B H    1 
ATOM   5648 H HA   . TYR   B 1 113 ? 35.403 -21.098 -1.517  1.00 14.58 ?  113 TYR   B HA   1 
ATOM   5649 H HB2  . TYR   B 1 113 ? 33.167 -22.693 -1.097  1.00 14.99 ?  113 TYR   B HB2  1 
ATOM   5650 H HB3  . TYR   B 1 113 ? 33.393 -22.155 -2.572  1.00 14.99 ?  113 TYR   B HB3  1 
ATOM   5651 H HD1  . TYR   B 1 113 ? 35.855 -22.629 -3.456  1.00 15.83 ?  113 TYR   B HD1  1 
ATOM   5652 H HD2  . TYR   B 1 113 ? 34.034 -24.824 -0.655  1.00 15.43 ?  113 TYR   B HD2  1 
ATOM   5653 H HE1  . TYR   B 1 113 ? 37.307 -24.362 -3.882  1.00 15.76 ?  113 TYR   B HE1  1 
ATOM   5654 H HE2  . TYR   B 1 113 ? 35.488 -26.572 -1.078  1.00 15.62 ?  113 TYR   B HE2  1 
ATOM   5655 H HH   . TYR   B 1 113 ? 37.246 -27.319 -2.306  1.00 16.50 ?  113 TYR   B HH   1 
ATOM   5656 N N    . GLU   B 1 114 ? 32.863 -19.294 -0.919  1.00 12.02 ?  114 GLU   B N    1 
ATOM   5657 C CA   . GLU   B 1 114 ? 32.180 -18.085 -1.378  1.00 12.00 ?  114 GLU   B CA   1 
ATOM   5658 C C    . GLU   B 1 114 ? 33.166 -16.964 -1.677  1.00 11.85 ?  114 GLU   B C    1 
ATOM   5659 O O    . GLU   B 1 114 ? 32.884 -16.101 -2.509  1.00 12.18 ?  114 GLU   B O    1 
ATOM   5660 C CB   . GLU   B 1 114 ? 31.127 -17.651 -0.357  1.00 12.79 ?  114 GLU   B CB   1 
ATOM   5661 C CG   . GLU   B 1 114 ? 29.900 -18.578 -0.422  1.00 12.70 ?  114 GLU   B CG   1 
ATOM   5662 C CD   . GLU   B 1 114 ? 28.885 -18.391 0.691   1.00 12.60 ?  114 GLU   B CD   1 
ATOM   5663 O OE1  . GLU   B 1 114 ? 29.177 -17.763 1.730   1.00 13.09 ?  114 GLU   B OE1  1 
ATOM   5664 O OE2  . GLU   B 1 114 ? 27.759 -18.922 0.527   1.00 13.72 -1 114 GLU   B OE2  1 
ATOM   5665 H H    . GLU   B 1 114 ? 32.602 -19.590 -0.151  1.00 14.42 ?  114 GLU   B H    1 
ATOM   5666 H HA   . GLU   B 1 114 ? 31.718 -18.284 -2.202  1.00 14.40 ?  114 GLU   B HA   1 
ATOM   5667 H HB2  . GLU   B 1 114 ? 31.500 -17.700 0.539   1.00 15.35 ?  114 GLU   B HB2  1 
ATOM   5668 H HB3  . GLU   B 1 114 ? 30.836 -16.748 -0.553  1.00 15.35 ?  114 GLU   B HB3  1 
ATOM   5669 H HG2  . GLU   B 1 114 ? 29.445 -18.427 -1.262  1.00 15.24 ?  114 GLU   B HG2  1 
ATOM   5670 H HG3  . GLU   B 1 114 ? 30.210 -19.499 -0.381  1.00 15.24 ?  114 GLU   B HG3  1 
ATOM   5671 N N    . ASN   B 1 115 ? 34.331 -16.957 -1.024  1.00 11.81 ?  115 ASN   B N    1 
ATOM   5672 C CA   . ASN   B 1 115 ? 35.319 -15.923 -1.319  1.00 11.40 ?  115 ASN   B CA   1 
ATOM   5673 C C    . ASN   B 1 115 ? 35.737 -15.939 -2.783  1.00 11.46 ?  115 ASN   B C    1 
ATOM   5674 O O    . ASN   B 1 115 ? 36.117 -14.897 -3.334  1.00 12.11 ?  115 ASN   B O    1 
ATOM   5675 C CB   . ASN   B 1 115 ? 36.557 -16.108 -0.434  1.00 12.40 ?  115 ASN   B CB   1 
ATOM   5676 C CG   . ASN   B 1 115 ? 36.284 -15.839 1.023   1.00 12.73 ?  115 ASN   B CG   1 
ATOM   5677 O OD1  . ASN   B 1 115 ? 36.275 -14.687 1.457   1.00 14.86 ?  115 ASN   B OD1  1 
ATOM   5678 N ND2  . ASN   B 1 115 ? 36.125 -16.903 1.804   1.00 13.07 ?  115 ASN   B ND2  1 
ATOM   5679 H H    . ASN   B 1 115 ? 34.563 -17.516 -0.407  1.00 14.17 ?  115 ASN   B H    1 
ATOM   5680 H HA   . ASN   B 1 115 ? 34.947 -15.052 -1.122  1.00 13.67 ?  115 ASN   B HA   1 
ATOM   5681 H HB2  . ASN   B 1 115 ? 36.875 -17.023 -0.518  1.00 14.88 ?  115 ASN   B HB2  1 
ATOM   5682 H HB3  . ASN   B 1 115 ? 37.250 -15.493 -0.721  1.00 14.88 ?  115 ASN   B HB3  1 
ATOM   5683 H HD21 . ASN   B 1 115 ? 35.980 -16.805 2.649   1.00 15.69 ?  115 ASN   B HD21 1 
ATOM   5684 H HD22 . ASN   B 1 115 ? 36.159 -17.698 1.471   1.00 15.69 ?  115 ASN   B HD22 1 
ATOM   5685 N N    . PHE   B 1 116 ? 35.717 -17.119 -3.421  1.00 11.29 ?  116 PHE   B N    1 
ATOM   5686 C CA   . PHE   B 1 116 ? 36.141 -17.211 -4.813  1.00 11.70 ?  116 PHE   B CA   1 
ATOM   5687 C C    . PHE   B 1 116 ? 35.239 -16.385 -5.724  1.00 11.47 ?  116 PHE   B C    1 
ATOM   5688 O O    . PHE   B 1 116 ? 35.673 -15.945 -6.795  1.00 11.86 ?  116 PHE   B O    1 
ATOM   5689 C CB   . PHE   B 1 116 ? 36.097 -18.664 -5.326  1.00 11.14 ?  116 PHE   B CB   1 
ATOM   5690 C CG   . PHE   B 1 116 ? 37.170 -19.616 -4.783  1.00 11.40 ?  116 PHE   B CG   1 
ATOM   5691 C CD1  . PHE   B 1 116 ? 37.827 -19.424 -3.581  1.00 12.39 ?  116 PHE   B CD1  1 
ATOM   5692 C CD2  . PHE   B 1 116 ? 37.473 -20.757 -5.519  1.00 11.86 ?  116 PHE   B CD2  1 
ATOM   5693 C CE1  . PHE   B 1 116 ? 38.760 -20.358 -3.129  1.00 12.40 ?  116 PHE   B CE1  1 
ATOM   5694 C CE2  . PHE   B 1 116 ? 38.407 -21.692 -5.075  1.00 12.06 ?  116 PHE   B CE2  1 
ATOM   5695 C CZ   . PHE   B 1 116 ? 39.046 -21.495 -3.885  1.00 12.00 ?  116 PHE   B CZ   1 
ATOM   5696 H H    . PHE   B 1 116 ? 35.458 -17.869 -3.076  1.00 13.55 ?  116 PHE   B H    1 
ATOM   5697 H HA   . PHE   B 1 116 ? 37.048 -16.888 -4.901  1.00 14.03 ?  116 PHE   B HA   1 
ATOM   5698 H HB2  . PHE   B 1 116 ? 35.225 -19.041 -5.097  1.00 13.37 ?  116 PHE   B HB2  1 
ATOM   5699 H HB3  . PHE   B 1 116 ? 36.182 -18.649 -6.295  1.00 13.37 ?  116 PHE   B HB3  1 
ATOM   5700 H HD1  . PHE   B 1 116 ? 37.629 -18.679 -3.065  1.00 14.87 ?  116 PHE   B HD1  1 
ATOM   5701 H HD2  . PHE   B 1 116 ? 37.028 -20.912 -6.327  1.00 14.23 ?  116 PHE   B HD2  1 
ATOM   5702 H HE1  . PHE   B 1 116 ? 39.203 -20.219 -2.324  1.00 14.89 ?  116 PHE   B HE1  1 
ATOM   5703 H HE2  . PHE   B 1 116 ? 38.595 -22.445 -5.590  1.00 14.47 ?  116 PHE   B HE2  1 
ATOM   5704 H HZ   . PHE   B 1 116 ? 39.684 -22.105 -3.591  1.00 14.40 ?  116 PHE   B HZ   1 
ATOM   5705 N N    . ASN   B 1 117 ? 33.973 -16.183 -5.337  1.00 11.80 ?  117 ASN   B N    1 
ATOM   5706 C CA   . ASN   B 1 117 ? 33.025 -15.476 -6.198  1.00 12.12 ?  117 ASN   B CA   1 
ATOM   5707 C C    . ASN   B 1 117 ? 33.341 -13.998 -6.352  1.00 12.48 ?  117 ASN   B C    1 
ATOM   5708 O O    . ASN   B 1 117 ? 32.747 -13.342 -7.213  1.00 13.49 ?  117 ASN   B O    1 
ATOM   5709 C CB   . ASN   B 1 117 ? 31.598 -15.696 -5.704  1.00 12.35 ?  117 ASN   B CB   1 
ATOM   5710 C CG   . ASN   B 1 117 ? 31.140 -17.103 -5.958  1.00 12.49 ?  117 ASN   B CG   1 
ATOM   5711 O OD1  . ASN   B 1 117 ? 31.498 -17.693 -6.980  1.00 13.57 ?  117 ASN   B OD1  1 
ATOM   5712 N ND2  . ASN   B 1 117 ? 30.397 -17.672 -5.020  1.00 12.66 ?  117 ASN   B ND2  1 
ATOM   5713 H H    . ASN   B 1 117 ? 33.649 -16.435 -4.577  1.00 14.16 ?  117 ASN   B H    1 
ATOM   5714 H HA   . ASN   B 1 117 ? 33.084 -15.874 -7.077  1.00 14.55 ?  117 ASN   B HA   1 
ATOM   5715 H HB2  . ASN   B 1 117 ? 31.558 -15.531 -4.745  1.00 14.81 ?  117 ASN   B HB2  1 
ATOM   5716 H HB3  . ASN   B 1 117 ? 31.002 -15.087 -6.169  1.00 14.81 ?  117 ASN   B HB3  1 
ATOM   5717 H HD21 . ASN   B 1 117 ? 30.114 -18.478 -5.122  1.00 15.19 ?  117 ASN   B HD21 1 
ATOM   5718 H HD22 . ASN   B 1 117 ? 30.174 -17.227 -4.316  1.00 15.19 ?  117 ASN   B HD22 1 
ATOM   5719 N N    . GLN   B 1 118 ? 34.270 -13.471 -5.570  1.00 11.99 ?  118 GLN   B N    1 
ATOM   5720 C CA   . GLN   B 1 118 ? 34.693 -12.083 -5.710  1.00 12.79 ?  118 GLN   B CA   1 
ATOM   5721 C C    . GLN   B 1 118 ? 35.765 -11.893 -6.781  1.00 12.79 ?  118 GLN   B C    1 
ATOM   5722 O O    . GLN   B 1 118 ? 36.240 -10.764 -6.960  1.00 14.38 ?  118 GLN   B O    1 
ATOM   5723 C CB   . GLN   B 1 118 ? 35.177 -11.549 -4.359  1.00 13.49 ?  118 GLN   B CB   1 
ATOM   5724 C CG   . GLN   B 1 118 ? 34.103 -11.588 -3.287  1.00 13.50 ?  118 GLN   B CG   1 
ATOM   5725 C CD   . GLN   B 1 118 ? 32.924 -10.679 -3.612  1.00 13.35 ?  118 GLN   B CD   1 
ATOM   5726 O OE1  . GLN   B 1 118 ? 33.106 -9.536  -4.055  1.00 14.01 ?  118 GLN   B OE1  1 
ATOM   5727 N NE2  . GLN   B 1 118 ? 31.709 -11.173 -3.398  1.00 13.90 ?  118 GLN   B NE2  1 
ATOM   5728 H H    . GLN   B 1 118 ? 34.693 -13.898 -4.950  1.00 14.38 ?  118 GLN   B H    1 
ATOM   5729 H HA   . GLN   B 1 118 ? 33.926 -11.557 -5.979  1.00 15.35 ?  118 GLN   B HA   1 
ATOM   5730 H HB2  . GLN   B 1 118 ? 35.923 -12.083 -4.054  1.00 16.19 ?  118 GLN   B HB2  1 
ATOM   5731 H HB3  . GLN   B 1 118 ? 35.453 -10.623 -4.466  1.00 16.19 ?  118 GLN   B HB3  1 
ATOM   5732 H HG2  . GLN   B 1 118 ? 33.772 -12.497 -3.203  1.00 16.20 ?  118 GLN   B HG2  1 
ATOM   5733 H HG3  . GLN   B 1 118 ? 34.487 -11.297 -2.444  1.00 16.20 ?  118 GLN   B HG3  1 
ATOM   5734 H HE21 . GLN   B 1 118 ? 31.618 -11.972 -3.085  1.00 16.68 ?  118 GLN   B HE21 1 
ATOM   5735 H HE22 . GLN   B 1 118 ? 31.019 -10.696 -3.566  1.00 16.68 ?  118 GLN   B HE22 1 
ATOM   5736 N N    . HIS   B 1 119 ? 36.131 -12.950 -7.513  1.00 12.19 ?  119 HIS   B N    1 
ATOM   5737 C CA   . HIS   B 1 119 ? 37.171 -12.893 -8.531  1.00 12.62 ?  119 HIS   B CA   1 
ATOM   5738 C C    . HIS   B 1 119 ? 36.692 -13.628 -9.768  1.00 12.43 ?  119 HIS   B C    1 
ATOM   5739 O O    . HIS   B 1 119 ? 36.187 -14.749 -9.665  1.00 13.00 ?  119 HIS   B O    1 
ATOM   5740 C CB   . HIS   B 1 119 ? 38.462 -13.515 -7.993  1.00 13.54 ?  119 HIS   B CB   1 
ATOM   5741 C CG   . HIS   B 1 119 ? 38.943 -12.824 -6.765  1.00 14.44 ?  119 HIS   B CG   1 
ATOM   5742 N ND1  . HIS   B 1 119 ? 39.729 -11.693 -6.814  1.00 16.20 ?  119 HIS   B ND1  1 
ATOM   5743 C CD2  . HIS   B 1 119 ? 38.659 -13.032 -5.460  1.00 15.74 ?  119 HIS   B CD2  1 
ATOM   5744 C CE1  . HIS   B 1 119 ? 39.940 -11.258 -5.585  1.00 17.45 ?  119 HIS   B CE1  1 
ATOM   5745 N NE2  . HIS   B 1 119 ? 39.297 -12.049 -4.746  1.00 17.54 ?  119 HIS   B NE2  1 
ATOM   5746 H H    . HIS   B 1 119 ? 35.772 -13.734 -7.437  1.00 14.63 ?  119 HIS   B H    1 
ATOM   5747 H HA   . HIS   B 1 119 ? 37.342 -11.967 -8.768  1.00 15.15 ?  119 HIS   B HA   1 
ATOM   5748 H HB2  . HIS   B 1 119 ? 38.301 -14.444 -7.782  1.00 16.24 ?  119 HIS   B HB2  1 
ATOM   5749 H HB3  . HIS   B 1 119 ? 39.151 -13.441 -8.677  1.00 16.24 ?  119 HIS   B HB3  1 
ATOM   5750 H HD2  . HIS   B 1 119 ? 38.138 -13.722 -5.114  1.00 18.88 ?  119 HIS   B HD2  1 
ATOM   5751 H HE1  . HIS   B 1 119 ? 40.465 -10.527 -5.349  1.00 20.94 ?  119 HIS   B HE1  1 
ATOM   5752 H HE2  . HIS   B 1 119 ? 39.308 -11.983 -3.889  1.00 21.05 ?  119 HIS   B HE2  1 
ATOM   5753 N N    . GLU   B 1 120 ? 36.849 -13.015 -10.939 1.00 12.87 ?  120 GLU   B N    1 
ATOM   5754 C CA   . GLU   B 1 120 ? 36.256 -13.600 -12.136 1.00 14.54 ?  120 GLU   B CA   1 
ATOM   5755 C C    . GLU   B 1 120 ? 36.930 -14.901 -12.549 1.00 13.41 ?  120 GLU   B C    1 
ATOM   5756 O O    . GLU   B 1 120 ? 36.266 -15.767 -13.129 1.00 13.72 ?  120 GLU   B O    1 
ATOM   5757 C CB   . GLU   B 1 120 ? 36.253 -12.594 -13.285 1.00 19.33 ?  120 GLU   B CB   1 
ATOM   5758 C CG   . GLU   B 1 120 ? 35.301 -11.434 -13.054 1.00 24.59 ?  120 GLU   B CG   1 
ATOM   5759 C CD   . GLU   B 1 120 ? 35.138 -10.547 -14.270 1.00 30.73 ?  120 GLU   B CD   1 
ATOM   5760 O OE1  . GLU   B 1 120 ? 36.134 -10.339 -14.996 1.00 33.42 ?  120 GLU   B OE1  1 
ATOM   5761 O OE2  . GLU   B 1 120 ? 34.010 -10.062 -14.498 1.00 34.46 -1 120 GLU   B OE2  1 
ATOM   5762 H H    . GLU   B 1 120 ? 37.280 -12.277 -11.068 1.00 15.44 ?  120 GLU   B H    1 
ATOM   5763 H HA   . GLU   B 1 120 ? 35.336 -13.813 -11.941 1.00 17.44 ?  120 GLU   B HA   1 
ATOM   5764 H HB2  . GLU   B 1 120 ? 37.142 -12.230 -13.396 1.00 23.20 ?  120 GLU   B HB2  1 
ATOM   5765 H HB3  . GLU   B 1 120 ? 35.974 -13.046 -14.100 1.00 23.20 ?  120 GLU   B HB3  1 
ATOM   5766 H HG2  . GLU   B 1 120 ? 34.425 -11.783 -12.824 1.00 29.51 ?  120 GLU   B HG2  1 
ATOM   5767 H HG3  . GLU   B 1 120 ? 35.639 -10.888 -12.329 1.00 29.51 ?  120 GLU   B HG3  1 
ATOM   5768 N N    . VAL   B 1 121 ? 38.231 -15.043 -12.293 1.00 12.83 ?  121 VAL   B N    1 
ATOM   5769 C CA   . VAL   B 1 121 ? 38.982 -16.245 -12.647 1.00 12.66 ?  121 VAL   B CA   1 
ATOM   5770 C C    . VAL   B 1 121 ? 40.088 -16.449 -11.621 1.00 12.31 ?  121 VAL   B C    1 
ATOM   5771 O O    . VAL   B 1 121 ? 40.758 -15.491 -11.222 1.00 13.12 ?  121 VAL   B O    1 
ATOM   5772 C CB   . VAL   B 1 121 ? 39.508 -16.189 -14.101 1.00 14.56 ?  121 VAL   B CB   1 
ATOM   5773 C CG1  . VAL   B 1 121 ? 40.381 -14.964 -14.334 1.00 16.54 ?  121 VAL   B CG1  1 
ATOM   5774 C CG2  . VAL   B 1 121 ? 40.245 -17.475 -14.454 1.00 16.05 ?  121 VAL   B CG2  1 
ATOM   5775 H H    . VAL   B 1 121 ? 38.720 -14.439 -11.918 1.00 15.40 ?  121 VAL   B H    1 
ATOM   5776 H HA   . VAL   B 1 121 ? 38.379 -17.002 -12.591 1.00 15.20 ?  121 VAL   B HA   1 
ATOM   5777 H HB   . VAL   B 1 121 ? 38.748 -16.121 -14.701 1.00 17.48 ?  121 VAL   B HB   1 
ATOM   5778 H HG11 . VAL   B 1 121 ? 40.693 -14.969 -15.254 1.00 19.85 ?  121 VAL   B HG11 1 
ATOM   5779 H HG12 . VAL   B 1 121 ? 39.857 -14.166 -14.168 1.00 19.85 ?  121 VAL   B HG12 1 
ATOM   5780 H HG13 . VAL   B 1 121 ? 41.139 -14.995 -13.729 1.00 19.85 ?  121 VAL   B HG13 1 
ATOM   5781 H HG21 . VAL   B 1 121 ? 40.456 -17.468 -15.403 1.00 19.27 ?  121 VAL   B HG21 1 
ATOM   5782 H HG22 . VAL   B 1 121 ? 41.064 -17.526 -13.937 1.00 19.27 ?  121 VAL   B HG22 1 
ATOM   5783 H HG23 . VAL   B 1 121 ? 39.676 -18.233 -14.251 1.00 19.27 ?  121 VAL   B HG23 1 
ATOM   5784 N N    . LEU   B 1 122 ? 40.271 -17.703 -11.189 1.00 11.90 ?  122 LEU   B N    1 
ATOM   5785 C CA   . LEU   B 1 122 ? 41.253 -18.061 -10.165 1.00 11.77 ?  122 LEU   B CA   1 
ATOM   5786 C C    . LEU   B 1 122 ? 41.911 -19.393 -10.490 1.00 11.44 ?  122 LEU   B C    1 
ATOM   5787 O O    . LEU   B 1 122 ? 41.256 -20.312 -10.994 1.00 12.52 ?  122 LEU   B O    1 
ATOM   5788 C CB   . LEU   B 1 122 ? 40.600 -18.289 -8.787  1.00 13.88 ?  122 LEU   B CB   1 
ATOM   5789 C CG   . LEU   B 1 122 ? 39.574 -17.263 -8.298  1.00 13.67 ?  122 LEU   B CG   1 
ATOM   5790 C CD1  . LEU   B 1 122 ? 38.162 -17.618 -8.761  1.00 14.42 ?  122 LEU   B CD1  1 
ATOM   5791 C CD2  . LEU   B 1 122 ? 39.631 -17.148 -6.787  1.00 12.93 ?  122 LEU   B CD2  1 
ATOM   5792 H H    . LEU   B 1 122 ? 39.827 -18.383 -11.484 1.00 14.28 ?  122 LEU   B H    1 
ATOM   5793 H HA   . LEU   B 1 122 ? 41.928 -17.369 -10.088 1.00 14.12 ?  122 LEU   B HA   1 
ATOM   5794 H HB2  . LEU   B 1 122 ? 40.145 -19.144 -8.810  1.00 16.66 ?  122 LEU   B HB2  1 
ATOM   5795 H HB3  . LEU   B 1 122 ? 41.302 -18.318 -8.124  1.00 16.66 ?  122 LEU   B HB3  1 
ATOM   5796 H HG   . LEU   B 1 122 ? 39.797 -16.395 -8.667  1.00 16.40 ?  122 LEU   B HG   1 
ATOM   5797 H HD11 . LEU   B 1 122 ? 37.540 -16.961 -8.407  1.00 17.30 ?  122 LEU   B HD11 1 
ATOM   5798 H HD12 . LEU   B 1 122 ? 38.136 -17.603 -9.731  1.00 17.30 ?  122 LEU   B HD12 1 
ATOM   5799 H HD13 . LEU   B 1 122 ? 37.934 -18.499 -8.435  1.00 17.30 ?  122 LEU   B HD13 1 
ATOM   5800 H HD21 . LEU   B 1 122 ? 38.955 -16.520 -6.489  1.00 15.52 ?  122 LEU   B HD21 1 
ATOM   5801 H HD22 . LEU   B 1 122 ? 39.472 -18.019 -6.395  1.00 15.52 ?  122 LEU   B HD22 1 
ATOM   5802 H HD23 . LEU   B 1 122 ? 40.513 -16.827 -6.529  1.00 15.52 ?  122 LEU   B HD23 1 
ATOM   5803 N N    . LEU   B 1 123 ? 43.197 -19.501 -10.134 1.00 11.22 ?  123 LEU   B N    1 
ATOM   5804 C CA   . LEU   B 1 123 ? 43.910 -20.770 -10.014 1.00 11.65 ?  123 LEU   B CA   1 
ATOM   5805 C C    . LEU   B 1 123 ? 43.881 -21.160 -8.541  1.00 11.17 ?  123 LEU   B C    1 
ATOM   5806 O O    . LEU   B 1 123 ? 44.236 -20.339 -7.688  1.00 11.57 ?  123 LEU   B O    1 
ATOM   5807 C CB   . LEU   B 1 123 ? 45.358 -20.577 -10.466 1.00 12.13 ?  123 LEU   B CB   1 
ATOM   5808 C CG   . LEU   B 1 123 ? 46.302 -21.761 -10.231 1.00 12.52 ?  123 LEU   B CG   1 
ATOM   5809 C CD1  . LEU   B 1 123 ? 45.880 -23.005 -11.015 1.00 13.17 ?  123 LEU   B CD1  1 
ATOM   5810 C CD2  . LEU   B 1 123 ? 47.727 -21.354 -10.585 1.00 13.14 ?  123 LEU   B CD2  1 
ATOM   5811 H H    . LEU   B 1 123 ? 43.694 -18.820 -9.940  1.00 13.46 ?  123 LEU   B H    1 
ATOM   5812 H HA   . LEU   B 1 123 ? 43.480 -21.456 -10.551 1.00 13.98 ?  123 LEU   B HA   1 
ATOM   5813 H HB2  . LEU   B 1 123 ? 45.356 -20.398 -11.421 1.00 14.55 ?  123 LEU   B HB2  1 
ATOM   5814 H HB3  . LEU   B 1 123 ? 45.725 -19.816 -9.996  1.00 14.55 ?  123 LEU   B HB3  1 
ATOM   5815 H HG   . LEU   B 1 123 ? 46.294 -21.989 -9.288  1.00 15.03 ?  123 LEU   B HG   1 
ATOM   5816 H HD11 . LEU   B 1 123 ? 46.520 -23.714 -10.846 1.00 15.81 ?  123 LEU   B HD11 1 
ATOM   5817 H HD12 . LEU   B 1 123 ? 44.998 -23.277 -10.719 1.00 15.81 ?  123 LEU   B HD12 1 
ATOM   5818 H HD13 . LEU   B 1 123 ? 45.864 -22.790 -11.959 1.00 15.81 ?  123 LEU   B HD13 1 
ATOM   5819 H HD21 . LEU   B 1 123 ? 48.317 -22.107 -10.432 1.00 15.77 ?  123 LEU   B HD21 1 
ATOM   5820 H HD22 . LEU   B 1 123 ? 47.756 -21.092 -11.518 1.00 15.77 ?  123 LEU   B HD22 1 
ATOM   5821 H HD23 . LEU   B 1 123 ? 47.989 -20.607 -10.023 1.00 15.77 ?  123 LEU   B HD23 1 
ATOM   5822 N N    . ALA   B 1 124 ? 43.452 -22.393 -8.236  1.00 11.22 ?  124 ALA   B N    1 
ATOM   5823 C CA   . ALA   B 1 124 ? 43.197 -22.717 -6.840  1.00 11.41 ?  124 ALA   B CA   1 
ATOM   5824 C C    . ALA   B 1 124 ? 43.462 -24.177 -6.508  1.00 11.12 ?  124 ALA   B C    1 
ATOM   5825 O O    . ALA   B 1 124 ? 43.328 -25.054 -7.376  1.00 11.85 ?  124 ALA   B O    1 
ATOM   5826 C CB   . ALA   B 1 124 ? 41.744 -22.396 -6.469  1.00 11.90 ?  124 ALA   B CB   1 
ATOM   5827 H H    . ALA   B 1 124 ? 43.298 -23.032 -8.800  1.00 13.47 ?  124 ALA   B H    1 
ATOM   5828 H HA   . ALA   B 1 124 ? 43.771 -22.167 -6.294  1.00 13.69 ?  124 ALA   B HA   1 
ATOM   5829 H HB1  . ALA   B 1 124 ? 41.593 -22.616 -5.536  1.00 14.28 ?  124 ALA   B HB1  1 
ATOM   5830 H HB2  . ALA   B 1 124 ? 41.583 -21.446 -6.611  1.00 14.28 ?  124 ALA   B HB2  1 
ATOM   5831 H HB3  . ALA   B 1 124 ? 41.146 -22.915 -7.031  1.00 14.28 ?  124 ALA   B HB3  1 
ATOM   5832 N N    . PRO   B 1 125 ? 43.768 -24.467 -5.246  1.00 11.36 ?  125 PRO   B N    1 
ATOM   5833 C CA   . PRO   B 1 125 ? 43.700 -25.834 -4.728  1.00 12.29 ?  125 PRO   B CA   1 
ATOM   5834 C C    . PRO   B 1 125 ? 42.298 -26.108 -4.185  1.00 11.97 ?  125 PRO   B C    1 
ATOM   5835 O O    . PRO   B 1 125 ? 41.500 -25.192 -3.976  1.00 12.86 ?  125 PRO   B O    1 
ATOM   5836 C CB   . PRO   B 1 125 ? 44.684 -25.767 -3.557  1.00 13.35 ?  125 PRO   B CB   1 
ATOM   5837 C CG   . PRO   B 1 125 ? 44.424 -24.373 -2.977  1.00 13.51 ?  125 PRO   B CG   1 
ATOM   5838 C CD   . PRO   B 1 125 ? 44.093 -23.501 -4.182  1.00 12.04 ?  125 PRO   B CD   1 
ATOM   5839 H HA   . PRO   B 1 125 ? 43.973 -26.498 -5.380  1.00 14.75 ?  125 PRO   B HA   1 
ATOM   5840 H HB2  . PRO   B 1 125 ? 44.480 -26.457 -2.904  1.00 16.02 ?  125 PRO   B HB2  1 
ATOM   5841 H HB3  . PRO   B 1 125 ? 45.596 -25.845 -3.875  1.00 16.02 ?  125 PRO   B HB3  1 
ATOM   5842 H HG2  . PRO   B 1 125 ? 43.669 -24.401 -2.363  1.00 16.21 ?  125 PRO   B HG2  1 
ATOM   5843 H HG3  . PRO   B 1 125 ? 45.218 -24.046 -2.519  1.00 16.21 ?  125 PRO   B HG3  1 
ATOM   5844 H HD2  . PRO   B 1 125 ? 43.336 -22.927 -3.997  1.00 14.45 ?  125 PRO   B HD2  1 
ATOM   5845 H HD3  . PRO   B 1 125 ? 44.877 -22.970 -4.436  1.00 14.45 ?  125 PRO   B HD3  1 
ATOM   5846 N N    . LEU   B 1 126 ? 42.028 -27.388 -3.909  1.00 12.78 ?  126 LEU   B N    1 
ATOM   5847 C CA   . LEU   B 1 126 ? 40.805 -27.758 -3.202  1.00 13.22 ?  126 LEU   B CA   1 
ATOM   5848 C C    . LEU   B 1 126 ? 40.915 -27.361 -1.737  1.00 13.19 ?  126 LEU   B C    1 
ATOM   5849 O O    . LEU   B 1 126 ? 41.804 -27.823 -1.017  1.00 15.03 ?  126 LEU   B O    1 
ATOM   5850 C CB   . LEU   B 1 126 ? 40.548 -29.256 -3.316  1.00 14.75 ?  126 LEU   B CB   1 
ATOM   5851 C CG   . LEU   B 1 126 ? 40.024 -29.740 -4.668  1.00 15.33 ?  126 LEU   B CG   1 
ATOM   5852 C CD1  . LEU   B 1 126 ? 40.075 -31.254 -4.755  1.00 17.56 ?  126 LEU   B CD1  1 
ATOM   5853 C CD2  . LEU   B 1 126 ? 38.603 -29.247 -4.918  1.00 16.16 ?  126 LEU   B CD2  1 
ATOM   5854 H H    . LEU   B 1 126 ? 42.535 -28.054 -4.114  1.00 15.34 ?  126 LEU   B H    1 
ATOM   5855 H HA   . LEU   B 1 126 ? 40.054 -27.285 -3.594  1.00 15.86 ?  126 LEU   B HA   1 
ATOM   5856 H HB2  . LEU   B 1 126 ? 41.376 -29.723 -3.143  1.00 17.70 ?  126 LEU   B HB2  1 
ATOM   5857 H HB3  . LEU   B 1 126 ? 39.888 -29.503 -2.648  1.00 17.70 ?  126 LEU   B HB3  1 
ATOM   5858 H HG   . LEU   B 1 126 ? 40.592 -29.377 -5.370  1.00 18.40 ?  126 LEU   B HG   1 
ATOM   5859 H HD11 . LEU   B 1 126 ? 39.736 -31.531 -5.621  1.00 21.07 ?  126 LEU   B HD11 1 
ATOM   5860 H HD12 . LEU   B 1 126 ? 40.989 -31.547 -4.644  1.00 21.07 ?  126 LEU   B HD12 1 
ATOM   5861 H HD13 . LEU   B 1 126 ? 39.517 -31.625 -4.050  1.00 21.07 ?  126 LEU   B HD13 1 
ATOM   5862 H HD21 . LEU   B 1 126 ? 38.265 -29.654 -5.732  1.00 19.39 ?  126 LEU   B HD21 1 
ATOM   5863 H HD22 . LEU   B 1 126 ? 38.044 -29.494 -4.167  1.00 19.39 ?  126 LEU   B HD22 1 
ATOM   5864 H HD23 . LEU   B 1 126 ? 38.611 -28.278 -5.017  1.00 19.39 ?  126 LEU   B HD23 1 
ATOM   5865 N N    . LEU   B 1 127 ? 39.983 -26.536 -1.279  1.00 13.20 ?  127 LEU   B N    1 
ATOM   5866 C CA   . LEU   B 1 127 ? 40.045 -26.040 0.081   1.00 13.55 ?  127 LEU   B CA   1 
ATOM   5867 C C    . LEU   B 1 127 ? 39.772 -27.158 1.078   1.00 13.32 ?  127 LEU   B C    1 
ATOM   5868 O O    . LEU   B 1 127 ? 38.949 -28.051 0.852   1.00 13.37 ?  127 LEU   B O    1 
ATOM   5869 C CB   . LEU   B 1 127 ? 39.031 -24.917 0.287   1.00 14.48 ?  127 LEU   B CB   1 
ATOM   5870 C CG   . LEU   B 1 127 ? 39.209 -23.648 -0.544  1.00 14.79 ?  127 LEU   B CG   1 
ATOM   5871 C CD1  . LEU   B 1 127 ? 38.089 -22.676 -0.209  1.00 15.11 ?  127 LEU   B CD1  1 
ATOM   5872 C CD2  . LEU   B 1 127 ? 40.570 -23.008 -0.303  1.00 15.48 ?  127 LEU   B CD2  1 
ATOM   5873 H H    . LEU   B 1 127 ? 39.312 -26.239 -1.737  1.00 15.84 ?  127 LEU   B H    1 
ATOM   5874 H HA   . LEU   B 1 127 ? 40.935 -25.682 0.253   1.00 16.25 ?  127 LEU   B HA   1 
ATOM   5875 H HB2  . LEU   B 1 127 ? 38.149 -25.264 0.085   1.00 17.37 ?  127 LEU   B HB2  1 
ATOM   5876 H HB3  . LEU   B 1 127 ? 39.060 -24.646 1.219   1.00 17.37 ?  127 LEU   B HB3  1 
ATOM   5877 H HG   . LEU   B 1 127 ? 39.132 -23.862 -1.484  1.00 17.75 ?  127 LEU   B HG   1 
ATOM   5878 H HD11 . LEU   B 1 127 ? 38.200 -21.865 -0.733  1.00 18.14 ?  127 LEU   B HD11 1 
ATOM   5879 H HD12 . LEU   B 1 127 ? 37.235 -23.087 -0.417  1.00 18.14 ?  127 LEU   B HD12 1 
ATOM   5880 H HD13 . LEU   B 1 127 ? 38.127 -22.460 0.739   1.00 18.14 ?  127 LEU   B HD13 1 
ATOM   5881 H HD21 . LEU   B 1 127 ? 40.610 -22.152 -0.765  1.00 18.57 ?  127 LEU   B HD21 1 
ATOM   5882 H HD22 . LEU   B 1 127 ? 40.695 -22.869 0.650   1.00 18.57 ?  127 LEU   B HD22 1 
ATOM   5883 H HD23 . LEU   B 1 127 ? 41.259 -23.597 -0.645  1.00 18.57 ?  127 LEU   B HD23 1 
ATOM   5884 N N    . SER   B 1 128 ? 40.457 -27.074 2.207   1.00 13.21 ?  128 SER   B N    1 
ATOM   5885 C CA   . SER   B 1 128 ? 40.348 -27.990 3.332   1.00 13.86 ?  128 SER   B CA   1 
ATOM   5886 C C    . SER   B 1 128 ? 40.840 -29.400 3.009   1.00 15.01 ?  128 SER   B C    1 
ATOM   5887 O O    . SER   B 1 128 ? 40.739 -30.282 3.861   1.00 16.57 ?  128 SER   B O    1 
ATOM   5888 C CB   . SER   B 1 128 ? 38.948 -28.000 3.969   1.00 14.32 ?  128 SER   B CB   1 
ATOM   5889 O OG   . SER   B 1 128 ? 38.623 -26.720 4.511   1.00 14.66 ?  128 SER   B OG   1 
ATOM   5890 H H    . SER   B 1 128 ? 41.029 -26.449 2.355   1.00 15.85 ?  128 SER   B H    1 
ATOM   5891 H HA   . SER   B 1 128 ? 40.942 -27.656 4.015   1.00 16.63 ?  128 SER   B HA   1 
ATOM   5892 H HB2  . SER   B 1 128 ? 38.290 -28.246 3.299   1.00 17.18 ?  128 SER   B HB2  1 
ATOM   5893 H HB3  . SER   B 1 128 ? 38.937 -28.667 4.689   1.00 17.18 ?  128 SER   B HB3  1 
ATOM   5894 H HG   . SER   B 1 128 ? 39.195 -26.516 5.093   1.00 17.59 ?  128 SER   B HG   1 
ATOM   5895 N N    . ALA   B 1 129 ? 41.411 -29.627 1.826   1.00 15.77 ?  129 ALA   B N    1 
ATOM   5896 C CA   . ALA   B 1 129 ? 41.959 -30.929 1.476   1.00 17.03 ?  129 ALA   B CA   1 
ATOM   5897 C C    . ALA   B 1 129 ? 43.352 -31.102 2.069   1.00 16.10 ?  129 ALA   B C    1 
ATOM   5898 O O    . ALA   B 1 129 ? 43.911 -30.200 2.708   1.00 15.81 ?  129 ALA   B O    1 
ATOM   5899 C CB   . ALA   B 1 129 ? 42.001 -31.103 -0.041  1.00 19.28 ?  129 ALA   B CB   1 
ATOM   5900 H H    . ALA   B 1 129 ? 41.491 -29.038 1.202   1.00 18.92 ?  129 ALA   B H    1 
ATOM   5901 H HA   . ALA   B 1 129 ? 41.387 -31.619 1.838   1.00 20.44 ?  129 ALA   B HA   1 
ATOM   5902 H HB1  . ALA   B 1 129 ? 42.358 -31.983 -0.247  1.00 23.14 ?  129 ALA   B HB1  1 
ATOM   5903 H HB2  . ALA   B 1 129 ? 41.103 -31.020 -0.393  1.00 23.14 ?  129 ALA   B HB2  1 
ATOM   5904 H HB3  . ALA   B 1 129 ? 42.573 -30.418 -0.422  1.00 23.14 ?  129 ALA   B HB3  1 
ATOM   5905 N N    . GLY   B 1 130 ? 43.915 -32.285 1.837   1.00 16.15 ?  130 GLY   B N    1 
ATOM   5906 C CA   . GLY   B 1 130 ? 45.300 -32.528 2.194   1.00 16.77 ?  130 GLY   B CA   1 
ATOM   5907 C C    . GLY   B 1 130 ? 45.515 -32.432 3.685   1.00 16.59 ?  130 GLY   B C    1 
ATOM   5908 O O    . GLY   B 1 130 ? 44.822 -33.076 4.485   1.00 17.59 ?  130 GLY   B O    1 
ATOM   5909 H H    . GLY   B 1 130 ? 43.517 -32.957 1.471   1.00 19.37 ?  130 GLY   B H    1 
ATOM   5910 H HA2  . GLY   B 1 130 ? 45.561 -33.419 1.901   1.00 20.12 ?  130 GLY   B HA2  1 
ATOM   5911 H HA3  . GLY   B 1 130 ? 45.871 -31.881 1.755   1.00 20.12 ?  130 GLY   B HA3  1 
ATOM   5912 N N    . ILE   B 1 131 ? 46.487 -31.598 4.072   1.00 16.85 ?  131 ILE   B N    1 
ATOM   5913 C CA   . ILE   B 1 131 ? 46.844 -31.465 5.477   1.00 17.88 ?  131 ILE   B CA   1 
ATOM   5914 C C    . ILE   B 1 131 ? 45.727 -30.865 6.310   1.00 16.70 ?  131 ILE   B C    1 
ATOM   5915 O O    . ILE   B 1 131 ? 45.796 -30.935 7.540   1.00 18.17 ?  131 ILE   B O    1 
ATOM   5916 C CB   . ILE   B 1 131 ? 48.163 -30.684 5.677   1.00 19.99 ?  131 ILE   B CB   1 
ATOM   5917 C CG1  . ILE   B 1 131 ? 47.995 -29.203 5.306   1.00 21.11 ?  131 ILE   B CG1  1 
ATOM   5918 C CG2  . ILE   B 1 131 ? 49.290 -31.325 4.868   1.00 21.20 ?  131 ILE   B CG2  1 
ATOM   5919 C CD1  . ILE   B 1 131 ? 49.215 -28.349 5.617   1.00 22.13 ?  131 ILE   B CD1  1 
ATOM   5920 H H    . ILE   B 1 131 ? 46.950 -31.111 3.541   1.00 20.22 ?  131 ILE   B H    1 
ATOM   5921 H HA   . ILE   B 1 131 ? 46.991 -32.354 5.828   1.00 21.45 ?  131 ILE   B HA   1 
ATOM   5922 H HB   . ILE   B 1 131 ? 48.398 -30.734 6.617   1.00 23.99 ?  131 ILE   B HB   1 
ATOM   5923 H HG12 . ILE   B 1 131 ? 47.817 -29.141 4.355   1.00 25.34 ?  131 ILE   B HG12 1 
ATOM   5924 H HG13 . ILE   B 1 131 ? 47.245 -28.833 5.802   1.00 25.34 ?  131 ILE   B HG13 1 
ATOM   5925 H HG21 . ILE   B 1 131 ? 50.129 -30.919 5.128   1.00 25.44 ?  131 ILE   B HG21 1 
ATOM   5926 H HG22 . ILE   B 1 131 ? 49.305 -32.274 5.052   1.00 25.44 ?  131 ILE   B HG22 1 
ATOM   5927 H HG23 . ILE   B 1 131 ? 49.122 -31.171 3.925   1.00 25.44 ?  131 ILE   B HG23 1 
ATOM   5928 H HD11 . ILE   B 1 131 ? 48.996 -27.418 5.451   1.00 26.56 ?  131 ILE   B HD11 1 
ATOM   5929 H HD12 . ILE   B 1 131 ? 49.456 -28.472 6.548   1.00 26.56 ?  131 ILE   B HD12 1 
ATOM   5930 H HD13 . ILE   B 1 131 ? 49.946 -28.625 5.045   1.00 26.56 ?  131 ILE   B HD13 1 
ATOM   5931 N N    . PHE   B 1 132 ? 44.698 -30.287 5.679   1.00 15.75 ?  132 PHE   B N    1 
ATOM   5932 C CA   . PHE   B 1 132 ? 43.538 -29.784 6.412   1.00 15.85 ?  132 PHE   B CA   1 
ATOM   5933 C C    . PHE   B 1 132 ? 42.515 -30.873 6.738   1.00 17.31 ?  132 PHE   B C    1 
ATOM   5934 O O    . PHE   B 1 132 ? 41.606 -30.624 7.535   1.00 19.35 ?  132 PHE   B O    1 
ATOM   5935 C CB   . PHE   B 1 132 ? 42.857 -28.647 5.640   1.00 15.12 ?  132 PHE   B CB   1 
ATOM   5936 C CG   . PHE   B 1 132 ? 43.557 -27.306 5.754   1.00 15.13 ?  132 PHE   B CG   1 
ATOM   5937 C CD1  . PHE   B 1 132 ? 44.851 -27.123 5.286   1.00 16.27 ?  132 PHE   B CD1  1 
ATOM   5938 C CD2  . PHE   B 1 132 ? 42.881 -26.210 6.279   1.00 14.72 ?  132 PHE   B CD2  1 
ATOM   5939 C CE1  . PHE   B 1 132 ? 45.471 -25.879 5.381   1.00 16.70 ?  132 PHE   B CE1  1 
ATOM   5940 C CE2  . PHE   B 1 132 ? 43.490 -24.966 6.368   1.00 15.62 ?  132 PHE   B CE2  1 
ATOM   5941 C CZ   . PHE   B 1 132 ? 44.787 -24.802 5.922   1.00 16.79 ?  132 PHE   B CZ   1 
ATOM   5942 H H    . PHE   B 1 132 ? 44.648 -30.173 4.825   1.00 18.90 ?  132 PHE   B H    1 
ATOM   5943 H HA   . PHE   B 1 132 ? 43.847 -29.413 7.251   1.00 19.02 ?  132 PHE   B HA   1 
ATOM   5944 H HB2  . PHE   B 1 132 ? 42.835 -28.880 4.701   1.00 18.14 ?  132 PHE   B HB2  1 
ATOM   5945 H HB3  . PHE   B 1 132 ? 41.954 -28.537 5.975   1.00 18.14 ?  132 PHE   B HB3  1 
ATOM   5946 H HD1  . PHE   B 1 132 ? 45.316 -27.844 4.929   1.00 19.52 ?  132 PHE   B HD1  1 
ATOM   5947 H HD2  . PHE   B 1 132 ? 42.009 -26.313 6.585   1.00 17.66 ?  132 PHE   B HD2  1 
ATOM   5948 H HE1  . PHE   B 1 132 ? 46.344 -25.771 5.080   1.00 20.04 ?  132 PHE   B HE1  1 
ATOM   5949 H HE2  . PHE   B 1 132 ? 43.030 -24.243 6.736   1.00 18.75 ?  132 PHE   B HE2  1 
ATOM   5950 H HZ   . PHE   B 1 132 ? 45.199 -23.967 5.987   1.00 20.14 ?  132 PHE   B HZ   1 
ATOM   5951 N N    . GLY   B 1 133 ? 42.613 -32.060 6.130   1.00 16.64 ?  133 GLY   B N    1 
ATOM   5952 C CA   . GLY   B 1 133 ? 41.905 -33.228 6.625   1.00 17.79 ?  133 GLY   B CA   1 
ATOM   5953 C C    . GLY   B 1 133 ? 40.511 -33.498 6.087   1.00 18.15 ?  133 GLY   B C    1 
ATOM   5954 O O    . GLY   B 1 133 ? 39.930 -34.526 6.449   1.00 20.35 ?  133 GLY   B O    1 
ATOM   5955 H H    . GLY   B 1 133 ? 43.093 -32.207 5.430   1.00 19.96 ?  133 GLY   B H    1 
ATOM   5956 H HA2  . GLY   B 1 133 ? 42.442 -34.010 6.432   1.00 21.35 ?  133 GLY   B HA2  1 
ATOM   5957 H HA3  . GLY   B 1 133 ? 41.837 -33.151 7.590   1.00 21.35 ?  133 GLY   B HA3  1 
ATOM   5958 N N    . ALA   B 1 134 ? 39.946 -32.633 5.254   1.00 17.36 ?  134 ALA   B N    1 
ATOM   5959 C CA   . ALA   B 1 134 ? 38.620 -32.919 4.725   1.00 17.83 ?  134 ALA   B CA   1 
ATOM   5960 C C    . ALA   B 1 134 ? 38.706 -33.905 3.565   1.00 17.67 ?  134 ALA   B C    1 
ATOM   5961 O O    . ALA   B 1 134 ? 39.761 -34.102 2.956   1.00 18.89 ?  134 ALA   B O    1 
ATOM   5962 C CB   . ALA   B 1 134 ? 37.940 -31.633 4.260   1.00 18.48 ?  134 ALA   B CB   1 
ATOM   5963 H H    . ALA   B 1 134 ? 40.296 -31.889 4.991   1.00 20.83 ?  134 ALA   B H    1 
ATOM   5964 H HA   . ALA   B 1 134 ? 38.073 -33.308 5.427   1.00 21.40 ?  134 ALA   B HA   1 
ATOM   5965 H HB1  . ALA   B 1 134 ? 37.055 -31.847 3.925   1.00 22.18 ?  134 ALA   B HB1  1 
ATOM   5966 H HB2  . ALA   B 1 134 ? 37.871 -31.018 5.008   1.00 22.18 ?  134 ALA   B HB2  1 
ATOM   5967 H HB3  . ALA   B 1 134 ? 38.472 -31.232 3.553   1.00 22.18 ?  134 ALA   B HB3  1 
ATOM   5968 N N    . ASP   B 1 135 ? 37.570 -34.528 3.268   1.00 17.72 ?  135 ASP   B N    1 
ATOM   5969 C CA   . ASP   B 1 135 ? 37.473 -35.423 2.122   1.00 18.47 ?  135 ASP   B CA   1 
ATOM   5970 C C    . ASP   B 1 135 ? 37.574 -34.583 0.855   1.00 17.18 ?  135 ASP   B C    1 
ATOM   5971 O O    . ASP   B 1 135 ? 36.721 -33.710 0.637   1.00 16.95 ?  135 ASP   B O    1 
ATOM   5972 C CB   . ASP   B 1 135 ? 36.131 -36.160 2.178   1.00 20.16 ?  135 ASP   B CB   1 
ATOM   5973 C CG   . ASP   B 1 135 ? 35.935 -37.140 1.032   1.00 22.08 ?  135 ASP   B CG   1 
ATOM   5974 O OD1  . ASP   B 1 135 ? 36.792 -37.197 0.125   1.00 22.03 ?  135 ASP   B OD1  1 
ATOM   5975 O OD2  . ASP   B 1 135 ? 34.921 -37.879 1.059   1.00 25.56 -1 135 ASP   B OD2  1 
ATOM   5976 H H    . ASP   B 1 135 ? 36.840 -34.447 3.715   1.00 21.26 ?  135 ASP   B H    1 
ATOM   5977 H HA   . ASP   B 1 135 ? 38.194 -36.072 2.155   1.00 22.16 ?  135 ASP   B HA   1 
ATOM   5978 H HB2  . ASP   B 1 135 ? 36.087 -36.656 3.006   1.00 24.20 ?  135 ASP   B HB2  1 
ATOM   5979 H HB3  . ASP   B 1 135 ? 35.421 -35.507 2.136   1.00 24.20 ?  135 ASP   B HB3  1 
ATOM   5980 N N    . PRO   B 1 136 ? 38.583 -34.790 0.006   1.00 17.45 ?  136 PRO   B N    1 
ATOM   5981 C CA   . PRO   B 1 136 ? 38.684 -33.966 -1.210  1.00 16.69 ?  136 PRO   B CA   1 
ATOM   5982 C C    . PRO   B 1 136 ? 37.493 -34.118 -2.139  1.00 16.19 ?  136 PRO   B C    1 
ATOM   5983 O O    . PRO   B 1 136 ? 37.176 -33.177 -2.875  1.00 15.45 ?  136 PRO   B O    1 
ATOM   5984 C CB   . PRO   B 1 136 ? 39.995 -34.444 -1.856  1.00 17.58 ?  136 PRO   B CB   1 
ATOM   5985 C CG   . PRO   B 1 136 ? 40.179 -35.845 -1.325  1.00 18.86 ?  136 PRO   B CG   1 
ATOM   5986 C CD   . PRO   B 1 136 ? 39.657 -35.795 0.083   1.00 18.51 ?  136 PRO   B CD   1 
ATOM   5987 H HA   . PRO   B 1 136 ? 38.775 -33.030 -0.973  1.00 20.03 ?  136 PRO   B HA   1 
ATOM   5988 H HB2  . PRO   B 1 136 ? 39.903 -34.450 -2.824  1.00 21.09 ?  136 PRO   B HB2  1 
ATOM   5989 H HB3  . PRO   B 1 136 ? 40.725 -33.869 -1.583  1.00 21.09 ?  136 PRO   B HB3  1 
ATOM   5990 H HG2  . PRO   B 1 136 ? 39.663 -36.473 -1.857  1.00 22.63 ?  136 PRO   B HG2  1 
ATOM   5991 H HG3  . PRO   B 1 136 ? 41.120 -36.081 -1.332  1.00 22.63 ?  136 PRO   B HG3  1 
ATOM   5992 H HD2  . PRO   B 1 136 ? 39.296 -36.657 0.344   1.00 22.21 ?  136 PRO   B HD2  1 
ATOM   5993 H HD3  . PRO   B 1 136 ? 40.350 -35.498 0.696   1.00 22.21 ?  136 PRO   B HD3  1 
ATOM   5994 N N    . ILE   B 1 137 ? 36.831 -35.284 -2.135  1.00 16.56 ?  137 ILE   B N    1 
ATOM   5995 C CA   . ILE   B 1 137 ? 35.614 -35.458 -2.926  1.00 16.81 ?  137 ILE   B CA   1 
ATOM   5996 C C    . ILE   B 1 137 ? 34.538 -34.489 -2.451  1.00 16.40 ?  137 ILE   B C    1 
ATOM   5997 O O    . ILE   B 1 137 ? 33.822 -33.875 -3.256  1.00 16.07 ?  137 ILE   B O    1 
ATOM   5998 C CB   . ILE   B 1 137 ? 35.149 -36.930 -2.867  1.00 18.64 ?  137 ILE   B CB   1 
ATOM   5999 C CG1  . ILE   B 1 137 ? 36.144 -37.829 -3.605  1.00 21.43 ?  137 ILE   B CG1  1 
ATOM   6000 C CG2  . ILE   B 1 137 ? 33.747 -37.079 -3.449  1.00 19.24 ?  137 ILE   B CG2  1 
ATOM   6001 C CD1  . ILE   B 1 137 ? 35.849 -39.313 -3.485  1.00 23.74 ?  137 ILE   B CD1  1 
ATOM   6002 H H    . ILE   B 1 137 ? 37.061 -35.978 -1.686  1.00 19.87 ?  137 ILE   B H    1 
ATOM   6003 H HA   . ILE   B 1 137 ? 35.810 -35.249 -3.855  1.00 20.17 ?  137 ILE   B HA   1 
ATOM   6004 H HB   . ILE   B 1 137 ? 35.119 -37.202 -1.941  1.00 22.37 ?  137 ILE   B HB   1 
ATOM   6005 H HG12 . ILE   B 1 137 ? 36.131 -37.600 -4.549  1.00 25.72 ?  137 ILE   B HG12 1 
ATOM   6006 H HG13 . ILE   B 1 137 ? 37.029 -37.673 -3.242  1.00 25.72 ?  137 ILE   B HG13 1 
ATOM   6007 H HG21 . ILE   B 1 137 ? 33.518 -38.020 -3.510  1.00 23.09 ?  137 ILE   B HG21 1 
ATOM   6008 H HG22 . ILE   B 1 137 ? 33.108 -36.634 -2.870  1.00 23.09 ?  137 ILE   B HG22 1 
ATOM   6009 H HG23 . ILE   B 1 137 ? 33.725 -36.680 -4.333  1.00 23.09 ?  137 ILE   B HG23 1 
ATOM   6010 H HD11 . ILE   B 1 137 ? 36.560 -39.800 -3.923  1.00 28.48 ?  137 ILE   B HD11 1 
ATOM   6011 H HD12 . ILE   B 1 137 ? 35.805 -39.554 -2.546  1.00 28.48 ?  137 ILE   B HD12 1 
ATOM   6012 H HD13 . ILE   B 1 137 ? 35.003 -39.511 -3.918  1.00 28.48 ?  137 ILE   B HD13 1 
ATOM   6013 N N    . HIS   B 1 138 ? 34.407 -34.336 -1.137  1.00 16.55 ?  138 HIS   B N    1 
ATOM   6014 C CA   . HIS   B 1 138 ? 33.458 -33.370 -0.601  1.00 16.89 ?  138 HIS   B CA   1 
ATOM   6015 C C    . HIS   B 1 138 ? 33.876 -31.940 -0.924  1.00 15.79 ?  138 HIS   B C    1 
ATOM   6016 O O    . HIS   B 1 138 ? 33.031 -31.094 -1.233  1.00 16.47 ?  138 HIS   B O    1 
ATOM   6017 C CB   . HIS   B 1 138 ? 33.333 -33.547 0.905   1.00 18.43 ?  138 HIS   B CB   1 
ATOM   6018 C CG   . HIS   B 1 138 ? 32.393 -32.571 1.534   1.00 18.99 ?  138 HIS   B CG   1 
ATOM   6019 N ND1  . HIS   B 1 138 ? 31.056 -32.514 1.204   1.00 20.55 ?  138 HIS   B ND1  1 
ATOM   6020 C CD2  . HIS   B 1 138 ? 32.599 -31.587 2.442   1.00 19.61 ?  138 HIS   B CD2  1 
ATOM   6021 C CE1  . HIS   B 1 138 ? 30.475 -31.552 1.897   1.00 20.20 ?  138 HIS   B CE1  1 
ATOM   6022 N NE2  . HIS   B 1 138 ? 31.388 -30.973 2.656   1.00 20.14 ?  138 HIS   B NE2  1 
ATOM   6023 H H    . HIS   B 1 138 ? 34.848 -34.777 -0.548  1.00 19.86 ?  138 HIS   B H    1 
ATOM   6024 H HA   . HIS   B 1 138 ? 32.585 -33.530 -0.998  1.00 20.27 ?  138 HIS   B HA   1 
ATOM   6025 H HB2  . HIS   B 1 138 ? 33.002 -34.438 1.092   1.00 22.11 ?  138 HIS   B HB2  1 
ATOM   6026 H HB3  . HIS   B 1 138 ? 34.204 -33.422 1.309   1.00 22.11 ?  138 HIS   B HB3  1 
ATOM   6027 H HD1  . HIS   B 1 138 ? 30.660 -33.033 0.637   1.00 24.66 ?  138 HIS   B HD1  1 
ATOM   6028 H HD2  . HIS   B 1 138 ? 33.398 -31.372 2.858   1.00 23.54 ?  138 HIS   B HD2  1 
ATOM   6029 H HE1  . HIS   B 1 138 ? 29.568 -31.328 1.855   1.00 24.24 ?  138 HIS   B HE1  1 
ATOM   6030 N N    . SER   B 1 139 ? 35.172 -31.644 -0.858  1.00 15.14 ?  139 SER   B N    1 
ATOM   6031 C CA   . SER   B 1 139 ? 35.613 -30.294 -1.174  1.00 14.87 ?  139 SER   B CA   1 
ATOM   6032 C C    . SER   B 1 139 ? 35.275 -29.935 -2.612  1.00 14.01 ?  139 SER   B C    1 
ATOM   6033 O O    . SER   B 1 139 ? 34.831 -28.816 -2.888  1.00 14.39 ?  139 SER   B O    1 
ATOM   6034 C CB   . SER   B 1 139 ? 37.107 -30.158 -0.910  1.00 14.98 ?  139 SER   B CB   1 
ATOM   6035 O OG   . SER   B 1 139 ? 37.517 -28.816 -1.154  1.00 15.06 ?  139 SER   B OG   1 
ATOM   6036 H H    . SER   B 1 139 ? 35.795 -32.195 -0.652  1.00 18.17 ?  139 SER   B H    1 
ATOM   6037 H HA   . SER   B 1 139 ? 35.145 -29.671 -0.605  1.00 17.84 ?  139 SER   B HA   1 
ATOM   6038 H HB2  . SER   B 1 139 ? 37.284 -30.391 0.016   1.00 17.98 ?  139 SER   B HB2  1 
ATOM   6039 H HB3  . SER   B 1 139 ? 37.594 -30.752 -1.502  1.00 17.98 ?  139 SER   B HB3  1 
ATOM   6040 H HG   . SER   B 1 139 ? 38.346 -28.743 -0.993  1.00 18.07 ?  139 SER   B HG   1 
ATOM   6041 N N    . LEU   B 1 140 ? 35.474 -30.873 -3.540  1.00 13.30 ?  140 LEU   B N    1 
ATOM   6042 C CA   . LEU   B 1 140 ? 35.104 -30.629 -4.928  1.00 13.40 ?  140 LEU   B CA   1 
ATOM   6043 C C    . LEU   B 1 140 ? 33.600 -30.403 -5.059  1.00 13.88 ?  140 LEU   B C    1 
ATOM   6044 O O    . LEU   B 1 140 ? 33.164 -29.523 -5.805  1.00 14.18 ?  140 LEU   B O    1 
ATOM   6045 C CB   . LEU   B 1 140 ? 35.576 -31.794 -5.803  1.00 13.97 ?  140 LEU   B CB   1 
ATOM   6046 C CG   . LEU   B 1 140 ? 35.223 -31.686 -7.280  1.00 14.14 ?  140 LEU   B CG   1 
ATOM   6047 C CD1  . LEU   B 1 140 ? 35.798 -30.405 -7.868  1.00 15.45 ?  140 LEU   B CD1  1 
ATOM   6048 C CD2  . LEU   B 1 140 ? 35.723 -32.910 -8.025  1.00 15.17 ?  140 LEU   B CD2  1 
ATOM   6049 H H    . LEU   B 1 140 ? 35.818 -31.649 -3.398  1.00 15.96 ?  140 LEU   B H    1 
ATOM   6050 H HA   . LEU   B 1 140 ? 35.557 -29.830 -5.239  1.00 16.08 ?  140 LEU   B HA   1 
ATOM   6051 H HB2  . LEU   B 1 140 ? 36.544 -31.860 -5.747  1.00 16.76 ?  140 LEU   B HB2  1 
ATOM   6052 H HB3  . LEU   B 1 140 ? 35.178 -32.616 -5.474  1.00 16.76 ?  140 LEU   B HB3  1 
ATOM   6053 H HG   . LEU   B 1 140 ? 34.255 -31.648 -7.375  1.00 16.96 ?  140 LEU   B HG   1 
ATOM   6054 H HD11 . LEU   B 1 140 ? 35.703 -30.433 -8.832  1.00 18.54 ?  140 LEU   B HD11 1 
ATOM   6055 H HD12 . LEU   B 1 140 ? 35.313 -29.645 -7.509  1.00 18.54 ?  140 LEU   B HD12 1 
ATOM   6056 H HD13 . LEU   B 1 140 ? 36.735 -30.346 -7.629  1.00 18.54 ?  140 LEU   B HD13 1 
ATOM   6057 H HD21 . LEU   B 1 140 ? 35.484 -32.821 -8.962  1.00 18.21 ?  140 LEU   B HD21 1 
ATOM   6058 H HD22 . LEU   B 1 140 ? 36.681 -32.962 -7.928  1.00 18.21 ?  140 LEU   B HD22 1 
ATOM   6059 H HD23 . LEU   B 1 140 ? 35.300 -33.695 -7.649  1.00 18.21 ?  140 LEU   B HD23 1 
ATOM   6060 N N    . ARG   B 1 141 ? 32.798 -31.186 -4.336  1.00 13.76 ?  141 ARG   B N    1 
ATOM   6061 C CA   . ARG   B 1 141 ? 31.348 -31.015 -4.329  1.00 15.20 ?  141 ARG   B CA   1 
ATOM   6062 C C    . ARG   B 1 141 ? 30.964 -29.607 -3.896  1.00 14.60 ?  141 ARG   B C    1 
ATOM   6063 O O    . ARG   B 1 141 ? 30.158 -28.932 -4.552  1.00 14.99 ?  141 ARG   B O    1 
ATOM   6064 C CB   . ARG   B 1 141 ? 30.764 -32.044 -3.355  1.00 16.90 ?  141 ARG   B CB   1 
ATOM   6065 C CG   . ARG   B 1 141 ? 29.301 -31.910 -3.015  1.00 19.53 ?  141 ARG   B CG   1 
ATOM   6066 C CD   . ARG   B 1 141 ? 28.488 -32.550 -4.069  1.00 21.42 ?  141 ARG   B CD   1 
ATOM   6067 N NE   . ARG   B 1 141 ? 28.232 -31.651 -5.182  1.00 21.71 ?  141 ARG   B NE   1 
ATOM   6068 C CZ   . ARG   B 1 141 ? 28.239 -32.011 -6.458  1.00 21.22 ?  141 ARG   B CZ   1 
ATOM   6069 N NH1  . ARG   B 1 141 ? 28.682 -33.198 -6.842  1.00 21.02 ?  141 ARG   B NH1  1 
ATOM   6070 N NH2  . ARG   B 1 141 ? 27.789 -31.158 -7.373  1.00 21.90 ?  141 ARG   B NH2  1 
ATOM   6071 H H    . ARG   B 1 141 ? 33.081 -31.826 -3.836  1.00 16.51 ?  141 ARG   B H    1 
ATOM   6072 H HA   . ARG   B 1 141 ? 30.993 -31.181 -5.212  1.00 18.24 ?  141 ARG   B HA   1 
ATOM   6073 H HB2  . ARG   B 1 141 ? 30.901 -32.932 -3.734  1.00 20.28 ?  141 ARG   B HB2  1 
ATOM   6074 H HB3  . ARG   B 1 141 ? 31.255 -31.987 -2.522  1.00 20.28 ?  141 ARG   B HB3  1 
ATOM   6075 H HG2  . ARG   B 1 141 ? 29.131 -32.353 -2.173  1.00 23.44 ?  141 ARG   B HG2  1 
ATOM   6076 H HG3  . ARG   B 1 141 ? 29.054 -30.971 -2.956  1.00 23.44 ?  141 ARG   B HG3  1 
ATOM   6077 H HD2  . ARG   B 1 141 ? 28.954 -33.339 -4.397  1.00 25.71 ?  141 ARG   B HD2  1 
ATOM   6078 H HD3  . ARG   B 1 141 ? 27.640 -32.813 -3.689  1.00 25.71 ?  141 ARG   B HD3  1 
ATOM   6079 H HE   . ARG   B 1 141 ? 28.044 -30.833 -4.996  1.00 26.06 ?  141 ARG   B HE   1 
ATOM   6080 H HH11 . ARG   B 1 141 ? 28.963 -33.768 -6.264  1.00 25.22 ?  141 ARG   B HH11 1 
ATOM   6081 H HH12 . ARG   B 1 141 ? 28.683 -33.403 -7.675  1.00 25.22 ?  141 ARG   B HH12 1 
ATOM   6082 H HH21 . ARG   B 1 141 ? 27.508 -30.377 -7.134  1.00 26.28 ?  141 ARG   B HH21 1 
ATOM   6083 H HH22 . ARG   B 1 141 ? 27.808 -31.366 -8.206  1.00 26.28 ?  141 ARG   B HH22 1 
ATOM   6084 N N    . VAL   B 1 142 ? 31.506 -29.166 -2.765  1.00 14.22 ?  142 VAL   B N    1 
ATOM   6085 C CA   . VAL   B 1 142 ? 31.178 -27.830 -2.280  1.00 14.34 ?  142 VAL   B CA   1 
ATOM   6086 C C    . VAL   B 1 142 ? 31.654 -26.773 -3.269  1.00 14.07 ?  142 VAL   B C    1 
ATOM   6087 O O    . VAL   B 1 142 ? 30.959 -25.780 -3.518  1.00 14.63 ?  142 VAL   B O    1 
ATOM   6088 C CB   . VAL   B 1 142 ? 31.734 -27.602 -0.863  1.00 15.11 ?  142 VAL   B CB   1 
ATOM   6089 C CG1  . VAL   B 1 142 ? 31.434 -26.172 -0.398  1.00 15.34 ?  142 VAL   B CG1  1 
ATOM   6090 C CG2  . VAL   B 1 142 ? 31.143 -28.619 0.105   1.00 15.66 ?  142 VAL   B CG2  1 
ATOM   6091 H H    . VAL   B 1 142 ? 32.055 -29.607 -2.268  1.00 17.07 ?  142 VAL   B H    1 
ATOM   6092 H HA   . VAL   B 1 142 ? 30.218 -27.754 -2.221  1.00 17.21 ?  142 VAL   B HA   1 
ATOM   6093 H HB   . VAL   B 1 142 ? 32.700 -27.722 -0.874  1.00 18.14 ?  142 VAL   B HB   1 
ATOM   6094 H HG11 . VAL   B 1 142 ? 31.621 -26.106 0.550   1.00 18.41 ?  142 VAL   B HG11 1 
ATOM   6095 H HG12 . VAL   B 1 142 ? 32.003 -25.555 -0.889  1.00 18.41 ?  142 VAL   B HG12 1 
ATOM   6096 H HG13 . VAL   B 1 142 ? 30.504 -25.976 -0.570  1.00 18.41 ?  142 VAL   B HG13 1 
ATOM   6097 H HG21 . VAL   B 1 142 ? 31.469 -28.431 0.998   1.00 18.79 ?  142 VAL   B HG21 1 
ATOM   6098 H HG22 . VAL   B 1 142 ? 30.178 -28.550 0.080   1.00 18.79 ?  142 VAL   B HG22 1 
ATOM   6099 H HG23 . VAL   B 1 142 ? 31.419 -29.510 -0.167  1.00 18.79 ?  142 VAL   B HG23 1 
ATOM   6100 N N    . CYS   B 1 143 ? 32.841 -26.967 -3.846  1.00 13.39 ?  143 CYS   B N    1 
ATOM   6101 C CA   . CYS   B 1 143 ? 33.344 -26.030 -4.848  1.00 13.46 ?  143 CYS   B CA   1 
ATOM   6102 C C    . CYS   B 1 143 ? 32.344 -25.878 -5.991  1.00 13.55 ?  143 CYS   B C    1 
ATOM   6103 O O    . CYS   B 1 143 ? 31.931 -24.765 -6.340  1.00 13.78 ?  143 CYS   B O    1 
ATOM   6104 C CB   . CYS   B 1 143 ? 34.703 -26.511 -5.371  1.00 13.87 ?  143 CYS   B CB   1 
ATOM   6105 S SG   . CYS   B 1 143 ? 35.440 -25.411 -6.597  1.00 14.49 ?  143 CYS   B SG   1 
ATOM   6106 H H    . CYS   B 1 143 ? 33.372 -27.622 -3.675  1.00 16.07 ?  143 CYS   B H    1 
ATOM   6107 H HA   . CYS   B 1 143 ? 33.470 -25.161 -4.440  1.00 16.15 ?  143 CYS   B HA   1 
ATOM   6108 H HB2  . CYS   B 1 143 ? 35.324 -26.585 -4.628  1.00 16.64 ?  143 CYS   B HB2  1 
ATOM   6109 H HB3  . CYS   B 1 143 ? 34.590 -27.379 -5.785  1.00 16.64 ?  143 CYS   B HB3  1 
ATOM   6110 H HG   . CYS   B 1 143 ? 36.512 -25.836 -6.921  1.00 17.39 ?  143 CYS   B HG   1 
ATOM   6111 N N    . VAL   B 1 144 ? 31.932 -26.997 -6.583  1.00 14.09 ?  144 VAL   B N    1 
ATOM   6112 C CA   . VAL   B 1 144 ? 31.032 -26.927 -7.729  1.00 14.93 ?  144 VAL   B CA   1 
ATOM   6113 C C    . VAL   B 1 144 ? 29.685 -26.322 -7.355  1.00 15.02 ?  144 VAL   B C    1 
ATOM   6114 O O    . VAL   B 1 144 ? 29.056 -25.635 -8.171  1.00 16.16 ?  144 VAL   B O    1 
ATOM   6115 C CB   . VAL   B 1 144 ? 30.883 -28.336 -8.324  1.00 18.14 ?  144 VAL   B CB   1 
ATOM   6116 C CG1  . VAL   B 1 144 ? 29.610 -28.457 -9.162  1.00 20.87 ?  144 VAL   B CG1  1 
ATOM   6117 C CG2  . VAL   B 1 144 ? 32.132 -28.719 -9.113  1.00 17.72 ?  144 VAL   B CG2  1 
ATOM   6118 H H    . VAL   B 1 144 ? 32.165 -27.795 -6.355  1.00 16.91 ?  144 VAL   B H    1 
ATOM   6119 H HA   . VAL   B 1 144 ? 31.427 -26.362 -8.409  1.00 17.92 ?  144 VAL   B HA   1 
ATOM   6120 H HB   . VAL   B 1 144 ? 30.807 -28.971 -7.594  1.00 21.77 ?  144 VAL   B HB   1 
ATOM   6121 H HG11 . VAL   B 1 144 ? 29.689 -29.238 -9.736  1.00 25.05 ?  144 VAL   B HG11 1 
ATOM   6122 H HG12 . VAL   B 1 144 ? 28.851 -28.562 -8.570  1.00 25.05 ?  144 VAL   B HG12 1 
ATOM   6123 H HG13 . VAL   B 1 144 ? 29.512 -27.662 -9.704  1.00 25.05 ?  144 VAL   B HG13 1 
ATOM   6124 H HG21 . VAL   B 1 144 ? 32.021 -29.611 -9.475  1.00 21.27 ?  144 VAL   B HG21 1 
ATOM   6125 H HG22 . VAL   B 1 144 ? 32.254 -28.082 -9.839  1.00 21.27 ?  144 VAL   B HG22 1 
ATOM   6126 H HG23 . VAL   B 1 144 ? 32.901 -28.693 -8.523  1.00 21.27 ?  144 VAL   B HG23 1 
ATOM   6127 N N    . ASP   B 1 145 ? 29.215 -26.567 -6.137  1.00 15.08 ?  145 ASP   B N    1 
ATOM   6128 C CA   . ASP   B 1 145 ? 27.908 -26.095 -5.704  1.00 16.02 ?  145 ASP   B CA   1 
ATOM   6129 C C    . ASP   B 1 145 ? 27.939 -24.675 -5.149  1.00 15.31 ?  145 ASP   B C    1 
ATOM   6130 O O    . ASP   B 1 145 ? 26.876 -24.140 -4.809  1.00 17.56 ?  145 ASP   B O    1 
ATOM   6131 C CB   . ASP   B 1 145 ? 27.333 -27.016 -4.620  1.00 17.76 ?  145 ASP   B CB   1 
ATOM   6132 C CG   . ASP   B 1 145 ? 26.961 -28.391 -5.133  1.00 19.56 ?  145 ASP   B CG   1 
ATOM   6133 O OD1  . ASP   B 1 145 ? 26.862 -28.593 -6.360  1.00 19.68 ?  145 ASP   B OD1  1 
ATOM   6134 O OD2  . ASP   B 1 145 ? 26.752 -29.273 -4.279  1.00 21.50 -1 145 ASP   B OD2  1 
ATOM   6135 H H    . ASP   B 1 145 ? 29.646 -27.002 -5.535  1.00 18.10 ?  145 ASP   B H    1 
ATOM   6136 H HA   . ASP   B 1 145 ? 27.307 -26.091 -6.463  1.00 19.23 ?  145 ASP   B HA   1 
ATOM   6137 H HB2  . ASP   B 1 145 ? 27.993 -27.137 -3.929  1.00 21.32 ?  145 ASP   B HB2  1 
ATOM   6138 H HB3  . ASP   B 1 145 ? 26.533 -26.604 -4.257  1.00 21.32 ?  145 ASP   B HB3  1 
ATOM   6139 N N    . THR   B 1 146 ? 29.118 -24.063 -5.029  1.00 13.98 ?  146 THR   B N    1 
ATOM   6140 C CA   . THR   B 1 146 ? 29.254 -22.741 -4.424  1.00 13.71 ?  146 THR   B CA   1 
ATOM   6141 C C    . THR   B 1 146 ? 29.885 -21.714 -5.344  1.00 13.53 ?  146 THR   B C    1 
ATOM   6142 O O    . THR   B 1 146 ? 29.428 -20.556 -5.391  1.00 13.86 ?  146 THR   B O    1 
ATOM   6143 C CB   . THR   B 1 146 ? 30.078 -22.845 -3.134  1.00 13.97 ?  146 THR   B CB   1 
ATOM   6144 O OG1  . THR   B 1 146 ? 29.505 -23.833 -2.272  1.00 14.21 ?  146 THR   B OG1  1 
ATOM   6145 C CG2  . THR   B 1 146 ? 30.146 -21.499 -2.413  1.00 14.24 ?  146 THR   B CG2  1 
ATOM   6146 H H    . THR   B 1 146 ? 29.866 -24.392 -5.298  1.00 16.77 ?  146 THR   B H    1 
ATOM   6147 H HA   . THR   B 1 146 ? 28.378 -22.409 -4.185  1.00 16.45 ?  146 THR   B HA   1 
ATOM   6148 H HB   . THR   B 1 146 ? 30.988 -23.099 -3.360  1.00 16.77 ?  146 THR   B HB   1 
ATOM   6149 H HG1  . THR   B 1 146 ? 29.541 -24.592 -2.650  1.00 17.06 ?  146 THR   B HG1  1 
ATOM   6150 H HG21 . THR   B 1 146 ? 30.505 -21.618 -1.521  1.00 17.09 ?  146 THR   B HG21 1 
ATOM   6151 H HG22 . THR   B 1 146 ? 30.721 -20.884 -2.901  1.00 17.09 ?  146 THR   B HG22 1 
ATOM   6152 H HG23 . THR   B 1 146 ? 29.259 -21.112 -2.347  1.00 17.09 ?  146 THR   B HG23 1 
ATOM   6153 N N    . VAL   B 1 147 ? 30.945 -22.090 -6.049  1.00 13.05 ?  147 VAL   B N    1 
ATOM   6154 C CA   . VAL   B 1 147 ? 31.669 -21.141 -6.879  1.00 12.92 ?  147 VAL   B CA   1 
ATOM   6155 C C    . VAL   B 1 147 ? 30.943 -20.999 -8.203  1.00 13.15 ?  147 VAL   B C    1 
ATOM   6156 O O    . VAL   B 1 147 ? 30.571 -21.995 -8.836  1.00 14.23 ?  147 VAL   B O    1 
ATOM   6157 C CB   . VAL   B 1 147 ? 33.123 -21.594 -7.079  1.00 13.34 ?  147 VAL   B CB   1 
ATOM   6158 C CG1  . VAL   B 1 147 ? 33.879 -20.561 -7.895  1.00 13.62 ?  147 VAL   B CG1  1 
ATOM   6159 C CG2  . VAL   B 1 147 ? 33.788 -21.813 -5.733  1.00 13.57 ?  147 VAL   B CG2  1 
ATOM   6160 H H    . VAL   B 1 147 ? 31.265 -22.894 -6.071  1.00 15.66 ?  147 VAL   B H    1 
ATOM   6161 H HA   . VAL   B 1 147 ? 31.683 -20.279 -6.441  1.00 15.51 ?  147 VAL   B HA   1 
ATOM   6162 H HB   . VAL   B 1 147 ? 33.139 -22.435 -7.567  1.00 16.01 ?  147 VAL   B HB   1 
ATOM   6163 H HG11 . VAL   B 1 147 ? 34.828 -20.770 -7.874  1.00 16.35 ?  147 VAL   B HG11 1 
ATOM   6164 H HG12 . VAL   B 1 147 ? 33.560 -20.575 -8.809  1.00 16.35 ?  147 VAL   B HG12 1 
ATOM   6165 H HG13 . VAL   B 1 147 ? 33.732 -19.682 -7.505  1.00 16.35 ?  147 VAL   B HG13 1 
ATOM   6166 H HG21 . VAL   B 1 147 ? 34.734 -21.990 -5.870  1.00 16.29 ?  147 VAL   B HG21 1 
ATOM   6167 H HG22 . VAL   B 1 147 ? 33.678 -21.015 -5.193  1.00 16.29 ?  147 VAL   B HG22 1 
ATOM   6168 H HG23 . VAL   B 1 147 ? 33.373 -22.571 -5.292  1.00 16.29 ?  147 VAL   B HG23 1 
ATOM   6169 N N    . ARG   B 1 148 ? 30.727 -19.747 -8.615  1.00 13.02 ?  148 ARG   B N    1 
ATOM   6170 C CA   . ARG   B 1 148 ? 30.104 -19.427 -9.889  1.00 13.25 ?  148 ARG   B CA   1 
ATOM   6171 C C    . ARG   B 1 148 ? 31.059 -18.765 -10.868 1.00 13.12 ?  148 ARG   B C    1 
ATOM   6172 O O    . ARG   B 1 148 ? 30.771 -18.750 -12.067 1.00 14.60 ?  148 ARG   B O    1 
ATOM   6173 C CB   . ARG   B 1 148 ? 28.865 -18.541 -9.674  1.00 13.67 ?  148 ARG   B CB   1 
ATOM   6174 C CG   . ARG   B 1 148 ? 27.788 -19.249 -8.863  1.00 14.70 ?  148 ARG   B CG   1 
ATOM   6175 C CD   . ARG   B 1 148 ? 26.582 -18.364 -8.567  1.00 15.50 ?  148 ARG   B CD   1 
ATOM   6176 N NE   . ARG   B 1 148 ? 26.959 -17.167 -7.828  1.00 15.44 ?  148 ARG   B NE   1 
ATOM   6177 C CZ   . ARG   B 1 148 ? 27.268 -17.142 -6.537  1.00 14.53 ?  148 ARG   B CZ   1 
ATOM   6178 N NH1  . ARG   B 1 148 ? 27.203 -18.232 -5.787  1.00 14.49 ?  148 ARG   B NH1  1 
ATOM   6179 N NH2  . ARG   B 1 148 ? 27.660 -15.995 -5.987  1.00 14.81 ?  148 ARG   B NH2  1 
ATOM   6180 H H    . ARG   B 1 148 ? 30.946 -19.048 -8.155  1.00 15.62 ?  148 ARG   B H    1 
ATOM   6181 H HA   . ARG   B 1 148 ? 29.801 -20.254 -10.293 1.00 15.90 ?  148 ARG   B HA   1 
ATOM   6182 H HB2  . ARG   B 1 148 ? 29.130 -17.740 -9.193  1.00 16.41 ?  148 ARG   B HB2  1 
ATOM   6183 H HB3  . ARG   B 1 148 ? 28.493 -18.306 -10.536 1.00 16.41 ?  148 ARG   B HB3  1 
ATOM   6184 H HG2  . ARG   B 1 148 ? 27.479 -20.022 -9.361  1.00 17.63 ?  148 ARG   B HG2  1 
ATOM   6185 H HG3  . ARG   B 1 148 ? 28.168 -19.533 -8.016  1.00 17.63 ?  148 ARG   B HG3  1 
ATOM   6186 H HD2  . ARG   B 1 148 ? 26.176 -18.087 -9.402  1.00 18.60 ?  148 ARG   B HD2  1 
ATOM   6187 H HD3  . ARG   B 1 148 ? 25.943 -18.863 -8.033  1.00 18.60 ?  148 ARG   B HD3  1 
ATOM   6188 H HE   . ARG   B 1 148 ? 26.996 -16.426 -8.257  1.00 18.53 ?  148 ARG   B HE   1 
ATOM   6189 H HH11 . ARG   B 1 148 ? 26.951 -18.981 -6.127  1.00 17.39 ?  148 ARG   B HH11 1 
ATOM   6190 H HH12 . ARG   B 1 148 ? 27.402 -18.191 -4.948  1.00 17.39 ?  148 ARG   B HH12 1 
ATOM   6191 H HH21 . ARG   B 1 148 ? 27.705 -15.284 -6.465  1.00 17.77 ?  148 ARG   B HH21 1 
ATOM   6192 H HH22 . ARG   B 1 148 ? 27.856 -15.964 -5.150  1.00 17.77 ?  148 ARG   B HH22 1 
ATOM   6193 N N    . THR   B 1 149 ? 32.164 -18.202 -10.383 1.00 13.15 ?  149 THR   B N    1 
ATOM   6194 C CA   . THR   B 1 149 ? 33.204 -17.642 -11.231 1.00 13.56 ?  149 THR   B CA   1 
ATOM   6195 C C    . THR   B 1 149 ? 34.090 -18.782 -11.738 1.00 13.16 ?  149 THR   B C    1 
ATOM   6196 O O    . THR   B 1 149 ? 33.889 -19.954 -11.405 1.00 13.72 ?  149 THR   B O    1 
ATOM   6197 C CB   . THR   B 1 149 ? 33.978 -16.592 -10.444 1.00 13.54 ?  149 THR   B CB   1 
ATOM   6198 O OG1  . THR   B 1 149 ? 34.435 -17.191 -9.232  1.00 13.60 ?  149 THR   B OG1  1 
ATOM   6199 C CG2  . THR   B 1 149 ? 33.088 -15.385 -10.138 1.00 14.15 ?  149 THR   B CG2  1 
ATOM   6200 H H    . THR   B 1 149 ? 32.329 -18.128 -9.544  1.00 15.78 ?  149 THR   B H    1 
ATOM   6201 H HA   . THR   B 1 149 ? 32.796 -17.210 -11.997 1.00 16.27 ?  149 THR   B HA   1 
ATOM   6202 H HB   . THR   B 1 149 ? 34.738 -16.297 -10.962 1.00 16.24 ?  149 THR   B HB   1 
ATOM   6203 H HG1  . THR   B 1 149 ? 34.856 -16.623 -8.770  1.00 16.32 ?  149 THR   B HG1  1 
ATOM   6204 H HG21 . THR   B 1 149 ? 33.592 -14.716 -9.650  1.00 16.97 ?  149 THR   B HG21 1 
ATOM   6205 H HG22 . THR   B 1 149 ? 32.763 -14.993 -10.965 1.00 16.97 ?  149 THR   B HG22 1 
ATOM   6206 H HG23 . THR   B 1 149 ? 32.326 -15.657 -9.601  1.00 16.97 ?  149 THR   B HG23 1 
ATOM   6207 N N    . ASN   B 1 150 ? 35.063 -18.461 -12.578 1.00 13.11 ?  150 ASN   B N    1 
ATOM   6208 C CA   . ASN   B 1 150 ? 35.828 -19.484 -13.285 1.00 13.49 ?  150 ASN   B CA   1 
ATOM   6209 C C    . ASN   B 1 150 ? 36.991 -19.935 -12.413 1.00 13.22 ?  150 ASN   B C    1 
ATOM   6210 O O    . ASN   B 1 150 ? 37.922 -19.164 -12.154 1.00 14.09 ?  150 ASN   B O    1 
ATOM   6211 C CB   . ASN   B 1 150 ? 36.300 -18.932 -14.623 1.00 15.34 ?  150 ASN   B CB   1 
ATOM   6212 C CG   . ASN   B 1 150 ? 35.158 -18.724 -15.575 1.00 18.17 ?  150 ASN   B CG   1 
ATOM   6213 O OD1  . ASN   B 1 150 ? 34.283 -19.574 -15.687 1.00 19.34 ?  150 ASN   B OD1  1 
ATOM   6214 N ND2  . ASN   B 1 150 ? 35.132 -17.580 -16.234 1.00 20.18 ?  150 ASN   B ND2  1 
ATOM   6215 H H    . ASN   B 1 150 ? 35.315 -17.653 -12.748 1.00 15.73 ?  150 ASN   B H    1 
ATOM   6216 H HA   . ASN   B 1 150 ? 35.252 -20.247 -13.459 1.00 16.19 ?  150 ASN   B HA   1 
ATOM   6217 H HB2  . ASN   B 1 150 ? 36.733 -18.073 -14.480 1.00 18.40 ?  150 ASN   B HB2  1 
ATOM   6218 H HB3  . ASN   B 1 150 ? 36.922 -19.556 -15.026 1.00 18.40 ?  150 ASN   B HB3  1 
ATOM   6219 H HD21 . ASN   B 1 150 ? 34.496 -17.416 -16.792 1.00 24.22 ?  150 ASN   B HD21 1 
ATOM   6220 H HD22 . ASN   B 1 150 ? 35.760 -17.001 -16.122 1.00 24.22 ?  150 ASN   B HD22 1 
ATOM   6221 N N    . VAL   B 1 151 ? 36.951 -21.184 -11.964 1.00 13.21 ?  151 VAL   B N    1 
ATOM   6222 C CA   . VAL   B 1 151 ? 37.969 -21.716 -11.070 1.00 13.00 ?  151 VAL   B CA   1 
ATOM   6223 C C    . VAL   B 1 151 ? 38.677 -22.886 -11.744 1.00 13.05 ?  151 VAL   B C    1 
ATOM   6224 O O    . VAL   B 1 151 ? 38.035 -23.821 -12.248 1.00 14.10 ?  151 VAL   B O    1 
ATOM   6225 C CB   . VAL   B 1 151 ? 37.409 -22.058 -9.674  1.00 14.29 ?  151 VAL   B CB   1 
ATOM   6226 C CG1  . VAL   B 1 151 ? 36.239 -23.044 -9.751  1.00 15.64 ?  151 VAL   B CG1  1 
ATOM   6227 C CG2  . VAL   B 1 151 ? 38.521 -22.568 -8.767  1.00 14.65 ?  151 VAL   B CG2  1 
ATOM   6228 H H    . VAL   B 1 151 ? 36.333 -21.752 -12.174 1.00 15.85 ?  151 VAL   B H    1 
ATOM   6229 H HA   . VAL   B 1 151 ? 38.633 -21.022 -10.940 1.00 15.61 ?  151 VAL   B HA   1 
ATOM   6230 H HB   . VAL   B 1 151 ? 37.068 -21.238 -9.278  1.00 17.14 ?  151 VAL   B HB   1 
ATOM   6231 H HG11 . VAL   B 1 151 ? 35.925 -23.235 -8.852  1.00 18.76 ?  151 VAL   B HG11 1 
ATOM   6232 H HG12 . VAL   B 1 151 ? 35.519 -22.647 -10.271 1.00 18.76 ?  151 VAL   B HG12 1 
ATOM   6233 H HG13 . VAL   B 1 151 ? 36.538 -23.862 -10.176 1.00 18.76 ?  151 VAL   B HG13 1 
ATOM   6234 H HG21 . VAL   B 1 151 ? 38.180 -22.637 -7.860  1.00 17.58 ?  151 VAL   B HG21 1 
ATOM   6235 H HG22 . VAL   B 1 151 ? 38.811 -23.439 -9.077  1.00 17.58 ?  151 VAL   B HG22 1 
ATOM   6236 H HG23 . VAL   B 1 151 ? 39.263 -21.942 -8.790  1.00 17.58 ?  151 VAL   B HG23 1 
ATOM   6237 N N    . TYR   B 1 152 ? 40.009 -22.799 -11.762 1.00 12.41 ?  152 TYR   B N    1 
ATOM   6238 C CA   . TYR   B 1 152 ? 40.912 -23.783 -12.341 1.00 12.63 ?  152 TYR   B CA   1 
ATOM   6239 C C    . TYR   B 1 152 ? 41.634 -24.462 -11.184 1.00 11.90 ?  152 TYR   B C    1 
ATOM   6240 O O    . TYR   B 1 152 ? 42.477 -23.846 -10.526 1.00 12.43 ?  152 TYR   B O    1 
ATOM   6241 C CB   . TYR   B 1 152 ? 41.880 -23.071 -13.286 1.00 13.47 ?  152 TYR   B CB   1 
ATOM   6242 C CG   . TYR   B 1 152 ? 41.199 -22.607 -14.551 1.00 14.15 ?  152 TYR   B CG   1 
ATOM   6243 C CD1  . TYR   B 1 152 ? 40.533 -21.383 -14.614 1.00 14.38 ?  152 TYR   B CD1  1 
ATOM   6244 C CD2  . TYR   B 1 152 ? 41.201 -23.408 -15.678 1.00 15.29 ?  152 TYR   B CD2  1 
ATOM   6245 C CE1  . TYR   B 1 152 ? 39.898 -20.977 -15.774 1.00 15.82 ?  152 TYR   B CE1  1 
ATOM   6246 C CE2  . TYR   B 1 152 ? 40.566 -23.019 -16.836 1.00 16.14 ?  152 TYR   B CE2  1 
ATOM   6247 C CZ   . TYR   B 1 152 ? 39.915 -21.804 -16.883 1.00 16.03 ?  152 TYR   B CZ   1 
ATOM   6248 O OH   . TYR   B 1 152 ? 39.291 -21.434 -18.050 1.00 18.81 ?  152 TYR   B OH   1 
ATOM   6249 H H    . TYR   B 1 152 ? 40.441 -22.136 -11.408 1.00 14.90 ?  152 TYR   B H    1 
ATOM   6250 H HA   . TYR   B 1 152 ? 40.405 -24.444 -12.837 1.00 15.16 ?  152 TYR   B HA   1 
ATOM   6251 H HB2  . TYR   B 1 152 ? 42.247 -22.293 -12.833 1.00 16.16 ?  152 TYR   B HB2  1 
ATOM   6252 H HB3  . TYR   B 1 152 ? 42.594 -23.680 -13.527 1.00 16.16 ?  152 TYR   B HB3  1 
ATOM   6253 H HD1  . TYR   B 1 152 ? 40.516 -20.832 -13.863 1.00 17.26 ?  152 TYR   B HD1  1 
ATOM   6254 H HD2  . TYR   B 1 152 ? 41.636 -24.232 -15.650 1.00 18.35 ?  152 TYR   B HD2  1 
ATOM   6255 H HE1  . TYR   B 1 152 ? 39.456 -20.160 -15.808 1.00 18.98 ?  152 TYR   B HE1  1 
ATOM   6256 H HE2  . TYR   B 1 152 ? 40.587 -23.571 -17.583 1.00 19.37 ?  152 TYR   B HE2  1 
ATOM   6257 H HH   . TYR   B 1 152 ? 38.939 -20.675 -17.955 1.00 22.57 ?  152 TYR   B HH   1 
