data_7HDR
# 
_entry.id   7HDR 
# 
_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   7HDR         pdb_00007hdr 10.2210/pdb7hdr/pdb 
WWPDB D_1001407345 ?            ?                   
# 
_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                        7HDR 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                      18178.766 2   
'3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'trifluoroacetic acid'                                                          114.023   1   ? ? ? ? 
3 non-polymer syn '(2S)-3-(4-fluorophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' 286.304   1   ? ? ? ? 
4 non-polymer syn '(2R)-3-(4-fluorophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' 286.304   1   ? ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                                                                  35.453    1   ? ? ? ? 
6 water       nat water                                                                           18.015    414 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                                          TFA   
3 '(2S)-3-(4-fluorophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' A1A80 
4 '(2R)-3-(4-fluorophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' A1A8Z 
5 'CHLORIDE ION'                                                                  CL    
6 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 
A1A80 non-polymer         . '(2S)-3-(4-fluorophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' ? 'C15 H15 F N4 O' 
286.304 
A1A8Z non-polymer         . '(2R)-3-(4-fluorophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' ? 'C15 H15 F N4 O' 
286.304 
ALA   'L-peptide linking' y ALANINE                                                                         ? 'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE                                                                        ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                      ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                 ? 'C4 H7 N O4'     
133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                                  ? 'Cl -1'          
35.453  
CYS   'L-peptide linking' y CYSTEINE                                                                        ? 'C3 H7 N O2 S'   
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                       ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                 ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                         ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                       ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                           ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                      ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                         ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                          ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                      ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                   ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                         ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                          ? 'C3 H7 N O3'     
105.093 
TFA   non-polymer         . 'trifluoroacetic acid'                                                          ? 'C2 H F3 O2'     
114.023 
THR   'L-peptide linking' y THREONINE                                                                       ? 'C4 H9 N O3'     
119.119 
TYR   'L-peptide linking' y TYROSINE                                                                        ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                          ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TFA   1   201 201  TFA   TFA A . 
D 3 A1A80 1   202 201  A1A80 LA1 A . 
E 4 A1A8Z 1   203 301  A1A8Z LA2 A . 
F 5 CL    1   204 1    CL    CL  A . 
G 6 HOH   1   301 292  HOH   HOH A . 
G 6 HOH   2   302 196  HOH   HOH A . 
G 6 HOH   3   303 1289 HOH   HOH A . 
G 6 HOH   4   304 229  HOH   HOH A . 
G 6 HOH   5   305 153  HOH   HOH A . 
G 6 HOH   6   306 86   HOH   HOH A . 
G 6 HOH   7   307 625  HOH   HOH A . 
G 6 HOH   8   308 493  HOH   HOH A . 
G 6 HOH   9   309 1290 HOH   HOH A . 
G 6 HOH   10  310 109  HOH   HOH A . 
G 6 HOH   11  311 281  HOH   HOH A . 
G 6 HOH   12  312 136  HOH   HOH A . 
G 6 HOH   13  313 151  HOH   HOH A . 
G 6 HOH   14  314 209  HOH   HOH A . 
G 6 HOH   15  315 76   HOH   HOH A . 
G 6 HOH   16  316 1    HOH   HOH A . 
G 6 HOH   17  317 192  HOH   HOH A . 
G 6 HOH   18  318 1295 HOH   HOH A . 
G 6 HOH   19  319 124  HOH   HOH A . 
G 6 HOH   20  320 630  HOH   HOH A . 
G 6 HOH   21  321 1283 HOH   HOH A . 
G 6 HOH   22  322 21   HOH   HOH A . 
G 6 HOH   23  323 661  HOH   HOH A . 
G 6 HOH   24  324 469  HOH   HOH A . 
G 6 HOH   25  325 17   HOH   HOH A . 
G 6 HOH   26  326 18   HOH   HOH A . 
G 6 HOH   27  327 247  HOH   HOH A . 
G 6 HOH   28  328 15   HOH   HOH A . 
G 6 HOH   29  329 164  HOH   HOH A . 
G 6 HOH   30  330 6    HOH   HOH A . 
G 6 HOH   31  331 337  HOH   HOH A . 
G 6 HOH   32  332 236  HOH   HOH A . 
G 6 HOH   33  333 8    HOH   HOH A . 
G 6 HOH   34  334 140  HOH   HOH A . 
G 6 HOH   35  335 225  HOH   HOH A . 
G 6 HOH   36  336 241  HOH   HOH A . 
G 6 HOH   37  337 1300 HOH   HOH A . 
G 6 HOH   38  338 39   HOH   HOH A . 
G 6 HOH   39  339 1301 HOH   HOH A . 
G 6 HOH   40  340 320  HOH   HOH A . 
G 6 HOH   41  341 74   HOH   HOH A . 
G 6 HOH   42  342 409  HOH   HOH A . 
G 6 HOH   43  343 165  HOH   HOH A . 
G 6 HOH   44  344 1310 HOH   HOH A . 
G 6 HOH   45  345 78   HOH   HOH A . 
G 6 HOH   46  346 964  HOH   HOH A . 
G 6 HOH   47  347 4    HOH   HOH A . 
G 6 HOH   48  348 393  HOH   HOH A . 
G 6 HOH   49  349 42   HOH   HOH A . 
G 6 HOH   50  350 33   HOH   HOH A . 
G 6 HOH   51  351 57   HOH   HOH A . 
G 6 HOH   52  352 92   HOH   HOH A . 
G 6 HOH   53  353 1313 HOH   HOH A . 
G 6 HOH   54  354 105  HOH   HOH A . 
G 6 HOH   55  355 169  HOH   HOH A . 
G 6 HOH   56  356 155  HOH   HOH A . 
G 6 HOH   57  357 93   HOH   HOH A . 
G 6 HOH   58  358 354  HOH   HOH A . 
G 6 HOH   59  359 24   HOH   HOH A . 
G 6 HOH   60  360 2    HOH   HOH A . 
G 6 HOH   61  361 36   HOH   HOH A . 
G 6 HOH   62  362 66   HOH   HOH A . 
G 6 HOH   63  363 102  HOH   HOH A . 
G 6 HOH   64  364 26   HOH   HOH A . 
G 6 HOH   65  365 19   HOH   HOH A . 
G 6 HOH   66  366 81   HOH   HOH A . 
G 6 HOH   67  367 139  HOH   HOH A . 
G 6 HOH   68  368 5    HOH   HOH A . 
G 6 HOH   69  369 396  HOH   HOH A . 
G 6 HOH   70  370 162  HOH   HOH A . 
G 6 HOH   71  371 662  HOH   HOH A . 
G 6 HOH   72  372 939  HOH   HOH A . 
G 6 HOH   73  373 45   HOH   HOH A . 
G 6 HOH   74  374 56   HOH   HOH A . 
G 6 HOH   75  375 138  HOH   HOH A . 
G 6 HOH   76  376 140  HOH   HOH A . 
G 6 HOH   77  377 154  HOH   HOH A . 
G 6 HOH   78  378 159  HOH   HOH A . 
G 6 HOH   79  379 35   HOH   HOH A . 
G 6 HOH   80  380 62   HOH   HOH A . 
G 6 HOH   81  381 218  HOH   HOH A . 
G 6 HOH   82  382 186  HOH   HOH A . 
G 6 HOH   83  383 3    HOH   HOH A . 
G 6 HOH   84  384 148  HOH   HOH A . 
G 6 HOH   85  385 115  HOH   HOH A . 
G 6 HOH   86  386 134  HOH   HOH A . 
G 6 HOH   87  387 1308 HOH   HOH A . 
G 6 HOH   88  388 46   HOH   HOH A . 
G 6 HOH   89  389 49   HOH   HOH A . 
G 6 HOH   90  390 366  HOH   HOH A . 
G 6 HOH   91  391 27   HOH   HOH A . 
G 6 HOH   92  392 132  HOH   HOH A . 
G 6 HOH   93  393 58   HOH   HOH A . 
G 6 HOH   94  394 333  HOH   HOH A . 
G 6 HOH   95  395 85   HOH   HOH A . 
G 6 HOH   96  396 6    HOH   HOH A . 
G 6 HOH   97  397 116  HOH   HOH A . 
G 6 HOH   98  398 83   HOH   HOH A . 
G 6 HOH   99  399 34   HOH   HOH A . 
G 6 HOH   100 400 12   HOH   HOH A . 
G 6 HOH   101 401 381  HOH   HOH A . 
G 6 HOH   102 402 1275 HOH   HOH A . 
G 6 HOH   103 403 351  HOH   HOH A . 
G 6 HOH   104 404 96   HOH   HOH A . 
G 6 HOH   105 405 405  HOH   HOH A . 
G 6 HOH   106 406 461  HOH   HOH A . 
G 6 HOH   107 407 296  HOH   HOH A . 
G 6 HOH   108 408 303  HOH   HOH A . 
G 6 HOH   109 409 1315 HOH   HOH A . 
G 6 HOH   110 410 278  HOH   HOH A . 
G 6 HOH   111 411 121  HOH   HOH A . 
G 6 HOH   112 412 1279 HOH   HOH A . 
G 6 HOH   113 413 67   HOH   HOH A . 
G 6 HOH   114 414 25   HOH   HOH A . 
G 6 HOH   115 415 1309 HOH   HOH A . 
G 6 HOH   116 416 1068 HOH   HOH A . 
G 6 HOH   117 417 3    HOH   HOH A . 
G 6 HOH   118 418 199  HOH   HOH A . 
G 6 HOH   119 419 123  HOH   HOH A . 
G 6 HOH   120 420 195  HOH   HOH A . 
G 6 HOH   121 421 68   HOH   HOH A . 
G 6 HOH   122 422 125  HOH   HOH A . 
G 6 HOH   123 423 397  HOH   HOH A . 
G 6 HOH   124 424 53   HOH   HOH A . 
G 6 HOH   125 425 95   HOH   HOH A . 
G 6 HOH   126 426 156  HOH   HOH A . 
G 6 HOH   127 427 582  HOH   HOH A . 
G 6 HOH   128 428 51   HOH   HOH A . 
G 6 HOH   129 429 122  HOH   HOH A . 
G 6 HOH   130 430 1222 HOH   HOH A . 
G 6 HOH   131 431 70   HOH   HOH A . 
G 6 HOH   132 432 7    HOH   HOH A . 
G 6 HOH   133 433 1238 HOH   HOH A . 
G 6 HOH   134 434 1094 HOH   HOH A . 
G 6 HOH   135 435 1296 HOH   HOH A . 
G 6 HOH   136 436 73   HOH   HOH A . 
G 6 HOH   137 437 80   HOH   HOH A . 
G 6 HOH   138 438 71   HOH   HOH A . 
G 6 HOH   139 439 944  HOH   HOH A . 
G 6 HOH   140 440 94   HOH   HOH A . 
G 6 HOH   141 441 188  HOH   HOH A . 
G 6 HOH   142 442 16   HOH   HOH A . 
G 6 HOH   143 443 40   HOH   HOH A . 
G 6 HOH   144 444 212  HOH   HOH A . 
G 6 HOH   145 445 952  HOH   HOH A . 
G 6 HOH   146 446 97   HOH   HOH A . 
G 6 HOH   147 447 576  HOH   HOH A . 
G 6 HOH   148 448 1286 HOH   HOH A . 
G 6 HOH   149 449 79   HOH   HOH A . 
G 6 HOH   150 450 104  HOH   HOH A . 
G 6 HOH   151 451 1189 HOH   HOH A . 
G 6 HOH   152 452 1119 HOH   HOH A . 
G 6 HOH   153 453 2    HOH   HOH A . 
G 6 HOH   154 454 330  HOH   HOH A . 
G 6 HOH   155 455 1134 HOH   HOH A . 
G 6 HOH   156 456 509  HOH   HOH A . 
G 6 HOH   157 457 107  HOH   HOH A . 
G 6 HOH   158 458 726  HOH   HOH A . 
G 6 HOH   159 459 163  HOH   HOH A . 
G 6 HOH   160 460 408  HOH   HOH A . 
G 6 HOH   161 461 756  HOH   HOH A . 
G 6 HOH   162 462 361  HOH   HOH A . 
G 6 HOH   163 463 126  HOH   HOH A . 
G 6 HOH   164 464 280  HOH   HOH A . 
G 6 HOH   165 465 319  HOH   HOH A . 
G 6 HOH   166 466 1276 HOH   HOH A . 
G 6 HOH   167 467 556  HOH   HOH A . 
G 6 HOH   168 468 801  HOH   HOH A . 
G 6 HOH   169 469 1307 HOH   HOH A . 
G 6 HOH   170 470 250  HOH   HOH A . 
G 6 HOH   171 471 63   HOH   HOH A . 
G 6 HOH   172 472 342  HOH   HOH A . 
G 6 HOH   173 473 267  HOH   HOH A . 
G 6 HOH   174 474 135  HOH   HOH A . 
G 6 HOH   175 475 370  HOH   HOH A . 
G 6 HOH   176 476 1306 HOH   HOH A . 
G 6 HOH   177 477 224  HOH   HOH A . 
G 6 HOH   178 478 1287 HOH   HOH A . 
G 6 HOH   179 479 695  HOH   HOH A . 
G 6 HOH   180 480 202  HOH   HOH A . 
G 6 HOH   181 481 674  HOH   HOH A . 
G 6 HOH   182 482 521  HOH   HOH A . 
G 6 HOH   183 483 919  HOH   HOH A . 
G 6 HOH   184 484 318  HOH   HOH A . 
G 6 HOH   185 485 1299 HOH   HOH A . 
G 6 HOH   186 486 309  HOH   HOH A . 
G 6 HOH   187 487 326  HOH   HOH A . 
G 6 HOH   188 488 1314 HOH   HOH A . 
G 6 HOH   189 489 805  HOH   HOH A . 
G 6 HOH   190 490 331  HOH   HOH A . 
G 6 HOH   191 491 941  HOH   HOH A . 
G 6 HOH   192 492 315  HOH   HOH A . 
G 6 HOH   193 493 711  HOH   HOH A . 
G 6 HOH   194 494 263  HOH   HOH A . 
G 6 HOH   195 495 356  HOH   HOH A . 
G 6 HOH   196 496 152  HOH   HOH A . 
G 6 HOH   197 497 208  HOH   HOH A . 
G 6 HOH   198 498 180  HOH   HOH A . 
G 6 HOH   199 499 1071 HOH   HOH A . 
G 6 HOH   200 500 350  HOH   HOH A . 
G 6 HOH   201 501 1284 HOH   HOH A . 
G 6 HOH   202 502 363  HOH   HOH A . 
G 6 HOH   203 503 371  HOH   HOH A . 
G 6 HOH   204 504 313  HOH   HOH A . 
G 6 HOH   205 505 5    HOH   HOH A . 
G 6 HOH   206 506 185  HOH   HOH A . 
G 6 HOH   207 507 429  HOH   HOH A . 
G 6 HOH   208 508 70   HOH   HOH A . 
G 6 HOH   209 509 376  HOH   HOH A . 
G 6 HOH   210 510 1074 HOH   HOH A . 
G 6 HOH   211 511 772  HOH   HOH A . 
G 6 HOH   212 512 1292 HOH   HOH A . 
G 6 HOH   213 513 346  HOH   HOH A . 
G 6 HOH   214 514 1078 HOH   HOH A . 
H 6 HOH   1   201 64   HOH   HOH B . 
H 6 HOH   2   202 549  HOH   HOH B . 
H 6 HOH   3   203 364  HOH   HOH B . 
H 6 HOH   4   204 358  HOH   HOH B . 
H 6 HOH   5   205 1249 HOH   HOH B . 
H 6 HOH   6   206 531  HOH   HOH B . 
H 6 HOH   7   207 900  HOH   HOH B . 
H 6 HOH   8   208 240  HOH   HOH B . 
H 6 HOH   9   209 50   HOH   HOH B . 
H 6 HOH   10  210 120  HOH   HOH B . 
H 6 HOH   11  211 232  HOH   HOH B . 
H 6 HOH   12  212 743  HOH   HOH B . 
H 6 HOH   13  213 398  HOH   HOH B . 
H 6 HOH   14  214 205  HOH   HOH B . 
H 6 HOH   15  215 758  HOH   HOH B . 
H 6 HOH   16  216 444  HOH   HOH B . 
H 6 HOH   17  217 353  HOH   HOH B . 
H 6 HOH   18  218 452  HOH   HOH B . 
H 6 HOH   19  219 1140 HOH   HOH B . 
H 6 HOH   20  220 264  HOH   HOH B . 
H 6 HOH   21  221 654  HOH   HOH B . 
H 6 HOH   22  222 332  HOH   HOH B . 
H 6 HOH   23  223 343  HOH   HOH B . 
H 6 HOH   24  224 131  HOH   HOH B . 
H 6 HOH   25  225 1278 HOH   HOH B . 
H 6 HOH   26  226 75   HOH   HOH B . 
H 6 HOH   27  227 54   HOH   HOH B . 
H 6 HOH   28  228 172  HOH   HOH B . 
H 6 HOH   29  229 60   HOH   HOH B . 
H 6 HOH   30  230 82   HOH   HOH B . 
H 6 HOH   31  231 272  HOH   HOH B . 
H 6 HOH   32  232 166  HOH   HOH B . 
H 6 HOH   33  233 69   HOH   HOH B . 
H 6 HOH   34  234 723  HOH   HOH B . 
H 6 HOH   35  235 276  HOH   HOH B . 
H 6 HOH   36  236 300  HOH   HOH B . 
H 6 HOH   37  237 282  HOH   HOH B . 
H 6 HOH   38  238 1    HOH   HOH B . 
H 6 HOH   39  239 128  HOH   HOH B . 
H 6 HOH   40  240 110  HOH   HOH B . 
H 6 HOH   41  241 325  HOH   HOH B . 
H 6 HOH   42  242 1312 HOH   HOH B . 
H 6 HOH   43  243 14   HOH   HOH B . 
H 6 HOH   44  244 144  HOH   HOH B . 
H 6 HOH   45  245 9    HOH   HOH B . 
H 6 HOH   46  246 133  HOH   HOH B . 
H 6 HOH   47  247 129  HOH   HOH B . 
H 6 HOH   48  248 181  HOH   HOH B . 
H 6 HOH   49  249 30   HOH   HOH B . 
H 6 HOH   50  250 41   HOH   HOH B . 
H 6 HOH   51  251 127  HOH   HOH B . 
H 6 HOH   52  252 231  HOH   HOH B . 
H 6 HOH   53  253 143  HOH   HOH B . 
H 6 HOH   54  254 52   HOH   HOH B . 
H 6 HOH   55  255 271  HOH   HOH B . 
H 6 HOH   56  256 103  HOH   HOH B . 
H 6 HOH   57  257 252  HOH   HOH B . 
H 6 HOH   58  258 31   HOH   HOH B . 
H 6 HOH   59  259 72   HOH   HOH B . 
H 6 HOH   60  260 347  HOH   HOH B . 
H 6 HOH   61  261 150  HOH   HOH B . 
H 6 HOH   62  262 391  HOH   HOH B . 
H 6 HOH   63  263 117  HOH   HOH B . 
H 6 HOH   64  264 243  HOH   HOH B . 
H 6 HOH   65  265 47   HOH   HOH B . 
H 6 HOH   66  266 10   HOH   HOH B . 
H 6 HOH   67  267 59   HOH   HOH B . 
H 6 HOH   68  268 77   HOH   HOH B . 
H 6 HOH   69  269 61   HOH   HOH B . 
H 6 HOH   70  270 1277 HOH   HOH B . 
H 6 HOH   71  271 84   HOH   HOH B . 
H 6 HOH   72  272 11   HOH   HOH B . 
H 6 HOH   73  273 175  HOH   HOH B . 
H 6 HOH   74  274 147  HOH   HOH B . 
H 6 HOH   75  275 416  HOH   HOH B . 
H 6 HOH   76  276 302  HOH   HOH B . 
H 6 HOH   77  277 221  HOH   HOH B . 
H 6 HOH   78  278 20   HOH   HOH B . 
H 6 HOH   79  279 216  HOH   HOH B . 
H 6 HOH   80  280 242  HOH   HOH B . 
H 6 HOH   81  281 287  HOH   HOH B . 
H 6 HOH   82  282 114  HOH   HOH B . 
H 6 HOH   83  283 43   HOH   HOH B . 
H 6 HOH   84  284 22   HOH   HOH B . 
H 6 HOH   85  285 1106 HOH   HOH B . 
H 6 HOH   86  286 99   HOH   HOH B . 
H 6 HOH   87  287 137  HOH   HOH B . 
H 6 HOH   88  288 220  HOH   HOH B . 
H 6 HOH   89  289 1066 HOH   HOH B . 
H 6 HOH   90  290 235  HOH   HOH B . 
H 6 HOH   91  291 1305 HOH   HOH B . 
H 6 HOH   92  292 106  HOH   HOH B . 
H 6 HOH   93  293 112  HOH   HOH B . 
H 6 HOH   94  294 13   HOH   HOH B . 
H 6 HOH   95  295 311  HOH   HOH B . 
H 6 HOH   96  296 299  HOH   HOH B . 
H 6 HOH   97  297 88   HOH   HOH B . 
H 6 HOH   98  298 160  HOH   HOH B . 
H 6 HOH   99  299 89   HOH   HOH B . 
H 6 HOH   100 300 297  HOH   HOH B . 
H 6 HOH   101 301 142  HOH   HOH B . 
H 6 HOH   102 302 215  HOH   HOH B . 
H 6 HOH   103 303 387  HOH   HOH B . 
H 6 HOH   104 304 316  HOH   HOH B . 
H 6 HOH   105 305 38   HOH   HOH B . 
H 6 HOH   106 306 101  HOH   HOH B . 
H 6 HOH   107 307 118  HOH   HOH B . 
H 6 HOH   108 308 32   HOH   HOH B . 
H 6 HOH   109 309 635  HOH   HOH B . 
H 6 HOH   110 310 182  HOH   HOH B . 
H 6 HOH   111 311 1274 HOH   HOH B . 
H 6 HOH   112 312 48   HOH   HOH B . 
H 6 HOH   113 313 1285 HOH   HOH B . 
H 6 HOH   114 314 37   HOH   HOH B . 
H 6 HOH   115 315 170  HOH   HOH B . 
H 6 HOH   116 316 141  HOH   HOH B . 
H 6 HOH   117 317 445  HOH   HOH B . 
H 6 HOH   118 318 197  HOH   HOH B . 
H 6 HOH   119 319 23   HOH   HOH B . 
H 6 HOH   120 320 28   HOH   HOH B . 
H 6 HOH   121 321 44   HOH   HOH B . 
H 6 HOH   122 322 177  HOH   HOH B . 
H 6 HOH   123 323 91   HOH   HOH B . 
H 6 HOH   124 324 1294 HOH   HOH B . 
H 6 HOH   125 325 100  HOH   HOH B . 
H 6 HOH   126 326 161  HOH   HOH B . 
H 6 HOH   127 327 29   HOH   HOH B . 
H 6 HOH   128 328 1291 HOH   HOH B . 
H 6 HOH   129 329 207  HOH   HOH B . 
H 6 HOH   130 330 55   HOH   HOH B . 
H 6 HOH   131 331 341  HOH   HOH B . 
H 6 HOH   132 332 98   HOH   HOH B . 
H 6 HOH   133 333 334  HOH   HOH B . 
H 6 HOH   134 334 1126 HOH   HOH B . 
H 6 HOH   135 335 704  HOH   HOH B . 
H 6 HOH   136 336 717  HOH   HOH B . 
H 6 HOH   137 337 1293 HOH   HOH B . 
H 6 HOH   138 338 65   HOH   HOH B . 
H 6 HOH   139 339 234  HOH   HOH B . 
H 6 HOH   140 340 619  HOH   HOH B . 
H 6 HOH   141 341 178  HOH   HOH B . 
H 6 HOH   142 342 960  HOH   HOH B . 
H 6 HOH   143 343 339  HOH   HOH B . 
H 6 HOH   144 344 362  HOH   HOH B . 
H 6 HOH   145 345 90   HOH   HOH B . 
H 6 HOH   146 346 87   HOH   HOH B . 
H 6 HOH   147 347 463  HOH   HOH B . 
H 6 HOH   148 348 623  HOH   HOH B . 
H 6 HOH   149 349 1304 HOH   HOH B . 
H 6 HOH   150 350 191  HOH   HOH B . 
H 6 HOH   151 351 1280 HOH   HOH B . 
H 6 HOH   152 352 335  HOH   HOH B . 
H 6 HOH   153 353 1046 HOH   HOH B . 
H 6 HOH   154 354 304  HOH   HOH B . 
H 6 HOH   155 355 203  HOH   HOH B . 
H 6 HOH   156 356 290  HOH   HOH B . 
H 6 HOH   157 357 541  HOH   HOH B . 
H 6 HOH   158 358 1077 HOH   HOH B . 
H 6 HOH   159 359 389  HOH   HOH B . 
H 6 HOH   160 360 718  HOH   HOH B . 
H 6 HOH   161 361 283  HOH   HOH B . 
H 6 HOH   162 362 1072 HOH   HOH B . 
H 6 HOH   163 363 479  HOH   HOH B . 
H 6 HOH   164 364 1316 HOH   HOH B . 
H 6 HOH   165 365 291  HOH   HOH B . 
H 6 HOH   166 366 898  HOH   HOH B . 
H 6 HOH   167 367 615  HOH   HOH B . 
H 6 HOH   168 368 373  HOH   HOH B . 
H 6 HOH   169 369 667  HOH   HOH B . 
H 6 HOH   170 370 340  HOH   HOH B . 
H 6 HOH   171 371 1303 HOH   HOH B . 
H 6 HOH   172 372 190  HOH   HOH B . 
H 6 HOH   173 373 310  HOH   HOH B . 
H 6 HOH   174 374 431  HOH   HOH B . 
H 6 HOH   175 375 149  HOH   HOH B . 
H 6 HOH   176 376 1000 HOH   HOH B . 
H 6 HOH   177 377 1173 HOH   HOH B . 
H 6 HOH   178 378 183  HOH   HOH B . 
H 6 HOH   179 379 1163 HOH   HOH B . 
H 6 HOH   180 380 418  HOH   HOH B . 
H 6 HOH   181 381 1311 HOH   HOH B . 
H 6 HOH   182 382 424  HOH   HOH B . 
H 6 HOH   183 383 176  HOH   HOH B . 
H 6 HOH   184 384 981  HOH   HOH B . 
H 6 HOH   185 385 491  HOH   HOH B . 
H 6 HOH   186 386 1298 HOH   HOH B . 
H 6 HOH   187 387 248  HOH   HOH B . 
H 6 HOH   188 388 265  HOH   HOH B . 
H 6 HOH   189 389 470  HOH   HOH B . 
H 6 HOH   190 390 184  HOH   HOH B . 
H 6 HOH   191 391 360  HOH   HOH B . 
H 6 HOH   192 392 410  HOH   HOH B . 
H 6 HOH   193 393 355  HOH   HOH B . 
H 6 HOH   194 394 274  HOH   HOH B . 
H 6 HOH   195 395 157  HOH   HOH B . 
H 6 HOH   196 396 314  HOH   HOH B . 
H 6 HOH   197 397 566  HOH   HOH B . 
H 6 HOH   198 398 321  HOH   HOH B . 
H 6 HOH   199 399 792  HOH   HOH B . 
H 6 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HDR 
_cell.length_a           88.716 
_cell.length_b           88.716 
_cell.length_c           39.460 
_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                         7HDR 
_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          7HDR 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.51 
_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                     7HDR 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.360 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   164857 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.500 
_reflns.pdbx_Rmerge_I_obs            0.037 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        17.800 
_reflns.B_iso_Wilson_estimate        12.140 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.040 
_reflns.pdbx_Rpim_I_all              0.016 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1051671 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 34184 7451 ? 1.274 ? ? ? 4.600 ? 0.900  ? ? ? ? ? ? 91.200 1.437 0.645 0.635 
1 2 5.480 44.360 ? 7498  1093 ? 0.024 ? ? ? 6.900 ? 66.600 ? ? ? ? ? ? 99.900 0.026 0.010 0.999 
# 
_refine.entry_id                                 7HDR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.3600 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.4500 
_refine.ls_number_reflns_obs                     164765 
_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                          0.1458 
_refine.ls_R_factor_R_work                       0.1451 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1582 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7941 
_refine.ls_number_reflns_R_work                  156824 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.7671 
_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                            0.0900 
_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                                69.120 
_refine.B_iso_min                                8.240 
_refine.pdbx_overall_phase_error                 17.5700 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        44.3600 
_refine_hist.pdbx_number_atoms_ligand         44 
_refine_hist.number_atoms_solvent             414 
_refine_hist.number_atoms_total               3000 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           17.42 
_refine_hist.pdbx_B_iso_mean_solvent          29.84 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 89.0000  4705 . 0.3968 0.3338 . 245 0.0000 4950 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 96.0000  5020 . 0.3174 0.3439 . 208 0.0000 5228 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5246 . 0.2732 0.2731 . 272 0.0000 5518 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5161 . 0.2396 0.2486 . 271 0.0000 5432 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5220 . 0.2179 0.2324 . 321 0.0000 5541 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5205 . 0.2020 0.2280 . 250 0.0000 5455 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5244 . 0.1851 0.2143 . 265 0.0000 5509 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5237 . 0.1702 0.1773 . 240 0.0000 5477 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5236 . 0.1631 0.1702 . 286 0.0000 5522 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5217 . 0.1499 0.1561 . 242 0.0000 5459 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5263 . 0.1397 0.1556 . 266 0.0000 5529 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5249 . 0.1341 0.1597 . 266 0.0000 5515 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5137 . 0.1271 0.1534 . 283 0.0000 5420 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5343 . 0.1223 0.1410 . 226 0.0000 5569 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5194 . 0.1231 0.1362 . 259 0.0000 5453 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5245 . 0.1241 0.1364 . 280 0.0000 5525 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5210 . 0.1257 0.1436 . 281 0.0000 5491 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5219 . 0.1305 0.1509 . 278 0.0000 5497 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5279 . 0.1347 0.1708 . 249 0.0000 5528 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5234 . 0.1332 0.1647 . 271 0.0000 5505 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5277 . 0.1272 0.1285 . 245 0.0000 5522 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5223 . 0.1211 0.1303 . 276 0.0000 5499 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5287 . 0.1216 0.1355 . 270 0.0000 5557 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5260 . 0.1278 0.1441 . 257 0.0000 5517 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5289 . 0.1378 0.1484 . 251 0.0000 5540 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5263 . 0.1341 0.1379 . 281 0.0000 5544 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5279 . 0.1404 0.1443 . 289 0.0000 5568 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5292 . 0.1378 0.1426 . 288 0.0000 5580 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5321 . 0.1501 0.1630 . 255 0.0000 5576 . 'X-RAY DIFFRACTION' 
3.1100 44.3600 30 100.0000 5469 . 0.1506 0.1722 . 270 0.0000 5739 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDR 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003640' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDR 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 6 ? 
# 
_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 7HDR A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDR 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 7HDR SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDR MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDR SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDR MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G 
2 1 B,H         
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HDR 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 15 ? B -143.89 17.60   
2 1 HIS A 86 ? ? 54.97   -133.33 
3 1 HIS B 86 ? ? 57.08   -127.72 
# 
_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 512 ? 5.93 . 
2 1 O ? A HOH 513 ? 5.99 . 
3 1 O ? A HOH 514 ? 7.58 . 
4 1 O ? B HOH 400 ? 6.50 . 
# 
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 
A1A80 N2   N  Y N 1   
A1A80 C3   C  N N 2   
A1A80 C6   C  Y N 3   
A1A80 C9   C  Y N 4   
A1A80 C12  C  Y N 5   
A1A80 C14  C  Y N 6   
A1A80 C1   C  N N 7   
A1A80 C10  C  Y N 8   
A1A80 C11  C  Y N 9   
A1A80 C13  C  Y N 10  
A1A80 C15  C  Y N 11  
A1A80 C2   C  N S 12  
A1A80 C4   C  Y N 13  
A1A80 C5   C  Y N 14  
A1A80 C7   C  Y N 15  
A1A80 C8   C  Y N 16  
A1A80 F1   F  N N 17  
A1A80 N1   N  N N 18  
A1A80 N3   N  Y N 19  
A1A80 N4   N  Y N 20  
A1A80 O1   O  N N 21  
A1A80 H5   H  N N 22  
A1A80 H6   H  N N 23  
A1A80 H8   H  N N 24  
A1A80 H10  H  N N 25  
A1A80 H13  H  N N 26  
A1A80 H3   H  N N 27  
A1A80 H4   H  N N 28  
A1A80 H12  H  N N 29  
A1A80 H14  H  N N 30  
A1A80 H1   H  N N 31  
A1A80 H7   H  N N 32  
A1A80 H9   H  N N 33  
A1A80 H11  H  N N 34  
A1A80 H15  H  N N 35  
A1A80 H2   H  N N 36  
A1A8Z O1   O  N N 37  
A1A8Z C1   C  N N 38  
A1A8Z C2   C  N R 39  
A1A8Z C3   C  N N 40  
A1A8Z C4   C  Y N 41  
A1A8Z C5   C  Y N 42  
A1A8Z C6   C  Y N 43  
A1A8Z C7   C  Y N 44  
A1A8Z C8   C  Y N 45  
A1A8Z C10  C  Y N 46  
A1A8Z C11  C  Y N 47  
A1A8Z C12  C  Y N 48  
A1A8Z C13  C  Y N 49  
A1A8Z C14  C  Y N 50  
A1A8Z C15  C  Y N 51  
A1A8Z C9   C  Y N 52  
A1A8Z F1   F  N N 53  
A1A8Z N1   N  N N 54  
A1A8Z N2   N  Y N 55  
A1A8Z N3   N  Y N 56  
A1A8Z N4   N  Y N 57  
A1A8Z H2   H  N N 58  
A1A8Z H4   H  N N 59  
A1A8Z H3   H  N N 60  
A1A8Z H1   H  N N 61  
A1A8Z H5   H  N N 62  
A1A8Z H6   H  N N 63  
A1A8Z H7   H  N N 64  
A1A8Z H8   H  N N 65  
A1A8Z H9   H  N N 66  
A1A8Z H12  H  N N 67  
A1A8Z H13  H  N N 68  
A1A8Z H14  H  N N 69  
A1A8Z H10  H  N N 70  
A1A8Z H11  H  N N 71  
A1A8Z H15  H  N N 72  
ALA   N    N  N N 73  
ALA   CA   C  N S 74  
ALA   C    C  N N 75  
ALA   O    O  N N 76  
ALA   CB   C  N N 77  
ALA   OXT  O  N N 78  
ALA   H    H  N N 79  
ALA   H2   H  N N 80  
ALA   HA   H  N N 81  
ALA   HB1  H  N N 82  
ALA   HB2  H  N N 83  
ALA   HB3  H  N N 84  
ALA   HXT  H  N N 85  
ARG   N    N  N N 86  
ARG   CA   C  N S 87  
ARG   C    C  N N 88  
ARG   O    O  N N 89  
ARG   CB   C  N N 90  
ARG   CG   C  N N 91  
ARG   CD   C  N N 92  
ARG   NE   N  N N 93  
ARG   CZ   C  N N 94  
ARG   NH1  N  N N 95  
ARG   NH2  N  N N 96  
ARG   OXT  O  N N 97  
ARG   H    H  N N 98  
ARG   H2   H  N N 99  
ARG   HA   H  N N 100 
ARG   HB2  H  N N 101 
ARG   HB3  H  N N 102 
ARG   HG2  H  N N 103 
ARG   HG3  H  N N 104 
ARG   HD2  H  N N 105 
ARG   HD3  H  N N 106 
ARG   HE   H  N N 107 
ARG   HH11 H  N N 108 
ARG   HH12 H  N N 109 
ARG   HH21 H  N N 110 
ARG   HH22 H  N N 111 
ARG   HXT  H  N N 112 
ASN   N    N  N N 113 
ASN   CA   C  N S 114 
ASN   C    C  N N 115 
ASN   O    O  N N 116 
ASN   CB   C  N N 117 
ASN   CG   C  N N 118 
ASN   OD1  O  N N 119 
ASN   ND2  N  N N 120 
ASN   OXT  O  N N 121 
ASN   H    H  N N 122 
ASN   H2   H  N N 123 
ASN   HA   H  N N 124 
ASN   HB2  H  N N 125 
ASN   HB3  H  N N 126 
ASN   HD21 H  N N 127 
ASN   HD22 H  N N 128 
ASN   HXT  H  N N 129 
ASP   N    N  N N 130 
ASP   CA   C  N S 131 
ASP   C    C  N N 132 
ASP   O    O  N N 133 
ASP   CB   C  N N 134 
ASP   CG   C  N N 135 
ASP   OD1  O  N N 136 
ASP   OD2  O  N N 137 
ASP   OXT  O  N N 138 
ASP   H    H  N N 139 
ASP   H2   H  N N 140 
ASP   HA   H  N N 141 
ASP   HB2  H  N N 142 
ASP   HB3  H  N N 143 
ASP   HD2  H  N N 144 
ASP   HXT  H  N N 145 
CL    CL   CL N N 146 
CYS   N    N  N N 147 
CYS   CA   C  N R 148 
CYS   C    C  N N 149 
CYS   O    O  N N 150 
CYS   CB   C  N N 151 
CYS   SG   S  N N 152 
CYS   OXT  O  N N 153 
CYS   H    H  N N 154 
CYS   H2   H  N N 155 
CYS   HA   H  N N 156 
CYS   HB2  H  N N 157 
CYS   HB3  H  N N 158 
CYS   HG   H  N N 159 
CYS   HXT  H  N N 160 
GLN   N    N  N N 161 
GLN   CA   C  N S 162 
GLN   C    C  N N 163 
GLN   O    O  N N 164 
GLN   CB   C  N N 165 
GLN   CG   C  N N 166 
GLN   CD   C  N N 167 
GLN   OE1  O  N N 168 
GLN   NE2  N  N N 169 
GLN   OXT  O  N N 170 
GLN   H    H  N N 171 
GLN   H2   H  N N 172 
GLN   HA   H  N N 173 
GLN   HB2  H  N N 174 
GLN   HB3  H  N N 175 
GLN   HG2  H  N N 176 
GLN   HG3  H  N N 177 
GLN   HE21 H  N N 178 
GLN   HE22 H  N N 179 
GLN   HXT  H  N N 180 
GLU   N    N  N N 181 
GLU   CA   C  N S 182 
GLU   C    C  N N 183 
GLU   O    O  N N 184 
GLU   CB   C  N N 185 
GLU   CG   C  N N 186 
GLU   CD   C  N N 187 
GLU   OE1  O  N N 188 
GLU   OE2  O  N N 189 
GLU   OXT  O  N N 190 
GLU   H    H  N N 191 
GLU   H2   H  N N 192 
GLU   HA   H  N N 193 
GLU   HB2  H  N N 194 
GLU   HB3  H  N N 195 
GLU   HG2  H  N N 196 
GLU   HG3  H  N N 197 
GLU   HE2  H  N N 198 
GLU   HXT  H  N N 199 
GLY   N    N  N N 200 
GLY   CA   C  N N 201 
GLY   C    C  N N 202 
GLY   O    O  N N 203 
GLY   OXT  O  N N 204 
GLY   H    H  N N 205 
GLY   H2   H  N N 206 
GLY   HA2  H  N N 207 
GLY   HA3  H  N N 208 
GLY   HXT  H  N N 209 
HIS   N    N  N N 210 
HIS   CA   C  N S 211 
HIS   C    C  N N 212 
HIS   O    O  N N 213 
HIS   CB   C  N N 214 
HIS   CG   C  Y N 215 
HIS   ND1  N  Y N 216 
HIS   CD2  C  Y N 217 
HIS   CE1  C  Y N 218 
HIS   NE2  N  Y N 219 
HIS   OXT  O  N N 220 
HIS   H    H  N N 221 
HIS   H2   H  N N 222 
HIS   HA   H  N N 223 
HIS   HB2  H  N N 224 
HIS   HB3  H  N N 225 
HIS   HD1  H  N N 226 
HIS   HD2  H  N N 227 
HIS   HE1  H  N N 228 
HIS   HE2  H  N N 229 
HIS   HXT  H  N N 230 
HOH   O    O  N N 231 
HOH   H1   H  N N 232 
HOH   H2   H  N N 233 
ILE   N    N  N N 234 
ILE   CA   C  N S 235 
ILE   C    C  N N 236 
ILE   O    O  N N 237 
ILE   CB   C  N S 238 
ILE   CG1  C  N N 239 
ILE   CG2  C  N N 240 
ILE   CD1  C  N N 241 
ILE   OXT  O  N N 242 
ILE   H    H  N N 243 
ILE   H2   H  N N 244 
ILE   HA   H  N N 245 
ILE   HB   H  N N 246 
ILE   HG12 H  N N 247 
ILE   HG13 H  N N 248 
ILE   HG21 H  N N 249 
ILE   HG22 H  N N 250 
ILE   HG23 H  N N 251 
ILE   HD11 H  N N 252 
ILE   HD12 H  N N 253 
ILE   HD13 H  N N 254 
ILE   HXT  H  N N 255 
LEU   N    N  N N 256 
LEU   CA   C  N S 257 
LEU   C    C  N N 258 
LEU   O    O  N N 259 
LEU   CB   C  N N 260 
LEU   CG   C  N N 261 
LEU   CD1  C  N N 262 
LEU   CD2  C  N N 263 
LEU   OXT  O  N N 264 
LEU   H    H  N N 265 
LEU   H2   H  N N 266 
LEU   HA   H  N N 267 
LEU   HB2  H  N N 268 
LEU   HB3  H  N N 269 
LEU   HG   H  N N 270 
LEU   HD11 H  N N 271 
LEU   HD12 H  N N 272 
LEU   HD13 H  N N 273 
LEU   HD21 H  N N 274 
LEU   HD22 H  N N 275 
LEU   HD23 H  N N 276 
LEU   HXT  H  N N 277 
LYS   N    N  N N 278 
LYS   CA   C  N S 279 
LYS   C    C  N N 280 
LYS   O    O  N N 281 
LYS   CB   C  N N 282 
LYS   CG   C  N N 283 
LYS   CD   C  N N 284 
LYS   CE   C  N N 285 
LYS   NZ   N  N N 286 
LYS   OXT  O  N N 287 
LYS   H    H  N N 288 
LYS   H2   H  N N 289 
LYS   HA   H  N N 290 
LYS   HB2  H  N N 291 
LYS   HB3  H  N N 292 
LYS   HG2  H  N N 293 
LYS   HG3  H  N N 294 
LYS   HD2  H  N N 295 
LYS   HD3  H  N N 296 
LYS   HE2  H  N N 297 
LYS   HE3  H  N N 298 
LYS   HZ1  H  N N 299 
LYS   HZ2  H  N N 300 
LYS   HZ3  H  N N 301 
LYS   HXT  H  N N 302 
MET   N    N  N N 303 
MET   CA   C  N S 304 
MET   C    C  N N 305 
MET   O    O  N N 306 
MET   CB   C  N N 307 
MET   CG   C  N N 308 
MET   SD   S  N N 309 
MET   CE   C  N N 310 
MET   OXT  O  N N 311 
MET   H    H  N N 312 
MET   H2   H  N N 313 
MET   HA   H  N N 314 
MET   HB2  H  N N 315 
MET   HB3  H  N N 316 
MET   HG2  H  N N 317 
MET   HG3  H  N N 318 
MET   HE1  H  N N 319 
MET   HE2  H  N N 320 
MET   HE3  H  N N 321 
MET   HXT  H  N N 322 
PHE   N    N  N N 323 
PHE   CA   C  N S 324 
PHE   C    C  N N 325 
PHE   O    O  N N 326 
PHE   CB   C  N N 327 
PHE   CG   C  Y N 328 
PHE   CD1  C  Y N 329 
PHE   CD2  C  Y N 330 
PHE   CE1  C  Y N 331 
PHE   CE2  C  Y N 332 
PHE   CZ   C  Y N 333 
PHE   OXT  O  N N 334 
PHE   H    H  N N 335 
PHE   H2   H  N N 336 
PHE   HA   H  N N 337 
PHE   HB2  H  N N 338 
PHE   HB3  H  N N 339 
PHE   HD1  H  N N 340 
PHE   HD2  H  N N 341 
PHE   HE1  H  N N 342 
PHE   HE2  H  N N 343 
PHE   HZ   H  N N 344 
PHE   HXT  H  N N 345 
PRO   N    N  N N 346 
PRO   CA   C  N S 347 
PRO   C    C  N N 348 
PRO   O    O  N N 349 
PRO   CB   C  N N 350 
PRO   CG   C  N N 351 
PRO   CD   C  N N 352 
PRO   OXT  O  N N 353 
PRO   H    H  N N 354 
PRO   HA   H  N N 355 
PRO   HB2  H  N N 356 
PRO   HB3  H  N N 357 
PRO   HG2  H  N N 358 
PRO   HG3  H  N N 359 
PRO   HD2  H  N N 360 
PRO   HD3  H  N N 361 
PRO   HXT  H  N N 362 
SER   N    N  N N 363 
SER   CA   C  N S 364 
SER   C    C  N N 365 
SER   O    O  N N 366 
SER   CB   C  N N 367 
SER   OG   O  N N 368 
SER   OXT  O  N N 369 
SER   H    H  N N 370 
SER   H2   H  N N 371 
SER   HA   H  N N 372 
SER   HB2  H  N N 373 
SER   HB3  H  N N 374 
SER   HG   H  N N 375 
SER   HXT  H  N N 376 
TFA   C1   C  N N 377 
TFA   C2   C  N N 378 
TFA   O    O  N N 379 
TFA   F1   F  N N 380 
TFA   F2   F  N N 381 
TFA   F3   F  N N 382 
TFA   OXT  O  N N 383 
TFA   HXT  H  N N 384 
THR   N    N  N N 385 
THR   CA   C  N S 386 
THR   C    C  N N 387 
THR   O    O  N N 388 
THR   CB   C  N R 389 
THR   OG1  O  N N 390 
THR   CG2  C  N N 391 
THR   OXT  O  N N 392 
THR   H    H  N N 393 
THR   H2   H  N N 394 
THR   HA   H  N N 395 
THR   HB   H  N N 396 
THR   HG1  H  N N 397 
THR   HG21 H  N N 398 
THR   HG22 H  N N 399 
THR   HG23 H  N N 400 
THR   HXT  H  N N 401 
TYR   N    N  N N 402 
TYR   CA   C  N S 403 
TYR   C    C  N N 404 
TYR   O    O  N N 405 
TYR   CB   C  N N 406 
TYR   CG   C  Y N 407 
TYR   CD1  C  Y N 408 
TYR   CD2  C  Y N 409 
TYR   CE1  C  Y N 410 
TYR   CE2  C  Y N 411 
TYR   CZ   C  Y N 412 
TYR   OH   O  N N 413 
TYR   OXT  O  N N 414 
TYR   H    H  N N 415 
TYR   H2   H  N N 416 
TYR   HA   H  N N 417 
TYR   HB2  H  N N 418 
TYR   HB3  H  N N 419 
TYR   HD1  H  N N 420 
TYR   HD2  H  N N 421 
TYR   HE1  H  N N 422 
TYR   HE2  H  N N 423 
TYR   HH   H  N N 424 
TYR   HXT  H  N N 425 
VAL   N    N  N N 426 
VAL   CA   C  N S 427 
VAL   C    C  N N 428 
VAL   O    O  N N 429 
VAL   CB   C  N N 430 
VAL   CG1  C  N N 431 
VAL   CG2  C  N N 432 
VAL   OXT  O  N N 433 
VAL   H    H  N N 434 
VAL   H2   H  N N 435 
VAL   HA   H  N N 436 
VAL   HB   H  N N 437 
VAL   HG11 H  N N 438 
VAL   HG12 H  N N 439 
VAL   HG13 H  N N 440 
VAL   HG21 H  N N 441 
VAL   HG22 H  N N 442 
VAL   HG23 H  N N 443 
VAL   HXT  H  N N 444 
# 
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 
A1A80 C6  C5   doub Y N 1   
A1A80 C6  C7   sing Y N 2   
A1A80 C5  C4   sing Y N 3   
A1A80 F1  C7   sing N N 4   
A1A80 C7  C8   doub Y N 5   
A1A80 C4  C3   sing N N 6   
A1A80 C4  C9   doub Y N 7   
A1A80 C3  C2   sing N N 8   
A1A80 C8  C9   sing Y N 9   
A1A80 O1  C1   sing N N 10  
A1A80 C1  C2   sing N N 11  
A1A80 C2  N1   sing N N 12  
A1A80 N1  C10  sing N N 13  
A1A80 C10 C13  doub Y N 14  
A1A80 C10 N2   sing Y N 15  
A1A80 C14 C13  sing Y N 16  
A1A80 C14 C15  doub Y N 17  
A1A80 C13 C12  sing Y N 18  
A1A80 N2  C11  doub Y N 19  
A1A80 C15 N4   sing Y N 20  
A1A80 C11 N3   sing Y N 21  
A1A80 C12 N4   sing Y N 22  
A1A80 C12 N3   doub Y N 23  
A1A80 C3  H5   sing N N 24  
A1A80 C3  H6   sing N N 25  
A1A80 C6  H8   sing N N 26  
A1A80 C9  H10  sing N N 27  
A1A80 C14 H13  sing N N 28  
A1A80 C1  H3   sing N N 29  
A1A80 C1  H4   sing N N 30  
A1A80 C11 H12  sing N N 31  
A1A80 C15 H14  sing N N 32  
A1A80 C2  H1   sing N N 33  
A1A80 C5  H7   sing N N 34  
A1A80 C8  H9   sing N N 35  
A1A80 N1  H11  sing N N 36  
A1A80 N4  H15  sing N N 37  
A1A80 O1  H2   sing N N 38  
A1A8Z F1  C7   sing N N 39  
A1A8Z C6  C7   doub Y N 40  
A1A8Z C6  C5   sing Y N 41  
A1A8Z C7  C8   sing Y N 42  
A1A8Z C5  C4   doub Y N 43  
A1A8Z C8  C9   doub Y N 44  
A1A8Z C4  C9   sing Y N 45  
A1A8Z C4  C3   sing N N 46  
A1A8Z O1  C1   sing N N 47  
A1A8Z C2  C3   sing N N 48  
A1A8Z C2  C1   sing N N 49  
A1A8Z C2  N1   sing N N 50  
A1A8Z N1  C10  sing N N 51  
A1A8Z C10 C13  doub Y N 52  
A1A8Z C10 N2   sing Y N 53  
A1A8Z C14 C13  sing Y N 54  
A1A8Z C14 C15  doub Y N 55  
A1A8Z C13 C12  sing Y N 56  
A1A8Z N2  C11  doub Y N 57  
A1A8Z C15 N4   sing Y N 58  
A1A8Z C11 N3   sing Y N 59  
A1A8Z C12 N4   sing Y N 60  
A1A8Z C12 N3   doub Y N 61  
A1A8Z O1  H2   sing N N 62  
A1A8Z C1  H4   sing N N 63  
A1A8Z C1  H3   sing N N 64  
A1A8Z C2  H1   sing N N 65  
A1A8Z C3  H5   sing N N 66  
A1A8Z C3  H6   sing N N 67  
A1A8Z C5  H7   sing N N 68  
A1A8Z C6  H8   sing N N 69  
A1A8Z C8  H9   sing N N 70  
A1A8Z C11 H12  sing N N 71  
A1A8Z C14 H13  sing N N 72  
A1A8Z C15 H14  sing N N 73  
A1A8Z C9  H10  sing N N 74  
A1A8Z N1  H11  sing N N 75  
A1A8Z N4  H15  sing N N 76  
ALA   N   CA   sing N N 77  
ALA   N   H    sing N N 78  
ALA   N   H2   sing N N 79  
ALA   CA  C    sing N N 80  
ALA   CA  CB   sing N N 81  
ALA   CA  HA   sing N N 82  
ALA   C   O    doub N N 83  
ALA   C   OXT  sing N N 84  
ALA   CB  HB1  sing N N 85  
ALA   CB  HB2  sing N N 86  
ALA   CB  HB3  sing N N 87  
ALA   OXT HXT  sing N N 88  
ARG   N   CA   sing N N 89  
ARG   N   H    sing N N 90  
ARG   N   H2   sing N N 91  
ARG   CA  C    sing N N 92  
ARG   CA  CB   sing N N 93  
ARG   CA  HA   sing N N 94  
ARG   C   O    doub N N 95  
ARG   C   OXT  sing N N 96  
ARG   CB  CG   sing N N 97  
ARG   CB  HB2  sing N N 98  
ARG   CB  HB3  sing N N 99  
ARG   CG  CD   sing N N 100 
ARG   CG  HG2  sing N N 101 
ARG   CG  HG3  sing N N 102 
ARG   CD  NE   sing N N 103 
ARG   CD  HD2  sing N N 104 
ARG   CD  HD3  sing N N 105 
ARG   NE  CZ   sing N N 106 
ARG   NE  HE   sing N N 107 
ARG   CZ  NH1  sing N N 108 
ARG   CZ  NH2  doub N N 109 
ARG   NH1 HH11 sing N N 110 
ARG   NH1 HH12 sing N N 111 
ARG   NH2 HH21 sing N N 112 
ARG   NH2 HH22 sing N N 113 
ARG   OXT HXT  sing N N 114 
ASN   N   CA   sing N N 115 
ASN   N   H    sing N N 116 
ASN   N   H2   sing N N 117 
ASN   CA  C    sing N N 118 
ASN   CA  CB   sing N N 119 
ASN   CA  HA   sing N N 120 
ASN   C   O    doub N N 121 
ASN   C   OXT  sing N N 122 
ASN   CB  CG   sing N N 123 
ASN   CB  HB2  sing N N 124 
ASN   CB  HB3  sing N N 125 
ASN   CG  OD1  doub N N 126 
ASN   CG  ND2  sing N N 127 
ASN   ND2 HD21 sing N N 128 
ASN   ND2 HD22 sing N N 129 
ASN   OXT HXT  sing N N 130 
ASP   N   CA   sing N N 131 
ASP   N   H    sing N N 132 
ASP   N   H2   sing N N 133 
ASP   CA  C    sing N N 134 
ASP   CA  CB   sing N N 135 
ASP   CA  HA   sing N N 136 
ASP   C   O    doub N N 137 
ASP   C   OXT  sing N N 138 
ASP   CB  CG   sing N N 139 
ASP   CB  HB2  sing N N 140 
ASP   CB  HB3  sing N N 141 
ASP   CG  OD1  doub N N 142 
ASP   CG  OD2  sing N N 143 
ASP   OD2 HD2  sing N N 144 
ASP   OXT HXT  sing N N 145 
CYS   N   CA   sing N N 146 
CYS   N   H    sing N N 147 
CYS   N   H2   sing N N 148 
CYS   CA  C    sing N N 149 
CYS   CA  CB   sing N N 150 
CYS   CA  HA   sing N N 151 
CYS   C   O    doub N N 152 
CYS   C   OXT  sing N N 153 
CYS   CB  SG   sing N N 154 
CYS   CB  HB2  sing N N 155 
CYS   CB  HB3  sing N N 156 
CYS   SG  HG   sing N N 157 
CYS   OXT HXT  sing N N 158 
GLN   N   CA   sing N N 159 
GLN   N   H    sing N N 160 
GLN   N   H2   sing N N 161 
GLN   CA  C    sing N N 162 
GLN   CA  CB   sing N N 163 
GLN   CA  HA   sing N N 164 
GLN   C   O    doub N N 165 
GLN   C   OXT  sing N N 166 
GLN   CB  CG   sing N N 167 
GLN   CB  HB2  sing N N 168 
GLN   CB  HB3  sing N N 169 
GLN   CG  CD   sing N N 170 
GLN   CG  HG2  sing N N 171 
GLN   CG  HG3  sing N N 172 
GLN   CD  OE1  doub N N 173 
GLN   CD  NE2  sing N N 174 
GLN   NE2 HE21 sing N N 175 
GLN   NE2 HE22 sing N N 176 
GLN   OXT HXT  sing N N 177 
GLU   N   CA   sing N N 178 
GLU   N   H    sing N N 179 
GLU   N   H2   sing N N 180 
GLU   CA  C    sing N N 181 
GLU   CA  CB   sing N N 182 
GLU   CA  HA   sing N N 183 
GLU   C   O    doub N N 184 
GLU   C   OXT  sing N N 185 
GLU   CB  CG   sing N N 186 
GLU   CB  HB2  sing N N 187 
GLU   CB  HB3  sing N N 188 
GLU   CG  CD   sing N N 189 
GLU   CG  HG2  sing N N 190 
GLU   CG  HG3  sing N N 191 
GLU   CD  OE1  doub N N 192 
GLU   CD  OE2  sing N N 193 
GLU   OE2 HE2  sing N N 194 
GLU   OXT HXT  sing N N 195 
GLY   N   CA   sing N N 196 
GLY   N   H    sing N N 197 
GLY   N   H2   sing N N 198 
GLY   CA  C    sing N N 199 
GLY   CA  HA2  sing N N 200 
GLY   CA  HA3  sing N N 201 
GLY   C   O    doub N N 202 
GLY   C   OXT  sing N N 203 
GLY   OXT HXT  sing N N 204 
HIS   N   CA   sing N N 205 
HIS   N   H    sing N N 206 
HIS   N   H2   sing N N 207 
HIS   CA  C    sing N N 208 
HIS   CA  CB   sing N N 209 
HIS   CA  HA   sing N N 210 
HIS   C   O    doub N N 211 
HIS   C   OXT  sing N N 212 
HIS   CB  CG   sing N N 213 
HIS   CB  HB2  sing N N 214 
HIS   CB  HB3  sing N N 215 
HIS   CG  ND1  sing Y N 216 
HIS   CG  CD2  doub Y N 217 
HIS   ND1 CE1  doub Y N 218 
HIS   ND1 HD1  sing N N 219 
HIS   CD2 NE2  sing Y N 220 
HIS   CD2 HD2  sing N N 221 
HIS   CE1 NE2  sing Y N 222 
HIS   CE1 HE1  sing N N 223 
HIS   NE2 HE2  sing N N 224 
HIS   OXT HXT  sing N N 225 
HOH   O   H1   sing N N 226 
HOH   O   H2   sing N N 227 
ILE   N   CA   sing N N 228 
ILE   N   H    sing N N 229 
ILE   N   H2   sing N N 230 
ILE   CA  C    sing N N 231 
ILE   CA  CB   sing N N 232 
ILE   CA  HA   sing N N 233 
ILE   C   O    doub N N 234 
ILE   C   OXT  sing N N 235 
ILE   CB  CG1  sing N N 236 
ILE   CB  CG2  sing N N 237 
ILE   CB  HB   sing N N 238 
ILE   CG1 CD1  sing N N 239 
ILE   CG1 HG12 sing N N 240 
ILE   CG1 HG13 sing N N 241 
ILE   CG2 HG21 sing N N 242 
ILE   CG2 HG22 sing N N 243 
ILE   CG2 HG23 sing N N 244 
ILE   CD1 HD11 sing N N 245 
ILE   CD1 HD12 sing N N 246 
ILE   CD1 HD13 sing N N 247 
ILE   OXT HXT  sing N N 248 
LEU   N   CA   sing N N 249 
LEU   N   H    sing N N 250 
LEU   N   H2   sing N N 251 
LEU   CA  C    sing N N 252 
LEU   CA  CB   sing N N 253 
LEU   CA  HA   sing N N 254 
LEU   C   O    doub N N 255 
LEU   C   OXT  sing N N 256 
LEU   CB  CG   sing N N 257 
LEU   CB  HB2  sing N N 258 
LEU   CB  HB3  sing N N 259 
LEU   CG  CD1  sing N N 260 
LEU   CG  CD2  sing N N 261 
LEU   CG  HG   sing N N 262 
LEU   CD1 HD11 sing N N 263 
LEU   CD1 HD12 sing N N 264 
LEU   CD1 HD13 sing N N 265 
LEU   CD2 HD21 sing N N 266 
LEU   CD2 HD22 sing N N 267 
LEU   CD2 HD23 sing N N 268 
LEU   OXT HXT  sing N N 269 
LYS   N   CA   sing N N 270 
LYS   N   H    sing N N 271 
LYS   N   H2   sing N N 272 
LYS   CA  C    sing N N 273 
LYS   CA  CB   sing N N 274 
LYS   CA  HA   sing N N 275 
LYS   C   O    doub N N 276 
LYS   C   OXT  sing N N 277 
LYS   CB  CG   sing N N 278 
LYS   CB  HB2  sing N N 279 
LYS   CB  HB3  sing N N 280 
LYS   CG  CD   sing N N 281 
LYS   CG  HG2  sing N N 282 
LYS   CG  HG3  sing N N 283 
LYS   CD  CE   sing N N 284 
LYS   CD  HD2  sing N N 285 
LYS   CD  HD3  sing N N 286 
LYS   CE  NZ   sing N N 287 
LYS   CE  HE2  sing N N 288 
LYS   CE  HE3  sing N N 289 
LYS   NZ  HZ1  sing N N 290 
LYS   NZ  HZ2  sing N N 291 
LYS   NZ  HZ3  sing N N 292 
LYS   OXT HXT  sing N N 293 
MET   N   CA   sing N N 294 
MET   N   H    sing N N 295 
MET   N   H2   sing N N 296 
MET   CA  C    sing N N 297 
MET   CA  CB   sing N N 298 
MET   CA  HA   sing N N 299 
MET   C   O    doub N N 300 
MET   C   OXT  sing N N 301 
MET   CB  CG   sing N N 302 
MET   CB  HB2  sing N N 303 
MET   CB  HB3  sing N N 304 
MET   CG  SD   sing N N 305 
MET   CG  HG2  sing N N 306 
MET   CG  HG3  sing N N 307 
MET   SD  CE   sing N N 308 
MET   CE  HE1  sing N N 309 
MET   CE  HE2  sing N N 310 
MET   CE  HE3  sing N N 311 
MET   OXT HXT  sing N N 312 
PHE   N   CA   sing N N 313 
PHE   N   H    sing N N 314 
PHE   N   H2   sing N N 315 
PHE   CA  C    sing N N 316 
PHE   CA  CB   sing N N 317 
PHE   CA  HA   sing N N 318 
PHE   C   O    doub N N 319 
PHE   C   OXT  sing N N 320 
PHE   CB  CG   sing N N 321 
PHE   CB  HB2  sing N N 322 
PHE   CB  HB3  sing N N 323 
PHE   CG  CD1  doub Y N 324 
PHE   CG  CD2  sing Y N 325 
PHE   CD1 CE1  sing Y N 326 
PHE   CD1 HD1  sing N N 327 
PHE   CD2 CE2  doub Y N 328 
PHE   CD2 HD2  sing N N 329 
PHE   CE1 CZ   doub Y N 330 
PHE   CE1 HE1  sing N N 331 
PHE   CE2 CZ   sing Y N 332 
PHE   CE2 HE2  sing N N 333 
PHE   CZ  HZ   sing N N 334 
PHE   OXT HXT  sing N N 335 
PRO   N   CA   sing N N 336 
PRO   N   CD   sing N N 337 
PRO   N   H    sing N N 338 
PRO   CA  C    sing N N 339 
PRO   CA  CB   sing N N 340 
PRO   CA  HA   sing N N 341 
PRO   C   O    doub N N 342 
PRO   C   OXT  sing N N 343 
PRO   CB  CG   sing N N 344 
PRO   CB  HB2  sing N N 345 
PRO   CB  HB3  sing N N 346 
PRO   CG  CD   sing N N 347 
PRO   CG  HG2  sing N N 348 
PRO   CG  HG3  sing N N 349 
PRO   CD  HD2  sing N N 350 
PRO   CD  HD3  sing N N 351 
PRO   OXT HXT  sing N N 352 
SER   N   CA   sing N N 353 
SER   N   H    sing N N 354 
SER   N   H2   sing N N 355 
SER   CA  C    sing N N 356 
SER   CA  CB   sing N N 357 
SER   CA  HA   sing N N 358 
SER   C   O    doub N N 359 
SER   C   OXT  sing N N 360 
SER   CB  OG   sing N N 361 
SER   CB  HB2  sing N N 362 
SER   CB  HB3  sing N N 363 
SER   OG  HG   sing N N 364 
SER   OXT HXT  sing N N 365 
TFA   C1  C2   sing N N 366 
TFA   C1  O    doub N N 367 
TFA   C1  OXT  sing N N 368 
TFA   C2  F1   sing N N 369 
TFA   C2  F2   sing N N 370 
TFA   C2  F3   sing N N 371 
TFA   OXT HXT  sing N N 372 
THR   N   CA   sing N N 373 
THR   N   H    sing N N 374 
THR   N   H2   sing N N 375 
THR   CA  C    sing N N 376 
THR   CA  CB   sing N N 377 
THR   CA  HA   sing N N 378 
THR   C   O    doub N N 379 
THR   C   OXT  sing N N 380 
THR   CB  OG1  sing N N 381 
THR   CB  CG2  sing N N 382 
THR   CB  HB   sing N N 383 
THR   OG1 HG1  sing N N 384 
THR   CG2 HG21 sing N N 385 
THR   CG2 HG22 sing N N 386 
THR   CG2 HG23 sing N N 387 
THR   OXT HXT  sing N N 388 
TYR   N   CA   sing N N 389 
TYR   N   H    sing N N 390 
TYR   N   H2   sing N N 391 
TYR   CA  C    sing N N 392 
TYR   CA  CB   sing N N 393 
TYR   CA  HA   sing N N 394 
TYR   C   O    doub N N 395 
TYR   C   OXT  sing N N 396 
TYR   CB  CG   sing N N 397 
TYR   CB  HB2  sing N N 398 
TYR   CB  HB3  sing N N 399 
TYR   CG  CD1  doub Y N 400 
TYR   CG  CD2  sing Y N 401 
TYR   CD1 CE1  sing Y N 402 
TYR   CD1 HD1  sing N N 403 
TYR   CD2 CE2  doub Y N 404 
TYR   CD2 HD2  sing N N 405 
TYR   CE1 CZ   doub Y N 406 
TYR   CE1 HE1  sing N N 407 
TYR   CE2 CZ   sing Y N 408 
TYR   CE2 HE2  sing N N 409 
TYR   CZ  OH   sing N N 410 
TYR   OH  HH   sing N N 411 
TYR   OXT HXT  sing N N 412 
VAL   N   CA   sing N N 413 
VAL   N   H    sing N N 414 
VAL   N   H2   sing N N 415 
VAL   CA  C    sing N N 416 
VAL   CA  CB   sing N N 417 
VAL   CA  HA   sing N N 418 
VAL   C   O    doub N N 419 
VAL   C   OXT  sing N N 420 
VAL   CB  CG1  sing N N 421 
VAL   CB  CG2  sing N N 422 
VAL   CB  HB   sing N N 423 
VAL   CG1 HG11 sing N N 424 
VAL   CG1 HG12 sing N N 425 
VAL   CG1 HG13 sing N N 426 
VAL   CG2 HG21 sing N N 427 
VAL   CG2 HG22 sing N N 428 
VAL   CG2 HG23 sing N N 429 
VAL   OXT HXT  sing N N 430 
# 
_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                    7HDR 
_atom_sites.fract_transf_matrix[1][1]   0.011272 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011272 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.025342 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . VAL   A 1 3   ? 19.535 -16.135 22.224  1.00 56.50 ?  3   VAL   A N    1 
ATOM   2    C  CA   . VAL   A 1 3   ? 18.591 -15.039 22.412  1.00 55.87 ?  3   VAL   A CA   1 
ATOM   3    C  C    . VAL   A 1 3   ? 19.256 -13.708 22.084  1.00 53.40 ?  3   VAL   A C    1 
ATOM   4    O  O    . VAL   A 1 3   ? 20.377 -13.442 22.518  1.00 54.12 ?  3   VAL   A O    1 
ATOM   5    C  CB   . VAL   A 1 3   ? 18.005 -15.042 23.840  1.00 57.19 ?  3   VAL   A CB   1 
ATOM   6    C  CG1  . VAL   A 1 3   ? 16.986 -13.920 24.005  1.00 57.59 ?  3   VAL   A CG1  1 
ATOM   7    C  CG2  . VAL   A 1 3   ? 17.372 -16.391 24.150  1.00 57.61 ?  3   VAL   A CG2  1 
ATOM   8    H  HA   . VAL   A 1 3   ? 17.853 -15.152 21.800  1.00 67.03 ?  3   VAL   A HA   1 
ATOM   9    H  HB   . VAL   A 1 3   ? 18.718 -14.893 24.479  1.00 68.61 ?  3   VAL   A HB   1 
ATOM   10   H  HG11 . VAL   A 1 3   ? 16.511 -14.046 24.842  1.00 69.09 ?  3   VAL   A HG11 1 
ATOM   11   H  HG12 . VAL   A 1 3   ? 17.449 -13.068 24.014  1.00 69.09 ?  3   VAL   A HG12 1 
ATOM   12   H  HG13 . VAL   A 1 3   ? 16.360 -13.951 23.264  1.00 69.09 ?  3   VAL   A HG13 1 
ATOM   13   H  HG21 . VAL   A 1 3   ? 16.938 -16.344 25.016  1.00 69.12 ?  3   VAL   A HG21 1 
ATOM   14   H  HG22 . VAL   A 1 3   ? 16.719 -16.597 23.463  1.00 69.12 ?  3   VAL   A HG22 1 
ATOM   15   H  HG23 . VAL   A 1 3   ? 18.065 -17.069 24.164  1.00 69.12 ?  3   VAL   A HG23 1 
ATOM   16   N  N    . ASN   A 1 4   ? 18.564 -12.879 21.303  1.00 49.65 ?  4   ASN   A N    1 
ATOM   17   C  CA   . ASN   A 1 4   ? 19.015 -11.527 20.995  1.00 45.47 ?  4   ASN   A CA   1 
ATOM   18   C  C    . ASN   A 1 4   ? 17.883 -10.544 21.288  1.00 41.38 ?  4   ASN   A C    1 
ATOM   19   O  O    . ASN   A 1 4   ? 16.789 -10.931 21.713  1.00 41.40 ?  4   ASN   A O    1 
ATOM   20   C  CB   . ASN   A 1 4   ? 19.553 -11.415 19.561  1.00 44.97 ?  4   ASN   A CB   1 
ATOM   21   C  CG   . ASN   A 1 4   ? 18.546 -11.842 18.520  1.00 44.34 ?  4   ASN   A CG   1 
ATOM   22   O  OD1  . ASN   A 1 4   ? 17.415 -11.357 18.496  1.00 44.15 ?  4   ASN   A OD1  1 
ATOM   23   N  ND2  . ASN   A 1 4   ? 18.952 -12.762 17.648  1.00 44.12 ?  4   ASN   A ND2  1 
ATOM   24   H  H    . ASN   A 1 4   ? 17.813 -13.084 20.933  1.00 59.56 ?  4   ASN   A H    1 
ATOM   25   H  HA   . ASN   A 1 4   ? 19.748 -11.313 21.585  1.00 54.55 ?  4   ASN   A HA   1 
ATOM   26   H  HB2  . ASN   A 1 4   ? 19.795 -10.491 19.385  1.00 53.94 ?  4   ASN   A HB2  1 
ATOM   27   H  HB3  . ASN   A 1 4   ? 20.335 -11.982 19.473  1.00 53.94 ?  4   ASN   A HB3  1 
ATOM   28   H  HD21 . ASN   A 1 4   ? 18.419 -13.039 17.033  1.00 52.92 ?  4   ASN   A HD21 1 
ATOM   29   H  HD22 . ASN   A 1 4   ? 19.751 -13.080 17.698  1.00 52.92 ?  4   ASN   A HD22 1 
ATOM   30   N  N    A SER   A 1 5   ? 18.151 -9.260  21.058  0.72 39.06 ?  5   SER   A N    1 
ATOM   31   N  N    B SER   A 1 5   ? 18.152 -9.260  21.053  0.28 39.35 ?  5   SER   A N    1 
ATOM   32   C  CA   A SER   A 1 5   ? 17.240 -8.187  21.437  0.72 36.72 ?  5   SER   A CA   1 
ATOM   33   C  CA   B SER   A 1 5   ? 17.246 -8.185  21.435  0.28 37.16 ?  5   SER   A CA   1 
ATOM   34   C  C    A SER   A 1 5   ? 16.371 -7.698  20.282  0.72 33.81 ?  5   SER   A C    1 
ATOM   35   C  C    B SER   A 1 5   ? 16.361 -7.706  20.289  0.28 34.20 ?  5   SER   A C    1 
ATOM   36   O  O    A SER   A 1 5   ? 15.705 -6.666  20.418  0.72 33.66 ?  5   SER   A O    1 
ATOM   37   O  O    B SER   A 1 5   ? 15.673 -6.691  20.437  0.28 34.33 ?  5   SER   A O    1 
ATOM   38   C  CB   A SER   A 1 5   ? 18.018 -7.017  22.043  0.72 37.41 ?  5   SER   A CB   1 
ATOM   39   C  CB   B SER   A 1 5   ? 18.035 -7.008  22.015  0.28 37.84 ?  5   SER   A CB   1 
ATOM   40   O  OG   A SER   A 1 5   ? 18.993 -6.529  21.138  0.72 37.78 ?  5   SER   A OG   1 
ATOM   41   O  OG   B SER   A 1 5   ? 18.917 -6.460  21.051  0.28 38.17 ?  5   SER   A OG   1 
ATOM   42   H  H    A SER   A 1 5   ? 18.868 -8.984  20.673  0.72 46.85 ?  5   SER   A H    1 
ATOM   43   H  H    B SER   A 1 5   ? 18.867 -8.987  20.662  0.28 47.20 ?  5   SER   A H    1 
ATOM   44   H  HA   A SER   A 1 5   ? 16.648 -8.522  22.126  0.72 44.04 ?  5   SER   A HA   1 
ATOM   45   H  HA   B SER   A 1 5   ? 16.664 -8.511  22.138  0.28 44.57 ?  5   SER   A HA   1 
ATOM   46   H  HB2  A SER   A 1 5   ? 17.399 -6.299  22.250  0.72 44.87 ?  5   SER   A HB2  1 
ATOM   47   H  HB2  B SER   A 1 5   ? 17.411 -6.320  22.300  0.28 45.38 ?  5   SER   A HB2  1 
ATOM   48   H  HB3  A SER   A 1 5   ? 18.459 -7.316  22.855  0.72 44.87 ?  5   SER   A HB3  1 
ATOM   49   H  HB3  B SER   A 1 5   ? 18.553 -7.318  22.775  0.28 45.38 ?  5   SER   A HB3  1 
ATOM   50   H  HG   A SER   A 1 5   ? 19.416 -5.891  21.488  0.72 45.31 ?  5   SER   A HG   1 
ATOM   51   H  HG   B SER   A 1 5   ? 19.341 -5.814  21.383  0.28 45.78 ?  5   SER   A HG   1 
ATOM   52   N  N    . PHE   A 1 6   ? 16.361 -8.402  19.154  1.00 30.91 ?  6   PHE   A N    1 
ATOM   53   C  CA   . PHE   A 1 6   ? 15.465 -8.035  18.063  1.00 25.35 ?  6   PHE   A CA   1 
ATOM   54   C  C    . PHE   A 1 6   ? 14.035 -8.402  18.445  1.00 24.06 ?  6   PHE   A C    1 
ATOM   55   O  O    . PHE   A 1 6   ? 13.779 -9.498  18.946  1.00 25.27 ?  6   PHE   A O    1 
ATOM   56   C  CB   . PHE   A 1 6   ? 15.873 -8.752  16.779  1.00 22.39 ?  6   PHE   A CB   1 
ATOM   57   C  CG   . PHE   A 1 6   ? 17.164 -8.243  16.187  1.00 20.49 ?  6   PHE   A CG   1 
ATOM   58   C  CD1  . PHE   A 1 6   ? 17.194 -7.056  15.477  1.00 19.80 ?  6   PHE   A CD1  1 
ATOM   59   C  CD2  . PHE   A 1 6   ? 18.341 -8.956  16.339  1.00 20.52 ?  6   PHE   A CD2  1 
ATOM   60   C  CE1  . PHE   A 1 6   ? 18.373 -6.587  14.928  1.00 19.62 ?  6   PHE   A CE1  1 
ATOM   61   C  CE2  . PHE   A 1 6   ? 19.521 -8.496  15.792  1.00 20.59 ?  6   PHE   A CE2  1 
ATOM   62   C  CZ   . PHE   A 1 6   ? 19.537 -7.306  15.087  1.00 20.00 ?  6   PHE   A CZ   1 
ATOM   63   H  H    A PHE   A 1 6   ? 16.854 -9.090  18.998  0.72 37.07 ?  6   PHE   A H    1 
ATOM   64   H  H    B PHE   A 1 6   ? 16.861 -9.084  18.994  0.28 37.07 ?  6   PHE   A H    1 
ATOM   65   H  HA   . PHE   A 1 6   ? 15.506 -7.084  17.917  1.00 30.39 ?  6   PHE   A HA   1 
ATOM   66   H  HB2  . PHE   A 1 6   ? 15.985 -9.698  16.969  1.00 26.84 ?  6   PHE   A HB2  1 
ATOM   67   H  HB3  . PHE   A 1 6   ? 15.174 -8.631  16.119  1.00 26.84 ?  6   PHE   A HB3  1 
ATOM   68   H  HD1  . PHE   A 1 6   ? 16.409 -6.570  15.367  1.00 23.74 ?  6   PHE   A HD1  1 
ATOM   69   H  HD2  . PHE   A 1 6   ? 18.333 -9.758  16.817  1.00 24.60 ?  6   PHE   A HD2  1 
ATOM   70   H  HE1  . PHE   A 1 6   ? 18.381 -5.788  14.452  1.00 23.52 ?  6   PHE   A HE1  1 
ATOM   71   H  HE2  . PHE   A 1 6   ? 20.307 -8.982  15.904  1.00 24.69 ?  6   PHE   A HE2  1 
ATOM   72   H  HZ   . PHE   A 1 6   ? 20.330 -6.993  14.720  1.00 23.98 ?  6   PHE   A HZ   1 
ATOM   73   N  N    A SER   A 1 7   ? 13.098 -7.486  18.192  0.72 22.69 ?  7   SER   A N    1 
ATOM   74   N  N    B SER   A 1 7   ? 13.102 -7.477  18.217  0.28 23.47 ?  7   SER   A N    1 
ATOM   75   C  CA   A SER   A 1 7   ? 11.726 -7.623  18.667  0.72 22.85 ?  7   SER   A CA   1 
ATOM   76   C  CA   B SER   A 1 7   ? 11.732 -7.616  18.689  0.28 23.24 ?  7   SER   A CA   1 
ATOM   77   C  C    A SER   A 1 7   ? 10.730 -7.383  17.539  0.72 20.51 ?  7   SER   A C    1 
ATOM   78   C  C    B SER   A 1 7   ? 10.748 -7.352  17.558  0.28 21.50 ?  7   SER   A C    1 
ATOM   79   O  O    A SER   A 1 7   ? 10.913 -6.478  16.718  0.72 20.82 ?  7   SER   A O    1 
ATOM   80   O  O    B SER   A 1 7   ? 11.022 -6.574  16.640  0.28 21.55 ?  7   SER   A O    1 
ATOM   81   C  CB   A SER   A 1 7   ? 11.457 -6.628  19.805  0.72 25.37 ?  7   SER   A CB   1 
ATOM   82   C  CB   B SER   A 1 7   ? 11.449 -6.642  19.843  0.28 24.64 ?  7   SER   A CB   1 
ATOM   83   O  OG   A SER   A 1 7   ? 10.120 -6.717  20.258  0.72 27.00 ?  7   SER   A OG   1 
ATOM   84   O  OG   B SER   A 1 7   ? 10.094 -6.710  20.249  0.28 25.62 ?  7   SER   A OG   1 
ATOM   85   H  H    A SER   A 1 7   ? 13.240 -6.771  17.738  0.72 27.20 ?  7   SER   A H    1 
ATOM   86   H  H    B SER   A 1 7   ? 13.245 -6.751  17.781  0.28 28.14 ?  7   SER   A H    1 
ATOM   87   H  HA   A SER   A 1 7   ? 11.589 -8.520  19.009  0.72 27.40 ?  7   SER   A HA   1 
ATOM   88   H  HA   B SER   A 1 7   ? 11.587 -8.518  19.012  0.28 27.87 ?  7   SER   A HA   1 
ATOM   89   H  HB2  A SER   A 1 7   ? 12.055 -6.827  20.545  0.72 30.42 ?  7   SER   A HB2  1 
ATOM   90   H  HB2  B SER   A 1 7   ? 12.014 -6.874  20.596  0.28 29.54 ?  7   SER   A HB2  1 
ATOM   91   H  HB3  A SER   A 1 7   ? 11.622 -5.728  19.482  0.72 30.42 ?  7   SER   A HB3  1 
ATOM   92   H  HB3  B SER   A 1 7   ? 11.646 -5.739  19.548  0.28 29.54 ?  7   SER   A HB3  1 
ATOM   93   H  HG   A SER   A 1 7   ? 9.989  -6.168  20.880  0.72 32.38 ?  7   SER   A HG   1 
ATOM   94   H  HG   B SER   A 1 7   ? 9.955  -6.171  20.879  0.28 30.72 ?  7   SER   A HG   1 
ATOM   95   N  N    A GLY   A 1 8   ? 9.674  -8.198  17.505  0.72 18.57 ?  8   GLY   A N    1 
ATOM   96   N  N    B GLY   A 1 8   ? 9.592  -8.012  17.639  0.28 19.94 ?  8   GLY   A N    1 
ATOM   97   C  CA   A GLY   A 1 8   ? 8.577  -7.965  16.586  0.72 17.45 ?  8   GLY   A CA   1 
ATOM   98   C  CA   B GLY   A 1 8   ? 8.520  -7.800  16.688  0.28 18.67 ?  8   GLY   A CA   1 
ATOM   99   C  C    A GLY   A 1 8   ? 8.788  -8.452  15.173  0.72 16.01 ?  8   GLY   A C    1 
ATOM   100  C  C    B GLY   A 1 8   ? 8.766  -8.339  15.302  0.28 17.28 ?  8   GLY   A C    1 
ATOM   101  O  O    A GLY   A 1 8   ? 8.049  -8.036  14.276  0.72 16.89 ?  8   GLY   A O    1 
ATOM   102  O  O    B GLY   A 1 8   ? 8.020  -7.992  14.381  0.28 17.46 ?  8   GLY   A O    1 
ATOM   103  H  H    A GLY   A 1 8   ? 9.578  -8.893  18.004  0.72 22.26 ?  8   GLY   A H    1 
ATOM   104  H  H    B GLY   A 1 8   ? 9.408  -8.595  18.244  0.28 23.90 ?  8   GLY   A H    1 
ATOM   105  H  HA2  A GLY   A 1 8   ? 7.784  -8.401  16.935  0.72 20.92 ?  8   GLY   A HA2  1 
ATOM   106  H  HA2  B GLY   A 1 8   ? 7.712  -8.217  17.025  0.28 22.38 ?  8   GLY   A HA2  1 
ATOM   107  H  HA3  A GLY   A 1 8   ? 8.403  -7.014  16.546  0.72 20.92 ?  8   GLY   A HA3  1 
ATOM   108  H  HA3  B GLY   A 1 8   ? 8.355  -6.850  16.604  0.28 22.38 ?  8   GLY   A HA3  1 
ATOM   109  N  N    A TYR   A 1 9   ? 9.767  -9.323  14.943  0.72 14.82 ?  9   TYR   A N    1 
ATOM   110  N  N    B TYR   A 1 9   ? 9.781  -9.177  15.115  0.28 16.13 ?  9   TYR   A N    1 
ATOM   111  C  CA   A TYR   A 1 9   ? 10.020 -9.857  13.615  0.72 13.64 ?  9   TYR   A CA   1 
ATOM   112  C  CA   B TYR   A 1 9   ? 10.102 -9.701  13.796  0.28 15.02 ?  9   TYR   A CA   1 
ATOM   113  C  C    A TYR   A 1 9   ? 9.159  -11.084 13.356  0.72 13.02 ?  9   TYR   A C    1 
ATOM   114  C  C    B TYR   A 1 9   ? 9.264  -10.932 13.481  0.28 14.33 ?  9   TYR   A C    1 
ATOM   115  O  O    A TYR   A 1 9   ? 8.863  -11.877 14.256  0.72 14.52 ?  9   TYR   A O    1 
ATOM   116  O  O    B TYR   A 1 9   ? 9.179  -11.863 14.289  0.28 14.71 ?  9   TYR   A O    1 
ATOM   117  C  CB   A TYR   A 1 9   ? 11.496 -10.243 13.442  0.72 13.92 ?  9   TYR   A CB   1 
ATOM   118  C  CB   B TYR   A 1 9   ? 11.587 -10.044 13.697  0.28 14.91 ?  9   TYR   A CB   1 
ATOM   119  C  CG   A TYR   A 1 9   ? 12.420 -9.058  13.309  0.72 14.34 ?  9   TYR   A CG   1 
ATOM   120  C  CG   B TYR   A 1 9   ? 12.458 -8.831  13.468  0.28 14.71 ?  9   TYR   A CG   1 
ATOM   121  C  CD1  A TYR   A 1 9   ? 12.771 -8.307  14.419  0.72 14.99 ?  9   TYR   A CD1  1 
ATOM   122  C  CD1  B TYR   A 1 9   ? 12.711 -7.936  14.497  0.28 14.93 ?  9   TYR   A CD1  1 
ATOM   123  C  CD2  A TYR   A 1 9   ? 12.920 -8.680  12.071  0.72 14.58 ?  9   TYR   A CD2  1 
ATOM   124  C  CD2  B TYR   A 1 9   ? 13.010 -8.571  12.220  0.28 14.55 ?  9   TYR   A CD2  1 
ATOM   125  C  CE1  A TYR   A 1 9   ? 13.600 -7.216  14.306  0.72 15.76 ?  9   TYR   A CE1  1 
ATOM   126  C  CE1  B TYR   A 1 9   ? 13.495 -6.819  14.295  0.28 15.08 ?  9   TYR   A CE1  1 
ATOM   127  C  CE2  A TYR   A 1 9   ? 13.748 -7.591  11.946  0.72 15.02 ?  9   TYR   A CE2  1 
ATOM   128  C  CE2  B TYR   A 1 9   ? 13.796 -7.454  12.007  0.28 14.56 ?  9   TYR   A CE2  1 
ATOM   129  C  CZ   A TYR   A 1 9   ? 14.081 -6.859  13.065  0.72 15.92 ?  9   TYR   A CZ   1 
ATOM   130  C  CZ   B TYR   A 1 9   ? 14.034 -6.582  13.048  0.28 14.92 ?  9   TYR   A CZ   1 
ATOM   131  O  OH   A TYR   A 1 9   ? 14.905 -5.772  12.929  0.72 17.09 ?  9   TYR   A OH   1 
ATOM   132  O  OH   B TYR   A 1 9   ? 14.812 -5.466  12.844  0.28 15.25 ?  9   TYR   A OH   1 
ATOM   133  H  H    A TYR   A 1 9   ? 10.290 -9.637  15.547  0.72 17.76 ?  9   TYR   A H    1 
ATOM   134  H  H    B TYR   A 1 9   ? 10.310 -9.454  15.739  0.28 19.33 ?  9   TYR   A H    1 
ATOM   135  H  HA   A TYR   A 1 9   ? 9.802  -9.186  12.949  0.72 16.34 ?  9   TYR   A HA   1 
ATOM   136  H  HA   B TYR   A 1 9   ? 9.900  -9.026  13.132  0.28 18.00 ?  9   TYR   A HA   1 
ATOM   137  H  HB2  A TYR   A 1 9   ? 11.777 -10.762 14.213  0.72 16.68 ?  9   TYR   A HB2  1 
ATOM   138  H  HB2  B TYR   A 1 9   ? 11.872 -10.486 14.514  0.28 17.87 ?  9   TYR   A HB2  1 
ATOM   139  H  HB3  A TYR   A 1 9   ? 11.578 -10.781 12.637  0.72 16.68 ?  9   TYR   A HB3  1 
ATOM   140  H  HB3  B TYR   A 1 9   ? 11.695 -10.640 12.943  0.28 17.87 ?  9   TYR   A HB3  1 
ATOM   141  H  HD1  A TYR   A 1 9   ? 12.434 -8.548  15.255  0.72 17.96 ?  9   TYR   A HD1  1 
ATOM   142  H  HD1  B TYR   A 1 9   ? 12.345 -8.098  15.338  0.28 17.89 ?  9   TYR   A HD1  1 
ATOM   143  H  HD2  A TYR   A 1 9   ? 12.692 -9.172  11.313  0.72 17.48 ?  9   TYR   A HD2  1 
ATOM   144  H  HD2  B TYR   A 1 9   ? 12.848 -9.160  11.516  0.28 17.43 ?  9   TYR   A HD2  1 
ATOM   145  H  HE1  A TYR   A 1 9   ? 13.826 -6.721  15.059  0.72 18.88 ?  9   TYR   A HE1  1 
ATOM   146  H  HE1  B TYR   A 1 9   ? 13.657 -6.233  14.995  0.28 18.07 ?  9   TYR   A HE1  1 
ATOM   147  H  HE2  A TYR   A 1 9   ? 14.083 -7.348  11.112  0.72 18.00 ?  9   TYR   A HE2  1 
ATOM   148  H  HE2  B TYR   A 1 9   ? 14.163 -7.293  11.168  0.28 17.45 ?  9   TYR   A HE2  1 
ATOM   149  H  HH   A TYR   A 1 9   ? 15.045 -5.421  13.679  0.72 20.49 ?  9   TYR   A HH   1 
ATOM   150  H  HH   B TYR   A 1 9   ? 14.879 -5.029  13.558  0.28 18.27 ?  9   TYR   A HH   1 
ATOM   151  N  N    A LEU   A 1 10  ? 8.772  -11.237 12.099  0.72 12.42 ?  10  LEU   A N    1 
ATOM   152  N  N    B LEU   A 1 10  ? 8.654  -10.931 12.298  0.28 13.85 ?  10  LEU   A N    1 
ATOM   153  C  CA   A LEU   A 1 10  ? 8.176  -12.464 11.607  0.72 11.99 ?  10  LEU   A CA   1 
ATOM   154  C  CA   B LEU   A 1 10  ? 7.991  -12.119 11.784  0.28 13.87 ?  10  LEU   A CA   1 
ATOM   155  C  C    A LEU   A 1 10  ? 9.303  -13.394 11.167  0.72 11.58 ?  10  LEU   A C    1 
ATOM   156  C  C    B LEU   A 1 10  ? 9.061  -13.107 11.336  0.28 12.88 ?  10  LEU   A C    1 
ATOM   157  O  O    A LEU   A 1 10  ? 10.269 -12.953 10.539  0.72 11.74 ?  10  LEU   A O    1 
ATOM   158  O  O    B LEU   A 1 10  ? 9.932  -12.766 10.529  0.28 12.86 ?  10  LEU   A O    1 
ATOM   159  C  CB   A LEU   A 1 10  ? 7.286  -12.128 10.416  0.72 12.64 ?  10  LEU   A CB   1 
ATOM   160  C  CB   B LEU   A 1 10  ? 7.102  -11.722 10.603  0.28 15.58 ?  10  LEU   A CB   1 
ATOM   161  C  CG   A LEU   A 1 10  ? 6.563  -13.272 9.724   0.72 14.41 ?  10  LEU   A CG   1 
ATOM   162  C  CG   B LEU   A 1 10  ? 5.850  -12.536 10.249  0.28 17.75 ?  10  LEU   A CG   1 
ATOM   163  C  CD1  A LEU   A 1 10  ? 5.485  -13.863 10.612  0.72 16.20 ?  10  LEU   A CD1  1 
ATOM   164  C  CD1  B LEU   A 1 10  ? 5.983  -13.176 8.869   0.28 18.51 ?  10  LEU   A CD1  1 
ATOM   165  C  CD2  A LEU   A 1 10  ? 5.989  -12.799 8.399   0.72 16.21 ?  10  LEU   A CD2  1 
ATOM   166  C  CD2  B LEU   A 1 10  ? 5.538  -13.582 11.303  0.28 18.19 ?  10  LEU   A CD2  1 
ATOM   167  H  H    A LEU   A 1 10  ? 8.865  -10.641 11.485  0.72 14.88 ?  10  LEU   A H    1 
ATOM   168  H  H    B LEU   A 1 10  ? 8.610  -10.250 11.772  0.28 16.60 ?  10  LEU   A H    1 
ATOM   169  H  HA   A LEU   A 1 10  ? 7.663  -12.904 12.301  0.72 14.36 ?  10  LEU   A HA   1 
ATOM   170  H  HA   B LEU   A 1 10  ? 7.455  -12.516 12.490  0.28 16.62 ?  10  LEU   A HA   1 
ATOM   171  H  HB2  A LEU   A 1 10  ? 6.616  -11.514 10.725  0.72 15.14 ?  10  LEU   A HB2  1 
ATOM   172  H  HB2  B LEU   A 1 10  ? 6.795  -10.814 10.760  0.28 18.67 ?  10  LEU   A HB2  1 
ATOM   173  H  HB3  A LEU   A 1 10  ? 7.840  -11.705 9.746   0.72 15.14 ?  10  LEU   A HB3  1 
ATOM   174  H  HB3  B LEU   A 1 10  ? 7.659  -11.726 9.810   0.28 18.67 ?  10  LEU   A HB3  1 
ATOM   175  H  HG   A LEU   A 1 10  ? 7.199  -13.982 9.535   0.72 17.27 ?  10  LEU   A HG   1 
ATOM   176  H  HG   B LEU   A 1 10  ? 5.094  -11.929 10.209  0.28 21.28 ?  10  LEU   A HG   1 
ATOM   177  H  HD11 A LEU   A 1 10  ? 5.071  -14.616 10.156  0.72 19.41 ?  10  LEU   A HD11 1 
ATOM   178  H  HD11 B LEU   A 1 10  ? 5.160  -13.647 8.658   0.28 22.20 ?  10  LEU   A HD11 1 
ATOM   179  H  HD12 A LEU   A 1 10  ? 5.883  -14.165 11.445  0.72 19.41 ?  10  LEU   A HD12 1 
ATOM   180  H  HD12 B LEU   A 1 10  ? 6.140  -12.480 8.210   0.28 22.20 ?  10  LEU   A HD12 1 
ATOM   181  H  HD13 A LEU   A 1 10  ? 4.815  -13.184 10.796  0.72 19.41 ?  10  LEU   A HD13 1 
ATOM   182  H  HD13 B LEU   A 1 10  ? 6.726  -13.796 8.879   0.28 22.20 ?  10  LEU   A HD13 1 
ATOM   183  H  HD21 A LEU   A 1 10  ? 5.521  -13.541 7.983   0.72 19.43 ?  10  LEU   A HD21 1 
ATOM   184  H  HD21 B LEU   A 1 10  ? 4.752  -14.077 11.031  0.28 21.80 ?  10  LEU   A HD21 1 
ATOM   185  H  HD22 A LEU   A 1 10  ? 5.378  -12.070 8.569   0.72 19.43 ?  10  LEU   A HD22 1 
ATOM   186  H  HD22 B LEU   A 1 10  ? 6.296  -14.179 11.382  0.28 21.80 ?  10  LEU   A HD22 1 
ATOM   187  H  HD23 A LEU   A 1 10  ? 6.718  -12.507 7.835   0.72 19.43 ?  10  LEU   A HD23 1 
ATOM   188  H  HD23 B LEU   A 1 10  ? 5.371  -13.136 12.149  0.28 21.80 ?  10  LEU   A HD23 1 
ATOM   189  N  N    A LYS   A 1 11  ? 9.191  -14.677 11.521  0.72 11.61 ?  11  LYS   A N    1 
ATOM   190  N  N    B LYS   A 1 11  ? 9.021  -14.318 11.881  0.28 12.27 ?  11  LYS   A N    1 
ATOM   191  C  CA   A LYS   A 1 11  ? 10.197 -15.678 11.184  0.72 11.75 ?  11  LYS   A CA   1 
ATOM   192  C  CA   B LYS   A 1 11  ? 9.985  -15.346 11.513  0.28 11.58 ?  11  LYS   A CA   1 
ATOM   193  C  C    A LYS   A 1 11  ? 9.854  -16.272 9.826   0.72 11.87 ?  11  LYS   A C    1 
ATOM   194  C  C    B LYS   A 1 11  ? 9.630  -15.890 10.133  0.28 10.97 ?  11  LYS   A C    1 
ATOM   195  O  O    A LYS   A 1 11  ? 8.790  -16.874 9.665   0.72 13.67 ?  11  LYS   A O    1 
ATOM   196  O  O    B LYS   A 1 11  ? 8.514  -16.377 9.922   0.28 11.02 ?  11  LYS   A O    1 
ATOM   197  C  CB   A LYS   A 1 11  ? 10.235 -16.762 12.263  0.72 11.77 ?  11  LYS   A CB   1 
ATOM   198  C  CB   B LYS   A 1 11  ? 9.969  -16.459 12.558  0.28 11.33 ?  11  LYS   A CB   1 
ATOM   199  C  CG   A LYS   A 1 11  ? 11.263 -17.867 12.060  0.72 12.03 ?  11  LYS   A CG   1 
ATOM   200  C  CG   B LYS   A 1 11  ? 10.987 -17.558 12.324  0.28 11.31 ?  11  LYS   A CG   1 
ATOM   201  C  CD   A LYS   A 1 11  ? 11.389 -18.693 13.350  0.72 12.63 ?  11  LYS   A CD   1 
ATOM   202  C  CD   B LYS   A 1 11  ? 10.936 -18.597 13.431  0.28 11.68 ?  11  LYS   A CD   1 
ATOM   203  C  CE   A LYS   A 1 11  ? 12.373 -19.851 13.241  0.72 13.17 ?  11  LYS   A CE   1 
ATOM   204  C  CE   B LYS   A 1 11  ? 11.987 -19.676 13.227  0.28 11.31 ?  11  LYS   A CE   1 
ATOM   205  N  NZ   A LYS   A 1 11  ? 13.741 -19.392 12.903  0.72 12.96 ?  11  LYS   A NZ   1 
ATOM   206  N  NZ   B LYS   A 1 11  ? 13.380 -19.140 13.292  0.28 11.36 ?  11  LYS   A NZ   1 
ATOM   207  H  H    A LYS   A 1 11  ? 8.529  -15.005 11.960  0.72 13.91 ?  11  LYS   A H    1 
ATOM   208  H  H    B LYS   A 1 11  ? 8.447  -14.564 12.473  0.28 14.70 ?  11  LYS   A H    1 
ATOM   209  H  HA   A LYS   A 1 11  ? 11.074 -15.267 11.127  0.72 14.08 ?  11  LYS   A HA   1 
ATOM   210  H  HA   B LYS   A 1 11  ? 10.874 -14.955 11.477  0.28 13.88 ?  11  LYS   A HA   1 
ATOM   211  H  HB2  A LYS   A 1 11  ? 10.437 -16.338 13.110  0.72 14.10 ?  11  LYS   A HB2  1 
ATOM   212  H  HB2  B LYS   A 1 11  ? 10.151 -16.066 13.428  0.28 13.58 ?  11  LYS   A HB2  1 
ATOM   213  H  HB3  A LYS   A 1 11  ? 9.366  -17.184 12.307  0.72 14.10 ?  11  LYS   A HB3  1 
ATOM   214  H  HB3  B LYS   A 1 11  ? 9.090  -16.863 12.561  0.28 13.58 ?  11  LYS   A HB3  1 
ATOM   215  H  HG2  A LYS   A 1 11  ? 10.975 -18.460 11.347  0.72 14.41 ?  11  LYS   A HG2  1 
ATOM   216  H  HG2  B LYS   A 1 11  ? 10.794 -18.001 11.484  0.28 13.56 ?  11  LYS   A HG2  1 
ATOM   217  H  HG3  A LYS   A 1 11  ? 12.129 -17.484 11.858  0.72 14.41 ?  11  LYS   A HG3  1 
ATOM   218  H  HG3  B LYS   A 1 11  ? 11.877 -17.174 12.309  0.28 13.56 ?  11  LYS   A HG3  1 
ATOM   219  H  HD2  A LYS   A 1 11  ? 11.691 -18.114 14.065  0.72 15.13 ?  11  LYS   A HD2  1 
ATOM   220  H  HD2  B LYS   A 1 11  ? 11.101 -18.168 14.286  0.28 14.00 ?  11  LYS   A HD2  1 
ATOM   221  H  HD3  A LYS   A 1 11  ? 10.520 -19.066 13.571  0.72 15.13 ?  11  LYS   A HD3  1 
ATOM   222  H  HD3  B LYS   A 1 11  ? 10.061 -19.020 13.435  0.28 14.00 ?  11  LYS   A HD3  1 
ATOM   223  H  HE2  A LYS   A 1 11  ? 12.416 -20.318 14.094  0.72 15.78 ?  11  LYS   A HE2  1 
ATOM   224  H  HE2  B LYS   A 1 11  ? 11.892 -20.349 13.918  0.28 13.55 ?  11  LYS   A HE2  1 
ATOM   225  H  HE3  A LYS   A 1 11  ? 12.080 -20.461 12.546  0.72 15.78 ?  11  LYS   A HE3  1 
ATOM   226  H  HE3  B LYS   A 1 11  ? 11.862 -20.078 12.352  0.28 13.55 ?  11  LYS   A HE3  1 
ATOM   227  H  HZ1  A LYS   A 1 11  ? 14.288 -20.091 12.830  0.72 15.53 ?  11  LYS   A HZ1  1 
ATOM   228  H  HZ1  B LYS   A 1 11  ? 13.967 -19.801 13.192  0.28 13.61 ?  11  LYS   A HZ1  1 
ATOM   229  H  HZ2  A LYS   A 1 11  ? 13.729 -18.952 12.131  0.72 15.53 ?  11  LYS   A HZ2  1 
ATOM   230  H  HZ2  B LYS   A 1 11  ? 13.507 -18.541 12.645  0.28 13.61 ?  11  LYS   A HZ2  1 
ATOM   231  H  HZ3  A LYS   A 1 11  ? 14.046 -18.852 13.541  0.72 15.53 ?  11  LYS   A HZ3  1 
ATOM   232  H  HZ3  B LYS   A 1 11  ? 13.519 -18.748 14.079  0.28 13.61 ?  11  LYS   A HZ3  1 
ATOM   233  N  N    A LEU   A 1 12  ? 10.752 -16.120 8.851   0.72 11.19 ?  12  LEU   A N    1 
ATOM   234  N  N    B LEU   A 1 12  ? 10.558 -15.771 9.184   0.28 11.06 ?  12  LEU   A N    1 
ATOM   235  C  CA   A LEU   A 1 12  ? 10.494 -16.702 7.538   0.72 11.21 ?  12  LEU   A CA   1 
ATOM   236  C  CA   B LEU   A 1 12  ? 10.342 -16.283 7.834   0.28 11.24 ?  12  LEU   A CA   1 
ATOM   237  C  C    A LEU   A 1 12  ? 11.079 -18.102 7.394   0.72 11.30 ?  12  LEU   A C    1 
ATOM   238  C  C    B LEU   A 1 12  ? 10.899 -17.691 7.654   0.28 11.15 ?  12  LEU   A C    1 
ATOM   239  O  O    A LEU   A 1 12  ? 10.455 -18.973 6.781   0.72 11.60 ?  12  LEU   A O    1 
ATOM   240  O  O    B LEU   A 1 12  ? 10.223 -18.566 7.105   0.28 11.30 ?  12  LEU   A O    1 
ATOM   241  C  CB   A LEU   A 1 12  ? 11.048 -15.806 6.425   0.72 11.39 ?  12  LEU   A CB   1 
ATOM   242  C  CB   B LEU   A 1 12  ? 10.960 -15.333 6.800   0.28 11.98 ?  12  LEU   A CB   1 
ATOM   243  C  CG   A LEU   A 1 12  ? 10.386 -14.439 6.235   0.72 12.23 ?  12  LEU   A CG   1 
ATOM   244  C  CG   B LEU   A 1 12  ? 10.300 -13.960 6.688   0.28 12.61 ?  12  LEU   A CG   1 
ATOM   245  C  CD1  A LEU   A 1 12  ? 11.121 -13.663 5.166   0.72 12.62 ?  12  LEU   A CD1  1 
ATOM   246  C  CD1  B LEU   A 1 12  ? 10.849 -13.193 5.493   0.28 13.01 ?  12  LEU   A CD1  1 
ATOM   247  C  CD2  A LEU   A 1 12  ? 8.904  -14.578 5.876   0.72 13.05 ?  12  LEU   A CD2  1 
ATOM   248  C  CD2  B LEU   A 1 12  ? 8.792  -14.115 6.587   0.28 12.91 ?  12  LEU   A CD2  1 
ATOM   249  H  H    A LEU   A 1 12  ? 11.508 -15.697 8.920   0.72 13.40 ?  12  LEU   A H    1 
ATOM   250  H  H    B LEU   A 1 12  ? 11.311 -15.370 9.294   0.28 13.25 ?  12  LEU   A H    1 
ATOM   251  H  HA   A LEU   A 1 12  ? 9.539  -16.772 7.415   0.72 13.43 ?  12  LEU   A HA   1 
ATOM   252  H  HA   B LEU   A 1 12  ? 9.390  -16.325 7.666   0.28 13.47 ?  12  LEU   A HA   1 
ATOM   253  H  HB2  A LEU   A 1 12  ? 11.986 -15.646 6.602   0.72 13.64 ?  12  LEU   A HB2  1 
ATOM   254  H  HB2  B LEU   A 1 12  ? 11.892 -15.186 7.028   0.28 14.36 ?  12  LEU   A HB2  1 
ATOM   255  H  HB3  A LEU   A 1 12  ? 10.959 -16.286 5.584   0.72 13.64 ?  12  LEU   A HB3  1 
ATOM   256  H  HB3  B LEU   A 1 12  ? 10.904 -15.749 5.925   0.28 14.36 ?  12  LEU   A HB3  1 
ATOM   257  H  HG   A LEU   A 1 12  ? 10.445 -13.945 7.065   0.72 14.65 ?  12  LEU   A HG   1 
ATOM   258  H  HG   B LEU   A 1 12  ? 10.498 -13.447 7.489   0.28 15.11 ?  12  LEU   A HG   1 
ATOM   259  H  HD11 A LEU   A 1 12  ? 10.695 -12.802 5.052   0.72 15.12 ?  12  LEU   A HD11 1 
ATOM   260  H  HD11 B LEU   A 1 12  ? 10.418 -12.323 5.451   0.28 15.59 ?  12  LEU   A HD11 1 
ATOM   261  H  HD12 A LEU   A 1 12  ? 12.043 -13.544 5.444   0.72 15.12 ?  12  LEU   A HD12 1 
ATOM   262  H  HD12 B LEU   A 1 12  ? 11.806 -13.083 5.600   0.28 15.59 ?  12  LEU   A HD12 1 
ATOM   263  H  HD13 A LEU   A 1 12  ? 11.089 -14.163 4.334   0.72 15.12 ?  12  LEU   A HD13 1 
ATOM   264  H  HD13 B LEU   A 1 12  ? 10.660 -13.694 4.684   0.28 15.59 ?  12  LEU   A HD13 1 
ATOM   265  H  HD21 A LEU   A 1 12  ? 8.542  -13.703 5.672   0.72 15.64 ?  12  LEU   A HD21 1 
ATOM   266  H  HD21 B LEU   A 1 12  ? 8.412  -13.294 6.245   0.28 15.47 ?  12  LEU   A HD21 1 
ATOM   267  H  HD22 A LEU   A 1 12  ? 8.816  -15.159 5.101   0.72 15.64 ?  12  LEU   A HD22 1 
ATOM   268  H  HD22 B LEU   A 1 12  ? 8.593  -14.852 5.988   0.28 15.47 ?  12  LEU   A HD22 1 
ATOM   269  H  HD23 A LEU   A 1 12  ? 8.425  -14.965 6.628   0.72 15.64 ?  12  LEU   A HD23 1 
ATOM   270  H  HD23 B LEU   A 1 12  ? 8.437  -14.304 7.471   0.28 15.47 ?  12  LEU   A HD23 1 
ATOM   271  N  N    A THR   A 1 13  ? 12.287 -18.313 7.911   0.72 11.65 ?  13  THR   A N    1 
ATOM   272  N  N    B THR   A 1 13  ? 12.135 -17.914 8.090   0.28 11.23 ?  13  THR   A N    1 
ATOM   273  C  CA   A THR   A 1 13  ? 12.986 -19.592 7.831   0.72 12.19 ?  13  THR   A CA   1 
ATOM   274  C  CA   B THR   A 1 13  ? 12.774 -19.216 7.982   0.28 11.46 ?  13  THR   A CA   1 
ATOM   275  C  C    A THR   A 1 13  ? 13.755 -19.798 9.131   0.72 12.24 ?  13  THR   A C    1 
ATOM   276  C  C    B THR   A 1 13  ? 13.527 -19.492 9.279   0.28 11.86 ?  13  THR   A C    1 
ATOM   277  O  O    A THR   A 1 13  ? 13.657 -19.007 10.074  0.72 12.48 ?  13  THR   A O    1 
ATOM   278  O  O    B THR   A 1 13  ? 13.407 -18.760 10.267  0.28 12.13 ?  13  THR   A O    1 
ATOM   279  C  CB   A THR   A 1 13  ? 13.967 -19.643 6.649   0.72 13.26 ?  13  THR   A CB   1 
ATOM   280  C  CB   B THR   A 1 13  ? 13.739 -19.270 6.789   0.28 11.24 ?  13  THR   A CB   1 
ATOM   281  O  OG1  A THR   A 1 13  ? 15.036 -18.723 6.881   0.72 13.95 ?  13  THR   A OG1  1 
ATOM   282  O  OG1  B THR   A 1 13  ? 14.826 -18.370 7.023   0.28 11.03 ?  13  THR   A OG1  1 
ATOM   283  C  CG2  A THR   A 1 13  ? 13.289 -19.314 5.331   0.72 14.34 ?  13  THR   A CG2  1 
ATOM   284  C  CG2  B THR   A 1 13  ? 13.044 -18.910 5.475   0.28 11.37 ?  13  THR   A CG2  1 
ATOM   285  H  H    A THR   A 1 13  ? 12.745 -17.707 8.312   0.72 13.96 ?  13  THR   A H    1 
ATOM   286  H  H    B THR   A 1 13  ? 12.628 -17.309 8.449   0.28 13.46 ?  13  THR   A H    1 
ATOM   287  H  HA   A THR   A 1 13  ? 12.344 -20.313 7.723   0.72 14.60 ?  13  THR   A HA   1 
ATOM   288  H  HA   B THR   A 1 13  ? 12.093 -19.894 7.859   0.28 13.73 ?  13  THR   A HA   1 
ATOM   289  H  HB   A THR   A 1 13  ? 14.339 -20.538 6.575   0.72 15.89 ?  13  THR   A HB   1 
ATOM   290  H  HB   B THR   A 1 13  ? 14.085 -20.169 6.705   0.28 13.47 ?  13  THR   A HB   1 
ATOM   291  H  HG1  A THR   A 1 13  ? 15.575 -18.738 6.230   0.72 16.72 ?  13  THR   A HG1  1 
ATOM   292  H  HG1  B THR   A 1 13  ? 15.359 -18.390 6.373   0.28 13.21 ?  13  THR   A HG1  1 
ATOM   293  H  HG21 A THR   A 1 13  ? 13.903 -19.478 4.594   0.72 17.18 ?  13  THR   A HG21 1 
ATOM   294  H  HG21 B THR   A 1 13  ? 13.668 -19.005 4.734   0.28 13.62 ?  13  THR   A HG21 1 
ATOM   295  H  HG22 A THR   A 1 13  ? 12.507 -19.873 5.215   0.72 17.18 ?  13  THR   A HG22 1 
ATOM   296  H  HG22 B THR   A 1 13  ? 12.290 -19.503 5.324   0.28 13.62 ?  13  THR   A HG22 1 
ATOM   297  H  HG23 A THR   A 1 13  ? 13.023 -18.384 5.319   0.72 17.18 ?  13  THR   A HG23 1 
ATOM   298  H  HG23 B THR   A 1 13  ? 12.727 -17.996 5.502   0.28 13.62 ?  13  THR   A HG23 1 
ATOM   299  N  N    A ASP   A 1 14  ? 14.567 -20.855 9.164   0.72 13.28 ?  14  ASP   A N    1 
ATOM   300  N  N    B ASP   A 1 14  ? 14.318 -20.562 9.257   0.28 12.41 ?  14  ASP   A N    1 
ATOM   301  C  CA   A ASP   A 1 14  ? 15.405 -21.102 10.329  0.72 14.47 ?  14  ASP   A CA   1 
ATOM   302  C  CA   B ASP   A 1 14  ? 15.184 -20.901 10.378  0.28 13.28 ?  14  ASP   A CA   1 
ATOM   303  C  C    A ASP   A 1 14  ? 16.186 -19.859 10.738  0.72 13.99 ?  14  ASP   A C    1 
ATOM   304  C  C    B ASP   A 1 14  ? 16.158 -19.784 10.719  0.28 12.31 ?  14  ASP   A C    1 
ATOM   305  O  O    A ASP   A 1 14  ? 16.300 -19.555 11.932  0.72 14.83 ?  14  ASP   A O    1 
ATOM   306  O  O    B ASP   A 1 14  ? 16.638 -19.724 11.857  0.28 12.23 ?  14  ASP   A O    1 
ATOM   307  C  CB   A ASP   A 1 14  ? 16.365 -22.255 10.042  0.72 16.96 ?  14  ASP   A CB   1 
ATOM   308  C  CB   B ASP   A 1 14  ? 15.988 -22.150 10.021  0.28 15.03 ?  14  ASP   A CB   1 
ATOM   309  C  CG   A ASP   A 1 14  ? 17.267 -22.551 11.214  0.72 21.02 ?  14  ASP   A CG   1 
ATOM   310  C  CG   B ASP   A 1 14  ? 17.004 -22.530 11.094  0.28 16.73 ?  14  ASP   A CG   1 
ATOM   311  O  OD1  A ASP   A 1 14  ? 16.766 -23.095 12.223  0.72 22.57 ?  14  ASP   A OD1  1 
ATOM   312  O  OD1  B ASP   A 1 14  ? 16.610 -22.671 12.271  0.28 17.23 ?  14  ASP   A OD1  1 
ATOM   313  O  OD2  A ASP   A 1 14  ? 18.465 -22.216 11.128  0.72 23.29 -1 14  ASP   A OD2  1 
ATOM   314  O  OD2  B ASP   A 1 14  ? 18.195 -22.707 10.757  0.28 17.69 -1 14  ASP   A OD2  1 
ATOM   315  H  H    A ASP   A 1 14  ? 14.660 -21.432 8.526   0.72 15.92 ?  14  ASP   A H    1 
ATOM   316  H  H    B ASP   A 1 14  ? 14.356 -21.103 8.596   0.28 14.87 ?  14  ASP   A H    1 
ATOM   317  H  HA   A ASP   A 1 14  ? 14.844 -21.364 11.074  0.72 17.34 ?  14  ASP   A HA   1 
ATOM   318  H  HA   B ASP   A 1 14  ? 14.629 -21.092 11.153  0.28 15.91 ?  14  ASP   A HA   1 
ATOM   319  H  HB2  A ASP   A 1 14  ? 15.845 -23.063 9.844   0.72 20.33 ?  14  ASP   A HB2  1 
ATOM   320  H  HB2  B ASP   A 1 14  ? 15.371 -22.884 9.894   0.28 18.02 ?  14  ASP   A HB2  1 
ATOM   321  H  HB3  A ASP   A 1 14  ? 16.922 -22.037 9.282   0.72 20.33 ?  14  ASP   A HB3  1 
ATOM   322  H  HB3  B ASP   A 1 14  ? 16.472 -21.973 9.199   0.28 18.02 ?  14  ASP   A HB3  1 
ATOM   323  N  N    A ASN   A 1 15  ? 16.718 -19.115 9.762   0.72 13.10 ?  15  ASN   A N    1 
ATOM   324  N  N    B ASN   A 1 15  ? 16.468 -18.899 9.762   0.28 11.78 ?  15  ASN   A N    1 
ATOM   325  C  CA   A ASN   A 1 15  ? 17.683 -18.059 10.043  0.72 13.38 ?  15  ASN   A CA   1 
ATOM   326  C  CA   B ASN   A 1 15  ? 17.516 -17.911 9.986   0.28 11.98 ?  15  ASN   A CA   1 
ATOM   327  C  C    A ASN   A 1 15  ? 17.279 -16.663 9.571   0.72 13.20 ?  15  ASN   A C    1 
ATOM   328  C  C    B ASN   A 1 15  ? 17.228 -16.552 9.348   0.28 12.07 ?  15  ASN   A C    1 
ATOM   329  O  O    A ASN   A 1 15  ? 17.989 -15.704 9.904   0.72 12.76 ?  15  ASN   A O    1 
ATOM   330  O  O    B ASN   A 1 15  ? 18.155 -15.746 9.203   0.28 12.27 ?  15  ASN   A O    1 
ATOM   331  C  CB   A ASN   A 1 15  ? 19.055 -18.403 9.433   0.72 13.42 ?  15  ASN   A CB   1 
ATOM   332  C  CB   B ASN   A 1 15  ? 18.864 -18.442 9.478   0.28 11.81 ?  15  ASN   A CB   1 
ATOM   333  C  CG   A ASN   A 1 15  ? 19.000 -18.541 7.925   0.72 14.16 ?  15  ASN   A CG   1 
ATOM   334  C  CG   B ASN   A 1 15  ? 18.953 -18.464 7.965   0.28 12.09 ?  15  ASN   A CG   1 
ATOM   335  O  OD1  A ASN   A 1 15  ? 18.199 -19.311 7.390   0.72 15.18 ?  15  ASN   A OD1  1 
ATOM   336  O  OD1  B ASN   A 1 15  ? 18.412 -19.359 7.309   0.28 12.66 ?  15  ASN   A OD1  1 
ATOM   337  N  ND2  A ASN   A 1 15  ? 19.836 -17.772 7.227   0.72 13.67 ?  15  ASN   A ND2  1 
ATOM   338  N  ND2  B ASN   A 1 15  ? 19.650 -17.480 7.401   0.28 11.64 ?  15  ASN   A ND2  1 
ATOM   339  H  H    A ASN   A 1 15  ? 16.546 -19.216 8.928   0.72 15.70 ?  15  ASN   A H    1 
ATOM   340  H  H    B ASN   A 1 15  ? 16.094 -18.861 8.990   0.28 14.11 ?  15  ASN   A H    1 
ATOM   341  H  HA   A ASN   A 1 15  ? 17.818 -18.015 11.002  0.72 16.03 ?  15  ASN   A HA   1 
ATOM   342  H  HA   B ASN   A 1 15  ? 17.601 -17.763 10.940  0.28 14.36 ?  15  ASN   A HA   1 
ATOM   343  H  HB2  A ASN   A 1 15  ? 19.692 -17.693 9.650   0.72 16.08 ?  15  ASN   A HB2  1 
ATOM   344  H  HB2  B ASN   A 1 15  ? 19.571 -17.871 9.810   0.28 14.15 ?  15  ASN   A HB2  1 
ATOM   345  H  HB3  A ASN   A 1 15  ? 19.376 -19.244 9.804   0.72 16.08 ?  15  ASN   A HB3  1 
ATOM   346  H  HB3  B ASN   A 1 15  ? 18.985 -19.348 9.797   0.28 14.15 ?  15  ASN   A HB3  1 
ATOM   347  H  HD21 A ASN   A 1 15  ? 19.844 -17.820 6.369   0.72 16.39 ?  15  ASN   A HD21 1 
ATOM   348  H  HD21 B ASN   A 1 15  ? 19.733 -17.442 6.547   0.28 13.95 ?  15  ASN   A HD21 1 
ATOM   349  H  HD22 A ASN   A 1 15  ? 20.383 -17.241 7.631   0.72 16.39 ?  15  ASN   A HD22 1 
ATOM   350  H  HD22 B ASN   A 1 15  ? 20.014 -16.873 7.894   0.28 13.95 ?  15  ASN   A HD22 1 
ATOM   351  N  N    A VAL   A 1 16  ? 16.194 -16.515 8.802   0.72 13.01 ?  16  VAL   A N    1 
ATOM   352  N  N    B VAL   A 1 16  ? 15.980 -16.259 8.982   0.28 11.68 ?  16  VAL   A N    1 
ATOM   353  C  CA   A VAL   A 1 16  ? 15.790 -15.233 8.226   0.72 12.66 ?  16  VAL   A CA   1 
ATOM   354  C  CA   B VAL   A 1 16  ? 15.613 -14.991 8.361   0.28 11.62 ?  16  VAL   A CA   1 
ATOM   355  C  C    A VAL   A 1 16  ? 14.504 -14.745 8.883   0.72 12.13 ?  16  VAL   A C    1 
ATOM   356  C  C    B VAL   A 1 16  ? 14.353 -14.467 9.044   0.28 11.45 ?  16  VAL   A C    1 
ATOM   357  O  O    A VAL   A 1 16  ? 13.510 -15.480 8.972   0.72 12.19 ?  16  VAL   A O    1 
ATOM   358  O  O    B VAL   A 1 16  ? 13.343 -15.176 9.127   0.28 11.31 ?  16  VAL   A O    1 
ATOM   359  C  CB   A VAL   A 1 16  ? 15.627 -15.306 6.698   0.72 13.48 ?  16  VAL   A CB   1 
ATOM   360  C  CB   B VAL   A 1 16  ? 15.402 -15.142 6.840   0.28 12.14 ?  16  VAL   A CB   1 
ATOM   361  C  CG1  A VAL   A 1 16  ? 15.214 -13.941 6.145   0.72 14.40 ?  16  VAL   A CG1  1 
ATOM   362  C  CG1  B VAL   A 1 16  ? 14.954 -13.823 6.215   0.28 12.57 ?  16  VAL   A CG1  1 
ATOM   363  C  CG2  A VAL   A 1 16  ? 16.908 -15.780 6.031   0.72 14.57 ?  16  VAL   A CG2  1 
ATOM   364  C  CG2  B VAL   A 1 16  ? 16.673 -15.653 6.161   0.28 12.63 ?  16  VAL   A CG2  1 
ATOM   365  H  H    A VAL   A 1 16  ? 15.681 -17.170 8.591   0.72 15.59 ?  16  VAL   A H    1 
ATOM   366  H  H    B VAL   A 1 16  ? 15.312 -16.784 9.093   0.28 14.00 ?  16  VAL   A H    1 
ATOM   367  H  HA   A VAL   A 1 16  ? 16.489 -14.585 8.413   0.72 15.17 ?  16  VAL   A HA   1 
ATOM   368  H  HA   B VAL   A 1 16  ? 16.322 -14.340 8.502   0.28 13.92 ?  16  VAL   A HA   1 
ATOM   369  H  HB   A VAL   A 1 16  ? 14.927 -15.941 6.489   0.72 16.15 ?  16  VAL   A HB   1 
ATOM   370  H  HB   B VAL   A 1 16  ? 14.706 -15.796 6.684   0.28 14.55 ?  16  VAL   A HB   1 
ATOM   371  H  HG11 A VAL   A 1 16  ? 15.305 -13.955 5.181   0.72 17.26 ?  16  VAL   A HG11 1 
ATOM   372  H  HG11 B VAL   A 1 16  ? 15.025 -13.895 5.249   0.28 15.07 ?  16  VAL   A HG11 1 
ATOM   373  H  HG12 A VAL   A 1 16  ? 14.288 -13.770 6.386   0.72 17.26 ?  16  VAL   A HG12 1 
ATOM   374  H  HG12 B VAL   A 1 16  ? 14.034 -13.653 6.466   0.28 15.07 ?  16  VAL   A HG12 1 
ATOM   375  H  HG13 A VAL   A 1 16  ? 15.787 -13.260 6.524   0.72 17.26 ?  16  VAL   A HG13 1 
ATOM   376  H  HG13 B VAL   A 1 16  ? 15.528 -13.112 6.536   0.28 15.07 ?  16  VAL   A HG13 1 
ATOM   377  H  HG21 A VAL   A 1 16  ? 16.792 -15.741 5.069   0.72 17.46 ?  16  VAL   A HG21 1 
ATOM   378  H  HG21 B VAL   A 1 16  ? 16.519 -15.716 5.204   0.28 15.14 ?  16  VAL   A HG21 1 
ATOM   379  H  HG22 A VAL   A 1 16  ? 17.638 -15.207 6.302   0.72 17.46 ?  16  VAL   A HG22 1 
ATOM   380  H  HG22 B VAL   A 1 16  ? 17.400 -15.037 6.337   0.28 15.14 ?  16  VAL   A HG22 1 
ATOM   381  H  HG23 A VAL   A 1 16  ? 17.084 -16.695 6.305   0.72 17.46 ?  16  VAL   A HG23 1 
ATOM   382  H  HG23 B VAL   A 1 16  ? 16.892 -16.531 6.516   0.28 15.14 ?  16  VAL   A HG23 1 
ATOM   383  N  N    A TYR   A 1 17  ? 14.523 -13.475 9.284   0.72 12.04 ?  17  TYR   A N    1 
ATOM   384  N  N    B TYR   A 1 17  ? 14.424 -13.227 9.532   0.28 11.46 ?  17  TYR   A N    1 
ATOM   385  C  CA   A TYR   A 1 17  ? 13.439 -12.792 9.969   0.72 11.70 ?  17  TYR   A CA   1 
ATOM   386  C  CA   B TYR   A 1 17  ? 13.349 -12.564 10.256  0.28 11.36 ?  17  TYR   A CA   1 
ATOM   387  C  C    A TYR   A 1 17  ? 13.167 -11.479 9.247   0.72 11.74 ?  17  TYR   A C    1 
ATOM   388  C  C    B TYR   A 1 17  ? 13.106 -11.206 9.613   0.28 11.06 ?  17  TYR   A C    1 
ATOM   389  O  O    A TYR   A 1 17  ? 14.066 -10.924 8.615   0.72 11.28 ?  17  TYR   A O    1 
ATOM   390  O  O    B TYR   A 1 17  ? 14.036 -10.589 9.093   0.28 10.93 ?  17  TYR   A O    1 
ATOM   391  C  CB   A TYR   A 1 17  ? 13.853 -12.506 11.413  0.72 12.40 ?  17  TYR   A CB   1 
ATOM   392  C  CB   B TYR   A 1 17  ? 13.747 -12.362 11.723  0.28 12.12 ?  17  TYR   A CB   1 
ATOM   393  C  CG   A TYR   A 1 17  ? 14.030 -13.755 12.244  0.72 13.75 ?  17  TYR   A CG   1 
ATOM   394  C  CG   B TYR   A 1 17  ? 14.028 -13.649 12.466  0.28 13.09 ?  17  TYR   A CG   1 
ATOM   395  C  CD1  A TYR   A 1 17  ? 15.203 -14.509 12.192  0.72 14.77 ?  17  TYR   A CD1  1 
ATOM   396  C  CD1  B TYR   A 1 17  ? 15.224 -14.337 12.289  0.28 13.87 ?  17  TYR   A CD1  1 
ATOM   397  C  CD2  A TYR   A 1 17  ? 13.011 -14.197 13.071  0.72 14.24 ?  17  TYR   A CD2  1 
ATOM   398  C  CD2  B TYR   A 1 17  ? 13.096 -14.177 13.346  0.28 13.68 ?  17  TYR   A CD2  1 
ATOM   399  C  CE1  A TYR   A 1 17  ? 15.348 -15.671 12.952  0.72 15.34 ?  17  TYR   A CE1  1 
ATOM   400  C  CE1  B TYR   A 1 17  ? 15.478 -15.518 12.965  0.28 14.44 ?  17  TYR   A CE1  1 
ATOM   401  C  CE2  A TYR   A 1 17  ? 13.146 -15.354 13.832  0.72 15.07 ?  17  TYR   A CE2  1 
ATOM   402  C  CE2  B TYR   A 1 17  ? 13.342 -15.358 14.028  0.28 14.17 ?  17  TYR   A CE2  1 
ATOM   403  C  CZ   A TYR   A 1 17  ? 14.315 -16.086 13.772  0.72 15.42 ?  17  TYR   A CZ   1 
ATOM   404  C  CZ   B TYR   A 1 17  ? 14.536 -16.023 13.835  0.28 14.59 ?  17  TYR   A CZ   1 
ATOM   405  O  OH   A TYR   A 1 17  ? 14.444 -17.232 14.531  0.72 16.07 ?  17  TYR   A OH   1 
ATOM   406  O  OH   B TYR   A 1 17  ? 14.787 -17.195 14.513  0.28 15.23 ?  17  TYR   A OH   1 
ATOM   407  H  H    A TYR   A 1 17  ? 15.206 -12.965 9.151   0.72 14.42 ?  17  TYR   A H    1 
ATOM   408  H  H    B TYR   A 1 17  ? 15.117 -12.725 9.448   0.28 13.73 ?  17  TYR   A H    1 
ATOM   409  H  HA   A TYR   A 1 17  ? 12.644 -13.348 9.957   0.72 14.01 ?  17  TYR   A HA   1 
ATOM   410  H  HA   B TYR   A 1 17  ? 12.530 -13.079 10.213  0.28 13.61 ?  17  TYR   A HA   1 
ATOM   411  H  HB2  A TYR   A 1 17  ? 14.691 -12.029 11.408  0.72 14.86 ?  17  TYR   A HB2  1 
ATOM   412  H  HB2  B TYR   A 1 17  ? 14.546 -11.815 11.756  0.28 14.52 ?  17  TYR   A HB2  1 
ATOM   413  H  HB3  A TYR   A 1 17  ? 13.162 -11.972 11.826  0.72 14.86 ?  17  TYR   A HB3  1 
ATOM   414  H  HB3  B TYR   A 1 17  ? 13.025 -11.914 12.184  0.28 14.52 ?  17  TYR   A HB3  1 
ATOM   415  H  HD1  A TYR   A 1 17  ? 15.902 -14.236 11.637  0.72 17.71 ?  17  TYR   A HD1  1 
ATOM   416  H  HD1  B TYR   A 1 17  ? 15.862 -14.001 11.702  0.28 16.62 ?  17  TYR   A HD1  1 
ATOM   417  H  HD2  A TYR   A 1 17  ? 12.217 -13.718 13.117  0.72 17.07 ?  17  TYR   A HD2  1 
ATOM   418  H  HD2  B TYR   A 1 17  ? 12.289 -13.731 13.478  0.28 16.39 ?  17  TYR   A HD2  1 
ATOM   419  H  HE1  A TYR   A 1 17  ? 16.141 -16.162 12.913  0.72 18.38 ?  17  TYR   A HE1  1 
ATOM   420  H  HE1  B TYR   A 1 17  ? 16.282 -15.968 12.835  0.28 17.31 ?  17  TYR   A HE1  1 
ATOM   421  H  HE2  A TYR   A 1 17  ? 12.452 -15.630 14.386  0.72 18.06 ?  17  TYR   A HE2  1 
ATOM   422  H  HE2  B TYR   A 1 17  ? 12.705 -15.697 14.614  0.28 16.99 ?  17  TYR   A HE2  1 
ATOM   423  H  HH   A TYR   A 1 17  ? 13.699 -17.451 14.843  0.72 19.26 ?  17  TYR   A HH   1 
ATOM   424  H  HH   B TYR   A 1 17  ? 15.535 -17.504 14.291  0.28 18.25 ?  17  TYR   A HH   1 
ATOM   425  N  N    A ILE   A 1 18  ? 11.938 -10.962 9.344   0.72 11.95 ?  18  ILE   A N    1 
ATOM   426  N  N    B ILE   A 1 18  ? 11.860 -10.730 9.649   0.28 10.65 ?  18  ILE   A N    1 
ATOM   427  C  CA   A ILE   A 1 18  ? 11.558 -9.770  8.583   0.72 11.83 ?  18  ILE   A CA   1 
ATOM   428  C  CA   B ILE   A 1 18  ? 11.487 -9.516  8.925   0.28 10.26 ?  18  ILE   A CA   1 
ATOM   429  C  C    A ILE   A 1 18  ? 10.583 -8.905  9.378   0.72 12.33 ?  18  ILE   A C    1 
ATOM   430  C  C    B ILE   A 1 18  ? 10.580 -8.642  9.782   0.28 10.04 ?  18  ILE   A C    1 
ATOM   431  O  O    A ILE   A 1 18  ? 9.762  -9.413  10.148  0.72 12.90 ?  18  ILE   A O    1 
ATOM   432  O  O    B ILE   A 1 18  ? 9.720  -9.144  10.514  0.28 10.15 ?  18  ILE   A O    1 
ATOM   433  C  CB   A ILE   A 1 18  ? 11.010 -10.176 7.196   0.72 11.38 ?  18  ILE   A CB   1 
ATOM   434  C  CB   B ILE   A 1 18  ? 10.845 -9.844  7.561   0.28 10.19 ?  18  ILE   A CB   1 
ATOM   435  C  CG1  A ILE   A 1 18  ? 10.966 -8.979  6.251   0.72 11.47 ?  18  ILE   A CG1  1 
ATOM   436  C  CG1  B ILE   A 1 18  ? 10.748 -8.585  6.695   0.28 11.12 ?  18  ILE   A CG1  1 
ATOM   437  C  CG2  A ILE   A 1 18  ? 9.653  -10.876 7.326   0.72 11.45 ?  18  ILE   A CG2  1 
ATOM   438  C  CG2  B ILE   A 1 18  ? 9.471  -10.483 7.744   0.28 10.47 ?  18  ILE   A CG2  1 
ATOM   439  C  CD1  A ILE   A 1 18  ? 10.749 -9.378  4.825   0.72 12.70 ?  18  ILE   A CD1  1 
ATOM   440  C  CD1  B ILE   A 1 18  ? 10.337 -8.863  5.264   0.28 12.11 ?  18  ILE   A CD1  1 
ATOM   441  H  H    A ILE   A 1 18  ? 11.315 -11.299 9.830   0.72 14.32 ?  18  ILE   A H    1 
ATOM   442  H  H    B ILE   A 1 18  ? 11.210 -11.091 10.084  0.28 12.76 ?  18  ILE   A H    1 
ATOM   443  H  HA   A ILE   A 1 18  ? 12.362 -9.250  8.430   0.72 14.17 ?  18  ILE   A HA   1 
ATOM   444  H  HA   B ILE   A 1 18  ? 12.289 -9.001  8.752   0.28 12.29 ?  18  ILE   A HA   1 
ATOM   445  H  HB   A ILE   A 1 18  ? 11.626 -10.822 6.813   0.72 13.63 ?  18  ILE   A HB   1 
ATOM   446  H  HB   B ILE   A 1 18  ? 11.420 -10.475 7.110   0.28 12.20 ?  18  ILE   A HB   1 
ATOM   447  H  HG12 A ILE   A 1 18  ? 10.246 -8.391  6.511   0.72 13.75 ?  18  ILE   A HG12 1 
ATOM   448  H  HG12 B ILE   A 1 18  ? 10.089 -7.984  7.080   0.28 13.33 ?  18  ILE   A HG12 1 
ATOM   449  H  HG13 A ILE   A 1 18  ? 11.816 -8.509  6.297   0.72 13.75 ?  18  ILE   A HG13 1 
ATOM   450  H  HG13 B ILE   A 1 18  ? 11.615 -8.147  6.674   0.28 13.33 ?  18  ILE   A HG13 1 
ATOM   451  H  HG21 A ILE   A 1 18  ? 9.415  -11.265 6.466   0.72 13.72 ?  18  ILE   A HG21 1 
ATOM   452  H  HG21 B ILE   A 1 18  ? 9.180  -10.849 6.892   0.28 12.54 ?  18  ILE   A HG21 1 
ATOM   453  H  HG22 A ILE   A 1 18  ? 9.721  -11.576 7.993   0.72 13.72 ?  18  ILE   A HG22 1 
ATOM   454  H  HG22 B ILE   A 1 18  ? 9.536  -11.190 8.402   0.28 12.54 ?  18  ILE   A HG22 1 
ATOM   455  H  HG23 A ILE   A 1 18  ? 8.985  -10.228 7.590   0.72 13.72 ?  18  ILE   A HG23 1 
ATOM   456  H  HG23 B ILE   A 1 18  ? 8.840  -9.808  8.043   0.28 12.54 ?  18  ILE   A HG23 1 
ATOM   457  H  HD11 A ILE   A 1 18  ? 10.789 -8.582  4.264   0.72 15.21 ?  18  ILE   A HD11 1 
ATOM   458  H  HD11 B ILE   A 1 18  ? 10.346 -8.031  4.764   0.28 14.51 ?  18  ILE   A HD11 1 
ATOM   459  H  HD12 A ILE   A 1 18  ? 11.438 -10.003 4.556   0.72 15.21 ?  18  ILE   A HD12 1 
ATOM   460  H  HD12 B ILE   A 1 18  ? 10.964 -9.490  4.872   0.28 14.51 ?  18  ILE   A HD12 1 
ATOM   461  H  HD13 A ILE   A 1 18  ? 9.874  -9.790  4.741   0.72 15.21 ?  18  ILE   A HD13 1 
ATOM   462  H  HD13 B ILE   A 1 18  ? 9.444  -9.240  5.258   0.28 14.51 ?  18  ILE   A HD13 1 
ATOM   463  N  N    A LYS   A 1 19  ? 10.660 -7.586  9.165   0.72 11.88 ?  19  LYS   A N    1 
ATOM   464  N  N    B LYS   A 1 19  ? 10.773 -7.324  9.676   0.28 10.18 ?  19  LYS   A N    1 
ATOM   465  C  CA   A LYS   A 1 19  ? 9.831  -6.630  9.893   0.72 12.71 ?  19  LYS   A CA   1 
ATOM   466  C  CA   B LYS   A 1 19  ? 9.998  -6.351  10.430  0.28 11.42 ?  19  LYS   A CA   1 
ATOM   467  C  C    A LYS   A 1 19  ? 9.666  -5.357  9.067   0.72 12.46 ?  19  LYS   A C    1 
ATOM   468  C  C    B LYS   A 1 19  ? 9.764  -5.135  9.551   0.28 12.14 ?  19  LYS   A C    1 
ATOM   469  O  O    A LYS   A 1 19  ? 10.565 -4.981  8.313   0.72 12.25 ?  19  LYS   A O    1 
ATOM   470  O  O    B LYS   A 1 19  ? 10.658 -4.720  8.810   0.28 12.00 ?  19  LYS   A O    1 
ATOM   471  C  CB   A LYS   A 1 19  ? 10.507 -6.295  11.229  0.72 14.15 ?  19  LYS   A CB   1 
ATOM   472  C  CB   B LYS   A 1 19  ? 10.752 -5.920  11.696  0.28 12.27 ?  19  LYS   A CB   1 
ATOM   473  C  CG   A LYS   A 1 19  ? 9.776  -5.306  12.117  0.72 15.46 ?  19  LYS   A CG   1 
ATOM   474  C  CG   B LYS   A 1 19  ? 9.954  -5.081  12.675  0.28 13.65 ?  19  LYS   A CG   1 
ATOM   475  C  CD   A LYS   A 1 19  ? 10.617 -5.035  13.354  0.72 17.35 ?  19  LYS   A CD   1 
ATOM   476  C  CD   B LYS   A 1 19  ? 10.824 -4.700  13.863  0.28 14.84 ?  19  LYS   A CD   1 
ATOM   477  C  CE   A LYS   A 1 19  ? 9.951  -4.071  14.313  0.72 18.47 ?  19  LYS   A CE   1 
ATOM   478  C  CE   B LYS   A 1 19  ? 10.072 -3.853  14.870  0.28 15.96 ?  19  LYS   A CE   1 
ATOM   479  N  NZ   A LYS   A 1 19  ? 10.834 -3.814  15.487  0.72 18.74 ?  19  LYS   A NZ   1 
ATOM   480  N  NZ   B LYS   A 1 19  ? 10.953 -3.472  16.006  0.28 16.61 ?  19  LYS   A NZ   1 
ATOM   481  H  H    A LYS   A 1 19  ? 11.198 -7.229  8.598   0.72 14.23 ?  19  LYS   A H    1 
ATOM   482  H  H    B LYS   A 1 19  ? 11.369 -6.952  9.162   0.28 12.20 ?  19  LYS   A H    1 
ATOM   483  H  HA   A LYS   A 1 19  ? 8.958  -7.030  10.064  0.72 15.23 ?  19  LYS   A HA   1 
ATOM   484  H  HA   B LYS   A 1 19  ? 9.143  -6.726  10.688  0.28 13.68 ?  19  LYS   A HA   1 
ATOM   485  H  HB2  A LYS   A 1 19  ? 10.602 -7.123  11.734  0.72 16.96 ?  19  LYS   A HB2  1 
ATOM   486  H  HB2  B LYS   A 1 19  ? 11.037 -6.714  12.173  0.28 14.70 ?  19  LYS   A HB2  1 
ATOM   487  H  HB3  A LYS   A 1 19  ? 11.381 -5.934  11.039  0.72 16.96 ?  19  LYS   A HB3  1 
ATOM   488  H  HB3  B LYS   A 1 19  ? 11.529 -5.399  11.438  0.28 14.70 ?  19  LYS   A HB3  1 
ATOM   489  H  HG2  A LYS   A 1 19  ? 9.646  -4.473  11.638  0.72 18.53 ?  19  LYS   A HG2  1 
ATOM   490  H  HG2  B LYS   A 1 19  ? 9.654  -4.267  12.243  0.28 16.36 ?  19  LYS   A HG2  1 
ATOM   491  H  HG3  A LYS   A 1 19  ? 8.923  -5.680  12.393  0.72 18.53 ?  19  LYS   A HG3  1 
ATOM   492  H  HG3  B LYS   A 1 19  ? 9.197  -5.592  13.003  0.28 16.36 ?  19  LYS   A HG3  1 
ATOM   493  H  HD2  A LYS   A 1 19  ? 10.767 -5.870  13.825  0.72 20.80 ?  19  LYS   A HD2  1 
ATOM   494  H  HD2  B LYS   A 1 19  ? 11.116 -5.509  14.312  0.28 17.78 ?  19  LYS   A HD2  1 
ATOM   495  H  HD3  A LYS   A 1 19  ? 11.465 -4.651  13.082  0.72 20.80 ?  19  LYS   A HD3  1 
ATOM   496  H  HD3  B LYS   A 1 19  ? 11.590 -4.195  13.550  0.28 17.78 ?  19  LYS   A HD3  1 
ATOM   497  H  HE2  A LYS   A 1 19  ? 9.787  -3.226  13.862  0.72 22.14 ?  19  LYS   A HE2  1 
ATOM   498  H  HE2  B LYS   A 1 19  ? 9.760  -3.043  14.438  0.28 19.13 ?  19  LYS   A HE2  1 
ATOM   499  H  HE3  A LYS   A 1 19  ? 9.118  -4.451  14.632  0.72 22.14 ?  19  LYS   A HE3  1 
ATOM   500  H  HE3  B LYS   A 1 19  ? 9.322  -4.360  15.220  0.28 19.13 ?  19  LYS   A HE3  1 
ATOM   501  H  HZ1  A LYS   A 1 19  ? 10.435 -3.254  16.051  0.72 22.46 ?  19  LYS   A HZ1  1 
ATOM   502  H  HZ1  B LYS   A 1 19  ? 10.497 -2.984  16.593  0.28 19.91 ?  19  LYS   A HZ1  1 
ATOM   503  H  HZ2  A LYS   A 1 19  ? 11.006 -4.578  15.909  0.72 22.46 ?  19  LYS   A HZ2  1 
ATOM   504  H  HZ2  B LYS   A 1 19  ? 11.258 -4.204  16.411  0.28 19.91 ?  19  LYS   A HZ2  1 
ATOM   505  H  HZ3  A LYS   A 1 19  ? 11.601 -3.454  15.216  0.72 22.46 ?  19  LYS   A HZ3  1 
ATOM   506  H  HZ3  B LYS   A 1 19  ? 11.644 -2.997  15.708  0.28 19.91 ?  19  LYS   A HZ3  1 
ATOM   507  N  N    A ASN   A 1 20  ? 8.509  -4.701  9.207   0.72 13.51 ?  20  ASN   A N    1 
ATOM   508  N  N    B ASN   A 1 20  ? 8.560  -4.574  9.626   0.28 13.43 ?  20  ASN   A N    1 
ATOM   509  C  CA   A ASN   A 1 20  ? 8.311  -3.361  8.651   0.72 14.82 ?  20  ASN   A CA   1 
ATOM   510  C  CA   B ASN   A 1 20  ? 8.242  -3.341  8.908   0.28 15.21 ?  20  ASN   A CA   1 
ATOM   511  C  C    A ASN   A 1 20  ? 8.947  -2.367  9.617   0.72 15.74 ?  20  ASN   A C    1 
ATOM   512  C  C    B ASN   A 1 20  ? 8.772  -2.172  9.725   0.28 15.61 ?  20  ASN   A C    1 
ATOM   513  O  O    A ASN   A 1 20  ? 8.430  -2.141  10.717  0.72 16.61 ?  20  ASN   A O    1 
ATOM   514  O  O    B ASN   A 1 20  ? 8.106  -1.660  10.626  0.28 15.90 ?  20  ASN   A O    1 
ATOM   515  C  CB   A ASN   A 1 20  ? 6.817  -3.098  8.446   0.72 15.46 ?  20  ASN   A CB   1 
ATOM   516  C  CB   B ASN   A 1 20  ? 6.740  -3.227  8.687   0.28 16.60 ?  20  ASN   A CB   1 
ATOM   517  C  CG   A ASN   A 1 20  ? 6.501  -1.670  7.999   0.72 16.72 ?  20  ASN   A CG   1 
ATOM   518  C  CG   B ASN   A 1 20  ? 6.321  -1.836  8.271   0.28 18.08 ?  20  ASN   A CG   1 
ATOM   519  O  OD1  A ASN   A 1 20  ? 5.436  -1.150  8.315   0.72 18.90 ?  20  ASN   A OD1  1 
ATOM   520  O  OD1  B ASN   A 1 20  ? 5.609  -1.149  9.002   0.28 19.16 ?  20  ASN   A OD1  1 
ATOM   521  N  ND2  A ASN   A 1 20  ? 7.404  -1.047  7.252   0.72 16.59 ?  20  ASN   A ND2  1 
ATOM   522  N  ND2  B ASN   A 1 20  ? 6.775  -1.404  7.100   0.28 18.36 ?  20  ASN   A ND2  1 
ATOM   523  H  H    A ASN   A 1 20  ? 7.821  -5.028  9.615   0.72 16.19 ?  20  ASN   A H    1 
ATOM   524  H  H    B ASN   A 1 20  ? 7.906  -4.896  10.080  0.28 16.10 ?  20  ASN   A H    1 
ATOM   525  H  HA   A ASN   A 1 20  ? 8.761  -3.308  7.797   0.72 17.77 ?  20  ASN   A HA   1 
ATOM   526  H  HA   B ASN   A 1 20  ? 8.685  -3.340  8.047   0.28 18.23 ?  20  ASN   A HA   1 
ATOM   527  H  HB2  A ASN   A 1 20  ? 6.484  -3.694  7.763   0.72 18.53 ?  20  ASN   A HB2  1 
ATOM   528  H  HB2  B ASN   A 1 20  ? 6.475  -3.844  7.988   0.28 19.90 ?  20  ASN   A HB2  1 
ATOM   529  H  HB3  A ASN   A 1 20  ? 6.357  -3.268  9.284   0.72 18.53 ?  20  ASN   A HB3  1 
ATOM   530  H  HB3  B ASN   A 1 20  ? 6.280  -3.446  9.513   0.28 19.90 ?  20  ASN   A HB3  1 
ATOM   531  H  HD21 A ASN   A 1 20  ? 7.263  -0.238  6.997   0.72 19.89 ?  20  ASN   A HD21 1 
ATOM   532  H  HD21 B ASN   A 1 20  ? 6.562  -0.620  6.818   0.28 22.01 ?  20  ASN   A HD21 1 
ATOM   533  H  HD22 A ASN   A 1 20  ? 8.137  -1.442  7.033   0.72 19.89 ?  20  ASN   A HD22 1 
ATOM   534  H  HD22 B ASN   A 1 20  ? 7.277  -1.912  6.620   0.28 22.01 ?  20  ASN   A HD22 1 
ATOM   535  N  N    A ALA   A 1 21  ? 10.085 -1.795  9.233   0.72 15.91 ?  21  ALA   A N    1 
ATOM   536  N  N    B ALA   A 1 21  ? 9.987  -1.735  9.397   0.28 15.60 ?  21  ALA   A N    1 
ATOM   537  C  CA   A ALA   A 1 21  ? 10.797 -0.925  10.157  0.72 15.92 ?  21  ALA   A CA   1 
ATOM   538  C  CA   B ALA   A 1 21  ? 10.640 -0.689  10.168  0.28 15.56 ?  21  ALA   A CA   1 
ATOM   539  C  C    A ALA   A 1 21  ? 11.737 -0.004  9.401   0.72 15.47 ?  21  ALA   A C    1 
ATOM   540  C  C    B ALA   A 1 21  ? 11.757 -0.066  9.345   0.28 14.92 ?  21  ALA   A C    1 
ATOM   541  O  O    A ALA   A 1 21  ? 12.190 -0.323  8.298   0.72 15.65 ?  21  ALA   A O    1 
ATOM   542  O  O    B ALA   A 1 21  ? 12.310 -0.698  8.441   0.28 14.75 ?  21  ALA   A O    1 
ATOM   543  C  CB   A ALA   A 1 21  ? 11.590 -1.731  11.188  0.72 16.47 ?  21  ALA   A CB   1 
ATOM   544  C  CB   B ALA   A 1 21  ? 11.203 -1.241  11.483  0.28 15.97 ?  21  ALA   A CB   1 
ATOM   545  H  H    A ALA   A 1 21  ? 10.456 -1.899  8.464   0.72 19.07 ?  21  ALA   A H    1 
ATOM   546  H  H    B ALA   A 1 21  ? 10.446 -2.024  8.729   0.28 18.69 ?  21  ALA   A H    1 
ATOM   547  H  HA   A ALA   A 1 21  ? 10.149 -0.381  10.633  0.72 19.08 ?  21  ALA   A HA   1 
ATOM   548  H  HA   B ALA   A 1 21  ? 9.994  0.001   10.381  0.28 18.64 ?  21  ALA   A HA   1 
ATOM   549  H  HB1  A ALA   A 1 21  ? 12.026 -1.116  11.794  0.72 19.74 ?  21  ALA   A HB1  1 
ATOM   550  H  HB1  B ALA   A 1 21  ? 11.650 -0.525  11.960  0.28 19.14 ?  21  ALA   A HB1  1 
ATOM   551  H  HB2  A ALA   A 1 21  ? 10.975 -2.302  11.681  0.72 19.74 ?  21  ALA   A HB2  1 
ATOM   552  H  HB2  B ALA   A 1 21  ? 10.473 -1.589  12.019  0.28 19.14 ?  21  ALA   A HB2  1 
ATOM   553  H  HB3  A ALA   A 1 21  ? 12.246 -2.273  10.727  0.72 19.74 ?  21  ALA   A HB3  1 
ATOM   554  H  HB3  B ALA   A 1 21  ? 11.835 -1.949  11.284  0.28 19.14 ?  21  ALA   A HB3  1 
ATOM   555  N  N    A ASP   A 1 22  ? 12.008 1.145   10.022  0.72 15.38 ?  22  ASP   A N    1 
ATOM   556  N  N    B ASP   A 1 22  ? 12.062 1.190   9.664   0.28 14.87 ?  22  ASP   A N    1 
ATOM   557  C  CA   A ASP   A 1 22  ? 13.038 2.077   9.578   0.72 15.26 ?  22  ASP   A CA   1 
ATOM   558  C  CA   B ASP   A 1 22  ? 13.235 1.859   9.117   0.28 14.92 ?  22  ASP   A CA   1 
ATOM   559  C  C    A ASP   A 1 22  ? 14.365 1.599   10.152  0.72 13.98 ?  22  ASP   A C    1 
ATOM   560  C  C    B ASP   A 1 22  ? 14.486 1.263   9.753   0.28 13.95 ?  22  ASP   A C    1 
ATOM   561  O  O    A ASP   A 1 22  ? 14.550 1.588   11.373  0.72 14.53 ?  22  ASP   A O    1 
ATOM   562  O  O    B ASP   A 1 22  ? 14.601 1.209   10.982  0.28 13.90 ?  22  ASP   A O    1 
ATOM   563  C  CB   A ASP   A 1 22  ? 12.689 3.477   10.079  0.72 17.11 ?  22  ASP   A CB   1 
ATOM   564  C  CB   B ASP   A 1 22  ? 13.141 3.352   9.441   0.28 16.08 ?  22  ASP   A CB   1 
ATOM   565  C  CG   A ASP   A 1 22  ? 13.697 4.534   9.643   0.72 19.18 ?  22  ASP   A CG   1 
ATOM   566  C  CG   B ASP   A 1 22  ? 14.234 4.179   8.795   0.28 16.94 ?  22  ASP   A CG   1 
ATOM   567  O  OD1  A ASP   A 1 22  ? 14.828 4.191   9.245   0.72 19.86 ?  22  ASP   A OD1  1 
ATOM   568  O  OD1  B ASP   A 1 22  ? 15.209 3.597   8.279   0.28 16.91 ?  22  ASP   A OD1  1 
ATOM   569  O  OD2  A ASP   A 1 22  ? 13.356 5.730   9.713   0.72 20.98 -1 22  ASP   A OD2  1 
ATOM   570  O  OD2  B ASP   A 1 22  ? 14.115 5.424   8.813   0.28 17.73 -1 22  ASP   A OD2  1 
ATOM   571  H  H    A ASP   A 1 22  ? 11.583 1.413   10.724  0.72 18.43 ?  22  ASP   A H    1 
ATOM   572  H  H    B ASP   A 1 22  ? 11.590 1.680   10.194  0.28 17.82 ?  22  ASP   A H    1 
ATOM   573  H  HA   A ASP   A 1 22  ? 13.086 2.086   8.611   0.72 18.29 ?  22  ASP   A HA   1 
ATOM   574  H  HA   B ASP   A 1 22  ? 13.268 1.735   8.152   0.28 17.88 ?  22  ASP   A HA   1 
ATOM   575  H  HB2  A ASP   A 1 22  ? 11.814 3.729   9.734   0.72 20.51 ?  22  ASP   A HB2  1 
ATOM   576  H  HB2  B ASP   A 1 22  ? 12.291 3.690   9.130   0.28 19.28 ?  22  ASP   A HB2  1 
ATOM   577  H  HB3  A ASP   A 1 22  ? 12.661 3.466   11.052  0.72 20.51 ?  22  ASP   A HB3  1 
ATOM   578  H  HB3  B ASP   A 1 22  ? 13.224 3.468   10.397  0.28 19.28 ?  22  ASP   A HB3  1 
ATOM   579  N  N    A ILE   A 1 23  ? 15.279 1.181   9.272   0.72 13.56 ?  23  ILE   A N    1 
ATOM   580  N  N    B ILE   A 1 23  ? 15.420 0.798   8.917   0.28 13.43 ?  23  ILE   A N    1 
ATOM   581  C  CA   A ILE   A 1 23  ? 16.529 0.562   9.711   0.72 13.33 ?  23  ILE   A CA   1 
ATOM   582  C  CA   B ILE   A 1 23  ? 16.638 0.175   9.435   0.28 12.85 ?  23  ILE   A CA   1 
ATOM   583  C  C    A ILE   A 1 23  ? 17.337 1.504   10.594  0.72 13.50 ?  23  ILE   A C    1 
ATOM   584  C  C    B ILE   A 1 23  ? 17.397 1.143   10.329  0.28 13.48 ?  23  ILE   A C    1 
ATOM   585  O  O    A ILE   A 1 23  ? 18.058 1.055   11.497  0.72 13.99 ?  23  ILE   A O    1 
ATOM   586  O  O    B ILE   A 1 23  ? 18.061 0.729   11.288  0.28 13.46 ?  23  ILE   A O    1 
ATOM   587  C  CB   A ILE   A 1 23  ? 17.324 0.055   8.488   0.72 13.33 ?  23  ILE   A CB   1 
ATOM   588  C  CB   B ILE   A 1 23  ? 17.517 -0.386  8.293   0.28 12.24 ?  23  ILE   A CB   1 
ATOM   589  C  CG1  A ILE   A 1 23  ? 18.455 -0.875  8.930   0.72 12.99 ?  23  ILE   A CG1  1 
ATOM   590  C  CG1  B ILE   A 1 23  ? 18.605 -1.300  8.869   0.28 11.85 ?  23  ILE   A CG1  1 
ATOM   591  C  CG2  A ILE   A 1 23  ? 17.833 1.223   7.646   0.72 13.70 ?  23  ILE   A CG2  1 
ATOM   592  C  CG2  B ILE   A 1 23  ? 18.147 0.741   7.478   0.28 11.94 ?  23  ILE   A CG2  1 
ATOM   593  C  CD1  A ILE   A 1 23  ? 19.127 -1.592  7.782   0.72 13.40 ?  23  ILE   A CD1  1 
ATOM   594  C  CD1  B ILE   A 1 23  ? 19.508 -1.934  7.828   0.28 11.82 ?  23  ILE   A CD1  1 
ATOM   595  H  H    A ILE   A 1 23  ? 15.189 1.239   8.424   0.72 16.25 ?  23  ILE   A H    1 
ATOM   596  H  H    B ILE   A 1 23  ? 15.372 0.828   8.067   0.28 16.10 ?  23  ILE   A H    1 
ATOM   597  H  HA   A ILE   A 1 23  ? 16.307 -0.211  10.252  0.72 15.98 ?  23  ILE   A HA   1 
ATOM   598  H  HA   B ILE   A 1 23  ? 16.377 -0.580  9.983   0.28 15.40 ?  23  ILE   A HA   1 
ATOM   599  H  HB   A ILE   A 1 23  ? 16.715 -0.463  7.939   0.72 15.97 ?  23  ILE   A HB   1 
ATOM   600  H  HB   B ILE   A 1 23  ? 16.958 -0.916  7.703   0.28 14.66 ?  23  ILE   A HB   1 
ATOM   601  H  HG12 A ILE   A 1 23  ? 19.128 -0.352  9.390   0.72 15.57 ?  23  ILE   A HG12 1 
ATOM   602  H  HG12 B ILE   A 1 23  ? 19.167 -0.783  9.466   0.28 14.19 ?  23  ILE   A HG12 1 
ATOM   603  H  HG13 A ILE   A 1 23  ? 18.092 -1.547  9.529   0.72 15.57 ?  23  ILE   A HG13 1 
ATOM   604  H  HG13 B ILE   A 1 23  ? 18.180 -2.020  9.363   0.28 14.19 ?  23  ILE   A HG13 1 
ATOM   605  H  HG21 A ILE   A 1 23  ? 18.184 0.881   6.809   0.72 16.42 ?  23  ILE   A HG21 1 
ATOM   606  H  HG21 B ILE   A 1 23  ? 18.513 0.371   6.657   0.28 14.31 ?  23  ILE   A HG21 1 
ATOM   607  H  HG22 A ILE   A 1 23  ? 17.092 1.829   7.466   0.72 16.42 ?  23  ILE   A HG22 1 
ATOM   608  H  HG22 B ILE   A 1 23  ? 17.467 1.397   7.270   0.28 14.31 ?  23  ILE   A HG22 1 
ATOM   609  H  HG23 A ILE   A 1 23  ? 18.527 1.690   8.132   0.72 16.42 ?  23  ILE   A HG23 1 
ATOM   610  H  HG23 B ILE   A 1 23  ? 18.856 1.150   7.998   0.28 14.31 ?  23  ILE   A HG23 1 
ATOM   611  H  HD11 A ILE   A 1 23  ? 19.783 -2.209  8.139   0.72 16.06 ?  23  ILE   A HD11 1 
ATOM   612  H  HD11 B ILE   A 1 23  ? 20.075 -2.592  8.263   0.28 14.16 ?  23  ILE   A HD11 1 
ATOM   613  H  HD12 A ILE   A 1 23  ? 18.454 -2.079  7.279   0.72 16.06 ?  23  ILE   A HD12 1 
ATOM   614  H  HD12 B ILE   A 1 23  ? 18.958 -2.364  7.156   0.28 14.16 ?  23  ILE   A HD12 1 
ATOM   615  H  HD13 A ILE   A 1 23  ? 19.558 -0.939  7.212   0.72 16.06 ?  23  ILE   A HD13 1 
ATOM   616  H  HD13 B ILE   A 1 23  ? 20.053 -1.245  7.421   0.28 14.16 ?  23  ILE   A HD13 1 
ATOM   617  N  N    A VAL   A 1 24  ? 17.222 2.816   10.369  0.72 14.11 ?  24  VAL   A N    1 
ATOM   618  N  N    B VAL   A 1 24  ? 17.300 2.443   10.045  0.28 14.40 ?  24  VAL   A N    1 
ATOM   619  C  CA   A VAL   A 1 24  ? 17.903 3.780   11.231  0.72 15.22 ?  24  VAL   A CA   1 
ATOM   620  C  CA   B VAL   A 1 24  ? 17.952 3.442   10.884  0.28 15.48 ?  24  VAL   A CA   1 
ATOM   621  C  C    A VAL   A 1 24  ? 17.366 3.689   12.653  0.72 15.70 ?  24  VAL   A C    1 
ATOM   622  C  C    B VAL   A 1 24  ? 17.347 3.438   12.281  0.28 16.43 ?  24  VAL   A C    1 
ATOM   623  O  O    A VAL   A 1 24  ? 18.129 3.587   13.624  0.72 16.28 ?  24  VAL   A O    1 
ATOM   624  O  O    B VAL   A 1 24  ? 18.066 3.502   13.286  0.28 17.15 ?  24  VAL   A O    1 
ATOM   625  C  CB   A VAL   A 1 24  ? 17.761 5.204   10.663  0.72 16.06 ?  24  VAL   A CB   1 
ATOM   626  C  CB   B VAL   A 1 24  ? 17.867 4.827   10.218  0.28 15.77 ?  24  VAL   A CB   1 
ATOM   627  C  CG1  A VAL   A 1 24  ? 18.238 6.244   11.678  0.72 16.85 ?  24  VAL   A CG1  1 
ATOM   628  C  CG1  B VAL   A 1 24  ? 18.538 5.877   11.085  0.28 16.44 ?  24  VAL   A CG1  1 
ATOM   629  C  CG2  A VAL   A 1 24  ? 18.519 5.333   9.353   0.72 16.82 ?  24  VAL   A CG2  1 
ATOM   630  C  CG2  B VAL   A 1 24  ? 18.491 4.782   8.831   0.28 15.49 ?  24  VAL   A CG2  1 
ATOM   631  H  H    A VAL   A 1 24  ? 16.763 3.167   9.730   0.72 16.91 ?  24  VAL   A H    1 
ATOM   632  H  H    B VAL   A 1 24  ? 16.862 2.765   9.382   0.28 17.25 ?  24  VAL   A H    1 
ATOM   633  H  HA   A VAL   A 1 24  ? 18.847 3.568   11.254  0.72 18.25 ?  24  VAL   A HA   1 
ATOM   634  H  HA   B VAL   A 1 24  ? 18.889 3.211   10.972  0.28 18.56 ?  24  VAL   A HA   1 
ATOM   635  H  HB   A VAL   A 1 24  ? 16.825 5.380   10.476  0.72 19.25 ?  24  VAL   A HB   1 
ATOM   636  H  HB   B VAL   A 1 24  ? 16.934 5.072   10.119  0.28 18.90 ?  24  VAL   A HB   1 
ATOM   637  H  HG11 A VAL   A 1 24  ? 18.394 7.084   11.217  0.72 20.20 ?  24  VAL   A HG11 1 
ATOM   638  H  HG11 B VAL   A 1 24  ? 18.748 6.649   10.539  0.28 19.70 ?  24  VAL   A HG11 1 
ATOM   639  H  HG12 A VAL   A 1 24  ? 17.557 6.362   12.355  0.72 20.20 ?  24  VAL   A HG12 1 
ATOM   640  H  HG12 B VAL   A 1 24  ? 17.926 6.130   11.793  0.28 19.70 ?  24  VAL   A HG12 1 
ATOM   641  H  HG13 A VAL   A 1 24  ? 19.064 5.933   12.081  0.72 20.20 ?  24  VAL   A HG13 1 
ATOM   642  H  HG13 B VAL   A 1 24  ? 19.349 5.505   11.462  0.28 19.70 ?  24  VAL   A HG13 1 
ATOM   643  H  HG21 A VAL   A 1 24  ? 18.420 6.238   9.013   0.72 20.17 ?  24  VAL   A HG21 1 
ATOM   644  H  HG21 B VAL   A 1 24  ? 18.551 5.685   8.484   0.28 18.57 ?  24  VAL   A HG21 1 
ATOM   645  H  HG22 A VAL   A 1 24  ? 19.459 5.143   9.509   0.72 20.17 ?  24  VAL   A HG22 1 
ATOM   646  H  HG22 B VAL   A 1 24  ? 19.377 4.395   8.898   0.28 18.57 ?  24  VAL   A HG22 1 
ATOM   647  H  HG23 A VAL   A 1 24  ? 18.158 4.700   8.712   0.72 20.17 ?  24  VAL   A HG23 1 
ATOM   648  H  HG23 B VAL   A 1 24  ? 17.936 4.239   8.251   0.28 18.57 ?  24  VAL   A HG23 1 
ATOM   649  N  N    A GLU   A 1 25  ? 16.041 3.738   12.796  0.72 16.56 ?  25  GLU   A N    1 
ATOM   650  N  N    B GLU   A 1 25  ? 16.017 3.347   12.370  0.28 16.84 ?  25  GLU   A N    1 
ATOM   651  C  CA   A GLU   A 1 25  ? 15.445 3.675   14.125  0.72 18.00 ?  25  GLU   A CA   1 
ATOM   652  C  CA   B GLU   A 1 25  ? 15.370 3.292   13.677  0.28 17.81 ?  25  GLU   A CA   1 
ATOM   653  C  C    A GLU   A 1 25  ? 15.675 2.313   14.767  0.72 17.16 ?  25  GLU   A C    1 
ATOM   654  C  C    B GLU   A 1 25  ? 15.630 1.959   14.369  0.28 17.60 ?  25  GLU   A C    1 
ATOM   655  O  O    A GLU   A 1 25  ? 15.896 2.223   15.981  0.72 17.71 ?  25  GLU   A O    1 
ATOM   656  O  O    B GLU   A 1 25  ? 15.820 1.915   15.590  0.28 17.86 ?  25  GLU   A O    1 
ATOM   657  C  CB   A GLU   A 1 25  ? 13.956 4.020   14.044  0.72 20.69 ?  25  GLU   A CB   1 
ATOM   658  C  CB   B GLU   A 1 25  ? 13.870 3.564   13.537  0.28 19.11 ?  25  GLU   A CB   1 
ATOM   659  C  CG   A GLU   A 1 25  ? 13.697 5.480   13.684  0.72 24.02 ?  25  GLU   A CG   1 
ATOM   660  C  CG   B GLU   A 1 25  ? 13.551 4.937   12.959  0.28 20.89 ?  25  GLU   A CG   1 
ATOM   661  C  CD   A GLU   A 1 25  ? 14.490 6.450   14.549  0.72 26.79 ?  25  GLU   A CD   1 
ATOM   662  C  CD   B GLU   A 1 25  ? 14.092 6.064   13.812  0.28 22.44 ?  25  GLU   A CD   1 
ATOM   663  O  OE1  A GLU   A 1 25  ? 14.555 6.241   15.780  0.72 27.58 ?  25  GLU   A OE1  1 
ATOM   664  O  OE1  B GLU   A 1 25  ? 14.176 5.883   15.045  0.28 23.29 ?  25  GLU   A OE1  1 
ATOM   665  O  OE2  A GLU   A 1 25  ? 15.067 7.406   13.992  0.72 28.04 -1 25  GLU   A OE2  1 
ATOM   666  O  OE2  B GLU   A 1 25  ? 14.438 7.126   13.251  0.28 23.03 -1 25  GLU   A OE2  1 
ATOM   667  H  H    A GLU   A 1 25  ? 15.478 3.818   12.148  0.72 19.85 ?  25  GLU   A H    1 
ATOM   668  H  H    B GLU   A 1 25  ? 15.479 3.316   11.700  0.28 20.18 ?  25  GLU   A H    1 
ATOM   669  H  HA   A GLU   A 1 25  ? 15.874 4.335   14.690  0.72 21.58 ?  25  GLU   A HA   1 
ATOM   670  H  HA   B GLU   A 1 25  ? 15.745 3.984   14.237  0.28 21.35 ?  25  GLU   A HA   1 
ATOM   671  H  HB2  A GLU   A 1 25  ? 13.535 3.472   13.360  0.72 24.80 ?  25  GLU   A HB2  1 
ATOM   672  H  HB2  B GLU   A 1 25  ? 13.482 2.900   12.948  0.28 22.91 ?  25  GLU   A HB2  1 
ATOM   673  H  HB3  A GLU   A 1 25  ? 13.539 3.852   14.903  0.72 24.80 ?  25  GLU   A HB3  1 
ATOM   674  H  HB3  B GLU   A 1 25  ? 13.459 3.509   14.414  0.28 22.91 ?  25  GLU   A HB3  1 
ATOM   675  H  HG2  A GLU   A 1 25  ? 13.956 5.628   12.762  0.72 28.80 ?  25  GLU   A HG2  1 
ATOM   676  H  HG2  B GLU   A 1 25  ? 13.950 5.014   12.079  0.28 25.04 ?  25  GLU   A HG2  1 
ATOM   677  H  HG3  A GLU   A 1 25  ? 12.751 5.671   13.799  0.72 28.80 ?  25  GLU   A HG3  1 
ATOM   678  H  HG3  B GLU   A 1 25  ? 12.590 5.044   12.901  0.28 25.04 ?  25  GLU   A HG3  1 
ATOM   679  N  N    A GLU   A 1 26  ? 15.644 1.243   13.968  0.72 16.89 ?  26  GLU   A N    1 
ATOM   680  N  N    B GLU   A 1 26  ? 15.647 0.859   13.609  0.28 17.07 ?  26  GLU   A N    1 
ATOM   681  C  CA   A GLU   A 1 26  ? 15.930 -0.084  14.504  0.72 16.75 ?  26  GLU   A CA   1 
ATOM   682  C  CA   B GLU   A 1 26  ? 15.999 -0.431  14.194  0.28 17.06 ?  26  GLU   A CA   1 
ATOM   683  C  C    A GLU   A 1 26  ? 17.356 -0.165  15.033  0.72 15.63 ?  26  GLU   A C    1 
ATOM   684  C  C    B GLU   A 1 26  ? 17.421 -0.417  14.739  0.28 16.83 ?  26  GLU   A C    1 
ATOM   685  O  O    A GLU   A 1 26  ? 17.598 -0.683  16.128  0.72 15.99 ?  26  GLU   A O    1 
ATOM   686  O  O    B GLU   A 1 26  ? 17.696 -0.996  15.796  0.28 16.57 ?  26  GLU   A O    1 
ATOM   687  C  CB   A GLU   A 1 26  ? 15.713 -1.142  13.423  0.72 18.40 ?  26  GLU   A CB   1 
ATOM   688  C  CB   B GLU   A 1 26  ? 15.838 -1.544  13.157  0.28 17.27 ?  26  GLU   A CB   1 
ATOM   689  C  CG   A GLU   A 1 26  ? 14.299 -1.675  13.322  0.72 21.73 ?  26  GLU   A CG   1 
ATOM   690  C  CG   B GLU   A 1 26  ? 14.400 -1.940  12.901  0.28 17.58 ?  26  GLU   A CG   1 
ATOM   691  C  CD   A GLU   A 1 26  ? 13.905 -2.545  14.508  0.72 23.62 ?  26  GLU   A CD   1 
ATOM   692  C  CD   B GLU   A 1 26  ? 13.711 -2.438  14.148  0.28 17.55 ?  26  GLU   A CD   1 
ATOM   693  O  OE1  A GLU   A 1 26  ? 14.327 -3.726  14.585  0.72 23.72 ?  26  GLU   A OE1  1 
ATOM   694  O  OE1  B GLU   A 1 26  ? 14.316 -3.255  14.871  0.28 17.92 ?  26  GLU   A OE1  1 
ATOM   695  O  OE2  A GLU   A 1 26  ? 13.169 -2.036  15.367  0.72 25.21 -1 26  GLU   A OE2  1 
ATOM   696  O  OE2  B GLU   A 1 26  ? 12.581 -1.986  14.417  0.28 16.58 -1 26  GLU   A OE2  1 
ATOM   697  H  H    A GLU   A 1 26  ? 15.462 1.270   13.127  0.72 20.25 ?  26  GLU   A H    1 
ATOM   698  H  H    B GLU   A 1 26  ? 15.459 0.833   12.771  0.28 20.46 ?  26  GLU   A H    1 
ATOM   699  H  HA   A GLU   A 1 26  ? 15.319 -0.260  15.235  0.72 20.08 ?  26  GLU   A HA   1 
ATOM   700  H  HA   B GLU   A 1 26  ? 15.402 -0.619  14.934  0.28 20.45 ?  26  GLU   A HA   1 
ATOM   701  H  HB2  A GLU   A 1 26  ? 15.944 -0.756  12.564  0.72 22.06 ?  26  GLU   A HB2  1 
ATOM   702  H  HB2  B GLU   A 1 26  ? 16.212 -1.247  12.313  0.28 20.70 ?  26  GLU   A HB2  1 
ATOM   703  H  HB3  A GLU   A 1 26  ? 16.298 -1.889  13.614  0.72 22.06 ?  26  GLU   A HB3  1 
ATOM   704  H  HB3  B GLU   A 1 26  ? 16.312 -2.335  13.464  0.28 20.70 ?  26  GLU   A HB3  1 
ATOM   705  H  HG2  A GLU   A 1 26  ? 13.684 -0.923  13.274  0.72 26.05 ?  26  GLU   A HG2  1 
ATOM   706  H  HG2  B GLU   A 1 26  ? 13.906 -1.168  12.595  0.28 21.08 ?  26  GLU   A HG2  1 
ATOM   707  H  HG3  A GLU   A 1 26  ? 14.221 -2.215  12.522  0.72 26.05 ?  26  GLU   A HG3  1 
ATOM   708  H  HG3  B GLU   A 1 26  ? 14.375 -2.644  12.233  0.28 21.08 ?  26  GLU   A HG3  1 
ATOM   709  N  N    A ALA   A 1 27  ? 18.321 0.332   14.259  0.72 14.83 ?  27  ALA   A N    1 
ATOM   710  N  N    B ALA   A 1 27  ? 18.341 0.233   14.027  0.28 16.72 ?  27  ALA   A N    1 
ATOM   711  C  CA   A ALA   A 1 27  ? 19.712 0.271   14.697  0.72 15.45 ?  27  ALA   A CA   1 
ATOM   712  C  CA   B ALA   A 1 27  ? 19.717 0.299   14.507  0.28 17.07 ?  27  ALA   A CA   1 
ATOM   713  C  C    A ALA   A 1 27  ? 19.919 1.056   15.985  0.72 16.85 ?  27  ALA   A C    1 
ATOM   714  C  C    B ALA   A 1 27  ? 19.824 1.167   15.756  0.28 17.98 ?  27  ALA   A C    1 
ATOM   715  O  O    A ALA   A 1 27  ? 20.605 0.593   16.904  0.72 17.00 ?  27  ALA   A O    1 
ATOM   716  O  O    B ALA   A 1 27  ? 20.497 0.792   16.723  0.28 17.86 ?  27  ALA   A O    1 
ATOM   717  C  CB   A ALA   A 1 27  ? 20.639 0.791   13.596  0.72 15.22 ?  27  ALA   A CB   1 
ATOM   718  C  CB   B ALA   A 1 27  ? 20.636 0.818   13.401  0.28 16.84 ?  27  ALA   A CB   1 
ATOM   719  H  H    A ALA   A 1 27  ? 18.200 0.704   13.494  0.72 17.78 ?  27  ALA   A H    1 
ATOM   720  H  H    B ALA   A 1 27  ? 18.196 0.628   13.278  0.28 20.04 ?  27  ALA   A H    1 
ATOM   721  H  HA   A ALA   A 1 27  ? 19.944 -0.652  14.868  0.72 18.52 ?  27  ALA   A HA   1 
ATOM   722  H  HA   B ALA   A 1 27  ? 20.009 -0.595  14.738  0.28 20.46 ?  27  ALA   A HA   1 
ATOM   723  H  HB1  A ALA   A 1 27  ? 21.558 0.737   13.906  0.72 18.24 ?  27  ALA   A HB1  1 
ATOM   724  H  HB1  B ALA   A 1 27  ? 21.545 0.855   13.740  0.28 20.18 ?  27  ALA   A HB1  1 
ATOM   725  H  HB2  A ALA   A 1 27  ? 20.527 0.241   12.804  0.72 18.24 ?  27  ALA   A HB2  1 
ATOM   726  H  HB2  B ALA   A 1 27  ? 20.592 0.213   12.642  0.28 20.18 ?  27  ALA   A HB2  1 
ATOM   727  H  HB3  A ALA   A 1 27  ? 20.411 1.711   13.395  0.72 18.24 ?  27  ALA   A HB3  1 
ATOM   728  H  HB3  B ALA   A 1 27  ? 20.345 1.703   13.135  0.28 20.18 ?  27  ALA   A HB3  1 
ATOM   729  N  N    A LYS   A 1 28  ? 19.336 2.252   16.074  0.72 18.60 ?  28  LYS   A N    1 
ATOM   730  N  N    B LYS   A 1 28  ? 19.156 2.324   15.763  0.28 19.32 ?  28  LYS   A N    1 
ATOM   731  C  CA   A LYS   A 1 28  ? 19.483 3.046   17.289  0.72 21.05 ?  28  LYS   A CA   1 
ATOM   732  C  CA   B LYS   A 1 28  ? 19.269 3.240   16.893  0.28 21.03 ?  28  LYS   A CA   1 
ATOM   733  C  C    A LYS   A 1 28  ? 18.900 2.323   18.495  0.72 21.88 ?  28  LYS   A C    1 
ATOM   734  C  C    B LYS   A 1 28  ? 18.749 2.643   18.193  0.28 22.08 ?  28  LYS   A C    1 
ATOM   735  O  O    A LYS   A 1 28  ? 19.456 2.393   19.597  0.72 23.11 ?  28  LYS   A O    1 
ATOM   736  O  O    B LYS   A 1 28  ? 19.101 3.138   19.269  0.28 22.15 ?  28  LYS   A O    1 
ATOM   737  C  CB   A LYS   A 1 28  ? 18.850 4.426   17.105  0.72 23.08 ?  28  LYS   A CB   1 
ATOM   738  C  CB   B LYS   A 1 28  ? 18.539 4.553   16.601  0.28 22.11 ?  28  LYS   A CB   1 
ATOM   739  C  CG   A LYS   A 1 28  ? 19.659 5.341   16.198  0.72 25.10 ?  28  LYS   A CG   1 
ATOM   740  C  CG   B LYS   A 1 28  ? 19.277 5.443   15.617  0.28 23.25 ?  28  LYS   A CG   1 
ATOM   741  C  CD   A LYS   A 1 28  ? 19.198 6.786   16.275  0.72 27.53 ?  28  LYS   A CD   1 
ATOM   742  C  CD   B LYS   A 1 28  ? 18.757 6.874   15.614  0.28 24.48 ?  28  LYS   A CD   1 
ATOM   743  C  CE   A LYS   A 1 28  ? 17.883 6.989   15.554  0.72 29.27 ?  28  LYS   A CE   1 
ATOM   744  C  CE   B LYS   A 1 28  ? 17.529 7.037   14.733  0.28 25.49 ?  28  LYS   A CE   1 
ATOM   745  N  NZ   A LYS   A 1 28  ? 17.527 8.432   15.473  0.72 30.42 ?  28  LYS   A NZ   1 
ATOM   746  N  NZ   B LYS   A 1 28  ? 17.175 8.474   14.546  0.28 25.95 ?  28  LYS   A NZ   1 
ATOM   747  H  H    A LYS   A 1 28  ? 18.872 2.620   15.458  0.72 22.30 ?  28  LYS   A H    1 
ATOM   748  H  H    B LYS   A 1 28  ? 18.644 2.597   15.130  0.28 23.16 ?  28  LYS   A H    1 
ATOM   749  H  HA   A LYS   A 1 28  ? 20.425 3.179   17.469  0.72 25.23 ?  28  LYS   A HA   1 
ATOM   750  H  HA   B LYS   A 1 28  ? 20.205 3.449   17.023  0.28 25.21 ?  28  LYS   A HA   1 
ATOM   751  H  HB2  A LYS   A 1 28  ? 17.972 4.323   16.711  0.72 27.68 ?  28  LYS   A HB2  1 
ATOM   752  H  HB2  B LYS   A 1 28  ? 17.666 4.351   16.230  0.28 26.51 ?  28  LYS   A HB2  1 
ATOM   753  H  HB3  A LYS   A 1 28  ? 18.777 4.861   17.970  0.72 27.68 ?  28  LYS   A HB3  1 
ATOM   754  H  HB3  B LYS   A 1 28  ? 18.438 5.043   17.434  0.28 26.51 ?  28  LYS   A HB3  1 
ATOM   755  H  HG2  A LYS   A 1 28  ? 20.592 5.309   16.462  0.72 30.10 ?  28  LYS   A HG2  1 
ATOM   756  H  HG2  B LYS   A 1 28  ? 20.216 5.465   15.856  0.28 27.87 ?  28  LYS   A HG2  1 
ATOM   757  H  HG3  A LYS   A 1 28  ? 19.562 5.044   15.279  0.72 30.10 ?  28  LYS   A HG3  1 
ATOM   758  H  HG3  B LYS   A 1 28  ? 19.171 5.081   14.724  0.28 27.87 ?  28  LYS   A HG3  1 
ATOM   759  H  HD2  A LYS   A 1 28  ? 19.076 7.034   17.205  0.72 33.01 ?  28  LYS   A HD2  1 
ATOM   760  H  HD2  B LYS   A 1 28  ? 18.515 7.129   16.518  0.28 29.36 ?  28  LYS   A HD2  1 
ATOM   761  H  HD3  A LYS   A 1 28  ? 19.863 7.357   15.860  0.72 33.01 ?  28  LYS   A HD3  1 
ATOM   762  H  HD3  B LYS   A 1 28  ? 19.451 7.462   15.277  0.28 29.36 ?  28  LYS   A HD3  1 
ATOM   763  H  HE2  A LYS   A 1 28  ? 17.956 6.643   14.650  0.72 35.10 ?  28  LYS   A HE2  1 
ATOM   764  H  HE2  B LYS   A 1 28  ? 17.709 6.653   13.861  0.28 30.56 ?  28  LYS   A HE2  1 
ATOM   765  H  HE3  A LYS   A 1 28  ? 17.178 6.528   16.034  0.72 35.10 ?  28  LYS   A HE3  1 
ATOM   766  H  HE3  B LYS   A 1 28  ? 16.775 6.590   15.146  0.28 30.56 ?  28  LYS   A HE3  1 
ATOM   767  H  HZ1  A LYS   A 1 28  ? 16.753 8.531   15.046  0.72 36.48 ?  28  LYS   A HZ1  1 
ATOM   768  H  HZ1  B LYS   A 1 28  ? 16.456 8.547   14.027  0.28 31.12 ?  28  LYS   A HZ1  1 
ATOM   769  H  HZ2  A LYS   A 1 28  ? 17.453 8.772   16.292  0.72 36.48 ?  28  LYS   A HZ2  1 
ATOM   770  H  HZ2  B LYS   A 1 28  ? 17.003 8.849   15.335  0.28 31.12 ?  28  LYS   A HZ2  1 
ATOM   771  H  HZ3  A LYS   A 1 28  ? 18.160 8.877   15.032  0.72 36.48 ?  28  LYS   A HZ3  1 
ATOM   772  H  HZ3  B LYS   A 1 28  ? 17.853 8.907   14.163  0.28 31.12 ?  28  LYS   A HZ3  1 
ATOM   773  N  N    A LYS   A 1 29  ? 17.789 1.607   18.303  0.72 22.70 ?  29  LYS   A N    1 
ATOM   774  N  N    B LYS   A 1 29  ? 17.924 1.599   18.126  0.28 23.29 ?  29  LYS   A N    1 
ATOM   775  C  CA   A LYS   A 1 29  ? 17.175 0.879   19.411  0.72 24.65 ?  29  LYS   A CA   1 
ATOM   776  C  CA   B LYS   A 1 29  ? 17.355 0.988   19.321  0.28 24.77 ?  29  LYS   A CA   1 
ATOM   777  C  C    A LYS   A 1 29  ? 17.992 -0.353  19.785  0.72 24.48 ?  29  LYS   A C    1 
ATOM   778  C  C    B LYS   A 1 29  ? 18.106 -0.268  19.743  0.28 24.52 ?  29  LYS   A C    1 
ATOM   779  O  O    A LYS   A 1 29  ? 18.270 -0.590  20.968  0.72 25.20 ?  29  LYS   A O    1 
ATOM   780  O  O    B LYS   A 1 29  ? 18.448 -0.428  20.919  0.28 25.08 ?  29  LYS   A O    1 
ATOM   781  C  CB   A LYS   A 1 29  ? 15.746 0.475   19.043  0.72 27.16 ?  29  LYS   A CB   1 
ATOM   782  C  CB   B LYS   A 1 29  ? 15.883 0.648   19.064  0.28 26.34 ?  29  LYS   A CB   1 
ATOM   783  C  CG   A LYS   A 1 29  ? 14.987 -0.225  20.163  0.72 29.85 ?  29  LYS   A CG   1 
ATOM   784  C  CG   B LYS   A 1 29  ? 15.108 0.199   20.290  0.28 27.77 ?  29  LYS   A CG   1 
ATOM   785  C  CD   A LYS   A 1 29  ? 14.692 0.731   21.310  0.72 32.27 ?  29  LYS   A CD   1 
ATOM   786  C  CD   B LYS   A 1 29  ? 14.816 1.365   21.216  0.28 28.95 ?  29  LYS   A CD   1 
ATOM   787  C  CE   A LYS   A 1 29  ? 13.816 0.078   22.367  0.72 33.91 ?  29  LYS   A CE   1 
ATOM   788  C  CE   B LYS   A 1 29  ? 13.860 0.963   22.325  0.28 29.85 ?  29  LYS   A CE   1 
ATOM   789  N  NZ   A LYS   A 1 29  ? 13.460 1.030   23.455  0.72 34.93 ?  29  LYS   A NZ   1 
ATOM   790  N  NZ   B LYS   A 1 29  ? 13.551 2.105   23.226  0.28 30.40 ?  29  LYS   A NZ   1 
ATOM   791  H  H    A LYS   A 1 29  ? 17.373 1.533   17.553  0.72 27.22 ?  29  LYS   A H    1 
ATOM   792  H  H    B LYS   A 1 29  ? 17.674 1.220   17.389  0.28 27.92 ?  29  LYS   A H    1 
ATOM   793  H  HA   A LYS   A 1 29  ? 17.130 1.458   20.187  0.72 29.56 ?  29  LYS   A HA   1 
ATOM   794  H  HA   B LYS   A 1 29  ? 17.397 1.626   20.050  0.28 29.70 ?  29  LYS   A HA   1 
ATOM   795  H  HB2  A LYS   A 1 29  ? 15.246 1.271   18.805  0.72 32.57 ?  29  LYS   A HB2  1 
ATOM   796  H  HB2  B LYS   A 1 29  ? 15.445 1.437   18.712  0.28 31.58 ?  29  LYS   A HB2  1 
ATOM   797  H  HB3  A LYS   A 1 29  ? 15.777 -0.131  18.287  0.72 32.57 ?  29  LYS   A HB3  1 
ATOM   798  H  HB3  B LYS   A 1 29  ? 15.844 -0.067  18.412  0.28 31.58 ?  29  LYS   A HB3  1 
ATOM   799  H  HG2  A LYS   A 1 29  ? 14.143 -0.556  19.820  0.72 35.80 ?  29  LYS   A HG2  1 
ATOM   800  H  HG2  B LYS   A 1 29  ? 14.262 -0.185  20.009  0.28 33.30 ?  29  LYS   A HG2  1 
ATOM   801  H  HG3  A LYS   A 1 29  ? 15.518 -0.961  20.509  0.72 35.80 ?  29  LYS   A HG3  1 
ATOM   802  H  HG3  B LYS   A 1 29  ? 15.627 -0.458  20.781  0.28 33.30 ?  29  LYS   A HG3  1 
ATOM   803  H  HD2  A LYS   A 1 29  ? 15.526 0.997   21.728  0.72 38.71 ?  29  LYS   A HD2  1 
ATOM   804  H  HD2  B LYS   A 1 29  ? 15.644 1.667   21.621  0.28 34.71 ?  29  LYS   A HD2  1 
ATOM   805  H  HD3  A LYS   A 1 29  ? 14.226 1.509   20.965  0.72 38.71 ?  29  LYS   A HD3  1 
ATOM   806  H  HD3  B LYS   A 1 29  ? 14.409 2.084   20.707  0.28 34.71 ?  29  LYS   A HD3  1 
ATOM   807  H  HE2  A LYS   A 1 29  ? 12.995 -0.232  21.954  0.72 40.67 ?  29  LYS   A HE2  1 
ATOM   808  H  HE2  B LYS   A 1 29  ? 13.029 0.652   21.932  0.28 35.79 ?  29  LYS   A HE2  1 
ATOM   809  H  HE3  A LYS   A 1 29  ? 14.294 -0.669  22.761  0.72 40.67 ?  29  LYS   A HE3  1 
ATOM   810  H  HE3  B LYS   A 1 29  ? 14.264 0.258   22.854  0.28 35.79 ?  29  LYS   A HE3  1 
ATOM   811  H  HZ1  A LYS   A 1 29  ? 12.948 0.623   24.059  0.72 41.89 ?  29  LYS   A HZ1  1 
ATOM   812  H  HZ1  B LYS   A 1 29  ? 12.990 1.844   23.866  0.28 36.46 ?  29  LYS   A HZ1  1 
ATOM   813  H  HZ2  A LYS   A 1 29  ? 14.199 1.325   23.854  0.72 41.89 ?  29  LYS   A HZ2  1 
ATOM   814  H  HZ2  B LYS   A 1 29  ? 14.299 2.406   23.602  0.28 36.46 ?  29  LYS   A HZ2  1 
ATOM   815  H  HZ3  A LYS   A 1 29  ? 13.015 1.723   23.119  0.72 41.89 ?  29  LYS   A HZ3  1 
ATOM   816  H  HZ3  B LYS   A 1 29  ? 13.175 2.765   22.762  0.28 36.46 ?  29  LYS   A HZ3  1 
ATOM   817  N  N    . VAL   A 1 30  ? 18.368 -1.164  18.794  1.00 23.80 ?  30  VAL   A N    1 
ATOM   818  C  CA   . VAL   A 1 30  ? 19.014 -2.438  19.098  1.00 22.96 ?  30  VAL   A CA   1 
ATOM   819  C  C    . VAL   A 1 30  ? 20.513 -2.280  19.330  1.00 21.76 ?  30  VAL   A C    1 
ATOM   820  O  O    . VAL   A 1 30  ? 21.097 -3.006  20.142  1.00 22.55 ?  30  VAL   A O    1 
ATOM   821  C  CB   . VAL   A 1 30  ? 18.721 -3.437  17.963  1.00 23.46 ?  30  VAL   A CB   1 
ATOM   822  C  CG1  . VAL   A 1 30  ? 19.482 -4.736  18.178  1.00 23.95 ?  30  VAL   A CG1  1 
ATOM   823  C  CG2  . VAL   A 1 30  ? 17.224 -3.701  17.859  1.00 24.09 ?  30  VAL   A CG2  1 
ATOM   824  H  H    A VAL   A 1 30  ? 18.258 -1.005  17.957  0.72 28.54 ?  30  VAL   A H    1 
ATOM   825  H  H    B VAL   A 1 30  ? 18.168 -1.060  17.965  0.28 28.54 ?  30  VAL   A H    1 
ATOM   826  H  HA   . VAL   A 1 30  ? 18.617 -2.798  19.907  1.00 27.53 ?  30  VAL   A HA   1 
ATOM   827  H  HB   . VAL   A 1 30  ? 19.016 -3.057  17.120  1.00 28.14 ?  30  VAL   A HB   1 
ATOM   828  H  HG11 . VAL   A 1 30  ? 19.108 -5.419  17.598  1.00 28.71 ?  30  VAL   A HG11 1 
ATOM   829  H  HG12 . VAL   A 1 30  ? 20.416 -4.597  17.964  1.00 28.71 ?  30  VAL   A HG12 1 
ATOM   830  H  HG13 . VAL   A 1 30  ? 19.387 -5.004  19.105  1.00 28.71 ?  30  VAL   A HG13 1 
ATOM   831  H  HG21 . VAL   A 1 30  ? 17.067 -4.366  17.169  1.00 28.89 ?  30  VAL   A HG21 1 
ATOM   832  H  HG22 . VAL   A 1 30  ? 16.902 -4.029  18.712  1.00 28.89 ?  30  VAL   A HG22 1 
ATOM   833  H  HG23 . VAL   A 1 30  ? 16.773 -2.874  17.629  1.00 28.89 ?  30  VAL   A HG23 1 
ATOM   834  N  N    . LYS   A 1 31  ? 21.155 -1.348  18.636  1.00 21.07 ?  31  LYS   A N    1 
ATOM   835  C  CA   . LYS   A 1 31  ? 22.609 -1.247  18.595  1.00 21.83 ?  31  LYS   A CA   1 
ATOM   836  C  C    . LYS   A 1 31  ? 23.221 -2.613  18.267  1.00 19.77 ?  31  LYS   A C    1 
ATOM   837  O  O    . LYS   A 1 31  ? 23.988 -3.167  19.060  1.00 20.74 ?  31  LYS   A O    1 
ATOM   838  C  CB   . LYS   A 1 31  ? 23.181 -0.686  19.889  1.00 26.33 ?  31  LYS   A CB   1 
ATOM   839  C  CG   . LYS   A 1 31  ? 22.493 0.579   20.372  1.00 31.62 ?  31  LYS   A CG   1 
ATOM   840  C  CD   . LYS   A 1 31  ? 23.499 1.645   20.779  1.00 35.78 ?  31  LYS   A CD   1 
ATOM   841  C  CE   . LYS   A 1 31  ? 22.871 2.681   21.699  1.00 38.75 ?  31  LYS   A CE   1 
ATOM   842  N  NZ   . LYS   A 1 31  ? 21.641 3.289   21.123  1.00 40.20 ?  31  LYS   A NZ   1 
ATOM   843  H  H    . LYS   A 1 31  ? 20.755 -0.748  18.166  1.00 25.27 ?  31  LYS   A H    1 
ATOM   844  H  HA   . LYS   A 1 31  ? 22.848 -0.634  17.887  1.00 26.18 ?  31  LYS   A HA   1 
ATOM   845  H  HB2  . LYS   A 1 31  ? 23.093 -1.356  20.577  1.00 31.58 ?  31  LYS   A HB2  1 
ATOM   846  H  HB3  . LYS   A 1 31  ? 24.118 -0.479  19.747  1.00 31.58 ?  31  LYS   A HB3  1 
ATOM   847  H  HG2  . LYS   A 1 31  ? 21.943 0.939   19.658  1.00 37.93 ?  31  LYS   A HG2  1 
ATOM   848  H  HG3  . LYS   A 1 31  ? 21.944 0.370   21.144  1.00 37.93 ?  31  LYS   A HG3  1 
ATOM   849  H  HD2  . LYS   A 1 31  ? 24.237 1.227   21.250  1.00 42.92 ?  31  LYS   A HD2  1 
ATOM   850  H  HD3  . LYS   A 1 31  ? 23.823 2.100   19.985  1.00 42.92 ?  31  LYS   A HD3  1 
ATOM   851  H  HE2  . LYS   A 1 31  ? 22.630 2.253   22.535  1.00 46.47 ?  31  LYS   A HE2  1 
ATOM   852  H  HE3  . LYS   A 1 31  ? 23.511 3.391   21.861  1.00 46.47 ?  31  LYS   A HE3  1 
ATOM   853  H  HZ1  . LYS   A 1 31  ? 21.319 3.906   21.679  1.00 48.22 ?  31  LYS   A HZ1  1 
ATOM   854  H  HZ2  . LYS   A 1 31  ? 21.827 3.672   20.342  1.00 48.22 ?  31  LYS   A HZ2  1 
ATOM   855  H  HZ3  . LYS   A 1 31  ? 21.020 2.663   20.999  1.00 48.22 ?  31  LYS   A HZ3  1 
ATOM   856  N  N    . PRO   A 1 32  ? 22.900 -3.171  17.104  1.00 17.36 ?  32  PRO   A N    1 
ATOM   857  C  CA   . PRO   A 1 32  ? 23.375 -4.514  16.773  1.00 17.45 ?  32  PRO   A CA   1 
ATOM   858  C  C    . PRO   A 1 32  ? 24.876 -4.526  16.561  1.00 17.22 ?  32  PRO   A C    1 
ATOM   859  O  O    . PRO   A 1 32  ? 25.517 -3.494  16.348  1.00 17.32 ?  32  PRO   A O    1 
ATOM   860  C  CB   . PRO   A 1 32  ? 22.648 -4.820  15.460  1.00 17.30 ?  32  PRO   A CB   1 
ATOM   861  C  CG   . PRO   A 1 32  ? 22.482 -3.475  14.829  1.00 16.20 ?  32  PRO   A CG   1 
ATOM   862  C  CD   . PRO   A 1 32  ? 22.188 -2.552  15.976  1.00 16.51 ?  32  PRO   A CD   1 
ATOM   863  H  HA   . PRO   A 1 32  ? 23.120 -5.155  17.457  1.00 20.92 ?  32  PRO   A HA   1 
ATOM   864  H  HB2  . PRO   A 1 32  ? 23.197 -5.404  14.908  1.00 20.73 ?  32  PRO   A HB2  1 
ATOM   865  H  HB3  . PRO   A 1 32  ? 21.788 -5.232  15.644  1.00 20.73 ?  32  PRO   A HB3  1 
ATOM   866  H  HG2  . PRO   A 1 32  ? 23.303 -3.229  14.378  1.00 19.42 ?  32  PRO   A HG2  1 
ATOM   867  H  HG3  . PRO   A 1 32  ? 21.740 -3.507  14.202  1.00 19.42 ?  32  PRO   A HG3  1 
ATOM   868  H  HD2  . PRO   A 1 32  ? 22.545 -1.671  15.783  1.00 19.79 ?  32  PRO   A HD2  1 
ATOM   869  H  HD3  . PRO   A 1 32  ? 21.236 -2.524  16.143  1.00 19.79 ?  32  PRO   A HD3  1 
ATOM   870  N  N    . THR   A 1 33  ? 25.431 -5.735  16.596  1.00 17.04 ?  33  THR   A N    1 
ATOM   871  C  CA   . THR   A 1 33  ? 26.843 -5.897  16.280  1.00 17.23 ?  33  THR   A CA   1 
ATOM   872  C  C    . THR   A 1 33  ? 27.141 -5.436  14.860  1.00 15.66 ?  33  THR   A C    1 
ATOM   873  O  O    . THR   A 1 33  ? 28.173 -4.795  14.613  1.00 16.01 ?  33  THR   A O    1 
ATOM   874  C  CB   . THR   A 1 33  ? 27.247 -7.356  16.476  1.00 18.92 ?  33  THR   A CB   1 
ATOM   875  O  OG1  . THR   A 1 33  ? 26.918 -7.759  17.809  1.00 20.64 ?  33  THR   A OG1  1 
ATOM   876  C  CG2  . THR   A 1 33  ? 28.737 -7.536  16.256  1.00 19.70 ?  33  THR   A CG2  1 
ATOM   877  H  H    . THR   A 1 33  ? 25.016 -6.464  16.789  1.00 20.43 ?  33  THR   A H    1 
ATOM   878  H  HA   . THR   A 1 33  ? 27.367 -5.358  16.891  1.00 20.66 ?  33  THR   A HA   1 
ATOM   879  H  HB   . THR   A 1 33  ? 26.769 -7.920  15.845  1.00 22.69 ?  33  THR   A HB   1 
ATOM   880  H  HG1  . THR   A 1 33  ? 27.330 -7.285  18.370  1.00 24.75 ?  33  THR   A HG1  1 
ATOM   881  H  HG21 . THR   A 1 33  ? 29.009 -8.424  16.537  1.00 23.62 ?  33  THR   A HG21 1 
ATOM   882  H  HG22 . THR   A 1 33  ? 28.950 -7.422  15.319  1.00 23.62 ?  33  THR   A HG22 1 
ATOM   883  H  HG23 . THR   A 1 33  ? 29.227 -6.880  16.776  1.00 23.62 ?  33  THR   A HG23 1 
ATOM   884  N  N    . VAL   A 1 34  ? 26.249 -5.746  13.918  1.00 14.00 ?  34  VAL   A N    1 
ATOM   885  C  CA   . VAL   A 1 34  ? 26.443 -5.426  12.508  1.00 12.83 ?  34  VAL   A CA   1 
ATOM   886  C  C    . VAL   A 1 34  ? 25.147 -4.864  11.937  1.00 12.06 ?  34  VAL   A C    1 
ATOM   887  O  O    . VAL   A 1 34  ? 24.105 -5.531  11.976  1.00 12.90 ?  34  VAL   A O    1 
ATOM   888  C  CB   . VAL   A 1 34  ? 26.882 -6.645  11.675  1.00 13.53 ?  34  VAL   A CB   1 
ATOM   889  C  CG1  . VAL   A 1 34  ? 27.058 -6.250  10.212  1.00 13.99 ?  34  VAL   A CG1  1 
ATOM   890  C  CG2  . VAL   A 1 34  ? 28.162 -7.257  12.234  1.00 14.87 ?  34  VAL   A CG2  1 
ATOM   891  H  H    . VAL   A 1 34  ? 25.506 -6.152  14.078  1.00 16.78 ?  34  VAL   A H    1 
ATOM   892  H  HA   . VAL   A 1 34  ? 27.129 -4.740  12.428  1.00 15.38 ?  34  VAL   A HA   1 
ATOM   893  H  HB   . VAL   A 1 34  ? 26.186 -7.317  11.725  1.00 16.21 ?  34  VAL   A HB   1 
ATOM   894  H  HG11 . VAL   A 1 34  ? 27.552 -6.949  9.759   1.00 16.76 ?  34  VAL   A HG11 1 
ATOM   895  H  HG12 . VAL   A 1 34  ? 26.184 -6.146  9.805   1.00 16.76 ?  34  VAL   A HG12 1 
ATOM   896  H  HG13 . VAL   A 1 34  ? 27.548 -5.415  10.168  1.00 16.76 ?  34  VAL   A HG13 1 
ATOM   897  H  HG21 . VAL   A 1 34  ? 28.425 -8.002  11.672  1.00 17.82 ?  34  VAL   A HG21 1 
ATOM   898  H  HG22 . VAL   A 1 34  ? 28.860 -6.583  12.237  1.00 17.82 ?  34  VAL   A HG22 1 
ATOM   899  H  HG23 . VAL   A 1 34  ? 27.999 -7.567  13.139  1.00 17.82 ?  34  VAL   A HG23 1 
ATOM   900  N  N    . VAL   A 1 35  ? 25.214 -3.652  11.386  1.00 11.51 ?  35  VAL   A N    1 
ATOM   901  C  CA   . VAL   A 1 35  ? 24.185 -3.138  10.494  1.00 10.80 ?  35  VAL   A CA   1 
ATOM   902  C  C    . VAL   A 1 35  ? 24.743 -3.147  9.080   1.00 10.56 ?  35  VAL   A C    1 
ATOM   903  O  O    . VAL   A 1 35  ? 25.889 -2.743  8.851   1.00 11.25 ?  35  VAL   A O    1 
ATOM   904  C  CB   . VAL   A 1 35  ? 23.660 -1.745  10.903  1.00 11.67 ?  35  VAL   A CB   1 
ATOM   905  C  CG1  . VAL   A 1 35  ? 24.741 -0.664  10.788  1.00 12.35 ?  35  VAL   A CG1  1 
ATOM   906  C  CG2  . VAL   A 1 35  ? 22.433 -1.388  10.067  1.00 12.41 ?  35  VAL   A CG2  1 
ATOM   907  H  H    . VAL   A 1 35  ? 25.857 -3.098  11.516  1.00 13.79 ?  35  VAL   A H    1 
ATOM   908  H  HA   . VAL   A 1 35  ? 23.426 -3.748  10.511  1.00 12.94 ?  35  VAL   A HA   1 
ATOM   909  H  HB   . VAL   A 1 35  ? 23.372 -1.780  11.825  1.00 13.99 ?  35  VAL   A HB   1 
ATOM   910  H  HG11 . VAL   A 1 35  ? 24.398 0.169   11.149  1.00 14.79 ?  35  VAL   A HG11 1 
ATOM   911  H  HG12 . VAL   A 1 35  ? 25.521 -0.945  11.292  1.00 14.79 ?  35  VAL   A HG12 1 
ATOM   912  H  HG13 . VAL   A 1 35  ? 24.980 -0.544  9.854   1.00 14.79 ?  35  VAL   A HG13 1 
ATOM   913  H  HG21 . VAL   A 1 35  ? 22.070 -0.547  10.375  1.00 14.87 ?  35  VAL   A HG21 1 
ATOM   914  H  HG22 . VAL   A 1 35  ? 22.695 -1.313  9.132   1.00 14.87 ?  35  VAL   A HG22 1 
ATOM   915  H  HG23 . VAL   A 1 35  ? 21.769 -2.092  10.161  1.00 14.87 ?  35  VAL   A HG23 1 
ATOM   916  N  N    . VAL   A 1 36  ? 23.931 -3.609  8.130   1.00 9.95  ?  36  VAL   A N    1 
ATOM   917  C  CA   . VAL   A 1 36  ? 24.308 -3.618  6.725   1.00 9.75  ?  36  VAL   A CA   1 
ATOM   918  C  C    . VAL   A 1 36  ? 23.852 -2.327  6.060   1.00 9.81  ?  36  VAL   A C    1 
ATOM   919  O  O    . VAL   A 1 36  ? 22.689 -1.925  6.190   1.00 10.43 ?  36  VAL   A O    1 
ATOM   920  C  CB   . VAL   A 1 36  ? 23.704 -4.833  6.004   1.00 9.67  ?  36  VAL   A CB   1 
ATOM   921  C  CG1  . VAL   A 1 36  ? 23.957 -4.761  4.516   1.00 10.34 ?  36  VAL   A CG1  1 
ATOM   922  C  CG2  . VAL   A 1 36  ? 24.250 -6.127  6.588   1.00 10.80 ?  36  VAL   A CG2  1 
ATOM   923  H  H    . VAL   A 1 36  ? 23.143 -3.934  8.277   1.00 11.91 ?  36  VAL   A H    1 
ATOM   924  H  HA   . VAL   A 1 36  ? 25.277 -3.680  6.653   1.00 11.68 ?  36  VAL   A HA   1 
ATOM   925  H  HB   . VAL   A 1 36  ? 22.745 -4.826  6.136   1.00 11.58 ?  36  VAL   A HB   1 
ATOM   926  H  HG11 . VAL   A 1 36  ? 23.812 -5.636  4.125   1.00 12.39 ?  36  VAL   A HG11 1 
ATOM   927  H  HG12 . VAL   A 1 36  ? 23.342 -4.120  4.115   1.00 12.39 ?  36  VAL   A HG12 1 
ATOM   928  H  HG13 . VAL   A 1 36  ? 24.872 -4.478  4.360   1.00 12.39 ?  36  VAL   A HG13 1 
ATOM   929  H  HG21 . VAL   A 1 36  ? 23.870 -6.882  6.106   1.00 12.94 ?  36  VAL   A HG21 1 
ATOM   930  H  HG22 . VAL   A 1 36  ? 25.217 -6.137  6.500   1.00 12.94 ?  36  VAL   A HG22 1 
ATOM   931  H  HG23 . VAL   A 1 36  ? 24.005 -6.183  7.526   1.00 12.94 ?  36  VAL   A HG23 1 
ATOM   932  N  N    . ASN   A 1 37  ? 24.770 -1.695  5.328   1.00 9.33  ?  37  ASN   A N    1 
ATOM   933  C  CA   . ASN   A 1 37  ? 24.446 -0.577  4.460   1.00 9.08  ?  37  ASN   A CA   1 
ATOM   934  C  C    . ASN   A 1 37  ? 24.312 -1.052  3.025   1.00 9.11  ?  37  ASN   A C    1 
ATOM   935  O  O    . ASN   A 1 37  ? 25.093 -1.885  2.553   1.00 9.93  ?  37  ASN   A O    1 
ATOM   936  C  CB   . ASN   A 1 37  ? 25.530 0.495   4.539   1.00 9.49  ?  37  ASN   A CB   1 
ATOM   937  C  CG   . ASN   A 1 37  ? 25.210 1.697   3.690   1.00 9.69  ?  37  ASN   A CG   1 
ATOM   938  O  OD1  . ASN   A 1 37  ? 24.036 2.033   3.496   1.00 10.30 ?  37  ASN   A OD1  1 
ATOM   939  N  ND2  . ASN   A 1 37  ? 26.246 2.343   3.167   1.00 10.10 ?  37  ASN   A ND2  1 
ATOM   940  H  H    . ASN   A 1 37  ? 25.610 -1.897  5.333   1.00 11.17 ?  37  ASN   A H    1 
ATOM   941  H  HA   . ASN   A 1 37  ? 23.608 -0.182  4.741   1.00 10.87 ?  37  ASN   A HA   1 
ATOM   942  H  HB2  . ASN   A 1 37  ? 25.619 0.793   5.461   1.00 11.36 ?  37  ASN   A HB2  1 
ATOM   943  H  HB3  . ASN   A 1 37  ? 26.374 0.122   4.232   1.00 11.36 ?  37  ASN   A HB3  1 
ATOM   944  H  HD21 . ASN   A 1 37  ? 26.115 3.034   2.670   1.00 12.09 ?  37  ASN   A HD21 1 
ATOM   945  H  HD22 . ASN   A 1 37  ? 27.044 2.080   3.322   1.00 12.09 ?  37  ASN   A HD22 1 
ATOM   946  N  N    . ALA   A 1 38  ? 23.297 -0.519  2.339   1.00 9.52  ?  38  ALA   A N    1 
ATOM   947  C  CA   . ALA   A 1 38  ? 23.118 -0.686  0.898   1.00 9.90  ?  38  ALA   A CA   1 
ATOM   948  C  C    . ALA   A 1 38  ? 24.016 0.325   0.182   1.00 9.68  ?  38  ALA   A C    1 
ATOM   949  O  O    . ALA   A 1 38  ? 23.587 1.401   -0.246  1.00 10.19 ?  38  ALA   A O    1 
ATOM   950  C  CB   . ALA   A 1 38  ? 21.653 -0.485  0.532   1.00 11.29 ?  38  ALA   A CB   1 
ATOM   951  H  H    . ALA   A 1 38  ? 22.695 -0.027  2.705   1.00 11.40 ?  38  ALA   A H    1 
ATOM   952  H  HA   . ALA   A 1 38  ? 23.385 -1.580  0.638   1.00 11.86 ?  38  ALA   A HA   1 
ATOM   953  H  HB1  . ALA   A 1 38  ? 21.523 -0.720  -0.400  1.00 13.53 ?  38  ALA   A HB1  1 
ATOM   954  H  HB2  . ALA   A 1 38  ? 21.103 -1.059  1.095   1.00 13.53 ?  38  ALA   A HB2  1 
ATOM   955  H  HB3  . ALA   A 1 38  ? 21.413 0.441   0.677   1.00 13.53 ?  38  ALA   A HB3  1 
ATOM   956  N  N    A ALA   A 1 39  ? 25.284 -0.053  0.035   0.72 9.81  ?  39  ALA   A N    1 
ATOM   957  N  N    B ALA   A 1 39  ? 25.293 -0.018  0.074   0.28 9.90  ?  39  ALA   A N    1 
ATOM   958  C  CA   A ALA   A 1 39  ? 26.336 0.824   -0.445  0.72 9.64  ?  39  ALA   A CA   1 
ATOM   959  C  CA   B ALA   A 1 39  ? 26.284 0.912   -0.440  0.28 10.15 ?  39  ALA   A CA   1 
ATOM   960  C  C    A ALA   A 1 39  ? 26.455 0.788   -1.967  0.72 9.96  ?  39  ALA   A C    1 
ATOM   961  C  C    B ALA   A 1 39  ? 26.447 0.772   -1.949  0.28 9.73  ?  39  ALA   A C    1 
ATOM   962  O  O    A ALA   A 1 39  ? 25.925 -0.096  -2.647  0.72 10.22 ?  39  ALA   A O    1 
ATOM   963  O  O    B ALA   A 1 39  ? 26.106 -0.252  -2.546  0.28 9.43  ?  39  ALA   A O    1 
ATOM   964  C  CB   A ALA   A 1 39  ? 27.664 0.428   0.204   0.72 10.40 ?  39  ALA   A CB   1 
ATOM   965  C  CB   B ALA   A 1 39  ? 27.632 0.673   0.238   0.28 10.99 ?  39  ALA   A CB   1 
ATOM   966  H  H    A ALA   A 1 39  ? 25.558 -0.849  0.226   0.72 11.75 ?  39  ALA   A H    1 
ATOM   967  H  H    B ALA   A 1 39  ? 25.608 -0.787  0.300   0.28 11.86 ?  39  ALA   A H    1 
ATOM   968  H  HA   A ALA   A 1 39  ? 26.125 1.734   -0.179  0.72 11.55 ?  39  ALA   A HA   1 
ATOM   969  H  HA   B ALA   A 1 39  ? 26.000 1.818   -0.241  0.28 12.16 ?  39  ALA   A HA   1 
ATOM   970  H  HB1  A ALA   A 1 39  ? 28.357 1.026   -0.119  0.72 12.46 ?  39  ALA   A HB1  1 
ATOM   971  H  HB1  B ALA   A 1 39  ? 28.277 1.302   -0.120  0.28 13.17 ?  39  ALA   A HB1  1 
ATOM   972  H  HB2  A ALA   A 1 39  ? 27.581 0.520   1.172   0.72 12.46 ?  39  ALA   A HB2  1 
ATOM   973  H  HB2  B ALA   A 1 39  ? 27.531 0.808   1.194   0.28 13.17 ?  39  ALA   A HB2  1 
ATOM   974  H  HB3  A ALA   A 1 39  ? 27.871 -0.484  -0.026  0.72 12.46 ?  39  ALA   A HB3  1 
ATOM   975  H  HB3  B ALA   A 1 39  ? 27.917 -0.235  0.059   0.28 13.17 ?  39  ALA   A HB3  1 
ATOM   976  N  N    A ASN   A 1 40  ? 27.180 1.772   -2.498  0.72 10.32 ?  40  ASN   A N    1 
ATOM   977  N  N    B ASN   A 1 40  ? 26.985 1.825   -2.560  0.28 9.73  ?  40  ASN   A N    1 
ATOM   978  C  CA   A ASN   A 1 40  ? 27.729 1.720   -3.846  0.72 10.23 ?  40  ASN   A CA   1 
ATOM   979  C  CA   B ASN   A 1 40  ? 27.472 1.775   -3.930  0.28 10.02 ?  40  ASN   A CA   1 
ATOM   980  C  C    A ASN   A 1 40  ? 29.253 1.618   -3.767  0.72 9.37  ?  40  ASN   A C    1 
ATOM   981  C  C    B ASN   A 1 40  ? 28.992 1.625   -3.921  0.28 9.72  ?  40  ASN   A C    1 
ATOM   982  O  O    A ASN   A 1 40  ? 29.850 1.730   -2.693  0.72 9.47  ?  40  ASN   A O    1 
ATOM   983  O  O    B ASN   A 1 40  ? 29.639 1.658   -2.872  0.28 9.94  ?  40  ASN   A O    1 
ATOM   984  C  CB   A ASN   A 1 40  ? 27.249 2.895   -4.718  0.72 10.96 ?  40  ASN   A CB   1 
ATOM   985  C  CB   B ASN   A 1 40  ? 27.045 3.026   -4.707  0.28 10.78 ?  40  ASN   A CB   1 
ATOM   986  C  CG   A ASN   A 1 40  ? 27.602 4.258   -4.147  0.72 11.72 ?  40  ASN   A CG   1 
ATOM   987  C  CG   B ASN   A 1 40  ? 27.491 4.311   -4.041  0.28 11.55 ?  40  ASN   A CG   1 
ATOM   988  O  OD1  A ASN   A 1 40  ? 28.756 4.512   -3.791  0.72 12.79 ?  40  ASN   A OD1  1 
ATOM   989  O  OD1  B ASN   A 1 40  ? 28.689 4.586   -3.939  0.28 11.84 ?  40  ASN   A OD1  1 
ATOM   990  N  ND2  A ASN   A 1 40  ? 26.599 5.147   -4.067  0.72 11.78 ?  40  ASN   A ND2  1 
ATOM   991  N  ND2  B ASN   A 1 40  ? 26.527 5.109   -3.588  0.28 12.06 ?  40  ASN   A ND2  1 
ATOM   992  H  H    A ASN   A 1 40  ? 27.382 2.487   -2.074  0.72 12.36 ?  40  ASN   A H    1 
ATOM   993  H  H    B ASN   A 1 40  ? 27.086 2.594   -2.188  0.28 11.66 ?  40  ASN   A H    1 
ATOM   994  H  HA   A ASN   A 1 40  ? 27.418 0.904   -4.267  0.72 12.25 ?  40  ASN   A HA   1 
ATOM   995  H  HA   B ASN   A 1 40  ? 27.089 1.000   -4.377  0.28 12.00 ?  40  ASN   A HA   1 
ATOM   996  H  HB2  A ASN   A 1 40  ? 27.659 2.820   -5.595  0.72 13.13 ?  40  ASN   A HB2  1 
ATOM   997  H  HB2  B ASN   A 1 40  ? 27.435 2.996   -5.592  0.28 12.92 ?  40  ASN   A HB2  1 
ATOM   998  H  HB3  A ASN   A 1 40  ? 26.285 2.846   -4.800  0.72 13.13 ?  40  ASN   A HB3  1 
ATOM   999  H  HB3  B ASN   A 1 40  ? 26.077 3.034   -4.773  0.28 12.92 ?  40  ASN   A HB3  1 
ATOM   1000 H  HD21 A ASN   A 1 40  ? 26.742 5.936   -3.753  0.72 14.12 ?  40  ASN   A HD21 1 
ATOM   1001 H  HD21 B ASN   A 1 40  ? 26.729 5.849   -3.201  0.28 14.45 ?  40  ASN   A HD21 1 
ATOM   1002 H  HD22 A ASN   A 1 40  ? 25.805 4.926   -4.319  0.72 14.12 ?  40  ASN   A HD22 1 
ATOM   1003 H  HD22 B ASN   A 1 40  ? 25.700 4.887   -3.685  0.28 14.45 ?  40  ASN   A HD22 1 
ATOM   1004 N  N    A VAL   A 1 41  ? 29.878 1.343   -4.916  0.72 9.71  ?  41  VAL   A N    1 
ATOM   1005 N  N    B VAL   A 1 41  ? 29.567 1.452   -5.114  0.28 9.56  ?  41  VAL   A N    1 
ATOM   1006 C  CA   A VAL   A 1 41  ? 31.307 1.036   -4.929  0.72 10.27 ?  41  VAL   A CA   1 
ATOM   1007 C  CA   B VAL   A 1 41  ? 30.987 1.117   -5.201  0.28 10.06 ?  41  VAL   A CA   1 
ATOM   1008 C  C    A VAL   A 1 41  ? 32.153 2.197   -4.447  0.72 10.39 ?  41  VAL   A C    1 
ATOM   1009 C  C    B VAL   A 1 41  ? 31.895 2.236   -4.704  0.28 10.17 ?  41  VAL   A C    1 
ATOM   1010 O  O    A VAL   A 1 41  ? 33.282 1.985   -3.990  0.72 10.61 ?  41  VAL   A O    1 
ATOM   1011 O  O    B VAL   A 1 41  ? 33.062 1.976   -4.384  0.28 9.88  ?  41  VAL   A O    1 
ATOM   1012 C  CB   A VAL   A 1 41  ? 31.802 0.547   -6.312  0.72 10.74 ?  41  VAL   A CB   1 
ATOM   1013 C  CB   B VAL   A 1 41  ? 31.390 0.691   -6.626  0.28 10.63 ?  41  VAL   A CB   1 
ATOM   1014 C  CG1  A VAL   A 1 41  ? 31.103 -0.745  -6.719  0.72 11.50 ?  41  VAL   A CG1  1 
ATOM   1015 C  CG1  B VAL   A 1 41  ? 30.723 -0.625  -6.996  0.28 11.20 ?  41  VAL   A CG1  1 
ATOM   1016 C  CG2  A VAL   A 1 41  ? 31.656 1.622   -7.383  0.72 10.69 ?  41  VAL   A CG2  1 
ATOM   1017 C  CG2  B VAL   A 1 41  ? 31.051 1.779   -7.633  0.28 11.04 ?  41  VAL   A CG2  1 
ATOM   1018 H  H    A VAL   A 1 41  ? 29.504 1.316   -5.685  0.72 11.63 ?  41  VAL   A H    1 
ATOM   1019 H  H    B VAL   A 1 41  ? 29.160 1.517   -5.870  0.28 11.44 ?  41  VAL   A H    1 
ATOM   1020 H  HA   A VAL   A 1 41  ? 31.470 0.309   -4.308  0.72 12.30 ?  41  VAL   A HA   1 
ATOM   1021 H  HA   B VAL   A 1 41  ? 31.137 0.347   -4.630  0.28 12.06 ?  41  VAL   A HA   1 
ATOM   1022 H  HB   A VAL   A 1 41  ? 32.749 0.343   -6.245  0.72 12.87 ?  41  VAL   A HB   1 
ATOM   1023 H  HB   B VAL   A 1 41  ? 32.349 0.549   -6.651  0.28 12.74 ?  41  VAL   A HB   1 
ATOM   1024 H  HG11 A VAL   A 1 41  ? 31.440 -1.039  -7.580  0.72 13.78 ?  41  VAL   A HG11 1 
ATOM   1025 H  HG11 B VAL   A 1 41  ? 30.927 -0.834  -7.920  0.28 13.42 ?  41  VAL   A HG11 1 
ATOM   1026 H  HG12 A VAL   A 1 41  ? 31.272 -1.426  -6.048  0.72 13.78 ?  41  VAL   A HG12 1 
ATOM   1027 H  HG12 B VAL   A 1 41  ? 31.063 -1.326  -6.416  0.28 13.42 ?  41  VAL   A HG12 1 
ATOM   1028 H  HG13 A VAL   A 1 41  ? 30.145 -0.582  -6.782  0.72 13.78 ?  41  VAL   A HG13 1 
ATOM   1029 H  HG13 B VAL   A 1 41  ? 29.765 -0.540  -6.880  0.28 13.42 ?  41  VAL   A HG13 1 
ATOM   1030 H  HG21 A VAL   A 1 41  ? 31.872 1.237   -8.249  0.72 12.80 ?  41  VAL   A HG21 1 
ATOM   1031 H  HG21 B VAL   A 1 41  ? 31.398 1.522   -8.501  0.28 13.22 ?  41  VAL   A HG21 1 
ATOM   1032 H  HG22 A VAL   A 1 41  ? 30.744 1.945   -7.383  0.72 12.80 ?  41  VAL   A HG22 1 
ATOM   1033 H  HG22 B VAL   A 1 41  ? 30.087 1.880   -7.680  0.28 13.22 ?  41  VAL   A HG22 1 
ATOM   1034 H  HG23 A VAL   A 1 41  ? 32.267 2.349   -7.185  0.72 12.80 ?  41  VAL   A HG23 1 
ATOM   1035 H  HG23 B VAL   A 1 41  ? 31.458 2.610   -7.346  0.28 13.22 ?  41  VAL   A HG23 1 
ATOM   1036 N  N    A TYR   A 1 42  ? 31.646 3.427   -4.563  0.72 10.67 ?  42  TYR   A N    1 
ATOM   1037 N  N    B TYR   A 1 42  ? 31.409 3.478   -4.652  0.28 10.37 ?  42  TYR   A N    1 
ATOM   1038 C  CA   A TYR   A 1 42  ? 32.365 4.627   -4.149  0.72 10.88 ?  42  TYR   A CA   1 
ATOM   1039 C  CA   B TYR   A 1 42  ? 32.221 4.618   -4.231  0.28 10.83 ?  42  TYR   A CA   1 
ATOM   1040 C  C    A TYR   A 1 42  ? 32.088 4.996   -2.704  0.72 10.62 ?  42  TYR   A C    1 
ATOM   1041 C  C    B TYR   A 1 42  ? 32.015 5.004   -2.771  0.28 10.63 ?  42  TYR   A C    1 
ATOM   1042 O  O    A TYR   A 1 42  ? 32.657 5.977   -2.201  0.72 11.35 ?  42  TYR   A O    1 
ATOM   1043 O  O    B TYR   A 1 42  ? 32.588 6.002   -2.318  0.28 10.89 ?  42  TYR   A O    1 
ATOM   1044 C  CB   A TYR   A 1 42  ? 32.000 5.804   -5.070  0.72 11.46 ?  42  TYR   A CB   1 
ATOM   1045 C  CB   B TYR   A 1 42  ? 31.925 5.831   -5.116  0.28 11.45 ?  42  TYR   A CB   1 
ATOM   1046 C  CG   A TYR   A 1 42  ? 32.214 5.486   -6.533  0.72 12.17 ?  42  TYR   A CG   1 
ATOM   1047 C  CG   B TYR   A 1 42  ? 32.051 5.547   -6.592  0.28 12.00 ?  42  TYR   A CG   1 
ATOM   1048 C  CD1  A TYR   A 1 42  ? 33.487 5.287   -7.039  0.72 12.93 ?  42  TYR   A CD1  1 
ATOM   1049 C  CD1  B TYR   A 1 42  ? 33.291 5.334   -7.175  0.28 12.16 ?  42  TYR   A CD1  1 
ATOM   1050 C  CD2  A TYR   A 1 42  ? 31.139 5.339   -7.400  0.72 13.45 ?  42  TYR   A CD2  1 
ATOM   1051 C  CD2  B TYR   A 1 42  ? 30.927 5.488   -7.404  0.28 12.74 ?  42  TYR   A CD2  1 
ATOM   1052 C  CE1  A TYR   A 1 42  ? 33.690 4.972   -8.371  0.72 13.39 ?  42  TYR   A CE1  1 
ATOM   1053 C  CE1  B TYR   A 1 42  ? 33.410 5.068   -8.525  0.28 12.49 ?  42  TYR   A CE1  1 
ATOM   1054 C  CE2  A TYR   A 1 42  ? 31.335 5.032   -8.736  0.72 14.41 ?  42  TYR   A CE2  1 
ATOM   1055 C  CE2  B TYR   A 1 42  ? 31.035 5.229   -8.753  0.28 13.11 ?  42  TYR   A CE2  1 
ATOM   1056 C  CZ   A TYR   A 1 42  ? 32.613 4.844   -9.214  0.72 14.14 ?  42  TYR   A CZ   1 
ATOM   1057 C  CZ   B TYR   A 1 42  ? 32.277 5.018   -9.310  0.28 13.00 ?  42  TYR   A CZ   1 
ATOM   1058 O  OH   A TYR   A 1 42  ? 32.811 4.528   -10.539 0.72 15.37 ?  42  TYR   A OH   1 
ATOM   1059 O  OH   B TYR   A 1 42  ? 32.385 4.759   -10.655 0.28 13.51 ?  42  TYR   A OH   1 
ATOM   1060 H  H    A TYR   A 1 42  ? 30.870 3.594   -4.889  0.72 12.78 ?  42  TYR   A H    1 
ATOM   1061 H  H    B TYR   A 1 42  ? 30.602 3.687   -4.886  0.28 12.42 ?  42  TYR   A H    1 
ATOM   1062 H  HA   A TYR   A 1 42  ? 33.318 4.476   -4.235  0.72 13.03 ?  42  TYR   A HA   1 
ATOM   1063 H  HA   B TYR   A 1 42  ? 33.152 4.386   -4.355  0.28 12.97 ?  42  TYR   A HA   1 
ATOM   1064 H  HB2  A TYR   A 1 42  ? 31.062 6.026   -4.946  0.72 13.73 ?  42  TYR   A HB2  1 
ATOM   1065 H  HB2  B TYR   A 1 42  ? 31.017 6.130   -4.946  0.28 13.72 ?  42  TYR   A HB2  1 
ATOM   1066 H  HB3  A TYR   A 1 42  ? 32.552 6.570   -4.846  0.72 13.73 ?  42  TYR   A HB3  1 
ATOM   1067 H  HB3  B TYR   A 1 42  ? 32.550 6.537   -4.892  0.28 13.72 ?  42  TYR   A HB3  1 
ATOM   1068 H  HD1  A TYR   A 1 42  ? 34.221 5.374   -6.474  0.72 15.50 ?  42  TYR   A HD1  1 
ATOM   1069 H  HD1  B TYR   A 1 42  ? 34.055 5.368   -6.645  0.28 14.57 ?  42  TYR   A HD1  1 
ATOM   1070 H  HD2  A TYR   A 1 42  ? 30.273 5.468   -7.082  0.72 16.11 ?  42  TYR   A HD2  1 
ATOM   1071 H  HD2  B TYR   A 1 42  ? 30.086 5.630   -7.033  0.28 15.26 ?  42  TYR   A HD2  1 
ATOM   1072 H  HE1  A TYR   A 1 42  ? 34.555 4.854   -8.697  0.72 16.04 ?  42  TYR   A HE1  1 
ATOM   1073 H  HE1  B TYR   A 1 42  ? 34.249 4.927   -8.902  0.28 14.96 ?  42  TYR   A HE1  1 
ATOM   1074 H  HE2  A TYR   A 1 42  ? 30.604 4.948   -9.308  0.72 17.27 ?  42  TYR   A HE2  1 
ATOM   1075 H  HE2  B TYR   A 1 42  ? 30.275 5.192   -9.286  0.28 15.71 ?  42  TYR   A HE2  1 
ATOM   1076 H  HH   A TYR   A 1 42  ? 33.631 4.433   -10.694 0.72 18.42 ?  42  TYR   A HH   1 
ATOM   1077 H  HH   B TYR   A 1 42  ? 31.627 4.755   -11.011 0.28 16.19 ?  42  TYR   A HH   1 
ATOM   1078 N  N    . LEU   A 1 43  ? 31.211 4.242   -2.035  1.00 10.41 ?  43  LEU   A N    1 
ATOM   1079 C  CA   . LEU   A 1 43  ? 30.778 4.584   -0.684  1.00 10.22 ?  43  LEU   A CA   1 
ATOM   1080 C  C    . LEU   A 1 43  ? 30.293 6.029   -0.595  1.00 10.35 ?  43  LEU   A C    1 
ATOM   1081 O  O    . LEU   A 1 43  ? 30.549 6.733   0.383   1.00 11.48 ?  43  LEU   A O    1 
ATOM   1082 C  CB   . LEU   A 1 43  ? 31.828 4.279   0.380   1.00 10.51 ?  43  LEU   A CB   1 
ATOM   1083 C  CG   . LEU   A 1 43  ? 32.309 2.827   0.474   1.00 10.94 ?  43  LEU   A CG   1 
ATOM   1084 C  CD1  . LEU   A 1 43  ? 33.347 2.705   1.582   1.00 11.92 ?  43  LEU   A CD1  1 
ATOM   1085 C  CD2  . LEU   A 1 43  ? 31.157 1.848   0.697   1.00 11.27 ?  43  LEU   A CD2  1 
ATOM   1086 H  H    A LEU   A 1 43  ? 30.855 3.514   -2.341  0.72 12.47 ?  43  LEU   A H    1 
ATOM   1087 H  H    B LEU   A 1 43  ? 30.882 3.489   -2.309  0.28 12.47 ?  43  LEU   A H    1 
ATOM   1088 H  HA   . LEU   A 1 43  ? 30.011 4.025   -0.475  1.00 12.24 ?  43  LEU   A HA   1 
ATOM   1089 H  HB2  . LEU   A 1 43  ? 32.605 4.831   0.214   1.00 12.59 ?  43  LEU   A HB2  1 
ATOM   1090 H  HB3  . LEU   A 1 43  ? 31.453 4.506   1.249   1.00 12.59 ?  43  LEU   A HB3  1 
ATOM   1091 H  HG   . LEU   A 1 43  ? 32.748 2.591   -0.357  1.00 13.11 ?  43  LEU   A HG   1 
ATOM   1092 H  HD11 . LEU   A 1 43  ? 33.650 1.785   1.636   1.00 14.29 ?  43  LEU   A HD11 1 
ATOM   1093 H  HD12 . LEU   A 1 43  ? 34.096 3.290   1.385   1.00 14.29 ?  43  LEU   A HD12 1 
ATOM   1094 H  HD13 . LEU   A 1 43  ? 32.941 2.967   2.427   1.00 14.29 ?  43  LEU   A HD13 1 
ATOM   1095 H  HD21 . LEU   A 1 43  ? 31.523 0.965   0.856   1.00 13.50 ?  43  LEU   A HD21 1 
ATOM   1096 H  HD22 . LEU   A 1 43  ? 30.643 2.139   1.464   1.00 13.50 ?  43  LEU   A HD22 1 
ATOM   1097 H  HD23 . LEU   A 1 43  ? 30.600 1.840   -0.096  1.00 13.50 ?  43  LEU   A HD23 1 
ATOM   1098 N  N    A LYS   A 1 44  ? 29.559 6.468   -1.617  0.72 10.42 ?  44  LYS   A N    1 
ATOM   1099 N  N    B LYS   A 1 44  ? 29.583 6.468   -1.635  0.28 10.76 ?  44  LYS   A N    1 
ATOM   1100 C  CA   A LYS   A 1 44  ? 28.930 7.788   -1.618  0.72 10.64 ?  44  LYS   A CA   1 
ATOM   1101 C  CA   B LYS   A 1 44  ? 28.907 7.761   -1.641  0.28 11.26 ?  44  LYS   A CA   1 
ATOM   1102 C  C    A LYS   A 1 44  ? 27.496 7.613   -1.135  0.72 9.90  ?  44  LYS   A C    1 
ATOM   1103 C  C    B LYS   A 1 44  ? 27.500 7.543   -1.108  0.28 10.39 ?  44  LYS   A C    1 
ATOM   1104 O  O    A LYS   A 1 44  ? 26.632 7.127   -1.869  0.72 11.24 ?  44  LYS   A O    1 
ATOM   1105 O  O    B LYS   A 1 44  ? 26.650 6.963   -1.793  0.28 10.49 ?  44  LYS   A O    1 
ATOM   1106 C  CB   A LYS   A 1 44  ? 28.999 8.428   -2.997  0.72 12.94 ?  44  LYS   A CB   1 
ATOM   1107 C  CB   B LYS   A 1 44  ? 28.877 8.349   -3.050  0.28 13.18 ?  44  LYS   A CB   1 
ATOM   1108 C  CG   A LYS   A 1 44  ? 30.400 8.856   -3.411  0.72 16.06 ?  44  LYS   A CG   1 
ATOM   1109 C  CG   B LYS   A 1 44  ? 30.195 8.955   -3.505  0.28 15.38 ?  44  LYS   A CG   1 
ATOM   1110 C  CD   A LYS   A 1 44  ? 31.083 9.744   -2.371  0.72 20.65 ?  44  LYS   A CD   1 
ATOM   1111 C  CD   B LYS   A 1 44  ? 30.740 9.947   -2.483  0.28 17.77 ?  44  LYS   A CD   1 
ATOM   1112 C  CE   A LYS   A 1 44  ? 32.418 10.262  -2.876  0.72 23.32 ?  44  LYS   A CE   1 
ATOM   1113 C  CE   B LYS   A 1 44  ? 32.031 10.579  -2.957  0.28 19.26 ?  44  LYS   A CE   1 
ATOM   1114 N  NZ   A LYS   A 1 44  ? 33.246 10.833  -1.779  0.72 24.58 ?  44  LYS   A NZ   1 
ATOM   1115 N  NZ   B LYS   A 1 44  ? 32.811 11.152  -1.826  0.28 20.37 ?  44  LYS   A NZ   1 
ATOM   1116 H  H    A LYS   A 1 44  ? 29.417 6.015   -2.338  0.72 12.48 ?  44  LYS   A H    1 
ATOM   1117 H  H    B LYS   A 1 44  ? 29.475 6.024   -2.363  0.28 12.89 ?  44  LYS   A H    1 
ATOM   1118 H  HA   A LYS   A 1 44  ? 29.382 8.358   -0.977  0.72 12.75 ?  44  LYS   A HA   1 
ATOM   1119 H  HA   B LYS   A 1 44  ? 29.352 8.372   -1.035  0.28 13.49 ?  44  LYS   A HA   1 
ATOM   1120 H  HB2  A LYS   A 1 44  ? 28.679 7.792   -3.653  0.72 15.50 ?  44  LYS   A HB2  1 
ATOM   1121 H  HB2  B LYS   A 1 44  ? 28.649 7.645   -3.678  0.28 15.80 ?  44  LYS   A HB2  1 
ATOM   1122 H  HB3  A LYS   A 1 44  ? 28.437 9.218   -3.001  0.72 15.50 ?  44  LYS   A HB3  1 
ATOM   1123 H  HB3  B LYS   A 1 44  ? 28.208 9.050   -3.089  0.28 15.80 ?  44  LYS   A HB3  1 
ATOM   1124 H  HG2  A LYS   A 1 44  ? 30.950 8.067   -3.538  0.72 19.25 ?  44  LYS   A HG2  1 
ATOM   1125 H  HG2  B LYS   A 1 44  ? 30.848 8.247   -3.624  0.28 18.44 ?  44  LYS   A HG2  1 
ATOM   1126 H  HG3  A LYS   A 1 44  ? 30.346 9.359   -4.241  0.72 19.25 ?  44  LYS   A HG3  1 
ATOM   1127 H  HG3  B LYS   A 1 44  ? 30.058 9.428   -4.343  0.28 18.44 ?  44  LYS   A HG3  1 
ATOM   1128 H  HD2  A LYS   A 1 44  ? 30.505 10.499  -2.171  0.72 24.76 ?  44  LYS   A HD2  1 
ATOM   1129 H  HD2  B LYS   A 1 44  ? 30.080 10.641  -2.329  0.28 21.30 ?  44  LYS   A HD2  1 
ATOM   1130 H  HD3  A LYS   A 1 44  ? 31.246 9.224   -1.567  0.72 24.76 ?  44  LYS   A HD3  1 
ATOM   1131 H  HD3  B LYS   A 1 44  ? 30.938 9.480   -1.654  0.28 21.30 ?  44  LYS   A HD3  1 
ATOM   1132 H  HE2  A LYS   A 1 44  ? 32.912 9.531   -3.277  0.72 27.97 ?  44  LYS   A HE2  1 
ATOM   1133 H  HE2  B LYS   A 1 44  ? 32.576 9.900   -3.389  0.28 23.10 ?  44  LYS   A HE2  1 
ATOM   1134 H  HE3  A LYS   A 1 44  ? 32.260 10.959  -3.533  0.72 27.97 ?  44  LYS   A HE3  1 
ATOM   1135 H  HE3  B LYS   A 1 44  ? 31.826 11.291  -3.577  0.28 23.10 ?  44  LYS   A HE3  1 
ATOM   1136 H  HZ1  A LYS   A 1 44  ? 34.018 11.131  -2.104  0.72 29.47 ?  44  LYS   A HZ1  1 
ATOM   1137 H  HZ1  B LYS   A 1 44  ? 33.564 11.514  -2.132  0.28 24.42 ?  44  LYS   A HZ1  1 
ATOM   1138 H  HZ2  A LYS   A 1 44  ? 32.813 11.515  -1.397  0.72 29.47 ?  44  LYS   A HZ2  1 
ATOM   1139 H  HZ2  B LYS   A 1 44  ? 32.334 11.777  -1.413  0.28 24.42 ?  44  LYS   A HZ2  1 
ATOM   1140 H  HZ3  A LYS   A 1 44  ? 33.407 10.214  -1.164  0.72 29.47 ?  44  LYS   A HZ3  1 
ATOM   1141 H  HZ3  B LYS   A 1 44  ? 33.017 10.511  -1.242  0.28 24.42 ?  44  LYS   A HZ3  1 
ATOM   1142 N  N    . HIS   A 1 45  ? 27.260 7.982   0.122   1.00 10.03 ?  45  HIS   A N    1 
ATOM   1143 C  CA   . HIS   A 1 45  ? 26.020 7.650   0.818   1.00 10.28 ?  45  HIS   A CA   1 
ATOM   1144 C  C    . HIS   A 1 45  ? 25.006 8.779   0.646   1.00 10.95 ?  45  HIS   A C    1 
ATOM   1145 O  O    . HIS   A 1 45  ? 24.718 9.546   1.563   1.00 12.74 ?  45  HIS   A O    1 
ATOM   1146 C  CB   . HIS   A 1 45  ? 26.312 7.397   2.282   1.00 10.12 ?  45  HIS   A CB   1 
ATOM   1147 C  CG   . HIS   A 1 45  ? 27.424 6.429   2.515   1.00 9.81  ?  45  HIS   A CG   1 
ATOM   1148 N  ND1  . HIS   A 1 45  ? 27.420 5.142   2.016   1.00 10.17 ?  45  HIS   A ND1  1 
ATOM   1149 C  CD2  . HIS   A 1 45  ? 28.587 6.583   3.189   1.00 10.04 ?  45  HIS   A CD2  1 
ATOM   1150 C  CE1  . HIS   A 1 45  ? 28.539 4.546   2.390   1.00 9.97  ?  45  HIS   A CE1  1 
ATOM   1151 N  NE2  . HIS   A 1 45  ? 29.263 5.396   3.101   1.00 10.18 ?  45  HIS   A NE2  1 
ATOM   1152 H  H    A HIS   A 1 45  ? 27.812 8.439   0.599   0.72 12.01 ?  45  HIS   A H    1 
ATOM   1153 H  H    B HIS   A 1 45  ? 27.802 8.471   0.580   0.28 12.01 ?  45  HIS   A H    1 
ATOM   1154 H  HA   . HIS   A 1 45  ? 25.642 6.840   0.435   1.00 12.32 ?  45  HIS   A HA   1 
ATOM   1155 H  HB2  . HIS   A 1 45  ? 26.548 8.239   2.702   1.00 12.12 ?  45  HIS   A HB2  1 
ATOM   1156 H  HB3  . HIS   A 1 45  ? 25.507 7.041   2.701   1.00 12.12 ?  45  HIS   A HB3  1 
ATOM   1157 H  HD2  . HIS   A 1 45  ? 28.876 7.353   3.629   1.00 12.02 ?  45  HIS   A HD2  1 
ATOM   1158 H  HE1  . HIS   A 1 45  ? 28.768 3.664   2.205   1.00 11.94 ?  45  HIS   A HE1  1 
ATOM   1159 H  HE2  . HIS   A 1 45  ? 30.031 5.228   3.452   1.00 12.19 ?  45  HIS   A HE2  1 
ATOM   1160 N  N    A GLY   A 1 46  ? 24.398 8.817   -0.534  0.72 11.98 ?  46  GLY   A N    1 
ATOM   1161 N  N    B GLY   A 1 46  ? 24.503 8.908   -0.579  0.28 11.34 ?  46  GLY   A N    1 
ATOM   1162 C  CA   A GLY   A 1 46  ? 23.554 9.941   -0.890  0.72 12.69 ?  46  GLY   A CA   1 
ATOM   1163 C  CA   B GLY   A 1 46  ? 23.735 10.087  -0.943  0.28 11.57 ?  46  GLY   A CA   1 
ATOM   1164 C  C    A GLY   A 1 46  ? 22.075 9.780   -0.602  0.72 12.81 ?  46  GLY   A C    1 
ATOM   1165 C  C    B GLY   A 1 46  ? 22.257 10.023  -0.613  0.28 11.47 ?  46  GLY   A C    1 
ATOM   1166 O  O    A GLY   A 1 46  ? 21.411 10.741  -0.192  0.72 13.65 ?  46  GLY   A O    1 
ATOM   1167 O  O    B GLY   A 1 46  ? 21.625 11.053  -0.357  0.28 11.99 ?  46  GLY   A O    1 
ATOM   1168 H  H    A GLY   A 1 46  ? 24.446 8.206   -1.138  0.72 14.35 ?  46  GLY   A H    1 
ATOM   1169 H  H    B GLY   A 1 46  ? 24.592 8.333   -1.212  0.28 13.58 ?  46  GLY   A H    1 
ATOM   1170 H  HA2  A GLY   A 1 46  ? 23.853 10.725  -0.405  0.72 15.20 ?  46  GLY   A HA2  1 
ATOM   1171 H  HA2  B GLY   A 1 46  ? 24.118 10.861  -0.494  0.28 13.87 ?  46  GLY   A HA2  1 
ATOM   1172 H  HA3  A GLY   A 1 46  ? 23.653 10.121  -1.837  0.72 15.20 ?  46  GLY   A HA3  1 
ATOM   1173 H  HA3  B GLY   A 1 46  ? 23.811 10.231  -1.898  0.28 13.87 ?  46  GLY   A HA3  1 
ATOM   1174 N  N    A GLY   A 1 47  ? 21.541 8.582   -0.823  0.72 12.60 ?  47  GLY   A N    1 
ATOM   1175 N  N    B GLY   A 1 47  ? 21.690 8.826   -0.642  0.28 10.99 ?  47  GLY   A N    1 
ATOM   1176 C  CA   A GLY   A 1 47  ? 20.111 8.376   -0.753  0.72 12.49 ?  47  GLY   A CA   1 
ATOM   1177 C  CA   B GLY   A 1 47  ? 20.278 8.648   -0.396  0.28 11.21 ?  47  GLY   A CA   1 
ATOM   1178 C  C    A GLY   A 1 47  ? 19.781 6.957   -0.345  0.72 11.97 ?  47  GLY   A C    1 
ATOM   1179 C  C    B GLY   A 1 47  ? 19.966 7.193   -0.119  0.28 11.34 ?  47  GLY   A C    1 
ATOM   1180 O  O    A GLY   A 1 47  ? 20.667 6.136   -0.094  0.72 11.84 ?  47  GLY   A O    1 
ATOM   1181 O  O    B GLY   A 1 47  ? 20.862 6.351   -0.024  0.28 11.61 ?  47  GLY   A O    1 
ATOM   1182 H  H    A GLY   A 1 47  ? 21.991 7.865   -1.000  0.72 15.09 ?  47  GLY   A H    1 
ATOM   1183 H  H    B GLY   A 1 47  ? 22.112 8.103   -0.808  0.28 13.16 ?  47  GLY   A H    1 
ATOM   1184 H  HA2  A GLY   A 1 47  ? 19.719 8.981   -0.105  0.72 14.97 ?  47  GLY   A HA2  1 
ATOM   1185 H  HA2  B GLY   A 1 47  ? 20.000 9.185   0.366   0.28 13.43 ?  47  GLY   A HA2  1 
ATOM   1186 H  HA3  A GLY   A 1 47  ? 19.711 8.544   -1.620  0.72 14.97 ?  47  GLY   A HA3  1 
ATOM   1187 H  HA3  B GLY   A 1 47  ? 19.774 8.936   -1.174  0.28 13.43 ?  47  GLY   A HA3  1 
ATOM   1188 N  N    A GLY   A 1 48  ? 18.486 6.665   -0.299  0.72 11.92 ?  48  GLY   A N    1 
ATOM   1189 N  N    B GLY   A 1 48  ? 18.674 6.904   0.012   0.28 11.75 ?  48  GLY   A N    1 
ATOM   1190 C  CA   A GLY   A 1 48  ? 18.070 5.353   0.132   0.72 12.35 ?  48  GLY   A CA   1 
ATOM   1191 C  CA   B GLY   A 1 48  ? 18.257 5.544   0.290   0.28 11.73 ?  48  GLY   A CA   1 
ATOM   1192 C  C    A GLY   A 1 48  ? 18.557 5.076   1.538   0.72 11.73 ?  48  GLY   A C    1 
ATOM   1193 C  C    B GLY   A 1 48  ? 18.686 5.093   1.677   0.28 11.35 ?  48  GLY   A C    1 
ATOM   1194 O  O    A GLY   A 1 48  ? 18.737 5.986   2.359   0.72 12.20 ?  48  GLY   A O    1 
ATOM   1195 O  O    B GLY   A 1 48  ? 18.766 5.881   2.626   0.28 11.80 ?  48  GLY   A O    1 
ATOM   1196 H  H    A GLY   A 1 48  ? 17.847 7.202   -0.496  0.72 14.28 ?  48  GLY   A H    1 
ATOM   1197 H  H    B GLY   A 1 48  ? 18.038 7.472   -0.052  0.28 14.08 ?  48  GLY   A H    1 
ATOM   1198 H  HA2  A GLY   A 1 48  ? 17.105 5.284   0.117   0.72 14.79 ?  48  GLY   A HA2  1 
ATOM   1199 H  HA2  B GLY   A 1 48  ? 17.294 5.482   0.224   0.28 14.05 ?  48  GLY   A HA2  1 
ATOM   1200 H  HA3  A GLY   A 1 48  ? 18.444 4.677   -0.457  0.72 14.79 ?  48  GLY   A HA3  1 
ATOM   1201 H  HA3  B GLY   A 1 48  ? 18.654 4.942   -0.361  0.28 14.05 ?  48  GLY   A HA3  1 
ATOM   1202 N  N    A VAL   A 1 49  ? 18.792 3.792   1.816   0.72 11.26 ?  49  VAL   A N    1 
ATOM   1203 N  N    B VAL   A 1 49  ? 18.961 3.791   1.790   0.28 10.80 ?  49  VAL   A N    1 
ATOM   1204 C  CA   A VAL   A 1 49  ? 19.296 3.390   3.123   0.72 11.38 ?  49  VAL   A CA   1 
ATOM   1205 C  CA   B VAL   A 1 49  ? 19.499 3.245   3.033   0.28 10.12 ?  49  VAL   A CA   1 
ATOM   1206 C  C    A VAL   A 1 49  ? 20.612 4.093   3.441   0.72 10.22 ?  49  VAL   A C    1 
ATOM   1207 C  C    B VAL   A 1 49  ? 20.778 3.974   3.425   0.28 9.43  ?  49  VAL   A C    1 
ATOM   1208 O  O    A VAL   A 1 49  ? 20.823 4.548   4.570   0.72 10.79 ?  49  VAL   A O    1 
ATOM   1209 O  O    B VAL   A 1 49  ? 20.980 4.324   4.593   0.28 9.44  ?  49  VAL   A O    1 
ATOM   1210 C  CB   A VAL   A 1 49  ? 19.426 1.854   3.183   0.72 12.10 ?  49  VAL   A CB   1 
ATOM   1211 C  CB   B VAL   A 1 49  ? 19.743 1.731   2.891   0.28 9.62  ?  49  VAL   A CB   1 
ATOM   1212 C  CG1  A VAL   A 1 49  ? 20.249 1.419   4.389   0.72 12.05 ?  49  VAL   A CG1  1 
ATOM   1213 C  CG1  B VAL   A 1 49  ? 20.602 1.223   4.044   0.28 9.46  ?  49  VAL   A CG1  1 
ATOM   1214 C  CG2  A VAL   A 1 49  ? 18.047 1.211   3.222   0.72 13.74 ?  49  VAL   A CG2  1 
ATOM   1215 C  CG2  B VAL   A 1 49  ? 18.428 0.970   2.819   0.28 9.24  ?  49  VAL   A CG2  1 
ATOM   1216 H  H    A VAL   A 1 49  ? 18.671 3.138   1.269   0.72 13.49 ?  49  VAL   A H    1 
ATOM   1217 H  H    B VAL   A 1 49  ? 18.849 3.209   1.168   0.28 12.93 ?  49  VAL   A H    1 
ATOM   1218 H  HA   A VAL   A 1 49  ? 18.658 3.648   3.801   0.72 13.64 ?  49  VAL   A HA   1 
ATOM   1219 H  HA   B VAL   A 1 49  ? 18.853 3.376   3.745   0.28 12.12 ?  49  VAL   A HA   1 
ATOM   1220 H  HB   A VAL   A 1 49  ? 19.885 1.538   2.386   0.72 14.50 ?  49  VAL   A HB   1 
ATOM   1221 H  HB   B VAL   A 1 49  ? 20.225 1.569   2.068   0.28 11.52 ?  49  VAL   A HB   1 
ATOM   1222 H  HG11 A VAL   A 1 49  ? 20.090 0.479   4.555   0.72 14.44 ?  49  VAL   A HG11 1 
ATOM   1223 H  HG11 B VAL   A 1 49  ? 20.488 0.265   4.125   0.28 11.33 ?  49  VAL   A HG11 1 
ATOM   1224 H  HG12 A VAL   A 1 49  ? 21.189 1.569   4.205   0.72 14.44 ?  49  VAL   A HG12 1 
ATOM   1225 H  HG12 B VAL   A 1 49  ? 21.534 1.427   3.861   0.28 11.33 ?  49  VAL   A HG12 1 
ATOM   1226 H  HG13 A VAL   A 1 49  ? 19.972 1.942   5.159   0.72 14.44 ?  49  VAL   A HG13 1 
ATOM   1227 H  HG13 B VAL   A 1 49  ? 20.321 1.657   4.864   0.28 11.33 ?  49  VAL   A HG13 1 
ATOM   1228 H  HG21 A VAL   A 1 49  ? 18.148 0.249   3.252   0.72 16.47 ?  49  VAL   A HG21 1 
ATOM   1229 H  HG21 B VAL   A 1 49  ? 18.616 0.027   2.687   0.28 11.07 ?  49  VAL   A HG21 1 
ATOM   1230 H  HG22 A VAL   A 1 49  ? 17.582 1.523   4.014   0.72 16.47 ?  49  VAL   A HG22 1 
ATOM   1231 H  HG22 B VAL   A 1 49  ? 17.944 1.098   3.649   0.28 11.07 ?  49  VAL   A HG22 1 
ATOM   1232 H  HG23 A VAL   A 1 49  ? 17.561 1.473   2.426   0.72 16.47 ?  49  VAL   A HG23 1 
ATOM   1233 H  HG23 B VAL   A 1 49  ? 17.909 1.311   2.075   0.28 11.07 ?  49  VAL   A HG23 1 
ATOM   1234 N  N    A ALA   A 1 50  ? 21.527 4.153   2.470   0.72 9.82  ?  50  ALA   A N    1 
ATOM   1235 N  N    B ALA   A 1 50  ? 21.678 4.174   2.459   0.28 9.11  ?  50  ALA   A N    1 
ATOM   1236 C  CA   A ALA   A 1 50  ? 22.851 4.711   2.734   0.72 9.53  ?  50  ALA   A CA   1 
ATOM   1237 C  CA   B ALA   A 1 50  ? 22.979 4.759   2.769   0.28 9.16  ?  50  ALA   A CA   1 
ATOM   1238 C  C    A ALA   A 1 50  ? 22.760 6.170   3.150   0.72 9.41  ?  50  ALA   A C    1 
ATOM   1239 C  C    B ALA   A 1 50  ? 22.841 6.215   3.189   0.28 9.28  ?  50  ALA   A C    1 
ATOM   1240 O  O    A ALA   A 1 50  ? 23.399 6.588   4.121   0.72 10.06 ?  50  ALA   A O    1 
ATOM   1241 O  O    B ALA   A 1 50  ? 23.452 6.648   4.173   0.28 9.40  ?  50  ALA   A O    1 
ATOM   1242 C  CB   A ALA   A 1 50  ? 23.724 4.576   1.493   0.72 9.32  ?  50  ALA   A CB   1 
ATOM   1243 C  CB   B ALA   A 1 50  ? 23.912 4.629   1.565   0.28 9.33  ?  50  ALA   A CB   1 
ATOM   1244 H  H    A ALA   A 1 50  ? 21.410 3.881   1.662   0.72 11.76 ?  50  ALA   A H    1 
ATOM   1245 H  H    B ALA   A 1 50  ? 21.560 3.977   1.629   0.28 10.91 ?  50  ALA   A H    1 
ATOM   1246 H  HA   A ALA   A 1 50  ? 23.270 4.220   3.458   0.72 11.41 ?  50  ALA   A HA   1 
ATOM   1247 H  HA   B ALA   A 1 50  ? 23.374 4.277   3.507   0.28 10.97 ?  50  ALA   A HA   1 
ATOM   1248 H  HB1  A ALA   A 1 50  ? 24.599 4.954   1.682   0.72 11.16 ?  50  ALA   A HB1  1 
ATOM   1249 H  HB1  B ALA   A 1 50  ? 24.771 5.023   1.788   0.28 11.18 ?  50  ALA   A HB1  1 
ATOM   1250 H  HB2  A ALA   A 1 50  ? 23.808 3.640   1.266   0.72 11.16 ?  50  ALA   A HB2  1 
ATOM   1251 H  HB2  B ALA   A 1 50  ? 24.025 3.689   1.352   0.28 11.18 ?  50  ALA   A HB2  1 
ATOM   1252 H  HB3  A ALA   A 1 50  ? 23.307 5.061   0.763   0.72 11.16 ?  50  ALA   A HB3  1 
ATOM   1253 H  HB3  B ALA   A 1 50  ? 23.522 5.094   0.808   0.28 11.18 ?  50  ALA   A HB3  1 
ATOM   1254 N  N    A GLY   A 1 51  ? 21.985 6.966   2.416   0.72 9.58  ?  51  GLY   A N    1 
ATOM   1255 N  N    B GLY   A 1 51  ? 22.042 6.987   2.454   0.28 9.69  ?  51  GLY   A N    1 
ATOM   1256 C  CA   A GLY   A 1 51  ? 21.828 8.356   2.798   0.72 10.14 ?  51  GLY   A CA   1 
ATOM   1257 C  CA   B GLY   A 1 51  ? 21.848 8.377   2.825   0.28 10.02 ?  51  GLY   A CA   1 
ATOM   1258 C  C    A GLY   A 1 51  ? 21.234 8.503   4.185   0.72 10.14 ?  51  GLY   A C    1 
ATOM   1259 C  C    B GLY   A 1 51  ? 21.216 8.525   4.194   0.28 10.13 ?  51  GLY   A C    1 
ATOM   1260 O  O    A GLY   A 1 51  ? 21.638 9.379   4.954   0.72 10.84 ?  51  GLY   A O    1 
ATOM   1261 O  O    B GLY   A 1 51  ? 21.574 9.423   4.961   0.28 10.41 ?  51  GLY   A O    1 
ATOM   1262 H  H    A GLY   A 1 51  ? 21.559 6.727   1.708   0.72 11.47 ?  51  GLY   A H    1 
ATOM   1263 H  H    B GLY   A 1 51  ? 21.613 6.732   1.753   0.28 11.61 ?  51  GLY   A H    1 
ATOM   1264 H  HA2  A GLY   A 1 51  ? 22.692 8.797   2.784   0.72 12.14 ?  51  GLY   A HA2  1 
ATOM   1265 H  HA2  B GLY   A 1 51  ? 22.705 8.831   2.832   0.28 12.00 ?  51  GLY   A HA2  1 
ATOM   1266 H  HA3  A GLY   A 1 51  ? 21.244 8.801   2.163   0.72 12.14 ?  51  GLY   A HA3  1 
ATOM   1267 H  HA3  B GLY   A 1 51  ? 21.276 8.809   2.172   0.28 12.00 ?  51  GLY   A HA3  1 
ATOM   1268 N  N    . ALA   A 1 52  ? 20.269 7.642   4.524   1.00 10.36 ?  52  ALA   A N    1 
ATOM   1269 C  CA   . ALA   A 1 52  ? 19.623 7.706   5.832   1.00 11.13 ?  52  ALA   A CA   1 
ATOM   1270 C  C    . ALA   A 1 52  ? 20.577 7.291   6.953   1.00 10.44 ?  52  ALA   A C    1 
ATOM   1271 O  O    . ALA   A 1 52  ? 20.659 7.957   7.991   1.00 11.32 ?  52  ALA   A O    1 
ATOM   1272 C  CB   . ALA   A 1 52  ? 18.362 6.839   5.828   1.00 12.48 ?  52  ALA   A CB   1 
ATOM   1273 H  H    A ALA   A 1 52  ? 19.979 7.011   4.014   0.72 12.41 ?  52  ALA   A H    1 
ATOM   1274 H  H    B ALA   A 1 52  ? 19.996 7.002   4.015   0.28 12.41 ?  52  ALA   A H    1 
ATOM   1275 H  HA   . ALA   A 1 52  ? 19.351 8.616   5.998   1.00 13.34 ?  52  ALA   A HA   1 
ATOM   1276 H  HB1  . ALA   A 1 52  ? 17.920 6.919   6.690   1.00 14.96 ?  52  ALA   A HB1  1 
ATOM   1277 H  HB2  . ALA   A 1 52  ? 17.766 7.151   5.127   1.00 14.96 ?  52  ALA   A HB2  1 
ATOM   1278 H  HB3  . ALA   A 1 52  ? 18.605 5.915   5.666   1.00 14.96 ?  52  ALA   A HB3  1 
ATOM   1279 N  N    . LEU   A 1 53  ? 21.304 6.186   6.771   1.00 10.04 ?  53  LEU   A N    1 
ATOM   1280 C  CA   . LEU   A 1 53  ? 22.280 5.785   7.785   1.00 10.70 ?  53  LEU   A CA   1 
ATOM   1281 C  C    . LEU   A 1 53  ? 23.328 6.869   7.982   1.00 10.08 ?  53  LEU   A C    1 
ATOM   1282 O  O    . LEU   A 1 53  ? 23.658 7.233   9.114   1.00 11.13 ?  53  LEU   A O    1 
ATOM   1283 C  CB   . LEU   A 1 53  ? 22.957 4.459   7.410   1.00 10.97 ?  53  LEU   A CB   1 
ATOM   1284 C  CG   . LEU   A 1 53  ? 22.101 3.188   7.469   1.00 11.70 ?  53  LEU   A CG   1 
ATOM   1285 C  CD1  . LEU   A 1 53  ? 22.862 2.020   6.869   1.00 12.62 ?  53  LEU   A CD1  1 
ATOM   1286 C  CD2  . LEU   A 1 53  ? 21.680 2.866   8.894   1.00 13.10 ?  53  LEU   A CD2  1 
ATOM   1287 H  H    . LEU   A 1 53  ? 21.255 5.662   6.090   1.00 12.02 ?  53  LEU   A H    1 
ATOM   1288 H  HA   . LEU   A 1 53  ? 21.822 5.661   8.629   1.00 12.82 ?  53  LEU   A HA   1 
ATOM   1289 H  HB2  . LEU   A 1 53  ? 23.289 4.533   6.501   1.00 13.15 ?  53  LEU   A HB2  1 
ATOM   1290 H  HB3  . LEU   A 1 53  ? 23.704 4.316   8.011   1.00 13.15 ?  53  LEU   A HB3  1 
ATOM   1291 H  HG   . LEU   A 1 53  ? 21.297 3.325   6.936   1.00 14.02 ?  53  LEU   A HG   1 
ATOM   1292 H  HD11 . LEU   A 1 53  ? 22.302 1.227   6.914   1.00 15.12 ?  53  LEU   A HD11 1 
ATOM   1293 H  HD12 . LEU   A 1 53  ? 23.074 2.221   5.945   1.00 15.12 ?  53  LEU   A HD12 1 
ATOM   1294 H  HD13 . LEU   A 1 53  ? 23.673 1.882   7.377   1.00 15.12 ?  53  LEU   A HD13 1 
ATOM   1295 H  HD21 . LEU   A 1 53  ? 20.941 2.236   8.867   1.00 15.70 ?  53  LEU   A HD21 1 
ATOM   1296 H  HD22 . LEU   A 1 53  ? 22.431 2.477   9.361   1.00 15.70 ?  53  LEU   A HD22 1 
ATOM   1297 H  HD23 . LEU   A 1 53  ? 21.398 3.680   9.338   1.00 15.70 ?  53  LEU   A HD23 1 
ATOM   1298 N  N    . ASN   A 1 54  ? 23.858 7.401   6.886   1.00 9.81  ?  54  ASN   A N    1 
ATOM   1299 C  CA   . ASN   A 1 54  ? 24.908 8.399   7.019   1.00 9.98  ?  54  ASN   A CA   1 
ATOM   1300 C  C    . ASN   A 1 54  ? 24.395 9.646   7.736   1.00 10.03 ?  54  ASN   A C    1 
ATOM   1301 O  O    . ASN   A 1 54  ? 25.083 10.201  8.603   1.00 10.78 ?  54  ASN   A O    1 
ATOM   1302 C  CB   . ASN   A 1 54  ? 25.473 8.759   5.654   1.00 9.93  ?  54  ASN   A CB   1 
ATOM   1303 C  CG   . ASN   A 1 54  ? 26.488 9.859   5.755   1.00 10.29 ?  54  ASN   A CG   1 
ATOM   1304 O  OD1  . ASN   A 1 54  ? 27.498 9.717   6.456   1.00 10.30 ?  54  ASN   A OD1  1 
ATOM   1305 N  ND2  . ASN   A 1 54  ? 26.230 10.972  5.088   1.00 11.07 ?  54  ASN   A ND2  1 
ATOM   1306 H  H    . ASN   A 1 54  ? 23.627 7.208   6.080   1.00 11.75 ?  54  ASN   A H    1 
ATOM   1307 H  HA   . ASN   A 1 54  ? 25.622 8.028   7.550   1.00 11.95 ?  54  ASN   A HA   1 
ATOM   1308 H  HB2  . ASN   A 1 54  ? 25.909 7.970   5.276   1.00 11.89 ?  54  ASN   A HB2  1 
ATOM   1309 H  HB3  . ASN   A 1 54  ? 24.757 9.049   5.071   1.00 11.89 ?  54  ASN   A HB3  1 
ATOM   1310 H  HD21 . ASN   A 1 54  ? 26.778 11.628  5.125   1.00 13.26 ?  54  ASN   A HD21 1 
ATOM   1311 H  HD22 . ASN   A 1 54  ? 25.510 11.033  4.619   1.00 13.26 ?  54  ASN   A HD22 1 
ATOM   1312 N  N    . LYS   A 1 55  ? 23.187 10.102  7.388   1.00 10.50 ?  55  LYS   A N    1 
ATOM   1313 C  CA   . LYS   A 1 55  ? 22.602 11.259  8.056   1.00 11.14 ?  55  LYS   A CA   1 
ATOM   1314 C  C    . LYS   A 1 55  ? 22.509 11.029  9.556   1.00 11.32 ?  55  LYS   A C    1 
ATOM   1315 O  O    . LYS   A 1 55  ? 22.789 11.934  10.352  1.00 12.12 ?  55  LYS   A O    1 
ATOM   1316 C  CB   . LYS   A 1 55  ? 21.230 11.548  7.449   1.00 11.83 ?  55  LYS   A CB   1 
ATOM   1317 C  CG   . LYS   A 1 55  ? 20.484 12.719  8.068   1.00 13.78 ?  55  LYS   A CG   1 
ATOM   1318 C  CD   . LYS   A 1 55  ? 19.158 12.945  7.338   1.00 15.26 ?  55  LYS   A CD   1 
ATOM   1319 C  CE   . LYS   A 1 55  ? 18.291 13.988  8.023   1.00 17.18 ?  55  LYS   A CE   1 
ATOM   1320 N  NZ   . LYS   A 1 55  ? 16.973 14.143  7.343   1.00 17.95 ?  55  LYS   A NZ   1 
ATOM   1321 H  H    . LYS   A 1 55  ? 22.680 9.752   6.781   1.00 12.57 ?  55  LYS   A H    1 
ATOM   1322 H  HA   . LYS   A 1 55  ? 23.166 12.030  7.905   1.00 13.34 ?  55  LYS   A HA   1 
ATOM   1323 H  HB2  . LYS   A 1 55  ? 21.340 11.745  6.508   1.00 14.17 ?  55  LYS   A HB2  1 
ATOM   1324 H  HB3  . LYS   A 1 55  ? 20.668 10.763  7.554   1.00 14.17 ?  55  LYS   A HB3  1 
ATOM   1325 H  HG2  . LYS   A 1 55  ? 20.284 12.527  8.999   1.00 16.51 ?  55  LYS   A HG2  1 
ATOM   1326 H  HG3  . LYS   A 1 55  ? 21.014 13.524  7.991   1.00 16.51 ?  55  LYS   A HG3  1 
ATOM   1327 H  HD2  . LYS   A 1 55  ? 19.341 13.249  6.434   1.00 18.29 ?  55  LYS   A HD2  1 
ATOM   1328 H  HD3  . LYS   A 1 55  ? 18.662 12.109  7.311   1.00 18.29 ?  55  LYS   A HD3  1 
ATOM   1329 H  HE2  . LYS   A 1 55  ? 18.128 13.715  8.939   1.00 20.59 ?  55  LYS   A HE2  1 
ATOM   1330 H  HE3  . LYS   A 1 55  ? 18.745 14.843  8.002   1.00 20.59 ?  55  LYS   A HE3  1 
ATOM   1331 H  HZ1  . LYS   A 1 55  ? 16.404 14.574  7.877   1.00 21.51 ?  55  LYS   A HZ1  1 
ATOM   1332 H  HZ2  . LYS   A 1 55  ? 17.069 14.611  6.591   1.00 21.51 ?  55  LYS   A HZ2  1 
ATOM   1333 H  HZ3  . LYS   A 1 55  ? 16.632 13.345  7.146   1.00 21.51 ?  55  LYS   A HZ3  1 
ATOM   1334 N  N    . ALA   A 1 56  ? 22.120 9.817   9.964   1.00 11.51 ?  56  ALA   A N    1 
ATOM   1335 C  CA   . ALA   A 1 56  ? 21.995 9.503   11.380  1.00 12.11 ?  56  ALA   A CA   1 
ATOM   1336 C  C    . ALA   A 1 56  ? 23.332 9.533   12.107  1.00 12.27 ?  56  ALA   A C    1 
ATOM   1337 O  O    . ALA   A 1 56  ? 23.348 9.726   13.325  1.00 13.57 ?  56  ALA   A O    1 
ATOM   1338 C  CB   . ALA   A 1 56  ? 21.299 8.153   11.571  1.00 13.19 ?  56  ALA   A CB   1 
ATOM   1339 H  H    . ALA   A 1 56  ? 21.925 9.169   9.438   1.00 13.79 ?  56  ALA   A H    1 
ATOM   1340 H  HA   . ALA   A 1 56  ? 21.438 10.168  11.797  1.00 14.51 ?  56  ALA   A HA   1 
ATOM   1341 H  HB1  . ALA   A 1 56  ? 21.229 7.962   12.522  1.00 15.80 ?  56  ALA   A HB1  1 
ATOM   1342 H  HB2  . ALA   A 1 56  ? 20.413 8.198   11.180  1.00 15.80 ?  56  ALA   A HB2  1 
ATOM   1343 H  HB3  . ALA   A 1 56  ? 21.818 7.458   11.135  1.00 15.80 ?  56  ALA   A HB3  1 
ATOM   1344 N  N    . THR   A 1 57  ? 24.448 9.336   11.397  1.00 11.51 ?  57  THR   A N    1 
ATOM   1345 C  CA   . THR   A 1 57  ? 25.787 9.464   11.973  1.00 11.51 ?  57  THR   A CA   1 
ATOM   1346 C  C    . THR   A 1 57  ? 26.340 10.883  11.888  1.00 11.83 ?  57  THR   A C    1 
ATOM   1347 O  O    . THR   A 1 57  ? 27.526 11.088  12.174  1.00 12.45 ?  57  THR   A O    1 
ATOM   1348 C  CB   . THR   A 1 57  ? 26.802 8.515   11.305  1.00 11.51 ?  57  THR   A CB   1 
ATOM   1349 O  OG1  . THR   A 1 57  ? 27.182 9.016   10.009  1.00 11.00 ?  57  THR   A OG1  1 
ATOM   1350 C  CG2  . THR   A 1 57  ? 26.269 7.091   11.196  1.00 11.45 ?  57  THR   A CG2  1 
ATOM   1351 H  H    . THR   A 1 57  ? 24.453 9.100   10.568  1.00 13.79 ?  57  THR   A H    1 
ATOM   1352 H  HA   . THR   A 1 57  ? 25.743 9.212   12.913  1.00 13.79 ?  57  THR   A HA   1 
ATOM   1353 H  HB   . THR   A 1 57  ? 27.602 8.474   11.864  1.00 13.79 ?  57  THR   A HB   1 
ATOM   1354 H  HG1  . THR   A 1 57  ? 26.503 9.071   9.519   1.00 13.17 ?  57  THR   A HG1  1 
ATOM   1355 H  HG21 . THR   A 1 57  ? 26.956 6.498   10.847  1.00 13.72 ?  57  THR   A HG21 1 
ATOM   1356 H  HG22 . THR   A 1 57  ? 25.992 6.767   12.068  1.00 13.72 ?  57  THR   A HG22 1 
ATOM   1357 H  HG23 . THR   A 1 57  ? 25.506 7.067   10.598  1.00 13.72 ?  57  THR   A HG23 1 
ATOM   1358 N  N    . ASN   A 1 58  ? 25.529 11.858  11.484  1.00 12.32 ?  58  ASN   A N    1 
ATOM   1359 C  CA   . ASN   A 1 58  ? 25.998 13.237  11.387  1.00 13.16 ?  58  ASN   A CA   1 
ATOM   1360 C  C    . ASN   A 1 58  ? 27.150 13.357  10.381  1.00 12.10 ?  58  ASN   A C    1 
ATOM   1361 O  O    . ASN   A 1 58  ? 28.046 14.186  10.540  1.00 12.88 ?  58  ASN   A O    1 
ATOM   1362 C  CB   . ASN   A 1 58  ? 26.371 13.766  12.787  1.00 16.01 ?  58  ASN   A CB   1 
ATOM   1363 C  CG   . ASN   A 1 58  ? 26.805 15.216  12.793  1.00 19.53 ?  58  ASN   A CG   1 
ATOM   1364 O  OD1  . ASN   A 1 58  ? 26.182 16.055  12.156  1.00 21.03 ?  58  ASN   A OD1  1 
ATOM   1365 N  ND2  . ASN   A 1 58  ? 27.873 15.521  13.540  1.00 20.65 ?  58  ASN   A ND2  1 
ATOM   1366 H  H    . ASN   A 1 58  ? 24.707 11.738  11.250  1.00 14.77 ?  58  ASN   A H    1 
ATOM   1367 H  HA   . ASN   A 1 58  ? 25.265 13.775  11.059  1.00 15.77 ?  58  ASN   A HA   1 
ATOM   1368 H  HB2  . ASN   A 1 58  ? 25.592 13.685  13.370  1.00 19.19 ?  58  ASN   A HB2  1 
ATOM   1369 H  HB3  . ASN   A 1 58  ? 27.098 13.242  13.146  1.00 19.19 ?  58  ASN   A HB3  1 
ATOM   1370 H  HD21 . ASN   A 1 58  ? 28.154 16.336  13.579  1.00 24.76 ?  58  ASN   A HD21 1 
ATOM   1371 H  HD22 . ASN   A 1 58  ? 28.276 14.906  13.978  1.00 24.76 ?  58  ASN   A HD22 1 
ATOM   1372 N  N    . ASN   A 1 59  ? 27.126 12.540  9.325   1.00 11.17 ?  59  ASN   A N    1 
ATOM   1373 C  CA   . ASN   A 1 59  ? 28.109 12.507  8.231   1.00 11.04 ?  59  ASN   A CA   1 
ATOM   1374 C  C    . ASN   A 1 59  ? 29.424 11.823  8.622   1.00 10.74 ?  59  ASN   A C    1 
ATOM   1375 O  O    . ASN   A 1 59  ? 30.342 11.777  7.797   1.00 10.84 ?  59  ASN   A O    1 
ATOM   1376 C  CB   . ASN   A 1 59  ? 28.401 13.893  7.622   1.00 11.36 ?  59  ASN   A CB   1 
ATOM   1377 C  CG   . ASN   A 1 59  ? 28.755 13.821  6.152   1.00 11.48 ?  59  ASN   A CG   1 
ATOM   1378 O  OD1  . ASN   A 1 59  ? 28.041 13.201  5.360   1.00 11.70 ?  59  ASN   A OD1  1 
ATOM   1379 N  ND2  . ASN   A 1 59  ? 29.849 14.475  5.769   1.00 11.96 ?  59  ASN   A ND2  1 
ATOM   1380 H  H    . ASN   A 1 59  ? 26.500 11.957  9.207   1.00 13.38 ?  59  ASN   A H    1 
ATOM   1381 H  HA   . ASN   A 1 59  ? 27.726 11.977  7.521   1.00 13.23 ?  59  ASN   A HA   1 
ATOM   1382 H  HB2  . ASN   A 1 59  ? 27.614 14.456  7.712   1.00 13.61 ?  59  ASN   A HB2  1 
ATOM   1383 H  HB3  . ASN   A 1 59  ? 29.149 14.298  8.088   1.00 13.61 ?  59  ASN   A HB3  1 
ATOM   1384 H  HD21 . ASN   A 1 59  ? 30.091 14.466  4.943   1.00 14.33 ?  59  ASN   A HD21 1 
ATOM   1385 H  HD22 . ASN   A 1 59  ? 30.325 14.899  6.349   1.00 14.33 ?  59  ASN   A HD22 1 
ATOM   1386 N  N    . ALA   A 1 60  ? 29.549 11.284  9.834   1.00 10.76 ?  60  ALA   A N    1 
ATOM   1387 C  CA   . ALA   A 1 60  ? 30.783 10.596  10.196  1.00 10.95 ?  60  ALA   A CA   1 
ATOM   1388 C  C    . ALA   A 1 60  ? 31.005 9.357   9.336   1.00 10.78 ?  60  ALA   A C    1 
ATOM   1389 O  O    . ALA   A 1 60  ? 32.149 9.028   9.005   1.00 11.31 ?  60  ALA   A O    1 
ATOM   1390 C  CB   . ALA   A 1 60  ? 30.768 10.241  11.679  1.00 11.56 ?  60  ALA   A CB   1 
ATOM   1391 H  H    . ALA   A 1 60  ? 28.952 11.298  10.451  1.00 12.89 ?  60  ALA   A H    1 
ATOM   1392 H  HA   . ALA   A 1 60  ? 31.533 11.198  10.042  1.00 13.12 ?  60  ALA   A HA   1 
ATOM   1393 H  HB1  . ALA   A 1 60  ? 31.595 9.788   11.904  1.00 13.85 ?  60  ALA   A HB1  1 
ATOM   1394 H  HB2  . ALA   A 1 60  ? 30.689 11.061  12.195  1.00 13.85 ?  60  ALA   A HB2  1 
ATOM   1395 H  HB3  . ALA   A 1 60  ? 30.012 9.664   11.855  1.00 13.85 ?  60  ALA   A HB3  1 
ATOM   1396 N  N    . MET   A 1 61  ? 29.928 8.667   8.953   1.00 10.39 ?  61  MET   A N    1 
ATOM   1397 C  CA   . MET   A 1 61  ? 30.066 7.526   8.053   1.00 10.09 ?  61  MET   A CA   1 
ATOM   1398 C  C    . MET   A 1 61  ? 30.701 7.947   6.731   1.00 10.29 ?  61  MET   A C    1 
ATOM   1399 O  O    . MET   A 1 61  ? 31.595 7.263   6.220   1.00 10.69 ?  61  MET   A O    1 
ATOM   1400 C  CB   . MET   A 1 61  ? 28.704 6.860   7.842   1.00 10.18 ?  61  MET   A CB   1 
ATOM   1401 C  CG   . MET   A 1 61  ? 28.717 5.694   6.867   1.00 11.09 ?  61  MET   A CG   1 
ATOM   1402 S  SD   . MET   A 1 61  ? 27.091 4.952   6.659   1.00 11.74 ?  61  MET   A SD   1 
ATOM   1403 C  CE   . MET   A 1 61  ? 26.950 4.063   8.219   1.00 13.31 ?  61  MET   A CE   1 
ATOM   1404 H  H    . MET   A 1 61  ? 29.123 8.839   9.196   1.00 12.44 ?  61  MET   A H    1 
ATOM   1405 H  HA   . MET   A 1 61  ? 30.646 6.874   8.475   1.00 12.09 ?  61  MET   A HA   1 
ATOM   1406 H  HB2  . MET   A 1 61  ? 28.387 6.526   8.694   1.00 12.19 ?  61  MET   A HB2  1 
ATOM   1407 H  HB3  . MET   A 1 61  ? 28.085 7.520   7.498   1.00 12.19 ?  61  MET   A HB3  1 
ATOM   1408 H  HG2  . MET   A 1 61  ? 29.008 5.999   5.996   1.00 13.28 ?  61  MET   A HG2  1 
ATOM   1409 H  HG3  . MET   A 1 61  ? 29.315 5.004   7.197   1.00 13.28 ?  61  MET   A HG3  1 
ATOM   1410 H  HE1  . MET   A 1 61  ? 26.110 3.582   8.238   1.00 15.95 ?  61  MET   A HE1  1 
ATOM   1411 H  HE2  . MET   A 1 61  ? 27.691 3.441   8.297   1.00 15.95 ?  61  MET   A HE2  1 
ATOM   1412 H  HE3  . MET   A 1 61  ? 26.980 4.701   8.954   1.00 15.95 ?  61  MET   A HE3  1 
ATOM   1413 N  N    . GLN   A 1 62  ? 30.262 9.080   6.169   1.00 10.17 ?  62  GLN   A N    1 
ATOM   1414 C  CA   . GLN   A 1 62  ? 30.828 9.548   4.908   1.00 10.47 ?  62  GLN   A CA   1 
ATOM   1415 C  C    . GLN   A 1 62  ? 32.299 9.923   5.055   1.00 10.45 ?  62  GLN   A C    1 
ATOM   1416 O  O    . GLN   A 1 62  ? 33.113 9.601   4.183   1.00 10.70 ?  62  GLN   A O    1 
ATOM   1417 C  CB   . GLN   A 1 62  ? 30.027 10.731  4.375   1.00 10.46 ?  62  GLN   A CB   1 
ATOM   1418 C  CG   . GLN   A 1 62  ? 30.414 11.090  2.952   1.00 10.32 ?  62  GLN   A CG   1 
ATOM   1419 C  CD   . GLN   A 1 62  ? 30.091 9.962   2.000   1.00 10.48 ?  62  GLN   A CD   1 
ATOM   1420 O  OE1  . GLN   A 1 62  ? 28.911 9.660   1.784   1.00 11.37 ?  62  GLN   A OE1  1 
ATOM   1421 N  NE2  . GLN   A 1 62  ? 31.114 9.293   1.472   1.00 11.09 ?  62  GLN   A NE2  1 
ATOM   1422 H  H    . GLN   A 1 62  ? 29.641 9.577   6.495   1.00 12.18 ?  62  GLN   A H    1 
ATOM   1423 H  HA   . GLN   A 1 62  ? 30.771 8.828   4.262   1.00 12.54 ?  62  GLN   A HA   1 
ATOM   1424 H  HB2  . GLN   A 1 62  ? 29.081 10.509  4.388   1.00 12.53 ?  62  GLN   A HB2  1 
ATOM   1425 H  HB3  . GLN   A 1 62  ? 30.192 11.506  4.937   1.00 12.53 ?  62  GLN   A HB3  1 
ATOM   1426 H  HG2  . GLN   A 1 62  ? 29.912 11.869  2.672   1.00 12.36 ?  62  GLN   A HG2  1 
ATOM   1427 H  HG3  . GLN   A 1 62  ? 31.364 11.262  2.908   1.00 12.36 ?  62  GLN   A HG3  1 
ATOM   1428 H  HE21 . GLN   A 1 62  ? 31.923 9.523   1.663   1.00 13.28 ?  62  GLN   A HE21 1 
ATOM   1429 H  HE22 . GLN   A 1 62  ? 30.971 8.639   0.933   1.00 13.28 ?  62  GLN   A HE22 1 
ATOM   1430 N  N    . VAL   A 1 63  ? 32.658 10.599  6.147   1.00 10.98 ?  63  VAL   A N    1 
ATOM   1431 C  CA   . VAL   A 1 63  ? 34.052 10.991  6.360   1.00 11.74 ?  63  VAL   A CA   1 
ATOM   1432 C  C    . VAL   A 1 63  ? 34.948 9.757   6.428   1.00 11.10 ?  63  VAL   A C    1 
ATOM   1433 O  O    . VAL   A 1 63  ? 36.002 9.685   5.776   1.00 11.72 ?  63  VAL   A O    1 
ATOM   1434 C  CB   . VAL   A 1 63  ? 34.162 11.869  7.620   1.00 13.41 ?  63  VAL   A CB   1 
ATOM   1435 C  CG1  . VAL   A 1 63  ? 35.611 12.111  7.988   1.00 15.15 ?  63  VAL   A CG1  1 
ATOM   1436 C  CG2  . VAL   A 1 63  ? 33.443 13.203  7.399   1.00 13.63 ?  63  VAL   A CG2  1 
ATOM   1437 H  H    . VAL   A 1 63  ? 32.117 10.840  6.778   1.00 13.16 ?  63  VAL   A H    1 
ATOM   1438 H  HA   . VAL   A 1 63  ? 34.337 11.524  5.603   1.00 14.07 ?  63  VAL   A HA   1 
ATOM   1439 H  HB   . VAL   A 1 63  ? 33.739 11.414  8.363   1.00 16.07 ?  63  VAL   A HB   1 
ATOM   1440 H  HG11 . VAL   A 1 63  ? 35.656 12.842  8.621   1.00 18.16 ?  63  VAL   A HG11 1 
ATOM   1441 H  HG12 . VAL   A 1 63  ? 35.979 11.305  8.384   1.00 18.16 ?  63  VAL   A HG12 1 
ATOM   1442 H  HG13 . VAL   A 1 63  ? 36.106 12.340  7.184   1.00 18.16 ?  63  VAL   A HG13 1 
ATOM   1443 H  HG21 . VAL   A 1 63  ? 33.534 13.748  8.197   1.00 16.34 ?  63  VAL   A HG21 1 
ATOM   1444 H  HG22 . VAL   A 1 63  ? 33.847 13.660  6.642   1.00 16.34 ?  63  VAL   A HG22 1 
ATOM   1445 H  HG23 . VAL   A 1 63  ? 32.507 13.032  7.219   1.00 16.34 ?  63  VAL   A HG23 1 
ATOM   1446 N  N    . GLU   A 1 64  ? 34.527 8.756   7.204   1.00 11.13 ?  64  GLU   A N    1 
ATOM   1447 C  CA   . GLU   A 1 64  ? 35.283 7.514   7.302   1.00 11.18 ?  64  GLU   A CA   1 
ATOM   1448 C  C    . GLU   A 1 64  ? 35.374 6.827   5.947   1.00 10.87 ?  64  GLU   A C    1 
ATOM   1449 O  O    . GLU   A 1 64  ? 36.422 6.278   5.576   1.00 11.36 ?  64  GLU   A O    1 
ATOM   1450 C  CB   . GLU   A 1 64  ? 34.595 6.607   8.320   1.00 11.52 ?  64  GLU   A CB   1 
ATOM   1451 C  CG   . GLU   A 1 64  ? 35.238 5.252   8.457   1.00 12.31 ?  64  GLU   A CG   1 
ATOM   1452 C  CD   . GLU   A 1 64  ? 34.358 4.260   9.189   1.00 13.00 ?  64  GLU   A CD   1 
ATOM   1453 O  OE1  . GLU   A 1 64  ? 33.119 4.354   9.053   1.00 13.74 ?  64  GLU   A OE1  1 
ATOM   1454 O  OE2  . GLU   A 1 64  ? 34.904 3.367   9.878   1.00 13.34 -1 64  GLU   A OE2  1 
ATOM   1455 H  H    . GLU   A 1 64  ? 33.804 8.768   7.670   1.00 13.33 ?  64  GLU   A H    1 
ATOM   1456 H  HA   . GLU   A 1 64  ? 36.182 7.713   7.614   1.00 13.39 ?  64  GLU   A HA   1 
ATOM   1457 H  HB2  . GLU   A 1 64  ? 34.628 7.043   9.192   1.00 13.80 ?  64  GLU   A HB2  1 
ATOM   1458 H  HB3  . GLU   A 1 64  ? 33.674 6.487   8.052   1.00 13.80 ?  64  GLU   A HB3  1 
ATOM   1459 H  HG2  . GLU   A 1 64  ? 35.425 4.890   7.572   1.00 14.75 ?  64  GLU   A HG2  1 
ATOM   1460 H  HG3  . GLU   A 1 64  ? 36.064 5.346   8.951   1.00 14.75 ?  64  GLU   A HG3  1 
ATOM   1461 N  N    . SER   A 1 65  ? 34.258 6.819   5.211   1.00 10.64 ?  65  SER   A N    1 
ATOM   1462 C  CA   . SER   A 1 65  ? 34.205 6.159   3.911   1.00 10.43 ?  65  SER   A CA   1 
ATOM   1463 C  C    . SER   A 1 65  ? 35.132 6.822   2.902   1.00 10.56 ?  65  SER   A C    1 
ATOM   1464 O  O    . SER   A 1 65  ? 35.769 6.138   2.093   1.00 11.60 ?  65  SER   A O    1 
ATOM   1465 C  CB   . SER   A 1 65  ? 32.774 6.169   3.377   1.00 10.62 ?  65  SER   A CB   1 
ATOM   1466 O  OG   . SER   A 1 65  ? 31.919 5.360   4.173   1.00 11.05 ?  65  SER   A OG   1 
ATOM   1467 H  H    . SER   A 1 65  ? 33.520 7.197   5.443   1.00 12.75 ?  65  SER   A H    1 
ATOM   1468 H  HA   . SER   A 1 65  ? 34.487 5.239   4.013   1.00 12.49 ?  65  SER   A HA   1 
ATOM   1469 H  HB2  . SER   A 1 65  ? 32.440 7.075   3.381   1.00 12.72 ?  65  SER   A HB2  1 
ATOM   1470 H  HB3  . SER   A 1 65  ? 32.779 5.819   2.471   1.00 12.72 ?  65  SER   A HB3  1 
ATOM   1471 H  HG   . SER   A 1 65  ? 31.911 5.645   4.968   1.00 13.24 ?  65  SER   A HG   1 
ATOM   1472 N  N    . ASP   A 1 66  ? 35.207 8.156   2.916   1.00 10.79 ?  66  ASP   A N    1 
ATOM   1473 C  CA   . ASP   A 1 66  ? 36.073 8.849   1.969   1.00 11.82 ?  66  ASP   A CA   1 
ATOM   1474 C  C    . ASP   A 1 66  ? 37.534 8.492   2.210   1.00 11.77 ?  66  ASP   A C    1 
ATOM   1475 O  O    . ASP   A 1 66  ? 38.306 8.315   1.260   1.00 12.50 ?  66  ASP   A O    1 
ATOM   1476 C  CB   . ASP   A 1 66  ? 35.858 10.357  2.072   1.00 13.12 ?  66  ASP   A CB   1 
ATOM   1477 C  CG   . ASP   A 1 66  ? 34.529 10.818  1.459   1.00 14.62 ?  66  ASP   A CG   1 
ATOM   1478 O  OD1  . ASP   A 1 66  ? 33.813 10.022  0.807   1.00 14.89 ?  66  ASP   A OD1  1 
ATOM   1479 O  OD2  . ASP   A 1 66  ? 34.227 12.019  1.614   1.00 17.33 -1 66  ASP   A OD2  1 
ATOM   1480 H  H    . ASP   A 1 66  ? 34.760 8.671   3.441   1.00 12.92 ?  66  ASP   A H    1 
ATOM   1481 H  HA   . ASP   A 1 66  ? 35.841 8.576   1.067   1.00 14.16 ?  66  ASP   A HA   1 
ATOM   1482 H  HB2  . ASP   A 1 66  ? 35.859 10.613  3.010   1.00 15.72 ?  66  ASP   A HB2  1 
ATOM   1483 H  HB3  . ASP   A 1 66  ? 36.578 10.812  1.606   1.00 15.72 ?  66  ASP   A HB3  1 
ATOM   1484 N  N    . ASP   A 1 67  ? 37.927 8.360   3.476   1.00 11.87 ?  67  ASP   A N    1 
ATOM   1485 C  CA   . ASP   A 1 67  ? 39.282 7.916   3.779   1.00 12.53 ?  67  ASP   A CA   1 
ATOM   1486 C  C    . ASP   A 1 67  ? 39.504 6.479   3.317   1.00 12.48 ?  67  ASP   A C    1 
ATOM   1487 O  O    . ASP   A 1 67  ? 40.565 6.151   2.770   1.00 13.14 ?  67  ASP   A O    1 
ATOM   1488 C  CB   . ASP   A 1 67  ? 39.544 8.055   5.277   1.00 13.77 ?  67  ASP   A CB   1 
ATOM   1489 C  CG   . ASP   A 1 67  ? 40.836 7.397   5.707   1.00 15.26 ?  67  ASP   A CG   1 
ATOM   1490 O  OD1  . ASP   A 1 67  ? 41.910 8.031   5.579   1.00 17.73 ?  67  ASP   A OD1  1 
ATOM   1491 O  OD2  . ASP   A 1 67  ? 40.779 6.236   6.169   1.00 15.23 -1 67  ASP   A OD2  1 
ATOM   1492 H  H    . ASP   A 1 67  ? 37.442 8.519   4.160   1.00 14.22 ?  67  ASP   A H    1 
ATOM   1493 H  HA   . ASP   A 1 67  ? 39.916 8.478   3.306   1.00 15.01 ?  67  ASP   A HA   1 
ATOM   1494 H  HB2  . ASP   A 1 67  ? 39.596 8.994   5.496   1.00 16.51 ?  67  ASP   A HB2  1 
ATOM   1495 H  HB3  . ASP   A 1 67  ? 38.820 7.632   5.761   1.00 16.51 ?  67  ASP   A HB3  1 
ATOM   1496 N  N    . TYR   A 1 68  ? 38.509 5.605   3.514   1.00 12.08 ?  68  TYR   A N    1 
ATOM   1497 C  CA   . TYR   A 1 68  ? 38.627 4.226   3.041   1.00 12.21 ?  68  TYR   A CA   1 
ATOM   1498 C  C    . TYR   A 1 68  ? 38.871 4.175   1.534   1.00 12.01 ?  68  TYR   A C    1 
ATOM   1499 O  O    . TYR   A 1 68  ? 39.748 3.441   1.059   1.00 12.47 ?  68  TYR   A O    1 
ATOM   1500 C  CB   . TYR   A 1 68  ? 37.371 3.412   3.412   1.00 12.55 ?  68  TYR   A CB   1 
ATOM   1501 C  CG   . TYR   A 1 68  ? 37.396 2.021   2.789   1.00 14.06 ?  68  TYR   A CG   1 
ATOM   1502 C  CD1  . TYR   A 1 68  ? 36.939 1.821   1.489   1.00 15.32 ?  68  TYR   A CD1  1 
ATOM   1503 C  CD2  . TYR   A 1 68  ? 37.930 0.933   3.465   1.00 15.51 ?  68  TYR   A CD2  1 
ATOM   1504 C  CE1  . TYR   A 1 68  ? 37.001 0.597   0.882   1.00 16.62 ?  68  TYR   A CE1  1 
ATOM   1505 C  CE2  . TYR   A 1 68  ? 37.990 -0.330  2.856   1.00 16.25 ?  68  TYR   A CE2  1 
ATOM   1506 C  CZ   . TYR   A 1 68  ? 37.535 -0.469  1.563   1.00 16.71 ?  68  TYR   A CZ   1 
ATOM   1507 O  OH   . TYR   A 1 68  ? 37.606 -1.683  0.937   1.00 17.77 ?  68  TYR   A OH   1 
ATOM   1508 H  H    . TYR   A 1 68  ? 37.767 5.783   3.914   1.00 14.47 ?  68  TYR   A H    1 
ATOM   1509 H  HA   . TYR   A 1 68  ? 39.382 3.809   3.477   1.00 14.63 ?  68  TYR   A HA   1 
ATOM   1510 H  HB2  . TYR   A 1 68  ? 37.327 3.309   4.374   1.00 15.04 ?  68  TYR   A HB2  1 
ATOM   1511 H  HB3  . TYR   A 1 68  ? 36.580 3.874   3.087   1.00 15.04 ?  68  TYR   A HB3  1 
ATOM   1512 H  HD1  . TYR   A 1 68  ? 36.592 2.546   1.015   1.00 18.36 ?  68  TYR   A HD1  1 
ATOM   1513 H  HD2  . TYR   A 1 68  ? 38.260 1.045   4.325   1.00 18.59 ?  68  TYR   A HD2  1 
ATOM   1514 H  HE1  . TYR   A 1 68  ? 36.685 0.492   0.015   1.00 19.93 ?  68  TYR   A HE1  1 
ATOM   1515 H  HE2  . TYR   A 1 68  ? 38.354 -1.055  3.303   1.00 19.48 ?  68  TYR   A HE2  1 
ATOM   1516 H  HH   . TYR   A 1 68  ? 37.934 -2.253  1.460   1.00 21.30 ?  68  TYR   A HH   1 
ATOM   1517 N  N    . ILE   A 1 69  ? 38.084 4.932   0.760   1.00 11.64 ?  69  ILE   A N    1 
ATOM   1518 C  CA   . ILE   A 1 69  ? 38.222 4.922   -0.698  1.00 11.65 ?  69  ILE   A CA   1 
ATOM   1519 C  C    . ILE   A 1 69  ? 39.557 5.524   -1.124  1.00 11.59 ?  69  ILE   A C    1 
ATOM   1520 O  O    . ILE   A 1 69  ? 40.202 5.039   -2.061  1.00 12.33 ?  69  ILE   A O    1 
ATOM   1521 C  CB   . ILE   A 1 69  ? 37.032 5.641   -1.363  1.00 12.57 ?  69  ILE   A CB   1 
ATOM   1522 C  CG1  . ILE   A 1 69  ? 35.715 4.915   -1.090  1.00 13.05 ?  69  ILE   A CG1  1 
ATOM   1523 C  CG2  . ILE   A 1 69  ? 37.271 5.825   -2.873  1.00 14.24 ?  69  ILE   A CG2  1 
ATOM   1524 C  CD1  . ILE   A 1 69  ? 35.556 3.621   -1.858  1.00 13.58 ?  69  ILE   A CD1  1 
ATOM   1525 H  H    . ILE   A 1 69  ? 37.477 5.463   1.054   1.00 13.94 ?  69  ILE   A H    1 
ATOM   1526 H  HA   . ILE   A 1 69  ? 38.213 4.001   -0.997  1.00 13.96 ?  69  ILE   A HA   1 
ATOM   1527 H  HB   . ILE   A 1 69  ? 36.966 6.522   -0.971  1.00 15.06 ?  69  ILE   A HB   1 
ATOM   1528 H  HG12 . ILE   A 1 69  ? 35.664 4.706   -0.144  1.00 15.63 ?  69  ILE   A HG12 1 
ATOM   1529 H  HG13 . ILE   A 1 69  ? 34.981 5.499   -1.337  1.00 15.63 ?  69  ILE   A HG13 1 
ATOM   1530 H  HG21 . ILE   A 1 69  ? 36.428 6.044   -3.303  1.00 17.07 ?  69  ILE   A HG21 1 
ATOM   1531 H  HG22 . ILE   A 1 69  ? 37.902 6.556   -3.009  1.00 17.07 ?  69  ILE   A HG22 1 
ATOM   1532 H  HG23 . ILE   A 1 69  ? 37.629 5.007   -3.245  1.00 17.07 ?  69  ILE   A HG23 1 
ATOM   1533 H  HD11 . ILE   A 1 69  ? 34.756 3.172   -1.547  1.00 16.27 ?  69  ILE   A HD11 1 
ATOM   1534 H  HD12 . ILE   A 1 69  ? 35.474 3.824   -2.804  1.00 16.27 ?  69  ILE   A HD12 1 
ATOM   1535 H  HD13 . ILE   A 1 69  ? 36.332 3.063   -1.703  1.00 16.27 ?  69  ILE   A HD13 1 
ATOM   1536 N  N    . ALA   A 1 70  ? 39.980 6.601   -0.467  1.00 12.26 ?  70  ALA   A N    1 
ATOM   1537 C  CA   . ALA   A 1 70  ? 41.259 7.205   -0.822  1.00 13.24 ?  70  ALA   A CA   1 
ATOM   1538 C  C    . ALA   A 1 70  ? 42.406 6.223   -0.640  1.00 13.66 ?  70  ALA   A C    1 
ATOM   1539 O  O    . ALA   A 1 70  ? 43.386 6.267   -1.389  1.00 15.59 ?  70  ALA   A O    1 
ATOM   1540 C  CB   . ALA   A 1 70  ? 41.496 8.467   0.010   1.00 13.93 ?  70  ALA   A CB   1 
ATOM   1541 H  H    . ALA   A 1 70  ? 39.555 6.993   0.167   1.00 14.69 ?  70  ALA   A H    1 
ATOM   1542 H  HA   . ALA   A 1 70  ? 41.234 7.472   -1.756  1.00 15.87 ?  70  ALA   A HA   1 
ATOM   1543 H  HB1  . ALA   A 1 70  ? 42.355 8.853   -0.240  1.00 16.69 ?  70  ALA   A HB1  1 
ATOM   1544 H  HB2  . ALA   A 1 70  ? 40.787 9.104   -0.163  1.00 16.69 ?  70  ALA   A HB2  1 
ATOM   1545 H  HB3  . ALA   A 1 70  ? 41.508 8.229   0.951   1.00 16.69 ?  70  ALA   A HB3  1 
ATOM   1546 N  N    . THR   A 1 71  ? 42.297 5.326   0.334   1.00 13.35 ?  71  THR   A N    1 
ATOM   1547 C  CA   . THR   A 1 71  ? 43.348 4.345   0.585   1.00 14.89 ?  71  THR   A CA   1 
ATOM   1548 C  C    . THR   A 1 71  ? 43.225 3.122   -0.313  1.00 14.91 ?  71  THR   A C    1 
ATOM   1549 O  O    . THR   A 1 71  ? 44.240 2.604   -0.805  1.00 16.63 ?  71  THR   A O    1 
ATOM   1550 C  CB   . THR   A 1 71  ? 43.273 3.895   2.040   1.00 17.04 ?  71  THR   A CB   1 
ATOM   1551 O  OG1  . THR   A 1 71  ? 43.497 5.021   2.893   1.00 18.34 ?  71  THR   A OG1  1 
ATOM   1552 C  CG2  . THR   A 1 71  ? 44.294 2.804   2.331   1.00 18.26 ?  71  THR   A CG2  1 
ATOM   1553 H  H    . THR   A 1 71  ? 41.623 5.261   0.860   1.00 16.00 ?  71  THR   A H    1 
ATOM   1554 H  HA   . THR   A 1 71  ? 44.214 4.750   0.430   1.00 17.84 ?  71  THR   A HA   1 
ATOM   1555 H  HB   . THR   A 1 71  ? 42.389 3.526   2.209   1.00 20.42 ?  71  THR   A HB   1 
ATOM   1556 H  HG1  . THR   A 1 71  ? 42.902 5.596   2.759   1.00 21.99 ?  71  THR   A HG1  1 
ATOM   1557 H  HG21 . THR   A 1 71  ? 44.423 2.721   3.289   1.00 21.89 ?  71  THR   A HG21 1 
ATOM   1558 H  HG22 . THR   A 1 71  ? 43.993 1.951   1.981   1.00 21.89 ?  71  THR   A HG22 1 
ATOM   1559 H  HG23 . THR   A 1 71  ? 45.147 3.029   1.922   1.00 21.89 ?  71  THR   A HG23 1 
ATOM   1560 N  N    . ASN   A 1 72  ? 41.999 2.622   -0.507  1.00 13.82 ?  72  ASN   A N    1 
ATOM   1561 C  CA   . ASN   A 1 72  ? 41.784 1.295   -1.067  1.00 13.90 ?  72  ASN   A CA   1 
ATOM   1562 C  C    . ASN   A 1 72  ? 41.166 1.280   -2.451  1.00 13.93 ?  72  ASN   A C    1 
ATOM   1563 O  O    . ASN   A 1 72  ? 41.171 0.221   -3.092  1.00 14.89 ?  72  ASN   A O    1 
ATOM   1564 C  CB   . ASN   A 1 72  ? 40.889 0.472   -0.132  1.00 14.66 ?  72  ASN   A CB   1 
ATOM   1565 C  CG   . ASN   A 1 72  ? 41.496 0.312   1.234   1.00 15.91 ?  72  ASN   A CG   1 
ATOM   1566 O  OD1  . ASN   A 1 72  ? 41.040 0.906   2.206   1.00 17.62 ?  72  ASN   A OD1  1 
ATOM   1567 N  ND2  . ASN   A 1 72  ? 42.550 -0.472  1.313   1.00 16.23 ?  72  ASN   A ND2  1 
ATOM   1568 H  H    . ASN   A 1 72  ? 41.266 3.042   -0.322  1.00 16.56 ?  72  ASN   A H    1 
ATOM   1569 H  HA   . ASN   A 1 72  ? 42.639 0.848   -1.130  1.00 16.65 ?  72  ASN   A HA   1 
ATOM   1570 H  HB2  . ASN   A 1 72  ? 40.033 0.914   -0.042  1.00 17.57 ?  72  ASN   A HB2  1 
ATOM   1571 H  HB3  . ASN   A 1 72  ? 40.770 -0.414  -0.516  1.00 17.57 ?  72  ASN   A HB3  1 
ATOM   1572 H  HD21 . ASN   A 1 72  ? 42.940 -0.587  2.072   1.00 19.45 ?  72  ASN   A HD21 1 
ATOM   1573 H  HD22 . ASN   A 1 72  ? 42.854 -0.859  0.610   1.00 19.45 ?  72  ASN   A HD22 1 
ATOM   1574 N  N    . GLY   A 1 73  ? 40.613 2.392   -2.916  1.00 13.55 ?  73  GLY   A N    1 
ATOM   1575 C  CA   . GLY   A 1 73  ? 39.888 2.400   -4.159  1.00 13.33 ?  73  GLY   A CA   1 
ATOM   1576 C  C    . GLY   A 1 73  ? 38.492 1.832   -3.987  1.00 12.77 ?  73  GLY   A C    1 
ATOM   1577 O  O    . GLY   A 1 73  ? 38.102 1.377   -2.903  1.00 13.07 ?  73  GLY   A O    1 
ATOM   1578 H  H    . GLY   A 1 73  ? 40.651 3.163   -2.530  1.00 16.24 ?  73  GLY   A H    1 
ATOM   1579 H  HA2  . GLY   A 1 73  ? 39.819 3.313   -4.490  1.00 15.97 ?  73  GLY   A HA2  1 
ATOM   1580 H  HA3  . GLY   A 1 73  ? 40.365 1.871   -4.821  1.00 15.97 ?  73  GLY   A HA3  1 
ATOM   1581 N  N    . PRO   A 1 74  ? 37.718 1.846   -5.068  1.00 13.12 ?  74  PRO   A N    1 
ATOM   1582 C  CA   . PRO   A 1 74  ? 36.318 1.428   -4.984  1.00 13.02 ?  74  PRO   A CA   1 
ATOM   1583 C  C    . PRO   A 1 74  ? 36.171 -0.053  -4.669  1.00 12.17 ?  74  PRO   A C    1 
ATOM   1584 O  O    . PRO   A 1 74  ? 37.037 -0.884  -4.951  1.00 13.30 ?  74  PRO   A O    1 
ATOM   1585 C  CB   . PRO   A 1 74  ? 35.771 1.734   -6.384  1.00 14.70 ?  74  PRO   A CB   1 
ATOM   1586 C  CG   . PRO   A 1 74  ? 36.735 2.691   -6.998  1.00 17.49 ?  74  PRO   A CG   1 
ATOM   1587 C  CD   . PRO   A 1 74  ? 38.067 2.337   -6.412  1.00 15.15 ?  74  PRO   A CD   1 
ATOM   1588 H  HA   . PRO   A 1 74  ? 35.844 1.955   -4.323  1.00 15.60 ?  74  PRO   A HA   1 
ATOM   1589 H  HB2  . PRO   A 1 74  ? 35.725 0.914   -6.899  1.00 17.61 ?  74  PRO   A HB2  1 
ATOM   1590 H  HB3  . PRO   A 1 74  ? 34.892 2.138   -6.305  1.00 17.61 ?  74  PRO   A HB3  1 
ATOM   1591 H  HG2  . PRO   A 1 74  ? 36.746 2.577   -7.961  1.00 20.97 ?  74  PRO   A HG2  1 
ATOM   1592 H  HG3  . PRO   A 1 74  ? 36.494 3.600   -6.763  1.00 20.97 ?  74  PRO   A HG3  1 
ATOM   1593 H  HD2  . PRO   A 1 74  ? 38.492 1.634   -6.934  1.00 18.16 ?  74  PRO   A HD2  1 
ATOM   1594 H  HD3  . PRO   A 1 74  ? 38.631 3.128   -6.365  1.00 18.16 ?  74  PRO   A HD3  1 
ATOM   1595 N  N    . LEU   A 1 75  ? 35.021 -0.375  -4.088  1.00 11.45 ?  75  LEU   A N    1 
ATOM   1596 C  CA   . LEU   A 1 75  ? 34.617 -1.765  -3.942  1.00 11.11 ?  75  LEU   A CA   1 
ATOM   1597 C  C    . LEU   A 1 75  ? 34.227 -2.337  -5.301  1.00 11.79 ?  75  LEU   A C    1 
ATOM   1598 O  O    . LEU   A 1 75  ? 34.114 -1.622  -6.301  1.00 13.25 ?  75  LEU   A O    1 
ATOM   1599 C  CB   . LEU   A 1 75  ? 33.426 -1.882  -2.992  1.00 11.38 ?  75  LEU   A CB   1 
ATOM   1600 C  CG   . LEU   A 1 75  ? 33.635 -1.461  -1.542  1.00 13.21 ?  75  LEU   A CG   1 
ATOM   1601 C  CD1  . LEU   A 1 75  ? 32.352 -1.638  -0.746  1.00 15.14 ?  75  LEU   A CD1  1 
ATOM   1602 C  CD2  . LEU   A 1 75  ? 34.772 -2.191  -0.886  1.00 16.13 ?  75  LEU   A CD2  1 
ATOM   1603 H  H    . LEU   A 1 75  ? 34.461 0.194   -3.768  1.00 13.71 ?  75  LEU   A H    1 
ATOM   1604 H  HA   . LEU   A 1 75  ? 35.353 -2.280  -3.590  1.00 13.31 ?  75  LEU   A HA   1 
ATOM   1605 H  HB2  . LEU   A 1 75  ? 32.704 -1.342  -3.345  1.00 13.63 ?  75  LEU   A HB2  1 
ATOM   1606 H  HB3  . LEU   A 1 75  ? 33.150 -2.813  -2.979  1.00 13.63 ?  75  LEU   A HB3  1 
ATOM   1607 H  HG   . LEU   A 1 75  ? 33.860 -0.515  -1.533  1.00 15.84 ?  75  LEU   A HG   1 
ATOM   1608 H  HD11 . LEU   A 1 75  ? 32.511 -1.357  0.169   1.00 18.14 ?  75  LEU   A HD11 1 
ATOM   1609 H  HD12 . LEU   A 1 75  ? 31.659 -1.087  -1.145  1.00 18.14 ?  75  LEU   A HD12 1 
ATOM   1610 H  HD13 . LEU   A 1 75  ? 32.093 -2.569  -0.770  1.00 18.14 ?  75  LEU   A HD13 1 
ATOM   1611 H  HD21 . LEU   A 1 75  ? 34.820 -1.932  0.047   1.00 19.33 ?  75  LEU   A HD21 1 
ATOM   1612 H  HD22 . LEU   A 1 75  ? 34.624 -3.145  -0.960  1.00 19.33 ?  75  LEU   A HD22 1 
ATOM   1613 H  HD23 . LEU   A 1 75  ? 35.606 -1.953  -1.333  1.00 19.33 ?  75  LEU   A HD23 1 
ATOM   1614 N  N    . LYS   A 1 76  ? 34.038 -3.655  -5.323  1.00 12.23 ?  76  LYS   A N    1 
ATOM   1615 C  CA   . LYS   A 1 76  ? 33.442 -4.369  -6.445  1.00 12.67 ?  76  LYS   A CA   1 
ATOM   1616 C  C    . LYS   A 1 76  ? 31.929 -4.454  -6.250  1.00 11.42 ?  76  LYS   A C    1 
ATOM   1617 O  O    . LYS   A 1 76  ? 31.449 -4.571  -5.125  1.00 11.60 ?  76  LYS   A O    1 
ATOM   1618 C  CB   . LYS   A 1 76  ? 33.986 -5.806  -6.501  1.00 14.25 ?  76  LYS   A CB   1 
ATOM   1619 C  CG   . LYS   A 1 76  ? 35.491 -5.918  -6.701  1.00 15.63 ?  76  LYS   A CG   1 
ATOM   1620 C  CD   . LYS   A 1 76  ? 36.004 -7.321  -6.470  1.00 17.09 ?  76  LYS   A CD   1 
ATOM   1621 C  CE   . LYS   A 1 76  ? 37.502 -7.389  -6.675  1.00 19.56 ?  76  LYS   A CE   1 
ATOM   1622 N  NZ   . LYS   A 1 76  ? 38.031 -8.746  -6.445  1.00 20.41 ?  76  LYS   A NZ   1 
ATOM   1623 H  H    . LYS   A 1 76  ? 34.256 -4.174  -4.670  1.00 14.65 ?  76  LYS   A H    1 
ATOM   1624 H  HA   . LYS   A 1 76  ? 33.639 -3.914  -7.279  1.00 15.18 ?  76  LYS   A HA   1 
ATOM   1625 H  HB2  . LYS   A 1 76  ? 33.766 -6.248  -5.666  1.00 17.08 ?  76  LYS   A HB2  1 
ATOM   1626 H  HB3  . LYS   A 1 76  ? 33.555 -6.267  -7.237  1.00 17.08 ?  76  LYS   A HB3  1 
ATOM   1627 H  HG2  . LYS   A 1 76  ? 35.707 -5.662  -7.612  1.00 18.73 ?  76  LYS   A HG2  1 
ATOM   1628 H  HG3  . LYS   A 1 76  ? 35.938 -5.326  -6.075  1.00 18.73 ?  76  LYS   A HG3  1 
ATOM   1629 H  HD2  . LYS   A 1 76  ? 35.805 -7.593  -5.559  1.00 20.49 ?  76  LYS   A HD2  1 
ATOM   1630 H  HD3  . LYS   A 1 76  ? 35.580 -7.927  -7.101  1.00 20.49 ?  76  LYS   A HD3  1 
ATOM   1631 H  HE2  . LYS   A 1 76  ? 37.710 -7.132  -7.586  1.00 23.45 ?  76  LYS   A HE2  1 
ATOM   1632 H  HE3  . LYS   A 1 76  ? 37.934 -6.787  -6.049  1.00 23.45 ?  76  LYS   A HE3  1 
ATOM   1633 H  HZ1  . LYS   A 1 76  ? 38.912 -8.761  -6.573  1.00 24.47 ?  76  LYS   A HZ1  1 
ATOM   1634 H  HZ2  . LYS   A 1 76  ? 37.856 -9.011  -5.613  1.00 24.47 ?  76  LYS   A HZ2  1 
ATOM   1635 H  HZ3  . LYS   A 1 76  ? 37.652 -9.324  -7.012  1.00 24.47 ?  76  LYS   A HZ3  1 
ATOM   1636 N  N    . VAL   A 1 77  ? 31.178 -4.415  -7.354  1.00 12.00 ?  77  VAL   A N    1 
ATOM   1637 C  CA   . VAL   A 1 77  ? 29.770 -4.799  -7.272  1.00 11.77 ?  77  VAL   A CA   1 
ATOM   1638 C  C    . VAL   A 1 77  ? 29.707 -6.252  -6.829  1.00 11.61 ?  77  VAL   A C    1 
ATOM   1639 O  O    . VAL   A 1 77  ? 30.365 -7.122  -7.412  1.00 11.89 ?  77  VAL   A O    1 
ATOM   1640 C  CB   . VAL   A 1 77  ? 29.048 -4.579  -8.611  1.00 12.92 ?  77  VAL   A CB   1 
ATOM   1641 C  CG1  . VAL   A 1 77  ? 27.588 -5.002  -8.495  1.00 13.63 ?  77  VAL   A CG1  1 
ATOM   1642 C  CG2  . VAL   A 1 77  ? 29.144 -3.124  -9.040  1.00 14.22 ?  77  VAL   A CG2  1 
ATOM   1643 H  H    . VAL   A 1 77  ? 31.456 -4.176  -8.132  1.00 14.38 ?  77  VAL   A H    1 
ATOM   1644 H  HA   . VAL   A 1 77  ? 29.336 -4.257  -6.598  1.00 14.10 ?  77  VAL   A HA   1 
ATOM   1645 H  HB   . VAL   A 1 77  ? 29.473 -5.121  -9.294  1.00 15.48 ?  77  VAL   A HB   1 
ATOM   1646 H  HG11 . VAL   A 1 77  ? 27.112 -4.693  -9.278  1.00 16.33 ?  77  VAL   A HG11 1 
ATOM   1647 H  HG12 . VAL   A 1 77  ? 27.544 -5.967  -8.435  1.00 16.33 ?  77  VAL   A HG12 1 
ATOM   1648 H  HG13 . VAL   A 1 77  ? 27.211 -4.600  -7.696  1.00 16.33 ?  77  VAL   A HG13 1 
ATOM   1649 H  HG21 . VAL   A 1 77  ? 28.638 -3.005  -9.859  1.00 17.04 ?  77  VAL   A HG21 1 
ATOM   1650 H  HG22 . VAL   A 1 77  ? 28.775 -2.564  -8.339  1.00 17.04 ?  77  VAL   A HG22 1 
ATOM   1651 H  HG23 . VAL   A 1 77  ? 30.075 -2.896  -9.190  1.00 17.04 ?  77  VAL   A HG23 1 
ATOM   1652 N  N    . GLY   A 1 78  ? 28.923 -6.523  -5.785  1.00 11.24 ?  78  GLY   A N    1 
ATOM   1653 C  CA   . GLY   A 1 78  ? 28.899 -7.812  -5.129  1.00 11.45 ?  78  GLY   A CA   1 
ATOM   1654 C  C    . GLY   A 1 78  ? 29.809 -7.905  -3.927  1.00 11.08 ?  78  GLY   A C    1 
ATOM   1655 O  O    . GLY   A 1 78  ? 29.747 -8.908  -3.198  1.00 11.61 ?  78  GLY   A O    1 
ATOM   1656 H  H    . GLY   A 1 78  ? 28.379 -5.948  -5.439  1.00 13.46 ?  78  GLY   A H    1 
ATOM   1657 H  HA2  . GLY   A 1 78  ? 27.995 -8.000  -4.841  1.00 13.72 ?  78  GLY   A HA2  1 
ATOM   1658 H  HA3  . GLY   A 1 78  ? 29.165 -8.492  -5.766  1.00 13.72 ?  78  GLY   A HA3  1 
ATOM   1659 N  N    . GLY   A 1 79  ? 30.664 -6.903  -3.704  1.00 11.01 ?  79  GLY   A N    1 
ATOM   1660 C  CA   . GLY   A 1 79  ? 31.622 -6.920  -2.622  1.00 11.07 ?  79  GLY   A CA   1 
ATOM   1661 C  C    . GLY   A 1 79  ? 31.176 -6.119  -1.411  1.00 10.59 ?  79  GLY   A C    1 
ATOM   1662 O  O    . GLY   A 1 79  ? 30.058 -5.604  -1.334  1.00 11.40 ?  79  GLY   A O    1 
ATOM   1663 H  H    . GLY   A 1 79  ? 30.705 -6.186  -4.183  1.00 13.19 ?  79  GLY   A H    1 
ATOM   1664 H  HA2  . GLY   A 1 79  ? 31.775 -7.841  -2.347  1.00 13.27 ?  79  GLY   A HA2  1 
ATOM   1665 H  HA3  . GLY   A 1 79  ? 32.467 -6.558  -2.936  1.00 13.27 ?  79  GLY   A HA3  1 
ATOM   1666 N  N    . SER   A 1 80  ? 32.086 -6.021  -0.441  1.00 11.30 ?  80  SER   A N    1 
ATOM   1667 C  CA   . SER   A 1 80  ? 31.761 -5.399  0.830   1.00 10.80 ?  80  SER   A CA   1 
ATOM   1668 C  C    . SER   A 1 80  ? 33.030 -4.949  1.534   1.00 10.79 ?  80  SER   A C    1 
ATOM   1669 O  O    . SER   A 1 80  ? 34.141 -5.388  1.211   1.00 12.37 ?  80  SER   A O    1 
ATOM   1670 C  CB   . SER   A 1 80  ? 31.000 -6.365  1.746   1.00 11.89 ?  80  SER   A CB   1 
ATOM   1671 O  OG   . SER   A 1 80  ? 31.832 -7.405  2.230   1.00 13.53 ?  80  SER   A OG   1 
ATOM   1672 H  H    . SER   A 1 80  ? 32.901 -6.296  -0.504  1.00 13.53 ?  80  SER   A H    1 
ATOM   1673 H  HA   . SER   A 1 80  ? 31.205 -4.620  0.655   1.00 12.94 ?  80  SER   A HA   1 
ATOM   1674 H  HB2  . SER   A 1 80  ? 30.652 -5.863  2.500   1.00 14.25 ?  80  SER   A HB2  1 
ATOM   1675 H  HB3  . SER   A 1 80  ? 30.265 -6.753  1.244   1.00 14.25 ?  80  SER   A HB3  1 
ATOM   1676 H  HG   . SER   A 1 80  ? 32.139 -7.844  1.580   1.00 16.21 ?  80  SER   A HG   1 
ATOM   1677 N  N    . CYS   A 1 81  ? 32.840 -4.094  2.537   1.00 10.62 ?  81  CYS   A N    1 
ATOM   1678 C  CA   . CYS   A 1 81  ? 33.893 -3.816  3.499   1.00 10.68 ?  81  CYS   A CA   1 
ATOM   1679 C  C    . CYS   A 1 81  ? 33.251 -3.577  4.856   1.00 10.56 ?  81  CYS   A C    1 
ATOM   1680 O  O    . CYS   A 1 81  ? 32.086 -3.172  4.943   1.00 11.74 ?  81  CYS   A O    1 
ATOM   1681 C  CB   . CYS   A 1 81  ? 34.769 -2.626  3.081   1.00 11.44 ?  81  CYS   A CB   1 
ATOM   1682 S  SG   . CYS   A 1 81  ? 33.874 -1.052  3.093   1.00 11.46 ?  81  CYS   A SG   1 
ATOM   1683 H  H    . CYS   A 1 81  ? 32.104 -3.667  2.685   1.00 12.72 ?  81  CYS   A H    1 
ATOM   1684 H  HA   . CYS   A 1 81  ? 34.463 -4.596  3.571   1.00 12.80 ?  81  CYS   A HA   1 
ATOM   1685 H  HB2  . CYS   A 1 81  ? 35.522 -2.560  3.693   1.00 13.70 ?  81  CYS   A HB2  1 
ATOM   1686 H  HB3  . CYS   A 1 81  ? 35.100 -2.784  2.177   1.00 13.70 ?  81  CYS   A HB3  1 
ATOM   1687 H  HG   . CYS   A 1 81  ? 34.622 -0.174  2.758   1.00 13.73 ?  81  CYS   A HG   1 
ATOM   1688 N  N    . VAL   A 1 82  ? 34.017 -3.839  5.911   1.00 10.89 ?  82  VAL   A N    1 
ATOM   1689 C  CA   . VAL   A 1 82  ? 33.588 -3.594  7.280   1.00 11.50 ?  82  VAL   A CA   1 
ATOM   1690 C  C    . VAL   A 1 82  ? 34.187 -2.278  7.752   1.00 11.88 ?  82  VAL   A C    1 
ATOM   1691 O  O    . VAL   A 1 82  ? 35.411 -2.109  7.744   1.00 12.48 ?  82  VAL   A O    1 
ATOM   1692 C  CB   . VAL   A 1 82  ? 34.009 -4.736  8.214   1.00 13.02 ?  82  VAL   A CB   1 
ATOM   1693 C  CG1  . VAL   A 1 82  ? 33.569 -4.436  9.637   1.00 14.34 ?  82  VAL   A CG1  1 
ATOM   1694 C  CG2  . VAL   A 1 82  ? 33.443 -6.063  7.737   1.00 14.10 ?  82  VAL   A CG2  1 
ATOM   1695 H  H    . VAL   A 1 82  ? 34.812 -4.179  5.852   1.00 13.05 ?  82  VAL   A H    1 
ATOM   1696 H  HA   . VAL   A 1 82  ? 32.622 -3.517  7.301   1.00 13.78 ?  82  VAL   A HA   1 
ATOM   1697 H  HB   . VAL   A 1 82  ? 34.974 -4.802  8.212   1.00 15.61 ?  82  VAL   A HB   1 
ATOM   1698 H  HG11 . VAL   A 1 82  ? 33.646 -5.245  10.166  1.00 17.18 ?  82  VAL   A HG11 1 
ATOM   1699 H  HG12 . VAL   A 1 82  ? 34.137 -3.743  10.010  1.00 17.18 ?  82  VAL   A HG12 1 
ATOM   1700 H  HG13 . VAL   A 1 82  ? 32.645 -4.137  9.627   1.00 17.18 ?  82  VAL   A HG13 1 
ATOM   1701 H  HG21 . VAL   A 1 82  ? 33.681 -6.754  8.373   1.00 16.89 ?  82  VAL   A HG21 1 
ATOM   1702 H  HG22 . VAL   A 1 82  ? 32.476 -5.989  7.675   1.00 16.89 ?  82  VAL   A HG22 1 
ATOM   1703 H  HG23 . VAL   A 1 82  ? 33.814 -6.270  6.866   1.00 16.89 ?  82  VAL   A HG23 1 
ATOM   1704 N  N    . LEU   A 1 83  ? 33.332 -1.351  8.169   1.00 11.22 ?  83  LEU   A N    1 
ATOM   1705 C  CA   . LEU   A 1 83  ? 33.757 -0.088  8.750   1.00 11.00 ?  83  LEU   A CA   1 
ATOM   1706 C  C    . LEU   A 1 83  ? 33.037 0.094   10.083  1.00 11.20 ?  83  LEU   A C    1 
ATOM   1707 O  O    . LEU   A 1 83  ? 32.313 -0.796  10.546  1.00 11.90 ?  83  LEU   A O    1 
ATOM   1708 C  CB   . LEU   A 1 83  ? 33.510 1.073   7.775   1.00 11.61 ?  83  LEU   A CB   1 
ATOM   1709 C  CG   . LEU   A 1 83  ? 34.408 1.060   6.536   1.00 12.31 ?  83  LEU   A CG   1 
ATOM   1710 C  CD1  . LEU   A 1 83  ? 33.980 2.109   5.528   1.00 12.93 ?  83  LEU   A CD1  1 
ATOM   1711 C  CD2  . LEU   A 1 83  ? 35.881 1.259   6.924   1.00 12.92 ?  83  LEU   A CD2  1 
ATOM   1712 H  H    . LEU   A 1 83  ? 32.477 -1.433  8.116   1.00 13.44 ?  83  LEU   A H    1 
ATOM   1713 H  HA   . LEU   A 1 83  ? 34.708 -0.125  8.930   1.00 13.17 ?  83  LEU   A HA   1 
ATOM   1714 H  HB2  . LEU   A 1 83  ? 32.593 1.035   7.465   1.00 13.91 ?  83  LEU   A HB2  1 
ATOM   1715 H  HB3  . LEU   A 1 83  ? 33.663 1.911   8.238   1.00 13.91 ?  83  LEU   A HB3  1 
ATOM   1716 H  HG   . LEU   A 1 83  ? 34.340 0.192   6.111   1.00 14.75 ?  83  LEU   A HG   1 
ATOM   1717 H  HD11 . LEU   A 1 83  ? 34.573 2.066   4.758   1.00 15.50 ?  83  LEU   A HD11 1 
ATOM   1718 H  HD12 . LEU   A 1 83  ? 33.070 1.924   5.254   1.00 15.50 ?  83  LEU   A HD12 1 
ATOM   1719 H  HD13 . LEU   A 1 83  ? 34.036 2.984   5.939   1.00 15.50 ?  83  LEU   A HD13 1 
ATOM   1720 H  HD21 . LEU   A 1 83  ? 36.406 1.421   6.121   1.00 15.48 ?  83  LEU   A HD21 1 
ATOM   1721 H  HD22 . LEU   A 1 83  ? 35.956 2.020   7.522   1.00 15.48 ?  83  LEU   A HD22 1 
ATOM   1722 H  HD23 . LEU   A 1 83  ? 36.210 0.460   7.370   1.00 15.48 ?  83  LEU   A HD23 1 
ATOM   1723 N  N    . SER   A 1 84  ? 33.253 1.244   10.718  1.00 11.99 ?  84  SER   A N    1 
ATOM   1724 C  CA   . SER   A 1 84  ? 32.606 1.505   11.994  1.00 12.28 ?  84  SER   A CA   1 
ATOM   1725 C  C    . SER   A 1 84  ? 31.088 1.592   11.845  1.00 11.94 ?  84  SER   A C    1 
ATOM   1726 O  O    . SER   A 1 84  ? 30.565 2.048   10.829  1.00 12.12 ?  84  SER   A O    1 
ATOM   1727 C  CB   . SER   A 1 84  ? 33.104 2.829   12.562  1.00 13.11 ?  84  SER   A CB   1 
ATOM   1728 O  OG   . SER   A 1 84  ? 32.468 3.109   13.791  1.00 13.85 ?  84  SER   A OG   1 
ATOM   1729 H  H    . SER   A 1 84  ? 33.762 1.880   10.429  1.00 14.37 ?  84  SER   A H    1 
ATOM   1730 H  HA   . SER   A 1 84  ? 32.826 0.798   12.616  1.00 14.71 ?  84  SER   A HA   1 
ATOM   1731 H  HB2  . SER   A 1 84  ? 34.066 2.779   12.698  1.00 15.71 ?  84  SER   A HB2  1 
ATOM   1732 H  HB3  . SER   A 1 84  ? 32.900 3.543   11.934  1.00 15.71 ?  84  SER   A HB3  1 
ATOM   1733 H  HG   . SER   A 1 84  ? 32.757 3.838   14.101  1.00 16.60 ?  84  SER   A HG   1 
ATOM   1734 N  N    . GLY   A 1 85  ? 30.379 1.182   12.893  1.00 12.78 ?  85  GLY   A N    1 
ATOM   1735 C  CA   . GLY   A 1 85  ? 28.956 1.413   12.981  1.00 13.45 ?  85  GLY   A CA   1 
ATOM   1736 C  C    . GLY   A 1 85  ? 28.588 2.734   13.618  1.00 13.05 ?  85  GLY   A C    1 
ATOM   1737 O  O    . GLY   A 1 85  ? 27.396 3.048   13.727  1.00 13.81 ?  85  GLY   A O    1 
ATOM   1738 H  H    . GLY   A 1 85  ? 30.715 0.762   13.568  1.00 15.31 ?  85  GLY   A H    1 
ATOM   1739 H  HA2  . GLY   A 1 85  ? 28.579 1.387   12.088  1.00 16.12 ?  85  GLY   A HA2  1 
ATOM   1740 H  HA3  . GLY   A 1 85  ? 28.553 0.703   13.500  1.00 16.12 ?  85  GLY   A HA3  1 
ATOM   1741 N  N    . HIS   A 1 86  ? 29.577 3.511   14.052  1.00 12.70 ?  86  HIS   A N    1 
ATOM   1742 C  CA   . HIS   A 1 86  ? 29.353 4.847   14.617  1.00 13.37 ?  86  HIS   A CA   1 
ATOM   1743 C  C    . HIS   A 1 86  ? 28.361 4.726   15.767  1.00 14.35 ?  86  HIS   A C    1 
ATOM   1744 O  O    . HIS   A 1 86  ? 28.542 3.851   16.628  1.00 15.52 ?  86  HIS   A O    1 
ATOM   1745 C  CB   . HIS   A 1 86  ? 28.988 5.831   13.511  1.00 13.25 ?  86  HIS   A CB   1 
ATOM   1746 C  CG   . HIS   A 1 86  ? 30.044 5.920   12.470  1.00 13.49 ?  86  HIS   A CG   1 
ATOM   1747 N  ND1  . HIS   A 1 86  ? 31.137 6.750   12.595  1.00 14.29 ?  86  HIS   A ND1  1 
ATOM   1748 C  CD2  . HIS   A 1 86  ? 30.220 5.223   11.325  1.00 12.95 ?  86  HIS   A CD2  1 
ATOM   1749 C  CE1  . HIS   A 1 86  ? 31.926 6.578   11.550  1.00 14.02 ?  86  HIS   A CE1  1 
ATOM   1750 N  NE2  . HIS   A 1 86  ? 31.400 5.650   10.772  1.00 13.46 ?  86  HIS   A NE2  1 
ATOM   1751 H  H    . HIS   A 1 86  ? 30.402 3.285   14.043  1.00 15.21 ?  86  HIS   A H    1 
ATOM   1752 H  HA   . HIS   A 1 86  ? 30.185 5.157   15.000  1.00 16.02 ?  86  HIS   A HA   1 
ATOM   1753 H  HB2  . HIS   A 1 86  ? 28.163 5.550   13.085  1.00 15.88 ?  86  HIS   A HB2  1 
ATOM   1754 H  HB3  . HIS   A 1 86  ? 28.874 6.720   13.893  1.00 15.88 ?  86  HIS   A HB3  1 
ATOM   1755 H  HD2  . HIS   A 1 86  ? 29.652 4.564   10.980  1.00 15.52 ?  86  HIS   A HD2  1 
ATOM   1756 H  HE1  . HIS   A 1 86  ? 32.721 7.030   11.378  1.00 16.80 ?  86  HIS   A HE1  1 
ATOM   1757 H  HE2  . HIS   A 1 86  ? 31.731 5.368   10.021  1.00 16.13 ?  86  HIS   A HE2  1 
ATOM   1758 N  N    . ASN   A 1 87  ? 27.349 5.581   15.836  1.00 15.13 ?  87  ASN   A N    1 
ATOM   1759 C  CA   . ASN   A 1 87  ? 26.365 5.572   16.900  1.00 15.96 ?  87  ASN   A CA   1 
ATOM   1760 C  C    . ASN   A 1 87  ? 25.239 4.579   16.660  1.00 17.14 ?  87  ASN   A C    1 
ATOM   1761 O  O    . ASN   A 1 87  ? 24.320 4.510   17.478  1.00 19.17 ?  87  ASN   A O    1 
ATOM   1762 C  CB   . ASN   A 1 87  ? 25.773 6.980   17.057  1.00 16.56 ?  87  ASN   A CB   1 
ATOM   1763 C  CG   . ASN   A 1 87  ? 25.268 7.557   15.739  1.00 17.55 ?  87  ASN   A CG   1 
ATOM   1764 O  OD1  . ASN   A 1 87  ? 25.910 7.432   14.698  1.00 18.09 ?  87  ASN   A OD1  1 
ATOM   1765 N  ND2  . ASN   A 1 87  ? 24.112 8.194   15.785  1.00 18.46 ?  87  ASN   A ND2  1 
ATOM   1766 H  H    . ASN   A 1 87  ? 27.202 6.190   15.255  1.00 18.14 ?  87  ASN   A H    1 
ATOM   1767 H  HA   . ASN   A 1 87  ? 26.792 5.330   17.740  1.00 19.13 ?  87  ASN   A HA   1 
ATOM   1768 H  HB2  . ASN   A 1 87  ? 25.024 6.943   17.681  1.00 19.85 ?  87  ASN   A HB2  1 
ATOM   1769 H  HB3  . ASN   A 1 87  ? 26.458 7.572   17.405  1.00 19.85 ?  87  ASN   A HB3  1 
ATOM   1770 H  HD21 . ASN   A 1 87  ? 23.787 8.531   15.067  1.00 22.13 ?  87  ASN   A HD21 1 
ATOM   1771 H  HD22 . ASN   A 1 87  ? 23.691 8.272   16.531  1.00 22.13 ?  87  ASN   A HD22 1 
ATOM   1772 N  N    . LEU   A 1 88  ? 25.294 3.800   15.584  1.00 15.83 ?  88  LEU   A N    1 
ATOM   1773 C  CA   . LEU   A 1 88  ? 24.184 2.939   15.185  1.00 15.90 ?  88  LEU   A CA   1 
ATOM   1774 C  C    . LEU   A 1 88  ? 24.398 1.463   15.497  1.00 15.27 ?  88  LEU   A C    1 
ATOM   1775 O  O    . LEU   A 1 88  ? 23.417 0.734   15.678  1.00 16.30 ?  88  LEU   A O    1 
ATOM   1776 C  CB   . LEU   A 1 88  ? 23.946 3.084   13.682  1.00 16.28 ?  88  LEU   A CB   1 
ATOM   1777 C  CG   . LEU   A 1 88  ? 23.647 4.501   13.188  1.00 18.12 ?  88  LEU   A CG   1 
ATOM   1778 C  CD1  . LEU   A 1 88  ? 23.499 4.507   11.678  1.00 18.49 ?  88  LEU   A CD1  1 
ATOM   1779 C  CD2  . LEU   A 1 88  ? 22.396 5.056   13.854  1.00 19.67 ?  88  LEU   A CD2  1 
ATOM   1780 H  H    . LEU   A 1 88  ? 25.977 3.752   15.068  1.00 18.97 ?  88  LEU   A H    1 
ATOM   1781 H  HA   . LEU   A 1 88  ? 23.382 3.229   15.644  1.00 19.06 ?  88  LEU   A HA   1 
ATOM   1782 H  HB2  . LEU   A 1 88  ? 24.736 2.780   13.213  1.00 19.51 ?  88  LEU   A HB2  1 
ATOM   1783 H  HB3  . LEU   A 1 88  ? 23.188 2.531   13.438  1.00 19.51 ?  88  LEU   A HB3  1 
ATOM   1784 H  HG   . LEU   A 1 88  ? 24.389 5.081   13.415  1.00 21.72 ?  88  LEU   A HG   1 
ATOM   1785 H  HD11 . LEU   A 1 88  ? 23.310 5.412   11.379  1.00 22.17 ?  88  LEU   A HD11 1 
ATOM   1786 H  HD12 . LEU   A 1 88  ? 24.325 4.194   11.277  1.00 22.17 ?  88  LEU   A HD12 1 
ATOM   1787 H  HD13 . LEU   A 1 88  ? 22.767 3.919   11.427  1.00 22.17 ?  88  LEU   A HD13 1 
ATOM   1788 H  HD21 . LEU   A 1 88  ? 22.163 5.898   13.431  1.00 23.58 ?  88  LEU   A HD21 1 
ATOM   1789 H  HD22 . LEU   A 1 88  ? 21.674 4.419   13.745  1.00 23.58 ?  88  LEU   A HD22 1 
ATOM   1790 H  HD23 . LEU   A 1 88  ? 22.579 5.196   14.795  1.00 23.58 ?  88  LEU   A HD23 1 
ATOM   1791 N  N    . ALA   A 1 89  ? 25.647 1.009   15.537  1.00 14.53 ?  89  ALA   A N    1 
ATOM   1792 C  CA   . ALA   A 1 89  ? 25.988 -0.403  15.642  1.00 14.33 ?  89  ALA   A CA   1 
ATOM   1793 C  C    . ALA   A 1 89  ? 27.472 -0.471  15.963  1.00 14.92 ?  89  ALA   A C    1 
ATOM   1794 O  O    . ALA   A 1 89  ? 28.186 0.523   15.847  1.00 15.58 ?  89  ALA   A O    1 
ATOM   1795 C  CB   . ALA   A 1 89  ? 25.713 -1.120  14.323  1.00 14.00 ?  89  ALA   A CB   1 
ATOM   1796 H  H    . ALA   A 1 89  ? 26.334 1.525   15.496  1.00 17.42 ?  89  ALA   A H    1 
ATOM   1797 H  HA   . ALA   A 1 89  ? 25.476 -0.818  16.356  1.00 17.18 ?  89  ALA   A HA   1 
ATOM   1798 H  HB1  . ALA   A 1 89  ? 25.959 -2.054  14.417  1.00 16.78 ?  89  ALA   A HB1  1 
ATOM   1799 H  HB2  . ALA   A 1 89  ? 24.767 -1.048  14.112  1.00 16.78 ?  89  ALA   A HB2  1 
ATOM   1800 H  HB3  . ALA   A 1 89  ? 26.240 -0.708  13.623  1.00 16.78 ?  89  ALA   A HB3  1 
ATOM   1801 N  N    . LYS   A 1 90  ? 27.944 -1.649  16.360  1.00 15.58 ?  90  LYS   A N    1 
ATOM   1802 C  CA   . LYS   A 1 90  ? 29.388 -1.810  16.508  1.00 16.23 ?  90  LYS   A CA   1 
ATOM   1803 C  C    . LYS   A 1 90  ? 30.089 -1.622  15.166  1.00 14.87 ?  90  LYS   A C    1 
ATOM   1804 O  O    . LYS   A 1 90  ? 31.026 -0.816  15.040  1.00 16.28 ?  90  LYS   A O    1 
ATOM   1805 C  CB   . LYS   A 1 90  ? 29.715 -3.175  17.114  1.00 18.95 ?  90  LYS   A CB   1 
ATOM   1806 C  CG   . LYS   A 1 90  ? 31.189 -3.338  17.459  1.00 23.75 ?  90  LYS   A CG   1 
ATOM   1807 C  CD   . LYS   A 1 90  ? 31.424 -4.568  18.323  1.00 29.10 ?  90  LYS   A CD   1 
ATOM   1808 C  CE   . LYS   A 1 90  ? 32.832 -4.591  18.903  1.00 33.20 ?  90  LYS   A CE   1 
ATOM   1809 N  NZ   . LYS   A 1 90  ? 33.862 -4.966  17.897  1.00 35.26 ?  90  LYS   A NZ   1 
ATOM   1810 H  H    . LYS   A 1 90  ? 27.466 -2.333  16.556  1.00 18.67 ?  90  LYS   A H    1 
ATOM   1811 H  HA   . LYS   A 1 90  ? 29.720 -1.128  17.110  1.00 19.45 ?  90  LYS   A HA   1 
ATOM   1812 H  HB2  . LYS   A 1 90  ? 29.200 -3.287  17.931  1.00 22.72 ?  90  LYS   A HB2  1 
ATOM   1813 H  HB3  . LYS   A 1 90  ? 29.476 -3.868  16.479  1.00 22.72 ?  90  LYS   A HB3  1 
ATOM   1814 H  HG2  . LYS   A 1 90  ? 31.700 -3.439  16.642  1.00 28.48 ?  90  LYS   A HG2  1 
ATOM   1815 H  HG3  . LYS   A 1 90  ? 31.491 -2.559  17.952  1.00 28.48 ?  90  LYS   A HG3  1 
ATOM   1816 H  HD2  . LYS   A 1 90  ? 30.793 -4.567  19.061  1.00 34.90 ?  90  LYS   A HD2  1 
ATOM   1817 H  HD3  . LYS   A 1 90  ? 31.306 -5.366  17.784  1.00 34.90 ?  90  LYS   A HD3  1 
ATOM   1818 H  HE2  . LYS   A 1 90  ? 33.050 -3.708  19.240  1.00 39.82 ?  90  LYS   A HE2  1 
ATOM   1819 H  HE3  . LYS   A 1 90  ? 32.867 -5.239  19.624  1.00 39.82 ?  90  LYS   A HE3  1 
ATOM   1820 H  HZ1  . LYS   A 1 90  ? 34.668 -4.977  18.276  1.00 42.29 ?  90  LYS   A HZ1  1 
ATOM   1821 H  HZ2  . LYS   A 1 90  ? 33.687 -5.775  17.569  1.00 42.29 ?  90  LYS   A HZ2  1 
ATOM   1822 H  HZ3  . LYS   A 1 90  ? 33.865 -4.378  17.230  1.00 42.29 ?  90  LYS   A HZ3  1 
ATOM   1823 N  N    . HIS   A 1 91  ? 29.617 -2.334  14.144  1.00 13.24 ?  91  HIS   A N    1 
ATOM   1824 C  CA   . HIS   A 1 91  ? 30.198 -2.326  12.816  1.00 12.58 ?  91  HIS   A CA   1 
ATOM   1825 C  C    . HIS   A 1 91  ? 29.117 -2.048  11.788  1.00 11.57 ?  91  HIS   A C    1 
ATOM   1826 O  O    . HIS   A 1 91  ? 27.949 -2.403  11.980  1.00 12.45 ?  91  HIS   A O    1 
ATOM   1827 C  CB   . HIS   A 1 91  ? 30.794 -3.695  12.463  1.00 15.14 ?  91  HIS   A CB   1 
ATOM   1828 C  CG   . HIS   A 1 91  ? 31.784 -4.204  13.460  1.00 19.18 ?  91  HIS   A CG   1 
ATOM   1829 N  ND1  . HIS   A 1 91  ? 33.063 -3.702  13.559  1.00 21.43 ?  91  HIS   A ND1  1 
ATOM   1830 C  CD2  . HIS   A 1 91  ? 31.690 -5.181  14.393  1.00 21.06 ?  91  HIS   A CD2  1 
ATOM   1831 C  CE1  . HIS   A 1 91  ? 33.714 -4.345  14.513  1.00 22.28 ?  91  HIS   A CE1  1 
ATOM   1832 N  NE2  . HIS   A 1 91  ? 32.903 -5.249  15.034  1.00 22.30 ?  91  HIS   A NE2  1 
ATOM   1833 H  H    . HIS   A 1 91  ? 28.927 -2.863  14.208  1.00 15.86 ?  91  HIS   A H    1 
ATOM   1834 H  HA   . HIS   A 1 91  ? 30.887 -1.653  12.756  1.00 15.07 ?  91  HIS   A HA   1 
ATOM   1835 H  HB2  . HIS   A 1 91  ? 30.075 -4.346  12.406  1.00 18.14 ?  91  HIS   A HB2  1 
ATOM   1836 H  HB3  . HIS   A 1 91  ? 31.243 -3.628  11.607  1.00 18.14 ?  91  HIS   A HB3  1 
ATOM   1837 H  HD1  . HIS   A 1 91  ? 33.390 -3.069  13.073  1.00 25.69 ?  91  HIS   A HD1  1 
ATOM   1838 H  HD2  . HIS   A 1 91  ? 30.948 -5.707  14.568  1.00 25.25 ?  91  HIS   A HD2  1 
ATOM   1839 H  HE1  . HIS   A 1 91  ? 34.598 -4.183  14.771  1.00 26.71 ?  91  HIS   A HE1  1 
ATOM   1840 N  N    . CYS   A 1 92  ? 29.529 -1.453  10.674  1.00 11.23 ?  92  CYS   A N    1 
ATOM   1841 C  CA   . CYS   A 1 92  ? 28.699 -1.372  9.480   1.00 11.02 ?  92  CYS   A CA   1 
ATOM   1842 C  C    . CYS   A 1 92  ? 29.349 -2.193  8.375   1.00 10.69 ?  92  CYS   A C    1 
ATOM   1843 O  O    . CYS   A 1 92  ? 30.507 -1.947  8.015   1.00 11.49 ?  92  CYS   A O    1 
ATOM   1844 C  CB   . CYS   A 1 92  ? 28.492 0.071   9.018   1.00 11.39 ?  92  CYS   A CB   1 
ATOM   1845 S  SG   . CYS   A 1 92  ? 27.479 0.179   7.508   1.00 10.94 ?  92  CYS   A SG   1 
ATOM   1846 H  H    . CYS   A 1 92  ? 30.304 -1.081  10.584  1.00 13.46 ?  92  CYS   A H    1 
ATOM   1847 H  HA   . CYS   A 1 92  ? 27.833 -1.752  9.670   1.00 13.20 ?  92  CYS   A HA   1 
ATOM   1848 H  HB2  . CYS   A 1 92  ? 28.039 0.569   9.717   1.00 13.64 ?  92  CYS   A HB2  1 
ATOM   1849 H  HB3  . CYS   A 1 92  ? 29.354 0.474   8.827   1.00 13.64 ?  92  CYS   A HB3  1 
ATOM   1850 H  HG   . CYS   A 1 92  ? 27.342 1.330   7.212   1.00 13.10 ?  92  CYS   A HG   1 
ATOM   1851 N  N    . LEU   A 1 93  ? 28.614 -3.183  7.869   1.00 10.38 ?  93  LEU   A N    1 
ATOM   1852 C  CA   . LEU   A 1 93  ? 29.019 -3.937  6.691   1.00 9.86  ?  93  LEU   A CA   1 
ATOM   1853 C  C    . LEU   A 1 93  ? 28.424 -3.242  5.473   1.00 9.53  ?  93  LEU   A C    1 
ATOM   1854 O  O    . LEU   A 1 93  ? 27.210 -3.301  5.242   1.00 9.96  ?  93  LEU   A O    1 
ATOM   1855 C  CB   . LEU   A 1 93  ? 28.539 -5.383  6.796   1.00 10.79 ?  93  LEU   A CB   1 
ATOM   1856 C  CG   . LEU   A 1 93  ? 28.922 -6.286  5.623   1.00 11.07 ?  93  LEU   A CG   1 
ATOM   1857 C  CD1  . LEU   A 1 93  ? 30.425 -6.552  5.605   1.00 11.97 ?  93  LEU   A CD1  1 
ATOM   1858 C  CD2  . LEU   A 1 93  ? 28.145 -7.605  5.657   1.00 11.88 ?  93  LEU   A CD2  1 
ATOM   1859 H  H    . LEU   A 1 93  ? 27.859 -3.436  8.203   1.00 12.43 ?  93  LEU   A H    1 
ATOM   1860 H  HA   . LEU   A 1 93  ? 29.982 -3.927  6.619   1.00 11.81 ?  93  LEU   A HA   1 
ATOM   1861 H  HB2  . LEU   A 1 93  ? 28.921 -5.772  7.602   1.00 12.92 ?  93  LEU   A HB2  1 
ATOM   1862 H  HB3  . LEU   A 1 93  ? 27.575 -5.386  6.862   1.00 12.92 ?  93  LEU   A HB3  1 
ATOM   1863 H  HG   . LEU   A 1 93  ? 28.703 -5.835  4.800   1.00 13.26 ?  93  LEU   A HG   1 
ATOM   1864 H  HD11 . LEU   A 1 93  ? 30.632 -7.161  4.877   1.00 14.35 ?  93  LEU   A HD11 1 
ATOM   1865 H  HD12 . LEU   A 1 93  ? 30.900 -5.718  5.485   1.00 14.35 ?  93  LEU   A HD12 1 
ATOM   1866 H  HD13 . LEU   A 1 93  ? 30.688 -6.961  6.452   1.00 14.35 ?  93  LEU   A HD13 1 
ATOM   1867 H  HD21 . LEU   A 1 93  ? 28.418 -8.151  4.899   1.00 14.24 ?  93  LEU   A HD21 1 
ATOM   1868 H  HD22 . LEU   A 1 93  ? 28.341 -8.073  6.484   1.00 14.24 ?  93  LEU   A HD22 1 
ATOM   1869 H  HD23 . LEU   A 1 93  ? 27.197 -7.415  5.599   1.00 14.24 ?  93  LEU   A HD23 1 
ATOM   1870 N  N    . HIS   A 1 94  ? 29.274 -2.551  4.717   1.00 9.70  ?  94  HIS   A N    1 
ATOM   1871 C  CA   . HIS   A 1 94  ? 28.858 -1.882  3.488   1.00 9.63  ?  94  HIS   A CA   1 
ATOM   1872 C  C    . HIS   A 1 94  ? 28.866 -2.917  2.377   1.00 9.73  ?  94  HIS   A C    1 
ATOM   1873 O  O    . HIS   A 1 94  ? 29.932 -3.433  2.031   1.00 11.09 ?  94  HIS   A O    1 
ATOM   1874 C  CB   . HIS   A 1 94  ? 29.822 -0.742  3.159   1.00 9.72  ?  94  HIS   A CB   1 
ATOM   1875 C  CG   . HIS   A 1 94  ? 29.806 0.354   4.170   1.00 9.47  ?  94  HIS   A CG   1 
ATOM   1876 N  ND1  . HIS   A 1 94  ? 28.929 1.416   4.111   1.00 9.88  ?  94  HIS   A ND1  1 
ATOM   1877 C  CD2  . HIS   A 1 94  ? 30.541 0.522   5.292   1.00 10.26 ?  94  HIS   A CD2  1 
ATOM   1878 C  CE1  . HIS   A 1 94  ? 29.140 2.196   5.156   1.00 10.09 ?  94  HIS   A CE1  1 
ATOM   1879 N  NE2  . HIS   A 1 94  ? 30.115 1.679   5.885   1.00 10.49 ?  94  HIS   A NE2  1 
ATOM   1880 H  H    . HIS   A 1 94  ? 30.110 -2.447  4.900   1.00 11.61 ?  94  HIS   A H    1 
ATOM   1881 H  HA   . HIS   A 1 94  ? 27.958 -1.525  3.588   1.00 11.54 ?  94  HIS   A HA   1 
ATOM   1882 H  HB2  . HIS   A 1 94  ? 30.718 -1.096  3.115   1.00 11.64 ?  94  HIS   A HB2  1 
ATOM   1883 H  HB3  . HIS   A 1 94  ? 29.569 -0.359  2.303   1.00 11.64 ?  94  HIS   A HB3  1 
ATOM   1884 H  HD2  . HIS   A 1 94  ? 31.217 -0.031  5.601   1.00 12.30 ?  94  HIS   A HD2  1 
ATOM   1885 H  HE1  . HIS   A 1 94  ? 28.672 2.984   5.341   1.00 12.08 ?  94  HIS   A HE1  1 
ATOM   1886 H  HE2  . HIS   A 1 94  ? 30.424 2.025   6.609   1.00 12.56 ?  94  HIS   A HE2  1 
ATOM   1887 N  N    . VAL   A 1 95  ? 27.693 -3.241  1.831   1.00 9.21  ?  95  VAL   A N    1 
ATOM   1888 C  CA   . VAL   A 1 95  ? 27.554 -4.277  0.811   1.00 9.56  ?  95  VAL   A CA   1 
ATOM   1889 C  C    . VAL   A 1 95  ? 27.012 -3.643  -0.457  1.00 9.28  ?  95  VAL   A C    1 
ATOM   1890 O  O    . VAL   A 1 95  ? 26.010 -2.920  -0.408  1.00 10.05 ?  95  VAL   A O    1 
ATOM   1891 C  CB   . VAL   A 1 95  ? 26.622 -5.414  1.263   1.00 9.93  ?  95  VAL   A CB   1 
ATOM   1892 C  CG1  . VAL   A 1 95  ? 26.517 -6.456  0.161   1.00 10.81 ?  95  VAL   A CG1  1 
ATOM   1893 C  CG2  . VAL   A 1 95  ? 27.121 -6.031  2.553   1.00 10.19 ?  95  VAL   A CG2  1 
ATOM   1894 H  H    . VAL   A 1 95  ? 26.943 -2.873  2.046   1.00 11.03 ?  95  VAL   A H    1 
ATOM   1895 H  HA   . VAL   A 1 95  ? 28.422 -4.656  0.615   1.00 11.45 ?  95  VAL   A HA   1 
ATOM   1896 H  HB   . VAL   A 1 95  ? 25.735 -5.059  1.422   1.00 11.90 ?  95  VAL   A HB   1 
ATOM   1897 H  HG11 . VAL   A 1 95  ? 26.135 -7.271  0.527   1.00 12.94 ?  95  VAL   A HG11 1 
ATOM   1898 H  HG12 . VAL   A 1 95  ? 25.951 -6.120  -0.550  1.00 12.94 ?  95  VAL   A HG12 1 
ATOM   1899 H  HG13 . VAL   A 1 95  ? 27.407 -6.643  -0.186  1.00 12.94 ?  95  VAL   A HG13 1 
ATOM   1900 H  HG21 . VAL   A 1 95  ? 26.560 -6.792  2.775   1.00 12.21 ?  95  VAL   A HG21 1 
ATOM   1901 H  HG22 . VAL   A 1 95  ? 28.037 -6.318  2.433   1.00 12.21 ?  95  VAL   A HG22 1 
ATOM   1902 H  HG23 . VAL   A 1 95  ? 27.068 -5.367  3.258   1.00 12.21 ?  95  VAL   A HG23 1 
ATOM   1903 N  N    . VAL   A 1 96  ? 27.642 -3.938  -1.593  1.00 9.36  ?  96  VAL   A N    1 
ATOM   1904 C  CA   . VAL   A 1 96  ? 27.236 -3.381  -2.877  1.00 9.92  ?  96  VAL   A CA   1 
ATOM   1905 C  C    . VAL   A 1 96  ? 26.432 -4.429  -3.639  1.00 10.34 ?  96  VAL   A C    1 
ATOM   1906 O  O    . VAL   A 1 96  ? 26.990 -5.375  -4.200  1.00 11.20 ?  96  VAL   A O    1 
ATOM   1907 C  CB   . VAL   A 1 96  ? 28.427 -2.902  -3.702  1.00 10.33 ?  96  VAL   A CB   1 
ATOM   1908 C  CG1  . VAL   A 1 96  ? 27.922 -2.267  -4.982  1.00 10.68 ?  96  VAL   A CG1  1 
ATOM   1909 C  CG2  . VAL   A 1 96  ? 29.285 -1.933  -2.909  1.00 10.71 ?  96  VAL   A CG2  1 
ATOM   1910 H  H    . VAL   A 1 96  ? 28.327 -4.462  -1.644  1.00 11.21 ?  96  VAL   A H    1 
ATOM   1911 H  HA   . VAL   A 1 96  ? 26.661 -2.619  -2.719  1.00 11.88 ?  96  VAL   A HA   1 
ATOM   1912 H  HB   . VAL   A 1 96  ? 28.979 -3.658  -3.940  1.00 12.38 ?  96  VAL   A HB   1 
ATOM   1913 H  HG11 . VAL   A 1 96  ? 28.658 -1.784  -5.398  1.00 12.79 ?  96  VAL   A HG11 1 
ATOM   1914 H  HG12 . VAL   A 1 96  ? 27.606 -2.959  -5.575  1.00 12.79 ?  96  VAL   A HG12 1 
ATOM   1915 H  HG13 . VAL   A 1 96  ? 27.208 -1.649  -4.767  1.00 12.79 ?  96  VAL   A HG13 1 
ATOM   1916 H  HG21 . VAL   A 1 96  ? 29.988 -1.585  -3.478  1.00 12.83 ?  96  VAL   A HG21 1 
ATOM   1917 H  HG22 . VAL   A 1 96  ? 28.728 -1.199  -2.591  1.00 12.83 ?  96  VAL   A HG22 1 
ATOM   1918 H  HG23 . VAL   A 1 96  ? 29.673 -2.397  -2.150  1.00 12.83 ?  96  VAL   A HG23 1 
ATOM   1919 N  N    A GLY   A 1 97  ? 25.112 -4.275  -3.662  0.72 10.48 ?  97  GLY   A N    1 
ATOM   1920 N  N    B GLY   A 1 97  ? 25.114 -4.249  -3.681  0.28 10.49 ?  97  GLY   A N    1 
ATOM   1921 C  CA   A GLY   A 1 97  ? 24.297 -5.031  -4.579  0.72 11.03 ?  97  GLY   A CA   1 
ATOM   1922 C  CA   B GLY   A 1 97  ? 24.277 -5.026  -4.561  0.28 10.81 ?  97  GLY   A CA   1 
ATOM   1923 C  C    A GLY   A 1 97  ? 24.308 -4.354  -5.937  0.72 11.04 ?  97  GLY   A C    1 
ATOM   1924 C  C    B GLY   A 1 97  ? 24.276 -4.431  -5.956  0.28 11.06 ?  97  GLY   A C    1 
ATOM   1925 O  O    A GLY   A 1 97  ? 24.615 -3.163  -6.051  0.72 11.91 ?  97  GLY   A O    1 
ATOM   1926 O  O    B GLY   A 1 97  ? 24.529 -3.236  -6.143  0.28 11.29 ?  97  GLY   A O    1 
ATOM   1927 H  H    A GLY   A 1 97  ? 24.673 -3.735  -3.152  0.72 12.55 ?  97  GLY   A H    1 
ATOM   1928 H  H    B GLY   A 1 97  ? 24.685 -3.675  -3.200  0.28 12.57 ?  97  GLY   A H    1 
ATOM   1929 H  HA2  A GLY   A 1 97  ? 24.653 -5.930  -4.660  0.72 13.22 ?  97  GLY   A HA2  1 
ATOM   1930 H  HA2  B GLY   A 1 97  ? 24.615 -5.934  -4.603  0.28 12.96 ?  97  GLY   A HA2  1 
ATOM   1931 H  HA3  A GLY   A 1 97  ? 23.388 -5.082  -4.244  0.72 13.22 ?  97  GLY   A HA3  1 
ATOM   1932 H  HA3  B GLY   A 1 97  ? 23.369 -5.044  -4.220  0.28 12.96 ?  97  GLY   A HA3  1 
ATOM   1933 N  N    A PRO   A 1 98  ? 23.975 -5.091  -6.994  0.72 10.86 ?  98  PRO   A N    1 
ATOM   1934 N  N    B PRO   A 1 98  ? 23.985 -5.247  -6.966  0.28 11.30 ?  98  PRO   A N    1 
ATOM   1935 C  CA   A PRO   A 1 98  ? 23.845 -4.455  -8.309  0.72 11.82 ?  98  PRO   A CA   1 
ATOM   1936 C  CA   B PRO   A 1 98  ? 23.989 -4.737  -8.342  0.28 11.80 ?  98  PRO   A CA   1 
ATOM   1937 C  C    A PRO   A 1 98  ? 22.719 -3.427  -8.324  0.72 11.66 ?  98  PRO   A C    1 
ATOM   1938 C  C    B PRO   A 1 98  ? 22.890 -3.707  -8.560  0.28 12.07 ?  98  PRO   A C    1 
ATOM   1939 O  O    A PRO   A 1 98  ? 21.658 -3.623  -7.725  0.72 11.19 ?  98  PRO   A O    1 
ATOM   1940 O  O    B PRO   A 1 98  ? 21.754 -3.870  -8.109  0.28 12.45 ?  98  PRO   A O    1 
ATOM   1941 C  CB   A PRO   A 1 98  ? 23.544 -5.633  -9.242  0.72 12.05 ?  98  PRO   A CB   1 
ATOM   1942 C  CB   B PRO   A 1 98  ? 23.747 -5.995  -9.184  0.28 11.48 ?  98  PRO   A CB   1 
ATOM   1943 C  CG   A PRO   A 1 98  ? 22.941 -6.676  -8.353  0.72 12.36 ?  98  PRO   A CG   1 
ATOM   1944 C  CG   B PRO   A 1 98  ? 23.004 -6.915  -8.270  0.28 11.62 ?  98  PRO   A CG   1 
ATOM   1945 C  CD   A PRO   A 1 98  ? 23.694 -6.538  -7.049  0.72 11.42 ?  98  PRO   A CD   1 
ATOM   1946 C  CD   B PRO   A 1 98  ? 23.583 -6.664  -6.902  0.28 11.16 ?  98  PRO   A CD   1 
ATOM   1947 H  HA   A PRO   A 1 98  ? 24.681 -4.039  -8.559  0.72 14.16 ?  98  PRO   A HA   1 
ATOM   1948 H  HA   B PRO   A 1 98  ? 24.852 -4.351  -8.566  0.28 14.13 ?  98  PRO   A HA   1 
ATOM   1949 H  HB2  A PRO   A 1 98  ? 22.913 -5.355  -9.922  0.72 14.44 ?  98  PRO   A HB2  1 
ATOM   1950 H  HB2  B PRO   A 1 98  ? 23.212 -5.772  -9.962  0.28 13.75 ?  98  PRO   A HB2  1 
ATOM   1951 H  HB3  A PRO   A 1 98  ? 24.367 -5.954  -9.641  0.72 14.44 ?  98  PRO   A HB3  1 
ATOM   1952 H  HB3  B PRO   A 1 98  ? 24.597 -6.384  -9.448  0.28 13.75 ?  98  PRO   A HB3  1 
ATOM   1953 H  HG2  A PRO   A 1 98  ? 21.997 -6.495  -8.224  0.72 14.81 ?  98  PRO   A HG2  1 
ATOM   1954 H  HG2  B PRO   A 1 98  ? 22.059 -6.694  -8.289  0.28 13.92 ?  98  PRO   A HG2  1 
ATOM   1955 H  HG3  A PRO   A 1 98  ? 23.077 -7.555  -8.737  0.72 14.81 ?  98  PRO   A HG3  1 
ATOM   1956 H  HG3  B PRO   A 1 98  ? 23.149 -7.832  -8.542  0.28 13.92 ?  98  PRO   A HG3  1 
ATOM   1957 H  HD2  A PRO   A 1 98  ? 23.135 -6.816  -6.301  0.72 13.68 ?  98  PRO   A HD2  1 
ATOM   1958 H  HD2  B PRO   A 1 98  ? 22.906 -6.793  -6.218  0.28 13.37 ?  98  PRO   A HD2  1 
ATOM   1959 H  HD3  A PRO   A 1 98  ? 24.523 -7.045  -7.076  0.72 13.68 ?  98  PRO   A HD3  1 
ATOM   1960 H  HD3  B PRO   A 1 98  ? 24.356 -7.230  -6.750  0.28 13.37 ?  98  PRO   A HD3  1 
ATOM   1961 N  N    A ASN   A 1 99  ? 22.968 -2.316  -9.015  0.72 12.49 ?  99  ASN   A N    1 
ATOM   1962 N  N    B ASN   A 1 99  ? 23.243 -2.634  -9.261  0.28 12.13 ?  99  ASN   A N    1 
ATOM   1963 C  CA   A ASN   A 1 99  ? 21.984 -1.254  -9.207  0.72 13.39 ?  99  ASN   A CA   1 
ATOM   1964 C  CA   B ASN   A 1 99  ? 22.300 -1.575  -9.604  0.28 12.31 ?  99  ASN   A CA   1 
ATOM   1965 C  C    A ASN   A 1 99  ? 21.427 -1.380  -10.621 0.72 14.55 ?  99  ASN   A C    1 
ATOM   1966 C  C    B ASN   A 1 99  ? 21.709 -1.897  -10.970 0.28 12.51 ?  99  ASN   A C    1 
ATOM   1967 O  O    A ASN   A 1 99  ? 22.107 -1.045  -11.601 0.72 15.41 ?  99  ASN   A O    1 
ATOM   1968 O  O    B ASN   A 1 99  ? 22.397 -1.813  -11.994 0.28 12.37 ?  99  ASN   A O    1 
ATOM   1969 C  CB   A ASN   A 1 99  ? 22.628 0.116   -8.988  0.72 13.47 ?  99  ASN   A CB   1 
ATOM   1970 C  CB   B ASN   A 1 99  ? 23.003 -0.221  -9.623  0.28 13.08 ?  99  ASN   A CB   1 
ATOM   1971 C  CG   A ASN   A 1 99  ? 21.615 1.256   -8.998  0.72 13.37 ?  99  ASN   A CG   1 
ATOM   1972 C  CG   B ASN   A 1 99  ? 22.046 0.931   -9.863  0.28 14.24 ?  99  ASN   A CG   1 
ATOM   1973 O  OD1  A ASN   A 1 99  ? 20.618 1.210   -9.717  0.72 13.99 ?  99  ASN   A OD1  1 
ATOM   1974 O  OD1  B ASN   A 1 99  ? 20.995 0.762   -10.481 0.28 14.26 ?  99  ASN   A OD1  1 
ATOM   1975 N  ND2  A ASN   A 1 99  ? 21.871 2.280   -8.192  0.72 13.81 ?  99  ASN   A ND2  1 
ATOM   1976 N  ND2  B ASN   A 1 99  ? 22.411 2.116   -9.378  0.28 15.32 ?  99  ASN   A ND2  1 
ATOM   1977 H  H    A ASN   A 1 99  ? 23.728 -2.149  -9.378  0.72 14.97 ?  99  ASN   A H    1 
ATOM   1978 H  H    B ASN   A 1 99  ? 24.035 -2.492  -9.553  0.28 14.54 ?  99  ASN   A H    1 
ATOM   1979 H  HA   A ASN   A 1 99  ? 21.257 -1.367  -8.563  0.72 16.04 ?  99  ASN   A HA   1 
ATOM   1980 H  HA   B ASN   A 1 99  ? 21.579 -1.548  -8.948  0.28 14.75 ?  99  ASN   A HA   1 
ATOM   1981 H  HB2  A ASN   A 1 99  ? 23.082 0.120   -8.131  0.72 16.14 ?  99  ASN   A HB2  1 
ATOM   1982 H  HB2  B ASN   A 1 99  ? 23.436 -0.081  -8.768  0.28 15.67 ?  99  ASN   A HB2  1 
ATOM   1983 H  HB3  A ASN   A 1 99  ? 23.263 0.274   -9.702  0.72 16.14 ?  99  ASN   A HB3  1 
ATOM   1984 H  HB3  B ASN   A 1 99  ? 23.655 -0.218  -10.336 0.28 15.67 ?  99  ASN   A HB3  1 
ATOM   1985 H  HD21 A ASN   A 1 99  ? 21.332 2.949   -8.159  0.72 16.55 ?  99  ASN   A HD21 1 
ATOM   1986 H  HD21 B ASN   A 1 99  ? 21.905 2.806   -9.484  0.28 18.36 ?  99  ASN   A HD21 1 
ATOM   1987 H  HD22 A ASN   A 1 99  ? 22.581 2.277   -7.705  0.72 16.55 ?  99  ASN   A HD22 1 
ATOM   1988 H  HD22 B ASN   A 1 99  ? 23.157 2.196   -8.957  0.28 18.36 ?  99  ASN   A HD22 1 
ATOM   1989 N  N    A VAL   A 1 100 ? 20.185 -1.866  -10.716 0.72 15.53 ?  100 VAL   A N    1 
ATOM   1990 N  N    B VAL   A 1 100 ? 20.427 -2.254  -10.977 0.28 13.85 ?  100 VAL   A N    1 
ATOM   1991 C  CA   A VAL   A 1 100 ? 19.556 -2.079  -12.016 0.72 16.80 ?  100 VAL   A CA   1 
ATOM   1992 C  CA   B VAL   A 1 100 ? 19.763 -2.661  -12.210 0.28 15.99 ?  100 VAL   A CA   1 
ATOM   1993 C  C    A VAL   A 1 100 ? 19.436 -0.770  -12.781 0.72 16.89 ?  100 VAL   A C    1 
ATOM   1994 C  C    B VAL   A 1 100 ? 19.662 -1.496  -13.177 0.28 16.40 ?  100 VAL   A C    1 
ATOM   1995 O  O    A VAL   A 1 100 ? 19.513 -0.752  -14.015 0.72 17.85 ?  100 VAL   A O    1 
ATOM   1996 O  O    B VAL   A 1 100 ? 19.704 -1.691  -14.398 0.28 16.34 ?  100 VAL   A O    1 
ATOM   1997 C  CB   A VAL   A 1 100 ? 18.198 -2.796  -11.840 0.72 18.19 ?  100 VAL   A CB   1 
ATOM   1998 C  CB   B VAL   A 1 100 ? 18.376 -3.248  -11.901 0.28 17.90 ?  100 VAL   A CB   1 
ATOM   1999 C  CG1  A VAL   A 1 100 ? 17.487 -2.963  -13.176 0.72 18.67 ?  100 VAL   A CG1  1 
ATOM   2000 C  CG1  B VAL   A 1 100 ? 18.061 -4.370  -12.867 0.28 18.57 ?  100 VAL   A CG1  1 
ATOM   2001 C  CG2  A VAL   A 1 100 ? 18.409 -4.155  -11.184 0.72 18.47 ?  100 VAL   A CG2  1 
ATOM   2002 C  CG2  B VAL   A 1 100 ? 18.321 -3.729  -10.467 0.28 18.53 ?  100 VAL   A CG2  1 
ATOM   2003 H  H    A VAL   A 1 100 ? 19.684 -2.080  -10.042 0.72 18.61 ?  100 VAL   A H    1 
ATOM   2004 H  H    B VAL   A 1 100 ? 19.936 -2.251  -10.275 0.28 16.60 ?  100 VAL   A H    1 
ATOM   2005 H  HA   A VAL   A 1 100 ? 20.120 -2.667  -12.536 0.72 20.14 ?  100 VAL   A HA   1 
ATOM   2006 H  HA   B VAL   A 1 100 ? 20.285 -3.349  -12.648 0.28 19.17 ?  100 VAL   A HA   1 
ATOM   2007 H  HB   A VAL   A 1 100 ? 17.627 -2.270  -11.261 0.72 21.81 ?  100 VAL   A HB   1 
ATOM   2008 H  HB   B VAL   A 1 100 ? 17.704 -2.554  -12.020 0.28 21.46 ?  100 VAL   A HB   1 
ATOM   2009 H  HG11 A VAL   A 1 100 ? 16.735 -3.569  -13.062 0.72 22.38 ?  100 VAL   A HG11 1 
ATOM   2010 H  HG11 B VAL   A 1 100 ? 17.168 -4.698  -12.683 0.28 22.27 ?  100 VAL   A HG11 1 
ATOM   2011 H  HG12 A VAL   A 1 100 ? 17.168 -2.099  -13.479 0.72 22.38 ?  100 VAL   A HG12 1 
ATOM   2012 H  HG12 B VAL   A 1 100 ? 18.113 -4.033  -13.774 0.28 22.27 ?  100 VAL   A HG12 1 
ATOM   2013 H  HG13 A VAL   A 1 100 ? 18.109 -3.333  -13.823 0.72 22.38 ?  100 VAL   A HG13 1 
ATOM   2014 H  HG13 B VAL   A 1 100 ? 18.709 -5.081  -12.739 0.28 22.27 ?  100 VAL   A HG13 1 
ATOM   2015 H  HG21 A VAL   A 1 100 ? 17.560 -4.622  -11.141 0.72 22.14 ?  100 VAL   A HG21 1 
ATOM   2016 H  HG21 B VAL   A 1 100 ? 17.578 -4.324  -10.376 0.28 22.21 ?  100 VAL   A HG21 1 
ATOM   2017 H  HG22 A VAL   A 1 100 ? 19.040 -4.667  -11.714 0.72 22.14 ?  100 VAL   A HG22 1 
ATOM   2018 H  HG22 B VAL   A 1 100 ? 19.150 -4.193  -10.255 0.28 22.21 ?  100 VAL   A HG22 1 
ATOM   2019 H  HG23 A VAL   A 1 100 ? 18.759 -4.023  -10.289 0.72 22.14 ?  100 VAL   A HG23 1 
ATOM   2020 H  HG23 B VAL   A 1 100 ? 18.208 -2.961  -9.880  0.28 22.21 ?  100 VAL   A HG23 1 
ATOM   2021 N  N    A ASN   A 1 101 ? 19.262 0.344   -12.077 0.72 17.77 ?  101 ASN   A N    1 
ATOM   2022 N  N    B ASN   A 1 101 ? 19.511 -0.272  -12.658 0.28 17.24 ?  101 ASN   A N    1 
ATOM   2023 C  CA   A ASN   A 1 101 ? 19.191 1.629   -12.758 0.72 18.95 ?  101 ASN   A CA   1 
ATOM   2024 C  CA   B ASN   A 1 101 ? 19.430 0.895   -13.529 0.28 18.13 ?  101 ASN   A CA   1 
ATOM   2025 C  C    A ASN   A 1 101 ? 20.543 2.085   -13.307 0.72 21.07 ?  101 ASN   A C    1 
ATOM   2026 C  C    B ASN   A 1 101 ? 20.744 1.134   -14.260 0.28 19.20 ?  101 ASN   A C    1 
ATOM   2027 O  O    A ASN   A 1 101 ? 20.603 3.145   -13.943 0.72 22.80 ?  101 ASN   A O    1 
ATOM   2028 O  O    B ASN   A 1 101 ? 20.747 1.706   -15.356 0.28 19.39 ?  101 ASN   A O    1 
ATOM   2029 C  CB   A ASN   A 1 101 ? 18.555 2.663   -11.828 0.72 18.66 ?  101 ASN   A CB   1 
ATOM   2030 C  CB   B ASN   A 1 101 ? 19.020 2.127   -12.718 0.28 18.07 ?  101 ASN   A CB   1 
ATOM   2031 C  CG   A ASN   A 1 101 ? 17.173 2.228   -11.352 0.72 18.51 ?  101 ASN   A CG   1 
ATOM   2032 C  CG   B ASN   A 1 101 ? 17.786 1.879   -11.866 0.28 18.37 ?  101 ASN   A CG   1 
ATOM   2033 O  OD1  A ASN   A 1 101 ? 16.364 1.726   -12.137 0.72 18.72 ?  101 ASN   A OD1  1 
ATOM   2034 O  OD1  B ASN   A 1 101 ? 16.842 1.215   -12.296 0.28 18.76 ?  101 ASN   A OD1  1 
ATOM   2035 N  ND2  A ASN   A 1 101 ? 16.909 2.391   -10.061 0.72 18.50 ?  101 ASN   A ND2  1 
ATOM   2036 N  ND2  B ASN   A 1 101 ? 17.795 2.404   -10.647 0.28 18.57 ?  101 ASN   A ND2  1 
ATOM   2037 H  H    A ASN   A 1 101 ? 19.173 0.380   -11.225 0.72 21.31 ?  101 ASN   A H    1 
ATOM   2038 H  H    B ASN   A 1 101 ? 19.454 -0.090  -11.816 0.28 20.67 ?  101 ASN   A H    1 
ATOM   2039 H  HA   A ASN   A 1 101 ? 18.603 1.533   -13.520 0.72 22.72 ?  101 ASN   A HA   1 
ATOM   2040 H  HA   B ASN   A 1 101 ? 18.746 0.750   -14.196 0.28 21.74 ?  101 ASN   A HA   1 
ATOM   2041 H  HB2  A ASN   A 1 101 ? 19.121 2.788   -11.052 0.72 22.37 ?  101 ASN   A HB2  1 
ATOM   2042 H  HB2  B ASN   A 1 101 ? 19.743 2.383   -12.124 0.28 21.66 ?  101 ASN   A HB2  1 
ATOM   2043 H  HB3  A ASN   A 1 101 ? 18.460 3.503   -12.309 0.72 22.37 ?  101 ASN   A HB3  1 
ATOM   2044 H  HB3  B ASN   A 1 101 ? 18.820 2.864   -13.325 0.28 21.66 ?  101 ASN   A HB3  1 
ATOM   2045 H  HD21 A ASN   A 1 101 ? 16.144 2.160   -9.746  0.72 22.18 ?  101 ASN   A HD21 1 
ATOM   2046 H  HD21 B ASN   A 1 101 ? 17.118 2.295   -10.127 0.28 22.26 ?  101 ASN   A HD21 1 
ATOM   2047 H  HD22 A ASN   A 1 101 ? 17.499 2.741   -9.542  0.72 22.18 ?  101 ASN   A HD22 1 
ATOM   2048 H  HD22 B ASN   A 1 101 ? 18.473 2.862   -10.380 0.28 22.26 ?  101 ASN   A HD22 1 
ATOM   2049 N  N    A LYS   A 1 102 ? 21.607 1.298   -13.099 0.72 22.60 ?  102 LYS   A N    1 
ATOM   2050 N  N    B LYS   A 1 102 ? 21.862 0.705   -13.675 0.28 20.38 ?  102 LYS   A N    1 
ATOM   2051 C  CA   A LYS   A 1 102 ? 22.901 1.501   -13.739 0.72 23.93 ?  102 LYS   A CA   1 
ATOM   2052 C  CA   B LYS   A 1 102 ? 23.156 0.754   -14.342 0.28 21.14 ?  102 LYS   A CA   1 
ATOM   2053 C  C    A LYS   A 1 102 ? 23.238 0.417   -14.753 0.72 24.66 ?  102 LYS   A C    1 
ATOM   2054 C  C    B LYS   A 1 102 ? 23.403 -0.458  -15.232 0.28 20.59 ?  102 LYS   A C    1 
ATOM   2055 O  O    A LYS   A 1 102 ? 24.316 0.468   -15.350 0.72 25.12 ?  102 LYS   A O    1 
ATOM   2056 O  O    B LYS   A 1 102 ? 24.505 -0.595  -15.773 0.28 20.20 ?  102 LYS   A O    1 
ATOM   2057 C  CB   A LYS   A 1 102 ? 24.023 1.544   -12.694 0.72 24.95 ?  102 LYS   A CB   1 
ATOM   2058 C  CB   B LYS   A 1 102 ? 24.288 0.833   -13.314 0.28 22.61 ?  102 LYS   A CB   1 
ATOM   2059 C  CG   A LYS   A 1 102 ? 23.923 2.671   -11.693 0.72 25.63 ?  102 LYS   A CG   1 
ATOM   2060 C  CG   B LYS   A 1 102 ? 24.490 2.194   -12.674 0.28 23.97 ?  102 LYS   A CG   1 
ATOM   2061 C  CD   A LYS   A 1 102 ? 25.093 2.622   -10.721 0.72 26.63 ?  102 LYS   A CD   1 
ATOM   2062 C  CD   B LYS   A 1 102 ? 25.975 2.493   -12.503 0.28 25.33 ?  102 LYS   A CD   1 
ATOM   2063 C  CE   A LYS   A 1 102 ? 25.018 3.737   -9.694  0.72 27.66 ?  102 LYS   A CE   1 
ATOM   2064 C  CE   B LYS   A 1 102 ? 26.257 3.216   -11.198 0.28 26.32 ?  102 LYS   A CE   1 
ATOM   2065 N  NZ   A LYS   A 1 102 ? 26.111 3.632   -8.687  0.72 28.09 ?  102 LYS   A NZ   1 
ATOM   2066 N  NZ   B LYS   A 1 102 ? 27.292 4.273   -11.359 0.28 26.82 ?  102 LYS   A NZ   1 
ATOM   2067 H  H    A LYS   A 1 102 ? 21.600 0.606   -12.584 0.72 27.10 ?  102 LYS   A H    1 
ATOM   2068 H  H    B LYS   A 1 102 ? 21.890 0.377   -12.881 0.28 24.44 ?  102 LYS   A H    1 
ATOM   2069 H  HA   A LYS   A 1 102 ? 22.895 2.345   -14.208 0.72 28.70 ?  102 LYS   A HA   1 
ATOM   2070 H  HA   B LYS   A 1 102 ? 23.197 1.558   -14.885 0.28 25.35 ?  102 LYS   A HA   1 
ATOM   2071 H  HB2  A LYS   A 1 102 ? 24.016 0.709   -12.202 0.72 29.92 ?  102 LYS   A HB2  1 
ATOM   2072 H  HB2  B LYS   A 1 102 ? 24.104 0.205   -12.600 0.28 27.11 ?  102 LYS   A HB2  1 
ATOM   2073 H  HB3  A LYS   A 1 102 ? 24.871 1.637   -13.159 0.72 29.92 ?  102 LYS   A HB3  1 
ATOM   2074 H  HB3  B LYS   A 1 102 ? 25.116 0.590   -13.756 0.28 27.11 ?  102 LYS   A HB3  1 
ATOM   2075 H  HG2  A LYS   A 1 102 ? 23.945 3.520   -12.162 0.72 30.74 ?  102 LYS   A HG2  1 
ATOM   2076 H  HG2  B LYS   A 1 102 ? 24.104 2.882   -13.240 0.28 28.74 ?  102 LYS   A HG2  1 
ATOM   2077 H  HG3  A LYS   A 1 102 ? 23.099 2.581   -11.191 0.72 30.74 ?  102 LYS   A HG3  1 
ATOM   2078 H  HG3  B LYS   A 1 102 ? 24.071 2.204   -11.799 0.28 28.74 ?  102 LYS   A HG3  1 
ATOM   2079 H  HD2  A LYS   A 1 102 ? 25.081 1.773   -10.251 0.72 31.94 ?  102 LYS   A HD2  1 
ATOM   2080 H  HD2  B LYS   A 1 102 ? 26.476 1.661   -12.499 0.28 30.37 ?  102 LYS   A HD2  1 
ATOM   2081 H  HD3  A LYS   A 1 102 ? 25.922 2.719   -11.216 0.72 31.94 ?  102 LYS   A HD3  1 
ATOM   2082 H  HD3  B LYS   A 1 102 ? 26.274 3.058   -13.234 0.28 30.37 ?  102 LYS   A HD3  1 
ATOM   2083 H  HE2  A LYS   A 1 102 ? 25.100 4.592   -10.146 0.72 33.17 ?  102 LYS   A HE2  1 
ATOM   2084 H  HE2  B LYS   A 1 102 ? 25.444 3.634   -10.880 0.28 31.56 ?  102 LYS   A HE2  1 
ATOM   2085 H  HE3  A LYS   A 1 102 ? 24.168 3.685   -9.229  0.72 33.17 ?  102 LYS   A HE3  1 
ATOM   2086 H  HE3  B LYS   A 1 102 ? 26.579 2.572   -10.544 0.28 31.56 ?  102 LYS   A HE3  1 
ATOM   2087 H  HZ1  A LYS   A 1 102 ? 26.046 4.295   -8.098  0.72 33.69 ?  102 LYS   A HZ1  1 
ATOM   2088 H  HZ1  B LYS   A 1 102 ? 27.435 4.677   -10.579 0.28 32.16 ?  102 LYS   A HZ1  1 
ATOM   2089 H  HZ2  A LYS   A 1 102 ? 26.054 2.855   -8.257  0.72 33.69 ?  102 LYS   A HZ2  1 
ATOM   2090 H  HZ2  B LYS   A 1 102 ? 28.054 3.913   -11.644 0.28 32.16 ?  102 LYS   A HZ2  1 
ATOM   2091 H  HZ3  A LYS   A 1 102 ? 26.902 3.681   -9.092  0.72 33.69 ?  102 LYS   A HZ3  1 
ATOM   2092 H  HZ3  B LYS   A 1 102 ? 27.017 4.877   -11.952 0.28 32.16 ?  102 LYS   A HZ3  1 
ATOM   2093 N  N    A GLY   A 1 103 ? 22.367 -0.572  -14.947 0.72 25.77 ?  103 GLY   A N    1 
ATOM   2094 N  N    B GLY   A 1 103 ? 22.423 -1.346  -15.376 0.28 20.55 ?  103 GLY   A N    1 
ATOM   2095 C  CA   A GLY   A 1 103 ? 22.632 -1.642  -15.890 0.72 26.26 ?  103 GLY   A CA   1 
ATOM   2096 C  CA   B GLY   A 1 103 ? 22.621 -2.540  -16.174 0.28 20.23 ?  103 GLY   A CA   1 
ATOM   2097 C  C    A GLY   A 1 103 ? 23.498 -2.761  -15.361 0.72 26.72 ?  103 GLY   A C    1 
ATOM   2098 C  C    B GLY   A 1 103 ? 23.496 -3.591  -15.532 0.28 19.38 ?  103 GLY   A C    1 
ATOM   2099 O  O    A GLY   A 1 103 ? 24.124 -3.468  -16.156 0.72 27.68 ?  103 GLY   A O    1 
ATOM   2100 O  O    B GLY   A 1 103 ? 23.953 -4.509  -16.218 0.28 19.41 ?  103 GLY   A O    1 
ATOM   2101 H  H    A GLY   A 1 103 ? 21.621 -0.654  -14.538 0.72 30.90 ?  103 GLY   A H    1 
ATOM   2102 H  H    B GLY   A 1 103 ? 21.641 -1.272  -15.023 0.28 24.64 ?  103 GLY   A H    1 
ATOM   2103 H  HA2  A GLY   A 1 103 ? 21.786 -2.021  -16.192 0.72 31.49 ?  103 GLY   A HA2  1 
ATOM   2104 H  HA2  B GLY   A 1 103 ? 21.760 -2.940  -16.356 0.28 24.25 ?  103 GLY   A HA2  1 
ATOM   2105 H  HA3  A GLY   A 1 103 ? 23.087 -1.283  -16.667 0.72 31.49 ?  103 GLY   A HA3  1 
ATOM   2106 H  HA3  B GLY   A 1 103 ? 23.021 -2.284  -17.020 0.28 24.25 ?  103 GLY   A HA3  1 
ATOM   2107 N  N    A GLU   A 1 104 ? 23.560 -2.947  -14.046 0.72 25.46 ?  104 GLU   A N    1 
ATOM   2108 N  N    B GLU   A 1 104 ? 23.736 -3.490  -14.228 0.28 18.62 ?  104 GLU   A N    1 
ATOM   2109 C  CA   A GLU   A 1 104 ? 24.432 -3.948  -13.448 0.72 24.31 ?  104 GLU   A CA   1 
ATOM   2110 C  CA   B GLU   A 1 104 ? 24.637 -4.416  -13.556 0.28 18.05 ?  104 GLU   A CA   1 
ATOM   2111 C  C    A GLU   A 1 104 ? 23.741 -5.309  -13.356 0.72 24.92 ?  104 GLU   A C    1 
ATOM   2112 C  C    B GLU   A 1 104 ? 23.970 -5.778  -13.385 0.28 18.18 ?  104 GLU   A C    1 
ATOM   2113 O  O    A GLU   A 1 104 ? 22.516 -5.405  -13.236 0.72 25.33 ?  104 GLU   A O    1 
ATOM   2114 O  O    B GLU   A 1 104 ? 22.769 -5.875  -13.112 0.28 18.00 ?  104 GLU   A O    1 
ATOM   2115 C  CB   A GLU   A 1 104 ? 24.924 -3.463  -12.080 0.72 22.40 ?  104 GLU   A CB   1 
ATOM   2116 C  CB   B GLU   A 1 104 ? 25.068 -3.831  -12.210 0.28 17.87 ?  104 GLU   A CB   1 
ATOM   2117 C  CG   A GLU   A 1 104 ? 25.890 -2.277  -12.226 0.72 21.38 ?  104 GLU   A CG   1 
ATOM   2118 C  CG   B GLU   A 1 104 ? 25.760 -2.475  -12.354 0.28 18.26 ?  104 GLU   A CG   1 
ATOM   2119 C  CD   A GLU   A 1 104 ? 26.184 -1.500  -10.947 0.72 20.28 ?  104 GLU   A CD   1 
ATOM   2120 C  CD   B GLU   A 1 104 ? 26.190 -1.864  -11.032 0.28 18.52 ?  104 GLU   A CD   1 
ATOM   2121 O  OE1  A GLU   A 1 104 ? 25.604 -1.804  -9.884  0.72 18.43 ?  104 GLU   A OE1  1 
ATOM   2122 O  OE1  B GLU   A 1 104 ? 25.698 -2.301  -9.972  0.28 18.51 ?  104 GLU   A OE1  1 
ATOM   2123 O  OE2  A GLU   A 1 104 ? 27.011 -0.559  -11.028 0.72 21.28 -1 104 GLU   A OE2  1 
ATOM   2124 O  OE2  B GLU   A 1 104 ? 27.025 -0.935  -11.058 0.28 19.17 -1 104 GLU   A OE2  1 
ATOM   2125 H  H    A GLU   A 1 104 ? 23.106 -2.492  -13.473 0.72 30.53 ?  104 GLU   A H    1 
ATOM   2126 H  H    B GLU   A 1 104 ? 23.385 -2.897  -13.714 0.28 22.32 ?  104 GLU   A H    1 
ATOM   2127 H  HA   A GLU   A 1 104 ? 25.207 -4.055  -14.018 0.72 29.15 ?  104 GLU   A HA   1 
ATOM   2128 H  HA   B GLU   A 1 104 ? 25.434 -4.531  -14.099 0.28 21.64 ?  104 GLU   A HA   1 
ATOM   2129 H  HB2  A GLU   A 1 104 ? 24.163 -3.179  -11.552 0.72 26.85 ?  104 GLU   A HB2  1 
ATOM   2130 H  HB2  B GLU   A 1 104 ? 24.286 -3.708  -11.650 0.28 21.42 ?  104 GLU   A HB2  1 
ATOM   2131 H  HB3  A GLU   A 1 104 ? 25.391 -4.188  -11.636 0.72 26.85 ?  104 GLU   A HB3  1 
ATOM   2132 H  HB3  B GLU   A 1 104 ? 25.692 -4.439  -11.784 0.28 21.42 ?  104 GLU   A HB3  1 
ATOM   2133 H  HG2  A GLU   A 1 104 ? 26.733 -2.613  -12.562 0.72 25.64 ?  104 GLU   A HG2  1 
ATOM   2134 H  HG2  B GLU   A 1 104 ? 26.552 -2.581  -12.904 0.28 21.89 ?  104 GLU   A HG2  1 
ATOM   2135 H  HG3  A GLU   A 1 104 ? 25.509 -1.652  -12.861 0.72 25.64 ?  104 GLU   A HG3  1 
ATOM   2136 H  HG3  B GLU   A 1 104 ? 25.149 -1.851  -12.778 0.28 21.89 ?  104 GLU   A HG3  1 
ATOM   2137 N  N    A ASP   A 1 105 ? 24.554 -6.366  -13.417 0.72 25.65 ?  105 ASP   A N    1 
ATOM   2138 N  N    B ASP   A 1 105 ? 24.766 -6.832  -13.554 0.28 19.16 ?  105 ASP   A N    1 
ATOM   2139 C  CA   A ASP   A 1 105 ? 24.056 -7.731  -13.562 0.72 26.79 ?  105 ASP   A CA   1 
ATOM   2140 C  CA   B ASP   A 1 105 ? 24.257 -8.199  -13.604 0.28 20.36 ?  105 ASP   A CA   1 
ATOM   2141 C  C    A ASP   A 1 105 ? 23.379 -8.200  -12.278 0.72 24.57 ?  105 ASP   A C    1 
ATOM   2142 C  C    B ASP   A 1 105 ? 23.513 -8.553  -12.322 0.28 19.91 ?  105 ASP   A C    1 
ATOM   2143 O  O    A ASP   A 1 105 ? 24.009 -8.246  -11.219 0.72 22.87 ?  105 ASP   A O    1 
ATOM   2144 O  O    B ASP   A 1 105 ? 24.102 -8.579  -11.237 0.28 18.52 ?  105 ASP   A O    1 
ATOM   2145 C  CB   A ASP   A 1 105 ? 25.226 -8.651  -13.906 0.72 29.90 ?  105 ASP   A CB   1 
ATOM   2146 C  CB   B ASP   A 1 105 ? 25.437 -9.149  -13.810 0.28 22.04 ?  105 ASP   A CB   1 
ATOM   2147 C  CG   A ASP   A 1 105 ? 24.793 -10.078 -14.153 0.72 32.48 ?  105 ASP   A CG   1 
ATOM   2148 C  CG   B ASP   A 1 105 ? 25.022 -10.607 -13.880 0.28 23.47 ?  105 ASP   A CG   1 
ATOM   2149 O  OD1  A ASP   A 1 105 ? 23.573 -10.318 -14.268 0.72 33.16 ?  105 ASP   A OD1  1 
ATOM   2150 O  OD1  B ASP   A 1 105 ? 23.811 -10.890 -13.981 0.28 23.65 ?  105 ASP   A OD1  1 
ATOM   2151 O  OD2  A ASP   A 1 105 ? 25.677 -10.959 -14.235 0.72 33.87 -1 105 ASP   A OD2  1 
ATOM   2152 O  OD2  B ASP   A 1 105 ? 25.922 -11.475 -13.829 0.28 24.29 -1 105 ASP   A OD2  1 
ATOM   2153 H  H    A ASP   A 1 105 ? 25.413 -6.316  -13.378 0.72 30.76 ?  105 ASP   A H    1 
ATOM   2154 H  H    B ASP   A 1 105 ? 25.617 -6.774  -13.649 0.28 22.97 ?  105 ASP   A H    1 
ATOM   2155 H  HA   A ASP   A 1 105 ? 23.412 -7.774  -14.284 0.72 32.12 ?  105 ASP   A HA   1 
ATOM   2156 H  HA   B ASP   A 1 105 ? 23.644 -8.285  -14.350 0.28 24.41 ?  105 ASP   A HA   1 
ATOM   2157 H  HB2  A ASP   A 1 105 ? 25.656 -8.333  -14.715 0.72 35.86 ?  105 ASP   A HB2  1 
ATOM   2158 H  HB2  B ASP   A 1 105 ? 25.886 -8.914  -14.637 0.28 26.43 ?  105 ASP   A HB2  1 
ATOM   2159 H  HB3  A ASP   A 1 105 ? 25.861 -8.649  -13.171 0.72 35.86 ?  105 ASP   A HB3  1 
ATOM   2160 H  HB3  B ASP   A 1 105 ? 26.046 -9.059  -13.063 0.28 26.43 ?  105 ASP   A HB3  1 
ATOM   2161 N  N    A ILE   A 1 106 ? 22.105 -8.589  -12.383 0.72 24.11 ?  106 ILE   A N    1 
ATOM   2162 N  N    B ILE   A 1 106 ? 22.216 -8.848  -12.452 0.28 20.80 ?  106 ILE   A N    1 
ATOM   2163 C  CA   A ILE   A 1 106 ? 21.345 -9.004  -11.209 0.72 23.38 ?  106 ILE   A CA   1 
ATOM   2164 C  CA   B ILE   A 1 106 ? 21.418 -9.223  -11.292 0.28 21.77 ?  106 ILE   A CA   1 
ATOM   2165 C  C    A ILE   A 1 106 ? 21.880 -10.297 -10.607 0.72 22.31 ?  106 ILE   A C    1 
ATOM   2166 C  C    B ILE   A 1 106 ? 21.945 -10.492 -10.642 0.28 22.09 ?  106 ILE   A C    1 
ATOM   2167 O  O    A ILE   A 1 106 ? 21.663 -10.553 -9.419  0.72 21.57 ?  106 ILE   A O    1 
ATOM   2168 O  O    B ILE   A 1 106 ? 21.711 -10.718 -9.450  0.28 22.03 ?  106 ILE   A O    1 
ATOM   2169 C  CB   A ILE   A 1 106 ? 19.839 -9.089  -11.540 0.72 24.59 ?  106 ILE   A CB   1 
ATOM   2170 C  CB   B ILE   A 1 106 ? 19.922 -9.347  -11.660 0.28 22.67 ?  106 ILE   A CB   1 
ATOM   2171 C  CG1  A ILE   A 1 106 ? 19.000 -9.175  -10.260 0.72 25.12 ?  106 ILE   A CG1  1 
ATOM   2172 C  CG1  B ILE   A 1 106 ? 19.051 -9.296  -10.401 0.28 23.15 ?  106 ILE   A CG1  1 
ATOM   2173 C  CG2  A ILE   A 1 106 ? 19.550 -10.288 -12.426 0.72 25.21 ?  106 ILE   A CG2  1 
ATOM   2174 C  CG2  B ILE   A 1 106 ? 19.656 -10.642 -12.403 0.28 22.91 ?  106 ILE   A CG2  1 
ATOM   2175 C  CD1  A ILE   A 1 106 ? 19.128 -7.969  -9.357  0.72 25.47 ?  106 ILE   A CD1  1 
ATOM   2176 C  CD1  B ILE   A 1 106 ? 19.160 -7.998  -9.630  0.28 23.41 ?  106 ILE   A CD1  1 
ATOM   2177 H  H    A ILE   A 1 106 ? 21.667 -8.618  -13.119 0.72 28.91 ?  106 ILE   A H    1 
ATOM   2178 H  H    B ILE   A 1 106 ? 21.785 -8.832  -13.194 0.28 24.94 ?  106 ILE   A H    1 
ATOM   2179 H  HA   A ILE   A 1 106 ? 21.455 -8.324  -10.534 0.72 28.03 ?  106 ILE   A HA   1 
ATOM   2180 H  HA   B ILE   A 1 106 ? 21.501 -8.519  -10.636 0.28 26.11 ?  106 ILE   A HA   1 
ATOM   2181 H  HB   A ILE   A 1 106 ? 19.586 -8.284  -12.019 0.72 29.49 ?  106 ILE   A HB   1 
ATOM   2182 H  HB   B ILE   A 1 106 ? 19.680 -8.603  -12.234 0.28 27.18 ?  106 ILE   A HB   1 
ATOM   2183 H  HG12 A ILE   A 1 106 ? 18.065 -9.257  -10.506 0.72 30.13 ?  106 ILE   A HG12 1 
ATOM   2184 H  HG12 B ILE   A 1 106 ? 18.122 -9.407  -10.658 0.28 27.76 ?  106 ILE   A HG12 1 
ATOM   2185 H  HG13 A ILE   A 1 106 ? 19.275 -9.955  -9.755  0.72 30.13 ?  106 ILE   A HG13 1 
ATOM   2186 H  HG13 B ILE   A 1 106 ? 19.315 -10.015 -9.807  0.28 27.76 ?  106 ILE   A HG13 1 
ATOM   2187 H  HG21 A ILE   A 1 106 ? 18.652 -10.205 -12.782 0.72 30.22 ?  106 ILE   A HG21 1 
ATOM   2188 H  HG21 B ILE   A 1 106 ? 18.795 -10.579 -12.845 0.28 27.47 ?  106 ILE   A HG21 1 
ATOM   2189 H  HG22 A ILE   A 1 106 ? 20.194 -10.303 -13.150 0.72 30.22 ?  106 ILE   A HG22 1 
ATOM   2190 H  HG22 B ILE   A 1 106 ? 20.357 -10.777 -13.057 0.28 27.47 ?  106 ILE   A HG22 1 
ATOM   2191 H  HG23 A ILE   A 1 106 ? 19.624 -11.097 -11.898 0.72 30.22 ?  106 ILE   A HG23 1 
ATOM   2192 H  HG23 B ILE   A 1 106 ? 19.648 -11.375 -11.767 0.28 27.47 ?  106 ILE   A HG23 1 
ATOM   2193 H  HD11 A ILE   A 1 106 ? 18.402 -7.977  -8.716  0.72 30.54 ?  106 ILE   A HD11 1 
ATOM   2194 H  HD11 B ILE   A 1 106 ? 18.391 -7.913  -9.047  0.28 28.07 ?  106 ILE   A HD11 1 
ATOM   2195 H  HD12 A ILE   A 1 106 ? 19.979 -8.012  -8.891  0.72 30.54 ?  106 ILE   A HD12 1 
ATOM   2196 H  HD12 B ILE   A 1 106 ? 19.975 -8.009  -9.103  0.28 28.07 ?  106 ILE   A HD12 1 
ATOM   2197 H  HD13 A ILE   A 1 106 ? 19.086 -7.164  -9.897  0.72 30.54 ?  106 ILE   A HD13 1 
ATOM   2198 H  HD13 B ILE   A 1 106 ? 19.181 -7.259  -10.259 0.28 28.07 ?  106 ILE   A HD13 1 
ATOM   2199 N  N    A GLN   A 1 107 ? 22.590 -11.114 -11.394 0.72 23.03 ?  107 GLN   A N    1 
ATOM   2200 N  N    B GLN   A 1 107 ? 22.663 -11.329 -11.397 0.28 22.50 ?  107 GLN   A N    1 
ATOM   2201 C  CA   A GLN   A 1 107 ? 23.191 -12.335 -10.861 0.72 24.97 ?  107 GLN   A CA   1 
ATOM   2202 C  CA   B GLN   A 1 107 ? 23.301 -12.494 -10.800 0.28 23.37 ?  107 GLN   A CA   1 
ATOM   2203 C  C    A GLN   A 1 107 ? 24.159 -12.032 -9.724  0.72 22.32 ?  107 GLN   A C    1 
ATOM   2204 C  C    B GLN   A 1 107 ? 24.322 -12.099 -9.745  0.28 21.35 ?  107 GLN   A C    1 
ATOM   2205 O  O    A GLN   A 1 107 ? 24.363 -12.871 -8.838  0.72 23.26 ?  107 GLN   A O    1 
ATOM   2206 O  O    B GLN   A 1 107 ? 24.732 -12.948 -8.947  0.28 21.96 ?  107 GLN   A O    1 
ATOM   2207 C  CB   A GLN   A 1 107 ? 23.897 -13.097 -11.988 0.72 29.24 ?  107 GLN   A CB   1 
ATOM   2208 C  CB   B GLN   A 1 107 ? 23.964 -13.353 -11.880 0.28 25.99 ?  107 GLN   A CB   1 
ATOM   2209 C  CG   A GLN   A 1 107 ? 23.024 -13.322 -13.221 0.72 33.79 ?  107 GLN   A CG   1 
ATOM   2210 C  CG   B GLN   A 1 107 ? 22.998 -13.852 -12.943 0.28 28.45 ?  107 GLN   A CG   1 
ATOM   2211 C  CD   A GLN   A 1 107 ? 21.750 -14.079 -12.903 0.72 37.44 ?  107 GLN   A CD   1 
ATOM   2212 C  CD   B GLN   A 1 107 ? 21.859 -14.667 -12.362 0.28 30.59 ?  107 GLN   A CD   1 
ATOM   2213 O  OE1  A GLN   A 1 107 ? 21.782 -15.129 -12.262 0.72 38.82 ?  107 GLN   A OE1  1 
ATOM   2214 O  OE1  B GLN   A 1 107 ? 22.043 -15.416 -11.402 0.28 31.33 ?  107 GLN   A OE1  1 
ATOM   2215 N  NE2  A GLN   A 1 107 ? 20.617 -13.544 -13.346 0.72 38.56 ?  107 GLN   A NE2  1 
ATOM   2216 N  NE2  B GLN   A 1 107 ? 20.671 -14.519 -12.938 0.28 31.25 ?  107 GLN   A NE2  1 
ATOM   2217 H  H    A GLN   A 1 107 ? 22.735 -10.983 -12.229 0.72 27.62 ?  107 GLN   A H    1 
ATOM   2218 H  H    B GLN   A 1 107 ? 22.795 -11.243 -12.241 0.28 26.97 ?  107 GLN   A H    1 
ATOM   2219 H  HA   A GLN   A 1 107 ? 22.499 -12.908 -10.507 0.72 29.94 ?  107 GLN   A HA   1 
ATOM   2220 H  HA   B GLN   A 1 107 ? 22.625 -13.033 -10.366 0.28 28.02 ?  107 GLN   A HA   1 
ATOM   2221 H  HB2  A GLN   A 1 107 ? 24.679 -12.598 -12.271 0.72 35.07 ?  107 GLN   A HB2  1 
ATOM   2222 H  HB2  B GLN   A 1 107 ? 24.650 -12.830 -12.323 0.28 31.17 ?  107 GLN   A HB2  1 
ATOM   2223 H  HB3  A GLN   A 1 107 ? 24.167 -13.971 -11.661 0.72 35.07 ?  107 GLN   A HB3  1 
ATOM   2224 H  HB3  B GLN   A 1 107 ? 24.367 -14.130 -11.459 0.28 31.17 ?  107 GLN   A HB3  1 
ATOM   2225 H  HG2  A GLN   A 1 107 ? 22.778 -12.464 -13.603 0.72 40.52 ?  107 GLN   A HG2  1 
ATOM   2226 H  HG2  B GLN   A 1 107 ? 22.617 -13.090 -13.407 0.28 34.12 ?  107 GLN   A HG2  1 
ATOM   2227 H  HG3  A GLN   A 1 107 ? 23.525 -13.838 -13.872 0.72 40.52 ?  107 GLN   A HG3  1 
ATOM   2228 H  HG3  B GLN   A 1 107 ? 23.479 -14.415 -13.569 0.28 34.12 ?  107 GLN   A HG3  1 
ATOM   2229 H  HE21 A GLN   A 1 107 ? 20.633 -12.808 -13.790 0.72 46.25 ?  107 GLN   A HE21 1 
ATOM   2230 H  HE21 B GLN   A 1 107 ? 20.580 -13.984 -13.606 0.28 37.48 ?  107 GLN   A HE21 1 
ATOM   2231 H  HE22 A GLN   A 1 107 ? 19.868 -13.936 -13.190 0.72 46.25 ?  107 GLN   A HE22 1 
ATOM   2232 H  HE22 B GLN   A 1 107 ? 19.992 -14.957 -12.644 0.28 37.48 ?  107 GLN   A HE22 1 
ATOM   2233 N  N    . LEU   A 1 108 ? 24.743 -10.833 -9.715  1.00 18.89 ?  108 LEU   A N    1 
ATOM   2234 C  CA   . LEU   A 1 108 ? 25.653 -10.406 -8.665  1.00 15.98 ?  108 LEU   A CA   1 
ATOM   2235 C  C    . LEU   A 1 108 ? 24.950 -10.230 -7.328  1.00 13.81 ?  108 LEU   A C    1 
ATOM   2236 O  O    . LEU   A 1 108 ? 25.629 -10.070 -6.312  1.00 13.99 ?  108 LEU   A O    1 
ATOM   2237 C  CB   . LEU   A 1 108 ? 26.377 -9.115  -9.072  1.00 15.81 ?  108 LEU   A CB   1 
ATOM   2238 C  CG   . LEU   A 1 108 ? 27.375 -9.306  -10.217 1.00 17.55 ?  108 LEU   A CG   1 
ATOM   2239 C  CD1  . LEU   A 1 108 ? 27.870 -7.972  -10.759 1.00 18.37 ?  108 LEU   A CD1  1 
ATOM   2240 C  CD2  . LEU   A 1 108 ? 28.556 -10.156 -9.770  1.00 19.14 ?  108 LEU   A CD2  1 
ATOM   2241 H  H    A LEU   A 1 108 ? 24.617 -10.236 -10.316 0.72 22.64 ?  108 LEU   A H    1 
ATOM   2242 H  H    B LEU   A 1 108 ? 24.536 -10.227 -10.284 0.28 22.64 ?  108 LEU   A H    1 
ATOM   2243 H  HA   . LEU   A 1 108 ? 26.327 -11.090 -8.540  1.00 19.16 ?  108 LEU   A HA   1 
ATOM   2244 H  HB2  . LEU   A 1 108 ? 25.720 -8.463  -9.360  1.00 18.95 ?  108 LEU   A HB2  1 
ATOM   2245 H  HB3  . LEU   A 1 108 ? 26.868 -8.774  -8.309  1.00 18.95 ?  108 LEU   A HB3  1 
ATOM   2246 H  HG   . LEU   A 1 108 ? 26.933 -9.775  -10.943 1.00 21.04 ?  108 LEU   A HG   1 
ATOM   2247 H  HD11 . LEU   A 1 108 ? 28.485 -8.138  -11.496 1.00 22.02 ?  108 LEU   A HD11 1 
ATOM   2248 H  HD12 . LEU   A 1 108 ? 27.114 -7.455  -11.072 1.00 22.02 ?  108 LEU   A HD12 1 
ATOM   2249 H  HD13 . LEU   A 1 108 ? 28.331 -7.494  -10.052 1.00 22.02 ?  108 LEU   A HD13 1 
ATOM   2250 H  HD21 . LEU   A 1 108 ? 29.249 -10.108 -10.444 1.00 22.94 ?  108 LEU   A HD21 1 
ATOM   2251 H  HD22 . LEU   A 1 108 ? 28.886 -9.811  -8.926  1.00 22.94 ?  108 LEU   A HD22 1 
ATOM   2252 H  HD23 . LEU   A 1 108 ? 28.260 -11.073 -9.661  1.00 22.94 ?  108 LEU   A HD23 1 
ATOM   2253 N  N    . LEU   A 1 109 ? 23.617 -10.287 -7.294  1.00 13.19 ?  109 LEU   A N    1 