ATOM   6258 N N    . LEU   B 1 153 ? 41.264 -25.715 -10.914 1.00 12.32 ?  153 LEU   B N    1 
ATOM   6259 C CA   . LEU   B 1 153 ? 41.772 -26.469 -9.778  1.00 12.42 ?  153 LEU   B CA   1 
ATOM   6260 C C    . LEU   B 1 153 ? 43.006 -27.268 -10.175 1.00 12.53 ?  153 LEU   B C    1 
ATOM   6261 O O    . LEU   B 1 153 ? 42.986 -28.000 -11.169 1.00 13.61 ?  153 LEU   B O    1 
ATOM   6262 C CB   . LEU   B 1 153 ? 40.691 -27.428 -9.273  1.00 12.81 ?  153 LEU   B CB   1 
ATOM   6263 C CG   . LEU   B 1 153 ? 39.434 -26.771 -8.700  1.00 13.43 ?  153 LEU   B CG   1 
ATOM   6264 C CD1  . LEU   B 1 153 ? 38.339 -27.816 -8.550  1.00 14.17 ?  153 LEU   B CD1  1 
ATOM   6265 C CD2  . LEU   B 1 153 ? 39.727 -26.114 -7.362  1.00 13.76 ?  153 LEU   B CD2  1 
ATOM   6266 H H    . LEU   B 1 153 ? 40.692 -26.160 -11.390 1.00 14.79 ?  153 LEU   B H    1 
ATOM   6267 H HA   . LEU   B 1 153 ? 41.997 -25.859 -9.063  1.00 14.90 ?  153 LEU   B HA   1 
ATOM   6268 H HB2  . LEU   B 1 153 ? 40.407 -27.993 -10.010 1.00 15.38 ?  153 LEU   B HB2  1 
ATOM   6269 H HB3  . LEU   B 1 153 ? 41.071 -27.981 -8.572  1.00 15.38 ?  153 LEU   B HB3  1 
ATOM   6270 H HG   . LEU   B 1 153 ? 39.123 -26.084 -9.310  1.00 16.11 ?  153 LEU   B HG   1 
ATOM   6271 H HD11 . LEU   B 1 153 ? 37.537 -27.380 -8.213  1.00 17.00 ?  153 LEU   B HD11 1 
ATOM   6272 H HD12 . LEU   B 1 153 ? 38.162 -28.208 -9.415  1.00 17.00 ?  153 LEU   B HD12 1 
ATOM   6273 H HD13 . LEU   B 1 153 ? 38.635 -28.492 -7.925  1.00 17.00 ?  153 LEU   B HD13 1 
ATOM   6274 H HD21 . LEU   B 1 153 ? 38.909 -25.745 -7.000  1.00 16.51 ?  153 LEU   B HD21 1 
ATOM   6275 H HD22 . LEU   B 1 153 ? 40.087 -26.783 -6.753  1.00 16.51 ?  153 LEU   B HD22 1 
ATOM   6276 H HD23 . LEU   B 1 153 ? 40.382 -25.407 -7.491  1.00 16.51 ?  153 LEU   B HD23 1 
ATOM   6277 N N    . ALA   B 1 154 ? 44.059 -27.157 -9.369  1.00 12.59 ?  154 ALA   B N    1 
ATOM   6278 C CA   . ALA   B 1 154 ? 45.286 -27.922 -9.555  1.00 13.74 ?  154 ALA   B CA   1 
ATOM   6279 C C    . ALA   B 1 154 ? 45.352 -29.002 -8.482  1.00 14.11 ?  154 ALA   B C    1 
ATOM   6280 O O    . ALA   B 1 154 ? 45.276 -28.702 -7.284  1.00 15.58 ?  154 ALA   B O    1 
ATOM   6281 C CB   . ALA   B 1 154 ? 46.508 -27.012 -9.489  1.00 14.86 ?  154 ALA   B CB   1 
ATOM   6282 H H    . ALA   B 1 154 ? 44.077 -26.628 -8.685  1.00 15.10 ?  154 ALA   B H    1 
ATOM   6283 H HA   . ALA   B 1 154 ? 45.267 -28.349 -10.419 1.00 16.49 ?  154 ALA   B HA   1 
ATOM   6284 H HB1  . ALA   B 1 154 ? 47.307 -27.545 -9.614  1.00 17.83 ?  154 ALA   B HB1  1 
ATOM   6285 H HB2  . ALA   B 1 154 ? 46.444 -26.342 -10.190 1.00 17.83 ?  154 ALA   B HB2  1 
ATOM   6286 H HB3  . ALA   B 1 154 ? 46.536 -26.574 -8.621  1.00 17.83 ?  154 ALA   B HB3  1 
ATOM   6287 N N    . VAL   B 1 155 ? 45.484 -30.250 -8.914  1.00 13.38 ?  155 VAL   B N    1 
ATOM   6288 C CA   . VAL   B 1 155 ? 45.588 -31.399 -8.023  1.00 13.77 ?  155 VAL   B CA   1 
ATOM   6289 C C    . VAL   B 1 155 ? 46.928 -32.069 -8.297  1.00 13.30 ?  155 VAL   B C    1 
ATOM   6290 O O    . VAL   B 1 155 ? 47.165 -32.565 -9.406  1.00 15.22 ?  155 VAL   B O    1 
ATOM   6291 C CB   . VAL   B 1 155 ? 44.423 -32.384 -8.220  1.00 15.00 ?  155 VAL   B CB   1 
ATOM   6292 C CG1  . VAL   B 1 155 ? 44.603 -33.598 -7.324  1.00 15.21 ?  155 VAL   B CG1  1 
ATOM   6293 C CG2  . VAL   B 1 155 ? 43.086 -31.685 -7.944  1.00 15.95 ?  155 VAL   B CG2  1 
ATOM   6294 H H    . VAL   B 1 155 ? 45.530 -30.462 -9.747  1.00 16.06 ?  155 VAL   B H    1 
ATOM   6295 H HA   . VAL   B 1 155 ? 45.578 -31.096 -7.101  1.00 16.52 ?  155 VAL   B HA   1 
ATOM   6296 H HB   . VAL   B 1 155 ? 44.416 -32.682 -9.143  1.00 18.00 ?  155 VAL   B HB   1 
ATOM   6297 H HG11 . VAL   B 1 155 ? 43.772 -34.100 -7.299  1.00 18.25 ?  155 VAL   B HG11 1 
ATOM   6298 H HG12 . VAL   B 1 155 ? 45.311 -34.159 -7.685  1.00 18.25 ?  155 VAL   B HG12 1 
ATOM   6299 H HG13 . VAL   B 1 155 ? 44.837 -33.305 -6.430  1.00 18.25 ?  155 VAL   B HG13 1 
ATOM   6300 H HG21 . VAL   B 1 155 ? 42.367 -32.331 -8.039  1.00 19.14 ?  155 VAL   B HG21 1 
ATOM   6301 H HG22 . VAL   B 1 155 ? 43.094 -31.333 -7.039  1.00 19.14 ?  155 VAL   B HG22 1 
ATOM   6302 H HG23 . VAL   B 1 155 ? 42.966 -30.962 -8.578  1.00 19.14 ?  155 VAL   B HG23 1 
ATOM   6303 N N    . PHE   B 1 156 ? 47.790 -32.109 -7.278  1.00 13.81 ?  156 PHE   B N    1 
ATOM   6304 C CA   . PHE   B 1 156 ? 49.168 -32.565 -7.471  1.00 14.98 ?  156 PHE   B CA   1 
ATOM   6305 C C    . PHE   B 1 156 ? 49.265 -34.064 -7.758  1.00 15.54 ?  156 PHE   B C    1 
ATOM   6306 O O    . PHE   B 1 156 ? 49.997 -34.487 -8.664  1.00 17.93 ?  156 PHE   B O    1 
ATOM   6307 C CB   . PHE   B 1 156 ? 49.994 -32.197 -6.239  1.00 15.46 ?  156 PHE   B CB   1 
ATOM   6308 C CG   . PHE   B 1 156 ? 51.420 -32.655 -6.303  1.00 15.77 ?  156 PHE   B CG   1 
ATOM   6309 C CD1  . PHE   B 1 156 ? 52.293 -32.114 -7.225  1.00 17.70 ?  156 PHE   B CD1  1 
ATOM   6310 C CD2  . PHE   B 1 156 ? 51.884 -33.622 -5.435  1.00 16.02 ?  156 PHE   B CD2  1 
ATOM   6311 C CE1  . PHE   B 1 156 ? 53.615 -32.528 -7.282  1.00 18.51 ?  156 PHE   B CE1  1 
ATOM   6312 C CE2  . PHE   B 1 156 ? 53.202 -34.048 -5.490  1.00 17.58 ?  156 PHE   B CE2  1 
ATOM   6313 C CZ   . PHE   B 1 156 ? 54.063 -33.499 -6.416  1.00 18.47 ?  156 PHE   B CZ   1 
ATOM   6314 H H    . PHE   B 1 156 ? 47.600 -31.885 -6.467  1.00 16.57 ?  156 PHE   B H    1 
ATOM   6315 H HA   . PHE   B 1 156 ? 49.544 -32.093 -8.227  1.00 17.98 ?  156 PHE   B HA   1 
ATOM   6316 H HB2  . PHE   B 1 156 ? 49.999 -31.231 -6.146  1.00 18.55 ?  156 PHE   B HB2  1 
ATOM   6317 H HB3  . PHE   B 1 156 ? 49.590 -32.600 -5.456  1.00 18.55 ?  156 PHE   B HB3  1 
ATOM   6318 H HD1  . PHE   B 1 156 ? 51.992 -31.453 -7.812  1.00 21.24 ?  156 PHE   B HD1  1 
ATOM   6319 H HD2  . PHE   B 1 156 ? 51.300 -33.999 -4.812  1.00 19.23 ?  156 PHE   B HD2  1 
ATOM   6320 H HE1  . PHE   B 1 156 ? 54.194 -32.154 -7.909  1.00 22.21 ?  156 PHE   B HE1  1 
ATOM   6321 H HE2  . PHE   B 1 156 ? 53.502 -34.706 -4.903  1.00 21.10 ?  156 PHE   B HE2  1 
ATOM   6322 H HZ   . PHE   B 1 156 ? 54.947 -33.782 -6.452  1.00 22.16 ?  156 PHE   B HZ   1 
ATOM   6323 N N    . ASP   B 1 157 ? 48.594 -34.884 -6.962  1.00 16.36 ?  157 ASP   B N    1 
ATOM   6324 C CA   . ASP   B 1 157 ? 48.745 -36.331 -7.059  1.00 17.82 ?  157 ASP   B CA   1 
ATOM   6325 C C    . ASP   B 1 157 ? 47.829 -36.878 -8.150  1.00 18.01 ?  157 ASP   B C    1 
ATOM   6326 O O    . ASP   B 1 157 ? 46.601 -36.765 -8.047  1.00 17.28 ?  157 ASP   B O    1 
ATOM   6327 C CB   . ASP   B 1 157 ? 48.385 -36.942 -5.712  1.00 19.52 ?  157 ASP   B CB   1 
ATOM   6328 C CG   . ASP   B 1 157 ? 48.514 -38.452 -5.695  1.00 21.67 ?  157 ASP   B CG   1 
ATOM   6329 O OD1  . ASP   B 1 157 ? 48.858 -39.054 -6.738  1.00 22.06 ?  157 ASP   B OD1  1 
ATOM   6330 O OD2  . ASP   B 1 157 ? 48.275 -39.030 -4.619  1.00 23.94 -1 157 ASP   B OD2  1 
ATOM   6331 H H    . ASP   B 1 157 ? 48.047 -34.628 -6.356  1.00 19.63 ?  157 ASP   B H    1 
ATOM   6332 H HA   . ASP   B 1 157 ? 49.665 -36.559 -7.276  1.00 21.38 ?  157 ASP   B HA   1 
ATOM   6333 H HB2  . ASP   B 1 157 ? 48.965 -36.565 -5.034  1.00 23.42 ?  157 ASP   B HB2  1 
ATOM   6334 H HB3  . ASP   B 1 157 ? 47.460 -36.724 -5.511  1.00 23.42 ?  157 ASP   B HB3  1 
ATOM   6335 N N    . LYS   B 1 158 ? 48.423 -37.487 -9.184  1.00 19.15 ?  158 LYS   B N    1 
ATOM   6336 C CA   . LYS   B 1 158 ? 47.646 -38.106 -10.262 1.00 20.22 ?  158 LYS   B CA   1 
ATOM   6337 C C    . LYS   B 1 158 ? 46.590 -39.075 -9.728  1.00 20.05 ?  158 LYS   B C    1 
ATOM   6338 O O    . LYS   B 1 158 ? 45.484 -39.166 -10.276 1.00 20.15 ?  158 LYS   B O    1 
ATOM   6339 C CB   . LYS   B 1 158 ? 48.592 -38.825 -11.233 1.00 22.25 ?  158 LYS   B CB   1 
ATOM   6340 C CG   . LYS   B 1 158 ? 47.911 -39.729 -12.254 1.00 24.36 ?  158 LYS   B CG   1 
ATOM   6341 C CD   . LYS   B 1 158 ? 47.057 -38.950 -13.230 1.00 26.51 ?  158 LYS   B CD   1 
ATOM   6342 C CE   . LYS   B 1 158 ? 46.461 -39.869 -14.282 1.00 28.24 ?  158 LYS   B CE   1 
ATOM   6343 N NZ   . LYS   B 1 158 ? 45.377 -39.204 -15.057 1.00 28.25 ?  158 LYS   B NZ   1 
ATOM   6344 H H    . LYS   B 1 158 ? 49.279 -37.554 -9.287  1.00 22.98 ?  158 LYS   B H    1 
ATOM   6345 H HA   . LYS   B 1 158 ? 47.193 -37.408 -10.763 1.00 24.26 ?  158 LYS   B HA   1 
ATOM   6346 H HB2  . LYS   B 1 158 ? 49.095 -38.158 -11.734 1.00 26.70 ?  158 LYS   B HB2  1 
ATOM   6347 H HB3  . LYS   B 1 158 ? 49.207 -39.373 -10.724 1.00 26.70 ?  158 LYS   B HB3  1 
ATOM   6348 H HG2  . LYS   B 1 158 ? 48.592 -40.195 -12.765 1.00 29.23 ?  158 LYS   B HG2  1 
ATOM   6349 H HG3  . LYS   B 1 158 ? 47.347 -40.379 -11.803 1.00 29.23 ?  158 LYS   B HG3  1 
ATOM   6350 H HD2  . LYS   B 1 158 ? 46.331 -38.518 -12.754 1.00 31.81 ?  158 LYS   B HD2  1 
ATOM   6351 H HD3  . LYS   B 1 158 ? 47.606 -38.288 -13.681 1.00 31.81 ?  158 LYS   B HD3  1 
ATOM   6352 H HE2  . LYS   B 1 158 ? 47.154 -40.137 -14.903 1.00 33.88 ?  158 LYS   B HE2  1 
ATOM   6353 H HE3  . LYS   B 1 158 ? 46.084 -40.651 -13.847 1.00 33.88 ?  158 LYS   B HE3  1 
ATOM   6354 H HZ1  . LYS   B 1 158 ? 45.046 -39.764 -15.663 1.00 33.90 ?  158 LYS   B HZ1  1 
ATOM   6355 H HZ2  . LYS   B 1 158 ? 44.723 -38.949 -14.509 1.00 33.90 ?  158 LYS   B HZ2  1 
ATOM   6356 H HZ3  . LYS   B 1 158 ? 45.700 -38.485 -15.473 1.00 33.90 ?  158 LYS   B HZ3  1 
ATOM   6357 N N    . ASN   B 1 159 ? 46.915 -39.832 -8.680  1.00 19.93 ?  159 ASN   B N    1 
ATOM   6358 C CA   . ASN   B 1 159 ? 45.960 -40.816 -8.177  1.00 20.82 ?  159 ASN   B CA   1 
ATOM   6359 C C    . ASN   B 1 159 ? 44.758 -40.144 -7.507  1.00 19.75 ?  159 ASN   B C    1 
ATOM   6360 O O    . ASN   B 1 159 ? 43.624 -40.629 -7.629  1.00 19.88 ?  159 ASN   B O    1 
ATOM   6361 C CB   . ASN   B 1 159 ? 46.666 -41.799 -7.246  1.00 22.28 ?  159 ASN   B CB   1 
ATOM   6362 C CG   . ASN   B 1 159 ? 47.695 -42.644 -7.971  1.00 24.51 ?  159 ASN   B CG   1 
ATOM   6363 O OD1  . ASN   B 1 159 ? 47.446 -43.128 -9.081  1.00 25.81 ?  159 ASN   B OD1  1 
ATOM   6364 N ND2  . ASN   B 1 159 ? 48.857 -42.830 -7.349  1.00 25.38 ?  159 ASN   B ND2  1 
ATOM   6365 H H    . ASN   B 1 159 ? 47.662 -39.788 -8.259  1.00 23.92 ?  159 ASN   B H    1 
ATOM   6366 H HA   . ASN   B 1 159 ? 45.627 -41.318 -8.936  1.00 24.99 ?  159 ASN   B HA   1 
ATOM   6367 H HB2  . ASN   B 1 159 ? 47.119 -41.307 -6.547  1.00 26.74 ?  159 ASN   B HB2  1 
ATOM   6368 H HB3  . ASN   B 1 159 ? 46.006 -42.396 -6.867  1.00 26.74 ?  159 ASN   B HB3  1 
ATOM   6369 H HD21 . ASN   B 1 159 ? 49.476 -43.303 -7.718  1.00 30.45 ?  159 ASN   B HD21 1 
ATOM   6370 H HD22 . ASN   B 1 159 ? 48.989 -42.488 -6.570  1.00 30.45 ?  159 ASN   B HD22 1 
ATOM   6371 N N    . LEU   B 1 160 ? 44.973 -39.020 -6.811  1.00 18.81 ?  160 LEU   B N    1 
ATOM   6372 C CA   . LEU   B 1 160 ? 43.840 -38.275 -6.271  1.00 17.79 ?  160 LEU   B CA   1 
ATOM   6373 C C    . LEU   B 1 160 ? 43.050 -37.613 -7.389  1.00 16.74 ?  160 LEU   B C    1 
ATOM   6374 O O    . LEU   B 1 160 ? 41.812 -37.614 -7.372  1.00 16.36 ?  160 LEU   B O    1 
ATOM   6375 C CB   . LEU   B 1 160 ? 44.314 -37.239 -5.250  1.00 17.22 ?  160 LEU   B CB   1 
ATOM   6376 C CG   . LEU   B 1 160 ? 43.181 -36.352 -4.709  1.00 17.05 ?  160 LEU   B CG   1 
ATOM   6377 C CD1  . LEU   B 1 160 ? 42.059 -37.195 -4.104  1.00 18.40 ?  160 LEU   B CD1  1 
ATOM   6378 C CD2  . LEU   B 1 160 ? 43.699 -35.349 -3.689  1.00 17.03 ?  160 LEU   B CD2  1 
ATOM   6379 H H    . LEU   B 1 160 ? 45.749 -38.679 -6.646  1.00 22.57 ?  160 LEU   B H    1 
ATOM   6380 H HA   . LEU   B 1 160 ? 43.253 -38.897 -5.820  1.00 21.35 ?  160 LEU   B HA   1 
ATOM   6381 H HB2  . LEU   B 1 160 ? 44.720 -37.703 -4.498  1.00 20.67 ?  160 LEU   B HB2  1 
ATOM   6382 H HB3  . LEU   B 1 160 ? 44.974 -36.660 -5.670  1.00 20.67 ?  160 LEU   B HB3  1 
ATOM   6383 H HG   . LEU   B 1 160 ? 42.804 -35.851 -5.445  1.00 20.46 ?  160 LEU   B HG   1 
ATOM   6384 H HD11 . LEU   B 1 160 ? 41.437 -36.611 -3.650  1.00 22.08 ?  160 LEU   B HD11 1 
ATOM   6385 H HD12 . LEU   B 1 160 ? 41.602 -37.679 -4.813  1.00 22.08 ?  160 LEU   B HD12 1 
ATOM   6386 H HD13 . LEU   B 1 160 ? 42.441 -37.828 -3.471  1.00 22.08 ?  160 LEU   B HD13 1 
ATOM   6387 H HD21 . LEU   B 1 160 ? 42.960 -34.794 -3.394  1.00 20.44 ?  160 LEU   B HD21 1 
ATOM   6388 H HD22 . LEU   B 1 160 ? 44.076 -35.828 -2.936  1.00 20.44 ?  160 LEU   B HD22 1 
ATOM   6389 H HD23 . LEU   B 1 160 ? 44.380 -34.799 -4.107  1.00 20.44 ?  160 LEU   B HD23 1 
ATOM   6390 N N    . TYR   B 1 161 ? 43.749 -37.044 -8.372  1.00 16.85 ?  161 TYR   B N    1 
ATOM   6391 C CA   . TYR   B 1 161 ? 43.077 -36.467 -9.530  1.00 16.91 ?  161 TYR   B CA   1 
ATOM   6392 C C    . TYR   B 1 161 ? 42.132 -37.481 -10.161 1.00 16.87 ?  161 TYR   B C    1 
ATOM   6393 O O    . TYR   B 1 161 ? 40.962 -37.183 -10.422 1.00 16.55 ?  161 TYR   B O    1 
ATOM   6394 C CB   . TYR   B 1 161 ? 44.122 -35.990 -10.545 1.00 17.75 ?  161 TYR   B CB   1 
ATOM   6395 C CG   . TYR   B 1 161 ? 43.546 -35.521 -11.859 1.00 18.09 ?  161 TYR   B CG   1 
ATOM   6396 C CD1  . TYR   B 1 161 ? 43.144 -34.200 -12.025 1.00 18.06 ?  161 TYR   B CD1  1 
ATOM   6397 C CD2  . TYR   B 1 161 ? 43.384 -36.397 -12.928 1.00 19.05 ?  161 TYR   B CD2  1 
ATOM   6398 C CE1  . TYR   B 1 161 ? 42.615 -33.765 -13.210 1.00 19.25 ?  161 TYR   B CE1  1 
ATOM   6399 C CE2  . TYR   B 1 161 ? 42.846 -35.966 -14.120 1.00 19.82 ?  161 TYR   B CE2  1 
ATOM   6400 C CZ   . TYR   B 1 161 ? 42.464 -34.646 -14.255 1.00 19.74 ?  161 TYR   B CZ   1 
ATOM   6401 O OH   . TYR   B 1 161 ? 41.923 -34.204 -15.436 1.00 21.57 ?  161 TYR   B OH   1 
ATOM   6402 H H    . TYR   B 1 161 ? 44.607 -36.984 -8.395  1.00 20.22 ?  161 TYR   B H    1 
ATOM   6403 H HA   . TYR   B 1 161 ? 42.556 -35.702 -9.251  1.00 20.29 ?  161 TYR   B HA   1 
ATOM   6404 H HB2  . TYR   B 1 161 ? 44.614 -35.246 -10.160 1.00 21.30 ?  161 TYR   B HB2  1 
ATOM   6405 H HB3  . TYR   B 1 161 ? 44.730 -36.718 -10.738 1.00 21.30 ?  161 TYR   B HB3  1 
ATOM   6406 H HD1  . TYR   B 1 161 ? 43.245 -33.593 -11.324 1.00 21.68 ?  161 TYR   B HD1  1 
ATOM   6407 H HD2  . TYR   B 1 161 ? 43.638 -37.285 -12.839 1.00 22.86 ?  161 TYR   B HD2  1 
ATOM   6408 H HE1  . TYR   B 1 161 ? 42.357 -32.872 -13.304 1.00 23.11 ?  161 TYR   B HE1  1 
ATOM   6409 H HE2  . TYR   B 1 161 ? 42.743 -36.557 -14.830 1.00 23.78 ?  161 TYR   B HE2  1 
ATOM   6410 H HH   . TYR   B 1 161 ? 41.890 -34.839 -15.990 1.00 25.88 ?  161 TYR   B HH   1 
ATOM   6411 N N    . ASP   B 1 162 ? 42.621 -38.704 -10.387 1.00 17.17 ?  162 ASP   B N    1 
ATOM   6412 C CA   . ASP   B 1 162 ? 41.796 -39.738 -11.005 1.00 17.89 ?  162 ASP   B CA   1 
ATOM   6413 C C    . ASP   B 1 162 ? 40.592 -40.084 -10.139 1.00 17.49 ?  162 ASP   B C    1 
ATOM   6414 O O    . ASP   B 1 162 ? 39.490 -40.297 -10.657 1.00 17.71 ?  162 ASP   B O    1 
ATOM   6415 C CB   . ASP   B 1 162 ? 42.625 -41.001 -11.268 1.00 19.53 ?  162 ASP   B CB   1 
ATOM   6416 C CG   . ASP   B 1 162 ? 43.633 -40.827 -12.390 1.00 21.14 ?  162 ASP   B CG   1 
ATOM   6417 O OD1  . ASP   B 1 162 ? 43.498 -39.880 -13.191 1.00 21.21 ?  162 ASP   B OD1  1 
ATOM   6418 O OD2  . ASP   B 1 162 ? 44.547 -41.674 -12.488 1.00 23.09 -1 162 ASP   B OD2  1 
ATOM   6419 H H    . ASP   B 1 162 ? 43.423 -38.954 -10.198 1.00 20.61 ?  162 ASP   B H    1 
ATOM   6420 H HA   . ASP   B 1 162 ? 41.467 -39.414 -11.855 1.00 21.47 ?  162 ASP   B HA   1 
ATOM   6421 H HB2  . ASP   B 1 162 ? 43.117 -41.231 -10.466 1.00 23.44 ?  162 ASP   B HB2  1 
ATOM   6422 H HB3  . ASP   B 1 162 ? 42.028 -41.725 -11.513 1.00 23.44 ?  162 ASP   B HB3  1 
ATOM   6423 N N    A LYS   B 1 163 ? 40.783 -40.164 -8.820  0.76 16.60 ?  163 LYS   B N    1 
ATOM   6424 N N    B LYS   B 1 163 ? 40.778 -40.144 -8.818  0.24 18.01 ?  163 LYS   B N    1 
ATOM   6425 C CA   A LYS   B 1 163 ? 39.657 -40.442 -7.935  0.76 16.94 ?  163 LYS   B CA   1 
ATOM   6426 C CA   B LYS   B 1 163 ? 39.658 -40.441 -7.930  0.24 18.59 ?  163 LYS   B CA   1 
ATOM   6427 C C    A LYS   B 1 163 ? 38.613 -39.336 -8.009  0.76 16.07 ?  163 LYS   B C    1 
ATOM   6428 C C    B LYS   B 1 163 ? 38.615 -39.329 -7.964  0.24 16.91 ?  163 LYS   B C    1 
ATOM   6429 O O    A LYS   B 1 163 ? 37.402 -39.608 -8.032  0.76 16.79 ?  163 LYS   B O    1 
ATOM   6430 O O    B LYS   B 1 163 ? 37.408 -39.597 -7.914  0.24 16.99 ?  163 LYS   B O    1 
ATOM   6431 C CB   A LYS   B 1 163 ? 40.141 -40.612 -6.497  0.76 19.36 ?  163 LYS   B CB   1 
ATOM   6432 C CB   B LYS   B 1 163 ? 40.164 -40.655 -6.505  0.24 21.12 ?  163 LYS   B CB   1 
ATOM   6433 C CG   A LYS   B 1 163 ? 39.052 -41.115 -5.570  0.76 23.95 ?  163 LYS   B CG   1 
ATOM   6434 C CG   B LYS   B 1 163 ? 39.091 -41.136 -5.548  0.24 24.10 ?  163 LYS   B CG   1 
ATOM   6435 C CD   A LYS   B 1 163 ? 39.492 -41.192 -4.120  0.76 27.71 ?  163 LYS   B CD   1 
ATOM   6436 C CD   B LYS   B 1 163 ? 39.638 -41.395 -4.157  0.24 26.79 ?  163 LYS   B CD   1 
ATOM   6437 C CE   A LYS   B 1 163 ? 38.421 -41.884 -3.284  0.76 30.85 ?  163 LYS   B CE   1 
ATOM   6438 C CE   B LYS   B 1 163 ? 38.605 -42.117 -3.309  0.24 28.08 ?  163 LYS   B CE   1 
ATOM   6439 N NZ   A LYS   B 1 163 ? 38.502 -41.531 -1.840  0.76 33.34 ?  163 LYS   B NZ   1 
ATOM   6440 N NZ   B LYS   B 1 163 ? 38.644 -41.687 -1.886  0.24 29.60 ?  163 LYS   B NZ   1 
ATOM   6441 H H    A LYS   B 1 163 ? 41.539 -40.058 -8.423  0.76 19.92 ?  163 LYS   B H    1 
ATOM   6442 H H    B LYS   B 1 163 ? 41.532 -40.022 -8.420  0.24 21.61 ?  163 LYS   B H    1 
ATOM   6443 H HA   A LYS   B 1 163 ? 39.237 -41.268 -8.210  0.76 20.33 ?  163 LYS   B HA   1 
ATOM   6444 H HA   B LYS   B 1 163 ? 39.230 -41.259 -8.223  0.24 22.31 ?  163 LYS   B HA   1 
ATOM   6445 H HB2  A LYS   B 1 163 ? 40.868 -41.257 -6.482  0.76 23.23 ?  163 LYS   B HB2  1 
ATOM   6446 H HB2  B LYS   B 1 163 ? 40.869 -41.322 -6.519  0.24 25.34 ?  163 LYS   B HB2  1 
ATOM   6447 H HB3  A LYS   B 1 163 ? 40.450 -39.758 -6.160  0.76 23.23 ?  163 LYS   B HB3  1 
ATOM   6448 H HB3  B LYS   B 1 163 ? 40.511 -39.817 -6.164  0.24 25.34 ?  163 LYS   B HB3  1 
ATOM   6449 H HG2  A LYS   B 1 163 ? 38.292 -40.517 -5.619  0.76 28.74 ?  163 LYS   B HG2  1 
ATOM   6450 H HG2  B LYS   B 1 163 ? 38.400 -40.459 -5.477  0.24 28.92 ?  163 LYS   B HG2  1 
ATOM   6451 H HG3  A LYS   B 1 163 ? 38.788 -42.008 -5.850  0.76 28.74 ?  163 LYS   B HG3  1 
ATOM   6452 H HG3  B LYS   B 1 163 ? 38.714 -41.965 -5.883  0.24 28.92 ?  163 LYS   B HG3  1 
ATOM   6453 H HD2  A LYS   B 1 163 ? 40.312 -41.708 -4.056  0.76 33.25 ?  163 LYS   B HD2  1 
ATOM   6454 H HD2  B LYS   B 1 163 ? 40.430 -41.952 -4.219  0.24 32.15 ?  163 LYS   B HD2  1 
ATOM   6455 H HD3  A LYS   B 1 163 ? 39.624 -40.297 -3.773  0.76 33.25 ?  163 LYS   B HD3  1 
ATOM   6456 H HD3  B LYS   B 1 163 ? 39.851 -40.550 -3.730  0.24 32.15 ?  163 LYS   B HD3  1 
ATOM   6457 H HE2  A LYS   B 1 163 ? 37.543 -41.634 -3.612  0.76 37.02 ?  163 LYS   B HE2  1 
ATOM   6458 H HE2  B LYS   B 1 163 ? 37.720 -41.929 -3.659  0.24 33.70 ?  163 LYS   B HE2  1 
ATOM   6459 H HE3  A LYS   B 1 163 ? 38.536 -42.843 -3.361  0.76 37.02 ?  163 LYS   B HE3  1 
ATOM   6460 H HE3  B LYS   B 1 163 ? 38.779 -43.072 -3.341  0.24 33.70 ?  163 LYS   B HE3  1 
ATOM   6461 H HZ1  A LYS   B 1 163 ? 37.860 -41.952 -1.388  0.76 40.01 ?  163 LYS   B HZ1  1 
ATOM   6462 H HZ1  B LYS   B 1 163 ? 38.027 -42.128 -1.419  0.24 35.52 ?  163 LYS   B HZ1  1 
ATOM   6463 H HZ2  A LYS   B 1 163 ? 39.293 -41.772 -1.513  0.76 40.01 ?  163 LYS   B HZ2  1 
ATOM   6464 H HZ2  B LYS   B 1 163 ? 39.445 -41.855 -1.540  0.24 35.52 ?  163 LYS   B HZ2  1 
ATOM   6465 H HZ3  A LYS   B 1 163 ? 38.400 -40.653 -1.735  0.76 40.01 ?  163 LYS   B HZ3  1 
ATOM   6466 H HZ3  B LYS   B 1 163 ? 38.480 -40.814 -1.829  0.24 35.52 ?  163 LYS   B HZ3  1 
ATOM   6467 N N    . LEU   B 1 164 ? 39.066 -38.076 -8.042  1.00 15.18 ?  164 LEU   B N    1 
ATOM   6468 C CA   . LEU   B 1 164 ? 38.150 -36.941 -8.092  1.00 15.02 ?  164 LEU   B CA   1 
ATOM   6469 C C    . LEU   B 1 164 ? 37.370 -36.920 -9.401  1.00 15.18 ?  164 LEU   B C    1 
ATOM   6470 O O    . LEU   B 1 164 ? 36.147 -36.727 -9.404  1.00 16.13 ?  164 LEU   B O    1 
ATOM   6471 C CB   . LEU   B 1 164 ? 38.949 -35.644 -7.927  1.00 14.23 ?  164 LEU   B CB   1 
ATOM   6472 C CG   . LEU   B 1 164 ? 39.476 -35.365 -6.526  1.00 15.43 ?  164 LEU   B CG   1 
ATOM   6473 C CD1  . LEU   B 1 164 ? 40.572 -34.307 -6.575  1.00 15.44 ?  164 LEU   B CD1  1 
ATOM   6474 C CD2  . LEU   B 1 164 ? 38.362 -34.927 -5.596  1.00 16.92 ?  164 LEU   B CD2  1 
ATOM   6475 H H    A LEU   B 1 164 ? 39.903 -37.856 -8.037  0.76 18.21 ?  164 LEU   B H    1 
ATOM   6476 H H    B LEU   B 1 164 ? 39.903 -37.857 -8.070  0.24 18.21 ?  164 LEU   B H    1 
ATOM   6477 H HA   . LEU   B 1 164 ? 37.522 -37.005 -7.363  1.00 18.02 ?  164 LEU   B HA   1 
ATOM   6478 H HB2  . LEU   B 1 164 ? 39.717 -35.675 -8.524  1.00 17.08 ?  164 LEU   B HB2  1 
ATOM   6479 H HB3  . LEU   B 1 164 ? 38.382 -34.899 -8.177  1.00 17.08 ?  164 LEU   B HB3  1 
ATOM   6480 H HG   . LEU   B 1 164 ? 39.867 -36.175 -6.169  1.00 18.51 ?  164 LEU   B HG   1 
ATOM   6481 H HD11 . LEU   B 1 164 ? 40.894 -34.135 -5.672  1.00 18.52 ?  164 LEU   B HD11 1 
ATOM   6482 H HD12 . LEU   B 1 164 ? 41.309 -34.630 -7.123  1.00 18.52 ?  164 LEU   B HD12 1 
ATOM   6483 H HD13 . LEU   B 1 164 ? 40.217 -33.488 -6.956  1.00 18.52 ?  164 LEU   B HD13 1 
ATOM   6484 H HD21 . LEU   B 1 164 ? 38.735 -34.710 -4.728  1.00 20.31 ?  164 LEU   B HD21 1 
ATOM   6485 H HD22 . LEU   B 1 164 ? 37.921 -34.149 -5.971  1.00 20.31 ?  164 LEU   B HD22 1 
ATOM   6486 H HD23 . LEU   B 1 164 ? 37.723 -35.655 -5.507  1.00 20.31 ?  164 LEU   B HD23 1 
ATOM   6487 N N    . VAL   B 1 165 ? 38.062 -37.097 -10.527 1.00 16.40 ?  165 VAL   B N    1 
ATOM   6488 C CA   . VAL   B 1 165 ? 37.403 -37.028 -11.827 1.00 17.55 ?  165 VAL   B CA   1 
ATOM   6489 C C    . VAL   B 1 165 ? 36.480 -38.222 -12.016 1.00 19.27 ?  165 VAL   B C    1 
ATOM   6490 O O    . VAL   B 1 165 ? 35.325 -38.081 -12.435 1.00 20.53 ?  165 VAL   B O    1 
ATOM   6491 C CB   . VAL   B 1 165 ? 38.446 -36.936 -12.957 1.00 18.80 ?  165 VAL   B CB   1 
ATOM   6492 C CG1  . VAL   B 1 165 ? 37.778 -37.041 -14.309 1.00 20.31 ?  165 VAL   B CG1  1 
ATOM   6493 C CG2  . VAL   B 1 165 ? 39.230 -35.639 -12.851 1.00 18.62 ?  165 VAL   B CG2  1 
ATOM   6494 H H    . VAL   B 1 165 ? 38.913 -37.251 -10.564 1.00 19.69 ?  165 VAL   B H    1 
ATOM   6495 H HA   . VAL   B 1 165 ? 36.864 -36.227 -11.862 1.00 21.06 ?  165 VAL   B HA   1 
ATOM   6496 H HB   . VAL   B 1 165 ? 39.079 -37.666 -12.871 1.00 22.56 ?  165 VAL   B HB   1 
ATOM   6497 H HG11 . VAL   B 1 165 ? 38.393 -36.736 -14.991 1.00 24.37 ?  165 VAL   B HG11 1 
ATOM   6498 H HG12 . VAL   B 1 165 ? 37.546 -37.971 -14.469 1.00 24.37 ?  165 VAL   B HG12 1 
ATOM   6499 H HG13 . VAL   B 1 165 ? 36.979 -36.495 -14.309 1.00 24.37 ?  165 VAL   B HG13 1 
ATOM   6500 H HG21 . VAL   B 1 165 ? 39.867 -35.590 -13.584 1.00 22.35 ?  165 VAL   B HG21 1 
ATOM   6501 H HG22 . VAL   B 1 165 ? 38.615 -34.889 -12.903 1.00 22.35 ?  165 VAL   B HG22 1 
ATOM   6502 H HG23 . VAL   B 1 165 ? 39.704 -35.617 -12.004 1.00 22.35 ?  165 VAL   B HG23 1 
ATOM   6503 N N    . SER   B 1 166 ? 36.986 -39.422 -11.712 1.00 20.20 ?  166 SER   B N    1 
ATOM   6504 C CA   . SER   B 1 166 ? 36.230 -40.633 -11.994 1.00 21.79 ?  166 SER   B CA   1 
ATOM   6505 C C    . SER   B 1 166 ? 34.973 -40.719 -11.143 1.00 22.10 ?  166 SER   B C    1 
ATOM   6506 O O    . SER   B 1 166 ? 34.002 -41.343 -11.564 1.00 23.51 ?  166 SER   B O    1 
ATOM   6507 C CB   . SER   B 1 166 ? 37.098 -41.886 -11.826 1.00 22.61 ?  166 SER   B CB   1 
ATOM   6508 O OG   . SER   B 1 166 ? 37.459 -42.099 -10.471 1.00 22.69 ?  166 SER   B OG   1 
ATOM   6509 H H    . SER   B 1 166 ? 37.763 -39.556 -11.354 1.00 24.24 ?  166 SER   B H    1 
ATOM   6510 H HA   . SER   B 1 166 ? 35.952 -40.605 -12.921 1.00 26.14 ?  166 SER   B HA   1 
ATOM   6511 H HB2  . SER   B 1 166 ? 36.601 -42.656 -12.142 1.00 27.13 ?  166 SER   B HB2  1 
ATOM   6512 H HB3  . SER   B 1 166 ? 37.906 -41.781 -12.359 1.00 27.13 ?  166 SER   B HB3  1 
ATOM   6513 H HG   . SER   B 1 166 ? 37.913 -41.451 -10.192 1.00 27.23 ?  166 SER   B HG   1 
ATOM   6514 N N    . SER   B 1 167 ? 34.954 -40.102 -9.964  1.00 20.93 ?  167 SER   B N    1 
ATOM   6515 C CA   . SER   B 1 167 ? 33.800 -40.159 -9.075  1.00 20.56 ?  167 SER   B CA   1 
ATOM   6516 C C    . SER   B 1 167 ? 32.888 -38.935 -9.170  1.00 20.24 ?  167 SER   B C    1 
ATOM   6517 O O    . SER   B 1 167 ? 31.812 -38.936 -8.560  1.00 20.61 ?  167 SER   B O    1 
ATOM   6518 C CB   . SER   B 1 167 ? 34.251 -40.343 -7.621  1.00 20.38 ?  167 SER   B CB   1 
ATOM   6519 O OG   . SER   B 1 167 ? 34.928 -39.183 -7.155  1.00 19.62 ?  167 SER   B OG   1 
ATOM   6520 H H    . SER   B 1 167 ? 35.610 -39.653 -9.654  1.00 25.11 ?  167 SER   B H    1 
ATOM   6521 H HA   . SER   B 1 167 ? 33.269 -40.936 -9.313  1.00 24.67 ?  167 SER   B HA   1 
ATOM   6522 H HB2  . SER   B 1 167 ? 33.469 -40.501 -7.067  1.00 24.45 ?  167 SER   B HB2  1 
ATOM   6523 H HB3  . SER   B 1 167 ? 34.843 -41.118 -7.572  1.00 24.45 ?  167 SER   B HB3  1 
ATOM   6524 H HG   . SER   B 1 167 ? 35.621 -39.062 -7.620  1.00 23.54 ?  167 SER   B HG   1 
ATOM   6525 N N    . PHE   B 1 168 ? 33.269 -37.903 -9.924  1.00 19.58 ?  168 PHE   B N    1 
ATOM   6526 C CA   . PHE   B 1 168 ? 32.436 -36.704 -9.997  1.00 19.03 ?  168 PHE   B CA   1 
ATOM   6527 C C    . PHE   B 1 168 ? 31.121 -36.974 -10.724 1.00 16.54 ?  168 PHE   B C    1 
ATOM   6528 O O    . PHE   B 1 168 ? 30.083 -36.374 -10.387 1.00 17.31 ?  168 PHE   B O    1 
ATOM   6529 C CB   . PHE   B 1 168 ? 33.207 -35.571 -10.677 1.00 19.94 ?  168 PHE   B CB   1 
ATOM   6530 C CG   . PHE   B 1 168 ? 32.410 -34.319 -10.819 1.00 19.92 ?  168 PHE   B CG   1 
ATOM   6531 C CD1  . PHE   B 1 168 ? 32.074 -33.575 -9.699  1.00 21.54 ?  168 PHE   B CD1  1 
ATOM   6532 C CD2  . PHE   B 1 168 ? 31.960 -33.903 -12.056 1.00 19.41 ?  168 PHE   B CD2  1 
ATOM   6533 C CE1  . PHE   B 1 168 ? 31.315 -32.424 -9.812  1.00 22.02 ?  168 PHE   B CE1  1 
ATOM   6534 C CE2  . PHE   B 1 168 ? 31.213 -32.737 -12.183 1.00 20.51 ?  168 PHE   B CE2  1 
ATOM   6535 C CZ   . PHE   B 1 168 ? 30.883 -31.999 -11.056 1.00 20.98 ?  168 PHE   B CZ   1 
ATOM   6536 H H    . PHE   B 1 168 ? 33.987 -37.873 -10.395 1.00 23.50 ?  168 PHE   B H    1 
ATOM   6537 H HA   . PHE   B 1 168 ? 32.219 -36.420 -9.100  1.00 22.83 ?  168 PHE   B HA   1 
ATOM   6538 H HB2  . PHE   B 1 168 ? 33.993 -35.363 -10.146 1.00 23.93 ?  168 PHE   B HB2  1 
ATOM   6539 H HB3  . PHE   B 1 168 ? 33.475 -35.854 -11.565 1.00 23.93 ?  168 PHE   B HB3  1 
ATOM   6540 H HD1  . PHE   B 1 168 ? 32.362 -33.857 -8.861  1.00 25.85 ?  168 PHE   B HD1  1 
ATOM   6541 H HD2  . PHE   B 1 168 ? 32.182 -34.389 -12.815 1.00 23.29 ?  168 PHE   B HD2  1 
ATOM   6542 H HE1  . PHE   B 1 168 ? 31.100 -31.930 -9.054  1.00 26.42 ?  168 PHE   B HE1  1 
ATOM   6543 H HE2  . PHE   B 1 168 ? 30.920 -32.461 -13.024 1.00 24.61 ?  168 PHE   B HE2  1 
ATOM   6544 H HZ   . PHE   B 1 168 ? 30.374 -31.223 -11.139 1.00 25.18 ?  168 PHE   B HZ   1 
ATOM   6545 N N    . LEU   B 1 169 ? 31.152 -37.849 -11.725 1.00 16.93 ?  169 LEU   B N    1 
ATOM   6546 C CA   . LEU   B 1 169 ? 29.969 -38.158 -12.521 1.00 19.51 ?  169 LEU   B CA   1 
ATOM   6547 C C    . LEU   B 1 169 ? 29.950 -39.596 -13.016 1.00 22.58 ?  169 LEU   B C    1 
ATOM   6548 O O    . LEU   B 1 169 ? 29.040 -40.003 -13.739 1.00 25.29 ?  169 LEU   B O    1 
ATOM   6549 C CB   . LEU   B 1 169 ? 29.880 -37.218 -13.724 1.00 21.41 ?  169 LEU   B CB   1 
ATOM   6550 C CG   . LEU   B 1 169 ? 28.614 -36.363 -13.808 1.00 24.86 ?  169 LEU   B CG   1 
ATOM   6551 C CD1  . LEU   B 1 169 ? 28.565 -35.646 -15.144 1.00 26.10 ?  169 LEU   B CD1  1 
ATOM   6552 C CD2  . LEU   B 1 169 ? 27.356 -37.189 -13.591 1.00 25.10 ?  169 LEU   B CD2  1 
ATOM   6553 O OXT  . LEU   B 1 169 ? 30.846 -40.375 -12.717 1.00 23.32 -1 169 LEU   B OXT  1 
ATOM   6554 H H    . LEU   B 1 169 ? 31.859 -38.276 -11.976 1.00 20.31 ?  169 LEU   B H    1 
ATOM   6555 H HA   . LEU   B 1 169 ? 29.189 -38.020 -11.971 1.00 23.42 ?  169 LEU   B HA   1 
ATOM   6556 H HB2  . LEU   B 1 169 ? 30.636 -36.612 -13.699 1.00 25.70 ?  169 LEU   B HB2  1 
ATOM   6557 H HB3  . LEU   B 1 169 ? 29.919 -37.748 -14.537 1.00 25.70 ?  169 LEU   B HB3  1 
ATOM   6558 H HG   . LEU   B 1 169 ? 28.648 -35.685 -13.114 1.00 29.84 ?  169 LEU   B HG   1 
ATOM   6559 H HD11 . LEU   B 1 169 ? 27.771 -35.091 -15.173 1.00 31.31 ?  169 LEU   B HD11 1 
ATOM   6560 H HD12 . LEU   B 1 169 ? 29.358 -35.096 -15.234 1.00 31.31 ?  169 LEU   B HD12 1 
ATOM   6561 H HD13 . LEU   B 1 169 ? 28.536 -36.307 -15.852 1.00 31.31 ?  169 LEU   B HD13 1 
ATOM   6562 H HD21 . LEU   B 1 169 ? 26.600 -36.730 -13.985 1.00 30.11 ?  169 LEU   B HD21 1 
ATOM   6563 H HD22 . LEU   B 1 169 ? 27.473 -38.057 -14.011 1.00 30.11 ?  169 LEU   B HD22 1 
ATOM   6564 H HD23 . LEU   B 1 169 ? 27.217 -37.301 -12.638 1.00 30.11 ?  169 LEU   B HD23 1 
HETATM 6565 C C1   T TFA   C 2 .   ? 12.134 -1.336  1.469   0.30 12.83 ?  201 TFA   A C1   1 
HETATM 6566 C C2   T TFA   C 2 .   ? 12.753 -1.755  0.112   0.30 14.91 ?  201 TFA   A C2   1 
HETATM 6567 O O    T TFA   C 2 .   ? 12.872 -1.577  2.435   0.30 11.34 ?  201 TFA   A O    1 
HETATM 6568 F F1   T TFA   C 2 .   ? 12.856 -3.093  0.058   0.30 16.15 ?  201 TFA   A F1   1 
HETATM 6569 F F2   T TFA   C 2 .   ? 12.025 -1.377  -0.951  0.30 15.24 ?  201 TFA   A F2   1 
HETATM 6570 F F3   T TFA   C 2 .   ? 13.974 -1.255  -0.093  0.30 16.46 ?  201 TFA   A F3   1 
HETATM 6571 O OXT  T TFA   C 2 .   ? 11.011 -0.826  1.406   0.30 13.22 ?  201 TFA   A OXT  1 
HETATM 6572 N N2   B A1A65 D 3 .   ? 14.400 0.045   4.348   0.24 14.36 ?  202 A1A65 A N2   1 
HETATM 6573 C C3   B A1A65 D 3 .   ? 13.630 -2.274  0.596   0.24 18.87 ?  202 A1A65 A C3   1 
HETATM 6574 C C6   B A1A65 D 3 .   ? 12.054 1.911   1.133   0.24 18.09 ?  202 A1A65 A C6   1 
HETATM 6575 C C9   B A1A65 D 3 .   ? 14.796 0.049   5.658   0.24 14.28 ?  202 A1A65 A C9   1 
HETATM 6576 C C12  B A1A65 D 3 .   ? 15.210 3.809   4.037   0.24 14.24 ?  202 A1A65 A C12  1 
HETATM 6577 C C1   B A1A65 D 3 .   ? 14.873 -0.302  -0.308  0.24 19.17 ?  202 A1A65 A C1   1 
HETATM 6578 C C10  B A1A65 D 3 .   ? 15.319 2.229   5.663   0.24 13.42 ?  202 A1A65 A C10  1 
HETATM 6579 C C11  B A1A65 D 3 .   ? 14.959 2.412   4.298   0.24 13.98 ?  202 A1A65 A C11  1 
HETATM 6580 C C13  B A1A65 D 3 .   ? 15.698 4.396   5.190   0.24 13.27 ?  202 A1A65 A C13  1 
HETATM 6581 C C2   B A1A65 D 3 .   ? 14.348 -0.973  0.971   0.24 18.78 ?  202 A1A65 A C2   1 
HETATM 6582 C C4   B A1A65 D 3 .   ? 13.357 -0.058  1.754   0.24 17.97 ?  202 A1A65 A C4   1 
HETATM 6583 C C5   B A1A65 D 3 .   ? 12.217 0.449   0.842   0.24 18.23 ?  202 A1A65 A C5   1 
HETATM 6584 C C7   B A1A65 D 3 .   ? 13.386 2.361   1.728   0.24 17.44 ?  202 A1A65 A C7   1 
HETATM 6585 C C8   B A1A65 D 3 .   ? 14.474 1.223   3.647   0.24 14.85 ?  202 A1A65 A C8   1 
HETATM 6586 N N1   B A1A65 D 3 .   ? 14.039 1.162   2.303   0.24 16.62 ?  202 A1A65 A N1   1 
HETATM 6587 N N3   B A1A65 D 3 .   ? 15.255 1.069   6.376   0.24 13.87 ?  202 A1A65 A N3   1 
HETATM 6588 N N4   B A1A65 D 3 .   ? 15.763 3.430   6.198   0.24 13.15 ?  202 A1A65 A N4   1 
HETATM 6589 O O1   B A1A65 D 3 .   ? 15.418 -1.218  1.828   0.24 19.25 ?  202 A1A65 A O1   1 
HETATM 6590 H H6   B A1A65 D 3 .   ? 12.708 -2.113  0.027   0.24 22.64 ?  202 A1A65 A H6   1 
HETATM 6591 H H5   B A1A65 D 3 .   ? 13.352 -2.853  1.485   0.24 22.64 ?  202 A1A65 A H5   1 
HETATM 6592 H H7   B A1A65 D 3 .   ? 14.256 -2.923  -0.020  0.24 22.64 ?  202 A1A65 A H7   1 
HETATM 6593 H H12  B A1A65 D 3 .   ? 11.201 2.079   1.819   0.24 21.71 ?  202 A1A65 A H12  1 
HETATM 6594 H H11  B A1A65 D 3 .   ? 11.763 2.475   0.237   0.24 21.71 ?  202 A1A65 A H11  1 
HETATM 6595 H H15  B A1A65 D 3 .   ? 14.746 -0.872  6.256   0.24 17.13 ?  202 A1A65 A H15  1 
HETATM 6596 H H16  B A1A65 D 3 .   ? 15.058 4.340   3.117   0.24 17.09 ?  202 A1A65 A H16  1 
HETATM 6597 H H3   B A1A65 D 3 .   ? 14.137 -0.272  -1.120  0.24 23.00 ?  202 A1A65 A H3   1 
HETATM 6598 H H4   B A1A65 D 3 .   ? 15.731 -0.791  -0.729  0.24 23.00 ?  202 A1A65 A H4   1 
HETATM 6599 H H2   B A1A65 D 3 .   ? 15.146 0.755   -0.134  0.24 23.00 ?  202 A1A65 A H2   1 
HETATM 6600 H H17  B A1A65 D 3 .   ? 16.011 5.412   5.425   0.24 15.92 ?  202 A1A65 A H17  1 
HETATM 6601 H H1   B A1A65 D 3 .   ? 12.880 -0.680  2.567   0.24 21.57 ?  202 A1A65 A H1   1 
HETATM 6602 H H10  B A1A65 D 3 .   ? 12.385 0.253   -0.231  0.24 21.88 ?  202 A1A65 A H10  1 
HETATM 6603 H H9   B A1A65 D 3 .   ? 11.258 -0.054  0.994   0.24 21.88 ?  202 A1A65 A H9   1 
HETATM 6604 H H14  B A1A65 D 3 .   ? 13.223 3.119   2.507   0.24 20.92 ?  202 A1A65 A H14  1 
HETATM 6605 H H13  B A1A65 D 3 .   ? 14.019 2.845   0.948   0.24 20.92 ?  202 A1A65 A H13  1 
HETATM 6606 H H18  B A1A65 D 3 .   ? 16.085 3.558   7.150   0.24 15.78 ?  202 A1A65 A H18  1 
HETATM 6607 H H8   B A1A65 D 3 .   ? 15.987 -1.856  1.401   0.24 23.10 ?  202 A1A65 A H8   1 
HETATM 6608 O O    . HOH   E 4 .   ? 4.759  3.815   0.649   1.00 25.56 ?  301 HOH   A O    1 
HETATM 6609 O O    . HOH   E 4 .   ? 14.793 -4.737  20.525  1.00 45.18 ?  302 HOH   A O    1 
HETATM 6610 O O    . HOH   E 4 .   ? 17.415 -1.760  0.476   1.00 19.47 ?  303 HOH   A O    1 
HETATM 6611 O O    . HOH   E 4 .   ? 34.418 -1.851  12.481  1.00 40.32 ?  304 HOH   A O    1 
HETATM 6612 O O    . HOH   E 4 .   ? 12.038 0.329   14.773  1.00 35.00 ?  305 HOH   A O    1 
HETATM 6613 O O    . HOH   E 4 .   ? 7.642  -6.334  -6.644  1.00 40.90 ?  306 HOH   A O    1 
HETATM 6614 O O    . HOH   E 4 .   ? 17.134 -18.041 15.053  1.00 27.30 ?  307 HOH   A O    1 
HETATM 6615 O O    . HOH   E 4 .   ? 15.148 -12.239 18.689  1.00 38.16 ?  308 HOH   A O    1 
HETATM 6616 O O    . HOH   E 4 .   ? 28.897 0.464   -9.737  1.00 22.53 ?  309 HOH   A O    1 
HETATM 6617 O O    . HOH   E 4 .   ? 0.761  -4.409  0.127   1.00 33.19 ?  310 HOH   A O    1 
HETATM 6618 O O    B HOH   E 4 .   ? 15.057 -3.329  3.709   0.24 20.38 ?  311 HOH   A O    1 
HETATM 6619 O O    . HOH   E 4 .   ? 28.187 -6.389  19.639  1.00 42.51 ?  312 HOH   A O    1 
HETATM 6620 O O    . HOH   E 4 .   ? 42.483 10.536  5.192   1.00 21.89 ?  313 HOH   A O    1 
HETATM 6621 O O    . HOH   E 4 .   ? 18.683 -2.424  -16.371 1.00 46.99 ?  314 HOH   A O    1 
HETATM 6622 O O    . HOH   E 4 .   ? 14.433 -24.707 11.614  1.00 39.23 ?  315 HOH   A O    1 
HETATM 6623 O O    . HOH   E 4 .   ? 8.852  -12.147 17.086  1.00 44.45 ?  316 HOH   A O    1 
HETATM 6624 O O    . HOH   E 4 .   ? 36.162 -5.047  -0.543  1.00 30.30 ?  317 HOH   A O    1 
HETATM 6625 O O    . HOH   E 4 .   ? 14.724 -13.987 16.699  1.00 24.41 ?  318 HOH   A O    1 
HETATM 6626 O O    . HOH   E 4 .   ? 9.189  -10.135 19.344  1.00 40.33 ?  319 HOH   A O    1 
HETATM 6627 O O    . HOH   E 4 .   ? 14.167 -4.530  -11.888 1.00 31.96 ?  320 HOH   A O    1 
HETATM 6628 O O    . HOH   E 4 .   ? 30.280 -13.315 -8.568  1.00 21.77 ?  321 HOH   A O    1 
HETATM 6629 O O    . HOH   E 4 .   ? 26.832 11.397  1.667   1.00 17.91 ?  322 HOH   A O    1 
HETATM 6630 O O    . HOH   E 4 .   ? 22.740 12.497  1.608   1.00 16.18 ?  323 HOH   A O    1 
HETATM 6631 O O    . HOH   E 4 .   ? 33.988 -0.998  -8.898  1.00 28.22 ?  324 HOH   A O    1 
HETATM 6632 O O    . HOH   E 4 .   ? 15.084 3.904   17.749  1.00 40.16 ?  325 HOH   A O    1 
HETATM 6633 O O    . HOH   E 4 .   ? 37.534 2.776   10.178  1.00 30.65 ?  326 HOH   A O    1 
HETATM 6634 O O    . HOH   E 4 .   ? 7.951  -12.580 -0.854  1.00 21.69 ?  327 HOH   A O    1 
HETATM 6635 O O    . HOH   E 4 .   ? 13.271 -1.450  -6.671  1.00 17.79 ?  328 HOH   A O    1 
HETATM 6636 O O    . HOH   E 4 .   ? 22.400 5.340   18.994  1.00 42.87 ?  329 HOH   A O    1 
HETATM 6637 O O    . HOH   E 4 .   ? 26.501 -19.359 -1.816  1.00 14.79 ?  330 HOH   A O    1 
HETATM 6638 O O    . HOH   E 4 .   ? 19.916 -12.552 -8.916  1.00 26.79 ?  331 HOH   A O    1 
HETATM 6639 O O    . HOH   E 4 .   ? 11.734 -10.901 -10.185 1.00 43.09 ?  332 HOH   A O    1 
HETATM 6640 O O    . HOH   E 4 .   ? -0.423 -2.960  2.992   1.00 41.46 ?  333 HOH   A O    1 
HETATM 6641 O O    . HOH   E 4 .   ? 8.087  -21.504 3.987   1.00 49.87 ?  334 HOH   A O    1 
HETATM 6642 O O    . HOH   E 4 .   ? 20.671 -19.753 -5.099  1.00 29.04 ?  335 HOH   A O    1 
HETATM 6643 O O    . HOH   E 4 .   ? 18.904 -21.992 6.947   1.00 35.95 ?  336 HOH   A O    1 
HETATM 6644 O O    . HOH   E 4 .   ? 31.030 -18.169 7.786   1.00 21.09 ?  337 HOH   A O    1 
HETATM 6645 O O    A HOH   E 4 .   ? 14.290 0.555   6.793   0.76 21.16 ?  338 HOH   A O    1 
HETATM 6646 O O    . HOH   E 4 .   ? -0.640 -8.468  2.138   1.00 44.71 ?  339 HOH   A O    1 
HETATM 6647 O O    . HOH   E 4 .   ? 20.096 4.526   -7.535  1.00 20.88 ?  340 HOH   A O    1 
HETATM 6648 O O    . HOH   E 4 .   ? 27.921 0.837   -7.147  1.00 15.02 ?  341 HOH   A O    1 
HETATM 6649 O O    . HOH   E 4 .   ? 27.354 13.802  2.857   1.00 31.86 ?  342 HOH   A O    1 
HETATM 6650 O O    . HOH   E 4 .   ? 18.688 -19.422 13.524  1.00 36.86 ?  343 HOH   A O    1 
HETATM 6651 O O    A HOH   E 4 .   ? 3.614  -9.485  9.709   0.76 27.03 ?  344 HOH   A O    1 
HETATM 6652 O O    . HOH   E 4 .   ? 15.207 -21.561 14.242  1.00 19.24 ?  345 HOH   A O    1 
HETATM 6653 O O    . HOH   E 4 .   ? 28.354 -0.132  -13.414 1.00 35.88 ?  346 HOH   A O    1 
HETATM 6654 O O    . HOH   E 4 .   ? 44.356 7.137   6.382   1.00 28.28 ?  347 HOH   A O    1 
HETATM 6655 O O    . HOH   E 4 .   ? 38.293 10.120  7.170   1.00 39.36 ?  348 HOH   A O    1 
HETATM 6656 O O    A HOH   E 4 .   ? 14.651 -3.668  3.086   0.76 15.49 ?  349 HOH   A O    1 
HETATM 6657 O O    . HOH   E 4 .   ? 9.876  -21.401 5.713   1.00 20.30 ?  350 HOH   A O    1 
HETATM 6658 O O    . HOH   E 4 .   ? 22.261 -19.318 11.353  1.00 33.82 ?  351 HOH   A O    1 
HETATM 6659 O O    . HOH   E 4 .   ? 38.577 4.965   6.978   1.00 17.01 ?  352 HOH   A O    1 
HETATM 6660 O O    . HOH   E 4 .   ? 21.245 -2.338  -2.257  1.00 16.55 ?  353 HOH   A O    1 
HETATM 6661 O O    . HOH   E 4 .   ? 13.544 -15.229 -7.487  1.00 28.32 ?  354 HOH   A O    1 
HETATM 6662 O O    . HOH   E 4 .   ? 17.170 -17.774 -5.027  1.00 27.81 ?  355 HOH   A O    1 
HETATM 6663 O O    . HOH   E 4 .   ? 31.737 8.186   14.863  1.00 24.81 ?  356 HOH   A O    1 
HETATM 6664 O O    . HOH   E 4 .   ? 42.597 4.283   5.383   1.00 33.26 ?  357 HOH   A O    1 
HETATM 6665 O O    . HOH   E 4 .   ? 24.027 -2.114  -2.086  1.00 11.25 ?  358 HOH   A O    1 
HETATM 6666 O O    . HOH   E 4 .   ? 39.788 -1.016  -5.186  1.00 22.37 ?  359 HOH   A O    1 
HETATM 6667 O O    . HOH   E 4 .   ? 33.659 -7.161  4.274   1.00 17.99 ?  360 HOH   A O    1 
HETATM 6668 O O    . HOH   E 4 .   ? 24.569 1.995   -7.014  1.00 20.71 ?  361 HOH   A O    1 
HETATM 6669 O O    . HOH   E 4 .   ? 14.348 -21.201 -4.283  1.00 30.95 ?  362 HOH   A O    1 
HETATM 6670 O O    . HOH   E 4 .   ? 37.414 11.932  4.958   1.00 33.18 ?  363 HOH   A O    1 
HETATM 6671 O O    . HOH   E 4 .   ? 35.807 -12.684 6.807   1.00 16.66 ?  364 HOH   A O    1 
HETATM 6672 O O    . HOH   E 4 .   ? 21.874 -21.906 8.380   1.00 29.81 ?  365 HOH   A O    1 
HETATM 6673 O O    . HOH   E 4 .   ? 31.096 -13.948 -2.501  1.00 14.39 ?  366 HOH   A O    1 
HETATM 6674 O O    . HOH   E 4 .   ? 30.828 3.084   8.271   1.00 12.83 ?  367 HOH   A O    1 
HETATM 6675 O O    . HOH   E 4 .   ? 43.915 8.436   -3.115  1.00 25.93 ?  368 HOH   A O    1 
HETATM 6676 O O    . HOH   E 4 .   ? 27.491 -10.632 14.042  1.00 18.74 ?  369 HOH   A O    1 
HETATM 6677 O O    . HOH   E 4 .   ? 15.512 11.888  7.920   1.00 35.67 ?  370 HOH   A O    1 
HETATM 6678 O O    A HOH   E 4 .   ? 6.963  -8.185  11.830  0.76 18.90 ?  371 HOH   A O    1 
HETATM 6679 O O    . HOH   E 4 .   ? 25.704 -0.806  -7.354  1.00 16.51 ?  372 HOH   A O    1 
HETATM 6680 O O    . HOH   E 4 .   ? 6.442  -5.537  11.116  1.00 20.67 ?  373 HOH   A O    1 
HETATM 6681 O O    . HOH   E 4 .   ? 37.258 -2.866  9.690   1.00 41.93 ?  374 HOH   A O    1 
HETATM 6682 O O    . HOH   E 4 .   ? 24.393 3.602   -1.787  1.00 16.25 ?  375 HOH   A O    1 
HETATM 6683 O O    . HOH   E 4 .   ? 18.569 9.457   8.997   1.00 22.87 ?  376 HOH   A O    1 
HETATM 6684 O O    . HOH   E 4 .   ? 31.869 -9.345  -6.643  1.00 23.20 ?  377 HOH   A O    1 
HETATM 6685 O O    . HOH   E 4 .   ? 17.014 -19.296 4.899   1.00 15.74 ?  378 HOH   A O    1 
HETATM 6686 O O    . HOH   E 4 .   ? 24.725 -17.532 12.722  1.00 25.09 ?  379 HOH   A O    1 
HETATM 6687 O O    . HOH   E 4 .   ? 16.514 -22.055 0.969   1.00 30.09 ?  380 HOH   A O    1 
HETATM 6688 O O    . HOH   E 4 .   ? 31.771 -7.299  -9.869  1.00 22.06 ?  381 HOH   A O    1 
HETATM 6689 O O    T HOH   E 4 .   ? 15.423 -0.435  2.379   0.30 12.72 ?  382 HOH   A O    1 
HETATM 6690 O O    . HOH   E 4 .   ? 6.724  -3.297  12.846  1.00 30.74 ?  383 HOH   A O    1 
HETATM 6691 O O    . HOH   E 4 .   ? 13.959 -4.972  17.468  1.00 26.56 ?  384 HOH   A O    1 
HETATM 6692 O O    . HOH   E 4 .   ? -1.372 -4.913  7.694   1.00 45.16 ?  385 HOH   A O    1 
HETATM 6693 O O    . HOH   E 4 .   ? 24.253 -7.792  14.445  1.00 18.50 ?  386 HOH   A O    1 
HETATM 6694 O O    . HOH   E 4 .   ? 21.304 3.065   -0.277  1.00 14.19 ?  387 HOH   A O    1 
HETATM 6695 O O    . HOH   E 4 .   ? 21.245 10.252  15.068  1.00 36.43 ?  388 HOH   A O    1 
HETATM 6696 O O    . HOH   E 4 .   ? 14.081 -23.068 7.455   1.00 19.79 ?  389 HOH   A O    1 
HETATM 6697 O O    . HOH   E 4 .   ? 37.556 -2.043  5.769   1.00 27.01 ?  390 HOH   A O    1 
HETATM 6698 O O    . HOH   E 4 .   ? 27.423 -6.049  -13.973 1.00 36.90 ?  391 HOH   A O    1 
HETATM 6699 O O    . HOH   E 4 .   ? 43.387 7.857   2.686   1.00 26.20 ?  392 HOH   A O    1 
HETATM 6700 O O    A HOH   E 4 .   ? 15.816 -0.961  5.262   0.76 20.63 ?  393 HOH   A O    1 
HETATM 6701 O O    . HOH   E 4 .   ? 30.709 1.866   16.691  1.00 23.17 ?  394 HOH   A O    1 
HETATM 6702 O O    . HOH   E 4 .   ? 20.559 -20.029 2.769   1.00 19.41 ?  395 HOH   A O    1 
HETATM 6703 O O    . HOH   E 4 .   ? 24.022 3.923   -4.833  1.00 23.67 ?  396 HOH   A O    1 
HETATM 6704 O O    A HOH   E 4 .   ? 11.083 -0.393  1.925   0.46 22.86 ?  397 HOH   A O    1 
HETATM 6705 O O    . HOH   E 4 .   ? 30.087 -10.111 12.997  1.00 22.85 ?  398 HOH   A O    1 
HETATM 6706 O O    . HOH   E 4 .   ? 22.683 -11.944 21.824  1.00 45.11 ?  399 HOH   A O    1 
HETATM 6707 O O    B HOH   E 4 .   ? 9.319  1.811   -1.123  0.24 29.59 ?  400 HOH   A O    1 
HETATM 6708 O O    . HOH   E 4 .   ? 10.394 -22.179 -1.245  1.00 42.80 ?  401 HOH   A O    1 
HETATM 6709 O O    . HOH   E 4 .   ? 14.513 -0.495  -12.121 1.00 26.51 ?  402 HOH   A O    1 
HETATM 6710 O O    . HOH   E 4 .   ? 30.940 6.238   -12.312 1.00 31.33 ?  403 HOH   A O    1 
HETATM 6711 O O    . HOH   E 4 .   ? 27.378 2.332   18.741  1.00 30.74 ?  404 HOH   A O    1 
HETATM 6712 O O    . HOH   E 4 .   ? 18.887 -0.701  -1.626  1.00 14.86 ?  405 HOH   A O    1 
HETATM 6713 O O    . HOH   E 4 .   ? 28.577 -10.663 -14.030 1.00 44.96 ?  406 HOH   A O    1 
HETATM 6714 O O    . HOH   E 4 .   ? 23.970 -15.699 -9.186  1.00 37.51 ?  407 HOH   A O    1 
HETATM 6715 O O    B HOH   E 4 .   ? 12.118 -1.574  -3.066  0.24 16.79 ?  408 HOH   A O    1 
HETATM 6716 O O    . HOH   E 4 .   ? 23.481 11.368  4.098   1.00 13.25 ?  409 HOH   A O    1 
HETATM 6717 O O    . HOH   E 4 .   ? 21.789 -13.869 -8.184  1.00 41.86 ?  410 HOH   A O    1 
HETATM 6718 O O    . HOH   E 4 .   ? 32.792 -9.277  5.901   1.00 20.93 ?  411 HOH   A O    1 
HETATM 6719 O O    . HOH   E 4 .   ? 15.153 -8.096  -9.730  1.00 24.25 ?  412 HOH   A O    1 
HETATM 6720 O O    . HOH   E 4 .   ? 40.908 -8.248  -6.775  1.00 36.82 ?  413 HOH   A O    1 
HETATM 6721 O O    . HOH   E 4 .   ? 26.944 4.151   -0.649  1.00 13.55 ?  414 HOH   A O    1 
HETATM 6722 O O    . HOH   E 4 .   ? 15.878 2.107   24.767  1.00 48.02 ?  415 HOH   A O    1 
HETATM 6723 O O    . HOH   E 4 .   ? 41.605 1.496   4.945   1.00 38.54 ?  416 HOH   A O    1 
HETATM 6724 O O    . HOH   E 4 .   ? 38.117 -1.331  -1.963  1.00 19.77 ?  417 HOH   A O    1 
HETATM 6725 O O    . HOH   E 4 .   ? 23.933 -20.296 -1.365  1.00 17.07 ?  418 HOH   A O    1 
HETATM 6726 O O    . HOH   E 4 .   ? 44.909 -0.669  2.986   1.00 42.82 ?  419 HOH   A O    1 
HETATM 6727 O O    . HOH   E 4 .   ? 32.562 -10.655 3.178   1.00 32.23 ?  420 HOH   A O    1 
HETATM 6728 O O    . HOH   E 4 .   ? 32.663 -4.309  -9.918  1.00 28.63 ?  421 HOH   A O    1 
HETATM 6729 O O    . HOH   E 4 .   ? 35.089 -5.225  -3.115  1.00 18.92 ?  422 HOH   A O    1 
HETATM 6730 O O    B HOH   E 4 .   ? 16.016 7.296   2.932   0.24 27.47 ?  423 HOH   A O    1 
HETATM 6731 O O    . HOH   E 4 .   ? 5.340  2.740   5.041   1.00 33.38 ?  424 HOH   A O    1 
HETATM 6732 O O    . HOH   E 4 .   ? 16.224 16.674  8.659   1.00 33.56 ?  425 HOH   A O    1 
HETATM 6733 O O    . HOH   E 4 .   ? 10.994 1.691   12.656  1.00 24.59 ?  426 HOH   A O    1 
HETATM 6734 O O    . HOH   E 4 .   ? 30.406 -12.963 13.468  1.00 21.34 ?  427 HOH   A O    1 
HETATM 6735 O O    . HOH   E 4 .   ? 36.754 -4.997  5.347   1.00 24.83 ?  428 HOH   A O    1 
HETATM 6736 O O    . HOH   E 4 .   ? 22.668 8.102   18.371  1.00 48.57 ?  429 HOH   A O    1 
HETATM 6737 O O    . HOH   E 4 .   ? 16.188 -14.175 20.218  1.00 50.90 ?  430 HOH   A O    1 
HETATM 6738 O O    . HOH   E 4 .   ? 10.385 -13.751 -1.676  1.00 17.94 ?  431 HOH   A O    1 
HETATM 6739 O O    A HOH   E 4 .   ? 16.033 6.941   2.991   0.76 16.51 ?  432 HOH   A O    1 
HETATM 6740 O O    B HOH   E 4 .   ? 7.281  1.825   7.245   0.24 24.49 ?  433 HOH   A O    1 
HETATM 6741 O O    . HOH   E 4 .   ? 11.691 -10.738 16.981  1.00 25.01 ?  434 HOH   A O    1 
HETATM 6742 O O    . HOH   E 4 .   ? 27.147 -3.221  19.331  1.00 39.49 ?  435 HOH   A O    1 
HETATM 6743 O O    . HOH   E 4 .   ? 16.146 2.870   -1.435  1.00 15.84 ?  436 HOH   A O    1 
HETATM 6744 O O    . HOH   E 4 .   ? 23.575 -8.057  17.088  1.00 23.07 ?  437 HOH   A O    1 
HETATM 6745 O O    B HOH   E 4 .   ? 18.530 2.025   -0.599  0.24 13.75 ?  438 HOH   A O    1 
HETATM 6746 O O    . HOH   E 4 .   ? 20.600 -17.801 24.772  1.00 53.44 ?  439 HOH   A O    1 
HETATM 6747 O O    . HOH   E 4 .   ? 9.496  -16.356 -1.979  1.00 43.29 ?  440 HOH   A O    1 
HETATM 6748 O O    . HOH   E 4 .   ? 18.531 4.907   -15.116 1.00 47.12 ?  441 HOH   A O    1 
HETATM 6749 O O    . HOH   E 4 .   ? 19.382 -11.052 24.095  1.00 70.32 ?  442 HOH   A O    1 
HETATM 6750 O O    . HOH   E 4 .   ? 23.351 -20.971 1.311   1.00 19.08 ?  443 HOH   A O    1 
HETATM 6751 O O    . HOH   E 4 .   ? 23.175 7.579   -3.206  1.00 31.10 ?  444 HOH   A O    1 
HETATM 6752 O O    . HOH   E 4 .   ? 34.425 -8.083  -0.564  1.00 30.49 ?  445 HOH   A O    1 
HETATM 6753 O O    . HOH   E 4 .   ? 21.297 -9.286  21.343  1.00 45.66 ?  446 HOH   A O    1 
HETATM 6754 O O    . HOH   E 4 .   ? 37.746 -8.838  -3.461  1.00 26.57 ?  447 HOH   A O    1 
HETATM 6755 O O    . HOH   E 4 .   ? 31.366 -12.784 -0.014  1.00 20.77 ?  448 HOH   A O    1 
HETATM 6756 O O    . HOH   E 4 .   ? 30.591 14.778  2.789   1.00 19.82 ?  449 HOH   A O    1 
HETATM 6757 O O    A HOH   E 4 .   ? 14.043 -0.353  3.454   0.46 40.27 ?  450 HOH   A O    1 
HETATM 6758 O O    . HOH   E 4 .   ? 18.461 -16.081 16.343  1.00 37.83 ?  451 HOH   A O    1 
HETATM 6759 O O    A HOH   E 4 .   ? 18.880 2.024   -0.755  0.76 14.75 ?  452 HOH   A O    1 
HETATM 6760 O O    B HOH   E 4 .   ? 10.454 4.645   2.603   0.24 24.64 ?  453 HOH   A O    1 
HETATM 6761 O O    . HOH   E 4 .   ? 21.582 -14.718 18.013  1.00 52.34 ?  454 HOH   A O    1 
HETATM 6762 O O    . HOH   E 4 .   ? 29.878 -16.101 10.666  1.00 36.48 ?  455 HOH   A O    1 
HETATM 6763 O O    . HOH   E 4 .   ? 27.782 7.018   -6.398  1.00 35.67 ?  456 HOH   A O    1 
HETATM 6764 O O    . HOH   E 4 .   ? 29.805 -1.938  -12.720 1.00 45.87 ?  457 HOH   A O    1 
HETATM 6765 O O    . HOH   E 4 .   ? 32.459 -15.948 10.805  1.00 35.33 ?  458 HOH   A O    1 
HETATM 6766 O O    . HOH   E 4 .   ? 25.404 8.203   -4.814  1.00 29.45 ?  459 HOH   A O    1 
HETATM 6767 O O    . HOH   E 4 .   ? 19.921 -17.358 -5.069  1.00 24.79 ?  460 HOH   A O    1 
HETATM 6768 O O    . HOH   E 4 .   ? 24.908 5.645   20.754  1.00 54.22 ?  461 HOH   A O    1 
HETATM 6769 O O    . HOH   E 4 .   ? 23.206 -22.383 -3.360  1.00 36.55 ?  462 HOH   A O    1 
HETATM 6770 O O    . HOH   E 4 .   ? 24.643 14.586  7.830   1.00 37.22 ?  463 HOH   A O    1 
HETATM 6771 O O    . HOH   E 4 .   ? 26.940 11.621  -1.342  1.00 32.40 ?  464 HOH   A O    1 
HETATM 6772 O O    . HOH   E 4 .   ? 21.906 5.174   -5.854  1.00 34.05 ?  465 HOH   A O    1 
HETATM 6773 O O    . HOH   E 4 .   ? 15.734 -21.531 3.689   1.00 24.74 ?  466 HOH   A O    1 
HETATM 6774 O O    . HOH   E 4 .   ? 18.787 10.863  11.307  1.00 34.26 ?  467 HOH   A O    1 
HETATM 6775 O O    . HOH   E 4 .   ? 27.536 -11.435 16.577  1.00 38.10 ?  468 HOH   A O    1 
HETATM 6776 O O    . HOH   E 4 .   ? 39.641 -6.987  -3.485  1.00 48.61 ?  469 HOH   A O    1 
HETATM 6777 O O    . HOH   E 4 .   ? 23.496 13.715  5.513   1.00 20.20 ?  470 HOH   A O    1 
HETATM 6778 O O    . HOH   E 4 .   ? 12.330 1.529   17.359  1.00 42.77 ?  471 HOH   A O    1 
HETATM 6779 O O    . HOH   E 4 .   ? 25.800 10.761  -3.716  1.00 27.18 ?  472 HOH   A O    1 
HETATM 6780 O O    . HOH   E 4 .   ? 12.003 -13.437 16.369  1.00 48.44 ?  473 HOH   A O    1 
HETATM 6781 O O    . HOH   E 4 .   ? 11.010 -15.069 -6.122  1.00 35.77 ?  474 HOH   A O    1 
HETATM 6782 O O    . HOH   E 4 .   ? 13.984 -10.352 -10.884 1.00 34.89 ?  475 HOH   A O    1 
HETATM 6783 O O    . HOH   E 4 .   ? 35.192 7.440   12.272  1.00 47.18 ?  476 HOH   A O    1 
HETATM 6784 O O    . HOH   E 4 .   ? 28.912 8.965   17.489  1.00 39.03 ?  477 HOH   A O    1 
HETATM 6785 O O    . HOH   E 4 .   ? 15.723 -17.116 -7.005  1.00 32.65 ?  478 HOH   A O    1 
HETATM 6786 O O    . HOH   E 4 .   ? 18.118 -16.280 -8.823  1.00 44.17 ?  479 HOH   A O    1 
HETATM 6787 O O    . HOH   E 4 .   ? 17.408 -18.729 19.821  1.00 52.54 ?  480 HOH   A O    1 
HETATM 6788 O O    . HOH   E 4 .   ? 30.862 0.696   19.126  1.00 40.77 ?  481 HOH   A O    1 
HETATM 6789 O O    . HOH   E 4 .   ? 41.006 -3.988  -0.357  1.00 36.59 ?  482 HOH   A O    1 
HETATM 6790 O O    . HOH   E 4 .   ? 23.155 11.834  -4.027  1.00 20.37 ?  483 HOH   A O    1 
HETATM 6791 O O    . HOH   E 4 .   ? 16.844 -20.556 16.144  1.00 31.12 ?  484 HOH   A O    1 
HETATM 6792 O O    B HOH   E 4 .   ? 10.782 -1.466  -5.510  0.24 15.76 ?  485 HOH   A O    1 
HETATM 6793 O O    . HOH   E 4 .   ? 28.615 -4.681  -12.289 1.00 38.81 ?  486 HOH   A O    1 
HETATM 6794 O O    . HOH   E 4 .   ? 20.542 -16.100 -7.404  1.00 30.73 ?  487 HOH   A O    1 
HETATM 6795 O O    . HOH   E 4 .   ? 41.677 9.234   -4.115  1.00 32.81 ?  488 HOH   A O    1 
HETATM 6796 O O    . HOH   E 4 .   ? 23.253 -12.919 19.304  1.00 47.10 ?  489 HOH   A O    1 
HETATM 6797 O O    . HOH   E 4 .   ? 44.545 10.458  -1.612  1.00 30.91 ?  490 HOH   A O    1 
HETATM 6798 O O    . HOH   E 4 .   ? 31.436 -0.569  -10.586 1.00 29.18 ?  491 HOH   A O    1 
HETATM 6799 O O    . HOH   E 4 .   ? 18.415 -23.198 1.885   1.00 44.52 ?  492 HOH   A O    1 
HETATM 6800 O O    . HOH   E 4 .   ? 28.718 -7.927  -15.287 1.00 48.52 ?  493 HOH   A O    1 
HETATM 6801 O O    . HOH   E 4 .   ? 39.198 2.392   7.517   1.00 34.48 ?  494 HOH   A O    1 
HETATM 6802 O O    . HOH   E 4 .   ? 40.546 -0.221  -7.817  1.00 35.41 ?  495 HOH   A O    1 
HETATM 6803 O O    . HOH   E 4 .   ? 16.029 -6.762  -11.876 1.00 43.08 ?  496 HOH   A O    1 
HETATM 6804 O O    . HOH   E 4 .   ? 13.987 -25.312 8.900   1.00 32.98 ?  497 HOH   A O    1 
HETATM 6805 O O    . HOH   E 4 .   ? 20.016 -22.376 4.169   1.00 28.96 ?  498 HOH   A O    1 
HETATM 6806 O O    . HOH   E 4 .   ? 16.176 -23.390 5.754   1.00 28.44 ?  499 HOH   A O    1 
HETATM 6807 O O    . HOH   E 4 .   ? 30.782 -5.824  -11.860 1.00 48.51 ?  500 HOH   A O    1 
HETATM 6808 O O    . HOH   E 4 .   ? 30.752 5.813   -14.723 1.00 37.67 ?  501 HOH   A O    1 
HETATM 6809 O O    . HOH   E 4 .   ? 37.415 -6.656  7.569   1.00 25.90 ?  502 HOH   A O    1 
HETATM 6810 O O    . HOH   E 4 .   ? 8.199  -3.043  -5.781  1.00 49.63 ?  503 HOH   A O    1 
HETATM 6811 O O    . HOH   E 4 .   ? 23.144 -23.790 1.634   1.00 32.28 ?  504 HOH   A O    1 
HETATM 6812 O O    . HOH   E 4 .   ? 39.563 0.001   6.589   1.00 30.15 ?  505 HOH   A O    1 
HETATM 6813 O O    . HOH   E 4 .   ? 29.013 14.431  0.856   1.00 48.67 ?  506 HOH   A O    1 
HETATM 6814 O O    . HOH   E 4 .   ? 38.027 13.938  6.718   1.00 48.13 ?  507 HOH   A O    1 
HETATM 6815 O O    . HOH   E 4 .   ? 14.850 8.266   5.047   1.00 44.70 ?  508 HOH   A O    1 
HETATM 6816 O O    . HOH   E 4 .   ? 22.021 -24.049 4.450   1.00 26.81 ?  509 HOH   A O    1 
HETATM 6817 O O    . HOH   E 4 .   ? 36.452 -6.522  10.131  1.00 44.87 ?  510 HOH   A O    1 
HETATM 6818 O O    B HOH   E 4 .   ? 9.930  1.049   -5.309  0.24 19.11 ?  511 HOH   A O    1 
HETATM 6819 O O    T HOH   E 4 .   ? 11.940 -2.155  -3.665  0.30 13.05 ?  512 HOH   A O    1 
HETATM 6820 O O    . HOH   E 4 .   ? 17.395 -6.550  -14.221 1.00 41.11 ?  513 HOH   A O    1 
HETATM 6821 O O    . HOH   E 4 .   ? 24.055 9.017   -7.227  1.00 37.11 ?  514 HOH   A O    1 
HETATM 6822 O O    . HOH   E 4 .   ? 16.324 -21.194 18.718  1.00 37.02 ?  515 HOH   A O    1 
HETATM 6823 O O    . HOH   E 4 .   ? 15.894 -12.260 27.465  1.00 44.94 ?  516 HOH   A O    1 
HETATM 6824 O O    . HOH   E 4 .   ? 14.717 -22.780 19.806  1.00 36.86 ?  517 HOH   A O    1 
HETATM 6825 O O    . HOH   F 4 .   ? 29.858 -22.439 5.459   1.00 21.49 ?  201 HOH   B O    1 
HETATM 6826 O O    . HOH   F 4 .   ? 49.407 -22.649 -19.762 1.00 48.57 ?  202 HOH   B O    1 
HETATM 6827 O O    . HOH   F 4 .   ? 48.146 -6.888  15.543  1.00 38.72 ?  203 HOH   B O    1 
HETATM 6828 O O    . HOH   F 4 .   ? 41.853 -35.973 -17.294 1.00 30.80 ?  204 HOH   B O    1 
HETATM 6829 O O    . HOH   F 4 .   ? 37.960 -39.474 -0.185  1.00 41.81 ?  205 HOH   B O    1 
HETATM 6830 O O    . HOH   F 4 .   ? 52.953 -13.436 -20.349 1.00 38.15 ?  206 HOH   B O    1 
HETATM 6831 O O    . HOH   F 4 .   ? 59.182 -18.751 6.827   1.00 39.58 ?  207 HOH   B O    1 
HETATM 6832 O O    . HOH   F 4 .   ? 41.430 -7.719  5.481   1.00 40.37 ?  208 HOH   B O    1 
HETATM 6833 O O    . HOH   F 4 .   ? 27.745 -29.170 -1.860  1.00 36.70 ?  209 HOH   B O    1 
HETATM 6834 O O    . HOH   F 4 .   ? 54.521 -9.388  -8.763  1.00 20.97 ?  210 HOH   B O    1 
HETATM 6835 O O    . HOH   F 4 .   ? 29.949 -26.320 3.997   1.00 29.33 ?  211 HOH   B O    1 
HETATM 6836 O O    . HOH   F 4 .   ? 27.873 -41.860 -15.188 1.00 36.39 ?  212 HOH   B O    1 
HETATM 6837 O O    . HOH   F 4 .   ? 47.405 -7.428  -3.930  1.00 39.78 ?  213 HOH   B O    1 
HETATM 6838 O O    . HOH   F 4 .   ? 56.398 -19.751 7.242   1.00 33.80 ?  214 HOH   B O    1 
HETATM 6839 O O    . HOH   F 4 .   ? 30.239 -41.028 -8.143  1.00 17.48 ?  215 HOH   B O    1 
HETATM 6840 O O    . HOH   F 4 .   ? 44.468 -7.263  2.082   1.00 36.29 ?  216 HOH   B O    1 
HETATM 6841 O O    . HOH   F 4 .   ? 50.313 -3.340  7.169   1.00 36.37 ?  217 HOH   B O    1 
HETATM 6842 O O    . HOH   F 4 .   ? 55.402 -16.486 -14.382 1.00 36.11 ?  218 HOH   B O    1 
HETATM 6843 O O    . HOH   F 4 .   ? 50.765 -6.126  0.177   1.00 28.81 ?  219 HOH   B O    1 
HETATM 6844 O O    . HOH   F 4 .   ? 57.243 -26.924 -7.622  1.00 41.69 ?  220 HOH   B O    1 
HETATM 6845 O O    . HOH   F 4 .   ? 56.757 -30.764 -7.796  1.00 35.41 ?  221 HOH   B O    1 
HETATM 6846 O O    . HOH   F 4 .   ? 57.777 -24.479 5.020   1.00 37.13 ?  222 HOH   B O    1 
HETATM 6847 O O    . HOH   F 4 .   ? 58.276 -12.916 8.410   1.00 34.26 ?  223 HOH   B O    1 
HETATM 6848 O O    . HOH   F 4 .   ? 36.019 -43.308 -8.555  1.00 32.35 ?  224 HOH   B O    1 
HETATM 6849 O O    . HOH   F 4 .   ? 29.813 -34.208 -0.469  1.00 35.46 ?  225 HOH   B O    1 
HETATM 6850 O O    . HOH   F 4 .   ? 37.154 -19.782 -18.106 1.00 42.07 ?  226 HOH   B O    1 
HETATM 6851 O O    . HOH   F 4 .   ? 30.879 -28.798 4.255   1.00 27.22 ?  227 HOH   B O    1 
HETATM 6852 O O    . HOH   F 4 .   ? 57.449 -16.256 -12.212 1.00 20.24 ?  228 HOH   B O    1 
HETATM 6853 O O    . HOH   F 4 .   ? 34.568 -36.412 -7.219  1.00 18.58 ?  229 HOH   B O    1 
HETATM 6854 O O    . HOH   F 4 .   ? 41.536 -39.175 -14.936 1.00 23.00 ?  230 HOH   B O    1 
HETATM 6855 O O    . HOH   F 4 .   ? 48.605 -36.471 -15.523 1.00 41.55 ?  231 HOH   B O    1 
HETATM 6856 O O    . HOH   F 4 .   ? 51.702 -6.490  4.424   1.00 21.76 ?  232 HOH   B O    1 
HETATM 6857 O O    . HOH   F 4 .   ? 45.212 -34.980 6.821   1.00 41.38 ?  233 HOH   B O    1 
HETATM 6858 O O    . HOH   F 4 .   ? 28.449 -19.712 -13.133 1.00 25.18 ?  234 HOH   B O    1 
HETATM 6859 O O    . HOH   F 4 .   ? 39.332 -10.920 6.118   1.00 27.20 ?  235 HOH   B O    1 
HETATM 6860 O O    . HOH   F 4 .   ? 40.701 -16.068 14.139  1.00 25.77 ?  236 HOH   B O    1 
HETATM 6861 O O    . HOH   F 4 .   ? 44.523 -27.754 -0.727  1.00 23.45 ?  237 HOH   B O    1 
HETATM 6862 O O    . HOH   F 4 .   ? 50.762 -12.975 -0.479  1.00 13.14 ?  238 HOH   B O    1 
HETATM 6863 O O    . HOH   F 4 .   ? 48.105 -24.533 -17.773 1.00 31.70 ?  239 HOH   B O    1 
HETATM 6864 O O    . HOH   F 4 .   ? 46.399 -1.593  13.266  1.00 29.41 ?  240 HOH   B O    1 
HETATM 6865 O O    . HOH   F 4 .   ? 35.142 -7.994  -3.054  1.00 18.65 ?  241 HOH   B O    1 
HETATM 6866 O O    . HOH   F 4 .   ? 41.422 -9.643  13.061  1.00 24.50 ?  242 HOH   B O    1 
HETATM 6867 O O    . HOH   F 4 .   ? 25.429 -25.976 -1.340  1.00 33.31 ?  243 HOH   B O    1 
HETATM 6868 O O    . HOH   F 4 .   ? 45.002 -43.569 -10.547 1.00 28.56 ?  244 HOH   B O    1 