ATOM   2254 C  CA   . LEU   A 1 109 ? 22.916 -10.166 -6.023  1.00 12.17 ?  109 LEU   A CA   1 
ATOM   2255 C  C    . LEU   A 1 109 ? 23.259 -11.316 -5.084  1.00 11.68 ?  109 LEU   A C    1 
ATOM   2256 O  O    . LEU   A 1 109 ? 23.397 -11.114 -3.872  1.00 12.03 ?  109 LEU   A O    1 
ATOM   2257 C  CB   . LEU   A 1 109 ? 21.414 -10.091 -6.278  1.00 12.85 ?  109 LEU   A CB   1 
ATOM   2258 C  CG   . LEU   A 1 109 ? 20.523 -9.800  -5.074  1.00 13.17 ?  109 LEU   A CG   1 
ATOM   2259 C  CD1  . LEU   A 1 109 ? 20.961 -8.532  -4.366  1.00 13.45 ?  109 LEU   A CD1  1 
ATOM   2260 C  CD2  . LEU   A 1 109 ? 19.069 -9.697  -5.524  1.00 14.15 ?  109 LEU   A CD2  1 
ATOM   2261 H  H    . LEU   A 1 109 ? 23.108 -10.392 -7.977  1.00 15.80 ?  109 LEU   A H    1 
ATOM   2262 H  HA   . LEU   A 1 109 ? 23.193 -9.338  -5.595  1.00 14.59 ?  109 LEU   A HA   1 
ATOM   2263 H  HB2  . LEU   A 1 109 ? 21.256 -9.387  -6.928  1.00 15.40 ?  109 LEU   A HB2  1 
ATOM   2264 H  HB3  . LEU   A 1 109 ? 21.130 -10.938 -6.647  1.00 15.40 ?  109 LEU   A HB3  1 
ATOM   2265 H  HG   . LEU   A 1 109 ? 20.590 -10.531 -4.445  1.00 15.78 ?  109 LEU   A HG   1 
ATOM   2266 H  HD11 . LEU   A 1 109 ? 20.278 -8.270  -3.729  1.00 16.12 ?  109 LEU   A HD11 1 
ATOM   2267 H  HD12 . LEU   A 1 109 ? 21.798 -8.691  -3.910  1.00 16.12 ?  109 LEU   A HD12 1 
ATOM   2268 H  HD13 . LEU   A 1 109 ? 21.074 -7.822  -5.027  1.00 16.12 ?  109 LEU   A HD13 1 
ATOM   2269 H  HD21 . LEU   A 1 109 ? 18.524 -9.397  -4.779  1.00 16.95 ?  109 LEU   A HD21 1 
ATOM   2270 H  HD22 . LEU   A 1 109 ? 19.002 -9.066  -6.256  1.00 16.95 ?  109 LEU   A HD22 1 
ATOM   2271 H  HD23 . LEU   A 1 109 ? 18.765 -10.574 -5.819  1.00 16.95 ?  109 LEU   A HD23 1 
ATOM   2272 N  N    . LYS   A 1 110 ? 23.404 -12.531 -5.615  1.00 11.59 ?  110 LYS   A N    1 
ATOM   2273 C  CA   . LYS   A 1 110 ? 23.779 -13.645 -4.753  1.00 11.70 ?  110 LYS   A CA   1 
ATOM   2274 C  C    . LYS   A 1 110 ? 25.161 -13.424 -4.149  1.00 11.07 ?  110 LYS   A C    1 
ATOM   2275 O  O    . LYS   A 1 110 ? 25.355 -13.624 -2.947  1.00 11.32 ?  110 LYS   A O    1 
ATOM   2276 C  CB   . LYS   A 1 110 ? 23.701 -14.971 -5.512  1.00 12.58 ?  110 LYS   A CB   1 
ATOM   2277 C  CG   . LYS   A 1 110 ? 23.900 -16.184 -4.602  1.00 12.85 ?  110 LYS   A CG   1 
ATOM   2278 C  CD   . LYS   A 1 110 ? 23.674 -17.506 -5.321  1.00 13.34 ?  110 LYS   A CD   1 
ATOM   2279 C  CE   . LYS   A 1 110 ? 23.783 -18.691 -4.368  1.00 13.86 ?  110 LYS   A CE   1 
ATOM   2280 N  NZ   . LYS   A 1 110 ? 22.593 -18.817 -3.489  1.00 14.37 ?  110 LYS   A NZ   1 
ATOM   2281 H  H    . LYS   A 1 110 ? 23.290 -12.729 -6.441  1.00 13.88 ?  110 LYS   A H    1 
ATOM   2282 H  HA   . LYS   A 1 110 ? 23.139 -13.695 -4.020  1.00 14.02 ?  110 LYS   A HA   1 
ATOM   2283 H  HB2  . LYS   A 1 110 ? 22.825 -15.050 -5.924  1.00 15.07 ?  110 LYS   A HB2  1 
ATOM   2284 H  HB3  . LYS   A 1 110 ? 24.391 -14.990 -6.188  1.00 15.07 ?  110 LYS   A HB3  1 
ATOM   2285 H  HG2  . LYS   A 1 110 ? 24.806 -16.177 -4.259  1.00 15.40 ?  110 LYS   A HG2  1 
ATOM   2286 H  HG3  . LYS   A 1 110 ? 23.267 -16.134 -3.866  1.00 15.40 ?  110 LYS   A HG3  1 
ATOM   2287 H  HD2  . LYS   A 1 110 ? 22.791 -17.512 -5.713  1.00 15.98 ?  110 LYS   A HD2  1 
ATOM   2288 H  HD3  . LYS   A 1 110 ? 24.352 -17.610 -6.010  1.00 15.98 ?  110 LYS   A HD3  1 
ATOM   2289 H  HE2  . LYS   A 1 110 ? 23.866 -19.507 -4.883  1.00 16.61 ?  110 LYS   A HE2  1 
ATOM   2290 H  HE3  . LYS   A 1 110 ? 24.564 -18.574 -3.801  1.00 16.61 ?  110 LYS   A HE3  1 
ATOM   2291 H  HZ1  . LYS   A 1 110 ? 22.684 -19.512 -2.947  1.00 17.22 ?  110 LYS   A HZ1  1 
ATOM   2292 H  HZ2  . LYS   A 1 110 ? 22.497 -18.076 -3.000  1.00 17.22 ?  110 LYS   A HZ2  1 
ATOM   2293 H  HZ3  . LYS   A 1 110 ? 21.860 -18.927 -3.985  1.00 17.22 ?  110 LYS   A HZ3  1 
ATOM   2294 N  N    . SER   A 1 111 ? 26.123 -12.988 -4.964  1.00 11.45 ?  111 SER   A N    1 
ATOM   2295 C  CA   . SER   A 1 111 ? 27.450 -12.679 -4.444  1.00 11.47 ?  111 SER   A CA   1 
ATOM   2296 C  C    . SER   A 1 111 ? 27.385 -11.627 -3.344  1.00 11.12 ?  111 SER   A C    1 
ATOM   2297 O  O    . SER   A 1 111 ? 28.079 -11.731 -2.328  1.00 11.77 ?  111 SER   A O    1 
ATOM   2298 C  CB   . SER   A 1 111 ? 28.338 -12.190 -5.586  1.00 12.84 ?  111 SER   A CB   1 
ATOM   2299 O  OG   . SER   A 1 111 ? 28.444 -13.183 -6.595  1.00 14.52 ?  111 SER   A OG   1 
ATOM   2300 H  H    . SER   A 1 111 ? 26.026 -12.863 -5.806  1.00 13.72 ?  111 SER   A H    1 
ATOM   2301 H  HA   . SER   A 1 111 ? 27.845 -13.486 -4.076  1.00 13.75 ?  111 SER   A HA   1 
ATOM   2302 H  HB2  . SER   A 1 111 ? 27.939 -11.398 -5.978  1.00 15.38 ?  111 SER   A HB2  1 
ATOM   2303 H  HB3  . SER   A 1 111 ? 29.217 -11.982 -5.236  1.00 15.38 ?  111 SER   A HB3  1 
ATOM   2304 H  HG   . SER   A 1 111 ? 28.953 -12.907 -7.213  1.00 17.40 ?  111 SER   A HG   1 
ATOM   2305 N  N    . ALA   A 1 112 ? 26.542 -10.610 -3.527  1.00 11.28 ?  112 ALA   A N    1 
ATOM   2306 C  CA   . ALA   A 1 112 ? 26.396 -9.573  -2.509  1.00 11.33 ?  112 ALA   A CA   1 
ATOM   2307 C  C    . ALA   A 1 112 ? 25.912 -10.170 -1.189  1.00 11.05 ?  112 ALA   A C    1 
ATOM   2308 O  O    . ALA   A 1 112 ? 26.455 -9.873  -0.118  1.00 11.41 ?  112 ALA   A O    1 
ATOM   2309 C  CB   . ALA   A 1 112 ? 25.441 -8.481  -3.002  1.00 11.66 ?  112 ALA   A CB   1 
ATOM   2310 H  H    . ALA   A 1 112 ? 26.048 -10.498 -4.219  1.00 13.51 ?  112 ALA   A H    1 
ATOM   2311 H  HA   . ALA   A 1 112 ? 27.257 -9.158  -2.348  1.00 13.58 ?  112 ALA   A HA   1 
ATOM   2312 H  HB1  . ALA   A 1 112 ? 25.372 -7.784  -2.324  1.00 13.97 ?  112 ALA   A HB1  1 
ATOM   2313 H  HB2  . ALA   A 1 112 ? 25.789 -8.099  -3.824  1.00 13.97 ?  112 ALA   A HB2  1 
ATOM   2314 H  HB3  . ALA   A 1 112 ? 24.566 -8.867  -3.162  1.00 13.97 ?  112 ALA   A HB3  1 
ATOM   2315 N  N    . TYR   A 1 113 ? 24.877 -11.014 -1.242  1.00 11.03 ?  113 TYR   A N    1 
ATOM   2316 C  CA   . TYR   A 1 113 ? 24.366 -11.619 -0.016  1.00 10.72 ?  113 TYR   A CA   1 
ATOM   2317 C  C    . TYR   A 1 113 ? 25.372 -12.565 0.636   1.00 10.66 ?  113 TYR   A C    1 
ATOM   2318 O  O    . TYR   A 1 113 ? 25.322 -12.751 1.856   1.00 11.24 ?  113 TYR   A O    1 
ATOM   2319 C  CB   . TYR   A 1 113 ? 23.043 -12.347 -0.285  1.00 11.25 ?  113 TYR   A CB   1 
ATOM   2320 C  CG   . TYR   A 1 113 ? 21.828 -11.455 -0.202  1.00 11.04 ?  113 TYR   A CG   1 
ATOM   2321 C  CD1  . TYR   A 1 113 ? 21.463 -10.862 1.002   1.00 11.20 ?  113 TYR   A CD1  1 
ATOM   2322 C  CD2  . TYR   A 1 113 ? 21.027 -11.229 -1.313  1.00 11.10 ?  113 TYR   A CD2  1 
ATOM   2323 C  CE1  . TYR   A 1 113 ? 20.338 -10.063 1.096   1.00 11.39 ?  113 TYR   A CE1  1 
ATOM   2324 C  CE2  . TYR   A 1 113 ? 19.883 -10.424 -1.227  1.00 11.32 ?  113 TYR   A CE2  1 
ATOM   2325 C  CZ   . TYR   A 1 113 ? 19.550 -9.849  -0.019  1.00 11.21 ?  113 TYR   A CZ   1 
ATOM   2326 O  OH   . TYR   A 1 113 ? 18.424 -9.060  0.099   1.00 11.83 ?  113 TYR   A OH   1 
ATOM   2327 H  H    . TYR   A 1 113 ? 24.467 -11.241 -1.961  1.00 13.22 ?  113 TYR   A H    1 
ATOM   2328 H  HA   . TYR   A 1 113 ? 24.190 -10.913 0.621   1.00 12.84 ?  113 TYR   A HA   1 
ATOM   2329 H  HB2  . TYR   A 1 113 ? 23.068 -12.723 -1.177  1.00 13.48 ?  113 TYR   A HB2  1 
ATOM   2330 H  HB3  . TYR   A 1 113 ? 22.939 -13.053 0.370   1.00 13.48 ?  113 TYR   A HB3  1 
ATOM   2331 H  HD1  . TYR   A 1 113 ? 21.987 -11.009 1.760   1.00 13.42 ?  113 TYR   A HD1  1 
ATOM   2332 H  HD2  . TYR   A 1 113 ? 21.245 -11.622 -2.121  1.00 13.30 ?  113 TYR   A HD2  1 
ATOM   2333 H  HE1  . TYR   A 1 113 ? 20.112 -9.674  1.912   1.00 13.64 ?  113 TYR   A HE1  1 
ATOM   2334 H  HE2  . TYR   A 1 113 ? 19.348 -10.275 -1.973  1.00 13.56 ?  113 TYR   A HE2  1 
ATOM   2335 H  HH   . TYR   A 1 113 ? 18.039 -9.005  -0.649  1.00 14.17 ?  113 TYR   A HH   1 
ATOM   2336 N  N    . GLU   A 1 114 ? 26.270 -13.185 -0.145  1.00 10.93 ?  114 GLU   A N    1 
ATOM   2337 C  CA   . GLU   A 1 114 ? 27.261 -14.077 0.454   1.00 11.15 ?  114 GLU   A CA   1 
ATOM   2338 C  C    . GLU   A 1 114 ? 28.107 -13.364 1.502   1.00 11.26 ?  114 GLU   A C    1 
ATOM   2339 O  O    . GLU   A 1 114 ? 28.580 -13.997 2.452   1.00 11.51 ?  114 GLU   A O    1 
ATOM   2340 C  CB   . GLU   A 1 114 ? 28.129 -14.722 -0.633  1.00 11.20 ?  114 GLU   A CB   1 
ATOM   2341 C  CG   . GLU   A 1 114 ? 27.369 -15.770 -1.412  1.00 11.87 ?  114 GLU   A CG   1 
ATOM   2342 C  CD   . GLU   A 1 114 ? 28.082 -16.306 -2.644  1.00 12.12 ?  114 GLU   A CD   1 
ATOM   2343 O  OE1  . GLU   A 1 114 ? 29.038 -15.678 -3.142  1.00 12.30 ?  114 GLU   A OE1  1 
ATOM   2344 O  OE2  . GLU   A 1 114 ? 27.639 -17.368 -3.135  1.00 13.26 -1 114 GLU   A OE2  1 
ATOM   2345 H  H    . GLU   A 1 114 ? 26.329 -13.097 -1.008  1.00 13.09 ?  114 GLU   A H    1 
ATOM   2346 H  HA   . GLU   A 1 114 ? 26.791 -14.791 0.898   1.00 13.36 ?  114 GLU   A HA   1 
ATOM   2347 H  HB2  . GLU   A 1 114 ? 28.423 -14.043 -1.263  1.00 13.41 ?  114 GLU   A HB2  1 
ATOM   2348 H  HB3  . GLU   A 1 114 ? 28.892 -15.154 -0.225  1.00 13.41 ?  114 GLU   A HB3  1 
ATOM   2349 H  HG2  . GLU   A 1 114 ? 27.189 -16.526 -0.830  1.00 14.23 ?  114 GLU   A HG2  1 
ATOM   2350 H  HG3  . GLU   A 1 114 ? 26.521 -15.390 -1.709  1.00 14.23 ?  114 GLU   A HG3  1 
ATOM   2351 N  N    . ASN   A 1 115 ? 28.287 -12.046 1.372   1.00 10.98 ?  115 ASN   A N    1 
ATOM   2352 C  CA   . ASN   A 1 115 ? 29.055 -11.322 2.379   1.00 11.11 ?  115 ASN   A CA   1 
ATOM   2353 C  C    . ASN   A 1 115 ? 28.436 -11.455 3.765   1.00 10.89 ?  115 ASN   A C    1 
ATOM   2354 O  O    . ASN   A 1 115 ? 29.146 -11.371 4.776   1.00 11.24 ?  115 ASN   A O    1 
ATOM   2355 C  CB   . ASN   A 1 115 ? 29.165 -9.845  2.001   1.00 11.66 ?  115 ASN   A CB   1 
ATOM   2356 C  CG   . ASN   A 1 115 ? 29.966 -9.630  0.736   1.00 12.16 ?  115 ASN   A CG   1 
ATOM   2357 O  OD1  . ASN   A 1 115 ? 31.185 -9.727  0.748   1.00 15.69 ?  115 ASN   A OD1  1 
ATOM   2358 N  ND2  . ASN   A 1 115 ? 29.291 -9.326  -0.355  1.00 11.49 ?  115 ASN   A ND2  1 
ATOM   2359 H  H    . ASN   A 1 115 ? 27.980 -11.560 0.730   1.00 13.16 ?  115 ASN   A H    1 
ATOM   2360 H  HA   . ASN   A 1 115 ? 29.950 -11.688 2.418   1.00 13.31 ?  115 ASN   A HA   1 
ATOM   2361 H  HB2  . ASN   A 1 115 ? 28.273 -9.485  1.868   1.00 13.98 ?  115 ASN   A HB2  1 
ATOM   2362 H  HB3  . ASN   A 1 115 ? 29.606 -9.368  2.726   1.00 13.98 ?  115 ASN   A HB3  1 
ATOM   2363 H  HD21 . ASN   A 1 115 ? 29.706 -9.197  -1.094  1.00 13.77 ?  115 ASN   A HD21 1 
ATOM   2364 H  HD22 . ASN   A 1 115 ? 28.430 -9.284  -0.332  1.00 13.77 ?  115 ASN   A HD22 1 
ATOM   2365 N  N    . PHE   A 1 116 ? 27.108 -11.614 3.839   1.00 11.04 ?  116 PHE   A N    1 
ATOM   2366 C  CA   . PHE   A 1 116 ? 26.453 -11.713 5.138   1.00 11.10 ?  116 PHE   A CA   1 
ATOM   2367 C  C    . PHE   A 1 116 ? 26.923 -12.944 5.909   1.00 11.35 ?  116 PHE   A C    1 
ATOM   2368 O  O    . PHE   A 1 116 ? 26.845 -12.966 7.139   1.00 11.85 ?  116 PHE   A O    1 
ATOM   2369 C  CB   . PHE   A 1 116 ? 24.926 -11.839 4.994   1.00 11.17 ?  116 PHE   A CB   1 
ATOM   2370 C  CG   . PHE   A 1 116 ? 24.175 -10.593 4.532   1.00 10.94 ?  116 PHE   A CG   1 
ATOM   2371 C  CD1  . PHE   A 1 116 ? 24.746 -9.565  3.794   1.00 10.93 ?  116 PHE   A CD1  1 
ATOM   2372 C  CD2  . PHE   A 1 116 ? 22.819 -10.496 4.845   1.00 11.33 ?  116 PHE   A CD2  1 
ATOM   2373 C  CE1  . PHE   A 1 116 ? 23.978 -8.483  3.378   1.00 11.34 ?  116 PHE   A CE1  1 
ATOM   2374 C  CE2  . PHE   A 1 116 ? 22.054 -9.424  4.441   1.00 11.56 ?  116 PHE   A CE2  1 
ATOM   2375 C  CZ   . PHE   A 1 116 ? 22.625 -8.415  3.706   1.00 11.06 ?  116 PHE   A CZ   1 
ATOM   2376 H  H    . PHE   A 1 116 ? 26.575 -11.661 3.163   1.00 13.22 ?  116 PHE   A H    1 
ATOM   2377 H  HA   . PHE   A 1 116 ? 26.647 -10.924 5.667   1.00 13.30 ?  116 PHE   A HA   1 
ATOM   2378 H  HB2  . PHE   A 1 116 ? 24.742 -12.544 4.352   1.00 13.38 ?  116 PHE   A HB2  1 
ATOM   2379 H  HB3  . PHE   A 1 116 ? 24.563 -12.095 5.858   1.00 13.38 ?  116 PHE   A HB3  1 
ATOM   2380 H  HD1  . PHE   A 1 116 ? 25.644 -9.618  3.567   1.00 13.10 ?  116 PHE   A HD1  1 
ATOM   2381 H  HD2  . PHE   A 1 116 ? 22.417 -11.186 5.332   1.00 13.58 ?  116 PHE   A HD2  1 
ATOM   2382 H  HE1  . PHE   A 1 116 ? 24.373 -7.799  2.890   1.00 13.58 ?  116 PHE   A HE1  1 
ATOM   2383 H  HE2  . PHE   A 1 116 ? 21.152 -9.393  4.669   1.00 13.85 ?  116 PHE   A HE2  1 
ATOM   2384 H  HZ   . PHE   A 1 116 ? 22.113 -7.686  3.446   1.00 13.25 ?  116 PHE   A HZ   1 
ATOM   2385 N  N    . ASN   A 1 117 ? 27.371 -13.993 5.208   1.00 11.79 ?  117 ASN   A N    1 
ATOM   2386 C  CA   . ASN   A 1 117 ? 27.734 -15.236 5.882   1.00 11.67 ?  117 ASN   A CA   1 
ATOM   2387 C  C    . ASN   A 1 117 ? 28.996 -15.120 6.719   1.00 12.30 ?  117 ASN   A C    1 
ATOM   2388 O  O    . ASN   A 1 117 ? 29.290 -16.043 7.489   1.00 13.13 ?  117 ASN   A O    1 
ATOM   2389 C  CB   . ASN   A 1 117 ? 27.853 -16.367 4.867   1.00 12.00 ?  117 ASN   A CB   1 
ATOM   2390 C  CG   . ASN   A 1 117 ? 26.506 -16.749 4.322   1.00 11.86 ?  117 ASN   A CG   1 
ATOM   2391 O  OD1  . ASN   A 1 117 ? 25.526 -16.764 5.068   1.00 12.70 ?  117 ASN   A OD1  1 
ATOM   2392 N  ND2  . ASN   A 1 117 ? 26.429 -17.013 3.031   1.00 11.92 ?  117 ASN   A ND2  1 
ATOM   2393 H  H    . ASN   A 1 117 ? 27.456 -14.010 4.349   1.00 14.12 ?  117 ASN   A H    1 
ATOM   2394 H  HA   . ASN   A 1 117 ? 27.007 -15.466 6.487   1.00 13.98 ?  117 ASN   A HA   1 
ATOM   2395 H  HB2  . ASN   A 1 117 ? 28.410 -16.078 4.129   1.00 14.38 ?  117 ASN   A HB2  1 
ATOM   2396 H  HB3  . ASN   A 1 117 ? 28.235 -17.144 5.299   1.00 14.38 ?  117 ASN   A HB3  1 
ATOM   2397 H  HD21 . ASN   A 1 117 ? 25.679 -17.227 2.683   1.00 14.29 ?  117 ASN   A HD21 1 
ATOM   2398 H  HD22 . ASN   A 1 117 ? 27.141 -16.978 2.545   1.00 14.29 ?  117 ASN   A HD22 1 
ATOM   2399 N  N    . GLN   A 1 118 ? 29.723 -14.009 6.608   1.00 12.22 ?  118 GLN   A N    1 
ATOM   2400 C  CA   . GLN   A 1 118 ? 30.899 -13.778 7.433   1.00 12.82 ?  118 GLN   A CA   1 
ATOM   2401 C  C    . GLN   A 1 118 ? 30.555 -13.204 8.802   1.00 12.80 ?  118 GLN   A C    1 
ATOM   2402 O  O    . GLN   A 1 118 ? 31.469 -12.909 9.583   1.00 14.27 ?  118 GLN   A O    1 
ATOM   2403 C  CB   . GLN   A 1 118 ? 31.892 -12.877 6.695   1.00 13.22 ?  118 GLN   A CB   1 
ATOM   2404 C  CG   . GLN   A 1 118 ? 32.370 -13.454 5.372   1.00 12.89 ?  118 GLN   A CG   1 
ATOM   2405 C  CD   . GLN   A 1 118 ? 33.203 -14.712 5.554   1.00 13.49 ?  118 GLN   A CD   1 
ATOM   2406 O  OE1  . GLN   A 1 118 ? 34.067 -14.777 6.441   1.00 14.28 ?  118 GLN   A OE1  1 
ATOM   2407 N  NE2  . GLN   A 1 118 ? 32.957 -15.715 4.709   1.00 13.56 ?  118 GLN   A NE2  1 
ATOM   2408 H  H    . GLN   A 1 118 ? 29.547 -13.362 6.058   1.00 14.64 ?  118 GLN   A H    1 
ATOM   2409 H  HA   . GLN   A 1 118 ? 31.329 -14.632 7.578   1.00 15.36 ?  118 GLN   A HA   1 
ATOM   2410 H  HB2  . GLN   A 1 118 ? 31.470 -12.026 6.515   1.00 15.84 ?  118 GLN   A HB2  1 
ATOM   2411 H  HB3  . GLN   A 1 118 ? 32.670 -12.750 7.260   1.00 15.84 ?  118 GLN   A HB3  1 
ATOM   2412 H  HG2  . GLN   A 1 118 ? 31.600 -13.675 4.821   1.00 15.45 ?  118 GLN   A HG2  1 
ATOM   2413 H  HG3  . GLN   A 1 118 ? 32.920 -12.794 4.917   1.00 15.45 ?  118 GLN   A HG3  1 
ATOM   2414 H  HE21 . GLN   A 1 118 ? 32.346 -15.629 4.102   1.00 16.25 ?  118 GLN   A HE21 1 
ATOM   2415 H  HE22 . GLN   A 1 118 ? 33.397 -16.447 4.769   1.00 16.25 ?  118 GLN   A HE22 1 
ATOM   2416 N  N    . HIS   A 1 119 ? 29.267 -13.045 9.109   1.00 12.80 ?  119 HIS   A N    1 
ATOM   2417 C  CA   . HIS   A 1 119 ? 28.810 -12.431 10.351  1.00 12.74 ?  119 HIS   A CA   1 
ATOM   2418 C  C    . HIS   A 1 119 ? 27.668 -13.252 10.925  1.00 13.15 ?  119 HIS   A C    1 
ATOM   2419 O  O    . HIS   A 1 119 ? 26.724 -13.591 10.207  1.00 13.62 ?  119 HIS   A O    1 
ATOM   2420 C  CB   . HIS   A 1 119 ? 28.359 -10.998 10.070  1.00 13.41 ?  119 HIS   A CB   1 
ATOM   2421 C  CG   . HIS   A 1 119 ? 29.447 -10.188 9.463   1.00 14.47 ?  119 HIS   A CG   1 
ATOM   2422 N  ND1  . HIS   A 1 119 ? 30.415 -9.575  10.224  1.00 16.80 ?  119 HIS   A ND1  1 
ATOM   2423 C  CD2  . HIS   A 1 119 ? 29.797 -10.001 8.170   1.00 15.33 ?  119 HIS   A CD2  1 
ATOM   2424 C  CE1  . HIS   A 1 119 ? 31.289 -8.996  9.421   1.00 16.96 ?  119 HIS   A CE1  1 
ATOM   2425 N  NE2  . HIS   A 1 119 ? 30.945 -9.248  8.171   1.00 16.74 ?  119 HIS   A NE2  1 
ATOM   2426 H  H    . HIS   A 1 119 ? 28.617 -13.308 8.604   1.00 15.34 ?  119 HIS   A H    1 
ATOM   2427 H  HA   . HIS   A 1 119 ? 29.541 -12.418 10.994  1.00 15.26 ?  119 HIS   A HA   1 
ATOM   2428 H  HB2  . HIS   A 1 119 ? 27.611 -11.026 9.453   1.00 16.07 ?  119 HIS   A HB2  1 
ATOM   2429 H  HB3  . HIS   A 1 119 ? 28.098 -10.586 10.903  1.00 16.07 ?  119 HIS   A HB3  1 
ATOM   2430 H  HD2  . HIS   A 1 119 ? 29.344 -10.316 7.417   1.00 18.37 ?  119 HIS   A HD2  1 
ATOM   2431 H  HE1  . HIS   A 1 119 ? 32.026 -8.498  9.688   1.00 20.33 ?  119 HIS   A HE1  1 
ATOM   2432 H  HE2  . HIS   A 1 119 ? 31.356 -8.957  7.470   1.00 20.06 ?  119 HIS   A HE2  1 
ATOM   2433 N  N    . GLU   A 1 120 ? 27.750 -13.557 12.221  1.00 14.03 ?  120 GLU   A N    1 
ATOM   2434 C  CA   . GLU   A 1 120 ? 26.790 -14.479 12.826  1.00 16.34 ?  120 GLU   A CA   1 
ATOM   2435 C  C    . GLU   A 1 120 ? 25.376 -13.911 12.881  1.00 14.91 ?  120 GLU   A C    1 
ATOM   2436 O  O    . GLU   A 1 120 ? 24.403 -14.675 12.775  1.00 15.12 ?  120 GLU   A O    1 
ATOM   2437 C  CB   . GLU   A 1 120 ? 27.255 -14.864 14.230  1.00 21.18 ?  120 GLU   A CB   1 
ATOM   2438 C  CG   . GLU   A 1 120 ? 28.435 -15.820 14.250  1.00 28.62 ?  120 GLU   A CG   1 
ATOM   2439 C  CD   . GLU   A 1 120 ? 28.585 -16.530 15.582  1.00 35.54 ?  120 GLU   A CD   1 
ATOM   2440 O  OE1  . GLU   A 1 120 ? 28.191 -15.949 16.616  1.00 37.30 ?  120 GLU   A OE1  1 
ATOM   2441 O  OE2  . GLU   A 1 120 ? 29.091 -17.673 15.596  1.00 39.29 -1 120 GLU   A OE2  1 
ATOM   2442 H  H    . GLU   A 1 120 ? 28.347 -13.250 12.764  1.00 16.82 ?  120 GLU   A H    1 
ATOM   2443 H  HA   . GLU   A 1 120 ? 26.767 -15.289 12.300  1.00 19.58 ?  120 GLU   A HA   1 
ATOM   2444 H  HB2  . GLU   A 1 120 ? 27.523 -14.068 14.714  1.00 25.39 ?  120 GLU   A HB2  1 
ATOM   2445 H  HB3  . GLU   A 1 120 ? 26.524 -15.300 14.700  1.00 25.39 ?  120 GLU   A HB3  1 
ATOM   2446 H  HG2  . GLU   A 1 120 ? 28.320 -16.491 13.559  1.00 34.32 ?  120 GLU   A HG2  1 
ATOM   2447 H  HG3  . GLU   A 1 120 ? 29.255 -15.327 14.104  1.00 34.32 ?  120 GLU   A HG3  1 
ATOM   2448 N  N    . VAL   A 1 121 ? 25.244 -12.598 13.081  1.00 14.13 ?  121 VAL   A N    1 
ATOM   2449 C  CA   . VAL   A 1 121 ? 23.950 -11.929 13.203  1.00 13.87 ?  121 VAL   A CA   1 
ATOM   2450 C  C    . VAL   A 1 121 ? 24.059 -10.552 12.558  1.00 12.82 ?  121 VAL   A C    1 
ATOM   2451 O  O    . VAL   A 1 121 ? 25.031 -9.828  12.791  1.00 13.37 ?  121 VAL   A O    1 
ATOM   2452 C  CB   . VAL   A 1 121 ? 23.521 -11.772 14.681  1.00 16.66 ?  121 VAL   A CB   1 
ATOM   2453 C  CG1  . VAL   A 1 121 ? 22.136 -11.144 14.772  1.00 17.15 ?  121 VAL   A CG1  1 
ATOM   2454 C  CG2  . VAL   A 1 121 ? 23.543 -13.099 15.418  1.00 18.76 ?  121 VAL   A CG2  1 
ATOM   2455 H  H    . VAL   A 1 121 ? 25.911 -12.056 13.151  1.00 16.93 ?  121 VAL   A H    1 
ATOM   2456 H  HA   . VAL   A 1 121 ? 23.274 -12.445 12.738  1.00 16.62 ?  121 VAL   A HA   1 
ATOM   2457 H  HB   . VAL   A 1 121 ? 24.142 -11.178 15.125  1.00 19.97 ?  121 VAL   A HB   1 
ATOM   2458 H  HG11 . VAL   A 1 121 ? 21.826 -11.196 15.691  1.00 20.56 ?  121 VAL   A HG11 1 
ATOM   2459 H  HG12 . VAL   A 1 121 ? 22.187 -10.216 14.495  1.00 20.56 ?  121 VAL   A HG12 1 
ATOM   2460 H  HG13 . VAL   A 1 121 ? 21.527 -11.631 14.193  1.00 20.56 ?  121 VAL   A HG13 1 
ATOM   2461 H  HG21 . VAL   A 1 121 ? 23.197 -12.967 16.319  1.00 22.49 ?  121 VAL   A HG21 1 
ATOM   2462 H  HG22 . VAL   A 1 121 ? 22.981 -13.736 14.945  1.00 22.49 ?  121 VAL   A HG22 1 
ATOM   2463 H  HG23 . VAL   A 1 121 ? 24.452 -13.427 15.460  1.00 22.49 ?  121 VAL   A HG23 1 
ATOM   2464 N  N    . LEU   A 1 122 ? 23.045 -10.167 11.780  1.00 12.30 ?  122 LEU   A N    1 
ATOM   2465 C  CA   . LEU   A 1 122 ? 23.054 -8.878  11.097  1.00 11.85 ?  122 LEU   A CA   1 
ATOM   2466 C  C    . LEU   A 1 122 ? 21.656 -8.286  11.067  1.00 11.70 ?  122 LEU   A C    1 
ATOM   2467 O  O    . LEU   A 1 122 ? 20.666 -9.006  10.927  1.00 12.71 ?  122 LEU   A O    1 
ATOM   2468 C  CB   . LEU   A 1 122 ? 23.473 -8.990  9.628   1.00 13.02 ?  122 LEU   A CB   1 
ATOM   2469 C  CG   . LEU   A 1 122 ? 24.686 -9.838  9.275   1.00 13.21 ?  122 LEU   A CG   1 
ATOM   2470 C  CD1  . LEU   A 1 122 ? 24.285 -11.284 9.045   1.00 14.02 ?  122 LEU   A CD1  1 
ATOM   2471 C  CD2  . LEU   A 1 122 ? 25.385 -9.270  8.049   1.00 12.86 ?  122 LEU   A CD2  1 
ATOM   2472 H  H    . LEU   A 1 122 ? 22.336 -10.636 11.628  1.00 14.74 ?  122 LEU   A H    1 
ATOM   2473 H  HA   . LEU   A 1 122 ? 23.650 -8.260  11.549  1.00 14.20 ?  122 LEU   A HA   1 
ATOM   2474 H  HB2  . LEU   A 1 122 ? 22.732 -9.361  9.132   1.00 15.61 ?  122 LEU   A HB2  1 
ATOM   2475 H  HB3  . LEU   A 1 122 ? 23.664 -8.101  9.300   1.00 15.61 ?  122 LEU   A HB3  1 
ATOM   2476 H  HG   . LEU   A 1 122 ? 25.323 -9.825  10.008  1.00 15.83 ?  122 LEU   A HG   1 
ATOM   2477 H  HD11 . LEU   A 1 122 ? 25.066 -11.805 8.799   1.00 16.80 ?  122 LEU   A HD11 1 
ATOM   2478 H  HD12 . LEU   A 1 122 ? 23.898 -11.641 9.862   1.00 16.80 ?  122 LEU   A HD12 1 
ATOM   2479 H  HD13 . LEU   A 1 122 ? 23.627 -11.323 8.329   1.00 16.80 ?  122 LEU   A HD13 1 
ATOM   2480 H  HD21 . LEU   A 1 122 ? 26.135 -9.844  7.807   1.00 15.41 ?  122 LEU   A HD21 1 
ATOM   2481 H  HD22 . LEU   A 1 122 ? 24.756 -9.230  7.312   1.00 15.41 ?  122 LEU   A HD22 1 
ATOM   2482 H  HD23 . LEU   A 1 122 ? 25.712 -8.379  8.254   1.00 15.41 ?  122 LEU   A HD23 1 
ATOM   2483 N  N    . LEU   A 1 123 ? 21.594 -6.957  11.170  1.00 11.41 ?  123 LEU   A N    1 
ATOM   2484 C  CA   . LEU   A 1 123 ? 20.426 -6.162  10.800  1.00 11.08 ?  123 LEU   A CA   1 
ATOM   2485 C  C    . LEU   A 1 123 ? 20.674 -5.638  9.393   1.00 10.80 ?  123 LEU   A C    1 
ATOM   2486 O  O    . LEU   A 1 123 ? 21.724 -5.043  9.147   1.00 11.45 ?  123 LEU   A O    1 
ATOM   2487 C  CB   . LEU   A 1 123 ? 20.289 -4.985  11.768  1.00 11.89 ?  123 LEU   A CB   1 
ATOM   2488 C  CG   . LEU   A 1 123 ? 19.242 -3.927  11.418  1.00 12.55 ?  123 LEU   A CG   1 
ATOM   2489 C  CD1  . LEU   A 1 123 ? 17.846 -4.530  11.401  1.00 13.09 ?  123 LEU   A CD1  1 
ATOM   2490 C  CD2  . LEU   A 1 123 ? 19.321 -2.755  12.396  1.00 13.33 ?  123 LEU   A CD2  1 
ATOM   2491 H  H    . LEU   A 1 123 ? 22.246 -6.475  11.461  1.00 13.67 ?  123 LEU   A H    1 
ATOM   2492 H  HA   . LEU   A 1 123 ? 19.619 -6.702  10.819  1.00 13.28 ?  123 LEU   A HA   1 
ATOM   2493 H  HB2  . LEU   A 1 123 ? 20.054 -5.334  12.645  1.00 14.25 ?  123 LEU   A HB2  1 
ATOM   2494 H  HB3  . LEU   A 1 123 ? 21.140 -4.529  11.823  1.00 14.25 ?  123 LEU   A HB3  1 
ATOM   2495 H  HG   . LEU   A 1 123 ? 19.419 -3.580  10.531  1.00 15.04 ?  123 LEU   A HG   1 
ATOM   2496 H  HD11 . LEU   A 1 123 ? 17.194 -3.835  11.227  1.00 15.69 ?  123 LEU   A HD11 1 
ATOM   2497 H  HD12 . LEU   A 1 123 ? 17.799 -5.207  10.704  1.00 15.69 ?  123 LEU   A HD12 1 
ATOM   2498 H  HD13 . LEU   A 1 123 ? 17.666 -4.941  12.265  1.00 15.69 ?  123 LEU   A HD13 1 
ATOM   2499 H  HD21 . LEU   A 1 123 ? 18.646 -2.097  12.160  1.00 15.98 ?  123 LEU   A HD21 1 
ATOM   2500 H  HD22 . LEU   A 1 123 ? 19.154 -3.085  13.296  1.00 15.98 ?  123 LEU   A HD22 1 
ATOM   2501 H  HD23 . LEU   A 1 123 ? 20.202 -2.362  12.345  1.00 15.98 ?  123 LEU   A HD23 1 
ATOM   2502 N  N    A ALA   A 1 124 ? 19.711 -5.806  8.482   0.72 10.30 ?  124 ALA   A N    1 
ATOM   2503 N  N    B ALA   A 1 124 ? 19.753 -5.894  8.474   0.28 10.62 ?  124 ALA   A N    1 
ATOM   2504 C  CA   A ALA   A 1 124 ? 20.007 -5.531  7.082   0.72 10.09 ?  124 ALA   A CA   1 
ATOM   2505 C  CA   B ALA   A 1 124 ? 20.025 -5.621  7.074   0.28 10.63 ?  124 ALA   A CA   1 
ATOM   2506 C  C    A ALA   A 1 124 ? 18.767 -5.099  6.312   0.72 10.01 ?  124 ALA   A C    1 
ATOM   2507 C  C    B ALA   A 1 124 ? 18.799 -5.056  6.378   0.28 10.72 ?  124 ALA   A C    1 
ATOM   2508 O  O    A ALA   A 1 124 ? 17.640 -5.488  6.651   0.72 10.61 ?  124 ALA   A O    1 
ATOM   2509 O  O    B ALA   A 1 124 ? 17.663 -5.284  6.808   0.28 10.89 ?  124 ALA   A O    1 
ATOM   2510 C  CB   A ALA   A 1 124 ? 20.617 -6.757  6.399   0.72 10.66 ?  124 ALA   A CB   1 
ATOM   2511 C  CB   B ALA   A 1 124 ? 20.488 -6.883  6.334   0.28 10.55 ?  124 ALA   A CB   1 
ATOM   2512 H  H    A ALA   A 1 124 ? 18.905 -6.070  8.644   0.72 12.34 ?  124 ALA   A H    1 
ATOM   2513 H  H    B ALA   A 1 124 ? 18.973 -6.228  8.634   0.28 12.72 ?  124 ALA   A H    1 
ATOM   2514 H  HA   A ALA   A 1 124 ? 20.658 -4.814  7.046   0.72 12.08 ?  124 ALA   A HA   1 
ATOM   2515 H  HA   B ALA   A 1 124 ? 20.736 -4.966  7.024   0.28 12.74 ?  124 ALA   A HA   1 
ATOM   2516 H  HB1  A ALA   A 1 124 ? 20.810 -6.545  5.472   0.72 12.77 ?  124 ALA   A HB1  1 
ATOM   2517 H  HB1  B ALA   A 1 124 ? 20.663 -6.662  5.405   0.28 12.63 ?  124 ALA   A HB1  1 
ATOM   2518 H  HB2  A ALA   A 1 124 ? 21.445 -6.996  6.856   0.72 12.77 ?  124 ALA   A HB2  1 
ATOM   2519 H  HB2  B ALA   A 1 124 ? 21.302 -7.216  6.750   0.28 12.63 ?  124 ALA   A HB2  1 
ATOM   2520 H  HB3  A ALA   A 1 124 ? 19.993 -7.495  6.448   0.72 12.77 ?  124 ALA   A HB3  1 
ATOM   2521 H  HB3  B ALA   A 1 124 ? 19.794 -7.558  6.388   0.28 12.63 ?  124 ALA   A HB3  1 
ATOM   2522 N  N    A PRO   A 1 125 ? 18.958 -4.359  5.221   0.72 9.87  ?  125 PRO   A N    1 
ATOM   2523 N  N    B PRO   A 1 125 ? 19.005 -4.312  5.295   0.28 10.89 ?  125 PRO   A N    1 
ATOM   2524 C  CA   A PRO   A 1 125 ? 17.902 -4.125  4.237   0.72 10.08 ?  125 PRO   A CA   1 
ATOM   2525 C  CA   B PRO   A 1 125 ? 17.901 -3.966  4.401   0.28 11.23 ?  125 PRO   A CA   1 
ATOM   2526 C  C    A PRO   A 1 125 ? 17.961 -5.197  3.155   0.72 9.85  ?  125 PRO   A C    1 
ATOM   2527 C  C    B PRO   A 1 125 ? 17.846 -4.974  3.266   0.28 11.49 ?  125 PRO   A C    1 
ATOM   2528 O  O    A PRO   A 1 125 ? 18.933 -5.948  3.037   0.72 10.17 ?  125 PRO   A O    1 
ATOM   2529 O  O    B PRO   A 1 125 ? 18.728 -5.833  3.161   0.28 11.62 ?  125 PRO   A O    1 
ATOM   2530 C  CB   A PRO   A 1 125 ? 18.339 -2.785  3.633   0.72 10.24 ?  125 PRO   A CB   1 
ATOM   2531 C  CB   B PRO   A 1 125 ? 18.322 -2.590  3.881   0.28 11.20 ?  125 PRO   A CB   1 
ATOM   2532 C  CG   A PRO   A 1 125 ? 19.855 -2.951  3.543   0.72 10.10 ?  125 PRO   A CG   1 
ATOM   2533 C  CG   B PRO   A 1 125 ? 19.830 -2.723  3.764   0.28 11.43 ?  125 PRO   A CG   1 
ATOM   2534 C  CD   A PRO   A 1 125 ? 20.221 -3.704  4.820   0.72 10.35 ?  125 PRO   A CD   1 
ATOM   2535 C  CD   B PRO   A 1 125 ? 20.268 -3.687  4.857   0.28 11.33 ?  125 PRO   A CD   1 
ATOM   2536 H  HA   A PRO   A 1 125 ? 17.020 -4.078  4.638   0.72 12.08 ?  125 PRO   A HA   1 
ATOM   2537 H  HA   B PRO   A 1 125 ? 17.051 -3.916  4.875   0.28 13.45 ?  125 PRO   A HA   1 
ATOM   2538 H  HB2  A PRO   A 1 125 ? 17.936 -2.672  2.754   0.72 12.27 ?  125 PRO   A HB2  1 
ATOM   2539 H  HB2  B PRO   A 1 125 ? 17.921 -2.432  3.013   0.28 13.42 ?  125 PRO   A HB2  1 
ATOM   2540 H  HB3  A PRO   A 1 125 ? 18.090 -2.062  4.228   0.72 12.27 ?  125 PRO   A HB3  1 
ATOM   2541 H  HB3  B PRO   A 1 125 ? 18.071 -1.897  4.515   0.28 13.42 ?  125 PRO   A HB3  1 
ATOM   2542 H  HG2  A PRO   A 1 125 ? 20.087 -3.473  2.755   0.72 12.10 ?  125 PRO   A HG2  1 
ATOM   2543 H  HG2  B PRO   A 1 125 ? 20.054 -3.077  2.889   0.28 13.70 ?  125 PRO   A HG2  1 
ATOM   2544 H  HG3  A PRO   A 1 125 ? 20.280 -2.080  3.515   0.72 12.10 ?  125 PRO   A HG3  1 
ATOM   2545 H  HG3  B PRO   A 1 125 ? 20.242 -1.856  3.892   0.28 13.70 ?  125 PRO   A HG3  1 
ATOM   2546 H  HD2  A PRO   A 1 125 ? 20.912 -4.358  4.640   0.72 12.39 ?  125 PRO   A HD2  1 
ATOM   2547 H  HD2  B PRO   A 1 125 ? 20.870 -4.357  4.495   0.28 13.57 ?  125 PRO   A HD2  1 
ATOM   2548 H  HD3  A PRO   A 1 125 ? 20.498 -3.075  5.508   0.72 12.39 ?  125 PRO   A HD3  1 
ATOM   2549 H  HD3  B PRO   A 1 125 ? 20.677 -3.201  5.590   0.28 13.57 ?  125 PRO   A HD3  1 
ATOM   2550 N  N    A LEU   A 1 126 ? 16.912 -5.232  2.339   0.72 9.91  ?  126 LEU   A N    1 
ATOM   2551 N  N    B LEU   A 1 126 ? 16.841 -4.874  2.403   0.28 11.98 ?  126 LEU   A N    1 
ATOM   2552 C  CA   A LEU   A 1 126 ? 16.934 -6.049  1.135   0.72 10.08 ?  126 LEU   A CA   1 
ATOM   2553 C  CA   B LEU   A 1 126 ? 16.754 -5.732  1.226   0.28 12.43 ?  126 LEU   A CA   1 
ATOM   2554 C  C    A LEU   A 1 126 ? 17.868 -5.425  0.102   0.72 10.21 ?  126 LEU   A C    1 
ATOM   2555 C  C    B LEU   A 1 126 ? 17.704 -5.193  0.161   0.28 11.71 ?  126 LEU   A C    1 
ATOM   2556 O  O    A LEU   A 1 126 ? 17.656 -4.297  -0.353  0.72 11.39 ?  126 LEU   A O    1 
ATOM   2557 O  O    B LEU   A 1 126 ? 17.445 -4.141  -0.433  0.28 12.25 ?  126 LEU   A O    1 
ATOM   2558 C  CB   A LEU   A 1 126 ? 15.524 -6.193  0.576   0.72 10.38 ?  126 LEU   A CB   1 
ATOM   2559 C  CB   B LEU   A 1 126 ? 15.317 -5.728  0.713   0.28 14.22 ?  126 LEU   A CB   1 
ATOM   2560 C  CG   A LEU   A 1 126 ? 14.606 -7.099  1.402   0.72 11.01 ?  126 LEU   A CG   1 
ATOM   2561 C  CG   B LEU   A 1 126 ? 14.670 -7.028  0.231   0.28 15.73 ?  126 LEU   A CG   1 
ATOM   2562 C  CD1  A LEU   A 1 126 ? 13.161 -6.948  0.966   0.72 12.48 ?  126 LEU   A CD1  1 
ATOM   2563 C  CD1  B LEU   A 1 126 ? 14.970 -8.177  1.168   0.28 16.27 ?  126 LEU   A CD1  1 
ATOM   2564 C  CD2  A LEU   A 1 126 ? 15.050 -8.568  1.291   0.72 11.66 ?  126 LEU   A CD2  1 
ATOM   2565 C  CD2  B LEU   A 1 126 ? 13.170 -6.833  0.122   0.28 15.99 ?  126 LEU   A CD2  1 
ATOM   2566 H  H    A LEU   A 1 126 ? 16.189 -4.791  2.453   0.72 11.87 ?  126 LEU   A H    1 
ATOM   2567 H  H    B LEU   A 1 126 ? 16.189 -4.317  2.484   0.28 14.35 ?  126 LEU   A H    1 
ATOM   2568 H  HA   A LEU   A 1 126 ? 17.269 -6.936  1.351   0.72 12.07 ?  126 LEU   A HA   1 
ATOM   2569 H  HA   B LEU   A 1 126 ? 17.026 -6.635  1.460   0.28 14.90 ?  126 LEU   A HA   1 
ATOM   2570 H  HB2  A LEU   A 1 126 ? 15.111 -5.319  0.539   0.72 12.43 ?  126 LEU   A HB2  1 
ATOM   2571 H  HB2  B LEU   A 1 126 ? 14.756 -5.390  1.425   0.28 17.04 ?  126 LEU   A HB2  1 
ATOM   2572 H  HB3  A LEU   A 1 126 ? 15.575 -6.571  -0.317  0.72 12.43 ?  126 LEU   A HB3  1 
ATOM   2573 H  HB3  B LEU   A 1 126 ? 15.283 -5.108  -0.032  0.28 17.04 ?  126 LEU   A HB3  1 
ATOM   2574 H  HG   A LEU   A 1 126 ? 14.660 -6.843  2.336   0.72 13.20 ?  126 LEU   A HG   1 
ATOM   2575 H  HG   B LEU   A 1 126 ? 15.013 -7.248  -0.650  0.28 18.85 ?  126 LEU   A HG   1 
ATOM   2576 H  HD11 A LEU   A 1 126 ? 12.603 -7.535  1.504   0.72 14.96 ?  126 LEU   A HD11 1 
ATOM   2577 H  HD11 B LEU   A 1 126 ? 14.337 -8.890  1.000   0.28 19.50 ?  126 LEU   A HD11 1 
ATOM   2578 H  HD12 A LEU   A 1 126 ? 12.888 -6.028  1.089   0.72 14.96 ?  126 LEU   A HD12 1 
ATOM   2579 H  HD12 B LEU   A 1 126 ? 15.873 -8.488  1.005   0.28 19.50 ?  126 LEU   A HD12 1 
ATOM   2580 H  HD13 A LEU   A 1 126 ? 13.086 -7.195  0.029   0.72 14.96 ?  126 LEU   A HD13 1 
ATOM   2581 H  HD13 B LEU   A 1 126 ? 14.883 -7.865  2.082   0.28 19.50 ?  126 LEU   A HD13 1 
ATOM   2582 H  HD21 A LEU   A 1 126 ? 14.382 -9.135  1.706   0.72 13.97 ?  126 LEU   A HD21 1 
ATOM   2583 H  HD21 B LEU   A 1 126 ? 12.768 -7.651  -0.208  0.28 19.17 ?  126 LEU   A HD21 1 
ATOM   2584 H  HD22 A LEU   A 1 126 ? 15.144 -8.798  0.353   0.72 13.97 ?  126 LEU   A HD22 1 
ATOM   2585 H  HD22 B LEU   A 1 126 ? 12.816 -6.625  1.002   0.28 19.17 ?  126 LEU   A HD22 1 
ATOM   2586 H  HD23 A LEU   A 1 126 ? 15.902 -8.675  1.744   0.72 13.97 ?  126 LEU   A HD23 1 
ATOM   2587 H  HD23 B LEU   A 1 126 ? 12.988 -6.102  -0.487  0.28 19.17 ?  126 LEU   A HD23 1 
ATOM   2588 N  N    A LEU   A 1 127 ? 18.907 -6.167  -0.267  0.72 10.18 ?  127 LEU   A N    1 
ATOM   2589 N  N    B LEU   A 1 127 ? 18.800 -5.904  -0.092  0.28 11.16 ?  127 LEU   A N    1 
ATOM   2590 C  CA   A LEU   A 1 127 ? 19.896 -5.672  -1.211  0.72 9.85  ?  127 LEU   A CA   1 
ATOM   2591 C  CA   B LEU   A 1 127 ? 19.797 -5.402  -1.029  0.28 11.08 ?  127 LEU   A CA   1 
ATOM   2592 C  C    A LEU   A 1 127 ? 19.281 -5.487  -2.587  0.72 9.40  ?  127 LEU   A C    1 
ATOM   2593 C  C    B LEU   A 1 127 ? 19.213 -5.280  -2.430  0.28 11.19 ?  127 LEU   A C    1 
ATOM   2594 O  O    A LEU   A 1 127 ? 18.460 -6.286  -3.042  0.72 9.82  ?  127 LEU   A O    1 
ATOM   2595 O  O    B LEU   A 1 127 ? 18.365 -6.070  -2.852  0.28 11.63 ?  127 LEU   A O    1 
ATOM   2596 C  CB   A LEU   A 1 127 ? 21.067 -6.649  -1.306  0.72 10.94 ?  127 LEU   A CB   1 
ATOM   2597 C  CB   B LEU   A 1 127 ? 21.020 -6.318  -1.068  0.28 11.03 ?  127 LEU   A CB   1 
ATOM   2598 C  CG   A LEU   A 1 127 ? 21.852 -6.900  -0.022  0.72 11.70 ?  127 LEU   A CG   1 
ATOM   2599 C  CG   B LEU   A 1 127 ? 21.850 -6.364  0.214   0.28 10.97 ?  127 LEU   A CG   1 
ATOM   2600 C  CD1  A LEU   A 1 127 ? 22.954 -7.893  -0.302  0.72 11.78 ?  127 LEU   A CD1  1 
ATOM   2601 C  CD1  B LEU   A 1 127 ? 23.012 -7.328  0.049   0.28 11.22 ?  127 LEU   A CD1  1 
ATOM   2602 C  CD2  A LEU   A 1 127 ? 22.444 -5.615  0.511   0.72 12.44 ?  127 LEU   A CD2  1 
ATOM   2603 C  CD2  B LEU   A 1 127 ? 22.347 -4.974  0.608   0.28 11.26 ?  127 LEU   A CD2  1 
ATOM   2604 H  H    A LEU   A 1 127 ? 19.064 -6.965  0.021   0.72 12.20 ?  127 LEU   A H    1 
ATOM   2605 H  H    B LEU   A 1 127 ? 18.986 -6.668  0.259   0.28 13.37 ?  127 LEU   A H    1 
ATOM   2606 H  HA   A LEU   A 1 127 ? 20.232 -4.817  -0.907  0.72 11.79 ?  127 LEU   A HA   1 
ATOM   2607 H  HA   B LEU   A 1 127 ? 20.082 -4.521  -0.744  0.28 13.28 ?  127 LEU   A HA   1 
ATOM   2608 H  HB2  A LEU   A 1 127 ? 20.724 -7.507  -1.604  0.72 13.10 ?  127 LEU   A HB2  1 
ATOM   2609 H  HB2  B LEU   A 1 127 ? 20.720 -7.220  -1.259  0.28 13.21 ?  127 LEU   A HB2  1 
ATOM   2610 H  HB3  A LEU   A 1 127 ? 21.695 -6.309  -1.960  0.72 13.10 ?  127 LEU   A HB3  1 
ATOM   2611 H  HB3  B LEU   A 1 127 ? 21.601 -6.013  -1.785  0.28 13.21 ?  127 LEU   A HB3  1 
ATOM   2612 H  HG   A LEU   A 1 127 ? 21.260 -7.279  0.654   0.72 14.02 ?  127 LEU   A HG   1 
ATOM   2613 H  HG   B LEU   A 1 127 ? 21.290 -6.694  0.932   0.28 13.14 ?  127 LEU   A HG   1 
ATOM   2614 H  HD11 A LEU   A 1 127 ? 23.435 -8.074  0.521   0.72 14.11 ?  127 LEU   A HD11 1 
ATOM   2615 H  HD11 B LEU   A 1 127 ? 23.553 -7.306  0.853   0.28 13.44 ?  127 LEU   A HD11 1 
ATOM   2616 H  HD12 A LEU   A 1 127 ? 22.564 -8.716  -0.642  0.72 14.11 ?  127 LEU   A HD12 1 
ATOM   2617 H  HD12 B LEU   A 1 127 ? 22.662 -8.222  -0.091  0.28 13.44 ?  127 LEU   A HD12 1 
ATOM   2618 H  HD13 A LEU   A 1 127 ? 23.555 -7.517  -0.962  0.72 14.11 ?  127 LEU   A HD13 1 
ATOM   2619 H  HD13 B LEU   A 1 127 ? 23.542 -7.056  -0.716  0.28 13.44 ?  127 LEU   A HD13 1 
ATOM   2620 H  HD21 A LEU   A 1 127 ? 23.034 -5.823  1.251   0.72 14.90 ?  127 LEU   A HD21 1 
ATOM   2621 H  HD21 B LEU   A 1 127 ? 23.007 -5.066  1.312   0.28 13.49 ?  127 LEU   A HD21 1 
ATOM   2622 H  HD22 A LEU   A 1 127 ? 22.946 -5.185  -0.201  0.72 14.90 ?  127 LEU   A HD22 1 
ATOM   2623 H  HD22 B LEU   A 1 127 ? 22.745 -4.550  -0.167  0.28 13.49 ?  127 LEU   A HD22 1 
ATOM   2624 H  HD23 A LEU   A 1 127 ? 21.728 -5.035  0.808   0.72 14.90 ?  127 LEU   A HD23 1 
ATOM   2625 H  HD23 B LEU   A 1 127 ? 21.596 -4.448  0.925   0.28 13.49 ?  127 LEU   A HD23 1 
ATOM   2626 N  N    A SER   A 1 128 ? 19.709 -4.430  -3.261  0.72 9.83  ?  128 SER   A N    1 
ATOM   2627 N  N    B SER   A 1 128 ? 19.685 -4.265  -3.150  0.28 11.24 ?  128 SER   A N    1 
ATOM   2628 C  CA   A SER   A 1 128 ? 19.305 -4.060  -4.608  0.72 10.22 ?  128 SER   A CA   1 
ATOM   2629 C  CA   B SER   A 1 128 ? 19.332 -3.938  -4.528  0.28 11.33 ?  128 SER   A CA   1 
ATOM   2630 C  C    A SER   A 1 128 ? 17.844 -3.622  -4.706  0.72 10.48 ?  128 SER   A C    1 
ATOM   2631 C  C    B SER   A 1 128 ? 17.888 -3.482  -4.707  0.28 11.57 ?  128 SER   A C    1 
ATOM   2632 O  O    A SER   A 1 128 ? 17.392 -3.315  -5.808  0.72 12.25 ?  128 SER   A O    1 
ATOM   2633 O  O    B SER   A 1 128 ? 17.492 -3.193  -5.841  0.28 11.67 ?  128 SER   A O    1 
ATOM   2634 C  CB   A SER   A 1 128 ? 19.642 -5.127  -5.663  0.72 11.03 ?  128 SER   A CB   1 
ATOM   2635 C  CB   B SER   A 1 128 ? 19.671 -5.050  -5.532  0.28 11.07 ?  128 SER   A CB   1 
ATOM   2636 O  OG   A SER   A 1 128 ? 21.047 -5.351  -5.723  0.72 11.68 ?  128 SER   A OG   1 
ATOM   2637 O  OG   B SER   A 1 128 ? 21.077 -5.193  -5.657  0.28 11.08 ?  128 SER   A OG   1 
ATOM   2638 H  H    A SER   A 1 128 ? 20.297 -3.888  -2.939  0.72 11.78 ?  128 SER   A H    1 
ATOM   2639 H  H    B SER   A 1 128 ? 20.265 -3.712  -2.837  0.28 13.46 ?  128 SER   A H    1 
ATOM   2640 H  HA   A SER   A 1 128 ? 19.831 -3.285  -4.846  0.72 12.24 ?  128 SER   A HA   1 
ATOM   2641 H  HA   B SER   A 1 128 ? 19.880 -3.183  -4.779  0.28 13.58 ?  128 SER   A HA   1 
ATOM   2642 H  HB2  A SER   A 1 128 ? 19.192 -5.954  -5.436  0.72 13.21 ?  128 SER   A HB2  1 
ATOM   2643 H  HB2  B SER   A 1 128 ? 19.287 -5.883  -5.224  0.28 13.26 ?  128 SER   A HB2  1 
ATOM   2644 H  HB3  A SER   A 1 128 ? 19.330 -4.813  -6.534  0.72 13.21 ?  128 SER   A HB3  1 
ATOM   2645 H  HB3  B SER   A 1 128 ? 19.298 -4.812  -6.400  0.28 13.26 ?  128 SER   A HB3  1 
ATOM   2646 H  HG   A SER   A 1 128 ? 21.440 -4.637  -5.925  0.72 14.00 ?  128 SER   A HG   1 
ATOM   2647 H  HG   B SER   A 1 128 ? 21.411 -4.466  -5.915  0.28 13.27 ?  128 SER   A HG   1 
ATOM   2648 N  N    A ALA   A 1 129 ? 17.108 -3.565  -3.595  0.72 11.05 ?  129 ALA   A N    1 
ATOM   2649 N  N    B ALA   A 1 129 ? 17.101 -3.379  -3.640  0.28 12.23 ?  129 ALA   A N    1 
ATOM   2650 C  CA   A ALA   A 1 129 ? 15.732 -3.087  -3.593  0.72 11.34 ?  129 ALA   A CA   1 
ATOM   2651 C  CA   B ALA   A 1 129 ? 15.751 -2.850  -3.737  0.28 12.92 ?  129 ALA   A CA   1 
ATOM   2652 C  C    A ALA   A 1 129 ? 15.726 -1.556  -3.551  0.72 10.75 ?  129 ALA   A C    1 
ATOM   2653 C  C    B ALA   A 1 129 ? 15.763 -1.329  -3.619  0.28 13.20 ?  129 ALA   A C    1 
ATOM   2654 O  O    A ALA   A 1 129 ? 16.765 -0.895  -3.661  0.72 10.76 ?  129 ALA   A O    1 
ATOM   2655 O  O    B ALA   A 1 129 ? 16.790 -0.700  -3.357  0.28 13.28 ?  129 ALA   A O    1 
ATOM   2656 C  CB   A ALA   A 1 129 ? 14.953 -3.723  -2.440  0.72 12.78 ?  129 ALA   A CB   1 
ATOM   2657 C  CB   B ALA   A 1 129 ? 14.851 -3.460  -2.663  0.28 13.58 ?  129 ALA   A CB   1 
ATOM   2658 H  H    A ALA   A 1 129 ? 17.398 -3.801  -2.813  0.72 13.24 ?  129 ALA   A H    1 
ATOM   2659 H  H    B ALA   A 1 129 ? 17.327 -3.605  -2.841  0.28 14.65 ?  129 ALA   A H    1 
ATOM   2660 H  HA   A ALA   A 1 129 ? 15.315 -3.369  -4.418  0.72 13.59 ?  129 ALA   A HA   1 
ATOM   2661 H  HA   B ALA   A 1 129 ? 15.382 -3.073  -4.601  0.28 15.48 ?  129 ALA   A HA   1 
ATOM   2662 H  HB1  A ALA   A 1 129 ? 14.039 -3.397  -2.464  0.72 15.31 ?  129 ALA   A HB1  1 
ATOM   2663 H  HB1  B ALA   A 1 129 ? 13.993 -3.003  -2.671  0.28 16.28 ?  129 ALA   A HB1  1 
ATOM   2664 H  HB2  A ALA   A 1 129 ? 14.965 -4.686  -2.541  0.72 15.31 ?  129 ALA   A HB2  1 
ATOM   2665 H  HB2  B ALA   A 1 129 ? 14.727 -4.400  -2.855  0.28 16.28 ?  129 ALA   A HB2  1 
ATOM   2666 H  HB3  A ALA   A 1 129 ? 15.370 -3.472  -1.599  0.72 15.31 ?  129 ALA   A HB3  1 
ATOM   2667 H  HB3  B ALA   A 1 129 ? 15.272 -3.349  -1.799  0.28 16.28 ?  129 ALA   A HB3  1 
ATOM   2668 N  N    A GLY   A 1 130 ? 14.535 -0.979  -3.417  0.72 10.78 ?  130 GLY   A N    1 
ATOM   2669 N  N    B GLY   A 1 130 ? 14.594 -0.741  -3.833  0.28 13.53 ?  130 GLY   A N    1 
ATOM   2670 C  CA   A GLY   A 1 130 ? 14.419 0.466   -3.370  0.72 11.34 ?  130 GLY   A CA   1 
ATOM   2671 C  CA   B GLY   A 1 130 ? 14.472 0.701   -3.740  0.28 14.00 ?  130 GLY   A CA   1 
ATOM   2672 C  C    A GLY   A 1 130 ? 15.015 1.107   -4.602  0.72 11.32 ?  130 GLY   A C    1 
ATOM   2673 C  C    B GLY   A 1 130 ? 15.158 1.360   -4.915  0.28 14.27 ?  130 GLY   A C    1 
ATOM   2674 O  O    A GLY   A 1 130 ? 14.790 0.663   -5.733  0.72 10.98 ?  130 GLY   A O    1 
ATOM   2675 O  O    B GLY   A 1 130 ? 14.931 1.006   -6.078  0.28 14.71 ?  130 GLY   A O    1 
ATOM   2676 H  H    A GLY   A 1 130 ? 13.791 -1.401  -3.366  0.72 12.91 ?  130 GLY   A H    1 
ATOM   2677 H  H    B GLY   A 1 130 ? 13.874 -1.148  -4.044  0.28 16.22 ?  130 GLY   A H    1 
ATOM   2678 H  HA2  A GLY   A 1 130 ? 13.480 0.714   -3.320  0.72 13.58 ?  130 GLY   A HA2  1 
ATOM   2679 H  HA2  B GLY   A 1 130 ? 13.530 0.946   -3.710  0.28 16.77 ?  130 GLY   A HA2  1 
ATOM   2680 H  HA3  A GLY   A 1 130 ? 14.877 0.808   -2.597  0.72 13.58 ?  130 GLY   A HA3  1 
ATOM   2681 H  HA3  B GLY   A 1 130 ? 14.899 1.023   -2.937  0.28 16.77 ?  130 GLY   A HA3  1 
ATOM   2682 N  N    A ILE   A 1 131 ? 15.781 2.182   -4.385  0.72 11.88 ?  131 ILE   A N    1 
ATOM   2683 N  N    B ILE   A 1 131 ? 16.039 2.315   -4.606  0.28 14.00 ?  131 ILE   A N    1 
ATOM   2684 C  CA   A ILE   A 1 131 ? 16.340 2.956   -5.491  0.72 11.60 ?  131 ILE   A CA   1 
ATOM   2685 C  CA   B ILE   A 1 131 ? 16.688 3.104   -5.647  0.28 13.62 ?  131 ILE   A CA   1 
ATOM   2686 C  C    A ILE   A 1 131 ? 17.387 2.194   -6.296  0.72 11.39 ?  131 ILE   A C    1 
ATOM   2687 C  C    B ILE   A 1 131 ? 17.657 2.276   -6.478  0.28 13.46 ?  131 ILE   A C    1 
ATOM   2688 O  O    A ILE   A 1 131 ? 17.821 2.700   -7.337  0.72 12.32 ?  131 ILE   A O    1 
ATOM   2689 O  O    B ILE   A 1 131 ? 18.041 2.703   -7.574  0.28 13.90 ?  131 ILE   A O    1 
ATOM   2690 C  CB   A ILE   A 1 131 ? 16.858 4.342   -5.041  0.72 12.64 ?  131 ILE   A CB   1 
ATOM   2691 C  CB   B ILE   A 1 131 ? 17.356 4.376   -5.078  0.28 13.64 ?  131 ILE   A CB   1 
ATOM   2692 C  CG1  A ILE   A 1 131 ? 18.055 4.214   -4.096  0.72 14.18 ?  131 ILE   A CG1  1 
ATOM   2693 C  CG1  B ILE   A 1 131 ? 18.621 4.039   -4.280  0.28 14.04 ?  131 ILE   A CG1  1 
ATOM   2694 C  CG2  A ILE   A 1 131 ? 15.732 5.147   -4.392  0.72 13.07 ?  131 ILE   A CG2  1 
ATOM   2695 C  CG2  B ILE   A 1 131 ? 16.375 5.156   -4.200  0.28 13.43 ?  131 ILE   A CG2  1 
ATOM   2696 C  CD1  A ILE   A 1 131 ? 18.679 5.557   -3.719  0.72 15.76 ?  131 ILE   A CD1  1 
ATOM   2697 C  CD1  B ILE   A 1 131 ? 19.317 5.273   -3.697  0.28 14.32 ?  131 ILE   A CD1  1 
ATOM   2698 H  H    A ILE   A 1 131 ? 15.972 2.493   -3.606  0.72 14.24 ?  131 ILE   A H    1 
ATOM   2699 H  H    B ILE   A 1 131 ? 16.269 2.513   -3.805  0.28 16.77 ?  131 ILE   A H    1 
ATOM   2700 H  HA   A ILE   A 1 131 ? 15.616 3.136   -6.104  0.72 13.90 ?  131 ILE   A HA   1 
ATOM   2701 H  HA   B ILE   A 1 131 ? 16.005 3.403   -6.257  0.28 16.32 ?  131 ILE   A HA   1 
ATOM   2702 H  HB   A ILE   A 1 131 ? 17.149 4.824   -5.828  0.72 15.15 ?  131 ILE   A HB   1 
ATOM   2703 H  HB   B ILE   A 1 131 ? 17.609 4.942   -5.824  0.28 16.34 ?  131 ILE   A HB   1 
ATOM   2704 H  HG12 A ILE   A 1 131 ? 17.767 3.781   -3.276  0.72 16.99 ?  131 ILE   A HG12 1 
ATOM   2705 H  HG12 B ILE   A 1 131 ? 18.384 3.456   -3.544  0.28 16.82 ?  131 ILE   A HG12 1 
ATOM   2706 H  HG13 A ILE   A 1 131 ? 18.742 3.681   -4.525  0.72 16.99 ?  131 ILE   A HG13 1 
ATOM   2707 H  HG13 B ILE   A 1 131 ? 19.260 3.599   -4.861  0.28 16.82 ?  131 ILE   A HG13 1 
ATOM   2708 H  HG21 A ILE   A 1 131 ? 16.026 6.059   -4.259  0.72 15.67 ?  131 ILE   A HG21 1 
ATOM   2709 H  HG21 B ILE   A 1 131 ? 16.728 6.047   -4.037  0.28 16.09 ?  131 ILE   A HG21 1 
ATOM   2710 H  HG22 A ILE   A 1 131 ? 14.958 5.131   -4.979  0.72 15.67 ?  131 ILE   A HG22 1 
ATOM   2711 H  HG22 B ILE   A 1 131 ? 15.523 5.220   -4.656  0.28 16.09 ?  131 ILE   A HG22 1 
ATOM   2712 H  HG23 A ILE   A 1 131 ? 15.504 4.741   -3.539  0.72 15.67 ?  131 ILE   A HG23 1 
ATOM   2713 H  HG23 B ILE   A 1 131 ? 16.263 4.688   -3.356  0.28 16.09 ?  131 ILE   A HG23 1 
ATOM   2714 H  HD11 A ILE   A 1 131 ? 19.497 5.399   -3.221  0.72 18.89 ?  131 ILE   A HD11 1 
ATOM   2715 H  HD11 B ILE   A 1 131 ? 20.186 5.016   -3.349  0.28 17.16 ?  131 ILE   A HD11 1 
ATOM   2716 H  HD12 A ILE   A 1 131 ? 18.876 6.053   -4.529  0.72 18.89 ?  131 ILE   A HD12 1 
ATOM   2717 H  HD12 B ILE   A 1 131 ? 19.427 5.938   -4.396  0.28 17.16 ?  131 ILE   A HD12 1 
ATOM   2718 H  HD13 A ILE   A 1 131 ? 18.052 6.057   -3.171  0.72 18.89 ?  131 ILE   A HD13 1 
ATOM   2719 H  HD13 B ILE   A 1 131 ? 18.773 5.640   -2.980  0.28 17.16 ?  131 ILE   A HD13 1 
ATOM   2720 N  N    A PHE   A 1 132 ? 17.801 0.991   -5.863  0.72 11.26 ?  132 PHE   A N    1 
ATOM   2721 N  N    B PHE   A 1 132 ? 18.067 1.098   -5.997  0.28 13.30 ?  132 PHE   A N    1 
ATOM   2722 C  CA   A PHE   A 1 132 ? 18.679 0.158   -6.681  0.72 11.44 ?  132 PHE   A CA   1 
ATOM   2723 C  CA   B PHE   A 1 132 ? 18.951 0.261   -6.800  0.28 13.13 ?  132 PHE   A CA   1 
ATOM   2724 C  C    A PHE   A 1 132 ? 17.926 -0.614  -7.767  0.72 11.96 ?  132 PHE   A C    1 
ATOM   2725 C  C    B PHE   A 1 132 ? 18.214 -0.420  -7.950  0.28 13.76 ?  132 PHE   A C    1 
ATOM   2726 O  O    A PHE   A 1 132 ? 18.565 -1.264  -8.604  0.72 12.22 ?  132 PHE   A O    1 
ATOM   2727 O  O    B PHE   A 1 132 ? 18.858 -0.849  -8.913  0.28 14.21 ?  132 PHE   A O    1 
ATOM   2728 C  CB   A PHE   A 1 132 ? 19.487 -0.810  -5.809  0.72 11.44 ?  132 PHE   A CB   1 
ATOM   2729 C  CB   B PHE   A 1 132 ? 19.681 -0.759  -5.926  0.28 12.05 ?  132 PHE   A CB   1 
ATOM   2730 C  CG   A PHE   A 1 132 ? 20.730 -0.208  -5.180  0.72 11.45 ?  132 PHE   A CG   1 
ATOM   2731 C  CG   B PHE   A 1 132 ? 20.849 -0.185  -5.159  0.28 11.49 ?  132 PHE   A CG   1 
ATOM   2732 C  CD1  A PHE   A 1 132 ? 20.650 0.873   -4.319  0.72 12.01 ?  132 PHE   A CD1  1 
ATOM   2733 C  CD1  B PHE   A 1 132 ? 20.644 0.695   -4.108  0.28 11.65 ?  132 PHE   A CD1  1 
ATOM   2734 C  CD2  A PHE   A 1 132 ? 21.975 -0.777  -5.414  0.72 12.12 ?  132 PHE   A CD2  1 
ATOM   2735 C  CD2  B PHE   A 1 132 ? 22.150 -0.544  -5.480  0.28 11.27 ?  132 PHE   A CD2  1 
ATOM   2736 C  CE1  A PHE   A 1 132 ? 21.797 1.393   -3.730  0.72 12.55 ?  132 PHE   A CE1  1 
ATOM   2737 C  CE1  B PHE   A 1 132 ? 21.717 1.215   -3.400  0.28 11.56 ?  132 PHE   A CE1  1 
ATOM   2738 C  CE2  A PHE   A 1 132 ? 23.122 -0.264  -4.827  0.72 12.46 ?  132 PHE   A CE2  1 
ATOM   2739 C  CE2  B PHE   A 1 132 ? 23.225 -0.028  -4.773  0.28 11.35 ?  132 PHE   A CE2  1 
ATOM   2740 C  CZ   A PHE   A 1 132 ? 23.030 0.825   -3.985  0.72 12.75 ?  132 PHE   A CZ   1 
ATOM   2741 C  CZ   B PHE   A 1 132 ? 23.004 0.853   -3.733  0.28 11.41 ?  132 PHE   A CZ   1 
ATOM   2742 H  H    A PHE   A 1 132 ? 17.597 0.645   -5.099  0.72 13.50 ?  132 PHE   A H    1 
ATOM   2743 H  H    B PHE   A 1 132 ? 17.857 0.776   -5.223  0.28 15.94 ?  132 PHE   A H    1 
ATOM   2744 H  HA   A PHE   A 1 132 ? 19.317 0.736   -7.123  0.72 13.70 ?  132 PHE   A HA   1 
ATOM   2745 H  HA   B PHE   A 1 132 ? 19.626 0.838   -7.185  0.28 15.73 ?  132 PHE   A HA   1 
ATOM   2746 H  HB2  A PHE   A 1 132 ? 18.921 -1.129  -5.087  0.72 13.70 ?  132 PHE   A HB2  1 
ATOM   2747 H  HB2  B PHE   A 1 132 ? 19.057 -1.120  -5.281  0.28 14.44 ?  132 PHE   A HB2  1 
ATOM   2748 H  HB3  A PHE   A 1 132 ? 19.769 -1.562  -6.356  0.72 13.70 ?  132 PHE   A HB3  1 
ATOM   2749 H  HB3  B PHE   A 1 132 ? 20.018 -1.470  -6.495  0.28 14.44 ?  132 PHE   A HB3  1 
ATOM   2750 H  HD1  A PHE   A 1 132 ? 19.827 1.259   -4.138  0.72 14.39 ?  132 PHE   A HD1  1 
ATOM   2751 H  HD1  B PHE   A 1 132 ? 19.780 0.946   -3.876  0.28 13.96 ?  132 PHE   A HD1  1 
ATOM   2752 H  HD2  A PHE   A 1 132 ? 22.046 -1.514  -5.983  0.72 14.53 ?  132 PHE   A HD2  1 
ATOM   2753 H  HD2  B PHE   A 1 132 ? 22.308 -1.139  -6.182  0.28 13.50 ?  132 PHE   A HD2  1 
ATOM   2754 H  HE1  A PHE   A 1 132 ? 21.738 2.125   -3.159  0.72 15.04 ?  132 PHE   A HE1  1 
ATOM   2755 H  HE1  B PHE   A 1 132 ? 21.569 1.808   -2.699  0.28 13.85 ?  132 PHE   A HE1  1 
ATOM   2756 H  HE2  A PHE   A 1 132 ? 23.951 -0.650  -5.006  0.72 14.93 ?  132 PHE   A HE2  1 
ATOM   2757 H  HE2  B PHE   A 1 132 ? 24.094 -0.272  -5.000  0.28 13.60 ?  132 PHE   A HE2  1 
ATOM   2758 H  HZ   A PHE   A 1 132 ? 23.798 1.177   -3.591  0.72 15.27 ?  132 PHE   A HZ   1 
ATOM   2759 H  HZ   B PHE   A 1 132 ? 23.724 1.202   -3.259  0.28 13.67 ?  132 PHE   A HZ   1 
ATOM   2760 N  N    A GLY   A 1 133 ? 16.592 -0.577  -7.769  0.72 12.13 ?  133 GLY   A N    1 
ATOM   2761 N  N    B GLY   A 1 133 ? 16.889 -0.545  -7.867  0.28 13.81 ?  133 GLY   A N    1 
ATOM   2762 C  CA   A GLY   A 1 133 ? 15.810 -0.939  -8.935  0.72 13.09 ?  133 GLY   A CA   1 
ATOM   2763 C  CA   B GLY   A 1 133 ? 16.058 -0.853  -9.016  0.28 13.97 ?  133 GLY   A CA   1 
ATOM   2764 C  C    A GLY   A 1 133 ? 15.519 -2.411  -9.160  0.72 13.54 ?  133 GLY   A C    1 
ATOM   2765 C  C    B GLY   A 1 133 ? 15.507 -2.262  -9.081  0.28 13.93 ?  133 GLY   A C    1 
ATOM   2766 O  O    A GLY   A 1 133 ? 14.922 -2.740  -10.192 0.72 14.55 ?  133 GLY   A O    1 
ATOM   2767 O  O    B GLY   A 1 133 ? 14.626 -2.516  -9.913  0.28 13.89 ?  133 GLY   A O    1 
ATOM   2768 H  H    A GLY   A 1 133 ? 16.117 -0.343  -7.090  0.72 14.53 ?  133 GLY   A H    1 
ATOM   2769 H  H    B GLY   A 1 133 ? 16.447 -0.463  -7.134  0.28 16.54 ?  133 GLY   A H    1 
ATOM   2770 H  HA2  A GLY   A 1 133 ? 14.957 -0.484  -8.882  0.72 15.69 ?  133 GLY   A HA2  1 
ATOM   2771 H  HA2  B GLY   A 1 133 ? 15.307 -0.241  -9.021  0.28 16.74 ?  133 GLY   A HA2  1 
ATOM   2772 H  HA3  A GLY   A 1 133 ? 16.269 -0.615  -9.724  0.72 15.69 ?  133 GLY   A HA3  1 
ATOM   2773 H  HA3  B GLY   A 1 133 ? 16.571 -0.699  -9.825  0.28 16.74 ?  133 GLY   A HA3  1 
ATOM   2774 N  N    A ALA   A 1 134 ? 15.913 -3.309  -8.260  0.72 12.88 ?  134 ALA   A N    1 
ATOM   2775 N  N    B ALA   A 1 134 ? 15.981 -3.183  -8.248  0.28 13.96 ?  134 ALA   A N    1 
ATOM   2776 C  CA   A ALA   A 1 134 ? 15.584 -4.716  -8.436  0.72 13.58 ?  134 ALA   A CA   1 
ATOM   2777 C  CA   B ALA   A 1 134 ? 15.568 -4.572  -8.375  0.28 14.12 ?  134 ALA   A CA   1 
ATOM   2778 C  C    A ALA   A 1 134 ? 14.216 -5.025  -7.831  0.72 13.90 ?  134 ALA   A C    1 
ATOM   2779 C  C    B ALA   A 1 134 ? 14.244 -4.824  -7.659  0.28 14.07 ?  134 ALA   A C    1 
ATOM   2780 O  O    A ALA   A 1 134 ? 13.631 -4.226  -7.097  0.72 15.03 ?  134 ALA   A O    1 
ATOM   2781 O  O    B ALA   A 1 134 ? 13.831 -4.078  -6.765  0.28 14.42 ?  134 ALA   A O    1 
ATOM   2782 C  CB   A ALA   A 1 134 ? 16.651 -5.620  -7.819  0.72 14.85 ?  134 ALA   A CB   1 
ATOM   2783 C  CB   B ALA   A 1 134 ? 16.636 -5.507  -7.814  0.28 14.71 ?  134 ALA   A CB   1 
ATOM   2784 H  H    A ALA   A 1 134 ? 16.374 -3.130  -7.554  0.72 15.43 ?  134 ALA   A H    1 
ATOM   2785 H  H    B ALA   A 1 134 ? 16.539 -3.028  -7.613  0.28 16.73 ?  134 ALA   A H    1 
ATOM   2786 H  HA   A ALA   A 1 134 ? 15.541 -4.914  -9.386  0.72 16.27 ?  134 ALA   A HA   1 
ATOM   2787 H  HA   B ALA   A 1 134 ? 15.447 -4.774  -9.314  0.28 16.92 ?  134 ALA   A HA   1 
ATOM   2788 H  HB1  A ALA   A 1 134 ? 16.407 -6.545  -7.974  0.72 17.80 ?  134 ALA   A HB1  1 
ATOM   2789 H  HB1  B ALA   A 1 134 ? 16.338 -6.422  -7.928  0.28 17.63 ?  134 ALA   A HB1  1 
ATOM   2790 H  HB2  A ALA   A 1 134 ? 17.505 -5.428  -8.239  0.72 17.80 ?  134 ALA   A HB2  1 
ATOM   2791 H  HB2  B ALA   A 1 134 ? 17.462 -5.362  -8.298  0.28 17.63 ?  134 ALA   A HB2  1 
ATOM   2792 H  HB3  A ALA   A 1 134 ? 16.702 -5.443  -6.869  0.72 17.80 ?  134 ALA   A HB3  1 
ATOM   2793 H  HB3  B ALA   A 1 134 ? 16.761 -5.312  -6.873  0.28 17.63 ?  134 ALA   A HB3  1 
ATOM   2794 N  N    A ASP   A 1 135 ? 13.707 -6.210  -8.160  0.72 14.09 ?  135 ASP   A N    1 
ATOM   2795 N  N    B ASP   A 1 135 ? 13.583 -5.904  -8.064  0.28 14.51 ?  135 ASP   A N    1 
ATOM   2796 C  CA   A ASP   A 1 135 ? 12.446 -6.690  -7.606  0.72 15.04 ?  135 ASP   A CA   1 
ATOM   2797 C  CA   B ASP   A 1 135 ? 12.328 -6.313  -7.450  0.28 15.05 ?  135 ASP   A CA   1 
ATOM   2798 C  C    A ASP   A 1 135 ? 12.670 -7.122  -6.162  0.72 14.63 ?  135 ASP   A C    1 
ATOM   2799 C  C    B ASP   A 1 135 ? 12.594 -6.819  -6.038  0.28 14.36 ?  135 ASP   A C    1 
ATOM   2800 O  O    A ASP   A 1 135 ? 13.479 -8.025  -5.920  0.72 14.33 ?  135 ASP   A O    1 
ATOM   2801 O  O    B ASP   A 1 135 ? 13.291 -7.828  -5.873  0.28 14.04 ?  135 ASP   A O    1 
ATOM   2802 C  CB   A ASP   A 1 135 ? 11.977 -7.877  -8.442  0.72 17.54 ?  135 ASP   A CB   1 
ATOM   2803 C  CB   B ASP   A 1 135 ? 11.685 -7.414  -8.280  0.28 16.42 ?  135 ASP   A CB   1 
ATOM   2804 C  CG   A ASP   A 1 135 ? 10.641 -8.444  -7.976  0.72 19.80 ?  135 ASP   A CG   1 
ATOM   2805 C  CG   B ASP   A 1 135 ? 10.649 -8.198  -7.500  0.28 17.87 ?  135 ASP   A CG   1 
ATOM   2806 O  OD1  A ASP   A 1 135 ? 10.138 -8.032  -6.908  0.72 20.13 ?  135 ASP   A OD1  1 
ATOM   2807 O  OD1  B ASP   A 1 135 ? 9.779  -7.562  -6.870  0.28 18.25 ?  135 ASP   A OD1  1 
ATOM   2808 O  OD2  A ASP   A 1 135 ? 10.086 -9.299  -8.695  0.72 21.93 -1 135 ASP   A OD2  1 
ATOM   2809 O  OD2  B ASP   A 1 135 ? 10.710 -9.445  -7.509  0.28 18.52 -1 135 ASP   A OD2  1 
ATOM   2810 H  H    A ASP   A 1 135 ? 14.073 -6.763  -8.711  0.72 16.89 ?  135 ASP   A H    1 
ATOM   2811 H  H    B ASP   A 1 135 ? 13.841 -6.422  -8.697  0.28 17.39 ?  135 ASP   A H    1 
ATOM   2812 H  HA   A ASP   A 1 135 ? 11.772 -5.993  -7.653  0.72 18.02 ?  135 ASP   A HA   1 
ATOM   2813 H  HA   B ASP   A 1 135 ? 11.718 -5.559  -7.426  0.28 18.04 ?  135 ASP   A HA   1 
ATOM   2814 H  HB2  A ASP   A 1 135 ? 11.870 -7.598  -9.367  0.72 21.03 ?  135 ASP   A HB2  1 
ATOM   2815 H  HB2  B ASP   A 1 135 ? 11.253 -7.014  -9.053  0.28 19.68 ?  135 ASP   A HB2  1 
ATOM   2816 H  HB3  A ASP   A 1 135 ? 12.638 -8.587  -8.390  0.72 21.03 ?  135 ASP   A HB3  1 
ATOM   2817 H  HB3  B ASP   A 1 135 ? 12.372 -8.033  -8.568  0.28 19.68 ?  135 ASP   A HB3  1 
ATOM   2818 N  N    A PRO   A 1 136 ? 12.008 -6.508  -5.179  0.72 14.30 ?  136 PRO   A N    1 
ATOM   2819 N  N    B PRO   A 1 136 ? 12.072 -6.161  -5.001  0.28 13.82 ?  136 PRO   A N    1 
ATOM   2820 C  CA   A PRO   A 1 136 ? 12.249 -6.907  -3.780  0.72 14.16 ?  136 PRO   A CA   1 
ATOM   2821 C  CA   B PRO   A 1 136 ? 12.353 -6.609  -3.626  0.28 13.73 ?  136 PRO   A CA   1 
ATOM   2822 C  C    A PRO   A 1 136 ? 11.836 -8.334  -3.462  0.72 13.48 ?  136 PRO   A C    1 
ATOM   2823 C  C    B PRO   A 1 136 ? 11.858 -8.011  -3.313  0.28 13.26 ?  136 PRO   A C    1 
ATOM   2824 O  O    A PRO   A 1 136 ? 12.446 -8.961  -2.587  0.72 13.16 ?  136 PRO   A O    1 
ATOM   2825 O  O    B PRO   A 1 136 ? 12.394 -8.649  -2.398  0.28 12.53 ?  136 PRO   A O    1 
ATOM   2826 C  CB   A PRO   A 1 136 ? 11.442 -5.877  -2.977  0.72 15.00 ?  136 PRO   A CB   1 
ATOM   2827 C  CB   B PRO   A 1 136 ? 11.671 -5.540  -2.758  0.28 14.01 ?  136 PRO   A CB   1 
ATOM   2828 C  CG   A PRO   A 1 136 ? 10.398 -5.386  -3.928  0.72 15.90 ?  136 PRO   A CG   1 
ATOM   2829 C  CG   B PRO   A 1 136 ? 10.696 -4.866  -3.671  0.28 14.30 ?  136 PRO   A CG   1 
ATOM   2830 C  CD   A PRO   A 1 136 ? 11.029 -5.413  -5.286  0.72 15.12 ?  136 PRO   A CD   1 
ATOM   2831 C  CD   B PRO   A 1 136 ? 11.279 -4.923  -5.030  0.28 13.93 ?  136 PRO   A CD   1 
ATOM   2832 H  HA   A PRO   A 1 136 ? 13.194 -6.805  -3.566  0.72 16.97 ?  136 PRO   A HA   1 
ATOM   2833 H  HA   B PRO   A 1 136 ? 13.305 -6.577  -3.456  0.28 16.45 ?  136 PRO   A HA   1 
ATOM   2834 H  HB2  A PRO   A 1 136 ? 11.038 -6.311  -2.209  0.72 17.98 ?  136 PRO   A HB2  1 
ATOM   2835 H  HB2  B PRO   A 1 136 ? 11.209 -5.956  -2.015  0.28 16.79 ?  136 PRO   A HB2  1 
ATOM   2836 H  HB3  A PRO   A 1 136 ? 12.029 -5.156  -2.696  0.72 17.98 ?  136 PRO   A HB3  1 
ATOM   2837 H  HB3  B PRO   A 1 136 ? 12.333 -4.903  -2.437  0.28 16.79 ?  136 PRO   A HB3  1 
ATOM   2838 H  HG2  A PRO   A 1 136 ? 9.632  -5.974  -3.897  0.72 19.06 ?  136 PRO   A HG2  1 
ATOM   2839 H  HG2  B PRO   A 1 136 ? 9.854  -5.342  -3.656  0.28 17.13 ?  136 PRO   A HG2  1 
ATOM   2840 H  HG3  A PRO   A 1 136 ? 10.152 -4.481  -3.692  0.72 19.06 ?  136 PRO   A HG3  1 
ATOM   2841 H  HG3  B PRO   A 1 136 ? 10.576 -3.944  -3.401  0.28 17.13 ?  136 PRO   A HG3  1 
ATOM   2842 H  HD2  A PRO   A 1 136 ? 10.365 -5.629  -5.962  0.72 18.12 ?  136 PRO   A HD2  1 
ATOM   2843 H  HD2  B PRO   A 1 136 ? 10.573 -4.986  -5.694  0.28 16.69 ?  136 PRO   A HD2  1 
ATOM   2844 H  HD3  A PRO   A 1 136 ? 11.476 -4.578  -5.479  0.72 18.12 ?  136 PRO   A HD3  1 
ATOM   2845 H  HD3  B PRO   A 1 136 ? 11.854 -4.158  -5.192  0.28 16.69 ?  136 PRO   A HD3  1 
ATOM   2846 N  N    A ILE   A 1 137 ? 10.801 -8.858  -4.122  0.72 13.45 ?  137 ILE   A N    1 
ATOM   2847 N  N    B ILE   A 1 137 ? 10.855 -8.516  -4.034  0.28 13.46 ?  137 ILE   A N    1 
ATOM   2848 C  CA   A ILE   A 1 137 ? 10.437 -10.259 -3.929  0.72 13.81 ?  137 ILE   A CA   1 
ATOM   2849 C  CA   B ILE   A 1 137 ? 10.425 -9.898  -3.831  0.28 13.71 ?  137 ILE   A CA   1 
ATOM   2850 C  C    A ILE   A 1 137 ? 11.605 -11.153 -4.321  0.72 13.40 ?  137 ILE   A C    1 
ATOM   2851 C  C    B ILE   A 1 137 ? 11.544 -10.857 -4.217  0.28 13.56 ?  137 ILE   A C    1 
ATOM   2852 O  O    A ILE   A 1 137 ? 11.932 -12.125 -3.628  0.72 13.38 ?  137 ILE   A O    1 
ATOM   2853 O  O    B ILE   A 1 137 ? 11.817 -11.839 -3.515  0.28 13.55 ?  137 ILE   A O    1 
ATOM   2854 C  CB   A ILE   A 1 137 ? 9.154  -10.595 -4.717  0.72 14.92 ?  137 ILE   A CB   1 
ATOM   2855 C  CB   B ILE   A 1 137 ? 9.132  -10.175 -4.624  0.28 14.22 ?  137 ILE   A CB   1 
ATOM   2856 C  CG1  A ILE   A 1 137 ? 7.964  -9.776  -4.195  0.72 16.51 ?  137 ILE   A CG1  1 
ATOM   2857 C  CG1  B ILE   A 1 137 ? 8.036  -9.175  -4.238  0.28 14.89 ?  137 ILE   A CG1  1 
ATOM   2858 C  CG2  A ILE   A 1 137 ? 8.864  -12.092 -4.644  0.72 15.39 ?  137 ILE   A CG2  1 
ATOM   2859 C  CG2  B ILE   A 1 137 ? 8.668  -11.614 -4.403  0.28 14.30 ?  137 ILE   A CG2  1 
ATOM   2860 C  CD1  A ILE   A 1 137 ? 6.694  -9.941  -5.009  0.72 17.81 ?  137 ILE   A CD1  1 
ATOM   2861 C  CD1  B ILE   A 1 137 ? 6.795  -9.274  -5.094  0.28 15.38 ?  137 ILE   A CD1  1 
ATOM   2862 H  H    A ILE   A 1 137 ? 10.301 -8.433  -4.673  0.72 16.11 ?  137 ILE   A H    1 
ATOM   2863 H  H    B ILE   A 1 137 ? 10.416 -8.083  -4.635  0.28 16.13 ?  137 ILE   A H    1 
ATOM   2864 H  HA   A ILE   A 1 137 ? 10.259 -10.416 -2.992  0.72 16.55 ?  137 ILE   A HA   1 
ATOM   2865 H  HA   B ILE   A 1 137 ? 10.226 -10.029 -2.891  0.28 16.43 ?  137 ILE   A HA   1 
ATOM   2866 H  HB   A ILE   A 1 137 ? 9.295  -10.364 -5.645  0.72 17.89 ?  137 ILE   A HB   1 
ATOM   2867 H  HB   B ILE   A 1 137 ? 9.323  -10.058 -5.565  0.28 17.04 ?  137 ILE   A HB   1 
ATOM   2868 H  HG12 A ILE   A 1 137 ? 7.774  -10.046 -3.284  0.72 19.78 ?  137 ILE   A HG12 1 
ATOM   2869 H  HG12 B ILE   A 1 137 ? 7.775  -9.333  -3.318  0.28 17.85 ?  137 ILE   A HG12 1 
ATOM   2870 H  HG13 A ILE   A 1 137 ? 8.208  -8.835  -4.213  0.72 19.78 ?  137 ILE   A HG13 1 
ATOM   2871 H  HG13 B ILE   A 1 137 ? 8.379  -8.271  -4.329  0.28 17.85 ?  137 ILE   A HG13 1 
ATOM   2872 H  HG21 A ILE   A 1 137 ? 7.958  -12.273 -4.950  0.72 18.45 ?  137 ILE   A HG21 1 
ATOM   2873 H  HG21 B ILE   A 1 137 ? 7.823  -11.750 -4.859  0.28 17.13 ?  137 ILE   A HG21 1 
ATOM   2874 H  HG22 A ILE   A 1 137 ? 9.491  -12.565 -5.211  0.72 18.45 ?  137 ILE   A HG22 1 
ATOM   2875 H  HG22 B ILE   A 1 137 ? 9.333  -12.220 -4.762  0.28 17.13 ?  137 ILE   A HG22 1 
ATOM   2876 H  HG23 A ILE   A 1 137 ? 8.957  -12.388 -3.727  0.72 18.45 ?  137 ILE   A HG23 1 
ATOM   2877 H  HG23 B ILE   A 1 137 ? 8.557  -11.768 -3.452  0.28 17.13 ?  137 ILE   A HG23 1 
ATOM   2878 H  HD11 A ILE   A 1 137 ? 5.963  -10.140 -4.409  0.72 21.35 ?  137 ILE   A HD11 1 
ATOM   2879 H  HD11 B ILE   A 1 137 ? 6.241  -8.495  -4.937  0.28 18.44 ?  137 ILE   A HD11 1 
ATOM   2880 H  HD12 A ILE   A 1 137 ? 6.528  -9.113  -5.481  0.72 21.35 ?  137 ILE   A HD12 1 
ATOM   2881 H  HD12 B ILE   A 1 137 ? 7.060  -9.310  -6.027  0.28 18.44 ?  137 ILE   A HD12 1 
ATOM   2882 H  HD13 A ILE   A 1 137 ? 6.810  -10.659 -5.648  0.72 21.35 ?  137 ILE   A HD13 1 
ATOM   2883 H  HD13 B ILE   A 1 137 ? 6.311  -10.079 -4.856  0.28 18.44 ?  137 ILE   A HD13 1 
ATOM   2884 N  N    A HIS   A 1 138 ? 12.261 -10.825 -5.434  0.72 13.58 ?  138 HIS   A N    1 
ATOM   2885 N  N    B HIS   A 1 138 ? 12.210 -10.584 -5.341  0.28 13.61 ?  138 HIS   A N    1 
ATOM   2886 C  CA   A HIS   A 1 138 ? 13.457 -11.555 -5.834  0.72 13.77 ?  138 HIS   A CA   1 
ATOM   2887 C  CA   B HIS   A 1 138 ? 13.314 -11.429 -5.787  0.28 13.44 ?  138 HIS   A CA   1 
ATOM   2888 C  C    A HIS   A 1 138 ? 14.581 -11.382 -4.819  0.72 13.05 ?  138 HIS   A C    1 
ATOM   2889 C  C    B HIS   A 1 138 ? 14.492 -11.357 -4.821  0.28 13.04 ?  138 HIS   A C    1 
ATOM   2890 O  O    A HIS   A 1 138 ? 15.258 -12.357 -4.463  0.72 13.43 ?  138 HIS   A O    1 
ATOM   2891 O  O    B HIS   A 1 138 ? 15.120 -12.378 -4.513  0.28 13.33 ?  138 HIS   A O    1 
ATOM   2892 C  CB   A HIS   A 1 138 ? 13.896 -11.109 -7.227  0.72 15.04 ?  138 HIS   A CB   1 
ATOM   2893 C  CB   B HIS   A 1 138 ? 13.729 -11.000 -7.195  0.28 13.72 ?  138 HIS   A CB   1 
ATOM   2894 C  CG   A HIS   A 1 138 ? 15.148 -11.778 -7.696  0.72 16.20 ?  138 HIS   A CG   1 
ATOM   2895 C  CG   B HIS   A 1 138 ? 15.022 -11.595 -7.652  0.28 14.06 ?  138 HIS   A CG   1 
ATOM   2896 N  ND1  A HIS   A 1 138 ? 15.231 -13.140 -7.897  0.72 17.56 ?  138 HIS   A ND1  1 
ATOM   2897 N  ND1  B HIS   A 1 138 ? 15.143 -12.916 -8.022  0.28 14.74 ?  138 HIS   A ND1  1 
ATOM   2898 C  CD2  A HIS   A 1 138 ? 16.372 -11.278 -7.983  0.72 16.54 ?  138 HIS   A CD2  1 
ATOM   2899 C  CD2  B HIS   A 1 138 ? 16.252 -11.048 -7.799  0.28 14.04 ?  138 HIS   A CD2  1 
ATOM   2900 C  CE1  A HIS   A 1 138 ? 16.451 -13.447 -8.300  0.72 18.06 ?  138 HIS   A CE1  1 
ATOM   2901 C  CE1  B HIS   A 1 138 ? 16.393 -13.158 -8.377  0.28 14.81 ?  138 HIS   A CE1  1 
ATOM   2902 N  NE2  A HIS   A 1 138 ? 17.163 -12.335 -8.359  0.72 17.37 ?  138 HIS   A NE2  1 
ATOM   2903 N  NE2  B HIS   A 1 138 ? 17.087 -12.041 -8.251  0.28 14.37 ?  138 HIS   A NE2  1 
ATOM   2904 H  H    A HIS   A 1 138 ? 12.031 -10.190 -5.974  0.72 16.27 ?  138 HIS   A H    1 
ATOM   2905 H  H    B HIS   A 1 138 ? 12.040 -9.915  -5.858  0.28 16.31 ?  138 HIS   A H    1 
ATOM   2906 H  HA   A HIS   A 1 138 ? 13.242 -12.496 -5.886  0.72 16.50 ?  138 HIS   A HA   1 
ATOM   2907 H  HA   B HIS   A 1 138 ? 13.010 -12.345 -5.828  0.28 16.10 ?  138 HIS   A HA   1 
ATOM   2908 H  HB2  A HIS   A 1 138 ? 13.188 -11.319 -7.863  0.72 18.03 ?  138 HIS   A HB2  1 
ATOM   2909 H  HB2  B HIS   A 1 138 ? 13.037 -11.274 -7.822  0.28 16.45 ?  138 HIS   A HB2  1 
ATOM   2910 H  HB3  A HIS   A 1 138 ? 14.052 -10.152 -7.220  0.72 18.03 ?  138 HIS   A HB3  1 
ATOM   2911 H  HB3  B HIS   A 1 138 ? 13.821 -10.034 -7.216  0.28 16.45 ?  138 HIS   A HB3  1 
ATOM   2912 H  HD1  A HIS   A 1 138 ? 14.586 -13.700 -7.785  0.72 21.05 ?  138 HIS   A HD1  1 
ATOM   2913 H  HD1  B HIS   A 1 138 ? 14.504 -13.494 -8.022  0.28 17.67 ?  138 HIS   A HD1  1 
ATOM   2914 H  HD2  A HIS   A 1 138 ? 16.621 -10.383 -7.937  0.72 19.82 ?  138 HIS   A HD2  1 
ATOM   2915 H  HD2  B HIS   A 1 138 ? 16.486 -10.165 -7.627  0.28 16.83 ?  138 HIS   A HD2  1 
ATOM   2916 H  HE1  A HIS   A 1 138 ? 16.756 -14.299 -8.504  0.72 21.65 ?  138 HIS   A HE1  1 
ATOM   2917 H  HE1  B HIS   A 1 138 ? 16.726 -13.977 -8.666  0.28 17.75 ?  138 HIS   A HE1  1 
ATOM   2918 N  N    . SER   A 1 139 ? 14.799 -10.155 -4.337  1.00 12.56 ?  139 SER   A N    1 
ATOM   2919 C  CA   . SER   A 1 139 ? 15.870 -9.967  -3.371  1.00 12.36 ?  139 SER   A CA   1 
ATOM   2920 C  C    . SER   A 1 139 ? 15.647 -10.805 -2.118  1.00 12.19 ?  139 SER   A C    1 
ATOM   2921 O  O    . SER   A 1 139 ? 16.592 -11.398 -1.587  1.00 12.36 ?  139 SER   A O    1 
ATOM   2922 C  CB   . SER   A 1 139 ? 16.007 -8.489  -3.021  1.00 12.24 ?  139 SER   A CB   1 
ATOM   2923 O  OG   . SER   A 1 139 ? 17.081 -8.314  -2.115  1.00 12.73 ?  139 SER   A OG   1 
ATOM   2924 H  H    A SER   A 1 139 ? 14.358 -9.446  -4.545  0.72 15.06 ?  139 SER   A H    1 
ATOM   2925 H  H    B SER   A 1 139 ? 14.390 -9.429  -4.552  0.28 15.06 ?  139 SER   A H    1 
ATOM   2926 H  HA   . SER   A 1 139 ? 16.707 -10.251 -3.770  1.00 14.81 ?  139 SER   A HA   1 
ATOM   2927 H  HB2  . SER   A 1 139 ? 16.183 -7.981  -3.828  1.00 14.66 ?  139 SER   A HB2  1 
ATOM   2928 H  HB3  . SER   A 1 139 ? 15.182 -8.181  -2.609  1.00 14.66 ?  139 SER   A HB3  1 
ATOM   2929 H  HG   . SER   A 1 139 ? 17.163 -7.498  -1.914  1.00 15.25 ?  139 SER   A HG   1 
ATOM   2930 N  N    . LEU   A 1 140 ? 14.406 -10.864 -1.628  1.00 11.85 ?  140 LEU   A N    1 
ATOM   2931 C  CA   . LEU   A 1 140 ? 14.122 -11.683 -0.452  1.00 11.70 ?  140 LEU   A CA   1 
ATOM   2932 C  C    . LEU   A 1 140 ? 14.392 -13.159 -0.730  1.00 12.11 ?  140 LEU   A C    1 
ATOM   2933 O  O    . LEU   A 1 140 ? 14.940 -13.870 0.122   1.00 13.04 ?  140 LEU   A O    1 
ATOM   2934 C  CB   . LEU   A 1 140 ? 12.680 -11.461 -0.007  1.00 12.23 ?  140 LEU   A CB   1 
ATOM   2935 C  CG   . LEU   A 1 140 ? 12.212 -12.296 1.184   1.00 12.88 ?  140 LEU   A CG   1 
ATOM   2936 C  CD1  . LEU   A 1 140 ? 13.122 -12.119 2.389   1.00 13.30 ?  140 LEU   A CD1  1 
ATOM   2937 C  CD2  . LEU   A 1 140 ? 10.756 -11.966 1.541   1.00 13.60 ?  140 LEU   A CD2  1 
ATOM   2938 H  H    . LEU   A 1 140 ? 13.727 -10.440 -1.947  1.00 14.20 ?  140 LEU   A H    1 
ATOM   2939 H  HA   . LEU   A 1 140 ? 14.701 -11.406 0.272   1.00 14.02 ?  140 LEU   A HA   1 
ATOM   2940 H  HB2  . LEU   A 1 140 ? 12.570 -10.535 0.233   1.00 14.65 ?  140 LEU   A HB2  1 
ATOM   2941 H  HB3  . LEU   A 1 140 ? 12.095 -11.678 -0.752  1.00 14.65 ?  140 LEU   A HB3  1 
ATOM   2942 H  HG   . LEU   A 1 140 ? 12.231 -13.236 0.935   1.00 15.44 ?  140 LEU   A HG   1 
ATOM   2943 H  HD11 . LEU   A 1 140 ? 12.732 -12.576 3.151   1.00 15.94 ?  140 LEU   A HD11 1 
ATOM   2944 H  HD12 . LEU   A 1 140 ? 13.989 -12.513 2.183   1.00 15.94 ?  140 LEU   A HD12 1 
ATOM   2945 H  HD13 . LEU   A 1 140 ? 13.220 -11.178 2.576   1.00 15.94 ?  140 LEU   A HD13 1 
ATOM   2946 H  HD21 . LEU   A 1 140 ? 10.466 -12.552 2.265   1.00 16.30 ?  140 LEU   A HD21 1 
ATOM   2947 H  HD22 . LEU   A 1 140 ? 10.700 -11.043 1.829   1.00 16.30 ?  140 LEU   A HD22 1 
ATOM   2948 H  HD23 . LEU   A 1 140 ? 10.194 -12.109 0.764   1.00 16.30 ?  140 LEU   A HD23 1 
ATOM   2949 N  N    . ARG   A 1 141 ? 14.008 -13.635 -1.917  1.00 12.64 ?  141 ARG   A N    1 
ATOM   2950 C  CA   . ARG   A 1 141 ? 14.251 -15.027 -2.282  1.00 13.64 ?  141 ARG   A CA   1 
ATOM   2951 C  C    . ARG   A 1 141 ? 15.746 -15.331 -2.289  1.00 13.10 ?  141 ARG   A C    1 
ATOM   2952 O  O    . ARG   A 1 141 ? 16.195 -16.342 -1.734  1.00 13.44 ?  141 ARG   A O    1 
ATOM   2953 C  CB   . ARG   A 1 141 ? 13.638 -15.289 -3.659  1.00 15.45 ?  141 ARG   A CB   1 
ATOM   2954 C  CG   . ARG   A 1 141 ? 13.626 -16.740 -4.087  1.00 18.21 ?  141 ARG   A CG   1 
ATOM   2955 C  CD   . ARG   A 1 141 ? 12.591 -17.494 -3.315  1.00 20.58 ?  141 ARG   A CD   1 
ATOM   2956 N  NE   . ARG   A 1 141 ? 13.196 -18.262 -2.240  1.00 21.37 ?  141 ARG   A NE   1 
ATOM   2957 C  CZ   . ARG   A 1 141 ? 12.505 -18.826 -1.257  1.00 22.12 ?  141 ARG   A CZ   1 
ATOM   2958 N  NH1  . ARG   A 1 141 ? 11.211 -18.595 -1.098  1.00 21.57 ?  141 ARG   A NH1  1 
ATOM   2959 N  NH2  . ARG   A 1 141 ? 13.130 -19.634 -0.405  1.00 22.97 ?  141 ARG   A NH2  1 
ATOM   2960 H  H    . ARG   A 1 141 ? 13.613 -13.171 -2.527  1.00 15.14 ?  141 ARG   A H    1 
ATOM   2961 H  HA   . ARG   A 1 141 ? 13.826 -15.607 -1.638  1.00 16.35 ?  141 ARG   A HA   1 
ATOM   2962 H  HB2  . ARG   A 1 141 ? 12.723 -14.970 -3.658  1.00 18.52 ?  141 ARG   A HB2  1 
ATOM   2963 H  HB3  . ARG   A 1 141 ? 14.149 -14.795 -4.322  1.00 18.52 ?  141 ARG   A HB3  1 
ATOM   2964 H  HG2  . ARG   A 1 141 ? 13.414 -16.799 -5.033  1.00 21.83 ?  141 ARG   A HG2  1 
ATOM   2965 H  HG3  . ARG   A 1 141 ? 14.496 -17.140 -3.913  1.00 21.83 ?  141 ARG   A HG3  1 
ATOM   2966 H  HD2  . ARG   A 1 141 ? 11.963 -16.871 -2.916  1.00 24.67 ?  141 ARG   A HD2  1 
ATOM   2967 H  HD3  . ARG   A 1 141 ? 12.122 -18.101 -3.913  1.00 24.67 ?  141 ARG   A HD3  1 
ATOM   2968 H  HE   . ARG   A 1 141 ? 14.023 -18.479 -2.317  1.00 25.62 ?  141 ARG   A HE   1 
ATOM   2969 H  HH11 . ARG   A 1 141 ? 10.787 -18.090 -1.650  1.00 25.87 ?  141 ARG   A HH11 1 
ATOM   2970 H  HH12 . ARG   A 1 141 ? 10.780 -18.970 -0.450  1.00 25.87 ?  141 ARG   A HH12 1 
ATOM   2971 H  HH21 . ARG   A 1 141 ? 13.970 -19.789 -0.497  1.00 27.54 ?  141 ARG   A HH21 1 
ATOM   2972 H  HH22 . ARG   A 1 141 ? 12.696 -19.995 0.246   1.00 27.54 ?  141 ARG   A HH22 1 
ATOM   2973 N  N    . VAL   A 1 142 ? 16.539 -14.465 -2.924  1.00 12.60 ?  142 VAL   A N    1 
ATOM   2974 C  CA   . VAL   A 1 142 ? 17.983 -14.675 -2.948  1.00 12.64 ?  142 VAL   A CA   1 
ATOM   2975 C  C    . VAL   A 1 142 ? 18.547 -14.650 -1.535  1.00 11.96 ?  142 VAL   A C    1 
ATOM   2976 O  O    . VAL   A 1 142 ? 19.406 -15.464 -1.183  1.00 12.40 ?  142 VAL   A O    1 
ATOM   2977 C  CB   . VAL   A 1 142 ? 18.678 -13.660 -3.875  1.00 12.64 ?  142 VAL   A CB   1 
ATOM   2978 C  CG1  . VAL   A 1 142 ? 20.190 -13.868 -3.839  1.00 12.73 ?  142 VAL   A CG1  1 
ATOM   2979 C  CG2  . VAL   A 1 142 ? 18.173 -13.802 -5.298  1.00 13.88 ?  142 VAL   A CG2  1 
ATOM   2980 H  H    . VAL   A 1 142 ? 16.273 -13.756 -3.338  1.00 15.10 ?  142 VAL   A H    1 
ATOM   2981 H  HA   . VAL   A 1 142 ? 18.160 -15.552 -3.311  1.00 15.15 ?  142 VAL   A HA   1 
ATOM   2982 H  HB   . VAL   A 1 142 ? 18.494 -12.755 -3.573  1.00 15.15 ?  142 VAL   A HB   1 
ATOM   2983 H  HG11 . VAL   A 1 142 ? 20.597 -13.379 -4.573  1.00 15.26 ?  142 VAL   A HG11 1 
ATOM   2984 H  HG12 . VAL   A 1 142 ? 20.539 -13.536 -2.994  1.00 15.26 ?  142 VAL   A HG12 1 
ATOM   2985 H  HG13 . VAL   A 1 142 ? 20.382 -14.813 -3.928  1.00 15.26 ?  142 VAL   A HG13 1 
ATOM   2986 H  HG21 . VAL   A 1 142 ? 18.649 -13.170 -5.863  1.00 16.63 ?  142 VAL   A HG21 1 
ATOM   2987 H  HG22 . VAL   A 1 142 ? 18.344 -14.707 -5.598  1.00 16.63 ?  142 VAL   A HG22 1 
ATOM   2988 H  HG23 . VAL   A 1 142 ? 17.227 -13.614 -5.312  1.00 16.63 ?  142 VAL   A HG23 1 
ATOM   2989 N  N    . CYS   A 1 143 ? 18.076 -13.722 -0.701  1.00 11.75 ?  143 CYS   A N    1 
ATOM   2990 C  CA   . CYS   A 1 143 ? 18.533 -13.674 0.684   1.00 11.96 ?  143 CYS   A CA   1 
ATOM   2991 C  C    . CYS   A 1 143 ? 18.310 -15.016 1.376   1.00 12.13 ?  143 CYS   A C    1 
ATOM   2992 O  O    . CYS   A 1 143 ? 19.231 -15.599 1.952   1.00 12.09 ?  143 CYS   A O    1 
ATOM   2993 C  CB   . CYS   A 1 143 ? 17.797 -12.562 1.426   1.00 12.35 ?  143 CYS   A CB   1 
ATOM   2994 S  SG   . CYS   A 1 143 ? 18.294 -12.380 3.145   1.00 12.71 ?  143 CYS   A SG   1 
ATOM   2995 H  H    . CYS   A 1 143 ? 17.498 -13.124 -0.908  1.00 14.07 ?  143 CYS   A H    1 
ATOM   2996 H  HA   . CYS   A 1 143 ? 19.482 -13.481 0.704   1.00 14.32 ?  143 CYS   A HA   1 
ATOM   2997 H  HB2  . CYS   A 1 143 ? 17.966 -11.719 0.976   1.00 14.79 ?  143 CYS   A HB2  1 
ATOM   2998 H  HB3  . CYS   A 1 143 ? 16.847 -12.752 1.410   1.00 14.79 ?  143 CYS   A HB3  1 
ATOM   2999 H  HG   . CYS   A 1 143 ? 17.706 -11.454 3.617   1.00 15.23 ?  143 CYS   A HG   1 
ATOM   3000 N  N    . VAL   A 1 144 ? 17.082 -15.520 1.320   1.00 12.91 ?  144 VAL   A N    1 
ATOM   3001 C  CA   . VAL   A 1 144 ? 16.738 -16.753 2.020   1.00 13.83 ?  144 VAL   A CA   1 
ATOM   3002 C  C    . VAL   A 1 144 ? 17.556 -17.924 1.495   1.00 13.80 ?  144 VAL   A C    1 
ATOM   3003 O  O    . VAL   A 1 144 ? 17.923 -18.832 2.253   1.00 14.35 ?  144 VAL   A O    1 
ATOM   3004 C  CB   . VAL   A 1 144 ? 15.223 -16.995 1.887   1.00 16.79 ?  144 VAL   A CB   1 
ATOM   3005 C  CG1  . VAL   A 1 144 ? 14.859 -18.426 2.225   1.00 18.78 ?  144 VAL   A CG1  1 
ATOM   3006 C  CG2  . VAL   A 1 144 ? 14.465 -15.994 2.756   1.00 16.55 ?  144 VAL   A CG2  1 
ATOM   3007 H  H    . VAL   A 1 144 ? 16.427 -15.164 0.883   1.00 15.47 ?  144 VAL   A H    1 
ATOM   3008 H  HA   . VAL   A 1 144 ? 16.933 -16.645 2.958   1.00 16.58 ?  144 VAL   A HA   1 
ATOM   3009 H  HB   . VAL   A 1 144 ? 14.957 -16.832 0.963   1.00 20.13 ?  144 VAL   A HB   1 
ATOM   3010 H  HG11 . VAL   A 1 144 ? 13.904 -18.473 2.410   1.00 22.51 ?  144 VAL   A HG11 1 
ATOM   3011 H  HG12 . VAL   A 1 144 ? 15.073 -18.996 1.472   1.00 22.51 ?  144 VAL   A HG12 1 
ATOM   3012 H  HG13 . VAL   A 1 144 ? 15.357 -18.699 3.008   1.00 22.51 ?  144 VAL   A HG13 1 
ATOM   3013 H  HG21 . VAL   A 1 144 ? 13.508 -16.152 2.672   1.00 19.84 ?  144 VAL   A HG21 1 
ATOM   3014 H  HG22 . VAL   A 1 144 ? 14.735 -16.104 3.680   1.00 19.84 ?  144 VAL   A HG22 1 
ATOM   3015 H  HG23 . VAL   A 1 144 ? 14.669 -15.089 2.459   1.00 19.84 ?  144 VAL   A HG23 1 
ATOM   3016 N  N    . ASP   A 1 145 ? 17.825 -17.942 0.193   1.00 13.88 ?  145 ASP   A N    1 
ATOM   3017 C  CA   . ASP   A 1 145 ? 18.539 -19.046 -0.438  1.00 14.43 ?  145 ASP   A CA   1 
ATOM   3018 C  C    . ASP   A 1 145 ? 20.060 -18.903 -0.387  1.00 14.28 ?  145 ASP   A C    1 
ATOM   3019 O  O    . ASP   A 1 145 ? 20.765 -19.799 -0.864  1.00 16.30 ?  145 ASP   A O    1 
ATOM   3020 C  CB   . ASP   A 1 145 ? 18.096 -19.185 -1.897  1.00 16.01 ?  145 ASP   A CB   1 
ATOM   3021 C  CG   . ASP   A 1 145 ? 16.650 -19.619 -2.033  1.00 18.25 ?  145 ASP   A CG   1 
ATOM   3022 O  OD1  . ASP   A 1 145 ? 16.075 -20.152 -1.058  1.00 18.88 ?  145 ASP   A OD1  1 
ATOM   3023 O  OD2  . ASP   A 1 145 ? 16.085 -19.422 -3.127  1.00 19.61 -1 145 ASP   A OD2  1 
ATOM   3024 H  H    . ASP   A 1 145 ? 17.582 -17.322 -0.359  1.00 16.63 ?  145 ASP   A H    1 
ATOM   3025 H  HA   . ASP   A 1 145 ? 18.300 -19.867 0.019   1.00 17.30 ?  145 ASP   A HA   1 
ATOM   3026 H  HB2  . ASP   A 1 145 ? 18.197 -18.331 -2.344  1.00 19.19 ?  145 ASP   A HB2  1 
ATOM   3027 H  HB3  . ASP   A 1 145 ? 18.643 -19.857 -2.330  1.00 19.19 ?  145 ASP   A HB3  1 
ATOM   3028 N  N    . THR   A 1 146 ? 20.580 -17.810 0.160   1.00 12.82 ?  146 THR   A N    1 
ATOM   3029 C  CA   . THR   A 1 146 ? 22.020 -17.559 0.180   1.00 12.27 ?  146 THR   A CA   1 
ATOM   3030 C  C    . THR   A 1 146 ? 22.577 -17.372 1.578   1.00 12.15 ?  146 THR   A C    1 
ATOM   3031 O  O    . THR   A 1 146 ? 23.652 -17.902 1.889   1.00 13.44 ?  146 THR   A O    1 
ATOM   3032 C  CB   . THR   A 1 146 ? 22.341 -16.309 -0.658  1.00 12.26 ?  146 THR   A CB   1 
ATOM   3033 O  OG1  . THR   A 1 146 ? 21.823 -16.475 -1.978  1.00 13.00 ?  146 THR   A OG1  1 
ATOM   3034 C  CG2  . THR   A 1 146 ? 23.843 -16.076 -0.750  1.00 12.90 ?  146 THR   A CG2  1 
ATOM   3035 H  H    . THR   A 1 146 ? 20.115 -17.179 0.521   1.00 15.36 ?  146 THR   A H    1 
ATOM   3036 H  HA   . THR   A 1 146 ? 22.479 -18.308 -0.222  1.00 14.71 ?  146 THR   A HA   1 
ATOM   3037 H  HB   . THR   A 1 146 ? 21.938 -15.526 -0.246  1.00 14.69 ?  146 THR   A HB   1 
ATOM   3038 H  HG1  . THR   A 1 146 ? 20.987 -16.551 -1.947  1.00 15.57 ?  146 THR   A HG1  1 
ATOM   3039 H  HG21 . THR   A 1 146 ? 24.031 -15.407 -1.427  1.00 15.46 ?  146 THR   A HG21 1 
ATOM   3040 H  HG22 . THR   A 1 146 ? 24.185 -15.767 0.102   1.00 15.46 ?  146 THR   A HG22 1 
ATOM   3041 H  HG23 . THR   A 1 146 ? 24.288 -16.902 -0.991  1.00 15.46 ?  146 THR   A HG23 1 
ATOM   3042 N  N    . VAL   A 1 147 ? 21.898 -16.590 2.409   1.00 12.00 ?  147 VAL   A N    1 
ATOM   3043 C  CA   . VAL   A 1 147 ? 22.376 -16.291 3.751   1.00 12.38 ?  147 VAL   A CA   1 
ATOM   3044 C  C    . VAL   A 1 147 ? 22.060 -17.460 4.671   1.00 12.71 ?  147 VAL   A C    1 
ATOM   3045 O  O    . VAL   A 1 147 ? 20.917 -17.935 4.730   1.00 13.48 ?  147 VAL   A O    1 
ATOM   3046 C  CB   . VAL   A 1 147 ? 21.755 -14.984 4.267   1.00 12.30 ?  147 VAL   A CB   1 
ATOM   3047 C  CG1  . VAL   A 1 147 ? 22.290 -14.669 5.647   1.00 13.56 ?  147 VAL   A CG1  1 
ATOM   3048 C  CG2  . VAL   A 1 147 ? 22.016 -13.837 3.295   1.00 12.52 ?  147 VAL   A CG2  1 
ATOM   3049 H  H    . VAL   A 1 147 ? 21.139 -16.223 2.221   1.00 14.38 ?  147 VAL   A H    1 
ATOM   3050 H  HA   . VAL   A 1 147 ? 23.336 -16.179 3.725   1.00 14.84 ?  147 VAL   A HA   1 
ATOM   3051 H  HB   . VAL   A 1 147 ? 20.796 -15.099 4.340   1.00 14.74 ?  147 VAL   A HB   1 
ATOM   3052 H  HG11 . VAL   A 1 147 ? 22.045 -13.763 5.880   1.00 16.25 ?  147 VAL   A HG11 1 
ATOM   3053 H  HG12 . VAL   A 1 147 ? 21.897 -15.291 6.286   1.00 16.25 ?  147 VAL   A HG12 1 
ATOM   3054 H  HG13 . VAL   A 1 147 ? 23.252 -14.766 5.643   1.00 16.25 ?  147 VAL   A HG13 1 
ATOM   3055 H  HG21 . VAL   A 1 147 ? 21.686 -13.015 3.688   1.00 15.00 ?  147 VAL   A HG21 1 
ATOM   3056 H  HG22 . VAL   A 1 147 ? 22.967 -13.774 3.134   1.00 15.00 ?  147 VAL   A HG22 1 
ATOM   3057 H  HG23 . VAL   A 1 147 ? 21.547 -14.019 2.466   1.00 15.00 ?  147 VAL   A HG23 1 
ATOM   3058 N  N    . ARG   A 1 148 ? 23.083 -17.925 5.388   1.00 13.00 ?  148 ARG   A N    1 
ATOM   3059 C  CA   . ARG   A 1 148 ? 22.950 -18.998 6.359   1.00 13.22 ?  148 ARG   A CA   1 
ATOM   3060 C  C    . ARG   A 1 148 ? 23.068 -18.520 7.795   1.00 13.38 ?  148 ARG   A C    1 
ATOM   3061 O  O    . ARG   A 1 148 ? 22.665 -19.247 8.710   1.00 14.93 ?  148 ARG   A O    1 
ATOM   3062 C  CB   . ARG   A 1 148 ? 23.996 -20.093 6.092   1.00 13.66 ?  148 ARG   A CB   1 
ATOM   3063 C  CG   . ARG   A 1 148 ? 23.843 -20.735 4.727   1.00 14.98 ?  148 ARG   A CG   1 
ATOM   3064 C  CD   . ARG   A 1 148 ? 24.930 -21.766 4.441   1.00 15.94 ?  148 ARG   A CD   1 
ATOM   3065 N  NE   . ARG   A 1 148 ? 26.268 -21.183 4.464   1.00 15.96 ?  148 ARG   A NE   1 
ATOM   3066 C  CZ   . ARG   A 1 148 ? 26.781 -20.453 3.484   1.00 15.23 ?  148 ARG   A CZ   1 
ATOM   3067 N  NH1  . ARG   A 1 148 ? 26.104 -20.220 2.371   1.00 15.63 ?  148 ARG   A NH1  1 
ATOM   3068 N  NH2  . ARG   A 1 148 ? 27.995 -19.920 3.634   1.00 15.56 ?  148 ARG   A NH2  1 
ATOM   3069 H  H    . ARG   A 1 148 ? 23.886 -17.623 5.316   1.00 15.58 ?  148 ARG   A H    1 
ATOM   3070 H  HA   . ARG   A 1 148 ? 22.079 -19.401 6.258   1.00 15.84 ?  148 ARG   A HA   1 
ATOM   3071 H  HB2  . ARG   A 1 148 ? 24.884 -19.710 6.143   1.00 16.37 ?  148 ARG   A HB2  1 
ATOM   3072 H  HB3  . ARG   A 1 148 ? 23.898 -20.794 6.758   1.00 16.37 ?  148 ARG   A HB3  1 
ATOM   3073 H  HG2  . ARG   A 1 148 ? 22.980 -21.173 4.681   1.00 17.95 ?  148 ARG   A HG2  1 
ATOM   3074 H  HG3  . ARG   A 1 148 ? 23.899 -20.040 4.050   1.00 17.95 ?  148 ARG   A HG3  1 
ATOM   3075 H  HD2  . ARG   A 1 148 ? 24.891 -22.463 5.118   1.00 19.11 ?  148 ARG   A HD2  1 
ATOM   3076 H  HD3  . ARG   A 1 148 ? 24.776 -22.154 3.562   1.00 19.11 ?  148 ARG   A HD3  1 
ATOM   3077 H  HE   . ARG   A 1 148 ? 26.754 -21.330 5.151   1.00 19.12 ?  148 ARG   A HE   1 
ATOM   3078 H  HH11 . ARG   A 1 148 ? 25.316 -20.544 2.266   1.00 18.74 ?  148 ARG   A HH11 1 
ATOM   3079 H  HH12 . ARG   A 1 148 ? 26.452 -19.731 1.752   1.00 18.74 ?  148 ARG   A HH12 1 
ATOM   3080 H  HH21 . ARG   A 1 148 ? 28.437 -20.063 4.356   1.00 18.65 ?  148 ARG   A HH21 1 
ATOM   3081 H  HH22 . ARG   A 1 148 ? 28.335 -19.438 3.008   1.00 18.65 ?  148 ARG   A HH22 1 
ATOM   3082 N  N    . THR   A 1 149 ? 23.608 -17.324 8.006   1.00 13.61 ?  149 THR   A N    1 
ATOM   3083 C  CA   . THR   A 1 149 ? 23.682 -16.720 9.321   1.00 13.71 ?  149 THR   A CA   1 
ATOM   3084 C  C    . THR   A 1 149 ? 22.357 -16.020 9.624   1.00 13.27 ?  149 THR   A C    1 
ATOM   3085 O  O    . THR   A 1 149 ? 21.421 -16.019 8.813   1.00 13.72 ?  149 THR   A O    1 
ATOM   3086 C  CB   . THR   A 1 149 ? 24.881 -15.779 9.380   1.00 14.10 ?  149 THR   A CB   1 
ATOM   3087 O  OG1  . THR   A 1 149 ? 24.764 -14.857 8.296   1.00 14.12 ?  149 THR   A OG1  1 
ATOM   3088 C  CG2  . THR   A 1 149 ? 26.194 -16.569 9.276   1.00 14.73 ?  149 THR   A CG2  1 
ATOM   3089 H  H    . THR   A 1 149 ? 23.952 -16.833 7.383   1.00 16.31 ?  149 THR   A H    1 
ATOM   3090 H  HA   . THR   A 1 149 ? 23.813 -17.422 9.978   1.00 16.43 ?  149 THR   A HA   1 
ATOM   3091 H  HB   . THR   A 1 149 ? 24.863 -15.296 10.219  1.00 16.90 ?  149 THR   A HB   1 
ATOM   3092 H  HG1  . THR   A 1 149 ? 25.416 -14.326 8.298   1.00 16.92 ?  149 THR   A HG1  1 
ATOM   3093 H  HG21 . THR   A 1 149 ? 26.949 -15.963 9.326   1.00 17.65 ?  149 THR   A HG21 1 
ATOM   3094 H  HG22 . THR   A 1 149 ? 26.257 -17.210 10.003  1.00 17.65 ?  149 THR   A HG22 1 
ATOM   3095 H  HG23 . THR   A 1 149 ? 26.231 -17.049 8.432   1.00 17.65 ?  149 THR   A HG23 1 
ATOM   3096 N  N    . ASN   A 1 150 ? 22.234 -15.479 10.829  1.00 13.31 ?  150 ASN   A N    1 
ATOM   3097 C  CA   . ASN   A 1 150 ? 20.950 -14.968 11.309  1.00 13.81 ?  150 ASN   A CA   1 
ATOM   3098 C  C    . ASN   A 1 150 ? 20.774 -13.530 10.843  1.00 12.74 ?  150 ASN   A C    1 
ATOM   3099 O  O    . ASN   A 1 150 ? 21.525 -12.636 11.254  1.00 14.17 ?  150 ASN   A O    1 
ATOM   3100 C  CB   . ASN   A 1 150 ? 20.878 -15.081 12.826  1.00 16.48 ?  150 ASN   A CB   1 
ATOM   3101 C  CG   . ASN   A 1 150 ? 20.776 -16.515 13.287  1.00 20.37 ?  150 ASN   A CG   1 
ATOM   3102 O  OD1  . ASN   A 1 150 ? 20.190 -17.351 12.599  1.00 21.69 ?  150 ASN   A OD1  1 
ATOM   3103 N  ND2  . ASN   A 1 150 ? 21.356 -16.815 14.448  1.00 22.71 ?  150 ASN   A ND2  1 
ATOM   3104 H  H    . ASN   A 1 150 ? 22.875 -15.409 11.395  1.00 15.95 ?  150 ASN   A H    1 
ATOM   3105 H  HA   . ASN   A 1 150 ? 20.230 -15.507 10.936  1.00 16.55 ?  150 ASN   A HA   1 
ATOM   3106 H  HB2  . ASN   A 1 150 ? 21.678 -14.699 13.216  1.00 19.75 ?  150 ASN   A HB2  1 
ATOM   3107 H  HB3  . ASN   A 1 150 ? 20.091 -14.615 13.147  1.00 19.75 ?  150 ASN   A HB3  1 
ATOM   3108 H  HD21 . ASN   A 1 150 ? 21.331 -17.624 14.755  1.00 27.23 ?  150 ASN   A HD21 1 
ATOM   3109 H  HD22 . ASN   A 1 150 ? 21.757 -16.204 14.905  1.00 27.23 ?  150 ASN   A HD22 1 
ATOM   3110 N  N    . VAL   A 1 151 ? 19.788 -13.302 9.983   1.00 12.44 ?  151 VAL   A N    1 
ATOM   3111 C  CA   . VAL   A 1 151 ? 19.581 -11.996 9.375   1.00 12.68 ?  151 VAL   A CA   1 
ATOM   3112 C  C    . VAL   A 1 151 ? 18.192 -11.477 9.732   1.00 12.50 ?  151 VAL   A C    1 
ATOM   3113 O  O    . VAL   A 1 151 ? 17.185 -12.188 9.588   1.00 13.74 ?  151 VAL   A O    1 
ATOM   3114 C  CB   . VAL   A 1 151 ? 19.875 -12.003 7.860   1.00 14.02 ?  151 VAL   A CB   1 
ATOM   3115 C  CG1  . VAL   A 1 151 ? 19.046 -13.031 7.124   1.00 15.29 ?  151 VAL   A CG1  1 
ATOM   3116 C  CG2  . VAL   A 1 151 ? 19.694 -10.606 7.264   1.00 14.17 ?  151 VAL   A CG2  1 
ATOM   3117 H  H    . VAL   A 1 151 ? 19.220 -13.901 9.733   1.00 14.91 ?  151 VAL   A H    1 
ATOM   3118 H  HA   . VAL   A 1 151 ? 20.224 -11.385 9.768   1.00 15.20 ?  151 VAL   A HA   1 
ATOM   3119 H  HB   . VAL   A 1 151 ? 20.807 -12.250 7.727   1.00 16.81 ?  151 VAL   A HB   1 
ATOM   3120 H  HG11 . VAL   A 1 151 ? 19.247 -12.993 6.175   1.00 18.32 ?  151 VAL   A HG11 1 
ATOM   3121 H  HG12 . VAL   A 1 151 ? 19.261 -13.921 7.464   1.00 18.32 ?  151 VAL   A HG12 1 
ATOM   3122 H  HG13 . VAL   A 1 151 ? 18.104 -12.850 7.269   1.00 18.32 ?  151 VAL   A HG13 1 
ATOM   3123 H  HG21 . VAL   A 1 151 ? 20.007 -10.613 6.343   1.00 16.99 ?  151 VAL   A HG21 1 
ATOM   3124 H  HG22 . VAL   A 1 151 ? 18.754 -10.372 7.287   1.00 16.99 ?  151 VAL   A HG22 1 
ATOM   3125 H  HG23 . VAL   A 1 151 ? 20.211 -9.974  7.783   1.00 16.99 ?  151 VAL   A HG23 1 
ATOM   3126 N  N    . TYR   A 1 152 ? 18.171 -10.235 10.212  1.00 12.36 ?  152 TYR   A N    1 
ATOM   3127 C  CA   . TYR   A 1 152 ? 16.973 -9.504  10.593  1.00 12.26 ?  152 TYR   A CA   1 
ATOM   3128 C  C    . TYR   A 1 152 ? 16.781 -8.401  9.566   1.00 11.54 ?  152 TYR   A C    1 
ATOM   3129 O  O    . TYR   A 1 152 ? 17.561 -7.442  9.519   1.00 12.04 ?  152 TYR   A O    1 
ATOM   3130 C  CB   . TYR   A 1 152 ? 17.144 -8.959  12.007  1.00 13.20 ?  152 TYR   A CB   1 
ATOM   3131 C  CG   . TYR   A 1 152 ? 17.100 -10.078 13.008  1.00 13.68 ?  152 TYR   A CG   1 
ATOM   3132 C  CD1  . TYR   A 1 152 ? 18.227 -10.841 13.286  1.00 15.35 ?  152 TYR   A CD1  1 
ATOM   3133 C  CD2  . TYR   A 1 152 ? 15.915 -10.418 13.637  1.00 14.19 ?  152 TYR   A CD2  1 
ATOM   3134 C  CE1  . TYR   A 1 152 ? 18.181 -11.896 14.176  1.00 16.82 ?  152 TYR   A CE1  1 
ATOM   3135 C  CE2  . TYR   A 1 152 ? 15.856 -11.483 14.532  1.00 15.94 ?  152 TYR   A CE2  1 
ATOM   3136 C  CZ   . TYR   A 1 152 ? 16.994 -12.214 14.801  1.00 16.95 ?  152 TYR   A CZ   1 
ATOM   3137 O  OH   . TYR   A 1 152 ? 16.951 -13.273 15.686  1.00 19.13 ?  152 TYR   A OH   1 
ATOM   3138 H  H    . TYR   A 1 152 ? 18.893 -9.760  10.307  1.00 14.81 ?  152 TYR   A H    1 
ATOM   3139 H  HA   . TYR   A 1 152 ? 16.211 -10.098 10.567  1.00 14.69 ?  152 TYR   A HA   1 
ATOM   3140 H  HB2  . TYR   A 1 152 ? 18.007 -8.521  12.079  1.00 15.82 ?  152 TYR   A HB2  1 
ATOM   3141 H  HB3  . TYR   A 1 152 ? 16.430 -8.342  12.202  1.00 15.82 ?  152 TYR   A HB3  1 
ATOM   3142 H  HD1  . TYR   A 1 152 ? 19.030 -10.634 12.861  1.00 18.40 ?  152 TYR   A HD1  1 
ATOM   3143 H  HD2  . TYR   A 1 152 ? 15.142 -9.928  13.454  1.00 17.00 ?  152 TYR   A HD2  1 
ATOM   3144 H  HE1  . TYR   A 1 152 ? 18.947 -12.386 14.354  1.00 20.16 ?  152 TYR   A HE1  1 
ATOM   3145 H  HE2  . TYR   A 1 152 ? 15.054 -11.688 14.955  1.00 19.11 ?  152 TYR   A HE2  1 
ATOM   3146 H  HH   . TYR   A 1 152 ? 16.175 -13.343 16.001  1.00 22.93 ?  152 TYR   A HH   1 
ATOM   3147 N  N    A LEU   A 1 153 ? 15.790 -8.591  8.694   0.72 11.62 ?  153 LEU   A N    1 
ATOM   3148 N  N    B LEU   A 1 153 ? 15.722 -8.499  8.777   0.28 11.21 ?  153 LEU   A N    1 
ATOM   3149 C  CA   A LEU   A 1 153 ? 15.540 -7.717  7.554   0.72 11.58 ?  153 LEU   A CA   1 
ATOM   3150 C  CA   B LEU   A 1 153 ? 15.472 -7.531  7.722   0.28 10.74 ?  153 LEU   A CA   1 
ATOM   3151 C  C    A LEU   A 1 153 ? 14.533 -6.636  7.919   0.72 11.51 ?  153 LEU   A C    1 
ATOM   3152 C  C    B LEU   A 1 153 ? 14.521 -6.451  8.212   0.28 10.82 ?  153 LEU   A C    1 
ATOM   3153 O  O    A LEU   A 1 153 ? 13.420 -6.935  8.362   0.72 12.35 ?  153 LEU   A O    1 
ATOM   3154 O  O    B LEU   A 1 153 ? 13.454 -6.752  8.759   0.28 11.00 ?  153 LEU   A O    1 
ATOM   3155 C  CB   A LEU   A 1 153 ? 14.987 -8.524  6.377   0.72 11.49 ?  153 LEU   A CB   1 
ATOM   3156 C  CB   B LEU   A 1 153 ? 14.889 -8.220  6.493   0.28 10.44 ?  153 LEU   A CB   1 
ATOM   3157 C  CG   A LEU   A 1 153 ? 15.928 -9.536  5.723   0.72 11.79 ?  153 LEU   A CG   1 
ATOM   3158 C  CG   B LEU   A 1 153 ? 15.804 -9.255  5.844   0.28 10.61 ?  153 LEU   A CG   1 
ATOM   3159 C  CD1  A LEU   A 1 153 ? 15.148 -10.436 4.779   0.72 12.03 ?  153 LEU   A CD1  1 
ATOM   3160 C  CD1  B LEU   A 1 153 ? 15.024 -10.041 4.808   0.28 10.96 ?  153 LEU   A CD1  1 
ATOM   3161 C  CD2  A LEU   A 1 153 ? 17.038 -8.826  4.971   0.72 12.34 ?  153 LEU   A CD2  1 
ATOM   3162 C  CD2  B LEU   A 1 153 ? 17.021 -8.585  5.220   0.28 11.01 ?  153 LEU   A CD2  1 
ATOM   3163 H  H    A LEU   A 1 153 ? 15.230 -9.248  8.748   0.72 13.92 ?  153 LEU   A H    1 
ATOM   3164 H  H    B LEU   A 1 153 ? 15.120 -9.118  8.837   0.28 13.43 ?  153 LEU   A H    1 
ATOM   3165 H  HA   A LEU   A 1 153 ? 16.365 -7.304  7.279   0.72 13.87 ?  153 LEU   A HA   1 
ATOM   3166 H  HA   B LEU   A 1 153 ? 16.305 -7.105  7.479   0.28 12.86 ?  153 LEU   A HA   1 
ATOM   3167 H  HB2  A LEU   A 1 153 ? 14.208 -9.022  6.682   0.72 13.77 ?  153 LEU   A HB2  1 
ATOM   3168 H  HB2  B LEU   A 1 153 ? 14.073 -8.668  6.756   0.28 12.51 ?  153 LEU   A HB2  1 
ATOM   3169 H  HB3  A LEU   A 1 153 ? 14.714 -7.906  5.682   0.72 13.77 ?  153 LEU   A HB3  1 
ATOM   3170 H  HB3  B LEU   A 1 153 ? 14.692 -7.540  5.832   0.28 12.51 ?  153 LEU   A HB3  1 
ATOM   3171 H  HG   A LEU   A 1 153 ? 16.334 -10.094 6.409   0.72 14.13 ?  153 LEU   A HG   1 
ATOM   3172 H  HG   B LEU   A 1 153 ? 16.118 -9.871  6.524   0.28 12.71 ?  153 LEU   A HG   1 
ATOM   3173 H  HD11 A LEU   A 1 153 ? 15.711 -11.176 4.506   0.72 14.42 ?  153 LEU   A HD11 1 
ATOM   3174 H  HD11 B LEU   A 1 153 ? 15.611 -10.693 4.400   0.28 13.12 ?  153 LEU   A HD11 1 
ATOM   3175 H  HD12 A LEU   A 1 153 ? 14.364 -10.770 5.238   0.72 14.42 ?  153 LEU   A HD12 1 
ATOM   3176 H  HD12 B LEU   A 1 153 ? 14.283 -10.488 5.246   0.28 13.12 ?  153 LEU   A HD12 1 
ATOM   3177 H  HD13 A LEU   A 1 153 ? 14.881 -9.918  4.002   0.72 14.42 ?  153 LEU   A HD13 1 
ATOM   3178 H  HD13 B LEU   A 1 153 ? 14.688 -9.427  4.135   0.28 13.12 ?  153 LEU   A HD13 1 
ATOM   3179 H  HD21 A LEU   A 1 153 ? 17.648 -9.488  4.615   0.72 14.78 ?  153 LEU   A HD21 1 
ATOM   3180 H  HD21 B LEU   A 1 153 ? 17.534 -9.254  4.741   0.28 13.18 ?  153 LEU   A HD21 1 
ATOM   3181 H  HD22 A LEU   A 1 153 ? 16.643 -8.313  4.251   0.72 14.78 ?  153 LEU   A HD22 1 
ATOM   3182 H  HD22 B LEU   A 1 153 ? 16.722 -7.895  4.609   0.28 13.18 ?  153 LEU   A HD22 1 
ATOM   3183 H  HD23 A LEU   A 1 153 ? 17.504 -8.240  5.584   0.72 14.78 ?  153 LEU   A HD23 1 
ATOM   3184 H  HD23 B LEU   A 1 153 ? 17.563 -8.192  5.923   0.28 13.18 ?  153 LEU   A HD23 1 
ATOM   3185 N  N    A ALA   A 1 154 ? 14.913 -5.385  7.690   0.72 11.40 ?  154 ALA   A N    1 
ATOM   3186 N  N    B ALA   A 1 154 ? 14.915 -5.196  8.014   0.28 10.77 ?  154 ALA   A N    1 
ATOM   3187 C  CA   A ALA   A 1 154 ? 14.049 -4.236  7.913   0.72 11.40 ?  154 ALA   A CA   1 
ATOM   3188 C  CA   B ALA   A 1 154 ? 14.082 -4.036  8.305   0.28 11.23 ?  154 ALA   A CA   1 
ATOM   3189 C  C    A ALA   A 1 154 ? 13.564 -3.738  6.559   0.72 10.63 ?  154 ALA   A C    1 
ATOM   3190 C  C    B ALA   A 1 154 ? 13.601 -3.492  6.968   0.28 11.17 ?  154 ALA   A C    1 
ATOM   3191 O  O    A ALA   A 1 154 ? 14.373 -3.374  5.703   0.72 11.51 ?  154 ALA   A O    1 
ATOM   3192 O  O    B ALA   A 1 154 ? 14.407 -3.024  6.158   0.28 11.04 ?  154 ALA   A O    1 
ATOM   3193 C  CB   A ALA   A 1 154 ? 14.813 -3.130  8.641   0.72 12.42 ?  154 ALA   A CB   1 
ATOM   3194 C  CB   B ALA   A 1 154 ? 14.876 -2.980  9.071   0.28 11.46 ?  154 ALA   A CB   1 
ATOM   3195 H  H    A ALA   A 1 154 ? 15.689 -5.178  7.386   0.72 13.66 ?  154 ALA   A H    1 
ATOM   3196 H  H    B ALA   A 1 154 ? 15.686 -4.981  7.692   0.28 12.90 ?  154 ALA   A H    1 
ATOM   3197 H  HA   A ALA   A 1 154 ? 13.283 -4.499  8.451   0.72 13.66 ?  154 ALA   A HA   1 
ATOM   3198 H  HA   B ALA   A 1 154 ? 13.314 -4.300  8.833   0.28 13.45 ?  154 ALA   A HA   1 
ATOM   3199 H  HB1  A ALA   A 1 154 ? 14.219 -2.380  8.783   0.72 14.88 ?  154 ALA   A HB1  1 
ATOM   3200 H  HB1  B ALA   A 1 154 ? 14.300 -2.221  9.252   0.28 13.73 ?  154 ALA   A HB1  1 
ATOM   3201 H  HB2  A ALA   A 1 154 ? 15.127 -3.472  9.495   0.72 14.88 ?  154 ALA   A HB2  1 
ATOM   3202 H  HB2  B ALA   A 1 154 ? 15.189 -3.366  9.903   0.28 13.73 ?  154 ALA   A HB2  1 
ATOM   3203 H  HB3  A ALA   A 1 154 ? 15.569 -2.861  8.097   0.72 14.88 ?  154 ALA   A HB3  1 
ATOM   3204 H  HB3  B ALA   A 1 154 ? 15.632 -2.700  8.530   0.28 13.73 ?  154 ALA   A HB3  1 
ATOM   3205 N  N    A VAL   A 1 155 ? 12.247 -3.738  6.368   0.32 8.24  ?  155 VAL   A N    1 
ATOM   3206 N  N    B VAL   A 1 155 ? 12.296 -3.570  6.734   0.28 10.76 ?  155 VAL   A N    1 
ATOM   3207 C  CA   A VAL   A 1 155 ? 11.600 -3.231  5.163   0.32 10.82 ?  155 VAL   A CA   1 
ATOM   3208 C  CA   B VAL   A 1 155 ? 11.680 -3.098  5.501   0.28 11.92 ?  155 VAL   A CA   1 
ATOM   3209 C  CA   T VAL   A 1 155 ? 11.574 -3.329  5.122   0.40 14.02 ?  155 VAL   A CA   1 
ATOM   3210 C  C    A VAL   A 1 155 ? 10.880 -1.943  5.544   0.32 12.39 ?  155 VAL   A C    1 
ATOM   3211 C  C    B VAL   A 1 155 ? 10.995 -1.770  5.797   0.28 13.03 ?  155 VAL   A C    1 
ATOM   3212 C  C    T VAL   A 1 155 ? 10.940 -1.969  5.425   0.40 13.98 ?  155 VAL   A C    1 
ATOM   3213 O  O    A VAL   A 1 155 ? 9.916  -1.971  6.318   0.32 12.72 ?  155 VAL   A O    1 
ATOM   3214 O  O    B VAL   A 1 155 ? 10.117 -1.694  6.666   0.28 12.75 ?  155 VAL   A O    1 
ATOM   3215 O  O    T VAL   A 1 155 ? 10.019 -1.869  6.231   0.40 14.12 ?  155 VAL   A O    1 
ATOM   3216 C  CB   A VAL   A 1 155 ? 10.630 -4.263  4.574   0.32 11.52 ?  155 VAL   A CB   1 
ATOM   3217 C  CB   B VAL   A 1 155 ? 10.696 -4.136  4.939   0.28 12.09 ?  155 VAL   A CB   1 
ATOM   3218 C  CB   T VAL   A 1 155 ? 10.550 -4.371  4.635   0.40 13.99 ?  155 VAL   A CB   1 
ATOM   3219 C  CG1  A VAL   A 1 155 ? 9.998  -3.730  3.298   0.32 12.03 ?  155 VAL   A CG1  1 
ATOM   3220 C  CG1  B VAL   A 1 155 ? 9.921  -3.555  3.771   0.28 11.99 ?  155 VAL   A CG1  1 
ATOM   3221 C  CG1  T VAL   A 1 155 ? 9.880  -3.905  3.354   0.40 14.20 ?  155 VAL   A CG1  1 
ATOM   3222 C  CG2  A VAL   A 1 155 ? 11.350 -5.583  4.316   0.32 12.25 ?  155 VAL   A CG2  1 
ATOM   3223 C  CG2  B VAL   A 1 155 ? 11.449 -5.393  4.514   0.28 12.81 ?  155 VAL   A CG2  1 
ATOM   3224 C  CG2  T VAL   A 1 155 ? 11.225 -5.722  4.419   0.40 14.41 ?  155 VAL   A CG2  1 
ATOM   3225 H  H    A VAL   A 1 155 ? 11.689 -4.064  6.940   0.32 9.86  ?  155 VAL   A H    1 
ATOM   3226 H  H    B VAL   A 1 155 ? 11.730 -3.888  7.295   0.28 12.89 ?  155 VAL   A H    1 
ATOM   3227 H  HA   A VAL   A 1 155 ? 12.274 -3.023  4.498   0.32 12.96 ?  155 VAL   A HA   1 
ATOM   3228 H  HA   B VAL   A 1 155 ? 12.368 -2.942  4.835   0.28 14.28 ?  155 VAL   A HA   1 
ATOM   3229 H  HB   A VAL   A 1 155 ? 9.918  -4.428  5.214   0.32 13.80 ?  155 VAL   A HB   1 
ATOM   3230 H  HB   B VAL   A 1 155 ? 10.063 -4.383  5.632   0.28 14.48 ?  155 VAL   A HB   1 
ATOM   3231 H  HB   T VAL   A 1 155 ? 9.866  -4.481  5.314   0.40 16.76 ?  155 VAL   A HB   1 
ATOM   3232 H  HG11 A VAL   A 1 155 ? 9.493  -4.443  2.877   0.32 14.41 ?  155 VAL   A HG11 1 
ATOM   3233 H  HG11 B VAL   A 1 155 ? 9.469  -4.276  3.306   0.28 14.36 ?  155 VAL   A HG11 1 
ATOM   3234 H  HG11 T VAL   A 1 155 ? 9.306  -4.613  3.024   0.40 17.02 ?  155 VAL   A HG11 1 
ATOM   3235 H  HG12 A VAL   A 1 155 ? 9.407  -2.993  3.519   0.32 14.41 ?  155 VAL   A HG12 1 
ATOM   3236 H  HG12 B VAL   A 1 155 ? 9.270  -2.920  4.106   0.28 14.36 ?  155 VAL   A HG12 1 
ATOM   3237 H  HG12 T VAL   A 1 155 ? 9.355  -3.112  3.540   0.40 17.02 ?  155 VAL   A HG12 1 
ATOM   3238 H  HG13 A VAL   A 1 155 ? 10.700 -3.426  2.703   0.32 14.41 ?  155 VAL   A HG13 1 
ATOM   3239 H  HG13 B VAL   A 1 155 ? 10.542 -3.114  3.171   0.28 14.36 ?  155 VAL   A HG13 1 
ATOM   3240 H  HG13 T VAL   A 1 155 ? 10.565 -3.703  2.696   0.40 17.02 ?  155 VAL   A HG13 1 
ATOM   3241 H  HG21 A VAL   A 1 155 ? 10.745 -6.188  3.861   0.32 14.68 ?  155 VAL   A HG21 1 
ATOM   3242 H  HG21 B VAL   A 1 155 ? 10.844 -5.975  4.028   0.28 15.36 ?  155 VAL   A HG21 1 
ATOM   3243 H  HG21 T VAL   A 1 155 ? 10.562 -6.360  4.114   0.40 17.27 ?  155 VAL   A HG21 1 
ATOM   3244 H  HG22 A VAL   A 1 155 ? 12.128 -5.413  3.763   0.32 14.68 ?  155 VAL   A HG22 1 
ATOM   3245 H  HG22 B VAL   A 1 155 ? 12.192 -5.138  3.944   0.28 15.36 ?  155 VAL   A HG22 1 
ATOM   3246 H  HG22 T VAL   A 1 155 ? 11.921 -5.622  3.749   0.40 17.27 ?  155 VAL   A HG22 1 
ATOM   3247 H  HG23 A VAL   A 1 155 ? 11.624 -5.964  5.165   0.32 14.68 ?  155 VAL   A HG23 1 
ATOM   3248 H  HG23 B VAL   A 1 155 ? 11.782 -5.846  5.305   0.28 15.36 ?  155 VAL   A HG23 1 
ATOM   3249 H  HG23 T VAL   A 1 155 ? 11.613 -6.019  5.256   0.40 17.27 ?  155 VAL   A HG23 1 
ATOM   3250 N  N    A PHE   A 1 156 ? 11.344 -0.810  5.003   0.32 13.98 ?  156 PHE   A N    1 
ATOM   3251 N  N    B PHE   A 1 156 ? 11.409 -0.719  5.082   0.28 14.51 ?  156 PHE   A N    1 
ATOM   3252 N  N    T PHE   A 1 156 ? 11.448 -0.928  4.759   0.40 14.43 ?  156 PHE   A N    1 
ATOM   3253 C  CA   A PHE   A 1 156 ? 10.790 0.488   5.393   0.32 15.46 ?  156 PHE   A CA   1 
ATOM   3254 C  CA   B PHE   A 1 156 ? 10.894 0.622   5.350   0.28 16.15 ?  156 PHE   A CA   1 
ATOM   3255 C  CA   T PHE   A 1 156 ? 11.048 0.446   5.063   0.40 14.75 ?  156 PHE   A CA   1 
ATOM   3256 C  C    A PHE   A 1 156 ? 9.329  0.632   4.975   0.32 16.05 ?  156 PHE   A C    1 
ATOM   3257 C  C    B PHE   A 1 156 ? 9.419  0.746   4.977   0.28 16.57 ?  156 PHE   A C    1 
ATOM   3258 C  C    T PHE   A 1 156 ? 9.583  0.686   4.733   0.40 15.32 ?  156 PHE   A C    1 
ATOM   3259 O  O    A PHE   A 1 156 ? 8.498  1.113   5.756   0.32 16.53 ?  156 PHE   A O    1 
ATOM   3260 O  O    B PHE   A 1 156 ? 8.627  1.320   5.736   0.28 16.90 ?  156 PHE   A O    1 
ATOM   3261 O  O    T PHE   A 1 156 ? 8.854  1.318   5.507   0.40 16.02 ?  156 PHE   A O    1 
ATOM   3262 C  CB   A PHE   A 1 156 ? 11.639 1.616   4.797   0.32 16.38 ?  156 PHE   A CB   1 
ATOM   3263 C  CB   B PHE   A 1 156 ? 11.728 1.645   4.574   0.28 17.41 ?  156 PHE   A CB   1 
ATOM   3264 C  CB   T PHE   A 1 156 ? 11.920 1.404   4.249   0.40 14.22 ?  156 PHE   A CB   1 
ATOM   3265 C  CG   A PHE   A 1 156 ? 11.131 2.999   5.117   0.32 17.05 ?  156 PHE   A CG   1 
ATOM   3266 C  CG   B PHE   A 1 156 ? 11.393 3.080   4.889   0.28 18.43 ?  156 PHE   A CG   1 
ATOM   3267 C  CG   T PHE   A 1 156 ? 11.575 2.865   4.433   0.40 14.13 ?  156 PHE   A CG   1 
ATOM   3268 C  CD1  A PHE   A 1 156 ? 11.020 3.419   6.431   0.32 17.16 ?  156 PHE   A CD1  1 
ATOM   3269 C  CD1  B PHE   A 1 156 ? 10.411 3.751   4.180   0.28 18.95 ?  156 PHE   A CD1  1 
ATOM   3270 C  CD1  T PHE   A 1 156 ? 11.925 3.524   5.600   0.40 15.43 ?  156 PHE   A CD1  1 
ATOM   3271 C  CD2  A PHE   A 1 156 ? 10.791 3.885   4.104   0.32 17.45 ?  156 PHE   A CD2  1 
ATOM   3272 C  CD2  B PHE   A 1 156 ? 12.075 3.762   5.886   0.28 18.81 ?  156 PHE   A CD2  1 
ATOM   3273 C  CD2  T PHE   A 1 156 ? 10.929 3.581   3.431   0.40 14.12 ?  156 PHE   A CD2  1 
ATOM   3274 C  CE1  A PHE   A 1 156 ? 10.562 4.689   6.732   0.32 17.51 ?  156 PHE   A CE1  1 
ATOM   3275 C  CE1  B PHE   A 1 156 ? 10.104 5.070   4.465   0.28 19.02 ?  156 PHE   A CE1  1 
ATOM   3276 C  CE1  T PHE   A 1 156 ? 11.625 4.860   5.777   0.40 16.01 ?  156 PHE   A CE1  1 
ATOM   3277 C  CE2  A PHE   A 1 156 ? 10.329 5.157   4.399   0.32 17.93 ?  156 PHE   A CE2  1 
ATOM   3278 C  CE2  B PHE   A 1 156 ? 11.777 5.082   6.176   0.28 19.04 ?  156 PHE   A CE2  1 
ATOM   3279 C  CE2  T PHE   A 1 156 ? 10.627 4.922   3.603   0.40 14.73 ?  156 PHE   A CE2  1 
ATOM   3280 C  CZ   A PHE   A 1 156 ? 10.218 5.560   5.715   0.32 18.00 ?  156 PHE   A CZ   1 
ATOM   3281 C  CZ   B PHE   A 1 156 ? 10.792 5.737   5.465   0.28 18.92 ?  156 PHE   A CZ   1 
ATOM   3282 C  CZ   T PHE   A 1 156 ? 10.977 5.561   4.778   0.40 15.43 ?  156 PHE   A CZ   1 
ATOM   3283 H  H    A PHE   A 1 156 ? 11.975 -0.770  4.419   0.32 16.76 ?  156 PHE   A H    1 
ATOM   3284 H  H    B PHE   A 1 156 ? 11.990 -0.756  4.447   0.28 17.39 ?  156 PHE   A H    1 
ATOM   3285 H  H    T PHE   A 1 156 ? 12.013 -0.999  4.120   0.40 17.29 ?  156 PHE   A H    1 
ATOM   3286 H  HA   A PHE   A 1 156 ? 10.832 0.569   6.357   0.32 18.53 ?  156 PHE   A HA   1 
ATOM   3287 H  HA   B PHE   A 1 156 ? 10.992 0.814   6.296   0.28 19.36 ?  156 PHE   A HA   1 
ATOM   3288 H  HA   T PHE   A 1 156 ? 11.187 0.626   6.008   0.40 17.67 ?  156 PHE   A HA   1 
ATOM   3289 H  HB2  A PHE   A 1 156 ? 12.545 1.546   5.145   0.32 19.63 ?  156 PHE   A HB2  1 
ATOM   3290 H  HB2  B PHE   A 1 156 ? 12.667 1.510   4.782   0.28 20.87 ?  156 PHE   A HB2  1 
ATOM   3291 H  HB2  T PHE   A 1 156 ? 12.845 1.278   4.514   0.40 17.04 ?  156 PHE   A HB2  1 
ATOM   3292 H  HB3  A PHE   A 1 156 ? 11.654 1.523   3.832   0.32 19.63 ?  156 PHE   A HB3  1 
ATOM   3293 H  HB3  B PHE   A 1 156 ? 11.584 1.510   3.624   0.28 20.87 ?  156 PHE   A HB3  1 
ATOM   3294 H  HB3  T PHE   A 1 156 ? 11.816 1.188   3.310   0.40 17.04 ?  156 PHE   A HB3  1 
ATOM   3295 H  HD1  A PHE   A 1 156 ? 11.251 2.837   7.121   0.32 20.57 ?  156 PHE   A HD1  1 
ATOM   3296 H  HD1  B PHE   A 1 156 ? 9.947  3.309   3.507   0.28 22.72 ?  156 PHE   A HD1  1 
ATOM   3297 H  HD1  T PHE   A 1 156 ? 12.359 3.051   6.280   0.40 18.49 ?  156 PHE   A HD1  1 
ATOM   3298 H  HD2  A PHE   A 1 156 ? 10.865 3.616   3.217   0.32 20.92 ?  156 PHE   A HD2  1 
ATOM   3299 H  HD2  B PHE   A 1 156 ? 12.740 3.325   6.370   0.28 22.55 ?  156 PHE   A HD2  1 
ATOM   3300 H  HD2  T PHE   A 1 156 ? 10.693 3.149   2.643   0.40 16.92 ?  156 PHE   A HD2  1 
ATOM   3301 H  HE1  A PHE   A 1 156 ? 10.487 4.958   7.621   0.32 20.99 ?  156 PHE   A HE1  1 
ATOM   3302 H  HE1  B PHE   A 1 156 ? 9.441  5.508   3.982   0.28 22.80 ?  156 PHE   A HE1  1 
ATOM   3303 H  HE1  T PHE   A 1 156 ? 11.859 5.283   6.573   0.40 19.19 ?  156 PHE   A HE1  1 
ATOM   3304 H  HE2  A PHE   A 1 156 ? 10.100 5.740   3.713   0.32 21.50 ?  156 PHE   A HE2  1 
ATOM   3305 H  HE2  B PHE   A 1 156 ? 12.239 5.525   6.851   0.28 22.83 ?  156 PHE   A HE2  1 
ATOM   3306 H  HE2  T PHE   A 1 156 ? 10.190 5.387   2.934   0.40 17.65 ?  156 PHE   A HE2  1 
ATOM   3307 H  HZ   A PHE   A 1 156 ? 9.909  6.413   5.920   0.32 21.58 ?  156 PHE   A HZ   1 
ATOM   3308 H  HZ   B PHE   A 1 156 ? 10.587 6.623   5.658   0.28 22.68 ?  156 PHE   A HZ   1 
ATOM   3309 H  HZ   T PHE   A 1 156 ? 10.774 6.457   4.901   0.40 18.49 ?  156 PHE   A HZ   1 
ATOM   3310 N  N    A ASP   A 1 157 ? 8.999  0.229   3.753   0.32 16.50 ?  157 ASP   A N    1 
ATOM   3311 N  N    B ASP   A 1 157 ? 9.033  0.226   3.816   0.28 16.74 ?  157 ASP   A N    1 
ATOM   3312 N  N    T ASP   A 1 157 ? 9.145  0.200   3.582   0.40 15.47 ?  157 ASP   A N    1 
ATOM   3313 C  CA   A ASP   A 1 157 ? 7.672  0.472   3.200   0.32 17.54 ?  157 ASP   A CA   1 
ATOM   3314 C  CA   B ASP   A 1 157 ? 7.704  0.455   3.264   0.28 17.43 ?  157 ASP   A CA   1 
ATOM   3315 C  CA   T ASP   A 1 157 ? 7.853  0.551   3.014   0.40 15.79 ?  157 ASP   A CA   1 
ATOM   3316 C  C    A ASP   A 1 157 ? 6.684  -0.557  3.744   0.32 17.68 ?  157 ASP   A C    1 
ATOM   3317 C  C    B ASP   A 1 157 ? 6.731  -0.649  3.671   0.28 17.40 ?  157 ASP   A C    1 
ATOM   3318 C  C    T ASP   A 1 157 ? 6.798  -0.408  3.560   0.40 16.04 ?  157 ASP   A C    1 
ATOM   3319 O  O    A ASP   A 1 157 ? 6.825  -1.758  3.482   0.32 17.00 ?  157 ASP   A O    1 
ATOM   3320 O  O    B ASP   A 1 157 ? 7.092  -1.827  3.722   0.28 17.20 ?  157 ASP   A O    1 
ATOM   3321 O  O    T ASP   A 1 157 ? 6.851  -1.616  3.296   0.40 15.65 ?  157 ASP   A O    1 
ATOM   3322 C  CB   A ASP   A 1 157 ? 7.746  0.400   1.678   0.32 18.47 ?  157 ASP   A CB   1 
ATOM   3323 C  CB   B ASP   A 1 157 ? 7.784  0.532   1.740   0.28 18.20 ?  157 ASP   A CB   1 
ATOM   3324 C  CB   T ASP   A 1 157 ? 7.971  0.462   1.498   0.40 16.06 ?  157 ASP   A CB   1 
ATOM   3325 C  CG   A ASP   A 1 157 ? 6.501  0.929   1.007   0.32 19.23 ?  157 ASP   A CG   1 
ATOM   3326 C  CG   B ASP   A 1 157 ? 6.454  0.893   1.106   0.28 18.89 ?  157 ASP   A CG   1 
ATOM   3327 C  CG   T ASP   A 1 157 ? 6.791  1.036   0.792   0.40 15.91 ?  157 ASP   A CG   1 
ATOM   3328 O  OD1  A ASP   A 1 157 ? 6.341  2.165   0.942   0.32 19.67 ?  157 ASP   A OD1  1 
ATOM   3329 O  OD1  B ASP   A 1 157 ? 5.901  1.964   1.434   0.28 19.26 ?  157 ASP   A OD1  1 
ATOM   3330 O  OD1  T ASP   A 1 157 ? 5.700  0.442   0.914   0.40 15.96 ?  157 ASP   A OD1  1 
ATOM   3331 O  OD2  A ASP   A 1 157 ? 5.683  0.106   0.542   0.32 19.21 -1 157 ASP   A OD2  1 
ATOM   3332 O  OD2  B ASP   A 1 157 ? 5.952  0.096   0.284   0.28 18.92 -1 157 ASP   A OD2  1 
ATOM   3333 O  OD2  T ASP   A 1 157 ? 6.949  2.077   0.124   0.40 15.56 -1 157 ASP   A OD2  1 
ATOM   3334 H  H    A ASP   A 1 157 ? 9.533  -0.192  3.221   0.32 19.78 ?  157 ASP   A H    1 
ATOM   3335 H  H    B ASP   A 1 157 ? 9.540  -0.264  3.321   0.28 20.06 ?  157 ASP   A H    1 
ATOM   3336 H  H    T ASP   A 1 157 ? 9.599  -0.345  3.091   0.40 18.55 ?  157 ASP   A H    1 
ATOM   3337 H  HA   A ASP   A 1 157 ? 7.373  1.359   3.454   0.32 21.03 ?  157 ASP   A HA   1 
ATOM   3338 H  HA   B ASP   A 1 157 ? 7.367  1.302   3.598   0.28 20.89 ?  157 ASP   A HA   1 
ATOM   3339 H  HA   T ASP   A 1 157 ? 7.622  1.461   3.268   0.40 18.93 ?  157 ASP   A HA   1 
ATOM   3340 H  HB2  A ASP   A 1 157 ? 8.505  0.920   1.375   0.32 22.14 ?  157 ASP   A HB2  1 
ATOM   3341 H  HB2  B ASP   A 1 157 ? 8.462  1.190   1.495   0.28 21.81 ?  157 ASP   A HB2  1 
ATOM   3342 H  HB2  T ASP   A 1 157 ? 8.755  0.950   1.211   0.40 19.25 ?  157 ASP   A HB2  1 
ATOM   3343 H  HB3  A ASP   A 1 157 ? 7.858  -0.519  1.411   0.32 22.14 ?  157 ASP   A HB3  1 
ATOM   3344 H  HB3  B ASP   A 1 157 ? 8.034  -0.338  1.394   0.28 21.81 ?  157 ASP   A HB3  1 
ATOM   3345 H  HB3  T ASP   A 1 157 ? 8.049  -0.470  1.245   0.40 19.25 ?  157 ASP   A HB3  1 
ATOM   3346 N  N    A LYS   A 1 158 ? 5.687  -0.091  4.504   0.32 18.62 ?  158 LYS   A N    1 
ATOM   3347 N  N    B LYS   A 1 158 ? 5.480  -0.258  3.928   0.28 17.53 ?  158 LYS   A N    1 
ATOM   3348 N  N    T LYS   A 1 158 ? 5.851  0.125   4.340   0.40 17.30 ?  158 LYS   A N    1 
ATOM   3349 C  CA   A LYS   A 1 158 ? 4.698  -1.006  5.072   0.32 19.51 ?  158 LYS   A CA   1 
ATOM   3350 C  CA   B LYS   A 1 158 ? 4.495  -1.187  4.479   0.28 17.93 ?  158 LYS   A CA   1 
ATOM   3351 C  CA   T LYS   A 1 158 ? 4.851  -0.735  4.968   0.40 18.61 ?  158 LYS   A CA   1 
ATOM   3352 C  C    A LYS   A 1 158 ? 3.952  -1.749  3.974   0.32 18.66 ?  158 LYS   A C    1 
ATOM   3353 C  C    B LYS   A 1 158 ? 3.830  -2.016  3.384   0.28 17.20 ?  158 LYS   A C    1 
ATOM   3354 C  C    T LYS   A 1 158 ? 4.067  -1.520  3.928   0.40 17.60 ?  158 LYS   A C    1 
ATOM   3355 O  O    A LYS   A 1 158 ? 3.759  -2.968  4.054   0.32 18.65 ?  158 LYS   A O    1 
ATOM   3356 O  O    B LYS   A 1 158 ? 3.675  -3.234  3.526   0.28 16.66 ?  158 LYS   A O    1 
ATOM   3357 O  O    T LYS   A 1 158 ? 3.797  -2.712  4.114   0.40 17.29 ?  158 LYS   A O    1 
ATOM   3358 C  CB   A LYS   A 1 158 ? 3.716  -0.248  5.968   0.32 20.93 ?  158 LYS   A CB   1 
ATOM   3359 C  CB   B LYS   A 1 158 ? 3.456  -0.407  5.291   0.28 19.32 ?  158 LYS   A CB   1 
ATOM   3360 C  CB   T LYS   A 1 158 ? 3.904  0.076   5.854   0.40 21.00 ?  158 LYS   A CB   1 
ATOM   3361 C  CG   A LYS   A 1 158 ? 2.476  -1.058  6.384   0.32 22.18 ?  158 LYS   A CG   1 
ATOM   3362 C  CG   B LYS   A 1 158 ? 2.212  -1.198  5.675   0.28 20.72 ?  158 LYS   A CG   1 
ATOM   3363 C  CG   T LYS   A 1 158 ? 2.671  -0.705  6.323   0.40 23.01 ?  158 LYS   A CG   1 
ATOM   3364 C  CD   A LYS   A 1 158 ? 2.830  -2.346  7.133   0.32 23.18 ?  158 LYS   A CD   1 
ATOM   3365 C  CD   B LYS   A 1 158 ? 2.522  -2.327  6.645   0.28 21.98 ?  158 LYS   A CD   1 
ATOM   3366 C  CD   T LYS   A 1 158 ? 3.041  -1.953  7.128   0.40 24.98 ?  158 LYS   A CD   1 
ATOM   3367 C  CE   A LYS   A 1 158 ? 1.579  -3.043  7.664   0.32 23.68 ?  158 LYS   A CE   1 
ATOM   3368 C  CE   B LYS   A 1 158 ? 1.239  -2.949  7.180   0.28 22.78 ?  158 LYS   A CE   1 
ATOM   3369 C  CE   T LYS   A 1 158 ? 1.797  -2.750  7.523   0.40 26.33 ?  158 LYS   A CE   1 
ATOM   3370 N  NZ   A LYS   A 1 158 ? 1.878  -4.362  8.297   0.32 23.98 ?  158 LYS   A NZ   1 
ATOM   3371 N  NZ   B LYS   A 1 158 ? 1.500  -4.098  8.091   0.28 23.22 ?  158 LYS   A NZ   1 
ATOM   3372 N  NZ   T LYS   A 1 158 ? 2.116  -3.983  8.305   0.40 27.08 ?  158 LYS   A NZ   1 
ATOM   3373 H  H    A LYS   A 1 158 ? 5.570  0.737   4.700   0.32 22.32 ?  158 LYS   A H    1 
ATOM   3374 H  H    B LYS   A 1 158 ? 5.181  0.532   3.783   0.28 21.02 ?  158 LYS   A H    1 
ATOM   3375 H  H    T LYS   A 1 158 ? 5.777  0.962   4.520   0.40 20.74 ?  158 LYS   A H    1 
ATOM   3376 H  HA   A LYS   A 1 158 ? 5.156  -1.663  5.618   0.32 23.39 ?  158 LYS   A HA   1 
ATOM   3377 H  HA   B LYS   A 1 158 ? 4.945  -1.797  5.085   0.28 21.50 ?  158 LYS   A HA   1 
ATOM   3378 H  HA   T LYS   A 1 158 ? 5.309  -1.375  5.536   0.40 22.31 ?  158 LYS   A HA   1 
ATOM   3379 H  HB2  A LYS   A 1 158 ? 4.174  0.028   6.777   0.32 25.09 ?  158 LYS   A HB2  1 
ATOM   3380 H  HB2  B LYS   A 1 158 ? 3.873  -0.103  6.116   0.28 23.17 ?  158 LYS   A HB2  1 
ATOM   3381 H  HB2  T LYS   A 1 158 ? 4.388  0.365   6.645   0.40 25.18 ?  158 LYS   A HB2  1 
ATOM   3382 H  HB3  A LYS   A 1 158 ? 3.405  0.536   5.490   0.32 25.09 ?  158 LYS   A HB3  1 
ATOM   3383 H  HB3  B LYS   A 1 158 ? 3.169  0.360   4.773   0.28 23.17 ?  158 LYS   A HB3  1 
ATOM   3384 H  HB3  T LYS   A 1 158 ? 3.595  0.848   5.357   0.40 25.18 ?  158 LYS   A HB3  1 
ATOM   3385 H  HG2  A LYS   A 1 158 ? 1.933  -0.514  6.973   0.32 26.60 ?  158 LYS   A HG2  1 
ATOM   3386 H  HG2  B LYS   A 1 158 ? 1.588  -0.599  6.109   0.28 24.84 ?  158 LYS   A HG2  1 
ATOM   3387 H  HG2  T LYS   A 1 158 ? 2.138  -0.134  6.895   0.40 27.59 ?  158 LYS   A HG2  1 
ATOM   3388 H  HG3  A LYS   A 1 158 ? 1.962  -1.297  5.595   0.32 26.60 ?  158 LYS   A HG3  1 
ATOM   3389 H  HG3  B LYS   A 1 158 ? 1.802  -1.578  4.882   0.28 24.84 ?  158 LYS   A HG3  1 
ATOM   3390 H  HG3  T LYS   A 1 158 ? 2.143  -0.983  5.556   0.40 27.59 ?  158 LYS   A HG3  1 
ATOM   3391 H  HD2  A LYS   A 1 158 ? 3.286  -2.955  6.532   0.32 27.80 ?  158 LYS   A HD2  1 
ATOM   3392 H  HD2  B LYS   A 1 158 ? 3.031  -3.016  6.189   0.28 26.35 ?  158 LYS   A HD2  1 
ATOM   3393 H  HD2  T LYS   A 1 158 ? 3.610  -2.530  6.595   0.40 29.95 ?  158 LYS   A HD2  1 
ATOM   3394 H  HD3  A LYS   A 1 158 ? 3.394  -2.131  7.890   0.32 27.80 ?  158 LYS   A HD3  1 
ATOM   3395 H  HD3  B LYS   A 1 158 ? 3.029  -1.975  7.396   0.28 26.35 ?  158 LYS   A HD3  1 
ATOM   3396 H  HD3  T LYS   A 1 158 ? 3.499  -1.687  7.941   0.40 29.95 ?  158 LYS   A HD3  1 
ATOM   3397 H  HE2  A LYS   A 1 158 ? 1.163  -2.477  8.333   0.32 28.40 ?  158 LYS   A HE2  1 
ATOM   3398 H  HE2  B LYS   A 1 158 ? 0.745  -2.276  7.676   0.28 27.32 ?  158 LYS   A HE2  1 
ATOM   3399 H  HE2  T LYS   A 1 158 ? 1.221  -2.192  8.068   0.40 31.57 ?  158 LYS   A HE2  1 
ATOM   3400 H  HE3  A LYS   A 1 158 ? 0.964  -3.193  6.930   0.32 28.40 ?  158 LYS   A HE3  1 
ATOM   3401 H  HE3  B LYS   A 1 158 ? 0.708  -3.268  6.434   0.28 27.32 ?  158 LYS   A HE3  1 
ATOM   3402 H  HE3  T LYS   A 1 158 ? 1.328  -3.023  6.719   0.40 31.57 ?  158 LYS   A HE3  1 
ATOM   3403 H  HZ1  A LYS   A 1 158 ? 1.126  -4.735  8.593   0.32 28.75 ?  158 LYS   A HZ1  1 
ATOM   3404 H  HZ1  B LYS   A 1 158 ? 0.730  -4.430  8.388   0.28 27.85 ?  158 LYS   A HZ1  1 
ATOM   3405 H  HZ1  T LYS   A 1 158 ? 1.365  -4.415  8.513   0.40 32.48 ?  158 LYS   A HZ1  1 
ATOM   3406 H  HZ2  A LYS   A 1 158 ? 2.256  -4.906  7.702   0.32 28.75 ?  158 LYS   A HZ2  1 
ATOM   3407 H  HZ2  B LYS   A 1 158 ? 1.943  -4.735  7.656   0.28 27.85 ?  158 LYS   A HZ2  1 
ATOM   3408 H  HZ2  T LYS   A 1 158 ? 2.635  -4.523  7.825   0.40 32.48 ?  158 LYS   A HZ2  1 
ATOM   3409 H  HZ3  A LYS   A 1 158 ? 2.435  -4.251  8.982   0.32 28.75 ?  158 LYS   A HZ3  1 
ATOM   3410 H  HZ3  B LYS   A 1 158 ? 1.987  -3.830  8.786   0.28 27.85 ?  158 LYS   A HZ3  1 
ATOM   3411 H  HZ3  T LYS   A 1 158 ? 2.540  -3.766  9.057   0.40 32.48 ?  158 LYS   A HZ3  1 
ATOM   3412 N  N    A ASN   A 1 159 ? 3.514  -1.030  2.941   0.32 18.01 ?  159 ASN   A N    1 
ATOM   3413 N  N    B ASN   A 1 159 ? 3.423  -1.372  2.288   0.28 17.41 ?  159 ASN   A N    1 
ATOM   3414 N  N    T ASN   A 1 159 ? 3.681  -0.876  2.834   0.40 17.60 ?  159 ASN   A N    1 
ATOM   3415 C  CA   A ASN   A 1 159 ? 2.842  -1.698  1.834   0.32 17.47 ?  159 ASN   A CA   1 
ATOM   3416 C  CA   B ASN   A 1 159 ? 2.818  -2.109  1.185   0.28 17.93 ?  159 ASN   A CA   1 
ATOM   3417 C  CA   T ASN   A 1 159 ? 2.936  -1.578  1.800   0.40 18.00 ?  159 ASN   A CA   1 
ATOM   3418 C  C    A ASN   A 1 159 ? 3.747  -2.748  1.207   0.32 16.25 ?  159 ASN   A C    1 
ATOM   3419 C  C    B ASN   A 1 159 ? 3.760  -3.194  0.681   0.28 16.88 ?  159 ASN   A C    1 
ATOM   3420 C  C    T ASN   A 1 159 ? 3.763  -2.698  1.179   0.40 17.89 ?  159 ASN   A C    1 
ATOM   3421 O  O    A ASN   A 1 159 ? 3.309  -3.870  0.930   0.32 15.52 ?  159 ASN   A O    1 
ATOM   3422 O  O    B ASN   A 1 159 ? 3.333  -4.317  0.384   0.28 16.78 ?  159 ASN   A O    1 
ATOM   3423 O  O    T ASN   A 1 159 ? 3.230  -3.756  0.857   0.40 17.38 ?  159 ASN   A O    1 
ATOM   3424 C  CB   A ASN   A 1 159 ? 2.363  -0.673  0.804   0.32 18.42 ?  159 ASN   A CB   1 
ATOM   3425 C  CB   B ASN   A 1 159 ? 2.442  -1.142  0.060   0.28 19.64 ?  159 ASN   A CB   1 
ATOM   3426 C  CB   T ASN   A 1 159 ? 2.415  -0.606  0.738   0.40 18.95 ?  159 ASN   A CB   1 
ATOM   3427 C  CG   A ASN   A 1 159 ? 1.117  0.068   1.259   0.32 19.63 ?  159 ASN   A CG   1 
ATOM   3428 C  CG   B ASN   A 1 159 ? 1.436  -0.096  0.505   0.28 21.37 ?  159 ASN   A CG   1 
ATOM   3429 C  CG   T ASN   A 1 159 ? 1.166  0.132   1.193   0.40 20.14 ?  159 ASN   A CG   1 
ATOM   3430 O  OD1  A ASN   A 1 159 ? 0.284  -0.486  1.975   0.32 20.50 ?  159 ASN   A OD1  1 
ATOM   3431 O  OD1  B ASN   A 1 159 ? 0.264  -0.402  0.722   0.28 22.25 ?  159 ASN   A OD1  1 
ATOM   3432 O  OD1  T ASN   A 1 159 ? 0.383  -0.391  1.983   0.40 21.06 ?  159 ASN   A OD1  1 
ATOM   3433 N  ND2  A ASN   A 1 159 ? 0.985  1.322   0.847   0.32 20.08 ?  159 ASN   A ND2  1 
ATOM   3434 N  ND2  B ASN   A 1 159 ? 1.887  1.148   0.636   0.28 22.06 ?  159 ASN   A ND2  1 
ATOM   3435 N  ND2  T ASN   A 1 159 ? 0.976  1.348   0.698   0.40 20.54 ?  159 ASN   A ND2  1 
ATOM   3436 H  H    A ASN   A 1 159 ? 3.596  -0.179  2.856   0.32 21.59 ?  159 ASN   A H    1 
ATOM   3437 H  H    B ASN   A 1 159 ? 3.496  -0.528  2.162   0.28 20.87 ?  159 ASN   A H    1 
ATOM   3438 H  H    T ASN   A 1 159 ? 3.829  -0.045  2.673   0.40 21.09 ?  159 ASN   A H    1 
ATOM   3439 H  HA   A ASN   A 1 159 ? 2.062  -2.159  2.174   0.32 20.95 ?  159 ASN   A HA   1 
ATOM   3440 H  HA   B ASN   A 1 159 ? 2.009  -2.539  1.492   0.28 21.49 ?  159 ASN   A HA   1 
ATOM   3441 H  HA   T ASN   A 1 159 ? 2.169  -1.998  2.210   0.40 21.58 ?  159 ASN   A HA   1 
ATOM   3442 H  HB2  A ASN   A 1 159 ? 3.060  -0.018  0.654   0.32 22.08 ?  159 ASN   A HB2  1 
ATOM   3443 H  HB2  B ASN   A 1 159 ? 3.239  -0.677  -0.243  0.28 23.55 ?  159 ASN   A HB2  1 
ATOM   3444 H  HB2  T ASN   A 1 159 ? 3.096  0.053   0.545   0.40 22.72 ?  159 ASN   A HB2  1 
ATOM   3445 H  HB3  A ASN   A 1 159 ? 2.152  -1.131  -0.027  0.32 22.08 ?  159 ASN   A HB3  1 
ATOM   3446 H  HB3  B ASN   A 1 159 ? 2.049  -1.639  -0.672  0.28 23.55 ?  159 ASN   A HB3  1 
ATOM   3447 H  HB3  T ASN   A 1 159 ? 2.195  -1.105  -0.067  0.40 22.72 ?  159 ASN   A HB3  1 
ATOM   3448 H  HD21 A ASN   A 1 159 ? 0.294  1.779   1.078   0.32 24.07 ?  159 ASN   A HD21 1 
ATOM   3449 H  HD21 B ASN   A 1 159 ? 1.352  1.775   0.887   0.28 26.45 ?  159 ASN   A HD21 1 
ATOM   3450 H  HD21 T ASN   A 1 159 ? 0.279  1.799   0.926   0.40 24.63 ?  159 ASN   A HD21 1 
ATOM   3451 H  HD22 A ASN   A 1 159 ? 1.588  1.675   0.349   0.32 24.07 ?  159 ASN   A HD22 1 
ATOM   3452 H  HD22 B ASN   A 1 159 ? 2.711  1.327   0.473   0.28 26.45 ?  159 ASN   A HD22 1 
ATOM   3453 H  HD22 T ASN   A 1 159 ? 1.545  1.681   0.151   0.40 24.63 ?  159 ASN   A HD22 1 
ATOM   3454 N  N    A LEU   A 1 160 ? 5.025  -2.422  1.008   0.32 15.52 ?  160 LEU   A N    1 
ATOM   3455 N  N    B LEU   A 1 160 ? 5.052  -2.882  0.608   0.28 15.67 ?  160 LEU   A N    1 
ATOM   3456 N  N    T LEU   A 1 160 ? 5.065  -2.490  1.033   0.40 18.07 ?  160 LEU   A N    1 
ATOM   3457 C  CA   A LEU   A 1 160 ? 5.942  -3.428  0.485   0.32 15.01 ?  160 LEU   A CA   1 
ATOM   3458 C  CA   B LEU   A 1 160 ? 6.035  -3.876  0.202   0.28 14.95 ?  160 LEU   A CA   1 
ATOM   3459 C  CA   T LEU   A 1 160 ? 5.917  -3.547  0.504   0.40 18.15 ?  160 LEU   A CA   1 
ATOM   3460 C  C    A LEU   A 1 160 ? 6.116  -4.581  1.466   0.32 13.95 ?  160 LEU   A C    1 
ATOM   3461 C  C    B LEU   A 1 160 ? 6.121  -5.000  1.226   0.28 13.72 ?  160 LEU   A C    1 
ATOM   3462 O  O    A LEU   A 1 160 ? 6.149  -5.748  1.060   0.32 13.14 ?  160 LEU   A O    1 
ATOM   3463 O  O    B LEU   A 1 160 ? 6.058  -6.184  0.874   0.28 13.75 ?  160 LEU   A O    1 
ATOM   3464 C  CB   A LEU   A 1 160 ? 7.293  -2.809  0.139   0.32 15.37 ?  160 LEU   A CB   1 
ATOM   3465 C  CB   B LEU   A 1 160 ? 7.395  -3.198  0.031   0.28 15.73 ?  160 LEU   A CB   1 
ATOM   3466 C  CB   T LEU   A 1 160 ? 7.253  -2.988  0.021   0.40 18.06 ?  160 LEU   A CB   1 
ATOM   3467 C  CG   A LEU   A 1 160 ? 8.317  -3.841  -0.339  0.32 15.92 ?  160 LEU   A CG   1 
ATOM   3468 C  CG   B LEU   A 1 160 ? 8.561  -4.148  -0.227  0.28 16.55 ?  160 LEU   A CG   1 
ATOM   3469 C  CG   T LEU   A 1 160 ? 8.249  -4.047  -0.452  0.40 18.22 ?  160 LEU   A CG   1 
ATOM   3470 C  CD1  A LEU   A 1 160 ? 7.803  -4.614  -1.544  0.32 16.34 ?  160 LEU   A CD1  1 
ATOM   3471 C  CD1  B LEU   A 1 160 ? 8.220  -5.042  -1.398  0.28 16.48 ?  160 LEU   A CD1  1 
ATOM   3472 C  CD1  T LEU   A 1 160 ? 7.736  -4.758  -1.690  0.40 18.62 ?  160 LEU   A CD1  1 
ATOM   3473 C  CD2  A LEU   A 1 160 ? 9.639  -3.178  -0.656  0.32 16.24 ?  160 LEU   A CD2  1 
ATOM   3474 C  CD2  B LEU   A 1 160 ? 9.842  -3.371  -0.485  0.28 17.04 ?  160 LEU   A CD2  1 
ATOM   3475 C  CD2  T LEU   A 1 160 ? 9.600  -3.414  -0.719  0.40 18.28 ?  160 LEU   A CD2  1 
ATOM   3476 H  H    A LEU   A 1 160 ? 5.375  -1.649  1.163   0.32 18.60 ?  160 LEU   A H    1 
ATOM   3477 H  H    B LEU   A 1 160 ? 5.386  -2.115  0.807   0.28 18.78 ?  160 LEU   A H    1 
ATOM   3478 H  H    T LEU   A 1 160 ? 5.481  -1.760  1.236   0.40 21.67 ?  160 LEU   A H    1 
ATOM   3479 H  HA   A LEU   A 1 160 ? 5.571  -3.787  -0.329  0.32 17.99 ?  160 LEU   A HA   1 
ATOM   3480 H  HA   B LEU   A 1 160 ? 5.776  -4.255  -0.651  0.28 17.92 ?  160 LEU   A HA   1 
ATOM   3481 H  HB2  A LEU   A 1 160 ? 7.186  -2.130  -0.556  0.32 18.42 ?  160 LEU   A HB2  1 
ATOM   3482 H  HB2  B LEU   A 1 160 ? 7.349  -2.587  -0.723  0.28 18.85 ?  160 LEU   A HB2  1 
ATOM   3483 H  HB2  T LEU   A 1 160 ? 7.095  -2.381  -0.721  0.40 21.65 ?  160 LEU   A HB2  1 
ATOM   3484 H  HB3  A LEU   A 1 160 ? 7.662  -2.414  0.940   0.32 18.42 ?  160 LEU   A HB3  1 
ATOM   3485 H  HB3  B LEU   A 1 160 ? 7.601  -2.698  0.838   0.28 18.85 ?  160 LEU   A HB3  1 
ATOM   3486 H  HB3  T LEU   A 1 160 ? 7.674  -2.508  0.752   0.40 21.65 ?  160 LEU   A HB3  1 
ATOM   3487 H  HG   A LEU   A 1 160 ? 8.481  -4.475  0.376   0.32 19.09 ?  160 LEU   A HG   1 
ATOM   3488 H  HG   B LEU   A 1 160 ? 8.706  -4.705  0.555   0.28 19.84 ?  160 LEU   A HG   1 
ATOM   3489 H  HG   T LEU   A 1 160 ? 8.367  -4.709  0.249   0.40 21.84 ?  160 LEU   A HG   1 
ATOM   3490 H  HD11 A LEU   A 1 160 ? 8.531  -5.135  -1.915  0.32 19.58 ?  160 LEU   A HD11 1 
ATOM   3491 H  HD11 B LEU   A 1 160 ? 8.999  -5.559  -1.631  0.28 19.75 ?  160 LEU   A HD11 1 
ATOM   3492 H  HD11 T LEU   A 1 160 ? 8.408  -5.387  -1.995  0.40 22.33 ?  160 LEU   A HD11 1 
ATOM   3493 H  HD12 A LEU   A 1 160 ? 7.087  -5.204  -1.260  0.32 19.58 ?  160 LEU   A HD12 1 
ATOM   3494 H  HD12 B LEU   A 1 160 ? 7.495  -5.634  -1.143  0.28 19.75 ?  160 LEU   A HD12 1 
ATOM   3495 H  HD12 T LEU   A 1 160 ? 6.919  -5.228  -1.465  0.40 22.33 ?  160 LEU   A HD12 1 
ATOM   3496 H  HD13 A LEU   A 1 160 ? 7.475  -3.986  -2.205  0.32 19.58 ?  160 LEU   A HD13 1 
ATOM   3497 H  HD13 B LEU   A 1 160 ? 7.948  -4.486  -2.146  0.28 19.75 ?  160 LEU   A HD13 1 
ATOM   3498 H  HD13 T LEU   A 1 160 ? 7.562  -4.099  -2.380  0.40 22.33 ?  160 LEU   A HD13 1 
ATOM   3499 H  HD21 A LEU   A 1 160 ? 10.271 -3.858  -0.945  0.32 19.46 ?  160 LEU   A HD21 1 
ATOM   3500 H  HD21 B LEU   A 1 160 ? 10.570 -3.996  -0.634  0.28 20.43 ?  160 LEU   A HD21 1 
ATOM   3501 H  HD21 T LEU   A 1 160 ? 10.220 -4.099  -1.017  0.40 21.91 ?  160 LEU   A HD21 1 
ATOM   3502 H  HD22 A LEU   A 1 160 ? 9.507  -2.528  -1.362  0.32 19.46 ?  160 LEU   A HD22 1 
ATOM   3503 H  HD22 B LEU   A 1 160 ? 9.722  -2.812  -1.269  0.28 20.43 ?  160 LEU   A HD22 1 
ATOM   3504 H  HD22 T LEU   A 1 160 ? 9.501  -2.736  -1.406  0.40 21.91 ?  160 LEU   A HD22 1 
ATOM   3505 H  HD23 A LEU   A 1 160 ? 9.973  -2.738  0.143   0.32 19.46 ?  160 LEU   A HD23 1 
ATOM   3506 H  HD23 B LEU   A 1 160 ? 10.040 -2.815  0.287   0.28 20.43 ?  160 LEU   A HD23 1 
ATOM   3507 H  HD23 T LEU   A 1 160 ? 9.927  -3.008  0.100   0.40 21.91 ?  160 LEU   A HD23 1 
ATOM   3508 N  N    A TYR   A 1 161 ? 6.250  -4.278  2.758   0.72 15.43 ?  161 TYR   A N    1 
ATOM   3509 N  N    B TYR   A 1 161 ? 6.275  -4.643  2.502   0.28 13.36 ?  161 TYR   A N    1 
ATOM   3510 C  CA   A TYR   A 1 161 ? 6.377  -5.337  3.752   0.72 15.56 ?  161 TYR   A CA   1 
ATOM   3511 C  CA   B TYR   A 1 161 ? 6.343  -5.642  3.563   0.28 13.52 ?  161 TYR   A CA   1 
ATOM   3512 C  C    A TYR   A 1 161 ? 5.220  -6.323  3.656   0.72 16.54 ?  161 TYR   A C    1 
ATOM   3513 C  C    B TYR   A 1 161 ? 5.144  -6.579  3.503   0.28 14.11 ?  161 TYR   A C    1 
ATOM   3514 O  O    A TYR   A 1 161 ? 5.426  -7.541  3.573   0.72 16.14 ?  161 TYR   A O    1 
ATOM   3515 O  O    B TYR   A 1 161 ? 5.281  -7.794  3.689   0.28 13.83 ?  161 TYR   A O    1 
ATOM   3516 C  CB   A TYR   A 1 161 ? 6.455  -4.749  5.160   0.72 15.78 ?  161 TYR   A CB   1 
ATOM   3517 C  CB   B TYR   A 1 161 ? 6.423  -4.928  4.918   0.28 13.37 ?  161 TYR   A CB   1 
ATOM   3518 C  CG   A TYR   A 1 161 ? 6.358  -5.823  6.209   0.72 15.32 ?  161 TYR   A CG   1 
ATOM   3519 C  CG   B TYR   A 1 161 ? 6.326  -5.828  6.133   0.28 13.60 ?  161 TYR   A CG   1 
ATOM   3520 C  CD1  A TYR   A 1 161 ? 7.463  -6.589  6.544   0.72 15.00 ?  161 TYR   A CD1  1 
ATOM   3521 C  CD1  B TYR   A 1 161 ? 7.453  -6.444  6.664   0.28 13.66 ?  161 TYR   A CD1  1 
ATOM   3522 C  CD2  A TYR   A 1 161 ? 5.155  -6.088  6.852   0.72 15.29 ?  161 TYR   A CD2  1 
ATOM   3523 C  CD2  B TYR   A 1 161 ? 5.108  -6.040  6.768   0.28 14.01 ?  161 TYR   A CD2  1 
ATOM   3524 C  CE1  A TYR   A 1 161 ? 7.377  -7.581  7.487   0.72 14.46 ?  161 TYR   A CE1  1 
ATOM   3525 C  CE1  B TYR   A 1 161 ? 7.366  -7.262  7.779   0.28 13.95 ?  161 TYR   A CE1  1 
ATOM   3526 C  CE2  A TYR   A 1 161 ? 5.059  -7.082  7.799   0.72 14.62 ?  161 TYR   A CE2  1 
ATOM   3527 C  CE2  B TYR   A 1 161 ? 5.011  -6.856  7.883   0.28 14.16 ?  161 TYR   A CE2  1 
ATOM   3528 C  CZ   A TYR   A 1 161 ? 6.173  -7.825  8.113   0.72 14.07 ?  161 TYR   A CZ   1 
ATOM   3529 C  CZ   B TYR   A 1 161 ? 6.142  -7.464  8.385   0.28 14.40 ?  161 TYR   A CZ   1 
ATOM   3530 O  OH   A TYR   A 1 161 ? 6.111  -8.815  9.060   0.72 14.08 ?  161 TYR   A OH   1 
ATOM   3531 O  OH   B TYR   A 1 161 ? 6.052  -8.278  9.494   0.28 15.43 ?  161 TYR   A OH   1 
ATOM   3532 H  H    A TYR   A 1 161 ? 6.271  -3.477  3.082   0.72 18.50 ?  161 TYR   A H    1 
ATOM   3533 H  H    B TYR   A 1 161 ? 6.329  -3.834  2.775   0.28 16.01 ?  161 TYR   A H    1 
ATOM   3534 H  HA   A TYR   A 1 161 ? 7.190  -5.828  3.593   0.72 18.65 ?  161 TYR   A HA   1 
ATOM   3535 H  HA   B TYR   A 1 161 ? 7.143  -6.175  3.454   0.28 16.20 ?  161 TYR   A HA   1 
ATOM   3536 H  HB2  A TYR   A 1 161 ? 7.306  -4.293  5.272   0.72 18.91 ?  161 TYR   A HB2  1 
ATOM   3537 H  HB2  B TYR   A 1 161 ? 7.274  -4.463  4.970   0.28 16.02 ?  161 TYR   A HB2  1 
ATOM   3538 H  HB3  A TYR   A 1 161 ? 5.723  -4.124  5.296   0.72 18.91 ?  161 TYR   A HB3  1 
ATOM   3539 H  HB3  B TYR   A 1 161 ? 5.700  -4.285  4.973   0.28 16.02 ?  161 TYR   A HB3  1 
ATOM   3540 H  HD1  A TYR   A 1 161 ? 8.274  -6.428  6.122   0.72 17.97 ?  161 TYR   A HD1  1 
ATOM   3541 H  HD1  B TYR   A 1 161 ? 8.279  -6.311  6.261   0.28 16.37 ?  161 TYR   A HD1  1 
ATOM   3542 H  HD2  A TYR   A 1 161 ? 4.397  -5.588  6.642   0.72 18.33 ?  161 TYR   A HD2  1 
ATOM   3543 H  HD2  B TYR   A 1 161 ? 4.340  -5.633  6.436   0.28 16.79 ?  161 TYR   A HD2  1 
ATOM   3544 H  HE1  A TYR   A 1 161 ? 8.126  -8.090  7.701   0.72 17.33 ?  161 TYR   A HE1  1 
ATOM   3545 H  HE1  B TYR   A 1 161 ? 8.129  -7.671  8.123   0.28 16.72 ?  161 TYR   A HE1  1 
ATOM   3546 H  HE2  A TYR   A 1 161 ? 4.243  -7.252  8.225   0.72 17.52 ?  161 TYR   A HE2  1 
ATOM   3547 H  HE2  B TYR   A 1 161 ? 4.185  -6.990  8.296   0.28 16.97 ?  161 TYR   A HE2  1 
ATOM   3548 H  HH   A TYR   A 1 161 ? 6.853  -9.191  9.145   0.72 16.88 ?  161 TYR   A HH   1 
ATOM   3549 H  HH   B TYR   A 1 161 ? 6.808  -8.583  9.695   0.28 18.50 ?  161 TYR   A HH   1 
ATOM   3550 N  N    A ASP   A 1 162 ? 3.985  -5.813  3.679   0.72 17.22 ?  162 ASP   A N    1 
ATOM   3551 N  N    B ASP   A 1 162 ? 3.960  -6.030  3.220   0.28 14.49 ?  162 ASP   A N    1 
ATOM   3552 C  CA   A ASP   A 1 162 ? 2.828  -6.702  3.595   0.72 18.10 ?  162 ASP   A CA   1 
ATOM   3553 C  CA   B ASP   A 1 162 ? 2.749  -6.842  3.129   0.28 15.36 ?  162 ASP   A CA   1 
ATOM   3554 C  C    A ASP   A 1 162 ? 2.863  -7.523  2.317   0.72 18.22 ?  162 ASP   A C    1 
ATOM   3555 C  C    B ASP   A 1 162 ? 2.846  -7.848  1.986   0.28 15.45 ?  162 ASP   A C    1 
ATOM   3556 O  O    A ASP   A 1 162 ? 2.510  -8.710  2.322   0.72 18.85 ?  162 ASP   A O    1 
ATOM   3557 O  O    B ASP   A 1 162 ? 2.504  -9.027  2.147   0.28 15.72 ?  162 ASP   A O    1 
ATOM   3558 C  CB   A ASP   A 1 162 ? 1.529  -5.904  3.665   0.72 19.04 ?  162 ASP   A CB   1 
ATOM   3559 C  CB   B ASP   A 1 162 ? 1.529  -5.929  2.954   0.28 16.42 ?  162 ASP   A CB   1 
ATOM   3560 C  CG   A ASP   A 1 162 ? 1.224  -5.408  5.048   0.72 20.17 ?  162 ASP   A CG   1 
ATOM   3561 C  CG   B ASP   A 1 162 ? 1.221  -5.105  4.202   0.28 17.28 ?  162 ASP   A CG   1 
ATOM   3562 O  OD1  A ASP   A 1 162 ? 1.863  -5.875  6.010   0.72 20.69 ?  162 ASP   A OD1  1 
ATOM   3563 O  OD1  B ASP   A 1 162 ? 1.726  -5.451  5.290   0.28 17.57 ?  162 ASP   A OD1  1 
ATOM   3564 O  OD2  A ASP   A 1 162 ? 0.335  -4.544  5.161   0.72 21.36 -1 162 ASP   A OD2  1 
ATOM   3565 O  OD2  B ASP   A 1 162 ? 0.451  -4.125  4.100   0.28 17.83 -1 162 ASP   A OD2  1 
ATOM   3566 H  H    A ASP   A 1 162 ? 3.789  -4.969  3.735   0.72 20.65 ?  162 ASP   A H    1 
ATOM   3567 H  H    B ASP   A 1 162 ? 3.833  -5.193  3.076   0.28 17.37 ?  162 ASP   A H    1 
ATOM   3568 H  HA   A ASP   A 1 162 ? 2.843  -7.314  4.340   0.72 21.70 ?  162 ASP   A HA   1 
ATOM   3569 H  HA   B ASP   A 1 162 ? 2.630  -7.336  3.951   0.28 18.41 ?  162 ASP   A HA   1 
ATOM   3570 H  HB2  A ASP   A 1 162 ? 1.591  -5.123  3.098   0.72 22.83 ?  162 ASP   A HB2  1 
ATOM   3571 H  HB2  B ASP   A 1 162 ? 1.689  -5.320  2.211   0.28 19.68 ?  162 ASP   A HB2  1 
ATOM   3572 H  HB3  A ASP   A 1 162 ? 0.788  -6.465  3.386   0.72 22.83 ?  162 ASP   A HB3  1 
ATOM   3573 H  HB3  B ASP   A 1 162 ? 0.745  -6.466  2.776   0.28 19.68 ?  162 ASP   A HB3  1 
ATOM   3574 N  N    A LYS   A 1 163 ? 3.273  -6.908  1.205   0.72 18.19 ?  163 LYS   A N    1 
ATOM   3575 N  N    B LYS   A 1 163 ? 3.313  -7.398  0.817   0.28 15.53 ?  163 LYS   A N    1 
ATOM   3576 C  CA   A LYS   A 1 163 ? 3.363  -7.658  -0.042  0.72 18.62 ?  163 LYS   A CA   1 
ATOM   3577 C  CA   B LYS   A 1 163 ? 3.439  -8.299  -0.326  0.28 15.91 ?  163 LYS   A CA   1 
ATOM   3578 C  C    A LYS   A 1 163 ? 4.424  -8.748  0.045   0.72 17.96 ?  163 LYS   A C    1 
ATOM   3579 C  C    B LYS   A 1 163 ? 4.547  -9.323  -0.101  0.28 15.31 ?  163 LYS   A C    1 
ATOM   3580 O  O    A LYS   A 1 163 ? 4.248  -9.839  -0.508  0.72 17.21 ?  163 LYS   A O    1 
ATOM   3581 O  O    B LYS   A 1 163 ? 4.391  -10.501 -0.445  0.28 15.76 ?  163 LYS   A O    1 
ATOM   3582 C  CB   A LYS   A 1 163 ? 3.650  -6.724  -1.220  0.72 20.62 ?  163 LYS   A CB   1 
ATOM   3583 C  CB   B LYS   A 1 163 ? 3.695  -7.488  -1.598  0.28 17.55 ?  163 LYS   A CB   1 
ATOM   3584 C  CG   A LYS   A 1 163 ? 3.761  -7.460  -2.549  0.72 23.21 ?  163 LYS   A CG   1 
ATOM   3585 C  CG   B LYS   A 1 163 ? 3.573  -8.289  -2.887  0.28 19.29 ?  163 LYS   A CG   1 
ATOM   3586 C  CD   A LYS   A 1 163 ? 4.155  -6.541  -3.689  0.72 25.94 ?  163 LYS   A CD   1 
ATOM   3587 C  CD   B LYS   A 1 163 ? 3.706  -7.396  -4.113  0.28 20.82 ?  163 LYS   A CD   1 
ATOM   3588 C  CE   A LYS   A 1 163 ? 4.172  -7.296  -5.012  0.72 27.95 ?  163 LYS   A CE   1 
ATOM   3589 C  CE   B LYS   A 1 163 ? 3.372  -8.155  -5.388  0.28 21.98 ?  163 LYS   A CE   1 
ATOM   3590 N  NZ   A LYS   A 1 163 ? 4.708  -6.467  -6.126  0.72 29.19 ?  163 LYS   A NZ   1 
ATOM   3591 N  NZ   B LYS   A 1 163 ? 3.586  -7.333  -6.612  0.28 22.52 ?  163 LYS   A NZ   1 
ATOM   3592 H  H    A LYS   A 1 163 ? 3.494  -6.071  1.147   0.72 21.80 ?  163 LYS   A H    1 
ATOM   3593 H  H    B LYS   A 1 163 ? 3.557  -6.585  0.661   0.28 18.61 ?  163 LYS   A H    1 
ATOM   3594 H  HA   A LYS   A 1 163 ? 2.511  -8.088  -0.207  0.72 22.33 ?  163 LYS   A HA   1 
ATOM   3595 H  HA   B LYS   A 1 163 ? 2.604  -8.777  -0.443  0.28 19.07 ?  163 LYS   A HA   1 
ATOM   3596 H  HB2  A LYS   A 1 163 ? 2.923  -6.080  -1.299  0.72 24.72 ?  163 LYS   A HB2  1 
ATOM   3597 H  HB2  B LYS   A 1 163 ? 3.051  -6.762  -1.643  0.28 21.03 ?  163 LYS   A HB2  1 
ATOM   3598 H  HB3  A LYS   A 1 163 ? 4.484  -6.260  -1.064  0.72 24.72 ?  163 LYS   A HB3  1 
ATOM   3599 H  HB3  B LYS   A 1 163 ? 4.593  -7.124  -1.563  0.28 21.03 ?  163 LYS   A HB3  1 
ATOM   3600 H  HG2  A LYS   A 1 163 ? 4.438  -8.150  -2.480  0.72 27.83 ?  163 LYS   A HG2  1 
ATOM   3601 H  HG2  B LYS   A 1 163 ? 4.278  -8.953  -2.920  0.28 23.13 ?  163 LYS   A HG2  1 
ATOM   3602 H  HG3  A LYS   A 1 163 ? 2.902  -7.859  -2.763  0.72 27.83 ?  163 LYS   A HG3  1 
ATOM   3603 H  HG3  B LYS   A 1 163 ? 2.704  -8.718  -2.919  0.28 23.13 ?  163 LYS   A HG3  1 
ATOM   3604 H  HD2  A LYS   A 1 163 ? 3.511  -5.820  -3.757  0.72 31.11 ?  163 LYS   A HD2  1 
ATOM   3605 H  HD2  B LYS   A 1 163 ? 3.092  -6.648  -4.034  0.28 24.97 ?  163 LYS   A HD2  1 
ATOM   3606 H  HD3  A LYS   A 1 163 ? 5.043  -6.190  -3.525  0.72 31.11 ?  163 LYS   A HD3  1 
ATOM   3607 H  HD3  B LYS   A 1 163 ? 4.619  -7.073  -4.180  0.28 24.97 ?  163 LYS   A HD3  1 
ATOM   3608 H  HE2  A LYS   A 1 163 ? 4.728  -8.085  -4.920  0.72 33.52 ?  163 LYS   A HE2  1 
ATOM   3609 H  HE2  B LYS   A 1 163 ? 3.939  -8.938  -5.449  0.28 26.36 ?  163 LYS   A HE2  1 
ATOM   3610 H  HE3  A LYS   A 1 163 ? 3.265  -7.557  -5.240  0.72 33.52 ?  163 LYS   A HE3  1 
ATOM   3611 H  HE3  B LYS   A 1 163 ? 2.438  -8.419  -5.364  0.28 26.36 ?  163 LYS   A HE3  1 
ATOM   3612 H  HZ1  A LYS   A 1 163 ? 4.705  -6.935  -6.883  0.72 35.01 ?  163 LYS   A HZ1  1 
ATOM   3613 H  HZ1  B LYS   A 1 163 ? 3.381  -7.807  -7.337  0.28 27.00 ?  163 LYS   A HZ1  1 
ATOM   3614 H  HZ2  A LYS   A 1 163 ? 4.204  -5.741  -6.233  0.72 35.01 ?  163 LYS   A HZ2  1 
ATOM   3615 H  HZ2  B LYS   A 1 163 ? 3.071  -6.608  -6.586  0.28 27.00 ?  163 LYS   A HZ2  1 
ATOM   3616 H  HZ3  A LYS   A 1 163 ? 5.542  -6.216  -5.944  0.72 35.01 ?  163 LYS   A HZ3  1 
ATOM   3617 H  HZ3  B LYS   A 1 163 ? 4.438  -7.081  -6.663  0.28 27.00 ?  163 LYS   A HZ3  1 
ATOM   3618 N  N    A LEU   A 1 164 ? 5.539  -8.473  0.728   0.72 16.89 ?  164 LEU   A N    1 
ATOM   3619 N  N    B LEU   A 1 164 ? 5.674  -8.888  0.469   0.28 14.15 ?  164 LEU   A N    1 
ATOM   3620 C  CA   A LEU   A 1 164 ? 6.608  -9.466  0.815   0.72 16.70 ?  164 LEU   A CA   1 
ATOM   3621 C  CA   B LEU   A 1 164 ? 6.763  -9.811  0.778   0.28 13.88 ?  164 LEU   A CA   1 
ATOM   3622 C  C    A LEU   A 1 164 ? 6.181  -10.671 1.643   0.72 17.16 ?  164 LEU   A C    1 
ATOM   3623 C  C    B LEU   A 1 164 ? 6.282  -10.930 1.692   0.28 14.47 ?  164 LEU   A C    1 
ATOM   3624 O  O    A LEU   A 1 164 ? 6.472  -11.817 1.278   0.72 17.25 ?  164 LEU   A O    1 
ATOM   3625 O  O    B LEU   A 1 164 ? 6.573  -12.109 1.458   0.28 14.30 ?  164 LEU   A O    1 
ATOM   3626 C  CB   A LEU   A 1 164 ? 7.858  -8.832  1.416   0.72 16.42 ?  164 LEU   A CB   1 
ATOM   3627 C  CB   B LEU   A 1 164 ? 7.912  -9.051  1.444   0.28 13.53 ?  164 LEU   A CB   1 
ATOM   3628 C  CG   A LEU   A 1 164 ? 8.607  -7.892  0.477   0.72 16.33 ?  164 LEU   A CG   1 
ATOM   3629 C  CG   B LEU   A 1 164 ? 8.782  -8.130  0.588   0.28 13.71 ?  164 LEU   A CG   1 
ATOM   3630 C  CD1  A LEU   A 1 164 ? 9.567  -7.039  1.277   0.72 15.73 ?  164 LEU   A CD1  1 
ATOM   3631 C  CD1  B LEU   A 1 164 ? 9.674  -7.275  1.478   0.28 13.90 ?  164 LEU   A CD1  1 
ATOM   3632 C  CD2  A LEU   A 1 164 ? 9.356  -8.671  -0.594  0.72 16.76 ?  164 LEU   A CD2  1 
ATOM   3633 C  CD2  B LEU   A 1 164 ? 9.629  -8.939  -0.373  0.28 13.67 ?  164 LEU   A CD2  1 
ATOM   3634 H  H    A LEU   A 1 164 ? 5.703  -7.723  1.138   0.72 20.25 ?  164 LEU   A H    1 
ATOM   3635 H  H    B LEU   A 1 164 ? 5.830  -8.072  0.687   0.28 16.95 ?  164 LEU   A H    1 
ATOM   3636 H  HA   A LEU   A 1 164 ? 6.826  -9.767  -0.077  0.72 20.01 ?  164 LEU   A HA   1 
ATOM   3637 H  HA   B LEU   A 1 164 ? 7.095  -10.209 -0.041  0.28 16.64 ?  164 LEU   A HA   1 