HETATM 6869 O O    . HOH   F 4 .   ? 42.593 -25.388 2.611   1.00 15.94 ?  245 HOH   B O    1 
HETATM 6870 O O    . HOH   F 4 .   ? 57.674 -24.386 -3.811  1.00 22.68 ?  246 HOH   B O    1 
HETATM 6871 O O    . HOH   F 4 .   ? 27.162 -31.848 -9.965  1.00 22.85 ?  247 HOH   B O    1 
HETATM 6872 O O    . HOH   F 4 .   ? 32.851 -43.840 -11.350 1.00 21.36 ?  248 HOH   B O    1 
HETATM 6873 O O    . HOH   F 4 .   ? 42.676 -22.897 3.829   1.00 12.39 ?  249 HOH   B O    1 
HETATM 6874 O O    . HOH   F 4 .   ? 43.144 -43.274 -8.279  1.00 30.12 ?  250 HOH   B O    1 
HETATM 6875 O O    . HOH   F 4 .   ? 40.362 -12.768 -11.516 1.00 15.85 ?  251 HOH   B O    1 
HETATM 6876 O O    . HOH   F 4 .   ? 39.509 -11.141 0.307   1.00 18.24 ?  252 HOH   B O    1 
HETATM 6877 O O    . HOH   F 4 .   ? 51.590 -13.882 11.019  1.00 28.79 ?  253 HOH   B O    1 
HETATM 6878 O O    . HOH   F 4 .   ? 34.910 -24.659 13.837  1.00 29.90 ?  254 HOH   B O    1 
HETATM 6879 O O    . HOH   F 4 .   ? 34.246 -18.529 11.405  1.00 24.85 ?  255 HOH   B O    1 
HETATM 6880 O O    . HOH   F 4 .   ? 30.889 -15.770 2.643   1.00 14.69 ?  256 HOH   B O    1 
HETATM 6881 O O    . HOH   F 4 .   ? 29.748 -25.227 -10.856 1.00 17.10 ?  257 HOH   B O    1 
HETATM 6882 O O    . HOH   F 4 .   ? 58.196 -10.626 -4.092  1.00 22.09 ?  258 HOH   B O    1 
HETATM 6883 O O    . HOH   F 4 .   ? 31.842 -17.924 -14.519 1.00 30.99 ?  259 HOH   B O    1 
HETATM 6884 O O    . HOH   F 4 .   ? 51.012 -39.977 -8.275  1.00 35.20 ?  260 HOH   B O    1 
HETATM 6885 O O    . HOH   F 4 .   ? 38.482 -11.065 -2.250  1.00 19.78 ?  261 HOH   B O    1 
HETATM 6886 O O    . HOH   F 4 .   ? 33.535 -17.029 8.039   1.00 20.12 ?  262 HOH   B O    1 
HETATM 6887 O O    . HOH   F 4 .   ? 34.515 -12.812 2.585   1.00 24.99 ?  263 HOH   B O    1 
HETATM 6888 O O    . HOH   F 4 .   ? 41.910 -23.546 9.269   1.00 18.13 ?  264 HOH   B O    1 
HETATM 6889 O O    . HOH   F 4 .   ? 48.022 -22.782 5.832   1.00 18.03 ?  265 HOH   B O    1 
HETATM 6890 O O    . HOH   F 4 .   ? 43.259 -32.372 -17.098 1.00 23.52 ?  266 HOH   B O    1 
HETATM 6891 O O    . HOH   F 4 .   ? 56.221 -23.499 -14.696 1.00 26.90 ?  267 HOH   B O    1 
HETATM 6892 O O    . HOH   F 4 .   ? 38.922 -12.039 12.341  1.00 36.19 ?  268 HOH   B O    1 
HETATM 6893 O O    . HOH   F 4 .   ? 28.308 -34.384 -9.467  1.00 20.53 ?  269 HOH   B O    1 
HETATM 6894 O O    . HOH   F 4 .   ? 49.356 -28.714 -6.912  1.00 16.01 ?  270 HOH   B O    1 
HETATM 6895 O O    . HOH   F 4 .   ? 49.796 -0.505  10.281  1.00 34.08 ?  271 HOH   B O    1 
HETATM 6896 O O    . HOH   F 4 .   ? 42.348 -9.913  9.368   1.00 22.75 ?  272 HOH   B O    1 
HETATM 6897 O O    . HOH   F 4 .   ? 57.541 -9.224  1.413   1.00 21.68 ?  273 HOH   B O    1 
HETATM 6898 O O    . HOH   F 4 .   ? 43.406 -15.793 -12.185 1.00 14.67 ?  274 HOH   B O    1 
HETATM 6899 O O    . HOH   F 4 .   ? 34.943 -33.398 -19.222 1.00 30.97 ?  275 HOH   B O    1 
HETATM 6900 O O    . HOH   F 4 .   ? 30.570 -42.296 -10.634 1.00 31.16 ?  276 HOH   B O    1 
HETATM 6901 O O    . HOH   F 4 .   ? 56.972 -8.635  8.442   1.00 21.40 ?  277 HOH   B O    1 
HETATM 6902 O O    . HOH   F 4 .   ? 46.635 -31.303 -4.803  1.00 22.27 ?  278 HOH   B O    1 
HETATM 6903 O O    . HOH   F 4 .   ? 46.888 -29.582 9.797   1.00 32.80 ?  279 HOH   B O    1 
HETATM 6904 O O    . HOH   F 4 .   ? 28.505 -30.906 -14.781 1.00 30.80 ?  280 HOH   B O    1 
HETATM 6905 O O    . HOH   F 4 .   ? 48.456 -25.064 3.110   1.00 14.00 ?  281 HOH   B O    1 
HETATM 6906 O O    . HOH   F 4 .   ? 42.435 -34.725 3.754   1.00 26.79 ?  282 HOH   B O    1 
HETATM 6907 O O    . HOH   F 4 .   ? 33.559 -15.321 -13.959 1.00 21.88 ?  283 HOH   B O    1 
HETATM 6908 O O    . HOH   F 4 .   ? 36.835 -12.795 -1.519  1.00 27.64 ?  284 HOH   B O    1 
HETATM 6909 O O    . HOH   F 4 .   ? 42.348 -9.984  -14.933 1.00 37.18 ?  285 HOH   B O    1 
HETATM 6910 O O    . HOH   F 4 .   ? 27.971 -22.907 -8.028  1.00 18.08 ?  286 HOH   B O    1 
HETATM 6911 O O    . HOH   F 4 .   ? 52.583 -10.409 13.006  1.00 23.99 ?  287 HOH   B O    1 
HETATM 6912 O O    . HOH   F 4 .   ? 27.606 -26.708 -15.650 1.00 33.68 ?  288 HOH   B O    1 
HETATM 6913 O O    . HOH   F 4 .   ? 59.809 -15.398 8.173   1.00 34.41 ?  289 HOH   B O    1 
HETATM 6914 O O    . HOH   F 4 .   ? 45.975 -40.478 -3.630  1.00 29.58 ?  290 HOH   B O    1 
HETATM 6915 O O    . HOH   F 4 .   ? 50.035 -24.628 5.801   1.00 35.51 ?  291 HOH   B O    1 
HETATM 6916 O O    . HOH   F 4 .   ? 45.409 -33.435 -15.946 1.00 24.07 ?  292 HOH   B O    1 
HETATM 6917 O O    . HOH   F 4 .   ? 42.907 -20.323 -20.795 1.00 37.93 ?  293 HOH   B O    1 
HETATM 6918 O O    . HOH   F 4 .   ? 37.389 -35.703 7.189   1.00 34.99 ?  294 HOH   B O    1 
HETATM 6919 O O    . HOH   F 4 .   ? 48.731 -20.058 5.934   1.00 14.78 ?  295 HOH   B O    1 
HETATM 6920 O O    . HOH   F 4 .   ? 51.289 -37.645 -9.605  1.00 27.17 ?  296 HOH   B O    1 
HETATM 6921 O O    . HOH   F 4 .   ? 41.210 -5.484  11.459  1.00 44.47 ?  297 HOH   B O    1 
HETATM 6922 O O    . HOH   F 4 .   ? 47.113 -34.004 -4.627  1.00 18.50 ?  298 HOH   B O    1 
HETATM 6923 O O    . HOH   F 4 .   ? 57.161 -12.069 12.385  1.00 37.40 ?  299 HOH   B O    1 
HETATM 6924 O O    . HOH   F 4 .   ? 44.651 -27.483 1.979   1.00 16.14 ?  300 HOH   B O    1 
HETATM 6925 O O    . HOH   F 4 .   ? 37.576 -18.210 13.114  1.00 30.19 ?  301 HOH   B O    1 
HETATM 6926 O O    . HOH   F 4 .   ? 44.056 -29.371 -4.718  1.00 25.00 ?  302 HOH   B O    1 
HETATM 6927 O O    . HOH   F 4 .   ? 42.778 -12.236 -18.530 1.00 28.29 ?  303 HOH   B O    1 
HETATM 6928 O O    . HOH   F 4 .   ? 35.084 -33.605 4.508   1.00 29.26 ?  304 HOH   B O    1 
HETATM 6929 O O    . HOH   F 4 .   ? 52.669 -35.686 -8.630  1.00 30.08 ?  305 HOH   B O    1 
HETATM 6930 O O    . HOH   F 4 .   ? 53.154 -16.051 -12.739 1.00 29.76 ?  306 HOH   B O    1 
HETATM 6931 O O    . HOH   F 4 .   ? 53.507 -30.231 4.485   1.00 19.81 ?  307 HOH   B O    1 
HETATM 6932 O O    . HOH   F 4 .   ? 40.285 -10.838 -9.573  1.00 17.96 ?  308 HOH   B O    1 
HETATM 6933 O O    . HOH   F 4 .   ? 52.598 -29.268 -13.037 1.00 24.93 ?  309 HOH   B O    1 
HETATM 6934 O O    . HOH   F 4 .   ? 25.978 -21.499 -3.547  1.00 17.06 ?  310 HOH   B O    1 
HETATM 6935 O O    . HOH   F 4 .   ? 37.857 -10.242 -10.754 1.00 17.80 ?  311 HOH   B O    1 
HETATM 6936 O O    . HOH   F 4 .   ? 62.872 -20.206 -0.799  1.00 41.20 ?  312 HOH   B O    1 
HETATM 6937 O O    . HOH   F 4 .   ? 43.539 -15.394 18.231  1.00 30.73 ?  313 HOH   B O    1 
HETATM 6938 O O    . HOH   F 4 .   ? 41.195 -24.502 15.807  1.00 44.76 ?  314 HOH   B O    1 
HETATM 6939 O O    . HOH   F 4 .   ? 37.145 -30.615 -21.039 1.00 33.07 ?  315 HOH   B O    1 
HETATM 6940 O O    . HOH   F 4 .   ? 43.249 -21.461 10.665  1.00 16.82 ?  316 HOH   B O    1 
HETATM 6941 O O    . HOH   F 4 .   ? 32.848 -34.619 -5.960  1.00 17.61 ?  317 HOH   B O    1 
HETATM 6942 O O    . HOH   F 4 .   ? 62.741 -13.591 4.709   1.00 29.06 ?  318 HOH   B O    1 
HETATM 6943 O O    . HOH   F 4 .   ? 48.118 -32.606 -16.652 1.00 44.94 ?  319 HOH   B O    1 
HETATM 6944 O O    . HOH   F 4 .   ? 38.379 -9.384  -13.291 1.00 28.63 ?  320 HOH   B O    1 
HETATM 6945 O O    . HOH   F 4 .   ? 41.747 -8.078  1.349   1.00 26.24 ?  321 HOH   B O    1 
HETATM 6946 O O    . HOH   F 4 .   ? 51.751 -5.916  -7.886  1.00 47.08 ?  322 HOH   B O    1 
HETATM 6947 O O    . HOH   F 4 .   ? 57.685 -22.097 3.170   1.00 30.66 ?  323 HOH   B O    1 
HETATM 6948 O O    . HOH   F 4 .   ? 26.364 -21.055 -6.262  1.00 17.22 ?  324 HOH   B O    1 
HETATM 6949 O O    . HOH   F 4 .   ? 53.665 -12.549 -22.282 1.00 37.74 ?  325 HOH   B O    1 
HETATM 6950 O O    . HOH   F 4 .   ? 51.442 -32.941 -10.792 1.00 41.26 ?  326 HOH   B O    1 
HETATM 6951 O O    . HOH   F 4 .   ? 44.603 -24.640 9.574   1.00 20.25 ?  327 HOH   B O    1 
HETATM 6952 O O    . HOH   F 4 .   ? 60.000 -17.176 -10.498 1.00 34.94 ?  328 HOH   B O    1 
HETATM 6953 O O    . HOH   F 4 .   ? 38.376 -12.779 7.900   1.00 19.09 ?  329 HOH   B O    1 
HETATM 6954 O O    . HOH   F 4 .   ? 36.754 -12.438 4.278   1.00 19.59 ?  330 HOH   B O    1 
HETATM 6955 O O    . HOH   F 4 .   ? 27.911 -14.775 -9.452  1.00 37.63 ?  331 HOH   B O    1 
HETATM 6956 O O    . HOH   F 4 .   ? 44.210 -1.773  7.549   1.00 47.98 ?  332 HOH   B O    1 
HETATM 6957 O O    . HOH   F 4 .   ? 33.616 -31.200 11.054  1.00 35.84 ?  333 HOH   B O    1 
HETATM 6958 O O    . HOH   F 4 .   ? 47.179 -24.533 8.159   1.00 26.61 ?  334 HOH   B O    1 
HETATM 6959 O O    . HOH   F 4 .   ? 43.145 -34.691 0.068   1.00 20.56 ?  335 HOH   B O    1 
HETATM 6960 O O    . HOH   F 4 .   ? 48.623 -11.968 -13.982 1.00 28.37 ?  336 HOH   B O    1 
HETATM 6961 O O    . HOH   F 4 .   ? 39.468 -23.525 -20.362 1.00 37.56 ?  337 HOH   B O    1 
HETATM 6962 O O    . HOH   F 4 .   ? 47.498 -27.467 2.000   1.00 15.76 ?  338 HOH   B O    1 
HETATM 6963 O O    . HOH   F 4 .   ? 37.032 -15.099 -16.504 1.00 39.91 ?  339 HOH   B O    1 
HETATM 6964 O O    . HOH   F 4 .   ? 42.891 -43.501 -14.440 1.00 45.14 ?  340 HOH   B O    1 
HETATM 6965 O O    . HOH   F 4 .   ? 46.851 -19.928 12.303  1.00 31.29 ?  341 HOH   B O    1 
HETATM 6966 O O    . HOH   F 4 .   ? 45.801 -36.250 -16.144 1.00 34.17 ?  342 HOH   B O    1 
HETATM 6967 O O    . HOH   F 4 .   ? 28.896 -42.925 -12.400 1.00 41.34 ?  343 HOH   B O    1 
HETATM 6968 O O    . HOH   F 4 .   ? 37.123 -45.239 -9.786  1.00 38.92 ?  344 HOH   B O    1 
HETATM 6969 O O    . HOH   F 4 .   ? 33.040 -14.718 1.055   1.00 19.29 ?  345 HOH   B O    1 
HETATM 6970 O O    . HOH   F 4 .   ? 38.493 -12.300 -16.278 1.00 40.81 ?  346 HOH   B O    1 
HETATM 6971 O O    . HOH   F 4 .   ? 39.857 -44.317 -11.209 1.00 40.04 ?  347 HOH   B O    1 
HETATM 6972 O O    . HOH   F 4 .   ? 27.756 -26.630 -0.618  1.00 31.34 ?  348 HOH   B O    1 
HETATM 6973 O O    . HOH   F 4 .   ? 40.457 -43.517 -9.125  1.00 28.03 ?  349 HOH   B O    1 
HETATM 6974 O O    . HOH   F 4 .   ? 38.560 -22.364 15.048  1.00 40.76 ?  350 HOH   B O    1 
HETATM 6975 O O    . HOH   F 4 .   ? 33.795 -9.314  -8.820  1.00 33.31 ?  351 HOH   B O    1 
HETATM 6976 O O    . HOH   F 4 .   ? 62.578 -20.238 -4.855  1.00 44.81 ?  352 HOH   B O    1 
HETATM 6977 O O    . HOH   F 4 .   ? 55.697 -8.260  10.790  1.00 25.93 ?  353 HOH   B O    1 
HETATM 6978 O O    . HOH   F 4 .   ? 23.253 -23.694 6.797   1.00 35.37 ?  354 HOH   B O    1 
HETATM 6979 O O    . HOH   F 4 .   ? 44.214 -37.374 -17.796 1.00 34.28 ?  355 HOH   B O    1 
HETATM 6980 O O    . HOH   F 4 .   ? 56.610 -7.309  3.127   1.00 28.69 ?  356 HOH   B O    1 
HETATM 6981 O O    . HOH   F 4 .   ? 36.136 -8.530  -9.678  1.00 35.63 ?  357 HOH   B O    1 
HETATM 6982 O O    . HOH   F 4 .   ? 34.678 -10.327 7.465   1.00 25.96 ?  358 HOH   B O    1 
HETATM 6983 O O    . HOH   F 4 .   ? 43.211 -12.731 -21.218 1.00 35.29 ?  359 HOH   B O    1 
HETATM 6984 O O    . HOH   F 4 .   ? 34.117 -7.808  11.456  1.00 42.78 ?  360 HOH   B O    1 
HETATM 6985 O O    . HOH   F 4 .   ? 61.561 -19.952 1.679   1.00 36.65 ?  361 HOH   B O    1 
HETATM 6986 O O    . HOH   F 4 .   ? 56.958 -21.556 -16.388 1.00 40.96 ?  362 HOH   B O    1 
HETATM 6987 O O    . HOH   F 4 .   ? 40.280 -8.851  9.879   1.00 40.51 ?  363 HOH   B O    1 
HETATM 6988 O O    . HOH   F 4 .   ? 27.192 -25.986 -11.467 1.00 34.50 ?  364 HOH   B O    1 
HETATM 6989 O O    . HOH   F 4 .   ? 54.249 -5.759  3.003   1.00 37.10 ?  365 HOH   B O    1 
HETATM 6990 O O    . HOH   F 4 .   ? 58.959 -10.462 9.194   1.00 41.36 ?  366 HOH   B O    1 
HETATM 6991 O O    . HOH   F 4 .   ? 32.550 -23.626 14.057  1.00 41.84 ?  367 HOH   B O    1 
HETATM 6992 O O    . HOH   F 4 .   ? 36.211 -8.748  8.960   1.00 40.55 ?  368 HOH   B O    1 
HETATM 6993 O O    . HOH   F 4 .   ? 48.391 -26.547 8.806   1.00 40.30 ?  369 HOH   B O    1 
HETATM 6994 O O    . HOH   F 4 .   ? 40.133 -11.363 -13.960 1.00 34.24 ?  370 HOH   B O    1 
HETATM 6995 O O    . HOH   F 4 .   ? 41.865 -10.047 -17.455 1.00 57.08 ?  371 HOH   B O    1 
HETATM 6996 O O    . HOH   F 4 .   ? 39.863 -7.052  7.823   1.00 41.96 ?  372 HOH   B O    1 
HETATM 6997 O O    . HOH   F 4 .   ? 56.099 -7.808  -0.601  1.00 37.72 ?  373 HOH   B O    1 
HETATM 6998 O O    . HOH   F 4 .   ? 52.066 -12.895 13.341  1.00 32.65 ?  374 HOH   B O    1 
HETATM 6999 O O    . HOH   F 4 .   ? 63.042 -12.419 6.925   1.00 39.57 ?  375 HOH   B O    1 
HETATM 7000 O O    . HOH   F 4 .   ? 38.080 -10.619 10.087  1.00 30.80 ?  376 HOH   B O    1 
HETATM 7001 O O    . HOH   F 4 .   ? 36.549 -22.844 13.267  1.00 27.07 ?  377 HOH   B O    1 
HETATM 7002 O O    . HOH   F 4 .   ? 41.862 -6.723  -4.846  1.00 48.67 ?  378 HOH   B O    1 
HETATM 7003 O O    . HOH   F 4 .   ? 44.055 -5.599  -3.537  1.00 44.90 ?  379 HOH   B O    1 
HETATM 7004 O O    . HOH   F 4 .   ? 42.683 -17.083 -23.213 1.00 43.19 ?  380 HOH   B O    1 
HETATM 7005 O O    . HOH   F 4 .   ? 40.180 -7.666  3.185   1.00 38.61 ?  381 HOH   B O    1 
HETATM 7006 O O    . HOH   F 4 .   ? 39.726 -14.127 15.723  1.00 51.18 ?  382 HOH   B O    1 
HETATM 7007 O O    . HOH   F 4 .   ? 52.879 -29.942 7.188   1.00 25.19 ?  383 HOH   B O    1 
HETATM 7008 O O    . HOH   F 4 .   ? 60.515 -22.289 2.816   1.00 48.66 ?  384 HOH   B O    1 
HETATM 7009 O O    . HOH   F 4 .   ? 46.795 -5.386  2.890   1.00 41.79 ?  385 HOH   B O    1 
HETATM 7010 O O    . HOH   F 4 .   ? 25.786 -18.890 -11.905 1.00 38.58 ?  386 HOH   B O    1 
HETATM 7011 O O    . HOH   F 4 .   ? 23.944 -20.847 -7.702  1.00 29.53 ?  387 HOH   B O    1 
HETATM 7012 O O    . HOH   F 4 .   ? 35.420 -33.773 7.263   1.00 41.47 ?  388 HOH   B O    1 
HETATM 7013 O O    . HOH   F 4 .   ? 40.893 -9.874  15.793  1.00 45.49 ?  389 HOH   B O    1 
HETATM 7014 O O    . HOH   F 4 .   ? 35.314 -20.365 13.317  1.00 32.03 ?  390 HOH   B O    1 
HETATM 7015 O O    . HOH   F 4 .   ? 40.719 -6.638  -0.879  1.00 27.02 ?  391 HOH   B O    1 
HETATM 7016 O O    . HOH   F 4 .   ? 44.145 -31.826 -3.872  1.00 33.59 ?  392 HOH   B O    1 
HETATM 7017 O O    . HOH   F 4 .   ? 26.670 -27.984 -13.533 1.00 36.61 ?  393 HOH   B O    1 
HETATM 7018 O O    . HOH   F 4 .   ? 27.947 -27.126 2.162   1.00 32.32 ?  394 HOH   B O    1 
HETATM 7019 O O    . HOH   F 4 .   ? 34.422 -33.448 9.614   1.00 34.45 ?  395 HOH   B O    1 
HETATM 7020 O O    . HOH   F 4 .   ? 24.628 -20.663 -10.469 1.00 38.35 ?  396 HOH   B O    1 
HETATM 7021 O O    . HOH   F 4 .   ? 50.650 -30.805 8.674   1.00 29.65 ?  397 HOH   B O    1 
HETATM 7022 O O    . HOH   F 4 .   ? 26.871 -30.682 -12.675 1.00 30.69 ?  398 HOH   B O    1 
HETATM 7023 O O    . HOH   F 4 .   ? 45.842 -20.250 15.154  1.00 52.83 ?  399 HOH   B O    1 
HETATM 7024 O O    . HOH   F 4 .   ? 57.590 -6.429  -2.358  1.00 34.70 ?  400 HOH   B O    1 
HETATM 7025 O O    . HOH   F 4 .   ? 40.954 -11.814 -22.347 1.00 40.93 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.6427 0.6456 0.6956 -0.0016 -0.0222 0.0847  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6384 0.6423 0.6665 -0.0068 -0.0159 0.0547  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6396 0.6423 0.6885 -0.0022 -0.0226 0.0823  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6357 0.6398 0.6623 -0.0073 -0.0164 0.0560  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.6270 0.6325 0.6605 -0.0093 -0.0238 0.0814  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6250 0.6320 0.6456 -0.0120 -0.0197 0.0667  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.6294 0.6339 0.6690 -0.0065 -0.0236 0.0843  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6275 0.6342 0.6519 -0.0105 -0.0193 0.0668  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6472 0.6471 0.7004 0.0025  -0.0193 0.0827  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.6416 0.6437 0.6685 -0.0042 -0.0135 0.0488  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6493 0.6486 0.7055 0.0033  -0.0175 0.0834  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.6435 0.6451 0.6726 -0.0032 -0.0122 0.0464  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6503 0.6485 0.7071 0.0046  -0.0176 0.0834  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.6438 0.6450 0.6730 -0.0028 -0.0122 0.0465  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.6094 0.6202 0.6118 -0.0191 -0.0225 0.0787  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.5756 0.5941 0.5269 -0.0376 -0.0212 0.0864  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.5355 0.5679 0.4769 -0.0551 -0.0090 0.0645  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.5392 0.5725 0.4681 -0.0559 -0.0124 0.0698  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.5811 0.5941 0.4883 -0.0407 -0.0320 0.1125  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.5864 0.5932 0.4529 -0.0456 -0.0391 0.1369  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.5896 0.5915 0.4303 -0.0477 -0.0400 0.1462  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.5872 0.5931 0.4403 -0.0474 -0.0432 0.1485  4   ASN   A ND2 
46   N N   . SER   A 5   ? 0.4904 0.5349 0.4305 -0.0725 0.0020  0.0376  5   SER   A N   
47   C CA  . SER   A 5   ? 0.4444 0.5050 0.3950 -0.0870 0.0145  0.0113  5   SER   A CA  
48   C C   . SER   A 5   ? 0.3956 0.4634 0.3270 -0.0939 0.0216  -0.0102 5   SER   A C   
49   O O   . SER   A 5   ? 0.3999 0.4765 0.3272 -0.0828 0.0246  -0.0251 5   SER   A O   
50   C CB  . SER   A 5   ? 0.4509 0.5141 0.4148 -0.0918 0.0223  0.0066  5   SER   A CB  
51   O OG  . SER   A 5   ? 0.4568 0.5206 0.4309 -0.0948 0.0319  0.0032  5   SER   A OG  
57   N N   . PHE   A 6   ? 0.3399 0.4055 0.2677 -0.1084 0.0285  -0.0120 6   PHE   A N   
58   C CA  . PHE   A 6   ? 0.2958 0.3529 0.2215 -0.1065 0.0370  0.0083  6   PHE   A CA  
59   C C   . PHE   A 6   ? 0.2853 0.3495 0.2451 -0.1028 0.0598  0.0078  6   PHE   A C   
60   O O   . PHE   A 6   ? 0.2893 0.3630 0.2868 -0.1105 0.0563  0.0194  6   PHE   A O   
61   C CB  . PHE   A 6   ? 0.2786 0.3140 0.1834 -0.0967 0.0317  0.0180  6   PHE   A CB  
62   C CG  . PHE   A 6   ? 0.2693 0.2910 0.1875 -0.0827 0.0204  0.0214  6   PHE   A CG  
63   C CD1 . PHE   A 6   ? 0.2631 0.2795 0.1944 -0.0735 0.0142  0.0278  6   PHE   A CD1 
64   C CD2 . PHE   A 6   ? 0.2753 0.2911 0.2084 -0.0669 0.0273  0.0289  6   PHE   A CD2 
65   C CE1 . PHE   A 6   ? 0.2613 0.2773 0.2146 -0.0674 0.0154  0.0311  6   PHE   A CE1 
66   C CE2 . PHE   A 6   ? 0.2731 0.2872 0.2309 -0.0617 0.0239  0.0234  6   PHE   A CE2 
67   C CZ  . PHE   A 6   ? 0.2672 0.2800 0.2207 -0.0664 0.0092  0.0195  6   PHE   A CZ  
77   N N   A SER   A 7   ? 0.2759 0.3382 0.2217 -0.1061 0.0798  0.0020  7   SER   A N   
78   N N   B SER   A 7   ? 0.2807 0.3425 0.2526 -0.0881 0.0564  0.0022  7   SER   A N   
79   C CA  A SER   A 7   ? 0.2833 0.3437 0.2373 -0.0941 0.0774  -0.0175 7   SER   A CA  
80   C CA  B SER   A 7   ? 0.2790 0.3345 0.2678 -0.0681 0.0483  -0.0043 7   SER   A CA  
81   C C   A SER   A 7   ? 0.2666 0.3076 0.2164 -0.0946 0.0844  -0.0208 7   SER   A C   
82   C C   B SER   A 7   ? 0.2697 0.3119 0.2531 -0.0541 0.0474  -0.0060 7   SER   A C   
83   O O   A SER   A 7   ? 0.2756 0.2977 0.2247 -0.0957 0.0865  -0.0256 7   SER   A O   
84   O O   B SER   A 7   ? 0.2753 0.3112 0.2539 -0.0503 0.0471  -0.0087 7   SER   A O   
85   C CB  A SER   A 7   ? 0.3028 0.3789 0.2760 -0.0823 0.0759  -0.0183 7   SER   A CB  
86   C CB  B SER   A 7   ? 0.2854 0.3446 0.2925 -0.0618 0.0455  -0.0031 7   SER   A CB  
87   O OG  A SER   A 7   ? 0.3235 0.4027 0.3120 -0.0698 0.0744  -0.0183 7   SER   A OG  
88   O OG  B SER   A 7   ? 0.2918 0.3502 0.3142 -0.0561 0.0434  -0.0001 7   SER   A OG  
99   N N   A GLY   A 8   ? 0.2457 0.2841 0.2165 -0.0871 0.0812  -0.0291 8   GLY   A N   
100  N N   B GLY   A 8   ? 0.2561 0.2913 0.2402 -0.0422 0.0455  -0.0051 8   GLY   A N   
101  C CA  A GLY   A 8   ? 0.2343 0.2641 0.2293 -0.0621 0.0769  -0.0286 8   GLY   A CA  
102  C CA  B GLY   A 8   ? 0.2445 0.2697 0.2335 -0.0302 0.0363  -0.0022 8   GLY   A CA  
103  C C   A GLY   A 8   ? 0.2081 0.2413 0.2284 -0.0474 0.0713  -0.0236 8   GLY   A C   
104  C C   B GLY   A 8   ? 0.2282 0.2485 0.2163 -0.0211 0.0254  0.0034  8   GLY   A C   
105  O O   A GLY   A 8   ? 0.2101 0.2414 0.2534 -0.0305 0.0647  -0.0415 8   GLY   A O   
106  O O   B GLY   A 8   ? 0.2302 0.2480 0.2265 -0.0151 0.0211  -0.0025 8   GLY   A O   
113  N N   A TYR   A 9   ? 0.1834 0.2185 0.2128 -0.0400 0.0612  -0.0121 9   TYR   A N   
114  N N   B TYR   A 9   ? 0.2132 0.2297 0.2039 -0.0167 0.0194  0.0160  9   TYR   A N   
115  C CA  A TYR   A 9   ? 0.1741 0.1991 0.1905 -0.0374 0.0425  -0.0056 9   TYR   A CA  
116  C CA  B TYR   A 9   ? 0.2031 0.2155 0.1940 -0.0153 0.0228  0.0176  9   TYR   A CA  
117  C C   A TYR   A 9   ? 0.1770 0.1802 0.1755 -0.0250 0.0372  0.0197  9   TYR   A C   
118  C C   B TYR   A 9   ? 0.1936 0.2054 0.1885 -0.0065 0.0231  0.0178  9   TYR   A C   
119  O O   A TYR   A 9   ? 0.1991 0.1962 0.1959 -0.0197 0.0434  0.0153  9   TYR   A O   
120  O O   B TYR   A 9   ? 0.1903 0.2069 0.1957 0.0004  0.0289  0.0188  9   TYR   A O   
121  C CB  A TYR   A 9   ? 0.1689 0.2156 0.1860 -0.0317 0.0380  -0.0129 9   TYR   A CB  
122  C CB  B TYR   A 9   ? 0.2041 0.2187 0.1980 -0.0185 0.0230  0.0127  9   TYR   A CB  
123  C CG  A TYR   A 9   ? 0.1658 0.2268 0.1874 -0.0203 0.0428  -0.0114 9   TYR   A CG  
124  C CG  B TYR   A 9   ? 0.2043 0.2213 0.2003 -0.0213 0.0226  0.0068  9   TYR   A CG  
125  C CD1 A TYR   A 9   ? 0.1672 0.2309 0.1924 -0.0359 0.0450  -0.0058 9   TYR   A CD1 
126  C CD1 B TYR   A 9   ? 0.2082 0.2250 0.2094 -0.0282 0.0235  0.0052  9   TYR   A CD1 
127  C CD2 A TYR   A 9   ? 0.1581 0.2241 0.1844 -0.0150 0.0335  0.0083  9   TYR   A CD2 
128  C CD2 B TYR   A 9   ? 0.2001 0.2176 0.1905 -0.0223 0.0172  0.0058  9   TYR   A CD2 
129  C CE1 A TYR   A 9   ? 0.1729 0.2409 0.2102 -0.0378 0.0405  -0.0103 9   TYR   A CE1 
130  C CE1 B TYR   A 9   ? 0.2074 0.2267 0.2107 -0.0307 0.0222  0.0001  9   TYR   A CE1 
131  C CE2 A TYR   A 9   ? 0.1626 0.2303 0.1876 -0.0176 0.0411  -0.0006 9   TYR   A CE2 
132  C CE2 B TYR   A 9   ? 0.1995 0.2193 0.1980 -0.0238 0.0230  0.0017  9   TYR   A CE2 
133  C CZ  A TYR   A 9   ? 0.1654 0.2444 0.2140 -0.0383 0.0542  -0.0062 9   TYR   A CZ  
134  C CZ  B TYR   A 9   ? 0.2036 0.2258 0.2111 -0.0307 0.0300  -0.0005 9   TYR   A CZ  
135  O OH  A TYR   A 9   ? 0.1748 0.2617 0.2429 -0.0477 0.0553  -0.0120 9   TYR   A OH  
136  O OH  B TYR   A 9   ? 0.2111 0.2333 0.2261 -0.0340 0.0409  0.0015  9   TYR   A OH  
155  N N   A LEU   A 10  ? 0.1718 0.1655 0.1841 -0.0282 0.0272  0.0240  10  LEU   A N   
156  N N   B LEU   A 10  ? 0.1932 0.1985 0.1842 -0.0080 0.0180  0.0145  10  LEU   A N   
157  C CA  A LEU   A 10  ? 0.1663 0.1596 0.1945 -0.0258 0.0199  0.0323  10  LEU   A CA  
158  C CA  B LEU   A 10  ? 0.1924 0.1945 0.1747 -0.0079 0.0140  0.0164  10  LEU   A CA  
159  C C   A LEU   A 10  ? 0.1659 0.1571 0.1903 -0.0226 0.0179  0.0401  10  LEU   A C   
160  C C   B LEU   A 10  ? 0.1917 0.1795 0.1751 -0.0095 0.0056  0.0202  10  LEU   A C   
161  O O   A LEU   A 10  ? 0.1574 0.1536 0.1954 -0.0230 0.0350  0.0448  10  LEU   A O   
162  O O   B LEU   A 10  ? 0.1885 0.1735 0.1805 -0.0117 0.0072  0.0262  10  LEU   A O   
163  C CB  A LEU   A 10  ? 0.1652 0.1693 0.2252 -0.0206 0.0021  0.0494  10  LEU   A CB  
164  C CB  B LEU   A 10  ? 0.1924 0.2052 0.1842 -0.0106 0.0093  0.0180  10  LEU   A CB  
165  C CG  A LEU   A 10  ? 0.1795 0.1814 0.2627 -0.0006 -0.0250 0.0549  10  LEU   A CG  
166  C CG  B LEU   A 10  ? 0.1967 0.2223 0.1922 -0.0168 0.0060  0.0192  10  LEU   A CG  
167  C CD1 A LEU   A 10  ? 0.2019 0.1950 0.2910 -0.0152 -0.0146 0.0616  10  LEU   A CD1 
168  C CD1 B LEU   A 10  ? 0.1999 0.2326 0.2054 -0.0130 0.0044  0.0113  10  LEU   A CD1 
169  C CD2 A LEU   A 10  ? 0.2027 0.2078 0.2773 -0.0022 -0.0212 0.0500  10  LEU   A CD2 
170  C CD2 B LEU   A 10  ? 0.1924 0.2222 0.1848 -0.0245 0.0115  0.0341  10  LEU   A CD2 
193  N N   A LYS   A 11  ? 0.1699 0.1587 0.1901 -0.0220 0.0211  0.0389  11  LYS   A N   
194  N N   B LYS   A 11  ? 0.1937 0.1703 0.1709 -0.0157 -0.0064 0.0197  11  LYS   A N   
195  C CA  A LYS   A 11  ? 0.1625 0.1560 0.2001 -0.0317 0.0127  0.0421  11  LYS   A CA  
196  C CA  B LYS   A 11  ? 0.1891 0.1551 0.1673 -0.0218 -0.0131 0.0160  11  LYS   A CA  
197  C C   A LYS   A 11  ? 0.1548 0.1587 0.2010 -0.0331 0.0211  0.0330  11  LYS   A C   
198  C C   B LYS   A 11  ? 0.1741 0.1472 0.1591 -0.0229 -0.0112 0.0134  11  LYS   A C   
199  O O   A LYS   A 11  ? 0.1682 0.1927 0.2266 -0.0518 0.0360  0.0100  11  LYS   A O   
200  O O   B LYS   A 11  ? 0.1688 0.1426 0.1673 -0.0197 -0.0089 0.0039  11  LYS   A O   
201  C CB  A LYS   A 11  ? 0.1707 0.1539 0.1908 -0.0285 0.0110  0.0324  11  LYS   A CB  
202  C CB  B LYS   A 11  ? 0.1966 0.1424 0.1687 -0.0268 -0.0137 0.0139  11  LYS   A CB  
203  C CG  A LYS   A 11  ? 0.1849 0.1607 0.2031 -0.0251 0.0170  0.0380  11  LYS   A CG  
204  C CG  B LYS   A 11  ? 0.2025 0.1357 0.1651 -0.0290 -0.0081 0.0261  11  LYS   A CG  
205  C CD  A LYS   A 11  ? 0.1917 0.1734 0.2049 -0.0167 0.0136  0.0406  11  LYS   A CD  
206  C CD  B LYS   A 11  ? 0.2063 0.1323 0.1668 -0.0312 -0.0017 0.0357  11  LYS   A CD  
207  C CE  A LYS   A 11  ? 0.1960 0.1776 0.2040 -0.0108 0.0024  0.0391  11  LYS   A CE  
208  C CE  B LYS   A 11  ? 0.2065 0.1294 0.1667 -0.0337 0.0015  0.0403  11  LYS   A CE  
209  N NZ  A LYS   A 11  ? 0.1923 0.1806 0.2169 0.0010  -0.0026 0.0354  11  LYS   A NZ  
210  N NZ  B LYS   A 11  ? 0.2048 0.1308 0.1798 -0.0342 0.0048  0.0334  11  LYS   A NZ  
237  N N   A LEU   A 12  ? 0.1401 0.1543 0.1884 -0.0282 0.0183  0.0292  12  LEU   A N   
238  N N   B LEU   A 12  ? 0.1644 0.1532 0.1541 -0.0184 -0.0037 0.0147  12  LEU   A N   
239  C CA  A LEU   A 12  ? 0.1422 0.1691 0.1843 -0.0164 0.0090  0.0325  12  LEU   A CA  
240  C CA  B LEU   A 12  ? 0.1608 0.1577 0.1454 -0.0193 0.0143  0.0204  12  LEU   A CA  
241  C C   A LEU   A 12  ? 0.1541 0.1638 0.1839 -0.0233 0.0044  0.0392  12  LEU   A C   
242  C C   B LEU   A 12  ? 0.1561 0.1586 0.1492 -0.0190 0.0185  0.0201  12  LEU   A C   
243  O O   A LEU   A 12  ? 0.1579 0.1662 0.1964 -0.0180 0.0098  0.0264  12  LEU   A O   
244  O O   B LEU   A 12  ? 0.1596 0.1599 0.1518 -0.0139 0.0141  0.0223  12  LEU   A O   
245  C CB  A LEU   A 12  ? 0.1586 0.1669 0.2073 -0.0108 0.0043  0.0380  12  LEU   A CB  
246  C CB  B LEU   A 12  ? 0.1673 0.1595 0.1584 -0.0166 0.0243  0.0218  12  LEU   A CB  
247  C CG  A LEU   A 12  ? 0.1619 0.1692 0.2409 -0.0043 0.0085  0.0417  12  LEU   A CG  
248  C CG  B LEU   A 12  ? 0.1698 0.1599 0.1768 -0.0133 0.0280  0.0236  12  LEU   A CG  
249  C CD1 A LEU   A 12  ? 0.1843 0.1629 0.2425 0.0000  0.0164  0.0484  12  LEU   A CD1 
250  C CD1 B LEU   A 12  ? 0.1718 0.1622 0.1726 -0.0139 0.0297  0.0153  12  LEU   A CD1 
251  C CD2 A LEU   A 12  ? 0.1636 0.1780 0.2671 -0.0038 0.0005  0.0457  12  LEU   A CD2 
252  C CD2 B LEU   A 12  ? 0.1709 0.1634 0.1887 -0.0164 0.0245  0.0307  12  LEU   A CD2 
275  N N   A THR   A 13  ? 0.1528 0.1524 0.1991 -0.0177 0.0003  0.0361  13  THR   A N   
276  N N   B THR   A 13  ? 0.1538 0.1626 0.1580 -0.0194 0.0135  0.0134  13  THR   A N   
277  C CA  A THR   A 13  ? 0.1563 0.1592 0.1967 -0.0124 0.0045  0.0292  13  THR   A CA  
278  C CA  B THR   A 13  ? 0.1562 0.1691 0.1640 -0.0201 0.0195  0.0174  13  THR   A CA  
279  C C   A THR   A 13  ? 0.1486 0.1550 0.2050 -0.0165 0.0020  0.0326  13  THR   A C   
280  C C   B THR   A 13  ? 0.1600 0.1753 0.1726 -0.0281 0.0193  0.0197  13  THR   A C   
281  O O   A THR   A 13  ? 0.1441 0.1581 0.2062 -0.0103 0.0029  0.0334  13  THR   A O   
282  O O   B THR   A 13  ? 0.1671 0.1803 0.1662 -0.0281 0.0218  0.0290  13  THR   A O   
283  C CB  A THR   A 13  ? 0.1620 0.1792 0.2164 -0.0155 0.0030  0.0329  13  THR   A CB  
284  C CB  B THR   A 13  ? 0.1495 0.1736 0.1710 -0.0109 0.0231  0.0223  13  THR   A CB  
285  O OG1 A THR   A 13  ? 0.1536 0.1640 0.2246 -0.0154 -0.0121 0.0454  13  THR   A OG1 
286  O OG1 B THR   A 13  ? 0.1371 0.1718 0.1812 -0.0094 0.0386  0.0380  13  THR   A OG1 
287  C CG2 A THR   A 13  ? 0.1651 0.1993 0.2386 -0.0239 -0.0016 0.0206  13  THR   A CG2 
288  C CG2 B THR   A 13  ? 0.1519 0.1808 0.1817 -0.0050 0.0223  0.0104  13  THR   A CG2 
303  N N   A ASP   A 14  ? 0.1556 0.1602 0.2266 -0.0215 0.0062  0.0457  14  ASP   A N   
304  N N   B ASP   A 14  ? 0.1590 0.1820 0.1974 -0.0344 0.0119  0.0216  14  ASP   A N   
305  C CA  A ASP   A 14  ? 0.1556 0.1798 0.2505 -0.0183 -0.0143 0.0646  14  ASP   A CA  
306  C CA  B ASP   A 14  ? 0.1571 0.1877 0.2156 -0.0364 0.0005  0.0368  14  ASP   A CA  
307  C C   A ASP   A 14  ? 0.1553 0.1845 0.2163 -0.0176 -0.0247 0.0599  14  ASP   A C   
308  C C   B ASP   A 14  ? 0.1530 0.1787 0.2078 -0.0343 -0.0060 0.0533  14  ASP   A C   
309  O O   A ASP   A 14  ? 0.1773 0.1932 0.2318 -0.0253 -0.0218 0.0550  14  ASP   A O   
310  O O   B ASP   A 14  ? 0.1501 0.1740 0.2130 -0.0404 -0.0107 0.0638  14  ASP   A O   
311  C CB  A ASP   A 14  ? 0.1687 0.2130 0.3218 -0.0229 -0.0127 0.0859  14  ASP   A CB  
312  C CB  B ASP   A 14  ? 0.1678 0.2063 0.2523 -0.0374 -0.0055 0.0357  14  ASP   A CB  
313  C CG  A ASP   A 14  ? 0.1895 0.2695 0.4114 -0.0282 -0.0031 0.0758  14  ASP   A CG  
314  C CG  B ASP   A 14  ? 0.1701 0.2265 0.2858 -0.0451 -0.0052 0.0340  14  ASP   A CG  
315  O OD1 A ASP   A 14  ? 0.2044 0.2943 0.4340 -0.0079 -0.0224 0.0788  14  ASP   A OD1 
316  O OD1 B ASP   A 14  ? 0.1731 0.2267 0.2915 -0.0489 0.0061  0.0443  14  ASP   A OD1 
317  O OD2 A ASP   A 14  ? 0.2130 0.3107 0.4594 -0.0339 -0.0033 0.0530  14  ASP   A OD2 
318  O OD2 B ASP   A 14  ? 0.1716 0.2451 0.3039 -0.0445 -0.0165 0.0265  14  ASP   A OD2 
327  N N   . ASN   A 15  ? 0.1568 0.1777 0.2058 -0.0318 -0.0051 0.0538  15  ASN   A N   
328  C CA  . ASN   A 15  ? 0.1597 0.1773 0.2161 -0.0244 -0.0097 0.0390  15  ASN   A CA  
329  C C   . ASN   A 15  ? 0.1599 0.1712 0.2305 -0.0311 0.0023  0.0434  15  ASN   A C   
330  O O   . ASN   A 15  ? 0.1707 0.1649 0.2837 -0.0228 -0.0196 0.0395  15  ASN   A O   
331  C CB  . ASN   A 15  ? 0.1558 0.1710 0.2103 -0.0197 -0.0068 0.0351  15  ASN   A CB  
332  C CG  . ASN   A 15  ? 0.1550 0.1753 0.2205 -0.0151 0.0042  0.0198  15  ASN   A CG  
333  O OD1 . ASN   A 15  ? 0.1712 0.1796 0.2386 -0.0279 0.0044  0.0265  15  ASN   A OD1 
334  N ND2 . ASN   A 15  ? 0.1585 0.1878 0.2116 -0.0202 0.0079  0.0210  15  ASN   A ND2 
342  N N   . VAL   A 16  ? 0.1612 0.1689 0.2119 -0.0235 -0.0001 0.0458  16  VAL   A N   
343  C CA  . VAL   A 16  ? 0.1589 0.1648 0.1961 -0.0169 0.0068  0.0487  16  VAL   A CA  
344  C C   . VAL   A 16  ? 0.1522 0.1640 0.1923 -0.0288 0.0069  0.0396  16  VAL   A C   
345  O O   . VAL   A 16  ? 0.1527 0.1627 0.2109 -0.0225 0.0135  0.0316  16  VAL   A O   
346  C CB  . VAL   A 16  ? 0.1698 0.1808 0.1976 -0.0026 0.0225  0.0534  16  VAL   A CB  
347  C CG1 . VAL   A 16  ? 0.1700 0.1919 0.2129 0.0068  0.0258  0.0548  16  VAL   A CG1 
348  C CG2 . VAL   A 16  ? 0.1768 0.1945 0.2100 0.0085  0.0412  0.0474  16  VAL   A CG2 
358  N N   A TYR   A 17  ? 0.1544 0.1600 0.1983 -0.0290 0.0200  0.0386  17  TYR   A N   
359  N N   B TYR   A 17  ? 0.1575 0.1646 0.1807 -0.0232 0.0131  0.0267  17  TYR   A N   
360  C CA  A TYR   A 17  ? 0.1595 0.1604 0.1857 -0.0303 0.0127  0.0364  17  TYR   A CA  
361  C CA  B TYR   A 17  ? 0.1644 0.1663 0.1653 -0.0199 0.0130  0.0162  17  TYR   A CA  
362  C C   A TYR   A 17  ? 0.1635 0.1584 0.1981 -0.0235 0.0143  0.0377  17  TYR   A C   
363  C C   B TYR   A 17  ? 0.1637 0.1608 0.1502 -0.0214 0.0165  0.0066  17  TYR   A C   
364  O O   A TYR   A 17  ? 0.1505 0.1571 0.1939 -0.0275 0.0058  0.0429  17  TYR   A O   
365  O O   B TYR   A 17  ? 0.1601 0.1520 0.1497 -0.0200 0.0256  0.0019  17  TYR   A O   
366  C CB  A TYR   A 17  ? 0.1705 0.1665 0.1799 -0.0350 -0.0040 0.0380  17  TYR   A CB  
367  C CB  B TYR   A 17  ? 0.1744 0.1733 0.1727 -0.0144 0.0073  0.0154  17  TYR   A CB  
368  C CG  A TYR   A 17  ? 0.2014 0.1786 0.1991 -0.0431 -0.0159 0.0389  17  TYR   A CG  
369  C CG  B TYR   A 17  ? 0.1888 0.1828 0.1878 -0.0080 0.0031  0.0134  17  TYR   A CG  
370  C CD1 A TYR   A 17  ? 0.2147 0.1831 0.2137 -0.0359 -0.0332 0.0467  17  TYR   A CD1 
371  C CD1 B TYR   A 17  ? 0.1958 0.1873 0.1969 0.0014  -0.0025 0.0168  17  TYR   A CD1 
372  C CD2 A TYR   A 17  ? 0.2215 0.1854 0.1804 -0.0645 -0.0117 0.0459  17  TYR   A CD2 
373  C CD2 B TYR   A 17  ? 0.1980 0.1899 0.1903 -0.0098 0.0041  0.0124  17  TYR   A CD2 
374  C CE1 A TYR   A 17  ? 0.2267 0.1855 0.2207 -0.0433 -0.0459 0.0412  17  TYR   A CE1 
375  C CE1 B TYR   A 17  ? 0.2018 0.1928 0.2030 0.0032  -0.0059 0.0204  17  TYR   A CE1 
376  C CE2 A TYR   A 17  ? 0.2345 0.1879 0.1983 -0.0641 -0.0254 0.0318  17  TYR   A CE2 
377  C CE2 B TYR   A 17  ? 0.2027 0.1949 0.1960 -0.0062 0.0026  0.0133  17  TYR   A CE2 
378  C CZ  A TYR   A 17  ? 0.2385 0.1867 0.2016 -0.0522 -0.0475 0.0409  17  TYR   A CZ  
379  C CZ  B TYR   A 17  ? 0.2021 0.1965 0.1987 -0.0009 -0.0039 0.0207  17  TYR   A CZ  
380  O OH  A TYR   A 17  ? 0.2560 0.1876 0.1985 -0.0520 -0.0465 0.0364  17  TYR   A OH  
381  O OH  B TYR   A 17  ? 0.1992 0.2007 0.1984 -0.0010 -0.0020 0.0250  17  TYR   A OH  
400  N N   A ILE   A 18  ? 0.1621 0.1635 0.1906 -0.0241 0.0175  0.0415  18  ILE   A N   
401  N N   B ILE   A 18  ? 0.1628 0.1669 0.1315 -0.0247 0.0116  0.0068  18  ILE   A N   
402  C CA  A ILE   A 18  ? 0.1615 0.1609 0.1855 -0.0229 0.0183  0.0283  18  ILE   A CA  
403  C CA  B ILE   A 18  ? 0.1647 0.1703 0.1302 -0.0195 0.0159  0.0020  18  ILE   A CA  
404  C C   A ILE   A 18  ? 0.1633 0.1655 0.1805 -0.0334 0.0153  0.0322  18  ILE   A C   
405  C C   B ILE   A 18  ? 0.1653 0.1846 0.1202 -0.0166 0.0111  0.0004  18  ILE   A C   
406  O O   A ILE   A 18  ? 0.1601 0.1805 0.1813 -0.0351 0.0213  0.0403  18  ILE   A O   
407  O O   B ILE   A 18  ? 0.1628 0.1898 0.1369 -0.0219 0.0149  0.0053  18  ILE   A O   
408  C CB  A ILE   A 18  ? 0.1708 0.1567 0.1720 -0.0035 0.0182  0.0369  18  ILE   A CB  
409  C CB  B ILE   A 18  ? 0.1627 0.1623 0.1264 -0.0199 0.0280  0.0093  18  ILE   A CB  
410  C CG1 A ILE   A 18  ? 0.1801 0.1608 0.1544 0.0052  0.0219  0.0242  18  ILE   A CG1 
411  C CG1 B ILE   A 18  ? 0.1662 0.1630 0.1425 -0.0234 0.0381  0.0176  18  ILE   A CG1 
412  C CG2 A ILE   A 18  ? 0.1755 0.1590 0.1892 -0.0017 0.0148  0.0320  18  ILE   A CG2 
413  C CG2 B ILE   A 18  ? 0.1679 0.1654 0.1188 -0.0241 0.0197  0.0108  18  ILE   A CG2 
414  C CD1 A ILE   A 18  ? 0.1989 0.1760 0.1788 0.0172  0.0213  0.0356  18  ILE   A CD1 
415  C CD1 B ILE   A 18  ? 0.1690 0.1657 0.1607 -0.0217 0.0453  0.0092  18  ILE   A CD1 
438  N N   A LYS   A 19  ? 0.1593 0.1696 0.1797 -0.0281 0.0363  0.0229  19  LYS   A N   
439  N N   B LYS   A 19  ? 0.1694 0.1899 0.1156 -0.0039 0.0138  -0.0160 19  LYS   A N   
440  C CA  A LYS   A 19  ? 0.1745 0.1836 0.1808 -0.0258 0.0315  0.0202  19  LYS   A CA  
441  C CA  B LYS   A 19  ? 0.1801 0.1987 0.1363 0.0006  0.0189  -0.0245 19  LYS   A CA  
442  C C   A LYS   A 19  ? 0.1642 0.1763 0.1994 -0.0162 0.0271  0.0355  19  LYS   A C   
443  C C   B LYS   A 19  ? 0.1879 0.2007 0.1462 0.0059  0.0212  -0.0209 19  LYS   A C   
444  O O   A LYS   A 19  ? 0.1583 0.1723 0.2067 -0.0082 0.0214  0.0397  19  LYS   A O   
445  O O   B LYS   A 19  ? 0.1916 0.1998 0.1554 0.0017  0.0161  -0.0137 19  LYS   A O   
446  C CB  A LYS   A 19  ? 0.1866 0.2080 0.1899 -0.0345 0.0394  0.0221  19  LYS   A CB  
447  C CB  B LYS   A 19  ? 0.1822 0.2055 0.1445 0.0012  0.0291  -0.0380 19  LYS   A CB  
448  C CG  A LYS   A 19  ? 0.2223 0.2317 0.2037 -0.0364 0.0336  0.0016  19  LYS   A CG  
449  C CG  B LYS   A 19  ? 0.1925 0.2140 0.1532 -0.0010 0.0309  -0.0341 19  LYS   A CG  
450  C CD  A LYS   A 19  ? 0.2517 0.2557 0.2264 -0.0356 0.0383  0.0008  19  LYS   A CD  
451  C CD  B LYS   A 19  ? 0.2041 0.2222 0.1650 -0.0063 0.0299  -0.0220 19  LYS   A CD  
452  C CE  A LYS   A 19  ? 0.2742 0.2659 0.2379 -0.0450 0.0297  -0.0056 19  LYS   A CE  
453  C CE  B LYS   A 19  ? 0.2154 0.2293 0.1794 -0.0106 0.0210  -0.0166 19  LYS   A CE  
454  N NZ  A LYS   A 19  ? 0.2809 0.2742 0.2329 -0.0571 0.0350  -0.0199 19  LYS   A NZ  
455  N NZ  B LYS   A 19  ? 0.2223 0.2318 0.1860 -0.0170 0.0259  -0.0214 19  LYS   A NZ  
482  N N   A ASN   A 20  ? 0.1689 0.1835 0.2190 -0.0194 0.0315  0.0494  20  ASN   A N   
483  N N   B ASN   A 20  ? 0.1985 0.2075 0.1648 0.0106  0.0259  -0.0249 20  ASN   A N   
484  C CA  A ASN   A 20  ? 0.1805 0.2067 0.2403 0.0052  0.0507  0.0445  20  ASN   A CA  
485  C CA  B ASN   A 20  ? 0.2085 0.2189 0.1836 0.0103  0.0227  -0.0262 20  ASN   A CA  
486  C C   A ASN   A 20  ? 0.2028 0.2026 0.2448 -0.0052 0.0789  0.0213  20  ASN   A C   
487  C C   B ASN   A 20  ? 0.2154 0.2167 0.1842 0.0005  0.0265  -0.0301 20  ASN   A C   
488  O O   A ASN   A 20  ? 0.2292 0.2090 0.2647 -0.0252 0.0848  0.0005  20  ASN   A O   
489  O O   B ASN   A 20  ? 0.2247 0.2220 0.1797 -0.0100 0.0259  -0.0370 20  ASN   A O   
490  C CB  A ASN   A 20  ? 0.1849 0.2260 0.2573 0.0205  0.0571  0.0703  20  ASN   A CB  
491  C CB  B ASN   A 20  ? 0.2123 0.2286 0.1947 0.0184  0.0198  -0.0275 20  ASN   A CB  
492  C CG  A ASN   A 20  ? 0.2002 0.2394 0.2943 0.0442  0.0662  0.0743  20  ASN   A CG  
493  C CG  B ASN   A 20  ? 0.2189 0.2353 0.2140 0.0243  0.0194  -0.0244 20  ASN   A CG  
494  O OD1 A ASN   A 20  ? 0.2291 0.2489 0.3457 0.0595  0.0797  0.0561  20  ASN   A OD1 
495  O OD1 B ASN   A 20  ? 0.2232 0.2392 0.2153 0.0267  0.0081  -0.0222 20  ASN   A OD1 
496  N ND2 A ASN   A 20  ? 0.2012 0.2397 0.3076 0.0453  0.0598  0.0864  20  ASN   A ND2 
497  N ND2 B ASN   A 20  ? 0.2213 0.2354 0.2225 0.0282  0.0252  -0.0233 20  ASN   A ND2 
510  N N   A ALA   A 21  ? 0.2057 0.1993 0.2415 -0.0052 0.0689  0.0096  21  ALA   A N   
511  N N   B ALA   A 21  ? 0.2171 0.2114 0.1958 -0.0022 0.0273  -0.0290 21  ALA   A N   
512  C CA  A ALA   A 21  ? 0.2127 0.1966 0.2472 -0.0057 0.0601  0.0127  21  ALA   A CA  
513  C CA  B ALA   A 21  ? 0.2194 0.2059 0.2030 -0.0046 0.0287  -0.0235 21  ALA   A CA  
514  C C   A ALA   A 21  ? 0.1974 0.1964 0.2426 -0.0071 0.0495  0.0193  21  ALA   A C   
515  C C   B ALA   A 21  ? 0.2163 0.2024 0.2024 -0.0071 0.0443  -0.0137 21  ALA   A C   
516  O O   A ALA   A 21  ? 0.1868 0.1994 0.2386 0.0077  0.0399  0.0264  21  ALA   A O   
517  O O   B ALA   A 21  ? 0.2192 0.2006 0.2051 -0.0071 0.0497  -0.0126 21  ALA   A O   
518  C CB  A ALA   A 21  ? 0.2356 0.2130 0.2513 -0.0140 0.0561  0.0192  21  ALA   A CB  
519  C CB  B ALA   A 21  ? 0.2254 0.2092 0.2165 -0.0068 0.0231  -0.0249 21  ALA   A CB  
530  N N   A ASP   A 22  ? 0.1981 0.1905 0.2597 -0.0128 0.0541  0.0270  22  ASP   A N   
531  N N   B ASP   A 22  ? 0.2091 0.2002 0.1997 -0.0088 0.0553  -0.0044 22  ASP   A N   
532  C CA  A ASP   A 22  ? 0.2040 0.1941 0.2695 -0.0102 0.0459  0.0480  22  ASP   A CA  
533  C CA  B ASP   A 22  ? 0.2048 0.2038 0.2130 -0.0121 0.0511  0.0022  22  ASP   A CA  
534  C C   A ASP   A 22  ? 0.1915 0.1993 0.2241 -0.0075 0.0526  0.0474  22  ASP   A C   
535  C C   B ASP   A 22  ? 0.1890 0.1939 0.1907 -0.0198 0.0540  0.0006  22  ASP   A C   
536  O O   A ASP   A 22  ? 0.2033 0.2059 0.2254 -0.0061 0.0496  0.0445  22  ASP   A O   
537  O O   B ASP   A 22  ? 0.1840 0.1855 0.1910 -0.0214 0.0649  -0.0042 22  ASP   A O   
538  C CB  A ASP   A 22  ? 0.2227 0.1979 0.3280 -0.0124 0.0451  0.0378  22  ASP   A CB  
539  C CB  B ASP   A 22  ? 0.2141 0.2142 0.2512 -0.0081 0.0460  0.0024  22  ASP   A CB  
540  C CG  A ASP   A 22  ? 0.2465 0.2072 0.3923 -0.0174 0.0195  0.0398  22  ASP   A CG  
541  C CG  B ASP   A 22  ? 0.2206 0.2175 0.2814 -0.0057 0.0478  0.0023  22  ASP   A CG  
542  O OD1 A ASP   A 22  ? 0.2460 0.2125 0.4167 -0.0311 0.0012  0.0548  22  ASP   A OD1 
543  O OD1 B ASP   A 22  ? 0.2240 0.2122 0.2784 -0.0031 0.0575  -0.0025 22  ASP   A OD1 
544  O OD2 A ASP   A 22  ? 0.2740 0.2185 0.4362 -0.0070 0.0134  0.0217  22  ASP   A OD2 
545  O OD2 B ASP   A 22  ? 0.2213 0.2273 0.3022 -0.0065 0.0452  0.0012  22  ASP   A OD2 
554  N N   A ILE   A 23  ? 0.1914 0.1954 0.2039 -0.0009 0.0454  0.0318  23  ILE   A N   
555  N N   B ILE   A 23  ? 0.1840 0.1950 0.1860 -0.0166 0.0436  -0.0019 23  ILE   A N   
556  C CA  A ILE   A 23  ? 0.1889 0.1873 0.1786 -0.0045 0.0425  0.0362  23  ILE   A CA  
557  C CA  B ILE   A 23  ? 0.1781 0.1978 0.1723 -0.0176 0.0309  0.0011  23  ILE   A CA  
558  C C   A ILE   A 23  ? 0.1905 0.1990 0.1828 -0.0023 0.0637  0.0236  23  ILE   A C   
559  C C   B ILE   A 23  ? 0.1824 0.2023 0.1806 -0.0232 0.0329  -0.0101 23  ILE   A C   
560  O O   A ILE   A 23  ? 0.2017 0.2014 0.1945 -0.0017 0.0567  0.0084  23  ILE   A O   
561  O O   B ILE   A 23  ? 0.1829 0.2007 0.1746 -0.0205 0.0336  -0.0163 23  ILE   A O   
562  C CB  A ILE   A 23  ? 0.1974 0.1805 0.1632 -0.0019 0.0368  0.0277  23  ILE   A CB  
563  C CB  B ILE   A 23  ? 0.1728 0.1931 0.1499 -0.0109 0.0202  0.0109  23  ILE   A CB  
564  C CG1 A ILE   A 23  ? 0.2021 0.1749 0.1682 -0.0020 0.0268  0.0061  23  ILE   A CG1 
565  C CG1 B ILE   A 23  ? 0.1705 0.1898 0.1466 -0.0123 0.0069  0.0013  23  ILE   A CG1 
566  C CG2 A ILE   A 23  ? 0.1989 0.1879 0.1740 0.0007  0.0463  0.0304  23  ILE   A CG2 
567  C CG2 B ILE   A 23  ? 0.1738 0.1913 0.1512 -0.0046 0.0204  0.0192  23  ILE   A CG2 
568  C CD1 A ILE   A 23  ? 0.2172 0.1704 0.1689 -0.0009 0.0130  0.0044  23  ILE   A CD1 
569  C CD1 B ILE   A 23  ? 0.1654 0.1907 0.1488 -0.0090 0.0006  -0.0086 23  ILE   A CD1 
592  N N   A VAL   A 24  ? 0.1935 0.2099 0.1951 -0.0112 0.0577  0.0125  24  VAL   A N   
593  N N   B VAL   A 24  ? 0.1860 0.2076 0.1984 -0.0322 0.0375  -0.0122 24  VAL   A N   
594  C CA  A VAL   A 24  ? 0.2111 0.2190 0.2275 -0.0203 0.0584  0.0055  24  VAL   A CA  
595  C CA  B VAL   A 24  ? 0.2000 0.2162 0.2179 -0.0351 0.0404  -0.0066 24  VAL   A CA  
596  C C   A VAL   A 24  ? 0.2290 0.2317 0.2383 -0.0367 0.0617  -0.0125 24  VAL   A C   
597  C C   B VAL   A 24  ? 0.2087 0.2309 0.2199 -0.0380 0.0510  -0.0134 24  VAL   A C   
598  O O   A VAL   A 24  ? 0.2463 0.2329 0.2371 -0.0408 0.0608  -0.0228 24  VAL   A O   
599  O O   B VAL   A 24  ? 0.2114 0.2354 0.2220 -0.0331 0.0557  -0.0081 24  VAL   A O   
600  C CB  A VAL   A 24  ? 0.2134 0.2303 0.2672 -0.0189 0.0597  0.0101  24  VAL   A CB  
601  C CB  B VAL   A 24  ? 0.2043 0.2142 0.2407 -0.0320 0.0353  0.0065  24  VAL   A CB  
602  C CG1 A VAL   A 24  ? 0.2164 0.2418 0.2852 -0.0150 0.0627  -0.0018 24  VAL   A CG1 
603  C CG1 B VAL   A 24  ? 0.2106 0.2156 0.2534 -0.0274 0.0229  0.0086  24  VAL   A CG1 
604  C CG2 A VAL   A 24  ? 0.2241 0.2357 0.2782 -0.0132 0.0734  0.0273  24  VAL   A CG2 
605  C CG2 B VAL   A 24  ? 0.2065 0.2128 0.2380 -0.0317 0.0418  0.0124  24  VAL   A CG2 
624  N N   A GLU   A 25  ? 0.2385 0.2540 0.2367 -0.0411 0.0735  -0.0299 25  GLU   A N   
625  N N   B GLU   A 25  ? 0.2189 0.2403 0.2234 -0.0430 0.0652  -0.0194 25  GLU   A N   
626  C CA  A GLU   A 25  ? 0.2556 0.2810 0.2492 -0.0335 0.0788  -0.0352 25  GLU   A CA  
627  C CA  B GLU   A 25  ? 0.2330 0.2482 0.2346 -0.0517 0.0673  -0.0228 25  GLU   A CA  
628  C C   A GLU   A 25  ? 0.2420 0.2809 0.2120 -0.0464 0.0845  -0.0339 25  GLU   A C   
629  C C   B GLU   A 25  ? 0.2340 0.2457 0.2177 -0.0571 0.0742  -0.0278 25  GLU   A C   
630  O O   A GLU   A 25  ? 0.2524 0.2906 0.2318 -0.0467 0.0800  -0.0296 25  GLU   A O   
631  O O   B GLU   A 25  ? 0.2414 0.2474 0.2202 -0.0613 0.0739  -0.0356 25  GLU   A O   
632  C CB  A GLU   A 25  ? 0.2844 0.3074 0.2984 -0.0277 0.0848  -0.0251 25  GLU   A CB  
633  C CB  B GLU   A 25  ? 0.2448 0.2556 0.2619 -0.0545 0.0657  -0.0184 25  GLU   A CB  
634  C CG  A GLU   A 25  ? 0.3188 0.3326 0.3683 -0.0293 0.0706  -0.0200 25  GLU   A CG  
635  C CG  B GLU   A 25  ? 0.2586 0.2632 0.2999 -0.0578 0.0603  -0.0122 25  GLU   A CG  
636  C CD  A GLU   A 25  ? 0.3447 0.3527 0.4274 -0.0340 0.0616  -0.0154 25  GLU   A CD  
637  C CD  B GLU   A 25  ? 0.2668 0.2676 0.3317 -0.0642 0.0562  -0.0045 25  GLU   A CD  
638  O OE1 A GLU   A 25  ? 0.3555 0.3573 0.4415 -0.0332 0.0504  -0.0257 25  GLU   A OE1 
639  O OE1 B GLU   A 25  ? 0.2677 0.2654 0.3403 -0.0656 0.0539  -0.0007 25  GLU   A OE1 
640  O OE2 A GLU   A 25  ? 0.3516 0.3635 0.4680 -0.0365 0.0611  -0.0187 25  GLU   A OE2 
641  O OE2 B GLU   A 25  ? 0.2738 0.2721 0.3483 -0.0665 0.0613  0.0005  25  GLU   A OE2 
654  N N   A GLU   A 26  ? 0.2312 0.2727 0.2158 -0.0676 0.0808  -0.0385 26  GLU   A N   
655  N N   B GLU   A 26  ? 0.2314 0.2393 0.2144 -0.0597 0.0789  -0.0298 26  GLU   A N   
656  C CA  A GLU   A 26  ? 0.2405 0.2739 0.1886 -0.0804 0.0737  -0.0309 26  GLU   A CA  
657  C CA  B GLU   A 26  ? 0.2346 0.2326 0.2058 -0.0572 0.0860  -0.0271 26  GLU   A CA  
658  C C   A GLU   A 26  ? 0.2488 0.2647 0.1822 -0.0745 0.0691  -0.0228 26  GLU   A C   
659  C C   B GLU   A 26  ? 0.2395 0.2405 0.1922 -0.0626 0.0770  -0.0284 26  GLU   A C   
660  O O   A GLU   A 26  ? 0.2575 0.2619 0.1660 -0.0874 0.0657  -0.0210 26  GLU   A O   
661  O O   B GLU   A 26  ? 0.2449 0.2376 0.1900 -0.0600 0.0790  -0.0433 26  GLU   A O   
662  C CB  A GLU   A 26  ? 0.2528 0.2875 0.2140 -0.0863 0.0566  -0.0334 26  GLU   A CB  
663  C CB  B GLU   A 26  ? 0.2379 0.2162 0.2226 -0.0486 0.0795  -0.0274 26  GLU   A CB  
664  C CG  A GLU   A 26  ? 0.2691 0.3087 0.2774 -0.0876 0.0574  -0.0334 26  GLU   A CG  
665  C CG  B GLU   A 26  ? 0.2345 0.1906 0.2189 -0.0569 0.0937  -0.0195 26  GLU   A CG  
666  C CD  A GLU   A 26  ? 0.2782 0.3323 0.3295 -0.0876 0.0748  -0.0241 26  GLU   A CD  
667  C CD  B GLU   A 26  ? 0.2336 0.1650 0.2099 -0.0656 0.1165  -0.0189 26  GLU   A CD  
668  O OE1 A GLU   A 26  ? 0.2846 0.3468 0.3345 -0.0838 0.0798  -0.0389 26  GLU   A OE1 
669  O OE1 B GLU   A 26  ? 0.2268 0.1428 0.2164 -0.0753 0.1071  -0.0363 26  GLU   A OE1 
670  O OE2 A GLU   A 26  ? 0.2855 0.3452 0.3692 -0.0873 0.0618  -0.0196 26  GLU   A OE2 
671  O OE2 B GLU   A 26  ? 0.2285 0.1699 0.1931 -0.0439 0.1214  -0.0256 26  GLU   A OE2 
684  N N   . ALA   A 27  ? 0.2362 0.2512 0.1881 -0.0744 0.0682  -0.0130 27  ALA   A N   
685  C CA  . ALA   A 27  ? 0.2436 0.2662 0.1830 -0.0623 0.0519  -0.0124 27  ALA   A CA  
686  C C   . ALA   A 27  ? 0.2709 0.2910 0.1961 -0.0774 0.0569  -0.0351 27  ALA   A C   
687  O O   . ALA   A 27  ? 0.2692 0.2775 0.2032 -0.0858 0.0419  -0.0301 27  ALA   A O   
688  C CB  . ALA   A 27  ? 0.2227 0.2490 0.1903 -0.0602 0.0450  -0.0020 27  ALA   A CB  
695  N N   A LYS   A 28  ? 0.2960 0.3078 0.1987 -0.0759 0.0543  -0.0637 28  LYS   A N   
696  N N   B LYS   A 28  ? 0.2979 0.3185 0.2236 -0.0747 0.0607  -0.0370 28  LYS   A N   
697  C CA  A LYS   A 28  ? 0.3324 0.3369 0.2413 -0.0647 0.0520  -0.0779 28  LYS   A CA  
698  C CA  B LYS   A 28  ? 0.3281 0.3479 0.2597 -0.0681 0.0609  -0.0397 28  LYS   A CA  
699  C C   A LYS   A 28  ? 0.3476 0.3619 0.2406 -0.0692 0.0671  -0.0614 28  LYS   A C   
700  C C   B LYS   A 28  ? 0.3433 0.3660 0.2483 -0.0725 0.0764  -0.0395 28  LYS   A C   
701  O O   A LYS   A 28  ? 0.3526 0.3704 0.2823 -0.0668 0.0469  -0.0543 28  LYS   A O   
702  O O   B LYS   A 28  ? 0.3457 0.3697 0.2702 -0.0709 0.0676  -0.0362 28  LYS   A O   
703  C CB  A LYS   A 28  ? 0.3529 0.3484 0.2956 -0.0458 0.0406  -0.0903 28  LYS   A CB  
704  C CB  B LYS   A 28  ? 0.3436 0.3592 0.3057 -0.0560 0.0468  -0.0403 28  LYS   A CB  
705  C CG  A LYS   A 28  ? 0.3697 0.3618 0.3548 -0.0288 0.0375  -0.0949 28  LYS   A CG  
706  C CG  B LYS   A 28  ? 0.3559 0.3700 0.3484 -0.0461 0.0371  -0.0396 28  LYS   A CG  
707  C CD  A LYS   A 28  ? 0.3855 0.3799 0.4222 -0.0156 0.0316  -0.0985 28  LYS   A CD  
708  C CD  B LYS   A 28  ? 0.3647 0.3810 0.3865 -0.0379 0.0285  -0.0386 28  LYS   A CD  
709  C CE  A LYS   A 28  ? 0.3941 0.3900 0.4720 -0.0091 0.0231  -0.0972 28  LYS   A CE  
710  C CE  B LYS   A 28  ? 0.3706 0.3884 0.4170 -0.0337 0.0208  -0.0371 28  LYS   A CE  
711  N NZ  A LYS   A 28  ? 0.4037 0.3954 0.5013 -0.0050 0.0178  -0.0881 28  LYS   A NZ  
712  N NZ  B LYS   A 28  ? 0.3738 0.3924 0.4321 -0.0309 0.0167  -0.0351 28  LYS   A NZ  
739  N N   . LYS   A 29  ? 0.3542 0.3795 0.2213 -0.0801 0.0983  -0.0385 29  LYS   A N   
740  C CA  . LYS   A 29  ? 0.3802 0.4145 0.2329 -0.0917 0.1180  -0.0226 29  LYS   A CA  
741  C C   . LYS   A 29  ? 0.3883 0.4156 0.1946 -0.1008 0.1015  -0.0241 29  LYS   A C   
742  O O   . LYS   A 29  ? 0.4048 0.4281 0.2145 -0.0917 0.0938  -0.0211 29  LYS   A O   
743  C CB  . LYS   A 29  ? 0.3981 0.4458 0.3191 -0.0852 0.1309  -0.0112 29  LYS   A CB  
744  C CG  . LYS   A 29  ? 0.4204 0.4704 0.4053 -0.0760 0.1283  -0.0129 29  LYS   A CG  
745  C CD  . LYS   A 29  ? 0.4380 0.4904 0.4791 -0.0692 0.1245  -0.0186 29  LYS   A CD  
746  C CE  . LYS   A 29  ? 0.4511 0.5002 0.5350 -0.0646 0.1222  -0.0170 29  LYS   A CE  
747  N NZ  . LYS   A 29  ? 0.4562 0.5070 0.5617 -0.0623 0.1201  -0.0124 29  LYS   A NZ  
762  N N   . VAL   A 30  ? 0.3759 0.3999 0.1926 -0.1178 0.0970  -0.0203 30  VAL   A N   
763  C CA  . VAL   A 30  ? 0.3719 0.3894 0.1762 -0.1313 0.0715  0.0075  30  VAL   A CA  
764  C C   . VAL   A 30  ? 0.3754 0.3743 0.1481 -0.1310 0.0499  0.0185  30  VAL   A C   
765  O O   . VAL   A 30  ? 0.3849 0.3765 0.1583 -0.1318 0.0354  0.0258  30  VAL   A O   
766  C CB  . VAL   A 30  ? 0.3693 0.3838 0.2290 -0.1388 0.0358  0.0022  30  VAL   A CB  
767  C CG1 . VAL   A 30  ? 0.3705 0.3866 0.2457 -0.1397 0.0184  0.0043  30  VAL   A CG1 
768  C CG2 . VAL   A 30  ? 0.3706 0.3812 0.2592 -0.1405 0.0373  0.0005  30  VAL   A CG2 
778  N N   . LYS   A 31  ? 0.3627 0.3506 0.1295 -0.1294 0.0298  0.0094  31  LYS   A N   
779  C CA  . LYS   A 31  ? 0.3770 0.3504 0.1428 -0.1230 0.0045  0.0104  31  LYS   A CA  
780  C C   . LYS   A 31  ? 0.3437 0.3210 0.1180 -0.1017 -0.0153 0.0411  31  LYS   A C   
781  O O   . LYS   A 31  ? 0.3490 0.3367 0.1339 -0.0932 -0.0300 0.0589  31  LYS   A O   
782  C CB  . LYS   A 31  ? 0.4159 0.3785 0.2632 -0.1182 -0.0118 -0.0132 31  LYS   A CB  
783  C CG  . LYS   A 31  ? 0.4674 0.4145 0.4052 -0.1054 -0.0278 -0.0251 31  LYS   A CG  
784  C CD  . LYS   A 31  ? 0.5036 0.4439 0.5177 -0.0969 -0.0424 -0.0366 31  LYS   A CD  
785  C CE  . LYS   A 31  ? 0.5219 0.4525 0.5863 -0.0893 -0.0525 -0.0439 31  LYS   A CE  
786  N NZ  . LYS   A 31  ? 0.5414 0.4673 0.6176 -0.0871 -0.0576 -0.0484 31  LYS   A NZ  
800  N N   . PRO   A 32  ? 0.3055 0.2853 0.1059 -0.1007 -0.0091 0.0277  32  PRO   A N   
801  C CA  . PRO   A 32  ? 0.2965 0.2659 0.1439 -0.0909 -0.0221 0.0441  32  PRO   A CA  
802  C C   . PRO   A 32  ? 0.2883 0.2622 0.1588 -0.0772 -0.0274 0.0483  32  PRO   A C   
803  O O   . PRO   A 32  ? 0.2806 0.2573 0.1567 -0.0783 -0.0407 0.0490  32  PRO   A O   
804  C CB  . PRO   A 32  ? 0.2904 0.2673 0.1526 -0.0899 -0.0173 0.0361  32  PRO   A CB  
805  C CG  . PRO   A 32  ? 0.2899 0.2748 0.0996 -0.0818 -0.0315 0.0290  32  PRO   A CG  
806  C CD  . PRO   A 32  ? 0.2870 0.2741 0.0960 -0.0857 -0.0122 0.0260  32  PRO   A CD  
814  N N   . THR   A 33  ? 0.2938 0.2617 0.1478 -0.0655 -0.0278 0.0527  33  THR   A N   
815  C CA  . THR   A 33  ? 0.2914 0.2530 0.1595 -0.0525 -0.0416 0.0483  33  THR   A CA  
816  C C   . THR   A 33  ? 0.2588 0.2363 0.1522 -0.0508 -0.0394 0.0430  33  THR   A C   
817  O O   . THR   A 33  ? 0.2553 0.2434 0.1619 -0.0525 -0.0511 0.0481  33  THR   A O   
818  C CB  . THR   A 33  ? 0.3173 0.2700 0.1700 -0.0387 -0.0465 0.0702  33  THR   A CB  
819  O OG1 . THR   A 33  ? 0.3399 0.2864 0.2004 -0.0179 -0.0396 0.0862  33  THR   A OG1 
820  C CG2 . THR   A 33  ? 0.3226 0.2783 0.1999 -0.0306 -0.0556 0.0670  33  THR   A CG2 
828  N N   . VAL   A 34  ? 0.2342 0.2167 0.1324 -0.0480 -0.0319 0.0402  34  VAL   A N   
829  C CA  . VAL   A 34  ? 0.2103 0.2024 0.1254 -0.0412 -0.0260 0.0374  34  VAL   A CA  
830  C C   . VAL   A 34  ? 0.1997 0.1901 0.1149 -0.0342 -0.0169 0.0262  34  VAL   A C   
831  O O   . VAL   A 34  ? 0.2010 0.1917 0.1376 -0.0472 -0.0089 0.0242  34  VAL   A O   
832  C CB  . VAL   A 34  ? 0.2111 0.2001 0.1483 -0.0420 -0.0129 0.0227  34  VAL   A CB  
833  C CG1 . VAL   A 34  ? 0.2171 0.2058 0.1555 -0.0410 0.0106  0.0133  34  VAL   A CG1 
834  C CG2 . VAL   A 34  ? 0.2182 0.2078 0.1773 -0.0350 -0.0296 0.0226  34  VAL   A CG2 
844  N N   . VAL   A 35  ? 0.1799 0.1759 0.1169 -0.0372 -0.0130 0.0187  35  VAL   A N   
845  C CA  . VAL   A 35  ? 0.1735 0.1728 0.1115 -0.0346 -0.0045 0.0104  35  VAL   A CA  
846  C C   . VAL   A 35  ? 0.1662 0.1568 0.1115 -0.0262 -0.0007 0.0154  35  VAL   A C   
847  O O   . VAL   A 35  ? 0.1582 0.1756 0.1316 -0.0308 0.0119  0.0079  35  VAL   A O   
848  C CB  . VAL   A 35  ? 0.1795 0.1788 0.1293 -0.0297 0.0091  -0.0017 35  VAL   A CB  
849  C CG1 . VAL   A 35  ? 0.1920 0.1860 0.1453 -0.0191 0.0030  -0.0034 35  VAL   A CG1 
850  C CG2 . VAL   A 35  ? 0.1773 0.1762 0.1657 -0.0153 0.0101  -0.0132 35  VAL   A CG2 
860  N N   . VAL   A 36  ? 0.1522 0.1534 0.1074 -0.0285 0.0048  0.0176  36  VAL   A N   
861  C CA  . VAL   A 36  ? 0.1401 0.1502 0.1082 -0.0162 -0.0017 0.0138  36  VAL   A CA  
862  C C   . VAL   A 36  ? 0.1371 0.1471 0.1304 -0.0158 0.0098  0.0070  36  VAL   A C   
863  O O   . VAL   A 36  ? 0.1466 0.1456 0.1394 -0.0105 0.0200  0.0101  36  VAL   A O   
864  C CB  . VAL   A 36  ? 0.1439 0.1457 0.1148 -0.0126 -0.0022 0.0112  36  VAL   A CB  
865  C CG1 . VAL   A 36  ? 0.1434 0.1478 0.1266 -0.0145 -0.0009 0.0035  36  VAL   A CG1 
866  C CG2 . VAL   A 36  ? 0.1593 0.1562 0.1377 -0.0144 -0.0044 0.0245  36  VAL   A CG2 
876  N N   . ASN   A 37  ? 0.1313 0.1423 0.1103 -0.0091 0.0031  0.0153  37  ASN   A N   
877  C CA  . ASN   A 37  ? 0.1331 0.1399 0.1055 -0.0015 0.0051  0.0141  37  ASN   A CA  
878  C C   . ASN   A 37  ? 0.1388 0.1358 0.1076 -0.0068 0.0119  0.0198  37  ASN   A C   
879  O O   . ASN   A 37  ? 0.1476 0.1526 0.1088 0.0053  0.0134  0.0011  37  ASN   A O   
880  C CB  . ASN   A 37  ? 0.1404 0.1392 0.1136 -0.0010 0.0037  0.0082  37  ASN   A CB  
881  C CG  . ASN   A 37  ? 0.1431 0.1354 0.1235 -0.0012 0.0011  0.0027  37  ASN   A CG  
882  O OD1 . ASN   A 37  ? 0.1445 0.1409 0.1410 0.0039  0.0036  0.0082  37  ASN   A OD1 
883  N ND2 . ASN   A 37  ? 0.1439 0.1374 0.1393 -0.0046 0.0017  0.0189  37  ASN   A ND2 
890  N N   A ALA   A 38  ? 0.1353 0.1461 0.1135 0.0010  0.0072  0.0116  38  ALA   A N   
891  N N   B ALA   A 38  ? 0.1327 0.1430 0.1285 -0.0081 0.0012  0.0139  38  ALA   A N   
892  C CA  A ALA   A 38  ? 0.1439 0.1508 0.0960 0.0017  0.0024  0.0041  38  ALA   A CA  
893  C CA  B ALA   A 38  ? 0.1331 0.1535 0.1429 -0.0085 -0.0088 0.0073  38  ALA   A CA  
894  C C   A ALA   A 38  ? 0.1438 0.1527 0.1107 0.0091  0.0011  0.0050  38  ALA   A C   
895  C C   B ALA   A 38  ? 0.1303 0.1534 0.1514 -0.0043 -0.0137 0.0051  38  ALA   A C   
896  O O   A ALA   A 38  ? 0.1401 0.1395 0.1205 0.0032  -0.0075 -0.0002 38  ALA   A O   
897  O O   B ALA   A 38  ? 0.1182 0.1500 0.1669 -0.0086 -0.0109 0.0074  38  ALA   A O   
898  C CB  A ALA   A 38  ? 0.1423 0.1732 0.1318 -0.0128 0.0044  0.0074  38  ALA   A CB  
899  C CB  B ALA   A 38  ? 0.1318 0.1607 0.1526 -0.0145 -0.0161 0.0023  38  ALA   A CB  
910  N N   A ALA   A 39  ? 0.1419 0.1414 0.1218 0.0040  0.0066  0.0097  39  ALA   A N   
911  N N   B ALA   A 39  ? 0.1423 0.1535 0.1538 0.0002  -0.0169 0.0067  39  ALA   A N   
912  C CA  A ALA   A 39  ? 0.1402 0.1440 0.1206 0.0058  0.0173  0.0095  39  ALA   A CA  
913  C CA  B ALA   A 39  ? 0.1525 0.1582 0.1502 0.0029  -0.0179 0.0113  39  ALA   A CA  
914  C C   A ALA   A 39  ? 0.1411 0.1446 0.1181 -0.0007 0.0018  0.0073  39  ALA   A C   
915  C C   B ALA   A 39  ? 0.1502 0.1490 0.1379 0.0002  -0.0121 0.0114  39  ALA   A C   
916  O O   A ALA   A 39  ? 0.1537 0.1424 0.1284 -0.0069 0.0049  0.0025  39  ALA   A O   
917  O O   B ALA   A 39  ? 0.1578 0.1443 0.1389 -0.0062 -0.0083 0.0095  39  ALA   A O   
918  C CB  A ALA   A 39  ? 0.1457 0.1448 0.1267 0.0096  -0.0019 -0.0085 39  ALA   A CB  
919  C CB  B ALA   A 39  ? 0.1624 0.1682 0.1494 0.0084  -0.0347 0.0072  39  ALA   A CB  
930  N N   A ASN   A 40  ? 0.1461 0.1471 0.1242 -0.0120 0.0149  0.0098  40  ASN   A N   
931  N N   B ASN   A 40  ? 0.1482 0.1471 0.1361 -0.0000 -0.0032 0.0137  40  ASN   A N   
932  C CA  A ASN   A 40  ? 0.1481 0.1443 0.1351 -0.0058 0.0077  0.0059  40  ASN   A CA  
933  C CA  B ASN   A 40  ? 0.1497 0.1461 0.1410 0.0019  -0.0032 0.0188  40  ASN   A CA  
934  C C   A ASN   A 40  ? 0.1407 0.1270 0.1204 -0.0072 0.0223  0.0187  40  ASN   A C   
935  C C   B ASN   A 40  ? 0.1523 0.1434 0.1441 -0.0020 0.0004  0.0244  40  ASN   A C   
936  O O   A ASN   A 40  ? 0.1457 0.1325 0.1266 -0.0085 0.0196  0.0101  40  ASN   A O   
937  O O   B ASN   A 40  ? 0.1492 0.1408 0.1453 -0.0103 -0.0083 0.0276  40  ASN   A O   
938  C CB  A ASN   A 40  ? 0.1576 0.1539 0.1473 0.0024  0.0022  0.0001  40  ASN   A CB  
939  C CB  B ASN   A 40  ? 0.1523 0.1491 0.1554 0.0074  -0.0087 0.0140  40  ASN   A CB  
940  C CG  A ASN   A 40  ? 0.1689 0.1522 0.1740 0.0045  0.0007  0.0106  40  ASN   A CG  
941  C CG  B ASN   A 40  ? 0.1556 0.1484 0.1741 0.0085  -0.0168 0.0110  40  ASN   A CG  
942  O OD1 A ASN   A 40  ? 0.1819 0.1489 0.2044 -0.0010 0.0052  0.0089  40  ASN   A OD1 
943  O OD1 B ASN   A 40  ? 0.1607 0.1507 0.2037 0.0105  -0.0240 -0.0039 40  ASN   A OD1 
944  N ND2 A ASN   A 40  ? 0.1688 0.1635 0.1823 0.0024  0.0159  -0.0030 40  ASN   A ND2 
945  N ND2 B ASN   A 40  ? 0.1555 0.1508 0.1733 -0.0050 0.0006  0.0074  40  ASN   A ND2 
958  N N   A VAL   A 41  ? 0.1557 0.1306 0.1224 0.0036  0.0182  0.0198  41  VAL   A N   
959  N N   B VAL   A 41  ? 0.1543 0.1442 0.1441 0.0036  0.0133  0.0241  41  VAL   A N   
960  C CA  A VAL   A 41  ? 0.1517 0.1403 0.1446 0.0053  0.0272  0.0148  41  VAL   A CA  
961  C CA  B VAL   A 41  ? 0.1585 0.1469 0.1358 0.0042  0.0205  0.0269  41  VAL   A CA  
962  C C   A VAL   A 41  ? 0.1569 0.1439 0.1652 0.0110  0.0348  0.0115  41  VAL   A C   
963  C C   B VAL   A 41  ? 0.1581 0.1466 0.1406 -0.0011 0.0262  0.0208  41  VAL   A C   
964  O O   A VAL   A 41  ? 0.1552 0.1342 0.1804 0.0083  0.0250  0.0071  41  VAL   A O   
965  O O   B VAL   A 41  ? 0.1584 0.1412 0.1514 -0.0053 0.0199  0.0181  41  VAL   A O   
966  C CB  A VAL   A 41  ? 0.1628 0.1468 0.1405 -0.0039 0.0275  0.0088  41  VAL   A CB  
967  C CB  B VAL   A 41  ? 0.1622 0.1493 0.1365 0.0118  0.0268  0.0335  41  VAL   A CB  
968  C CG1 A VAL   A 41  ? 0.1767 0.1646 0.1518 0.0023  0.0276  0.0039  41  VAL   A CG1 
969  C CG1 B VAL   A 41  ? 0.1713 0.1555 0.1338 0.0072  0.0396  0.0236  41  VAL   A CG1 
970  C CG2 A VAL   A 41  ? 0.1697 0.1572 0.1303 -0.0011 0.0407  0.0066  41  VAL   A CG2 
971  C CG2 B VAL   A 41  ? 0.1624 0.1576 0.1459 0.0181  0.0157  0.0397  41  VAL   A CG2 
990  N N   A TYR   A 42  ? 0.1446 0.1387 0.1788 0.0013  0.0364  0.0177  42  TYR   A N   
991  N N   B TYR   A 42  ? 0.1579 0.1478 0.1440 -0.0013 0.0256  0.0213  42  TYR   A N   
992  C CA  A TYR   A 42  ? 0.1581 0.1318 0.1646 -0.0055 0.0438  0.0235  42  TYR   A CA  
993  C CA  B TYR   A 42  ? 0.1621 0.1476 0.1551 -0.0032 0.0259  0.0168  42  TYR   A CA  
994  C C   A TYR   A 42  ? 0.1510 0.1273 0.1737 -0.0003 0.0324  0.0264  42  TYR   A C   
995  C C   B TYR   A 42  ? 0.1571 0.1384 0.1528 -0.0022 0.0216  0.0225  42  TYR   A C   
996  O O   A TYR   A 42  ? 0.1470 0.1302 0.1947 -0.0108 0.0262  0.0026  42  TYR   A O   
997  O O   B TYR   A 42  ? 0.1560 0.1369 0.1558 -0.0055 0.0191  0.0276  42  TYR   A O   
998  C CB  A TYR   A 42  ? 0.1901 0.1463 0.1580 -0.0035 0.0371  0.0305  42  TYR   A CB  
999  C CB  B TYR   A 42  ? 0.1740 0.1617 0.1666 -0.0047 0.0191  0.0103  42  TYR   A CB  
1000 C CG  A TYR   A 42  ? 0.2189 0.1561 0.1534 0.0024  0.0298  0.0329  42  TYR   A CG  
1001 C CG  B TYR   A 42  ? 0.1842 0.1740 0.1749 -0.0088 0.0136  0.0051  42  TYR   A CG  
1002 C CD1 A TYR   A 42  ? 0.2293 0.1645 0.1723 -0.0110 0.0427  0.0327  42  TYR   A CD1 
1003 C CD1 B TYR   A 42  ? 0.1903 0.1802 0.1841 -0.0143 0.0164  0.0036  42  TYR   A CD1 
1004 C CD2 A TYR   A 42  ? 0.2347 0.1744 0.1806 0.0024  0.0298  0.0198  42  TYR   A CD2 
1005 C CD2 B TYR   A 42  ? 0.1887 0.1852 0.1863 -0.0109 0.0103  -0.0010 42  TYR   A CD2 
1006 C CE1 A TYR   A 42  ? 0.2361 0.1704 0.1820 -0.0145 0.0479  0.0298  42  TYR   A CE1 
1007 C CE1 B TYR   A 42  ? 0.1945 0.1866 0.1904 -0.0162 0.0158  0.0021  42  TYR   A CE1 
1008 C CE2 A TYR   A 42  ? 0.2475 0.1864 0.1958 -0.0136 0.0383  0.0264  42  TYR   A CE2 
1009 C CE2 B TYR   A 42  ? 0.1945 0.1937 0.1929 -0.0186 0.0123  0.0045  42  TYR   A CE2 
1010 C CZ  A TYR   A 42  ? 0.2551 0.1877 0.1823 -0.0188 0.0577  0.0272  42  TYR   A CZ  
1011 C CZ  B TYR   A 42  ? 0.2008 0.1972 0.1921 -0.0184 0.0196  0.0025  42  TYR   A CZ  
1012 O OH  A TYR   A 42  ? 0.2681 0.2052 0.2197 -0.0311 0.0535  0.0162  42  TYR   A OH  
1013 O OH  B TYR   A 42  ? 0.2083 0.2072 0.2054 -0.0222 0.0164  -0.0033 42  TYR   A OH  
1032 N N   . LEU   A 43  ? 0.1497 0.1314 0.1499 -0.0033 0.0169  0.0075  43  LEU   A N   
1033 C CA  . LEU   A 43  ? 0.1419 0.1314 0.1426 -0.0031 0.0087  0.0074  43  LEU   A CA  
1034 C C   . LEU   A 43  ? 0.1427 0.1387 0.1458 0.0004  0.0098  0.0074  43  LEU   A C   
1035 O O   . LEU   A 43  ? 0.1632 0.1445 0.1710 0.0040  -0.0057 -0.0017 43  LEU   A O   
1036 C CB  . LEU   A 43  ? 0.1519 0.1320 0.1558 -0.0061 0.0149  0.0049  43  LEU   A CB  
1037 C CG  . LEU   A 43  ? 0.1513 0.1350 0.1658 -0.0038 0.0075  0.0052  43  LEU   A CG  
1038 C CD1 . LEU   A 43  ? 0.1639 0.1448 0.1806 -0.0002 -0.0018 0.0172  43  LEU   A CD1 
1039 C CD2 . LEU   A 43  ? 0.1727 0.1398 0.1587 -0.0023 0.0093  0.0177  43  LEU   A CD2 
1052 N N   A LYS   A 44  ? 0.1484 0.1410 0.1338 -0.0024 0.0110  0.0097  44  LYS   A N   
1053 N N   B LYS   A 44  ? 0.1578 0.1483 0.1586 0.0028  0.0035  0.0056  44  LYS   A N   
1054 C CA  A LYS   A 44  ? 0.1564 0.1334 0.1350 -0.0080 0.0208  0.0219  44  LYS   A CA  
1055 C CA  B LYS   A 44  ? 0.1745 0.1559 0.1746 0.0045  0.0031  0.0064  44  LYS   A CA  
1056 C C   A LYS   A 44  ? 0.1459 0.1347 0.1301 -0.0000 0.0089  0.0122  44  LYS   A C   
1057 C C   B LYS   A 44  ? 0.1696 0.1509 0.1545 0.0065  -0.0049 0.0063  44  LYS   A C   
1058 O O   A LYS   A 44  ? 0.1562 0.1489 0.1602 0.0021  0.0086  -0.0046 44  LYS   A O   
1059 O O   B LYS   A 44  ? 0.1687 0.1507 0.1502 0.0034  -0.0001 0.0013  44  LYS   A O   
1060 C CB  A LYS   A 44  ? 0.1837 0.1536 0.1942 -0.0053 0.0311  0.0290  44  LYS   A CB  
1061 C CB  B LYS   A 44  ? 0.1923 0.1723 0.2101 0.0044  0.0139  0.0125  44  LYS   A CB  
1062 C CG  A LYS   A 44  ? 0.2164 0.1753 0.2763 -0.0155 0.0516  0.0325  44  LYS   A CG  
1063 C CG  B LYS   A 44  ? 0.2085 0.1897 0.2544 0.0039  0.0249  0.0169  44  LYS   A CG  
1064 C CD  A LYS   A 44  ? 0.2596 0.2342 0.3784 -0.0181 0.0353  0.0233  44  LYS   A CD  
1065 C CD  B LYS   A 44  ? 0.2262 0.2144 0.3019 0.0014  0.0207  0.0123  44  LYS   A CD  
1066 C CE  A LYS   A 44  ? 0.2802 0.2675 0.4319 -0.0244 0.0216  0.0240  44  LYS   A CE  
1067 C CE  B LYS   A 44  ? 0.2347 0.2277 0.3332 -0.0020 0.0168  0.0119  44  LYS   A CE  
1068 N NZ  A LYS   A 44  ? 0.2956 0.2937 0.4542 -0.0311 0.0208  0.0275  44  LYS   A NZ  
1069 N NZ  B LYS   A 44  ? 0.2429 0.2369 0.3487 -0.0080 0.0136  0.0090  44  LYS   A NZ  
1096 N N   A HIS   A 45  ? 0.1334 0.1301 0.1437 0.0004  0.0081  0.0187  45  HIS   A N   
1097 N N   B HIS   A 45  ? 0.1663 0.1481 0.1494 0.0077  -0.0133 0.0139  45  HIS   A N   
1098 C CA  A HIS   A 45  ? 0.1357 0.1390 0.1457 0.0030  0.0091  0.0054  45  HIS   A CA  
1099 C CA  B HIS   A 45  ? 0.1656 0.1496 0.1481 0.0151  -0.0176 0.0014  45  HIS   A CA  
1100 C C   A HIS   A 45  ? 0.1457 0.1495 0.1691 0.0027  0.0042  0.0052  45  HIS   A C   
1101 C C   B HIS   A 45  ? 0.1671 0.1534 0.1551 0.0232  -0.0181 0.0026  45  HIS   A C   
1102 O O   A HIS   A 45  ? 0.1671 0.1606 0.1965 0.0218  -0.0049 -0.0105 45  HIS   A O   
1103 O O   B HIS   A 45  ? 0.1718 0.1576 0.1703 0.0315  -0.0212 -0.0061 45  HIS   A O   
1104 C CB  A HIS   A 45  ? 0.1325 0.1400 0.1305 -0.0079 0.0040  0.0113  45  HIS   A CB  
1105 C CB  B HIS   A 45  ? 0.1658 0.1457 0.1476 0.0179  -0.0220 -0.0117 45  HIS   A CB  
1106 C CG  A HIS   A 45  ? 0.1338 0.1406 0.1220 -0.0164 0.0040  0.0179  45  HIS   A CG  
1107 C CG  B HIS   A 45  ? 0.1625 0.1399 0.1326 0.0221  -0.0062 -0.0189 45  HIS   A CG  
1108 N ND1 A HIS   A 45  ? 0.1341 0.1440 0.1487 -0.0125 -0.0003 0.0186  45  HIS   A ND1 
1109 N ND1 B HIS   A 45  ? 0.1579 0.1377 0.1418 0.0248  -0.0042 -0.0206 45  HIS   A ND1 
1110 C CD2 A HIS   A 45  ? 0.1393 0.1461 0.1323 -0.0192 -0.0060 0.0283  45  HIS   A CD2 
1111 C CD2 B HIS   A 45  ? 0.1648 0.1381 0.1245 0.0252  0.0027  -0.0241 45  HIS   A CD2 
1112 C CE1 A HIS   A 45  ? 0.1321 0.1500 0.1348 -0.0106 -0.0049 0.0250  45  HIS   A CE1 
1113 C CE1 B HIS   A 45  ? 0.1569 0.1365 0.1357 0.0243  -0.0000 -0.0228 45  HIS   A CE1 
1114 N NE2 A HIS   A 45  ? 0.1425 0.1536 0.1317 -0.0129 -0.0009 0.0312  45  HIS   A NE2 
1115 N NE2 B HIS   A 45  ? 0.1607 0.1375 0.1265 0.0262  0.0077  -0.0256 45  HIS   A NE2 
1130 N N   A GLY   A 46  ? 0.1593 0.1559 0.1776 0.0113  -0.0099 0.0171  46  GLY   A N   
1131 N N   B GLY   A 46  ? 0.1690 0.1527 0.1513 0.0266  -0.0207 0.0099  46  GLY   A N   
1132 C CA  A GLY   A 46  ? 0.1668 0.1764 0.1900 0.0134  -0.0183 0.0190  46  GLY   A CA  
1133 C CA  B GLY   A 46  ? 0.1689 0.1494 0.1502 0.0271  -0.0255 0.0227  46  GLY   A CA  
1134 C C   A GLY   A 46  ? 0.1635 0.1718 0.2022 0.0193  -0.0247 0.0189  46  GLY   A C   
1135 C C   B GLY   A 46  ? 0.1632 0.1359 0.1417 0.0326  -0.0359 0.0370  46  GLY   A C   
1136 O O   A GLY   A 46  ? 0.1757 0.1797 0.2431 0.0202  -0.0295 -0.0014 46  GLY   A O   
1137 O O   B GLY   A 46  ? 0.1661 0.1354 0.1627 0.0354  -0.0369 0.0507  46  GLY   A O   
1144 N N   A GLY   A 47  ? 0.1682 0.1695 0.1853 0.0136  -0.0205 0.0037  47  GLY   A N   
1145 N N   B GLY   A 47  ? 0.1568 0.1300 0.1461 0.0290  -0.0415 0.0217  47  GLY   A N   
1146 C CA  A GLY   A 47  ? 0.1781 0.1814 0.1734 0.0126  -0.0400 -0.0074 47  GLY   A CA  
1147 C CA  B GLY   A 47  ? 0.1632 0.1393 0.1586 0.0254  -0.0446 0.0114  47  GLY   A CA  
1148 C C   A GLY   A 47  ? 0.1736 0.1599 0.1787 0.0164  -0.0510 -0.0016 47  GLY   A C   
1149 C C   B GLY   A 47  ? 0.1659 0.1428 0.1615 0.0204  -0.0364 -0.0033 47  GLY   A C   
1150 O O   A GLY   A 47  ? 0.1741 0.1490 0.1892 0.0247  -0.0504 0.0121  47  GLY   A O   
1151 O O   B GLY   A 47  ? 0.1712 0.1438 0.1631 0.0162  -0.0325 -0.0038 47  GLY   A O   
1158 N N   A GLY   A 48  ? 0.1658 0.1647 0.2067 0.0162  -0.0580 0.0015  48  GLY   A N   
1159 N N   B GLY   A 48  ? 0.1644 0.1447 0.1817 0.0135  -0.0359 -0.0125 48  GLY   A N   
1160 C CA  A GLY   A 48  ? 0.1551 0.1641 0.2158 0.0117  -0.0492 -0.0063 48  GLY   A CA  
1161 C CA  B GLY   A 48  ? 0.1566 0.1450 0.1789 0.0087  -0.0276 -0.0196 48  GLY   A CA  
1162 C C   A GLY   A 48  ? 0.1433 0.1596 0.1940 0.0048  -0.0192 -0.0047 48  GLY   A C   
1163 C C   B GLY   A 48  ? 0.1471 0.1425 0.1684 0.0029  -0.0096 -0.0209 48  GLY   A C   
1164 O O   A GLY   A 48  ? 0.1455 0.1596 0.2133 0.0085  -0.0137 -0.0139 48  GLY   A O   
1165 O O   B GLY   A 48  ? 0.1489 0.1348 0.1518 0.0036  -0.0009 -0.0393 48  GLY   A O   
1172 N N   . VAL   A 49  ? 0.1386 0.1460 0.1818 0.0003  -0.0086 -0.0106 49  VAL   A N   
1173 C CA  . VAL   A 49  ? 0.1476 0.1392 0.1726 -0.0070 0.0108  -0.0030 49  VAL   A CA  
1174 C C   . VAL   A 49  ? 0.1459 0.1364 0.1411 0.0012  0.0117  -0.0007 49  VAL   A C   
1175 O O   . VAL   A 49  ? 0.1469 0.1476 0.1484 -0.0073 0.0170  -0.0096 49  VAL   A O   
1176 C CB  . VAL   A 49  ? 0.1594 0.1438 0.1786 -0.0132 0.0038  -0.0014 49  VAL   A CB  
1177 C CG1 . VAL   A 49  ? 0.1749 0.1424 0.1911 -0.0077 0.0035  0.0162  49  VAL   A CG1 
1178 C CG2 . VAL   A 49  ? 0.1787 0.1591 0.2419 -0.0311 0.0024  0.0041  49  VAL   A CG2 
1189 N N   . ALA   A 50  ? 0.1402 0.1307 0.1379 -0.0014 -0.0058 0.0001  50  ALA   A N   
1190 C CA  . ALA   A 50  ? 0.1402 0.1372 0.1327 -0.0074 -0.0041 0.0078  50  ALA   A CA  
1191 C C   . ALA   A 50  ? 0.1356 0.1416 0.1222 -0.0084 -0.0040 0.0008  50  ALA   A C   
1192 O O   . ALA   A 50  ? 0.1343 0.1431 0.1435 -0.0002 -0.0023 -0.0006 50  ALA   A O   
1193 C CB  . ALA   A 50  ? 0.1369 0.1389 0.1344 -0.0014 -0.0024 -0.0030 50  ALA   A CB  
1199 N N   . GLY   A 51  ? 0.1345 0.1352 0.1457 0.0045  -0.0094 0.0006  51  GLY   A N   
1200 C CA  . GLY   A 51  ? 0.1517 0.1301 0.1536 0.0081  -0.0100 -0.0019 51  GLY   A CA  
1201 C C   . GLY   A 51  ? 0.1379 0.1361 0.1635 0.0046  -0.0056 -0.0091 51  GLY   A C   
1202 O O   . GLY   A 51  ? 0.1453 0.1482 0.1706 -0.0009 -0.0056 -0.0165 51  GLY   A O   
1206 N N   . ALA   A 52  ? 0.1344 0.1528 0.1565 -0.0005 -0.0062 -0.0184 52  ALA   A N   
1207 C CA  . ALA   A 52  ? 0.1403 0.1627 0.1542 -0.0035 -0.0007 -0.0183 52  ALA   A CA  
1208 C C   . ALA   A 52  ? 0.1406 0.1608 0.1407 -0.0126 0.0117  -0.0125 52  ALA   A C   
1209 O O   . ALA   A 52  ? 0.1530 0.1744 0.1678 -0.0063 0.0085  -0.0155 52  ALA   A O   
1210 C CB  . ALA   A 52  ? 0.1516 0.1874 0.1914 -0.0043 0.0010  -0.0151 52  ALA   A CB  
1216 N N   A LEU   A 53  ? 0.1381 0.1549 0.1418 -0.0106 0.0032  -0.0134 53  LEU   A N   
1217 N N   B LEU   A 53  ? 0.1369 0.1539 0.1393 -0.0099 0.0089  -0.0084 53  LEU   A N   
1218 C CA  A LEU   A 53  ? 0.1517 0.1622 0.1239 -0.0084 0.0059  -0.0069 53  LEU   A CA  
1219 C CA  B LEU   A 53  ? 0.1387 0.1514 0.1318 -0.0075 0.0077  -0.0001 53  LEU   A CA  
1220 C C   A LEU   A 53  ? 0.1476 0.1621 0.1092 0.0080  0.0069  -0.0103 53  LEU   A C   
1221 C C   B LEU   A 53  ? 0.1377 0.1521 0.1276 -0.0023 0.0087  -0.0032 53  LEU   A C   
1222 O O   A LEU   A 53  ? 0.1628 0.1664 0.1287 -0.0078 0.0080  -0.0074 53  LEU   A O   
1223 O O   B LEU   A 53  ? 0.1397 0.1548 0.1367 -0.0124 0.0125  0.0008  53  LEU   A O   
1224 C CB  A LEU   A 53  ? 0.1602 0.1682 0.1361 -0.0157 0.0042  0.0001  53  LEU   A CB  
1225 C CB  B LEU   A 53  ? 0.1376 0.1482 0.1367 -0.0067 0.0067  0.0089  53  LEU   A CB  
1226 C CG  A LEU   A 53  ? 0.1823 0.1712 0.1610 -0.0219 0.0107  0.0033  53  LEU   A CG  
1227 C CG  B LEU   A 53  ? 0.1404 0.1411 0.1311 -0.0084 0.0098  0.0106  53  LEU   A CG  
1228 C CD1 A LEU   A 53  ? 0.1968 0.1797 0.1657 -0.0067 0.0088  -0.0032 53  LEU   A CD1 
1229 C CD1 B LEU   A 53  ? 0.1469 0.1448 0.1394 -0.0008 0.0061  0.0104  53  LEU   A CD1 
1230 C CD2 A LEU   A 53  ? 0.1927 0.1853 0.1761 -0.0247 0.0059  0.0068  53  LEU   A CD2 
1231 C CD2 B LEU   A 53  ? 0.1381 0.1384 0.1255 -0.0101 0.0156  0.0040  53  LEU   A CD2 
1254 N N   . ASN   A 54  ? 0.1356 0.1490 0.1240 -0.0008 0.0048  0.0009  54  ASN   A N   
1255 C CA  . ASN   A 54  ? 0.1258 0.1432 0.1402 -0.0078 -0.0015 -0.0087 54  ASN   A CA  
1256 C C   . ASN   A 54  ? 0.1389 0.1544 0.1430 -0.0081 0.0002  -0.0109 54  ASN   A C   
1257 O O   . ASN   A 54  ? 0.1445 0.1609 0.1473 -0.0056 -0.0053 -0.0200 54  ASN   A O   
1258 C CB  . ASN   A 54  ? 0.1278 0.1466 0.1478 -0.0064 -0.0118 -0.0064 54  ASN   A CB  
1259 C CG  . ASN   A 54  ? 0.1350 0.1542 0.1429 0.0003  -0.0051 -0.0027 54  ASN   A CG  
1260 O OD1 . ASN   A 54  ? 0.1400 0.1561 0.1490 -0.0049 -0.0104 -0.0045 54  ASN   A OD1 
1261 N ND2 . ASN   A 54  ? 0.1371 0.1604 0.1654 -0.0100 -0.0097 0.0121  54  ASN   A ND2 
1269 N N   . LYS   A 55  ? 0.1459 0.1591 0.1382 -0.0050 0.0001  -0.0151 55  LYS   A N   
1270 C CA  . LYS   A 55  ? 0.1529 0.1681 0.1525 0.0071  -0.0095 -0.0248 55  LYS   A CA  
1271 C C   . LYS   A 55  ? 0.1463 0.1728 0.1486 -0.0062 0.0036  -0.0280 55  LYS   A C   
1272 O O   . LYS   A 55  ? 0.1575 0.1926 0.1587 0.0021  -0.0023 -0.0368 55  LYS   A O   
1273 C CB  . LYS   A 55  ? 0.1608 0.1769 0.1717 0.0162  -0.0080 -0.0282 55  LYS   A CB  
1274 C CG  . LYS   A 55  ? 0.1753 0.2015 0.1956 0.0272  -0.0201 -0.0361 55  LYS   A CG  
1275 C CD  . LYS   A 55  ? 0.1864 0.2242 0.2056 0.0342  -0.0058 -0.0321 55  LYS   A CD  
1276 C CE  . LYS   A 55  ? 0.2067 0.2606 0.2260 0.0369  -0.0124 -0.0320 55  LYS   A CE  
1277 N NZ  . LYS   A 55  ? 0.2160 0.2779 0.2347 0.0411  -0.0262 -0.0145 55  LYS   A NZ  
1291 N N   . ALA   A 56  ? 0.1625 0.1765 0.1553 -0.0118 0.0128  -0.0269 56  ALA   A N   
1292 C CA  . ALA   A 56  ? 0.1712 0.2004 0.1570 -0.0145 0.0144  -0.0339 56  ALA   A CA  
1293 C C   . ALA   A 56  ? 0.1795 0.2064 0.1357 -0.0111 0.0189  -0.0353 56  ALA   A C   
1294 O O   . ALA   A 56  ? 0.1882 0.2356 0.1507 -0.0009 0.0204  -0.0297 56  ALA   A O   
1295 C CB  . ALA   A 56  ? 0.1817 0.2198 0.1612 -0.0186 0.0189  -0.0138 56  ALA   A CB  
1301 N N   . THR   A 57  ? 0.1636 0.1832 0.1397 -0.0085 0.0149  -0.0295 57  THR   A N   
1302 C CA  . THR   A 57  ? 0.1621 0.1854 0.1423 -0.0120 -0.0012 -0.0253 57  THR   A CA  
1303 C C   . THR   A 57  ? 0.1593 0.1950 0.1515 -0.0089 -0.0064 -0.0333 57  THR   A C   
1304 O O   . THR   A 57  ? 0.1590 0.1980 0.1698 -0.0085 -0.0156 -0.0357 57  THR   A O   
1305 C CB  . THR   A 57  ? 0.1605 0.1835 0.1493 -0.0119 0.0029  -0.0236 57  THR   A CB  
1306 O OG1 . THR   A 57  ? 0.1504 0.1761 0.1502 -0.0078 0.0072  -0.0146 57  THR   A OG1 
1307 C CG2 . THR   A 57  ? 0.1642 0.1911 0.1307 -0.0132 -0.0015 -0.0087 57  THR   A CG2 
1315 N N   . ASN   A 58  ? 0.1592 0.1901 0.1685 -0.0131 0.0059  -0.0469 58  ASN   A N   
1316 C CA  . ASN   A 58  ? 0.1831 0.1815 0.1954 -0.0116 0.0163  -0.0569 58  ASN   A CA  
1317 C C   . ASN   A 58  ? 0.1654 0.1690 0.1815 -0.0032 -0.0006 -0.0353 58  ASN   A C   
1318 O O   . ASN   A 58  ? 0.1661 0.1764 0.1936 -0.0154 -0.0071 -0.0357 58  ASN   A O   
1319 C CB  . ASN   A 58  ? 0.2251 0.1965 0.2285 -0.0214 0.0476  -0.0746 58  ASN   A CB  
1320 C CG  . ASN   A 58  ? 0.2736 0.2195 0.3114 -0.0196 0.0464  -0.0568 58  ASN   A CG  
1321 O OD1 . ASN   A 58  ? 0.3043 0.2067 0.3631 0.0211  0.0798  -0.0535 58  ASN   A OD1 
1322 N ND2 . ASN   A 58  ? 0.2879 0.2360 0.3400 -0.0261 0.0268  -0.0494 58  ASN   A ND2 
1329 N N   . ASN   A 59  ? 0.1534 0.1545 0.1555 -0.0081 -0.0057 -0.0160 59  ASN   A N   
1330 C CA  . ASN   A 59  ? 0.1507 0.1433 0.1534 -0.0025 -0.0052 -0.0159 59  ASN   A CA  
1331 C C   . ASN   A 59  ? 0.1511 0.1500 0.1509 -0.0033 -0.0071 -0.0048 59  ASN   A C   
1332 O O   . ASN   A 59  ? 0.1477 0.1559 0.1499 -0.0074 -0.0009 -0.0022 59  ASN   A O   
1333 C CB  . ASN   A 59  ? 0.1528 0.1436 0.1655 0.0002  -0.0167 -0.0229 59  ASN   A CB  
1334 C CG  . ASN   A 59  ? 0.1522 0.1492 0.1745 0.0029  -0.0324 -0.0058 59  ASN   A CG  
1335 O OD1 . ASN   A 59  ? 0.1673 0.1602 0.1581 -0.0137 -0.0261 0.0004  59  ASN   A OD1 
1336 N ND2 . ASN   A 59  ? 0.1610 0.1483 0.2064 -0.0092 -0.0295 0.0031  59  ASN   A ND2 
1343 N N   . ALA   A 60  ? 0.1435 0.1497 0.1515 -0.0023 -0.0032 -0.0056 60  ALA   A N   
1344 C CA  . ALA   A 60  ? 0.1472 0.1533 0.1561 -0.0028 -0.0105 -0.0043 60  ALA   A CA  
1345 C C   . ALA   A 60  ? 0.1473 0.1510 0.1578 -0.0010 0.0010  -0.0137 60  ALA   A C   
1346 O O   . ALA   A 60  ? 0.1409 0.1520 0.1840 -0.0022 -0.0124 -0.0147 60  ALA   A O   
1347 C CB  . ALA   A 60  ? 0.1549 0.1657 0.1649 -0.0079 -0.0204 -0.0254 60  ALA   A CB  
1353 N N   . MET   A 61  ? 0.1460 0.1401 0.1539 -0.0118 -0.0040 -0.0116 61  MET   A N   
1354 C CA  . MET   A 61  ? 0.1366 0.1435 0.1481 -0.0085 0.0006  0.0046  61  MET   A CA  
1355 C C   . MET   A 61  ? 0.1326 0.1442 0.1486 -0.0069 0.0003  -0.0075 61  MET   A C   
1356 O O   . MET   A 61  ? 0.1340 0.1439 0.1573 -0.0067 0.0048  -0.0044 61  MET   A O   
1357 C CB  . MET   A 61  ? 0.1435 0.1456 0.1435 -0.0078 -0.0030 0.0003  61  MET   A CB  
1358 C CG  . MET   A 61  ? 0.1389 0.1542 0.1531 -0.0057 0.0061  -0.0021 61  MET   A CG  
1359 S SD  . MET   A 61  ? 0.1499 0.1545 0.1934 -0.0094 0.0017  -0.0211 61  MET   A SD  
1360 C CE  . MET   A 61  ? 0.1728 0.1631 0.2115 -0.0153 0.0158  -0.0235 61  MET   A CE  
1370 N N   . GLN   A 62  ? 0.1392 0.1376 0.1552 -0.0058 -0.0024 -0.0012 62  GLN   A N   
1371 C CA  . GLN   A 62  ? 0.1408 0.1326 0.1593 -0.0029 0.0040  0.0033  62  GLN   A CA  
1372 C C   . GLN   A 62  ? 0.1432 0.1230 0.1660 -0.0014 0.0069  -0.0028 62  GLN   A C   
1373 O O   . GLN   A 62  ? 0.1465 0.1479 0.1584 -0.0017 0.0058  -0.0039 62  GLN   A O   
1374 C CB  . GLN   A 62  ? 0.1422 0.1334 0.1720 -0.0044 0.0013  0.0004  62  GLN   A CB  
1375 C CG  . GLN   A 62  ? 0.1448 0.1292 0.1594 -0.0099 -0.0048 0.0058  62  GLN   A CG  
1376 C CD  . GLN   A 62  ? 0.1561 0.1373 0.1533 -0.0037 0.0103  0.0012  62  GLN   A CD  
1377 O OE1 . GLN   A 62  ? 0.1582 0.1518 0.1614 -0.0041 -0.0007 0.0000  62  GLN   A OE1 
1378 N NE2 . GLN   A 62  ? 0.1661 0.1360 0.1700 0.0011  0.0039  -0.0119 62  GLN   A NE2 
1387 N N   . VAL   A 63  ? 0.1379 0.1341 0.1727 -0.0093 0.0165  -0.0207 63  VAL   A N   
1388 C CA  . VAL   A 63  ? 0.1331 0.1535 0.1850 -0.0152 0.0027  -0.0226 63  VAL   A CA  
1389 C C   . VAL   A 63  ? 0.1325 0.1516 0.1732 -0.0144 -0.0017 -0.0235 63  VAL   A C   
1390 O O   . VAL   A 63  ? 0.1365 0.1501 0.1937 -0.0211 0.0044  -0.0153 63  VAL   A O   
1391 C CB  . VAL   A 63  ? 0.1510 0.1728 0.2252 -0.0149 -0.0001 -0.0449 63  VAL   A CB  
1392 C CG1 . VAL   A 63  ? 0.1609 0.1901 0.2677 -0.0178 -0.0064 -0.0659 63  VAL   A CG1 
1393 C CG2 . VAL   A 63  ? 0.1554 0.1705 0.2478 -0.0118 0.0088  -0.0390 63  VAL   A CG2 
1403 N N   . GLU   A 64  ? 0.1378 0.1573 0.1674 -0.0036 -0.0009 -0.0127 64  GLU   A N   
1404 C CA  . GLU   A 64  ? 0.1385 0.1487 0.1722 -0.0078 -0.0087 -0.0074 64  GLU   A CA  
1405 C C   . GLU   A 64  ? 0.1423 0.1387 0.1761 -0.0038 -0.0032 -0.0035 64  GLU   A C   
1406 O O   . GLU   A 64  ? 0.1489 0.1486 0.1748 -0.0024 -0.0019 -0.0054 64  GLU   A O   
1407 C CB  . GLU   A 64  ? 0.1415 0.1664 0.1855 -0.0103 -0.0015 -0.0066 64  GLU   A CB  
1408 C CG  . GLU   A 64  ? 0.1582 0.1692 0.1879 -0.0164 -0.0029 -0.0017 64  GLU   A CG  
1409 C CD  . GLU   A 64  ? 0.1680 0.1816 0.1896 -0.0196 0.0002  -0.0050 64  GLU   A CD  
1410 O OE1 . GLU   A 64  ? 0.1753 0.1903 0.2117 -0.0224 0.0139  -0.0002 64  GLU   A OE1 
1411 O OE2 . GLU   A 64  ? 0.1842 0.1865 0.1925 -0.0296 -0.0065 0.0042  64  GLU   A OE2 
1418 N N   . SER   A 65  ? 0.1398 0.1378 0.1643 -0.0039 -0.0071 -0.0011 65  SER   A N   
1419 C CA  . SER   A 65  ? 0.1432 0.1409 0.1523 -0.0059 -0.0033 -0.0042 65  SER   A CA  
1420 C C   . SER   A 65  ? 0.1443 0.1422 0.1539 -0.0053 -0.0013 -0.0049 65  SER   A C   
1421 O O   . SER   A 65  ? 0.1440 0.1501 0.1752 -0.0009 0.0150  -0.0123 65  SER   A O   
1422 C CB  . SER   A 65  ? 0.1421 0.1447 0.1546 -0.0151 -0.0049 -0.0004 65  SER   A CB  
1423 O OG  . SER   A 65  ? 0.1430 0.1546 0.1555 -0.0098 -0.0008 0.0106  65  SER   A OG  
1429 N N   . ASP   A 66  ? 0.1423 0.1418 0.1633 -0.0059 0.0131  -0.0020 66  ASP   A N   
1430 C CA  . ASP   A 66  ? 0.1549 0.1449 0.1777 -0.0021 0.0090  0.0125  66  ASP   A CA  
1431 C C   . ASP   A 66  ? 0.1433 0.1542 0.1947 -0.0114 0.0095  0.0197  66  ASP   A C   
1432 O O   . ASP   A 66  ? 0.1547 0.1633 0.2099 -0.0054 0.0236  0.0223  66  ASP   A O   
1433 C CB  . ASP   A 66  ? 0.1565 0.1622 0.2169 0.0051  0.0155  0.0281  66  ASP   A CB  
1434 C CG  . ASP   A 66  ? 0.1798 0.1738 0.2578 0.0001  0.0010  0.0457  66  ASP   A CG  
1435 O OD1 . ASP   A 66  ? 0.1805 0.1980 0.2245 -0.0039 -0.0092 0.0497  66  ASP   A OD1 
1436 O OD2 . ASP   A 66  ? 0.1922 0.1894 0.3463 0.0247  -0.0249 0.0175  66  ASP   A OD2 
1441 N N   . ASP   A 67  ? 0.1294 0.1569 0.2110 -0.0037 0.0081  0.0152  67  ASP   A N   
1442 C CA  . ASP   A 67  ? 0.1372 0.1718 0.2267 -0.0048 0.0026  0.0219  67  ASP   A CA  
1443 C C   . ASP   A 67  ? 0.1486 0.1680 0.2181 -0.0019 0.0152  0.0258  67  ASP   A C   
1444 O O   . ASP   A 67  ? 0.1507 0.1687 0.2314 -0.0006 0.0294  0.0324  67  ASP   A O   
1445 C CB  . ASP   A 67  ? 0.1538 0.1737 0.2574 -0.0045 -0.0246 0.0235  67  ASP   A CB  
1446 C CG  . ASP   A 67  ? 0.1592 0.1867 0.2808 -0.0151 -0.0380 0.0344  67  ASP   A CG  
1447 O OD1 . ASP   A 67  ? 0.1611 0.2017 0.3718 -0.0165 -0.0441 0.0497  67  ASP   A OD1 
1448 O OD2 . ASP   A 67  ? 0.1577 0.1935 0.2617 -0.0017 -0.0197 0.0258  67  ASP   A OD2 
1453 N N   . TYR   A 68  ? 0.1461 0.1513 0.2094 0.0040  0.0213  0.0224  68  TYR   A N   
1454 C CA  . TYR   A 68  ? 0.1512 0.1529 0.2040 0.0015  0.0273  0.0207  68  TYR   A CA  
1455 C C   . TYR   A 68  ? 0.1417 0.1535 0.1983 -0.0023 0.0317  0.0132  68  TYR   A C   
1456 O O   . TYR   A 68  ? 0.1509 0.1529 0.2037 0.0065  0.0254  0.0202  68  TYR   A O   
1457 C CB  . TYR   A 68  ? 0.1523 0.1422 0.2271 0.0049  0.0442  0.0217  68  TYR   A CB  
1458 C CG  . TYR   A 68  ? 0.1582 0.1742 0.2543 0.0046  0.0552  0.0196  68  TYR   A CG  
1459 C CD1 . TYR   A 68  ? 0.1683 0.1868 0.2763 -0.0184 0.0479  -0.0298 68  TYR   A CD1 
1460 C CD2 . TYR   A 68  ? 0.1833 0.1769 0.2867 0.0114  0.0577  0.0261  68  TYR   A CD2 
1461 C CE1 . TYR   A 68  ? 0.1754 0.1947 0.3165 -0.0191 0.0630  -0.0375 68  TYR   A CE1 
1462 C CE2 . TYR   A 68  ? 0.1802 0.1770 0.3277 -0.0029 0.0730  -0.0056 68  TYR   A CE2 
1463 C CZ  . TYR   A 68  ? 0.1839 0.1833 0.3370 -0.0200 0.0653  -0.0330 68  TYR   A CZ  
1464 O OH  . TYR   A 68  ? 0.2125 0.1898 0.3600 -0.0162 0.0435  -0.0584 68  TYR   A OH  
1474 N N   . ILE   A 69  ? 0.1417 0.1429 0.1912 0.0013  0.0240  0.0160  69  ILE   A N   
1475 C CA  . ILE   A 69  ? 0.1545 0.1494 0.1922 0.0044  0.0172  0.0060  69  ILE   A CA  
1476 C C   . ILE   A 69  ? 0.1504 0.1522 0.1877 0.0067  0.0261  0.0141  69  ILE   A C   
1477 O O   . ILE   A 69  ? 0.1622 0.1645 0.1808 -0.0045 0.0283  0.0165  69  ILE   A O   
1478 C CB  . ILE   A 69  ? 0.1602 0.1681 0.1974 0.0080  0.0166  -0.0028 69  ILE   A CB  
1479 C CG1 . ILE   A 69  ? 0.1724 0.1746 0.1948 0.0110  0.0173  -0.0175 69  ILE   A CG1 
1480 C CG2 . ILE   A 69  ? 0.1831 0.1948 0.2201 0.0173  0.0038  -0.0104 69  ILE   A CG2 
1481 C CD1 . ILE   A 69  ? 0.1745 0.1812 0.2084 0.0021  0.0101  -0.0114 69  ILE   A CD1 
1493 N N   . ALA   A 70  ? 0.1562 0.1529 0.1924 -0.0061 0.0222  0.0101  70  ALA   A N   
1494 C CA  . ALA   A 70  ? 0.1594 0.1644 0.2171 -0.0202 0.0348  0.0206  70  ALA   A CA  
1495 C C   . ALA   A 70  ? 0.1694 0.1852 0.2133 -0.0150 0.0384  0.0258  70  ALA   A C   
1496 O O   . ALA   A 70  ? 0.1849 0.2126 0.2492 0.0074  0.0588  0.0418  70  ALA   A O   
1497 C CB  . ALA   A 70  ? 0.1679 0.1619 0.2365 -0.0214 0.0347  0.0098  70  ALA   A CB  
1503 N N   . THR   A 71  ? 0.1579 0.1757 0.2079 -0.0018 0.0270  0.0194  71  THR   A N   
1504 C CA  . THR   A 71  ? 0.1722 0.1883 0.2455 0.0118  0.0287  0.0212  71  THR   A CA  
1505 C C   . THR   A 71  ? 0.1617 0.1872 0.2515 0.0140  0.0428  0.0154  71  THR   A C   
1506 O O   . THR   A 71  ? 0.1686 0.2159 0.2988 0.0081  0.0510  -0.0162 71  THR   A O   
1507 C CB  . THR   A 71  ? 0.1984 0.2073 0.2696 0.0259  -0.0132 0.0254  71  THR   A CB  
1508 O OG1 . THR   A 71  ? 0.2261 0.2274 0.2720 0.0236  -0.0413 0.0125  71  THR   A OG1 
1509 C CG2 . THR   A 71  ? 0.2101 0.2232 0.2978 0.0332  -0.0274 0.0329  71  THR   A CG2 
1517 N N   . ASN   A 72  ? 0.1592 0.1749 0.2216 0.0070  0.0291  0.0173  72  ASN   A N   
1518 C CA  . ASN   A 72  ? 0.1615 0.1710 0.2385 0.0155  0.0453  0.0136  72  ASN   A CA  
1519 C C   . ASN   A 72  ? 0.1693 0.1770 0.2264 0.0123  0.0600  0.0052  72  ASN   A C   
1520 O O   . ASN   A 72  ? 0.1857 0.1782 0.2493 0.0189  0.0511  -0.0041 72  ASN   A O   
1521 C CB  . ASN   A 72  ? 0.1801 0.1806 0.2380 0.0168  0.0384  0.0197  72  ASN   A CB  
1522 C CG  . ASN   A 72  ? 0.1987 0.1995 0.2382 0.0214  0.0349  0.0236  72  ASN   A CG  
1523 O OD1 . ASN   A 72  ? 0.2208 0.2295 0.2616 0.0236  0.0417  0.0342  72  ASN   A OD1 
1524 N ND2 . ASN   A 72  ? 0.2204 0.1969 0.2390 0.0460  0.0157  0.0124  72  ASN   A ND2 
1531 N N   . GLY   A 73  ? 0.1756 0.1722 0.2115 0.0018  0.0525  0.0032  73  GLY   A N   
1532 C CA  . GLY   A 73  ? 0.1850 0.1684 0.1931 -0.0103 0.0538  0.0092  73  GLY   A CA  
1533 C C   . GLY   A 73  ? 0.1824 0.1522 0.1736 0.0007  0.0597  0.0255  73  GLY   A C   
1534 O O   . GLY   A 73  ? 0.1712 0.1651 0.1972 0.0121  0.0350  0.0287  73  GLY   A O   
1538 N N   . PRO   A 74  ? 0.1999 0.1527 0.1882 -0.0124 0.0561  0.0170  74  PRO   A N   
1539 C CA  . PRO   A 74  ? 0.1960 0.1511 0.2006 -0.0063 0.0506  0.0171  74  PRO   A CA  
1540 C C   . PRO   A 74  ? 0.1865 0.1393 0.1836 0.0026  0.0332  0.0057  74  PRO   A C   
1541 O O   . PRO   A 74  ? 0.1836 0.1463 0.2112 -0.0007 0.0420  -0.0112 74  PRO   A O   
1542 C CB  . PRO   A 74  ? 0.2130 0.1759 0.2236 -0.0045 0.0492  0.0256  74  PRO   A CB  
1543 C CG  . PRO   A 74  ? 0.2393 0.2089 0.2664 -0.0186 0.0367  0.0116  74  PRO   A CG  
1544 C CD  . PRO   A 74  ? 0.2178 0.1861 0.2259 -0.0185 0.0427  0.0063  74  PRO   A CD  
1552 N N   . LEU   A 75  ? 0.1821 0.1379 0.1577 0.0012  0.0335  0.0049  75  LEU   A N   
1553 C CA  . LEU   A 75  ? 0.1833 0.1381 0.1482 0.0042  0.0160  0.0072  75  LEU   A CA  
1554 C C   . LEU   A 75  ? 0.1847 0.1531 0.1459 0.0069  0.0184  0.0127  75  LEU   A C   
1555 O O   . LEU   A 75  ? 0.2187 0.1714 0.1548 0.0119  0.0102  0.0054  75  LEU   A O   
1556 C CB  . LEU   A 75  ? 0.1858 0.1433 0.1422 -0.0047 0.0178  0.0169  75  LEU   A CB  
1557 C CG  . LEU   A 75  ? 0.2007 0.1753 0.1551 -0.0336 0.0108  0.0131  75  LEU   A CG  
1558 C CD1 . LEU   A 75  ? 0.2140 0.2240 0.1679 -0.0358 0.0073  0.0006  75  LEU   A CD1 
1559 C CD2 . LEU   A 75  ? 0.2350 0.2159 0.2324 -0.0130 0.0050  0.0253  75  LEU   A CD2 
1571 N N   . LYS   A 76  ? 0.1850 0.1543 0.1624 -0.0062 0.0107  -0.0010 76  LYS   A N   
1572 C CA  . LYS   A 76  ? 0.1738 0.1732 0.1701 -0.0043 0.0125  -0.0154 76  LYS   A CA  
1573 C C   . LYS   A 76  ? 0.1675 0.1579 0.1387 0.0019  0.0091  0.0021  76  LYS   A C   
1574 O O   . LYS   A 76  ? 0.1753 0.1511 0.1387 -0.0007 0.0144  0.0071  76  LYS   A O   
1575 C CB  . LYS   A 76  ? 0.1744 0.2048 0.2228 0.0095  0.0174  -0.0425 76  LYS   A CB  
1576 C CG  . LYS   A 76  ? 0.1858 0.1971 0.2741 0.0114  0.0146  -0.0375 76  LYS   A CG  
1577 C CD  . LYS   A 76  ? 0.1975 0.1953 0.3178 0.0141  0.0083  -0.0429 76  LYS   A CD  
1578 C CE  . LYS   A 76  ? 0.2170 0.2107 0.3770 -0.0000 0.0150  -0.0575 76  LYS   A CE  
1579 N NZ  . LYS   A 76  ? 0.2192 0.2005 0.4213 -0.0152 0.0150  -0.0702 76  LYS   A NZ  
1593 N N   . VAL   A 77  ? 0.1762 0.1630 0.1374 0.0037  0.0153  0.0151  77  VAL   A N   
1594 C CA  . VAL   A 77  ? 0.1761 0.1608 0.1439 0.0049  0.0097  0.0089  77  VAL   A CA  
1595 C C   . VAL   A 77  ? 0.1762 0.1568 0.1379 0.0110  0.0124  0.0016  77  VAL   A C   
1596 O O   . VAL   A 77  ? 0.1868 0.1657 0.1409 0.0155  0.0268  -0.0049 77  VAL   A O   
1597 C CB  . VAL   A 77  ? 0.1932 0.1776 0.1588 0.0026  0.0043  0.0210  77  VAL   A CB  
1598 C CG1 . VAL   A 77  ? 0.1944 0.1917 0.1752 0.0132  -0.0079 0.0154  77  VAL   A CG1 
1599 C CG2 . VAL   A 77  ? 0.2191 0.1869 0.1874 -0.0027 -0.0061 0.0264  77  VAL   A CG2 
1609 N N   . GLY   A 78  ? 0.1721 0.1519 0.1256 0.0098  0.0193  0.0086  78  GLY   A N   
1610 C CA  . GLY   A 78  ? 0.1667 0.1491 0.1431 0.0033  0.0274  0.0117  78  GLY   A CA  
1611 C C   . GLY   A 78  ? 0.1571 0.1483 0.1379 0.0067  0.0220  0.0151  78  GLY   A C   
1612 O O   . GLY   A 78  ? 0.1566 0.1518 0.1566 0.0017  0.0180  0.0201  78  GLY   A O   
1616 N N   . GLY   A 79  ? 0.1587 0.1495 0.1359 -0.0018 0.0169  0.0146  79  GLY   A N   
1617 C CA  . GLY   A 79  ? 0.1599 0.1501 0.1518 0.0039  0.0181  0.0109  79  GLY   A CA  
1618 C C   . GLY   A 79  ? 0.1458 0.1412 0.1440 0.0043  0.0135  0.0076  79  GLY   A C   
1619 O O   . GLY   A 79  ? 0.1519 0.1506 0.1461 0.0173  0.0141  0.0045  79  GLY   A O   
1623 N N   . SER   A 80  ? 0.1464 0.1514 0.1627 -0.0016 0.0129  -0.0012 80  SER   A N   
1624 C CA  . SER   A 80  ? 0.1460 0.1424 0.1499 -0.0015 0.0016  0.0046  80  SER   A CA  
1625 C C   . SER   A 80  ? 0.1469 0.1506 0.1492 0.0028  0.0063  0.0114  80  SER   A C   
1626 O O   . SER   A 80  ? 0.1486 0.1669 0.1781 0.0142  0.0096  0.0001  80  SER   A O   
1627 C CB  . SER   A 80  ? 0.1544 0.1464 0.1894 -0.0058 0.0100  0.0088  80  SER   A CB  
1628 O OG  . SER   A 80  ? 0.1777 0.1504 0.2237 0.0048  -0.0077 0.0259  80  SER   A OG  
1634 N N   . CYS   A 81  ? 0.1397 0.1446 0.1441 0.0003  -0.0010 0.0148  81  CYS   A N   
1635 C CA  . CYS   A 81  ? 0.1358 0.1530 0.1512 -0.0100 -0.0071 0.0230  81  CYS   A CA  
1636 C C   . CYS   A 81  ? 0.1364 0.1464 0.1550 -0.0099 -0.0106 0.0277  81  CYS   A C   
1637 O O   . CYS   A 81  ? 0.1349 0.1726 0.1672 -0.0016 -0.0014 0.0275  81  CYS   A O   
1638 C CB  . CYS   A 81  ? 0.1397 0.1550 0.1770 -0.0120 -0.0009 0.0192  81  CYS   A CB  
1639 S SG  . CYS   A 81  ? 0.1583 0.1482 0.1752 -0.0128 0.0015  0.0130  81  CYS   A SG  
1645 N N   . VAL   A 82  ? 0.1392 0.1558 0.1591 -0.0042 -0.0140 0.0165  82  VAL   A N   
1646 C CA  . VAL   A 82  ? 0.1494 0.1687 0.1540 -0.0051 -0.0077 0.0239  82  VAL   A CA  
1647 C C   . VAL   A 82  ? 0.1504 0.1737 0.1591 -0.0089 -0.0107 0.0167  82  VAL   A C   
1648 O O   . VAL   A 82  ? 0.1472 0.1789 0.1840 -0.0048 -0.0116 -0.0057 82  VAL   A O   
1649 C CB  . VAL   A 82  ? 0.1800 0.1838 0.1766 -0.0028 0.0015  0.0289  82  VAL   A CB  
1650 C CG1 . VAL   A 82  ? 0.2010 0.1979 0.1994 0.0070  0.0043  0.0328  82  VAL   A CG1 
1651 C CG2 . VAL   A 82  ? 0.1910 0.1828 0.1999 -0.0029 -0.0067 0.0295  82  VAL   A CG2 
1661 N N   . LEU   A 83  ? 0.1485 0.1717 0.1404 -0.0154 -0.0084 0.0106  83  LEU   A N   
1662 C CA  . LEU   A 83  ? 0.1511 0.1698 0.1416 -0.0117 -0.0072 0.0063  83  LEU   A CA  
1663 C C   . LEU   A 83  ? 0.1594 0.1702 0.1410 -0.0182 -0.0144 0.0117  83  LEU   A C   
1664 O O   . LEU   A 83  ? 0.1637 0.1734 0.1474 -0.0173 -0.0084 0.0189  83  LEU   A O   
1665 C CB  . LEU   A 83  ? 0.1590 0.1719 0.1533 -0.0132 -0.0089 0.0168  83  LEU   A CB  
1666 C CG  . LEU   A 83  ? 0.1704 0.1836 0.1624 -0.0137 0.0059  0.0110  83  LEU   A CG  
1667 C CD1 . LEU   A 83  ? 0.1807 0.1800 0.1611 -0.0240 0.0024  0.0250  83  LEU   A CD1 
1668 C CD2 . LEU   A 83  ? 0.1737 0.1935 0.1770 -0.0138 0.0157  0.0173  83  LEU   A CD2 
1680 N N   . SER   A 84  ? 0.1693 0.1737 0.1469 -0.0212 -0.0157 0.0070  84  SER   A N   
1681 C CA  . SER   A 84  ? 0.1797 0.1805 0.1340 -0.0169 -0.0136 0.0125  84  SER   A CA  
1682 C C   . SER   A 84  ? 0.1868 0.1744 0.1305 -0.0257 -0.0040 0.0092  84  SER   A C   
1683 O O   . SER   A 84  ? 0.1864 0.1901 0.1262 -0.0190 -0.0079 0.0091  84  SER   A O   
1684 C CB  . SER   A 84  ? 0.1884 0.1985 0.1524 -0.0156 -0.0043 -0.0035 84  SER   A CB  
1685 O OG  . SER   A 84  ? 0.1863 0.2155 0.1665 -0.0135 -0.0161 -0.0101 84  SER   A OG  
1691 N N   . GLY   A 85  ? 0.1970 0.1878 0.1429 -0.0292 0.0067  0.0025  85  GLY   A N   
1692 C CA  . GLY   A 85  ? 0.2034 0.1899 0.1541 -0.0318 0.0062  -0.0077 85  GLY   A CA  
1693 C C   . GLY   A 85  ? 0.1989 0.1939 0.1447 -0.0262 -0.0003 -0.0045 85  GLY   A C   
1694 O O   . GLY   A 85  ? 0.1998 0.2074 0.1572 -0.0304 0.0147  -0.0196 85  GLY   A O   
1698 N N   . HIS   A 86  ? 0.2002 0.1858 0.1332 -0.0282 -0.0034 0.0036  86  HIS   A N   
1699 C CA  . HIS   A 86  ? 0.2181 0.2021 0.1194 -0.0342 -0.0007 0.0085  86  HIS   A CA  
1700 C C   . HIS   A 86  ? 0.2410 0.2117 0.1270 -0.0342 0.0001  0.0062  86  HIS   A C   
1701 O O   . HIS   A 86  ? 0.2571 0.2373 0.1330 -0.0287 0.0091  0.0011  86  HIS   A O   
1702 C CB  . HIS   A 86  ? 0.2215 0.1999 0.1249 -0.0205 0.0126  0.0039  86  HIS   A CB  
1703 C CG  . HIS   A 86  ? 0.2081 0.2023 0.1402 -0.0139 0.0066  0.0072  86  HIS   A CG  
1704 N ND1 . HIS   A 86  ? 0.2082 0.1985 0.1807 -0.0261 -0.0019 0.0126  86  HIS   A ND1 
1705 C CD2 . HIS   A 86  ? 0.2072 0.1977 0.1343 -0.0008 0.0155  0.0095  86  HIS   A CD2 
1706 C CE1 . HIS   A 86  ? 0.2020 0.2032 0.1679 -0.0148 0.0173  0.0156  86  HIS   A CE1 
1707 N NE2 . HIS   A 86  ? 0.2007 0.2017 0.1468 0.0012  0.0198  0.0259  86  HIS   A NE2 
1715 N N   . ASN   A 87  ? 0.2525 0.2267 0.1474 -0.0269 0.0263  -0.0145 87  ASN   A N   
1716 C CA  . ASN   A 87  ? 0.2730 0.2358 0.1561 -0.0247 0.0536  -0.0239 87  ASN   A CA  
1717 C C   . ASN   A 87  ? 0.2736 0.2494 0.1905 -0.0276 0.0771  -0.0182 87  ASN   A C   
1718 O O   . ASN   A 87  ? 0.2994 0.2666 0.2307 -0.0407 0.1054  -0.0249 87  ASN   A O   
1719 C CB  . ASN   A 87  ? 0.2899 0.2432 0.1639 -0.0147 0.0478  -0.0272 87  ASN   A CB  
1720 C CG  . ASN   A 87  ? 0.3017 0.2533 0.1624 0.0017  0.0660  -0.0187 87  ASN   A CG  
1721 O OD1 . ASN   A 87  ? 0.3191 0.2511 0.1737 0.0226  0.0643  -0.0059 87  ASN   A OD1 
1722 N ND2 . ASN   A 87  ? 0.3034 0.2814 0.1737 0.0002  0.0687  -0.0091 87  ASN   A ND2 
1729 N N   . LEU   A 88  ? 0.2487 0.2417 0.1841 -0.0334 0.0552  -0.0063 88  LEU   A N   
1730 C CA  . LEU   A 88  ? 0.2316 0.2397 0.1990 -0.0390 0.0465  0.0143  88  LEU   A CA  
1731 C C   . LEU   A 88  ? 0.2223 0.2414 0.1855 -0.0351 0.0515  0.0309  88  LEU   A C   
1732 O O   . LEU   A 88  ? 0.2285 0.2485 0.2222 -0.0322 0.0472  0.0478  88  LEU   A O   
1733 C CB  . LEU   A 88  ? 0.2312 0.2499 0.2212 -0.0422 0.0100  0.0286  88  LEU   A CB  
1734 C CG  . LEU   A 88  ? 0.2426 0.2585 0.2538 -0.0435 -0.0060 0.0247  88  LEU   A CG  
1735 C CD1 . LEU   A 88  ? 0.2505 0.2689 0.2442 -0.0394 -0.0109 0.0099  88  LEU   A CD1 
1736 C CD2 . LEU   A 88  ? 0.2578 0.2668 0.2966 -0.0402 -0.0095 0.0167  88  LEU   A CD2 
1748 N N   . ALA   A 89  ? 0.2206 0.2321 0.1604 -0.0346 0.0285  0.0088  89  ALA   A N   
1749 C CA  . ALA   A 89  ? 0.2262 0.2327 0.1387 -0.0295 0.0111  0.0218  89  ALA   A CA  
1750 C C   . ALA   A 89  ? 0.2350 0.2327 0.1488 -0.0269 -0.0120 0.0187  89  ALA   A C   
1751 O O   . ALA   A 89  ? 0.2344 0.2324 0.1825 -0.0368 -0.0169 -0.0064 89  ALA   A O   
1752 C CB  . ALA   A 89  ? 0.2123 0.2302 0.1277 -0.0276 0.0071  0.0223  89  ALA   A CB  
1758 N N   . LYS   A 90  ? 0.2422 0.2475 0.1515 -0.0378 -0.0248 0.0236  90  LYS   A N   
1759 C CA  . LYS   A 90  ? 0.2472 0.2619 0.1538 -0.0343 -0.0278 0.0290  90  LYS   A CA  
1760 C C   . LYS   A 90  ? 0.2226 0.2487 0.1371 -0.0385 -0.0361 0.0154  90  LYS   A C   
1761 O O   . LYS   A 90  ? 0.2240 0.2720 0.1772 -0.0428 -0.0416 0.0036  90  LYS   A O   
1762 C CB  . LYS   A 90  ? 0.2734 0.2933 0.2008 -0.0303 -0.0334 0.0469  90  LYS   A CB  
1763 C CG  . LYS   A 90  ? 0.3184 0.3326 0.3041 -0.0266 -0.0375 0.0490  90  LYS   A CG  
1764 C CD  . LYS   A 90  ? 0.3544 0.3683 0.4021 -0.0278 -0.0299 0.0617  90  LYS   A CD  
1765 C CE  . LYS   A 90  ? 0.3672 0.3764 0.4836 -0.0291 -0.0176 0.0617  90  LYS   A CE  
1766 N NZ  . LYS   A 90  ? 0.4019 0.4073 0.5300 -0.0301 -0.0074 0.0507  90  LYS   A NZ  
1780 N N   . HIS   A 91  ? 0.2134 0.2173 0.1203 -0.0332 -0.0404 0.0199  91  HIS   A N   
1781 C CA  . HIS   A 91  ? 0.2079 0.1950 0.1246 -0.0274 -0.0377 0.0244  91  HIS   A CA  
1782 C C   . HIS   A 91  ? 0.1824 0.1840 0.1157 -0.0225 -0.0195 0.0194  91  HIS   A C   
1783 O O   . HIS   A 91  ? 0.1718 0.1955 0.1386 -0.0251 -0.0067 0.0171  91  HIS   A O   
1784 C CB  . HIS   A 91  ? 0.2289 0.2216 0.1897 -0.0050 -0.0530 0.0269  91  HIS   A CB  
1785 C CG  . HIS   A 91  ? 0.2736 0.2742 0.2646 0.0054  -0.0818 0.0140  91  HIS   A CG  
1786 N ND1 . HIS   A 91  ? 0.2842 0.2997 0.3066 0.0117  -0.0931 -0.0146 91  HIS   A ND1 
1787 C CD2 . HIS   A 91  ? 0.2921 0.2965 0.2910 0.0156  -0.0972 0.0235  91  HIS   A CD2 
1788 C CE1 . HIS   A 91  ? 0.2948 0.3076 0.3288 0.0176  -0.0904 -0.0002 91  HIS   A CE1 
1789 N NE2 . HIS   A 91  ? 0.3020 0.3087 0.3215 0.0235  -0.1016 0.0119  91  HIS   A NE2 
1797 N N   . CYS   A 92  ? 0.1646 0.1712 0.1145 -0.0193 -0.0186 0.0195  92  CYS   A N   
1798 C CA  . CYS   A 92  ? 0.1581 0.1644 0.1336 -0.0173 0.0011  0.0228  92  CYS   A CA  
1799 C C   . CYS   A 92  ? 0.1513 0.1624 0.1351 -0.0194 0.0026  0.0171  92  CYS   A C   
1800 O O   . CYS   A 92  ? 0.1580 0.1698 0.1394 -0.0267 -0.0057 0.0141  92  CYS   A O   
1801 C CB  . CYS   A 92  ? 0.1600 0.1664 0.1540 -0.0079 -0.0033 0.0138  92  CYS   A CB  
1802 S SG  . CYS   A 92  ? 0.1586 0.1557 0.1296 -0.0160 -0.0047 0.0069  92  CYS   A SG  
1808 N N   . LEU   A 93  ? 0.1458 0.1544 0.1378 -0.0163 0.0016  0.0171  93  LEU   A N   
1809 C CA  . LEU   A 93  ? 0.1292 0.1474 0.1370 -0.0110 -0.0039 0.0071  93  LEU   A CA  
1810 C C   . LEU   A 93  ? 0.1388 0.1448 0.1195 -0.0065 -0.0029 0.0055  93  LEU   A C   
1811 O O   . LEU   A 93  ? 0.1368 0.1507 0.1195 -0.0078 -0.0019 0.0097  93  LEU   A O   
1812 C CB  . LEU   A 93  ? 0.1404 0.1556 0.1466 -0.0062 -0.0082 0.0125  93  LEU   A CB  
1813 C CG  . LEU   A 93  ? 0.1525 0.1506 0.1442 -0.0112 -0.0019 0.0207  93  LEU   A CG  
1814 C CD1 . LEU   A 93  ? 0.1597 0.1567 0.1713 -0.0044 0.0044  0.0166  93  LEU   A CD1 
1815 C CD2 . LEU   A 93  ? 0.1702 0.1499 0.1515 -0.0115 -0.0027 0.0147  93  LEU   A CD2 
1827 N N   . HIS   A 94  ? 0.1310 0.1310 0.1251 -0.0028 0.0064  0.0117  94  HIS   A N   
1828 C CA  . HIS   A 94  ? 0.1285 0.1455 0.1150 -0.0069 0.0010  0.0093  94  HIS   A CA  
1829 C C   . HIS   A 94  ? 0.1357 0.1354 0.1289 -0.0068 0.0043  0.0058  94  HIS   A C   
1830 O O   . HIS   A 94  ? 0.1367 0.1501 0.1608 -0.0010 0.0044  -0.0070 94  HIS   A O   
1831 C CB  . HIS   A 94  ? 0.1344 0.1362 0.1315 -0.0057 -0.0009 0.0132  94  HIS   A CB  
1832 C CG  . HIS   A 94  ? 0.1375 0.1362 0.1186 -0.0043 0.0014  0.0135  94  HIS   A CG  
1833 N ND1 . HIS   A 94  ? 0.1404 0.1362 0.1305 -0.0026 -0.0024 0.0164  94  HIS   A ND1 
1834 C CD2 . HIS   A 94  ? 0.1426 0.1509 0.1320 -0.0067 -0.0077 0.0091  94  HIS   A CD2 
1835 C CE1 . HIS   A 94  ? 0.1412 0.1354 0.1293 -0.0098 -0.0117 0.0103  94  HIS   A CE1 
1836 N NE2 . HIS   A 94  ? 0.1460 0.1457 0.1282 -0.0064 -0.0062 -0.0014 94  HIS   A NE2 
1844 N N   . VAL   A 95  ? 0.1336 0.1314 0.1084 -0.0029 0.0023  -0.0003 95  VAL   A N   
1845 C CA  . VAL   A 95  ? 0.1345 0.1410 0.1116 -0.0090 0.0088  0.0127  95  VAL   A CA  
1846 C C   . VAL   A 95  ? 0.1373 0.1312 0.1063 -0.0148 -0.0031 -0.0016 95  VAL   A C   
1847 O O   . VAL   A 95  ? 0.1374 0.1499 0.1168 0.0110  0.0072  0.0056  95  VAL   A O   
1848 C CB  . VAL   A 95  ? 0.1366 0.1403 0.1393 -0.0125 0.0075  0.0008  95  VAL   A CB  
1849 C CG1 . VAL   A 95  ? 0.1549 0.1429 0.1501 -0.0207 0.0050  -0.0024 95  VAL   A CG1 
1850 C CG2 . VAL   A 95  ? 0.1438 0.1409 0.1428 -0.0187 0.0092  0.0189  95  VAL   A CG2 
1860 N N   . VAL   A 96  ? 0.1428 0.1328 0.0983 -0.0039 0.0031  0.0042  96  VAL   A N   
1861 C CA  . VAL   A 96  ? 0.1501 0.1385 0.1119 -0.0024 0.0070  0.0122  96  VAL   A CA  
1862 C C   . VAL   A 96  ? 0.1482 0.1561 0.1195 0.0031  0.0116  0.0114  96  VAL   A C   
1863 O O   . VAL   A 96  ? 0.1542 0.1636 0.1321 -0.0062 0.0182  -0.0023 96  VAL   A O   
1864 C CB  . VAL   A 96  ? 0.1553 0.1423 0.1311 -0.0026 0.0243  0.0088  96  VAL   A CB  
1865 C CG1 . VAL   A 96  ? 0.1659 0.1424 0.1258 -0.0033 0.0212  0.0108  96  VAL   A CG1 
1866 C CG2 . VAL   A 96  ? 0.1510 0.1494 0.1602 -0.0171 0.0178  0.0079  96  VAL   A CG2 
1876 N N   . GLY   A 97  ? 0.1459 0.1564 0.1206 -0.0036 0.0044  0.0088  97  GLY   A N   
1877 C CA  . GLY   A 97  ? 0.1635 0.1642 0.1257 0.0025  -0.0052 0.0103  97  GLY   A CA  
1878 C C   . GLY   A 97  ? 0.1590 0.1772 0.1202 -0.0091 -0.0047 0.0109  97  GLY   A C   
1879 O O   . GLY   A 97  ? 0.1703 0.1738 0.1430 -0.0143 0.0046  0.0200  97  GLY   A O   
1883 N N   A PRO   A 98  ? 0.1611 0.1742 0.1091 0.0021  -0.0124 0.0202  98  PRO   A N   
1884 N N   B PRO   A 98  ? 0.1693 0.1764 0.1306 -0.0062 -0.0058 0.0205  98  PRO   A N   
1885 C CA  A PRO   A 98  ? 0.1785 0.2038 0.1190 -0.0031 -0.0005 0.0064  98  PRO   A CA  
1886 C CA  B PRO   A 98  ? 0.1825 0.1855 0.1412 -0.0088 -0.0089 0.0194  98  PRO   A CA  
1887 C C   A PRO   A 98  ? 0.1841 0.2136 0.1081 -0.0129 0.0089  0.0274  98  PRO   A C   
1888 C C   B PRO   A 98  ? 0.2007 0.1870 0.1417 -0.0152 -0.0167 0.0322  98  PRO   A C   
1889 O O   A PRO   A 98  ? 0.1773 0.1944 0.1304 -0.0144 0.0047  0.0268  98  PRO   A O   
1890 O O   B PRO   A 98  ? 0.1974 0.1808 0.1595 -0.0164 -0.0172 0.0314  98  PRO   A O   
1891 C CB  A PRO   A 98  ? 0.1821 0.2113 0.1255 0.0084  0.0009  -0.0045 98  PRO   A CB  
1892 C CB  B PRO   A 98  ? 0.1802 0.1866 0.1400 -0.0036 -0.0029 0.0171  98  PRO   A CB  
1893 C CG  A PRO   A 98  ? 0.1780 0.2008 0.1284 0.0078  -0.0010 -0.0148 98  PRO   A CG  
1894 C CG  B PRO   A 98  ? 0.1799 0.1848 0.1413 -0.0054 -0.0042 0.0152  98  PRO   A CG  
1895 C CD  A PRO   A 98  ? 0.1702 0.1825 0.1151 0.0095  -0.0070 -0.0014 98  PRO   A CD  
1896 C CD  B PRO   A 98  ? 0.1737 0.1794 0.1335 -0.0048 -0.0055 0.0194  98  PRO   A CD  
1911 N N   A ASN   A 99  ? 0.1848 0.2386 0.1172 -0.0081 0.0109  0.0419  99  ASN   A N   
1912 N N   B ASN   A 99  ? 0.2202 0.1935 0.1426 -0.0157 -0.0185 0.0446  99  ASN   A N   
1913 C CA  A ASN   A 99  ? 0.1962 0.2542 0.1298 -0.0164 -0.0007 0.0783  99  ASN   A CA  
1914 C CA  B ASN   A 99  ? 0.2397 0.1973 0.1554 -0.0175 -0.0222 0.0586  99  ASN   A CA  
1915 C C   A ASN   A 99  ? 0.2145 0.2920 0.1165 -0.0317 -0.0040 0.0827  99  ASN   A C   
1916 C C   B ASN   A 99  ? 0.2514 0.2105 0.1726 -0.0156 -0.0287 0.0372  99  ASN   A C   
1917 O O   A ASN   A 99  ? 0.2262 0.3122 0.1350 -0.0313 -0.0114 0.0708  99  ASN   A O   
1918 O O   B ASN   A 99  ? 0.2484 0.1920 0.1687 -0.0145 -0.0429 0.0203  99  ASN   A O   
1919 C CB  A ASN   A 99  ? 0.1901 0.2479 0.1555 -0.0157 -0.0043 0.0638  99  ASN   A CB  
1920 C CB  B ASN   A 99  ? 0.2475 0.1945 0.1670 -0.0188 -0.0223 0.0733  99  ASN   A CB  
1921 C CG  A ASN   A 99  ? 0.1952 0.2418 0.1593 -0.0052 -0.0053 0.0440  99  ASN   A CG  
1922 C CG  B ASN   A 99  ? 0.2544 0.1936 0.1753 -0.0234 -0.0197 0.0892  99  ASN   A CG  
1923 O OD1 A ASN   A 99  ? 0.2052 0.2495 0.1741 0.0118  -0.0029 0.0284  99  ASN   A OD1 
1924 O OD1 B ASN   A 99  ? 0.2583 0.1985 0.1629 -0.0239 -0.0178 0.1008  99  ASN   A OD1 
1925 N ND2 A ASN   A 99  ? 0.2023 0.2362 0.1780 -0.0033 -0.0005 0.0673  99  ASN   A ND2 
1926 N ND2 B ASN   A 99  ? 0.2563 0.1904 0.2014 -0.0214 -0.0220 0.0805  99  ASN   A ND2 
1939 N N   A VAL   A 100 ? 0.2319 0.3211 0.1279 -0.0497 -0.0323 0.0798  100 VAL   A N   
1940 N N   B VAL   A 100 ? 0.2657 0.2424 0.2008 -0.0182 -0.0226 0.0264  100 VAL   A N   
1941 C CA  A VAL   A 100 ? 0.2553 0.3553 0.1771 -0.0596 -0.0383 0.0769  100 VAL   A CA  
1942 C CA  B VAL   A 100 ? 0.2811 0.2736 0.2382 -0.0194 -0.0164 0.0249  100 VAL   A CA  
1943 C C   A VAL   A 100 ? 0.2625 0.3791 0.1706 -0.0741 -0.0437 0.1161  100 VAL   A C   
1944 C C   B VAL   A 100 ? 0.2961 0.3021 0.2601 -0.0213 -0.0128 0.0351  100 VAL   A C   
1945 O O   A VAL   A 100 ? 0.2706 0.3959 0.2083 -0.0741 -0.0168 0.1124  100 VAL   A O   
1946 O O   B VAL   A 100 ? 0.3007 0.3146 0.2698 -0.0218 -0.0098 0.0358  100 VAL   A O   
1947 C CB  A VAL   A 100 ? 0.2737 0.3617 0.2124 -0.0565 -0.0486 0.0547  100 VAL   A CB  
1948 C CB  B VAL   A 100 ? 0.2819 0.2756 0.2489 -0.0200 -0.0196 0.0210  100 VAL   A CB  
1949 C CG1 A VAL   A 100 ? 0.2780 0.3669 0.2325 -0.0584 -0.0395 0.0500  100 VAL   A CG1 
1950 C CG1 B VAL   A 100 ? 0.2834 0.2780 0.2559 -0.0191 -0.0204 0.0204  100 VAL   A CG1 
1951 C CG2 A VAL   A 100 ? 0.2849 0.3695 0.2145 -0.0552 -0.0498 0.0414  100 VAL   A CG2 
1952 C CG2 B VAL   A 100 ? 0.2818 0.2764 0.2461 -0.0198 -0.0197 0.0167  100 VAL   A CG2 
1971 N N   A ASN   A 101 ? 0.2698 0.3815 0.2022 -0.0730 -0.0550 0.1405  101 ASN   A N   
1972 N N   B ASN   A 101 ? 0.3057 0.3141 0.2828 -0.0222 -0.0130 0.0449  101 ASN   A N   
1973 C CA  A ASN   A 101 ? 0.2974 0.3914 0.2465 -0.0784 -0.0568 0.1687  101 ASN   A CA  
1974 C CA  B ASN   A 101 ? 0.3152 0.3215 0.3002 -0.0221 -0.0134 0.0498  101 ASN   A CA  
1975 C C   A ASN   A 101 ? 0.3256 0.4116 0.2646 -0.0783 -0.0235 0.1805  101 ASN   A C   
1976 C C   B ASN   A 101 ? 0.3296 0.3285 0.3200 -0.0210 -0.0034 0.0500  101 ASN   A C   
1977 O O   A ASN   A 101 ? 0.3465 0.4259 0.3215 -0.0776 -0.0199 0.1758  101 ASN   A O   
1978 O O   B ASN   A 101 ? 0.3349 0.3302 0.3381 -0.0200 -0.0037 0.0441  101 ASN   A O   
1979 C CB  A ASN   A 101 ? 0.2955 0.3694 0.2493 -0.0736 -0.0829 0.1606  101 ASN   A CB  
1980 C CB  B ASN   A 101 ? 0.3105 0.3189 0.2949 -0.0216 -0.0194 0.0454  101 ASN   A CB  
1981 C CG  A ASN   A 101 ? 0.2971 0.3545 0.2468 -0.0749 -0.0922 0.1288  101 ASN   A CG  
1982 C CG  B ASN   A 101 ? 0.3060 0.3117 0.2838 -0.0206 -0.0221 0.0373  101 ASN   A CG  
1983 O OD1 A ASN   A 101 ? 0.2968 0.3597 0.2702 -0.0737 -0.0963 0.0817  101 ASN   A OD1 
1984 O OD1 B ASN   A 101 ? 0.3044 0.3117 0.2802 -0.0137 -0.0221 0.0246  101 ASN   A OD1 
1985 N ND2 A ASN   A 101 ? 0.2984 0.3413 0.2609 -0.0765 -0.0878 0.1311  101 ASN   A ND2 
1986 N ND2 B ASN   A 101 ? 0.3037 0.3066 0.2824 -0.0240 -0.0270 0.0381  101 ASN   A ND2 
1999 N N   A LYS   A 102 ? 0.3326 0.4392 0.2767 -0.0962 -0.0067 0.1802  102 LYS   A N   
2000 N N   B LYS   A 102 ? 0.3376 0.3320 0.3189 -0.0214 0.0047  0.0482  102 LYS   A N   
2001 C CA  A LYS   A 102 ? 0.3507 0.4633 0.2823 -0.0933 -0.0097 0.1550  102 LYS   A CA  
2002 C CA  B LYS   A 102 ? 0.3450 0.3344 0.3120 -0.0217 0.0087  0.0459  102 LYS   A CA  
2003 C C   A LYS   A 102 ? 0.3605 0.4835 0.2610 -0.0827 -0.0040 0.1359  102 LYS   A C   
2004 C C   B LYS   A 102 ? 0.3428 0.3286 0.2880 -0.0220 0.0004  0.0561  102 LYS   A C   
2005 O O   A LYS   A 102 ? 0.3689 0.4993 0.2584 -0.0753 -0.0001 0.1202  102 LYS   A O   
2006 O O   B LYS   A 102 ? 0.3449 0.3273 0.2863 -0.0246 -0.0023 0.0590  102 LYS   A O   
2007 C CB  A LYS   A 102 ? 0.3603 0.4658 0.3221 -0.0950 -0.0235 0.1373  102 LYS   A CB  
2008 C CB  B LYS   A 102 ? 0.3534 0.3421 0.3334 -0.0233 0.0145  0.0299  102 LYS   A CB  
2009 C CG  A LYS   A 102 ? 0.3681 0.4693 0.3522 -0.0937 -0.0368 0.1097  102 LYS   A CG  
2010 C CG  B LYS   A 102 ? 0.3597 0.3471 0.3572 -0.0248 0.0190  0.0156  102 LYS   A CG  
2011 C CD  A LYS   A 102 ? 0.3767 0.4723 0.3872 -0.0931 -0.0527 0.0793  102 LYS   A CD  
2012 C CD  B LYS   A 102 ? 0.3641 0.3512 0.3810 -0.0263 0.0227  0.0032  102 LYS   A CD  
2013 C CE  A LYS   A 102 ? 0.3837 0.4747 0.4062 -0.0927 -0.0608 0.0616  102 LYS   A CE  
2014 C CE  B LYS   A 102 ? 0.3666 0.3552 0.3989 -0.0274 0.0222  -0.0061 102 LYS   A CE  
2015 N NZ  A LYS   A 102 ? 0.3871 0.4745 0.4249 -0.0980 -0.0563 0.0478  102 LYS   A NZ  
2016 N NZ  B LYS   A 102 ? 0.3678 0.3581 0.4106 -0.0274 0.0222  -0.0097 102 LYS   A NZ  
2043 N N   A GLY   A 103 ? 0.3597 0.4919 0.2633 -0.0742 -0.0132 0.1093  103 GLY   A N   
2044 N N   B GLY   A 103 ? 0.3376 0.3258 0.2709 -0.0193 -0.0089 0.0573  103 GLY   A N   
2045 C CA  A GLY   A 103 ? 0.3619 0.4958 0.2570 -0.0622 -0.0114 0.0877  103 GLY   A CA  
2046 C CA  B GLY   A 103 ? 0.3325 0.3222 0.2576 -0.0199 -0.0155 0.0642  103 GLY   A CA  
2047 C C   A GLY   A 103 ? 0.3580 0.4996 0.2555 -0.0530 -0.0015 0.0657  103 GLY   A C   
2048 C C   B GLY   A 103 ? 0.3252 0.3171 0.2360 -0.0230 -0.0154 0.0702  103 GLY   A C   
2049 O O   A GLY   A 103 ? 0.3698 0.5068 0.2725 -0.0466 0.0050  0.0486  103 GLY   A O   
2050 O O   B GLY   A 103 ? 0.3265 0.3136 0.2195 -0.0266 -0.0166 0.0822  103 GLY   A O   
2057 N N   A GLU   A 104 ? 0.3355 0.4905 0.2050 -0.0568 0.0059  0.0575  104 GLU   A N   
2058 N N   B GLU   A 104 ? 0.3167 0.3154 0.2303 -0.0216 -0.0190 0.0637  104 GLU   A N   
2059 C CA  A GLU   A 104 ? 0.3071 0.4765 0.1780 -0.0670 0.0126  0.0466  104 GLU   A CA  
2060 C CA  B GLU   A 104 ? 0.3087 0.3134 0.2302 -0.0227 -0.0230 0.0488  104 GLU   A CA  
2061 C C   A GLU   A 104 ? 0.3042 0.4799 0.1709 -0.0705 0.0186  0.0234  104 GLU   A C   
2062 C C   B GLU   A 104 ? 0.3108 0.3168 0.2437 -0.0198 -0.0165 0.0368  104 GLU   A C   
2063 O O   A GLU   A 104 ? 0.2932 0.4804 0.1991 -0.0742 0.0032  0.0199  104 GLU   A O   
2064 O O   B GLU   A 104 ? 0.3073 0.3108 0.2437 -0.0195 -0.0163 0.0460  104 GLU   A O   
2065 C CB  A GLU   A 104 ? 0.2794 0.4559 0.1516 -0.0695 0.0232  0.0649  104 GLU   A CB  
2066 C CB  B GLU   A 104 ? 0.3002 0.3097 0.2231 -0.0250 -0.0299 0.0455  104 GLU   A CB  
2067 C CG  A GLU   A 104 ? 0.2609 0.4376 0.1662 -0.0667 0.0226  0.0792  104 GLU   A CG  
2068 C CG  B GLU   A 104 ? 0.2946 0.3063 0.2282 -0.0252 -0.0381 0.0439  104 GLU   A CG  
2069 C CD  A GLU   A 104 ? 0.2347 0.4224 0.1629 -0.0637 0.0264  0.0905  104 GLU   A CD  
2070 C CD  B GLU   A 104 ? 0.2888 0.3027 0.2311 -0.0249 -0.0445 0.0436  104 GLU   A CD  
2071 O OE1 A GLU   A 104 ? 0.2185 0.4032 0.1384 -0.0596 0.0080  0.0809  104 GLU   A OE1 
2072 O OE1 B GLU   A 104 ? 0.2872 0.3010 0.2254 -0.0233 -0.0523 0.0430  104 GLU   A OE1 
2073 O OE2 A GLU   A 104 ? 0.2527 0.4176 0.1898 -0.0588 0.0302  0.1161  104 GLU   A OE2 
2074 O OE2 B GLU   A 104 ? 0.2900 0.3012 0.2465 -0.0266 -0.0413 0.0450  104 GLU   A OE2 
2087 N N   A ASP   A 105 ? 0.3126 0.4816 0.1838 -0.0677 0.0374  -0.0041 105 ASP   A N   
2088 N N   B ASP   A 105 ? 0.3197 0.3289 0.2620 -0.0198 -0.0094 0.0176  105 ASP   A N   
2089 C CA  A ASP   A 105 ? 0.3210 0.4842 0.2255 -0.0622 0.0461  -0.0385 105 ASP   A CA  
2090 C CA  B ASP   A 105 ? 0.3277 0.3396 0.2862 -0.0179 -0.0023 -0.0034 105 ASP   A CA  
2091 C C   A ASP   A 105 ? 0.2888 0.4648 0.1830 -0.0728 0.0354  -0.0666 105 ASP   A C   
2092 C C   B ASP   A 105 ? 0.3234 0.3419 0.2790 -0.0221 0.0010  -0.0130 105 ASP   A C   
2093 O O   A ASP   A 105 ? 0.2713 0.4405 0.1457 -0.0722 0.0282  -0.0846 105 ASP   A O   
2094 O O   B ASP   A 105 ? 0.3214 0.3433 0.2699 -0.0219 0.0016  -0.0146 105 ASP   A O   
2095 C CB  A ASP   A 105 ? 0.3556 0.4989 0.3007 -0.0487 0.0571  -0.0503 105 ASP   A CB  
2096 C CB  B ASP   A 105 ? 0.3388 0.3459 0.3155 -0.0129 -0.0007 -0.0138 105 ASP   A CB  
2097 C CG  A ASP   A 105 ? 0.3827 0.5125 0.3687 -0.0385 0.0606  -0.0610 105 ASP   A CG  
2098 C CG  B ASP   A 105 ? 0.3478 0.3497 0.3381 -0.0072 -0.0015 -0.0226 105 ASP   A CG  
2099 O OD1 A ASP   A 105 ? 0.3893 0.5185 0.3761 -0.0410 0.0592  -0.0738 105 ASP   A OD1 
2100 O OD1 B ASP   A 105 ? 0.3542 0.3488 0.3401 -0.0057 -0.0046 -0.0262 105 ASP   A OD1 
2101 O OD2 A ASP   A 105 ? 0.4041 0.5163 0.4102 -0.0334 0.0661  -0.0538 105 ASP   A OD2 
2102 O OD2 B ASP   A 105 ? 0.3498 0.3533 0.3579 -0.0072 -0.0033 -0.0234 105 ASP   A OD2 
2111 N N   A ILE   A 106 ? 0.2747 0.4414 0.2148 -0.0714 0.0059  -0.0601 106 ILE   A N   
2112 N N   B ILE   A 106 ? 0.3215 0.3419 0.2860 -0.0260 -0.0004 -0.0182 106 ILE   A N   
2113 C CA  A ILE   A 106 ? 0.2508 0.4180 0.2321 -0.0820 -0.0218 -0.0753 106 ILE   A CA  
2114 C CA  B ILE   A 106 ? 0.3179 0.3411 0.2947 -0.0329 -0.0008 -0.0240 106 ILE   A CA  
2115 C C   A ILE   A 106 ? 0.2373 0.3901 0.2373 -0.0974 -0.0098 -0.0965 106 ILE   A C   
2116 C C   B ILE   A 106 ? 0.3122 0.3324 0.2953 -0.0397 0.0077  -0.0323 106 ILE   A C   
2117 O O   A ILE   A 106 ? 0.2114 0.3771 0.2450 -0.1046 0.0063  -0.1025 106 ILE   A O   
2118 O O   B ILE   A 106 ? 0.3105 0.3315 0.2931 -0.0384 0.0088  -0.0365 106 ILE   A O   
2119 C CB  A ILE   A 106 ? 0.2523 0.4314 0.2899 -0.0717 -0.0439 -0.0486 106 ILE   A CB  
2120 C CB  B ILE   A 106 ? 0.3217 0.3491 0.3110 -0.0319 -0.0074 -0.0169 106 ILE   A CB  
2121 C CG1 A ILE   A 106 ? 0.2383 0.4376 0.3203 -0.0610 -0.0536 -0.0272 106 ILE   A CG1 
2122 C CG1 B ILE   A 106 ? 0.3221 0.3538 0.3209 -0.0298 -0.0110 -0.0091 106 ILE   A CG1 
2123 C CG2 A ILE   A 106 ? 0.2624 0.4345 0.3072 -0.0691 -0.0467 -0.0488 106 ILE   A CG2 
2124 C CG2 B ILE   A 106 ? 0.3236 0.3505 0.3161 -0.0318 -0.0093 -0.0173 106 ILE   A CG2 
2125 C CD1 A ILE   A 106 ? 0.2383 0.4390 0.3413 -0.0484 -0.0448 -0.0236 106 ILE   A CD1 
2126 C CD1 B ILE   A 106 ? 0.3234 0.3554 0.3251 -0.0272 -0.0110 -0.0069 106 ILE   A CD1 
2149 N N   A GLN   A 107 ? 0.2597 0.3719 0.2550 -0.0925 0.0043  -0.1148 107 GLN   A N   
2150 N N   B GLN   A 107 ? 0.3085 0.3222 0.3051 -0.0460 0.0167  -0.0386 107 GLN   A N   
2151 C CA  A GLN   A 107 ? 0.2860 0.3516 0.3424 -0.0720 0.0362  -0.1035 107 GLN   A CA  
2152 C CA  B GLN   A 107 ? 0.3035 0.3109 0.3283 -0.0491 0.0291  -0.0474 107 GLN   A CA  
2153 C C   A GLN   A 107 ? 0.2608 0.2989 0.3309 -0.0592 0.0594  -0.0758 107 GLN   A C   
2154 C C   B GLN   A 107 ? 0.2724 0.2832 0.3033 -0.0528 0.0452  -0.0544 107 GLN   A C   
2155 O O   A GLN   A 107 ? 0.2671 0.2945 0.3957 -0.0480 0.0660  -0.0719 107 GLN   A O   
2156 O O   B GLN   A 107 ? 0.2774 0.2835 0.3275 -0.0516 0.0440  -0.0486 107 GLN   A O   
2157 C CB  A GLN   A 107 ? 0.3295 0.3825 0.4317 -0.0747 0.0225  -0.1098 107 GLN   A CB  
2158 C CB  B GLN   A 107 ? 0.3258 0.3261 0.3762 -0.0504 0.0200  -0.0406 107 GLN   A CB  
2159 C CG  A GLN   A 107 ? 0.3677 0.4139 0.5357 -0.0726 0.0116  -0.1015 107 GLN   A CG  
2160 C CG  B GLN   A 107 ? 0.3467 0.3414 0.4265 -0.0514 0.0126  -0.0321 107 GLN   A CG  
2161 C CD  A GLN   A 107 ? 0.3924 0.4354 0.6204 -0.0726 0.0113  -0.0859 107 GLN   A CD  
2162 C CD  B GLN   A 107 ? 0.3658 0.3568 0.4689 -0.0501 0.0094  -0.0236 107 GLN   A CD  
2163 O OE1 A GLN   A 107 ? 0.4139 0.4446 0.6573 -0.0706 0.0109  -0.0837 107 GLN   A OE1 
2164 O OE1 B GLN   A 107 ? 0.3687 0.3612 0.4833 -0.0494 0.0102  -0.0194 107 GLN   A OE1 
2165 N NE2 A GLN   A 107 ? 0.4096 0.4515 0.6483 -0.0776 0.0106  -0.0816 107 GLN   A NE2 
2166 N NE2 B GLN   A 107 ? 0.3753 0.3642 0.4853 -0.0514 0.0064  -0.0219 107 GLN   A NE2 
2183 N N   . LEU   A 108 ? 0.2358 0.2534 0.2608 -0.0579 0.0542  -0.0650 108 LEU   A N   
2184 C CA  . LEU   A 108 ? 0.2052 0.2092 0.2087 -0.0278 0.0404  -0.0241 108 LEU   A CA  
2185 C C   . LEU   A 108 ? 0.1739 0.1739 0.2076 -0.0099 0.0302  0.0043  108 LEU   A C   
2186 O O   . LEU   A 108 ? 0.1755 0.1630 0.2322 0.0017  0.0347  0.0041  108 LEU   A O   
2187 C CB  . LEU   A 108 ? 0.2134 0.2168 0.1853 -0.0231 0.0455  -0.0193 108 LEU   A CB  
2188 C CG  . LEU   A 108 ? 0.2226 0.2403 0.2240 -0.0211 0.0538  -0.0184 108 LEU   A CG  
2189 C CD1 . LEU   A 108 ? 0.2339 0.2478 0.2222 -0.0307 0.0688  -0.0118 108 LEU   A CD1 
2190 C CD2 . LEU   A 108 ? 0.2222 0.2621 0.2731 -0.0107 0.0522  -0.0055 108 LEU   A CD2 
2203 N N   . LEU   A 109 ? 0.1588 0.1632 0.1990 -0.0004 0.0217  0.0155  109 LEU   A N   
2204 C CA  . LEU   A 109 ? 0.1568 0.1633 0.1728 -0.0010 0.0057  0.0169  109 LEU   A CA  
2205 C C   . LEU   A 109 ? 0.1530 0.1533 0.1562 -0.0087 0.0139  0.0046  109 LEU   A C   
2206 O O   . LEU   A 109 ? 0.1574 0.1451 0.1729 -0.0064 0.0024  -0.0009 109 LEU   A O   
2207 C CB  . LEU   A 109 ? 0.1636 0.1680 0.1921 0.0116  0.0060  0.0307  109 LEU   A CB  
2208 C CG  . LEU   A 109 ? 0.1584 0.1781 0.1990 0.0046  0.0103  0.0313  109 LEU   A CG  
2209 C CD1 . LEU   A 109 ? 0.1613 0.1672 0.2249 0.0012  0.0126  0.0018  109 LEU   A CD1 
2210 C CD2 . LEU   A 109 ? 0.1645 0.1940 0.2246 -0.0008 0.0046  0.0287  109 LEU   A CD2 
2222 N N   . LYS   A 110 ? 0.1537 0.1503 0.1651 -0.0063 0.0029  0.0020  110 LYS   A N   
2223 C CA  . LYS   A 110 ? 0.1536 0.1456 0.1766 -0.0090 -0.0050 0.0080  110 LYS   A CA  
2224 C C   . LYS   A 110 ? 0.1561 0.1350 0.1601 -0.0099 0.0000  -0.0018 110 LYS   A C   
2225 O O   . LYS   A 110 ? 0.1453 0.1382 0.1747 -0.0103 0.0064  -0.0055 110 LYS   A O   
2226 C CB  . LYS   A 110 ? 0.1600 0.1488 0.2059 -0.0087 -0.0150 -0.0051 110 LYS   A CB  
2227 C CG  . LYS   A 110 ? 0.1624 0.1483 0.2031 -0.0035 -0.0136 -0.0045 110 LYS   A CG  
2228 C CD  . LYS   A 110 ? 0.1699 0.1593 0.2117 -0.0129 -0.0111 -0.0078 110 LYS   A CD  
2229 C CE  . LYS   A 110 ? 0.1747 0.1651 0.2439 -0.0166 0.0051  -0.0108 110 LYS   A CE  
2230 N NZ  . LYS   A 110 ? 0.1761 0.1709 0.2407 -0.0265 0.0183  -0.0112 110 LYS   A NZ  
2244 N N   . SER   A 111 ? 0.1578 0.1471 0.1636 -0.0008 -0.0006 0.0050  111 SER   A N   
2245 C CA  . SER   A 111 ? 0.1540 0.1516 0.1509 -0.0010 0.0077  0.0037  111 SER   A CA  
2246 C C   . SER   A 111 ? 0.1419 0.1463 0.1610 -0.0054 0.0040  0.0012  111 SER   A C   
2247 O O   . SER   A 111 ? 0.1521 0.1327 0.1865 -0.0034 0.0075  0.0036  111 SER   A O   
2248 C CB  . SER   A 111 ? 0.1699 0.1768 0.1730 -0.0057 0.0194  -0.0153 111 SER   A CB  
2249 O OG  . SER   A 111 ? 0.2149 0.1951 0.1826 0.0003  0.0226  -0.0142 111 SER   A OG  
2255 N N   . ALA   A 112 ? 0.1481 0.1394 0.1719 -0.0023 0.0125  -0.0012 112 ALA   A N   
2256 C CA  . ALA   A 112 ? 0.1418 0.1371 0.1546 -0.0072 0.0189  -0.0015 112 ALA   A CA  
2257 C C   . ALA   A 112 ? 0.1362 0.1292 0.1752 0.0027  0.0092  0.0015  112 ALA   A C   