ATOM   3638 H  HB2  A LEU   A 1 164 ? 7.606  -8.318  2.200   0.72 19.68 ?  164 LEU   A HB2  1 
ATOM   3639 H  HB2  B LEU   A 1 164 ? 7.536  -8.499  2.145   0.28 16.21 ?  164 LEU   A HB2  1 
ATOM   3640 H  HB3  A LEU   A 1 164 ? 8.472  -9.537  1.671   0.72 19.68 ?  164 LEU   A HB3  1 
ATOM   3641 H  HB3  B LEU   A 1 164 ? 8.510  -9.702  1.840   0.28 16.21 ?  164 LEU   A HB3  1 
ATOM   3642 H  HG   A LEU   A 1 164 ? 7.976  -7.301  0.038   0.72 19.58 ?  164 LEU   A HG   1 
ATOM   3643 H  HG   B LEU   A 1 164 ? 8.217  -7.535  0.071   0.28 16.43 ?  164 LEU   A HG   1 
ATOM   3644 H  HD11 A LEU   A 1 164 ? 10.046 -6.449  0.676   0.72 18.86 ?  164 LEU   A HD11 1 
ATOM   3645 H  HD11 B LEU   A 1 164 ? 10.225 -6.701  0.922   0.28 16.65 ?  164 LEU   A HD11 1 
ATOM   3646 H  HD12 A LEU   A 1 164 ? 9.064  -6.519  1.924   0.72 18.86 ?  164 LEU   A HD12 1 
ATOM   3647 H  HD12 B LEU   A 1 164 ? 9.118  -6.734  2.061   0.28 16.65 ?  164 LEU   A HD12 1 
ATOM   3648 H  HD13 A LEU   A 1 164 ? 10.194 -7.620  1.739   0.72 18.86 ?  164 LEU   A HD13 1 
ATOM   3649 H  HD13 B LEU   A 1 164 ? 10.242 -7.857  2.011   0.28 16.65 ?  164 LEU   A HD13 1 
ATOM   3650 H  HD21 A LEU   A 1 164 ? 9.880  -8.053  -1.128  0.72 20.08 ?  164 LEU   A HD21 1 
ATOM   3651 H  HD21 B LEU   A 1 164 ? 10.189 -8.337  -0.887  0.28 16.39 ?  164 LEU   A HD21 1 
ATOM   3652 H  HD22 A LEU   A 1 164 ? 9.941  -9.315  -0.164  0.72 20.08 ?  164 LEU   A HD22 1 
ATOM   3653 H  HD22 B LEU   A 1 164 ? 10.182 -9.553  0.135   0.28 16.39 ?  164 LEU   A HD22 1 
ATOM   3654 H  HD23 A LEU   A 1 164 ? 8.713  -9.131  -1.156  0.72 20.08 ?  164 LEU   A HD23 1 
ATOM   3655 H  HD23 B LEU   A 1 164 ? 9.043  -9.434  -0.965  0.28 16.39 ?  164 LEU   A HD23 1 
ATOM   3656 N  N    A VAL   A 1 165 ? 5.508  -10.430 2.768   0.72 16.71 ?  165 VAL   A N    1 
ATOM   3657 N  N    B VAL   A 1 165 ? 5.559  -10.573 2.754   0.28 14.73 ?  165 VAL   A N    1 
ATOM   3658 C  CA   A VAL   A 1 165 ? 5.061  -11.526 3.623   0.72 16.80 ?  165 VAL   A CA   1 
ATOM   3659 C  CA   B VAL   A 1 165 ? 4.994  -11.581 3.645   0.28 15.32 ?  165 VAL   A CA   1 
ATOM   3660 C  C    A VAL   A 1 165 ? 4.043  -12.390 2.892   0.72 16.83 ?  165 VAL   A C    1 
ATOM   3661 C  C    B VAL   A 1 165 ? 3.940  -12.404 2.914   0.28 15.93 ?  165 VAL   A C    1 
ATOM   3662 O  O    A VAL   A 1 165 ? 4.154  -13.622 2.857   0.72 16.85 ?  165 VAL   A O    1 
ATOM   3663 O  O    B VAL   A 1 165 ? 3.978  -13.640 2.919   0.28 16.00 ?  165 VAL   A O    1 
ATOM   3664 C  CB   A VAL   A 1 165 ? 4.494  -10.968 4.942   0.72 17.51 ?  165 VAL   A CB   1 
ATOM   3665 C  CB   B VAL   A 1 165 ? 4.422  -10.917 4.911   0.28 15.68 ?  165 VAL   A CB   1 
ATOM   3666 C  CG1  A VAL   A 1 165 ? 3.761  -12.057 5.721   0.72 17.75 ?  165 VAL   A CG1  1 
ATOM   3667 C  CG1  B VAL   A 1 165 ? 3.672  -11.937 5.757   0.28 15.79 ?  165 VAL   A CG1  1 
ATOM   3668 C  CG2  A VAL   A 1 165 ? 5.610  -10.341 5.775   0.72 17.86 ?  165 VAL   A CG2  1 
ATOM   3669 C  CG2  B VAL   A 1 165 ? 5.533  -10.259 5.722   0.28 15.85 ?  165 VAL   A CG2  1 
ATOM   3670 H  H    A VAL   A 1 165 ? 5.300  -9.643  3.056   0.72 20.03 ?  165 VAL   A H    1 
ATOM   3671 H  H    B VAL   A 1 165 ? 5.389  -9.759  2.981   0.28 17.65 ?  165 VAL   A H    1 
ATOM   3672 H  HA   A VAL   A 1 165 ? 5.820  -12.082 3.842   0.72 20.14 ?  165 VAL   A HA   1 
ATOM   3673 H  HA   B VAL   A 1 165 ? 5.701  -12.182 3.925   0.28 18.36 ?  165 VAL   A HA   1 
ATOM   3674 H  HB   A VAL   A 1 165 ? 3.853  -10.268 4.740   0.72 20.99 ?  165 VAL   A HB   1 
ATOM   3675 H  HB   B VAL   A 1 165 ? 3.794  -10.225 4.652   0.28 18.79 ?  165 VAL   A HB   1 
ATOM   3676 H  HG11 A VAL   A 1 165 ? 3.665  -11.774 6.644   0.72 21.28 ?  165 VAL   A HG11 1 
ATOM   3677 H  HG11 B VAL   A 1 165 ? 3.541  -11.572 6.647   0.28 18.93 ?  165 VAL   A HG11 1 
ATOM   3678 H  HG12 A VAL   A 1 165 ? 2.883  -12.192 5.328   0.72 21.28 ?  165 VAL   A HG12 1 
ATOM   3679 H  HG12 B VAL   A 1 165 ? 2.812  -12.119 5.347   0.28 18.93 ?  165 VAL   A HG12 1 
ATOM   3680 H  HG13 A VAL   A 1 165 ? 4.275  -12.876 5.678   0.72 21.28 ?  165 VAL   A HG13 1 
ATOM   3681 H  HG13 B VAL   A 1 165 ? 4.197  -12.750 5.808   0.28 18.93 ?  165 VAL   A HG13 1 
ATOM   3682 H  HG21 A VAL   A 1 165 ? 5.241  -10.031 6.618   0.72 21.42 ?  165 VAL   A HG21 1 
ATOM   3683 H  HG21 B VAL   A 1 165 ? 5.141  -9.801  6.483   0.28 19.00 ?  165 VAL   A HG21 1 
ATOM   3684 H  HG22 A VAL   A 1 165 ? 6.295  -11.006 5.939   0.72 21.42 ?  165 VAL   A HG22 1 
ATOM   3685 H  HG22 B VAL   A 1 165 ? 6.147  -10.943 6.030   0.28 19.00 ?  165 VAL   A HG22 1 
ATOM   3686 H  HG23 A VAL   A 1 165 ? 5.986  -9.591  5.286   0.72 21.42 ?  165 VAL   A HG23 1 
ATOM   3687 H  HG23 B VAL   A 1 165 ? 6.002  -9.622  5.160   0.28 19.00 ?  165 VAL   A HG23 1 
ATOM   3688 N  N    A SER   A 1 166 ? 3.034  -11.753 2.294   0.72 17.23 ?  166 SER   A N    1 
ATOM   3689 N  N    B SER   A 1 166 ? 2.983  -11.728 2.271   0.28 16.56 ?  166 SER   A N    1 
ATOM   3690 C  CA   A SER   A 1 166 ? 1.927  -12.507 1.714   0.72 18.32 ?  166 SER   A CA   1 
ATOM   3691 C  CA   B SER   A 1 166 ? 1.863  -12.427 1.649   0.28 17.40 ?  166 SER   A CA   1 
ATOM   3692 C  C    A SER   A 1 166 ? 2.377  -13.363 0.541   0.72 18.95 ?  166 SER   A C    1 
ATOM   3693 C  C    B SER   A 1 166 ? 2.271  -13.236 0.427   0.28 17.80 ?  166 SER   A C    1 
ATOM   3694 O  O    A SER   A 1 166 ? 1.770  -14.411 0.278   0.72 20.76 ?  166 SER   A O    1 
ATOM   3695 O  O    B SER   A 1 166 ? 1.511  -14.114 0.005   0.28 17.82 ?  166 SER   A O    1 
ATOM   3696 C  CB   A SER   A 1 166 ? 0.807  -11.560 1.276   0.72 19.83 ?  166 SER   A CB   1 
ATOM   3697 C  CB   B SER   A 1 166 ? 0.772  -11.437 1.237   0.28 18.14 ?  166 SER   A CB   1 
ATOM   3698 O  OG   A SER   A 1 166 ? 0.141  -10.988 2.389   0.72 21.79 ?  166 SER   A OG   1 
ATOM   3699 O  OG   B SER   A 1 166 ? 0.184  -10.815 2.363   0.28 19.05 ?  166 SER   A OG   1 
ATOM   3700 H  H    A SER   A 1 166 ? 2.961  -10.900 2.223   0.72 20.65 ?  166 SER   A H    1 
ATOM   3701 H  H    B SER   A 1 166 ? 2.957  -10.871 2.195   0.28 19.85 ?  166 SER   A H    1 
ATOM   3702 H  HA   A SER   A 1 166 ? 1.559  -13.102 2.385   0.72 21.96 ?  166 SER   A HA   1 
ATOM   3703 H  HA   B SER   A 1 166 ? 1.480  -13.034 2.298   0.28 20.86 ?  166 SER   A HA   1 
ATOM   3704 H  HB2  A SER   A 1 166 ? 1.184  -10.857 0.723   0.72 23.77 ?  166 SER   A HB2  1 
ATOM   3705 H  HB2  B SER   A 1 166 ? 1.163  -10.758 0.668   0.28 21.75 ?  166 SER   A HB2  1 
ATOM   3706 H  HB3  A SER   A 1 166 ? 0.147  -12.058 0.770   0.72 23.77 ?  166 SER   A HB3  1 
ATOM   3707 H  HB3  B SER   A 1 166 ? 0.084  -11.920 0.749   0.28 21.75 ?  166 SER   A HB3  1 
ATOM   3708 H  HG   A SER   A 1 166 ? -0.445 -10.444 2.129   0.72 26.13 ?  166 SER   A HG   1 
ATOM   3709 H  HG   B SER   A 1 166 ? 0.769  -10.395 2.793   0.28 22.83 ?  166 SER   A HG   1 
ATOM   3710 N  N    . SER   A 1 167 ? 3.424  -12.943 -0.173  1.00 18.14 ?  167 SER   A N    1 
ATOM   3711 C  CA   . SER   A 1 167 ? 3.896  -13.671 -1.342  1.00 19.40 ?  167 SER   A CA   1 
ATOM   3712 C  C    . SER   A 1 167 ? 5.038  -14.632 -1.032  1.00 19.61 ?  167 SER   A C    1 
ATOM   3713 O  O    . SER   A 1 167 ? 5.532  -15.299 -1.948  1.00 20.48 ?  167 SER   A O    1 
ATOM   3714 C  CB   . SER   A 1 167 ? 4.317  -12.701 -2.460  1.00 19.87 ?  167 SER   A CB   1 
ATOM   3715 O  OG   . SER   A 1 167 ? 5.370  -11.842 -2.044  1.00 20.16 ?  167 SER   A OG   1 
ATOM   3716 H  H    A SER   A 1 167 ? 3.881  -12.229 0.007   0.72 21.75 ?  167 SER   A H    1 
ATOM   3717 H  H    B SER   A 1 167 ? 3.946  -12.296 0.071   0.28 21.75 ?  167 SER   A H    1 
ATOM   3718 H  HA   . SER   A 1 167 ? 3.163  -14.194 -1.690  1.00 23.26 ?  167 SER   A HA   1 
ATOM   3719 H  HB2  . SER   A 1 167 ? 4.622  -13.221 -3.224  1.00 23.82 ?  167 SER   A HB2  1 
ATOM   3720 H  HB3  . SER   A 1 167 ? 3.547  -12.166 -2.721  1.00 23.82 ?  167 SER   A HB3  1 
ATOM   3721 H  HG   . SER   A 1 167 ? 5.044  -11.087 -1.839  1.00 24.17 ?  167 SER   A HG   1 
ATOM   3722 N  N    . PHE   A 1 168 ? 5.470  -14.725 0.223   1.00 19.33 ?  168 PHE   A N    1 
ATOM   3723 C  CA   . PHE   A 1 168 ? 6.643  -15.532 0.536   1.00 19.99 ?  168 PHE   A CA   1 
ATOM   3724 C  C    . PHE   A 1 168 ? 6.327  -17.014 0.425   1.00 23.30 ?  168 PHE   A C    1 
ATOM   3725 O  O    . PHE   A 1 168 ? 5.325  -17.492 0.969   1.00 24.21 ?  168 PHE   A O    1 
ATOM   3726 C  CB   . PHE   A 1 168 ? 7.145  -15.256 1.949   1.00 18.77 ?  168 PHE   A CB   1 
ATOM   3727 C  CG   . PHE   A 1 168 ? 8.409  -16.001 2.273   1.00 17.66 ?  168 PHE   A CG   1 
ATOM   3728 C  CD1  . PHE   A 1 168 ? 9.597  -15.631 1.675   1.00 17.81 ?  168 PHE   A CD1  1 
ATOM   3729 C  CD2  . PHE   A 1 168 ? 8.415  -17.084 3.139   1.00 17.36 ?  168 PHE   A CD2  1 
ATOM   3730 C  CE1  . PHE   A 1 168 ? 10.767 -16.308 1.943   1.00 17.40 ?  168 PHE   A CE1  1 
ATOM   3731 C  CE2  . PHE   A 1 168 ? 9.595  -17.765 3.415   1.00 17.75 ?  168 PHE   A CE2  1 
ATOM   3732 C  CZ   . PHE   A 1 168 ? 10.766 -17.372 2.813   1.00 17.63 ?  168 PHE   A CZ   1 
ATOM   3733 H  H    . PHE   A 1 168 ? 5.122  -14.317 0.896   1.00 23.18 ?  168 PHE   A H    1 
ATOM   3734 H  HA   . PHE   A 1 168 ? 7.359  -15.317 -0.090  1.00 23.97 ?  168 PHE   A HA   1 
ATOM   3735 H  HB2  . PHE   A 1 168 ? 7.327  -14.309 2.044   1.00 22.50 ?  168 PHE   A HB2  1 
ATOM   3736 H  HB3  . PHE   A 1 168 ? 6.464  -15.529 2.582   1.00 22.50 ?  168 PHE   A HB3  1 
ATOM   3737 H  HD1  . PHE   A 1 168 ? 9.611  -14.913 1.087   1.00 21.35 ?  168 PHE   A HD1  1 
ATOM   3738 H  HD2  . PHE   A 1 168 ? 7.624  -17.353 3.550   1.00 20.81 ?  168 PHE   A HD2  1 
ATOM   3739 H  HE1  . PHE   A 1 168 ? 11.566 -16.044 1.539   1.00 20.85 ?  168 PHE   A HE1  1 
ATOM   3740 H  HE2  . PHE   A 1 168 ? 9.592  -18.488 4.002   1.00 21.27 ?  168 PHE   A HE2  1 
ATOM   3741 H  HZ   . PHE   A 1 168 ? 11.560 -17.828 2.994   1.00 21.13 ?  168 PHE   A HZ   1 
ATOM   3742 N  N    A LEU   A 1 169 ? 7.202  -17.746 -0.257  0.72 26.02 ?  169 LEU   A N    1 
ATOM   3743 N  N    B LEU   A 1 169 ? 7.197  -17.750 -0.260  0.28 25.80 ?  169 LEU   A N    1 
ATOM   3744 C  CA   A LEU   A 1 169 ? 7.010  -19.176 -0.421  0.72 30.27 ?  169 LEU   A CA   1 
ATOM   3745 C  CA   B LEU   A 1 169 ? 7.006  -19.186 -0.400  0.28 28.70 ?  169 LEU   A CA   1 
ATOM   3746 C  C    A LEU   A 1 169 ? 7.893  -19.931 0.562   0.72 31.59 ?  169 LEU   A C    1 
ATOM   3747 C  C    B LEU   A 1 169 ? 7.846  -19.937 0.626   0.28 29.43 ?  169 LEU   A C    1 
ATOM   3748 O  O    A LEU   A 1 169 ? 7.417  -20.377 1.608   0.72 31.96 ?  169 LEU   A O    1 
ATOM   3749 O  O    B LEU   A 1 169 ? 7.308  -20.517 1.571   0.28 29.65 ?  169 LEU   A O    1 
ATOM   3750 C  CB   A LEU   A 1 169 ? 7.311  -19.598 -1.862  0.72 32.35 ?  169 LEU   A CB   1 
ATOM   3751 C  CB   B LEU   A 1 169 ? 7.358  -19.646 -1.817  0.28 30.36 ?  169 LEU   A CB   1 
ATOM   3752 C  CG   A LEU   A 1 169 ? 6.979  -21.050 -2.214  0.72 34.12 ?  169 LEU   A CG   1 
ATOM   3753 C  CG   B LEU   A 1 169 ? 7.046  -21.112 -2.131  0.28 31.72 ?  169 LEU   A CG   1 
ATOM   3754 C  CD1  A LEU   A 1 169 ? 5.551  -21.388 -1.814  0.72 34.74 ?  169 LEU   A CD1  1 
ATOM   3755 C  CD1  B LEU   A 1 169 ? 5.623  -21.458 -1.721  0.28 32.17 ?  169 LEU   A CD1  1 
ATOM   3756 C  CD2  A LEU   A 1 169 ? 7.192  -21.304 -3.699  0.72 34.66 ?  169 LEU   A CD2  1 
ATOM   3757 C  CD2  B LEU   A 1 169 ? 7.260  -21.400 -3.609  0.28 32.15 ?  169 LEU   A CD2  1 
ATOM   3758 O  OXT  A LEU   A 1 169 ? 9.095  -20.099 0.347   0.72 31.64 -1 169 LEU   A OXT  1 
ATOM   3759 O  OXT  B LEU   A 1 169 ? 9.074  -19.975 0.542   0.28 29.42 -1 169 LEU   A OXT  1 
ATOM   3760 H  H    A LEU   A 1 169 ? 7.916  -17.437 -0.631  0.72 31.21 ?  169 LEU   A H    1 
ATOM   3761 H  H    B LEU   A 1 169 ? 7.902  -17.441 -0.651  0.28 30.93 ?  169 LEU   A H    1 
ATOM   3762 H  HA   A LEU   A 1 169 ? 6.088  -19.392 -0.223  0.72 36.30 ?  169 LEU   A HA   1 
ATOM   3763 H  HA   B LEU   A 1 169 ? 6.075  -19.388 -0.234  0.28 34.42 ?  169 LEU   A HA   1 
ATOM   3764 H  HB2  A LEU   A 1 169 ? 6.796  -19.032 -2.460  0.72 38.80 ?  169 LEU   A HB2  1 
ATOM   3765 H  HB2  B LEU   A 1 169 ? 6.861  -19.103 -2.447  0.28 36.41 ?  169 LEU   A HB2  1 
ATOM   3766 H  HB3  A LEU   A 1 169 ? 8.256  -19.469 -2.030  0.72 38.80 ?  169 LEU   A HB3  1 
ATOM   3767 H  HB3  B LEU   A 1 169 ? 8.308  -19.516 -1.955  0.28 36.41 ?  169 LEU   A HB3  1 
ATOM   3768 H  HG   A LEU   A 1 169 ? 7.574  -21.638 -1.724  0.72 40.92 ?  169 LEU   A HG   1 
ATOM   3769 H  HG   B LEU   A 1 169 ? 7.649  -21.679 -1.626  0.28 38.04 ?  169 LEU   A HG   1 
ATOM   3770 H  HD11 A LEU   A 1 169 ? 5.292  -22.218 -2.242  0.72 41.67 ?  169 LEU   A HD11 1 
ATOM   3771 H  HD11 B LEU   A 1 169 ? 5.371  -22.297 -2.133  0.28 38.58 ?  169 LEU   A HD11 1 
ATOM   3772 H  HD12 A LEU   A 1 169 ? 5.507  -21.485 -0.850  0.72 41.67 ?  169 LEU   A HD12 1 
ATOM   3773 H  HD12 B LEU   A 1 169 ? 5.583  -21.539 -0.754  0.28 38.58 ?  169 LEU   A HD12 1 
ATOM   3774 H  HD13 A LEU   A 1 169 ? 4.965  -20.670 -2.103  0.72 41.67 ?  169 LEU   A HD13 1 
ATOM   3775 H  HD13 B LEU   A 1 169 ? 5.029  -20.750 -2.019  0.28 38.58 ?  169 LEU   A HD13 1 
ATOM   3776 H  HD21 A LEU   A 1 169 ? 6.983  -22.231 -3.895  0.72 41.57 ?  169 LEU   A HD21 1 
ATOM   3777 H  HD21 B LEU   A 1 169 ? 7.064  -22.335 -3.781  0.28 38.56 ?  169 LEU   A HD21 1 
ATOM   3778 H  HD22 A LEU   A 1 169 ? 6.606  -20.719 -4.206  0.72 41.57 ?  169 LEU   A HD22 1 
ATOM   3779 H  HD22 B LEU   A 1 169 ? 6.666  -20.837 -4.130  0.28 38.56 ?  169 LEU   A HD22 1 
ATOM   3780 H  HD23 A LEU   A 1 169 ? 8.117  -21.119 -3.922  0.72 41.57 ?  169 LEU   A HD23 1 
ATOM   3781 H  HD23 B LEU   A 1 169 ? 8.183  -21.208 -3.838  0.28 38.56 ?  169 LEU   A HD23 1 
ATOM   3782 N  N    A SER   B 1 1   ? 50.783 -9.258  -23.691 0.72 27.19 ?  1   SER   B N    1 
ATOM   3783 N  N    B SER   B 1 1   ? 50.702 -9.250  -23.652 0.28 26.49 ?  1   SER   B N    1 
ATOM   3784 C  CA   A SER   B 1 1   ? 51.264 -10.300 -22.760 0.72 27.30 ?  1   SER   B CA   1 
ATOM   3785 C  CA   B SER   B 1 1   ? 51.217 -10.260 -22.706 0.28 26.45 ?  1   SER   B CA   1 
ATOM   3786 C  C    A SER   B 1 1   ? 50.187 -11.348 -22.503 0.72 26.47 ?  1   SER   B C    1 
ATOM   3787 C  C    B SER   B 1 1   ? 50.184 -11.352 -22.490 0.28 25.90 ?  1   SER   B C    1 
ATOM   3788 O  O    A SER   B 1 1   ? 48.994 -11.137 -22.763 0.72 26.57 ?  1   SER   B O    1 
ATOM   3789 O  O    B SER   B 1 1   ? 48.996 -11.174 -22.772 0.28 25.88 ?  1   SER   B O    1 
ATOM   3790 C  CB   A SER   B 1 1   ? 51.701 -9.681  -21.436 0.72 28.03 ?  1   SER   B CB   1 
ATOM   3791 C  CB   B SER   B 1 1   ? 51.561 -9.616  -21.368 0.28 26.76 ?  1   SER   B CB   1 
ATOM   3792 O  OG   A SER   B 1 1   ? 50.580 -9.369  -20.631 0.72 29.84 ?  1   SER   B OG   1 
ATOM   3793 O  OG   B SER   B 1 1   ? 50.394 -9.417  -20.592 0.28 27.46 ?  1   SER   B OG   1 
ATOM   3794 H  H1   A SER   B 1 1   ? 50.713 -9.606  -24.505 0.72 32.60 ?  1   SER   B H1   1 
ATOM   3795 H  H1   B SER   B 1 1   ? 50.633 -9.616  -24.458 0.28 31.76 ?  1   SER   B H1   1 
ATOM   3796 H  H2   A SER   B 1 1   ? 49.992 -8.969  -23.416 0.72 32.60 ?  1   SER   B H2   1 
ATOM   3797 H  H2   B SER   B 1 1   ? 49.907 -8.973  -23.376 0.28 31.76 ?  1   SER   B H2   1 
ATOM   3798 H  H3   A SER   B 1 1   ? 51.366 -8.588  -23.699 0.72 32.60 ?  1   SER   B H3   1 
ATOM   3799 H  H3   B SER   B 1 1   ? 51.269 -8.568  -23.679 0.28 31.76 ?  1   SER   B H3   1 
ATOM   3800 H  HA   A SER   B 1 1   ? 52.032 -10.729 -23.166 0.72 32.74 ?  1   SER   B HA   1 
ATOM   3801 H  HA   B SER   B 1 1   ? 52.017 -10.654 -23.080 0.28 31.72 ?  1   SER   B HA   1 
ATOM   3802 H  HB2  A SER   B 1 1   ? 52.258 -10.319 -20.967 0.72 33.62 ?  1   SER   B HB2  1 
ATOM   3803 H  HB2  B SER   B 1 1   ? 52.171 -10.200 -20.893 0.28 32.09 ?  1   SER   B HB2  1 
ATOM   3804 H  HB3  A SER   B 1 1   ? 52.201 -8.869  -21.613 0.72 33.62 ?  1   SER   B HB3  1 
ATOM   3805 H  HB3  B SER   B 1 1   ? 51.978 -8.756  -21.529 0.28 32.09 ?  1   SER   B HB3  1 
ATOM   3806 H  HG   A SER   B 1 1   ? 50.823 -8.894  -19.981 0.72 35.78 ?  1   SER   B HG   1 
ATOM   3807 H  HG   B SER   B 1 1   ? 50.563 -8.898  -19.954 0.28 32.94 ?  1   SER   B HG   1 
ATOM   3808 N  N    A MET   B 1 2   ? 50.631 -12.477 -21.968 0.72 25.88 ?  2   MET   B N    1 
ATOM   3809 N  N    B MET   B 1 2   ? 50.649 -12.482 -21.974 0.28 25.31 ?  2   MET   B N    1 
ATOM   3810 C  CA   A MET   B 1 2   ? 49.810 -13.670 -21.816 0.72 26.07 ?  2   MET   B CA   1 
ATOM   3811 C  CA   B MET   B 1 2   ? 49.825 -13.668 -21.789 0.28 24.86 ?  2   MET   B CA   1 
ATOM   3812 C  C    A MET   B 1 2   ? 49.548 -13.887 -20.332 0.72 24.05 ?  2   MET   B C    1 
ATOM   3813 C  C    B MET   B 1 2   ? 49.560 -13.830 -20.303 0.28 23.30 ?  2   MET   B C    1 
ATOM   3814 O  O    A MET   B 1 2   ? 50.466 -14.221 -19.577 0.72 24.26 ?  2   MET   B O    1 
ATOM   3815 O  O    B MET   B 1 2   ? 50.488 -14.066 -19.522 0.28 23.22 ?  2   MET   B O    1 
ATOM   3816 C  CB   A MET   B 1 2   ? 50.548 -14.859 -22.418 0.72 29.68 ?  2   MET   B CB   1 
ATOM   3817 C  CB   B MET   B 1 2   ? 50.553 -14.878 -22.344 0.28 26.41 ?  2   MET   B CB   1 
ATOM   3818 C  CG   A MET   B 1 2   ? 49.705 -16.107 -22.594 0.72 33.06 ?  2   MET   B CG   1 
ATOM   3819 C  CG   B MET   B 1 2   ? 49.649 -16.020 -22.785 0.28 27.68 ?  2   MET   B CG   1 
ATOM   3820 S  SD   A MET   B 1 2   ? 50.554 -17.315 -23.628 0.72 36.39 ?  2   MET   B SD   1 
ATOM   3821 S  SD   B MET   B 1 2   ? 50.530 -17.144 -23.869 0.28 28.81 ?  2   MET   B SD   1 
ATOM   3822 C  CE   A MET   B 1 2   ? 51.068 -16.256 -24.973 0.72 36.73 ?  2   MET   B CE   1 
ATOM   3823 C  CE   B MET   B 1 2   ? 51.604 -15.989 -24.702 0.28 29.11 ?  2   MET   B CE   1 
ATOM   3824 H  H    A MET   B 1 2   ? 51.438 -12.581 -21.679 0.72 31.03 ?  2   MET   B H    1 
ATOM   3825 H  H    B MET   B 1 2   ? 51.465 -12.595 -21.720 0.28 30.35 ?  2   MET   B H    1 
ATOM   3826 H  HA   A MET   B 1 2   ? 48.974 -13.558 -22.290 0.72 31.26 ?  2   MET   B HA   1 
ATOM   3827 H  HA   B MET   B 1 2   ? 48.994 -13.576 -22.279 0.28 29.81 ?  2   MET   B HA   1 
ATOM   3828 H  HB2  A MET   B 1 2   ? 50.880 -14.573 -23.279 0.72 35.60 ?  2   MET   B HB2  1 
ATOM   3829 H  HB2  B MET   B 1 2   ? 51.041 -14.514 -23.088 0.28 31.67 ?  2   MET   B HB2  1 
ATOM   3830 H  HB3  A MET   B 1 2   ? 51.292 -15.101 -21.849 0.72 35.60 ?  2   MET   B HB3  1 
ATOM   3831 H  HB3  B MET   B 1 2   ? 51.170 -15.243 -21.695 0.28 31.67 ?  2   MET   B HB3  1 
ATOM   3832 H  HG2  A MET   B 1 2   ? 49.536 -16.507 -21.722 0.72 39.64 ?  2   MET   B HG2  1 
ATOM   3833 H  HG2  B MET   B 1 2   ? 49.351 -16.520 -22.003 0.28 33.19 ?  2   MET   B HG2  1 
ATOM   3834 H  HG3  A MET   B 1 2   ? 48.867 -15.879 -23.027 0.72 39.64 ?  2   MET   B HG3  1 
ATOM   3835 H  HG3  B MET   B 1 2   ? 48.886 -15.675 -23.270 0.28 33.19 ?  2   MET   B HG3  1 
ATOM   3836 H  HE1  A MET   B 1 2   ? 51.210 -16.798 -25.751 0.72 44.06 ?  2   MET   B HE1  1 
ATOM   3837 H  HE1  B MET   B 1 2   ? 51.968 -16.444 -25.442 0.28 34.91 ?  2   MET   B HE1  1 
ATOM   3838 H  HE2  A MET   B 1 2   ? 50.364 -15.605 -25.138 0.72 44.06 ?  2   MET   B HE2  1 
ATOM   3839 H  HE2  B MET   B 1 2   ? 51.084 -15.216 -25.001 0.28 34.91 ?  2   MET   B HE2  1 
ATOM   3840 H  HE3  A MET   B 1 2   ? 51.890 -15.794 -24.728 0.72 44.06 ?  2   MET   B HE3  1 
ATOM   3841 H  HE3  B MET   B 1 2   ? 52.325 -15.704 -24.104 0.28 34.91 ?  2   MET   B HE3  1 
ATOM   3842 N  N    . VAL   B 1 3   ? 48.298 -13.689 -19.917 1.00 21.83 ?  3   VAL   B N    1 
ATOM   3843 C  CA   . VAL   B 1 3   ? 47.876 -13.914 -18.544 1.00 20.27 ?  3   VAL   B CA   1 
ATOM   3844 C  C    . VAL   B 1 3   ? 46.637 -14.797 -18.567 1.00 18.57 ?  3   VAL   B C    1 
ATOM   3845 O  O    . VAL   B 1 3   ? 45.903 -14.861 -19.556 1.00 19.49 ?  3   VAL   B O    1 
ATOM   3846 C  CB   . VAL   B 1 3   ? 47.598 -12.600 -17.782 1.00 21.81 ?  3   VAL   B CB   1 
ATOM   3847 C  CG1  . VAL   B 1 3   ? 48.876 -11.763 -17.653 1.00 22.40 ?  3   VAL   B CG1  1 
ATOM   3848 C  CG2  . VAL   B 1 3   ? 46.494 -11.813 -18.468 1.00 22.38 ?  3   VAL   B CG2  1 
ATOM   3849 H  H    A VAL   B 1 3   ? 47.664 -13.430 -20.437 0.72 26.17 ?  3   VAL   B H    1 
ATOM   3850 H  H    B VAL   B 1 3   ? 47.662 -13.453 -20.445 0.28 26.17 ?  3   VAL   B H    1 
ATOM   3851 H  HA   . VAL   B 1 3   ? 48.575 -14.392 -18.072 1.00 24.31 ?  3   VAL   B HA   1 
ATOM   3852 H  HB   . VAL   B 1 3   ? 47.297 -12.822 -16.887 1.00 26.15 ?  3   VAL   B HB   1 
ATOM   3853 H  HG11 . VAL   B 1 3   ? 48.670 -10.951 -17.164 1.00 26.85 ?  3   VAL   B HG11 1 
ATOM   3854 H  HG12 . VAL   B 1 3   ? 49.543 -12.278 -17.172 1.00 26.85 ?  3   VAL   B HG12 1 
ATOM   3855 H  HG13 . VAL   B 1 3   ? 49.200 -11.545 -18.539 1.00 26.85 ?  3   VAL   B HG13 1 
ATOM   3856 H  HG21 . VAL   B 1 3   ? 46.429 -10.940 -18.056 1.00 26.84 ?  3   VAL   B HG21 1 
ATOM   3857 H  HG22 . VAL   B 1 3   ? 46.707 -11.722 -19.409 1.00 26.84 ?  3   VAL   B HG22 1 
ATOM   3858 H  HG23 . VAL   B 1 3   ? 45.654 -12.291 -18.365 1.00 26.84 ?  3   VAL   B HG23 1 
ATOM   3859 N  N    . ASN   B 1 4   ? 46.418 -15.494 -17.457 1.00 16.40 ?  4   ASN   B N    1 
ATOM   3860 C  CA   . ASN   B 1 4   ? 45.279 -16.400 -17.336 1.00 15.73 ?  4   ASN   B CA   1 
ATOM   3861 C  C    . ASN   B 1 4   ? 45.220 -17.365 -18.516 1.00 15.92 ?  4   ASN   B C    1 
ATOM   3862 O  O    . ASN   B 1 4   ? 44.161 -17.612 -19.088 1.00 16.49 ?  4   ASN   B O    1 
ATOM   3863 C  CB   . ASN   B 1 4   ? 43.965 -15.626 -17.187 1.00 15.25 ?  4   ASN   B CB   1 
ATOM   3864 C  CG   . ASN   B 1 4   ? 43.915 -14.820 -15.907 1.00 14.55 ?  4   ASN   B CG   1 
ATOM   3865 O  OD1  . ASN   B 1 4   ? 44.195 -15.335 -14.826 1.00 14.50 ?  4   ASN   B OD1  1 
ATOM   3866 N  ND2  . ASN   B 1 4   ? 43.579 -13.544 -16.023 1.00 15.29 ?  4   ASN   B ND2  1 
ATOM   3867 H  H    . ASN   B 1 4   ? 46.923 -15.472 -16.762 1.00 19.66 ?  4   ASN   B H    1 
ATOM   3868 H  HA   . ASN   B 1 4   ? 45.397 -16.935 -16.536 1.00 18.85 ?  4   ASN   B HA   1 
ATOM   3869 H  HB2  . ASN   B 1 4   ? 43.870 -15.015 -17.934 1.00 18.27 ?  4   ASN   B HB2  1 
ATOM   3870 H  HB3  . ASN   B 1 4   ? 43.225 -16.256 -17.179 1.00 18.27 ?  4   ASN   B HB3  1 
ATOM   3871 H  HD21 . ASN   B 1 4   ? 43.542 -13.043 -15.323 1.00 18.32 ?  4   ASN   B HD21 1 
ATOM   3872 H  HD22 . ASN   B 1 4   ? 43.397 -13.212 -16.796 1.00 18.32 ?  4   ASN   B HD22 1 
ATOM   3873 N  N    . SER   B 1 5   ? 46.375 -17.915 -18.886 1.00 16.91 ?  5   SER   B N    1 
ATOM   3874 C  CA   . SER   B 1 5   ? 46.472 -18.827 -20.025 1.00 19.27 ?  5   SER   B CA   1 
ATOM   3875 C  C    . SER   B 1 5   ? 46.454 -20.263 -19.510 1.00 20.94 ?  5   SER   B C    1 
ATOM   3876 O  O    . SER   B 1 5   ? 47.462 -20.961 -19.477 1.00 23.20 ?  5   SER   B O    1 
ATOM   3877 C  CB   . SER   B 1 5   ? 47.728 -18.530 -20.840 1.00 20.40 ?  5   SER   B CB   1 
ATOM   3878 O  OG   . SER   B 1 5   ? 48.898 -18.694 -20.056 1.00 22.86 ?  5   SER   B OG   1 
ATOM   3879 H  H    . SER   B 1 5   ? 47.125 -17.787 -18.486 1.00 20.27 ?  5   SER   B H    1 
ATOM   3880 H  HA   . SER   B 1 5   ? 45.705 -18.708 -20.601 1.00 23.11 ?  5   SER   B HA   1 
ATOM   3881 H  HB2  . SER   B 1 5   ? 47.762 -19.133 -21.602 1.00 24.45 ?  5   SER   B HB2  1 
ATOM   3882 H  HB3  . SER   B 1 5   ? 47.676 -17.613 -21.152 1.00 24.45 ?  5   SER   B HB3  1 
ATOM   3883 H  HG   . SER   B 1 5   ? 48.967 -19.490 -19.800 1.00 27.41 ?  5   SER   B HG   1 
ATOM   3884 N  N    . PHE   B 1 6   ? 45.269 -20.675 -19.072 1.00 21.47 ?  6   PHE   B N    1 
ATOM   3885 C  CA   . PHE   B 1 6   ? 45.064 -22.021 -18.559 1.00 21.33 ?  6   PHE   B CA   1 
ATOM   3886 C  C    . PHE   B 1 6   ? 44.974 -22.994 -19.724 1.00 24.83 ?  6   PHE   B C    1 
ATOM   3887 O  O    . PHE   B 1 6   ? 44.288 -22.722 -20.713 1.00 26.76 ?  6   PHE   B O    1 
ATOM   3888 C  CB   . PHE   B 1 6   ? 43.777 -22.069 -17.738 1.00 19.29 ?  6   PHE   B CB   1 
ATOM   3889 C  CG   . PHE   B 1 6   ? 43.807 -21.205 -16.510 1.00 17.46 ?  6   PHE   B CG   1 
ATOM   3890 C  CD1  . PHE   B 1 6   ? 44.312 -21.696 -15.320 1.00 16.47 ?  6   PHE   B CD1  1 
ATOM   3891 C  CD2  . PHE   B 1 6   ? 43.327 -19.904 -16.545 1.00 16.69 ?  6   PHE   B CD2  1 
ATOM   3892 C  CE1  . PHE   B 1 6   ? 44.335 -20.908 -14.181 1.00 15.77 ?  6   PHE   B CE1  1 
ATOM   3893 C  CE2  . PHE   B 1 6   ? 43.356 -19.106 -15.415 1.00 16.98 ?  6   PHE   B CE2  1 
ATOM   3894 C  CZ   . PHE   B 1 6   ? 43.863 -19.603 -14.234 1.00 16.30 ?  6   PHE   B CZ   1 
ATOM   3895 H  H    . PHE   B 1 6   ? 44.559 -20.191 -19.062 1.00 25.74 ?  6   PHE   B H    1 
ATOM   3896 H  HA   . PHE   B 1 6   ? 45.806 -22.279 -17.993 1.00 25.58 ?  6   PHE   B HA   1 
ATOM   3897 H  HB2  . PHE   B 1 6   ? 43.039 -21.771 -18.295 1.00 23.13 ?  6   PHE   B HB2  1 
ATOM   3898 H  HB3  . PHE   B 1 6   ? 43.619 -22.985 -17.454 1.00 23.13 ?  6   PHE   B HB3  1 
ATOM   3899 H  HD1  . PHE   B 1 6   ? 44.639 -22.565 -15.283 1.00 19.74 ?  6   PHE   B HD1  1 
ATOM   3900 H  HD2  . PHE   B 1 6   ? 42.981 -19.565 -17.338 1.00 20.00 ?  6   PHE   B HD2  1 
ATOM   3901 H  HE1  . PHE   B 1 6   ? 44.689 -21.243 -13.388 1.00 18.90 ?  6   PHE   B HE1  1 
ATOM   3902 H  HE2  . PHE   B 1 6   ? 43.027 -18.236 -15.451 1.00 20.36 ?  6   PHE   B HE2  1 
ATOM   3903 H  HZ   . PHE   B 1 6   ? 43.880 -19.072 -13.471 1.00 19.54 ?  6   PHE   B HZ   1 
ATOM   3904 N  N    . SER   B 1 7   ? 45.683 -24.117 -19.614 1.00 26.05 ?  7   SER   B N    1 
ATOM   3905 C  CA   . SER   B 1 7   ? 45.749 -25.095 -20.689 1.00 28.85 ?  7   SER   B CA   1 
ATOM   3906 C  C    . SER   B 1 7   ? 45.689 -26.502 -20.115 1.00 27.85 ?  7   SER   B C    1 
ATOM   3907 O  O    . SER   B 1 7   ? 46.301 -26.791 -19.082 1.00 28.49 ?  7   SER   B O    1 
ATOM   3908 C  CB   . SER   B 1 7   ? 47.039 -24.926 -21.502 1.00 31.93 ?  7   SER   B CB   1 
ATOM   3909 O  OG   . SER   B 1 7   ? 46.985 -25.676 -22.704 1.00 33.49 ?  7   SER   B OG   1 
ATOM   3910 H  H    . SER   B 1 7   ? 46.146 -24.330 -18.917 1.00 31.24 ?  7   SER   B H    1 
ATOM   3911 H  HA   . SER   B 1 7   ? 44.995 -24.976 -21.283 1.00 34.60 ?  7   SER   B HA   1 
ATOM   3912 H  HB2  . SER   B 1 7   ? 47.154 -23.986 -21.719 1.00 38.29 ?  7   SER   B HB2  1 
ATOM   3913 H  HB3  . SER   B 1 7   ? 47.791 -25.236 -20.972 1.00 38.29 ?  7   SER   B HB3  1 
ATOM   3914 H  HG   . SER   B 1 7   ? 47.696 -25.570 -23.141 1.00 40.17 ?  7   SER   B HG   1 
ATOM   3915 N  N    . GLY   B 1 8   ? 44.950 -27.375 -20.796 1.00 27.39 ?  8   GLY   B N    1 
ATOM   3916 C  CA   . GLY   B 1 8   ? 44.900 -28.770 -20.422 1.00 26.35 ?  8   GLY   B CA   1 
ATOM   3917 C  C    . GLY   B 1 8   ? 43.974 -29.097 -19.279 1.00 24.75 ?  8   GLY   B C    1 
ATOM   3918 O  O    . GLY   B 1 8   ? 44.124 -30.161 -18.665 1.00 26.06 ?  8   GLY   B O    1 
ATOM   3919 H  H    . GLY   B 1 8   ? 44.471 -27.172 -21.478 1.00 32.84 ?  8   GLY   B H    1 
ATOM   3920 H  HA2  . GLY   B 1 8   ? 44.613 -29.289 -21.186 1.00 31.60 ?  8   GLY   B HA2  1 
ATOM   3921 H  HA3  . GLY   B 1 8   ? 45.788 -29.062 -20.172 1.00 31.60 ?  8   GLY   B HA3  1 
ATOM   3922 N  N    . TYR   B 1 9   ? 43.002 -28.237 -18.983 1.00 22.83 ?  9   TYR   B N    1 
ATOM   3923 C  CA   . TYR   B 1 9   ? 42.060 -28.513 -17.911 1.00 20.86 ?  9   TYR   B CA   1 
ATOM   3924 C  C    . TYR   B 1 9   ? 40.876 -29.313 -18.420 1.00 20.38 ?  9   TYR   B C    1 
ATOM   3925 O  O    . TYR   B 1 9   ? 40.451 -29.182 -19.572 1.00 22.05 ?  9   TYR   B O    1 
ATOM   3926 C  CB   . TYR   B 1 9   ? 41.552 -27.226 -17.266 1.00 19.98 ?  9   TYR   B CB   1 
ATOM   3927 C  CG   . TYR   B 1 9   ? 42.581 -26.600 -16.358 1.00 19.30 ?  9   TYR   B CG   1 
ATOM   3928 C  CD1  . TYR   B 1 9   ? 43.666 -25.917 -16.882 1.00 19.62 ?  9   TYR   B CD1  1 
ATOM   3929 C  CD2  . TYR   B 1 9   ? 42.484 -26.715 -14.978 1.00 18.58 ?  9   TYR   B CD2  1 
ATOM   3930 C  CE1  . TYR   B 1 9   ? 44.623 -25.358 -16.061 1.00 19.68 ?  9   TYR   B CE1  1 
ATOM   3931 C  CE2  . TYR   B 1 9   ? 43.438 -26.154 -14.145 1.00 18.59 ?  9   TYR   B CE2  1 
ATOM   3932 C  CZ   . TYR   B 1 9   ? 44.507 -25.475 -14.695 1.00 19.37 ?  9   TYR   B CZ   1 
ATOM   3933 O  OH   . TYR   B 1 9   ? 45.463 -24.924 -13.878 1.00 19.97 ?  9   TYR   B OH   1 
ATOM   3934 H  H    . TYR   B 1 9   ? 42.853 -27.498 -19.398 1.00 27.37 ?  9   TYR   B H    1 
ATOM   3935 H  HA   . TYR   B 1 9   ? 42.497 -29.034 -17.224 1.00 25.00 ?  9   TYR   B HA   1 
ATOM   3936 H  HB2  . TYR   B 1 9   ? 41.319 -26.581 -17.955 1.00 23.96 ?  9   TYR   B HB2  1 
ATOM   3937 H  HB3  . TYR   B 1 9   ? 40.775 -27.440 -16.732 1.00 23.96 ?  9   TYR   B HB3  1 
ATOM   3938 H  HD1  . TYR   B 1 9   ? 43.745 -25.835 -17.805 1.00 23.53 ?  9   TYR   B HD1  1 
ATOM   3939 H  HD2  . TYR   B 1 9   ? 41.759 -27.176 -14.607 1.00 22.28 ?  9   TYR   B HD2  1 
ATOM   3940 H  HE1  . TYR   B 1 9   ? 45.336 -24.902 -16.430 1.00 23.60 ?  9   TYR   B HE1  1 
ATOM   3941 H  HE2  . TYR   B 1 9   ? 43.351 -26.243 -13.222 1.00 22.29 ?  9   TYR   B HE2  1 
ATOM   3942 H  HH   . TYR   B 1 9   ? 46.042 -24.542 -14.344 1.00 23.94 ?  9   TYR   B HH   1 
ATOM   3943 N  N    . LEU   B 1 10  ? 40.356 -30.159 -17.540 1.00 18.77 ?  10  LEU   B N    1 
ATOM   3944 C  CA   . LEU   B 1 10  ? 39.150 -30.921 -17.801 1.00 18.46 ?  10  LEU   B CA   1 
ATOM   3945 C  C    . LEU   B 1 10  ? 37.966 -30.150 -17.237 1.00 17.96 ?  10  LEU   B C    1 
ATOM   3946 O  O    . LEU   B 1 10  ? 37.986 -29.727 -16.077 1.00 17.70 ?  10  LEU   B O    1 
ATOM   3947 C  CB   . LEU   B 1 10  ? 39.256 -32.288 -17.127 1.00 19.36 ?  10  LEU   B CB   1 
ATOM   3948 C  CG   . LEU   B 1 10  ? 38.121 -33.255 -17.440 1.00 21.09 ?  10  LEU   B CG   1 
ATOM   3949 C  CD1  . LEU   B 1 10  ? 38.216 -33.742 -18.879 1.00 22.17 ?  10  LEU   B CD1  1 
ATOM   3950 C  CD2  . LEU   B 1 10  ? 38.127 -34.422 -16.469 1.00 22.08 ?  10  LEU   B CD2  1 
ATOM   3951 H  H    . LEU   B 1 10  ? 40.688 -30.304 -16.757 1.00 22.50 ?  10  LEU   B H    1 
ATOM   3952 H  HA   . LEU   B 1 10  ? 39.027 -31.042 -18.752 1.00 22.13 ?  10  LEU   B HA   1 
ATOM   3953 H  HB2  . LEU   B 1 10  ? 40.082 -32.707 -17.411 1.00 23.21 ?  10  LEU   B HB2  1 
ATOM   3954 H  HB3  . LEU   B 1 10  ? 39.271 -32.160 -16.165 1.00 23.21 ?  10  LEU   B HB3  1 
ATOM   3955 H  HG   . LEU   B 1 10  ? 37.275 -32.791 -17.339 1.00 25.29 ?  10  LEU   B HG   1 
ATOM   3956 H  HD11 . LEU   B 1 10  ? 37.527 -34.406 -19.031 1.00 26.59 ?  10  LEU   B HD11 1 
ATOM   3957 H  HD12 . LEU   B 1 10  ? 38.084 -32.986 -19.475 1.00 26.59 ?  10  LEU   B HD12 1 
ATOM   3958 H  HD13 . LEU   B 1 10  ? 39.091 -34.129 -19.023 1.00 26.59 ?  10  LEU   B HD13 1 
ATOM   3959 H  HD21 . LEU   B 1 10  ? 37.400 -35.020 -16.696 1.00 26.48 ?  10  LEU   B HD21 1 
ATOM   3960 H  HD22 . LEU   B 1 10  ? 38.975 -34.883 -16.542 1.00 26.48 ?  10  LEU   B HD22 1 
ATOM   3961 H  HD23 . LEU   B 1 10  ? 38.009 -34.078 -15.570 1.00 26.48 ?  10  LEU   B HD23 1 
ATOM   3962 N  N    . LYS   B 1 11  ? 36.942 -29.967 -18.062 1.00 19.05 ?  11  LYS   B N    1 
ATOM   3963 C  CA   . LYS   B 1 11  ? 35.743 -29.253 -17.651 1.00 21.33 ?  11  LYS   B CA   1 
ATOM   3964 C  C    . LYS   B 1 11  ? 34.880 -30.181 -16.805 1.00 20.31 ?  11  LYS   B C    1 
ATOM   3965 O  O    . LYS   B 1 11  ? 34.513 -31.274 -17.252 1.00 21.92 ?  11  LYS   B O    1 
ATOM   3966 C  CB   . LYS   B 1 11  ? 34.985 -28.799 -18.899 1.00 25.36 ?  11  LYS   B CB   1 
ATOM   3967 C  CG   . LYS   B 1 11  ? 33.816 -27.863 -18.648 1.00 28.82 ?  11  LYS   B CG   1 
ATOM   3968 C  CD   . LYS   B 1 11  ? 33.071 -27.580 -19.947 1.00 31.59 ?  11  LYS   B CD   1 
ATOM   3969 C  CE   . LYS   B 1 11  ? 32.057 -26.462 -19.784 1.00 33.58 ?  11  LYS   B CE   1 
ATOM   3970 N  NZ   . LYS   B 1 11  ? 32.714 -25.149 -19.551 1.00 34.64 ?  11  LYS   B NZ   1 
ATOM   3971 H  H    . LYS   B 1 11  ? 36.909 -30.263 -18.870 1.00 22.83 ?  11  LYS   B H    1 
ATOM   3972 H  HA   . LYS   B 1 11  ? 35.983 -28.475 -17.126 1.00 25.57 ?  11  LYS   B HA   1 
ATOM   3973 H  HB2  . LYS   B 1 11  ? 35.606 -28.333 -19.483 1.00 30.41 ?  11  LYS   B HB2  1 
ATOM   3974 H  HB3  . LYS   B 1 11  ? 34.638 -29.580 -19.354 1.00 30.41 ?  11  LYS   B HB3  1 
ATOM   3975 H  HG2  . LYS   B 1 11  ? 33.198 -28.276 -18.026 1.00 34.56 ?  11  LYS   B HG2  1 
ATOM   3976 H  HG3  . LYS   B 1 11  ? 34.144 -27.022 -18.294 1.00 34.56 ?  11  LYS   B HG3  1 
ATOM   3977 H  HD2  . LYS   B 1 11  ? 33.708 -27.313 -20.630 1.00 37.89 ?  11  LYS   B HD2  1 
ATOM   3978 H  HD3  . LYS   B 1 11  ? 32.599 -28.380 -20.227 1.00 37.89 ?  11  LYS   B HD3  1 
ATOM   3979 H  HE2  . LYS   B 1 11  ? 31.522 -26.396 -20.591 1.00 40.27 ?  11  LYS   B HE2  1 
ATOM   3980 H  HE3  . LYS   B 1 11  ? 31.489 -26.661 -19.023 1.00 40.27 ?  11  LYS   B HE3  1 
ATOM   3981 H  HZ1  . LYS   B 1 11  ? 32.100 -24.508 -19.495 1.00 41.55 ?  11  LYS   B HZ1  1 
ATOM   3982 H  HZ2  . LYS   B 1 11  ? 33.180 -25.171 -18.794 1.00 41.55 ?  11  LYS   B HZ2  1 
ATOM   3983 H  HZ3  . LYS   B 1 11  ? 33.265 -24.962 -20.225 1.00 41.55 ?  11  LYS   B HZ3  1 
ATOM   3984 N  N    . LEU   B 1 12  ? 34.560 -29.756 -15.582 1.00 18.37 ?  12  LEU   B N    1 
ATOM   3985 C  CA   . LEU   B 1 12  ? 33.604 -30.461 -14.736 1.00 17.80 ?  12  LEU   B CA   1 
ATOM   3986 C  C    . LEU   B 1 12  ? 32.215 -29.852 -14.825 1.00 17.63 ?  12  LEU   B C    1 
ATOM   3987 O  O    . LEU   B 1 12  ? 31.229 -30.568 -14.999 1.00 18.12 ?  12  LEU   B O    1 
ATOM   3988 C  CB   . LEU   B 1 12  ? 34.069 -30.482 -13.274 1.00 17.16 ?  12  LEU   B CB   1 
ATOM   3989 C  CG   . LEU   B 1 12  ? 35.408 -31.163 -12.998 1.00 17.01 ?  12  LEU   B CG   1 
ATOM   3990 C  CD1  . LEU   B 1 12  ? 35.761 -31.107 -11.521 1.00 17.33 ?  12  LEU   B CD1  1 
ATOM   3991 C  CD2  . LEU   B 1 12  ? 35.403 -32.603 -13.492 1.00 17.55 ?  12  LEU   B CD2  1 
ATOM   3992 H  H    . LEU   B 1 12  ? 34.889 -29.047 -15.215 1.00 22.02 ?  12  LEU   B H    1 
ATOM   3993 H  HA   . LEU   B 1 12  ? 33.532 -31.375 -15.040 1.00 21.34 ?  12  LEU   B HA   1 
ATOM   3994 H  HB2  . LEU   B 1 12  ? 34.139 -29.569 -12.963 1.00 20.57 ?  12  LEU   B HB2  1 
ATOM   3995 H  HB3  . LEU   B 1 12  ? 33.395 -30.950 -12.751 1.00 20.57 ?  12  LEU   B HB3  1 
ATOM   3996 H  HG   . LEU   B 1 12  ? 36.099 -30.691 -13.484 1.00 20.40 ?  12  LEU   B HG   1 
ATOM   3997 H  HD11 . LEU   B 1 12  ? 36.620 -31.545 -11.385 1.00 20.78 ?  12  LEU   B HD11 1 
ATOM   3998 H  HD12 . LEU   B 1 12  ? 35.821 -30.180 -11.244 1.00 20.78 ?  12  LEU   B HD12 1 
ATOM   3999 H  HD13 . LEU   B 1 12  ? 35.076 -31.564 -11.010 1.00 20.78 ?  12  LEU   B HD13 1 
ATOM   4000 H  HD21 . LEU   B 1 12  ? 36.211 -33.044 -13.189 1.00 21.04 ?  12  LEU   B HD21 1 
ATOM   4001 H  HD22 . LEU   B 1 12  ? 34.624 -33.058 -13.133 1.00 21.04 ?  12  LEU   B HD22 1 
ATOM   4002 H  HD23 . LEU   B 1 12  ? 35.368 -32.605 -14.461 1.00 21.04 ?  12  LEU   B HD23 1 
ATOM   4003 N  N    . THR   B 1 13  ? 32.126 -28.534 -14.706 1.00 17.48 ?  13  THR   B N    1 
ATOM   4004 C  CA   . THR   B 1 13  ? 30.901 -27.786 -14.914 1.00 17.71 ?  13  THR   B CA   1 
ATOM   4005 C  C    . THR   B 1 13  ? 31.236 -26.592 -15.801 1.00 19.84 ?  13  THR   B C    1 
ATOM   4006 O  O    . THR   B 1 13  ? 32.383 -26.405 -16.223 1.00 20.81 ?  13  THR   B O    1 
ATOM   4007 C  CB   . THR   B 1 13  ? 30.304 -27.304 -13.588 1.00 17.24 ?  13  THR   B CB   1 
ATOM   4008 O  OG1  . THR   B 1 13  ? 31.151 -26.289 -13.040 1.00 16.98 ?  13  THR   B OG1  1 
ATOM   4009 C  CG2  . THR   B 1 13  ? 30.182 -28.455 -12.592 1.00 17.67 ?  13  THR   B CG2  1 
ATOM   4010 H  H    . THR   B 1 13  ? 32.792 -28.030 -14.494 1.00 20.96 ?  13  THR   B H    1 
ATOM   4011 H  HA   . THR   B 1 13  ? 30.245 -28.343 -15.361 1.00 21.23 ?  13  THR   B HA   1 
ATOM   4012 H  HB   . THR   B 1 13  ? 29.419 -26.935 -13.745 1.00 20.66 ?  13  THR   B HB   1 
ATOM   4013 H  HG1  . THR   B 1 13  ? 30.851 -25.524 -13.237 1.00 20.35 ?  13  THR   B HG1  1 
ATOM   4014 H  HG21 . THR   B 1 13  ? 29.679 -28.170 -11.813 1.00 21.18 ?  13  THR   B HG21 1 
ATOM   4015 H  HG22 . THR   B 1 13  ? 29.723 -29.203 -13.005 1.00 21.18 ?  13  THR   B HG22 1 
ATOM   4016 H  HG23 . THR   B 1 13  ? 31.063 -28.746 -12.308 1.00 21.18 ?  13  THR   B HG23 1 
ATOM   4017 N  N    A ASP   B 1 14  ? 30.227 -25.763 -16.069 0.72 20.76 ?  14  ASP   B N    1 
ATOM   4018 N  N    B ASP   B 1 14  ? 30.229 -25.755 -16.061 0.28 20.50 ?  14  ASP   B N    1 
ATOM   4019 C  CA   A ASP   B 1 14  ? 30.447 -24.610 -16.934 0.72 22.26 ?  14  ASP   B CA   1 
ATOM   4020 C  CA   B ASP   B 1 14  ? 30.432 -24.605 -16.935 0.28 21.31 ?  14  ASP   B CA   1 
ATOM   4021 C  C    A ASP   B 1 14  ? 31.545 -23.699 -16.400 0.72 20.39 ?  14  ASP   B C    1 
ATOM   4022 C  C    B ASP   B 1 14  ? 31.422 -23.598 -16.372 0.28 19.67 ?  14  ASP   B C    1 
ATOM   4023 O  O    A ASP   B 1 14  ? 32.211 -23.013 -17.186 0.72 21.47 ?  14  ASP   B O    1 
ATOM   4024 O  O    B ASP   B 1 14  ? 31.861 -22.713 -17.116 0.28 19.82 ?  14  ASP   B O    1 
ATOM   4025 C  CB   A ASP   B 1 14  ? 29.146 -23.829 -17.115 0.72 25.84 ?  14  ASP   B CB   1 
ATOM   4026 C  CB   B ASP   B 1 14  ? 29.108 -23.892 -17.207 0.28 23.74 ?  14  ASP   B CB   1 
ATOM   4027 C  CG   A ASP   B 1 14  ? 28.176 -24.518 -18.052 0.72 29.42 ?  14  ASP   B CG   1 
ATOM   4028 C  CG   B ASP   B 1 14  ? 28.236 -24.640 -18.197 0.28 25.90 ?  14  ASP   B CG   1 
ATOM   4029 O  OD1  A ASP   B 1 14  ? 28.568 -25.493 -18.733 0.72 30.68 ?  14  ASP   B OD1  1 
ATOM   4030 O  OD1  B ASP   B 1 14  ? 28.792 -25.315 -19.090 0.28 26.70 ?  14  ASP   B OD1  1 
ATOM   4031 O  OD2  A ASP   B 1 14  ? 27.006 -24.087 -18.101 0.72 30.73 -1 14  ASP   B OD2  1 
ATOM   4032 O  OD2  B ASP   B 1 14  ? 26.996 -24.557 -18.084 0.28 26.54 -1 14  ASP   B OD2  1 
ATOM   4033 H  H    A ASP   B 1 14  ? 29.427 -25.837 -15.760 0.72 24.89 ?  14  ASP   B H    1 
ATOM   4034 H  H    B ASP   B 1 14  ? 29.433 -25.822 -15.738 0.28 24.58 ?  14  ASP   B H    1 
ATOM   4035 H  HA   A ASP   B 1 14  ? 30.729 -24.920 -17.805 0.72 26.69 ?  14  ASP   B HA   1 
ATOM   4036 H  HA   B ASP   B 1 14  ? 30.777 -24.922 -17.783 0.28 25.55 ?  14  ASP   B HA   1 
ATOM   4037 H  HB2  A ASP   B 1 14  ? 28.699 -23.741 -16.261 0.72 30.98 ?  14  ASP   B HB2  1 
ATOM   4038 H  HB2  B ASP   B 1 14  ? 28.617 -23.810 -16.376 0.28 28.47 ?  14  ASP   B HB2  1 
ATOM   4039 H  HB3  A ASP   B 1 14  ? 29.343 -22.954 -17.483 0.72 30.98 ?  14  ASP   B HB3  1 
ATOM   4040 H  HB3  B ASP   B 1 14  ? 29.298 -23.007 -17.567 0.28 28.47 ?  14  ASP   B HB3  1 
ATOM   4041 N  N    . ASN   B 1 15  ? 31.762 -23.686 -15.083 1.00 18.12 ?  15  ASN   B N    1 
ATOM   4042 C  CA   . ASN   B 1 15  ? 32.723 -22.766 -14.482 1.00 15.60 ?  15  ASN   B CA   1 
ATOM   4043 C  C    . ASN   B 1 15  ? 33.814 -23.423 -13.648 1.00 14.30 ?  15  ASN   B C    1 
ATOM   4044 O  O    . ASN   B 1 15  ? 34.668 -22.700 -13.126 1.00 14.48 ?  15  ASN   B O    1 
ATOM   4045 C  CB   . ASN   B 1 15  ? 32.008 -21.715 -13.617 1.00 15.73 ?  15  ASN   B CB   1 
ATOM   4046 C  CG   . ASN   B 1 15  ? 31.395 -22.316 -12.371 1.00 15.32 ?  15  ASN   B CG   1 
ATOM   4047 O  OD1  . ASN   B 1 15  ? 30.453 -23.111 -12.458 1.00 16.89 ?  15  ASN   B OD1  1 
ATOM   4048 N  ND2  . ASN   B 1 15  ? 31.926 -21.964 -11.211 1.00 14.38 ?  15  ASN   B ND2  1 
ATOM   4049 H  H    A ASN   B 1 15  ? 31.365 -24.203 -14.519 0.72 21.73 ?  15  ASN   B H    1 
ATOM   4050 H  H    B ASN   B 1 15  ? 31.421 -24.253 -14.531 0.28 21.73 ?  15  ASN   B H    1 
ATOM   4051 H  HA   . ASN   B 1 15  ? 33.170 -22.285 -15.185 1.00 18.70 ?  15  ASN   B HA   1 
ATOM   4052 H  HB2  . ASN   B 1 15  ? 32.653 -21.037 -13.342 1.00 18.85 ?  15  ASN   B HB2  1 
ATOM   4053 H  HB3  . ASN   B 1 15  ? 31.297 -21.300 -14.131 1.00 18.85 ?  15  ASN   B HB3  1 
ATOM   4054 H  HD21 . ASN   B 1 15  ? 31.614 -22.278 -10.472 1.00 17.24 ?  15  ASN   B HD21 1 
ATOM   4055 H  HD22 . ASN   B 1 15  ? 32.595 -21.412 -11.184 1.00 17.24 ?  15  ASN   B HD22 1 
ATOM   4056 N  N    . VAL   B 1 16  ? 33.818 -24.746 -13.493 1.00 14.07 ?  16  VAL   B N    1 
ATOM   4057 C  CA   . VAL   B 1 16  ? 34.815 -25.440 -12.681 1.00 13.81 ?  16  VAL   B CA   1 
ATOM   4058 C  C    . VAL   B 1 16  ? 35.610 -26.377 -13.574 1.00 13.92 ?  16  VAL   B C    1 
ATOM   4059 O  O    . VAL   B 1 16  ? 35.036 -27.259 -14.234 1.00 14.98 ?  16  VAL   B O    1 
ATOM   4060 C  CB   . VAL   B 1 16  ? 34.191 -26.207 -11.506 1.00 14.20 ?  16  VAL   B CB   1 
ATOM   4061 C  CG1  . VAL   B 1 16  ? 35.282 -26.941 -10.722 1.00 13.98 ?  16  VAL   B CG1  1 
ATOM   4062 C  CG2  . VAL   B 1 16  ? 33.400 -25.256 -10.606 1.00 14.95 ?  16  VAL   B CG2  1 
ATOM   4063 H  H    . VAL   B 1 16  ? 33.234 -25.277 -13.849 1.00 16.87 ?  16  VAL   B H    1 
ATOM   4064 H  HA   . VAL   B 1 16  ? 35.426 -24.789 -12.310 1.00 16.55 ?  16  VAL   B HA   1 
ATOM   4065 H  HB   . VAL   B 1 16  ? 33.575 -26.874 -11.851 1.00 17.02 ?  16  VAL   B HB   1 
ATOM   4066 H  HG11 . VAL   B 1 16  ? 34.919 -27.228 -9.869  1.00 16.75 ?  16  VAL   B HG11 1 
ATOM   4067 H  HG12 . VAL   B 1 16  ? 35.579 -27.711 -11.230 1.00 16.75 ?  16  VAL   B HG12 1 
ATOM   4068 H  HG13 . VAL   B 1 16  ? 36.025 -26.333 -10.574 1.00 16.75 ?  16  VAL   B HG13 1 
ATOM   4069 H  HG21 . VAL   B 1 16  ? 33.060 -25.751 -9.843  1.00 17.92 ?  16  VAL   B HG21 1 
ATOM   4070 H  HG22 . VAL   B 1 16  ? 33.984 -24.545 -10.306 1.00 17.92 ?  16  VAL   B HG22 1 
ATOM   4071 H  HG23 . VAL   B 1 16  ? 32.659 -24.886 -11.113 1.00 17.92 ?  16  VAL   B HG23 1 
ATOM   4072 N  N    . TYR   B 1 17  ? 36.931 -26.208 -13.551 1.00 14.33 ?  17  TYR   B N    1 
ATOM   4073 C  CA   . TYR   B 1 17  ? 37.876 -26.956 -14.365 1.00 14.68 ?  17  TYR   B CA   1 
ATOM   4074 C  C    . TYR   B 1 17  ? 38.927 -27.570 -13.451 1.00 13.84 ?  17  TYR   B C    1 
ATOM   4075 O  O    . TYR   B 1 17  ? 39.208 -27.041 -12.373 1.00 14.16 ?  17  TYR   B O    1 
ATOM   4076 C  CB   . TYR   B 1 17  ? 38.580 -26.024 -15.358 1.00 17.47 ?  17  TYR   B CB   1 
ATOM   4077 C  CG   . TYR   B 1 17  ? 37.653 -25.258 -16.269 1.00 20.78 ?  17  TYR   B CG   1 
ATOM   4078 C  CD1  . TYR   B 1 17  ? 37.062 -24.070 -15.858 1.00 22.63 ?  17  TYR   B CD1  1 
ATOM   4079 C  CD2  . TYR   B 1 17  ? 37.372 -25.722 -17.546 1.00 22.97 ?  17  TYR   B CD2  1 
ATOM   4080 C  CE1  . TYR   B 1 17  ? 36.214 -23.365 -16.694 1.00 24.47 ?  17  TYR   B CE1  1 
ATOM   4081 C  CE2  . TYR   B 1 17  ? 36.529 -25.027 -18.389 1.00 24.70 ?  17  TYR   B CE2  1 
ATOM   4082 C  CZ   . TYR   B 1 17  ? 35.950 -23.851 -17.958 1.00 25.55 ?  17  TYR   B CZ   1 
ATOM   4083 O  OH   . TYR   B 1 17  ? 35.111 -23.156 -18.798 1.00 26.74 ?  17  TYR   B OH   1 
ATOM   4084 H  H    . TYR   B 1 17  ? 37.324 -25.629 -13.046 1.00 17.17 ?  17  TYR   B H    1 
ATOM   4085 H  HA   . TYR   B 1 17  ? 37.416 -27.663 -14.852 1.00 17.59 ?  17  TYR   B HA   1 
ATOM   4086 H  HB2  . TYR   B 1 17  ? 39.111 -25.382 -14.864 1.00 20.94 ?  17  TYR   B HB2  1 
ATOM   4087 H  HB3  . TYR   B 1 17  ? 39.152 -26.559 -15.923 1.00 20.94 ?  17  TYR   B HB3  1 
ATOM   4088 H  HD1  . TYR   B 1 17  ? 37.239 -23.742 -15.007 1.00 27.14 ?  17  TYR   B HD1  1 
ATOM   4089 H  HD2  . TYR   B 1 17  ? 37.757 -26.515 -17.841 1.00 27.54 ?  17  TYR   B HD2  1 
ATOM   4090 H  HE1  . TYR   B 1 17  ? 35.823 -22.570 -16.407 1.00 29.34 ?  17  TYR   B HE1  1 
ATOM   4091 H  HE2  . TYR   B 1 17  ? 36.346 -25.351 -19.243 1.00 29.62 ?  17  TYR   B HE2  1 
ATOM   4092 H  HH   . TYR   B 1 17  ? 35.035 -23.557 -19.532 1.00 32.07 ?  17  TYR   B HH   1 
ATOM   4093 N  N    . ILE   B 1 18  ? 39.532 -28.677 -13.881 1.00 14.15 ?  18  ILE   B N    1 
ATOM   4094 C  CA   . ILE   B 1 18  ? 40.465 -29.398 -13.022 1.00 14.17 ?  18  ILE   B CA   1 
ATOM   4095 C  C    . ILE   B 1 18  ? 41.624 -29.946 -13.846 1.00 14.58 ?  18  ILE   B C    1 
ATOM   4096 O  O    . ILE   B 1 18  ? 41.460 -30.334 -15.008 1.00 15.64 ?  18  ILE   B O    1 
ATOM   4097 C  CB   . ILE   B 1 18  ? 39.723 -30.500 -12.220 1.00 14.78 ?  18  ILE   B CB   1 
ATOM   4098 C  CG1  . ILE   B 1 18  ? 40.584 -31.037 -11.072 1.00 15.12 ?  18  ILE   B CG1  1 
ATOM   4099 C  CG2  . ILE   B 1 18  ? 39.241 -31.633 -13.139 1.00 15.04 ?  18  ILE   B CG2  1 
ATOM   4100 C  CD1  . ILE   B 1 18  ? 39.782 -31.832 -10.047 1.00 16.32 ?  18  ILE   B CD1  1 
ATOM   4101 H  H    . ILE   B 1 18  ? 39.416 -29.032 -14.656 1.00 16.95 ?  18  ILE   B H    1 
ATOM   4102 H  HA   . ILE   B 1 18  ? 40.829 -28.781 -12.374 1.00 16.98 ?  18  ILE   B HA   1 
ATOM   4103 H  HB   . ILE   B 1 18  ? 38.935 -30.103 -11.820 1.00 17.71 ?  18  ILE   B HB   1 
ATOM   4104 H  HG12 . ILE   B 1 18  ? 41.269 -31.619 -11.429 1.00 18.12 ?  18  ILE   B HG12 1 
ATOM   4105 H  HG13 . ILE   B 1 18  ? 40.992 -30.287 -10.608 1.00 18.12 ?  18  ILE   B HG13 1 
ATOM   4106 H  HG21 . ILE   B 1 18  ? 38.652 -32.220 -12.637 1.00 18.03 ?  18  ILE   B HG21 1 
ATOM   4107 H  HG22 . ILE   B 1 18  ? 38.760 -31.242 -13.884 1.00 18.03 ?  18  ILE   B HG22 1 
ATOM   4108 H  HG23 . ILE   B 1 18  ? 40.008 -32.129 -13.461 1.00 18.03 ?  18  ILE   B HG23 1 
ATOM   4109 H  HD11 . ILE   B 1 18  ? 40.372 -32.107 -9.326  1.00 19.57 ?  18  ILE   B HD11 1 
ATOM   4110 H  HD12 . ILE   B 1 18  ? 39.072 -31.272 -9.695  1.00 19.57 ?  18  ILE   B HD12 1 
ATOM   4111 H  HD13 . ILE   B 1 18  ? 39.404 -32.614 -10.479 1.00 19.57 ?  18  ILE   B HD13 1 
ATOM   4112 N  N    . LYS   B 1 19  ? 42.804 -29.989 -13.224 1.00 15.19 ?  19  LYS   B N    1 
ATOM   4113 C  CA   . LYS   B 1 19  ? 44.014 -30.455 -13.884 1.00 15.90 ?  19  LYS   B CA   1 
ATOM   4114 C  C    . LYS   B 1 19  ? 44.918 -31.135 -12.866 1.00 15.55 ?  19  LYS   B C    1 
ATOM   4115 O  O    . LYS   B 1 19  ? 45.003 -30.709 -11.713 1.00 15.11 ?  19  LYS   B O    1 
ATOM   4116 C  CB   . LYS   B 1 19  ? 44.773 -29.286 -14.519 1.00 17.60 ?  19  LYS   B CB   1 
ATOM   4117 C  CG   . LYS   B 1 19  ? 45.951 -29.690 -15.384 1.00 19.52 ?  19  LYS   B CG   1 
ATOM   4118 C  CD   . LYS   B 1 19  ? 46.677 -28.459 -15.907 1.00 21.24 ?  19  LYS   B CD   1 
ATOM   4119 C  CE   . LYS   B 1 19  ? 47.837 -28.833 -16.806 1.00 22.94 ?  19  LYS   B CE   1 
ATOM   4120 N  NZ   . LYS   B 1 19  ? 48.578 -27.638 -17.286 1.00 23.76 ?  19  LYS   B NZ   1 
ATOM   4121 H  H    . LYS   B 1 19  ? 42.917 -29.747 -12.405 1.00 18.20 ?  19  LYS   B H    1 
ATOM   4122 H  HA   . LYS   B 1 19  ? 43.776 -31.095 -14.574 1.00 19.06 ?  19  LYS   B HA   1 
ATOM   4123 H  HB2  . LYS   B 1 19  ? 44.155 -28.792 -15.077 1.00 21.09 ?  19  LYS   B HB2  1 
ATOM   4124 H  HB3  . LYS   B 1 19  ? 45.103 -28.713 -13.808 1.00 21.09 ?  19  LYS   B HB3  1 
ATOM   4125 H  HG2  . LYS   B 1 19  ? 46.567 -30.218 -14.856 1.00 23.40 ?  19  LYS   B HG2  1 
ATOM   4126 H  HG3  . LYS   B 1 19  ? 45.623 -30.206 -16.140 1.00 23.40 ?  19  LYS   B HG3  1 
ATOM   4127 H  HD2  . LYS   B 1 19  ? 46.053 -27.916 -16.417 1.00 25.46 ?  19  LYS   B HD2  1 
ATOM   4128 H  HD3  . LYS   B 1 19  ? 47.021 -27.952 -15.154 1.00 25.46 ?  19  LYS   B HD3  1 
ATOM   4129 H  HE2  . LYS   B 1 19  ? 48.452 -29.396 -16.311 1.00 27.51 ?  19  LYS   B HE2  1 
ATOM   4130 H  HE3  . LYS   B 1 19  ? 47.495 -29.312 -17.579 1.00 27.51 ?  19  LYS   B HE3  1 
ATOM   4131 H  HZ1  . LYS   B 1 19  ? 49.206 -27.884 -17.867 1.00 28.49 ?  19  LYS   B HZ1  1 
ATOM   4132 H  HZ2  . LYS   B 1 19  ? 48.019 -27.073 -17.686 1.00 28.49 ?  19  LYS   B HZ2  1 
ATOM   4133 H  HZ3  . LYS   B 1 19  ? 48.964 -27.224 -16.600 1.00 28.49 ?  19  LYS   B HZ3  1 
ATOM   4134 N  N    . ASN   B 1 20  ? 45.600 -32.190 -13.301 1.00 16.81 ?  20  ASN   B N    1 
ATOM   4135 C  CA   . ASN   B 1 20  ? 46.628 -32.825 -12.483 1.00 18.06 ?  20  ASN   B CA   1 
ATOM   4136 C  C    . ASN   B 1 20  ? 47.902 -32.007 -12.663 1.00 18.35 ?  20  ASN   B C    1 
ATOM   4137 O  O    . ASN   B 1 20  ? 48.553 -32.081 -13.709 1.00 20.40 ?  20  ASN   B O    1 
ATOM   4138 C  CB   . ASN   B 1 20  ? 46.800 -34.276 -12.927 1.00 19.69 ?  20  ASN   B CB   1 
ATOM   4139 C  CG   . ASN   B 1 20  ? 47.964 -34.979 -12.247 1.00 21.18 ?  20  ASN   B CG   1 
ATOM   4140 O  OD1  . ASN   B 1 20  ? 48.635 -35.820 -12.859 1.00 23.24 ?  20  ASN   B OD1  1 
ATOM   4141 N  ND2  . ASN   B 1 20  ? 48.200 -34.664 -10.983 1.00 20.75 ?  20  ASN   B ND2  1 
ATOM   4142 H  H    . ASN   B 1 20  ? 45.482 -32.557 -14.068 1.00 20.15 ?  20  ASN   B H    1 
ATOM   4143 H  HA   . ASN   B 1 20  ? 46.353 -32.812 -11.549 1.00 21.65 ?  20  ASN   B HA   1 
ATOM   4144 H  HB2  . ASN   B 1 20  ? 45.987 -34.771 -12.717 1.00 23.60 ?  20  ASN   B HB2  1 
ATOM   4145 H  HB3  . ASN   B 1 20  ? 46.954 -34.294 -13.883 1.00 23.60 ?  20  ASN   B HB3  1 
ATOM   4146 H  HD21 . ASN   B 1 20  ? 48.850 -35.033 -10.563 1.00 24.88 ?  20  ASN   B HD21 1 
ATOM   4147 H  HD22 . ASN   B 1 20  ? 47.711 -34.075 -10.583 1.00 24.88 ?  20  ASN   B HD22 1 
ATOM   4148 N  N    . ALA   B 1 21  ? 48.257 -31.207 -11.654 1.00 17.78 ?  21  ALA   B N    1 
ATOM   4149 C  CA   . ALA   B 1 21  ? 49.383 -30.301 -11.807 1.00 18.45 ?  21  ALA   B CA   1 
ATOM   4150 C  C    . ALA   B 1 21  ? 49.840 -29.787 -10.450 1.00 17.43 ?  21  ALA   B C    1 
ATOM   4151 O  O    . ALA   B 1 21  ? 49.100 -29.814 -9.463  1.00 17.21 ?  21  ALA   B O    1 
ATOM   4152 C  CB   . ALA   B 1 21  ? 49.022 -29.142 -12.732 1.00 20.00 ?  21  ALA   B CB   1 
ATOM   4153 H  H    . ALA   B 1 21  ? 47.863 -31.182 -10.885 1.00 21.32 ?  21  ALA   B H    1 
ATOM   4154 H  HA   . ALA   B 1 21  ? 50.119 -30.794 -12.205 1.00 22.11 ?  21  ALA   B HA   1 
ATOM   4155 H  HB1  . ALA   B 1 21  ? 49.820 -28.624 -12.887 1.00 23.98 ?  21  ALA   B HB1  1 
ATOM   4156 H  HB2  . ALA   B 1 21  ? 48.693 -29.510 -13.568 1.00 23.98 ?  21  ALA   B HB2  1 
ATOM   4157 H  HB3  . ALA   B 1 21  ? 48.337 -28.609 -12.309 1.00 23.98 ?  21  ALA   B HB3  1 
ATOM   4158 N  N    . ASP   B 1 22  ? 51.095 -29.339 -10.433 1.00 16.66 ?  22  ASP   B N    1 
ATOM   4159 C  CA   . ASP   B 1 22  ? 51.710 -28.641 -9.309  1.00 15.91 ?  22  ASP   B CA   1 
ATOM   4160 C  C    . ASP   B 1 22  ? 51.299 -27.170 -9.387  1.00 14.58 ?  22  ASP   B C    1 
ATOM   4161 O  O    . ASP   B 1 22  ? 51.605 -26.493 -10.372 1.00 14.68 ?  22  ASP   B O    1 
ATOM   4162 C  CB   . ASP   B 1 22  ? 53.229 -28.805 -9.466  1.00 17.23 ?  22  ASP   B CB   1 
ATOM   4163 C  CG   . ASP   B 1 22  ? 54.051 -28.061 -8.420  1.00 18.71 ?  22  ASP   B CG   1 
ATOM   4164 O  OD1  . ASP   B 1 22  ? 53.674 -26.957 -7.999  1.00 18.70 ?  22  ASP   B OD1  1 
ATOM   4165 O  OD2  . ASP   B 1 22  ? 55.131 -28.572 -8.047  1.00 20.88 -1 22  ASP   B OD2  1 
ATOM   4166 H  H    . ASP   B 1 22  ? 51.637 -29.439 -11.099 1.00 19.97 ?  22  ASP   B H    1 
ATOM   4167 H  HA   . ASP   B 1 22  ? 51.423 -29.027 -8.465  1.00 19.07 ?  22  ASP   B HA   1 
ATOM   4168 H  HB2  . ASP   B 1 22  ? 53.458 -29.739 -9.405  1.00 20.65 ?  22  ASP   B HB2  1 
ATOM   4169 H  HB3  . ASP   B 1 22  ? 53.493 -28.451 -10.331 1.00 20.65 ?  22  ASP   B HB3  1 
ATOM   4170 N  N    . ILE   B 1 23  ? 50.586 -26.681 -8.365  1.00 13.49 ?  23  ILE   B N    1 
ATOM   4171 C  CA   . ILE   B 1 23  ? 49.996 -25.340 -8.429  1.00 12.88 ?  23  ILE   B CA   1 
ATOM   4172 C  C    . ILE   B 1 23  ? 51.052 -24.251 -8.566  1.00 12.31 ?  23  ILE   B C    1 
ATOM   4173 O  O    . ILE   B 1 23  ? 50.787 -23.208 -9.172  1.00 12.28 ?  23  ILE   B O    1 
ATOM   4174 C  CB   . ILE   B 1 23  ? 49.058 -25.096 -7.232  1.00 13.42 ?  23  ILE   B CB   1 
ATOM   4175 C  CG1  . ILE   B 1 23  ? 48.221 -23.836 -7.453  1.00 13.71 ?  23  ILE   B CG1  1 
ATOM   4176 C  CG2  . ILE   B 1 23  ? 49.822 -25.043 -5.929  1.00 14.18 ?  23  ILE   B CG2  1 
ATOM   4177 C  CD1  . ILE   B 1 23  ? 47.108 -23.659 -6.434  1.00 14.50 ?  23  ILE   B CD1  1 
ATOM   4178 H  H    . ILE   B 1 23  ? 50.432 -27.108 -7.636  1.00 16.16 ?  23  ILE   B H    1 
ATOM   4179 H  HA   . ILE   B 1 23  ? 49.448 -25.300 -9.225  1.00 15.43 ?  23  ILE   B HA   1 
ATOM   4180 H  HB   . ILE   B 1 23  ? 48.440 -25.849 -7.184  1.00 16.08 ?  23  ILE   B HB   1 
ATOM   4181 H  HG12 . ILE   B 1 23  ? 48.805 -23.061 -7.394  1.00 16.43 ?  23  ILE   B HG12 1 
ATOM   4182 H  HG13 . ILE   B 1 23  ? 47.818 -23.873 -8.337  1.00 16.43 ?  23  ILE   B HG13 1 
ATOM   4183 H  HG21 . ILE   B 1 23  ? 49.192 -25.051 -5.193  1.00 16.99 ?  23  ILE   B HG21 1 
ATOM   4184 H  HG22 . ILE   B 1 23  ? 50.407 -25.812 -5.876  1.00 16.99 ?  23  ILE   B HG22 1 
ATOM   4185 H  HG23 . ILE   B 1 23  ? 50.346 -24.225 -5.908  1.00 16.99 ?  23  ILE   B HG23 1 
ATOM   4186 H  HD11 . ILE   B 1 23  ? 46.574 -22.889 -6.682  1.00 17.38 ?  23  ILE   B HD11 1 
ATOM   4187 H  HD12 . ILE   B 1 23  ? 46.555 -24.458 -6.436  1.00 17.38 ?  23  ILE   B HD12 1 
ATOM   4188 H  HD13 . ILE   B 1 23  ? 47.499 -23.528 -5.559  1.00 17.38 ?  23  ILE   B HD13 1 
ATOM   4189 N  N    . VAL   B 1 24  ? 52.248 -24.457 -8.007  1.00 13.00 ?  24  VAL   B N    1 
ATOM   4190 C  CA   . VAL   B 1 24  ? 53.326 -23.482 -8.177  1.00 13.64 ?  24  VAL   B CA   1 
ATOM   4191 C  C    . VAL   B 1 24  ? 53.778 -23.438 -9.629  1.00 13.65 ?  24  VAL   B C    1 
ATOM   4192 O  O    . VAL   B 1 24  ? 53.924 -22.358 -10.219 1.00 13.97 ?  24  VAL   B O    1 
ATOM   4193 C  CB   . VAL   B 1 24  ? 54.500 -23.799 -7.229  1.00 14.49 ?  24  VAL   B CB   1 
ATOM   4194 C  CG1  . VAL   B 1 24  ? 55.712 -22.920 -7.556  1.00 15.24 ?  24  VAL   B CG1  1 
ATOM   4195 C  CG2  . VAL   B 1 24  ? 54.086 -23.621 -5.785  1.00 15.74 ?  24  VAL   B CG2  1 
ATOM   4196 H  H    . VAL   B 1 24  ? 52.459 -25.144 -7.533  1.00 15.58 ?  24  VAL   B H    1 
ATOM   4197 H  HA   . VAL   B 1 24  ? 52.994 -22.606 -7.942  1.00 16.35 ?  24  VAL   B HA   1 
ATOM   4198 H  HB   . VAL   B 1 24  ? 54.766 -24.727 -7.346  1.00 17.37 ?  24  VAL   B HB   1 
ATOM   4199 H  HG11 . VAL   B 1 24  ? 56.311 -22.915 -6.793  1.00 18.27 ?  24  VAL   B HG11 1 
ATOM   4200 H  HG12 . VAL   B 1 24  ? 56.165 -23.285 -8.329  1.00 18.27 ?  24  VAL   B HG12 1 
ATOM   4201 H  HG13 . VAL   B 1 24  ? 55.403 -22.020 -7.739  1.00 18.27 ?  24  VAL   B HG13 1 
ATOM   4202 H  HG21 . VAL   B 1 24  ? 54.819 -23.887 -5.208  1.00 18.87 ?  24  VAL   B HG21 1 
ATOM   4203 H  HG22 . VAL   B 1 24  ? 53.867 -22.689 -5.634  1.00 18.87 ?  24  VAL   B HG22 1 
ATOM   4204 H  HG23 . VAL   B 1 24  ? 53.309 -24.177 -5.608  1.00 18.87 ?  24  VAL   B HG23 1 
ATOM   4205 N  N    . GLU   B 1 25  ? 54.048 -24.609 -10.216 1.00 14.62 ?  25  GLU   B N    1 
ATOM   4206 C  CA   . GLU   B 1 25  ? 54.438 -24.643 -11.620 1.00 16.11 ?  25  GLU   B CA   1 
ATOM   4207 C  C    . GLU   B 1 25  ? 53.328 -24.097 -12.503 1.00 14.84 ?  25  GLU   B C    1 
ATOM   4208 O  O    . GLU   B 1 25  ? 53.592 -23.381 -13.477 1.00 15.80 ?  25  GLU   B O    1 
ATOM   4209 C  CB   . GLU   B 1 25  ? 54.826 -26.064 -12.024 1.00 20.14 ?  25  GLU   B CB   1 
ATOM   4210 C  CG   . GLU   B 1 25  ? 56.126 -26.517 -11.380 1.00 25.41 ?  25  GLU   B CG   1 
ATOM   4211 C  CD   . GLU   B 1 25  ? 57.238 -25.478 -11.474 1.00 30.04 ?  25  GLU   B CD   1 
ATOM   4212 O  OE1  . GLU   B 1 25  ? 57.642 -25.131 -12.605 1.00 31.99 ?  25  GLU   B OE1  1 
ATOM   4213 O  OE2  . GLU   B 1 25  ? 57.697 -24.989 -10.414 1.00 31.58 -1 25  GLU   B OE2  1 
ATOM   4214 H  H    . GLU   B 1 25  ? 54.009 -25.379 -9.830  1.00 17.52 ?  25  GLU   B H    1 
ATOM   4215 H  HA   . GLU   B 1 25  ? 55.196 -24.059 -11.744 1.00 19.31 ?  25  GLU   B HA   1 
ATOM   4216 H  HB2  . GLU   B 1 25  ? 54.125 -26.677 -11.745 1.00 24.15 ?  25  GLU   B HB2  1 
ATOM   4217 H  HB3  . GLU   B 1 25  ? 54.933 -26.101 -12.987 1.00 24.15 ?  25  GLU   B HB3  1 
ATOM   4218 H  HG2  . GLU   B 1 25  ? 55.975 -26.681 -10.442 1.00 30.46 ?  25  GLU   B HG2  1 
ATOM   4219 H  HG3  . GLU   B 1 25  ? 56.431 -27.324 -11.824 1.00 30.46 ?  25  GLU   B HG3  1 
ATOM   4220 N  N    A GLU   B 1 26  ? 52.076 -24.418 -12.171 0.72 14.01 ?  26  GLU   B N    1 
ATOM   4221 N  N    B GLU   B 1 26  ? 52.075 -24.420 -12.174 0.28 14.60 ?  26  GLU   B N    1 
ATOM   4222 C  CA   A GLU   B 1 26  ? 50.948 -23.891 -12.931 0.72 14.68 ?  26  GLU   B CA   1 
ATOM   4223 C  CA   B GLU   B 1 26  ? 50.948 -23.890 -12.936 0.28 14.98 ?  26  GLU   B CA   1 
ATOM   4224 C  C    A GLU   B 1 26  ? 50.900 -22.374 -12.853 0.72 13.92 ?  26  GLU   B C    1 
ATOM   4225 C  C    B GLU   B 1 26  ? 50.901 -22.372 -12.855 0.28 14.00 ?  26  GLU   B C    1 
ATOM   4226 O  O    A GLU   B 1 26  ? 50.699 -21.697 -13.866 0.72 15.08 ?  26  GLU   B O    1 
ATOM   4227 O  O    B GLU   B 1 26  ? 50.718 -21.690 -13.869 0.28 14.48 ?  26  GLU   B O    1 
ATOM   4228 C  CB   A GLU   B 1 26  ? 49.640 -24.479 -12.401 0.72 16.79 ?  26  GLU   B CB   1 
ATOM   4229 C  CB   B GLU   B 1 26  ? 49.639 -24.485 -12.419 0.28 16.52 ?  26  GLU   B CB   1 
ATOM   4230 C  CG   A GLU   B 1 26  ? 49.208 -25.761 -13.075 0.72 20.05 ?  26  GLU   B CG   1 
ATOM   4231 C  CG   B GLU   B 1 26  ? 49.233 -25.775 -13.098 0.28 18.49 ?  26  GLU   B CG   1 
ATOM   4232 C  CD   A GLU   B 1 26  ? 48.928 -25.572 -14.564 0.72 21.85 ?  26  GLU   B CD   1 
ATOM   4233 C  CD   B GLU   B 1 26  ? 48.981 -25.619 -14.588 0.28 19.79 ?  26  GLU   B CD   1 
ATOM   4234 O  OE1  A GLU   B 1 26  ? 47.928 -24.917 -14.933 0.72 22.50 ?  26  GLU   B OE1  1 
ATOM   4235 O  OE1  B GLU   B 1 26  ? 48.090 -24.835 -14.976 0.28 20.11 ?  26  GLU   B OE1  1 
ATOM   4236 O  OE2  A GLU   B 1 26  ? 49.719 -26.082 -15.369 0.72 23.63 -1 26  GLU   B OE2  1 
ATOM   4237 O  OE2  B GLU   B 1 26  ? 49.676 -26.292 -15.372 0.28 20.92 -1 26  GLU   B OE2  1 
ATOM   4238 H  H    A GLU   B 1 26  ? 51.854 -24.941 -11.521 0.72 16.78 ?  26  GLU   B H    1 
ATOM   4239 H  H    B GLU   B 1 26  ? 51.852 -24.941 -11.524 0.28 17.49 ?  26  GLU   B H    1 
ATOM   4240 H  HA   A GLU   B 1 26  ? 51.044 -24.144 -13.860 0.72 17.60 ?  26  GLU   B HA   1 
ATOM   4241 H  HA   B GLU   B 1 26  ? 51.051 -24.137 -13.865 0.28 17.96 ?  26  GLU   B HA   1 
ATOM   4242 H  HB2  A GLU   B 1 26  ? 49.739 -24.665 -11.454 0.72 20.13 ?  26  GLU   B HB2  1 
ATOM   4243 H  HB2  B GLU   B 1 26  ? 49.732 -24.672 -11.469 0.28 19.80 ?  26  GLU   B HB2  1 
ATOM   4244 H  HB3  A GLU   B 1 26  ? 48.930 -23.830 -12.533 0.72 20.13 ?  26  GLU   B HB3  1 
ATOM   4245 H  HB3  B GLU   B 1 26  ? 48.927 -23.842 -12.554 0.28 19.80 ?  26  GLU   B HB3  1 
ATOM   4246 H  HG2  A GLU   B 1 26  ? 49.913 -26.419 -12.964 0.72 24.04 ?  26  GLU   B HG2  1 
ATOM   4247 H  HG2  B GLU   B 1 26  ? 49.945 -26.418 -12.985 0.28 22.17 ?  26  GLU   B HG2  1 
ATOM   4248 H  HG3  A GLU   B 1 26  ? 48.391 -26.078 -12.659 0.72 24.04 ?  26  GLU   B HG3  1 
ATOM   4249 H  HG3  B GLU   B 1 26  ? 48.416 -26.097 -12.692 0.28 22.17 ?  26  GLU   B HG3  1 
ATOM   4250 N  N    . ALA   B 1 27  ? 51.048 -21.824 -11.648 1.00 13.01 ?  27  ALA   B N    1 
ATOM   4251 C  CA   . ALA   B 1 27  ? 51.010 -20.375 -11.496 1.00 13.22 ?  27  ALA   B CA   1 
ATOM   4252 C  C    . ALA   B 1 27  ? 52.079 -19.709 -12.356 1.00 14.11 ?  27  ALA   B C    1 
ATOM   4253 O  O    . ALA   B 1 27  ? 51.813 -18.706 -13.034 1.00 14.93 ?  27  ALA   B O    1 
ATOM   4254 C  CB   . ALA   B 1 27  ? 51.166 -20.000 -10.023 1.00 13.47 ?  27  ALA   B CB   1 
ATOM   4255 H  H    A ALA   B 1 27  ? 51.169 -22.262 -10.915 0.72 15.59 ?  27  ALA   B H    1 
ATOM   4256 H  H    B ALA   B 1 27  ? 51.173 -22.263 -10.916 0.28 15.59 ?  27  ALA   B H    1 
ATOM   4257 H  HA   . ALA   B 1 27  ? 50.152 -20.050 -11.791 1.00 15.84 ?  27  ALA   B HA   1 
ATOM   4258 H  HB1  . ALA   B 1 27  ? 51.134 -19.035 -9.934  1.00 16.14 ?  27  ALA   B HB1  1 
ATOM   4259 H  HB2  . ALA   B 1 27  ? 50.436 -20.400 -9.517  1.00 16.14 ?  27  ALA   B HB2  1 
ATOM   4260 H  HB3  . ALA   B 1 27  ? 52.014 -20.336 -9.693  1.00 16.14 ?  27  ALA   B HB3  1 
ATOM   4261 N  N    . LYS   B 1 28  ? 53.295 -20.255 -12.351 1.00 15.73 ?  28  LYS   B N    1 
ATOM   4262 C  CA   . LYS   B 1 28  ? 54.366 -19.634 -13.120 1.00 17.64 ?  28  LYS   B CA   1 
ATOM   4263 C  C    . LYS   B 1 28  ? 54.113 -19.722 -14.618 1.00 18.30 ?  28  LYS   B C    1 
ATOM   4264 O  O    . LYS   B 1 28  ? 54.529 -18.828 -15.366 1.00 19.35 ?  28  LYS   B O    1 
ATOM   4265 C  CB   . LYS   B 1 28  ? 55.721 -20.237 -12.738 1.00 20.28 ?  28  LYS   B CB   1 
ATOM   4266 C  CG   . LYS   B 1 28  ? 56.126 -19.904 -11.309 1.00 23.71 ?  28  LYS   B CG   1 
ATOM   4267 C  CD   . LYS   B 1 28  ? 57.555 -20.309 -10.980 1.00 28.22 ?  28  LYS   B CD   1 
ATOM   4268 C  CE   . LYS   B 1 28  ? 57.670 -21.784 -10.676 1.00 31.74 ?  28  LYS   B CE   1 
ATOM   4269 N  NZ   . LYS   B 1 28  ? 59.030 -22.121 -10.166 1.00 33.50 ?  28  LYS   B NZ   1 
ATOM   4270 H  H    . LYS   B 1 28  ? 53.522 -20.965 -11.918 1.00 18.85 ?  28  LYS   B H    1 
ATOM   4271 H  HA   . LYS   B 1 28  ? 54.398 -18.692 -12.895 1.00 21.14 ?  28  LYS   B HA   1 
ATOM   4272 H  HB2  . LYS   B 1 28  ? 55.679 -21.201 -12.820 1.00 24.31 ?  28  LYS   B HB2  1 
ATOM   4273 H  HB3  . LYS   B 1 28  ? 56.406 -19.883 -13.332 1.00 24.31 ?  28  LYS   B HB3  1 
ATOM   4274 H  HG2  . LYS   B 1 28  ? 56.046 -18.945 -11.179 1.00 28.43 ?  28  LYS   B HG2  1 
ATOM   4275 H  HG3  . LYS   B 1 28  ? 55.532 -20.371 -10.702 1.00 28.43 ?  28  LYS   B HG3  1 
ATOM   4276 H  HD2  . LYS   B 1 28  ? 58.124 -20.108 -11.740 1.00 33.84 ?  28  LYS   B HD2  1 
ATOM   4277 H  HD3  . LYS   B 1 28  ? 57.851 -19.812 -10.201 1.00 33.84 ?  28  LYS   B HD3  1 
ATOM   4278 H  HE2  . LYS   B 1 28  ? 57.020 -22.023 -9.996  1.00 38.07 ?  28  LYS   B HE2  1 
ATOM   4279 H  HE3  . LYS   B 1 28  ? 57.512 -22.293 -11.487 1.00 38.07 ?  28  LYS   B HE3  1 
ATOM   4280 H  HZ1  . LYS   B 1 28  ? 59.083 -22.991 -9.991  1.00 40.18 ?  28  LYS   B HZ1  1 
ATOM   4281 H  HZ2  . LYS   B 1 28  ? 59.643 -21.909 -10.775 1.00 40.18 ?  28  LYS   B HZ2  1 
ATOM   4282 H  HZ3  . LYS   B 1 28  ? 59.196 -21.665 -9.419  1.00 40.18 ?  28  LYS   B HZ3  1 
ATOM   4283 N  N    . LYS   B 1 29  ? 53.411 -20.760 -15.073 1.00 19.33 ?  29  LYS   B N    1 
ATOM   4284 C  CA   . LYS   B 1 29  ? 53.132 -20.909 -16.496 1.00 22.24 ?  29  LYS   B CA   1 
ATOM   4285 C  C    . LYS   B 1 29  ? 51.876 -20.164 -16.937 1.00 21.12 ?  29  LYS   B C    1 
ATOM   4286 O  O    . LYS   B 1 29  ? 51.870 -19.554 -18.012 1.00 22.33 ?  29  LYS   B O    1 
ATOM   4287 C  CB   . LYS   B 1 29  ? 53.005 -22.392 -16.853 1.00 26.87 ?  29  LYS   B CB   1 
ATOM   4288 C  CG   . LYS   B 1 29  ? 52.922 -22.671 -18.344 1.00 31.27 ?  29  LYS   B CG   1 
ATOM   4289 C  CD   . LYS   B 1 29  ? 53.118 -24.150 -18.644 1.00 34.98 ?  29  LYS   B CD   1 
ATOM   4290 C  CE   . LYS   B 1 29  ? 51.962 -24.992 -18.124 1.00 37.69 ?  29  LYS   B CE   1 
ATOM   4291 N  NZ   . LYS   B 1 29  ? 52.178 -26.446 -18.376 1.00 38.90 ?  29  LYS   B NZ   1 
ATOM   4292 H  H    . LYS   B 1 29  ? 53.085 -21.392 -14.575 1.00 23.17 ?  29  LYS   B H    1 
ATOM   4293 H  HA   . LYS   B 1 29  ? 53.877 -20.546 -16.993 1.00 26.66 ?  29  LYS   B HA   1 
ATOM   4294 H  HB2  . LYS   B 1 29  ? 53.783 -22.861 -16.512 1.00 32.22 ?  29  LYS   B HB2  1 
ATOM   4295 H  HB3  . LYS   B 1 29  ? 52.203 -22.745 -16.444 1.00 32.22 ?  29  LYS   B HB3  1 
ATOM   4296 H  HG2  . LYS   B 1 29  ? 52.048 -22.407 -18.671 1.00 37.51 ?  29  LYS   B HG2  1 
ATOM   4297 H  HG3  . LYS   B 1 29  ? 53.617 -22.172 -18.803 1.00 37.51 ?  29  LYS   B HG3  1 
ATOM   4298 H  HD2  . LYS   B 1 29  ? 53.178 -24.275 -19.603 1.00 41.95 ?  29  LYS   B HD2  1 
ATOM   4299 H  HD3  . LYS   B 1 29  ? 53.933 -24.456 -18.215 1.00 41.95 ?  29  LYS   B HD3  1 
ATOM   4300 H  HE2  . LYS   B 1 29  ? 51.874 -24.864 -17.167 1.00 45.20 ?  29  LYS   B HE2  1 
ATOM   4301 H  HE3  . LYS   B 1 29  ? 51.145 -24.725 -18.574 1.00 45.20 ?  29  LYS   B HE3  1 
ATOM   4302 H  HZ1  . LYS   B 1 29  ? 51.489 -26.915 -18.063 1.00 46.66 ?  29  LYS   B HZ1  1 
ATOM   4303 H  HZ2  . LYS   B 1 29  ? 52.256 -26.596 -19.250 1.00 46.66 ?  29  LYS   B HZ2  1 
ATOM   4304 H  HZ3  . LYS   B 1 29  ? 52.921 -26.719 -17.968 1.00 46.66 ?  29  LYS   B HZ3  1 
ATOM   4305 N  N    . VAL   B 1 30  ? 50.815 -20.206 -16.126 1.00 19.33 ?  30  VAL   B N    1 
ATOM   4306 C  CA   . VAL   B 1 30  ? 49.523 -19.626 -16.502 1.00 19.43 ?  30  VAL   B CA   1 
ATOM   4307 C  C    . VAL   B 1 30  ? 49.523 -18.112 -16.366 1.00 18.38 ?  30  VAL   B C    1 
ATOM   4308 O  O    . VAL   B 1 30  ? 48.772 -17.414 -17.067 1.00 19.11 ?  30  VAL   B O    1 
ATOM   4309 C  CB   . VAL   B 1 30  ? 48.423 -20.239 -15.614 1.00 20.66 ?  30  VAL   B CB   1 
ATOM   4310 C  CG1  . VAL   B 1 30  ? 47.134 -19.425 -15.686 1.00 20.95 ?  30  VAL   B CG1  1 
ATOM   4311 C  CG2  . VAL   B 1 30  ? 48.181 -21.688 -15.999 1.00 21.61 ?  30  VAL   B CG2  1 
ATOM   4312 H  H    . VAL   B 1 30  ? 50.809 -20.583 -15.343 1.00 23.17 ?  30  VAL   B H    1 
ATOM   4313 H  HA   . VAL   B 1 30  ? 49.327 -19.862 -17.422 1.00 23.29 ?  30  VAL   B HA   1 
ATOM   4314 H  HB   . VAL   B 1 30  ? 48.719 -20.232 -14.690 1.00 24.77 ?  30  VAL   B HB   1 
ATOM   4315 H  HG11 . VAL   B 1 30  ? 46.393 -20.003 -15.445 1.00 25.12 ?  30  VAL   B HG11 1 
ATOM   4316 H  HG12 . VAL   B 1 30  ? 47.187 -18.686 -15.062 1.00 25.12 ?  30  VAL   B HG12 1 
ATOM   4317 H  HG13 . VAL   B 1 30  ? 47.010 -19.104 -16.588 1.00 25.12 ?  30  VAL   B HG13 1 
ATOM   4318 H  HG21 . VAL   B 1 30  ? 47.492 -22.062 -15.423 1.00 25.91 ?  30  VAL   B HG21 1 
ATOM   4319 H  HG22 . VAL   B 1 30  ? 47.886 -21.723 -16.925 1.00 25.91 ?  30  VAL   B HG22 1 
ATOM   4320 H  HG23 . VAL   B 1 30  ? 49.004 -22.185 -15.895 1.00 25.91 ?  30  VAL   B HG23 1 
ATOM   4321 N  N    . LYS   B 1 31  ? 50.318 -17.599 -15.438 1.00 17.70 ?  31  LYS   B N    1 
ATOM   4322 C  CA   . LYS   B 1 31  ? 50.340 -16.188 -15.083 1.00 18.10 ?  31  LYS   B CA   1 
ATOM   4323 C  C    . LYS   B 1 31  ? 48.940 -15.694 -14.696 1.00 16.10 ?  31  LYS   B C    1 
ATOM   4324 O  O    . LYS   B 1 31  ? 48.402 -14.778 -15.323 1.00 16.77 ?  31  LYS   B O    1 
ATOM   4325 C  CB   . LYS   B 1 31  ? 50.966 -15.357 -16.197 1.00 21.06 ?  31  LYS   B CB   1 
ATOM   4326 C  CG   . LYS   B 1 31  ? 52.417 -15.789 -16.486 1.00 24.40 ?  31  LYS   B CG   1 
ATOM   4327 C  CD   . LYS   B 1 31  ? 53.005 -15.071 -17.690 1.00 27.93 ?  31  LYS   B CD   1 
ATOM   4328 C  CE   . LYS   B 1 31  ? 54.498 -15.326 -17.821 1.00 30.50 ?  31  LYS   B CE   1 
ATOM   4329 N  NZ   . LYS   B 1 31  ? 55.222 -14.878 -16.601 1.00 31.92 ?  31  LYS   B NZ   1 
ATOM   4330 H  H    . LYS   B 1 31  ? 50.865 -18.069 -14.991 1.00 21.21 ?  31  LYS   B H    1 
ATOM   4331 H  HA   . LYS   B 1 31  ? 50.887 -16.091 -14.297 1.00 21.70 ?  31  LYS   B HA   1 
ATOM   4332 H  HB2  . LYS   B 1 31  ? 50.466 -15.476 -17.020 1.00 25.25 ?  31  LYS   B HB2  1 
ATOM   4333 H  HB3  . LYS   B 1 31  ? 50.989 -14.429 -15.944 1.00 25.25 ?  31  LYS   B HB3  1 
ATOM   4334 H  HG2  . LYS   B 1 31  ? 52.959 -15.590 -15.706 1.00 29.26 ?  31  LYS   B HG2  1 
ATOM   4335 H  HG3  . LYS   B 1 31  ? 52.434 -16.747 -16.662 1.00 29.26 ?  31  LYS   B HG3  1 
ATOM   4336 H  HD2  . LYS   B 1 31  ? 52.568 -15.394 -18.492 1.00 33.49 ?  31  LYS   B HD2  1 
ATOM   4337 H  HD3  . LYS   B 1 31  ? 52.864 -14.120 -17.586 1.00 33.49 ?  31  LYS   B HD3  1 
ATOM   4338 H  HE2  . LYS   B 1 31  ? 54.662 -16.277 -17.940 1.00 36.58 ?  31  LYS   B HE2  1 
ATOM   4339 H  HE3  . LYS   B 1 31  ? 54.847 -14.829 -18.580 1.00 36.58 ?  31  LYS   B HE3  1 
ATOM   4340 H  HZ1  . LYS   B 1 31  ? 56.100 -14.902 -16.740 1.00 38.28 ?  31  LYS   B HZ1  1 
ATOM   4341 H  HZ2  . LYS   B 1 31  ? 54.982 -14.046 -16.397 1.00 38.28 ?  31  LYS   B HZ2  1 
ATOM   4342 H  HZ3  . LYS   B 1 31  ? 55.022 -15.413 -15.917 1.00 38.28 ?  31  LYS   B HZ3  1 
ATOM   4343 N  N    . PRO   B 1 32  ? 48.332 -16.287 -13.657 1.00 14.27 ?  32  PRO   B N    1 
ATOM   4344 C  CA   . PRO   B 1 32  ? 46.959 -15.924 -13.285 1.00 13.70 ?  32  PRO   B CA   1 
ATOM   4345 C  C    . PRO   B 1 32  ? 46.882 -14.580 -12.578 1.00 13.75 ?  32  PRO   B C    1 
ATOM   4346 O  O    . PRO   B 1 32  ? 47.804 -14.160 -11.874 1.00 14.93 ?  32  PRO   B O    1 
ATOM   4347 C  CB   . PRO   B 1 32  ? 46.564 -17.036 -12.308 1.00 13.65 ?  32  PRO   B CB   1 
ATOM   4348 C  CG   . PRO   B 1 32  ? 47.876 -17.391 -11.649 1.00 13.84 ?  32  PRO   B CG   1 
ATOM   4349 C  CD   . PRO   B 1 32  ? 48.919 -17.268 -12.718 1.00 14.35 ?  32  PRO   B CD   1 
ATOM   4350 H  HA   . PRO   B 1 32  ? 46.370 -15.936 -14.057 1.00 16.42 ?  32  PRO   B HA   1 
ATOM   4351 H  HB2  . PRO   B 1 32  ? 45.927 -16.695 -11.657 1.00 16.36 ?  32  PRO   B HB2  1 
ATOM   4352 H  HB3  . PRO   B 1 32  ? 46.198 -17.790 -12.792 1.00 16.36 ?  32  PRO   B HB3  1 
ATOM   4353 H  HG2  . PRO   B 1 32  ? 48.061 -16.770 -10.924 1.00 16.58 ?  32  PRO   B HG2  1 
ATOM   4354 H  HG3  . PRO   B 1 32  ? 47.841 -18.301 -11.313 1.00 16.58 ?  32  PRO   B HG3  1 
ATOM   4355 H  HD2  . PRO   B 1 32  ? 49.747 -16.927 -12.344 1.00 17.20 ?  32  PRO   B HD2  1 
ATOM   4356 H  HD3  . PRO   B 1 32  ? 49.050 -18.122 -13.156 1.00 17.20 ?  32  PRO   B HD3  1 
ATOM   4357 N  N    . THR   B 1 33  ? 45.732 -13.921 -12.745 1.00 12.97 ?  33  THR   B N    1 
ATOM   4358 C  CA   . THR   B 1 33  ? 45.440 -12.746 -11.933 1.00 13.26 ?  33  THR   B CA   1 
ATOM   4359 C  C    . THR   B 1 33  ? 45.397 -13.102 -10.451 1.00 13.02 ?  33  THR   B C    1 
ATOM   4360 O  O    . THR   B 1 33  ? 45.873 -12.329 -9.607  1.00 13.92 ?  33  THR   B O    1 
ATOM   4361 C  CB   . THR   B 1 33  ? 44.120 -12.108 -12.375 1.00 13.89 ?  33  THR   B CB   1 
ATOM   4362 O  OG1  . THR   B 1 33  ? 44.153 -11.858 -13.782 1.00 14.03 ?  33  THR   B OG1  1 
ATOM   4363 C  CG2  . THR   B 1 33  ? 43.877 -10.808 -11.623 1.00 14.98 ?  33  THR   B CG2  1 
ATOM   4364 H  H    . THR   B 1 33  ? 45.112 -14.134 -13.308 1.00 15.55 ?  33  THR   B H    1 
ATOM   4365 H  HA   . THR   B 1 33  ? 46.138 -12.090 -12.066 1.00 15.88 ?  33  THR   B HA   1 
ATOM   4366 H  HB   . THR   B 1 33  ? 43.382 -12.715 -12.179 1.00 16.64 ?  33  THR   B HB   1 
ATOM   4367 H  HG1  . THR   B 1 33  ? 43.432 -11.489 -14.028 1.00 16.82 ?  33  THR   B HG1  1 
ATOM   4368 H  HG21 . THR   B 1 33  ? 43.127 -10.336 -12.009 1.00 17.95 ?  33  THR   B HG21 1 
ATOM   4369 H  HG22 . THR   B 1 33  ? 43.687 -10.994 -10.689 1.00 17.95 ?  33  THR   B HG22 1 
ATOM   4370 H  HG23 . THR   B 1 33  ? 44.667 -10.247 -11.678 1.00 17.95 ?  33  THR   B HG23 1 
ATOM   4371 N  N    . VAL   B 1 34  ? 44.844 -14.269 -10.113 1.00 12.25 ?  34  VAL   B N    1 
ATOM   4372 C  CA   . VAL   B 1 34  ? 44.647 -14.663 -8.721  1.00 11.71 ?  34  VAL   B CA   1 
ATOM   4373 C  C    . VAL   B 1 34  ? 45.066 -16.114 -8.550  1.00 10.80 ?  34  VAL   B C    1 
ATOM   4374 O  O    . VAL   B 1 34  ? 44.541 -17.002 -9.234  1.00 11.47 ?  34  VAL   B O    1 
ATOM   4375 C  CB   . VAL   B 1 34  ? 43.174 -14.520 -8.284  1.00 12.46 ?  34  VAL   B CB   1 
ATOM   4376 C  CG1  . VAL   B 1 34  ? 43.002 -14.969 -6.842  1.00 12.96 ?  34  VAL   B CG1  1 
ATOM   4377 C  CG2  . VAL   B 1 34  ? 42.679 -13.095 -8.479  1.00 13.26 ?  34  VAL   B CG2  1 
ATOM   4378 H  H    . VAL   B 1 34  ? 44.580 -14.861 -10.681 1.00 14.67 ?  34  VAL   B H    1 
ATOM   4379 H  HA   . VAL   B 1 34  ? 45.197 -14.110 -8.143  1.00 14.03 ?  34  VAL   B HA   1 
ATOM   4380 H  HB   . VAL   B 1 34  ? 42.628 -15.095 -8.839  1.00 14.93 ?  34  VAL   B HB   1 
ATOM   4381 H  HG11 . VAL   B 1 34  ? 42.149 -14.644 -6.509  1.00 15.53 ?  34  VAL   B HG11 1 
ATOM   4382 H  HG12 . VAL   B 1 34  ? 43.020 -15.938 -6.805  1.00 15.53 ?  34  VAL   B HG12 1 
ATOM   4383 H  HG13 . VAL   B 1 34  ? 43.723 -14.602 -6.306  1.00 15.53 ?  34  VAL   B HG13 1 
ATOM   4384 H  HG21 . VAL   B 1 34  ? 41.760 -13.034 -8.170  1.00 15.89 ?  34  VAL   B HG21 1 
ATOM   4385 H  HG22 . VAL   B 1 34  ? 43.240 -12.490 -7.971  1.00 15.89 ?  34  VAL   B HG22 1 
ATOM   4386 H  HG23 . VAL   B 1 34  ? 42.722 -12.872 -9.424  1.00 15.89 ?  34  VAL   B HG23 1 
ATOM   4387 N  N    . VAL   B 1 35  ? 45.973 -16.365 -7.610  1.00 10.32 ?  35  VAL   B N    1 
ATOM   4388 C  CA   . VAL   B 1 35  ? 46.202 -17.710 -7.090  1.00 10.14 ?  35  VAL   B CA   1 
ATOM   4389 C  C    . VAL   B 1 35  ? 45.665 -17.765 -5.670  1.00 9.88  ?  35  VAL   B C    1 
ATOM   4390 O  O    . VAL   B 1 35  ? 45.884 -16.839 -4.882  1.00 10.41 ?  35  VAL   B O    1 
ATOM   4391 C  CB   . VAL   B 1 35  ? 47.683 -18.132 -7.168  1.00 10.84 ?  35  VAL   B CB   1 
ATOM   4392 C  CG1  . VAL   B 1 35  ? 48.585 -17.291 -6.249  1.00 11.55 ?  35  VAL   B CG1  1 
ATOM   4393 C  CG2  . VAL   B 1 35  ? 47.825 -19.629 -6.847  1.00 11.46 ?  35  VAL   B CG2  1 
ATOM   4394 H  H    . VAL   B 1 35  ? 46.475 -15.764 -7.254  1.00 12.36 ?  35  VAL   B H    1 
ATOM   4395 H  HA   . VAL   B 1 35  ? 45.686 -18.338 -7.617  1.00 12.15 ?  35  VAL   B HA   1 
ATOM   4396 H  HB   . VAL   B 1 35  ? 47.991 -18.008 -8.078  1.00 12.98 ?  35  VAL   B HB   1 
ATOM   4397 H  HG11 . VAL   B 1 35  ? 49.507 -17.520 -6.426  1.00 13.84 ?  35  VAL   B HG11 1 
ATOM   4398 H  HG12 . VAL   B 1 35  ? 48.425 -16.358 -6.431  1.00 13.84 ?  35  VAL   B HG12 1 
ATOM   4399 H  HG13 . VAL   B 1 35  ? 48.363 -17.496 -5.325  1.00 13.84 ?  35  VAL   B HG13 1 
ATOM   4400 H  HG21 . VAL   B 1 35  ? 48.747 -19.898 -6.953  1.00 13.73 ?  35  VAL   B HG21 1 
ATOM   4401 H  HG22 . VAL   B 1 35  ? 47.536 -19.792 -5.931  1.00 13.73 ?  35  VAL   B HG22 1 
ATOM   4402 H  HG23 . VAL   B 1 35  ? 47.260 -20.144 -7.456  1.00 13.73 ?  35  VAL   B HG23 1 
ATOM   4403 N  N    . VAL   B 1 36  ? 44.938 -18.840 -5.352  1.00 9.71  ?  36  VAL   B N    1 
ATOM   4404 C  CA   . VAL   B 1 36  ? 44.396 -19.038 -4.019  1.00 9.63  ?  36  VAL   B CA   1 
ATOM   4405 C  C    . VAL   B 1 36  ? 45.407 -19.799 -3.170  1.00 9.36  ?  36  VAL   B C    1 
ATOM   4406 O  O    . VAL   B 1 36  ? 45.949 -20.831 -3.593  1.00 10.64 ?  36  VAL   B O    1 
ATOM   4407 C  CB   . VAL   B 1 36  ? 43.062 -19.800 -4.091  1.00 10.10 ?  36  VAL   B CB   1 
ATOM   4408 C  CG1  . VAL   B 1 36  ? 42.555 -20.160 -2.698  1.00 10.71 ?  36  VAL   B CG1  1 
ATOM   4409 C  CG2  . VAL   B 1 36  ? 42.033 -18.974 -4.841  1.00 10.42 ?  36  VAL   B CG2  1 
ATOM   4410 H  H    . VAL   B 1 36  ? 44.752 -19.476 -5.901  1.00 11.63 ?  36  VAL   B H    1 
ATOM   4411 H  HA   . VAL   B 1 36  ? 44.226 -18.180 -3.605  1.00 11.54 ?  36  VAL   B HA   1 
ATOM   4412 H  HB   . VAL   B 1 36  ? 43.191 -20.629 -4.581  1.00 12.10 ?  36  VAL   B HB   1 
ATOM   4413 H  HG11 . VAL   B 1 36  ? 41.617 -20.401 -2.754  1.00 12.83 ?  36  VAL   B HG11 1 
ATOM   4414 H  HG12 . VAL   B 1 36  ? 43.069 -20.902 -2.352  1.00 12.83 ?  36  VAL   B HG12 1 
ATOM   4415 H  HG13 . VAL   B 1 36  ? 42.658 -19.384 -2.119  1.00 12.83 ?  36  VAL   B HG13 1 
ATOM   4416 H  HG21 . VAL   B 1 36  ? 41.188 -19.453 -4.855  1.00 12.48 ?  36  VAL   B HG21 1 
ATOM   4417 H  HG22 . VAL   B 1 36  ? 41.922 -18.123 -4.390  1.00 12.48 ?  36  VAL   B HG22 1 
ATOM   4418 H  HG23 . VAL   B 1 36  ? 42.343 -18.829 -5.749  1.00 12.48 ?  36  VAL   B HG23 1 
ATOM   4419 N  N    . ASN   B 1 37  ? 45.624 -19.311 -1.952  1.00 9.63  ?  37  ASN   B N    1 
ATOM   4420 C  CA   . ASN   B 1 37  ? 46.374 -20.035 -0.942  1.00 10.01 ?  37  ASN   B CA   1 
ATOM   4421 C  C    . ASN   B 1 37  ? 45.426 -20.705 0.042   1.00 10.15 ?  37  ASN   B C    1 
ATOM   4422 O  O    . ASN   B 1 37  ? 44.414 -20.128 0.449   1.00 10.58 ?  37  ASN   B O    1 
ATOM   4423 C  CB   . ASN   B 1 37  ? 47.292 -19.085 -0.179  1.00 10.01 ?  37  ASN   B CB   1 
ATOM   4424 C  CG   . ASN   B 1 37  ? 48.152 -19.799 0.829   1.00 10.51 ?  37  ASN   B CG   1 
ATOM   4425 O  OD1  . ASN   B 1 37  ? 48.494 -20.975 0.651   1.00 11.25 ?  37  ASN   B OD1  1 
ATOM   4426 N  ND2  . ASN   B 1 37  ? 48.503 -19.100 1.901   1.00 10.34 ?  37  ASN   B ND2  1 
ATOM   4427 H  H    . ASN   B 1 37  ? 45.342 -18.541 -1.677  1.00 11.53 ?  37  ASN   B H    1 
ATOM   4428 H  HA   . ASN   B 1 37  ? 46.910 -20.724 -1.356  1.00 11.99 ?  37  ASN   B HA   1 
ATOM   4429 H  HB2  . ASN   B 1 37  ? 47.878 -18.647 -0.811  1.00 11.99 ?  37  ASN   B HB2  1 
ATOM   4430 H  HB3  . ASN   B 1 37  ? 46.755 -18.432 0.294   1.00 11.99 ?  37  ASN   B HB3  1 
ATOM   4431 H  HD21 . ASN   B 1 37  ? 49.003 -19.460 2.504   1.00 12.38 ?  37  ASN   B HD21 1 
ATOM   4432 H  HD22 . ASN   B 1 37  ? 48.251 -18.289 1.991   1.00 12.38 ?  37  ASN   B HD22 1 
ATOM   4433 N  N    . ALA   B 1 38  ? 45.778 -21.935 0.422   1.00 10.48 ?  38  ALA   B N    1 
ATOM   4434 C  CA   . ALA   B 1 38  ? 45.120 -22.680 1.498   1.00 10.69 ?  38  ALA   B CA   1 
ATOM   4435 C  C    . ALA   B 1 38  ? 45.702 -22.190 2.820   1.00 10.35 ?  38  ALA   B C    1 
ATOM   4436 O  O    . ALA   B 1 38  ? 46.605 -22.792 3.408   1.00 11.39 ?  38  ALA   B O    1 
ATOM   4437 C  CB   . ALA   B 1 38  ? 45.342 -24.175 1.311   1.00 12.00 ?  38  ALA   B CB   1 
ATOM   4438 H  H    . ALA   B 1 38  ? 46.428 -22.373 0.072   1.00 12.56 ?  38  ALA   B H    1 
ATOM   4439 H  HA   . ALA   B 1 38  ? 44.166 -22.501 1.490   1.00 12.80 ?  38  ALA   B HA   1 
ATOM   4440 H  HB1  . ALA   B 1 38  ? 44.893 -24.656 2.032   1.00 14.38 ?  38  ALA   B HB1  1 
ATOM   4441 H  HB2  . ALA   B 1 38  ? 44.964 -24.446 0.458   1.00 14.38 ?  38  ALA   B HB2  1 
ATOM   4442 H  HB3  . ALA   B 1 38  ? 46.289 -24.364 1.331   1.00 14.38 ?  38  ALA   B HB3  1 
ATOM   4443 N  N    . ALA   B 1 39  ? 45.183 -21.051 3.277   1.00 10.41 ?  39  ALA   B N    1 
ATOM   4444 C  CA   . ALA   B 1 39  ? 45.735 -20.318 4.404   1.00 10.80 ?  39  ALA   B CA   1 
ATOM   4445 C  C    . ALA   B 1 39  ? 45.114 -20.755 5.729   1.00 10.86 ?  39  ALA   B C    1 
ATOM   4446 O  O    . ALA   B 1 39  ? 44.085 -21.432 5.783   1.00 11.87 ?  39  ALA   B O    1 
ATOM   4447 C  CB   . ALA   B 1 39  ? 45.501 -18.817 4.209   1.00 11.40 ?  39  ALA   B CB   1 
ATOM   4448 H  H    . ALA   B 1 39  ? 44.487 -20.676 2.932   1.00 12.46 ?  39  ALA   B H    1 
ATOM   4449 H  HA   . ALA   B 1 39  ? 46.688 -20.473 4.448   1.00 12.93 ?  39  ALA   B HA   1 
ATOM   4450 H  HB1  . ALA   B 1 39  ? 45.876 -18.338 4.966   1.00 13.66 ?  39  ALA   B HB1  1 
ATOM   4451 H  HB2  . ALA   B 1 39  ? 45.940 -18.532 3.390   1.00 13.66 ?  39  ALA   B HB2  1 
ATOM   4452 H  HB3  . ALA   B 1 39  ? 44.548 -18.647 4.148   1.00 13.66 ?  39  ALA   B HB3  1 
ATOM   4453 N  N    . ASN   B 1 40  ? 45.759 -20.330 6.813   1.00 11.36 ?  40  ASN   B N    1 
ATOM   4454 C  CA   . ASN   B 1 40  ? 45.198 -20.382 8.152   1.00 12.12 ?  40  ASN   B CA   1 
ATOM   4455 C  C    . ASN   B 1 40  ? 45.017 -18.955 8.677   1.00 11.56 ?  40  ASN   B C    1 
ATOM   4456 O  O    . ASN   B 1 40  ? 45.429 -17.976 8.047   1.00 11.81 ?  40  ASN   B O    1 
ATOM   4457 C  CB   . ASN   B 1 40  ? 46.045 -21.258 9.092   1.00 13.03 ?  40  ASN   B CB   1 
ATOM   4458 C  CG   . ASN   B 1 40  ? 47.501 -20.853 9.123   1.00 14.19 ?  40  ASN   B CG   1 
ATOM   4459 O  OD1  . ASN   B 1 40  ? 47.820 -19.672 9.183   1.00 16.02 ?  40  ASN   B OD1  1 
ATOM   4460 N  ND2  . ASN   B 1 40  ? 48.391 -21.829 9.088   1.00 14.22 ?  40  ASN   B ND2  1 
ATOM   4461 H  H    . ASN   B 1 40  ? 46.552 -19.999 6.790   1.00 13.61 ?  40  ASN   B H    1 
ATOM   4462 H  HA   . ASN   B 1 40  ? 44.316 -20.781 8.103   1.00 14.52 ?  40  ASN   B HA   1 
ATOM   4463 H  HB2  . ASN   B 1 40  ? 45.693 -21.185 9.993   1.00 15.61 ?  40  ASN   B HB2  1 
ATOM   4464 H  HB3  . ASN   B 1 40  ? 45.998 -22.178 8.791   1.00 15.61 ?  40  ASN   B HB3  1 
ATOM   4465 H  HD21 . ASN   B 1 40  ? 49.231 -21.647 9.106   1.00 17.05 ?  40  ASN   B HD21 1 
ATOM   4466 H  HD22 . ASN   B 1 40  ? 48.129 -22.647 9.046   1.00 17.05 ?  40  ASN   B HD22 1 
ATOM   4467 N  N    . VAL   B 1 41  ? 44.369 -18.833 9.837   1.00 12.32 ?  41  VAL   B N    1 
ATOM   4468 C  CA   . VAL   B 1 41  ? 43.906 -17.519 10.284  1.00 13.00 ?  41  VAL   B CA   1 
ATOM   4469 C  C    . VAL   B 1 41  ? 45.056 -16.563 10.574  1.00 12.95 ?  41  VAL   B C    1 
ATOM   4470 O  O    . VAL   B 1 41  ? 44.877 -15.344 10.485  1.00 13.13 ?  41  VAL   B O    1 
ATOM   4471 C  CB   . VAL   B 1 41  ? 42.940 -17.607 11.481  1.00 14.66 ?  41  VAL   B CB   1 
ATOM   4472 C  CG1  . VAL   B 1 41  ? 41.637 -18.280 11.076  1.00 14.90 ?  41  VAL   B CG1  1 
ATOM   4473 C  CG2  . VAL   B 1 41  ? 43.595 -18.308 12.660  1.00 15.53 ?  41  VAL   B CG2  1 
ATOM   4474 H  H    . VAL   B 1 41  ? 44.194 -19.480 10.371  1.00 14.76 ?  41  VAL   B H    1 
ATOM   4475 H  HA   . VAL   B 1 41  ? 43.402 -17.125 9.558   1.00 15.58 ?  41  VAL   B HA   1 
ATOM   4476 H  HB   . VAL   B 1 41  ? 42.719 -16.708 11.767  1.00 17.57 ?  41  VAL   B HB   1 
ATOM   4477 H  HG11 . VAL   B 1 41  ? 41.036 -18.294 11.839  1.00 17.86 ?  41  VAL   B HG11 1 
ATOM   4478 H  HG12 . VAL   B 1 41  ? 41.236 -17.782 10.348  1.00 17.86 ?  41  VAL   B HG12 1 
ATOM   4479 H  HG13 . VAL   B 1 41  ? 41.826 -19.189 10.792  1.00 17.86 ?  41  VAL   B HG13 1 
ATOM   4480 H  HG21 . VAL   B 1 41  ? 42.973 -18.325 13.401  1.00 18.61 ?  41  VAL   B HG21 1 
ATOM   4481 H  HG22 . VAL   B 1 41  ? 43.823 -19.216 12.400  1.00 18.61 ?  41  VAL   B HG22 1 
ATOM   4482 H  HG23 . VAL   B 1 41  ? 44.397 -17.824 12.907  1.00 18.61 ?  41  VAL   B HG23 1 
ATOM   4483 N  N    . TYR   B 1 42  ? 46.226 -17.072 10.958  1.00 12.94 ?  42  TYR   B N    1 
ATOM   4484 C  CA   . TYR   B 1 42  ? 47.375 -16.219 11.228  1.00 13.25 ?  42  TYR   B CA   1 
ATOM   4485 C  C    . TYR   B 1 42  ? 48.343 -16.156 10.050  1.00 12.67 ?  42  TYR   B C    1 
ATOM   4486 O  O    . TYR   B 1 42  ? 49.437 -15.594 10.184  1.00 13.91 ?  42  TYR   B O    1 
ATOM   4487 C  CB   . TYR   B 1 42  ? 48.064 -16.634 12.533  1.00 15.12 ?  42  TYR   B CB   1 
ATOM   4488 C  CG   . TYR   B 1 42  ? 47.473 -15.945 13.760  1.00 15.25 ?  42  TYR   B CG   1 
ATOM   4489 C  CD1  . TYR   B 1 42  ? 47.685 -14.591 13.975  1.00 14.60 ?  42  TYR   B CD1  1 
ATOM   4490 C  CD2  . TYR   B 1 42  ? 46.705 -16.638 14.687  1.00 16.53 ?  42  TYR   B CD2  1 
ATOM   4491 C  CE1  . TYR   B 1 42  ? 47.161 -13.944 15.071  1.00 15.42 ?  42  TYR   B CE1  1 
ATOM   4492 C  CE2  . TYR   B 1 42  ? 46.176 -15.994 15.799  1.00 17.08 ?  42  TYR   B CE2  1 
ATOM   4493 C  CZ   . TYR   B 1 42  ? 46.409 -14.640 15.982  1.00 17.30 ?  42  TYR   B CZ   1 
ATOM   4494 O  OH   . TYR   B 1 42  ? 45.901 -13.967 17.077  1.00 19.79 ?  42  TYR   B OH   1 
ATOM   4495 H  H    . TYR   B 1 42  ? 46.375 -17.916 11.061  1.00 15.50 ?  42  TYR   B H    1 
ATOM   4496 H  HA   . TYR   B 1 42  ? 47.047 -15.321 11.363  1.00 15.87 ?  42  TYR   B HA   1 
ATOM   4497 H  HB2  . TYR   B 1 42  ? 47.970 -17.592 12.655  1.00 18.13 ?  42  TYR   B HB2  1 
ATOM   4498 H  HB3  . TYR   B 1 42  ? 49.004 -16.397 12.483  1.00 18.13 ?  42  TYR   B HB3  1 
ATOM   4499 H  HD1  . TYR   B 1 42  ? 48.197 -14.109 13.359  1.00 17.50 ?  42  TYR   B HD1  1 
ATOM   4500 H  HD2  . TYR   B 1 42  ? 46.548 -17.550 14.562  1.00 19.82 ?  42  TYR   B HD2  1 
ATOM   4501 H  HE1  . TYR   B 1 42  ? 47.320 -13.036 15.191  1.00 18.48 ?  42  TYR   B HE1  1 
ATOM   4502 H  HE2  . TYR   B 1 42  ? 45.662 -16.470 16.411  1.00 20.47 ?  42  TYR   B HE2  1 
ATOM   4503 H  HH   . TYR   B 1 42  ? 46.123 -13.162 17.042  1.00 23.72 ?  42  TYR   B HH   1 
ATOM   4504 N  N    . LEU   B 1 43  ? 47.944 -16.672 8.891   1.00 11.78 ?  43  LEU   B N    1 
ATOM   4505 C  CA   . LEU   B 1 43  ? 48.753 -16.603 7.681   1.00 11.53 ?  43  LEU   B CA   1 
ATOM   4506 C  C    . LEU   B 1 43  ? 50.166 -17.108 7.938   1.00 11.63 ?  43  LEU   B C    1 
ATOM   4507 O  O    . LEU   B 1 43  ? 51.147 -16.511 7.493   1.00 12.57 ?  43  LEU   B O    1 
ATOM   4508 C  CB   . LEU   B 1 43  ? 48.770 -15.199 7.073   1.00 11.74 ?  43  LEU   B CB   1 
ATOM   4509 C  CG   . LEU   B 1 43  ? 47.419 -14.579 6.701   1.00 12.17 ?  43  LEU   B CG   1 
ATOM   4510 C  CD1  . LEU   B 1 43  ? 47.633 -13.191 6.098   1.00 13.34 ?  43  LEU   B CD1  1 
ATOM   4511 C  CD2  . LEU   B 1 43  ? 46.637 -15.484 5.748   1.00 12.37 ?  43  LEU   B CD2  1 
ATOM   4512 H  H    . LEU   B 1 43  ? 47.199 -17.086 8.779   1.00 14.11 ?  43  LEU   B H    1 
ATOM   4513 H  HA   . LEU   B 1 43  ? 48.356 -17.195 7.018   1.00 13.82 ?  43  LEU   B HA   1 
ATOM   4514 H  HB2  . LEU   B 1 43  ? 49.193 -14.606 7.708   1.00 14.07 ?  43  LEU   B HB2  1 
ATOM   4515 H  HB3  . LEU   B 1 43  ? 49.298 -15.234 6.261   1.00 14.07 ?  43  LEU   B HB3  1 
ATOM   4516 H  HG   . LEU   B 1 43  ? 46.893 -14.470 7.508   1.00 14.58 ?  43  LEU   B HG   1 
ATOM   4517 H  HD11 . LEU   B 1 43  ? 46.770 -12.810 5.869   1.00 15.98 ?  43  LEU   B HD11 1 
ATOM   4518 H  HD12 . LEU   B 1 43  ? 48.080 -12.628 6.750   1.00 15.98 ?  43  LEU   B HD12 1 
ATOM   4519 H  HD13 . LEU   B 1 43  ? 48.180 -13.273 5.301   1.00 15.98 ?  43  LEU   B HD13 1 
ATOM   4520 H  HD21 . LEU   B 1 43  ? 45.837 -15.017 5.457   1.00 14.83 ?  43  LEU   B HD21 1 
ATOM   4521 H  HD22 . LEU   B 1 43  ? 47.193 -15.698 4.986   1.00 14.83 ?  43  LEU   B HD22 1 
ATOM   4522 H  HD23 . LEU   B 1 43  ? 46.390 -16.297 6.219   1.00 14.83 ?  43  LEU   B HD23 1 
ATOM   4523 N  N    . LYS   B 1 44  ? 50.266 -18.229 8.655   1.00 11.88 ?  44  LYS   B N    1 
ATOM   4524 C  CA   . LYS   B 1 44  ? 51.534 -18.906 8.897   1.00 12.76 ?  44  LYS   B CA   1 
ATOM   4525 C  C    . LYS   B 1 44  ? 51.655 -20.028 7.874   1.00 12.30 ?  44  LYS   B C    1 
ATOM   4526 O  O    . LYS   B 1 44  ? 50.963 -21.047 7.966   1.00 13.50 ?  44  LYS   B O    1 
ATOM   4527 C  CB   . LYS   B 1 44  ? 51.594 -19.412 10.336  1.00 14.56 ?  44  LYS   B CB   1 
ATOM   4528 C  CG   . LYS   B 1 44  ? 51.797 -18.295 11.349  1.00 17.15 ?  44  LYS   B CG   1 
ATOM   4529 C  CD   . LYS   B 1 44  ? 52.986 -17.428 10.922  1.00 20.26 ?  44  LYS   B CD   1 
ATOM   4530 C  CE   . LYS   B 1 44  ? 53.547 -16.588 12.037  1.00 22.93 ?  44  LYS   B CE   1 
ATOM   4531 N  NZ   . LYS   B 1 44  ? 54.705 -15.770 11.607  1.00 24.08 ?  44  LYS   B NZ   1 
ATOM   4532 H  H    . LYS   B 1 44  ? 49.593 -18.618 9.020   1.00 14.23 ?  44  LYS   B H    1 
ATOM   4533 H  HA   . LYS   B 1 44  ? 52.265 -18.292 8.730   1.00 15.29 ?  44  LYS   B HA   1 
ATOM   4534 H  HB2  . LYS   B 1 44  ? 50.755 -19.854 10.551  1.00 17.46 ?  44  LYS   B HB2  1 
ATOM   4535 H  HB3  . LYS   B 1 44  ? 52.329 -20.033 10.426  1.00 17.46 ?  44  LYS   B HB3  1 
ATOM   4536 H  HG2  . LYS   B 1 44  ? 51.004 -17.744 11.392  1.00 20.56 ?  44  LYS   B HG2  1 
ATOM   4537 H  HG3  . LYS   B 1 44  ? 51.994 -18.683 12.221  1.00 20.56 ?  44  LYS   B HG3  1 
ATOM   4538 H  HD2  . LYS   B 1 44  ? 53.688 -18.013 10.580  1.00 24.29 ?  44  LYS   B HD2  1 
ATOM   4539 H  HD3  . LYS   B 1 44  ? 52.690 -16.828 10.218  1.00 24.29 ?  44  LYS   B HD3  1 
ATOM   4540 H  HE2  . LYS   B 1 44  ? 52.860 -15.972 12.309  1.00 27.50 ?  44  LYS   B HE2  1 
ATOM   4541 H  HE3  . LYS   B 1 44  ? 53.817 -17.162 12.774  1.00 27.50 ?  44  LYS   B HE3  1 
ATOM   4542 H  HZ1  . LYS   B 1 44  ? 54.998 -15.278 12.288  1.00 28.88 ?  44  LYS   B HZ1  1 
ATOM   4543 H  HZ2  . LYS   B 1 44  ? 55.364 -16.293 11.321  1.00 28.88 ?  44  LYS   B HZ2  1 
ATOM   4544 H  HZ3  . LYS   B 1 44  ? 54.460 -15.225 10.943  1.00 28.88 ?  44  LYS   B HZ3  1 
ATOM   4545 N  N    . HIS   B 1 45  ? 52.503 -19.808 6.872   1.00 12.00 ?  45  HIS   B N    1 
ATOM   4546 C  CA   . HIS   B 1 45  ? 52.530 -20.639 5.668   1.00 12.15 ?  45  HIS   B CA   1 
ATOM   4547 C  C    . HIS   B 1 45  ? 53.548 -21.764 5.834   1.00 14.21 ?  45  HIS   B C    1 
ATOM   4548 O  O    . HIS   B 1 45  ? 54.607 -21.788 5.213   1.00 16.49 ?  45  HIS   B O    1 
ATOM   4549 C  CB   . HIS   B 1 45  ? 52.846 -19.785 4.451   1.00 12.08 ?  45  HIS   B CB   1 
ATOM   4550 C  CG   . HIS   B 1 45  ? 51.972 -18.584 4.334   1.00 11.90 ?  45  HIS   B CG   1 
ATOM   4551 N  ND1  . HIS   B 1 45  ? 50.595 -18.665 4.293   1.00 11.84 ?  45  HIS   B ND1  1 
ATOM   4552 C  CD2  . HIS   B 1 45  ? 52.287 -17.271 4.260   1.00 12.55 ?  45  HIS   B CD2  1 
ATOM   4553 C  CE1  . HIS   B 1 45  ? 50.106 -17.442 4.184   1.00 11.73 ?  45  HIS   B CE1  1 
ATOM   4554 N  NE2  . HIS   B 1 45  ? 51.109 -16.580 4.164   1.00 12.24 ?  45  HIS   B NE2  1 
ATOM   4555 H  H    . HIS   B 1 45  ? 53.063 -19.158 6.856   1.00 14.37 ?  45  HIS   B H    1 
ATOM   4556 H  HA   . HIS   B 1 45  ? 51.652 -21.037 5.535   1.00 14.55 ?  45  HIS   B HA   1 
ATOM   4557 H  HB2  . HIS   B 1 45  ? 53.765 -19.486 4.506   1.00 14.48 ?  45  HIS   B HB2  1 
ATOM   4558 H  HB3  . HIS   B 1 45  ? 52.724 -20.327 3.649   1.00 14.48 ?  45  HIS   B HB3  1 
ATOM   4559 H  HD2  . HIS   B 1 45  ? 53.143 -16.905 4.274   1.00 15.03 ?  45  HIS   B HD2  1 
ATOM   4560 H  HE1  . HIS   B 1 45  ? 49.203 -17.228 4.118   1.00 14.05 ?  45  HIS   B HE1  1 
ATOM   4561 H  HE2  . HIS   B 1 45  ? 51.031 -15.726 4.104   1.00 14.67 ?  45  HIS   B HE2  1 
ATOM   4562 N  N    A GLY   B 1 46  ? 53.180 -22.732 6.671   0.72 15.05 ?  46  GLY   B N    1 
ATOM   4563 N  N    B GLY   B 1 46  ? 53.191 -22.714 6.692   0.28 14.99 ?  46  GLY   B N    1 
ATOM   4564 C  CA   A GLY   B 1 46  ? 54.100 -23.786 7.057   0.72 16.77 ?  46  GLY   B CA   1 
ATOM   4565 C  CA   B GLY   B 1 46  ? 54.104 -23.783 7.035   0.28 16.07 ?  46  GLY   B CA   1 
ATOM   4566 C  C    A GLY   B 1 46  ? 54.158 -25.006 6.158   0.72 18.30 ?  46  GLY   B C    1 
ATOM   4567 C  C    B GLY   B 1 46  ? 54.138 -24.922 6.037   0.28 17.13 ?  46  GLY   B C    1 
ATOM   4568 O  O    A GLY   B 1 46  ? 55.241 -25.435 5.749   0.72 21.03 ?  46  GLY   B O    1 
ATOM   4569 O  O    B GLY   B 1 46  ? 55.169 -25.180 5.410   0.28 17.72 ?  46  GLY   B O    1 
ATOM   4570 H  H    A GLY   B 1 46  ? 52.400 -22.785 7.041   0.72 18.03 ?  46  GLY   B H    1 
ATOM   4571 H  H    B GLY   B 1 46  ? 52.423 -22.755 7.091   0.28 17.97 ?  46  GLY   B H    1 
ATOM   4572 H  HA2  A GLY   B 1 46  ? 54.990 -23.409 7.109   0.72 20.11 ?  46  GLY   B HA2  1 
ATOM   4573 H  HA2  B GLY   B 1 46  ? 54.998 -23.417 7.105   0.28 19.26 ?  46  GLY   B HA2  1 
ATOM   4574 H  HA3  A GLY   B 1 46  ? 53.855 -24.097 7.942   0.72 20.11 ?  46  GLY   B HA3  1 
ATOM   4575 H  HA3  B GLY   B 1 46  ? 53.855 -24.141 7.901   0.28 19.26 ?  46  GLY   B HA3  1 
ATOM   4576 N  N    . GLY   B 1 47  ? 53.006 -25.603 5.864   1.00 17.78 ?  47  GLY   B N    1 
ATOM   4577 C  CA   . GLY   B 1 47  ? 52.959 -26.862 5.149   1.00 15.95 ?  47  GLY   B CA   1 
ATOM   4578 C  C    . GLY   B 1 47  ? 52.034 -26.840 3.947   1.00 13.86 ?  47  GLY   B C    1 
ATOM   4579 O  O    . GLY   B 1 47  ? 51.377 -25.841 3.656   1.00 13.74 ?  47  GLY   B O    1 
ATOM   4580 H  H    A GLY   B 1 47  ? 52.232 -25.305 6.096   0.72 21.31 ?  47  GLY   B H    1 
ATOM   4581 H  H    B GLY   B 1 47  ? 52.240 -25.346 6.163   0.28 21.31 ?  47  GLY   B H    1 
ATOM   4582 H  HA2  . GLY   B 1 47  ? 53.848 -27.095 4.839   1.00 19.12 ?  47  GLY   B HA2  1 
ATOM   4583 H  HA3  . GLY   B 1 47  ? 52.659 -27.559 5.754   1.00 19.12 ?  47  GLY   B HA3  1 
ATOM   4584 N  N    . GLY   B 1 48  ? 51.991 -27.978 3.258   1.00 12.90 ?  48  GLY   B N    1 
ATOM   4585 C  CA   . GLY   B 1 48  ? 51.058 -28.122 2.158   1.00 12.64 ?  48  GLY   B CA   1 
ATOM   4586 C  C    . GLY   B 1 48  ? 51.202 -27.018 1.136   1.00 12.04 ?  48  GLY   B C    1 
ATOM   4587 O  O    . GLY   B 1 48  ? 52.304 -26.553 0.829   1.00 12.72 ?  48  GLY   B O    1 
ATOM   4588 H  H    . GLY   B 1 48  ? 52.489 -28.657 3.403   1.00 15.45 ?  48  GLY   B H    1 
ATOM   4589 H  HA2  . GLY   B 1 48  ? 51.206 -28.974 1.720   1.00 15.15 ?  48  GLY   B HA2  1 
ATOM   4590 H  HA3  . GLY   B 1 48  ? 50.149 -28.106 2.499   1.00 15.15 ?  48  GLY   B HA3  1 
ATOM   4591 N  N    . VAL   B 1 49  ? 50.058 -26.595 0.595   1.00 12.06 ?  49  VAL   B N    1 
ATOM   4592 C  CA   . VAL   B 1 49  ? 50.037 -25.567 -0.443  1.00 12.03 ?  49  VAL   B CA   1 
ATOM   4593 C  C    . VAL   B 1 49  ? 50.693 -24.280 0.046   1.00 11.06 ?  49  VAL   B C    1 
ATOM   4594 O  O    . VAL   B 1 49  ? 51.479 -23.658 -0.675  1.00 12.02 ?  49  VAL   B O    1 
ATOM   4595 C  CB   . VAL   B 1 49  ? 48.592 -25.316 -0.916  1.00 13.27 ?  49  VAL   B CB   1 
ATOM   4596 C  CG1  . VAL   B 1 49  ? 48.523 -24.075 -1.797  1.00 13.39 ?  49  VAL   B CG1  1 
ATOM   4597 C  CG2  . VAL   B 1 49  ? 48.046 -26.530 -1.660  1.00 14.65 ?  49  VAL   B CG2  1 
ATOM   4598 H  H    . VAL   B 1 49  ? 49.273 -26.889 0.811   1.00 14.44 ?  49  VAL   B H    1 
ATOM   4599 H  HA   . VAL   B 1 49  ? 50.537 -25.885 -1.209  1.00 14.42 ?  49  VAL   B HA   1 
ATOM   4600 H  HB   . VAL   B 1 49  ? 48.024 -25.161 -0.146  1.00 15.90 ?  49  VAL   B HB   1 
ATOM   4601 H  HG11 . VAL   B 1 49  ? 47.693 -24.088 -2.303  1.00 16.04 ?  49  VAL   B HG11 1 
ATOM   4602 H  HG12 . VAL   B 1 49  ? 48.547 -23.281 -1.235  1.00 16.04 ?  49  VAL   B HG12 1 
ATOM   4603 H  HG13 . VAL   B 1 49  ? 49.277 -24.073 -2.406  1.00 16.04 ?  49  VAL   B HG13 1 
ATOM   4604 H  HG21 . VAL   B 1 49  ? 47.136 -26.348 -1.948  1.00 17.55 ?  49  VAL   B HG21 1 
ATOM   4605 H  HG22 . VAL   B 1 49  ? 48.606 -26.705 -2.435  1.00 17.55 ?  49  VAL   B HG22 1 
ATOM   4606 H  HG23 . VAL   B 1 49  ? 48.057 -27.295 -1.066  1.00 17.55 ?  49  VAL   B HG23 1 
ATOM   4607 N  N    . ALA   B 1 50  ? 50.343 -23.833 1.253   1.00 10.89 ?  50  ALA   B N    1 
ATOM   4608 C  CA   . ALA   B 1 50  ? 50.867 -22.557 1.730   1.00 10.85 ?  50  ALA   B CA   1 
ATOM   4609 C  C    . ALA   B 1 50  ? 52.387 -22.588 1.835   1.00 11.30 ?  50  ALA   B C    1 
ATOM   4610 O  O    . ALA   B 1 50  ? 53.067 -21.621 1.470   1.00 11.42 ?  50  ALA   B O    1 
ATOM   4611 C  CB   . ALA   B 1 50  ? 50.236 -22.196 3.072   1.00 11.18 ?  50  ALA   B CB   1 
ATOM   4612 H  H    . ALA   B 1 50  ? 49.816 -24.238 1.798   1.00 13.05 ?  50  ALA   B H    1 
ATOM   4613 H  HA   . ALA   B 1 50  ? 50.636 -21.867 1.096   1.00 13.00 ?  50  ALA   B HA   1 
ATOM   4614 H  HB1  . ALA   B 1 50  ? 50.595 -21.344 3.372   1.00 13.39 ?  50  ALA   B HB1  1 
ATOM   4615 H  HB2  . ALA   B 1 50  ? 49.273 -22.121 2.958   1.00 13.39 ?  50  ALA   B HB2  1 
ATOM   4616 H  HB3  . ALA   B 1 50  ? 50.438 -22.887 3.719   1.00 13.39 ?  50  ALA   B HB3  1 
ATOM   4617 N  N    . GLY   B 1 51  ? 52.938 -23.681 2.354   1.00 11.86 ?  51  GLY   B N    1 
ATOM   4618 C  CA   . GLY   B 1 51  ? 54.382 -23.784 2.425   1.00 12.43 ?  51  GLY   B CA   1 
ATOM   4619 C  C    . GLY   B 1 51  ? 55.030 -23.733 1.057   1.00 12.29 ?  51  GLY   B C    1 
ATOM   4620 O  O    . GLY   B 1 51  ? 56.075 -23.100 0.877   1.00 13.23 ?  51  GLY   B O    1 
ATOM   4621 H  H    . GLY   B 1 51  ? 52.511 -24.360 2.664   1.00 14.21 ?  51  GLY   B H    1 
ATOM   4622 H  HA2  . GLY   B 1 51  ? 54.737 -23.054 2.955   1.00 14.89 ?  51  GLY   B HA2  1 
ATOM   4623 H  HA3  . GLY   B 1 51  ? 54.630 -24.621 2.851   1.00 14.89 ?  51  GLY   B HA3  1 
ATOM   4624 N  N    . ALA   B 1 52  ? 54.429 -24.405 0.076   1.00 11.79 ?  52  ALA   B N    1 
ATOM   4625 C  CA   . ALA   B 1 52  ? 54.984 -24.410 -1.270  1.00 12.39 ?  52  ALA   B CA   1 
ATOM   4626 C  C    . ALA   B 1 52  ? 54.906 -23.028 -1.914  1.00 11.82 ?  52  ALA   B C    1 
ATOM   4627 O  O    . ALA   B 1 52  ? 55.875 -22.573 -2.541  1.00 12.58 ?  52  ALA   B O    1 
ATOM   4628 C  CB   . ALA   B 1 52  ? 54.271 -25.451 -2.127  1.00 13.08 ?  52  ALA   B CB   1 
ATOM   4629 H  H    . ALA   B 1 52  ? 53.700 -24.856 0.162   1.00 14.12 ?  52  ALA   B H    1 
ATOM   4630 H  HA   . ALA   B 1 52  ? 55.919 -24.657 -1.219  1.00 14.85 ?  52  ALA   B HA   1 
ATOM   4631 H  HB1  . ALA   B 1 52  ? 54.658 -25.442 -3.019  1.00 15.68 ?  52  ALA   B HB1  1 
ATOM   4632 H  HB2  . ALA   B 1 52  ? 54.398 -26.327 -1.725  1.00 15.68 ?  52  ALA   B HB2  1 
ATOM   4633 H  HB3  . ALA   B 1 52  ? 53.330 -25.238 -2.171  1.00 15.68 ?  52  ALA   B HB3  1 
ATOM   4634 N  N    . LEU   B 1 53  ? 53.759 -22.354 -1.798  1.00 11.36 ?  53  LEU   B N    1 
ATOM   4635 C  CA   . LEU   B 1 53  ? 53.650 -21.016 -2.373  1.00 11.31 ?  53  LEU   B CA   1 
ATOM   4636 C  C    . LEU   B 1 53  ? 54.658 -20.074 -1.725  1.00 11.37 ?  53  LEU   B C    1 
ATOM   4637 O  O    . LEU   B 1 53  ? 55.365 -19.327 -2.411  1.00 12.23 ?  53  LEU   B O    1 
ATOM   4638 C  CB   . LEU   B 1 53  ? 52.231 -20.466 -2.205  1.00 11.90 ?  53  LEU   B CB   1 
ATOM   4639 C  CG   . LEU   B 1 53  ? 51.091 -21.196 -2.918  1.00 12.33 ?  53  LEU   B CG   1 
ATOM   4640 C  CD1  . LEU   B 1 53  ? 49.762 -20.573 -2.561  1.00 13.54 ?  53  LEU   B CD1  1 
ATOM   4641 C  CD2  . LEU   B 1 53  ? 51.290 -21.201 -4.428  1.00 13.85 ?  53  LEU   B CD2  1 
ATOM   4642 H  H    . LEU   B 1 53  ? 53.052 -22.637 -1.404  1.00 13.61 ?  53  LEU   B H    1 
ATOM   4643 H  HA   . LEU   B 1 53  ? 53.849 -21.061 -3.325  1.00 13.55 ?  53  LEU   B HA   1 
ATOM   4644 H  HB2  . LEU   B 1 53  ? 52.023 -20.472 -1.261  1.00 14.26 ?  53  LEU   B HB2  1 
ATOM   4645 H  HB3  . LEU   B 1 53  ? 52.227 -19.553 -2.529  1.00 14.26 ?  53  LEU   B HB3  1 
ATOM   4646 H  HG   . LEU   B 1 53  ? 51.074 -22.115 -2.618  1.00 14.77 ?  53  LEU   B HG   1 
ATOM   4647 H  HD11 . LEU   B 1 53  ? 49.054 -21.055 -3.019  1.00 16.23 ?  53  LEU   B HD11 1 
ATOM   4648 H  HD12 . LEU   B 1 53  ? 49.632 -20.638 -1.600  1.00 16.23 ?  53  LEU   B HD12 1 
ATOM   4649 H  HD13 . LEU   B 1 53  ? 49.761 -19.645 -2.833  1.00 16.23 ?  53  LEU   B HD13 1 
ATOM   4650 H  HD21 . LEU   B 1 53  ? 50.570 -21.710 -4.837  1.00 16.60 ?  53  LEU   B HD21 1 
ATOM   4651 H  HD22 . LEU   B 1 53  ? 51.273 -20.290 -4.754  1.00 16.60 ?  53  LEU   B HD22 1 
ATOM   4652 H  HD23 . LEU   B 1 53  ? 52.141 -21.616 -4.635  1.00 16.60 ?  53  LEU   B HD23 1 
ATOM   4653 N  N    . ASN   B 1 54  ? 54.747 -20.102 -0.398  1.00 11.24 ?  54  ASN   B N    1 
ATOM   4654 C  CA   . ASN   B 1 54  ? 55.662 -19.190 0.274   1.00 11.84 ?  54  ASN   B CA   1 
ATOM   4655 C  C    . ASN   B 1 54  ? 57.106 -19.469 -0.120  1.00 12.30 ?  54  ASN   B C    1 
ATOM   4656 O  O    . ASN   B 1 54  ? 57.883 -18.535 -0.350  1.00 12.68 ?  54  ASN   B O    1 
ATOM   4657 C  CB   . ASN   B 1 54  ? 55.504 -19.272 1.784   1.00 12.55 ?  54  ASN   B CB   1 
ATOM   4658 C  CG   . ASN   B 1 54  ? 56.481 -18.357 2.498   1.00 13.00 ?  54  ASN   B CG   1 
ATOM   4659 O  OD1  . ASN   B 1 54  ? 56.500 -17.145 2.255   1.00 13.14 ?  54  ASN   B OD1  1 
ATOM   4660 N  ND2  . ASN   B 1 54  ? 57.324 -18.931 3.351   1.00 14.52 ?  54  ASN   B ND2  1 
ATOM   4661 H  H    . ASN   B 1 54  ? 54.308 -20.628 0.117   1.00 13.47 ?  54  ASN   B H    1 
ATOM   4662 H  HA   . ASN   B 1 54  ? 55.449 -18.283 0.001   1.00 14.18 ?  54  ASN   B HA   1 
ATOM   4663 H  HB2  . ASN   B 1 54  ? 54.605 -19.004 2.027   1.00 15.04 ?  54  ASN   B HB2  1 
ATOM   4664 H  HB3  . ASN   B 1 54  ? 55.675 -20.181 2.073   1.00 15.04 ?  54  ASN   B HB3  1 
ATOM   4665 H  HD21 . ASN   B 1 54  ? 57.903 -18.452 3.774   1.00 17.40 ?  54  ASN   B HD21 1 
ATOM   4666 H  HD22 . ASN   B 1 54  ? 57.294 -19.780 3.484   1.00 17.40 ?  54  ASN   B HD22 1 
ATOM   4667 N  N    . LYS   B 1 55  ? 57.491 -20.746 -0.179  1.00 12.96 ?  55  LYS   B N    1 
ATOM   4668 C  CA   . LYS   B 1 55  ? 58.844 -21.092 -0.600  1.00 13.81 ?  55  LYS   B CA   1 
ATOM   4669 C  C    . LYS   B 1 55  ? 59.137 -20.555 -1.994  1.00 13.51 ?  55  LYS   B C    1 
ATOM   4670 O  O    . LYS   B 1 55  ? 60.235 -20.048 -2.252  1.00 14.27 ?  55  LYS   B O    1 
ATOM   4671 C  CB   . LYS   B 1 55  ? 59.030 -22.608 -0.552  1.00 15.91 ?  55  LYS   B CB   1 
ATOM   4672 C  CG   . LYS   B 1 55  ? 60.389 -23.083 -1.023  1.00 19.38 ?  55  LYS   B CG   1 
ATOM   4673 C  CD   . LYS   B 1 55  ? 60.554 -24.580 -0.815  1.00 22.63 ?  55  LYS   B CD   1 
ATOM   4674 C  CE   . LYS   B 1 55  ? 60.689 -24.935 0.665   1.00 25.51 ?  55  LYS   B CE   1 
ATOM   4675 N  NZ   . LYS   B 1 55  ? 61.032 -26.364 0.871   1.00 26.83 ?  55  LYS   B NZ   1 
ATOM   4676 H  H    . LYS   B 1 55  ? 56.987 -21.415 0.011   1.00 15.53 ?  55  LYS   B H    1 
ATOM   4677 H  HA   . LYS   B 1 55  ? 59.475 -20.690 0.013   1.00 16.55 ?  55  LYS   B HA   1 
ATOM   4678 H  HB2  . LYS   B 1 55  ? 58.910 -22.898 0.367   1.00 19.07 ?  55  LYS   B HB2  1 
ATOM   4679 H  HB3  . LYS   B 1 55  ? 58.358 -23.021 -1.115  1.00 19.07 ?  55  LYS   B HB3  1 
ATOM   4680 H  HG2  . LYS   B 1 55  ? 60.485 -22.897 -1.970  1.00 23.24 ?  55  LYS   B HG2  1 
ATOM   4681 H  HG3  . LYS   B 1 55  ? 61.081 -22.626 -0.520  1.00 23.24 ?  55  LYS   B HG3  1 
ATOM   4682 H  HD2  . LYS   B 1 55  ? 59.777 -25.044 -1.166  1.00 27.13 ?  55  LYS   B HD2  1 
ATOM   4683 H  HD3  . LYS   B 1 55  ? 61.357 -24.884 -1.269  1.00 27.13 ?  55  LYS   B HD3  1 
ATOM   4684 H  HE2  . LYS   B 1 55  ? 61.391 -24.389 1.056   1.00 30.59 ?  55  LYS   B HE2  1 
ATOM   4685 H  HE3  . LYS   B 1 55  ? 59.844 -24.756 1.111   1.00 30.59 ?  55  LYS   B HE3  1 
ATOM   4686 H  HZ1  . LYS   B 1 55  ? 61.069 -26.542 1.743   1.00 32.18 ?  55  LYS   B HZ1  1 
ATOM   4687 H  HZ2  . LYS   B 1 55  ? 60.411 -26.879 0.496   1.00 32.18 ?  55  LYS   B HZ2  1 
ATOM   4688 H  HZ3  . LYS   B 1 55  ? 61.820 -26.542 0.504   1.00 32.18 ?  55  LYS   B HZ3  1 
ATOM   4689 N  N    . ALA   B 1 56  ? 58.165 -20.643 -2.906  1.00 13.13 ?  56  ALA   B N    1 
ATOM   4690 C  CA   . ALA   B 1 56  ? 58.387 -20.142 -4.256  1.00 13.90 ?  56  ALA   B CA   1 
ATOM   4691 C  C    . ALA   B 1 56  ? 58.671 -18.645 -4.256  1.00 13.70 ?  56  ALA   B C    1 
ATOM   4692 O  O    . ALA   B 1 56  ? 59.402 -18.151 -5.123  1.00 14.87 ?  56  ALA   B O    1 
ATOM   4693 C  CB   . ALA   B 1 56  ? 57.187 -20.468 -5.145  1.00 14.63 ?  56  ALA   B CB   1 
ATOM   4694 H  H    . ALA   B 1 56  ? 57.380 -20.972 -2.766  1.00 15.73 ?  56  ALA   B H    1 
ATOM   4695 H  HA   . ALA   B 1 56  ? 59.159 -20.585 -4.631  1.00 16.65 ?  56  ALA   B HA   1 
ATOM   4696 H  HB1  . ALA   B 1 56  ? 57.354 -20.134 -6.042  1.00 17.53 ?  56  ALA   B HB1  1 
ATOM   4697 H  HB2  . ALA   B 1 56  ? 57.067 -21.432 -5.172  1.00 17.53 ?  56  ALA   B HB2  1 
ATOM   4698 H  HB3  . ALA   B 1 56  ? 56.393 -20.048 -4.780  1.00 17.53 ?  56  ALA   B HB3  1 
ATOM   4699 N  N    . THR   B 1 57  ? 58.104 -17.908 -3.299  1.00 13.48 ?  57  THR   B N    1 
ATOM   4700 C  CA   . THR   B 1 57  ? 58.345 -16.475 -3.178  1.00 13.46 ?  57  THR   B CA   1 
ATOM   4701 C  C    . THR   B 1 57  ? 59.595 -16.147 -2.367  1.00 14.21 ?  57  THR   B C    1 
ATOM   4702 O  O    . THR   B 1 57  ? 59.839 -14.970 -2.072  1.00 14.67 ?  57  THR   B O    1 
ATOM   4703 C  CB   . THR   B 1 57  ? 57.141 -15.747 -2.550  1.00 12.69 ?  57  THR   B CB   1 
ATOM   4704 O  OG1  . THR   B 1 57  ? 57.116 -15.956 -1.130  1.00 13.19 ?  57  THR   B OG1  1 
ATOM   4705 C  CG2  . THR   B 1 57  ? 55.825 -16.174 -3.187  1.00 12.66 ?  57  THR   B CG2  1 
ATOM   4706 H  H    . THR   B 1 57  ? 57.562 -18.220 -2.704  1.00 16.15 ?  57  THR   B H    1 
ATOM   4707 H  HA   . THR   B 1 57  ? 58.469 -16.111 -4.069  1.00 16.13 ?  57  THR   B HA   1 
ATOM   4708 H  HB   . THR   B 1 57  ? 57.243 -14.797 -2.719  1.00 15.20 ?  57  THR   B HB   1 
ATOM   4709 H  HG1  . THR   B 1 57  ? 57.046 -16.777 -0.967  1.00 15.80 ?  57  THR   B HG1  1 
ATOM   4710 H  HG21 . THR   B 1 57  ? 55.103 -15.619 -2.861  1.00 15.17 ?  57  THR   B HG21 1 
ATOM   4711 H  HG22 . THR   B 1 57  ? 55.880 -16.089 -4.153  1.00 15.17 ?  57  THR   B HG22 1 
ATOM   4712 H  HG23 . THR   B 1 57  ? 55.636 -17.100 -2.966  1.00 15.17 ?  57  THR   B HG23 1 
ATOM   4713 N  N    . ASN   B 1 58  ? 60.388 -17.151 -2.001  1.00 15.08 ?  58  ASN   B N    1 
ATOM   4714 C  CA   . ASN   B 1 58  ? 61.586 -16.935 -1.194  1.00 18.22 ?  58  ASN   B CA   1 
ATOM   4715 C  C    . ASN   B 1 58  ? 61.252 -16.217 0.114   1.00 15.83 ?  58  ASN   B C    1 
ATOM   4716 O  O    . ASN   B 1 58  ? 61.991 -15.342 0.576   1.00 16.32 ?  58  ASN   B O    1 
ATOM   4717 C  CB   . ASN   B 1 58  ? 62.677 -16.197 -1.978  1.00 26.15 ?  58  ASN   B CB   1 
ATOM   4718 C  CG   . ASN   B 1 58  ? 64.050 -16.362 -1.358  1.00 34.79 ?  58  ASN   B CG   1 
ATOM   4719 O  OD1  . ASN   B 1 58  ? 64.336 -17.373 -0.718  1.00 37.37 ?  58  ASN   B OD1  1 
ATOM   4720 N  ND2  . ASN   B 1 58  ? 64.907 -15.364 -1.542  1.00 40.18 ?  58  ASN   B ND2  1 
ATOM   4721 H  H    . ASN   B 1 58  ? 60.249 -17.978 -2.207  1.00 18.08 ?  58  ASN   B H    1 
ATOM   4722 H  HA   . ASN   B 1 58  ? 61.946 -17.808 -0.965  1.00 21.84 ?  58  ASN   B HA   1 
ATOM   4723 H  HB2  . ASN   B 1 58  ? 62.711 -16.549 -2.885  1.00 31.36 ?  58  ASN   B HB2  1 
ATOM   4724 H  HB3  . ASN   B 1 58  ? 62.469 -15.252 -1.998  1.00 31.36 ?  58  ASN   B HB3  1 
ATOM   4725 H  HD21 . ASN   B 1 58  ? 65.700 -15.410 -1.211  1.00 48.19 ?  58  ASN   B HD21 1 
ATOM   4726 H  HD22 . ASN   B 1 58  ? 64.670 -14.671 -1.993  1.00 48.19 ?  58  ASN   B HD22 1 
ATOM   4727 N  N    . ASN   B 1 59  ? 60.126 -16.597 0.719   1.00 14.93 ?  59  ASN   B N    1 
ATOM   4728 C  CA   . ASN   B 1 59  ? 59.651 -16.125 2.022   1.00 14.69 ?  59  ASN   B CA   1 
ATOM   4729 C  C    . ASN   B 1 59  ? 59.048 -14.723 1.968   1.00 14.16 ?  59  ASN   B C    1 
ATOM   4730 O  O    . ASN   B 1 59  ? 58.617 -14.214 3.014   1.00 14.33 ?  59  ASN   B O    1 
ATOM   4731 C  CB   . ASN   B 1 59  ? 60.722 -16.181 3.125   1.00 15.85 ?  59  ASN   B CB   1 
ATOM   4732 C  CG   . ASN   B 1 59  ? 60.131 -16.361 4.508   1.00 16.94 ?  59  ASN   B CG   1 
ATOM   4733 O  OD1  . ASN   B 1 59  ? 59.305 -17.248 4.734   1.00 17.10 ?  59  ASN   B OD1  1 
ATOM   4734 N  ND2  . ASN   B 1 59  ? 60.552 -15.520 5.445   1.00 17.42 ?  59  ASN   B ND2  1 
ATOM   4735 H  H    . ASN   B 1 59  ? 59.583 -17.173 0.371   1.00 17.89 ?  59  ASN   B H    1 
ATOM   4736 H  HA   . ASN   B 1 59  ? 58.943 -16.723 2.305   1.00 17.60 ?  59  ASN   B HA   1 
ATOM   4737 H  HB2  . ASN   B 1 59  ? 61.317 -16.930 2.961   1.00 19.00 ?  59  ASN   B HB2  1 
ATOM   4738 H  HB3  . ASN   B 1 59  ? 61.225 -15.353 3.128   1.00 19.00 ?  59  ASN   B HB3  1 
ATOM   4739 H  HD21 . ASN   B 1 59  ? 60.246 -15.582 6.248   1.00 20.89 ?  59  ASN   B HD21 1 
ATOM   4740 H  HD22 . ASN   B 1 59  ? 61.127 -14.912 5.252   1.00 20.89 ?  59  ASN   B HD22 1 
ATOM   4741 N  N    . ALA   B 1 60  ? 58.982 -14.082 0.797   1.00 13.81 ?  60  ALA   B N    1 
ATOM   4742 C  CA   . ALA   B 1 60  ? 58.394 -12.748 0.721   1.00 13.86 ?  60  ALA   B CA   1 
ATOM   4743 C  C    . ALA   B 1 60  ? 56.922 -12.772 1.112   1.00 12.92 ?  60  ALA   B C    1 
ATOM   4744 O  O    . ALA   B 1 60  ? 56.415 -11.825 1.727   1.00 13.45 ?  60  ALA   B O    1 
ATOM   4745 C  CB   . ALA   B 1 60  ? 58.565 -12.177 -0.685  1.00 15.07 ?  60  ALA   B CB   1 
ATOM   4746 H  H    . ALA   B 1 60  ? 59.273 -14.397 0.052   1.00 16.54 ?  60  ALA   B H    1 
ATOM   4747 H  HA   . ALA   B 1 60  ? 58.856 -12.167 1.342   1.00 16.61 ?  60  ALA   B HA   1 
ATOM   4748 H  HB1  . ALA   B 1 60  ? 58.170 -11.296 -0.716  1.00 18.06 ?  60  ALA   B HB1  1 
ATOM   4749 H  HB2  . ALA   B 1 60  ? 59.515 -12.125 -0.889  1.00 18.06 ?  60  ALA   B HB2  1 
ATOM   4750 H  HB3  . ALA   B 1 60  ? 58.126 -12.765 -1.320  1.00 18.06 ?  60  ALA   B HB3  1 
ATOM   4751 N  N    . MET   B 1 61  ? 56.217 -13.849 0.762   1.00 12.30 ?  61  MET   B N    1 
ATOM   4752 C  CA   . MET   B 1 61  ? 54.821 -13.974 1.157   1.00 11.89 ?  61  MET   B CA   1 
ATOM   4753 C  C    . MET   B 1 61  ? 54.683 -13.974 2.677   1.00 11.86 ?  61  MET   B C    1 
ATOM   4754 O  O    . MET   B 1 61  ? 53.782 -13.327 3.224   1.00 11.69 ?  61  MET   B O    1 
ATOM   4755 C  CB   . MET   B 1 61  ? 54.242 -15.248 0.536   1.00 11.90 ?  61  MET   B CB   1 
ATOM   4756 C  CG   . MET   B 1 61  ? 52.799 -15.539 0.947   1.00 11.63 ?  61  MET   B CG   1 
ATOM   4757 S  SD   . MET   B 1 61  ? 52.156 -17.040 0.181   1.00 12.17 ?  61  MET   B SD   1 
ATOM   4758 C  CE   . MET   B 1 61  ? 51.893 -16.455 -1.492  1.00 13.46 ?  61  MET   B CE   1 
ATOM   4759 H  H    . MET   B 1 61  ? 56.522 -14.519 0.307   1.00 14.73 ?  61  MET   B H    1 
ATOM   4760 H  HA   . MET   B 1 61  ? 54.325 -13.225 0.792   1.00 14.24 ?  61  MET   B HA   1 
ATOM   4761 H  HB2  . MET   B 1 61  ? 54.257 -15.166 -0.433  1.00 14.26 ?  61  MET   B HB2  1 
ATOM   4762 H  HB3  . MET   B 1 61  ? 54.782 -16.007 0.806   1.00 14.26 ?  61  MET   B HB3  1 
ATOM   4763 H  HG2  . MET   B 1 61  ? 52.756 -15.657 1.913   1.00 13.93 ?  61  MET   B HG2  1 
ATOM   4764 H  HG3  . MET   B 1 61  ? 52.233 -14.795 0.682   1.00 13.93 ?  61  MET   B HG3  1 
ATOM   4765 H  HE1  . MET   B 1 61  ? 51.510 -17.174 -2.020  1.00 16.13 ?  61  MET   B HE1  1 
ATOM   4766 H  HE2  . MET   B 1 61  ? 51.277 -15.701 -1.473  1.00 16.13 ?  61  MET   B HE2  1 
ATOM   4767 H  HE3  . MET   B 1 61  ? 52.739 -16.178 -1.871  1.00 16.13 ?  61  MET   B HE3  1 
ATOM   4768 N  N    . GLN   B 1 62  ? 55.558 -14.696 3.381   1.00 11.84 ?  62  GLN   B N    1 
ATOM   4769 C  CA   . GLN   B 1 62  ? 55.449 -14.753 4.835   1.00 12.25 ?  62  GLN   B CA   1 
ATOM   4770 C  C    . GLN   B 1 62  ? 55.731 -13.397 5.469   1.00 12.30 ?  62  GLN   B C    1 
ATOM   4771 O  O    . GLN   B 1 62  ? 55.041 -12.995 6.414   1.00 12.86 ?  62  GLN   B O    1 
ATOM   4772 C  CB   . GLN   B 1 62  ? 56.399 -15.810 5.401   1.00 12.64 ?  62  GLN   B CB   1 
ATOM   4773 C  CG   . GLN   B 1 62  ? 56.182 -16.072 6.880   1.00 13.14 ?  62  GLN   B CG   1 
ATOM   4774 C  CD   . GLN   B 1 62  ? 54.808 -16.663 7.127   1.00 12.46 ?  62  GLN   B CD   1 
ATOM   4775 O  OE1  . GLN   B 1 62  ? 54.551 -17.815 6.768   1.00 12.93 ?  62  GLN   B OE1  1 
ATOM   4776 N  NE2  . GLN   B 1 62  ? 53.898 -15.867 7.688   1.00 12.86 ?  62  GLN   B NE2  1 
ATOM   4777 H  H    . GLN   B 1 62  ? 56.206 -15.154 3.043   1.00 14.18 ?  62  GLN   B H    1 
ATOM   4778 H  HA   . GLN   B 1 62  ? 54.541 -15.009 5.066   1.00 14.68 ?  62  GLN   B HA   1 
ATOM   4779 H  HB2  . GLN   B 1 62  ? 56.262 -16.648 4.927   1.00 15.15 ?  62  GLN   B HB2  1 
ATOM   4780 H  HB3  . GLN   B 1 62  ? 57.313 -15.510 5.280   1.00 15.15 ?  62  GLN   B HB3  1 
ATOM   4781 H  HG2  . GLN   B 1 62  ? 56.847 -16.704 7.193   1.00 15.75 ?  62  GLN   B HG2  1 
ATOM   4782 H  HG3  . GLN   B 1 62  ? 56.252 -15.238 7.370   1.00 15.75 ?  62  GLN   B HG3  1 
ATOM   4783 H  HE21 . GLN   B 1 62  ? 54.112 -15.066 7.917   1.00 15.41 ?  62  GLN   B HE21 1 
ATOM   4784 H  HE22 . GLN   B 1 62  ? 53.108 -16.164 7.844   1.00 15.41 ?  62  GLN   B HE22 1 
ATOM   4785 N  N    . VAL   B 1 63  ? 56.751 -12.688 4.982   1.00 13.19 ?  63  VAL   B N    1 
ATOM   4786 C  CA   . VAL   B 1 63  ? 57.057 -11.371 5.534   1.00 13.98 ?  63  VAL   B CA   1 
ATOM   4787 C  C    . VAL   B 1 63  ? 55.867 -10.436 5.352   1.00 13.12 ?  63  VAL   B C    1 
ATOM   4788 O  O    . VAL   B 1 63  ? 55.452 -9.730  6.282   1.00 13.99 ?  63  VAL   B O    1 
ATOM   4789 C  CB   . VAL   B 1 63  ? 58.350 -10.816 4.910   1.00 15.11 ?  63  VAL   B CB   1 
ATOM   4790 C  CG1  . VAL   B 1 63  ? 58.577 -9.374  5.350   1.00 15.82 ?  63  VAL   B CG1  1 
ATOM   4791 C  CG2  . VAL   B 1 63  ? 59.534 -11.692 5.307   1.00 15.89 ?  63  VAL   B CG2  1 
ATOM   4792 H  H    . VAL   B 1 63  ? 57.260 -12.943 4.334   1.00 15.80 ?  63  VAL   B H    1 
ATOM   4793 H  HA   . VAL   B 1 63  ? 57.212 -11.470 6.482   1.00 16.75 ?  63  VAL   B HA   1 
ATOM   4794 H  HB   . VAL   B 1 63  ? 58.280 -10.837 3.943   1.00 18.11 ?  63  VAL   B HB   1 
ATOM   4795 H  HG11 . VAL   B 1 63  ? 59.496 -9.132  5.164   1.00 18.96 ?  63  VAL   B HG11 1 
ATOM   4796 H  HG12 . VAL   B 1 63  ? 57.974 -8.800  4.858   1.00 18.96 ?  63  VAL   B HG12 1 
ATOM   4797 H  HG13 . VAL   B 1 63  ? 58.404 -9.309  6.302   1.00 18.96 ?  63  VAL   B HG13 1 
ATOM   4798 H  HG21 . VAL   B 1 63  ? 60.346 -11.321 4.926   1.00 19.04 ?  63  VAL   B HG21 1 
ATOM   4799 H  HG22 . VAL   B 1 63  ? 59.604 -11.708 6.277   1.00 19.04 ?  63  VAL   B HG22 1 
ATOM   4800 H  HG23 . VAL   B 1 63  ? 59.393 -12.592 4.973   1.00 19.04 ?  63  VAL   B HG23 1 
ATOM   4801 N  N    . GLU   B 1 64  ? 55.296 -10.426 4.147   1.00 12.61 ?  64  GLU   B N    1 
ATOM   4802 C  CA   . GLU   B 1 64  ? 54.132 -9.588  3.870   1.00 12.56 ?  64  GLU   B CA   1 
ATOM   4803 C  C    . GLU   B 1 64  ? 52.948 -9.987  4.743   1.00 12.10 ?  64  GLU   B C    1 
ATOM   4804 O  O    . GLU   B 1 64  ? 52.199 -9.126  5.237   1.00 12.72 ?  64  GLU   B O    1 
ATOM   4805 C  CB   . GLU   B 1 64  ? 53.773 -9.735  2.391   1.00 12.91 ?  64  GLU   B CB   1 
ATOM   4806 C  CG   . GLU   B 1 64  ? 52.507 -9.004  1.958   1.00 13.11 ?  64  GLU   B CG   1 
ATOM   4807 C  CD   . GLU   B 1 64  ? 51.974 -9.498  0.621   1.00 13.62 ?  64  GLU   B CD   1 
ATOM   4808 O  OE1  . GLU   B 1 64  ? 52.149 -10.705 0.308   1.00 14.25 ?  64  GLU   B OE1  1 
ATOM   4809 O  OE2  . GLU   B 1 64  ? 51.358 -8.684  -0.109  1.00 14.42 -1 64  GLU   B OE2  1 
ATOM   4810 H  H    . GLU   B 1 64  ? 55.568 -10.891 3.469   1.00 15.11 ?  64  GLU   B H    1 
ATOM   4811 H  HA   . GLU   B 1 64  ? 54.350 -8.660  4.043   1.00 15.05 ?  64  GLU   B HA   1 
ATOM   4812 H  HB2  . GLU   B 1 64  ? 54.501 -9.378  1.854   1.00 15.47 ?  64  GLU   B HB2  1 
ATOM   4813 H  HB3  . GLU   B 1 64  ? 53.650 -10.671 2.190   1.00 15.47 ?  64  GLU   B HB3  1 
ATOM   4814 H  HG2  . GLU   B 1 64  ? 51.805 -9.140  2.617   1.00 15.71 ?  64  GLU   B HG2  1 
ATOM   4815 H  HG3  . GLU   B 1 64  ? 52.697 -8.056  1.875   1.00 15.71 ?  64  GLU   B HG3  1 
ATOM   4816 N  N    . SER   B 1 65  ? 52.763 -11.293 4.933   1.00 11.78 ?  65  SER   B N    1 
ATOM   4817 C  CA   . SER   B 1 65  ? 51.655 -11.799 5.732   1.00 11.83 ?  65  SER   B CA   1 
ATOM   4818 C  C    . SER   B 1 65  ? 51.788 -11.400 7.196   1.00 12.05 ?  65  SER   B C    1 
ATOM   4819 O  O    . SER   B 1 65  ? 50.790 -11.030 7.832   1.00 12.40 ?  65  SER   B O    1 
ATOM   4820 C  CB   . SER   B 1 65  ? 51.574 -13.318 5.602   1.00 12.00 ?  65  SER   B CB   1 
ATOM   4821 O  OG   . SER   B 1 65  ? 51.224 -13.722 4.288   1.00 12.34 ?  65  SER   B OG   1 
ATOM   4822 H  H    . SER   B 1 65  ? 53.271 -11.913 4.612   1.00 14.12 ?  65  SER   B H    1 
ATOM   4823 H  HA   . SER   B 1 65  ? 50.823 -11.425 5.395   1.00 14.17 ?  65  SER   B HA   1 
ATOM   4824 H  HB2  . SER   B 1 65  ? 52.434 -13.698 5.823   1.00 14.37 ?  65  SER   B HB2  1 
ATOM   4825 H  HB3  . SER   B 1 65  ? 50.898 -13.648 6.219   1.00 14.37 ?  65  SER   B HB3  1 
ATOM   4826 H  HG   . SER   B 1 65  ? 51.792 -13.432 3.737   1.00 14.78 ?  65  SER   B HG   1 
ATOM   4827 N  N    . ASP   B 1 66  ? 52.996 -11.498 7.760   1.00 12.38 ?  66  ASP   B N    1 
ATOM   4828 C  CA   . ASP   B 1 66  ? 53.179 -11.108 9.155   1.00 12.76 ?  66  ASP   B CA   1 
ATOM   4829 C  C    . ASP   B 1 66  ? 52.867 -9.629  9.351   1.00 12.90 ?  66  ASP   B C    1 
ATOM   4830 O  O    . ASP   B 1 66  ? 52.293 -9.235  10.373  1.00 13.34 ?  66  ASP   B O    1 
ATOM   4831 C  CB   . ASP   B 1 66  ? 54.606 -11.419 9.613   1.00 14.01 ?  66  ASP   B CB   1 
ATOM   4832 C  CG   . ASP   B 1 66  ? 54.871 -12.913 9.767   1.00 16.04 ?  66  ASP   B CG   1 
ATOM   4833 O  OD1  . ASP   B 1 66  ? 53.922 -13.727 9.692   1.00 16.52 ?  66  ASP   B OD1  1 
ATOM   4834 O  OD2  . ASP   B 1 66  ? 56.048 -13.278 9.981   1.00 18.48 -1 66  ASP   B OD2  1 
ATOM   4835 H  H    . ASP   B 1 66  ? 53.699 -11.795 7.371   1.00 14.83 ?  66  ASP   B H    1 
ATOM   4836 H  HA   . ASP   B 1 66  ? 52.570 -11.613 9.715   1.00 15.29 ?  66  ASP   B HA   1 
ATOM   4837 H  HB2  . ASP   B 1 66  ? 55.231 -11.072 8.959   1.00 16.79 ?  66  ASP   B HB2  1 
ATOM   4838 H  HB3  . ASP   B 1 66  ? 54.760 -10.996 10.475  1.00 16.79 ?  66  ASP   B HB3  1 
ATOM   4839 N  N    . ASP   B 1 67  ? 53.246 -8.788  8.384   1.00 12.68 ?  67  ASP   B N    1 
ATOM   4840 C  CA   . ASP   B 1 67  ? 52.901 -7.376  8.465   1.00 13.29 ?  67  ASP   B CA   1 
ATOM   4841 C  C    . ASP   B 1 67  ? 51.388 -7.172  8.388   1.00 13.44 ?  67  ASP   B C    1 
ATOM   4842 O  O    . ASP   B 1 67  ? 50.828 -6.364  9.137   1.00 13.84 ?  67  ASP   B O    1 
ATOM   4843 C  CB   . ASP   B 1 67  ? 53.612 -6.608  7.359   1.00 14.70 ?  67  ASP   B CB   1 
ATOM   4844 C  CG   . ASP   B 1 67  ? 53.190 -5.166  7.313   1.00 16.13 ?  67  ASP   B CG   1 
ATOM   4845 O  OD1  . ASP   B 1 67  ? 53.687 -4.354  8.129   1.00 17.33 ?  67  ASP   B OD1  1 
ATOM   4846 O  OD2  . ASP   B 1 67  ? 52.326 -4.864  6.474   1.00 16.87 -1 67  ASP   B OD2  1 
ATOM   4847 H  H    . ASP   B 1 67  ? 53.701 -9.012  7.687   1.00 15.19 ?  67  ASP   B H    1 
ATOM   4848 H  HA   . ASP   B 1 67  ? 53.207 -7.027  9.313   1.00 15.93 ?  67  ASP   B HA   1 
ATOM   4849 H  HB2  . ASP   B 1 67  ? 54.568 -6.631  7.514   1.00 17.62 ?  67  ASP   B HB2  1 
ATOM   4850 H  HB3  . ASP   B 1 67  ? 53.407 -7.019  6.500   1.00 17.62 ?  67  ASP   B HB3  1 
ATOM   4851 N  N    . TYR   B 1 68  ? 50.708 -7.901  7.497   1.00 13.18 ?  68  TYR   B N    1 
ATOM   4852 C  CA   . TYR   B 1 68  ? 49.250 -7.824  7.427   1.00 13.60 ?  68  TYR   B CA   1 
ATOM   4853 C  C    . TYR   B 1 68  ? 48.618 -8.161  8.774   1.00 13.25 ?  68  TYR   B C    1 
ATOM   4854 O  O    . TYR   B 1 68  ? 47.681 -7.489  9.220   1.00 14.03 ?  68  TYR   B O    1 
ATOM   4855 C  CB   . TYR   B 1 68  ? 48.718 -8.759  6.334   1.00 14.34 ?  68  TYR   B CB   1 
ATOM   4856 C  CG   . TYR   B 1 68  ? 47.215 -8.906  6.391   1.00 15.52 ?  68  TYR   B CG   1 
ATOM   4857 C  CD1  . TYR   B 1 68  ? 46.624 -9.862  7.210   1.00 16.37 ?  68  TYR   B CD1  1 
ATOM   4858 C  CD2  . TYR   B 1 68  ? 46.388 -8.068  5.665   1.00 16.70 ?  68  TYR   B CD2  1 
ATOM   4859 C  CE1  . TYR   B 1 68  ? 45.260 -9.984  7.296   1.00 17.57 ?  68  TYR   B CE1  1 
ATOM   4860 C  CE2  . TYR   B 1 68  ? 45.008 -8.194  5.737   1.00 17.06 ?  68  TYR   B CE2  1 
ATOM   4861 C  CZ   . TYR   B 1 68  ? 44.463 -9.149  6.559   1.00 17.50 ?  68  TYR   B CZ   1 
ATOM   4862 O  OH   . TYR   B 1 68  ? 43.095 -9.267  6.646   1.00 18.54 ?  68  TYR   B OH   1 
ATOM   4863 H  H    . TYR   B 1 68  ? 51.067 -8.447  6.930   1.00 15.79 ?  68  TYR   B H    1 
ATOM   4864 H  HA   . TYR   B 1 68  ? 49.000 -6.919  7.199   1.00 16.30 ?  68  TYR   B HA   1 
ATOM   4865 H  HB2  . TYR   B 1 68  ? 48.946 -8.397  5.467   1.00 17.19 ?  68  TYR   B HB2  1 
ATOM   4866 H  HB3  . TYR   B 1 68  ? 49.108 -9.639  6.448   1.00 17.19 ?  68  TYR   B HB3  1 
ATOM   4867 H  HD1  . TYR   B 1 68  ? 47.158 -10.434 7.714   1.00 19.62 ?  68  TYR   B HD1  1 
ATOM   4868 H  HD2  . TYR   B 1 68  ? 46.761 -7.415  5.126   1.00 20.02 ?  68  TYR   B HD2  1 
ATOM   4869 H  HE1  . TYR   B 1 68  ? 44.874 -10.640 7.839   1.00 21.07 ?  68  TYR   B HE1  1 
ATOM   4870 H  HE2  . TYR   B 1 68  ? 44.454 -7.624  5.252   1.00 20.45 ?  68  TYR   B HE2  1 
ATOM   4871 H  HH   . TYR   B 1 68  ? 42.707 -8.707  6.143   1.00 22.23 ?  68  TYR   B HH   1 
ATOM   4872 N  N    . ILE   B 1 69  ? 49.095 -9.232  9.416   1.00 12.88 ?  69  ILE   B N    1 
ATOM   4873 C  CA   . ILE   B 1 69  ? 48.542 -9.655  10.699  1.00 13.66 ?  69  ILE   B CA   1 
ATOM   4874 C  C    . ILE   B 1 69  ? 48.798 -8.609  11.775  1.00 13.58 ?  69  ILE   B C    1 
ATOM   4875 O  O    . ILE   B 1 69  ? 47.927 -8.329  12.606  1.00 13.79 ?  69  ILE   B O    1 
ATOM   4876 C  CB   . ILE   B 1 69  ? 49.119 -11.027 11.090  1.00 14.46 ?  69  ILE   B CB   1 
ATOM   4877 C  CG1  . ILE   B 1 69  ? 48.589 -12.125 10.158  1.00 14.75 ?  69  ILE   B CG1  1 
ATOM   4878 C  CG2  . ILE   B 1 69  ? 48.829 -11.343 12.553  1.00 15.11 ?  69  ILE   B CG2  1 
ATOM   4879 C  CD1  . ILE   B 1 69  ? 47.115 -12.444 10.323  1.00 15.06 ?  69  ILE   B CD1  1 
ATOM   4880 H  H    . ILE   B 1 69  ? 49.737 -9.726  9.134   1.00 15.43 ?  69  ILE   B H    1 
ATOM   4881 H  HA   . ILE   B 1 69  ? 47.583 -9.752  10.608  1.00 16.37 ?  69  ILE   B HA   1 
ATOM   4882 H  HB   . ILE   B 1 69  ? 50.083 -10.987 10.984  1.00 17.33 ?  69  ILE   B HB   1 
ATOM   4883 H  HG12 . ILE   B 1 69  ? 48.731 -11.844 9.240   1.00 17.68 ?  69  ILE   B HG12 1 
ATOM   4884 H  HG13 . ILE   B 1 69  ? 49.089 -12.941 10.327  1.00 17.68 ?  69  ILE   B HG13 1 
ATOM   4885 H  HG21 . ILE   B 1 69  ? 48.968 -12.292 12.702  1.00 18.11 ?  69  ILE   B HG21 1 
ATOM   4886 H  HG22 . ILE   B 1 69  ? 49.435 -10.834 13.116  1.00 18.11 ?  69  ILE   B HG22 1 
ATOM   4887 H  HG23 . ILE   B 1 69  ? 47.911 -11.109 12.752  1.00 18.11 ?  69  ILE   B HG23 1 
ATOM   4888 H  HD11 . ILE   B 1 69  ? 46.881 -13.153 9.704   1.00 18.05 ?  69  ILE   B HD11 1 
ATOM   4889 H  HD12 . ILE   B 1 69  ? 46.953 -12.734 11.233  1.00 18.05 ?  69  ILE   B HD12 1 
ATOM   4890 H  HD13 . ILE   B 1 69  ? 46.596 -11.651 10.127  1.00 18.05 ?  69  ILE   B HD13 1 
ATOM   4891 N  N    . ALA   B 1 70  ? 49.993 -8.018  11.793  1.00 13.58 ?  70  ALA   B N    1 
ATOM   4892 C  CA   . ALA   B 1 70  ? 50.274 -6.982  12.780  1.00 13.37 ?  70  ALA   B CA   1 
ATOM   4893 C  C    . ALA   B 1 70  ? 49.274 -5.841  12.669  1.00 13.58 ?  70  ALA   B C    1 
ATOM   4894 O  O    . ALA   B 1 70  ? 48.837 -5.287  13.683  1.00 13.99 ?  70  ALA   B O    1 
ATOM   4895 C  CB   . ALA   B 1 70  ? 51.700 -6.469  12.602  1.00 13.59 ?  70  ALA   B CB   1 
ATOM   4896 H  H    . ALA   B 1 70  ? 50.634 -8.198  11.260  1.00 16.27 ?  70  ALA   B H    1 
ATOM   4897 H  HA   . ALA   B 1 70  ? 50.200 -7.359  13.670  1.00 16.02 ?  70  ALA   B HA   1 
ATOM   4898 H  HB1  . ALA   B 1 70  ? 51.887 -5.808  13.288  1.00 16.29 ?  70  ALA   B HB1  1 
ATOM   4899 H  HB2  . ALA   B 1 70  ? 52.317 -7.213  12.686  1.00 16.29 ?  70  ALA   B HB2  1 
ATOM   4900 H  HB3  . ALA   B 1 70  ? 51.786 -6.067  11.723  1.00 16.29 ?  70  ALA   B HB3  1 
ATOM   4901 N  N    . THR   B 1 71  ? 48.895 -5.480  11.444  1.00 14.04 ?  71  THR   B N    1 
ATOM   4902 C  CA   . THR   B 1 71  ? 48.000 -4.347  11.240  1.00 15.12 ?  71  THR   B CA   1 
ATOM   4903 C  C    . THR   B 1 71  ? 46.536 -4.716  11.446  1.00 15.72 ?  71  THR   B C    1 
ATOM   4904 O  O    . THR   B 1 71  ? 45.755 -3.906  11.965  1.00 17.03 ?  71  THR   B O    1 
ATOM   4905 C  CB   . THR   B 1 71  ? 48.211 -3.773  9.837   1.00 16.98 ?  71  THR   B CB   1 
ATOM   4906 O  OG1  . THR   B 1 71  ? 49.537 -3.242  9.735   1.00 19.31 ?  71  THR   B OG1  1 
ATOM   4907 C  CG2  . THR   B 1 71  ? 47.192 -2.681  9.527   1.00 18.25 ?  71  THR   B CG2  1 
ATOM   4908 H  H    . THR   B 1 71  ? 49.147 -5.870  10.721  1.00 16.83 ?  71  THR   B H    1 
ATOM   4909 H  HA   . THR   B 1 71  ? 48.221 -3.650  11.875  1.00 18.13 ?  71  THR   B HA   1 
ATOM   4910 H  HB   . THR   B 1 71  ? 48.109 -4.476  9.177   1.00 20.35 ?  71  THR   B HB   1 
ATOM   4911 H  HG1  . THR   B 1 71  ? 49.662 -2.907  8.970   1.00 23.15 ?  71  THR   B HG1  1 
ATOM   4912 H  HG21 . THR   B 1 71  ? 47.493 -2.151  8.769   1.00 21.87 ?  71  THR   B HG21 1 
ATOM   4913 H  HG22 . THR   B 1 71  ? 46.334 -3.075  9.311   1.00 21.87 ?  71  THR   B HG22 1 
ATOM   4914 H  HG23 . THR   B 1 71  ? 47.090 -2.095  10.294  1.00 21.87 ?  71  THR   B HG23 1 
ATOM   4915 N  N    . ASN   B 1 72  ? 46.145 -5.927  11.048  1.00 15.24 ?  72  ASN   B N    1 
ATOM   4916 C  CA   . ASN   B 1 72  ? 44.742 -6.288  10.924  1.00 15.86 ?  72  ASN   B CA   1 
ATOM   4917 C  C    . ASN   B 1 72  ? 44.274 -7.382  11.870  1.00 16.32 ?  72  ASN   B C    1 
ATOM   4918 O  O    . ASN   B 1 72  ? 43.059 -7.542  12.037  1.00 17.40 ?  72  ASN   B O    1 
ATOM   4919 C  CB   . ASN   B 1 72  ? 44.433 -6.724  9.483   1.00 16.76 ?  72  ASN   B CB   1 
ATOM   4920 C  CG   . ASN   B 1 72  ? 44.709 -5.627  8.482   1.00 17.73 ?  72  ASN   B CG   1 
ATOM   4921 O  OD1  . ASN   B 1 72  ? 45.726 -5.638  7.783   1.00 18.54 ?  72  ASN   B OD1  1 
ATOM   4922 N  ND2  . ASN   B 1 72  ? 43.829 -4.647  8.438   1.00 19.26 ?  72  ASN   B ND2  1 
ATOM   4923 H  H    . ASN   B 1 72  ? 46.685 -6.569  10.839  1.00 18.27 ?  72  ASN   B H    1 
ATOM   4924 H  HA   . ASN   B 1 72  ? 44.207 -5.502  11.108  1.00 19.01 ?  72  ASN   B HA   1 
ATOM   4925 H  HB2  . ASN   B 1 72  ? 44.990 -7.486  9.255   1.00 20.09 ?  72  ASN   B HB2  1 
ATOM   4926 H  HB3  . ASN   B 1 72  ? 43.496 -6.964  9.418   1.00 20.09 ?  72  ASN   B HB3  1 
ATOM   4927 H  HD21 . ASN   B 1 72  ? 43.936 -3.994  7.887   1.00 23.09 ?  72  ASN   B HD21 1 
ATOM   4928 H  HD22 . ASN   B 1 72  ? 43.133 -4.667  8.947   1.00 23.09 ?  72  ASN   B HD22 1 
ATOM   4929 N  N    . GLY   B 1 73  ? 45.179 -8.133  12.489  1.00 15.66 ?  73  GLY   B N    1 
ATOM   4930 C  CA   . GLY   B 1 73  ? 44.789 -9.277  13.277  1.00 15.11 ?  73  GLY   B CA   1 
ATOM   4931 C  C    . GLY   B 1 73  ? 44.425 -10.462 12.408  1.00 13.90 ?  73  GLY   B C    1 
ATOM   4932 O  O    . GLY   B 1 73  ? 44.406 -10.377 11.176  1.00 13.79 ?  73  GLY   B O    1 
ATOM   4933 H  H    . GLY   B 1 73  ? 46.030 -7.994  12.465  1.00 18.77 ?  73  GLY   B H    1 
ATOM   4934 H  HA2  . GLY   B 1 73  ? 45.520 -9.532  13.865  1.00 18.11 ?  73  GLY   B HA2  1 
ATOM   4935 H  HA3  . GLY   B 1 73  ? 44.022 -9.046  13.827  1.00 18.11 ?  73  GLY   B HA3  1 
ATOM   4936 N  N    . PRO   B 1 74  ? 44.121 -11.590 13.047  1.00 14.23 ?  74  PRO   B N    1 
ATOM   4937 C  CA   . PRO   B 1 74  ? 43.867 -12.825 12.303  1.00 13.51 ?  74  PRO   B CA   1 
ATOM   4938 C  C    . PRO   B 1 74  ? 42.568 -12.766 11.511  1.00 12.98 ?  74  PRO   B C    1 
ATOM   4939 O  O    . PRO   B 1 74  ? 41.628 -12.029 11.829  1.00 14.26 ?  74  PRO   B O    1 
ATOM   4940 C  CB   . PRO   B 1 74  ? 43.784 -13.886 13.408  1.00 14.56 ?  74  PRO   B CB   1 
ATOM   4941 C  CG   . PRO   B 1 74  ? 43.338 -13.133 14.614  1.00 15.95 ?  74  PRO   B CG   1 
ATOM   4942 C  CD   . PRO   B 1 74  ? 44.005 -11.790 14.501  1.00 15.45 ?  74  PRO   B CD   1 
ATOM   4943 H  HA   . PRO   B 1 74  ? 44.613 -13.022 11.709  1.00 16.20 ?  74  PRO   B HA   1 
ATOM   4944 H  HB2  . PRO   B 1 74  ? 43.132 -14.560 13.160  1.00 17.45 ?  74  PRO   B HB2  1 
ATOM   4945 H  HB3  . PRO   B 1 74  ? 44.656 -14.281 13.549  1.00 17.45 ?  74  PRO   B HB3  1 
ATOM   4946 H  HG2  . PRO   B 1 74  ? 42.371 -13.041 14.602  1.00 19.11 ?  74  PRO   B HG2  1 
ATOM   4947 H  HG3  . PRO   B 1 74  ? 43.629 -13.598 15.412  1.00 19.11 ?  74  PRO   B HG3  1 
ATOM   4948 H  HD2  . PRO   B 1 74  ? 43.445 -11.101 14.901  1.00 18.52 ?  74  PRO   B HD2  1 
ATOM   4949 H  HD3  . PRO   B 1 74  ? 44.884 -11.811 14.908  1.00 18.52 ?  74  PRO   B HD3  1 
ATOM   4950 N  N    . LEU   B 1 75  ? 42.536 -13.579 10.458  1.00 12.25 ?  75  LEU   B N    1 
ATOM   4951 C  CA   . LEU   B 1 75  ? 41.325 -13.788 9.687   1.00 12.48 ?  75  LEU   B CA   1 
ATOM   4952 C  C    . LEU   B 1 75  ? 40.345 -14.643 10.487  1.00 12.95 ?  75  LEU   B C    1 
ATOM   4953 O  O    . LEU   B 1 75  ? 40.684 -15.213 11.524  1.00 13.99 ?  75  LEU   B O    1 
ATOM   4954 C  CB   . LEU   B 1 75  ? 41.647 -14.502 8.373   1.00 12.68 ?  75  LEU   B CB   1 
ATOM   4955 C  CG   . LEU   B 1 75  ? 42.506 -13.751 7.351   1.00 14.27 ?  75  LEU   B CG   1 
ATOM   4956 C  CD1  . LEU   B 1 75  ? 42.701 -14.574 6.082   1.00 15.63 ?  75  LEU   B CD1  1 
ATOM   4957 C  CD2  . LEU   B 1 75  ? 41.915 -12.406 7.019   1.00 17.45 ?  75  LEU   B CD2  1 
ATOM   4958 H  H    . LEU   B 1 75  ? 43.208 -14.033 10.171  1.00 14.68 ?  75  LEU   B H    1 
ATOM   4959 H  HA   . LEU   B 1 75  ? 40.904 -12.939 9.491   1.00 14.95 ?  75  LEU   B HA   1 
ATOM   4960 H  HB2  . LEU   B 1 75  ? 42.113 -15.327 8.581   1.00 15.19 ?  75  LEU   B HB2  1 
ATOM   4961 H  HB3  . LEU   B 1 75  ? 40.809 -14.716 7.930   1.00 15.19 ?  75  LEU   B HB3  1 
ATOM   4962 H  HG   . LEU   B 1 75  ? 43.383 -13.601 7.738   1.00 17.10 ?  75  LEU   B HG   1 
ATOM   4963 H  HD11 . LEU   B 1 75  ? 43.256 -14.070 5.461   1.00 18.74 ?  75  LEU   B HD11 1 
ATOM   4964 H  HD12 . LEU   B 1 75  ? 43.141 -15.409 6.308   1.00 18.74 ?  75  LEU   B HD12 1 
ATOM   4965 H  HD13 . LEU   B 1 75  ? 41.837 -14.751 5.681   1.00 18.74 ?  75  LEU   B HD13 1 
ATOM   4966 H  HD21 . LEU   B 1 75  ? 42.420 -12.010 6.293   1.00 20.92 ?  75  LEU   B HD21 1 
ATOM   4967 H  HD22 . LEU   B 1 75  ? 40.990 -12.525 6.757   1.00 20.92 ?  75  LEU   B HD22 1 
ATOM   4968 H  HD23 . LEU   B 1 75  ? 41.966 -11.838 7.805   1.00 20.92 ?  75  LEU   B HD23 1 
ATOM   4969 N  N    . LYS   B 1 76  ? 39.111 -14.723 9.990   1.00 14.31 ?  76  LYS   B N    1 
ATOM   4970 C  CA   . LYS   B 1 76  ? 38.131 -15.685 10.476  1.00 15.86 ?  76  LYS   B CA   1 
ATOM   4971 C  C    . LYS   B 1 76  ? 38.224 -16.957 9.639   1.00 14.40 ?  76  LYS   B C    1 
ATOM   4972 O  O    . LYS   B 1 76  ? 38.501 -16.902 8.441   1.00 14.06 ?  76  LYS   B O    1 
ATOM   4973 C  CB   . LYS   B 1 76  ? 36.710 -15.130 10.304  1.00 17.88 ?  76  LYS   B CB   1 
ATOM   4974 C  CG   . LYS   B 1 76  ? 36.430 -13.752 10.919  1.00 19.51 ?  76  LYS   B CG   1 
ATOM   4975 C  CD   . LYS   B 1 76  ? 35.023 -13.241 10.566  1.00 20.70 ?  76  LYS   B CD   1 
ATOM   4976 C  CE   . LYS   B 1 76  ? 34.754 -11.867 11.168  1.00 22.54 ?  76  LYS   B CE   1 
ATOM   4977 N  NZ   . LYS   B 1 76  ? 33.459 -11.279 10.722  1.00 23.16 ?  76  LYS   B NZ   1 
ATOM   4978 H  H    . LYS   B 1 76  ? 38.816 -14.225 9.356   1.00 17.15 ?  76  LYS   B H    1 
ATOM   4979 H  HA   . LYS   B 1 76  ? 38.290 -15.900 11.409  1.00 19.01 ?  76  LYS   B HA   1 
ATOM   4980 H  HB2  . LYS   B 1 76  ? 36.525 -15.065 9.354   1.00 21.43 ?  76  LYS   B HB2  1 
ATOM   4981 H  HB3  . LYS   B 1 76  ? 36.089 -15.756 10.710  1.00 21.43 ?  76  LYS   B HB3  1 
ATOM   4982 H  HG2  . LYS   B 1 76  ? 36.502 -13.814 11.884  1.00 23.39 ?  76  LYS   B HG2  1 
ATOM   4983 H  HG3  . LYS   B 1 76  ? 37.082 -13.116 10.577  1.00 23.39 ?  76  LYS   B HG3  1 
ATOM   4984 H  HD2  . LYS   B 1 76  ? 34.942 -13.173 9.601   1.00 24.82 ?  76  LYS   B HD2  1 
ATOM   4985 H  HD3  . LYS   B 1 76  ? 34.365 -13.862 10.914  1.00 24.82 ?  76  LYS   B HD3  1 
ATOM   4986 H  HE2  . LYS   B 1 76  ? 34.733 -11.948 12.134  1.00 27.02 ?  76  LYS   B HE2  1 
ATOM   4987 H  HE3  . LYS   B 1 76  ? 35.467 -11.264 10.902  1.00 27.02 ?  76  LYS   B HE3  1 
ATOM   4988 H  HZ1  . LYS   B 1 76  ? 33.344 -10.478 11.097  1.00 27.78 ?  76  LYS   B HZ1  1 
ATOM   4989 H  HZ2  . LYS   B 1 76  ? 33.454 -11.184 9.837   1.00 27.78 ?  76  LYS   B HZ2  1 
ATOM   4990 H  HZ3  . LYS   B 1 76  ? 32.784 -11.808 10.960  1.00 27.78 ?  76  LYS   B HZ3  1 
ATOM   4991 N  N    . VAL   B 1 77  ? 37.973 -18.110 10.269  1.00 15.00 ?  77  VAL   B N    1 
ATOM   4992 C  CA   . VAL   B 1 77  ? 37.773 -19.325 9.486   1.00 15.03 ?  77  VAL   B CA   1 
ATOM   4993 C  C    . VAL   B 1 77  ? 36.582 -19.098 8.568   1.00 13.79 ?  77  VAL   B C    1 
ATOM   4994 O  O    . VAL   B 1 77  ? 35.513 -18.657 9.012   1.00 13.88 ?  77  VAL   B O    1 
ATOM   4995 C  CB   . VAL   B 1 77  ? 37.574 -20.546 10.398  1.00 16.40 ?  77  VAL   B CB   1 
ATOM   4996 C  CG1  . VAL   B 1 77  ? 37.312 -21.786 9.552   1.00 17.09 ?  77  VAL   B CG1  1 
ATOM   4997 C  CG2  . VAL   B 1 77  ? 38.798 -20.756 11.290  1.00 17.69 ?  77  VAL   B CG2  1 
ATOM   4998 H  H    . VAL   B 1 77  ? 37.912 -18.212 11.116  1.00 17.98 ?  77  VAL   B H    1 
ATOM   4999 H  HA   . VAL   B 1 77  ? 38.550 -19.484 8.932   1.00 18.01 ?  77  VAL   B HA   1 
ATOM   5000 H  HB   . VAL   B 1 77  ? 36.799 -20.397 10.967  1.00 19.65 ?  77  VAL   B HB   1 
ATOM   5001 H  HG11 . VAL   B 1 77  ? 37.369 -22.571 10.121  1.00 20.48 ?  77  VAL   B HG11 1 
ATOM   5002 H  HG12 . VAL   B 1 77  ? 36.422 -21.728 9.165   1.00 20.48 ?  77  VAL   B HG12 1 
ATOM   5003 H  HG13 . VAL   B 1 77  ? 37.976 -21.837 8.851   1.00 20.48 ?  77  VAL   B HG13 1 
ATOM   5004 H  HG21 . VAL   B 1 77  ? 38.662 -21.555 11.820  1.00 21.21 ?  77  VAL   B HG21 1 
ATOM   5005 H  HG22 . VAL   B 1 77  ? 39.578 -20.856 10.727  1.00 21.21 ?  77  VAL   B HG22 1 
ATOM   5006 H  HG23 . VAL   B 1 77  ? 38.898 -19.985 11.869  1.00 21.21 ?  77  VAL   B HG23 1 
ATOM   5007 N  N    . GLY   B 1 78  ? 36.767 -19.372 7.278   1.00 13.23 ?  78  GLY   B N    1 
ATOM   5008 C  CA   . GLY   B 1 78  ? 35.790 -19.058 6.262   1.00 12.88 ?  78  GLY   B CA   1 
ATOM   5009 C  C    . GLY   B 1 78  ? 36.030 -17.740 5.560   1.00 12.37 ?  78  GLY   B C    1 
ATOM   5010 O  O    . GLY   B 1 78  ? 35.346 -17.455 4.571   1.00 12.79 ?  78  GLY   B O    1 
ATOM   5011 H  H    . GLY   B 1 78  ? 37.473 -19.754 6.963   1.00 15.86 ?  78  GLY   B H    1 
ATOM   5012 H  HA2  . GLY   B 1 78  ? 35.788 -19.755 5.590   1.00 15.43 ?  78  GLY   B HA2  1 
ATOM   5013 H  HA3  . GLY   B 1 78  ? 34.909 -19.022 6.665   1.00 15.43 ?  78  GLY   B HA3  1 
ATOM   5014 N  N    . GLY   B 1 79  ? 36.976 -16.933 6.046   1.00 12.31 ?  79  GLY   B N    1 
ATOM   5015 C  CA   . GLY   B 1 79  ? 37.273 -15.640 5.465   1.00 11.71 ?  79  GLY   B CA   1 
ATOM   5016 C  C    . GLY   B 1 79  ? 38.514 -15.663 4.580   1.00 11.45 ?  79  GLY   B C    1 
ATOM   5017 O  O    . GLY   B 1 79  ? 39.132 -16.699 4.331   1.00 11.85 ?  79  GLY   B O    1 
ATOM   5018 H  H    . GLY   B 1 79  ? 37.473 -17.123 6.717   1.00 14.75 ?  79  GLY   B H    1 
ATOM   5019 H  HA2  . GLY   B 1 79  ? 36.518 -15.341 4.928   1.00 14.03 ?  79  GLY   B HA2  1 
ATOM   5020 H  HA3  . GLY   B 1 79  ? 37.417 -14.992 6.172   1.00 14.03 ?  79  GLY   B HA3  1 
ATOM   5021 N  N    . SER   B 1 80  ? 38.878 -14.471 4.103   1.00 11.63 ?  80  SER   B N    1 