2258 O O   . ALA   A 112 ? 0.1432 0.1365 0.1762 -0.0137 0.0083  0.0088  112 ALA   A O   
2259 C CB  . ALA   A 112 ? 0.1558 0.1405 0.1698 -0.0085 0.0071  -0.0015 112 ALA   A CB  
2265 N N   . TYR   A 113 ? 0.1238 0.1377 0.1836 -0.0081 0.0083  0.0030  113 TYR   A N   
2266 C CA  . TYR   A 113 ? 0.1311 0.1326 0.1674 -0.0118 0.0231  0.0138  113 TYR   A CA  
2267 C C   . TYR   A 113 ? 0.1357 0.1310 0.1626 -0.0149 0.0068  0.0105  113 TYR   A C   
2268 O O   . TYR   A 113 ? 0.1403 0.1407 0.1645 -0.0073 0.0145  0.0024  113 TYR   A O   
2269 C CB  . TYR   A 113 ? 0.1357 0.1461 0.1670 -0.0007 -0.0008 0.0204  113 TYR   A CB  
2270 C CG  . TYR   A 113 ? 0.1422 0.1410 0.1550 -0.0146 0.0120  0.0206  113 TYR   A CG  
2271 C CD1 . TYR   A 113 ? 0.1378 0.1514 0.1673 0.0006  0.0101  0.0269  113 TYR   A CD1 
2272 C CD2 . TYR   A 113 ? 0.1531 0.1483 0.1511 -0.0132 0.0122  0.0183  113 TYR   A CD2 
2273 C CE1 . TYR   A 113 ? 0.1443 0.1567 0.1599 -0.0057 0.0081  0.0231  113 TYR   A CE1 
2274 C CE2 . TYR   A 113 ? 0.1475 0.1481 0.1558 -0.0111 0.0098  0.0146  113 TYR   A CE2 
2275 C CZ  . TYR   A 113 ? 0.1399 0.1497 0.1570 -0.0001 0.0165  0.0295  113 TYR   A CZ  
2276 O OH  . TYR   A 113 ? 0.1438 0.1605 0.1830 0.0066  0.0068  0.0310  113 TYR   A OH  
2286 N N   . GLU   A 114 ? 0.1318 0.1392 0.1665 -0.0044 0.0162  0.0040  114 GLU   A N   
2287 C CA  . GLU   A 114 ? 0.1404 0.1238 0.1721 0.0046  0.0080  0.0110  114 GLU   A CA  
2288 C C   . GLU   A 114 ? 0.1394 0.1307 0.1624 -0.0004 0.0139  0.0054  114 GLU   A C   
2289 O O   . GLU   A 114 ? 0.1481 0.1395 0.1670 -0.0010 0.0027  0.0058  114 GLU   A O   
2290 C CB  . GLU   A 114 ? 0.1424 0.1283 0.1680 -0.0089 0.0069  0.0114  114 GLU   A CB  
2291 C CG  . GLU   A 114 ? 0.1486 0.1266 0.1788 -0.0012 0.0135  0.0026  114 GLU   A CG  
2292 C CD  . GLU   A 114 ? 0.1562 0.1346 0.1926 -0.0063 0.0006  -0.0044 114 GLU   A CD  
2293 O OE1 . GLU   A 114 ? 0.1550 0.1406 0.1820 -0.0067 0.0103  -0.0080 114 GLU   A OE1 
2294 O OE2 . GLU   A 114 ? 0.1704 0.1457 0.2102 -0.0062 0.0095  -0.0141 114 GLU   A OE2 
2301 N N   . ASN   A 115 ? 0.1351 0.1360 0.1561 -0.0072 0.0060  -0.0001 115 ASN   A N   
2302 C CA  . ASN   A 115 ? 0.1382 0.1422 0.1665 -0.0102 0.0099  0.0107  115 ASN   A CA  
2303 C C   . ASN   A 115 ? 0.1408 0.1419 0.1565 -0.0147 0.0003  0.0066  115 ASN   A C   
2304 O O   . ASN   A 115 ? 0.1394 0.1478 0.1702 -0.0137 0.0121  0.0106  115 ASN   A O   
2305 C CB  . ASN   A 115 ? 0.1480 0.1479 0.1618 -0.0153 0.0052  0.0038  115 ASN   A CB  
2306 C CG  . ASN   A 115 ? 0.1471 0.1660 0.1717 -0.0184 0.0131  0.0039  115 ASN   A CG  
2307 O OD1 . ASN   A 115 ? 0.1510 0.2626 0.1862 -0.0163 0.0219  0.0216  115 ASN   A OD1 
2308 N ND2 . ASN   A 115 ? 0.1488 0.1501 0.1733 -0.0096 0.0225  0.0057  115 ASN   A ND2 
2315 N N   . PHE   A 116 ? 0.1311 0.1458 0.1652 -0.0048 0.0055  0.0082  116 PHE   A N   
2316 C CA  . PHE   A 116 ? 0.1377 0.1573 0.1496 -0.0014 0.0119  0.0156  116 PHE   A CA  
2317 C C   . PHE   A 116 ? 0.1293 0.1634 0.1664 -0.0076 0.0180  0.0177  116 PHE   A C   
2318 O O   . PHE   A 116 ? 0.1432 0.1620 0.1680 -0.0047 0.0150  0.0220  116 PHE   A O   
2319 C CB  . PHE   A 116 ? 0.1288 0.1485 0.1750 -0.0031 0.0140  0.0160  116 PHE   A CB  
2320 C CG  . PHE   A 116 ? 0.1395 0.1464 0.1559 -0.0094 0.0144  0.0142  116 PHE   A CG  
2321 C CD1 . PHE   A 116 ? 0.1378 0.1466 0.1525 -0.0052 0.0144  0.0139  116 PHE   A CD1 
2322 C CD2 . PHE   A 116 ? 0.1480 0.1541 0.1605 -0.0085 0.0171  0.0142  116 PHE   A CD2 
2323 C CE1 . PHE   A 116 ? 0.1430 0.1416 0.1695 -0.0160 0.0054  0.0113  116 PHE   A CE1 
2324 C CE2 . PHE   A 116 ? 0.1434 0.1520 0.1768 -0.0059 0.0134  0.0094  116 PHE   A CE2 
2325 C CZ  . PHE   A 116 ? 0.1492 0.1354 0.1628 -0.0042 0.0123  0.0164  116 PHE   A CZ  
2335 N N   . ASN   A 117 ? 0.1386 0.1549 0.1737 -0.0016 0.0072  0.0226  117 ASN   A N   
2336 C CA  . ASN   A 117 ? 0.1442 0.1545 0.1863 -0.0018 0.0020  0.0225  117 ASN   A CA  
2337 C C   . ASN   A 117 ? 0.1436 0.1566 0.1993 0.0003  0.0070  0.0303  117 ASN   A C   
2338 O O   . ASN   A 117 ? 0.1524 0.1603 0.2187 -0.0083 -0.0139 0.0386  117 ASN   A O   
2339 C CB  . ASN   A 117 ? 0.1438 0.1558 0.1790 -0.0069 0.0036  0.0247  117 ASN   A CB  
2340 C CG  . ASN   A 117 ? 0.1453 0.1437 0.1812 -0.0091 0.0119  0.0208  117 ASN   A CG  
2341 O OD1 . ASN   A 117 ? 0.1482 0.1707 0.1860 -0.0161 0.0105  0.0116  117 ASN   A OD1 
2342 N ND2 . ASN   A 117 ? 0.1373 0.1446 0.1936 0.0007  0.0097  0.0148  117 ASN   A ND2 
2349 N N   . GLN   A 118 ? 0.1405 0.1533 0.2000 -0.0043 -0.0036 0.0288  118 GLN   A N   
2350 C CA  . GLN   A 118 ? 0.1513 0.1658 0.2017 -0.0098 -0.0119 0.0240  118 GLN   A CA  
2351 C C   . GLN   A 118 ? 0.1489 0.1739 0.1896 -0.0083 -0.0075 0.0252  118 GLN   A C   
2352 O O   . GLN   A 118 ? 0.1517 0.2055 0.2241 -0.0013 -0.0191 0.0166  118 GLN   A O   
2353 C CB  . GLN   A 118 ? 0.1467 0.1620 0.2119 -0.0083 0.0078  0.0267  118 GLN   A CB  
2354 C CG  . GLN   A 118 ? 0.1364 0.1651 0.2067 -0.0011 0.0014  0.0281  118 GLN   A CG  
2355 C CD  . GLN   A 118 ? 0.1472 0.1751 0.2073 0.0009  0.0006  0.0191  118 GLN   A CD  
2356 O OE1 . GLN   A 118 ? 0.1500 0.1796 0.2242 0.0104  -0.0079 0.0099  118 GLN   A OE1 
2357 N NE2 . GLN   A 118 ? 0.1578 0.1741 0.2037 -0.0013 -0.0012 0.0197  118 GLN   A NE2 
2366 N N   . HIS   A 119 ? 0.1571 0.1651 0.1729 -0.0048 -0.0025 0.0251  119 HIS   A N   
2367 C CA  . HIS   A 119 ? 0.1624 0.1783 0.1742 -0.0092 0.0026  0.0328  119 HIS   A CA  
2368 C C   . HIS   A 119 ? 0.1768 0.1851 0.1604 -0.0173 0.0021  0.0367  119 HIS   A C   
2369 O O   . HIS   A 119 ? 0.1757 0.1986 0.1720 -0.0343 -0.0133 0.0232  119 HIS   A O   
2370 C CB  . HIS   A 119 ? 0.1658 0.1776 0.1895 -0.0083 0.0178  0.0330  119 HIS   A CB  
2371 C CG  . HIS   A 119 ? 0.1616 0.1817 0.2341 -0.0015 0.0150  0.0349  119 HIS   A CG  
2372 N ND1 . HIS   A 119 ? 0.1770 0.2073 0.2839 -0.0171 0.0122  0.0281  119 HIS   A ND1 
2373 C CD2 . HIS   A 119 ? 0.1712 0.1880 0.2508 0.0069  0.0353  0.0523  119 HIS   A CD2 
2374 C CE1 . HIS   A 119 ? 0.1805 0.2086 0.3110 -0.0129 0.0306  0.0541  119 HIS   A CE1 
2375 N NE2 . HIS   A 119 ? 0.1788 0.1991 0.3050 -0.0063 0.0456  0.0621  119 HIS   A NE2 
2383 N N   . GLU   A 120 ? 0.1921 0.2086 0.1739 -0.0162 -0.0098 0.0519  120 GLU   A N   
2384 C CA  . GLU   A 120 ? 0.2123 0.2380 0.2024 -0.0092 -0.0052 0.0901  120 GLU   A CA  
2385 C C   . GLU   A 120 ? 0.1902 0.2206 0.1797 -0.0183 -0.0043 0.0829  120 GLU   A C   
2386 O O   . GLU   A 120 ? 0.1832 0.2122 0.1924 -0.0203 -0.0103 0.0708  120 GLU   A O   
2387 C CB  . GLU   A 120 ? 0.2763 0.3097 0.2754 0.0066  -0.0033 0.1443  120 GLU   A CB  
2388 C CG  . GLU   A 120 ? 0.3476 0.3666 0.3981 0.0214  -0.0059 0.1495  120 GLU   A CG  
2389 C CD  . GLU   A 120 ? 0.4361 0.4455 0.5209 0.0349  -0.0016 0.1335  120 GLU   A CD  
2390 O OE1 . GLU   A 120 ? 0.4738 0.4597 0.5597 0.0361  -0.0024 0.1245  120 GLU   A OE1 
2391 O OE2 . GLU   A 120 ? 0.5261 0.5261 0.5752 0.0407  0.0006  0.1306  120 GLU   A OE2 
2398 N N   . VAL   A 121 ? 0.1868 0.2267 0.1616 -0.0205 0.0038  0.0616  121 VAL   A N   
2399 C CA  . VAL   A 121 ? 0.1889 0.2322 0.1430 -0.0213 0.0100  0.0599  121 VAL   A CA  
2400 C C   . VAL   A 121 ? 0.1792 0.2121 0.1272 -0.0327 0.0018  0.0415  121 VAL   A C   
2401 O O   . VAL   A 121 ? 0.1802 0.2163 0.1630 -0.0385 -0.0100 0.0333  121 VAL   A O   
2402 C CB  . VAL   A 121 ? 0.2215 0.2663 0.1905 -0.0100 0.0249  0.0698  121 VAL   A CB  
2403 C CG1 . VAL   A 121 ? 0.2213 0.2843 0.2001 -0.0040 0.0252  0.0705  121 VAL   A CG1 
2404 C CG2 . VAL   A 121 ? 0.2419 0.2863 0.2542 -0.0202 0.0168  0.0539  121 VAL   A CG2 
2414 N N   . LEU   A 122 ? 0.1705 0.1924 0.1442 -0.0300 -0.0004 0.0384  122 LEU   A N   
2415 C CA  . LEU   A 122 ? 0.1750 0.1777 0.1456 -0.0309 0.0251  0.0308  122 LEU   A CA  
2416 C C   . LEU   A 122 ? 0.1721 0.1724 0.1503 -0.0353 0.0205  0.0264  122 LEU   A C   
2417 O O   . LEU   A 122 ? 0.1693 0.1793 0.1820 -0.0393 0.0098  0.0230  122 LEU   A O   
2418 C CB  . LEU   A 122 ? 0.1889 0.1836 0.1894 -0.0149 0.0142  0.0450  122 LEU   A CB  
2419 C CG  . LEU   A 122 ? 0.1861 0.1817 0.1871 -0.0162 0.0223  0.0277  122 LEU   A CG  
2420 C CD1 . LEU   A 122 ? 0.2031 0.1960 0.1922 -0.0237 0.0208  0.0270  122 LEU   A CD1 
2421 C CD2 . LEU   A 122 ? 0.1793 0.1744 0.1782 -0.0151 0.0309  0.0228  122 LEU   A CD2 
2433 N N   A LEU   A 123 ? 0.1641 0.1708 0.1397 -0.0319 0.0061  0.0267  123 LEU   A N   
2434 N N   B LEU   A 123 ? 0.1701 0.1664 0.1518 -0.0299 0.0097  0.0158  123 LEU   A N   
2435 C CA  A LEU   A 123 ? 0.1684 0.1743 0.1391 -0.0256 0.0129  0.0226  123 LEU   A CA  
2436 C CA  B LEU   A 123 ? 0.1724 0.1651 0.1514 -0.0265 0.0029  0.0058  123 LEU   A CA  
2437 C C   A LEU   A 123 ? 0.1599 0.1593 0.1278 -0.0168 0.0166  0.0209  123 LEU   A C   
2438 C C   B LEU   A 123 ? 0.1696 0.1566 0.1392 -0.0208 0.0028  0.0042  123 LEU   A C   
2439 O O   A LEU   A 123 ? 0.1517 0.1558 0.1356 -0.0256 0.0155  0.0154  123 LEU   A O   
2440 O O   B LEU   A 123 ? 0.1631 0.1557 0.1292 -0.0199 0.0026  -0.0135 123 LEU   A O   
2441 C CB  A LEU   A 123 ? 0.1795 0.1892 0.1247 -0.0279 0.0280  0.0291  123 LEU   A CB  
2442 C CB  B LEU   A 123 ? 0.1764 0.1714 0.1566 -0.0289 -0.0058 0.0005  123 LEU   A CB  
2443 C CG  A LEU   A 123 ? 0.1856 0.2032 0.1501 -0.0243 0.0211  0.0156  123 LEU   A CG  
2444 C CG  B LEU   A 123 ? 0.1784 0.1756 0.1645 -0.0326 -0.0040 0.0009  123 LEU   A CG  
2445 C CD1 A LEU   A 123 ? 0.1893 0.2051 0.1669 -0.0167 0.0202  0.0017  123 LEU   A CD1 
2446 C CD1 B LEU   A 123 ? 0.1807 0.1736 0.1726 -0.0312 -0.0005 -0.0036 123 LEU   A CD1 
2447 C CD2 A LEU   A 123 ? 0.1998 0.2118 0.1492 -0.0234 0.0152  0.0077  123 LEU   A CD2 
2448 C CD2 B LEU   A 123 ? 0.1813 0.1794 0.1651 -0.0348 -0.0066 -0.0012 123 LEU   A CD2 
2471 N N   A ALA   A 124 ? 0.1491 0.1483 0.1203 -0.0131 0.0086  0.0177  124 ALA   A N   
2472 N N   B ALA   A 124 ? 0.1676 0.1451 0.1421 -0.0158 0.0040  0.0097  124 ALA   A N   
2473 C CA  A ALA   A 124 ? 0.1357 0.1458 0.1311 -0.0134 0.0029  0.0177  124 ALA   A CA  
2474 C CA  B ALA   A 124 ? 0.1661 0.1500 0.1531 -0.0158 0.0016  0.0099  124 ALA   A CA  
2475 C C   A ALA   A 124 ? 0.1304 0.1496 0.1393 -0.0134 0.0103  0.0219  124 ALA   A C   
2476 C C   B ALA   A 124 ? 0.1598 0.1453 0.1498 -0.0076 -0.0010 0.0137  124 ALA   A C   
2477 O O   A ALA   A 124 ? 0.1241 0.1585 0.1634 -0.0127 0.0175  0.0317  124 ALA   A O   
2478 O O   B ALA   A 124 ? 0.1654 0.1442 0.1567 -0.0012 -0.0053 0.0130  124 ALA   A O   
2479 C CB  A ALA   A 124 ? 0.1357 0.1374 0.1613 -0.0131 0.0062  0.0128  124 ALA   A CB  
2480 C CB  B ALA   A 124 ? 0.1733 0.1507 0.1688 -0.0198 0.0066  0.0073  124 ALA   A CB  
2491 N N   A PRO   A 125 ? 0.1342 0.1431 0.1368 -0.0110 0.0051  0.0217  125 PRO   A N   
2492 N N   B PRO   A 125 ? 0.1431 0.1446 0.1233 -0.0052 -0.0044 0.0190  125 PRO   A N   
2493 C CA  A PRO   A 125 ? 0.1523 0.1596 0.1319 -0.0096 0.0009  0.0219  125 PRO   A CA  
2494 C CA  B PRO   A 125 ? 0.1428 0.1468 0.1180 -0.0052 -0.0012 0.0176  125 PRO   A CA  
2495 C C   A PRO   A 125 ? 0.1504 0.1610 0.1483 -0.0139 0.0060  0.0228  125 PRO   A C   
2496 C C   B PRO   A 125 ? 0.1488 0.1535 0.1301 -0.0060 0.0008  0.0111  125 PRO   A C   
2497 O O   A PRO   A 125 ? 0.1570 0.1479 0.1659 -0.0117 -0.0011 0.0194  125 PRO   A O   
2498 O O   B PRO   A 125 ? 0.1516 0.1470 0.1354 -0.0028 -0.0017 0.0085  125 PRO   A O   
2499 C CB  A PRO   A 125 ? 0.1572 0.1572 0.1387 -0.0202 0.0048  0.0220  125 PRO   A CB  
2500 C CB  B PRO   A 125 ? 0.1327 0.1430 0.1085 -0.0065 -0.0042 0.0207  125 PRO   A CB  
2501 C CG  A PRO   A 125 ? 0.1547 0.1535 0.1467 -0.0200 0.0102  0.0299  125 PRO   A CG  
2502 C CG  B PRO   A 125 ? 0.1263 0.1423 0.1190 -0.0083 -0.0022 0.0203  125 PRO   A CG  
2503 C CD  A PRO   A 125 ? 0.1424 0.1501 0.1504 -0.0210 0.0092  0.0221  125 PRO   A CD  
2504 C CD  B PRO   A 125 ? 0.1297 0.1392 0.1268 -0.0071 0.0024  0.0182  125 PRO   A CD  
2519 N N   A LEU   A 126 ? 0.1431 0.1688 0.1546 -0.0044 0.0087  0.0152  126 LEU   A N   
2520 N N   B LEU   A 126 ? 0.1536 0.1605 0.1395 -0.0051 0.0003  0.0093  126 LEU   A N   
2521 C CA  A LEU   A 126 ? 0.1452 0.1573 0.1683 -0.0057 0.0117  0.0187  126 LEU   A CA  
2522 C CA  B LEU   A 126 ? 0.1571 0.1546 0.1476 -0.0101 0.0015  0.0075  126 LEU   A CA  
2523 C C   A LEU   A 126 ? 0.1567 0.1428 0.1637 0.0015  0.0095  0.0123  126 LEU   A C   
2524 C C   B LEU   A 126 ? 0.1594 0.1441 0.1456 -0.0023 0.0046  0.0093  126 LEU   A C   
2525 O O   A LEU   A 126 ? 0.1661 0.1452 0.1888 0.0014  0.0270  0.0167  126 LEU   A O   
2526 O O   B LEU   A 126 ? 0.1727 0.1421 0.1691 -0.0003 0.0136  0.0165  126 LEU   A O   
2527 C CB  A LEU   A 126 ? 0.1526 0.1635 0.1775 -0.0107 0.0011  0.0169  126 LEU   A CB  
2528 C CB  B LEU   A 126 ? 0.1624 0.1629 0.1611 -0.0214 -0.0011 -0.0006 126 LEU   A CB  
2529 C CG  A LEU   A 126 ? 0.1530 0.1878 0.2009 -0.0139 0.0136  0.0169  126 LEU   A CG  
2530 C CG  B LEU   A 126 ? 0.1666 0.1651 0.1649 -0.0224 0.0018  -0.0082 126 LEU   A CG  
2531 C CD1 A LEU   A 126 ? 0.1608 0.2159 0.2364 -0.0179 0.0094  0.0219  126 LEU   A CD1 
2532 C CD1 B LEU   A 126 ? 0.1679 0.1719 0.1800 -0.0243 -0.0041 -0.0062 126 LEU   A CD1 
2533 C CD2 A LEU   A 126 ? 0.1587 0.1751 0.1911 -0.0235 0.0093  0.0226  126 LEU   A CD2 
2534 C CD2 B LEU   A 126 ? 0.1721 0.1669 0.1577 -0.0187 0.0006  -0.0139 126 LEU   A CD2 
2557 N N   A LEU   A 127 ? 0.1533 0.1521 0.1516 0.0061  0.0087  0.0168  127 LEU   A N   
2558 N N   B LEU   A 127 ? 0.1491 0.1419 0.1319 0.0013  0.0020  0.0198  127 LEU   A N   
2559 C CA  A LEU   A 127 ? 0.1495 0.1588 0.1386 -0.0065 0.0029  0.0180  127 LEU   A CA  
2560 C CA  B LEU   A 127 ? 0.1426 0.1417 0.1245 0.0028  -0.0039 0.0335  127 LEU   A CA  
2561 C C   A LEU   A 127 ? 0.1414 0.1512 0.1422 -0.0009 -0.0083 0.0133  127 LEU   A C   
2562 C C   B LEU   A 127 ? 0.1446 0.1440 0.1388 0.0013  0.0014  0.0247  127 LEU   A C   
2563 O O   A LEU   A 127 ? 0.1498 0.1470 0.1565 -0.0129 -0.0102 0.0131  127 LEU   A O   
2564 O O   B LEU   A 127 ? 0.1483 0.1420 0.1483 -0.0012 0.0183  0.0212  127 LEU   A O   
2565 C CB  A LEU   A 127 ? 0.1532 0.1717 0.1599 0.0053  0.0113  0.0186  127 LEU   A CB  
2566 C CB  B LEU   A 127 ? 0.1389 0.1493 0.1244 0.0056  -0.0154 0.0326  127 LEU   A CB  
2567 C CG  A LEU   A 127 ? 0.1604 0.1699 0.1684 0.0085  0.0072  0.0148  127 LEU   A CG  
2568 C CG  B LEU   A 127 ? 0.1363 0.1620 0.1190 0.0057  -0.0280 0.0390  127 LEU   A CG  
2569 C CD1 A LEU   A 127 ? 0.1629 0.1609 0.1851 0.0094  0.0121  0.0132  127 LEU   A CD1 
2570 C CD1 B LEU   A 127 ? 0.1315 0.1655 0.1340 0.0049  -0.0159 0.0426  127 LEU   A CD1 
2571 C CD2 A LEU   A 127 ? 0.1690 0.1754 0.2003 0.0167  0.0024  0.0107  127 LEU   A CD2 
2572 C CD2 B LEU   A 127 ? 0.1431 0.1712 0.1095 0.0073  -0.0480 0.0268  127 LEU   A CD2 
2595 N N   A SER   A 128 ? 0.1472 0.1523 0.1372 -0.0085 0.0069  0.0175  128 SER   A N   
2596 N N   B SER   A 128 ? 0.1503 0.1473 0.1476 -0.0066 -0.0045 0.0226  128 SER   A N   
2597 C CA  A SER   A 128 ? 0.1559 0.1589 0.1205 -0.0056 0.0118  0.0277  128 SER   A CA  
2598 C CA  B SER   A 128 ? 0.1513 0.1471 0.1418 -0.0115 -0.0079 0.0175  128 SER   A CA  
2599 C C   A SER   A 128 ? 0.1607 0.1546 0.1387 0.0065  0.0062  0.0382  128 SER   A C   
2600 C C   B SER   A 128 ? 0.1478 0.1395 0.1434 -0.0203 -0.0242 0.0153  128 SER   A C   
2601 O O   A SER   A 128 ? 0.1748 0.1796 0.1692 0.0070  0.0030  0.0280  128 SER   A O   
2602 O O   B SER   A 128 ? 0.1431 0.1395 0.1468 -0.0302 -0.0326 0.0054  128 SER   A O   
2603 C CB  A SER   A 128 ? 0.1585 0.1616 0.1270 -0.0043 -0.0013 0.0188  128 SER   A CB  
2604 C CB  B SER   A 128 ? 0.1570 0.1515 0.1408 -0.0079 -0.0032 0.0235  128 SER   A CB  
2605 O OG  A SER   A 128 ? 0.1625 0.1696 0.1380 -0.0058 0.0062  0.0086  128 SER   A OG  
2606 O OG  B SER   A 128 ? 0.1603 0.1563 0.1426 -0.0064 0.0073  0.0359  128 SER   A OG  
2617 N N   A ALA   A 129 ? 0.1565 0.1594 0.1744 0.0045  0.0038  0.0420  129 ALA   A N   
2618 N N   B ALA   A 129 ? 0.1532 0.1470 0.1577 -0.0146 -0.0259 0.0208  129 ALA   A N   
2619 C CA  A ALA   A 129 ? 0.1518 0.1611 0.1979 -0.0006 0.0096  0.0443  129 ALA   A CA  
2620 C CA  B ALA   A 129 ? 0.1610 0.1558 0.1702 -0.0087 -0.0298 0.0287  129 ALA   A CA  
2621 C C   A ALA   A 129 ? 0.1637 0.1591 0.1637 0.0008  0.0185  0.0258  129 ALA   A C   
2622 C C   B ALA   A 129 ? 0.1570 0.1602 0.1805 -0.0068 -0.0316 0.0265  129 ALA   A C   
2623 O O   A ALA   A 129 ? 0.1660 0.1655 0.1552 -0.0053 0.0130  0.0309  129 ALA   A O   
2624 O O   B ALA   A 129 ? 0.1529 0.1644 0.1854 -0.0001 -0.0318 0.0192  129 ALA   A O   
2625 C CB  A ALA   A 129 ? 0.1589 0.1761 0.2304 0.0098  0.0223  0.0665  129 ALA   A CB  
2626 C CB  B ALA   A 129 ? 0.1720 0.1642 0.1778 -0.0030 -0.0242 0.0316  129 ALA   A CB  
2637 N N   A GLY   A 130 ? 0.1679 0.1516 0.1735 0.0018  0.0171  0.0186  130 GLY   A N   
2638 N N   B GLY   A 130 ? 0.1586 0.1638 0.1768 -0.0040 -0.0327 0.0328  130 GLY   A N   
2639 C CA  A GLY   A 130 ? 0.1839 0.1531 0.1865 0.0010  0.0154  0.0172  130 GLY   A CA  
2640 C CA  B GLY   A 130 ? 0.1632 0.1658 0.1934 -0.0079 -0.0276 0.0291  130 GLY   A CA  
2641 C C   A GLY   A 130 ? 0.1796 0.1474 0.1652 0.0000  0.0024  0.0167  130 GLY   A C   
2642 C C   B GLY   A 130 ? 0.1667 0.1666 0.1977 -0.0018 -0.0283 0.0355  130 GLY   A C   
2643 O O   A GLY   A 130 ? 0.1784 0.1455 0.1650 -0.0073 -0.0068 0.0119  130 GLY   A O   
2644 O O   B GLY   A 130 ? 0.1783 0.1701 0.2062 0.0019  -0.0260 0.0476  130 GLY   A O   
2651 N N   A ILE   A 131 ? 0.1819 0.1517 0.1674 -0.0112 0.0020  0.0110  131 ILE   A N   
2652 N N   B ILE   A 131 ? 0.1634 0.1678 0.1948 -0.0036 -0.0217 0.0318  131 ILE   A N   
2653 C CA  A ILE   A 131 ? 0.1858 0.1556 0.1359 -0.0193 0.0007  0.0146  131 ILE   A CA  
2654 C CA  B ILE   A 131 ? 0.1620 0.1715 0.1906 0.0008  -0.0301 0.0300  131 ILE   A CA  
2655 C C   A ILE   A 131 ? 0.1799 0.1595 0.1337 -0.0169 0.0025  0.0258  131 ILE   A C   
2656 C C   B ILE   A 131 ? 0.1636 0.1751 0.1876 -0.0002 -0.0251 0.0367  131 ILE   A C   
2657 O O   A ILE   A 131 ? 0.1923 0.1626 0.1517 -0.0051 -0.0015 0.0227  131 ILE   A O   
2658 O O   B ILE   A 131 ? 0.1658 0.1797 0.2045 0.0043  -0.0245 0.0435  131 ILE   A O   
2659 C CB  A ILE   A 131 ? 0.2060 0.1722 0.1628 -0.0244 -0.0029 -0.0025 131 ILE   A CB  
2660 C CB  B ILE   A 131 ? 0.1606 0.1779 0.1919 0.0047  -0.0368 0.0176  131 ILE   A CB  
2661 C CG1 A ILE   A 131 ? 0.2089 0.2134 0.1791 -0.0265 -0.0175 -0.0106 131 ILE   A CG1 
2662 C CG1 B ILE   A 131 ? 0.1663 0.1899 0.1946 0.0075  -0.0383 0.0059  131 ILE   A CG1 
2663 C CG2 A ILE   A 131 ? 0.2235 0.1616 0.1907 -0.0195 0.0098  -0.0150 131 ILE   A CG2 
2664 C CG2 B ILE   A 131 ? 0.1597 0.1766 0.1947 0.0030  -0.0306 0.0115  131 ILE   A CG2 
2665 C CD1 A ILE   A 131 ? 0.2076 0.2365 0.2314 -0.0272 -0.0243 -0.0165 131 ILE   A CD1 
2666 C CD1 B ILE   A 131 ? 0.1715 0.1981 0.1990 0.0088  -0.0394 -0.0090 131 ILE   A CD1 
2689 N N   A PHE   A 132 ? 0.1686 0.1632 0.1469 -0.0097 0.0015  0.0235  132 PHE   A N   
2690 N N   B PHE   A 132 ? 0.1676 0.1756 0.1751 0.0036  -0.0216 0.0288  132 PHE   A N   
2691 C CA  A PHE   A 132 ? 0.1758 0.1692 0.1351 -0.0130 0.0090  0.0098  132 PHE   A CA  
2692 C CA  B PHE   A 132 ? 0.1723 0.1746 0.1711 0.0007  -0.0237 0.0226  132 PHE   A CA  
2693 C C   A PHE   A 132 ? 0.1827 0.1804 0.1473 -0.0053 0.0070  0.0093  132 PHE   A C   
2694 C C   B PHE   A 132 ? 0.1836 0.1787 0.1752 0.0025  -0.0218 0.0256  132 PHE   A C   
2695 O O   A PHE   A 132 ? 0.1879 0.1957 0.1480 -0.0158 0.0080  0.0098  132 PHE   A O   
2696 O O   B PHE   A 132 ? 0.1905 0.1877 0.1803 -0.0020 -0.0141 0.0310  132 PHE   A O   
2697 C CB  A PHE   A 132 ? 0.1795 0.1583 0.1273 -0.0125 -0.0009 0.0162  132 PHE   A CB  
2698 C CB  B PHE   A 132 ? 0.1641 0.1653 0.1533 -0.0018 -0.0251 0.0275  132 PHE   A CB  
2699 C CG  A PHE   A 132 ? 0.1854 0.1544 0.1304 -0.0013 -0.0071 0.0072  132 PHE   A CG  
2700 C CG  B PHE   A 132 ? 0.1642 0.1600 0.1515 0.0034  -0.0209 0.0075  132 PHE   A CG  
2701 C CD1 A PHE   A 132 ? 0.1907 0.1712 0.1625 0.0096  -0.0124 -0.0086 132 PHE   A CD1 
2702 C CD1 B PHE   A 132 ? 0.1661 0.1649 0.1626 0.0075  -0.0134 -0.0040 132 PHE   A CD1 
2703 C CD2 A PHE   A 132 ? 0.1833 0.1662 0.1455 -0.0025 -0.0077 0.0079  132 PHE   A CD2 
2704 C CD2 B PHE   A 132 ? 0.1630 0.1619 0.1472 0.0059  -0.0211 -0.0062 132 PHE   A CD2 
2705 C CE1 A PHE   A 132 ? 0.1895 0.1814 0.1720 0.0087  -0.0306 -0.0043 132 PHE   A CE1 
2706 C CE1 B PHE   A 132 ? 0.1633 0.1692 0.1585 0.0100  -0.0172 -0.0079 132 PHE   A CE1 
2707 C CE2 A PHE   A 132 ? 0.1879 0.1654 0.1732 0.0044  -0.0187 0.0083  132 PHE   A CE2 
2708 C CE2 B PHE   A 132 ? 0.1629 0.1651 0.1553 0.0123  -0.0187 -0.0130 132 PHE   A CE2 
2709 C CZ  A PHE   A 132 ? 0.1895 0.1747 0.1766 0.0021  -0.0278 0.0018  132 PHE   A CZ  
2710 C CZ  B PHE   A 132 ? 0.1627 0.1676 0.1577 0.0098  -0.0172 -0.0105 132 PHE   A CZ  
2729 N N   A GLY   A 133 ? 0.1812 0.1786 0.1475 -0.0066 -0.0170 0.0178  133 GLY   A N   
2730 N N   B GLY   A 133 ? 0.1858 0.1761 0.1784 0.0024  -0.0270 0.0233  133 GLY   A N   
2731 C CA  A GLY   A 133 ? 0.2008 0.1926 0.1668 -0.0103 -0.0327 0.0090  133 GLY   A CA  
2732 C CA  B GLY   A 133 ? 0.1877 0.1799 0.1837 0.0049  -0.0275 0.0140  133 GLY   A CA  
2733 C C   A GLY   A 133 ? 0.2087 0.2031 0.1594 -0.0122 -0.0535 -0.0010 133 GLY   A C   
2734 C C   B GLY   A 133 ? 0.1889 0.1855 0.1782 0.0105  -0.0292 0.0010  133 GLY   A C   
2735 O O   A GLY   A 133 ? 0.2317 0.2166 0.1732 -0.0056 -0.0439 -0.0273 133 GLY   A O   
2736 O O   B GLY   A 133 ? 0.1930 0.1924 0.1738 0.0160  -0.0300 -0.0151 133 GLY   A O   
2743 N N   A ALA   A 134 ? 0.2077 0.1926 0.1559 -0.0221 -0.0330 -0.0008 134 ALA   A N   
2744 N N   B ALA   A 134 ? 0.1876 0.1799 0.1808 0.0113  -0.0188 -0.0038 134 ALA   A N   
2745 C CA  A ALA   A 134 ? 0.2106 0.1946 0.1912 -0.0166 -0.0332 0.0003  134 ALA   A CA  
2746 C CA  B ALA   A 134 ? 0.1868 0.1761 0.1864 0.0106  -0.0136 -0.0077 134 ALA   A CA  
2747 C C   A ALA   A 134 ? 0.2068 0.1973 0.2021 -0.0185 -0.0343 0.0101  134 ALA   A C   
2748 C C   B ALA   A 134 ? 0.1854 0.1697 0.1805 0.0055  -0.0097 -0.0033 134 ALA   A C   
2749 O O   A ALA   A 134 ? 0.2163 0.1987 0.2088 -0.0175 -0.0270 0.0044  134 ALA   A O   
2750 O O   B ALA   A 134 ? 0.1818 0.1654 0.1810 0.0014  0.0034  -0.0034 134 ALA   A O   
2751 C CB  A ALA   A 134 ? 0.2135 0.1894 0.2161 -0.0164 -0.0369 -0.0015 134 ALA   A CB  
2752 C CB  B ALA   A 134 ? 0.1874 0.1753 0.1973 0.0108  -0.0158 -0.0103 134 ALA   A CB  
2763 N N   A ASP   A 135 ? 0.2107 0.1974 0.1990 -0.0211 -0.0375 0.0169  135 ASP   A N   
2764 N N   B ASP   A 135 ? 0.1941 0.1702 0.1766 -0.0001 -0.0182 -0.0013 135 ASP   A N   
2765 C CA  A ASP   A 135 ? 0.2009 0.2009 0.2271 -0.0244 -0.0458 0.0274  135 ASP   A CA  
2766 C CA  B ASP   A 135 ? 0.1921 0.1683 0.1858 -0.0065 -0.0308 -0.0017 135 ASP   A CA  
2767 C C   A ASP   A 135 ? 0.1877 0.1815 0.2271 -0.0183 -0.0330 0.0290  135 ASP   A C   
2768 C C   B ASP   A 135 ? 0.1789 0.1581 0.1835 -0.0060 -0.0321 -0.0046 135 ASP   A C   
2769 O O   A ASP   A 135 ? 0.1853 0.1728 0.2300 -0.0083 -0.0217 0.0314  135 ASP   A O   
2770 O O   B ASP   A 135 ? 0.1725 0.1544 0.1757 -0.0115 -0.0326 -0.0012 135 ASP   A O   
2771 C CB  A ASP   A 135 ? 0.2210 0.2318 0.2771 -0.0467 -0.0621 0.0134  135 ASP   A CB  
2772 C CB  B ASP   A 135 ? 0.2024 0.1759 0.2025 -0.0098 -0.0392 -0.0022 135 ASP   A CB  
2773 C CG  A ASP   A 135 ? 0.2392 0.2555 0.3259 -0.0676 -0.0734 0.0104  135 ASP   A CG  
2774 C CG  B ASP   A 135 ? 0.2108 0.1868 0.2208 -0.0118 -0.0418 -0.0029 135 ASP   A CG  
2775 O OD1 A ASP   A 135 ? 0.2337 0.2607 0.3227 -0.0743 -0.0840 0.0350  135 ASP   A OD1 
2776 O OD1 B ASP   A 135 ? 0.2140 0.1881 0.2210 -0.0097 -0.0439 -0.0034 135 ASP   A OD1 
2777 O OD2 A ASP   A 135 ? 0.2672 0.2769 0.3842 -0.0728 -0.0496 0.0079  135 ASP   A OD2 
2778 O OD2 B ASP   A 135 ? 0.2147 0.1923 0.2353 -0.0117 -0.0409 -0.0021 135 ASP   A OD2 
2787 N N   A PRO   A 136 ? 0.1704 0.1777 0.2428 -0.0070 -0.0211 0.0423  136 PRO   A N   
2788 N N   B PRO   A 136 ? 0.1716 0.1454 0.1902 0.0007  -0.0227 -0.0119 136 PRO   A N   
2789 C CA  A PRO   A 136 ? 0.1667 0.1783 0.2441 -0.0120 -0.0091 0.0222  136 PRO   A CA  
2790 C CA  B PRO   A 136 ? 0.1704 0.1525 0.1853 -0.0009 -0.0102 -0.0205 136 PRO   A CA  
2791 C C   A PRO   A 136 ? 0.1475 0.1714 0.2281 -0.0036 -0.0058 0.0187  136 PRO   A C   
2792 C C   B PRO   A 136 ? 0.1669 0.1562 0.1714 0.0050  -0.0011 -0.0186 136 PRO   A C   
2793 O O   A PRO   A 136 ? 0.1481 0.1770 0.2151 -0.0101 -0.0059 0.0195  136 PRO   A O   
2794 O O   B PRO   A 136 ? 0.1629 0.1497 0.1530 0.0188  0.0152  -0.0229 136 PRO   A O   
2795 C CB  A PRO   A 136 ? 0.1835 0.1778 0.2659 -0.0067 -0.0118 0.0138  136 PRO   A CB  
2796 C CB  B PRO   A 136 ? 0.1747 0.1497 0.2009 0.0007  -0.0120 -0.0198 136 PRO   A CB  
2797 C CG  A PRO   A 136 ? 0.1952 0.1874 0.2878 0.0011  -0.0087 0.0192  136 PRO   A CG  
2798 C CG  B PRO   A 136 ? 0.1798 0.1476 0.2106 0.0021  -0.0161 -0.0242 136 PRO   A CG  
2799 C CD  A PRO   A 136 ? 0.1900 0.1830 0.2709 -0.0013 -0.0083 0.0367  136 PRO   A CD  
2800 C CD  B PRO   A 136 ? 0.1768 0.1409 0.2016 0.0047  -0.0157 -0.0156 136 PRO   A CD  
2815 N N   A ILE   A 137 ? 0.1434 0.1721 0.2359 0.0002  -0.0185 0.0214  137 ILE   A N   
2816 N N   B ILE   A 137 ? 0.1719 0.1571 0.1837 -0.0006 -0.0082 -0.0175 137 ILE   A N   
2817 C CA  A ILE   A 137 ? 0.1506 0.1748 0.2364 -0.0114 -0.0260 0.0316  137 ILE   A CA  
2818 C CA  B ILE   A 137 ? 0.1739 0.1624 0.1887 -0.0004 -0.0093 -0.0097 137 ILE   A CA  
2819 C C   A ILE   A 137 ? 0.1540 0.1798 0.2131 -0.0099 -0.0263 0.0357  137 ILE   A C   
2820 C C   B ILE   A 137 ? 0.1679 0.1577 0.1845 -0.0082 -0.0050 -0.0068 137 ILE   A C   
2821 O O   A ILE   A 137 ? 0.1583 0.1767 0.2246 -0.0140 -0.0138 0.0286  137 ILE   A O   
2822 O O   B ILE   A 137 ? 0.1602 0.1545 0.1906 -0.0086 -0.0050 -0.0023 137 ILE   A O   
2823 C CB  A ILE   A 137 ? 0.1624 0.1860 0.2774 -0.0120 -0.0402 0.0293  137 ILE   A CB  
2824 C CB  B ILE   A 137 ? 0.1816 0.1652 0.2078 0.0056  -0.0113 -0.0023 137 ILE   A CB  
2825 C CG1 A ILE   A 137 ? 0.1777 0.2094 0.3275 -0.0069 -0.0468 0.0290  137 ILE   A CG1 
2826 C CG1 B ILE   A 137 ? 0.1885 0.1706 0.2309 0.0123  -0.0205 -0.0047 137 ILE   A CG1 
2827 C CG2 A ILE   A 137 ? 0.1724 0.1920 0.2857 -0.0153 -0.0488 0.0156  137 ILE   A CG2 
2828 C CG2 B ILE   A 137 ? 0.1846 0.1649 0.2150 0.0129  -0.0118 -0.0000 137 ILE   A CG2 
2829 C CD1 A ILE   A 137 ? 0.1969 0.2198 0.3639 0.0020  -0.0422 0.0240  137 ILE   A CD1 
2830 C CD1 B ILE   A 137 ? 0.1940 0.1726 0.2423 0.0129  -0.0265 -0.0028 137 ILE   A CD1 
2853 N N   A HIS   A 138 ? 0.1544 0.1888 0.2099 -0.0063 -0.0154 0.0263  138 HIS   A N   
2854 N N   B HIS   A 138 ? 0.1646 0.1601 0.1794 -0.0119 0.0042  -0.0137 138 HIS   A N   
2855 C CA  A HIS   A 138 ? 0.1584 0.1992 0.1921 -0.0034 -0.0085 0.0166  138 HIS   A CA  
2856 C CA  B HIS   A 138 ? 0.1618 0.1604 0.1676 -0.0172 0.0067  -0.0111 138 HIS   A CA  
2857 C C   A HIS   A 138 ? 0.1567 0.1889 0.1952 -0.0028 -0.0033 0.0145  138 HIS   A C   
2858 C C   B HIS   A 138 ? 0.1593 0.1547 0.1601 -0.0187 0.0027  -0.0042 138 HIS   A C   
2859 O O   A HIS   A 138 ? 0.1721 0.1872 0.1981 -0.0047 -0.0035 0.0214  138 HIS   A O   
2860 O O   B HIS   A 138 ? 0.1644 0.1511 0.1500 -0.0196 0.0035  0.0005  138 HIS   A O   
2861 C CB  A HIS   A 138 ? 0.1795 0.2115 0.1838 -0.0019 -0.0202 0.0096  138 HIS   A CB  
2862 C CB  B HIS   A 138 ? 0.1623 0.1634 0.1665 -0.0116 0.0141  -0.0190 138 HIS   A CB  
2863 C CG  A HIS   A 138 ? 0.2018 0.2285 0.1927 -0.0064 -0.0157 0.0051  138 HIS   A CG  
2864 C CG  B HIS   A 138 ? 0.1665 0.1709 0.1698 -0.0091 0.0169  -0.0277 138 HIS   A CG  
2865 N ND1 A HIS   A 138 ? 0.2152 0.2406 0.2265 -0.0039 -0.0102 -0.0015 138 HIS   A ND1 
2866 N ND1 B HIS   A 138 ? 0.1753 0.1796 0.1894 -0.0055 0.0080  -0.0307 138 HIS   A ND1 
2867 C CD2 A HIS   A 138 ? 0.2070 0.2442 0.2030 -0.0047 -0.0158 0.0129  138 HIS   A CD2 
2868 C CD2 B HIS   A 138 ? 0.1670 0.1747 0.1762 -0.0063 0.0212  -0.0255 138 HIS   A CD2 
2869 C CE1 A HIS   A 138 ? 0.2221 0.2551 0.2403 0.0015  -0.0124 0.0030  138 HIS   A CE1 
2870 C CE1 B HIS   A 138 ? 0.1771 0.1813 0.1973 0.0004  0.0073  -0.0297 138 HIS   A CE1 
2871 N NE2 A HIS   A 138 ? 0.2134 0.2592 0.2165 0.0008  -0.0128 0.0049  138 HIS   A NE2 
2872 N NE2 B HIS   A 138 ? 0.1724 0.1811 0.1860 -0.0003 0.0154  -0.0300 138 HIS   A NE2 
2887 N N   A SER   A 139 ? 0.1498 0.1731 0.1842 0.0055  -0.0025 0.0209  139 SER   A N   
2888 N N   B SER   A 139 ? 0.1583 0.1505 0.1593 -0.0158 -0.0015 -0.0035 139 SER   A N   
2889 C CA  A SER   A 139 ? 0.1508 0.1633 0.1838 -0.0017 0.0035  0.0327  139 SER   A CA  
2890 C CA  B SER   A 139 ? 0.1557 0.1492 0.1577 -0.0111 -0.0009 -0.0004 139 SER   A CA  
2891 C C   A SER   A 139 ? 0.1402 0.1584 0.1866 -0.0132 0.0030  0.0205  139 SER   A C   
2892 C C   B SER   A 139 ? 0.1565 0.1481 0.1515 -0.0101 -0.0075 0.0012  139 SER   A C   
2893 O O   A SER   A 139 ? 0.1377 0.1563 0.1931 -0.0094 0.0030  0.0212  139 SER   A O   
2894 O O   B SER   A 139 ? 0.1587 0.1450 0.1560 -0.0067 -0.0231 0.0132  139 SER   A O   
2895 C CB  A SER   A 139 ? 0.1471 0.1613 0.1771 -0.0099 0.0073  0.0326  139 SER   A CB  
2896 C CB  B SER   A 139 ? 0.1490 0.1488 0.1620 -0.0133 -0.0046 0.0022  139 SER   A CB  
2897 O OG  A SER   A 139 ? 0.1497 0.1543 0.1690 -0.0074 -0.0032 0.0259  139 SER   A OG  
2898 O OG  B SER   A 139 ? 0.1498 0.1492 0.1641 -0.0190 -0.0051 0.0005  139 SER   A OG  
2909 N N   A LEU   A 140 ? 0.1332 0.1692 0.1838 -0.0088 0.0051  0.0339  140 LEU   A N   
2910 N N   B LEU   A 140 ? 0.1573 0.1575 0.1487 -0.0099 -0.0032 0.0150  140 LEU   A N   
2911 C CA  A LEU   A 140 ? 0.1327 0.1741 0.1844 -0.0078 0.0073  0.0300  140 LEU   A CA  
2912 C CA  B LEU   A 140 ? 0.1587 0.1610 0.1507 -0.0097 -0.0008 0.0207  140 LEU   A CA  
2913 C C   A LEU   A 140 ? 0.1266 0.1806 0.1755 -0.0206 0.0037  0.0362  140 LEU   A C   
2914 C C   B LEU   A 140 ? 0.1638 0.1691 0.1647 -0.0143 -0.0040 0.0220  140 LEU   A C   
2915 O O   A LEU   A 140 ? 0.1288 0.1819 0.2084 -0.0099 0.0001  0.0354  140 LEU   A O   
2916 O O   B LEU   A 140 ? 0.1701 0.1678 0.1725 -0.0083 -0.0074 0.0258  140 LEU   A O   
2917 C CB  A LEU   A 140 ? 0.1380 0.1899 0.2060 -0.0082 0.0114  0.0295  140 LEU   A CB  
2918 C CB  B LEU   A 140 ? 0.1541 0.1657 0.1476 -0.0112 -0.0031 0.0319  140 LEU   A CB  
2919 C CG  A LEU   A 140 ? 0.1429 0.2021 0.2098 -0.0229 0.0144  0.0348  140 LEU   A CG  
2920 C CG  B LEU   A 140 ? 0.1512 0.1708 0.1484 -0.0158 -0.0119 0.0450  140 LEU   A CG  
2921 C CD1 A LEU   A 140 ? 0.1490 0.2068 0.2112 -0.0248 0.0139  0.0445  140 LEU   A CD1 
2922 C CD1 B LEU   A 140 ? 0.1505 0.1729 0.1452 -0.0140 -0.0215 0.0481  140 LEU   A CD1 
2923 C CD2 A LEU   A 140 ? 0.1498 0.2158 0.2313 -0.0183 0.0229  0.0207  140 LEU   A CD2 
2924 C CD2 B LEU   A 140 ? 0.1526 0.1768 0.1584 -0.0176 -0.0090 0.0450  140 LEU   A CD2 
2947 N N   A ARG   A 141 ? 0.1371 0.1801 0.1852 -0.0137 -0.0001 0.0200  141 ARG   A N   
2948 N N   B ARG   A 141 ? 0.1664 0.1735 0.1805 -0.0170 -0.0049 0.0150  141 ARG   A N   
2949 C CA  A ARG   A 141 ? 0.1555 0.1930 0.2021 -0.0252 -0.0082 0.0053  141 ARG   A CA  
2950 C CA  B ARG   A 141 ? 0.1686 0.1859 0.2008 -0.0212 -0.0068 0.0053  141 ARG   A CA  
2951 C C   A ARG   A 141 ? 0.1529 0.1752 0.1989 -0.0158 -0.0074 0.0075  141 ARG   A C   
2952 C C   B ARG   A 141 ? 0.1582 0.1780 0.1954 -0.0191 -0.0050 0.0059  141 ARG   A C   
2953 O O   A ARG   A 141 ? 0.1486 0.1699 0.2195 -0.0180 0.0101  0.0054  141 ARG   A O   
2954 O O   B ARG   A 141 ? 0.1583 0.1784 0.1965 -0.0231 -0.0015 0.0032  141 ARG   A O   
2955 C CB  A ARG   A 141 ? 0.1700 0.2159 0.2335 -0.0389 -0.0163 -0.0249 141 ARG   A CB  
2956 C CB  B ARG   A 141 ? 0.1793 0.2031 0.2311 -0.0226 -0.0134 -0.0078 141 ARG   A CB  
2957 C CG  A ARG   A 141 ? 0.2005 0.2505 0.2777 -0.0389 -0.0089 -0.0281 141 ARG   A CG  
2958 C CG  B ARG   A 141 ? 0.1931 0.2202 0.2597 -0.0233 -0.0103 -0.0065 141 ARG   A CG  
2959 C CD  A ARG   A 141 ? 0.2347 0.2778 0.3241 -0.0418 0.0027  -0.0262 141 ARG   A CD  
2960 C CD  B ARG   A 141 ? 0.2073 0.2313 0.2796 -0.0217 -0.0099 -0.0027 141 ARG   A CD  
2961 N NE  A ARG   A 141 ? 0.2314 0.3123 0.3436 -0.0419 -0.0010 -0.0265 141 ARG   A NE  
2962 N NE  B ARG   A 141 ? 0.2071 0.2384 0.2901 -0.0192 -0.0140 0.0019  141 ARG   A NE  
2963 C CZ  A ARG   A 141 ? 0.2244 0.3354 0.3447 -0.0523 0.0047  -0.0217 141 ARG   A CZ  
2964 C CZ  B ARG   A 141 ? 0.2116 0.2529 0.2990 -0.0167 -0.0085 0.0061  141 ARG   A CZ  
2965 N NH1 A ARG   A 141 ? 0.2078 0.3339 0.3267 -0.0623 0.0205  -0.0344 141 ARG   A NH1 
2966 N NH1 B ARG   A 141 ? 0.2164 0.2657 0.3084 -0.0145 -0.0018 0.0037  141 ARG   A NH1 
2967 N NH2 A ARG   A 141 ? 0.2321 0.3553 0.3647 -0.0531 -0.0110 -0.0106 141 ARG   A NH2 
2968 N NH2 B ARG   A 141 ? 0.2079 0.2504 0.3045 -0.0144 -0.0147 0.0117  141 ARG   A NH2 
2995 N N   . VAL   A 142 ? 0.1449 0.1738 0.1905 -0.0137 -0.0035 0.0072  142 VAL   A N   
2996 C CA  . VAL   A 142 ? 0.1479 0.1758 0.1856 -0.0089 0.0116  0.0020  142 VAL   A CA  
2997 C C   . VAL   A 142 ? 0.1337 0.1675 0.1797 -0.0200 0.0087  0.0083  142 VAL   A C   
2998 O O   . VAL   A 142 ? 0.1463 0.1605 0.1953 -0.0031 0.0073  0.0125  142 VAL   A O   
2999 C CB  . VAL   A 142 ? 0.1585 0.1811 0.1813 -0.0095 0.0092  0.0094  142 VAL   A CB  
3000 C CG1 . VAL   A 142 ? 0.1579 0.1759 0.1867 -0.0128 0.0133  0.0099  142 VAL   A CG1 
3001 C CG2 . VAL   A 142 ? 0.1615 0.1921 0.1981 -0.0000 0.0074  0.0137  142 VAL   A CG2 
3012 N N   . CYS   A 143 ? 0.1402 0.1685 0.1705 -0.0167 0.0057  0.0063  143 CYS   A N   
3013 C CA  . CYS   A 143 ? 0.1471 0.1648 0.1751 -0.0117 0.0139  0.0154  143 CYS   A CA  
3014 C C   . CYS   A 143 ? 0.1514 0.1522 0.1745 -0.0175 0.0014  0.0261  143 CYS   A C   
3015 O O   . CYS   A 143 ? 0.1471 0.1596 0.1801 -0.0108 -0.0051 0.0272  143 CYS   A O   
3016 C CB  . CYS   A 143 ? 0.1497 0.1693 0.1849 -0.0047 0.0205  0.0222  143 CYS   A CB  
3017 S SG  . CYS   A 143 ? 0.1665 0.1716 0.1863 0.0018  0.0116  0.0153  143 CYS   A SG  
3023 N N   . VAL   A 144 ? 0.1505 0.1572 0.2022 -0.0124 0.0123  0.0340  144 VAL   A N   
3024 C CA  . VAL   A 144 ? 0.1463 0.1744 0.2424 -0.0131 0.0178  0.0324  144 VAL   A CA  
3025 C C   . VAL   A 144 ? 0.1442 0.1708 0.2307 -0.0213 -0.0104 0.0226  144 VAL   A C   
3026 O O   . VAL   A 144 ? 0.1625 0.1785 0.2363 -0.0084 -0.0111 0.0363  144 VAL   A O   
3027 C CB  . VAL   A 144 ? 0.1680 0.1936 0.3158 -0.0075 0.0358  0.0347  144 VAL   A CB  
3028 C CG1 . VAL   A 144 ? 0.1869 0.2126 0.3567 -0.0113 0.0100  0.0428  144 VAL   A CG1 
3029 C CG2 . VAL   A 144 ? 0.1567 0.1985 0.3176 -0.0112 0.0454  0.0409  144 VAL   A CG2 
3039 N N   . ASP   A 145 ? 0.1555 0.1625 0.2349 -0.0165 -0.0003 0.0065  145 ASP   A N   
3040 C CA  . ASP   A 145 ? 0.1606 0.1709 0.2388 -0.0231 -0.0112 -0.0021 145 ASP   A CA  
3041 C C   . ASP   A 145 ? 0.1636 0.1592 0.2375 -0.0147 -0.0053 0.0005  145 ASP   A C   
3042 O O   . ASP   A 145 ? 0.1777 0.1663 0.2965 -0.0109 -0.0093 -0.0377 145 ASP   A O   
3043 C CB  . ASP   A 145 ? 0.1791 0.2023 0.2627 -0.0267 -0.0238 -0.0027 145 ASP   A CB  
3044 C CG  . ASP   A 145 ? 0.1946 0.2248 0.2951 -0.0382 -0.0290 0.0113  145 ASP   A CG  
3045 O OD1 . ASP   A 145 ? 0.1958 0.2363 0.3081 -0.0552 -0.0216 0.0225  145 ASP   A OD1 
3046 O OD2 . ASP   A 145 ? 0.2163 0.2487 0.3083 -0.0519 -0.0437 0.0022  145 ASP   A OD2 
3051 N N   . THR   A 146 ? 0.1526 0.1513 0.1994 -0.0174 0.0071  0.0112  146 THR   A N   
3052 C CA  . THR   A 146 ? 0.1372 0.1544 0.1829 -0.0081 0.0044  0.0044  146 THR   A CA  
3053 C C   . THR   A 146 ? 0.1393 0.1513 0.1924 -0.0037 0.0083  0.0136  146 THR   A C   
3054 O O   . THR   A 146 ? 0.1482 0.1535 0.2112 0.0048  -0.0032 0.0076  146 THR   A O   
3055 C CB  . THR   A 146 ? 0.1385 0.1550 0.1754 -0.0033 0.0069  0.0147  146 THR   A CB  
3056 O OG1 . THR   A 146 ? 0.1466 0.1754 0.1932 -0.0006 0.0005  0.0085  146 THR   A OG1 
3057 C CG2 . THR   A 146 ? 0.1541 0.1574 0.2025 -0.0097 0.0143  0.0094  146 THR   A CG2 
3065 N N   . VAL   A 147 ? 0.1376 0.1510 0.1853 -0.0000 0.0063  0.0204  147 VAL   A N   
3066 C CA  . VAL   A 147 ? 0.1400 0.1506 0.1899 -0.0111 0.0212  0.0208  147 VAL   A CA  
3067 C C   . VAL   A 147 ? 0.1491 0.1489 0.2029 -0.0171 0.0153  0.0317  147 VAL   A C   
3068 O O   . VAL   A 147 ? 0.1554 0.1500 0.2137 -0.0215 0.0083  0.0233  147 VAL   A O   
3069 C CB  . VAL   A 147 ? 0.1500 0.1557 0.1838 -0.0138 0.0164  0.0251  147 VAL   A CB  
3070 C CG1 . VAL   A 147 ? 0.1749 0.1689 0.1845 -0.0110 0.0112  0.0313  147 VAL   A CG1 
3071 C CG2 . VAL   A 147 ? 0.1588 0.1560 0.1830 -0.0147 0.0062  0.0199  147 VAL   A CG2 
3081 N N   . ARG   A 148 ? 0.1520 0.1564 0.2022 -0.0170 0.0130  0.0435  148 ARG   A N   
3082 C CA  . ARG   A 148 ? 0.1560 0.1581 0.1996 -0.0147 0.0073  0.0498  148 ARG   A CA  
3083 C C   . ARG   A 148 ? 0.1705 0.1573 0.1962 -0.0161 0.0135  0.0590  148 ARG   A C   
3084 O O   . ARG   A 148 ? 0.2005 0.1689 0.2251 -0.0231 0.0160  0.0500  148 ARG   A O   
3085 C CB  . ARG   A 148 ? 0.1573 0.1633 0.2166 -0.0111 0.0187  0.0443  148 ARG   A CB  
3086 C CG  . ARG   A 148 ? 0.1725 0.1639 0.2435 -0.0096 0.0265  0.0288  148 ARG   A CG  
3087 C CD  . ARG   A 148 ? 0.1894 0.1597 0.2763 -0.0028 0.0382  0.0485  148 ARG   A CD  
3088 N NE  . ARG   A 148 ? 0.1859 0.1703 0.2794 0.0045  0.0462  0.0472  148 ARG   A NE  
3089 C CZ  . ARG   A 148 ? 0.1831 0.1534 0.2591 0.0048  0.0474  0.0403  148 ARG   A CZ  
3090 N NH1 . ARG   A 148 ? 0.1866 0.1649 0.2707 -0.0091 0.0407  0.0202  148 ARG   A NH1 
3091 N NH2 . ARG   A 148 ? 0.1766 0.1764 0.2652 0.0097  0.0476  0.0464  148 ARG   A NH2 
3105 N N   . THR   A 149 ? 0.1648 0.1677 0.1932 -0.0169 -0.0043 0.0455  149 THR   A N   
3106 C CA  . THR   A 149 ? 0.1636 0.1748 0.1969 -0.0165 -0.0020 0.0501  149 THR   A CA  
3107 C C   . THR   A 149 ? 0.1605 0.1766 0.1879 -0.0304 0.0118  0.0530  149 THR   A C   
3108 O O   . THR   A 149 ? 0.1566 0.1851 0.2063 -0.0285 0.0044  0.0474  149 THR   A O   
3109 C CB  . THR   A 149 ? 0.1658 0.1896 0.2058 -0.0196 0.0059  0.0386  149 THR   A CB  
3110 O OG1 . THR   A 149 ? 0.1712 0.1747 0.2184 -0.0292 0.0038  0.0288  149 THR   A OG1 
3111 C CG2 . THR   A 149 ? 0.1700 0.2042 0.2125 -0.0146 -0.0112 0.0323  149 THR   A CG2 
3119 N N   . ASN   A 150 ? 0.1582 0.1772 0.1817 -0.0097 0.0069  0.0522  150 ASN   A N   
3120 C CA  . ASN   A 150 ? 0.1824 0.1935 0.1761 -0.0170 0.0177  0.0498  150 ASN   A CA  
3121 C C   . ASN   A 150 ? 0.1669 0.1772 0.1791 -0.0223 0.0039  0.0406  150 ASN   A C   
3122 O O   . ASN   A 150 ? 0.1736 0.1874 0.2263 -0.0212 -0.0169 0.0351  150 ASN   A O   
3123 C CB  . ASN   A 150 ? 0.2314 0.2195 0.2137 -0.0219 0.0382  0.0664  150 ASN   A CB  
3124 C CG  . ASN   A 150 ? 0.2872 0.2522 0.2917 -0.0186 0.0109  0.0742  150 ASN   A CG  
3125 O OD1 . ASN   A 150 ? 0.3134 0.2620 0.3078 -0.0310 0.0041  0.0936  150 ASN   A OD1 
3126 N ND2 . ASN   A 150 ? 0.3147 0.2740 0.3291 -0.0145 -0.0061 0.0714  150 ASN   A ND2 
3133 N N   . VAL   A 151 ? 0.1651 0.1671 0.1769 -0.0252 0.0024  0.0404  151 VAL   A N   
3134 C CA  . VAL   A 151 ? 0.1671 0.1692 0.1697 -0.0244 0.0053  0.0411  151 VAL   A CA  
3135 C C   . VAL   A 151 ? 0.1642 0.1609 0.1809 -0.0350 0.0078  0.0406  151 VAL   A C   
3136 O O   . VAL   A 151 ? 0.1721 0.1696 0.2137 -0.0314 0.0075  0.0322  151 VAL   A O   
3137 C CB  . VAL   A 151 ? 0.1947 0.1869 0.1824 -0.0098 0.0075  0.0390  151 VAL   A CB  
3138 C CG1 . VAL   A 151 ? 0.1932 0.2060 0.2046 -0.0120 -0.0020 0.0434  151 VAL   A CG1 
3139 C CG2 . VAL   A 151 ? 0.2091 0.1825 0.1838 -0.0093 0.0173  0.0372  151 VAL   A CG2 
3149 N N   . TYR   A 152 ? 0.1591 0.1637 0.1885 -0.0298 0.0073  0.0372  152 TYR   A N   
3150 C CA  . TYR   A 152 ? 0.1609 0.1755 0.1622 -0.0296 0.0115  0.0339  152 TYR   A CA  
3151 C C   . TYR   A 152 ? 0.1566 0.1720 0.1467 -0.0236 0.0137  0.0366  152 TYR   A C   
3152 O O   . TYR   A 152 ? 0.1587 0.1666 0.1660 -0.0269 0.0249  0.0274  152 TYR   A O   
3153 C CB  . TYR   A 152 ? 0.1815 0.1760 0.1584 -0.0247 0.0214  0.0339  152 TYR   A CB  
3154 C CG  . TYR   A 152 ? 0.1922 0.1952 0.1674 -0.0260 0.0275  0.0386  152 TYR   A CG  
3155 C CD1 . TYR   A 152 ? 0.1977 0.2182 0.1965 -0.0124 0.0273  0.0472  152 TYR   A CD1 
3156 C CD2 . TYR   A 152 ? 0.1972 0.2087 0.1621 -0.0428 0.0166  0.0363  152 TYR   A CD2 
3157 C CE1 . TYR   A 152 ? 0.2230 0.2317 0.1993 -0.0105 0.0050  0.0658  152 TYR   A CE1 
3158 C CE2 . TYR   A 152 ? 0.2189 0.2285 0.1825 -0.0407 0.0188  0.0380  152 TYR   A CE2 
3159 C CZ  . TYR   A 152 ? 0.2403 0.2345 0.1712 -0.0284 0.0051  0.0674  152 TYR   A CZ  
3160 O OH  . TYR   A 152 ? 0.2773 0.2615 0.2107 -0.0195 0.0116  0.0811  152 TYR   A OH  
3170 N N   A LEU   A 153 ? 0.1533 0.1742 0.1560 -0.0276 0.0125  0.0364  153 LEU   A N   
3171 N N   B LEU   A 153 ? 0.1573 0.1791 0.1447 -0.0192 0.0094  0.0324  153 LEU   A N   
3172 C CA  A LEU   A 153 ? 0.1509 0.1620 0.1792 -0.0132 0.0163  0.0364  153 LEU   A CA  
3173 C CA  B LEU   A 153 ? 0.1583 0.1802 0.1443 -0.0078 0.0120  0.0255  153 LEU   A CA  
3174 C C   A LEU   A 153 ? 0.1501 0.1588 0.1857 -0.0146 0.0325  0.0368  153 LEU   A C   
3175 C C   B LEU   A 153 ? 0.1579 0.1821 0.1362 -0.0071 0.0170  0.0181  153 LEU   A C   
3176 O O   A LEU   A 153 ? 0.1633 0.1701 0.2119 -0.0183 0.0445  0.0242  153 LEU   A O   
3177 O O   B LEU   A 153 ? 0.1615 0.1888 0.1517 -0.0120 0.0202  0.0161  153 LEU   A O   
3178 C CB  A LEU   A 153 ? 0.1369 0.1558 0.1886 -0.0127 0.0203  0.0368  153 LEU   A CB  
3179 C CB  B LEU   A 153 ? 0.1557 0.1795 0.1552 -0.0012 0.0109  0.0275  153 LEU   A CB  
3180 C CG  A LEU   A 153 ? 0.1422 0.1523 0.1903 -0.0169 0.0279  0.0224  153 LEU   A CG  
3181 C CG  B LEU   A 153 ? 0.1598 0.1797 0.1594 0.0008  0.0111  0.0281  153 LEU   A CG  
3182 C CD1 A LEU   A 153 ? 0.1601 0.1440 0.1943 -0.0131 0.0129  0.0195  153 LEU   A CD1 
3183 C CD1 B LEU   A 153 ? 0.1660 0.1782 0.1646 0.0061  0.0071  0.0301  153 LEU   A CD1 
3184 C CD2 A LEU   A 153 ? 0.1510 0.1661 0.1914 -0.0213 0.0339  0.0004  153 LEU   A CD2 
3185 C CD2 B LEU   A 153 ? 0.1620 0.1850 0.1670 -0.0026 0.0129  0.0233  153 LEU   A CD2 
3208 N N   A ALA   A 154 ? 0.1488 0.1522 0.1912 -0.0133 0.0288  0.0353  154 ALA   A N   
3209 N N   B ALA   A 154 ? 0.1603 0.1805 0.1246 -0.0051 0.0179  0.0163  154 ALA   A N   
3210 C CA  A ALA   A 154 ? 0.1636 0.1552 0.1974 -0.0093 0.0347  0.0234  154 ALA   A CA  
3211 C CA  B ALA   A 154 ? 0.1692 0.1811 0.1373 -0.0038 0.0106  0.0119  154 ALA   A CA  
3212 C C   A ALA   A 154 ? 0.1574 0.1429 0.1825 -0.0031 0.0269  0.0300  154 ALA   A C   
3213 C C   B ALA   A 154 ? 0.1699 0.1781 0.1334 -0.0026 0.0046  0.0160  154 ALA   A C   
3214 O O   A ALA   A 154 ? 0.1621 0.1554 0.1926 -0.0112 0.0170  0.0211  154 ALA   A O   
3215 O O   B ALA   A 154 ? 0.1756 0.1748 0.1260 -0.0100 0.0113  0.0136  154 ALA   A O   
3216 C CB  A ALA   A 154 ? 0.1843 0.1608 0.1890 0.0028  0.0363  0.0088  154 ALA   A CB  
3217 C CB  B ALA   A 154 ? 0.1769 0.1826 0.1467 -0.0023 0.0046  0.0062  154 ALA   A CB  
3228 N N   A VAL   A 155 ? 0.1398 0.1215 0.1458 0.0031  0.0316  0.0399  155 VAL   A N   
3229 N N   B VAL   A 155 ? 0.1726 0.1792 0.1482 0.0051  0.0023  0.0241  155 VAL   A N   
3230 C CA  A VAL   A 155 ? 0.1502 0.1464 0.2052 -0.0038 0.0259  0.0502  155 VAL   A CA  
3231 C CA  B VAL   A 155 ? 0.1872 0.1954 0.1780 0.0078  -0.0106 0.0164  155 VAL   A CA  
3232 C CA  T VAL   A 155 ? 0.1868 0.1932 0.2081 -0.0095 0.0286  0.0540  155 VAL   A CA  
3233 C C   A VAL   A 155 ? 0.1585 0.1660 0.2355 0.0129  0.0295  0.0627  155 VAL   A C   
3234 C C   B VAL   A 155 ? 0.2036 0.2141 0.2146 0.0171  -0.0123 0.0129  155 VAL   A C   
3235 C C   T VAL   A 155 ? 0.1911 0.1948 0.1925 0.0019  0.0395  0.0599  155 VAL   A C   
3236 O O   A VAL   A 155 ? 0.1581 0.1736 0.2686 0.0243  0.0440  0.0529  155 VAL   A O   
3237 O O   B VAL   A 155 ? 0.2042 0.2219 0.2265 0.0204  -0.0110 0.0137  155 VAL   A O   
3238 O O   T VAL   A 155 ? 0.1892 0.2033 0.1861 0.0027  0.0463  0.0550  155 VAL   A O   
3239 C CB  A VAL   A 155 ? 0.1582 0.1550 0.2266 -0.0098 0.0125  0.0439  155 VAL   A CB  
3240 C CB  B VAL   A 155 ? 0.1865 0.1922 0.1812 0.0038  -0.0133 0.0119  155 VAL   A CB  
3241 C CB  T VAL   A 155 ? 0.1868 0.1951 0.2193 -0.0123 0.0163  0.0466  155 VAL   A CB  
3242 C CG1 A VAL   A 155 ? 0.1725 0.1618 0.2352 -0.0078 -0.0032 0.0360  155 VAL   A CG1 
3243 C CG1 B VAL   A 155 ? 0.1870 0.1945 0.1890 -0.0017 -0.0139 0.0182  155 VAL   A CG1 
3244 C CG1 T VAL   A 155 ? 0.1917 0.1970 0.2223 -0.0097 0.0059  0.0440  155 VAL   A CG1 
3245 C CG2 A VAL   A 155 ? 0.1666 0.1659 0.2460 -0.0076 -0.0035 0.0402  155 VAL   A CG2 
3246 C CG2 B VAL   A 155 ? 0.1846 0.1896 0.1773 0.0002  -0.0180 0.0076  155 VAL   A CG2 
3247 C CG2 T VAL   A 155 ? 0.1894 0.2003 0.2296 -0.0123 0.0088  0.0429  155 VAL   A CG2 
3273 N N   A PHE   A 156 ? 0.1739 0.1750 0.2605 0.0203  0.0236  0.0728  156 PHE   A N   
3274 N N   B PHE   A 156 ? 0.2193 0.2225 0.2304 0.0230  -0.0073 0.0068  156 PHE   A N   
3275 N N   T PHE   A 156 ? 0.2023 0.1864 0.1974 0.0125  0.0420  0.0695  156 PHE   A N   
3276 C CA  A PHE   A 156 ? 0.1921 0.1881 0.2994 0.0286  0.0211  0.0665  156 PHE   A CA  
3277 C CA  B PHE   A 156 ? 0.2351 0.2329 0.2505 0.0279  0.0061  -0.0019 156 PHE   A CA  
3278 C CA  T PHE   A 156 ? 0.2178 0.1824 0.2026 0.0188  0.0425  0.0714  156 PHE   A CA  
3279 C C   A PHE   A 156 ? 0.1911 0.1922 0.3091 0.0383  0.0377  0.0760  156 PHE   A C   
3280 C C   B PHE   A 156 ? 0.2421 0.2464 0.2640 0.0245  0.0100  0.0089  156 PHE   A C   
3281 C C   T PHE   A 156 ? 0.2172 0.1938 0.2274 0.0257  0.0532  0.0717  156 PHE   A C   
3282 O O   A PHE   A 156 ? 0.2032 0.1984 0.3223 0.0259  0.0478  0.0677  156 PHE   A O   
3283 O O   B PHE   A 156 ? 0.2428 0.2460 0.2699 0.0243  0.0055  0.0095  156 PHE   A O   
3284 O O   T PHE   A 156 ? 0.2233 0.1938 0.2294 0.0243  0.0671  0.0601  156 PHE   A O   
3285 C CB  A PHE   A 156 ? 0.2085 0.1965 0.3091 0.0237  0.0008  0.0582  156 PHE   A CB  
3286 C CB  B PHE   A 156 ? 0.2452 0.2353 0.2528 0.0311  0.0131  -0.0161 156 PHE   A CB  
3287 C CB  T PHE   A 156 ? 0.2253 0.1682 0.1836 0.0191  0.0283  0.0649  156 PHE   A CB  
3288 C CG  A PHE   A 156 ? 0.2298 0.2071 0.3268 0.0224  -0.0154 0.0490  156 PHE   A CG  
3289 C CG  B PHE   A 156 ? 0.2551 0.2388 0.2576 0.0344  0.0150  -0.0236 156 PHE   A CG  
3290 C CG  T PHE   A 156 ? 0.2304 0.1646 0.1676 0.0208  0.0256  0.0573  156 PHE   A CG  
3291 C CD1 A PHE   A 156 ? 0.2378 0.2126 0.3231 0.0254  -0.0088 0.0457  156 PHE   A CD1 
3292 C CD1 B PHE   A 156 ? 0.2595 0.2389 0.2583 0.0386  0.0175  -0.0293 156 PHE   A CD1 
3293 C CD1 T PHE   A 156 ? 0.2310 0.1689 0.1793 0.0206  0.0199  0.0441  156 PHE   A CD1 
3294 C CD2 A PHE   A 156 ? 0.2446 0.2211 0.3365 0.0270  -0.0244 0.0442  156 PHE   A CD2 
3295 C CD2 B PHE   A 156 ? 0.2570 0.2406 0.2624 0.0334  0.0113  -0.0273 156 PHE   A CD2 
3296 C CD2 T PHE   A 156 ? 0.2345 0.1675 0.1721 0.0235  0.0289  0.0517  156 PHE   A CD2 
3297 C CE1 A PHE   A 156 ? 0.2486 0.2213 0.3364 0.0276  -0.0034 0.0364  156 PHE   A CE1 
3298 C CE1 B PHE   A 156 ? 0.2621 0.2399 0.2620 0.0369  0.0191  -0.0296 156 PHE   A CE1 
3299 C CE1 T PHE   A 156 ? 0.2346 0.1713 0.1908 0.0190  0.0195  0.0380  156 PHE   A CE1 
3300 C CE2 A PHE   A 156 ? 0.2577 0.2308 0.3394 0.0283  -0.0205 0.0333  156 PHE   A CE2 
3301 C CE2 B PHE   A 156 ? 0.2608 0.2420 0.2637 0.0357  0.0125  -0.0286 156 PHE   A CE2 
3302 C CE2 T PHE   A 156 ? 0.2403 0.1723 0.1837 0.0193  0.0282  0.0439  156 PHE   A CE2 
3303 C CZ  A PHE   A 156 ? 0.2570 0.2298 0.3384 0.0313  -0.0051 0.0283  156 PHE   A CZ  
3304 C CZ  B PHE   A 156 ? 0.2622 0.2411 0.2639 0.0361  0.0164  -0.0295 156 PHE   A CZ  
3305 C CZ  T PHE   A 156 ? 0.2382 0.1687 0.1947 0.0146  0.0227  0.0402  156 PHE   A CZ  
3333 N N   A ASP   A 157 ? 0.1855 0.1990 0.2957 0.0466  0.0330  0.0890  157 ASP   A N   
3334 N N   B ASP   A 157 ? 0.2461 0.2572 0.2745 0.0220  0.0125  0.0140  157 ASP   A N   
3335 N N   T ASP   A 157 ? 0.2066 0.2065 0.2415 0.0251  0.0420  0.0856  157 ASP   A N   
3336 C CA  A ASP   A 157 ? 0.1975 0.2209 0.3012 0.0513  0.0408  0.0916  157 ASP   A CA  
3337 C CA  B ASP   A 157 ? 0.2487 0.2721 0.2841 0.0192  0.0209  0.0286  157 ASP   A CA  
3338 C CA  T ASP   A 157 ? 0.2045 0.2200 0.2458 0.0305  0.0452  0.0966  157 ASP   A CA  
3339 C C   A ASP   A 157 ? 0.1841 0.2413 0.3156 0.0551  0.0495  0.1031  157 ASP   A C   
3340 C C   B ASP   A 157 ? 0.2458 0.2805 0.3008 0.0202  0.0183  0.0323  157 ASP   A C   
3341 C C   T ASP   A 157 ? 0.2080 0.2363 0.2591 0.0344  0.0489  0.1050  157 ASP   A C   
3342 O O   A ASP   A 157 ? 0.1699 0.2385 0.2970 0.0525  0.0550  0.1138  157 ASP   A O   
3343 O O   B ASP   A 157 ? 0.2461 0.2827 0.3019 0.0163  0.0202  0.0301  157 ASP   A O   
3344 O O   T ASP   A 157 ? 0.1988 0.2342 0.2567 0.0366  0.0466  0.1081  157 ASP   A O   
3345 C CB  A ASP   A 157 ? 0.2213 0.2282 0.3118 0.0594  0.0388  0.0815  157 ASP   A CB  
3346 C CB  B ASP   A 157 ? 0.2508 0.2761 0.2793 0.0173  0.0328  0.0385  157 ASP   A CB  
3347 C CB  T ASP   A 157 ? 0.2005 0.2183 0.2501 0.0362  0.0423  0.0987  157 ASP   A CB  
3348 C CG  A ASP   A 157 ? 0.2421 0.2389 0.3335 0.0668  0.0350  0.0716  157 ASP   A CG  
3349 C CG  B ASP   A 157 ? 0.2503 0.2783 0.2741 0.0154  0.0461  0.0480  157 ASP   A CG  
3350 C CG  T ASP   A 157 ? 0.1966 0.2155 0.2548 0.0392  0.0324  0.0952  157 ASP   A CG  
3351 O OD1 A ASP   A 157 ? 0.2600 0.2478 0.3447 0.0614  0.0282  0.0647  157 ASP   A OD1 
3352 O OD1 B ASP   A 157 ? 0.2518 0.2736 0.2648 0.0132  0.0474  0.0577  157 ASP   A OD1 
3353 O OD1 T ASP   A 157 ? 0.1967 0.2150 0.2686 0.0349  0.0385  0.0750  157 ASP   A OD1 
3354 O OD2 A ASP   A 157 ? 0.2379 0.2329 0.3536 0.0695  0.0423  0.0755  157 ASP   A OD2 
3355 O OD2 B ASP   A 157 ? 0.2441 0.2841 0.2794 0.0103  0.0596  0.0457  157 ASP   A OD2 
3356 O OD2 T ASP   A 157 ? 0.1859 0.2130 0.2452 0.0392  0.0182  0.1091  157 ASP   A OD2 
3369 N N   A LYS   A 158 ? 0.1905 0.2672 0.3509 0.0630  0.0626  0.0924  158 LYS   A N   
3370 N N   B LYS   A 158 ? 0.2457 0.2867 0.3188 0.0247  0.0136  0.0387  158 LYS   A N   
3371 N N   T LYS   A 158 ? 0.2215 0.2578 0.2852 0.0383  0.0563  0.0969  158 LYS   A N   
3372 C CA  A LYS   A 158 ? 0.1906 0.2928 0.3673 0.0662  0.0767  0.0858  158 LYS   A CA  
3373 C CA  B LYS   A 158 ? 0.2462 0.2942 0.3265 0.0280  0.0163  0.0470  158 LYS   A CA  
3374 C CA  T LYS   A 158 ? 0.2343 0.2815 0.3111 0.0409  0.0539  0.0850  158 LYS   A CA  
3375 C C   A LYS   A 158 ? 0.1711 0.3054 0.3530 0.0692  0.0614  0.0990  158 LYS   A C   
3376 C C   B LYS   A 158 ? 0.2303 0.2964 0.3143 0.0319  0.0076  0.0581  158 LYS   A C   
3377 C C   T LYS   A 158 ? 0.2323 0.2919 0.3106 0.0411  0.0397  0.0841  158 LYS   A C   
3378 O O   A LYS   A 158 ? 0.1614 0.3142 0.3642 0.0612  0.0622  0.0966  158 LYS   A O   
3379 O O   B LYS   A 158 ? 0.2253 0.2991 0.3142 0.0260  0.0035  0.0622  158 LYS   A O   
3380 O O   T LYS   A 158 ? 0.2312 0.2975 0.3193 0.0403  0.0374  0.0794  158 LYS   A O   
3381 C CB  A LYS   A 158 ? 0.2145 0.3028 0.3987 0.0620  0.0969  0.0773  158 LYS   A CB  
3382 C CB  B LYS   A 158 ? 0.2593 0.3008 0.3483 0.0263  0.0286  0.0422  158 LYS   A CB  
3383 C CB  T LYS   A 158 ? 0.2540 0.2954 0.3476 0.0415  0.0584  0.0690  158 LYS   A CB  
3384 C CG  A LYS   A 158 ? 0.2416 0.3118 0.4260 0.0596  0.1103  0.0782  158 LYS   A CG  
3385 C CG  B LYS   A 158 ? 0.2708 0.3084 0.3678 0.0223  0.0436  0.0386  158 LYS   A CG  
3386 C CG  T LYS   A 158 ? 0.2737 0.3079 0.3792 0.0424  0.0639  0.0614  158 LYS   A CG  
3387 C CD  A LYS   A 158 ? 0.2627 0.3222 0.4458 0.0579  0.1261  0.0833  158 LYS   A CD  
3388 C CD  B LYS   A 158 ? 0.2791 0.3137 0.3818 0.0194  0.0582  0.0387  158 LYS   A CD  
3389 C CD  T LYS   A 158 ? 0.2895 0.3184 0.4085 0.0446  0.0680  0.0602  158 LYS   A CD  
3390 C CE  A LYS   A 158 ? 0.2747 0.3259 0.4605 0.0516  0.1398  0.0933  158 LYS   A CE  
3391 C CE  B LYS   A 158 ? 0.2848 0.3151 0.3945 0.0191  0.0680  0.0381  158 LYS   A CE  
3392 C CE  T LYS   A 158 ? 0.3002 0.3232 0.4320 0.0447  0.0704  0.0612  158 LYS   A CE  
3393 N NZ  A LYS   A 158 ? 0.2793 0.3299 0.4693 0.0453  0.1469  0.0999  158 LYS   A NZ  
3394 N NZ  B LYS   A 158 ? 0.2864 0.3157 0.3998 0.0196  0.0735  0.0373  158 LYS   A NZ  
3395 N NZ  T LYS   A 158 ? 0.3055 0.3271 0.4435 0.0452  0.0702  0.0608  158 LYS   A NZ  
3435 N N   A ASN   A 159 ? 0.1702 0.3117 0.3518 0.0678  0.0396  0.1032  159 ASN   A N   
3436 N N   B ASN   A 159 ? 0.2216 0.2974 0.3094 0.0399  0.0059  0.0584  159 ASN   A N   
3437 N N   T ASN   A 159 ? 0.2353 0.2977 0.3184 0.0361  0.0261  0.0783  159 ASN   A N   
3438 C CA  A ASN   A 159 ? 0.1736 0.3158 0.3373 0.0564  0.0237  0.1119  159 ASN   A CA  
3439 C CA  B ASN   A 159 ? 0.2154 0.2983 0.2984 0.0418  0.0056  0.0524  159 ASN   A CA  
3440 C CA  T ASN   A 159 ? 0.2419 0.3032 0.3177 0.0255  0.0193  0.0743  159 ASN   A CA  
3441 C C   A ASN   A 159 ? 0.1609 0.3154 0.3091 0.0439  0.0250  0.1071  159 ASN   A C   
3442 C C   B ASN   A 159 ? 0.2041 0.2941 0.2864 0.0397  0.0043  0.0449  159 ASN   A C   
3443 C C   T ASN   A 159 ? 0.2424 0.3063 0.3094 0.0154  0.0222  0.0633  159 ASN   A C   
3444 O O   A ASN   A 159 ? 0.1397 0.3255 0.3039 0.0417  0.0152  0.0893  159 ASN   A O   
3445 O O   B ASN   A 159 ? 0.1986 0.3023 0.2911 0.0432  -0.0072 0.0474  159 ASN   A O   
3446 O O   T ASN   A 159 ? 0.2390 0.3107 0.3135 0.0126  0.0203  0.0513  159 ASN   A O   
3447 C CB  A ASN   A 159 ? 0.2027 0.3258 0.3655 0.0506  0.0126  0.1149  159 ASN   A CB  
3448 C CB  B ASN   A 159 ? 0.2220 0.3025 0.3028 0.0424  0.0076  0.0481  159 ASN   A CB  
3449 C CB  T ASN   A 159 ? 0.2529 0.3088 0.3355 0.0222  0.0122  0.0768  159 ASN   A CB  
3450 C CG  A ASN   A 159 ? 0.2277 0.3395 0.3984 0.0410  0.0115  0.1090  159 ASN   A CG  
3451 C CG  B ASN   A 159 ? 0.2269 0.3076 0.3076 0.0340  0.0138  0.0387  159 ASN   A CG  
3452 C CG  T ASN   A 159 ? 0.2631 0.3159 0.3569 0.0180  0.0090  0.0756  159 ASN   A CG  
3453 O OD1 A ASN   A 159 ? 0.2384 0.3503 0.4192 0.0349  0.0223  0.1034  159 ASN   A OD1 
3454 O OD1 B ASN   A 159 ? 0.2312 0.3139 0.3203 0.0301  0.0212  0.0334  159 ASN   A OD1 
3455 O OD1 T ASN   A 159 ? 0.2671 0.3234 0.3732 0.0153  0.0161  0.0705  159 ASN   A OD1 
3456 N ND2 A ASN   A 159 ? 0.2355 0.3454 0.4100 0.0403  0.0068  0.1026  159 ASN   A ND2 
3457 N ND2 B ASN   A 159 ? 0.2258 0.3081 0.3079 0.0315  0.0095  0.0389  159 ASN   A ND2 
3458 N ND2 T ASN   A 159 ? 0.2667 0.3190 0.3614 0.0181  0.0028  0.0747  159 ASN   A ND2 
3477 N N   A LEU   A 160 ? 0.1570 0.3006 0.2761 0.0339  0.0110  0.1224  160 LEU   A N   
3478 N N   B LEU   A 160 ? 0.1956 0.2813 0.2680 0.0314  0.0055  0.0373  160 LEU   A N   
3479 N N   T LEU   A 160 ? 0.2417 0.3013 0.2979 0.0073  0.0190  0.0654  160 LEU   A N   
3480 C CA  A LEU   A 160 ? 0.1612 0.2819 0.2363 0.0171  0.0119  0.1283  160 LEU   A CA  
3481 C CA  B LEU   A 160 ? 0.1877 0.2673 0.2342 0.0252  0.0086  0.0284  160 LEU   A CA  
3482 C CA  T LEU   A 160 ? 0.2442 0.2939 0.2811 -0.0021 0.0202  0.0665  160 LEU   A CA  
3483 C C   A LEU   A 160 ? 0.1415 0.2721 0.2007 0.0076  0.0158  0.1186  160 LEU   A C   
3484 C C   B LEU   A 160 ? 0.1762 0.2580 0.1985 0.0232  0.0202  0.0228  160 LEU   A C   
3485 O O   A LEU   A 160 ? 0.1247 0.2763 0.1896 0.0026  0.0046  0.1191  160 LEU   A O   
3486 O O   B LEU   A 160 ? 0.1672 0.2576 0.1825 0.0220  0.0190  0.0330  160 LEU   A O   
3487 C CB  A LEU   A 160 ? 0.1699 0.2775 0.2281 0.0082  0.0112  0.1253  160 LEU   A CB  
3488 C CB  B LEU   A 160 ? 0.1924 0.2646 0.2325 0.0153  0.0114  0.0244  160 LEU   A CB  
3489 C CB  T LEU   A 160 ? 0.2443 0.2888 0.2632 -0.0126 0.0234  0.0631  160 LEU   A CB  
3490 C CG  A LEU   A 160 ? 0.1847 0.2808 0.2512 -0.0055 0.0096  0.0953  160 LEU   A CG  
3491 C CG  B LEU   A 160 ? 0.1967 0.2642 0.2330 0.0065  0.0085  0.0163  160 LEU   A CG  
3492 C CG  T LEU   A 160 ? 0.2470 0.2869 0.2593 -0.0225 0.0242  0.0520  160 LEU   A CG  
3493 C CD1 A LEU   A 160 ? 0.1938 0.2878 0.2585 -0.0079 0.0031  0.0828  160 LEU   A CD1 
3494 C CD1 B LEU   A 160 ? 0.2017 0.2638 0.2334 0.0016  0.0032  0.0155  160 LEU   A CD1 
3495 C CD1 T LEU   A 160 ? 0.2499 0.2894 0.2597 -0.0229 0.0206  0.0460  160 LEU   A CD1 
3496 C CD2 A LEU   A 160 ? 0.1850 0.2794 0.2615 -0.0122 0.0174  0.0816  160 LEU   A CD2 
3497 C CD2 B LEU   A 160 ? 0.1963 0.2659 0.2265 0.0035  0.0160  0.0090  160 LEU   A CD2 
3498 C CD2 T LEU   A 160 ? 0.2454 0.2834 0.2588 -0.0284 0.0306  0.0494  160 LEU   A CD2 
3531 N N   A TYR   A 161 ? 0.1585 0.2628 0.2191 0.0036  0.0232  0.1010  161 TYR   A N   
3532 N N   B TYR   A 161 ? 0.1827 0.2497 0.1912 0.0230  0.0177  0.0049  161 TYR   A N   
3533 C CA  A TYR   A 161 ? 0.1673 0.2539 0.2043 -0.0016 0.0274  0.0935  161 TYR   A CA  
3534 C CA  B TYR   A 161 ? 0.1912 0.2419 0.1886 0.0193  0.0216  -0.0072 161 TYR   A CA  
3535 C C   A TYR   A 161 ? 0.1670 0.2749 0.2178 -0.0116 0.0193  0.0841  161 TYR   A C   
3536 C C   B TYR   A 161 ? 0.2010 0.2522 0.1846 0.0123  0.0243  -0.0104 161 TYR   A C   
3537 O O   A TYR   A 161 ? 0.1537 0.2794 0.2033 -0.0182 0.0128  0.0836  161 TYR   A O   
3538 O O   B TYR   A 161 ? 0.1968 0.2539 0.1779 0.0070  0.0315  -0.0151 161 TYR   A O   
3539 C CB  A TYR   A 161 ? 0.1782 0.2321 0.2015 -0.0059 0.0361  0.0668  161 TYR   A CB  
3540 C CB  B TYR   A 161 ? 0.1914 0.2291 0.1915 0.0176  0.0265  -0.0126 161 TYR   A CB  
3541 C CG  A TYR   A 161 ? 0.1793 0.2207 0.1987 -0.0068 0.0220  0.0466  161 TYR   A CG  
3542 C CG  B TYR   A 161 ? 0.1968 0.2217 0.1883 0.0119  0.0289  -0.0141 161 TYR   A CG  
3543 C CD1 A TYR   A 161 ? 0.1775 0.2084 0.2052 -0.0080 0.0157  0.0423  161 TYR   A CD1 
3544 C CD1 B TYR   A 161 ? 0.1988 0.2175 0.1846 0.0096  0.0286  -0.0121 161 TYR   A CD1 
3545 C CD2 A TYR   A 161 ? 0.1771 0.2210 0.2012 -0.0054 0.0194  0.0356  161 TYR   A CD2 
3546 C CD2 B TYR   A 161 ? 0.2019 0.2203 0.1903 0.0110  0.0303  -0.0060 161 TYR   A CD2 
3547 C CE1 A TYR   A 161 ? 0.1758 0.1979 0.2038 -0.0091 0.0103  0.0436  161 TYR   A CE1 
3548 C CE1 B TYR   A 161 ? 0.2064 0.2185 0.1923 0.0062  0.0297  -0.0032 161 TYR   A CE1 
3549 C CE2 A TYR   A 161 ? 0.1769 0.2086 0.2000 -0.0084 0.0123  0.0431  161 TYR   A CE2 
3550 C CE2 B TYR   A 161 ? 0.2081 0.2196 0.2004 0.0076  0.0286  0.0027  161 TYR   A CE2 
3551 C CZ  A TYR   A 161 ? 0.1853 0.1993 0.1993 -0.0137 0.0007  0.0437  161 TYR   A CZ  
3552 C CZ  B TYR   A 161 ? 0.2147 0.2216 0.2024 0.0059  0.0330  0.0061  161 TYR   A CZ  
3553 O OH  A TYR   A 161 ? 0.1994 0.2048 0.2010 -0.0241 -0.0049 0.0435  161 TYR   A OH  
3554 O OH  B TYR   A 161 ? 0.2271 0.2240 0.2183 0.0018  0.0291  0.0146  161 TYR   A OH  
3573 N N   A ASP   A 162 ? 0.1642 0.2894 0.2350 -0.0073 0.0257  0.0904  162 ASP   A N   
3574 N N   B ASP   A 162 ? 0.2101 0.2602 0.1928 0.0126  0.0180  -0.0139 162 ASP   A N   
3575 C CA  A ASP   A 162 ? 0.1561 0.3114 0.2376 -0.0118 0.0299  0.0790  162 ASP   A CA  
3576 C CA  B ASP   A 162 ? 0.2169 0.2689 0.2139 0.0143  0.0172  -0.0161 162 ASP   A CA  
3577 C C   A ASP   A 162 ? 0.1479 0.3265 0.2284 -0.0167 0.0353  0.0796  162 ASP   A C   
3578 C C   B ASP   A 162 ? 0.2194 0.2742 0.2170 0.0130  0.0150  -0.0152 162 ASP   A C   
3579 O O   A ASP   A 162 ? 0.1515 0.3239 0.2388 -0.0174 0.0324  0.0636  162 ASP   A O   
3580 O O   B ASP   A 162 ? 0.2189 0.2737 0.2090 0.0124  0.0168  -0.0189 162 ASP   A O   
3581 C CB  A ASP   A 162 ? 0.1622 0.3250 0.2721 -0.0000 0.0302  0.0592  162 ASP   A CB  
3582 C CB  B ASP   A 162 ? 0.2183 0.2742 0.2311 0.0202  0.0205  -0.0187 162 ASP   A CB  
3583 C CG  A ASP   A 162 ? 0.1844 0.3465 0.3068 0.0086  0.0304  0.0262  162 ASP   A CG  
3584 C CG  B ASP   A 162 ? 0.2231 0.2836 0.2555 0.0244  0.0194  -0.0216 162 ASP   A CG  
3585 O OD1 A ASP   A 162 ? 0.1919 0.3504 0.3167 -0.0040 0.0341  0.0168  162 ASP   A OD1 
3586 O OD1 B ASP   A 162 ? 0.2287 0.2900 0.2598 0.0193  0.0154  -0.0270 162 ASP   A OD1 
3587 O OD2 A ASP   A 162 ? 0.2035 0.3596 0.3233 0.0282  0.0301  0.0070  162 ASP   A OD2 
3588 O OD2 B ASP   A 162 ? 0.2251 0.2863 0.2670 0.0291  0.0214  -0.0211 162 ASP   A OD2 
3597 N N   A LYS   A 163 ? 0.1618 0.3494 0.2390 -0.0149 0.0073  0.0831  163 LYS   A N   
3598 N N   B LYS   A 163 ? 0.2263 0.2810 0.2255 0.0148  0.0057  -0.0096 163 LYS   A N   
3599 C CA  A LYS   A 163 ? 0.1731 0.3666 0.2386 -0.0112 0.0010  0.0779  163 LYS   A CA  
3600 C CA  B LYS   A 163 ? 0.2313 0.2876 0.2425 0.0140  0.0003  -0.0039 163 LYS   A CA  
3601 C C   A LYS   A 163 ? 0.1667 0.3549 0.2252 -0.0192 0.0086  0.0792  163 LYS   A C   
3602 C C   B LYS   A 163 ? 0.2208 0.2828 0.2218 0.0091  0.0067  0.0036  163 LYS   A C   
3603 O O   A LYS   A 163 ? 0.1643 0.3722 0.2383 -0.0195 0.0060  0.0650  163 LYS   A O   
3604 O O   B LYS   A 163 ? 0.2199 0.2867 0.2153 0.0078  0.0054  0.0018  163 LYS   A O   
3605 C CB  A LYS   A 163 ? 0.2124 0.3940 0.2889 0.0086  -0.0135 0.0648  163 LYS   A CB  
3606 C CB  B LYS   A 163 ? 0.2485 0.2997 0.2775 0.0203  -0.0101 -0.0103 163 LYS   A CB  
3607 C CG  A LYS   A 163 ? 0.2552 0.4183 0.3584 0.0090  -0.0118 0.0555  163 LYS   A CG  
3608 C CG  B LYS   A 163 ? 0.2639 0.3113 0.3126 0.0217  -0.0139 -0.0146 163 LYS   A CG  
3609 C CD  A LYS   A 163 ? 0.2902 0.4393 0.4229 0.0098  -0.0139 0.0517  163 LYS   A CD  
3610 C CD  B LYS   A 163 ? 0.2774 0.3212 0.3458 0.0229  -0.0122 -0.0179 163 LYS   A CD  
3611 C CE  A LYS   A 163 ? 0.3059 0.4527 0.4768 0.0064  -0.0126 0.0503  163 LYS   A CE  
3612 C CE  B LYS   A 163 ? 0.2863 0.3284 0.3691 0.0236  -0.0073 -0.0197 163 LYS   A CE  
3613 N NZ  A LYS   A 163 ? 0.3177 0.4601 0.5059 0.0039  -0.0160 0.0474  163 LYS   A NZ  
3614 N NZ  B LYS   A 163 ? 0.2897 0.3316 0.3814 0.0240  -0.0050 -0.0206 163 LYS   A NZ  
3641 N N   A LEU   A 164 ? 0.1555 0.3213 0.1968 -0.0338 -0.0018 0.0758  164 LEU   A N   
3642 N N   B LEU   A 164 ? 0.2090 0.2702 0.2203 0.0038  0.0148  0.0082  164 LEU   A N   
3643 C CA  A LEU   A 164 ? 0.1690 0.2956 0.1861 -0.0412 0.0147  0.0701  164 LEU   A CA  
3644 C CA  B LEU   A 164 ? 0.2029 0.2576 0.2140 -0.0010 0.0197  0.0134  164 LEU   A CA  
3645 C C   A LEU   A 164 ? 0.1715 0.2916 0.1968 -0.0394 0.0187  0.0670  164 LEU   A C   
3646 C C   B LEU   A 164 ? 0.2005 0.2547 0.2193 -0.0066 0.0235  0.0190  164 LEU   A C   
3647 O O   A LEU   A 164 ? 0.1806 0.2943 0.2046 -0.0462 0.0368  0.0463  164 LEU   A O   
3648 O O   B LEU   A 164 ? 0.1965 0.2555 0.2188 -0.0109 0.0328  0.0134  164 LEU   A O   
3649 C CB  A LEU   A 164 ? 0.1639 0.2808 0.1877 -0.0457 0.0195  0.0706  164 LEU   A CB  
3650 C CB  B LEU   A 164 ? 0.1983 0.2490 0.2007 0.0018  0.0232  0.0143  164 LEU   A CB  
3651 C CG  A LEU   A 164 ? 0.1653 0.2742 0.1985 -0.0335 0.0152  0.0568  164 LEU   A CG  
3652 C CG  B LEU   A 164 ? 0.1990 0.2420 0.1976 0.0103  0.0231  0.0150  164 LEU   A CG  
3653 C CD1 A LEU   A 164 ? 0.1545 0.2709 0.1997 -0.0221 0.0040  0.0556  164 LEU   A CD1 
3654 C CD1 B LEU   A 164 ? 0.1983 0.2410 0.1961 0.0168  0.0266  0.0071  164 LEU   A CD1 
3655 C CD2 A LEU   A 164 ? 0.1733 0.2736 0.2116 -0.0345 0.0108  0.0402  164 LEU   A CD2 
3656 C CD2 B LEU   A 164 ? 0.1975 0.2385 0.1919 0.0104  0.0212  0.0151  164 LEU   A CD2 
3679 N N   A VAL   A 165 ? 0.1603 0.2855 0.1992 -0.0402 0.0268  0.0746  165 VAL   A N   
3680 N N   B VAL   A 165 ? 0.2005 0.2526 0.2210 -0.0091 0.0147  0.0283  165 VAL   A N   
3681 C CA  A VAL   A 165 ? 0.1638 0.2837 0.1886 -0.0380 0.0324  0.0731  165 VAL   A CA  
3682 C CA  B VAL   A 165 ? 0.2010 0.2540 0.2281 -0.0132 0.0084  0.0317  165 VAL   A CA  
3683 C C   A VAL   A 165 ? 0.1694 0.2929 0.1877 -0.0341 0.0359  0.0750  165 VAL   A C   
3684 C C   B VAL   A 165 ? 0.1988 0.2578 0.2344 -0.0120 0.0051  0.0295  165 VAL   A C   
3685 O O   A VAL   A 165 ? 0.1688 0.2887 0.1804 -0.0310 0.0441  0.0626  165 VAL   A O   
3686 O O   B VAL   A 165 ? 0.2006 0.2572 0.2290 -0.0190 0.0054  0.0276  165 VAL   A O   
3687 C CB  A VAL   A 165 ? 0.1827 0.2722 0.1949 -0.0364 0.0262  0.0656  165 VAL   A CB  
3688 C CB  B VAL   A 165 ? 0.2036 0.2534 0.2304 -0.0150 0.0023  0.0335  165 VAL   A CB  
3689 C CG1 A VAL   A 165 ? 0.1925 0.2746 0.2126 -0.0378 0.0250  0.0515  165 VAL   A CG1 
3690 C CG1 B VAL   A 165 ? 0.2005 0.2489 0.2198 -0.0153 -0.0062 0.0360  165 VAL   A CG1 
3691 C CG2 A VAL   A 165 ? 0.1924 0.2682 0.2086 -0.0275 0.0215  0.0677  165 VAL   A CG2 
3692 C CG2 B VAL   A 165 ? 0.2070 0.2595 0.2369 -0.0172 0.0047  0.0311  165 VAL   A CG2 
3711 N N   A SER   A 166 ? 0.1609 0.3071 0.2220 -0.0325 0.0223  0.0639  166 SER   A N   
3712 N N   B SER   A 166 ? 0.1894 0.2631 0.2429 -0.0065 0.0071  0.0305  166 SER   A N   
3713 C CA  A SER   A 166 ? 0.1626 0.3238 0.2611 -0.0351 0.0267  0.0531  166 SER   A CA  
3714 C CA  B SER   A 166 ? 0.1801 0.2692 0.2385 -0.0025 0.0037  0.0325  166 SER   A CA  
3715 C C   A SER   A 166 ? 0.1561 0.3401 0.2791 -0.0256 0.0186  0.0408  166 SER   A C   
3716 C C   B SER   A 166 ? 0.1779 0.2852 0.2410 0.0030  -0.0026 0.0331  166 SER   A C   
3717 O O   A SER   A 166 ? 0.1706 0.3504 0.3350 -0.0249 0.0252  0.0159  166 SER   A O   
3718 O O   B SER   A 166 ? 0.1739 0.2875 0.2532 0.0036  -0.0012 0.0292  166 SER   A O   
3719 C CB  A SER   A 166 ? 0.1746 0.3319 0.2886 -0.0275 0.0264  0.0434  166 SER   A CB  
3720 C CB  B SER   A 166 ? 0.1737 0.2627 0.2368 -0.0006 -0.0000 0.0310  166 SER   A CB  
3721 O OG  A SER   A 166 ? 0.1914 0.3401 0.3104 -0.0280 0.0263  0.0484  166 SER   A OG  
3722 O OG  B SER   A 166 ? 0.1681 0.2579 0.2417 -0.0029 -0.0049 0.0356  166 SER   A OG  
3733 N N   A SER   A 167 ? 0.1663 0.3476 0.2432 -0.0031 0.0073  0.0453  167 SER   A N   
3734 N N   B SER   A 167 ? 0.1862 0.3024 0.2378 0.0103  -0.0052 0.0375  167 SER   A N   
3735 C CA  A SER   A 167 ? 0.1900 0.3553 0.2394 0.0053  -0.0037 0.0312  167 SER   A CA  
3736 C CA  B SER   A 167 ? 0.1968 0.3199 0.2454 0.0158  -0.0047 0.0349  167 SER   A CA  
3737 C C   A SER   A 167 ? 0.1969 0.3555 0.2344 0.0161  0.0158  0.0302  167 SER   A C   
3738 C C   B SER   A 167 ? 0.2006 0.3331 0.2361 0.0209  0.0063  0.0354  167 SER   A C   
3739 O O   A SER   A 167 ? 0.2098 0.3619 0.2606 0.0203  0.0061  0.0346  167 SER   A O   
3740 O O   B SER   A 167 ? 0.2084 0.3305 0.2449 0.0226  -0.0017 0.0423  167 SER   A O   
3741 C CB  A SER   A 167 ? 0.1993 0.3612 0.2417 0.0037  -0.0016 0.0386  167 SER   A CB  
3742 C CB  B SER   A 167 ? 0.2054 0.3256 0.2664 0.0167  -0.0086 0.0380  167 SER   A CB  
3743 O OG  A SER   A 167 ? 0.1996 0.3656 0.2166 0.0040  0.0227  0.0546  167 SER   A OG  
3744 O OG  B SER   A 167 ? 0.2103 0.3294 0.2810 0.0184  -0.0107 0.0421  167 SER   A OG  
3755 N N   . PHE   A 168 ? 0.1988 0.3501 0.2225 0.0283  0.0117  0.0301  168 PHE   A N   
3756 C CA  . PHE   A 168 ? 0.2088 0.3615 0.2465 0.0157  0.0117  0.0238  168 PHE   A CA  
3757 C C   . PHE   A 168 ? 0.2519 0.3958 0.3221 -0.0082 0.0347  0.0119  168 PHE   A C   
3758 O O   . PHE   A 168 ? 0.2453 0.3944 0.3580 -0.0231 0.0467  0.0310  168 PHE   A O   
3759 C CB  . PHE   A 168 ? 0.1925 0.3436 0.2187 0.0064  -0.0060 0.0287  168 PHE   A CB  
3760 C CG  . PHE   A 168 ? 0.1899 0.3279 0.2059 -0.0069 -0.0124 0.0350  168 PHE   A CG  
3761 C CD1 . PHE   A 168 ? 0.1891 0.3271 0.2155 -0.0158 -0.0100 0.0457  168 PHE   A CD1 
3762 C CD2 . PHE   A 168 ? 0.1935 0.3170 0.2054 -0.0127 0.0016  0.0295  168 PHE   A CD2 
3763 C CE1 . PHE   A 168 ? 0.1806 0.3196 0.2127 -0.0225 -0.0048 0.0524  168 PHE   A CE1 
3764 C CE2 . PHE   A 168 ? 0.1960 0.3089 0.2160 -0.0165 0.0045  0.0434  168 PHE   A CE2 
3765 C CZ  . PHE   A 168 ? 0.1861 0.3073 0.2203 -0.0236 0.0037  0.0466  168 PHE   A CZ  
3776 N N   A LEU   A 169 ? 0.2958 0.4187 0.3723 -0.0203 0.0232  -0.0146 169 LEU   A N   
3777 N N   B LEU   A 169 ? 0.2940 0.4132 0.3727 -0.0112 0.0201  0.0016  169 LEU   A N   
3778 C CA  A LEU   A 169 ? 0.3574 0.4477 0.4451 -0.0189 -0.0012 -0.0279 169 LEU   A CA  
3779 C CA  B LEU   A 169 ? 0.3360 0.4312 0.4220 -0.0099 0.0041  -0.0037 169 LEU   A CA  
3780 C C   A LEU   A 169 ? 0.3766 0.4509 0.4782 -0.0183 -0.0078 -0.0218 169 LEU   A C   
3781 C C   B LEU   A 169 ? 0.3459 0.4339 0.4366 -0.0103 -0.0014 0.0001  169 LEU   A C   
3782 O O   A LEU   A 169 ? 0.3899 0.4500 0.4889 -0.0186 -0.0065 -0.0222 169 LEU   A O   
3783 O O   B LEU   A 169 ? 0.3449 0.4331 0.4432 -0.0112 -0.0025 0.0015  169 LEU   A O   
3784 C CB  A LEU   A 169 ? 0.3961 0.4666 0.4754 -0.0190 -0.0155 -0.0447 169 LEU   A CB  
3785 C CB  B LEU   A 169 ? 0.3614 0.4424 0.4501 -0.0093 -0.0033 -0.0110 169 LEU   A CB  
3786 C CG  A LEU   A 169 ? 0.4289 0.4793 0.4945 -0.0198 -0.0231 -0.0594 169 LEU   A CG  
3787 C CG  B LEU   A 169 ? 0.3799 0.4499 0.4673 -0.0092 -0.0076 -0.0181 169 LEU   A CG  
3788 C CD1 A LEU   A 169 ? 0.4441 0.4828 0.5082 -0.0179 -0.0244 -0.0619 169 LEU   A CD1 
3789 C CD1 B LEU   A 169 ? 0.3876 0.4512 0.4774 -0.0081 -0.0086 -0.0199 169 LEU   A CD1 
3790 C CD2 A LEU   A 169 ? 0.4392 0.4836 0.4990 -0.0209 -0.0226 -0.0637 169 LEU   A CD2 
3791 C CD2 B LEU   A 169 ? 0.3838 0.4528 0.4741 -0.0096 -0.0078 -0.0205 169 LEU   A CD2 
3792 O OXT A LEU   A 169 ? 0.3713 0.4526 0.4904 -0.0184 -0.0058 -0.0183 169 LEU   A OXT 
3793 O OXT B LEU   A 169 ? 0.3494 0.4360 0.4419 -0.0107 -0.0007 0.0014  169 LEU   A OXT 
3816 N N   A SER   B 1   ? 0.3798 0.3849 0.3983 -0.1251 -0.0808 0.0437  1   SER   B N   
3817 N N   B SER   B 1   ? 0.3521 0.3537 0.3693 -0.0643 -0.0450 0.0200  1   SER   B N   
3818 C CA  A SER   B 1   ? 0.3666 0.3863 0.3884 -0.1297 -0.0903 0.0428  1   SER   B CA  
3819 C CA  B SER   B 1   ? 0.3472 0.3546 0.3628 -0.0650 -0.0462 0.0203  1   SER   B CA  
3820 C C   A SER   B 1   ? 0.3362 0.3852 0.3701 -0.1319 -0.0958 0.0612  1   SER   B C   
3821 C C   B SER   B 1   ? 0.3367 0.3543 0.3554 -0.0625 -0.0495 0.0296  1   SER   B C   
3822 O O   A SER   B 1   ? 0.3463 0.3860 0.3542 -0.1231 -0.0844 0.0590  1   SER   B O   
3823 O O   B SER   B 1   ? 0.3396 0.3543 0.3491 -0.0619 -0.0503 0.0274  1   SER   B O   
3824 C CB  A SER   B 1   ? 0.3800 0.3855 0.4125 -0.1257 -0.0813 0.0269  1   SER   B CB  
3825 C CB  B SER   B 1   ? 0.3510 0.3542 0.3750 -0.0663 -0.0408 0.0107  1   SER   B CB  
3826 O OG  A SER   B 1   ? 0.3943 0.3925 0.4449 -0.1200 -0.0624 0.0217  1   SER   B OG  
3827 O OG  B SER   B 1   ? 0.3540 0.3559 0.3835 -0.0677 -0.0366 0.0048  1   SER   B OG  
3842 N N   A MET   B 2   ? 0.3097 0.3788 0.3660 -0.1352 -0.0924 0.1024  2   MET   B N   
3843 N N   B MET   B 2   ? 0.3261 0.3529 0.3534 -0.0595 -0.0476 0.0469  2   MET   B N   
3844 C CA  A MET   B 2   ? 0.2962 0.3738 0.3840 -0.1101 -0.0947 0.1258  2   MET   B CA  
3845 C CA  B MET   B 2   ? 0.3146 0.3490 0.3511 -0.0513 -0.0458 0.0615  2   MET   B CA  
3846 C C   A MET   B 2   ? 0.2622 0.3449 0.3538 -0.0861 -0.1037 0.1528  2   MET   B C   
3847 C C   B MET   B 2   ? 0.2947 0.3296 0.3240 -0.0482 -0.0403 0.0673  2   MET   B C   
3848 O O   A MET   B 2   ? 0.2619 0.3553 0.3572 -0.0687 -0.1189 0.1571  2   MET   B O   
3849 O O   B MET   B 2   ? 0.2967 0.3341 0.3286 -0.0460 -0.0342 0.0668  2   MET   B O   
3850 C CB  A MET   B 2   ? 0.3297 0.4079 0.4688 -0.0869 -0.0826 0.1010  2   MET   B CB  
3851 C CB  B MET   B 2   ? 0.3247 0.3647 0.3829 -0.0419 -0.0499 0.0670  2   MET   B CB  
3852 C CG  A MET   B 2   ? 0.3561 0.4405 0.5518 -0.0651 -0.0704 0.0910  2   MET   B CG  
3853 C CG  B MET   B 2   ? 0.3307 0.3760 0.4079 -0.0334 -0.0548 0.0780  2   MET   B CG  
3854 S SD  A MET   B 2   ? 0.3825 0.4667 0.6243 -0.0471 -0.0579 0.0789  2   MET   B SD  
3855 S SD  B MET   B 2   ? 0.3371 0.3857 0.4295 -0.0257 -0.0611 0.0890  2   MET   B SD  
3856 C CE  A MET   B 2   ? 0.3821 0.4730 0.6270 -0.0464 -0.0469 0.0770  2   MET   B CE  
3857 C CE  B MET   B 2   ? 0.3363 0.3860 0.4383 -0.0259 -0.0561 0.0815  2   MET   B CE  
3876 N N   A VAL   B 3   ? 0.2338 0.2981 0.3206 -0.0915 -0.0864 0.1637  3   VAL   B N   
3877 N N   B VAL   B 3   ? 0.2732 0.3037 0.2949 -0.0490 -0.0399 0.0717  3   VAL   B N   
3878 C CA  A VAL   B 3   ? 0.2300 0.2641 0.3183 -0.0776 -0.0793 0.1335  3   VAL   B CA  
3879 C CA  B VAL   B 3   ? 0.2554 0.2789 0.2744 -0.0459 -0.0422 0.0706  3   VAL   B CA  
3880 C C   A VAL   B 3   ? 0.2151 0.2496 0.2665 -0.0638 -0.0711 0.1127  3   VAL   B C   
3881 C C   B VAL   B 3   ? 0.2319 0.2561 0.2467 -0.0470 -0.0459 0.0780  3   VAL   B C   
3882 O O   A VAL   B 3   ? 0.2098 0.2570 0.2786 -0.0610 -0.0743 0.1204  3   VAL   B O   
3883 O O   B VAL   B 3   ? 0.2311 0.2627 0.2400 -0.0382 -0.0434 0.0797  3   VAL   B O   
3884 C CB  A VAL   B 3   ? 0.2472 0.2537 0.3761 -0.0780 -0.0769 0.1237  3   VAL   B CB  
3885 C CB  B VAL   B 3   ? 0.2616 0.2778 0.2858 -0.0450 -0.0398 0.0647  3   VAL   B CB  
3886 C CG1 A VAL   B 3   ? 0.2540 0.2471 0.3985 -0.0753 -0.0808 0.1152  3   VAL   B CG1 
3887 C CG1 B VAL   B 3   ? 0.2641 0.2759 0.2911 -0.0456 -0.0403 0.0595  3   VAL   B CG1 
3888 C CG2 A VAL   B 3   ? 0.2541 0.2582 0.3953 -0.0748 -0.0690 0.1330  3   VAL   B CG2 
3889 C CG2 B VAL   B 3   ? 0.2648 0.2786 0.2896 -0.0439 -0.0384 0.0667  3   VAL   B CG2 
3908 N N   . ASN   B 4   ? 0.2094 0.2269 0.2342 -0.0567 -0.0545 0.0886  4   ASN   B N   
3909 C CA  . ASN   B 4   ? 0.2119 0.2197 0.2022 -0.0526 -0.0459 0.0482  4   ASN   B CA  
3910 C C   . ASN   B 4   ? 0.2242 0.2266 0.2039 -0.0507 -0.0348 0.0238  4   ASN   B C   
3911 O O   . ASN   B 4   ? 0.2246 0.2293 0.2288 -0.0523 -0.0348 0.0074  4   ASN   B O   
3912 C CB  . ASN   B 4   ? 0.2077 0.2132 0.1926 -0.0469 -0.0560 0.0437  4   ASN   B CB  
3913 C CG  . ASN   B 4   ? 0.2017 0.1999 0.1733 -0.0430 -0.0542 0.0374  4   ASN   B CG  
3914 O OD1 . ASN   B 4   ? 0.2018 0.1901 0.1846 -0.0456 -0.0557 0.0333  4   ASN   B OD1 
3915 N ND2 . ASN   B 4   ? 0.2188 0.2041 0.1799 -0.0215 -0.0374 0.0333  4   ASN   B ND2 
3923 N N   . SER   B 5   ? 0.2337 0.2407 0.1922 -0.0518 -0.0062 0.0225  5   SER   B N   
3924 C CA  . SER   B 5   ? 0.2637 0.2804 0.2296 -0.0386 0.0167  0.0272  5   SER   B CA  
3925 C C   . SER   B 5   ? 0.2781 0.2878 0.2690 -0.0549 0.0409  0.0366  5   SER   B C   
3926 O O   . SER   B 5   ? 0.2869 0.2874 0.3543 -0.0446 0.0701  0.0322  5   SER   B O   
3927 C CB  . SER   B 5   ? 0.2716 0.3071 0.2545 -0.0322 0.0197  0.0404  5   SER   B CB  
3928 O OG  . SER   B 5   ? 0.3025 0.3471 0.3201 -0.0165 0.0216  0.0436  5   SER   B OG  
3934 N N   . PHE   B 6   ? 0.2921 0.3106 0.2536 -0.0642 0.0448  0.0393  6   PHE   B N   
3935 C CA  . PHE   B 6   ? 0.2989 0.3121 0.2064 -0.0860 0.0441  0.0225  6   PHE   B CA  
3936 C C   . PHE   B 6   ? 0.3437 0.3420 0.2550 -0.0849 0.0655  -0.0072 6   PHE   B C   
3937 O O   . PHE   B 6   ? 0.3608 0.3765 0.2913 -0.0749 0.0449  -0.0343 6   PHE   B O   
3938 C CB  . PHE   B 6   ? 0.2686 0.2910 0.1798 -0.0836 0.0145  0.0180  6   PHE   B CB  
3939 C CG  . PHE   B 6   ? 0.2322 0.2586 0.1732 -0.0718 -0.0016 0.0142  6   PHE   B CG  
3940 C CD1 . PHE   B 6   ? 0.2276 0.2352 0.1663 -0.0632 -0.0236 0.0107  6   PHE   B CD1 
3941 C CD2 . PHE   B 6   ? 0.2081 0.2547 0.1831 -0.0568 0.0081  0.0387  6   PHE   B CD2 
3942 C CE1 . PHE   B 6   ? 0.2204 0.2161 0.1693 -0.0497 -0.0192 0.0053  6   PHE   B CE1 
3943 C CE2 . PHE   B 6   ? 0.2128 0.2441 0.2142 -0.0378 0.0171  0.0311  6   PHE   B CE2 
3944 C CZ  . PHE   B 6   ? 0.2146 0.2215 0.1919 -0.0413 0.0025  0.0085  6   PHE   B CZ  
3954 N N   . SER   B 7   ? 0.3765 0.3279 0.2610 -0.1053 0.0929  -0.0349 7   SER   B N   
3955 C CA  . SER   B 7   ? 0.4130 0.3322 0.3138 -0.1050 0.1174  -0.0399 7   SER   B CA  
3956 C C   . SER   B 7   ? 0.4092 0.3138 0.3012 -0.1075 0.1307  -0.0504 7   SER   B C   
3957 O O   . SER   B 7   ? 0.4197 0.3169 0.3341 -0.1109 0.1368  -0.0389 7   SER   B O   
3958 C CB  . SER   B 7   ? 0.4407 0.3356 0.3785 -0.1019 0.1306  -0.0343 7   SER   B CB  
3959 O OG  . SER   B 7   ? 0.4611 0.3847 0.4413 -0.1003 0.1323  -0.0202 7   SER   B OG  
3965 N N   A GLY   B 8   ? 0.4081 0.3022 0.3061 -0.0935 0.1289  -0.0664 8   GLY   B N   
3966 N N   B GLY   B 8   ? 0.4021 0.3006 0.3019 -0.0991 0.1271  -0.0570 8   GLY   B N   
3967 C CA  A GLY   B 8   ? 0.3985 0.2872 0.3139 -0.0882 0.1325  -0.0732 8   GLY   B CA  
3968 C CA  B GLY   B 8   ? 0.3934 0.2860 0.3008 -0.0939 0.1230  -0.0598 8   GLY   B CA  
3969 C C   A GLY   B 8   ? 0.3869 0.2703 0.3049 -0.0864 0.1404  -0.0606 8   GLY   B C   
3970 C C   B GLY   B 8   ? 0.3838 0.2707 0.2950 -0.0894 0.1235  -0.0581 8   GLY   B C   
3971 O O   A GLY   B 8   ? 0.3970 0.2782 0.3364 -0.0789 0.1407  -0.0600 8   GLY   B O   
3972 O O   B GLY   B 8   ? 0.3875 0.2753 0.3052 -0.0866 0.1210  -0.0558 8   GLY   B O   
3979 N N   . TYR   B 9   ? 0.3730 0.2514 0.2766 -0.0828 0.1196  -0.0641 9   TYR   B N   
3980 C CA  . TYR   B 9   ? 0.3447 0.2205 0.2378 -0.0610 0.0921  -0.0498 9   TYR   B CA  
3981 C C   . TYR   B 9   ? 0.3350 0.2193 0.2175 -0.0541 0.0492  -0.0395 9   TYR   B C   
3982 O O   . TYR   B 9   ? 0.3481 0.2424 0.2592 -0.0584 0.0394  -0.0187 9   TYR   B O   
3983 C CB  . TYR   B 9   ? 0.3330 0.1935 0.2501 -0.0565 0.0830  -0.0442 9   TYR   B CB  
3984 C CG  . TYR   B 9   ? 0.3192 0.1778 0.2470 -0.0615 0.0742  -0.0470 9   TYR   B CG  
3985 C CD1 . TYR   B 9   ? 0.3208 0.1832 0.2666 -0.0771 0.0753  -0.0452 9   TYR   B CD1 
3986 C CD2 . TYR   B 9   ? 0.3035 0.1705 0.2295 -0.0491 0.0716  -0.0534 9   TYR   B CD2 
3987 C CE1 . TYR   B 9   ? 0.3152 0.1965 0.2689 -0.0793 0.0858  -0.0587 9   TYR   B CE1 
3988 C CE2 . TYR   B 9   ? 0.3057 0.1692 0.2463 -0.0499 0.0702  -0.0468 9   TYR   B CE2 
3989 C CZ  . TYR   B 9   ? 0.3102 0.1910 0.2636 -0.0654 0.0787  -0.0632 9   TYR   B CZ  
3990 O OH  . TYR   B 9   ? 0.3074 0.2009 0.2857 -0.0773 0.0707  -0.0780 9   TYR   B OH  
4001 N N   . LEU   B 10  ? 0.3128 0.2007 0.1935 -0.0523 0.0284  -0.0364 10  LEU   B N   
4002 C CA  . LEU   B 10  ? 0.3062 0.1984 0.1938 -0.0644 -0.0045 -0.0408 10  LEU   B CA  
4003 C C   . LEU   B 10  ? 0.2849 0.1995 0.2040 -0.0627 -0.0225 -0.0346 10  LEU   B C   
4004 O O   . LEU   B 10  ? 0.2703 0.1996 0.2048 -0.0481 -0.0161 -0.0226 10  LEU   B O   
4005 C CB  . LEU   B 10  ? 0.3201 0.2010 0.2202 -0.0702 -0.0255 -0.0112 10  LEU   B CB  
4006 C CG  . LEU   B 10  ? 0.3381 0.2138 0.2543 -0.0596 -0.0587 0.0032  10  LEU   B CG  
4007 C CD1 . LEU   B 10  ? 0.3489 0.2296 0.2887 -0.0559 -0.0618 0.0007  10  LEU   B CD1 
4008 C CD2 . LEU   B 10  ? 0.3456 0.2159 0.2843 -0.0570 -0.0482 0.0130  10  LEU   B CD2 
4020 N N   . LYS   B 11  ? 0.2966 0.2302 0.2110 -0.0542 -0.0314 -0.0324 11  LYS   B N   
4021 C CA  . LYS   B 11  ? 0.3062 0.2546 0.2265 -0.0414 -0.0520 -0.0388 11  LYS   B CA  
4022 C C   . LYS   B 11  ? 0.2861 0.2378 0.2393 -0.0579 -0.0500 -0.0504 11  LYS   B C   
4023 O O   . LYS   B 11  ? 0.3025 0.2620 0.2875 -0.0684 -0.0490 -0.0791 11  LYS   B O   
4024 C CB  . LYS   B 11  ? 0.3351 0.3038 0.2936 -0.0142 -0.0522 -0.0259 11  LYS   B CB  
4025 C CG  . LYS   B 11  ? 0.3645 0.3357 0.3718 0.0025  -0.0566 -0.0197 11  LYS   B CG  
4026 C CD  . LYS   B 11  ? 0.3912 0.3622 0.4373 0.0128  -0.0594 -0.0245 11  LYS   B CD  
4027 C CE  . LYS   B 11  ? 0.4084 0.3813 0.4847 0.0164  -0.0544 -0.0252 11  LYS   B CE  
4028 N NZ  . LYS   B 11  ? 0.4202 0.3947 0.5134 0.0188  -0.0490 -0.0204 11  LYS   B NZ  
4042 N N   . LEU   B 12  ? 0.2511 0.2109 0.2410 -0.0523 -0.0430 -0.0388 12  LEU   B N   
4043 C CA  . LEU   B 12  ? 0.2350 0.1904 0.2602 -0.0494 -0.0391 -0.0335 12  LEU   B CA  
4044 C C   . LEU   B 12  ? 0.2258 0.1938 0.2677 -0.0471 -0.0507 -0.0313 12  LEU   B C   
4045 O O   . LEU   B 12  ? 0.2274 0.1895 0.2914 -0.0539 -0.0581 -0.0214 12  LEU   B O   
4046 C CB  . LEU   B 12  ? 0.2364 0.1689 0.2605 -0.0415 -0.0278 -0.0410 12  LEU   B CB  
4047 C CG  . LEU   B 12  ? 0.2354 0.1755 0.2570 -0.0394 -0.0203 -0.0314 12  LEU   B CG  
4048 C CD1 . LEU   B 12  ? 0.2447 0.1705 0.2435 -0.0233 -0.0116 -0.0169 12  LEU   B CD1 
4049 C CD2 . LEU   B 12  ? 0.2447 0.1826 0.2751 -0.0374 -0.0152 -0.0410 12  LEU   B CD2 
4061 N N   . THR   B 13  ? 0.2116 0.1959 0.2810 -0.0436 -0.0444 -0.0449 13  THR   B N   
4062 C CA  . THR   B 13  ? 0.2167 0.1998 0.2675 -0.0546 -0.0580 -0.0316 13  THR   B CA  
4063 C C   . THR   B 13  ? 0.2571 0.2157 0.2778 -0.0594 -0.0701 -0.0212 13  THR   B C   
4064 O O   . THR   B 13  ? 0.2778 0.2129 0.2977 -0.0552 -0.0289 -0.0216 13  THR   B O   
4065 C CB  . THR   B 13  ? 0.2085 0.2097 0.2752 -0.0530 -0.0515 -0.0162 13  THR   B CB  
4066 O OG1 . THR   B 13  ? 0.1992 0.2055 0.2738 -0.0448 -0.0419 -0.0216 13  THR   B OG1 
4067 C CG2 . THR   B 13  ? 0.2228 0.2147 0.2692 -0.0475 -0.0459 0.0007  13  THR   B CG2 
4075 N N   A ASP   B 14  ? 0.2724 0.2303 0.2879 -0.0656 -0.1095 -0.0089 14  ASP   B N   
4076 N N   B ASP   B 14  ? 0.2679 0.2273 0.2920 -0.0586 -0.0751 -0.0140 14  ASP   B N   
4077 C CA  A ASP   B 14  ? 0.2859 0.2551 0.3117 -0.0644 -0.1156 0.0166  14  ASP   B CA  
4078 C CA  B ASP   B 14  ? 0.2726 0.2386 0.3058 -0.0560 -0.0769 -0.0026 14  ASP   B CA  
4079 C C   A ASP   B 14  ? 0.2715 0.2362 0.2641 -0.0719 -0.1002 0.0148  14  ASP   B C   
4080 C C   B ASP   B 14  ? 0.2561 0.2241 0.2681 -0.0560 -0.0835 0.0007  14  ASP   B C   
4081 O O   A ASP   B 14  ? 0.3079 0.2571 0.2798 -0.0723 -0.0906 0.0281  14  ASP   B O   
4082 O O   B ASP   B 14  ? 0.2645 0.2254 0.2690 -0.0524 -0.0862 -0.0000 14  ASP   B O   
4083 C CB  A ASP   B 14  ? 0.3107 0.2942 0.3903 -0.0573 -0.1272 0.0187  14  ASP   B CB  
4084 C CB  B ASP   B 14  ? 0.2919 0.2606 0.3552 -0.0512 -0.0710 -0.0019 14  ASP   B CB  
4085 C CG  A ASP   B 14  ? 0.3437 0.3291 0.4733 -0.0455 -0.1185 0.0059  14  ASP   B CG  
4086 C CG  B ASP   B 14  ? 0.3112 0.2797 0.3978 -0.0440 -0.0622 -0.0076 14  ASP   B CG  
4087 O OD1 A ASP   B 14  ? 0.3667 0.3485 0.4966 -0.0476 -0.1130 -0.0125 14  ASP   B OD1 
4088 O OD1 B ASP   B 14  ? 0.3160 0.2880 0.4126 -0.0419 -0.0559 -0.0139 14  ASP   B OD1 
4089 O OD2 A ASP   B 14  ? 0.3499 0.3523 0.5168 -0.0428 -0.1178 0.0124  14  ASP   B OD2 
4090 O OD2 B ASP   B 14  ? 0.3192 0.2863 0.4162 -0.0450 -0.0632 -0.0066 14  ASP   B OD2 
4099 N N   . ASN   B 15  ? 0.2383 0.2065 0.2351 -0.0518 -0.0831 0.0065  15  ASN   B N   
4100 C CA  . ASN   B 15  ? 0.1960 0.1769 0.2222 -0.0369 -0.0579 -0.0023 15  ASN   B CA  
4101 C C   . ASN   B 15  ? 0.1831 0.1605 0.2094 -0.0251 -0.0446 -0.0031 15  ASN   B C   
4102 O O   . ASN   B 15  ? 0.1851 0.1565 0.2353 -0.0247 -0.0496 -0.0133 15  ASN   B O   
4103 C CB  . ASN   B 15  ? 0.1861 0.1743 0.2491 -0.0160 -0.0501 0.0023  15  ASN   B CB  
4104 C CG  . ASN   B 15  ? 0.1745 0.1743 0.2469 -0.0231 -0.0268 -0.0038 15  ASN   B CG  
4105 O OD1 . ASN   B 15  ? 0.1880 0.2053 0.2734 -0.0464 -0.0326 0.0034  15  ASN   B OD1 
4106 N ND2 . ASN   B 15  ? 0.1745 0.1565 0.2333 -0.0113 -0.0048 -0.0193 15  ASN   B ND2 
4114 N N   . VAL   B 16  ? 0.1813 0.1546 0.2103 -0.0323 -0.0505 -0.0030 16  VAL   B N   
4115 C CA  . VAL   B 16  ? 0.1821 0.1651 0.1890 -0.0216 -0.0353 -0.0187 16  VAL   B CA  
4116 C C   . VAL   B 16  ? 0.1796 0.1763 0.1918 -0.0317 -0.0407 -0.0131 16  VAL   B C   
4117 O O   . VAL   B 16  ? 0.1800 0.1887 0.2146 -0.0261 -0.0331 -0.0246 16  VAL   B O   
4118 C CB  . VAL   B 16  ? 0.1870 0.1676 0.1999 -0.0131 -0.0207 -0.0152 16  VAL   B CB  
4119 C CG1 . VAL   B 16  ? 0.1916 0.1525 0.1948 -0.0027 -0.0163 -0.0115 16  VAL   B CG1 
4120 C CG2 . VAL   B 16  ? 0.1925 0.1694 0.2246 -0.0070 -0.0152 -0.0109 16  VAL   B CG2 
4130 N N   . TYR   B 17  ? 0.1864 0.1786 0.1960 -0.0301 -0.0332 -0.0190 17  TYR   B N   
4131 C CA  . TYR   B 17  ? 0.1969 0.1876 0.1911 -0.0396 -0.0334 -0.0067 17  TYR   B CA  
4132 C C   . TYR   B 17  ? 0.1913 0.1705 0.1815 -0.0333 -0.0221 -0.0126 17  TYR   B C   
4133 O O   . TYR   B 17  ? 0.1930 0.1711 0.2034 -0.0270 -0.0320 -0.0300 17  TYR   B O   
4134 C CB  . TYR   B 17  ? 0.2260 0.2288 0.2075 -0.0249 -0.0285 0.0393  17  TYR   B CB  
4135 C CG  . TYR   B 17  ? 0.2564 0.2740 0.2504 -0.0152 -0.0399 0.0412  17  TYR   B CG  
4136 C CD1 . TYR   B 17  ? 0.2736 0.2855 0.2662 -0.0097 -0.0505 0.0543  17  TYR   B CD1 
4137 C CD2 . TYR   B 17  ? 0.2837 0.3093 0.2719 -0.0055 -0.0440 0.0369  17  TYR   B CD2 
4138 C CE1 . TYR   B 17  ? 0.2969 0.3159 0.2909 0.0017  -0.0596 0.0449  17  TYR   B CE1 
4139 C CE2 . TYR   B 17  ? 0.3007 0.3303 0.2887 0.0085  -0.0631 0.0442  17  TYR   B CE2 
4140 C CZ  . TYR   B 17  ? 0.3113 0.3368 0.2944 0.0129  -0.0732 0.0444  17  TYR   B CZ  
4141 O OH  . TYR   B 17  ? 0.3258 0.3628 0.3153 0.0208  -0.0897 0.0462  17  TYR   B OH  
4151 N N   . ILE   B 18  ? 0.1991 0.1685 0.1790 -0.0321 -0.0101 -0.0159 18  ILE   B N   
4152 C CA  . ILE   B 18  ? 0.2071 0.1596 0.1714 -0.0363 -0.0103 -0.0211 18  ILE   B CA  
4153 C C   . ILE   B 18  ? 0.2199 0.1634 0.1780 -0.0395 -0.0060 -0.0321 18  ILE   B C   
4154 O O   . ILE   B 18  ? 0.2383 0.1744 0.1915 -0.0378 0.0075  -0.0340 18  ILE   B O   
4155 C CB  . ILE   B 18  ? 0.2061 0.1614 0.1906 -0.0441 -0.0143 -0.0178 18  ILE   B CB  
4156 C CG1 . ILE   B 18  ? 0.2072 0.1695 0.2011 -0.0431 -0.0125 -0.0035 18  ILE   B CG1 
4157 C CG2 . ILE   B 18  ? 0.2090 0.1665 0.1997 -0.0391 -0.0208 -0.0158 18  ILE   B CG2 
4158 C CD1 . ILE   B 18  ? 0.2120 0.1996 0.2292 -0.0428 -0.0257 0.0138  18  ILE   B CD1 
4170 N N   . LYS   B 19  ? 0.2175 0.1603 0.2030 -0.0234 0.0249  -0.0375 19  LYS   B N   
4171 C CA  . LYS   B 19  ? 0.2219 0.1658 0.2063 -0.0270 0.0285  -0.0325 19  LYS   B CA  
4172 C C   . LYS   B 19  ? 0.2065 0.1667 0.2186 -0.0205 0.0328  -0.0443 19  LYS   B C   
4173 O O   . LYS   B 19  ? 0.1956 0.1667 0.2151 -0.0109 0.0208  -0.0394 19  LYS   B O   
4174 C CB  . LYS   B 19  ? 0.2415 0.1879 0.2155 -0.0287 0.0375  -0.0170 19  LYS   B CB  
4175 C CG  . LYS   B 19  ? 0.2660 0.2112 0.2499 -0.0371 0.0491  -0.0195 19  LYS   B CG  
4176 C CD  . LYS   B 19  ? 0.2925 0.2365 0.2732 -0.0470 0.0539  -0.0152 19  LYS   B CD  
4177 C CE  . LYS   B 19  ? 0.3191 0.2637 0.2898 -0.0522 0.0455  -0.0193 19  LYS   B CE  
4178 N NZ  . LYS   B 19  ? 0.3443 0.2833 0.3002 -0.0574 0.0503  -0.0206 19  LYS   B NZ  
4192 N N   . ASN   B 20  ? 0.2107 0.1771 0.2510 -0.0196 0.0364  -0.0583 20  ASN   B N   
4193 C CA  . ASN   B 20  ? 0.2044 0.1897 0.2789 -0.0125 0.0419  -0.0720 20  ASN   B CA  
4194 C C   . ASN   B 20  ? 0.2018 0.2132 0.2759 -0.0183 0.0505  -0.0811 20  ASN   B C   
4195 O O   . ASN   B 20  ? 0.2183 0.2514 0.3074 -0.0321 0.0532  -0.0760 20  ASN   B O   
4196 C CB  . ASN   B 20  ? 0.2306 0.1944 0.3044 0.0055  0.0262  -0.0715 20  ASN   B CB  
4197 C CG  . ASN   B 20  ? 0.2563 0.2042 0.3218 0.0356  0.0216  -0.0877 20  ASN   B CG  
4198 O OD1 . ASN   B 20  ? 0.2875 0.2362 0.3581 0.0559  0.0236  -0.0908 20  ASN   B OD1 
4199 N ND2 . ASN   B 20  ? 0.2509 0.2022 0.3090 0.0315  0.0036  -0.0856 20  ASN   B ND2 
4206 N N   . ALA   B 21  ? 0.2050 0.1933 0.2736 -0.0271 0.0475  -0.0703 21  ALA   B N   
4207 C CA  . ALA   B 21  ? 0.2168 0.2047 0.3042 -0.0346 0.0385  -0.0463 21  ALA   B CA  
4208 C C   . ALA   B 21  ? 0.2178 0.1777 0.2867 -0.0250 0.0467  -0.0350 21  ALA   B C   
4209 O O   . ALA   B 21  ? 0.2165 0.1730 0.2774 -0.0368 0.0427  -0.0340 21  ALA   B O   
4210 C CB  . ALA   B 21  ? 0.2328 0.2344 0.3120 -0.0471 0.0325  -0.0326 21  ALA   B CB  
4216 N N   . ASP   B 22  ? 0.2080 0.1627 0.2788 -0.0232 0.0394  -0.0238 22  ASP   B N   
4217 C CA  . ASP   B 22  ? 0.2053 0.1575 0.2588 -0.0082 0.0289  -0.0198 22  ASP   B CA  
4218 C C   . ASP   B 22  ? 0.1936 0.1538 0.2233 -0.0169 0.0132  -0.0070 22  ASP   B C   
4219 O O   . ASP   B 22  ? 0.1890 0.1662 0.2295 -0.0088 0.0124  -0.0049 22  ASP   B O   
4220 C CB  . ASP   B 22  ? 0.2155 0.1640 0.3027 0.0019  0.0333  -0.0065 22  ASP   B CB  
4221 C CG  . ASP   B 22  ? 0.2207 0.1866 0.3476 0.0064  0.0012  -0.0044 22  ASP   B CG  
4222 O OD1 . ASP   B 22  ? 0.2241 0.1827 0.3410 0.0095  -0.0244 0.0007  22  ASP   B OD1 
4223 O OD2 . ASP   B 22  ? 0.2332 0.2124 0.3981 0.0137  -0.0212 -0.0192 22  ASP   B OD2 
4228 N N   . ILE   B 23  ? 0.1922 0.1571 0.1915 -0.0119 0.0029  0.0205  23  ILE   B N   
4229 C CA  . ILE   B 23  ? 0.1832 0.1585 0.1714 -0.0091 0.0012  0.0040  23  ILE   B CA  
4230 C C   . ILE   B 23  ? 0.1740 0.1648 0.1699 -0.0073 -0.0098 0.0058  23  ILE   B C   
4231 O O   . ILE   B 23  ? 0.1664 0.1656 0.1691 -0.0053 -0.0056 0.0135  23  ILE   B O   
4232 C CB  . ILE   B 23  ? 0.1774 0.1649 0.1941 -0.0171 0.0035  0.0147  23  ILE   B CB  
4233 C CG1 . ILE   B 23  ? 0.1861 0.1715 0.2112 -0.0084 0.0151  0.0276  23  ILE   B CG1 
4234 C CG2 . ILE   B 23  ? 0.1901 0.1901 0.2051 -0.0141 0.0082  0.0089  23  ILE   B CG2 
4235 C CD1 . ILE   B 23  ? 0.1959 0.1730 0.2267 -0.0045 0.0191  0.0184  23  ILE   B CD1 
4247 N N   . VAL   B 24  ? 0.1778 0.1610 0.1820 -0.0065 -0.0085 -0.0010 24  VAL   B N   
4248 C CA  . VAL   B 24  ? 0.1673 0.1684 0.2131 -0.0119 -0.0152 -0.0012 24  VAL   B CA  
4249 C C   . VAL   B 24  ? 0.1640 0.1721 0.2317 -0.0162 -0.0031 0.0017  24  VAL   B C   
4250 O O   . VAL   B 24  ? 0.1577 0.1818 0.2352 -0.0176 -0.0016 0.0159  24  VAL   B O   
4251 C CB  . VAL   B 24  ? 0.1793 0.1821 0.2235 0.0033  -0.0231 0.0037  24  VAL   B CB  
4252 C CG1 . VAL   B 24  ? 0.1834 0.1825 0.2620 -0.0038 -0.0204 0.0025  24  VAL   B CG1 
4253 C CG2 . VAL   B 24  ? 0.1912 0.2160 0.2243 0.0076  -0.0235 -0.0106 24  VAL   B CG2 
4263 N N   . GLU   B 25  ? 0.1920 0.1774 0.2285 -0.0159 0.0067  0.0003  25  GLU   B N   
4264 C CA  . GLU   B 25  ? 0.2027 0.2018 0.2449 -0.0008 0.0135  -0.0049 25  GLU   B CA  
4265 C C   . GLU   B 25  ? 0.1979 0.1920 0.2116 -0.0090 0.0124  0.0040  25  GLU   B C   
4266 O O   . GLU   B 25  ? 0.2039 0.2056 0.2338 -0.0031 0.0247  0.0091  25  GLU   B O   
4267 C CB  . GLU   B 25  ? 0.2307 0.2495 0.3098 0.0175  0.0233  -0.0027 25  GLU   B CB  
4268 C CG  . GLU   B 25  ? 0.2697 0.3029 0.4127 0.0246  0.0164  -0.0107 25  GLU   B CG  
4269 C CD  . GLU   B 25  ? 0.3290 0.3555 0.4927 0.0173  0.0103  -0.0123 25  GLU   B CD  
4270 O OE1 . GLU   B 25  ? 0.3332 0.3886 0.5302 0.0220  0.0179  -0.0103 25  GLU   B OE1 
4271 O OE2 . GLU   B 25  ? 0.3340 0.3842 0.5317 0.0157  0.0044  -0.0204 25  GLU   B OE2 
4278 N N   . GLU   B 26  ? 0.1936 0.1849 0.1881 -0.0267 0.0087  0.0114  26  GLU   B N   
4279 C CA  . GLU   B 26  ? 0.2028 0.1901 0.2018 -0.0358 -0.0073 0.0114  26  GLU   B CA  
4280 C C   . GLU   B 26  ? 0.1789 0.1856 0.1858 -0.0265 0.0062  0.0163  26  GLU   B C   
4281 O O   . GLU   B 26  ? 0.1962 0.2118 0.1844 -0.0214 0.0005  0.0301  26  GLU   B O   
4282 C CB  . GLU   B 26  ? 0.2384 0.2109 0.2339 -0.0483 0.0057  0.0236  26  GLU   B CB  
4283 C CG  . GLU   B 26  ? 0.2783 0.2561 0.2837 -0.0533 0.0143  0.0013  26  GLU   B CG  
4284 C CD  . GLU   B 26  ? 0.3043 0.2818 0.2999 -0.0755 0.0305  -0.0356 26  GLU   B CD  
4285 O OE1 . GLU   B 26  ? 0.3269 0.2649 0.2995 -0.0903 0.0734  -0.0324 26  GLU   B OE1 
4286 O OE2 . GLU   B 26  ? 0.3016 0.3275 0.3368 -0.0706 0.0227  -0.0320 26  GLU   B OE2 
4293 N N   . ALA   B 27  ? 0.1598 0.1777 0.1909 -0.0225 0.0088  0.0139  27  ALA   B N   
4294 C CA  . ALA   B 27  ? 0.1706 0.1687 0.2009 -0.0171 -0.0027 0.0233  27  ALA   B CA  
4295 C C   . ALA   B 27  ? 0.1790 0.1777 0.2224 -0.0087 0.0126  0.0383  27  ALA   B C   
4296 O O   . ALA   B 27  ? 0.1829 0.1861 0.2428 -0.0014 0.0172  0.0490  27  ALA   B O   
4297 C CB  . ALA   B 27  ? 0.1907 0.1600 0.2099 -0.0169 -0.0024 0.0196  27  ALA   B CB  
4303 N N   . LYS   B 28  ? 0.1775 0.1943 0.2693 -0.0110 0.0220  0.0631  28  LYS   B N   
4304 C CA  . LYS   B 28  ? 0.1913 0.2336 0.2939 -0.0016 0.0560  0.0953  28  LYS   B CA  
4305 C C   . LYS   B 28  ? 0.2151 0.2574 0.2782 0.0019  0.0674  0.0850  28  LYS   B C   
4306 O O   . LYS   B 28  ? 0.2334 0.2709 0.2933 0.0010  0.0723  0.0822  28  LYS   B O   
4307 C CB  . LYS   B 28  ? 0.2106 0.2679 0.3473 0.0116  0.0744  0.1111  28  LYS   B CB  
4308 C CG  . LYS   B 28  ? 0.2337 0.3252 0.3934 0.0223  0.0737  0.1187  28  LYS   B CG  
4309 C CD  . LYS   B 28  ? 0.2546 0.3709 0.4536 0.0274  0.0855  0.1129  28  LYS   B CD  
4310 C CE  . LYS   B 28  ? 0.2905 0.4041 0.4878 0.0407  0.0891  0.1131  28  LYS   B CE  
4311 N NZ  . LYS   B 28  ? 0.3457 0.4639 0.5165 0.0561  0.0894  0.1197  28  LYS   B NZ  
4325 N N   . LYS   B 29  ? 0.2339 0.2758 0.2768 0.0240  0.0640  0.0688  29  LYS   B N   
4326 C CA  . LYS   B 29  ? 0.2740 0.3080 0.3063 0.0306  0.0582  0.0672  29  LYS   B CA  
4327 C C   . LYS   B 29  ? 0.2646 0.3138 0.2761 0.0319  0.0441  0.0782  29  LYS   B C   
4328 O O   . LYS   B 29  ? 0.2795 0.3404 0.2896 0.0379  0.0442  0.0798  29  LYS   B O   
4329 C CB  . LYS   B 29  ? 0.3237 0.3408 0.3868 0.0309  0.0555  0.0563  29  LYS   B CB  
4330 C CG  . LYS   B 29  ? 0.3697 0.3704 0.4633 0.0286  0.0572  0.0518  29  LYS   B CG  
4331 C CD  . LYS   B 29  ? 0.4042 0.3906 0.5302 0.0248  0.0666  0.0423  29  LYS   B CD  
4332 C CE  . LYS   B 29  ? 0.4134 0.4035 0.5784 0.0223  0.0775  0.0353  29  LYS   B CE  
4333 N NZ  . LYS   B 29  ? 0.4340 0.4121 0.5994 0.0221  0.0800  0.0337  29  LYS   B NZ  
4347 N N   . VAL   B 30  ? 0.2363 0.2931 0.2530 0.0179  0.0349  0.0825  30  VAL   B N   
4348 C CA  . VAL   B 30  ? 0.2187 0.2807 0.2849 0.0036  0.0075  0.0832  30  VAL   B CA  
4349 C C   . VAL   B 30  ? 0.1978 0.2778 0.2705 -0.0017 0.0114  0.1038  30  VAL   B C   
4350 O O   . VAL   B 30  ? 0.2156 0.2920 0.2744 0.0042  0.0166  0.1243  30  VAL   B O   
4351 C CB  . VAL   B 30  ? 0.2240 0.2731 0.3365 -0.0121 -0.0206 0.0706  30  VAL   B CB  
4352 C CG1 . VAL   B 30  ? 0.2252 0.2860 0.3343 -0.0153 -0.0225 0.0604  30  VAL   B CG1 
4353 C CG2 . VAL   B 30  ? 0.2363 0.2637 0.3614 -0.0202 -0.0278 0.0549  30  VAL   B CG2 
4363 N N   . LYS   B 31  ? 0.1878 0.2422 0.3031 -0.0191 0.0051  0.1066  31  LYS   B N   
4364 C CA  . LYS   B 31  ? 0.1785 0.2372 0.3431 -0.0328 -0.0038 0.1100  31  LYS   B CA  
4365 C C   . LYS   B 31  ? 0.1712 0.1984 0.2998 -0.0308 -0.0255 0.0911  31  LYS   B C   
4366 O O   . LYS   B 31  ? 0.1765 0.2191 0.3196 -0.0233 -0.0173 0.1027  31  LYS   B O   
4367 C CB  . LYS   B 31  ? 0.1944 0.2845 0.4060 -0.0240 0.0162  0.1241  31  LYS   B CB  
4368 C CG  . LYS   B 31  ? 0.2298 0.3288 0.4532 -0.0282 0.0379  0.1227  31  LYS   B CG  
4369 C CD  . LYS   B 31  ? 0.2467 0.3649 0.4928 -0.0186 0.0271  0.1092  31  LYS   B CD  
4370 C CE  . LYS   B 31  ? 0.2778 0.3875 0.5274 -0.0110 0.0090  0.0950  31  LYS   B CE  
4371 N NZ  . LYS   B 31  ? 0.3074 0.4131 0.5463 0.0013  -0.0090 0.0774  31  LYS   B NZ  
4385 N N   . PRO   B 32  ? 0.1753 0.1685 0.2365 -0.0287 -0.0421 0.0504  32  PRO   B N   
4386 C CA  . PRO   B 32  ? 0.1916 0.1628 0.1846 -0.0358 -0.0395 0.0336  32  PRO   B CA  
4387 C C   . PRO   B 32  ? 0.2061 0.1498 0.1971 -0.0390 -0.0557 0.0328  32  PRO   B C   
4388 O O   . PRO   B 32  ? 0.2232 0.1524 0.2365 -0.0428 -0.0752 0.0354  32  PRO   B O   
4389 C CB  . PRO   B 32  ? 0.2073 0.1629 0.1838 -0.0393 -0.0307 0.0164  32  PRO   B CB  
4390 C CG  . PRO   B 32  ? 0.2259 0.1487 0.1872 -0.0274 -0.0525 0.0202  32  PRO   B CG  
4391 C CD  . PRO   B 32  ? 0.2110 0.1582 0.2101 -0.0234 -0.0625 0.0276  32  PRO   B CD  
4399 N N   . THR   B 33  ? 0.2090 0.1460 0.1829 -0.0270 -0.0509 0.0224  33  THR   B N   
4400 C CA  . THR   B 33  ? 0.2130 0.1559 0.1817 -0.0338 -0.0481 0.0307  33  THR   B CA  
4401 C C   . THR   B 33  ? 0.2120 0.1497 0.1620 -0.0300 -0.0487 0.0231  33  THR   B C   
4402 O O   . THR   B 33  ? 0.2349 0.1542 0.1806 -0.0442 -0.0552 0.0231  33  THR   B O   
4403 C CB  . THR   B 33  ? 0.2212 0.1617 0.1906 -0.0235 -0.0592 0.0365  33  THR   B CB  
4404 O OG1 . THR   B 33  ? 0.2102 0.1721 0.1967 -0.0245 -0.0560 0.0441  33  THR   B OG1 
4405 C CG2 . THR   B 33  ? 0.2441 0.1641 0.2047 -0.0127 -0.0570 0.0290  33  THR   B CG2 
4413 N N   . VAL   B 34  ? 0.1907 0.1439 0.1530 -0.0318 -0.0440 0.0161  34  VAL   B N   
4414 C CA  . VAL   B 34  ? 0.1756 0.1424 0.1533 -0.0239 -0.0440 0.0110  34  VAL   B CA  
4415 C C   . VAL   B 34  ? 0.1650 0.1354 0.1447 -0.0251 -0.0244 0.0031  34  VAL   B C   
4416 O O   . VAL   B 34  ? 0.1793 0.1420 0.1397 -0.0204 -0.0312 0.0088  34  VAL   B O   
4417 C CB  . VAL   B 34  ? 0.1850 0.1479 0.1838 -0.0023 -0.0321 0.0080  34  VAL   B CB  
4418 C CG1 . VAL   B 34  ? 0.1850 0.1658 0.1919 -0.0003 -0.0165 -0.0111 34  VAL   B CG1 
4419 C CG2 . VAL   B 34  ? 0.1887 0.1561 0.2131 -0.0051 -0.0315 0.0001  34  VAL   B CG2 
4429 N N   . VAL   B 35  ? 0.1650 0.1301 0.1308 -0.0296 -0.0163 0.0053  35  VAL   B N   
4430 C CA  . VAL   B 35  ? 0.1596 0.1356 0.1312 -0.0227 -0.0129 0.0054  35  VAL   B CA  
4431 C C   . VAL   B 35  ? 0.1451 0.1334 0.1347 -0.0208 -0.0186 0.0095  35  VAL   B C   
4432 O O   . VAL   B 35  ? 0.1528 0.1380 0.1367 -0.0224 -0.0052 -0.0065 35  VAL   B O   
4433 C CB  . VAL   B 35  ? 0.1551 0.1592 0.1411 -0.0167 -0.0030 0.0101  35  VAL   B CB  
4434 C CG1 . VAL   B 35  ? 0.1470 0.1760 0.1619 -0.0242 -0.0047 0.0045  35  VAL   B CG1 
4435 C CG2 . VAL   B 35  ? 0.1506 0.1565 0.1705 -0.0085 -0.0049 0.0048  35  VAL   B CG2 
4445 N N   . VAL   B 36  ? 0.1407 0.1347 0.1375 -0.0153 -0.0187 0.0117  36  VAL   B N   
4446 C CA  . VAL   B 36  ? 0.1471 0.1275 0.1295 -0.0124 -0.0130 0.0049  36  VAL   B CA  
4447 C C   . VAL   B 36  ? 0.1428 0.1286 0.1278 -0.0113 -0.0072 -0.0007 36  VAL   B C   
4448 O O   . VAL   B 36  ? 0.1461 0.1426 0.1465 -0.0089 -0.0031 -0.0060 36  VAL   B O   
4449 C CB  . VAL   B 36  ? 0.1422 0.1350 0.1433 -0.0176 -0.0117 0.0028  36  VAL   B CB  
4450 C CG1 . VAL   B 36  ? 0.1419 0.1497 0.1528 -0.0187 -0.0131 0.0063  36  VAL   B CG1 
4451 C CG2 . VAL   B 36  ? 0.1496 0.1419 0.1478 -0.0147 -0.0208 0.0087  36  VAL   B CG2 
4461 N N   . ASN   B 37  ? 0.1438 0.1325 0.1248 -0.0029 -0.0064 0.0070  37  ASN   B N   
4462 C CA  . ASN   B 37  ? 0.1496 0.1285 0.1459 -0.0006 -0.0129 0.0084  37  ASN   B CA  
4463 C C   . ASN   B 37  ? 0.1494 0.1328 0.1415 0.0027  -0.0039 0.0081  37  ASN   B C   
4464 O O   . ASN   B 37  ? 0.1545 0.1407 0.1398 -0.0003 0.0005  0.0067  37  ASN   B O   
4465 C CB  . ASN   B 37  ? 0.1457 0.1423 0.1357 -0.0028 -0.0203 0.0066  37  ASN   B CB  
4466 C CG  . ASN   B 37  ? 0.1455 0.1453 0.1393 -0.0015 -0.0132 -0.0029 37  ASN   B CG  
4467 O OD1 . ASN   B 37  ? 0.1557 0.1519 0.1440 0.0050  -0.0149 0.0014  37  ASN   B OD1 
4468 N ND2 . ASN   B 37  ? 0.1499 0.1333 0.1447 0.0042  -0.0149 0.0073  37  ASN   B ND2 
4475 N N   . ALA   B 38  ? 0.1537 0.1349 0.1443 0.0065  0.0057  0.0037  38  ALA   B N   
4476 C CA  . ALA   B 38  ? 0.1627 0.1370 0.1419 0.0003  0.0023  0.0056  38  ALA   B CA  
4477 C C   . ALA   B 38  ? 0.1570 0.1411 0.1519 0.0019  0.0011  0.0068  38  ALA   B C   
4478 O O   . ALA   B 38  ? 0.1697 0.1503 0.1497 0.0045  -0.0043 0.0102  38  ALA   B O   
4479 C CB  . ALA   B 38  ? 0.1846 0.1518 0.1578 -0.0095 0.0130  0.0096  38  ALA   B CB  
4485 N N   . ALA   B 39  ? 0.1550 0.1466 0.1371 0.0080  -0.0071 0.0054  39  ALA   B N   
4486 C CA  . ALA   B 39  ? 0.1595 0.1484 0.1280 0.0081  -0.0058 0.0007  39  ALA   B CA  
4487 C C   . ALA   B 39  ? 0.1685 0.1517 0.1194 0.0087  0.0014  -0.0051 39  ALA   B C   
4488 O O   . ALA   B 39  ? 0.1681 0.1663 0.1476 -0.0010 -0.0041 0.0058  39  ALA   B O   
4489 C CB  . ALA   B 39  ? 0.1691 0.1530 0.1527 -0.0010 -0.0033 -0.0056 39  ALA   B CB  
4495 N N   . ASN   B 40  ? 0.1696 0.1774 0.1211 -0.0028 0.0000  -0.0117 40  ASN   B N   
4496 C CA  . ASN   B 40  ? 0.1787 0.1841 0.1343 -0.0026 -0.0071 -0.0184 40  ASN   B CA  
4497 C C   . ASN   B 40  ? 0.1758 0.1850 0.1269 0.0010  -0.0162 -0.0092 40  ASN   B C   
4498 O O   . ASN   B 40  ? 0.1796 0.1737 0.1328 0.0053  -0.0112 -0.0024 40  ASN   B O   
4499 C CB  . ASN   B 40  ? 0.1907 0.1828 0.1615 0.0098  -0.0104 0.0061  40  ASN   B CB  
4500 C CG  . ASN   B 40  ? 0.2020 0.1808 0.1894 0.0077  -0.0268 0.0133  40  ASN   B CG  
4501 O OD1 . ASN   B 40  ? 0.2023 0.1722 0.2776 0.0027  -0.0380 0.0175  40  ASN   B OD1 
4502 N ND2 . ASN   B 40  ? 0.2011 0.1879 0.1940 0.0003  -0.0223 0.0148  40  ASN   B ND2 
4509 N N   . VAL   B 41  ? 0.1856 0.1870 0.1290 0.0122  -0.0008 -0.0110 41  VAL   B N   
4510 C CA  . VAL   B 41  ? 0.1948 0.2037 0.1409 0.0115  -0.0031 -0.0166 41  VAL   B CA  
4511 C C   . VAL   B 41  ? 0.1955 0.2011 0.1325 0.0204  -0.0131 -0.0164 41  VAL   B C   
4512 O O   . VAL   B 41  ? 0.1968 0.2004 0.1573 0.0142  -0.0183 -0.0161 41  VAL   B O   
4513 C CB  . VAL   B 41  ? 0.2092 0.2204 0.1722 0.0031  0.0112  -0.0304 41  VAL   B CB  
4514 C CG1 . VAL   B 41  ? 0.2098 0.2275 0.1830 -0.0039 0.0236  -0.0261 41  VAL   B CG1 
4515 C CG2 . VAL   B 41  ? 0.2193 0.2383 0.1844 -0.0090 0.0115  -0.0330 41  VAL   B CG2 
4525 N N   . TYR   B 42  ? 0.2026 0.1992 0.1500 0.0146  -0.0230 -0.0022 42  TYR   B N   
4526 C CA  . TYR   B 42  ? 0.2057 0.2031 0.1575 0.0141  -0.0325 -0.0175 42  TYR   B CA  
4527 C C   . TYR   B 42  ? 0.1883 0.1823 0.1679 0.0191  -0.0340 -0.0210 42  TYR   B C   
4528 O O   . TYR   B 42  ? 0.1937 0.1872 0.2116 0.0192  -0.0419 -0.0242 42  TYR   B O   
4529 C CB  . TYR   B 42  ? 0.2299 0.2286 0.1799 0.0123  -0.0446 -0.0062 42  TYR   B CB  
4530 C CG  . TYR   B 42  ? 0.2353 0.2474 0.1737 0.0087  -0.0386 0.0101  42  TYR   B CG  
4531 C CD1 . TYR   B 42  ? 0.2307 0.2497 0.1521 0.0090  -0.0278 -0.0089 42  TYR   B CD1 
4532 C CD2 . TYR   B 42  ? 0.2521 0.2657 0.2293 0.0126  -0.0172 0.0214  42  TYR   B CD2 
4533 C CE1 . TYR   B 42  ? 0.2427 0.2681 0.1567 0.0136  -0.0137 -0.0075 42  TYR   B CE1 
4534 C CE2 . TYR   B 42  ? 0.2606 0.2744 0.2197 0.0190  0.0064  0.0297  42  TYR   B CE2 
4535 C CZ  . TYR   B 42  ? 0.2679 0.2858 0.2003 0.0319  0.0128  0.0131  42  TYR   B CZ  
4536 O OH  . TYR   B 42  ? 0.3045 0.3234 0.2508 0.0499  0.0275  0.0285  42  TYR   B OH  
4546 N N   . LEU   B 43  ? 0.1749 0.1641 0.1549 0.0073  -0.0177 -0.0067 43  LEU   B N   
4547 C CA  . LEU   B 43  ? 0.1752 0.1675 0.1422 0.0044  -0.0148 -0.0003 43  LEU   B CA  
4548 C C   . LEU   B 43  ? 0.1839 0.1626 0.1513 -0.0011 -0.0211 -0.0053 43  LEU   B C   
4549 O O   . LEU   B 43  ? 0.1768 0.1658 0.1854 0.0043  -0.0231 -0.0025 43  LEU   B O   
4550 C CB  . LEU   B 43  ? 0.1742 0.1671 0.1579 0.0009  -0.0273 -0.0151 43  LEU   B CB  
4551 C CG  . LEU   B 43  ? 0.1770 0.1584 0.1569 -0.0022 -0.0326 -0.0130 43  LEU   B CG  
4552 C CD1 . LEU   B 43  ? 0.1874 0.1700 0.2031 -0.0032 -0.0362 -0.0124 43  LEU   B CD1 
4553 C CD2 . LEU   B 43  ? 0.1783 0.1626 0.1786 -0.0047 -0.0347 -0.0041 43  LEU   B CD2 
4565 N N   . LYS   B 44  ? 0.1786 0.1613 0.1644 0.0042  -0.0111 -0.0089 44  LYS   B N   
4566 C CA  . LYS   B 44  ? 0.1878 0.1761 0.1552 0.0036  -0.0162 0.0052  44  LYS   B CA  
4567 C C   . LYS   B 44  ? 0.1773 0.1774 0.1580 0.0056  -0.0177 0.0025  44  LYS   B C   
4568 O O   . LYS   B 44  ? 0.1899 0.1782 0.1929 -0.0034 -0.0128 0.0040  44  LYS   B O   
4569 C CB  . LYS   B 44  ? 0.2174 0.1965 0.1713 0.0113  -0.0340 0.0012  44  LYS   B CB  
4570 C CG  . LYS   B 44  ? 0.2562 0.2242 0.2058 0.0113  -0.0659 0.0059  44  LYS   B CG  
4571 C CD  . LYS   B 44  ? 0.2978 0.2525 0.2723 -0.0069 -0.0761 0.0057  44  LYS   B CD  
4572 C CE  . LYS   B 44  ? 0.3275 0.2797 0.3286 -0.0159 -0.0696 0.0132  44  LYS   B CE  
4573 N NZ  . LYS   B 44  ? 0.3409 0.2913 0.3561 -0.0118 -0.0738 0.0220  44  LYS   B NZ  
4587 N N   . HIS   B 45  ? 0.1728 0.1802 0.1498 0.0027  -0.0167 0.0116  45  HIS   B N   
4588 C CA  . HIS   B 45  ? 0.1814 0.1669 0.1565 0.0038  -0.0135 0.0018  45  HIS   B CA  
4589 C C   . HIS   B 45  ? 0.2057 0.1880 0.1854 0.0119  -0.0254 -0.0045 45  HIS   B C   
4590 O O   . HIS   B 45  ? 0.2134 0.2140 0.2388 0.0419  0.0114  0.0004  45  HIS   B O   
4591 C CB  . HIS   B 45  ? 0.1788 0.1653 0.1619 0.0017  -0.0080 0.0008  45  HIS   B CB  
4592 C CG  . HIS   B 45  ? 0.1712 0.1644 0.1477 -0.0073 -0.0147 0.0064  45  HIS   B CG  
4593 N ND1 . HIS   B 45  ? 0.1802 0.1688 0.1596 0.0021  -0.0214 -0.0057 45  HIS   B ND1 
4594 C CD2 . HIS   B 45  ? 0.1817 0.1712 0.1760 -0.0120 -0.0266 0.0051  45  HIS   B CD2 
4595 C CE1 . HIS   B 45  ? 0.1851 0.1567 0.1657 0.0022  -0.0361 -0.0074 45  HIS   B CE1 
4596 N NE2 . HIS   B 45  ? 0.1889 0.1634 0.1723 -0.0032 -0.0264 -0.0056 45  HIS   B NE2 
4604 N N   A GLY   B 46  ? 0.2232 0.1825 0.2141 0.0191  -0.0549 -0.0008 46  GLY   B N   
4605 N N   B GLY   B 46  ? 0.2180 0.1958 0.2097 0.0154  -0.0364 0.0012  46  GLY   B N   
4606 C CA  A GLY   B 46  ? 0.2326 0.1910 0.2524 0.0118  -0.0693 0.0017  46  GLY   B CA  
4607 C CA  B GLY   B 46  ? 0.2261 0.2067 0.2328 0.0127  -0.0422 0.0067  46  GLY   B CA  
4608 C C   A GLY   B 46  ? 0.2309 0.2076 0.3047 0.0159  -0.0590 0.0034  46  GLY   B C   
4609 C C   B GLY   B 46  ? 0.2286 0.2173 0.2612 0.0108  -0.0419 0.0096  46  GLY   B C   
4610 O O   A GLY   B 46  ? 0.2418 0.2274 0.4002 0.0176  -0.0277 -0.0250 46  GLY   B O   
4611 O O   B GLY   B 46  ? 0.2319 0.2277 0.2746 0.0146  -0.0400 0.0191  46  GLY   B O   
4618 N N   . GLY   B 47  ? 0.2292 0.2210 0.2794 0.0029  -0.0347 -0.0045 47  GLY   B N   
4619 C CA  . GLY   B 47  ? 0.2136 0.1949 0.2276 0.0003  -0.0214 0.0004  47  GLY   B CA  
4620 C C   . GLY   B 47  ? 0.1862 0.1802 0.1921 0.0007  -0.0048 -0.0000 47  GLY   B C   
4621 O O   . GLY   B 47  ? 0.1923 0.1637 0.2035 -0.0003 -0.0131 0.0101  47  GLY   B O   
4626 N N   . GLY   B 48  ? 0.1697 0.1733 0.1927 0.0060  -0.0119 0.0234  48  GLY   B N   
4627 C CA  . GLY   B 48  ? 0.1712 0.1662 0.1839 0.0009  -0.0033 0.0155  48  GLY   B CA  
4628 C C   . GLY   B 48  ? 0.1640 0.1556 0.1661 0.0004  0.0080  0.0081  48  GLY   B C   
4629 O O   . GLY   B 48  ? 0.1576 0.1592 0.1973 0.0061  -0.0025 0.0060  48  GLY   B O   
4633 N N   . VAL   B 49  ? 0.1712 0.1620 0.1643 0.0142  0.0008  0.0088  49  VAL   B N   
4634 C CA  . VAL   B 49  ? 0.1694 0.1730 0.1467 0.0119  -0.0107 -0.0065 49  VAL   B CA  
4635 C C   . VAL   B 49  ? 0.1627 0.1564 0.1323 0.0124  -0.0122 0.0048  49  VAL   B C   
4636 O O   . VAL   B 49  ? 0.1711 0.1596 0.1631 0.0069  0.0017  0.0043  49  VAL   B O   
4637 C CB  . VAL   B 49  ? 0.1688 0.1871 0.1865 0.0020  -0.0263 -0.0040 49  VAL   B CB  
4638 C CG1 . VAL   B 49  ? 0.1678 0.1929 0.1914 0.0072  -0.0337 0.0024  49  VAL   B CG1 
4639 C CG2 . VAL   B 49  ? 0.1839 0.2055 0.2143 -0.0076 -0.0482 -0.0073 49  VAL   B CG2 
4649 N N   . ALA   B 50  ? 0.1546 0.1506 0.1501 0.0011  -0.0084 0.0085  50  ALA   B N   
4650 C CA  . ALA   B 50  ? 0.1543 0.1491 0.1502 0.0086  -0.0073 0.0052  50  ALA   B CA  
4651 C C   . ALA   B 50  ? 0.1555 0.1548 0.1498 0.0022  -0.0025 0.0104  50  ALA   B C   
4652 O O   . ALA   B 50  ? 0.1589 0.1602 0.1494 0.0045  -0.0006 0.0097  50  ALA   B O   
4653 C CB  . ALA   B 50  ? 0.1648 0.1468 0.1688 -0.0021 -0.0012 0.0096  50  ALA   B CB  
4659 N N   . GLY   B 51  ? 0.1553 0.1684 0.1612 0.0108  -0.0089 0.0123  51  GLY   B N   
4660 C CA  . GLY   B 51  ? 0.1623 0.1687 0.1790 0.0180  -0.0155 0.0086  51  GLY   B CA  
4661 C C   . GLY   B 51  ? 0.1624 0.1616 0.1800 0.0202  -0.0093 0.0103  51  GLY   B C   
4662 O O   . GLY   B 51  ? 0.1599 0.1799 0.2013 0.0094  -0.0091 0.0019  51  GLY   B O   
4666 N N   . ALA   B 52  ? 0.1577 0.1609 0.1707 0.0199  -0.0042 0.0126  52  ALA   B N   
4667 C CA  . ALA   B 52  ? 0.1665 0.1678 0.1777 0.0204  0.0040  -0.0020 52  ALA   B CA  
4668 C C   . ALA   B 52  ? 0.1578 0.1639 0.1599 0.0130  0.0042  -0.0013 52  ALA   B C   
4669 O O   . ALA   B 52  ? 0.1658 0.1680 0.1802 0.0101  0.0058  0.0047  52  ALA   B O   
4670 C CB  . ALA   B 52  ? 0.1833 0.1687 0.1861 0.0117  0.0056  0.0000  52  ALA   B CB  
4676 N N   . LEU   B 53  ? 0.1486 0.1641 0.1539 0.0174  0.0029  0.0103  53  LEU   B N   
4677 C CA  . LEU   B 53  ? 0.1551 0.1713 0.1517 0.0147  -0.0059 0.0068  53  LEU   B CA  
4678 C C   . LEU   B 53  ? 0.1609 0.1605 0.1524 0.0108  0.0016  0.0083  53  LEU   B C   
4679 O O   . LEU   B 53  ? 0.1653 0.1702 0.1660 -0.0008 0.0037  0.0207  53  LEU   B O   
4680 C CB  . LEU   B 53  ? 0.1581 0.1726 0.1701 0.0082  -0.0051 0.0181  53  LEU   B CB  
4681 C CG  . LEU   B 53  ? 0.1517 0.1834 0.1756 0.0007  -0.0038 0.0326  53  LEU   B CG  
4682 C CD1 . LEU   B 53  ? 0.1563 0.2084 0.2032 0.0186  -0.0030 0.0217  53  LEU   B CD1 
4683 C CD2 . LEU   B 53  ? 0.1659 0.2163 0.2112 -0.0148 -0.0161 0.0003  53  LEU   B CD2 
4695 N N   . ASN   B 54  ? 0.1585 0.1505 0.1543 0.0048  -0.0019 0.0035  54  ASN   B N   
4696 C CA  . ASN   B 54  ? 0.1660 0.1634 0.1707 0.0060  -0.0086 -0.0119 54  ASN   B CA  
4697 C C   . ASN   B 54  ? 0.1563 0.1672 0.1934 0.0073  0.0002  0.0035  54  ASN   B C   
4698 O O   . ASN   B 54  ? 0.1575 0.1721 0.2007 -0.0026 0.0033  0.0084  54  ASN   B O   
4699 C CB  . ASN   B 54  ? 0.1736 0.1785 0.1821 0.0048  -0.0035 -0.0024 54  ASN   B CB  
4700 C CG  . ASN   B 54  ? 0.1725 0.1867 0.1674 0.0033  -0.0098 -0.0050 54  ASN   B CG  
4701 O OD1 . ASN   B 54  ? 0.1605 0.1864 0.1855 -0.0008 -0.0191 -0.0136 54  ASN   B OD1 
4702 N ND2 . ASN   B 54  ? 0.1815 0.1982 0.2092 -0.0032 -0.0309 0.0098  54  ASN   B ND2 
4709 N N   . LYS   B 55  ? 0.1503 0.1772 0.2067 0.0092  0.0050  -0.0001 55  LYS   B N   
4710 C CA  . LYS   B 55  ? 0.1683 0.1882 0.2294 0.0146  0.0007  0.0037  55  LYS   B CA  
4711 C C   . LYS   B 55  ? 0.1555 0.1837 0.2201 0.0087  0.0035  -0.0005 55  LYS   B C   
4712 O O   . LYS   B 55  ? 0.1510 0.1969 0.2347 0.0115  0.0025  -0.0069 55  LYS   B O   
4713 C CB  . LYS   B 55  ? 0.1754 0.1961 0.2573 0.0263  0.0106  0.0193  55  LYS   B CB  
4714 C CG  . LYS   B 55  ? 0.2184 0.2285 0.3483 0.0270  0.0186  0.0367  55  LYS   B CG  
4715 C CD  . LYS   B 55  ? 0.2589 0.2542 0.4213 0.0402  0.0347  0.0446  55  LYS   B CD  
4716 C CE  . LYS   B 55  ? 0.2881 0.2749 0.4749 0.0502  0.0535  0.0493  55  LYS   B CE  
4717 N NZ  . LYS   B 55  ? 0.3013 0.2920 0.5031 0.0520  0.0376  0.0658  55  LYS   B NZ  
4731 N N   . ALA   B 56  ? 0.1539 0.1914 0.1975 0.0075  -0.0017 -0.0044 56  ALA   B N   
4732 C CA  . ALA   B 56  ? 0.1689 0.2061 0.1991 0.0015  -0.0005 0.0035  56  ALA   B CA  
4733 C C   . ALA   B 56  ? 0.1641 0.2003 0.1883 -0.0007 0.0110  0.0076  56  ALA   B C   
4734 O O   . ALA   B 56  ? 0.1778 0.2155 0.2208 -0.0001 0.0359  0.0125  56  ALA   B O   
4735 C CB  . ALA   B 56  ? 0.1806 0.2276 0.2039 -0.0116 -0.0014 0.0038  56  ALA   B CB  
4741 N N   . THR   B 57  ? 0.1699 0.1876 0.1936 -0.0052 0.0170  0.0042  57  THR   B N   
4742 C CA  . THR   B 57  ? 0.1779 0.1861 0.1933 -0.0023 0.0201  0.0158  57  THR   B CA  
4743 C C   . THR   B 57  ? 0.1761 0.1921 0.2118 -0.0035 0.0114  0.0124  57  THR   B C   
4744 O O   . THR   B 57  ? 0.1790 0.1993 0.2206 -0.0213 0.0091  0.0074  57  THR   B O   
4745 C CB  . THR   B 57  ? 0.1822 0.1713 0.1678 -0.0061 0.0155  0.0244  57  THR   B CB  
4746 O OG1 . THR   B 57  ? 0.1801 0.1692 0.2004 -0.0050 0.0132  0.0153  57  THR   B OG1 
4747 C CG2 . THR   B 57  ? 0.1819 0.1703 0.1754 -0.0087 0.0105  0.0122  57  THR   B CG2 
4755 N N   . ASN   B 58  ? 0.1617 0.2150 0.2431 -0.0166 0.0017  -0.0071 58  ASN   B N   
4756 C CA  . ASN   B 58  ? 0.1876 0.2613 0.2833 -0.0240 0.0327  0.0050  58  ASN   B CA  
4757 C C   . ASN   B 58  ? 0.1660 0.2406 0.2422 -0.0159 0.0047  0.0024  58  ASN   B C   
4758 O O   . ASN   B 58  ? 0.1720 0.2490 0.2501 -0.0227 -0.0011 -0.0107 58  ASN   B O   
4759 C CB  . ASN   B 58  ? 0.2525 0.3201 0.4115 -0.0383 0.0629  0.0114  58  ASN   B CB  
4760 C CG  . ASN   B 58  ? 0.3766 0.4018 0.5649 -0.0446 0.0701  0.0357  58  ASN   B CG  
4761 O OD1 . ASN   B 58  ? 0.4247 0.4247 0.6196 -0.0438 0.0674  0.0432  58  ASN   B OD1 
4762 N ND2 . ASN   B 58  ? 0.5016 0.5016 0.6165 -0.0501 0.0742  0.0450  58  ASN   B ND2 
4769 N N   . ASN   B 59  ? 0.1613 0.2179 0.2283 -0.0119 -0.0057 0.0111  59  ASN   B N   
4770 C CA  . ASN   B 59  ? 0.1661 0.2189 0.2250 -0.0148 -0.0143 0.0166  59  ASN   B CA  
4771 C C   . ASN   B 59  ? 0.1581 0.2072 0.2169 -0.0196 -0.0178 -0.0011 59  ASN   B C   
4772 O O   . ASN   B 59  ? 0.1640 0.2067 0.2182 -0.0150 -0.0120 0.0046  59  ASN   B O   
4773 C CB  . ASN   B 59  ? 0.1696 0.2397 0.2439 -0.0131 -0.0264 0.0183  59  ASN   B CB  
4774 C CG  . ASN   B 59  ? 0.1850 0.2590 0.2522 -0.0087 -0.0432 0.0154  59  ASN   B CG  
4775 O OD1 . ASN   B 59  ? 0.1901 0.2565 0.2523 -0.0025 -0.0251 0.0285  59  ASN   B OD1 
4776 N ND2 . ASN   B 59  ? 0.1912 0.2677 0.2643 -0.0192 -0.0532 0.0156  59  ASN   B ND2 
4783 N N   . ALA   B 60  ? 0.1580 0.1971 0.2161 -0.0141 -0.0054 -0.0022 60  ALA   B N   
4784 C CA  . ALA   B 60  ? 0.1721 0.1900 0.2067 -0.0221 -0.0053 0.0086  60  ALA   B CA  
4785 C C   . ALA   B 60  ? 0.1734 0.1868 0.1845 -0.0155 -0.0080 0.0073  60  ALA   B C   
4786 O O   . ALA   B 60  ? 0.1747 0.1903 0.2015 -0.0175 -0.0039 -0.0057 60  ALA   B O   
4787 C CB  . ALA   B 60  ? 0.1881 0.1861 0.2394 -0.0228 0.0059  0.0219  60  ALA   B CB  
4793 N N   . MET   B 61  ? 0.1602 0.1717 0.1793 -0.0109 -0.0060 0.0093  61  MET   B N   
4794 C CA  . MET   B 61  ? 0.1614 0.1663 0.1815 -0.0069 -0.0174 0.0107  61  MET   B CA  
4795 C C   . MET   B 61  ? 0.1713 0.1588 0.1780 -0.0142 -0.0153 0.0149  61  MET   B C   
4796 O O   . MET   B 61  ? 0.1686 0.1596 0.1699 -0.0060 -0.0100 -0.0083 61  MET   B O   
4797 C CB  . MET   B 61  ? 0.1530 0.1641 0.1846 -0.0057 -0.0205 0.0016  61  MET   B CB  
4798 C CG  . MET   B 61  ? 0.1488 0.1690 0.1720 -0.0026 -0.0117 0.0054  61  MET   B CG  
4799 S SD  . MET   B 61  ? 0.1574 0.1632 0.2007 -0.0054 -0.0085 -0.0065 61  MET   B SD  
4800 C CE  . MET   B 61  ? 0.1651 0.1878 0.2175 -0.0015 -0.0081 -0.0184 61  MET   B CE  
4810 N N   . GLN   B 62  ? 0.1624 0.1652 0.1702 -0.0057 -0.0228 0.0065  62  GLN   B N   
4811 C CA  . GLN   B 62  ? 0.1601 0.1706 0.1917 -0.0024 -0.0266 0.0072  62  GLN   B CA  
4812 C C   . GLN   B 62  ? 0.1682 0.1714 0.1944 -0.0063 -0.0320 -0.0013 62  GLN   B C   
4813 O O   . GLN   B 62  ? 0.1828 0.1740 0.2009 -0.0068 -0.0369 -0.0157 62  GLN   B O   
4814 C CB  . GLN   B 62  ? 0.1608 0.1778 0.1781 0.0020  -0.0213 0.0107  62  GLN   B CB  
4815 C CG  . GLN   B 62  ? 0.1701 0.1815 0.1856 -0.0018 -0.0302 0.0043  62  GLN   B CG  
4816 C CD  . GLN   B 62  ? 0.1731 0.1760 0.1760 -0.0008 -0.0295 0.0127  62  GLN   B CD  
4817 O OE1 . GLN   B 62  ? 0.1729 0.1682 0.1929 -0.0010 -0.0316 0.0007  62  GLN   B OE1 
4818 N NE2 . GLN   B 62  ? 0.1728 0.1862 0.1837 0.0002  -0.0238 -0.0032 62  GLN   B NE2 
4827 N N   . VAL   B 63  ? 0.1729 0.1755 0.2002 -0.0135 -0.0299 -0.0104 63  VAL   B N   
4828 C CA  . VAL   B 63  ? 0.1868 0.1809 0.2244 -0.0170 -0.0288 -0.0043 63  VAL   B CA  
4829 C C   . VAL   B 63  ? 0.1826 0.1693 0.2072 -0.0186 -0.0358 -0.0158 63  VAL   B C   
4830 O O   . VAL   B 63  ? 0.1910 0.1724 0.2230 -0.0169 -0.0509 -0.0122 63  VAL   B O   
4831 C CB  . VAL   B 63  ? 0.1838 0.1966 0.2692 -0.0250 -0.0338 -0.0100 63  VAL   B CB  
4832 C CG1 . VAL   B 63  ? 0.1928 0.2047 0.2886 -0.0289 -0.0300 -0.0131 63  VAL   B CG1 
4833 C CG2 . VAL   B 63  ? 0.1798 0.2155 0.2909 -0.0156 -0.0403 -0.0050 63  VAL   B CG2 
4843 N N   . GLU   B 64  ? 0.1808 0.1659 0.2017 -0.0138 -0.0354 -0.0092 64  GLU   B N   
4844 C CA  . GLU   B 64  ? 0.1777 0.1596 0.1844 -0.0154 -0.0410 -0.0028 64  GLU   B CA  
4845 C C   . GLU   B 64  ? 0.1750 0.1601 0.1794 -0.0110 -0.0364 -0.0140 64  GLU   B C   
4846 O O   . GLU   B 64  ? 0.1909 0.1704 0.1769 -0.0115 -0.0349 -0.0156 64  GLU   B O   
4847 C CB  . GLU   B 64  ? 0.1802 0.1689 0.1957 -0.0191 -0.0299 -0.0053 64  GLU   B CB  
4848 C CG  . GLU   B 64  ? 0.1885 0.1693 0.1954 -0.0220 -0.0318 -0.0178 64  GLU   B CG  
4849 C CD  . GLU   B 64  ? 0.1893 0.1883 0.2025 -0.0364 -0.0318 -0.0181 64  GLU   B CD  
4850 O OE1 . GLU   B 64  ? 0.1908 0.2029 0.2066 -0.0411 -0.0220 -0.0320 64  GLU   B OE1 
4851 O OE2 . GLU   B 64  ? 0.2058 0.1967 0.2030 -0.0414 -0.0454 -0.0094 64  GLU   B OE2 
4858 N N   . SER   B 65  ? 0.1764 0.1545 0.1732 -0.0165 -0.0235 -0.0128 65  SER   B N   
4859 C CA  . SER   B 65  ? 0.1775 0.1515 0.1787 -0.0022 -0.0246 -0.0168 65  SER   B CA  
4860 C C   . SER   B 65  ? 0.1854 0.1619 0.1748 0.0055  -0.0348 -0.0213 65  SER   B C   
4861 O O   . SER   B 65  ? 0.1813 0.1692 0.1804 -0.0025 -0.0269 -0.0170 65  SER   B O   
4862 C CB  . SER   B 65  ? 0.1838 0.1583 0.1714 -0.0068 -0.0225 -0.0115 65  SER   B CB  
4863 O OG  . SER   B 65  ? 0.1864 0.1580 0.1818 -0.0114 -0.0150 -0.0156 65  SER   B OG  