ATOM   5022 C  CA   . SER   B 1 80  ? 39.988 -14.338 3.169   1.00 11.44 ?  80  SER   B CA   1 
ATOM   5023 C  C    . SER   B 1 80  ? 40.568 -12.932 3.226   1.00 11.28 ?  80  SER   B C    1 
ATOM   5024 O  O    . SER   B 1 80  ? 39.953 -11.996 3.741   1.00 12.44 ?  80  SER   B O    1 
ATOM   5025 C  CB   . SER   B 1 80  ? 39.543 -14.630 1.733   1.00 11.81 ?  80  SER   B CB   1 
ATOM   5026 O  OG   . SER   B 1 80  ? 38.704 -13.603 1.235   1.00 12.70 ?  80  SER   B OG   1 
ATOM   5027 H  H    . SER   B 1 80  ? 38.505 -13.727 4.311   1.00 13.93 ?  80  SER   B H    1 
ATOM   5028 H  HA   . SER   B 1 80  ? 40.680 -14.969 3.413   1.00 13.70 ?  80  SER   B HA   1 
ATOM   5029 H  HB2  . SER   B 1 80  ? 40.324 -14.691 1.162   1.00 14.15 ?  80  SER   B HB2  1 
ATOM   5030 H  HB3  . SER   B 1 80  ? 39.054 -15.467 1.716   1.00 14.15 ?  80  SER   B HB3  1 
ATOM   5031 H  HG   . SER   B 1 80  ? 38.013 -13.535 1.719   1.00 15.22 ?  80  SER   B HG   1 
ATOM   5032 N  N    . CYS   B 1 81  ? 41.754 -12.789 2.640   1.00 10.96 ?  81  CYS   B N    1 
ATOM   5033 C  CA   . CYS   B 1 81  ? 42.304 -11.476 2.331   1.00 11.17 ?  81  CYS   B CA   1 
ATOM   5034 C  C    . CYS   B 1 81  ? 43.074 -11.562 1.022   1.00 10.71 ?  81  CYS   B C    1 
ATOM   5035 O  O    . CYS   B 1 81  ? 43.579 -12.627 0.647   1.00 11.49 ?  81  CYS   B O    1 
ATOM   5036 C  CB   . CYS   B 1 81  ? 43.198 -10.925 3.451   1.00 11.98 ?  81  CYS   B CB   1 
ATOM   5037 S  SG   . CYS   B 1 81  ? 44.712 -11.859 3.700   1.00 12.34 ?  81  CYS   B SG   1 
ATOM   5038 H  H    . CYS   B 1 81  ? 42.267 -13.444 2.403   1.00 13.13 ?  81  CYS   B H    1 
ATOM   5039 H  HA   . CYS   B 1 81  ? 41.571 -10.852 2.204   1.00 13.38 ?  81  CYS   B HA   1 
ATOM   5040 H  HB2  . CYS   B 1 81  ? 43.447 -10.012 3.234   1.00 14.35 ?  81  CYS   B HB2  1 
ATOM   5041 H  HB3  . CYS   B 1 81  ? 42.696 -10.936 4.284   1.00 14.35 ?  81  CYS   B HB3  1 
ATOM   5042 H  HG   . CYS   B 1 81  ? 45.334 -11.360 4.597   1.00 14.79 ?  81  CYS   B HG   1 
ATOM   5043 N  N    . VAL   B 1 82  ? 43.180 -10.418 0.346   1.00 10.87 ?  82  VAL   B N    1 
ATOM   5044 C  CA   . VAL   B 1 82  ? 43.943 -10.294 -0.892  1.00 11.13 ?  82  VAL   B CA   1 
ATOM   5045 C  C    . VAL   B 1 82  ? 45.285 -9.655  -0.570  1.00 11.19 ?  82  VAL   B C    1 
ATOM   5046 O  O    . VAL   B 1 82  ? 45.337 -8.540  -0.033  1.00 12.30 ?  82  VAL   B O    1 
ATOM   5047 C  CB   . VAL   B 1 82  ? 43.199 -9.455  -1.942  1.00 12.29 ?  82  VAL   B CB   1 
ATOM   5048 C  CG1  . VAL   B 1 82  ? 44.060 -9.296  -3.194  1.00 13.66 ?  82  VAL   B CG1  1 
ATOM   5049 C  CG2  . VAL   B 1 82  ? 41.853 -10.069 -2.276  1.00 13.25 ?  82  VAL   B CG2  1 
ATOM   5050 H  H    . VAL   B 1 82  ? 42.799 -9.678  0.587   1.00 13.03 ?  82  VAL   B H    1 
ATOM   5051 H  HA   . VAL   B 1 82  ? 44.101 -11.174 -1.262  1.00 13.33 ?  82  VAL   B HA   1 
ATOM   5052 H  HB   . VAL   B 1 82  ? 43.035 -8.572  -1.585  1.00 14.72 ?  82  VAL   B HB   1 
ATOM   5053 H  HG11 . VAL   B 1 82  ? 43.502 -8.990  -3.928  1.00 16.37 ?  82  VAL   B HG11 1 
ATOM   5054 H  HG12 . VAL   B 1 82  ? 44.755 -8.637  -3.020  1.00 16.37 ?  82  VAL   B HG12 1 
ATOM   5055 H  HG13 . VAL   B 1 82  ? 44.461 -10.148 -3.418  1.00 16.37 ?  82  VAL   B HG13 1 
ATOM   5056 H  HG21 . VAL   B 1 82  ? 41.419 -9.540  -2.968  1.00 15.87 ?  82  VAL   B HG21 1 
ATOM   5057 H  HG22 . VAL   B 1 82  ? 41.985 -10.978 -2.600  1.00 15.87 ?  82  VAL   B HG22 1 
ATOM   5058 H  HG23 . VAL   B 1 82  ? 41.300 -10.084 -1.480  1.00 15.87 ?  82  VAL   B HG23 1 
ATOM   5059 N  N    . LEU   B 1 83  ? 46.361 -10.341 -0.937  1.00 10.90 ?  83  LEU   B N    1 
ATOM   5060 C  CA   . LEU   B 1 83  ? 47.719 -9.829  -0.821  1.00 10.91 ?  83  LEU   B CA   1 
ATOM   5061 C  C    . LEU   B 1 83  ? 48.420 -9.974  -2.173  1.00 10.93 ?  83  LEU   B C    1 
ATOM   5062 O  O    . LEU   B 1 83  ? 47.818 -10.391 -3.165  1.00 10.97 ?  83  LEU   B O    1 
ATOM   5063 C  CB   . LEU   B 1 83  ? 48.468 -10.506 0.335   1.00 11.34 ?  83  LEU   B CB   1 
ATOM   5064 C  CG   . LEU   B 1 83  ? 47.960 -10.150 1.735   1.00 12.54 ?  83  LEU   B CG   1 
ATOM   5065 C  CD1  . LEU   B 1 83  ? 48.594 -11.018 2.806   1.00 13.25 ?  83  LEU   B CD1  1 
ATOM   5066 C  CD2  . LEU   B 1 83  ? 48.161 -8.663  2.052   1.00 13.43 ?  83  LEU   B CD2  1 
ATOM   5067 H  H    . LEU   B 1 83  ? 46.322 -11.138 -1.267  1.00 13.06 ?  83  LEU   B H    1 
ATOM   5068 H  HA   . LEU   B 1 83  ? 47.667 -8.884  -0.624  1.00 13.07 ?  83  LEU   B HA   1 
ATOM   5069 H  HB2  . LEU   B 1 83  ? 48.399 -11.462 0.232   1.00 13.59 ?  83  LEU   B HB2  1 
ATOM   5070 H  HB3  . LEU   B 1 83  ? 49.400 -10.237 0.287   1.00 13.59 ?  83  LEU   B HB3  1 
ATOM   5071 H  HG   . LEU   B 1 83  ? 47.008 -10.319 1.757   1.00 15.03 ?  83  LEU   B HG   1 
ATOM   5072 H  HD11 . LEU   B 1 83  ? 48.235 -10.763 3.671   1.00 15.88 ?  83  LEU   B HD11 1 
ATOM   5073 H  HD12 . LEU   B 1 83  ? 48.379 -11.949 2.624   1.00 15.88 ?  83  LEU   B HD12 1 
ATOM   5074 H  HD13 . LEU   B 1 83  ? 49.553 -10.892 2.794   1.00 15.88 ?  83  LEU   B HD13 1 
ATOM   5075 H  HD21 . LEU   B 1 83  ? 47.959 -8.512  2.989   1.00 16.10 ?  83  LEU   B HD21 1 
ATOM   5076 H  HD22 . LEU   B 1 83  ? 49.078 -8.418  1.865   1.00 16.10 ?  83  LEU   B HD22 1 
ATOM   5077 H  HD23 . LEU   B 1 83  ? 47.558 -8.138  1.499   1.00 16.10 ?  83  LEU   B HD23 1 
ATOM   5078 N  N    . SER   B 1 84  ? 49.695 -9.596  -2.229  1.00 11.86 ?  84  SER   B N    1 
ATOM   5079 C  CA   . SER   B 1 84  ? 50.427 -9.721  -3.480  1.00 12.07 ?  84  SER   B CA   1 
ATOM   5080 C  C    . SER   B 1 84  ? 50.585 -11.182 -3.884  1.00 11.29 ?  84  SER   B C    1 
ATOM   5081 O  O    . SER   B 1 84  ? 50.700 -12.075 -3.045  1.00 11.36 ?  84  SER   B O    1 
ATOM   5082 C  CB   . SER   B 1 84  ? 51.821 -9.114  -3.336  1.00 13.95 ?  84  SER   B CB   1 
ATOM   5083 O  OG   . SER   B 1 84  ? 52.572 -9.331  -4.515  1.00 15.06 ?  84  SER   B OG   1 
ATOM   5084 H  H    . SER   B 1 84  ? 50.143 -9.258  -1.576  1.00 14.20 ?  84  SER   B H    1 
ATOM   5085 H  HA   . SER   B 1 84  ? 49.959 -9.252  -4.185  1.00 14.47 ?  84  SER   B HA   1 
ATOM   5086 H  HB2  . SER   B 1 84  ? 51.738 -8.155  -3.178  1.00 16.72 ?  84  SER   B HB2  1 
ATOM   5087 H  HB3  . SER   B 1 84  ? 52.280 -9.529  -2.590  1.00 16.72 ?  84  SER   B HB3  1 
ATOM   5088 H  HG   . SER   B 1 84  ? 53.337 -8.981  -4.437  1.00 18.05 ?  84  SER   B HG   1 
ATOM   5089 N  N    . GLY   B 1 85  ? 50.647 -11.408 -5.188  1.00 12.49 ?  85  GLY   B N    1 
ATOM   5090 C  CA   . GLY   B 1 85  ? 50.996 -12.702 -5.722  1.00 13.23 ?  85  GLY   B CA   1 
ATOM   5091 C  C    . GLY   B 1 85  ? 52.468 -12.898 -6.018  1.00 12.37 ?  85  GLY   B C    1 
ATOM   5092 O  O    . GLY   B 1 85  ? 52.849 -13.974 -6.479  1.00 12.82 ?  85  GLY   B O    1 
ATOM   5093 H  H    . GLY   B 1 85  ? 50.503 -10.815 -5.789  1.00 14.96 ?  85  GLY   B H    1 
ATOM   5094 H  HA2  . GLY   B 1 85  ? 50.732 -13.387 -5.089  1.00 15.86 ?  85  GLY   B HA2  1 
ATOM   5095 H  HA3  . GLY   B 1 85  ? 50.514 -12.846 -6.543  1.00 15.86 ?  85  GLY   B HA3  1 
ATOM   5096 N  N    . HIS   B 1 86  ? 53.321 -11.900 -5.793  1.00 12.44 ?  86  HIS   B N    1 
ATOM   5097 C  CA   . HIS   B 1 86  ? 54.786 -12.062 -5.882  1.00 12.24 ?  86  HIS   B CA   1 
ATOM   5098 C  C    . HIS   B 1 86  ? 55.158 -12.575 -7.272  1.00 12.31 ?  86  HIS   B C    1 
ATOM   5099 O  O    . HIS   B 1 86  ? 54.765 -11.964 -8.278  1.00 13.35 ?  86  HIS   B O    1 
ATOM   5100 C  CB   . HIS   B 1 86  ? 55.285 -12.894 -4.704  1.00 12.67 ?  86  HIS   B CB   1 
ATOM   5101 C  CG   . HIS   B 1 86  ? 54.960 -12.289 -3.381  1.00 12.81 ?  86  HIS   B CG   1 
ATOM   5102 N  ND1  . HIS   B 1 86  ? 55.789 -11.386 -2.753  1.00 14.24 ?  86  HIS   B ND1  1 
ATOM   5103 C  CD2  . HIS   B 1 86  ? 53.876 -12.430 -2.580  1.00 13.09 ?  86  HIS   B CD2  1 
ATOM   5104 C  CE1  . HIS   B 1 86  ? 55.228 -10.997 -1.621  1.00 13.91 ?  86  HIS   B CE1  1 
ATOM   5105 N  NE2  . HIS   B 1 86  ? 54.065 -11.611 -1.496  1.00 13.44 ?  86  HIS   B NE2  1 
ATOM   5106 H  H    . HIS   B 1 86  ? 53.082 -11.104 -5.579  1.00 14.91 ?  86  HIS   B H    1 
ATOM   5107 H  HA   . HIS   B 1 86  ? 55.191 -11.188 -5.788  1.00 14.67 ?  86  HIS   B HA   1 
ATOM   5108 H  HB2  . HIS   B 1 86  ? 54.881 -13.774 -4.739  1.00 15.18 ?  86  HIS   B HB2  1 
ATOM   5109 H  HB3  . HIS   B 1 86  ? 56.254 -12.975 -4.759  1.00 15.18 ?  86  HIS   B HB3  1 
ATOM   5110 H  HD2  . HIS   B 1 86  ? 53.130 -12.964 -2.745  1.00 15.68 ?  86  HIS   B HD2  1 
ATOM   5111 H  HE1  . HIS   B 1 86  ? 55.595 -10.403 -1.006  1.00 16.67 ?  86  HIS   B HE1  1 
ATOM   5112 H  HE2  . HIS   B 1 86  ? 53.519 -11.525 -0.832  1.00 16.11 ?  86  HIS   B HE2  1 
ATOM   5113 N  N    . ASN   B 1 87  ? 55.926 -13.658 -7.381  1.00 12.85 ?  87  ASN   B N    1 
ATOM   5114 C  CA   . ASN   B 1 87  ? 56.317 -14.234 -8.658  1.00 13.47 ?  87  ASN   B CA   1 
ATOM   5115 C  C    . ASN   B 1 87  ? 55.334 -15.275 -9.164  1.00 13.35 ?  87  ASN   B C    1 
ATOM   5116 O  O    . ASN   B 1 87  ? 55.648 -15.985 -10.126 1.00 15.28 ?  87  ASN   B O    1 
ATOM   5117 C  CB   . ASN   B 1 87  ? 57.708 -14.865 -8.542  1.00 15.66 ?  87  ASN   B CB   1 
ATOM   5118 C  CG   . ASN   B 1 87  ? 57.763 -15.977 -7.501  1.00 16.27 ?  87  ASN   B CG   1 
ATOM   5119 O  OD1  . ASN   B 1 87  ? 57.125 -15.895 -6.449  1.00 15.33 ?  87  ASN   B OD1  1 
ATOM   5120 N  ND2  . ASN   B 1 87  ? 58.513 -17.039 -7.805  1.00 18.30 ?  87  ASN   B ND2  1 
ATOM   5121 H  H    . ASN   B 1 87  ? 56.226 -14.098 -6.706  1.00 15.39 ?  87  ASN   B H    1 
ATOM   5122 H  HA   . ASN   B 1 87  ? 56.359 -13.527 -9.316  1.00 16.14 ?  87  ASN   B HA   1 
ATOM   5123 H  HB2  . ASN   B 1 87  ? 57.955 -15.242 -9.402  1.00 18.76 ?  87  ASN   B HB2  1 
ATOM   5124 H  HB3  . ASN   B 1 87  ? 58.342 -14.179 -8.285  1.00 18.76 ?  87  ASN   B HB3  1 
ATOM   5125 H  HD21 . ASN   B 1 87  ? 58.581 -17.690 -7.251  1.00 21.94 ?  87  ASN   B HD21 1 
ATOM   5126 H  HD22 . ASN   B 1 87  ? 58.941 -17.063 -8.554  1.00 21.94 ?  87  ASN   B HD22 1 
ATOM   5127 N  N    . LEU   B 1 88  ? 54.154 -15.376 -8.547  1.00 12.55 ?  88  LEU   B N    1 
ATOM   5128 C  CA   . LEU   B 1 88  ? 53.173 -16.405 -8.874  1.00 12.71 ?  88  LEU   B CA   1 
ATOM   5129 C  C    . LEU   B 1 88  ? 51.942 -15.887 -9.596  1.00 12.53 ?  88  LEU   B C    1 
ATOM   5130 O  O    . LEU   B 1 88  ? 51.339 -16.635 -10.378 1.00 14.07 ?  88  LEU   B O    1 
ATOM   5131 C  CB   . LEU   B 1 88  ? 52.701 -17.088 -7.589  1.00 13.60 ?  88  LEU   B CB   1 
ATOM   5132 C  CG   . LEU   B 1 88  ? 53.811 -17.762 -6.795  1.00 16.05 ?  88  LEU   B CG   1 
ATOM   5133 C  CD1  . LEU   B 1 88  ? 53.306 -18.146 -5.414  1.00 17.51 ?  88  LEU   B CD1  1 
ATOM   5134 C  CD2  . LEU   B 1 88  ? 54.319 -18.977 -7.548  1.00 18.96 ?  88  LEU   B CD2  1 
ATOM   5135 H  H    . LEU   B 1 88  ? 53.891 -14.846 -7.915  1.00 15.04 ?  88  LEU   B H    1 
ATOM   5136 H  HA   . LEU   B 1 88  ? 53.584 -17.068 -9.437  1.00 15.23 ?  88  LEU   B HA   1 
ATOM   5137 H  HB2  . LEU   B 1 88  ? 52.284 -16.430 -7.011  1.00 16.30 ?  88  LEU   B HB2  1 
ATOM   5138 H  HB3  . LEU   B 1 88  ? 52.049 -17.774 -7.822  1.00 16.30 ?  88  LEU   B HB3  1 
ATOM   5139 H  HG   . LEU   B 1 88  ? 54.545 -17.142 -6.685  1.00 19.24 ?  88  LEU   B HG   1 
ATOM   5140 H  HD11 . LEU   B 1 88  ? 53.951 -18.735 -4.993  1.00 21.00 ?  88  LEU   B HD11 1 
ATOM   5141 H  HD12 . LEU   B 1 88  ? 53.192 -17.344 -4.883  1.00 21.00 ?  88  LEU   B HD12 1 
ATOM   5142 H  HD13 . LEU   B 1 88  ? 52.454 -18.604 -5.508  1.00 21.00 ?  88  LEU   B HD13 1 
ATOM   5143 H  HD21 . LEU   B 1 88  ? 54.954 -19.450 -6.988  1.00 22.74 ?  88  LEU   B HD21 1 
ATOM   5144 H  HD22 . LEU   B 1 88  ? 53.570 -19.554 -7.760  1.00 22.74 ?  88  LEU   B HD22 1 
ATOM   5145 H  HD23 . LEU   B 1 88  ? 54.752 -18.683 -8.364  1.00 22.74 ?  88  LEU   B HD23 1 
ATOM   5146 N  N    . ALA   B 1 89  ? 51.536 -14.652 -9.322  1.00 11.70 ?  89  ALA   B N    1 
ATOM   5147 C  CA   . ALA   B 1 89  ? 50.245 -14.152 -9.770  1.00 11.09 ?  89  ALA   B CA   1 
ATOM   5148 C  C    . ALA   B 1 89  ? 50.224 -12.662 -9.488  1.00 11.82 ?  89  ALA   B C    1 
ATOM   5149 O  O    . ALA   B 1 89  ? 51.061 -12.148 -8.744  1.00 12.60 ?  89  ALA   B O    1 
ATOM   5150 C  CB   . ALA   B 1 89  ? 49.100 -14.818 -9.015  1.00 11.57 ?  89  ALA   B CB   1 
ATOM   5151 H  H    . ALA   B 1 89  ? 51.983 -14.075 -8.859  1.00 14.02 ?  89  ALA   B H    1 
ATOM   5152 H  HA   . ALA   B 1 89  ? 50.134 -14.295 -10.723 1.00 13.28 ?  89  ALA   B HA   1 
ATOM   5153 H  HB1  . ALA   B 1 89  ? 48.254 -14.478 -9.357  1.00 13.87 ?  89  ALA   B HB1  1 
ATOM   5154 H  HB2  . ALA   B 1 89  ? 49.149 -15.776 -9.161  1.00 13.87 ?  89  ALA   B HB2  1 
ATOM   5155 H  HB3  . ALA   B 1 89  ? 49.182 -14.618 -8.075  1.00 13.87 ?  89  ALA   B HB3  1 
ATOM   5156 N  N    . LYS   B 1 90  ? 49.238 -11.969 -10.054 1.00 12.65 ?  90  LYS   B N    1 
ATOM   5157 C  CA   . LYS   B 1 90  ? 49.052 -10.582 -9.647  1.00 12.62 ?  90  LYS   B CA   1 
ATOM   5158 C  C    . LYS   B 1 90  ? 48.738 -10.509 -8.158  1.00 12.24 ?  90  LYS   B C    1 
ATOM   5159 O  O    . LYS   B 1 90  ? 49.379 -9.756  -7.407  1.00 13.23 ?  90  LYS   B O    1 
ATOM   5160 C  CB   . LYS   B 1 90  ? 47.972 -9.915  -10.497 1.00 14.33 ?  90  LYS   B CB   1 
ATOM   5161 C  CG   . LYS   B 1 90  ? 47.678 -8.472  -10.111 1.00 14.58 ?  90  LYS   B CG   1 
ATOM   5162 C  CD   . LYS   B 1 90  ? 48.894 -7.582  -10.181 1.00 16.96 ?  90  LYS   B CD   1 
ATOM   5163 C  CE   . LYS   B 1 90  ? 48.456 -6.166  -9.908  1.00 18.96 ?  90  LYS   B CE   1 
ATOM   5164 N  NZ   . LYS   B 1 90  ? 49.602 -5.231  -9.806  1.00 18.94 ?  90  LYS   B NZ   1 
ATOM   5165 H  H    . LYS   B 1 90  ? 48.686 -12.264 -10.644 1.00 15.16 ?  90  LYS   B H    1 
ATOM   5166 H  HA   . LYS   B 1 90  ? 49.877 -10.104 -9.796  1.00 15.12 ?  90  LYS   B HA   1 
ATOM   5167 H  HB2  . LYS   B 1 90  ? 48.260 -9.916  -11.427 1.00 17.18 ?  90  LYS   B HB2  1 
ATOM   5168 H  HB3  . LYS   B 1 90  ? 47.146 -10.417 -10.416 1.00 17.18 ?  90  LYS   B HB3  1 
ATOM   5169 H  HG2  . LYS   B 1 90  ? 47.009 -8.110  -10.717 1.00 17.47 ?  90  LYS   B HG2  1 
ATOM   5170 H  HG3  . LYS   B 1 90  ? 47.338 -8.448  -9.201  1.00 17.47 ?  90  LYS   B HG3  1 
ATOM   5171 H  HD2  . LYS   B 1 90  ? 49.537 -7.844  -9.503  1.00 20.33 ?  90  LYS   B HD2  1 
ATOM   5172 H  HD3  . LYS   B 1 90  ? 49.287 -7.625  -11.066 1.00 20.33 ?  90  LYS   B HD3  1 
ATOM   5173 H  HE2  . LYS   B 1 90  ? 47.889 -5.856  -10.635 1.00 22.73 ?  90  LYS   B HE2  1 
ATOM   5174 H  HE3  . LYS   B 1 90  ? 47.970 -6.129  -9.070  1.00 22.73 ?  90  LYS   B HE3  1 
ATOM   5175 H  HZ1  . LYS   B 1 90  ? 49.314 -4.402  -9.648  1.00 22.70 ?  90  LYS   B HZ1  1 
ATOM   5176 H  HZ2  . LYS   B 1 90  ? 50.141 -5.479  -9.142  1.00 22.70 ?  90  LYS   B HZ2  1 
ATOM   5177 H  HZ3  . LYS   B 1 90  ? 50.067 -5.231  -10.568 1.00 22.70 ?  90  LYS   B HZ3  1 
ATOM   5178 N  N    . HIS   B 1 91  ? 47.774 -11.319 -7.715  1.00 10.92 ?  91  HIS   B N    1 
ATOM   5179 C  CA   . HIS   B 1 91  ? 47.307 -11.344 -6.342  1.00 10.98 ?  91  HIS   B CA   1 
ATOM   5180 C  C    . HIS   B 1 91  ? 47.306 -12.770 -5.822  1.00 10.40 ?  91  HIS   B C    1 
ATOM   5181 O  O    . HIS   B 1 91  ? 47.074 -13.724 -6.574  1.00 11.15 ?  91  HIS   B O    1 
ATOM   5182 C  CB   . HIS   B 1 91  ? 45.858 -10.862 -6.229  1.00 12.59 ?  91  HIS   B CB   1 
ATOM   5183 C  CG   . HIS   B 1 91  ? 45.651 -9.451  -6.662  1.00 16.03 ?  91  HIS   B CG   1 
ATOM   5184 N  ND1  . HIS   B 1 91  ? 46.265 -8.380  -6.047  1.00 18.39 ?  91  HIS   B ND1  1 
ATOM   5185 C  CD2  . HIS   B 1 91  ? 44.868 -8.930  -7.632  1.00 18.25 ?  91  HIS   B CD2  1 
ATOM   5186 C  CE1  . HIS   B 1 91  ? 45.883 -7.258  -6.634  1.00 19.36 ?  91  HIS   B CE1  1 
ATOM   5187 N  NE2  . HIS   B 1 91  ? 45.031 -7.565  -7.596  1.00 19.47 ?  91  HIS   B NE2  1 
ATOM   5188 H  H    . HIS   B 1 91  ? 47.355 -11.882 -8.216  1.00 13.08 ?  91  HIS   B H    1 
ATOM   5189 H  HA   . HIS   B 1 91  ? 47.880 -10.788 -5.780  1.00 13.15 ?  91  HIS   B HA   1 
ATOM   5190 H  HB2  . HIS   B 1 91  ? 45.297 -11.424 -6.781  1.00 15.08 ?  91  HIS   B HB2  1 
ATOM   5191 H  HB3  . HIS   B 1 91  ? 45.576 -10.928 -5.300  1.00 15.08 ?  91  HIS   B HB3  1 
ATOM   5192 H  HD1  . HIS   B 1 91  ? 46.815 -8.432  -5.387  1.00 22.04 ?  91  HIS   B HD1  1 
ATOM   5193 H  HD2  . HIS   B 1 91  ? 44.327 -9.396  -8.222  1.00 21.87 ?  91  HIS   B HD2  1 
ATOM   5194 H  HE1  . HIS   B 1 91  ? 46.165 -6.399  -6.403  1.00 23.21 ?  91  HIS   B HE1  1 
ATOM   5195 N  N    . CYS   B 1 92  ? 47.493 -12.904 -4.516  1.00 10.22 ?  92  CYS   B N    1 
ATOM   5196 C  CA   . CYS   B 1 92  ? 47.187 -14.138 -3.802  1.00 10.09 ?  92  CYS   B CA   1 
ATOM   5197 C  C    . CYS   B 1 92  ? 45.965 -13.897 -2.923  1.00 9.74  ?  92  CYS   B C    1 
ATOM   5198 O  O    . CYS   B 1 92  ? 45.967 -12.993 -2.076  1.00 10.93 ?  92  CYS   B O    1 
ATOM   5199 C  CB   . CYS   B 1 92  ? 48.369 -14.596 -2.952  1.00 10.69 ?  92  CYS   B CB   1 
ATOM   5200 S  SG   . CYS   B 1 92  ? 48.005 -16.132 -2.054  1.00 10.75 ?  92  CYS   B SG   1 
ATOM   5201 H  H    . CYS   B 1 92  ? 47.820 -12.285 -4.007  1.00 12.24 ?  92  CYS   B H    1 
ATOM   5202 H  HA   . CYS   B 1 92  ? 46.986 -14.835 -4.445  1.00 12.08 ?  92  CYS   B HA   1 
ATOM   5203 H  HB2  . CYS   B 1 92  ? 49.133 -14.748 -3.522  1.00 12.81 ?  92  CYS   B HB2  1 
ATOM   5204 H  HB3  . CYS   B 1 92  ? 48.569 -13.903 -2.298  1.00 12.81 ?  92  CYS   B HB3  1 
ATOM   5205 H  HG   . CYS   B 1 92  ? 48.979 -16.448 -1.425  1.00 12.88 ?  92  CYS   B HG   1 
ATOM   5206 N  N    . LEU   B 1 93  ? 44.928 -14.705 -3.134  1.00 9.80  ?  93  LEU   B N    1 
ATOM   5207 C  CA   . LEU   B 1 93  ? 43.752 -14.712 -2.274  1.00 9.90  ?  93  LEU   B CA   1 
ATOM   5208 C  C    . LEU   B 1 93  ? 43.981 -15.775 -1.207  1.00 9.48  ?  93  LEU   B C    1 
ATOM   5209 O  O    . LEU   B 1 93  ? 43.931 -16.978 -1.496  1.00 10.24 ?  93  LEU   B O    1 
ATOM   5210 C  CB   . LEU   B 1 93  ? 42.494 -15.014 -3.082  1.00 10.37 ?  93  LEU   B CB   1 
ATOM   5211 C  CG   . LEU   B 1 93  ? 41.191 -15.026 -2.274  1.00 11.04 ?  93  LEU   B CG   1 
ATOM   5212 C  CD1  . LEU   B 1 93  ? 40.837 -13.636 -1.788  1.00 11.57 ?  93  LEU   B CD1  1 
ATOM   5213 C  CD2  . LEU   B 1 93  ? 40.064 -15.619 -3.098  1.00 11.31 ?  93  LEU   B CD2  1 
ATOM   5214 H  H    . LEU   B 1 93  ? 44.889 -15.282 -3.780  1.00 11.74 ?  93  LEU   B H    1 
ATOM   5215 H  HA   . LEU   B 1 93  ? 43.659 -13.847 -1.848  1.00 11.86 ?  93  LEU   B HA   1 
ATOM   5216 H  HB2  . LEU   B 1 93  ? 42.404 -14.330 -3.772  1.00 12.42 ?  93  LEU   B HB2  1 
ATOM   5217 H  HB3  . LEU   B 1 93  ? 42.593 -15.880 -3.498  1.00 12.42 ?  93  LEU   B HB3  1 
ATOM   5218 H  HG   . LEU   B 1 93  ? 41.313 -15.587 -1.497  1.00 13.23 ?  93  LEU   B HG   1 
ATOM   5219 H  HD11 . LEU   B 1 93  ? 39.981 -13.669 -1.337  1.00 13.86 ?  93  LEU   B HD11 1 
ATOM   5220 H  HD12 . LEU   B 1 93  ? 41.524 -13.328 -1.179  1.00 13.86 ?  93  LEU   B HD12 1 
ATOM   5221 H  HD13 . LEU   B 1 93  ? 40.783 -13.037 -2.554  1.00 13.86 ?  93  LEU   B HD13 1 
ATOM   5222 H  HD21 . LEU   B 1 93  ? 39.252 -15.611 -2.568  1.00 13.55 ?  93  LEU   B HD21 1 
ATOM   5223 H  HD22 . LEU   B 1 93  ? 39.942 -15.084 -3.898  1.00 13.55 ?  93  LEU   B HD22 1 
ATOM   5224 H  HD23 . LEU   B 1 93  ? 40.295 -16.529 -3.339  1.00 13.55 ?  93  LEU   B HD23 1 
ATOM   5225 N  N    . HIS   B 1 94  ? 44.255 -15.340 0.015   1.00 9.53  ?  94  HIS   B N    1 
ATOM   5226 C  CA   . HIS   B 1 94  ? 44.473 -16.248 1.133   1.00 9.69  ?  94  HIS   B CA   1 
ATOM   5227 C  C    . HIS   B 1 94  ? 43.111 -16.603 1.712   1.00 10.04 ?  94  HIS   B C    1 
ATOM   5228 O  O    . HIS   B 1 94  ? 42.442 -15.732 2.268   1.00 11.55 ?  94  HIS   B O    1 
ATOM   5229 C  CB   . HIS   B 1 94  ? 45.344 -15.573 2.190   1.00 10.19 ?  94  HIS   B CB   1 
ATOM   5230 C  CG   . HIS   B 1 94  ? 46.726 -15.272 1.720   1.00 10.25 ?  94  HIS   B CG   1 
ATOM   5231 N  ND1  . HIS   B 1 94  ? 47.750 -16.188 1.799   1.00 10.67 ?  94  HIS   B ND1  1 
ATOM   5232 C  CD2  . HIS   B 1 94  ? 47.236 -14.162 1.131   1.00 10.72 ?  94  HIS   B CD2  1 
ATOM   5233 C  CE1  . HIS   B 1 94  ? 48.840 -15.639 1.288   1.00 10.45 ?  94  HIS   B CE1  1 
ATOM   5234 N  NE2  . HIS   B 1 94  ? 48.557 -14.414 0.876   1.00 10.69 ?  94  HIS   B NE2  1 
ATOM   5235 H  H    . HIS   B 1 94  ? 44.330 -14.506 0.224   1.00 11.42 ?  94  HIS   B H    1 
ATOM   5236 H  HA   . HIS   B 1 94  ? 44.909 -17.058 0.824   1.00 11.60 ?  94  HIS   B HA   1 
ATOM   5237 H  HB2  . HIS   B 1 94  ? 44.929 -14.739 2.449   1.00 12.21 ?  94  HIS   B HB2  1 
ATOM   5238 H  HB3  . HIS   B 1 94  ? 45.415 -16.164 2.954   1.00 12.21 ?  94  HIS   B HB3  1 
ATOM   5239 H  HD2  . HIS   B 1 94  ? 46.778 -13.378 0.938   1.00 12.84 ?  94  HIS   B HD2  1 
ATOM   5240 H  HE1  . HIS   B 1 94  ? 49.672 -16.054 1.226   1.00 12.51 ?  94  HIS   B HE1  1 
ATOM   5241 H  HE2  . HIS   B 1 94  ? 49.113 -13.870 0.510   1.00 12.81 ?  94  HIS   B HE2  1 
ATOM   5242 N  N    . VAL   B 1 95  ? 42.678 -17.854 1.556   1.00 9.99  ?  95  VAL   B N    1 
ATOM   5243 C  CA   . VAL   B 1 95  ? 41.352 -18.293 1.989   1.00 10.01 ?  95  VAL   B CA   1 
ATOM   5244 C  C    . VAL   B 1 95  ? 41.520 -19.327 3.088   1.00 10.40 ?  95  VAL   B C    1 
ATOM   5245 O  O    . VAL   B 1 95  ? 42.294 -20.280 2.933   1.00 11.04 ?  95  VAL   B O    1 
ATOM   5246 C  CB   . VAL   B 1 95  ? 40.536 -18.901 0.831   1.00 10.49 ?  95  VAL   B CB   1 
ATOM   5247 C  CG1  . VAL   B 1 95  ? 39.155 -19.351 1.317   1.00 11.77 ?  95  VAL   B CG1  1 
ATOM   5248 C  CG2  . VAL   B 1 95  ? 40.407 -17.926 -0.314  1.00 10.49 ?  95  VAL   B CG2  1 
ATOM   5249 H  H    . VAL   B 1 95  ? 43.143 -18.479 1.193   1.00 11.97 ?  95  VAL   B H    1 
ATOM   5250 H  HA   . VAL   B 1 95  ? 40.857 -17.538 2.347   1.00 11.98 ?  95  VAL   B HA   1 
ATOM   5251 H  HB   . VAL   B 1 95  ? 40.996 -19.682 0.499   1.00 12.57 ?  95  VAL   B HB   1 
ATOM   5252 H  HG11 . VAL   B 1 95  ? 38.595 -19.551 0.544   1.00 14.10 ?  95  VAL   B HG11 1 
ATOM   5253 H  HG12 . VAL   B 1 95  ? 39.249 -20.148 1.862   1.00 14.10 ?  95  VAL   B HG12 1 
ATOM   5254 H  HG13 . VAL   B 1 95  ? 38.747 -18.639 1.835   1.00 14.10 ?  95  VAL   B HG13 1 
ATOM   5255 H  HG21 . VAL   B 1 95  ? 39.837 -18.321 -0.996  1.00 12.57 ?  95  VAL   B HG21 1 
ATOM   5256 H  HG22 . VAL   B 1 95  ? 40.007 -17.107 0.015   1.00 12.57 ?  95  VAL   B HG22 1 
ATOM   5257 H  HG23 . VAL   B 1 95  ? 41.285 -17.752 -0.674  1.00 12.57 ?  95  VAL   B HG23 1 
ATOM   5258 N  N    . VAL   B 1 96  ? 40.788 -19.152 4.184   1.00 10.82 ?  96  VAL   B N    1 
ATOM   5259 C  CA   . VAL   B 1 96  ? 40.870 -20.065 5.323   1.00 11.35 ?  96  VAL   B CA   1 
ATOM   5260 C  C    . VAL   B 1 96  ? 39.682 -21.023 5.276   1.00 11.81 ?  96  VAL   B C    1 
ATOM   5261 O  O    . VAL   B 1 96  ? 38.565 -20.672 5.664   1.00 12.55 ?  96  VAL   B O    1 
ATOM   5262 C  CB   . VAL   B 1 96  ? 40.925 -19.318 6.658   1.00 12.19 ?  96  VAL   B CB   1 
ATOM   5263 C  CG1  . VAL   B 1 96  ? 41.100 -20.314 7.800   1.00 12.98 ?  96  VAL   B CG1  1 
ATOM   5264 C  CG2  . VAL   B 1 96  ? 42.045 -18.292 6.666   1.00 12.81 ?  96  VAL   B CG2  1 
ATOM   5265 H  H    . VAL   B 1 96  ? 40.228 -18.511 4.296   1.00 12.96 ?  96  VAL   B H    1 
ATOM   5266 H  HA   . VAL   B 1 96  ? 41.683 -20.593 5.248   1.00 13.60 ?  96  VAL   B HA   1 
ATOM   5267 H  HB   . VAL   B 1 96  ? 40.087 -18.849 6.795   1.00 14.61 ?  96  VAL   B HB   1 
ATOM   5268 H  HG11 . VAL   B 1 96  ? 41.296 -19.827 8.618   1.00 15.55 ?  96  VAL   B HG11 1 
ATOM   5269 H  HG12 . VAL   B 1 96  ? 40.283 -20.824 7.909   1.00 15.55 ?  96  VAL   B HG12 1 
ATOM   5270 H  HG13 . VAL   B 1 96  ? 41.838 -20.910 7.590   1.00 15.55 ?  96  VAL   B HG13 1 
ATOM   5271 H  HG21 . VAL   B 1 96  ? 42.095 -17.880 7.546   1.00 15.36 ?  96  VAL   B HG21 1 
ATOM   5272 H  HG22 . VAL   B 1 96  ? 42.884 -18.733 6.463   1.00 15.36 ?  96  VAL   B HG22 1 
ATOM   5273 H  HG23 . VAL   B 1 96  ? 41.860 -17.611 5.998   1.00 15.36 ?  96  VAL   B HG23 1 
ATOM   5274 N  N    . GLY   B 1 97  ? 39.922 -22.256 4.839   1.00 11.89 ?  97  GLY   B N    1 
ATOM   5275 C  CA   . GLY   B 1 97  ? 38.946 -23.311 4.992   1.00 12.68 ?  97  GLY   B CA   1 
ATOM   5276 C  C    . GLY   B 1 97  ? 39.072 -23.929 6.368   1.00 13.77 ?  97  GLY   B C    1 
ATOM   5277 O  O    . GLY   B 1 97  ? 40.113 -23.806 7.028   1.00 14.19 ?  97  GLY   B O    1 
ATOM   5278 H  H    . GLY   B 1 97  ? 40.651 -22.500 4.446   1.00 14.25 ?  97  GLY   B H    1 
ATOM   5279 H  HA2  . GLY   B 1 97  ? 38.052 -22.940 4.878   1.00 15.19 ?  97  GLY   B HA2  1 
ATOM   5280 H  HA3  . GLY   B 1 97  ? 39.087 -23.990 4.313   1.00 15.19 ?  97  GLY   B HA3  1 
ATOM   5281 N  N    . PRO   B 1 98  ? 38.025 -24.612 6.830   1.00 14.71 ?  98  PRO   B N    1 
ATOM   5282 C  CA   . PRO   B 1 98  ? 38.122 -25.304 8.118   1.00 15.63 ?  98  PRO   B CA   1 
ATOM   5283 C  C    . PRO   B 1 98  ? 39.145 -26.429 8.072   1.00 15.47 ?  98  PRO   B C    1 
ATOM   5284 O  O    . PRO   B 1 98  ? 39.253 -27.161 7.090   1.00 15.65 ?  98  PRO   B O    1 
ATOM   5285 C  CB   . PRO   B 1 98  ? 36.702 -25.841 8.336   1.00 15.90 ?  98  PRO   B CB   1 
ATOM   5286 C  CG   . PRO   B 1 98  ? 36.133 -25.975 6.967   1.00 15.57 ?  98  PRO   B CG   1 
ATOM   5287 C  CD   . PRO   B 1 98  ? 36.705 -24.806 6.200   1.00 14.90 ?  98  PRO   B CD   1 
ATOM   5288 H  HA   . PRO   B 1 98  ? 38.353 -24.680 8.819   1.00 18.73 ?  98  PRO   B HA   1 
ATOM   5289 H  HB2  . PRO   B 1 98  ? 36.747 -26.707 8.776   1.00 19.06 ?  98  PRO   B HB2  1 
ATOM   5290 H  HB3  . PRO   B 1 98  ? 36.192 -25.211 8.862   1.00 19.06 ?  98  PRO   B HB3  1 
ATOM   5291 H  HG2  . PRO   B 1 98  ? 36.418 -26.818 6.574   1.00 18.66 ?  98  PRO   B HG2  1 
ATOM   5292 H  HG3  . PRO   B 1 98  ? 35.167 -25.924 7.008   1.00 18.66 ?  98  PRO   B HG3  1 
ATOM   5293 H  HD2  . PRO   B 1 98  ? 36.796 -25.034 5.258   1.00 17.86 ?  98  PRO   B HD2  1 
ATOM   5294 H  HD3  . PRO   B 1 98  ? 36.153 -24.019 6.322   1.00 17.86 ?  98  PRO   B HD3  1 
ATOM   5295 N  N    . ASN   B 1 99  ? 39.892 -26.566 9.159   1.00 16.52 ?  99  ASN   B N    1 
ATOM   5296 C  CA   . ASN   B 1 99  ? 40.874 -27.635 9.316   1.00 17.53 ?  99  ASN   B CA   1 
ATOM   5297 C  C    . ASN   B 1 99  ? 40.249 -28.720 10.192  1.00 20.13 ?  99  ASN   B C    1 
ATOM   5298 O  O    . ASN   B 1 99  ? 40.181 -28.579 11.416  1.00 20.71 ?  99  ASN   B O    1 
ATOM   5299 C  CB   . ASN   B 1 99  ? 42.144 -27.076 9.944   1.00 17.81 ?  99  ASN   B CB   1 
ATOM   5300 C  CG   . ASN   B 1 99  ? 43.282 -28.071 9.941   1.00 18.72 ?  99  ASN   B CG   1 
ATOM   5301 O  OD1  . ASN   B 1 99  ? 43.069 -29.265 10.105  1.00 19.40 ?  99  ASN   B OD1  1 
ATOM   5302 N  ND2  . ASN   B 1 99  ? 44.494 -27.585 9.752   1.00 18.77 ?  99  ASN   B ND2  1 
ATOM   5303 H  H    . ASN   B 1 99  ? 39.843 -26.040 9.834   1.00 19.80 ?  99  ASN   B H    1 
ATOM   5304 H  HA   . ASN   B 1 99  ? 41.085 -28.023 8.454   1.00 21.02 ?  99  ASN   B HA   1 
ATOM   5305 H  HB2  . ASN   B 1 99  ? 42.419 -26.299 9.449   1.00 21.35 ?  99  ASN   B HB2  1 
ATOM   5306 H  HB3  . ASN   B 1 99  ? 41.953 -26.841 10.868  1.00 21.35 ?  99  ASN   B HB3  1 
ATOM   5307 H  HD21 . ASN   B 1 99  ? 45.169 -28.113 9.738   1.00 22.50 ?  99  ASN   B HD21 1 
ATOM   5308 H  HD22 . ASN   B 1 99  ? 44.598 -26.741 9.645   1.00 22.50 ?  99  ASN   B HD22 1 
ATOM   5309 N  N    A VAL   B 1 100 ? 39.777 -29.799 9.560   0.72 22.03 ?  100 VAL   B N    1 
ATOM   5310 N  N    B VAL   B 1 100 ? 39.787 -29.800 9.555   0.28 22.09 ?  100 VAL   B N    1 
ATOM   5311 C  CA   A VAL   B 1 100 ? 39.161 -30.891 10.314  0.72 24.44 ?  100 VAL   B CA   1 
ATOM   5312 C  CA   B VAL   B 1 100 ? 39.169 -30.903 10.289  0.28 24.12 ?  100 VAL   B CA   1 
ATOM   5313 C  C    A VAL   B 1 100 ? 40.172 -31.553 11.242  0.72 24.83 ?  100 VAL   B C    1 
ATOM   5314 C  C    B VAL   B 1 100 ? 40.170 -31.557 11.231  0.28 24.77 ?  100 VAL   B C    1 
ATOM   5315 O  O    A VAL   B 1 100 ? 39.805 -32.057 12.311  0.72 25.42 ?  100 VAL   B O    1 
ATOM   5316 O  O    B VAL   B 1 100 ? 39.796 -32.051 12.302  0.28 25.06 ?  100 VAL   B O    1 
ATOM   5317 C  CB   A VAL   B 1 100 ? 38.494 -31.902 9.358   0.72 26.53 ?  100 VAL   B CB   1 
ATOM   5318 C  CB   B VAL   B 1 100 ? 38.544 -31.916 9.306   0.28 25.45 ?  100 VAL   B CB   1 
ATOM   5319 C  CG1  A VAL   B 1 100 ? 37.977 -33.108 10.127  0.72 27.55 ?  100 VAL   B CG1  1 
ATOM   5320 C  CG1  B VAL   B 1 100 ? 38.004 -33.131 10.050  0.28 25.98 ?  100 VAL   B CG1  1 
ATOM   5321 C  CG2  A VAL   B 1 100 ? 37.359 -31.240 8.592   0.72 26.80 ?  100 VAL   B CG2  1 
ATOM   5322 C  CG2  B VAL   B 1 100 ? 37.439 -31.253 8.498   0.28 25.82 ?  100 VAL   B CG2  1 
ATOM   5323 H  H    A VAL   B 1 100 ? 39.789 -29.917 8.706   0.72 26.41 ?  100 VAL   B H    1 
ATOM   5324 H  H    B VAL   B 1 100 ? 39.817 -29.915 8.703   0.28 26.49 ?  100 VAL   B H    1 
ATOM   5325 H  HA   A VAL   B 1 100 ? 38.456 -30.521 10.866  0.72 29.31 ?  100 VAL   B HA   1 
ATOM   5326 H  HA   B VAL   B 1 100 ? 38.447 -30.549 10.830  0.28 28.92 ?  100 VAL   B HA   1 
ATOM   5327 H  HB   A VAL   B 1 100 ? 39.149 -32.215 8.717   0.72 31.81 ?  100 VAL   B HB   1 
ATOM   5328 H  HB   B VAL   B 1 100 ? 39.225 -32.224 8.688   0.28 30.52 ?  100 VAL   B HB   1 
ATOM   5329 H  HG11 A VAL   B 1 100 ? 37.387 -33.622 9.550   0.72 33.03 ?  100 VAL   B HG11 1 
ATOM   5330 H  HG11 B VAL   B 1 100 ? 37.441 -33.645 9.447   0.28 31.15 ?  100 VAL   B HG11 1 
ATOM   5331 H  HG12 A VAL   B 1 100 ? 38.726 -33.660 10.402  0.72 33.03 ?  100 VAL   B HG12 1 
ATOM   5332 H  HG12 B VAL   B 1 100 ? 38.746 -33.678 10.351  0.28 31.15 ?  100 VAL   B HG12 1 
ATOM   5333 H  HG13 A VAL   B 1 100 ? 37.486 -32.803 10.907  0.72 33.03 ?  100 VAL   B HG13 1 
ATOM   5334 H  HG13 B VAL   B 1 100 ? 37.481 -32.830 10.809  0.28 31.15 ?  100 VAL   B HG13 1 
ATOM   5335 H  HG21 A VAL   B 1 100 ? 36.953 -31.896 8.002   0.72 32.14 ?  100 VAL   B HG21 1 
ATOM   5336 H  HG21 B VAL   B 1 100 ? 37.040 -31.911 7.908   0.28 30.96 ?  100 VAL   B HG21 1 
ATOM   5337 H  HG22 A VAL   B 1 100 ? 36.699 -30.914 9.225   0.72 32.14 ?  100 VAL   B HG22 1 
ATOM   5338 H  HG22 B VAL   B 1 100 ? 36.769 -30.906 9.108   0.28 30.96 ?  100 VAL   B HG22 1 
ATOM   5339 H  HG23 A VAL   B 1 100 ? 37.715 -30.504 8.074   0.72 32.14 ?  100 VAL   B HG23 1 
ATOM   5340 H  HG23 B VAL   B 1 100 ? 37.820 -30.529 7.978   0.28 30.96 ?  100 VAL   B HG23 1 
ATOM   5341 N  N    . ASN   B 1 101 ? 41.450 -31.582 10.853  1.00 25.19 ?  101 ASN   B N    1 
ATOM   5342 C  CA   . ASN   B 1 101 ? 42.490 -32.115 11.733  1.00 27.04 ?  101 ASN   B CA   1 
ATOM   5343 C  C    . ASN   B 1 101 ? 42.689 -31.274 12.988  1.00 29.45 ?  101 ASN   B C    1 
ATOM   5344 O  O    . ASN   B 1 101 ? 43.343 -31.741 13.929  1.00 30.55 ?  101 ASN   B O    1 
ATOM   5345 C  CB   . ASN   B 1 101 ? 43.819 -32.239 10.984  1.00 26.89 ?  101 ASN   B CB   1 
ATOM   5346 C  CG   . ASN   B 1 101 ? 43.826 -33.392 10.002  1.00 26.47 ?  101 ASN   B CG   1 
ATOM   5347 O  OD1  . ASN   B 1 101 ? 43.167 -34.401 10.220  1.00 27.14 ?  101 ASN   B OD1  1 
ATOM   5348 N  ND2  . ASN   B 1 101 ? 44.561 -33.242 8.908   1.00 26.07 ?  101 ASN   B ND2  1 
ATOM   5349 H  H    A ASN   B 1 101 ? 41.731 -31.317 10.084  0.72 30.21 ?  101 ASN   B H    1 
ATOM   5350 H  H    B ASN   B 1 101 ? 41.736 -31.304 10.091  0.28 30.21 ?  101 ASN   B H    1 
ATOM   5351 H  HA   . ASN   B 1 101 ? 42.226 -33.002 12.013  1.00 32.43 ?  101 ASN   B HA   1 
ATOM   5352 H  HB2  . ASN   B 1 101 ? 43.988 -31.425 10.488  1.00 32.24 ?  101 ASN   B HB2  1 
ATOM   5353 H  HB3  . ASN   B 1 101 ? 44.530 -32.388 11.630  1.00 32.24 ?  101 ASN   B HB3  1 
ATOM   5354 H  HD21 . ASN   B 1 101 ? 44.597 -33.872 8.324   1.00 31.27 ?  101 ASN   B HD21 1 
ATOM   5355 H  HD22 . ASN   B 1 101 ? 45.001 -32.515 8.785   1.00 31.27 ?  101 ASN   B HD22 1 
ATOM   5356 N  N    . LYS   B 1 102 ? 42.159 -30.049 13.014  1.00 31.86 ?  102 LYS   B N    1 
ATOM   5357 C  CA   . LYS   B 1 102 ? 42.125 -29.213 14.206  1.00 34.55 ?  102 LYS   B CA   1 
ATOM   5358 C  C    . LYS   B 1 102 ? 40.741 -29.168 14.842  1.00 34.18 ?  102 LYS   B C    1 
ATOM   5359 O  O    . LYS   B 1 102 ? 40.512 -28.359 15.747  1.00 34.76 ?  102 LYS   B O    1 
ATOM   5360 C  CB   . LYS   B 1 102 ? 42.567 -27.788 13.870  1.00 37.70 ?  102 LYS   B CB   1 
ATOM   5361 C  CG   . LYS   B 1 102 ? 44.034 -27.635 13.514  1.00 40.68 ?  102 LYS   B CG   1 
ATOM   5362 C  CD   . LYS   B 1 102 ? 44.311 -26.219 13.029  1.00 43.46 ?  102 LYS   B CD   1 
ATOM   5363 C  CE   . LYS   B 1 102 ? 45.796 -25.944 12.880  1.00 45.47 ?  102 LYS   B CE   1 
ATOM   5364 N  NZ   . LYS   B 1 102 ? 46.042 -24.549 12.415  1.00 46.67 ?  102 LYS   B NZ   1 
ATOM   5365 H  H    . LYS   B 1 102 ? 41.802 -29.670 12.330  1.00 38.20 ?  102 LYS   B H    1 
ATOM   5366 H  HA   . LYS   B 1 102 ? 42.746 -29.569 14.858  1.00 41.43 ?  102 LYS   B HA   1 
ATOM   5367 H  HB2  . LYS   B 1 102 ? 42.047 -27.474 13.114  1.00 45.22 ?  102 LYS   B HB2  1 
ATOM   5368 H  HB3  . LYS   B 1 102 ? 42.393 -27.221 14.639  1.00 45.22 ?  102 LYS   B HB3  1 
ATOM   5369 H  HG2  . LYS   B 1 102 ? 44.579 -27.803 14.299  1.00 48.80 ?  102 LYS   B HG2  1 
ATOM   5370 H  HG3  . LYS   B 1 102 ? 44.262 -28.254 12.803  1.00 48.80 ?  102 LYS   B HG3  1 
ATOM   5371 H  HD2  . LYS   B 1 102 ? 43.891 -26.092 12.163  1.00 52.13 ?  102 LYS   B HD2  1 
ATOM   5372 H  HD3  . LYS   B 1 102 ? 43.949 -25.587 13.670  1.00 52.13 ?  102 LYS   B HD3  1 
ATOM   5373 H  HE2  . LYS   B 1 102 ? 46.232 -26.061 13.739  1.00 54.54 ?  102 LYS   B HE2  1 
ATOM   5374 H  HE3  . LYS   B 1 102 ? 46.171 -26.554 12.226  1.00 54.54 ?  102 LYS   B HE3  1 
ATOM   5375 H  HZ1  . LYS   B 1 102 ? 46.917 -24.406 12.333  1.00 55.98 ?  102 LYS   B HZ1  1 
ATOM   5376 H  HZ2  . LYS   B 1 102 ? 45.652 -24.419 11.625  1.00 55.98 ?  102 LYS   B HZ2  1 
ATOM   5377 H  HZ3  . LYS   B 1 102 ? 45.707 -23.970 13.002  1.00 55.98 ?  102 LYS   B HZ3  1 
ATOM   5378 N  N    . GLY   B 1 103 ? 39.811 -29.999 14.379  1.00 33.59 ?  103 GLY   B N    1 
ATOM   5379 C  CA   . GLY   B 1 103 ? 38.481 -30.054 14.951  1.00 33.14 ?  103 GLY   B CA   1 
ATOM   5380 C  C    . GLY   B 1 103 ? 37.535 -28.967 14.496  1.00 32.12 ?  103 GLY   B C    1 
ATOM   5381 O  O    . GLY   B 1 103 ? 36.442 -28.845 15.061  1.00 32.57 ?  103 GLY   B O    1 
ATOM   5382 H  H    . GLY   B 1 103 ? 39.930 -30.542 13.726  1.00 40.29 ?  103 GLY   B H    1 
ATOM   5383 H  HA2  . GLY   B 1 103 ? 38.079 -30.906 14.726  1.00 39.74 ?  103 GLY   B HA2  1 
ATOM   5384 H  HA3  . GLY   B 1 103 ? 38.552 -30.001 15.917  1.00 39.74 ?  103 GLY   B HA3  1 
ATOM   5385 N  N    A GLU   B 1 104 ? 37.918 -28.172 13.499  0.72 30.96 ?  104 GLU   B N    1 
ATOM   5386 N  N    B GLU   B 1 104 ? 37.906 -28.181 13.491  0.28 31.46 ?  104 GLU   B N    1 
ATOM   5387 C  CA   A GLU   B 1 104 ? 37.082 -27.071 13.049  0.72 29.70 ?  104 GLU   B CA   1 
ATOM   5388 C  CA   B GLU   B 1 104 ? 37.048 -27.103 13.026  0.28 30.61 ?  104 GLU   B CA   1 
ATOM   5389 C  C    A GLU   B 1 104 ? 35.895 -27.591 12.239  0.72 30.07 ?  104 GLU   B C    1 
ATOM   5390 C  C    B GLU   B 1 104 ? 35.891 -27.653 12.198  0.28 30.59 ?  104 GLU   B C    1 
ATOM   5391 O  O    A GLU   B 1 104 ? 35.931 -28.678 11.654  0.72 30.60 ?  104 GLU   B O    1 
ATOM   5392 O  O    B GLU   B 1 104 ? 35.978 -28.730 11.600  0.28 30.77 ?  104 GLU   B O    1 
ATOM   5393 C  CB   A GLU   B 1 104 ? 37.915 -26.071 12.244  0.72 28.43 ?  104 GLU   B CB   1 
ATOM   5394 C  CB   B GLU   B 1 104 ? 37.863 -26.088 12.225  0.28 29.82 ?  104 GLU   B CB   1 
ATOM   5395 C  CG   A GLU   B 1 104 ? 39.012 -25.425 13.082  0.72 27.03 ?  104 GLU   B CG   1 
ATOM   5396 C  CG   B GLU   B 1 104 ? 38.955 -25.425 13.055  0.28 29.07 ?  104 GLU   B CG   1 
ATOM   5397 C  CD   A GLU   B 1 104 ? 39.952 -24.546 12.284  0.72 25.58 ?  104 GLU   B CD   1 
ATOM   5398 C  CD   B GLU   B 1 104 ? 39.890 -24.563 12.232  0.28 28.42 ?  104 GLU   B CD   1 
ATOM   5399 O  OE1  A GLU   B 1 104 ? 39.939 -24.606 11.036  0.72 23.87 ?  104 GLU   B OE1  1 
ATOM   5400 O  OE1  B GLU   B 1 104 ? 39.803 -24.599 10.986  0.28 27.93 ?  104 GLU   B OE1  1 
ATOM   5401 O  OE2  A GLU   B 1 104 ? 40.712 -23.787 12.919  0.72 25.55 -1 104 GLU   B OE2  1 
ATOM   5402 O  OE2  B GLU   B 1 104 ? 40.715 -23.847 12.836  0.28 28.33 -1 104 GLU   B OE2  1 
ATOM   5403 H  H    A GLU   B 1 104 ? 38.659 -28.250 13.073  0.72 37.13 ?  104 GLU   B H    1 
ATOM   5404 H  H    B GLU   B 1 104 ? 38.651 -28.249 13.067  0.28 37.73 ?  104 GLU   B H    1 
ATOM   5405 H  HA   A GLU   B 1 104 ? 36.734 -26.605 13.825  0.72 35.62 ?  104 GLU   B HA   1 
ATOM   5406 H  HA   B GLU   B 1 104 ? 36.674 -26.645 13.794  0.28 36.71 ?  104 GLU   B HA   1 
ATOM   5407 H  HB2  A GLU   B 1 104 ? 38.336 -26.531 11.501  0.72 34.09 ?  104 GLU   B HB2  1 
ATOM   5408 H  HB2  B GLU   B 1 104 ? 38.286 -26.539 11.478  0.28 35.77 ?  104 GLU   B HB2  1 
ATOM   5409 H  HB3  A GLU   B 1 104 ? 37.335 -25.366 11.914  0.72 34.09 ?  104 GLU   B HB3  1 
ATOM   5410 H  HB3  B GLU   B 1 104 ? 37.270 -25.391 11.900  0.28 35.77 ?  104 GLU   B HB3  1 
ATOM   5411 H  HG2  A GLU   B 1 104 ? 38.603 -24.871 13.766  0.72 32.42 ?  104 GLU   B HG2  1 
ATOM   5412 H  HG2  B GLU   B 1 104 ? 38.541 -24.860 13.728  0.28 34.86 ?  104 GLU   B HG2  1 
ATOM   5413 H  HG3  A GLU   B 1 104 ? 39.545 -26.120 13.498  0.72 32.42 ?  104 GLU   B HG3  1 
ATOM   5414 H  HG3  B GLU   B 1 104 ? 39.485 -26.114 13.488  0.28 34.86 ?  104 GLU   B HG3  1 
ATOM   5415 N  N    A ASP   B 1 105 ? 34.829 -26.792 12.216  0.72 29.76 ?  105 ASP   B N    1 
ATOM   5416 N  N    B ASP   B 1 105 ? 34.796 -26.896 12.173  0.28 30.20 ?  105 ASP   B N    1 
ATOM   5417 C  CA   A ASP   B 1 105 ? 33.553 -27.241 11.672  0.72 30.25 ?  105 ASP   B CA   1 
ATOM   5418 C  CA   B ASP   B 1 105 ? 33.542 -27.373 11.603  0.28 30.04 ?  105 ASP   B CA   1 
ATOM   5419 C  C    A ASP   B 1 105 ? 33.614 -27.300 10.150  0.72 28.21 ?  105 ASP   B C    1 
ATOM   5420 C  C    B ASP   B 1 105 ? 33.625 -27.383 10.081  0.28 28.99 ?  105 ASP   B C    1 
ATOM   5421 O  O    A ASP   B 1 105 ? 33.783 -26.271 9.488   0.72 27.09 ?  105 ASP   B O    1 
ATOM   5422 O  O    B ASP   B 1 105 ? 33.848 -26.342 9.454   0.28 28.62 ?  105 ASP   B O    1 
ATOM   5423 C  CB   A ASP   B 1 105 ? 32.445 -26.292 12.122  0.72 33.00 ?  105 ASP   B CB   1 
ATOM   5424 C  CB   B ASP   B 1 105 ? 32.394 -26.480 12.070  0.28 30.86 ?  105 ASP   B CB   1 
ATOM   5425 C  CG   A ASP   B 1 105 ? 31.068 -26.750 11.683  0.72 35.37 ?  105 ASP   B CG   1 
ATOM   5426 C  CG   B ASP   B 1 105 ? 31.032 -27.057 11.730  0.28 31.62 ?  105 ASP   B CG   1 
ATOM   5427 O  OD1  A ASP   B 1 105 ? 30.955 -27.864 11.130  0.72 35.65 ?  105 ASP   B OD1  1 
ATOM   5428 O  OD1  B ASP   B 1 105 ? 30.979 -28.095 11.037  0.28 31.78 ?  105 ASP   B OD1  1 
ATOM   5429 O  OD2  A ASP   B 1 105 ? 30.095 -25.992 11.889  0.72 36.66 -1 105 ASP   B OD2  1 
ATOM   5430 O  OD2  B ASP   B 1 105 ? 30.013 -26.477 12.162  0.28 31.83 -1 105 ASP   B OD2  1 
ATOM   5431 H  H    A ASP   B 1 105 ? 34.820 -25.982 12.509  0.72 35.69 ?  105 ASP   B H    1 
ATOM   5432 H  H    B ASP   B 1 105 ? 34.757 -26.097 12.478  0.28 36.22 ?  105 ASP   B H    1 
ATOM   5433 H  HA   A ASP   B 1 105 ? 33.352 -28.129 12.008  0.72 36.28 ?  105 ASP   B HA   1 
ATOM   5434 H  HA   B ASP   B 1 105 ? 33.364 -28.277 11.907  0.28 36.03 ?  105 ASP   B HA   1 
ATOM   5435 H  HB2  A ASP   B 1 105 ? 32.462 -26.224 13.091  0.72 39.57 ?  105 ASP   B HB2  1 
ATOM   5436 H  HB2  B ASP   B 1 105 ? 32.442 -26.376 13.034  0.28 37.01 ?  105 ASP   B HB2  1 
ATOM   5437 H  HB3  A ASP   B 1 105 ? 32.594 -25.421 11.726  0.72 39.57 ?  105 ASP   B HB3  1 
ATOM   5438 H  HB3  B ASP   B 1 105 ? 32.471 -25.611 11.642  0.28 37.01 ?  105 ASP   B HB3  1 
ATOM   5439 N  N    A ILE   B 1 106 ? 33.446 -28.505 9.598   0.72 27.51 ?  106 ILE   B N    1 
ATOM   5440 N  N    B ILE   B 1 106 ? 33.434 -28.565 9.488   0.28 28.25 ?  106 ILE   B N    1 
ATOM   5441 C  CA   A ILE   B 1 106 ? 33.452 -28.690 8.152   0.72 26.57 ?  106 ILE   B CA   1 
ATOM   5442 C  CA   B ILE   B 1 106 ? 33.454 -28.705 8.037   0.28 27.58 ?  106 ILE   B CA   1 
ATOM   5443 C  C    A ILE   B 1 106 ? 32.359 -27.871 7.471   0.72 25.30 ?  106 ILE   B C    1 
ATOM   5444 C  C    B ILE   B 1 106 ? 32.352 -27.886 7.375   0.28 26.87 ?  106 ILE   B C    1 
ATOM   5445 O  O    A ILE   B 1 106 ? 32.469 -27.563 6.280   0.72 24.64 ?  106 ILE   B O    1 
ATOM   5446 O  O    B ILE   B 1 106 ? 32.433 -27.595 6.177   0.28 26.62 ?  106 ILE   B O    1 
ATOM   5447 C  CB   A ILE   B 1 106 ? 33.355 -30.198 7.820   0.72 27.37 ?  106 ILE   B CB   1 
ATOM   5448 C  CB   B ILE   B 1 106 ? 33.373 -30.202 7.657   0.28 27.75 ?  106 ILE   B CB   1 
ATOM   5449 C  CG1  A ILE   B 1 106 ? 33.616 -30.453 6.335   0.72 27.77 ?  106 ILE   B CG1  1 
ATOM   5450 C  CG1  B ILE   B 1 106 ? 33.661 -30.408 6.167   0.28 27.77 ?  106 ILE   B CG1  1 
ATOM   5451 C  CG2  A ILE   B 1 106 ? 31.993 -30.753 8.224   0.72 28.06 ?  106 ILE   B CG2  1 
ATOM   5452 C  CG2  B ILE   B 1 106 ? 32.009 -30.775 8.019   0.28 28.00 ?  106 ILE   B CG2  1 
ATOM   5453 C  CD1  A ILE   B 1 106 ? 34.977 -29.992 5.875   0.72 27.69 ?  106 ILE   B CD1  1 
ATOM   5454 C  CD1  B ILE   B 1 106 ? 35.011 -29.889 5.732   0.28 27.76 ?  106 ILE   B CD1  1 
ATOM   5455 H  H    A ILE   B 1 106 ? 33.330 -29.228 10.046  0.72 32.99 ?  106 ILE   B H    1 
ATOM   5456 H  H    B ILE   B 1 106 ? 33.302 -29.301 9.909   0.28 33.87 ?  106 ILE   B H    1 
ATOM   5457 H  HA   A ILE   B 1 106 ? 34.298 -28.371 7.817   0.72 31.86 ?  106 ILE   B HA   1 
ATOM   5458 H  HA   B ILE   B 1 106 ? 34.298 -28.362 7.715   0.28 33.07 ?  106 ILE   B HA   1 
ATOM   5459 H  HB   A ILE   B 1 106 ? 34.032 -30.668 8.332   0.72 32.83 ?  106 ILE   B HB   1 
ATOM   5460 H  HB   B ILE   B 1 106 ? 34.046 -30.681 8.164   0.28 33.27 ?  106 ILE   B HB   1 
ATOM   5461 H  HG12 A ILE   B 1 106 ? 33.557 -31.408 6.165   0.72 33.31 ?  106 ILE   B HG12 1 
ATOM   5462 H  HG12 B ILE   B 1 106 ? 33.636 -31.360 5.973   0.28 33.31 ?  106 ILE   B HG12 1 
ATOM   5463 H  HG13 A ILE   B 1 106 ? 32.950 -29.986 5.811   0.72 33.31 ?  106 ILE   B HG13 1 
ATOM   5464 H  HG13 B ILE   B 1 106 ? 32.984 -29.950 5.647   0.28 33.31 ?  106 ILE   B HG13 1 
ATOM   5465 H  HG21 A ILE   B 1 106 ? 32.005 -31.720 8.136   0.72 33.65 ?  106 ILE   B HG21 1 
ATOM   5466 H  HG21 B ILE   B 1 106 ? 32.035 -31.739 7.918   0.28 33.58 ?  106 ILE   B HG21 1 
ATOM   5467 H  HG22 A ILE   B 1 106 ? 31.813 -30.510 9.147   0.72 33.65 ?  106 ILE   B HG22 1 
ATOM   5468 H  HG22 B ILE   B 1 106 ? 31.805 -30.545 8.939   0.28 33.58 ?  106 ILE   B HG22 1 
ATOM   5469 H  HG23 A ILE   B 1 106 ? 31.311 -30.378 7.645   0.72 33.65 ?  106 ILE   B HG23 1 
ATOM   5470 H  HG23 B ILE   B 1 106 ? 31.339 -30.399 7.428   0.28 33.58 ?  106 ILE   B HG23 1 
ATOM   5471 H  HD11 A ILE   B 1 106 ? 35.176 -30.400 5.019   0.72 33.20 ?  106 ILE   B HD11 1 
ATOM   5472 H  HD11 B ILE   B 1 106 ? 35.236 -30.279 4.875   0.28 33.29 ?  106 ILE   B HD11 1 
ATOM   5473 H  HD12 A ILE   B 1 106 ? 34.971 -29.025 5.786   0.72 33.20 ?  106 ILE   B HD12 1 
ATOM   5474 H  HD12 B ILE   B 1 106 ? 34.968 -28.923 5.656   0.28 33.29 ?  106 ILE   B HD12 1 
ATOM   5475 H  HD13 A ILE   B 1 106 ? 35.641 -30.260 6.531   0.72 33.20 ?  106 ILE   B HD13 1 
ATOM   5476 H  HD13 B ILE   B 1 106 ? 35.673 -30.142 6.395   0.28 33.29 ?  106 ILE   B HD13 1 
ATOM   5477 N  N    A GLN   B 1 107 ? 31.308 -27.495 8.204   0.72 25.65 ?  107 GLN   B N    1 
ATOM   5478 N  N    B GLN   B 1 107 ? 31.319 -27.502 8.129   0.28 26.69 ?  107 GLN   B N    1 
ATOM   5479 C  CA   A GLN   B 1 107 ? 30.234 -26.700 7.617   0.72 25.98 ?  107 GLN   B CA   1 
ATOM   5480 C  CA   B GLN   B 1 107 ? 30.237 -26.701 7.566   0.28 26.46 ?  107 GLN   B CA   1 
ATOM   5481 C  C    A GLN   B 1 107 ? 30.723 -25.350 7.106   0.72 23.80 ?  107 GLN   B C    1 
ATOM   5482 C  C    B GLN   B 1 107 ? 30.716 -25.331 7.102   0.28 24.16 ?  107 GLN   B C    1 
ATOM   5483 O  O    A GLN   B 1 107 ? 30.081 -24.768 6.226   0.72 24.15 ?  107 GLN   B O    1 
ATOM   5484 O  O    B GLN   B 1 107 ? 30.056 -24.712 6.260   0.28 24.32 ?  107 GLN   B O    1 
ATOM   5485 C  CB   A GLN   B 1 107 ? 29.116 -26.497 8.645   0.72 29.50 ?  107 GLN   B CB   1 
ATOM   5486 C  CB   B GLN   B 1 107 ? 29.113 -26.552 8.596   0.28 28.74 ?  107 GLN   B CB   1 
ATOM   5487 C  CG   A GLN   B 1 107 ? 27.792 -26.005 8.063   0.72 33.02 ?  107 GLN   B CG   1 
ATOM   5488 C  CG   B GLN   B 1 107 ? 27.790 -26.045 8.030   0.28 30.87 ?  107 GLN   B CG   1 
ATOM   5489 C  CD   A GLN   B 1 107 ? 27.713 -24.490 7.962   0.72 35.72 ?  107 GLN   B CD   1 
ATOM   5490 C  CD   B GLN   B 1 107 ? 27.679 -24.531 8.049   0.28 32.56 ?  107 GLN   B CD   1 
ATOM   5491 O  OE1  A GLN   B 1 107 ? 28.541 -23.773 8.527   0.72 36.67 ?  107 GLN   B OE1  1 
ATOM   5492 O  OE1  B GLN   B 1 107 ? 28.509 -23.841 8.643   0.28 33.12 ?  107 GLN   B OE1  1 
ATOM   5493 N  NE2  A GLN   B 1 107 ? 26.709 -23.996 7.241   0.72 36.64 ?  107 GLN   B NE2  1 
ATOM   5494 N  NE2  B GLN   B 1 107 ? 26.645 -24.007 7.399   0.28 33.17 ?  107 GLN   B NE2  1 
ATOM   5495 H  H    A GLN   B 1 107 ? 31.197 -27.681 9.032   0.72 30.76 ?  107 GLN   B H    1 
ATOM   5496 H  H    B GLN   B 1 107 ? 31.220 -27.694 8.959   0.28 32.01 ?  107 GLN   B H    1 
ATOM   5497 H  HA   A GLN   B 1 107 ? 29.860 -27.186 6.864   0.72 31.16 ?  107 GLN   B HA   1 
ATOM   5498 H  HA   B GLN   B 1 107 ? 29.871 -27.167 6.797   0.28 31.73 ?  107 GLN   B HA   1 
ATOM   5499 H  HB2  A GLN   B 1 107 ? 28.946 -27.342 9.082   0.72 35.38 ?  107 GLN   B HB2  1 
ATOM   5500 H  HB2  B GLN   B 1 107 ? 28.944 -27.417 8.994   0.28 34.47 ?  107 GLN   B HB2  1 
ATOM   5501 H  HB3  A GLN   B 1 107 ? 29.413 -25.845 9.299   0.72 35.38 ?  107 GLN   B HB3  1 
ATOM   5502 H  HB3  B GLN   B 1 107 ? 29.400 -25.929 9.282   0.28 34.47 ?  107 GLN   B HB3  1 
ATOM   5503 H  HG2  A GLN   B 1 107 ? 27.681 -26.368 7.171   0.72 39.60 ?  107 GLN   B HG2  1 
ATOM   5504 H  HG2  B GLN   B 1 107 ? 27.705 -26.338 7.110   0.28 37.02 ?  107 GLN   B HG2  1 
ATOM   5505 H  HG3  A GLN   B 1 107 ? 27.065 -26.307 8.635   0.72 39.60 ?  107 GLN   B HG3  1 
ATOM   5506 H  HG3  B GLN   B 1 107 ? 27.061 -26.408 8.561   0.28 37.02 ?  107 GLN   B HG3  1 
ATOM   5507 H  HE21 A GLN   B 1 107 ? 26.149 -24.528 6.860   0.72 43.94 ?  107 GLN   B HE21 1 
ATOM   5508 H  HE21 B GLN   B 1 107 ? 26.085 -24.519 6.994   0.28 39.78 ?  107 GLN   B HE21 1 
ATOM   5509 H  HE22 A GLN   B 1 107 ? 26.616 -23.145 7.156   0.72 43.94 ?  107 GLN   B HE22 1 
ATOM   5510 H  HE22 B GLN   B 1 107 ? 26.536 -23.154 7.383   0.28 39.78 ?  107 GLN   B HE22 1 
ATOM   5511 N  N    . LEU   B 1 108 ? 31.846 -24.844 7.623   1.00 21.84 ?  108 LEU   B N    1 
ATOM   5512 C  CA   . LEU   B 1 108 ? 32.382 -23.545 7.213   1.00 19.16 ?  108 LEU   B CA   1 
ATOM   5513 C  C    . LEU   B 1 108 ? 33.031 -23.565 5.836   1.00 16.48 ?  108 LEU   B C    1 
ATOM   5514 O  O    . LEU   B 1 108 ? 33.462 -22.507 5.347   1.00 15.80 ?  108 LEU   B O    1 
ATOM   5515 C  CB   . LEU   B 1 108 ? 33.381 -23.045 8.255   1.00 19.64 ?  108 LEU   B CB   1 
ATOM   5516 C  CG   . LEU   B 1 108 ? 32.748 -22.565 9.562   1.00 20.72 ?  108 LEU   B CG   1 
ATOM   5517 C  CD1  . LEU   B 1 108 ? 33.764 -22.556 10.688  1.00 21.01 ?  108 LEU   B CD1  1 
ATOM   5518 C  CD2  . LEU   B 1 108 ? 32.161 -21.176 9.372   1.00 21.75 ?  108 LEU   B CD2  1 
ATOM   5519 H  H    A LEU   B 1 108 ? 32.308 -25.236 8.230   0.72 26.19 ?  108 LEU   B H    1 
ATOM   5520 H  H    B LEU   B 1 108 ? 32.309 -25.244 8.224   0.28 26.19 ?  108 LEU   B H    1 
ATOM   5521 H  HA   . LEU   B 1 108 ? 31.652 -22.909 7.178   1.00 22.97 ?  108 LEU   B HA   1 
ATOM   5522 H  HB2  . LEU   B 1 108 ? 33.986 -23.767 8.475   1.00 23.54 ?  108 LEU   B HB2  1 
ATOM   5523 H  HB3  . LEU   B 1 108 ? 33.873 -22.302 7.880   1.00 23.54 ?  108 LEU   B HB3  1 
ATOM   5524 H  HG   . LEU   B 1 108 ? 32.024 -23.164 9.813   1.00 24.84 ?  108 LEU   B HG   1 
ATOM   5525 H  HD11 . LEU   B 1 108 ? 33.331 -22.254 11.504  1.00 25.19 ?  108 LEU   B HD11 1 
ATOM   5526 H  HD12 . LEU   B 1 108 ? 34.108 -23.453 10.809  1.00 25.19 ?  108 LEU   B HD12 1 
ATOM   5527 H  HD13 . LEU   B 1 108 ? 34.485 -21.950 10.455  1.00 25.19 ?  108 LEU   B HD13 1 
ATOM   5528 H  HD21 . LEU   B 1 108 ? 31.787 -20.871 10.214  1.00 26.08 ?  108 LEU   B HD21 1 
ATOM   5529 H  HD22 . LEU   B 1 108 ? 32.864 -20.574 9.085   1.00 26.08 ?  108 LEU   B HD22 1 
ATOM   5530 H  HD23 . LEU   B 1 108 ? 31.464 -21.217 8.698   1.00 26.08 ?  108 LEU   B HD23 1 
ATOM   5531 N  N    . LEU   B 1 109 ? 33.095 -24.734 5.203   1.00 15.53 ?  109 LEU   B N    1 
ATOM   5532 C  CA   . LEU   B 1 109 ? 33.726 -24.844 3.895   1.00 14.31 ?  109 LEU   B CA   1 
ATOM   5533 C  C    . LEU   B 1 109 ? 32.962 -24.062 2.834   1.00 13.81 ?  109 LEU   B C    1 
ATOM   5534 O  O    . LEU   B 1 109 ? 33.580 -23.465 1.944   1.00 13.51 ?  109 LEU   B O    1 
ATOM   5535 C  CB   . LEU   B 1 109 ? 33.843 -26.320 3.517   1.00 14.54 ?  109 LEU   B CB   1 
ATOM   5536 C  CG   . LEU   B 1 109 ? 34.622 -26.668 2.251   1.00 14.38 ?  109 LEU   B CG   1 
ATOM   5537 C  CD1  . LEU   B 1 109 ? 36.000 -26.007 2.257   1.00 14.01 ?  109 LEU   B CD1  1 
ATOM   5538 C  CD2  . LEU   B 1 109 ? 34.761 -28.175 2.115   1.00 15.09 ?  109 LEU   B CD2  1 
ATOM   5539 H  H    . LEU   B 1 109 ? 32.797 -25.478 5.509   1.00 18.61 ?  109 LEU   B H    1 
ATOM   5540 H  HA   . LEU   B 1 109 ? 34.621 -24.481 3.942   1.00 17.15 ?  109 LEU   B HA   1 
ATOM   5541 H  HB2  . LEU   B 1 109 ? 34.283 -26.787 4.246   1.00 17.43 ?  109 LEU   B HB2  1 
ATOM   5542 H  HB3  . LEU   B 1 109 ? 32.952 -26.680 3.401   1.00 17.43 ?  109 LEU   B HB3  1 
ATOM   5543 H  HG   . LEU   B 1 109 ? 34.135 -26.349 1.474   1.00 17.23 ?  109 LEU   B HG   1 
ATOM   5544 H  HD11 . LEU   B 1 109 ? 36.530 -26.373 1.530   1.00 16.78 ?  109 LEU   B HD11 1 
ATOM   5545 H  HD12 . LEU   B 1 109 ? 35.890 -25.054 2.138   1.00 16.78 ?  109 LEU   B HD12 1 
ATOM   5546 H  HD13 . LEU   B 1 109 ? 36.433 -26.193 3.104   1.00 16.78 ?  109 LEU   B HD13 1 
ATOM   5547 H  HD21 . LEU   B 1 109 ? 35.333 -28.376 1.354   1.00 18.09 ?  109 LEU   B HD21 1 
ATOM   5548 H  HD22 . LEU   B 1 109 ? 35.155 -28.533 2.925   1.00 18.09 ?  109 LEU   B HD22 1 
ATOM   5549 H  HD23 . LEU   B 1 109 ? 33.882 -28.566 1.975   1.00 18.09 ?  109 LEU   B HD23 1 
ATOM   5550 N  N    . LYS   B 1 110 ? 31.627 -24.028 2.913   1.00 13.56 ?  110 LYS   B N    1 
ATOM   5551 C  CA   . LYS   B 1 110 ? 30.871 -23.268 1.922   1.00 13.25 ?  110 LYS   B CA   1 
ATOM   5552 C  C    . LYS   B 1 110 ? 31.206 -21.778 2.007   1.00 12.95 ?  110 LYS   B C    1 
ATOM   5553 O  O    . LYS   B 1 110 ? 31.465 -21.133 0.986   1.00 12.55 ?  110 LYS   B O    1 
ATOM   5554 C  CB   . LYS   B 1 110 ? 29.366 -23.522 2.062   1.00 13.84 ?  110 LYS   B CB   1 
ATOM   5555 C  CG   . LYS   B 1 110 ? 28.564 -22.911 0.914   1.00 14.08 ?  110 LYS   B CG   1 
ATOM   5556 C  CD   . LYS   B 1 110 ? 27.092 -23.323 0.951   1.00 14.64 ?  110 LYS   B CD   1 
ATOM   5557 C  CE   . LYS   B 1 110 ? 26.334 -22.789 -0.263  1.00 15.29 ?  110 LYS   B CE   1 
ATOM   5558 N  NZ   . LYS   B 1 110 ? 26.663 -23.506 -1.523  1.00 15.61 ?  110 LYS   B NZ   1 
ATOM   5559 H  H    . LYS   B 1 110 ? 31.157 -24.432 3.503   1.00 16.25 ?  110 LYS   B H    1 
ATOM   5560 H  HA   . LYS   B 1 110 ? 31.134 -23.570 1.036   1.00 15.88 ?  110 LYS   B HA   1 
ATOM   5561 H  HB2  . LYS   B 1 110 ? 29.207 -24.483 2.060   1.00 16.58 ?  110 LYS   B HB2  1 
ATOM   5562 H  HB3  . LYS   B 1 110 ? 29.053 -23.135 2.890   1.00 16.58 ?  110 LYS   B HB3  1 
ATOM   5563 H  HG2  . LYS   B 1 110 ? 28.602 -21.946 0.976   1.00 16.88 ?  110 LYS   B HG2  1 
ATOM   5564 H  HG3  . LYS   B 1 110 ? 28.934 -23.209 0.069   1.00 16.88 ?  110 LYS   B HG3  1 
ATOM   5565 H  HD2  . LYS   B 1 110 ? 27.028 -24.295 0.946   1.00 17.55 ?  110 LYS   B HD2  1 
ATOM   5566 H  HD3  . LYS   B 1 110 ? 26.676 -22.968 1.753   1.00 17.55 ?  110 LYS   B HD3  1 
ATOM   5567 H  HE2  . LYS   B 1 110 ? 25.383 -22.877 -0.108  1.00 18.33 ?  110 LYS   B HE2  1 
ATOM   5568 H  HE3  . LYS   B 1 110 ? 26.564 -21.852 -0.385  1.00 18.33 ?  110 LYS   B HE3  1 
ATOM   5569 H  HZ1  . LYS   B 1 110 ? 26.205 -23.160 -2.200  1.00 18.71 ?  110 LYS   B HZ1  1 
ATOM   5570 H  HZ2  . LYS   B 1 110 ? 27.535 -23.434 -1.696  1.00 18.71 ?  110 LYS   B HZ2  1 
ATOM   5571 H  HZ3  . LYS   B 1 110 ? 26.457 -24.369 -1.442  1.00 18.71 ?  110 LYS   B HZ3  1 
ATOM   5572 N  N    . SER   B 1 111 ? 31.225 -21.222 3.224   1.00 13.40 ?  111 SER   B N    1 
ATOM   5573 C  CA   . SER   B 1 111 ? 31.618 -19.825 3.398   1.00 13.22 ?  111 SER   B CA   1 
ATOM   5574 C  C    . SER   B 1 111 ? 33.000 -19.571 2.809   1.00 12.93 ?  111 SER   B C    1 
ATOM   5575 O  O    . SER   B 1 111 ? 33.231 -18.538 2.161   1.00 12.83 ?  111 SER   B O    1 
ATOM   5576 C  CB   . SER   B 1 111 ? 31.618 -19.466 4.883   1.00 14.38 ?  111 SER   B CB   1 
ATOM   5577 O  OG   . SER   B 1 111 ? 30.313 -19.457 5.420   1.00 15.96 ?  111 SER   B OG   1 
ATOM   5578 H  H    . SER   B 1 111 ? 31.022 -21.635 3.951   1.00 16.06 ?  111 SER   B H    1 
ATOM   5579 H  HA   . SER   B 1 111 ? 30.985 -19.254 2.944   1.00 15.84 ?  111 SER   B HA   1 
ATOM   5580 H  HB2  . SER   B 1 111 ? 32.142 -20.125 5.367   1.00 17.23 ?  111 SER   B HB2  1 
ATOM   5581 H  HB3  . SER   B 1 111 ? 32.007 -18.589 4.995   1.00 17.23 ?  111 SER   B HB3  1 
ATOM   5582 H  HG   . SER   B 1 111 ? 30.338 -19.253 6.242   1.00 19.13 ?  111 SER   B HG   1 
ATOM   5583 N  N    . ALA   B 1 112 ? 33.935 -20.491 3.038   1.00 12.83 ?  112 ALA   B N    1 
ATOM   5584 C  CA   . ALA   B 1 112 ? 35.277 -20.323 2.494   1.00 12.39 ?  112 ALA   B CA   1 
ATOM   5585 C  C    . ALA   B 1 112 ? 35.247 -20.229 0.970   1.00 11.79 ?  112 ALA   B C    1 
ATOM   5586 O  O    . ALA   B 1 112 ? 35.876 -19.344 0.375   1.00 12.07 ?  112 ALA   B O    1 
ATOM   5587 C  CB   . ALA   B 1 112 ? 36.177 -21.467 2.969   1.00 13.13 ?  112 ALA   B CB   1 
ATOM   5588 H  H    . ALA   B 1 112 ? 33.822 -21.214 3.504   1.00 15.37 ?  112 ALA   B H    1 
ATOM   5589 H  HA   . ALA   B 1 112 ? 35.647 -19.496 2.836   1.00 14.85 ?  112 ALA   B HA   1 
ATOM   5590 H  HB1  . ALA   B 1 112 ? 37.068 -21.336 2.604   1.00 15.73 ?  112 ALA   B HB1  1 
ATOM   5591 H  HB2  . ALA   B 1 112 ? 36.218 -21.456 3.940   1.00 15.73 ?  112 ALA   B HB2  1 
ATOM   5592 H  HB3  . ALA   B 1 112 ? 35.813 -22.308 2.662   1.00 15.73 ?  112 ALA   B HB3  1 
ATOM   5593 N  N    . TYR   B 1 113 ? 34.515 -21.132 0.317   1.00 11.87 ?  113 TYR   B N    1 
ATOM   5594 C  CA   . TYR   B 1 113 ? 34.441 -21.087 -1.137  1.00 11.55 ?  113 TYR   B CA   1 
ATOM   5595 C  C    . TYR   B 1 113 ? 33.733 -19.838 -1.655  1.00 11.35 ?  113 TYR   B C    1 
ATOM   5596 O  O    . TYR   B 1 113 ? 34.002 -19.409 -2.781  1.00 11.47 ?  113 TYR   B O    1 
ATOM   5597 C  CB   . TYR   B 1 113 ? 33.769 -22.344 -1.684  1.00 11.90 ?  113 TYR   B CB   1 
ATOM   5598 C  CG   . TYR   B 1 113 ? 34.731 -23.493 -1.944  1.00 12.43 ?  113 TYR   B CG   1 
ATOM   5599 C  CD1  . TYR   B 1 113 ? 35.725 -23.387 -2.911  1.00 12.63 ?  113 TYR   B CD1  1 
ATOM   5600 C  CD2  . TYR   B 1 113 ? 34.635 -24.685 -1.238  1.00 12.51 ?  113 TYR   B CD2  1 
ATOM   5601 C  CE1  . TYR   B 1 113 ? 36.608 -24.418 -3.151  1.00 12.63 ?  113 TYR   B CE1  1 
ATOM   5602 C  CE2  . TYR   B 1 113 ? 35.509 -25.737 -1.480  1.00 12.71 ?  113 TYR   B CE2  1 
ATOM   5603 C  CZ   . TYR   B 1 113 ? 36.490 -25.601 -2.441  1.00 12.62 ?  113 TYR   B CZ   1 
ATOM   5604 O  OH   . TYR   B 1 113 ? 37.373 -26.618 -2.713  1.00 13.51 ?  113 TYR   B OH   1 
ATOM   5605 H  H    . TYR   B 1 113 ? 34.050 -21.762 0.692   1.00 14.22 ?  113 TYR   B H    1 
ATOM   5606 H  HA   . TYR   B 1 113 ? 35.344 -21.071 -1.474  1.00 13.83 ?  113 TYR   B HA   1 
ATOM   5607 H  HB2  . TYR   B 1 113 ? 33.108 -22.659 -1.043  1.00 14.26 ?  113 TYR   B HB2  1 
ATOM   5608 H  HB3  . TYR   B 1 113 ? 33.332 -22.128 -2.521  1.00 14.26 ?  113 TYR   B HB3  1 
ATOM   5609 H  HD1  . TYR   B 1 113 ? 35.812 -22.593 -3.395  1.00 15.13 ?  113 TYR   B HD1  1 
ATOM   5610 H  HD2  . TYR   B 1 113 ? 33.968 -24.779 -0.597  1.00 14.99 ?  113 TYR   B HD2  1 
ATOM   5611 H  HE1  . TYR   B 1 113 ? 37.268 -24.329 -3.806  1.00 15.13 ?  113 TYR   B HE1  1 
ATOM   5612 H  HE2  . TYR   B 1 113 ? 35.425 -26.531 -1.003  1.00 15.23 ?  113 TYR   B HE2  1 
ATOM   5613 H  HH   . TYR   B 1 113 ? 37.201 -27.285 -2.232  1.00 16.19 ?  113 TYR   B HH   1 
ATOM   5614 N  N    . GLU   B 1 114 ? 32.813 -19.259 -0.877  1.00 11.35 ?  114 GLU   B N    1 
ATOM   5615 C  CA   . GLU   B 1 114 ? 32.131 -18.053 -1.337  1.00 11.49 ?  114 GLU   B CA   1 
ATOM   5616 C  C    . GLU   B 1 114 ? 33.113 -16.931 -1.638  1.00 11.38 ?  114 GLU   B C    1 
ATOM   5617 O  O    . GLU   B 1 114 ? 32.829 -16.072 -2.477  1.00 11.68 ?  114 GLU   B O    1 
ATOM   5618 C  CB   . GLU   B 1 114 ? 31.075 -17.627 -0.315  1.00 11.93 ?  114 GLU   B CB   1 
ATOM   5619 C  CG   . GLU   B 1 114 ? 29.853 -18.538 -0.390  1.00 12.13 ?  114 GLU   B CG   1 
ATOM   5620 C  CD   . GLU   B 1 114 ? 28.832 -18.360 0.723   1.00 12.31 ?  114 GLU   B CD   1 
ATOM   5621 O  OE1  . GLU   B 1 114 ? 29.118 -17.738 1.762   1.00 12.62 ?  114 GLU   B OE1  1 
ATOM   5622 O  OE2  . GLU   B 1 114 ? 27.711 -18.897 0.565   1.00 13.20 -1 114 GLU   B OE2  1 
ATOM   5623 H  H    . GLU   B 1 114 ? 32.563 -19.547 -0.103  1.00 13.59 ?  114 GLU   B H    1 
ATOM   5624 H  HA   . GLU   B 1 114 ? 31.671 -18.257 -2.161  1.00 13.77 ?  114 GLU   B HA   1 
ATOM   5625 H  HB2  . GLU   B 1 114 ? 31.444 -17.689 0.580   1.00 14.29 ?  114 GLU   B HB2  1 
ATOM   5626 H  HB3  . GLU   B 1 114 ? 30.789 -16.723 -0.503  1.00 14.29 ?  114 GLU   B HB3  1 
ATOM   5627 H  HG2  . GLU   B 1 114 ? 29.405 -18.376 -1.230  1.00 14.53 ?  114 GLU   B HG2  1 
ATOM   5628 H  HG3  . GLU   B 1 114 ? 30.160 -19.459 -0.356  1.00 14.53 ?  114 GLU   B HG3  1 
ATOM   5629 N  N    . ASN   B 1 115 ? 34.276 -16.922 -0.982  1.00 11.21 ?  115 ASN   B N    1 
ATOM   5630 C  CA   . ASN   B 1 115 ? 35.268 -15.891 -1.283  1.00 10.78 ?  115 ASN   B CA   1 
ATOM   5631 C  C    . ASN   B 1 115 ? 35.675 -15.913 -2.749  1.00 10.53 ?  115 ASN   B C    1 
ATOM   5632 O  O    . ASN   B 1 115 ? 36.069 -14.876 -3.303  1.00 11.48 ?  115 ASN   B O    1 
ATOM   5633 C  CB   . ASN   B 1 115 ? 36.506 -16.065 -0.401  1.00 11.55 ?  115 ASN   B CB   1 
ATOM   5634 C  CG   . ASN   B 1 115 ? 36.236 -15.798 1.059   1.00 11.98 ?  115 ASN   B CG   1 
ATOM   5635 O  OD1  . ASN   B 1 115 ? 36.243 -14.654 1.505   1.00 14.00 ?  115 ASN   B OD1  1 
ATOM   5636 N  ND2  . ASN   B 1 115 ? 36.069 -16.863 1.830   1.00 12.31 ?  115 ASN   B ND2  1 
ATOM   5637 H  H    . ASN   B 1 115 ? 34.513 -17.485 -0.369  1.00 13.43 ?  115 ASN   B H    1 
ATOM   5638 H  HA   . ASN   B 1 115 ? 34.890 -15.021 -1.093  1.00 12.91 ?  115 ASN   B HA   1 
ATOM   5639 H  HB2  . ASN   B 1 115 ? 36.834 -16.974 -0.487  1.00 13.83 ?  115 ASN   B HB2  1 
ATOM   5640 H  HB3  . ASN   B 1 115 ? 37.193 -15.440 -0.693  1.00 13.83 ?  115 ASN   B HB3  1 
ATOM   5641 H  HD21 . ASN   B 1 115 ? 35.923 -16.766 2.673   1.00 14.75 ?  115 ASN   B HD21 1 
ATOM   5642 H  HD22 . ASN   B 1 115 ? 36.092 -17.653 1.489   1.00 14.75 ?  115 ASN   B HD22 1 
ATOM   5643 N  N    . PHE   B 1 116 ? 35.654 -17.092 -3.380  1.00 10.44 ?  116 PHE   B N    1 
ATOM   5644 C  CA   . PHE   B 1 116 ? 36.088 -17.185 -4.769  1.00 10.89 ?  116 PHE   B CA   1 
ATOM   5645 C  C    . PHE   B 1 116 ? 35.185 -16.363 -5.687  1.00 10.69 ?  116 PHE   B C    1 
ATOM   5646 O  O    . PHE   B 1 116 ? 35.620 -15.932 -6.762  1.00 11.20 ?  116 PHE   B O    1 
ATOM   5647 C  CB   . PHE   B 1 116 ? 36.051 -18.633 -5.280  1.00 10.57 ?  116 PHE   B CB   1 
ATOM   5648 C  CG   . PHE   B 1 116 ? 37.119 -19.586 -4.735  1.00 10.61 ?  116 PHE   B CG   1 
ATOM   5649 C  CD1  . PHE   B 1 116 ? 37.764 -19.404 -3.527  1.00 11.34 ?  116 PHE   B CD1  1 
ATOM   5650 C  CD2  . PHE   B 1 116 ? 37.420 -20.727 -5.468  1.00 10.92 ?  116 PHE   B CD2  1 
ATOM   5651 C  CE1  . PHE   B 1 116 ? 38.697 -20.337 -3.073  1.00 11.47 ?  116 PHE   B CE1  1 
ATOM   5652 C  CE2  . PHE   B 1 116 ? 38.353 -21.659 -5.021  1.00 11.23 ?  116 PHE   B CE2  1 
ATOM   5653 C  CZ   . PHE   B 1 116 ? 38.984 -21.469 -3.827  1.00 11.18 ?  116 PHE   B CZ   1 
ATOM   5654 H  H    . PHE   B 1 116 ? 35.396 -17.840 -3.031  1.00 12.51 ?  116 PHE   B H    1 
ATOM   5655 H  HA   . PHE   B 1 116 ? 36.996 -16.860 -4.849  1.00 13.05 ?  116 PHE   B HA   1 
ATOM   5656 H  HB2  . PHE   B 1 116 ? 35.181 -19.013 -5.053  1.00 12.66 ?  116 PHE   B HB2  1 
ATOM   5657 H  HB3  . PHE   B 1 116 ? 36.141 -18.618 -6.246  1.00 12.66 ?  116 PHE   B HB3  1 
ATOM   5658 H  HD1  . PHE   B 1 116 ? 37.563 -18.655 -3.012  1.00 13.59 ?  116 PHE   B HD1  1 
ATOM   5659 H  HD2  . PHE   B 1 116 ? 36.987 -20.877 -6.277  1.00 13.08 ?  116 PHE   B HD2  1 
ATOM   5660 H  HE1  . PHE   B 1 116 ? 39.130 -20.198 -2.262  1.00 13.74 ?  116 PHE   B HE1  1 
ATOM   5661 H  HE2  . PHE   B 1 116 ? 38.544 -22.411 -5.533  1.00 13.45 ?  116 PHE   B HE2  1 
ATOM   5662 H  HZ   . PHE   B 1 116 ? 39.619 -22.079 -3.528  1.00 13.39 ?  116 PHE   B HZ   1 
ATOM   5663 N  N    . ASN   B 1 117 ? 33.917 -16.160 -5.301  1.00 11.31 ?  117 ASN   B N    1 
ATOM   5664 C  CA   . ASN   B 1 117 ? 32.971 -15.462 -6.172  1.00 11.63 ?  117 ASN   B CA   1 
ATOM   5665 C  C    . ASN   B 1 117 ? 33.281 -13.981 -6.323  1.00 11.81 ?  117 ASN   B C    1 
ATOM   5666 O  O    . ASN   B 1 117 ? 32.680 -13.326 -7.179  1.00 12.88 ?  117 ASN   B O    1 
ATOM   5667 C  CB   . ASN   B 1 117 ? 31.548 -15.678 -5.681  1.00 11.67 ?  117 ASN   B CB   1 
ATOM   5668 C  CG   . ASN   B 1 117 ? 31.092 -17.088 -5.927  1.00 11.93 ?  117 ASN   B CG   1 
ATOM   5669 O  OD1  . ASN   B 1 117 ? 31.450 -17.683 -6.943  1.00 12.88 ?  117 ASN   B OD1  1 
ATOM   5670 N  ND2  . ASN   B 1 117 ? 30.354 -17.658 -4.986  1.00 12.06 ?  117 ASN   B ND2  1 
ATOM   5671 H  H    . ASN   B 1 117 ? 33.593 -16.412 -4.541  1.00 13.55 ?  117 ASN   B H    1 
ATOM   5672 H  HA   . ASN   B 1 117 ? 33.038 -15.861 -7.048  1.00 13.93 ?  117 ASN   B HA   1 
ATOM   5673 H  HB2  . ASN   B 1 117 ? 31.507 -15.506 -4.724  1.00 13.98 ?  117 ASN   B HB2  1 
ATOM   5674 H  HB3  . ASN   B 1 117 ? 30.957 -15.069 -6.153  1.00 13.98 ?  117 ASN   B HB3  1 
ATOM   5675 H  HD21 . ASN   B 1 117 ? 30.069 -18.462 -5.092  1.00 14.45 ?  117 ASN   B HD21 1 
ATOM   5676 H  HD22 . ASN   B 1 117 ? 30.131 -17.212 -4.285  1.00 14.45 ?  117 ASN   B HD22 1 
ATOM   5677 N  N    . GLN   B 1 118 ? 34.210 -13.450 -5.539  1.00 11.35 ?  118 GLN   B N    1 
ATOM   5678 C  CA   . GLN   B 1 118 ? 34.645 -12.065 -5.680  1.00 12.13 ?  118 GLN   B CA   1 
ATOM   5679 C  C    . GLN   B 1 118 ? 35.714 -11.876 -6.750  1.00 12.15 ?  118 GLN   B C    1 
ATOM   5680 O  O    . GLN   B 1 118 ? 36.187 -10.751 -6.929  1.00 13.50 ?  118 GLN   B O    1 
ATOM   5681 C  CB   . GLN   B 1 118 ? 35.128 -11.532 -4.327  1.00 12.63 ?  118 GLN   B CB   1 
ATOM   5682 C  CG   . GLN   B 1 118 ? 34.044 -11.567 -3.255  1.00 12.74 ?  118 GLN   B CG   1 
ATOM   5683 C  CD   . GLN   B 1 118 ? 32.869 -10.666 -3.587  1.00 12.68 ?  118 GLN   B CD   1 
ATOM   5684 O  OE1  . GLN   B 1 118 ? 33.052 -9.526  -4.025  1.00 13.36 ?  118 GLN   B OE1  1 
ATOM   5685 N  NE2  . GLN   B 1 118 ? 31.657 -11.170 -3.390  1.00 13.27 ?  118 GLN   B NE2  1 
ATOM   5686 H  H    . GLN   B 1 118 ? 34.621 -13.875 -4.913  1.00 13.60 ?  118 GLN   B H    1 
ATOM   5687 H  HA   . GLN   B 1 118 ? 33.885 -11.533 -5.951  1.00 14.54 ?  118 GLN   B HA   1 
ATOM   5688 H  HB2  . GLN   B 1 118 ? 35.875 -12.065 -4.020  1.00 15.13 ?  118 GLN   B HB2  1 
ATOM   5689 H  HB3  . GLN   B 1 118 ? 35.409 -10.603 -4.434  1.00 15.13 ?  118 GLN   B HB3  1 
ATOM   5690 H  HG2  . GLN   B 1 118 ? 33.716 -12.475 -3.171  1.00 15.27 ?  118 GLN   B HG2  1 
ATOM   5691 H  HG3  . GLN   B 1 118 ? 34.425 -11.272 -2.412  1.00 15.27 ?  118 GLN   B HG3  1 
ATOM   5692 H  HE21 . GLN   B 1 118 ? 31.572 -11.970 -3.080  1.00 15.90 ?  118 GLN   B HE21 1 
ATOM   5693 H  HE22 . GLN   B 1 118 ? 30.966 -10.698 -3.561  1.00 15.90 ?  118 GLN   B HE22 1 
ATOM   5694 N  N    . HIS   B 1 119 ? 36.067 -12.934 -7.484  1.00 11.34 ?  119 HIS   B N    1 
ATOM   5695 C  CA   . HIS   B 1 119 ? 37.110 -12.890 -8.501  1.00 11.69 ?  119 HIS   B CA   1 
ATOM   5696 C  C    . HIS   B 1 119 ? 36.631 -13.621 -9.741  1.00 11.79 ?  119 HIS   B C    1 
ATOM   5697 O  O    . HIS   B 1 119 ? 36.122 -14.738 -9.639  1.00 12.58 ?  119 HIS   B O    1 
ATOM   5698 C  CB   . HIS   B 1 119 ? 38.391 -13.518 -7.955  1.00 12.38 ?  119 HIS   B CB   1 
ATOM   5699 C  CG   . HIS   B 1 119 ? 38.864 -12.832 -6.720  1.00 13.50 ?  119 HIS   B CG   1 
ATOM   5700 N  ND1  . HIS   B 1 119 ? 39.661 -11.708 -6.759  1.00 15.07 ?  119 HIS   B ND1  1 
ATOM   5701 C  CD2  . HIS   B 1 119 ? 38.558 -13.036 -5.417  1.00 14.42 ?  119 HIS   B CD2  1 
ATOM   5702 C  CE1  . HIS   B 1 119 ? 39.863 -11.280 -5.526  1.00 15.88 ?  119 HIS   B CE1  1 
ATOM   5703 N  NE2  . HIS   B 1 119 ? 39.197 -12.060 -4.695  1.00 15.94 ?  119 HIS   B NE2  1 
ATOM   5704 H  H    . HIS   B 1 119 ? 35.697 -13.712 -7.414  1.00 13.58 ?  119 HIS   B H    1 
ATOM   5705 H  HA   . HIS   B 1 119 ? 37.291 -11.967 -8.741  1.00 14.01 ?  119 HIS   B HA   1 
ATOM   5706 H  HB2  . HIS   B 1 119 ? 38.228 -14.447 -7.746  1.00 14.83 ?  119 HIS   B HB2  1 
ATOM   5707 H  HB3  . HIS   B 1 119 ? 39.091 -13.443 -8.628  1.00 14.83 ?  119 HIS   B HB3  1 
ATOM   5708 H  HD2  . HIS   B 1 119 ? 38.017 -13.716 -5.078  1.00 17.28 ?  119 HIS   B HD2  1 
ATOM   5709 H  HE1  . HIS   B 1 119 ? 40.395 -10.558 -5.277  1.00 19.03 ?  119 HIS   B HE1  1 
ATOM   5710 H  HE2  . HIS   B 1 119 ? 39.191 -11.993 -3.834  1.00 19.10 ?  119 HIS   B HE2  1 
ATOM   5711 N  N    . GLU   B 1 120 ? 36.784 -13.001 -10.911 1.00 12.35 ?  120 GLU   B N    1 
ATOM   5712 C  CA   . GLU   B 1 120 ? 36.200 -13.583 -12.115 1.00 14.00 ?  120 GLU   B CA   1 
ATOM   5713 C  C    . GLU   B 1 120 ? 36.877 -14.885 -12.523 1.00 12.66 ?  120 GLU   B C    1 
ATOM   5714 O  O    . GLU   B 1 120 ? 36.218 -15.761 -13.092 1.00 13.04 ?  120 GLU   B O    1 
ATOM   5715 C  CB   . GLU   B 1 120 ? 36.218 -12.572 -13.260 1.00 18.84 ?  120 GLU   B CB   1 
ATOM   5716 C  CG   . GLU   B 1 120 ? 35.253 -11.416 -13.050 1.00 25.49 ?  120 GLU   B CG   1 
ATOM   5717 C  CD   . GLU   B 1 120 ? 35.177 -10.484 -14.243 1.00 31.32 ?  120 GLU   B CD   1 
ATOM   5718 O  OE1  . GLU   B 1 120 ? 36.181 -10.372 -14.980 1.00 33.37 ?  120 GLU   B OE1  1 
ATOM   5719 O  OE2  . GLU   B 1 120 ? 34.112 -9.863  -14.442 1.00 33.81 -1 120 GLU   B OE2  1 
ATOM   5720 H  H    . GLU   B 1 120 ? 37.208 -12.261 -11.034 1.00 14.80 ?  120 GLU   B H    1 
ATOM   5721 H  HA   . GLU   B 1 120 ? 35.275 -13.791 -11.933 1.00 16.78 ?  120 GLU   B HA   1 
ATOM   5722 H  HB2  . GLU   B 1 120 ? 37.108 -12.201 -13.345 1.00 22.59 ?  120 GLU   B HB2  1 
ATOM   5723 H  HB3  . GLU   B 1 120 ? 35.966 -13.021 -14.083 1.00 22.59 ?  120 GLU   B HB3  1 
ATOM   5724 H  HG2  . GLU   B 1 120 ? 34.362 -11.771 -12.892 1.00 30.57 ?  120 GLU   B HG2  1 
ATOM   5725 H  HG3  . GLU   B 1 120 ? 35.541 -10.896 -12.285 1.00 30.57 ?  120 GLU   B HG3  1 
ATOM   5726 N  N    . VAL   B 1 121 ? 38.175 -15.030 -12.255 1.00 12.26 ?  121 VAL   B N    1 
ATOM   5727 C  CA   . VAL   B 1 121 ? 38.921 -16.237 -12.606 1.00 11.96 ?  121 VAL   B CA   1 
ATOM   5728 C  C    . VAL   B 1 121 ? 40.034 -16.441 -11.587 1.00 11.36 ?  121 VAL   B C    1 
ATOM   5729 O  O    . VAL   B 1 121 ? 40.705 -15.483 -11.189 1.00 12.28 ?  121 VAL   B O    1 
ATOM   5730 C  CB   . VAL   B 1 121 ? 39.435 -16.188 -14.064 1.00 13.88 ?  121 VAL   B CB   1 
ATOM   5731 C  CG1  . VAL   B 1 121 ? 40.307 -14.961 -14.309 1.00 15.53 ?  121 VAL   B CG1  1 
ATOM   5732 C  CG2  . VAL   B 1 121 ? 40.177 -17.475 -14.420 1.00 15.23 ?  121 VAL   B CG2  1 
ATOM   5733 H  H    . VAL   B 1 121 ? 38.659 -14.428 -11.876 1.00 14.68 ?  121 VAL   B H    1 
ATOM   5734 H  HA   . VAL   B 1 121 ? 38.315 -16.992 -12.545 1.00 14.34 ?  121 VAL   B HA   1 
ATOM   5735 H  HB   . VAL   B 1 121 ? 38.668 -16.125 -14.663 1.00 16.64 ?  121 VAL   B HB   1 
ATOM   5736 H  HG11 . VAL   B 1 121 ? 40.613 -14.969 -15.231 1.00 18.61 ?  121 VAL   B HG11 1 
ATOM   5737 H  HG12 . VAL   B 1 121 ? 39.781 -14.163 -14.144 1.00 18.61 ?  121 VAL   B HG12 1 
ATOM   5738 H  HG13 . VAL   B 1 121 ? 41.066 -14.990 -13.709 1.00 18.61 ?  121 VAL   B HG13 1 
ATOM   5739 H  HG21 . VAL   B 1 121 ? 40.375 -17.473 -15.372 1.00 18.25 ?  121 VAL   B HG21 1 
ATOM   5740 H  HG22 . VAL   B 1 121 ? 41.002 -17.514 -13.913 1.00 18.25 ?  121 VAL   B HG22 1 
ATOM   5741 H  HG23 . VAL   B 1 121 ? 39.615 -18.235 -14.203 1.00 18.25 ?  121 VAL   B HG23 1 
ATOM   5742 N  N    . LEU   B 1 122 ? 40.217 -17.694 -11.152 1.00 11.13 ?  122 LEU   B N    1 
ATOM   5743 C  CA   . LEU   B 1 122 ? 41.198 -18.039 -10.128 1.00 10.90 ?  122 LEU   B CA   1 
ATOM   5744 C  C    . LEU   B 1 122 ? 41.845 -19.373 -10.449 1.00 11.03 ?  122 LEU   B C    1 
ATOM   5745 O  O    . LEU   B 1 122 ? 41.184 -20.290 -10.953 1.00 12.00 ?  122 LEU   B O    1 
ATOM   5746 C  CB   . LEU   B 1 122 ? 40.547 -18.258 -8.747  1.00 12.71 ?  122 LEU   B CB   1 
ATOM   5747 C  CG   . LEU   B 1 122 ? 39.502 -17.249 -8.261  1.00 12.83 ?  122 LEU   B CG   1 
ATOM   5748 C  CD1  . LEU   B 1 122 ? 38.110 -17.610 -8.747  1.00 13.64 ?  122 LEU   B CD1  1 
ATOM   5749 C  CD2  . LEU   B 1 122 ? 39.532 -17.140 -6.749  1.00 12.38 ?  122 LEU   B CD2  1 
ATOM   5750 H  H    . LEU   B 1 122 ? 39.771 -18.373 -11.440 1.00 13.33 ?  122 LEU   B H    1 
ATOM   5751 H  HA   . LEU   B 1 122 ? 41.877 -17.347 -10.061 1.00 13.06 ?  122 LEU   B HA   1 
ATOM   5752 H  HB2  . LEU   B 1 122 ? 40.115 -19.120 -8.757  1.00 15.22 ?  122 LEU   B HB2  1 
ATOM   5753 H  HB3  . LEU   B 1 122 ? 41.254 -18.260 -8.085  1.00 15.22 ?  122 LEU   B HB3  1 
ATOM   5754 H  HG   . LEU   B 1 122 ? 39.718 -16.374 -8.620  1.00 15.37 ?  122 LEU   B HG   1 
ATOM   5755 H  HD11 . LEU   B 1 122 ? 37.471 -16.980 -8.377  1.00 16.35 ?  122 LEU   B HD11 1 
ATOM   5756 H  HD12 . LEU   B 1 122 ? 38.091 -17.560 -9.718  1.00 16.35 ?  122 LEU   B HD12 1 
ATOM   5757 H  HD13 . LEU   B 1 122 ? 37.895 -18.508 -8.458  1.00 16.35 ?  122 LEU   B HD13 1 
ATOM   5758 H  HD21 . LEU   B 1 122 ? 38.843 -16.519 -6.459  1.00 14.84 ?  122 LEU   B HD21 1 
ATOM   5759 H  HD22 . LEU   B 1 122 ? 39.370 -18.014 -6.363  1.00 14.84 ?  122 LEU   B HD22 1 
ATOM   5760 H  HD23 . LEU   B 1 122 ? 40.404 -16.813 -6.472  1.00 14.84 ?  122 LEU   B HD23 1 
ATOM   5761 N  N    . LEU   B 1 123 ? 43.131 -19.482 -10.096 1.00 10.47 ?  123 LEU   B N    1 
ATOM   5762 C  CA   . LEU   B 1 123 ? 43.840 -20.751 -9.968  1.00 10.73 ?  123 LEU   B CA   1 
ATOM   5763 C  C    . LEU   B 1 123 ? 43.813 -21.139 -8.495  1.00 10.37 ?  123 LEU   B C    1 
ATOM   5764 O  O    . LEU   B 1 123 ? 44.162 -20.316 -7.641  1.00 10.93 ?  123 LEU   B O    1 
ATOM   5765 C  CB   . LEU   B 1 123 ? 45.288 -20.576 -10.432 1.00 11.16 ?  123 LEU   B CB   1 
ATOM   5766 C  CG   . LEU   B 1 123 ? 46.234 -21.757 -10.193 1.00 11.43 ?  123 LEU   B CG   1 
ATOM   5767 C  CD1  . LEU   B 1 123 ? 45.823 -23.008 -10.974 1.00 12.11 ?  123 LEU   B CD1  1 
ATOM   5768 C  CD2  . LEU   B 1 123 ? 47.651 -21.357 -10.558 1.00 12.30 ?  123 LEU   B CD2  1 
ATOM   5769 H  H    . LEU   B 1 123 ? 43.629 -18.804 -9.911  1.00 12.54 ?  123 LEU   B H    1 
ATOM   5770 H  HA   . LEU   B 1 123 ? 43.401 -21.442 -10.495 1.00 12.85 ?  123 LEU   B HA   1 
ATOM   5771 H  HB2  . LEU   B 1 123 ? 45.273 -20.410 -11.389 1.00 13.36 ?  123 LEU   B HB2  1 
ATOM   5772 H  HB3  . LEU   B 1 123 ? 45.658 -19.812 -9.976  1.00 13.36 ?  123 LEU   B HB3  1 
ATOM   5773 H  HG   . LEU   B 1 123 ? 46.227 -21.983 -9.251  1.00 13.69 ?  123 LEU   B HG   1 
ATOM   5774 H  HD11 . LEU   B 1 123 ? 46.461 -23.714 -10.790 1.00 14.51 ?  123 LEU   B HD11 1 
ATOM   5775 H  HD12 . LEU   B 1 123 ? 44.937 -23.278 -10.689 1.00 14.51 ?  123 LEU   B HD12 1 
ATOM   5776 H  HD13 . LEU   B 1 123 ? 45.821 -22.800 -11.920 1.00 14.51 ?  123 LEU   B HD13 1 
ATOM   5777 H  HD21 . LEU   B 1 123 ? 48.242 -22.111 -10.404 1.00 14.74 ?  123 LEU   B HD21 1 
ATOM   5778 H  HD22 . LEU   B 1 123 ? 47.677 -21.104 -11.495 1.00 14.74 ?  123 LEU   B HD22 1 
ATOM   5779 H  HD23 . LEU   B 1 123 ? 47.920 -20.607 -10.005 1.00 14.74 ?  123 LEU   B HD23 1 
ATOM   5780 N  N    . ALA   B 1 124 ? 43.383 -22.371 -8.188  1.00 10.42 ?  124 ALA   B N    1 
ATOM   5781 C  CA   . ALA   B 1 124 ? 43.130 -22.693 -6.792  1.00 10.69 ?  124 ALA   B CA   1 
ATOM   5782 C  C    . ALA   B 1 124 ? 43.397 -24.152 -6.460  1.00 10.29 ?  124 ALA   B C    1 
ATOM   5783 O  O    . ALA   B 1 124 ? 43.256 -25.027 -7.324  1.00 11.16 ?  124 ALA   B O    1 
ATOM   5784 C  CB   . ALA   B 1 124 ? 41.675 -22.376 -6.420  1.00 11.06 ?  124 ALA   B CB   1 
ATOM   5785 H  H    . ALA   B 1 124 ? 43.218 -23.010 -8.750  1.00 12.48 ?  124 ALA   B H    1 
ATOM   5786 H  HA   . ALA   B 1 124 ? 43.703 -22.139 -6.246  1.00 12.81 ?  124 ALA   B HA   1 
ATOM   5787 H  HB1  . ALA   B 1 124 ? 41.525 -22.588 -5.486  1.00 13.25 ?  124 ALA   B HB1  1 
ATOM   5788 H  HB2  . ALA   B 1 124 ? 41.510 -21.424 -6.567  1.00 13.25 ?  124 ALA   B HB2  1 
ATOM   5789 H  HB3  . ALA   B 1 124 ? 41.078 -22.896 -6.979  1.00 13.25 ?  124 ALA   B HB3  1 
ATOM   5790 N  N    . PRO   B 1 125 ? 43.695 -24.441 -5.199  1.00 10.75 ?  125 PRO   B N    1 
ATOM   5791 C  CA   . PRO   B 1 125 ? 43.629 -25.806 -4.678  1.00 11.47 ?  125 PRO   B CA   1 
ATOM   5792 C  C    . PRO   B 1 125 ? 42.232 -26.079 -4.126  1.00 11.25 ?  125 PRO   B C    1 
ATOM   5793 O  O    . PRO   B 1 125 ? 41.438 -25.162 -3.917  1.00 11.82 ?  125 PRO   B O    1 
ATOM   5794 C  CB   . PRO   B 1 125 ? 44.618 -25.735 -3.514  1.00 12.47 ?  125 PRO   B CB   1 
ATOM   5795 C  CG   . PRO   B 1 125 ? 44.369 -24.344 -2.943  1.00 12.42 ?  125 PRO   B CG   1 
ATOM   5796 C  CD   . PRO   B 1 125 ? 44.031 -23.474 -4.139  1.00 11.37 ?  125 PRO   B CD   1 
ATOM   5797 H  HA   . PRO   B 1 125 ? 43.896 -26.473 -5.327  1.00 13.74 ?  125 PRO   B HA   1 
ATOM   5798 H  HB2  . PRO   B 1 125 ? 44.417 -26.417 -2.854  1.00 14.95 ?  125 PRO   B HB2  1 
ATOM   5799 H  HB3  . PRO   B 1 125 ? 45.527 -25.817 -3.838  1.00 14.95 ?  125 PRO   B HB3  1 
ATOM   5800 H  HG2  . PRO   B 1 125 ? 43.626 -24.367 -2.319  1.00 14.88 ?  125 PRO   B HG2  1 
ATOM   5801 H  HG3  . PRO   B 1 125 ? 45.173 -24.019 -2.497  1.00 14.88 ?  125 PRO   B HG3  1 
ATOM   5802 H  HD2  . PRO   B 1 125 ? 43.273 -22.903 -3.945  1.00 13.62 ?  125 PRO   B HD2  1 
ATOM   5803 H  HD3  . PRO   B 1 125 ? 44.810 -22.943 -4.400  1.00 13.62 ?  125 PRO   B HD3  1 
ATOM   5804 N  N    . LEU   B 1 126 ? 41.965 -27.355 -3.841  1.00 11.99 ?  126 LEU   B N    1 
ATOM   5805 C  CA   . LEU   B 1 126 ? 40.745 -27.719 -3.128  1.00 12.59 ?  126 LEU   B CA   1 
ATOM   5806 C  C    . LEU   B 1 126 ? 40.860 -27.316 -1.666  1.00 12.78 ?  126 LEU   B C    1 
ATOM   5807 O  O    . LEU   B 1 126 ? 41.747 -27.786 -0.947  1.00 14.28 ?  126 LEU   B O    1 
ATOM   5808 C  CB   . LEU   B 1 126 ? 40.492 -29.218 -3.237  1.00 13.92 ?  126 LEU   B CB   1 
ATOM   5809 C  CG   . LEU   B 1 126 ? 39.968 -29.707 -4.588  1.00 14.87 ?  126 LEU   B CG   1 
ATOM   5810 C  CD1  . LEU   B 1 126 ? 40.001 -31.220 -4.657  1.00 16.79 ?  126 LEU   B CD1  1 
ATOM   5811 C  CD2  . LEU   B 1 126 ? 38.560 -29.208 -4.850  1.00 15.23 ?  126 LEU   B CD2  1 
ATOM   5812 H  H    . LEU   B 1 126 ? 42.473 -28.018 -4.039  1.00 14.37 ?  126 LEU   B H    1 
ATOM   5813 H  HA   . LEU   B 1 126 ? 39.992 -27.247 -3.517  1.00 15.08 ?  126 LEU   B HA   1 
ATOM   5814 H  HB2  . LEU   B 1 126 ? 41.325 -29.680 -3.063  1.00 16.68 ?  126 LEU   B HB2  1 
ATOM   5815 H  HB3  . LEU   B 1 126 ? 39.836 -29.466 -2.567  1.00 16.68 ?  126 LEU   B HB3  1 
ATOM   5816 H  HG   . LEU   B 1 126 ? 40.545 -29.366 -5.292  1.00 17.82 ?  126 LEU   B HG   1 
ATOM   5817 H  HD11 . LEU   B 1 126 ? 39.665 -31.504 -5.522  1.00 20.13 ?  126 LEU   B HD11 1 
ATOM   5818 H  HD12 . LEU   B 1 126 ? 40.910 -31.526 -4.535  1.00 20.13 ?  126 LEU   B HD12 1 
ATOM   5819 H  HD13 . LEU   B 1 126 ? 39.433 -31.578 -3.952  1.00 20.13 ?  126 LEU   B HD13 1 
ATOM   5820 H  HD21 . LEU   B 1 126 ? 38.219 -29.628 -5.654  1.00 18.25 ?  126 LEU   B HD21 1 
ATOM   5821 H  HD22 . LEU   B 1 126 ? 37.999 -29.433 -4.093  1.00 18.25 ?  126 LEU   B HD22 1 
ATOM   5822 H  HD23 . LEU   B 1 126 ? 38.583 -28.243 -4.968  1.00 18.25 ?  126 LEU   B HD23 1 
ATOM   5823 N  N    . LEU   B 1 127 ? 39.935 -26.481 -1.212  1.00 12.61 ?  127 LEU   B N    1 
ATOM   5824 C  CA   . LEU   B 1 127 ? 39.986 -25.992 0.153   1.00 13.03 ?  127 LEU   B CA   1 
ATOM   5825 C  C    . LEU   B 1 127 ? 39.716 -27.114 1.148   1.00 12.73 ?  127 LEU   B C    1 
ATOM   5826 O  O    . LEU   B 1 127 ? 38.895 -28.013 0.916   1.00 13.20 ?  127 LEU   B O    1 
ATOM   5827 C  CB   . LEU   B 1 127 ? 38.962 -24.873 0.353   1.00 13.67 ?  127 LEU   B CB   1 
ATOM   5828 C  CG   . LEU   B 1 127 ? 39.151 -23.608 -0.487  1.00 14.21 ?  127 LEU   B CG   1 
ATOM   5829 C  CD1  . LEU   B 1 127 ? 38.032 -22.634 -0.169  1.00 14.32 ?  127 LEU   B CD1  1 
ATOM   5830 C  CD2  . LEU   B 1 127 ? 40.516 -22.970 -0.246  1.00 14.92 ?  127 LEU   B CD2  1 
ATOM   5831 H  H    . LEU   B 1 127 ? 39.269 -26.178 -1.674  1.00 15.11 ?  127 LEU   B H    1 
ATOM   5832 H  HA   . LEU   B 1 127 ? 40.869 -25.627 0.330   1.00 15.61 ?  127 LEU   B HA   1 
ATOM   5833 H  HB2  . LEU   B 1 127 ? 38.081 -25.226 0.147   1.00 16.38 ?  127 LEU   B HB2  1 
ATOM   5834 H  HB3  . LEU   B 1 127 ? 38.984 -24.601 1.285   1.00 16.38 ?  127 LEU   B HB3  1 
ATOM   5835 H  HG   . LEU   B 1 127 ? 39.075 -23.832 -1.426  1.00 17.03 ?  127 LEU   B HG   1 
ATOM   5836 H  HD11 . LEU   B 1 127 ? 38.154 -21.821 -0.694  1.00 17.16 ?  127 LEU   B HD11 1 
ATOM   5837 H  HD12 . LEU   B 1 127 ? 37.177 -23.036 -0.388  1.00 17.16 ?  127 LEU   B HD12 1 
ATOM   5838 H  HD13 . LEU   B 1 127 ? 38.058 -22.411 0.777   1.00 17.16 ?  127 LEU   B HD13 1 
ATOM   5839 H  HD21 . LEU   B 1 127 ? 40.553 -22.114 -0.702  1.00 17.88 ?  127 LEU   B HD21 1 
ATOM   5840 H  HD22 . LEU   B 1 127 ? 40.640 -22.841 0.708   1.00 17.88 ?  127 LEU   B HD22 1 
ATOM   5841 H  HD23 . LEU   B 1 127 ? 41.200 -23.561 -0.592  1.00 17.88 ?  127 LEU   B HD23 1 
ATOM   5842 N  N    . SER   B 1 128 ? 40.404 -27.031 2.279   1.00 12.89 ?  128 SER   B N    1 
ATOM   5843 C  CA   . SER   B 1 128 ? 40.285 -27.943 3.404   1.00 13.58 ?  128 SER   B CA   1 
ATOM   5844 C  C    . SER   B 1 128 ? 40.772 -29.353 3.087   1.00 14.62 ?  128 SER   B C    1 
ATOM   5845 O  O    . SER   B 1 128 ? 40.671 -30.230 3.945   1.00 15.92 ?  128 SER   B O    1 
ATOM   5846 C  CB   . SER   B 1 128 ? 38.879 -27.949 4.018   1.00 13.74 ?  128 SER   B CB   1 
ATOM   5847 O  OG   . SER   B 1 128 ? 38.561 -26.674 4.563   1.00 14.29 ?  128 SER   B OG   1 
ATOM   5848 H  H    . SER   B 1 128 ? 40.981 -26.409 2.424   1.00 15.45 ?  128 SER   B H    1 
ATOM   5849 H  HA   . SER   B 1 128 ? 40.869 -27.612 4.092   1.00 16.27 ?  128 SER   B HA   1 
ATOM   5850 H  HB2  . SER   B 1 128 ? 38.227 -28.182 3.336   1.00 16.46 ?  128 SER   B HB2  1 
ATOM   5851 H  HB3  . SER   B 1 128 ? 38.850 -28.617 4.732   1.00 16.46 ?  128 SER   B HB3  1 
ATOM   5852 H  HG   . SER   B 1 128 ? 39.116 -26.471 5.155   1.00 17.13 ?  128 SER   B HG   1 
ATOM   5853 N  N    . ALA   B 1 129 ? 41.348 -29.580 1.904   1.00 15.62 ?  129 ALA   B N    1 
ATOM   5854 C  CA   . ALA   B 1 129 ? 41.893 -30.880 1.547   1.00 16.41 ?  129 ALA   B CA   1 
ATOM   5855 C  C    . ALA   B 1 129 ? 43.288 -31.052 2.134   1.00 15.64 ?  129 ALA   B C    1 
ATOM   5856 O  O    . ALA   B 1 129 ? 43.847 -30.154 2.780   1.00 15.32 ?  129 ALA   B O    1 
ATOM   5857 C  CB   . ALA   B 1 129 ? 41.936 -31.037 0.029   1.00 18.42 ?  129 ALA   B CB   1 
ATOM   5858 H  H    . ALA   B 1 129 ? 41.434 -28.986 1.281   1.00 18.72 ?  129 ALA   B H    1 
ATOM   5859 H  HA   . ALA   B 1 129 ? 41.321 -31.573 1.904   1.00 19.67 ?  129 ALA   B HA   1 
ATOM   5860 H  HB1  . ALA   B 1 129 ? 42.291 -31.915 -0.189  1.00 22.08 ?  129 ALA   B HB1  1 
ATOM   5861 H  HB2  . ALA   B 1 129 ? 41.039 -30.947 -0.325  1.00 22.08 ?  129 ALA   B HB2  1 
ATOM   5862 H  HB3  . ALA   B 1 129 ? 42.510 -30.350 -0.346  1.00 22.08 ?  129 ALA   B HB3  1 
ATOM   5863 N  N    . GLY   B 1 130 ? 43.854 -32.232 1.895   1.00 15.48 ?  130 GLY   B N    1 
ATOM   5864 C  CA   . GLY   B 1 130 ? 45.242 -32.466 2.245   1.00 16.06 ?  130 GLY   B CA   1 
ATOM   5865 C  C    . GLY   B 1 130 ? 45.456 -32.380 3.738   1.00 16.21 ?  130 GLY   B C    1 
ATOM   5866 O  O    . GLY   B 1 130 ? 44.754 -33.020 4.534   1.00 17.07 ?  130 GLY   B O    1 
ATOM   5867 H  H    . GLY   B 1 130 ? 43.459 -32.906 1.525   1.00 18.55 ?  130 GLY   B H    1 
ATOM   5868 H  HA2  . GLY   B 1 130 ? 45.510 -33.349 1.943   1.00 19.25 ?  130 GLY   B HA2  1 
ATOM   5869 H  HA3  . GLY   B 1 130 ? 45.802 -31.806 1.806   1.00 19.25 ?  130 GLY   B HA3  1 
ATOM   5870 N  N    . ILE   B 1 131 ? 46.435 -31.556 4.126   1.00 16.58 ?  131 ILE   B N    1 
ATOM   5871 C  CA   . ILE   B 1 131 ? 46.791 -31.422 5.532   1.00 17.53 ?  131 ILE   B CA   1 
ATOM   5872 C  C    . ILE   B 1 131 ? 45.672 -30.822 6.365   1.00 16.68 ?  131 ILE   B C    1 
ATOM   5873 O  O    . ILE   B 1 131 ? 45.744 -30.887 7.596   1.00 18.13 ?  131 ILE   B O    1 
ATOM   5874 C  CB   . ILE   B 1 131 ? 48.113 -30.648 5.734   1.00 19.32 ?  131 ILE   B CB   1 
ATOM   5875 C  CG1  . ILE   B 1 131 ? 47.947 -29.165 5.373   1.00 20.36 ?  131 ILE   B CG1  1 
ATOM   5876 C  CG2  . ILE   B 1 131 ? 49.234 -31.284 4.913   1.00 20.24 ?  131 ILE   B CG2  1 
ATOM   5877 C  CD1  . ILE   B 1 131 ? 49.171 -28.313 5.681   1.00 21.47 ?  131 ILE   B CD1  1 
ATOM   5878 H  H    . ILE   B 1 131 ? 46.901 -31.063 3.597   1.00 19.87 ?  131 ILE   B H    1 
ATOM   5879 H  HA   . ILE   B 1 131 ? 46.932 -32.310 5.880   1.00 21.01 ?  131 ILE   B HA   1 
ATOM   5880 H  HB   . ILE   B 1 131 ? 48.350 -30.704 6.674   1.00 23.16 ?  131 ILE   B HB   1 
ATOM   5881 H  HG12 . ILE   B 1 131 ? 47.765 -29.096 4.422   1.00 24.41 ?  131 ILE   B HG12 1 
ATOM   5882 H  HG13 . ILE   B 1 131 ? 47.200 -28.792 5.873   1.00 24.41 ?  131 ILE   B HG13 1 
ATOM   5883 H  HG21 . ILE   B 1 131 ? 50.075 -30.884 5.172   1.00 24.26 ?  131 ILE   B HG21 1 
ATOM   5884 H  HG22 . ILE   B 1 131 ? 49.244 -32.235 5.085   1.00 24.26 ?  131 ILE   B HG22 1 
ATOM   5885 H  HG23 . ILE   B 1 131 ? 49.059 -31.116 3.972   1.00 24.26 ?  131 ILE   B HG23 1 
ATOM   5886 H  HD11 . ILE   B 1 131 ? 48.956 -27.381 5.522   1.00 25.74 ?  131 ILE   B HD11 1 
ATOM   5887 H  HD12 . ILE   B 1 131 ? 49.418 -28.441 6.611   1.00 25.74 ?  131 ILE   B HD12 1 
ATOM   5888 H  HD13 . ILE   B 1 131 ? 49.901 -28.588 5.105   1.00 25.74 ?  131 ILE   B HD13 1 
ATOM   5889 N  N    . PHE   B 1 132 ? 44.641 -30.246 5.735   1.00 15.58 ?  132 PHE   B N    1 
ATOM   5890 C  CA   . PHE   B 1 132 ? 43.485 -29.734 6.464   1.00 16.01 ?  132 PHE   B CA   1 
ATOM   5891 C  C    . PHE   B 1 132 ? 42.460 -30.817 6.800   1.00 17.34 ?  132 PHE   B C    1 
ATOM   5892 O  O    . PHE   B 1 132 ? 41.556 -30.559 7.604   1.00 18.87 ?  132 PHE   B O    1 
ATOM   5893 C  CB   . PHE   B 1 132 ? 42.811 -28.600 5.680   1.00 14.97 ?  132 PHE   B CB   1 
ATOM   5894 C  CG   . PHE   B 1 132 ? 43.514 -27.260 5.786   1.00 14.71 ?  132 PHE   B CG   1 
ATOM   5895 C  CD1  . PHE   B 1 132 ? 44.803 -27.081 5.305   1.00 15.52 ?  132 PHE   B CD1  1 
ATOM   5896 C  CD2  . PHE   B 1 132 ? 42.850 -26.162 6.318   1.00 14.12 ?  132 PHE   B CD2  1 
ATOM   5897 C  CE1  . PHE   B 1 132 ? 45.426 -25.846 5.394   1.00 15.91 ?  132 PHE   B CE1  1 
ATOM   5898 C  CE2  . PHE   B 1 132 ? 43.462 -24.922 6.399   1.00 14.70 ?  132 PHE   B CE2  1 
ATOM   5899 C  CZ   . PHE   B 1 132 ? 44.749 -24.767 5.939   1.00 15.41 ?  132 PHE   B CZ   1 
ATOM   5900 H  H    . PHE   B 1 132 ? 44.583 -30.148 4.881   1.00 18.67 ?  132 PHE   B H    1 
ATOM   5901 H  HA   . PHE   B 1 132 ? 43.793 -29.362 7.301   1.00 19.19 ?  132 PHE   B HA   1 
ATOM   5902 H  HB2  . PHE   B 1 132 ? 42.794 -28.844 4.744   1.00 17.94 ?  132 PHE   B HB2  1 
ATOM   5903 H  HB3  . PHE   B 1 132 ? 41.906 -28.488 6.010   1.00 17.94 ?  132 PHE   B HB3  1 
ATOM   5904 H  HD1  . PHE   B 1 132 ? 45.262 -27.807 4.943   1.00 18.60 ?  132 PHE   B HD1  1 
ATOM   5905 H  HD2  . PHE   B 1 132 ? 41.983 -26.264 6.636   1.00 16.92 ?  132 PHE   B HD2  1 
ATOM   5906 H  HE1  . PHE   B 1 132 ? 46.295 -25.740 5.079   1.00 19.07 ?  132 PHE   B HE1  1 
ATOM   5907 H  HE2  . PHE   B 1 132 ? 43.013 -24.196 6.773   1.00 17.61 ?  132 PHE   B HE2  1 
ATOM   5908 H  HZ   . PHE   B 1 132 ? 45.168 -23.934 5.998   1.00 18.46 ?  132 PHE   B HZ   1 
ATOM   5909 N  N    . GLY   B 1 133 ? 42.559 -32.010 6.205   1.00 17.15 ?  133 GLY   B N    1 
ATOM   5910 C  CA   . GLY   B 1 133 ? 41.846 -33.171 6.704   1.00 17.95 ?  133 GLY   B CA   1 
ATOM   5911 C  C    . GLY   B 1 133 ? 40.455 -33.442 6.162   1.00 18.33 ?  133 GLY   B C    1 
ATOM   5912 O  O    . GLY   B 1 133 ? 39.876 -34.471 6.521   1.00 20.11 ?  133 GLY   B O    1 
ATOM   5913 H  H    . GLY   B 1 133 ? 43.042 -32.165 5.509   1.00 20.56 ?  133 GLY   B H    1 
ATOM   5914 H  HA2  . GLY   B 1 133 ? 42.387 -33.955 6.527   1.00 21.51 ?  133 GLY   B HA2  1 
ATOM   5915 H  HA3  . GLY   B 1 133 ? 41.762 -33.083 7.664   1.00 21.51 ?  133 GLY   B HA3  1 
ATOM   5916 N  N    . ALA   B 1 134 ? 39.890 -32.574 5.330   1.00 17.32 ?  134 ALA   B N    1 
ATOM   5917 C  CA   . ALA   B 1 134 ? 38.569 -32.863 4.793   1.00 17.22 ?  134 ALA   B CA   1 
ATOM   5918 C  C    . ALA   B 1 134 ? 38.662 -33.850 3.633   1.00 17.40 ?  134 ALA   B C    1 
ATOM   5919 O  O    . ALA   B 1 134 ? 39.715 -34.035 3.018   1.00 18.39 ?  134 ALA   B O    1 
ATOM   5920 C  CB   . ALA   B 1 134 ? 37.883 -31.580 4.325   1.00 17.54 ?  134 ALA   B CB   1 
ATOM   5921 H  H    . ALA   B 1 134 ? 40.236 -31.823 5.076   1.00 20.76 ?  134 ALA   B H    1 
ATOM   5922 H  HA   . ALA   B 1 134 ? 38.023 -33.256 5.493   1.00 20.64 ?  134 ALA   B HA   1 
ATOM   5923 H  HB1  . ALA   B 1 134 ? 36.997 -31.800 3.992   1.00 21.03 ?  134 ALA   B HB1  1 
ATOM   5924 H  HB2  . ALA   B 1 134 ? 37.809 -30.966 5.073   1.00 21.03 ?  134 ALA   B HB2  1 
ATOM   5925 H  HB3  . ALA   B 1 134 ? 38.410 -31.178 3.618   1.00 21.03 ?  134 ALA   B HB3  1 
ATOM   5926 N  N    . ASP   B 1 135 ? 37.532 -34.479 3.341   1.00 17.83 ?  135 ASP   B N    1 
ATOM   5927 C  CA   . ASP   B 1 135 ? 37.437 -35.371 2.198   1.00 18.65 ?  135 ASP   B CA   1 
ATOM   5928 C  C    . ASP   B 1 135 ? 37.535 -34.534 0.930   1.00 17.47 ?  135 ASP   B C    1 
ATOM   5929 O  O    . ASP   B 1 135 ? 36.686 -33.657 0.713   1.00 17.25 ?  135 ASP   B O    1 
ATOM   5930 C  CB   . ASP   B 1 135 ? 36.098 -36.101 2.251   1.00 20.42 ?  135 ASP   B CB   1 
ATOM   5931 C  CG   . ASP   B 1 135 ? 35.922 -37.098 1.125   1.00 22.09 ?  135 ASP   B CG   1 
ATOM   5932 O  OD1  . ASP   B 1 135 ? 36.792 -37.152 0.228   1.00 21.82 ?  135 ASP   B OD1  1 
ATOM   5933 O  OD2  . ASP   B 1 135 ? 34.915 -37.843 1.151   1.00 24.72 -1 135 ASP   B OD2  1 
ATOM   5934 H  H    . ASP   B 1 135 ? 36.802 -34.402 3.789   1.00 21.37 ?  135 ASP   B H    1 
ATOM   5935 H  HA   . ASP   B 1 135 ? 38.156 -36.024 2.231   1.00 22.36 ?  135 ASP   B HA   1 
ATOM   5936 H  HB2  . ASP   B 1 135 ? 36.040 -36.586 3.087   1.00 24.49 ?  135 ASP   B HB2  1 
ATOM   5937 H  HB3  . ASP   B 1 135 ? 35.386 -35.451 2.189   1.00 24.49 ?  135 ASP   B HB3  1 
ATOM   5938 N  N    . PRO   B 1 136 ? 38.541 -34.747 0.080   1.00 17.31 ?  136 PRO   B N    1 
ATOM   5939 C  CA   . PRO   B 1 136 ? 38.642 -33.923 -1.135  1.00 16.42 ?  136 PRO   B CA   1 
ATOM   5940 C  C    . PRO   B 1 136 ? 37.449 -34.074 -2.059  1.00 15.98 ?  136 PRO   B C    1 
ATOM   5941 O  O    . PRO   B 1 136 ? 37.121 -33.127 -2.781  1.00 15.23 ?  136 PRO   B O    1 
ATOM   5942 C  CB   . PRO   B 1 136 ? 39.953 -34.399 -1.781  1.00 17.30 ?  136 PRO   B CB   1 
ATOM   5943 C  CG   . PRO   B 1 136 ? 40.154 -35.788 -1.240  1.00 18.44 ?  136 PRO   B CG   1 
ATOM   5944 C  CD   . PRO   B 1 136 ? 39.617 -35.747 0.161   1.00 18.15 ?  136 PRO   B CD   1 
ATOM   5945 H  HA   . PRO   B 1 136 ? 38.734 -32.989 -0.899  1.00 19.68 ?  136 PRO   B HA   1 
ATOM   5946 H  HB2  . PRO   B 1 136 ? 39.860 -34.419 -2.749  1.00 20.74 ?  136 PRO   B HB2  1 
ATOM   5947 H  HB3  . PRO   B 1 136 ? 40.682 -33.818 -1.518  1.00 20.74 ?  136 PRO   B HB3  1 
ATOM   5948 H  HG2  . PRO   B 1 136 ? 39.658 -36.430 -1.774  1.00 22.11 ?  136 PRO   B HG2  1 
ATOM   5949 H  HG3  . PRO   B 1 136 ? 41.101 -36.010 -1.234  1.00 22.11 ?  136 PRO   B HG3  1 
ATOM   5950 H  HD2  . PRO   B 1 136 ? 39.258 -36.613 0.414   1.00 21.76 ?  136 PRO   B HD2  1 
ATOM   5951 H  HD3  . PRO   B 1 136 ? 40.305 -35.454 0.783   1.00 21.76 ?  136 PRO   B HD3  1 
ATOM   5952 N  N    . ILE   B 1 137 ? 36.791 -35.238 -2.059  1.00 16.35 ?  137 ILE   B N    1 
ATOM   5953 C  CA   . ILE   B 1 137 ? 35.569 -35.405 -2.845  1.00 16.81 ?  137 ILE   B CA   1 
ATOM   5954 C  C    . ILE   B 1 137 ? 34.498 -34.434 -2.365  1.00 16.26 ?  137 ILE   B C    1 
ATOM   5955 O  O    . ILE   B 1 137 ? 33.780 -33.819 -3.166  1.00 15.78 ?  137 ILE   B O    1 
ATOM   5956 C  CB   . ILE   B 1 137 ? 35.092 -36.873 -2.780  1.00 18.69 ?  137 ILE   B CB   1 
ATOM   5957 C  CG1  . ILE   B 1 137 ? 36.097 -37.784 -3.489  1.00 20.93 ?  137 ILE   B CG1  1 
ATOM   5958 C  CG2  . ILE   B 1 137 ? 33.694 -37.011 -3.382  1.00 18.72 ?  137 ILE   B CG2  1 
ATOM   5959 C  CD1  . ILE   B 1 137 ? 35.765 -39.261 -3.395  1.00 23.10 ?  137 ILE   B CD1  1 
ATOM   5960 H  H    . ILE   B 1 137 ? 37.029 -35.941 -1.624  1.00 19.60 ?  137 ILE   B H    1 
ATOM   5961 H  HA   . ILE   B 1 137 ? 35.761 -35.201 -3.775  1.00 20.16 ?  137 ILE   B HA   1 
ATOM   5962 H  HB   . ILE   B 1 137 ? 35.045 -37.138 -1.854  1.00 22.41 ?  137 ILE   B HB   1 
ATOM   5963 H  HG12 . ILE   B 1 137 ? 36.128 -37.554 -4.430  1.00 25.09 ?  137 ILE   B HG12 1 
ATOM   5964 H  HG13 . ILE   B 1 137 ? 36.971 -37.657 -3.090  1.00 25.09 ?  137 ILE   B HG13 1 
ATOM   5965 H  HG21 . ILE   B 1 137 ? 33.427 -37.945 -3.383  1.00 22.44 ?  137 ILE   B HG21 1 
ATOM   5966 H  HG22 . ILE   B 1 137 ? 33.060 -36.509 -2.848  1.00 22.44 ?  137 ILE   B HG22 1 
ATOM   5967 H  HG23 . ILE   B 1 137 ? 33.701 -36.674 -4.291  1.00 22.44 ?  137 ILE   B HG23 1 
ATOM   5968 H  HD11 . ILE   B 1 137 ? 36.392 -39.746 -3.949  1.00 27.69 ?  137 ILE   B HD11 1 
ATOM   5969 H  HD12 . ILE   B 1 137 ? 35.843 -39.548 -2.470  1.00 27.69 ?  137 ILE   B HD12 1 
ATOM   5970 H  HD13 . ILE   B 1 137 ? 34.865 -39.420 -3.718  1.00 27.69 ?  137 ILE   B HD13 1 
ATOM   5971 N  N    . HIS   B 1 138 ? 34.368 -34.285 -1.051  1.00 16.55 ?  138 HIS   B N    1 
ATOM   5972 C  CA   . HIS   B 1 138 ? 33.415 -33.323 -0.517  1.00 16.85 ?  138 HIS   B CA   1 
ATOM   5973 C  C    . HIS   B 1 138 ? 33.830 -31.894 -0.842  1.00 15.74 ?  138 HIS   B C    1 
ATOM   5974 O  O    . HIS   B 1 138 ? 32.985 -31.054 -1.163  1.00 16.13 ?  138 HIS   B O    1 
ATOM   5975 C  CB   . HIS   B 1 138 ? 33.290 -33.505 0.988   1.00 18.04 ?  138 HIS   B CB   1 
ATOM   5976 C  CG   . HIS   B 1 138 ? 32.362 -32.524 1.623   1.00 19.27 ?  138 HIS   B CG   1 
ATOM   5977 N  ND1  . HIS   B 1 138 ? 31.024 -32.450 1.301   1.00 20.56 ?  138 HIS   B ND1  1 
ATOM   5978 C  CD2  . HIS   B 1 138 ? 32.583 -31.553 2.540   1.00 19.93 ?  138 HIS   B CD2  1 
ATOM   5979 C  CE1  . HIS   B 1 138 ? 30.457 -31.486 2.003   1.00 20.76 ?  138 HIS   B CE1  1 
ATOM   5980 N  NE2  . HIS   B 1 138 ? 31.382 -30.927 2.764   1.00 20.20 ?  138 HIS   B NE2  1 
ATOM   5981 H  H    . HIS   B 1 138 ? 34.815 -34.721 -0.461  1.00 19.83 ?  138 HIS   B H    1 
ATOM   5982 H  HA   . HIS   B 1 138 ? 32.544 -33.489 -0.916  1.00 20.20 ?  138 HIS   B HA   1 
ATOM   5983 H  HB2  . HIS   B 1 138 ? 32.947 -34.394 1.172   1.00 21.63 ?  138 HIS   B HB2  1 
ATOM   5984 H  HB3  . HIS   B 1 138 ? 34.161 -33.394 1.393   1.00 21.63 ?  138 HIS   B HB3  1 
ATOM   5985 H  HD1  . HIS   B 1 138 ? 30.618 -32.958 0.735   1.00 24.66 ?  138 HIS   B HD1  1 
ATOM   5986 H  HD2  . HIS   B 1 138 ? 33.387 -31.353 2.955   1.00 23.90 ?  138 HIS   B HD2  1 
ATOM   5987 H  HE1  . HIS   B 1 138 ? 29.553 -31.249 1.973   1.00 24.89 ?  138 HIS   B HE1  1 
ATOM   5988 N  N    . SER   B 1 139 ? 35.123 -31.593 -0.761  1.00 15.29 ?  139 SER   B N    1 
ATOM   5989 C  CA   . SER   B 1 139 ? 35.560 -30.243 -1.082  1.00 14.74 ?  139 SER   B CA   1 
ATOM   5990 C  C    . SER   B 1 139 ? 35.229 -29.894 -2.524  1.00 13.74 ?  139 SER   B C    1 
ATOM   5991 O  O    . SER   B 1 139 ? 34.777 -28.779 -2.805  1.00 13.72 ?  139 SER   B O    1 
ATOM   5992 C  CB   . SER   B 1 139 ? 37.053 -30.106 -0.809  1.00 15.07 ?  139 SER   B CB   1 
ATOM   5993 O  OG   . SER   B 1 139 ? 37.470 -28.776 -1.068  1.00 15.00 ?  139 SER   B OG   1 
ATOM   5994 H  H    . SER   B 1 139 ? 35.742 -32.137 -0.536  1.00 18.32 ?  139 SER   B H    1 
ATOM   5995 H  HA   . SER   B 1 139 ? 35.086 -29.618 -0.515  1.00 17.66 ?  139 SER   B HA   1 
ATOM   5996 H  HB2  . SER   B 1 139 ? 37.224 -30.321 0.123   1.00 18.06 ?  139 SER   B HB2  1 
ATOM   5997 H  HB3  . SER   B 1 139 ? 37.542 -30.712 -1.386  1.00 18.06 ?  139 SER   B HB3  1 
ATOM   5998 H  HG   . SER   B 1 139 ? 38.297 -28.701 -0.908  1.00 17.97 ?  139 SER   B HG   1 
ATOM   5999 N  N    . LEU   B 1 140 ? 35.417 -30.841 -3.448  1.00 13.38 ?  140 LEU   B N    1 
ATOM   6000 C  CA   . LEU   B 1 140 ? 35.053 -30.596 -4.837  1.00 13.26 ?  140 LEU   B CA   1 
ATOM   6001 C  C    . LEU   B 1 140 ? 33.552 -30.370 -4.972  1.00 13.68 ?  140 LEU   B C    1 
ATOM   6002 O  O    . LEU   B 1 140 ? 33.115 -29.489 -5.718  1.00 13.79 ?  140 LEU   B O    1 
ATOM   6003 C  CB   . LEU   B 1 140 ? 35.529 -31.754 -5.715  1.00 13.50 ?  140 LEU   B CB   1 
ATOM   6004 C  CG   . LEU   B 1 140 ? 35.162 -31.658 -7.191  1.00 14.15 ?  140 LEU   B CG   1 
ATOM   6005 C  CD1  . LEU   B 1 140 ? 35.716 -30.378 -7.802  1.00 14.78 ?  140 LEU   B CD1  1 
ATOM   6006 C  CD2  . LEU   B 1 140 ? 35.653 -32.888 -7.930  1.00 15.17 ?  140 LEU   B CD2  1 
ATOM   6007 H  H    . LEU   B 1 140 ? 35.748 -31.621 -3.299  1.00 16.03 ?  140 LEU   B H    1 
ATOM   6008 H  HA   . LEU   B 1 140 ? 35.506 -29.793 -5.140  1.00 15.89 ?  140 LEU   B HA   1 
ATOM   6009 H  HB2  . LEU   B 1 140 ? 36.497 -31.806 -5.661  1.00 16.18 ?  140 LEU   B HB2  1 
ATOM   6010 H  HB3  . LEU   B 1 140 ? 35.142 -32.577 -5.377  1.00 16.18 ?  140 LEU   B HB3  1 
ATOM   6011 H  HG   . LEU   B 1 140 ? 34.197 -31.624 -7.272  1.00 16.96 ?  140 LEU   B HG   1 
ATOM   6012 H  HD11 . LEU   B 1 140 ? 35.578 -30.407 -8.760  1.00 17.71 ?  140 LEU   B HD11 1 
ATOM   6013 H  HD12 . LEU   B 1 140 ? 35.245 -29.618 -7.422  1.00 17.71 ?  140 LEU   B HD12 1 
ATOM   6014 H  HD13 . LEU   B 1 140 ? 36.661 -30.318 -7.602  1.00 17.71 ?  140 LEU   B HD13 1 
ATOM   6015 H  HD21 . LEU   B 1 140 ? 35.407 -32.806 -8.865  1.00 18.18 ?  140 LEU   B HD21 1 
ATOM   6016 H  HD22 . LEU   B 1 140 ? 36.612 -32.948 -7.839  1.00 18.18 ?  140 LEU   B HD22 1 
ATOM   6017 H  HD23 . LEU   B 1 140 ? 35.227 -33.669 -7.544  1.00 18.18 ?  140 LEU   B HD23 1 
ATOM   6018 N  N    . ARG   B 1 141 ? 32.751 -31.157 -4.249  1.00 14.01 ?  141 ARG   B N    1 
ATOM   6019 C  CA   . ARG   B 1 141 ? 31.301 -30.981 -4.228  1.00 14.97 ?  141 ARG   B CA   1 
ATOM   6020 C  C    . ARG   B 1 141 ? 30.928 -29.568 -3.805  1.00 14.56 ?  141 ARG   B C    1 
ATOM   6021 O  O    . ARG   B 1 141 ? 30.120 -28.895 -4.462  1.00 14.76 ?  141 ARG   B O    1 
ATOM   6022 C  CB   . ARG   B 1 141 ? 30.715 -32.004 -3.245  1.00 16.27 ?  141 ARG   B CB   1 
ATOM   6023 C  CG   . ARG   B 1 141 ? 29.247 -31.888 -2.922  1.00 17.89 ?  141 ARG   B CG   1 
ATOM   6024 C  CD   . ARG   B 1 141 ? 28.450 -32.530 -3.985  1.00 19.58 ?  141 ARG   B CD   1 
ATOM   6025 N  NE   . ARG   B 1 141 ? 28.184 -31.626 -5.093  1.00 19.70 ?  141 ARG   B NE   1 
ATOM   6026 C  CZ   . ARG   B 1 141 ? 28.190 -31.979 -6.370  1.00 19.46 ?  141 ARG   B CZ   1 
ATOM   6027 N  NH1  . ARG   B 1 141 ? 28.631 -33.165 -6.760  1.00 19.38 ?  141 ARG   B NH1  1 
ATOM   6028 N  NH2  . ARG   B 1 141 ? 27.738 -31.121 -7.281  1.00 20.26 ?  141 ARG   B NH2  1 
ATOM   6029 H  H    . ARG   B 1 141 ? 33.033 -31.801 -3.753  1.00 16.79 ?  141 ARG   B H    1 
ATOM   6030 H  HA   . ARG   B 1 141 ? 30.937 -31.148 -5.106  1.00 17.94 ?  141 ARG   B HA   1 
ATOM   6031 H  HB2  . ARG   B 1 141 ? 30.871 -32.892 -3.607  1.00 19.50 ?  141 ARG   B HB2  1 
ATOM   6032 H  HB3  . ARG   B 1 141 ? 31.197 -31.925 -2.406  1.00 19.50 ?  141 ARG   B HB3  1 
ATOM   6033 H  HG2  . ARG   B 1 141 ? 29.073 -32.333 -2.081  1.00 21.45 ?  141 ARG   B HG2  1 
ATOM   6034 H  HG3  . ARG   B 1 141 ? 28.994 -30.949 -2.862  1.00 21.45 ?  141 ARG   B HG3  1 
ATOM   6035 H  HD2  . ARG   B 1 141 ? 28.932 -33.308 -4.317  1.00 23.47 ?  141 ARG   B HD2  1 
ATOM   6036 H  HD3  . ARG   B 1 141 ? 27.605 -32.811 -3.611  1.00 23.47 ?  141 ARG   B HD3  1 
ATOM   6037 H  HE   . ARG   B 1 141 ? 27.989 -30.812 -4.904  1.00 23.61 ?  141 ARG   B HE   1 
ATOM   6038 H  HH11 . ARG   B 1 141 ? 28.918 -33.739 -6.184  1.00 23.23 ?  141 ARG   B HH11 1 
ATOM   6039 H  HH12 . ARG   B 1 141 ? 28.638 -33.368 -7.594  1.00 23.23 ?  141 ARG   B HH12 1 
ATOM   6040 H  HH21 . ARG   B 1 141 ? 27.460 -30.344 -7.040  1.00 24.29 ?  141 ARG   B HH21 1 
ATOM   6041 H  HH22 . ARG   B 1 141 ? 27.761 -31.329 -8.117  1.00 24.29 ?  141 ARG   B HH22 1 
ATOM   6042 N  N    . VAL   B 1 142 ? 31.478 -29.119 -2.681  1.00 14.19 ?  142 VAL   B N    1 
ATOM   6043 C  CA   . VAL   B 1 142 ? 31.134 -27.788 -2.198  1.00 13.99 ?  142 VAL   B CA   1 
ATOM   6044 C  C    . VAL   B 1 142 ? 31.606 -26.730 -3.188  1.00 13.81 ?  142 VAL   B C    1 
ATOM   6045 O  O    . VAL   B 1 142 ? 30.907 -25.745 -3.446  1.00 14.27 ?  142 VAL   B O    1 
ATOM   6046 C  CB   . VAL   B 1 142 ? 31.676 -27.557 -0.774  1.00 14.79 ?  142 VAL   B CB   1 
ATOM   6047 C  CG1  . VAL   B 1 142 ? 31.363 -26.139 -0.305  1.00 14.74 ?  142 VAL   B CG1  1 
ATOM   6048 C  CG2  . VAL   B 1 142 ? 31.078 -28.573 0.184   1.00 15.58 ?  142 VAL   B CG2  1 
ATOM   6049 H  H    . VAL   B 1 142 ? 32.043 -29.550 -2.191  1.00 17.00 ?  142 VAL   B H    1 
ATOM   6050 H  HA   . VAL   B 1 142 ? 30.174 -27.721 -2.147  1.00 16.77 ?  142 VAL   B HA   1 
ATOM   6051 H  HB   . VAL   B 1 142 ? 32.640 -27.671 -0.770  1.00 17.72 ?  142 VAL   B HB   1 
ATOM   6052 H  HG11 . VAL   B 1 142 ? 31.543 -26.076 0.645   1.00 17.66 ?  142 VAL   B HG11 1 
ATOM   6053 H  HG12 . VAL   B 1 142 ? 31.927 -25.515 -0.789  1.00 17.66 ?  142 VAL   B HG12 1 
ATOM   6054 H  HG13 . VAL   B 1 142 ? 30.430 -25.950 -0.480  1.00 17.66 ?  142 VAL   B HG13 1 
ATOM   6055 H  HG21 . VAL   B 1 142 ? 31.391 -28.386 1.082   1.00 18.67 ?  142 VAL   B HG21 1 
ATOM   6056 H  HG22 . VAL   B 1 142 ? 30.110 -28.506 0.150   1.00 18.67 ?  142 VAL   B HG22 1 
ATOM   6057 H  HG23 . VAL   B 1 142 ? 31.356 -29.463 -0.085  1.00 18.67 ?  142 VAL   B HG23 1 
ATOM   6058 N  N    . CYS   B 1 143 ? 32.792 -26.923 -3.767  1.00 13.26 ?  143 CYS   B N    1 
ATOM   6059 C  CA   . CYS   B 1 143 ? 33.284 -25.991 -4.777  1.00 13.23 ?  143 CYS   B CA   1 
ATOM   6060 C  C    . CYS   B 1 143 ? 32.281 -25.848 -5.916  1.00 13.44 ?  143 CYS   B C    1 
ATOM   6061 O  O    . CYS   B 1 143 ? 31.876 -24.735 -6.279  1.00 13.42 ?  143 CYS   B O    1 
ATOM   6062 C  CB   . CYS   B 1 143 ? 34.640 -26.479 -5.299  1.00 13.48 ?  143 CYS   B CB   1 
ATOM   6063 S  SG   . CYS   B 1 143 ? 35.386 -25.382 -6.527  1.00 13.57 ?  143 CYS   B SG   1 
ATOM   6064 H  H    . CYS   B 1 143 ? 33.332 -27.568 -3.589  1.00 15.89 ?  143 CYS   B H    1 
ATOM   6065 H  HA   . CYS   B 1 143 ? 33.419 -25.117 -4.379  1.00 15.85 ?  143 CYS   B HA   1 
ATOM   6066 H  HB2  . CYS   B 1 143 ? 35.268 -26.554 -4.558  1.00 16.15 ?  143 CYS   B HB2  1 
ATOM   6067 H  HB3  . CYS   B 1 143 ? 34.532 -27.347 -5.712  1.00 16.15 ?  143 CYS   B HB3  1 
ATOM   6068 H  HG   . CYS   B 1 143 ? 36.470 -25.807 -6.841  1.00 16.26 ?  143 CYS   B HG   1 
ATOM   6069 N  N    . VAL   B 1 144 ? 31.877 -26.972 -6.502  1.00 13.89 ?  144 VAL   B N    1 
ATOM   6070 C  CA   . VAL   B 1 144 ? 30.971 -26.922 -7.643  1.00 14.87 ?  144 VAL   B CA   1 
ATOM   6071 C  C    . VAL   B 1 144 ? 29.632 -26.300 -7.264  1.00 15.05 ?  144 VAL   B C    1 
ATOM   6072 O  O    . VAL   B 1 144 ? 29.013 -25.597 -8.070  1.00 16.26 ?  144 VAL   B O    1 
ATOM   6073 C  CB   . VAL   B 1 144 ? 30.811 -28.336 -8.213  1.00 17.15 ?  144 VAL   B CB   1 
ATOM   6074 C  CG1  . VAL   B 1 144 ? 29.542 -28.469 -9.046  1.00 19.41 ?  144 VAL   B CG1  1 
ATOM   6075 C  CG2  . VAL   B 1 144 ? 32.058 -28.731 -8.998  1.00 17.11 ?  144 VAL   B CG2  1 
ATOM   6076 H  H    . VAL   B 1 144 ? 32.125 -27.764 -6.276  1.00 16.65 ?  144 VAL   B H    1 
ATOM   6077 H  HA   . VAL   B 1 144 ? 31.356 -26.368 -8.333  1.00 17.82 ?  144 VAL   B HA   1 
ATOM   6078 H  HB   . VAL   B 1 144 ? 30.735 -28.959 -7.473  1.00 20.56 ?  144 VAL   B HB   1 
ATOM   6079 H  HG11 . VAL   B 1 144 ? 29.620 -29.258 -9.609  1.00 23.28 ?  144 VAL   B HG11 1 
ATOM   6080 H  HG12 . VAL   B 1 144 ? 28.784 -28.566 -8.451  1.00 23.28 ?  144 VAL   B HG12 1 
ATOM   6081 H  HG13 . VAL   B 1 144 ? 29.442 -27.681 -9.598  1.00 23.28 ?  144 VAL   B HG13 1 
ATOM   6082 H  HG21 . VAL   B 1 144 ? 31.943 -29.631 -9.346  1.00 20.51 ?  144 VAL   B HG21 1 
ATOM   6083 H  HG22 . VAL   B 1 144 ? 32.180 -28.108 -9.733  1.00 20.51 ?  144 VAL   B HG22 1 
ATOM   6084 H  HG23 . VAL   B 1 144 ? 32.827 -28.702 -8.408  1.00 20.51 ?  144 VAL   B HG23 1 
ATOM   6085 N  N    . ASP   B 1 145 ? 29.162 -26.551 -6.046  1.00 15.20 ?  145 ASP   B N    1 
ATOM   6086 C  CA   . ASP   B 1 145 ? 27.854 -26.076 -5.613  1.00 15.72 ?  145 ASP   B CA   1 
ATOM   6087 C  C    . ASP   B 1 145 ? 27.886 -24.653 -5.072  1.00 15.34 ?  145 ASP   B C    1 
ATOM   6088 O  O    . ASP   B 1 145 ? 26.825 -24.113 -4.733  1.00 16.85 ?  145 ASP   B O    1 
ATOM   6089 C  CB   . ASP   B 1 145 ? 27.265 -26.992 -4.533  1.00 17.22 ?  145 ASP   B CB   1 
ATOM   6090 C  CG   . ASP   B 1 145 ? 26.901 -28.363 -5.045  1.00 19.09 ?  145 ASP   B CG   1 
ATOM   6091 O  OD1  . ASP   B 1 145 ? 26.799 -28.553 -6.274  1.00 19.33 ?  145 ASP   B OD1  1 
ATOM   6092 O  OD2  . ASP   B 1 145 ? 26.712 -29.247 -4.191  1.00 21.29 -1 145 ASP   B OD2  1 
ATOM   6093 H  H    . ASP   B 1 145 ? 29.594 -26.981 -5.445  1.00 18.22 ?  145 ASP   B H    1 
ATOM   6094 H  HA   . ASP   B 1 145 ? 27.258 -26.070 -6.371  1.00 18.84 ?  145 ASP   B HA   1 
ATOM   6095 H  HB2  . ASP   B 1 145 ? 27.910 -27.109 -3.830  1.00 20.64 ?  145 ASP   B HB2  1 
ATOM   6096 H  HB3  . ASP   B 1 145 ? 26.454 -26.582 -4.188  1.00 20.64 ?  145 ASP   B HB3  1 
ATOM   6097 N  N    . THR   B 1 146 ? 29.064 -24.041 -4.971  1.00 13.59 ?  146 THR   B N    1 
ATOM   6098 C  CA   . THR   B 1 146 ? 29.198 -22.715 -4.370  1.00 13.17 ?  146 THR   B CA   1 
ATOM   6099 C  C    . THR   B 1 146 ? 29.826 -21.685 -5.292  1.00 13.03 ?  146 THR   B C    1 
ATOM   6100 O  O    . THR   B 1 146 ? 29.368 -20.524 -5.339  1.00 13.23 ?  146 THR   B O    1 
ATOM   6101 C  CB   . THR   B 1 146 ? 30.026 -22.815 -3.081  1.00 13.61 ?  146 THR   B CB   1 
ATOM   6102 O  OG1  . THR   B 1 146 ? 29.448 -23.801 -2.218  1.00 13.97 ?  146 THR   B OG1  1 
ATOM   6103 C  CG2  . THR   B 1 146 ? 30.102 -21.473 -2.372  1.00 14.04 ?  146 THR   B CG2  1 
ATOM   6104 H  H    . THR   B 1 146 ? 29.810 -24.371 -5.249  1.00 16.29 ?  146 THR   B H    1 
ATOM   6105 H  HA   . THR   B 1 146 ? 28.324 -22.386 -4.131  1.00 15.78 ?  146 THR   B HA   1 
ATOM   6106 H  HB   . THR   B 1 146 ? 30.934 -23.079 -3.306  1.00 16.31 ?  146 THR   B HB   1 
ATOM   6107 H  HG1  . THR   B 1 146 ? 29.483 -24.557 -2.595  1.00 16.74 ?  146 THR   B HG1  1 
ATOM   6108 H  HG21 . THR   B 1 146 ? 30.445 -21.594 -1.475  1.00 16.82 ?  146 THR   B HG21 1 
ATOM   6109 H  HG22 . THR   B 1 146 ? 30.695 -20.874 -2.857  1.00 16.82 ?  146 THR   B HG22 1 
ATOM   6110 H  HG23 . THR   B 1 146 ? 29.221 -21.076 -2.325  1.00 16.82 ?  146 THR   B HG23 1 
ATOM   6111 N  N    . VAL   B 1 147 ? 30.890 -22.060 -5.995  1.00 12.71 ?  147 VAL   B N    1 
ATOM   6112 C  CA   . VAL   B 1 147 ? 31.614 -21.117 -6.834  1.00 12.52 ?  147 VAL   B CA   1 
ATOM   6113 C  C    . VAL   B 1 147 ? 30.881 -20.985 -8.157  1.00 12.48 ?  147 VAL   B C    1 
ATOM   6114 O  O    . VAL   B 1 147 ? 30.516 -21.989 -8.786  1.00 13.49 ?  147 VAL   B O    1 
ATOM   6115 C  CB   . VAL   B 1 147 ? 33.067 -21.573 -7.039  1.00 12.60 ?  147 VAL   B CB   1 
ATOM   6116 C  CG1  . VAL   B 1 147 ? 33.823 -20.543 -7.852  1.00 12.64 ?  147 VAL   B CG1  1 
ATOM   6117 C  CG2  . VAL   B 1 147 ? 33.745 -21.787 -5.698  1.00 12.73 ?  147 VAL   B CG2  1 
ATOM   6118 H  H    . VAL   B 1 147 ? 31.213 -22.862 -6.015  1.00 15.23 ?  147 VAL   B H    1 
ATOM   6119 H  HA   . VAL   B 1 147 ? 31.632 -20.249 -6.404  1.00 15.01 ?  147 VAL   B HA   1 
ATOM   6120 H  HB   . VAL   B 1 147 ? 33.079 -22.416 -7.527  1.00 15.10 ?  147 VAL   B HB   1 
ATOM   6121 H  HG11 . VAL   B 1 147 ? 34.768 -20.756 -7.836  1.00 15.15 ?  147 VAL   B HG11 1 
ATOM   6122 H  HG12 . VAL   B 1 147 ? 33.496 -20.551 -8.764  1.00 15.15 ?  147 VAL   B HG12 1 
ATOM   6123 H  HG13 . VAL   B 1 147 ? 33.677 -19.666 -7.457  1.00 15.15 ?  147 VAL   B HG13 1 
ATOM   6124 H  HG21 . VAL   B 1 147 ? 34.685 -21.978 -5.844  1.00 15.26 ?  147 VAL   B HG21 1 
ATOM   6125 H  HG22 . VAL   B 1 147 ? 33.650 -20.980 -5.168  1.00 15.26 ?  147 VAL   B HG22 1 
ATOM   6126 H  HG23 . VAL   B 1 147 ? 33.323 -22.533 -5.244  1.00 15.26 ?  147 VAL   B HG23 1 
ATOM   6127 N  N    . ARG   B 1 148 ? 30.668 -19.738 -8.578  1.00 12.56 ?  148 ARG   B N    1 
ATOM   6128 C  CA   . ARG   B 1 148 ? 30.046 -19.419 -9.852  1.00 12.53 ?  148 ARG   B CA   1 
ATOM   6129 C  C    . ARG   B 1 148 ? 31.001 -18.744 -10.824 1.00 12.82 ?  148 ARG   B C    1 
ATOM   6130 O  O    . ARG   B 1 148 ? 30.715 -18.712 -12.024 1.00 14.27 ?  148 ARG   B O    1 
ATOM   6131 C  CB   . ARG   B 1 148 ? 28.811 -18.531 -9.635  1.00 13.01 ?  148 ARG   B CB   1 
ATOM   6132 C  CG   . ARG   B 1 148 ? 27.735 -19.241 -8.829  1.00 14.10 ?  148 ARG   B CG   1 
ATOM   6133 C  CD   . ARG   B 1 148 ? 26.531 -18.353 -8.515  1.00 15.04 ?  148 ARG   B CD   1 
ATOM   6134 N  NE   . ARG   B 1 148 ? 26.917 -17.153 -7.783  1.00 14.93 ?  148 ARG   B NE   1 
ATOM   6135 C  CZ   . ARG   B 1 148 ? 27.215 -17.120 -6.491  1.00 13.93 ?  148 ARG   B CZ   1 
ATOM   6136 N  NH1  . ARG   B 1 148 ? 27.153 -18.208 -5.737  1.00 14.34 ?  148 ARG   B NH1  1 
ATOM   6137 N  NH2  . ARG   B 1 148 ? 27.611 -15.972 -5.945  1.00 13.94 ?  148 ARG   B NH2  1 
ATOM   6138 H  H    . ARG   B 1 148 ? 30.887 -19.036 -8.121  1.00 15.05 ?  148 ARG   B H    1 
ATOM   6139 H  HA   . ARG   B 1 148 ? 29.743 -20.242 -10.260 1.00 15.02 ?  148 ARG   B HA   1 
ATOM   6140 H  HB2  . ARG   B 1 148 ? 29.071 -17.731 -9.149  1.00 15.59 ?  148 ARG   B HB2  1 
ATOM   6141 H  HB3  . ARG   B 1 148 ? 28.435 -18.289 -10.496 1.00 15.59 ?  148 ARG   B HB3  1 
ATOM   6142 H  HG2  . ARG   B 1 148 ? 27.414 -20.005 -9.339  1.00 16.89 ?  148 ARG   B HG2  1 
ATOM   6143 H  HG3  . ARG   B 1 148 ? 28.112 -19.540 -7.990  1.00 16.89 ?  148 ARG   B HG3  1 
ATOM   6144 H  HD2  . ARG   B 1 148 ? 26.112 -18.079 -9.345  1.00 18.02 ?  148 ARG   B HD2  1 
ATOM   6145 H  HD3  . ARG   B 1 148 ? 25.900 -18.852 -7.971  1.00 18.02 ?  148 ARG   B HD3  1 
ATOM   6146 H  HE   . ARG   B 1 148 ? 26.963 -16.417 -8.221  1.00 17.89 ?  148 ARG   B HE   1 
ATOM   6147 H  HH11 . ARG   B 1 148 ? 26.896 -18.958 -6.074  1.00 17.19 ?  148 ARG   B HH11 1 
ATOM   6148 H  HH12 . ARG   B 1 148 ? 27.347 -18.164 -4.899  1.00 17.19 ?  148 ARG   B HH12 1 
ATOM   6149 H  HH21 . ARG   B 1 148 ? 27.666 -15.265 -6.429  1.00 16.71 ?  148 ARG   B HH21 1 
ATOM   6150 H  HH22 . ARG   B 1 148 ? 27.812 -15.940 -5.110  1.00 16.71 ?  148 ARG   B HH22 1 
ATOM   6151 N  N    . THR   B 1 149 ? 32.107 -18.194 -10.336 1.00 12.74 ?  149 THR   B N    1 
ATOM   6152 C  CA   . THR   B 1 149 ? 33.145 -17.632 -11.185 1.00 12.90 ?  149 THR   B CA   1 
ATOM   6153 C  C    . THR   B 1 149 ? 34.031 -18.770 -11.692 1.00 12.63 ?  149 THR   B C    1 
ATOM   6154 O  O    . THR   B 1 149 ? 33.840 -19.939 -11.349 1.00 13.02 ?  149 THR   B O    1 
ATOM   6155 C  CB   . THR   B 1 149 ? 33.916 -16.579 -10.400 1.00 12.88 ?  149 THR   B CB   1 
ATOM   6156 O  OG1  . THR   B 1 149 ? 34.376 -17.175 -9.185  1.00 12.96 ?  149 THR   B OG1  1 
ATOM   6157 C  CG2  . THR   B 1 149 ? 33.022 -15.377 -10.096 1.00 13.61 ?  149 THR   B CG2  1 
ATOM   6158 H  H    . THR   B 1 149 ? 32.273 -18.129 -9.499  1.00 15.27 ?  149 THR   B H    1 
ATOM   6159 H  HA   . THR   B 1 149 ? 32.734 -17.197 -11.950 1.00 15.46 ?  149 THR   B HA   1 
ATOM   6160 H  HB   . THR   B 1 149 ? 34.675 -16.281 -10.918 1.00 15.44 ?  149 THR   B HB   1 
ATOM   6161 H  HG1  . THR   B 1 149 ? 34.796 -16.603 -8.725  1.00 15.53 ?  149 THR   B HG1  1 
ATOM   6162 H  HG21 . THR   B 1 149 ? 33.526 -14.704 -9.609  1.00 16.31 ?  149 THR   B HG21 1 
ATOM   6163 H  HG22 . THR   B 1 149 ? 32.699 -14.986 -10.924 1.00 16.31 ?  149 THR   B HG22 1 
ATOM   6164 H  HG23 . THR   B 1 149 ? 32.262 -15.649 -9.559  1.00 16.31 ?  149 THR   B HG23 1 
ATOM   6165 N  N    . ASN   B 1 150 ? 34.994 -18.446 -12.542 1.00 12.62 ?  150 ASN   B N    1 
ATOM   6166 C  CA   . ASN   B 1 150 ? 35.765 -19.469 -13.241 1.00 12.97 ?  150 ASN   B CA   1 
ATOM   6167 C  C    . ASN   B 1 150 ? 36.929 -19.919 -12.365 1.00 12.51 ?  150 ASN   B C    1 
ATOM   6168 O  O    . ASN   B 1 150 ? 37.865 -19.152 -12.114 1.00 13.00 ?  150 ASN   B O    1 
ATOM   6169 C  CB   . ASN   B 1 150 ? 36.236 -18.932 -14.585 1.00 14.69 ?  150 ASN   B CB   1 
ATOM   6170 C  CG   . ASN   B 1 150 ? 35.092 -18.719 -15.537 1.00 17.49 ?  150 ASN   B CG   1 
ATOM   6171 O  OD1  . ASN   B 1 150 ? 34.197 -19.552 -15.628 1.00 18.43 ?  150 ASN   B OD1  1 
ATOM   6172 N  ND2  . ASN   B 1 150 ? 35.090 -17.591 -16.230 1.00 19.17 ?  150 ASN   B ND2  1 
ATOM   6173 H  H    . ASN   B 1 150 ? 35.230 -17.638 -12.726 1.00 15.12 ?  150 ASN   B H    1 
ATOM   6174 H  HA   . ASN   B 1 150 ? 35.190 -20.235 -13.408 1.00 15.55 ?  150 ASN   B HA   1 
ATOM   6175 H  HB2  . ASN   B 1 150 ? 36.678 -18.076 -14.446 1.00 17.61 ?  150 ASN   B HB2  1 
ATOM   6176 H  HB3  . ASN   B 1 150 ? 36.847 -19.563 -14.985 1.00 17.61 ?  150 ASN   B HB3  1 
ATOM   6177 H  HD21 . ASN   B 1 150 ? 34.454 -17.423 -16.787 1.00 22.98 ?  150 ASN   B HD21 1 
ATOM   6178 H  HD22 . ASN   B 1 150 ? 35.733 -17.024 -16.136 1.00 22.98 ?  150 ASN   B HD22 1 
ATOM   6179 N  N    . VAL   B 1 151 ? 36.880 -21.165 -11.905 1.00 12.30 ?  151 VAL   B N    1 
ATOM   6180 C  CA   . VAL   B 1 151 ? 37.897 -21.699 -11.014 1.00 12.36 ?  151 VAL   B CA   1 
ATOM   6181 C  C    . VAL   B 1 151 ? 38.601 -22.866 -11.695 1.00 12.18 ?  151 VAL   B C    1 
ATOM   6182 O  O    . VAL   B 1 151 ? 37.959 -23.798 -12.199 1.00 13.29 ?  151 VAL   B O    1 
ATOM   6183 C  CB   . VAL   B 1 151 ? 37.340 -22.042 -9.617  1.00 13.45 ?  151 VAL   B CB   1 
ATOM   6184 C  CG1  . VAL   B 1 151 ? 36.175 -23.035 -9.698  1.00 14.30 ?  151 VAL   B CG1  1 
ATOM   6185 C  CG2  . VAL   B 1 151 ? 38.452 -22.539 -8.706  1.00 13.84 ?  151 VAL   B CG2  1 
ATOM   6186 H  H    . VAL   B 1 151 ? 36.251 -21.727 -12.100 1.00 14.74 ?  151 VAL   B H    1 
ATOM   6187 H  HA   . VAL   B 1 151 ? 38.562 -21.006 -10.881 1.00 14.80 ?  151 VAL   B HA   1 
ATOM   6188 H  HB   . VAL   B 1 151 ? 36.988 -21.225 -9.223  1.00 16.12 ?  151 VAL   B HB   1 
ATOM   6189 H  HG11 . VAL   B 1 151 ? 35.855 -23.226 -8.800  1.00 17.14 ?  151 VAL   B HG11 1 
ATOM   6190 H  HG12 . VAL   B 1 151 ? 35.457 -22.648 -10.226 1.00 17.14 ?  151 VAL   B HG12 1 
ATOM   6191 H  HG13 . VAL   B 1 151 ? 36.484 -23.855 -10.116 1.00 17.14 ?  151 VAL   B HG13 1 
ATOM   6192 H  HG21 . VAL   B 1 151 ? 38.106 -22.615 -7.802  1.00 16.58 ?  151 VAL   B HG21 1 
ATOM   6193 H  HG22 . VAL   B 1 151 ? 38.754 -23.405 -9.018  1.00 16.58 ?  151 VAL   B HG22 1 
ATOM   6194 H  HG23 . VAL   B 1 151 ? 39.184 -21.903 -8.725  1.00 16.58 ?  151 VAL   B HG23 1 
ATOM   6195 N  N    . TYR   B 1 152 ? 39.930 -22.779 -11.720 1.00 11.58 ?  152 TYR   B N    1 
ATOM   6196 C  CA   . TYR   B 1 152 ? 40.834 -23.764 -12.297 1.00 11.57 ?  152 TYR   B CA   1 
ATOM   6197 C  C    . TYR   B 1 152 ? 41.555 -24.440 -11.134 1.00 11.30 ?  152 TYR   B C    1 
ATOM   6198 O  O    . TYR   B 1 152 ? 42.411 -23.824 -10.488 1.00 11.98 ?  152 TYR   B O    1 
ATOM   6199 C  CB   . TYR   B 1 152 ? 41.808 -23.059 -13.244 1.00 12.41 ?  152 TYR   B CB   1 
ATOM   6200 C  CG   . TYR   B 1 152 ? 41.130 -22.588 -14.508 1.00 13.10 ?  152 TYR   B CG   1 
ATOM   6201 C  CD1  . TYR   B 1 152 ? 40.471 -21.364 -14.570 1.00 13.81 ?  152 TYR   B CD1  1 
ATOM   6202 C  CD2  . TYR   B 1 152 ? 41.110 -23.397 -15.632 1.00 14.59 ?  152 TYR   B CD2  1 
ATOM   6203 C  CE1  . TYR   B 1 152 ? 39.827 -20.960 -15.727 1.00 15.14 ?  152 TYR   B CE1  1 
ATOM   6204 C  CE2  . TYR   B 1 152 ? 40.472 -23.006 -16.788 1.00 15.46 ?  152 TYR   B CE2  1 
ATOM   6205 C  CZ   . TYR   B 1 152 ? 39.835 -21.784 -16.835 1.00 15.77 ?  152 TYR   B CZ   1 
ATOM   6206 O  OH   . TYR   B 1 152 ? 39.204 -21.410 -17.998 1.00 18.18 ?  152 TYR   B OH   1 
ATOM   6207 H  H    . TYR   B 1 152 ? 40.362 -22.114 -11.373 1.00 13.88 ?  152 TYR   B H    1 
ATOM   6208 H  HA   . TYR   B 1 152 ? 40.328 -24.431 -12.791 1.00 13.86 ?  152 TYR   B HA   1 
ATOM   6209 H  HB2  . TYR   B 1 152 ? 42.180 -22.285 -12.791 1.00 14.87 ?  152 TYR   B HB2  1 
ATOM   6210 H  HB3  . TYR   B 1 152 ? 42.516 -23.673 -13.489 1.00 14.87 ?  152 TYR   B HB3  1 
ATOM   6211 H  HD1  . TYR   B 1 152 ? 40.463 -20.806 -13.823 1.00 16.55 ?  152 TYR   B HD1  1 
ATOM   6212 H  HD2  . TYR   B 1 152 ? 41.532 -24.225 -15.605 1.00 17.49 ?  152 TYR   B HD2  1 
ATOM   6213 H  HE1  . TYR   B 1 152 ? 39.397 -20.136 -15.762 1.00 18.14 ?  152 TYR   B HE1  1 
ATOM   6214 H  HE2  . TYR   B 1 152 ? 40.475 -23.563 -17.535 1.00 18.53 ?  152 TYR   B HE2  1 
ATOM   6215 H  HH   . TYR   B 1 152 ? 38.853 -20.652 -17.901 1.00 21.79 ?  152 TYR   B HH   1 
ATOM   6216 N  N    . LEU   B 1 153 ? 41.185 -25.695 -10.858 1.00 11.64 ?  153 LEU   B N    1 
ATOM   6217 C  CA   . LEU   B 1 153 ? 41.697 -26.439 -9.719  1.00 11.47 ?  153 LEU   B CA   1 
ATOM   6218 C  C    . LEU   B 1 153 ? 42.928 -27.238 -10.119 1.00 11.82 ?  153 LEU   B C    1 
ATOM   6219 O  O    . LEU   B 1 153 ? 42.907 -27.969 -11.114 1.00 13.03 ?  153 LEU   B O    1 
ATOM   6220 C  CB   . LEU   B 1 153 ? 40.622 -27.399 -9.199  1.00 11.94 ?  153 LEU   B CB   1 
ATOM   6221 C  CG   . LEU   B 1 153 ? 39.363 -26.741 -8.631  1.00 13.03 ?  153 LEU   B CG   1 
ATOM   6222 C  CD1  . LEU   B 1 153 ? 38.259 -27.777 -8.458  1.00 13.77 ?  153 LEU   B CD1  1 
ATOM   6223 C  CD2  . LEU   B 1 153 ? 39.663 -26.057 -7.303  1.00 13.36 ?  153 LEU   B CD2  1 
ATOM   6224 H  H    . LEU   B 1 153 ? 40.610 -26.140 -11.328 1.00 13.95 ?  153 LEU   B H    1 
ATOM   6225 H  HA   . LEU   B 1 153 ? 41.927 -25.824 -9.009  1.00 13.74 ?  153 LEU   B HA   1 
ATOM   6226 H  HB2  . LEU   B 1 153 ? 40.342 -27.974 -9.926  1.00 14.30 ?  153 LEU   B HB2  1 
ATOM   6227 H  HB3  . LEU   B 1 153 ? 41.008 -27.938 -8.489  1.00 14.30 ?  153 LEU   B HB3  1 
ATOM   6228 H  HG   . LEU   B 1 153 ? 39.045 -26.063 -9.252  1.00 15.61 ?  153 LEU   B HG   1 
ATOM   6229 H  HD11 . LEU   B 1 153 ? 37.450 -27.324 -8.165  1.00 16.50 ?  153 LEU   B HD11 1 
ATOM   6230 H  HD12 . LEU   B 1 153 ? 38.107 -28.212 -9.306  1.00 16.50 ?  153 LEU   B HD12 1 
ATOM   6231 H  HD13 . LEU   B 1 153 ? 38.539 -28.419 -7.791  1.00 16.50 ?  153 LEU   B HD13 1 
ATOM   6232 H  HD21 . LEU   B 1 153 ? 38.844 -25.686 -6.940  1.00 16.01 ?  153 LEU   B HD21 1 
ATOM   6233 H  HD22 . LEU   B 1 153 ? 40.033 -26.709 -6.688  1.00 16.01 ?  153 LEU   B HD22 1 
ATOM   6234 H  HD23 . LEU   B 1 153 ? 40.308 -25.344 -7.453  1.00 16.01 ?  153 LEU   B HD23 1 
ATOM   6235 N  N    . ALA   B 1 154 ? 43.985 -27.123 -9.324  1.00 11.97 ?  154 ALA   B N    1 
ATOM   6236 C  CA   . ALA   B 1 154 ? 45.209 -27.893 -9.507  1.00 13.35 ?  154 ALA   B CA   1 
ATOM   6237 C  C    . ALA   B 1 154 ? 45.276 -28.968 -8.428  1.00 13.66 ?  154 ALA   B C    1 
ATOM   6238 O  O    . ALA   B 1 154 ? 45.208 -28.665 -7.230  1.00 14.93 ?  154 ALA   B O    1 
ATOM   6239 C  CB   . ALA   B 1 154 ? 46.437 -26.984 -9.455  1.00 14.21 ?  154 ALA   B CB   1 
ATOM   6240 H  H    . ALA   B 1 154 ? 44.016 -26.584 -8.651  1.00 14.34 ?  154 ALA   B H    1 
ATOM   6241 H  HA   . ALA   B 1 154 ? 45.194 -28.324 -10.373 1.00 16.00 ?  154 ALA   B HA   1 
ATOM   6242 H  HB1  . ALA   B 1 154 ? 47.239 -27.517 -9.580  1.00 17.03 ?  154 ALA   B HB1  1 
ATOM   6243 H  HB2  . ALA   B 1 154 ? 46.375 -26.318 -10.163 1.00 17.03 ?  154 ALA   B HB2  1 
ATOM   6244 H  HB3  . ALA   B 1 154 ? 46.472 -26.537 -8.593  1.00 17.03 ?  154 ALA   B HB3  1 
ATOM   6245 N  N    . VAL   B 1 155 ? 45.385 -30.219 -8.858  1.00 13.18 ?  155 VAL   B N    1 
ATOM   6246 C  CA   . VAL   B 1 155 ? 45.496 -31.364 -7.963  1.00 13.31 ?  155 VAL   B CA   1 
ATOM   6247 C  C    . VAL   B 1 155 ? 46.836 -32.035 -8.243  1.00 13.18 ?  155 VAL   B C    1 
ATOM   6248 O  O    . VAL   B 1 155 ? 47.071 -32.529 -9.354  1.00 15.12 ?  155 VAL   B O    1 
ATOM   6249 C  CB   . VAL   B 1 155 ? 44.340 -32.357 -8.158  1.00 14.89 ?  155 VAL   B CB   1 
ATOM   6250 C  CG1  . VAL   B 1 155 ? 44.524 -33.560 -7.251  1.00 14.82 ?  155 VAL   B CG1  1 
ATOM   6251 C  CG2  . VAL   B 1 155 ? 43.008 -31.668 -7.893  1.00 15.39 ?  155 VAL   B CG2  1 
ATOM   6252 H  H    . VAL   B 1 155 ? 45.410 -30.436 -9.691  1.00 15.79 ?  155 VAL   B H    1 
ATOM   6253 H  HA   . VAL   B 1 155 ? 45.488 -31.060 -7.042  1.00 15.95 ?  155 VAL   B HA   1 
ATOM   6254 H  HB   . VAL   B 1 155 ? 44.337 -32.662 -9.079  1.00 17.85 ?  155 VAL   B HB   1 
ATOM   6255 H  HG11 . VAL   B 1 155 ? 43.694 -34.066 -7.222  1.00 17.76 ?  155 VAL   B HG11 1 
ATOM   6256 H  HG12 . VAL   B 1 155 ? 45.234 -34.122 -7.604  1.00 17.76 ?  155 VAL   B HG12 1 
ATOM   6257 H  HG13 . VAL   B 1 155 ? 44.754 -33.257 -6.359  1.00 17.76 ?  155 VAL   B HG13 1 
ATOM   6258 H  HG21 . VAL   B 1 155 ? 42.294 -32.321 -7.976  1.00 18.45 ?  155 VAL   B HG21 1 
ATOM   6259 H  HG22 . VAL   B 1 155 ? 43.016 -31.302 -6.994  1.00 18.45 ?  155 VAL   B HG22 1 
ATOM   6260 H  HG23 . VAL   B 1 155 ? 42.882 -30.956 -8.538  1.00 18.45 ?  155 VAL   B HG23 1 
ATOM   6261 N  N    . PHE   B 1 156 ? 47.703 -32.076 -7.231  1.00 13.72 ?  156 PHE   B N    1 
ATOM   6262 C  CA   . PHE   B 1 156 ? 49.080 -32.528 -7.438  1.00 15.19 ?  156 PHE   B CA   1 
ATOM   6263 C  C    . PHE   B 1 156 ? 49.175 -34.028 -7.719  1.00 16.26 ?  156 PHE   B C    1 
ATOM   6264 O  O    . PHE   B 1 156 ? 49.890 -34.454 -8.636  1.00 18.25 ?  156 PHE   B O    1 
ATOM   6265 C  CB   . PHE   B 1 156 ? 49.917 -32.156 -6.218  1.00 14.98 ?  156 PHE   B CB   1 
ATOM   6266 C  CG   . PHE   B 1 156 ? 51.336 -32.622 -6.285  1.00 15.45 ?  156 PHE   B CG   1 
ATOM   6267 C  CD1  . PHE   B 1 156 ? 52.213 -32.083 -7.204  1.00 16.97 ?  156 PHE   B CD1  1 
ATOM   6268 C  CD2  . PHE   B 1 156 ? 51.801 -33.578 -5.404  1.00 15.76 ?  156 PHE   B CD2  1 
ATOM   6269 C  CE1  . PHE   B 1 156 ? 53.531 -32.495 -7.254  1.00 17.57 ?  156 PHE   B CE1  1 
ATOM   6270 C  CE2  . PHE   B 1 156 ? 53.118 -33.994 -5.452  1.00 17.06 ?  156 PHE   B CE2  1 
ATOM   6271 C  CZ   . PHE   B 1 156 ? 53.974 -33.454 -6.383  1.00 17.53 ?  156 PHE   B CZ   1 
ATOM   6272 H  H    . PHE   B 1 156 ? 47.517 -31.864 -6.420  1.00 16.44 ?  156 PHE   B H    1 
ATOM   6273 H  HA   . PHE   B 1 156 ? 49.444 -32.063 -8.203  1.00 18.20 ?  156 PHE   B HA   1 
ATOM   6274 H  HB2  . PHE   B 1 156 ? 49.928 -31.189 -6.136  1.00 17.95 ?  156 PHE   B HB2  1 
ATOM   6275 H  HB3  . PHE   B 1 156 ? 49.515 -32.547 -5.428  1.00 17.95 ?  156 PHE   B HB3  1 
ATOM   6276 H  HD1  . PHE   B 1 156 ? 51.918 -31.427 -7.797  1.00 20.34 ?  156 PHE   B HD1  1 
ATOM   6277 H  HD2  . PHE   B 1 156 ? 51.216 -33.949 -4.778  1.00 18.89 ?  156 PHE   B HD2  1 
ATOM   6278 H  HE1  . PHE   B 1 156 ? 54.114 -32.126 -7.882  1.00 21.07 ?  156 PHE   B HE1  1 
ATOM   6279 H  HE2  . PHE   B 1 156 ? 53.417 -34.651 -4.861  1.00 20.44 ?  156 PHE   B HE2  1 
ATOM   6280 H  HZ   . PHE   B 1 156 ? 54.861 -33.737 -6.415  1.00 21.01 ?  156 PHE   B HZ   1 
ATOM   6281 N  N    . ASP   B 1 157 ? 48.509 -34.846 -6.915  1.00 16.55 ?  157 ASP   B N    1 
ATOM   6282 C  CA   . ASP   B 1 157 ? 48.654 -36.294 -7.007  1.00 17.85 ?  157 ASP   B CA   1 
ATOM   6283 C  C    . ASP   B 1 157 ? 47.745 -36.844 -8.100  1.00 18.01 ?  157 ASP   B C    1 
ATOM   6284 O  O    . ASP   B 1 157 ? 46.519 -36.721 -8.009  1.00 17.23 ?  157 ASP   B O    1 
ATOM   6285 C  CB   . ASP   B 1 157 ? 48.281 -36.907 -5.663  1.00 19.48 ?  157 ASP   B CB   1 
ATOM   6286 C  CG   . ASP   B 1 157 ? 48.426 -38.412 -5.646  1.00 21.15 ?  157 ASP   B CG   1 
ATOM   6287 O  OD1  . ASP   B 1 157 ? 48.761 -39.008 -6.697  1.00 21.50 ?  157 ASP   B OD1  1 
ATOM   6288 O  OD2  . ASP   B 1 157 ? 48.224 -38.995 -4.564  1.00 22.93 -1 157 ASP   B OD2  1 
ATOM   6289 H  H    . ASP   B 1 157 ? 47.970 -34.592 -6.300  1.00 19.84 ?  157 ASP   B H    1 
ATOM   6290 H  HA   . ASP   B 1 157 ? 49.573 -36.531 -7.213  1.00 21.40 ?  157 ASP   B HA   1 
ATOM   6291 H  HB2  . ASP   B 1 157 ? 48.848 -36.530 -4.975  1.00 23.36 ?  157 ASP   B HB2  1 
ATOM   6292 H  HB3  . ASP   B 1 157 ? 47.350 -36.701 -5.469  1.00 23.36 ?  157 ASP   B HB3  1 
ATOM   6293 N  N    A LYS   B 1 158 ? 48.344 -37.464 -9.123  0.72 18.77 ?  158 LYS   B N    1 
ATOM   6294 N  N    B LYS   B 1 158 ? 48.345 -37.479 -9.112  0.28 18.43 ?  158 LYS   B N    1 
ATOM   6295 C  CA   A LYS   B 1 158 ? 47.573 -38.075 -10.207 0.72 19.86 ?  158 LYS   B CA   1 
ATOM   6296 C  CA   B LYS   B 1 158 ? 47.572 -38.068 -10.203 0.28 19.12 ?  158 LYS   B CA   1 
ATOM   6297 C  C    A LYS   B 1 158 ? 46.508 -39.034 -9.679  0.72 19.56 ?  158 LYS   B C    1 
ATOM   6298 C  C    B LYS   B 1 158 ? 46.512 -39.038 -9.686  0.28 19.07 ?  158 LYS   B C    1 
ATOM   6299 O  O    A LYS   B 1 158 ? 45.399 -39.108 -10.224 0.72 19.65 ?  158 LYS   B O    1 
ATOM   6300 O  O    B LYS   B 1 158 ? 45.409 -39.116 -10.239 0.28 18.82 ?  158 LYS   B O    1 
ATOM   6301 C  CB   A LYS   B 1 158 ? 48.524 -38.796 -11.173 0.72 21.58 ?  158 LYS   B CB   1 
ATOM   6302 C  CB   B LYS   B 1 158 ? 48.521 -38.766 -11.185 0.28 20.17 ?  158 LYS   B CB   1 
ATOM   6303 C  CG   A LYS   B 1 158 ? 47.850 -39.717 -12.184 0.72 23.66 ?  158 LYS   B CG   1 
ATOM   6304 C  CG   B LYS   B 1 158 ? 47.847 -39.654 -12.226 0.28 21.46 ?  158 LYS   B CG   1 
ATOM   6305 C  CD   A LYS   B 1 158 ? 46.966 -38.959 -13.155 0.72 25.43 ?  158 LYS   B CD   1 
ATOM   6306 C  CD   B LYS   B 1 158 ? 46.951 -38.862 -13.163 0.28 22.68 ?  158 LYS   B CD   1 
ATOM   6307 C  CE   A LYS   B 1 158 ? 46.380 -39.896 -14.201 0.72 26.87 ?  158 LYS   B CE   1 
ATOM   6308 C  CE   B LYS   B 1 158 ? 46.376 -39.758 -14.251 0.28 23.68 ?  158 LYS   B CE   1 
ATOM   6309 N  NZ   A LYS   B 1 158 ? 45.296 -39.249 -14.993 0.72 27.25 ?  158 LYS   B NZ   1 
ATOM   6310 N  NZ   B LYS   B 1 158 ? 45.362 -39.056 -15.085 0.28 24.10 ?  158 LYS   B NZ   1 
ATOM   6311 H  H    A LYS   B 1 158 ? 49.198 -37.551 -9.206  0.72 22.51 ?  158 LYS   B H    1 
ATOM   6312 H  H    B LYS   B 1 158 ? 49.197 -37.586 -9.185  0.28 22.09 ?  158 LYS   B H    1 
ATOM   6313 H  HA   A LYS   B 1 158 ? 47.127 -37.375 -10.705 0.72 23.81 ?  158 LYS   B HA   1 
ATOM   6314 H  HA   B LYS   B 1 158 ? 47.120 -37.359 -10.687 0.28 22.92 ?  158 LYS   B HA   1 
ATOM   6315 H  HB2  A LYS   B 1 158 ? 49.020 -38.127 -11.678 0.72 25.87 ?  158 LYS   B HB2  1 
ATOM   6316 H  HB2  B LYS   B 1 158 ? 49.023 -38.086 -11.668 0.28 24.18 ?  158 LYS   B HB2  1 
ATOM   6317 H  HB3  A LYS   B 1 158 ? 49.145 -39.332 -10.657 0.72 25.87 ?  158 LYS   B HB3  1 
ATOM   6318 H  HB3  B LYS   B 1 158 ? 49.136 -39.321 -10.681 0.28 24.18 ?  158 LYS   B HB3  1 
ATOM   6319 H  HG2  A LYS   B 1 158 ? 48.538 -40.167 -12.699 0.72 28.37 ?  158 LYS   B HG2  1 
ATOM   6320 H  HG2  B LYS   B 1 158 ? 48.533 -40.082 -12.762 0.28 25.74 ?  158 LYS   B HG2  1 
ATOM   6321 H  HG3  A LYS   B 1 158 ? 47.308 -40.377 -11.723 0.72 28.37 ?  158 LYS   B HG3  1 
ATOM   6322 H  HG3  B LYS   B 1 158 ? 47.309 -40.331 -11.785 0.28 25.74 ?  158 LYS   B HG3  1 
ATOM   6323 H  HD2  A LYS   B 1 158 ? 46.235 -38.544 -12.671 0.72 30.50 ?  158 LYS   B HD2  1 
ATOM   6324 H  HD2  B LYS   B 1 158 ? 46.215 -38.480 -12.661 0.28 27.20 ?  158 LYS   B HD2  1 
ATOM   6325 H  HD3  A LYS   B 1 158 ? 47.494 -38.284 -13.612 0.72 30.50 ?  158 LYS   B HD3  1 
ATOM   6326 H  HD3  B LYS   B 1 158 ? 47.470 -38.161 -13.589 0.28 27.20 ?  158 LYS   B HD3  1 
ATOM   6327 H  HE2  A LYS   B 1 158 ? 47.080 -40.165 -14.815 0.72 32.22 ?  158 LYS   B HE2  1 
ATOM   6328 H  HE2  B LYS   B 1 158 ? 47.094 -40.053 -14.833 0.28 28.40 ?  158 LYS   B HE2  1 
ATOM   6329 H  HE3  A LYS   B 1 158 ? 46.008 -40.675 -13.759 0.72 32.22 ?  158 LYS   B HE3  1 
ATOM   6330 H  HE3  B LYS   B 1 158 ? 45.949 -40.526 -13.838 0.28 28.40 ?  158 LYS   B HE3  1 
ATOM   6331 H  HZ1  A LYS   B 1 158 ? 44.973 -39.821 -15.594 0.72 32.68 ?  158 LYS   B HZ1  1 
ATOM   6332 H  HZ1  B LYS   B 1 158 ? 45.047 -39.608 -15.709 0.28 28.90 ?  158 LYS   B HZ1  1 
ATOM   6333 H  HZ2  A LYS   B 1 158 ? 44.635 -38.994 -14.453 0.72 32.68 ?  158 LYS   B HZ2  1 
ATOM   6334 H  HZ2  B LYS   B 1 158 ? 44.687 -38.781 -14.575 0.28 28.90 ?  158 LYS   B HZ2  1 
ATOM   6335 H  HZ3  A LYS   B 1 158 ? 45.614 -38.533 -15.417 0.72 32.68 ?  158 LYS   B HZ3  1 
ATOM   6336 H  HZ3  B LYS   B 1 158 ? 45.731 -38.351 -15.482 0.28 28.90 ?  158 LYS   B HZ3  1 
ATOM   6337 N  N    . ASN   B 1 159 ? 46.829 -39.794 -8.631  1.00 19.64 ?  159 ASN   B N    1 
ATOM   6338 C  CA   . ASN   B 1 159 ? 45.871 -40.772 -8.119  1.00 20.45 ?  159 ASN   B CA   1 
ATOM   6339 C  C    . ASN   B 1 159 ? 44.674 -40.095 -7.446  1.00 19.55 ?  159 ASN   B C    1 
ATOM   6340 O  O    . ASN   B 1 159 ? 43.540 -40.585 -7.546  1.00 19.97 ?  159 ASN   B O    1 
ATOM   6341 C  CB   . ASN   B 1 159 ? 46.575 -41.754 -7.185  1.00 22.08 ?  159 ASN   B CB   1 
ATOM   6342 C  CG   . ASN   B 1 159 ? 47.602 -42.597 -7.908  1.00 24.09 ?  159 ASN   B CG   1 
ATOM   6343 O  OD1  . ASN   B 1 159 ? 47.358 -43.078 -9.022  1.00 24.71 ?  159 ASN   B OD1  1 
ATOM   6344 N  ND2  . ASN   B 1 159 ? 48.760 -42.784 -7.283  1.00 24.79 ?  159 ASN   B ND2  1 
ATOM   6345 H  H    A ASN   B 1 159 ? 47.577 -39.760 -8.210  0.72 23.55 ?  159 ASN   B H    1 
ATOM   6346 H  H    B ASN   B 1 159 ? 47.577 -39.759 -8.209  0.28 23.55 ?  159 ASN   B H    1 
ATOM   6347 H  HA   . ASN   B 1 159 ? 45.532 -41.283 -8.872  1.00 24.52 ?  159 ASN   B HA   1 
ATOM   6348 H  HB2  . ASN   B 1 159 ? 47.028 -41.260 -6.486  1.00 26.48 ?  159 ASN   B HB2  1 
ATOM   6349 H  HB3  . ASN   B 1 159 ? 45.918 -42.353 -6.804  1.00 26.48 ?  159 ASN   B HB3  1 
ATOM   6350 H  HD21 . ASN   B 1 159 ? 49.382 -43.257 -7.651  1.00 29.72 ?  159 ASN   B HD21 1 
ATOM   6351 H  HD22 . ASN   B 1 159 ? 48.889 -42.449 -6.501  1.00 29.72 ?  159 ASN   B HD22 1 
ATOM   6352 N  N    . LEU   B 1 160 ? 44.893 -38.966 -6.764  1.00 18.53 ?  160 LEU   B N    1 
ATOM   6353 C  CA   . LEU   B 1 160 ? 43.760 -38.230 -6.216  1.00 17.83 ?  160 LEU   B CA   1 
ATOM   6354 C  C    . LEU   B 1 160 ? 42.968 -37.562 -7.328  1.00 17.07 ?  160 LEU   B C    1 
ATOM   6355 O  O    . LEU   B 1 160 ? 41.731 -37.568 -7.306  1.00 16.70 ?  160 LEU   B O    1 
ATOM   6356 C  CB   . LEU   B 1 160 ? 44.225 -37.200 -5.189  1.00 17.30 ?  160 LEU   B CB   1 
ATOM   6357 C  CG   . LEU   B 1 160 ? 43.100 -36.299 -4.662  1.00 16.90 ?  160 LEU   B CG   1 
ATOM   6358 C  CD1  . LEU   B 1 160 ? 41.972 -37.126 -4.059  1.00 17.64 ?  160 LEU   B CD1  1 
ATOM   6359 C  CD2  . LEU   B 1 160 ? 43.633 -35.314 -3.643  1.00 16.88 ?  160 LEU   B CD2  1 
ATOM   6360 H  H    . LEU   B 1 160 ? 45.670 -38.619 -6.612  1.00 22.21 ?  160 LEU   B H    1 
ATOM   6361 H  HA   . LEU   B 1 160 ? 43.176 -38.861 -5.772  1.00 21.37 ?  160 LEU   B HA   1 
ATOM   6362 H  HB2  . LEU   B 1 160 ? 44.617 -37.674 -4.434  1.00 20.74 ?  160 LEU   B HB2  1 
ATOM   6363 H  HB3  . LEU   B 1 160 ? 44.899 -36.634 -5.600  1.00 20.74 ?  160 LEU   B HB3  1 
ATOM   6364 H  HG   . LEU   B 1 160 ? 42.731 -35.796 -5.400  1.00 20.25 ?  160 LEU   B HG   1 
ATOM   6365 H  HD11 . LEU   B 1 160 ? 41.344 -36.531 -3.625  1.00 21.15 ?  160 LEU   B HD11 1 
ATOM   6366 H  HD12 . LEU   B 1 160 ? 41.522 -37.623 -4.764  1.00 21.15 ?  160 LEU   B HD12 1 
ATOM   6367 H  HD13 . LEU   B 1 160 ? 42.343 -37.747 -3.408  1.00 21.15 ?  160 LEU   B HD13 1 
ATOM   6368 H  HD21 . LEU   B 1 160 ? 42.906 -34.742 -3.355  1.00 20.23 ?  160 LEU   B HD21 1 
ATOM   6369 H  HD22 . LEU   B 1 160 ? 43.990 -35.804 -2.886  1.00 20.23 ?  160 LEU   B HD22 1 
ATOM   6370 H  HD23 . LEU   B 1 160 ? 44.331 -34.784 -4.056  1.00 20.23 ?  160 LEU   B HD23 1 
ATOM   6371 N  N    . TYR   B 1 161 ? 43.664 -36.991 -8.316  1.00 17.13 ?  161 TYR   B N    1 
ATOM   6372 C  CA   . TYR   B 1 161 ? 42.987 -36.427 -9.479  1.00 16.89 ?  161 TYR   B CA   1 
ATOM   6373 C  C    . TYR   B 1 161 ? 42.039 -37.451 -10.096 1.00 16.76 ?  161 TYR   B C    1 
ATOM   6374 O  O    . TYR   B 1 161 ? 40.868 -37.155 -10.357 1.00 16.51 ?  161 TYR   B O    1 
ATOM   6375 C  CB   . TYR   B 1 161 ? 44.024 -35.945 -10.505 1.00 17.39 ?  161 TYR   B CB   1 
ATOM   6376 C  CG   . TYR   B 1 161 ? 43.441 -35.479 -11.821 1.00 18.10 ?  161 TYR   B CG   1 
ATOM   6377 C  CD1  . TYR   B 1 161 ? 43.048 -34.157 -11.994 1.00 18.03 ?  161 TYR   B CD1  1 
ATOM   6378 C  CD2  . TYR   B 1 161 ? 43.278 -36.356 -12.889 1.00 18.70 ?  161 TYR   B CD2  1 
ATOM   6379 C  CE1  . TYR   B 1 161 ? 42.513 -33.722 -13.184 1.00 19.01 ?  161 TYR   B CE1  1 
ATOM   6380 C  CE2  . TYR   B 1 161 ? 42.740 -35.929 -14.085 1.00 19.73 ?  161 TYR   B CE2  1 
ATOM   6381 C  CZ   . TYR   B 1 161 ? 42.363 -34.609 -14.228 1.00 19.54 ?  161 TYR   B CZ   1 
ATOM   6382 O  OH   . TYR   B 1 161 ? 41.821 -34.176 -15.414 1.00 21.47 ?  161 TYR   B OH   1 
ATOM   6383 H  H    . TYR   B 1 161 ? 44.518 -36.932 -8.345  1.00 20.53 ?  161 TYR   B H    1 
ATOM   6384 H  HA   . TYR   B 1 161 ? 42.460 -35.664 -9.204  1.00 20.25 ?  161 TYR   B HA   1 
ATOM   6385 H  HB2  . TYR   B 1 161 ? 44.510 -35.193 -10.125 1.00 20.84 ?  161 TYR   B HB2  1 
ATOM   6386 H  HB3  . TYR   B 1 161 ? 44.637 -36.666 -10.700 1.00 20.84 ?  161 TYR   B HB3  1 
ATOM   6387 H  HD1  . TYR   B 1 161 ? 43.148 -33.548 -11.296 1.00 21.61 ?  161 TYR   B HD1  1 
ATOM   6388 H  HD2  . TYR   B 1 161 ? 43.528 -37.246 -12.797 1.00 22.41 ?  161 TYR   B HD2  1 
ATOM   6389 H  HE1  . TYR   B 1 161 ? 42.255 -32.829 -13.283 1.00 22.79 ?  161 TYR   B HE1  1 
ATOM   6390 H  HE2  . TYR   B 1 161 ? 42.630 -36.524 -14.793 1.00 23.65 ?  161 TYR   B HE2  1 
ATOM   6391 H  HH   . TYR   B 1 161 ? 41.778 -34.808 -15.964 1.00 25.74 ?  161 TYR   B HH   1 
ATOM   6392 N  N    . ASP   B 1 162 ? 42.532 -38.674 -10.318 1.00 17.40 ?  162 ASP   B N    1 
ATOM   6393 C  CA   . ASP   B 1 162 ? 41.705 -39.711 -10.929 1.00 17.96 ?  162 ASP   B CA   1 
ATOM   6394 C  C    . ASP   B 1 162 ? 40.501 -40.044 -10.056 1.00 17.12 ?  162 ASP   B C    1 
ATOM   6395 O  O    . ASP   B 1 162 ? 39.394 -40.254 -10.567 1.00 17.74 ?  162 ASP   B O    1 
ATOM   6396 C  CB   . ASP   B 1 162 ? 42.537 -40.974 -11.181 1.00 19.39 ?  162 ASP   B CB   1 
ATOM   6397 C  CG   . ASP   B 1 162 ? 43.542 -40.810 -12.308 1.00 20.95 ?  162 ASP   B CG   1 
ATOM   6398 O  OD1  . ASP   B 1 162 ? 43.419 -39.865 -13.109 1.00 21.37 ?  162 ASP   B OD1  1 
ATOM   6399 O  OD2  . ASP   B 1 162 ? 44.447 -41.663 -12.410 1.00 22.44 -1 162 ASP   B OD2  1 
ATOM   6400 H  H    . ASP   B 1 162 ? 43.331 -38.921 -10.127 1.00 20.86 ?  162 ASP   B H    1 
ATOM   6401 H  HA   . ASP   B 1 162 ? 41.374 -39.393 -11.781 1.00 21.53 ?  162 ASP   B HA   1 
ATOM   6402 H  HB2  . ASP   B 1 162 ? 43.034 -41.193 -10.380 1.00 23.25 ?  162 ASP   B HB2  1 
ATOM   6403 H  HB3  . ASP   B 1 162 ? 41.939 -41.703 -11.413 1.00 23.25 ?  162 ASP   B HB3  1 
ATOM   6404 N  N    A LYS   B 1 163 ? 40.699 -40.120 -8.738  0.72 16.36 ?  163 LYS   B N    1 
ATOM   6405 N  N    B LYS   B 1 163 ? 40.695 -40.105 -8.736  0.28 17.06 ?  163 LYS   B N    1 