4869 N N   . ASP   B 66  ? 0.1941 0.1676 0.1710 -0.0008 -0.0418 -0.0239 66  ASP   B N   
4870 C CA  . ASP   B 66  ? 0.1959 0.1697 0.1730 0.0059  -0.0472 -0.0148 66  ASP   B CA  
4871 C C   . ASP   B 66  ? 0.1999 0.1803 0.1749 -0.0055 -0.0375 -0.0231 66  ASP   B C   
4872 O O   . ASP   B 66  ? 0.2019 0.1891 0.1725 0.0046  -0.0352 -0.0251 66  ASP   B O   
4873 C CB  . ASP   B 66  ? 0.2106 0.1840 0.2088 0.0085  -0.0559 -0.0169 66  ASP   B CB  
4874 C CG  . ASP   B 66  ? 0.2426 0.2011 0.2351 0.0165  -0.0576 -0.0037 66  ASP   B CG  
4875 O OD1 . ASP   B 66  ? 0.2706 0.1987 0.2356 0.0052  -0.0561 0.0019  66  ASP   B OD1 
4876 O OD2 . ASP   B 66  ? 0.2577 0.2219 0.2927 0.0389  -0.0492 0.0000  66  ASP   B OD2 
4881 N N   . ASP   B 67  ? 0.1961 0.1720 0.1722 -0.0105 -0.0283 -0.0189 67  ASP   B N   
4882 C CA  . ASP   B 67  ? 0.2146 0.1673 0.1761 -0.0089 -0.0265 -0.0130 67  ASP   B CA  
4883 C C   . ASP   B 67  ? 0.2063 0.1662 0.1892 0.0017  -0.0288 -0.0129 67  ASP   B C   
4884 O O   . ASP   B 67  ? 0.2075 0.1738 0.2208 -0.0025 -0.0171 -0.0276 67  ASP   B O   
4885 C CB  . ASP   B 67  ? 0.2332 0.1799 0.2016 -0.0135 -0.0468 -0.0113 67  ASP   B CB  
4886 C CG  . ASP   B 67  ? 0.2723 0.1851 0.2091 -0.0110 -0.0741 -0.0192 67  ASP   B CG  
4887 O OD1 . ASP   B 67  ? 0.2987 0.1928 0.2313 -0.0131 -0.0730 -0.0115 67  ASP   B OD1 
4888 O OD2 . ASP   B 67  ? 0.2891 0.1944 0.2308 0.0047  -0.0759 -0.0121 67  ASP   B OD2 
4893 N N   . TYR   B 68  ? 0.1987 0.1736 0.1656 -0.0028 -0.0375 -0.0226 68  TYR   B N   
4894 C CA  . TYR   B 68  ? 0.1922 0.1868 0.1985 0.0055  -0.0418 -0.0322 68  TYR   B CA  
4895 C C   . TYR   B 68  ? 0.1781 0.1824 0.2037 0.0046  -0.0382 -0.0409 68  TYR   B C   
4896 O O   . TYR   B 68  ? 0.1885 0.1941 0.2167 0.0106  -0.0382 -0.0578 68  TYR   B O   
4897 C CB  . TYR   B 68  ? 0.1993 0.2077 0.2069 0.0109  -0.0494 -0.0444 68  TYR   B CB  
4898 C CG  . TYR   B 68  ? 0.2070 0.2212 0.2204 0.0134  -0.0406 -0.0652 68  TYR   B CG  
4899 C CD1 . TYR   B 68  ? 0.2083 0.2282 0.2424 -0.0020 -0.0373 -0.0777 68  TYR   B CD1 
4900 C CD2 . TYR   B 68  ? 0.2108 0.2427 0.2399 0.0169  -0.0553 -0.0621 68  TYR   B CD2 
4901 C CE1 . TYR   B 68  ? 0.2147 0.2422 0.2631 -0.0013 -0.0295 -0.0803 68  TYR   B CE1 
4902 C CE2 . TYR   B 68  ? 0.2063 0.2479 0.2544 0.0142  -0.0456 -0.0841 68  TYR   B CE2 
4903 C CZ  . TYR   B 68  ? 0.2077 0.2474 0.2681 0.0044  -0.0373 -0.0834 68  TYR   B CZ  
4904 O OH  . TYR   B 68  ? 0.2082 0.2603 0.3116 -0.0036 -0.0277 -0.0590 68  TYR   B OH  
4914 N N   . ILE   B 69  ? 0.1805 0.1730 0.1946 0.0046  -0.0367 -0.0406 69  ILE   B N   
4915 C CA  . ILE   B 69  ? 0.1973 0.1853 0.1999 -0.0028 -0.0239 -0.0426 69  ILE   B CA  
4916 C C   . ILE   B 69  ? 0.2014 0.1797 0.1864 0.0049  -0.0386 -0.0379 69  ILE   B C   
4917 O O   . ILE   B 69  ? 0.2089 0.1895 0.1865 0.0063  -0.0298 -0.0340 69  ILE   B O   
4918 C CB  . ILE   B 69  ? 0.1982 0.1842 0.2217 -0.0059 0.0068  -0.0399 69  ILE   B CB  
4919 C CG1 . ILE   B 69  ? 0.1990 0.1886 0.2334 -0.0119 0.0098  -0.0397 69  ILE   B CG1 
4920 C CG2 . ILE   B 69  ? 0.2138 0.1900 0.2347 -0.0078 0.0059  -0.0294 69  ILE   B CG2 
4921 C CD1 . ILE   B 69  ? 0.1974 0.1959 0.2483 -0.0221 0.0050  -0.0447 69  ILE   B CD1 
4933 N N   . ALA   B 70  ? 0.2011 0.1775 0.1975 0.0072  -0.0500 -0.0354 70  ALA   B N   
4934 C CA  . ALA   B 70  ? 0.2024 0.1826 0.1931 0.0031  -0.0538 -0.0299 70  ALA   B CA  
4935 C C   . ALA   B 70  ? 0.2056 0.1838 0.2089 0.0013  -0.0603 -0.0420 70  ALA   B C   
4936 O O   . ALA   B 70  ? 0.2103 0.1800 0.2048 0.0098  -0.0511 -0.0431 70  ALA   B O   
4937 C CB  . ALA   B 70  ? 0.2031 0.1973 0.1982 -0.0026 -0.0536 -0.0268 70  ALA   B CB  
4943 N N   . THR   B 71  ? 0.2113 0.1880 0.2180 0.0041  -0.0736 -0.0335 71  THR   B N   
4944 C CA  . THR   B 71  ? 0.2260 0.1956 0.2232 0.0115  -0.0849 -0.0420 71  THR   B CA  
4945 C C   . THR   B 71  ? 0.2174 0.1983 0.2539 0.0335  -0.0811 -0.0648 71  THR   B C   
4946 O O   . THR   B 71  ? 0.2319 0.2072 0.2911 0.0364  -0.0761 -0.0730 71  THR   B O   
4947 C CB  . THR   B 71  ? 0.2513 0.2165 0.2529 0.0029  -0.0892 -0.0200 71  THR   B CB  
4948 O OG1 . THR   B 71  ? 0.2664 0.2368 0.2994 -0.0178 -0.0853 -0.0059 71  THR   B OG1 
4949 C CG2 . THR   B 71  ? 0.2733 0.2150 0.2743 0.0110  -0.0744 -0.0014 71  THR   B CG2 
4957 N N   . ASN   B 72  ? 0.2100 0.2011 0.2478 0.0202  -0.0735 -0.0776 72  ASN   B N   
4958 C CA  . ASN   B 72  ? 0.2153 0.2065 0.2385 0.0173  -0.0606 -0.0843 72  ASN   B CA  
4959 C C   . ASN   B 72  ? 0.2170 0.2211 0.2554 0.0050  -0.0340 -0.0758 72  ASN   B C   
4960 O O   . ASN   B 72  ? 0.2174 0.2363 0.2765 0.0144  -0.0082 -0.0770 72  ASN   B O   
4961 C CB  . ASN   B 72  ? 0.2169 0.2205 0.2535 0.0146  -0.0702 -0.0704 72  ASN   B CB  
4962 C CG  . ASN   B 72  ? 0.2299 0.2324 0.2695 0.0342  -0.0595 -0.0505 72  ASN   B CG  
4963 O OD1 . ASN   B 72  ? 0.2517 0.2501 0.2738 0.0198  -0.0485 -0.0517 72  ASN   B OD1 
4964 N ND2 . ASN   B 72  ? 0.2385 0.2420 0.3020 0.0519  -0.0439 -0.0074 72  ASN   B ND2 
4971 N N   . GLY   B 73  ? 0.2162 0.2167 0.2255 0.0013  -0.0390 -0.0796 73  GLY   B N   
4972 C CA  . GLY   B 73  ? 0.1977 0.2314 0.2080 -0.0026 -0.0341 -0.0645 73  GLY   B CA  
4973 C C   . GLY   B 73  ? 0.1929 0.2282 0.1562 0.0059  -0.0326 -0.0615 73  GLY   B C   
4974 O O   . GLY   B 73  ? 0.1883 0.2162 0.1723 0.0102  -0.0243 -0.0466 73  GLY   B O   
4978 N N   . PRO   B 74  ? 0.1983 0.2376 0.1538 0.0087  -0.0324 -0.0465 74  PRO   B N   
4979 C CA  . PRO   B 74  ? 0.1923 0.2327 0.1458 0.0170  -0.0283 -0.0278 74  PRO   B CA  
4980 C C   . PRO   B 74  ? 0.1823 0.2152 0.1436 0.0146  -0.0172 -0.0207 74  PRO   B C   
4981 O O   . PRO   B 74  ? 0.1886 0.2149 0.1929 0.0137  -0.0146 -0.0412 74  PRO   B O   
4982 C CB  . PRO   B 74  ? 0.2071 0.2537 0.1482 0.0125  -0.0286 -0.0230 74  PRO   B CB  
4983 C CG  . PRO   B 74  ? 0.2260 0.2645 0.1926 0.0106  -0.0236 -0.0156 74  PRO   B CG  
4984 C CD  . PRO   B 74  ? 0.2222 0.2529 0.1771 0.0096  -0.0235 -0.0336 74  PRO   B CD  
4992 N N   . LEU   B 75  ? 0.1780 0.2010 0.1361 0.0156  -0.0183 -0.0229 75  LEU   B N   
4993 C CA  . LEU   B 75  ? 0.1749 0.2074 0.1388 0.0082  -0.0204 -0.0115 75  LEU   B CA  
4994 C C   . LEU   B 75  ? 0.1844 0.2136 0.1399 0.0074  -0.0121 -0.0109 75  LEU   B C   
4995 O O   . LEU   B 75  ? 0.1980 0.2216 0.1574 -0.0028 -0.0107 -0.0054 75  LEU   B O   
4996 C CB  . LEU   B 75  ? 0.1836 0.2135 0.1371 -0.0042 -0.0189 0.0040  75  LEU   B CB  
4997 C CG  . LEU   B 75  ? 0.2088 0.2253 0.1541 -0.0332 -0.0154 -0.0086 75  LEU   B CG  
4998 C CD1 . LEU   B 75  ? 0.2424 0.2333 0.1508 -0.0484 0.0114  -0.0129 75  LEU   B CD1 
4999 C CD2 . LEU   B 75  ? 0.2413 0.2490 0.2340 -0.0283 -0.0081 0.0035  75  LEU   B CD2 
5011 N N   . LYS   B 76  ? 0.1895 0.2329 0.1637 0.0030  -0.0037 -0.0010 76  LYS   B N   
5012 C CA  . LYS   B 76  ? 0.2004 0.2409 0.2016 -0.0073 0.0180  -0.0036 76  LYS   B CA  
5013 C C   . LYS   B 76  ? 0.1854 0.2234 0.1603 -0.0005 0.0081  0.0207  76  LYS   B C   
5014 O O   . LYS   B 76  ? 0.1801 0.2108 0.1655 0.0027  -0.0019 0.0207  76  LYS   B O   
5015 C CB  . LYS   B 76  ? 0.2101 0.2512 0.2717 -0.0132 0.0406  -0.0393 76  LYS   B CB  
5016 C CG  . LYS   B 76  ? 0.2173 0.2747 0.3196 -0.0006 0.0303  -0.0415 76  LYS   B CG  
5017 C CD  . LYS   B 76  ? 0.2225 0.2888 0.3749 0.0118  0.0203  -0.0546 76  LYS   B CD  
5018 C CE  . LYS   B 76  ? 0.2332 0.3055 0.4187 0.0205  0.0107  -0.0626 76  LYS   B CE  
5019 N NZ  . LYS   B 76  ? 0.2296 0.3117 0.4438 0.0200  -0.0166 -0.0850 76  LYS   B NZ  
5033 N N   . VAL   B 77  ? 0.1911 0.2318 0.1623 0.0054  0.0012  0.0223  77  VAL   B N   
5034 C CA  . VAL   B 77  ? 0.1946 0.2190 0.1678 0.0135  0.0075  0.0401  77  VAL   B CA  
5035 C C   . VAL   B 77  ? 0.1799 0.1938 0.1589 0.0170  0.0161  0.0274  77  VAL   B C   
5036 O O   . VAL   B 77  ? 0.1874 0.1902 0.1565 0.0288  0.0231  0.0186  77  VAL   B O   
5037 C CB  . VAL   B 77  ? 0.2015 0.2298 0.2084 0.0136  0.0232  0.0586  77  VAL   B CB  
5038 C CG1 . VAL   B 77  ? 0.2139 0.2173 0.2419 0.0057  0.0190  0.0678  77  VAL   B CG1 
5039 C CG2 . VAL   B 77  ? 0.2191 0.2491 0.2404 0.0142  0.0067  0.0762  77  VAL   B CG2 
5049 N N   . GLY   B 78  ? 0.1808 0.1788 0.1620 0.0104  0.0080  0.0191  78  GLY   B N   
5050 C CA  . GLY   B 78  ? 0.1802 0.1701 0.1589 0.0165  0.0136  0.0121  78  GLY   B CA  
5051 C C   . GLY   B 78  ? 0.1717 0.1670 0.1541 0.0143  0.0120  0.0176  78  GLY   B C   
5052 O O   . GLY   B 78  ? 0.1750 0.1633 0.1727 0.0146  0.0047  0.0181  78  GLY   B O   
5056 N N   . GLY   B 79  ? 0.1659 0.1813 0.1553 0.0067  0.0082  0.0046  79  GLY   B N   
5057 C CA  . GLY   B 79  ? 0.1665 0.1754 0.1392 0.0057  0.0082  0.0078  79  GLY   B CA  
5058 C C   . GLY   B 79  ? 0.1578 0.1630 0.1590 0.0102  0.0006  0.0046  79  GLY   B C   
5059 O O   . GLY   B 79  ? 0.1682 0.1624 0.1654 0.0126  0.0092  0.0149  79  GLY   B O   
5063 N N   . SER   B 80  ? 0.1563 0.1590 0.1559 0.0034  0.0165  0.0036  80  SER   B N   
5064 C CA  . SER   B 80  ? 0.1493 0.1576 0.1576 0.0005  -0.0057 -0.0007 80  SER   B CA  
5065 C C   . SER   B 80  ? 0.1501 0.1546 0.1575 0.0105  -0.0061 -0.0103 80  SER   B C   
5066 O O   . SER   B 80  ? 0.1721 0.1532 0.1928 0.0126  -0.0036 -0.0109 80  SER   B O   
5067 C CB  . SER   B 80  ? 0.1563 0.1635 0.1751 -0.0019 -0.0104 0.0059  80  SER   B CB  
5068 O OG  . SER   B 80  ? 0.1704 0.1713 0.1876 -0.0019 -0.0190 0.0072  80  SER   B OG  
5074 N N   . CYS   B 81  ? 0.1517 0.1421 0.1656 0.0040  -0.0082 -0.0100 81  CYS   B N   
5075 C CA  . CYS   B 81  ? 0.1635 0.1411 0.1702 0.0033  -0.0218 -0.0091 81  CYS   B CA  
5076 C C   . CYS   B 81  ? 0.1581 0.1420 0.1425 0.0084  -0.0210 0.0004  81  CYS   B C   
5077 O O   . CYS   B 81  ? 0.1779 0.1446 0.1604 0.0106  -0.0064 -0.0065 81  CYS   B O   
5078 C CB  . CYS   B 81  ? 0.1737 0.1480 0.1765 -0.0045 -0.0255 0.0001  81  CYS   B CB  
5079 S SG  . CYS   B 81  ? 0.1764 0.1679 0.1821 -0.0049 -0.0320 -0.0123 81  CYS   B SG  
5085 N N   . VAL   B 82  ? 0.1631 0.1458 0.1443 0.0018  -0.0174 -0.0033 82  VAL   B N   
5086 C CA  . VAL   B 82  ? 0.1731 0.1465 0.1522 -0.0057 -0.0172 0.0025  82  VAL   B CA  
5087 C C   . VAL   B 82  ? 0.1790 0.1350 0.1685 -0.0030 -0.0120 -0.0056 82  VAL   B C   
5088 O O   . VAL   B 82  ? 0.1816 0.1385 0.1997 -0.0048 -0.0120 -0.0189 82  VAL   B O   
5089 C CB  . VAL   B 82  ? 0.1808 0.1615 0.1732 0.0007  -0.0156 0.0075  82  VAL   B CB  
5090 C CG1 . VAL   B 82  ? 0.2050 0.1841 0.1751 0.0014  -0.0207 0.0192  82  VAL   B CG1 
5091 C CG2 . VAL   B 82  ? 0.1927 0.1678 0.1877 -0.0075 -0.0342 0.0092  82  VAL   B CG2 
5101 N N   . LEU   B 83  ? 0.1632 0.1334 0.1685 -0.0164 -0.0201 -0.0123 83  LEU   B N   
5102 C CA  . LEU   B 83  ? 0.1627 0.1451 0.1507 -0.0102 -0.0276 -0.0076 83  LEU   B CA  
5103 C C   . LEU   B 83  ? 0.1657 0.1407 0.1587 -0.0171 -0.0257 -0.0078 83  LEU   B C   
5104 O O   . LEU   B 83  ? 0.1598 0.1473 0.1510 -0.0204 -0.0158 0.0061  83  LEU   B O   
5105 C CB  . LEU   B 83  ? 0.1702 0.1497 0.1604 -0.0164 -0.0303 -0.0144 83  LEU   B CB  
5106 C CG  . LEU   B 83  ? 0.1958 0.1736 0.1639 -0.0217 -0.0181 -0.0137 83  LEU   B CG  
5107 C CD1 . LEU   B 83  ? 0.2066 0.1819 0.1727 -0.0118 -0.0263 -0.0034 83  LEU   B CD1 
5108 C CD2 . LEU   B 83  ? 0.2090 0.1853 0.1798 -0.0139 -0.0164 -0.0176 83  LEU   B CD2 
5120 N N   . SER   B 84  ? 0.1767 0.1484 0.1818 -0.0263 -0.0229 0.0022  84  SER   B N   
5121 C CA  . SER   B 84  ? 0.1692 0.1692 0.1769 -0.0263 -0.0217 0.0199  84  SER   B CA  
5122 C C   . SER   B 84  ? 0.1658 0.1856 0.1366 -0.0184 -0.0295 0.0218  84  SER   B C   
5123 O O   . SER   B 84  ? 0.1736 0.1656 0.1305 -0.0146 -0.0188 0.0047  84  SER   B O   
5124 C CB  . SER   B 84  ? 0.1858 0.1703 0.2376 -0.0316 0.0038  0.0258  84  SER   B CB  
5125 O OG  . SER   B 84  ? 0.1926 0.1924 0.2776 -0.0460 0.0033  0.0301  84  SER   B OG  
5131 N N   . GLY   B 85  ? 0.1689 0.2030 0.1449 -0.0219 -0.0235 0.0235  85  GLY   B N   
5132 C CA  . GLY   B 85  ? 0.1644 0.2114 0.1578 -0.0337 -0.0066 -0.0054 85  GLY   B CA  
5133 C C   . GLY   B 85  ? 0.1658 0.1897 0.1489 -0.0392 -0.0092 0.0060  85  GLY   B C   
5134 O O   . GLY   B 85  ? 0.1721 0.1933 0.1619 -0.0519 0.0055  -0.0042 85  GLY   B O   
5138 N N   . HIS   B 86  ? 0.1663 0.1738 0.1727 -0.0306 -0.0203 0.0128  86  HIS   B N   
5139 C CA  . HIS   B 86  ? 0.1661 0.1723 0.1730 -0.0316 -0.0209 0.0151  86  HIS   B CA  
5140 C C   . HIS   B 86  ? 0.1614 0.1915 0.1610 -0.0408 -0.0161 0.0370  86  HIS   B C   
5141 O O   . HIS   B 86  ? 0.1791 0.1997 0.1679 -0.0329 0.0007  0.0343  86  HIS   B O   
5142 C CB  . HIS   B 86  ? 0.1758 0.1741 0.1811 -0.0210 -0.0249 0.0082  86  HIS   B CB  
5143 C CG  . HIS   B 86  ? 0.1788 0.1824 0.1737 -0.0123 -0.0308 0.0141  86  HIS   B CG  
5144 N ND1 . HIS   B 86  ? 0.1885 0.2079 0.1959 -0.0259 -0.0350 0.0022  86  HIS   B ND1 
5145 C CD2 . HIS   B 86  ? 0.1785 0.1900 0.1782 -0.0097 -0.0351 0.0090  86  HIS   B CD2 
5146 C CE1 . HIS   B 86  ? 0.1910 0.2009 0.1834 -0.0192 -0.0135 -0.0185 86  HIS   B CE1 
5147 N NE2 . HIS   B 86  ? 0.1865 0.1972 0.1699 -0.0044 -0.0204 0.0031  86  HIS   B NE2 
5155 N N   . ASN   B 87  ? 0.1687 0.1944 0.1637 -0.0338 -0.0081 0.0378  87  ASN   B N   
5156 C CA  . ASN   B 87  ? 0.1820 0.2079 0.1744 -0.0311 0.0163  0.0210  87  ASN   B CA  
5157 C C   . ASN   B 87  ? 0.1956 0.1953 0.1632 -0.0328 0.0329  0.0125  87  ASN   B C   
5158 O O   . ASN   B 87  ? 0.2193 0.1983 0.2065 -0.0257 0.0511  0.0153  87  ASN   B O   
5159 C CB  . ASN   B 87  ? 0.1848 0.2469 0.2043 -0.0286 0.0191  0.0182  87  ASN   B CB  
5160 C CG  . ASN   B 87  ? 0.1899 0.2680 0.2132 0.0020  0.0248  0.0336  87  ASN   B CG  
5161 O OD1 . ASN   B 87  ? 0.1825 0.2574 0.2058 0.0114  0.0363  0.0545  87  ASN   B OD1 
5162 N ND2 . ASN   B 87  ? 0.2173 0.2820 0.2452 0.0025  0.0299  0.0232  87  ASN   B ND2 
5169 N N   . LEU   B 88  ? 0.1809 0.1864 0.1556 -0.0367 0.0124  0.0111  88  LEU   B N   
5170 C CA  . LEU   B 88  ? 0.1878 0.1745 0.1599 -0.0361 0.0032  0.0052  88  LEU   B CA  
5171 C C   . LEU   B 88  ? 0.1859 0.1680 0.1568 -0.0388 -0.0071 0.0042  88  LEU   B C   
5172 O O   . LEU   B 88  ? 0.2053 0.1823 0.1841 -0.0200 -0.0313 -0.0030 88  LEU   B O   
5173 C CB  . LEU   B 88  ? 0.1947 0.1779 0.1820 -0.0397 -0.0146 0.0193  88  LEU   B CB  
5174 C CG  . LEU   B 88  ? 0.2310 0.2116 0.1969 -0.0325 -0.0403 0.0415  88  LEU   B CG  
5175 C CD1 . LEU   B 88  ? 0.2476 0.2457 0.2044 -0.0423 -0.0252 0.0558  88  LEU   B CD1 
5176 C CD2 . LEU   B 88  ? 0.2680 0.2390 0.2504 0.0084  -0.0630 0.0247  88  LEU   B CD2 
5188 N N   . ALA   B 89  ? 0.1728 0.1648 0.1431 -0.0367 0.0098  0.0062  89  ALA   B N   
5189 C CA  . ALA   B 89  ? 0.1734 0.1608 0.1253 -0.0313 0.0003  0.0170  89  ALA   B CA  
5190 C C   . ALA   B 89  ? 0.1767 0.1597 0.1355 -0.0380 0.0075  0.0049  89  ALA   B C   
5191 O O   . ALA   B 89  ? 0.1667 0.1696 0.1754 -0.0395 0.0068  -0.0229 89  ALA   B O   
5192 C CB  . ALA   B 89  ? 0.1612 0.1579 0.1568 -0.0312 0.0017  0.0199  89  ALA   B CB  
5198 N N   . LYS   B 90  ? 0.2091 0.1536 0.1475 -0.0402 -0.0101 0.0162  90  LYS   B N   
5199 C CA  . LYS   B 90  ? 0.2216 0.1512 0.1478 -0.0451 -0.0129 0.0115  90  LYS   B CA  
5200 C C   . LYS   B 90  ? 0.2081 0.1452 0.1601 -0.0417 -0.0076 -0.0084 90  LYS   B C   
5201 O O   . LYS   B 90  ? 0.2216 0.1632 0.1750 -0.0578 -0.0005 -0.0018 90  LYS   B O   
5202 C CB  . LYS   B 90  ? 0.2485 0.1567 0.1972 -0.0366 -0.0062 0.0194  90  LYS   B CB  
5203 C CG  . LYS   B 90  ? 0.2494 0.1815 0.1898 -0.0245 0.0226  0.0150  90  LYS   B CG  
5204 C CD  . LYS   B 90  ? 0.2766 0.2107 0.2407 -0.0157 0.0497  -0.0035 90  LYS   B CD  
5205 C CE  . LYS   B 90  ? 0.3087 0.2350 0.2949 -0.0232 0.0569  -0.0138 90  LYS   B CE  
5206 N NZ  . LYS   B 90  ? 0.3027 0.2352 0.2922 -0.0406 0.0751  -0.0152 90  LYS   B NZ  
5220 N N   . HIS   B 91  ? 0.1816 0.1382 0.1397 -0.0329 -0.0132 0.0091  91  HIS   B N   
5221 C CA  . HIS   B 91  ? 0.1787 0.1375 0.1557 -0.0234 -0.0195 0.0044  91  HIS   B CA  
5222 C C   . HIS   B 91  ? 0.1661 0.1474 0.1320 -0.0272 -0.0140 0.0085  91  HIS   B C   
5223 O O   . HIS   B 91  ? 0.1787 0.1545 0.1286 -0.0286 -0.0202 0.0016  91  HIS   B O   
5224 C CB  . HIS   B 91  ? 0.1931 0.1393 0.1923 -0.0077 -0.0145 0.0157  91  HIS   B CB  
5225 C CG  . HIS   B 91  ? 0.2327 0.1614 0.2604 0.0009  0.0184  0.0243  91  HIS   B CG  
5226 N ND1 . HIS   B 91  ? 0.2657 0.1709 0.3255 0.0064  0.0315  0.0158  91  HIS   B ND1 
5227 C CD2 . HIS   B 91  ? 0.2470 0.1898 0.3148 0.0168  0.0071  0.0580  91  HIS   B CD2 
5228 C CE1 . HIS   B 91  ? 0.2684 0.1843 0.3474 0.0251  0.0372  0.0187  91  HIS   B CE1 
5229 N NE2 . HIS   B 91  ? 0.2600 0.2001 0.3575 0.0326  0.0259  0.0568  91  HIS   B NE2 
5237 N N   . CYS   B 92  ? 0.1599 0.1469 0.1256 -0.0301 -0.0194 0.0016  92  CYS   B N   
5238 C CA  . CYS   B 92  ? 0.1686 0.1440 0.1188 -0.0273 -0.0129 -0.0004 92  CYS   B CA  
5239 C C   . CYS   B 92  ? 0.1603 0.1396 0.1158 -0.0187 -0.0047 -0.0041 92  CYS   B C   
5240 O O   . CYS   B 92  ? 0.1645 0.1471 0.1413 -0.0200 -0.0032 -0.0005 92  CYS   B O   
5241 C CB  . CYS   B 92  ? 0.1643 0.1451 0.1391 -0.0162 -0.0077 0.0077  92  CYS   B CB  
5242 S SG  . CYS   B 92  ? 0.1595 0.1513 0.1401 -0.0124 -0.0128 0.0048  92  CYS   B SG  
5248 N N   . LEU   B 93  ? 0.1486 0.1393 0.1224 -0.0175 -0.0050 0.0002  93  LEU   B N   
5249 C CA  . LEU   B 93  ? 0.1586 0.1395 0.1284 -0.0014 -0.0113 0.0007  93  LEU   B CA  
5250 C C   . LEU   B 93  ? 0.1468 0.1330 0.1170 0.0001  -0.0067 0.0095  93  LEU   B C   
5251 O O   . LEU   B 93  ? 0.1477 0.1348 0.1430 -0.0041 -0.0051 -0.0003 93  LEU   B O   
5252 C CB  . LEU   B 93  ? 0.1556 0.1352 0.1576 0.0051  -0.0140 0.0007  93  LEU   B CB  
5253 C CG  . LEU   B 93  ? 0.1476 0.1521 0.1719 -0.0024 -0.0041 0.0148  93  LEU   B CG  
5254 C CD1 . LEU   B 93  ? 0.1501 0.1627 0.1652 0.0119  -0.0017 0.0010  93  LEU   B CD1 
5255 C CD2 . LEU   B 93  ? 0.1416 0.1546 0.1678 -0.0058 -0.0156 0.0075  93  LEU   B CD2 
5267 N N   . HIS   B 94  ? 0.1485 0.1241 0.1222 -0.0054 -0.0128 0.0061  94  HIS   B N   
5268 C CA  . HIS   B 94  ? 0.1528 0.1315 0.1269 -0.0025 -0.0021 0.0014  94  HIS   B CA  
5269 C C   . HIS   B 94  ? 0.1428 0.1361 0.1455 -0.0074 -0.0031 0.0053  94  HIS   B C   
5270 O O   . HIS   B 94  ? 0.1452 0.1485 0.1800 -0.0058 0.0088  -0.0114 94  HIS   B O   
5271 C CB  . HIS   B 94  ? 0.1541 0.1461 0.1328 0.0001  -0.0090 -0.0053 94  HIS   B CB  
5272 C CG  . HIS   B 94  ? 0.1516 0.1395 0.1439 -0.0069 -0.0214 0.0037  94  HIS   B CG  
5273 N ND1 . HIS   B 94  ? 0.1592 0.1430 0.1385 -0.0046 -0.0215 0.0009  94  HIS   B ND1 
5274 C CD2 . HIS   B 94  ? 0.1601 0.1404 0.1395 -0.0002 -0.0151 0.0075  94  HIS   B CD2 
5275 C CE1 . HIS   B 94  ? 0.1637 0.1396 0.1428 -0.0093 -0.0203 0.0032  94  HIS   B CE1 
5276 N NE2 . HIS   B 94  ? 0.1573 0.1450 0.1440 -0.0145 -0.0158 0.0025  94  HIS   B NE2 
5284 N N   . VAL   B 95  ? 0.1373 0.1387 0.1404 -0.0014 -0.0033 0.0021  95  VAL   B N   
5285 C CA  . VAL   B 95  ? 0.1433 0.1462 0.1347 -0.0034 0.0003  0.0157  95  VAL   B CA  
5286 C C   . VAL   B 95  ? 0.1574 0.1461 0.1396 -0.0058 0.0051  0.0048  95  VAL   B C   
5287 O O   . VAL   B 95  ? 0.1539 0.1450 0.1519 0.0028  0.0047  0.0115  95  VAL   B O   
5288 C CB  . VAL   B 95  ? 0.1545 0.1441 0.1404 -0.0063 -0.0105 0.0015  95  VAL   B CB  
5289 C CG1 . VAL   B 95  ? 0.1580 0.1545 0.1703 -0.0112 -0.0044 0.0066  95  VAL   B CG1 
5290 C CG2 . VAL   B 95  ? 0.1635 0.1437 0.1388 0.0047  -0.0078 -0.0009 95  VAL   B CG2 
5300 N N   . VAL   B 96  ? 0.1626 0.1487 0.1328 0.0080  0.0030  0.0109  96  VAL   B N   
5301 C CA  . VAL   B 96  ? 0.1670 0.1658 0.1251 0.0067  0.0014  0.0161  96  VAL   B CA  
5302 C C   . VAL   B 96  ? 0.1683 0.1597 0.1516 0.0123  0.0103  0.0174  96  VAL   B C   
5303 O O   . VAL   B 96  ? 0.1674 0.1645 0.1753 0.0038  0.0127  0.0018  96  VAL   B O   
5304 C CB  . VAL   B 96  ? 0.1774 0.1822 0.1325 0.0113  0.0049  0.0056  96  VAL   B CB  
5305 C CG1 . VAL   B 96  ? 0.1750 0.2001 0.1494 0.0233  0.0005  0.0084  96  VAL   B CG1 
5306 C CG2 . VAL   B 96  ? 0.1857 0.1821 0.1511 0.0068  0.0101  -0.0096 96  VAL   B CG2 
5316 N N   . GLY   B 97  ? 0.1711 0.1564 0.1425 0.0052  0.0062  0.0206  97  GLY   B N   
5317 C CA  . GLY   B 97  ? 0.1812 0.1668 0.1573 -0.0009 0.0078  0.0228  97  GLY   B CA  
5318 C C   . GLY   B 97  ? 0.2049 0.1683 0.1649 0.0069  -0.0024 0.0172  97  GLY   B C   
5319 O O   . GLY   B 97  ? 0.2133 0.1797 0.1542 0.0034  -0.0028 0.0122  97  GLY   B O   
5323 N N   . PRO   B 98  ? 0.2134 0.1696 0.1708 0.0048  0.0231  0.0231  98  PRO   B N   
5324 C CA  . PRO   B 98  ? 0.2188 0.1805 0.1725 0.0120  0.0366  0.0167  98  PRO   B CA  
5325 C C   . PRO   B 98  ? 0.2304 0.1825 0.1552 0.0277  0.0373  0.0320  98  PRO   B C   
5326 O O   . PRO   B 98  ? 0.2266 0.1877 0.1727 0.0293  0.0344  0.0329  98  PRO   B O   
5327 C CB  . PRO   B 98  ? 0.2045 0.1819 0.1973 0.0042  0.0398  0.0192  98  PRO   B CB  
5328 C CG  . PRO   B 98  ? 0.2013 0.1803 0.1935 0.0094  0.0298  0.0272  98  PRO   B CG  
5329 C CD  . PRO   B 98  ? 0.1900 0.1691 0.1930 0.0097  0.0311  0.0301  98  PRO   B CD  
5337 N N   . ASN   B 99  ? 0.2402 0.2004 0.1672 0.0420  0.0332  0.0117  99  ASN   B N   
5338 C CA  . ASN   B 99  ? 0.2590 0.2088 0.1694 0.0446  0.0257  0.0395  99  ASN   B CA  
5339 C C   . ASN   B 99  ? 0.2875 0.2437 0.1949 0.0410  0.0428  0.0623  99  ASN   B C   
5340 O O   . ASN   B 99  ? 0.3038 0.2498 0.2126 0.0412  0.0295  0.0590  99  ASN   B O   
5341 C CB  . ASN   B 99  ? 0.2640 0.2085 0.1860 0.0449  0.0114  0.0393  99  ASN   B CB  
5342 C CG  . ASN   B 99  ? 0.2675 0.2187 0.2075 0.0382  -0.0036 0.0365  99  ASN   B CG  
5343 O OD1 . ASN   B 99  ? 0.2797 0.2217 0.2294 0.0313  -0.0069 0.0428  99  ASN   B OD1 
5344 N ND2 . ASN   B 99  ? 0.2611 0.2207 0.2165 0.0480  -0.0238 0.0359  99  ASN   B ND2 
5351 N N   A VAL   B 100 ? 0.2988 0.2510 0.2269 0.0278  0.0604  0.0865  100 VAL   B N   
5352 N N   B VAL   B 100 ? 0.3091 0.2546 0.2307 0.0348  0.0390  0.0716  100 VAL   B N   
5353 C CA  A VAL   B 100 ? 0.3265 0.2702 0.2895 0.0172  0.0590  0.0894  100 VAL   B CA  
5354 C CA  B VAL   B 100 ? 0.3346 0.2712 0.2739 0.0296  0.0324  0.0758  100 VAL   B CA  
5355 C C   A VAL   B 100 ? 0.3540 0.2753 0.2805 0.0282  0.0538  0.1042  100 VAL   B C   
5356 C C   B VAL   B 100 ? 0.3556 0.2780 0.2754 0.0340  0.0335  0.0932  100 VAL   B C   
5357 O O   A VAL   B 100 ? 0.3648 0.2839 0.2812 0.0218  0.0658  0.0989  100 VAL   B O   
5358 O O   B VAL   B 100 ? 0.3603 0.2837 0.2787 0.0296  0.0361  0.0902  100 VAL   B O   
5359 C CB  A VAL   B 100 ? 0.3338 0.2873 0.3714 -0.0101 0.0528  0.0879  100 VAL   B CB  
5360 C CB  B VAL   B 100 ? 0.3404 0.2818 0.3155 0.0176  0.0256  0.0678  100 VAL   B CB  
5361 C CG1 A VAL   B 100 ? 0.3386 0.2941 0.3985 -0.0196 0.0538  0.0854  100 VAL   B CG1 
5362 C CG1 B VAL   B 100 ? 0.3434 0.2862 0.3292 0.0139  0.0250  0.0653  100 VAL   B CG1 
5363 C CG2 A VAL   B 100 ? 0.3357 0.2914 0.3846 -0.0162 0.0567  0.0973  100 VAL   B CG2 
5364 C CG2 B VAL   B 100 ? 0.3415 0.2838 0.3241 0.0144  0.0251  0.0685  100 VAL   B CG2 
5383 N N   . ASN   B 101 ? 0.3709 0.2811 0.2757 0.0419  0.0337  0.1099  101 ASN   B N   
5384 C CA  . ASN   B 101 ? 0.4104 0.2982 0.3062 0.0570  0.0130  0.1280  101 ASN   B CA  
5385 C C   . ASN   B 101 ? 0.4527 0.3311 0.2967 0.0628  -0.0037 0.1521  101 ASN   B C   
5386 O O   . ASN   B 101 ? 0.4607 0.3475 0.3260 0.0705  -0.0024 0.1169  101 ASN   B O   
5387 C CB  . ASN   B 101 ? 0.4084 0.2893 0.3228 0.0540  0.0180  0.1054  101 ASN   B CB  
5388 C CG  . ASN   B 101 ? 0.4039 0.2797 0.3256 0.0520  0.0138  0.1022  101 ASN   B CG  
5389 O OD1 . ASN   B 101 ? 0.4078 0.2832 0.3612 0.0448  0.0304  0.1009  101 ASN   B OD1 
5390 N ND2 . ASN   B 101 ? 0.3961 0.2757 0.3217 0.0509  0.0045  0.0920  101 ASN   B ND2 
5398 N N   . LYS   B 102 ? 0.4847 0.3618 0.3001 0.0528  0.0019  0.1514  102 LYS   B N   
5399 C CA  . LYS   B 102 ? 0.5162 0.4047 0.3352 0.0390  0.0145  0.1227  102 LYS   B CA  
5400 C C   . LYS   B 102 ? 0.5097 0.4060 0.3213 0.0402  0.0273  0.1167  102 LYS   B C   
5401 O O   . LYS   B 102 ? 0.5212 0.4136 0.3347 0.0411  0.0159  0.1057  102 LYS   B O   
5402 C CB  . LYS   B 102 ? 0.5477 0.4452 0.3891 0.0283  0.0248  0.0850  102 LYS   B CB  
5403 C CG  . LYS   B 102 ? 0.5720 0.4811 0.4647 0.0221  0.0320  0.0438  102 LYS   B CG  
5404 C CD  . LYS   B 102 ? 0.5937 0.5073 0.5300 0.0164  0.0412  0.0117  102 LYS   B CD  
5405 C CE  . LYS   B 102 ? 0.6065 0.5293 0.5861 0.0102  0.0515  -0.0088 102 LYS   B CE  
5406 N NZ  . LYS   B 102 ? 0.6158 0.5418 0.6208 0.0059  0.0580  -0.0198 102 LYS   B NZ  
5420 N N   . GLY   B 103 ? 0.4866 0.3967 0.3058 0.0368  0.0533  0.1150  103 GLY   B N   
5421 C CA  . GLY   B 103 ? 0.4640 0.3878 0.3227 0.0330  0.0780  0.0913  103 GLY   B CA  
5422 C C   . GLY   B 103 ? 0.4371 0.3756 0.3185 0.0220  0.0946  0.0703  103 GLY   B C   
5423 O O   . GLY   B 103 ? 0.4441 0.3859 0.3253 0.0164  0.0968  0.0682  103 GLY   B O   
5427 N N   A GLU   B 104 ? 0.4161 0.3557 0.2929 0.0194  0.1168  0.0587  104 GLU   B N   
5428 N N   B GLU   B 104 ? 0.4225 0.3687 0.3235 0.0174  0.0762  0.0542  104 GLU   B N   
5429 C CA  A GLU   B 104 ? 0.3953 0.3377 0.2668 0.0192  0.1297  0.0459  104 GLU   B CA  
5430 C CA  B GLU   B 104 ? 0.4067 0.3611 0.3212 0.0136  0.0581  0.0366  104 GLU   B CA  
5431 C C   A GLU   B 104 ? 0.4020 0.3425 0.2855 0.0076  0.1547  0.0402  104 GLU   B C   
5432 C C   B GLU   B 104 ? 0.3982 0.3579 0.3304 0.0068  0.0593  0.0279  104 GLU   B C   
5433 O O   A GLU   B 104 ? 0.4021 0.3430 0.3243 0.0078  0.1493  0.0322  104 GLU   B O   
5434 O O   B GLU   B 104 ? 0.3976 0.3574 0.3401 0.0072  0.0585  0.0247  104 GLU   B O   
5435 C CB  A GLU   B 104 ? 0.3766 0.3127 0.2502 0.0299  0.0894  0.0216  104 GLU   B CB  
5436 C CB  B GLU   B 104 ? 0.4004 0.3553 0.3088 0.0153  0.0383  0.0251  104 GLU   B CB  
5437 C CG  A GLU   B 104 ? 0.3616 0.2919 0.2206 0.0360  0.0420  -0.0110 104 GLU   B CG  
5438 C CG  B GLU   B 104 ? 0.3937 0.3487 0.2955 0.0157  0.0197  0.0122  104 GLU   B CG  
5439 C CD  A GLU   B 104 ? 0.3476 0.2709 0.1950 0.0363  0.0073  -0.0201 104 GLU   B CD  
5440 C CD  B GLU   B 104 ? 0.3873 0.3418 0.2858 0.0138  0.0063  0.0035  104 GLU   B CD  
5441 O OE1 A GLU   B 104 ? 0.3256 0.2483 0.1697 0.0407  0.0177  -0.0117 104 GLU   B OE1 
5442 O OE1 B GLU   B 104 ? 0.3828 0.3372 0.2783 0.0117  0.0060  0.0023  104 GLU   B OE1 
5443 O OE2 A GLU   B 104 ? 0.3546 0.2844 0.2132 0.0304  -0.0307 -0.0343 104 GLU   B OE2 
5444 O OE2 B GLU   B 104 ? 0.3871 0.3428 0.2910 0.0138  -0.0036 -0.0029 104 GLU   B OE2 
5457 N N   A ASP   B 105 ? 0.4043 0.3508 0.2904 -0.0059 0.1784  0.0477  105 ASP   B N   
5458 N N   B ASP   B 105 ? 0.3898 0.3565 0.3329 -0.0007 0.0616  0.0245  105 ASP   B N   
5459 C CA  A ASP   B 105 ? 0.4096 0.3564 0.3094 -0.0206 0.1989  0.0400  105 ASP   B CA  
5460 C CA  B ASP   B 105 ? 0.3827 0.3539 0.3388 -0.0081 0.0644  0.0180  105 ASP   B CA  
5461 C C   A ASP   B 105 ? 0.3916 0.3233 0.2909 -0.0298 0.1903  0.0314  105 ASP   B C   
5462 C C   B ASP   B 105 ? 0.3735 0.3449 0.3231 -0.0107 0.0604  0.0085  105 ASP   B C   
5463 O O   A ASP   B 105 ? 0.3855 0.3158 0.2898 -0.0269 0.1892  0.0313  105 ASP   B O   
5464 O O   B ASP   B 105 ? 0.3720 0.3430 0.3197 -0.0103 0.0587  0.0059  105 ASP   B O   
5465 C CB  A ASP   B 105 ? 0.4282 0.3902 0.3815 -0.0108 0.2052  0.0166  105 ASP   B CB  
5466 C CB  B ASP   B 105 ? 0.3830 0.3584 0.3621 -0.0100 0.0700  0.0177  105 ASP   B CB  
5467 C CG  A ASP   B 105 ? 0.4378 0.4099 0.4445 -0.0062 0.2151  0.0024  105 ASP   B CG  
5468 C CG  B ASP   B 105 ? 0.3818 0.3590 0.3804 -0.0130 0.0757  0.0192  105 ASP   B CG  
5469 O OD1 A ASP   B 105 ? 0.4375 0.4147 0.4458 -0.0153 0.2315  0.0133  105 ASP   B OD1 
5470 O OD1 B ASP   B 105 ? 0.3801 0.3584 0.3862 -0.0161 0.0772  0.0209  105 ASP   B OD1 
5471 O OD2 A ASP   B 105 ? 0.4438 0.4242 0.4937 0.0017  0.2002  -0.0136 105 ASP   B OD2 
5472 O OD2 B ASP   B 105 ? 0.3798 0.3598 0.3875 -0.0159 0.0806  0.0223  105 ASP   B OD2 
5481 N N   A ILE   B 106 ? 0.3804 0.2972 0.3083 -0.0326 0.1718  0.0196  106 ILE   B N   
5482 N N   B ILE   B 106 ? 0.3654 0.3374 0.3187 -0.0110 0.0545  0.0022  106 ILE   B N   
5483 C CA  A ILE   B 106 ? 0.3611 0.2675 0.3249 -0.0414 0.1731  0.0135  106 ILE   B CA  
5484 C CA  B ILE   B 106 ? 0.3561 0.3299 0.3186 -0.0110 0.0532  -0.0032 106 ILE   B CA  
5485 C C   A ILE   B 106 ? 0.3268 0.2581 0.3099 -0.0420 0.1672  -0.0054 106 ILE   B C   
5486 C C   B ILE   B 106 ? 0.3421 0.3256 0.3162 -0.0098 0.0521  -0.0101 106 ILE   B C   
5487 O O   A ILE   B 106 ? 0.3153 0.2384 0.3092 -0.0486 0.1548  -0.0148 106 ILE   B O   
5488 O O   B ILE   B 106 ? 0.3414 0.3230 0.3127 -0.0113 0.0456  -0.0142 106 ILE   B O   
5489 C CB  A ILE   B 106 ? 0.3836 0.2602 0.3516 -0.0450 0.1637  0.0184  106 ILE   B CB  
5490 C CB  B ILE   B 106 ? 0.3613 0.3294 0.3210 -0.0126 0.0522  -0.0019 106 ILE   B CB  
5491 C CG1 A ILE   B 106 ? 0.3925 0.2609 0.3635 -0.0349 0.1528  0.0108  106 ILE   B CG1 
5492 C CG1 B ILE   B 106 ? 0.3643 0.3296 0.3230 -0.0112 0.0496  -0.0017 106 ILE   B CG1 
5493 C CG2 A ILE   B 106 ? 0.3913 0.2631 0.3795 -0.0527 0.1613  0.0208  106 ILE   B CG2 
5494 C CG2 B ILE   B 106 ? 0.3626 0.3305 0.3288 -0.0140 0.0521  -0.0019 106 ILE   B CG2 
5495 C CD1 A ILE   B 106 ? 0.3993 0.2659 0.3586 -0.0259 0.1512  0.0099  106 ILE   B CD1 
5496 C CD1 B ILE   B 106 ? 0.3665 0.3306 0.3229 -0.0093 0.0492  -0.0009 106 ILE   B CD1 
5519 N N   A GLN   B 107 ? 0.3137 0.2838 0.3304 -0.0422 0.1521  -0.0085 107 GLN   B N   
5520 N N   B GLN   B 107 ? 0.3302 0.3262 0.3272 -0.0093 0.0544  -0.0120 107 GLN   B N   
5521 C CA  A GLN   B 107 ? 0.2987 0.3022 0.3469 -0.0375 0.1379  -0.0030 107 GLN   B CA  
5522 C CA  B GLN   B 107 ? 0.3175 0.3241 0.3405 -0.0065 0.0568  -0.0106 107 GLN   B CA  
5523 C C   A GLN   B 107 ? 0.2719 0.2840 0.3194 -0.0199 0.0984  -0.0118 107 GLN   B C   
5524 C C   B GLN   B 107 ? 0.2869 0.2996 0.3060 -0.0021 0.0642  -0.0146 107 GLN   B C   
5525 O O   A GLN   B 107 ? 0.2606 0.2866 0.3626 -0.0119 0.0699  -0.0254 107 GLN   B O   
5526 O O   B GLN   B 107 ? 0.2865 0.3035 0.3182 -0.0010 0.0560  -0.0173 107 GLN   B O   
5527 C CB  A GLN   B 107 ? 0.3314 0.3469 0.4172 -0.0386 0.1247  0.0039  107 GLN   B CB  
5528 C CB  B GLN   B 107 ? 0.3382 0.3465 0.3883 -0.0067 0.0480  -0.0065 107 GLN   B CB  
5529 C CG  A GLN   B 107 ? 0.3659 0.3878 0.4942 -0.0282 0.0907  0.0072  107 GLN   B CG  
5530 C CG  B GLN   B 107 ? 0.3562 0.3662 0.4379 -0.0037 0.0363  -0.0032 107 GLN   B CG  
5531 C CD  A GLN   B 107 ? 0.3888 0.4134 0.5516 -0.0198 0.0667  0.0109  107 GLN   B CD  
5532 C CD  B GLN   B 107 ? 0.3701 0.3802 0.4763 -0.0007 0.0270  -0.0002 107 GLN   B CD  
5533 O OE1 A GLN   B 107 ? 0.4018 0.4287 0.5760 -0.0094 0.0636  0.0093  107 GLN   B OE1 
5534 O OE1 B GLN   B 107 ? 0.3741 0.3857 0.4911 0.0023  0.0262  0.0005  107 GLN   B OE1 
5535 N NE2 A GLN   B 107 ? 0.3995 0.4235 0.5737 -0.0191 0.0568  0.0178  107 GLN   B NE2 
5536 N NE2 B GLN   B 107 ? 0.3770 0.3842 0.4914 0.0002  0.0235  0.0028  107 GLN   B NE2 
5553 N N   . LEU   B 108 ? 0.2537 0.2696 0.2644 0.0036  0.0777  -0.0136 108 LEU   B N   
5554 C CA  . LEU   B 108 ? 0.2383 0.2427 0.2284 0.0222  0.0557  0.0016  108 LEU   B CA  
5555 C C   . LEU   B 108 ? 0.2062 0.2045 0.2193 0.0212  0.0331  0.0245  108 LEU   B C   
5556 O O   . LEU   B 108 ? 0.2004 0.1910 0.2210 0.0188  0.0262  0.0243  108 LEU   B O   
5557 C CB  . LEU   B 108 ? 0.2553 0.2623 0.2257 0.0190  0.0564  0.0111  108 LEU   B CB  
5558 C CG  . LEU   B 108 ? 0.2758 0.2908 0.2345 0.0249  0.0517  -0.0104 108 LEU   B CG  
5559 C CD1 . LEU   B 108 ? 0.2801 0.3008 0.2192 0.0189  0.0554  -0.0051 108 LEU   B CD1 
5560 C CD2 . LEU   B 108 ? 0.2961 0.3050 0.2528 0.0340  0.0480  -0.0307 108 LEU   B CD2 
5573 N N   . LEU   B 109 ? 0.1930 0.1872 0.2008 0.0139  0.0340  0.0176  109 LEU   B N   
5574 C CA  . LEU   B 109 ? 0.1764 0.1648 0.2167 0.0107  0.0327  0.0260  109 LEU   B CA  
5575 C C   . LEU   B 109 ? 0.1620 0.1449 0.2228 0.0017  0.0369  0.0185  109 LEU   B C   
5576 O O   . LEU   B 109 ? 0.1621 0.1517 0.2170 0.0063  0.0258  0.0256  109 LEU   B O   
5577 C CB  . LEU   B 109 ? 0.1848 0.1515 0.2315 0.0037  0.0237  0.0344  109 LEU   B CB  
5578 C CG  . LEU   B 109 ? 0.1801 0.1469 0.2138 0.0042  0.0223  0.0201  109 LEU   B CG  
5579 C CD1 . LEU   B 109 ? 0.1759 0.1641 0.2157 0.0106  0.0238  0.0156  109 LEU   B CD1 
5580 C CD2 . LEU   B 109 ? 0.1958 0.1539 0.2359 0.0043  0.0120  0.0185  109 LEU   B CD2 
5592 N N   . LYS   B 110 ? 0.1638 0.1486 0.2077 -0.0049 0.0370  0.0232  110 LYS   B N   
5593 C CA  . LYS   B 110 ? 0.1557 0.1428 0.2152 0.0003  0.0237  0.0140  110 LYS   B CA  
5594 C C   . LYS   B 110 ? 0.1531 0.1443 0.2028 -0.0010 0.0224  0.0074  110 LYS   B C   
5595 O O   . LYS   B 110 ? 0.1494 0.1529 0.1915 -0.0020 0.0158  0.0008  110 LYS   B O   
5596 C CB  . LYS   B 110 ? 0.1627 0.1508 0.2400 -0.0010 0.0244  0.0089  110 LYS   B CB  
5597 C CG  . LYS   B 110 ? 0.1654 0.1444 0.2438 -0.0049 0.0139  0.0155  110 LYS   B CG  
5598 C CD  . LYS   B 110 ? 0.1675 0.1392 0.2683 -0.0102 0.0164  0.0082  110 LYS   B CD  
5599 C CE  . LYS   B 110 ? 0.1606 0.1634 0.2793 -0.0091 0.0119  -0.0018 110 LYS   B CE  
5600 N NZ  . LYS   B 110 ? 0.1600 0.1718 0.2676 -0.0043 0.0007  -0.0005 110 LYS   B NZ  
5614 N N   . SER   B 111 ? 0.1654 0.1539 0.2032 -0.0082 0.0282  0.0122  111 SER   B N   
5615 C CA  . SER   B 111 ? 0.1688 0.1596 0.1776 -0.0016 0.0246  0.0095  111 SER   B CA  
5616 C C   . SER   B 111 ? 0.1550 0.1491 0.1919 -0.0047 0.0100  0.0089  111 SER   B C   
5617 O O   . SER   B 111 ? 0.1496 0.1528 0.2039 -0.0035 0.0038  0.0080  111 SER   B O   
5618 C CB  . SER   B 111 ? 0.1786 0.1754 0.2036 0.0029  0.0371  0.0290  111 SER   B CB  
5619 O OG  . SER   B 111 ? 0.1968 0.2202 0.2173 0.0103  0.0474  0.0242  111 SER   B OG  
5625 N N   . ALA   B 112 ? 0.1514 0.1486 0.2049 0.0026  0.0181  0.0172  112 ALA   B N   
5626 C CA  . ALA   B 112 ? 0.1485 0.1534 0.1819 0.0039  0.0049  0.0077  112 ALA   B CA  
5627 C C   . ALA   B 112 ? 0.1380 0.1471 0.1709 -0.0013 0.0095  -0.0008 112 ALA   B C   
5628 O O   . ALA   B 112 ? 0.1417 0.1527 0.1842 -0.0040 0.0060  0.0030  112 ALA   B O   
5629 C CB  . ALA   B 112 ? 0.1599 0.1562 0.2040 0.0100  0.0004  0.0142  112 ALA   B CB  
5635 N N   . TYR   B 113 ? 0.1406 0.1353 0.1919 0.0015  0.0028  0.0081  113 TYR   B N   
5636 C CA  . TYR   B 113 ? 0.1395 0.1377 0.1845 -0.0044 0.0066  0.0001  113 TYR   B CA  
5637 C C   . TYR   B 113 ? 0.1351 0.1313 0.1849 -0.0085 0.0107  0.0085  113 TYR   B C   
5638 O O   . TYR   B 113 ? 0.1403 0.1371 0.1731 -0.0063 0.0040  0.0009  113 TYR   B O   
5639 C CB  . TYR   B 113 ? 0.1447 0.1400 0.1898 -0.0000 0.0197  0.0094  113 TYR   B CB  
5640 C CG  . TYR   B 113 ? 0.1483 0.1425 0.1934 -0.0067 0.0052  0.0130  113 TYR   B CG  
5641 C CD1 . TYR   B 113 ? 0.1539 0.1448 0.2027 -0.0072 0.0059  0.0231  113 TYR   B CD1 
5642 C CD2 . TYR   B 113 ? 0.1519 0.1472 0.1896 -0.0085 0.0036  0.0051  113 TYR   B CD2 
5643 C CE1 . TYR   B 113 ? 0.1543 0.1552 0.1896 -0.0033 0.0113  0.0128  113 TYR   B CE1 
5644 C CE2 . TYR   B 113 ? 0.1614 0.1381 0.1950 0.0018  0.0059  0.0144  113 TYR   B CE2 
5645 C CZ  . TYR   B 113 ? 0.1467 0.1466 0.2020 0.0090  0.0049  0.0096  113 TYR   B CZ  
5646 O OH  . TYR   B 113 ? 0.1601 0.1380 0.2244 0.0089  0.0132  0.0111  113 TYR   B OH  
5656 N N   . GLU   B 114 ? 0.1280 0.1282 0.2004 -0.0050 0.0077  0.0030  114 GLU   B N   
5657 C CA  . GLU   B 114 ? 0.1409 0.1279 0.1870 -0.0017 0.0020  -0.0008 114 GLU   B CA  
5658 C C   . GLU   B 114 ? 0.1436 0.1397 0.1667 0.0039  0.0029  -0.0026 114 GLU   B C   
5659 O O   . GLU   B 114 ? 0.1382 0.1381 0.1866 0.0045  -0.0034 0.0078  114 GLU   B O   
5660 C CB  . GLU   B 114 ? 0.1482 0.1331 0.2047 0.0004  0.0115  0.0038  114 GLU   B CB  
5661 C CG  . GLU   B 114 ? 0.1548 0.1289 0.1988 -0.0010 0.0124  0.0047  114 GLU   B CG  
5662 C CD  . GLU   B 114 ? 0.1442 0.1347 0.1997 -0.0050 0.0063  0.0006  114 GLU   B CD  
5663 O OE1 . GLU   B 114 ? 0.1405 0.1556 0.2014 -0.0059 0.0137  0.0014  114 GLU   B OE1 
5664 O OE2 . GLU   B 114 ? 0.1447 0.1553 0.2214 -0.0208 0.0093  0.0015  114 GLU   B OE2 
5671 N N   . ASN   B 115 ? 0.1527 0.1292 0.1668 -0.0025 -0.0054 -0.0023 115 ASN   B N   
5672 C CA  . ASN   B 115 ? 0.1501 0.1364 0.1465 -0.0068 -0.0061 0.0043  115 ASN   B CA  
5673 C C   . ASN   B 115 ? 0.1376 0.1423 0.1555 -0.0132 -0.0033 -0.0088 115 ASN   B C   
5674 O O   . ASN   B 115 ? 0.1481 0.1423 0.1696 -0.0130 0.0015  -0.0013 115 ASN   B O   
5675 C CB  . ASN   B 115 ? 0.1638 0.1457 0.1615 -0.0046 -0.0020 0.0039  115 ASN   B CB  
5676 C CG  . ASN   B 115 ? 0.1647 0.1585 0.1605 -0.0046 -0.0042 -0.0024 115 ASN   B CG  
5677 O OD1 . ASN   B 115 ? 0.2095 0.1674 0.1876 -0.0052 0.0108  -0.0148 115 ASN   B OD1 
5678 N ND2 . ASN   B 115 ? 0.1566 0.1709 0.1693 -0.0055 0.0040  0.0092  115 ASN   B ND2 
5685 N N   . PHE   B 116 ? 0.1357 0.1474 0.1459 -0.0031 -0.0050 -0.0020 116 PHE   B N   
5686 C CA  . PHE   B 116 ? 0.1440 0.1419 0.1585 -0.0098 -0.0091 -0.0023 116 PHE   B CA  
5687 C C   . PHE   B 116 ? 0.1396 0.1239 0.1722 -0.0127 -0.0045 0.0058  116 PHE   B C   
5688 O O   . PHE   B 116 ? 0.1465 0.1292 0.1749 -0.0022 -0.0071 0.0061  116 PHE   B O   
5689 C CB  . PHE   B 116 ? 0.1410 0.1262 0.1560 -0.0035 -0.0085 0.0057  116 PHE   B CB  
5690 C CG  . PHE   B 116 ? 0.1323 0.1447 0.1561 -0.0071 0.0004  0.0019  116 PHE   B CG  
5691 C CD1 . PHE   B 116 ? 0.1424 0.1479 0.1807 -0.0002 0.0046  -0.0033 116 PHE   B CD1 
5692 C CD2 . PHE   B 116 ? 0.1387 0.1539 0.1579 -0.0019 -0.0031 -0.0104 116 PHE   B CD2 
5693 C CE1 . PHE   B 116 ? 0.1410 0.1474 0.1830 -0.0035 -0.0139 -0.0009 116 PHE   B CE1 
5694 C CE2 . PHE   B 116 ? 0.1428 0.1446 0.1707 -0.0011 -0.0050 0.0035  116 PHE   B CE2 
5695 C CZ  . PHE   B 116 ? 0.1303 0.1470 0.1786 -0.0022 -0.0070 0.0076  116 PHE   B CZ  
5705 N N   . ASN   B 117 ? 0.1443 0.1349 0.1691 -0.0046 -0.0095 -0.0001 117 ASN   B N   
5706 C CA  . ASN   B 117 ? 0.1516 0.1322 0.1768 0.0033  -0.0058 -0.0041 117 ASN   B CA  
5707 C C   . ASN   B 117 ? 0.1527 0.1278 0.1936 -0.0001 -0.0079 0.0022  117 ASN   B C   
5708 O O   . ASN   B 117 ? 0.1599 0.1350 0.2176 -0.0081 -0.0323 0.0076  117 ASN   B O   
5709 C CB  . ASN   B 117 ? 0.1553 0.1351 0.1787 0.0036  -0.0025 -0.0046 117 ASN   B CB  
5710 C CG  . ASN   B 117 ? 0.1496 0.1369 0.1881 0.0026  -0.0029 -0.0089 117 ASN   B CG  
5711 O OD1 . ASN   B 117 ? 0.1659 0.1375 0.2123 -0.0125 -0.0024 -0.0036 117 ASN   B OD1 
5712 N ND2 . ASN   B 117 ? 0.1541 0.1442 0.1826 -0.0025 -0.0040 0.0004  117 ASN   B ND2 
5719 N N   . GLN   B 118 ? 0.1539 0.1228 0.1787 -0.0110 -0.0125 0.0003  118 GLN   B N   
5720 C CA  . GLN   B 118 ? 0.1623 0.1363 0.1874 0.0069  -0.0152 0.0028  118 GLN   B CA  
5721 C C   . GLN   B 118 ? 0.1535 0.1367 0.1959 -0.0006 -0.0048 -0.0068 118 GLN   B C   
5722 O O   . GLN   B 118 ? 0.1680 0.1387 0.2396 -0.0116 0.0058  0.0002  118 GLN   B O   
5723 C CB  . GLN   B 118 ? 0.1696 0.1437 0.1991 0.0029  -0.0103 -0.0017 118 GLN   B CB  
5724 C CG  . GLN   B 118 ? 0.1718 0.1470 0.1941 0.0042  -0.0037 -0.0140 118 GLN   B CG  
5725 C CD  . GLN   B 118 ? 0.1748 0.1364 0.1961 0.0070  -0.0090 -0.0171 118 GLN   B CD  
5726 O OE1 . GLN   B 118 ? 0.1801 0.1411 0.2110 0.0035  0.0068  0.0058  118 GLN   B OE1 
5727 N NE2 . GLN   B 118 ? 0.1791 0.1385 0.2107 0.0082  -0.0185 -0.0032 118 GLN   B NE2 
5736 N N   . HIS   B 119 ? 0.1637 0.1383 0.1611 -0.0067 -0.0080 0.0021  119 HIS   B N   
5737 C CA  . HIS   B 119 ? 0.1709 0.1500 0.1588 -0.0030 -0.0168 0.0052  119 HIS   B CA  
5738 C C   . HIS   B 119 ? 0.1625 0.1441 0.1657 -0.0005 -0.0246 0.0094  119 HIS   B C   
5739 O O   . HIS   B 119 ? 0.1786 0.1445 0.1710 -0.0266 -0.0115 0.0049  119 HIS   B O   
5740 C CB  . HIS   B 119 ? 0.1693 0.1571 0.1879 -0.0011 -0.0236 -0.0041 119 HIS   B CB  
5741 C CG  . HIS   B 119 ? 0.1742 0.1838 0.1908 0.0102  -0.0409 -0.0220 119 HIS   B CG  
5742 N ND1 . HIS   B 119 ? 0.1832 0.1983 0.2341 0.0042  -0.0506 -0.0436 119 HIS   B ND1 
5743 C CD2 . HIS   B 119 ? 0.1902 0.2029 0.2048 0.0334  -0.0478 -0.0279 119 HIS   B CD2 
5744 C CE1 . HIS   B 119 ? 0.2131 0.2126 0.2374 0.0187  -0.0539 -0.0553 119 HIS   B CE1 
5745 N NE2 . HIS   B 119 ? 0.2136 0.2269 0.2260 0.0275  -0.0565 -0.0424 119 HIS   B NE2 
5753 N N   . GLU   B 120 ? 0.1814 0.1412 0.1663 -0.0016 -0.0293 0.0111  120 GLU   B N   
5754 C CA  . GLU   B 120 ? 0.2130 0.1681 0.1712 0.0020  -0.0465 0.0292  120 GLU   B CA  
5755 C C   . GLU   B 120 ? 0.1870 0.1585 0.1641 -0.0115 -0.0293 0.0196  120 GLU   B C   
5756 O O   . GLU   B 120 ? 0.1853 0.1681 0.1678 -0.0113 -0.0284 0.0073  120 GLU   B O   
5757 C CB  . GLU   B 120 ? 0.2767 0.2057 0.2522 0.0295  -0.0741 0.0453  120 GLU   B CB  
5758 C CG  . GLU   B 120 ? 0.3274 0.2503 0.3568 0.0390  -0.0951 0.0656  120 GLU   B CG  
5759 C CD  . GLU   B 120 ? 0.3720 0.3221 0.4737 0.0346  -0.0947 0.0783  120 GLU   B CD  
5760 O OE1 . GLU   B 120 ? 0.4012 0.3530 0.5154 0.0244  -0.0839 0.0881  120 GLU   B OE1 
5761 O OE2 . GLU   B 120 ? 0.4111 0.3629 0.5353 0.0335  -0.0922 0.0684  120 GLU   B OE2 
5768 N N   . VAL   B 121 ? 0.1761 0.1529 0.1584 -0.0173 -0.0156 0.0131  121 VAL   B N   
5769 C CA  . VAL   B 121 ? 0.1757 0.1595 0.1459 -0.0150 -0.0183 0.0077  121 VAL   B CA  
5770 C C   . VAL   B 121 ? 0.1713 0.1521 0.1441 -0.0242 -0.0149 0.0121  121 VAL   B C   
5771 O O   . VAL   B 121 ? 0.1776 0.1481 0.1729 -0.0275 -0.0224 0.0003  121 VAL   B O   
5772 C CB  . VAL   B 121 ? 0.1920 0.2004 0.1610 0.0040  -0.0215 0.0129  121 VAL   B CB  
5773 C CG1 . VAL   B 121 ? 0.1947 0.2128 0.2210 -0.0136 -0.0004 0.0157  121 VAL   B CG1 
5774 C CG2 . VAL   B 121 ? 0.2194 0.2228 0.1678 0.0098  -0.0221 0.0030  121 VAL   B CG2 
5784 N N   . LEU   B 122 ? 0.1612 0.1461 0.1448 -0.0149 -0.0200 0.0081  122 LEU   B N   
5785 C CA  . LEU   B 122 ? 0.1455 0.1599 0.1417 -0.0157 -0.0187 0.0072  122 LEU   B CA  
5786 C C   . LEU   B 122 ? 0.1489 0.1433 0.1425 -0.0203 -0.0127 0.0022  122 LEU   B C   
5787 O O   . LEU   B 122 ? 0.1591 0.1433 0.1734 -0.0243 -0.0178 -0.0057 122 LEU   B O   
5788 C CB  . LEU   B 122 ? 0.1763 0.1688 0.1823 0.0047  -0.0290 0.0032  122 LEU   B CB  
5789 C CG  . LEU   B 122 ? 0.1660 0.1732 0.1801 -0.0125 -0.0138 0.0020  122 LEU   B CG  
5790 C CD1 . LEU   B 122 ? 0.1717 0.1897 0.1863 -0.0137 -0.0216 0.0050  122 LEU   B CD1 
5791 C CD2 . LEU   B 122 ? 0.1740 0.1705 0.1469 -0.0060 -0.0147 -0.0066 122 LEU   B CD2 
5803 N N   . LEU   B 123 ? 0.1561 0.1312 0.1389 -0.0189 -0.0120 0.0052  123 LEU   B N   
5804 C CA  . LEU   B 123 ? 0.1620 0.1357 0.1448 -0.0234 -0.0232 -0.0057 123 LEU   B CA  
5805 C C   . LEU   B 123 ? 0.1586 0.1273 0.1385 -0.0176 -0.0215 -0.0017 123 LEU   B C   
5806 O O   . LEU   B 123 ? 0.1660 0.1374 0.1362 -0.0268 -0.0127 -0.0021 123 LEU   B O   
5807 C CB  . LEU   B 123 ? 0.1600 0.1442 0.1566 -0.0288 -0.0115 0.0066  123 LEU   B CB  
5808 C CG  . LEU   B 123 ? 0.1567 0.1463 0.1728 -0.0164 -0.0029 0.0072  123 LEU   B CG  
5809 C CD1 . LEU   B 123 ? 0.1649 0.1567 0.1789 -0.0150 0.0045  -0.0070 123 LEU   B CD1 
5810 C CD2 . LEU   B 123 ? 0.1733 0.1451 0.1808 -0.0143 -0.0001 0.0220  123 LEU   B CD2 
5822 N N   . ALA   B 124 ? 0.1527 0.1296 0.1442 -0.0140 -0.0119 -0.0008 124 ALA   B N   
5823 C CA  . ALA   B 124 ? 0.1403 0.1363 0.1570 -0.0138 -0.0149 -0.0043 124 ALA   B CA  
5824 C C   . ALA   B 124 ? 0.1413 0.1315 0.1499 -0.0228 -0.0063 0.0015  124 ALA   B C   
5825 O O   . ALA   B 124 ? 0.1526 0.1392 0.1584 -0.0154 -0.0128 -0.0025 124 ALA   B O   
5826 C CB  . ALA   B 124 ? 0.1494 0.1414 0.1614 -0.0004 -0.0006 0.0018  124 ALA   B CB  
5832 N N   . PRO   B 125 ? 0.1531 0.1386 0.1397 -0.0176 -0.0138 0.0103  125 PRO   B N   
5833 C CA  . PRO   B 125 ? 0.1648 0.1444 0.1578 -0.0182 -0.0170 0.0199  125 PRO   B CA  
5834 C C   . PRO   B 125 ? 0.1559 0.1337 0.1651 -0.0186 -0.0154 0.0172  125 PRO   B C   
5835 O O   . PRO   B 125 ? 0.1547 0.1366 0.1971 -0.0100 -0.0095 0.0119  125 PRO   B O   
5836 C CB  . PRO   B 125 ? 0.1639 0.1664 0.1770 -0.0236 -0.0274 0.0312  125 PRO   B CB  
5837 C CG  . PRO   B 125 ? 0.1711 0.1718 0.1703 -0.0358 -0.0275 0.0168  125 PRO   B CG  
5838 C CD  . PRO   B 125 ? 0.1631 0.1546 0.1398 -0.0387 -0.0173 0.0093  125 PRO   B CD  
5846 N N   . LEU   B 126 ? 0.1635 0.1357 0.1866 -0.0171 0.0145  0.0073  126 LEU   B N   
5847 C CA  . LEU   B 126 ? 0.1713 0.1357 0.1952 -0.0107 0.0214  0.0124  126 LEU   B CA  
5848 C C   . LEU   B 126 ? 0.1644 0.1475 0.1893 0.0042  0.0158  0.0149  126 LEU   B C   
5849 O O   . LEU   B 126 ? 0.1777 0.1754 0.2179 0.0168  -0.0056 -0.0091 126 LEU   B O   
5850 C CB  . LEU   B 126 ? 0.1845 0.1433 0.2327 -0.0165 0.0315  -0.0014 126 LEU   B CB  
5851 C CG  . LEU   B 126 ? 0.2043 0.1453 0.2330 -0.0298 0.0265  -0.0186 126 LEU   B CG  
5852 C CD1 . LEU   B 126 ? 0.2193 0.1657 0.2822 -0.0292 0.0170  -0.0227 126 LEU   B CD1 
5853 C CD2 . LEU   B 126 ? 0.2105 0.1595 0.2438 -0.0357 0.0235  -0.0099 126 LEU   B CD2 
5865 N N   . LEU   B 127 ? 0.1631 0.1329 0.2056 0.0012  0.0219  0.0111  127 LEU   B N   
5866 C CA  . LEU   B 127 ? 0.1566 0.1531 0.2049 -0.0018 0.0244  0.0172  127 LEU   B CA  
5867 C C   . LEU   B 127 ? 0.1508 0.1476 0.2077 -0.0016 0.0148  0.0172  127 LEU   B C   
5868 O O   . LEU   B 127 ? 0.1519 0.1508 0.2054 -0.0114 0.0070  0.0152  127 LEU   B O   
5869 C CB  . LEU   B 127 ? 0.1709 0.1509 0.2284 -0.0028 0.0188  0.0235  127 LEU   B CB  
5870 C CG  . LEU   B 127 ? 0.1843 0.1482 0.2294 -0.0002 0.0248  0.0180  127 LEU   B CG  
5871 C CD1 . LEU   B 127 ? 0.1932 0.1511 0.2300 0.0003  0.0125  0.0031  127 LEU   B CD1 
5872 C CD2 . LEU   B 127 ? 0.1848 0.1588 0.2446 -0.0102 0.0261  0.0341  127 LEU   B CD2 
5884 N N   . SER   B 128 ? 0.1547 0.1452 0.2019 0.0035  -0.0000 0.0171  128 SER   B N   
5885 C CA  . SER   B 128 ? 0.1665 0.1522 0.2080 0.0119  -0.0072 0.0168  128 SER   B CA  
5886 C C   . SER   B 128 ? 0.1784 0.1567 0.2351 0.0107  -0.0256 0.0192  128 SER   B C   
5887 O O   . SER   B 128 ? 0.1988 0.1564 0.2743 0.0075  -0.0233 0.0310  128 SER   B O   
5888 C CB  . SER   B 128 ? 0.1774 0.1575 0.2092 0.0079  0.0015  0.0243  128 SER   B CB  
5889 O OG  . SER   B 128 ? 0.1859 0.1684 0.2026 0.0113  0.0129  0.0318  128 SER   B OG  
5895 N N   . ALA   B 129 ? 0.1924 0.1618 0.2449 0.0279  -0.0121 0.0067  129 ALA   B N   
5896 C CA  . ALA   B 129 ? 0.2081 0.1744 0.2646 0.0290  -0.0120 -0.0039 129 ALA   B CA  
5897 C C   . ALA   B 129 ? 0.1928 0.1683 0.2508 0.0208  0.0077  0.0002  129 ALA   B C   
5898 O O   . ALA   B 129 ? 0.1850 0.1686 0.2471 0.0174  -0.0010 0.0109  129 ALA   B O   
5899 C CB  . ALA   B 129 ? 0.2339 0.2008 0.2980 0.0291  -0.0028 -0.0157 129 ALA   B CB  
5905 N N   . GLY   B 130 ? 0.1966 0.1667 0.2501 0.0290  0.0093  -0.0096 130 GLY   B N   
5906 C CA  . GLY   B 130 ? 0.2000 0.1788 0.2584 0.0229  0.0310  -0.0056 130 GLY   B CA  
5907 C C   . GLY   B 130 ? 0.2060 0.1760 0.2484 0.0167  0.0177  0.0029  130 GLY   B C   
5908 O O   . GLY   B 130 ? 0.2224 0.1830 0.2628 0.0147  0.0135  0.0069  130 GLY   B O   
5912 N N   . ILE   B 131 ? 0.1974 0.1870 0.2556 0.0361  0.0138  0.0075  131 ILE   B N   
5913 C CA  . ILE   B 131 ? 0.2163 0.2036 0.2594 0.0299  -0.0038 0.0238  131 ILE   B CA  
5914 C C   . ILE   B 131 ? 0.2267 0.1920 0.2159 0.0182  -0.0026 0.0358  131 ILE   B C   
5915 O O   . ILE   B 131 ? 0.2564 0.2106 0.2235 0.0210  -0.0204 0.0354  131 ILE   B O   
5916 C CB  . ILE   B 131 ? 0.2185 0.2320 0.3091 0.0291  -0.0120 0.0297  131 ILE   B CB  
5917 C CG1 . ILE   B 131 ? 0.2347 0.2452 0.3223 0.0010  -0.0033 0.0366  131 ILE   B CG1 
5918 C CG2 . ILE   B 131 ? 0.2177 0.2491 0.3386 0.0407  -0.0101 0.0149  131 ILE   B CG2 
5919 C CD1 . ILE   B 131 ? 0.2469 0.2589 0.3351 -0.0149 -0.0086 0.0460  131 ILE   B CD1 
5931 N N   . PHE   B 132 ? 0.2104 0.1736 0.2145 0.0151  0.0084  0.0241  132 PHE   B N   
5932 C CA  . PHE   B 132 ? 0.2175 0.1801 0.2045 0.0029  0.0230  0.0132  132 PHE   B CA  
5933 C C   . PHE   B 132 ? 0.2380 0.1968 0.2227 0.0026  0.0374  0.0071  132 PHE   B C   
5934 O O   . PHE   B 132 ? 0.2600 0.2088 0.2663 0.0012  0.0562  0.0190  132 PHE   B O   
5935 C CB  . PHE   B 132 ? 0.1983 0.1763 0.1999 0.0084  0.0275  0.0170  132 PHE   B CB  
5936 C CG  . PHE   B 132 ? 0.1958 0.1827 0.1964 0.0148  0.0245  0.0136  132 PHE   B CG  
5937 C CD1 . PHE   B 132 ? 0.1993 0.1865 0.2323 0.0083  0.0267  0.0220  132 PHE   B CD1 
5938 C CD2 . PHE   B 132 ? 0.1929 0.1856 0.1807 0.0225  0.0173  0.0269  132 PHE   B CD2 
5939 C CE1 . PHE   B 132 ? 0.2010 0.1902 0.2435 0.0104  0.0239  0.0245  132 PHE   B CE1 
5940 C CE2 . PHE   B 132 ? 0.2016 0.1963 0.1957 0.0196  0.0109  0.0166  132 PHE   B CE2 
5941 C CZ  . PHE   B 132 ? 0.2038 0.1946 0.2394 0.0144  -0.0034 0.0340  132 PHE   B CZ  
5951 N N   . GLY   B 133 ? 0.2364 0.1837 0.2119 -0.0052 0.0158  0.0257  133 GLY   B N   
5952 C CA  . GLY   B 133 ? 0.2433 0.1976 0.2351 -0.0245 0.0082  0.0279  133 GLY   B CA  
5953 C C   . GLY   B 133 ? 0.2475 0.2069 0.2352 -0.0316 0.0185  0.0407  133 GLY   B C   
5954 O O   . GLY   B 133 ? 0.2662 0.2169 0.2902 -0.0408 0.0207  0.0529  133 GLY   B O   
5958 N N   . ALA   B 134 ? 0.2340 0.2088 0.2168 -0.0301 0.0240  0.0213  134 ALA   B N   
5959 C CA  . ALA   B 134 ? 0.2324 0.2071 0.2381 -0.0189 0.0353  0.0084  134 ALA   B CA  
5960 C C   . ALA   B 134 ? 0.2339 0.1970 0.2406 -0.0117 0.0349  0.0309  134 ALA   B C   
5961 O O   . ALA   B 134 ? 0.2442 0.2144 0.2590 0.0023  0.0331  0.0272  134 ALA   B O   
5962 C CB  . ALA   B 134 ? 0.2362 0.2031 0.2629 -0.0113 0.0362  -0.0083 134 ALA   B CB  
5968 N N   . ASP   B 135 ? 0.2422 0.1829 0.2482 -0.0171 0.0218  0.0295  135 ASP   B N   
5969 C CA  . ASP   B 135 ? 0.2586 0.1772 0.2660 -0.0116 -0.0019 0.0316  135 ASP   B CA  
5970 C C   . ASP   B 135 ? 0.2319 0.1765 0.2445 -0.0045 -0.0097 0.0288  135 ASP   B C   
5971 O O   . ASP   B 135 ? 0.2209 0.1702 0.2529 -0.0072 -0.0032 0.0303  135 ASP   B O   
5972 C CB  . ASP   B 135 ? 0.2906 0.1853 0.2902 -0.0366 -0.0044 0.0384  135 ASP   B CB  
5973 C CG  . ASP   B 135 ? 0.3203 0.1913 0.3275 -0.0595 0.0008  0.0295  135 ASP   B CG  
5974 O OD1 . ASP   B 135 ? 0.3370 0.1748 0.3253 -0.0379 -0.0084 0.0309  135 ASP   B OD1 
5975 O OD2 . ASP   B 135 ? 0.3450 0.2295 0.3968 -0.0766 0.0067  0.0068  135 ASP   B OD2 
5980 N N   . PRO   B 136 ? 0.2256 0.1784 0.2592 0.0174  -0.0209 0.0220  136 PRO   B N   
5981 C CA  . PRO   B 136 ? 0.2049 0.1653 0.2640 0.0140  -0.0163 0.0146  136 PRO   B CA  
5982 C C   . PRO   B 136 ? 0.1929 0.1606 0.2616 0.0128  -0.0073 0.0087  136 PRO   B C   
5983 O O   . PRO   B 136 ? 0.1721 0.1532 0.2620 0.0084  -0.0081 0.0067  136 PRO   B O   
5984 C CB  . PRO   B 136 ? 0.2053 0.1866 0.2760 0.0278  -0.0262 0.0004  136 PRO   B CB  
5985 C CG  . PRO   B 136 ? 0.2283 0.1973 0.2910 0.0299  -0.0143 -0.0014 136 PRO   B CG  
5986 C CD  . PRO   B 136 ? 0.2306 0.1880 0.2848 0.0352  -0.0107 0.0088  136 PRO   B CD  
5994 N N   . ILE   B 137 ? 0.2059 0.1528 0.2705 0.0116  -0.0058 0.0031  137 ILE   B N   
5995 C CA  . ILE   B 137 ? 0.2124 0.1479 0.2784 0.0002  -0.0023 -0.0007 137 ILE   B CA  
5996 C C   . ILE   B 137 ? 0.2036 0.1497 0.2698 -0.0086 0.0086  0.0135  137 ILE   B C   
5997 O O   . ILE   B 137 ? 0.1951 0.1505 0.2650 -0.0116 0.0025  0.0091  137 ILE   B O   
5998 C CB  . ILE   B 137 ? 0.2359 0.1497 0.3226 -0.0007 -0.0037 -0.0016 137 ILE   B CB  
5999 C CG1 . ILE   B 137 ? 0.2551 0.1781 0.3812 0.0057  0.0080  -0.0146 137 ILE   B CG1 
6000 C CG2 . ILE   B 137 ? 0.2422 0.1537 0.3351 -0.0267 -0.0057 0.0025  137 ILE   B CG2 
6001 C CD1 . ILE   B 137 ? 0.2789 0.2023 0.4207 0.0170  0.0021  0.0009  137 ILE   B CD1 
6013 N N   . HIS   B 138 ? 0.2135 0.1488 0.2666 -0.0037 0.0192  0.0136  138 HIS   B N   
6014 C CA  . HIS   B 138 ? 0.2213 0.1616 0.2589 -0.0056 0.0333  0.0195  138 HIS   B CA  
6015 C C   . HIS   B 138 ? 0.2027 0.1524 0.2447 -0.0094 0.0286  0.0244  138 HIS   B C   
6016 O O   . HIS   B 138 ? 0.1939 0.1657 0.2661 -0.0027 0.0308  0.0369  138 HIS   B O   
6017 C CB  . HIS   B 138 ? 0.2440 0.1760 0.2801 -0.0083 0.0497  0.0209  138 HIS   B CB  
6018 C CG  . HIS   B 138 ? 0.2561 0.1747 0.2908 -0.0071 0.0642  0.0416  138 HIS   B CG  
6019 N ND1 . HIS   B 138 ? 0.2606 0.1976 0.3226 -0.0013 0.0727  0.0284  138 HIS   B ND1 
6020 C CD2 . HIS   B 138 ? 0.2709 0.1867 0.2877 -0.0127 0.0667  0.0328  138 HIS   B CD2 
6021 C CE1 . HIS   B 138 ? 0.2590 0.1906 0.3179 -0.0090 0.0726  0.0350  138 HIS   B CE1 
6022 N NE2 . HIS   B 138 ? 0.2751 0.1892 0.3008 -0.0026 0.0742  0.0296  138 HIS   B NE2 
6030 N N   . SER   B 139 ? 0.1982 0.1330 0.2442 0.0019  0.0218  0.0101  139 SER   B N   
6031 C CA  . SER   B 139 ? 0.1928 0.1351 0.2370 -0.0035 0.0213  0.0103  139 SER   B CA  
6032 C C   . SER   B 139 ? 0.1705 0.1359 0.2257 -0.0004 0.0166  0.0099  139 SER   B C   
6033 O O   . SER   B 139 ? 0.1687 0.1357 0.2422 0.0050  -0.0000 0.0054  139 SER   B O   
6034 C CB  . SER   B 139 ? 0.1934 0.1436 0.2323 0.0005  0.0085  0.0097  139 SER   B CB  
6035 O OG  . SER   B 139 ? 0.1921 0.1452 0.2349 -0.0039 -0.0099 0.0175  139 SER   B OG  
6041 N N   . LEU   B 140 ? 0.1627 0.1287 0.2138 -0.0027 0.0155  -0.0065 140 LEU   B N   
6042 C CA  . LEU   B 140 ? 0.1596 0.1351 0.2145 -0.0012 0.0085  0.0049  140 LEU   B CA  
6043 C C   . LEU   B 140 ? 0.1529 0.1372 0.2373 -0.0044 0.0044  0.0011  140 LEU   B C   
6044 O O   . LEU   B 140 ? 0.1561 0.1391 0.2438 -0.0008 0.0006  0.0015  140 LEU   B O   
6045 C CB  . LEU   B 140 ? 0.1626 0.1376 0.2305 -0.0121 0.0089  -0.0010 140 LEU   B CB  
6046 C CG  . LEU   B 140 ? 0.1684 0.1428 0.2260 -0.0091 0.0063  0.0167  140 LEU   B CG  
6047 C CD1 . LEU   B 140 ? 0.1817 0.1508 0.2545 -0.0151 0.0092  0.0114  140 LEU   B CD1 
6048 C CD2 . LEU   B 140 ? 0.1893 0.1530 0.2342 -0.0045 0.0030  -0.0079 140 LEU   B CD2 
6060 N N   . ARG   B 141 ? 0.1489 0.1375 0.2365 -0.0082 0.0048  0.0049  141 ARG   B N   
6061 C CA  . ARG   B 141 ? 0.1578 0.1401 0.2798 -0.0198 0.0204  0.0002  141 ARG   B CA  
6062 C C   . ARG   B 141 ? 0.1487 0.1330 0.2729 -0.0174 0.0136  -0.0018 141 ARG   B C   
6063 O O   . ARG   B 141 ? 0.1619 0.1376 0.2699 -0.0142 -0.0050 -0.0057 141 ARG   B O   
6064 C CB  . ARG   B 141 ? 0.1756 0.1511 0.3153 -0.0255 0.0379  0.0016  141 ARG   B CB  
6065 C CG  . ARG   B 141 ? 0.2174 0.1778 0.3469 -0.0173 0.0397  0.0053  141 ARG   B CG  
6066 C CD  . ARG   B 141 ? 0.2630 0.1918 0.3592 -0.0125 0.0255  -0.0113 141 ARG   B CD  
6067 N NE  . ARG   B 141 ? 0.2822 0.1925 0.3502 -0.0347 0.0215  -0.0117 141 ARG   B NE  
6068 C CZ  . ARG   B 141 ? 0.2908 0.1864 0.3288 -0.0283 0.0294  -0.0253 141 ARG   B CZ  
6069 N NH1 . ARG   B 141 ? 0.3107 0.1771 0.3107 -0.0266 0.0319  -0.0228 141 ARG   B NH1 
6070 N NH2 . ARG   B 141 ? 0.3007 0.1930 0.3385 -0.0186 0.0117  -0.0195 141 ARG   B NH2 
6084 N N   . VAL   B 142 ? 0.1558 0.1336 0.2511 -0.0092 0.0191  -0.0062 142 VAL   B N   
6085 C CA  . VAL   B 142 ? 0.1561 0.1419 0.2469 -0.0032 0.0198  0.0007  142 VAL   B CA  
6086 C C   . VAL   B 142 ? 0.1507 0.1368 0.2472 -0.0012 0.0158  -0.0061 142 VAL   B C   
6087 O O   . VAL   B 142 ? 0.1601 0.1350 0.2609 -0.0003 0.0163  -0.0053 142 VAL   B O   
6088 C CB  . VAL   B 142 ? 0.1654 0.1480 0.2608 -0.0002 0.0219  0.0119  142 VAL   B CB  
6089 C CG1 . VAL   B 142 ? 0.1678 0.1385 0.2766 0.0122  0.0218  0.0090  142 VAL   B CG1 
6090 C CG2 . VAL   B 142 ? 0.1851 0.1504 0.2595 -0.0003 0.0194  0.0102  142 VAL   B CG2 
6100 N N   . CYS   B 143 ? 0.1458 0.1356 0.2275 -0.0045 0.0066  0.0072  143 CYS   B N   
6101 C CA  . CYS   B 143 ? 0.1437 0.1373 0.2303 -0.0072 0.0011  -0.0051 143 CYS   B CA  
6102 C C   . CYS   B 143 ? 0.1431 0.1428 0.2288 -0.0087 0.0098  -0.0078 143 CYS   B C   
6103 O O   . CYS   B 143 ? 0.1519 0.1458 0.2258 -0.0058 -0.0039 -0.0065 143 CYS   B O   
6104 C CB  . CYS   B 143 ? 0.1464 0.1487 0.2319 -0.0094 0.0040  -0.0057 143 CYS   B CB  
6105 S SG  . CYS   B 143 ? 0.1560 0.1561 0.2385 -0.0030 0.0059  0.0000  143 CYS   B SG  
6111 N N   . VAL   B 144 ? 0.1464 0.1452 0.2438 -0.0079 0.0034  -0.0201 144 VAL   B N   
6112 C CA  . VAL   B 144 ? 0.1539 0.1502 0.2632 -0.0125 -0.0095 -0.0229 144 VAL   B CA  
6113 C C   . VAL   B 144 ? 0.1470 0.1526 0.2710 -0.0107 -0.0116 -0.0093 144 VAL   B C   
6114 O O   . VAL   B 144 ? 0.1562 0.1656 0.2921 -0.0022 -0.0131 0.0152  144 VAL   B O   
6115 C CB  . VAL   B 144 ? 0.1769 0.1685 0.3438 -0.0075 -0.0246 -0.0360 144 VAL   B CB  
6116 C CG1 . VAL   B 144 ? 0.2007 0.2132 0.3792 -0.0114 -0.0233 -0.0301 144 VAL   B CG1 
6117 C CG2 . VAL   B 144 ? 0.1920 0.1616 0.3198 0.0053  -0.0364 -0.0405 144 VAL   B CG2 
6127 N N   . ASP   B 145 ? 0.1513 0.1424 0.2793 -0.0070 -0.0007 -0.0253 145 ASP   B N   
6128 C CA  . ASP   B 145 ? 0.1608 0.1424 0.3057 -0.0077 0.0114  -0.0083 145 ASP   B CA  
6129 C C   . ASP   B 145 ? 0.1577 0.1369 0.2871 -0.0076 0.0169  -0.0113 145 ASP   B C   
6130 O O   . ASP   B 145 ? 0.1600 0.1625 0.3446 -0.0142 0.0128  -0.0235 145 ASP   B O   
6131 C CB  . ASP   B 145 ? 0.1716 0.1569 0.3464 -0.0188 0.0212  0.0014  145 ASP   B CB  
6132 C CG  . ASP   B 145 ? 0.1870 0.1650 0.3912 -0.0222 0.0390  -0.0081 145 ASP   B CG  
6133 O OD1 . ASP   B 145 ? 0.1883 0.1612 0.3982 -0.0220 0.0056  -0.0266 145 ASP   B OD1 
6134 O OD2 . ASP   B 145 ? 0.2131 0.1745 0.4291 -0.0282 0.0576  -0.0012 145 ASP   B OD2 
6139 N N   . THR   B 146 ? 0.1524 0.1414 0.2371 -0.0157 0.0073  -0.0005 146 THR   B N   
6140 C CA  . THR   B 146 ? 0.1557 0.1453 0.2198 -0.0114 0.0077  -0.0032 146 THR   B CA  
6141 C C   . THR   B 146 ? 0.1475 0.1422 0.2243 -0.0040 -0.0024 0.0034  146 THR   B C   
6142 O O   . THR   B 146 ? 0.1539 0.1444 0.2285 -0.0026 -0.0090 0.0018  146 THR   B O   
6143 C CB  . THR   B 146 ? 0.1525 0.1427 0.2358 -0.0057 0.0165  0.0022  146 THR   B CB  
6144 O OG1 . THR   B 146 ? 0.1565 0.1407 0.2429 -0.0065 0.0142  0.0070  146 THR   B OG1 