ATOM   6406 C  CA   A LYS   B 1 163 ? 39.576 -40.396 -7.850  0.72 16.94 ?  163 LYS   B CA   1 
ATOM   6407 C  CA   B LYS   B 1 163 ? 39.577 -40.396 -7.843  0.28 17.57 ?  163 LYS   B CA   1 
ATOM   6408 C  C    A LYS   B 1 163 ? 38.538 -39.283 -7.919  0.72 16.09 ?  163 LYS   B C    1 
ATOM   6409 C  C    B LYS   B 1 163 ? 38.541 -39.279 -7.872  0.28 16.25 ?  163 LYS   B C    1 
ATOM   6410 O  O    A LYS   B 1 163 ? 37.326 -39.549 -7.940  0.72 16.83 ?  163 LYS   B O    1 
ATOM   6411 O  O    B LYS   B 1 163 ? 37.333 -39.541 -7.812  0.28 16.48 ?  163 LYS   B O    1 
ATOM   6412 C  CB   A LYS   B 1 163 ? 40.061 -40.582 -6.414  0.72 19.59 ?  163 LYS   B CB   1 
ATOM   6413 C  CB   B LYS   B 1 163 ? 40.085 -40.614 -6.418  0.28 19.78 ?  163 LYS   B CB   1 
ATOM   6414 C  CG   A LYS   B 1 163 ? 38.979 -41.120 -5.500  0.72 23.79 ?  163 LYS   B CG   1 
ATOM   6415 C  CG   B LYS   B 1 163 ? 39.008 -41.101 -5.467  0.28 22.33 ?  163 LYS   B CG   1 
ATOM   6416 C  CD   A LYS   B 1 163 ? 39.395 -41.147 -4.043  0.72 27.38 ?  163 LYS   B CD   1 
ATOM   6417 C  CD   B LYS   B 1 163 ? 39.514 -41.225 -4.043  0.28 24.86 ?  163 LYS   B CD   1 
ATOM   6418 C  CE   A LYS   B 1 163 ? 38.324 -41.830 -3.201  0.72 29.88 ?  163 LYS   B CE   1 
ATOM   6419 C  CE   B LYS   B 1 163 ? 38.459 -41.867 -3.156  0.28 26.75 ?  163 LYS   B CE   1 
ATOM   6420 N  NZ   A LYS   B 1 163 ? 38.469 -41.547 -1.747  0.72 31.43 ?  163 LYS   B NZ   1 
ATOM   6421 N  NZ   B LYS   B 1 163 ? 38.750 -41.681 -1.709  0.28 27.54 ?  163 LYS   B NZ   1 
ATOM   6422 H  H    A LYS   B 1 163 ? 41.459 -40.019 -8.345  0.72 19.61 ?  163 LYS   B H    1 
ATOM   6423 H  H    B LYS   B 1 163 ? 41.452 -39.987 -8.341  0.28 20.45 ?  163 LYS   B H    1 
ATOM   6424 H  HA   A LYS   B 1 163 ? 39.150 -41.218 -8.132  0.72 20.31 ?  163 LYS   B HA   1 
ATOM   6425 H  HA   B LYS   B 1 163 ? 39.146 -41.213 -8.136  0.28 21.07 ?  163 LYS   B HA   1 
ATOM   6426 H  HB2  A LYS   B 1 163 ? 40.799 -41.215 -6.410  0.72 23.48 ?  163 LYS   B HB2  1 
ATOM   6427 H  HB2  B LYS   B 1 163 ? 40.791 -41.281 -6.433  0.28 23.71 ?  163 LYS   B HB2  1 
ATOM   6428 H  HB3  A LYS   B 1 163 ? 40.354 -39.729 -6.064  0.72 23.48 ?  163 LYS   B HB3  1 
ATOM   6429 H  HB3  B LYS   B 1 163 ? 40.430 -39.777 -6.073  0.28 23.71 ?  163 LYS   B HB3  1 
ATOM   6430 H  HG2  A LYS   B 1 163 ? 38.191 -40.562 -5.575  0.72 28.52 ?  163 LYS   B HG2  1 
ATOM   6431 H  HG2  B LYS   B 1 163 ? 38.270 -40.472 -5.468  0.28 26.78 ?  163 LYS   B HG2  1 
ATOM   6432 H  HG3  A LYS   B 1 163 ? 38.765 -42.031 -5.767  0.72 28.52 ?  163 LYS   B HG3  1 
ATOM   6433 H  HG3  B LYS   B 1 163 ? 38.700 -41.976 -5.755  0.28 26.78 ?  163 LYS   B HG3  1 
ATOM   6434 H  HD2  A LYS   B 1 163 ? 40.222 -41.646 -3.951  0.72 32.83 ?  163 LYS   B HD2  1 
ATOM   6435 H  HD2  B LYS   B 1 163 ? 40.308 -41.783 -4.029  0.28 29.81 ?  163 LYS   B HD2  1 
ATOM   6436 H  HD3  A LYS   B 1 163 ? 39.507 -40.240 -3.723  0.72 32.83 ?  163 LYS   B HD3  1 
ATOM   6437 H  HD3  B LYS   B 1 163 ? 39.715 -40.343 -3.693  0.28 29.81 ?  163 LYS   B HD3  1 
ATOM   6438 H  HE2  A LYS   B 1 163 ? 37.449 -41.525 -3.486  0.72 35.83 ?  163 LYS   B HE2  1 
ATOM   6439 H  HE2  B LYS   B 1 163 ? 37.596 -41.468 -3.347  0.28 32.08 ?  163 LYS   B HE2  1 
ATOM   6440 H  HE3  A LYS   B 1 163 ? 38.392 -42.789 -3.327  0.72 35.83 ?  163 LYS   B HE3  1 
ATOM   6441 H  HE3  B LYS   B 1 163 ? 38.430 -42.820 -3.338  0.28 32.08 ?  163 LYS   B HE3  1 
ATOM   6442 H  HZ1  A LYS   B 1 163 ? 37.825 -41.962 -1.293  0.72 37.69 ?  163 LYS   B HZ1  1 
ATOM   6443 H  HZ1  B LYS   B 1 163 ? 38.114 -42.066 -1.220  0.28 33.03 ?  163 LYS   B HZ1  1 
ATOM   6444 H  HZ2  A LYS   B 1 163 ? 39.259 -41.837 -1.460  0.72 37.69 ?  163 LYS   B HZ2  1 
ATOM   6445 H  HZ2  B LYS   B 1 163 ? 39.534 -42.048 -1.508  0.28 33.03 ?  163 LYS   B HZ2  1 
ATOM   6446 H  HZ3  A LYS   B 1 163 ? 38.409 -40.672 -1.600  0.72 37.69 ?  163 LYS   B HZ3  1 
ATOM   6447 H  HZ3  B LYS   B 1 163 ? 38.777 -40.812 -1.515  0.28 33.03 ?  163 LYS   B HZ3  1 
ATOM   6448 N  N    . LEU   B 1 164 ? 38.998 -38.027 -7.953  1.00 15.06 ?  164 LEU   B N    1 
ATOM   6449 C  CA   . LEU   B 1 164 ? 38.083 -36.891 -8.011  1.00 14.76 ?  164 LEU   B CA   1 
ATOM   6450 C  C    . LEU   B 1 164 ? 37.298 -36.875 -9.319  1.00 14.98 ?  164 LEU   B C    1 
ATOM   6451 O  O    . LEU   B 1 164 ? 36.073 -36.680 -9.319  1.00 16.00 ?  164 LEU   B O    1 
ATOM   6452 C  CB   . LEU   B 1 164 ? 38.884 -35.598 -7.855  1.00 14.32 ?  164 LEU   B CB   1 
ATOM   6453 C  CG   . LEU   B 1 164 ? 39.415 -35.317 -6.452  1.00 15.14 ?  164 LEU   B CG   1 
ATOM   6454 C  CD1  . LEU   B 1 164 ? 40.496 -34.246 -6.513  1.00 14.95 ?  164 LEU   B CD1  1 
ATOM   6455 C  CD2  . LEU   B 1 164 ? 38.296 -34.897 -5.517  1.00 16.86 ?  164 LEU   B CD2  1 
ATOM   6456 H  H    A LEU   B 1 164 ? 39.834 -37.811 -7.940  0.72 18.05 ?  164 LEU   B H    1 
ATOM   6457 H  H    B LEU   B 1 164 ? 39.835 -37.813 -7.973  0.28 18.05 ?  164 LEU   B H    1 
ATOM   6458 H  HA   . LEU   B 1 164 ? 37.456 -36.950 -7.282  1.00 17.68 ?  164 LEU   B HA   1 
ATOM   6459 H  HB2  . LEU   B 1 164 ? 39.654 -35.636 -8.451  1.00 17.17 ?  164 LEU   B HB2  1 
ATOM   6460 H  HB3  . LEU   B 1 164 ? 38.322 -34.854 -8.105  1.00 17.17 ?  164 LEU   B HB3  1 
ATOM   6461 H  HG   . LEU   B 1 164 ? 39.823 -36.121 -6.102  1.00 18.14 ?  164 LEU   B HG   1 
ATOM   6462 H  HD11 . LEU   B 1 164 ? 40.820 -34.066 -5.615  1.00 17.92 ?  164 LEU   B HD11 1 
ATOM   6463 H  HD12 . LEU   B 1 164 ? 41.232 -34.561 -7.067  1.00 17.92 ?  164 LEU   B HD12 1 
ATOM   6464 H  HD13 . LEU   B 1 164 ? 40.125 -33.434 -6.896  1.00 17.92 ?  164 LEU   B HD13 1 
ATOM   6465 H  HD21 . LEU   B 1 164 ? 38.671 -34.660 -4.657  1.00 20.22 ?  164 LEU   B HD21 1 
ATOM   6466 H  HD22 . LEU   B 1 164 ? 37.829 -34.139 -5.898  1.00 20.22 ?  164 LEU   B HD22 1 
ATOM   6467 H  HD23 . LEU   B 1 164 ? 37.681 -35.644 -5.414  1.00 20.22 ?  164 LEU   B HD23 1 
ATOM   6468 N  N    . VAL   B 1 165 ? 37.990 -37.050 -10.446 1.00 16.61 ?  165 VAL   B N    1 
ATOM   6469 C  CA   . VAL   B 1 165 ? 37.331 -36.990 -11.747 1.00 18.28 ?  165 VAL   B CA   1 
ATOM   6470 C  C    . VAL   B 1 165 ? 36.400 -38.182 -11.925 1.00 20.03 ?  165 VAL   B C    1 
ATOM   6471 O  O    . VAL   B 1 165 ? 35.236 -38.035 -12.319 1.00 21.32 ?  165 VAL   B O    1 
ATOM   6472 C  CB   . VAL   B 1 165 ? 38.376 -36.913 -12.876 1.00 19.26 ?  165 VAL   B CB   1 
ATOM   6473 C  CG1  . VAL   B 1 165 ? 37.710 -37.035 -14.227 1.00 20.61 ?  165 VAL   B CG1  1 
ATOM   6474 C  CG2  . VAL   B 1 165 ? 39.162 -35.618 -12.787 1.00 18.84 ?  165 VAL   B CG2  1 
ATOM   6475 H  H    . VAL   B 1 165 ? 38.843 -37.201 -10.486 1.00 19.91 ?  165 VAL   B H    1 
ATOM   6476 H  HA   . VAL   B 1 165 ? 36.796 -36.188 -11.789 1.00 21.92 ?  165 VAL   B HA   1 
ATOM   6477 H  HB   . VAL   B 1 165 ? 39.007 -37.645 -12.782 1.00 23.09 ?  165 VAL   B HB   1 
ATOM   6478 H  HG11 . VAL   B 1 165 ? 38.325 -36.735 -14.912 1.00 24.71 ?  165 VAL   B HG11 1 
ATOM   6479 H  HG12 . VAL   B 1 165 ? 37.483 -37.968 -14.379 1.00 24.71 ?  165 VAL   B HG12 1 
ATOM   6480 H  HG13 . VAL   B 1 165 ? 36.910 -36.493 -14.235 1.00 24.71 ?  165 VAL   B HG13 1 
ATOM   6481 H  HG21 . VAL   B 1 165 ? 39.800 -35.579 -13.519 1.00 22.58 ?  165 VAL   B HG21 1 
ATOM   6482 H  HG22 . VAL   B 1 165 ? 38.547 -34.868 -12.850 1.00 22.58 ?  165 VAL   B HG22 1 
ATOM   6483 H  HG23 . VAL   B 1 165 ? 39.633 -35.586 -11.940 1.00 22.58 ?  165 VAL   B HG23 1 
ATOM   6484 N  N    . SER   B 1 166 ? 36.906 -39.384 -11.633 1.00 20.65 ?  166 SER   B N    1 
ATOM   6485 C  CA   . SER   B 1 166 ? 36.149 -40.594 -11.920 1.00 21.72 ?  166 SER   B CA   1 
ATOM   6486 C  C    . SER   B 1 166 ? 34.891 -40.678 -11.072 1.00 22.00 ?  166 SER   B C    1 
ATOM   6487 O  O    . SER   B 1 166 ? 33.920 -41.304 -11.493 1.00 23.17 ?  166 SER   B O    1 
ATOM   6488 C  CB   . SER   B 1 166 ? 37.011 -41.850 -11.743 1.00 22.55 ?  166 SER   B CB   1 
ATOM   6489 O  OG   . SER   B 1 166 ? 37.387 -42.054 -10.391 1.00 22.55 ?  166 SER   B OG   1 
ATOM   6490 H  H    . SER   B 1 166 ? 37.681 -39.526 -11.277 1.00 24.75 ?  166 SER   B H    1 
ATOM   6491 H  HA   . SER   B 1 166 ? 35.873 -40.572 -12.851 1.00 26.04 ?  166 SER   B HA   1 
ATOM   6492 H  HB2  . SER   B 1 166 ? 36.506 -42.625 -12.044 1.00 27.04 ?  166 SER   B HB2  1 
ATOM   6493 H  HB3  . SER   B 1 166 ? 37.813 -41.760 -12.285 1.00 27.04 ?  166 SER   B HB3  1 
ATOM   6494 H  HG   . SER   B 1 166 ? 37.842 -41.402 -10.122 1.00 27.04 ?  166 SER   B HG   1 
ATOM   6495 N  N    . SER   B 1 167 ? 34.874 -40.066 -9.891  1.00 20.57 ?  167 SER   B N    1 
ATOM   6496 C  CA   . SER   B 1 167 ? 33.723 -40.126 -8.997  1.00 20.09 ?  167 SER   B CA   1 
ATOM   6497 C  C    . SER   B 1 167 ? 32.811 -38.902 -9.087  1.00 19.64 ?  167 SER   B C    1 
ATOM   6498 O  O    . SER   B 1 167 ? 31.731 -38.909 -8.485  1.00 20.10 ?  167 SER   B O    1 
ATOM   6499 C  CB   . SER   B 1 167 ? 34.179 -40.313 -7.543  1.00 20.07 ?  167 SER   B CB   1 
ATOM   6500 O  OG   . SER   B 1 167 ? 34.838 -39.149 -7.056  1.00 20.23 ?  167 SER   B OG   1 
ATOM   6501 H  H    . SER   B 1 167 ? 35.523 -39.608 -9.588  1.00 24.66 ?  167 SER   B H    1 
ATOM   6502 H  HA   . SER   B 1 167 ? 33.185 -40.902 -9.236  1.00 24.09 ?  167 SER   B HA   1 
ATOM   6503 H  HB2  . SER   B 1 167 ? 33.398 -40.500 -6.994  1.00 24.06 ?  167 SER   B HB2  1 
ATOM   6504 H  HB3  . SER   B 1 167 ? 34.788 -41.073 -7.507  1.00 24.06 ?  167 SER   B HB3  1 
ATOM   6505 H  HG   . SER   B 1 167 ? 35.509 -38.997 -7.528  1.00 24.26 ?  167 SER   B HG   1 
ATOM   6506 N  N    . PHE   B 1 168 ? 33.189 -37.867 -9.837  1.00 19.13 ?  168 PHE   B N    1 
ATOM   6507 C  CA   . PHE   B 1 168 ? 32.351 -36.669 -9.907  1.00 18.30 ?  168 PHE   B CA   1 
ATOM   6508 C  C    . PHE   B 1 168 ? 31.046 -36.935 -10.653 1.00 15.96 ?  168 PHE   B C    1 
ATOM   6509 O  O    . PHE   B 1 168 ? 29.996 -36.349 -10.321 1.00 16.32 ?  168 PHE   B O    1 
ATOM   6510 C  CB   . PHE   B 1 168 ? 33.116 -35.526 -10.572 1.00 19.23 ?  168 PHE   B CB   1 
ATOM   6511 C  CG   . PHE   B 1 168 ? 32.307 -34.279 -10.723 1.00 19.26 ?  168 PHE   B CG   1 
ATOM   6512 C  CD1  . PHE   B 1 168 ? 31.958 -33.533 -9.607  1.00 20.40 ?  168 PHE   B CD1  1 
ATOM   6513 C  CD2  . PHE   B 1 168 ? 31.873 -33.861 -11.965 1.00 18.56 ?  168 PHE   B CD2  1 
ATOM   6514 C  CE1  . PHE   B 1 168 ? 31.194 -32.388 -9.724  1.00 20.67 ?  168 PHE   B CE1  1 
ATOM   6515 C  CE2  . PHE   B 1 168 ? 31.117 -32.704 -12.097 1.00 19.64 ?  168 PHE   B CE2  1 
ATOM   6516 C  CZ   . PHE   B 1 168 ? 30.771 -31.967 -10.970 1.00 20.01 ?  168 PHE   B CZ   1 
ATOM   6517 H  H    . PHE   B 1 168 ? 33.903 -37.836 -10.308 1.00 22.93 ?  168 PHE   B H    1 
ATOM   6518 H  HA   . PHE   B 1 168 ? 32.119 -36.394 -9.009  1.00 21.94 ?  168 PHE   B HA   1 
ATOM   6519 H  HB2  . PHE   B 1 168 ? 33.888 -35.313 -10.029 1.00 23.05 ?  168 PHE   B HB2  1 
ATOM   6520 H  HB3  . PHE   B 1 168 ? 33.394 -35.805 -11.456 1.00 23.05 ?  168 PHE   B HB3  1 
ATOM   6521 H  HD1  . PHE   B 1 168 ? 32.236 -33.817 -8.765  1.00 24.45 ?  168 PHE   B HD1  1 
ATOM   6522 H  HD2  . PHE   B 1 168 ? 32.098 -34.348 -12.722 1.00 22.24 ?  168 PHE   B HD2  1 
ATOM   6523 H  HE1  . PHE   B 1 168 ? 30.970 -31.901 -8.965  1.00 24.79 ?  168 PHE   B HE1  1 
ATOM   6524 H  HE2  . PHE   B 1 168 ? 30.827 -32.425 -12.938 1.00 23.54 ?  168 PHE   B HE2  1 
ATOM   6525 H  HZ   . PHE   B 1 168 ? 30.259 -31.194 -11.055 1.00 23.98 ?  168 PHE   B HZ   1 
ATOM   6526 N  N    . LEU   B 1 169 ? 31.093 -37.806 -11.659 1.00 16.36 ?  169 LEU   B N    1 
ATOM   6527 C  CA   . LEU   B 1 169 ? 29.923 -38.124 -12.468 1.00 18.41 ?  169 LEU   B CA   1 
ATOM   6528 C  C    . LEU   B 1 169 ? 29.928 -39.566 -12.959 1.00 20.90 ?  169 LEU   B C    1 
ATOM   6529 O  O    . LEU   B 1 169 ? 29.030 -39.983 -13.696 1.00 23.26 ?  169 LEU   B O    1 
ATOM   6530 C  CB   . LEU   B 1 169 ? 29.848 -37.187 -13.673 1.00 20.44 ?  169 LEU   B CB   1 
ATOM   6531 C  CG   . LEU   B 1 169 ? 28.592 -36.324 -13.760 1.00 23.13 ?  169 LEU   B CG   1 
ATOM   6532 C  CD1  . LEU   B 1 169 ? 28.535 -35.638 -15.108 1.00 24.06 ?  169 LEU   B CD1  1 
ATOM   6533 C  CD2  . LEU   B 1 169 ? 27.337 -37.145 -13.521 1.00 23.06 ?  169 LEU   B CD2  1 
ATOM   6534 O  OXT  . LEU   B 1 169 ? 30.831 -40.333 -12.636 1.00 21.78 -1 169 LEU   B OXT  1 
ATOM   6535 H  H    . LEU   B 1 169 ? 31.801 -38.227 -11.906 1.00 19.61 ?  169 LEU   B H    1 
ATOM   6536 H  HA   . LEU   B 1 169 ? 29.132 -37.991 -11.927 1.00 22.07 ?  169 LEU   B HA   1 
ATOM   6537 H  HB2  . LEU   B 1 169 ? 30.609 -36.585 -13.646 1.00 24.51 ?  169 LEU   B HB2  1 
ATOM   6538 H  HB3  . LEU   B 1 169 ? 29.885 -37.717 -14.486 1.00 24.51 ?  169 LEU   B HB3  1 
ATOM   6539 H  HG   . LEU   B 1 169 ? 28.633 -35.633 -13.078 1.00 27.74 ?  169 LEU   B HG   1 
ATOM   6540 H  HD11 . LEU   B 1 169 ? 27.749 -35.072 -15.140 1.00 28.85 ?  169 LEU   B HD11 1 
ATOM   6541 H  HD12 . LEU   B 1 169 ? 29.335 -35.103 -15.221 1.00 28.85 ?  169 LEU   B HD12 1 
ATOM   6542 H  HD13 . LEU   B 1 169 ? 28.486 -36.315 -15.800 1.00 28.85 ?  169 LEU   B HD13 1 
ATOM   6543 H  HD21 . LEU   B 1 169 ? 26.588 -36.715 -13.957 1.00 27.65 ?  169 LEU   B HD21 1 
ATOM   6544 H  HD22 . LEU   B 1 169 ? 27.470 -38.034 -13.890 1.00 27.65 ?  169 LEU   B HD22 1 
ATOM   6545 H  HD23 . LEU   B 1 169 ? 27.178 -37.205 -12.567 1.00 27.65 ?  169 LEU   B HD23 1 
HETATM 6546 C  C1   T TFA   C 2 .   ? 12.140 -1.274  1.450   0.40 12.44 ?  201 TFA   A C1   1 
HETATM 6547 C  C2   T TFA   C 2 .   ? 12.760 -1.733  0.107   0.40 14.82 ?  201 TFA   A C2   1 
HETATM 6548 O  O    T TFA   C 2 .   ? 12.841 -1.546  2.428   0.40 10.50 ?  201 TFA   A O    1 
HETATM 6549 F  F1   T TFA   C 2 .   ? 12.810 -3.075  0.074   0.40 16.12 ?  201 TFA   A F1   1 
HETATM 6550 F  F2   T TFA   C 2 .   ? 12.061 -1.349  -0.972  0.40 15.16 ?  201 TFA   A F2   1 
HETATM 6551 F  F3   T TFA   C 2 .   ? 14.000 -1.276  -0.086  0.40 16.06 ?  201 TFA   A F3   1 
HETATM 6552 O  OXT  T TFA   C 2 .   ? 11.055 -0.701  1.365   0.40 12.64 ?  201 TFA   A OXT  1 
HETATM 6553 N  N2   B A1A80 D 3 .   ? 14.839 -0.101  3.886   0.20 16.25 ?  202 A1A80 A N2   1 
HETATM 6554 C  C3   B A1A80 D 3 .   ? 14.181 -0.136  -0.454  0.20 18.28 ?  202 A1A80 A C3   1 
HETATM 6555 C  C6   B A1A80 D 3 .   ? 10.458 0.456   -1.436  0.20 19.41 ?  202 A1A80 A C6   1 
HETATM 6556 C  C9   B A1A80 D 3 .   ? 12.469 1.780   -0.033  0.20 19.00 ?  202 A1A80 A C9   1 
HETATM 6557 C  C12  B A1A80 D 3 .   ? 15.356 2.169   5.272   0.20 15.19 ?  202 A1A80 A C12  1 
HETATM 6558 C  C14  B A1A80 D 3 .   ? 15.652 3.659   3.566   0.20 14.82 ?  202 A1A80 A C14  1 
HETATM 6559 C  C1   B A1A80 D 3 .   ? 16.027 -1.257  0.959   0.20 18.16 ?  202 A1A80 A C1   1 
HETATM 6560 C  C10  B A1A80 D 3 .   ? 15.070 1.032   3.139   0.20 16.21 ?  202 A1A80 A C10  1 
HETATM 6561 C  C11  B A1A80 D 3 .   ? 14.879 -0.031  5.256   0.20 16.20 ?  202 A1A80 A C11  1 
HETATM 6562 C  C13  B A1A80 D 3 .   ? 15.351 2.264   3.835   0.20 15.42 ?  202 A1A80 A C13  1 
HETATM 6563 C  C15  B A1A80 D 3 .   ? 15.811 4.311   4.782   0.20 14.26 ?  202 A1A80 A C15  1 
HETATM 6564 C  C2   B A1A80 D 3 .   ? 14.720 -0.365  1.022   0.20 17.74 ?  202 A1A80 A C2   1 
HETATM 6565 C  C4   B A1A80 D 3 .   ? 12.779 0.521   -0.593  0.20 18.76 ?  202 A1A80 A C4   1 
HETATM 6566 C  C5   B A1A80 D 3 .   ? 11.733 -0.112  -1.290  0.20 19.07 ?  202 A1A80 A C5   1 
HETATM 6567 C  C7   B A1A80 D 3 .   ? 10.206 1.704   -0.860  0.20 19.60 ?  202 A1A80 A C7   1 
HETATM 6568 C  C8   B A1A80 D 3 .   ? 11.207 2.379   -0.151  0.20 19.45 ?  202 A1A80 A C8   1 
HETATM 6569 F  F1   B A1A80 D 3 .   ? 8.990  2.256   -0.991  0.20 19.92 ?  202 A1A80 A F1   1 
HETATM 6570 N  N1   B A1A80 D 3 .   ? 15.020 0.898   1.750   0.20 16.92 ?  202 A1A80 A N1   1 
HETATM 6571 N  N3   B A1A80 D 3 .   ? 15.123 1.046   6.006   0.20 15.93 ?  202 A1A80 A N3   1 
HETATM 6572 N  N4   B A1A80 D 3 .   ? 15.635 3.400   5.785   0.20 14.21 ?  202 A1A80 A N4   1 
HETATM 6573 O  O1   B A1A80 D 3 .   ? 15.723 -2.404  0.225   0.20 18.46 ?  202 A1A80 A O1   1 
HETATM 6574 H  H5   B A1A80 D 3 .   ? 14.935 0.462   -0.992  0.20 21.91 ?  202 A1A80 A H5   1 
HETATM 6575 H  H6   B A1A80 D 3 .   ? 14.233 -1.081  -1.036  0.20 21.91 ?  202 A1A80 A H6   1 
HETATM 6576 H  H8   B A1A80 D 3 .   ? 9.659  -0.058  -1.990  0.20 23.27 ?  202 A1A80 A H8   1 
HETATM 6577 H  H10  B A1A80 D 3 .   ? 13.245 2.326   0.530   0.20 22.77 ?  202 A1A80 A H10  1 
HETATM 6578 H  H13  B A1A80 D 3 .   ? 15.743 4.166   2.625   0.20 17.76 ?  202 A1A80 A H13  1 
HETATM 6579 H  H3   B A1A80 D 3 .   ? 16.890 -0.701  0.518   0.20 21.77 ?  202 A1A80 A H3   1 
HETATM 6580 H  H4   B A1A80 D 3 .   ? 16.347 -1.553  1.973   0.20 21.77 ?  202 A1A80 A H4   1 
HETATM 6581 H  H12  B A1A80 D 3 .   ? 14.689 -0.941  5.852   0.20 19.42 ?  202 A1A80 A H12  1 
HETATM 6582 H  H14  B A1A80 D 3 .   ? 16.038 5.333   5.066   0.20 17.09 ?  202 A1A80 A H14  1 
HETATM 6583 H  H1   B A1A80 D 3 .   ? 13.912 -0.909  1.547   0.20 21.27 ?  202 A1A80 A H1   1 
HETATM 6584 H  H7   B A1A80 D 3 .   ? 11.906 -1.092  -1.754  0.20 22.86 ?  202 A1A80 A H7   1 
HETATM 6585 H  H9   B A1A80 D 3 .   ? 10.984 3.366   0.294   0.20 23.31 ?  202 A1A80 A H9   1 
HETATM 6586 H  H11  B A1A80 D 3 .   ? 15.202 1.719   1.181   0.20 20.28 ?  202 A1A80 A H11  1 
HETATM 6587 H  H15  B A1A80 D 3 .   ? 15.701 3.633   6.802   0.20 17.03 ?  202 A1A80 A H15  1 
HETATM 6588 H  H2   B A1A80 D 3 .   ? 16.540 -2.819  -0.075  0.20 22.13 ?  202 A1A80 A H2   1 
HETATM 6589 O  O1   C A1A8Z E 4 .   ? 15.456 -2.528  0.254   0.08 16.16 ?  203 A1A8Z A O1   1 
HETATM 6590 C  C1   C A1A8Z E 4 .   ? 15.803 -1.504  1.144   0.08 15.98 ?  203 A1A8Z A C1   1 
HETATM 6591 C  C2   C A1A8Z E 4 .   ? 14.863 -0.280  0.811   0.08 15.74 ?  203 A1A8Z A C2   1 
HETATM 6592 C  C3   C A1A8Z E 4 .   ? 13.343 -0.746  0.895   0.08 16.04 ?  203 A1A8Z A C3   1 
HETATM 6593 C  C4   C A1A8Z E 4 .   ? 12.312 0.164   0.239   0.08 16.34 ?  203 A1A8Z A C4   1 
HETATM 6594 C  C5   C A1A8Z E 4 .   ? 11.501 -0.271  -0.826  0.08 16.45 ?  203 A1A8Z A C5   1 
HETATM 6595 C  C6   C A1A8Z E 4 .   ? 10.558 0.546   -1.437  0.08 16.64 ?  203 A1A8Z A C6   1 
HETATM 6596 C  C7   C A1A8Z E 4 .   ? 10.385 1.853   -0.999  0.08 16.69 ?  203 A1A8Z A C7   1 
HETATM 6597 C  C8   C A1A8Z E 4 .   ? 11.163 2.324   0.050   0.08 16.65 ?  203 A1A8Z A C8   1 
HETATM 6598 C  C10  C A1A8Z E 4 .   ? 15.174 0.997   3.080   0.08 14.81 ?  203 A1A8Z A C10  1 
HETATM 6599 C  C11  C A1A8Z E 4 .   ? 14.886 -0.050  5.176   0.08 14.69 ?  203 A1A8Z A C11  1 
HETATM 6600 C  C12  C A1A8Z E 4 .   ? 15.384 2.127   5.255   0.08 14.17 ?  203 A1A8Z A C12  1 
HETATM 6601 C  C13  C A1A8Z E 4 .   ? 15.440 2.229   3.788   0.08 14.35 ?  203 A1A8Z A C13  1 
HETATM 6602 C  C14  C A1A8Z E 4 .   ? 15.766 3.616   3.540   0.08 14.01 ?  203 A1A8Z A C14  1 
HETATM 6603 C  C15  C A1A8Z E 4 .   ? 15.894 4.303   4.762   0.08 13.76 ?  203 A1A8Z A C15  1 
HETATM 6604 C  C9   C A1A8Z E 4 .   ? 12.100 1.493   0.646   0.08 16.50 ?  203 A1A8Z A C9   1 
HETATM 6605 F  F1   C A1A8Z E 4 .   ? 9.494  2.640   -1.568  0.08 16.74 ?  203 A1A8Z A F1   1 
HETATM 6606 N  N1   C A1A8Z E 4 .   ? 15.188 0.919   1.676   0.08 15.25 ?  203 A1A8Z A N1   1 
HETATM 6607 N  N2   C A1A8Z E 4 .   ? 14.897 -0.135  3.797   0.08 14.77 ?  203 A1A8Z A N2   1 
HETATM 6608 N  N3   C A1A8Z E 4 .   ? 15.113 1.015   5.935   0.08 14.53 ?  203 A1A8Z A N3   1 
HETATM 6609 N  N4   C A1A8Z E 4 .   ? 15.660 3.368   5.704   0.08 13.68 ?  203 A1A8Z A N4   1 
HETATM 6610 H  H2   C A1A8Z E 4 .   ? 15.922 -3.319  0.536   0.08 19.37 ?  203 A1A8Z A H2   1 
HETATM 6611 H  H4   C A1A8Z E 4 .   ? 16.875 -1.221  0.996   0.08 19.15 ?  203 A1A8Z A H4   1 
HETATM 6612 H  H3   C A1A8Z E 4 .   ? 15.744 -1.852  2.191   0.08 19.15 ?  203 A1A8Z A H3   1 
HETATM 6613 H  H1   C A1A8Z E 4 .   ? 15.015 0.002   -0.253  0.08 18.87 ?  203 A1A8Z A H1   1 
HETATM 6614 H  H5   C A1A8Z E 4 .   ? 13.215 -1.759  0.450   0.08 19.22 ?  203 A1A8Z A H5   1 
HETATM 6615 H  H6   C A1A8Z E 4 .   ? 13.032 -0.944  1.941   0.08 19.22 ?  203 A1A8Z A H6   1 
HETATM 6616 H  H7   C A1A8Z E 4 .   ? 11.609 -1.290  -1.196  0.08 19.72 ?  203 A1A8Z A H7   1 
HETATM 6617 H  H8   C A1A8Z E 4 .   ? 9.935  0.176   -2.271  0.08 19.94 ?  203 A1A8Z A H8   1 
HETATM 6618 H  H9   C A1A8Z E 4 .   ? 11.018 3.366   0.390   0.08 19.96 ?  203 A1A8Z A H9   1 
HETATM 6619 H  H12  C A1A8Z E 4 .   ? 14.663 -0.957  5.756   0.08 17.61 ?  203 A1A8Z A H12  1 
HETATM 6620 H  H13  C A1A8Z E 4 .   ? 15.899 4.106   2.596   0.08 16.79 ?  203 A1A8Z A H13  1 
HETATM 6621 H  H14  C A1A8Z E 4 .   ? 16.122 5.312   4.983   0.08 16.49 ?  203 A1A8Z A H14  1 
HETATM 6622 H  H10  C A1A8Z E 4 .   ? 12.689 1.905   1.464   0.08 19.78 ?  203 A1A8Z A H10  1 
HETATM 6623 H  H11  C A1A8Z E 4 .   ? 15.442 1.756   1.195   0.08 18.27 ?  203 A1A8Z A H11  1 
HETATM 6624 H  H15  C A1A8Z E 4 .   ? 15.685 3.578   6.692   0.08 16.39 ?  203 A1A8Z A H15  1 
HETATM 6625 CL CL   B CL    F 5 .   ? 16.087 2.786   -1.349  0.28 15.37 ?  204 CL    A CL   1 
HETATM 6626 O  O    . HOH   G 6 .   ? 14.654 -4.611  20.487  1.00 46.35 ?  301 HOH   A O    1 
HETATM 6627 O  O    . HOH   G 6 .   ? 4.667  3.742   0.526   1.00 22.07 ?  302 HOH   A O    1 
HETATM 6628 O  O    . HOH   G 6 .   ? 18.598 -2.354  -16.411 1.00 43.30 ?  303 HOH   A O    1 
HETATM 6629 O  O    . HOH   G 6 .   ? 11.945 0.355   14.716  1.00 33.44 ?  304 HOH   A O    1 
HETATM 6630 O  O    . HOH   G 6 .   ? 17.056 -17.960 15.016  1.00 26.22 ?  305 HOH   A O    1 
HETATM 6631 O  O    . HOH   G 6 .   ? 6.832  -7.970  11.803  1.00 18.12 ?  306 HOH   A O    1 
HETATM 6632 O  O    . HOH   G 6 .   ? 34.279 -1.845  12.505  1.00 37.75 ?  307 HOH   A O    1 
HETATM 6633 O  O    . HOH   G 6 .   ? 7.625  -6.280  -6.640  1.00 38.89 ?  308 HOH   A O    1 
HETATM 6634 O  O    . HOH   G 6 .   ? -0.647 -8.435  2.128   1.00 40.26 ?  309 HOH   A O    1 
HETATM 6635 O  O    . HOH   G 6 .   ? 28.903 0.484   -9.697  1.00 21.66 ?  310 HOH   A O    1 
HETATM 6636 O  O    . HOH   G 6 .   ? 30.979 6.188   -12.236 1.00 28.30 ?  311 HOH   A O    1 
HETATM 6637 O  O    . HOH   G 6 .   ? 14.649 -13.919 16.656  1.00 25.39 ?  312 HOH   A O    1 
HETATM 6638 O  O    . HOH   G 6 .   ? 19.878 -12.475 -8.948  1.00 25.01 ?  313 HOH   A O    1 
HETATM 6639 O  O    . HOH   G 6 .   ? 14.956 -12.155 18.629  1.00 40.46 ?  314 HOH   A O    1 
HETATM 6640 O  O    . HOH   G 6 .   ? 42.411 10.539  5.102   1.00 19.91 ?  315 HOH   A O    1 
HETATM 6641 O  O    B HOH   G 6 .   ? 11.220 -0.848  2.482   0.28 25.90 ?  316 HOH   A O    1 
HETATM 6642 O  O    . HOH   G 6 .   ? 14.131 -4.564  -11.888 1.00 30.27 ?  317 HOH   A O    1 
HETATM 6643 O  O    . HOH   G 6 .   ? 28.119 -6.296  19.613  1.00 41.12 ?  318 HOH   A O    1 
HETATM 6644 O  O    . HOH   G 6 .   ? 30.211 -13.319 -8.528  1.00 21.00 ?  319 HOH   A O    1 
HETATM 6645 O  O    . HOH   G 6 .   ? 18.624 -19.341 13.534  1.00 34.37 ?  320 HOH   A O    1 
HETATM 6646 O  O    . HOH   G 6 .   ? 14.980 4.013   17.681  1.00 40.44 ?  321 HOH   A O    1 
HETATM 6647 O  O    A HOH   G 6 .   ? 14.600 -3.621  3.091   0.72 13.80 ?  322 HOH   A O    1 
HETATM 6648 O  O    . HOH   G 6 .   ? 9.140  -10.043 19.312  1.00 37.34 ?  323 HOH   A O    1 
HETATM 6649 O  O    . HOH   G 6 .   ? 38.207 10.154  7.157   1.00 38.45 ?  324 HOH   A O    1 
HETATM 6650 O  O    . HOH   G 6 .   ? 21.260 -2.298  -2.335  1.00 16.05 ?  325 HOH   A O    1 
HETATM 6651 O  O    . HOH   G 6 .   ? 22.691 12.489  1.597   1.00 14.72 ?  326 HOH   A O    1 
HETATM 6652 O  O    . HOH   G 6 .   ? 0.697  -4.243  0.092   1.00 29.88 ?  327 HOH   A O    1 
HETATM 6653 O  O    . HOH   G 6 .   ? 26.454 -19.316 -1.769  1.00 14.09 ?  328 HOH   A O    1 
HETATM 6654 O  O    . HOH   G 6 .   ? 37.484 2.817   10.243  1.00 28.40 ?  329 HOH   A O    1 
HETATM 6655 O  O    B HOH   G 6 .   ? 15.270 6.879   6.904   0.28 20.82 ?  330 HOH   A O    1 
HETATM 6656 O  O    . HOH   G 6 .   ? 18.871 -21.966 6.995   1.00 31.47 ?  331 HOH   A O    1 
HETATM 6657 O  O    . HOH   G 6 .   ? 36.165 -5.109  -0.505  1.00 29.45 ?  332 HOH   A O    1 
HETATM 6658 O  O    . HOH   G 6 .   ? 27.909 0.819   -7.114  1.00 13.74 ?  333 HOH   A O    1 
HETATM 6659 O  O    . HOH   G 6 .   ? 30.985 -18.090 7.819   1.00 19.20 ?  334 HOH   A O    1 
HETATM 6660 O  O    . HOH   G 6 .   ? 33.979 -1.042  -8.913  1.00 27.07 ?  335 HOH   A O    1 
HETATM 6661 O  O    . HOH   G 6 .   ? 27.298 13.793  2.854   1.00 29.46 ?  336 HOH   A O    1 
HETATM 6662 O  O    . HOH   G 6 .   ? 22.230 5.399   18.904  1.00 40.10 ?  337 HOH   A O    1 
HETATM 6663 O  O    . HOH   G 6 .   ? 13.206 -1.472  -6.661  1.00 16.87 ?  338 HOH   A O    1 
HETATM 6664 O  O    . HOH   G 6 .   ? 11.725 -10.884 -10.116 1.00 43.70 ?  339 HOH   A O    1 
HETATM 6665 O  O    . HOH   G 6 .   ? 20.629 -19.729 -5.080  1.00 26.64 ?  340 HOH   A O    1 
HETATM 6666 O  O    . HOH   G 6 .   ? 15.153 -21.492 14.207  1.00 18.30 ?  341 HOH   A O    1 
HETATM 6667 O  O    A HOH   G 6 .   ? -0.512 -3.049  3.084   0.72 31.85 ?  342 HOH   A O    1 
HETATM 6668 O  O    . HOH   G 6 .   ? 44.315 7.143   6.424   1.00 25.95 ?  343 HOH   A O    1 
HETATM 6669 O  O    . HOH   G 6 .   ? 28.495 -10.675 -13.999 1.00 42.82 ?  344 HOH   A O    1 
HETATM 6670 O  O    . HOH   G 6 .   ? 20.056 4.504   -7.523  1.00 18.86 ?  345 HOH   A O    1 
HETATM 6671 O  O    . HOH   G 6 .   ? 28.312 -0.119  -13.358 1.00 33.93 ?  346 HOH   A O    1 
HETATM 6672 O  O    . HOH   G 6 .   ? 18.868 -0.737  -1.626  1.00 13.78 ?  347 HOH   A O    1 
HETATM 6673 O  O    A HOH   G 6 .   ? 3.557  -9.421  9.719   0.72 23.85 ?  348 HOH   A O    1 
HETATM 6674 O  O    . HOH   G 6 .   ? 38.532 4.990   7.022   1.00 15.25 ?  349 HOH   A O    1 
HETATM 6675 O  O    A HOH   G 6 .   ? 14.240 0.608   6.792   0.72 15.97 ?  350 HOH   A O    1 
HETATM 6676 O  O    . HOH   G 6 .   ? 9.830  -21.348 5.636   1.00 19.14 ?  351 HOH   A O    1 
HETATM 6677 O  O    . HOH   G 6 .   ? 39.739 -1.042  -5.156  1.00 21.07 ?  352 HOH   A O    1 
HETATM 6678 O  O    . HOH   G 6 .   ? 15.852 2.127   24.668  1.00 41.56 ?  353 HOH   A O    1 
HETATM 6679 O  O    . HOH   G 6 .   ? 7.908  -12.546 -0.913  1.00 20.64 ?  354 HOH   A O    1 
HETATM 6680 O  O    . HOH   G 6 .   ? 14.350 -21.206 -4.227  1.00 30.13 ?  355 HOH   A O    1 
HETATM 6681 O  O    . HOH   G 6 .   ? 13.521 -15.225 -7.495  1.00 25.20 ?  356 HOH   A O    1 
HETATM 6682 O  O    . HOH   G 6 .   ? 26.845 11.434  1.645   1.00 16.69 ?  357 HOH   A O    1 
HETATM 6683 O  O    . HOH   G 6 .   ? 42.548 4.281   5.462   1.00 30.97 ?  358 HOH   A O    1 
HETATM 6684 O  O    . HOH   G 6 .   ? 6.389  -5.436  11.040  1.00 17.71 ?  359 HOH   A O    1 
HETATM 6685 O  O    . HOH   G 6 .   ? 24.004 -2.088  -2.072  1.00 10.40 ?  360 HOH   A O    1 
HETATM 6686 O  O    A HOH   G 6 .   ? 17.464 -1.683  0.437   0.72 17.12 ?  361 HOH   A O    1 
HETATM 6687 O  O    . HOH   G 6 .   ? 35.728 -12.642 6.876   1.00 15.66 ?  362 HOH   A O    1 
HETATM 6688 O  O    . HOH   G 6 .   ? 31.639 8.209   14.859  1.00 24.39 ?  363 HOH   A O    1 
HETATM 6689 O  O    . HOH   G 6 .   ? 25.677 -0.785  -7.334  1.00 15.19 ?  364 HOH   A O    1 
HETATM 6690 O  O    . HOH   G 6 .   ? 31.051 -13.937 -2.459  1.00 13.60 ?  365 HOH   A O    1 
HETATM 6691 O  O    . HOH   G 6 .   ? 31.788 -9.352  -6.664  1.00 21.73 ?  366 HOH   A O    1 
HETATM 6692 O  O    . HOH   G 6 .   ? 17.111 -17.752 -5.060  1.00 26.61 ?  367 HOH   A O    1 
HETATM 6693 O  O    . HOH   G 6 .   ? 30.763 3.092   8.284   1.00 12.06 ?  368 HOH   A O    1 
HETATM 6694 O  O    . HOH   G 6 .   ? 22.099 -19.244 11.412  1.00 34.18 ?  369 HOH   A O    1 
HETATM 6695 O  O    . HOH   G 6 .   ? 37.284 11.984  4.937   1.00 27.41 ?  370 HOH   A O    1 
HETATM 6696 O  O    . HOH   G 6 .   ? 7.947  -21.535 4.061   1.00 43.90 ?  371 HOH   A O    1 
HETATM 6697 O  O    . HOH   G 6 .   ? 37.208 -2.771  9.738   1.00 40.14 ?  372 HOH   A O    1 
HETATM 6698 O  O    . HOH   G 6 .   ? 33.609 -7.134  4.336   1.00 16.31 ?  373 HOH   A O    1 
HETATM 6699 O  O    . HOH   G 6 .   ? 18.569 9.478   9.010   1.00 20.40 ?  374 HOH   A O    1 
HETATM 6700 O  O    . HOH   G 6 .   ? 21.837 -21.890 8.437   1.00 27.88 ?  375 HOH   A O    1 
HETATM 6701 O  O    T HOH   G 6 .   ? 15.374 -0.389  2.380   0.40 13.37 ?  376 HOH   A O    1 
HETATM 6702 O  O    . HOH   G 6 .   ? 24.616 -17.452 12.737  1.00 24.11 ?  377 HOH   A O    1 
HETATM 6703 O  O    . HOH   G 6 .   ? 43.933 8.445   -3.043  1.00 27.18 ?  378 HOH   A O    1 
HETATM 6704 O  O    . HOH   G 6 .   ? 24.158 -7.728  14.407  1.00 16.91 ?  379 HOH   A O    1 
HETATM 6705 O  O    . HOH   G 6 .   ? 33.478 -16.929 8.116   1.00 19.56 ?  380 HOH   A O    1 
HETATM 6706 O  O    . HOH   G 6 .   ? 43.343 7.801   2.703   1.00 27.84 ?  381 HOH   A O    1 
HETATM 6707 O  O    . HOH   G 6 .   ? 16.481 -22.043 0.955   1.00 26.63 ?  382 HOH   A O    1 
HETATM 6708 O  O    B HOH   G 6 .   ? 14.833 -2.897  3.401   0.28 19.07 ?  383 HOH   A O    1 
HETATM 6709 O  O    . HOH   G 6 .   ? 13.879 -4.921  17.397  1.00 27.15 ?  384 HOH   A O    1 
HETATM 6710 O  O    A HOH   G 6 .   ? 11.034 -0.345  1.925   0.32 16.24 ?  385 HOH   A O    1 
HETATM 6711 O  O    . HOH   G 6 .   ? 31.766 -7.288  -9.827  1.00 21.33 ?  386 HOH   A O    1 
HETATM 6712 O  O    . HOH   G 6 .   ? 27.425 -6.054  -13.959 1.00 37.60 ?  387 HOH   A O    1 
HETATM 6713 O  O    . HOH   G 6 .   ? 27.405 -10.595 14.066  1.00 17.73 ?  388 HOH   A O    1 
HETATM 6714 O  O    . HOH   G 6 .   ? 16.942 -19.235 4.883   1.00 14.84 ?  389 HOH   A O    1 
HETATM 6715 O  O    . HOH   G 6 .   ? 21.177 10.273  15.024  1.00 33.88 ?  390 HOH   A O    1 
HETATM 6716 O  O    . HOH   G 6 .   ? 24.375 3.598   -1.816  1.00 14.84 ?  391 HOH   A O    1 
HETATM 6717 O  O    . HOH   G 6 .   ? 10.923 1.738   12.549  1.00 23.68 ?  392 HOH   A O    1 
HETATM 6718 O  O    . HOH   G 6 .   ? 32.726 -9.223  5.986   1.00 19.97 ?  393 HOH   A O    1 
HETATM 6719 O  O    . HOH   G 6 .   ? 21.762 -13.749 -8.192  1.00 35.39 ?  394 HOH   A O    1 
HETATM 6720 O  O    . HOH   G 6 .   ? 24.553 1.992   -6.998  1.00 19.16 ?  395 HOH   A O    1 
HETATM 6721 O  O    . HOH   G 6 .   ? 21.315 3.077   -0.313  1.00 13.40 ?  396 HOH   A O    1 
HETATM 6722 O  O    . HOH   G 6 .   ? 37.514 -2.057  5.852   1.00 27.23 ?  397 HOH   A O    1 
HETATM 6723 O  O    . HOH   G 6 .   ? 30.611 1.916   16.689  1.00 20.80 ?  398 HOH   A O    1 
HETATM 6724 O  O    . HOH   G 6 .   ? 14.004 -23.016 7.418   1.00 18.01 ?  399 HOH   A O    1 
HETATM 6725 O  O    . HOH   G 6 .   ? 23.461 11.378  4.075   1.00 12.33 ?  400 HOH   A O    1 
HETATM 6726 O  O    . HOH   G 6 .   ? 5.375  2.885   4.851   1.00 33.84 ?  401 HOH   A O    1 
HETATM 6727 O  O    . HOH   G 6 .   ? 14.456 -24.634 11.588  1.00 38.13 ?  402 HOH   A O    1 
HETATM 6728 O  O    . HOH   G 6 .   ? 6.640  -3.135  12.702  1.00 27.45 ?  403 HOH   A O    1 
HETATM 6729 O  O    . HOH   G 6 .   ? 15.158 -8.070  -9.763  1.00 22.35 ?  404 HOH   A O    1 
HETATM 6730 O  O    . HOH   G 6 .   ? 8.827  -12.023 17.115  1.00 45.03 ?  405 HOH   A O    1 
HETATM 6731 O  O    . HOH   G 6 .   ? 22.597 -11.826 21.745  1.00 46.23 ?  406 HOH   A O    1 
HETATM 6732 O  O    . HOH   G 6 .   ? 15.471 11.783  7.903   1.00 38.89 ?  407 HOH   A O    1 
HETATM 6733 O  O    A HOH   G 6 .   ? 15.765 -0.912  5.264   0.72 17.19 ?  408 HOH   A O    1 
HETATM 6734 O  O    . HOH   G 6 .   ? 27.291 2.333   18.714  1.00 30.32 ?  409 HOH   A O    1 
HETATM 6735 O  O    . HOH   G 6 .   ? 16.176 16.600  8.592   1.00 34.26 ?  410 HOH   A O    1 
HETATM 6736 O  O    . HOH   G 6 .   ? 29.976 -10.043 13.023  1.00 22.08 ?  411 HOH   A O    1 
HETATM 6737 O  O    . HOH   G 6 .   ? 44.806 -0.700  3.079   1.00 39.10 ?  412 HOH   A O    1 
HETATM 6738 O  O    . HOH   G 6 .   ? 20.526 -20.015 2.782   1.00 18.24 ?  413 HOH   A O    1 
HETATM 6739 O  O    . HOH   G 6 .   ? 23.896 -20.263 -1.363  1.00 16.87 ?  414 HOH   A O    1 
HETATM 6740 O  O    . HOH   G 6 .   ? 10.333 -22.182 -1.217  1.00 44.90 ?  415 HOH   A O    1 
HETATM 6741 O  O    . HOH   G 6 .   ? 40.852 -8.236  -6.798  1.00 35.12 ?  416 HOH   A O    1 
HETATM 6742 O  O    . HOH   G 6 .   ? 26.910 4.181   -0.663  1.00 12.50 ?  417 HOH   A O    1 
HETATM 6743 O  O    . HOH   G 6 .   ? 23.890 -15.714 -9.144  1.00 34.36 ?  418 HOH   A O    1 
HETATM 6744 O  O    . HOH   G 6 .   ? 30.261 -12.894 13.522  1.00 19.80 ?  419 HOH   A O    1 
HETATM 6745 O  O    . HOH   G 6 .   ? 14.533 -0.543  -12.160 1.00 22.77 ?  420 HOH   A O    1 
HETATM 6746 O  O    . HOH   G 6 .   ? 38.085 -1.362  -1.927  1.00 19.42 ?  421 HOH   A O    1 
HETATM 6747 O  O    . HOH   G 6 .   ? 32.631 -4.315  -9.890  1.00 28.00 ?  422 HOH   A O    1 
HETATM 6748 O  O    . HOH   G 6 .   ? 41.526 1.546   5.022   1.00 38.39 ?  423 HOH   A O    1 
HETATM 6749 O  O    . HOH   G 6 .   ? 35.047 -5.231  -3.070  1.00 17.54 ?  424 HOH   A O    1 
HETATM 6750 O  O    . HOH   G 6 .   ? 36.683 -4.955  5.409   1.00 23.53 ?  425 HOH   A O    1 
HETATM 6751 O  O    . HOH   G 6 .   ? 32.486 -10.637 3.220   1.00 32.03 ?  426 HOH   A O    1 
HETATM 6752 O  O    . HOH   G 6 .   ? 16.188 -14.175 20.154  1.00 49.55 ?  427 HOH   A O    1 
HETATM 6753 O  O    . HOH   G 6 .   ? 10.341 -13.697 -1.701  1.00 16.68 ?  428 HOH   A O    1 
HETATM 6754 O  O    . HOH   G 6 .   ? 24.013 3.925   -4.834  1.00 22.02 ?  429 HOH   A O    1 
HETATM 6755 O  O    . HOH   G 6 .   ? 22.586 8.216   18.339  1.00 47.06 ?  430 HOH   A O    1 
HETATM 6756 O  O    . HOH   G 6 .   ? 11.604 -10.659 16.945  1.00 23.39 ?  431 HOH   A O    1 
HETATM 6757 O  O    . HOH   G 6 .   ? 15.946 6.839   2.982   1.00 17.00 ?  432 HOH   A O    1 
HETATM 6758 O  O    . HOH   G 6 .   ? 18.508 4.909   -15.130 1.00 44.12 ?  433 HOH   A O    1 
HETATM 6759 O  O    . HOH   G 6 .   ? -1.450 -4.883  7.532   1.00 43.11 ?  434 HOH   A O    1 
HETATM 6760 O  O    . HOH   G 6 .   ? 19.462 -10.980 23.969  1.00 66.40 ?  435 HOH   A O    1 
HETATM 6761 O  O    . HOH   G 6 .   ? 37.690 -8.826  -3.439  1.00 22.94 ?  436 HOH   A O    1 
HETATM 6762 O  O    . HOH   G 6 .   ? 23.332 -20.901 1.351   1.00 18.58 ?  437 HOH   A O    1 
HETATM 6763 O  O    . HOH   G 6 .   ? 23.452 -8.004  17.086  1.00 21.96 ?  438 HOH   A O    1 
HETATM 6764 O  O    . HOH   G 6 .   ? 18.358 -15.930 16.286  1.00 38.13 ?  439 HOH   A O    1 
HETATM 6765 O  O    . HOH   G 6 .   ? 34.369 -8.067  -0.536  1.00 27.40 ?  440 HOH   A O    1 
HETATM 6766 O  O    . HOH   G 6 .   ? 23.170 7.564   -3.215  1.00 32.69 ?  441 HOH   A O    1 
HETATM 6767 O  O    . HOH   G 6 .   ? 18.838 1.969   -0.682  1.00 12.99 ?  442 HOH   A O    1 
HETATM 6768 O  O    A HOH   G 6 .   ? 16.230 2.979   -1.448  0.72 19.46 ?  443 HOH   A O    1 
HETATM 6769 O  O    . HOH   G 6 .   ? 27.053 -3.150  19.389  1.00 37.11 ?  444 HOH   A O    1 
HETATM 6770 O  O    . HOH   G 6 .   ? 9.418  -16.249 -2.006  1.00 38.34 ?  445 HOH   A O    1 
HETATM 6771 O  O    . HOH   G 6 .   ? 30.572 14.750  2.773   1.00 18.47 ?  446 HOH   A O    1 
HETATM 6772 O  O    . HOH   G 6 .   ? 21.409 -14.629 17.924  1.00 51.37 ?  447 HOH   A O    1 
HETATM 6773 O  O    . HOH   G 6 .   ? 21.245 -9.154  21.328  1.00 52.08 ?  448 HOH   A O    1 
HETATM 6774 O  O    A HOH   G 6 .   ? 13.994 -0.305  3.454   0.32 16.48 ?  449 HOH   A O    1 
HETATM 6775 O  O    . HOH   G 6 .   ? 31.306 -12.765 -0.006  1.00 19.96 ?  450 HOH   A O    1 
HETATM 6776 O  O    . HOH   G 6 .   ? 20.568 -17.670 24.797  1.00 52.16 ?  451 HOH   A O    1 
HETATM 6777 O  O    . HOH   G 6 .   ? 27.744 7.003   -6.523  1.00 37.36 ?  452 HOH   A O    1 
HETATM 6778 O  O    B HOH   G 6 .   ? 12.764 -3.114  1.516   0.28 26.09 ?  453 HOH   A O    1 
HETATM 6779 O  O    . HOH   G 6 .   ? 29.746 -16.043 10.778  1.00 36.32 ?  454 HOH   A O    1 
HETATM 6780 O  O    . HOH   G 6 .   ? 29.786 -1.903  -12.722 1.00 44.27 ?  455 HOH   A O    1 
HETATM 6781 O  O    . HOH   G 6 .   ? 32.398 -15.884 10.892  1.00 29.34 ?  456 HOH   A O    1 
HETATM 6782 O  O    . HOH   G 6 .   ? 25.398 8.230   -4.823  1.00 31.28 ?  457 HOH   A O    1 
HETATM 6783 O  O    . HOH   G 6 .   ? 24.844 5.607   20.724  1.00 54.46 ?  458 HOH   A O    1 
HETATM 6784 O  O    . HOH   G 6 .   ? 19.852 -17.351 -5.054  1.00 23.08 ?  459 HOH   A O    1 
HETATM 6785 O  O    . HOH   G 6 .   ? 23.104 -22.325 -3.328  1.00 35.38 ?  460 HOH   A O    1 
HETATM 6786 O  O    . HOH   G 6 .   ? 24.586 14.652  7.811   1.00 35.77 ?  461 HOH   A O    1 
HETATM 6787 O  O    . HOH   G 6 .   ? 26.907 11.632  -1.391  1.00 33.21 ?  462 HOH   A O    1 
HETATM 6788 O  O    . HOH   G 6 .   ? 15.696 -21.484 3.694   1.00 23.87 ?  463 HOH   A O    1 
HETATM 6789 O  O    . HOH   G 6 .   ? 21.821 5.120   -5.713  1.00 30.08 ?  464 HOH   A O    1 
HETATM 6790 O  O    . HOH   G 6 .   ? 18.745 10.922  11.287  1.00 32.46 ?  465 HOH   A O    1 
HETATM 6791 O  O    . HOH   G 6 .   ? 11.946 -13.396 16.383  1.00 50.84 ?  466 HOH   A O    1 
HETATM 6792 O  O    . HOH   G 6 .   ? 39.609 -7.023  -3.422  1.00 42.63 ?  467 HOH   A O    1 
HETATM 6793 O  O    . HOH   G 6 .   ? 27.408 -11.364 16.594  1.00 36.92 ?  468 HOH   A O    1 
HETATM 6794 O  O    . HOH   G 6 .   ? 12.317 1.690   17.339  1.00 39.42 ?  469 HOH   A O    1 
HETATM 6795 O  O    . HOH   G 6 .   ? 25.791 10.774  -3.768  1.00 26.27 ?  470 HOH   A O    1 
HETATM 6796 O  O    . HOH   G 6 .   ? 23.478 13.728  5.500   1.00 18.14 ?  471 HOH   A O    1 
HETATM 6797 O  O    . HOH   G 6 .   ? 10.975 -15.077 -6.108  1.00 34.70 ?  472 HOH   A O    1 
HETATM 6798 O  O    . HOH   G 6 .   ? 13.959 -10.342 -10.912 1.00 32.66 ?  473 HOH   A O    1 
HETATM 6799 O  O    . HOH   G 6 .   ? 23.093 11.802  -4.061  1.00 19.21 ?  474 HOH   A O    1 
HETATM 6800 O  O    . HOH   G 6 .   ? 18.035 -16.268 -8.860  1.00 38.98 ?  475 HOH   A O    1 
HETATM 6801 O  O    . HOH   G 6 .   ? 35.138 7.477   12.241  1.00 44.20 ?  476 HOH   A O    1 
HETATM 6802 O  O    . HOH   G 6 .   ? 15.697 -17.093 -6.985  1.00 31.08 ?  477 HOH   A O    1 
HETATM 6803 O  O    . HOH   G 6 .   ? 28.819 9.024   17.523  1.00 37.18 ?  478 HOH   A O    1 
HETATM 6804 O  O    . HOH   G 6 .   ? 17.368 -18.709 19.854  1.00 50.80 ?  479 HOH   A O    1 
HETATM 6805 O  O    . HOH   G 6 .   ? 16.767 -20.482 16.094  1.00 27.85 ?  480 HOH   A O    1 
HETATM 6806 O  O    . HOH   G 6 .   ? 40.949 -3.943  -0.397  1.00 37.70 ?  481 HOH   A O    1 
HETATM 6807 O  O    . HOH   G 6 .   ? 28.554 -4.668  -12.287 1.00 36.33 ?  482 HOH   A O    1 
HETATM 6808 O  O    . HOH   G 6 .   ? 30.815 0.722   19.139  1.00 40.62 ?  483 HOH   A O    1 
HETATM 6809 O  O    . HOH   G 6 .   ? 44.500 10.418  -1.609  1.00 31.50 ?  484 HOH   A O    1 
HETATM 6810 O  O    . HOH   G 6 .   ? 23.168 -12.837 19.281  1.00 47.15 ?  485 HOH   A O    1 
HETATM 6811 O  O    . HOH   G 6 .   ? 41.738 9.326   -3.951  1.00 30.56 ?  486 HOH   A O    1 
HETATM 6812 O  O    . HOH   G 6 .   ? 20.491 -16.073 -7.392  1.00 28.68 ?  487 HOH   A O    1 
HETATM 6813 O  O    . HOH   G 6 .   ? 28.622 -7.926  -15.263 1.00 48.47 ?  488 HOH   A O    1 
HETATM 6814 O  O    . HOH   G 6 .   ? 18.355 -23.153 1.936   1.00 42.67 ?  489 HOH   A O    1 
HETATM 6815 O  O    . HOH   G 6 .   ? 39.135 2.409   7.457   1.00 31.72 ?  490 HOH   A O    1 
HETATM 6816 O  O    . HOH   G 6 .   ? 13.849 -25.170 8.893   1.00 31.44 ?  491 HOH   A O    1 
HETATM 6817 O  O    . HOH   G 6 .   ? 31.423 -0.580  -10.540 1.00 30.31 ?  492 HOH   A O    1 
HETATM 6818 O  O    . HOH   G 6 .   ? 16.015 -6.802  -11.920 1.00 41.35 ?  493 HOH   A O    1 
HETATM 6819 O  O    . HOH   G 6 .   ? 40.569 -0.269  -7.782  1.00 33.60 ?  494 HOH   A O    1 
HETATM 6820 O  O    . HOH   G 6 .   ? 30.773 5.778   -14.747 1.00 32.28 ?  495 HOH   A O    1 
HETATM 6821 O  O    . HOH   G 6 .   ? 20.029 -22.335 4.218   1.00 27.04 ?  496 HOH   A O    1 
HETATM 6822 O  O    . HOH   G 6 .   ? 16.174 -23.368 5.749   1.00 27.21 ?  497 HOH   A O    1 
HETATM 6823 O  O    . HOH   G 6 .   ? 37.301 -6.618  7.633   1.00 26.14 ?  498 HOH   A O    1 
HETATM 6824 O  O    . HOH   G 6 .   ? 30.725 -5.828  -11.873 1.00 45.59 ?  499 HOH   A O    1 
HETATM 6825 O  O    . HOH   G 6 .   ? 23.160 -23.775 1.586   1.00 32.37 ?  500 HOH   A O    1 
HETATM 6826 O  O    . HOH   G 6 .   ? 8.078  -3.203  -5.855  1.00 45.25 ?  501 HOH   A O    1 
HETATM 6827 O  O    . HOH   G 6 .   ? 39.511 -0.001  6.620   1.00 30.70 ?  502 HOH   A O    1 
HETATM 6828 O  O    . HOH   G 6 .   ? 28.964 14.442  0.857   1.00 48.30 ?  503 HOH   A O    1 
HETATM 6829 O  O    . HOH   G 6 .   ? 37.983 13.950  6.723   1.00 40.01 ?  504 HOH   A O    1 
HETATM 6830 O  O    B HOH   G 6 .   ? 14.741 8.054   4.749   0.28 23.95 ?  505 HOH   A O    1 
HETATM 6831 O  O    . HOH   G 6 .   ? 21.985 -23.983 4.493   1.00 26.19 ?  506 HOH   A O    1 
HETATM 6832 O  O    . HOH   G 6 .   ? 36.414 -6.540  10.193  1.00 46.14 ?  507 HOH   A O    1 
HETATM 6833 O  O    T HOH   G 6 .   ? 11.892 -2.115  -3.662  0.40 13.27 ?  508 HOH   A O    1 
HETATM 6834 O  O    A HOH   G 6 .   ? 14.821 8.684   4.880   0.72 42.61 ?  509 HOH   A O    1 
HETATM 6835 O  O    . HOH   G 6 .   ? 24.064 8.986   -7.228  1.00 35.38 ?  510 HOH   A O    1 
HETATM 6836 O  O    . HOH   G 6 .   ? 17.028 -6.913  -14.334 1.00 43.78 ?  511 HOH   A O    1 
HETATM 6837 O  O    . HOH   G 6 .   ? 15.749 -12.295 27.386  1.00 46.51 ?  512 HOH   A O    1 
HETATM 6838 O  O    . HOH   G 6 .   ? 16.369 -21.118 18.756  1.00 37.14 ?  513 HOH   A O    1 
HETATM 6839 O  O    . HOH   G 6 .   ? 14.710 -22.753 19.818  1.00 34.08 ?  514 HOH   A O    1 
HETATM 6840 O  O    . HOH   H 6 .   ? 29.793 -22.408 5.524   1.00 20.08 ?  201 HOH   B O    1 
HETATM 6841 O  O    . HOH   H 6 .   ? 41.694 -35.987 -17.150 1.00 32.00 ?  202 HOH   B O    1 
HETATM 6842 O  O    . HOH   H 6 .   ? 59.104 -18.655 6.851   1.00 35.28 ?  203 HOH   B O    1 
HETATM 6843 O  O    . HOH   H 6 .   ? 48.019 -6.851  15.555  1.00 34.01 ?  204 HOH   B O    1 
HETATM 6844 O  O    . HOH   H 6 .   ? 37.959 -39.423 -0.134  1.00 39.97 ?  205 HOH   B O    1 
HETATM 6845 O  O    . HOH   H 6 .   ? 52.882 -13.458 -20.268 1.00 32.91 ?  206 HOH   B O    1 
HETATM 6846 O  O    . HOH   H 6 .   ? 49.398 -22.642 -19.770 1.00 47.77 ?  207 HOH   B O    1 
HETATM 6847 O  O    . HOH   H 6 .   ? 27.721 -29.163 -1.810  1.00 35.57 ?  208 HOH   B O    1 
HETATM 6848 O  O    . HOH   H 6 .   ? 30.191 -40.973 -8.050  1.00 17.21 ?  209 HOH   B O    1 
HETATM 6849 O  O    . HOH   H 6 .   ? 54.456 -9.394  -8.678  1.00 19.53 ?  210 HOH   B O    1 
HETATM 6850 O  O    . HOH   H 6 .   ? 29.907 -26.271 4.083   1.00 27.43 ?  211 HOH   B O    1 
HETATM 6851 O  O    . HOH   H 6 .   ? 56.300 -19.696 7.302   1.00 31.36 ?  212 HOH   B O    1 
HETATM 6852 O  O    . HOH   H 6 .   ? 27.841 -41.824 -15.139 1.00 37.07 ?  213 HOH   B O    1 
HETATM 6853 O  O    . HOH   H 6 .   ? 30.911 -28.755 4.376   1.00 27.82 ?  214 HOH   B O    1 
HETATM 6854 O  O    . HOH   H 6 .   ? 41.324 -7.723  5.467   1.00 38.25 ?  215 HOH   B O    1 
HETATM 6855 O  O    . HOH   H 6 .   ? 44.374 -7.213  2.031   1.00 33.80 ?  216 HOH   B O    1 
HETATM 6856 O  O    . HOH   H 6 .   ? 50.169 -3.354  7.178   1.00 36.40 ?  217 HOH   B O    1 
HETATM 6857 O  O    . HOH   H 6 .   ? 57.682 -24.431 5.074   1.00 35.36 ?  218 HOH   B O    1 
HETATM 6858 O  O    . HOH   H 6 .   ? 57.089 -26.837 -7.629  1.00 39.92 ?  219 HOH   B O    1 
HETATM 6859 O  O    . HOH   H 6 .   ? 58.169 -12.958 8.399   1.00 31.04 ?  220 HOH   B O    1 
HETATM 6860 O  O    . HOH   H 6 .   ? 47.340 -7.373  -3.825  1.00 39.92 ?  221 HOH   B O    1 
HETATM 6861 O  O    . HOH   H 6 .   ? 56.647 -30.741 -7.710  1.00 29.23 ?  222 HOH   B O    1 
HETATM 6862 O  O    . HOH   H 6 .   ? 55.321 -16.501 -14.329 1.00 31.85 ?  223 HOH   B O    1 
HETATM 6863 O  O    . HOH   H 6 .   ? 50.737 -6.099  0.168   1.00 25.84 ?  224 HOH   B O    1 
HETATM 6864 O  O    . HOH   H 6 .   ? 37.031 -19.847 -18.103 1.00 37.16 ?  225 HOH   B O    1 
HETATM 6865 O  O    . HOH   H 6 .   ? 34.516 -36.370 -7.146  1.00 18.77 ?  226 HOH   B O    1 
HETATM 6866 O  O    . HOH   H 6 .   ? 57.366 -16.258 -12.191 1.00 18.22 ?  227 HOH   B O    1 
HETATM 6867 O  O    . HOH   H 6 .   ? 34.857 -24.624 13.839  1.00 33.63 ?  228 HOH   B O    1 
HETATM 6868 O  O    . HOH   H 6 .   ? 51.628 -6.469  4.404   1.00 19.42 ?  229 HOH   B O    1 
HETATM 6869 O  O    . HOH   H 6 .   ? 41.484 -39.153 -14.872 1.00 22.10 ?  230 HOH   B O    1 
HETATM 6870 O  O    . HOH   H 6 .   ? 39.271 -10.876 6.123   1.00 24.41 ?  231 HOH   B O    1 
HETATM 6871 O  O    . HOH   H 6 .   ? 44.907 -43.548 -10.504 1.00 27.67 ?  232 HOH   B O    1 
HETATM 6872 O  O    . HOH   H 6 .   ? 32.753 -43.764 -11.273 1.00 21.00 ?  233 HOH   B O    1 
HETATM 6873 O  O    . HOH   H 6 .   ? 45.093 -34.946 6.839   1.00 43.29 ?  234 HOH   B O    1 
HETATM 6874 O  O    . HOH   H 6 .   ? 29.810 -34.192 -0.420  1.00 35.04 ?  235 HOH   B O    1 
HETATM 6875 O  O    . HOH   H 6 .   ? 25.411 -25.921 -1.247  1.00 31.31 ?  236 HOH   B O    1 
HETATM 6876 O  O    . HOH   H 6 .   ? 36.047 -43.359 -8.395  1.00 35.12 ?  237 HOH   B O    1 
HETATM 6877 O  O    . HOH   H 6 .   ? 50.704 -12.968 -0.459  1.00 11.84 ?  238 HOH   B O    1 
HETATM 6878 O  O    . HOH   H 6 .   ? 40.595 -16.057 14.126  1.00 23.16 ?  239 HOH   B O    1 
HETATM 6879 O  O    . HOH   H 6 .   ? 35.074 -7.996  -2.994  1.00 17.71 ?  240 HOH   B O    1 
HETATM 6880 O  O    . HOH   H 6 .   ? 46.370 -1.552  13.221  1.00 27.64 ?  241 HOH   B O    1 
HETATM 6881 O  O    . HOH   H 6 .   ? 48.487 -36.507 -15.506 1.00 45.10 ?  242 HOH   B O    1 
HETATM 6882 O  O    . HOH   H 6 .   ? 42.534 -25.342 2.682   1.00 15.17 ?  243 HOH   B O    1 
HETATM 6883 O  O    . HOH   H 6 .   ? 34.202 -18.418 11.417  1.00 25.17 ?  244 HOH   B O    1 
HETATM 6884 O  O    . HOH   H 6 .   ? 42.594 -22.846 3.877   1.00 11.74 ?  245 HOH   B O    1 
HETATM 6885 O  O    . HOH   H 6 .   ? 44.484 -27.755 -0.665  1.00 22.12 ?  246 HOH   B O    1 
HETATM 6886 O  O    . HOH   H 6 .   ? 43.011 -43.213 -8.169  1.00 28.66 ?  247 HOH   B O    1 
HETATM 6887 O  O    . HOH   H 6 .   ? 28.370 -19.687 -13.090 1.00 23.51 ?  248 HOH   B O    1 
HETATM 6888 O  O    . HOH   H 6 .   ? 39.468 -11.106 0.347   1.00 16.37 ?  249 HOH   B O    1 
HETATM 6889 O  O    . HOH   H 6 .   ? 38.453 -11.054 -2.236  1.00 19.03 ?  250 HOH   B O    1 
HETATM 6890 O  O    . HOH   H 6 .   ? 41.332 -9.590  13.089  1.00 22.33 ?  251 HOH   B O    1 
HETATM 6891 O  O    . HOH   H 6 .   ? 51.510 -13.819 11.033  1.00 26.24 ?  252 HOH   B O    1 
HETATM 6892 O  O    . HOH   H 6 .   ? 43.152 -32.387 -17.044 1.00 23.48 ?  253 HOH   B O    1 
HETATM 6893 O  O    . HOH   H 6 .   ? 57.595 -24.355 -3.765  1.00 21.28 ?  254 HOH   B O    1 
HETATM 6894 O  O    . HOH   H 6 .   ? 31.769 -17.909 -14.456 1.00 30.70 ?  255 HOH   B O    1 
HETATM 6895 O  O    . HOH   H 6 .   ? 27.099 -31.823 -9.884  1.00 19.97 ?  256 HOH   B O    1 
HETATM 6896 O  O    . HOH   H 6 .   ? 47.987 -24.515 -17.730 1.00 30.76 ?  257 HOH   B O    1 
HETATM 6897 O  O    . HOH   H 6 .   ? 40.318 -12.746 -11.497 1.00 15.01 ?  258 HOH   B O    1 
HETATM 6898 O  O    . HOH   H 6 .   ? 41.834 -23.499 9.322   1.00 17.80 ?  259 HOH   B O    1 
HETATM 6899 O  O    . HOH   H 6 .   ? 38.894 -11.960 12.383  1.00 34.21 ?  260 HOH   B O    1 
HETATM 6900 O  O    . HOH   H 6 .   ? 58.151 -10.648 -4.043  1.00 19.91 ?  261 HOH   B O    1 
HETATM 6901 O  O    . HOH   H 6 .   ? 50.942 -39.913 -8.196  1.00 34.21 ?  262 HOH   B O    1 
HETATM 6902 O  O    . HOH   H 6 .   ? 42.306 -9.909  9.383   1.00 20.93 ?  263 HOH   B O    1 
HETATM 6903 O  O    . HOH   H 6 .   ? 28.464 -30.893 -14.676 1.00 29.96 ?  264 HOH   B O    1 
HETATM 6904 O  O    . HOH   H 6 .   ? 29.697 -25.217 -10.763 1.00 17.11 ?  265 HOH   B O    1 
HETATM 6905 O  O    . HOH   H 6 .   ? 30.845 -15.722 2.677   1.00 13.75 ?  266 HOH   B O    1 
HETATM 6906 O  O    . HOH   H 6 .   ? 47.980 -22.747 5.861   1.00 17.29 ?  267 HOH   B O    1 
HETATM 6907 O  O    . HOH   H 6 .   ? 28.248 -34.343 -9.409  1.00 17.97 ?  268 HOH   B O    1 
HETATM 6908 O  O    . HOH   H 6 .   ? 57.442 -9.218  1.444   1.00 19.34 ?  269 HOH   B O    1 
HETATM 6909 O  O    . HOH   H 6 .   ? 34.908 -33.321 -19.149 1.00 32.91 ?  270 HOH   B O    1 
HETATM 6910 O  O    . HOH   H 6 .   ? 56.880 -8.628  8.451   1.00 18.66 ?  271 HOH   B O    1 
HETATM 6911 O  O    . HOH   H 6 .   ? 43.342 -15.789 -12.152 1.00 14.16 ?  272 HOH   B O    1 
HETATM 6912 O  O    . HOH   H 6 .   ? 34.459 -12.788 2.660   1.00 23.53 ?  273 HOH   B O    1 
HETATM 6913 O  O    . HOH   H 6 .   ? 42.351 -34.689 3.812   1.00 25.86 ?  274 HOH   B O    1 
HETATM 6914 O  O    . HOH   H 6 .   ? 42.859 -20.279 -20.718 1.00 33.78 ?  275 HOH   B O    1 
HETATM 6915 O  O    . HOH   H 6 .   ? 49.652 -0.456  10.226  1.00 30.14 ?  276 HOH   B O    1 
HETATM 6916 O  O    . HOH   H 6 .   ? 30.473 -42.218 -10.554 1.00 29.84 ?  277 HOH   B O    1 
HETATM 6917 O  O    . HOH   H 6 .   ? 49.278 -28.689 -6.848  1.00 15.10 ?  278 HOH   B O    1 
HETATM 6918 O  O    . HOH   H 6 .   ? 59.741 -15.286 8.153   1.00 30.85 ?  279 HOH   B O    1 
HETATM 6919 O  O    . HOH   H 6 .   ? 56.140 -23.564 -14.710 1.00 26.52 ?  280 HOH   B O    1 
HETATM 6920 O  O    . HOH   H 6 .   ? 46.820 -29.556 9.863   1.00 31.78 ?  281 HOH   B O    1 
HETATM 6921 O  O    . HOH   H 6 .   ? 46.606 -31.213 -4.754  1.00 22.27 ?  282 HOH   B O    1 
HETATM 6922 O  O    . HOH   H 6 .   ? 27.944 -22.889 -7.955  1.00 18.01 ?  283 HOH   B O    1 
HETATM 6923 O  O    . HOH   H 6 .   ? 48.373 -25.032 3.141   1.00 13.45 ?  284 HOH   B O    1 
HETATM 6924 O  O    . HOH   H 6 .   ? 57.076 -12.091 12.382  1.00 37.11 ?  285 HOH   B O    1 
HETATM 6925 O  O    . HOH   H 6 .   ? 45.304 -33.381 -15.896 1.00 24.60 ?  286 HOH   B O    1 
HETATM 6926 O  O    . HOH   H 6 .   ? 51.175 -37.563 -9.606  1.00 26.24 ?  287 HOH   B O    1 
HETATM 6927 O  O    . HOH   H 6 .   ? 49.917 -24.636 5.826   1.00 33.28 ?  288 HOH   B O    1 
HETATM 6928 O  O    . HOH   H 6 .   ? 36.773 -12.748 -1.492  1.00 26.24 ?  289 HOH   B O    1 
HETATM 6929 O  O    . HOH   H 6 .   ? 27.524 -26.658 -15.592 1.00 32.10 ?  290 HOH   B O    1 
HETATM 6930 O  O    . HOH   H 6 .   ? 41.129 -5.461  11.502  1.00 45.38 ?  291 HOH   B O    1 
HETATM 6931 O  O    . HOH   H 6 .   ? 33.491 -15.275 -13.920 1.00 20.79 ?  292 HOH   B O    1 
HETATM 6932 O  O    . HOH   H 6 .   ? 44.594 -27.455 2.047   1.00 15.36 ?  293 HOH   B O    1 
HETATM 6933 O  O    . HOH   H 6 .   ? 48.660 -20.013 5.972   1.00 14.08 ?  294 HOH   B O    1 
HETATM 6934 O  O    . HOH   H 6 .   ? 37.484 -18.066 13.132  1.00 30.93 ?  295 HOH   B O    1 
HETATM 6935 O  O    . HOH   H 6 .   ? 45.869 -40.368 -3.560  1.00 28.90 ?  296 HOH   B O    1 
HETATM 6936 O  O    . HOH   H 6 .   ? 52.451 -10.360 13.049  1.00 22.39 ?  297 HOH   B O    1 
HETATM 6937 O  O    . HOH   H 6 .   ? 42.727 -12.217 -18.466 1.00 28.38 ?  298 HOH   B O    1 
HETATM 6938 O  O    . HOH   H 6 .   ? 47.036 -33.949 -4.573  1.00 17.66 ?  299 HOH   B O    1 
HETATM 6939 O  O    . HOH   H 6 .   ? 35.061 -33.586 4.599   1.00 29.44 ?  300 HOH   B O    1 
HETATM 6940 O  O    . HOH   H 6 .   ? 44.024 -29.331 -4.646  1.00 22.93 ?  301 HOH   B O    1 
HETATM 6941 O  O    . HOH   H 6 .   ? 52.974 -16.008 -12.720 1.00 25.71 ?  302 HOH   B O    1 
HETATM 6942 O  O    . HOH   H 6 .   ? 42.327 -9.827  -14.836 1.00 38.04 ?  303 HOH   B O    1 
HETATM 6943 O  O    . HOH   H 6 .   ? 52.575 -35.622 -8.651  1.00 28.90 ?  304 HOH   B O    1 
HETATM 6944 O  O    . HOH   H 6 .   ? 25.934 -21.471 -3.504  1.00 16.60 ?  305 HOH   B O    1 
HETATM 6945 O  O    . HOH   H 6 .   ? 53.446 -30.185 4.527   1.00 18.49 ?  306 HOH   B O    1 
HETATM 6946 O  O    . HOH   H 6 .   ? 52.464 -29.256 -13.031 1.00 25.01 ?  307 HOH   B O    1 
HETATM 6947 O  O    . HOH   H 6 .   ? 40.222 -10.836 -9.511  1.00 16.92 ?  308 HOH   B O    1 
HETATM 6948 O  O    . HOH   H 6 .   ? 37.283 -35.654 7.247   1.00 32.58 ?  309 HOH   B O    1 
HETATM 6949 O  O    . HOH   H 6 .   ? 38.341 -9.367  -13.248 1.00 26.65 ?  310 HOH   B O    1 
HETATM 6950 O  O    . HOH   H 6 .   ? 51.348 -33.054 -10.781 1.00 41.73 ?  311 HOH   B O    1 
HETATM 6951 O  O    . HOH   H 6 .   ? 32.783 -34.564 -5.842  1.00 17.52 ?  312 HOH   B O    1 
HETATM 6952 O  O    . HOH   H 6 .   ? 51.696 -5.976  -7.863  1.00 44.80 ?  313 HOH   B O    1 
HETATM 6953 O  O    . HOH   H 6 .   ? 37.841 -10.242 -10.754 1.00 17.17 ?  314 HOH   B O    1 
HETATM 6954 O  O    . HOH   H 6 .   ? 62.660 -13.552 4.773   1.00 27.71 ?  315 HOH   B O    1 
HETATM 6955 O  O    . HOH   H 6 .   ? 57.631 -22.083 3.184   1.00 28.16 ?  316 HOH   B O    1 
HETATM 6956 O  O    . HOH   H 6 .   ? 45.624 -36.268 -16.055 1.00 34.45 ?  317 HOH   B O    1 
HETATM 6957 O  O    . HOH   H 6 .   ? 53.609 -12.590 -22.153 1.00 34.10 ?  318 HOH   B O    1 
HETATM 6958 O  O    . HOH   H 6 .   ? 43.173 -21.413 10.700  1.00 16.03 ?  319 HOH   B O    1 
HETATM 6959 O  O    . HOH   H 6 .   ? 26.326 -21.024 -6.209  1.00 16.46 ?  320 HOH   B O    1 
HETATM 6960 O  O    . HOH   H 6 .   ? 38.296 -12.716 7.951   1.00 17.99 ?  321 HOH   B O    1 
HETATM 6961 O  O    . HOH   H 6 .   ? 37.044 -30.577 -20.979 1.00 31.27 ?  322 HOH   B O    1 
HETATM 6962 O  O    . HOH   H 6 .   ? 41.701 -8.051  1.423   1.00 24.40 ?  323 HOH   B O    1 
HETATM 6963 O  O    . HOH   H 6 .   ? 44.094 -1.779  7.628   1.00 44.14 ?  324 HOH   B O    1 
HETATM 6964 O  O    . HOH   H 6 .   ? 44.577 -24.590 9.616   1.00 20.26 ?  325 HOH   B O    1 
HETATM 6965 O  O    . HOH   H 6 .   ? 59.917 -17.141 -10.457 1.00 33.24 ?  326 HOH   B O    1 
HETATM 6966 O  O    . HOH   H 6 .   ? 36.701 -12.383 4.308   1.00 17.86 ?  327 HOH   B O    1 
HETATM 6967 O  O    . HOH   H 6 .   ? 47.992 -32.662 -16.632 1.00 41.79 ?  328 HOH   B O    1 
HETATM 6968 O  O    . HOH   H 6 .   ? 48.554 -12.006 -14.089 1.00 26.31 ?  329 HOH   B O    1 
HETATM 6969 O  O    . HOH   H 6 .   ? 43.091 -34.582 0.127   1.00 20.60 ?  330 HOH   B O    1 
HETATM 6970 O  O    . HOH   H 6 .   ? 43.457 -15.398 18.178  1.00 30.53 ?  331 HOH   B O    1 
HETATM 6971 O  O    . HOH   H 6 .   ? 47.162 -24.464 8.194   1.00 24.73 ?  332 HOH   B O    1 
HETATM 6972 O  O    . HOH   H 6 .   ? 27.901 -14.788 -9.439  1.00 34.50 ?  333 HOH   B O    1 
HETATM 6973 O  O    . HOH   H 6 .   ? 41.187 -24.449 15.863  1.00 45.59 ?  334 HOH   B O    1 
HETATM 6974 O  O    . HOH   H 6 .   ? 62.854 -20.179 -0.685  1.00 37.07 ?  335 HOH   B O    1 
HETATM 6975 O  O    . HOH   H 6 .   ? 33.599 -31.172 11.090  1.00 34.48 ?  336 HOH   B O    1 
HETATM 6976 O  O    . HOH   H 6 .   ? 36.989 -15.147 -16.499 1.00 40.76 ?  337 HOH   B O    1 
HETATM 6977 O  O    . HOH   H 6 .   ? 47.436 -27.420 2.057   1.00 14.78 ?  338 HOH   B O    1 
HETATM 6978 O  O    . HOH   H 6 .   ? 42.809 -43.497 -14.332 1.00 41.75 ?  339 HOH   B O    1 
HETATM 6979 O  O    . HOH   H 6 .   ? 46.774 -19.849 12.294  1.00 29.17 ?  340 HOH   B O    1 
HETATM 6980 O  O    . HOH   H 6 .   ? 37.017 -45.092 -9.721  1.00 36.04 ?  341 HOH   B O    1 
HETATM 6981 O  O    . HOH   H 6 .   ? 38.418 -12.254 -16.253 1.00 45.09 ?  342 HOH   B O    1 
HETATM 6982 O  O    . HOH   H 6 .   ? 39.501 -23.637 -20.340 1.00 36.66 ?  343 HOH   B O    1 
HETATM 6983 O  O    . HOH   H 6 .   ? 28.865 -42.917 -12.297 1.00 38.90 ?  344 HOH   B O    1 
HETATM 6984 O  O    . HOH   H 6 .   ? 32.981 -14.681 1.073   1.00 18.76 ?  345 HOH   B O    1 
HETATM 6985 O  O    . HOH   H 6 .   ? 34.476 -10.322 7.684   1.00 23.52 ?  346 HOH   B O    1 
HETATM 6986 O  O    . HOH   H 6 .   ? 39.796 -44.253 -11.180 1.00 39.02 ?  347 HOH   B O    1 
HETATM 6987 O  O    . HOH   H 6 .   ? 33.650 -9.584  -8.828  1.00 32.01 ?  348 HOH   B O    1 
HETATM 6988 O  O    . HOH   H 6 .   ? 38.534 -22.312 15.042  1.00 40.01 ?  349 HOH   B O    1 
HETATM 6989 O  O    . HOH   H 6 .   ? 40.396 -43.471 -9.069  1.00 26.24 ?  350 HOH   B O    1 
HETATM 6990 O  O    . HOH   H 6 .   ? 44.155 -37.342 -17.766 1.00 33.17 ?  351 HOH   B O    1 
HETATM 6991 O  O    . HOH   H 6 .   ? 27.727 -26.589 -0.548  1.00 30.08 ?  352 HOH   B O    1 
HETATM 6992 O  O    . HOH   H 6 .   ? 62.532 -20.043 -4.786  1.00 45.73 ?  353 HOH   B O    1 
HETATM 6993 O  O    . HOH   H 6 .   ? 55.598 -8.246  10.851  1.00 23.65 ?  354 HOH   B O    1 
HETATM 6994 O  O    . HOH   H 6 .   ? 23.190 -23.651 6.830   1.00 34.91 ?  355 HOH   B O    1 
HETATM 6995 O  O    . HOH   H 6 .   ? 56.548 -7.279  3.106   1.00 26.39 ?  356 HOH   B O    1 
HETATM 6996 O  O    . HOH   H 6 .   ? 36.105 -8.514  -9.715  1.00 33.81 ?  357 HOH   B O    1 
HETATM 6997 O  O    . HOH   H 6 .   ? 34.016 -7.768  11.492  1.00 39.29 ?  358 HOH   B O    1 
HETATM 6998 O  O    . HOH   H 6 .   ? 61.460 -19.897 1.724   1.00 35.53 ?  359 HOH   B O    1 
HETATM 6999 O  O    . HOH   H 6 .   ? 56.858 -21.552 -16.372 1.00 39.70 ?  360 HOH   B O    1 
HETATM 7000 O  O    . HOH   H 6 .   ? 40.222 -8.848  9.930   1.00 34.87 ?  361 HOH   B O    1 
HETATM 7001 O  O    . HOH   H 6 .   ? 27.142 -25.933 -11.338 1.00 33.80 ?  362 HOH   B O    1 
HETATM 7002 O  O    . HOH   H 6 .   ? 43.153 -12.689 -21.152 1.00 39.61 ?  363 HOH   B O    1 
HETATM 7003 O  O    . HOH   H 6 .   ? 54.138 -5.715  3.056   1.00 34.72 ?  364 HOH   B O    1 
HETATM 7004 O  O    . HOH   H 6 .   ? 40.220 -11.318 -13.907 1.00 32.46 ?  365 HOH   B O    1 
HETATM 7005 O  O    . HOH   H 6 .   ? 32.544 -23.615 14.112  1.00 39.16 ?  366 HOH   B O    1 
HETATM 7006 O  O    . HOH   H 6 .   ? 48.351 -26.503 8.845   1.00 39.68 ?  367 HOH   B O    1 
HETATM 7007 O  O    . HOH   H 6 .   ? 58.877 -10.387 9.222   1.00 39.08 ?  368 HOH   B O    1 
HETATM 7008 O  O    . HOH   H 6 .   ? 39.819 -7.036  7.836   1.00 38.99 ?  369 HOH   B O    1 
HETATM 7009 O  O    . HOH   H 6 .   ? 36.132 -8.625  8.998   1.00 36.24 ?  370 HOH   B O    1 
HETATM 7010 O  O    . HOH   H 6 .   ? 41.785 -10.020 -17.435 1.00 54.88 ?  371 HOH   B O    1 
HETATM 7011 O  O    . HOH   H 6 .   ? 55.985 -7.756  -0.596  1.00 32.90 ?  372 HOH   B O    1 
HETATM 7012 O  O    . HOH   H 6 .   ? 52.020 -12.883 13.381  1.00 29.54 ?  373 HOH   B O    1 
HETATM 7013 O  O    . HOH   H 6 .   ? 62.987 -12.393 6.997   1.00 36.88 ?  374 HOH   B O    1 
HETATM 7014 O  O    . HOH   H 6 .   ? 37.979 -10.570 10.107  1.00 29.35 ?  375 HOH   B O    1 
HETATM 7015 O  O    . HOH   H 6 .   ? 42.590 -17.097 -23.087 1.00 42.48 ?  376 HOH   B O    1 
HETATM 7016 O  O    . HOH   H 6 .   ? 41.801 -6.691  -4.843  1.00 46.68 ?  377 HOH   B O    1 
HETATM 7017 O  O    . HOH   H 6 .   ? 36.483 -22.855 13.288  1.00 28.93 ?  378 HOH   B O    1 
HETATM 7018 O  O    . HOH   H 6 .   ? 44.082 -5.545  -3.574  1.00 41.89 ?  379 HOH   B O    1 
HETATM 7019 O  O    . HOH   H 6 .   ? 40.085 -7.648  3.199   1.00 36.14 ?  380 HOH   B O    1 
HETATM 7020 O  O    . HOH   H 6 .   ? 39.616 -14.056 15.690  1.00 47.57 ?  381 HOH   B O    1 
HETATM 7021 O  O    . HOH   H 6 .   ? 60.411 -22.211 2.871   1.00 47.20 ?  382 HOH   B O    1 
HETATM 7022 O  O    . HOH   H 6 .   ? 52.804 -29.876 7.222   1.00 22.97 ?  383 HOH   B O    1 
HETATM 7023 O  O    . HOH   H 6 .   ? 25.776 -18.828 -11.801 1.00 39.73 ?  384 HOH   B O    1 
HETATM 7024 O  O    . HOH   H 6 .   ? 46.773 -5.385  2.917   1.00 39.56 ?  385 HOH   B O    1 
HETATM 7025 O  O    . HOH   H 6 .   ? 40.993 -9.784  15.821  1.00 44.22 ?  386 HOH   B O    1 
HETATM 7026 O  O    . HOH   H 6 .   ? 23.903 -20.883 -7.616  1.00 28.71 ?  387 HOH   B O    1 
HETATM 7027 O  O    . HOH   H 6 .   ? 35.335 -20.339 13.343  1.00 31.65 ?  388 HOH   B O    1 
HETATM 7028 O  O    . HOH   H 6 .   ? 35.393 -33.742 7.429   1.00 40.41 ?  389 HOH   B O    1 
HETATM 7029 O  O    . HOH   H 6 .   ? 40.660 -6.617  -0.846  1.00 25.21 ?  390 HOH   B O    1 
HETATM 7030 O  O    . HOH   H 6 .   ? 44.079 -31.749 -3.786  1.00 37.45 ?  391 HOH   B O    1 
HETATM 7031 O  O    . HOH   H 6 .   ? 27.893 -27.071 2.214   1.00 28.77 ?  392 HOH   B O    1 
HETATM 7032 O  O    . HOH   H 6 .   ? 26.572 -27.935 -13.427 1.00 35.28 ?  393 HOH   B O    1 
HETATM 7033 O  O    . HOH   H 6 .   ? 24.611 -20.634 -10.498 1.00 36.23 ?  394 HOH   B O    1 
HETATM 7034 O  O    . HOH   H 6 .   ? 26.838 -30.680 -12.613 1.00 28.02 ?  395 HOH   B O    1 
HETATM 7035 O  O    . HOH   H 6 .   ? 50.617 -30.806 8.760   1.00 29.36 ?  396 HOH   B O    1 
HETATM 7036 O  O    . HOH   H 6 .   ? 34.339 -33.494 9.631   1.00 35.85 ?  397 HOH   B O    1 
HETATM 7037 O  O    . HOH   H 6 .   ? 57.586 -6.488  -2.295  1.00 33.10 ?  398 HOH   B O    1 
HETATM 7038 O  O    . HOH   H 6 .   ? 45.688 -20.149 15.235  1.00 51.30 ?  399 HOH   B O    1 
HETATM 7039 O  O    . HOH   H 6 .   ? 40.865 -11.758 -22.239 1.00 37.35 ?  400 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . VAL   A 3   ? 0.6771 0.6917 0.7780 -0.0215 -0.0356 0.0947  3   VAL   A N   
2    C  CA  . VAL   A 3   ? 0.6723 0.6873 0.7634 -0.0234 -0.0346 0.0940  3   VAL   A CA  
3    C  C   . VAL   A 3   ? 0.6460 0.6665 0.7166 -0.0331 -0.0358 0.0948  3   VAL   A C   
4    O  O   . VAL   A 3   ? 0.6509 0.6708 0.7345 -0.0315 -0.0384 0.0977  3   VAL   A O   
5    C  CB  . VAL   A 3   ? 0.6896 0.7006 0.7829 -0.0180 -0.0322 0.0924  3   VAL   A CB  
6    C  CG1 . VAL   A 3   ? 0.6957 0.7048 0.7877 -0.0158 -0.0317 0.0918  3   VAL   A CG1 
7    C  CG2 . VAL   A 3   ? 0.6956 0.7054 0.7881 -0.0165 -0.0312 0.0921  3   VAL   A CG2 
16   N  N   . ASN   A 4   ? 0.6104 0.6377 0.6383 -0.0454 -0.0334 0.0914  4   ASN   A N   
17   C  CA  . ASN   A 4   ? 0.5703 0.6053 0.5521 -0.0590 -0.0297 0.0859  4   ASN   A CA  
18   C  C   . ASN   A 4   ? 0.5153 0.5668 0.4901 -0.0744 -0.0111 0.0504  4   ASN   A C   
19   O  O   . ASN   A 4   ? 0.5175 0.5687 0.4868 -0.0741 -0.0134 0.0532  4   ASN   A O   
20   C  CB  . ASN   A 4   ? 0.5807 0.6089 0.5191 -0.0580 -0.0430 0.1152  4   ASN   A CB  
21   C  CG  . ASN   A 4   ? 0.5878 0.6104 0.4863 -0.0581 -0.0542 0.1413  4   ASN   A CG  
22   O  OD1 . ASN   A 4   ? 0.5918 0.6106 0.4751 -0.0583 -0.0588 0.1512  4   ASN   A OD1 
23   N  ND2 . ASN   A 4   ? 0.5891 0.6106 0.4768 -0.0576 -0.0575 0.1516  4   ASN   A ND2 
30   N  N   A SER   A 5   ? 0.4855 0.5454 0.4531 -0.0836 -0.0000 0.0310  5   SER   A N   
31   N  N   B SER   A 5   ? 0.4858 0.5447 0.4646 -0.0823 0.0002  0.0324  5   SER   A N   
32   C  CA  A SER   A 5   ? 0.4539 0.5228 0.4183 -0.0921 0.0128  0.0127  5   SER   A CA  
33   C  CA  B SER   A 5   ? 0.4541 0.5211 0.4369 -0.0909 0.0124  0.0161  5   SER   A CA  
34   C  C   A SER   A 5   ? 0.4172 0.4920 0.3753 -0.1014 0.0255  0.0058  5   SER   A C   
35   C  C   B SER   A 5   ? 0.4175 0.4909 0.3909 -0.1015 0.0251  0.0090  5   SER   A C   
36   O  O   A SER   A 5   ? 0.4183 0.4951 0.3656 -0.0985 0.0269  -0.0016 5   SER   A O   
37   O  O   B SER   A 5   ? 0.4191 0.4930 0.3924 -0.1007 0.0255  0.0043  5   SER   A O   
38   C  CB  A SER   A 5   ? 0.4589 0.5296 0.4328 -0.0922 0.0137  0.0036  5   SER   A CB  
39   C  CB  B SER   A 5   ? 0.4578 0.5258 0.4540 -0.0896 0.0122  0.0094  5   SER   A CB  
40   O  OG  A SER   A 5   ? 0.4614 0.5329 0.4411 -0.0932 0.0145  -0.0011 5   SER   A OG  
41   O  OG  B SER   A 5   ? 0.4595 0.5281 0.4627 -0.0890 0.0119  0.0061  5   SER   A OG  
52   N  N   . PHE   A 6   ? 0.3779 0.4573 0.3394 -0.1127 0.0367  0.0105  6   PHE   A N   
53   C  CA  . PHE   A 6   ? 0.3068 0.3899 0.2664 -0.1261 0.0469  0.0223  6   PHE   A CA  
54   C  C   . PHE   A 6   ? 0.2875 0.3698 0.2570 -0.1229 0.0554  0.0131  6   PHE   A C   
55   O  O   . PHE   A 6   ? 0.2947 0.3784 0.2871 -0.1238 0.0572  0.0274  6   PHE   A O   
56   C  CB  . PHE   A 6   ? 0.2738 0.3482 0.2287 -0.1236 0.0301  0.0362  6   PHE   A CB  
57   C  CG  . PHE   A 6   ? 0.2529 0.3170 0.2087 -0.1083 0.0122  0.0373  6   PHE   A CG  
58   C  CD1 . PHE   A 6   ? 0.2446 0.3042 0.2034 -0.0958 0.0110  0.0385  6   PHE   A CD1 
59   C  CD2 . PHE   A 6   ? 0.2565 0.3082 0.2149 -0.0899 0.0150  0.0423  6   PHE   A CD2 
60   C  CE1 . PHE   A 6   ? 0.2407 0.2990 0.2057 -0.0901 0.0181  0.0441  6   PHE   A CE1 
61   C  CE2 . PHE   A 6   ? 0.2518 0.3035 0.2272 -0.0832 0.0126  0.0362  6   PHE   A CE2 
62   C  CZ  . PHE   A 6   ? 0.2429 0.2984 0.2186 -0.0875 0.0136  0.0358  6   PHE   A CZ  
73   N  N   A SER   A 7   ? 0.2727 0.3532 0.2361 -0.1258 0.0611  0.0030  7   SER   A N   
74   N  N   B SER   A 7   ? 0.2783 0.3553 0.2580 -0.1093 0.0513  0.0032  7   SER   A N   
75   C  CA  A SER   A 7   ? 0.2696 0.3486 0.2501 -0.1122 0.0604  -0.0122 7   SER   A CA  
76   C  CA  B SER   A 7   ? 0.2735 0.3418 0.2677 -0.0905 0.0455  -0.0058 7   SER   A CA  
77   C  C   A SER   A 7   ? 0.2478 0.3085 0.2229 -0.1087 0.0679  -0.0130 7   SER   A C   
78   C  C   B SER   A 7   ? 0.2592 0.3159 0.2419 -0.0773 0.0474  -0.0051 7   SER   A C   
79   O  O   A SER   A 7   ? 0.2588 0.3025 0.2297 -0.1154 0.0738  -0.0137 7   SER   A O   
80   O  O   B SER   A 7   ? 0.2632 0.3136 0.2420 -0.0774 0.0500  -0.0065 7   SER   A O   
81   C  CB  A SER   A 7   ? 0.2931 0.3769 0.2940 -0.0963 0.0537  -0.0168 7   SER   A CB  
82   C  CB  B SER   A 7   ? 0.2844 0.3518 0.2999 -0.0828 0.0397  -0.0100 7   SER   A CB  
83   O  OG  A SER   A 7   ? 0.3113 0.3857 0.3291 -0.0859 0.0495  -0.0204 7   SER   A OG  
84   O  OG  B SER   A 7   ? 0.2924 0.3586 0.3225 -0.0774 0.0366  -0.0124 7   SER   A OG  
95   N  N   A GLY   A 8   ? 0.2189 0.2763 0.2104 -0.0952 0.0592  -0.0172 8   GLY   A N   
96   N  N   B GLY   A 8   ? 0.2421 0.2928 0.2225 -0.0633 0.0453  -0.0021 8   GLY   A N   
97   C  CA  A GLY   A 8   ? 0.2007 0.2485 0.2139 -0.0664 0.0530  -0.0087 8   GLY   A CA  
98   C  CA  B GLY   A 8   ? 0.2283 0.2687 0.2123 -0.0483 0.0396  0.0036  8   GLY   A CA  
99   C  C   A GLY   A 8   ? 0.1759 0.2242 0.2083 -0.0452 0.0416  -0.0041 8   GLY   A C   
100  C  C   B GLY   A 8   ? 0.2114 0.2461 0.1991 -0.0367 0.0356  0.0083  8   GLY   A C   
101  O  O   A GLY   A 8   ? 0.1836 0.2242 0.2339 -0.0251 0.0453  -0.0194 8   GLY   A O   
102  O  O   B GLY   A 8   ? 0.2134 0.2458 0.2043 -0.0299 0.0359  0.0019  8   GLY   A O   
109  N  N   A TYR   A 9   ? 0.1559 0.2095 0.1975 -0.0298 0.0293  0.0135  9   TYR   A N   
110  N  N   B TYR   A 9   ? 0.1952 0.2272 0.1903 -0.0294 0.0302  0.0181  9   TYR   A N   
111  C  CA  A TYR   A 9   ? 0.1422 0.1967 0.1793 -0.0310 0.0211  0.0229  9   TYR   A CA  
112  C  CA  B TYR   A 9   ? 0.1815 0.2091 0.1800 -0.0271 0.0280  0.0218  9   TYR   A CA  
113  C  C   A TYR   A 9   ? 0.1373 0.1782 0.1792 -0.0192 0.0265  0.0453  9   TYR   A C   
114  C  C   B TYR   A 9   ? 0.1779 0.1911 0.1756 -0.0197 0.0304  0.0201  9   TYR   A C   
115  O  O   A TYR   A 9   ? 0.1560 0.1903 0.2054 -0.0213 0.0158  0.0501  9   TYR   A O   
116  O  O   B TYR   A 9   ? 0.1787 0.1974 0.1827 -0.0205 0.0299  0.0172  9   TYR   A O   
117  C  CB  A TYR   A 9   ? 0.1405 0.2117 0.1765 -0.0264 0.0206  0.0102  9   TYR   A CB  
118  C  CB  B TYR   A 9   ? 0.1731 0.2129 0.1806 -0.0282 0.0228  0.0208  9   TYR   A CB  
119  C  CG  A TYR   A 9   ? 0.1436 0.2172 0.1841 -0.0221 0.0271  -0.0027 9   TYR   A CG  
120  C  CG  B TYR   A 9   ? 0.1677 0.2140 0.1772 -0.0274 0.0191  0.0191  9   TYR   A CG  
121  C  CD1 A TYR   A 9   ? 0.1522 0.2207 0.1966 -0.0314 0.0362  -0.0071 9   TYR   A CD1 
122  C  CD1 B TYR   A 9   ? 0.1687 0.2157 0.1827 -0.0310 0.0230  0.0183  9   TYR   A CD1 
123  C  CD2 A TYR   A 9   ? 0.1442 0.2119 0.1980 -0.0147 0.0227  0.0094  9   TYR   A CD2 
124  C  CD2 B TYR   A 9   ? 0.1653 0.2117 0.1757 -0.0230 0.0159  0.0238  9   TYR   A CD2 
125  C  CE1 A TYR   A 9   ? 0.1582 0.2256 0.2149 -0.0307 0.0430  -0.0125 9   TYR   A CE1 
126  C  CE1 B TYR   A 9   ? 0.1683 0.2165 0.1880 -0.0314 0.0263  0.0179  9   TYR   A CE1 
127  C  CE2 A TYR   A 9   ? 0.1473 0.2195 0.2038 -0.0152 0.0330  -0.0028 9   TYR   A CE2 
128  C  CE2 B TYR   A 9   ? 0.1631 0.2139 0.1763 -0.0215 0.0204  0.0215  9   TYR   A CE2 
129  C  CZ  A TYR   A 9   ? 0.1543 0.2276 0.2231 -0.0340 0.0520  -0.0104 9   TYR   A CZ  
130  C  CZ  B TYR   A 9   ? 0.1633 0.2149 0.1885 -0.0272 0.0311  0.0198  9   TYR   A CZ  
131  O  OH  A TYR   A 9   ? 0.1638 0.2393 0.2464 -0.0529 0.0565  -0.0101 9   TYR   A OH  
132  O  OH  B TYR   A 9   ? 0.1613 0.2173 0.2007 -0.0306 0.0369  0.0229  9   TYR   A OH  
151  N  N   A LEU   A 10  ? 0.1353 0.1582 0.1784 -0.0146 0.0180  0.0377  10  LEU   A N   
152  N  N   B LEU   A 10  ? 0.1804 0.1733 0.1725 -0.0134 0.0281  0.0138  10  LEU   A N   
153  C  CA  A LEU   A 10  ? 0.1231 0.1484 0.1838 -0.0178 0.0118  0.0414  10  LEU   A CA  
154  C  CA  B LEU   A 10  ? 0.1837 0.1632 0.1799 -0.0119 0.0240  0.0101  10  LEU   A CA  
155  C  C   A LEU   A 10  ? 0.1208 0.1400 0.1794 -0.0192 0.0069  0.0439  10  LEU   A C   
156  C  C   B LEU   A 10  ? 0.1714 0.1499 0.1679 -0.0099 0.0196  0.0153  10  LEU   A C   
157  O  O   A LEU   A 10  ? 0.1232 0.1395 0.1835 -0.0096 0.0209  0.0507  10  LEU   A O   
158  O  O   B LEU   A 10  ? 0.1697 0.1478 0.1712 -0.0114 0.0202  0.0223  10  LEU   A O   
159  C  CB  A LEU   A 10  ? 0.1278 0.1560 0.1964 -0.0169 -0.0037 0.0540  10  LEU   A CB  
160  C  CB  B LEU   A 10  ? 0.2058 0.1729 0.2133 -0.0179 0.0201  0.0041  10  LEU   A CB  
161  C  CG  A LEU   A 10  ? 0.1450 0.1714 0.2311 -0.0059 -0.0362 0.0626  10  LEU   A CG  
162  C  CG  B LEU   A 10  ? 0.2296 0.1903 0.2546 -0.0227 0.0179  0.0008  10  LEU   A CG  
163  C  CD1 A LEU   A 10  ? 0.1697 0.1878 0.2580 -0.0173 -0.0257 0.0524  10  LEU   A CD1 
164  C  CD1 B LEU   A 10  ? 0.2395 0.1959 0.2680 -0.0192 0.0209  0.0037  10  LEU   A CD1 
165  C  CD2 A LEU   A 10  ? 0.1737 0.1913 0.2510 -0.0076 -0.0206 0.0608  10  LEU   A CD2 
166  C  CD2 B LEU   A 10  ? 0.2315 0.1945 0.2649 -0.0307 0.0117  -0.0037 10  LEU   A CD2 
189  N  N   A LYS   A 11  ? 0.1273 0.1408 0.1731 -0.0209 0.0137  0.0350  11  LYS   A N   
190  N  N   B LYS   A 11  ? 0.1664 0.1428 0.1568 -0.0100 0.0161  0.0144  11  LYS   A N   
191  C  CA  A LYS   A 11  ? 0.1332 0.1358 0.1774 -0.0212 0.0164  0.0327  11  LYS   A CA  
192  C  CA  B LYS   A 11  ? 0.1579 0.1355 0.1466 -0.0118 0.0179  0.0143  11  LYS   A CA  
193  C  C   A LYS   A 11  ? 0.1293 0.1398 0.1821 -0.0242 0.0155  0.0214  11  LYS   A C   
194  C  C   B LYS   A 11  ? 0.1442 0.1232 0.1496 -0.0140 0.0182  0.0061  11  LYS   A C   
195  O  O   A LYS   A 11  ? 0.1425 0.1701 0.2069 -0.0503 0.0239  0.0070  11  LYS   A O   
196  O  O   B LYS   A 11  ? 0.1391 0.1140 0.1657 -0.0123 0.0151  -0.0084 11  LYS   A O   
197  C  CB  A LYS   A 11  ? 0.1394 0.1318 0.1759 -0.0206 0.0141  0.0258  11  LYS   A CB  
198  C  CB  B LYS   A 11  ? 0.1622 0.1332 0.1352 -0.0092 0.0172  0.0154  11  LYS   A CB  
199  C  CG  A LYS   A 11  ? 0.1472 0.1306 0.1791 -0.0205 0.0149  0.0294  11  LYS   A CG  
200  C  CG  B LYS   A 11  ? 0.1646 0.1381 0.1273 -0.0037 0.0160  0.0279  11  LYS   A CG  
201  C  CD  A LYS   A 11  ? 0.1525 0.1425 0.1848 -0.0201 0.0146  0.0282  11  LYS   A CD  
202  C  CD  B LYS   A 11  ? 0.1648 0.1470 0.1321 0.0019  0.0209  0.0307  11  LYS   A CD  
203  C  CE  A LYS   A 11  ? 0.1658 0.1444 0.1901 -0.0120 0.0102  0.0354  11  LYS   A CE  
204  C  CE  B LYS   A 11  ? 0.1628 0.1473 0.1197 0.0057  0.0246  0.0358  11  LYS   A CE  
205  N  NZ  A LYS   A 11  ? 0.1646 0.1426 0.1853 0.0001  0.0157  0.0297  11  LYS   A NZ  
206  N  NZ  B LYS   A 11  ? 0.1635 0.1513 0.1167 0.0116  0.0251  0.0297  11  LYS   A NZ  
233  N  N   A LEU   A 12  ? 0.1243 0.1307 0.1701 -0.0228 0.0165  0.0207  12  LEU   A N   
234  N  N   B LEU   A 12  ? 0.1375 0.1299 0.1529 -0.0050 0.0159  0.0006  12  LEU   A N   
235  C  CA  A LEU   A 12  ? 0.1278 0.1377 0.1605 -0.0135 0.0087  0.0237  12  LEU   A CA  
236  C  CA  B LEU   A 12  ? 0.1361 0.1371 0.1540 -0.0028 0.0171  0.0029  12  LEU   A CA  
237  C  C   A LEU   A 12  ? 0.1352 0.1279 0.1664 -0.0172 0.0113  0.0290  12  LEU   A C   
238  C  C   B LEU   A 12  ? 0.1326 0.1400 0.1510 -0.0029 0.0284  0.0055  12  LEU   A C   
239  O  O   A LEU   A 12  ? 0.1409 0.1331 0.1669 -0.0131 0.0205  0.0100  12  LEU   A O   
240  O  O   B LEU   A 12  ? 0.1422 0.1381 0.1491 0.0012  0.0270  0.0037  12  LEU   A O   
241  C  CB  A LEU   A 12  ? 0.1389 0.1366 0.1572 -0.0122 0.0031  0.0242  12  LEU   A CB  
242  C  CB  B LEU   A 12  ? 0.1438 0.1436 0.1679 -0.0033 0.0144  0.0035  12  LEU   A CB  
243  C  CG  A LEU   A 12  ? 0.1471 0.1459 0.1716 -0.0086 0.0122  0.0221  12  LEU   A CG  
244  C  CG  B LEU   A 12  ? 0.1458 0.1453 0.1880 -0.0005 0.0175  0.0022  12  LEU   A CG  
245  C  CD1 A LEU   A 12  ? 0.1573 0.1433 0.1788 0.0046  0.0233  0.0345  12  LEU   A CD1 
246  C  CD1 B LEU   A 12  ? 0.1438 0.1522 0.1984 0.0050  0.0273  0.0038  12  LEU   A CD1 
247  C  CD2 A LEU   A 12  ? 0.1485 0.1481 0.1993 -0.0080 0.0120  0.0184  12  LEU   A CD2 
248  C  CD2 B LEU   A 12  ? 0.1478 0.1491 0.1936 -0.0032 0.0146  -0.0083 12  LEU   A CD2 
271  N  N   A THR   A 13  ? 0.1335 0.1271 0.1821 -0.0142 0.0102  0.0256  13  THR   A N   
272  N  N   B THR   A 13  ? 0.1277 0.1394 0.1597 -0.0045 0.0225  0.0098  13  THR   A N   
273  C  CA  A THR   A 13  ? 0.1352 0.1331 0.1948 -0.0089 0.0165  0.0177  13  THR   A CA  
274  C  CA  B THR   A 13  ? 0.1280 0.1432 0.1641 -0.0104 0.0191  0.0154  13  THR   A CA  
275  C  C   A THR   A 13  ? 0.1316 0.1323 0.2014 -0.0135 0.0058  0.0314  13  THR   A C   
276  C  C   B THR   A 13  ? 0.1339 0.1499 0.1669 -0.0148 0.0185  0.0184  13  THR   A C   
277  O  O   A THR   A 13  ? 0.1341 0.1366 0.2035 -0.0104 0.0027  0.0306  13  THR   A O   
278  O  O   B THR   A 13  ? 0.1422 0.1538 0.1647 -0.0215 0.0201  0.0254  13  THR   A O   
279  C  CB  A THR   A 13  ? 0.1412 0.1456 0.2169 -0.0079 0.0207  0.0221  13  THR   A CB  
280  C  CB  B THR   A 13  ? 0.1230 0.1434 0.1607 -0.0083 0.0211  0.0211  13  THR   A CB  
281  O  OG1 A THR   A 13  ? 0.1503 0.1445 0.2352 -0.0127 0.0100  0.0289  13  THR   A OG1 
282  O  OG1 B THR   A 13  ? 0.1127 0.1456 0.1607 -0.0086 0.0354  0.0302  13  THR   A OG1 
283  C  CG2 A THR   A 13  ? 0.1541 0.1583 0.2324 -0.0086 0.0275  0.0122  13  THR   A CG2 
284  C  CG2 B THR   A 13  ? 0.1232 0.1457 0.1630 -0.0008 0.0191  0.0190  13  THR   A CG2 
299  N  N   A ASP   A 14  ? 0.1398 0.1390 0.2260 -0.0192 0.0045  0.0480  14  ASP   A N   
300  N  N   B ASP   A 14  ? 0.1361 0.1534 0.1822 -0.0115 0.0100  0.0200  14  ASP   A N   
301  C  CA  A ASP   A 14  ? 0.1408 0.1550 0.2539 -0.0177 -0.0037 0.0738  14  ASP   A CA  
302  C  CA  B ASP   A 14  ? 0.1465 0.1611 0.1968 -0.0050 -0.0054 0.0326  14  ASP   A CA  
303  C  C   A ASP   A 14  ? 0.1399 0.1617 0.2298 -0.0218 -0.0084 0.0666  14  ASP   A C   
304  C  C   B ASP   A 14  ? 0.1383 0.1576 0.1719 -0.0059 -0.0152 0.0494  14  ASP   A C   
305  O  O   A ASP   A 14  ? 0.1511 0.1747 0.2377 -0.0328 -0.0046 0.0673  14  ASP   A O   
306  O  O   B ASP   A 14  ? 0.1372 0.1633 0.1641 0.0003  -0.0220 0.0575  14  ASP   A O   
307  C  CB  A ASP   A 14  ? 0.1533 0.1784 0.3128 -0.0246 -0.0002 0.0963  14  ASP   A CB  
308  C  CB  B ASP   A 14  ? 0.1619 0.1757 0.2336 0.0007  -0.0118 0.0297  14  ASP   A CB  
309  C  CG  A ASP   A 14  ? 0.1804 0.2230 0.3954 -0.0253 -0.0033 0.0851  14  ASP   A CG  
310  C  CG  B ASP   A 14  ? 0.1728 0.1981 0.2648 0.0024  -0.0131 0.0289  14  ASP   A CG  
311  O  OD1 A ASP   A 14  ? 0.1996 0.2367 0.4211 -0.0118 -0.0155 0.0864  14  ASP   A OD1 
312  O  OD1 B ASP   A 14  ? 0.1828 0.2019 0.2700 0.0164  -0.0160 0.0399  14  ASP   A OD1 
313  O  OD2 A ASP   A 14  ? 0.2016 0.2483 0.4352 -0.0303 -0.0158 0.0641  14  ASP   A OD2 
314  O  OD2 B ASP   A 14  ? 0.1750 0.2130 0.2840 -0.0079 -0.0190 0.0169  14  ASP   A OD2 
323  N  N   A ASN   A 15  ? 0.1272 0.1509 0.2197 -0.0212 -0.0066 0.0634  15  ASN   A N   
324  N  N   B ASN   A 15  ? 0.1299 0.1475 0.1702 -0.0146 -0.0079 0.0566  15  ASN   A N   
325  C  CA  A ASN   A 15  ? 0.1319 0.1494 0.2269 -0.0157 -0.0138 0.0573  15  ASN   A CA  
326  C  CA  B ASN   A 15  ? 0.1294 0.1474 0.1786 -0.0194 -0.0068 0.0484  15  ASN   A CA  
327  C  C   A ASN   A 15  ? 0.1314 0.1454 0.2248 -0.0200 -0.0016 0.0459  15  ASN   A C   
328  C  C   B ASN   A 15  ? 0.1283 0.1453 0.1850 -0.0185 0.0066  0.0479  15  ASN   A C   
329  O  O   A ASN   A 15  ? 0.1338 0.1453 0.2057 -0.0193 -0.0062 0.0437  15  ASN   A O   
330  O  O   B ASN   A 15  ? 0.1331 0.1492 0.1840 -0.0204 0.0167  0.0504  15  ASN   A O   
331  C  CB  A ASN   A 15  ? 0.1267 0.1532 0.2300 -0.0094 -0.0009 0.0562  15  ASN   A CB  
332  C  CB  B ASN   A 15  ? 0.1249 0.1463 0.1777 -0.0252 -0.0050 0.0420  15  ASN   A CB  
333  C  CG  A ASN   A 15  ? 0.1347 0.1560 0.2475 -0.0102 0.0046  0.0362  15  ASN   A CG  
334  C  CG  B ASN   A 15  ? 0.1248 0.1513 0.1834 -0.0198 -0.0057 0.0238  15  ASN   A CG  
335  O  OD1 A ASN   A 15  ? 0.1447 0.1620 0.2701 -0.0223 0.0112  0.0437  15  ASN   A OD1 
336  O  OD1 B ASN   A 15  ? 0.1265 0.1582 0.1962 -0.0262 -0.0052 0.0236  15  ASN   A OD1 
337  N  ND2 A ASN   A 15  ? 0.1327 0.1584 0.2285 -0.0111 0.0215  0.0287  15  ASN   A ND2 
338  N  ND2 B ASN   A 15  ? 0.1216 0.1486 0.1721 -0.0134 0.0007  0.0164  15  ASN   A ND2 
351  N  N   A VAL   A 16  ? 0.1303 0.1375 0.2266 -0.0091 0.0102  0.0436  16  VAL   A N   
352  N  N   B VAL   A 16  ? 0.1236 0.1390 0.1812 -0.0107 0.0079  0.0490  16  VAL   A N   
353  C  CA  A VAL   A 16  ? 0.1273 0.1380 0.2157 -0.0076 0.0142  0.0416  16  VAL   A CA  
354  C  CA  B VAL   A 16  ? 0.1277 0.1413 0.1724 -0.0069 0.0126  0.0461  16  VAL   A CA  
355  C  C   A VAL   A 16  ? 0.1245 0.1317 0.2047 -0.0135 0.0087  0.0368  16  VAL   A C   
356  C  C   B VAL   A 16  ? 0.1251 0.1455 0.1645 -0.0071 0.0107  0.0425  16  VAL   A C   
357  O  O   A VAL   A 16  ? 0.1175 0.1213 0.2246 -0.0147 0.0128  0.0234  16  VAL   A O   
358  O  O   B VAL   A 16  ? 0.1239 0.1419 0.1639 -0.0073 0.0203  0.0432  16  VAL   A O   
359  C  CB  A VAL   A 16  ? 0.1337 0.1611 0.2173 0.0071  0.0302  0.0518  16  VAL   A CB  
360  C  CB  B VAL   A 16  ? 0.1401 0.1482 0.1730 0.0029  0.0265  0.0449  16  VAL   A CB  
361  C  CG1 A VAL   A 16  ? 0.1426 0.1747 0.2299 0.0104  0.0330  0.0551  16  VAL   A CG1 
362  C  CG1 B VAL   A 16  ? 0.1481 0.1523 0.1774 0.0067  0.0272  0.0457  16  VAL   A CG1 
363  C  CG2 A VAL   A 16  ? 0.1442 0.1763 0.2331 0.0061  0.0448  0.0496  16  VAL   A CG2 
364  C  CG2 B VAL   A 16  ? 0.1448 0.1517 0.1835 0.0086  0.0307  0.0436  16  VAL   A CG2 
383  N  N   A TYR   A 17  ? 0.1229 0.1327 0.2018 -0.0161 0.0133  0.0391  17  TYR   A N   
384  N  N   B TYR   A 17  ? 0.1281 0.1473 0.1598 -0.0107 0.0034  0.0355  17  TYR   A N   
385  C  CA  A TYR   A 17  ? 0.1279 0.1360 0.1805 -0.0187 0.0113  0.0347  17  TYR   A CA  
386  C  CA  B TYR   A 17  ? 0.1334 0.1514 0.1467 -0.0177 0.0000  0.0255  17  TYR   A CA  
387  C  C   A TYR   A 17  ? 0.1324 0.1296 0.1842 -0.0156 0.0137  0.0253  17  TYR   A C   
388  C  C   B TYR   A 17  ? 0.1307 0.1499 0.1397 -0.0216 0.0090  0.0252  17  TYR   A C   
389  O  O   A TYR   A 17  ? 0.1290 0.1264 0.1734 -0.0122 0.0152  0.0305  17  TYR   A O   
390  O  O   B TYR   A 17  ? 0.1272 0.1496 0.1384 -0.0264 0.0103  0.0232  17  TYR   A O   
391  C  CB  A TYR   A 17  ? 0.1454 0.1445 0.1813 -0.0271 0.0036  0.0395  17  TYR   A CB  
392  C  CB  B TYR   A 17  ? 0.1488 0.1573 0.1545 -0.0202 -0.0040 0.0218  17  TYR   A CB  
393  C  CG  A TYR   A 17  ? 0.1752 0.1590 0.1881 -0.0391 -0.0150 0.0436  17  TYR   A CG  
394  C  CG  B TYR   A 17  ? 0.1663 0.1665 0.1645 -0.0193 -0.0100 0.0181  17  TYR   A CG  
395  C  CD1 A TYR   A 17  ? 0.1898 0.1654 0.2061 -0.0304 -0.0241 0.0424  17  TYR   A CD1 
396  C  CD1 B TYR   A 17  ? 0.1767 0.1713 0.1789 -0.0110 -0.0097 0.0220  17  TYR   A CD1 
397  C  CD2 A TYR   A 17  ? 0.1921 0.1680 0.1811 -0.0551 -0.0209 0.0523  17  TYR   A CD2 
398  C  CD2 B TYR   A 17  ? 0.1742 0.1753 0.1702 -0.0204 -0.0116 0.0169  17  TYR   A CD2 
399  C  CE1 A TYR   A 17  ? 0.2017 0.1676 0.2134 -0.0392 -0.0337 0.0501  17  TYR   A CE1 
400  C  CE1 B TYR   A 17  ? 0.1837 0.1770 0.1882 -0.0094 -0.0110 0.0294  17  TYR   A CE1 
401  C  CE2 A TYR   A 17  ? 0.2069 0.1709 0.1949 -0.0561 -0.0347 0.0443  17  TYR   A CE2 
402  C  CE2 B TYR   A 17  ? 0.1817 0.1799 0.1770 -0.0160 -0.0152 0.0183  17  TYR   A CE2 
403  C  CZ  A TYR   A 17  ? 0.2150 0.1661 0.2049 -0.0505 -0.0410 0.0511  17  TYR   A CZ  
404  C  CZ  B TYR   A 17  ? 0.1863 0.1812 0.1870 -0.0105 -0.0170 0.0285  17  TYR   A CZ  
405  O  OH  A TYR   A 17  ? 0.2320 0.1655 0.2131 -0.0495 -0.0431 0.0504  17  TYR   A OH  
406  O  OH  B TYR   A 17  ? 0.1896 0.1866 0.2024 -0.0051 -0.0177 0.0352  17  TYR   A OH  
425  N  N   A ILE   A 18  ? 0.1365 0.1323 0.1852 -0.0143 0.0169  0.0344  18  ILE   A N   
426  N  N   B ILE   A 18  ? 0.1263 0.1466 0.1317 -0.0226 0.0156  0.0225  18  ILE   A N   
427  C  CA  A ILE   A 18  ? 0.1394 0.1325 0.1775 -0.0124 0.0201  0.0220  18  ILE   A CA  
428  C  CA  B ILE   A 18  ? 0.1254 0.1450 0.1193 -0.0165 0.0211  0.0134  18  ILE   A CA  
429  C  C   A ILE   A 18  ? 0.1441 0.1424 0.1818 -0.0259 0.0158  0.0212  18  ILE   A C   
430  C  C   B ILE   A 18  ? 0.1258 0.1520 0.1036 -0.0179 0.0153  0.0158  18  ILE   A C   
431  O  O   A ILE   A 18  ? 0.1463 0.1538 0.1900 -0.0308 0.0288  0.0220  18  ILE   A O   
432  O  O   B ILE   A 18  ? 0.1242 0.1546 0.1069 -0.0181 0.0182  0.0211  18  ILE   A O   
433  C  CB  A ILE   A 18  ? 0.1415 0.1299 0.1609 0.0012  0.0225  0.0222  18  ILE   A CB  
434  C  CB  B ILE   A 18  ? 0.1313 0.1396 0.1161 -0.0048 0.0342  0.0089  18  ILE   A CB  
435  C  CG1 A ILE   A 18  ? 0.1452 0.1333 0.1574 0.0156  0.0229  0.0244  18  ILE   A CG1 
436  C  CG1 B ILE   A 18  ? 0.1434 0.1456 0.1337 -0.0040 0.0440  0.0050  18  ILE   A CG1 
437  C  CG2 A ILE   A 18  ? 0.1436 0.1327 0.1587 0.0035  0.0163  0.0153  18  ILE   A CG2 
438  C  CG2 B ILE   A 18  ? 0.1359 0.1422 0.1196 -0.0047 0.0328  0.0107  18  ILE   A CG2 
439  C  CD1 A ILE   A 18  ? 0.1698 0.1510 0.1616 0.0273  0.0255  0.0325  18  ILE   A CD1 
440  C  CD1 B ILE   A 18  ? 0.1504 0.1542 0.1555 0.0011  0.0475  -0.0026 18  ILE   A CD1 
463  N  N   A LYS   A 19  ? 0.1420 0.1446 0.1646 -0.0184 0.0225  0.0254  19  LYS   A N   
464  N  N   B LYS   A 19  ? 0.1308 0.1560 0.1001 -0.0155 0.0243  0.0051  19  LYS   A N   
465  C  CA  A LYS   A 19  ? 0.1575 0.1598 0.1656 -0.0219 0.0322  0.0244  19  LYS   A CA  
466  C  CA  B LYS   A 19  ? 0.1470 0.1710 0.1160 -0.0096 0.0324  -0.0055 19  LYS   A CA  
467  C  C   A LYS   A 19  ? 0.1485 0.1486 0.1764 -0.0113 0.0380  0.0314  19  LYS   A C   
468  C  C   B LYS   A 19  ? 0.1551 0.1760 0.1300 0.0021  0.0323  -0.0104 19  LYS   A C   
469  O  O   A LYS   A 19  ? 0.1475 0.1418 0.1762 -0.0047 0.0336  0.0345  19  LYS   A O   
470  O  O   B LYS   A 19  ? 0.1557 0.1739 0.1265 -0.0058 0.0248  -0.0139 19  LYS   A O   
471  C  CB  A LYS   A 19  ? 0.1817 0.1838 0.1721 -0.0256 0.0240  0.0120  19  LYS   A CB  
472  C  CB  B LYS   A 19  ? 0.1521 0.1799 0.1341 -0.0104 0.0345  -0.0157 19  LYS   A CB  
473  C  CG  A LYS   A 19  ? 0.2127 0.2003 0.1745 -0.0295 0.0262  0.0051  19  LYS   A CG  
474  C  CG  B LYS   A 19  ? 0.1752 0.1954 0.1481 -0.0098 0.0286  -0.0191 19  LYS   A CG  
475  C  CD  A LYS   A 19  ? 0.2389 0.2211 0.1992 -0.0370 0.0287  -0.0071 19  LYS   A CD  
476  C  CD  B LYS   A 19  ? 0.1950 0.2080 0.1607 -0.0155 0.0271  -0.0151 19  LYS   A CD  
477  C  CE  A LYS   A 19  ? 0.2604 0.2303 0.2110 -0.0480 0.0294  -0.0142 19  LYS   A CE  
478  C  CE  B LYS   A 19  ? 0.2106 0.2202 0.1756 -0.0209 0.0249  -0.0138 19  LYS   A CE  
479  N  NZ  A LYS   A 19  ? 0.2710 0.2321 0.2088 -0.0604 0.0373  -0.0230 19  LYS   A NZ  
480  N  NZ  B LYS   A 19  ? 0.2208 0.2278 0.1824 -0.0263 0.0275  -0.0165 19  LYS   A NZ  
507  N  N   A ASN   A 20  ? 0.1511 0.1549 0.2074 -0.0153 0.0341  0.0451  20  ASN   A N   
508  N  N   B ASN   A 20  ? 0.1666 0.1850 0.1588 0.0150  0.0359  -0.0166 20  ASN   A N   
509  C  CA  A ASN   A 20  ? 0.1605 0.1677 0.2351 0.0023  0.0475  0.0446  20  ASN   A CA  
510  C  CA  B ASN   A 20  ? 0.1811 0.1980 0.1989 0.0254  0.0350  -0.0097 20  ASN   A CA  
511  C  C   A ASN   A 20  ? 0.1791 0.1725 0.2465 -0.0064 0.0647  0.0267  20  ASN   A C   
512  C  C   B ASN   A 20  ? 0.1895 0.1936 0.2101 0.0240  0.0473  -0.0095 20  ASN   A C   
513  O  O   A ASN   A 20  ? 0.2028 0.1763 0.2521 -0.0177 0.0708  0.0071  20  ASN   A O   
514  O  O   B ASN   A 20  ? 0.1938 0.1902 0.2202 0.0317  0.0527  -0.0115 20  ASN   A O   
515  C  CB  A ASN   A 20  ? 0.1672 0.1776 0.2425 0.0196  0.0541  0.0638  20  ASN   A CB  
516  C  CB  B ASN   A 20  ? 0.1910 0.2138 0.2261 0.0356  0.0258  -0.0029 20  ASN   A CB  
517  C  CG  A ASN   A 20  ? 0.1792 0.1885 0.2674 0.0367  0.0663  0.0746  20  ASN   A CG  
518  C  CG  B ASN   A 20  ? 0.2042 0.2273 0.2555 0.0454  0.0158  0.0053  20  ASN   A CG  
519  O  OD1 A ASN   A 20  ? 0.2114 0.2037 0.3031 0.0550  0.0827  0.0635  20  ASN   A OD1 
520  O  OD1 B ASN   A 20  ? 0.2200 0.2347 0.2734 0.0489  0.0150  0.0078  20  ASN   A OD1 
521  N  ND2 A ASN   A 20  ? 0.1694 0.1801 0.2811 0.0326  0.0479  0.0797  20  ASN   A ND2 
522  N  ND2 B ASN   A 20  ? 0.2040 0.2297 0.2639 0.0516  0.0061  0.0089  20  ASN   A ND2 
535  N  N   A ALA   A 21  ? 0.1799 0.1744 0.2501 -0.0052 0.0599  0.0239  21  ALA   A N   
536  N  N   B ALA   A 21  ? 0.1930 0.1875 0.2121 0.0197  0.0434  -0.0086 21  ALA   A N   
537  C  CA  A ALA   A 21  ? 0.1867 0.1755 0.2427 -0.0082 0.0534  0.0318  21  ALA   A CA  
538  C  CA  B ALA   A 21  ? 0.1979 0.1820 0.2112 0.0102  0.0447  -0.0007 21  ALA   A CA  
539  C  C   A ALA   A 21  ? 0.1759 0.1740 0.2378 -0.0087 0.0460  0.0371  21  ALA   A C   
540  C  C   B ALA   A 21  ? 0.1917 0.1750 0.2003 0.0033  0.0554  0.0062  21  ALA   A C   
541  O  O   A ALA   A 21  ? 0.1764 0.1787 0.2395 0.0018  0.0388  0.0464  21  ALA   A O   
542  O  O   B ALA   A 21  ? 0.1885 0.1680 0.2039 0.0080  0.0587  0.0066  21  ALA   A O   
543  C  CB  A ALA   A 21  ? 0.2011 0.1808 0.2438 -0.0066 0.0530  0.0276  21  ALA   A CB  
544  C  CB  B ALA   A 21  ? 0.2028 0.1799 0.2240 0.0131  0.0403  -0.0035 21  ALA   A CB  
555  N  N   A ASP   A 22  ? 0.1732 0.1674 0.2438 -0.0089 0.0453  0.0329  22  ASP   A N   
556  N  N   B ASP   A 22  ? 0.1922 0.1744 0.1983 -0.0054 0.0612  0.0134  22  ASP   A N   
557  C  CA  A ASP   A 22  ? 0.1724 0.1691 0.2384 -0.0006 0.0353  0.0287  22  ASP   A CA  
558  C  CA  B ASP   A 22  ? 0.1920 0.1733 0.2015 -0.0093 0.0597  0.0141  22  ASP   A CA  
559  C  C   A ASP   A 22  ? 0.1632 0.1713 0.1967 -0.0014 0.0324  0.0217  22  ASP   A C   
560  C  C   B ASP   A 22  ? 0.1785 0.1709 0.1808 -0.0221 0.0605  0.0058  22  ASP   A C   
561  O  O   A ASP   A 22  ? 0.1705 0.1805 0.2009 -0.0048 0.0351  0.0123  22  ASP   A O   
562  O  O   B ASP   A 22  ? 0.1755 0.1732 0.1795 -0.0301 0.0577  -0.0056 22  ASP   A O   
563  C  CB  A ASP   A 22  ? 0.1900 0.1714 0.2887 -0.0004 0.0219  0.0249  22  ASP   A CB  
564  C  CB  B ASP   A 22  ? 0.2077 0.1766 0.2267 -0.0014 0.0533  0.0163  22  ASP   A CB  
565  C  CG  A ASP   A 22  ? 0.2059 0.1810 0.3420 -0.0077 -0.0015 0.0360  22  ASP   A CG  
566  C  CG  B ASP   A 22  ? 0.2195 0.1790 0.2451 0.0025  0.0466  0.0222  22  ASP   A CG  
567  O  OD1 A ASP   A 22  ? 0.2026 0.1843 0.3676 -0.0245 -0.0154 0.0501  22  ASP   A OD1 
568  O  OD1 B ASP   A 22  ? 0.2232 0.1761 0.2433 0.0024  0.0471  0.0205  22  ASP   A OD1 
569  O  OD2 A ASP   A 22  ? 0.2299 0.1922 0.3750 0.0005  -0.0012 0.0233  22  ASP   A OD2 
570  O  OD2 B ASP   A 22  ? 0.2240 0.1864 0.2634 0.0038  0.0501  0.0248  22  ASP   A OD2 
579  N  N   A ILE   A 23  ? 0.1639 0.1696 0.1816 -0.0022 0.0333  0.0185  23  ILE   A N   
580  N  N   B ILE   A 23  ? 0.1734 0.1650 0.1719 -0.0249 0.0518  0.0059  23  ILE   A N   
581  C  CA  A ILE   A 23  ? 0.1646 0.1659 0.1761 -0.0058 0.0299  0.0231  23  ILE   A CA  
582  C  CA  B ILE   A 23  ? 0.1678 0.1664 0.1542 -0.0272 0.0389  0.0108  23  ILE   A CA  
583  C  C   A ILE   A 23  ? 0.1604 0.1772 0.1753 -0.0012 0.0386  0.0160  23  ILE   A C   
584  C  C   B ILE   A 23  ? 0.1732 0.1739 0.1651 -0.0343 0.0384  0.0003  23  ILE   A C   
585  O  O   A ILE   A 23  ? 0.1705 0.1885 0.1725 -0.0003 0.0345  0.0085  23  ILE   A O   
586  O  O   B ILE   A 23  ? 0.1753 0.1683 0.1680 -0.0373 0.0391  0.0035  23  ILE   A O   
587  C  CB  A ILE   A 23  ? 0.1766 0.1633 0.1665 -0.0013 0.0262  0.0143  23  ILE   A CB  
588  C  CB  B ILE   A 23  ? 0.1642 0.1635 0.1373 -0.0171 0.0223  0.0190  23  ILE   A CB  
589  C  CG1 A ILE   A 23  ? 0.1774 0.1626 0.1537 -0.0009 0.0197  0.0175  23  ILE   A CG1 
590  C  CG1 B ILE   A 23  ? 0.1620 0.1619 0.1262 -0.0197 0.0129  0.0154  23  ILE   A CG1 
591  C  CG2 A ILE   A 23  ? 0.1834 0.1688 0.1684 0.0010  0.0277  0.0171  23  ILE   A CG2 
592  C  CG2 B ILE   A 23  ? 0.1623 0.1601 0.1313 -0.0111 0.0125  0.0234  23  ILE   A CG2 
593  C  CD1 A ILE   A 23  ? 0.1802 0.1661 0.1628 0.0003  0.0086  0.0062  23  ILE   A CD1 
594  C  CD1 B ILE   A 23  ? 0.1597 0.1636 0.1259 -0.0160 0.0045  0.0115  23  ILE   A CD1 
617  N  N   A VAL   A 24  ? 0.1702 0.1796 0.1864 -0.0110 0.0409  0.0113  24  VAL   A N   
618  N  N   B VAL   A 24  ? 0.1814 0.1851 0.1805 -0.0405 0.0350  -0.0084 24  VAL   A N   
619  C  CA  A VAL   A 24  ? 0.1868 0.1920 0.1997 -0.0219 0.0426  -0.0008 24  VAL   A CA  
620  C  CA  B VAL   A 24  ? 0.1969 0.1952 0.1962 -0.0415 0.0360  -0.0073 24  VAL   A CA  
621  C  C   A VAL   A 24  ? 0.1895 0.2110 0.1960 -0.0322 0.0369  -0.0052 24  VAL   A C   
622  C  C   B VAL   A 24  ? 0.2066 0.2105 0.2074 -0.0370 0.0339  -0.0109 24  VAL   A C   
623  O  O   A VAL   A 24  ? 0.2018 0.2178 0.1991 -0.0326 0.0429  -0.0051 24  VAL   A O   
624  O  O   B VAL   A 24  ? 0.2140 0.2152 0.2223 -0.0343 0.0355  -0.0074 24  VAL   A O   
625  C  CB  A VAL   A 24  ? 0.1945 0.1909 0.2249 -0.0178 0.0479  -0.0028 24  VAL   A CB  
626  C  CB  B VAL   A 24  ? 0.2014 0.1945 0.2033 -0.0438 0.0390  -0.0031 24  VAL   A CB  
627  C  CG1 A VAL   A 24  ? 0.2022 0.1982 0.2400 -0.0081 0.0470  -0.0144 24  VAL   A CG1 
628  C  CG1 B VAL   A 24  ? 0.2092 0.1987 0.2166 -0.0386 0.0392  -0.0031 24  VAL   A CG1 
629  C  CG2 A VAL   A 24  ? 0.2079 0.1965 0.2347 -0.0180 0.0599  0.0092  24  VAL   A CG2 
630  C  CG2 B VAL   A 24  ? 0.2011 0.1899 0.1976 -0.0520 0.0399  -0.0029 24  VAL   A CG2 
649  N  N   A GLU   A 25  ? 0.1932 0.2352 0.2010 -0.0392 0.0491  -0.0103 25  GLU   A N   
650  N  N   B GLU   A 25  ? 0.2099 0.2234 0.2064 -0.0341 0.0355  -0.0192 25  GLU   A N   
651  C  CA  A GLU   A 25  ? 0.2138 0.2610 0.2093 -0.0338 0.0563  -0.0201 25  GLU   A CA  
652  C  CA  B GLU   A 25  ? 0.2190 0.2401 0.2177 -0.0346 0.0318  -0.0183 25  GLU   A CA  
653  C  C   A GLU   A 25  ? 0.2042 0.2661 0.1819 -0.0478 0.0608  -0.0215 25  GLU   A C   
654  C  C   B GLU   A 25  ? 0.2164 0.2453 0.2072 -0.0352 0.0369  -0.0203 25  GLU   A C   
655  O  O   A GLU   A 25  ? 0.2053 0.2762 0.1915 -0.0496 0.0608  -0.0219 25  GLU   A O   
656  O  O   B GLU   A 25  ? 0.2184 0.2471 0.2130 -0.0367 0.0385  -0.0235 25  GLU   A O   
657  C  CB  A GLU   A 25  ? 0.2410 0.2895 0.2555 -0.0230 0.0542  -0.0191 25  GLU   A CB  
658  C  CB  B GLU   A 25  ? 0.2295 0.2493 0.2473 -0.0343 0.0251  -0.0181 25  GLU   A CB  
659  C  CG  A GLU   A 25  ? 0.2712 0.3155 0.3261 -0.0194 0.0352  -0.0214 25  GLU   A CG  
660  C  CG  B GLU   A 25  ? 0.2432 0.2601 0.2904 -0.0340 0.0150  -0.0172 25  GLU   A CG  
661  C  CD  A GLU   A 25  ? 0.2948 0.3382 0.3851 -0.0151 0.0173  -0.0221 25  GLU   A CD  
662  C  CD  B GLU   A 25  ? 0.2522 0.2705 0.3300 -0.0335 0.0030  -0.0151 25  GLU   A CD  
663  O  OE1 A GLU   A 25  ? 0.3051 0.3469 0.3959 -0.0095 0.0057  -0.0279 25  GLU   A OE1 
664  O  OE1 B GLU   A 25  ? 0.2581 0.2762 0.3506 -0.0327 -0.0010 -0.0139 25  GLU   A OE1 
665  O  OE2 A GLU   A 25  ? 0.3022 0.3476 0.4157 -0.0168 0.0094  -0.0262 25  GLU   A OE2 
666  O  OE2 B GLU   A 25  ? 0.2556 0.2743 0.3451 -0.0321 -0.0015 -0.0137 25  GLU   A OE2 
679  N  N   A GLU   A 26  ? 0.1948 0.2611 0.1859 -0.0640 0.0635  -0.0203 26  GLU   A N   
680  N  N   B GLU   A 26  ? 0.2117 0.2464 0.1905 -0.0366 0.0448  -0.0183 26  GLU   A N   
681  C  CA  A GLU   A 26  ? 0.2041 0.2611 0.1712 -0.0748 0.0601  -0.0132 26  GLU   A CA  
682  C  CA  B GLU   A 26  ? 0.2140 0.2482 0.1862 -0.0360 0.0410  -0.0114 26  GLU   A CA  
683  C  C   A GLU   A 26  ? 0.2008 0.2500 0.1429 -0.0753 0.0571  -0.0114 26  GLU   A C   
684  C  C   B GLU   A 26  ? 0.2148 0.2438 0.1810 -0.0327 0.0390  -0.0038 26  GLU   A C   
685  O  O   A GLU   A 26  ? 0.2129 0.2498 0.1448 -0.0850 0.0493  -0.0073 26  GLU   A O   
686  O  O   B GLU   A 26  ? 0.2165 0.2400 0.1731 -0.0374 0.0435  -0.0016 26  GLU   A O   
687  C  CB  A GLU   A 26  ? 0.2282 0.2658 0.2051 -0.0838 0.0559  -0.0008 26  GLU   A CB  
688  C  CB  B GLU   A 26  ? 0.2170 0.2508 0.1884 -0.0399 0.0303  -0.0110 26  GLU   A CB  
689  C  CG  A GLU   A 26  ? 0.2589 0.2822 0.2845 -0.0871 0.0516  -0.0080 26  GLU   A CG  
690  C  CG  B GLU   A 26  ? 0.2205 0.2534 0.1942 -0.0446 0.0284  -0.0155 26  GLU   A CG  
691  C  CD  A GLU   A 26  ? 0.2777 0.2898 0.3299 -0.0969 0.0641  -0.0111 26  GLU   A CD  
692  C  CD  B GLU   A 26  ? 0.2214 0.2534 0.1919 -0.0518 0.0272  -0.0177 26  GLU   A CD  
693  O  OE1 A GLU   A 26  ? 0.2726 0.3029 0.3258 -0.0945 0.0883  -0.0513 26  GLU   A OE1 
694  O  OE1 B GLU   A 26  ? 0.2273 0.2625 0.1913 -0.0440 0.0315  -0.0209 26  GLU   A OE1 
695  O  OE2 A GLU   A 26  ? 0.2988 0.2961 0.3631 -0.0969 0.0552  0.0041  26  GLU   A OE2 
696  O  OE2 B GLU   A 26  ? 0.2157 0.2470 0.1674 -0.0616 0.0326  -0.0214 26  GLU   A OE2 
709  N  N   A ALA   A 27  ? 0.1856 0.2375 0.1405 -0.0779 0.0547  -0.0071 27  ALA   A N   
710  N  N   B ALA   A 27  ? 0.2132 0.2430 0.1790 -0.0231 0.0348  0.0006  27  ALA   A N   
711  C  CA  A ALA   A 27  ? 0.1958 0.2448 0.1467 -0.0729 0.0475  -0.0053 27  ALA   A CA  
712  C  CA  B ALA   A 27  ? 0.2198 0.2488 0.1799 -0.0131 0.0261  0.0030  27  ALA   A CA  
713  C  C   A ALA   A 27  ? 0.2245 0.2575 0.1581 -0.0788 0.0438  -0.0187 27  ALA   A C   
714  C  C   B ALA   A 27  ? 0.2339 0.2607 0.1886 -0.0104 0.0201  -0.0031 27  ALA   A C   
715  O  O   A ALA   A 27  ? 0.2312 0.2508 0.1641 -0.0836 0.0289  -0.0076 27  ALA   A O   
716  O  O   B ALA   A 27  ? 0.2319 0.2578 0.1891 -0.0083 0.0171  0.0002  27  ALA   A O   
717  C  CB  A ALA   A 27  ? 0.1800 0.2394 0.1587 -0.0759 0.0326  -0.0067 27  ALA   A CB  
718  C  CB  B ALA   A 27  ? 0.2151 0.2456 0.1790 -0.0125 0.0241  0.0062  27  ALA   A CB  
729  N  N   A LYS   A 28  ? 0.2546 0.2791 0.1729 -0.0770 0.0380  -0.0482 28  LYS   A N   
730  N  N   B LYS   A 28  ? 0.2530 0.2755 0.2056 -0.0101 0.0126  -0.0139 28  LYS   A N   
731  C  CA  A LYS   A 28  ? 0.2882 0.3095 0.2019 -0.0709 0.0376  -0.0638 28  LYS   A CA  
732  C  CA  B LYS   A 28  ? 0.2735 0.2944 0.2310 -0.0085 0.0039  -0.0222 28  LYS   A CA  
733  C  C   A LYS   A 28  ? 0.3060 0.3350 0.1903 -0.0752 0.0542  -0.0518 28  LYS   A C   
734  C  C   B LYS   A 28  ? 0.2927 0.3125 0.2338 -0.0197 0.0131  -0.0156 28  LYS   A C   
735  O  O   A LYS   A 28  ? 0.3134 0.3407 0.2241 -0.0722 0.0356  -0.0514 28  LYS   A O   
736  O  O   B LYS   A 28  ? 0.2960 0.3122 0.2335 -0.0184 0.0076  -0.0121 28  LYS   A O   
737  C  CB  A LYS   A 28  ? 0.3050 0.3207 0.2512 -0.0568 0.0240  -0.0773 28  LYS   A CB  
738  C  CB  B LYS   A 28  ? 0.2783 0.2981 0.2637 0.0019  -0.0131 -0.0330 28  LYS   A CB  
739  C  CG  A LYS   A 28  ? 0.3211 0.3306 0.3022 -0.0461 0.0152  -0.0816 28  LYS   A CG  
740  C  CG  B LYS   A 28  ? 0.2843 0.3017 0.2972 0.0081  -0.0264 -0.0389 28  LYS   A CG  
741  C  CD  A LYS   A 28  ? 0.3362 0.3459 0.3639 -0.0366 0.0038  -0.0778 28  LYS   A CD  
742  C  CD  B LYS   A 28  ? 0.2916 0.3079 0.3307 0.0126  -0.0357 -0.0425 28  LYS   A CD  
743  C  CE  A LYS   A 28  ? 0.3474 0.3569 0.4078 -0.0298 -0.0055 -0.0788 28  LYS   A CE  
744  C  CE  B LYS   A 28  ? 0.2986 0.3130 0.3567 0.0145  -0.0411 -0.0459 28  LYS   A CE  
745  N  NZ  A LYS   A 28  ? 0.3541 0.3630 0.4385 -0.0243 -0.0076 -0.0818 28  LYS   A NZ  
746  N  NZ  B LYS   A 28  ? 0.3021 0.3158 0.3683 0.0158  -0.0467 -0.0503 28  LYS   A NZ  
773  N  N   A LYS   A 29  ? 0.3152 0.3579 0.1895 -0.0818 0.0896  -0.0301 29  LYS   A N   
774  N  N   B LYS   A 29  ? 0.3082 0.3316 0.2450 -0.0338 0.0307  -0.0092 29  LYS   A N   
775  C  CA  A LYS   A 29  ? 0.3333 0.3848 0.2187 -0.0812 0.1092  -0.0112 29  LYS   A CA  
776  C  CA  B LYS   A 29  ? 0.3248 0.3513 0.2649 -0.0462 0.0464  -0.0030 29  LYS   A CA  
777  C  C   A LYS   A 29  ? 0.3410 0.3826 0.2064 -0.0822 0.0906  0.0016  29  LYS   A C   
778  C  C   B LYS   A 29  ? 0.3313 0.3618 0.2387 -0.0671 0.0614  0.0060  29  LYS   A C   
779  O  O   A LYS   A 29  ? 0.3554 0.3950 0.2073 -0.0754 0.0869  0.0010  29  LYS   A O   
780  O  O   B LYS   A 29  ? 0.3374 0.3673 0.2484 -0.0644 0.0586  0.0063  29  LYS   A O   
781  C  CB  A LYS   A 29  ? 0.3456 0.4133 0.2732 -0.0729 0.1301  -0.0062 29  LYS   A CB  
782  C  CB  B LYS   A 29  ? 0.3329 0.3594 0.3084 -0.0367 0.0459  -0.0042 29  LYS   A CB  
783  C  CG  A LYS   A 29  ? 0.3613 0.4382 0.3349 -0.0631 0.1365  -0.0030 29  LYS   A CG  
784  C  CG  B LYS   A 29  ? 0.3404 0.3663 0.3484 -0.0282 0.0448  -0.0049 29  LYS   A CG  
785  C  CD  A LYS   A 29  ? 0.3740 0.4574 0.3949 -0.0552 0.1384  -0.0017 29  LYS   A CD  
786  C  CD  B LYS   A 29  ? 0.3456 0.3711 0.3831 -0.0214 0.0422  -0.0050 29  LYS   A CD  
787  C  CE  A LYS   A 29  ? 0.3825 0.4699 0.4361 -0.0504 0.1405  -0.0005 29  LYS   A CE  
788  C  CE  B LYS   A 29  ? 0.3493 0.3751 0.4096 -0.0167 0.0408  -0.0068 29  LYS   A CE  
789  N  NZ  A LYS   A 29  ? 0.3863 0.4765 0.4644 -0.0472 0.1383  -0.0006 29  LYS   A NZ  
790  N  NZ  B LYS   A 29  ? 0.3515 0.3784 0.4251 -0.0144 0.0387  -0.0076 29  LYS   A NZ  
817  N  N   . VAL   A 30  ? 0.3315 0.3668 0.2059 -0.0887 0.0762  0.0119  30  VAL   A N   
818  C  CA  . VAL   A 30  ? 0.3296 0.3555 0.1871 -0.1097 0.0490  0.0301  30  VAL   A CA  
819  C  C   . VAL   A 30  ? 0.3331 0.3462 0.1474 -0.1161 0.0324  0.0402  30  VAL   A C   
820  O  O   . VAL   A 30  ? 0.3434 0.3488 0.1645 -0.1140 0.0219  0.0410  30  VAL   A O   
821  C  CB  . VAL   A 30  ? 0.3266 0.3482 0.2167 -0.1241 0.0284  0.0410  30  VAL   A CB  
822  C  CG1 . VAL   A 30  ? 0.3323 0.3468 0.2308 -0.1255 0.0134  0.0451  30  VAL   A CG1 
823  C  CG2 . VAL   A 30  ? 0.3241 0.3494 0.2419 -0.1311 0.0287  0.0397  30  VAL   A CG2 
834  N  N   . LYS   A 31  ? 0.3268 0.3335 0.1405 -0.1201 0.0039  0.0294  31  LYS   A N   
835  C  CA  . LYS   A 31  ? 0.3362 0.3320 0.1614 -0.1082 -0.0181 0.0273  31  LYS   A CA  
836  C  C   . LYS   A 31  ? 0.3115 0.3109 0.1287 -0.0899 -0.0202 0.0627  31  LYS   A C   
837  O  O   . LYS   A 31  ? 0.3191 0.3250 0.1441 -0.0862 -0.0319 0.0727  31  LYS   A O   
838  C  CB  . LYS   A 31  ? 0.3773 0.3584 0.2648 -0.1048 -0.0379 -0.0019 31  LYS   A CB  
839  C  CG  . LYS   A 31  ? 0.4225 0.3872 0.3919 -0.0928 -0.0565 -0.0211 31  LYS   A CG  
840  C  CD  . LYS   A 31  ? 0.4579 0.4142 0.4875 -0.0829 -0.0735 -0.0390 31  LYS   A CD  
841  C  CE  . LYS   A 31  ? 0.4847 0.4355 0.5520 -0.0754 -0.0850 -0.0518 31  LYS   A CE  
842  N  NZ  . LYS   A 31  ? 0.4987 0.4408 0.5879 -0.0704 -0.0922 -0.0598 31  LYS   A NZ  
856  N  N   . PRO   A 32  ? 0.2722 0.2738 0.1136 -0.0846 -0.0171 0.0488  32  PRO   A N   
857  C  CA  . PRO   A 32  ? 0.2602 0.2558 0.1470 -0.0748 -0.0269 0.0570  32  PRO   A CA  
858  C  C   . PRO   A 32  ? 0.2517 0.2485 0.1540 -0.0653 -0.0337 0.0675  32  PRO   A C   
859  O  O   . PRO   A 32  ? 0.2464 0.2428 0.1689 -0.0643 -0.0481 0.0653  32  PRO   A O   
860  C  CB  . PRO   A 32  ? 0.2491 0.2565 0.1516 -0.0745 -0.0214 0.0425  32  PRO   A CB  
861  C  CG  . PRO   A 32  ? 0.2465 0.2634 0.1056 -0.0711 -0.0320 0.0277  32  PRO   A CG  
862  C  CD  . PRO   A 32  ? 0.2533 0.2666 0.1075 -0.0777 -0.0246 0.0314  32  PRO   A CD  
870  N  N   . THR   A 33  ? 0.2573 0.2463 0.1438 -0.0572 -0.0367 0.0671  33  THR   A N   
871  C  CA  . THR   A 33  ? 0.2559 0.2443 0.1546 -0.0454 -0.0440 0.0709  33  THR   A CA  
872  C  C   . THR   A 33  ? 0.2251 0.2245 0.1456 -0.0495 -0.0406 0.0536  33  THR   A C   
873  O  O   . THR   A 33  ? 0.2213 0.2239 0.1632 -0.0552 -0.0522 0.0558  33  THR   A O   
874  C  CB  . THR   A 33  ? 0.2809 0.2667 0.1714 -0.0369 -0.0512 0.0897  33  THR   A CB  
875  O  OG1 . THR   A 33  ? 0.3046 0.2827 0.1971 -0.0230 -0.0458 0.0971  33  THR   A OG1 
876  C  CG2 . THR   A 33  ? 0.2824 0.2771 0.1889 -0.0340 -0.0562 0.0824  33  THR   A CG2 
884  N  N   . VAL   A 34  ? 0.2000 0.2050 0.1270 -0.0459 -0.0301 0.0481  34  VAL   A N   
885  C  CA  . VAL   A 34  ? 0.1799 0.1845 0.1232 -0.0383 -0.0193 0.0377  34  VAL   A CA  
886  C  C   . VAL   A 34  ? 0.1668 0.1726 0.1190 -0.0330 -0.0072 0.0299  34  VAL   A C   
887  O  O   . VAL   A 34  ? 0.1672 0.1742 0.1487 -0.0350 -0.0057 0.0396  34  VAL   A O   
888  C  CB  . VAL   A 34  ? 0.1822 0.1851 0.1466 -0.0373 -0.0124 0.0308  34  VAL   A CB  
889  C  CG1 . VAL   A 34  ? 0.1855 0.1877 0.1583 -0.0363 -0.0060 0.0214  34  VAL   A CG1 
890  C  CG2 . VAL   A 34  ? 0.1895 0.1987 0.1768 -0.0264 -0.0197 0.0298  34  VAL   A CG2 
900  N  N   . VAL   A 35  ? 0.1546 0.1602 0.1224 -0.0317 -0.0084 0.0270  35  VAL   A N   
901  C  CA  . VAL   A 35  ? 0.1483 0.1566 0.1054 -0.0250 -0.0009 0.0205  35  VAL   A CA  
902  C  C   . VAL   A 35  ? 0.1377 0.1446 0.1191 -0.0219 -0.0031 0.0256  35  VAL   A C   
903  O  O   . VAL   A 35  ? 0.1293 0.1565 0.1416 -0.0279 0.0093  0.0187  35  VAL   A O   
904  C  CB  . VAL   A 35  ? 0.1501 0.1631 0.1303 -0.0183 0.0073  0.0083  35  VAL   A CB  
905  C  CG1 . VAL   A 35  ? 0.1583 0.1707 0.1401 -0.0142 0.0021  0.0055  35  VAL   A CG1 
906  C  CG2 . VAL   A 35  ? 0.1477 0.1703 0.1535 -0.0140 0.0088  0.0007  35  VAL   A CG2 
916  N  N   . VAL   A 36  ? 0.1245 0.1394 0.1139 -0.0191 0.0008  0.0259  36  VAL   A N   
917  C  CA  . VAL   A 36  ? 0.1251 0.1303 0.1150 -0.0102 0.0007  0.0129  36  VAL   A CA  
918  C  C   . VAL   A 36  ? 0.1205 0.1317 0.1203 -0.0129 0.0023  0.0153  36  VAL   A C   
919  O  O   . VAL   A 36  ? 0.1226 0.1305 0.1433 -0.0077 0.0165  0.0163  36  VAL   A O   
920  C  CB  . VAL   A 36  ? 0.1249 0.1202 0.1223 -0.0149 -0.0012 0.0194  36  VAL   A CB  
921  C  CG1 . VAL   A 36  ? 0.1304 0.1228 0.1397 -0.0165 0.0021  0.0031  36  VAL   A CG1 
922  C  CG2 . VAL   A 36  ? 0.1342 0.1306 0.1458 -0.0090 -0.0047 0.0282  36  VAL   A CG2 
932  N  N   . ASN   A 37  ? 0.1146 0.1240 0.1157 -0.0114 0.0050  0.0175  37  ASN   A N   
933  C  CA  . ASN   A 37  ? 0.1152 0.1191 0.1106 -0.0019 0.0041  0.0187  37  ASN   A CA  
934  C  C   . ASN   A 37  ? 0.1127 0.1160 0.1175 -0.0038 0.0114  0.0258  37  ASN   A C   
935  O  O   . ASN   A 37  ? 0.1253 0.1264 0.1254 0.0035  0.0136  0.0112  37  ASN   A O   
936  C  CB  . ASN   A 37  ? 0.1184 0.1220 0.1200 0.0007  0.0027  0.0127  37  ASN   A CB  
937  C  CG  . ASN   A 37  ? 0.1174 0.1178 0.1330 -0.0013 0.0055  0.0067  37  ASN   A CG  
938  O  OD1 . ASN   A 37  ? 0.1204 0.1197 0.1511 -0.0031 0.0046  0.0178  37  ASN   A OD1 
939  N  ND2 . ASN   A 37  ? 0.1204 0.1195 0.1438 -0.0044 0.0030  0.0319  37  ASN   A ND2 
946  N  N   . ALA   A 38  ? 0.1152 0.1228 0.1236 -0.0003 0.0115  0.0144  38  ALA   A N   
947  C  CA  . ALA   A 38  ? 0.1197 0.1337 0.1229 -0.0057 0.0011  0.0095  38  ALA   A CA  
948  C  C   . ALA   A 38  ? 0.1168 0.1336 0.1176 0.0000  -0.0009 0.0088  38  ALA   A C   
949  O  O   . ALA   A 38  ? 0.1238 0.1299 0.1333 0.0049  -0.0042 0.0113  38  ALA   A O   
950  C  CB  . ALA   A 38  ? 0.1256 0.1669 0.1364 -0.0182 -0.0044 0.0030  38  ALA   A CB  
956  N  N   A ALA   A 39  ? 0.1162 0.1240 0.1325 0.0003  0.0061  0.0143  39  ALA   A N   
957  N  N   B ALA   A 39  ? 0.1224 0.1328 0.1210 -0.0066 0.0011  0.0161  39  ALA   A N   
958  C  CA  A ALA   A 39  ? 0.1157 0.1210 0.1298 0.0025  0.0086  -0.0033 39  ALA   A CA  
959  C  CA  B ALA   A 39  ? 0.1291 0.1363 0.1203 -0.0108 0.0034  0.0187  39  ALA   A CA  
960  C  C   A ALA   A 39  ? 0.1180 0.1219 0.1384 0.0035  0.0004  -0.0021 39  ALA   A C   
961  C  C   B ALA   A 39  ? 0.1267 0.1293 0.1138 -0.0111 0.0079  0.0212  39  ALA   A C   
962  O  O   A ALA   A 39  ? 0.1283 0.1234 0.1365 0.0062  -0.0035 0.0021  39  ALA   A O   
963  O  O   B ALA   A 39  ? 0.1248 0.1245 0.1091 -0.0197 0.0122  0.0264  39  ALA   A O   
964  C  CB  A ALA   A 39  ? 0.1173 0.1316 0.1463 0.0017  -0.0102 -0.0087 39  ALA   A CB  
965  C  CB  B ALA   A 39  ? 0.1364 0.1482 0.1330 -0.0106 -0.0060 0.0146  39  ALA   A CB  
976  N  N   A ASN   A 40  ? 0.1207 0.1257 0.1458 -0.0067 0.0196  -0.0004 40  ASN   A N   
977  N  N   B ASN   A 40  ? 0.1296 0.1272 0.1131 -0.0071 0.0170  0.0245  40  ASN   A N   
978  C  CA  A ASN   A 40  ? 0.1275 0.1226 0.1385 0.0004  0.0094  0.0028  40  ASN   A CA  
979  C  CA  B ASN   A 40  ? 0.1339 0.1243 0.1225 0.0021  0.0115  0.0215  40  ASN   A CA  
980  C  C   A ASN   A 40  ? 0.1286 0.1144 0.1132 -0.0061 0.0123  0.0147  40  ASN   A C   
981  C  C   B ASN   A 40  ? 0.1337 0.1202 0.1153 0.0019  0.0152  0.0264  40  ASN   A C   
982  O  O   A ASN   A 40  ? 0.1244 0.1195 0.1160 -0.0099 0.0115  0.0143  40  ASN   A O   
983  O  O   B ASN   A 40  ? 0.1332 0.1223 0.1221 0.0028  0.0149  0.0216  40  ASN   A O   
984  C  CB  A ASN   A 40  ? 0.1413 0.1305 0.1447 0.0028  -0.0021 0.0058  40  ASN   A CB  
985  C  CB  B ASN   A 40  ? 0.1445 0.1290 0.1361 0.0050  0.0136  0.0190  40  ASN   A CB  
986  C  CG  A ASN   A 40  ? 0.1527 0.1288 0.1638 -0.0013 -0.0073 0.0131  40  ASN   A CG  
987  C  CG  B ASN   A 40  ? 0.1500 0.1337 0.1553 0.0042  0.0208  0.0182  40  ASN   A CG  
988  O  OD1 A ASN   A 40  ? 0.1633 0.1242 0.1985 0.0000  -0.0087 0.0102  40  ASN   A OD1 
989  O  OD1 B ASN   A 40  ? 0.1545 0.1356 0.1599 0.0009  0.0277  0.0209  40  ASN   A OD1 
990  N  ND2 A ASN   A 40  ? 0.1554 0.1405 0.1519 -0.0013 -0.0024 -0.0074 40  ASN   A ND2 
991  N  ND2 B ASN   A 40  ? 0.1513 0.1438 0.1632 0.0037  0.0290  0.0051  40  ASN   A ND2 
1004 N  N   A VAL   A 41  ? 0.1296 0.1202 0.1191 -0.0013 0.0128  0.0158  41  VAL   A N   
1005 N  N   B VAL   A 41  ? 0.1347 0.1212 0.1072 0.0037  0.0134  0.0287  41  VAL   A N   
1006 C  CA  A VAL   A 41  ? 0.1300 0.1261 0.1340 0.0010  0.0154  0.0164  41  VAL   A CA  
1007 C  CA  B VAL   A 41  ? 0.1369 0.1273 0.1182 0.0047  0.0248  0.0260  41  VAL   A CA  
1008 C  C   A VAL   A 41  ? 0.1301 0.1234 0.1413 0.0024  0.0171  0.0183  41  VAL   A C   
1009 C  C   B VAL   A 41  ? 0.1380 0.1280 0.1206 -0.0006 0.0301  0.0199  41  VAL   A C   
1010 O  O   A VAL   A 41  ? 0.1388 0.1185 0.1458 0.0025  0.0056  0.0087  41  VAL   A O   
1011 O  O   B VAL   A 41  ? 0.1414 0.1213 0.1125 -0.0037 0.0233  0.0111  41  VAL   A O   
1012 C  CB  A VAL   A 41  ? 0.1370 0.1331 0.1380 -0.0021 0.0214  0.0150  41  VAL   A CB  
1013 C  CB  B VAL   A 41  ? 0.1388 0.1344 0.1307 0.0080  0.0293  0.0311  41  VAL   A CB  
1014 C  CG1 A VAL   A 41  ? 0.1450 0.1422 0.1497 -0.0006 0.0123  0.0145  41  VAL   A CG1 
1015 C  CG1 B VAL   A 41  ? 0.1504 0.1359 0.1395 0.0056  0.0333  0.0234  41  VAL   A CG1 
1016 C  CG2 A VAL   A 41  ? 0.1474 0.1357 0.1229 -0.0056 0.0335  0.0056  41  VAL   A CG2 
1017 C  CG2 B VAL   A 41  ? 0.1368 0.1427 0.1398 0.0112  0.0214  0.0335  41  VAL   A CG2 
1036 N  N   A TYR   A 42  ? 0.1227 0.1217 0.1611 -0.0026 0.0238  0.0243  42  TYR   A N   
1037 N  N   B TYR   A 42  ? 0.1342 0.1298 0.1298 0.0013  0.0313  0.0270  42  TYR   A N   
1038 C  CA  A TYR   A 42  ? 0.1295 0.1195 0.1643 -0.0095 0.0320  0.0227  42  TYR   A CA  
1039 C  CA  B TYR   A 42  ? 0.1401 0.1308 0.1406 0.0017  0.0294  0.0257  42  TYR   A CA  
1040 C  C   A TYR   A 42  ? 0.1246 0.1146 0.1643 -0.0065 0.0256  0.0248  42  TYR   A C   
1041 C  C   B TYR   A 42  ? 0.1352 0.1266 0.1420 -0.0013 0.0257  0.0273  42  TYR   A C   
1042 O  O   A TYR   A 42  ? 0.1275 0.1168 0.1869 -0.0179 0.0169  0.0070  42  TYR   A O   
1043 O  O   B TYR   A 42  ? 0.1366 0.1322 0.1452 -0.0058 0.0246  0.0300  42  TYR   A O   
1044 C  CB  A TYR   A 42  ? 0.1521 0.1274 0.1560 -0.0078 0.0407  0.0349  42  TYR   A CB  
1045 C  CB  B TYR   A 42  ? 0.1544 0.1359 0.1447 0.0071  0.0213  0.0290  42  TYR   A CB  
1046 C  CG  A TYR   A 42  ? 0.1664 0.1366 0.1595 -0.0075 0.0332  0.0388  42  TYR   A CG  
1047 C  CG  B TYR   A 42  ? 0.1653 0.1415 0.1494 0.0131  0.0093  0.0274  42  TYR   A CG  
1048 C  CD1 A TYR   A 42  ? 0.1738 0.1487 0.1690 -0.0170 0.0353  0.0332  42  TYR   A CD1 
1049 C  CD1 B TYR   A 42  ? 0.1684 0.1450 0.1486 0.0104  0.0069  0.0292  42  TYR   A CD1 
1050 C  CD2 A TYR   A 42  ? 0.1775 0.1550 0.1785 -0.0025 0.0221  0.0290  42  TYR   A CD2 
1051 C  CD2 B TYR   A 42  ? 0.1738 0.1514 0.1588 0.0162  0.0041  0.0228  42  TYR   A CD2 
1052 C  CE1 A TYR   A 42  ? 0.1837 0.1575 0.1675 -0.0146 0.0285  0.0247  42  TYR   A CE1 
1053 C  CE1 B TYR   A 42  ? 0.1722 0.1512 0.1512 0.0110  0.0089  0.0258  42  TYR   A CE1 
1054 C  CE2 A TYR   A 42  ? 0.1894 0.1687 0.1895 -0.0062 0.0185  0.0276  42  TYR   A CE2 
1055 C  CE2 B TYR   A 42  ? 0.1801 0.1574 0.1605 0.0165  0.0087  0.0215  42  TYR   A CE2 
1056 C  CZ  A TYR   A 42  ? 0.1943 0.1690 0.1740 -0.0170 0.0314  0.0268  42  TYR   A CZ  
1057 C  CZ  B TYR   A 42  ? 0.1785 0.1592 0.1564 0.0106  0.0133  0.0207  42  TYR   A CZ  
1058 O  OH  A TYR   A 42  ? 0.2052 0.1822 0.1965 -0.0188 0.0214  0.0168  42  TYR   A OH  
1059 O  OH  B TYR   A 42  ? 0.1801 0.1683 0.1650 0.0055  0.0202  0.0167  42  TYR   A OH  
1078 N  N   . LEU   A 43  ? 0.1276 0.1187 0.1493 -0.0054 0.0199  0.0092  43  LEU   A N   
1079 C  CA  . LEU   A 43  ? 0.1185 0.1214 0.1484 -0.0061 0.0172  0.0046  43  LEU   A CA  
1080 C  C   . LEU   A 43  ? 0.1214 0.1240 0.1478 -0.0052 0.0082  0.0042  43  LEU   A C   
1081 O  O   . LEU   A 43  ? 0.1375 0.1261 0.1725 -0.0016 -0.0071 0.0003  43  LEU   A O   
1082 C  CB  . LEU   A 43  ? 0.1228 0.1207 0.1558 -0.0072 0.0087  0.0123  43  LEU   A CB  
1083 C  CG  . LEU   A 43  ? 0.1305 0.1247 0.1607 -0.0066 0.0077  0.0118  43  LEU   A CG  
1084 C  CD1 . LEU   A 43  ? 0.1412 0.1343 0.1776 -0.0043 -0.0098 0.0156  43  LEU   A CD1 
1085 C  CD2 . LEU   A 43  ? 0.1469 0.1204 0.1610 -0.0075 0.0072  0.0155  43  LEU   A CD2 
1098 N  N   A LYS   A 44  ? 0.1293 0.1191 0.1476 -0.0042 0.0065  0.0088  44  LYS   A N   
1099 N  N   B LYS   A 44  ? 0.1309 0.1267 0.1513 -0.0055 0.0059  0.0099  44  LYS   A N   
1100 C  CA  A LYS   A 44  ? 0.1396 0.1213 0.1434 -0.0034 0.0146  0.0126  44  LYS   A CA  
1101 C  CA  B LYS   A 44  ? 0.1405 0.1307 0.1568 -0.0056 0.0071  0.0137  44  LYS   A CA  
1102 C  C   A LYS   A 44  ? 0.1301 0.1255 0.1206 0.0022  0.0032  0.0136  44  LYS   A C   
1103 C  C   B LYS   A 44  ? 0.1299 0.1271 0.1378 -0.0056 0.0055  0.0165  44  LYS   A C   
1104 O  O   A LYS   A 44  ? 0.1401 0.1403 0.1468 0.0058  0.0013  -0.0056 44  LYS   A O   
1105 O  O   B LYS   A 44  ? 0.1301 0.1280 0.1406 -0.0096 0.0124  0.0154  44  LYS   A O   
1106 C  CB  A LYS   A 44  ? 0.1702 0.1390 0.1824 -0.0025 0.0318  0.0357  44  LYS   A CB  
1107 C  CB  B LYS   A 44  ? 0.1631 0.1454 0.1924 -0.0010 0.0136  0.0215  44  LYS   A CB  
1108 C  CG  A LYS   A 44  ? 0.1992 0.1655 0.2456 -0.0054 0.0506  0.0489  44  LYS   A CG  
1109 C  CG  B LYS   A 44  ? 0.1816 0.1642 0.2387 0.0025  0.0172  0.0281  44  LYS   A CG  
1110 C  CD  A LYS   A 44  ? 0.2273 0.2183 0.3390 -0.0038 0.0413  0.0386  44  LYS   A CD  
1111 C  CD  B LYS   A 44  ? 0.1981 0.1876 0.2894 0.0029  0.0087  0.0273  44  LYS   A CD  
1112 C  CE  A LYS   A 44  ? 0.2406 0.2471 0.3985 -0.0025 0.0394  0.0335  44  LYS   A CE  
1113 C  CE  B LYS   A 44  ? 0.2056 0.2051 0.3212 0.0012  0.0028  0.0317  44  LYS   A CE  
1114 N  NZ  A LYS   A 44  ? 0.2454 0.2636 0.4250 -0.0024 0.0341  0.0311  44  LYS   A NZ  
1115 N  NZ  B LYS   A 44  ? 0.2130 0.2185 0.3425 -0.0038 0.0016  0.0327  44  LYS   A NZ  
1142 N  N   . HIS   A 45  ? 0.1228 0.1217 0.1365 -0.0041 0.0011  0.0174  45  HIS   A N   
1143 C  CA  . HIS   A 45  ? 0.1220 0.1210 0.1476 -0.0053 -0.0041 0.0091  45  HIS   A CA  
1144 C  C   . HIS   A 45  ? 0.1281 0.1314 0.1565 0.0046  0.0007  0.0136  45  HIS   A C   
1145 O  O   . HIS   A 45  ? 0.1482 0.1501 0.1856 0.0248  -0.0071 -0.0061 45  HIS   A O   
1146 C  CB  . HIS   A 45  ? 0.1235 0.1200 0.1409 -0.0041 0.0005  0.0073  45  HIS   A CB  
1147 C  CG  . HIS   A 45  ? 0.1171 0.1200 0.1355 -0.0077 0.0047  0.0096  45  HIS   A CG  
1148 N  ND1 . HIS   A 45  ? 0.1134 0.1269 0.1462 -0.0033 -0.0040 0.0158  45  HIS   A ND1 
1149 C  CD2 . HIS   A 45  ? 0.1172 0.1247 0.1395 -0.0111 -0.0002 0.0219  45  HIS   A CD2 
1150 C  CE1 . HIS   A 45  ? 0.1149 0.1338 0.1300 -0.0070 -0.0026 0.0220  45  HIS   A CE1 
1151 N  NE2 . HIS   A 45  ? 0.1133 0.1359 0.1376 -0.0068 0.0013  0.0225  45  HIS   A NE2 
1160 N  N   A GLY   A 46  ? 0.1437 0.1385 0.1728 0.0103  -0.0109 0.0188  46  GLY   A N   
1161 N  N   B GLY   A 46  ? 0.1324 0.1377 0.1607 0.0138  -0.0160 0.0163  46  GLY   A N   
1162 C  CA  A GLY   A 46  ? 0.1464 0.1465 0.1892 0.0089  -0.0097 0.0183  46  GLY   A CA  
1163 C  CA  B GLY   A 46  ? 0.1361 0.1382 0.1654 0.0179  -0.0255 0.0194  46  GLY   A CA  
1164 C  C   A GLY   A 46  ? 0.1485 0.1426 0.1955 0.0136  -0.0110 0.0248  46  GLY   A C   
1165 C  C   B GLY   A 46  ? 0.1393 0.1303 0.1662 0.0233  -0.0318 0.0230  46  GLY   A C   
1166 O  O   A GLY   A 46  ? 0.1517 0.1493 0.2175 0.0068  -0.0188 0.0159  46  GLY   A O   
1167 O  O   B GLY   A 46  ? 0.1469 0.1221 0.1864 0.0265  -0.0332 0.0288  46  GLY   A O   
1174 N  N   A GLY   A 47  ? 0.1536 0.1388 0.1861 0.0122  -0.0172 0.0071  47  GLY   A N   
1175 N  N   B GLY   A 47  ? 0.1330 0.1320 0.1524 0.0219  -0.0387 0.0130  47  GLY   A N   
1176 C  CA  A GLY   A 47  ? 0.1534 0.1435 0.1777 0.0154  -0.0380 -0.0113 47  GLY   A CA  
1177 C  CA  B GLY   A 47  ? 0.1351 0.1396 0.1512 0.0167  -0.0520 0.0065  47  GLY   A CA  
1178 C  C   A GLY   A 47  ? 0.1441 0.1331 0.1776 0.0138  -0.0418 -0.0138 47  GLY   A C   
1179 C  C   B GLY   A 47  ? 0.1343 0.1456 0.1509 0.0140  -0.0384 -0.0051 47  GLY   A C   
1180 O  O   A GLY   A 47  ? 0.1409 0.1298 0.1792 0.0155  -0.0359 0.0027  47  GLY   A O   
1181 O  O   B GLY   A 47  ? 0.1333 0.1483 0.1594 0.0191  -0.0301 0.0062  47  GLY   A O   
1188 N  N   A GLY   A 48  ? 0.1413 0.1359 0.1756 0.0151  -0.0569 -0.0116 48  GLY   A N   
1189 N  N   B GLY   A 48  ? 0.1374 0.1496 0.1594 0.0065  -0.0348 -0.0132 48  GLY   A N   
1190 C  CA  A GLY   A 48  ? 0.1377 0.1323 0.1991 0.0072  -0.0484 -0.0091 48  GLY   A CA  
1191 C  CA  B GLY   A 48  ? 0.1347 0.1474 0.1635 0.0060  -0.0191 -0.0185 48  GLY   A CA  
1192 C  C   A GLY   A 48  ? 0.1252 0.1321 0.1883 -0.0009 -0.0203 -0.0040 48  GLY   A C   
1193 C  C   B GLY   A 48  ? 0.1278 0.1459 0.1577 0.0064  0.0016  -0.0126 48  GLY   A C   
1194 O  O   A GLY   A 48  ? 0.1449 0.1309 0.1878 0.0030  -0.0160 -0.0030 48  GLY   A O   
1195 O  O   B GLY   A 48  ? 0.1398 0.1471 0.1614 0.0058  0.0062  -0.0164 48  GLY   A O   
1202 N  N   A VAL   A 49  ? 0.1108 0.1254 0.1916 -0.0072 -0.0059 -0.0026 49  VAL   A N   
1203 N  N   B VAL   A 49  ? 0.1159 0.1392 0.1552 0.0021  0.0073  -0.0087 49  VAL   A N   
1204 C  CA  A VAL   A 49  ? 0.1311 0.1238 0.1776 -0.0059 0.0158  -0.0025 49  VAL   A CA  
1205 C  CA  B VAL   A 49  ? 0.1115 0.1331 0.1399 -0.0038 0.0150  -0.0027 49  VAL   A CA  
1206 C  C   A VAL   A 49  ? 0.1298 0.1139 0.1447 0.0023  0.0150  0.0048  49  VAL   A C   
1207 C  C   B VAL   A 49  ? 0.1100 0.1234 0.1248 0.0004  0.0148  -0.0043 49  VAL   A C   
1208 O  O   A VAL   A 49  ? 0.1395 0.1200 0.1504 -0.0018 0.0216  0.0019  49  VAL   A O   
1209 O  O   B VAL   A 49  ? 0.1079 0.1183 0.1325 0.0030  0.0170  -0.0071 49  VAL   A O   
1210 C  CB  A VAL   A 49  ? 0.1489 0.1299 0.1809 -0.0094 0.0275  -0.0141 49  VAL   A CB  
1211 C  CB  B VAL   A 49  ? 0.1050 0.1270 0.1335 -0.0006 0.0134  -0.0080 49  VAL   A CB  
1212 C  CG1 A VAL   A 49  ? 0.1583 0.1177 0.1820 0.0009  0.0335  -0.0134 49  VAL   A CG1 
1213 C  CG1 B VAL   A 49  ? 0.1049 0.1235 0.1312 0.0086  0.0164  -0.0067 49  VAL   A CG1 
1214 C  CG2 A VAL   A 49  ? 0.1593 0.1389 0.2241 -0.0274 0.0320  -0.0110 49  VAL   A CG2 
1215 C  CG2 B VAL   A 49  ? 0.1027 0.1264 0.1221 -0.0037 0.0273  -0.0067 49  VAL   A CG2 
1234 N  N   A ALA   A 50  ? 0.1214 0.1119 0.1399 -0.0022 -0.0059 0.0091  50  ALA   A N   
1235 N  N   B ALA   A 50  ? 0.1140 0.1212 0.1109 0.0030  0.0084  -0.0041 50  ALA   A N   
1236 C  CA  A ALA   A 50  ? 0.1146 0.1133 0.1340 -0.0125 -0.0018 0.0131  50  ALA   A CA  
1237 C  CA  B ALA   A 50  ? 0.1185 0.1218 0.1076 -0.0002 -0.0014 -0.0029 50  ALA   A CA  
1238 C  C   A ALA   A 50  ? 0.1129 0.1167 0.1281 -0.0112 -0.0027 0.0083  50  ALA   A C   
1239 C  C   B ALA   A 50  ? 0.1216 0.1244 0.1065 0.0029  0.0042  -0.0014 50  ALA   A C   
1240 O  O   A ALA   A 50  ? 0.1141 0.1185 0.1496 -0.0058 -0.0070 0.0049  50  ALA   A O   
1241 O  O   B ALA   A 50  ? 0.1219 0.1265 0.1087 0.0088  0.0121  0.0046  50  ALA   A O   
1242 C  CB  A ALA   A 50  ? 0.1156 0.1178 0.1207 -0.0114 -0.0099 0.0024  50  ALA   A CB  
1243 C  CB  B ALA   A 50  ? 0.1254 0.1206 0.1087 0.0015  -0.0031 -0.0101 50  ALA   A CB  
1254 N  N   A GLY   A 51  ? 0.1201 0.1076 0.1361 0.0023  -0.0103 0.0095  51  GLY   A N   
1255 N  N   B GLY   A 51  ? 0.1250 0.1241 0.1192 0.0045  -0.0057 -0.0038 51  GLY   A N   
1256 C  CA  A GLY   A 51  ? 0.1341 0.1080 0.1431 0.0041  -0.0142 0.0101  51  GLY   A CA  
1257 C  CA  B GLY   A 51  ? 0.1296 0.1258 0.1252 0.0024  -0.0118 -0.0056 51  GLY   A CA  
1258 C  C   A GLY   A 51  ? 0.1217 0.1231 0.1406 0.0042  -0.0099 -0.0004 51  GLY   A C   
1259 C  C   B GLY   A 51  ? 0.1240 0.1315 0.1295 0.0007  -0.0124 -0.0096 51  GLY   A C   
1260 O  O   A GLY   A 51  ? 0.1234 0.1308 0.1576 0.0034  -0.0074 -0.0075 51  GLY   A O   
1261 O  O   B GLY   A 51  ? 0.1260 0.1351 0.1342 -0.0011 -0.0174 -0.0143 51  GLY   A O   
1268 N  N   . ALA   A 52  ? 0.1214 0.1348 0.1374 -0.0014 -0.0067 -0.0137 52  ALA   A N   
1269 C  CA  . ALA   A 52  ? 0.1247 0.1443 0.1540 -0.0001 0.0052  -0.0164 52  ALA   A CA  
1270 C  C   . ALA   A 52  ? 0.1190 0.1404 0.1373 -0.0101 0.0086  -0.0090 52  ALA   A C   
1271 O  O   . ALA   A 52  ? 0.1304 0.1456 0.1541 -0.0092 0.0084  -0.0117 52  ALA   A O   
1272 C  CB  . ALA   A 52  ? 0.1338 0.1678 0.1727 -0.0088 -0.0016 -0.0035 52  ALA   A CB  
1279 N  N   . LEU   A 53  ? 0.1140 0.1367 0.1306 -0.0085 0.0072  -0.0051 53  LEU   A N   
1280 C  CA  . LEU   A 53  ? 0.1325 0.1405 0.1335 -0.0039 0.0061  0.0042  53  LEU   A CA  
1281 C  C   . LEU   A 53  ? 0.1306 0.1441 0.1085 0.0043  0.0028  -0.0006 53  LEU   A C   
1282 O  O   . LEU   A 53  ? 0.1427 0.1546 0.1255 -0.0125 0.0040  0.0025  53  LEU   A O   
1283 C  CB  . LEU   A 53  ? 0.1375 0.1407 0.1388 -0.0093 0.0090  0.0030  53  LEU   A CB  
1284 C  CG  . LEU   A 53  ? 0.1579 0.1397 0.1470 -0.0164 0.0025  0.0083  53  LEU   A CG  
1285 C  CD1 . LEU   A 53  ? 0.1723 0.1518 0.1553 -0.0100 0.0038  0.0072  53  LEU   A CD1 
1286 C  CD2 . LEU   A 53  ? 0.1871 0.1521 0.1585 -0.0257 0.0123  0.0080  53  LEU   A CD2 
1298 N  N   . ASN   A 54  ? 0.1251 0.1356 0.1120 -0.0010 -0.0004 0.0063  54  ASN   A N   
1299 C  CA  . ASN   A 54  ? 0.1151 0.1308 0.1332 -0.0028 -0.0041 0.0044  54  ASN   A CA  
1300 C  C   . ASN   A 54  ? 0.1211 0.1273 0.1326 -0.0078 0.0050  -0.0014 54  ASN   A C   
1301 O  O   . ASN   A 54  ? 0.1243 0.1378 0.1473 -0.0047 -0.0023 -0.0131 54  ASN   A O   
1302 C  CB  . ASN   A 54  ? 0.1077 0.1293 0.1403 -0.0060 -0.0109 0.0021  54  ASN   A CB  
1303 C  CG  . ASN   A 54  ? 0.1149 0.1318 0.1444 -0.0003 -0.0049 0.0013  54  ASN   A CG  
1304 O  OD1 . ASN   A 54  ? 0.1179 0.1338 0.1399 -0.0036 -0.0073 0.0003  54  ASN   A OD1 
1305 N  ND2 . ASN   A 54  ? 0.1260 0.1342 0.1604 -0.0111 -0.0121 0.0131  54  ASN   A ND2 
1312 N  N   . LYS   A 55  ? 0.1237 0.1316 0.1435 -0.0023 -0.0016 -0.0092 55  LYS   A N   
1313 C  CA  . LYS   A 55  ? 0.1332 0.1446 0.1453 0.0068  -0.0030 -0.0185 55  LYS   A CA  
1314 C  C   . LYS   A 55  ? 0.1346 0.1473 0.1482 -0.0028 0.0023  -0.0256 55  LYS   A C   
1315 O  O   . LYS   A 55  ? 0.1416 0.1575 0.1612 0.0006  -0.0013 -0.0248 55  LYS   A O   
1316 C  CB  . LYS   A 55  ? 0.1362 0.1538 0.1594 0.0134  -0.0056 -0.0195 55  LYS   A CB  
1317 C  CG  . LYS   A 55  ? 0.1537 0.1812 0.1888 0.0237  -0.0194 -0.0248 55  LYS   A CG  
1318 C  CD  . LYS   A 55  ? 0.1705 0.2085 0.2008 0.0354  -0.0165 -0.0227 55  LYS   A CD  
1319 C  CE  . LYS   A 55  ? 0.1912 0.2379 0.2236 0.0490  -0.0253 -0.0249 55  LYS   A CE  
1320 N  NZ  . LYS   A 55  ? 0.1979 0.2507 0.2333 0.0591  -0.0304 -0.0243 55  LYS   A NZ  
1334 N  N   . ALA   A 56  ? 0.1371 0.1539 0.1465 -0.0069 0.0023  -0.0252 56  ALA   A N   
1335 C  CA  . ALA   A 56  ? 0.1423 0.1733 0.1446 -0.0114 0.0127  -0.0227 56  ALA   A CA  
1336 C  C   . ALA   A 56  ? 0.1505 0.1859 0.1299 -0.0122 0.0088  -0.0214 56  ALA   A C   
1337 O  O   . ALA   A 56  ? 0.1555 0.2176 0.1424 0.0016  0.0141  -0.0179 56  ALA   A O   
1338 C  CB  . ALA   A 56  ? 0.1497 0.1921 0.1592 -0.0191 0.0149  -0.0114 56  ALA   A CB  
1344 N  N   . THR   A 57  ? 0.1350 0.1688 0.1335 -0.0168 0.0095  -0.0213 57  THR   A N   
1345 C  CA  . THR   A 57  ? 0.1424 0.1636 0.1315 -0.0158 0.0004  -0.0129 57  THR   A CA  
1346 C  C   . THR   A 57  ? 0.1411 0.1717 0.1369 -0.0075 -0.0066 -0.0160 57  THR   A C   
1347 O  O   . THR   A 57  ? 0.1358 0.1770 0.1602 -0.0140 -0.0089 -0.0268 57  THR   A O   
1348 C  CB  . THR   A 57  ? 0.1366 0.1634 0.1373 -0.0103 0.0075  -0.0108 57  THR   A CB  
1349 O  OG1 . THR   A 57  ? 0.1247 0.1563 0.1369 -0.0083 0.0006  -0.0096 57  THR   A OG1 
1350 C  CG2 . THR   A 57  ? 0.1446 0.1613 0.1291 -0.0102 0.0062  -0.0024 57  THR   A CG2 
1358 N  N   . ASN   A 58  ? 0.1411 0.1669 0.1602 -0.0101 0.0028  -0.0300 58  ASN   A N   
1359 C  CA  . ASN   A 58  ? 0.1606 0.1579 0.1815 -0.0130 0.0087  -0.0416 58  ASN   A CA  
1360 C  C   . ASN   A 58  ? 0.1388 0.1486 0.1723 -0.0054 -0.0032 -0.0257 58  ASN   A C   
1361 O  O   . ASN   A 58  ? 0.1399 0.1603 0.1890 -0.0184 -0.0048 -0.0283 58  ASN   A O   
1362 C  CB  . ASN   A 58  ? 0.2080 0.1762 0.2241 -0.0192 0.0354  -0.0571 58  ASN   A CB  
1363 C  CG  . ASN   A 58  ? 0.2466 0.1995 0.2961 -0.0180 0.0373  -0.0421 58  ASN   A CG  
1364 O  OD1 . ASN   A 58  ? 0.2702 0.1991 0.3299 0.0153  0.0664  -0.0292 58  ASN   A OD1 
1365 N  ND2 . ASN   A 58  ? 0.2549 0.2093 0.3205 -0.0258 0.0246  -0.0450 58  ASN   A ND2 
1372 N  N   . ASN   A 59  ? 0.1261 0.1407 0.1577 -0.0060 -0.0135 -0.0131 59  ASN   A N   
1373 C  CA  . ASN   A 59  ? 0.1291 0.1317 0.1587 -0.0022 -0.0056 -0.0123 59  ASN   A CA  
1374 C  C   . ASN   A 59  ? 0.1268 0.1382 0.1432 -0.0063 -0.0079 -0.0091 59  ASN   A C   
1375 O  O   . ASN   A 59  ? 0.1259 0.1332 0.1529 -0.0076 -0.0003 0.0026  59  ASN   A O   
1376 C  CB  . ASN   A 59  ? 0.1358 0.1299 0.1658 -0.0010 -0.0181 -0.0118 59  ASN   A CB  
1377 C  CG  . ASN   A 59  ? 0.1376 0.1360 0.1625 -0.0019 -0.0294 -0.0015 59  ASN   A CG  
1378 O  OD1 . ASN   A 59  ? 0.1471 0.1414 0.1561 -0.0101 -0.0256 0.0081  59  ASN   A OD1 
1379 N  ND2 . ASN   A 59  ? 0.1445 0.1384 0.1715 -0.0156 -0.0161 0.0045  59  ASN   A ND2 
1386 N  N   . ALA   A 60  ? 0.1215 0.1416 0.1458 -0.0072 -0.0069 -0.0079 60  ALA   A N   
1387 C  CA  . ALA   A 60  ? 0.1234 0.1415 0.1513 -0.0046 -0.0136 -0.0011 60  ALA   A CA  
1388 C  C   . ALA   A 60  ? 0.1277 0.1317 0.1502 -0.0042 -0.0062 -0.0014 60  ALA   A C   
1389 O  O   . ALA   A 60  ? 0.1200 0.1326 0.1772 -0.0033 -0.0085 -0.0051 60  ALA   A O   
1390 C  CB  . ALA   A 60  ? 0.1321 0.1544 0.1528 -0.0042 -0.0178 -0.0148 60  ALA   A CB  
1396 N  N   . MET   A 61  ? 0.1238 0.1279 0.1430 -0.0099 -0.0031 -0.0001 61  MET   A N   
1397 C  CA  . MET   A 61  ? 0.1213 0.1262 0.1359 -0.0057 0.0029  0.0025  61  MET   A CA  
1398 C  C   . MET   A 61  ? 0.1165 0.1237 0.1507 -0.0052 -0.0034 -0.0039 61  MET   A C   
1399 O  O   . MET   A 61  ? 0.1191 0.1262 0.1609 -0.0034 0.0063  0.0033  61  MET   A O   
1400 C  CB  . MET   A 61  ? 0.1266 0.1297 0.1304 -0.0101 0.0003  0.0022  61  MET   A CB  
1401 C  CG  . MET   A 61  ? 0.1279 0.1380 0.1552 -0.0053 -0.0009 0.0015  61  MET   A CG  
1402 S  SD  . MET   A 61  ? 0.1299 0.1369 0.1794 -0.0116 -0.0022 -0.0163 61  MET   A SD  
1403 C  CE  . MET   A 61  ? 0.1496 0.1429 0.2131 -0.0156 0.0150  -0.0099 61  MET   A CE  
1413 N  N   . GLN   A 62  ? 0.1155 0.1205 0.1504 -0.0108 -0.0073 -0.0076 62  GLN   A N   
1414 C  CA  . GLN   A 62  ? 0.1216 0.1194 0.1569 -0.0050 0.0015  0.0039  62  GLN   A CA  
1415 C  C   . GLN   A 62  ? 0.1212 0.1120 0.1639 -0.0009 0.0078  -0.0018 62  GLN   A C   
1416 O  O   . GLN   A 62  ? 0.1255 0.1236 0.1575 -0.0007 0.0030  -0.0016 62  GLN   A O   
1417 C  CB  . GLN   A 62  ? 0.1212 0.1184 0.1580 -0.0050 0.0057  0.0058  62  GLN   A CB  
1418 C  CG  . GLN   A 62  ? 0.1260 0.1174 0.1485 -0.0079 0.0025  0.0139  62  GLN   A CG  
1419 C  CD  . GLN   A 62  ? 0.1310 0.1207 0.1464 -0.0066 0.0093  0.0135  62  GLN   A CD  
1420 O  OE1 . GLN   A 62  ? 0.1361 0.1330 0.1628 -0.0073 0.0009  0.0033  62  GLN   A OE1 
1421 N  NE2 . GLN   A 62  ? 0.1359 0.1273 0.1581 0.0037  0.0071  -0.0029 62  GLN   A NE2 
1430 N  N   . VAL   A 63  ? 0.1179 0.1210 0.1783 -0.0078 0.0105  -0.0159 63  VAL   A N   
1431 C  CA  . VAL   A 63  ? 0.1235 0.1302 0.1926 -0.0125 0.0004  -0.0134 63  VAL   A CA  
1432 C  C   . VAL   A 63  ? 0.1132 0.1325 0.1762 -0.0148 -0.0033 -0.0135 63  VAL   A C   
1433 O  O   . VAL   A 63  ? 0.1154 0.1310 0.1987 -0.0157 0.0004  -0.0071 63  VAL   A O   
1434 C  CB  . VAL   A 63  ? 0.1346 0.1485 0.2262 -0.0164 -0.0010 -0.0377 63  VAL   A CB  
1435 C  CG1 . VAL   A 63  ? 0.1442 0.1705 0.2610 -0.0136 -0.0091 -0.0585 63  VAL   A CG1 
1436 C  CG2 . VAL   A 63  ? 0.1423 0.1446 0.2310 -0.0144 0.0130  -0.0234 63  VAL   A CG2 
1446 N  N   . GLU   A 64  ? 0.1168 0.1385 0.1676 -0.0053 0.0029  -0.0067 64  GLU   A N   
1447 C  CA  . GLU   A 64  ? 0.1182 0.1340 0.1725 -0.0085 -0.0079 0.0026  64  GLU   A CA  
1448 C  C   . GLU   A 64  ? 0.1129 0.1274 0.1728 -0.0066 -0.0039 0.0047  64  GLU   A C   
1449 O  O   . GLU   A 64  ? 0.1228 0.1310 0.1777 -0.0025 -0.0003 -0.0032 64  GLU   A O   
1450 C  CB  . GLU   A 64  ? 0.1218 0.1469 0.1689 -0.0092 -0.0058 -0.0015 64  GLU   A CB  
1451 C  CG  . GLU   A 64  ? 0.1335 0.1522 0.1821 -0.0132 -0.0005 -0.0004 64  GLU   A CG  
1452 C  CD  . GLU   A 64  ? 0.1455 0.1606 0.1879 -0.0186 0.0065  0.0027  64  GLU   A CD  
1453 O  OE1 . GLU   A 64  ? 0.1454 0.1692 0.2075 -0.0238 0.0105  0.0003  64  GLU   A OE1 
1454 O  OE2 . GLU   A 64  ? 0.1663 0.1609 0.1795 -0.0273 -0.0068 0.0137  64  GLU   A OE2 
1461 N  N   . SER   A 65  ? 0.1116 0.1293 0.1635 -0.0005 -0.0023 0.0047  65  SER   A N   
1462 C  CA  . SER   A 65  ? 0.1166 0.1208 0.1588 -0.0066 -0.0050 -0.0017 65  SER   A CA  
1463 C  C   . SER   A 65  ? 0.1172 0.1267 0.1572 -0.0075 -0.0042 0.0030  65  SER   A C   
1464 O  O   . SER   A 65  ? 0.1278 0.1318 0.1813 -0.0007 0.0104  -0.0046 65  SER   A O   
1465 C  CB  . SER   A 65  ? 0.1172 0.1233 0.1631 -0.0103 0.0026  0.0077  65  SER   A CB  
1466 O  OG  . SER   A 65  ? 0.1200 0.1375 0.1624 -0.0114 -0.0059 0.0125  65  SER   A OG  
1472 N  N   . ASP   A 66  ? 0.1212 0.1260 0.1627 -0.0032 0.0136  0.0057  66  ASP   A N   
1473 C  CA  . ASP   A 66  ? 0.1293 0.1402 0.1795 -0.0047 0.0147  0.0153  66  ASP   A CA  
1474 C  C   . ASP   A 66  ? 0.1287 0.1364 0.1821 -0.0072 0.0163  0.0173  66  ASP   A C   
1475 O  O   . ASP   A 66  ? 0.1317 0.1459 0.1974 -0.0053 0.0296  0.0220  66  ASP   A O   
1476 C  CB  . ASP   A 66  ? 0.1380 0.1524 0.2080 0.0081  0.0196  0.0295  66  ASP   A CB  
1477 C  CG  . ASP   A 66  ? 0.1588 0.1615 0.2353 0.0006  0.0053  0.0437  66  ASP   A CG  
1478 O  OD1 . ASP   A 66  ? 0.1613 0.1874 0.2169 -0.0083 -0.0041 0.0483  66  ASP   A OD1 
1479 O  OD2 . ASP   A 66  ? 0.1727 0.1731 0.3125 0.0204  -0.0103 0.0246  66  ASP   A OD2 
1484 N  N   . ASP   A 67  ? 0.1204 0.1380 0.1926 -0.0045 0.0117  0.0186  67  ASP   A N   
1485 C  CA  . ASP   A 67  ? 0.1203 0.1520 0.2038 -0.0027 0.0043  0.0257  67  ASP   A CA  
1486 C  C   . ASP   A 67  ? 0.1238 0.1509 0.1994 0.0021  0.0099  0.0224  67  ASP   A C   
1487 O  O   . ASP   A 67  ? 0.1201 0.1550 0.2239 0.0018  0.0240  0.0295  67  ASP   A O   
1488 C  CB  . ASP   A 67  ? 0.1304 0.1580 0.2349 -0.0074 -0.0082 0.0402  67  ASP   A CB  
1489 C  CG  . ASP   A 67  ? 0.1338 0.1716 0.2744 -0.0110 -0.0265 0.0458  67  ASP   A CG  
1490 O  OD1 . ASP   A 67  ? 0.1388 0.1888 0.3461 -0.0168 -0.0379 0.0532  67  ASP   A OD1 
1491 O  OD2 . ASP   A 67  ? 0.1356 0.1770 0.2663 0.0005  -0.0136 0.0334  67  ASP   A OD2 
1496 N  N   . TYR   A 68  ? 0.1215 0.1380 0.1994 0.0012  0.0149  0.0301  68  TYR   A N   
1497 C  CA  . TYR   A 68  ? 0.1324 0.1388 0.1926 0.0032  0.0199  0.0285  68  TYR   A CA  
1498 C  C   . TYR   A 68  ? 0.1268 0.1362 0.1933 0.0005  0.0230  0.0181  68  TYR   A C   
1499 O  O   . TYR   A 68  ? 0.1345 0.1386 0.2006 0.0069  0.0288  0.0178  68  TYR   A O   
1500 C  CB  . TYR   A 68  ? 0.1368 0.1362 0.2040 0.0071  0.0387  0.0238  68  TYR   A CB  
1501 C  CG  . TYR   A 68  ? 0.1417 0.1545 0.2381 0.0017  0.0469  0.0291  68  TYR   A CG  
1502 C  CD1 . TYR   A 68  ? 0.1514 0.1611 0.2696 -0.0241 0.0399  -0.0023 68  TYR   A CD1 
1503 C  CD2 . TYR   A 68  ? 0.1612 0.1566 0.2716 0.0126  0.0541  0.0431  68  TYR   A CD2 
1504 C  CE1 . TYR   A 68  ? 0.1581 0.1685 0.3050 -0.0172 0.0499  -0.0133 68  TYR   A CE1 
1505 C  CE2 . TYR   A 68  ? 0.1613 0.1624 0.2938 0.0049  0.0625  0.0161  68  TYR   A CE2 
1506 C  CZ  . TYR   A 68  ? 0.1624 0.1606 0.3121 -0.0179 0.0494  -0.0130 68  TYR   A CZ  
1507 O  OH  . TYR   A 68  ? 0.1877 0.1571 0.3305 -0.0087 0.0238  -0.0306 68  TYR   A OH  
1517 N  N   . ILE   A 69  ? 0.1239 0.1299 0.1884 -0.0002 0.0201  0.0171  69  ILE   A N   
1518 C  CA  . ILE   A 69  ? 0.1330 0.1360 0.1736 0.0041  0.0122  0.0131  69  ILE   A CA  
1519 C  C   . ILE   A 69  ? 0.1319 0.1383 0.1702 0.0054  0.0203  0.0161  69  ILE   A C   
1520 O  O   . ILE   A 69  ? 0.1402 0.1434 0.1850 0.0001  0.0314  0.0180  69  ILE   A O   
1521 C  CB  . ILE   A 69  ? 0.1376 0.1586 0.1812 0.0093  0.0103  0.0065  69  ILE   A CB  
1522 C  CG1 . ILE   A 69  ? 0.1360 0.1673 0.1924 0.0085  0.0157  -0.0121 69  ILE   A CG1 
1523 C  CG2 . ILE   A 69  ? 0.1618 0.1751 0.2042 0.0182  -0.0007 -0.0032 69  ILE   A CG2 
1524 C  CD1 . ILE   A 69  ? 0.1344 0.1759 0.2055 -0.0024 0.0130  -0.0082 69  ILE   A CD1 
1536 N  N   . ALA   A 70  ? 0.1386 0.1385 0.1889 -0.0049 0.0236  0.0154  70  ALA   A N   
1537 C  CA  . ALA   A 70  ? 0.1419 0.1482 0.2131 -0.0159 0.0334  0.0185  70  ALA   A CA  
1538 C  C   . ALA   A 70  ? 0.1405 0.1624 0.2161 -0.0105 0.0323  0.0154  70  ALA   A C   
1539 O  O   . ALA   A 70  ? 0.1567 0.1944 0.2413 0.0031  0.0487  0.0352  70  ALA   A O   
1540 C  CB  . ALA   A 70  ? 0.1491 0.1466 0.2337 -0.0198 0.0310  0.0166  70  ALA   A CB  
1546 N  N   . THR   A 71  ? 0.1344 0.1625 0.2104 -0.0039 0.0210  0.0193  71  THR   A N   
1547 C  CA  . THR   A 71  ? 0.1442 0.1817 0.2397 0.0058  0.0226  0.0195  71  THR   A CA  
1548 C  C   . THR   A 71  ? 0.1383 0.1716 0.2566 0.0145  0.0362  0.0142  71  THR   A C   
1549 O  O   . THR   A 71  ? 0.1418 0.1941 0.2959 0.0114  0.0423  -0.0054 71  THR   A O   
1550 C  CB  . THR   A 71  ? 0.1726 0.2074 0.2673 0.0172  -0.0107 0.0285  71  THR   A CB  
1551 O  OG1 . THR   A 71  ? 0.1962 0.2250 0.2756 0.0092  -0.0269 0.0279  71  THR   A OG1 
1552 C  CG2 . THR   A 71  ? 0.1854 0.2208 0.2878 0.0282  -0.0224 0.0462  71  THR   A CG2 
1560 N  N   . ASN   A 72  ? 0.1416 0.1518 0.2317 0.0081  0.0272  0.0188  72  ASN   A N   
1561 C  CA  . ASN   A 72  ? 0.1471 0.1529 0.2280 0.0123  0.0318  0.0174  72  ASN   A CA  
1562 C  C   . ASN   A 72  ? 0.1577 0.1536 0.2178 0.0093  0.0450  0.0086  72  ASN   A C   
1563 O  O   . ASN   A 72  ? 0.1696 0.1533 0.2429 0.0130  0.0405  0.0018  72  ASN   A O   
1564 C  CB  . ASN   A 72  ? 0.1661 0.1621 0.2288 0.0060  0.0364  0.0189  72  ASN   A CB  
1565 C  CG  . ASN   A 72  ? 0.1909 0.1773 0.2364 0.0195  0.0351  0.0233  72  ASN   A CG  
1566 O  OD1 . ASN   A 72  ? 0.2041 0.2120 0.2534 0.0226  0.0376  0.0257  72  ASN   A OD1 
1567 N  ND2 . ASN   A 72  ? 0.2037 0.1743 0.2387 0.0465  0.0139  0.0167  72  ASN   A ND2 
1574 N  N   . GLY   A 73  ? 0.1566 0.1503 0.2080 -0.0007 0.0460  0.0055  73  GLY   A N   
1575 C  CA  . GLY   A 73  ? 0.1593 0.1513 0.1959 -0.0076 0.0426  0.0061  73  GLY   A CA  
1576 C  C   . GLY   A 73  ? 0.1605 0.1435 0.1812 0.0018  0.0476  0.0221  73  GLY   A C   
1577 O  O   . GLY   A 73  ? 0.1559 0.1453 0.1955 0.0104  0.0325  0.0246  73  GLY   A O   
1581 N  N   . PRO   A 74  ? 0.1710 0.1422 0.1853 -0.0182 0.0502  0.0131  74  PRO   A N   
1582 C  CA  . PRO   A 74  ? 0.1618 0.1370 0.1959 -0.0051 0.0436  0.0184  74  PRO   A CA  
1583 C  C   . PRO   A 74  ? 0.1562 0.1224 0.1836 -0.0004 0.0354  0.0066  74  PRO   A C   
1584 O  O   . PRO   A 74  ? 0.1644 0.1331 0.2077 0.0006  0.0332  -0.0068 74  PRO   A O   
1585 C  CB  . PRO   A 74  ? 0.1760 0.1661 0.2163 -0.0005 0.0430  0.0289  74  PRO   A CB  
1586 C  CG  . PRO   A 74  ? 0.2036 0.2018 0.2592 -0.0225 0.0322  0.0124  74  PRO   A CG  
1587 C  CD  . PRO   A 74  ? 0.1871 0.1766 0.2121 -0.0293 0.0389  0.0049  74  PRO   A CD  
1595 N  N   . LEU   A 75  ? 0.1522 0.1208 0.1620 -0.0049 0.0187  0.0008  75  LEU   A N   
1596 C  CA  . LEU   A 75  ? 0.1537 0.1189 0.1496 0.0037  0.0052  0.0087  75  LEU   A CA  
1597 C  C   . LEU   A 75  ? 0.1652 0.1301 0.1526 0.0056  0.0073  0.0135  75  LEU   A C   
1598 O  O   . LEU   A 75  ? 0.1965 0.1514 0.1555 0.0133  0.0086  0.0080  75  LEU   A O   
1599 C  CB  . LEU   A 75  ? 0.1595 0.1277 0.1452 -0.0082 0.0052  0.0167  75  LEU   A CB  
1600 C  CG  . LEU   A 75  ? 0.1782 0.1660 0.1578 -0.0354 0.0049  0.0156  75  LEU   A CG  
1601 C  CD1 . LEU   A 75  ? 0.1873 0.2159 0.1719 -0.0367 0.0046  -0.0030 75  LEU   A CD1 
1602 C  CD2 . LEU   A 75  ? 0.2043 0.2019 0.2067 -0.0155 -0.0047 0.0192  75  LEU   A CD2 
1614 N  N   . LYS   A 76  ? 0.1649 0.1309 0.1689 -0.0023 0.0102  0.0003  76  LYS   A N   
1615 C  CA  . LYS   A 76  ? 0.1630 0.1509 0.1677 -0.0040 0.0150  -0.0109 76  LYS   A CA  
1616 C  C   . LYS   A 76  ? 0.1593 0.1322 0.1422 0.0005  0.0147  0.0116  76  LYS   A C   
1617 O  O   . LYS   A 76  ? 0.1608 0.1300 0.1501 -0.0026 0.0176  0.0130  76  LYS   A O   
1618 C  CB  . LYS   A 76  ? 0.1622 0.1747 0.2045 0.0047  0.0099  -0.0356 76  LYS   A CB  
1619 C  CG  . LYS   A 76  ? 0.1737 0.1685 0.2518 0.0083  0.0014  -0.0307 76  LYS   A CG  
1620 C  CD  . LYS   A 76  ? 0.1808 0.1680 0.3007 0.0132  -0.0069 -0.0309 76  LYS   A CD  
1621 C  CE  . LYS   A 76  ? 0.1998 0.1898 0.3537 0.0043  -0.0028 -0.0404 76  LYS   A CE  
1622 N  NZ  . LYS   A 76  ? 0.2014 0.1837 0.3904 -0.0083 -0.0062 -0.0496 76  LYS   A NZ  
1636 N  N   . VAL   A 77  ? 0.1692 0.1412 0.1457 -0.0009 0.0279  0.0139  77  VAL   A N   
1637 C  CA  . VAL   A 77  ? 0.1653 0.1433 0.1387 0.0058  0.0193  0.0112  77  VAL   A CA  
1638 C  C   . VAL   A 77  ? 0.1553 0.1380 0.1476 0.0065  0.0176  0.0060  77  VAL   A C   
1639 O  O   . VAL   A 77  ? 0.1637 0.1395 0.1485 0.0124  0.0325  -0.0014 77  VAL   A O   
1640 C  CB  . VAL   A 77  ? 0.1801 0.1608 0.1500 0.0035  0.0122  0.0178  77  VAL   A CB  
1641 C  CG1 . VAL   A 77  ? 0.1734 0.1745 0.1697 0.0109  0.0011  0.0071  77  VAL   A CG1 
1642 C  CG2 . VAL   A 77  ? 0.2089 0.1673 0.1640 0.0003  0.0043  0.0207  77  VAL   A CG2 
1652 N  N   . GLY   A 78  ? 0.1504 0.1341 0.1425 0.0038  0.0247  0.0089  78  GLY   A N   
1653 C  CA  . GLY   A 78  ? 0.1520 0.1303 0.1528 0.0001  0.0251  0.0093  78  GLY   A CA  
1654 C  C   . GLY   A 78  ? 0.1399 0.1253 0.1557 0.0026  0.0237  0.0129  78  GLY   A C   
1655 O  O   . GLY   A 78  ? 0.1355 0.1336 0.1721 0.0024  0.0199  0.0252  78  GLY   A O   
1659 N  N   . GLY   A 79  ? 0.1450 0.1230 0.1503 0.0029  0.0180  0.0177  79  GLY   A N   
1660 C  CA  . GLY   A 79  ? 0.1419 0.1276 0.1512 0.0045  0.0149  0.0171  79  GLY   A CA  
1661 C  C   . GLY   A 79  ? 0.1331 0.1202 0.1492 -0.0030 0.0159  0.0063  79  GLY   A C   
1662 O  O   . GLY   A 79  ? 0.1349 0.1329 0.1655 0.0190  0.0162  0.0084  79  GLY   A O   
1666 N  N   . SER   A 80  ? 0.1283 0.1371 0.1638 -0.0027 0.0144  -0.0019 80  SER   A N   
1667 C  CA  . SER   A 80  ? 0.1226 0.1320 0.1559 -0.0011 0.0040  0.0078  80  SER   A CA  
1668 C  C   . SER   A 80  ? 0.1244 0.1326 0.1532 -0.0020 0.0103  0.0154  80  SER   A C   
1669 O  O   . SER   A 80  ? 0.1266 0.1532 0.1903 0.0091  0.0128  0.0001  80  SER   A O   
1670 C  CB  . SER   A 80  ? 0.1394 0.1297 0.1828 -0.0027 0.0085  0.0084  80  SER   A CB  
1671 O  OG  . SER   A 80  ? 0.1627 0.1306 0.2208 0.0076  -0.0013 0.0248  80  SER   A OG  
1677 N  N   . CYS   A 81  ? 0.1223 0.1290 0.1520 -0.0012 -0.0022 0.0126  81  CYS   A N   
1678 C  CA  . CYS   A 81  ? 0.1222 0.1369 0.1469 -0.0065 -0.0042 0.0193  81  CYS   A CA  
1679 C  C   . CYS   A 81  ? 0.1210 0.1346 0.1455 -0.0096 -0.0020 0.0318  81  CYS   A C   
1680 O  O   . CYS   A 81  ? 0.1165 0.1582 0.1714 -0.0025 -0.0005 0.0327  81  CYS   A O   
1681 C  CB  . CYS   A 81  ? 0.1285 0.1420 0.1641 -0.0106 -0.0009 0.0218  81  CYS   A CB  
1682 S  SG  . CYS   A 81  ? 0.1402 0.1340 0.1613 -0.0158 0.0013  0.0166  81  CYS   A SG  
1688 N  N   . VAL   A 82  ? 0.1269 0.1358 0.1513 -0.0020 -0.0115 0.0237  82  VAL   A N   
1689 C  CA  . VAL   A 82  ? 0.1388 0.1457 0.1526 -0.0038 -0.0088 0.0329  82  VAL   A CA  
1690 C  C   . VAL   A 82  ? 0.1341 0.1495 0.1677 -0.0071 -0.0107 0.0300  82  VAL   A C   
1691 O  O   . VAL   A 82  ? 0.1249 0.1562 0.1932 -0.0060 -0.0067 0.0088  82  VAL   A O   
1692 C  CB  . VAL   A 82  ? 0.1656 0.1618 0.1674 0.0034  -0.0052 0.0373  82  VAL   A CB  
1693 C  CG1 . VAL   A 82  ? 0.1857 0.1708 0.1883 0.0079  -0.0033 0.0319  82  VAL   A CG1 
1694 C  CG2 . VAL   A 82  ? 0.1702 0.1665 0.1990 -0.0028 -0.0066 0.0371  82  VAL   A CG2 
1704 N  N   . LEU   A 83  ? 0.1285 0.1485 0.1493 -0.0114 -0.0095 0.0134  83  LEU   A N   
1705 C  CA  . LEU   A 83  ? 0.1326 0.1466 0.1387 -0.0125 -0.0121 0.0095  83  LEU   A CA  
1706 C  C   . LEU   A 83  ? 0.1384 0.1489 0.1381 -0.0106 -0.0142 0.0169  83  LEU   A C   
1707 O  O   . LEU   A 83  ? 0.1450 0.1517 0.1554 -0.0196 -0.0085 0.0238  83  LEU   A O   
1708 C  CB  . LEU   A 83  ? 0.1387 0.1522 0.1501 -0.0151 -0.0098 0.0152  83  LEU   A CB  
1709 C  CG  . LEU   A 83  ? 0.1517 0.1605 0.1555 -0.0169 0.0061  0.0117  83  LEU   A CG  
1710 C  CD1 . LEU   A 83  ? 0.1607 0.1628 0.1679 -0.0310 0.0039  0.0211  83  LEU   A CD1 
1711 C  CD2 . LEU   A 83  ? 0.1473 0.1712 0.1723 -0.0180 0.0108  0.0133  83  LEU   A CD2 
1723 N  N   . SER   A 84  ? 0.1524 0.1581 0.1451 -0.0149 -0.0128 0.0226  84  SER   A N   
1724 C  CA  . SER   A 84  ? 0.1632 0.1648 0.1384 -0.0164 -0.0164 0.0207  84  SER   A CA  
1725 C  C   . SER   A 84  ? 0.1630 0.1643 0.1262 -0.0243 -0.0026 0.0134  84  SER   A C   
1726 O  O   . SER   A 84  ? 0.1579 0.1763 0.1262 -0.0212 -0.0101 0.0149  84  SER   A O   
1727 C  CB  . SER   A 84  ? 0.1659 0.1858 0.1465 -0.0149 -0.0149 0.0083  84  SER   A CB  
1728 O  OG  . SER   A 84  ? 0.1652 0.2042 0.1570 -0.0142 -0.0193 -0.0043 84  SER   A OG  
1734 N  N   . GLY   A 85  ? 0.1801 0.1767 0.1286 -0.0270 0.0025  0.0094  85  GLY   A N   
1735 C  CA  . GLY   A 85  ? 0.1807 0.1865 0.1439 -0.0276 0.0130  0.0041  85  GLY   A CA  
1736 C  C   . GLY   A 85  ? 0.1752 0.1912 0.1295 -0.0271 0.0007  0.0037  85  GLY   A C   
1737 O  O   . GLY   A 85  ? 0.1736 0.1993 0.1517 -0.0326 0.0060  -0.0085 85  GLY   A O   
1741 N  N   . HIS   A 86  ? 0.1734 0.1846 0.1244 -0.0248 -0.0046 0.0065  86  HIS   A N   
1742 C  CA  . HIS   A 86  ? 0.1909 0.1921 0.1250 -0.0288 -0.0055 0.0029  86  HIS   A CA  
1743 C  C   . HIS   A 86  ? 0.2143 0.2068 0.1242 -0.0275 -0.0115 -0.0002 86  HIS   A C   
1744 O  O   . HIS   A 86  ? 0.2186 0.2287 0.1425 -0.0270 0.0040  0.0033  86  HIS   A O   
1745 C  CB  . HIS   A 86  ? 0.1867 0.1814 0.1355 -0.0245 -0.0023 0.0098  86  HIS   A CB  
1746 C  CG  . HIS   A 86  ? 0.1819 0.1835 0.1472 -0.0137 -0.0001 0.0084  86  HIS   A CG  
1747 N  ND1 . HIS   A 86  ? 0.1866 0.1793 0.1770 -0.0236 -0.0061 0.0080  86  HIS   A ND1 
1748 C  CD2 . HIS   A 86  ? 0.1798 0.1752 0.1371 -0.0038 0.0031  0.0139  86  HIS   A CD2 
1749 C  CE1 . HIS   A 86  ? 0.1798 0.1809 0.1720 -0.0159 0.0144  0.0126  86  HIS   A CE1 
1750 N  NE2 . HIS   A 86  ? 0.1797 0.1754 0.1564 -0.0005 0.0123  0.0216  86  HIS   A NE2 
1758 N  N   . ASN   A 87  ? 0.2293 0.2148 0.1308 -0.0233 0.0107  -0.0062 87  ASN   A N   
1759 C  CA  . ASN   A 87  ? 0.2505 0.2260 0.1300 -0.0217 0.0356  -0.0071 87  ASN   A CA  
1760 C  C   . ASN   A 87  ? 0.2503 0.2409 0.1599 -0.0304 0.0567  0.0012  87  ASN   A C   
1761 O  O   . ASN   A 87  ? 0.2719 0.2578 0.1987 -0.0409 0.0839  -0.0103 87  ASN   A O   
1762 C  CB  . ASN   A 87  ? 0.2655 0.2313 0.1325 -0.0100 0.0373  -0.0145 87  ASN   A CB  
1763 C  CG  . ASN   A 87  ? 0.2766 0.2444 0.1460 -0.0023 0.0491  -0.0061 87  ASN   A CG  
1764 O  OD1 . ASN   A 87  ? 0.2910 0.2423 0.1540 0.0155  0.0385  0.0035  87  ASN   A OD1 
1765 N  ND2 . ASN   A 87  ? 0.2787 0.2656 0.1572 -0.0017 0.0549  -0.0051 87  ASN   A ND2 
1772 N  N   . LEU   A 88  ? 0.2194 0.2301 0.1520 -0.0341 0.0347  0.0104  88  LEU   A N   
1773 C  CA  . LEU   A 88  ? 0.2001 0.2300 0.1742 -0.0377 0.0315  0.0217  88  LEU   A CA  
1774 C  C   . LEU   A 88  ? 0.1889 0.2327 0.1587 -0.0346 0.0378  0.0330  88  LEU   A C   
1775 O  O   . LEU   A 88  ? 0.1897 0.2308 0.1988 -0.0280 0.0404  0.0494  88  LEU   A O   
1776 C  CB  . LEU   A 88  ? 0.1992 0.2354 0.1838 -0.0465 -0.0042 0.0354  88  LEU   A CB  
1777 C  CG  . LEU   A 88  ? 0.2179 0.2528 0.2178 -0.0470 -0.0092 0.0408  88  LEU   A CG  
1778 C  CD1 . LEU   A 88  ? 0.2288 0.2604 0.2134 -0.0443 -0.0106 0.0380  88  LEU   A CD1 
1779 C  CD2 . LEU   A 88  ? 0.2317 0.2620 0.2537 -0.0411 -0.0040 0.0354  88  LEU   A CD2 
1791 N  N   . ALA   A 89  ? 0.1866 0.2266 0.1390 -0.0343 0.0218  0.0112  89  ALA   A N   
1792 C  CA  . ALA   A 89  ? 0.1969 0.2241 0.1236 -0.0294 0.0087  0.0248  89  ALA   A CA  
1793 C  C   . ALA   A 89  ? 0.2077 0.2224 0.1367 -0.0271 -0.0072 0.0237  89  ALA   A C   
1794 O  O   . ALA   A 89  ? 0.2018 0.2138 0.1763 -0.0360 -0.0113 -0.0003 89  ALA   A O   
1795 C  CB  . ALA   A 89  ? 0.1926 0.2258 0.1136 -0.0275 0.0035  0.0234  89  ALA   A CB  
1801 N  N   . LYS   A 90  ? 0.2173 0.2370 0.1375 -0.0338 -0.0215 0.0281  90  LYS   A N   
1802 C  CA  . LYS   A 90  ? 0.2267 0.2521 0.1379 -0.0275 -0.0395 0.0276  90  LYS   A CA  
1803 C  C   . LYS   A 90  ? 0.2030 0.2317 0.1303 -0.0291 -0.0372 0.0165  90  LYS   A C   
1804 O  O   . LYS   A 90  ? 0.2032 0.2460 0.1693 -0.0342 -0.0374 0.0002  90  LYS   A O   
1805 C  CB  . LYS   A 90  ? 0.2532 0.2881 0.1788 -0.0257 -0.0464 0.0489  90  LYS   A CB  
1806 C  CG  . LYS   A 90  ? 0.2972 0.3256 0.2798 -0.0233 -0.0394 0.0531  90  LYS   A CG  
1807 C  CD  . LYS   A 90  ? 0.3513 0.3698 0.3845 -0.0244 -0.0204 0.0541  90  LYS   A CD  
1808 C  CE  . LYS   A 90  ? 0.3913 0.4055 0.4647 -0.0245 -0.0049 0.0504  90  LYS   A CE  
1809 N  NZ  . LYS   A 90  ? 0.4065 0.4166 0.5164 -0.0254 0.0040  0.0477  90  LYS   A NZ  
1823 N  N   . HIS   A 91  ? 0.1877 0.2057 0.1095 -0.0271 -0.0403 0.0287  91  HIS   A N   
1824 C  CA  . HIS   A 91  ? 0.1705 0.1836 0.1238 -0.0190 -0.0302 0.0236  91  HIS   A CA  
1825 C  C   . HIS   A 91  ? 0.1559 0.1687 0.1150 -0.0165 -0.0157 0.0209  91  HIS   A C   
1826 O  O   . HIS   A 91  ? 0.1525 0.1807 0.1398 -0.0259 -0.0082 0.0205  91  HIS   A O   
1827 C  CB  . HIS   A 91  ? 0.1880 0.2088 0.1783 0.0023  -0.0380 0.0224  91  HIS   A CB  
1828 C  CG  . HIS   A 91  ? 0.2311 0.2557 0.2420 0.0195  -0.0642 0.0138  91  HIS   A CG  
1829 N  ND1 . HIS   A 91  ? 0.2443 0.2835 0.2863 0.0245  -0.0733 -0.0070 91  HIS   A ND1 
1830 C  CD2 . HIS   A 91  ? 0.2580 0.2763 0.2659 0.0274  -0.0791 0.0194  91  HIS   A CD2 
1831 C  CE1 . HIS   A 91  ? 0.2567 0.2930 0.2968 0.0290  -0.0786 0.0017  91  HIS   A CE1 
1832 N  NE2 . HIS   A 91  ? 0.2680 0.2912 0.2883 0.0347  -0.0862 0.0138  91  HIS   A NE2 
1840 N  N   . CYS   A 92  ? 0.1433 0.1601 0.1234 -0.0210 -0.0123 0.0234  92  CYS   A N   
1841 C  CA  . CYS   A 92  ? 0.1336 0.1550 0.1301 -0.0169 -0.0062 0.0178  92  CYS   A CA  
1842 C  C   . CYS   A 92  ? 0.1312 0.1479 0.1273 -0.0195 0.0006  0.0147  92  CYS   A C   
1843 O  O   . CYS   A 92  ? 0.1313 0.1552 0.1500 -0.0199 -0.0055 0.0179  92  CYS   A O   
1844 C  CB  . CYS   A 92  ? 0.1436 0.1516 0.1375 -0.0058 -0.0102 0.0128  92  CYS   A CB  
1845 S  SG  . CYS   A 92  ? 0.1380 0.1389 0.1386 -0.0124 -0.0058 0.0145  92  CYS   A SG  
1851 N  N   . LEU   A 93  ? 0.1279 0.1308 0.1357 -0.0124 0.0051  0.0174  93  LEU   A N   
1852 C  CA  . LEU   A 93  ? 0.1201 0.1262 0.1283 -0.0111 -0.0003 0.0195  93  LEU   A CA  
1853 C  C   . LEU   A 93  ? 0.1201 0.1191 0.1230 -0.0075 0.0018  0.0135  93  LEU   A C   
1854 O  O   . LEU   A 93  ? 0.1134 0.1302 0.1349 -0.0055 -0.0006 0.0154  93  LEU   A O   
1855 C  CB  . LEU   A 93  ? 0.1282 0.1347 0.1470 -0.0084 -0.0051 0.0225  93  LEU   A CB  
1856 C  CG  . LEU   A 93  ? 0.1360 0.1309 0.1537 -0.0067 -0.0005 0.0266  93  LEU   A CG  
1857 C  CD1 . LEU   A 93  ? 0.1369 0.1372 0.1808 -0.0039 0.0048  0.0177  93  LEU   A CD1 
1858 C  CD2 . LEU   A 93  ? 0.1518 0.1301 0.1696 -0.0105 -0.0034 0.0202  93  LEU   A CD2 
1870 N  N   . HIS   A 94  ? 0.1129 0.1174 0.1381 -0.0043 0.0039  0.0188  94  HIS   A N   
1871 C  CA  . HIS   A 94  ? 0.1135 0.1192 0.1333 -0.0058 -0.0026 0.0156  94  HIS   A CA  
1872 C  C   . HIS   A 94  ? 0.1132 0.1141 0.1424 -0.0042 -0.0038 0.0120  94  HIS   A C   
1873 O  O   . HIS   A 94  ? 0.1155 0.1355 0.1704 -0.0011 0.0007  -0.0056 94  HIS   A O   
1874 C  CB  . HIS   A 94  ? 0.1137 0.1160 0.1395 -0.0040 -0.0044 0.0134  94  HIS   A CB  
1875 C  CG  . HIS   A 94  ? 0.1210 0.1160 0.1229 -0.0069 -0.0044 0.0209  94  HIS   A CG  
1876 N  ND1 . HIS   A 94  ? 0.1183 0.1199 0.1370 -0.0019 0.0002  0.0171  94  HIS   A ND1 
1877 C  CD2 . HIS   A 94  ? 0.1259 0.1318 0.1323 -0.0072 -0.0061 0.0123  94  HIS   A CD2 
1878 C  CE1 . HIS   A 94  ? 0.1214 0.1257 0.1362 -0.0108 -0.0056 0.0110  94  HIS   A CE1 
1879 N  NE2 . HIS   A 94  ? 0.1278 0.1257 0.1448 -0.0129 -0.0034 0.0036  94  HIS   A NE2 
1887 N  N   . VAL   A 95  ? 0.1097 0.1157 0.1245 -0.0059 0.0074  0.0063  95  VAL   A N   
1888 C  CA  . VAL   A 95  ? 0.1197 0.1167 0.1267 -0.0050 0.0091  0.0106  95  VAL   A CA  
1889 C  C   . VAL   A 95  ? 0.1192 0.1125 0.1209 -0.0112 0.0015  0.0078  95  VAL   A C   
1890 O  O   . VAL   A 95  ? 0.1209 0.1241 0.1367 0.0060  0.0064  0.0039  95  VAL   A O   
1891 C  CB  . VAL   A 95  ? 0.1180 0.1190 0.1404 -0.0094 0.0043  0.0084  95  VAL   A CB  
1892 C  CG1 . VAL   A 95  ? 0.1337 0.1255 0.1514 -0.0134 0.0037  0.0020  95  VAL   A CG1 
1893 C  CG2 . VAL   A 95  ? 0.1189 0.1285 0.1398 -0.0117 0.0047  0.0242  95  VAL   A CG2 
1903 N  N   . VAL   A 96  ? 0.1214 0.1168 0.1173 -0.0064 0.0077  0.0135  96  VAL   A N   
1904 C  CA  . VAL   A 96  ? 0.1299 0.1195 0.1275 -0.0060 0.0074  0.0176  96  VAL   A CA  
1905 C  C   . VAL   A 96  ? 0.1294 0.1252 0.1383 -0.0025 0.0150  0.0163  96  VAL   A C   
1906 O  O   . VAL   A 96  ? 0.1360 0.1329 0.1566 -0.0037 0.0198  0.0020  96  VAL   A O   
1907 C  CB  . VAL   A 96  ? 0.1293 0.1223 0.1410 -0.0075 0.0209  0.0173  96  VAL   A CB  
1908 C  CG1 . VAL   A 96  ? 0.1384 0.1328 0.1347 -0.0062 0.0151  0.0128  96  VAL   A CG1 
1909 C  CG2 . VAL   A 96  ? 0.1353 0.1307 0.1409 -0.0130 0.0171  0.0129  96  VAL   A CG2 
1919 N  N   A GLY   A 97  ? 0.1296 0.1295 0.1391 -0.0072 0.0063  0.0119  97  GLY   A N   
1920 N  N   B GLY   A 97  ? 0.1346 0.1308 0.1332 -0.0022 0.0070  0.0160  97  GLY   A N   
1921 C  CA  A GLY   A 97  ? 0.1395 0.1454 0.1343 -0.0049 0.0040  0.0126  97  GLY   A CA  
1922 C  CA  B GLY   A 97  ? 0.1435 0.1376 0.1297 -0.0011 0.0032  0.0182  97  GLY   A CA  
1923 C  C   A GLY   A 97  ? 0.1415 0.1553 0.1227 -0.0108 0.0076  0.0096  97  GLY   A C   
1924 C  C   B GLY   A 97  ? 0.1504 0.1431 0.1268 -0.0026 0.0007  0.0189  97  GLY   A C   
1925 O  O   A GLY   A 97  ? 0.1540 0.1533 0.1452 -0.0138 -0.0014 0.0135  97  GLY   A O   
1926 O  O   B GLY   A 97  ? 0.1544 0.1448 0.1299 -0.0023 -0.0047 0.0237  97  GLY   A O   
1933 N  N   A PRO   A 98  ? 0.1410 0.1564 0.1151 -0.0055 0.0024  0.0144  98  PRO   A N   
1934 N  N   B PRO   A 98  ? 0.1557 0.1425 0.1312 -0.0040 -0.0035 0.0202  98  PRO   A N   
1935 C  CA  A PRO   A 98  ? 0.1537 0.1735 0.1219 -0.0037 0.0042  0.0086  98  PRO   A CA  
1936 C  CA  B PRO   A 98  ? 0.1642 0.1472 0.1368 -0.0052 -0.0032 0.0135  98  PRO   A CA  
1937 C  C   A PRO   A 98  ? 0.1533 0.1805 0.1095 -0.0121 0.0071  0.0149  98  PRO   A C   
1938 C  C   B PRO   A 98  ? 0.1748 0.1485 0.1354 -0.0082 -0.0030 0.0208  98  PRO   A C   
1939 O  O   A PRO   A 98  ? 0.1468 0.1627 0.1155 -0.0090 0.0037  0.0046  98  PRO   A O   
1940 O  O   B PRO   A 98  ? 0.1722 0.1459 0.1549 -0.0059 -0.0027 0.0139  98  PRO   A O   
1941 C  CB  A PRO   A 98  ? 0.1645 0.1821 0.1115 0.0047  0.0010  -0.0045 98  PRO   A CB  
1942 C  CB  B PRO   A 98  ? 0.1661 0.1447 0.1252 -0.0022 -0.0057 0.0181  98  PRO   A CB  
1943 C  CG  A PRO   A 98  ? 0.1648 0.1804 0.1243 0.0043  0.0018  -0.0064 98  PRO   A CG  
1944 C  CG  B PRO   A 98  ? 0.1679 0.1455 0.1279 -0.0050 -0.0030 0.0160  98  PRO   A CG  
1945 C  CD  A PRO   A 98  ? 0.1497 0.1630 0.1212 0.0025  0.0080  0.0050  98  PRO   A CD  
1946 C  CD  B PRO   A 98  ? 0.1606 0.1410 0.1225 -0.0040 -0.0003 0.0232  98  PRO   A CD  
1961 N  N   A ASN   A 99  ? 0.1545 0.2062 0.1139 -0.0058 0.0166  0.0299  99  ASN   A N   
1962 N  N   B ASN   A 99  ? 0.1899 0.1501 0.1210 -0.0086 -0.0041 0.0353  99  ASN   A N   
1963 C  CA  A ASN   A 99  ? 0.1726 0.2243 0.1117 -0.0020 0.0123  0.0327  99  ASN   A CA  
1964 C  CA  B ASN   A 99  ? 0.2064 0.1520 0.1093 -0.0102 -0.0012 0.0521  99  ASN   A CA  
1965 C  C   A ASN   A 99  ? 0.1891 0.2491 0.1145 -0.0098 0.0169  0.0347  99  ASN   A C   
1966 C  C   B ASN   A 99  ? 0.2128 0.1556 0.1070 -0.0062 -0.0041 0.0601  99  ASN   A C   
1967 O  O   A ASN   A 99  ? 0.1967 0.2643 0.1246 -0.0029 0.0077  0.0334  99  ASN   A O   
1968 O  O   B ASN   A 99  ? 0.2122 0.1457 0.1122 0.0026  -0.0073 0.0420  99  ASN   A O   
1969 C  CB  A ASN   A 99  ? 0.1722 0.2198 0.1196 -0.0040 0.0058  0.0356  99  ASN   A CB  
1970 C  CB  B ASN   A 99  ? 0.2153 0.1536 0.1280 -0.0138 -0.0015 0.0535  99  ASN   A CB  
1971 C  CG  A ASN   A 99  ? 0.1723 0.2171 0.1186 0.0018  -0.0034 0.0312  99  ASN   A CG  
1972 C  CG  B ASN   A 99  ? 0.2254 0.1616 0.1541 -0.0163 0.0012  0.0544  99  ASN   A CG  
1973 O  OD1 A ASN   A 99  ? 0.1830 0.2253 0.1234 0.0095  -0.0040 0.0163  99  ASN   A OD1 
1974 O  OD1 B ASN   A 99  ? 0.2285 0.1640 0.1492 -0.0100 0.0008  0.0574  99  ASN   A OD1 
1975 N  ND2 A ASN   A 99  ? 0.1720 0.2091 0.1437 -0.0055 -0.0150 0.0485  99  ASN   A ND2 
1976 N  ND2 B ASN   A 99  ? 0.2316 0.1661 0.1844 -0.0163 -0.0040 0.0466  99  ASN   A ND2 
1989 N  N   A VAL   A 100 ? 0.2050 0.2603 0.1246 -0.0247 -0.0070 0.0272  100 VAL   A N   
1990 N  N   B VAL   A 100 ? 0.2232 0.1802 0.1229 -0.0039 -0.0127 0.0652  100 VAL   A N   
1991 C  CA  A VAL   A 100 ? 0.2279 0.2721 0.1383 -0.0342 -0.0200 0.0245  100 VAL   A CA  
1992 C  CA  B VAL   A 100 ? 0.2384 0.2033 0.1660 -0.0012 -0.0164 0.0528  100 VAL   A CA  
1993 C  C   A VAL   A 100 ? 0.2377 0.2799 0.1240 -0.0420 -0.0224 0.0443  100 VAL   A C   
1994 C  C   B VAL   A 100 ? 0.2407 0.2113 0.1712 0.0058  -0.0221 0.0448  100 VAL   A C   
1995 O  O   A VAL   A 100 ? 0.2515 0.2835 0.1432 -0.0364 -0.0065 0.0430  100 VAL   A O   
1996 O  O   B VAL   A 100 ? 0.2392 0.2070 0.1746 0.0075  -0.0197 0.0368  100 VAL   A O   
1997 C  CB  A VAL   A 100 ? 0.2459 0.2744 0.1708 -0.0425 -0.0286 0.0129  100 VAL   A CB  
1998 C  CB  B VAL   A 100 ? 0.2520 0.2183 0.2100 -0.0015 -0.0164 0.0384  100 VAL   A CB  
1999 C  CG1 A VAL   A 100 ? 0.2451 0.2789 0.1853 -0.0504 -0.0208 0.0116  100 VAL   A CG1 
2000 C  CG1 B VAL   A 100 ? 0.2550 0.2244 0.2263 -0.0015 -0.0170 0.0305  100 VAL   A CG1 
2001 C  CG2 A VAL   A 100 ? 0.2581 0.2765 0.1673 -0.0459 -0.0304 0.0043  100 VAL   A CG2 
2002 C  CG2 B VAL   A 100 ? 0.2565 0.2220 0.2254 -0.0014 -0.0124 0.0318  100 VAL   A CG2 
2021 N  N   A ASN   A 101 ? 0.2365 0.2918 0.1471 -0.0533 -0.0237 0.0625  101 ASN   A N   
2022 N  N   B ASN   A 101 ? 0.2498 0.2224 0.1829 0.0100  -0.0254 0.0425  101 ASN   A N   
2023 C  CA  A ASN   A 101 ? 0.2498 0.3060 0.1644 -0.0618 -0.0222 0.0914  101 ASN   A CA  
2024 C  CA  B ASN   A 101 ? 0.2616 0.2319 0.1955 0.0142  -0.0217 0.0393  101 ASN   A CA  
2025 C  C   A ASN   A 101 ? 0.2738 0.3381 0.1887 -0.0673 -0.0025 0.1157  101 ASN   A C   
2026 C  C   B ASN   A 101 ? 0.2770 0.2425 0.2098 0.0149  -0.0133 0.0474  101 ASN   A C   
2027 O  O   A ASN   A 101 ? 0.2896 0.3451 0.2315 -0.0645 -0.0060 0.1064  101 ASN   A O   
2028 O  O   B ASN   A 101 ? 0.2830 0.2457 0.2081 0.0125  -0.0174 0.0560  101 ASN   A O   
2029 C  CB  A ASN   A 101 ? 0.2469 0.2955 0.1667 -0.0573 -0.0407 0.0834  101 ASN   A CB  
2030 C  CB  B ASN   A 101 ? 0.2584 0.2313 0.1966 0.0158  -0.0215 0.0321  101 ASN   A CB  
2031 C  CG  A ASN   A 101 ? 0.2437 0.2862 0.1735 -0.0539 -0.0497 0.0603  101 ASN   A CG  
2032 C  CG  B ASN   A 101 ? 0.2578 0.2339 0.2064 0.0166  -0.0225 0.0267  101 ASN   A CG  
2033 O  OD1 A ASN   A 101 ? 0.2368 0.2883 0.1860 -0.0366 -0.0452 0.0354  101 ASN   A OD1 
2034 O  OD1 B ASN   A 101 ? 0.2631 0.2362 0.2136 0.0133  -0.0201 0.0278  101 ASN   A OD1 
2035 N  ND2 A ASN   A 101 ? 0.2477 0.2773 0.1780 -0.0665 -0.0413 0.0665  101 ASN   A ND2 
2036 N  ND2 B ASN   A 101 ? 0.2547 0.2348 0.2159 0.0213  -0.0221 0.0147  101 ASN   A ND2 
2049 N  N   A LYS   A 102 ? 0.2778 0.3651 0.2158 -0.0760 0.0128  0.1145  102 LYS   A N   
2050 N  N   B LYS   A 102 ? 0.2857 0.2521 0.2368 0.0169  0.0026  0.0434  102 LYS   A N   
2051 C  CA  A LYS   A 102 ? 0.2896 0.3906 0.2291 -0.0806 0.0157  0.1012  102 LYS   A CA  
2052 C  CA  B LYS   A 102 ? 0.2947 0.2602 0.2485 0.0154  0.0119  0.0412  102 LYS   A CA  
2053 C  C   A LYS   A 102 ? 0.3030 0.4145 0.2196 -0.0722 0.0211  0.0899  102 LYS   A C   
2054 C  C   B LYS   A 102 ? 0.2934 0.2568 0.2322 0.0148  0.0069  0.0558  102 LYS   A C   
2055 O  O   A LYS   A 102 ? 0.3051 0.4241 0.2253 -0.0696 0.0349  0.0820  102 LYS   A O   
2056 O  O   B LYS   A 102 ? 0.2938 0.2506 0.2232 0.0149  0.0064  0.0687  102 LYS   A O   
2057 C  CB  A LYS   A 102 ? 0.2952 0.3935 0.2592 -0.0872 0.0111  0.0876  102 LYS   A CB  
2058 C  CB  B LYS   A 102 ? 0.3050 0.2704 0.2837 0.0154  0.0174  0.0250  102 LYS   A CB  
2059 C  CG  A LYS   A 102 ? 0.3027 0.3941 0.2772 -0.0932 0.0070  0.0781  102 LYS   A CG  
2060 C  CG  B LYS   A 102 ? 0.3143 0.2805 0.3160 0.0148  0.0233  0.0119  102 LYS   A CG  
2061 C  CD  A LYS   A 102 ? 0.3146 0.3962 0.3012 -0.0958 0.0038  0.0646  102 LYS   A CD  
2062 C  CD  B LYS   A 102 ? 0.3228 0.2911 0.3483 0.0138  0.0285  0.0018  102 LYS   A CD  
2063 C  CE  A LYS   A 102 ? 0.3272 0.3987 0.3252 -0.0939 0.0008  0.0547  102 LYS   A CE  
2064 C  CE  B LYS   A 102 ? 0.3284 0.2979 0.3735 0.0126  0.0317  -0.0037 102 LYS   A CE  
2065 N  NZ  A LYS   A 102 ? 0.3329 0.3981 0.3363 -0.0960 0.0008  0.0475  102 LYS   A NZ  
2066 N  NZ  B LYS   A 102 ? 0.3305 0.3011 0.3873 0.0129  0.0344  -0.0057 102 LYS   A NZ  
2093 N  N   A GLY   A 103 ? 0.3123 0.4291 0.2378 -0.0624 0.0114  0.0684  103 GLY   A N   
2094 N  N   B GLY   A 103 ? 0.2923 0.2624 0.2262 0.0133  -0.0037 0.0547  103 GLY   A N   
2095 C  CA  A GLY   A 103 ? 0.3209 0.4387 0.2380 -0.0534 0.0123  0.0527  103 GLY   A CA  
2096 C  CA  B GLY   A 103 ? 0.2895 0.2629 0.2162 0.0096  -0.0107 0.0602  103 GLY   A CA  
2097 C  C   A GLY   A 103 ? 0.3228 0.4477 0.2446 -0.0473 0.0204  0.0432  103 GLY   A C   
2098 C  C   B GLY   A 103 ? 0.2826 0.2587 0.1950 0.0043  -0.0110 0.0638  103 GLY   A C   
2099 O  O   A GLY   A 103 ? 0.3339 0.4539 0.2639 -0.0442 0.0230  0.0378  103 GLY   A O   
2100 O  O   B GLY   A 103 ? 0.2859 0.2600 0.1914 -0.0008 -0.0113 0.0697  103 GLY   A O   
2107 N  N   A GLU   A 104 ? 0.3090 0.4455 0.2130 -0.0482 0.0302  0.0365  104 GLU   A N   
2108 N  N   B GLU   A 104 ? 0.2731 0.2537 0.1808 0.0070  -0.0194 0.0609  104 GLU   A N   
2109 C  CA  A GLU   A 104 ? 0.2923 0.4391 0.1923 -0.0547 0.0332  0.0284  104 GLU   A CA  
2110 C  CA  B GLU   A 104 ? 0.2666 0.2489 0.1704 0.0059  -0.0249 0.0488  104 GLU   A CA  
2111 C  C   A GLU   A 104 ? 0.2994 0.4478 0.1997 -0.0537 0.0350  0.0039  104 GLU   A C   
2112 C  C   B GLU   A 104 ? 0.2650 0.2485 0.1772 0.0120  -0.0190 0.0311  104 GLU   A C   
2113 O  O   A GLU   A 104 ? 0.2944 0.4517 0.2163 -0.0535 0.0244  0.0009  104 GLU   A O   
2114 O  O   B GLU   A 104 ? 0.2630 0.2403 0.1805 0.0155  -0.0160 0.0356  104 GLU   A O   
2115 C  CB  A GLU   A 104 ? 0.2633 0.4214 0.1662 -0.0627 0.0357  0.0515  104 GLU   A CB  
2116 C  CB  B GLU   A 104 ? 0.2642 0.2470 0.1676 -0.0005 -0.0298 0.0502  104 GLU   A CB  
2117 C  CG  A GLU   A 104 ? 0.2431 0.4032 0.1661 -0.0649 0.0296  0.0676  104 GLU   A CG  
2118 C  CG  B GLU   A 104 ? 0.2648 0.2507 0.1782 -0.0034 -0.0362 0.0512  104 GLU   A CG  
2119 C  CD  A GLU   A 104 ? 0.2220 0.3841 0.1647 -0.0679 0.0236  0.0799  104 GLU   A CD  
2120 C  CD  B GLU   A 104 ? 0.2642 0.2546 0.1850 -0.0046 -0.0439 0.0506  104 GLU   A CD  
2121 O  OE1 A GLU   A 104 ? 0.1999 0.3618 0.1387 -0.0679 0.0117  0.0780  104 GLU   A OE1 
2122 O  OE1 B GLU   A 104 ? 0.2629 0.2575 0.1829 -0.0020 -0.0486 0.0521  104 GLU   A OE1 
2123 O  OE2 A GLU   A 104 ? 0.2375 0.3836 0.1876 -0.0693 0.0256  0.1000  104 GLU   A OE2 
2124 O  OE2 B GLU   A 104 ? 0.2694 0.2563 0.2025 -0.0080 -0.0432 0.0456  104 GLU   A OE2 
2137 N  N   A ASP   A 105 ? 0.3122 0.4518 0.2107 -0.0508 0.0417  -0.0227 105 ASP   A N   
2138 N  N   B ASP   A 105 ? 0.2712 0.2587 0.1981 0.0115  -0.0130 0.0105  105 ASP   A N   
2139 C  CA  A ASP   A 105 ? 0.3197 0.4539 0.2442 -0.0469 0.0478  -0.0484 105 ASP   A CA  
2140 C  CA  B ASP   A 105 ? 0.2774 0.2696 0.2267 0.0115  -0.0007 -0.0158 105 ASP   A CA  
2141 C  C   A ASP   A 105 ? 0.2929 0.4374 0.2033 -0.0585 0.0392  -0.0669 105 ASP   A C   
2142 C  C   B ASP   A 105 ? 0.2758 0.2711 0.2098 0.0019  0.0026  -0.0262 105 ASP   A C   
2143 O  O   A ASP   A 105 ? 0.2809 0.4339 0.1541 -0.0610 0.0437  -0.0918 105 ASP   A O   
2144 O  O   B ASP   A 105 ? 0.2691 0.2648 0.1699 0.0028  0.0048  -0.0370 105 ASP   A O   
2145 C  CB  A ASP   A 105 ? 0.3495 0.4705 0.3160 -0.0333 0.0539  -0.0569 105 ASP   A CB  
2146 C  CB  B ASP   A 105 ? 0.2848 0.2790 0.2738 0.0200  0.0059  -0.0288 105 ASP   A CB  
2147 C  CG  A ASP   A 105 ? 0.3722 0.4839 0.3781 -0.0222 0.0552  -0.0662 105 ASP   A CG  
2148 C  CG  B ASP   A 105 ? 0.2907 0.2857 0.3153 0.0291  0.0118  -0.0407 105 ASP   A CG  
2149 O  OD1 A ASP   A 105 ? 0.3784 0.4898 0.3916 -0.0202 0.0555  -0.0760 105 ASP   A OD1 
2150 O  OD1 B ASP   A 105 ? 0.2924 0.2862 0.3201 0.0301  0.0118  -0.0469 105 ASP   A OD1 
2151 O  OD2 A ASP   A 105 ? 0.3834 0.4894 0.4140 -0.0189 0.0551  -0.0617 105 ASP   A OD2 
2152 O  OD2 B ASP   A 105 ? 0.2945 0.2894 0.3389 0.0323  0.0133  -0.0415 105 ASP   A OD2 
2161 N  N   A ILE   A 106 ? 0.2764 0.4209 0.2188 -0.0698 0.0123  -0.0680 106 ILE   A N   
2162 N  N   B ILE   A 106 ? 0.2792 0.2783 0.2329 -0.0079 0.0003  -0.0269 106 ILE   A N   
2163 C  CA  A ILE   A 106 ? 0.2531 0.4006 0.2346 -0.0842 -0.0172 -0.0796 106 ILE   A CA  
2164 C  CA  B ILE   A 106 ? 0.2817 0.2874 0.2582 -0.0214 -0.0029 -0.0305 106 ILE   A CA  
2165 C  C   A ILE   A 106 ? 0.2349 0.3720 0.2409 -0.1019 -0.0139 -0.0982 106 ILE   A C   
2166 C  C   B ILE   A 106 ? 0.2816 0.2888 0.2688 -0.0309 0.0057  -0.0304 106 ILE   A C   
2167 O  O   A ILE   A 106 ? 0.2133 0.3633 0.2429 -0.1082 0.0029  -0.1010 106 ILE   A O   
2168 O  O   B ILE   A 106 ? 0.2791 0.2895 0.2685 -0.0304 0.0085  -0.0291 106 ILE   A O   
2169 C  CB  A ILE   A 106 ? 0.2552 0.4095 0.2696 -0.0710 -0.0371 -0.0510 106 ILE   A CB  
2170 C  CB  B ILE   A 106 ? 0.2848 0.2961 0.2804 -0.0234 -0.0137 -0.0264 106 ILE   A CB  
2171 C  CG1 A ILE   A 106 ? 0.2491 0.4104 0.2951 -0.0578 -0.0441 -0.0299 106 ILE   A CG1 
2172 C  CG1 B ILE   A 106 ? 0.2835 0.3006 0.2954 -0.0206 -0.0185 -0.0205 106 ILE   A CG1 
2173 C  CG2 A ILE   A 106 ? 0.2632 0.4128 0.2817 -0.0690 -0.0408 -0.0479 106 ILE   A CG2 
2174 C  CG2 B ILE   A 106 ? 0.2874 0.2984 0.2847 -0.0256 -0.0162 -0.0260 106 ILE   A CG2 
2175 C  CD1 A ILE   A 106 ? 0.2499 0.4099 0.3080 -0.0444 -0.0403 -0.0171 106 ILE   A CD1 
2176 C  CD1 B ILE   A 106 ? 0.2836 0.3022 0.3037 -0.0167 -0.0189 -0.0174 106 ILE   A CD1 
2199 N  N   A GLN   A 107 ? 0.2517 0.3535 0.2701 -0.0973 -0.0019 -0.1053 107 GLN   A N   
2200 N  N   B GLN   A 107 ? 0.2835 0.2873 0.2840 -0.0387 0.0147  -0.0332 107 GLN   A N   
2201 C  CA  A GLN   A 107 ? 0.2744 0.3355 0.3389 -0.0784 0.0226  -0.0936 107 GLN   A CA  
2202 C  CA  B GLN   A 107 ? 0.2855 0.2870 0.3155 -0.0449 0.0241  -0.0351 107 GLN   A CA  
2203 C  C   A GLN   A 107 ? 0.2460 0.2870 0.3151 -0.0655 0.0516  -0.0728 107 GLN   A C   
2204 C  C   B GLN   A 107 ? 0.2552 0.2646 0.2913 -0.0511 0.0428  -0.0450 107 GLN   A C   
2205 O  O   A GLN   A 107 ? 0.2454 0.2828 0.3556 -0.0581 0.0738  -0.0737 107 GLN   A O   
2206 O  O   B GLN   A 107 ? 0.2601 0.2653 0.3089 -0.0517 0.0485  -0.0435 107 GLN   A O   
2207 C  CB  A GLN   A 107 ? 0.3167 0.3619 0.4325 -0.0787 0.0115  -0.0924 107 GLN   A CB  
2208 C  CB  B GLN   A 107 ? 0.3127 0.3069 0.3680 -0.0470 0.0135  -0.0251 107 GLN   A CB  
2209 C  CG  A GLN   A 107 ? 0.3636 0.3897 0.5304 -0.0734 0.0019  -0.0825 107 GLN   A CG  
2210 C  CG  B GLN   A 107 ? 0.3362 0.3238 0.4211 -0.0473 0.0032  -0.0139 107 GLN   A CG  
2211 C  CD  A GLN   A 107 ? 0.3989 0.4093 0.6142 -0.0696 -0.0043 -0.0708 107 GLN   A CD  
2212 C  CD  B GLN   A 107 ? 0.3562 0.3386 0.4675 -0.0455 -0.0051 -0.0034 107 GLN   A CD  
2213 O  OE1 A GLN   A 107 ? 0.4113 0.4167 0.6471 -0.0684 -0.0068 -0.0669 107 GLN   A OE1 
2214 O  OE1 B GLN   A 107 ? 0.3638 0.3448 0.4817 -0.0447 -0.0078 0.0011  107 GLN   A OE1 
2215 N  NE2 A GLN   A 107 ? 0.4078 0.4151 0.6424 -0.0694 -0.0071 -0.0691 107 GLN   A NE2 
2216 N  NE2 B GLN   A 107 ? 0.3624 0.3432 0.4819 -0.0447 -0.0103 0.0004  107 GLN   A NE2 
2233 N  N   . LEU   A 108 ? 0.2191 0.2416 0.2569 -0.0588 0.0499  -0.0602 108 LEU   A N   
2234 C  CA  . LEU   A 108 ? 0.1891 0.1949 0.2233 -0.0275 0.0411  -0.0263 108 LEU   A CA  
2235 C  C   . LEU   A 108 ? 0.1632 0.1494 0.2121 -0.0105 0.0398  0.0050  108 LEU   A C   
2236 O  O   . LEU   A 108 ? 0.1583 0.1482 0.2252 0.0034  0.0378  0.0043  108 LEU   A O   
2237 C  CB  . LEU   A 108 ? 0.1918 0.2057 0.2032 -0.0289 0.0462  -0.0240 108 LEU   A CB  
2238 C  CG  . LEU   A 108 ? 0.2072 0.2285 0.2310 -0.0266 0.0497  -0.0291 108 LEU   A CG  
2239 C  CD1 . LEU   A 108 ? 0.2264 0.2325 0.2389 -0.0344 0.0502  -0.0283 108 LEU   A CD1 
2240 C  CD2 . LEU   A 108 ? 0.2099 0.2488 0.2683 -0.0176 0.0461  -0.0213 108 LEU   A CD2 
2253 N  N   . LEU   A 109 ? 0.1516 0.1477 0.2016 0.0019  0.0286  0.0154  109 LEU   A N   
2254 C  CA  . LEU   A 109 ? 0.1435 0.1353 0.1837 0.0049  0.0134  0.0172  109 LEU   A CA  
2255 C  C   . LEU   A 109 ? 0.1321 0.1340 0.1775 -0.0050 0.0114  0.0106  109 LEU   A C   
2256 O  O   . LEU   A 109 ? 0.1425 0.1262 0.1885 -0.0045 -0.0001 0.0061  109 LEU   A O   
2257 C  CB  . LEU   A 109 ? 0.1503 0.1407 0.1972 0.0131  0.0098  0.0288  109 LEU   A CB  
2258 C  CG  . LEU   A 109 ? 0.1443 0.1508 0.2052 0.0067  0.0107  0.0311  109 LEU   A CG  
2259 C  CD1 . LEU   A 109 ? 0.1506 0.1403 0.2202 0.0018  0.0178  0.0144  109 LEU   A CD1 
2260 C  CD2 . LEU   A 109 ? 0.1437 0.1705 0.2234 0.0010  0.0105  0.0291  109 LEU   A CD2 
2272 N  N   . LYS   A 110 ? 0.1349 0.1314 0.1741 -0.0019 0.0036  0.0067  110 LYS   A N   
2273 C  CA  . LYS   A 110 ? 0.1360 0.1265 0.1821 -0.0068 -0.0005 0.0123  110 LYS   A CA  
2274 C  C   . LYS   A 110 ? 0.1346 0.1202 0.1660 -0.0082 -0.0011 -0.0017 110 LYS   A C   
2275 O  O   . LYS   A 110 ? 0.1294 0.1201 0.1805 -0.0096 0.0054  -0.0025 110 LYS   A O   
2276 C  CB  . LYS   A 110 ? 0.1405 0.1322 0.2052 -0.0074 -0.0070 0.0020  110 LYS   A CB  
2277 C  CG  . LYS   A 110 ? 0.1458 0.1307 0.2119 -0.0024 -0.0084 0.0014  110 LYS   A CG  
2278 C  CD  . LYS   A 110 ? 0.1478 0.1363 0.2226 -0.0105 -0.0075 -0.0048 110 LYS   A CD  
2279 C  CE  . LYS   A 110 ? 0.1535 0.1409 0.2323 -0.0085 0.0105  -0.0101 110 LYS   A CE  
2280 N  NZ  . LYS   A 110 ? 0.1565 0.1447 0.2448 -0.0140 0.0139  -0.0077 110 LYS   A NZ  
2294 N  N   . SER   A 111 ? 0.1335 0.1255 0.1761 -0.0018 0.0036  0.0021  111 SER   A N   
2295 C  CA  . SER   A 111 ? 0.1266 0.1294 0.1799 -0.0023 0.0099  0.0013  111 SER   A CA  
2296 C  C   . SER   A 111 ? 0.1251 0.1251 0.1723 -0.0059 0.0157  0.0061  111 SER   A C   
2297 O  O   . SER   A 111 ? 0.1376 0.1174 0.1922 -0.0090 0.0148  0.0111  111 SER   A O   
2298 C  CB  . SER   A 111 ? 0.1428 0.1480 0.1970 0.0008  0.0176  -0.0034 111 SER   A CB  
2299 O  OG  . SER   A 111 ? 0.1872 0.1710 0.1935 0.0050  0.0278  -0.0152 111 SER   A OG  
2305 N  N   . ALA   A 112 ? 0.1294 0.1173 0.1820 -0.0013 0.0171  0.0083  112 ALA   A N   
2306 C  CA  . ALA   A 112 ? 0.1348 0.1177 0.1781 -0.0044 0.0242  -0.0019 112 ALA   A CA  
2307 C  C   . ALA   A 112 ? 0.1247 0.1106 0.1846 -0.0050 0.0101  0.0038  112 ALA   A C   
2308 O  O   . ALA   A 112 ? 0.1267 0.1133 0.1937 -0.0128 0.0160  0.0098  112 ALA   A O   
2309 C  CB  . ALA   A 112 ? 0.1436 0.1235 0.1758 -0.0033 0.0163  0.0055  112 ALA   A CB  
2315 N  N   . TYR   A 113 ? 0.1198 0.1180 0.1814 -0.0030 0.0083  0.0077  113 TYR   A N   
2316 C  CA  . TYR   A 113 ? 0.1213 0.1134 0.1726 -0.0041 0.0162  0.0110  113 TYR   A CA  
2317 C  C   . TYR   A 113 ? 0.1155 0.1118 0.1779 -0.0101 0.0096  0.0100  113 TYR   A C   
2318 O  O   . TYR   A 113 ? 0.1224 0.1178 0.1869 -0.0083 0.0154  0.0051  113 TYR   A O   
2319 C  CB  . TYR   A 113 ? 0.1221 0.1219 0.1835 -0.0065 0.0060  0.0225  113 TYR   A CB  
2320 C  CG  . TYR   A 113 ? 0.1217 0.1266 0.1713 -0.0100 0.0117  0.0203  113 TYR   A CG  
2321 C  CD1 . TYR   A 113 ? 0.1235 0.1321 0.1699 0.0017  0.0116  0.0180  113 TYR   A CD1 
2322 C  CD2 . TYR   A 113 ? 0.1269 0.1287 0.1661 -0.0097 0.0056  0.0187  113 TYR   A CD2 
2323 C  CE1 . TYR   A 113 ? 0.1286 0.1419 0.1623 -0.0077 0.0063  0.0264  113 TYR   A CE1 
2324 C  CE2 . TYR   A 113 ? 0.1285 0.1379 0.1637 -0.0095 0.0048  0.0226  113 TYR   A CE2 
2325 C  CZ  . TYR   A 113 ? 0.1275 0.1396 0.1588 0.0023  0.0144  0.0256  113 TYR   A CZ  
2326 O  OH  . TYR   A 113 ? 0.1265 0.1481 0.1747 0.0105  0.0140  0.0256  113 TYR   A OH  
2336 N  N   . GLU   A 114 ? 0.1153 0.1134 0.1865 -0.0018 0.0167  0.0086  114 GLU   A N   
2337 C  CA  . GLU   A 114 ? 0.1191 0.1071 0.1974 0.0034  0.0084  0.0164  114 GLU   A CA  
2338 C  C   . GLU   A 114 ? 0.1148 0.1182 0.1949 0.0022  0.0121  0.0100  114 GLU   A C   
2339 O  O   . GLU   A 114 ? 0.1284 0.1201 0.1887 -0.0004 0.0021  0.0116  114 GLU   A O   
2340 C  CB  . GLU   A 114 ? 0.1215 0.1113 0.1926 -0.0041 0.0042  0.0188  114 GLU   A CB  
2341 C  CG  . GLU   A 114 ? 0.1299 0.1184 0.2028 -0.0002 0.0109  0.0044  114 GLU   A CG  
2342 C  CD  . GLU   A 114 ? 0.1359 0.1192 0.2053 -0.0079 0.0060  0.0053  114 GLU   A CD  
2343 O  OE1 . GLU   A 114 ? 0.1383 0.1185 0.2105 -0.0085 0.0175  -0.0034 114 GLU   A OE1 
2344 O  OE2 . GLU   A 114 ? 0.1571 0.1268 0.2198 -0.0122 0.0104  -0.0065 114 GLU   A OE2 
2351 N  N   . ASN   A 115 ? 0.1237 0.1205 0.1731 -0.0061 0.0155  0.0072  115 ASN   A N   
2352 C  CA  . ASN   A 115 ? 0.1243 0.1240 0.1740 -0.0099 0.0138  0.0104  115 ASN   A CA  
2353 C  C   . ASN   A 115 ? 0.1252 0.1223 0.1664 -0.0153 0.0014  0.0039  115 ASN   A C   
2354 O  O   . ASN   A 115 ? 0.1252 0.1314 0.1705 -0.0100 0.0127  0.0168  115 ASN   A O   
2355 C  CB  . ASN   A 115 ? 0.1339 0.1356 0.1738 -0.0170 0.0051  0.0095  115 ASN   A CB  
2356 C  CG  . ASN   A 115 ? 0.1333 0.1529 0.1757 -0.0217 0.0233  0.0110  115 ASN   A CG  
2357 O  OD1 . ASN   A 115 ? 0.1374 0.2477 0.2110 -0.0178 0.0306  0.0207  115 ASN   A OD1 
2358 N  ND2 . ASN   A 115 ? 0.1363 0.1307 0.1696 -0.0141 0.0296  0.0141  115 ASN   A ND2 
2365 N  N   . PHE   A 116 ? 0.1193 0.1195 0.1806 -0.0015 0.0145  0.0198  116 PHE   A N   
2366 C  CA  . PHE   A 116 ? 0.1198 0.1285 0.1733 -0.0006 0.0155  0.0173  116 PHE   A CA  
2367 C  C   . PHE   A 116 ? 0.1170 0.1334 0.1807 -0.0082 0.0159  0.0221  116 PHE   A C   
2368 O  O   . PHE   A 116 ? 0.1235 0.1397 0.1870 -0.0017 0.0124  0.0336  116 PHE   A O   
2369 C  CB  . PHE   A 116 ? 0.1246 0.1200 0.1796 -0.0050 0.0182  0.0217  116 PHE   A CB  
2370 C  CG  . PHE   A 116 ? 0.1247 0.1241 0.1669 -0.0087 0.0130  0.0154  116 PHE   A CG  
2371 C  CD1 . PHE   A 116 ? 0.1259 0.1200 0.1694 -0.0105 0.0089  0.0149  116 PHE   A CD1 
2372 C  CD2 . PHE   A 116 ? 0.1308 0.1268 0.1731 -0.0078 0.0141  0.0205  116 PHE   A CD2 
2373 C  CE1 . PHE   A 116 ? 0.1328 0.1175 0.1806 -0.0157 0.0045  0.0100  116 PHE   A CE1 
2374 C  CE2 . PHE   A 116 ? 0.1290 0.1260 0.1841 -0.0057 0.0147  0.0112  116 PHE   A CE2 
2375 C  CZ  . PHE   A 116 ? 0.1320 0.1121 0.1761 -0.0022 0.0042  0.0074  116 PHE   A CZ  
2385 N  N   . ASN   A 117 ? 0.1219 0.1305 0.1955 -0.0049 0.0151  0.0270  117 ASN   A N   
2386 C  CA  . ASN   A 117 ? 0.1200 0.1282 0.1953 -0.0059 0.0118  0.0260  117 ASN   A CA  
2387 C  C   . ASN   A 117 ? 0.1247 0.1362 0.2064 -0.0022 0.0067  0.0256  117 ASN   A C   
2388 O  O   . ASN   A 117 ? 0.1347 0.1449 0.2192 -0.0069 -0.0146 0.0406  117 ASN   A O   
2389 C  CB  . ASN   A 117 ? 0.1266 0.1318 0.1976 -0.0005 0.0110  0.0317  117 ASN   A CB  
2390 C  CG  . ASN   A 117 ? 0.1224 0.1300 0.1981 -0.0030 0.0088  0.0282  117 ASN   A CG  
2391 O  OD1 . ASN   A 117 ? 0.1239 0.1486 0.2102 -0.0107 0.0121  0.0195  117 ASN   A OD1 
2392 N  ND2 . ASN   A 117 ? 0.1216 0.1248 0.2067 -0.0025 0.0123  0.0270  117 ASN   A ND2 
2399 N  N   . GLN   A 118 ? 0.1231 0.1326 0.2085 -0.0092 -0.0000 0.0325  118 GLN   A N   
2400 C  CA  . GLN   A 118 ? 0.1283 0.1479 0.2109 -0.0075 -0.0007 0.0280  118 GLN   A CA  
2401 C  C   . GLN   A 118 ? 0.1308 0.1566 0.1989 -0.0102 -0.0030 0.0364  118 GLN   A C   
2402 O  O   . GLN   A 118 ? 0.1324 0.1847 0.2252 -0.0058 -0.0119 0.0144  118 GLN   A O   
2403 C  CB  . GLN   A 118 ? 0.1298 0.1485 0.2238 -0.0027 0.0075  0.0249  118 GLN   A CB  
2404 C  CG  . GLN   A 118 ? 0.1262 0.1472 0.2165 -0.0049 0.0097  0.0289  118 GLN   A CG  
2405 C  CD  . GLN   A 118 ? 0.1267 0.1532 0.2327 -0.0007 0.0080  0.0255  118 GLN   A CD  
2406 O  OE1 . GLN   A 118 ? 0.1299 0.1642 0.2483 0.0096  0.0025  0.0210  118 GLN   A OE1 
2407 N  NE2 . GLN   A 118 ? 0.1386 0.1492 0.2273 0.0021  0.0014  0.0300  118 GLN   A NE2 
2416 N  N   . HIS   A 119 ? 0.1369 0.1527 0.1968 -0.0047 -0.0016 0.0390  119 HIS   A N   
2417 C  CA  . HIS   A 119 ? 0.1389 0.1583 0.1868 -0.0074 -0.0015 0.0406  119 HIS   A CA  
2418 C  C   . HIS   A 119 ? 0.1492 0.1689 0.1815 -0.0124 0.0028  0.0411  119 HIS   A C   
2419 O  O   . HIS   A 119 ? 0.1508 0.1770 0.1899 -0.0288 -0.0055 0.0433  119 HIS   A O   
2420 C  CB  . HIS   A 119 ? 0.1464 0.1528 0.2103 -0.0041 0.0130  0.0382  119 HIS   A CB  
2421 C  CG  . HIS   A 119 ? 0.1506 0.1553 0.2440 0.0027  0.0125  0.0454  119 HIS   A CG  
2422 N  ND1 . HIS   A 119 ? 0.1657 0.1756 0.2971 -0.0120 0.0095  0.0337  119 HIS   A ND1 
2423 C  CD2 . HIS   A 119 ? 0.1651 0.1624 0.2548 0.0152  0.0345  0.0589  119 HIS   A CD2 
2424 C  CE1 . HIS   A 119 ? 0.1663 0.1727 0.3054 -0.0138 0.0279  0.0566  119 HIS   A CE1 
2425 N  NE2 . HIS   A 119 ? 0.1727 0.1683 0.2950 0.0030  0.0444  0.0675  119 HIS   A NE2 
2433 N  N   . GLU   A 120 ? 0.1559 0.1897 0.1877 -0.0078 -0.0099 0.0659  120 GLU   A N   
2434 C  CA  . GLU   A 120 ? 0.1784 0.2206 0.2218 -0.0015 -0.0123 0.1104  120 GLU   A CA  
2435 C  C   . GLU   A 120 ? 0.1601 0.2085 0.1980 -0.0125 -0.0034 0.1031  120 GLU   A C   
2436 O  O   . GLU   A 120 ? 0.1588 0.2017 0.2138 -0.0181 -0.0033 0.0946  120 GLU   A O   
2437 C  CB  . GLU   A 120 ? 0.2465 0.2816 0.2767 0.0138  -0.0100 0.1603  120 GLU   A CB  
2438 C  CG  . GLU   A 120 ? 0.3444 0.3566 0.3863 0.0247  -0.0101 0.1657  120 GLU   A CG  
2439 C  CD  . GLU   A 120 ? 0.4254 0.4203 0.5045 0.0343  -0.0020 0.1509  120 GLU   A CD  
2440 O  OE1 . GLU   A 120 ? 0.4485 0.4393 0.5296 0.0368  0.0001  0.1453  120 GLU   A OE1 
2441 O  OE2 . GLU   A 120 ? 0.4651 0.4651 0.5625 0.0369  0.0011  0.1447  120 GLU   A OE2 
2448 N  N   . VAL   A 121 ? 0.1562 0.2092 0.1715 -0.0105 -0.0012 0.0808  121 VAL   A N   
2449 C  CA  . VAL   A 121 ? 0.1622 0.2121 0.1529 -0.0151 0.0074  0.0776  121 VAL   A CA  
2450 C  C   . VAL   A 121 ? 0.1535 0.1924 0.1413 -0.0213 0.0025  0.0541  121 VAL   A C   
2451 O  O   . VAL   A 121 ? 0.1572 0.1924 0.1585 -0.0294 -0.0131 0.0487  121 VAL   A O   
2452 C  CB  . VAL   A 121 ? 0.1995 0.2457 0.1878 -0.0054 0.0117  0.0790  121 VAL   A CB  
2453 C  CG1 . VAL   A 121 ? 0.2016 0.2602 0.1900 0.0014  0.0255  0.0769  121 VAL   A CG1 
2454 C  CG2 . VAL   A 121 ? 0.2212 0.2614 0.2301 -0.0121 0.0146  0.0671  121 VAL   A CG2 
2464 N  N   . LEU   A 122 ? 0.1424 0.1717 0.1532 -0.0214 0.0022  0.0474  122 LEU   A N   
2465 C  CA  . LEU   A 122 ? 0.1499 0.1549 0.1455 -0.0216 0.0129  0.0407  122 LEU   A CA  
2466 C  C   . LEU   A 122 ? 0.1440 0.1537 0.1471 -0.0294 -0.0028 0.0356  122 LEU   A C   
2467 O  O   . LEU   A 122 ? 0.1460 0.1615 0.1753 -0.0323 -0.0026 0.0355  122 LEU   A O   
2468 C  CB  . LEU   A 122 ? 0.1655 0.1551 0.1743 -0.0101 0.0051  0.0456  122 LEU   A CB  
2469 C  CG  . LEU   A 122 ? 0.1619 0.1607 0.1795 -0.0090 0.0084  0.0367  122 LEU   A CG  
2470 C  CD1 . LEU   A 122 ? 0.1820 0.1635 0.1873 -0.0199 0.0187  0.0371  122 LEU   A CD1 
2471 C  CD2 . LEU   A 122 ? 0.1572 0.1563 0.1750 -0.0064 0.0248  0.0355  122 LEU   A CD2 
2483 N  N   . LEU   A 123 ? 0.1360 0.1555 0.1421 -0.0278 -0.0024 0.0295  123 LEU   A N   
2484 C  CA  . LEU   A 123 ? 0.1391 0.1499 0.1322 -0.0218 0.0087  0.0286  123 LEU   A CA  
2485 C  C   . LEU   A 123 ? 0.1373 0.1455 0.1276 -0.0175 0.0040  0.0332  123 LEU   A C   
2486 O  O   . LEU   A 123 ? 0.1332 0.1619 0.1399 -0.0301 0.0047  0.0343  123 LEU   A O   
2487 C  CB  . LEU   A 123 ? 0.1497 0.1615 0.1406 -0.0243 0.0056  0.0271  123 LEU   A CB  
2488 C  CG  . LEU   A 123 ? 0.1497 0.1750 0.1521 -0.0201 0.0129  0.0117  123 LEU   A CG  
2489 C  CD1 . LEU   A 123 ? 0.1563 0.1818 0.1593 -0.0151 0.0102  0.0031  123 LEU   A CD1 
2490 C  CD2 . LEU   A 123 ? 0.1671 0.1814 0.1581 -0.0154 0.0060  0.0185  123 LEU   A CD2 
2502 N  N   A ALA   A 124 ? 0.1306 0.1344 0.1264 -0.0154 0.0091  0.0250  124 ALA   A N   
2503 N  N   B ALA   A 124 ? 0.1357 0.1465 0.1214 -0.0147 -0.0009 0.0232  124 ALA   A N   
2504 C  CA  A ALA   A 124 ? 0.1244 0.1282 0.1306 -0.0112 0.0056  0.0220  124 ALA   A CA  
2505 C  CA  B ALA   A 124 ? 0.1346 0.1498 0.1196 -0.0156 -0.0070 0.0218  124 ALA   A CA  
2506 C  C   A ALA   A 124 ? 0.1183 0.1298 0.1323 -0.0078 0.0101  0.0245  124 ALA   A C   
2507 C  C   B ALA   A 124 ? 0.1413 0.1539 0.1121 -0.0140 -0.0010 0.0216  124 ALA   A C   
2508 O  O   A ALA   A 124 ? 0.1200 0.1295 0.1536 -0.0161 0.0177  0.0276  124 ALA   A O   
2509 O  O   B ALA   A 124 ? 0.1459 0.1565 0.1115 -0.0144 0.0064  0.0251  124 ALA   A O   
2510 C  CB  A ALA   A 124 ? 0.1258 0.1263 0.1529 -0.0103 0.0071  0.0239  124 ALA   A CB  
2511 C  CB  B ALA   A 124 ? 0.1266 0.1482 0.1260 -0.0131 -0.0106 0.0236  124 ALA   A CB  
2522 N  N   A PRO   A 125 ? 0.1129 0.1265 0.1356 -0.0130 0.0085  0.0346  125 PRO   A N   
2523 N  N   B PRO   A 125 ? 0.1439 0.1535 0.1165 -0.0155 -0.0015 0.0237  125 PRO   A N   
2524 C  CA  A PRO   A 125 ? 0.1231 0.1239 0.1361 -0.0046 0.0075  0.0202  125 PRO   A CA  
2525 C  CA  B PRO   A 125 ? 0.1495 0.1539 0.1232 -0.0136 -0.0005 0.0133  125 PRO   A CA  
2526 C  C   A PRO   A 125 ? 0.1167 0.1208 0.1368 -0.0041 0.0076  0.0266  125 PRO   A C   
2527 C  C   B PRO   A 125 ? 0.1493 0.1571 0.1304 -0.0111 0.0002  0.0078  125 PRO   A C   
2528 O  O   A PRO   A 125 ? 0.1180 0.1192 0.1493 0.0034  0.0067  0.0190  125 PRO   A O   
2529 O  O   B PRO   A 125 ? 0.1472 0.1602 0.1340 -0.0111 0.0012  0.0080  125 PRO   A O   
2530 C  CB  A PRO   A 125 ? 0.1360 0.1217 0.1316 -0.0117 0.0098  0.0183  125 PRO   A CB  
2531 C  CB  B PRO   A 125 ? 0.1518 0.1518 0.1220 -0.0157 0.0018  0.0140  125 PRO   A CB  
2532 C  CG  A PRO   A 125 ? 0.1330 0.1166 0.1342 -0.0110 0.0152  0.0261  125 PRO   A CG  
2533 C  CG  B PRO   A 125 ? 0.1524 0.1534 0.1286 -0.0184 0.0006  0.0135  125 PRO   A CG  
2534 C  CD  A PRO   A 125 ? 0.1184 0.1312 0.1436 -0.0185 0.0161  0.0305  125 PRO   A CD  
2535 C  CD  B PRO   A 125 ? 0.1472 0.1564 0.1268 -0.0182 0.0019  0.0196  125 PRO   A CD  
2550 N  N   A LEU   A 126 ? 0.1102 0.1284 0.1379 0.0022  0.0124  0.0235  126 LEU   A N   
2551 N  N   B LEU   A 126 ? 0.1553 0.1564 0.1433 -0.0082 -0.0056 0.0006  126 LEU   A N   
2552 C  CA  A LEU   A 126 ? 0.1092 0.1287 0.1450 0.0016  0.0132  0.0173  126 LEU   A CA  
2553 C  CA  B LEU   A 126 ? 0.1591 0.1577 0.1556 -0.0038 -0.0042 -0.0012 126 LEU   A CA  
2554 C  C   A LEU   A 126 ? 0.1174 0.1242 0.1464 0.0060  0.0048  0.0125  126 LEU   A C   
2555 C  C   B LEU   A 126 ? 0.1512 0.1475 0.1461 0.0081  0.0045  -0.0097 126 LEU   A C   
2556 O  O   A LEU   A 126 ? 0.1273 0.1283 0.1771 0.0111  0.0205  0.0269  126 LEU   A O   
2557 O  O   B LEU   A 126 ? 0.1566 0.1496 0.1593 0.0044  -0.0009 -0.0006 126 LEU   A O   
2558 C  CB  A LEU   A 126 ? 0.1134 0.1333 0.1477 -0.0013 0.0099  0.0165  126 LEU   A CB  
2559 C  CB  B LEU   A 126 ? 0.1712 0.1749 0.1943 -0.0124 -0.0100 0.0013  126 LEU   A CB  
2560 C  CG  A LEU   A 126 ? 0.1169 0.1564 0.1451 -0.0148 0.0155  0.0119  126 LEU   A CG  
2561 C  CG  B LEU   A 126 ? 0.1813 0.1882 0.2281 -0.0160 -0.0167 0.0095  126 LEU   A CG  
2562 C  CD1 A LEU   A 126 ? 0.1275 0.1757 0.1711 -0.0208 0.0085  0.0086  126 LEU   A CD1 
2563 C  CD1 B LEU   A 126 ? 0.1864 0.1909 0.2408 -0.0177 -0.0171 0.0107  126 LEU   A CD1 
2564 C  CD2 A LEU   A 126 ? 0.1296 0.1517 0.1618 -0.0253 0.0095  0.0141  126 LEU   A CD2 
2565 C  CD2 B LEU   A 126 ? 0.1823 0.1940 0.2314 -0.0165 -0.0204 0.0134  126 LEU   A CD2 
2588 N  N   A LEU   A 127 ? 0.1257 0.1289 0.1323 0.0004  0.0063  0.0165  127 LEU   A N   
2589 N  N   B LEU   A 127 ? 0.1451 0.1417 0.1371 0.0150  0.0117  -0.0098 127 LEU   A N   
2590 C  CA  A LEU   A 127 ? 0.1222 0.1313 0.1206 -0.0017 0.0010  0.0076  127 LEU   A CA  
2591 C  CA  B LEU   A 127 ? 0.1424 0.1452 0.1334 0.0117  0.0082  -0.0010 127 LEU   A CA  
2592 C  C   A LEU   A 127 ? 0.1176 0.1224 0.1173 0.0022  0.0017  0.0060  127 LEU   A C   
2593 C  C   B LEU   A 127 ? 0.1454 0.1449 0.1348 0.0011  0.0114  -0.0037 127 LEU   A C   
2594 O  O   A LEU   A 127 ? 0.1220 0.1228 0.1284 -0.0128 -0.0016 0.0107  127 LEU   A O   
2595 O  O   B LEU   A 127 ? 0.1501 0.1432 0.1487 -0.0027 0.0198  -0.0055 127 LEU   A O   
2596 C  CB  A LEU   A 127 ? 0.1344 0.1435 0.1377 0.0095  0.0070  0.0124  127 LEU   A CB  
2597 C  CB  B LEU   A 127 ? 0.1389 0.1520 0.1280 0.0152  -0.0002 0.0031  127 LEU   A CB  
2598 C  CG  A LEU   A 127 ? 0.1441 0.1455 0.1550 0.0108  0.0003  0.0126  127 LEU   A CG  
2599 C  CG  B LEU   A 127 ? 0.1327 0.1591 0.1248 0.0198  -0.0108 0.0131  127 LEU   A CG  
2600 C  CD1 A LEU   A 127 ? 0.1445 0.1337 0.1694 0.0041  -0.0009 0.0105  127 LEU   A CD1 
2601 C  CD1 B LEU   A 127 ? 0.1332 0.1638 0.1293 0.0219  -0.0009 0.0174  127 LEU   A CD1 
2602 C  CD2 A LEU   A 127 ? 0.1563 0.1414 0.1748 0.0244  -0.0087 0.0121  127 LEU   A CD2 
2603 C  CD2 B LEU   A 127 ? 0.1360 0.1673 0.1244 0.0211  -0.0188 0.0088  127 LEU   A CD2 
2626 N  N   A SER   A 128 ? 0.1239 0.1235 0.1262 -0.0050 -0.0017 0.0159  128 SER   A N   
2627 N  N   B SER   A 128 ? 0.1430 0.1477 0.1362 -0.0072 0.0072  0.0051  128 SER   A N   
2628 C  CA  A SER   A 128 ? 0.1376 0.1244 0.1264 -0.0026 0.0001  0.0129  128 SER   A CA  
2629 C  CA  B SER   A 128 ? 0.1426 0.1509 0.1372 -0.0154 -0.0030 0.0132  128 SER   A CA  
2630 C  C   A SER   A 128 ? 0.1442 0.1232 0.1309 0.0083  -0.0040 0.0197  128 SER   A C   
2631 C  C   B SER   A 128 ? 0.1478 0.1495 0.1423 -0.0214 -0.0090 0.0218  128 SER   A C   
2632 O  O   A SER   A 128 ? 0.1593 0.1450 0.1610 0.0137  -0.0074 0.0132  128 SER   A O   
2633 O  O   B SER   A 128 ? 0.1472 0.1493 0.1468 -0.0311 -0.0119 0.0225  128 SER   A O   
2634 C  CB  A SER   A 128 ? 0.1430 0.1384 0.1376 -0.0019 0.0009  0.0081  128 SER   A CB  
2635 C  CB  B SER   A 128 ? 0.1370 0.1539 0.1296 -0.0176 -0.0069 0.0108  128 SER   A CB  
2636 O  OG  A SER   A 128 ? 0.1446 0.1470 0.1523 -0.0030 0.0070  0.0099  128 SER   A OG  
2637 O  OG  B SER   A 128 ? 0.1325 0.1559 0.1324 -0.0185 -0.0038 0.0095  128 SER   A OG  
2648 N  N   A ALA   A 129 ? 0.1379 0.1280 0.1540 0.0069  -0.0059 0.0239  129 ALA   A N   
2649 N  N   B ALA   A 129 ? 0.1549 0.1558 0.1540 -0.0173 -0.0124 0.0312  129 ALA   A N   
2650 C  CA  A ALA   A 129 ? 0.1283 0.1296 0.1731 0.0102  0.0012  0.0291  129 ALA   A CA  
2651 C  CA  B ALA   A 129 ? 0.1626 0.1618 0.1663 -0.0170 -0.0160 0.0337  129 ALA   A CA  
2652 C  C   A ALA   A 129 ? 0.1334 0.1298 0.1453 0.0069  -0.0027 0.0139  129 ALA   A C   
2653 C  C   B ALA   A 129 ? 0.1692 0.1620 0.1706 -0.0228 -0.0197 0.0226  129 ALA   A C   
2654 O  O   A ALA   A 129 ? 0.1387 0.1351 0.1349 0.0012  -0.0029 0.0153  129 ALA   A O   
2655 O  O   B ALA   A 129 ? 0.1692 0.1618 0.1735 -0.0255 -0.0188 0.0198  129 ALA   A O   
2656 C  CB  A ALA   A 129 ? 0.1328 0.1480 0.2046 0.0140  0.0096  0.0514  129 ALA   A CB  
2657 C  CB  B ALA   A 129 ? 0.1671 0.1720 0.1771 -0.0119 -0.0163 0.0392  129 ALA   A CB  
2668 N  N   A GLY   A 130 ? 0.1347 0.1257 0.1491 0.0051  -0.0023 0.0209  130 GLY   A N   
2669 N  N   B GLY   A 130 ? 0.1786 0.1637 0.1719 -0.0248 -0.0210 0.0258  130 GLY   A N   
2670 C  CA  A GLY   A 130 ? 0.1538 0.1284 0.1486 0.0064  -0.0004 0.0186  130 GLY   A CA  
2671 C  CA  B GLY   A 130 ? 0.1879 0.1642 0.1797 -0.0238 -0.0239 0.0225  130 GLY   A CA  
2672 C  C   A GLY   A 130 ? 0.1552 0.1272 0.1478 0.0044  -0.0026 0.0189  130 GLY   A C   
2673 C  C   B GLY   A 130 ? 0.1915 0.1683 0.1822 -0.0219 -0.0297 0.0260  130 GLY   A C   
2674 O  O   A GLY   A 130 ? 0.1546 0.1183 0.1443 -0.0006 -0.0124 0.0245  130 GLY   A O   
2675 O  O   B GLY   A 130 ? 0.2000 0.1699 0.1890 -0.0204 -0.0295 0.0319  130 GLY   A O   
2682 N  N   A ILE   A 131 ? 0.1627 0.1292 0.1595 -0.0063 -0.0065 0.0188  131 ILE   A N   
2683 N  N   B ILE   A 131 ? 0.1867 0.1656 0.1796 -0.0197 -0.0301 0.0283  131 ILE   A N   
2684 C  CA  A ILE   A 131 ? 0.1720 0.1312 0.1376 -0.0144 -0.0181 0.0158  131 ILE   A CA  
2685 C  CA  B ILE   A 131 ? 0.1835 0.1620 0.1720 -0.0112 -0.0357 0.0287  131 ILE   A CA  
2686 C  C   A ILE   A 131 ? 0.1663 0.1384 0.1280 -0.0117 -0.0121 0.0239  131 ILE   A C   
2687 C  C   B ILE   A 131 ? 0.1828 0.1645 0.1641 -0.0063 -0.0303 0.0289  131 ILE   A C   
2688 O  O   A ILE   A 131 ? 0.1779 0.1481 0.1423 -0.0054 -0.0054 0.0302  131 ILE   A O   
2689 O  O   B ILE   A 131 ? 0.1899 0.1672 0.1710 -0.0052 -0.0265 0.0299  131 ILE   A O   
2690 C  CB  A ILE   A 131 ? 0.1861 0.1444 0.1499 -0.0267 -0.0182 -0.0001 131 ILE   A CB  
2691 C  CB  B ILE   A 131 ? 0.1790 0.1651 0.1740 -0.0048 -0.0487 0.0227  131 ILE   A CB  
2692 C  CG1 A ILE   A 131 ? 0.1910 0.1808 0.1669 -0.0288 -0.0272 -0.0123 131 ILE   A CG1 
2693 C  CG1 B ILE   A 131 ? 0.1779 0.1756 0.1799 0.0010  -0.0506 0.0216  131 ILE   A CG1 
2694 C  CG2 A ILE   A 131 ? 0.2010 0.1303 0.1654 -0.0147 -0.0180 -0.0131 131 ILE   A CG2 
2695 C  CG2 B ILE   A 131 ? 0.1748 0.1619 0.1734 -0.0075 -0.0510 0.0138  131 ILE   A CG2 
2696 C  CD1 A ILE   A 131 ? 0.1960 0.1969 0.2058 -0.0281 -0.0261 -0.0188 131 ILE   A CD1 
2697 C  CD1 B ILE   A 131 ? 0.1769 0.1795 0.1875 0.0051  -0.0580 0.0164  131 ILE   A CD1 
2720 N  N   A PHE   A 132 ? 0.1599 0.1338 0.1342 -0.0151 -0.0045 0.0227  132 PHE   A N   
2721 N  N   B PHE   A 132 ? 0.1773 0.1643 0.1638 -0.0013 -0.0242 0.0261  132 PHE   A N   
2722 C  CA  A PHE   A 132 ? 0.1614 0.1378 0.1353 -0.0173 -0.0013 0.0187  132 PHE   A CA  
2723 C  CA  B PHE   A 132 ? 0.1757 0.1611 0.1621 -0.0016 -0.0171 0.0233  132 PHE   A CA  
2724 C  C   A PHE   A 132 ? 0.1649 0.1518 0.1377 -0.0199 -0.0062 0.0172  132 PHE   A C   
2725 C  C   B PHE   A 132 ? 0.1828 0.1726 0.1674 -0.0022 -0.0144 0.0302  132 PHE   A C   
2726 O  O   A PHE   A 132 ? 0.1753 0.1562 0.1329 -0.0275 -0.0040 0.0241  132 PHE   A O   
2727 O  O   B PHE   A 132 ? 0.1918 0.1820 0.1660 -0.0079 -0.0073 0.0419  132 PHE   A O   
2728 C  CB  A PHE   A 132 ? 0.1599 0.1350 0.1397 -0.0146 -0.0044 0.0194  132 PHE   A CB  
2729 C  CB  B PHE   A 132 ? 0.1646 0.1487 0.1447 -0.0032 -0.0078 0.0181  132 PHE   A CB  
2730 C  CG  A PHE   A 132 ? 0.1631 0.1370 0.1352 -0.0028 -0.0142 0.0217  132 PHE   A CG  
2731 C  CG  B PHE   A 132 ? 0.1597 0.1423 0.1345 0.0030  -0.0064 0.0057  132 PHE   A CG  
2732 C  CD1 A PHE   A 132 ? 0.1631 0.1468 0.1465 0.0037  -0.0151 0.0126  132 PHE   A CD1 
2733 C  CD1 B PHE   A 132 ? 0.1588 0.1459 0.1379 0.0091  -0.0001 -0.0014 132 PHE   A CD1 
2734 C  CD2 A PHE   A 132 ? 0.1631 0.1478 0.1498 0.0002  -0.0119 0.0086  132 PHE   A CD2 
2735 C  CD2 B PHE   A 132 ? 0.1556 0.1417 0.1309 0.0053  -0.0090 -0.0072 132 PHE   A CD2 
2736 C  CE1 A PHE   A 132 ? 0.1653 0.1546 0.1571 -0.0053 -0.0179 0.0119  132 PHE   A CE1 
2737 C  CE1 B PHE   A 132 ? 0.1567 0.1481 0.1344 0.0096  -0.0048 0.0034  132 PHE   A CE1 
2738 C  CE2 A PHE   A 132 ? 0.1633 0.1545 0.1558 -0.0021 -0.0193 0.0089  132 PHE   A CE2 
2739 C  CE2 B PHE   A 132 ? 0.1527 0.1463 0.1323 0.0091  -0.0123 -0.0066 132 PHE   A CE2 
2740 C  CZ  A PHE   A 132 ? 0.1637 0.1588 0.1618 -0.0060 -0.0230 0.0089  132 PHE   A CZ  
2741 C  CZ  B PHE   A 132 ? 0.1531 0.1488 0.1317 0.0089  -0.0093 0.0007  132 PHE   A CZ  
2760 N  N   A GLY   A 133 ? 0.1648 0.1588 0.1371 -0.0176 -0.0220 0.0156  133 GLY   A N   
2761 N  N   B GLY   A 133 ? 0.1822 0.1749 0.1674 -0.0022 -0.0179 0.0224  133 GLY   A N   
2762 C  CA  A GLY   A 133 ? 0.1760 0.1716 0.1499 -0.0196 -0.0248 0.0201  133 GLY   A CA  
2763 C  CA  B GLY   A 133 ? 0.1831 0.1792 0.1685 -0.0006 -0.0174 0.0139  133 GLY   A CA  
2764 C  C   A GLY   A 133 ? 0.1834 0.1781 0.1529 -0.0178 -0.0384 0.0070  133 GLY   A C   
2765 C  C   B GLY   A 133 ? 0.1813 0.1838 0.1641 0.0059  -0.0202 -0.0058 133 GLY   A C   
2766 O  O   A GLY   A 133 ? 0.2042 0.1901 0.1586 -0.0140 -0.0324 -0.0124 133 GLY   A O   
2767 O  O   B GLY   A 133 ? 0.1854 0.1876 0.1549 0.0103  -0.0216 -0.0273 133 GLY   A O   
2774 N  N   A ALA   A 134 ? 0.1818 0.1636 0.1439 -0.0220 -0.0336 0.0080  134 ALA   A N   
2775 N  N   B ALA   A 134 ? 0.1808 0.1817 0.1679 0.0051  -0.0174 -0.0041 134 ALA   A N   
2776 C  CA  A ALA   A 134 ? 0.1848 0.1642 0.1668 -0.0200 -0.0260 0.0044  134 ALA   A CA  
2777 C  CA  B ALA   A 134 ? 0.1792 0.1822 0.1750 0.0048  -0.0174 -0.0030 134 ALA   A CA  
2778 C  C   A ALA   A 134 ? 0.1852 0.1693 0.1735 -0.0221 -0.0259 0.0088  134 ALA   A C   
2779 C  C   B ALA   A 134 ? 0.1776 0.1797 0.1773 -0.0004 -0.0220 0.0032  134 ALA   A C   
2780 O  O   A ALA   A 134 ? 0.1992 0.1787 0.1934 -0.0268 -0.0158 0.0051  134 ALA   A O   
2781 O  O   B ALA   A 134 ? 0.1782 0.1823 0.1875 -0.0044 -0.0202 0.0044  134 ALA   A O   
2782 C  CB  A ALA   A 134 ? 0.1978 0.1641 0.2023 -0.0141 -0.0247 -0.0013 134 ALA   A CB  
2783 C  CB  B ALA   A 134 ? 0.1848 0.1841 0.1901 0.0084  -0.0146 -0.0039 134 ALA   A CB  
2794 N  N   A ASP   A 135 ? 0.1832 0.1689 0.1834 -0.0197 -0.0281 0.0236  135 ASP   A N   
2795 N  N   B ASP   A 135 ? 0.1839 0.1818 0.1856 -0.0038 -0.0267 0.0133  135 ASP   A N   
2796 C  CA  A ASP   A 135 ? 0.1752 0.1817 0.2144 -0.0258 -0.0423 0.0283  135 ASP   A CA  
2797 C  CA  B ASP   A 135 ? 0.1856 0.1839 0.2023 -0.0065 -0.0284 0.0161  135 ASP   A CA  
2798 C  C   A ASP   A 135 ? 0.1642 0.1673 0.2244 -0.0221 -0.0259 0.0379  135 ASP   A C   
2799 C  C   B ASP   A 135 ? 0.1772 0.1722 0.1962 -0.0022 -0.0225 0.0122  135 ASP   A C   
2800 O  O   A ASP   A 135 ? 0.1600 0.1611 0.2234 -0.0163 -0.0279 0.0432  135 ASP   A O   
2801 O  O   B ASP   A 135 ? 0.1734 0.1675 0.1927 -0.0002 -0.0235 0.0196  135 ASP   A O   
2802 C  CB  A ASP   A 135 ? 0.1940 0.2156 0.2570 -0.0411 -0.0550 0.0218  135 ASP   A CB  
2803 C  CB  B ASP   A 135 ? 0.1947 0.2002 0.2288 -0.0094 -0.0306 0.0234  135 ASP   A CB  
2804 C  CG  A ASP   A 135 ? 0.2077 0.2490 0.2956 -0.0584 -0.0641 0.0168  135 ASP   A CG  
2805 C  CG  B ASP   A 135 ? 0.1996 0.2200 0.2595 -0.0088 -0.0328 0.0327  135 ASP   A CG  
2806 O  OD1 A ASP   A 135 ? 0.1942 0.2667 0.3040 -0.0580 -0.0626 0.0331  135 ASP   A OD1 
2807 O  OD1 B ASP   A 135 ? 0.1989 0.2186 0.2759 -0.0047 -0.0357 0.0381  135 ASP   A OD1 
2808 O  OD2 A ASP   A 135 ? 0.2322 0.2695 0.3315 -0.0639 -0.0576 0.0065  135 ASP   A OD2 
2809 O  OD2 B ASP   A 135 ? 0.2004 0.2328 0.2703 -0.0083 -0.0333 0.0431  135 ASP   A OD2 
2818 N  N   A PRO   A 136 ? 0.1482 0.1599 0.2353 -0.0122 -0.0131 0.0462  136 PRO   A N   
2819 N  N   B PRO   A 136 ? 0.1719 0.1627 0.1905 -0.0026 -0.0170 0.0011  136 PRO   A N   
2820 C  CA  A PRO   A 136 ? 0.1405 0.1534 0.2440 -0.0126 -0.0059 0.0319  136 PRO   A CA  
2821 C  CA  B PRO   A 136 ? 0.1701 0.1648 0.1867 -0.0052 -0.0077 -0.0070 136 PRO   A CA  
2822 C  C   A PRO   A 136 ? 0.1255 0.1515 0.2351 -0.0028 -0.0044 0.0224  136 PRO   A C   
2823 C  C   B PRO   A 136 ? 0.1612 0.1678 0.1749 -0.0042 -0.0033 -0.0025 136 PRO   A C   
2824 O  O   A PRO   A 136 ? 0.1238 0.1550 0.2212 -0.0042 0.0031  0.0213  136 PRO   A O   
2825 O  O   B PRO   A 136 ? 0.1590 0.1625 0.1548 0.0015  0.0079  -0.0034 136 PRO   A O   
2826 C  CB  A PRO   A 136 ? 0.1568 0.1508 0.2625 -0.0154 -0.0015 0.0287  136 PRO   A CB  
2827 C  CB  B PRO   A 136 ? 0.1779 0.1610 0.1935 -0.0057 -0.0102 -0.0134 136 PRO   A CB  
2828 C  CG  A PRO   A 136 ? 0.1690 0.1619 0.2731 -0.0117 -0.0046 0.0355  136 PRO   A CG  
2829 C  CG  B PRO   A 136 ? 0.1831 0.1583 0.2017 -0.0068 -0.0183 -0.0132 136 PRO   A CG  
2830 C  CD  A PRO   A 136 ? 0.1596 0.1624 0.2526 -0.0112 -0.0059 0.0451  136 PRO   A CD  
2831 C  CD  B PRO   A 136 ? 0.1758 0.1573 0.1961 -0.0027 -0.0166 -0.0018 136 PRO   A CD  
2846 N  N   A ILE   A 137 ? 0.1249 0.1476 0.2384 -0.0038 -0.0125 0.0290  137 ILE   A N   
2847 N  N   B ILE   A 137 ? 0.1603 0.1681 0.1832 -0.0071 -0.0041 0.0017  137 ILE   A N   
2848 C  CA  A ILE   A 137 ? 0.1332 0.1559 0.2357 -0.0119 -0.0162 0.0339  137 ILE   A CA  
2849 C  CA  B ILE   A 137 ? 0.1617 0.1720 0.1874 -0.0048 0.0007  -0.0012 137 ILE   A CA  
2850 C  C   A ILE   A 137 ? 0.1324 0.1601 0.2167 -0.0140 -0.0212 0.0305  137 ILE   A C   
2851 C  C   B ILE   A 137 ? 0.1569 0.1779 0.1807 -0.0066 0.0082  -0.0055 137 ILE   A C   
2852 O  O   A ILE   A 137 ? 0.1360 0.1521 0.2201 -0.0174 -0.0161 0.0224  137 ILE   A O   
2853 O  O   B ILE   A 137 ? 0.1546 0.1804 0.1797 -0.0049 0.0152  -0.0056 137 ILE   A O   
2854 C  CB  A ILE   A 137 ? 0.1421 0.1671 0.2578 -0.0138 -0.0302 0.0272  137 ILE   A CB  
2855 C  CB  B ILE   A 137 ? 0.1681 0.1692 0.2030 -0.0025 -0.0104 0.0028  137 ILE   A CB  
2856 C  CG1 A ILE   A 137 ? 0.1520 0.1885 0.2866 -0.0133 -0.0270 0.0336  137 ILE   A CG1 
2857 C  CG1 B ILE   A 137 ? 0.1764 0.1700 0.2195 -0.0010 -0.0259 0.0083  137 ILE   A CG1 
2858 C  CG2 A ILE   A 137 ? 0.1533 0.1702 0.2613 -0.0163 -0.0315 0.0158  137 ILE   A CG2 
2859 C  CG2 B ILE   A 137 ? 0.1705 0.1663 0.2065 -0.0001 -0.0101 0.0004  137 ILE   A CG2 
2860 C  CD1 A ILE   A 137 ? 0.1676 0.2030 0.3062 -0.0097 -0.0211 0.0386  137 ILE   A CD1 
2861 C  CD1 B ILE   A 137 ? 0.1818 0.1675 0.2351 -0.0010 -0.0344 0.0141  137 ILE   A CD1 
2884 N  N   A HIS   A 138 ? 0.1333 0.1779 0.2048 -0.0152 -0.0112 0.0236  138 HIS   A N   
2885 N  N   B HIS   A 138 ? 0.1536 0.1830 0.1806 -0.0098 0.0122  -0.0077 138 HIS   A N   
2886 C  CA  A HIS   A 138 ? 0.1393 0.1884 0.1953 -0.0171 -0.0012 0.0209  138 HIS   A CA  
2887 C  CA  B HIS   A 138 ? 0.1507 0.1821 0.1778 -0.0096 0.0143  -0.0000 138 HIS   A CA  
2888 C  C   A HIS   A 138 ? 0.1343 0.1786 0.1828 -0.0095 -0.0040 0.0238  138 HIS   A C   
2889 C  C   B HIS   A 138 ? 0.1431 0.1747 0.1775 -0.0094 0.0104  0.0155  138 HIS   A C   
2890 O  O   A HIS   A 138 ? 0.1453 0.1821 0.1827 -0.0090 0.0029  0.0236  138 HIS   A O   
2891 O  O   B HIS   A 138 ? 0.1490 0.1766 0.1806 -0.0118 0.0122  0.0189  138 HIS   A O   
2892 C  CB  A HIS   A 138 ? 0.1613 0.2147 0.1955 -0.0167 -0.0128 0.0171  138 HIS   A CB  
2893 C  CB  B HIS   A 138 ? 0.1528 0.1909 0.1778 -0.0047 0.0131  -0.0116 138 HIS   A CB  
2894 C  CG  A HIS   A 138 ? 0.1852 0.2299 0.2004 -0.0271 -0.0071 0.0101  138 HIS   A CG  
2895 C  CG  B HIS   A 138 ? 0.1586 0.1954 0.1801 -0.0065 0.0119  -0.0210 138 HIS   A CG  
2896 N  ND1 A HIS   A 138 ? 0.2005 0.2404 0.2264 -0.0280 -0.0055 0.0005  138 HIS   A ND1 
2897 N  ND1 B HIS   A 138 ? 0.1647 0.2001 0.1954 -0.0028 0.0094  -0.0264 138 HIS   A ND1 
2898 C  CD2 A HIS   A 138 ? 0.1910 0.2370 0.2003 -0.0220 -0.0009 0.0117  138 HIS   A CD2 
2899 C  CD2 B HIS   A 138 ? 0.1585 0.1952 0.1799 -0.0045 0.0151  -0.0212 138 HIS   A CD2 
2900 C  CE1 A HIS   A 138 ? 0.2080 0.2466 0.2317 -0.0145 -0.0038 0.0008  138 HIS   A CE1 
2901 C  CE1 B HIS   A 138 ? 0.1663 0.1989 0.1976 0.0028  0.0115  -0.0275 138 HIS   A CE1 
2902 N  NE2 A HIS   A 138 ? 0.2008 0.2475 0.2118 -0.0128 0.0051  0.0070  138 HIS   A NE2 
2903 N  NE2 B HIS   A 138 ? 0.1625 0.1979 0.1857 0.0013  0.0175  -0.0260 138 HIS   A NE2 
2918 N  N   . SER   A 139 ? 0.1311 0.1651 0.1811 -0.0093 0.0019  0.0247  139 SER   A N   
2919 C  CA  . SER   A 139 ? 0.1305 0.1589 0.1802 -0.0116 0.0022  0.0317  139 SER   A CA  
2920 C  C   . SER   A 139 ? 0.1267 0.1543 0.1821 -0.0059 0.0093  0.0221  139 SER   A C   
2921 O  O   . SER   A 139 ? 0.1223 0.1506 0.1969 -0.0091 0.0029  0.0257  139 SER   A O   
2922 C  CB  . SER   A 139 ? 0.1289 0.1582 0.1779 -0.0194 -0.0023 0.0359  139 SER   A CB  
2923 O  OG  . SER   A 139 ? 0.1333 0.1597 0.1906 -0.0216 -0.0123 0.0437  139 SER   A OG  
2930 N  N   . LEU   A 140 ? 0.1232 0.1590 0.1681 -0.0063 0.0047  0.0351  140 LEU   A N   
2931 C  CA  . LEU   A 140 ? 0.1203 0.1526 0.1717 -0.0068 -0.0005 0.0289  140 LEU   A CA  
2932 C  C   . LEU   A 140 ? 0.1165 0.1597 0.1837 -0.0124 0.0043  0.0305  140 LEU   A C   
2933 O  O   . LEU   A 140 ? 0.1238 0.1612 0.2104 -0.0095 -0.0007 0.0365  140 LEU   A O   
2934 C  CB  . LEU   A 140 ? 0.1246 0.1612 0.1789 -0.0130 0.0007  0.0304  140 LEU   A CB  
2935 C  CG  . LEU   A 140 ? 0.1256 0.1737 0.1903 -0.0236 0.0045  0.0427  140 LEU   A CG  
2936 C  CD1 . LEU   A 140 ? 0.1367 0.1811 0.1877 -0.0129 0.0069  0.0389  140 LEU   A CD1 
2937 C  CD2 . LEU   A 140 ? 0.1285 0.1920 0.1962 -0.0189 0.0121  0.0410  140 LEU   A CD2 
2949 N  N   . ARG   A 141 ? 0.1263 0.1569 0.1970 -0.0099 0.0012  0.0229  141 ARG   A N   
2950 C  CA  . ARG   A 141 ? 0.1394 0.1698 0.2092 -0.0194 -0.0022 0.0123  141 ARG   A CA  
2951 C  C   . ARG   A 141 ? 0.1405 0.1552 0.2022 -0.0136 -0.0026 0.0108  141 ARG   A C   
2952 O  O   . ARG   A 141 ? 0.1347 0.1548 0.2211 -0.0154 0.0004  0.0135  141 ARG   A O   
2953 C  CB  . ARG   A 141 ? 0.1530 0.1979 0.2362 -0.0272 -0.0054 -0.0087 141 ARG   A CB  
2954 C  CG  . ARG   A 141 ? 0.1908 0.2339 0.2671 -0.0331 0.0103  -0.0158 141 ARG   A CG  
2955 C  CD  . ARG   A 141 ? 0.2219 0.2596 0.3004 -0.0409 0.0095  -0.0225 141 ARG   A CD  
2956 N  NE  . ARG   A 141 ? 0.2149 0.2787 0.3184 -0.0413 -0.0005 -0.0202 141 ARG   A NE  
2957 C  CZ  . ARG   A 141 ? 0.2172 0.3003 0.3228 -0.0568 0.0100  -0.0096 141 ARG   A CZ  
2958 N  NH1 . ARG   A 141 ? 0.2031 0.3040 0.3126 -0.0733 0.0368  -0.0216 141 ARG   A NH1 
2959 N  NH2 . ARG   A 141 ? 0.2241 0.3079 0.3406 -0.0526 -0.0065 0.0025  141 ARG   A NH2 
2973 N  N   . VAL   A 142 ? 0.1351 0.1512 0.1923 -0.0112 -0.0013 0.0081  142 VAL   A N   
2974 C  CA  . VAL   A 142 ? 0.1367 0.1515 0.1922 -0.0089 0.0123  0.0068  142 VAL   A CA  
2975 C  C   . VAL   A 142 ? 0.1212 0.1440 0.1893 -0.0126 0.0088  0.0110  142 VAL   A C   
2976 O  O   . VAL   A 142 ? 0.1255 0.1428 0.2027 -0.0012 0.0098  0.0118  142 VAL   A O   
2977 C  CB  . VAL   A 142 ? 0.1437 0.1566 0.1802 -0.0117 0.0149  0.0116  142 VAL   A CB  
2978 C  CG1 . VAL   A 142 ? 0.1438 0.1543 0.1858 -0.0175 0.0180  0.0057  142 VAL   A CG1 
2979 C  CG2 . VAL   A 142 ? 0.1585 0.1719 0.1970 -0.0048 0.0214  0.0125  142 VAL   A CG2 
2989 N  N   . CYS   A 143 ? 0.1236 0.1431 0.1796 -0.0127 0.0067  0.0125  143 CYS   A N   
2990 C  CA  . CYS   A 143 ? 0.1245 0.1436 0.1862 -0.0140 0.0099  0.0227  143 CYS   A CA  
2991 C  C   . CYS   A 143 ? 0.1228 0.1417 0.1963 -0.0100 0.0058  0.0288  143 CYS   A C   
2992 O  O   . CYS   A 143 ? 0.1200 0.1408 0.1985 -0.0094 0.0041  0.0307  143 CYS   A O   
2993 C  CB  . CYS   A 143 ? 0.1342 0.1498 0.1851 -0.0098 0.0191  0.0308  143 CYS   A CB  
2994 S  SG  . CYS   A 143 ? 0.1509 0.1538 0.1784 0.0035  0.0104  0.0208  143 CYS   A SG  
3000 N  N   . VAL   A 144 ? 0.1214 0.1491 0.2201 -0.0133 0.0097  0.0331  144 VAL   A N   
3001 C  CA  . VAL   A 144 ? 0.1306 0.1589 0.2361 -0.0161 0.0150  0.0375  144 VAL   A CA  
3002 C  C   . VAL   A 144 ? 0.1339 0.1500 0.2405 -0.0193 -0.0008 0.0286  144 VAL   A C   
3003 O  O   . VAL   A 144 ? 0.1537 0.1493 0.2422 -0.0048 -0.0071 0.0327  144 VAL   A O   
3004 C  CB  . VAL   A 144 ? 0.1539 0.1820 0.3021 -0.0048 0.0308  0.0475  144 VAL   A CB  
3005 C  CG1 . VAL   A 144 ? 0.1708 0.2021 0.3405 -0.0142 0.0175  0.0486  144 VAL   A CG1 
3006 C  CG2 . VAL   A 144 ? 0.1337 0.1868 0.3084 -0.0050 0.0393  0.0600  144 VAL   A CG2 
3016 N  N   . ASP   A 145 ? 0.1379 0.1414 0.2481 -0.0190 -0.0006 0.0202  145 ASP   A N   
3017 C  CA  . ASP   A 145 ? 0.1503 0.1448 0.2533 -0.0215 -0.0054 0.0105  145 ASP   A CA  
3018 C  C   . ASP   A 145 ? 0.1510 0.1378 0.2536 -0.0142 0.0001  0.0053  145 ASP   A C   
3019 O  O   . ASP   A 145 ? 0.1664 0.1488 0.3039 -0.0132 -0.0028 -0.0228 145 ASP   A O   
3020 C  CB  . ASP   A 145 ? 0.1613 0.1754 0.2717 -0.0270 -0.0223 0.0087  145 ASP   A CB  
3021 C  CG  . ASP   A 145 ? 0.1781 0.2171 0.2984 -0.0447 -0.0338 0.0142  145 ASP   A CG  
3022 O  OD1 . ASP   A 145 ? 0.1735 0.2351 0.3086 -0.0571 -0.0252 0.0142  145 ASP   A OD1 
3023 O  OD2 . ASP   A 145 ? 0.2014 0.2391 0.3046 -0.0514 -0.0509 0.0142  145 ASP   A OD2 
3028 N  N   . THR   A 146 ? 0.1326 0.1341 0.2203 -0.0185 0.0075  0.0125  146 THR   A N   
3029 C  CA  . THR   A 146 ? 0.1318 0.1315 0.2031 -0.0091 0.0039  0.0042  146 THR   A CA  
3030 C  C   . THR   A 146 ? 0.1268 0.1263 0.2085 0.0011  0.0087  0.0186  146 THR   A C   
3031 O  O   . THR   A 146 ? 0.1400 0.1426 0.2280 0.0085  -0.0038 0.0153  146 THR   A O   
3032 C  CB  . THR   A 146 ? 0.1281 0.1309 0.2067 -0.0042 0.0002  0.0114  146 THR   A CB  
3033 O  OG1 . THR   A 146 ? 0.1283 0.1506 0.2150 -0.0003 -0.0022 0.0110  146 THR   A OG1 
3034 C  CG2 . THR   A 146 ? 0.1296 0.1367 0.2238 -0.0067 0.0012  0.0117  146 THR   A CG2 
3042 N  N   . VAL   A 147 ? 0.1238 0.1341 0.1981 0.0022  0.0039  0.0180  147 VAL   A N   
3043 C  CA  . VAL   A 147 ? 0.1286 0.1402 0.2017 -0.0055 0.0219  0.0253  147 VAL   A CA  
3044 C  C   . VAL   A 147 ? 0.1278 0.1352 0.2199 -0.0093 0.0201  0.0333  147 VAL   A C   
3045 O  O   . VAL   A 147 ? 0.1303 0.1428 0.2390 -0.0178 0.0133  0.0358  147 VAL   A O   
3046 C  CB  . VAL   A 147 ? 0.1362 0.1420 0.1892 -0.0125 0.0211  0.0314  147 VAL   A CB  
3047 C  CG1 . VAL   A 147 ? 0.1665 0.1516 0.1972 -0.0055 0.0221  0.0347  147 VAL   A CG1 
3048 C  CG2 . VAL   A 147 ? 0.1421 0.1411 0.1924 -0.0134 0.0132  0.0189  147 VAL   A CG2 
3058 N  N   . ARG   A 148 ? 0.1281 0.1377 0.2283 -0.0125 0.0169  0.0460  148 ARG   A N   
3059 C  CA  . ARG   A 148 ? 0.1356 0.1431 0.2236 -0.0171 0.0059  0.0498  148 ARG   A CA  
3060 C  C   . ARG   A 148 ? 0.1433 0.1438 0.2213 -0.0130 0.0106  0.0637  148 ARG   A C   
3061 O  O   . ARG   A 148 ? 0.1716 0.1548 0.2410 -0.0213 0.0154  0.0526  148 ARG   A O   
3062 C  CB  . ARG   A 148 ? 0.1434 0.1421 0.2336 -0.0111 0.0189  0.0431  148 ARG   A CB  
3063 C  CG  . ARG   A 148 ? 0.1581 0.1416 0.2695 -0.0095 0.0285  0.0386  148 ARG   A CG  
3064 C  CD  . ARG   A 148 ? 0.1707 0.1420 0.2930 -0.0078 0.0437  0.0515  148 ARG   A CD  
3065 N  NE  . ARG   A 148 ? 0.1675 0.1482 0.2906 0.0101  0.0479  0.0543  148 ARG   A NE  
3066 C  CZ  . ARG   A 148 ? 0.1669 0.1310 0.2806 0.0007  0.0462  0.0426  148 ARG   A CZ  
3067 N  NH1 . ARG   A 148 ? 0.1711 0.1368 0.2860 -0.0084 0.0492  0.0209  148 ARG   A NH1 
3068 N  NH2 . ARG   A 148 ? 0.1606 0.1494 0.2813 0.0112  0.0478  0.0480  148 ARG   A NH2 
3082 N  N   . THR   A 149 ? 0.1455 0.1543 0.2173 -0.0189 -0.0034 0.0605  149 THR   A N   
3083 C  CA  . THR   A 149 ? 0.1465 0.1589 0.2154 -0.0187 -0.0031 0.0548  149 THR   A CA  
3084 C  C   . THR   A 149 ? 0.1401 0.1591 0.2050 -0.0223 0.0002  0.0532  149 THR   A C   
3085 O  O   . THR   A 149 ? 0.1415 0.1670 0.2128 -0.0262 0.0078  0.0542  149 THR   A O   
3086 C  CB  . THR   A 149 ? 0.1472 0.1704 0.2183 -0.0164 -0.0014 0.0510  149 THR   A CB  
3087 O  OG1 . THR   A 149 ? 0.1450 0.1602 0.2313 -0.0245 0.0049  0.0467  149 THR   A OG1 
3088 C  CG2 . THR   A 149 ? 0.1451 0.1796 0.2349 -0.0144 -0.0073 0.0398  149 THR   A CG2 
3096 N  N   . ASN   A 150 ? 0.1438 0.1628 0.1989 -0.0113 -0.0056 0.0634  150 ASN   A N   
3097 C  CA  . ASN   A 150 ? 0.1588 0.1742 0.1916 -0.0169 -0.0025 0.0579  150 ASN   A CA  
3098 C  C   . ASN   A 150 ? 0.1387 0.1584 0.1871 -0.0209 -0.0054 0.0561  150 ASN   A C   
3099 O  O   . ASN   A 150 ? 0.1483 0.1726 0.2173 -0.0202 -0.0180 0.0452  150 ASN   A O   
3100 C  CB  . ASN   A 150 ? 0.2039 0.1977 0.2246 -0.0240 0.0117  0.0793  150 ASN   A CB  
3101 C  CG  . ASN   A 150 ? 0.2524 0.2287 0.2927 -0.0250 -0.0009 0.0804  150 ASN   A CG  
3102 O  OD1 . ASN   A 150 ? 0.2715 0.2353 0.3174 -0.0326 0.0060  0.0901  150 ASN   A OD1 
3103 N  ND2 . ASN   A 150 ? 0.2809 0.2520 0.3299 -0.0188 -0.0135 0.0764  150 ASN   A ND2 
3110 N  N   . VAL   A 151 ? 0.1387 0.1475 0.1866 -0.0229 -0.0013 0.0508  151 VAL   A N   
3111 C  CA  . VAL   A 151 ? 0.1479 0.1528 0.1811 -0.0215 0.0039  0.0451  151 VAL   A CA  
3112 C  C   . VAL   A 151 ? 0.1349 0.1462 0.1940 -0.0308 0.0046  0.0460  151 VAL   A C   
3113 O  O   . VAL   A 151 ? 0.1466 0.1512 0.2243 -0.0212 0.0081  0.0386  151 VAL   A O   
3114 C  CB  . VAL   A 151 ? 0.1751 0.1715 0.1862 -0.0096 0.0062  0.0419  151 VAL   A CB  
3115 C  CG1 . VAL   A 151 ? 0.1757 0.1924 0.2128 -0.0132 0.0009  0.0458  151 VAL   A CG1 
3116 C  CG2 . VAL   A 151 ? 0.1863 0.1659 0.1864 -0.0011 0.0207  0.0395  151 VAL   A CG2 
3126 N  N   . TYR   A 152 ? 0.1330 0.1509 0.1857 -0.0267 0.0010  0.0427  152 TYR   A N   
3127 C  CA  . TYR   A 152 ? 0.1385 0.1586 0.1686 -0.0247 0.0040  0.0457  152 TYR   A CA  
3128 C  C   . TYR   A 152 ? 0.1313 0.1482 0.1591 -0.0213 0.0113  0.0402  152 TYR   A C   
3129 O  O   . TYR   A 152 ? 0.1419 0.1443 0.1713 -0.0244 0.0115  0.0327  152 TYR   A O   
3130 C  CB  . TYR   A 152 ? 0.1531 0.1732 0.1754 -0.0240 0.0127  0.0495  152 TYR   A CB  
3131 C  CG  . TYR   A 152 ? 0.1583 0.1928 0.1688 -0.0263 0.0189  0.0586  152 TYR   A CG  
3132 C  CD1 . TYR   A 152 ? 0.1753 0.2139 0.1941 -0.0135 0.0203  0.0615  152 TYR   A CD1 
3133 C  CD2 . TYR   A 152 ? 0.1665 0.2018 0.1707 -0.0352 0.0099  0.0540  152 TYR   A CD2 
3134 C  CE1 . TYR   A 152 ? 0.2106 0.2250 0.2035 -0.0056 0.0097  0.0713  152 TYR   A CE1 
3135 C  CE2 . TYR   A 152 ? 0.2008 0.2162 0.1886 -0.0360 0.0141  0.0642  152 TYR   A CE2 
3136 C  CZ  . TYR   A 152 ? 0.2248 0.2199 0.1994 -0.0218 0.0075  0.0838  152 TYR   A CZ  
3137 O  OH  . TYR   A 152 ? 0.2550 0.2381 0.2337 -0.0182 0.0105  0.0958  152 TYR   A OH  
3147 N  N   A LEU   A 153 ? 0.1301 0.1420 0.1695 -0.0228 0.0161  0.0414  153 LEU   A N   
3148 N  N   B LEU   A 153 ? 0.1338 0.1479 0.1441 -0.0170 0.0027  0.0355  153 LEU   A N   
3149 C  CA  A LEU   A 153 ? 0.1269 0.1360 0.1771 -0.0125 0.0221  0.0375  153 LEU   A CA  
3150 C  CA  B LEU   A 153 ? 0.1323 0.1453 0.1303 -0.0056 0.0035  0.0267  153 LEU   A CA  
3151 C  C   A LEU   A 153 ? 0.1302 0.1363 0.1708 -0.0150 0.0258  0.0251  153 LEU   A C   
3152 C  C   B LEU   A 153 ? 0.1348 0.1531 0.1232 0.0011  0.0075  0.0193  153 LEU   A C   
3153 O  O   A LEU   A 153 ? 0.1397 0.1408 0.1886 -0.0214 0.0331  0.0211  153 LEU   A O   
3154 O  O   B LEU   A 153 ? 0.1366 0.1602 0.1210 0.0002  0.0095  0.0170  153 LEU   A O   
3155 C  CB  A LEU   A 153 ? 0.1228 0.1274 0.1864 -0.0110 0.0167  0.0327  153 LEU   A CB  
3156 C  CB  B LEU   A 153 ? 0.1270 0.1360 0.1337 0.0007  0.0013  0.0306  153 LEU   A CB  
3157 C  CG  A LEU   A 153 ? 0.1255 0.1294 0.1930 -0.0096 0.0219  0.0214  153 LEU   A CG  
3158 C  CG  B LEU   A 153 ? 0.1301 0.1336 0.1393 0.0024  -0.0001 0.0265  153 LEU   A CG  
3159 C  CD1 A LEU   A 153 ? 0.1353 0.1203 0.2015 -0.0014 0.0112  0.0214  153 LEU   A CD1 
3160 C  CD1 B LEU   A 153 ? 0.1353 0.1335 0.1476 0.0045  0.0004  0.0296  153 LEU   A CD1 
3161 C  CD2 A LEU   A 153 ? 0.1355 0.1413 0.1919 -0.0124 0.0309  0.0004  153 LEU   A CD2 
3162 C  CD2 B LEU   A 153 ? 0.1345 0.1372 0.1465 0.0043  0.0011  0.0147  153 LEU   A CD2 
3185 N  N   A ALA   A 154 ? 0.1289 0.1297 0.1746 -0.0186 0.0228  0.0301  154 ALA   A N   
3186 N  N   B ALA   A 154 ? 0.1351 0.1523 0.1217 0.0046  0.0088  0.0126  154 ALA   A N   
3187 C  CA  A ALA   A 154 ? 0.1395 0.1320 0.1618 -0.0147 0.0274  0.0210  154 ALA   A CA  
3188 C  CA  B ALA   A 154 ? 0.1409 0.1528 0.1331 0.0064  0.0022  0.0088  154 ALA   A CA  
3189 C  C   A ALA   A 154 ? 0.1290 0.1242 0.1506 -0.0102 0.0239  0.0191  154 ALA   A C   
3190 C  C   B ALA   A 154 ? 0.1401 0.1533 0.1309 0.0042  -0.0061 0.0124  154 ALA   A C   
3191 O  O   A ALA   A 154 ? 0.1434 0.1391 0.1547 -0.0132 0.0253  0.0166  154 ALA   A O   
3192 O  O   B ALA   A 154 ? 0.1459 0.1535 0.1201 0.0028  -0.0036 0.0136  154 ALA   A O   
3193 C  CB  A ALA   A 154 ? 0.1562 0.1433 0.1721 -0.0032 0.0249  0.0166  154 ALA   A CB  
3194 C  CB  B ALA   A 154 ? 0.1443 0.1545 0.1367 0.0053  -0.0041 0.0060  154 ALA   A CB  
3205 N  N   A VAL   A 155 ? 0.1062 0.0936 0.1132 -0.0021 0.0364  0.0349  155 VAL   A N   
3206 N  N   B VAL   A 155 ? 0.1344 0.1464 0.1281 0.0090  -0.0047 0.0216  155 VAL   A N   
3207 C  CA  A VAL   A 155 ? 0.1312 0.1188 0.1610 0.0062  0.0217  0.0408  155 VAL   A CA  
3208 C  CA  B VAL   A 155 ? 0.1520 0.1612 0.1397 0.0082  -0.0088 0.0209  155 VAL   A CA  
3209 C  CA  T VAL   A 155 ? 0.1768 0.1615 0.1942 -0.0066 0.0481  0.0458  155 VAL   A CA  
3210 C  C   A VAL   A 155 ? 0.1452 0.1343 0.1914 0.0195  0.0204  0.0481  155 VAL   A C   
3211 C  C   B VAL   A 155 ? 0.1632 0.1701 0.1619 0.0169  -0.0177 0.0200  155 VAL   A C   
3212 C  C   T VAL   A 155 ? 0.1800 0.1626 0.1884 0.0056  0.0555  0.0524  155 VAL   A C   
3213 O  O   A VAL   A 155 ? 0.1440 0.1383 0.2009 0.0236  0.0250  0.0404  155 VAL   A O   
3214 O  O   B VAL   A 155 ? 0.1614 0.1734 0.1497 0.0151  -0.0242 0.0067  155 VAL   A O   
3215 O  O   T VAL   A 155 ? 0.1770 0.1695 0.1900 0.0090  0.0639  0.0497  155 VAL   A O   
3216 C  CB  A VAL   A 155 ? 0.1439 0.1258 0.1680 0.0117  0.0074  0.0368  155 VAL   A CB  
3217 C  CB  B VAL   A 155 ? 0.1582 0.1649 0.1361 0.0090  -0.0115 0.0172  155 VAL   A CB  
3218 C  CB  T VAL   A 155 ? 0.1783 0.1628 0.1903 -0.0058 0.0309  0.0421  155 VAL   A CB  
3219 C  CG1 A VAL   A 155 ? 0.1527 0.1296 0.1747 0.0169  0.0049  0.0353  155 VAL   A CG1 
3220 C  CG1 B VAL   A 155 ? 0.1603 0.1659 0.1293 0.0090  -0.0076 0.0141  155 VAL   A CG1 
3221 C  CG1 T VAL   A 155 ? 0.1829 0.1661 0.1907 -0.0011 0.0280  0.0429  155 VAL   A CG1 
3222 C  CG2 A VAL   A 155 ? 0.1520 0.1310 0.1824 0.0159  -0.0089 0.0340  155 VAL   A CG2 
3223 C  CG2 B VAL   A 155 ? 0.1663 0.1678 0.1529 0.0112  -0.0165 0.0148  155 VAL   A CG2 
3224 C  CG2 T VAL   A 155 ? 0.1818 0.1647 0.2011 -0.0037 0.0145  0.0380  155 VAL   A CG2 
3250 N  N   A PHE   A 156 ? 0.1599 0.1481 0.2233 0.0249  0.0272  0.0590  156 PHE   A N   
3251 N  N   B PHE   A 156 ? 0.1779 0.1766 0.1968 0.0240  -0.0127 0.0310  156 PHE   A N   
3252 N  N   T PHE   A 156 ? 0.1887 0.1583 0.2011 0.0119  0.0616  0.0595  156 PHE   A N   
3253 C  CA  A PHE   A 156 ? 0.1743 0.1636 0.2496 0.0309  0.0297  0.0656  156 PHE   A CA  
3254 C  CA  B PHE   A 156 ? 0.1950 0.1854 0.2332 0.0281  -0.0062 0.0374  156 PHE   A CA  
3255 C  CA  T PHE   A 156 ? 0.2014 0.1559 0.2031 0.0183  0.0601  0.0633  156 PHE   A CA  
3256 C  C   A PHE   A 156 ? 0.1786 0.1731 0.2582 0.0374  0.0436  0.0709  156 PHE   A C   
3257 C  C   B PHE   A 156 ? 0.1975 0.1901 0.2421 0.0366  0.0155  0.0458  156 PHE   A C   
3258 C  C   T PHE   A 156 ? 0.1962 0.1696 0.2163 0.0232  0.0671  0.0706  156 PHE   A C   
3259 O  O   A PHE   A 156 ? 0.1816 0.1782 0.2683 0.0285  0.0545  0.0634  156 PHE   A O   
3260 O  O   B PHE   A 156 ? 0.2011 0.1904 0.2507 0.0339  0.0244  0.0421  156 PHE   A O   
3261 O  O   T PHE   A 156 ? 0.2059 0.1763 0.2264 0.0216  0.0748  0.0576  156 PHE   A O   
3262 C  CB  A PHE   A 156 ? 0.1839 0.1742 0.2642 0.0239  0.0212  0.0636  156 PHE   A CB  
3263 C  CB  B PHE   A 156 ? 0.2083 0.1963 0.2570 0.0193  -0.0176 0.0313  156 PHE   A CB  
3264 C  CB  T PHE   A 156 ? 0.2125 0.1446 0.1830 0.0188  0.0558  0.0582  156 PHE   A CB  
3265 C  CG  A PHE   A 156 ? 0.1935 0.1812 0.2729 0.0273  0.0147  0.0533  156 PHE   A CG  
3266 C  CG  B PHE   A 156 ? 0.2204 0.2051 0.2748 0.0139  -0.0276 0.0186  156 PHE   A CG  
3267 C  CG  T PHE   A 156 ? 0.2239 0.1453 0.1677 0.0221  0.0487  0.0665  156 PHE   A CG  
3268 C  CD1 A PHE   A 156 ? 0.1958 0.1830 0.2732 0.0328  0.0201  0.0453  156 PHE   A CD1 
3269 C  CD1 B PHE   A 156 ? 0.2249 0.2124 0.2828 0.0119  -0.0291 0.0120  156 PHE   A CD1 
3270 C  CD1 T PHE   A 156 ? 0.2332 0.1541 0.1990 0.0190  0.0303  0.0569  156 PHE   A CD1 
3271 C  CD2 A PHE   A 156 ? 0.1998 0.1901 0.2734 0.0348  0.0093  0.0491  156 PHE   A CD2 
3272 C  CD2 B PHE   A 156 ? 0.2230 0.2089 0.2829 0.0098  -0.0329 0.0118  156 PHE   A CD2 
3273 C  CD2 T PHE   A 156 ? 0.2245 0.1434 0.1684 0.0302  0.0487  0.0754  156 PHE   A CD2 
3274 C  CE1 A PHE   A 156 ? 0.2034 0.1868 0.2752 0.0350  0.0213  0.0407  156 PHE   A CE1 
3275 C  CE1 B PHE   A 156 ? 0.2259 0.2138 0.2828 0.0091  -0.0319 0.0064  156 PHE   A CE1 
3276 C  CE1 T PHE   A 156 ? 0.2378 0.1564 0.2140 0.0195  0.0291  0.0493  156 PHE   A CE1 
3277 C  CE2 A PHE   A 156 ? 0.2094 0.1957 0.2762 0.0361  0.0100  0.0391  156 PHE   A CE2 
3278 C  CE2 B PHE   A 156 ? 0.2255 0.2124 0.2856 0.0072  -0.0354 0.0043  156 PHE   A CE2 
3279 C  CE2 T PHE   A 156 ? 0.2298 0.1471 0.1826 0.0267  0.0453  0.0700  156 PHE   A CE2 
3280 C  CZ  A PHE   A 156 ? 0.2107 0.1957 0.2776 0.0356  0.0183  0.0365  156 PHE   A CZ  
3281 C  CZ  B PHE   A 156 ? 0.2247 0.2128 0.2815 0.0069  -0.0336 0.0051  156 PHE   A CZ  
3282 C  CZ  T PHE   A 156 ? 0.2329 0.1456 0.2076 0.0188  0.0374  0.0581  156 PHE   A CZ  
3310 N  N   A ASP   A 157 ? 0.1832 0.1840 0.2599 0.0463  0.0337  0.0793  157 ASP   A N   
3311 N  N   B ASP   A 157 ? 0.1966 0.1971 0.2423 0.0430  0.0168  0.0534  157 ASP   A N   
3312 N  N   T ASP   A 157 ? 0.1750 0.1818 0.2312 0.0240  0.0501  0.0879  157 ASP   A N   
3313 C  CA  A ASP   A 157 ? 0.1991 0.2056 0.2619 0.0506  0.0306  0.0790  157 ASP   A CA  
3314 C  CA  B ASP   A 157 ? 0.2055 0.2129 0.2439 0.0472  0.0226  0.0558  157 ASP   A CA  
3315 C  CA  T ASP   A 157 ? 0.1682 0.1994 0.2324 0.0272  0.0409  0.0918  157 ASP   A CA  
3316 C  C   A ASP   A 157 ? 0.1927 0.2186 0.2603 0.0560  0.0276  0.0805  157 ASP   A C   
3317 C  C   B ASP   A 157 ? 0.1958 0.2256 0.2396 0.0533  0.0246  0.0565  157 ASP   A C   
3318 C  C   T ASP   A 157 ? 0.1633 0.2182 0.2280 0.0325  0.0438  0.0977  157 ASP   A C   
3319 O  O   A ASP   A 157 ? 0.1866 0.2124 0.2468 0.0635  0.0117  0.0992  157 ASP   A O   
3320 O  O   B ASP   A 157 ? 0.1920 0.2243 0.2370 0.0587  0.0162  0.0599  157 ASP   A O   
3321 O  O   T ASP   A 157 ? 0.1547 0.2182 0.2215 0.0337  0.0432  0.1105  157 ASP   A O   
3322 C  CB  A ASP   A 157 ? 0.2151 0.2137 0.2730 0.0554  0.0313  0.0705  157 ASP   A CB  
3323 C  CB  B ASP   A 157 ? 0.2201 0.2162 0.2550 0.0500  0.0261  0.0528  157 ASP   A CB  
3324 C  CB  T ASP   A 157 ? 0.1670 0.1976 0.2455 0.0283  0.0260  0.0841  157 ASP   A CB  
3325 C  CG  A ASP   A 157 ? 0.2266 0.2192 0.2850 0.0607  0.0323  0.0668  157 ASP   A CG  
3326 C  CG  B ASP   A 157 ? 0.2315 0.2187 0.2676 0.0525  0.0301  0.0534  157 ASP   A CG  
3327 C  CG  T ASP   A 157 ? 0.1574 0.1920 0.2551 0.0260  0.0121  0.0786  157 ASP   A CG  
3328 O  OD1 A ASP   A 157 ? 0.2349 0.2247 0.2877 0.0588  0.0325  0.0650  157 ASP   A OD1 
3329 O  OD1 B ASP   A 157 ? 0.2385 0.2206 0.2727 0.0513  0.0382  0.0530  157 ASP   A OD1 
3330 O  OD1 T ASP   A 157 ? 0.1494 0.1840 0.2729 0.0207  0.0118  0.0580  157 ASP   A OD1 
3331 O  OD2 A ASP   A 157 ? 0.2240 0.2131 0.2927 0.0654  0.0358  0.0714  157 ASP   A OD2 
3332 O  OD2 B ASP   A 157 ? 0.2309 0.2144 0.2734 0.0524  0.0280  0.0610  157 ASP   A OD2 
3333 O  OD2 T ASP   A 157 ? 0.1543 0.1922 0.2446 0.0347  0.0061  0.0901  157 ASP   A OD2 
3346 N  N   A LYS   A 158 ? 0.2007 0.2375 0.2692 0.0502  0.0372  0.0667  158 LYS   A N   
3347 N  N   B LYS   A 158 ? 0.1946 0.2395 0.2321 0.0536  0.0308  0.0568  158 LYS   A N   
3348 N  N   T LYS   A 158 ? 0.1792 0.2376 0.2407 0.0277  0.0470  0.0744  158 LYS   A N   
3349 C  CA  A LYS   A 158 ? 0.2034 0.2543 0.2835 0.0483  0.0450  0.0536  158 LYS   A CA  
3350 C  CA  B LYS   A 158 ? 0.1962 0.2546 0.2306 0.0528  0.0342  0.0522  158 LYS   A CA  
3351 C  CA  T LYS   A 158 ? 0.1884 0.2550 0.2636 0.0298  0.0484  0.0519  158 LYS   A CA  
3352 C  C   A LYS   A 158 ? 0.1903 0.2542 0.2644 0.0530  0.0374  0.0511  158 LYS   A C   
3353 C  C   B LYS   A 158 ? 0.1853 0.2577 0.2104 0.0609  0.0223  0.0591  158 LYS   A C   
3354 C  C   T LYS   A 158 ? 0.1767 0.2453 0.2468 0.0317  0.0362  0.0365  158 LYS   A C   
3355 O  O   A LYS   A 158 ? 0.1870 0.2590 0.2625 0.0522  0.0453  0.0460  158 LYS   A O   
3356 O  O   B LYS   A 158 ? 0.1787 0.2612 0.1930 0.0558  0.0264  0.0603  158 LYS   A O   
3357 O  O   T LYS   A 158 ? 0.1705 0.2425 0.2440 0.0313  0.0444  0.0245  158 LYS   A O   
3358 C  CB  A LYS   A 158 ? 0.2190 0.2641 0.3120 0.0424  0.0609  0.0505  158 LYS   A CB  
3359 C  CB  B LYS   A 158 ? 0.2088 0.2674 0.2580 0.0433  0.0414  0.0428  158 LYS   A CB  
3360 C  CB  T LYS   A 158 ? 0.2110 0.2770 0.3099 0.0281  0.0638  0.0433  158 LYS   A CB  
3361 C  CG  A LYS   A 158 ? 0.2342 0.2711 0.3375 0.0414  0.0679  0.0533  158 LYS   A CG  
3362 C  CG  B LYS   A 158 ? 0.2215 0.2782 0.2875 0.0376  0.0412  0.0407  158 LYS   A CG  
3363 C  CG  T LYS   A 158 ? 0.2304 0.2935 0.3506 0.0300  0.0727  0.0427  158 LYS   A CG  
3364 C  CD  A LYS   A 158 ? 0.2453 0.2761 0.3595 0.0402  0.0787  0.0605  158 LYS   A CD  
3365 C  CD  B LYS   A 158 ? 0.2327 0.2862 0.3162 0.0319  0.0407  0.0407  158 LYS   A CD  
3366 C  CD  T LYS   A 158 ? 0.2488 0.3075 0.3928 0.0347  0.0758  0.0430  158 LYS   A CD  
3367 C  CE  A LYS   A 158 ? 0.2520 0.2774 0.3705 0.0382  0.0864  0.0724  158 LYS   A CE  
3368 C  CE  B LYS   A 158 ? 0.2378 0.2908 0.3371 0.0301  0.0403  0.0431  158 LYS   A CE  
3369 C  CE  T LYS   A 158 ? 0.2627 0.3165 0.4213 0.0362  0.0758  0.0465  158 LYS   A CE  
3370 N  NZ  A LYS   A 158 ? 0.2547 0.2780 0.3783 0.0369  0.0913  0.0789  158 LYS   A NZ  
3371 N  NZ  B LYS   A 158 ? 0.2385 0.2935 0.3503 0.0282  0.0387  0.0456  158 LYS   A NZ  
3372 N  NZ  T LYS   A 158 ? 0.2705 0.3217 0.4368 0.0378  0.0767  0.0479  158 LYS   A NZ  
3412 N  N   A ASN   A 159 ? 0.1820 0.2456 0.2567 0.0524  0.0235  0.0502  159 ASN   A N   
3413 N  N   B ASN   A 159 ? 0.1844 0.2592 0.2181 0.0665  0.0130  0.0592  159 ASN   A N   
3414 N  N   T ASN   A 159 ? 0.1775 0.2404 0.2507 0.0284  0.0205  0.0304  159 ASN   A N   
3415 C  CA  A ASN   A 159 ? 0.1758 0.2386 0.2496 0.0442  0.0118  0.0530  159 ASN   A CA  
3416 C  CA  B ASN   A 159 ? 0.1878 0.2612 0.2322 0.0626  0.0131  0.0530  159 ASN   A CA  
3417 C  CA  T ASN   A 159 ? 0.1851 0.2404 0.2584 0.0222  0.0080  0.0354  159 ASN   A CA  
3418 C  C   A ASN   A 159 ? 0.1586 0.2284 0.2304 0.0371  0.0144  0.0442  159 ASN   A C   
3419 C  C   B ASN   A 159 ? 0.1727 0.2551 0.2135 0.0578  0.0092  0.0522  159 ASN   A C   
3420 C  C   T ASN   A 159 ? 0.1855 0.2382 0.2562 0.0130  0.0175  0.0255  159 ASN   A C   
3421 O  O   A ASN   A 159 ? 0.1449 0.2211 0.2237 0.0389  0.0089  0.0297  159 ASN   A O   
3422 O  O   B ASN   A 159 ? 0.1647 0.2620 0.2109 0.0661  0.0013  0.0475  159 ASN   A O   
3423 O  O   T ASN   A 159 ? 0.1783 0.2287 0.2532 0.0072  0.0167  0.0038  159 ASN   A O   
3424 C  CB  A ASN   A 159 ? 0.1848 0.2444 0.2705 0.0421  0.0051  0.0625  159 ASN   A CB  
3425 C  CB  B ASN   A 159 ? 0.2048 0.2696 0.2720 0.0581  0.0193  0.0463  159 ASN   A CB  
3426 C  CB  T ASN   A 159 ? 0.1937 0.2466 0.2797 0.0260  -0.0041 0.0524  159 ASN   A CB  
3427 C  CG  A ASN   A 159 ? 0.1940 0.2543 0.2974 0.0382  0.0017  0.0650  159 ASN   A CG  
3428 C  CG  B ASN   A 159 ? 0.2190 0.2809 0.3120 0.0448  0.0286  0.0349  159 ASN   A CG  
3429 C  CG  T ASN   A 159 ? 0.2016 0.2566 0.3069 0.0282  -0.0104 0.0633  159 ASN   A CG  
3430 O  OD1 A ASN   A 159 ? 0.2021 0.2633 0.3135 0.0346  0.0082  0.0681  159 ASN   A OD1 
3431 O  OD1 B ASN   A 159 ? 0.2239 0.2884 0.3330 0.0398  0.0281  0.0330  159 ASN   A OD1 
3432 O  OD1 T ASN   A 159 ? 0.2074 0.2674 0.3254 0.0274  -0.0014 0.0661  159 ASN   A OD1 
3433 N  ND2 A ASN   A 159 ? 0.1961 0.2570 0.3098 0.0409  -0.0033 0.0615  159 ASN   A ND2 
3434 N  ND2 B ASN   A 159 ? 0.2259 0.2852 0.3270 0.0381  0.0371  0.0273  159 ASN   A ND2 
3435 N  ND2 T ASN   A 159 ? 0.2039 0.2597 0.3169 0.0334  -0.0189 0.0648  159 ASN   A ND2 
3454 N  N   A LEU   A 160 ? 0.1503 0.2217 0.2178 0.0338  0.0139  0.0556  160 LEU   A N   
3455 N  N   B LEU   A 160 ? 0.1621 0.2386 0.1946 0.0449  0.0077  0.0672  160 LEU   A N   
3456 N  N   T LEU   A 160 ? 0.1886 0.2424 0.2557 0.0127  0.0204  0.0414  160 LEU   A N   
3457 C  CA  A LEU   A 160 ? 0.1443 0.2164 0.2097 0.0256  0.0209  0.0670  160 LEU   A CA  
3458 C  CA  B LEU   A 160 ? 0.1537 0.2254 0.1889 0.0328  0.0169  0.0753  160 LEU   A CA  
3459 C  CA  T LEU   A 160 ? 0.1923 0.2452 0.2520 0.0078  0.0263  0.0580  160 LEU   A CA  
3460 C  C   A LEU   A 160 ? 0.1269 0.2075 0.1955 0.0122  0.0254  0.0684  160 LEU   A C   
3461 C  C   B LEU   A 160 ? 0.1291 0.2199 0.1721 0.0243  0.0193  0.0768  160 LEU   A C   
3462 O  O   A LEU   A 160 ? 0.1101 0.2015 0.1875 -0.0010 0.0201  0.0717  160 LEU   A O   
3463 O  O   B LEU   A 160 ? 0.1244 0.2204 0.1776 0.0180  0.0100  0.0761  160 LEU   A O   
3464 C  CB  A LEU   A 160 ? 0.1479 0.2197 0.2164 0.0303  0.0127  0.0727  160 LEU   A CB  
3465 C  CB  B LEU   A 160 ? 0.1680 0.2224 0.2073 0.0259  0.0200  0.0700  160 LEU   A CB  
3466 C  CB  T LEU   A 160 ? 0.1925 0.2479 0.2459 0.0017  0.0255  0.0686  160 LEU   A CB  
3467 C  CG  A LEU   A 160 ? 0.1495 0.2245 0.2309 0.0290  0.0069  0.0657  160 LEU   A CG  
3468 C  CG  B LEU   A 160 ? 0.1759 0.2221 0.2310 0.0206  0.0199  0.0616  160 LEU   A CG  
3469 C  CG  T LEU   A 160 ? 0.1918 0.2513 0.2490 -0.0084 0.0239  0.0656  160 LEU   A CG  
3470 C  CD1 A LEU   A 160 ? 0.1544 0.2269 0.2395 0.0277  0.0053  0.0585  160 LEU   A CD1 
3471 C  CD1 B LEU   A 160 ? 0.1737 0.2204 0.2320 0.0231  0.0226  0.0648  160 LEU   A CD1 
3472 C  CD1 T LEU   A 160 ? 0.1972 0.2560 0.2544 -0.0075 0.0207  0.0602  160 LEU   A CD1 
3473 C  CD2 A LEU   A 160 ? 0.1490 0.2272 0.2408 0.0281  0.0096  0.0574  160 LEU   A CD2 
3474 C  CD2 B LEU   A 160 ? 0.1838 0.2224 0.2413 0.0149  0.0165  0.0546  160 LEU   A CD2 
3475 C  CD2 T LEU   A 160 ? 0.1903 0.2504 0.2538 -0.0157 0.0265  0.0614  160 LEU   A CD2 
3508 N  N   A TYR   A 161 ? 0.1468 0.2088 0.2306 0.0088  0.0290  0.0670  161 TYR   A N   
3509 N  N   B TYR   A 161 ? 0.1266 0.2134 0.1676 0.0211  0.0347  0.0721  161 TYR   A N   
3510 C  CA  A TYR   A 161 ? 0.1483 0.2183 0.2245 -0.0007 0.0249  0.0620  161 TYR   A CA  
3511 C  CA  B TYR   A 161 ? 0.1328 0.2125 0.1683 0.0121  0.0290  0.0743  161 TYR   A CA  
3512 C  C   A TYR   A 161 ? 0.1497 0.2459 0.2329 -0.0089 0.0218  0.0625  161 TYR   A C   
3513 C  C   B TYR   A 161 ? 0.1279 0.2273 0.1811 0.0044  0.0243  0.0727  161 TYR   A C   
3514 O  O   A TYR   A 161 ? 0.1387 0.2494 0.2249 -0.0150 0.0234  0.0761  161 TYR   A O   
3515 O  O   B TYR   A 161 ? 0.1219 0.2261 0.1775 -0.0080 0.0264  0.0803  161 TYR   A O   
3516 C  CB  A TYR   A 161 ? 0.1583 0.2149 0.2264 0.0005  0.0220  0.0556  161 TYR   A CB  
3517 C  CB  B TYR   A 161 ? 0.1456 0.2014 0.1608 0.0066  0.0287  0.0717  161 TYR   A CB  
3518 C  CG  A TYR   A 161 ? 0.1497 0.2045 0.2281 0.0022  0.0144  0.0452  161 TYR   A CG  
3519 C  CG  B TYR   A 161 ? 0.1520 0.1924 0.1722 0.0053  0.0286  0.0516  161 TYR   A CG  
3520 C  CD1 A TYR   A 161 ? 0.1463 0.1967 0.2268 0.0005  0.0103  0.0414  161 TYR   A CD1 
3521 C  CD1 B TYR   A 161 ? 0.1563 0.1860 0.1769 0.0050  0.0264  0.0402  161 TYR   A CD1 
3522 C  CD2 A TYR   A 161 ? 0.1490 0.2007 0.2312 0.0152  0.0108  0.0449  161 TYR   A CD2 
3523 C  CD2 B TYR   A 161 ? 0.1574 0.1901 0.1849 0.0086  0.0307  0.0458  161 TYR   A CD2 
3524 C  CE1 A TYR   A 161 ? 0.1416 0.1853 0.2226 0.0041  0.0013  0.0407  161 TYR   A CE1 
3525 C  CE1 B TYR   A 161 ? 0.1599 0.1826 0.1876 0.0083  0.0205  0.0323  161 TYR   A CE1 
3526 C  CE2 A TYR   A 161 ? 0.1465 0.1889 0.2200 0.0095  0.0085  0.0459  161 TYR   A CE2 
3527 C  CE2 B TYR   A 161 ? 0.1606 0.1858 0.1916 0.0060  0.0286  0.0408  161 TYR   A CE2 
3528 C  CZ  A TYR   A 161 ? 0.1499 0.1787 0.2062 0.0014  -0.0031 0.0473  161 TYR   A CZ  
3529 C  CZ  B TYR   A 161 ? 0.1663 0.1831 0.1977 0.0069  0.0235  0.0327  161 TYR   A CZ  
3530 O  OH  A TYR   A 161 ? 0.1672 0.1669 0.2009 -0.0035 -0.0046 0.0483  161 TYR   A OH  
3531 O  OH  B TYR   A 161 ? 0.1799 0.1841 0.2224 0.0053  0.0152  0.0236  161 TYR   A OH  
3550 N  N   A ASP   A 162 ? 0.1544 0.2721 0.2279 -0.0030 0.0325  0.0585  162 ASP   A N   
3551 N  N   B ASP   A 162 ? 0.1239 0.2420 0.1848 0.0050  0.0288  0.0734  162 ASP   A N   
3552 C  CA  A ASP   A 162 ? 0.1563 0.2981 0.2334 0.0026  0.0302  0.0448  162 ASP   A CA  
3553 C  CA  B ASP   A 162 ? 0.1254 0.2593 0.1989 0.0028  0.0221  0.0693  162 ASP   A CA  
3554 C  C   A ASP   A 162 ? 0.1536 0.2964 0.2421 0.0020  0.0200  0.0295  162 ASP   A C   
3555 C  C   B ASP   A 162 ? 0.1217 0.2583 0.2072 -0.0050 0.0154  0.0688  162 ASP   A C   
3556 O  O   A ASP   A 162 ? 0.1594 0.3019 0.2550 0.0036  0.0202  0.0216  162 ASP   A O   
3557 O  O   B ASP   A 162 ? 0.1206 0.2611 0.2157 -0.0120 0.0141  0.0681  162 ASP   A O   
3558 C  CB  A ASP   A 162 ? 0.1639 0.3200 0.2396 0.0089  0.0395  0.0456  162 ASP   A CB  
3559 C  CB  B ASP   A 162 ? 0.1338 0.2748 0.2152 0.0103  0.0199  0.0687  162 ASP   A CB  
3560 C  CG  A ASP   A 162 ? 0.1727 0.3395 0.2542 0.0103  0.0507  0.0545  162 ASP   A CG  
3561 C  CG  B ASP   A 162 ? 0.1431 0.2846 0.2288 0.0174  0.0102  0.0830  162 ASP   A CG  
3562 O  OD1 A ASP   A 162 ? 0.1855 0.3467 0.2538 0.0030  0.0431  0.0671  162 ASP   A OD1 
3563 O  OD1 B ASP   A 162 ? 0.1484 0.2872 0.2318 0.0193  0.0111  0.0961  162 ASP   A OD1 
3564 O  OD2 A ASP   A 162 ? 0.1840 0.3474 0.2802 0.0253  0.0530  0.0462  162 ASP   A OD2 
3565 O  OD2 B ASP   A 162 ? 0.1492 0.2910 0.2372 0.0219  0.0104  0.0875  162 ASP   A OD2 
3574 N  N   A LYS   A 163 ? 0.1592 0.2956 0.2362 0.0039  0.0114  0.0184  163 LYS   A N   
3575 N  N   B LYS   A 163 ? 0.1263 0.2545 0.2092 -0.0058 0.0077  0.0607  163 LYS   A N   
3576 C  CA  A LYS   A 163 ? 0.1696 0.2962 0.2418 0.0035  -0.0006 0.0214  163 LYS   A CA  
3577 C  CA  B LYS   A 163 ? 0.1368 0.2528 0.2150 -0.0060 0.0062  0.0491  163 LYS   A CA  
3578 C  C   A LYS   A 163 ? 0.1620 0.2829 0.2376 -0.0014 0.0074  0.0369  163 LYS   A C   
3579 C  C   B LYS   A 163 ? 0.1292 0.2463 0.2060 -0.0093 0.0124  0.0446  163 LYS   A C   
3580 O  O   A LYS   A 163 ? 0.1519 0.2718 0.2300 -0.0033 0.0104  0.0358  163 LYS   A O   
3581 O  O   B LYS   A 163 ? 0.1292 0.2508 0.2188 -0.0097 0.0096  0.0493  163 LYS   A O   
3582 C  CB  A LYS   A 163 ? 0.2009 0.3124 0.2701 0.0153  -0.0145 0.0179  163 LYS   A CB  
3583 C  CB  B LYS   A 163 ? 0.1600 0.2593 0.2474 -0.0005 -0.0045 0.0392  163 LYS   A CB  
3584 C  CG  A LYS   A 163 ? 0.2341 0.3286 0.3192 0.0165  -0.0151 0.0140  163 LYS   A CG  
3585 C  CG  B LYS   A 163 ? 0.1824 0.2654 0.2852 -0.0004 -0.0062 0.0310  163 LYS   A CG  
3586 C  CD  A LYS   A 163 ? 0.2619 0.3434 0.3805 0.0171  -0.0124 0.0098  163 LYS   A CD  
3587 C  CD  B LYS   A 163 ? 0.1986 0.2698 0.3229 -0.0002 -0.0067 0.0237  163 LYS   A CD  
3588 C  CE  A LYS   A 163 ? 0.2833 0.3538 0.4249 0.0158  -0.0059 0.0119  163 LYS   A CE  
3589 C  CE  B LYS   A 163 ? 0.2091 0.2722 0.3540 0.0032  -0.0068 0.0183  163 LYS   A CE  
3590 N  NZ  A LYS   A 163 ? 0.2970 0.3606 0.4515 0.0140  -0.0047 0.0134  163 LYS   A NZ  
3591 N  NZ  B LYS   A 163 ? 0.2133 0.2733 0.3689 0.0035  -0.0072 0.0164  163 LYS   A NZ  
3618 N  N   A LEU   A 164 ? 0.1464 0.2735 0.2219 -0.0065 0.0170  0.0483  164 LEU   A N   
3619 N  N   B LEU   A 164 ? 0.1182 0.2340 0.1853 -0.0157 0.0194  0.0427  164 LEU   A N   
3620 C  CA  A LEU   A 164 ? 0.1562 0.2678 0.2104 -0.0151 0.0183  0.0542  164 LEU   A CA  
3621 C  CA  B LEU   A 164 ? 0.1212 0.2276 0.1787 -0.0186 0.0254  0.0459  164 LEU   A CA  
3622 C  C   A LEU   A 164 ? 0.1643 0.2743 0.2132 -0.0223 0.0184  0.0521  164 LEU   A C   
3623 C  C   B LEU   A 164 ? 0.1371 0.2351 0.1775 -0.0213 0.0237  0.0418  164 LEU   A C   
3624 O  O   A LEU   A 164 ? 0.1682 0.2726 0.2148 -0.0322 0.0345  0.0507  164 LEU   A O   
3625 O  O   B LEU   A 164 ? 0.1419 0.2370 0.1646 -0.0289 0.0343  0.0444  164 LEU   A O   
3626 C  CB  A LEU   A 164 ? 0.1566 0.2549 0.2125 -0.0099 0.0114  0.0564  164 LEU   A CB  
3627 C  CB  B LEU   A 164 ? 0.1184 0.2171 0.1784 -0.0169 0.0310  0.0517  164 LEU   A CB  
3628 C  CG  A LEU   A 164 ? 0.1613 0.2423 0.2169 -0.0059 0.0040  0.0614  164 LEU   A CG  
3629 C  CG  B LEU   A 164 ? 0.1208 0.2124 0.1877 -0.0091 0.0318  0.0508  164 LEU   A CG  
3630 C  CD1 A LEU   A 164 ? 0.1524 0.2354 0.2099 -0.0016 -0.0050 0.0742  164 LEU   A CD1 
3631 C  CD1 B LEU   A 164 ? 0.1203 0.2099 0.1979 -0.0086 0.0349  0.0483  164 LEU   A CD1 
3632 C  CD2 A LEU   A 164 ? 0.1764 0.2388 0.2214 -0.0067 0.0085  0.0573  164 LEU   A CD2 
3633 C  CD2 B LEU   A 164 ? 0.1222 0.2141 0.1833 -0.0024 0.0334  0.0494  164 LEU   A CD2 
3656 N  N   A VAL   A 165 ? 0.1534 0.2779 0.2036 -0.0298 0.0204  0.0610  165 VAL   A N   
3657 N  N   B VAL   A 165 ? 0.1416 0.2369 0.1812 -0.0226 0.0187  0.0431  165 VAL   A N   
3658 C  CA  A VAL   A 165 ? 0.1582 0.2848 0.1955 -0.0303 0.0242  0.0656  165 VAL   A CA  
3659 C  CA  B VAL   A 165 ? 0.1546 0.2421 0.1853 -0.0256 0.0141  0.0414  165 VAL   A CA  
3660 C  C   A VAL   A 165 ? 0.1441 0.2955 0.2000 -0.0262 0.0247  0.0692  165 VAL   A C   
3661 C  C   B VAL   A 165 ? 0.1552 0.2554 0.1947 -0.0232 0.0086  0.0404  165 VAL   A C   
3662 O  O   A VAL   A 165 ? 0.1372 0.2986 0.2044 -0.0262 0.0323  0.0612  165 VAL   A O   
3663 O  O   B VAL   A 165 ? 0.1545 0.2537 0.1995 -0.0257 0.0103  0.0365  165 VAL   A O   
3664 C  CB  A VAL   A 165 ? 0.1794 0.2838 0.2021 -0.0323 0.0321  0.0606  165 VAL   A CB  
3665 C  CB  B VAL   A 165 ? 0.1691 0.2371 0.1896 -0.0271 0.0160  0.0364  165 VAL   A CB  
3666 C  CG1 A VAL   A 165 ? 0.1832 0.2882 0.2031 -0.0321 0.0419  0.0497  165 VAL   A CG1 
3667 C  CG1 B VAL   A 165 ? 0.1722 0.2374 0.1904 -0.0272 0.0185  0.0295  165 VAL   A CG1 
3668 C  CG2 A VAL   A 165 ? 0.1921 0.2825 0.2042 -0.0312 0.0244  0.0714  165 VAL   A CG2 
3669 C  CG2 B VAL   A 165 ? 0.1769 0.2352 0.1903 -0.0253 0.0114  0.0417  165 VAL   A CG2 
3688 N  N   A SER   A 166 ? 0.1315 0.3056 0.2176 -0.0216 0.0256  0.0628  166 SER   A N   
3689 N  N   B SER   A 166 ? 0.1544 0.2718 0.2030 -0.0177 0.0040  0.0375  166 SER   A N   
3690 C  CA  A SER   A 166 ? 0.1400 0.3212 0.2349 -0.0209 0.0221  0.0527  166 SER   A CA  
3691 C  CA  B SER   A 166 ? 0.1577 0.2905 0.2130 -0.0148 0.0016  0.0348  166 SER   A CA  
3692 C  C   A SER   A 166 ? 0.1462 0.3318 0.2420 -0.0222 0.0041  0.0353  166 SER   A C   
3693 C  C   B SER   A 166 ? 0.1521 0.3072 0.2169 -0.0117 -0.0039 0.0338  166 SER   A C   
3694 O  O   A SER   A 166 ? 0.1639 0.3480 0.2770 -0.0292 -0.0005 0.0140  166 SER   A O   
3695 O  O   B SER   A 166 ? 0.1518 0.3080 0.2173 -0.0114 -0.0144 0.0285  166 SER   A O   
3696 C  CB  A SER   A 166 ? 0.1588 0.3286 0.2658 -0.0112 0.0134  0.0502  166 SER   A CB  
3697 C  CB  B SER   A 166 ? 0.1691 0.2933 0.2270 -0.0106 -0.0036 0.0313  166 SER   A CB  
3698 O  OG  A SER   A 166 ? 0.1887 0.3376 0.3018 -0.0097 0.0136  0.0521  166 SER   A OG  
3699 O  OG  B SER   A 166 ? 0.1830 0.2972 0.2435 -0.0117 -0.0027 0.0316  166 SER   A OG  
3710 N  N   . SER   A 167 ? 0.1493 0.3245 0.2154 -0.0078 0.0021  0.0407  167 SER   A N   
3711 C  CA  . SER   A 167 ? 0.1773 0.3357 0.2241 0.0082  -0.0039 0.0300  167 SER   A CA  
3712 C  C   . SER   A 167 ? 0.1850 0.3396 0.2206 0.0152  0.0185  0.0285  167 SER   A C   
3713 O  O   . SER   A 167 ? 0.2046 0.3426 0.2309 0.0214  0.0101  0.0310  167 SER   A O   
3714 C  CB  . SER   A 167 ? 0.1854 0.3418 0.2277 0.0168  -0.0002 0.0384  167 SER   A CB  
3715 O  OG  . SER   A 167 ? 0.1856 0.3460 0.2344 0.0176  0.0213  0.0480  167 SER   A OG  
3722 N  N   . PHE   A 168 ? 0.1781 0.3414 0.2151 0.0236  0.0242  0.0244  168 PHE   A N   
3723 C  CA  . PHE   A 168 ? 0.1842 0.3469 0.2286 0.0162  0.0334  0.0174  168 PHE   A CA  
3724 C  C   . PHE   A 168 ? 0.2234 0.3731 0.2888 -0.0033 0.0672  0.0021  168 PHE   A C   
3725 O  O   . PHE   A 168 ? 0.2175 0.3763 0.3262 -0.0172 0.0812  0.0169  168 PHE   A O   
3726 C  CB  . PHE   A 168 ? 0.1769 0.3280 0.2084 0.0129  0.0140  0.0211  168 PHE   A CB  
3727 C  CG  . PHE   A 168 ? 0.1642 0.3107 0.1963 0.0028  0.0043  0.0324  168 PHE   A CG  
3728 C  CD1 . PHE   A 168 ? 0.1632 0.3097 0.2038 -0.0072 0.0042  0.0413  168 PHE   A CD1 
3729 C  CD2 . PHE   A 168 ? 0.1621 0.3027 0.1949 -0.0042 0.0208  0.0294  168 PHE   A CD2 
3730 C  CE1 . PHE   A 168 ? 0.1555 0.3046 0.2009 -0.0081 0.0051  0.0458  168 PHE   A CE1 
3731 C  CE2 . PHE   A 168 ? 0.1697 0.2946 0.2100 -0.0050 0.0151  0.0353  168 PHE   A CE2 
3732 C  CZ  . PHE   A 168 ? 0.1639 0.2988 0.2070 -0.0099 0.0100  0.0415  168 PHE   A CZ  
3742 N  N   A LEU   A 169 ? 0.2699 0.3871 0.3318 -0.0174 0.0577  -0.0200 169 LEU   A N   
3743 N  N   B LEU   A 169 ? 0.2638 0.3842 0.3321 -0.0111 0.0470  -0.0034 169 LEU   A N   
3744 C  CA  A LEU   A 169 ? 0.3362 0.4078 0.4061 -0.0240 0.0274  -0.0314 169 LEU   A CA  
3745 C  CA  B LEU   A 169 ? 0.3089 0.3970 0.3845 -0.0157 0.0207  -0.0056 169 LEU   A CA  
3746 C  C   A LEU   A 169 ? 0.3543 0.4106 0.4355 -0.0271 0.0186  -0.0229 169 LEU   A C   
3747 C  C   B LEU   A 169 ? 0.3204 0.3983 0.3995 -0.0189 0.0098  0.0011  169 LEU   A C   
3748 O  O   A LEU   A 169 ? 0.3603 0.4120 0.4420 -0.0254 0.0177  -0.0250 169 LEU   A O   
3749 O  O   B LEU   A 169 ? 0.3251 0.3990 0.4025 -0.0193 0.0067  0.0020  169 LEU   A O   
3750 C  CB  A LEU   A 169 ? 0.3726 0.4227 0.4339 -0.0286 0.0121  -0.0504 169 LEU   A CB  
3751 C  CB  B LEU   A 169 ? 0.3360 0.4066 0.4110 -0.0179 0.0097  -0.0146 169 LEU   A CB  
3752 C  CG  A LEU   A 169 ? 0.4021 0.4347 0.4595 -0.0343 0.0016  -0.0699 169 LEU   A CG  
3753 C  CG  B LEU   A 169 ? 0.3572 0.4140 0.4340 -0.0204 0.0023  -0.0239 169 LEU   A CG  
3754 C  CD1 A LEU   A 169 ? 0.4118 0.4379 0.4702 -0.0363 -0.0034 -0.0759 169 LEU   A CD1 
3755 C  CD1 B LEU   A 169 ? 0.3642 0.4160 0.4422 -0.0211 -0.0008 -0.0269 169 LEU   A CD1 
3756 C  CD2 A LEU   A 169 ? 0.4116 0.4398 0.4655 -0.0368 0.0004  -0.0768 169 LEU   A CD2 
3757 C  CD2 B LEU   A 169 ? 0.3645 0.4169 0.4403 -0.0216 0.0012  -0.0273 169 LEU   A CD2 
3758 O  OXT A LEU   A 169 ? 0.3508 0.4107 0.4405 -0.0307 0.0193  -0.0174 169 LEU   A OXT 
3759 O  OXT B LEU   A 169 ? 0.3201 0.3979 0.3997 -0.0213 0.0075  0.0044  169 LEU   A OXT 
3782 N  N   A SER   B 1   ? 0.3578 0.3474 0.3278 -0.1115 -0.0800 0.0300  1   SER   B N   
3783 N  N   B SER   B 1   ? 0.3336 0.3383 0.3346 -0.0623 -0.0480 0.0237  1   SER   B N   
3784 C  CA  A SER   B 1   ? 0.3490 0.3507 0.3375 -0.1196 -0.0874 0.0233  1   SER   B CA  
3785 C  CA  B SER   B 1   ? 0.3290 0.3394 0.3366 -0.0651 -0.0496 0.0234  1   SER   B CA  
3786 C  C   A SER   B 1   ? 0.3259 0.3529 0.3269 -0.1234 -0.0934 0.0391  1   SER   B C   
3787 C  C   B SER   B 1   ? 0.3164 0.3393 0.3283 -0.0676 -0.0562 0.0386  1   SER   B C   
3788 O  O   A SER   B 1   ? 0.3368 0.3567 0.3162 -0.1160 -0.0830 0.0390  1   SER   B O   
3789 O  O   B SER   B 1   ? 0.3206 0.3405 0.3222 -0.0658 -0.0533 0.0351  1   SER   B O   
3790 C  CB  A SER   B 1   ? 0.3614 0.3502 0.3537 -0.1182 -0.0817 0.0068  1   SER   B CB  
3791 C  CB  B SER   B 1   ? 0.3345 0.3392 0.3430 -0.0639 -0.0443 0.0107  1   SER   B CB  
3792 O  OG  A SER   B 1   ? 0.3763 0.3586 0.3988 -0.1126 -0.0704 0.0041  1   SER   B OG  
3793 O  OG  B SER   B 1   ? 0.3400 0.3420 0.3615 -0.0634 -0.0410 0.0046  1   SER   B OG  
3808 N  N   A MET   B 2   ? 0.3006 0.3499 0.3327 -0.1262 -0.0916 0.0733  2   MET   B N   
3809 N  N   B MET   B 2   ? 0.3007 0.3364 0.3244 -0.0707 -0.0623 0.0652  2   MET   B N   
3810 C  CA  A MET   B 2   ? 0.2861 0.3521 0.3522 -0.1070 -0.0927 0.0965  2   MET   B CA  
3811 C  CA  B MET   B 2   ? 0.2860 0.3342 0.3243 -0.0685 -0.0707 0.0905  2   MET   B CA  
3812 C  C   A MET   B 2   ? 0.2582 0.3338 0.3217 -0.0834 -0.0986 0.1259  2   MET   B C   
3813 C  C   B MET   B 2   ? 0.2605 0.3188 0.3060 -0.0720 -0.0816 0.1169  2   MET   B C   
3814 O  O   A MET   B 2   ? 0.2573 0.3457 0.3188 -0.0695 -0.1097 0.1302  2   MET   B O   
3815 O  O   B MET   B 2   ? 0.2601 0.3212 0.3010 -0.0694 -0.0838 0.1175  2   MET   B O   
3816 C  CB  A MET   B 2   ? 0.3143 0.3811 0.4323 -0.0914 -0.0723 0.0758  2   MET   B CB  
3817 C  CB  B MET   B 2   ? 0.3000 0.3495 0.3541 -0.0564 -0.0639 0.0850  2   MET   B CB  
3818 C  CG  A MET   B 2   ? 0.3410 0.4088 0.5062 -0.0719 -0.0511 0.0630  2   MET   B CG  
3819 C  CG  B MET   B 2   ? 0.3116 0.3630 0.3770 -0.0438 -0.0581 0.0867  2   MET   B CG  
3820 S  SD  A MET   B 2   ? 0.3681 0.4361 0.5785 -0.0527 -0.0356 0.0526  2   MET   B SD  
3821 S  SD  B MET   B 2   ? 0.3225 0.3766 0.3955 -0.0316 -0.0562 0.0901  2   MET   B SD  
3822 C  CE  A MET   B 2   ? 0.3718 0.4393 0.5845 -0.0517 -0.0298 0.0524  2   MET   B CE  
3823 C  CE  B MET   B 2   ? 0.3245 0.3791 0.4026 -0.0317 -0.0524 0.0849  2   MET   B CE  
3842 N  N   . VAL   B 3   ? 0.2352 0.2986 0.2955 -0.0804 -0.0898 0.1399  3   VAL   B N   
3843 C  CA  . VAL   B 3   ? 0.2202 0.2573 0.2928 -0.0709 -0.0826 0.1294  3   VAL   B CA  
3844 C  C   . VAL   B 3   ? 0.1987 0.2461 0.2608 -0.0674 -0.0709 0.1124  3   VAL   B C   
3845 O  O   . VAL   B 3   ? 0.2012 0.2673 0.2721 -0.0678 -0.0710 0.1177  3   VAL   B O   
3846 C  CB  . VAL   B 3   ? 0.2360 0.2453 0.3473 -0.0728 -0.0691 0.1101  3   VAL   B CB  
3847 C  CG1 . VAL   B 3   ? 0.2439 0.2399 0.3672 -0.0763 -0.0602 0.1042  3   VAL   B CG1 
3848 C  CG2 . VAL   B 3   ? 0.2385 0.2490 0.3628 -0.0663 -0.0594 0.1188  3   VAL   B CG2 
3859 N  N   . ASN   B 4   ? 0.1851 0.2117 0.2265 -0.0660 -0.0595 0.0843  4   ASN   B N   
3860 C  CA  . ASN   B 4   ? 0.1870 0.2112 0.1994 -0.0594 -0.0487 0.0471  4   ASN   B CA  
3861 C  C   . ASN   B 4   ? 0.1889 0.2238 0.1924 -0.0585 -0.0395 0.0357  4   ASN   B C   
3862 O  O   . ASN   B 4   ? 0.1903 0.2285 0.2079 -0.0524 -0.0306 0.0181  4   ASN   B O   
3863 C  CB  . ASN   B 4   ? 0.1859 0.2074 0.1860 -0.0534 -0.0591 0.0352  4   ASN   B CB  
3864 C  CG  . ASN   B 4   ? 0.1882 0.1892 0.1753 -0.0491 -0.0565 0.0347  4   ASN   B CG  
3865 O  OD1 . ASN   B 4   ? 0.1935 0.1743 0.1832 -0.0480 -0.0551 0.0355  4   ASN   B OD1 
3866 N  ND2 . ASN   B 4   ? 0.2041 0.1949 0.1819 -0.0267 -0.0394 0.0290  4   ASN   B ND2 
3873 N  N   . SER   B 5   ? 0.2010 0.2441 0.1974 -0.0595 -0.0287 0.0324  5   SER   B N   
3874 C  CA  . SER   B 5   ? 0.2308 0.2814 0.2202 -0.0493 -0.0115 0.0314  5   SER   B CA  
3875 C  C   . SER   B 5   ? 0.2543 0.2896 0.2519 -0.0672 0.0155  0.0341  5   SER   B C   
3876 O  O   . SER   B 5   ? 0.2730 0.2868 0.3216 -0.0605 0.0479  0.0376  5   SER   B O   
3877 C  CB  . SER   B 5   ? 0.2424 0.2992 0.2333 -0.0384 -0.0052 0.0416  5   SER   B CB  
3878 O  OG  . SER   B 5   ? 0.2631 0.3212 0.2842 -0.0243 -0.0033 0.0449  5   SER   B OG  
3884 N  N   . PHE   B 6   ? 0.2726 0.3097 0.2333 -0.0763 0.0262  0.0433  6   PHE   B N   
3885 C  CA  . PHE   B 6   ? 0.2842 0.3157 0.2107 -0.0973 0.0322  0.0228  6   PHE   B CA  
3886 C  C   . PHE   B 6   ? 0.3362 0.3521 0.2552 -0.1038 0.0604  -0.0051 6   PHE   B C   
3887 O  O   . PHE   B 6   ? 0.3507 0.3821 0.2840 -0.0955 0.0516  -0.0184 6   PHE   B O   
3888 C  CB  . PHE   B 6   ? 0.2545 0.2923 0.1863 -0.0893 0.0121  0.0192  6   PHE   B CB  
3889 C  CG  . PHE   B 6   ? 0.2249 0.2584 0.1801 -0.0846 -0.0039 0.0180  6   PHE   B CG  
3890 C  CD1 . PHE   B 6   ? 0.2290 0.2326 0.1640 -0.0767 -0.0143 0.0162  6   PHE   B CD1 
3891 C  CD2 . PHE   B 6   ? 0.2013 0.2533 0.1794 -0.0722 -0.0057 0.0434  6   PHE   B CD2 
3892 C  CE1 . PHE   B 6   ? 0.2210 0.2114 0.1668 -0.0679 -0.0183 0.0187  6   PHE   B CE1 
3893 C  CE2 . PHE   B 6   ? 0.2031 0.2383 0.2039 -0.0618 -0.0020 0.0381  6   PHE   B CE2 
3894 C  CZ  . PHE   B 6   ? 0.2110 0.2178 0.1907 -0.0604 -0.0112 0.0217  6   PHE   B CZ  
3904 N  N   . SER   B 7   ? 0.3712 0.3434 0.2753 -0.1280 0.0922  -0.0266 7   SER   B N   
3905 C  CA  . SER   B 7   ? 0.4070 0.3634 0.3259 -0.1299 0.1148  -0.0384 7   SER   B CA  
3906 C  C   . SER   B 7   ? 0.4075 0.3408 0.3100 -0.1297 0.1309  -0.0575 7   SER   B C   
3907 O  O   . SER   B 7   ? 0.4159 0.3354 0.3311 -0.1336 0.1288  -0.0640 7   SER   B O   
3908 C  CB  . SER   B 7   ? 0.4295 0.3932 0.3903 -0.1295 0.1265  -0.0295 7   SER   B CB  
3909 O  OG  . SER   B 7   ? 0.4338 0.3992 0.4395 -0.1298 0.1305  -0.0220 7   SER   B OG  
3915 N  N   . GLY   B 8   ? 0.4037 0.3284 0.3084 -0.1138 0.1371  -0.0707 8   GLY   B N   
3916 C  CA  . GLY   B 8   ? 0.3900 0.3093 0.3018 -0.1046 0.1396  -0.0755 8   GLY   B CA  
3917 C  C   . GLY   B 8   ? 0.3684 0.2799 0.2921 -0.0997 0.1387  -0.0714 8   GLY   B C   
3918 O  O   . GLY   B 8   ? 0.3796 0.2855 0.3249 -0.0893 0.1362  -0.0814 8   GLY   B O   
3922 N  N   . TYR   B 9   ? 0.3473 0.2533 0.2666 -0.0894 0.1133  -0.0754 9   TYR   B N   
3923 C  CA  . TYR   B 9   ? 0.3258 0.2252 0.2414 -0.0765 0.0865  -0.0598 9   TYR   B CA  
3924 C  C   . TYR   B 9   ? 0.3210 0.2215 0.2317 -0.0750 0.0543  -0.0471 9   TYR   B C   
3925 O  O   . TYR   B 9   ? 0.3322 0.2400 0.2657 -0.0747 0.0569  -0.0386 9   TYR   B O   
3926 C  CB  . TYR   B 9   ? 0.3139 0.2004 0.2449 -0.0688 0.0824  -0.0567 9   TYR   B CB  
3927 C  CG  . TYR   B 9   ? 0.3037 0.1836 0.2459 -0.0754 0.0717  -0.0562 9   TYR   B CG  
3928 C  CD1 . TYR   B 9   ? 0.3046 0.1839 0.2571 -0.0886 0.0730  -0.0503 9   TYR   B CD1 
3929 C  CD2 . TYR   B 9   ? 0.2924 0.1839 0.2298 -0.0719 0.0606  -0.0593 9   TYR   B CD2 
3930 C  CE1 . TYR   B 9   ? 0.3000 0.1939 0.2540 -0.0921 0.0786  -0.0647 9   TYR   B CE1 
3931 C  CE2 . TYR   B 9   ? 0.2934 0.1806 0.2324 -0.0719 0.0634  -0.0567 9   TYR   B CE2 
3932 C  CZ  . TYR   B 9   ? 0.2966 0.1937 0.2456 -0.0835 0.0733  -0.0652 9   TYR   B CZ  
3933 O  OH  . TYR   B 9   ? 0.2944 0.2046 0.2596 -0.0930 0.0717  -0.0798 9   TYR   B OH  
3943 N  N   . LEU   B 10  ? 0.3061 0.1975 0.2095 -0.0728 0.0281  -0.0425 10  LEU   B N   
3944 C  CA  . LEU   B 10  ? 0.3011 0.1930 0.2073 -0.0829 -0.0104 -0.0377 10  LEU   B CA  
3945 C  C   . LEU   B 10  ? 0.2824 0.1918 0.2082 -0.0827 -0.0283 -0.0313 10  LEU   B C   
3946 O  O   . LEU   B 10  ? 0.2634 0.1931 0.2162 -0.0671 -0.0207 -0.0206 10  LEU   B O   
3947 C  CB  . LEU   B 10  ? 0.3188 0.1906 0.2262 -0.0821 -0.0289 -0.0251 10  LEU   B CB  
3948 C  CG  . LEU   B 10  ? 0.3384 0.1994 0.2635 -0.0750 -0.0495 -0.0091 10  LEU   B CG  
3949 C  CD1 . LEU   B 10  ? 0.3528 0.2081 0.2816 -0.0706 -0.0468 -0.0080 10  LEU   B CD1 
3950 C  CD2 . LEU   B 10  ? 0.3444 0.2030 0.2916 -0.0751 -0.0448 0.0106  10  LEU   B CD2 
3962 N  N   . LYS   B 11  ? 0.2971 0.2178 0.2088 -0.0755 -0.0374 -0.0218 11  LYS   B N   
3963 C  CA  . LYS   B 11  ? 0.3117 0.2460 0.2528 -0.0607 -0.0459 -0.0264 11  LYS   B CA  
3964 C  C   . LYS   B 11  ? 0.2895 0.2249 0.2573 -0.0790 -0.0432 -0.0369 11  LYS   B C   
3965 O  O   . LYS   B 11  ? 0.3039 0.2418 0.2873 -0.0933 -0.0430 -0.0655 11  LYS   B O   
3966 C  CB  . LYS   B 11  ? 0.3439 0.2955 0.3240 -0.0351 -0.0481 -0.0255 11  LYS   B CB  
3967 C  CG  . LYS   B 11  ? 0.3743 0.3274 0.3932 -0.0195 -0.0474 -0.0261 11  LYS   B CG  
3968 C  CD  . LYS   B 11  ? 0.3978 0.3486 0.4540 -0.0116 -0.0461 -0.0295 11  LYS   B CD  
3969 C  CE  . LYS   B 11  ? 0.4137 0.3638 0.4984 -0.0089 -0.0477 -0.0315 11  LYS   B CE  
3970 N  NZ  . LYS   B 11  ? 0.4226 0.3730 0.5208 -0.0085 -0.0511 -0.0312 11  LYS   B NZ  
3984 N  N   . LEU   B 12  ? 0.2506 0.1968 0.2507 -0.0706 -0.0405 -0.0350 12  LEU   B N   
3985 C  CA  . LEU   B 12  ? 0.2343 0.1805 0.2616 -0.0564 -0.0305 -0.0310 12  LEU   B CA  
3986 C  C   . LEU   B 12  ? 0.2234 0.1777 0.2688 -0.0580 -0.0401 -0.0284 12  LEU   B C   
3987 O  O   . LEU   B 12  ? 0.2212 0.1800 0.2872 -0.0622 -0.0556 -0.0229 12  LEU   B O   
3988 C  CB  . LEU   B 12  ? 0.2312 0.1601 0.2607 -0.0433 -0.0202 -0.0344 12  LEU   B CB  
3989 C  CG  . LEU   B 12  ? 0.2282 0.1542 0.2641 -0.0435 -0.0102 -0.0259 12  LEU   B CG  
3990 C  CD1 . LEU   B 12  ? 0.2381 0.1572 0.2633 -0.0274 -0.0085 -0.0057 12  LEU   B CD1 
3991 C  CD2 . LEU   B 12  ? 0.2324 0.1619 0.2726 -0.0435 -0.0019 -0.0290 12  LEU   B CD2 
4003 N  N   . THR   B 13  ? 0.2170 0.1800 0.2673 -0.0573 -0.0451 -0.0363 13  THR   B N   
4004 C  CA  . THR   B 13  ? 0.2162 0.1904 0.2664 -0.0648 -0.0612 -0.0198 13  THR   B CA  
4005 C  C   . THR   B 13  ? 0.2540 0.2125 0.2875 -0.0762 -0.0792 -0.0112 13  THR   B C   
4006 O  O   . THR   B 13  ? 0.2729 0.2115 0.3065 -0.0819 -0.0471 -0.0097 13  THR   B O   
4007 C  CB  . THR   B 13  ? 0.1950 0.1908 0.2692 -0.0551 -0.0543 -0.0149 13  THR   B CB  
4008 O  OG1 . THR   B 13  ? 0.1843 0.1843 0.2765 -0.0466 -0.0425 -0.0195 13  THR   B OG1 
4009 C  CG2 . THR   B 13  ? 0.1958 0.2006 0.2749 -0.0489 -0.0424 -0.0014 13  THR   B CG2 
4017 N  N   A ASP   B 14  ? 0.2679 0.2287 0.2922 -0.0802 -0.1118 0.0001  14  ASP   B N   
4018 N  N   B ASP   B 14  ? 0.2618 0.2221 0.2950 -0.0737 -0.0843 -0.0032 14  ASP   B N   
4019 C  CA  A ASP   B 14  ? 0.2816 0.2451 0.3189 -0.0802 -0.1188 0.0169  14  ASP   B CA  
4020 C  CA  B ASP   B 14  ? 0.2690 0.2313 0.3096 -0.0702 -0.0816 0.0056  14  ASP   B CA  
4021 C  C   A ASP   B 14  ? 0.2698 0.2259 0.2788 -0.0821 -0.1047 0.0133  14  ASP   B C   
4022 C  C   B ASP   B 14  ? 0.2556 0.2156 0.2760 -0.0702 -0.0879 0.0064  14  ASP   B C   
4023 O  O   A ASP   B 14  ? 0.2963 0.2411 0.2785 -0.0794 -0.0992 0.0208  14  ASP   B O   
4024 O  O   B ASP   B 14  ? 0.2641 0.2180 0.2711 -0.0671 -0.0895 0.0059  14  ASP   B O   
4025 C  CB  A ASP   B 14  ? 0.3030 0.2812 0.3975 -0.0769 -0.1338 0.0213  14  ASP   B CB  
4026 C  CB  B ASP   B 14  ? 0.2867 0.2547 0.3607 -0.0660 -0.0723 0.0087  14  ASP   B CB  
4027 C  CG  A ASP   B 14  ? 0.3284 0.3125 0.4770 -0.0681 -0.1274 0.0134  14  ASP   B CG  
4028 C  CG  B ASP   B 14  ? 0.3033 0.2745 0.4065 -0.0611 -0.0622 0.0056  14  ASP   B CG  
4029 O  OD1 A ASP   B 14  ? 0.3426 0.3232 0.5000 -0.0679 -0.1244 0.0028  14  ASP   B OD1 
4030 O  OD1 B ASP   B 14  ? 0.3105 0.2843 0.4197 -0.0594 -0.0571 0.0029  14  ASP   B OD1 
4031 O  OD2 A ASP   B 14  ? 0.3316 0.3261 0.5099 -0.0657 -0.1246 0.0155  14  ASP   B OD2 
4032 O  OD2 B ASP   B 14  ? 0.3068 0.2795 0.4222 -0.0631 -0.0607 0.0054  14  ASP   B OD2 
4041 N  N   . ASN   B 15  ? 0.2338 0.1973 0.2574 -0.0656 -0.0914 0.0132  15  ASN   B N   
4042 C  CA  . ASN   B 15  ? 0.1896 0.1648 0.2385 -0.0428 -0.0677 0.0065  15  ASN   B CA  
4043 C  C   . ASN   B 15  ? 0.1711 0.1492 0.2231 -0.0252 -0.0476 -0.0036 15  ASN   B C   
4044 O  O   . ASN   B 15  ? 0.1689 0.1435 0.2376 -0.0251 -0.0509 -0.0114 15  ASN   B O   
4045 C  CB  . ASN   B 15  ? 0.1830 0.1598 0.2549 -0.0234 -0.0623 0.0100  15  ASN   B CB  
4046 C  CG  . ASN   B 15  ? 0.1662 0.1547 0.2614 -0.0282 -0.0393 0.0068  15  ASN   B CG  
4047 O  OD1 . ASN   B 15  ? 0.1721 0.1808 0.2891 -0.0481 -0.0439 0.0117  15  ASN   B OD1 
4048 N  ND2 . ASN   B 15  ? 0.1656 0.1330 0.2480 -0.0155 -0.0111 -0.0113 15  ASN   B ND2 
4056 N  N   . VAL   B 16  ? 0.1713 0.1437 0.2197 -0.0308 -0.0493 -0.0040 16  VAL   B N   
4057 C  CA  . VAL   B 16  ? 0.1720 0.1500 0.2025 -0.0311 -0.0358 -0.0238 16  VAL   B CA  
4058 C  C   . VAL   B 16  ? 0.1687 0.1645 0.1959 -0.0387 -0.0287 -0.0135 16  VAL   B C   
4059 O  O   . VAL   B 16  ? 0.1757 0.1773 0.2162 -0.0342 -0.0336 -0.0248 16  VAL   B O   
4060 C  CB  . VAL   B 16  ? 0.1783 0.1498 0.2115 -0.0190 -0.0274 -0.0175 16  VAL   B CB  
4061 C  CG1 . VAL   B 16  ? 0.1870 0.1434 0.2007 -0.0062 -0.0257 -0.0084 16  VAL   B CG1 
4062 C  CG2 . VAL   B 16  ? 0.1806 0.1561 0.2314 -0.0092 -0.0256 -0.0135 16  VAL   B CG2 
4072 N  N   . TYR   B 17  ? 0.1745 0.1698 0.1999 -0.0361 -0.0251 -0.0225 17  TYR   B N   
4073 C  CA  . TYR   B 17  ? 0.1817 0.1793 0.1967 -0.0449 -0.0277 -0.0068 17  TYR   B CA  
4074 C  C   . TYR   B 17  ? 0.1789 0.1528 0.1942 -0.0429 -0.0177 -0.0075 17  TYR   B C   
4075 O  O   . TYR   B 17  ? 0.1785 0.1579 0.2015 -0.0400 -0.0218 -0.0305 17  TYR   B O   
4076 C  CB  . TYR   B 17  ? 0.2137 0.2246 0.2255 -0.0244 -0.0308 0.0294  17  TYR   B CB  
4077 C  CG  . TYR   B 17  ? 0.2441 0.2754 0.2702 -0.0122 -0.0523 0.0420  17  TYR   B CG  
4078 C  CD1 . TYR   B 17  ? 0.2631 0.2942 0.3027 -0.0081 -0.0592 0.0511  17  TYR   B CD1 
4079 C  CD2 . TYR   B 17  ? 0.2646 0.3051 0.3031 -0.0023 -0.0612 0.0450  17  TYR   B CD2 
4080 C  CE1 . TYR   B 17  ? 0.2806 0.3226 0.3265 0.0010  -0.0695 0.0478  17  TYR   B CE1 
4081 C  CE2 . TYR   B 17  ? 0.2809 0.3286 0.3291 0.0087  -0.0742 0.0504  17  TYR   B CE2 
4082 C  CZ  . TYR   B 17  ? 0.2911 0.3381 0.3415 0.0097  -0.0787 0.0512  17  TYR   B CZ  
4083 O  OH  . TYR   B 17  ? 0.3056 0.3519 0.3586 0.0153  -0.0849 0.0517  17  TYR   B OH  
4093 N  N   . ILE   B 18  ? 0.1897 0.1505 0.1973 -0.0326 -0.0092 -0.0174 18  ILE   B N   
4094 C  CA  . ILE   B 18  ? 0.1928 0.1475 0.1981 -0.0382 -0.0032 -0.0244 18  ILE   B CA  
4095 C  C   . ILE   B 18  ? 0.2086 0.1528 0.1924 -0.0488 -0.0010 -0.0366 18  ILE   B C   
4096 O  O   . ILE   B 18  ? 0.2278 0.1680 0.1984 -0.0423 0.0013  -0.0428 18  ILE   B O   
4097 C  CB  . ILE   B 18  ? 0.1970 0.1502 0.2143 -0.0418 -0.0076 -0.0187 18  ILE   B CB  
4098 C  CG1 . ILE   B 18  ? 0.1960 0.1546 0.2237 -0.0433 -0.0047 -0.0127 18  ILE   B CG1 
4099 C  CG2 . ILE   B 18  ? 0.1985 0.1588 0.2142 -0.0451 -0.0114 -0.0168 18  ILE   B CG2 
4100 C  CD1 . ILE   B 18  ? 0.2021 0.1793 0.2388 -0.0416 -0.0135 0.0067  18  ILE   B CD1 
4112 N  N   . LYS   B 19  ? 0.2104 0.1559 0.2108 -0.0300 0.0386  -0.0358 19  LYS   B N   
4113 C  CA  . LYS   B 19  ? 0.2129 0.1585 0.2328 -0.0336 0.0358  -0.0478 19  LYS   B CA  
4114 C  C   . LYS   B 19  ? 0.1919 0.1541 0.2449 -0.0367 0.0371  -0.0524 19  LYS   B C   
4115 O  O   . LYS   B 19  ? 0.1880 0.1629 0.2230 -0.0243 0.0277  -0.0494 19  LYS   B O   
4116 C  CB  . LYS   B 19  ? 0.2390 0.1818 0.2477 -0.0368 0.0470  -0.0341 19  LYS   B CB  
4117 C  CG  . LYS   B 19  ? 0.2670 0.2047 0.2701 -0.0451 0.0538  -0.0325 19  LYS   B CG  
4118 C  CD  . LYS   B 19  ? 0.2962 0.2333 0.2774 -0.0518 0.0634  -0.0297 19  LYS   B CD  
4119 C  CE  . LYS   B 19  ? 0.3224 0.2565 0.2928 -0.0509 0.0591  -0.0352 19  LYS   B CE  
4120 N  NZ  . LYS   B 19  ? 0.3349 0.2720 0.2958 -0.0519 0.0653  -0.0318 19  LYS   B NZ  
4134 N  N   . ASN   B 20  ? 0.1900 0.1716 0.2770 -0.0252 0.0435  -0.0675 20  ASN   B N   
4135 C  CA  . ASN   B 20  ? 0.1951 0.1871 0.3040 -0.0167 0.0414  -0.0831 20  ASN   B CA  
4136 C  C   . ASN   B 20  ? 0.1939 0.2023 0.3011 -0.0218 0.0527  -0.0965 20  ASN   B C   
4137 O  O   . ASN   B 20  ? 0.2161 0.2378 0.3214 -0.0369 0.0513  -0.0964 20  ASN   B O   
4138 C  CB  . ASN   B 20  ? 0.2218 0.1911 0.3350 0.0054  0.0309  -0.0856 20  ASN   B CB  
4139 C  CG  . ASN   B 20  ? 0.2478 0.1981 0.3588 0.0333  0.0284  -0.0923 20  ASN   B CG  
4140 O  OD1 . ASN   B 20  ? 0.2782 0.2209 0.3839 0.0451  0.0268  -0.0922 20  ASN   B OD1 
4141 N  ND2 . ASN   B 20  ? 0.2347 0.1961 0.3576 0.0372  0.0203  -0.0906 20  ASN   B ND2 
4148 N  N   . ALA   B 21  ? 0.1909 0.1882 0.2965 -0.0261 0.0580  -0.0766 21  ALA   B N   
4149 C  CA  . ALA   B 21  ? 0.2020 0.1917 0.3071 -0.0326 0.0443  -0.0618 21  ALA   B CA  
4150 C  C   . ALA   B 21  ? 0.2008 0.1684 0.2931 -0.0226 0.0460  -0.0448 21  ALA   B C   
4151 O  O   . ALA   B 21  ? 0.2052 0.1570 0.2919 -0.0325 0.0432  -0.0342 21  ALA   B O   
4152 C  CB  . ALA   B 21  ? 0.2191 0.2197 0.3212 -0.0426 0.0446  -0.0503 21  ALA   B CB  
4158 N  N   . ASP   B 22  ? 0.1888 0.1615 0.2827 -0.0208 0.0372  -0.0365 22  ASP   B N   
4159 C  CA  . ASP   B 22  ? 0.1862 0.1515 0.2667 -0.0115 0.0284  -0.0278 22  ASP   B CA  
4160 C  C   . ASP   B 22  ? 0.1785 0.1503 0.2250 -0.0216 0.0181  -0.0121 22  ASP   B C   
4161 O  O   . ASP   B 22  ? 0.1778 0.1590 0.2209 -0.0180 0.0151  -0.0102 22  ASP   B O   
4162 C  CB  . ASP   B 22  ? 0.1949 0.1633 0.2963 -0.0042 0.0264  -0.0135 22  ASP   B CB  
4163 C  CG  . ASP   B 22  ? 0.1974 0.1819 0.3317 0.0037  0.0086  -0.0165 22  ASP   B CG  
4164 O  OD1 . ASP   B 22  ? 0.2071 0.1777 0.3259 0.0068  -0.0101 -0.0172 22  ASP   B OD1 
4165 O  OD2 . ASP   B 22  ? 0.2049 0.2054 0.3829 0.0087  -0.0139 -0.0228 22  ASP   B OD2 
4170 N  N   . ILE   B 23  ? 0.1812 0.1416 0.1896 -0.0141 0.0030  0.0128  23  ILE   B N   
4171 C  CA  . ILE   B 23  ? 0.1700 0.1408 0.1785 -0.0088 -0.0020 0.0055  23  ILE   B CA  
4172 C  C   . ILE   B 23  ? 0.1581 0.1420 0.1677 -0.0060 -0.0087 0.0047  23  ILE   B C   
4173 O  O   . ILE   B 23  ? 0.1534 0.1450 0.1683 -0.0145 -0.0070 0.0110  23  ILE   B O   
4174 C  CB  . ILE   B 23  ? 0.1664 0.1464 0.1971 -0.0158 0.0037  0.0157  23  ILE   B CB  
4175 C  CG1 . ILE   B 23  ? 0.1639 0.1530 0.2039 -0.0135 0.0054  0.0216  23  ILE   B CG1 
4176 C  CG2 . ILE   B 23  ? 0.1748 0.1661 0.1977 -0.0133 0.0059  0.0116  23  ILE   B CG2 
4177 C  CD1 . ILE   B 23  ? 0.1687 0.1664 0.2161 -0.0080 -0.0024 0.0222  23  ILE   B CD1 
4189 N  N   . VAL   B 24  ? 0.1629 0.1440 0.1870 -0.0083 -0.0083 0.0049  24  VAL   B N   
4190 C  CA  . VAL   B 24  ? 0.1577 0.1471 0.2134 -0.0066 -0.0162 0.0002  24  VAL   B CA  
4191 C  C   . VAL   B 24  ? 0.1559 0.1510 0.2118 -0.0129 -0.0096 0.0077  24  VAL   B C   
4192 O  O   . VAL   B 24  ? 0.1505 0.1609 0.2194 -0.0196 -0.0055 0.0106  24  VAL   B O   
4193 C  CB  . VAL   B 24  ? 0.1689 0.1598 0.2221 0.0051  -0.0209 0.0023  24  VAL   B CB  
4194 C  CG1 . VAL   B 24  ? 0.1665 0.1607 0.2520 -0.0083 -0.0255 -0.0013 24  VAL   B CG1 
4195 C  CG2 . VAL   B 24  ? 0.1781 0.1905 0.2296 0.0098  -0.0224 -0.0017 24  VAL   B CG2 
4205 N  N   . GLU   B 25  ? 0.1771 0.1614 0.2171 -0.0096 0.0042  0.0079  25  GLU   B N   
4206 C  CA  . GLU   B 25  ? 0.1893 0.1862 0.2367 0.0009  0.0156  -0.0030 25  GLU   B CA  
4207 C  C   . GLU   B 25  ? 0.1829 0.1822 0.1986 -0.0108 0.0166  -0.0002 25  GLU   B C   
4208 O  O   . GLU   B 25  ? 0.1828 0.1989 0.2188 -0.0097 0.0169  0.0044  25  GLU   B O   
4209 C  CB  . GLU   B 25  ? 0.2288 0.2334 0.3031 0.0277  0.0259  -0.0048 25  GLU   B CB  
4210 C  CG  . GLU   B 25  ? 0.2673 0.2951 0.4029 0.0342  0.0231  -0.0040 25  GLU   B CG  
4211 C  CD  . GLU   B 25  ? 0.3083 0.3499 0.4831 0.0292  0.0229  -0.0052 25  GLU   B CD  
4212 O  OE1 . GLU   B 25  ? 0.3326 0.3714 0.5113 0.0330  0.0272  -0.0030 25  GLU   B OE1 
4213 O  OE2 . GLU   B 25  ? 0.3273 0.3654 0.5074 0.0277  0.0159  -0.0095 25  GLU   B OE2 
4220 N  N   A GLU   B 26  ? 0.1823 0.1752 0.1746 -0.0288 0.0071  -0.0019 26  GLU   B N   
4221 N  N   B GLU   B 26  ? 0.1835 0.1828 0.1883 -0.0217 0.0120  0.0024  26  GLU   B N   
4222 C  CA  A GLU   B 26  ? 0.1804 0.1897 0.1877 -0.0438 -0.0059 0.0053  26  GLU   B CA  
4223 C  CA  B GLU   B 26  ? 0.1839 0.1914 0.1941 -0.0316 0.0069  0.0079  26  GLU   B CA  
4224 C  C   A GLU   B 26  ? 0.1639 0.1917 0.1732 -0.0276 0.0005  0.0173  26  GLU   B C   
4225 C  C   B GLU   B 26  ? 0.1675 0.1869 0.1776 -0.0264 0.0063  0.0154  26  GLU   B C   
4226 O  O   A GLU   B 26  ? 0.1839 0.2114 0.1777 -0.0244 -0.0012 0.0157  26  GLU   B O   
4227 O  O   B GLU   B 26  ? 0.1763 0.1959 0.1779 -0.0253 0.0044  0.0136  26  GLU   B O   
4228 C  CB  A GLU   B 26  ? 0.2129 0.2096 0.2156 -0.0544 -0.0013 0.0168  26  GLU   B CB  
4229 C  CB  B GLU   B 26  ? 0.2053 0.2063 0.2159 -0.0395 0.0122  0.0118  26  GLU   B CB  
4230 C  CG  A GLU   B 26  ? 0.2529 0.2415 0.2673 -0.0562 0.0151  -0.0000 26  GLU   B CG  
4231 C  CG  B GLU   B 26  ? 0.2291 0.2260 0.2475 -0.0440 0.0244  0.0067  26  GLU   B CG  
4232 C  CD  A GLU   B 26  ? 0.2760 0.2629 0.2914 -0.0695 0.0263  -0.0330 26  GLU   B CD  
4233 C  CD  B GLU   B 26  ? 0.2450 0.2424 0.2644 -0.0533 0.0388  -0.0023 26  GLU   B CD  
4234 O  OE1 A GLU   B 26  ? 0.2910 0.2546 0.3091 -0.0803 0.0481  -0.0414 26  GLU   B OE1 
4235 O  OE1 B GLU   B 26  ? 0.2558 0.2414 0.2669 -0.0565 0.0601  0.0031  26  GLU   B OE1 
4236 O  OE2 A GLU   B 26  ? 0.2810 0.2925 0.3241 -0.0643 0.0253  -0.0297 26  GLU   B OE2 
4237 O  OE2 B GLU   B 26  ? 0.2476 0.2583 0.2889 -0.0540 0.0373  0.0003  26  GLU   B OE2 
4250 N  N   . ALA   B 27  ? 0.1502 0.1719 0.1723 -0.0261 0.0070  0.0213  27  ALA   B N   
4251 C  CA  . ALA   B 27  ? 0.1494 0.1644 0.1884 -0.0167 -0.0004 0.0343  27  ALA   B CA  
4252 C  C   . ALA   B 27  ? 0.1542 0.1759 0.2059 -0.0149 0.0100  0.0385  27  ALA   B C   
4253 O  O   . ALA   B 27  ? 0.1652 0.1829 0.2189 -0.0051 0.0096  0.0445  27  ALA   B O   
4254 C  CB  . ALA   B 27  ? 0.1649 0.1480 0.1989 -0.0162 0.0005  0.0275  27  ALA   B CB  
4261 N  N   . LYS   B 28  ? 0.1515 0.1971 0.2489 -0.0203 0.0177  0.0518  28  LYS   B N   
4262 C  CA  . LYS   B 28  ? 0.1678 0.2285 0.2739 -0.0142 0.0506  0.0805  28  LYS   B CA  
4263 C  C   . LYS   B 28  ? 0.1876 0.2435 0.2644 -0.0098 0.0630  0.0685  28  LYS   B C   
4264 O  O   . LYS   B 28  ? 0.2150 0.2424 0.2778 -0.0090 0.0615  0.0640  28  LYS   B O   
4265 C  CB  . LYS   B 28  ? 0.1907 0.2587 0.3212 -0.0011 0.0744  0.0965  28  LYS   B CB  
4266 C  CG  . LYS   B 28  ? 0.2265 0.3072 0.3672 0.0051  0.0841  0.1035  28  LYS   B CG  
4267 C  CD  . LYS   B 28  ? 0.2812 0.3669 0.4241 0.0064  0.0986  0.1082  28  LYS   B CD  
4268 C  CE  . LYS   B 28  ? 0.3253 0.4085 0.4724 0.0107  0.1009  0.1139  28  LYS   B CE  
4269 N  NZ  . LYS   B 28  ? 0.3538 0.4248 0.4944 0.0152  0.1004  0.1188  28  LYS   B NZ  
4283 N  N   . LYS   B 29  ? 0.2051 0.2686 0.2606 0.0078  0.0709  0.0657  29  LYS   B N   
4284 C  CA  . LYS   B 29  ? 0.2493 0.3049 0.2908 0.0109  0.0661  0.0603  29  LYS   B CA  
4285 C  C   . LYS   B 29  ? 0.2439 0.3037 0.2549 0.0114  0.0443  0.0713  29  LYS   B C   
4286 O  O   . LYS   B 29  ? 0.2643 0.3242 0.2600 0.0179  0.0414  0.0787  29  LYS   B O   
4287 C  CB  . LYS   B 29  ? 0.3073 0.3434 0.3700 0.0087  0.0682  0.0461  29  LYS   B CB  
4288 C  CG  . LYS   B 29  ? 0.3575 0.3739 0.4569 0.0064  0.0685  0.0397  29  LYS   B CG  
4289 C  CD  . LYS   B 29  ? 0.4018 0.4011 0.5261 0.0042  0.0726  0.0315  29  LYS   B CD  
4290 C  CE  . LYS   B 29  ? 0.4369 0.4207 0.5743 0.0016  0.0780  0.0254  29  LYS   B CE  
4291 N  NZ  . LYS   B 29  ? 0.4509 0.4238 0.6035 0.0001  0.0796  0.0218  29  LYS   B NZ  
4305 N  N   . VAL   B 30  ? 0.2128 0.2824 0.2391 -0.0007 0.0274  0.0676  30  VAL   B N   
4306 C  CA  . VAL   B 30  ? 0.2003 0.2711 0.2668 -0.0141 -0.0053 0.0703  30  VAL   B CA  
4307 C  C   . VAL   B 30  ? 0.1805 0.2628 0.2552 -0.0168 0.0008  0.0814  30  VAL   B C   
4308 O  O   . VAL   B 30  ? 0.1951 0.2749 0.2562 -0.0080 -0.0048 0.0938  30  VAL   B O   
4309 C  CB  . VAL   B 30  ? 0.2064 0.2705 0.3081 -0.0269 -0.0313 0.0692  30  VAL   B CB  
4310 C  CG1 . VAL   B 30  ? 0.2148 0.2761 0.3051 -0.0241 -0.0294 0.0671  30  VAL   B CG1 
4311 C  CG2 . VAL   B 30  ? 0.2187 0.2717 0.3308 -0.0364 -0.0391 0.0566  30  VAL   B CG2 
4321 N  N   . LYS   B 31  ? 0.1706 0.2299 0.2719 -0.0323 0.0001  0.0918  31  LYS   B N   
4322 C  CA  . LYS   B 31  ? 0.1583 0.2258 0.3036 -0.0404 -0.0088 0.0909  31  LYS   B CA  
4323 C  C   . LYS   B 31  ? 0.1536 0.1885 0.2695 -0.0388 -0.0282 0.0781  31  LYS   B C   
4324 O  O   . LYS   B 31  ? 0.1593 0.2020 0.2759 -0.0340 -0.0245 0.0952  31  LYS   B O   
4325 C  CB  . LYS   B 31  ? 0.1757 0.2686 0.3560 -0.0388 0.0200  0.1011  31  LYS   B CB  
4326 C  CG  . LYS   B 31  ? 0.2086 0.3164 0.4021 -0.0361 0.0322  0.0944  31  LYS   B CG  
4327 C  CD  . LYS   B 31  ? 0.2497 0.3646 0.4469 -0.0318 0.0259  0.0807  31  LYS   B CD  
4328 C  CE  . LYS   B 31  ? 0.2778 0.3932 0.4878 -0.0311 0.0157  0.0693  31  LYS   B CE  
4329 N  NZ  . LYS   B 31  ? 0.2943 0.4150 0.5036 -0.0259 0.0053  0.0599  31  LYS   B NZ  
4343 N  N   . PRO   B 32  ? 0.1665 0.1556 0.2200 -0.0356 -0.0425 0.0502  32  PRO   B N   
4344 C  CA  . PRO   B 32  ? 0.1804 0.1531 0.1870 -0.0321 -0.0431 0.0317  32  PRO   B CA  
4345 C  C   . PRO   B 32  ? 0.1906 0.1450 0.1868 -0.0365 -0.0567 0.0404  32  PRO   B C   
4346 O  O   . PRO   B 32  ? 0.2031 0.1477 0.2166 -0.0408 -0.0734 0.0351  32  PRO   B O   
4347 C  CB  . PRO   B 32  ? 0.1931 0.1486 0.1772 -0.0423 -0.0383 0.0188  32  PRO   B CB  
4348 C  CG  . PRO   B 32  ? 0.2091 0.1371 0.1796 -0.0349 -0.0491 0.0207  32  PRO   B CG  
4349 C  CD  . PRO   B 32  ? 0.1948 0.1433 0.2071 -0.0277 -0.0572 0.0273  32  PRO   B CD  
4357 N  N   . THR   B 33  ? 0.1910 0.1346 0.1674 -0.0330 -0.0525 0.0310  33  THR   B N   
4358 C  CA  . THR   B 33  ? 0.1969 0.1428 0.1639 -0.0381 -0.0485 0.0295  33  THR   B CA  
4359 C  C   . THR   B 33  ? 0.1992 0.1333 0.1624 -0.0394 -0.0475 0.0184  33  THR   B C   
4360 O  O   . THR   B 33  ? 0.2213 0.1360 0.1718 -0.0480 -0.0530 0.0193  33  THR   B O   
4361 C  CB  . THR   B 33  ? 0.2022 0.1556 0.1698 -0.0259 -0.0525 0.0306  33  THR   B CB  
4362 O  OG1 . THR   B 33  ? 0.1923 0.1569 0.1840 -0.0265 -0.0494 0.0368  33  THR   B OG1 
4363 C  CG2 . THR   B 33  ? 0.2226 0.1651 0.1814 -0.0146 -0.0535 0.0244  33  THR   B CG2 
4371 N  N   . VAL   B 34  ? 0.1820 0.1289 0.1543 -0.0375 -0.0409 0.0157  34  VAL   B N   
4372 C  CA  . VAL   B 34  ? 0.1688 0.1316 0.1446 -0.0283 -0.0335 0.0092  34  VAL   B CA  
4373 C  C   . VAL   B 34  ? 0.1530 0.1238 0.1335 -0.0283 -0.0218 0.0094  34  VAL   B C   
4374 O  O   . VAL   B 34  ? 0.1659 0.1270 0.1429 -0.0229 -0.0322 0.0066  34  VAL   B O   
4375 C  CB  . VAL   B 34  ? 0.1720 0.1350 0.1663 -0.0115 -0.0291 0.0018  34  VAL   B CB  
4376 C  CG1 . VAL   B 34  ? 0.1708 0.1486 0.1731 -0.0131 -0.0145 -0.0067 34  VAL   B CG1 
4377 C  CG2 . VAL   B 34  ? 0.1742 0.1417 0.1880 -0.0110 -0.0202 0.0144  34  VAL   B CG2 
4387 N  N   . VAL   B 35  ? 0.1427 0.1235 0.1259 -0.0272 -0.0174 0.0092  35  VAL   B N   
4388 C  CA  . VAL   B 35  ? 0.1348 0.1246 0.1259 -0.0212 -0.0102 0.0102  35  VAL   B CA  
4389 C  C   . VAL   B 35  ? 0.1296 0.1183 0.1275 -0.0194 -0.0176 0.0076  35  VAL   B C   
4390 O  O   . VAL   B 35  ? 0.1340 0.1257 0.1358 -0.0239 -0.0078 -0.0044 35  VAL   B O   
4391 C  CB  . VAL   B 35  ? 0.1377 0.1407 0.1334 -0.0207 0.0037  0.0071  35  VAL   B CB  
4392 C  CG1 . VAL   B 35  ? 0.1311 0.1472 0.1607 -0.0224 -0.0007 0.0037  35  VAL   B CG1 
4393 C  CG2 . VAL   B 35  ? 0.1389 0.1389 0.1576 -0.0118 -0.0018 0.0048  35  VAL   B CG2 
4403 N  N   . VAL   B 36  ? 0.1268 0.1188 0.1235 -0.0162 -0.0147 0.0093  36  VAL   B N   
4404 C  CA  . VAL   B 36  ? 0.1280 0.1134 0.1246 -0.0140 -0.0098 0.0079  36  VAL   B CA  
4405 C  C   . VAL   B 36  ? 0.1251 0.1168 0.1136 -0.0115 -0.0060 0.0071  36  VAL   B C   
4406 O  O   . VAL   B 36  ? 0.1290 0.1254 0.1498 -0.0123 -0.0028 -0.0027 36  VAL   B O   
4407 C  CB  . VAL   B 36  ? 0.1303 0.1202 0.1333 -0.0178 -0.0103 0.0087  36  VAL   B CB  
4408 C  CG1 . VAL   B 36  ? 0.1303 0.1293 0.1473 -0.0205 -0.0092 0.0071  36  VAL   B CG1 
4409 C  CG2 . VAL   B 36  ? 0.1347 0.1234 0.1376 -0.0114 -0.0141 0.0064  36  VAL   B CG2 
4419 N  N   . ASN   B 37  ? 0.1250 0.1205 0.1205 -0.0007 -0.0068 0.0084  37  ASN   B N   
4420 C  CA  . ASN   B 37  ? 0.1269 0.1208 0.1327 -0.0025 -0.0151 0.0062  37  ASN   B CA  
4421 C  C   . ASN   B 37  ? 0.1255 0.1238 0.1362 0.0023  -0.0119 0.0069  37  ASN   B C   
4422 O  O   . ASN   B 37  ? 0.1325 0.1307 0.1388 0.0016  -0.0014 0.0079  37  ASN   B O   
4423 C  CB  . ASN   B 37  ? 0.1280 0.1270 0.1254 -0.0025 -0.0135 0.0068  37  ASN   B CB  
4424 C  CG  . ASN   B 37  ? 0.1359 0.1260 0.1372 -0.0049 -0.0074 -0.0014 37  ASN   B CG  
4425 O  OD1 . ASN   B 37  ? 0.1412 0.1287 0.1574 0.0062  -0.0154 0.0000  37  ASN   B OD1 
4426 N  ND2 . ASN   B 37  ? 0.1406 0.1210 0.1312 0.0021  -0.0148 0.0067  37  ASN   B ND2 
4433 N  N   . ALA   B 38  ? 0.1355 0.1230 0.1398 0.0042  0.0022  0.0045  38  ALA   B N   
4434 C  CA  . ALA   B 38  ? 0.1430 0.1226 0.1405 0.0028  -0.0002 0.0082  38  ALA   B CA  
4435 C  C   . ALA   B 38  ? 0.1362 0.1215 0.1354 0.0026  0.0022  0.0106  38  ALA   B C   
4436 O  O   . ALA   B 38  ? 0.1505 0.1307 0.1515 0.0036  -0.0014 0.0080  38  ALA   B O   
4437 C  CB  . ALA   B 38  ? 0.1670 0.1359 0.1532 -0.0075 0.0013  0.0093  38  ALA   B CB  
4443 N  N   . ALA   B 39  ? 0.1412 0.1233 0.1308 0.0090  -0.0042 0.0019  39  ALA   B N   
4444 C  CA  . ALA   B 39  ? 0.1491 0.1303 0.1309 0.0087  -0.0088 0.0099  39  ALA   B CA  
4445 C  C   . ALA   B 39  ? 0.1575 0.1375 0.1176 0.0130  -0.0068 0.0070  39  ALA   B C   
4446 O  O   . ALA   B 39  ? 0.1579 0.1437 0.1494 -0.0011 -0.0107 0.0146  39  ALA   B O   
4447 C  CB  . ALA   B 39  ? 0.1439 0.1340 0.1554 -0.0019 -0.0017 0.0023  39  ALA   B CB  
4453 N  N   . ASN   B 40  ? 0.1569 0.1549 0.1198 0.0038  0.0014  -0.0067 40  ASN   B N   
4454 C  CA  . ASN   B 40  ? 0.1678 0.1640 0.1287 0.0057  -0.0058 -0.0060 40  ASN   B CA  
4455 C  C   . ASN   B 40  ? 0.1706 0.1620 0.1066 0.0107  -0.0073 0.0015  40  ASN   B C   
4456 O  O   . ASN   B 40  ? 0.1634 0.1559 0.1296 0.0090  -0.0092 -0.0008 40  ASN   B O   
4457 C  CB  . ASN   B 40  ? 0.1792 0.1623 0.1536 0.0100  -0.0166 0.0101  40  ASN   B CB  
4458 C  CG  . ASN   B 40  ? 0.1836 0.1670 0.1884 0.0021  -0.0240 0.0157  40  ASN   B CG  
4459 O  OD1 . ASN   B 40  ? 0.1783 0.1647 0.2655 0.0068  -0.0388 0.0159  40  ASN   B OD1 
4460 N  ND2 . ASN   B 40  ? 0.1865 0.1669 0.1870 0.0018  -0.0175 0.0134  40  ASN   B ND2 
4467 N  N   . VAL   B 41  ? 0.1805 0.1632 0.1243 0.0171  0.0059  -0.0002 41  VAL   B N   
4468 C  CA  . VAL   B 41  ? 0.1850 0.1764 0.1326 0.0119  0.0038  -0.0075 41  VAL   B CA  
4469 C  C   . VAL   B 41  ? 0.1819 0.1748 0.1353 0.0205  -0.0057 -0.0058 41  VAL   B C   
4470 O  O   . VAL   B 41  ? 0.1787 0.1704 0.1497 0.0173  -0.0097 -0.0118 41  VAL   B O   
4471 C  CB  . VAL   B 41  ? 0.1996 0.1981 0.1593 -0.0037 0.0242  -0.0173 41  VAL   B CB  
4472 C  CG1 . VAL   B 41  ? 0.1951 0.1941 0.1771 -0.0114 0.0305  -0.0194 41  VAL   B CG1 
4473 C  CG2 . VAL   B 41  ? 0.2133 0.2185 0.1582 -0.0125 0.0232  -0.0169 41  VAL   B CG2 
4483 N  N   . TYR   B 42  ? 0.1893 0.1779 0.1243 0.0176  -0.0210 0.0020  42  TYR   B N   
4484 C  CA  . TYR   B 42  ? 0.1896 0.1806 0.1331 0.0187  -0.0302 -0.0091 42  TYR   B CA  
4485 C  C   . TYR   B 42  ? 0.1733 0.1637 0.1443 0.0184  -0.0234 -0.0073 42  TYR   B C   
4486 O  O   . TYR   B 42  ? 0.1740 0.1667 0.1877 0.0133  -0.0252 -0.0095 42  TYR   B O   
4487 C  CB  . TYR   B 42  ? 0.2100 0.2029 0.1617 0.0184  -0.0281 0.0002  42  TYR   B CB  
4488 C  CG  . TYR   B 42  ? 0.2087 0.2147 0.1559 0.0020  -0.0300 0.0107  42  TYR   B CG  
4489 C  CD1 . TYR   B 42  ? 0.2068 0.2142 0.1337 -0.0044 -0.0163 0.0057  42  TYR   B CD1 
4490 C  CD2 . TYR   B 42  ? 0.2176 0.2218 0.1887 0.0009  -0.0124 0.0114  42  TYR   B CD2 
4491 C  CE1 . TYR   B 42  ? 0.2181 0.2268 0.1409 0.0028  -0.0098 0.0041  42  TYR   B CE1 
4492 C  CE2 . TYR   B 42  ? 0.2230 0.2361 0.1897 0.0052  0.0096  0.0207  42  TYR   B CE2 
4493 C  CZ  . TYR   B 42  ? 0.2355 0.2469 0.1749 0.0196  0.0113  0.0109  42  TYR   B CZ  
4494 O  OH  . TYR   B 42  ? 0.2698 0.2716 0.2104 0.0332  0.0180  0.0196  42  TYR   B OH  
4504 N  N   . LEU   B 43  ? 0.1643 0.1496 0.1335 0.0044  -0.0150 -0.0078 43  LEU   B N   
4505 C  CA  . LEU   B 43  ? 0.1606 0.1494 0.1282 0.0023  -0.0152 0.0007  43  LEU   B CA  
4506 C  C   . LEU   B 43  ? 0.1700 0.1503 0.1217 0.0009  -0.0127 0.0035  43  LEU   B C   
4507 O  O   . LEU   B 43  ? 0.1643 0.1526 0.1607 0.0044  -0.0222 0.0058  43  LEU   B O   
4508 C  CB  . LEU   B 43  ? 0.1572 0.1421 0.1469 0.0014  -0.0251 -0.0064 43  LEU   B CB  
4509 C  CG  . LEU   B 43  ? 0.1659 0.1401 0.1564 0.0005  -0.0285 -0.0060 43  LEU   B CG  
4510 C  CD1 . LEU   B 43  ? 0.1764 0.1445 0.1859 0.0001  -0.0419 -0.0045 43  LEU   B CD1 
4511 C  CD2 . LEU   B 43  ? 0.1645 0.1404 0.1653 -0.0046 -0.0280 -0.0063 43  LEU   B CD2 
4523 N  N   . LYS   B 44  ? 0.1662 0.1505 0.1345 0.0090  -0.0127 0.0004  44  LYS   B N   
4524 C  CA  . LYS   B 44  ? 0.1762 0.1633 0.1453 0.0118  -0.0165 0.0067  44  LYS   B CA  
4525 C  C   . LYS   B 44  ? 0.1665 0.1568 0.1440 0.0144  -0.0181 0.0036  44  LYS   B C   
4526 O  O   . LYS   B 44  ? 0.1836 0.1539 0.1756 0.0011  -0.0093 0.0031  44  LYS   B O   
4527 C  CB  . LYS   B 44  ? 0.2021 0.1800 0.1713 0.0244  -0.0328 0.0008  44  LYS   B CB  
4528 C  CG  . LYS   B 44  ? 0.2389 0.2063 0.2064 0.0178  -0.0583 0.0051  44  LYS   B CG  
4529 C  CD  . LYS   B 44  ? 0.2753 0.2278 0.2666 0.0023  -0.0613 0.0028  44  LYS   B CD  
4530 C  CE  . LYS   B 44  ? 0.3053 0.2536 0.3125 -0.0016 -0.0641 0.0143  44  LYS   B CE  
4531 N  NZ  . LYS   B 44  ? 0.3141 0.2642 0.3369 -0.0010 -0.0700 0.0284  44  LYS   B NZ  
4545 N  N   . HIS   B 45  ? 0.1568 0.1593 0.1398 0.0074  -0.0151 0.0082  45  HIS   B N   
4546 C  CA  . HIS   B 45  ? 0.1614 0.1524 0.1477 0.0109  -0.0102 0.0017  45  HIS   B CA  