6145 C CG2 . THR   B 146 ? 0.1611 0.1435 0.2365 -0.0135 0.0151  -0.0095 146 THR   B CG2 
6153 N N   . VAL   B 147 ? 0.1499 0.1407 0.2053 -0.0042 0.0132  0.0026  147 VAL   B N   
6154 C CA  . VAL   B 147 ? 0.1567 0.1341 0.2002 -0.0092 -0.0018 -0.0021 147 VAL   B CA  
6155 C C   . VAL   B 147 ? 0.1498 0.1404 0.2096 -0.0195 -0.0160 -0.0102 147 VAL   B C   
6156 O O   . VAL   B 147 ? 0.1603 0.1616 0.2189 -0.0203 -0.0315 -0.0133 147 VAL   B O   
6157 C CB  . VAL   B 147 ? 0.1600 0.1514 0.1957 -0.0089 -0.0030 0.0032  147 VAL   B CB  
6158 C CG1 . VAL   B 147 ? 0.1585 0.1666 0.1925 -0.0132 -0.0072 0.0083  147 VAL   B CG1 
6159 C CG2 . VAL   B 147 ? 0.1651 0.1468 0.2038 -0.0066 0.0011  0.0035  147 VAL   B CG2 
6169 N N   . ARG   B 148 ? 0.1469 0.1376 0.2101 -0.0059 -0.0173 -0.0102 148 ARG   B N   
6170 C CA  . ARG   B 148 ? 0.1598 0.1447 0.1988 -0.0041 -0.0222 -0.0096 148 ARG   B CA  
6171 C C   . ARG   B 148 ? 0.1667 0.1550 0.1767 -0.0100 -0.0273 -0.0060 148 ARG   B C   
6172 O O   . ARG   B 148 ? 0.1781 0.1868 0.1899 -0.0254 -0.0319 0.0026  148 ARG   B O   
6173 C CB  . ARG   B 148 ? 0.1656 0.1554 0.1984 -0.0033 -0.0287 -0.0129 148 ARG   B CB  
6174 C CG  . ARG   B 148 ? 0.1656 0.1811 0.2116 -0.0107 -0.0284 -0.0316 148 ARG   B CG  
6175 C CD  . ARG   B 148 ? 0.1701 0.1946 0.2244 0.0061  -0.0257 -0.0353 148 ARG   B CD  
6176 N NE  . ARG   B 148 ? 0.1689 0.1926 0.2253 0.0174  -0.0414 -0.0368 148 ARG   B NE  
6177 C CZ  . ARG   B 148 ? 0.1598 0.1846 0.2077 0.0081  -0.0276 -0.0284 148 ARG   B CZ  
6178 N NH1 . ARG   B 148 ? 0.1576 0.1869 0.2061 -0.0062 0.0050  -0.0162 148 ARG   B NH1 
6179 N NH2 . ARG   B 148 ? 0.1753 0.1791 0.2082 0.0127  -0.0215 -0.0186 148 ARG   B NH2 
6193 N N   . THR   B 149 ? 0.1694 0.1467 0.1835 -0.0108 -0.0215 -0.0035 149 THR   B N   
6194 C CA  . THR   B 149 ? 0.1684 0.1594 0.1873 -0.0146 -0.0212 -0.0001 149 THR   B CA  
6195 C C   . THR   B 149 ? 0.1654 0.1579 0.1768 -0.0183 -0.0236 -0.0025 149 THR   B C   
6196 O O   . THR   B 149 ? 0.1730 0.1599 0.1885 -0.0195 -0.0119 -0.0070 149 THR   B O   
6197 C CB  . THR   B 149 ? 0.1698 0.1521 0.1924 -0.0152 -0.0237 -0.0032 149 THR   B CB  
6198 O OG1 . THR   B 149 ? 0.1720 0.1612 0.1836 -0.0252 -0.0258 -0.0013 149 THR   B OG1 
6199 C CG2 . THR   B 149 ? 0.1758 0.1531 0.2086 -0.0013 -0.0122 -0.0036 149 THR   B CG2 
6207 N N   . ASN   B 150 ? 0.1719 0.1476 0.1785 -0.0145 -0.0311 -0.0032 150 ASN   B N   
6208 C CA  . ASN   B 150 ? 0.1794 0.1571 0.1761 -0.0153 -0.0277 -0.0067 150 ASN   B CA  
6209 C C   . ASN   B 150 ? 0.1712 0.1487 0.1823 -0.0092 -0.0257 0.0014  150 ASN   B C   
6210 O O   . ASN   B 150 ? 0.1789 0.1542 0.2024 -0.0272 -0.0395 -0.0031 150 ASN   B O   
6211 C CB  . ASN   B 150 ? 0.2047 0.1909 0.1871 -0.0151 -0.0380 0.0051  150 ASN   B CB  
6212 C CG  . ASN   B 150 ? 0.2316 0.2313 0.2276 -0.0187 -0.0393 0.0244  150 ASN   B CG  
6213 O OD1 . ASN   B 150 ? 0.2381 0.2486 0.2481 -0.0320 -0.0584 0.0203  150 ASN   B OD1 
6214 N ND2 . ASN   B 150 ? 0.2446 0.2551 0.2671 -0.0102 -0.0452 0.0658  150 ASN   B ND2 
6221 N N   . VAL   B 151 ? 0.1644 0.1568 0.1808 -0.0170 -0.0230 0.0039  151 VAL   B N   
6222 C CA  . VAL   B 151 ? 0.1616 0.1625 0.1700 -0.0211 -0.0216 0.0011  151 VAL   B CA  
6223 C C   . VAL   B 151 ? 0.1623 0.1568 0.1766 -0.0286 -0.0302 -0.0034 151 VAL   B C   
6224 O O   . VAL   B 151 ? 0.1723 0.1652 0.1981 -0.0262 -0.0234 -0.0137 151 VAL   B O   
6225 C CB  . VAL   B 151 ? 0.1800 0.1719 0.1910 -0.0083 -0.0223 -0.0053 151 VAL   B CB  
6226 C CG1 . VAL   B 151 ? 0.1879 0.1752 0.2309 -0.0150 -0.0049 -0.0213 151 VAL   B CG1 
6227 C CG2 . VAL   B 151 ? 0.1989 0.1875 0.1701 0.0113  -0.0227 0.0125  151 VAL   B CG2 
6237 N N   . TYR   B 152 ? 0.1603 0.1461 0.1653 -0.0191 -0.0230 -0.0008 152 TYR   B N   
6238 C CA  . TYR   B 152 ? 0.1600 0.1533 0.1668 -0.0228 -0.0133 -0.0089 152 TYR   B CA  
6239 C C   . TYR   B 152 ? 0.1583 0.1372 0.1566 -0.0213 -0.0141 -0.0145 152 TYR   B C   
6240 O O   . TYR   B 152 ? 0.1704 0.1446 0.1572 -0.0243 -0.0112 -0.0046 152 TYR   B O   
6241 C CB  . TYR   B 152 ? 0.1685 0.1619 0.1813 -0.0228 -0.0182 0.0099  152 TYR   B CB  
6242 C CG  . TYR   B 152 ? 0.1892 0.1730 0.1753 -0.0356 -0.0177 0.0046  152 TYR   B CG  
6243 C CD1 . TYR   B 152 ? 0.1978 0.1854 0.1633 -0.0284 -0.0352 0.0110  152 TYR   B CD1 
6244 C CD2 . TYR   B 152 ? 0.2121 0.1921 0.1767 -0.0323 -0.0107 -0.0127 152 TYR   B CD2 
6245 C CE1 . TYR   B 152 ? 0.2153 0.2014 0.1845 -0.0253 -0.0351 0.0276  152 TYR   B CE1 
6246 C CE2 . TYR   B 152 ? 0.2232 0.2085 0.1816 -0.0314 -0.0155 -0.0104 152 TYR   B CE2 
6247 C CZ  . TYR   B 152 ? 0.2210 0.2210 0.1668 -0.0319 -0.0471 0.0170  152 TYR   B CZ  
6248 O OH  . TYR   B 152 ? 0.2447 0.2589 0.2112 -0.0192 -0.0419 0.0116  152 TYR   B OH  
6258 N N   . LEU   B 153 ? 0.1607 0.1364 0.1712 -0.0253 -0.0170 -0.0079 153 LEU   B N   
6259 C CA  . LEU   B 153 ? 0.1758 0.1348 0.1612 -0.0174 -0.0048 -0.0091 153 LEU   B CA  
6260 C C   . LEU   B 153 ? 0.1741 0.1365 0.1653 -0.0176 -0.0043 -0.0100 153 LEU   B C   
6261 O O   . LEU   B 153 ? 0.1772 0.1628 0.1772 -0.0084 -0.0065 -0.0305 153 LEU   B O   
6262 C CB  . LEU   B 153 ? 0.1714 0.1373 0.1781 -0.0245 0.0024  -0.0106 153 LEU   B CB  
6263 C CG  . LEU   B 153 ? 0.1637 0.1429 0.2036 -0.0224 0.0020  -0.0068 153 LEU   B CG  
6264 C CD1 . LEU   B 153 ? 0.1719 0.1629 0.2034 -0.0228 0.0055  0.0005  153 LEU   B CD1 
6265 C CD2 . LEU   B 153 ? 0.1649 0.1582 0.1995 -0.0262 0.0127  -0.0061 153 LEU   B CD2 
6277 N N   . ALA   B 154 ? 0.1640 0.1410 0.1733 -0.0089 -0.0198 -0.0135 154 ALA   B N   
6278 C CA  . ALA   B 154 ? 0.1703 0.1515 0.2003 -0.0025 -0.0214 -0.0157 154 ALA   B CA  
6279 C C   . ALA   B 154 ? 0.1848 0.1528 0.1984 0.0022  -0.0293 -0.0281 154 ALA   B C   
6280 O O   . ALA   B 154 ? 0.2219 0.1528 0.2174 0.0079  -0.0157 -0.0121 154 ALA   B O   
6281 C CB  . ALA   B 154 ? 0.1660 0.1677 0.2309 -0.0049 -0.0207 -0.0249 154 ALA   B CB  
6287 N N   . VAL   B 155 ? 0.1566 0.1432 0.2087 -0.0039 -0.0036 -0.0157 155 VAL   B N   
6288 C CA  . VAL   B 155 ? 0.1566 0.1426 0.2238 -0.0011 -0.0117 -0.0069 155 VAL   B CA  
6289 C C   . VAL   B 155 ? 0.1489 0.1464 0.2099 -0.0022 -0.0103 -0.0181 155 VAL   B C   
6290 O O   . VAL   B 155 ? 0.1675 0.1692 0.2415 0.0037  -0.0071 -0.0295 155 VAL   B O   
6291 C CB  . VAL   B 155 ? 0.1603 0.1601 0.2496 -0.0043 -0.0239 0.0099  155 VAL   B CB  
6292 C CG1 . VAL   B 155 ? 0.1644 0.1577 0.2558 -0.0106 -0.0178 0.0047  155 VAL   B CG1 
6293 C CG2 . VAL   B 155 ? 0.1577 0.1657 0.2825 -0.0088 -0.0208 0.0398  155 VAL   B CG2 
6303 N N   . PHE   B 156 ? 0.1454 0.1522 0.2272 0.0016  -0.0034 -0.0159 156 PHE   B N   
6304 C CA  . PHE   B 156 ? 0.1478 0.1586 0.2629 0.0076  -0.0021 -0.0114 156 PHE   B CA  
6305 C C   . PHE   B 156 ? 0.1463 0.1633 0.2810 0.0088  -0.0122 -0.0322 156 PHE   B C   
6306 O O   . PHE   B 156 ? 0.1815 0.1903 0.3094 0.0211  0.0001  -0.0369 156 PHE   B O   
6307 C CB  . PHE   B 156 ? 0.1628 0.1611 0.2634 0.0002  -0.0137 -0.0159 156 PHE   B CB  
6308 C CG  . PHE   B 156 ? 0.1589 0.1673 0.2728 -0.0011 -0.0183 0.0056  156 PHE   B CG  
6309 C CD1 . PHE   B 156 ? 0.1647 0.1911 0.3167 -0.0004 -0.0011 0.0452  156 PHE   B CD1 
6310 C CD2 . PHE   B 156 ? 0.1697 0.1744 0.2647 0.0081  -0.0273 0.0041  156 PHE   B CD2 
6311 C CE1 . PHE   B 156 ? 0.1690 0.2071 0.3271 0.0037  -0.0013 0.0455  156 PHE   B CE1 
6312 C CE2 . PHE   B 156 ? 0.1735 0.1949 0.2997 0.0127  -0.0218 0.0083  156 PHE   B CE2 
6313 C CZ  . PHE   B 156 ? 0.1667 0.2033 0.3317 0.0128  -0.0182 0.0260  156 PHE   B CZ  
6323 N N   . ASP   B 157 ? 0.1599 0.1515 0.3103 0.0094  -0.0231 -0.0204 157 ASP   B N   
6324 C CA  . ASP   B 157 ? 0.1748 0.1572 0.3451 0.0026  -0.0220 -0.0296 157 ASP   B CA  
6325 C C   . ASP   B 157 ? 0.1710 0.1568 0.3563 0.0095  -0.0244 -0.0500 157 ASP   B C   
6326 O O   . ASP   B 157 ? 0.1567 0.1668 0.3331 0.0095  -0.0221 -0.0423 157 ASP   B O   
6327 C CB  . ASP   B 157 ? 0.1972 0.1803 0.3640 0.0005  -0.0395 -0.0134 157 ASP   B CB  
6328 C CG  . ASP   B 157 ? 0.2359 0.1928 0.3949 -0.0047 -0.0226 -0.0103 157 ASP   B CG  
6329 O OD1 . ASP   B 157 ? 0.2411 0.1883 0.4090 0.0080  -0.0320 -0.0034 157 ASP   B OD1 
6330 O OD2 . ASP   B 157 ? 0.2754 0.2051 0.4290 -0.0058 0.0012  -0.0095 157 ASP   B OD2 
6335 N N   . LYS   B 158 ? 0.1759 0.1835 0.3681 0.0080  -0.0144 -0.0656 158 LYS   B N   
6336 C CA  . LYS   B 158 ? 0.1916 0.1956 0.3809 0.0057  -0.0077 -0.0818 158 LYS   B CA  
6337 C C   . LYS   B 158 ? 0.1867 0.1856 0.3894 0.0093  -0.0146 -0.0748 158 LYS   B C   
6338 O O   . LYS   B 158 ? 0.1845 0.1823 0.3990 -0.0025 -0.0107 -0.0801 158 LYS   B O   
6339 C CB  . LYS   B 158 ? 0.2147 0.2400 0.3908 0.0073  0.0044  -0.1077 158 LYS   B CB  
6340 C CG  . LYS   B 158 ? 0.2503 0.2742 0.4011 0.0125  0.0167  -0.1161 158 LYS   B CG  
6341 C CD  . LYS   B 158 ? 0.2777 0.3137 0.4158 0.0087  0.0248  -0.1032 158 LYS   B CD  
6342 C CE  . LYS   B 158 ? 0.3021 0.3432 0.4277 0.0130  0.0283  -0.0921 158 LYS   B CE  
6343 N NZ  . LYS   B 158 ? 0.2992 0.3534 0.4207 0.0124  0.0352  -0.0899 158 LYS   B NZ  
6357 N N   . ASN   B 159 ? 0.1829 0.1709 0.4037 0.0085  -0.0227 -0.0569 159 ASN   B N   
6358 C CA  . ASN   B 159 ? 0.2003 0.1693 0.4216 0.0177  -0.0358 -0.0365 159 ASN   B CA  
6359 C C   . ASN   B 159 ? 0.1837 0.1574 0.4094 0.0045  -0.0512 -0.0315 159 ASN   B C   
6360 O O   . ASN   B 159 ? 0.1906 0.1411 0.4235 -0.0039 -0.0520 -0.0335 159 ASN   B O   
6361 C CB  . ASN   B 159 ? 0.2168 0.1873 0.4426 0.0269  -0.0390 -0.0295 159 ASN   B CB  
6362 C CG  . ASN   B 159 ? 0.2471 0.2159 0.4685 0.0307  -0.0450 -0.0526 159 ASN   B CG  
6363 O OD1 . ASN   B 159 ? 0.2699 0.2262 0.4846 0.0383  -0.0463 -0.0672 159 ASN   B OD1 
6364 N ND2 . ASN   B 159 ? 0.2483 0.2272 0.4887 0.0314  -0.0536 -0.0606 159 ASN   B ND2 
6371 N N   . LEU   B 160 ? 0.1721 0.1589 0.3838 0.0060  -0.0446 -0.0294 160 LEU   B N   
6372 C CA  . LEU   B 160 ? 0.1723 0.1647 0.3391 0.0087  -0.0326 -0.0187 160 LEU   B CA  
6373 C C   . LEU   B 160 ? 0.1628 0.1535 0.3196 -0.0030 -0.0209 -0.0279 160 LEU   B C   
6374 O O   . LEU   B 160 ? 0.1562 0.1635 0.3021 -0.0012 -0.0281 -0.0159 160 LEU   B O   
6375 C CB  . LEU   B 160 ? 0.1693 0.1665 0.3186 0.0091  -0.0323 -0.0045 160 LEU   B CB  
6376 C CG  . LEU   B 160 ? 0.1696 0.1786 0.2995 0.0075  -0.0333 0.0014  160 LEU   B CG  
6377 C CD1 . LEU   B 160 ? 0.1836 0.2026 0.3129 -0.0011 -0.0267 -0.0044 160 LEU   B CD1 
6378 C CD2 . LEU   B 160 ? 0.1652 0.1831 0.2988 0.0140  -0.0264 -0.0074 160 LEU   B CD2 
6390 N N   . TYR   B 161 ? 0.1532 0.1595 0.3274 -0.0063 0.0013  -0.0374 161 TYR   B N   
6391 C CA  . TYR   B 161 ? 0.1640 0.1608 0.3176 -0.0183 0.0164  -0.0441 161 TYR   B CA  
6392 C C   . TYR   B 161 ? 0.1742 0.1617 0.3050 -0.0061 0.0182  -0.0401 161 TYR   B C   
6393 O O   . TYR   B 161 ? 0.1806 0.1572 0.2908 -0.0136 -0.0000 -0.0325 161 TYR   B O   
6394 C CB  . TYR   B 161 ? 0.1834 0.1760 0.3151 -0.0230 0.0315  -0.0556 161 TYR   B CB  
6395 C CG  . TYR   B 161 ? 0.2040 0.1725 0.3108 -0.0273 0.0433  -0.0587 161 TYR   B CG  
6396 C CD1 . TYR   B 161 ? 0.2105 0.1675 0.3084 -0.0349 0.0438  -0.0531 161 TYR   B CD1 
6397 C CD2 . TYR   B 161 ? 0.2289 0.1849 0.3099 -0.0203 0.0426  -0.0514 161 TYR   B CD2 
6398 C CE1 . TYR   B 161 ? 0.2303 0.1896 0.3117 -0.0419 0.0410  -0.0518 161 TYR   B CE1 
6399 C CE2 . TYR   B 161 ? 0.2472 0.1986 0.3072 -0.0295 0.0392  -0.0464 161 TYR   B CE2 
6400 C CZ  . TYR   B 161 ? 0.2449 0.2003 0.3048 -0.0425 0.0331  -0.0397 161 TYR   B CZ  
6401 O OH  . TYR   B 161 ? 0.2675 0.2238 0.3282 -0.0469 0.0288  -0.0379 161 TYR   B OH  
6411 N N   . ASP   B 162 ? 0.1781 0.1617 0.3127 -0.0071 -0.0023 -0.0529 162 ASP   B N   
6412 C CA  . ASP   B 162 ? 0.1965 0.1718 0.3114 -0.0083 -0.0084 -0.0545 162 ASP   B CA  
6413 C C   . ASP   B 162 ? 0.1937 0.1609 0.3099 -0.0156 -0.0047 -0.0500 162 ASP   B C   
6414 O O   . ASP   B 162 ? 0.1970 0.1663 0.3097 -0.0219 -0.0201 -0.0429 162 ASP   B O   
6415 C CB  . ASP   B 162 ? 0.2119 0.1880 0.3423 0.0011  -0.0175 -0.0681 162 ASP   B CB  
6416 C CG  . ASP   B 162 ? 0.2169 0.2177 0.3686 0.0095  -0.0087 -0.0828 162 ASP   B CG  
6417 O OD1 . ASP   B 162 ? 0.2130 0.2388 0.3542 -0.0010 0.0138  -0.0895 162 ASP   B OD1 
6418 O OD2 . ASP   B 162 ? 0.2377 0.2341 0.4056 0.0244  0.0055  -0.0777 162 ASP   B OD2 
6423 N N   A LYS   B 163 ? 0.1775 0.1443 0.3089 -0.0080 -0.0200 -0.0312 163 LYS   B N   
6424 N N   B LYS   B 163 ? 0.1969 0.1757 0.3118 -0.0132 -0.0110 -0.0347 163 LYS   B N   
6425 C CA  A LYS   B 163 ? 0.1850 0.1501 0.3088 -0.0090 -0.0214 0.0011  163 LYS   B CA  
6426 C CA  B LYS   B 163 ? 0.2010 0.1910 0.3143 -0.0128 -0.0104 -0.0160 163 LYS   B CA  
6427 C C   A LYS   B 163 ? 0.1606 0.1541 0.2959 -0.0202 -0.0187 -0.0040 163 LYS   B C   
6428 C C   B LYS   B 163 ? 0.1735 0.1748 0.2943 -0.0133 -0.0107 -0.0100 163 LYS   B C   
6429 O O   A LYS   B 163 ? 0.1615 0.1534 0.3230 -0.0237 -0.0202 0.0027  163 LYS   B O   
6430 O O   B LYS   B 163 ? 0.1721 0.1733 0.3000 -0.0121 -0.0097 -0.0074 163 LYS   B O   
6431 C CB  A LYS   B 163 ? 0.2290 0.1677 0.3389 -0.0005 -0.0287 0.0223  163 LYS   B CB  
6432 C CB  B LYS   B 163 ? 0.2323 0.2232 0.3469 -0.0128 -0.0116 -0.0091 163 LYS   B CB  
6433 C CG  A LYS   B 163 ? 0.2962 0.2234 0.3905 -0.0048 -0.0135 0.0175  163 LYS   B CG  
6434 C CG  B LYS   B 163 ? 0.2685 0.2635 0.3835 -0.0128 -0.0077 -0.0072 163 LYS   B CG  
6435 C CD  A LYS   B 163 ? 0.3380 0.2705 0.4443 -0.0152 -0.0074 0.0054  163 LYS   B CD  
6436 C CD  B LYS   B 163 ? 0.3003 0.2962 0.4215 -0.0146 -0.0057 -0.0080 163 LYS   B CD  
6437 C CE  A LYS   B 163 ? 0.3888 0.3039 0.4796 -0.0251 -0.0036 0.0019  163 LYS   B CE  
6438 C CE  B LYS   B 163 ? 0.3141 0.3017 0.4513 -0.0174 -0.0046 -0.0068 163 LYS   B CE  
6439 N NZ  A LYS   B 163 ? 0.4294 0.3372 0.5004 -0.0298 -0.0029 -0.0030 163 LYS   B NZ  
6440 N NZ  B LYS   B 163 ? 0.3331 0.3237 0.4679 -0.0186 -0.0047 -0.0072 163 LYS   B NZ  
6467 N N   . LEU   B 164 ? 0.1495 0.1573 0.2698 -0.0118 -0.0131 -0.0025 164 LEU   B N   
6468 C CA  . LEU   B 164 ? 0.1538 0.1578 0.2588 -0.0118 -0.0229 -0.0017 164 LEU   B CA  
6469 C C   . LEU   B 164 ? 0.1576 0.1558 0.2633 -0.0116 -0.0225 -0.0018 164 LEU   B C   
6470 O O   . LEU   B 164 ? 0.1603 0.1718 0.2810 -0.0157 -0.0218 -0.0055 164 LEU   B O   
6471 C CB  . LEU   B 164 ? 0.1472 0.1488 0.2448 -0.0122 -0.0239 -0.0065 164 LEU   B CB  
6472 C CG  . LEU   B 164 ? 0.1676 0.1552 0.2633 -0.0098 -0.0081 -0.0043 164 LEU   B CG  
6473 C CD1 . LEU   B 164 ? 0.1683 0.1577 0.2605 -0.0203 -0.0229 -0.0139 164 LEU   B CD1 
6474 C CD2 . LEU   B 164 ? 0.1839 0.1882 0.2709 -0.0114 0.0032  -0.0240 164 LEU   B CD2 
6487 N N   . VAL   B 165 ? 0.1903 0.1576 0.2754 -0.0270 -0.0341 -0.0073 165 VAL   B N   
6488 C CA  . VAL   B 165 ? 0.2222 0.1732 0.2714 -0.0319 -0.0520 -0.0113 165 VAL   B CA  
6489 C C   . VAL   B 165 ? 0.2528 0.1834 0.2960 -0.0374 -0.0843 -0.0133 165 VAL   B C   
6490 O O   . VAL   B 165 ? 0.2723 0.1990 0.3088 -0.0435 -0.0857 -0.0110 165 VAL   B O   
6491 C CB  . VAL   B 165 ? 0.2461 0.1965 0.2716 -0.0154 -0.0178 -0.0180 165 VAL   B CB  
6492 C CG1 . VAL   B 165 ? 0.2629 0.2022 0.3066 -0.0168 -0.0029 -0.0135 165 VAL   B CG1 
6493 C CG2 . VAL   B 165 ? 0.2396 0.1981 0.2699 -0.0117 -0.0191 -0.0166 165 VAL   B CG2 
6503 N N   . SER   B 166 ? 0.2663 0.1680 0.3333 -0.0384 -0.0857 -0.0318 166 SER   B N   
6504 C CA  . SER   B 166 ? 0.2648 0.1748 0.3882 -0.0343 -0.0729 -0.0364 166 SER   B CA  
6505 C C   . SER   B 166 ? 0.2462 0.1780 0.4155 -0.0388 -0.0750 -0.0054 166 SER   B C   
6506 O O   . SER   B 166 ? 0.2476 0.1986 0.4471 -0.0485 -0.1034 -0.0253 166 SER   B O   
6507 C CB  . SER   B 166 ? 0.2630 0.1787 0.4173 -0.0264 -0.0612 -0.0338 166 SER   B CB  
6508 O OG  . SER   B 166 ? 0.2498 0.1768 0.4356 -0.0207 -0.0692 -0.0137 166 SER   B OG  
6514 N N   . SER   B 167 ? 0.2242 0.1767 0.3943 -0.0437 -0.0709 0.0305  167 SER   B N   
6515 C CA  . SER   B 167 ? 0.2144 0.1921 0.3747 -0.0330 -0.0555 0.0338  167 SER   B CA  
6516 C C   . SER   B 167 ? 0.2051 0.2028 0.3611 -0.0490 -0.0548 0.0491  167 SER   B C   
6517 O O   . SER   B 167 ? 0.2090 0.2104 0.3636 -0.0582 -0.0506 0.0471  167 SER   B O   
6518 C CB  . SER   B 167 ? 0.2021 0.1996 0.3725 -0.0331 -0.0348 0.0280  167 SER   B CB  
6519 O OG  . SER   B 167 ? 0.1955 0.2009 0.3490 -0.0312 -0.0181 0.0314  167 SER   B OG  
6525 N N   . PHE   B 168 ? 0.2034 0.1935 0.3472 -0.0422 -0.0353 0.0585  168 PHE   B N   
6526 C CA  . PHE   B 168 ? 0.2113 0.1854 0.3263 -0.0445 -0.0370 0.0355  168 PHE   B CA  
6527 C C   . PHE   B 168 ? 0.1901 0.1664 0.2718 -0.0267 -0.0134 0.0127  168 PHE   B C   
6528 O O   . PHE   B 168 ? 0.2191 0.1619 0.2767 -0.0052 -0.0130 -0.0043 168 PHE   B O   
6529 C CB  . PHE   B 168 ? 0.2321 0.1883 0.3372 -0.0550 -0.0477 0.0480  168 PHE   B CB  
6530 C CG  . PHE   B 168 ? 0.2613 0.1736 0.3218 -0.0559 -0.0440 0.0343  168 PHE   B CG  
6531 C CD1 . PHE   B 168 ? 0.2971 0.1910 0.3304 -0.0511 -0.0572 0.0346  168 PHE   B CD1 
6532 C CD2 . PHE   B 168 ? 0.2575 0.1618 0.3180 -0.0510 -0.0469 0.0280  168 PHE   B CD2 
6533 C CE1 . PHE   B 168 ? 0.3153 0.1944 0.3269 -0.0392 -0.0513 0.0424  168 PHE   B CE1 
6534 C CE2 . PHE   B 168 ? 0.2847 0.1712 0.3233 -0.0362 -0.0573 0.0233  168 PHE   B CE2 
6535 C CZ  . PHE   B 168 ? 0.3020 0.1747 0.3205 -0.0310 -0.0645 0.0422  168 PHE   B CZ  
6545 N N   . LEU   B 169 ? 0.1960 0.1835 0.2637 -0.0033 -0.0002 -0.0041 169 LEU   B N   
6546 C CA  . LEU   B 169 ? 0.2208 0.2141 0.3066 -0.0103 -0.0062 -0.0336 169 LEU   B CA  
6547 C C   . LEU   B 169 ? 0.2516 0.2418 0.3646 0.0059  -0.0094 -0.0627 169 LEU   B C   
6548 O O   . LEU   B 169 ? 0.2790 0.2628 0.4192 0.0010  -0.0159 -0.0862 169 LEU   B O   
6549 C CB  . LEU   B 169 ? 0.2396 0.2602 0.3139 -0.0164 -0.0162 0.0004  169 LEU   B CB  
6550 C CG  . LEU   B 169 ? 0.2806 0.3016 0.3625 -0.0023 -0.0034 0.0121  169 LEU   B CG  
6551 C CD1 . LEU   B 169 ? 0.2996 0.3215 0.3705 -0.0018 -0.0089 0.0263  169 LEU   B CD1 
6552 C CD2 . LEU   B 169 ? 0.2752 0.3126 0.3657 0.0150  0.0165  0.0027  169 LEU   B CD2 
6553 O OXT . LEU   B 169 ? 0.2704 0.2521 0.3638 0.0378  0.0067  -0.0642 169 LEU   B OXT 
6565 C C1  T TFA   C .   ? 0.1712 0.1725 0.1438 -0.0199 0.0256  0.0085  201 TFA   A C1  
6566 C C2  T TFA   C .   ? 0.1916 0.1988 0.1763 -0.0220 0.0176  -0.0030 201 TFA   A C2  
6567 O O   T TFA   C .   ? 0.1485 0.1453 0.1371 -0.0235 0.0368  0.0155  201 TFA   A O   
6568 F F1  T TFA   C .   ? 0.2010 0.2024 0.2103 -0.0243 0.0093  -0.0112 201 TFA   A F1  
6569 F F2  T TFA   C .   ? 0.1954 0.2083 0.1755 -0.0182 0.0185  0.0132  201 TFA   A F2  
6570 F F3  T TFA   C .   ? 0.2042 0.2186 0.2028 -0.0272 0.0311  -0.0138 201 TFA   A F3  
6571 O OXT T TFA   C .   ? 0.1747 0.1698 0.1577 -0.0074 0.0286  0.0084  201 TFA   A OXT 
6572 N N2  B A1A65 D .   ? 0.1814 0.1701 0.1943 0.0132  0.0032  0.0046  202 A1A65 A N2  
6573 C C3  B A1A65 D .   ? 0.2335 0.2250 0.2585 -0.0077 -0.0315 0.0006  202 A1A65 A C3  
6574 C C6  B A1A65 D .   ? 0.2131 0.2017 0.2726 0.0053  0.0094  0.0060  202 A1A65 A C6  
6575 C C9  B A1A65 D .   ? 0.1814 0.1749 0.1862 0.0125  0.0106  0.0059  202 A1A65 A C9  
6576 C C12 B A1A65 D .   ? 0.1942 0.1562 0.1907 0.0034  -0.0108 -0.0014 202 A1A65 A C12 
6577 C C1  B A1A65 D .   ? 0.2316 0.2292 0.2675 -0.0114 -0.0250 0.0004  202 A1A65 A C1  
6578 C C10 B A1A65 D .   ? 0.1762 0.1611 0.1726 0.0132  -0.0036 0.0027  202 A1A65 A C10 
6579 C C11 B A1A65 D .   ? 0.1876 0.1611 0.1826 0.0102  -0.0081 -0.0002 202 A1A65 A C11 
6580 C C13 B A1A65 D .   ? 0.1738 0.1476 0.1826 0.0006  -0.0127 0.0128  202 A1A65 A C13 
6581 C C2  B A1A65 D .   ? 0.2314 0.2242 0.2581 -0.0083 -0.0271 -0.0001 202 A1A65 A C2  
6582 C C4  B A1A65 D .   ? 0.2192 0.2059 0.2578 0.0011  -0.0135 0.0117  202 A1A65 A C4  
6583 C C5  B A1A65 D .   ? 0.2179 0.2062 0.2687 0.0017  -0.0036 0.0122  202 A1A65 A C5  
6584 C C7  B A1A65 D .   ? 0.2104 0.1952 0.2569 0.0095  0.0126  0.0086  202 A1A65 A C7  
6585 C C8  B A1A65 D .   ? 0.1908 0.1690 0.2045 0.0132  -0.0066 0.0066  202 A1A65 A C8  
6586 N N1  B A1A65 D .   ? 0.2077 0.1868 0.2369 0.0105  -0.0035 0.0138  202 A1A65 A N1  
6587 N N3  B A1A65 D .   ? 0.1815 0.1725 0.1732 0.0108  0.0101  0.0048  202 A1A65 A N3  
6588 N N4  B A1A65 D .   ? 0.1693 0.1489 0.1816 0.0083  -0.0129 0.0169  202 A1A65 A N4  
6589 O O1  B A1A65 D .   ? 0.2371 0.2329 0.2613 -0.0133 -0.0340 -0.0083 202 A1A65 A O1  
6608 O O   . HOH   E .   ? 0.3310 0.2603 0.3798 -0.0357 -0.0230 0.0518  301 HOH   A O   
6609 O O   . HOH   E .   ? 0.4245 0.7915 0.5008 -0.1273 0.0341  0.0944  302 HOH   A O   
6610 O O   . HOH   E .   ? 0.3062 0.1935 0.2400 0.0036  0.0358  0.0032  303 HOH   A O   
6611 O O   . HOH   E .   ? 0.6680 0.4777 0.3861 0.1963  -0.1362 0.0621  304 HOH   A O   
6612 O O   . HOH   E .   ? 0.4893 0.3626 0.4778 -0.0346 0.1363  -0.0363 305 HOH   A O   
6613 O O   . HOH   E .   ? 0.2970 0.6536 0.6036 -0.0387 -0.0622 0.2070  306 HOH   A O   
6614 O O   . HOH   E .   ? 0.3023 0.2881 0.4469 -0.0286 -0.1301 0.1227  307 HOH   A O   
6615 O O   . HOH   E .   ? 0.5824 0.3587 0.5088 -0.0563 0.1629  0.1018  308 HOH   A O   
6616 O O   . HOH   E .   ? 0.3088 0.3557 0.1914 -0.0283 0.0650  0.0563  309 HOH   A O   
6617 O O   . HOH   E .   ? 0.2788 0.5501 0.4320 -0.0162 -0.0565 0.0946  310 HOH   A O   
6618 O O   B HOH   E .   ? 0.2322 0.3563 0.1861 0.0657  -0.0937 0.0305  311 HOH   A O   
6619 O O   . HOH   E .   ? 0.6726 0.5556 0.3869 -0.0254 -0.0755 0.1161  312 HOH   A O   
6620 O O   . HOH   E .   ? 0.2323 0.2024 0.3970 -0.0439 0.0123  -0.0170 313 HOH   A O   
6621 O O   . HOH   E .   ? 0.7371 0.5662 0.4820 -0.1074 0.0551  0.2091  314 HOH   A O   
6622 O O   . HOH   E .   ? 0.5149 0.4324 0.5431 0.0341  0.1747  -0.1488 315 HOH   A O   
6623 O O   . HOH   E .   ? 0.6603 0.5385 0.4901 -0.1294 0.0474  0.2375  316 HOH   A O   
6624 O O   . HOH   E .   ? 0.3941 0.3345 0.4227 -0.0677 0.1813  0.0110  317 HOH   A O   
6625 O O   . HOH   E .   ? 0.3234 0.3087 0.2953 -0.0965 0.0116  0.0781  318 HOH   A O   
6626 O O   . HOH   E .   ? 0.5403 0.4992 0.4928 -0.0741 0.1338  0.1924  319 HOH   A O   
6627 O O   . HOH   E .   ? 0.5116 0.3796 0.3231 -0.1042 -0.0683 -0.0157 320 HOH   A O   
6628 O O   . HOH   E .   ? 0.1956 0.3376 0.2941 0.0310  -0.0274 -0.0237 321 HOH   A O   
6629 O O   . HOH   E .   ? 0.2274 0.1935 0.2595 0.0246  -0.0298 0.0024  322 HOH   A O   
6630 O O   . HOH   E .   ? 0.1934 0.1909 0.2304 0.0148  -0.0195 0.0252  323 HOH   A O   
6631 O O   . HOH   E .   ? 0.3734 0.4499 0.2489 -0.0094 0.0660  0.0247  324 HOH   A O   
6632 O O   . HOH   E .   ? 0.4468 0.5682 0.5110 0.1467  0.1205  -0.0797 325 HOH   A O   
6633 O O   . HOH   E .   ? 0.2436 0.4843 0.4368 -0.0110 -0.0619 0.1892  326 HOH   A O   
6634 O O   . HOH   E .   ? 0.1754 0.3827 0.2660 -0.0009 0.0287  0.0611  327 HOH   A O   
6635 O O   . HOH   E .   ? 0.2382 0.1930 0.2447 -0.0046 -0.0577 -0.0001 328 HOH   A O   
6636 O O   . HOH   E .   ? 0.5833 0.5059 0.5394 0.0614  0.2536  -0.0807 329 HOH   A O   
6637 O O   . HOH   E .   ? 0.1690 0.1699 0.2231 -0.0207 0.0061  0.0052  330 HOH   A O   
6638 O O   . HOH   E .   ? 0.2152 0.3273 0.4753 -0.0371 0.0463  -0.1091 331 HOH   A O   
6639 O O   . HOH   E .   ? 0.5585 0.6094 0.4696 -0.1144 -0.1188 -0.0937 332 HOH   A O   
6640 O O   . HOH   E .   ? 0.2815 0.5716 0.7222 0.0668  0.1049  0.0321  333 HOH   A O   
6641 O O   . HOH   E .   ? 0.8903 0.4196 0.5849 -0.0799 -0.1484 0.0913  334 HOH   A O   
6642 O O   . HOH   E .   ? 0.3244 0.3807 0.3983 -0.0814 -0.0804 -0.0399 335 HOH   A O   
6643 O O   . HOH   E .   ? 0.6146 0.2155 0.5356 0.0811  -0.0260 -0.0047 336 HOH   A O   
6644 O O   . HOH   E .   ? 0.2651 0.2266 0.3097 0.0295  0.0269  0.0303  337 HOH   A O   
6645 O O   A HOH   E .   ? 0.2432 0.3083 0.2524 0.0706  0.0162  -0.0185 338 HOH   A O   
6646 O O   . HOH   E .   ? 0.6631 0.4196 0.6162 0.0737  -0.0477 0.0043  339 HOH   A O   
6647 O O   . HOH   E .   ? 0.2664 0.2331 0.2938 0.0048  -0.0012 0.0719  340 HOH   A O   
6648 O O   . HOH   E .   ? 0.2231 0.1822 0.1655 -0.0074 0.0253  0.0188  341 HOH   A O   
6649 O O   . HOH   E .   ? 0.5034 0.2195 0.4874 0.0436  -0.1684 0.0556  342 HOH   A O   
6650 O O   . HOH   E .   ? 0.4941 0.4755 0.4310 -0.2260 -0.0929 0.2063  343 HOH   A O   
6651 O O   A HOH   E .   ? 0.2286 0.3368 0.4617 -0.0107 0.0938  0.1738  344 HOH   A O   
6652 O O   . HOH   E .   ? 0.2212 0.2377 0.2723 -0.0099 -0.0170 0.0841  345 HOH   A O   
6653 O O   . HOH   E .   ? 0.5184 0.5654 0.2796 -0.1285 0.1108  0.1223  346 HOH   A O   
6654 O O   . HOH   E .   ? 0.2520 0.4317 0.3906 0.1070  -0.0581 -0.0200 347 HOH   A O   
6655 O O   . HOH   E .   ? 0.5415 0.5049 0.4493 0.0045  -0.0564 -0.1049 348 HOH   A O   
6656 O O   A HOH   E .   ? 0.1471 0.2456 0.1958 0.0245  0.0247  0.0323  349 HOH   A O   
6657 O O   . HOH   E .   ? 0.2871 0.2263 0.2580 -0.0468 0.0077  -0.0213 350 HOH   A O   
6658 O O   . HOH   E .   ? 0.5656 0.4007 0.3187 0.0253  0.0584  0.1270  351 HOH   A O   
6659 O O   . HOH   E .   ? 0.1645 0.2405 0.2414 -0.0015 -0.0020 0.0575  352 HOH   A O   
6660 O O   . HOH   E .   ? 0.1577 0.1887 0.2824 0.0077  -0.0320 -0.0643 353 HOH   A O   
6661 O O   . HOH   E .   ? 0.3670 0.3181 0.3911 -0.1056 -0.0193 -0.0260 354 HOH   A O   
6662 O O   . HOH   E .   ? 0.2779 0.4249 0.3538 -0.0319 0.0550  -0.0011 355 HOH   A O   
6663 O O   . HOH   E .   ? 0.3134 0.3687 0.2605 -0.0744 -0.0223 -0.0789 356 HOH   A O   
6664 O O   . HOH   E .   ? 0.3723 0.4342 0.4573 0.1642  0.0662  0.0455  357 HOH   A O   
6665 O O   . HOH   E .   ? 0.1488 0.1459 0.1329 -0.0048 0.0128  0.0066  358 HOH   A O   
6666 O O   . HOH   E .   ? 0.2219 0.2156 0.4124 0.0107  0.1040  -0.0034 359 HOH   A O   
6667 O O   . HOH   E .   ? 0.2257 0.2109 0.2470 -0.0401 0.0003  0.0244  360 HOH   A O   
6668 O O   . HOH   E .   ? 0.2251 0.2224 0.3395 0.0010  -0.0530 0.0334  361 HOH   A O   
6669 O O   . HOH   E .   ? 0.3223 0.3368 0.5170 -0.0618 -0.1106 -0.0884 362 HOH   A O   
6670 O O   . HOH   E .   ? 0.5548 0.2861 0.4198 -0.1716 0.1824  -0.0557 363 HOH   A O   
6671 O O   . HOH   E .   ? 0.1628 0.2002 0.2698 0.0098  -0.0156 0.0086  364 HOH   A O   
6672 O O   . HOH   E .   ? 0.4110 0.2641 0.4574 -0.1245 0.0663  0.0284  365 HOH   A O   
6673 O O   . HOH   E .   ? 0.1741 0.1457 0.2271 -0.0108 0.0214  -0.0111 366 HOH   A O   
6674 O O   . HOH   E .   ? 0.1625 0.1754 0.1494 -0.0056 -0.0069 -0.0026 367 HOH   A O   
6675 O O   . HOH   E .   ? 0.2948 0.4146 0.2758 0.0394  0.0745  0.1394  368 HOH   A O   
6676 O O   . HOH   E .   ? 0.2172 0.2619 0.2330 -0.0451 -0.0424 0.0483  369 HOH   A O   
6677 O O   . HOH   E .   ? 0.3361 0.4766 0.5427 0.1444  0.0732  0.0745  370 HOH   A O   
6678 O O   A HOH   E .   ? 0.2357 0.2418 0.2405 -0.0575 0.0304  0.0525  371 HOH   A O   
6679 O O   . HOH   E .   ? 0.1927 0.2267 0.2079 -0.0132 0.0099  0.0613  372 HOH   A O   
6680 O O   . HOH   E .   ? 0.1973 0.2728 0.3154 -0.0230 0.0687  0.0508  373 HOH   A O   
6681 O O   . HOH   E .   ? 0.4087 0.7070 0.4775 -0.0555 -0.1515 0.0742  374 HOH   A O   
6682 O O   . HOH   E .   ? 0.2210 0.2095 0.1870 0.0093  0.0132  0.0174  375 HOH   A O   
6683 O O   . HOH   E .   ? 0.2274 0.2778 0.3639 0.0255  0.0871  -0.0703 376 HOH   A O   
6684 O O   . HOH   E .   ? 0.4263 0.2326 0.2223 0.1343  0.0450  0.0200  377 HOH   A O   
6685 O O   . HOH   E .   ? 0.1846 0.1838 0.2297 -0.0243 0.0056  0.0331  378 HOH   A O   
6686 O O   . HOH   E .   ? 0.3137 0.2797 0.3597 -0.0159 -0.0638 0.0887  379 HOH   A O   
6687 O O   . HOH   E .   ? 0.3651 0.2538 0.5244 -0.0668 -0.0355 0.0067  380 HOH   A O   
6688 O O   . HOH   E .   ? 0.3196 0.2962 0.2224 0.0370  0.0794  0.0020  381 HOH   A O   
6689 O O   T HOH   E .   ? 0.1270 0.1428 0.2134 -0.0241 0.0234  0.0102  382 HOH   A O   
6690 O O   . HOH   E .   ? 0.3282 0.3709 0.4687 -0.0429 0.1548  -0.0083 383 HOH   A O   
6691 O O   . HOH   E .   ? 0.3025 0.3453 0.3612 -0.1138 0.0914  -0.0159 384 HOH   A O   
6692 O O   . HOH   E .   ? 0.7277 0.4652 0.5231 -0.0344 0.0936  0.1212  385 HOH   A O   
6693 O O   . HOH   E .   ? 0.2843 0.2159 0.2027 -0.0734 0.0076  0.0238  386 HOH   A O   
6694 O O   . HOH   E .   ? 0.1547 0.1972 0.1871 0.0140  -0.0256 -0.0383 387 HOH   A O   
6695 O O   . HOH   E .   ? 0.3276 0.6795 0.3770 0.0953  0.0588  -0.1218 388 HOH   A O   
6696 O O   . HOH   E .   ? 0.2680 0.2097 0.2742 -0.0127 0.0165  0.0322  389 HOH   A O   
6697 O O   . HOH   E .   ? 0.2932 0.3572 0.3759 -0.0346 0.1078  -0.0566 390 HOH   A O   
6698 O O   . HOH   E .   ? 0.3393 0.6592 0.4034 -0.0757 0.0114  0.1137  391 HOH   A O   
6699 O O   . HOH   E .   ? 0.2462 0.4149 0.3345 -0.0370 -0.0030 0.0654  392 HOH   A O   
6700 O O   A HOH   E .   ? 0.2285 0.2099 0.3455 -0.0142 0.0411  -0.0101 393 HOH   A O   
6701 O O   . HOH   E .   ? 0.3431 0.2860 0.2514 -0.0737 -0.1046 0.0268  394 HOH   A O   
6702 O O   . HOH   E .   ? 0.2337 0.1954 0.3085 0.0034  -0.0357 0.0024  395 HOH   A O   
6703 O O   . HOH   E .   ? 0.2505 0.2519 0.3971 -0.0010 -0.0223 -0.0480 396 HOH   A O   
6704 O O   A HOH   E .   ? 0.3162 0.2250 0.3273 0.1027  0.0241  0.0515  397 HOH   A O   
6705 O O   . HOH   E .   ? 0.2135 0.2790 0.3758 -0.0271 -0.0248 0.0238  398 HOH   A O   
6706 O O   . HOH   E .   ? 0.5696 0.5301 0.6143 -0.1099 -0.0271 0.1182  399 HOH   A O   
6707 O O   B HOH   E .   ? 0.3395 0.3116 0.4733 -0.0366 0.0979  -0.0012 400 HOH   A O   
6708 O O   . HOH   E .   ? 0.5099 0.5557 0.5607 -0.0448 0.1050  -0.0165 401 HOH   A O   
6709 O O   . HOH   E .   ? 0.3696 0.3868 0.2507 0.0130  -0.0949 0.0223  402 HOH   A O   
6710 O O   . HOH   E .   ? 0.5475 0.3073 0.3355 -0.1112 0.0658  0.0358  403 HOH   A O   
6711 O O   . HOH   E .   ? 0.5543 0.4002 0.2135 -0.0330 0.0902  0.0546  404 HOH   A O   
6712 O O   . HOH   E .   ? 0.1819 0.1873 0.1956 0.0018  -0.0307 -0.0026 405 HOH   A O   
6713 O O   . HOH   E .   ? 0.6535 0.6259 0.4287 0.2428  -0.0467 -0.0406 406 HOH   A O   
6714 O O   . HOH   E .   ? 0.6008 0.3304 0.4939 0.0945  -0.0330 -0.0296 407 HOH   A O   
6715 O O   B HOH   E .   ? 0.1485 0.1496 0.3398 -0.0304 -0.0171 0.0035  408 HOH   A O   
6716 O O   . HOH   E .   ? 0.1507 0.1622 0.1908 -0.0002 -0.0126 -0.0005 409 HOH   A O   
6717 O O   . HOH   E .   ? 0.4197 0.6331 0.5376 0.1274  -0.0055 0.1002  410 HOH   A O   
6718 O O   . HOH   E .   ? 0.1990 0.2014 0.3949 0.0358  0.0968  0.0941  411 HOH   A O   
6719 O O   . HOH   E .   ? 0.2620 0.3231 0.3362 -0.0043 -0.0177 -0.0430 412 HOH   A O   
6720 O O   . HOH   E .   ? 0.2970 0.3856 0.7165 -0.0227 0.1184  -0.0515 413 HOH   A O   
6721 O O   . HOH   E .   ? 0.1858 0.1606 0.1683 -0.0173 0.0149  -0.0036 414 HOH   A O   
6722 O O   . HOH   E .   ? 0.5933 0.6755 0.5557 0.0339  0.0984  0.0160  415 HOH   A O   
6723 O O   . HOH   E .   ? 0.4541 0.6503 0.3598 -0.0933 -0.0104 0.1206  416 HOH   A O   
6724 O O   . HOH   E .   ? 0.2717 0.2014 0.2782 -0.0554 -0.0061 0.0577  417 HOH   A O   
6725 O O   . HOH   E .   ? 0.1619 0.1759 0.3108 0.0011  0.0007  0.0174  418 HOH   A O   
6726 O O   . HOH   E .   ? 0.6824 0.4059 0.5388 0.1692  -0.0739 0.1710  419 HOH   A O   
6727 O O   . HOH   E .   ? 0.4315 0.2358 0.5572 -0.0862 -0.2493 0.0989  420 HOH   A O   
6728 O O   . HOH   E .   ? 0.3001 0.6040 0.1836 -0.0385 0.0436  0.0093  421 HOH   A O   
6729 O O   . HOH   E .   ? 0.3465 0.1420 0.2306 0.0015  -0.0530 0.0151  422 HOH   A O   
6730 O O   B HOH   E .   ? 0.2537 0.4730 0.3172 0.1503  -0.0898 0.0044  423 HOH   A O   
6731 O O   . HOH   E .   ? 0.4518 0.3414 0.4751 0.1435  0.0788  0.0281  424 HOH   A O   
6732 O O   . HOH   E .   ? 0.4336 0.4660 0.3756 0.1454  -0.0687 -0.1472 425 HOH   A O   
6733 O O   . HOH   E .   ? 0.2778 0.3313 0.3252 -0.0280 0.1045  -0.0309 426 HOH   A O   
6734 O O   . HOH   E .   ? 0.2364 0.3029 0.2716 -0.0082 -0.0708 0.0525  427 HOH   A O   
6735 O O   . HOH   E .   ? 0.2371 0.4367 0.2697 0.1529  -0.0152 0.0030  428 HOH   A O   
6736 O O   . HOH   E .   ? 0.6204 0.7776 0.4475 0.0572  0.2926  -0.0781 429 HOH   A O   
6737 O O   . HOH   E .   ? 0.6061 0.6762 0.6515 -0.1084 -0.0751 -0.0856 430 HOH   A O   
6738 O O   . HOH   E .   ? 0.1774 0.2122 0.2919 -0.0214 -0.0009 0.0383  431 HOH   A O   
6739 O O   A HOH   E .   ? 0.2032 0.1743 0.2498 0.0177  -0.0458 0.0095  432 HOH   A O   
6740 O O   B HOH   E .   ? 0.4321 0.2291 0.2693 0.0265  0.0268  0.0547  433 HOH   A O   
6741 O O   . HOH   E .   ? 0.3910 0.3079 0.2512 -0.0460 -0.0404 0.0171  434 HOH   A O   
6742 O O   . HOH   E .   ? 0.6144 0.5020 0.3841 -0.0507 -0.1497 0.0368  435 HOH   A O   
6743 O O   . HOH   E .   ? 0.2226 0.1905 0.1888 -0.0059 -0.0194 -0.0024 436 HOH   A O   
6744 O O   . HOH   E .   ? 0.3906 0.2840 0.2020 -0.0876 0.0088  0.0416  437 HOH   A O   
6745 O O   B HOH   E .   ? 0.2382 0.1143 0.1700 -0.0617 0.1018  -0.0500 438 HOH   A O   
6746 O O   . HOH   E .   ? 0.7007 0.6879 0.6419 0.0972  -0.1242 0.0097  439 HOH   A O   
6747 O O   . HOH   E .   ? 0.5399 0.5180 0.5868 0.1209  0.0805  -0.1033 440 HOH   A O   
6748 O O   . HOH   E .   ? 0.6448 0.7200 0.4253 0.2065  -0.0904 0.1823  441 HOH   A O   
6749 O O   . HOH   E .   ? 0.9518 0.9820 0.7380 -0.0198 -0.0473 -0.0583 442 HOH   A O   
6750 O O   . HOH   E .   ? 0.2675 0.1808 0.2765 0.0063  0.0197  0.0115  443 HOH   A O   
6751 O O   . HOH   E .   ? 0.3109 0.3522 0.5186 0.0019  0.0790  -0.1433 444 HOH   A O   
6752 O O   . HOH   E .   ? 0.4377 0.3870 0.3339 0.2335  -0.0574 -0.0448 445 HOH   A O   
6753 O O   . HOH   E .   ? 0.5231 0.5867 0.6249 -0.1651 -0.0232 -0.1266 446 HOH   A O   
6754 O O   . HOH   E .   ? 0.1956 0.2398 0.5740 -0.0296 -0.0918 0.0901  447 HOH   A O   
6755 O O   . HOH   E .   ? 0.2308 0.3047 0.2535 0.0073  -0.0108 -0.0592 448 HOH   A O   
6756 O O   . HOH   E .   ? 0.2521 0.2113 0.2895 0.0196  0.0389  0.0089  449 HOH   A O   
6757 O O   A HOH   E .   ? 0.6749 0.4680 0.3872 0.1757  0.1510  0.1697  450 HOH   A O   
6758 O O   . HOH   E .   ? 0.4387 0.4652 0.5335 -0.1271 -0.0880 -0.1203 451 HOH   A O   
6759 O O   A HOH   E .   ? 0.1805 0.2086 0.1714 0.0107  -0.0218 -0.0057 452 HOH   A O   
6760 O O   B HOH   E .   ? 0.3480 0.3180 0.2703 -0.0279 0.0746  0.0670  453 HOH   A O   
6761 O O   . HOH   E .   ? 0.6389 0.5609 0.7889 0.1107  -0.1177 0.1819  454 HOH   A O   
6762 O O   . HOH   E .   ? 0.5937 0.3408 0.4516 -0.0012 0.0068  0.1251  455 HOH   A O   
6763 O O   . HOH   E .   ? 0.4394 0.4433 0.4725 0.1098  -0.0003 0.0888  456 HOH   A O   
6764 O O   . HOH   E .   ? 0.6596 0.6065 0.4767 -0.0790 0.0997  0.0545  457 HOH   A O   
6765 O O   . HOH   E .   ? 0.4725 0.3954 0.4743 0.0156  -0.0003 0.0749  458 HOH   A O   
6766 O O   . HOH   E .   ? 0.3402 0.3516 0.4271 0.1259  -0.0484 0.0527  459 HOH   A O   
6767 O O   . HOH   E .   ? 0.3195 0.2701 0.3526 -0.0455 0.0380  -0.0683 460 HOH   A O   
6768 O O   . HOH   E .   ? 0.7176 0.8327 0.5099 0.0040  -0.1025 -0.0190 461 HOH   A O   
6769 O O   . HOH   E .   ? 0.3167 0.4897 0.5822 -0.1331 0.0910  -0.1823 462 HOH   A O   
6770 O O   . HOH   E .   ? 0.3499 0.5581 0.5063 0.0390  -0.1006 0.1505  463 HOH   A O   
6771 O O   . HOH   E .   ? 0.3309 0.4640 0.4363 0.0032  -0.0205 -0.0043 464 HOH   A O   
6772 O O   . HOH   E .   ? 0.3382 0.2729 0.6828 0.0997  -0.1459 -0.0382 465 HOH   A O   
6773 O O   . HOH   E .   ? 0.2753 0.2872 0.3774 -0.0877 0.0465  -0.0674 466 HOH   A O   
6774 O O   . HOH   E .   ? 0.2810 0.4461 0.5745 0.0576  -0.0083 -0.2090 467 HOH   A O   
6775 O O   . HOH   E .   ? 0.4302 0.6250 0.3924 -0.0871 -0.0805 0.2081  468 HOH   A O   
6776 O O   . HOH   E .   ? 0.7445 0.3301 0.7725 0.0257  0.0649  0.2157  469 HOH   A O   
6777 O O   . HOH   E .   ? 0.2917 0.2057 0.2701 0.0342  -0.0950 -0.0235 470 HOH   A O   
6778 O O   . HOH   E .   ? 0.5871 0.5258 0.5120 0.0122  0.1198  0.0409  471 HOH   A O   
6779 O O   . HOH   E .   ? 0.3345 0.2882 0.4099 0.0260  0.0692  -0.0052 472 HOH   A O   
6780 O O   . HOH   E .   ? 0.6666 0.5573 0.6165 0.1235  0.2418  0.2548  473 HOH   A O   
6781 O O   . HOH   E .   ? 0.4252 0.5564 0.3775 0.0166  -0.0192 -0.0716 474 HOH   A O   
6782 O O   . HOH   E .   ? 0.4904 0.4839 0.3514 -0.0576 -0.0494 -0.0196 475 HOH   A O   
6783 O O   . HOH   E .   ? 0.5530 0.6266 0.6130 -0.1800 -0.0890 0.0171  476 HOH   A O   
6784 O O   . HOH   E .   ? 0.4730 0.4538 0.5561 -0.1927 -0.0281 -0.0359 477 HOH   A O   
6785 O O   . HOH   E .   ? 0.4394 0.5175 0.2839 -0.0142 -0.0037 0.0025  478 HOH   A O   
6786 O O   . HOH   E .   ? 0.5533 0.5860 0.5391 0.1476  -0.0876 -0.0948 479 HOH   A O   
6787 O O   . HOH   E .   ? 0.6817 0.6108 0.7039 -0.1191 0.0599  -0.0749 480 HOH   A O   
6788 O O   . HOH   E .   ? 0.8262 0.3838 0.3391 -0.0367 -0.1290 0.0226  481 HOH   A O   
6789 O O   . HOH   E .   ? 0.5982 0.3592 0.4327 0.0345  0.0371  -0.1169 482 HOH   A O   
6790 O O   . HOH   E .   ? 0.2550 0.2454 0.2737 0.0062  0.0015  -0.0079 483 HOH   A O   
6791 O O   . HOH   E .   ? 0.5245 0.2852 0.3725 -0.0811 -0.1260 0.0739  484 HOH   A O   
6792 O O   B HOH   E .   ? 0.1455 0.1694 0.2837 0.0296  -0.0404 0.0912  485 HOH   A O   
6793 O O   . HOH   E .   ? 0.6093 0.4142 0.4511 -0.0088 0.1267  -0.0040 486 HOH   A O   
6794 O O   . HOH   E .   ? 0.3043 0.4979 0.3653 -0.0109 -0.0388 -0.0909 487 HOH   A O   
6795 O O   . HOH   E .   ? 0.2803 0.6018 0.3644 0.1270  0.0927  0.2454  488 HOH   A O   
6796 O O   . HOH   E .   ? 0.6316 0.6731 0.4846 -0.0542 0.1281  0.1431  489 HOH   A O   
6797 O O   . HOH   E .   ? 0.2729 0.3963 0.5053 0.0141  0.1127  0.0963  490 HOH   A O   
6798 O O   . HOH   E .   ? 0.4112 0.3923 0.3050 -0.0926 0.1297  -0.0808 491 HOH   A O   
6799 O O   . HOH   E .   ? 0.5481 0.5747 0.5685 -0.0135 -0.1106 0.0256  492 HOH   A O   
6800 O O   . HOH   E .   ? 0.5532 0.6081 0.6823 0.1023  0.1433  -0.1074 493 HOH   A O   
6801 O O   . HOH   E .   ? 0.2655 0.2867 0.7578 -0.0313 -0.1604 0.0389  494 HOH   A O   
6802 O O   . HOH   E .   ? 0.4813 0.3375 0.5268 -0.0322 0.2492  0.0059  495 HOH   A O   
6803 O O   . HOH   E .   ? 0.6183 0.5266 0.4922 -0.0803 -0.0667 -0.0789 496 HOH   A O   
6804 O O   . HOH   E .   ? 0.4527 0.3217 0.4786 -0.1054 0.0630  0.0581  497 HOH   A O   
6805 O O   . HOH   E .   ? 0.2777 0.2388 0.5838 -0.0029 0.0038  0.0917  498 HOH   A O   
6806 O O   . HOH   E .   ? 0.2779 0.3298 0.4727 -0.0049 0.0893  -0.0388 499 HOH   A O   
6807 O O   . HOH   E .   ? 0.4380 0.8356 0.5695 -0.0923 -0.0355 0.2485  500 HOH   A O   
6808 O O   . HOH   E .   ? 0.6494 0.2932 0.4889 -0.0868 0.0351  0.0862  501 HOH   A O   
6809 O O   . HOH   E .   ? 0.2494 0.3448 0.3900 0.0403  -0.0653 0.0793  502 HOH   A O   
6810 O O   . HOH   E .   ? 0.7436 0.6532 0.4890 0.2246  -0.1320 0.0672  503 HOH   A O   
6811 O O   . HOH   E .   ? 0.4916 0.2658 0.4689 -0.1247 -0.0009 0.0379  504 HOH   A O   
6812 O O   . HOH   E .   ? 0.3021 0.4334 0.4102 0.0379  -0.0499 0.0098  505 HOH   A O   
6813 O O   . HOH   E .   ? 0.6252 0.6974 0.5267 0.1556  -0.0804 0.0412  506 HOH   A O   
6814 O O   . HOH   E .   ? 0.7729 0.4939 0.5620 -0.0115 -0.0128 0.0629  507 HOH   A O   
6815 O O   . HOH   E .   ? 0.4021 0.8132 0.4829 0.1418  0.1845  -0.0542 508 HOH   A O   
6816 O O   . HOH   E .   ? 0.3127 0.2393 0.4666 0.0256  0.0314  0.0618  509 HOH   A O   
6817 O O   . HOH   E .   ? 0.5063 0.7286 0.4699 0.2903  0.0156  0.1561  510 HOH   A O   
6818 O O   B HOH   E .   ? 0.2899 0.1827 0.2534 0.0320  -0.0469 0.0312  511 HOH   A O   
6819 O O   T HOH   E .   ? 0.1535 0.1247 0.2178 -0.0470 -0.0194 0.0415  512 HOH   A O   
6820 O O   . HOH   E .   ? 0.5274 0.5673 0.4674 -0.0438 -0.0501 -0.1520 513 HOH   A O   
6821 O O   . HOH   E .   ? 0.2847 0.7277 0.3974 0.0469  0.0310  -0.0331 514 HOH   A O   
6822 O O   . HOH   E .   ? 0.4826 0.4923 0.4318 0.1133  0.0142  0.1012  515 HOH   A O   
6823 O O   . HOH   E .   ? 0.4768 0.6763 0.5544 -0.0768 -0.0657 -0.0152 516 HOH   A O   
6824 O O   . HOH   E .   ? 0.3350 0.4761 0.5895 -0.0179 -0.0958 0.2786  517 HOH   A O   
6825 O O   . HOH   F .   ? 0.2516 0.2406 0.3242 0.0233  0.0875  0.0328  201 HOH   B O   
6826 O O   . HOH   F .   ? 0.6439 0.5848 0.6168 0.1890  0.0875  0.0360  202 HOH   B O   
6827 O O   . HOH   F .   ? 0.5790 0.5462 0.3459 0.0684  -0.0253 -0.1532 203 HOH   B O   
6828 O O   . HOH   F .   ? 0.4357 0.3343 0.4003 -0.0471 0.0025  -0.1110 204 HOH   B O   
6829 O O   . HOH   F .   ? 0.7491 0.3550 0.4846 0.0738  0.1494  0.0126  205 HOH   B O   
6830 O O   . HOH   F .   ? 0.4228 0.4649 0.5618 -0.1104 -0.0044 -0.1512 206 HOH   B O   
6831 O O   . HOH   F .   ? 0.3962 0.7028 0.4050 0.0252  -0.0079 0.2697  207 HOH   B O   
6832 O O   . HOH   F .   ? 0.4907 0.6218 0.4214 0.2881  -0.1281 -0.0156 208 HOH   B O   
6833 O O   . HOH   F .   ? 0.3527 0.3883 0.6532 -0.0632 0.0180  -0.0471 209 HOH   B O   
6834 O O   . HOH   F .   ? 0.2055 0.2538 0.3377 -0.0088 0.0195  -0.0021 210 HOH   B O   
6835 O O   . HOH   F .   ? 0.3263 0.2081 0.5800 0.0172  0.2033  0.0680  211 HOH   B O   
6836 O O   . HOH   F .   ? 0.2906 0.5298 0.5621 0.0007  0.1660  -0.1804 212 HOH   B O   
6837 O O   . HOH   F .   ? 0.4728 0.3999 0.6386 0.0458  -0.0889 0.2615  213 HOH   B O   
6838 O O   . HOH   F .   ? 0.2924 0.2907 0.7012 0.0557  -0.1081 0.0697  214 HOH   B O   
6839 O O   . HOH   F .   ? 0.1672 0.2075 0.2894 -0.0175 0.0008  0.0007  215 HOH   B O   
6840 O O   . HOH   F .   ? 0.4800 0.4857 0.4131 0.0352  0.0690  -0.1489 216 HOH   B O   
6841 O O   . HOH   F .   ? 0.4744 0.5242 0.3833 0.2491  -0.0440 0.0287  217 HOH   B O   
6842 O O   . HOH   F .   ? 0.5823 0.3330 0.4566 -0.1703 0.0102  0.0210  218 HOH   B O   
6843 O O   . HOH   F .   ? 0.5058 0.2158 0.3731 -0.0045 -0.0871 0.0057  219 HOH   B O   
6844 O O   . HOH   F .   ? 0.4639 0.4740 0.6461 -0.0118 -0.1737 -0.0769 220 HOH   B O   
6845 O O   . HOH   F .   ? 0.4149 0.3645 0.5659 0.0320  -0.0895 0.0234  221 HOH   B O   
6846 O O   . HOH   F .   ? 0.3897 0.5629 0.4581 0.2319  0.0152  -0.0551 222 HOH   B O   
6847 O O   . HOH   F .   ? 0.4804 0.4312 0.3903 -0.0268 -0.0921 0.0812  223 HOH   B O   
6848 O O   . HOH   F .   ? 0.3120 0.3415 0.5757 -0.0277 0.0527  -0.0162 224 HOH   B O   
6849 O O   . HOH   F .   ? 0.3962 0.4014 0.5498 -0.1611 -0.0003 0.0717  225 HOH   B O   
6850 O O   . HOH   F .   ? 0.4649 0.7580 0.3756 0.2878  0.0243  0.0091  226 HOH   B O   
6851 O O   . HOH   F .   ? 0.3116 0.2480 0.4747 -0.0149 0.1397  0.0127  227 HOH   B O   
6852 O O   . HOH   F .   ? 0.2667 0.1900 0.3123 -0.0310 0.1140  0.0071  228 HOH   B O   
6853 O O   . HOH   F .   ? 0.1804 0.2258 0.2999 -0.0094 0.0054  -0.0044 229 HOH   B O   
6854 O O   . HOH   F .   ? 0.2560 0.2285 0.3892 -0.0257 -0.0135 -0.0634 230 HOH   B O   
6855 O O   . HOH   F .   ? 0.6724 0.4117 0.4946 0.1454  -0.0075 -0.1051 231 HOH   B O   
6856 O O   . HOH   F .   ? 0.3869 0.1961 0.2440 0.0075  -0.0788 -0.0127 232 HOH   B O   
6857 O O   . HOH   F .   ? 0.5489 0.7028 0.3207 0.0811  -0.0356 0.0647  233 HOH   B O   
6858 O O   . HOH   F .   ? 0.2436 0.3711 0.3420 -0.0390 -0.0607 -0.0529 234 HOH   B O   
6859 O O   . HOH   F .   ? 0.2744 0.3905 0.3684 -0.0755 -0.0013 0.0443  235 HOH   B O   
6860 O O   . HOH   F .   ? 0.3837 0.3723 0.2231 0.0378  0.0655  0.0512  236 HOH   B O   
6861 O O   . HOH   F .   ? 0.2377 0.4121 0.2410 -0.0387 -0.0290 0.0702  237 HOH   B O   
6862 O O   . HOH   F .   ? 0.1730 0.1539 0.1723 -0.0152 -0.0093 0.0014  238 HOH   B O   
6863 O O   . HOH   F .   ? 0.4641 0.3722 0.3680 -0.1042 0.0664  -0.0732 239 HOH   B O   
6864 O O   . HOH   F .   ? 0.3840 0.2732 0.4601 0.0426  -0.0862 -0.1171 240 HOH   B O   
6865 O O   . HOH   F .   ? 0.2278 0.1385 0.3423 0.0060  -0.0581 -0.0183 241 HOH   B O   
6866 O O   . HOH   F .   ? 0.3207 0.2903 0.3197 0.0638  0.0013  -0.1043 242 HOH   B O   
6867 O O   . HOH   F .   ? 0.5314 0.3183 0.4160 -0.2193 -0.0308 0.0166  243 HOH   B O   
6868 O O   . HOH   F .   ? 0.3751 0.2805 0.4293 0.0716  -0.0539 -0.0748 244 HOH   B O   
6869 O O   . HOH   F .   ? 0.1701 0.1626 0.2729 -0.0051 -0.0041 -0.0195 245 HOH   B O   
6870 O O   . HOH   F .   ? 0.2998 0.2520 0.3097 0.0950  0.0642  0.0198  246 HOH   B O   
6871 O O   . HOH   F .   ? 0.2189 0.2339 0.4154 0.0091  -0.0530 -0.0494 247 HOH   B O   
6872 O O   . HOH   F .   ? 0.2308 0.2537 0.3270 -0.0545 0.0060  -0.0316 248 HOH   B O   
6873 O O   . HOH   F .   ? 0.1571 0.1508 0.1629 -0.0046 -0.0082 0.0042  249 HOH   B O   
6874 O O   . HOH   F .   ? 0.3328 0.1773 0.6343 -0.0180 -0.1242 -0.0129 250 HOH   B O   
6875 O O   . HOH   F .   ? 0.2272 0.1568 0.2181 -0.0256 -0.0311 0.0219  251 HOH   B O   
6876 O O   . HOH   F .   ? 0.2491 0.2174 0.2266 -0.0344 -0.0562 0.0119  252 HOH   B O   
6877 O O   . HOH   F .   ? 0.2998 0.4305 0.3638 -0.1111 -0.0265 -0.0728 253 HOH   B O   
6878 O O   . HOH   F .   ? 0.4958 0.3409 0.2992 0.0608  0.1076  -0.0159 254 HOH   B O   
6879 O O   . HOH   F .   ? 0.3377 0.3702 0.2365 0.0342  0.0719  0.0099  255 HOH   B O   
6880 O O   . HOH   F .   ? 0.1622 0.1826 0.2132 -0.0059 0.0119  0.0133  256 HOH   B O   
6881 O O   . HOH   F .   ? 0.1743 0.1779 0.2974 -0.0164 -0.0216 0.0038  257 HOH   B O   
6882 O O   . HOH   F .   ? 0.2612 0.3329 0.2452 -0.0525 0.0455  0.0384  258 HOH   B O   
6883 O O   . HOH   F .   ? 0.3682 0.4618 0.3473 -0.0563 -0.1249 0.0950  259 HOH   B O   
6884 O O   . HOH   F .   ? 0.2784 0.5072 0.5518 0.1584  -0.0797 -0.1138 260 HOH   B O   
6885 O O   . HOH   F .   ? 0.2552 0.2408 0.2556 0.0822  -0.0772 -0.0732 261 HOH   B O   
6886 O O   . HOH   F .   ? 0.1990 0.2818 0.2837 0.0423  0.0379  0.1002  262 HOH   B O   
6887 O O   . HOH   F .   ? 0.2633 0.3239 0.3621 -0.0433 0.0385  -0.1047 263 HOH   B O   
6888 O O   . HOH   F .   ? 0.2654 0.2194 0.2041 0.0127  -0.0142 -0.0025 264 HOH   B O   
6889 O O   . HOH   F .   ? 0.2306 0.2357 0.2187 0.0137  -0.0063 -0.0018 265 HOH   B O   
6890 O O   . HOH   F .   ? 0.3071 0.2682 0.3185 -0.0267 0.0171  -0.0516 266 HOH   B O   
6891 O O   . HOH   F .   ? 0.2503 0.4028 0.3689 0.0362  0.0898  0.0401  267 HOH   B O   
6892 O O   . HOH   F .   ? 0.2644 0.4741 0.6366 0.0368  0.0276  -0.0999 268 HOH   B O   
6893 O O   . HOH   F .   ? 0.1942 0.1583 0.4276 -0.0055 -0.0341 0.0002  269 HOH   B O   
6894 O O   . HOH   F .   ? 0.2214 0.1638 0.2230 -0.0232 -0.0213 0.0060  270 HOH   B O   
6895 O O   . HOH   F .   ? 0.4348 0.3856 0.4747 0.0093  -0.1062 -0.0703 271 HOH   B O   
6896 O O   . HOH   F .   ? 0.2678 0.3154 0.2811 -0.0424 -0.0933 0.0014  272 HOH   B O   
6897 O O   . HOH   F .   ? 0.2998 0.2106 0.3132 -0.0664 0.0236  -0.0144 273 HOH   B O   
6898 O O   . HOH   F .   ? 0.2094 0.1910 0.1568 -0.0405 -0.0357 0.0054  274 HOH   B O   
6899 O O   . HOH   F .   ? 0.2690 0.3400 0.5677 -0.0137 0.0023  -0.1569 275 HOH   B O   
6900 O O   . HOH   F .   ? 0.4987 0.3828 0.3026 0.0693  -0.0018 -0.1097 276 HOH   B O   
6901 O O   . HOH   F .   ? 0.2797 0.2773 0.2562 -0.0539 -0.0850 -0.0368 277 HOH   B O   
6902 O O   . HOH   F .   ? 0.2608 0.3380 0.2473 0.0815  -0.0229 -0.0150 278 HOH   B O   
6903 O O   . HOH   F .   ? 0.3649 0.3798 0.5015 0.1216  -0.0844 -0.0993 279 HOH   B O   
6904 O O   . HOH   F .   ? 0.2245 0.4313 0.5146 -0.0431 -0.0234 -0.1748 280 HOH   B O   
6905 O O   . HOH   F .   ? 0.1849 0.1622 0.1849 -0.0016 0.0045  -0.0004 281 HOH   B O   
6906 O O   . HOH   F .   ? 0.2878 0.2342 0.4960 0.0136  0.0500  0.0444  282 HOH   B O   
6907 O O   . HOH   F .   ? 0.2600 0.2729 0.2985 0.0247  -0.0686 0.0228  283 HOH   B O   
6908 O O   . HOH   F .   ? 0.3726 0.2300 0.4477 -0.0874 -0.2004 0.0882  284 HOH   B O   
6909 O O   . HOH   F .   ? 0.3440 0.7222 0.3463 0.1584  -0.0478 0.0667  285 HOH   B O   
6910 O O   . HOH   F .   ? 0.1749 0.1669 0.3451 -0.0132 0.0105  0.0007  286 HOH   B O   
6911 O O   . HOH   F .   ? 0.3893 0.2879 0.2344 0.0441  -0.0740 -0.0013 287 HOH   B O   
6912 O O   . HOH   F .   ? 0.2723 0.5202 0.4873 -0.0957 -0.1180 0.0937  288 HOH   B O   
6913 O O   . HOH   F .   ? 0.2752 0.7383 0.2941 0.0836  -0.0336 -0.0534 289 HOH   B O   
6914 O O   . HOH   F .   ? 0.3230 0.2911 0.5096 -0.0221 -0.0694 0.1226  290 HOH   B O   
6915 O O   . HOH   F .   ? 0.6169 0.4151 0.3173 0.2786  0.1288  0.1079  291 HOH   B O   
6916 O O   . HOH   F .   ? 0.3334 0.2897 0.2914 -0.0275 0.0116  -0.1255 292 HOH   B O   
6917 O O   . HOH   F .   ? 0.4478 0.7320 0.2615 -0.0219 -0.0854 0.1317  293 HOH   B O   
6918 O O   . HOH   F .   ? 0.4541 0.3586 0.5167 -0.1040 0.0067  0.1322  294 HOH   B O   
6919 O O   . HOH   F .   ? 0.1787 0.2143 0.1686 -0.0141 -0.0216 0.0057  295 HOH   B O   
6920 O O   . HOH   F .   ? 0.1882 0.3296 0.5144 0.0339  0.0058  -0.1326 296 HOH   B O   
6921 O O   . HOH   F .   ? 0.2837 0.6685 0.7374 0.0999  -0.0684 -0.1094 297 HOH   B O   
6922 O O   . HOH   F .   ? 0.1935 0.2067 0.3026 0.0117  -0.0085 -0.0019 298 HOH   B O   
6923 O O   . HOH   F .   ? 0.4196 0.4592 0.5421 -0.0146 -0.1298 -0.0162 299 HOH   B O   
6924 O O   . HOH   F .   ? 0.1952 0.1811 0.2369 0.0143  0.0006  0.0082  300 HOH   B O   
6925 O O   . HOH   F .   ? 0.4540 0.4662 0.2269 0.0210  0.0628  0.0699  301 HOH   B O   
6926 O O   . HOH   F .   ? 0.3737 0.2029 0.3735 0.0737  0.1289  0.0626  302 HOH   B O   
6927 O O   . HOH   F .   ? 0.4215 0.3977 0.2559 0.1146  -0.0739 0.0453  303 HOH   B O   
6928 O O   . HOH   F .   ? 0.3091 0.3868 0.4157 -0.1147 0.1214  -0.0668 304 HOH   B O   
6929 O O   . HOH   F .   ? 0.2054 0.2900 0.6473 0.0396  -0.0280 -0.0938 305 HOH   B O   
6930 O O   . HOH   F .   ? 0.5547 0.3135 0.2626 -0.2020 0.0962  -0.0345 306 HOH   B O   
6931 O O   . HOH   F .   ? 0.2139 0.1821 0.3568 0.0351  -0.0980 -0.0007 307 HOH   B O   
6932 O O   . HOH   F .   ? 0.2317 0.1699 0.2807 -0.0275 -0.0344 -0.0081 308 HOH   B O   
6933 O O   . HOH   F .   ? 0.2927 0.3134 0.3409 -0.0393 0.0989  -0.0725 309 HOH   B O   
6934 O O   . HOH   F .   ? 0.1697 0.1715 0.3069 0.0061  0.0012  -0.0063 310 HOH   B O   
6935 O O   . HOH   F .   ? 0.2455 0.1656 0.2651 -0.0095 -0.0175 0.0419  311 HOH   B O   
6936 O O   . HOH   F .   ? 0.4732 0.4596 0.6326 0.0716  0.0102  0.0445  312 HOH   B O   
6937 O O   . HOH   F .   ? 0.4846 0.4270 0.2560 0.1336  -0.0623 -0.0196 313 HOH   B O   
6938 O O   . HOH   F .   ? 0.6005 0.5577 0.5426 -0.1188 -0.0192 0.1120  314 HOH   B O   
6939 O O   . HOH   F .   ? 0.4905 0.4750 0.2912 0.0764  -0.0476 -0.0845 315 HOH   B O   
6940 O O   . HOH   F .   ? 0.2268 0.2151 0.1972 -0.0046 0.0128  0.0273  316 HOH   B O   
6941 O O   . HOH   F .   ? 0.1765 0.1983 0.2943 -0.0270 -0.0055 0.0056  317 HOH   B O   
6942 O O   . HOH   F .   ? 0.2570 0.3480 0.4989 -0.0465 -0.0451 0.0092  318 HOH   B O   
6943 O O   . HOH   F .   ? 0.6492 0.4405 0.6178 0.1007  0.1493  -0.0027 319 HOH   B O   
6944 O O   . HOH   F .   ? 0.5179 0.2539 0.3158 0.0271  0.0620  0.0876  320 HOH   B O   
6945 O O   . HOH   F .   ? 0.4486 0.2661 0.2825 0.1642  0.1037  0.0259  321 HOH   B O   
6946 O O   . HOH   F .   ? 0.6780 0.5884 0.5223 0.2849  -0.0085 -0.0248 322 HOH   B O   
6947 O O   . HOH   F .   ? 0.2768 0.3697 0.5184 -0.0670 -0.1655 0.1326  323 HOH   B O   
6948 O O   . HOH   F .   ? 0.1889 0.1699 0.2956 -0.0126 -0.0181 -0.0104 324 HOH   B O   
6949 O O   . HOH   F .   ? 0.2546 0.6526 0.5270 -0.0982 -0.0385 -0.0477 325 HOH   B O   
6950 O O   . HOH   F .   ? 0.3593 0.4231 0.7855 -0.0023 -0.0749 0.2533  326 HOH   B O   
6951 O O   . HOH   F .   ? 0.2800 0.2365 0.2530 0.0266  -0.0183 0.0209  327 HOH   B O   
6952 O O   . HOH   F .   ? 0.4401 0.3279 0.5597 0.1198  0.2106  0.1660  328 HOH   B O   
6953 O O   . HOH   F .   ? 0.1910 0.2882 0.2461 -0.0081 -0.0226 0.0602  329 HOH   B O   
6954 O O   . HOH   F .   ? 0.2192 0.2133 0.3119 0.0384  0.0391  0.0161  330 HOH   B O   
6955 O O   . HOH   F .   ? 0.8825 0.2265 0.3206 0.0000  -0.0689 0.0186  331 HOH   B O   
6956 O O   . HOH   F .   ? 0.6517 0.5322 0.6392 0.0884  -0.1187 0.2058  332 HOH   B O   
6957 O O   . HOH   F .   ? 0.6259 0.3614 0.3746 -0.0161 0.1343  0.1123  333 HOH   B O   
6958 O O   . HOH   F .   ? 0.2991 0.2065 0.5053 -0.0112 0.0112  0.0309  334 HOH   B O   
6959 O O   . HOH   F .   ? 0.1866 0.2975 0.2970 0.0308  -0.0119 -0.0621 335 HOH   B O   
6960 O O   . HOH   F .   ? 0.2325 0.2406 0.6047 -0.0418 0.0063  0.1460  336 HOH   B O   
6961 O O   . HOH   F .   ? 0.4771 0.5393 0.4107 -0.0041 -0.0946 0.0427  337 HOH   B O   
6962 O O   . HOH   F .   ? 0.1952 0.1605 0.2430 0.0096  -0.0250 0.0139  338 HOH   B O   
6963 O O   . HOH   F .   ? 0.4479 0.7086 0.3599 0.0391  -0.0218 0.1682  339 HOH   B O   
6964 O O   . HOH   F .   ? 0.6284 0.4309 0.6560 -0.0710 -0.0676 -0.1160 340 HOH   B O   
6965 O O   . HOH   F .   ? 0.5256 0.3087 0.3548 0.0486  -0.1245 -0.0816 341 HOH   B O   
6966 O O   . HOH   F .   ? 0.5515 0.3366 0.4100 0.0484  0.0572  -0.1247 342 HOH   B O   
6967 O O   . HOH   F .   ? 0.2160 0.6585 0.6961 0.0172  -0.0772 -0.0025 343 HOH   B O   
6968 O O   . HOH   F .   ? 0.4164 0.6477 0.4148 -0.1083 -0.1043 -0.0662 344 HOH   B O   
6969 O O   . HOH   F .   ? 0.2285 0.2198 0.2847 -0.0154 0.0595  -0.0288 345 HOH   B O   
6970 O O   . HOH   F .   ? 0.6885 0.5776 0.2846 0.0372  -0.0477 0.0969  346 HOH   B O   
6971 O O   . HOH   F .   ? 0.4307 0.5217 0.5692 0.0408  -0.0655 0.0825  347 HOH   B O   
6972 O O   . HOH   F .   ? 0.2387 0.4017 0.5502 -0.0030 0.0304  0.0138  348 HOH   B O   
6973 O O   . HOH   F .   ? 0.2936 0.2486 0.5229 -0.0279 -0.1098 -0.0648 349 HOH   B O   
6974 O O   . HOH   F .   ? 0.5388 0.5232 0.4868 -0.1082 0.0907  0.0796  350 HOH   B O   
6975 O O   . HOH   F .   ? 0.2358 0.6016 0.4280 0.1463  -0.0573 -0.1517 351 HOH   B O   
6976 O O   . HOH   F .   ? 0.4740 0.6018 0.6267 0.0253  0.0025  -0.0788 352 HOH   B O   
6977 O O   . HOH   F .   ? 0.3724 0.2250 0.3879 -0.0492 0.0235  -0.0816 353 HOH   B O   
6978 O O   . HOH   F .   ? 0.4681 0.2994 0.5765 -0.0764 0.1478  0.0533  354 HOH   B O   
6979 O O   . HOH   F .   ? 0.3629 0.4332 0.5062 -0.1682 0.0285  -0.0259 355 HOH   B O   
6980 O O   . HOH   F .   ? 0.3959 0.2649 0.4294 -0.0822 -0.0149 -0.0615 356 HOH   B O   
6981 O O   . HOH   F .   ? 0.5530 0.3854 0.4153 0.0648  0.1343  -0.0540 357 HOH   B O   
6982 O O   . HOH   F .   ? 0.3052 0.2166 0.4647 0.0615  -0.1430 -0.0668 358 HOH   B O   
6983 O O   . HOH   F .   ? 0.4304 0.4091 0.5013 -0.0060 -0.0682 0.0074  359 HOH   B O   
6984 O O   . HOH   F .   ? 0.4609 0.6151 0.5493 0.2097  -0.1188 0.1578  360 HOH   B O   
6985 O O   . HOH   F .   ? 0.5001 0.3618 0.5304 0.0116  -0.1682 -0.0350 361 HOH   B O   
6986 O O   . HOH   F .   ? 0.5221 0.4086 0.6257 0.0323  0.0611  0.1165  362 HOH   B O   
6987 O O   . HOH   F .   ? 0.5189 0.7166 0.3037 0.2577  0.0059  0.0407  363 HOH   B O   
6988 O O   . HOH   F .   ? 0.2230 0.3948 0.6931 -0.0679 -0.0626 -0.0814 364 HOH   B O   
6989 O O   . HOH   F .   ? 0.4906 0.3326 0.5865 -0.1404 -0.0620 0.0325  365 HOH   B O   
6990 O O   . HOH   F .   ? 0.5750 0.6194 0.3772 0.1774  -0.1299 0.0774  366 HOH   B O   
6991 O O   . HOH   F .   ? 0.6442 0.4657 0.4800 0.1353  0.0661  0.0726  367 HOH   B O   
6992 O O   . HOH   F .   ? 0.5794 0.3913 0.5700 0.1194  -0.1337 0.0262  368 HOH   B O   
6993 O O   . HOH   F .   ? 0.4996 0.5497 0.4820 -0.0397 -0.0702 -0.1158 369 HOH   B O   
6994 O O   . HOH   F .   ? 0.6827 0.2213 0.3970 0.0039  0.0217  0.0599  370 HOH   B O   
6995 O O   . HOH   F .   ? 0.8156 0.7968 0.5564 0.2991  -0.1434 0.1142  371 HOH   B O   
6996 O O   . HOH   F .   ? 0.4917 0.5610 0.5415 0.2913  0.1092  0.1056  372 HOH   B O   
6997 O O   . HOH   F .   ? 0.6819 0.4214 0.3299 -0.1411 -0.1109 -0.0724 373 HOH   B O   
6998 O O   . HOH   F .   ? 0.4171 0.3844 0.4393 0.0754  -0.1381 -0.0468 374 HOH   B O   
6999 O O   . HOH   F .   ? 0.4682 0.5233 0.5118 -0.0924 -0.0732 0.0329  375 HOH   B O   
7000 O O   . HOH   F .   ? 0.2795 0.4184 0.4725 0.0320  -0.0661 -0.0673 376 HOH   B O   
7001 O O   . HOH   F .   ? 0.3675 0.4122 0.2489 0.0760  0.0322  0.0129  377 HOH   B O   
7002 O O   . HOH   F .   ? 0.4808 0.7507 0.6178 0.1706  0.0764  0.2940  378 HOH   B O   
7003 O O   . HOH   F .   ? 0.7699 0.3856 0.5504 -0.0660 -0.0671 -0.0083 379 HOH   B O   
7004 O O   . HOH   F .   ? 0.5087 0.6895 0.4429 -0.1355 -0.0009 -0.1693 380 HOH   B O   
7005 O O   . HOH   F .   ? 0.3736 0.5108 0.5825 0.1420  -0.0476 0.0526  381 HOH   B O   
7006 O O   . HOH   F .   ? 0.5489 0.7355 0.6600 -0.0523 0.1651  0.1412  382 HOH   B O   
7007 O O   . HOH   F .   ? 0.3143 0.2887 0.3539 0.0105  0.0228  0.0506  383 HOH   B O   
7008 O O   . HOH   F .   ? 0.4315 0.8349 0.5827 0.0915  0.2155  0.1430  384 HOH   B O   
7009 O O   . HOH   F .   ? 0.6753 0.4279 0.4845 0.1062  0.1055  -0.0565 385 HOH   B O   
7010 O O   . HOH   F .   ? 0.5785 0.4582 0.4292 -0.0103 -0.0554 -0.0605 386 HOH   B O   
7011 O O   . HOH   F .   ? 0.2524 0.4726 0.3968 -0.0774 -0.0907 -0.0319 387 HOH   B O   
7012 O O   . HOH   F .   ? 0.5734 0.4627 0.5396 -0.0508 0.0285  0.0225  388 HOH   B O   
7013 O O   . HOH   F .   ? 0.6843 0.5927 0.4513 0.2345  0.0090  0.1065  389 HOH   B O   
7014 O O   . HOH   F .   ? 0.4999 0.3812 0.3357 0.0025  0.0474  -0.0400 390 HOH   B O   
7015 O O   . HOH   F .   ? 0.4408 0.2416 0.3442 0.0888  -0.0208 0.0136  391 HOH   B O   
7016 O O   . HOH   F .   ? 0.4849 0.4059 0.3854 -0.0056 0.0106  0.0546  392 HOH   B O   
7017 O O   . HOH   F .   ? 0.2532 0.4660 0.6719 -0.1309 -0.0752 0.0098  393 HOH   B O   
7018 O O   . HOH   F .   ? 0.4572 0.2432 0.5277 -0.0522 0.0664  0.0464  394 HOH   B O   
7019 O O   . HOH   F .   ? 0.4315 0.4431 0.4343 -0.0307 0.0741  0.0698  395 HOH   B O   
7020 O O   . HOH   F .   ? 0.4741 0.6050 0.3781 0.1390  -0.0056 -0.0830 396 HOH   B O   
7021 O O   . HOH   F .   ? 0.3350 0.3985 0.3931 0.0432  0.0140  -0.0567 397 HOH   B O   
7022 O O   . HOH   F .   ? 0.2110 0.3132 0.6418 -0.0420 -0.0849 -0.0099 398 HOH   B O   
7023 O O   . HOH   F .   ? 0.5980 0.6724 0.7367 0.1914  -0.0862 0.1667  399 HOH   B O   
7024 O O   . HOH   F .   ? 0.5562 0.4387 0.3234 -0.2148 -0.0345 0.1136  400 HOH   B O   
7025 O O   . HOH   F .   ? 0.5339 0.6404 0.3810 0.1420  0.0346  -0.0110 401 HOH   B O   
# 