4547 C  C   . HIS   B 45  ? 0.1860 0.1722 0.1816 0.0178  -0.0175 -0.0042 45  HIS   B C   
4548 O  O   . HIS   B 45  ? 0.2037 0.2013 0.2217 0.0424  0.0042  -0.0019 45  HIS   B O   
4549 C  CB  . HIS   B 45  ? 0.1551 0.1531 0.1509 0.0010  -0.0118 -0.0030 45  HIS   B CB  
4550 C  CG  . HIS   B 45  ? 0.1568 0.1479 0.1473 -0.0039 -0.0082 0.0025  45  HIS   B CG  
4551 N  ND1 . HIS   B 45  ? 0.1615 0.1439 0.1446 -0.0020 -0.0137 -0.0036 45  HIS   B ND1 
4552 C  CD2 . HIS   B 45  ? 0.1665 0.1510 0.1592 -0.0075 -0.0192 0.0016  45  HIS   B CD2 
4553 C  CE1 . HIS   B 45  ? 0.1754 0.1366 0.1336 -0.0002 -0.0223 0.0006  45  HIS   B CE1 
4554 N  NE2 . HIS   B 45  ? 0.1771 0.1417 0.1464 0.0010  -0.0198 -0.0011 45  HIS   B NE2 
4562 N  N   A GLY   B 46  ? 0.1912 0.1631 0.2173 0.0184  -0.0366 0.0030  46  GLY   B N   
4563 N  N   B GLY   B 46  ? 0.1911 0.1760 0.2025 0.0167  -0.0279 0.0028  46  GLY   B N   
4564 C  CA  A GLY   B 46  ? 0.2073 0.1775 0.2526 0.0197  -0.0430 0.0049  46  GLY   B CA  
4565 C  CA  B GLY   B 46  ? 0.1995 0.1876 0.2233 0.0160  -0.0332 0.0085  46  GLY   B CA  
4566 C  C   A GLY   B 46  ? 0.2100 0.1914 0.2940 0.0278  -0.0362 0.0037  46  GLY   B C   
4567 C  C   B GLY   B 46  ? 0.2039 0.1991 0.2480 0.0188  -0.0311 0.0142  46  GLY   B C   
4568 O  O   A GLY   B 46  ? 0.2211 0.2025 0.3755 0.0330  -0.0128 -0.0228 46  GLY   B O   
4569 O  O   B GLY   B 46  ? 0.2071 0.2087 0.2574 0.0203  -0.0284 0.0231  46  GLY   B O   
4576 N  N   . GLY   B 47  ? 0.2059 0.2038 0.2657 0.0113  -0.0206 0.0042  47  GLY   B N   
4577 C  CA  . GLY   B 47  ? 0.1954 0.1784 0.2323 0.0044  -0.0179 0.0054  47  GLY   B CA  
4578 C  C   . GLY   B 47  ? 0.1754 0.1532 0.1980 0.0018  -0.0057 0.0101  47  GLY   B C   
4579 O  O   . GLY   B 47  ? 0.1811 0.1391 0.2018 0.0033  -0.0100 0.0122  47  GLY   B O   
4584 N  N   . GLY   B 48  ? 0.1537 0.1438 0.1925 0.0030  -0.0148 0.0169  48  GLY   B N   
4585 C  CA  . GLY   B 48  ? 0.1510 0.1406 0.1887 -0.0022 -0.0069 0.0092  48  GLY   B CA  
4586 C  C   . GLY   B 48  ? 0.1459 0.1373 0.1742 0.0011  -0.0041 0.0059  48  GLY   B C   
4587 O  O   . GLY   B 48  ? 0.1425 0.1385 0.2023 0.0032  -0.0091 0.0068  48  GLY   B O   
4591 N  N   . VAL   B 49  ? 0.1481 0.1431 0.1668 0.0129  -0.0036 0.0076  49  VAL   B N   
4592 C  CA  . VAL   B 49  ? 0.1503 0.1489 0.1581 0.0157  -0.0107 -0.0024 49  VAL   B CA  
4593 C  C   . VAL   B 49  ? 0.1425 0.1377 0.1398 0.0087  -0.0074 0.0027  49  VAL   B C   
4594 O  O   . VAL   B 49  ? 0.1489 0.1465 0.1612 0.0039  -0.0021 0.0044  49  VAL   B O   
4595 C  CB  . VAL   B 49  ? 0.1540 0.1643 0.1858 0.0065  -0.0248 -0.0053 49  VAL   B CB  
4596 C  CG1 . VAL   B 49  ? 0.1550 0.1686 0.1851 0.0155  -0.0323 0.0060  49  VAL   B CG1 
4597 C  CG2 . VAL   B 49  ? 0.1707 0.1796 0.2062 -0.0047 -0.0397 -0.0080 49  VAL   B CG2 
4607 N  N   . ALA   B 50  ? 0.1370 0.1359 0.1410 0.0032  -0.0021 0.0040  50  ALA   B N   
4608 C  CA  . ALA   B 50  ? 0.1371 0.1293 0.1458 0.0080  -0.0092 0.0034  50  ALA   B CA  
4609 C  C   . ALA   B 50  ? 0.1463 0.1327 0.1502 0.0057  -0.0048 -0.0035 50  ALA   B C   
4610 O  O   . ALA   B 50  ? 0.1461 0.1353 0.1524 0.0039  -0.0043 -0.0025 50  ALA   B O   
4611 C  CB  . ALA   B 50  ? 0.1406 0.1329 0.1512 0.0048  -0.0080 0.0016  50  ALA   B CB  
4617 N  N   . GLY   B 51  ? 0.1433 0.1451 0.1620 0.0108  -0.0161 0.0101  51  GLY   B N   
4618 C  CA  . GLY   B 51  ? 0.1419 0.1525 0.1778 0.0182  -0.0178 0.0086  51  GLY   B CA  
4619 C  C   . GLY   B 51  ? 0.1446 0.1474 0.1749 0.0179  -0.0127 0.0057  51  GLY   B C   
4620 O  O   . GLY   B 51  ? 0.1467 0.1624 0.1934 0.0076  -0.0142 -0.0017 51  GLY   B O   
4624 N  N   . ALA   B 52  ? 0.1410 0.1398 0.1670 0.0172  -0.0067 0.0040  52  ALA   B N   
4625 C  CA  . ALA   B 52  ? 0.1497 0.1505 0.1707 0.0165  0.0003  -0.0051 52  ALA   B CA  
4626 C  C   . ALA   B 52  ? 0.1406 0.1500 0.1584 0.0097  0.0010  -0.0003 52  ALA   B C   
4627 O  O   . ALA   B 52  ? 0.1440 0.1540 0.1799 0.0095  -0.0002 -0.0009 52  ALA   B O   
4628 C  CB  . ALA   B 52  ? 0.1662 0.1502 0.1807 0.0074  0.0053  -0.0069 52  ALA   B CB  
4634 N  N   . LEU   B 53  ? 0.1350 0.1433 0.1533 0.0179  -0.0018 0.0006  53  LEU   B N   
4635 C  CA  . LEU   B 53  ? 0.1355 0.1487 0.1455 0.0109  -0.0096 -0.0009 53  LEU   B CA  
4636 C  C   . LEU   B 53  ? 0.1379 0.1426 0.1515 0.0104  0.0009  0.0021  53  LEU   B C   
4637 O  O   . LEU   B 53  ? 0.1435 0.1486 0.1725 -0.0001 0.0006  0.0118  53  LEU   B O   
4638 C  CB  . LEU   B 53  ? 0.1401 0.1553 0.1567 0.0059  -0.0059 0.0138  53  LEU   B CB  
4639 C  CG  . LEU   B 53  ? 0.1350 0.1653 0.1682 -0.0011 -0.0037 0.0192  53  LEU   B CG  
4640 C  CD1 . LEU   B 53  ? 0.1373 0.1820 0.1952 0.0127  -0.0074 0.0020  53  LEU   B CD1 
4641 C  CD2 . LEU   B 53  ? 0.1470 0.1929 0.1863 -0.0132 -0.0110 -0.0087 53  LEU   B CD2 
4653 N  N   . ASN   B 54  ? 0.1387 0.1378 0.1507 0.0047  -0.0054 0.0006  54  ASN   B N   
4654 C  CA  . ASN   B 54  ? 0.1457 0.1465 0.1575 0.0061  -0.0048 0.0001  54  ASN   B CA  
4655 C  C   . ASN   B 54  ? 0.1386 0.1489 0.1797 0.0038  0.0016  0.0008  54  ASN   B C   
4656 O  O   . ASN   B 54  ? 0.1389 0.1569 0.1860 -0.0051 0.0026  0.0019  54  ASN   B O   
4657 C  CB  . ASN   B 54  ? 0.1480 0.1621 0.1669 0.0055  -0.0033 0.0025  54  ASN   B CB  
4658 C  CG  . ASN   B 54  ? 0.1477 0.1683 0.1779 0.0054  -0.0098 -0.0022 54  ASN   B CG  
4659 O  OD1 . ASN   B 54  ? 0.1431 0.1652 0.1911 -0.0015 -0.0130 -0.0095 54  ASN   B OD1 
4660 N  ND2 . ASN   B 54  ? 0.1627 0.1880 0.2009 -0.0005 -0.0326 0.0086  54  ASN   B ND2 
4667 N  N   . LYS   B 55  ? 0.1377 0.1545 0.2001 0.0077  -0.0030 -0.0030 55  LYS   B N   
4668 C  CA  . LYS   B 55  ? 0.1436 0.1670 0.2140 0.0167  -0.0122 -0.0045 55  LYS   B CA  
4669 C  C   . LYS   B 55  ? 0.1416 0.1661 0.2056 0.0126  0.0034  -0.0117 55  LYS   B C   
4670 O  O   . LYS   B 55  ? 0.1399 0.1799 0.2223 0.0094  0.0044  -0.0065 55  LYS   B O   
4671 C  CB  . LYS   B 55  ? 0.1554 0.1876 0.2614 0.0268  0.0016  0.0082  55  LYS   B CB  
4672 C  CG  . LYS   B 55  ? 0.1892 0.2113 0.3359 0.0326  0.0110  0.0219  55  LYS   B CG  
4673 C  CD  . LYS   B 55  ? 0.2228 0.2352 0.4017 0.0376  0.0237  0.0306  55  LYS   B CD  
4674 C  CE  . LYS   B 55  ? 0.2485 0.2552 0.4656 0.0369  0.0368  0.0363  55  LYS   B CE  
4675 N  NZ  . LYS   B 55  ? 0.2541 0.2684 0.4970 0.0379  0.0224  0.0479  55  LYS   B NZ  
4689 N  N   . ALA   B 56  ? 0.1426 0.1712 0.1850 0.0099  0.0042  -0.0117 56  ALA   B N   
4690 C  CA  . ALA   B 56  ? 0.1521 0.1874 0.1886 0.0064  0.0081  -0.0077 56  ALA   B CA  
4691 C  C   . ALA   B 56  ? 0.1524 0.1843 0.1839 0.0065  0.0135  0.0014  56  ALA   B C   
4692 O  O   . ALA   B 56  ? 0.1639 0.1953 0.2057 0.0079  0.0267  -0.0002 56  ALA   B O   
4693 C  CB  . ALA   B 56  ? 0.1577 0.2078 0.1904 -0.0051 0.0024  -0.0110 56  ALA   B CB  
4699 N  N   . THR   B 57  ? 0.1481 0.1726 0.1915 -0.0021 0.0143  0.0041  57  THR   B N   
4700 C  CA  . THR   B 57  ? 0.1555 0.1745 0.1813 -0.0066 0.0203  0.0031  57  THR   B CA  
4701 C  C   . THR   B 57  ? 0.1525 0.1843 0.2029 -0.0030 0.0233  0.0028  57  THR   B C   
4702 O  O   . THR   B 57  ? 0.1629 0.1853 0.2092 -0.0197 0.0148  -0.0009 57  THR   B O   
4703 C  CB  . THR   B 57  ? 0.1626 0.1563 0.1632 -0.0028 0.0183  0.0045  57  THR   B CB  
4704 O  OG1 . THR   B 57  ? 0.1595 0.1518 0.1897 -0.0049 0.0151  0.0004  57  THR   B OG1 
4705 C  CG2 . THR   B 57  ? 0.1604 0.1652 0.1555 -0.0067 0.0105  0.0060  57  THR   B CG2 
4713 N  N   . ASN   B 58  ? 0.1400 0.2042 0.2289 -0.0108 0.0090  -0.0093 58  ASN   B N   
4714 C  CA  . ASN   B 58  ? 0.1652 0.2496 0.2774 -0.0293 0.0241  -0.0022 58  ASN   B CA  
4715 C  C   . ASN   B 58  ? 0.1438 0.2217 0.2359 -0.0205 -0.0019 -0.0006 58  ASN   B C   
4716 O  O   . ASN   B 58  ? 0.1512 0.2288 0.2402 -0.0224 0.0012  -0.0167 58  ASN   B O   
4717 C  CB  . ASN   B 58  ? 0.2640 0.3306 0.3990 -0.0474 0.0610  0.0122  58  ASN   B CB  
4718 C  CG  . ASN   B 58  ? 0.3766 0.4075 0.5376 -0.0502 0.0816  0.0325  58  ASN   B CG  
4719 O  OD1 . ASN   B 58  ? 0.3988 0.4283 0.5929 -0.0520 0.0873  0.0383  58  ASN   B OD1 
4720 N  ND2 . ASN   B 58  ? 0.4726 0.4726 0.5815 -0.0518 0.0907  0.0384  58  ASN   B ND2 
4727 N  N   . ASN   B 59  ? 0.1457 0.2037 0.2178 -0.0126 -0.0075 0.0057  59  ASN   B N   
4728 C  CA  . ASN   B 59  ? 0.1485 0.2030 0.2065 -0.0126 -0.0209 0.0110  59  ASN   B CA  
4729 C  C   . ASN   B 59  ? 0.1411 0.1945 0.2022 -0.0163 -0.0159 0.0020  59  ASN   B C   
4730 O  O   . ASN   B 59  ? 0.1478 0.1954 0.2012 -0.0139 -0.0151 0.0010  59  ASN   B O   
4731 C  CB  . ASN   B 59  ? 0.1616 0.2210 0.2195 -0.0074 -0.0318 0.0115  59  ASN   B CB  
4732 C  CG  . ASN   B 59  ? 0.1720 0.2362 0.2353 -0.0059 -0.0409 0.0041  59  ASN   B CG  
4733 O  OD1 . ASN   B 59  ? 0.1721 0.2395 0.2381 -0.0044 -0.0319 0.0210  59  ASN   B OD1 
4734 N  ND2 . ASN   B 59  ? 0.1792 0.2445 0.2383 -0.0097 -0.0434 -0.0079 59  ASN   B ND2 
4741 N  N   . ALA   B 60  ? 0.1410 0.1832 0.2003 -0.0133 -0.0052 -0.0003 60  ALA   B N   
4742 C  CA  . ALA   B 60  ? 0.1520 0.1709 0.2036 -0.0161 -0.0078 0.0040  60  ALA   B CA  
4743 C  C   . ALA   B 60  ? 0.1551 0.1589 0.1770 -0.0143 -0.0085 0.0008  60  ALA   B C   
4744 O  O   . ALA   B 60  ? 0.1578 0.1620 0.1913 -0.0210 -0.0011 -0.0118 60  ALA   B O   
4745 C  CB  . ALA   B 60  ? 0.1713 0.1704 0.2308 -0.0134 0.0026  0.0046  60  ALA   B CB  
4751 N  N   . MET   B 61  ? 0.1495 0.1489 0.1689 -0.0126 -0.0037 0.0039  61  MET   B N   
4752 C  CA  . MET   B 61  ? 0.1415 0.1485 0.1616 -0.0107 -0.0083 0.0012  61  MET   B CA  
4753 C  C   . MET   B 61  ? 0.1482 0.1457 0.1567 -0.0130 -0.0117 0.0022  61  MET   B C   
4754 O  O   . MET   B 61  ? 0.1542 0.1435 0.1463 -0.0037 -0.0051 -0.0111 61  MET   B O   
4755 C  CB  . MET   B 61  ? 0.1334 0.1511 0.1679 -0.0014 -0.0089 0.0001  61  MET   B CB  
4756 C  CG  . MET   B 61  ? 0.1355 0.1465 0.1597 0.0001  -0.0150 0.0009  61  MET   B CG  
4757 S  SD  . MET   B 61  ? 0.1401 0.1494 0.1730 -0.0023 -0.0093 -0.0091 61  MET   B SD  
4758 C  CE  . MET   B 61  ? 0.1478 0.1656 0.1978 0.0056  -0.0029 -0.0250 61  MET   B CE  
4768 N  N   . GLN   B 62  ? 0.1449 0.1539 0.1509 -0.0084 -0.0209 0.0007  62  GLN   B N   
4769 C  CA  . GLN   B 62  ? 0.1501 0.1562 0.1592 -0.0002 -0.0240 -0.0030 62  GLN   B CA  
4770 C  C   . GLN   B 62  ? 0.1499 0.1577 0.1599 -0.0016 -0.0251 -0.0075 62  GLN   B C   
4771 O  O   . GLN   B 62  ? 0.1636 0.1597 0.1654 -0.0039 -0.0263 -0.0105 62  GLN   B O   
4772 C  CB  . GLN   B 62  ? 0.1522 0.1616 0.1664 0.0015  -0.0166 0.0012  62  GLN   B CB  
4773 C  CG  . GLN   B 62  ? 0.1596 0.1681 0.1715 0.0001  -0.0233 -0.0047 62  GLN   B CG  
4774 C  CD  . GLN   B 62  ? 0.1592 0.1600 0.1544 0.0040  -0.0275 0.0046  62  GLN   B CD  
4775 O  OE1 . GLN   B 62  ? 0.1611 0.1558 0.1745 0.0033  -0.0308 -0.0089 62  GLN   B OE1 
4776 N  NE2 . GLN   B 62  ? 0.1594 0.1664 0.1629 0.0049  -0.0205 -0.0068 62  GLN   B NE2 
4785 N  N   . VAL   B 63  ? 0.1496 0.1621 0.1894 -0.0085 -0.0260 -0.0095 63  VAL   B N   
4786 C  CA  . VAL   B 63  ? 0.1622 0.1629 0.2060 -0.0127 -0.0362 -0.0045 63  VAL   B CA  
4787 C  C   . VAL   B 63  ? 0.1615 0.1546 0.1823 -0.0194 -0.0357 -0.0107 63  VAL   B C   
4788 O  O   . VAL   B 63  ? 0.1711 0.1567 0.2039 -0.0169 -0.0432 -0.0180 63  VAL   B O   
4789 C  CB  . VAL   B 63  ? 0.1590 0.1800 0.2350 -0.0223 -0.0322 -0.0112 63  VAL   B CB  
4790 C  CG1 . VAL   B 63  ? 0.1686 0.1851 0.2473 -0.0319 -0.0224 -0.0069 63  VAL   B CG1 
4791 C  CG2 . VAL   B 63  ? 0.1564 0.1994 0.2479 -0.0144 -0.0341 -0.0124 63  VAL   B CG2 
4801 N  N   . GLU   B 64  ? 0.1589 0.1481 0.1721 -0.0118 -0.0266 -0.0077 64  GLU   B N   
4802 C  CA  . GLU   B 64  ? 0.1605 0.1422 0.1744 -0.0150 -0.0324 -0.0060 64  GLU   B CA  
4803 C  C   . GLU   B 64  ? 0.1550 0.1393 0.1654 -0.0087 -0.0301 -0.0118 64  GLU   B C   
4804 O  O   . GLU   B 64  ? 0.1679 0.1507 0.1647 -0.0124 -0.0286 -0.0155 64  GLU   B O   
4805 C  CB  . GLU   B 64  ? 0.1621 0.1496 0.1789 -0.0118 -0.0254 -0.0016 64  GLU   B CB  
4806 C  CG  . GLU   B 64  ? 0.1683 0.1542 0.1757 -0.0276 -0.0256 -0.0133 64  GLU   B CG  
4807 C  CD  . GLU   B 64  ? 0.1710 0.1695 0.1769 -0.0335 -0.0309 -0.0088 64  GLU   B CD  
4808 O  OE1 . GLU   B 64  ? 0.1715 0.1850 0.1849 -0.0324 -0.0228 -0.0242 64  GLU   B OE1 
4809 O  OE2 . GLU   B 64  ? 0.1855 0.1813 0.1813 -0.0378 -0.0390 -0.0067 64  GLU   B OE2 
4816 N  N   . SER   B 65  ? 0.1540 0.1366 0.1572 -0.0120 -0.0242 -0.0121 65  SER   B N   
4817 C  CA  . SER   B 65  ? 0.1539 0.1352 0.1602 -0.0024 -0.0256 -0.0119 65  SER   B CA  
4818 C  C   . SER   B 65  ? 0.1560 0.1409 0.1609 -0.0004 -0.0266 -0.0165 65  SER   B C   
4819 O  O   . SER   B 65  ? 0.1586 0.1481 0.1645 -0.0018 -0.0276 -0.0216 65  SER   B O   
4820 C  CB  . SER   B 65  ? 0.1513 0.1439 0.1606 -0.0086 -0.0212 -0.0109 65  SER   B CB  
4821 O  OG  . SER   B 65  ? 0.1602 0.1453 0.1633 -0.0102 -0.0219 -0.0176 65  SER   B OG  
4827 N  N   . ASP   B 66  ? 0.1641 0.1482 0.1579 -0.0032 -0.0296 -0.0182 66  ASP   B N   
4828 C  CA  . ASP   B 66  ? 0.1749 0.1563 0.1536 0.0024  -0.0329 -0.0162 66  ASP   B CA  
4829 C  C   . ASP   B 66  ? 0.1816 0.1576 0.1511 -0.0029 -0.0278 -0.0197 66  ASP   B C   
4830 O  O   . ASP   B 66  ? 0.1810 0.1631 0.1627 0.0044  -0.0294 -0.0227 66  ASP   B O   
4831 C  CB  . ASP   B 66  ? 0.1892 0.1662 0.1768 0.0105  -0.0421 -0.0135 66  ASP   B CB  
4832 C  CG  . ASP   B 66  ? 0.2173 0.1831 0.2091 0.0198  -0.0559 -0.0069 66  ASP   B CG  
4833 O  OD1 . ASP   B 66  ? 0.2383 0.1757 0.2136 0.0174  -0.0553 0.0020  66  ASP   B OD1 
4834 O  OD2 . ASP   B 66  ? 0.2340 0.2038 0.2643 0.0373  -0.0512 -0.0086 66  ASP   B OD2 
4839 N  N   . ASP   B 67  ? 0.1758 0.1531 0.1529 -0.0094 -0.0307 -0.0190 67  ASP   B N   
4840 C  CA  . ASP   B 67  ? 0.1876 0.1480 0.1694 -0.0051 -0.0309 -0.0072 67  ASP   B CA  
4841 C  C   . ASP   B 67  ? 0.1829 0.1501 0.1777 0.0027  -0.0303 -0.0144 67  ASP   B C   
4842 O  O   . ASP   B 67  ? 0.1851 0.1552 0.1856 0.0004  -0.0131 -0.0207 67  ASP   B O   
4843 C  CB  . ASP   B 67  ? 0.2084 0.1588 0.1912 -0.0140 -0.0429 -0.0076 67  ASP   B CB  
4844 C  CG  . ASP   B 67  ? 0.2438 0.1689 0.2001 -0.0101 -0.0659 -0.0114 67  ASP   B CG  
4845 O  OD1 . ASP   B 67  ? 0.2659 0.1750 0.2176 -0.0143 -0.0676 -0.0146 67  ASP   B OD1 
4846 O  OD2 . ASP   B 67  ? 0.2596 0.1734 0.2080 0.0042  -0.0707 -0.0089 67  ASP   B OD2 
4851 N  N   . TYR   B 68  ? 0.1743 0.1512 0.1752 0.0060  -0.0424 -0.0228 68  TYR   B N   
4852 C  CA  . TYR   B 68  ? 0.1718 0.1645 0.1805 0.0079  -0.0431 -0.0275 68  TYR   B CA  
4853 C  C   . TYR   B 68  ? 0.1662 0.1617 0.1755 0.0040  -0.0370 -0.0333 68  TYR   B C   
4854 O  O   . TYR   B 68  ? 0.1727 0.1720 0.1883 0.0113  -0.0322 -0.0454 68  TYR   B O   
4855 C  CB  . TYR   B 68  ? 0.1730 0.1839 0.1879 0.0120  -0.0455 -0.0402 68  TYR   B CB  
4856 C  CG  . TYR   B 68  ? 0.1848 0.1995 0.2052 0.0139  -0.0379 -0.0561 68  TYR   B CG  
4857 C  CD1 . TYR   B 68  ? 0.1891 0.2024 0.2303 -0.0082 -0.0318 -0.0645 68  TYR   B CD1 
4858 C  CD2 . TYR   B 68  ? 0.1856 0.2188 0.2303 0.0207  -0.0468 -0.0474 68  TYR   B CD2 
4859 C  CE1 . TYR   B 68  ? 0.1947 0.2178 0.2552 -0.0046 -0.0274 -0.0639 68  TYR   B CE1 
4860 C  CE2 . TYR   B 68  ? 0.1877 0.2243 0.2361 0.0190  -0.0345 -0.0611 68  TYR   B CE2 
4861 C  CZ  . TYR   B 68  ? 0.1876 0.2255 0.2516 0.0058  -0.0358 -0.0666 68  TYR   B CZ  
4862 O  OH  . TYR   B 68  ? 0.1818 0.2438 0.2789 0.0030  -0.0328 -0.0479 68  TYR   B OH  
4872 N  N   . ILE   B 69  ? 0.1655 0.1539 0.1699 0.0019  -0.0393 -0.0360 69  ILE   B N   
4873 C  CA  . ILE   B 69  ? 0.1759 0.1598 0.1833 -0.0036 -0.0242 -0.0322 69  ILE   B CA  
4874 C  C   . ILE   B 69  ? 0.1728 0.1595 0.1837 0.0027  -0.0347 -0.0268 69  ILE   B C   
4875 O  O   . ILE   B 69  ? 0.1790 0.1668 0.1782 0.0053  -0.0233 -0.0328 69  ILE   B O   
4876 C  CB  . ILE   B 69  ? 0.1846 0.1647 0.2002 -0.0021 -0.0051 -0.0280 69  ILE   B CB  
4877 C  CG1 . ILE   B 69  ? 0.1792 0.1666 0.2146 -0.0027 0.0020  -0.0303 69  ILE   B CG1 
4878 C  CG2 . ILE   B 69  ? 0.2005 0.1715 0.2021 -0.0025 -0.0041 -0.0200 69  ILE   B CG2 
4879 C  CD1 . ILE   B 69  ? 0.1737 0.1743 0.2241 -0.0152 0.0022  -0.0336 69  ILE   B CD1 
4891 N  N   . ALA   B 70  ? 0.1709 0.1592 0.1857 0.0018  -0.0403 -0.0277 70  ALA   B N   
4892 C  CA  . ALA   B 70  ? 0.1707 0.1661 0.1713 -0.0020 -0.0443 -0.0208 70  ALA   B CA  
4893 C  C   . ALA   B 70  ? 0.1755 0.1624 0.1779 -0.0039 -0.0429 -0.0294 70  ALA   B C   
4894 O  O   . ALA   B 70  ? 0.1805 0.1627 0.1883 0.0036  -0.0388 -0.0343 70  ALA   B O   
4895 C  CB  . ALA   B 70  ? 0.1748 0.1799 0.1619 -0.0031 -0.0376 -0.0253 70  ALA   B CB  
4901 N  N   . THR   B 71  ? 0.1851 0.1612 0.1873 0.0025  -0.0541 -0.0319 71  THR   B N   
4902 C  CA  . THR   B 71  ? 0.2028 0.1646 0.2072 0.0097  -0.0693 -0.0315 71  THR   B CA  
4903 C  C   . THR   B 71  ? 0.1981 0.1701 0.2293 0.0280  -0.0654 -0.0457 71  THR   B C   
4904 O  O   . THR   B 71  ? 0.2100 0.1724 0.2647 0.0341  -0.0547 -0.0563 71  THR   B O   
4905 C  CB  . THR   B 71  ? 0.2301 0.1780 0.2370 -0.0017 -0.0780 -0.0110 71  THR   B CB  
4906 O  OG1 . THR   B 71  ? 0.2475 0.2094 0.2766 -0.0196 -0.0779 0.0098  71  THR   B OG1 
4907 C  CG2 . THR   B 71  ? 0.2488 0.1746 0.2699 0.0043  -0.0665 0.0027  71  THR   B CG2 
4915 N  N   . ASN   B 72  ? 0.1819 0.1804 0.2167 0.0210  -0.0641 -0.0686 72  ASN   B N   
4916 C  CA  . ASN   B 72  ? 0.1808 0.1911 0.2306 0.0222  -0.0478 -0.0738 72  ASN   B CA  
4917 C  C   . ASN   B 72  ? 0.1809 0.1993 0.2398 0.0038  -0.0246 -0.0710 72  ASN   B C   
4918 O  O   . ASN   B 72  ? 0.1827 0.2136 0.2649 0.0079  -0.0074 -0.0720 72  ASN   B O   
4919 C  CB  . ASN   B 72  ? 0.1905 0.2066 0.2397 0.0187  -0.0657 -0.0647 72  ASN   B CB  
4920 C  CG  . ASN   B 72  ? 0.2055 0.2186 0.2496 0.0321  -0.0616 -0.0376 72  ASN   B CG  
4921 O  OD1 . ASN   B 72  ? 0.2259 0.2362 0.2424 0.0191  -0.0443 -0.0391 72  ASN   B OD1 
4922 N  ND2 . ASN   B 72  ? 0.2183 0.2225 0.2911 0.0514  -0.0519 -0.0063 72  ASN   B ND2 
4929 N  N   . GLY   B 73  ? 0.1821 0.1946 0.2183 -0.0041 -0.0260 -0.0683 73  GLY   B N   
4930 C  CA  . GLY   B 73  ? 0.1766 0.2034 0.1942 -0.0084 -0.0240 -0.0519 73  GLY   B CA  
4931 C  C   . GLY   B 73  ? 0.1747 0.2011 0.1523 0.0040  -0.0264 -0.0490 73  GLY   B C   
4932 O  O   . GLY   B 73  ? 0.1692 0.1874 0.1675 0.0090  -0.0185 -0.0303 73  GLY   B O   
4936 N  N   . PRO   B 74  ? 0.1774 0.2109 0.1521 0.0047  -0.0262 -0.0363 74  PRO   B N   
4937 C  CA  . PRO   B 74  ? 0.1706 0.2080 0.1350 0.0069  -0.0185 -0.0226 74  PRO   B CA  
4938 C  C   . PRO   B 74  ? 0.1588 0.1945 0.1400 0.0081  -0.0107 -0.0156 74  PRO   B C   
4939 O  O   . PRO   B 74  ? 0.1613 0.1959 0.1846 0.0091  -0.0047 -0.0242 74  PRO   B O   
4940 C  CB  . PRO   B 74  ? 0.1827 0.2244 0.1461 0.0024  -0.0200 -0.0120 74  PRO   B CB  
4941 C  CG  . PRO   B 74  ? 0.2009 0.2347 0.1703 0.0030  -0.0166 -0.0106 74  PRO   B CG  
4942 C  CD  . PRO   B 74  ? 0.1986 0.2251 0.1635 0.0062  -0.0147 -0.0262 74  PRO   B CD  
4950 N  N   . LEU   B 75  ? 0.1557 0.1831 0.1267 0.0084  -0.0175 -0.0166 75  LEU   B N   
4951 C  CA  . LEU   B 75  ? 0.1625 0.1839 0.1277 0.0054  -0.0177 -0.0046 75  LEU   B CA  
4952 C  C   . LEU   B 75  ? 0.1643 0.1972 0.1306 0.0075  -0.0074 -0.0064 75  LEU   B C   
4953 O  O   . LEU   B 75  ? 0.1772 0.2100 0.1445 0.0002  -0.0079 0.0043  75  LEU   B O   
4954 C  CB  . LEU   B 75  ? 0.1738 0.1900 0.1180 -0.0075 -0.0192 0.0103  75  LEU   B CB  
4955 C  CG  . LEU   B 75  ? 0.2036 0.2011 0.1376 -0.0246 -0.0073 0.0083  75  LEU   B CG  
4956 C  CD1 . LEU   B 75  ? 0.2330 0.2166 0.1443 -0.0333 0.0108  0.0033  75  LEU   B CD1 
4957 C  CD2 . LEU   B 75  ? 0.2362 0.2189 0.2081 -0.0201 0.0070  0.0170  75  LEU   B CD2 
4969 N  N   . LYS   B 76  ? 0.1644 0.2168 0.1624 0.0072  0.0027  0.0041  76  LYS   B N   
4970 C  CA  . LYS   B 76  ? 0.1784 0.2246 0.1998 -0.0038 0.0212  0.0014  76  LYS   B CA  
4971 C  C   . LYS   B 76  ? 0.1694 0.2085 0.1694 -0.0012 0.0124  0.0218  76  LYS   B C   
4972 O  O   . LYS   B 76  ? 0.1704 0.1891 0.1748 -0.0026 0.0053  0.0172  76  LYS   B O   
4973 C  CB  . LYS   B 76  ? 0.1943 0.2299 0.2551 -0.0105 0.0401  -0.0297 76  LYS   B CB  
4974 C  CG  . LYS   B 76  ? 0.2029 0.2459 0.2924 -0.0026 0.0309  -0.0369 76  LYS   B CG  
4975 C  CD  . LYS   B 76  ? 0.2044 0.2547 0.3274 0.0053  0.0222  -0.0501 76  LYS   B CD  
4976 C  CE  . LYS   B 76  ? 0.2117 0.2682 0.3764 0.0048  0.0068  -0.0565 76  LYS   B CE  
4977 N  NZ  . LYS   B 76  ? 0.2164 0.2740 0.3897 0.0030  -0.0144 -0.0725 76  LYS   B NZ  
4991 N  N   . VAL   B 77  ? 0.1804 0.2208 0.1687 0.0073  0.0133  0.0305  77  VAL   B N   
4992 C  CA  . VAL   B 77  ? 0.1814 0.2110 0.1785 0.0114  0.0174  0.0501  77  VAL   B CA  
4993 C  C   . VAL   B 77  ? 0.1672 0.1859 0.1708 0.0135  0.0222  0.0371  77  VAL   B C   
4994 O  O   . VAL   B 77  ? 0.1694 0.1831 0.1749 0.0245  0.0270  0.0304  77  VAL   B O   
4995 C  CB  . VAL   B 77  ? 0.1904 0.2208 0.2118 0.0101  0.0273  0.0662  77  VAL   B CB  
4996 C  CG1 . VAL   B 77  ? 0.1921 0.2166 0.2406 0.0029  0.0288  0.0779  77  VAL   B CG1 
4997 C  CG2 . VAL   B 77  ? 0.2070 0.2347 0.2305 0.0054  0.0058  0.0719  77  VAL   B CG2 
5007 N  N   . GLY   B 78  ? 0.1625 0.1708 0.1696 0.0080  0.0208  0.0323  78  GLY   B N   
5008 C  CA  . GLY   B 78  ? 0.1587 0.1639 0.1666 0.0068  0.0250  0.0212  78  GLY   B CA  
5009 C  C   . GLY   B 78  ? 0.1545 0.1576 0.1579 0.0083  0.0192  0.0175  78  GLY   B C   
5010 O  O   . GLY   B 78  ? 0.1529 0.1542 0.1789 0.0182  0.0160  0.0216  78  GLY   B O   
5014 N  N   . GLY   B 79  ? 0.1530 0.1615 0.1531 0.0083  0.0136  0.0162  79  GLY   B N   
5015 C  CA  . GLY   B 79  ? 0.1511 0.1529 0.1411 0.0150  0.0014  0.0115  79  GLY   B CA  
5016 C  C   . GLY   B 79  ? 0.1417 0.1457 0.1476 0.0117  0.0069  0.0047  79  GLY   B C   
5017 O  O   . GLY   B 79  ? 0.1482 0.1431 0.1589 0.0095  0.0155  0.0132  79  GLY   B O   
5021 N  N   . SER   B 80  ? 0.1405 0.1369 0.1643 0.0036  0.0175  0.0030  80  SER   B N   
5022 C  CA  . SER   B 80  ? 0.1331 0.1402 0.1614 0.0001  0.0043  0.0072  80  SER   B CA  
5023 C  C   . SER   B 80  ? 0.1378 0.1355 0.1552 0.0072  -0.0024 0.0025  80  SER   B C   
5024 O  O   . SER   B 80  ? 0.1474 0.1403 0.1849 0.0071  0.0078  0.0025  80  SER   B O   
5025 C  CB  . SER   B 80  ? 0.1374 0.1477 0.1637 0.0003  0.0018  0.0053  80  SER   B CB  
5026 O  OG  . SER   B 80  ? 0.1461 0.1584 0.1781 -0.0005 -0.0105 0.0080  80  SER   B OG  
5032 N  N   . CYS   B 81  ? 0.1388 0.1218 0.1558 0.0015  -0.0055 0.0003  81  CYS   B N   
5033 C  CA  . CYS   B 81  ? 0.1444 0.1240 0.1558 0.0048  -0.0155 0.0009  81  CYS   B CA  
5034 C  C   . CYS   B 81  ? 0.1407 0.1248 0.1414 -0.0004 -0.0150 0.0002  81  CYS   B C   
5035 O  O   . CYS   B 81  ? 0.1587 0.1245 0.1534 0.0078  -0.0047 -0.0055 81  CYS   B O   
5036 C  CB  . CYS   B 81  ? 0.1592 0.1356 0.1602 -0.0016 -0.0140 0.0016  81  CYS   B CB  
5037 S  SG  . CYS   B 81  ? 0.1584 0.1559 0.1548 -0.0031 -0.0260 -0.0076 81  CYS   B SG  
5043 N  N   . VAL   B 82  ? 0.1437 0.1226 0.1469 -0.0040 -0.0163 -0.0018 82  VAL   B N   
5044 C  CA  . VAL   B 82  ? 0.1534 0.1253 0.1441 -0.0096 -0.0108 0.0070  82  VAL   B CA  
5045 C  C   . VAL   B 82  ? 0.1560 0.1172 0.1520 -0.0026 -0.0044 -0.0007 82  VAL   B C   
5046 O  O   . VAL   B 82  ? 0.1614 0.1186 0.1874 -0.0061 -0.0090 -0.0131 82  VAL   B O   
5047 C  CB  . VAL   B 82  ? 0.1583 0.1453 0.1633 -0.0071 -0.0181 0.0074  82  VAL   B CB  
5048 C  CG1 . VAL   B 82  ? 0.1787 0.1718 0.1685 0.0005  -0.0198 0.0186  82  VAL   B CG1 
5049 C  CG2 . VAL   B 82  ? 0.1634 0.1574 0.1824 -0.0075 -0.0245 0.0145  82  VAL   B CG2 
5059 N  N   . LEU   B 83  ? 0.1448 0.1159 0.1536 -0.0152 -0.0201 -0.0056 83  LEU   B N   
5060 C  CA  . LEU   B 83  ? 0.1469 0.1223 0.1452 -0.0156 -0.0195 -0.0047 83  LEU   B CA  
5061 C  C   . LEU   B 83  ? 0.1484 0.1221 0.1446 -0.0155 -0.0204 0.0001  83  LEU   B C   
5062 O  O   . LEU   B 83  ? 0.1446 0.1307 0.1413 -0.0193 -0.0129 0.0043  83  LEU   B O   
5063 C  CB  . LEU   B 83  ? 0.1505 0.1353 0.1451 -0.0160 -0.0220 -0.0101 83  LEU   B CB  
5064 C  CG  . LEU   B 83  ? 0.1664 0.1583 0.1518 -0.0226 -0.0183 -0.0054 83  LEU   B CG  
5065 C  CD1 . LEU   B 83  ? 0.1777 0.1655 0.1602 -0.0133 -0.0239 -0.0047 83  LEU   B CD1 
5066 C  CD2 . LEU   B 83  ? 0.1871 0.1613 0.1621 -0.0140 -0.0212 -0.0149 83  LEU   B CD2 
5078 N  N   . SER   B 84  ? 0.1549 0.1285 0.1671 -0.0245 -0.0203 0.0004  84  SER   B N   
5079 C  CA  . SER   B 84  ? 0.1511 0.1536 0.1540 -0.0271 -0.0149 0.0105  84  SER   B CA  
5080 C  C   . SER   B 84  ? 0.1424 0.1678 0.1186 -0.0180 -0.0197 0.0215  84  SER   B C   
5081 O  O   . SER   B 84  ? 0.1481 0.1580 0.1255 -0.0199 -0.0153 0.0049  84  SER   B O   
5082 C  CB  . SER   B 84  ? 0.1687 0.1616 0.1998 -0.0284 0.0035  0.0110  84  SER   B CB  
5083 O  OG  . SER   B 84  ? 0.1647 0.1771 0.2305 -0.0397 0.0039  0.0229  84  SER   B OG  
5089 N  N   . GLY   B 85  ? 0.1445 0.1901 0.1398 -0.0232 -0.0176 0.0262  85  GLY   B N   
5090 C  CA  . GLY   B 85  ? 0.1437 0.1985 0.1606 -0.0343 -0.0026 -0.0036 85  GLY   B CA  
5091 C  C   . GLY   B 85  ? 0.1478 0.1816 0.1406 -0.0396 -0.0064 0.0019  85  GLY   B C   
5092 O  O   . GLY   B 85  ? 0.1561 0.1762 0.1548 -0.0487 0.0133  -0.0092 85  GLY   B O   
5096 N  N   . HIS   B 86  ? 0.1470 0.1659 0.1598 -0.0312 -0.0175 0.0123  86  HIS   B N   
5097 C  CA  . HIS   B 86  ? 0.1464 0.1654 0.1533 -0.0323 -0.0162 0.0137  86  HIS   B CA  
5098 C  C   . HIS   B 86  ? 0.1465 0.1793 0.1419 -0.0439 -0.0099 0.0313  86  HIS   B C   
5099 O  O   . HIS   B 86  ? 0.1623 0.1962 0.1486 -0.0328 0.0045  0.0275  86  HIS   B O   
5100 C  CB  . HIS   B 86  ? 0.1560 0.1693 0.1560 -0.0248 -0.0252 0.0037  86  HIS   B CB  
5101 C  CG  . HIS   B 86  ? 0.1577 0.1740 0.1551 -0.0198 -0.0237 0.0147  86  HIS   B CG  
5102 N  ND1 . HIS   B 86  ? 0.1707 0.1939 0.1764 -0.0264 -0.0275 -0.0020 86  HIS   B ND1 
5103 C  CD2 . HIS   B 86  ? 0.1613 0.1791 0.1569 -0.0128 -0.0204 0.0141  86  HIS   B CD2 
5104 C  CE1 . HIS   B 86  ? 0.1761 0.1928 0.1597 -0.0184 -0.0111 -0.0171 86  HIS   B CE1 
5105 N  NE2 . HIS   B 86  ? 0.1669 0.1879 0.1559 -0.0045 -0.0137 0.0007  86  HIS   B NE2 
5113 N  N   . ASN   B 87  ? 0.1509 0.1796 0.1575 -0.0373 -0.0050 0.0229  87  ASN   B N   
5114 C  CA  . ASN   B 87  ? 0.1593 0.1944 0.1579 -0.0344 0.0185  0.0183  87  ASN   B CA  
5115 C  C   . ASN   B 87  ? 0.1754 0.1803 0.1516 -0.0321 0.0327  0.0137  87  ASN   B C   
5116 O  O   . ASN   B 87  ? 0.1981 0.1928 0.1895 -0.0262 0.0440  0.0064  87  ASN   B O   
5117 C  CB  . ASN   B 87  ? 0.1631 0.2339 0.1979 -0.0288 0.0228  0.0176  87  ASN   B CB  
5118 C  CG  . ASN   B 87  ? 0.1634 0.2519 0.2028 0.0012  0.0255  0.0310  87  ASN   B CG  
5119 O  OD1 . ASN   B 87  ? 0.1546 0.2388 0.1893 0.0028  0.0416  0.0461  87  ASN   B OD1 
5120 N  ND2 . ASN   B 87  ? 0.1955 0.2628 0.2371 0.0076  0.0280  0.0317  87  ASN   B ND2 
5127 N  N   . LEU   B 88  ? 0.1625 0.1697 0.1447 -0.0360 0.0177  0.0118  88  LEU   B N   
5128 C  CA  . LEU   B 88  ? 0.1708 0.1650 0.1471 -0.0369 0.0045  -0.0021 88  LEU   B CA  
5129 C  C   . LEU   B 88  ? 0.1687 0.1587 0.1487 -0.0360 0.0019  -0.0014 88  LEU   B C   
5130 O  O   . LEU   B 88  ? 0.1970 0.1652 0.1725 -0.0237 -0.0218 -0.0048 88  LEU   B O   
5131 C  CB  . LEU   B 88  ? 0.1822 0.1689 0.1658 -0.0403 -0.0057 0.0122  88  LEU   B CB  
5132 C  CG  . LEU   B 88  ? 0.2212 0.1979 0.1908 -0.0323 -0.0201 0.0303  88  LEU   B CG  
5133 C  CD1 . LEU   B 88  ? 0.2331 0.2272 0.2052 -0.0407 -0.0188 0.0418  88  LEU   B CD1 
5134 C  CD2 . LEU   B 88  ? 0.2550 0.2206 0.2449 0.0056  -0.0420 0.0096  88  LEU   B CD2 
5146 N  N   . ALA   B 89  ? 0.1573 0.1537 0.1335 -0.0364 0.0177  -0.0006 89  ALA   B N   
5147 C  CA  . ALA   B 89  ? 0.1555 0.1489 0.1169 -0.0398 0.0012  0.0101  89  ALA   B CA  
5148 C  C   . ALA   B 89  ? 0.1645 0.1518 0.1329 -0.0426 0.0080  0.0040  89  ALA   B C   
5149 O  O   . ALA   B 89  ? 0.1511 0.1568 0.1707 -0.0405 0.0123  -0.0235 89  ALA   B O   
5150 C  CB  . ALA   B 89  ? 0.1471 0.1532 0.1394 -0.0403 0.0006  0.0183  89  ALA   B CB  
5156 N  N   . LYS   B 90  ? 0.1964 0.1404 0.1439 -0.0478 -0.0084 0.0091  90  LYS   B N   
5157 C  CA  . LYS   B 90  ? 0.2105 0.1403 0.1288 -0.0459 -0.0099 0.0098  90  LYS   B CA  
5158 C  C   . LYS   B 90  ? 0.1894 0.1337 0.1421 -0.0458 -0.0084 0.0027  90  LYS   B C   
5159 O  O   . LYS   B 90  ? 0.1959 0.1457 0.1610 -0.0566 0.0046  -0.0004 90  LYS   B O   
5160 C  CB  . LYS   B 90  ? 0.2274 0.1496 0.1676 -0.0381 -0.0052 0.0161  90  LYS   B CB  
5161 C  CG  . LYS   B 90  ? 0.2289 0.1588 0.1662 -0.0198 0.0225  0.0226  90  LYS   B CG  
5162 C  CD  . LYS   B 90  ? 0.2507 0.1763 0.2173 -0.0110 0.0385  0.0067  90  LYS   B CD  
5163 C  CE  . LYS   B 90  ? 0.2615 0.1932 0.2658 -0.0155 0.0475  -0.0020 90  LYS   B CE  
5164 N  NZ  . LYS   B 90  ? 0.2700 0.1862 0.2634 -0.0284 0.0654  -0.0031 90  LYS   B NZ  
5178 N  N   . HIS   B 91  ? 0.1635 0.1241 0.1272 -0.0333 -0.0121 0.0093  91  HIS   B N   
5179 C  CA  . HIS   B 91  ? 0.1525 0.1259 0.1388 -0.0261 -0.0163 0.0022  91  HIS   B CA  
5180 C  C   . HIS   B 91  ? 0.1447 0.1279 0.1227 -0.0295 -0.0068 0.0090  91  HIS   B C   
5181 O  O   . HIS   B 91  ? 0.1579 0.1309 0.1351 -0.0286 -0.0216 0.0036  91  HIS   B O   
5182 C  CB  . HIS   B 91  ? 0.1757 0.1311 0.1715 -0.0110 -0.0104 0.0132  91  HIS   B CB  
5183 C  CG  . HIS   B 91  ? 0.2147 0.1503 0.2440 -0.0010 0.0148  0.0237  91  HIS   B CG  
5184 N  ND1 . HIS   B 91  ? 0.2413 0.1579 0.2993 0.0009  0.0223  0.0091  91  HIS   B ND1 
5185 C  CD2 . HIS   B 91  ? 0.2273 0.1765 0.2895 0.0146  0.0036  0.0523  91  HIS   B CD2 
5186 C  CE1 . HIS   B 91  ? 0.2477 0.1709 0.3168 0.0157  0.0249  0.0128  91  HIS   B CE1 
5187 N  NE2 . HIS   B 91  ? 0.2393 0.1824 0.3179 0.0292  0.0179  0.0546  91  HIS   B NE2 
5195 N  N   . CYS   B 92  ? 0.1382 0.1262 0.1239 -0.0261 -0.0153 0.0035  92  CYS   B N   
5196 C  CA  . CYS   B 92  ? 0.1372 0.1242 0.1218 -0.0192 -0.0109 0.0036  92  CYS   B CA  
5197 C  C   . CYS   B 92  ? 0.1355 0.1197 0.1149 -0.0105 -0.0045 0.0018  92  CYS   B C   
5198 O  O   . CYS   B 92  ? 0.1411 0.1272 0.1472 -0.0180 -0.0052 -0.0040 92  CYS   B O   
5199 C  CB  . CYS   B 92  ? 0.1382 0.1315 0.1367 -0.0161 -0.0140 0.0081  92  CYS   B CB  
5200 S  SG  . CYS   B 92  ? 0.1372 0.1334 0.1379 -0.0131 -0.0129 0.0057  92  CYS   B SG  
5206 N  N   . LEU   B 93  ? 0.1243 0.1242 0.1241 -0.0128 -0.0097 -0.0019 93  LEU   B N   
5207 C  CA  . LEU   B 93  ? 0.1287 0.1233 0.1241 -0.0059 -0.0136 0.0066  93  LEU   B CA  
5208 C  C   . LEU   B 93  ? 0.1238 0.1191 0.1173 -0.0083 -0.0092 0.0087  93  LEU   B C   
5209 O  O   . LEU   B 93  ? 0.1318 0.1194 0.1381 -0.0085 -0.0086 0.0013  93  LEU   B O   
5210 C  CB  . LEU   B 93  ? 0.1319 0.1241 0.1379 0.0000  -0.0130 0.0043  93  LEU   B CB  
5211 C  CG  . LEU   B 93  ? 0.1280 0.1322 0.1594 -0.0045 -0.0104 0.0106  93  LEU   B CG  
5212 C  CD1 . LEU   B 93  ? 0.1340 0.1392 0.1664 0.0067  -0.0059 0.0032  93  LEU   B CD1 
5213 C  CD2 . LEU   B 93  ? 0.1279 0.1342 0.1678 -0.0043 -0.0109 0.0072  93  LEU   B CD2 
5225 N  N   . HIS   B 94  ? 0.1333 0.1151 0.1138 -0.0061 -0.0092 0.0063  94  HIS   B N   
5226 C  CA  . HIS   B 94  ? 0.1329 0.1151 0.1201 -0.0035 -0.0075 0.0026  94  HIS   B CA  
5227 C  C   . HIS   B 94  ? 0.1280 0.1179 0.1355 -0.0029 -0.0061 0.0076  94  HIS   B C   
5228 O  O   . HIS   B 94  ? 0.1303 0.1303 0.1784 -0.0081 0.0138  -0.0082 94  HIS   B O   
5229 C  CB  . HIS   B 94  ? 0.1288 0.1241 0.1342 0.0015  -0.0122 0.0038  94  HIS   B CB  
5230 C  CG  . HIS   B 94  ? 0.1326 0.1212 0.1356 -0.0040 -0.0237 0.0049  94  HIS   B CG  
5231 N  ND1 . HIS   B 94  ? 0.1374 0.1253 0.1426 -0.0048 -0.0219 0.0017  94  HIS   B ND1 
5232 C  CD2 . HIS   B 94  ? 0.1382 0.1285 0.1406 -0.0002 -0.0134 0.0055  94  HIS   B CD2 
5233 C  CE1 . HIS   B 94  ? 0.1381 0.1281 0.1308 -0.0075 -0.0243 0.0023  94  HIS   B CE1 
5234 N  NE2 . HIS   B 94  ? 0.1313 0.1324 0.1426 -0.0141 -0.0185 0.0006  94  HIS   B NE2 
5242 N  N   . VAL   B 95  ? 0.1181 0.1183 0.1432 -0.0006 -0.0016 0.0067  95  VAL   B N   
5243 C  CA  . VAL   B 95  ? 0.1217 0.1228 0.1357 0.0032  0.0000  0.0121  95  VAL   B CA  
5244 C  C   . VAL   B 95  ? 0.1322 0.1254 0.1376 -0.0002 0.0082  0.0090  95  VAL   B C   
5245 O  O   . VAL   B 95  ? 0.1384 0.1221 0.1590 0.0076  -0.0002 0.0131  95  VAL   B O   
5246 C  CB  . VAL   B 95  ? 0.1311 0.1249 0.1426 -0.0034 -0.0087 0.0082  95  VAL   B CB  
5247 C  CG1 . VAL   B 95  ? 0.1363 0.1410 0.1699 -0.0090 -0.0061 0.0172  95  VAL   B CG1 
5248 C  CG2 . VAL   B 95  ? 0.1394 0.1234 0.1359 0.0039  -0.0076 0.0085  95  VAL   B CG2 
5258 N  N   . VAL   B 96  ? 0.1428 0.1334 0.1350 0.0072  0.0045  0.0172  96  VAL   B N   
5259 C  CA  . VAL   B 96  ? 0.1513 0.1457 0.1342 0.0075  0.0041  0.0205  96  VAL   B CA  
5260 C  C   . VAL   B 96  ? 0.1549 0.1446 0.1492 0.0062  0.0129  0.0227  96  VAL   B C   
5261 O  O   . VAL   B 96  ? 0.1563 0.1472 0.1732 0.0056  0.0218  0.0109  96  VAL   B O   
5262 C  CB  . VAL   B 96  ? 0.1602 0.1631 0.1399 0.0074  0.0025  0.0156  96  VAL   B CB  
5263 C  CG1 . VAL   B 96  ? 0.1612 0.1782 0.1538 0.0197  0.0027  0.0134  96  VAL   B CG1 
5264 C  CG2 . VAL   B 96  ? 0.1673 0.1672 0.1524 0.0053  0.0113  0.0092  96  VAL   B CG2 
5274 N  N   . GLY   B 97  ? 0.1577 0.1453 0.1488 0.0028  0.0056  0.0271  97  GLY   B N   
5275 C  CA  . GLY   B 97  ? 0.1771 0.1516 0.1529 0.0031  0.0086  0.0240  97  GLY   B CA  
5276 C  C   . GLY   B 97  ? 0.1978 0.1604 0.1649 0.0117  0.0079  0.0207  97  GLY   B C   
5277 O  O   . GLY   B 97  ? 0.2130 0.1682 0.1581 0.0057  0.0007  0.0170  97  GLY   B O   
5281 N  N   . PRO   B 98  ? 0.2136 0.1656 0.1799 0.0116  0.0362  0.0359  98  PRO   B N   
5282 C  CA  . PRO   B 98  ? 0.2276 0.1816 0.1846 0.0235  0.0519  0.0318  98  PRO   B CA  
5283 C  C   . PRO   B 98  ? 0.2408 0.1808 0.1664 0.0372  0.0536  0.0527  98  PRO   B C   
5284 O  O   . PRO   B 98  ? 0.2316 0.1775 0.1857 0.0341  0.0519  0.0496  98  PRO   B O   
5285 C  CB  . PRO   B 98  ? 0.2175 0.1866 0.2002 0.0186  0.0606  0.0346  98  PRO   B CB  
5286 C  CG  . PRO   B 98  ? 0.2137 0.1788 0.1990 0.0138  0.0512  0.0466  98  PRO   B CG  
5287 C  CD  . PRO   B 98  ? 0.2019 0.1692 0.1952 0.0134  0.0405  0.0435  98  PRO   B CD  
5295 N  N   . ASN   B 99  ? 0.2502 0.2004 0.1771 0.0559  0.0531  0.0312  99  ASN   B N   
5296 C  CA  . ASN   B 99  ? 0.2711 0.2150 0.1801 0.0593  0.0463  0.0548  99  ASN   B CA  
5297 C  C   . ASN   B 99  ? 0.2982 0.2516 0.2150 0.0573  0.0588  0.0841  99  ASN   B C   
5298 O  O   . ASN   B 99  ? 0.3069 0.2623 0.2179 0.0598  0.0481  0.0893  99  ASN   B O   
5299 C  CB  . ASN   B 99  ? 0.2809 0.2139 0.1818 0.0615  0.0381  0.0497  99  ASN   B CB  
5300 C  CG  . ASN   B 99  ? 0.2883 0.2201 0.2029 0.0599  0.0275  0.0446  99  ASN   B CG  
5301 O  OD1 . ASN   B 99  ? 0.2892 0.2193 0.2287 0.0628  0.0326  0.0576  99  ASN   B OD1 
5302 N  ND2 . ASN   B 99  ? 0.2878 0.2188 0.2067 0.0659  0.0015  0.0400  99  ASN   B ND2 
5309 N  N   A VAL   B 100 ? 0.3138 0.2610 0.2622 0.0478  0.0644  0.1050  100 VAL   B N   
5310 N  N   B VAL   B 100 ? 0.3188 0.2638 0.2568 0.0500  0.0508  0.0950  100 VAL   B N   
5311 C  CA  A VAL   B 100 ? 0.3395 0.2768 0.3124 0.0346  0.0632  0.1209  100 VAL   B CA  
5312 C  CA  B VAL   B 100 ? 0.3430 0.2777 0.2958 0.0415  0.0419  0.1036  100 VAL   B CA  
5313 C  C   A VAL   B 100 ? 0.3607 0.2814 0.3013 0.0398  0.0597  0.1369  100 VAL   B C   
5314 C  C   B VAL   B 100 ? 0.3617 0.2829 0.2964 0.0437  0.0427  0.1240  100 VAL   B C   
5315 O  O   A VAL   B 100 ? 0.3685 0.2908 0.3067 0.0372  0.0696  0.1310  100 VAL   B O   
5316 O  O   B VAL   B 100 ? 0.3659 0.2880 0.2983 0.0417  0.0442  0.1206  100 VAL   B O   
5317 C  CB  A VAL   B 100 ? 0.3473 0.2906 0.3700 0.0107  0.0652  0.1286  100 VAL   B CB  
5318 C  CB  B VAL   B 100 ? 0.3491 0.2868 0.3311 0.0295  0.0345  0.0954  100 VAL   B CB  
5319 C  CG1 A VAL   B 100 ? 0.3532 0.2975 0.3959 0.0080  0.0629  0.1254  100 VAL   B CG1 
5320 C  CG1 B VAL   B 100 ? 0.3522 0.2904 0.3444 0.0272  0.0321  0.0921  100 VAL   B CG1 
5321 C  CG2 A VAL   B 100 ? 0.3464 0.2920 0.3797 -0.0006 0.0724  0.1413  100 VAL   B CG2 
5322 C  CG2 B VAL   B 100 ? 0.3503 0.2893 0.3415 0.0250  0.0330  0.0947  100 VAL   B CG2 
5341 N  N   . ASN   B 101 ? 0.3757 0.2848 0.2967 0.0488  0.0448  0.1420  101 ASN   B N   
5342 C  CA  . ASN   B 101 ? 0.4119 0.3029 0.3128 0.0557  0.0245  0.1438  101 ASN   B CA  
5343 C  C   . ASN   B 101 ? 0.4536 0.3408 0.3245 0.0539  0.0139  0.1498  101 ASN   B C   
5344 O  O   . ASN   B 101 ? 0.4590 0.3544 0.3475 0.0573  0.0179  0.1241  101 ASN   B O   
5345 C  CB  . ASN   B 101 ? 0.4087 0.2896 0.3234 0.0529  0.0265  0.1260  101 ASN   B CB  
5346 C  CG  . ASN   B 101 ? 0.4047 0.2743 0.3267 0.0542  0.0242  0.1230  101 ASN   B CG  
5347 O  OD1 . ASN   B 101 ? 0.4059 0.2725 0.3530 0.0463  0.0383  0.1133  101 ASN   B OD1 
5348 N  ND2 . ASN   B 101 ? 0.4005 0.2689 0.3213 0.0585  0.0178  0.1127  101 ASN   B ND2 
5356 N  N   . LYS   B 102 ? 0.4866 0.3730 0.3507 0.0432  0.0153  0.1459  102 LYS   B N   
5357 C  CA  . LYS   B 102 ? 0.5165 0.4129 0.3832 0.0298  0.0225  0.1204  102 LYS   B CA  
5358 C  C   . LYS   B 102 ? 0.5143 0.4156 0.3689 0.0292  0.0278  0.1288  102 LYS   B C   
5359 O  O   . LYS   B 102 ? 0.5232 0.4197 0.3779 0.0297  0.0158  0.1309  102 LYS   B O   
5360 C  CB  . LYS   B 102 ? 0.5441 0.4461 0.4423 0.0183  0.0324  0.0771  102 LYS   B CB  
5361 C  CG  . LYS   B 102 ? 0.5676 0.4754 0.5028 0.0087  0.0428  0.0339  102 LYS   B CG  
5362 C  CD  . LYS   B 102 ? 0.5876 0.4989 0.5649 0.0017  0.0536  -0.0011 102 LYS   B CD  
5363 C  CE  . LYS   B 102 ? 0.6013 0.5147 0.6115 -0.0039 0.0613  -0.0258 102 LYS   B CE  
5364 N  NZ  . LYS   B 102 ? 0.6089 0.5244 0.6400 -0.0067 0.0639  -0.0389 102 LYS   B NZ  
5378 N  N   . GLY   B 103 ? 0.4990 0.4109 0.3665 0.0275  0.0460  0.1230  103 GLY   B N   
5379 C  CA  . GLY   B 103 ? 0.4802 0.4039 0.3748 0.0274  0.0624  0.1032  103 GLY   B CA  
5380 C  C   . GLY   B 103 ? 0.4578 0.3930 0.3695 0.0269  0.0776  0.0835  103 GLY   B C   
5381 O  O   . GLY   B 103 ? 0.4629 0.3982 0.3764 0.0257  0.0819  0.0845  103 GLY   B O   
5385 N  N   A GLU   B 104 ? 0.4427 0.3813 0.3522 0.0312  0.0942  0.0718  104 GLU   B N   
5386 N  N   B GLU   B 104 ? 0.4431 0.3863 0.3660 0.0234  0.0675  0.0676  104 GLU   B N   
5387 C  CA  A GLU   B 104 ? 0.4258 0.3692 0.3334 0.0387  0.1050  0.0570  104 GLU   B CA  
5388 C  CA  B GLU   B 104 ? 0.4268 0.3784 0.3580 0.0207  0.0567  0.0488  104 GLU   B CA  
5389 C  C   A GLU   B 104 ? 0.4274 0.3725 0.3426 0.0208  0.1417  0.0603  104 GLU   B C   
5390 C  C   B GLU   B 104 ? 0.4196 0.3766 0.3661 0.0147  0.0642  0.0412  104 GLU   B C   
5391 O  O   A GLU   B 104 ? 0.4289 0.3764 0.3574 0.0172  0.1431  0.0608  104 GLU   B O   
5392 O  O   B GLU   B 104 ? 0.4201 0.3776 0.3714 0.0137  0.0646  0.0396  104 GLU   B O   
5393 C  CB  A GLU   B 104 ? 0.4105 0.3522 0.3174 0.0632  0.0716  0.0299  104 GLU   B CB  
5394 C  CB  B GLU   B 104 ? 0.4185 0.3710 0.3436 0.0234  0.0380  0.0341  104 GLU   B CB  
5395 C  CG  A GLU   B 104 ? 0.3957 0.3363 0.2950 0.0871  0.0348  0.0011  104 GLU   B CG  
5396 C  CG  B GLU   B 104 ? 0.4115 0.3645 0.3285 0.0260  0.0193  0.0187  104 GLU   B CG  
5397 C  CD  A GLU   B 104 ? 0.3819 0.3211 0.2691 0.1089  0.0002  -0.0159 104 GLU   B CD  
5398 C  CD  B GLU   B 104 ? 0.4062 0.3587 0.3149 0.0278  0.0032  0.0074  104 GLU   B CD  
5399 O  OE1 A GLU   B 104 ? 0.3671 0.3051 0.2347 0.1270  -0.0027 -0.0156 104 GLU   B OE1 
5400 O  OE1 B GLU   B 104 ? 0.4029 0.3546 0.3036 0.0280  0.0017  0.0061  104 GLU   B OE1 
5401 O  OE2 A GLU   B 104 ? 0.3832 0.3257 0.2619 0.1080  -0.0237 -0.0305 104 GLU   B OE2 
5402 O  OE2 B GLU   B 104 ? 0.4056 0.3589 0.3118 0.0286  -0.0075 -0.0001 104 GLU   B OE2 
5415 N  N   A ASP   B 105 ? 0.4234 0.3710 0.3364 0.0083  0.1704  0.0631  105 ASP   B N   
5416 N  N   B ASP   B 105 ? 0.4105 0.3731 0.3639 0.0097  0.0697  0.0356  105 ASP   B N   
5417 C  CA  A ASP   B 105 ? 0.4228 0.3714 0.3552 -0.0021 0.1891  0.0489  105 ASP   B CA  
5418 C  CA  B ASP   B 105 ? 0.4029 0.3695 0.3691 0.0051  0.0731  0.0262  105 ASP   B CA  
5419 C  C   A ASP   B 105 ? 0.4050 0.3461 0.3207 -0.0145 0.1948  0.0473  105 ASP   B C   
5420 C  C   B ASP   B 105 ? 0.3927 0.3596 0.3491 0.0013  0.0738  0.0202  105 ASP   B C   
5421 O  O   A ASP   B 105 ? 0.3897 0.3393 0.3003 -0.0130 0.1924  0.0479  105 ASP   B O   
5422 O  O   B ASP   B 105 ? 0.3915 0.3577 0.3383 0.0014  0.0767  0.0215  105 ASP   B O   
5423 C  CB  A ASP   B 105 ? 0.4377 0.3933 0.4227 0.0027  0.1918  0.0282  105 ASP   B CB  
5424 C  CB  B ASP   B 105 ? 0.4041 0.3747 0.3937 0.0057  0.0752  0.0216  105 ASP   B CB  
5425 C  CG  A ASP   B 105 ? 0.4482 0.4098 0.4858 0.0048  0.1986  0.0135  105 ASP   B CG  
5426 C  CG  B ASP   B 105 ? 0.4048 0.3779 0.4185 0.0050  0.0786  0.0195  105 ASP   B CG  
5427 O  OD1 A ASP   B 105 ? 0.4470 0.4139 0.4937 -0.0001 0.2129  0.0166  105 ASP   B OD1 
5428 O  OD1 B ASP   B 105 ? 0.4042 0.3795 0.4240 0.0028  0.0807  0.0200  105 ASP   B OD1 
5429 O  OD2 A ASP   B 105 ? 0.4549 0.4178 0.5202 0.0112  0.1902  0.0008  105 ASP   B OD2 
5430 O  OD2 B ASP   B 105 ? 0.4044 0.3787 0.4264 0.0052  0.0807  0.0190  105 ASP   B OD2 
5439 N  N   A ILE   B 106 ? 0.3965 0.3246 0.3241 -0.0248 0.1886  0.0469  106 ILE   B N   
5440 N  N   B ILE   B 106 ? 0.3828 0.3505 0.3400 -0.0010 0.0701  0.0150  106 ILE   B N   
5441 C  CA  A ILE   B 106 ? 0.3780 0.2983 0.3334 -0.0403 0.1863  0.0436  106 ILE   B CA  
5442 C  CA  B ILE   B 106 ? 0.3702 0.3409 0.3367 -0.0035 0.0683  0.0093  106 ILE   B CA  
5443 C  C   A ILE   B 106 ? 0.3453 0.2911 0.3251 -0.0344 0.1894  0.0301  106 ILE   B C   
5444 C  C   B ILE   B 106 ? 0.3527 0.3346 0.3338 -0.0013 0.0695  0.0041  106 ILE   B C   
5445 O  O   A ILE   B 106 ? 0.3363 0.2738 0.3261 -0.0344 0.1882  0.0239  106 ILE   B O   
5446 O  O   B ILE   B 106 ? 0.3505 0.3301 0.3308 -0.0026 0.0667  0.0012  106 ILE   B O   
5447 C  CB  A ILE   B 106 ? 0.3956 0.2875 0.3569 -0.0530 0.1728  0.0489  106 ILE   B CB  
5448 C  CB  B ILE   B 106 ? 0.3753 0.3398 0.3391 -0.0073 0.0655  0.0085  106 ILE   B CB  
5449 C  CG1 A ILE   B 106 ? 0.4030 0.2876 0.3646 -0.0461 0.1613  0.0384  106 ILE   B CG1 
5450 C  CG1 B ILE   B 106 ? 0.3767 0.3389 0.3397 -0.0062 0.0621  0.0064  106 ILE   B CG1 
5451 C  CG2 A ILE   B 106 ? 0.4021 0.2874 0.3766 -0.0626 0.1692  0.0550  106 ILE   B CG2 
5452 C  CG2 B ILE   B 106 ? 0.3778 0.3415 0.3447 -0.0096 0.0657  0.0087  106 ILE   B CG2 
5453 C  CD1 A ILE   B 106 ? 0.4062 0.2881 0.3577 -0.0419 0.1598  0.0382  106 ILE   B CD1 
5454 C  CD1 B ILE   B 106 ? 0.3772 0.3383 0.3392 -0.0053 0.0605  0.0059  106 ILE   B CD1 
5477 N  N   A GLN   B 107 ? 0.3287 0.3067 0.3391 -0.0276 0.1762  0.0272  107 GLN   B N   
5478 N  N   B GLN   B 107 ? 0.3386 0.3338 0.3419 0.0009  0.0722  0.0038  107 GLN   B N   
5479 C  CA  A GLN   B 107 ? 0.3099 0.3195 0.3579 -0.0237 0.1536  0.0269  107 GLN   B CA  
5480 C  CA  B GLN   B 107 ? 0.3235 0.3310 0.3510 0.0028  0.0739  0.0070  107 GLN   B CA  
5481 C  C   A GLN   B 107 ? 0.2806 0.2967 0.3269 -0.0104 0.1239  0.0147  107 GLN   B C   
5482 C  C   B GLN   B 107 ? 0.2928 0.3061 0.3189 0.0065  0.0859  0.0076  107 GLN   B C   
5483 O  O   A GLN   B 107 ? 0.2703 0.2935 0.3537 -0.0047 0.1006  -0.0029 107 GLN   B O   
5484 O  O   B GLN   B 107 ? 0.2908 0.3076 0.3256 0.0086  0.0768  0.0008  107 GLN   B O   
5485 C  CB  A GLN   B 107 ? 0.3365 0.3567 0.4277 -0.0240 0.1281  0.0294  107 GLN   B CB  
5486 C  CB  B GLN   B 107 ? 0.3410 0.3520 0.3991 0.0025  0.0599  0.0082  107 GLN   B CB  
5487 C  CG  A GLN   B 107 ? 0.3661 0.3917 0.4968 -0.0195 0.0918  0.0284  107 GLN   B CG  
5488 C  CG  B GLN   B 107 ? 0.3570 0.3703 0.4456 0.0033  0.0441  0.0091  107 GLN   B CG  
5489 C  CD  A GLN   B 107 ? 0.3877 0.4177 0.5518 -0.0195 0.0656  0.0288  107 GLN   B CD  
5490 C  CD  B GLN   B 107 ? 0.3691 0.3841 0.4839 0.0026  0.0321  0.0102  107 GLN   B CD  
5491 O  OE1 A GLN   B 107 ? 0.3952 0.4273 0.5707 -0.0191 0.0604  0.0264  107 GLN   B OE1 
5492 O  OE1 B GLN   B 107 ? 0.3731 0.3891 0.4961 0.0025  0.0297  0.0100  107 GLN   B OE1 
5493 N  NE2 A GLN   B 107 ? 0.3959 0.4255 0.5707 -0.0171 0.0546  0.0315  107 GLN   B NE2 
5494 N  NE2 B GLN   B 107 ? 0.3739 0.3886 0.4976 0.0035  0.0274  0.0112  107 GLN   B NE2 
5511 N  N   . LEU   B 108 ? 0.2620 0.2779 0.2901 0.0126  0.1045  0.0140  108 LEU   B N   
5512 C  CA  . LEU   B 108 ? 0.2343 0.2433 0.2506 0.0285  0.0753  0.0293  108 LEU   B CA  
5513 C  C   . LEU   B 108 ? 0.1945 0.1968 0.2348 0.0292  0.0482  0.0356  108 LEU   B C   
5514 O  O   . LEU   B 108 ? 0.1933 0.1857 0.2214 0.0273  0.0399  0.0305  108 LEU   B O   
5515 C  CB  . LEU   B 108 ? 0.2458 0.2593 0.2411 0.0306  0.0764  0.0384  108 LEU   B CB  
5516 C  CG  . LEU   B 108 ? 0.2589 0.2832 0.2451 0.0312  0.0698  0.0203  108 LEU   B CG  
5517 C  CD1 . LEU   B 108 ? 0.2680 0.2940 0.2363 0.0239  0.0688  0.0192  108 LEU   B CD1 
5518 C  CD2 . LEU   B 108 ? 0.2732 0.2953 0.2580 0.0360  0.0557  0.0040  108 LEU   B CD2 
5531 N  N   . LEU   B 109 ? 0.1761 0.1739 0.2398 0.0156  0.0430  0.0267  109 LEU   B N   
5532 C  CA  . LEU   B 109 ? 0.1560 0.1457 0.2419 0.0084  0.0396  0.0330  109 LEU   B CA  
5533 C  C   . LEU   B 109 ? 0.1462 0.1315 0.2471 0.0010  0.0338  0.0231  109 LEU   B C   
5534 O  O   . LEU   B 109 ? 0.1421 0.1267 0.2444 -0.0014 0.0315  0.0322  109 LEU   B O   
5535 C  CB  . LEU   B 109 ? 0.1642 0.1388 0.2494 0.0073  0.0330  0.0423  109 LEU   B CB  
5536 C  CG  . LEU   B 109 ? 0.1620 0.1351 0.2492 0.0042  0.0256  0.0301  109 LEU   B CG  
5537 C  CD1 . LEU   B 109 ? 0.1592 0.1458 0.2271 0.0122  0.0225  0.0314  109 LEU   B CD1 
5538 C  CD2 . LEU   B 109 ? 0.1704 0.1424 0.2606 0.0054  0.0260  0.0259  109 LEU   B CD2 
5550 N  N   . LYS   B 110 ? 0.1427 0.1347 0.2379 -0.0018 0.0311  0.0258  110 LYS   B N   
5551 C  CA  . LYS   B 110 ? 0.1410 0.1333 0.2293 -0.0027 0.0320  0.0202  110 LYS   B CA  
5552 C  C   . LYS   B 110 ? 0.1367 0.1326 0.2228 -0.0033 0.0299  0.0138  110 LYS   B C   
5553 O  O   . LYS   B 110 ? 0.1278 0.1332 0.2156 -0.0075 0.0194  0.0069  110 LYS   B O   
5554 C  CB  . LYS   B 110 ? 0.1459 0.1294 0.2503 -0.0032 0.0312  0.0200  110 LYS   B CB  
5555 C  CG  . LYS   B 110 ? 0.1424 0.1292 0.2635 -0.0037 0.0205  0.0194  110 LYS   B CG  
5556 C  CD  . LYS   B 110 ? 0.1514 0.1329 0.2720 -0.0119 0.0181  0.0172  110 LYS   B CD  
5557 C  CE  . LYS   B 110 ? 0.1440 0.1506 0.2864 -0.0035 0.0173  0.0057  110 LYS   B CE  
5558 N  NZ  . LYS   B 110 ? 0.1464 0.1686 0.2782 0.0055  0.0051  0.0032  110 LYS   B NZ  
5572 N  N   . SER   B 111 ? 0.1395 0.1355 0.2341 -0.0029 0.0301  0.0195  111 SER   B N   
5573 C  CA  . SER   B 111 ? 0.1472 0.1350 0.2199 -0.0001 0.0238  0.0197  111 SER   B CA  
5574 C  C   . SER   B 111 ? 0.1459 0.1333 0.2122 -0.0012 0.0172  0.0124  111 SER   B C   
5575 O  O   . SER   B 111 ? 0.1386 0.1351 0.2137 -0.0012 0.0142  0.0137  111 SER   B O   
5576 C  CB  . SER   B 111 ? 0.1589 0.1583 0.2292 0.0056  0.0385  0.0304  111 SER   B CB  
5577 O  OG  . SER   B 111 ? 0.1772 0.1923 0.2369 0.0128  0.0444  0.0313  111 SER   B OG  
5583 N  N   . ALA   B 112 ? 0.1345 0.1337 0.2191 0.0076  0.0255  0.0206  112 ALA   B N   
5584 C  CA  . ALA   B 112 ? 0.1328 0.1386 0.1995 0.0017  0.0106  0.0081  112 ALA   B CA  
5585 C  C   . ALA   B 112 ? 0.1217 0.1334 0.1928 0.0005  0.0090  0.0055  112 ALA   B C   
5586 O  O   . ALA   B 112 ? 0.1234 0.1356 0.1997 -0.0089 0.0086  0.0017  112 ALA   B O   
5587 C  CB  . ALA   B 112 ? 0.1389 0.1413 0.2185 0.0049  0.0127  0.0145  112 ALA   B CB  
5593 N  N   . TYR   B 113 ? 0.1210 0.1217 0.2083 -0.0054 0.0142  0.0049  113 TYR   B N   
5594 C  CA  . TYR   B 113 ? 0.1201 0.1182 0.2005 -0.0035 0.0152  -0.0014 113 TYR   B CA  
5595 C  C   . TYR   B 113 ? 0.1196 0.1181 0.1935 -0.0049 0.0112  0.0027  113 TYR   B C   
5596 O  O   . TYR   B 113 ? 0.1266 0.1235 0.1858 -0.0051 0.0072  -0.0028 113 TYR   B O   
5597 C  CB  . TYR   B 113 ? 0.1273 0.1144 0.2105 -0.0032 0.0170  0.0081  113 TYR   B CB  
5598 C  CG  . TYR   B 113 ? 0.1310 0.1199 0.2213 -0.0095 0.0083  0.0114  113 TYR   B CG  
5599 C  CD1 . TYR   B 113 ? 0.1339 0.1231 0.2228 -0.0059 0.0117  0.0206  113 TYR   B CD1 
5600 C  CD2 . TYR   B 113 ? 0.1350 0.1204 0.2199 -0.0073 0.0124  0.0149  113 TYR   B CD2 
5601 C  CE1 . TYR   B 113 ? 0.1350 0.1267 0.2180 -0.0004 0.0150  0.0090  113 TYR   B CE1 
5602 C  CE2 . TYR   B 113 ? 0.1415 0.1152 0.2262 0.0012  0.0092  0.0157  113 TYR   B CE2 
5603 C  CZ  . TYR   B 113 ? 0.1315 0.1193 0.2287 0.0036  0.0084  0.0096  113 TYR   B CZ  
5604 O  OH  . TYR   B 113 ? 0.1400 0.1183 0.2549 0.0073  0.0159  0.0063  113 TYR   B OH  
5614 N  N   . GLU   B 114 ? 0.1149 0.1111 0.2051 -0.0035 0.0134  0.0116  114 GLU   B N   
5615 C  CA  . GLU   B 114 ? 0.1187 0.1148 0.2031 0.0053  0.0031  0.0041  114 GLU   B CA  
5616 C  C   . GLU   B 114 ? 0.1222 0.1158 0.1943 -0.0030 0.0072  0.0053  114 GLU   B C   
5617 O  O   . GLU   B 114 ? 0.1231 0.1156 0.2052 0.0005  0.0005  0.0091  114 GLU   B O   
5618 C  CB  . GLU   B 114 ? 0.1226 0.1234 0.2071 -0.0027 0.0081  0.0062  114 GLU   B CB  
5619 C  CG  . GLU   B 114 ? 0.1281 0.1203 0.2124 -0.0021 0.0129  0.0137  114 GLU   B CG  
5620 C  CD  . GLU   B 114 ? 0.1279 0.1242 0.2158 -0.0043 0.0117  0.0060  114 GLU   B CD  
5621 O  OE1 . GLU   B 114 ? 0.1256 0.1381 0.2159 -0.0075 0.0200  0.0033  114 GLU   B OE1 
5622 O  OE2 . GLU   B 114 ? 0.1286 0.1414 0.2316 -0.0172 0.0129  0.0058  114 GLU   B OE2 
5629 N  N   . ASN   B 115 ? 0.1258 0.1085 0.1917 -0.0040 -0.0056 0.0028  115 ASN   B N   
5630 C  CA  . ASN   B 115 ? 0.1255 0.1170 0.1670 -0.0089 0.0000  0.0105  115 ASN   B CA  
5631 C  C   . ASN   B 115 ? 0.1194 0.1144 0.1665 -0.0098 -0.0042 -0.0013 115 ASN   B C   
5632 O  O   . ASN   B 115 ? 0.1328 0.1177 0.1858 -0.0134 0.0030  0.0059  115 ASN   B O   
5633 C  CB  . ASN   B 115 ? 0.1322 0.1322 0.1744 -0.0162 -0.0004 0.0116  115 ASN   B CB  
5634 C  CG  . ASN   B 115 ? 0.1436 0.1368 0.1748 -0.0041 -0.0012 0.0013  115 ASN   B CG  
5635 O  OD1 . ASN   B 115 ? 0.1819 0.1490 0.2010 -0.0034 0.0111  -0.0148 115 ASN   B OD1 
5636 N  ND2 . ASN   B 115 ? 0.1449 0.1501 0.1728 -0.0058 0.0077  0.0079  115 ASN   B ND2 
5643 N  N   . PHE   B 116 ? 0.1220 0.1166 0.1582 -0.0033 -0.0014 0.0019  116 PHE   B N   
5644 C  CA  . PHE   B 116 ? 0.1300 0.1179 0.1660 -0.0098 -0.0006 0.0034  116 PHE   B CA  
5645 C  C   . PHE   B 116 ? 0.1302 0.1075 0.1684 -0.0103 -0.0042 0.0055  116 PHE   B C   
5646 O  O   . PHE   B 116 ? 0.1294 0.1185 0.1779 -0.0023 -0.0069 0.0105  116 PHE   B O   
5647 C  CB  . PHE   B 116 ? 0.1234 0.1151 0.1632 -0.0099 -0.0130 0.0070  116 PHE   B CB  
5648 C  CG  . PHE   B 116 ? 0.1209 0.1155 0.1670 -0.0076 -0.0026 0.0040  116 PHE   B CG  
5649 C  CD1 . PHE   B 116 ? 0.1282 0.1190 0.1838 -0.0040 -0.0004 0.0039  116 PHE   B CD1 
5650 C  CD2 . PHE   B 116 ? 0.1240 0.1246 0.1662 -0.0060 0.0001  -0.0006 116 PHE   B CD2 
5651 C  CE1 . PHE   B 116 ? 0.1307 0.1240 0.1811 -0.0020 -0.0101 0.0072  116 PHE   B CE1 
5652 C  CE2 . PHE   B 116 ? 0.1275 0.1268 0.1724 -0.0027 -0.0016 0.0045  116 PHE   B CE2 
5653 C  CZ  . PHE   B 116 ? 0.1199 0.1271 0.1777 -0.0042 -0.0132 0.0094  116 PHE   B CZ  
5663 N  N   . ASN   B 117 ? 0.1262 0.1165 0.1868 -0.0056 -0.0063 0.0067  117 ASN   B N   
5664 C  CA  . ASN   B 117 ? 0.1322 0.1187 0.1909 -0.0047 -0.0074 0.0013  117 ASN   B CA  
5665 C  C   . ASN   B 117 ? 0.1328 0.1149 0.2011 -0.0011 -0.0094 0.0030  117 ASN   B C   
5666 O  O   . ASN   B 117 ? 0.1373 0.1241 0.2281 -0.0056 -0.0270 0.0124  117 ASN   B O   
5667 C  CB  . ASN   B 117 ? 0.1286 0.1204 0.1944 -0.0009 -0.0072 -0.0047 117 ASN   B CB  
5668 C  CG  . ASN   B 117 ? 0.1227 0.1218 0.2088 0.0021  -0.0016 -0.0050 117 ASN   B CG  
5669 O  OD1 . ASN   B 117 ? 0.1463 0.1208 0.2222 -0.0099 0.0069  -0.0025 117 ASN   B OD1 
5670 N  ND2 . ASN   B 117 ? 0.1306 0.1250 0.2026 -0.0029 0.0020  0.0003  117 ASN   B ND2 
5677 N  N   . GLN   B 118 ? 0.1291 0.1121 0.1901 -0.0085 -0.0106 0.0002  118 GLN   B N   
5678 C  CA  . GLN   B 118 ? 0.1373 0.1211 0.2026 0.0007  -0.0114 0.0050  118 GLN   B CA  
5679 C  C   . GLN   B 118 ? 0.1402 0.1187 0.2027 -0.0016 -0.0085 -0.0010 118 GLN   B C   
5680 O  O   . GLN   B 118 ? 0.1599 0.1143 0.2388 -0.0089 0.0003  0.0052  118 GLN   B O   
5681 C  CB  . GLN   B 118 ? 0.1409 0.1233 0.2155 -0.0004 -0.0129 0.0044  118 GLN   B CB  
5682 C  CG  . GLN   B 118 ? 0.1503 0.1198 0.2140 0.0037  -0.0019 -0.0028 118 GLN   B CG  
5683 C  CD  . GLN   B 118 ? 0.1560 0.1178 0.2078 -0.0036 -0.0136 -0.0188 118 GLN   B CD  
5684 O  OE1 . GLN   B 118 ? 0.1613 0.1168 0.2297 -0.0027 0.0034  0.0020  118 GLN   B OE1 
5685 N  NE2 . GLN   B 118 ? 0.1656 0.1230 0.2157 -0.0046 -0.0188 -0.0050 118 GLN   B NE2 
5694 N  N   . HIS   B 119 ? 0.1430 0.1201 0.1676 -0.0071 -0.0089 0.0078  119 HIS   B N   
5695 C  CA  . HIS   B 119 ? 0.1573 0.1324 0.1544 -0.0057 -0.0227 0.0064  119 HIS   B CA  
5696 C  C   . HIS   B 119 ? 0.1584 0.1326 0.1568 -0.0052 -0.0277 0.0084  119 HIS   B C   
5697 O  O   . HIS   B 119 ? 0.1619 0.1275 0.1885 -0.0244 -0.0215 0.0095  119 HIS   B O   
5698 C  CB  . HIS   B 119 ? 0.1570 0.1390 0.1743 -0.0061 -0.0225 0.0021  119 HIS   B CB  
5699 C  CG  . HIS   B 119 ? 0.1597 0.1637 0.1897 0.0061  -0.0400 -0.0114 119 HIS   B CG  
5700 N  ND1 . HIS   B 119 ? 0.1707 0.1787 0.2233 0.0037  -0.0449 -0.0261 119 HIS   B ND1 
5701 C  CD2 . HIS   B 119 ? 0.1717 0.1821 0.1941 0.0340  -0.0406 -0.0183 119 HIS   B CD2 
5702 C  CE1 . HIS   B 119 ? 0.1847 0.1953 0.2234 0.0165  -0.0507 -0.0405 119 HIS   B CE1 
5703 N  NE2 . HIS   B 119 ? 0.1838 0.2051 0.2167 0.0312  -0.0424 -0.0313 119 HIS   B NE2 
5711 N  N   . GLU   B 120 ? 0.1758 0.1353 0.1582 -0.0095 -0.0383 0.0158  120 GLU   B N   
5712 C  CA  . GLU   B 120 ? 0.2028 0.1523 0.1768 -0.0046 -0.0482 0.0286  120 GLU   B CA  
5713 C  C   . GLU   B 120 ? 0.1774 0.1392 0.1645 -0.0164 -0.0369 0.0239  120 GLU   B C   
5714 O  O   . GLU   B 120 ? 0.1719 0.1525 0.1709 -0.0167 -0.0391 0.0116  120 GLU   B O   
5715 C  CB  . GLU   B 120 ? 0.2725 0.1932 0.2504 0.0148  -0.0773 0.0539  120 GLU   B CB  
5716 C  CG  . GLU   B 120 ? 0.3398 0.2759 0.3528 0.0294  -0.0967 0.0749  120 GLU   B CG  
5717 C  CD  . GLU   B 120 ? 0.3890 0.3497 0.4512 0.0354  -0.1031 0.0839  120 GLU   B CD  
5718 O  OE1 . GLU   B 120 ? 0.4081 0.3748 0.4850 0.0311  -0.1000 0.0925  120 GLU   B OE1 
5719 O  OE2 . GLU   B 120 ? 0.4075 0.3799 0.4972 0.0388  -0.1037 0.0786  120 GLU   B OE2 
5726 N  N   . VAL   B 121 ? 0.1653 0.1341 0.1663 -0.0249 -0.0219 0.0209  121 VAL   B N   
5727 C  CA  . VAL   B 121 ? 0.1650 0.1459 0.1437 -0.0222 -0.0212 0.0115  121 VAL   B CA  
5728 C  C   . VAL   B 121 ? 0.1523 0.1378 0.1414 -0.0248 -0.0180 0.0140  121 VAL   B C   
5729 O  O   . VAL   B 121 ? 0.1604 0.1364 0.1697 -0.0313 -0.0284 0.0075  121 VAL   B O   
5730 C  CB  . VAL   B 121 ? 0.1898 0.1830 0.1546 -0.0101 -0.0282 0.0213  121 VAL   B CB  
5731 C  CG1 . VAL   B 121 ? 0.1995 0.1962 0.1944 -0.0188 -0.0164 0.0154  121 VAL   B CG1 
5732 C  CG2 . VAL   B 121 ? 0.2128 0.2064 0.1595 -0.0013 -0.0253 0.0098  121 VAL   B CG2 
5742 N  N   . LEU   B 122 ? 0.1478 0.1329 0.1420 -0.0127 -0.0253 0.0057  122 LEU   B N   
5743 C  CA  . LEU   B 122 ? 0.1369 0.1422 0.1351 -0.0179 -0.0205 0.0111  122 LEU   B CA  
5744 C  C   . LEU   B 122 ? 0.1378 0.1308 0.1506 -0.0274 -0.0170 0.0069  122 LEU   B C   
5745 O  O   . LEU   B 122 ? 0.1493 0.1291 0.1777 -0.0291 -0.0260 0.0038  122 LEU   B O   
5746 C  CB  . LEU   B 122 ? 0.1661 0.1477 0.1690 -0.0079 -0.0261 0.0146  122 LEU   B CB  
5747 C  CG  . LEU   B 122 ? 0.1526 0.1553 0.1794 -0.0159 -0.0124 0.0148  122 LEU   B CG  
5748 C  CD1 . LEU   B 122 ? 0.1527 0.1778 0.1879 -0.0245 -0.0189 0.0129  122 LEU   B CD1 
5749 C  CD2 . LEU   B 122 ? 0.1537 0.1551 0.1617 -0.0124 -0.0111 -0.0017 122 LEU   B CD2 
5761 N  N   . LEU   B 123 ? 0.1421 0.1163 0.1396 -0.0238 -0.0147 0.0094  123 LEU   B N   
5762 C  CA  . LEU   B 123 ? 0.1451 0.1190 0.1435 -0.0258 -0.0183 -0.0003 123 LEU   B CA  
5763 C  C   . LEU   B 123 ? 0.1401 0.1173 0.1368 -0.0263 -0.0187 -0.0010 123 LEU   B C   
5764 O  O   . LEU   B 123 ? 0.1478 0.1235 0.1439 -0.0316 -0.0152 0.0005  123 LEU   B O   
5765 C  CB  . LEU   B 123 ? 0.1498 0.1232 0.1509 -0.0275 -0.0176 0.0030  123 LEU   B CB  
5766 C  CG  . LEU   B 123 ? 0.1492 0.1347 0.1503 -0.0184 -0.0077 0.0106  123 LEU   B CG  
5767 C  CD1 . LEU   B 123 ? 0.1594 0.1338 0.1670 -0.0190 0.0037  -0.0095 123 LEU   B CD1 
5768 C  CD2 . LEU   B 123 ? 0.1528 0.1458 0.1688 -0.0150 -0.0036 0.0247  123 LEU   B CD2 
5780 N  N   . ALA   B 124 ? 0.1328 0.1177 0.1453 -0.0224 -0.0072 -0.0025 124 ALA   B N   
5781 C  CA  . ALA   B 124 ? 0.1275 0.1218 0.1570 -0.0181 -0.0110 -0.0047 124 ALA   B CA  
5782 C  C   . ALA   B 124 ? 0.1279 0.1172 0.1460 -0.0173 -0.0141 0.0026  124 ALA   B C   
5783 O  O   . ALA   B 124 ? 0.1406 0.1214 0.1622 -0.0117 -0.0130 0.0007  124 ALA   B O   
5784 C  CB  . ALA   B 124 ? 0.1344 0.1243 0.1615 -0.0101 -0.0021 -0.0026 124 ALA   B CB  
5790 N  N   . PRO   B 125 ? 0.1392 0.1171 0.1521 -0.0169 -0.0173 0.0144  125 PRO   B N   
5791 C  CA  . PRO   B 125 ? 0.1464 0.1210 0.1685 -0.0181 -0.0177 0.0178  125 PRO   B CA  
5792 C  C   . PRO   B 125 ? 0.1366 0.1151 0.1758 -0.0139 -0.0100 0.0066  125 PRO   B C   
5793 O  O   . PRO   B 125 ? 0.1384 0.1165 0.1943 -0.0101 -0.0033 0.0130  125 PRO   B O   
5794 C  CB  . PRO   B 125 ? 0.1489 0.1485 0.1766 -0.0189 -0.0197 0.0329  125 PRO   B CB  
5795 C  CG  . PRO   B 125 ? 0.1527 0.1555 0.1638 -0.0311 -0.0192 0.0180  125 PRO   B CG  
5796 C  CD  . PRO   B 125 ? 0.1481 0.1334 0.1504 -0.0303 -0.0131 0.0126  125 PRO   B CD  
5804 N  N   . LEU   B 126 ? 0.1440 0.1132 0.1984 -0.0174 0.0086  0.0155  126 LEU   B N   
5805 C  CA  . LEU   B 126 ? 0.1496 0.1254 0.2032 -0.0148 0.0185  0.0119  126 LEU   B CA  
5806 C  C   . LEU   B 126 ? 0.1415 0.1332 0.2108 0.0002  0.0234  0.0216  126 LEU   B C   
5807 O  O   . LEU   B 126 ? 0.1653 0.1571 0.2201 0.0195  -0.0021 -0.0039 126 LEU   B O   
5808 C  CB  . LEU   B 126 ? 0.1706 0.1303 0.2278 -0.0218 0.0249  0.0107  126 LEU   B CB  
5809 C  CG  . LEU   B 126 ? 0.1837 0.1397 0.2416 -0.0254 0.0263  -0.0089 126 LEU   B CG  
5810 C  CD1 . LEU   B 126 ? 0.2018 0.1474 0.2889 -0.0242 0.0227  -0.0146 126 LEU   B CD1 
5811 C  CD2 . LEU   B 126 ? 0.1843 0.1489 0.2454 -0.0292 0.0275  -0.0126 126 LEU   B CD2 
5823 N  N   . LEU   B 127 ? 0.1396 0.1200 0.2195 0.0035  0.0290  0.0174  127 LEU   B N   
5824 C  CA  . LEU   B 127 ? 0.1430 0.1312 0.2208 -0.0034 0.0276  0.0222  127 LEU   B CA  
5825 C  C   . LEU   B 127 ? 0.1385 0.1274 0.2176 0.0016  0.0200  0.0237  127 LEU   B C   
5826 O  O   . LEU   B 127 ? 0.1413 0.1316 0.2285 -0.0145 0.0146  0.0225  127 LEU   B O   
5827 C  CB  . LEU   B 127 ? 0.1542 0.1314 0.2338 -0.0013 0.0261  0.0211  127 LEU   B CB  
5828 C  CG  . LEU   B 127 ? 0.1663 0.1337 0.2399 0.0010  0.0245  0.0229  127 LEU   B CG  
5829 C  CD1 . LEU   B 127 ? 0.1748 0.1276 0.2417 0.0084  0.0098  0.0139  127 LEU   B CD1 
5830 C  CD2 . LEU   B 127 ? 0.1747 0.1409 0.2512 -0.0186 0.0237  0.0345  127 LEU   B CD2 
5842 N  N   . SER   B 128 ? 0.1447 0.1312 0.2139 0.0070  0.0051  0.0220  128 SER   B N   
5843 C  CA  . SER   B 128 ? 0.1616 0.1385 0.2157 0.0090  -0.0048 0.0279  128 SER   B CA  
5844 C  C   . SER   B 128 ? 0.1686 0.1430 0.2439 0.0079  -0.0239 0.0224  128 SER   B C   
5845 O  O   . SER   B 128 ? 0.1838 0.1450 0.2762 0.0043  -0.0212 0.0347  128 SER   B O   
5846 C  CB  . SER   B 128 ? 0.1666 0.1399 0.2154 0.0071  0.0039  0.0389  128 SER   B CB  
5847 O  OG  . SER   B 128 ? 0.1687 0.1538 0.2206 0.0106  0.0120  0.0399  128 SER   B OG  
5853 N  N   . ALA   B 129 ? 0.1791 0.1480 0.2665 0.0229  -0.0177 0.0089  129 ALA   B N   
5854 C  CA  . ALA   B 129 ? 0.1927 0.1509 0.2798 0.0302  -0.0167 -0.0021 129 ALA   B CA  
5855 C  C   . ALA   B 129 ? 0.1837 0.1437 0.2670 0.0212  0.0014  0.0026  129 ALA   B C   
5856 O  O   . ALA   B 129 ? 0.1716 0.1474 0.2632 0.0154  -0.0002 0.0043  129 ALA   B O   
5857 C  CB  . ALA   B 129 ? 0.2124 0.1758 0.3116 0.0328  -0.0071 -0.0045 129 ALA   B CB  
5863 N  N   . GLY   B 130 ? 0.1826 0.1424 0.2631 0.0278  0.0061  0.0024  130 GLY   B N   
5864 C  CA  . GLY   B 130 ? 0.1887 0.1528 0.2689 0.0269  0.0205  0.0008  130 GLY   B CA  
5865 C  C   . GLY   B 130 ? 0.1941 0.1567 0.2651 0.0204  0.0207  0.0095  130 GLY   B C   
5866 O  O   . GLY   B 130 ? 0.2091 0.1644 0.2750 0.0191  0.0177  0.0192  130 GLY   B O   
5870 N  N   . ILE   B 131 ? 0.1863 0.1695 0.2740 0.0366  0.0161  0.0080  131 ILE   B N   
5871 C  CA  . ILE   B 131 ? 0.2058 0.1856 0.2746 0.0299  0.0001  0.0176  131 ILE   B CA  
5872 C  C   . ILE   B 131 ? 0.2192 0.1729 0.2416 0.0211  -0.0033 0.0185  131 ILE   B C   
5873 O  O   . ILE   B 131 ? 0.2448 0.1944 0.2495 0.0200  -0.0216 0.0216  131 ILE   B O   
5874 C  CB  . ILE   B 131 ? 0.2051 0.2176 0.3112 0.0258  -0.0119 0.0255  131 ILE   B CB  
5875 C  CG1 . ILE   B 131 ? 0.2061 0.2380 0.3297 0.0011  -0.0051 0.0316  131 ILE   B CG1 
5876 C  CG2 . ILE   B 131 ? 0.2069 0.2309 0.3312 0.0362  -0.0047 0.0200  131 ILE   B CG2 
5877 C  CD1 . ILE   B 131 ? 0.2131 0.2564 0.3463 -0.0149 -0.0126 0.0396  131 ILE   B CD1 
5889 N  N   . PHE   B 132 ? 0.2028 0.1572 0.2320 0.0164  0.0122  0.0239  132 PHE   B N   
5890 C  CA  . PHE   B 132 ? 0.2147 0.1595 0.2341 0.0083  0.0332  0.0192  132 PHE   B CA  
5891 C  C   . PHE   B 132 ? 0.2327 0.1735 0.2527 0.0106  0.0473  0.0175  132 PHE   B C   
5892 O  O   . PHE   B 132 ? 0.2516 0.1910 0.2742 0.0048  0.0611  0.0193  132 PHE   B O   
5893 C  CB  . PHE   B 132 ? 0.2012 0.1581 0.2096 0.0114  0.0388  0.0235  132 PHE   B CB  
5894 C  CG  . PHE   B 132 ? 0.1927 0.1598 0.2066 0.0151  0.0281  0.0258  132 PHE   B CG  
5895 C  CD1 . PHE   B 132 ? 0.1948 0.1611 0.2337 0.0133  0.0273  0.0227  132 PHE   B CD1 
5896 C  CD2 . PHE   B 132 ? 0.1909 0.1642 0.1812 0.0254  0.0243  0.0302  132 PHE   B CD2 
5897 C  CE1 . PHE   B 132 ? 0.2007 0.1660 0.2378 0.0059  0.0234  0.0216  132 PHE   B CE1 
5898 C  CE2 . PHE   B 132 ? 0.1974 0.1717 0.1894 0.0204  0.0150  0.0259  132 PHE   B CE2 
5899 C  CZ  . PHE   B 132 ? 0.1981 0.1697 0.2176 0.0072  0.0046  0.0357  132 PHE   B CZ  
5909 N  N   . GLY   B 133 ? 0.2317 0.1682 0.2519 0.0029  0.0346  0.0384  133 GLY   B N   
5910 C  CA  . GLY   B 133 ? 0.2398 0.1791 0.2631 -0.0148 0.0363  0.0475  133 GLY   B CA  
5911 C  C   . GLY   B 133 ? 0.2438 0.1840 0.2686 -0.0293 0.0372  0.0470  133 GLY   B C   
5912 O  O   . GLY   B 133 ? 0.2626 0.1940 0.3074 -0.0383 0.0399  0.0567  133 GLY   B O   
5916 N  N   . ALA   B 134 ? 0.2250 0.1815 0.2517 -0.0316 0.0359  0.0335  134 ALA   B N   
5917 C  CA  . ALA   B 134 ? 0.2200 0.1797 0.2545 -0.0220 0.0401  0.0211  134 ALA   B CA  
5918 C  C   . ALA   B 134 ? 0.2277 0.1704 0.2631 -0.0154 0.0378  0.0324  134 ALA   B C   
5919 O  O   . ALA   B 134 ? 0.2321 0.1880 0.2787 -0.0036 0.0300  0.0278  134 ALA   B O   
5920 C  CB  . ALA   B 134 ? 0.2176 0.1836 0.2653 -0.0170 0.0353  0.0107  134 ALA   B CB  
5926 N  N   . ASP   B 135 ? 0.2397 0.1649 0.2729 -0.0152 0.0261  0.0395  135 ASP   B N   
5927 C  CA  . ASP   B 135 ? 0.2538 0.1594 0.2954 -0.0123 0.0090  0.0389  135 ASP   B CA  
5928 C  C   . ASP   B 135 ? 0.2327 0.1490 0.2821 -0.0027 0.0043  0.0323  135 ASP   B C   
5929 O  O   . ASP   B 135 ? 0.2238 0.1456 0.2858 -0.0064 0.0120  0.0323  135 ASP   B O   
5930 C  CB  . ASP   B 135 ? 0.2800 0.1686 0.3274 -0.0323 0.0075  0.0397  135 ASP   B CB  
5931 C  CG  . ASP   B 135 ? 0.3041 0.1690 0.3664 -0.0530 0.0067  0.0393  135 ASP   B CG  
5932 O  OD1 . ASP   B 135 ? 0.3101 0.1559 0.3629 -0.0362 -0.0038 0.0342  135 ASP   B OD1 
5933 O  OD2 . ASP   B 135 ? 0.3242 0.2024 0.4126 -0.0725 0.0060  0.0225  135 ASP   B OD2 
5938 N  N   . PRO   B 136 ? 0.2211 0.1538 0.2827 0.0156  -0.0150 0.0283  136 PRO   B N   
5939 C  CA  . PRO   B 136 ? 0.2014 0.1421 0.2805 0.0124  -0.0152 0.0180  136 PRO   B CA  
5940 C  C   . PRO   B 136 ? 0.1813 0.1323 0.2936 0.0083  -0.0093 0.0141  136 PRO   B C   
5941 O  O   . PRO   B 136 ? 0.1648 0.1313 0.2824 0.0070  0.0057  0.0144  136 PRO   B O   
5942 C  CB  . PRO   B 136 ? 0.2089 0.1618 0.2867 0.0246  -0.0185 0.0026  136 PRO   B CB  
5943 C  CG  . PRO   B 136 ? 0.2275 0.1737 0.2996 0.0293  -0.0130 0.0084  136 PRO   B CG  
5944 C  CD  . PRO   B 136 ? 0.2282 0.1682 0.2933 0.0365  -0.0088 0.0139  136 PRO   B CD  
5952 N  N   . ILE   B 137 ? 0.1914 0.1255 0.3044 0.0082  -0.0135 0.0075  137 ILE   B N   
5953 C  CA  . ILE   B 137 ? 0.1986 0.1259 0.3144 -0.0030 -0.0058 0.0072  137 ILE   B CA  
5954 C  C   . ILE   B 137 ? 0.1895 0.1287 0.2995 -0.0077 0.0124  0.0171  137 ILE   B C   
5955 O  O   . ILE   B 137 ? 0.1837 0.1340 0.2818 -0.0118 0.0100  0.0157  137 ILE   B O   
5956 C  CB  . ILE   B 137 ? 0.2228 0.1330 0.3545 -0.0041 -0.0033 0.0121  137 ILE   B CB  
5957 C  CG1 . ILE   B 137 ? 0.2470 0.1549 0.3932 0.0040  0.0069  0.0061  137 ILE   B CG1 
5958 C  CG2 . ILE   B 137 ? 0.2213 0.1311 0.3589 -0.0273 -0.0041 0.0109  137 ILE   B CG2 
5959 C  CD1 . ILE   B 137 ? 0.2687 0.1815 0.4274 0.0173  0.0055  0.0112  137 ILE   B CD1 
5971 N  N   . HIS   B 138 ? 0.1948 0.1295 0.3044 -0.0067 0.0239  0.0180  138 HIS   B N   
5972 C  CA  . HIS   B 138 ? 0.2039 0.1392 0.2972 -0.0062 0.0347  0.0214  138 HIS   B CA  
5973 C  C   . HIS   B 138 ? 0.1850 0.1356 0.2775 -0.0067 0.0318  0.0211  138 HIS   B C   
5974 O  O   . HIS   B 138 ? 0.1725 0.1423 0.2982 -0.0024 0.0370  0.0320  138 HIS   B O   
5975 C  CB  . HIS   B 138 ? 0.2292 0.1515 0.3049 -0.0072 0.0536  0.0163  138 HIS   B CB  
5976 C  CG  . HIS   B 138 ? 0.2534 0.1701 0.3087 -0.0126 0.0731  0.0329  138 HIS   B CG  
5977 N  ND1 . HIS   B 138 ? 0.2632 0.1863 0.3319 -0.0074 0.0851  0.0284  138 HIS   B ND1 
5978 C  CD2 . HIS   B 138 ? 0.2704 0.1798 0.3071 -0.0119 0.0791  0.0336  138 HIS   B CD2 
5979 C  CE1 . HIS   B 138 ? 0.2715 0.1867 0.3308 -0.0077 0.0887  0.0315  138 HIS   B CE1 
5980 N  NE2 . HIS   B 138 ? 0.2793 0.1785 0.3097 -0.0040 0.0871  0.0294  138 HIS   B NE2 
5988 N  N   . SER   B 139 ? 0.1818 0.1241 0.2749 0.0007  0.0233  0.0172  139 SER   B N   
5989 C  CA  . SER   B 139 ? 0.1770 0.1209 0.2621 -0.0023 0.0244  0.0096  139 SER   B CA  
5990 C  C   . SER   B 139 ? 0.1508 0.1180 0.2534 -0.0010 0.0212  0.0093  139 SER   B C   
5991 O  O   . SER   B 139 ? 0.1518 0.1180 0.2517 0.0018  0.0059  0.0114  139 SER   B O   
5992 C  CB  . SER   B 139 ? 0.1828 0.1196 0.2700 -0.0007 0.0050  0.0073  139 SER   B CB  
5993 O  OG  . SER   B 139 ? 0.1795 0.1202 0.2700 0.0028  -0.0056 0.0159  139 SER   B OG  
5999 N  N   . LEU   B 140 ? 0.1510 0.1129 0.2445 -0.0055 0.0158  0.0037  140 LEU   B N   
6000 C  CA  . LEU   B 140 ? 0.1447 0.1099 0.2491 -0.0070 0.0106  0.0051  140 LEU   B CA  
6001 C  C   . LEU   B 140 ? 0.1390 0.1147 0.2661 -0.0081 -0.0035 0.0016  140 LEU   B C   
6002 O  O   . LEU   B 140 ? 0.1380 0.1176 0.2682 -0.0018 -0.0039 0.0066  140 LEU   B O   
6003 C  CB  . LEU   B 140 ? 0.1436 0.1135 0.2558 -0.0070 0.0155  -0.0043 140 LEU   B CB  
6004 C  CG  . LEU   B 140 ? 0.1575 0.1199 0.2604 -0.0149 -0.0013 0.0050  140 LEU   B CG  
6005 C  CD1 . LEU   B 140 ? 0.1626 0.1300 0.2688 -0.0144 0.0076  0.0094  140 LEU   B CD1 
6006 C  CD2 . LEU   B 140 ? 0.1773 0.1268 0.2721 -0.0148 -0.0043 -0.0107 140 LEU   B CD2 
6018 N  N   . ARG   B 141 ? 0.1357 0.1165 0.2801 -0.0142 0.0050  -0.0042 141 ARG   B N   
6019 C  CA  . ARG   B 141 ? 0.1380 0.1200 0.3108 -0.0166 0.0233  -0.0023 141 ARG   B CA  
6020 C  C   . ARG   B 141 ? 0.1336 0.1182 0.3016 -0.0140 0.0109  -0.0012 141 ARG   B C   
6021 O  O   . ARG   B 141 ? 0.1360 0.1232 0.3016 -0.0102 0.0013  -0.0084 141 ARG   B O   
6022 C  CB  . ARG   B 141 ? 0.1574 0.1328 0.3280 -0.0249 0.0332  0.0020  141 ARG   B CB  
6023 C  CG  . ARG   B 141 ? 0.1893 0.1574 0.3331 -0.0197 0.0333  0.0018  141 ARG   B CG  
6024 C  CD  . ARG   B 141 ? 0.2281 0.1801 0.3357 -0.0141 0.0146  -0.0125 141 ARG   B CD  
6025 N  NE  . ARG   B 141 ? 0.2451 0.1753 0.3280 -0.0300 0.0173  -0.0233 141 ARG   B NE  
6026 C  CZ  . ARG   B 141 ? 0.2612 0.1652 0.3129 -0.0273 0.0254  -0.0320 141 ARG   B CZ  
6027 N  NH1 . ARG   B 141 ? 0.2723 0.1576 0.3063 -0.0267 0.0228  -0.0318 141 ARG   B NH1 
6028 N  NH2 . ARG   B 141 ? 0.2693 0.1765 0.3238 -0.0166 0.0146  -0.0255 141 ARG   B NH2 
6042 N  N   . VAL   B 142 ? 0.1376 0.1140 0.2875 -0.0114 0.0161  0.0005  142 VAL   B N   
6043 C  CA  . VAL   B 142 ? 0.1342 0.1193 0.2781 -0.0077 0.0155  -0.0040 142 VAL   B CA  
6044 C  C   . VAL   B 142 ? 0.1316 0.1176 0.2754 -0.0061 0.0109  -0.0036 142 VAL   B C   
6045 O  O   . VAL   B 142 ? 0.1413 0.1176 0.2834 -0.0003 0.0154  0.0034  142 VAL   B O   
6046 C  CB  . VAL   B 142 ? 0.1474 0.1308 0.2837 -0.0020 0.0212  0.0088  142 VAL   B CB  
6047 C  CG1 . VAL   B 142 ? 0.1469 0.1323 0.2807 0.0098  0.0273  0.0035  142 VAL   B CG1 
6048 C  CG2 . VAL   B 142 ? 0.1654 0.1339 0.2927 -0.0009 0.0165  0.0114  142 VAL   B CG2 
6058 N  N   . CYS   B 143 ? 0.1293 0.1195 0.2550 -0.0041 0.0122  0.0064  143 CYS   B N   
6059 C  CA  . CYS   B 143 ? 0.1274 0.1213 0.2539 -0.0089 0.0002  0.0003  143 CYS   B CA  
6060 C  C   . CYS   B 143 ? 0.1277 0.1249 0.2579 -0.0052 0.0057  -0.0038 143 CYS   B C   
6061 O  O   . CYS   B 143 ? 0.1309 0.1262 0.2527 -0.0062 0.0023  -0.0021 143 CYS   B O   
6062 C  CB  . CYS   B 143 ? 0.1347 0.1298 0.2476 -0.0049 0.0023  -0.0040 143 CYS   B CB  
6063 S  SG  . CYS   B 143 ? 0.1385 0.1403 0.2367 -0.0048 0.0038  0.0047  143 CYS   B SG  
6069 N  N   . VAL   B 144 ? 0.1315 0.1222 0.2742 -0.0075 0.0005  -0.0166 144 VAL   B N   
6070 C  CA  . VAL   B 144 ? 0.1354 0.1260 0.3037 -0.0152 -0.0111 -0.0215 144 VAL   B CA  
6071 C  C   . VAL   B 144 ? 0.1306 0.1318 0.3094 -0.0101 -0.0162 -0.0070 144 VAL   B C   
6072 O  O   . VAL   B 144 ? 0.1405 0.1530 0.3243 0.0027  -0.0139 0.0156  144 VAL   B O   
6073 C  CB  . VAL   B 144 ? 0.1612 0.1426 0.3479 -0.0219 -0.0180 -0.0310 144 VAL   B CB  
6074 C  CG1 . VAL   B 144 ? 0.1849 0.1814 0.3713 -0.0112 -0.0259 -0.0182 144 VAL   B CG1 
6075 C  CG2 . VAL   B 144 ? 0.1739 0.1450 0.3312 -0.0076 -0.0283 -0.0413 144 VAL   B CG2 
6085 N  N   . ASP   B 145 ? 0.1356 0.1241 0.3180 -0.0063 -0.0074 -0.0153 145 ASP   B N   
6086 C  CA  . ASP   B 145 ? 0.1352 0.1292 0.3329 -0.0097 0.0061  -0.0116 145 ASP   B CA  
6087 C  C   . ASP   B 145 ? 0.1335 0.1327 0.3166 -0.0049 -0.0020 -0.0091 145 ASP   B C   
6088 O  O   . ASP   B 145 ? 0.1380 0.1443 0.3579 -0.0108 0.0035  -0.0199 145 ASP   B O   
6089 C  CB  . ASP   B 145 ? 0.1438 0.1377 0.3727 -0.0168 0.0249  -0.0064 145 ASP   B CB  
6090 C  CG  . ASP   B 145 ? 0.1617 0.1417 0.4220 -0.0259 0.0314  -0.0098 145 ASP   B CG  
6091 O  OD1 . ASP   B 145 ? 0.1640 0.1451 0.4253 -0.0224 -0.0028 -0.0143 145 ASP   B OD1 
6092 O  OD2 . ASP   B 145 ? 0.1954 0.1506 0.4631 -0.0283 0.0573  -0.0066 145 ASP   B OD2 
6097 N  N   . THR   B 146 ? 0.1261 0.1188 0.2715 -0.0093 -0.0024 0.0018  146 THR   B N   
6098 C  CA  . THR   B 146 ? 0.1302 0.1218 0.2483 -0.0080 0.0088  0.0022  146 THR   B CA  
6099 C  C   . THR   B 146 ? 0.1309 0.1240 0.2404 -0.0064 0.0068  0.0022  146 THR   B C   
6100 O  O   . THR   B 146 ? 0.1366 0.1212 0.2448 -0.0079 0.0010  -0.0015 146 THR   B O   
6101 C  CB  . THR   B 146 ? 0.1372 0.1233 0.2568 -0.0075 0.0203  0.0030  146 THR   B CB  
6102 O  OG1 . THR   B 146 ? 0.1409 0.1187 0.2712 -0.0094 0.0207  0.0110  146 THR   B OG1 
6103 C  CG2 . THR   B 146 ? 0.1446 0.1256 0.2632 -0.0037 0.0153  -0.0029 146 THR   B CG2 
6111 N  N   . VAL   B 147 ? 0.1325 0.1243 0.2264 -0.0043 0.0105  0.0045  147 VAL   B N   
6112 C  CA  . VAL   B 147 ? 0.1367 0.1227 0.2164 -0.0101 -0.0081 0.0050  147 VAL   B CA  
6113 C  C   . VAL   B 147 ? 0.1322 0.1210 0.2210 -0.0195 -0.0076 -0.0022 147 VAL   B C   
6114 O  O   . VAL   B 147 ? 0.1446 0.1333 0.2346 -0.0215 -0.0272 -0.0122 147 VAL   B O   
6115 C  CB  . VAL   B 147 ? 0.1387 0.1353 0.2047 -0.0082 -0.0117 -0.0002 147 VAL   B CB  
6116 C  CG1 . VAL   B 147 ? 0.1380 0.1472 0.1951 -0.0152 -0.0032 0.0055  147 VAL   B CG1 
6117 C  CG2 . VAL   B 147 ? 0.1410 0.1328 0.2100 -0.0125 -0.0048 0.0017  147 VAL   B CG2 
6127 N  N   . ARG   B 148 ? 0.1368 0.1228 0.2177 -0.0098 -0.0204 -0.0053 148 ARG   B N   
6128 C  CA  . ARG   B 148 ? 0.1396 0.1301 0.2066 -0.0076 -0.0281 -0.0070 148 ARG   B CA  
6129 C  C   . ARG   B 148 ? 0.1457 0.1409 0.2005 -0.0107 -0.0308 -0.0059 148 ARG   B C   
6130 O  O   . ARG   B 148 ? 0.1628 0.1694 0.2099 -0.0253 -0.0400 -0.0010 148 ARG   B O   
6131 C  CB  . ARG   B 148 ? 0.1479 0.1387 0.2076 -0.0015 -0.0341 -0.0165 148 ARG   B CB  
6132 C  CG  . ARG   B 148 ? 0.1480 0.1525 0.2351 -0.0126 -0.0271 -0.0259 148 ARG   B CG  
6133 C  CD  . ARG   B 148 ? 0.1537 0.1698 0.2479 0.0053  -0.0304 -0.0325 148 ARG   B CD  
6134 N  NE  . ARG   B 148 ? 0.1547 0.1683 0.2440 0.0233  -0.0332 -0.0287 148 ARG   B NE  
6135 C  CZ  . ARG   B 148 ? 0.1444 0.1607 0.2239 0.0162  -0.0247 -0.0220 148 ARG   B CZ  
6136 N  NH1 . ARG   B 148 ? 0.1421 0.1707 0.2321 -0.0015 -0.0054 -0.0219 148 ARG   B NH1 
6137 N  NH2 . ARG   B 148 ? 0.1675 0.1441 0.2182 0.0123  -0.0162 -0.0154 148 ARG   B NH2 
6151 N  N   . THR   B 149 ? 0.1464 0.1333 0.2044 -0.0158 -0.0297 -0.0028 149 THR   B N   
6152 C  CA  . THR   B 149 ? 0.1529 0.1404 0.1970 -0.0177 -0.0268 0.0049  149 THR   B CA  
6153 C  C   . THR   B 149 ? 0.1529 0.1392 0.1878 -0.0144 -0.0295 0.0053  149 THR   B C   
6154 O  O   . THR   B 149 ? 0.1554 0.1379 0.2014 -0.0222 -0.0160 0.0013  149 THR   B O   
6155 C  CB  . THR   B 149 ? 0.1567 0.1368 0.1960 -0.0149 -0.0295 0.0001  149 THR   B CB  
6156 O  OG1 . THR   B 149 ? 0.1571 0.1449 0.1904 -0.0234 -0.0325 0.0000  149 THR   B OG1 
6157 C  CG2 . THR   B 149 ? 0.1621 0.1424 0.2125 -0.0026 -0.0250 -0.0012 149 THR   B CG2 
6165 N  N   . ASN   B 150 ? 0.1575 0.1347 0.1872 -0.0143 -0.0380 0.0027  150 ASN   B N   
6166 C  CA  . ASN   B 150 ? 0.1646 0.1497 0.1787 -0.0228 -0.0332 -0.0005 150 ASN   B CA  
6167 C  C   . ASN   B 150 ? 0.1545 0.1443 0.1766 -0.0173 -0.0275 -0.0032 150 ASN   B C   
6168 O  O   . ASN   B 150 ? 0.1604 0.1373 0.1962 -0.0260 -0.0402 -0.0023 150 ASN   B O   
6169 C  CB  . ASN   B 150 ? 0.1881 0.1820 0.1882 -0.0229 -0.0471 0.0129  150 ASN   B CB  
6170 C  CG  . ASN   B 150 ? 0.2149 0.2234 0.2263 -0.0215 -0.0500 0.0271  150 ASN   B CG  
6171 O  OD1 . ASN   B 150 ? 0.2202 0.2394 0.2408 -0.0305 -0.0605 0.0223  150 ASN   B OD1 
6172 N  ND2 . ASN   B 150 ? 0.2328 0.2420 0.2537 -0.0097 -0.0546 0.0639  150 ASN   B ND2 
6179 N  N   . VAL   B 151 ? 0.1475 0.1376 0.1823 -0.0173 -0.0291 -0.0023 151 VAL   B N   
6180 C  CA  . VAL   B 151 ? 0.1460 0.1393 0.1842 -0.0241 -0.0239 0.0014  151 VAL   B CA  
6181 C  C   . VAL   B 151 ? 0.1503 0.1358 0.1768 -0.0319 -0.0266 -0.0032 151 VAL   B C   
6182 O  O   . VAL   B 151 ? 0.1581 0.1442 0.2026 -0.0313 -0.0208 -0.0111 151 VAL   B O   
6183 C  CB  . VAL   B 151 ? 0.1679 0.1546 0.1887 -0.0073 -0.0175 -0.0022 151 VAL   B CB  
6184 C  CG1 . VAL   B 151 ? 0.1726 0.1552 0.2157 -0.0194 -0.0081 -0.0043 151 VAL   B CG1 
6185 C  CG2 . VAL   B 151 ? 0.1843 0.1683 0.1731 0.0077  -0.0224 0.0130  151 VAL   B CG2 
6195 N  N   . TYR   B 152 ? 0.1461 0.1228 0.1713 -0.0247 -0.0222 -0.0005 152 TYR   B N   
6196 C  CA  . TYR   B 152 ? 0.1488 0.1397 0.1512 -0.0323 -0.0218 -0.0037 152 TYR   B CA  
6197 C  C   . TYR   B 152 ? 0.1494 0.1300 0.1498 -0.0245 -0.0110 -0.0069 152 TYR   B C   
6198 O  O   . TYR   B 152 ? 0.1561 0.1307 0.1685 -0.0277 -0.0116 -0.0022 152 TYR   B O   
6199 C  CB  . TYR   B 152 ? 0.1631 0.1548 0.1535 -0.0314 -0.0175 0.0038  152 TYR   B CB  
6200 C  CG  . TYR   B 152 ? 0.1807 0.1649 0.1520 -0.0430 -0.0162 0.0012  152 TYR   B CG  
6201 C  CD1 . TYR   B 152 ? 0.1907 0.1802 0.1538 -0.0359 -0.0257 0.0053  152 TYR   B CD1 
6202 C  CD2 . TYR   B 152 ? 0.2039 0.1877 0.1627 -0.0428 -0.0138 -0.0058 152 TYR   B CD2 
6203 C  CE1 . TYR   B 152 ? 0.2078 0.1984 0.1689 -0.0334 -0.0310 0.0171  152 TYR   B CE1 
6204 C  CE2 . TYR   B 152 ? 0.2160 0.2091 0.1622 -0.0454 -0.0204 -0.0094 152 TYR   B CE2 
6205 C  CZ  . TYR   B 152 ? 0.2193 0.2210 0.1587 -0.0397 -0.0373 0.0128  152 TYR   B CZ  
6206 O  OH  . TYR   B 152 ? 0.2427 0.2540 0.1941 -0.0215 -0.0437 0.0175  152 TYR   B OH  
6216 N  N   . LEU   B 153 ? 0.1501 0.1264 0.1658 -0.0298 -0.0157 -0.0050 153 LEU   B N   
6217 C  CA  . LEU   B 153 ? 0.1513 0.1284 0.1562 -0.0234 -0.0064 -0.0086 153 LEU   B CA  
6218 C  C   . LEU   B 153 ? 0.1552 0.1226 0.1712 -0.0283 -0.0014 -0.0151 153 LEU   B C   
6219 O  O   . LEU   B 153 ? 0.1670 0.1450 0.1832 -0.0157 -0.0046 -0.0322 153 LEU   B O   
6220 C  CB  . LEU   B 153 ? 0.1507 0.1229 0.1799 -0.0258 -0.0020 -0.0095 153 LEU   B CB  
6221 C  CG  . LEU   B 153 ? 0.1503 0.1355 0.2093 -0.0244 -0.0051 -0.0053 153 LEU   B CG  
6222 C  CD1 . LEU   B 153 ? 0.1602 0.1458 0.2173 -0.0248 0.0032  0.0018  153 LEU   B CD1 
6223 C  CD2 . LEU   B 153 ? 0.1532 0.1464 0.2081 -0.0270 0.0075  0.0071  153 LEU   B CD2 
6235 N  N   . ALA   B 154 ? 0.1457 0.1281 0.1811 -0.0135 -0.0121 -0.0117 154 ALA   B N   
6236 C  CA  . ALA   B 154 ? 0.1567 0.1414 0.2093 -0.0025 -0.0188 -0.0259 154 ALA   B CA  
6237 C  C   . ALA   B 154 ? 0.1665 0.1409 0.2117 0.0006  -0.0282 -0.0316 154 ALA   B C   
6238 O  O   . ALA   B 154 ? 0.2020 0.1383 0.2270 0.0036  -0.0089 -0.0077 154 ALA   B O   
6239 C  CB  . ALA   B 154 ? 0.1554 0.1588 0.2256 -0.0039 -0.0115 -0.0299 154 ALA   B CB  
6245 N  N   . VAL   B 155 ? 0.1389 0.1336 0.2281 -0.0050 -0.0010 -0.0209 155 VAL   B N   
6246 C  CA  . VAL   B 155 ? 0.1339 0.1283 0.2434 -0.0018 -0.0118 -0.0143 155 VAL   B CA  
6247 C  C   . VAL   B 155 ? 0.1373 0.1264 0.2370 -0.0075 -0.0136 -0.0264 155 VAL   B C   
6248 O  O   . VAL   B 155 ? 0.1538 0.1464 0.2742 0.0029  -0.0084 -0.0445 155 VAL   B O   
6249 C  CB  . VAL   B 155 ? 0.1408 0.1472 0.2778 -0.0042 -0.0185 -0.0026 155 VAL   B CB  
6250 C  CG1 . VAL   B 155 ? 0.1512 0.1400 0.2717 -0.0104 -0.0089 -0.0103 155 VAL   B CG1 
6251 C  CG2 . VAL   B 155 ? 0.1317 0.1574 0.2956 -0.0084 -0.0147 0.0228  155 VAL   B CG2 
6261 N  N   . PHE   B 156 ? 0.1279 0.1356 0.2578 0.0009  -0.0058 -0.0221 156 PHE   B N   
6262 C  CA  . PHE   B 156 ? 0.1356 0.1451 0.2963 0.0044  -0.0066 -0.0205 156 PHE   B CA  
6263 C  C   . PHE   B 156 ? 0.1320 0.1563 0.3294 0.0108  -0.0110 -0.0358 156 PHE   B C   
6264 O  O   . PHE   B 156 ? 0.1580 0.1799 0.3553 0.0188  0.0038  -0.0466 156 PHE   B O   
6265 C  CB  . PHE   B 156 ? 0.1438 0.1402 0.2852 0.0012  -0.0083 -0.0101 156 PHE   B CB  
6266 C  CG  . PHE   B 156 ? 0.1436 0.1528 0.2907 0.0003  -0.0079 0.0014  156 PHE   B CG  
6267 C  CD1 . PHE   B 156 ? 0.1458 0.1769 0.3222 0.0063  0.0046  0.0329  156 PHE   B CD1 
6268 C  CD2 . PHE   B 156 ? 0.1472 0.1671 0.2844 0.0091  -0.0156 0.0065  156 PHE   B CD2 
6269 C  CE1 . PHE   B 156 ? 0.1449 0.1909 0.3319 0.0016  0.0011  0.0336  156 PHE   B CE1 
6270 C  CE2 . PHE   B 156 ? 0.1528 0.1887 0.3065 0.0105  -0.0175 0.0151  156 PHE   B CE2 
6271 C  CZ  . PHE   B 156 ? 0.1436 0.1952 0.3273 0.0122  -0.0175 0.0224  156 PHE   B CZ  
6281 N  N   . ASP   B 157 ? 0.1362 0.1487 0.3440 0.0110  -0.0249 -0.0235 157 ASP   B N   
6282 C  CA  . ASP   B 157 ? 0.1488 0.1604 0.3692 0.0102  -0.0275 -0.0347 157 ASP   B CA  
6283 C  C   . ASP   B 157 ? 0.1541 0.1623 0.3680 0.0087  -0.0206 -0.0562 157 ASP   B C   
6284 O  O   . ASP   B 157 ? 0.1398 0.1523 0.3626 0.0055  -0.0168 -0.0440 157 ASP   B O   
6285 C  CB  . ASP   B 157 ? 0.1788 0.1802 0.3813 0.0070  -0.0418 -0.0187 157 ASP   B CB  
6286 C  CG  . ASP   B 157 ? 0.2096 0.1922 0.4018 0.0011  -0.0318 -0.0165 157 ASP   B CG  
6287 O  OD1 . ASP   B 157 ? 0.2178 0.1808 0.4184 0.0085  -0.0264 -0.0139 157 ASP   B OD1 
6288 O  OD2 . ASP   B 157 ? 0.2324 0.2163 0.4227 -0.0008 -0.0181 -0.0113 157 ASP   B OD2 
6293 N  N   A LYS   B 158 ? 0.1582 0.1829 0.3723 0.0120  -0.0066 -0.0864 158 LYS   B N   
6294 N  N   B LYS   B 158 ? 0.1673 0.1801 0.3529 0.0108  -0.0132 -0.0645 158 LYS   B N   
6295 C  CA  A LYS   B 158 ? 0.1738 0.1995 0.3814 0.0061  -0.0002 -0.0956 158 LYS   B CA  
6296 C  CA  B LYS   B 158 ? 0.1836 0.1940 0.3488 0.0106  -0.0095 -0.0669 158 LYS   B CA  
6297 C  C   A LYS   B 158 ? 0.1711 0.1854 0.3867 0.0071  -0.0106 -0.0885 158 LYS   B C   
6298 C  C   B LYS   B 158 ? 0.1789 0.1861 0.3595 0.0106  -0.0154 -0.0694 158 LYS   B C   
6299 O  O   A LYS   B 158 ? 0.1701 0.1825 0.3939 -0.0066 -0.0063 -0.0970 158 LYS   B O   
6300 O  O   B LYS   B 158 ? 0.1800 0.1860 0.3491 0.0062  -0.0133 -0.0726 158 LYS   B O   
6301 C  CB  A LYS   B 158 ? 0.2006 0.2413 0.3780 0.0078  0.0112  -0.1100 158 LYS   B CB  
6302 C  CB  B LYS   B 158 ? 0.2066 0.2187 0.3409 0.0129  -0.0025 -0.0655 158 LYS   B CB  
6303 C  CG  A LYS   B 158 ? 0.2311 0.2835 0.3844 0.0074  0.0145  -0.1115 158 LYS   B CG  
6304 C  CG  B LYS   B 158 ? 0.2296 0.2403 0.3456 0.0142  0.0016  -0.0614 158 LYS   B CG  
6305 C  CD  A LYS   B 158 ? 0.2524 0.3238 0.3901 0.0041  0.0153  -0.1059 158 LYS   B CD  
6306 C  CD  B LYS   B 158 ? 0.2474 0.2607 0.3537 0.0139  0.0035  -0.0551 158 LYS   B CD  
6307 C  CE  A LYS   B 158 ? 0.2696 0.3522 0.3989 0.0049  0.0105  -0.1010 158 LYS   B CE  
6308 C  CE  B LYS   B 158 ? 0.2610 0.2747 0.3642 0.0157  0.0025  -0.0499 158 LYS   B CE  
6309 N  NZ  A LYS   B 158 ? 0.2720 0.3659 0.3977 0.0003  0.0054  -0.0985 158 LYS   B NZ  
6310 N  NZ  B LYS   B 158 ? 0.2660 0.2813 0.3684 0.0154  0.0016  -0.0472 158 LYS   B NZ  
6337 N  N   . ASN   B 159 ? 0.1746 0.1793 0.3923 0.0098  -0.0224 -0.0674 159 ASN   B N   
6338 C  CA  . ASN   B 159 ? 0.1884 0.1658 0.4227 0.0199  -0.0347 -0.0553 159 ASN   B CA  
6339 C  C   . ASN   B 159 ? 0.1688 0.1491 0.4247 0.0077  -0.0451 -0.0424 159 ASN   B C   
6340 O  O   . ASN   B 159 ? 0.1704 0.1409 0.4476 -0.0068 -0.0505 -0.0303 159 ASN   B O   
6341 C  CB  . ASN   B 159 ? 0.2078 0.1797 0.4515 0.0294  -0.0403 -0.0566 159 ASN   B CB  
6342 C  CG  . ASN   B 159 ? 0.2353 0.2034 0.4767 0.0305  -0.0478 -0.0656 159 ASN   B CG  
6343 O  OD1 . ASN   B 159 ? 0.2477 0.2112 0.4799 0.0391  -0.0503 -0.0679 159 ASN   B OD1 
6344 N  ND2 . ASN   B 159 ? 0.2387 0.2149 0.4883 0.0302  -0.0519 -0.0607 159 ASN   B ND2 
6352 N  N   . LEU   B 160 ? 0.1561 0.1427 0.4052 0.0055  -0.0467 -0.0375 160 LEU   B N   
6353 C  CA  . LEU   B 160 ? 0.1517 0.1503 0.3754 0.0075  -0.0375 -0.0224 160 LEU   B CA  
6354 C  C   . LEU   B 160 ? 0.1468 0.1365 0.3655 0.0002  -0.0256 -0.0297 160 LEU   B C   
6355 O  O   . LEU   B 160 ? 0.1374 0.1428 0.3545 -0.0008 -0.0312 -0.0178 160 LEU   B O   
6356 C  CB  . LEU   B 160 ? 0.1486 0.1611 0.3477 0.0025  -0.0335 -0.0136 160 LEU   B CB  
6357 C  CG  . LEU   B 160 ? 0.1493 0.1717 0.3210 0.0077  -0.0324 -0.0060 160 LEU   B CG  
6358 C  CD1 . LEU   B 160 ? 0.1646 0.1891 0.3167 -0.0000 -0.0212 -0.0041 160 LEU   B CD1 
6359 C  CD2 . LEU   B 160 ? 0.1555 0.1758 0.3100 0.0173  -0.0325 -0.0170 160 LEU   B CD2 
6371 N  N   . TYR   B 161 ? 0.1437 0.1460 0.3611 -0.0054 -0.0020 -0.0468 161 TYR   B N   
6372 C  CA  . TYR   B 161 ? 0.1557 0.1447 0.3415 -0.0157 0.0127  -0.0482 161 TYR   B CA  
6373 C  C   . TYR   B 161 ? 0.1649 0.1434 0.3286 -0.0097 0.0131  -0.0407 161 TYR   B C   
6374 O  O   . TYR   B 161 ? 0.1696 0.1463 0.3114 -0.0186 0.0053  -0.0384 161 TYR   B O   
6375 C  CB  . TYR   B 161 ? 0.1703 0.1568 0.3336 -0.0263 0.0364  -0.0565 161 TYR   B CB  
6376 C  CG  . TYR   B 161 ? 0.1958 0.1631 0.3287 -0.0325 0.0434  -0.0681 161 TYR   B CG  
6377 C  CD1 . TYR   B 161 ? 0.2016 0.1634 0.3200 -0.0433 0.0467  -0.0686 161 TYR   B CD1 
6378 C  CD2 . TYR   B 161 ? 0.2169 0.1705 0.3230 -0.0318 0.0369  -0.0626 161 TYR   B CD2 
6379 C  CE1 . TYR   B 161 ? 0.2204 0.1845 0.3175 -0.0443 0.0440  -0.0620 161 TYR   B CE1 
6380 C  CE2 . TYR   B 161 ? 0.2363 0.1878 0.3256 -0.0356 0.0355  -0.0607 161 TYR   B CE2 
6381 C  CZ  . TYR   B 161 ? 0.2345 0.1921 0.3158 -0.0511 0.0315  -0.0549 161 TYR   B CZ  
6382 O  OH  . TYR   B 161 ? 0.2631 0.2160 0.3367 -0.0534 0.0281  -0.0490 161 TYR   B OH  
6392 N  N   . ASP   B 162 ? 0.1705 0.1460 0.3447 -0.0085 0.0011  -0.0530 162 ASP   B N   
6393 C  CA  . ASP   B 162 ? 0.1785 0.1530 0.3509 -0.0079 -0.0080 -0.0555 162 ASP   B CA  
6394 C  C   . ASP   B 162 ? 0.1713 0.1415 0.3376 -0.0113 -0.0096 -0.0376 162 ASP   B C   
6395 O  O   . ASP   B 162 ? 0.1775 0.1488 0.3479 -0.0220 -0.0260 -0.0282 162 ASP   B O   
6396 C  CB  . ASP   B 162 ? 0.1973 0.1658 0.3737 -0.0018 -0.0150 -0.0744 162 ASP   B CB  
6397 C  CG  . ASP   B 162 ? 0.2051 0.1924 0.3983 0.0093  -0.0157 -0.0892 162 ASP   B CG  
6398 O  OD1 . ASP   B 162 ? 0.2011 0.2111 0.3998 0.0010  -0.0014 -0.0839 162 ASP   B OD1 
6399 O  OD2 . ASP   B 162 ? 0.2165 0.2108 0.4253 0.0262  -0.0114 -0.0863 162 ASP   B OD2 
6404 N  N   A LYS   B 163 ? 0.1658 0.1259 0.3300 -0.0127 -0.0233 -0.0242 163 LYS   B N   
6405 N  N   B LYS   B 163 ? 0.1730 0.1484 0.3268 -0.0121 -0.0160 -0.0238 163 LYS   B N   
6406 C  CA  A LYS   B 163 ? 0.1762 0.1341 0.3334 -0.0201 -0.0192 -0.0064 163 LYS   B CA  
6407 C  CA  B LYS   B 163 ? 0.1804 0.1629 0.3245 -0.0139 -0.0156 -0.0098 163 LYS   B CA  
6408 C  C   A LYS   B 163 ? 0.1517 0.1335 0.3262 -0.0178 -0.0201 -0.0011 163 LYS   B C   
6409 C  C   B LYS   B 163 ? 0.1582 0.1471 0.3122 -0.0140 -0.0187 -0.0032 163 LYS   B C   
6410 O  O   A LYS   B 163 ? 0.1503 0.1411 0.3482 -0.0202 -0.0230 0.0001  163 LYS   B O   
6411 O  O   B LYS   B 163 ? 0.1592 0.1502 0.3169 -0.0155 -0.0195 0.0004  163 LYS   B O   
6412 C  CB  A LYS   B 163 ? 0.2196 0.1647 0.3600 -0.0197 -0.0202 0.0072  163 LYS   B CB  
6413 C  CB  B LYS   B 163 ? 0.2098 0.1964 0.3453 -0.0134 -0.0158 -0.0031 163 LYS   B CB  
6414 C  CG  A LYS   B 163 ? 0.2848 0.2224 0.3967 -0.0220 -0.0117 0.0116  163 LYS   B CG  
6415 C  CG  B LYS   B 163 ? 0.2430 0.2324 0.3732 -0.0138 -0.0125 0.0005  163 LYS   B CG  
6416 C  CD  A LYS   B 163 ? 0.3403 0.2650 0.4350 -0.0291 -0.0079 0.0032  163 LYS   B CD  
6417 C  CD  B LYS   B 163 ? 0.2742 0.2661 0.4042 -0.0157 -0.0104 -0.0005 163 LYS   B CD  
6418 C  CE  A LYS   B 163 ? 0.3788 0.2974 0.4590 -0.0336 -0.0021 -0.0011 163 LYS   B CE  
6419 C  CE  B LYS   B 163 ? 0.2974 0.2916 0.4273 -0.0175 -0.0071 -0.0011 163 LYS   B CE  
6420 N  NZ  A LYS   B 163 ? 0.4032 0.3144 0.4767 -0.0362 0.0003  -0.0076 163 LYS   B NZ  
6421 N  NZ  B LYS   B 163 ? 0.3058 0.2979 0.4428 -0.0181 -0.0056 -0.0029 163 LYS   B NZ  
6448 N  N   . LEU   B 164 ? 0.1380 0.1297 0.3044 -0.0136 -0.0221 -0.0034 164 LEU   B N   
6449 C  CA  . LEU   B 164 ? 0.1410 0.1325 0.2871 -0.0147 -0.0256 -0.0026 164 LEU   B CA  
6450 C  C   . LEU   B 164 ? 0.1486 0.1328 0.2879 -0.0183 -0.0334 0.0005  164 LEU   B C   
6451 O  O   . LEU   B 164 ? 0.1527 0.1536 0.3015 -0.0171 -0.0338 -0.0023 164 LEU   B O   
6452 C  CB  . LEU   B 164 ? 0.1375 0.1314 0.2753 -0.0129 -0.0211 -0.0028 164 LEU   B CB  
6453 C  CG  . LEU   B 164 ? 0.1494 0.1445 0.2812 -0.0115 -0.0115 0.0004  164 LEU   B CG  
6454 C  CD1 . LEU   B 164 ? 0.1532 0.1443 0.2707 -0.0156 -0.0170 -0.0076 164 LEU   B CD1 
6455 C  CD2 . LEU   B 164 ? 0.1626 0.1795 0.2987 -0.0100 0.0000  -0.0076 164 LEU   B CD2 
6468 N  N   . VAL   B 165 ? 0.1832 0.1419 0.3060 -0.0229 -0.0400 -0.0026 165 VAL   B N   
6469 C  CA  . VAL   B 165 ? 0.2225 0.1551 0.3170 -0.0309 -0.0579 -0.0029 165 VAL   B CA  
6470 C  C   . VAL   B 165 ? 0.2465 0.1651 0.3496 -0.0395 -0.0843 -0.0051 165 VAL   B C   
6471 O  O   . VAL   B 165 ? 0.2660 0.1798 0.3642 -0.0453 -0.0887 0.0025  165 VAL   B O   
6472 C  CB  . VAL   B 165 ? 0.2461 0.1689 0.3168 -0.0146 -0.0316 -0.0124 165 VAL   B CB  
6473 C  CG1 . VAL   B 165 ? 0.2610 0.1813 0.3407 -0.0149 -0.0211 -0.0082 165 VAL   B CG1 
6474 C  CG2 . VAL   B 165 ? 0.2433 0.1678 0.3047 -0.0096 -0.0203 -0.0142 165 VAL   B CG2 
6484 N  N   . SER   B 166 ? 0.2528 0.1544 0.3772 -0.0373 -0.0933 -0.0233 166 SER   B N   
6485 C  CA  . SER   B 166 ? 0.2489 0.1558 0.4205 -0.0350 -0.0815 -0.0311 166 SER   B CA  
6486 C  C   . SER   B 166 ? 0.2351 0.1655 0.4354 -0.0351 -0.0765 -0.0096 166 SER   B C   
6487 O  O   . SER   B 166 ? 0.2409 0.1834 0.4562 -0.0503 -0.0843 -0.0277 166 SER   B O   
6488 C  CB  . SER   B 166 ? 0.2483 0.1661 0.4423 -0.0247 -0.0760 -0.0389 166 SER   B CB  
6489 O  OG  . SER   B 166 ? 0.2363 0.1647 0.4559 -0.0202 -0.0758 -0.0226 166 SER   B OG  
6495 N  N   . SER   B 167 ? 0.2122 0.1579 0.4115 -0.0396 -0.0815 0.0275  167 SER   B N   
6496 C  CA  . SER   B 167 ? 0.2027 0.1670 0.3938 -0.0351 -0.0568 0.0305  167 SER   B CA  
6497 C  C   . SER   B 167 ? 0.1977 0.1757 0.3727 -0.0523 -0.0510 0.0454  167 SER   B C   
6498 O  O   . SER   B 167 ? 0.1947 0.1882 0.3808 -0.0581 -0.0433 0.0471  167 SER   B O   
6499 C  CB  . SER   B 167 ? 0.1934 0.1727 0.3966 -0.0330 -0.0332 0.0256  167 SER   B CB  
6500 O  OG  . SER   B 167 ? 0.1893 0.1855 0.3940 -0.0222 -0.0181 0.0282  167 SER   B OG  
6506 N  N   . PHE   B 168 ? 0.1977 0.1743 0.3547 -0.0450 -0.0388 0.0554  168 PHE   B N   
6507 C  CA  . PHE   B 168 ? 0.2015 0.1711 0.3229 -0.0473 -0.0349 0.0322  168 PHE   B CA  
6508 C  C   . PHE   B 168 ? 0.1766 0.1586 0.2712 -0.0298 -0.0111 0.0152  168 PHE   B C   
6509 O  O   . PHE   B 168 ? 0.2021 0.1524 0.2656 -0.0002 -0.0134 -0.0029 168 PHE   B O   
6510 C  CB  . PHE   B 168 ? 0.2209 0.1770 0.3326 -0.0524 -0.0414 0.0452  168 PHE   B CB  
6511 C  CG  . PHE   B 168 ? 0.2404 0.1657 0.3258 -0.0562 -0.0472 0.0229  168 PHE   B CG  
6512 C  CD1 . PHE   B 168 ? 0.2673 0.1712 0.3365 -0.0487 -0.0477 0.0215  168 PHE   B CD1 
6513 C  CD2 . PHE   B 168 ? 0.2274 0.1576 0.3200 -0.0519 -0.0481 0.0265  168 PHE   B CD2 
6514 C  CE1 . PHE   B 168 ? 0.2765 0.1794 0.3296 -0.0403 -0.0416 0.0286  168 PHE   B CE1 
6515 C  CE2 . PHE   B 168 ? 0.2536 0.1678 0.3248 -0.0384 -0.0545 0.0202  168 PHE   B CE2 
6516 C  CZ  . PHE   B 168 ? 0.2677 0.1670 0.3254 -0.0301 -0.0527 0.0295  168 PHE   B CZ  
6526 N  N   . LEU   B 169 ? 0.1828 0.1722 0.2667 -0.0071 0.0029  -0.0026 169 LEU   B N   
6527 C  CA  . LEU   B 169 ? 0.2078 0.1994 0.2923 -0.0083 0.0032  -0.0282 169 LEU   B CA  
6528 C  C   . LEU   B 169 ? 0.2363 0.2222 0.3355 0.0018  -0.0009 -0.0469 169 LEU   B C   
6529 O  O   . LEU   B 169 ? 0.2574 0.2430 0.3834 -0.0010 0.0026  -0.0616 169 LEU   B O   
6530 C  CB  . LEU   B 169 ? 0.2298 0.2391 0.3078 -0.0108 0.0011  -0.0076 169 LEU   B CB  
6531 C  CG  . LEU   B 169 ? 0.2654 0.2709 0.3426 -0.0012 -0.0007 -0.0015 169 LEU   B CG  
6532 C  CD1 . LEU   B 169 ? 0.2775 0.2884 0.3483 -0.0021 -0.0048 0.0156  169 LEU   B CD1 
6533 C  CD2 . LEU   B 169 ? 0.2602 0.2753 0.3407 0.0119  0.0119  -0.0120 169 LEU   B CD2 
6534 O  OXT . LEU   B 169 ? 0.2507 0.2390 0.3377 0.0276  0.0019  -0.0481 169 LEU   B OXT 
6546 C  C1  T TFA   C .   ? 0.1507 0.1691 0.1530 -0.0090 0.0241  0.0162  201 TFA   A C1  
6547 C  C2  T TFA   C .   ? 0.1751 0.1943 0.1939 -0.0208 0.0221  0.0045  201 TFA   A C2  
6548 O  O   T TFA   C .   ? 0.1223 0.1505 0.1260 -0.0093 0.0167  0.0170  201 TFA   A O   
6549 F  F1  T TFA   C .   ? 0.1913 0.2035 0.2177 -0.0223 0.0164  0.0032  201 TFA   A F1  
6550 F  F2  T TFA   C .   ? 0.1835 0.1967 0.1958 -0.0223 0.0272  0.0049  201 TFA   A F2  
6551 F  F3  T TFA   C .   ? 0.1834 0.2108 0.2158 -0.0313 0.0339  -0.0036 201 TFA   A F3  
6552 O  OXT T TFA   C .   ? 0.1516 0.1635 0.1651 0.0145  0.0330  0.0128  201 TFA   A OXT 
6553 N  N2  B A1A80 D .   ? 0.1983 0.2178 0.2013 -0.0221 -0.0065 -0.0023 202 A1A80 A N2  
6554 C  C3  B A1A80 D .   ? 0.2397 0.2321 0.2227 -0.0303 0.0068  0.0021  202 A1A80 A C3  
6555 C  C6  B A1A80 D .   ? 0.2588 0.2421 0.2366 -0.0298 0.0065  0.0146  202 A1A80 A C6  
6556 C  C9  B A1A80 D .   ? 0.2561 0.2392 0.2264 -0.0300 0.0074  0.0098  202 A1A80 A C9  
6557 C  C12 B A1A80 D .   ? 0.1800 0.2110 0.1861 -0.0142 -0.0110 0.0077  202 A1A80 A C12 
6558 C  C14 B A1A80 D .   ? 0.1724 0.2115 0.1792 -0.0178 -0.0038 0.0128  202 A1A80 A C14 
6559 C  C1  B A1A80 D .   ? 0.2294 0.2290 0.2317 -0.0342 0.0097  -0.0094 202 A1A80 A C1  
6560 C  C10 B A1A80 D .   ? 0.1989 0.2178 0.1993 -0.0231 -0.0026 0.0025  202 A1A80 A C10 
6561 C  C11 B A1A80 D .   ? 0.1961 0.2180 0.2015 -0.0177 -0.0095 0.0020  202 A1A80 A C11 
6562 C  C13 B A1A80 D .   ? 0.1845 0.2142 0.1873 -0.0180 -0.0045 0.0074  202 A1A80 A C13 
6563 C  C15 B A1A80 D .   ? 0.1608 0.2042 0.1769 -0.0189 -0.0133 0.0158  202 A1A80 A C15 
6564 C  C2  B A1A80 D .   ? 0.2272 0.2264 0.2205 -0.0318 0.0070  -0.0017 202 A1A80 A C2  
6565 C  C4  B A1A80 D .   ? 0.2502 0.2363 0.2263 -0.0296 0.0085  0.0073  202 A1A80 A C4  
6566 C  C5  B A1A80 D .   ? 0.2553 0.2384 0.2309 -0.0295 0.0080  0.0096  202 A1A80 A C5  
6567 C  C7  B A1A80 D .   ? 0.2606 0.2452 0.2390 -0.0291 0.0070  0.0195  202 A1A80 A C7  
6568 C  C8  B A1A80 D .   ? 0.2605 0.2440 0.2344 -0.0306 0.0084  0.0126  202 A1A80 A C8  
6569 F  F1  B A1A80 D .   ? 0.2602 0.2500 0.2465 -0.0265 0.0035  0.0270  202 A1A80 A F1  
6570 N  N1  B A1A80 D .   ? 0.2123 0.2204 0.2101 -0.0283 0.0034  0.0008  202 A1A80 A N1  
6571 N  N3  B A1A80 D .   ? 0.1916 0.2161 0.1975 -0.0149 -0.0108 0.0059  202 A1A80 A N3  
6572 N  N4  B A1A80 D .   ? 0.1643 0.2022 0.1733 -0.0132 -0.0161 0.0180  202 A1A80 A N4  
6573 O  O1  B A1A80 D .   ? 0.2290 0.2318 0.2406 -0.0365 0.0131  -0.0125 202 A1A80 A O1  
6589 O  O1  C A1A8Z E .   ? 0.1899 0.2080 0.2161 -0.0152 0.0089  0.0015  203 A1A8Z A O1  
6590 C  C1  C A1A8Z E .   ? 0.1889 0.2057 0.2126 -0.0162 0.0076  0.0020  203 A1A8Z A C1  
6591 C  C2  C A1A8Z E .   ? 0.1867 0.2032 0.2084 -0.0174 0.0056  0.0036  203 A1A8Z A C2  
6592 C  C3  C A1A8Z E .   ? 0.1904 0.2064 0.2126 -0.0193 0.0077  0.0060  203 A1A8Z A C3  
6593 C  C4  C A1A8Z E .   ? 0.1935 0.2101 0.2171 -0.0207 0.0106  0.0080  203 A1A8Z A C4  
6594 C  C5  C A1A8Z E .   ? 0.1953 0.2111 0.2186 -0.0206 0.0114  0.0101  203 A1A8Z A C5  
6595 C  C6  C A1A8Z E .   ? 0.1969 0.2134 0.2218 -0.0212 0.0093  0.0116  203 A1A8Z A C6  
6596 C  C7  C A1A8Z E .   ? 0.1969 0.2148 0.2226 -0.0219 0.0087  0.0126  203 A1A8Z A C7  
6597 C  C8  C A1A8Z E .   ? 0.1967 0.2144 0.2215 -0.0234 0.0112  0.0097  203 A1A8Z A C8  
6598 C  C10 C A1A8Z E .   ? 0.1781 0.1946 0.1899 -0.0134 -0.0033 0.0017  203 A1A8Z A C10 
6599 C  C11 C A1A8Z E .   ? 0.1779 0.1932 0.1872 -0.0110 -0.0071 0.0000  203 A1A8Z A C11 
6600 C  C12 C A1A8Z E .   ? 0.1716 0.1892 0.1777 -0.0093 -0.0080 0.0021  203 A1A8Z A C12 
6601 C  C13 C A1A8Z E .   ? 0.1732 0.1916 0.1804 -0.0109 -0.0056 0.0029  203 A1A8Z A C13 
6602 C  C14 C A1A8Z E .   ? 0.1683 0.1895 0.1746 -0.0099 -0.0061 0.0048  203 A1A8Z A C14 
6603 C  C15 C A1A8Z E .   ? 0.1647 0.1859 0.1723 -0.0104 -0.0090 0.0054  203 A1A8Z A C15 
6604 C  C9  C A1A8Z E .   ? 0.1944 0.2126 0.2199 -0.0228 0.0122  0.0066  203 A1A8Z A C9  
6605 F  F1  C A1A8Z E .   ? 0.1968 0.2158 0.2237 -0.0197 0.0046  0.0157  203 A1A8Z A F1  
6606 N  N1  C A1A8Z E .   ? 0.1816 0.1979 0.1998 -0.0157 0.0010  0.0027  203 A1A8Z A N1  
6607 N  N2  C A1A8Z E .   ? 0.1782 0.1938 0.1893 -0.0132 -0.0056 -0.0013 203 A1A8Z A N2  
6608 N  N3  C A1A8Z E .   ? 0.1763 0.1918 0.1839 -0.0099 -0.0082 0.0015  203 A1A8Z A N3  
6609 N  N4  C A1A8Z E .   ? 0.1652 0.1846 0.1699 -0.0083 -0.0094 0.0056  203 A1A8Z A N4  
6625 CL CL  B CL    F .   ? 0.1766 0.1494 0.2581 -0.0106 -0.0109 -0.0161 204 CL    A CL  
6626 O  O   . HOH   G .   ? 0.4215 0.8093 0.5303 -0.1185 0.0853  0.1032  301 HOH   A O   
6627 O  O   . HOH   G .   ? 0.2397 0.2246 0.3741 -0.0229 -0.0278 0.0468  302 HOH   A O   
6628 O  O   . HOH   G .   ? 0.6862 0.5646 0.3943 -0.1474 0.0021  0.1897  303 HOH   A O   
6629 O  O   . HOH   G .   ? 0.4656 0.3637 0.4413 -0.0244 0.1337  -0.0385 304 HOH   A O   
6630 O  O   . HOH   G .   ? 0.2977 0.2684 0.4302 -0.0347 -0.1263 0.1217  305 HOH   A O   
6631 O  O   . HOH   G .   ? 0.2105 0.2348 0.2432 -0.0165 0.0383  0.0536  306 HOH   A O   
6632 O  O   . HOH   G .   ? 0.6348 0.4834 0.3161 0.1964  -0.1367 0.0342  307 HOH   A O   
6633 O  O   . HOH   G .   ? 0.2956 0.6250 0.5569 -0.0451 -0.0907 0.1919  308 HOH   A O   
6634 O  O   . HOH   G .   ? 0.5923 0.4107 0.5265 0.0661  -0.0501 0.0203  309 HOH   A O   
6635 O  O   . HOH   G .   ? 0.2852 0.3545 0.1831 -0.0415 0.0479  0.0562  310 HOH   A O   
6636 O  O   . HOH   G .   ? 0.5140 0.2482 0.3131 -0.1096 0.0688  0.0300  311 HOH   A O   
6637 O  O   . HOH   G .   ? 0.3494 0.3367 0.2784 -0.1188 0.0170  0.0831  312 HOH   A O   
6638 O  O   . HOH   G .   ? 0.1905 0.3531 0.4068 -0.0325 0.0381  -0.1043 313 HOH   A O   
6639 O  O   . HOH   G .   ? 0.5761 0.4153 0.5459 -0.0868 0.1491  0.1057  314 HOH   A O   
6640 O  O   . HOH   G .   ? 0.2105 0.1840 0.3618 -0.0470 0.0167  -0.0256 315 HOH   A O   
6641 O  O   B HOH   G .   ? 0.3657 0.2983 0.3199 -0.0147 0.0137  -0.0116 316 HOH   A O   
6642 O  O   . HOH   G .   ? 0.5311 0.3305 0.2883 -0.0781 -0.0608 0.0199  317 HOH   A O   
6643 O  O   . HOH   G .   ? 0.6213 0.5796 0.3614 -0.0578 -0.0441 0.1449  318 HOH   A O   
6644 O  O   . HOH   G .   ? 0.1756 0.3142 0.3081 0.0313  -0.0205 -0.0029 319 HOH   A O   
6645 O  O   . HOH   G .   ? 0.4733 0.3949 0.4377 -0.1881 -0.1066 0.1971  320 HOH   A O   
6646 O  O   . HOH   G .   ? 0.4584 0.4910 0.5871 0.1408  0.1199  -0.1034 321 HOH   A O   
6647 O  O   A HOH   G .   ? 0.1325 0.1973 0.1946 0.0340  0.0352  0.0463  322 HOH   A O   
6648 O  O   . HOH   G .   ? 0.4553 0.4492 0.5143 -0.0650 0.0856  0.1994  323 HOH   A O   
6649 O  O   . HOH   G .   ? 0.4877 0.5394 0.4337 -0.0605 -0.0250 -0.1100 324 HOH   A O   
6650 O  O   . HOH   G .   ? 0.1590 0.1853 0.2655 0.0165  -0.0425 -0.0685 325 HOH   A O   
6651 O  O   . HOH   G .   ? 0.1751 0.1651 0.2190 0.0165  -0.0259 0.0288  326 HOH   A O   
6652 O  O   . HOH   G .   ? 0.2630 0.4866 0.3854 0.0156  -0.0521 0.0310  327 HOH   A O   
6653 O  O   . HOH   G .   ? 0.1524 0.1478 0.2351 -0.0223 0.0063  0.0084  328 HOH   A O   
6654 O  O   . HOH   G .   ? 0.2052 0.4654 0.4084 -0.0399 -0.0615 0.2048  329 HOH   A O   
6655 O  O   B HOH   G .   ? 0.1807 0.2844 0.3257 -0.0485 0.0256  -0.0230 330 HOH   A O   
6656 O  O   . HOH   G .   ? 0.4633 0.2028 0.5297 0.0483  0.0298  0.0050  331 HOH   A O   
6657 O  O   . HOH   G .   ? 0.3341 0.3903 0.3947 -0.0849 0.1535  0.0145  332 HOH   A O   
6658 O  O   . HOH   G .   ? 0.1921 0.1619 0.1679 -0.0089 0.0182  0.0269  333 HOH   A O   
6659 O  O   . HOH   G .   ? 0.2274 0.2226 0.2794 0.0405  0.0252  0.0443  334 HOH   A O   
6660 O  O   . HOH   G .   ? 0.3248 0.4297 0.2740 -0.0278 0.0623  0.0307  335 HOH   A O   
6661 O  O   . HOH   G .   ? 0.4834 0.1963 0.4395 0.0074  -0.1783 0.0642  336 HOH   A O   
6662 O  O   . HOH   G .   ? 0.5189 0.5183 0.4864 0.0472  0.2192  -0.0944 337 HOH   A O   
6663 O  O   . HOH   G .   ? 0.2202 0.1706 0.2500 -0.0044 -0.0521 -0.0003 338 HOH   A O   
6664 O  O   . HOH   G .   ? 0.5498 0.5960 0.5145 -0.1251 -0.1221 -0.0850 339 HOH   A O   
6665 O  O   . HOH   G .   ? 0.2730 0.3438 0.3956 -0.0832 -0.0689 -0.0520 340 HOH   A O   
6666 O  O   . HOH   G .   ? 0.1928 0.2179 0.2846 -0.0121 -0.0307 0.0869  341 HOH   A O   
6667 O  O   A HOH   G .   ? 0.2236 0.4750 0.5115 0.0500  0.0476  0.0543  342 HOH   A O   
6668 O  O   . HOH   G .   ? 0.2219 0.4049 0.3594 0.0961  -0.0671 -0.0331 343 HOH   A O   
6669 O  O   . HOH   G .   ? 0.6097 0.6001 0.4171 0.1966  -0.0271 -0.0043 344 HOH   A O   
6670 O  O   . HOH   G .   ? 0.2194 0.2302 0.2670 0.0157  -0.0070 0.0622  345 HOH   A O   
6671 O  O   . HOH   G .   ? 0.4896 0.5211 0.2786 -0.1428 0.1242  0.0699  346 HOH   A O   
6672 O  O   . HOH   G .   ? 0.1623 0.1696 0.1917 0.0032  -0.0253 0.0082  347 HOH   A O   
6673 O  O   A HOH   G .   ? 0.2189 0.2788 0.4087 0.0313  0.1131  0.1613  348 HOH   A O   
6674 O  O   . HOH   G .   ? 0.1435 0.2049 0.2311 0.0023  -0.0061 0.0456  349 HOH   A O   
6675 O  O   A HOH   G .   ? 0.1785 0.2089 0.2193 0.0169  0.0153  0.0107  350 HOH   A O   
6676 O  O   . HOH   G .   ? 0.2550 0.2216 0.2508 -0.0222 -0.0061 -0.0201 351 HOH   A O   
6677 O  O   . HOH   G .   ? 0.1954 0.1962 0.4090 0.0196  0.1022  -0.0140 352 HOH   A O   
6678 O  O   . HOH   G .   ? 0.5252 0.5308 0.5232 -0.0104 0.0999  0.0372  353 HOH   A O   
6679 O  O   . HOH   G .   ? 0.1466 0.3748 0.2629 0.0033  0.0267  0.0685  354 HOH   A O   
6680 O  O   . HOH   G .   ? 0.3119 0.3540 0.4789 -0.0911 -0.1011 -0.0779 355 HOH   A O   
6681 O  O   . HOH   G .   ? 0.3243 0.2927 0.3405 -0.0911 -0.0023 -0.0162 356 HOH   A O   
6682 O  O   . HOH   G .   ? 0.2172 0.1710 0.2461 0.0278  -0.0344 0.0013  357 HOH   A O   
6683 O  O   . HOH   G .   ? 0.3561 0.4053 0.4155 0.1827  0.0637  0.0479  358 HOH   A O   
6684 O  O   . HOH   G .   ? 0.1755 0.2302 0.2672 -0.0268 0.0570  0.0485  359 HOH   A O   
6685 O  O   . HOH   G .   ? 0.1299 0.1269 0.1384 -0.0021 0.0149  0.0118  360 HOH   A O   
6686 O  O   A HOH   G .   ? 0.3221 0.1464 0.1820 0.0197  0.0195  0.0142  361 HOH   A O   
6687 O  O   . HOH   G .   ? 0.1478 0.1872 0.2600 0.0061  -0.0082 0.0127  362 HOH   A O   
6688 O  O   . HOH   G .   ? 0.3253 0.3801 0.2212 -0.1215 -0.0160 -0.0597 363 HOH   A O   
6689 O  O   . HOH   G .   ? 0.1750 0.2174 0.1847 -0.0207 -0.0014 0.0651  364 HOH   A O   
6690 O  O   . HOH   G .   ? 0.1560 0.1313 0.2297 -0.0107 0.0165  -0.0105 365 HOH   A O   
6691 O  O   . HOH   G .   ? 0.3745 0.2049 0.2462 0.1005  0.0466  0.0406  366 HOH   A O   
6692 O  O   . HOH   G .   ? 0.2683 0.3999 0.3428 -0.0470 0.0717  0.0135  367 HOH   A O   
6693 O  O   . HOH   G .   ? 0.1414 0.1508 0.1658 -0.0096 -0.0108 -0.0023 368 HOH   A O   
6694 O  O   . HOH   G .   ? 0.5736 0.3921 0.3329 0.0063  -0.0173 0.1611  369 HOH   A O   
6695 O  O   . HOH   G .   ? 0.4127 0.2511 0.3778 -0.1446 0.1112  -0.0354 370 HOH   A O   
6696 O  O   . HOH   G .   ? 0.7563 0.3790 0.5327 -0.0759 -0.1337 0.0345  371 HOH   A O   
6697 O  O   . HOH   G .   ? 0.3622 0.6910 0.4719 -0.0612 -0.1253 0.0632  372 HOH   A O   
6698 O  O   . HOH   G .   ? 0.1853 0.1870 0.2473 -0.0288 0.0009  0.0407  373 HOH   A O   
6699 O  O   . HOH   G .   ? 0.1913 0.2430 0.3408 0.0196  0.0708  -0.0596 374 HOH   A O   
6700 O  O   . HOH   G .   ? 0.3767 0.2512 0.4315 -0.1155 0.0926  0.0389  375 HOH   A O   
6701 O  O   T HOH   G .   ? 0.1169 0.1208 0.2704 -0.0207 0.0095  0.0408  376 HOH   A O   
6702 O  O   . HOH   G .   ? 0.3351 0.2607 0.3204 -0.0232 -0.0404 0.0993  377 HOH   A O   
6703 O  O   . HOH   G .   ? 0.2724 0.4504 0.3100 0.0543  0.0758  0.1997  378 HOH   A O   
6704 O  O   . HOH   G .   ? 0.2549 0.2116 0.1761 -0.0730 -0.0005 0.0352  379 HOH   A O   
6705 O  O   . HOH   G .   ? 0.1881 0.2761 0.2790 0.0439  0.0467  0.1000  380 HOH   A O   
6706 O  O   . HOH   G .   ? 0.2303 0.4451 0.3824 -0.0336 -0.0005 0.1161  381 HOH   A O   
6707 O  O   . HOH   G .   ? 0.2899 0.2441 0.4777 -0.0578 -0.0254 0.0067  382 HOH   A O   
6708 O  O   B HOH   G .   ? 0.2882 0.1878 0.2487 0.0105  -0.0154 -0.0151 383 HOH   A O   
6709 O  O   . HOH   G .   ? 0.3179 0.3736 0.3399 -0.1536 0.0858  -0.0122 384 HOH   A O   
6710 O  O   A HOH   G .   ? 0.2310 0.2208 0.1652 0.0780  0.0787  0.0528  385 HOH   A O   
6711 O  O   . HOH   G .   ? 0.3033 0.2842 0.2230 0.0266  0.0804  0.0142  386 HOH   A O   
6712 O  O   . HOH   G .   ? 0.3478 0.6624 0.4186 -0.0915 -0.0118 0.1570  387 HOH   A O   
6713 O  O   . HOH   G .   ? 0.1924 0.2374 0.2440 -0.0381 -0.0426 0.0545  388 HOH   A O   
6714 O  O   . HOH   G .   ? 0.1642 0.1679 0.2319 -0.0202 0.0106  0.0359  389 HOH   A O   
6715 O  O   . HOH   G .   ? 0.3056 0.6325 0.3491 0.1300  0.0506  -0.0790 390 HOH   A O   
6716 O  O   . HOH   G .   ? 0.1872 0.2007 0.1760 0.0063  0.0143  0.0224  391 HOH   A O   
6717 O  O   . HOH   G .   ? 0.2705 0.3267 0.3027 -0.0467 0.0892  -0.0421 392 HOH   A O   
6718 O  O   . HOH   G .   ? 0.1816 0.1932 0.3839 0.0385  0.0956  0.1079  393 HOH   A O   
6719 O  O   . HOH   G .   ? 0.3327 0.5023 0.5095 0.1000  0.0717  0.0369  394 HOH   A O   
6720 O  O   . HOH   G .   ? 0.2010 0.2051 0.3221 -0.0034 -0.0484 0.0387  395 HOH   A O   
6721 O  O   . HOH   G .   ? 0.1468 0.1761 0.1863 0.0133  -0.0285 -0.0338 396 HOH   A O   
6722 O  O   . HOH   G .   ? 0.2472 0.3971 0.3903 -0.0284 0.0919  -0.0936 397 HOH   A O   
6723 O  O   . HOH   G .   ? 0.3142 0.2519 0.2241 -0.0684 -0.0879 0.0303  398 HOH   A O   
6724 O  O   . HOH   G .   ? 0.2421 0.1776 0.2646 0.0006  0.0168  0.0297  399 HOH   A O   
6725 O  O   . HOH   G .   ? 0.1299 0.1423 0.1962 -0.0002 -0.0151 0.0083  400 HOH   A O   
6726 O  O   . HOH   G .   ? 0.4462 0.4982 0.3414 0.2383  0.0063  -0.0736 401 HOH   A O   
6727 O  O   . HOH   G .   ? 0.5335 0.3624 0.5528 0.0517  0.1551  -0.1382 402 HOH   A O   
6728 O  O   . HOH   G .   ? 0.3043 0.3699 0.3688 -0.0680 0.1398  0.0095  403 HOH   A O   
6729 O  O   . HOH   G .   ? 0.2614 0.2857 0.3021 0.0023  -0.0355 -0.0593 404 HOH   A O   
6730 O  O   . HOH   G .   ? 0.6765 0.5933 0.4410 -0.1064 0.0194  0.2501  405 HOH   A O   
6731 O  O   . HOH   G .   ? 0.5579 0.5610 0.6377 -0.1022 0.0018  0.1618  406 HOH   A O   
6732 O  O   . HOH   G .   ? 0.3659 0.5702 0.5416 -0.0165 -0.0760 0.1994  407 HOH   A O   
6733 O  O   A HOH   G .   ? 0.1781 0.1722 0.3027 -0.0167 0.0347  0.0022  408 HOH   A O   
6734 O  O   . HOH   G .   ? 0.4717 0.4616 0.2186 -0.0191 0.0926  0.0885  409 HOH   A O   
6735 O  O   . HOH   G .   ? 0.4389 0.4701 0.3926 0.1668  -0.1220 -0.1617 410 HOH   A O   
6736 O  O   . HOH   G .   ? 0.1856 0.2563 0.3973 -0.0113 -0.0340 0.0247  411 HOH   A O   
6737 O  O   . HOH   G .   ? 0.5976 0.4074 0.4804 0.1793  -0.0931 0.1560  412 HOH   A O   
6738 O  O   . HOH   G .   ? 0.2118 0.1715 0.3096 0.0040  -0.0326 0.0068  413 HOH   A O   
6739 O  O   . HOH   G .   ? 0.1514 0.1604 0.3293 -0.0030 -0.0026 0.0263  414 HOH   A O   
6740 O  O   . HOH   G .   ? 0.5220 0.6040 0.5799 0.0597  0.1011  0.0679  415 HOH   A O   
6741 O  O   . HOH   G .   ? 0.2689 0.3578 0.7076 -0.0310 0.0749  -0.0478 416 HOH   A O   
6742 O  O   . HOH   G .   ? 0.1683 0.1357 0.1710 -0.0229 0.0124  0.0025  417 HOH   A O   
6743 O  O   . HOH   G .   ? 0.5258 0.2708 0.5088 0.0690  0.0205  0.0185  418 HOH   A O   
6744 O  O   . HOH   G .   ? 0.2017 0.2975 0.2530 -0.0170 -0.0526 0.0676  419 HOH   A O   
6745 O  O   . HOH   G .   ? 0.3026 0.3572 0.2054 -0.0287 -0.0646 0.0409  420 HOH   A O   
6746 O  O   . HOH   G .   ? 0.2439 0.2166 0.2773 -0.0594 -0.0070 0.0728  421 HOH   A O   
6747 O  O   . HOH   G .   ? 0.2804 0.6088 0.1746 -0.0317 0.0419  0.0077  422 HOH   A O   
6748 O  O   . HOH   G .   ? 0.5067 0.6204 0.3317 -0.1018 0.0108  0.1422  423 HOH   A O   
6749 O  O   . HOH   G .   ? 0.3226 0.1232 0.2205 0.0064  -0.0606 0.0093  424 HOH   A O   
6750 O  O   . HOH   G .   ? 0.2290 0.4116 0.2536 0.1402  0.0015  0.0261  425 HOH   A O   
6751 O  O   . HOH   G .   ? 0.4079 0.2369 0.5722 -0.0831 -0.2370 0.1227  426 HOH   A O   
6752 O  O   . HOH   G .   ? 0.5649 0.6366 0.6810 -0.1422 -0.0598 -0.0730 427 HOH   A O   
6753 O  O   . HOH   G .   ? 0.1615 0.1983 0.2741 -0.0127 0.0051  0.0418  428 HOH   A O   
6754 O  O   . HOH   G .   ? 0.2033 0.2286 0.4049 0.0029  -0.0394 -0.0546 429 HOH   A O   
6755 O  O   . HOH   G .   ? 0.6413 0.7150 0.4316 0.0959  0.2788  -0.0712 430 HOH   A O   
6756 O  O   . HOH   G .   ? 0.3206 0.3321 0.2361 -0.0701 -0.0635 0.0452  431 HOH   A O   
6757 O  O   . HOH   G .   ? 0.1935 0.1711 0.2812 0.0213  -0.0554 0.0132  432 HOH   A O   
6758 O  O   . HOH   G .   ? 0.5328 0.7493 0.3943 0.1452  -0.0897 0.1948  433 HOH   A O   
6759 O  O   . HOH   G .   ? 0.8169 0.3338 0.4873 0.0466  0.1434  0.1563  434 HOH   A O   
6760 O  O   . HOH   G .   ? 0.8848 0.8991 0.7391 -0.0041 0.0242  -0.0422 435 HOH   A O   
6761 O  O   . HOH   G .   ? 0.1799 0.2214 0.4703 -0.0228 -0.0839 0.0686  436 HOH   A O   
6762 O  O   . HOH   G .   ? 0.2524 0.1644 0.2891 0.0129  0.0129  0.0168  437 HOH   A O   
6763 O  O   . HOH   G .   ? 0.3537 0.2937 0.1870 -0.0840 0.0227  0.0680  438 HOH   A O   
6764 O  O   . HOH   G .   ? 0.4729 0.4701 0.5057 -0.1256 -0.0966 -0.1169 439 HOH   A O   
6765 O  O   . HOH   G .   ? 0.3851 0.3557 0.3002 0.2160  -0.0656 -0.0443 440 HOH   A O   
6766 O  O   . HOH   G .   ? 0.2818 0.4339 0.5264 -0.0052 0.1127  -0.1796 441 HOH   A O   
6767 O  O   . HOH   G .   ? 0.1651 0.1549 0.1736 -0.0028 -0.0122 -0.0063 442 HOH   A O   
6768 O  O   A HOH   G .   ? 0.2536 0.2200 0.2660 -0.0081 -0.0437 0.0155  443 HOH   A O   
6769 O  O   . HOH   G .   ? 0.5346 0.5025 0.3729 -0.0495 -0.1445 0.0314  444 HOH   A O   
6770 O  O   . HOH   G .   ? 0.5652 0.3126 0.5789 0.0405  0.0984  -0.1002 445 HOH   A O   
6771 O  O   . HOH   G .   ? 0.2120 0.1992 0.2907 0.0085  0.0138  0.0238  446 HOH   A O   
6772 O  O   . HOH   G .   ? 0.6582 0.5614 0.7324 0.1700  -0.1137 0.1747  447 HOH   A O   
6773 O  O   . HOH   G .   ? 0.6284 0.6358 0.7147 -0.1409 -0.0426 -0.1306 448 HOH   A O   
6774 O  O   A HOH   G .   ? 0.2351 0.1592 0.2317 -0.0251 -0.0178 0.0610  449 HOH   A O   
6775 O  O   . HOH   G .   ? 0.2143 0.2768 0.2675 0.0083  -0.0164 -0.0490 450 HOH   A O   
6776 O  O   . HOH   G .   ? 0.7117 0.6191 0.6511 0.0467  -0.1205 -0.0269 451 HOH   A O   
6777 O  O   . HOH   G .   ? 0.4775 0.4953 0.4465 0.0509  0.0083  0.0735  452 HOH   A O   
6778 O  O   B HOH   G .   ? 0.3129 0.3450 0.3335 0.0451  0.0998  0.0313  453 HOH   A O   
6779 O  O   . HOH   G .   ? 0.5267 0.4492 0.4040 -0.0589 0.0718  0.0345  454 HOH   A O   
6780 O  O   . HOH   G .   ? 0.6346 0.5932 0.4542 -0.0957 0.0851  0.0881  455 HOH   A O   
6781 O  O   . HOH   G .   ? 0.3696 0.3497 0.3956 0.0164  0.0366  0.0278  456 HOH   A O   
6782 O  O   . HOH   G .   ? 0.3509 0.4293 0.4083 0.1698  -0.0530 0.0928  457 HOH   A O   
6783 O  O   . HOH   G .   ? 0.7333 0.8294 0.5064 0.1010  -0.1182 0.0312  458 HOH   A O   
6784 O  O   . HOH   G .   ? 0.2643 0.2695 0.3432 -0.0465 0.0274  -0.0684 459 HOH   A O   
6785 O  O   . HOH   G .   ? 0.3194 0.5016 0.5230 -0.1537 0.0787  -0.1458 460 HOH   A O   
6786 O  O   . HOH   G .   ? 0.3906 0.4984 0.4703 0.0602  -0.0177 0.1079  461 HOH   A O   
6787 O  O   . HOH   G .   ? 0.3470 0.4892 0.4258 -0.0982 0.0010  0.0121  462 HOH   A O   
6788 O  O   . HOH   G .   ? 0.2651 0.2812 0.3608 -0.1024 0.0641  -0.0297 463 HOH   A O   
6789 O  O   . HOH   G .   ? 0.2923 0.2662 0.5845 0.0679  -0.1654 -0.0722 464 HOH   A O   
6790 O  O   . HOH   G .   ? 0.2627 0.4358 0.5348 0.0534  0.0053  -0.1868 465 HOH   A O   
6791 O  O   . HOH   G .   ? 0.6663 0.6175 0.6481 0.0354  0.1395  0.1728  466 HOH   A O   
6792 O  O   . HOH   G .   ? 0.6276 0.3527 0.6395 0.0863  0.0134  0.2015  467 HOH   A O   
6793 O  O   . HOH   G .   ? 0.4040 0.6226 0.3762 -0.0944 -0.0952 0.2207  468 HOH   A O   
6794 O  O   . HOH   G .   ? 0.5358 0.4760 0.4859 0.0079  0.0852  0.0575  469 HOH   A O   
6795 O  O   . HOH   G .   ? 0.3841 0.2518 0.3623 0.0271  0.1034  -0.0070 470 HOH   A O   
6796 O  O   . HOH   G .   ? 0.2547 0.1707 0.2638 0.0228  -0.0749 -0.0290 471 HOH   A O   
6797 O  O   . HOH   G .   ? 0.4140 0.5255 0.3790 0.0600  -0.0757 -0.0967 472 HOH   A O   
6798 O  O   . HOH   G .   ? 0.4273 0.4956 0.3180 -0.0320 -0.0570 -0.0304 473 HOH   A O   
6799 O  O   . HOH   G .   ? 0.2478 0.2254 0.2567 0.0191  -0.0114 0.0063  474 HOH   A O   
6800 O  O   . HOH   G .   ? 0.4986 0.5138 0.4688 0.0392  -0.0932 -0.0703 475 HOH   A O   
6801 O  O   . HOH   G .   ? 0.5201 0.5597 0.5996 -0.1663 -0.1294 -0.0676 476 HOH   A O   
6802 O  O   . HOH   G .   ? 0.4280 0.4873 0.2656 0.0427  -0.0082 0.0045  477 HOH   A O   
6803 O  O   . HOH   G .   ? 0.4586 0.4359 0.5182 -0.1928 -0.0546 -0.0368 478 HOH   A O   
6804 O  O   . HOH   G .   ? 0.6599 0.5932 0.6772 -0.1090 0.0500  -0.1182 479 HOH   A O   
6805 O  O   . HOH   G .   ? 0.4352 0.2771 0.3460 -0.0776 -0.1346 0.0588  480 HOH   A O   
6806 O  O   . HOH   G .   ? 0.5463 0.4410 0.4451 -0.0068 0.0013  -0.1147 481 HOH   A O   
6807 O  O   . HOH   G .   ? 0.5977 0.3646 0.4182 -0.0179 0.1041  -0.0387 482 HOH   A O   
6808 O  O   . HOH   G .   ? 0.8254 0.3926 0.3253 -0.0421 -0.1269 0.0243  483 HOH   A O   
6809 O  O   . HOH   G .   ? 0.3234 0.3566 0.5167 -0.0061 0.1536  0.0980  484 HOH   A O   
6810 O  O   . HOH   G .   ? 0.6003 0.7081 0.4830 -0.1030 0.1293  0.1373  485 HOH   A O   
6811 O  O   . HOH   G .   ? 0.2738 0.5137 0.3736 0.1056  0.1162  0.2261  486 HOH   A O   
6812 O  O   . HOH   G .   ? 0.2880 0.4535 0.3483 -0.0212 -0.0310 -0.0959 487 HOH   A O   
6813 O  O   . HOH   G .   ? 0.5874 0.5975 0.6567 0.0742  0.2362  -0.1177 488 HOH   A O   
6814 O  O   . HOH   G .   ? 0.5198 0.5088 0.5927 0.0461  -0.0775 0.0940  489 HOH   A O   
6815 O  O   . HOH   G .   ? 0.2540 0.2556 0.6957 -0.0075 -0.1361 0.0413  490 HOH   A O   
6816 O  O   . HOH   G .   ? 0.4097 0.3213 0.4637 -0.1074 -0.0058 0.1094  491 HOH   A O   
6817 O  O   . HOH   G .   ? 0.4654 0.4194 0.2668 -0.1457 0.1440  -0.0711 492 HOH   A O   
6818 O  O   . HOH   G .   ? 0.6026 0.4602 0.5082 -0.0422 -0.1216 -0.0821 493 HOH   A O   
6819 O  O   . HOH   G .   ? 0.4746 0.3112 0.4907 -0.0194 0.2289  0.0228  494 HOH   A O   
6820 O  O   . HOH   G .   ? 0.5547 0.2651 0.4067 -0.0770 0.0679  0.0594  495 HOH   A O   
6821 O  O   . HOH   G .   ? 0.2905 0.2222 0.5148 0.0097  0.0286  0.0954  496 HOH   A O   
6822 O  O   . HOH   G .   ? 0.2702 0.2917 0.4720 -0.0120 0.1061  -0.0374 497 HOH   A O   
6823 O  O   . HOH   G .   ? 0.2606 0.3953 0.3372 0.0825  -0.0472 0.0691  498 HOH   A O   
6824 O  O   . HOH   G .   ? 0.4008 0.7543 0.5771 -0.1270 -0.0707 0.1903  499 HOH   A O   
6825 O  O   . HOH   G .   ? 0.4840 0.3119 0.4340 -0.1800 -0.0343 0.0581  500 HOH   A O   
6826 O  O   . HOH   G .   ? 0.6376 0.5899 0.4917 0.1781  -0.1410 -0.0286 501 HOH   A O   
6827 O  O   . HOH   G .   ? 0.2914 0.4181 0.4571 0.0396  -0.0575 0.0071  502 HOH   A O   
6828 O  O   . HOH   G .   ? 0.5811 0.7473 0.5069 0.0943  -0.1015 0.0837  503 HOH   A O   
6829 O  O   . HOH   G .   ? 0.6376 0.3853 0.4973 0.1979  0.0003  0.0840  504 HOH   A O   
6830 O  O   B HOH   G .   ? 0.2484 0.3558 0.3058 0.0401  0.0666  0.0543  505 HOH   A O   
6831 O  O   . HOH   G .   ? 0.2776 0.2443 0.4732 0.0192  0.0079  0.0795  506 HOH   A O   
6832 O  O   . HOH   G .   ? 0.5333 0.6766 0.5433 0.3141  0.0148  0.1578  507 HOH   A O   
6833 O  O   T HOH   G .   ? 0.1127 0.1427 0.2488 -0.0188 -0.0174 0.0677  508 HOH   A O   
6834 O  O   A HOH   G .   ? 0.4378 0.7639 0.4174 0.2030  0.0338  -0.0110 509 HOH   A O   
6835 O  O   . HOH   G .   ? 0.2530 0.6372 0.4541 0.0050  0.0426  -0.0866 510 HOH   A O   
6836 O  O   . HOH   G .   ? 0.5581 0.6319 0.4734 -0.0575 -0.0157 -0.1065 511 HOH   A O   
6837 O  O   . HOH   G .   ? 0.4867 0.7306 0.5499 -0.0523 -0.0899 0.0807  512 HOH   A O   
6838 O  O   . HOH   G .   ? 0.4489 0.4717 0.4906 0.1257  0.0105  0.1350  513 HOH   A O   
6839 O  O   . HOH   G .   ? 0.2667 0.4398 0.5883 -0.0091 -0.0728 0.2739  514 HOH   A O   
6840 O  O   . HOH   H .   ? 0.2212 0.2196 0.3223 0.0122  0.0617  0.0453  201 HOH   B O   
6841 O  O   . HOH   H .   ? 0.4703 0.3397 0.4059 -0.0195 -0.0008 -0.1444 202 HOH   B O   
6842 O  O   . HOH   H .   ? 0.3075 0.6758 0.3572 0.0428  0.0146  0.2199  203 HOH   B O   
6843 O  O   . HOH   H .   ? 0.4509 0.5478 0.2936 0.0228  -0.0188 -0.1466 204 HOH   B O   
6844 O  O   . HOH   H .   ? 0.7282 0.3548 0.4358 0.1162  0.0967  0.0219  205 HOH   B O   
6845 O  O   . HOH   H .   ? 0.3504 0.4012 0.4989 -0.0796 0.0013  -0.1266 206 HOH   B O   
6846 O  O   . HOH   H .   ? 0.6081 0.6124 0.5947 0.1523  0.0739  -0.0085 207 HOH   B O   
6847 O  O   . HOH   H .   ? 0.3555 0.3825 0.6135 -0.0728 0.0324  -0.0357 208 HOH   B O   
6848 O  O   . HOH   H .   ? 0.1576 0.1973 0.2989 -0.0152 -0.0094 0.0094  209 HOH   B O   
6849 O  O   . HOH   H .   ? 0.1903 0.2239 0.3281 0.0045  0.0282  -0.0342 210 HOH   B O   
6850 O  O   . HOH   H .   ? 0.2856 0.2000 0.5568 0.0227  0.1825  0.0899  211 HOH   B O   
6851 O  O   . HOH   H .   ? 0.2687 0.2864 0.6363 0.0514  -0.0945 0.0442  212 HOH   B O   
6852 O  O   . HOH   H .   ? 0.3106 0.5616 0.5362 0.0019  0.1829  -0.1623 213 HOH   B O   
6853 O  O   . HOH   H .   ? 0.3119 0.2367 0.5085 0.0028  0.1820  0.0433  214 HOH   B O   
6854 O  O   . HOH   H .   ? 0.4374 0.5898 0.4263 0.2675  -0.1100 -0.0057 215 HOH   B O   
6855 O  O   . HOH   H .   ? 0.4239 0.4582 0.4023 0.0244  0.0866  -0.1690 216 HOH   B O   
6856 O  O   . HOH   H .   ? 0.4511 0.5562 0.3756 0.2633  -0.0239 0.0055  217 HOH   B O   
6857 O  O   . HOH   H .   ? 0.3599 0.5293 0.4544 0.2292  0.0396  -0.0144 218 HOH   B O   
6858 O  O   . HOH   H .   ? 0.4470 0.4226 0.6473 -0.0268 -0.1597 -0.0979 219 HOH   B O   
6859 O  O   . HOH   H .   ? 0.4414 0.3662 0.3718 0.0273  -0.1161 0.0317  220 HOH   B O   
6860 O  O   . HOH   H .   ? 0.4925 0.4269 0.5974 0.0384  -0.0969 0.2693  221 HOH   B O   
6861 O  O   . HOH   H .   ? 0.3139 0.3386 0.4579 0.0475  -0.0747 0.0397  222 HOH   B O   
6862 O  O   . HOH   H .   ? 0.5662 0.2904 0.3537 -0.1626 0.0102  0.0283  223 HOH   B O   
6863 O  O   . HOH   H .   ? 0.4773 0.2075 0.2972 0.0002  -0.1140 0.0061  224 HOH   B O   
6864 O  O   . HOH   H .   ? 0.4331 0.6080 0.3706 0.1901  0.0559  -0.0001 225 HOH   B O   
6865 O  O   . HOH   H .   ? 0.1747 0.2127 0.3259 -0.0181 0.0084  -0.0075 226 HOH   B O   
6866 O  O   . HOH   H .   ? 0.2396 0.1760 0.2766 -0.0350 0.0904  -0.0135 227 HOH   B O   
6867 O  O   . HOH   H .   ? 0.6583 0.3666 0.2529 -0.0409 0.0549  -0.0026 228 HOH   B O   
6868 O  O   . HOH   H .   ? 0.3544 0.1738 0.2097 0.0175  -0.0824 -0.0124 229 HOH   B O   
6869 O  O   . HOH   H .   ? 0.2233 0.2178 0.3987 -0.0414 0.0063  -0.0522 230 HOH   B O   
6870 O  O   . HOH   H .   ? 0.2766 0.3366 0.3145 -0.0712 0.0359  0.0027  231 HOH   B O   
6871 O  O   . HOH   H .   ? 0.3997 0.2518 0.3998 0.0889  -0.0256 -0.0579 232 HOH   B O   
6872 O  O   . HOH   H .   ? 0.2166 0.2583 0.3228 -0.0577 0.0073  -0.0303 233 HOH   B O   
6873 O  O   . HOH   H .   ? 0.6238 0.6863 0.3346 0.0296  -0.0146 0.0433  234 HOH   B O   
6874 O  O   . HOH   H .   ? 0.3863 0.4492 0.4956 -0.1620 0.0028  0.0581  235 HOH   B O   
6875 O  O   . HOH   H .   ? 0.4764 0.3214 0.3917 -0.2239 -0.0323 0.0288  236 HOH   B O   
6876 O  O   . HOH   H .   ? 0.3672 0.3772 0.5902 0.0043  0.0673  -0.0258 237 HOH   B O   
6877 O  O   . HOH   H .   ? 0.1492 0.1402 0.1606 -0.0103 -0.0041 0.0019  238 HOH   B O   
6878 O  O   . HOH   H .   ? 0.3446 0.3030 0.2325 0.0406  0.0566  0.0429  239 HOH   B O   
6879 O  O   . HOH   H .   ? 0.1971 0.1337 0.3421 0.0088  -0.0560 -0.0118 240 HOH   B O   
6880 O  O   . HOH   H .   ? 0.3548 0.2611 0.4344 0.0471  -0.0988 -0.1368 241 HOH   B O   
6881 O  O   . HOH   H .   ? 0.7414 0.4997 0.4726 0.1924  -0.0176 -0.1202 242 HOH   B O   
6882 O  O   . HOH   H .   ? 0.1602 0.1431 0.2731 -0.0046 -0.0015 -0.0024 243 HOH   B O   
6883 O  O   . HOH   H .   ? 0.3188 0.4196 0.2177 0.0212  0.0795  0.0408  244 HOH   B O   
6884 O  O   . HOH   H .   ? 0.1471 0.1270 0.1719 0.0015  -0.0084 0.0123  245 HOH   B O   
6885 O  O   . HOH   H .   ? 0.2100 0.3818 0.2488 -0.0491 -0.0185 0.0492  246 HOH   B O   
6886 O  O   . HOH   H .   ? 0.3025 0.1691 0.6174 -0.0173 -0.1067 -0.0214 247 HOH   B O   
6887 O  O   . HOH   H .   ? 0.2253 0.3644 0.3034 -0.0534 -0.0581 -0.0415 248 HOH   B O   
6888 O  O   . HOH   H .   ? 0.2109 0.1985 0.2127 -0.0345 -0.0493 0.0168  249 HOH   B O   
6889 O  O   . HOH   H .   ? 0.2380 0.2153 0.2698 0.0714  -0.0750 -0.0589 250 HOH   B O   
6890 O  O   . HOH   H .   ? 0.2662 0.2619 0.3201 0.0518  0.0165  -0.0943 251 HOH   B O   
6891 O  O   . HOH   H .   ? 0.2964 0.4203 0.2802 -0.0947 -0.0424 -0.0519 252 HOH   B O   
6892 O  O   . HOH   H .   ? 0.3249 0.2543 0.3131 -0.0415 0.0269  -0.0601 253 HOH   B O   
6893 O  O   . HOH   H .   ? 0.2780 0.2167 0.3139 0.0777  0.0779  -0.0004 254 HOH   B O   
6894 O  O   . HOH   H .   ? 0.3421 0.4903 0.3340 -0.0176 -0.1130 0.0956  255 HOH   B O   
6895 O  O   . HOH   H .   ? 0.2014 0.1805 0.3769 0.0007  -0.0453 -0.0125 256 HOH   B O   
6896 O  O   . HOH   H .   ? 0.4279 0.3540 0.3870 -0.0938 0.0621  -0.1020 257 HOH   B O   
6897 O  O   . HOH   H .   ? 0.2020 0.1462 0.2221 -0.0323 -0.0363 0.0278  258 HOH   B O   
6898 O  O   . HOH   H .   ? 0.2592 0.2205 0.1968 0.0093  -0.0173 -0.0010 259 HOH   B O   
6899 O  O   . HOH   H .   ? 0.2564 0.4345 0.6089 0.0038  0.0388  -0.1206 260 HOH   B O   
6900 O  O   . HOH   H .   ? 0.2214 0.3195 0.2157 -0.0588 0.0221  0.0402  261 HOH   B O   
6901 O  O   . HOH   H .   ? 0.2452 0.4756 0.5790 0.1248  -0.0778 -0.1253 262 HOH   B O   
6902 O  O   . HOH   H .   ? 0.2440 0.2836 0.2678 -0.0358 -0.0844 0.0187  263 HOH   B O   
6903 O  O   . HOH   H .   ? 0.2082 0.4291 0.5010 -0.0460 -0.0344 -0.1437 264 HOH   B O   
6904 O  O   . HOH   H .   ? 0.1585 0.1661 0.3257 -0.0201 -0.0178 0.0103  265 HOH   B O   
6905 O  O   . HOH   H .   ? 0.1413 0.1654 0.2158 -0.0066 0.0088  0.0127  266 HOH   B O   
6906 O  O   . HOH   H .   ? 0.2392 0.1970 0.2207 0.0178  -0.0109 -0.0047 267 HOH   B O   
6907 O  O   . HOH   H .   ? 0.1715 0.1444 0.3668 -0.0119 -0.0200 -0.0148 268 HOH   B O   
6908 O  O   . HOH   H .   ? 0.2501 0.1979 0.2870 -0.0670 0.0222  -0.0182 269 HOH   B O   
6909 O  O   . HOH   H .   ? 0.3746 0.3318 0.5439 -0.0137 0.0345  -0.0214 270 HOH   B O   
6910 O  O   . HOH   H .   ? 0.2260 0.2585 0.2243 -0.0312 -0.0566 -0.0425 271 HOH   B O   
6911 O  O   . HOH   H .   ? 0.1807 0.1824 0.1749 -0.0471 -0.0431 0.0115  272 HOH   B O   
6912 O  O   . HOH   H .   ? 0.2317 0.3253 0.3371 -0.0431 0.0413  -0.1001 273 HOH   B O   
6913 O  O   . HOH   H .   ? 0.2910 0.2067 0.4850 0.0064  0.0444  0.0480  274 HOH   B O   
6914 O  O   . HOH   H .   ? 0.4387 0.6015 0.2433 0.0054  -0.0837 0.0715  275 HOH   B O   
6915 O  O   . HOH   H .   ? 0.4077 0.2966 0.4409 -0.0097 -0.1519 -0.0290 276 HOH   B O   
6916 O  O   . HOH   H .   ? 0.4880 0.3680 0.2779 0.0215  -0.0244 -0.0800 277 HOH   B O   
6917 O  O   . HOH   H .   ? 0.1998 0.1497 0.2242 -0.0215 -0.0079 0.0117  278 HOH   B O   
6918 O  O   . HOH   H .   ? 0.2624 0.6533 0.2563 0.0621  -0.0392 -0.0468 279 HOH   B O   
6919 O  O   . HOH   H .   ? 0.2541 0.3822 0.3715 0.0374  0.1183  0.0178  280 HOH   B O   
6920 O  O   . HOH   H .   ? 0.3840 0.3902 0.4334 0.1581  -0.0912 -0.1298 281 HOH   B O   
6921 O  O   . HOH   H .   ? 0.2268 0.3834 0.2359 0.1123  -0.0283 -0.0339 282 HOH   B O   
6922 O  O   . HOH   H .   ? 0.1590 0.1541 0.3712 -0.0149 0.0032  -0.0025 283 HOH   B O   
6923 O  O   . HOH   H .   ? 0.1686 0.1492 0.1930 0.0030  0.0090  0.0023  284 HOH   B O   
6924 O  O   . HOH   H .   ? 0.4503 0.4838 0.4762 0.0236  -0.1539 0.0237  285 HOH   B O   
6925 O  O   . HOH   H .   ? 0.3315 0.2905 0.3127 -0.0196 0.0013  -0.1361 286 HOH   B O   
6926 O  O   . HOH   H .   ? 0.1731 0.3397 0.4841 0.0221  0.0033  -0.1313 287 HOH   B O   
6927 O  O   . HOH   H .   ? 0.5666 0.3762 0.3215 0.2557  0.1130  0.0872  288 HOH   B O   
6928 O  O   . HOH   H .   ? 0.3638 0.2142 0.4192 -0.0890 -0.2052 0.0876  289 HOH   B O   
6929 O  O   . HOH   H .   ? 0.2742 0.4714 0.4740 -0.0986 -0.1113 0.0711  290 HOH   B O   
6930 O  O   . HOH   H .   ? 0.2948 0.7037 0.7256 0.1809  -0.0478 -0.1232 291 HOH   B O   
6931 O  O   . HOH   H .   ? 0.2421 0.2626 0.2853 0.0119  -0.0744 0.0213  292 HOH   B O   
6932 O  O   . HOH   H .   ? 0.1723 0.1623 0.2489 0.0057  0.0043  0.0162  293 HOH   B O   
6933 O  O   . HOH   H .   ? 0.1631 0.2062 0.1659 -0.0141 -0.0217 0.0084  294 HOH   B O   
6934 O  O   . HOH   H .   ? 0.4504 0.4902 0.2346 0.0305  0.0871  0.1081  295 HOH   B O   
6935 O  O   . HOH   H .   ? 0.3125 0.3000 0.4856 -0.0481 -0.0980 0.1139  296 HOH   B O   
6936 O  O   . HOH   H .   ? 0.3630 0.2620 0.2257 0.0136  -0.0943 0.0002  297 HOH   B O   
6937 O  O   . HOH   H .   ? 0.4802 0.3559 0.2424 0.1301  -0.0937 0.0425  298 HOH   B O   
6938 O  O   . HOH   H .   ? 0.1652 0.2117 0.2940 0.0126  -0.0049 0.0140  299 HOH   B O   
6939 O  O   . HOH   H .   ? 0.3658 0.3592 0.3938 -0.1664 0.1094  -0.0349 300 HOH   B O   
6940 O  O   . HOH   H .   ? 0.3307 0.1900 0.3504 0.0668  0.1105  0.0432  301 HOH   B O   
6941 O  O   . HOH   H .   ? 0.4724 0.2854 0.2190 -0.1593 0.0563  -0.0167 302 HOH   B O   
6942 O  O   . HOH   H .   ? 0.3785 0.7013 0.3656 0.1300  -0.0834 0.1264  303 HOH   B O   
6943 O  O   . HOH   H .   ? 0.1944 0.2851 0.6185 0.0445  -0.0389 -0.1335 304 HOH   B O   
6944 O  O   . HOH   H .   ? 0.1598 0.1464 0.3245 0.0100  -0.0081 -0.0053 305 HOH   B O   
6945 O  O   . HOH   H .   ? 0.1988 0.1584 0.3453 0.0380  -0.0857 -0.0051 306 HOH   B O   
6946 O  O   . HOH   H .   ? 0.2791 0.2901 0.3810 -0.0537 0.1158  -0.0955 307 HOH   B O   
6947 O  O   . HOH   H .   ? 0.2133 0.1576 0.2720 -0.0253 -0.0308 -0.0001 308 HOH   B O   
6948 O  O   . HOH   H .   ? 0.4465 0.3504 0.4411 -0.0477 0.0357  0.1444  309 HOH   B O   
6949 O  O   . HOH   H .   ? 0.4436 0.2472 0.3218 0.0232  0.0090  0.0747  310 HOH   B O   
6950 O  O   . HOH   H .   ? 0.3729 0.4481 0.7646 -0.0245 -0.1141 0.2265  311 HOH   B O   
6951 O  O   . HOH   H .   ? 0.1642 0.1847 0.3169 -0.0285 -0.0160 0.0130  312 HOH   B O   
6952 O  O   . HOH   H .   ? 0.6096 0.6257 0.4668 0.2833  -0.0372 -0.0431 313 HOH   B O   
6953 O  O   . HOH   H .   ? 0.2470 0.1470 0.2585 -0.0114 -0.0298 0.0231  314 HOH   B O   
6954 O  O   . HOH   H .   ? 0.2299 0.3200 0.5031 -0.0215 -0.0548 -0.0177 315 HOH   B O   
6955 O  O   . HOH   H .   ? 0.2567 0.3446 0.4686 -0.0421 -0.1366 0.0939  316 HOH   B O   
6956 O  O   . HOH   H .   ? 0.5197 0.3283 0.4608 -0.0198 0.0885  -0.1448 317 HOH   B O   
6957 O  O   . HOH   H .   ? 0.2044 0.5854 0.5058 -0.0752 -0.0216 -0.0095 318 HOH   B O   
6958 O  O   . HOH   H .   ? 0.2215 0.1928 0.1948 -0.0075 0.0203  0.0219  319 HOH   B O   
6959 O  O   . HOH   H .   ? 0.1614 0.1620 0.3019 -0.0149 -0.0117 -0.0166 320 HOH   B O   
6960 O  O   . HOH   H .   ? 0.1710 0.2923 0.2202 -0.0169 -0.0159 0.0736  321 HOH   B O   
6961 O  O   . HOH   H .   ? 0.4968 0.4162 0.2751 0.0150  -0.0362 -0.0484 322 HOH   B O   
6962 O  O   . HOH   H .   ? 0.4181 0.2262 0.2827 0.1439  0.1236  0.0427  323 HOH   B O   
6963 O  O   . HOH   H .   ? 0.5563 0.4388 0.6821 0.1184  -0.1075 0.1826  324 HOH   B O   
6964 O  O   . HOH   H .   ? 0.3018 0.2244 0.2435 0.0247  -0.0202 0.0295  325 HOH   B O   
6965 O  O   . HOH   H .   ? 0.4337 0.3052 0.5242 0.0888  0.1983  0.1730  326 HOH   B O   
6966 O  O   . HOH   H .   ? 0.1895 0.1980 0.2909 0.0284  0.0397  0.0283  327 HOH   B O   
6967 O  O   . HOH   H .   ? 0.6255 0.4018 0.5603 0.0930  0.1489  -0.0129 328 HOH   B O   
6968 O  O   . HOH   H .   ? 0.2205 0.2251 0.5541 -0.0414 0.0158  0.1311  329 HOH   B O   
6969 O  O   . HOH   H .   ? 0.1758 0.2858 0.3210 0.0294  -0.0241 -0.0717 330 HOH   B O   
6970 O  O   . HOH   H .   ? 0.4820 0.4419 0.2362 0.1725  -0.1000 -0.0243 331 HOH   B O   
6971 O  O   . HOH   H .   ? 0.2767 0.1921 0.4708 -0.0018 0.0103  0.0407  332 HOH   B O   
6972 O  O   . HOH   H .   ? 0.8096 0.2097 0.2914 0.0423  -0.0729 -0.0032 333 HOH   B O   
6973 O  O   . HOH   H .   ? 0.6237 0.5657 0.5430 -0.1079 -0.0334 0.1926  334 HOH   B O   
6974 O  O   . HOH   H .   ? 0.4590 0.4350 0.5144 0.0615  0.0144  0.0491  335 HOH   B O   
6975 O  O   . HOH   H .   ? 0.5509 0.3708 0.3884 0.0504  0.1306  0.1686  336 HOH   B O   
6976 O  O   . HOH   H .   ? 0.4399 0.7158 0.3929 -0.0606 -0.0686 0.1949  337 HOH   B O   
6977 O  O   . HOH   H .   ? 0.1732 0.1441 0.2441 0.0049  -0.0186 0.0088  338 HOH   B O   
6978 O  O   . HOH   H .   ? 0.5484 0.4175 0.6203 -0.0269 -0.0923 -0.1172 339 HOH   B O   
6979 O  O   . HOH   H .   ? 0.4721 0.3124 0.3238 0.0502  -0.1234 -0.0784 340 HOH   B O   
6980 O  O   . HOH   H .   ? 0.3377 0.6108 0.4210 -0.0782 -0.0689 -0.0688 341 HOH   B O   
6981 O  O   . HOH   H .   ? 0.7852 0.6053 0.3229 0.0268  -0.0593 0.0993  342 HOH   B O   
6982 O  O   . HOH   H .   ? 0.5006 0.5407 0.3518 0.0115  -0.1091 0.0078  343 HOH   B O   
6983 O  O   . HOH   H .   ? 0.2468 0.5824 0.6488 0.0017  -0.0827 0.0325  344 HOH   B O   
6984 O  O   . HOH   H .   ? 0.2062 0.1935 0.3131 -0.0071 0.0591  -0.0119 345 HOH   B O   
6985 O  O   . HOH   H .   ? 0.2892 0.1922 0.4123 0.0364  -0.1109 -0.0519 346 HOH   B O   
6986 O  O   . HOH   H .   ? 0.4188 0.4956 0.5681 -0.0020 -0.1079 0.0476  347 HOH   B O   
6987 O  O   . HOH   H .   ? 0.2482 0.6188 0.3494 0.1638  -0.0594 -0.1379 348 HOH   B O   
6988 O  O   . HOH   H .   ? 0.4813 0.5618 0.4771 -0.1198 0.0402  0.1190  349 HOH   B O   
6989 O  O   . HOH   H .   ? 0.2817 0.2253 0.4901 -0.0182 -0.0914 -0.0476 350 HOH   B O   
6990 O  O   . HOH   H .   ? 0.3440 0.4362 0.4802 -0.1527 0.0087  -0.0520 351 HOH   B O   
6991 O  O   . HOH   H .   ? 0.2160 0.4422 0.4845 0.0335  0.0376  0.0032  352 HOH   B O   
6992 O  O   . HOH   H .   ? 0.4453 0.6571 0.6351 0.0181  0.0289  -0.0817 353 HOH   B O   
6993 O  O   . HOH   H .   ? 0.3632 0.2101 0.3252 -0.0687 0.0259  -0.0743 354 HOH   B O   
6994 O  O   . HOH   H .   ? 0.4585 0.3478 0.5202 -0.1126 0.1326  0.0630  355 HOH   B O   
6995 O  O   . HOH   H .   ? 0.4023 0.2811 0.3191 -0.1119 0.0078  -0.0639 356 HOH   B O   
6996 O  O   . HOH   H .   ? 0.5445 0.3496 0.3907 0.0373  0.1298  -0.0509 357 HOH   B O   
6997 O  O   . HOH   H .   ? 0.4647 0.5361 0.4922 0.1706  -0.1288 0.1626  358 HOH   B O   
6998 O  O   . HOH   H .   ? 0.5005 0.3388 0.5107 0.0064  -0.1557 -0.0557 359 HOH   B O   
6999 O  O   . HOH   H .   ? 0.4681 0.3965 0.6437 0.0007  0.0687  0.1159  360 HOH   B O   
7000 O  O   . HOH   H .   ? 0.4169 0.6241 0.2839 0.1840  -0.0023 0.0246  361 HOH   B O   
7001 O  O   . HOH   H .   ? 0.2372 0.3778 0.6693 -0.0929 -0.0636 -0.0768 362 HOH   B O   
7002 O  O   . HOH   H .   ? 0.5020 0.4673 0.5356 -0.0788 -0.0261 0.0337  363 HOH   B O   
7003 O  O   . HOH   H .   ? 0.4626 0.3170 0.5394 -0.1274 -0.0466 0.0321  364 HOH   B O   
7004 O  O   . HOH   H .   ? 0.6340 0.2220 0.3772 -0.0047 0.0056  0.0765  365 HOH   B O   
7005 O  O   . HOH   H .   ? 0.6068 0.4760 0.4050 0.1199  0.0498  0.0617  366 HOH   B O   
7006 O  O   . HOH   H .   ? 0.5096 0.5612 0.4368 -0.0992 -0.0273 -0.1188 367 HOH   B O   
7007 O  O   . HOH   H .   ? 0.5665 0.5811 0.3374 0.0761  -0.1637 0.0608  368 HOH   B O   
7008 O  O   . HOH   H .   ? 0.4154 0.5596 0.5067 0.2348  0.0984  0.1550  369 HOH   B O   
7009 O  O   . HOH   H .   ? 0.4895 0.3542 0.5332 0.0785  -0.1433 0.0152  370 HOH   B O   
7010 O  O   . HOH   H .   ? 0.7631 0.7851 0.5370 0.2088  -0.1380 0.0668  371 HOH   B O   
7011 O  O   . HOH   H .   ? 0.5675 0.3734 0.3092 -0.0791 -0.0996 -0.0495 372 HOH   B O   
7012 O  O   . HOH   H .   ? 0.3870 0.3347 0.4006 0.0802  -0.1344 -0.0511 373 HOH   B O   
7013 O  O   . HOH   H .   ? 0.4378 0.5026 0.4609 -0.0873 -0.0573 0.0361  374 HOH   B O   
7014 O  O   . HOH   H .   ? 0.2264 0.4771 0.4115 -0.0033 -0.0486 -0.0759 375 HOH   B O   
7015 O  O   . HOH   H .   ? 0.5275 0.6773 0.4093 -0.1365 -0.0254 -0.1478 376 HOH   B O   
7016 O  O   . HOH   H .   ? 0.4662 0.6895 0.6181 0.1637  0.0524  0.2525  377 HOH   B O   
7017 O  O   . HOH   H .   ? 0.3469 0.5305 0.2218 -0.0190 0.0429  0.0041  378 HOH   B O   
7018 O  O   . HOH   H .   ? 0.7098 0.3933 0.4885 -0.1045 -0.0424 0.0012  379 HOH   B O   
7019 O  O   . HOH   H .   ? 0.3752 0.4424 0.5556 0.1342  -0.0030 0.0186  380 HOH   B O   
7020 O  O   . HOH   H .   ? 0.5561 0.6501 0.6012 -0.0226 0.1578  0.1598  381 HOH   B O   
7021 O  O   . HOH   H .   ? 0.4403 0.8180 0.5351 0.0109  0.1860  0.0728  382 HOH   B O   
7022 O  O   . HOH   H .   ? 0.2969 0.2615 0.3144 0.0067  0.0219  0.0255  383 HOH   B O   
7023 O  O   . HOH   H .   ? 0.5106 0.5047 0.4943 0.0471  -0.0666 -0.0688 384 HOH   B O   
7024 O  O   . HOH   H .   ? 0.6267 0.4577 0.4187 0.0960  0.1188  -0.0408 385 HOH   B O   
7025 O  O   . HOH   H .   ? 0.6851 0.5743 0.4207 0.1805  0.0084  -0.0181 386 HOH   B O   
7026 O  O   . HOH   H .   ? 0.2623 0.4113 0.4174 -0.0665 -0.1168 -0.0249 387 HOH   B O   
7027 O  O   . HOH   H .   ? 0.4552 0.3779 0.3695 -0.0216 0.0462  -0.0329 388 HOH   B O   
7028 O  O   . HOH   H .   ? 0.5840 0.4536 0.4979 -0.0781 0.0774  -0.0278 389 HOH   B O   
7029 O  O   . HOH   H .   ? 0.3693 0.2307 0.3581 0.0733  -0.0466 0.0145  390 HOH   B O   
7030 O  O   . HOH   H .   ? 0.5449 0.4343 0.4438 0.0535  0.0789  0.0552  391 HOH   B O   
7031 O  O   . HOH   H .   ? 0.3798 0.2201 0.4931 -0.0412 0.0436  0.0536  392 HOH   B O   
7032 O  O   . HOH   H .   ? 0.2551 0.4170 0.6682 -0.1216 -0.0457 -0.0385 393 HOH   B O   
7033 O  O   . HOH   H .   ? 0.4032 0.5803 0.3930 0.0736  -0.0008 -0.1202 394 HOH   B O   
7034 O  O   . HOH   H .   ? 0.2018 0.2760 0.5868 -0.0544 -0.0922 0.0277  395 HOH   B O   
7035 O  O   . HOH   H .   ? 0.3381 0.3711 0.4065 0.0253  0.0222  -0.0780 396 HOH   B O   
7036 O  O   . HOH   H .   ? 0.4275 0.4205 0.5143 0.0317  0.0683  0.1085  397 HOH   B O   
7037 O  O   . HOH   H .   ? 0.5175 0.4368 0.3034 -0.2164 -0.0491 0.1196  398 HOH   B O   
7038 O  O   . HOH   H .   ? 0.6356 0.6363 0.6771 0.1135  -0.1342 0.2087  399 HOH   B O   
7039 O  O   . HOH   H .   ? 0.5162 0.5550 0.3478 0.1484  -0.0212 -0.0383 400 HOH   B O   
# 
